data_5AB0
# 
_entry.id   5AB0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5AB0         
PDBE  EBI-64560    
WWPDB D_1290064560 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          5AB2 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        'CRYSTAL STRUCTURE OF AMINOPEPTIDASE ERAP2 WITH LIGAND' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        5AB0 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2015-07-31 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Mpakali, A.'   1 
'Giastas, P.'   2 
'Saridakis, E.' 3 
'Stratikos, E.' 4 
# 
_citation.id                        primary 
_citation.title                     
'Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (Er) Aminopeptidase 2.' 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            290 
_citation.page_first                26021 
_citation.page_last                 ? 
_citation.year                      2015 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   26381406 
_citation.pdbx_database_id_DOI      10.1074/JBC.M115.685909 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Mpakali, A.'      1 
primary 'Giastas, P.'      2 
primary 'Mathioudakis, N.' 3 
primary 'Mavridis, I.M.'   4 
primary 'Saridakis, E.'    5 
primary 'Stratikos, E.'    6 
# 
_cell.entry_id           5AB0 
_cell.length_a           75.350 
_cell.length_b           134.420 
_cell.length_c           129.000 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.49 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5AB0 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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 'ENDOPLASMATIC RETICULUM AMINOPEPTIDASE 2' 111563.422 2   '3.4.11.1, 3.4.11.6' ? ? ? 
2 polymer     syn DG025                                      1313.528   2   ?                    ? ? ? 
3 non-polymer syn 'ZINC ION'                                 65.409     2   ?                    ? ? ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE                     221.208    22  ?                    ? ? ? 
5 non-polymer man BETA-D-MANNOSE                             180.156    5   ?                    ? ? ? 
6 non-polymer syn 1,2-ETHANEDIOL                             62.068     4   ?                    ? ? ? 
7 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'     195.237    1   ?                    ? ? ? 
8 water       nat water                                      18.015     403 ?                    ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'LEUKOCYTE-DERIVED ARGININE AMINOPEPTIDASE, L-RAP' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDL
FVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHL
KYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVK
TIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPL
SKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYME
LIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQ
YLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLR
LQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGW
DQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISE
NLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQ
TTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENW
THLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
RHHHHHH
;
;MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDL
FVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHL
KYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVK
TIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPL
SKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYME
LIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQ
YLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLR
LQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGW
DQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISE
NLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQ
TTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENW
THLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
RHHHHHH
;
A,C ? 
2 'polypeptide(L)' no yes '(2X0)(7GA)KHHAFSF(LYN)' XXKHHAFSFK E,F ? 
# 
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   PHE n 
1 3   HIS n 
1 4   SER n 
1 5   SER n 
1 6   ALA n 
1 7   MET n 
1 8   VAL n 
1 9   ASN n 
1 10  SER n 
1 11  HIS n 
1 12  ARG n 
1 13  LYS n 
1 14  PRO n 
1 15  MET n 
1 16  PHE n 
1 17  ASN n 
1 18  ILE n 
1 19  HIS n 
1 20  ARG n 
1 21  GLY n 
1 22  PHE n 
1 23  TYR n 
1 24  CYS n 
1 25  LEU n 
1 26  THR n 
1 27  ALA n 
1 28  ILE n 
1 29  LEU n 
1 30  PRO n 
1 31  GLN n 
1 32  ILE n 
1 33  CYS n 
1 34  ILE n 
1 35  CYS n 
1 36  SER n 
1 37  GLN n 
1 38  PHE n 
1 39  SER n 
1 40  VAL n 
1 41  PRO n 
1 42  SER n 
1 43  SER n 
1 44  TYR n 
1 45  HIS n 
1 46  PHE n 
1 47  THR n 
1 48  GLU n 
1 49  ASP n 
1 50  PRO n 
1 51  GLY n 
1 52  ALA n 
1 53  PHE n 
1 54  PRO n 
1 55  VAL n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  GLY n 
1 60  GLU n 
1 61  ARG n 
1 62  PHE n 
1 63  PRO n 
1 64  TRP n 
1 65  GLN n 
1 66  GLU n 
1 67  LEU n 
1 68  ARG n 
1 69  LEU n 
1 70  PRO n 
1 71  SER n 
1 72  VAL n 
1 73  VAL n 
1 74  ILE n 
1 75  PRO n 
1 76  LEU n 
1 77  HIS n 
1 78  TYR n 
1 79  ASP n 
1 80  LEU n 
1 81  PHE n 
1 82  VAL n 
1 83  HIS n 
1 84  PRO n 
1 85  ASN n 
1 86  LEU n 
1 87  THR n 
1 88  SER n 
1 89  LEU n 
1 90  ASP n 
1 91  PHE n 
1 92  VAL n 
1 93  ALA n 
1 94  SER n 
1 95  GLU n 
1 96  LYS n 
1 97  ILE n 
1 98  GLU n 
1 99  VAL n 
1 100 LEU n 
1 101 VAL n 
1 102 SER n 
1 103 ASN n 
1 104 ALA n 
1 105 THR n 
1 106 GLN n 
1 107 PHE n 
1 108 ILE n 
1 109 ILE n 
1 110 LEU n 
1 111 HIS n 
1 112 SER n 
1 113 LYS n 
1 114 ASP n 
1 115 LEU n 
1 116 GLU n 
1 117 ILE n 
1 118 THR n 
1 119 ASN n 
1 120 ALA n 
1 121 THR n 
1 122 LEU n 
1 123 GLN n 
1 124 SER n 
1 125 GLU n 
1 126 GLU n 
1 127 ASP n 
1 128 SER n 
1 129 ARG n 
1 130 TYR n 
1 131 MET n 
1 132 LYS n 
1 133 PRO n 
1 134 GLY n 
1 135 LYS n 
1 136 GLU n 
1 137 LEU n 
1 138 LYS n 
1 139 VAL n 
1 140 LEU n 
1 141 SER n 
1 142 TYR n 
1 143 PRO n 
1 144 ALA n 
1 145 HIS n 
1 146 GLU n 
1 147 GLN n 
1 148 ILE n 
1 149 ALA n 
1 150 LEU n 
1 151 LEU n 
1 152 VAL n 
1 153 PRO n 
1 154 GLU n 
1 155 LYS n 
1 156 LEU n 
1 157 THR n 
1 158 PRO n 
1 159 HIS n 
1 160 LEU n 
1 161 LYS n 
1 162 TYR n 
1 163 TYR n 
1 164 VAL n 
1 165 ALA n 
1 166 MET n 
1 167 ASP n 
1 168 PHE n 
1 169 GLN n 
1 170 ALA n 
1 171 LYS n 
1 172 LEU n 
1 173 GLY n 
1 174 ASP n 
1 175 GLY n 
1 176 PHE n 
1 177 GLU n 
1 178 GLY n 
1 179 PHE n 
1 180 TYR n 
1 181 LYS n 
1 182 SER n 
1 183 THR n 
1 184 TYR n 
1 185 ARG n 
1 186 THR n 
1 187 LEU n 
1 188 GLY n 
1 189 GLY n 
1 190 GLU n 
1 191 THR n 
1 192 ARG n 
1 193 ILE n 
1 194 LEU n 
1 195 ALA n 
1 196 VAL n 
1 197 THR n 
1 198 ASP n 
1 199 PHE n 
1 200 GLU n 
1 201 PRO n 
1 202 THR n 
1 203 GLN n 
1 204 ALA n 
1 205 ARG n 
1 206 MET n 
1 207 ALA n 
1 208 PHE n 
1 209 PRO n 
1 210 CYS n 
1 211 PHE n 
1 212 ASP n 
1 213 GLU n 
1 214 PRO n 
1 215 LEU n 
1 216 PHE n 
1 217 LYS n 
1 218 ALA n 
1 219 ASN n 
1 220 PHE n 
1 221 SER n 
1 222 ILE n 
1 223 LYS n 
1 224 ILE n 
1 225 ARG n 
1 226 ARG n 
1 227 GLU n 
1 228 SER n 
1 229 ARG n 
1 230 HIS n 
1 231 ILE n 
1 232 ALA n 
1 233 LEU n 
1 234 SER n 
1 235 ASN n 
1 236 MET n 
1 237 PRO n 
1 238 LYS n 
1 239 VAL n 
1 240 LYS n 
1 241 THR n 
1 242 ILE n 
1 243 GLU n 
1 244 LEU n 
1 245 GLU n 
1 246 GLY n 
1 247 GLY n 
1 248 LEU n 
1 249 LEU n 
1 250 GLU n 
1 251 ASP n 
1 252 HIS n 
1 253 PHE n 
1 254 GLU n 
1 255 THR n 
1 256 THR n 
1 257 VAL n 
1 258 LYS n 
1 259 MET n 
1 260 SER n 
1 261 THR n 
1 262 TYR n 
1 263 LEU n 
1 264 VAL n 
1 265 ALA n 
1 266 TYR n 
1 267 ILE n 
1 268 VAL n 
1 269 CYS n 
1 270 ASP n 
1 271 PHE n 
1 272 HIS n 
1 273 SER n 
1 274 LEU n 
1 275 SER n 
1 276 GLY n 
1 277 PHE n 
1 278 THR n 
1 279 SER n 
1 280 SER n 
1 281 GLY n 
1 282 VAL n 
1 283 LYS n 
1 284 VAL n 
1 285 SER n 
1 286 ILE n 
1 287 TYR n 
1 288 ALA n 
1 289 SER n 
1 290 PRO n 
1 291 ASP n 
1 292 LYS n 
1 293 ARG n 
1 294 ASN n 
1 295 GLN n 
1 296 THR n 
1 297 HIS n 
1 298 TYR n 
1 299 ALA n 
1 300 LEU n 
1 301 GLN n 
1 302 ALA n 
1 303 SER n 
1 304 LEU n 
1 305 LYS n 
1 306 LEU n 
1 307 LEU n 
1 308 ASP n 
1 309 PHE n 
1 310 TYR n 
1 311 GLU n 
1 312 LYS n 
1 313 TYR n 
1 314 PHE n 
1 315 ASP n 
1 316 ILE n 
1 317 TYR n 
1 318 TYR n 
1 319 PRO n 
1 320 LEU n 
1 321 SER n 
1 322 LYS n 
1 323 LEU n 
1 324 ASP n 
1 325 LEU n 
1 326 ILE n 
1 327 ALA n 
1 328 ILE n 
1 329 PRO n 
1 330 ASP n 
1 331 PHE n 
1 332 ALA n 
1 333 PRO n 
1 334 GLY n 
1 335 ALA n 
1 336 MET n 
1 337 GLU n 
1 338 ASN n 
1 339 TRP n 
1 340 GLY n 
1 341 LEU n 
1 342 ILE n 
1 343 THR n 
1 344 TYR n 
1 345 ARG n 
1 346 GLU n 
1 347 THR n 
1 348 SER n 
1 349 LEU n 
1 350 LEU n 
1 351 PHE n 
1 352 ASP n 
1 353 PRO n 
1 354 LYS n 
1 355 THR n 
1 356 SER n 
1 357 SER n 
1 358 ALA n 
1 359 SER n 
1 360 ASP n 
1 361 LYS n 
1 362 LEU n 
1 363 TRP n 
1 364 VAL n 
1 365 THR n 
1 366 ARG n 
1 367 VAL n 
1 368 ILE n 
1 369 ALA n 
1 370 HIS n 
1 371 GLU n 
1 372 LEU n 
1 373 ALA n 
1 374 HIS n 
1 375 GLN n 
1 376 TRP n 
1 377 PHE n 
1 378 GLY n 
1 379 ASN n 
1 380 LEU n 
1 381 VAL n 
1 382 THR n 
1 383 MET n 
1 384 GLU n 
1 385 TRP n 
1 386 TRP n 
1 387 ASN n 
1 388 ASP n 
1 389 ILE n 
1 390 TRP n 
1 391 LEU n 
1 392 ASN n 
1 393 GLU n 
1 394 GLY n 
1 395 PHE n 
1 396 ALA n 
1 397 LYS n 
1 398 TYR n 
1 399 MET n 
1 400 GLU n 
1 401 LEU n 
1 402 ILE n 
1 403 ALA n 
1 404 VAL n 
1 405 ASN n 
1 406 ALA n 
1 407 THR n 
1 408 TYR n 
1 409 PRO n 
1 410 GLU n 
1 411 LEU n 
1 412 GLN n 
1 413 PHE n 
1 414 ASP n 
1 415 ASP n 
1 416 TYR n 
1 417 PHE n 
1 418 LEU n 
1 419 ASN n 
1 420 VAL n 
1 421 CYS n 
1 422 PHE n 
1 423 GLU n 
1 424 VAL n 
1 425 ILE n 
1 426 THR n 
1 427 LYS n 
1 428 ASP n 
1 429 SER n 
1 430 LEU n 
1 431 ASN n 
1 432 SER n 
1 433 SER n 
1 434 ARG n 
1 435 PRO n 
1 436 ILE n 
1 437 SER n 
1 438 LYS n 
1 439 PRO n 
1 440 ALA n 
1 441 GLU n 
1 442 THR n 
1 443 PRO n 
1 444 THR n 
1 445 GLN n 
1 446 ILE n 
1 447 GLN n 
1 448 GLU n 
1 449 MET n 
1 450 PHE n 
1 451 ASP n 
1 452 GLU n 
1 453 VAL n 
1 454 SER n 
1 455 TYR n 
1 456 ASN n 
1 457 LYS n 
1 458 GLY n 
1 459 ALA n 
1 460 CYS n 
1 461 ILE n 
1 462 LEU n 
1 463 ASN n 
1 464 MET n 
1 465 LEU n 
1 466 LYS n 
1 467 ASP n 
1 468 PHE n 
1 469 LEU n 
1 470 GLY n 
1 471 GLU n 
1 472 GLU n 
1 473 LYS n 
1 474 PHE n 
1 475 GLN n 
1 476 LYS n 
1 477 GLY n 
1 478 ILE n 
1 479 ILE n 
1 480 GLN n 
1 481 TYR n 
1 482 LEU n 
1 483 LYS n 
1 484 LYS n 
1 485 PHE n 
1 486 SER n 
1 487 TYR n 
1 488 ARG n 
1 489 ASN n 
1 490 ALA n 
1 491 LYS n 
1 492 ASN n 
1 493 ASP n 
1 494 ASP n 
1 495 LEU n 
1 496 TRP n 
1 497 SER n 
1 498 SER n 
1 499 LEU n 
1 500 SER n 
1 501 ASN n 
1 502 SER n 
1 503 CYS n 
1 504 LEU n 
1 505 GLU n 
1 506 SER n 
1 507 ASP n 
1 508 PHE n 
1 509 THR n 
1 510 SER n 
1 511 GLY n 
1 512 GLY n 
1 513 VAL n 
1 514 CYS n 
1 515 HIS n 
1 516 SER n 
1 517 ASP n 
1 518 PRO n 
1 519 LYS n 
1 520 MET n 
1 521 THR n 
1 522 SER n 
1 523 ASN n 
1 524 MET n 
1 525 LEU n 
1 526 ALA n 
1 527 PHE n 
1 528 LEU n 
1 529 GLY n 
1 530 GLU n 
1 531 ASN n 
1 532 ALA n 
1 533 GLU n 
1 534 VAL n 
1 535 LYS n 
1 536 GLU n 
1 537 MET n 
1 538 MET n 
1 539 THR n 
1 540 THR n 
1 541 TRP n 
1 542 THR n 
1 543 LEU n 
1 544 GLN n 
1 545 LYS n 
1 546 GLY n 
1 547 ILE n 
1 548 PRO n 
1 549 LEU n 
1 550 LEU n 
1 551 VAL n 
1 552 VAL n 
1 553 LYS n 
1 554 GLN n 
1 555 ASP n 
1 556 GLY n 
1 557 CYS n 
1 558 SER n 
1 559 LEU n 
1 560 ARG n 
1 561 LEU n 
1 562 GLN n 
1 563 GLN n 
1 564 GLU n 
1 565 ARG n 
1 566 PHE n 
1 567 LEU n 
1 568 GLN n 
1 569 GLY n 
1 570 VAL n 
1 571 PHE n 
1 572 GLN n 
1 573 GLU n 
1 574 ASP n 
1 575 PRO n 
1 576 GLU n 
1 577 TRP n 
1 578 ARG n 
1 579 ALA n 
1 580 LEU n 
1 581 GLN n 
1 582 GLU n 
1 583 ARG n 
1 584 TYR n 
1 585 LEU n 
1 586 TRP n 
1 587 HIS n 
1 588 ILE n 
1 589 PRO n 
1 590 LEU n 
1 591 THR n 
1 592 TYR n 
1 593 SER n 
1 594 THR n 
1 595 SER n 
1 596 SER n 
1 597 SER n 
1 598 ASN n 
1 599 VAL n 
1 600 ILE n 
1 601 HIS n 
1 602 ARG n 
1 603 HIS n 
1 604 ILE n 
1 605 LEU n 
1 606 LYS n 
1 607 SER n 
1 608 LYS n 
1 609 THR n 
1 610 ASP n 
1 611 THR n 
1 612 LEU n 
1 613 ASP n 
1 614 LEU n 
1 615 PRO n 
1 616 GLU n 
1 617 LYS n 
1 618 THR n 
1 619 SER n 
1 620 TRP n 
1 621 VAL n 
1 622 LYS n 
1 623 PHE n 
1 624 ASN n 
1 625 VAL n 
1 626 ASP n 
1 627 SER n 
1 628 ASN n 
1 629 GLY n 
1 630 TYR n 
1 631 TYR n 
1 632 ILE n 
1 633 VAL n 
1 634 HIS n 
1 635 TYR n 
1 636 GLU n 
1 637 GLY n 
1 638 HIS n 
1 639 GLY n 
1 640 TRP n 
1 641 ASP n 
1 642 GLN n 
1 643 LEU n 
1 644 ILE n 
1 645 THR n 
1 646 GLN n 
1 647 LEU n 
1 648 ASN n 
1 649 GLN n 
1 650 ASN n 
1 651 HIS n 
1 652 THR n 
1 653 LEU n 
1 654 LEU n 
1 655 ARG n 
1 656 PRO n 
1 657 LYS n 
1 658 ASP n 
1 659 ARG n 
1 660 VAL n 
1 661 GLY n 
1 662 LEU n 
1 663 ILE n 
1 664 HIS n 
1 665 ASP n 
1 666 VAL n 
1 667 PHE n 
1 668 GLN n 
1 669 LEU n 
1 670 VAL n 
1 671 GLY n 
1 672 ALA n 
1 673 GLY n 
1 674 ARG n 
1 675 LEU n 
1 676 THR n 
1 677 LEU n 
1 678 ASP n 
1 679 LYS n 
1 680 ALA n 
1 681 LEU n 
1 682 ASP n 
1 683 MET n 
1 684 THR n 
1 685 TYR n 
1 686 TYR n 
1 687 LEU n 
1 688 GLN n 
1 689 HIS n 
1 690 GLU n 
1 691 THR n 
1 692 SER n 
1 693 SER n 
1 694 PRO n 
1 695 ALA n 
1 696 LEU n 
1 697 LEU n 
1 698 GLU n 
1 699 GLY n 
1 700 LEU n 
1 701 SER n 
1 702 TYR n 
1 703 LEU n 
1 704 GLU n 
1 705 SER n 
1 706 PHE n 
1 707 TYR n 
1 708 HIS n 
1 709 MET n 
1 710 MET n 
1 711 ASP n 
1 712 ARG n 
1 713 ARG n 
1 714 ASN n 
1 715 ILE n 
1 716 SER n 
1 717 ASP n 
1 718 ILE n 
1 719 SER n 
1 720 GLU n 
1 721 ASN n 
1 722 LEU n 
1 723 LYS n 
1 724 ARG n 
1 725 TYR n 
1 726 LEU n 
1 727 LEU n 
1 728 GLN n 
1 729 TYR n 
1 730 PHE n 
1 731 LYS n 
1 732 PRO n 
1 733 VAL n 
1 734 ILE n 
1 735 ASP n 
1 736 ARG n 
1 737 GLN n 
1 738 SER n 
1 739 TRP n 
1 740 SER n 
1 741 ASP n 
1 742 LYS n 
1 743 GLY n 
1 744 SER n 
1 745 VAL n 
1 746 TRP n 
1 747 ASP n 
1 748 ARG n 
1 749 MET n 
1 750 LEU n 
1 751 ARG n 
1 752 SER n 
1 753 ALA n 
1 754 LEU n 
1 755 LEU n 
1 756 LYS n 
1 757 LEU n 
1 758 ALA n 
1 759 CYS n 
1 760 ASP n 
1 761 LEU n 
1 762 ASN n 
1 763 HIS n 
1 764 ALA n 
1 765 PRO n 
1 766 CYS n 
1 767 ILE n 
1 768 GLN n 
1 769 LYS n 
1 770 ALA n 
1 771 ALA n 
1 772 GLU n 
1 773 LEU n 
1 774 PHE n 
1 775 SER n 
1 776 GLN n 
1 777 TRP n 
1 778 MET n 
1 779 GLU n 
1 780 SER n 
1 781 SER n 
1 782 GLY n 
1 783 LYS n 
1 784 LEU n 
1 785 ASN n 
1 786 ILE n 
1 787 PRO n 
1 788 THR n 
1 789 ASP n 
1 790 VAL n 
1 791 LEU n 
1 792 LYS n 
1 793 ILE n 
1 794 VAL n 
1 795 TYR n 
1 796 SER n 
1 797 VAL n 
1 798 GLY n 
1 799 ALA n 
1 800 GLN n 
1 801 THR n 
1 802 THR n 
1 803 ALA n 
1 804 GLY n 
1 805 TRP n 
1 806 ASN n 
1 807 TYR n 
1 808 LEU n 
1 809 LEU n 
1 810 GLU n 
1 811 GLN n 
1 812 TYR n 
1 813 GLU n 
1 814 LEU n 
1 815 SER n 
1 816 MET n 
1 817 SER n 
1 818 SER n 
1 819 ALA n 
1 820 GLU n 
1 821 GLN n 
1 822 ASN n 
1 823 LYS n 
1 824 ILE n 
1 825 LEU n 
1 826 TYR n 
1 827 ALA n 
1 828 LEU n 
1 829 SER n 
1 830 THR n 
1 831 SER n 
1 832 LYS n 
1 833 HIS n 
1 834 GLN n 
1 835 GLU n 
1 836 LYS n 
1 837 LEU n 
1 838 LEU n 
1 839 LYS n 
1 840 LEU n 
1 841 ILE n 
1 842 GLU n 
1 843 LEU n 
1 844 GLY n 
1 845 MET n 
1 846 GLU n 
1 847 GLY n 
1 848 LYS n 
1 849 VAL n 
1 850 ILE n 
1 851 LYS n 
1 852 THR n 
1 853 GLN n 
1 854 ASN n 
1 855 LEU n 
1 856 ALA n 
1 857 ALA n 
1 858 LEU n 
1 859 LEU n 
1 860 HIS n 
1 861 ALA n 
1 862 ILE n 
1 863 ALA n 
1 864 ARG n 
1 865 ARG n 
1 866 PRO n 
1 867 LYS n 
1 868 GLY n 
1 869 GLN n 
1 870 GLN n 
1 871 LEU n 
1 872 ALA n 
1 873 TRP n 
1 874 ASP n 
1 875 PHE n 
1 876 VAL n 
1 877 ARG n 
1 878 GLU n 
1 879 ASN n 
1 880 TRP n 
1 881 THR n 
1 882 HIS n 
1 883 LEU n 
1 884 LEU n 
1 885 LYS n 
1 886 LYS n 
1 887 PHE n 
1 888 ASP n 
1 889 LEU n 
1 890 GLY n 
1 891 SER n 
1 892 TYR n 
1 893 ASP n 
1 894 ILE n 
1 895 ARG n 
1 896 MET n 
1 897 ILE n 
1 898 ILE n 
1 899 SER n 
1 900 GLY n 
1 901 THR n 
1 902 THR n 
1 903 ALA n 
1 904 HIS n 
1 905 PHE n 
1 906 SER n 
1 907 SER n 
1 908 LYS n 
1 909 ASP n 
1 910 LYS n 
1 911 LEU n 
1 912 GLN n 
1 913 GLU n 
1 914 VAL n 
1 915 LYS n 
1 916 LEU n 
1 917 PHE n 
1 918 PHE n 
1 919 GLU n 
1 920 SER n 
1 921 LEU n 
1 922 GLU n 
1 923 ALA n 
1 924 GLN n 
1 925 GLY n 
1 926 SER n 
1 927 HIS n 
1 928 LEU n 
1 929 ASP n 
1 930 ILE n 
1 931 PHE n 
1 932 GLN n 
1 933 THR n 
1 934 VAL n 
1 935 LEU n 
1 936 GLU n 
1 937 THR n 
1 938 ILE n 
1 939 THR n 
1 940 LYS n 
1 941 ASN n 
1 942 ILE n 
1 943 LYS n 
1 944 TRP n 
1 945 LEU n 
1 946 GLU n 
1 947 LYS n 
1 948 ASN n 
1 949 LEU n 
1 950 PRO n 
1 951 THR n 
1 952 LEU n 
1 953 ARG n 
1 954 THR n 
1 955 TRP n 
1 956 LEU n 
1 957 MET n 
1 958 VAL n 
1 959 ASN n 
1 960 THR n 
1 961 ARG n 
1 962 HIS n 
1 963 HIS n 
1 964 HIS n 
1 965 HIS n 
1 966 HIS n 
1 967 HIS n 
2 1   2X0 n 
2 2   7GA n 
2 3   LYS n 
2 4   HIS n 
2 5   HIS n 
2 6   ALA n 
2 7   PHE n 
2 8   SER n 
2 9   PHE n 
2 10  LYN 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      '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               'CABBAGE LOOPER' 
_entity_src_gen.pdbx_host_org_scientific_name      'TRICHOPLUSIA NI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7111 
_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            HI5 
_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          BACULOVIRUS 
_entity_src_gen.pdbx_host_org_vector               PFASTBAC 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       ? 
_pdbx_entity_src_syn.pdbx_end_seq_num       ? 
_pdbx_entity_src_syn.organism_scientific    'SYNTHETIC CONSTRUCT' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP ERAP2_HUMAN 1 ? ? Q6P179 ? 
2 PDB 5AB0        2 ? ? 5AB0   ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5AB0 A 1 ? 960 ? Q6P179 1 ? 960 ? 1 960 
2 1 5AB0 C 1 ? 960 ? Q6P179 1 ? 960 ? 1 960 
3 2 5AB0 E 1 ? 10  ? 5AB0   1 ? 10  ? 1 10  
4 2 5AB0 F 1 ? 10  ? 5AB0   1 ? 10  ? 1 10  
# 
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 5AB0 ARG A 961 ? UNP Q6P179 ?   ?   'expression tag' 961 1  
1 5AB0 HIS A 962 ? UNP Q6P179 ?   ?   'expression tag' 962 2  
1 5AB0 HIS A 963 ? UNP Q6P179 ?   ?   'expression tag' 963 3  
1 5AB0 HIS A 964 ? UNP Q6P179 ?   ?   'expression tag' 964 4  
1 5AB0 HIS A 965 ? UNP Q6P179 ?   ?   'expression tag' 965 5  
1 5AB0 HIS A 966 ? UNP Q6P179 ?   ?   'expression tag' 966 6  
1 5AB0 HIS A 967 ? UNP Q6P179 ?   ?   'expression tag' 967 7  
1 5AB0 ASN A 392 ? UNP Q6P179 LYS 392 variant          392 8  
2 5AB0 ARG C 961 ? UNP Q6P179 ?   ?   'expression tag' 961 9  
2 5AB0 HIS C 962 ? UNP Q6P179 ?   ?   'expression tag' 962 10 
2 5AB0 HIS C 963 ? UNP Q6P179 ?   ?   'expression tag' 963 11 
2 5AB0 HIS C 964 ? UNP Q6P179 ?   ?   'expression tag' 964 12 
2 5AB0 HIS C 965 ? UNP Q6P179 ?   ?   'expression tag' 965 13 
2 5AB0 HIS C 966 ? UNP Q6P179 ?   ?   'expression tag' 966 14 
2 5AB0 HIS C 967 ? UNP Q6P179 ?   ?   'expression tag' 967 15 
2 5AB0 ASN C 392 ? UNP Q6P179 LYS 392 variant          392 16 
# 
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 
2X0 non-polymer         . '[(1R)-1-amino-3-phenylpropyl]phosphonic acid' ?                 'C9 H14 N O3 P'  215.186 
7GA non-polymer         . 2,4-DIMETHYLPENTANAL                           ?                 'C7 H14 O2'      130.185 
ALA 'L-peptide linking' y ALANINE                                        ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                       ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                     ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                ?                 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE                                 ?                 'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE                                       ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                 'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
LYN 'L-peptide linking' n '2,6-DIAMINO-HEXANOIC ACID AMIDE'              ?                 'C6 H16 N3 O 1'  146.211 
LYS 'L-peptide linking' y LYSINE                                         ?                 'C6 H15 N2 O2 1' 147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'         ?                 'C6 H13 N O4 S'  195.237 
MET 'L-peptide linking' y METHIONINE                                     ?                 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                         ?                 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                                  ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                        ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                         ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                      ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                     ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                       ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                         ?                 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                                     ?                 'Zn 2'           65.409  
# 
_exptl.entry_id          5AB0 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.19 
_exptl_crystal.density_percent_sol   38.45 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.3 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '6 %(W/V) PEG MW 8000, 25 %(V/V) ETHYLENE GLYCOL, 59 MM MES AND 41 MM IMIDAZOLE AT PH 6.3' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 2M' 
_diffrn_detector.pdbx_collection_date   2014-11-30 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.pdbx_synchrotron_site       ALBA 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_wavelength             1.0000 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     5AB0 
_reflns.observed_criterion_sigma_I   1.6 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             65.70 
_reflns.d_resolution_high            2.50 
_reflns.number_obs                   88335 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.11 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.00 
_reflns.B_iso_Wilson_estimate        54.5 
_reflns.pdbx_redundancy              3.7 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.50 
_reflns_shell.d_res_low              2.64 
_reflns_shell.percent_possible_all   99.5 
_reflns_shell.Rmerge_I_obs           0.81 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.60 
_reflns_shell.pdbx_redundancy        3.6 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5AB0 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     88244 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             65.726 
_refine.ls_d_res_high                            2.500 
_refine.ls_percent_reflns_obs                    99.38 
_refine.ls_R_factor_obs                          0.2010 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1981 
_refine.ls_R_factor_R_free                       0.2580 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  4416 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               56.3 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 4E36' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.37 
_refine.pdbx_overall_phase_error                 27.84 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        14765 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         393 
_refine_hist.number_atoms_solvent             403 
_refine_hist.number_atoms_total               15561 
_refine_hist.d_res_high                       2.500 
_refine_hist.d_res_low                        65.726 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.009  ? ? 15624 'X-RAY DIFFRACTION' ? 
f_angle_d          1.282  ? ? 21212 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 16.556 ? ? 5768  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.053  ? ? 2396  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.005  ? ? 2633  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 2.5000 2.5284  2793 0.3177 99.00  0.3924 . . 147 . . 
'X-RAY DIFFRACTION' . 2.5284 2.5582  2754 0.2807 100.00 0.3924 . . 131 . . 
'X-RAY DIFFRACTION' . 2.5582 2.5894  2837 0.2680 100.00 0.3180 . . 155 . . 
'X-RAY DIFFRACTION' . 2.5894 2.6221  2748 0.2614 99.00  0.3093 . . 158 . . 
'X-RAY DIFFRACTION' . 2.6221 2.6566  2791 0.2620 99.00  0.3351 . . 140 . . 
'X-RAY DIFFRACTION' . 2.6566 2.6930  2787 0.2607 99.00  0.3523 . . 157 . . 
'X-RAY DIFFRACTION' . 2.6930 2.7315  2703 0.2551 99.00  0.3349 . . 175 . . 
'X-RAY DIFFRACTION' . 2.7315 2.7723  2796 0.2498 99.00  0.3127 . . 157 . . 
'X-RAY DIFFRACTION' . 2.7723 2.8156  2780 0.2425 99.00  0.3358 . . 140 . . 
'X-RAY DIFFRACTION' . 2.8156 2.8618  2802 0.2449 100.00 0.3330 . . 154 . . 
'X-RAY DIFFRACTION' . 2.8618 2.9111  2828 0.2416 100.00 0.3240 . . 120 . . 
'X-RAY DIFFRACTION' . 2.9111 2.9640  2756 0.2280 99.00  0.3020 . . 143 . . 
'X-RAY DIFFRACTION' . 2.9640 3.0211  2813 0.2214 99.00  0.2353 . . 137 . . 
'X-RAY DIFFRACTION' . 3.0211 3.0827  2768 0.2210 99.00  0.2934 . . 156 . . 
'X-RAY DIFFRACTION' . 3.0827 3.1498  2790 0.2287 99.00  0.3095 . . 151 . . 
'X-RAY DIFFRACTION' . 3.1498 3.2230  2734 0.2264 99.00  0.2793 . . 162 . . 
'X-RAY DIFFRACTION' . 3.2230 3.3036  2814 0.2292 99.00  0.3010 . . 156 . . 
'X-RAY DIFFRACTION' . 3.3036 3.3929  2786 0.2213 99.00  0.3139 . . 132 . . 
'X-RAY DIFFRACTION' . 3.3929 3.4928  2805 0.2259 99.00  0.3062 . . 140 . . 
'X-RAY DIFFRACTION' . 3.4928 3.6055  2805 0.2125 99.00  0.2672 . . 125 . . 
'X-RAY DIFFRACTION' . 3.6055 3.7344  2834 0.2039 100.00 0.2890 . . 131 . . 
'X-RAY DIFFRACTION' . 3.7344 3.8839  2773 0.1987 100.00 0.2630 . . 167 . . 
'X-RAY DIFFRACTION' . 3.8839 4.0606  2807 0.1814 100.00 0.2449 . . 153 . . 
'X-RAY DIFFRACTION' . 4.0606 4.2746  2802 0.1698 100.00 0.2236 . . 139 . . 
'X-RAY DIFFRACTION' . 4.2746 4.5424  2785 0.1565 99.00  0.2415 . . 157 . . 
'X-RAY DIFFRACTION' . 4.5424 4.8930  2815 0.1572 100.00 0.1923 . . 144 . . 
'X-RAY DIFFRACTION' . 4.8930 5.3852  2845 0.1658 99.00  0.2111 . . 127 . . 
'X-RAY DIFFRACTION' . 5.3852 6.1640  2805 0.1866 99.00  0.2489 . . 150 . . 
'X-RAY DIFFRACTION' . 6.1640 7.7640  2782 0.1738 99.00  0.2222 . . 172 . . 
'X-RAY DIFFRACTION' . 7.7640 65.7486 2890 0.1606 99.00  0.1788 . . 140 . . 
# 
_struct.entry_id                  5AB0 
_struct.title                     'Crystal structure of aminopeptidase ERAP2 with ligand' 
_struct.pdbx_descriptor           'ENDOPLASMATIC RETICULUM AMINOPEPTIDASE 2 (E.C.3.4.11.1, 3.4.11.6), DG025' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        5AB0 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'AMINOPEPTIDASE, ERAP2, ZINC ION BINDING, ENDOPLASMIC RETICULUM, HYDROLASE, METALLOPROTEASE, L-RAP, ANTIGEN PRESENTATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 2 ? 
E  N N 3 ? 
F  N N 4 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 5 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 5 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 6 ? 
U  N N 6 ? 
V  N N 7 ? 
W  N N 5 ? 
X  N N 5 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 5 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 4 ? 
GA N N 4 ? 
HA N N 4 ? 
IA N N 4 ? 
JA N N 3 ? 
KA N N 6 ? 
LA N N 6 ? 
MA N N 8 ? 
NA N N 8 ? 
# 
_struct_biol.id   1 
# 
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  1  ASP A 127 ? MET A 131 ? ASP A 127 MET A 131 5 ? 5  
HELX_P HELX_P2  2  PRO A 143 ? HIS A 145 ? PRO A 143 HIS A 145 5 ? 3  
HELX_P HELX_P3  3  GLN A 203 ? ALA A 207 ? GLN A 203 ALA A 207 5 ? 5  
HELX_P HELX_P4  4  SER A 260 ? VAL A 264 ? SER A 260 VAL A 264 5 ? 5  
HELX_P HELX_P5  5  SER A 289 ? GLN A 295 ? SER A 289 GLN A 295 5 ? 7  
HELX_P HELX_P6  6  THR A 296 ? ASP A 315 ? THR A 296 ASP A 315 1 ? 20 
HELX_P HELX_P7  7  GLU A 346 ? LEU A 350 ? GLU A 346 LEU A 350 1 ? 5  
HELX_P HELX_P8  8  SER A 357 ? PHE A 377 ? SER A 357 PHE A 377 1 ? 21 
HELX_P HELX_P9  9  TRP A 385 ? ASN A 387 ? TRP A 385 ASN A 387 5 ? 3  
HELX_P HELX_P10 10 ASP A 388 ? TYR A 408 ? ASP A 388 TYR A 408 1 ? 21 
HELX_P HELX_P11 11 PRO A 409 ? TYR A 416 ? PRO A 409 TYR A 416 5 ? 8  
HELX_P HELX_P12 12 PHE A 417 ? SER A 429 ? PHE A 417 SER A 429 1 ? 13 
HELX_P HELX_P13 13 THR A 442 ? MET A 449 ? THR A 442 MET A 449 1 ? 8  
HELX_P HELX_P14 14 TYR A 455 ? GLY A 470 ? TYR A 455 GLY A 470 1 ? 16 
HELX_P HELX_P15 15 GLY A 470 ? SER A 486 ? GLY A 470 SER A 486 1 ? 17 
HELX_P HELX_P16 16 LYS A 491 ? ASN A 501 ? LYS A 491 ASN A 501 1 ? 11 
HELX_P HELX_P17 17 THR A 521 ? GLN A 544 ? THR A 521 GLN A 544 1 ? 24 
HELX_P HELX_P18 18 VAL A 625 ? ASN A 628 ? VAL A 625 ASN A 628 5 ? 4  
HELX_P HELX_P19 19 HIS A 638 ? HIS A 651 ? HIS A 638 HIS A 651 1 ? 14 
HELX_P HELX_P20 20 THR A 652 ? LEU A 654 ? THR A 652 LEU A 654 5 ? 3  
HELX_P HELX_P21 21 ARG A 655 ? ALA A 672 ? ARG A 655 ALA A 672 1 ? 18 
HELX_P HELX_P22 22 THR A 676 ? THR A 684 ? THR A 676 THR A 684 1 ? 9  
HELX_P HELX_P23 23 TYR A 685 ? HIS A 689 ? TYR A 685 HIS A 689 5 ? 5  
HELX_P HELX_P24 24 SER A 692 ? ARG A 713 ? SER A 692 ARG A 713 1 ? 22 
HELX_P HELX_P25 25 ILE A 715 ? TYR A 729 ? ILE A 715 TYR A 729 1 ? 15 
HELX_P HELX_P26 26 PHE A 730 ? ARG A 736 ? PHE A 730 ARG A 736 1 ? 7  
HELX_P HELX_P27 27 SER A 744 ? LEU A 761 ? SER A 744 LEU A 761 1 ? 18 
HELX_P HELX_P28 28 HIS A 763 ? SER A 780 ? HIS A 763 SER A 780 1 ? 18 
HELX_P HELX_P29 29 PRO A 787 ? ASP A 789 ? PRO A 787 ASP A 789 5 ? 3  
HELX_P HELX_P30 30 VAL A 790 ? ALA A 799 ? VAL A 790 ALA A 799 1 ? 10 
HELX_P HELX_P31 31 THR A 801 ? SER A 815 ? THR A 801 SER A 815 1 ? 15 
HELX_P HELX_P32 32 SER A 817 ? THR A 830 ? SER A 817 THR A 830 1 ? 14 
HELX_P HELX_P33 33 HIS A 833 ? GLY A 847 ? HIS A 833 GLY A 847 1 ? 15 
HELX_P HELX_P34 34 LYS A 851 ? GLN A 853 ? LYS A 851 GLN A 853 5 ? 3  
HELX_P HELX_P35 35 ASN A 854 ? ARG A 864 ? ASN A 854 ARG A 864 1 ? 11 
HELX_P HELX_P36 36 ARG A 865 ? ASN A 879 ? ARG A 865 ASN A 879 1 ? 15 
HELX_P HELX_P37 37 ASN A 879 ? PHE A 887 ? ASN A 879 PHE A 887 1 ? 9  
HELX_P HELX_P38 38 SER A 891 ? ALA A 903 ? SER A 891 ALA A 903 1 ? 13 
HELX_P HELX_P39 39 SER A 907 ? GLU A 922 ? SER A 907 GLU A 922 1 ? 16 
HELX_P HELX_P40 40 LEU A 928 ? HIS A 962 ? LEU A 928 HIS A 962 1 ? 35 
HELX_P HELX_P41 41 GLN B 203 ? ALA B 207 ? GLN C 203 ALA C 207 5 ? 5  
HELX_P HELX_P42 42 SER B 260 ? VAL B 264 ? SER C 260 VAL C 264 5 ? 5  
HELX_P HELX_P43 43 SER B 289 ? GLN B 295 ? SER C 289 GLN C 295 5 ? 7  
HELX_P HELX_P44 44 THR B 296 ? PHE B 314 ? THR C 296 PHE C 314 1 ? 19 
HELX_P HELX_P45 45 GLU B 346 ? LEU B 349 ? GLU C 346 LEU C 349 5 ? 4  
HELX_P HELX_P46 46 SER B 357 ? PHE B 377 ? SER C 357 PHE C 377 1 ? 21 
HELX_P HELX_P47 47 TRP B 385 ? ASP B 388 ? TRP C 385 ASP C 388 5 ? 4  
HELX_P HELX_P48 48 ILE B 389 ? TYR B 408 ? ILE C 389 TYR C 408 1 ? 20 
HELX_P HELX_P49 49 PRO B 409 ? ASP B 415 ? PRO C 409 ASP C 415 5 ? 7  
HELX_P HELX_P50 50 TYR B 416 ? SER B 429 ? TYR C 416 SER C 429 1 ? 14 
HELX_P HELX_P51 51 THR B 442 ? MET B 449 ? THR C 442 MET C 449 1 ? 8  
HELX_P HELX_P52 52 ASP B 451 ? SER B 486 ? ASP C 451 SER C 486 1 ? 36 
HELX_P HELX_P53 53 LYS B 491 ? ASN B 501 ? LYS C 491 ASN C 501 1 ? 11 
HELX_P HELX_P54 54 ASN B 531 ? LEU B 543 ? ASN C 531 LEU C 543 1 ? 13 
HELX_P HELX_P55 55 ASP B 574 ? ARG B 578 ? ASP C 574 ARG C 578 5 ? 5  
HELX_P HELX_P56 56 VAL B 625 ? ASN B 628 ? VAL C 625 ASN C 628 5 ? 4  
HELX_P HELX_P57 57 GLY B 639 ? ASN B 650 ? GLY C 639 ASN C 650 1 ? 12 
HELX_P HELX_P58 58 HIS B 651 ? LEU B 654 ? HIS C 651 LEU C 654 5 ? 4  
HELX_P HELX_P59 59 ARG B 655 ? GLY B 673 ? ARG C 655 GLY C 673 1 ? 19 
HELX_P HELX_P60 60 THR B 676 ? TYR B 685 ? THR C 676 TYR C 685 1 ? 10 
HELX_P HELX_P61 61 TYR B 686 ? GLN B 688 ? TYR C 686 GLN C 688 5 ? 3  
HELX_P HELX_P62 62 SER B 692 ? ARG B 713 ? SER C 692 ARG C 713 1 ? 22 
HELX_P HELX_P63 63 ILE B 715 ? TYR B 729 ? ILE C 715 TYR C 729 1 ? 15 
HELX_P HELX_P64 64 LYS B 731 ? GLN B 737 ? LYS C 731 GLN C 737 1 ? 7  
HELX_P HELX_P65 65 SER B 744 ? ASN B 762 ? SER C 744 ASN C 762 1 ? 19 
HELX_P HELX_P66 66 HIS B 763 ? GLU B 779 ? HIS C 763 GLU C 779 1 ? 17 
HELX_P HELX_P67 67 VAL B 790 ? GLY B 798 ? VAL C 790 GLY C 798 1 ? 9  
HELX_P HELX_P68 68 THR B 801 ? SER B 815 ? THR C 801 SER C 815 1 ? 15 
HELX_P HELX_P69 69 SER B 817 ? SER B 829 ? SER C 817 SER C 829 1 ? 13 
HELX_P HELX_P70 70 HIS B 833 ? GLY B 847 ? HIS C 833 GLY C 847 1 ? 15 
HELX_P HELX_P71 71 LYS B 851 ? GLN B 853 ? LYS C 851 GLN C 853 5 ? 3  
HELX_P HELX_P72 72 ASN B 854 ? ALA B 863 ? ASN C 854 ALA C 863 1 ? 10 
HELX_P HELX_P73 73 ARG B 865 ? PHE B 887 ? ARG C 865 PHE C 887 1 ? 23 
HELX_P HELX_P74 74 SER B 891 ? THR B 901 ? SER C 891 THR C 901 1 ? 11 
HELX_P HELX_P75 75 ASP B 909 ? GLU B 922 ? ASP C 909 GLU C 922 1 ? 14 
HELX_P HELX_P76 76 LEU B 928 ? ASN B 959 ? LEU C 928 ASN C 959 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 421 SG  ? ? ? 1_555 A  CYS 460 SG  ? ? A CYS 421  A CYS 460  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf2  disulf ? ? A  CYS 503 SG  ? ? ? 1_555 A  CYS 514 SG  ? ? A CYS 503  A CYS 514  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf3  disulf ? ? A  CYS 759 SG  ? ? ? 1_555 A  CYS 766 SG  ? ? A CYS 759  A CYS 766  1_555 ? ? ? ? ? ? ? 2.937 ? 
disulf4  disulf ? ? B  CYS 421 SG  ? ? ? 1_555 B  CYS 460 SG  ? ? C CYS 421  C CYS 460  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf5  disulf ? ? B  CYS 759 SG  ? ? ? 1_555 B  CYS 766 SG  ? ? C CYS 759  C CYS 766  1_555 ? ? ? ? ? ? ? 2.034 ? 
covale1  covale ? ? A  ASN 85  ND2 ? ? ? 1_555 H  NAG .   C1  ? ? A ASN 85   A NAG 1071 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale2  covale ? ? A  ASN 103 ND2 ? ? ? 1_555 F  NAG .   C1  ? ? A ASN 103  A NAG 1069 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale3  covale ? ? A  ASN 119 ND2 ? ? ? 1_555 R  NAG .   C1  ? ? A ASN 119  A NAG 1081 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale4  covale ? ? A  ASN 219 ND2 ? ? ? 1_555 J  NAG .   C1  ? ? A ASN 219  A NAG 1073 1_555 ? ? ? ? ? ? ? 1.466 ? 
covale5  covale ? ? A  ASN 405 ND2 ? ? ? 1_555 M  NAG .   C1  ? ? A ASN 405  A NAG 1076 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale6  covale ? ? A  ASN 431 ND2 ? ? ? 1_555 G  NAG .   C1  ? ? A ASN 431  A NAG 1070 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale7  covale ? ? A  ASN 650 ND2 ? ? ? 1_555 P  NAG .   C1  ? ? A ASN 650  A NAG 1079 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale8  covale ? ? A  ASN 714 ND2 ? ? ? 1_555 S  NAG .   C1  ? ? A ASN 714  A NAG 1082 1_555 ? ? ? ? ? ? ? 1.458 ? 
metalc1  metalc ? ? E  ZN  .   ZN  ? ? ? 1_555 A  HIS 370 NE2 ? ? A ZN  1008 A HIS 370  1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc2  metalc ? ? E  ZN  .   ZN  ? ? ? 1_555 A  GLU 393 OE1 ? ? A ZN  1008 A GLU 393  1_555 ? ? ? ? ? ? ? 1.899 ? 
metalc3  metalc ? ? E  ZN  .   ZN  ? ? ? 1_555 A  HIS 374 NE2 ? ? A ZN  1008 A HIS 374  1_555 ? ? ? ? ? ? ? 2.074 ? 
metalc4  metalc ? ? E  ZN  .   ZN  ? ? ? 1_555 A  GLU 393 OE2 ? ? A ZN  1008 A GLU 393  1_555 ? ? ? ? ? ? ? 2.252 ? 
covale9  covale ? ? H  NAG .   O4  ? ? ? 1_555 I  NAG .   C1  ? ? A NAG 1071 A NAG 1072 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale10 covale ? ? J  NAG .   O4  ? ? ? 1_555 K  NAG .   C1  ? ? A NAG 1073 A NAG 1074 1_555 ? ? ? ? ? ? ? 1.432 ? 
covale11 covale ? ? K  NAG .   O4  ? ? ? 1_555 L  BMA .   C1  ? ? A NAG 1074 A BMA 1075 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale12 covale ? ? M  NAG .   O4  ? ? ? 1_555 N  NAG .   C1  ? ? A NAG 1076 A NAG 1077 1_555 ? ? ? ? ? ? ? 1.454 ? 
covale13 covale ? ? N  NAG .   O4  ? ? ? 1_555 O  BMA .   C1  ? ? A NAG 1077 A BMA 1078 1_555 ? ? ? ? ? ? ? 1.461 ? 
covale14 covale ? ? P  NAG .   O4  ? ? ? 1_555 Q  NAG .   C1  ? ? A NAG 1079 A NAG 1080 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale15 covale ? ? B  ASN 85  ND2 ? ? ? 1_555 Y  NAG .   C1  ? ? C ASN 85   C NAG 1003 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale16 covale ? ? B  ASN 103 ND2 ? ? ? 1_555 BA NAG .   C1  ? ? C ASN 103  C NAG 1006 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale17 covale ? ? B  ASN 219 ND2 ? ? ? 1_555 CA NAG .   C1  ? ? C ASN 219  C NAG 1007 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale18 covale ? ? B  ASN 294 ND2 ? ? ? 1_555 FA NAG .   C1  ? ? C ASN 294  C NAG 1010 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale19 covale ? ? B  ASN 405 ND2 ? ? ? 1_555 GA NAG .   C1  ? ? C ASN 405  C NAG 1011 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale20 covale ? ? B  ASN 431 ND2 ? ? ? 1_555 EA NAG .   C1  ? ? C ASN 431  C NAG 1009 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale21 covale ? ? B  ASN 650 ND2 ? ? ? 1_555 IA NAG .   C1  ? ? C ASN 650  C NAG 1013 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale22 covale ? ? B  ASN 714 ND2 ? ? ? 1_555 HA NAG .   C1  ? ? C ASN 714  C NAG 1012 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale23 covale ? ? W  BMA .   O6  ? ? ? 1_555 AA BMA .   C1  ? ? C BMA 1001 C BMA 1005 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale24 covale ? ? W  BMA .   C1  ? ? ? 1_555 Z  NAG .   O4  ? ? C BMA 1001 C NAG 1004 1_555 ? ? ? ? ? ? ? 1.420 ? 
covale25 covale ? ? W  BMA .   O4  ? ? ? 1_555 X  BMA .   C1  ? ? C BMA 1001 C BMA 1002 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale26 covale ? ? Y  NAG .   O4  ? ? ? 1_555 Z  NAG .   C1  ? ? C NAG 1003 C NAG 1004 1_555 ? ? ? ? ? ? ? 1.424 ? 
covale27 covale ? ? CA NAG .   O4  ? ? ? 1_555 DA NAG .   C1  ? ? C NAG 1007 C NAG 1008 1_555 ? ? ? ? ? ? ? 1.457 ? 
metalc5  metalc ? ? JA ZN  .   ZN  ? ? ? 1_555 B  HIS 374 NE2 ? ? C ZN  1020 C HIS 374  1_555 ? ? ? ? ? ? ? 2.018 ? 
metalc6  metalc ? ? JA ZN  .   ZN  ? ? ? 1_555 B  GLU 393 OE1 ? ? C ZN  1020 C GLU 393  1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc7  metalc ? ? JA ZN  .   ZN  ? ? ? 1_555 B  HIS 370 NE2 ? ? C ZN  1020 C HIS 370  1_555 ? ? ? ? ? ? ? 2.021 ? 
metalc8  metalc ? ? C  2X0 1   O12 ? ? ? 1_555 E  ZN  .   ZN  ? ? E 2X0 1    A ZN  1008 1_555 ? ? ? ? ? ? ? 2.067 ? 
covale28 covale ? ? C  7GA 2   C   ? ? ? 1_555 C  LYS 3   N   ? ? E 7GA 2    E LYS 3    1_555 ? ? ? ? ? ? ? 1.436 ? 
covale29 covale ? ? C  2X0 1   P11 ? ? ? 1_555 C  7GA 2   C6  ? ? E 2X0 1    E 7GA 2    1_555 ? ? ? ? ? ? ? 1.587 ? 
covale30 covale ? ? C  PHE 9   C   ? ? ? 1_555 C  LYN 10  N   ? ? E PHE 9    E LYN 10   1_555 ? ? ? ? ? ? ? 1.336 ? 
metalc9  metalc ? ? D  2X0 1   O12 ? ? ? 1_555 JA ZN  .   ZN  ? ? F 2X0 1    C ZN  1020 1_555 ? ? ? ? ? ? ? 2.431 ? 
covale31 covale ? ? D  2X0 1   P11 ? ? ? 1_555 D  7GA 2   C6  ? ? F 2X0 1    F 7GA 2    1_555 ? ? ? ? ? ? ? 1.595 ? 
covale32 covale ? ? D  7GA 2   C   ? ? ? 1_555 D  LYS 3   N   ? ? F 7GA 2    F LYS 3    1_555 ? ? ? ? ? ? ? 1.425 ? 
covale33 covale ? ? D  PHE 9   C   ? ? ? 1_555 D  LYN 10  N   ? ? F PHE 9    F LYN 10   1_555 ? ? ? ? ? ? ? 1.335 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  ALA 56  A . ? ALA 56  A THR 57  A ? THR 57  A 1 -10.47 
2  LYS 132 A . ? LYS 132 A PRO 133 A ? PRO 133 A 1 4.37   
3  GLY 134 A . ? GLY 134 A LYS 135 A ? LYS 135 A 1 7.23   
4  GLU 200 A . ? GLU 200 A PRO 201 A ? PRO 201 A 1 -0.86  
5  ASP 507 A . ? ASP 507 A PHE 508 A ? PHE 508 A 1 -23.25 
6  PHE 508 A . ? PHE 508 A THR 509 A ? THR 509 A 1 3.86   
7  SER 510 A . ? SER 510 A GLY 511 A ? GLY 511 A 1 -3.26  
8  CYS 514 A . ? CYS 514 A HIS 515 A ? HIS 515 A 1 -7.37  
9  ALA 923 A . ? ALA 923 A GLN 924 A ? GLN 924 A 1 4.07   
10 HIS 962 A . ? HIS 962 A HIS 963 A ? HIS 963 A 1 -4.50  
11 HIS 962 A . ? HIS 962 A HIS 963 A ? HIS 963 A 1 -3.93  
12 ALA 56  B . ? ALA 56  C THR 57  B ? THR 57  C 1 -7.66  
13 LYS 132 B . ? LYS 132 C PRO 133 B ? PRO 133 C 1 7.35   
14 GLY 134 B . ? GLY 134 C LYS 135 B ? LYS 135 C 1 11.97  
15 GLU 200 B . ? GLU 200 C PRO 201 B ? PRO 201 C 1 6.37   
16 LEU 889 B . ? LEU 889 C GLY 890 B ? GLY 890 C 1 10.14  
17 SER 926 B . ? SER 926 C HIS 927 B ? HIS 927 C 1 12.26  
18 ALA 6   C . ? ALA 6   E PHE 7   C ? PHE 7   E 1 -17.37 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 7 ? 
AB ? 3 ? 
AC ? 4 ? 
AD ? 5 ? 
AE ? 2 ? 
AF ? 4 ? 
AG ? 3 ? 
CA ? 7 ? 
CB ? 3 ? 
CC ? 2 ? 
CD ? 2 ? 
CE ? 5 ? 
CF ? 2 ? 
CG ? 4 ? 
CH ? 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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? parallel      
AA 5 6 ? anti-parallel 
AA 6 7 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AC 3 4 ? anti-parallel 
AD 1 2 ? anti-parallel 
AD 2 3 ? parallel      
AD 3 4 ? parallel      
AD 4 5 ? anti-parallel 
AE 1 2 ? parallel      
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? parallel      
AG 1 2 ? anti-parallel 
AG 2 3 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CA 4 5 ? parallel      
CA 5 6 ? anti-parallel 
CA 6 7 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CC 1 2 ? anti-parallel 
CD 1 2 ? anti-parallel 
CE 1 2 ? anti-parallel 
CE 2 3 ? parallel      
CE 3 4 ? parallel      
CE 4 5 ? anti-parallel 
CF 1 2 ? parallel      
CG 1 2 ? anti-parallel 
CG 2 3 ? anti-parallel 
CG 3 4 ? parallel      
CH 1 2 ? anti-parallel 
CH 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA 1 GLU A 116 ? GLN A 123 ? GLU A 116 GLN A 123 
AA 2 LEU A 160 ? LYS A 171 ? LEU A 160 LYS A 171 
AA 3 ASP A 90  ? VAL A 101 ? ASP A 90  VAL A 101 
AA 4 VAL A 73  ? ASN A 85  ? VAL A 73  ASN A 85  
AA 5 ASN A 219 ? ARG A 226 ? ASN A 219 ARG A 226 
AA 6 LEU A 249 ? PHE A 253 ? LEU A 249 PHE A 253 
AA 7 LYS A 238 ? GLU A 243 ? LYS A 238 GLU A 243 
AB 1 PHE A 107 ? HIS A 111 ? PHE A 107 HIS A 111 
AB 2 GLN A 147 ? LEU A 151 ? GLN A 147 LEU A 151 
AB 3 LYS A 138 ? TYR A 142 ? LYS A 138 TYR A 142 
AC 1 GLY A 178 ? ARG A 185 ? GLY A 178 ARG A 185 
AC 2 THR A 191 ? ASP A 198 ? THR A 191 ASP A 198 
AC 3 TYR A 266 ? CYS A 269 ? TYR A 266 CYS A 269 
AC 4 ILE A 231 ? SER A 234 ? ILE A 231 SER A 234 
AD 1 HIS A 272 ? PHE A 277 ? HIS A 272 PHE A 277 
AD 2 LYS A 283 ? ALA A 288 ? LYS A 283 ALA A 288 
AD 3 LYS A 322 ? ILE A 328 ? LYS A 322 ILE A 328 
AD 4 LEU A 341 ? ARG A 345 ? LEU A 341 ARG A 345 
AD 5 ALA A 335 ? MET A 336 ? ALA A 335 MET A 336 
AE 1 VAL A 381 ? MET A 383 ? VAL A 381 MET A 383 
AE 2 ARG A 488 ? ALA A 490 ? ARG A 488 ALA A 490 
AF 1 THR A 609 ? ASP A 613 ? THR A 609 ASP A 613 
AF 2 SER A 558 ? ARG A 565 ? SER A 558 ARG A 565 
AF 3 PRO A 548 ? LYS A 553 ? PRO A 548 LYS A 553 
AF 4 ILE A 632 ? TYR A 635 ? ILE A 632 TYR A 635 
AG 1 SER A 597 ? LEU A 605 ? SER A 597 LEU A 605 
AG 2 ILE A 588 ? THR A 594 ? ILE A 588 THR A 594 
AG 3 VAL A 621 ? PHE A 623 ? VAL A 621 PHE A 623 
CA 1 GLU B 116 ? SER B 124 ? GLU C 116 SER C 124 
CA 2 LEU B 160 ? LYS B 171 ? LEU C 160 LYS C 171 
CA 3 ASP B 90  ? VAL B 101 ? ASP C 90  VAL C 101 
CA 4 VAL B 73  ? ASN B 85  ? VAL C 73  ASN C 85  
CA 5 ASN B 219 ? ARG B 226 ? ASN C 219 ARG C 226 
CA 6 LEU B 249 ? PHE B 253 ? LEU C 249 PHE C 253 
CA 7 LYS B 238 ? GLU B 243 ? LYS C 238 GLU C 243 
CB 1 PHE B 107 ? HIS B 111 ? PHE C 107 HIS C 111 
CB 2 GLN B 147 ? LEU B 151 ? GLN C 147 LEU C 151 
CB 3 LYS B 138 ? TYR B 142 ? LYS C 138 TYR C 142 
CC 1 GLY B 178 ? ARG B 185 ? GLY C 178 ARG C 185 
CC 2 THR B 191 ? ASP B 198 ? THR C 191 ASP C 198 
CD 1 ILE B 231 ? SER B 234 ? ILE C 231 SER C 234 
CD 2 TYR B 266 ? CYS B 269 ? TYR C 266 CYS C 269 
CE 1 HIS B 272 ? PHE B 277 ? HIS C 272 PHE C 277 
CE 2 LYS B 283 ? ALA B 288 ? LYS C 283 ALA C 288 
CE 3 LYS B 322 ? ALA B 327 ? LYS C 322 ALA C 327 
CE 4 LEU B 341 ? TYR B 344 ? LEU C 341 TYR C 344 
CE 5 ALA B 335 ? MET B 336 ? ALA C 335 MET C 336 
CF 1 VAL B 381 ? MET B 383 ? VAL C 381 MET C 383 
CF 2 ARG B 488 ? ALA B 490 ? ARG C 488 ALA C 490 
CG 1 THR B 609 ? ASP B 613 ? THR C 609 ASP C 613 
CG 2 SER B 558 ? ARG B 565 ? SER C 558 ARG C 565 
CG 3 PRO B 548 ? ASP B 555 ? PRO C 548 ASP C 555 
CG 4 ILE B 632 ? TYR B 635 ? ILE C 632 TYR C 635 
CH 1 HIS B 601 ? LEU B 605 ? HIS C 601 LEU C 605 
CH 2 ILE B 588 ? THR B 594 ? ILE C 588 THR C 594 
CH 3 VAL B 621 ? PHE B 623 ? VAL C 621 PHE C 623 
# 
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 
AA 1 2 N GLN A 123 ? N GLN A 123 O TYR A 163 ? O TYR A 163 
AA 2 3 N ALA A 170 ? N ALA A 170 O PHE A 91  ? O PHE A 91  
AA 3 4 N LEU A 100 ? N LEU A 100 O ILE A 74  ? O ILE A 74  
AA 4 5 N TYR A 78  ? N TYR A 78  O ASN A 219 ? O ASN A 219 
AA 5 6 N ARG A 226 ? N ARG A 226 O LEU A 249 ? O LEU A 249 
AA 6 7 O HIS A 252 ? O HIS A 252 N VAL A 239 ? N VAL A 239 
AB 1 2 N LEU A 110 ? N LEU A 110 O ILE A 148 ? O ILE A 148 
AB 2 3 N LEU A 151 ? N LEU A 151 O LYS A 138 ? O LYS A 138 
AC 1 2 N TYR A 184 ? N TYR A 184 O ARG A 192 ? O ARG A 192 
AC 2 3 N THR A 197 ? N THR A 197 O TYR A 266 ? O TYR A 266 
AC 3 4 N CYS A 269 ? N CYS A 269 O ILE A 231 ? O ILE A 231 
AD 1 2 N GLY A 276 ? N GLY A 276 O VAL A 284 ? O VAL A 284 
AD 2 3 N SER A 285 ? N SER A 285 O LEU A 323 ? O LEU A 323 
AD 3 4 N ILE A 326 ? N ILE A 326 O ILE A 342 ? O ILE A 342 
AD 4 5 N THR A 343 ? N THR A 343 O MET A 336 ? O MET A 336 
AE 1 2 N THR A 382 ? N THR A 382 O ARG A 488 ? O ARG A 488 
AF 1 2 N LEU A 612 ? N LEU A 612 O LEU A 559 ? O LEU A 559 
AF 2 3 N GLU A 564 ? N GLU A 564 O LEU A 549 ? O LEU A 549 
AF 3 4 N LEU A 550 ? N LEU A 550 O ILE A 632 ? O ILE A 632 
AG 1 2 N LEU A 605 ? N LEU A 605 O ILE A 588 ? O ILE A 588 
AG 2 3 N SER A 593 ? N SER A 593 O LYS A 622 ? O LYS A 622 
CA 1 2 N GLN B 123 ? N GLN C 123 O TYR B 163 ? O TYR C 163 
CA 2 3 N ALA B 170 ? N ALA C 170 O PHE B 91  ? O PHE C 91  
CA 3 4 N LEU B 100 ? N LEU C 100 O ILE B 74  ? O ILE C 74  
CA 4 5 N TYR B 78  ? N TYR C 78  O ASN B 219 ? O ASN C 219 
CA 5 6 N ARG B 226 ? N ARG C 226 O LEU B 249 ? O LEU C 249 
CA 6 7 O HIS B 252 ? O HIS C 252 N VAL B 239 ? N VAL C 239 
CB 1 2 N LEU B 110 ? N LEU C 110 O ILE B 148 ? O ILE C 148 
CB 2 3 N LEU B 151 ? N LEU C 151 O LYS B 138 ? O LYS C 138 
CC 1 2 N TYR B 184 ? N TYR C 184 O ARG B 192 ? O ARG C 192 
CD 1 2 N LEU B 233 ? N LEU C 233 O ILE B 267 ? O ILE C 267 
CE 1 2 N GLY B 276 ? N GLY C 276 O VAL B 284 ? O VAL C 284 
CE 2 3 N SER B 285 ? N SER C 285 O LEU B 323 ? O LEU C 323 
CE 3 4 N ILE B 326 ? N ILE C 326 O ILE B 342 ? O ILE C 342 
CE 4 5 N THR B 343 ? N THR C 343 O MET B 336 ? O MET C 336 
CF 1 2 N THR B 382 ? N THR C 382 O ARG B 488 ? O ARG C 488 
CG 1 2 N LEU B 612 ? N LEU C 612 O LEU B 559 ? O LEU C 559 
CG 2 3 N GLU B 564 ? N GLU C 564 O LEU B 549 ? O LEU C 549 
CG 3 4 N LEU B 550 ? N LEU C 550 O ILE B 632 ? O ILE C 632 
CH 1 2 N LEU B 605 ? N LEU C 605 O ILE B 588 ? O ILE C 588 
CH 2 3 N SER B 593 ? N SER C 593 O LYS B 622 ? O LYS C 622 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A 1008'                                                       
AC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE EDO A 1964'                                                      
AC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE EDO A 1965'                                                      
AC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MES A 2002'                                                      
AC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN C 1020'                                                       
AC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE EDO C 1962'                                                      
AC7 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE EDO C 1963'                                                      
AC8 Software ? ? ? ? 6  'Binding site for Poly-Saccharide residues NAG A1071 through NAG A1072 bound to ASN A 85'  
AC9 Software ? ? ? ? 4  'Binding site for Mono-Saccharide NAG A1069 bound to ASN A 103'                            
BC1 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG A1081 bound to ASN A 119'                            
BC2 Software ? ? ? ? 8  'Binding site for Poly-Saccharide residues NAG A1073 through BMA A1075 bound to ASN A 219' 
BC3 Software ? ? ? ? 2  'Binding site for Poly-Saccharide residues NAG A1076 through BMA A1078 bound to ASN A 405' 
BC4 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG A1070 bound to ASN A 431'                            
BC5 Software ? ? ? ? 3  'Binding site for Poly-Saccharide residues NAG A1079 through NAG A1080 bound to ASN A 650' 
BC6 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG A1082 bound to ASN A 714'                            
BC7 Software ? ? ? ? 16 'Binding site for Poly-Saccharide residues BMA C1001 through BMA C1005 bound to ASN C 85'  
BC8 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG C1006 bound to ASN C 103'                            
BC9 Software ? ? ? ? 7  'Binding site for Poly-Saccharide residues NAG C1007 through NAG C1008 bound to ASN C 219' 
CC1 Software ? ? ? ? 1  'Binding site for Mono-Saccharide NAG C1010 bound to ASN C 294'                            
CC2 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG C1011 bound to ASN C 405'                            
CC3 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG C1009 bound to ASN C 431'                            
CC4 Software ? ? ? ? 1  'Binding site for Mono-Saccharide NAG C1013 bound to ASN C 650'                            
CC5 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG C1012 bound to ASN C 714'                            
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A  370 ? HIS A 370  . ? 1_555 ? 
2  AC1 4  HIS A  374 ? HIS A 374  . ? 1_555 ? 
3  AC1 4  GLU A  393 ? GLU A 393  . ? 1_555 ? 
4  AC1 4  2X0 C  1   ? 2X0 E 1    . ? 1_555 ? 
5  AC2 3  HIS A  77  ? HIS A 77   . ? 1_555 ? 
6  AC2 3  ASP A  79  ? ASP A 79   . ? 1_555 ? 
7  AC2 3  SER A  221 ? SER A 221  . ? 1_555 ? 
8  AC3 3  LYS A  283 ? LYS A 283  . ? 1_555 ? 
9  AC3 3  SER A  285 ? SER A 285  . ? 1_555 ? 
10 AC3 3  TYR A  287 ? TYR A 287  . ? 1_555 ? 
11 AC4 4  NAG K  .   ? NAG A 1074 . ? 1_555 ? 
12 AC4 4  BMA L  .   ? BMA A 1075 . ? 1_555 ? 
13 AC4 4  HOH MA .   ? HOH A 3276 . ? 1_555 ? 
14 AC4 4  HOH MA .   ? HOH A 3277 . ? 1_555 ? 
15 AC5 4  HIS B  370 ? HIS C 370  . ? 1_555 ? 
16 AC5 4  HIS B  374 ? HIS C 374  . ? 1_555 ? 
17 AC5 4  GLU B  393 ? GLU C 393  . ? 1_555 ? 
18 AC5 4  2X0 D  1   ? 2X0 F 1    . ? 1_555 ? 
19 AC6 7  SER B  280 ? SER C 280  . ? 1_555 ? 
20 AC6 7  GLY B  281 ? GLY C 281  . ? 1_555 ? 
21 AC6 7  VAL B  282 ? VAL C 282  . ? 1_555 ? 
22 AC6 7  TYR B  318 ? TYR C 318  . ? 1_555 ? 
23 AC6 7  PRO B  319 ? PRO C 319  . ? 1_555 ? 
24 AC6 7  LEU B  320 ? LEU C 320  . ? 1_555 ? 
25 AC6 7  HOH NA .   ? HOH C 3124 . ? 1_555 ? 
26 AC7 1  GLN B  728 ? GLN C 728  . ? 1_555 ? 
27 AC8 6  HIS A  83  ? HIS A 83   . ? 1_555 ? 
28 AC8 6  ASN A  85  ? ASN A 85   . ? 1_555 ? 
29 AC8 6  GLU A  227 ? GLU A 227  . ? 1_555 ? 
30 AC8 6  GLY A  246 ? GLY A 246  . ? 1_555 ? 
31 AC8 6  LEU A  248 ? LEU A 248  . ? 1_555 ? 
32 AC8 6  ASP B  291 ? ASP C 291  . ? 1_555 ? 
33 AC9 4  SER A  102 ? SER A 102  . ? 1_555 ? 
34 AC9 4  ASN A  103 ? ASN A 103  . ? 1_555 ? 
35 AC9 4  HOH MA .   ? HOH A 3269 . ? 1_555 ? 
36 AC9 4  HOH MA .   ? HOH A 3270 . ? 1_555 ? 
37 BC1 2  THR A  118 ? THR A 118  . ? 1_555 ? 
38 BC1 2  ASN A  119 ? ASN A 119  . ? 1_555 ? 
39 BC2 8  ASN A  219 ? ASN A 219  . ? 1_555 ? 
40 BC2 8  THR A  255 ? THR A 255  . ? 1_555 ? 
41 BC2 8  VAL A  257 ? VAL A 257  . ? 1_555 ? 
42 BC2 8  LYS A  258 ? LYS A 258  . ? 1_555 ? 
43 BC2 8  TYR A  487 ? TYR A 487  . ? 1_555 ? 
44 BC2 8  MES V  .   ? MES A 2002 . ? 1_555 ? 
45 BC2 8  HOH MA .   ? HOH A 3271 . ? 1_555 ? 
46 BC2 8  HOH MA .   ? HOH A 3275 . ? 1_555 ? 
47 BC3 2  ASN A  405 ? ASN A 405  . ? 1_555 ? 
48 BC3 2  ASP A  414 ? ASP A 414  . ? 1_555 ? 
49 BC4 2  ASN A  431 ? ASN A 431  . ? 1_555 ? 
50 BC4 2  LYS A  545 ? LYS A 545  . ? 1_555 ? 
51 BC5 3  ASN A  650 ? ASN A 650  . ? 1_555 ? 
52 BC5 3  LEU A  653 ? LEU A 653  . ? 1_555 ? 
53 BC5 3  HOH MA .   ? HOH A 3273 . ? 1_555 ? 
54 BC6 2  ASN A  714 ? ASN A 714  . ? 1_555 ? 
55 BC6 2  HOH MA .   ? HOH A 3274 . ? 1_555 ? 
56 BC7 16 HIS A  272 ? HIS A 272  . ? 1_555 ? 
57 BC7 16 SER A  273 ? SER A 273  . ? 1_555 ? 
58 BC7 16 LEU A  274 ? LEU A 274  . ? 1_555 ? 
59 BC7 16 PRO A  290 ? PRO A 290  . ? 1_555 ? 
60 BC7 16 ASP A  291 ? ASP A 291  . ? 1_555 ? 
61 BC7 16 ARG A  293 ? ARG A 293  . ? 1_555 ? 
62 BC7 16 HOH MA .   ? HOH A 3084 . ? 1_555 ? 
63 BC7 16 HIS B  83  ? HIS C 83   . ? 1_555 ? 
64 BC7 16 ASN B  85  ? ASN C 85   . ? 1_555 ? 
65 BC7 16 GLU B  227 ? GLU C 227  . ? 1_555 ? 
66 BC7 16 LEU B  248 ? LEU C 248  . ? 1_555 ? 
67 BC7 16 HOH NA .   ? HOH C 3009 . ? 1_555 ? 
68 BC7 16 HOH NA .   ? HOH C 3117 . ? 1_555 ? 
69 BC7 16 HOH NA .   ? HOH C 3118 . ? 1_555 ? 
70 BC7 16 HOH NA .   ? HOH C 3119 . ? 1_555 ? 
71 BC7 16 HOH NA .   ? HOH C 3122 . ? 1_555 ? 
72 BC8 2  SER B  102 ? SER C 102  . ? 1_555 ? 
73 BC8 2  ASN B  103 ? ASN C 103  . ? 1_555 ? 
74 BC9 7  ASN B  219 ? ASN C 219  . ? 1_555 ? 
75 BC9 7  THR B  255 ? THR C 255  . ? 1_555 ? 
76 BC9 7  THR B  256 ? THR C 256  . ? 1_555 ? 
77 BC9 7  VAL B  257 ? VAL C 257  . ? 1_555 ? 
78 BC9 7  LYS B  258 ? LYS C 258  . ? 1_555 ? 
79 BC9 7  TYR B  487 ? TYR C 487  . ? 1_555 ? 
80 BC9 7  HOH NA .   ? HOH C 3120 . ? 1_555 ? 
81 CC1 1  ASN B  294 ? ASN C 294  . ? 1_555 ? 
82 CC2 2  ASN B  405 ? ASN C 405  . ? 1_555 ? 
83 CC2 2  ASP B  414 ? ASP C 414  . ? 1_555 ? 
84 CC3 3  ASN B  431 ? ASN C 431  . ? 1_555 ? 
85 CC3 3  LYS B  545 ? LYS C 545  . ? 1_555 ? 
86 CC3 3  LEU B  580 ? LEU C 580  . ? 1_555 ? 
87 CC4 1  ASN B  650 ? ASN C 650  . ? 1_555 ? 
88 CC5 2  ASN B  714 ? ASN C 714  . ? 1_555 ? 
89 CC5 2  HOH NA .   ? HOH C 3123 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          5AB0 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    5AB0 
_atom_sites.fract_transf_matrix[1][1]   0.013271 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000114 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007439 
_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]   0.007752 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
P  
S  
ZN 
# 
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   . PRO A  1 54  ? -15.387 -3.453  -2.386  1.00 82.09  ? 54   PRO A N   1 
ATOM   2     C  CA  . PRO A  1 54  ? -14.034 -2.883  -2.329  1.00 81.86  ? 54   PRO A CA  1 
ATOM   3     C  C   . PRO A  1 54  ? -13.976 -1.726  -1.326  1.00 74.14  ? 54   PRO A C   1 
ATOM   4     O  O   . PRO A  1 54  ? -13.493 -0.650  -1.659  1.00 72.74  ? 54   PRO A O   1 
ATOM   5     C  CB  . PRO A  1 54  ? -13.795 -2.390  -3.766  1.00 86.59  ? 54   PRO A CB  1 
ATOM   6     C  CG  . PRO A  1 54  ? -14.918 -2.978  -4.601  1.00 81.62  ? 54   PRO A CG  1 
ATOM   7     C  CD  . PRO A  1 54  ? -16.058 -3.179  -3.667  1.00 73.44  ? 54   PRO A CD  1 
ATOM   8     N  N   . VAL A  1 55  ? -14.445 -1.969  -0.103  1.00 70.06  ? 55   VAL A N   1 
ATOM   9     C  CA  . VAL A  1 55  ? -15.028 -0.914  0.717   1.00 75.09  ? 55   VAL A CA  1 
ATOM   10    C  C   . VAL A  1 55  ? -14.915 -1.045  2.252   1.00 70.79  ? 55   VAL A C   1 
ATOM   11    O  O   . VAL A  1 55  ? -15.172 -2.095  2.823   1.00 70.03  ? 55   VAL A O   1 
ATOM   12    C  CB  . VAL A  1 55  ? -16.517 -0.809  0.358   1.00 85.85  ? 55   VAL A CB  1 
ATOM   13    C  CG1 . VAL A  1 55  ? -17.307 -0.104  1.438   1.00 82.96  ? 55   VAL A CG1 1 
ATOM   14    C  CG2 . VAL A  1 55  ? -16.702 -0.178  -1.026  1.00 77.98  ? 55   VAL A CG2 1 
ATOM   15    N  N   . ALA A  1 56  ? -14.573 0.064   2.910   1.00 70.62  ? 56   ALA A N   1 
ATOM   16    C  CA  . ALA A  1 56  ? -14.406 0.150   4.378   1.00 73.45  ? 56   ALA A CA  1 
ATOM   17    C  C   . ALA A  1 56  ? -14.572 1.636   4.765   1.00 68.90  ? 56   ALA A C   1 
ATOM   18    O  O   . ALA A  1 56  ? -14.748 2.434   3.824   1.00 77.87  ? 56   ALA A O   1 
ATOM   19    C  CB  . ALA A  1 56  ? -13.028 -0.403  4.777   1.00 70.33  ? 56   ALA A CB  1 
ATOM   20    N  N   . THR A  1 57  ? -14.556 2.068   6.039   1.00 61.77  ? 57   THR A N   1 
ATOM   21    C  CA  . THR A  1 57  ? -14.599 1.258   7.234   1.00 73.55  ? 57   THR A CA  1 
ATOM   22    C  C   . THR A  1 57  ? -15.953 1.203   7.870   1.00 78.03  ? 57   THR A C   1 
ATOM   23    O  O   . THR A  1 57  ? -16.338 0.137   8.357   1.00 80.82  ? 57   THR A O   1 
ATOM   24    C  CB  . THR A  1 57  ? -13.608 1.775   8.330   1.00 67.27  ? 57   THR A CB  1 
ATOM   25    O  OG1 . THR A  1 57  ? -13.869 3.148   8.619   1.00 71.37  ? 57   THR A OG1 1 
ATOM   26    C  CG2 . THR A  1 57  ? -12.199 1.644   7.925   1.00 61.32  ? 57   THR A CG2 1 
ATOM   27    N  N   . ASN A  1 58  ? -16.614 2.347   7.973   1.00 78.88  ? 58   ASN A N   1 
ATOM   28    C  CA  A ASN A  1 58  ? -17.938 2.433   8.537   0.65 80.22  ? 58   ASN A CA  1 
ATOM   29    C  CA  B ASN A  1 58  ? -17.936 2.315   8.564   0.35 79.94  ? 58   ASN A CA  1 
ATOM   30    C  C   . ASN A  1 58  ? -19.010 2.141   7.504   1.00 77.59  ? 58   ASN A C   1 
ATOM   31    O  O   . ASN A  1 58  ? -19.993 2.869   7.453   1.00 72.35  ? 58   ASN A O   1 
ATOM   32    C  CB  A ASN A  1 58  ? -18.144 3.829   9.122   0.65 77.83  ? 58   ASN A CB  1 
ATOM   33    C  CB  B ASN A  1 58  ? -18.193 3.552   9.404   0.35 77.38  ? 58   ASN A CB  1 
ATOM   34    C  CG  A ASN A  1 58  ? -17.889 4.938   8.102   0.65 72.61  ? 58   ASN A CG  1 
ATOM   35    C  CG  B ASN A  1 58  ? -19.197 3.270   10.508  0.35 71.75  ? 58   ASN A CG  1 
ATOM   36    O  OD1 A ASN A  1 58  ? -17.617 4.678   6.929   0.65 69.02  ? 58   ASN A OD1 1 
ATOM   37    O  OD1 B ASN A  1 58  ? -19.646 2.131   10.664  0.35 67.76  ? 58   ASN A OD1 1 
ATOM   38    N  ND2 A ASN A  1 58  ? -17.975 6.184   8.558   0.65 68.77  ? 58   ASN A ND2 1 
ATOM   39    N  ND2 B ASN A  1 58  ? -19.527 4.281   11.294  0.35 70.59  ? 58   ASN A ND2 1 
ATOM   40    N  N   . GLY A  1 59  ? -18.836 1.097   6.697   1.00 78.16  ? 59   GLY A N   1 
ATOM   41    C  CA  . GLY A  1 59  ? -19.748 0.879   5.596   1.00 77.82  ? 59   GLY A CA  1 
ATOM   42    C  C   . GLY A  1 59  ? -19.362 1.947   4.604   1.00 73.73  ? 59   GLY A C   1 
ATOM   43    O  O   . GLY A  1 59  ? -18.243 2.435   4.669   1.00 73.31  ? 59   GLY A O   1 
ATOM   44    N  N   . GLU A  1 60  ? -20.275 2.318   3.712   1.00 82.82  ? 60   GLU A N   1 
ATOM   45    C  CA  . GLU A  1 60  ? -20.057 3.415   2.765   1.00 78.26  ? 60   GLU A CA  1 
ATOM   46    C  C   . GLU A  1 60  ? -18.946 3.060   1.787   1.00 69.57  ? 60   GLU A C   1 
ATOM   47    O  O   . GLU A  1 60  ? -17.843 2.709   2.174   1.00 66.79  ? 60   GLU A O   1 
ATOM   48    C  CB  . GLU A  1 60  ? -19.743 4.720   3.507   1.00 76.56  ? 60   GLU A CB  1 
ATOM   49    C  CG  . GLU A  1 60  ? -20.693 5.868   3.191   1.00 77.04  ? 60   GLU A CG  1 
ATOM   50    C  CD  . GLU A  1 60  ? -20.498 7.061   4.121   1.00 85.89  ? 60   GLU A CD  1 
ATOM   51    O  OE1 . GLU A  1 60  ? -20.314 6.850   5.341   1.00 78.87  ? 60   GLU A OE1 1 
ATOM   52    O  OE2 . GLU A  1 60  ? -20.530 8.213   3.632   1.00 93.60  ? 60   GLU A OE2 1 
ATOM   53    N  N   . ARG A  1 61  ? -19.252 3.151   0.504   1.00 76.56  ? 61   ARG A N   1 
ATOM   54    C  CA  . ARG A  1 61  ? -18.310 2.731   -0.520  1.00 78.91  ? 61   ARG A CA  1 
ATOM   55    C  C   . ARG A  1 61  ? -17.070 3.635   -0.602  1.00 77.22  ? 61   ARG A C   1 
ATOM   56    O  O   . ARG A  1 61  ? -17.177 4.864   -0.587  1.00 79.22  ? 61   ARG A O   1 
ATOM   57    C  CB  . ARG A  1 61  ? -19.017 2.659   -1.876  1.00 75.69  ? 61   ARG A CB  1 
ATOM   58    C  CG  . ARG A  1 61  ? -18.099 2.365   -3.038  1.00 75.67  ? 61   ARG A CG  1 
ATOM   59    C  CD  . ARG A  1 61  ? -18.775 1.508   -4.099  1.00 81.97  ? 61   ARG A CD  1 
ATOM   60    N  NE  . ARG A  1 61  ? -17.933 1.387   -5.286  1.00 86.35  ? 61   ARG A NE  1 
ATOM   61    C  CZ  . ARG A  1 61  ? -16.840 0.630   -5.353  1.00 91.49  ? 61   ARG A CZ  1 
ATOM   62    N  NH1 . ARG A  1 61  ? -16.452 -0.080  -4.297  1.00 86.15  ? 61   ARG A NH1 1 
ATOM   63    N  NH2 . ARG A  1 61  ? -16.127 0.588   -6.473  1.00 90.30  ? 61   ARG A NH2 1 
ATOM   64    N  N   . PHE A  1 62  ? -15.893 3.020   -0.667  1.00 65.62  ? 62   PHE A N   1 
ATOM   65    C  CA  . PHE A  1 62  ? -14.680 3.777   -0.891  1.00 65.20  ? 62   PHE A CA  1 
ATOM   66    C  C   . PHE A  1 62  ? -14.520 4.023   -2.396  1.00 63.49  ? 62   PHE A C   1 
ATOM   67    O  O   . PHE A  1 62  ? -14.369 3.084   -3.178  1.00 65.62  ? 62   PHE A O   1 
ATOM   68    C  CB  . PHE A  1 62  ? -13.467 3.049   -0.307  1.00 71.46  ? 62   PHE A CB  1 
ATOM   69    C  CG  . PHE A  1 62  ? -12.288 3.951   -0.046  1.00 62.19  ? 62   PHE A CG  1 
ATOM   70    C  CD1 . PHE A  1 62  ? -12.243 4.740   1.089   1.00 61.25  ? 62   PHE A CD1 1 
ATOM   71    C  CD2 . PHE A  1 62  ? -11.239 4.014   -0.942  1.00 61.24  ? 62   PHE A CD2 1 
ATOM   72    C  CE1 . PHE A  1 62  ? -11.179 5.571   1.327   1.00 56.57  ? 62   PHE A CE1 1 
ATOM   73    C  CE2 . PHE A  1 62  ? -10.167 4.842   -0.707  1.00 58.16  ? 62   PHE A CE2 1 
ATOM   74    C  CZ  . PHE A  1 62  ? -10.144 5.625   0.427   1.00 58.76  ? 62   PHE A CZ  1 
ATOM   75    N  N   . PRO A  1 63  ? -14.562 5.297   -2.801  1.00 59.02  ? 63   PRO A N   1 
ATOM   76    C  CA  . PRO A  1 63  ? -14.657 5.746   -4.201  1.00 58.00  ? 63   PRO A CA  1 
ATOM   77    C  C   . PRO A  1 63  ? -13.551 5.240   -5.120  1.00 56.05  ? 63   PRO A C   1 
ATOM   78    O  O   . PRO A  1 63  ? -13.583 5.520   -6.317  1.00 48.93  ? 63   PRO A O   1 
ATOM   79    C  CB  . PRO A  1 63  ? -14.573 7.273   -4.090  1.00 56.53  ? 63   PRO A CB  1 
ATOM   80    C  CG  . PRO A  1 63  ? -14.978 7.593   -2.685  1.00 61.69  ? 63   PRO A CG  1 
ATOM   81    C  CD  . PRO A  1 63  ? -14.592 6.416   -1.842  1.00 62.67  ? 63   PRO A CD  1 
ATOM   82    N  N   . TRP A  1 64  ? -12.595 4.498   -4.581  1.00 60.04  ? 64   TRP A N   1 
ATOM   83    C  CA  . TRP A  1 64  ? -11.386 4.187   -5.332  1.00 60.03  ? 64   TRP A CA  1 
ATOM   84    C  C   . TRP A  1 64  ? -10.799 2.839   -4.938  1.00 60.36  ? 64   TRP A C   1 
ATOM   85    O  O   . TRP A  1 64  ? -10.792 2.478   -3.763  1.00 61.79  ? 64   TRP A O   1 
ATOM   86    C  CB  . TRP A  1 64  ? -10.365 5.300   -5.109  1.00 61.28  ? 64   TRP A CB  1 
ATOM   87    C  CG  . TRP A  1 64  ? -9.110  5.115   -5.840  1.00 51.73  ? 64   TRP A CG  1 
ATOM   88    C  CD1 . TRP A  1 64  ? -7.948  4.617   -5.346  1.00 48.63  ? 64   TRP A CD1 1 
ATOM   89    C  CD2 . TRP A  1 64  ? -8.869  5.433   -7.216  1.00 51.89  ? 64   TRP A CD2 1 
ATOM   90    N  NE1 . TRP A  1 64  ? -6.988  4.601   -6.335  1.00 54.65  ? 64   TRP A NE1 1 
ATOM   91    C  CE2 . TRP A  1 64  ? -7.531  5.092   -7.494  1.00 51.91  ? 64   TRP A CE2 1 
ATOM   92    C  CE3 . TRP A  1 64  ? -9.656  5.967   -8.241  1.00 50.64  ? 64   TRP A CE3 1 
ATOM   93    C  CZ2 . TRP A  1 64  ? -6.960  5.268   -8.753  1.00 50.45  ? 64   TRP A CZ2 1 
ATOM   94    C  CZ3 . TRP A  1 64  ? -9.088  6.144   -9.489  1.00 53.37  ? 64   TRP A CZ3 1 
ATOM   95    C  CH2 . TRP A  1 64  ? -7.751  5.795   -9.734  1.00 55.40  ? 64   TRP A CH2 1 
ATOM   96    N  N   . GLN A  1 65  ? -10.290 2.102   -5.914  1.00 61.05  ? 65   GLN A N   1 
ATOM   97    C  CA  . GLN A  1 65  ? -9.905  0.713   -5.670  1.00 68.47  ? 65   GLN A CA  1 
ATOM   98    C  C   . GLN A  1 65  ? -8.403  0.435   -5.706  1.00 66.12  ? 65   GLN A C   1 
ATOM   99    O  O   . GLN A  1 65  ? -7.933  -0.501  -5.058  1.00 66.51  ? 65   GLN A O   1 
ATOM   100   C  CB  . GLN A  1 65  ? -10.596 -0.193  -6.685  1.00 71.66  ? 65   GLN A CB  1 
ATOM   101   C  CG  . GLN A  1 65  ? -12.102 -0.014  -6.732  1.00 79.24  ? 65   GLN A CG  1 
ATOM   102   C  CD  . GLN A  1 65  ? -12.630 -0.130  -8.143  1.00 92.15  ? 65   GLN A CD  1 
ATOM   103   O  OE1 . GLN A  1 65  ? -11.870 -0.035  -9.111  1.00 93.56  ? 65   GLN A OE1 1 
ATOM   104   N  NE2 . GLN A  1 65  ? -13.934 -0.339  -8.273  1.00 89.95  ? 65   GLN A NE2 1 
ATOM   105   N  N   . GLU A  1 66  ? -7.655  1.240   -6.456  1.00 59.75  ? 66   GLU A N   1 
ATOM   106   C  CA  . GLU A  1 66  ? -6.240  0.969   -6.710  1.00 56.26  ? 66   GLU A CA  1 
ATOM   107   C  C   . GLU A  1 66  ? -5.307  1.426   -5.582  1.00 54.43  ? 66   GLU A C   1 
ATOM   108   O  O   . GLU A  1 66  ? -5.511  2.492   -4.995  1.00 58.89  ? 66   GLU A O   1 
ATOM   109   C  CB  . GLU A  1 66  ? -5.828  1.631   -8.028  1.00 56.58  ? 66   GLU A CB  1 
ATOM   110   C  CG  . GLU A  1 66  ? -6.828  1.426   -9.172  1.00 54.92  ? 66   GLU A CG  1 
ATOM   111   C  CD  . GLU A  1 66  ? -7.028  -0.047  -9.536  1.00 74.73  ? 66   GLU A CD  1 
ATOM   112   O  OE1 . GLU A  1 66  ? -6.148  -0.886  -9.223  1.00 67.10  ? 66   GLU A OE1 1 
ATOM   113   O  OE2 . GLU A  1 66  ? -8.073  -0.370  -10.144 1.00 88.88  ? 66   GLU A OE2 1 
ATOM   114   N  N   . LEU A  1 67  ? -4.281  0.633   -5.271  1.00 54.37  ? 67   LEU A N   1 
ATOM   115   C  CA  . LEU A  1 67  ? -3.329  1.063   -4.243  1.00 53.36  ? 67   LEU A CA  1 
ATOM   116   C  C   . LEU A  1 67  ? -2.522  2.245   -4.768  1.00 47.23  ? 67   LEU A C   1 
ATOM   117   O  O   . LEU A  1 67  ? -2.165  3.123   -4.005  1.00 56.88  ? 67   LEU A O   1 
ATOM   118   C  CB  . LEU A  1 67  ? -2.408  -0.084  -3.781  1.00 52.06  ? 67   LEU A CB  1 
ATOM   119   C  CG  . LEU A  1 67  ? -1.528  -0.906  -4.738  1.00 61.36  ? 67   LEU A CG  1 
ATOM   120   C  CD1 . LEU A  1 67  ? -0.299  -0.146  -5.295  1.00 60.90  ? 67   LEU A CD1 1 
ATOM   121   C  CD2 . LEU A  1 67  ? -1.072  -2.162  -4.030  1.00 58.18  ? 67   LEU A CD2 1 
ATOM   122   N  N   . ARG A  1 68  ? -2.229  2.272   -6.062  1.00 39.23  ? 68   ARG A N   1 
ATOM   123   C  CA  . ARG A  1 68  ? -1.719  3.493   -6.681  1.00 49.06  ? 68   ARG A CA  1 
ATOM   124   C  C   . ARG A  1 68  ? -2.800  4.586   -6.640  1.00 54.65  ? 68   ARG A C   1 
ATOM   125   O  O   . ARG A  1 68  ? -3.976  4.303   -6.889  1.00 53.11  ? 68   ARG A O   1 
ATOM   126   C  CB  . ARG A  1 68  ? -1.284  3.253   -8.130  1.00 40.63  ? 68   ARG A CB  1 
ATOM   127   C  CG  . ARG A  1 68  ? -0.201  2.209   -8.311  1.00 47.57  ? 68   ARG A CG  1 
ATOM   128   C  CD  . ARG A  1 68  ? 1.111   2.582   -7.624  1.00 38.77  ? 68   ARG A CD  1 
ATOM   129   N  NE  . ARG A  1 68  ? 1.715   3.782   -8.181  1.00 36.47  ? 68   ARG A NE  1 
ATOM   130   C  CZ  . ARG A  1 68  ? 2.407   3.829   -9.317  1.00 38.97  ? 68   ARG A CZ  1 
ATOM   131   N  NH1 . ARG A  1 68  ? 2.606   2.739   -10.039 1.00 34.75  ? 68   ARG A NH1 1 
ATOM   132   N  NH2 . ARG A  1 68  ? 2.902   4.986   -9.739  1.00 42.38  ? 68   ARG A NH2 1 
ATOM   133   N  N   . LEU A  1 69  ? -2.405  5.825   -6.336  1.00 48.84  ? 69   LEU A N   1 
ATOM   134   C  CA  . LEU A  1 69  ? -3.361  6.923   -6.182  1.00 47.60  ? 69   LEU A CA  1 
ATOM   135   C  C   . LEU A  1 69  ? -3.888  7.378   -7.530  1.00 50.10  ? 69   LEU A C   1 
ATOM   136   O  O   . LEU A  1 69  ? -3.292  7.064   -8.567  1.00 48.49  ? 69   LEU A O   1 
ATOM   137   C  CB  . LEU A  1 69  ? -2.717  8.111   -5.456  1.00 43.77  ? 69   LEU A CB  1 
ATOM   138   C  CG  . LEU A  1 69  ? -2.331  7.893   -3.993  1.00 44.29  ? 69   LEU A CG  1 
ATOM   139   C  CD1 . LEU A  1 69  ? -1.575  9.096   -3.496  1.00 40.95  ? 69   LEU A CD1 1 
ATOM   140   C  CD2 . LEU A  1 69  ? -3.523  7.564   -3.081  1.00 42.99  ? 69   LEU A CD2 1 
ATOM   141   N  N   . PRO A  1 70  ? -5.003  8.129   -7.531  1.00 45.60  ? 70   PRO A N   1 
ATOM   142   C  CA  . PRO A  1 70  ? -5.394  8.687   -8.823  1.00 47.78  ? 70   PRO A CA  1 
ATOM   143   C  C   . PRO A  1 70  ? -4.380  9.729   -9.254  1.00 48.02  ? 70   PRO A C   1 
ATOM   144   O  O   . PRO A  1 70  ? -3.540  10.148  -8.455  1.00 48.51  ? 70   PRO A O   1 
ATOM   145   C  CB  . PRO A  1 70  ? -6.766  9.313   -8.542  1.00 46.87  ? 70   PRO A CB  1 
ATOM   146   C  CG  . PRO A  1 70  ? -7.275  8.598   -7.354  1.00 43.66  ? 70   PRO A CG  1 
ATOM   147   C  CD  . PRO A  1 70  ? -6.049  8.323   -6.518  1.00 51.19  ? 70   PRO A CD  1 
ATOM   148   N  N   . SER A  1 71  ? -4.447  10.139  -10.507 1.00 45.68  ? 71   SER A N   1 
ATOM   149   C  CA  . SER A  1 71  ? -3.568  11.190  -10.990 1.00 47.55  ? 71   SER A CA  1 
ATOM   150   C  C   . SER A  1 71  ? -4.345  12.503  -11.191 1.00 51.03  ? 71   SER A C   1 
ATOM   151   O  O   . SER A  1 71  ? -3.836  13.485  -11.739 1.00 46.01  ? 71   SER A O   1 
ATOM   152   C  CB  . SER A  1 71  ? -2.923  10.747  -12.288 1.00 41.10  ? 71   SER A CB  1 
ATOM   153   O  OG  . SER A  1 71  ? -3.912  10.682  -13.302 1.00 55.83  ? 71   SER A OG  1 
ATOM   154   N  N   . VAL A  1 72  ? -5.590  12.501  -10.734 1.00 49.78  ? 72   VAL A N   1 
ATOM   155   C  CA  . VAL A  1 72  ? -6.525  13.562  -11.052 1.00 53.12  ? 72   VAL A CA  1 
ATOM   156   C  C   . VAL A  1 72  ? -6.152  14.847  -10.335 1.00 55.58  ? 72   VAL A C   1 
ATOM   157   O  O   . VAL A  1 72  ? -6.145  15.926  -10.926 1.00 54.38  ? 72   VAL A O   1 
ATOM   158   C  CB  . VAL A  1 72  ? -7.951  13.165  -10.666 1.00 52.74  ? 72   VAL A CB  1 
ATOM   159   C  CG1 . VAL A  1 72  ? -8.923  14.180  -11.187 1.00 65.36  ? 72   VAL A CG1 1 
ATOM   160   C  CG2 . VAL A  1 72  ? -8.278  11.819  -11.233 1.00 54.00  ? 72   VAL A CG2 1 
ATOM   161   N  N   . VAL A  1 73  ? -5.864  14.716  -9.048  1.00 52.62  ? 73   VAL A N   1 
ATOM   162   C  CA  . VAL A  1 73  ? -5.441  15.843  -8.245  1.00 52.53  ? 73   VAL A CA  1 
ATOM   163   C  C   . VAL A  1 73  ? -3.917  15.823  -8.073  1.00 49.74  ? 73   VAL A C   1 
ATOM   164   O  O   . VAL A  1 73  ? -3.314  14.815  -7.705  1.00 43.29  ? 73   VAL A O   1 
ATOM   165   C  CB  . VAL A  1 73  ? -6.151  15.836  -6.889  1.00 44.36  ? 73   VAL A CB  1 
ATOM   166   C  CG1 . VAL A  1 73  ? -7.634  15.872  -7.105  1.00 53.83  ? 73   VAL A CG1 1 
ATOM   167   C  CG2 . VAL A  1 73  ? -5.836  14.582  -6.159  1.00 61.67  ? 73   VAL A CG2 1 
ATOM   168   N  N   . ILE A  1 74  ? -3.302  16.954  -8.371  1.00 47.76  ? 74   ILE A N   1 
ATOM   169   C  CA  . ILE A  1 74  ? -1.861  17.085  -8.339  1.00 44.64  ? 74   ILE A CA  1 
ATOM   170   C  C   . ILE A  1 74  ? -1.475  18.073  -7.266  1.00 44.32  ? 74   ILE A C   1 
ATOM   171   O  O   . ILE A  1 74  ? -1.881  19.237  -7.331  1.00 45.11  ? 74   ILE A O   1 
ATOM   172   C  CB  . ILE A  1 74  ? -1.319  17.559  -9.703  1.00 49.18  ? 74   ILE A CB  1 
ATOM   173   C  CG1 . ILE A  1 74  ? -1.548  16.489  -10.770 1.00 49.29  ? 74   ILE A CG1 1 
ATOM   174   C  CG2 . ILE A  1 74  ? 0.151   17.938  -9.618  1.00 44.32  ? 74   ILE A CG2 1 
ATOM   175   C  CD1 . ILE A  1 74  ? -1.649  17.072  -12.186 1.00 53.07  ? 74   ILE A CD1 1 
ATOM   176   N  N   . PRO A  1 75  ? -0.710  17.611  -6.259  1.00 45.87  ? 75   PRO A N   1 
ATOM   177   C  CA  . PRO A  1 75  ? -0.211  18.469  -5.181  1.00 37.89  ? 75   PRO A CA  1 
ATOM   178   C  C   . PRO A  1 75  ? 0.820   19.418  -5.718  1.00 38.68  ? 75   PRO A C   1 
ATOM   179   O  O   . PRO A  1 75  ? 1.529   19.081  -6.669  1.00 39.04  ? 75   PRO A O   1 
ATOM   180   C  CB  . PRO A  1 75  ? 0.418   17.482  -4.213  1.00 44.45  ? 75   PRO A CB  1 
ATOM   181   C  CG  . PRO A  1 75  ? 0.834   16.353  -5.076  1.00 39.20  ? 75   PRO A CG  1 
ATOM   182   C  CD  . PRO A  1 75  ? -0.256  16.225  -6.092  1.00 43.19  ? 75   PRO A CD  1 
ATOM   183   N  N   . LEU A  1 76  ? 0.916   20.594  -5.129  1.00 36.95  ? 76   LEU A N   1 
ATOM   184   C  CA  . LEU A  1 76  ? 1.887   21.552  -5.622  1.00 43.46  ? 76   LEU A CA  1 
ATOM   185   C  C   . LEU A  1 76  ? 2.717   22.070  -4.475  1.00 35.71  ? 76   LEU A C   1 
ATOM   186   O  O   . LEU A  1 76  ? 3.897   22.408  -4.614  1.00 32.84  ? 76   LEU A O   1 
ATOM   187   C  CB  . LEU A  1 76  ? 1.190   22.709  -6.332  1.00 40.16  ? 76   LEU A CB  1 
ATOM   188   C  CG  . LEU A  1 76  ? 0.383   22.400  -7.588  1.00 42.57  ? 76   LEU A CG  1 
ATOM   189   C  CD1 . LEU A  1 76  ? -0.331  23.684  -8.076  1.00 42.09  ? 76   LEU A CD1 1 
ATOM   190   C  CD2 . LEU A  1 76  ? 1.286   21.827  -8.660  1.00 31.87  ? 76   LEU A CD2 1 
ATOM   191   N  N   . HIS A  1 77  ? 2.078   22.120  -3.327  1.00 37.46  ? 77   HIS A N   1 
ATOM   192   C  CA  . HIS A  1 77  ? 2.651   22.831  -2.207  1.00 40.67  ? 77   HIS A CA  1 
ATOM   193   C  C   . HIS A  1 77  ? 1.962   22.423  -0.923  1.00 36.69  ? 77   HIS A C   1 
ATOM   194   O  O   . HIS A  1 77  ? 0.741   22.364  -0.863  1.00 38.45  ? 77   HIS A O   1 
ATOM   195   C  CB  . HIS A  1 77  ? 2.542   24.348  -2.416  1.00 34.07  ? 77   HIS A CB  1 
ATOM   196   C  CG  . HIS A  1 77  ? 3.144   25.131  -1.300  1.00 36.95  ? 77   HIS A CG  1 
ATOM   197   N  ND1 . HIS A  1 77  ? 4.390   25.709  -1.388  1.00 40.23  ? 77   HIS A ND1 1 
ATOM   198   C  CD2 . HIS A  1 77  ? 2.706   25.369  -0.043  1.00 34.57  ? 77   HIS A CD2 1 
ATOM   199   C  CE1 . HIS A  1 77  ? 4.685   26.294  -0.243  1.00 41.65  ? 77   HIS A CE1 1 
ATOM   200   N  NE2 . HIS A  1 77  ? 3.679   26.102  0.591   1.00 42.02  ? 77   HIS A NE2 1 
ATOM   201   N  N   . TYR A  1 78  ? 2.754   22.127  0.096   1.00 35.81  ? 78   TYR A N   1 
ATOM   202   C  CA  . TYR A  1 78  ? 2.202   21.817  1.406   1.00 35.51  ? 78   TYR A CA  1 
ATOM   203   C  C   . TYR A  1 78  ? 2.618   22.886  2.401   1.00 34.67  ? 78   TYR A C   1 
ATOM   204   O  O   . TYR A  1 78  ? 3.796   23.213  2.486   1.00 39.74  ? 78   TYR A O   1 
ATOM   205   C  CB  . TYR A  1 78  ? 2.694   20.458  1.917   1.00 31.14  ? 78   TYR A CB  1 
ATOM   206   C  CG  . TYR A  1 78  ? 2.286   19.221  1.162   1.00 32.02  ? 78   TYR A CG  1 
ATOM   207   C  CD1 . TYR A  1 78  ? 2.763   18.967  -0.132  1.00 31.55  ? 78   TYR A CD1 1 
ATOM   208   C  CD2 . TYR A  1 78  ? 1.499   18.242  1.779   1.00 32.93  ? 78   TYR A CD2 1 
ATOM   209   C  CE1 . TYR A  1 78  ? 2.426   17.789  -0.811  1.00 27.90  ? 78   TYR A CE1 1 
ATOM   210   C  CE2 . TYR A  1 78  ? 1.145   17.064  1.111   1.00 29.35  ? 78   TYR A CE2 1 
ATOM   211   C  CZ  . TYR A  1 78  ? 1.617   16.848  -0.180  1.00 34.26  ? 78   TYR A CZ  1 
ATOM   212   O  OH  . TYR A  1 78  ? 1.280   15.688  -0.835  1.00 39.25  ? 78   TYR A OH  1 
ATOM   213   N  N   . ASP A  1 79  ? 1.673   23.445  3.142   1.00 39.75  ? 79   ASP A N   1 
ATOM   214   C  CA  . ASP A  1 79  ? 2.036   24.146  4.374   1.00 43.17  ? 79   ASP A CA  1 
ATOM   215   C  C   . ASP A  1 79  ? 1.910   23.111  5.452   1.00 35.98  ? 79   ASP A C   1 
ATOM   216   O  O   . ASP A  1 79  ? 0.856   22.532  5.618   1.00 40.75  ? 79   ASP A O   1 
ATOM   217   C  CB  . ASP A  1 79  ? 1.145   25.358  4.678   1.00 41.91  ? 79   ASP A CB  1 
ATOM   218   C  CG  . ASP A  1 79  ? 1.322   26.481  3.671   1.00 57.15  ? 79   ASP A CG  1 
ATOM   219   O  OD1 . ASP A  1 79  ? 2.277   26.407  2.872   1.00 50.29  ? 79   ASP A OD1 1 
ATOM   220   O  OD2 . ASP A  1 79  ? 0.514   27.443  3.673   1.00 69.42  ? 79   ASP A OD2 1 
ATOM   221   N  N   . LEU A  1 80  ? 2.987   22.865  6.174   1.00 35.97  ? 80   LEU A N   1 
ATOM   222   C  CA  . LEU A  1 80  ? 2.987   21.812  7.162   1.00 34.61  ? 80   LEU A CA  1 
ATOM   223   C  C   . LEU A  1 80  ? 3.436   22.360  8.502   1.00 35.52  ? 80   LEU A C   1 
ATOM   224   O  O   . LEU A  1 80  ? 4.542   22.881  8.633   1.00 41.09  ? 80   LEU A O   1 
ATOM   225   C  CB  . LEU A  1 80  ? 3.892   20.667  6.696   1.00 37.70  ? 80   LEU A CB  1 
ATOM   226   C  CG  . LEU A  1 80  ? 4.119   19.501  7.656   1.00 40.24  ? 80   LEU A CG  1 
ATOM   227   C  CD1 . LEU A  1 80  ? 2.786   18.883  8.113   1.00 34.46  ? 80   LEU A CD1 1 
ATOM   228   C  CD2 . LEU A  1 80  ? 5.043   18.454  6.998   1.00 36.18  ? 80   LEU A CD2 1 
ATOM   229   N  N   . PHE A  1 81  ? 2.557   22.277  9.489   1.00 33.21  ? 81   PHE A N   1 
ATOM   230   C  CA  . PHE A  1 81  ? 2.877   22.696  10.834  1.00 34.41  ? 81   PHE A CA  1 
ATOM   231   C  C   . PHE A  1 81  ? 2.792   21.484  11.753  1.00 39.18  ? 81   PHE A C   1 
ATOM   232   O  O   . PHE A  1 81  ? 1.819   20.729  11.694  1.00 37.81  ? 81   PHE A O   1 
ATOM   233   C  CB  . PHE A  1 81  ? 1.924   23.801  11.317  1.00 38.64  ? 81   PHE A CB  1 
ATOM   234   C  CG  . PHE A  1 81  ? 1.931   23.984  12.817  1.00 45.26  ? 81   PHE A CG  1 
ATOM   235   C  CD1 . PHE A  1 81  ? 2.891   24.791  13.429  1.00 42.60  ? 81   PHE A CD1 1 
ATOM   236   C  CD2 . PHE A  1 81  ? 0.995   23.324  13.626  1.00 44.30  ? 81   PHE A CD2 1 
ATOM   237   C  CE1 . PHE A  1 81  ? 2.910   24.954  14.825  1.00 46.22  ? 81   PHE A CE1 1 
ATOM   238   C  CE2 . PHE A  1 81  ? 1.004   23.475  15.018  1.00 40.52  ? 81   PHE A CE2 1 
ATOM   239   C  CZ  . PHE A  1 81  ? 1.971   24.295  15.618  1.00 44.21  ? 81   PHE A CZ  1 
ATOM   240   N  N   . VAL A  1 82  ? 3.805   21.317  12.604  1.00 39.54  ? 82   VAL A N   1 
ATOM   241   C  CA  . VAL A  1 82  ? 3.912   20.167  13.497  1.00 36.11  ? 82   VAL A CA  1 
ATOM   242   C  C   . VAL A  1 82  ? 4.257   20.648  14.891  1.00 36.32  ? 82   VAL A C   1 
ATOM   243   O  O   . VAL A  1 82  ? 5.168   21.459  15.060  1.00 43.10  ? 82   VAL A O   1 
ATOM   244   C  CB  . VAL A  1 82  ? 4.997   19.147  13.017  1.00 37.93  ? 82   VAL A CB  1 
ATOM   245   C  CG1 . VAL A  1 82  ? 5.043   17.921  13.936  1.00 32.02  ? 82   VAL A CG1 1 
ATOM   246   C  CG2 . VAL A  1 82  ? 4.744   18.710  11.581  1.00 28.15  ? 82   VAL A CG2 1 
ATOM   247   N  N   . HIS A  1 83  ? 3.528   20.154  15.890  1.00 39.78  ? 83   HIS A N   1 
ATOM   248   C  CA  . HIS A  1 83  ? 3.704   20.584  17.281  1.00 42.31  ? 83   HIS A CA  1 
ATOM   249   C  C   . HIS A  1 83  ? 3.902   19.348  18.154  1.00 44.79  ? 83   HIS A C   1 
ATOM   250   O  O   . HIS A  1 83  ? 2.950   18.808  18.706  1.00 45.07  ? 83   HIS A O   1 
ATOM   251   C  CB  . HIS A  1 83  ? 2.498   21.419  17.740  1.00 41.51  ? 83   HIS A CB  1 
ATOM   252   C  CG  . HIS A  1 83  ? 2.569   21.894  19.165  1.00 49.19  ? 83   HIS A CG  1 
ATOM   253   N  ND1 . HIS A  1 83  ? 1.521   22.549  19.783  1.00 48.77  ? 83   HIS A ND1 1 
ATOM   254   C  CD2 . HIS A  1 83  ? 3.553   21.812  20.093  1.00 49.26  ? 83   HIS A CD2 1 
ATOM   255   C  CE1 . HIS A  1 83  ? 1.858   22.851  21.024  1.00 44.33  ? 83   HIS A CE1 1 
ATOM   256   N  NE2 . HIS A  1 83  ? 3.085   22.414  21.238  1.00 46.21  ? 83   HIS A NE2 1 
ATOM   257   N  N   . PRO A  1 84  ? 5.148   18.869  18.251  1.00 48.06  ? 84   PRO A N   1 
ATOM   258   C  CA  . PRO A  1 84  ? 5.352   17.682  19.077  1.00 40.79  ? 84   PRO A CA  1 
ATOM   259   C  C   . PRO A  1 84  ? 5.613   18.049  20.524  1.00 44.73  ? 84   PRO A C   1 
ATOM   260   O  O   . PRO A  1 84  ? 6.187   19.112  20.791  1.00 45.08  ? 84   PRO A O   1 
ATOM   261   C  CB  . PRO A  1 84  ? 6.577   17.019  18.441  1.00 38.57  ? 84   PRO A CB  1 
ATOM   262   C  CG  . PRO A  1 84  ? 7.337   18.134  17.824  1.00 41.49  ? 84   PRO A CG  1 
ATOM   263   C  CD  . PRO A  1 84  ? 6.328   19.187  17.423  1.00 45.31  ? 84   PRO A CD  1 
ATOM   264   N  N   . ASN A  1 85  ? 5.171   17.194  21.444  1.00 39.35  ? 85   ASN A N   1 
ATOM   265   C  CA  . ASN A  1 85  ? 5.537   17.343  22.834  1.00 41.89  ? 85   ASN A CA  1 
ATOM   266   C  C   . ASN A  1 85  ? 6.362   16.138  23.237  1.00 41.24  ? 85   ASN A C   1 
ATOM   267   O  O   . ASN A  1 85  ? 5.929   15.000  23.093  1.00 45.12  ? 85   ASN A O   1 
ATOM   268   C  CB  . ASN A  1 85  ? 4.308   17.502  23.743  1.00 44.74  ? 85   ASN A CB  1 
ATOM   269   C  CG  . ASN A  1 85  ? 4.679   18.045  25.101  1.00 48.84  ? 85   ASN A CG  1 
ATOM   270   O  OD1 . ASN A  1 85  ? 5.260   17.328  25.916  1.00 52.26  ? 85   ASN A OD1 1 
ATOM   271   N  ND2 . ASN A  1 85  ? 4.365   19.324  25.354  1.00 50.04  ? 85   ASN A ND2 1 
ATOM   272   N  N   . LEU A  1 86  ? 7.562   16.389  23.732  1.00 42.52  ? 86   LEU A N   1 
ATOM   273   C  CA  . LEU A  1 86  ? 8.486   15.310  24.026  1.00 41.62  ? 86   LEU A CA  1 
ATOM   274   C  C   . LEU A  1 86  ? 8.392   14.889  25.493  1.00 53.04  ? 86   LEU A C   1 
ATOM   275   O  O   . LEU A  1 86  ? 9.189   14.077  25.966  1.00 56.36  ? 86   LEU A O   1 
ATOM   276   C  CB  . LEU A  1 86  ? 9.918   15.721  23.662  1.00 44.57  ? 86   LEU A CB  1 
ATOM   277   C  CG  . LEU A  1 86  ? 10.291  15.693  22.162  1.00 37.31  ? 86   LEU A CG  1 
ATOM   278   C  CD1 . LEU A  1 86  ? 9.551   16.737  21.377  1.00 32.23  ? 86   LEU A CD1 1 
ATOM   279   C  CD2 . LEU A  1 86  ? 11.795  15.846  21.949  1.00 31.81  ? 86   LEU A CD2 1 
ATOM   280   N  N   . THR A  1 87  ? 7.412   15.435  26.212  1.00 50.69  ? 87   THR A N   1 
ATOM   281   C  CA  . THR A  1 87  ? 7.087   14.947  27.547  1.00 48.67  ? 87   THR A CA  1 
ATOM   282   C  C   . THR A  1 87  ? 5.936   13.955  27.490  1.00 46.68  ? 87   THR A C   1 
ATOM   283   O  O   . THR A  1 87  ? 5.993   12.897  28.117  1.00 43.03  ? 87   THR A O   1 
ATOM   284   C  CB  . THR A  1 87  ? 6.701   16.078  28.502  1.00 52.41  ? 87   THR A CB  1 
ATOM   285   O  OG1 . THR A  1 87  ? 7.794   16.999  28.636  1.00 53.66  ? 87   THR A OG1 1 
ATOM   286   C  CG2 . THR A  1 87  ? 6.338   15.504  29.860  1.00 42.93  ? 87   THR A CG2 1 
ATOM   287   N  N   . SER A  1 88  ? 4.897   14.309  26.736  1.00 41.43  ? 88   SER A N   1 
ATOM   288   C  CA  . SER A  1 88  ? 3.756   13.428  26.524  1.00 41.02  ? 88   SER A CA  1 
ATOM   289   C  C   . SER A  1 88  ? 3.893   12.529  25.300  1.00 46.98  ? 88   SER A C   1 
ATOM   290   O  O   . SER A  1 88  ? 2.965   11.789  24.970  1.00 51.21  ? 88   SER A O   1 
ATOM   291   C  CB  . SER A  1 88  ? 2.481   14.242  26.394  1.00 43.91  ? 88   SER A CB  1 
ATOM   292   O  OG  . SER A  1 88  ? 2.712   15.380  25.594  1.00 54.59  ? 88   SER A OG  1 
ATOM   293   N  N   . LEU A  1 89  ? 5.038   12.613  24.620  1.00 51.55  ? 89   LEU A N   1 
ATOM   294   C  CA  . LEU A  1 89  ? 5.384   11.720  23.504  1.00 42.90  ? 89   LEU A CA  1 
ATOM   295   C  C   . LEU A  1 89  ? 4.266   11.615  22.464  1.00 38.00  ? 89   LEU A C   1 
ATOM   296   O  O   . LEU A  1 89  ? 3.941   10.549  21.961  1.00 40.18  ? 89   LEU A O   1 
ATOM   297   C  CB  . LEU A  1 89  ? 5.763   10.340  24.055  1.00 41.86  ? 89   LEU A CB  1 
ATOM   298   C  CG  . LEU A  1 89  ? 6.792   10.420  25.201  1.00 38.33  ? 89   LEU A CG  1 
ATOM   299   C  CD1 . LEU A  1 89  ? 7.219   9.061   25.655  1.00 37.92  ? 89   LEU A CD1 1 
ATOM   300   C  CD2 . LEU A  1 89  ? 8.026   11.242  24.814  1.00 37.63  ? 89   LEU A CD2 1 
ATOM   301   N  N   . ASP A  1 90  ? 3.692   12.759  22.130  1.00 43.21  ? 90   ASP A N   1 
ATOM   302   C  CA  . ASP A  1 90  ? 2.649   12.834  21.116  1.00 41.84  ? 90   ASP A CA  1 
ATOM   303   C  C   . ASP A  1 90  ? 2.846   14.075  20.239  1.00 43.46  ? 90   ASP A C   1 
ATOM   304   O  O   . ASP A  1 90  ? 3.745   14.893  20.487  1.00 39.50  ? 90   ASP A O   1 
ATOM   305   C  CB  . ASP A  1 90  ? 1.277   12.867  21.780  1.00 41.72  ? 90   ASP A CB  1 
ATOM   306   C  CG  . ASP A  1 90  ? 1.196   13.903  22.901  1.00 52.57  ? 90   ASP A CG  1 
ATOM   307   O  OD1 . ASP A  1 90  ? 1.723   15.033  22.736  1.00 48.48  ? 90   ASP A OD1 1 
ATOM   308   O  OD2 . ASP A  1 90  ? 0.624   13.578  23.962  1.00 56.20  ? 90   ASP A OD2 1 
ATOM   309   N  N   . PHE A  1 91  ? 2.005   14.226  19.225  1.00 35.60  ? 91   PHE A N   1 
ATOM   310   C  CA  . PHE A  1 91  ? 2.025   15.465  18.474  1.00 40.30  ? 91   PHE A CA  1 
ATOM   311   C  C   . PHE A  1 91  ? 0.657   15.816  17.919  1.00 39.28  ? 91   PHE A C   1 
ATOM   312   O  O   . PHE A  1 91  ? -0.169  14.944  17.628  1.00 41.56  ? 91   PHE A O   1 
ATOM   313   C  CB  . PHE A  1 91  ? 3.049   15.405  17.320  1.00 40.51  ? 91   PHE A CB  1 
ATOM   314   C  CG  . PHE A  1 91  ? 2.625   14.536  16.174  1.00 35.74  ? 91   PHE A CG  1 
ATOM   315   C  CD1 . PHE A  1 91  ? 2.946   13.180  16.159  1.00 35.55  ? 91   PHE A CD1 1 
ATOM   316   C  CD2 . PHE A  1 91  ? 1.896   15.069  15.106  1.00 34.07  ? 91   PHE A CD2 1 
ATOM   317   C  CE1 . PHE A  1 91  ? 2.543   12.359  15.094  1.00 32.73  ? 91   PHE A CE1 1 
ATOM   318   C  CE2 . PHE A  1 91  ? 1.494   14.261  14.039  1.00 38.15  ? 91   PHE A CE2 1 
ATOM   319   C  CZ  . PHE A  1 91  ? 1.830   12.894  14.036  1.00 35.62  ? 91   PHE A CZ  1 
ATOM   320   N  N   . VAL A  1 92  ? 0.477   17.118  17.760  1.00 34.22  ? 92   VAL A N   1 
ATOM   321   C  CA  . VAL A  1 92  ? -0.637  17.763  17.096  1.00 36.62  ? 92   VAL A CA  1 
ATOM   322   C  C   . VAL A  1 92  ? -0.068  18.418  15.825  1.00 40.78  ? 92   VAL A C   1 
ATOM   323   O  O   . VAL A  1 92  ? 1.049   18.938  15.845  1.00 38.90  ? 92   VAL A O   1 
ATOM   324   C  CB  . VAL A  1 92  ? -1.291  18.836  18.037  1.00 44.18  ? 92   VAL A CB  1 
ATOM   325   C  CG1 . VAL A  1 92  ? -2.031  19.869  17.267  1.00 42.83  ? 92   VAL A CG1 1 
ATOM   326   C  CG2 . VAL A  1 92  ? -2.195  18.183  19.107  1.00 35.48  ? 92   VAL A CG2 1 
ATOM   327   N  N   . ALA A  1 93  ? -0.817  18.398  14.723  1.00 41.78  ? 93   ALA A N   1 
ATOM   328   C  CA  . ALA A  1 93  ? -0.340  18.991  13.477  1.00 40.19  ? 93   ALA A CA  1 
ATOM   329   C  C   . ALA A  1 93  ? -1.468  19.502  12.585  1.00 43.04  ? 93   ALA A C   1 
ATOM   330   O  O   . ALA A  1 93  ? -2.646  19.237  12.820  1.00 45.16  ? 93   ALA A O   1 
ATOM   331   C  CB  . ALA A  1 93  ? 0.493   17.985  12.703  1.00 37.61  ? 93   ALA A CB  1 
ATOM   332   N  N   . SER A  1 94  ? -1.090  20.221  11.539  1.00 39.79  ? 94   SER A N   1 
ATOM   333   C  CA  . SER A  1 94  ? -2.059  20.663  10.549  1.00 47.59  ? 94   SER A CA  1 
ATOM   334   C  C   . SER A  1 94  ? -1.373  20.915  9.234   1.00 40.66  ? 94   SER A C   1 
ATOM   335   O  O   . SER A  1 94  ? -0.187  21.234  9.202   1.00 40.97  ? 94   SER A O   1 
ATOM   336   C  CB  . SER A  1 94  ? -2.769  21.938  10.999  1.00 47.29  ? 94   SER A CB  1 
ATOM   337   O  OG  . SER A  1 94  ? -1.860  23.016  10.992  1.00 46.83  ? 94   SER A OG  1 
ATOM   338   N  N   . GLU A  1 95  ? -2.116  20.794  8.145   1.00 39.43  ? 95   GLU A N   1 
ATOM   339   C  CA  . GLU A  1 95  ? -1.526  21.043  6.848   1.00 39.61  ? 95   GLU A CA  1 
ATOM   340   C  C   . GLU A  1 95  ? -2.504  21.726  5.918   1.00 41.27  ? 95   GLU A C   1 
ATOM   341   O  O   . GLU A  1 95  ? -3.709  21.631  6.094   1.00 48.27  ? 95   GLU A O   1 
ATOM   342   C  CB  . GLU A  1 95  ? -1.062  19.739  6.220   1.00 40.60  ? 95   GLU A CB  1 
ATOM   343   C  CG  . GLU A  1 95  ? -2.227  18.846  5.808   1.00 41.49  ? 95   GLU A CG  1 
ATOM   344   C  CD  . GLU A  1 95  ? -1.778  17.496  5.271   1.00 48.89  ? 95   GLU A CD  1 
ATOM   345   O  OE1 . GLU A  1 95  ? -0.611  17.404  4.834   1.00 42.56  ? 95   GLU A OE1 1 
ATOM   346   O  OE2 . GLU A  1 95  ? -2.593  16.535  5.280   1.00 51.13  ? 95   GLU A OE2 1 
ATOM   347   N  N   . LYS A  1 96  ? -1.963  22.385  4.909   1.00 41.05  ? 96   LYS A N   1 
ATOM   348   C  CA  . LYS A  1 96  ? -2.747  22.950  3.835   1.00 43.90  ? 96   LYS A CA  1 
ATOM   349   C  C   . LYS A  1 96  ? -2.074  22.525  2.536   1.00 42.31  ? 96   LYS A C   1 
ATOM   350   O  O   . LYS A  1 96  ? -0.899  22.807  2.331   1.00 41.71  ? 96   LYS A O   1 
ATOM   351   C  CB  . LYS A  1 96  ? -2.827  24.481  3.967   1.00 44.65  ? 96   LYS A CB  1 
ATOM   352   C  CG  . LYS A  1 96  ? -3.878  25.141  3.076   1.00 54.64  ? 96   LYS A CG  1 
ATOM   353   C  CD  . LYS A  1 96  ? -4.041  26.640  3.367   1.00 61.80  ? 96   LYS A CD  1 
ATOM   354   C  CE  . LYS A  1 96  ? -2.825  27.462  2.901   1.00 64.99  ? 96   LYS A CE  1 
ATOM   355   N  NZ  . LYS A  1 96  ? -2.905  28.927  3.244   1.00 81.04  ? 96   LYS A NZ  1 
ATOM   356   N  N   . ILE A  1 97  ? -2.794  21.827  1.664   1.00 41.82  ? 97   ILE A N   1 
ATOM   357   C  CA  . ILE A  1 97  ? -2.182  21.346  0.422   1.00 41.83  ? 97   ILE A CA  1 
ATOM   358   C  C   . ILE A  1 97  ? -2.743  22.037  -0.810  1.00 42.88  ? 97   ILE A C   1 
ATOM   359   O  O   . ILE A  1 97  ? -3.901  21.836  -1.176  1.00 46.44  ? 97   ILE A O   1 
ATOM   360   C  CB  . ILE A  1 97  ? -2.381  19.808  0.212   1.00 40.35  ? 97   ILE A CB  1 
ATOM   361   C  CG1 . ILE A  1 97  ? -2.093  19.017  1.483   1.00 31.42  ? 97   ILE A CG1 1 
ATOM   362   C  CG2 . ILE A  1 97  ? -1.540  19.295  -0.951  1.00 27.89  ? 97   ILE A CG2 1 
ATOM   363   C  CD1 . ILE A  1 97  ? -2.472  17.562  1.332   1.00 36.88  ? 97   ILE A CD1 1 
ATOM   364   N  N   . GLU A  1 98  ? -1.921  22.819  -1.485  1.00 44.51  ? 98   GLU A N   1 
ATOM   365   C  CA  . GLU A  1 98  ? -2.367  23.394  -2.736  1.00 45.51  ? 98   GLU A CA  1 
ATOM   366   C  C   . GLU A  1 98  ? -2.347  22.305  -3.806  1.00 38.93  ? 98   GLU A C   1 
ATOM   367   O  O   . GLU A  1 98  ? -1.301  21.776  -4.140  1.00 38.16  ? 98   GLU A O   1 
ATOM   368   C  CB  . GLU A  1 98  ? -1.502  24.584  -3.144  1.00 41.77  ? 98   GLU A CB  1 
ATOM   369   C  CG  . GLU A  1 98  ? -1.998  25.266  -4.407  1.00 44.86  ? 98   GLU A CG  1 
ATOM   370   C  CD  . GLU A  1 98  ? -1.102  26.398  -4.823  1.00 52.56  ? 98   GLU A CD  1 
ATOM   371   O  OE1 . GLU A  1 98  ? -0.522  27.043  -3.932  1.00 56.38  ? 98   GLU A OE1 1 
ATOM   372   O  OE2 . GLU A  1 98  ? -0.958  26.633  -6.036  1.00 59.36  ? 98   GLU A OE2 1 
ATOM   373   N  N   . VAL A  1 99  ? -3.530  21.983  -4.317  1.00 41.21  ? 99   VAL A N   1 
ATOM   374   C  CA  . VAL A  1 99  ? -3.711  20.988  -5.362  1.00 42.21  ? 99   VAL A CA  1 
ATOM   375   C  C   . VAL A  1 99  ? -4.229  21.630  -6.647  1.00 49.25  ? 99   VAL A C   1 
ATOM   376   O  O   . VAL A  1 99  ? -4.963  22.623  -6.624  1.00 42.37  ? 99   VAL A O   1 
ATOM   377   C  CB  . VAL A  1 99  ? -4.707  19.881  -4.938  1.00 36.77  ? 99   VAL A CB  1 
ATOM   378   C  CG1 . VAL A  1 99  ? -4.146  19.053  -3.788  1.00 39.04  ? 99   VAL A CG1 1 
ATOM   379   C  CG2 . VAL A  1 99  ? -6.020  20.488  -4.532  1.00 38.18  ? 99   VAL A CG2 1 
ATOM   380   N  N   . LEU A  1 100 ? -3.825  21.052  -7.770  1.00 47.56  ? 100  LEU A N   1 
ATOM   381   C  CA  . LEU A  1 100 ? -4.394  21.375  -9.063  1.00 45.78  ? 100  LEU A CA  1 
ATOM   382   C  C   . LEU A  1 100 ? -5.303  20.224  -9.471  1.00 52.66  ? 100  LEU A C   1 
ATOM   383   O  O   . LEU A  1 100 ? -4.939  19.065  -9.320  1.00 54.15  ? 100  LEU A O   1 
ATOM   384   C  CB  . LEU A  1 100 ? -3.299  21.588  -10.091 1.00 50.81  ? 100  LEU A CB  1 
ATOM   385   C  CG  . LEU A  1 100 ? -3.724  21.755  -11.541 1.00 54.11  ? 100  LEU A CG  1 
ATOM   386   C  CD1 . LEU A  1 100 ? -4.658  22.931  -11.639 1.00 52.92  ? 100  LEU A CD1 1 
ATOM   387   C  CD2 . LEU A  1 100 ? -2.501  21.978  -12.406 1.00 40.99  ? 100  LEU A CD2 1 
ATOM   388   N  N   . VAL A  1 101 ? -6.493  20.529  -9.965  1.00 55.73  ? 101  VAL A N   1 
ATOM   389   C  CA  . VAL A  1 101 ? -7.425  19.479  -10.346 1.00 51.64  ? 101  VAL A CA  1 
ATOM   390   C  C   . VAL A  1 101 ? -7.477  19.370  -11.864 1.00 53.28  ? 101  VAL A C   1 
ATOM   391   O  O   . VAL A  1 101 ? -7.842  20.315  -12.556 1.00 54.71  ? 101  VAL A O   1 
ATOM   392   C  CB  . VAL A  1 101 ? -8.818  19.731  -9.763  1.00 50.81  ? 101  VAL A CB  1 
ATOM   393   C  CG1 . VAL A  1 101 ? -9.811  18.774  -10.348 1.00 53.05  ? 101  VAL A CG1 1 
ATOM   394   C  CG2 . VAL A  1 101 ? -8.777  19.574  -8.251  1.00 50.93  ? 101  VAL A CG2 1 
ATOM   395   N  N   . SER A  1 102 ? -7.081  18.211  -12.376 1.00 56.14  ? 102  SER A N   1 
ATOM   396   C  CA  . SER A  1 102 ? -6.906  18.025  -13.811 1.00 60.95  ? 102  SER A CA  1 
ATOM   397   C  C   . SER A  1 102 ? -8.189  17.593  -14.490 1.00 61.69  ? 102  SER A C   1 
ATOM   398   O  O   . SER A  1 102 ? -8.487  18.019  -15.599 1.00 65.10  ? 102  SER A O   1 
ATOM   399   C  CB  . SER A  1 102 ? -5.811  16.993  -14.081 1.00 62.78  ? 102  SER A CB  1 
ATOM   400   O  OG  . SER A  1 102 ? -4.586  17.419  -13.518 1.00 63.21  ? 102  SER A OG  1 
ATOM   401   N  N   . ASN A  1 103 ? -8.934  16.727  -13.819 1.00 59.90  ? 103  ASN A N   1 
ATOM   402   C  CA  . ASN A  1 103 ? -10.202 16.238  -14.332 1.00 62.72  ? 103  ASN A CA  1 
ATOM   403   C  C   . ASN A  1 103 ? -11.244 16.407  -13.246 1.00 60.00  ? 103  ASN A C   1 
ATOM   404   O  O   . ASN A  1 103 ? -10.918 16.381  -12.063 1.00 59.52  ? 103  ASN A O   1 
ATOM   405   C  CB  . ASN A  1 103 ? -10.092 14.771  -14.775 1.00 68.50  ? 103  ASN A CB  1 
ATOM   406   C  CG  . ASN A  1 103 ? -10.347 14.592  -16.264 1.00 88.35  ? 103  ASN A CG  1 
ATOM   407   O  OD1 . ASN A  1 103 ? -11.496 14.652  -16.720 1.00 90.48  ? 103  ASN A OD1 1 
ATOM   408   N  ND2 . ASN A  1 103 ? -9.285  14.369  -17.033 1.00 87.03  ? 103  ASN A ND2 1 
ATOM   409   N  N   . ALA A  1 104 ? -12.492 16.605  -13.633 1.00 58.98  ? 104  ALA A N   1 
ATOM   410   C  CA  . ALA A  1 104 ? -13.540 16.816  -12.641 1.00 59.89  ? 104  ALA A CA  1 
ATOM   411   C  C   . ALA A  1 104 ? -13.619 15.629  -11.680 1.00 57.39  ? 104  ALA A C   1 
ATOM   412   O  O   . ALA A  1 104 ? -13.557 14.490  -12.116 1.00 62.60  ? 104  ALA A O   1 
ATOM   413   C  CB  . ALA A  1 104 ? -14.881 17.045  -13.333 1.00 52.39  ? 104  ALA A CB  1 
ATOM   414   N  N   . THR A  1 105 ? -13.729 15.887  -10.381 1.00 53.59  ? 105  THR A N   1 
ATOM   415   C  CA  . THR A  1 105 ? -13.886 14.798  -9.420  1.00 56.64  ? 105  THR A CA  1 
ATOM   416   C  C   . THR A  1 105 ? -14.808 15.159  -8.287  1.00 59.17  ? 105  THR A C   1 
ATOM   417   O  O   . THR A  1 105 ? -14.995 16.333  -7.978  1.00 62.64  ? 105  THR A O   1 
ATOM   418   C  CB  . THR A  1 105 ? -12.546 14.355  -8.758  1.00 62.73  ? 105  THR A CB  1 
ATOM   419   O  OG1 . THR A  1 105 ? -11.575 15.406  -8.850  1.00 60.67  ? 105  THR A OG1 1 
ATOM   420   C  CG2 . THR A  1 105 ? -12.010 13.063  -9.369  1.00 59.25  ? 105  THR A CG2 1 
ATOM   421   N  N   . GLN A  1 106 ? -15.330 14.121  -7.644  1.00 57.86  ? 106  GLN A N   1 
ATOM   422   C  CA  . GLN A  1 106 ? -16.164 14.240  -6.466  1.00 56.30  ? 106  GLN A CA  1 
ATOM   423   C  C   . GLN A  1 106 ? -15.340 13.945  -5.222  1.00 58.08  ? 106  GLN A C   1 
ATOM   424   O  O   . GLN A  1 106 ? -15.764 14.217  -4.086  1.00 55.02  ? 106  GLN A O   1 
ATOM   425   C  CB  . GLN A  1 106 ? -17.338 13.265  -6.550  1.00 60.37  ? 106  GLN A CB  1 
ATOM   426   C  CG  . GLN A  1 106 ? -18.574 13.725  -5.819  1.00 72.84  ? 106  GLN A CG  1 
ATOM   427   C  CD  . GLN A  1 106 ? -19.453 14.605  -6.684  1.00 77.30  ? 106  GLN A CD  1 
ATOM   428   O  OE1 . GLN A  1 106 ? -19.827 14.220  -7.796  1.00 82.15  ? 106  GLN A OE1 1 
ATOM   429   N  NE2 . GLN A  1 106 ? -19.790 15.792  -6.181  1.00 74.14  ? 106  GLN A NE2 1 
ATOM   430   N  N   . PHE A  1 107 ? -14.164 13.362  -5.437  1.00 60.46  ? 107  PHE A N   1 
ATOM   431   C  CA  . PHE A  1 107 ? -13.343 12.892  -4.317  1.00 58.37  ? 107  PHE A CA  1 
ATOM   432   C  C   . PHE A  1 107 ? -11.856 13.150  -4.513  1.00 54.93  ? 107  PHE A C   1 
ATOM   433   O  O   . PHE A  1 107 ? -11.355 13.288  -5.635  1.00 56.34  ? 107  PHE A O   1 
ATOM   434   C  CB  . PHE A  1 107 ? -13.575 11.392  -4.069  1.00 58.78  ? 107  PHE A CB  1 
ATOM   435   C  CG  . PHE A  1 107 ? -13.528 10.547  -5.318  1.00 56.86  ? 107  PHE A CG  1 
ATOM   436   C  CD1 . PHE A  1 107 ? -14.680 10.315  -6.058  1.00 53.67  ? 107  PHE A CD1 1 
ATOM   437   C  CD2 . PHE A  1 107 ? -12.333 9.975   -5.746  1.00 56.43  ? 107  PHE A CD2 1 
ATOM   438   C  CE1 . PHE A  1 107 ? -14.647 9.536   -7.213  1.00 57.04  ? 107  PHE A CE1 1 
ATOM   439   C  CE2 . PHE A  1 107 ? -12.292 9.191   -6.898  1.00 55.99  ? 107  PHE A CE2 1 
ATOM   440   C  CZ  . PHE A  1 107 ? -13.457 8.972   -7.635  1.00 52.72  ? 107  PHE A CZ  1 
ATOM   441   N  N   . ILE A  1 108 ? -11.163 13.237  -3.391  1.00 53.52  ? 108  ILE A N   1 
ATOM   442   C  CA  . ILE A  1 108 ? -9.719  13.343  -3.380  1.00 53.11  ? 108  ILE A CA  1 
ATOM   443   C  C   . ILE A  1 108 ? -9.200  12.123  -2.645  1.00 51.30  ? 108  ILE A C   1 
ATOM   444   O  O   . ILE A  1 108 ? -9.630  11.842  -1.524  1.00 47.19  ? 108  ILE A O   1 
ATOM   445   C  CB  . ILE A  1 108 ? -9.232  14.627  -2.687  1.00 52.51  ? 108  ILE A CB  1 
ATOM   446   C  CG1 . ILE A  1 108 ? -9.989  15.851  -3.217  1.00 48.88  ? 108  ILE A CG1 1 
ATOM   447   C  CG2 . ILE A  1 108 ? -7.732  14.780  -2.870  1.00 45.43  ? 108  ILE A CG2 1 
ATOM   448   C  CD1 . ILE A  1 108 ? -9.498  17.183  -2.647  1.00 39.80  ? 108  ILE A CD1 1 
ATOM   449   N  N   . ILE A  1 109 ? -8.315  11.366  -3.285  1.00 51.03  ? 109  ILE A N   1 
ATOM   450   C  CA  . ILE A  1 109 ? -7.705  10.233  -2.610  1.00 51.15  ? 109  ILE A CA  1 
ATOM   451   C  C   . ILE A  1 109 ? -6.265  10.559  -2.244  1.00 47.63  ? 109  ILE A C   1 
ATOM   452   O  O   . ILE A  1 109 ? -5.486  10.975  -3.098  1.00 51.31  ? 109  ILE A O   1 
ATOM   453   C  CB  . ILE A  1 109 ? -7.734  8.966   -3.479  1.00 50.31  ? 109  ILE A CB  1 
ATOM   454   C  CG1 . ILE A  1 109 ? -9.149  8.682   -3.981  1.00 44.49  ? 109  ILE A CG1 1 
ATOM   455   C  CG2 . ILE A  1 109 ? -7.217  7.787   -2.684  1.00 48.37  ? 109  ILE A CG2 1 
ATOM   456   C  CD1 . ILE A  1 109 ? -10.090 8.230   -2.912  1.00 45.15  ? 109  ILE A CD1 1 
ATOM   457   N  N   . LEU A  1 110 ? -5.909  10.381  -0.980  1.00 42.14  ? 110  LEU A N   1 
ATOM   458   C  CA  . LEU A  1 110 ? -4.500  10.455  -0.612  1.00 46.31  ? 110  LEU A CA  1 
ATOM   459   C  C   . LEU A  1 110 ? -4.137  9.458   0.515   1.00 51.29  ? 110  LEU A C   1 
ATOM   460   O  O   . LEU A  1 110 ? -4.998  8.734   1.036   1.00 50.78  ? 110  LEU A O   1 
ATOM   461   C  CB  . LEU A  1 110 ? -4.121  11.902  -0.234  1.00 51.83  ? 110  LEU A CB  1 
ATOM   462   C  CG  . LEU A  1 110 ? -4.759  12.740  0.881   1.00 42.14  ? 110  LEU A CG  1 
ATOM   463   C  CD1 . LEU A  1 110 ? -4.486  12.118  2.176   1.00 50.43  ? 110  LEU A CD1 1 
ATOM   464   C  CD2 . LEU A  1 110 ? -4.179  14.142  0.928   1.00 44.98  ? 110  LEU A CD2 1 
ATOM   465   N  N   . HIS A  1 111 ? -2.861  9.412   0.885   1.00 44.12  ? 111  HIS A N   1 
ATOM   466   C  CA  . HIS A  1 111 ? -2.416  8.454   1.887   1.00 39.30  ? 111  HIS A CA  1 
ATOM   467   C  C   . HIS A  1 111 ? -2.503  8.994   3.297   1.00 40.68  ? 111  HIS A C   1 
ATOM   468   O  O   . HIS A  1 111 ? -2.305  10.183  3.530   1.00 42.28  ? 111  HIS A O   1 
ATOM   469   C  CB  . HIS A  1 111 ? -0.989  8.018   1.617   1.00 34.68  ? 111  HIS A CB  1 
ATOM   470   C  CG  . HIS A  1 111 ? -0.853  7.132   0.431   1.00 36.65  ? 111  HIS A CG  1 
ATOM   471   N  ND1 . HIS A  1 111 ? -0.303  7.565   -0.756  1.00 37.40  ? 111  HIS A ND1 1 
ATOM   472   C  CD2 . HIS A  1 111 ? -1.212  5.841   0.237   1.00 33.58  ? 111  HIS A CD2 1 
ATOM   473   C  CE1 . HIS A  1 111 ? -0.313  6.572   -1.628  1.00 42.10  ? 111  HIS A CE1 1 
ATOM   474   N  NE2 . HIS A  1 111 ? -0.862  5.515   -1.051  1.00 40.59  ? 111  HIS A NE2 1 
ATOM   475   N  N   . SER A  1 112 ? -2.783  8.099   4.235   1.00 38.02  ? 112  SER A N   1 
ATOM   476   C  CA  . SER A  1 112 ? -2.782  8.449   5.638   1.00 36.66  ? 112  SER A CA  1 
ATOM   477   C  C   . SER A  1 112 ? -2.822  7.156   6.431   1.00 37.90  ? 112  SER A C   1 
ATOM   478   O  O   . SER A  1 112 ? -3.625  6.281   6.148   1.00 42.85  ? 112  SER A O   1 
ATOM   479   C  CB  . SER A  1 112 ? -3.967  9.355   5.978   1.00 34.06  ? 112  SER A CB  1 
ATOM   480   O  OG  . SER A  1 112 ? -3.897  9.780   7.322   1.00 42.75  ? 112  SER A OG  1 
ATOM   481   N  N   . LYS A  1 113 ? -1.942  7.015   7.407   1.00 39.10  ? 113  LYS A N   1 
ATOM   482   C  CA  . LYS A  1 113 ? -1.911  5.787   8.187   1.00 45.29  ? 113  LYS A CA  1 
ATOM   483   C  C   . LYS A  1 113 ? -1.595  6.075   9.642   1.00 45.60  ? 113  LYS A C   1 
ATOM   484   O  O   . LYS A  1 113 ? -0.654  6.809   9.936   1.00 44.90  ? 113  LYS A O   1 
ATOM   485   C  CB  . LYS A  1 113 ? -0.891  4.805   7.606   1.00 44.78  ? 113  LYS A CB  1 
ATOM   486   C  CG  . LYS A  1 113 ? -0.689  3.559   8.439   1.00 48.23  ? 113  LYS A CG  1 
ATOM   487   C  CD  . LYS A  1 113 ? 0.604   2.848   8.069   1.00 56.06  ? 113  LYS A CD  1 
ATOM   488   C  CE  . LYS A  1 113 ? 0.723   1.506   8.787   1.00 56.60  ? 113  LYS A CE  1 
ATOM   489   N  NZ  . LYS A  1 113 ? 0.210   0.397   7.930   1.00 51.73  ? 113  LYS A NZ  1 
ATOM   490   N  N   . ASP A  1 114 ? -2.402  5.509   10.539  1.00 42.72  ? 114  ASP A N   1 
ATOM   491   C  CA  . ASP A  1 114 ? -2.232  5.678   11.981  1.00 46.12  ? 114  ASP A CA  1 
ATOM   492   C  C   . ASP A  1 114 ? -2.384  7.124   12.431  1.00 47.27  ? 114  ASP A C   1 
ATOM   493   O  O   . ASP A  1 114 ? -1.965  7.489   13.528  1.00 46.03  ? 114  ASP A O   1 
ATOM   494   C  CB  . ASP A  1 114 ? -0.869  5.145   12.420  1.00 54.42  ? 114  ASP A CB  1 
ATOM   495   C  CG  . ASP A  1 114 ? -0.791  3.641   12.341  1.00 54.84  ? 114  ASP A CG  1 
ATOM   496   O  OD1 . ASP A  1 114 ? -1.832  3.003   12.585  1.00 58.43  ? 114  ASP A OD1 1 
ATOM   497   O  OD2 . ASP A  1 114 ? 0.296   3.099   12.040  1.00 61.43  ? 114  ASP A OD2 1 
ATOM   498   N  N   . LEU A  1 115 ? -2.991  7.946   11.586  1.00 46.88  ? 115  LEU A N   1 
ATOM   499   C  CA  . LEU A  1 115 ? -3.248  9.336   11.942  1.00 51.12  ? 115  LEU A CA  1 
ATOM   500   C  C   . LEU A  1 115 ? -4.730  9.579   12.185  1.00 51.93  ? 115  LEU A C   1 
ATOM   501   O  O   . LEU A  1 115 ? -5.581  9.158   11.387  1.00 45.87  ? 115  LEU A O   1 
ATOM   502   C  CB  . LEU A  1 115 ? -2.736  10.276  10.848  1.00 46.72  ? 115  LEU A CB  1 
ATOM   503   C  CG  . LEU A  1 115 ? -1.220  10.344  10.801  1.00 37.99  ? 115  LEU A CG  1 
ATOM   504   C  CD1 . LEU A  1 115 ? -0.761  11.023  9.535   1.00 40.88  ? 115  LEU A CD1 1 
ATOM   505   C  CD2 . LEU A  1 115 ? -0.741  11.084  12.041  1.00 46.15  ? 115  LEU A CD2 1 
ATOM   506   N  N   . GLU A  1 116 ? -5.026  10.243  13.300  1.00 44.85  ? 116  GLU A N   1 
ATOM   507   C  CA  . GLU A  1 116 ? -6.380  10.655  13.602  1.00 44.52  ? 116  GLU A CA  1 
ATOM   508   C  C   . GLU A  1 116 ? -6.642  12.034  13.013  1.00 52.73  ? 116  GLU A C   1 
ATOM   509   O  O   . GLU A  1 116 ? -6.196  13.051  13.562  1.00 49.00  ? 116  GLU A O   1 
ATOM   510   C  CB  . GLU A  1 116 ? -6.612  10.670  15.105  1.00 48.43  ? 116  GLU A CB  1 
ATOM   511   C  CG  . GLU A  1 116 ? -7.996  11.180  15.502  1.00 63.57  ? 116  GLU A CG  1 
ATOM   512   C  CD  . GLU A  1 116 ? -8.202  11.272  17.014  1.00 69.19  ? 116  GLU A CD  1 
ATOM   513   O  OE1 . GLU A  1 116 ? -7.295  10.851  17.770  1.00 67.65  ? 116  GLU A OE1 1 
ATOM   514   O  OE2 . GLU A  1 116 ? -9.273  11.770  17.441  1.00 65.88  ? 116  GLU A OE2 1 
ATOM   515   N  N   . ILE A  1 117 ? -7.356  12.054  11.888  1.00 48.44  ? 117  ILE A N   1 
ATOM   516   C  CA  . ILE A  1 117 ? -7.760  13.288  11.222  1.00 46.34  ? 117  ILE A CA  1 
ATOM   517   C  C   . ILE A  1 117 ? -9.019  13.849  11.852  1.00 49.86  ? 117  ILE A C   1 
ATOM   518   O  O   . ILE A  1 117 ? -10.018 13.156  11.964  1.00 60.37  ? 117  ILE A O   1 
ATOM   519   C  CB  . ILE A  1 117 ? -7.990  13.045  9.731   1.00 47.61  ? 117  ILE A CB  1 
ATOM   520   C  CG1 . ILE A  1 117 ? -6.694  12.542  9.105   1.00 44.67  ? 117  ILE A CG1 1 
ATOM   521   C  CG2 . ILE A  1 117 ? -8.465  14.299  9.031   1.00 47.05  ? 117  ILE A CG2 1 
ATOM   522   C  CD1 . ILE A  1 117 ? -6.900  11.530  8.045   1.00 47.22  ? 117  ILE A CD1 1 
ATOM   523   N  N   . THR A  1 118 ? -8.966  15.114  12.253  1.00 58.81  ? 118  THR A N   1 
ATOM   524   C  CA  . THR A  1 118 ? -9.994  15.711  13.104  1.00 57.41  ? 118  THR A CA  1 
ATOM   525   C  C   . THR A  1 118 ? -10.738 16.885  12.467  1.00 62.36  ? 118  THR A C   1 
ATOM   526   O  O   . THR A  1 118 ? -11.798 17.288  12.943  1.00 68.79  ? 118  THR A O   1 
ATOM   527   C  CB  . THR A  1 118 ? -9.377  16.204  14.424  1.00 61.02  ? 118  THR A CB  1 
ATOM   528   O  OG1 . THR A  1 118 ? -8.816  17.511  14.234  1.00 60.06  ? 118  THR A OG1 1 
ATOM   529   C  CG2 . THR A  1 118 ? -8.288  15.248  14.886  1.00 56.90  ? 118  THR A CG2 1 
ATOM   530   N  N   . ASN A  1 119 ? -10.185 17.425  11.390  1.00 59.53  ? 119  ASN A N   1 
ATOM   531   C  CA  . ASN A  1 119 ? -10.723 18.618  10.755  1.00 58.89  ? 119  ASN A CA  1 
ATOM   532   C  C   . ASN A  1 119 ? -10.349 18.588  9.287   1.00 59.38  ? 119  ASN A C   1 
ATOM   533   O  O   . ASN A  1 119 ? -9.189  18.352  8.964   1.00 58.65  ? 119  ASN A O   1 
ATOM   534   C  CB  . ASN A  1 119 ? -10.139 19.858  11.420  1.00 69.46  ? 119  ASN A CB  1 
ATOM   535   C  CG  . ASN A  1 119 ? -11.171 20.920  11.755  1.00 84.65  ? 119  ASN A CG  1 
ATOM   536   O  OD1 . ASN A  1 119 ? -12.234 21.018  11.137  1.00 87.46  ? 119  ASN A OD1 1 
ATOM   537   N  ND2 . ASN A  1 119 ? -10.827 21.741  12.756  1.00 92.80  ? 119  ASN A ND2 1 
ATOM   538   N  N   . ALA A  1 120 ? -11.289 18.829  8.385   1.00 53.31  ? 120  ALA A N   1 
ATOM   539   C  CA  . ALA A  1 120 ? -10.920 18.825  6.974   1.00 51.69  ? 120  ALA A CA  1 
ATOM   540   C  C   . ALA A  1 120 ? -11.772 19.793  6.162   1.00 54.54  ? 120  ALA A C   1 
ATOM   541   O  O   . ALA A  1 120 ? -12.996 19.760  6.240   1.00 59.71  ? 120  ALA A O   1 
ATOM   542   C  CB  . ALA A  1 120 ? -11.021 17.414  6.400   1.00 47.27  ? 120  ALA A CB  1 
ATOM   543   N  N   . THR A  1 121 ? -11.120 20.654  5.382   1.00 47.64  ? 121  THR A N   1 
ATOM   544   C  CA  . THR A  1 121 ? -11.819 21.706  4.648   1.00 50.81  ? 121  THR A CA  1 
ATOM   545   C  C   . THR A  1 121 ? -11.210 21.930  3.281   1.00 55.26  ? 121  THR A C   1 
ATOM   546   O  O   . THR A  1 121 ? -10.002 21.779  3.082   1.00 57.66  ? 121  THR A O   1 
ATOM   547   C  CB  . THR A  1 121 ? -11.807 23.071  5.392   1.00 55.66  ? 121  THR A CB  1 
ATOM   548   O  OG1 . THR A  1 121 ? -10.465 23.568  5.463   1.00 65.00  ? 121  THR A OG1 1 
ATOM   549   C  CG2 . THR A  1 121 ? -12.384 22.972  6.800   1.00 41.22  ? 121  THR A CG2 1 
ATOM   550   N  N   . LEU A  1 122 ? -12.058 22.284  2.327   1.00 55.08  ? 122  LEU A N   1 
ATOM   551   C  CA  . LEU A  1 122 ? -11.580 22.652  1.014   1.00 53.69  ? 122  LEU A CA  1 
ATOM   552   C  C   . LEU A  1 122 ? -11.785 24.147  0.829   1.00 50.21  ? 122  LEU A C   1 
ATOM   553   O  O   . LEU A  1 122 ? -12.819 24.671  1.208   1.00 46.54  ? 122  LEU A O   1 
ATOM   554   C  CB  . LEU A  1 122 ? -12.302 21.860  -0.075  1.00 51.74  ? 122  LEU A CB  1 
ATOM   555   C  CG  . LEU A  1 122 ? -11.635 22.055  -1.430  1.00 50.83  ? 122  LEU A CG  1 
ATOM   556   C  CD1 . LEU A  1 122 ? -10.216 21.541  -1.324  1.00 45.47  ? 122  LEU A CD1 1 
ATOM   557   C  CD2 . LEU A  1 122 ? -12.394 21.350  -2.533  1.00 50.34  ? 122  LEU A CD2 1 
ATOM   558   N  N   . GLN A  1 123 ? -10.781 24.824  0.281   1.00 52.44  ? 123  GLN A N   1 
ATOM   559   C  CA  . GLN A  1 123 ? -10.878 26.239  -0.074  1.00 49.91  ? 123  GLN A CA  1 
ATOM   560   C  C   . GLN A  1 123 ? -10.369 26.483  -1.490  1.00 50.01  ? 123  GLN A C   1 
ATOM   561   O  O   . GLN A  1 123 ? -9.660  25.642  -2.055  1.00 45.53  ? 123  GLN A O   1 
ATOM   562   C  CB  . GLN A  1 123 ? -10.091 27.109  0.909   1.00 52.29  ? 123  GLN A CB  1 
ATOM   563   C  CG  . GLN A  1 123 ? -10.654 27.120  2.326   1.00 58.31  ? 123  GLN A CG  1 
ATOM   564   C  CD  . GLN A  1 123 ? -10.169 28.309  3.146   1.00 49.57  ? 123  GLN A CD  1 
ATOM   565   O  OE1 . GLN A  1 123 ? -9.706  29.303  2.606   1.00 49.35  ? 123  GLN A OE1 1 
ATOM   566   N  NE2 . GLN A  1 123 ? -10.274 28.198  4.456   1.00 51.67  ? 123  GLN A NE2 1 
ATOM   567   N  N   . SER A  1 124 ? -10.726 27.634  -2.065  1.00 52.71  ? 124  SER A N   1 
ATOM   568   C  CA  . SER A  1 124 ? -10.201 28.020  -3.377  1.00 49.19  ? 124  SER A CA  1 
ATOM   569   C  C   . SER A  1 124 ? -10.353 29.498  -3.651  1.00 53.88  ? 124  SER A C   1 
ATOM   570   O  O   . SER A  1 124 ? -11.344 30.126  -3.272  1.00 52.60  ? 124  SER A O   1 
ATOM   571   C  CB  . SER A  1 124 ? -10.884 27.238  -4.508  1.00 48.67  ? 124  SER A CB  1 
ATOM   572   O  OG  . SER A  1 124 ? -10.299 27.545  -5.766  1.00 39.66  ? 124  SER A OG  1 
ATOM   573   N  N   . GLU A  1 125 ? -9.359  30.038  -4.346  1.00 57.87  ? 125  GLU A N   1 
ATOM   574   C  CA  . GLU A  1 125 ? -9.371  31.427  -4.763  1.00 54.20  ? 125  GLU A CA  1 
ATOM   575   C  C   . GLU A  1 125 ? -9.743  31.533  -6.234  1.00 54.78  ? 125  GLU A C   1 
ATOM   576   O  O   . GLU A  1 125 ? -9.908  32.642  -6.756  1.00 59.65  ? 125  GLU A O   1 
ATOM   577   C  CB  . GLU A  1 125 ? -8.010  32.076  -4.517  1.00 52.55  ? 125  GLU A CB  1 
ATOM   578   C  CG  . GLU A  1 125 ? -7.612  32.138  -3.057  1.00 55.64  ? 125  GLU A CG  1 
ATOM   579   C  CD  . GLU A  1 125 ? -6.197  32.639  -2.878  1.00 68.16  ? 125  GLU A CD  1 
ATOM   580   O  OE1 . GLU A  1 125 ? -5.582  33.045  -3.897  1.00 61.06  ? 125  GLU A OE1 1 
ATOM   581   O  OE2 . GLU A  1 125 ? -5.700  32.620  -1.725  1.00 66.76  ? 125  GLU A OE2 1 
ATOM   582   N  N   . GLU A  1 126 ? -9.869  30.383  -6.893  1.00 46.31  ? 126  GLU A N   1 
ATOM   583   C  CA  . GLU A  1 126 ? -10.228 30.341  -8.303  1.00 49.96  ? 126  GLU A CA  1 
ATOM   584   C  C   . GLU A  1 126 ? -11.662 29.852  -8.460  1.00 52.84  ? 126  GLU A C   1 
ATOM   585   O  O   . GLU A  1 126 ? -12.334 30.148  -9.446  1.00 59.01  ? 126  GLU A O   1 
ATOM   586   C  CB  . GLU A  1 126 ? -9.263  29.442  -9.085  1.00 52.91  ? 126  GLU A CB  1 
ATOM   587   C  CG  . GLU A  1 126 ? -7.794  29.775  -8.869  1.00 48.88  ? 126  GLU A CG  1 
ATOM   588   C  CD  . GLU A  1 126 ? -6.858  29.056  -9.835  1.00 55.62  ? 126  GLU A CD  1 
ATOM   589   O  OE1 . GLU A  1 126 ? -7.236  27.998  -10.381 1.00 60.12  ? 126  GLU A OE1 1 
ATOM   590   O  OE2 . GLU A  1 126 ? -5.728  29.547  -10.049 1.00 59.40  ? 126  GLU A OE2 1 
ATOM   591   N  N   . ASP A  1 127 ? -12.126 29.111  -7.466  1.00 53.27  ? 127  ASP A N   1 
ATOM   592   C  CA  . ASP A  1 127 ? -13.455 28.512  -7.480  1.00 54.89  ? 127  ASP A CA  1 
ATOM   593   C  C   . ASP A  1 127 ? -14.296 29.067  -6.330  1.00 58.40  ? 127  ASP A C   1 
ATOM   594   O  O   . ASP A  1 127 ? -14.246 28.550  -5.210  1.00 55.34  ? 127  ASP A O   1 
ATOM   595   C  CB  . ASP A  1 127 ? -13.326 26.992  -7.376  1.00 53.00  ? 127  ASP A CB  1 
ATOM   596   C  CG  . ASP A  1 127 ? -14.658 26.273  -7.461  1.00 58.56  ? 127  ASP A CG  1 
ATOM   597   O  OD1 . ASP A  1 127 ? -15.595 26.630  -6.728  1.00 57.20  ? 127  ASP A OD1 1 
ATOM   598   O  OD2 . ASP A  1 127 ? -14.764 25.323  -8.264  1.00 61.53  ? 127  ASP A OD2 1 
ATOM   599   N  N   . SER A  1 128 ? -15.084 30.102  -6.613  1.00 61.92  ? 128  SER A N   1 
ATOM   600   C  CA  . SER A  1 128 ? -15.770 30.865  -5.565  1.00 59.39  ? 128  SER A CA  1 
ATOM   601   C  C   . SER A  1 128 ? -16.711 30.018  -4.701  1.00 55.28  ? 128  SER A C   1 
ATOM   602   O  O   . SER A  1 128 ? -17.063 30.412  -3.584  1.00 51.22  ? 128  SER A O   1 
ATOM   603   C  CB  . SER A  1 128 ? -16.545 32.035  -6.187  1.00 55.84  ? 128  SER A CB  1 
ATOM   604   O  OG  . SER A  1 128 ? -17.455 31.588  -7.179  1.00 59.27  ? 128  SER A OG  1 
ATOM   605   N  N   . ARG A  1 129 ? -17.109 28.854  -5.203  1.00 53.12  ? 129  ARG A N   1 
ATOM   606   C  CA  . ARG A  1 129 ? -17.916 27.949  -4.394  1.00 55.67  ? 129  ARG A CA  1 
ATOM   607   C  C   . ARG A  1 129 ? -17.161 27.547  -3.134  1.00 56.23  ? 129  ARG A C   1 
ATOM   608   O  O   . ARG A  1 129 ? -17.774 27.221  -2.120  1.00 58.61  ? 129  ARG A O   1 
ATOM   609   C  CB  . ARG A  1 129 ? -18.311 26.702  -5.182  1.00 59.34  ? 129  ARG A CB  1 
ATOM   610   C  CG  . ARG A  1 129 ? -19.112 26.988  -6.430  1.00 63.49  ? 129  ARG A CG  1 
ATOM   611   C  CD  . ARG A  1 129 ? -19.337 25.727  -7.226  1.00 63.20  ? 129  ARG A CD  1 
ATOM   612   N  NE  . ARG A  1 129 ? -18.078 25.173  -7.714  1.00 72.25  ? 129  ARG A NE  1 
ATOM   613   C  CZ  . ARG A  1 129 ? -17.943 23.941  -8.196  1.00 68.26  ? 129  ARG A CZ  1 
ATOM   614   N  NH1 . ARG A  1 129 ? -18.997 23.143  -8.244  1.00 69.59  ? 129  ARG A NH1 1 
ATOM   615   N  NH2 . ARG A  1 129 ? -16.763 23.506  -8.628  1.00 62.36  ? 129  ARG A NH2 1 
ATOM   616   N  N   . TYR A  1 130 ? -15.831 27.585  -3.195  1.00 52.01  ? 130  TYR A N   1 
ATOM   617   C  CA  . TYR A  1 130 ? -15.012 27.185  -2.053  1.00 56.49  ? 130  TYR A CA  1 
ATOM   618   C  C   . TYR A  1 130 ? -14.257 28.370  -1.466  1.00 56.67  ? 130  TYR A C   1 
ATOM   619   O  O   . TYR A  1 130 ? -13.227 28.197  -0.812  1.00 52.71  ? 130  TYR A O   1 
ATOM   620   C  CB  . TYR A  1 130 ? -14.037 26.064  -2.455  1.00 51.56  ? 130  TYR A CB  1 
ATOM   621   C  CG  . TYR A  1 130 ? -14.744 24.750  -2.756  1.00 52.27  ? 130  TYR A CG  1 
ATOM   622   C  CD1 . TYR A  1 130 ? -15.091 23.865  -1.732  1.00 53.04  ? 130  TYR A CD1 1 
ATOM   623   C  CD2 . TYR A  1 130 ? -15.087 24.407  -4.066  1.00 53.70  ? 130  TYR A CD2 1 
ATOM   624   C  CE1 . TYR A  1 130 ? -15.754 22.658  -2.010  1.00 52.62  ? 130  TYR A CE1 1 
ATOM   625   C  CE2 . TYR A  1 130 ? -15.739 23.209  -4.360  1.00 51.38  ? 130  TYR A CE2 1 
ATOM   626   C  CZ  . TYR A  1 130 ? -16.072 22.343  -3.329  1.00 57.08  ? 130  TYR A CZ  1 
ATOM   627   O  OH  . TYR A  1 130 ? -16.722 21.174  -3.630  1.00 55.93  ? 130  TYR A OH  1 
ATOM   628   N  N   . MET A  1 131 ? -14.783 29.570  -1.707  1.00 58.37  ? 131  MET A N   1 
ATOM   629   C  CA  . MET A  1 131 ? -14.194 30.804  -1.198  1.00 57.51  ? 131  MET A CA  1 
ATOM   630   C  C   . MET A  1 131 ? -14.159 30.753  0.316   1.00 53.27  ? 131  MET A C   1 
ATOM   631   O  O   . MET A  1 131 ? -15.099 30.267  0.925   1.00 59.53  ? 131  MET A O   1 
ATOM   632   C  CB  . MET A  1 131 ? -14.984 32.024  -1.672  1.00 55.81  ? 131  MET A CB  1 
ATOM   633   C  CG  . MET A  1 131 ? -14.469 33.356  -1.130  1.00 60.18  ? 131  MET A CG  1 
ATOM   634   S  SD  . MET A  1 131 ? -15.476 34.783  -1.618  1.00 60.44  ? 131  MET A SD  1 
ATOM   635   C  CE  . MET A  1 131 ? -15.044 35.001  -3.351  1.00 46.66  ? 131  MET A CE  1 
ATOM   636   N  N   . LYS A  1 132 ? -13.059 31.227  0.893   1.00 48.01  ? 132  LYS A N   1 
ATOM   637   C  CA  . LYS A  1 132 ? -12.840 31.255  2.334   1.00 52.62  ? 132  LYS A CA  1 
ATOM   638   C  C   . LYS A  1 132 ? -14.128 31.582  3.073   1.00 60.14  ? 132  LYS A C   1 
ATOM   639   O  O   . LYS A  1 132 ? -14.834 32.522  2.692   1.00 54.46  ? 132  LYS A O   1 
ATOM   640   C  CB  . LYS A  1 132 ? -11.739 32.280  2.664   1.00 55.93  ? 132  LYS A CB  1 
ATOM   641   C  CG  . LYS A  1 132 ? -11.508 32.560  4.136   1.00 55.02  ? 132  LYS A CG  1 
ATOM   642   C  CD  . LYS A  1 132 ? -10.350 33.524  4.333   1.00 58.38  ? 132  LYS A CD  1 
ATOM   643   C  CE  . LYS A  1 132 ? -10.178 33.931  5.799   1.00 71.87  ? 132  LYS A CE  1 
ATOM   644   N  NZ  . LYS A  1 132 ? -9.410  35.217  5.970   1.00 74.39  ? 132  LYS A NZ  1 
ATOM   645   N  N   . PRO A  1 133 ? -14.456 30.796  4.121   1.00 63.23  ? 133  PRO A N   1 
ATOM   646   C  CA  . PRO A  1 133 ? -13.634 29.713  4.662   1.00 60.50  ? 133  PRO A CA  1 
ATOM   647   C  C   . PRO A  1 133 ? -14.057 28.308  4.244   1.00 59.02  ? 133  PRO A C   1 
ATOM   648   O  O   . PRO A  1 133 ? -13.200 27.435  4.271   1.00 59.14  ? 133  PRO A O   1 
ATOM   649   C  CB  . PRO A  1 133 ? -13.842 29.871  6.158   1.00 49.73  ? 133  PRO A CB  1 
ATOM   650   C  CG  . PRO A  1 133 ? -15.296 30.212  6.236   1.00 49.97  ? 133  PRO A CG  1 
ATOM   651   C  CD  . PRO A  1 133 ? -15.611 31.050  5.001   1.00 47.05  ? 133  PRO A CD  1 
ATOM   652   N  N   . GLY A  1 134 ? -15.333 28.098  3.902   1.00 64.34  ? 134  GLY A N   1 
ATOM   653   C  CA  . GLY A  1 134 ? -15.898 26.762  3.715   1.00 59.40  ? 134  GLY A CA  1 
ATOM   654   C  C   . GLY A  1 134 ? -15.220 26.085  2.552   1.00 61.86  ? 134  GLY A C   1 
ATOM   655   O  O   . GLY A  1 134 ? -14.508 26.764  1.805   1.00 60.74  ? 134  GLY A O   1 
ATOM   656   N  N   . LYS A  1 135 ? -15.432 24.781  2.367   1.00 59.48  ? 135  LYS A N   1 
ATOM   657   C  CA  . LYS A  1 135 ? -16.394 23.995  3.124   1.00 57.76  ? 135  LYS A CA  1 
ATOM   658   C  C   . LYS A  1 135 ? -15.766 22.737  3.704   1.00 56.27  ? 135  LYS A C   1 
ATOM   659   O  O   . LYS A  1 135 ? -14.691 22.326  3.278   1.00 57.32  ? 135  LYS A O   1 
ATOM   660   C  CB  . LYS A  1 135 ? -17.562 23.596  2.228   1.00 60.43  ? 135  LYS A CB  1 
ATOM   661   C  CG  . LYS A  1 135 ? -17.996 24.678  1.262   1.00 64.50  ? 135  LYS A CG  1 
ATOM   662   C  CD  . LYS A  1 135 ? -19.350 24.353  0.664   1.00 69.23  ? 135  LYS A CD  1 
ATOM   663   C  CE  . LYS A  1 135 ? -19.843 25.481  -0.220  1.00 71.67  ? 135  LYS A CE  1 
ATOM   664   N  NZ  . LYS A  1 135 ? -19.793 26.786  0.490   1.00 76.24  ? 135  LYS A NZ  1 
ATOM   665   N  N   . GLU A  1 136 ? -16.453 22.113  4.659   1.00 60.80  ? 136  GLU A N   1 
ATOM   666   C  CA  . GLU A  1 136 ? -15.977 20.865  5.256   1.00 65.13  ? 136  GLU A CA  1 
ATOM   667   C  C   . GLU A  1 136 ? -15.889 19.747  4.236   1.00 61.61  ? 136  GLU A C   1 
ATOM   668   O  O   . GLU A  1 136 ? -16.744 19.627  3.371   1.00 65.05  ? 136  GLU A O   1 
ATOM   669   C  CB  . GLU A  1 136 ? -16.882 20.414  6.401   1.00 61.29  ? 136  GLU A CB  1 
ATOM   670   C  CG  . GLU A  1 136 ? -16.812 21.290  7.618   1.00 70.81  ? 136  GLU A CG  1 
ATOM   671   C  CD  . GLU A  1 136 ? -17.231 20.557  8.875   1.00 90.56  ? 136  GLU A CD  1 
ATOM   672   O  OE1 . GLU A  1 136 ? -16.407 19.770  9.399   1.00 95.88  ? 136  GLU A OE1 1 
ATOM   673   O  OE2 . GLU A  1 136 ? -18.378 20.765  9.338   1.00 89.00  ? 136  GLU A OE2 1 
ATOM   674   N  N   . LEU A  1 137 ? -14.842 18.939  4.333   1.00 58.63  ? 137  LEU A N   1 
ATOM   675   C  CA  . LEU A  1 137 ? -14.744 17.732  3.531   1.00 61.46  ? 137  LEU A CA  1 
ATOM   676   C  C   . LEU A  1 137 ? -15.242 16.547  4.348   1.00 61.76  ? 137  LEU A C   1 
ATOM   677   O  O   . LEU A  1 137 ? -15.069 16.503  5.566   1.00 51.89  ? 137  LEU A O   1 
ATOM   678   C  CB  . LEU A  1 137 ? -13.305 17.505  3.069   1.00 54.54  ? 137  LEU A CB  1 
ATOM   679   C  CG  . LEU A  1 137 ? -12.835 18.540  2.053   1.00 58.57  ? 137  LEU A CG  1 
ATOM   680   C  CD1 . LEU A  1 137 ? -11.318 18.665  2.018   1.00 50.76  ? 137  LEU A CD1 1 
ATOM   681   C  CD2 . LEU A  1 137 ? -13.377 18.156  0.689   1.00 55.69  ? 137  LEU A CD2 1 
ATOM   682   N  N   . LYS A  1 138 ? -15.887 15.597  3.685   1.00 64.77  ? 138  LYS A N   1 
ATOM   683   C  CA  . LYS A  1 138 ? -16.228 14.349  4.351   1.00 64.49  ? 138  LYS A CA  1 
ATOM   684   C  C   . LYS A  1 138 ? -15.024 13.419  4.211   1.00 61.91  ? 138  LYS A C   1 
ATOM   685   O  O   . LYS A  1 138 ? -14.473 13.267  3.102   1.00 54.16  ? 138  LYS A O   1 
ATOM   686   C  CB  . LYS A  1 138 ? -17.493 13.726  3.751   1.00 69.02  ? 138  LYS A CB  1 
ATOM   687   C  CG  . LYS A  1 138 ? -17.997 12.491  4.493   1.00 71.67  ? 138  LYS A CG  1 
ATOM   688   C  CD  . LYS A  1 138 ? -18.276 12.808  5.950   1.00 70.15  ? 138  LYS A CD  1 
ATOM   689   C  CE  . LYS A  1 138 ? -18.639 11.554  6.723   1.00 81.14  ? 138  LYS A CE  1 
ATOM   690   N  NZ  . LYS A  1 138 ? -18.834 11.847  8.180   1.00 97.24  ? 138  LYS A NZ  1 
ATOM   691   N  N   . VAL A  1 139 ? -14.617 12.819  5.329   1.00 54.12  ? 139  VAL A N   1 
ATOM   692   C  CA  . VAL A  1 139 ? -13.416 11.982  5.372   1.00 57.67  ? 139  VAL A CA  1 
ATOM   693   C  C   . VAL A  1 139 ? -13.734 10.501  5.565   1.00 59.27  ? 139  VAL A C   1 
ATOM   694   O  O   . VAL A  1 139 ? -14.330 10.105  6.570   1.00 63.69  ? 139  VAL A O   1 
ATOM   695   C  CB  . VAL A  1 139 ? -12.462 12.417  6.508   1.00 58.95  ? 139  VAL A CB  1 
ATOM   696   C  CG1 . VAL A  1 139 ? -11.274 11.481  6.592   1.00 51.54  ? 139  VAL A CG1 1 
ATOM   697   C  CG2 . VAL A  1 139 ? -12.008 13.866  6.317   1.00 51.44  ? 139  VAL A CG2 1 
ATOM   698   N  N   . LEU A  1 140 ? -13.303 9.696   4.597   1.00 61.09  ? 140  LEU A N   1 
ATOM   699   C  CA  . LEU A  1 140 ? -13.444 8.240   4.624   1.00 62.95  ? 140  LEU A CA  1 
ATOM   700   C  C   . LEU A  1 140 ? -12.091 7.522   4.606   1.00 63.64  ? 140  LEU A C   1 
ATOM   701   O  O   . LEU A  1 140 ? -11.270 7.760   3.709   1.00 59.67  ? 140  LEU A O   1 
ATOM   702   C  CB  . LEU A  1 140 ? -14.267 7.770   3.427   1.00 62.43  ? 140  LEU A CB  1 
ATOM   703   C  CG  . LEU A  1 140 ? -15.767 8.047   3.467   1.00 72.36  ? 140  LEU A CG  1 
ATOM   704   C  CD1 . LEU A  1 140 ? -16.452 7.438   2.229   1.00 66.50  ? 140  LEU A CD1 1 
ATOM   705   C  CD2 . LEU A  1 140 ? -16.364 7.528   4.784   1.00 68.03  ? 140  LEU A CD2 1 
ATOM   706   N  N   . SER A  1 141 ? -11.880 6.617   5.562   1.00 63.25  ? 141  SER A N   1 
ATOM   707   C  CA  . SER A  1 141 ? -10.587 5.944   5.716   1.00 58.63  ? 141  SER A CA  1 
ATOM   708   C  C   . SER A  1 141 ? -10.611 4.449   5.362   1.00 59.15  ? 141  SER A C   1 
ATOM   709   O  O   . SER A  1 141 ? -11.434 3.701   5.862   1.00 65.18  ? 141  SER A O   1 
ATOM   710   C  CB  . SER A  1 141 ? -10.089 6.113   7.143   1.00 52.52  ? 141  SER A CB  1 
ATOM   711   O  OG  . SER A  1 141 ? -10.058 4.857   7.780   1.00 62.90  ? 141  SER A OG  1 
ATOM   712   N  N   . TYR A  1 142 ? -9.696  4.026   4.493   1.00 63.24  ? 142  TYR A N   1 
ATOM   713   C  CA  . TYR A  1 142 ? -9.621  2.641   4.004   1.00 52.29  ? 142  TYR A CA  1 
ATOM   714   C  C   . TYR A  1 142 ? -8.226  2.075   4.242   1.00 50.04  ? 142  TYR A C   1 
ATOM   715   O  O   . TYR A  1 142 ? -7.412  2.027   3.314   1.00 54.92  ? 142  TYR A O   1 
ATOM   716   C  CB  . TYR A  1 142 ? -9.959  2.592   2.514   1.00 53.56  ? 142  TYR A CB  1 
ATOM   717   C  CG  . TYR A  1 142 ? -9.867  1.231   1.841   1.00 56.93  ? 142  TYR A CG  1 
ATOM   718   C  CD1 . TYR A  1 142 ? -10.289 0.068   2.486   1.00 58.81  ? 142  TYR A CD1 1 
ATOM   719   C  CD2 . TYR A  1 142 ? -9.392  1.118   0.531   1.00 61.19  ? 142  TYR A CD2 1 
ATOM   720   C  CE1 . TYR A  1 142 ? -10.212 -1.170  1.855   1.00 61.15  ? 142  TYR A CE1 1 
ATOM   721   C  CE2 . TYR A  1 142 ? -9.316  -0.116  -0.108  1.00 60.29  ? 142  TYR A CE2 1 
ATOM   722   C  CZ  . TYR A  1 142 ? -9.730  -1.255  0.557   1.00 63.02  ? 142  TYR A CZ  1 
ATOM   723   O  OH  . TYR A  1 142 ? -9.657  -2.480  -0.077  1.00 65.05  ? 142  TYR A OH  1 
ATOM   724   N  N   . PRO A  1 143 ? -7.951  1.629   5.478   1.00 42.56  ? 143  PRO A N   1 
ATOM   725   C  CA  . PRO A  1 143 ? -6.592  1.295   5.918   1.00 46.81  ? 143  PRO A CA  1 
ATOM   726   C  C   . PRO A  1 143 ? -5.846  0.272   5.068   1.00 48.42  ? 143  PRO A C   1 
ATOM   727   O  O   . PRO A  1 143 ? -4.627  0.230   5.115   1.00 51.59  ? 143  PRO A O   1 
ATOM   728   C  CB  . PRO A  1 143 ? -6.821  0.735   7.319   1.00 37.68  ? 143  PRO A CB  1 
ATOM   729   C  CG  . PRO A  1 143 ? -8.058  1.445   7.782   1.00 45.47  ? 143  PRO A CG  1 
ATOM   730   C  CD  . PRO A  1 143 ? -8.925  1.479   6.574   1.00 39.39  ? 143  PRO A CD  1 
ATOM   731   N  N   . ALA A  1 144 ? -6.558  -0.537  4.305   1.00 45.52  ? 144  ALA A N   1 
ATOM   732   C  CA  . ALA A  1 144 ? -5.923  -1.646  3.619   1.00 54.33  ? 144  ALA A CA  1 
ATOM   733   C  C   . ALA A  1 144 ? -5.112  -1.158  2.426   1.00 55.91  ? 144  ALA A C   1 
ATOM   734   O  O   . ALA A  1 144 ? -4.241  -1.863  1.930   1.00 57.17  ? 144  ALA A O   1 
ATOM   735   C  CB  . ALA A  1 144 ? -6.972  -2.664  3.180   1.00 56.69  ? 144  ALA A CB  1 
ATOM   736   N  N   . HIS A  1 145 ? -5.416  0.045   1.960   1.00 53.15  ? 145  HIS A N   1 
ATOM   737   C  CA  . HIS A  1 145 ? -4.626  0.682   0.920   1.00 48.70  ? 145  HIS A CA  1 
ATOM   738   C  C   . HIS A  1 145 ? -3.895  1.875   1.506   1.00 49.04  ? 145  HIS A C   1 
ATOM   739   O  O   . HIS A  1 145 ? -3.226  2.636   0.778   1.00 43.17  ? 145  HIS A O   1 
ATOM   740   C  CB  . HIS A  1 145 ? -5.509  1.113   -0.240  1.00 51.68  ? 145  HIS A CB  1 
ATOM   741   C  CG  . HIS A  1 145 ? -5.795  0.014   -1.206  1.00 61.14  ? 145  HIS A CG  1 
ATOM   742   N  ND1 . HIS A  1 145 ? -5.742  -1.317  -0.848  1.00 64.13  ? 145  HIS A ND1 1 
ATOM   743   C  CD2 . HIS A  1 145 ? -6.114  0.040   -2.521  1.00 63.50  ? 145  HIS A CD2 1 
ATOM   744   C  CE1 . HIS A  1 145 ? -6.020  -2.064  -1.902  1.00 62.88  ? 145  HIS A CE1 1 
ATOM   745   N  NE2 . HIS A  1 145 ? -6.254  -1.266  -2.929  1.00 58.18  ? 145  HIS A NE2 1 
ATOM   746   N  N   . GLU A  1 146 ? -4.035  2.014   2.827   1.00 43.10  ? 146  GLU A N   1 
ATOM   747   C  CA  . GLU A  1 146 ? -3.425  3.090   3.596   1.00 47.87  ? 146  GLU A CA  1 
ATOM   748   C  C   . GLU A  1 146 ? -3.837  4.427   2.969   1.00 49.26  ? 146  GLU A C   1 
ATOM   749   O  O   . GLU A  1 146 ? -3.054  5.389   2.880   1.00 46.01  ? 146  GLU A O   1 
ATOM   750   C  CB  . GLU A  1 146 ? -1.900  2.905   3.666   1.00 45.68  ? 146  GLU A CB  1 
ATOM   751   C  CG  . GLU A  1 146 ? -1.485  1.724   4.531   1.00 48.77  ? 146  GLU A CG  1 
ATOM   752   C  CD  . GLU A  1 146 ? 0.018   1.435   4.501   1.00 55.96  ? 146  GLU A CD  1 
ATOM   753   O  OE1 . GLU A  1 146 ? 0.764   2.222   3.878   1.00 52.83  ? 146  GLU A OE1 1 
ATOM   754   O  OE2 . GLU A  1 146 ? 0.455   0.420   5.103   1.00 52.14  ? 146  GLU A OE2 1 
ATOM   755   N  N   . GLN A  1 147 ? -5.098  4.452   2.544   1.00 47.70  ? 147  GLN A N   1 
ATOM   756   C  CA  . GLN A  1 147 ? -5.702  5.596   1.891   1.00 47.71  ? 147  GLN A CA  1 
ATOM   757   C  C   . GLN A  1 147 ? -6.796  6.236   2.746   1.00 50.05  ? 147  GLN A C   1 
ATOM   758   O  O   . GLN A  1 147 ? -7.308  5.633   3.691   1.00 49.15  ? 147  GLN A O   1 
ATOM   759   C  CB  . GLN A  1 147 ? -6.271  5.177   0.540   1.00 45.26  ? 147  GLN A CB  1 
ATOM   760   C  CG  . GLN A  1 147 ? -5.228  4.678   -0.450  1.00 44.33  ? 147  GLN A CG  1 
ATOM   761   C  CD  . GLN A  1 147 ? -5.834  4.322   -1.792  1.00 49.49  ? 147  GLN A CD  1 
ATOM   762   O  OE1 . GLN A  1 147 ? -7.052  4.199   -1.910  1.00 65.35  ? 147  GLN A OE1 1 
ATOM   763   N  NE2 . GLN A  1 147 ? -4.996  4.158   -2.812  1.00 41.70  ? 147  GLN A NE2 1 
ATOM   764   N  N   . ILE A  1 148 ? -7.106  7.489   2.437   1.00 50.21  ? 148  ILE A N   1 
ATOM   765   C  CA  . ILE A  1 148 ? -8.324  8.121   2.921   1.00 53.42  ? 148  ILE A CA  1 
ATOM   766   C  C   . ILE A  1 148 ? -9.002  8.782   1.745   1.00 48.61  ? 148  ILE A C   1 
ATOM   767   O  O   . ILE A  1 148 ? -8.361  9.065   0.731   1.00 50.15  ? 148  ILE A O   1 
ATOM   768   C  CB  . ILE A  1 148 ? -8.079  9.170   4.012   1.00 46.64  ? 148  ILE A CB  1 
ATOM   769   C  CG1 . ILE A  1 148 ? -7.059  10.213  3.542   1.00 46.61  ? 148  ILE A CG1 1 
ATOM   770   C  CG2 . ILE A  1 148 ? -7.652  8.518   5.299   1.00 39.41  ? 148  ILE A CG2 1 
ATOM   771   C  CD1 . ILE A  1 148 ? -6.876  11.357  4.531   1.00 41.80  ? 148  ILE A CD1 1 
ATOM   772   N  N   . ALA A  1 149 ? -10.300 9.014   1.866   1.00 54.54  ? 149  ALA A N   1 
ATOM   773   C  CA  . ALA A  1 149 ? -11.017 9.733   0.816   1.00 54.17  ? 149  ALA A CA  1 
ATOM   774   C  C   . ALA A  1 149 ? -11.608 11.015  1.372   1.00 52.80  ? 149  ALA A C   1 
ATOM   775   O  O   . ALA A  1 149 ? -12.338 10.990  2.357   1.00 53.39  ? 149  ALA A O   1 
ATOM   776   C  CB  . ALA A  1 149 ? -12.097 8.876   0.214   1.00 53.61  ? 149  ALA A CB  1 
ATOM   777   N  N   . LEU A  1 150 ? -11.264 12.134  0.747   1.00 53.81  ? 150  LEU A N   1 
ATOM   778   C  CA  . LEU A  1 150 ? -11.915 13.398  1.027   1.00 53.27  ? 150  LEU A CA  1 
ATOM   779   C  C   . LEU A  1 150 ? -13.079 13.581  0.061   1.00 50.48  ? 150  LEU A C   1 
ATOM   780   O  O   . LEU A  1 150 ? -12.889 13.650  -1.141  1.00 52.36  ? 150  LEU A O   1 
ATOM   781   C  CB  . LEU A  1 150 ? -10.926 14.548  0.914   1.00 51.63  ? 150  LEU A CB  1 
ATOM   782   C  CG  . LEU A  1 150 ? -9.695  14.380  1.795   1.00 52.01  ? 150  LEU A CG  1 
ATOM   783   C  CD1 . LEU A  1 150 ? -8.781  15.562  1.620   1.00 50.25  ? 150  LEU A CD1 1 
ATOM   784   C  CD2 . LEU A  1 150 ? -10.076 14.210  3.249   1.00 47.35  ? 150  LEU A CD2 1 
ATOM   785   N  N   . LEU A  1 151 ? -14.289 13.631  0.598   1.00 57.05  ? 151  LEU A N   1 
ATOM   786   C  CA  . LEU A  1 151 ? -15.478 13.783  -0.229  1.00 59.98  ? 151  LEU A CA  1 
ATOM   787   C  C   . LEU A  1 151 ? -15.912 15.257  -0.356  1.00 59.07  ? 151  LEU A C   1 
ATOM   788   O  O   . LEU A  1 151 ? -16.176 15.963  0.620   1.00 58.51  ? 151  LEU A O   1 
ATOM   789   C  CB  . LEU A  1 151 ? -16.601 12.923  0.339   1.00 58.76  ? 151  LEU A CB  1 
ATOM   790   C  CG  . LEU A  1 151 ? -16.092 11.533  0.726   1.00 62.40  ? 151  LEU A CG  1 
ATOM   791   C  CD1 . LEU A  1 151 ? -17.192 10.780  1.439   1.00 63.94  ? 151  LEU A CD1 1 
ATOM   792   C  CD2 . LEU A  1 151 ? -15.554 10.749  -0.501  1.00 50.83  ? 151  LEU A CD2 1 
ATOM   793   N  N   . VAL A  1 152 ? -15.974 15.707  -1.593  1.00 61.80  ? 152  VAL A N   1 
ATOM   794   C  CA  . VAL A  1 152 ? -16.243 17.094  -1.898  1.00 62.09  ? 152  VAL A CA  1 
ATOM   795   C  C   . VAL A  1 152 ? -17.745 17.302  -2.143  1.00 66.56  ? 152  VAL A C   1 
ATOM   796   O  O   . VAL A  1 152 ? -18.395 16.472  -2.788  1.00 65.71  ? 152  VAL A O   1 
ATOM   797   C  CB  . VAL A  1 152 ? -15.407 17.518  -3.125  1.00 57.57  ? 152  VAL A CB  1 
ATOM   798   C  CG1 . VAL A  1 152 ? -16.246 18.160  -4.148  1.00 60.13  ? 152  VAL A CG1 1 
ATOM   799   C  CG2 . VAL A  1 152 ? -14.284 18.427  -2.722  1.00 58.41  ? 152  VAL A CG2 1 
ATOM   800   N  N   . PRO A  1 153 ? -18.307 18.401  -1.611  1.00 68.92  ? 153  PRO A N   1 
ATOM   801   C  CA  . PRO A  1 153 ? -19.719 18.739  -1.844  1.00 67.02  ? 153  PRO A CA  1 
ATOM   802   C  C   . PRO A  1 153 ? -20.051 18.936  -3.332  1.00 69.38  ? 153  PRO A C   1 
ATOM   803   O  O   . PRO A  1 153 ? -21.038 18.383  -3.817  1.00 75.71  ? 153  PRO A O   1 
ATOM   804   C  CB  . PRO A  1 153 ? -19.903 20.043  -1.058  1.00 65.45  ? 153  PRO A CB  1 
ATOM   805   C  CG  . PRO A  1 153 ? -18.523 20.596  -0.884  1.00 61.89  ? 153  PRO A CG  1 
ATOM   806   C  CD  . PRO A  1 153 ? -17.632 19.402  -0.766  1.00 64.26  ? 153  PRO A CD  1 
ATOM   807   N  N   . GLU A  1 154 ? -19.222 19.685  -4.054  1.00 64.59  ? 154  GLU A N   1 
ATOM   808   C  CA  . GLU A  1 154 ? -19.474 19.944  -5.470  1.00 68.68  ? 154  GLU A CA  1 
ATOM   809   C  C   . GLU A  1 154 ? -18.301 19.565  -6.398  1.00 62.42  ? 154  GLU A C   1 
ATOM   810   O  O   . GLU A  1 154 ? -17.188 20.057  -6.223  1.00 55.99  ? 154  GLU A O   1 
ATOM   811   C  CB  . GLU A  1 154 ? -19.811 21.425  -5.661  1.00 72.12  ? 154  GLU A CB  1 
ATOM   812   C  CG  . GLU A  1 154 ? -20.724 22.019  -4.596  1.00 75.12  ? 154  GLU A CG  1 
ATOM   813   C  CD  . GLU A  1 154 ? -21.261 23.379  -4.997  1.00 86.94  ? 154  GLU A CD  1 
ATOM   814   O  OE1 . GLU A  1 154 ? -21.450 23.599  -6.221  1.00 82.11  ? 154  GLU A OE1 1 
ATOM   815   O  OE2 . GLU A  1 154 ? -21.486 24.226  -4.097  1.00 85.99  ? 154  GLU A OE2 1 
ATOM   816   N  N   . LYS A  1 155 ? -18.563 18.711  -7.387  1.00 62.43  ? 155  LYS A N   1 
ATOM   817   C  CA  . LYS A  1 155 ? -17.543 18.285  -8.352  1.00 62.18  ? 155  LYS A CA  1 
ATOM   818   C  C   . LYS A  1 155 ? -16.521 19.385  -8.671  1.00 67.37  ? 155  LYS A C   1 
ATOM   819   O  O   . LYS A  1 155 ? -16.872 20.481  -9.131  1.00 64.52  ? 155  LYS A O   1 
ATOM   820   C  CB  . LYS A  1 155 ? -18.199 17.814  -9.649  1.00 65.43  ? 155  LYS A CB  1 
ATOM   821   C  CG  . LYS A  1 155 ? -18.997 16.528  -9.533  1.00 72.59  ? 155  LYS A CG  1 
ATOM   822   C  CD  . LYS A  1 155 ? -20.103 16.465  -10.596 1.00 83.90  ? 155  LYS A CD  1 
ATOM   823   C  CE  . LYS A  1 155 ? -20.595 15.042  -10.854 1.00 84.82  ? 155  LYS A CE  1 
ATOM   824   N  NZ  . LYS A  1 155 ? -19.634 14.237  -11.669 1.00 89.82  ? 155  LYS A NZ  1 
ATOM   825   N  N   . LEU A  1 156 ? -15.259 19.100  -8.386  1.00 61.80  ? 156  LEU A N   1 
ATOM   826   C  CA  . LEU A  1 156 ? -14.215 20.091  -8.568  1.00 59.62  ? 156  LEU A CA  1 
ATOM   827   C  C   . LEU A  1 156 ? -14.018 20.429  -10.042 1.00 61.71  ? 156  LEU A C   1 
ATOM   828   O  O   . LEU A  1 156 ? -14.304 19.622  -10.926 1.00 60.68  ? 156  LEU A O   1 
ATOM   829   C  CB  . LEU A  1 156 ? -12.902 19.606  -7.954  1.00 55.13  ? 156  LEU A CB  1 
ATOM   830   C  CG  . LEU A  1 156 ? -12.943 19.410  -6.443  1.00 52.54  ? 156  LEU A CG  1 
ATOM   831   C  CD1 . LEU A  1 156 ? -11.540 19.498  -5.886  1.00 51.82  ? 156  LEU A CD1 1 
ATOM   832   C  CD2 . LEU A  1 156 ? -13.842 20.429  -5.797  1.00 54.39  ? 156  LEU A CD2 1 
ATOM   833   N  N   . THR A  1 157 ? -13.515 21.633  -10.292 1.00 56.22  ? 157  THR A N   1 
ATOM   834   C  CA  . THR A  1 157 ? -13.359 22.142  -11.640 1.00 54.24  ? 157  THR A CA  1 
ATOM   835   C  C   . THR A  1 157 ? -11.976 21.873  -12.168 1.00 53.25  ? 157  THR A C   1 
ATOM   836   O  O   . THR A  1 157 ? -11.003 22.207  -11.503 1.00 57.51  ? 157  THR A O   1 
ATOM   837   C  CB  . THR A  1 157 ? -13.608 23.661  -11.684 1.00 55.79  ? 157  THR A CB  1 
ATOM   838   O  OG1 . THR A  1 157 ? -14.875 23.955  -11.086 1.00 56.26  ? 157  THR A OG1 1 
ATOM   839   C  CG2 . THR A  1 157 ? -13.581 24.177  -13.107 1.00 48.95  ? 157  THR A CG2 1 
ATOM   840   N  N   . PRO A  1 158 ? -11.881 21.288  -13.371 1.00 55.91  ? 158  PRO A N   1 
ATOM   841   C  CA  . PRO A  1 158 ? -10.602 21.118  -14.078 1.00 57.22  ? 158  PRO A CA  1 
ATOM   842   C  C   . PRO A  1 158 ? -9.823  22.426  -14.164 1.00 55.40  ? 158  PRO A C   1 
ATOM   843   O  O   . PRO A  1 158 ? -10.422 23.479  -14.381 1.00 61.01  ? 158  PRO A O   1 
ATOM   844   C  CB  . PRO A  1 158 ? -11.018 20.659  -15.483 1.00 56.43  ? 158  PRO A CB  1 
ATOM   845   C  CG  . PRO A  1 158 ? -12.385 20.100  -15.319 1.00 56.57  ? 158  PRO A CG  1 
ATOM   846   C  CD  . PRO A  1 158 ? -13.028 20.798  -14.154 1.00 55.50  ? 158  PRO A CD  1 
ATOM   847   N  N   . HIS A  1 159 ? -8.512  22.345  -13.980 1.00 53.92  ? 159  HIS A N   1 
ATOM   848   C  CA  . HIS A  1 159 ? -7.582  23.471  -14.132 1.00 52.71  ? 159  HIS A CA  1 
ATOM   849   C  C   . HIS A  1 159 ? -7.726  24.530  -13.060 1.00 55.72  ? 159  HIS A C   1 
ATOM   850   O  O   . HIS A  1 159 ? -7.102  25.587  -13.137 1.00 57.34  ? 159  HIS A O   1 
ATOM   851   C  CB  . HIS A  1 159 ? -7.720  24.101  -15.511 1.00 51.43  ? 159  HIS A CB  1 
ATOM   852   C  CG  . HIS A  1 159 ? -7.554  23.114  -16.617 1.00 66.94  ? 159  HIS A CG  1 
ATOM   853   N  ND1 . HIS A  1 159 ? -8.550  22.229  -16.976 1.00 72.78  ? 159  HIS A ND1 1 
ATOM   854   C  CD2 . HIS A  1 159 ? -6.494  22.829  -17.408 1.00 66.48  ? 159  HIS A CD2 1 
ATOM   855   C  CE1 . HIS A  1 159 ? -8.121  21.461  -17.963 1.00 74.24  ? 159  HIS A CE1 1 
ATOM   856   N  NE2 . HIS A  1 159 ? -6.874  21.801  -18.240 1.00 77.19  ? 159  HIS A NE2 1 
ATOM   857   N  N   . LEU A  1 160 ? -8.502  24.226  -12.031 1.00 47.85  ? 160  LEU A N   1 
ATOM   858   C  CA  . LEU A  1 160 ? -8.587  25.121  -10.902 1.00 51.34  ? 160  LEU A CA  1 
ATOM   859   C  C   . LEU A  1 160 ? -7.774  24.584  -9.722  1.00 56.98  ? 160  LEU A C   1 
ATOM   860   O  O   . LEU A  1 160 ? -7.798  23.388  -9.425  1.00 55.91  ? 160  LEU A O   1 
ATOM   861   C  CB  . LEU A  1 160 ? -10.051 25.340  -10.494 1.00 56.29  ? 160  LEU A CB  1 
ATOM   862   C  CG  . LEU A  1 160 ? -10.975 26.045  -11.498 1.00 57.04  ? 160  LEU A CG  1 
ATOM   863   C  CD1 . LEU A  1 160 ? -12.026 26.842  -10.765 1.00 51.30  ? 160  LEU A CD1 1 
ATOM   864   C  CD2 . LEU A  1 160 ? -10.215 26.944  -12.476 1.00 53.60  ? 160  LEU A CD2 1 
ATOM   865   N  N   . LYS A  1 161 ? -7.059  25.479  -9.053  1.00 52.34  ? 161  LYS A N   1 
ATOM   866   C  CA  . LYS A  1 161 ? -6.322  25.135  -7.853  1.00 45.82  ? 161  LYS A CA  1 
ATOM   867   C  C   . LYS A  1 161 ? -7.219  25.194  -6.623  1.00 48.49  ? 161  LYS A C   1 
ATOM   868   O  O   . LYS A  1 161 ? -8.095  26.043  -6.529  1.00 50.76  ? 161  LYS A O   1 
ATOM   869   C  CB  . LYS A  1 161 ? -5.134  26.080  -7.677  1.00 50.82  ? 161  LYS A CB  1 
ATOM   870   C  CG  . LYS A  1 161 ? -4.168  26.115  -8.855  1.00 51.87  ? 161  LYS A CG  1 
ATOM   871   C  CD  . LYS A  1 161 ? -3.025  27.083  -8.564  1.00 59.99  ? 161  LYS A CD  1 
ATOM   872   C  CE  . LYS A  1 161 ? -1.910  26.999  -9.601  1.00 55.54  ? 161  LYS A CE  1 
ATOM   873   N  NZ  . LYS A  1 161 ? -2.331  27.435  -10.964 1.00 64.69  ? 161  LYS A NZ  1 
ATOM   874   N  N   . TYR A  1 162 ? -7.009  24.285  -5.678  1.00 51.06  ? 162  TYR A N   1 
ATOM   875   C  CA  . TYR A  1 162 ? -7.770  24.300  -4.439  1.00 41.79  ? 162  TYR A CA  1 
ATOM   876   C  C   . TYR A  1 162 ? -6.824  24.138  -3.286  1.00 46.52  ? 162  TYR A C   1 
ATOM   877   O  O   . TYR A  1 162 ? -5.669  23.779  -3.477  1.00 48.34  ? 162  TYR A O   1 
ATOM   878   C  CB  . TYR A  1 162 ? -8.805  23.194  -4.403  1.00 38.48  ? 162  TYR A CB  1 
ATOM   879   C  CG  . TYR A  1 162 ? -9.857  23.301  -5.469  1.00 45.24  ? 162  TYR A CG  1 
ATOM   880   C  CD1 . TYR A  1 162 ? -9.548  23.058  -6.803  1.00 44.20  ? 162  TYR A CD1 1 
ATOM   881   C  CD2 . TYR A  1 162 ? -11.166 23.612  -5.146  1.00 49.13  ? 162  TYR A CD2 1 
ATOM   882   C  CE1 . TYR A  1 162 ? -10.488 23.151  -7.779  1.00 46.17  ? 162  TYR A CE1 1 
ATOM   883   C  CE2 . TYR A  1 162 ? -12.129 23.693  -6.122  1.00 51.71  ? 162  TYR A CE2 1 
ATOM   884   C  CZ  . TYR A  1 162 ? -11.778 23.462  -7.445  1.00 53.47  ? 162  TYR A CZ  1 
ATOM   885   O  OH  . TYR A  1 162 ? -12.718 23.543  -8.445  1.00 56.65  ? 162  TYR A OH  1 
ATOM   886   N  N   . TYR A  1 163 ? -7.316  24.393  -2.084  1.00 48.64  ? 163  TYR A N   1 
ATOM   887   C  CA  . TYR A  1 163 ? -6.516  24.195  -0.893  1.00 46.23  ? 163  TYR A CA  1 
ATOM   888   C  C   . TYR A  1 163 ? -7.151  23.188  0.051   1.00 47.07  ? 163  TYR A C   1 
ATOM   889   O  O   . TYR A  1 163 ? -8.251  23.404  0.562   1.00 47.25  ? 163  TYR A O   1 
ATOM   890   C  CB  . TYR A  1 163 ? -6.309  25.520  -0.186  1.00 48.46  ? 163  TYR A CB  1 
ATOM   891   C  CG  . TYR A  1 163 ? -5.528  26.491  -1.014  1.00 49.35  ? 163  TYR A CG  1 
ATOM   892   C  CD1 . TYR A  1 163 ? -4.150  26.414  -1.085  1.00 46.72  ? 163  TYR A CD1 1 
ATOM   893   C  CD2 . TYR A  1 163 ? -6.168  27.489  -1.731  1.00 53.42  ? 163  TYR A CD2 1 
ATOM   894   C  CE1 . TYR A  1 163 ? -3.428  27.313  -1.839  1.00 53.69  ? 163  TYR A CE1 1 
ATOM   895   C  CE2 . TYR A  1 163 ? -5.457  28.388  -2.496  1.00 55.04  ? 163  TYR A CE2 1 
ATOM   896   C  CZ  . TYR A  1 163 ? -4.087  28.299  -2.548  1.00 60.09  ? 163  TYR A CZ  1 
ATOM   897   O  OH  . TYR A  1 163 ? -3.371  29.206  -3.303  1.00 68.09  ? 163  TYR A OH  1 
ATOM   898   N  N   . VAL A  1 164 ? -6.450  22.083  0.284   1.00 48.71  ? 164  VAL A N   1 
ATOM   899   C  CA  . VAL A  1 164 ? -6.929  21.071  1.217   1.00 43.14  ? 164  VAL A CA  1 
ATOM   900   C  C   . VAL A  1 164 ? -6.294  21.265  2.579   1.00 45.51  ? 164  VAL A C   1 
ATOM   901   O  O   . VAL A  1 164 ? -5.071  21.258  2.719   1.00 49.04  ? 164  VAL A O   1 
ATOM   902   C  CB  . VAL A  1 164 ? -6.633  19.659  0.739   1.00 42.50  ? 164  VAL A CB  1 
ATOM   903   C  CG1 . VAL A  1 164 ? -7.159  18.679  1.752   1.00 48.24  ? 164  VAL A CG1 1 
ATOM   904   C  CG2 . VAL A  1 164 ? -7.267  19.397  -0.611  1.00 40.71  ? 164  VAL A CG2 1 
ATOM   905   N  N   . ALA A  1 165 ? -7.135  21.437  3.586   1.00 49.92  ? 165  ALA A N   1 
ATOM   906   C  CA  . ALA A  1 165 ? -6.665  21.741  4.925   1.00 43.88  ? 165  ALA A CA  1 
ATOM   907   C  C   . ALA A  1 165 ? -7.126  20.678  5.884   1.00 47.82  ? 165  ALA A C   1 
ATOM   908   O  O   . ALA A  1 165 ? -8.269  20.250  5.829   1.00 54.10  ? 165  ALA A O   1 
ATOM   909   C  CB  . ALA A  1 165 ? -7.163  23.095  5.366   1.00 45.83  ? 165  ALA A CB  1 
ATOM   910   N  N   . MET A  1 166 ? -6.238  20.261  6.779   1.00 53.15  ? 166  MET A N   1 
ATOM   911   C  CA  . MET A  1 166 ? -6.524  19.131  7.658   1.00 53.04  ? 166  MET A CA  1 
ATOM   912   C  C   . MET A  1 166 ? -5.828  19.279  9.022   1.00 46.89  ? 166  MET A C   1 
ATOM   913   O  O   . MET A  1 166 ? -4.704  19.769  9.087   1.00 46.22  ? 166  MET A O   1 
ATOM   914   C  CB  . MET A  1 166 ? -6.099  17.829  6.960   1.00 45.43  ? 166  MET A CB  1 
ATOM   915   C  CG  . MET A  1 166 ? -7.258  16.910  6.621   1.00 54.67  ? 166  MET A CG  1 
ATOM   916   S  SD  . MET A  1 166 ? -6.757  15.343  5.885   1.00 62.53  ? 166  MET A SD  1 
ATOM   917   C  CE  . MET A  1 166 ? -6.155  15.891  4.281   1.00 44.62  ? 166  MET A CE  1 
ATOM   918   N  N   . ASP A  1 167 ? -6.501  18.889  10.102  1.00 45.10  ? 167  ASP A N   1 
ATOM   919   C  CA  . ASP A  1 167 ? -5.848  18.783  11.410  1.00 44.56  ? 167  ASP A CA  1 
ATOM   920   C  C   . ASP A  1 167 ? -5.679  17.312  11.776  1.00 50.05  ? 167  ASP A C   1 
ATOM   921   O  O   . ASP A  1 167 ? -6.565  16.492  11.522  1.00 48.90  ? 167  ASP A O   1 
ATOM   922   C  CB  . ASP A  1 167 ? -6.637  19.492  12.494  1.00 47.72  ? 167  ASP A CB  1 
ATOM   923   C  CG  . ASP A  1 167 ? -6.674  20.996  12.308  1.00 64.28  ? 167  ASP A CG  1 
ATOM   924   O  OD1 . ASP A  1 167 ? -5.635  21.589  11.964  1.00 64.51  ? 167  ASP A OD1 1 
ATOM   925   O  OD2 . ASP A  1 167 ? -7.749  21.598  12.512  1.00 73.89  ? 167  ASP A OD2 1 
ATOM   926   N  N   . PHE A  1 168 ? -4.541  16.958  12.354  1.00 43.89  ? 168  PHE A N   1 
ATOM   927   C  CA  . PHE A  1 168 ? -4.327  15.562  12.682  1.00 45.06  ? 168  PHE A CA  1 
ATOM   928   C  C   . PHE A  1 168 ? -3.404  15.442  13.860  1.00 43.65  ? 168  PHE A C   1 
ATOM   929   O  O   . PHE A  1 168 ? -2.738  16.405  14.240  1.00 37.56  ? 168  PHE A O   1 
ATOM   930   C  CB  . PHE A  1 168 ? -3.776  14.782  11.483  1.00 45.59  ? 168  PHE A CB  1 
ATOM   931   C  CG  . PHE A  1 168 ? -2.643  15.473  10.769  1.00 51.25  ? 168  PHE A CG  1 
ATOM   932   C  CD1 . PHE A  1 168 ? -2.891  16.519  9.867   1.00 49.14  ? 168  PHE A CD1 1 
ATOM   933   C  CD2 . PHE A  1 168 ? -1.335  15.072  10.972  1.00 43.78  ? 168  PHE A CD2 1 
ATOM   934   C  CE1 . PHE A  1 168 ? -1.845  17.160  9.206   1.00 45.35  ? 168  PHE A CE1 1 
ATOM   935   C  CE2 . PHE A  1 168 ? -0.291  15.713  10.298  1.00 42.35  ? 168  PHE A CE2 1 
ATOM   936   C  CZ  . PHE A  1 168 ? -0.547  16.753  9.424   1.00 36.99  ? 168  PHE A CZ  1 
ATOM   937   N  N   . GLN A  1 169 ? -3.383  14.245  14.435  1.00 41.81  ? 169  GLN A N   1 
ATOM   938   C  CA  . GLN A  1 169 ? -2.624  13.987  15.650  1.00 40.68  ? 169  GLN A CA  1 
ATOM   939   C  C   . GLN A  1 169 ? -2.387  12.497  15.865  1.00 47.07  ? 169  GLN A C   1 
ATOM   940   O  O   . GLN A  1 169 ? -3.151  11.639  15.392  1.00 48.47  ? 169  GLN A O   1 
ATOM   941   C  CB  . GLN A  1 169 ? -3.352  14.561  16.857  1.00 40.20  ? 169  GLN A CB  1 
ATOM   942   C  CG  . GLN A  1 169 ? -4.736  13.967  17.031  1.00 46.01  ? 169  GLN A CG  1 
ATOM   943   C  CD  . GLN A  1 169 ? -5.451  14.514  18.247  1.00 54.81  ? 169  GLN A CD  1 
ATOM   944   O  OE1 . GLN A  1 169 ? -5.869  13.759  19.133  1.00 56.74  ? 169  GLN A OE1 1 
ATOM   945   N  NE2 . GLN A  1 169 ? -5.593  15.832  18.303  1.00 49.97  ? 169  GLN A NE2 1 
ATOM   946   N  N   . ALA A  1 170 ? -1.314  12.197  16.584  1.00 37.47  ? 170  ALA A N   1 
ATOM   947   C  CA  . ALA A  1 170 ? -1.010  10.830  16.947  1.00 36.84  ? 170  ALA A CA  1 
ATOM   948   C  C   . ALA A  1 170 ? 0.055   10.850  18.038  1.00 40.03  ? 170  ALA A C   1 
ATOM   949   O  O   . ALA A  1 170 ? 0.617   11.915  18.353  1.00 39.75  ? 170  ALA A O   1 
ATOM   950   C  CB  . ALA A  1 170 ? -0.543  10.034  15.733  1.00 34.01  ? 170  ALA A CB  1 
ATOM   951   N  N   . LYS A  1 171 ? 0.319   9.687   18.624  1.00 34.58  ? 171  LYS A N   1 
ATOM   952   C  CA  . LYS A  1 171 ? 1.482   9.543   19.491  1.00 42.12  ? 171  LYS A CA  1 
ATOM   953   C  C   . LYS A  1 171 ? 2.726   9.445   18.600  1.00 35.82  ? 171  LYS A C   1 
ATOM   954   O  O   . LYS A  1 171 ? 2.635   9.004   17.448  1.00 34.63  ? 171  LYS A O   1 
ATOM   955   C  CB  . LYS A  1 171 ? 1.339   8.324   20.424  1.00 34.63  ? 171  LYS A CB  1 
ATOM   956   C  CG  . LYS A  1 171 ? 0.347   8.583   21.597  1.00 53.76  ? 171  LYS A CG  1 
ATOM   957   C  CD  . LYS A  1 171 ? 0.706   7.837   22.901  1.00 65.35  ? 171  LYS A CD  1 
ATOM   958   C  CE  . LYS A  1 171 ? 0.405   8.663   24.169  1.00 64.94  ? 171  LYS A CE  1 
ATOM   959   N  NZ  . LYS A  1 171 ? -1.052  8.749   24.512  1.00 68.49  ? 171  LYS A NZ  1 
ATOM   960   N  N   . LEU A  1 172 ? 3.868   9.901   19.111  1.00 35.17  ? 172  LEU A N   1 
ATOM   961   C  CA  . LEU A  1 172 ? 5.136   9.647   18.437  1.00 37.75  ? 172  LEU A CA  1 
ATOM   962   C  C   . LEU A  1 172 ? 5.326   8.151   18.330  1.00 38.85  ? 172  LEU A C   1 
ATOM   963   O  O   . LEU A  1 172 ? 5.115   7.445   19.310  1.00 34.32  ? 172  LEU A O   1 
ATOM   964   C  CB  . LEU A  1 172 ? 6.308   10.264  19.187  1.00 33.13  ? 172  LEU A CB  1 
ATOM   965   C  CG  . LEU A  1 172 ? 6.490   11.764  19.027  1.00 34.70  ? 172  LEU A CG  1 
ATOM   966   C  CD1 . LEU A  1 172 ? 7.695   12.164  19.824  1.00 38.79  ? 172  LEU A CD1 1 
ATOM   967   C  CD2 . LEU A  1 172 ? 6.659   12.151  17.547  1.00 36.02  ? 172  LEU A CD2 1 
ATOM   968   N  N   . GLY A  1 173 ? 5.705   7.673   17.144  1.00 39.01  ? 173  GLY A N   1 
ATOM   969   C  CA  . GLY A  1 173 ? 5.968   6.260   16.945  1.00 39.05  ? 173  GLY A CA  1 
ATOM   970   C  C   . GLY A  1 173 ? 6.974   5.720   17.950  1.00 43.75  ? 173  GLY A C   1 
ATOM   971   O  O   . GLY A  1 173 ? 7.782   6.460   18.512  1.00 41.97  ? 173  GLY A O   1 
ATOM   972   N  N   . ASP A  1 174 ? 6.908   4.425   18.205  1.00 41.31  ? 174  ASP A N   1 
ATOM   973   C  CA  . ASP A  1 174 ? 7.892   3.791   19.056  1.00 46.51  ? 174  ASP A CA  1 
ATOM   974   C  C   . ASP A  1 174 ? 8.513   2.655   18.296  1.00 53.68  ? 174  ASP A C   1 
ATOM   975   O  O   . ASP A  1 174 ? 8.675   1.553   18.825  1.00 56.72  ? 174  ASP A O   1 
ATOM   976   C  CB  . ASP A  1 174 ? 7.264   3.273   20.339  1.00 46.59  ? 174  ASP A CB  1 
ATOM   977   C  CG  . ASP A  1 174 ? 6.065   2.410   20.071  1.00 56.26  ? 174  ASP A CG  1 
ATOM   978   O  OD1 . ASP A  1 174 ? 5.534   2.497   18.942  1.00 68.73  ? 174  ASP A OD1 1 
ATOM   979   O  OD2 . ASP A  1 174 ? 5.648   1.650   20.969  1.00 60.93  ? 174  ASP A OD2 1 
ATOM   980   N  N   . GLY A  1 175 ? 8.855   2.913   17.044  1.00 46.77  ? 175  GLY A N   1 
ATOM   981   C  CA  . GLY A  1 175 ? 9.408   1.864   16.235  1.00 36.75  ? 175  GLY A CA  1 
ATOM   982   C  C   . GLY A  1 175 ? 10.073  2.291   14.947  1.00 47.63  ? 175  GLY A C   1 
ATOM   983   O  O   . GLY A  1 175 ? 9.676   1.820   13.879  1.00 53.69  ? 175  GLY A O   1 
ATOM   984   N  N   . PHE A  1 176 ? 11.071  3.166   15.021  1.00 36.44  ? 176  PHE A N   1 
ATOM   985   C  CA  . PHE A  1 176 ? 11.967  3.311   13.881  1.00 45.11  ? 176  PHE A CA  1 
ATOM   986   C  C   . PHE A  1 176 ? 11.373  3.954   12.635  1.00 41.26  ? 176  PHE A C   1 
ATOM   987   O  O   . PHE A  1 176 ? 12.097  4.147   11.670  1.00 41.37  ? 176  PHE A O   1 
ATOM   988   C  CB  . PHE A  1 176 ? 12.502  1.935   13.437  1.00 48.91  ? 176  PHE A CB  1 
ATOM   989   C  CG  . PHE A  1 176 ? 13.556  1.349   14.330  1.00 56.10  ? 176  PHE A CG  1 
ATOM   990   C  CD1 . PHE A  1 176 ? 14.485  2.164   14.976  1.00 56.25  ? 176  PHE A CD1 1 
ATOM   991   C  CD2 . PHE A  1 176 ? 13.637  -0.038  14.497  1.00 54.15  ? 176  PHE A CD2 1 
ATOM   992   C  CE1 . PHE A  1 176 ? 15.478  1.609   15.785  1.00 55.07  ? 176  PHE A CE1 1 
ATOM   993   C  CE2 . PHE A  1 176 ? 14.625  -0.600  15.300  1.00 58.86  ? 176  PHE A CE2 1 
ATOM   994   C  CZ  . PHE A  1 176 ? 15.548  0.225   15.946  1.00 55.95  ? 176  PHE A CZ  1 
ATOM   995   N  N   . GLU A  1 177 ? 10.074  4.226   12.594  1.00 39.78  ? 177  GLU A N   1 
ATOM   996   C  CA  . GLU A  1 177 ? 9.529   4.778   11.357  1.00 42.82  ? 177  GLU A CA  1 
ATOM   997   C  C   . GLU A  1 177 ? 8.472   5.834   11.602  1.00 38.97  ? 177  GLU A C   1 
ATOM   998   O  O   . GLU A  1 177 ? 7.916   5.923   12.688  1.00 43.83  ? 177  GLU A O   1 
ATOM   999   C  CB  . GLU A  1 177 ? 8.967   3.661   10.468  1.00 42.62  ? 177  GLU A CB  1 
ATOM   1000  C  CG  . GLU A  1 177 ? 7.727   2.993   11.013  1.00 54.24  ? 177  GLU A CG  1 
ATOM   1001  C  CD  . GLU A  1 177 ? 7.358   1.695   10.292  1.00 57.59  ? 177  GLU A CD  1 
ATOM   1002  O  OE1 . GLU A  1 177 ? 7.802   1.455   9.144   1.00 60.12  ? 177  GLU A OE1 1 
ATOM   1003  O  OE2 . GLU A  1 177 ? 6.610   0.909   10.893  1.00 65.11  ? 177  GLU A OE2 1 
ATOM   1004  N  N   . GLY A  1 178 ? 8.217   6.648   10.582  1.00 34.95  ? 178  GLY A N   1 
ATOM   1005  C  CA  . GLY A  1 178 ? 7.278   7.748   10.691  1.00 32.11  ? 178  GLY A CA  1 
ATOM   1006  C  C   . GLY A  1 178 ? 7.945   8.828   11.496  1.00 31.12  ? 178  GLY A C   1 
ATOM   1007  O  O   . GLY A  1 178 ? 9.156   8.978   11.438  1.00 32.67  ? 178  GLY A O   1 
ATOM   1008  N  N   . PHE A  1 179 ? 7.154   9.569   12.257  1.00 36.23  ? 179  PHE A N   1 
ATOM   1009  C  CA  . PHE A  1 179 ? 7.677   10.553  13.192  1.00 31.32  ? 179  PHE A CA  1 
ATOM   1010  C  C   . PHE A  1 179 ? 7.770   9.821   14.517  1.00 33.46  ? 179  PHE A C   1 
ATOM   1011  O  O   . PHE A  1 179 ? 6.763   9.461   15.077  1.00 34.97  ? 179  PHE A O   1 
ATOM   1012  C  CB  . PHE A  1 179 ? 6.758   11.778  13.265  1.00 27.65  ? 179  PHE A CB  1 
ATOM   1013  C  CG  . PHE A  1 179 ? 7.350   12.953  14.009  1.00 36.41  ? 179  PHE A CG  1 
ATOM   1014  C  CD1 . PHE A  1 179 ? 8.725   13.093  14.148  1.00 31.94  ? 179  PHE A CD1 1 
ATOM   1015  C  CD2 . PHE A  1 179 ? 6.523   13.929  14.568  1.00 33.77  ? 179  PHE A CD2 1 
ATOM   1016  C  CE1 . PHE A  1 179 ? 9.261   14.175  14.833  1.00 32.12  ? 179  PHE A CE1 1 
ATOM   1017  C  CE2 . PHE A  1 179 ? 7.055   15.004  15.260  1.00 30.49  ? 179  PHE A CE2 1 
ATOM   1018  C  CZ  . PHE A  1 179 ? 8.423   15.129  15.395  1.00 34.69  ? 179  PHE A CZ  1 
ATOM   1019  N  N   . TYR A  1 180 ? 8.977   9.565   15.009  1.00 37.76  ? 180  TYR A N   1 
ATOM   1020  C  CA  . TYR A  1 180 ? 9.111   8.661   16.141  1.00 34.82  ? 180  TYR A CA  1 
ATOM   1021  C  C   . TYR A  1 180 ? 10.091  9.122   17.199  1.00 36.31  ? 180  TYR A C   1 
ATOM   1022  O  O   . TYR A  1 180 ? 10.994  9.918   16.930  1.00 35.24  ? 180  TYR A O   1 
ATOM   1023  C  CB  . TYR A  1 180 ? 9.518   7.265   15.647  1.00 31.93  ? 180  TYR A CB  1 
ATOM   1024  C  CG  . TYR A  1 180 ? 10.912  7.182   15.098  1.00 31.65  ? 180  TYR A CG  1 
ATOM   1025  C  CD1 . TYR A  1 180 ? 11.173  7.416   13.743  1.00 35.53  ? 180  TYR A CD1 1 
ATOM   1026  C  CD2 . TYR A  1 180 ? 11.974  6.877   15.925  1.00 28.76  ? 180  TYR A CD2 1 
ATOM   1027  C  CE1 . TYR A  1 180 ? 12.474  7.352   13.239  1.00 31.90  ? 180  TYR A CE1 1 
ATOM   1028  C  CE2 . TYR A  1 180 ? 13.261  6.802   15.442  1.00 34.29  ? 180  TYR A CE2 1 
ATOM   1029  C  CZ  . TYR A  1 180 ? 13.516  7.025   14.105  1.00 36.50  ? 180  TYR A CZ  1 
ATOM   1030  O  OH  . TYR A  1 180 ? 14.823  6.944   13.669  1.00 38.32  ? 180  TYR A OH  1 
ATOM   1031  N  N   . LYS A  1 181 ? 9.914   8.552   18.388  1.00 31.63  ? 181  LYS A N   1 
ATOM   1032  C  CA  . LYS A  1 181 ? 10.701  8.844   19.580  1.00 34.55  ? 181  LYS A CA  1 
ATOM   1033  C  C   . LYS A  1 181 ? 12.008  8.063   19.640  1.00 33.63  ? 181  LYS A C   1 
ATOM   1034  O  O   . LYS A  1 181 ? 12.063  6.903   19.259  1.00 34.20  ? 181  LYS A O   1 
ATOM   1035  C  CB  . LYS A  1 181 ? 9.862   8.538   20.827  1.00 40.63  ? 181  LYS A CB  1 
ATOM   1036  C  CG  . LYS A  1 181 ? 10.638  8.372   22.096  1.00 37.92  ? 181  LYS A CG  1 
ATOM   1037  C  CD  . LYS A  1 181 ? 10.018  7.300   22.956  1.00 51.50  ? 181  LYS A CD  1 
ATOM   1038  C  CE  . LYS A  1 181 ? 10.899  6.973   24.169  1.00 55.54  ? 181  LYS A CE  1 
ATOM   1039  N  NZ  . LYS A  1 181 ? 10.573  5.628   24.765  1.00 60.40  ? 181  LYS A NZ  1 
ATOM   1040  N  N   . SER A  1 182 ? 13.058  8.705   20.143  1.00 33.33  ? 182  SER A N   1 
ATOM   1041  C  CA  . SER A  1 182 ? 14.378  8.097   20.215  1.00 36.46  ? 182  SER A CA  1 
ATOM   1042  C  C   . SER A  1 182 ? 15.092  8.670   21.434  1.00 34.43  ? 182  SER A C   1 
ATOM   1043  O  O   . SER A  1 182 ? 14.783  9.773   21.872  1.00 35.80  ? 182  SER A O   1 
ATOM   1044  C  CB  . SER A  1 182 ? 15.180  8.363   18.925  1.00 36.46  ? 182  SER A CB  1 
ATOM   1045  O  OG  . SER A  1 182 ? 16.535  7.959   19.085  1.00 38.85  ? 182  SER A OG  1 
ATOM   1046  N  N   . THR A  1 183 ? 16.049  7.936   21.978  1.00 27.28  ? 183  THR A N   1 
ATOM   1047  C  CA  . THR A  1 183 ? 16.663  8.352   23.230  1.00 35.35  ? 183  THR A CA  1 
ATOM   1048  C  C   . THR A  1 183 ? 18.152  8.207   23.189  1.00 33.35  ? 183  THR A C   1 
ATOM   1049  O  O   . THR A  1 183 ? 18.664  7.406   22.459  1.00 34.38  ? 183  THR A O   1 
ATOM   1050  C  CB  . THR A  1 183 ? 16.169  7.518   24.434  1.00 40.94  ? 183  THR A CB  1 
ATOM   1051  O  OG1 . THR A  1 183 ? 16.466  6.126   24.201  1.00 47.04  ? 183  THR A OG1 1 
ATOM   1052  C  CG2 . THR A  1 183 ? 14.664  7.712   24.683  1.00 31.88  ? 183  THR A CG2 1 
ATOM   1053  N  N   . TYR A  1 184 ? 18.861  8.953   24.010  1.00 37.37  ? 184  TYR A N   1 
ATOM   1054  C  CA  . TYR A  1 184 ? 20.286  8.723   24.087  1.00 35.28  ? 184  TYR A CA  1 
ATOM   1055  C  C   . TYR A  1 184 ? 20.777  8.982   25.490  1.00 34.22  ? 184  TYR A C   1 
ATOM   1056  O  O   . TYR A  1 184 ? 20.057  9.542   26.298  1.00 34.29  ? 184  TYR A O   1 
ATOM   1057  C  CB  . TYR A  1 184 ? 21.025  9.592   23.093  1.00 32.22  ? 184  TYR A CB  1 
ATOM   1058  C  CG  . TYR A  1 184 ? 20.973  11.072  23.392  1.00 32.61  ? 184  TYR A CG  1 
ATOM   1059  C  CD1 . TYR A  1 184 ? 19.883  11.837  23.003  1.00 30.29  ? 184  TYR A CD1 1 
ATOM   1060  C  CD2 . TYR A  1 184 ? 22.023  11.702  24.049  1.00 28.07  ? 184  TYR A CD2 1 
ATOM   1061  C  CE1 . TYR A  1 184 ? 19.835  13.186  23.263  1.00 29.79  ? 184  TYR A CE1 1 
ATOM   1062  C  CE2 . TYR A  1 184 ? 21.992  13.055  24.295  1.00 30.95  ? 184  TYR A CE2 1 
ATOM   1063  C  CZ  . TYR A  1 184 ? 20.894  13.792  23.905  1.00 34.96  ? 184  TYR A CZ  1 
ATOM   1064  O  OH  . TYR A  1 184 ? 20.852  15.145  24.173  1.00 39.75  ? 184  TYR A OH  1 
ATOM   1065  N  N   . ARG A  1 185 ? 22.010  8.561   25.747  1.00 38.38  ? 185  ARG A N   1 
ATOM   1066  C  CA  . ARG A  1 185 ? 22.649  8.629   27.059  1.00 43.51  ? 185  ARG A CA  1 
ATOM   1067  C  C   . ARG A  1 185 ? 23.752  9.699   27.086  1.00 42.67  ? 185  ARG A C   1 
ATOM   1068  O  O   . ARG A  1 185 ? 24.524  9.829   26.144  1.00 43.41  ? 185  ARG A O   1 
ATOM   1069  C  CB  . ARG A  1 185 ? 23.235  7.261   27.424  1.00 44.04  ? 185  ARG A CB  1 
ATOM   1070  C  CG  . ARG A  1 185 ? 23.935  7.231   28.769  1.00 54.75  ? 185  ARG A CG  1 
ATOM   1071  C  CD  . ARG A  1 185 ? 24.435  5.842   29.136  1.00 53.63  ? 185  ARG A CD  1 
ATOM   1072  N  NE  . ARG A  1 185 ? 24.899  5.784   30.527  1.00 65.77  ? 185  ARG A NE  1 
ATOM   1073  C  CZ  . ARG A  1 185 ? 26.104  6.172   30.959  1.00 64.72  ? 185  ARG A CZ  1 
ATOM   1074  N  NH1 . ARG A  1 185 ? 27.014  6.665   30.116  1.00 54.19  ? 185  ARG A NH1 1 
ATOM   1075  N  NH2 . ARG A  1 185 ? 26.402  6.063   32.252  1.00 62.21  ? 185  ARG A NH2 1 
ATOM   1076  N  N   . THR A  1 186 ? 23.825  10.483  28.150  1.00 41.11  ? 186  THR A N   1 
ATOM   1077  C  CA  . THR A  1 186 ? 24.871  11.496  28.222  1.00 38.20  ? 186  THR A CA  1 
ATOM   1078  C  C   . THR A  1 186 ? 26.068  10.920  28.947  1.00 39.86  ? 186  THR A C   1 
ATOM   1079  O  O   . THR A  1 186 ? 26.050  9.771   29.394  1.00 35.02  ? 186  THR A O   1 
ATOM   1080  C  CB  . THR A  1 186 ? 24.404  12.751  28.938  1.00 38.05  ? 186  THR A CB  1 
ATOM   1081  O  OG1 . THR A  1 186 ? 24.229  12.457  30.328  1.00 46.02  ? 186  THR A OG1 1 
ATOM   1082  C  CG2 . THR A  1 186 ? 23.068  13.242  28.368  1.00 39.08  ? 186  THR A CG2 1 
ATOM   1083  N  N   . LEU A  1 187 ? 27.120  11.714  29.054  1.00 43.26  ? 187  LEU A N   1 
ATOM   1084  C  CA  . LEU A  1 187 ? 28.315  11.275  29.767  1.00 43.90  ? 187  LEU A CA  1 
ATOM   1085  C  C   . LEU A  1 187 ? 28.050  11.220  31.264  1.00 42.48  ? 187  LEU A C   1 
ATOM   1086  O  O   . LEU A  1 187 ? 28.688  10.463  31.993  1.00 44.31  ? 187  LEU A O   1 
ATOM   1087  C  CB  . LEU A  1 187 ? 29.485  12.208  29.475  1.00 44.92  ? 187  LEU A CB  1 
ATOM   1088  C  CG  . LEU A  1 187 ? 30.780  11.901  30.219  1.00 40.44  ? 187  LEU A CG  1 
ATOM   1089  C  CD1 . LEU A  1 187 ? 31.327  10.560  29.803  1.00 40.85  ? 187  LEU A CD1 1 
ATOM   1090  C  CD2 . LEU A  1 187 ? 31.788  12.990  29.968  1.00 38.40  ? 187  LEU A CD2 1 
ATOM   1091  N  N   . GLY A  1 188 ? 27.097  12.034  31.709  1.00 44.46  ? 188  GLY A N   1 
ATOM   1092  C  CA  . GLY A  1 188 ? 26.694  12.084  33.104  1.00 41.60  ? 188  GLY A CA  1 
ATOM   1093  C  C   . GLY A  1 188 ? 25.833  10.889  33.483  1.00 48.15  ? 188  GLY A C   1 
ATOM   1094  O  O   . GLY A  1 188 ? 25.761  10.503  34.653  1.00 46.77  ? 188  GLY A O   1 
ATOM   1095  N  N   . GLY A  1 189 ? 25.188  10.283  32.494  1.00 42.36  ? 189  GLY A N   1 
ATOM   1096  C  CA  . GLY A  1 189 ? 24.357  9.120   32.742  1.00 38.86  ? 189  GLY A CA  1 
ATOM   1097  C  C   . GLY A  1 189 ? 22.916  9.525   32.584  1.00 39.89  ? 189  GLY A C   1 
ATOM   1098  O  O   . GLY A  1 189 ? 21.994  8.806   32.945  1.00 46.61  ? 189  GLY A O   1 
ATOM   1099  N  N   . GLU A  1 190 ? 22.718  10.713  32.048  1.00 41.29  ? 190  GLU A N   1 
ATOM   1100  C  CA  . GLU A  1 190 ? 21.368  11.186  31.827  1.00 48.74  ? 190  GLU A CA  1 
ATOM   1101  C  C   . GLU A  1 190 ? 20.804  10.535  30.571  1.00 44.16  ? 190  GLU A C   1 
ATOM   1102  O  O   . GLU A  1 190 ? 21.542  9.992   29.757  1.00 47.41  ? 190  GLU A O   1 
ATOM   1103  C  CB  . GLU A  1 190 ? 21.345  12.713  31.730  1.00 43.65  ? 190  GLU A CB  1 
ATOM   1104  C  CG  . GLU A  1 190 ? 22.049  13.396  32.918  1.00 43.05  ? 190  GLU A CG  1 
ATOM   1105  C  CD  . GLU A  1 190 ? 21.747  14.886  33.024  1.00 49.73  ? 190  GLU A CD  1 
ATOM   1106  O  OE1 . GLU A  1 190 ? 20.581  15.282  32.789  1.00 49.77  ? 190  GLU A OE1 1 
ATOM   1107  O  OE2 . GLU A  1 190 ? 22.684  15.664  33.343  1.00 54.81  ? 190  GLU A OE2 1 
ATOM   1108  N  N   . THR A  1 191 ? 19.492  10.589  30.435  1.00 38.83  ? 191  THR A N   1 
ATOM   1109  C  CA  . THR A  1 191 ? 18.790  10.000  29.322  1.00 38.52  ? 191  THR A CA  1 
ATOM   1110  C  C   . THR A  1 191 ? 17.971  11.098  28.677  1.00 41.96  ? 191  THR A C   1 
ATOM   1111  O  O   . THR A  1 191 ? 17.113  11.677  29.328  1.00 47.21  ? 191  THR A O   1 
ATOM   1112  C  CB  . THR A  1 191 ? 17.871  8.841   29.785  1.00 48.57  ? 191  THR A CB  1 
ATOM   1113  O  OG1 . THR A  1 191 ? 18.671  7.740   30.231  1.00 47.53  ? 191  THR A OG1 1 
ATOM   1114  C  CG2 . THR A  1 191 ? 16.981  8.366   28.662  1.00 48.98  ? 191  THR A CG2 1 
ATOM   1115  N  N   . ARG A  1 192 ? 18.226  11.414  27.412  1.00 45.35  ? 192  ARG A N   1 
ATOM   1116  C  CA  . ARG A  1 192 ? 17.427  12.450  26.759  1.00 40.51  ? 192  ARG A CA  1 
ATOM   1117  C  C   . ARG A  1 192 ? 16.591  11.908  25.624  1.00 35.08  ? 192  ARG A C   1 
ATOM   1118  O  O   . ARG A  1 192 ? 16.841  10.823  25.119  1.00 39.04  ? 192  ARG A O   1 
ATOM   1119  C  CB  . ARG A  1 192 ? 18.306  13.568  26.237  1.00 42.94  ? 192  ARG A CB  1 
ATOM   1120  C  CG  . ARG A  1 192 ? 19.287  14.078  27.234  1.00 44.09  ? 192  ARG A CG  1 
ATOM   1121  C  CD  . ARG A  1 192 ? 18.895  15.428  27.777  1.00 48.03  ? 192  ARG A CD  1 
ATOM   1122  N  NE  . ARG A  1 192 ? 19.851  15.818  28.810  1.00 53.53  ? 192  ARG A NE  1 
ATOM   1123  C  CZ  . ARG A  1 192 ? 21.019  16.405  28.561  1.00 53.15  ? 192  ARG A CZ  1 
ATOM   1124  N  NH1 . ARG A  1 192 ? 21.367  16.703  27.307  1.00 49.47  ? 192  ARG A NH1 1 
ATOM   1125  N  NH2 . ARG A  1 192 ? 21.831  16.705  29.566  1.00 46.48  ? 192  ARG A NH2 1 
ATOM   1126  N  N   . ILE A  1 193 ? 15.610  12.688  25.203  1.00 35.56  ? 193  ILE A N   1 
ATOM   1127  C  CA  . ILE A  1 193 ? 14.706  12.256  24.153  1.00 35.84  ? 193  ILE A CA  1 
ATOM   1128  C  C   . ILE A  1 193 ? 14.819  13.160  22.933  1.00 35.30  ? 193  ILE A C   1 
ATOM   1129  O  O   . ILE A  1 193 ? 15.088  14.358  23.048  1.00 37.91  ? 193  ILE A O   1 
ATOM   1130  C  CB  . ILE A  1 193 ? 13.261  12.213  24.680  1.00 32.31  ? 193  ILE A CB  1 
ATOM   1131  C  CG1 . ILE A  1 193 ? 13.067  10.973  25.533  1.00 38.76  ? 193  ILE A CG1 1 
ATOM   1132  C  CG2 . ILE A  1 193 ? 12.252  12.128  23.572  1.00 37.15  ? 193  ILE A CG2 1 
ATOM   1133  C  CD1 . ILE A  1 193 ? 11.893  11.104  26.468  1.00 49.18  ? 193  ILE A CD1 1 
ATOM   1134  N  N   . LEU A  1 194 ? 14.665  12.575  21.753  1.00 35.36  ? 194  LEU A N   1 
ATOM   1135  C  CA  . LEU A  1 194 ? 14.475  13.366  20.545  1.00 32.93  ? 194  LEU A CA  1 
ATOM   1136  C  C   . LEU A  1 194 ? 13.327  12.764  19.777  1.00 32.48  ? 194  LEU A C   1 
ATOM   1137  O  O   . LEU A  1 194 ? 12.944  11.623  20.008  1.00 29.33  ? 194  LEU A O   1 
ATOM   1138  C  CB  . LEU A  1 194 ? 15.740  13.412  19.679  1.00 28.04  ? 194  LEU A CB  1 
ATOM   1139  C  CG  . LEU A  1 194 ? 16.262  12.069  19.119  1.00 36.90  ? 194  LEU A CG  1 
ATOM   1140  C  CD1 . LEU A  1 194 ? 16.993  12.248  17.796  1.00 33.39  ? 194  LEU A CD1 1 
ATOM   1141  C  CD2 . LEU A  1 194 ? 17.168  11.350  20.109  1.00 35.88  ? 194  LEU A CD2 1 
ATOM   1142  N  N   . ALA A  1 195 ? 12.768  13.556  18.878  1.00 32.28  ? 195  ALA A N   1 
ATOM   1143  C  CA  . ALA A  1 195 ? 11.799  13.066  17.921  1.00 32.45  ? 195  ALA A CA  1 
ATOM   1144  C  C   . ALA A  1 195 ? 12.374  13.262  16.530  1.00 31.05  ? 195  ALA A C   1 
ATOM   1145  O  O   . ALA A  1 195 ? 12.865  14.360  16.197  1.00 27.45  ? 195  ALA A O   1 
ATOM   1146  C  CB  . ALA A  1 195 ? 10.481  13.797  18.064  1.00 41.56  ? 195  ALA A CB  1 
ATOM   1147  N  N   . VAL A  1 196 ? 12.322  12.201  15.729  1.00 30.28  ? 196  VAL A N   1 
ATOM   1148  C  CA  . VAL A  1 196 ? 12.923  12.228  14.406  1.00 30.04  ? 196  VAL A CA  1 
ATOM   1149  C  C   . VAL A  1 196 ? 12.001  11.550  13.385  1.00 28.71  ? 196  VAL A C   1 
ATOM   1150  O  O   . VAL A  1 196 ? 11.140  10.757  13.739  1.00 31.04  ? 196  VAL A O   1 
ATOM   1151  C  CB  . VAL A  1 196 ? 14.330  11.583  14.448  1.00 29.38  ? 196  VAL A CB  1 
ATOM   1152  C  CG1 . VAL A  1 196 ? 14.265  10.212  15.042  1.00 31.40  ? 196  VAL A CG1 1 
ATOM   1153  C  CG2 . VAL A  1 196 ? 14.983  11.571  13.074  1.00 30.22  ? 196  VAL A CG2 1 
ATOM   1154  N  N   . THR A  1 197 ? 12.139  11.939  12.128  1.00 27.54  ? 197  THR A N   1 
ATOM   1155  C  CA  . THR A  1 197 ? 11.397  11.346  11.029  1.00 30.70  ? 197  THR A CA  1 
ATOM   1156  C  C   . THR A  1 197 ? 12.234  10.371  10.216  1.00 29.52  ? 197  THR A C   1 
ATOM   1157  O  O   . THR A  1 197 ? 13.439  10.557  10.072  1.00 24.72  ? 197  THR A O   1 
ATOM   1158  C  CB  . THR A  1 197 ? 10.891  12.420  10.061  1.00 31.74  ? 197  THR A CB  1 
ATOM   1159  O  OG1 . THR A  1 197 ? 12.012  13.192  9.632   1.00 30.49  ? 197  THR A OG1 1 
ATOM   1160  C  CG2 . THR A  1 197 ? 9.876   13.336  10.730  1.00 27.92  ? 197  THR A CG2 1 
ATOM   1161  N  N   . ASP A  1 198 ? 11.576  9.345   9.681   1.00 29.50  ? 198  ASP A N   1 
ATOM   1162  C  CA  . ASP A  1 198 ? 12.150  8.474   8.647   1.00 27.29  ? 198  ASP A CA  1 
ATOM   1163  C  C   . ASP A  1 198 ? 11.034  7.902   7.797   1.00 28.29  ? 198  ASP A C   1 
ATOM   1164  O  O   . ASP A  1 198 ? 10.198  7.130   8.260   1.00 31.87  ? 198  ASP A O   1 
ATOM   1165  C  CB  . ASP A  1 198 ? 12.984  7.337   9.241   1.00 30.13  ? 198  ASP A CB  1 
ATOM   1166  C  CG  . ASP A  1 198 ? 13.712  6.558   8.179   1.00 35.03  ? 198  ASP A CG  1 
ATOM   1167  O  OD1 . ASP A  1 198 ? 14.617  7.141   7.536   1.00 38.25  ? 198  ASP A OD1 1 
ATOM   1168  O  OD2 . ASP A  1 198 ? 13.377  5.375   7.958   1.00 41.68  ? 198  ASP A OD2 1 
ATOM   1169  N  N   . PHE A  1 199 ? 11.027  8.283   6.535   1.00 29.49  ? 199  PHE A N   1 
ATOM   1170  C  CA  . PHE A  1 199 ? 9.837   8.084   5.731   1.00 33.66  ? 199  PHE A CA  1 
ATOM   1171  C  C   . PHE A  1 199 ? 9.992   7.096   4.591   1.00 31.56  ? 199  PHE A C   1 
ATOM   1172  O  O   . PHE A  1 199 ? 8.993   6.549   4.137   1.00 34.08  ? 199  PHE A O   1 
ATOM   1173  C  CB  . PHE A  1 199 ? 9.363   9.433   5.173   1.00 26.24  ? 199  PHE A CB  1 
ATOM   1174  C  CG  . PHE A  1 199 ? 8.842   10.367  6.230   1.00 28.11  ? 199  PHE A CG  1 
ATOM   1175  C  CD1 . PHE A  1 199 ? 8.412   9.883   7.443   1.00 25.97  ? 199  PHE A CD1 1 
ATOM   1176  C  CD2 . PHE A  1 199 ? 8.759   11.732  5.993   1.00 26.65  ? 199  PHE A CD2 1 
ATOM   1177  C  CE1 . PHE A  1 199 ? 7.924   10.749  8.404   1.00 28.28  ? 199  PHE A CE1 1 
ATOM   1178  C  CE2 . PHE A  1 199 ? 8.259   12.590  6.947   1.00 29.96  ? 199  PHE A CE2 1 
ATOM   1179  C  CZ  . PHE A  1 199 ? 7.846   12.100  8.151   1.00 29.24  ? 199  PHE A CZ  1 
ATOM   1180  N  N   . GLU A  1 200 ? 11.212  6.883   4.108   1.00 25.74  ? 200  GLU A N   1 
ATOM   1181  C  CA  . GLU A  1 200 ? 11.373  6.056   2.919   1.00 30.69  ? 200  GLU A CA  1 
ATOM   1182  C  C   . GLU A  1 200 ? 11.132  4.593   3.273   1.00 36.42  ? 200  GLU A C   1 
ATOM   1183  O  O   . GLU A  1 200 ? 11.631  4.119   4.297   1.00 32.57  ? 200  GLU A O   1 
ATOM   1184  C  CB  . GLU A  1 200 ? 12.757  6.240   2.279   1.00 28.99  ? 200  GLU A CB  1 
ATOM   1185  C  CG  . GLU A  1 200 ? 12.806  5.689   0.845   1.00 30.68  ? 200  GLU A CG  1 
ATOM   1186  C  CD  . GLU A  1 200 ? 14.210  5.651   0.240   1.00 35.52  ? 200  GLU A CD  1 
ATOM   1187  O  OE1 . GLU A  1 200 ? 15.175  5.714   1.029   1.00 37.20  ? 200  GLU A OE1 1 
ATOM   1188  O  OE2 . GLU A  1 200 ? 14.356  5.559   -1.012  1.00 28.27  ? 200  GLU A OE2 1 
ATOM   1189  N  N   . PRO A  1 201 ? 10.352  3.872   2.439   1.00 37.22  ? 201  PRO A N   1 
ATOM   1190  C  CA  . PRO A  1 201 ? 9.671   4.318   1.213   1.00 33.87  ? 201  PRO A CA  1 
ATOM   1191  C  C   . PRO A  1 201 ? 8.300   4.949   1.403   1.00 36.37  ? 201  PRO A C   1 
ATOM   1192  O  O   . PRO A  1 201 ? 7.962   5.874   0.670   1.00 35.79  ? 201  PRO A O   1 
ATOM   1193  C  CB  . PRO A  1 201 ? 9.493   3.022   0.414   1.00 28.11  ? 201  PRO A CB  1 
ATOM   1194  C  CG  . PRO A  1 201 ? 10.261  1.987   1.152   1.00 31.63  ? 201  PRO A CG  1 
ATOM   1195  C  CD  . PRO A  1 201 ? 10.312  2.409   2.560   1.00 32.13  ? 201  PRO A CD  1 
ATOM   1196  N  N   . THR A  1 202 ? 7.500   4.425   2.323   1.00 32.39  ? 202  THR A N   1 
ATOM   1197  C  CA  . THR A  1 202 ? 6.083   4.760   2.333   1.00 33.60  ? 202  THR A CA  1 
ATOM   1198  C  C   . THR A  1 202 ? 5.593   5.122   3.704   1.00 33.21  ? 202  THR A C   1 
ATOM   1199  O  O   . THR A  1 202 ? 4.461   4.804   4.045   1.00 33.89  ? 202  THR A O   1 
ATOM   1200  C  CB  . THR A  1 202 ? 5.198   3.582   1.819   1.00 37.62  ? 202  THR A CB  1 
ATOM   1201  O  OG1 . THR A  1 202 ? 5.162   2.532   2.803   1.00 41.86  ? 202  THR A OG1 1 
ATOM   1202  C  CG2 . THR A  1 202 ? 5.729   3.036   0.533   1.00 27.15  ? 202  THR A CG2 1 
ATOM   1203  N  N   . GLN A  1 203 ? 6.428   5.781   4.501   1.00 33.92  ? 203  GLN A N   1 
ATOM   1204  C  CA  . GLN A  1 203 ? 6.010   6.080   5.865   1.00 34.43  ? 203  GLN A CA  1 
ATOM   1205  C  C   . GLN A  1 203 ? 5.692   7.559   6.121   1.00 33.04  ? 203  GLN A C   1 
ATOM   1206  O  O   . GLN A  1 203 ? 5.292   7.900   7.240   1.00 33.31  ? 203  GLN A O   1 
ATOM   1207  C  CB  . GLN A  1 203 ? 7.069   5.609   6.867   1.00 36.91  ? 203  GLN A CB  1 
ATOM   1208  C  CG  . GLN A  1 203 ? 7.078   4.112   7.100   1.00 37.08  ? 203  GLN A CG  1 
ATOM   1209  C  CD  . GLN A  1 203 ? 7.778   3.359   5.996   1.00 41.03  ? 203  GLN A CD  1 
ATOM   1210  O  OE1 . GLN A  1 203 ? 8.888   3.715   5.605   1.00 41.90  ? 203  GLN A OE1 1 
ATOM   1211  N  NE2 . GLN A  1 203 ? 7.131   2.312   5.475   1.00 41.89  ? 203  GLN A NE2 1 
ATOM   1212  N  N   . ALA A  1 204 ? 5.869   8.431   5.123   1.00 26.09  ? 204  ALA A N   1 
ATOM   1213  C  CA  . ALA A  1 204 ? 5.523   9.852   5.335   1.00 32.12  ? 204  ALA A CA  1 
ATOM   1214  C  C   . ALA A  1 204 ? 4.054   9.977   5.740   1.00 32.35  ? 204  ALA A C   1 
ATOM   1215  O  O   . ALA A  1 204 ? 3.686   10.849  6.539   1.00 33.88  ? 204  ALA A O   1 
ATOM   1216  C  CB  . ALA A  1 204 ? 5.803   10.695  4.088   1.00 25.11  ? 204  ALA A CB  1 
ATOM   1217  N  N   . ARG A  1 205 ? 3.250   9.053   5.217   1.00 26.65  ? 205  ARG A N   1 
ATOM   1218  C  CA  . ARG A  1 205 ? 1.819   8.990   5.444   1.00 31.99  ? 205  ARG A CA  1 
ATOM   1219  C  C   . ARG A  1 205 ? 1.519   8.666   6.908   1.00 31.19  ? 205  ARG A C   1 
ATOM   1220  O  O   . ARG A  1 205 ? 0.400   8.842   7.375   1.00 32.91  ? 205  ARG A O   1 
ATOM   1221  C  CB  . ARG A  1 205 ? 1.183   7.946   4.507   1.00 35.13  ? 205  ARG A CB  1 
ATOM   1222  C  CG  . ARG A  1 205 ? 1.674   6.515   4.765   1.00 37.36  ? 205  ARG A CG  1 
ATOM   1223  C  CD  . ARG A  1 205 ? 1.245   5.490   3.700   1.00 37.05  ? 205  ARG A CD  1 
ATOM   1224  N  NE  . ARG A  1 205 ? 1.781   5.769   2.369   1.00 38.37  ? 205  ARG A NE  1 
ATOM   1225  C  CZ  . ARG A  1 205 ? 1.787   4.886   1.368   1.00 34.27  ? 205  ARG A CZ  1 
ATOM   1226  N  NH1 . ARG A  1 205 ? 1.307   3.688   1.557   1.00 27.48  ? 205  ARG A NH1 1 
ATOM   1227  N  NH2 . ARG A  1 205 ? 2.268   5.198   0.175   1.00 34.33  ? 205  ARG A NH2 1 
ATOM   1228  N  N   . MET A  1 206 ? 2.520   8.193   7.635   1.00 29.42  ? 206  MET A N   1 
ATOM   1229  C  CA  . MET A  1 206 ? 2.348   7.972   9.069   1.00 37.31  ? 206  MET A CA  1 
ATOM   1230  C  C   . MET A  1 206 ? 2.580   9.232   9.873   1.00 37.13  ? 206  MET A C   1 
ATOM   1231  O  O   . MET A  1 206 ? 2.419   9.212   11.092  1.00 40.84  ? 206  MET A O   1 
ATOM   1232  C  CB  . MET A  1 206 ? 3.299   6.889   9.598   1.00 38.50  ? 206  MET A CB  1 
ATOM   1233  C  CG  . MET A  1 206 ? 3.188   5.542   8.915   1.00 39.58  ? 206  MET A CG  1 
ATOM   1234  S  SD  . MET A  1 206 ? 4.328   4.331   9.614   1.00 47.33  ? 206  MET A SD  1 
ATOM   1235  C  CE  . MET A  1 206 ? 3.310   3.612   10.900  1.00 52.56  ? 206  MET A CE  1 
ATOM   1236  N  N   . ALA A  1 207 ? 2.997   10.310  9.208   1.00 37.88  ? 207  ALA A N   1 
ATOM   1237  C  CA  . ALA A  1 207 ? 3.333   11.540  9.918   1.00 39.13  ? 207  ALA A CA  1 
ATOM   1238  C  C   . ALA A  1 207 ? 2.393   12.692  9.569   1.00 39.55  ? 207  ALA A C   1 
ATOM   1239  O  O   . ALA A  1 207 ? 2.129   13.552  10.396  1.00 36.45  ? 207  ALA A O   1 
ATOM   1240  C  CB  . ALA A  1 207 ? 4.763   11.928  9.639   1.00 28.94  ? 207  ALA A CB  1 
ATOM   1241  N  N   . PHE A  1 208 ? 1.891   12.687  8.343   1.00 35.26  ? 208  PHE A N   1 
ATOM   1242  C  CA  . PHE A  1 208 ? 0.946   13.688  7.891   1.00 36.28  ? 208  PHE A CA  1 
ATOM   1243  C  C   . PHE A  1 208 ? 0.280   13.125  6.662   1.00 40.50  ? 208  PHE A C   1 
ATOM   1244  O  O   . PHE A  1 208 ? 0.929   12.423  5.897   1.00 39.29  ? 208  PHE A O   1 
ATOM   1245  C  CB  . PHE A  1 208 ? 1.636   15.023  7.586   1.00 39.65  ? 208  PHE A CB  1 
ATOM   1246  C  CG  . PHE A  1 208 ? 2.732   14.930  6.565   1.00 34.14  ? 208  PHE A CG  1 
ATOM   1247  C  CD1 . PHE A  1 208 ? 4.011   14.536  6.932   1.00 34.99  ? 208  PHE A CD1 1 
ATOM   1248  C  CD2 . PHE A  1 208 ? 2.486   15.235  5.249   1.00 33.12  ? 208  PHE A CD2 1 
ATOM   1249  C  CE1 . PHE A  1 208 ? 5.024   14.435  5.987   1.00 31.43  ? 208  PHE A CE1 1 
ATOM   1250  C  CE2 . PHE A  1 208 ? 3.488   15.157  4.301   1.00 36.79  ? 208  PHE A CE2 1 
ATOM   1251  C  CZ  . PHE A  1 208 ? 4.764   14.755  4.665   1.00 34.22  ? 208  PHE A CZ  1 
ATOM   1252  N  N   . PRO A  1 209 ? -1.021  13.402  6.473   1.00 40.16  ? 209  PRO A N   1 
ATOM   1253  C  CA  . PRO A  1 209 ? -1.714  12.867  5.297   1.00 33.10  ? 209  PRO A CA  1 
ATOM   1254  C  C   . PRO A  1 209 ? -1.113  13.488  4.056   1.00 40.82  ? 209  PRO A C   1 
ATOM   1255  O  O   . PRO A  1 209 ? -0.784  14.669  4.119   1.00 40.88  ? 209  PRO A O   1 
ATOM   1256  C  CB  . PRO A  1 209 ? -3.167  13.309  5.495   1.00 34.74  ? 209  PRO A CB  1 
ATOM   1257  C  CG  . PRO A  1 209 ? -3.268  13.776  6.872   1.00 40.14  ? 209  PRO A CG  1 
ATOM   1258  C  CD  . PRO A  1 209 ? -1.909  14.187  7.337   1.00 39.39  ? 209  PRO A CD  1 
ATOM   1259  N  N   . CYS A  1 210 ? -0.955  12.738  2.968   1.00 39.45  ? 210  CYS A N   1 
ATOM   1260  C  CA  . CYS A  1 210 ? -0.334  13.286  1.757   1.00 35.09  ? 210  CYS A CA  1 
ATOM   1261  C  C   . CYS A  1 210 ? -0.475  12.317  0.603   1.00 36.47  ? 210  CYS A C   1 
ATOM   1262  O  O   . CYS A  1 210 ? -0.967  11.215  0.770   1.00 35.60  ? 210  CYS A O   1 
ATOM   1263  C  CB  . CYS A  1 210 ? 1.159   13.598  1.988   1.00 36.90  ? 210  CYS A CB  1 
ATOM   1264  S  SG  . CYS A  1 210 ? 2.214   12.181  2.625   1.00 36.20  ? 210  CYS A SG  1 
ATOM   1265  N  N   . PHE A  1 211 ? -0.019  12.745  -0.566  1.00 41.98  ? 211  PHE A N   1 
ATOM   1266  C  CA  . PHE A  1 211 ? 0.054   11.898  -1.749  1.00 41.49  ? 211  PHE A CA  1 
ATOM   1267  C  C   . PHE A  1 211 ? 1.383   11.165  -1.710  1.00 40.49  ? 211  PHE A C   1 
ATOM   1268  O  O   . PHE A  1 211 ? 2.344   11.577  -2.357  1.00 34.64  ? 211  PHE A O   1 
ATOM   1269  C  CB  . PHE A  1 211 ? -0.068  12.729  -3.038  1.00 41.05  ? 211  PHE A CB  1 
ATOM   1270  C  CG  . PHE A  1 211 ? -1.317  13.562  -3.103  1.00 45.34  ? 211  PHE A CG  1 
ATOM   1271  C  CD1 . PHE A  1 211 ? -1.380  14.804  -2.472  1.00 41.70  ? 211  PHE A CD1 1 
ATOM   1272  C  CD2 . PHE A  1 211 ? -2.432  13.107  -3.792  1.00 46.65  ? 211  PHE A CD2 1 
ATOM   1273  C  CE1 . PHE A  1 211 ? -2.530  15.564  -2.517  1.00 43.79  ? 211  PHE A CE1 1 
ATOM   1274  C  CE2 . PHE A  1 211 ? -3.595  13.872  -3.848  1.00 44.34  ? 211  PHE A CE2 1 
ATOM   1275  C  CZ  . PHE A  1 211 ? -3.644  15.102  -3.206  1.00 45.49  ? 211  PHE A CZ  1 
ATOM   1276  N  N   . ASP A  1 212 ? 1.439   10.089  -0.934  1.00 37.34  ? 212  ASP A N   1 
ATOM   1277  C  CA  . ASP A  1 212 ? 2.708   9.425   -0.657  1.00 36.92  ? 212  ASP A CA  1 
ATOM   1278  C  C   . ASP A  1 212 ? 3.204   8.501   -1.786  1.00 36.31  ? 212  ASP A C   1 
ATOM   1279  O  O   . ASP A  1 212 ? 3.281   7.285   -1.609  1.00 40.82  ? 212  ASP A O   1 
ATOM   1280  C  CB  . ASP A  1 212 ? 2.591   8.629   0.646   1.00 38.65  ? 212  ASP A CB  1 
ATOM   1281  C  CG  . ASP A  1 212 ? 3.906   8.519   1.378   1.00 35.45  ? 212  ASP A CG  1 
ATOM   1282  O  OD1 . ASP A  1 212 ? 4.903   9.011   0.833   1.00 38.33  ? 212  ASP A OD1 1 
ATOM   1283  O  OD2 . ASP A  1 212 ? 3.949   7.947   2.490   1.00 33.91  ? 212  ASP A OD2 1 
ATOM   1284  N  N   . GLU A  1 213 ? 3.544   9.082   -2.931  1.00 32.27  ? 213  GLU A N   1 
ATOM   1285  C  CA  . GLU A  1 213 ? 4.214   8.368   -4.017  1.00 33.24  ? 213  GLU A CA  1 
ATOM   1286  C  C   . GLU A  1 213 ? 5.226   9.314   -4.659  1.00 34.25  ? 213  GLU A C   1 
ATOM   1287  O  O   . GLU A  1 213 ? 4.944   10.482  -4.864  1.00 39.31  ? 213  GLU A O   1 
ATOM   1288  C  CB  . GLU A  1 213 ? 3.223   7.866   -5.075  1.00 34.97  ? 213  GLU A CB  1 
ATOM   1289  C  CG  . GLU A  1 213 ? 2.037   7.026   -4.566  1.00 39.37  ? 213  GLU A CG  1 
ATOM   1290  C  CD  . GLU A  1 213 ? 1.157   6.504   -5.709  1.00 41.81  ? 213  GLU A CD  1 
ATOM   1291  O  OE1 . GLU A  1 213 ? 1.509   6.737   -6.886  1.00 44.87  ? 213  GLU A OE1 1 
ATOM   1292  O  OE2 . GLU A  1 213 ? 0.122   5.854   -5.444  1.00 43.58  ? 213  GLU A OE2 1 
ATOM   1293  N  N   . PRO A  1 214 ? 6.401   8.806   -5.007  1.00 35.37  ? 214  PRO A N   1 
ATOM   1294  C  CA  . PRO A  1 214 ? 7.525   9.647   -5.435  1.00 36.81  ? 214  PRO A CA  1 
ATOM   1295  C  C   . PRO A  1 214 ? 7.269   10.588  -6.628  1.00 38.41  ? 214  PRO A C   1 
ATOM   1296  O  O   . PRO A  1 214 ? 7.924   11.619  -6.712  1.00 37.66  ? 214  PRO A O   1 
ATOM   1297  C  CB  . PRO A  1 214 ? 8.587   8.624   -5.817  1.00 37.31  ? 214  PRO A CB  1 
ATOM   1298  C  CG  . PRO A  1 214 ? 8.214   7.406   -5.079  1.00 39.31  ? 214  PRO A CG  1 
ATOM   1299  C  CD  . PRO A  1 214 ? 6.748   7.377   -4.985  1.00 30.51  ? 214  PRO A CD  1 
ATOM   1300  N  N   . LEU A  1 215 ? 6.366   10.242  -7.537  1.00 37.41  ? 215  LEU A N   1 
ATOM   1301  C  CA  . LEU A  1 215 ? 6.093   11.096  -8.702  1.00 34.25  ? 215  LEU A CA  1 
ATOM   1302  C  C   . LEU A  1 215 ? 5.405   12.421  -8.338  1.00 41.36  ? 215  LEU A C   1 
ATOM   1303  O  O   . LEU A  1 215 ? 5.481   13.402  -9.088  1.00 46.20  ? 215  LEU A O   1 
ATOM   1304  C  CB  . LEU A  1 215 ? 5.232   10.332  -9.695  1.00 36.79  ? 215  LEU A CB  1 
ATOM   1305  C  CG  . LEU A  1 215 ? 4.933   10.818  -11.105 1.00 41.63  ? 215  LEU A CG  1 
ATOM   1306  C  CD1 . LEU A  1 215 ? 6.212   11.277  -11.809 1.00 35.98  ? 215  LEU A CD1 1 
ATOM   1307  C  CD2 . LEU A  1 215 ? 4.258   9.666   -11.871 1.00 35.82  ? 215  LEU A CD2 1 
ATOM   1308  N  N   . PHE A  1 216 ? 4.735   12.448  -7.191  1.00 35.49  ? 216  PHE A N   1 
ATOM   1309  C  CA  . PHE A  1 216 ? 3.997   13.621  -6.748  1.00 35.05  ? 216  PHE A CA  1 
ATOM   1310  C  C   . PHE A  1 216 ? 4.863   14.631  -6.017  1.00 36.82  ? 216  PHE A C   1 
ATOM   1311  O  O   . PHE A  1 216 ? 4.612   14.942  -4.851  1.00 32.20  ? 216  PHE A O   1 
ATOM   1312  C  CB  . PHE A  1 216 ? 2.872   13.214  -5.808  1.00 35.61  ? 216  PHE A CB  1 
ATOM   1313  C  CG  . PHE A  1 216 ? 1.837   12.360  -6.438  1.00 39.42  ? 216  PHE A CG  1 
ATOM   1314  C  CD1 . PHE A  1 216 ? 2.034   10.990  -6.552  1.00 41.84  ? 216  PHE A CD1 1 
ATOM   1315  C  CD2 . PHE A  1 216 ? 0.650   12.912  -6.899  1.00 36.65  ? 216  PHE A CD2 1 
ATOM   1316  C  CE1 . PHE A  1 216 ? 1.075   10.183  -7.131  1.00 42.12  ? 216  PHE A CE1 1 
ATOM   1317  C  CE2 . PHE A  1 216 ? -0.321  12.110  -7.474  1.00 43.94  ? 216  PHE A CE2 1 
ATOM   1318  C  CZ  . PHE A  1 216 ? -0.108  10.741  -7.591  1.00 43.15  ? 216  PHE A CZ  1 
ATOM   1319  N  N   . LYS A  1 217 ? 5.875   15.152  -6.682  1.00 35.12  ? 217  LYS A N   1 
ATOM   1320  C  CA  . LYS A  1 217 ? 6.724   16.149  -6.047  1.00 35.68  ? 217  LYS A CA  1 
ATOM   1321  C  C   . LYS A  1 217 ? 5.979   17.470  -5.800  1.00 36.55  ? 217  LYS A C   1 
ATOM   1322  O  O   . LYS A  1 217 ? 5.123   17.889  -6.584  1.00 36.25  ? 217  LYS A O   1 
ATOM   1323  C  CB  . LYS A  1 217 ? 7.961   16.389  -6.900  1.00 33.11  ? 217  LYS A CB  1 
ATOM   1324  C  CG  . LYS A  1 217 ? 8.700   15.112  -7.231  1.00 30.30  ? 217  LYS A CG  1 
ATOM   1325  C  CD  . LYS A  1 217 ? 10.027  15.409  -7.856  1.00 29.28  ? 217  LYS A CD  1 
ATOM   1326  C  CE  . LYS A  1 217 ? 10.970  14.238  -7.702  1.00 27.40  ? 217  LYS A CE  1 
ATOM   1327  N  NZ  . LYS A  1 217 ? 12.323  14.566  -8.258  1.00 31.98  ? 217  LYS A NZ  1 
ATOM   1328  N  N   . ALA A  1 218 ? 6.316   18.098  -4.684  1.00 33.75  ? 218  ALA A N   1 
ATOM   1329  C  CA  . ALA A  1 218 ? 5.689   19.316  -4.221  1.00 34.73  ? 218  ALA A CA  1 
ATOM   1330  C  C   . ALA A  1 218 ? 6.726   20.197  -3.514  1.00 36.76  ? 218  ALA A C   1 
ATOM   1331  O  O   . ALA A  1 218 ? 7.797   19.705  -3.124  1.00 33.82  ? 218  ALA A O   1 
ATOM   1332  C  CB  . ALA A  1 218 ? 4.553   18.991  -3.300  1.00 30.09  ? 218  ALA A CB  1 
ATOM   1333  N  N   . ASN A  1 219 ? 6.437   21.494  -3.385  1.00 31.59  ? 219  ASN A N   1 
ATOM   1334  C  CA  . ASN A  1 219 ? 7.179   22.314  -2.440  1.00 30.87  ? 219  ASN A CA  1 
ATOM   1335  C  C   . ASN A  1 219 ? 6.631   22.044  -1.022  1.00 31.88  ? 219  ASN A C   1 
ATOM   1336  O  O   . ASN A  1 219 ? 5.435   21.795  -0.840  1.00 31.30  ? 219  ASN A O   1 
ATOM   1337  C  CB  . ASN A  1 219 ? 7.075   23.807  -2.742  1.00 32.46  ? 219  ASN A CB  1 
ATOM   1338  C  CG  . ASN A  1 219 ? 7.430   24.187  -4.173  1.00 33.19  ? 219  ASN A CG  1 
ATOM   1339  O  OD1 . ASN A  1 219 ? 6.600   24.076  -5.058  1.00 38.73  ? 219  ASN A OD1 1 
ATOM   1340  N  ND2 . ASN A  1 219 ? 8.649   24.682  -4.395  1.00 35.24  ? 219  ASN A ND2 1 
ATOM   1341  N  N   . PHE A  1 220 ? 7.501   22.102  -0.024  1.00 30.04  ? 220  PHE A N   1 
ATOM   1342  C  CA  . PHE A  1 220 ? 7.083   21.929  1.364   1.00 31.99  ? 220  PHE A CA  1 
ATOM   1343  C  C   . PHE A  1 220 ? 7.507   23.105  2.204   1.00 30.23  ? 220  PHE A C   1 
ATOM   1344  O  O   . PHE A  1 220 ? 8.693   23.410  2.281   1.00 34.59  ? 220  PHE A O   1 
ATOM   1345  C  CB  . PHE A  1 220 ? 7.671   20.639  1.960   1.00 32.31  ? 220  PHE A CB  1 
ATOM   1346  C  CG  . PHE A  1 220 ? 7.116   19.401  1.346   1.00 31.87  ? 220  PHE A CG  1 
ATOM   1347  C  CD1 . PHE A  1 220 ? 7.606   18.939  0.130   1.00 31.60  ? 220  PHE A CD1 1 
ATOM   1348  C  CD2 . PHE A  1 220 ? 6.060   18.727  1.946   1.00 28.68  ? 220  PHE A CD2 1 
ATOM   1349  C  CE1 . PHE A  1 220 ? 7.069   17.797  -0.455  1.00 33.48  ? 220  PHE A CE1 1 
ATOM   1350  C  CE2 . PHE A  1 220 ? 5.517   17.589  1.362   1.00 21.60  ? 220  PHE A CE2 1 
ATOM   1351  C  CZ  . PHE A  1 220 ? 6.026   17.122  0.177   1.00 29.83  ? 220  PHE A CZ  1 
ATOM   1352  N  N   . SER A  1 221 ? 6.541   23.762  2.831   1.00 31.45  ? 221  SER A N   1 
ATOM   1353  C  CA  . SER A  1 221 ? 6.833   24.837  3.791   1.00 34.86  ? 221  SER A CA  1 
ATOM   1354  C  C   . SER A  1 221 ? 6.554   24.387  5.210   1.00 33.42  ? 221  SER A C   1 
ATOM   1355  O  O   . SER A  1 221 ? 5.397   24.218  5.601   1.00 37.63  ? 221  SER A O   1 
ATOM   1356  C  CB  . SER A  1 221 ? 6.015   26.090  3.479   1.00 36.58  ? 221  SER A CB  1 
ATOM   1357  O  OG  . SER A  1 221 ? 6.400   26.634  2.232   1.00 40.49  ? 221  SER A OG  1 
ATOM   1358  N  N   . ILE A  1 222 ? 7.608   24.210  5.995   1.00 33.13  ? 222  ILE A N   1 
ATOM   1359  C  CA  . ILE A  1 222 ? 7.451   23.574  7.295   1.00 32.60  ? 222  ILE A CA  1 
ATOM   1360  C  C   . ILE A  1 222 ? 7.635   24.527  8.469   1.00 33.65  ? 222  ILE A C   1 
ATOM   1361  O  O   . ILE A  1 222 ? 8.505   25.403  8.443   1.00 36.15  ? 222  ILE A O   1 
ATOM   1362  C  CB  . ILE A  1 222 ? 8.432   22.380  7.404   1.00 35.84  ? 222  ILE A CB  1 
ATOM   1363  C  CG1 . ILE A  1 222 ? 8.115   21.389  6.277   1.00 29.60  ? 222  ILE A CG1 1 
ATOM   1364  C  CG2 . ILE A  1 222 ? 8.351   21.711  8.793   1.00 30.55  ? 222  ILE A CG2 1 
ATOM   1365  C  CD1 . ILE A  1 222 ? 9.134   20.353  6.042   1.00 26.97  ? 222  ILE A CD1 1 
ATOM   1366  N  N   . LYS A  1 223 ? 6.788   24.354  9.483   1.00 33.53  ? 223  LYS A N   1 
ATOM   1367  C  CA  . LYS A  1 223 ? 6.898   25.059  10.777  1.00 36.57  ? 223  LYS A CA  1 
ATOM   1368  C  C   . LYS A  1 223 ? 6.858   24.101  11.986  1.00 40.98  ? 223  LYS A C   1 
ATOM   1369  O  O   . LYS A  1 223 ? 6.086   23.127  12.006  1.00 36.60  ? 223  LYS A O   1 
ATOM   1370  C  CB  . LYS A  1 223 ? 5.772   26.090  10.946  1.00 40.56  ? 223  LYS A CB  1 
ATOM   1371  C  CG  . LYS A  1 223 ? 5.440   26.910  9.713   1.00 39.82  ? 223  LYS A CG  1 
ATOM   1372  C  CD  . LYS A  1 223 ? 4.392   27.954  10.079  1.00 52.29  ? 223  LYS A CD  1 
ATOM   1373  C  CE  . LYS A  1 223 ? 4.446   29.193  9.168   1.00 58.24  ? 223  LYS A CE  1 
ATOM   1374  N  NZ  . LYS A  1 223 ? 3.777   30.381  9.810   1.00 62.05  ? 223  LYS A NZ  1 
ATOM   1375  N  N   . ILE A  1 224 ? 7.675   24.385  12.997  1.00 38.40  ? 224  ILE A N   1 
ATOM   1376  C  CA  . ILE A  1 224 ? 7.733   23.541  14.186  1.00 40.69  ? 224  ILE A CA  1 
ATOM   1377  C  C   . ILE A  1 224 ? 7.670   24.365  15.490  1.00 44.41  ? 224  ILE A C   1 
ATOM   1378  O  O   . ILE A  1 224 ? 8.484   25.263  15.724  1.00 37.78  ? 224  ILE A O   1 
ATOM   1379  C  CB  . ILE A  1 224 ? 9.026   22.695  14.234  1.00 38.59  ? 224  ILE A CB  1 
ATOM   1380  C  CG1 . ILE A  1 224 ? 9.271   21.975  12.914  1.00 33.71  ? 224  ILE A CG1 1 
ATOM   1381  C  CG2 . ILE A  1 224 ? 8.963   21.698  15.394  1.00 29.70  ? 224  ILE A CG2 1 
ATOM   1382  C  CD1 . ILE A  1 224 ? 8.282   20.895  12.650  1.00 39.18  ? 224  ILE A CD1 1 
ATOM   1383  N  N   . ARG A  1 225 ? 6.715   24.040  16.346  1.00 38.80  ? 225  ARG A N   1 
ATOM   1384  C  CA  . ARG A  1 225 ? 6.684   24.620  17.681  1.00 47.10  ? 225  ARG A CA  1 
ATOM   1385  C  C   . ARG A  1 225 ? 7.484   23.748  18.664  1.00 43.82  ? 225  ARG A C   1 
ATOM   1386  O  O   . ARG A  1 225 ? 7.545   22.532  18.519  1.00 36.98  ? 225  ARG A O   1 
ATOM   1387  C  CB  . ARG A  1 225 ? 5.242   24.793  18.141  1.00 43.06  ? 225  ARG A CB  1 
ATOM   1388  C  CG  . ARG A  1 225 ? 5.089   25.556  19.421  1.00 44.29  ? 225  ARG A CG  1 
ATOM   1389  C  CD  . ARG A  1 225 ? 3.618   25.845  19.635  1.00 47.45  ? 225  ARG A CD  1 
ATOM   1390  N  NE  . ARG A  1 225 ? 3.121   26.712  18.580  1.00 48.30  ? 225  ARG A NE  1 
ATOM   1391  C  CZ  . ARG A  1 225 ? 1.846   27.008  18.380  1.00 55.07  ? 225  ARG A CZ  1 
ATOM   1392  N  NH1 . ARG A  1 225 ? 0.900   26.481  19.146  1.00 47.27  ? 225  ARG A NH1 1 
ATOM   1393  N  NH2 . ARG A  1 225 ? 1.523   27.823  17.391  1.00 60.12  ? 225  ARG A NH2 1 
ATOM   1394  N  N   . ARG A  1 226 ? 8.111   24.371  19.656  1.00 42.95  ? 226  ARG A N   1 
ATOM   1395  C  CA  . ARG A  1 226 ? 9.059   23.641  20.480  1.00 44.92  ? 226  ARG A CA  1 
ATOM   1396  C  C   . ARG A  1 226 ? 9.388   24.363  21.760  1.00 42.73  ? 226  ARG A C   1 
ATOM   1397  O  O   . ARG A  1 226 ? 9.138   25.556  21.888  1.00 51.39  ? 226  ARG A O   1 
ATOM   1398  C  CB  . ARG A  1 226 ? 10.358  23.410  19.718  1.00 35.94  ? 226  ARG A CB  1 
ATOM   1399  C  CG  . ARG A  1 226 ? 11.067  24.711  19.432  1.00 39.62  ? 226  ARG A CG  1 
ATOM   1400  C  CD  . ARG A  1 226 ? 12.498  24.479  19.027  1.00 38.69  ? 226  ARG A CD  1 
ATOM   1401  N  NE  . ARG A  1 226 ? 13.037  25.676  18.420  1.00 35.69  ? 226  ARG A NE  1 
ATOM   1402  C  CZ  . ARG A  1 226 ? 13.520  26.695  19.119  1.00 44.08  ? 226  ARG A CZ  1 
ATOM   1403  N  NH1 . ARG A  1 226 ? 13.526  26.638  20.451  1.00 42.76  ? 226  ARG A NH1 1 
ATOM   1404  N  NH2 . ARG A  1 226 ? 13.993  27.762  18.492  1.00 33.87  ? 226  ARG A NH2 1 
ATOM   1405  N  N   . GLU A  1 227 ? 9.975   23.629  22.696  1.00 37.83  ? 227  GLU A N   1 
ATOM   1406  C  CA  . GLU A  1 227 ? 10.449  24.201  23.940  1.00 43.46  ? 227  GLU A CA  1 
ATOM   1407  C  C   . GLU A  1 227 ? 11.791  24.876  23.726  1.00 41.92  ? 227  GLU A C   1 
ATOM   1408  O  O   . GLU A  1 227 ? 12.445  24.640  22.724  1.00 42.04  ? 227  GLU A O   1 
ATOM   1409  C  CB  . GLU A  1 227 ? 10.553  23.128  25.013  1.00 40.93  ? 227  GLU A CB  1 
ATOM   1410  C  CG  . GLU A  1 227 ? 9.222   22.792  25.633  1.00 41.79  ? 227  GLU A CG  1 
ATOM   1411  C  CD  . GLU A  1 227 ? 9.285   21.546  26.489  1.00 47.78  ? 227  GLU A CD  1 
ATOM   1412  O  OE1 . GLU A  1 227 ? 10.395  21.211  26.968  1.00 45.54  ? 227  GLU A OE1 1 
ATOM   1413  O  OE2 . GLU A  1 227 ? 8.231   20.892  26.666  1.00 54.21  ? 227  GLU A OE2 1 
ATOM   1414  N  N   . SER A  1 228 ? 12.191  25.726  24.666  1.00 43.02  ? 228  SER A N   1 
ATOM   1415  C  CA  . SER A  1 228 ? 13.431  26.484  24.525  1.00 47.26  ? 228  SER A CA  1 
ATOM   1416  C  C   . SER A  1 228 ? 14.651  25.593  24.720  1.00 43.28  ? 228  SER A C   1 
ATOM   1417  O  O   . SER A  1 228 ? 15.753  25.937  24.291  1.00 48.60  ? 228  SER A O   1 
ATOM   1418  C  CB  . SER A  1 228 ? 13.475  27.650  25.525  1.00 51.01  ? 228  SER A CB  1 
ATOM   1419  O  OG  . SER A  1 228 ? 13.832  27.200  26.830  1.00 51.28  ? 228  SER A OG  1 
ATOM   1420  N  N   . ARG A  1 229 ? 14.463  24.457  25.380  1.00 37.74  ? 229  ARG A N   1 
ATOM   1421  C  CA  . ARG A  1 229 ? 15.560  23.514  25.588  1.00 40.31  ? 229  ARG A CA  1 
ATOM   1422  C  C   . ARG A  1 229 ? 15.852  22.635  24.361  1.00 36.94  ? 229  ARG A C   1 
ATOM   1423  O  O   . ARG A  1 229 ? 16.730  21.774  24.397  1.00 37.22  ? 229  ARG A O   1 
ATOM   1424  C  CB  . ARG A  1 229 ? 15.262  22.615  26.786  1.00 38.31  ? 229  ARG A CB  1 
ATOM   1425  C  CG  . ARG A  1 229 ? 14.079  21.692  26.572  1.00 40.75  ? 229  ARG A CG  1 
ATOM   1426  C  CD  . ARG A  1 229 ? 13.892  20.724  27.737  1.00 37.54  ? 229  ARG A CD  1 
ATOM   1427  N  NE  . ARG A  1 229 ? 12.596  20.064  27.632  1.00 37.01  ? 229  ARG A NE  1 
ATOM   1428  C  CZ  . ARG A  1 229 ? 12.428  18.744  27.625  1.00 39.56  ? 229  ARG A CZ  1 
ATOM   1429  N  NH1 . ARG A  1 229 ? 13.484  17.940  27.738  1.00 39.70  ? 229  ARG A NH1 1 
ATOM   1430  N  NH2 . ARG A  1 229 ? 11.205  18.230  27.521  1.00 33.38  ? 229  ARG A NH2 1 
ATOM   1431  N  N   . HIS A  1 230 ? 15.106  22.827  23.284  1.00 35.48  ? 230  HIS A N   1 
ATOM   1432  C  CA  . HIS A  1 230 ? 15.356  22.075  22.067  1.00 33.46  ? 230  HIS A CA  1 
ATOM   1433  C  C   . HIS A  1 230 ? 15.695  23.007  20.927  1.00 33.73  ? 230  HIS A C   1 
ATOM   1434  O  O   . HIS A  1 230 ? 15.399  24.193  21.001  1.00 34.91  ? 230  HIS A O   1 
ATOM   1435  C  CB  . HIS A  1 230 ? 14.141  21.252  21.684  1.00 33.56  ? 230  HIS A CB  1 
ATOM   1436  C  CG  . HIS A  1 230 ? 13.774  20.205  22.682  1.00 32.76  ? 230  HIS A CG  1 
ATOM   1437  N  ND1 . HIS A  1 230 ? 12.472  19.971  23.064  1.00 31.28  ? 230  HIS A ND1 1 
ATOM   1438  C  CD2 . HIS A  1 230 ? 14.532  19.302  23.347  1.00 37.11  ? 230  HIS A CD2 1 
ATOM   1439  C  CE1 . HIS A  1 230 ? 12.445  18.975  23.932  1.00 34.55  ? 230  HIS A CE1 1 
ATOM   1440  N  NE2 . HIS A  1 230 ? 13.683  18.554  24.124  1.00 35.70  ? 230  HIS A NE2 1 
ATOM   1441  N  N   . ILE A  1 231 ? 16.320  22.461  19.889  1.00 30.39  ? 231  ILE A N   1 
ATOM   1442  C  CA  . ILE A  1 231 ? 16.310  23.057  18.556  1.00 29.42  ? 231  ILE A CA  1 
ATOM   1443  C  C   . ILE A  1 231 ? 15.437  22.204  17.638  1.00 31.04  ? 231  ILE A C   1 
ATOM   1444  O  O   . ILE A  1 231 ? 15.128  21.052  17.948  1.00 34.71  ? 231  ILE A O   1 
ATOM   1445  C  CB  . ILE A  1 231 ? 17.698  23.128  17.953  1.00 31.65  ? 231  ILE A CB  1 
ATOM   1446  C  CG1 . ILE A  1 231 ? 18.189  21.700  17.709  1.00 26.91  ? 231  ILE A CG1 1 
ATOM   1447  C  CG2 . ILE A  1 231 ? 18.644  23.914  18.858  1.00 29.14  ? 231  ILE A CG2 1 
ATOM   1448  C  CD1 . ILE A  1 231 ? 19.566  21.602  17.231  1.00 27.18  ? 231  ILE A CD1 1 
ATOM   1449  N  N   . ALA A  1 232 ? 15.054  22.753  16.495  1.00 30.97  ? 232  ALA A N   1 
ATOM   1450  C  CA  . ALA A  1 232 ? 14.310  21.990  15.517  1.00 25.41  ? 232  ALA A CA  1 
ATOM   1451  C  C   . ALA A  1 232 ? 15.044  22.084  14.190  1.00 30.90  ? 232  ALA A C   1 
ATOM   1452  O  O   . ALA A  1 232 ? 15.515  23.156  13.824  1.00 32.82  ? 232  ALA A O   1 
ATOM   1453  C  CB  . ALA A  1 232 ? 12.899  22.500  15.398  1.00 31.13  ? 232  ALA A CB  1 
ATOM   1454  N  N   . LEU A  1 233 ? 15.163  20.964  13.478  1.00 27.74  ? 233  LEU A N   1 
ATOM   1455  C  CA  . LEU A  1 233 ? 15.850  20.946  12.185  1.00 26.24  ? 233  LEU A CA  1 
ATOM   1456  C  C   . LEU A  1 233 ? 14.909  20.411  11.134  1.00 24.51  ? 233  LEU A C   1 
ATOM   1457  O  O   . LEU A  1 233 ? 14.045  19.600  11.444  1.00 26.39  ? 233  LEU A O   1 
ATOM   1458  C  CB  . LEU A  1 233 ? 17.122  20.091  12.252  1.00 22.80  ? 233  LEU A CB  1 
ATOM   1459  C  CG  . LEU A  1 233 ? 18.202  20.533  13.232  1.00 29.13  ? 233  LEU A CG  1 
ATOM   1460  C  CD1 . LEU A  1 233 ? 19.273  19.466  13.364  1.00 26.02  ? 233  LEU A CD1 1 
ATOM   1461  C  CD2 . LEU A  1 233 ? 18.822  21.868  12.828  1.00 28.79  ? 233  LEU A CD2 1 
ATOM   1462  N  N   . SER A  1 234 ? 15.041  20.861  9.893   1.00 20.20  ? 234  SER A N   1 
ATOM   1463  C  CA  . SER A  1 234 ? 14.275  20.241  8.819   1.00 25.24  ? 234  SER A CA  1 
ATOM   1464  C  C   . SER A  1 234 ? 15.085  20.313  7.524   1.00 24.82  ? 234  SER A C   1 
ATOM   1465  O  O   . SER A  1 234 ? 16.266  20.594  7.580   1.00 30.07  ? 234  SER A O   1 
ATOM   1466  C  CB  . SER A  1 234 ? 12.874  20.875  8.730   1.00 25.04  ? 234  SER A CB  1 
ATOM   1467  O  OG  . SER A  1 234 ? 12.600  21.401  7.470   1.00 41.04  ? 234  SER A OG  1 
ATOM   1468  N  N   . ASN A  1 235 ? 14.491  20.011  6.375   1.00 24.90  ? 235  ASN A N   1 
ATOM   1469  C  CA  . ASN A  1 235 ? 15.241  20.068  5.122   1.00 28.20  ? 235  ASN A CA  1 
ATOM   1470  C  C   . ASN A  1 235 ? 15.955  21.392  4.871   1.00 32.11  ? 235  ASN A C   1 
ATOM   1471  O  O   . ASN A  1 235 ? 17.113  21.409  4.475   1.00 30.35  ? 235  ASN A O   1 
ATOM   1472  C  CB  . ASN A  1 235 ? 14.325  19.777  3.950   1.00 30.12  ? 235  ASN A CB  1 
ATOM   1473  C  CG  . ASN A  1 235 ? 13.501  18.532  4.163   1.00 31.05  ? 235  ASN A CG  1 
ATOM   1474  O  OD1 . ASN A  1 235 ? 12.455  18.577  4.810   1.00 29.40  ? 235  ASN A OD1 1 
ATOM   1475  N  ND2 . ASN A  1 235 ? 13.957  17.417  3.606   1.00 28.19  ? 235  ASN A ND2 1 
ATOM   1476  N  N   . MET A  1 236 ? 15.267  22.491  5.154   1.00 31.19  ? 236  MET A N   1 
ATOM   1477  C  CA  . MET A  1 236 ? 15.705  23.816  4.749   1.00 28.13  ? 236  MET A CA  1 
ATOM   1478  C  C   . MET A  1 236 ? 16.223  24.662  5.909   1.00 28.83  ? 236  MET A C   1 
ATOM   1479  O  O   . MET A  1 236 ? 15.963  24.341  7.067   1.00 28.09  ? 236  MET A O   1 
ATOM   1480  C  CB  . MET A  1 236 ? 14.538  24.519  4.058   1.00 28.59  ? 236  MET A CB  1 
ATOM   1481  C  CG  . MET A  1 236 ? 13.978  23.746  2.879   1.00 24.46  ? 236  MET A CG  1 
ATOM   1482  S  SD  . MET A  1 236 ? 15.121  23.669  1.478   1.00 39.53  ? 236  MET A SD  1 
ATOM   1483  C  CE  . MET A  1 236 ? 15.252  25.390  0.994   1.00 34.02  ? 236  MET A CE  1 
ATOM   1484  N  N   . PRO A  1 237 ? 16.965  25.748  5.612   1.00 33.68  ? 237  PRO A N   1 
ATOM   1485  C  CA  . PRO A  1 237 ? 17.366  26.648  6.710   1.00 34.24  ? 237  PRO A CA  1 
ATOM   1486  C  C   . PRO A  1 237 ? 16.188  27.297  7.419   1.00 34.17  ? 237  PRO A C   1 
ATOM   1487  O  O   . PRO A  1 237 ? 15.151  27.568  6.806   1.00 34.20  ? 237  PRO A O   1 
ATOM   1488  C  CB  . PRO A  1 237 ? 18.221  27.729  6.026   1.00 28.21  ? 237  PRO A CB  1 
ATOM   1489  C  CG  . PRO A  1 237 ? 18.132  27.469  4.561   1.00 39.29  ? 237  PRO A CG  1 
ATOM   1490  C  CD  . PRO A  1 237 ? 17.645  26.071  4.347   1.00 34.20  ? 237  PRO A CD  1 
ATOM   1491  N  N   . LYS A  1 238 ? 16.354  27.521  8.716   1.00 31.79  ? 238  LYS A N   1 
ATOM   1492  C  CA  . LYS A  1 238 ? 15.412  28.326  9.474   1.00 38.97  ? 238  LYS A CA  1 
ATOM   1493  C  C   . LYS A  1 238 ? 15.384  29.744  8.920   1.00 41.30  ? 238  LYS A C   1 
ATOM   1494  O  O   . LYS A  1 238 ? 16.419  30.324  8.617   1.00 36.33  ? 238  LYS A O   1 
ATOM   1495  C  CB  . LYS A  1 238 ? 15.788  28.358  10.937  1.00 38.14  ? 238  LYS A CB  1 
ATOM   1496  C  CG  . LYS A  1 238 ? 14.612  28.323  11.847  1.00 39.18  ? 238  LYS A CG  1 
ATOM   1497  C  CD  . LYS A  1 238 ? 15.093  28.431  13.257  1.00 43.25  ? 238  LYS A CD  1 
ATOM   1498  C  CE  . LYS A  1 238 ? 15.974  29.653  13.399  1.00 42.23  ? 238  LYS A CE  1 
ATOM   1499  N  NZ  . LYS A  1 238 ? 16.400  29.861  14.804  1.00 51.15  ? 238  LYS A NZ  1 
ATOM   1500  N  N   . VAL A  1 239 ? 14.186  30.271  8.742   1.00 40.11  ? 239  VAL A N   1 
ATOM   1501  C  CA  . VAL A  1 239 ? 14.022  31.639  8.296   1.00 47.11  ? 239  VAL A CA  1 
ATOM   1502  C  C   . VAL A  1 239 ? 13.925  32.568  9.496   1.00 46.79  ? 239  VAL A C   1 
ATOM   1503  O  O   . VAL A  1 239 ? 14.506  33.651  9.509   1.00 45.97  ? 239  VAL A O   1 
ATOM   1504  C  CB  . VAL A  1 239 ? 12.754  31.814  7.454   1.00 49.89  ? 239  VAL A CB  1 
ATOM   1505  C  CG1 . VAL A  1 239 ? 12.445  33.301  7.284   1.00 54.97  ? 239  VAL A CG1 1 
ATOM   1506  C  CG2 . VAL A  1 239 ? 12.894  31.119  6.116   1.00 35.84  ? 239  VAL A CG2 1 
ATOM   1507  N  N   . LYS A  1 240 ? 13.213  32.095  10.514  1.00 44.06  ? 240  LYS A N   1 
ATOM   1508  C  CA  . LYS A  1 240 ? 12.696  32.948  11.562  1.00 48.99  ? 240  LYS A CA  1 
ATOM   1509  C  C   . LYS A  1 240 ? 12.140  32.124  12.739  1.00 41.97  ? 240  LYS A C   1 
ATOM   1510  O  O   . LYS A  1 240 ? 11.488  31.121  12.540  1.00 48.70  ? 240  LYS A O   1 
ATOM   1511  C  CB  . LYS A  1 240 ? 11.620  33.855  10.943  1.00 51.94  ? 240  LYS A CB  1 
ATOM   1512  C  CG  . LYS A  1 240 ? 10.505  34.284  11.848  1.00 46.20  ? 240  LYS A CG  1 
ATOM   1513  C  CD  . LYS A  1 240 ? 9.193   34.362  11.089  1.00 51.30  ? 240  LYS A CD  1 
ATOM   1514  C  CE  . LYS A  1 240 ? 9.256   35.343  9.930   1.00 61.77  ? 240  LYS A CE  1 
ATOM   1515  N  NZ  . LYS A  1 240 ? 7.923   35.505  9.258   1.00 65.64  ? 240  LYS A NZ  1 
ATOM   1516  N  N   . THR A  1 241 ? 12.429  32.549  13.959  1.00 45.18  ? 241  THR A N   1 
ATOM   1517  C  CA  . THR A  1 241 ? 11.872  31.957  15.166  1.00 41.56  ? 241  THR A CA  1 
ATOM   1518  C  C   . THR A  1 241 ? 10.985  32.992  15.833  1.00 45.39  ? 241  THR A C   1 
ATOM   1519  O  O   . THR A  1 241 ? 11.441  34.099  16.091  1.00 46.27  ? 241  THR A O   1 
ATOM   1520  C  CB  . THR A  1 241 ? 12.966  31.541  16.150  1.00 40.05  ? 241  THR A CB  1 
ATOM   1521  O  OG1 . THR A  1 241 ? 13.797  30.555  15.540  1.00 50.40  ? 241  THR A OG1 1 
ATOM   1522  C  CG2 . THR A  1 241 ? 12.369  30.980  17.434  1.00 38.89  ? 241  THR A CG2 1 
ATOM   1523  N  N   . ILE A  1 242 ? 9.729   32.671  16.113  1.00 42.60  ? 242  ILE A N   1 
ATOM   1524  C  CA  . ILE A  1 242 ? 8.895   33.664  16.772  1.00 52.18  ? 242  ILE A CA  1 
ATOM   1525  C  C   . ILE A  1 242 ? 8.464   33.203  18.170  1.00 52.55  ? 242  ILE A C   1 
ATOM   1526  O  O   . ILE A  1 242 ? 8.067   32.048  18.361  1.00 50.17  ? 242  ILE A O   1 
ATOM   1527  C  CB  . ILE A  1 242 ? 7.654   34.045  15.906  1.00 48.29  ? 242  ILE A CB  1 
ATOM   1528  C  CG1 . ILE A  1 242 ? 6.806   32.841  15.547  1.00 48.81  ? 242  ILE A CG1 1 
ATOM   1529  C  CG2 . ILE A  1 242 ? 8.080   34.736  14.615  1.00 42.07  ? 242  ILE A CG2 1 
ATOM   1530  C  CD1 . ILE A  1 242 ? 5.737   33.193  14.519  1.00 43.00  ? 242  ILE A CD1 1 
ATOM   1531  N  N   . GLU A  1 243 ? 8.586   34.112  19.143  1.00 56.21  ? 243  GLU A N   1 
ATOM   1532  C  CA  . GLU A  1 243 ? 8.185   33.850  20.536  1.00 61.60  ? 243  GLU A CA  1 
ATOM   1533  C  C   . GLU A  1 243 ? 6.680   33.832  20.721  1.00 54.92  ? 243  GLU A C   1 
ATOM   1534  O  O   . GLU A  1 243 ? 5.988   34.791  20.383  1.00 55.91  ? 243  GLU A O   1 
ATOM   1535  C  CB  . GLU A  1 243 ? 8.774   34.890  21.478  1.00 59.98  ? 243  GLU A CB  1 
ATOM   1536  C  CG  . GLU A  1 243 ? 10.195  34.619  21.908  1.00 63.13  ? 243  GLU A CG  1 
ATOM   1537  C  CD  . GLU A  1 243 ? 10.324  34.553  23.407  1.00 72.72  ? 243  GLU A CD  1 
ATOM   1538  O  OE1 . GLU A  1 243 ? 9.904   33.529  23.997  1.00 71.17  ? 243  GLU A OE1 1 
ATOM   1539  O  OE2 . GLU A  1 243 ? 10.837  35.532  23.991  1.00 73.13  ? 243  GLU A OE2 1 
ATOM   1540  N  N   . LEU A  1 244 ? 6.175   32.736  21.260  1.00 49.97  ? 244  LEU A N   1 
ATOM   1541  C  CA  . LEU A  1 244 ? 4.747   32.614  21.473  1.00 58.02  ? 244  LEU A CA  1 
ATOM   1542  C  C   . LEU A  1 244 ? 4.389   32.994  22.900  1.00 67.44  ? 244  LEU A C   1 
ATOM   1543  O  O   . LEU A  1 244 ? 5.271   33.144  23.761  1.00 63.91  ? 244  LEU A O   1 
ATOM   1544  C  CB  . LEU A  1 244 ? 4.280   31.201  21.163  1.00 55.89  ? 244  LEU A CB  1 
ATOM   1545  C  CG  . LEU A  1 244 ? 4.414   30.843  19.683  1.00 60.20  ? 244  LEU A CG  1 
ATOM   1546  C  CD1 . LEU A  1 244 ? 4.396   29.362  19.519  1.00 53.08  ? 244  LEU A CD1 1 
ATOM   1547  C  CD2 . LEU A  1 244 ? 3.292   31.468  18.863  1.00 60.28  ? 244  LEU A CD2 1 
ATOM   1548  N  N   A GLU A  1 245 ? 3.087   33.153  23.117  0.41 67.09  ? 245  GLU A N   1 
ATOM   1549  N  N   B GLU A  1 245 ? 3.095   33.132  23.168  0.59 66.98  ? 245  GLU A N   1 
ATOM   1550  C  CA  A GLU A  1 245 ? 2.509   33.540  24.395  0.41 67.81  ? 245  GLU A CA  1 
ATOM   1551  C  CA  B GLU A  1 245 ? 2.650   33.643  24.458  0.59 67.84  ? 245  GLU A CA  1 
ATOM   1552  C  C   A GLU A  1 245 ? 3.137   32.810  25.576  0.41 67.50  ? 245  GLU A C   1 
ATOM   1553  C  C   B GLU A  1 245 ? 3.183   32.808  25.623  0.59 67.20  ? 245  GLU A C   1 
ATOM   1554  O  O   A GLU A  1 245 ? 3.932   33.383  26.321  0.41 69.59  ? 245  GLU A O   1 
ATOM   1555  O  O   B GLU A  1 245 ? 3.976   33.316  26.417  0.59 69.70  ? 245  GLU A O   1 
ATOM   1556  C  CB  A GLU A  1 245 ? 0.989   33.300  24.375  0.41 69.18  ? 245  GLU A CB  1 
ATOM   1557  C  CB  B GLU A  1 245 ? 1.122   33.724  24.516  0.59 69.22  ? 245  GLU A CB  1 
ATOM   1558  C  CG  A GLU A  1 245 ? 0.527   31.979  23.726  0.41 65.44  ? 245  GLU A CG  1 
ATOM   1559  C  CG  B GLU A  1 245 ? 0.612   34.683  25.586  0.59 64.59  ? 245  GLU A CG  1 
ATOM   1560  C  CD  A GLU A  1 245 ? 0.524   32.027  22.207  0.41 66.51  ? 245  GLU A CD  1 
ATOM   1561  C  CD  B GLU A  1 245 ? -0.877  34.951  25.484  0.59 69.01  ? 245  GLU A CD  1 
ATOM   1562  O  OE1 A GLU A  1 245 ? 0.582   33.144  21.650  0.41 65.39  ? 245  GLU A OE1 1 
ATOM   1563  O  OE1 B GLU A  1 245 ? -1.434  34.868  24.369  0.59 63.51  ? 245  GLU A OE1 1 
ATOM   1564  O  OE2 A GLU A  1 245 ? 0.472   30.950  21.571  0.41 60.98  ? 245  GLU A OE2 1 
ATOM   1565  O  OE2 B GLU A  1 245 ? -1.493  35.249  26.528  0.59 76.06  ? 245  GLU A OE2 1 
ATOM   1566  N  N   . GLY A  1 246 ? 2.786   31.540  25.722  1.00 64.86  ? 246  GLY A N   1 
ATOM   1567  C  CA  . GLY A  1 246 ? 3.212   30.716  26.849  1.00 69.60  ? 246  GLY A CA  1 
ATOM   1568  C  C   . GLY A  1 246 ? 4.711   30.499  27.029  1.00 70.63  ? 246  GLY A C   1 
ATOM   1569  O  O   . GLY A  1 246 ? 5.141   29.849  27.984  1.00 68.50  ? 246  GLY A O   1 
ATOM   1570  N  N   . GLY A  1 247 ? 5.508   31.037  26.110  1.00 71.68  ? 247  GLY A N   1 
ATOM   1571  C  CA  . GLY A  1 247 ? 6.951   30.916  26.186  1.00 66.66  ? 247  GLY A CA  1 
ATOM   1572  C  C   . GLY A  1 247 ? 7.514   29.883  25.222  1.00 62.20  ? 247  GLY A C   1 
ATOM   1573  O  O   . GLY A  1 247 ? 8.723   29.660  25.191  1.00 60.20  ? 247  GLY A O   1 
ATOM   1574  N  N   . LEU A  1 248 ? 6.651   29.232  24.450  1.00 49.51  ? 248  LEU A N   1 
ATOM   1575  C  CA  . LEU A  1 248 ? 7.130   28.320  23.424  1.00 51.29  ? 248  LEU A CA  1 
ATOM   1576  C  C   . LEU A  1 248 ? 7.691   29.099  22.242  1.00 54.68  ? 248  LEU A C   1 
ATOM   1577  O  O   . LEU A  1 248 ? 7.409   30.286  22.078  1.00 54.62  ? 248  LEU A O   1 
ATOM   1578  C  CB  . LEU A  1 248 ? 6.019   27.389  22.955  1.00 45.90  ? 248  LEU A CB  1 
ATOM   1579  C  CG  . LEU A  1 248 ? 5.629   26.369  24.008  1.00 46.10  ? 248  LEU A CG  1 
ATOM   1580  C  CD1 . LEU A  1 248 ? 4.555   25.439  23.471  1.00 44.56  ? 248  LEU A CD1 1 
ATOM   1581  C  CD2 . LEU A  1 248 ? 6.870   25.607  24.477  1.00 48.60  ? 248  LEU A CD2 1 
ATOM   1582  N  N   . LEU A  1 249 ? 8.500   28.429  21.427  1.00 51.02  ? 249  LEU A N   1 
ATOM   1583  C  CA  . LEU A  1 249 ? 9.022   29.040  20.211  1.00 47.07  ? 249  LEU A CA  1 
ATOM   1584  C  C   . LEU A  1 249 ? 8.490   28.337  18.973  1.00 42.61  ? 249  LEU A C   1 
ATOM   1585  O  O   . LEU A  1 249 ? 8.025   27.209  19.027  1.00 45.10  ? 249  LEU A O   1 
ATOM   1586  C  CB  . LEU A  1 249 ? 10.542  29.026  20.243  1.00 42.07  ? 249  LEU A CB  1 
ATOM   1587  C  CG  . LEU A  1 249 ? 10.982  29.727  21.531  1.00 50.96  ? 249  LEU A CG  1 
ATOM   1588  C  CD1 . LEU A  1 249 ? 12.279  29.182  22.074  1.00 48.49  ? 249  LEU A CD1 1 
ATOM   1589  C  CD2 . LEU A  1 249 ? 11.096  31.226  21.299  1.00 52.73  ? 249  LEU A CD2 1 
ATOM   1590  N  N   . GLU A  1 250 ? 8.530   29.026  17.851  1.00 48.67  ? 250  GLU A N   1 
ATOM   1591  C  CA  . GLU A  1 250 ? 8.044   28.455  16.615  1.00 39.82  ? 250  GLU A CA  1 
ATOM   1592  C  C   . GLU A  1 250 ? 9.072   28.701  15.534  1.00 44.66  ? 250  GLU A C   1 
ATOM   1593  O  O   . GLU A  1 250 ? 9.303   29.844  15.141  1.00 43.10  ? 250  GLU A O   1 
ATOM   1594  C  CB  . GLU A  1 250 ? 6.696   29.055  16.237  1.00 44.10  ? 250  GLU A CB  1 
ATOM   1595  C  CG  . GLU A  1 250 ? 6.074   28.448  15.011  1.00 48.13  ? 250  GLU A CG  1 
ATOM   1596  C  CD  . GLU A  1 250 ? 4.556   28.460  15.072  1.00 55.81  ? 250  GLU A CD  1 
ATOM   1597  O  OE1 . GLU A  1 250 ? 4.005   28.104  16.139  1.00 58.10  ? 250  GLU A OE1 1 
ATOM   1598  O  OE2 . GLU A  1 250 ? 3.917   28.810  14.054  1.00 54.89  ? 250  GLU A OE2 1 
ATOM   1599  N  N   . ASP A  1 251 ? 9.718   27.630  15.072  1.00 43.63  ? 251  ASP A N   1 
ATOM   1600  C  CA  . ASP A  1 251 ? 10.655  27.765  13.968  1.00 42.15  ? 251  ASP A CA  1 
ATOM   1601  C  C   . ASP A  1 251 ? 9.954   27.680  12.599  1.00 41.53  ? 251  ASP A C   1 
ATOM   1602  O  O   . ASP A  1 251 ? 9.173   26.760  12.343  1.00 38.58  ? 251  ASP A O   1 
ATOM   1603  C  CB  . ASP A  1 251 ? 11.746  26.717  14.080  1.00 40.51  ? 251  ASP A CB  1 
ATOM   1604  C  CG  . ASP A  1 251 ? 12.632  26.935  15.286  1.00 45.92  ? 251  ASP A CG  1 
ATOM   1605  O  OD1 . ASP A  1 251 ? 12.680  28.088  15.775  1.00 41.82  ? 251  ASP A OD1 1 
ATOM   1606  O  OD2 . ASP A  1 251 ? 13.288  25.958  15.739  1.00 44.74  ? 251  ASP A OD2 1 
ATOM   1607  N  N   . HIS A  1 252 ? 10.221  28.672  11.748  1.00 40.25  ? 252  HIS A N   1 
ATOM   1608  C  CA  . HIS A  1 252 ? 9.744   28.695  10.365  1.00 40.82  ? 252  HIS A CA  1 
ATOM   1609  C  C   . HIS A  1 252 ? 10.912  28.351  9.465   1.00 40.18  ? 252  HIS A C   1 
ATOM   1610  O  O   . HIS A  1 252 ? 11.997  28.933  9.602   1.00 41.70  ? 252  HIS A O   1 
ATOM   1611  C  CB  . HIS A  1 252 ? 9.206   30.072  9.941   1.00 44.87  ? 252  HIS A CB  1 
ATOM   1612  C  CG  . HIS A  1 252 ? 7.966   30.514  10.656  1.00 52.28  ? 252  HIS A CG  1 
ATOM   1613  N  ND1 . HIS A  1 252 ? 7.760   30.303  12.004  1.00 50.78  ? 252  HIS A ND1 1 
ATOM   1614  C  CD2 . HIS A  1 252 ? 6.880   31.188  10.208  1.00 47.26  ? 252  HIS A CD2 1 
ATOM   1615  C  CE1 . HIS A  1 252 ? 6.588   30.803  12.349  1.00 48.81  ? 252  HIS A CE1 1 
ATOM   1616  N  NE2 . HIS A  1 252 ? 6.040   31.355  11.281  1.00 51.86  ? 252  HIS A NE2 1 
ATOM   1617  N  N   . PHE A  1 253 ? 10.689  27.450  8.519   1.00 35.56  ? 253  PHE A N   1 
ATOM   1618  C  CA  . PHE A  1 253 ? 11.751  27.051  7.613   1.00 35.95  ? 253  PHE A CA  1 
ATOM   1619  C  C   . PHE A  1 253 ? 11.462  27.517  6.198   1.00 29.66  ? 253  PHE A C   1 
ATOM   1620  O  O   . PHE A  1 253 ? 10.320  27.533  5.772   1.00 34.31  ? 253  PHE A O   1 
ATOM   1621  C  CB  . PHE A  1 253 ? 11.937  25.522  7.677   1.00 32.64  ? 253  PHE A CB  1 
ATOM   1622  C  CG  . PHE A  1 253 ? 12.324  25.029  9.039   1.00 31.32  ? 253  PHE A CG  1 
ATOM   1623  C  CD1 . PHE A  1 253 ? 11.366  24.744  9.978   1.00 31.69  ? 253  PHE A CD1 1 
ATOM   1624  C  CD2 . PHE A  1 253 ? 13.656  24.896  9.389   1.00 29.42  ? 253  PHE A CD2 1 
ATOM   1625  C  CE1 . PHE A  1 253 ? 11.727  24.319  11.235  1.00 29.36  ? 253  PHE A CE1 1 
ATOM   1626  C  CE2 . PHE A  1 253 ? 14.025  24.463  10.630  1.00 28.25  ? 253  PHE A CE2 1 
ATOM   1627  C  CZ  . PHE A  1 253 ? 13.056  24.167  11.563  1.00 29.25  ? 253  PHE A CZ  1 
ATOM   1628  N  N   . GLU A  1 254 ? 12.506  27.906  5.479   1.00 32.01  ? 254  GLU A N   1 
ATOM   1629  C  CA  . GLU A  1 254 ? 12.406  28.207  4.050   1.00 30.84  ? 254  GLU A CA  1 
ATOM   1630  C  C   . GLU A  1 254 ? 11.652  27.102  3.324   1.00 32.52  ? 254  GLU A C   1 
ATOM   1631  O  O   . GLU A  1 254 ? 11.838  25.925  3.611   1.00 41.75  ? 254  GLU A O   1 
ATOM   1632  C  CB  . GLU A  1 254 ? 13.806  28.395  3.445   1.00 36.36  ? 254  GLU A CB  1 
ATOM   1633  C  CG  . GLU A  1 254 ? 13.852  29.188  2.139   1.00 40.26  ? 254  GLU A CG  1 
ATOM   1634  C  CD  . GLU A  1 254 ? 15.244  29.210  1.438   1.00 53.31  ? 254  GLU A CD  1 
ATOM   1635  O  OE1 . GLU A  1 254 ? 16.299  29.111  2.126   1.00 41.13  ? 254  GLU A OE1 1 
ATOM   1636  O  OE2 . GLU A  1 254 ? 15.275  29.338  0.179   1.00 49.49  ? 254  GLU A OE2 1 
ATOM   1637  N  N   . THR A  1 255 ? 10.770  27.488  2.415   1.00 33.67  ? 255  THR A N   1 
ATOM   1638  C  CA  . THR A  1 255 ? 10.047  26.569  1.543   1.00 34.95  ? 255  THR A CA  1 
ATOM   1639  C  C   . THR A  1 255 ? 11.001  25.687  0.730   1.00 31.35  ? 255  THR A C   1 
ATOM   1640  O  O   . THR A  1 255 ? 11.977  26.191  0.194   1.00 36.75  ? 255  THR A O   1 
ATOM   1641  C  CB  . THR A  1 255 ? 9.148   27.372  0.583   1.00 35.38  ? 255  THR A CB  1 
ATOM   1642  O  OG1 . THR A  1 255 ? 8.337   28.269  1.349   1.00 37.58  ? 255  THR A OG1 1 
ATOM   1643  C  CG2 . THR A  1 255 ? 8.266   26.462  -0.266  1.00 33.53  ? 255  THR A CG2 1 
ATOM   1644  N  N   . THR A  1 256 ? 10.732  24.388  0.622   1.00 29.26  ? 256  THR A N   1 
ATOM   1645  C  CA  . THR A  1 256 ? 11.651  23.526  -0.145  1.00 34.19  ? 256  THR A CA  1 
ATOM   1646  C  C   . THR A  1 256 ? 11.451  23.729  -1.631  1.00 30.82  ? 256  THR A C   1 
ATOM   1647  O  O   . THR A  1 256 ? 10.422  24.252  -2.060  1.00 32.70  ? 256  THR A O   1 
ATOM   1648  C  CB  . THR A  1 256 ? 11.470  22.002  0.123   1.00 28.39  ? 256  THR A CB  1 
ATOM   1649  O  OG1 . THR A  1 256 ? 10.346  21.521  -0.620  1.00 29.08  ? 256  THR A OG1 1 
ATOM   1650  C  CG2 . THR A  1 256 ? 11.284  21.675  1.606   1.00 29.10  ? 256  THR A CG2 1 
ATOM   1651  N  N   . VAL A  1 257 ? 12.422  23.281  -2.416  1.00 28.19  ? 257  VAL A N   1 
ATOM   1652  C  CA  . VAL A  1 257 ? 12.207  23.115  -3.855  1.00 30.19  ? 257  VAL A CA  1 
ATOM   1653  C  C   . VAL A  1 257 ? 11.264  21.940  -4.108  1.00 29.43  ? 257  VAL A C   1 
ATOM   1654  O  O   . VAL A  1 257 ? 10.845  21.262  -3.177  1.00 29.41  ? 257  VAL A O   1 
ATOM   1655  C  CB  . VAL A  1 257 ? 13.499  22.873  -4.581  1.00 27.54  ? 257  VAL A CB  1 
ATOM   1656  C  CG1 . VAL A  1 257 ? 14.487  23.984  -4.255  1.00 27.18  ? 257  VAL A CG1 1 
ATOM   1657  C  CG2 . VAL A  1 257 ? 14.059  21.531  -4.178  1.00 30.50  ? 257  VAL A CG2 1 
ATOM   1658  N  N   . LYS A  1 258 ? 10.909  21.703  -5.359  1.00 26.69  ? 258  LYS A N   1 
ATOM   1659  C  CA  . LYS A  1 258 ? 10.095  20.527  -5.683  1.00 34.44  ? 258  LYS A CA  1 
ATOM   1660  C  C   . LYS A  1 258 ? 10.775  19.217  -5.229  1.00 32.31  ? 258  LYS A C   1 
ATOM   1661  O  O   . LYS A  1 258 ? 11.921  18.961  -5.598  1.00 28.33  ? 258  LYS A O   1 
ATOM   1662  C  CB  . LYS A  1 258 ? 9.819   20.483  -7.188  1.00 32.23  ? 258  LYS A CB  1 
ATOM   1663  C  CG  . LYS A  1 258 ? 9.001   21.652  -7.694  1.00 29.08  ? 258  LYS A CG  1 
ATOM   1664  C  CD  . LYS A  1 258 ? 7.538   21.509  -7.259  1.00 34.19  ? 258  LYS A CD  1 
ATOM   1665  C  CE  . LYS A  1 258 ? 6.677   22.672  -7.786  1.00 31.36  ? 258  LYS A CE  1 
ATOM   1666  N  NZ  . LYS A  1 258 ? 5.243   22.436  -7.482  1.00 34.33  ? 258  LYS A NZ  1 
ATOM   1667  N  N   . MET A  1 259 ? 10.089  18.414  -4.412  1.00 31.63  ? 259  MET A N   1 
ATOM   1668  C  CA  . MET A  1 259 ? 10.648  17.130  -3.966  1.00 26.87  ? 259  MET A CA  1 
ATOM   1669  C  C   . MET A  1 259 ? 9.593   16.098  -3.578  1.00 33.09  ? 259  MET A C   1 
ATOM   1670  O  O   . MET A  1 259 ? 8.437   16.443  -3.415  1.00 32.88  ? 259  MET A O   1 
ATOM   1671  C  CB  . MET A  1 259 ? 11.576  17.344  -2.783  1.00 26.34  ? 259  MET A CB  1 
ATOM   1672  C  CG  . MET A  1 259 ? 10.874  17.766  -1.477  1.00 31.17  ? 259  MET A CG  1 
ATOM   1673  S  SD  . MET A  1 259 ? 12.097  17.921  -0.143  1.00 35.93  ? 259  MET A SD  1 
ATOM   1674  C  CE  . MET A  1 259 ? 11.047  17.951  1.295   1.00 36.15  ? 259  MET A CE  1 
ATOM   1675  N  N   . SER A  1 260 ? 10.009  14.838  -3.402  1.00 31.96  ? 260  SER A N   1 
ATOM   1676  C  CA  . SER A  1 260 ? 9.093   13.750  -3.062  1.00 26.71  ? 260  SER A CA  1 
ATOM   1677  C  C   . SER A  1 260 ? 8.828   13.670  -1.576  1.00 29.03  ? 260  SER A C   1 
ATOM   1678  O  O   . SER A  1 260 ? 9.680   14.046  -0.776  1.00 28.73  ? 260  SER A O   1 
ATOM   1679  C  CB  . SER A  1 260 ? 9.643   12.395  -3.528  1.00 29.42  ? 260  SER A CB  1 
ATOM   1680  O  OG  . SER A  1 260 ? 10.153  12.438  -4.837  1.00 32.88  ? 260  SER A OG  1 
ATOM   1681  N  N   . THR A  1 261 ? 7.663   13.137  -1.209  1.00 28.09  ? 261  THR A N   1 
ATOM   1682  C  CA  . THR A  1 261 ? 7.243   13.126  0.190   1.00 22.20  ? 261  THR A CA  1 
ATOM   1683  C  C   . THR A  1 261 ? 8.172   12.324  1.088   1.00 27.72  ? 261  THR A C   1 
ATOM   1684  O  O   . THR A  1 261 ? 8.348   12.671  2.255   1.00 28.67  ? 261  THR A O   1 
ATOM   1685  C  CB  . THR A  1 261 ? 5.832   12.566  0.352   1.00 32.56  ? 261  THR A CB  1 
ATOM   1686  O  OG1 . THR A  1 261 ? 5.668   11.433  -0.512  1.00 35.05  ? 261  THR A OG1 1 
ATOM   1687  C  CG2 . THR A  1 261 ? 4.816   13.607  -0.004  1.00 31.19  ? 261  THR A CG2 1 
ATOM   1688  N  N   . TYR A  1 262 ? 8.788   11.272  0.552   1.00 25.43  ? 262  TYR A N   1 
ATOM   1689  C  CA  . TYR A  1 262 ? 9.547   10.377  1.395   1.00 23.54  ? 262  TYR A CA  1 
ATOM   1690  C  C   . TYR A  1 262 ? 10.823  11.023  1.912   1.00 27.26  ? 262  TYR A C   1 
ATOM   1691  O  O   . TYR A  1 262 ? 11.459  10.476  2.798   1.00 30.81  ? 262  TYR A O   1 
ATOM   1692  C  CB  . TYR A  1 262 ? 9.867   9.067   0.668   1.00 26.87  ? 262  TYR A CB  1 
ATOM   1693  C  CG  . TYR A  1 262 ? 10.916  9.121   -0.416  1.00 26.14  ? 262  TYR A CG  1 
ATOM   1694  C  CD1 . TYR A  1 262 ? 12.266  8.943   -0.125  1.00 26.20  ? 262  TYR A CD1 1 
ATOM   1695  C  CD2 . TYR A  1 262 ? 10.559  9.295   -1.733  1.00 29.71  ? 262  TYR A CD2 1 
ATOM   1696  C  CE1 . TYR A  1 262 ? 13.235  8.963   -1.111  1.00 26.10  ? 262  TYR A CE1 1 
ATOM   1697  C  CE2 . TYR A  1 262 ? 11.526  9.332   -2.750  1.00 32.22  ? 262  TYR A CE2 1 
ATOM   1698  C  CZ  . TYR A  1 262 ? 12.862  9.158   -2.434  1.00 35.24  ? 262  TYR A CZ  1 
ATOM   1699  O  OH  . TYR A  1 262 ? 13.805  9.188   -3.452  1.00 30.00  ? 262  TYR A OH  1 
ATOM   1700  N  N   . LEU A  1 263 ? 11.169  12.197  1.388   1.00 28.58  ? 263  LEU A N   1 
ATOM   1701  C  CA  . LEU A  1 263 ? 12.391  12.909  1.772   1.00 25.26  ? 263  LEU A CA  1 
ATOM   1702  C  C   . LEU A  1 263 ? 12.114  14.053  2.736   1.00 28.91  ? 263  LEU A C   1 
ATOM   1703  O  O   . LEU A  1 263 ? 13.052  14.661  3.255   1.00 28.28  ? 263  LEU A O   1 
ATOM   1704  C  CB  . LEU A  1 263 ? 13.104  13.471  0.532   1.00 26.38  ? 263  LEU A CB  1 
ATOM   1705  C  CG  . LEU A  1 263 ? 13.637  12.444  -0.456  1.00 31.25  ? 263  LEU A CG  1 
ATOM   1706  C  CD1 . LEU A  1 263 ? 13.656  13.032  -1.836  1.00 28.39  ? 263  LEU A CD1 1 
ATOM   1707  C  CD2 . LEU A  1 263 ? 15.035  11.973  -0.042  1.00 26.82  ? 263  LEU A CD2 1 
ATOM   1708  N  N   . VAL A  1 264 ? 10.837  14.372  2.951   1.00 24.96  ? 264  VAL A N   1 
ATOM   1709  C  CA  . VAL A  1 264 ? 10.496  15.395  3.928   1.00 26.12  ? 264  VAL A CA  1 
ATOM   1710  C  C   . VAL A  1 264 ? 11.095  15.005  5.271   1.00 26.64  ? 264  VAL A C   1 
ATOM   1711  O  O   . VAL A  1 264 ? 10.968  13.856  5.677   1.00 26.36  ? 264  VAL A O   1 
ATOM   1712  C  CB  . VAL A  1 264 ? 8.984   15.563  4.063   1.00 24.38  ? 264  VAL A CB  1 
ATOM   1713  C  CG1 . VAL A  1 264 ? 8.685   16.382  5.253   1.00 28.25  ? 264  VAL A CG1 1 
ATOM   1714  C  CG2 . VAL A  1 264 ? 8.401   16.210  2.816   1.00 22.83  ? 264  VAL A CG2 1 
ATOM   1715  N  N   . ALA A  1 265 ? 11.756  15.925  5.966   1.00 28.47  ? 265  ALA A N   1 
ATOM   1716  C  CA  . ALA A  1 265 ? 12.299  15.568  7.291   1.00 28.69  ? 265  ALA A CA  1 
ATOM   1717  C  C   . ALA A  1 265 ? 12.201  16.674  8.344   1.00 24.63  ? 265  ALA A C   1 
ATOM   1718  O  O   . ALA A  1 265 ? 12.257  17.835  8.017   1.00 29.13  ? 265  ALA A O   1 
ATOM   1719  C  CB  . ALA A  1 265 ? 13.753  15.131  7.159   1.00 25.98  ? 265  ALA A CB  1 
ATOM   1720  N  N   . TYR A  1 266 ? 12.076  16.303  9.613   1.00 26.95  ? 266  TYR A N   1 
ATOM   1721  C  CA  . TYR A  1 266 ? 12.137  17.273  10.702  1.00 26.34  ? 266  TYR A CA  1 
ATOM   1722  C  C   . TYR A  1 266 ? 12.466  16.584  12.017  1.00 27.83  ? 266  TYR A C   1 
ATOM   1723  O  O   . TYR A  1 266 ? 12.137  15.423  12.219  1.00 29.84  ? 266  TYR A O   1 
ATOM   1724  C  CB  . TYR A  1 266 ? 10.831  18.083  10.828  1.00 29.26  ? 266  TYR A CB  1 
ATOM   1725  C  CG  . TYR A  1 266 ? 9.545   17.306  10.607  1.00 31.64  ? 266  TYR A CG  1 
ATOM   1726  C  CD1 . TYR A  1 266 ? 8.895   16.681  11.668  1.00 29.75  ? 266  TYR A CD1 1 
ATOM   1727  C  CD2 . TYR A  1 266 ? 8.972   17.216  9.338   1.00 31.23  ? 266  TYR A CD2 1 
ATOM   1728  C  CE1 . TYR A  1 266 ? 7.714   15.984  11.475  1.00 26.43  ? 266  TYR A CE1 1 
ATOM   1729  C  CE2 . TYR A  1 266 ? 7.804   16.507  9.132   1.00 31.63  ? 266  TYR A CE2 1 
ATOM   1730  C  CZ  . TYR A  1 266 ? 7.177   15.904  10.208  1.00 28.59  ? 266  TYR A CZ  1 
ATOM   1731  O  OH  . TYR A  1 266 ? 6.025   15.203  9.993   1.00 32.27  ? 266  TYR A OH  1 
ATOM   1732  N  N   . ILE A  1 267 ? 13.166  17.309  12.886  1.00 26.13  ? 267  ILE A N   1 
ATOM   1733  C  CA  . ILE A  1 267 ? 13.736  16.741  14.085  1.00 28.72  ? 267  ILE A CA  1 
ATOM   1734  C  C   . ILE A  1 267 ? 13.628  17.717  15.241  1.00 32.45  ? 267  ILE A C   1 
ATOM   1735  O  O   . ILE A  1 267 ? 13.824  18.915  15.043  1.00 31.72  ? 267  ILE A O   1 
ATOM   1736  C  CB  . ILE A  1 267 ? 15.218  16.378  13.910  1.00 24.65  ? 267  ILE A CB  1 
ATOM   1737  C  CG1 . ILE A  1 267 ? 15.422  15.416  12.737  1.00 26.86  ? 267  ILE A CG1 1 
ATOM   1738  C  CG2 . ILE A  1 267 ? 15.742  15.779  15.211  1.00 24.98  ? 267  ILE A CG2 1 
ATOM   1739  C  CD1 . ILE A  1 267 ? 16.865  14.959  12.556  1.00 28.59  ? 267  ILE A CD1 1 
ATOM   1740  N  N   . VAL A  1 268 ? 13.297  17.211  16.432  1.00 28.73  ? 268  VAL A N   1 
ATOM   1741  C  CA  . VAL A  1 268 ? 13.374  18.015  17.631  1.00 29.29  ? 268  VAL A CA  1 
ATOM   1742  C  C   . VAL A  1 268 ? 14.349  17.333  18.609  1.00 31.21  ? 268  VAL A C   1 
ATOM   1743  O  O   . VAL A  1 268 ? 14.221  16.153  18.924  1.00 27.95  ? 268  VAL A O   1 
ATOM   1744  C  CB  . VAL A  1 268 ? 11.986  18.239  18.272  1.00 33.75  ? 268  VAL A CB  1 
ATOM   1745  C  CG1 . VAL A  1 268 ? 12.090  19.198  19.500  1.00 27.80  ? 268  VAL A CG1 1 
ATOM   1746  C  CG2 . VAL A  1 268 ? 11.021  18.810  17.259  1.00 28.80  ? 268  VAL A CG2 1 
ATOM   1747  N  N   . CYS A  1 269 ? 15.338  18.096  19.061  1.00 30.45  ? 269  CYS A N   1 
ATOM   1748  C  CA  . CYS A  1 269 ? 16.439  17.568  19.851  1.00 33.19  ? 269  CYS A CA  1 
ATOM   1749  C  C   . CYS A  1 269 ? 17.242  18.696  20.485  1.00 33.47  ? 269  CYS A C   1 
ATOM   1750  O  O   . CYS A  1 269 ? 16.891  19.866  20.369  1.00 37.87  ? 269  CYS A O   1 
ATOM   1751  C  CB  . CYS A  1 269 ? 17.355  16.690  18.991  1.00 28.01  ? 269  CYS A CB  1 
ATOM   1752  S  SG  . CYS A  1 269 ? 18.396  17.535  17.725  1.00 35.57  ? 269  CYS A SG  1 
ATOM   1753  N  N   . ASP A  1 270 ? 18.319  18.336  21.163  1.00 31.06  ? 270  ASP A N   1 
ATOM   1754  C  CA  . ASP A  1 270 ? 19.201  19.316  21.776  1.00 31.09  ? 270  ASP A CA  1 
ATOM   1755  C  C   . ASP A  1 270 ? 20.628  19.051  21.376  1.00 32.64  ? 270  ASP A C   1 
ATOM   1756  O  O   . ASP A  1 270 ? 21.508  19.098  22.206  1.00 36.21  ? 270  ASP A O   1 
ATOM   1757  C  CB  . ASP A  1 270 ? 19.074  19.294  23.307  1.00 33.90  ? 270  ASP A CB  1 
ATOM   1758  C  CG  . ASP A  1 270 ? 19.393  17.930  23.907  1.00 41.83  ? 270  ASP A CG  1 
ATOM   1759  O  OD1 . ASP A  1 270 ? 19.550  16.935  23.158  1.00 43.72  ? 270  ASP A OD1 1 
ATOM   1760  O  OD2 . ASP A  1 270 ? 19.488  17.837  25.142  1.00 50.02  ? 270  ASP A OD2 1 
ATOM   1761  N  N   . PHE A  1 271 ? 20.856  18.767  20.100  1.00 38.21  ? 271  PHE A N   1 
ATOM   1762  C  CA  . PHE A  1 271 ? 22.167  18.302  19.663  1.00 34.78  ? 271  PHE A CA  1 
ATOM   1763  C  C   . PHE A  1 271 ? 23.135  19.460  19.471  1.00 33.06  ? 271  PHE A C   1 
ATOM   1764  O  O   . PHE A  1 271 ? 22.706  20.587  19.308  1.00 36.03  ? 271  PHE A O   1 
ATOM   1765  C  CB  . PHE A  1 271 ? 22.022  17.494  18.378  1.00 27.45  ? 271  PHE A CB  1 
ATOM   1766  C  CG  . PHE A  1 271 ? 21.658  16.051  18.620  1.00 35.57  ? 271  PHE A CG  1 
ATOM   1767  C  CD1 . PHE A  1 271 ? 21.274  15.632  19.891  1.00 33.12  ? 271  PHE A CD1 1 
ATOM   1768  C  CD2 . PHE A  1 271 ? 21.747  15.094  17.590  1.00 28.48  ? 271  PHE A CD2 1 
ATOM   1769  C  CE1 . PHE A  1 271 ? 20.953  14.281  20.137  1.00 32.46  ? 271  PHE A CE1 1 
ATOM   1770  C  CE2 . PHE A  1 271 ? 21.439  13.766  17.825  1.00 29.49  ? 271  PHE A CE2 1 
ATOM   1771  C  CZ  . PHE A  1 271 ? 21.032  13.355  19.100  1.00 33.64  ? 271  PHE A CZ  1 
ATOM   1772  N  N   . HIS A  1 272 ? 24.436  19.186  19.490  1.00 27.94  ? 272  HIS A N   1 
ATOM   1773  C  CA  . HIS A  1 272 ? 25.438  20.208  19.141  1.00 33.72  ? 272  HIS A CA  1 
ATOM   1774  C  C   . HIS A  1 272 ? 25.936  20.012  17.711  1.00 33.14  ? 272  HIS A C   1 
ATOM   1775  O  O   . HIS A  1 272 ? 25.782  18.945  17.136  1.00 38.04  ? 272  HIS A O   1 
ATOM   1776  C  CB  . HIS A  1 272 ? 26.638  20.176  20.099  1.00 36.92  ? 272  HIS A CB  1 
ATOM   1777  C  CG  . HIS A  1 272 ? 26.356  20.744  21.455  1.00 40.36  ? 272  HIS A CG  1 
ATOM   1778  N  ND1 . HIS A  1 272 ? 25.122  21.245  21.816  1.00 38.97  ? 272  HIS A ND1 1 
ATOM   1779  C  CD2 . HIS A  1 272 ? 27.155  20.890  22.540  1.00 40.79  ? 272  HIS A CD2 1 
ATOM   1780  C  CE1 . HIS A  1 272 ? 25.170  21.673  23.065  1.00 32.16  ? 272  HIS A CE1 1 
ATOM   1781  N  NE2 . HIS A  1 272 ? 26.395  21.483  23.522  1.00 38.10  ? 272  HIS A NE2 1 
ATOM   1782  N  N   . SER A  1 273 ? 26.570  21.025  17.148  1.00 30.19  ? 273  SER A N   1 
ATOM   1783  C  CA  . SER A  1 273 ? 27.007  20.942  15.774  1.00 32.82  ? 273  SER A CA  1 
ATOM   1784  C  C   . SER A  1 273 ? 28.371  21.568  15.618  1.00 37.09  ? 273  SER A C   1 
ATOM   1785  O  O   . SER A  1 273 ? 28.776  22.355  16.455  1.00 37.76  ? 273  SER A O   1 
ATOM   1786  C  CB  . SER A  1 273 ? 26.008  21.640  14.862  1.00 33.29  ? 273  SER A CB  1 
ATOM   1787  O  OG  . SER A  1 273 ? 25.815  22.972  15.326  1.00 37.73  ? 273  SER A OG  1 
ATOM   1788  N  N   . LEU A  1 274 ? 29.080  21.160  14.568  1.00 31.75  ? 274  LEU A N   1 
ATOM   1789  C  CA  . LEU A  1 274 ? 30.237  21.865  14.041  1.00 28.35  ? 274  LEU A CA  1 
ATOM   1790  C  C   . LEU A  1 274 ? 29.890  22.168  12.599  1.00 33.85  ? 274  LEU A C   1 
ATOM   1791  O  O   . LEU A  1 274 ? 29.210  21.375  11.953  1.00 35.31  ? 274  LEU A O   1 
ATOM   1792  C  CB  . LEU A  1 274 ? 31.518  21.039  14.084  1.00 30.32  ? 274  LEU A CB  1 
ATOM   1793  C  CG  . LEU A  1 274 ? 32.073  20.547  15.418  1.00 44.51  ? 274  LEU A CG  1 
ATOM   1794  C  CD1 . LEU A  1 274 ? 33.356  19.770  15.192  1.00 43.71  ? 274  LEU A CD1 1 
ATOM   1795  C  CD2 . LEU A  1 274 ? 32.296  21.679  16.420  1.00 53.23  ? 274  LEU A CD2 1 
ATOM   1796  N  N   . SER A  1 275 ? 30.402  23.275  12.084  1.00 27.45  ? 275  SER A N   1 
ATOM   1797  C  CA  . SER A  1 275 ? 30.021  23.797  10.791  1.00 28.57  ? 275  SER A CA  1 
ATOM   1798  C  C   . SER A  1 275 ? 31.239  24.147  9.934   1.00 36.98  ? 275  SER A C   1 
ATOM   1799  O  O   . SER A  1 275 ? 32.337  24.391  10.444  1.00 33.20  ? 275  SER A O   1 
ATOM   1800  C  CB  . SER A  1 275 ? 29.144  25.044  10.953  1.00 29.35  ? 275  SER A CB  1 
ATOM   1801  O  OG  . SER A  1 275 ? 27.935  24.755  11.638  1.00 37.97  ? 275  SER A OG  1 
ATOM   1802  N  N   . GLY A  1 276 ? 31.020  24.187  8.623   1.00 32.04  ? 276  GLY A N   1 
ATOM   1803  C  CA  . GLY A  1 276 ? 32.015  24.653  7.678   1.00 29.41  ? 276  GLY A CA  1 
ATOM   1804  C  C   . GLY A  1 276 ? 31.291  25.023  6.406   1.00 30.77  ? 276  GLY A C   1 
ATOM   1805  O  O   . GLY A  1 276 ? 30.123  24.682  6.224   1.00 32.73  ? 276  GLY A O   1 
ATOM   1806  N  N   . PHE A  1 277 ? 31.975  25.729  5.522   1.00 32.72  ? 277  PHE A N   1 
ATOM   1807  C  CA  . PHE A  1 277 ? 31.380  26.069  4.243   1.00 25.77  ? 277  PHE A CA  1 
ATOM   1808  C  C   . PHE A  1 277 ? 32.121  25.333  3.154   1.00 26.40  ? 277  PHE A C   1 
ATOM   1809  O  O   . PHE A  1 277 ? 33.322  25.123  3.251   1.00 32.26  ? 277  PHE A O   1 
ATOM   1810  C  CB  . PHE A  1 277 ? 31.411  27.584  4.017   1.00 28.34  ? 277  PHE A CB  1 
ATOM   1811  C  CG  . PHE A  1 277 ? 30.459  28.338  4.893   1.00 27.33  ? 277  PHE A CG  1 
ATOM   1812  C  CD1 . PHE A  1 277 ? 30.831  28.722  6.169   1.00 31.42  ? 277  PHE A CD1 1 
ATOM   1813  C  CD2 . PHE A  1 277 ? 29.178  28.634  4.453   1.00 25.95  ? 277  PHE A CD2 1 
ATOM   1814  C  CE1 . PHE A  1 277 ? 29.940  29.398  7.000   1.00 30.36  ? 277  PHE A CE1 1 
ATOM   1815  C  CE2 . PHE A  1 277 ? 28.282  29.304  5.266   1.00 26.83  ? 277  PHE A CE2 1 
ATOM   1816  C  CZ  . PHE A  1 277 ? 28.662  29.696  6.547   1.00 27.29  ? 277  PHE A CZ  1 
ATOM   1817  N  N   . THR A  1 278 ? 31.391  24.883  2.146   1.00 26.48  ? 278  THR A N   1 
ATOM   1818  C  CA  . THR A  1 278 ? 32.012  24.379  0.926   1.00 31.17  ? 278  THR A CA  1 
ATOM   1819  C  C   . THR A  1 278 ? 32.499  25.511  0.032   1.00 32.20  ? 278  THR A C   1 
ATOM   1820  O  O   . THR A  1 278 ? 32.166  26.673  0.243   1.00 32.78  ? 278  THR A O   1 
ATOM   1821  C  CB  . THR A  1 278 ? 31.033  23.523  0.115   1.00 35.02  ? 278  THR A CB  1 
ATOM   1822  O  OG1 . THR A  1 278 ? 29.952  24.352  -0.324  1.00 35.23  ? 278  THR A OG1 1 
ATOM   1823  C  CG2 . THR A  1 278 ? 30.467  22.367  0.975   1.00 29.30  ? 278  THR A CG2 1 
ATOM   1824  N  N   . SER A  1 279 ? 33.268  25.151  -0.989  1.00 39.46  ? 279  SER A N   1 
ATOM   1825  C  CA  . SER A  1 279 ? 33.738  26.093  -2.006  1.00 35.79  ? 279  SER A CA  1 
ATOM   1826  C  C   . SER A  1 279 ? 32.614  26.906  -2.608  1.00 34.91  ? 279  SER A C   1 
ATOM   1827  O  O   . SER A  1 279 ? 32.791  28.084  -2.943  1.00 41.97  ? 279  SER A O   1 
ATOM   1828  C  CB  . SER A  1 279 ? 34.444  25.335  -3.116  1.00 36.81  ? 279  SER A CB  1 
ATOM   1829  O  OG  . SER A  1 279 ? 35.541  24.632  -2.591  1.00 48.14  ? 279  SER A OG  1 
ATOM   1830  N  N   . SER A  1 280 ? 31.468  26.256  -2.767  1.00 28.36  ? 280  SER A N   1 
ATOM   1831  C  CA  . SER A  1 280 ? 30.316  26.838  -3.413  1.00 32.00  ? 280  SER A CA  1 
ATOM   1832  C  C   . SER A  1 280 ? 29.400  27.493  -2.382  1.00 32.72  ? 280  SER A C   1 
ATOM   1833  O  O   . SER A  1 280 ? 28.315  27.999  -2.703  1.00 33.59  ? 280  SER A O   1 
ATOM   1834  C  CB  . SER A  1 280 ? 29.555  25.774  -4.198  1.00 36.62  ? 280  SER A CB  1 
ATOM   1835  O  OG  . SER A  1 280 ? 28.613  25.124  -3.346  1.00 37.96  ? 280  SER A OG  1 
ATOM   1836  N  N   . GLY A  1 281 ? 29.845  27.484  -1.134  1.00 36.65  ? 281  GLY A N   1 
ATOM   1837  C  CA  . GLY A  1 281 ? 29.187  28.266  -0.112  1.00 31.21  ? 281  GLY A CA  1 
ATOM   1838  C  C   . GLY A  1 281 ? 28.011  27.592  0.534   1.00 33.94  ? 281  GLY A C   1 
ATOM   1839  O  O   . GLY A  1 281 ? 27.133  28.286  1.028   1.00 36.08  ? 281  GLY A O   1 
ATOM   1840  N  N   . VAL A  1 282 ? 27.982  26.257  0.535   1.00 32.13  ? 282  VAL A N   1 
ATOM   1841  C  CA  . VAL A  1 282 ? 26.978  25.542  1.321   1.00 28.34  ? 282  VAL A CA  1 
ATOM   1842  C  C   . VAL A  1 282 ? 27.447  25.439  2.780   1.00 30.45  ? 282  VAL A C   1 
ATOM   1843  O  O   . VAL A  1 282 ? 28.598  25.046  3.073   1.00 29.97  ? 282  VAL A O   1 
ATOM   1844  C  CB  . VAL A  1 282 ? 26.673  24.118  0.761   1.00 28.96  ? 282  VAL A CB  1 
ATOM   1845  C  CG1 . VAL A  1 282 ? 25.567  23.442  1.581   1.00 24.93  ? 282  VAL A CG1 1 
ATOM   1846  C  CG2 . VAL A  1 282 ? 26.248  24.185  -0.693  1.00 28.36  ? 282  VAL A CG2 1 
ATOM   1847  N  N   . LYS A  1 283 ? 26.570  25.821  3.696   1.00 24.65  ? 283  LYS A N   1 
ATOM   1848  C  CA  . LYS A  1 283 ? 26.830  25.545  5.106   1.00 23.72  ? 283  LYS A CA  1 
ATOM   1849  C  C   . LYS A  1 283 ? 26.553  24.051  5.454   1.00 31.22  ? 283  LYS A C   1 
ATOM   1850  O  O   . LYS A  1 283 ? 25.395  23.572  5.441   1.00 25.10  ? 283  LYS A O   1 
ATOM   1851  C  CB  . LYS A  1 283 ? 26.002  26.460  5.993   1.00 26.50  ? 283  LYS A CB  1 
ATOM   1852  C  CG  . LYS A  1 283 ? 26.596  26.585  7.406   1.00 36.96  ? 283  LYS A CG  1 
ATOM   1853  C  CD  . LYS A  1 283 ? 25.698  27.339  8.389   1.00 32.27  ? 283  LYS A CD  1 
ATOM   1854  C  CE  . LYS A  1 283 ? 26.506  27.731  9.592   1.00 37.75  ? 283  LYS A CE  1 
ATOM   1855  N  NZ  . LYS A  1 283 ? 25.675  28.290  10.685  1.00 57.05  ? 283  LYS A NZ  1 
ATOM   1856  N  N   . VAL A  1 284 ? 27.638  23.324  5.727   1.00 30.91  ? 284  VAL A N   1 
ATOM   1857  C  CA  . VAL A  1 284 ? 27.572  21.926  6.148   1.00 28.53  ? 284  VAL A CA  1 
ATOM   1858  C  C   . VAL A  1 284 ? 27.724  21.843  7.664   1.00 27.91  ? 284  VAL A C   1 
ATOM   1859  O  O   . VAL A  1 284 ? 28.713  22.291  8.218   1.00 33.18  ? 284  VAL A O   1 
ATOM   1860  C  CB  . VAL A  1 284 ? 28.664  21.074  5.451   1.00 32.34  ? 284  VAL A CB  1 
ATOM   1861  C  CG1 . VAL A  1 284 ? 28.635  19.641  5.929   1.00 24.67  ? 284  VAL A CG1 1 
ATOM   1862  C  CG2 . VAL A  1 284 ? 28.496  21.130  3.937   1.00 27.56  ? 284  VAL A CG2 1 
ATOM   1863  N  N   . SER A  1 285 ? 26.722  21.305  8.337   1.00 30.10  ? 285  SER A N   1 
ATOM   1864  C  CA  . SER A  1 285 ? 26.783  21.113  9.785   1.00 26.86  ? 285  SER A CA  1 
ATOM   1865  C  C   . SER A  1 285 ? 26.713  19.629  10.133  1.00 28.26  ? 285  SER A C   1 
ATOM   1866  O  O   . SER A  1 285 ? 25.971  18.878  9.510   1.00 27.85  ? 285  SER A O   1 
ATOM   1867  C  CB  . SER A  1 285 ? 25.639  21.846  10.478  1.00 26.12  ? 285  SER A CB  1 
ATOM   1868  O  OG  . SER A  1 285 ? 25.822  23.245  10.434  1.00 37.90  ? 285  SER A OG  1 
ATOM   1869  N  N   . ILE A  1 286 ? 27.485  19.212  11.122  1.00 27.43  ? 286  ILE A N   1 
ATOM   1870  C  CA  . ILE A  1 286 ? 27.358  17.865  11.654  1.00 25.16  ? 286  ILE A CA  1 
ATOM   1871  C  C   . ILE A  1 286 ? 26.771  17.952  13.085  1.00 31.16  ? 286  ILE A C   1 
ATOM   1872  O  O   . ILE A  1 286 ? 27.361  18.583  13.963  1.00 30.30  ? 286  ILE A O   1 
ATOM   1873  C  CB  . ILE A  1 286 ? 28.721  17.111  11.675  1.00 22.71  ? 286  ILE A CB  1 
ATOM   1874  C  CG1 . ILE A  1 286 ? 29.517  17.314  10.378  1.00 26.66  ? 286  ILE A CG1 1 
ATOM   1875  C  CG2 . ILE A  1 286 ? 28.528  15.639  11.906  1.00 25.04  ? 286  ILE A CG2 1 
ATOM   1876  C  CD1 . ILE A  1 286 ? 28.825  16.909  9.112   1.00 24.29  ? 286  ILE A CD1 1 
ATOM   1877  N  N   . TYR A  1 287 ? 25.605  17.334  13.294  1.00 26.75  ? 287  TYR A N   1 
ATOM   1878  C  CA  . TYR A  1 287 ? 24.964  17.270  14.598  1.00 25.32  ? 287  TYR A CA  1 
ATOM   1879  C  C   . TYR A  1 287 ? 25.128  15.927  15.272  1.00 30.61  ? 287  TYR A C   1 
ATOM   1880  O  O   . TYR A  1 287 ? 25.138  14.865  14.645  1.00 29.32  ? 287  TYR A O   1 
ATOM   1881  C  CB  . TYR A  1 287 ? 23.467  17.571  14.500  1.00 27.39  ? 287  TYR A CB  1 
ATOM   1882  C  CG  . TYR A  1 287 ? 23.131  19.009  14.173  1.00 30.44  ? 287  TYR A CG  1 
ATOM   1883  C  CD1 . TYR A  1 287 ? 23.249  19.483  12.869  1.00 25.84  ? 287  TYR A CD1 1 
ATOM   1884  C  CD2 . TYR A  1 287 ? 22.703  19.907  15.164  1.00 32.46  ? 287  TYR A CD2 1 
ATOM   1885  C  CE1 . TYR A  1 287 ? 22.937  20.787  12.544  1.00 26.76  ? 287  TYR A CE1 1 
ATOM   1886  C  CE2 . TYR A  1 287 ? 22.387  21.229  14.844  1.00 27.61  ? 287  TYR A CE2 1 
ATOM   1887  C  CZ  . TYR A  1 287 ? 22.510  21.654  13.520  1.00 32.43  ? 287  TYR A CZ  1 
ATOM   1888  O  OH  . TYR A  1 287 ? 22.218  22.945  13.140  1.00 36.60  ? 287  TYR A OH  1 
ATOM   1889  N  N   . ALA A  1 288 ? 25.217  15.991  16.586  1.00 30.61  ? 288  ALA A N   1 
ATOM   1890  C  CA  . ALA A  1 288 ? 25.373  14.812  17.397  1.00 27.61  ? 288  ALA A CA  1 
ATOM   1891  C  C   . ALA A  1 288 ? 24.970  15.202  18.819  1.00 31.61  ? 288  ALA A C   1 
ATOM   1892  O  O   . ALA A  1 288 ? 24.857  16.379  19.139  1.00 36.02  ? 288  ALA A O   1 
ATOM   1893  C  CB  . ALA A  1 288 ? 26.801  14.304  17.335  1.00 22.22  ? 288  ALA A CB  1 
ATOM   1894  N  N   . SER A  1 289 ? 24.724  14.219  19.662  1.00 31.79  ? 289  SER A N   1 
ATOM   1895  C  CA  . SER A  1 289 ? 24.470  14.489  21.056  1.00 37.80  ? 289  SER A CA  1 
ATOM   1896  C  C   . SER A  1 289 ? 25.651  15.296  21.599  1.00 35.30  ? 289  SER A C   1 
ATOM   1897  O  O   . SER A  1 289 ? 26.777  15.159  21.114  1.00 33.39  ? 289  SER A O   1 
ATOM   1898  C  CB  . SER A  1 289 ? 24.255  13.175  21.826  1.00 33.77  ? 289  SER A CB  1 
ATOM   1899  O  OG  . SER A  1 289 ? 25.363  12.315  21.672  1.00 41.25  ? 289  SER A OG  1 
ATOM   1900  N  N   . PRO A  1 290 ? 25.386  16.168  22.582  1.00 34.82  ? 290  PRO A N   1 
ATOM   1901  C  CA  . PRO A  1 290 ? 26.347  17.226  22.935  1.00 36.93  ? 290  PRO A CA  1 
ATOM   1902  C  C   . PRO A  1 290 ? 27.690  16.694  23.440  1.00 33.59  ? 290  PRO A C   1 
ATOM   1903  O  O   . PRO A  1 290 ? 28.715  17.276  23.132  1.00 34.20  ? 290  PRO A O   1 
ATOM   1904  C  CB  . PRO A  1 290 ? 25.614  18.010  24.031  1.00 36.84  ? 290  PRO A CB  1 
ATOM   1905  C  CG  . PRO A  1 290 ? 24.156  17.712  23.799  1.00 33.40  ? 290  PRO A CG  1 
ATOM   1906  C  CD  . PRO A  1 290 ? 24.126  16.291  23.334  1.00 33.22  ? 290  PRO A CD  1 
ATOM   1907  N  N   . ASP A  1 291 ? 27.696  15.598  24.182  1.00 32.80  ? 291  ASP A N   1 
ATOM   1908  C  CA  . ASP A  1 291 ? 28.964  15.049  24.654  1.00 33.65  ? 291  ASP A CA  1 
ATOM   1909  C  C   . ASP A  1 291 ? 29.803  14.387  23.568  1.00 40.21  ? 291  ASP A C   1 
ATOM   1910  O  O   . ASP A  1 291 ? 30.888  13.887  23.846  1.00 39.76  ? 291  ASP A O   1 
ATOM   1911  C  CB  . ASP A  1 291 ? 28.710  14.038  25.757  1.00 41.31  ? 291  ASP A CB  1 
ATOM   1912  C  CG  . ASP A  1 291 ? 28.062  14.668  26.978  1.00 44.83  ? 291  ASP A CG  1 
ATOM   1913  O  OD1 . ASP A  1 291 ? 28.499  15.777  27.391  1.00 36.80  ? 291  ASP A OD1 1 
ATOM   1914  O  OD2 . ASP A  1 291 ? 27.102  14.061  27.500  1.00 46.87  ? 291  ASP A OD2 1 
ATOM   1915  N  N   . LYS A  1 292 ? 29.311  14.375  22.331  1.00 37.46  ? 292  LYS A N   1 
ATOM   1916  C  CA  . LYS A  1 292 ? 29.995  13.638  21.292  1.00 35.76  ? 292  LYS A CA  1 
ATOM   1917  C  C   . LYS A  1 292 ? 30.501  14.547  20.196  1.00 35.84  ? 292  LYS A C   1 
ATOM   1918  O  O   . LYS A  1 292 ? 31.028  14.063  19.200  1.00 35.71  ? 292  LYS A O   1 
ATOM   1919  C  CB  . LYS A  1 292 ? 29.077  12.557  20.713  1.00 38.78  ? 292  LYS A CB  1 
ATOM   1920  C  CG  . LYS A  1 292 ? 29.038  11.273  21.555  1.00 29.00  ? 292  LYS A CG  1 
ATOM   1921  C  CD  . LYS A  1 292 ? 28.220  10.180  20.866  1.00 35.20  ? 292  LYS A CD  1 
ATOM   1922  C  CE  . LYS A  1 292 ? 28.101  8.905   21.708  1.00 40.80  ? 292  LYS A CE  1 
ATOM   1923  N  NZ  . LYS A  1 292 ? 27.492  7.780   20.949  1.00 39.31  ? 292  LYS A NZ  1 
ATOM   1924  N  N   . ARG A  1 293 ? 30.383  15.859  20.410  1.00 38.13  ? 293  ARG A N   1 
ATOM   1925  C  CA  . ARG A  1 293 ? 30.706  16.835  19.374  1.00 44.84  ? 293  ARG A CA  1 
ATOM   1926  C  C   . ARG A  1 293 ? 32.123  16.615  18.841  1.00 39.22  ? 293  ARG A C   1 
ATOM   1927  O  O   . ARG A  1 293 ? 32.407  16.785  17.661  1.00 35.71  ? 293  ARG A O   1 
ATOM   1928  C  CB  . ARG A  1 293 ? 30.547  18.258  19.908  1.00 44.94  ? 293  ARG A CB  1 
ATOM   1929  C  CG  . ARG A  1 293 ? 30.616  19.303  18.807  1.00 49.67  ? 293  ARG A CG  1 
ATOM   1930  C  CD  . ARG A  1 293 ? 30.473  20.701  19.338  1.00 40.76  ? 293  ARG A CD  1 
ATOM   1931  N  NE  . ARG A  1 293 ? 31.611  21.025  20.178  1.00 50.20  ? 293  ARG A NE  1 
ATOM   1932  C  CZ  . ARG A  1 293 ? 31.639  22.053  21.014  1.00 48.37  ? 293  ARG A CZ  1 
ATOM   1933  N  NH1 . ARG A  1 293 ? 30.588  22.850  21.114  1.00 52.28  ? 293  ARG A NH1 1 
ATOM   1934  N  NH2 . ARG A  1 293 ? 32.707  22.266  21.752  1.00 49.05  ? 293  ARG A NH2 1 
ATOM   1935  N  N   . ASN A  1 294 ? 32.992  16.205  19.743  1.00 36.93  ? 294  ASN A N   1 
ATOM   1936  C  CA  . ASN A  1 294 ? 34.339  15.765  19.425  1.00 41.60  ? 294  ASN A CA  1 
ATOM   1937  C  C   . ASN A  1 294 ? 34.424  14.804  18.222  1.00 40.12  ? 294  ASN A C   1 
ATOM   1938  O  O   . ASN A  1 294 ? 35.415  14.776  17.494  1.00 39.49  ? 294  ASN A O   1 
ATOM   1939  C  CB  . ASN A  1 294 ? 34.921  15.072  20.667  1.00 47.88  ? 294  ASN A CB  1 
ATOM   1940  C  CG  . ASN A  1 294 ? 36.338  15.472  20.938  1.00 58.56  ? 294  ASN A CG  1 
ATOM   1941  O  OD1 . ASN A  1 294 ? 36.962  16.138  20.110  1.00 60.82  ? 294  ASN A OD1 1 
ATOM   1942  N  ND2 . ASN A  1 294 ? 36.876  15.056  22.100  1.00 62.11  ? 294  ASN A ND2 1 
ATOM   1943  N  N   . GLN A  1 295 ? 33.390  13.994  18.026  1.00 36.93  ? 295  GLN A N   1 
ATOM   1944  C  CA  . GLN A  1 295 ? 33.509  12.870  17.113  1.00 35.87  ? 295  GLN A CA  1 
ATOM   1945  C  C   . GLN A  1 295 ? 33.030  13.218  15.702  1.00 33.77  ? 295  GLN A C   1 
ATOM   1946  O  O   . GLN A  1 295 ? 32.987  12.363  14.822  1.00 30.38  ? 295  GLN A O   1 
ATOM   1947  C  CB  . GLN A  1 295 ? 32.749  11.652  17.672  1.00 32.56  ? 295  GLN A CB  1 
ATOM   1948  C  CG  . GLN A  1 295 ? 33.440  10.928  18.844  1.00 27.98  ? 295  GLN A CG  1 
ATOM   1949  C  CD  . GLN A  1 295 ? 32.531  9.886   19.503  1.00 30.49  ? 295  GLN A CD  1 
ATOM   1950  O  OE1 . GLN A  1 295 ? 31.908  9.066   18.837  1.00 30.76  ? 295  GLN A OE1 1 
ATOM   1951  N  NE2 . GLN A  1 295 ? 32.444  9.933   20.812  1.00 31.46  ? 295  GLN A NE2 1 
ATOM   1952  N  N   . THR A  1 296 ? 32.696  14.478  15.480  1.00 32.37  ? 296  THR A N   1 
ATOM   1953  C  CA  . THR A  1 296 ? 32.066  14.842  14.240  1.00 25.05  ? 296  THR A CA  1 
ATOM   1954  C  C   . THR A  1 296 ? 33.067  15.447  13.294  1.00 30.53  ? 296  THR A C   1 
ATOM   1955  O  O   . THR A  1 296 ? 32.724  15.776  12.166  1.00 28.73  ? 296  THR A O   1 
ATOM   1956  C  CB  . THR A  1 296 ? 30.933  15.826  14.446  1.00 26.97  ? 296  THR A CB  1 
ATOM   1957  O  OG1 . THR A  1 296 ? 31.446  17.018  15.038  1.00 31.80  ? 296  THR A OG1 1 
ATOM   1958  C  CG2 . THR A  1 296 ? 29.876  15.230  15.331  1.00 32.97  ? 296  THR A CG2 1 
ATOM   1959  N  N   . HIS A  1 297 ? 34.309  15.570  13.740  1.00 33.28  ? 297  HIS A N   1 
ATOM   1960  C  CA  . HIS A  1 297 ? 35.304  16.301  12.961  1.00 31.84  ? 297  HIS A CA  1 
ATOM   1961  C  C   . HIS A  1 297 ? 35.574  15.651  11.623  1.00 28.26  ? 297  HIS A C   1 
ATOM   1962  O  O   . HIS A  1 297 ? 35.646  16.333  10.592  1.00 28.00  ? 297  HIS A O   1 
ATOM   1963  C  CB  . HIS A  1 297 ? 36.616  16.455  13.757  1.00 34.77  ? 297  HIS A CB  1 
ATOM   1964  C  CG  . HIS A  1 297 ? 36.569  17.567  14.752  1.00 36.23  ? 297  HIS A CG  1 
ATOM   1965  N  ND1 . HIS A  1 297 ? 36.373  17.354  16.099  1.00 41.19  ? 297  HIS A ND1 1 
ATOM   1966  C  CD2 . HIS A  1 297 ? 36.643  18.910  14.593  1.00 45.81  ? 297  HIS A CD2 1 
ATOM   1967  C  CE1 . HIS A  1 297 ? 36.340  18.515  16.729  1.00 45.59  ? 297  HIS A CE1 1 
ATOM   1968  N  NE2 . HIS A  1 297 ? 36.497  19.477  15.838  1.00 41.96  ? 297  HIS A NE2 1 
ATOM   1969  N  N   . TYR A  1 298 ? 35.705  14.330  11.625  1.00 30.51  ? 298  TYR A N   1 
ATOM   1970  C  CA  . TYR A  1 298 ? 36.060  13.665  10.385  1.00 27.44  ? 298  TYR A CA  1 
ATOM   1971  C  C   . TYR A  1 298 ? 34.933  13.807  9.381   1.00 28.02  ? 298  TYR A C   1 
ATOM   1972  O  O   . TYR A  1 298 ? 35.177  14.016  8.199   1.00 33.52  ? 298  TYR A O   1 
ATOM   1973  C  CB  . TYR A  1 298 ? 36.392  12.195  10.592  1.00 31.15  ? 298  TYR A CB  1 
ATOM   1974  C  CG  . TYR A  1 298 ? 36.642  11.559  9.265   1.00 31.55  ? 298  TYR A CG  1 
ATOM   1975  C  CD1 . TYR A  1 298 ? 37.733  11.946  8.494   1.00 28.08  ? 298  TYR A CD1 1 
ATOM   1976  C  CD2 . TYR A  1 298 ? 35.743  10.642  8.729   1.00 29.65  ? 298  TYR A CD2 1 
ATOM   1977  C  CE1 . TYR A  1 298 ? 37.944  11.409  7.241   1.00 28.75  ? 298  TYR A CE1 1 
ATOM   1978  C  CE2 . TYR A  1 298 ? 35.950  10.100  7.472   1.00 29.35  ? 298  TYR A CE2 1 
ATOM   1979  C  CZ  . TYR A  1 298 ? 37.049  10.485  6.741   1.00 27.53  ? 298  TYR A CZ  1 
ATOM   1980  O  OH  . TYR A  1 298 ? 37.256  9.926   5.509   1.00 34.88  ? 298  TYR A OH  1 
ATOM   1981  N  N   . ALA A  1 299 ? 33.701  13.705  9.860   1.00 26.44  ? 299  ALA A N   1 
ATOM   1982  C  CA  . ALA A  1 299 ? 32.540  13.816  8.994   1.00 30.91  ? 299  ALA A CA  1 
ATOM   1983  C  C   . ALA A  1 299 ? 32.472  15.197  8.345   1.00 25.96  ? 299  ALA A C   1 
ATOM   1984  O  O   . ALA A  1 299 ? 32.126  15.322  7.188   1.00 26.02  ? 299  ALA A O   1 
ATOM   1985  C  CB  . ALA A  1 299 ? 31.250  13.526  9.780   1.00 27.23  ? 299  ALA A CB  1 
ATOM   1986  N  N   . LEU A  1 300 ? 32.829  16.229  9.089   1.00 24.81  ? 300  LEU A N   1 
ATOM   1987  C  CA  . LEU A  1 300 ? 32.769  17.577  8.539   1.00 31.71  ? 300  LEU A CA  1 
ATOM   1988  C  C   . LEU A  1 300 ? 33.791  17.705  7.422   1.00 29.80  ? 300  LEU A C   1 
ATOM   1989  O  O   . LEU A  1 300 ? 33.508  18.202  6.333   1.00 30.58  ? 300  LEU A O   1 
ATOM   1990  C  CB  . LEU A  1 300 ? 33.017  18.637  9.615   1.00 27.89  ? 300  LEU A CB  1 
ATOM   1991  C  CG  . LEU A  1 300 ? 33.022  20.073  9.073   1.00 28.95  ? 300  LEU A CG  1 
ATOM   1992  C  CD1 . LEU A  1 300 ? 31.684  20.421  8.455   1.00 24.84  ? 300  LEU A CD1 1 
ATOM   1993  C  CD2 . LEU A  1 300 ? 33.383  21.078  10.186  1.00 28.76  ? 300  LEU A CD2 1 
ATOM   1994  N  N   . GLN A  1 301 ? 34.983  17.213  7.704   1.00 29.93  ? 301  GLN A N   1 
ATOM   1995  C  CA  . GLN A  1 301 ? 36.032  17.228  6.726   1.00 27.35  ? 301  GLN A CA  1 
ATOM   1996  C  C   . GLN A  1 301 ? 35.602  16.439  5.462   1.00 30.82  ? 301  GLN A C   1 
ATOM   1997  O  O   . GLN A  1 301 ? 35.646  16.984  4.358   1.00 35.23  ? 301  GLN A O   1 
ATOM   1998  C  CB  . GLN A  1 301 ? 37.313  16.688  7.366   1.00 28.53  ? 301  GLN A CB  1 
ATOM   1999  C  CG  . GLN A  1 301 ? 38.394  16.176  6.372   1.00 38.87  ? 301  GLN A CG  1 
ATOM   2000  C  CD  . GLN A  1 301 ? 39.595  15.552  7.096   1.00 41.60  ? 301  GLN A CD  1 
ATOM   2001  O  OE1 . GLN A  1 301 ? 39.837  15.835  8.272   1.00 55.54  ? 301  GLN A OE1 1 
ATOM   2002  N  NE2 . GLN A  1 301 ? 40.331  14.690  6.406   1.00 43.73  ? 301  GLN A NE2 1 
ATOM   2003  N  N   . ALA A  1 302 ? 35.129  15.200  5.608   1.00 27.09  ? 302  ALA A N   1 
ATOM   2004  C  CA  . ALA A  1 302 ? 34.781  14.394  4.418   1.00 30.89  ? 302  ALA A CA  1 
ATOM   2005  C  C   . ALA A  1 302 ? 33.581  14.936  3.631   1.00 32.96  ? 302  ALA A C   1 
ATOM   2006  O  O   . ALA A  1 302 ? 33.612  14.981  2.380   1.00 32.28  ? 302  ALA A O   1 
ATOM   2007  C  CB  . ALA A  1 302 ? 34.522  12.928  4.804   1.00 24.74  ? 302  ALA A CB  1 
ATOM   2008  N  N   . SER A  1 303 ? 32.530  15.347  4.338   1.00 27.02  ? 303  SER A N   1 
ATOM   2009  C  CA  . SER A  1 303 ? 31.353  15.818  3.625   1.00 29.30  ? 303  SER A CA  1 
ATOM   2010  C  C   . SER A  1 303 ? 31.660  17.099  2.845   1.00 27.29  ? 303  SER A C   1 
ATOM   2011  O  O   . SER A  1 303 ? 31.140  17.262  1.756   1.00 33.08  ? 303  SER A O   1 
ATOM   2012  C  CB  . SER A  1 303 ? 30.149  16.006  4.574   1.00 27.79  ? 303  SER A CB  1 
ATOM   2013  O  OG  . SER A  1 303 ? 30.451  16.830  5.684   1.00 29.15  ? 303  SER A OG  1 
ATOM   2014  N  N   . LEU A  1 304 ? 32.515  17.987  3.356   1.00 32.40  ? 304  LEU A N   1 
ATOM   2015  C  CA  . LEU A  1 304 ? 32.910  19.185  2.557   1.00 35.91  ? 304  LEU A CA  1 
ATOM   2016  C  C   . LEU A  1 304 ? 33.656  18.778  1.294   1.00 32.05  ? 304  LEU A C   1 
ATOM   2017  O  O   . LEU A  1 304 ? 33.327  19.193  0.185   1.00 33.82  ? 304  LEU A O   1 
ATOM   2018  C  CB  . LEU A  1 304 ? 33.815  20.153  3.337   1.00 29.25  ? 304  LEU A CB  1 
ATOM   2019  C  CG  . LEU A  1 304 ? 33.378  20.911  4.585   1.00 27.83  ? 304  LEU A CG  1 
ATOM   2020  C  CD1 . LEU A  1 304 ? 34.544  21.796  5.012   1.00 28.59  ? 304  LEU A CD1 1 
ATOM   2021  C  CD2 . LEU A  1 304 ? 32.103  21.731  4.402   1.00 24.27  ? 304  LEU A CD2 1 
ATOM   2022  N  N   . LYS A  1 305 ? 34.681  17.959  1.479   1.00 31.74  ? 305  LYS A N   1 
ATOM   2023  C  CA  . LYS A  1 305 ? 35.459  17.459  0.354   1.00 35.47  ? 305  LYS A CA  1 
ATOM   2024  C  C   . LYS A  1 305 ? 34.581  16.709  -0.685  1.00 34.46  ? 305  LYS A C   1 
ATOM   2025  O  O   . LYS A  1 305 ? 34.750  16.867  -1.888  1.00 31.57  ? 305  LYS A O   1 
ATOM   2026  C  CB  . LYS A  1 305 ? 36.560  16.560  0.890   1.00 34.11  ? 305  LYS A CB  1 
ATOM   2027  C  CG  . LYS A  1 305 ? 37.891  16.748  0.255   1.00 37.88  ? 305  LYS A CG  1 
ATOM   2028  C  CD  . LYS A  1 305 ? 38.958  16.012  1.072   1.00 44.95  ? 305  LYS A CD  1 
ATOM   2029  C  CE  . LYS A  1 305 ? 40.342  16.107  0.419   1.00 48.70  ? 305  LYS A CE  1 
ATOM   2030  N  NZ  . LYS A  1 305 ? 40.389  15.504  -0.962  1.00 42.02  ? 305  LYS A NZ  1 
ATOM   2031  N  N   . LEU A  1 306 ? 33.625  15.916  -0.209  1.00 32.70  ? 306  LEU A N   1 
ATOM   2032  C  CA  . LEU A  1 306 ? 32.830  15.095  -1.109  1.00 30.61  ? 306  LEU A CA  1 
ATOM   2033  C  C   . LEU A  1 306 ? 31.754  15.926  -1.779  1.00 31.14  ? 306  LEU A C   1 
ATOM   2034  O  O   . LEU A  1 306 ? 31.461  15.711  -2.956  1.00 33.80  ? 306  LEU A O   1 
ATOM   2035  C  CB  . LEU A  1 306 ? 32.205  13.886  -0.366  1.00 29.11  ? 306  LEU A CB  1 
ATOM   2036  C  CG  . LEU A  1 306 ? 33.106  12.664  -0.093  1.00 26.39  ? 306  LEU A CG  1 
ATOM   2037  C  CD1 . LEU A  1 306 ? 32.612  11.824  1.123   1.00 21.53  ? 306  LEU A CD1 1 
ATOM   2038  C  CD2 . LEU A  1 306 ? 33.233  11.795  -1.335  1.00 25.22  ? 306  LEU A CD2 1 
ATOM   2039  N  N   . LEU A  1 307 ? 31.148  16.863  -1.053  1.00 29.56  ? 307  LEU A N   1 
ATOM   2040  C  CA  . LEU A  1 307 ? 30.133  17.702  -1.683  1.00 28.84  ? 307  LEU A CA  1 
ATOM   2041  C  C   . LEU A  1 307 ? 30.778  18.516  -2.829  1.00 36.33  ? 307  LEU A C   1 
ATOM   2042  O  O   . LEU A  1 307 ? 30.209  18.626  -3.928  1.00 34.68  ? 307  LEU A O   1 
ATOM   2043  C  CB  . LEU A  1 307 ? 29.454  18.621  -0.673  1.00 29.80  ? 307  LEU A CB  1 
ATOM   2044  C  CG  . LEU A  1 307 ? 28.077  19.055  -1.194  1.00 35.42  ? 307  LEU A CG  1 
ATOM   2045  C  CD1 . LEU A  1 307 ? 27.143  17.887  -1.146  1.00 30.92  ? 307  LEU A CD1 1 
ATOM   2046  C  CD2 . LEU A  1 307 ? 27.470  20.232  -0.438  1.00 26.35  ? 307  LEU A CD2 1 
ATOM   2047  N  N   . ASP A  1 308 ? 31.976  19.053  -2.585  1.00 37.28  ? 308  ASP A N   1 
ATOM   2048  C  CA  . ASP A  1 308 ? 32.718  19.778  -3.621  1.00 31.92  ? 308  ASP A CA  1 
ATOM   2049  C  C   . ASP A  1 308 ? 32.961  18.912  -4.860  1.00 38.18  ? 308  ASP A C   1 
ATOM   2050  O  O   . ASP A  1 308 ? 32.691  19.344  -5.993  1.00 36.70  ? 308  ASP A O   1 
ATOM   2051  C  CB  . ASP A  1 308 ? 34.066  20.296  -3.084  1.00 34.00  ? 308  ASP A CB  1 
ATOM   2052  C  CG  . ASP A  1 308 ? 33.915  21.510  -2.176  1.00 42.29  ? 308  ASP A CG  1 
ATOM   2053  O  OD1 . ASP A  1 308 ? 32.980  22.326  -2.393  1.00 46.71  ? 308  ASP A OD1 1 
ATOM   2054  O  OD2 . ASP A  1 308 ? 34.733  21.658  -1.230  1.00 52.59  ? 308  ASP A OD2 1 
ATOM   2055  N  N   . PHE A  1 309 ? 33.469  17.696  -4.656  1.00 37.12  ? 309  PHE A N   1 
ATOM   2056  C  CA  . PHE A  1 309 ? 33.683  16.788  -5.777  1.00 32.41  ? 309  PHE A CA  1 
ATOM   2057  C  C   . PHE A  1 309 ? 32.381  16.541  -6.528  1.00 33.80  ? 309  PHE A C   1 
ATOM   2058  O  O   . PHE A  1 309 ? 32.348  16.591  -7.738  1.00 35.10  ? 309  PHE A O   1 
ATOM   2059  C  CB  . PHE A  1 309 ? 34.272  15.455  -5.324  1.00 30.61  ? 309  PHE A CB  1 
ATOM   2060  C  CG  . PHE A  1 309 ? 34.184  14.400  -6.361  1.00 29.27  ? 309  PHE A CG  1 
ATOM   2061  C  CD1 . PHE A  1 309 ? 33.060  13.601  -6.468  1.00 32.36  ? 309  PHE A CD1 1 
ATOM   2062  C  CD2 . PHE A  1 309 ? 35.204  14.224  -7.259  1.00 32.77  ? 309  PHE A CD2 1 
ATOM   2063  C  CE1 . PHE A  1 309 ? 32.957  12.667  -7.471  1.00 33.80  ? 309  PHE A CE1 1 
ATOM   2064  C  CE2 . PHE A  1 309 ? 35.109  13.286  -8.256  1.00 31.19  ? 309  PHE A CE2 1 
ATOM   2065  C  CZ  . PHE A  1 309 ? 33.992  12.508  -8.366  1.00 30.78  ? 309  PHE A CZ  1 
ATOM   2066  N  N   . TYR A  1 310 ? 31.298  16.261  -5.829  1.00 30.43  ? 310  TYR A N   1 
ATOM   2067  C  CA  . TYR A  1 310 ? 30.072  16.004  -6.568  1.00 30.31  ? 310  TYR A CA  1 
ATOM   2068  C  C   . TYR A  1 310 ? 29.595  17.190  -7.415  1.00 32.83  ? 310  TYR A C   1 
ATOM   2069  O  O   . TYR A  1 310 ? 28.983  17.001  -8.467  1.00 36.69  ? 310  TYR A O   1 
ATOM   2070  C  CB  . TYR A  1 310 ? 28.971  15.572  -5.613  1.00 30.68  ? 310  TYR A CB  1 
ATOM   2071  C  CG  . TYR A  1 310 ? 29.088  14.128  -5.160  1.00 33.29  ? 310  TYR A CG  1 
ATOM   2072  C  CD1 . TYR A  1 310 ? 29.319  13.101  -6.080  1.00 25.46  ? 310  TYR A CD1 1 
ATOM   2073  C  CD2 . TYR A  1 310 ? 28.978  13.796  -3.803  1.00 26.01  ? 310  TYR A CD2 1 
ATOM   2074  C  CE1 . TYR A  1 310 ? 29.417  11.784  -5.655  1.00 29.08  ? 310  TYR A CE1 1 
ATOM   2075  C  CE2 . TYR A  1 310 ? 29.077  12.501  -3.376  1.00 23.88  ? 310  TYR A CE2 1 
ATOM   2076  C  CZ  . TYR A  1 310 ? 29.289  11.493  -4.296  1.00 31.65  ? 310  TYR A CZ  1 
ATOM   2077  O  OH  . TYR A  1 310 ? 29.383  10.194  -3.853  1.00 28.54  ? 310  TYR A OH  1 
ATOM   2078  N  N   . GLU A  1 311 ? 29.863  18.410  -6.980  1.00 34.73  ? 311  GLU A N   1 
ATOM   2079  C  CA  . GLU A  1 311 ? 29.402  19.573  -7.740  1.00 34.58  ? 311  GLU A CA  1 
ATOM   2080  C  C   . GLU A  1 311 ? 30.209  19.701  -9.054  1.00 32.71  ? 311  GLU A C   1 
ATOM   2081  O  O   . GLU A  1 311 ? 29.660  19.973  -10.116 1.00 32.64  ? 311  GLU A O   1 
ATOM   2082  C  CB  . GLU A  1 311 ? 29.485  20.851  -6.879  1.00 29.16  ? 311  GLU A CB  1 
ATOM   2083  C  CG  . GLU A  1 311 ? 28.461  20.868  -5.771  1.00 34.09  ? 311  GLU A CG  1 
ATOM   2084  C  CD  . GLU A  1 311 ? 28.345  22.208  -5.053  1.00 36.78  ? 311  GLU A CD  1 
ATOM   2085  O  OE1 . GLU A  1 311 ? 29.389  22.823  -4.763  1.00 40.88  ? 311  GLU A OE1 1 
ATOM   2086  O  OE2 . GLU A  1 311 ? 27.209  22.629  -4.749  1.00 33.61  ? 311  GLU A OE2 1 
ATOM   2087  N  N   . LYS A  1 312 ? 31.507  19.453  -8.971  1.00 38.68  ? 312  LYS A N   1 
ATOM   2088  C  CA  . LYS A  1 312 ? 32.364  19.419  -10.149 1.00 39.27  ? 312  LYS A CA  1 
ATOM   2089  C  C   . LYS A  1 312 ? 31.948  18.275  -11.059 1.00 35.09  ? 312  LYS A C   1 
ATOM   2090  O  O   . LYS A  1 312 ? 31.655  18.467  -12.224 1.00 37.32  ? 312  LYS A O   1 
ATOM   2091  C  CB  . LYS A  1 312 ? 33.837  19.276  -9.733  1.00 41.29  ? 312  LYS A CB  1 
ATOM   2092  C  CG  . LYS A  1 312 ? 34.848  19.379  -10.867 1.00 54.54  ? 312  LYS A CG  1 
ATOM   2093  C  CD  . LYS A  1 312 ? 35.151  20.821  -11.267 1.00 67.49  ? 312  LYS A CD  1 
ATOM   2094  C  CE  . LYS A  1 312 ? 36.466  20.912  -12.061 1.00 76.54  ? 312  LYS A CE  1 
ATOM   2095  N  NZ  . LYS A  1 312 ? 37.649  20.422  -11.275 1.00 65.40  ? 312  LYS A NZ  1 
ATOM   2096  N  N   . TYR A  1 313 ? 31.894  17.074  -10.512 1.00 40.52  ? 313  TYR A N   1 
ATOM   2097  C  CA  . TYR A  1 313 ? 31.634  15.900  -11.333 1.00 36.80  ? 313  TYR A CA  1 
ATOM   2098  C  C   . TYR A  1 313 ? 30.280  15.980  -12.033 1.00 36.67  ? 313  TYR A C   1 
ATOM   2099  O  O   . TYR A  1 313 ? 30.190  15.696  -13.229 1.00 30.87  ? 313  TYR A O   1 
ATOM   2100  C  CB  . TYR A  1 313 ? 31.719  14.622  -10.499 1.00 33.48  ? 313  TYR A CB  1 
ATOM   2101  C  CG  . TYR A  1 313 ? 31.729  13.391  -11.357 1.00 36.76  ? 313  TYR A CG  1 
ATOM   2102  C  CD1 . TYR A  1 313 ? 32.860  13.054  -12.093 1.00 34.09  ? 313  TYR A CD1 1 
ATOM   2103  C  CD2 . TYR A  1 313 ? 30.597  12.582  -11.469 1.00 33.36  ? 313  TYR A CD2 1 
ATOM   2104  C  CE1 . TYR A  1 313 ? 32.875  11.932  -12.898 1.00 36.53  ? 313  TYR A CE1 1 
ATOM   2105  C  CE2 . TYR A  1 313 ? 30.604  11.461  -12.276 1.00 32.40  ? 313  TYR A CE2 1 
ATOM   2106  C  CZ  . TYR A  1 313 ? 31.747  11.140  -12.982 1.00 37.78  ? 313  TYR A CZ  1 
ATOM   2107  O  OH  . TYR A  1 313 ? 31.769  10.035  -13.794 1.00 41.78  ? 313  TYR A OH  1 
ATOM   2108  N  N   . PHE A  1 314 ? 29.232  16.368  -11.307 1.00 32.37  ? 314  PHE A N   1 
ATOM   2109  C  CA  . PHE A  1 314 ? 27.896  16.349  -11.908 1.00 33.16  ? 314  PHE A CA  1 
ATOM   2110  C  C   . PHE A  1 314 ? 27.651  17.601  -12.752 1.00 33.90  ? 314  PHE A C   1 
ATOM   2111  O  O   . PHE A  1 314 ? 26.666  17.666  -13.488 1.00 30.47  ? 314  PHE A O   1 
ATOM   2112  C  CB  . PHE A  1 314 ? 26.801  16.219  -10.831 1.00 31.09  ? 314  PHE A CB  1 
ATOM   2113  C  CG  . PHE A  1 314 ? 26.788  14.893  -10.132 1.00 30.40  ? 314  PHE A CG  1 
ATOM   2114  C  CD1 . PHE A  1 314 ? 27.015  13.721  -10.834 1.00 34.12  ? 314  PHE A CD1 1 
ATOM   2115  C  CD2 . PHE A  1 314 ? 26.584  14.820  -8.764  1.00 34.46  ? 314  PHE A CD2 1 
ATOM   2116  C  CE1 . PHE A  1 314 ? 27.019  12.511  -10.200 1.00 33.34  ? 314  PHE A CE1 1 
ATOM   2117  C  CE2 . PHE A  1 314 ? 26.577  13.595  -8.115  1.00 33.48  ? 314  PHE A CE2 1 
ATOM   2118  C  CZ  . PHE A  1 314 ? 26.805  12.445  -8.828  1.00 30.56  ? 314  PHE A CZ  1 
ATOM   2119  N  N   . ASP A  1 315 ? 28.559  18.577  -12.632 1.00 34.69  ? 315  ASP A N   1 
ATOM   2120  C  CA  . ASP A  1 315 ? 28.367  19.928  -13.145 1.00 35.16  ? 315  ASP A CA  1 
ATOM   2121  C  C   . ASP A  1 315 ? 27.034  20.540  -12.695 1.00 35.28  ? 315  ASP A C   1 
ATOM   2122  O  O   . ASP A  1 315 ? 26.376  21.243  -13.454 1.00 42.93  ? 315  ASP A O   1 
ATOM   2123  C  CB  . ASP A  1 315 ? 28.454  19.939  -14.684 1.00 36.30  ? 315  ASP A CB  1 
ATOM   2124  C  CG  . ASP A  1 315 ? 28.547  21.360  -15.260 1.00 46.43  ? 315  ASP A CG  1 
ATOM   2125  O  OD1 . ASP A  1 315 ? 29.396  22.150  -14.773 1.00 43.21  ? 315  ASP A OD1 1 
ATOM   2126  O  OD2 . ASP A  1 315 ? 27.749  21.693  -16.173 1.00 44.55  ? 315  ASP A OD2 1 
ATOM   2127  N  N   . ILE A  1 316 ? 26.621  20.277  -11.463 1.00 37.85  ? 316  ILE A N   1 
ATOM   2128  C  CA  . ILE A  1 316 ? 25.387  20.882  -10.933 1.00 34.66  ? 316  ILE A CA  1 
ATOM   2129  C  C   . ILE A  1 316 ? 25.549  21.235  -9.473  1.00 38.33  ? 316  ILE A C   1 
ATOM   2130  O  O   . ILE A  1 316 ? 25.918  20.376  -8.673  1.00 36.69  ? 316  ILE A O   1 
ATOM   2131  C  CB  . ILE A  1 316 ? 24.175  19.953  -11.015 1.00 35.31  ? 316  ILE A CB  1 
ATOM   2132  C  CG1 . ILE A  1 316 ? 23.937  19.431  -12.426 1.00 31.51  ? 316  ILE A CG1 1 
ATOM   2133  C  CG2 . ILE A  1 316 ? 22.929  20.640  -10.477 1.00 27.09  ? 316  ILE A CG2 1 
ATOM   2134  C  CD1 . ILE A  1 316 ? 22.801  18.446  -12.439 1.00 27.26  ? 316  ILE A CD1 1 
ATOM   2135  N  N   . TYR A  1 317 ? 25.249  22.477  -9.106  1.00 38.78  ? 317  TYR A N   1 
ATOM   2136  C  CA  . TYR A  1 317 ? 25.406  22.871  -7.720  1.00 33.85  ? 317  TYR A CA  1 
ATOM   2137  C  C   . TYR A  1 317 ? 24.400  22.141  -6.850  1.00 33.14  ? 317  TYR A C   1 
ATOM   2138  O  O   . TYR A  1 317 ? 23.295  21.841  -7.307  1.00 31.26  ? 317  TYR A O   1 
ATOM   2139  C  CB  . TYR A  1 317 ? 25.231  24.381  -7.559  1.00 33.49  ? 317  TYR A CB  1 
ATOM   2140  C  CG  . TYR A  1 317 ? 26.348  25.202  -8.131  1.00 32.53  ? 317  TYR A CG  1 
ATOM   2141  C  CD1 . TYR A  1 317 ? 27.605  25.174  -7.566  1.00 33.89  ? 317  TYR A CD1 1 
ATOM   2142  C  CD2 . TYR A  1 317 ? 26.139  26.022  -9.232  1.00 32.40  ? 317  TYR A CD2 1 
ATOM   2143  C  CE1 . TYR A  1 317 ? 28.623  25.912  -8.078  1.00 37.97  ? 317  TYR A CE1 1 
ATOM   2144  C  CE2 . TYR A  1 317 ? 27.151  26.773  -9.752  1.00 32.07  ? 317  TYR A CE2 1 
ATOM   2145  C  CZ  . TYR A  1 317 ? 28.400  26.718  -9.178  1.00 40.55  ? 317  TYR A CZ  1 
ATOM   2146  O  OH  . TYR A  1 317 ? 29.431  27.483  -9.684  1.00 42.37  ? 317  TYR A OH  1 
ATOM   2147  N  N   . TYR A  1 318 ? 24.790  21.841  -5.610  1.00 29.97  ? 318  TYR A N   1 
ATOM   2148  C  CA  . TYR A  1 318 ? 23.824  21.499  -4.577  1.00 30.33  ? 318  TYR A CA  1 
ATOM   2149  C  C   . TYR A  1 318 ? 22.962  22.742  -4.414  1.00 36.50  ? 318  TYR A C   1 
ATOM   2150  O  O   . TYR A  1 318 ? 23.484  23.835  -4.156  1.00 39.69  ? 318  TYR A O   1 
ATOM   2151  C  CB  . TYR A  1 318 ? 24.521  21.131  -3.272  1.00 34.00  ? 318  TYR A CB  1 
ATOM   2152  C  CG  . TYR A  1 318 ? 23.606  20.872  -2.098  1.00 27.78  ? 318  TYR A CG  1 
ATOM   2153  C  CD1 . TYR A  1 318 ? 22.989  19.629  -1.918  1.00 26.15  ? 318  TYR A CD1 1 
ATOM   2154  C  CD2 . TYR A  1 318 ? 23.391  21.849  -1.148  1.00 27.64  ? 318  TYR A CD2 1 
ATOM   2155  C  CE1 . TYR A  1 318 ? 22.154  19.389  -0.831  1.00 23.75  ? 318  TYR A CE1 1 
ATOM   2156  C  CE2 . TYR A  1 318 ? 22.559  21.629  -0.059  1.00 26.80  ? 318  TYR A CE2 1 
ATOM   2157  C  CZ  . TYR A  1 318 ? 21.937  20.405  0.093   1.00 28.45  ? 318  TYR A CZ  1 
ATOM   2158  O  OH  . TYR A  1 318 ? 21.117  20.198  1.187   1.00 30.27  ? 318  TYR A OH  1 
ATOM   2159  N  N   . PRO A  1 319 ? 21.649  22.600  -4.591  1.00 28.58  ? 319  PRO A N   1 
ATOM   2160  C  CA  . PRO A  1 319 ? 20.761  23.771  -4.693  1.00 22.38  ? 319  PRO A CA  1 
ATOM   2161  C  C   . PRO A  1 319 ? 20.419  24.454  -3.359  1.00 31.85  ? 319  PRO A C   1 
ATOM   2162  O  O   . PRO A  1 319 ? 20.054  25.627  -3.352  1.00 31.22  ? 319  PRO A O   1 
ATOM   2163  C  CB  . PRO A  1 319 ? 19.491  23.200  -5.343  1.00 23.40  ? 319  PRO A CB  1 
ATOM   2164  C  CG  . PRO A  1 319 ? 19.528  21.703  -5.080  1.00 24.10  ? 319  PRO A CG  1 
ATOM   2165  C  CD  . PRO A  1 319 ? 20.947  21.315  -4.692  1.00 26.00  ? 319  PRO A CD  1 
ATOM   2166  N  N   . LEU A  1 320 ? 20.527  23.747  -2.244  1.00 32.22  ? 320  LEU A N   1 
ATOM   2167  C  CA  . LEU A  1 320 ? 20.089  24.310  -0.981  1.00 27.47  ? 320  LEU A CA  1 
ATOM   2168  C  C   . LEU A  1 320 ? 21.244  25.045  -0.298  1.00 34.19  ? 320  LEU A C   1 
ATOM   2169  O  O   . LEU A  1 320 ? 22.416  24.830  -0.639  1.00 27.98  ? 320  LEU A O   1 
ATOM   2170  C  CB  . LEU A  1 320 ? 19.529  23.216  -0.091  1.00 30.05  ? 320  LEU A CB  1 
ATOM   2171  C  CG  . LEU A  1 320 ? 18.484  22.317  -0.757  1.00 31.04  ? 320  LEU A CG  1 
ATOM   2172  C  CD1 . LEU A  1 320 ? 17.943  21.343  0.271   1.00 29.84  ? 320  LEU A CD1 1 
ATOM   2173  C  CD2 . LEU A  1 320 ? 17.343  23.136  -1.333  1.00 25.71  ? 320  LEU A CD2 1 
ATOM   2174  N  N   . SER A  1 321 ? 20.925  25.911  0.663   1.00 30.84  ? 321  SER A N   1 
ATOM   2175  C  CA  . SER A  1 321 ? 21.955  26.799  1.174   1.00 33.20  ? 321  SER A CA  1 
ATOM   2176  C  C   . SER A  1 321 ? 22.682  26.156  2.362   1.00 33.94  ? 321  SER A C   1 
ATOM   2177  O  O   . SER A  1 321 ? 23.798  26.563  2.740   1.00 34.27  ? 321  SER A O   1 
ATOM   2178  C  CB  . SER A  1 321 ? 21.346  28.157  1.539   1.00 37.93  ? 321  SER A CB  1 
ATOM   2179  O  OG  . SER A  1 321 ? 21.554  28.468  2.903   1.00 44.75  ? 321  SER A OG  1 
ATOM   2180  N  N   . LYS A  1 322 ? 22.062  25.138  2.938   1.00 25.76  ? 322  LYS A N   1 
ATOM   2181  C  CA  . LYS A  1 322 ? 22.732  24.365  3.967   1.00 28.84  ? 322  LYS A CA  1 
ATOM   2182  C  C   . LYS A  1 322 ? 22.578  22.843  3.757   1.00 30.87  ? 322  LYS A C   1 
ATOM   2183  O  O   . LYS A  1 322 ? 21.637  22.366  3.117   1.00 27.85  ? 322  LYS A O   1 
ATOM   2184  C  CB  . LYS A  1 322 ? 22.221  24.767  5.363   1.00 28.06  ? 322  LYS A CB  1 
ATOM   2185  C  CG  . LYS A  1 322 ? 20.766  24.453  5.672   1.00 31.46  ? 322  LYS A CG  1 
ATOM   2186  C  CD  . LYS A  1 322 ? 20.566  23.047  6.294   1.00 32.90  ? 322  LYS A CD  1 
ATOM   2187  C  CE  . LYS A  1 322 ? 19.098  22.808  6.702   1.00 32.99  ? 322  LYS A CE  1 
ATOM   2188  N  NZ  . LYS A  1 322 ? 18.842  21.471  7.320   1.00 28.49  ? 322  LYS A NZ  1 
ATOM   2189  N  N   . LEU A  1 323 ? 23.512  22.093  4.319   1.00 25.58  ? 323  LEU A N   1 
ATOM   2190  C  CA  . LEU A  1 323 ? 23.399  20.646  4.374   1.00 24.19  ? 323  LEU A CA  1 
ATOM   2191  C  C   . LEU A  1 323 ? 23.745  20.178  5.780   1.00 29.12  ? 323  LEU A C   1 
ATOM   2192  O  O   . LEU A  1 323 ? 24.840  20.445  6.274   1.00 27.91  ? 323  LEU A O   1 
ATOM   2193  C  CB  . LEU A  1 323 ? 24.311  19.968  3.327   1.00 23.68  ? 323  LEU A CB  1 
ATOM   2194  C  CG  . LEU A  1 323 ? 24.383  18.436  3.436   1.00 25.27  ? 323  LEU A CG  1 
ATOM   2195  C  CD1 . LEU A  1 323 ? 23.008  17.835  3.292   1.00 22.91  ? 323  LEU A CD1 1 
ATOM   2196  C  CD2 . LEU A  1 323 ? 25.354  17.841  2.396   1.00 29.88  ? 323  LEU A CD2 1 
ATOM   2197  N  N   . ASP A  1 324 ? 22.793  19.500  6.423   1.00 28.18  ? 324  ASP A N   1 
ATOM   2198  C  CA  . ASP A  1 324 ? 22.998  18.952  7.767   1.00 21.98  ? 324  ASP A CA  1 
ATOM   2199  C  C   . ASP A  1 324 ? 23.139  17.435  7.779   1.00 25.25  ? 324  ASP A C   1 
ATOM   2200  O  O   . ASP A  1 324 ? 22.404  16.705  7.108   1.00 23.95  ? 324  ASP A O   1 
ATOM   2201  C  CB  . ASP A  1 324 ? 21.859  19.350  8.688   1.00 25.03  ? 324  ASP A CB  1 
ATOM   2202  C  CG  . ASP A  1 324 ? 21.857  20.845  8.990   1.00 32.15  ? 324  ASP A CG  1 
ATOM   2203  O  OD1 . ASP A  1 324 ? 22.914  21.498  8.876   1.00 30.11  ? 324  ASP A OD1 1 
ATOM   2204  O  OD2 . ASP A  1 324 ? 20.791  21.371  9.357   1.00 36.57  ? 324  ASP A OD2 1 
ATOM   2205  N  N   . LEU A  1 325 ? 24.126  16.973  8.530   1.00 24.69  ? 325  LEU A N   1 
ATOM   2206  C  CA  . LEU A  1 325 ? 24.323  15.555  8.759   1.00 22.62  ? 325  LEU A CA  1 
ATOM   2207  C  C   . LEU A  1 325 ? 24.182  15.311  10.275  1.00 28.51  ? 325  LEU A C   1 
ATOM   2208  O  O   . LEU A  1 325 ? 24.903  15.908  11.085  1.00 28.00  ? 325  LEU A O   1 
ATOM   2209  C  CB  . LEU A  1 325 ? 25.679  15.093  8.241   1.00 21.06  ? 325  LEU A CB  1 
ATOM   2210  C  CG  . LEU A  1 325 ? 25.963  14.960  6.742   1.00 24.71  ? 325  LEU A CG  1 
ATOM   2211  C  CD1 . LEU A  1 325 ? 25.923  16.307  6.030   1.00 27.67  ? 325  LEU A CD1 1 
ATOM   2212  C  CD2 . LEU A  1 325 ? 27.324  14.305  6.538   1.00 24.26  ? 325  LEU A CD2 1 
ATOM   2213  N  N   . ILE A  1 326 ? 23.233  14.466  10.656  1.00 22.92  ? 326  ILE A N   1 
ATOM   2214  C  CA  . ILE A  1 326 ? 22.955  14.279  12.056  1.00 23.48  ? 326  ILE A CA  1 
ATOM   2215  C  C   . ILE A  1 326 ? 23.001  12.816  12.505  1.00 29.07  ? 326  ILE A C   1 
ATOM   2216  O  O   . ILE A  1 326 ? 22.348  11.936  11.919  1.00 26.83  ? 326  ILE A O   1 
ATOM   2217  C  CB  . ILE A  1 326 ? 21.596  14.913  12.406  1.00 29.75  ? 326  ILE A CB  1 
ATOM   2218  C  CG1 . ILE A  1 326 ? 21.218  14.617  13.856  1.00 29.18  ? 326  ILE A CG1 1 
ATOM   2219  C  CG2 . ILE A  1 326 ? 20.520  14.527  11.397  1.00 25.19  ? 326  ILE A CG2 1 
ATOM   2220  C  CD1 . ILE A  1 326 ? 20.146  15.540  14.342  1.00 26.19  ? 326  ILE A CD1 1 
ATOM   2221  N  N   . ALA A  1 327 ? 23.808  12.573  13.540  1.00 28.04  ? 327  ALA A N   1 
ATOM   2222  C  CA  . ALA A  1 327 ? 24.004  11.232  14.072  1.00 28.16  ? 327  ALA A CA  1 
ATOM   2223  C  C   . ALA A  1 327 ? 22.905  10.890  15.051  1.00 32.41  ? 327  ALA A C   1 
ATOM   2224  O  O   . ALA A  1 327 ? 22.944  11.327  16.189  1.00 35.09  ? 327  ALA A O   1 
ATOM   2225  C  CB  . ALA A  1 327 ? 25.358  11.107  14.747  1.00 28.48  ? 327  ALA A CB  1 
ATOM   2226  N  N   . ILE A  1 328 ? 21.931  10.110  14.586  1.00 35.94  ? 328  ILE A N   1 
ATOM   2227  C  CA  . ILE A  1 328 ? 20.792  9.653   15.379  1.00 33.54  ? 328  ILE A CA  1 
ATOM   2228  C  C   . ILE A  1 328 ? 21.096  8.370   16.143  1.00 37.03  ? 328  ILE A C   1 
ATOM   2229  O  O   . ILE A  1 328 ? 21.523  7.378   15.552  1.00 41.96  ? 328  ILE A O   1 
ATOM   2230  C  CB  . ILE A  1 328 ? 19.570  9.375   14.489  1.00 32.55  ? 328  ILE A CB  1 
ATOM   2231  C  CG1 . ILE A  1 328 ? 19.244  10.575  13.621  1.00 32.45  ? 328  ILE A CG1 1 
ATOM   2232  C  CG2 . ILE A  1 328 ? 18.375  9.034   15.337  1.00 42.25  ? 328  ILE A CG2 1 
ATOM   2233  C  CD1 . ILE A  1 328 ? 18.661  11.698  14.378  1.00 31.39  ? 328  ILE A CD1 1 
ATOM   2234  N  N   . PRO A  1 329 ? 20.840  8.371   17.457  1.00 43.82  ? 329  PRO A N   1 
ATOM   2235  C  CA  . PRO A  1 329 ? 21.112  7.248   18.379  1.00 43.35  ? 329  PRO A CA  1 
ATOM   2236  C  C   . PRO A  1 329 ? 20.263  5.971   18.148  1.00 45.25  ? 329  PRO A C   1 
ATOM   2237  O  O   . PRO A  1 329 ? 20.813  4.870   18.236  1.00 40.19  ? 329  PRO A O   1 
ATOM   2238  C  CB  . PRO A  1 329 ? 20.805  7.853   19.753  1.00 34.74  ? 329  PRO A CB  1 
ATOM   2239  C  CG  . PRO A  1 329 ? 20.904  9.327   19.554  1.00 36.84  ? 329  PRO A CG  1 
ATOM   2240  C  CD  . PRO A  1 329 ? 20.424  9.587   18.177  1.00 37.93  ? 329  PRO A CD  1 
ATOM   2241  N  N   . ASP A  1 330 ? 18.959  6.107   17.893  1.00 45.84  ? 330  ASP A N   1 
ATOM   2242  C  CA  . ASP A  1 330 ? 18.133  4.966   17.461  1.00 42.35  ? 330  ASP A CA  1 
ATOM   2243  C  C   . ASP A  1 330 ? 17.781  5.100   16.005  1.00 49.89  ? 330  ASP A C   1 
ATOM   2244  O  O   . ASP A  1 330 ? 16.760  5.708   15.666  1.00 50.84  ? 330  ASP A O   1 
ATOM   2245  C  CB  . ASP A  1 330 ? 16.807  4.848   18.227  1.00 48.43  ? 330  ASP A CB  1 
ATOM   2246  C  CG  . ASP A  1 330 ? 16.982  4.798   19.718  1.00 49.88  ? 330  ASP A CG  1 
ATOM   2247  O  OD1 . ASP A  1 330 ? 17.256  3.698   20.244  1.00 48.61  ? 330  ASP A OD1 1 
ATOM   2248  O  OD2 . ASP A  1 330 ? 16.816  5.868   20.360  1.00 53.50  ? 330  ASP A OD2 1 
ATOM   2249  N  N   . PHE A  1 331 ? 18.596  4.538   15.129  1.00 46.97  ? 331  PHE A N   1 
ATOM   2250  C  CA  . PHE A  1 331 ? 18.286  4.679   13.728  1.00 41.90  ? 331  PHE A CA  1 
ATOM   2251  C  C   . PHE A  1 331 ? 18.336  3.312   13.028  1.00 43.36  ? 331  PHE A C   1 
ATOM   2252  O  O   . PHE A  1 331 ? 19.364  2.646   13.014  1.00 43.70  ? 331  PHE A O   1 
ATOM   2253  C  CB  . PHE A  1 331 ? 19.233  5.699   13.080  1.00 35.78  ? 331  PHE A CB  1 
ATOM   2254  C  CG  . PHE A  1 331 ? 18.676  6.312   11.825  1.00 39.07  ? 331  PHE A CG  1 
ATOM   2255  C  CD1 . PHE A  1 331 ? 17.514  7.075   11.873  1.00 34.79  ? 331  PHE A CD1 1 
ATOM   2256  C  CD2 . PHE A  1 331 ? 19.288  6.095   10.593  1.00 35.39  ? 331  PHE A CD2 1 
ATOM   2257  C  CE1 . PHE A  1 331 ? 16.982  7.623   10.726  1.00 31.91  ? 331  PHE A CE1 1 
ATOM   2258  C  CE2 . PHE A  1 331 ? 18.756  6.640   9.425   1.00 35.01  ? 331  PHE A CE2 1 
ATOM   2259  C  CZ  . PHE A  1 331 ? 17.605  7.400   9.492   1.00 35.47  ? 331  PHE A CZ  1 
ATOM   2260  N  N   . ALA A  1 332 ? 17.206  2.902   12.459  1.00 39.24  ? 332  ALA A N   1 
ATOM   2261  C  CA  . ALA A  1 332 ? 17.092  1.596   11.828  1.00 44.32  ? 332  ALA A CA  1 
ATOM   2262  C  C   . ALA A  1 332 ? 17.950  1.464   10.554  1.00 42.38  ? 332  ALA A C   1 
ATOM   2263  O  O   . ALA A  1 332 ? 18.796  0.560   10.488  1.00 35.04  ? 332  ALA A O   1 
ATOM   2264  C  CB  . ALA A  1 332 ? 15.624  1.280   11.526  1.00 41.36  ? 332  ALA A CB  1 
ATOM   2265  N  N   . PRO A  1 333 ? 17.755  2.359   9.551   1.00 36.39  ? 333  PRO A N   1 
ATOM   2266  C  CA  . PRO A  1 333 ? 18.649  2.224   8.397   1.00 33.55  ? 333  PRO A CA  1 
ATOM   2267  C  C   . PRO A  1 333 ? 20.051  2.669   8.772   1.00 37.38  ? 333  PRO A C   1 
ATOM   2268  O  O   . PRO A  1 333 ? 20.256  3.257   9.848   1.00 33.54  ? 333  PRO A O   1 
ATOM   2269  C  CB  . PRO A  1 333 ? 18.033  3.159   7.348   1.00 35.93  ? 333  PRO A CB  1 
ATOM   2270  C  CG  . PRO A  1 333 ? 16.816  3.792   8.011   1.00 37.31  ? 333  PRO A CG  1 
ATOM   2271  C  CD  . PRO A  1 333 ? 16.984  3.610   9.476   1.00 35.12  ? 333  PRO A CD  1 
ATOM   2272  N  N   . GLY A  1 334 ? 21.012  2.388   7.904   1.00 35.58  ? 334  GLY A N   1 
ATOM   2273  C  CA  . GLY A  1 334 ? 22.368  2.847   8.145   1.00 37.84  ? 334  GLY A CA  1 
ATOM   2274  C  C   . GLY A  1 334 ? 22.427  4.367   8.093   1.00 34.21  ? 334  GLY A C   1 
ATOM   2275  O  O   . GLY A  1 334 ? 23.230  5.013   8.784   1.00 30.84  ? 334  GLY A O   1 
ATOM   2276  N  N   . ALA A  1 335 ? 21.530  4.921   7.284   1.00 30.90  ? 335  ALA A N   1 
ATOM   2277  C  CA  . ALA A  1 335 ? 21.572  6.307   6.885   1.00 28.46  ? 335  ALA A CA  1 
ATOM   2278  C  C   . ALA A  1 335 ? 20.348  6.613   6.016   1.00 33.52  ? 335  ALA A C   1 
ATOM   2279  O  O   . ALA A  1 335 ? 19.773  5.687   5.434   1.00 30.16  ? 335  ALA A O   1 
ATOM   2280  C  CB  . ALA A  1 335 ? 22.838  6.582   6.158   1.00 23.44  ? 335  ALA A CB  1 
ATOM   2281  N  N   . MET A  1 336 ? 19.940  7.885   5.945   1.00 25.71  ? 336  MET A N   1 
ATOM   2282  C  CA  . MET A  1 336 ? 18.806  8.299   5.109   1.00 22.66  ? 336  MET A CA  1 
ATOM   2283  C  C   . MET A  1 336 ? 19.009  9.700   4.520   1.00 26.86  ? 336  MET A C   1 
ATOM   2284  O  O   . MET A  1 336 ? 19.358  10.621  5.237   1.00 27.77  ? 336  MET A O   1 
ATOM   2285  C  CB  . MET A  1 336 ? 17.503  8.282   5.891   1.00 31.01  ? 336  MET A CB  1 
ATOM   2286  C  CG  . MET A  1 336 ? 16.302  8.669   5.042   1.00 30.29  ? 336  MET A CG  1 
ATOM   2287  S  SD  . MET A  1 336 ? 16.164  7.575   3.606   1.00 29.70  ? 336  MET A SD  1 
ATOM   2288  C  CE  . MET A  1 336 ? 15.276  8.657   2.515   1.00 23.34  ? 336  MET A CE  1 
ATOM   2289  N  N   . GLU A  1 337 ? 18.769  9.862   3.218   1.00 25.95  ? 337  GLU A N   1 
ATOM   2290  C  CA  . GLU A  1 337 ? 19.274  11.023  2.501   1.00 24.93  ? 337  GLU A CA  1 
ATOM   2291  C  C   . GLU A  1 337 ? 18.311  12.199  2.421   1.00 25.68  ? 337  GLU A C   1 
ATOM   2292  O  O   . GLU A  1 337 ? 18.369  12.942  1.443   1.00 25.58  ? 337  GLU A O   1 
ATOM   2293  C  CB  . GLU A  1 337 ? 19.682  10.632  1.061   1.00 25.60  ? 337  GLU A CB  1 
ATOM   2294  C  CG  . GLU A  1 337 ? 18.523  10.212  0.119   1.00 25.01  ? 337  GLU A CG  1 
ATOM   2295  C  CD  . GLU A  1 337 ? 18.212  8.703   0.140   1.00 32.75  ? 337  GLU A CD  1 
ATOM   2296  O  OE1 . GLU A  1 337 ? 18.903  7.946   0.871   1.00 29.41  ? 337  GLU A OE1 1 
ATOM   2297  O  OE2 . GLU A  1 337 ? 17.281  8.279   -0.587  1.00 29.04  ? 337  GLU A OE2 1 
ATOM   2298  N  N   . ASN A  1 338 ? 17.436  12.359  3.413   1.00 22.55  ? 338  ASN A N   1 
ATOM   2299  C  CA  . ASN A  1 338 ? 16.538  13.504  3.445   1.00 23.23  ? 338  ASN A CA  1 
ATOM   2300  C  C   . ASN A  1 338 ? 17.285  14.741  2.980   1.00 24.87  ? 338  ASN A C   1 
ATOM   2301  O  O   . ASN A  1 338 ? 18.382  15.025  3.479   1.00 26.99  ? 338  ASN A O   1 
ATOM   2302  C  CB  . ASN A  1 338 ? 15.979  13.767  4.833   1.00 26.27  ? 338  ASN A CB  1 
ATOM   2303  C  CG  . ASN A  1 338 ? 15.623  12.512  5.576   1.00 30.52  ? 338  ASN A CG  1 
ATOM   2304  O  OD1 . ASN A  1 338 ? 14.627  11.854  5.265   1.00 34.72  ? 338  ASN A OD1 1 
ATOM   2305  N  ND2 . ASN A  1 338 ? 16.416  12.188  6.600   1.00 26.46  ? 338  ASN A ND2 1 
ATOM   2306  N  N   . TRP A  1 339 ? 16.702  15.428  1.996   1.00 25.13  ? 339  TRP A N   1 
ATOM   2307  C  CA  . TRP A  1 339 ? 17.337  16.542  1.289   1.00 24.94  ? 339  TRP A CA  1 
ATOM   2308  C  C   . TRP A  1 339 ? 17.638  17.660  2.284   1.00 27.49  ? 339  TRP A C   1 
ATOM   2309  O  O   . TRP A  1 339 ? 16.711  18.196  2.881   1.00 31.40  ? 339  TRP A O   1 
ATOM   2310  C  CB  . TRP A  1 339 ? 16.414  17.037  0.158   1.00 23.61  ? 339  TRP A CB  1 
ATOM   2311  C  CG  . TRP A  1 339 ? 17.118  17.612  -1.035  1.00 27.96  ? 339  TRP A CG  1 
ATOM   2312  C  CD1 . TRP A  1 339 ? 18.435  17.972  -1.127  1.00 25.67  ? 339  TRP A CD1 1 
ATOM   2313  C  CD2 . TRP A  1 339 ? 16.546  17.865  -2.324  1.00 27.84  ? 339  TRP A CD2 1 
ATOM   2314  N  NE1 . TRP A  1 339 ? 18.713  18.423  -2.392  1.00 22.56  ? 339  TRP A NE1 1 
ATOM   2315  C  CE2 . TRP A  1 339 ? 17.570  18.370  -3.144  1.00 29.38  ? 339  TRP A CE2 1 
ATOM   2316  C  CE3 . TRP A  1 339 ? 15.265  17.712  -2.864  1.00 22.08  ? 339  TRP A CE3 1 
ATOM   2317  C  CZ2 . TRP A  1 339 ? 17.351  18.722  -4.473  1.00 28.14  ? 339  TRP A CZ2 1 
ATOM   2318  C  CZ3 . TRP A  1 339 ? 15.058  18.053  -4.154  1.00 23.74  ? 339  TRP A CZ3 1 
ATOM   2319  C  CH2 . TRP A  1 339 ? 16.096  18.546  -4.958  1.00 27.32  ? 339  TRP A CH2 1 
ATOM   2320  N  N   . GLY A  1 340 ? 18.915  17.960  2.514   1.00 26.17  ? 340  GLY A N   1 
ATOM   2321  C  CA  . GLY A  1 340 ? 19.302  18.984  3.481   1.00 27.48  ? 340  GLY A CA  1 
ATOM   2322  C  C   . GLY A  1 340 ? 19.397  18.592  4.964   1.00 34.20  ? 340  GLY A C   1 
ATOM   2323  O  O   . GLY A  1 340 ? 19.926  19.359  5.795   1.00 28.87  ? 340  GLY A O   1 
ATOM   2324  N  N   . LEU A  1 341 ? 18.900  17.401  5.305   1.00 26.41  ? 341  LEU A N   1 
ATOM   2325  C  CA  . LEU A  1 341 ? 18.955  16.911  6.682   1.00 23.43  ? 341  LEU A CA  1 
ATOM   2326  C  C   . LEU A  1 341 ? 19.161  15.370  6.707   1.00 31.50  ? 341  LEU A C   1 
ATOM   2327  O  O   . LEU A  1 341 ? 18.232  14.584  6.924   1.00 27.66  ? 341  LEU A O   1 
ATOM   2328  C  CB  . LEU A  1 341 ? 17.687  17.298  7.407   1.00 24.79  ? 341  LEU A CB  1 
ATOM   2329  C  CG  . LEU A  1 341 ? 17.521  16.787  8.829   1.00 28.74  ? 341  LEU A CG  1 
ATOM   2330  C  CD1 . LEU A  1 341 ? 18.661  17.237  9.736   1.00 26.14  ? 341  LEU A CD1 1 
ATOM   2331  C  CD2 . LEU A  1 341 ? 16.196  17.257  9.345   1.00 27.24  ? 341  LEU A CD2 1 
ATOM   2332  N  N   . ILE A  1 342 ? 20.398  14.953  6.469   1.00 26.49  ? 342  ILE A N   1 
ATOM   2333  C  CA  . ILE A  1 342 ? 20.721  13.562  6.282   1.00 20.47  ? 342  ILE A CA  1 
ATOM   2334  C  C   . ILE A  1 342 ? 20.955  12.916  7.603   1.00 23.89  ? 342  ILE A C   1 
ATOM   2335  O  O   . ILE A  1 342 ? 21.829  13.361  8.337   1.00 22.31  ? 342  ILE A O   1 
ATOM   2336  C  CB  . ILE A  1 342 ? 21.987  13.364  5.416   1.00 22.42  ? 342  ILE A CB  1 
ATOM   2337  C  CG1 . ILE A  1 342 ? 21.832  14.062  4.058   1.00 18.14  ? 342  ILE A CG1 1 
ATOM   2338  C  CG2 . ILE A  1 342 ? 22.260  11.891  5.249   1.00 21.14  ? 342  ILE A CG2 1 
ATOM   2339  C  CD1 . ILE A  1 342 ? 23.114  14.197  3.283   1.00 18.91  ? 342  ILE A CD1 1 
ATOM   2340  N  N   . THR A  1 343 ? 20.185  11.855  7.881   1.00 25.73  ? 343  THR A N   1 
ATOM   2341  C  CA  . THR A  1 343 ? 20.288  11.089  9.131   1.00 26.29  ? 343  THR A CA  1 
ATOM   2342  C  C   . THR A  1 343 ? 21.210  9.848   9.063   1.00 21.80  ? 343  THR A C   1 
ATOM   2343  O  O   . THR A  1 343 ? 21.185  9.091   8.113   1.00 24.94  ? 343  THR A O   1 
ATOM   2344  C  CB  . THR A  1 343 ? 18.925  10.610  9.567   1.00 26.83  ? 343  THR A CB  1 
ATOM   2345  O  OG1 . THR A  1 343 ? 18.233  10.130  8.414   1.00 27.91  ? 343  THR A OG1 1 
ATOM   2346  C  CG2 . THR A  1 343 ? 18.127  11.727  10.211  1.00 22.96  ? 343  THR A CG2 1 
ATOM   2347  N  N   . TYR A  1 344 ? 22.001  9.637   10.105  1.00 29.34  ? 344  TYR A N   1 
ATOM   2348  C  CA  . TYR A  1 344 ? 22.916  8.490   10.189  1.00 27.88  ? 344  TYR A CA  1 
ATOM   2349  C  C   . TYR A  1 344 ? 22.794  7.738   11.522  1.00 28.38  ? 344  TYR A C   1 
ATOM   2350  O  O   . TYR A  1 344 ? 22.404  8.315   12.536  1.00 29.30  ? 344  TYR A O   1 
ATOM   2351  C  CB  . TYR A  1 344 ? 24.368  8.928   10.061  1.00 24.08  ? 344  TYR A CB  1 
ATOM   2352  C  CG  . TYR A  1 344 ? 24.735  9.648   8.815   1.00 23.52  ? 344  TYR A CG  1 
ATOM   2353  C  CD1 . TYR A  1 344 ? 24.350  10.980  8.608   1.00 23.85  ? 344  TYR A CD1 1 
ATOM   2354  C  CD2 . TYR A  1 344 ? 25.527  9.024   7.864   1.00 20.09  ? 344  TYR A CD2 1 
ATOM   2355  C  CE1 . TYR A  1 344 ? 24.714  11.645  7.462   1.00 20.87  ? 344  TYR A CE1 1 
ATOM   2356  C  CE2 . TYR A  1 344 ? 25.910  9.665   6.734   1.00 19.31  ? 344  TYR A CE2 1 
ATOM   2357  C  CZ  . TYR A  1 344 ? 25.496  10.977  6.519   1.00 24.38  ? 344  TYR A CZ  1 
ATOM   2358  O  OH  . TYR A  1 344 ? 25.893  11.594  5.359   1.00 20.22  ? 344  TYR A OH  1 
ATOM   2359  N  N   . ARG A  1 345 ? 23.143  6.456   11.509  1.00 26.43  ? 345  ARG A N   1 
ATOM   2360  C  CA  . ARG A  1 345 ? 23.608  5.804   12.708  1.00 21.33  ? 345  ARG A CA  1 
ATOM   2361  C  C   . ARG A  1 345 ? 24.898  6.480   13.163  1.00 26.99  ? 345  ARG A C   1 
ATOM   2362  O  O   . ARG A  1 345 ? 25.691  6.958   12.354  1.00 30.46  ? 345  ARG A O   1 
ATOM   2363  C  CB  . ARG A  1 345 ? 23.886  4.317   12.477  1.00 29.68  ? 345  ARG A CB  1 
ATOM   2364  C  CG  . ARG A  1 345 ? 22.663  3.458   12.422  1.00 31.06  ? 345  ARG A CG  1 
ATOM   2365  C  CD  . ARG A  1 345 ? 23.048  2.017   12.490  1.00 38.39  ? 345  ARG A CD  1 
ATOM   2366  N  NE  . ARG A  1 345 ? 21.907  1.180   12.162  1.00 44.48  ? 345  ARG A NE  1 
ATOM   2367  C  CZ  . ARG A  1 345 ? 21.621  0.050   12.787  1.00 45.07  ? 345  ARG A CZ  1 
ATOM   2368  N  NH1 . ARG A  1 345 ? 22.407  -0.369  13.766  1.00 47.53  ? 345  ARG A NH1 1 
ATOM   2369  N  NH2 . ARG A  1 345 ? 20.553  -0.648  12.438  1.00 44.67  ? 345  ARG A NH2 1 
ATOM   2370  N  N   . GLU A  1 346 ? 25.126  6.494   14.458  1.00 27.17  ? 346  GLU A N   1 
ATOM   2371  C  CA  . GLU A  1 346 ? 26.364  7.025   14.965  1.00 28.50  ? 346  GLU A CA  1 
ATOM   2372  C  C   . GLU A  1 346 ? 27.543  6.266   14.365  1.00 28.05  ? 346  GLU A C   1 
ATOM   2373  O  O   . GLU A  1 346 ? 28.546  6.869   13.964  1.00 28.32  ? 346  GLU A O   1 
ATOM   2374  C  CB  . GLU A  1 346 ? 26.378  6.961   16.492  1.00 30.06  ? 346  GLU A CB  1 
ATOM   2375  C  CG  . GLU A  1 346 ? 25.116  7.553   17.097  1.00 35.18  ? 346  GLU A CG  1 
ATOM   2376  C  CD  . GLU A  1 346 ? 25.236  7.872   18.577  1.00 41.67  ? 346  GLU A CD  1 
ATOM   2377  O  OE1 . GLU A  1 346 ? 25.816  8.925   18.891  1.00 48.03  ? 346  GLU A OE1 1 
ATOM   2378  O  OE2 . GLU A  1 346 ? 24.727  7.096   19.418  1.00 46.35  ? 346  GLU A OE2 1 
ATOM   2379  N  N   . THR A  1 347 ? 27.412  4.949   14.257  1.00 21.13  ? 347  THR A N   1 
ATOM   2380  C  CA  . THR A  1 347 ? 28.494  4.184   13.675  1.00 21.47  ? 347  THR A CA  1 
ATOM   2381  C  C   . THR A  1 347 ? 28.754  4.533   12.203  1.00 26.00  ? 347  THR A C   1 
ATOM   2382  O  O   . THR A  1 347 ? 29.803  4.178   11.683  1.00 27.93  ? 347  THR A O   1 
ATOM   2383  C  CB  . THR A  1 347 ? 28.250  2.672   13.787  1.00 27.15  ? 347  THR A CB  1 
ATOM   2384  O  OG1 . THR A  1 347 ? 26.945  2.333   13.310  1.00 27.28  ? 347  THR A OG1 1 
ATOM   2385  C  CG2 . THR A  1 347 ? 28.421  2.229   15.222  1.00 22.57  ? 347  THR A CG2 1 
ATOM   2386  N  N   . SER A  1 348 ? 27.811  5.242   11.566  1.00 24.53  ? 348  SER A N   1 
ATOM   2387  C  CA  . SER A  1 348 ? 27.877  5.607   10.156  1.00 28.90  ? 348  SER A CA  1 
ATOM   2388  C  C   . SER A  1 348 ? 28.525  6.973   9.969   1.00 32.16  ? 348  SER A C   1 
ATOM   2389  O  O   . SER A  1 348 ? 28.885  7.339   8.847   1.00 30.09  ? 348  SER A O   1 
ATOM   2390  C  CB  . SER A  1 348 ? 26.459  5.650   9.515   1.00 29.68  ? 348  SER A CB  1 
ATOM   2391  O  OG  . SER A  1 348 ? 25.955  4.380   9.140   1.00 30.89  ? 348  SER A OG  1 
ATOM   2392  N  N   . LEU A  1 349 ? 28.618  7.755   11.041  1.00 28.62  ? 349  LEU A N   1 
ATOM   2393  C  CA  . LEU A  1 349 ? 28.970  9.167   10.879  1.00 26.16  ? 349  LEU A CA  1 
ATOM   2394  C  C   . LEU A  1 349 ? 30.082  9.592   11.818  1.00 26.09  ? 349  LEU A C   1 
ATOM   2395  O  O   . LEU A  1 349 ? 31.001  10.293  11.443  1.00 27.13  ? 349  LEU A O   1 
ATOM   2396  C  CB  . LEU A  1 349 ? 27.737  10.032  11.107  1.00 23.51  ? 349  LEU A CB  1 
ATOM   2397  C  CG  . LEU A  1 349 ? 27.863  11.535  10.891  1.00 25.96  ? 349  LEU A CG  1 
ATOM   2398  C  CD1 . LEU A  1 349 ? 28.003  11.790  9.389   1.00 20.62  ? 349  LEU A CD1 1 
ATOM   2399  C  CD2 . LEU A  1 349 ? 26.649  12.280  11.477  1.00 18.26  ? 349  LEU A CD2 1 
ATOM   2400  N  N   . LEU A  1 350 ? 29.986  9.133   13.052  1.00 28.82  ? 350  LEU A N   1 
ATOM   2401  C  CA  . LEU A  1 350 ? 30.890  9.555   14.092  1.00 26.48  ? 350  LEU A CA  1 
ATOM   2402  C  C   . LEU A  1 350 ? 32.188  8.764   14.016  1.00 29.45  ? 350  LEU A C   1 
ATOM   2403  O  O   . LEU A  1 350 ? 32.188  7.561   13.756  1.00 31.53  ? 350  LEU A O   1 
ATOM   2404  C  CB  . LEU A  1 350 ? 30.223  9.397   15.443  1.00 23.34  ? 350  LEU A CB  1 
ATOM   2405  C  CG  . LEU A  1 350 ? 28.911  10.184  15.639  1.00 28.68  ? 350  LEU A CG  1 
ATOM   2406  C  CD1 . LEU A  1 350 ? 28.413  10.088  17.093  1.00 28.82  ? 350  LEU A CD1 1 
ATOM   2407  C  CD2 . LEU A  1 350 ? 29.019  11.663  15.209  1.00 25.40  ? 350  LEU A CD2 1 
ATOM   2408  N  N   . PHE A  1 351 ? 33.301  9.458   14.210  1.00 29.92  ? 351  PHE A N   1 
ATOM   2409  C  CA  . PHE A  1 351 ? 34.598  8.819   14.189  1.00 32.40  ? 351  PHE A CA  1 
ATOM   2410  C  C   . PHE A  1 351 ? 35.475  9.310   15.322  1.00 35.45  ? 351  PHE A C   1 
ATOM   2411  O  O   . PHE A  1 351 ? 35.574  10.515  15.597  1.00 32.37  ? 351  PHE A O   1 
ATOM   2412  C  CB  . PHE A  1 351 ? 35.299  9.060   12.858  1.00 32.10  ? 351  PHE A CB  1 
ATOM   2413  C  CG  . PHE A  1 351 ? 36.676  8.481   12.801  1.00 31.33  ? 351  PHE A CG  1 
ATOM   2414  C  CD1 . PHE A  1 351 ? 36.871  7.175   12.401  1.00 29.33  ? 351  PHE A CD1 1 
ATOM   2415  C  CD2 . PHE A  1 351 ? 37.779  9.243   13.154  1.00 30.66  ? 351  PHE A CD2 1 
ATOM   2416  C  CE1 . PHE A  1 351 ? 38.148  6.624   12.369  1.00 34.20  ? 351  PHE A CE1 1 
ATOM   2417  C  CE2 . PHE A  1 351 ? 39.056  8.715   13.109  1.00 31.51  ? 351  PHE A CE2 1 
ATOM   2418  C  CZ  . PHE A  1 351 ? 39.244  7.400   12.729  1.00 33.66  ? 351  PHE A CZ  1 
ATOM   2419  N  N   . ASP A  1 352 ? 36.133  8.358   15.958  1.00 34.44  ? 352  ASP A N   1 
ATOM   2420  C  CA  . ASP A  1 352 ? 36.921  8.628   17.147  1.00 37.32  ? 352  ASP A CA  1 
ATOM   2421  C  C   . ASP A  1 352 ? 38.270  7.909   17.107  1.00 39.90  ? 352  ASP A C   1 
ATOM   2422  O  O   . ASP A  1 352 ? 38.339  6.692   17.190  1.00 38.67  ? 352  ASP A O   1 
ATOM   2423  C  CB  . ASP A  1 352 ? 36.131  8.209   18.378  1.00 39.92  ? 352  ASP A CB  1 
ATOM   2424  C  CG  . ASP A  1 352 ? 36.996  8.035   19.590  1.00 46.96  ? 352  ASP A CG  1 
ATOM   2425  O  OD1 . ASP A  1 352 ? 37.784  8.965   19.919  1.00 47.81  ? 352  ASP A OD1 1 
ATOM   2426  O  OD2 . ASP A  1 352 ? 36.894  6.946   20.199  1.00 51.25  ? 352  ASP A OD2 1 
ATOM   2427  N  N   . PRO A  1 353 ? 39.354  8.675   17.039  1.00 44.02  ? 353  PRO A N   1 
ATOM   2428  C  CA  . PRO A  1 353 ? 40.680  8.103   16.780  1.00 43.33  ? 353  PRO A CA  1 
ATOM   2429  C  C   . PRO A  1 353 ? 41.102  7.054   17.808  1.00 45.47  ? 353  PRO A C   1 
ATOM   2430  O  O   . PRO A  1 353 ? 41.813  6.112   17.467  1.00 48.58  ? 353  PRO A O   1 
ATOM   2431  C  CB  . PRO A  1 353 ? 41.610  9.326   16.835  1.00 46.84  ? 353  PRO A CB  1 
ATOM   2432  C  CG  . PRO A  1 353 ? 40.693  10.531  16.646  1.00 43.17  ? 353  PRO A CG  1 
ATOM   2433  C  CD  . PRO A  1 353 ? 39.400  10.125  17.303  1.00 40.83  ? 353  PRO A CD  1 
ATOM   2434  N  N   . LYS A  1 354 ? 40.663  7.199   19.044  1.00 39.02  ? 354  LYS A N   1 
ATOM   2435  C  CA  . LYS A  1 354 ? 41.048  6.236   20.064  1.00 49.24  ? 354  LYS A CA  1 
ATOM   2436  C  C   . LYS A  1 354 ? 40.424  4.831   19.897  1.00 44.59  ? 354  LYS A C   1 
ATOM   2437  O  O   . LYS A  1 354 ? 41.027  3.851   20.312  1.00 44.42  ? 354  LYS A O   1 
ATOM   2438  C  CB  . LYS A  1 354 ? 40.702  6.784   21.463  1.00 48.46  ? 354  LYS A CB  1 
ATOM   2439  C  CG  . LYS A  1 354 ? 41.601  6.215   22.563  1.00 62.40  ? 354  LYS A CG  1 
ATOM   2440  C  CD  . LYS A  1 354 ? 41.006  6.351   23.956  1.00 68.66  ? 354  LYS A CD  1 
ATOM   2441  C  CE  . LYS A  1 354 ? 41.387  5.147   24.821  1.00 69.71  ? 354  LYS A CE  1 
ATOM   2442  N  NZ  . LYS A  1 354 ? 40.693  5.120   26.139  1.00 72.08  ? 354  LYS A NZ  1 
ATOM   2443  N  N   . THR A  1 355 ? 39.225  4.727   19.323  1.00 42.53  ? 355  THR A N   1 
ATOM   2444  C  CA  . THR A  1 355 ? 38.535  3.428   19.268  1.00 39.71  ? 355  THR A CA  1 
ATOM   2445  C  C   . THR A  1 355 ? 37.938  3.090   17.925  1.00 42.43  ? 355  THR A C   1 
ATOM   2446  O  O   . THR A  1 355 ? 37.523  1.956   17.703  1.00 42.79  ? 355  THR A O   1 
ATOM   2447  C  CB  . THR A  1 355 ? 37.394  3.326   20.278  1.00 37.81  ? 355  THR A CB  1 
ATOM   2448  O  OG1 . THR A  1 355 ? 36.623  4.527   20.236  1.00 44.96  ? 355  THR A OG1 1 
ATOM   2449  C  CG2 . THR A  1 355 ? 37.939  3.114   21.681  1.00 37.73  ? 355  THR A CG2 1 
ATOM   2450  N  N   . SER A  1 356 ? 37.871  4.070   17.035  1.00 40.82  ? 356  SER A N   1 
ATOM   2451  C  CA  . SER A  1 356 ? 37.486  3.784   15.665  1.00 38.10  ? 356  SER A CA  1 
ATOM   2452  C  C   . SER A  1 356 ? 38.707  3.315   14.917  1.00 37.88  ? 356  SER A C   1 
ATOM   2453  O  O   . SER A  1 356 ? 39.772  3.941   14.997  1.00 37.48  ? 356  SER A O   1 
ATOM   2454  C  CB  . SER A  1 356 ? 36.875  5.005   14.971  1.00 33.03  ? 356  SER A CB  1 
ATOM   2455  O  OG  . SER A  1 356 ? 35.541  5.200   15.365  1.00 35.39  ? 356  SER A OG  1 
ATOM   2456  N  N   . SER A  1 357 ? 38.539  2.217   14.186  1.00 37.79  ? 357  SER A N   1 
ATOM   2457  C  CA  . SER A  1 357 ? 39.608  1.644   13.368  1.00 40.31  ? 357  SER A CA  1 
ATOM   2458  C  C   . SER A  1 357 ? 39.653  2.203   11.948  1.00 35.36  ? 357  SER A C   1 
ATOM   2459  O  O   . SER A  1 357 ? 38.797  2.983   11.532  1.00 34.06  ? 357  SER A O   1 
ATOM   2460  C  CB  . SER A  1 357 ? 39.460  0.125   13.287  1.00 40.59  ? 357  SER A CB  1 
ATOM   2461  O  OG  . SER A  1 357 ? 38.287  -0.232  12.563  1.00 42.34  ? 357  SER A OG  1 
ATOM   2462  N  N   . ALA A  1 358 ? 40.663  1.765   11.210  1.00 36.10  ? 358  ALA A N   1 
ATOM   2463  C  CA  . ALA A  1 358 ? 40.839  2.143   9.818   1.00 35.77  ? 358  ALA A CA  1 
ATOM   2464  C  C   . ALA A  1 358 ? 39.679  1.684   8.957   1.00 36.07  ? 358  ALA A C   1 
ATOM   2465  O  O   . ALA A  1 358 ? 39.388  2.278   7.942   1.00 42.64  ? 358  ALA A O   1 
ATOM   2466  C  CB  . ALA A  1 358 ? 42.127  1.563   9.269   1.00 42.26  ? 358  ALA A CB  1 
ATOM   2467  N  N   . SER A  1 359 ? 39.021  0.609   9.339   1.00 36.97  ? 359  SER A N   1 
ATOM   2468  C  CA  . SER A  1 359 ? 37.977  0.119   8.485   1.00 38.60  ? 359  SER A CA  1 
ATOM   2469  C  C   . SER A  1 359 ? 36.689  0.817   8.888   1.00 35.21  ? 359  SER A C   1 
ATOM   2470  O  O   . SER A  1 359 ? 35.753  0.912   8.100   1.00 36.27  ? 359  SER A O   1 
ATOM   2471  C  CB  . SER A  1 359 ? 37.869  -1.407  8.574   1.00 33.43  ? 359  SER A CB  1 
ATOM   2472  O  OG  . SER A  1 359 ? 37.193  -1.790  9.734   1.00 35.81  ? 359  SER A OG  1 
ATOM   2473  N  N   . ASP A  1 360 ? 36.657  1.315   10.121  1.00 35.72  ? 360  ASP A N   1 
ATOM   2474  C  CA  . ASP A  1 360 ? 35.571  2.168   10.560  1.00 30.15  ? 360  ASP A CA  1 
ATOM   2475  C  C   . ASP A  1 360 ? 35.606  3.453   9.725   1.00 33.52  ? 360  ASP A C   1 
ATOM   2476  O  O   . ASP A  1 360 ? 34.586  3.910   9.209   1.00 30.54  ? 360  ASP A O   1 
ATOM   2477  C  CB  . ASP A  1 360 ? 35.693  2.497   12.043  1.00 35.42  ? 360  ASP A CB  1 
ATOM   2478  C  CG  . ASP A  1 360 ? 35.432  1.293   12.957  1.00 41.31  ? 360  ASP A CG  1 
ATOM   2479  O  OD1 . ASP A  1 360 ? 34.568  0.436   12.634  1.00 38.76  ? 360  ASP A OD1 1 
ATOM   2480  O  OD2 . ASP A  1 360 ? 36.089  1.236   14.035  1.00 44.79  ? 360  ASP A OD2 1 
ATOM   2481  N  N   . LYS A  1 361 ? 36.796  4.021   9.580   1.00 31.94  ? 361  LYS A N   1 
ATOM   2482  C  CA  . LYS A  1 361 ? 36.953  5.243   8.795   1.00 37.48  ? 361  LYS A CA  1 
ATOM   2483  C  C   . LYS A  1 361 ? 36.449  5.034   7.353   1.00 32.02  ? 361  LYS A C   1 
ATOM   2484  O  O   . LYS A  1 361 ? 35.665  5.821   6.830   1.00 34.02  ? 361  LYS A O   1 
ATOM   2485  C  CB  . LYS A  1 361 ? 38.422  5.698   8.800   1.00 34.25  ? 361  LYS A CB  1 
ATOM   2486  C  CG  . LYS A  1 361 ? 38.738  6.829   7.808   1.00 35.71  ? 361  LYS A CG  1 
ATOM   2487  C  CD  . LYS A  1 361 ? 38.736  8.191   8.494   1.00 34.90  ? 361  LYS A CD  1 
ATOM   2488  C  CE  . LYS A  1 361 ? 39.910  8.294   9.453   1.00 39.37  ? 361  LYS A CE  1 
ATOM   2489  N  NZ  . LYS A  1 361 ? 40.232  9.700   9.816   1.00 42.82  ? 361  LYS A NZ  1 
ATOM   2490  N  N   . LEU A  1 362 ? 36.891  3.952   6.741   1.00 32.55  ? 362  LEU A N   1 
ATOM   2491  C  CA  . LEU A  1 362 ? 36.459  3.586   5.408   1.00 36.58  ? 362  LEU A CA  1 
ATOM   2492  C  C   . LEU A  1 362 ? 34.944  3.563   5.288   1.00 34.34  ? 362  LEU A C   1 
ATOM   2493  O  O   . LEU A  1 362 ? 34.374  4.174   4.384   1.00 32.32  ? 362  LEU A O   1 
ATOM   2494  C  CB  . LEU A  1 362 ? 37.028  2.227   5.043   1.00 31.88  ? 362  LEU A CB  1 
ATOM   2495  C  CG  . LEU A  1 362 ? 36.790  1.882   3.585   1.00 47.46  ? 362  LEU A CG  1 
ATOM   2496  C  CD1 . LEU A  1 362 ? 37.142  3.084   2.705   1.00 49.73  ? 362  LEU A CD1 1 
ATOM   2497  C  CD2 . LEU A  1 362 ? 37.598  0.647   3.201   1.00 54.02  ? 362  LEU A CD2 1 
ATOM   2498  N  N   . TRP A  1 363 ? 34.305  2.882   6.231   1.00 32.51  ? 363  TRP A N   1 
ATOM   2499  C  CA  . TRP A  1 363 ? 32.857  2.769   6.249   1.00 31.77  ? 363  TRP A CA  1 
ATOM   2500  C  C   . TRP A  1 363 ? 32.180  4.154   6.389   1.00 29.06  ? 363  TRP A C   1 
ATOM   2501  O  O   . TRP A  1 363 ? 31.243  4.479   5.633   1.00 33.36  ? 363  TRP A O   1 
ATOM   2502  C  CB  . TRP A  1 363 ? 32.428  1.797   7.367   1.00 25.57  ? 363  TRP A CB  1 
ATOM   2503  C  CG  . TRP A  1 363 ? 30.951  1.763   7.640   1.00 30.99  ? 363  TRP A CG  1 
ATOM   2504  C  CD1 . TRP A  1 363 ? 30.302  2.256   8.739   1.00 29.76  ? 363  TRP A CD1 1 
ATOM   2505  C  CD2 . TRP A  1 363 ? 29.940  1.239   6.785   1.00 35.41  ? 363  TRP A CD2 1 
ATOM   2506  N  NE1 . TRP A  1 363 ? 28.952  2.059   8.624   1.00 28.22  ? 363  TRP A NE1 1 
ATOM   2507  C  CE2 . TRP A  1 363 ? 28.703  1.425   7.437   1.00 31.89  ? 363  TRP A CE2 1 
ATOM   2508  C  CE3 . TRP A  1 363 ? 29.958  0.616   5.532   1.00 30.23  ? 363  TRP A CE3 1 
ATOM   2509  C  CZ2 . TRP A  1 363 ? 27.504  1.015   6.882   1.00 35.61  ? 363  TRP A CZ2 1 
ATOM   2510  C  CZ3 . TRP A  1 363 ? 28.767  0.215   4.979   1.00 28.47  ? 363  TRP A CZ3 1 
ATOM   2511  C  CH2 . TRP A  1 363 ? 27.556  0.418   5.648   1.00 36.59  ? 363  TRP A CH2 1 
ATOM   2512  N  N   . VAL A  1 364 ? 32.658  4.975   7.315   1.00 25.31  ? 364  VAL A N   1 
ATOM   2513  C  CA  . VAL A  1 364 ? 32.056  6.305   7.523   1.00 29.52  ? 364  VAL A CA  1 
ATOM   2514  C  C   . VAL A  1 364 ? 32.137  7.143   6.247   1.00 30.84  ? 364  VAL A C   1 
ATOM   2515  O  O   . VAL A  1 364 ? 31.192  7.860   5.900   1.00 31.78  ? 364  VAL A O   1 
ATOM   2516  C  CB  . VAL A  1 364 ? 32.730  7.067   8.672   1.00 27.81  ? 364  VAL A CB  1 
ATOM   2517  C  CG1 . VAL A  1 364 ? 32.239  8.501   8.725   1.00 21.41  ? 364  VAL A CG1 1 
ATOM   2518  C  CG2 . VAL A  1 364 ? 32.481  6.337   10.006  1.00 24.82  ? 364  VAL A CG2 1 
ATOM   2519  N  N   . THR A  1 365 ? 33.242  6.975   5.525   1.00 25.09  ? 365  THR A N   1 
ATOM   2520  C  CA  . THR A  1 365 ? 33.495  7.707   4.307   1.00 28.74  ? 365  THR A CA  1 
ATOM   2521  C  C   . THR A  1 365 ? 32.581  7.254   3.191   1.00 29.38  ? 365  THR A C   1 
ATOM   2522  O  O   . THR A  1 365 ? 32.084  8.074   2.415   1.00 27.94  ? 365  THR A O   1 
ATOM   2523  C  CB  . THR A  1 365 ? 34.963  7.562   3.855   1.00 29.31  ? 365  THR A CB  1 
ATOM   2524  O  OG1 . THR A  1 365 ? 35.833  7.949   4.933   1.00 27.34  ? 365  THR A OG1 1 
ATOM   2525  C  CG2 . THR A  1 365 ? 35.226  8.444   2.642   1.00 22.10  ? 365  THR A CG2 1 
ATOM   2526  N  N   . ARG A  1 366 ? 32.364  5.947   3.122   1.00 33.32  ? 366  ARG A N   1 
ATOM   2527  C  CA  . ARG A  1 366 ? 31.457  5.343   2.148   1.00 27.92  ? 366  ARG A CA  1 
ATOM   2528  C  C   . ARG A  1 366 ? 30.068  5.886   2.358   1.00 24.55  ? 366  ARG A C   1 
ATOM   2529  O  O   . ARG A  1 366 ? 29.422  6.339   1.423   1.00 24.89  ? 366  ARG A O   1 
ATOM   2530  C  CB  . ARG A  1 366 ? 31.391  3.815   2.308   1.00 31.18  ? 366  ARG A CB  1 
ATOM   2531  C  CG  . ARG A  1 366 ? 32.368  2.960   1.577   1.00 39.77  ? 366  ARG A CG  1 
ATOM   2532  C  CD  . ARG A  1 366 ? 31.799  1.516   1.588   1.00 44.20  ? 366  ARG A CD  1 
ATOM   2533  N  NE  . ARG A  1 366 ? 30.344  1.554   1.410   1.00 43.60  ? 366  ARG A NE  1 
ATOM   2534  C  CZ  . ARG A  1 366 ? 29.562  0.487   1.273   1.00 45.71  ? 366  ARG A CZ  1 
ATOM   2535  N  NH1 . ARG A  1 366 ? 30.086  -0.736  1.313   1.00 60.60  ? 366  ARG A NH1 1 
ATOM   2536  N  NH2 . ARG A  1 366 ? 28.250  0.646   1.099   1.00 47.78  ? 366  ARG A NH2 1 
ATOM   2537  N  N   . VAL A  1 367 ? 29.597  5.784   3.598   1.00 24.04  ? 367  VAL A N   1 
ATOM   2538  C  CA  . VAL A  1 367 ? 28.215  6.110   3.877   1.00 25.63  ? 367  VAL A CA  1 
ATOM   2539  C  C   . VAL A  1 367 ? 27.955  7.579   3.573   1.00 23.27  ? 367  VAL A C   1 
ATOM   2540  O  O   . VAL A  1 367 ? 26.944  7.919   2.972   1.00 23.03  ? 367  VAL A O   1 
ATOM   2541  C  CB  . VAL A  1 367 ? 27.823  5.765   5.334   1.00 28.83  ? 367  VAL A CB  1 
ATOM   2542  C  CG1 . VAL A  1 367 ? 26.331  6.025   5.562   1.00 20.08  ? 367  VAL A CG1 1 
ATOM   2543  C  CG2 . VAL A  1 367 ? 28.145  4.272   5.628   1.00 21.96  ? 367  VAL A CG2 1 
ATOM   2544  N  N   . ILE A  1 368 ? 28.895  8.444   3.923   1.00 25.91  ? 368  ILE A N   1 
ATOM   2545  C  CA  . ILE A  1 368 ? 28.744  9.860   3.622   1.00 21.36  ? 368  ILE A CA  1 
ATOM   2546  C  C   . ILE A  1 368 ? 28.759  10.078  2.112   1.00 25.29  ? 368  ILE A C   1 
ATOM   2547  O  O   . ILE A  1 368 ? 27.980  10.879  1.574   1.00 24.86  ? 368  ILE A O   1 
ATOM   2548  C  CB  . ILE A  1 368 ? 29.842  10.685  4.297   1.00 23.17  ? 368  ILE A CB  1 
ATOM   2549  C  CG1 . ILE A  1 368 ? 29.588  10.719  5.798   1.00 21.59  ? 368  ILE A CG1 1 
ATOM   2550  C  CG2 . ILE A  1 368 ? 29.895  12.133  3.739   1.00 21.22  ? 368  ILE A CG2 1 
ATOM   2551  C  CD1 . ILE A  1 368 ? 30.799  11.125  6.603   1.00 23.57  ? 368  ILE A CD1 1 
ATOM   2552  N  N   . ALA A  1 369 ? 29.631  9.335   1.432   1.00 24.63  ? 369  ALA A N   1 
ATOM   2553  C  CA  . ALA A  1 369 ? 29.723  9.410   -0.020  1.00 22.75  ? 369  ALA A CA  1 
ATOM   2554  C  C   . ALA A  1 369 ? 28.392  9.000   -0.623  1.00 24.70  ? 369  ALA A C   1 
ATOM   2555  O  O   . ALA A  1 369 ? 27.878  9.685   -1.497  1.00 25.78  ? 369  ALA A O   1 
ATOM   2556  C  CB  . ALA A  1 369 ? 30.837  8.534   -0.542  1.00 21.70  ? 369  ALA A CB  1 
ATOM   2557  N  N   . HIS A  1 370 ? 27.846  7.889   -0.132  1.00 23.82  ? 370  HIS A N   1 
ATOM   2558  C  CA  . HIS A  1 370 ? 26.561  7.354   -0.573  1.00 24.29  ? 370  HIS A CA  1 
ATOM   2559  C  C   . HIS A  1 370 ? 25.457  8.377   -0.361  1.00 22.51  ? 370  HIS A C   1 
ATOM   2560  O  O   . HIS A  1 370 ? 24.678  8.636   -1.258  1.00 25.64  ? 370  HIS A O   1 
ATOM   2561  C  CB  . HIS A  1 370 ? 26.227  6.040   0.183   1.00 25.55  ? 370  HIS A CB  1 
ATOM   2562  C  CG  . HIS A  1 370 ? 25.060  5.280   -0.371  1.00 22.02  ? 370  HIS A CG  1 
ATOM   2563  N  ND1 . HIS A  1 370 ? 25.223  4.250   -1.263  1.00 24.21  ? 370  HIS A ND1 1 
ATOM   2564  C  CD2 . HIS A  1 370 ? 23.722  5.389   -0.166  1.00 20.88  ? 370  HIS A CD2 1 
ATOM   2565  C  CE1 . HIS A  1 370 ? 24.042  3.749   -1.582  1.00 31.90  ? 370  HIS A CE1 1 
ATOM   2566  N  NE2 . HIS A  1 370 ? 23.111  4.420   -0.929  1.00 20.62  ? 370  HIS A NE2 1 
ATOM   2567  N  N   . GLU A  1 371 ? 25.376  8.966   0.818   1.00 24.61  ? 371  GLU A N   1 
ATOM   2568  C  CA  . GLU A  1 371 ? 24.262  9.871   1.076   1.00 22.58  ? 371  GLU A CA  1 
ATOM   2569  C  C   . GLU A  1 371 ? 24.397  11.166  0.286   1.00 25.06  ? 371  GLU A C   1 
ATOM   2570  O  O   . GLU A  1 371 ? 23.415  11.676  -0.230  1.00 25.36  ? 371  GLU A O   1 
ATOM   2571  C  CB  . GLU A  1 371 ? 24.135  10.179  2.566   1.00 20.25  ? 371  GLU A CB  1 
ATOM   2572  C  CG  . GLU A  1 371 ? 23.926  8.955   3.387   1.00 19.52  ? 371  GLU A CG  1 
ATOM   2573  C  CD  . GLU A  1 371 ? 22.666  8.258   3.005   1.00 22.47  ? 371  GLU A CD  1 
ATOM   2574  O  OE1 . GLU A  1 371 ? 21.648  8.948   2.837   1.00 24.77  ? 371  GLU A OE1 1 
ATOM   2575  O  OE2 . GLU A  1 371 ? 22.689  7.024   2.854   1.00 22.44  ? 371  GLU A OE2 1 
ATOM   2576  N  N   . LEU A  1 372 ? 25.607  11.703  0.186   1.00 21.53  ? 372  LEU A N   1 
ATOM   2577  C  CA  . LEU A  1 372 ? 25.759  12.921  -0.584  1.00 22.55  ? 372  LEU A CA  1 
ATOM   2578  C  C   . LEU A  1 372 ? 25.418  12.649  -2.056  1.00 24.73  ? 372  LEU A C   1 
ATOM   2579  O  O   . LEU A  1 372 ? 24.733  13.447  -2.683  1.00 30.88  ? 372  LEU A O   1 
ATOM   2580  C  CB  . LEU A  1 372 ? 27.165  13.510  -0.466  1.00 24.02  ? 372  LEU A CB  1 
ATOM   2581  C  CG  . LEU A  1 372 ? 27.608  14.043  0.893   1.00 27.62  ? 372  LEU A CG  1 
ATOM   2582  C  CD1 . LEU A  1 372 ? 28.542  15.223  0.748   1.00 26.34  ? 372  LEU A CD1 1 
ATOM   2583  C  CD2 . LEU A  1 372 ? 26.459  14.348  1.823   1.00 25.37  ? 372  LEU A CD2 1 
ATOM   2584  N  N   . ALA A  1 373 ? 25.858  11.518  -2.591  1.00 24.70  ? 373  ALA A N   1 
ATOM   2585  C  CA  . ALA A  1 373 ? 25.517  11.160  -3.966  1.00 29.52  ? 373  ALA A CA  1 
ATOM   2586  C  C   . ALA A  1 373 ? 24.012  11.172  -4.179  1.00 29.24  ? 373  ALA A C   1 
ATOM   2587  O  O   . ALA A  1 373 ? 23.540  11.560  -5.236  1.00 33.26  ? 373  ALA A O   1 
ATOM   2588  C  CB  . ALA A  1 373 ? 26.083  9.803   -4.324  1.00 24.80  ? 373  ALA A CB  1 
ATOM   2589  N  N   . HIS A  1 374 ? 23.266  10.749  -3.167  1.00 24.64  ? 374  HIS A N   1 
ATOM   2590  C  CA  . HIS A  1 374 ? 21.816  10.745  -3.229  1.00 22.58  ? 374  HIS A CA  1 
ATOM   2591  C  C   . HIS A  1 374 ? 21.156  12.126  -3.397  1.00 29.29  ? 374  HIS A C   1 
ATOM   2592  O  O   . HIS A  1 374 ? 19.979  12.195  -3.772  1.00 28.77  ? 374  HIS A O   1 
ATOM   2593  C  CB  . HIS A  1 374 ? 21.266  10.142  -1.958  1.00 27.57  ? 374  HIS A CB  1 
ATOM   2594  C  CG  . HIS A  1 374 ? 20.993  8.673   -2.019  1.00 30.73  ? 374  HIS A CG  1 
ATOM   2595  N  ND1 . HIS A  1 374 ? 20.494  8.047   -3.135  1.00 29.19  ? 374  HIS A ND1 1 
ATOM   2596  C  CD2 . HIS A  1 374 ? 21.096  7.721   -1.059  1.00 26.28  ? 374  HIS A CD2 1 
ATOM   2597  C  CE1 . HIS A  1 374 ? 20.308  6.765   -2.868  1.00 27.76  ? 374  HIS A CE1 1 
ATOM   2598  N  NE2 . HIS A  1 374 ? 20.668  6.546   -1.620  1.00 28.98  ? 374  HIS A NE2 1 
ATOM   2599  N  N   . GLN A  1 375 ? 21.868  13.216  -3.069  1.00 28.67  ? 375  GLN A N   1 
ATOM   2600  C  CA  . GLN A  1 375 ? 21.257  14.553  -3.176  1.00 26.87  ? 375  GLN A CA  1 
ATOM   2601  C  C   . GLN A  1 375 ? 20.954  14.840  -4.636  1.00 26.48  ? 375  GLN A C   1 
ATOM   2602  O  O   . GLN A  1 375 ? 19.955  15.471  -4.931  1.00 30.58  ? 375  GLN A O   1 
ATOM   2603  C  CB  . GLN A  1 375 ? 22.141  15.660  -2.567  1.00 22.55  ? 375  GLN A CB  1 
ATOM   2604  C  CG  . GLN A  1 375 ? 22.583  15.383  -1.153  1.00 26.19  ? 375  GLN A CG  1 
ATOM   2605  C  CD  . GLN A  1 375 ? 21.421  15.307  -0.166  1.00 22.67  ? 375  GLN A CD  1 
ATOM   2606  O  OE1 . GLN A  1 375 ? 20.750  16.294  0.081   1.00 27.94  ? 375  GLN A OE1 1 
ATOM   2607  N  NE2 . GLN A  1 375 ? 21.178  14.119  0.384   1.00 26.26  ? 375  GLN A NE2 1 
ATOM   2608  N  N   . TRP A  1 376 ? 21.809  14.362  -5.542  1.00 28.12  ? 376  TRP A N   1 
ATOM   2609  C  CA  . TRP A  1 376 ? 21.504  14.319  -6.995  1.00 27.80  ? 376  TRP A CA  1 
ATOM   2610  C  C   . TRP A  1 376 ? 20.710  13.073  -7.469  1.00 29.77  ? 376  TRP A C   1 
ATOM   2611  O  O   . TRP A  1 376 ? 19.564  13.195  -7.937  1.00 27.94  ? 376  TRP A O   1 
ATOM   2612  C  CB  . TRP A  1 376 ? 22.794  14.393  -7.785  1.00 28.93  ? 376  TRP A CB  1 
ATOM   2613  C  CG  . TRP A  1 376 ? 23.519  15.704  -7.598  1.00 30.92  ? 376  TRP A CG  1 
ATOM   2614  C  CD1 . TRP A  1 376 ? 23.469  16.769  -8.417  1.00 26.95  ? 376  TRP A CD1 1 
ATOM   2615  C  CD2 . TRP A  1 376 ? 24.389  16.063  -6.523  1.00 28.50  ? 376  TRP A CD2 1 
ATOM   2616  N  NE1 . TRP A  1 376 ? 24.256  17.777  -7.942  1.00 31.19  ? 376  TRP A NE1 1 
ATOM   2617  C  CE2 . TRP A  1 376 ? 24.844  17.370  -6.780  1.00 32.51  ? 376  TRP A CE2 1 
ATOM   2618  C  CE3 . TRP A  1 376 ? 24.827  15.408  -5.364  1.00 27.20  ? 376  TRP A CE3 1 
ATOM   2619  C  CZ2 . TRP A  1 376 ? 25.709  18.056  -5.913  1.00 33.00  ? 376  TRP A CZ2 1 
ATOM   2620  C  CZ3 . TRP A  1 376 ? 25.710  16.070  -4.517  1.00 28.57  ? 376  TRP A CZ3 1 
ATOM   2621  C  CH2 . TRP A  1 376 ? 26.135  17.383  -4.791  1.00 33.01  ? 376  TRP A CH2 1 
ATOM   2622  N  N   . PHE A  1 377 ? 21.323  11.889  -7.365  1.00 27.55  ? 377  PHE A N   1 
ATOM   2623  C  CA  . PHE A  1 377 ? 20.621  10.617  -7.647  1.00 26.79  ? 377  PHE A CA  1 
ATOM   2624  C  C   . PHE A  1 377 ? 19.669  10.207  -6.530  1.00 25.98  ? 377  PHE A C   1 
ATOM   2625  O  O   . PHE A  1 377 ? 20.024  9.435   -5.650  1.00 29.39  ? 377  PHE A O   1 
ATOM   2626  C  CB  . PHE A  1 377 ? 21.621  9.464   -7.895  1.00 24.95  ? 377  PHE A CB  1 
ATOM   2627  C  CG  . PHE A  1 377 ? 22.376  9.595   -9.182  1.00 26.71  ? 377  PHE A CG  1 
ATOM   2628  C  CD1 . PHE A  1 377 ? 21.766  9.331   -10.376 1.00 23.07  ? 377  PHE A CD1 1 
ATOM   2629  C  CD2 . PHE A  1 377 ? 23.692  10.034  -9.188  1.00 27.73  ? 377  PHE A CD2 1 
ATOM   2630  C  CE1 . PHE A  1 377 ? 22.464  9.473   -11.556 1.00 31.23  ? 377  PHE A CE1 1 
ATOM   2631  C  CE2 . PHE A  1 377 ? 24.380  10.176  -10.341 1.00 27.43  ? 377  PHE A CE2 1 
ATOM   2632  C  CZ  . PHE A  1 377 ? 23.766  9.898   -11.539 1.00 34.26  ? 377  PHE A CZ  1 
ATOM   2633  N  N   . GLY A  1 378 ? 18.440  10.687  -6.584  1.00 30.42  ? 378  GLY A N   1 
ATOM   2634  C  CA  . GLY A  1 378 ? 17.468  10.370  -5.559  1.00 22.04  ? 378  GLY A CA  1 
ATOM   2635  C  C   . GLY A  1 378 ? 16.634  11.586  -5.274  1.00 28.53  ? 378  GLY A C   1 
ATOM   2636  O  O   . GLY A  1 378 ? 15.412  11.538  -5.363  1.00 31.40  ? 378  GLY A O   1 
ATOM   2637  N  N   . ASN A  1 379 ? 17.299  12.699  -4.955  1.00 32.31  ? 379  ASN A N   1 
ATOM   2638  C  CA  . ASN A  1 379 ? 16.592  13.901  -4.523  1.00 24.07  ? 379  ASN A CA  1 
ATOM   2639  C  C   . ASN A  1 379 ? 16.293  14.822  -5.702  1.00 25.77  ? 379  ASN A C   1 
ATOM   2640  O  O   . ASN A  1 379 ? 15.129  15.057  -6.004  1.00 26.53  ? 379  ASN A O   1 
ATOM   2641  C  CB  . ASN A  1 379 ? 17.382  14.613  -3.430  1.00 22.33  ? 379  ASN A CB  1 
ATOM   2642  C  CG  . ASN A  1 379 ? 17.682  13.691  -2.220  1.00 30.03  ? 379  ASN A CG  1 
ATOM   2643  O  OD1 . ASN A  1 379 ? 17.195  12.567  -2.156  1.00 29.61  ? 379  ASN A OD1 1 
ATOM   2644  N  ND2 . ASN A  1 379 ? 18.464  14.186  -1.251  1.00 28.83  ? 379  ASN A ND2 1 
ATOM   2645  N  N   . LEU A  1 380 ? 17.340  15.335  -6.350  1.00 24.82  ? 380  LEU A N   1 
ATOM   2646  C  CA  . LEU A  1 380 ? 17.212  16.140  -7.560  1.00 26.90  ? 380  LEU A CA  1 
ATOM   2647  C  C   . LEU A  1 380 ? 16.486  15.359  -8.655  1.00 27.73  ? 380  LEU A C   1 
ATOM   2648  O  O   . LEU A  1 380 ? 15.483  15.824  -9.189  1.00 32.08  ? 380  LEU A O   1 
ATOM   2649  C  CB  . LEU A  1 380 ? 18.586  16.585  -8.048  1.00 23.99  ? 380  LEU A CB  1 
ATOM   2650  C  CG  . LEU A  1 380 ? 18.618  17.633  -9.163  1.00 25.08  ? 380  LEU A CG  1 
ATOM   2651  C  CD1 . LEU A  1 380 ? 17.859  18.920  -8.809  1.00 24.86  ? 380  LEU A CD1 1 
ATOM   2652  C  CD2 . LEU A  1 380 ? 20.056  17.964  -9.475  1.00 26.65  ? 380  LEU A CD2 1 
ATOM   2653  N  N   . VAL A  1 381 ? 16.984  14.161  -8.964  1.00 27.29  ? 381  VAL A N   1 
ATOM   2654  C  CA  . VAL A  1 381 ? 16.287  13.259  -9.869  1.00 28.60  ? 381  VAL A CA  1 
ATOM   2655  C  C   . VAL A  1 381 ? 15.761  12.049  -9.117  1.00 29.92  ? 381  VAL A C   1 
ATOM   2656  O  O   . VAL A  1 381 ? 16.536  11.301  -8.533  1.00 33.44  ? 381  VAL A O   1 
ATOM   2657  C  CB  . VAL A  1 381 ? 17.204  12.786  -10.999 1.00 27.56  ? 381  VAL A CB  1 
ATOM   2658  C  CG1 . VAL A  1 381 ? 16.461  11.849  -11.894 1.00 29.54  ? 381  VAL A CG1 1 
ATOM   2659  C  CG2 . VAL A  1 381 ? 17.751  13.977  -11.761 1.00 21.98  ? 381  VAL A CG2 1 
ATOM   2660  N  N   . THR A  1 382 ? 14.452  11.845  -9.127  1.00 27.48  ? 382  THR A N   1 
ATOM   2661  C  CA  . THR A  1 382 ? 13.870  10.714  -8.408  1.00 29.95  ? 382  THR A CA  1 
ATOM   2662  C  C   . THR A  1 382 ? 13.273  9.676   -9.367  1.00 33.38  ? 382  THR A C   1 
ATOM   2663  O  O   . THR A  1 382 ? 12.776  10.026  -10.439 1.00 33.91  ? 382  THR A O   1 
ATOM   2664  C  CB  . THR A  1 382 ? 12.770  11.181  -7.414  1.00 31.78  ? 382  THR A CB  1 
ATOM   2665  O  OG1 . THR A  1 382 ? 13.263  12.244  -6.584  1.00 27.27  ? 382  THR A OG1 1 
ATOM   2666  C  CG2 . THR A  1 382 ? 12.320  10.034  -6.528  1.00 30.27  ? 382  THR A CG2 1 
ATOM   2667  N  N   . MET A  1 383 ? 13.305  8.400   -8.996  1.00 32.92  ? 383  MET A N   1 
ATOM   2668  C  CA  . MET A  1 383 ? 12.677  7.393   -9.855  1.00 34.49  ? 383  MET A CA  1 
ATOM   2669  C  C   . MET A  1 383 ? 11.174  7.597   -9.854  1.00 30.38  ? 383  MET A C   1 
ATOM   2670  O  O   . MET A  1 383 ? 10.606  8.072   -8.887  1.00 31.99  ? 383  MET A O   1 
ATOM   2671  C  CB  . MET A  1 383 ? 13.004  5.960   -9.414  1.00 34.60  ? 383  MET A CB  1 
ATOM   2672  C  CG  . MET A  1 383 ? 12.056  5.417   -8.335  1.00 32.53  ? 383  MET A CG  1 
ATOM   2673  S  SD  . MET A  1 383 ? 12.470  6.139   -6.737  1.00 42.01  ? 383  MET A SD  1 
ATOM   2674  C  CE  . MET A  1 383 ? 14.142  5.800   -6.986  1.00 31.82  ? 383  MET A CE  1 
ATOM   2675  N  N   . GLU A  1 384 ? 10.544  7.234   -10.958 1.00 38.07  ? 384  GLU A N   1 
ATOM   2676  C  CA  . GLU A  1 384 ? 9.116   7.441   -11.141 1.00 39.71  ? 384  GLU A CA  1 
ATOM   2677  C  C   . GLU A  1 384 ? 8.295   6.595   -10.174 1.00 34.27  ? 384  GLU A C   1 
ATOM   2678  O  O   . GLU A  1 384 ? 7.309   7.064   -9.600  1.00 32.41  ? 384  GLU A O   1 
ATOM   2679  C  CB  . GLU A  1 384 ? 8.746   7.115   -12.586 1.00 38.93  ? 384  GLU A CB  1 
ATOM   2680  C  CG  . GLU A  1 384 ? 7.409   7.645   -13.033 1.00 41.84  ? 384  GLU A CG  1 
ATOM   2681  C  CD  . GLU A  1 384 ? 7.182   7.417   -14.510 1.00 45.16  ? 384  GLU A CD  1 
ATOM   2682  O  OE1 . GLU A  1 384 ? 7.945   7.968   -15.339 1.00 48.43  ? 384  GLU A OE1 1 
ATOM   2683  O  OE2 . GLU A  1 384 ? 6.246   6.672   -14.835 1.00 50.90  ? 384  GLU A OE2 1 
ATOM   2684  N  N   . TRP A  1 385 ? 8.714   5.348   -10.004 1.00 27.94  ? 385  TRP A N   1 
ATOM   2685  C  CA  . TRP A  1 385 ? 8.061   4.422   -9.090  1.00 27.64  ? 385  TRP A CA  1 
ATOM   2686  C  C   . TRP A  1 385 ? 9.116   3.401   -8.583  1.00 31.98  ? 385  TRP A C   1 
ATOM   2687  O  O   . TRP A  1 385 ? 10.165  3.208   -9.200  1.00 35.73  ? 385  TRP A O   1 
ATOM   2688  C  CB  . TRP A  1 385 ? 6.868   3.730   -9.788  1.00 32.29  ? 385  TRP A CB  1 
ATOM   2689  C  CG  . TRP A  1 385 ? 6.117   2.786   -8.928  1.00 32.49  ? 385  TRP A CG  1 
ATOM   2690  C  CD1 . TRP A  1 385 ? 6.054   1.429   -9.060  1.00 31.93  ? 385  TRP A CD1 1 
ATOM   2691  C  CD2 . TRP A  1 385 ? 5.362   3.109   -7.753  1.00 30.13  ? 385  TRP A CD2 1 
ATOM   2692  N  NE1 . TRP A  1 385 ? 5.278   0.889   -8.059  1.00 22.52  ? 385  TRP A NE1 1 
ATOM   2693  C  CE2 . TRP A  1 385 ? 4.853   1.894   -7.236  1.00 27.13  ? 385  TRP A CE2 1 
ATOM   2694  C  CE3 . TRP A  1 385 ? 5.055   4.300   -7.097  1.00 28.71  ? 385  TRP A CE3 1 
ATOM   2695  C  CZ2 . TRP A  1 385 ? 4.061   1.838   -6.086  1.00 33.80  ? 385  TRP A CZ2 1 
ATOM   2696  C  CZ3 . TRP A  1 385 ? 4.260   4.246   -5.953  1.00 32.43  ? 385  TRP A CZ3 1 
ATOM   2697  C  CH2 . TRP A  1 385 ? 3.777   3.019   -5.458  1.00 34.88  ? 385  TRP A CH2 1 
ATOM   2698  N  N   . TRP A  1 386 ? 8.833   2.742   -7.476  1.00 28.29  ? 386  TRP A N   1 
ATOM   2699  C  CA  . TRP A  1 386 ? 9.817   1.890   -6.821  1.00 33.19  ? 386  TRP A CA  1 
ATOM   2700  C  C   . TRP A  1 386 ? 10.366  0.720   -7.642  1.00 35.35  ? 386  TRP A C   1 
ATOM   2701  O  O   . TRP A  1 386 ? 11.300  0.049   -7.218  1.00 33.03  ? 386  TRP A O   1 
ATOM   2702  C  CB  . TRP A  1 386 ? 9.205   1.359   -5.545  1.00 27.09  ? 386  TRP A CB  1 
ATOM   2703  C  CG  . TRP A  1 386 ? 8.666   2.448   -4.745  1.00 33.02  ? 386  TRP A CG  1 
ATOM   2704  C  CD1 . TRP A  1 386 ? 7.367   2.821   -4.652  1.00 32.54  ? 386  TRP A CD1 1 
ATOM   2705  C  CD2 . TRP A  1 386 ? 9.415   3.372   -3.941  1.00 31.71  ? 386  TRP A CD2 1 
ATOM   2706  N  NE1 . TRP A  1 386 ? 7.252   3.897   -3.823  1.00 26.01  ? 386  TRP A NE1 1 
ATOM   2707  C  CE2 . TRP A  1 386 ? 8.496   4.262   -3.377  1.00 27.92  ? 386  TRP A CE2 1 
ATOM   2708  C  CE3 . TRP A  1 386 ? 10.772  3.520   -3.639  1.00 29.42  ? 386  TRP A CE3 1 
ATOM   2709  C  CZ2 . TRP A  1 386 ? 8.884   5.296   -2.507  1.00 30.97  ? 386  TRP A CZ2 1 
ATOM   2710  C  CZ3 . TRP A  1 386 ? 11.158  4.536   -2.773  1.00 34.03  ? 386  TRP A CZ3 1 
ATOM   2711  C  CH2 . TRP A  1 386 ? 10.215  5.418   -2.224  1.00 33.03  ? 386  TRP A CH2 1 
ATOM   2712  N  N   . ASN A  1 387 ? 9.791   0.487   -8.814  1.00 34.23  ? 387  ASN A N   1 
ATOM   2713  C  CA  . ASN A  1 387 ? 10.260  -0.588  -9.673  1.00 32.74  ? 387  ASN A CA  1 
ATOM   2714  C  C   . ASN A  1 387 ? 11.607  -0.199  -10.234 1.00 35.65  ? 387  ASN A C   1 
ATOM   2715  O  O   . ASN A  1 387 ? 12.373  -1.070  -10.648 1.00 38.00  ? 387  ASN A O   1 
ATOM   2716  C  CB  . ASN A  1 387 ? 9.266   -0.881  -10.811 1.00 33.78  ? 387  ASN A CB  1 
ATOM   2717  C  CG  . ASN A  1 387 ? 8.995   0.335   -11.663 1.00 38.81  ? 387  ASN A CG  1 
ATOM   2718  O  OD1 . ASN A  1 387 ? 8.708   1.429   -11.144 1.00 39.43  ? 387  ASN A OD1 1 
ATOM   2719  N  ND2 . ASN A  1 387 ? 9.135   0.178   -12.970 1.00 42.29  ? 387  ASN A ND2 1 
ATOM   2720  N  N   . ASP A  1 388 ? 11.900  1.106   -10.246 1.00 29.97  ? 388  ASP A N   1 
ATOM   2721  C  CA  . ASP A  1 388 ? 13.220  1.574   -10.667 1.00 31.47  ? 388  ASP A CA  1 
ATOM   2722  C  C   . ASP A  1 388 ? 14.014  2.216   -9.510  1.00 27.67  ? 388  ASP A C   1 
ATOM   2723  O  O   . ASP A  1 388 ? 14.894  3.061   -9.755  1.00 29.88  ? 388  ASP A O   1 
ATOM   2724  C  CB  . ASP A  1 388 ? 13.108  2.563   -11.849 1.00 37.67  ? 388  ASP A CB  1 
ATOM   2725  C  CG  . ASP A  1 388 ? 12.608  1.906   -13.133 1.00 42.47  ? 388  ASP A CG  1 
ATOM   2726  O  OD1 . ASP A  1 388 ? 12.964  0.730   -13.381 1.00 42.17  ? 388  ASP A OD1 1 
ATOM   2727  O  OD2 . ASP A  1 388 ? 11.862  2.568   -13.899 1.00 39.07  ? 388  ASP A OD2 1 
ATOM   2728  N  N   . ILE A  1 389 ? 13.729  1.798   -8.268  1.00 27.10  ? 389  ILE A N   1 
ATOM   2729  C  CA  . ILE A  1 389 ? 14.494  2.240   -7.092  1.00 27.71  ? 389  ILE A CA  1 
ATOM   2730  C  C   . ILE A  1 389 ? 16.000  2.233   -7.350  1.00 30.91  ? 389  ILE A C   1 
ATOM   2731  O  O   . ILE A  1 389 ? 16.709  3.092   -6.827  1.00 36.67  ? 389  ILE A O   1 
ATOM   2732  C  CB  . ILE A  1 389 ? 14.192  1.363   -5.852  1.00 32.01  ? 389  ILE A CB  1 
ATOM   2733  C  CG1 . ILE A  1 389 ? 14.893  1.893   -4.579  1.00 30.69  ? 389  ILE A CG1 1 
ATOM   2734  C  CG2 . ILE A  1 389 ? 14.579  -0.081  -6.117  1.00 29.33  ? 389  ILE A CG2 1 
ATOM   2735  C  CD1 . ILE A  1 389 ? 14.764  3.409   -4.307  1.00 25.61  ? 389  ILE A CD1 1 
ATOM   2736  N  N   . TRP A  1 390 ? 16.469  1.310   -8.196  1.00 23.62  ? 390  TRP A N   1 
ATOM   2737  C  CA  . TRP A  1 390 ? 17.874  1.187   -8.538  1.00 27.68  ? 390  TRP A CA  1 
ATOM   2738  C  C   . TRP A  1 390 ? 18.439  2.439   -9.201  1.00 30.24  ? 390  TRP A C   1 
ATOM   2739  O  O   . TRP A  1 390 ? 19.642  2.700   -9.087  1.00 30.50  ? 390  TRP A O   1 
ATOM   2740  C  CB  . TRP A  1 390 ? 18.117  -0.033  -9.461  1.00 31.15  ? 390  TRP A CB  1 
ATOM   2741  C  CG  . TRP A  1 390 ? 18.007  0.281   -10.922 1.00 34.12  ? 390  TRP A CG  1 
ATOM   2742  C  CD1 . TRP A  1 390 ? 16.868  0.287   -11.668 1.00 36.85  ? 390  TRP A CD1 1 
ATOM   2743  C  CD2 . TRP A  1 390 ? 19.070  0.649   -11.814 1.00 31.65  ? 390  TRP A CD2 1 
ATOM   2744  N  NE1 . TRP A  1 390 ? 17.153  0.639   -12.953 1.00 35.98  ? 390  TRP A NE1 1 
ATOM   2745  C  CE2 . TRP A  1 390 ? 18.498  0.870   -13.071 1.00 29.90  ? 390  TRP A CE2 1 
ATOM   2746  C  CE3 . TRP A  1 390 ? 20.445  0.826   -11.662 1.00 31.54  ? 390  TRP A CE3 1 
ATOM   2747  C  CZ2 . TRP A  1 390 ? 19.247  1.247   -14.176 1.00 28.02  ? 390  TRP A CZ2 1 
ATOM   2748  C  CZ3 . TRP A  1 390 ? 21.194  1.195   -12.761 1.00 24.61  ? 390  TRP A CZ3 1 
ATOM   2749  C  CH2 . TRP A  1 390 ? 20.587  1.414   -14.000 1.00 29.95  ? 390  TRP A CH2 1 
ATOM   2750  N  N   . LEU A  1 391 ? 17.599  3.203   -9.907  1.00 31.75  ? 391  LEU A N   1 
ATOM   2751  C  CA  . LEU A  1 391 ? 18.031  4.518   -10.434 1.00 27.78  ? 391  LEU A CA  1 
ATOM   2752  C  C   . LEU A  1 391 ? 18.637  5.359   -9.319  1.00 31.47  ? 391  LEU A C   1 
ATOM   2753  O  O   . LEU A  1 391 ? 19.685  5.974   -9.519  1.00 32.21  ? 391  LEU A O   1 
ATOM   2754  C  CB  . LEU A  1 391 ? 16.872  5.256   -11.120 1.00 30.64  ? 391  LEU A CB  1 
ATOM   2755  C  CG  . LEU A  1 391 ? 16.468  4.614   -12.483 1.00 35.59  ? 391  LEU A CG  1 
ATOM   2756  C  CD1 . LEU A  1 391 ? 15.297  5.282   -13.174 1.00 29.64  ? 391  LEU A CD1 1 
ATOM   2757  C  CD2 . LEU A  1 391 ? 17.647  4.533   -13.449 1.00 30.28  ? 391  LEU A CD2 1 
ATOM   2758  N  N   . ASN A  1 392 ? 18.008  5.327   -8.135  1.00 28.09  ? 392  ASN A N   1 
ATOM   2759  C  CA  . ASN A  1 392 ? 18.600  5.890   -6.918  1.00 28.87  ? 392  ASN A CA  1 
ATOM   2760  C  C   . ASN A  1 392 ? 19.787  5.099   -6.373  1.00 30.66  ? 392  ASN A C   1 
ATOM   2761  O  O   . ASN A  1 392 ? 20.893  5.636   -6.230  1.00 29.52  ? 392  ASN A O   1 
ATOM   2762  C  CB  . ASN A  1 392 ? 17.573  5.984   -5.785  1.00 30.87  ? 392  ASN A CB  1 
ATOM   2763  C  CG  . ASN A  1 392 ? 16.597  7.101   -5.973  1.00 31.16  ? 392  ASN A CG  1 
ATOM   2764  O  OD1 . ASN A  1 392 ? 16.458  7.632   -7.081  1.00 28.88  ? 392  ASN A OD1 1 
ATOM   2765  N  ND2 . ASN A  1 392 ? 15.828  7.402   -4.924  1.00 23.96  ? 392  ASN A ND2 1 
ATOM   2766  N  N   . GLU A  1 393 ? 19.547  3.828   -6.052  1.00 26.89  ? 393  GLU A N   1 
ATOM   2767  C  CA  . GLU A  1 393 ? 20.490  3.107   -5.223  1.00 26.42  ? 393  GLU A CA  1 
ATOM   2768  C  C   . GLU A  1 393 ? 21.663  2.502   -5.939  1.00 27.29  ? 393  GLU A C   1 
ATOM   2769  O  O   . GLU A  1 393 ? 22.772  2.561   -5.425  1.00 28.97  ? 393  GLU A O   1 
ATOM   2770  C  CB  . GLU A  1 393 ? 19.757  2.051   -4.422  1.00 24.75  ? 393  GLU A CB  1 
ATOM   2771  C  CG  . GLU A  1 393 ? 18.890  2.712   -3.384  1.00 29.19  ? 393  GLU A CG  1 
ATOM   2772  C  CD  . GLU A  1 393 ? 19.681  3.438   -2.295  1.00 27.69  ? 393  GLU A CD  1 
ATOM   2773  O  OE1 . GLU A  1 393 ? 20.898  3.726   -2.386  1.00 33.05  ? 393  GLU A OE1 1 
ATOM   2774  O  OE2 . GLU A  1 393 ? 19.093  3.729   -1.282  1.00 29.72  ? 393  GLU A OE2 1 
ATOM   2775  N  N   . GLY A  1 394 ? 21.434  1.937   -7.120  1.00 29.91  ? 394  GLY A N   1 
ATOM   2776  C  CA  . GLY A  1 394 ? 22.525  1.428   -7.929  1.00 28.84  ? 394  GLY A CA  1 
ATOM   2777  C  C   . GLY A  1 394 ? 23.500  2.548   -8.253  1.00 30.51  ? 394  GLY A C   1 
ATOM   2778  O  O   . GLY A  1 394 ? 24.702  2.330   -8.301  1.00 33.31  ? 394  GLY A O   1 
ATOM   2779  N  N   . PHE A  1 395 ? 22.978  3.758   -8.422  1.00 31.11  ? 395  PHE A N   1 
ATOM   2780  C  CA  . PHE A  1 395 ? 23.803  4.924   -8.743  1.00 29.62  ? 395  PHE A CA  1 
ATOM   2781  C  C   . PHE A  1 395 ? 24.568  5.532   -7.554  1.00 33.07  ? 395  PHE A C   1 
ATOM   2782  O  O   . PHE A  1 395 ? 25.764  5.847   -7.668  1.00 29.47  ? 395  PHE A O   1 
ATOM   2783  C  CB  . PHE A  1 395 ? 22.924  5.988   -9.408  1.00 24.32  ? 395  PHE A CB  1 
ATOM   2784  C  CG  . PHE A  1 395 ? 23.066  5.995   -10.901 1.00 30.64  ? 395  PHE A CG  1 
ATOM   2785  C  CD1 . PHE A  1 395 ? 24.115  6.681   -11.500 1.00 25.37  ? 395  PHE A CD1 1 
ATOM   2786  C  CD2 . PHE A  1 395 ? 22.217  5.229   -11.708 1.00 35.06  ? 395  PHE A CD2 1 
ATOM   2787  C  CE1 . PHE A  1 395 ? 24.278  6.666   -12.895 1.00 31.03  ? 395  PHE A CE1 1 
ATOM   2788  C  CE2 . PHE A  1 395 ? 22.381  5.200   -13.107 1.00 31.05  ? 395  PHE A CE2 1 
ATOM   2789  C  CZ  . PHE A  1 395 ? 23.416  5.921   -13.697 1.00 27.71  ? 395  PHE A CZ  1 
ATOM   2790  N  N   . ALA A  1 396 ? 23.892  5.684   -6.417  1.00 27.73  ? 396  ALA A N   1 
ATOM   2791  C  CA  . ALA A  1 396 ? 24.570  6.145   -5.220  1.00 26.56  ? 396  ALA A CA  1 
ATOM   2792  C  C   . ALA A  1 396 ? 25.682  5.170   -4.922  1.00 31.88  ? 396  ALA A C   1 
ATOM   2793  O  O   . ALA A  1 396 ? 26.811  5.569   -4.615  1.00 31.54  ? 396  ALA A O   1 
ATOM   2794  C  CB  . ALA A  1 396 ? 23.616  6.247   -4.048  1.00 26.67  ? 396  ALA A CB  1 
ATOM   2795  N  N   . LYS A  1 397 ? 25.360  3.882   -5.054  1.00 29.84  ? 397  LYS A N   1 
ATOM   2796  C  CA  . LYS A  1 397 ? 26.307  2.840   -4.721  1.00 29.49  ? 397  LYS A CA  1 
ATOM   2797  C  C   . LYS A  1 397 ? 27.549  3.007   -5.583  1.00 30.46  ? 397  LYS A C   1 
ATOM   2798  O  O   . LYS A  1 397 ? 28.662  3.029   -5.078  1.00 29.60  ? 397  LYS A O   1 
ATOM   2799  C  CB  . LYS A  1 397 ? 25.685  1.463   -4.915  1.00 29.38  ? 397  LYS A CB  1 
ATOM   2800  C  CG  . LYS A  1 397 ? 26.568  0.314   -4.461  1.00 31.93  ? 397  LYS A CG  1 
ATOM   2801  C  CD  . LYS A  1 397 ? 26.373  0.018   -2.990  1.00 33.21  ? 397  LYS A CD  1 
ATOM   2802  C  CE  . LYS A  1 397 ? 27.308  -1.080  -2.516  1.00 36.41  ? 397  LYS A CE  1 
ATOM   2803  N  NZ  . LYS A  1 397 ? 28.545  -0.540  -1.867  1.00 41.25  ? 397  LYS A NZ  1 
ATOM   2804  N  N   . TYR A  1 398 ? 27.350  3.163   -6.885  1.00 32.48  ? 398  TYR A N   1 
ATOM   2805  C  CA  . TYR A  1 398 ? 28.470  3.375   -7.787  1.00 31.02  ? 398  TYR A CA  1 
ATOM   2806  C  C   . TYR A  1 398 ? 29.248  4.678   -7.520  1.00 34.57  ? 398  TYR A C   1 
ATOM   2807  O  O   . TYR A  1 398 ? 30.489  4.680   -7.596  1.00 33.86  ? 398  TYR A O   1 
ATOM   2808  C  CB  . TYR A  1 398 ? 28.001  3.370   -9.243  1.00 31.17  ? 398  TYR A CB  1 
ATOM   2809  C  CG  . TYR A  1 398 ? 29.178  3.236   -10.165 1.00 40.14  ? 398  TYR A CG  1 
ATOM   2810  C  CD1 . TYR A  1 398 ? 30.126  2.242   -9.935  1.00 44.93  ? 398  TYR A CD1 1 
ATOM   2811  C  CD2 . TYR A  1 398 ? 29.382  4.110   -11.226 1.00 41.29  ? 398  TYR A CD2 1 
ATOM   2812  C  CE1 . TYR A  1 398 ? 31.229  2.112   -10.736 1.00 44.53  ? 398  TYR A CE1 1 
ATOM   2813  C  CE2 . TYR A  1 398 ? 30.495  3.980   -12.052 1.00 43.46  ? 398  TYR A CE2 1 
ATOM   2814  C  CZ  . TYR A  1 398 ? 31.415  2.978   -11.798 1.00 45.91  ? 398  TYR A CZ  1 
ATOM   2815  O  OH  . TYR A  1 398 ? 32.539  2.809   -12.595 1.00 55.51  ? 398  TYR A OH  1 
ATOM   2816  N  N   . MET A  1 399 ? 28.536  5.775   -7.233  1.00 28.05  ? 399  MET A N   1 
ATOM   2817  C  CA  . MET A  1 399 ? 29.201  7.065   -7.000  1.00 26.27  ? 399  MET A CA  1 
ATOM   2818  C  C   . MET A  1 399 ? 30.111  7.021   -5.787  1.00 29.35  ? 399  MET A C   1 
ATOM   2819  O  O   . MET A  1 399 ? 31.104  7.730   -5.754  1.00 34.62  ? 399  MET A O   1 
ATOM   2820  C  CB  . MET A  1 399 ? 28.190  8.225   -6.855  1.00 31.33  ? 399  MET A CB  1 
ATOM   2821  C  CG  . MET A  1 399 ? 27.467  8.659   -8.157  1.00 23.06  ? 399  MET A CG  1 
ATOM   2822  S  SD  . MET A  1 399 ? 28.509  8.718   -9.647  1.00 37.03  ? 399  MET A SD  1 
ATOM   2823  C  CE  . MET A  1 399 ? 29.794  9.869   -9.148  1.00 32.52  ? 399  MET A CE  1 
ATOM   2824  N  N   . GLU A  1 400 ? 29.792  6.177   -4.807  1.00 28.61  ? 400  GLU A N   1 
ATOM   2825  C  CA  . GLU A  1 400 ? 30.736  5.862   -3.742  1.00 31.24  ? 400  GLU A CA  1 
ATOM   2826  C  C   . GLU A  1 400 ? 32.122  5.609   -4.304  1.00 33.35  ? 400  GLU A C   1 
ATOM   2827  O  O   . GLU A  1 400 ? 33.082  6.278   -3.943  1.00 39.34  ? 400  GLU A O   1 
ATOM   2828  C  CB  . GLU A  1 400 ? 30.326  4.619   -2.940  1.00 30.96  ? 400  GLU A CB  1 
ATOM   2829  C  CG  . GLU A  1 400 ? 29.026  4.673   -2.211  1.00 33.79  ? 400  GLU A CG  1 
ATOM   2830  C  CD  . GLU A  1 400 ? 28.727  3.341   -1.508  1.00 34.36  ? 400  GLU A CD  1 
ATOM   2831  O  OE1 . GLU A  1 400 ? 29.689  2.632   -1.173  1.00 39.98  ? 400  GLU A OE1 1 
ATOM   2832  O  OE2 . GLU A  1 400 ? 27.548  2.998   -1.294  1.00 32.94  ? 400  GLU A OE2 1 
ATOM   2833  N  N   . LEU A  1 401 ? 32.226  4.615   -5.169  1.00 30.49  ? 401  LEU A N   1 
ATOM   2834  C  CA  . LEU A  1 401 ? 33.493  4.329   -5.826  1.00 35.94  ? 401  LEU A CA  1 
ATOM   2835  C  C   . LEU A  1 401 ? 34.088  5.544   -6.552  1.00 35.74  ? 401  LEU A C   1 
ATOM   2836  O  O   . LEU A  1 401 ? 35.247  5.869   -6.349  1.00 34.75  ? 401  LEU A O   1 
ATOM   2837  C  CB  . LEU A  1 401 ? 33.331  3.172   -6.821  1.00 36.27  ? 401  LEU A CB  1 
ATOM   2838  C  CG  . LEU A  1 401 ? 34.590  2.851   -7.641  1.00 42.52  ? 401  LEU A CG  1 
ATOM   2839  C  CD1 . LEU A  1 401 ? 35.702  2.258   -6.753  1.00 41.51  ? 401  LEU A CD1 1 
ATOM   2840  C  CD2 . LEU A  1 401 ? 34.267  1.940   -8.831  1.00 37.79  ? 401  LEU A CD2 1 
ATOM   2841  N  N   . ILE A  1 402 ? 33.318  6.222   -7.394  1.00 31.69  ? 402  ILE A N   1 
ATOM   2842  C  CA  . ILE A  1 402 ? 33.923  7.308   -8.153  1.00 36.23  ? 402  ILE A CA  1 
ATOM   2843  C  C   . ILE A  1 402 ? 34.404  8.428   -7.229  1.00 36.93  ? 402  ILE A C   1 
ATOM   2844  O  O   . ILE A  1 402 ? 35.493  8.977   -7.423  1.00 39.13  ? 402  ILE A O   1 
ATOM   2845  C  CB  . ILE A  1 402 ? 32.966  7.910   -9.201  1.00 35.02  ? 402  ILE A CB  1 
ATOM   2846  C  CG1 . ILE A  1 402 ? 32.322  6.816   -10.053 1.00 36.23  ? 402  ILE A CG1 1 
ATOM   2847  C  CG2 . ILE A  1 402 ? 33.724  8.879   -10.082 1.00 39.34  ? 402  ILE A CG2 1 
ATOM   2848  C  CD1 . ILE A  1 402 ? 33.318  5.854   -10.645 1.00 37.47  ? 402  ILE A CD1 1 
ATOM   2849  N  N   . ALA A  1 403 ? 33.610  8.741   -6.208  1.00 35.11  ? 403  ALA A N   1 
ATOM   2850  C  CA  . ALA A  1 403 ? 33.867  9.914   -5.380  1.00 30.86  ? 403  ALA A CA  1 
ATOM   2851  C  C   . ALA A  1 403 ? 34.930  9.659   -4.311  1.00 33.41  ? 403  ALA A C   1 
ATOM   2852  O  O   . ALA A  1 403 ? 35.790  10.517  -4.063  1.00 35.22  ? 403  ALA A O   1 
ATOM   2853  C  CB  . ALA A  1 403 ? 32.593  10.385  -4.751  1.00 29.45  ? 403  ALA A CB  1 
ATOM   2854  N  N   . VAL A  1 404 ? 34.886  8.495   -3.677  1.00 25.99  ? 404  VAL A N   1 
ATOM   2855  C  CA  . VAL A  1 404 ? 35.876  8.192   -2.653  1.00 30.53  ? 404  VAL A CA  1 
ATOM   2856  C  C   . VAL A  1 404 ? 37.248  8.046   -3.312  1.00 39.45  ? 404  VAL A C   1 
ATOM   2857  O  O   . VAL A  1 404 ? 38.248  8.570   -2.801  1.00 32.55  ? 404  VAL A O   1 
ATOM   2858  C  CB  . VAL A  1 404 ? 35.510  6.924   -1.847  1.00 32.58  ? 404  VAL A CB  1 
ATOM   2859  C  CG1 . VAL A  1 404 ? 36.577  6.608   -0.815  1.00 27.91  ? 404  VAL A CG1 1 
ATOM   2860  C  CG2 . VAL A  1 404 ? 34.188  7.130   -1.124  1.00 33.21  ? 404  VAL A CG2 1 
ATOM   2861  N  N   . ASN A  1 405 ? 37.276  7.354   -4.458  1.00 37.40  ? 405  ASN A N   1 
ATOM   2862  C  CA  . ASN A  1 405 ? 38.465  7.260   -5.302  1.00 37.79  ? 405  ASN A CA  1 
ATOM   2863  C  C   . ASN A  1 405 ? 39.070  8.599   -5.698  1.00 41.74  ? 405  ASN A C   1 
ATOM   2864  O  O   . ASN A  1 405 ? 40.283  8.741   -5.699  1.00 50.06  ? 405  ASN A O   1 
ATOM   2865  C  CB  . ASN A  1 405 ? 38.155  6.488   -6.573  1.00 43.72  ? 405  ASN A CB  1 
ATOM   2866  C  CG  . ASN A  1 405 ? 39.400  6.145   -7.368  1.00 48.01  ? 405  ASN A CG  1 
ATOM   2867  O  OD1 . ASN A  1 405 ? 40.269  5.436   -6.881  1.00 49.39  ? 405  ASN A OD1 1 
ATOM   2868  N  ND2 . ASN A  1 405 ? 39.479  6.641   -8.599  1.00 54.89  ? 405  ASN A ND2 1 
ATOM   2869  N  N   . ALA A  1 406 ? 38.230  9.577   -6.027  1.00 34.49  ? 406  ALA A N   1 
ATOM   2870  C  CA  . ALA A  1 406 ? 38.712  10.913  -6.379  1.00 39.31  ? 406  ALA A CA  1 
ATOM   2871  C  C   . ALA A  1 406 ? 39.128  11.791  -5.182  1.00 45.41  ? 406  ALA A C   1 
ATOM   2872  O  O   . ALA A  1 406 ? 40.009  12.628  -5.305  1.00 49.41  ? 406  ALA A O   1 
ATOM   2873  C  CB  . ALA A  1 406 ? 37.662  11.625  -7.176  1.00 33.08  ? 406  ALA A CB  1 
ATOM   2874  N  N   . THR A  1 407 ? 38.497  11.611  -4.031  1.00 43.35  ? 407  THR A N   1 
ATOM   2875  C  CA  . THR A  1 407 ? 38.737  12.513  -2.911  1.00 39.29  ? 407  THR A CA  1 
ATOM   2876  C  C   . THR A  1 407 ? 39.645  11.901  -1.857  1.00 37.61  ? 407  THR A C   1 
ATOM   2877  O  O   . THR A  1 407 ? 40.324  12.617  -1.122  1.00 40.21  ? 407  THR A O   1 
ATOM   2878  C  CB  . THR A  1 407 ? 37.429  12.917  -2.241  1.00 36.40  ? 407  THR A CB  1 
ATOM   2879  O  OG1 . THR A  1 407 ? 36.689  11.728  -1.943  1.00 46.17  ? 407  THR A OG1 1 
ATOM   2880  C  CG2 . THR A  1 407 ? 36.595  13.764  -3.166  1.00 30.98  ? 407  THR A CG2 1 
ATOM   2881  N  N   . TYR A  1 408 ? 39.656  10.576  -1.783  1.00 39.14  ? 408  TYR A N   1 
ATOM   2882  C  CA  . TYR A  1 408 ? 40.447  9.877   -0.778  1.00 40.99  ? 408  TYR A CA  1 
ATOM   2883  C  C   . TYR A  1 408 ? 41.090  8.614   -1.309  1.00 42.06  ? 408  TYR A C   1 
ATOM   2884  O  O   . TYR A  1 408 ? 40.898  7.545   -0.725  1.00 43.66  ? 408  TYR A O   1 
ATOM   2885  C  CB  . TYR A  1 408 ? 39.585  9.487   0.431   1.00 35.46  ? 408  TYR A CB  1 
ATOM   2886  C  CG  . TYR A  1 408 ? 39.124  10.604  1.319   1.00 31.24  ? 408  TYR A CG  1 
ATOM   2887  C  CD1 . TYR A  1 408 ? 39.954  11.102  2.299   1.00 38.00  ? 408  TYR A CD1 1 
ATOM   2888  C  CD2 . TYR A  1 408 ? 37.842  11.135  1.203   1.00 27.36  ? 408  TYR A CD2 1 
ATOM   2889  C  CE1 . TYR A  1 408 ? 39.535  12.107  3.152   1.00 41.32  ? 408  TYR A CE1 1 
ATOM   2890  C  CE2 . TYR A  1 408 ? 37.412  12.135  2.032   1.00 33.37  ? 408  TYR A CE2 1 
ATOM   2891  C  CZ  . TYR A  1 408 ? 38.270  12.630  3.013   1.00 43.95  ? 408  TYR A CZ  1 
ATOM   2892  O  OH  . TYR A  1 408 ? 37.888  13.643  3.869   1.00 39.91  ? 408  TYR A OH  1 
ATOM   2893  N  N   . PRO A  1 409 ? 41.870  8.719   -2.393  1.00 45.24  ? 409  PRO A N   1 
ATOM   2894  C  CA  . PRO A  1 409 ? 42.476  7.513   -2.966  1.00 44.40  ? 409  PRO A CA  1 
ATOM   2895  C  C   . PRO A  1 409 ? 43.245  6.669   -1.940  1.00 50.32  ? 409  PRO A C   1 
ATOM   2896  O  O   . PRO A  1 409 ? 43.323  5.449   -2.087  1.00 50.90  ? 409  PRO A O   1 
ATOM   2897  C  CB  . PRO A  1 409 ? 43.423  8.071   -4.030  1.00 37.82  ? 409  PRO A CB  1 
ATOM   2898  C  CG  . PRO A  1 409 ? 43.629  9.473   -3.668  1.00 39.44  ? 409  PRO A CG  1 
ATOM   2899  C  CD  . PRO A  1 409 ? 42.343  9.933   -3.072  1.00 44.17  ? 409  PRO A CD  1 
ATOM   2900  N  N   . GLU A  1 410 ? 43.774  7.300   -0.896  1.00 50.99  ? 410  GLU A N   1 
ATOM   2901  C  CA  . GLU A  1 410 ? 44.501  6.559   0.127   1.00 52.45  ? 410  GLU A CA  1 
ATOM   2902  C  C   . GLU A  1 410 ? 43.624  5.502   0.807   1.00 52.89  ? 410  GLU A C   1 
ATOM   2903  O  O   . GLU A  1 410 ? 44.136  4.571   1.430   1.00 51.35  ? 410  GLU A O   1 
ATOM   2904  C  CB  . GLU A  1 410 ? 45.084  7.516   1.169   1.00 46.61  ? 410  GLU A CB  1 
ATOM   2905  C  CG  . GLU A  1 410 ? 44.050  8.193   2.057   1.00 62.65  ? 410  GLU A CG  1 
ATOM   2906  C  CD  . GLU A  1 410 ? 43.659  9.603   1.592   1.00 73.03  ? 410  GLU A CD  1 
ATOM   2907  O  OE1 . GLU A  1 410 ? 43.646  9.868   0.367   1.00 69.86  ? 410  GLU A OE1 1 
ATOM   2908  O  OE2 . GLU A  1 410 ? 43.359  10.441  2.474   1.00 64.99  ? 410  GLU A OE2 1 
ATOM   2909  N  N   . LEU A  1 411 ? 42.306  5.634   0.678   1.00 51.28  ? 411  LEU A N   1 
ATOM   2910  C  CA  . LEU A  1 411 ? 41.391  4.665   1.282   1.00 45.65  ? 411  LEU A CA  1 
ATOM   2911  C  C   . LEU A  1 411 ? 41.274  3.377   0.478   1.00 44.80  ? 411  LEU A C   1 
ATOM   2912  O  O   . LEU A  1 411 ? 40.683  2.407   0.959   1.00 46.16  ? 411  LEU A O   1 
ATOM   2913  C  CB  . LEU A  1 411 ? 40.000  5.274   1.471   1.00 40.16  ? 411  LEU A CB  1 
ATOM   2914  C  CG  . LEU A  1 411 ? 39.948  6.329   2.565   1.00 40.70  ? 411  LEU A CG  1 
ATOM   2915  C  CD1 . LEU A  1 411 ? 38.518  6.768   2.810   1.00 38.81  ? 411  LEU A CD1 1 
ATOM   2916  C  CD2 . LEU A  1 411 ? 40.594  5.796   3.826   1.00 38.13  ? 411  LEU A CD2 1 
ATOM   2917  N  N   . GLN A  1 412 ? 41.812  3.378   -0.745  1.00 47.32  ? 412  GLN A N   1 
ATOM   2918  C  CA  . GLN A  1 412 ? 41.915  2.168   -1.569  1.00 41.86  ? 412  GLN A CA  1 
ATOM   2919  C  C   . GLN A  1 412 ? 40.574  1.560   -1.933  1.00 46.62  ? 412  GLN A C   1 
ATOM   2920  O  O   . GLN A  1 412 ? 40.488  0.338   -2.157  1.00 48.28  ? 412  GLN A O   1 
ATOM   2921  C  CB  . GLN A  1 412 ? 42.745  1.100   -0.851  1.00 51.89  ? 412  GLN A CB  1 
ATOM   2922  C  CG  . GLN A  1 412 ? 44.117  1.570   -0.426  1.00 53.15  ? 412  GLN A CG  1 
ATOM   2923  C  CD  . GLN A  1 412 ? 44.951  1.938   -1.621  1.00 61.81  ? 412  GLN A CD  1 
ATOM   2924  O  OE1 . GLN A  1 412 ? 45.402  1.065   -2.372  1.00 64.19  ? 412  GLN A OE1 1 
ATOM   2925  N  NE2 . GLN A  1 412 ? 45.138  3.242   -1.834  1.00 61.36  ? 412  GLN A NE2 1 
ATOM   2926  N  N   . PHE A  1 413 ? 39.532  2.388   -2.000  1.00 35.70  ? 413  PHE A N   1 
ATOM   2927  C  CA  . PHE A  1 413 ? 38.203  1.859   -2.223  1.00 42.66  ? 413  PHE A CA  1 
ATOM   2928  C  C   . PHE A  1 413 ? 38.089  1.169   -3.600  1.00 44.49  ? 413  PHE A C   1 
ATOM   2929  O  O   . PHE A  1 413 ? 37.250  0.288   -3.787  1.00 46.55  ? 413  PHE A O   1 
ATOM   2930  C  CB  . PHE A  1 413 ? 37.128  2.955   -2.050  1.00 39.62  ? 413  PHE A CB  1 
ATOM   2931  C  CG  . PHE A  1 413 ? 35.753  2.392   -1.824  1.00 51.19  ? 413  PHE A CG  1 
ATOM   2932  C  CD1 . PHE A  1 413 ? 35.555  1.376   -0.878  1.00 61.15  ? 413  PHE A CD1 1 
ATOM   2933  C  CD2 . PHE A  1 413 ? 34.672  2.807   -2.582  1.00 48.16  ? 413  PHE A CD2 1 
ATOM   2934  C  CE1 . PHE A  1 413 ? 34.287  0.804   -0.663  1.00 55.48  ? 413  PHE A CE1 1 
ATOM   2935  C  CE2 . PHE A  1 413 ? 33.395  2.232   -2.381  1.00 55.83  ? 413  PHE A CE2 1 
ATOM   2936  C  CZ  . PHE A  1 413 ? 33.210  1.233   -1.412  1.00 58.46  ? 413  PHE A CZ  1 
ATOM   2937  N  N   . ASP A  1 414 ? 38.948  1.539   -4.546  1.00 44.71  ? 414  ASP A N   1 
ATOM   2938  C  CA  . ASP A  1 414 ? 38.945  0.922   -5.878  1.00 40.84  ? 414  ASP A CA  1 
ATOM   2939  C  C   . ASP A  1 414 ? 39.358  -0.563  -5.820  1.00 49.70  ? 414  ASP A C   1 
ATOM   2940  O  O   . ASP A  1 414 ? 38.925  -1.382  -6.638  1.00 50.61  ? 414  ASP A O   1 
ATOM   2941  C  CB  . ASP A  1 414 ? 39.872  1.702   -6.829  1.00 36.13  ? 414  ASP A CB  1 
ATOM   2942  C  CG  . ASP A  1 414 ? 39.923  1.101   -8.237  1.00 51.65  ? 414  ASP A CG  1 
ATOM   2943  O  OD1 . ASP A  1 414 ? 38.995  1.357   -9.038  1.00 53.15  ? 414  ASP A OD1 1 
ATOM   2944  O  OD2 . ASP A  1 414 ? 40.890  0.361   -8.548  1.00 50.62  ? 414  ASP A OD2 1 
ATOM   2945  N  N   . ASP A  1 415 ? 40.189  -0.914  -4.847  1.00 49.58  ? 415  ASP A N   1 
ATOM   2946  C  CA  . ASP A  1 415 ? 40.595  -2.300  -4.693  1.00 49.72  ? 415  ASP A CA  1 
ATOM   2947  C  C   . ASP A  1 415 ? 39.546  -3.122  -3.960  1.00 54.02  ? 415  ASP A C   1 
ATOM   2948  O  O   . ASP A  1 415 ? 39.660  -4.341  -3.907  1.00 57.03  ? 415  ASP A O   1 
ATOM   2949  C  CB  . ASP A  1 415 ? 41.930  -2.392  -3.953  1.00 46.00  ? 415  ASP A CB  1 
ATOM   2950  C  CG  . ASP A  1 415 ? 43.103  -1.985  -4.819  1.00 54.00  ? 415  ASP A CG  1 
ATOM   2951  O  OD1 . ASP A  1 415 ? 43.045  -2.184  -6.051  1.00 49.10  ? 415  ASP A OD1 1 
ATOM   2952  O  OD2 . ASP A  1 415 ? 44.092  -1.462  -4.264  1.00 66.20  ? 415  ASP A OD2 1 
ATOM   2953  N  N   . TYR A  1 416 ? 38.543  -2.468  -3.379  1.00 48.22  ? 416  TYR A N   1 
ATOM   2954  C  CA  . TYR A  1 416 ? 37.531  -3.183  -2.611  1.00 51.29  ? 416  TYR A CA  1 
ATOM   2955  C  C   . TYR A  1 416 ? 36.318  -3.441  -3.486  1.00 52.19  ? 416  TYR A C   1 
ATOM   2956  O  O   . TYR A  1 416 ? 35.510  -4.322  -3.186  1.00 53.53  ? 416  TYR A O   1 
ATOM   2957  C  CB  . TYR A  1 416 ? 37.108  -2.402  -1.341  1.00 60.87  ? 416  TYR A CB  1 
ATOM   2958  C  CG  . TYR A  1 416 ? 35.993  -3.066  -0.513  1.00 72.42  ? 416  TYR A CG  1 
ATOM   2959  C  CD1 . TYR A  1 416 ? 34.632  -2.897  -0.838  1.00 72.37  ? 416  TYR A CD1 1 
ATOM   2960  C  CD2 . TYR A  1 416 ? 36.298  -3.861  0.598   1.00 80.17  ? 416  TYR A CD2 1 
ATOM   2961  C  CE1 . TYR A  1 416 ? 33.611  -3.523  -0.088  1.00 73.74  ? 416  TYR A CE1 1 
ATOM   2962  C  CE2 . TYR A  1 416 ? 35.284  -4.480  1.357   1.00 82.70  ? 416  TYR A CE2 1 
ATOM   2963  C  CZ  . TYR A  1 416 ? 33.947  -4.309  1.010   1.00 81.55  ? 416  TYR A CZ  1 
ATOM   2964  O  OH  . TYR A  1 416 ? 32.958  -4.928  1.759   1.00 84.38  ? 416  TYR A OH  1 
ATOM   2965  N  N   . PHE A  1 417 ? 36.185  -2.679  -4.564  1.00 37.72  ? 417  PHE A N   1 
ATOM   2966  C  CA  . PHE A  1 417 ? 34.932  -2.669  -5.301  1.00 35.94  ? 417  PHE A CA  1 
ATOM   2967  C  C   . PHE A  1 417 ? 34.474  -4.032  -5.871  1.00 37.98  ? 417  PHE A C   1 
ATOM   2968  O  O   . PHE A  1 417 ? 33.280  -4.326  -5.838  1.00 37.54  ? 417  PHE A O   1 
ATOM   2969  C  CB  . PHE A  1 417 ? 34.995  -1.651  -6.439  1.00 39.23  ? 417  PHE A CB  1 
ATOM   2970  C  CG  . PHE A  1 417 ? 33.698  -1.507  -7.165  1.00 35.76  ? 417  PHE A CG  1 
ATOM   2971  C  CD1 . PHE A  1 417 ? 32.599  -0.957  -6.531  1.00 35.42  ? 417  PHE A CD1 1 
ATOM   2972  C  CD2 . PHE A  1 417 ? 33.560  -1.971  -8.455  1.00 34.32  ? 417  PHE A CD2 1 
ATOM   2973  C  CE1 . PHE A  1 417 ? 31.395  -0.844  -7.186  1.00 36.92  ? 417  PHE A CE1 1 
ATOM   2974  C  CE2 . PHE A  1 417 ? 32.363  -1.861  -9.125  1.00 37.84  ? 417  PHE A CE2 1 
ATOM   2975  C  CZ  . PHE A  1 417 ? 31.275  -1.297  -8.489  1.00 41.32  ? 417  PHE A CZ  1 
ATOM   2976  N  N   . LEU A  1 418 ? 35.389  -4.861  -6.381  1.00 35.97  ? 418  LEU A N   1 
ATOM   2977  C  CA  . LEU A  1 418 ? 34.978  -6.160  -6.932  1.00 38.52  ? 418  LEU A CA  1 
ATOM   2978  C  C   . LEU A  1 418 ? 34.121  -6.977  -5.924  1.00 36.47  ? 418  LEU A C   1 
ATOM   2979  O  O   . LEU A  1 418 ? 33.274  -7.795  -6.330  1.00 33.62  ? 418  LEU A O   1 
ATOM   2980  C  CB  . LEU A  1 418 ? 36.195  -6.986  -7.385  1.00 35.14  ? 418  LEU A CB  1 
ATOM   2981  C  CG  . LEU A  1 418 ? 36.899  -6.535  -8.684  1.00 45.32  ? 418  LEU A CG  1 
ATOM   2982  C  CD1 . LEU A  1 418 ? 38.071  -7.435  -9.099  1.00 38.34  ? 418  LEU A CD1 1 
ATOM   2983  C  CD2 . LEU A  1 418 ? 35.926  -6.397  -9.842  1.00 38.44  ? 418  LEU A CD2 1 
ATOM   2984  N  N   . ASN A  1 419 ? 34.306  -6.717  -4.629  1.00 30.92  ? 419  ASN A N   1 
ATOM   2985  C  CA  . ASN A  1 419 ? 33.519  -7.393  -3.593  1.00 37.22  ? 419  ASN A CA  1 
ATOM   2986  C  C   . ASN A  1 419 ? 32.037  -7.079  -3.711  1.00 38.16  ? 419  ASN A C   1 
ATOM   2987  O  O   . ASN A  1 419 ? 31.215  -7.971  -3.515  1.00 36.05  ? 419  ASN A O   1 
ATOM   2988  C  CB  . ASN A  1 419 ? 34.011  -7.036  -2.189  1.00 43.15  ? 419  ASN A CB  1 
ATOM   2989  C  CG  . ASN A  1 419 ? 35.412  -7.569  -1.900  1.00 57.39  ? 419  ASN A CG  1 
ATOM   2990  O  OD1 . ASN A  1 419 ? 35.675  -8.766  -1.999  1.00 46.75  ? 419  ASN A OD1 1 
ATOM   2991  N  ND2 . ASN A  1 419 ? 36.319  -6.669  -1.539  1.00 70.17  ? 419  ASN A ND2 1 
ATOM   2992  N  N   . VAL A  1 420 ? 31.711  -5.824  -4.041  1.00 35.41  ? 420  VAL A N   1 
ATOM   2993  C  CA  . VAL A  1 420 ? 30.342  -5.421  -4.384  1.00 37.34  ? 420  VAL A CA  1 
ATOM   2994  C  C   . VAL A  1 420 ? 29.717  -6.395  -5.400  1.00 32.66  ? 420  VAL A C   1 
ATOM   2995  O  O   . VAL A  1 420 ? 28.590  -6.842  -5.241  1.00 29.32  ? 420  VAL A O   1 
ATOM   2996  C  CB  . VAL A  1 420 ? 30.302  -3.954  -4.960  1.00 36.63  ? 420  VAL A CB  1 
ATOM   2997  C  CG1 . VAL A  1 420 ? 28.891  -3.499  -5.252  1.00 27.98  ? 420  VAL A CG1 1 
ATOM   2998  C  CG2 . VAL A  1 420 ? 30.951  -2.985  -3.992  1.00 35.82  ? 420  VAL A CG2 1 
ATOM   2999  N  N   . CYS A  1 421 ? 30.481  -6.753  -6.420  1.00 34.81  ? 421  CYS A N   1 
ATOM   3000  C  CA  . CYS A  1 421 ? 29.964  -7.595  -7.493  1.00 28.19  ? 421  CYS A CA  1 
ATOM   3001  C  C   . CYS A  1 421 ? 29.914  -9.073  -7.099  1.00 33.27  ? 421  CYS A C   1 
ATOM   3002  O  O   . CYS A  1 421 ? 28.910  -9.757  -7.351  1.00 33.05  ? 421  CYS A O   1 
ATOM   3003  C  CB  . CYS A  1 421 ? 30.799  -7.341  -8.746  1.00 29.87  ? 421  CYS A CB  1 
ATOM   3004  S  SG  . CYS A  1 421 ? 30.940  -5.493  -9.073  1.00 41.55  ? 421  CYS A SG  1 
ATOM   3005  N  N   . PHE A  1 422 ? 30.956  -9.557  -6.430  1.00 30.54  ? 422  PHE A N   1 
ATOM   3006  C  CA  . PHE A  1 422 ? 30.968  -10.945 -5.973  1.00 29.98  ? 422  PHE A CA  1 
ATOM   3007  C  C   . PHE A  1 422 ? 29.812  -11.244 -5.001  1.00 36.35  ? 422  PHE A C   1 
ATOM   3008  O  O   . PHE A  1 422 ? 29.228  -12.338 -5.040  1.00 36.09  ? 422  PHE A O   1 
ATOM   3009  C  CB  . PHE A  1 422 ? 32.306  -11.290 -5.308  1.00 28.96  ? 422  PHE A CB  1 
ATOM   3010  C  CG  . PHE A  1 422 ? 33.511  -11.098 -6.207  1.00 33.97  ? 422  PHE A CG  1 
ATOM   3011  C  CD1 . PHE A  1 422 ? 33.391  -11.179 -7.595  1.00 28.82  ? 422  PHE A CD1 1 
ATOM   3012  C  CD2 . PHE A  1 422 ? 34.765  -10.830 -5.660  1.00 29.83  ? 422  PHE A CD2 1 
ATOM   3013  C  CE1 . PHE A  1 422 ? 34.489  -11.017 -8.421  1.00 26.21  ? 422  PHE A CE1 1 
ATOM   3014  C  CE2 . PHE A  1 422 ? 35.861  -10.654 -6.476  1.00 30.58  ? 422  PHE A CE2 1 
ATOM   3015  C  CZ  . PHE A  1 422 ? 35.721  -10.754 -7.864  1.00 32.85  ? 422  PHE A CZ  1 
ATOM   3016  N  N   . GLU A  1 423 ? 29.455  -10.284 -4.148  1.00 32.72  ? 423  GLU A N   1 
ATOM   3017  C  CA  . GLU A  1 423 ? 28.365  -10.530 -3.217  1.00 32.61  ? 423  GLU A CA  1 
ATOM   3018  C  C   . GLU A  1 423 ? 27.047  -10.719 -3.962  1.00 34.70  ? 423  GLU A C   1 
ATOM   3019  O  O   . GLU A  1 423 ? 26.274  -11.586 -3.581  1.00 41.51  ? 423  GLU A O   1 
ATOM   3020  C  CB  . GLU A  1 423 ? 28.216  -9.402  -2.200  1.00 36.13  ? 423  GLU A CB  1 
ATOM   3021  C  CG  . GLU A  1 423 ? 29.438  -9.098  -1.386  1.00 43.94  ? 423  GLU A CG  1 
ATOM   3022  C  CD  . GLU A  1 423 ? 29.442  -7.642  -0.895  1.00 57.34  ? 423  GLU A CD  1 
ATOM   3023  O  OE1 . GLU A  1 423 ? 28.379  -6.983  -1.018  1.00 58.13  ? 423  GLU A OE1 1 
ATOM   3024  O  OE2 . GLU A  1 423 ? 30.496  -7.156  -0.402  1.00 57.15  ? 423  GLU A OE2 1 
ATOM   3025  N  N   . VAL A  1 424 ? 26.778  -9.917  -4.995  1.00 27.17  ? 424  VAL A N   1 
ATOM   3026  C  CA  . VAL A  1 424 ? 25.569  -10.125 -5.798  1.00 36.95  ? 424  VAL A CA  1 
ATOM   3027  C  C   . VAL A  1 424 ? 25.564  -11.454 -6.502  1.00 35.63  ? 424  VAL A C   1 
ATOM   3028  O  O   . VAL A  1 424 ? 24.528  -12.097 -6.595  1.00 34.92  ? 424  VAL A O   1 
ATOM   3029  C  CB  . VAL A  1 424 ? 25.340  -9.107  -6.976  1.00 39.98  ? 424  VAL A CB  1 
ATOM   3030  C  CG1 . VAL A  1 424 ? 23.897  -8.632  -7.010  1.00 39.52  ? 424  VAL A CG1 1 
ATOM   3031  C  CG2 . VAL A  1 424 ? 26.317  -7.995  -7.006  1.00 35.00  ? 424  VAL A CG2 1 
ATOM   3032  N  N   . ILE A  1 425 ? 26.707  -11.810 -7.079  1.00 36.19  ? 425  ILE A N   1 
ATOM   3033  C  CA  . ILE A  1 425 ? 26.766  -12.996 -7.929  1.00 40.00  ? 425  ILE A CA  1 
ATOM   3034  C  C   . ILE A  1 425 ? 26.270  -14.227 -7.151  1.00 37.76  ? 425  ILE A C   1 
ATOM   3035  O  O   . ILE A  1 425 ? 25.582  -15.081 -7.705  1.00 39.67  ? 425  ILE A O   1 
ATOM   3036  C  CB  . ILE A  1 425 ? 28.174  -13.203 -8.490  1.00 30.45  ? 425  ILE A CB  1 
ATOM   3037  C  CG1 . ILE A  1 425 ? 28.403  -12.227 -9.637  1.00 37.10  ? 425  ILE A CG1 1 
ATOM   3038  C  CG2 . ILE A  1 425 ? 28.306  -14.571 -9.046  1.00 40.33  ? 425  ILE A CG2 1 
ATOM   3039  C  CD1 . ILE A  1 425 ? 29.830  -11.743 -9.771  1.00 38.27  ? 425  ILE A CD1 1 
ATOM   3040  N  N   . THR A  1 426 ? 26.553  -14.250 -5.852  1.00 32.73  ? 426  THR A N   1 
ATOM   3041  C  CA  . THR A  1 426 ? 26.006  -15.241 -4.940  1.00 36.45  ? 426  THR A CA  1 
ATOM   3042  C  C   . THR A  1 426 ? 24.500  -15.338 -5.073  1.00 39.90  ? 426  THR A C   1 
ATOM   3043  O  O   . THR A  1 426 ? 23.978  -16.428 -5.198  1.00 46.42  ? 426  THR A O   1 
ATOM   3044  C  CB  . THR A  1 426 ? 26.368  -14.903 -3.471  1.00 46.76  ? 426  THR A CB  1 
ATOM   3045  O  OG1 . THR A  1 426 ? 27.707  -15.322 -3.208  1.00 49.00  ? 426  THR A OG1 1 
ATOM   3046  C  CG2 . THR A  1 426 ? 25.436  -15.585 -2.482  1.00 41.45  ? 426  THR A CG2 1 
ATOM   3047  N  N   . LYS A  1 427 ? 23.806  -14.199 -5.044  1.00 43.46  ? 427  LYS A N   1 
ATOM   3048  C  CA  . LYS A  1 427 ? 22.354  -14.170 -5.230  1.00 41.36  ? 427  LYS A CA  1 
ATOM   3049  C  C   . LYS A  1 427 ? 21.945  -14.399 -6.679  1.00 40.06  ? 427  LYS A C   1 
ATOM   3050  O  O   . LYS A  1 427 ? 20.921  -15.024 -6.950  1.00 43.61  ? 427  LYS A O   1 
ATOM   3051  C  CB  . LYS A  1 427 ? 21.759  -12.827 -4.773  1.00 42.91  ? 427  LYS A CB  1 
ATOM   3052  C  CG  . LYS A  1 427 ? 22.087  -12.412 -3.349  1.00 43.31  ? 427  LYS A CG  1 
ATOM   3053  C  CD  . LYS A  1 427 ? 21.014  -12.784 -2.367  1.00 44.34  ? 427  LYS A CD  1 
ATOM   3054  C  CE  . LYS A  1 427 ? 21.417  -12.319 -0.964  1.00 55.40  ? 427  LYS A CE  1 
ATOM   3055  N  NZ  . LYS A  1 427 ? 22.874  -12.578 -0.697  1.00 54.45  ? 427  LYS A NZ  1 
ATOM   3056  N  N   . ASP A  1 428 ? 22.735  -13.875 -7.605  1.00 37.14  ? 428  ASP A N   1 
ATOM   3057  C  CA  . ASP A  1 428 ? 22.310  -13.767 -8.994  1.00 38.96  ? 428  ASP A CA  1 
ATOM   3058  C  C   . ASP A  1 428 ? 22.476  -15.110 -9.747  1.00 39.49  ? 428  ASP A C   1 
ATOM   3059  O  O   . ASP A  1 428 ? 21.823  -15.372 -10.757 1.00 39.92  ? 428  ASP A O   1 
ATOM   3060  C  CB  . ASP A  1 428 ? 23.093  -12.632 -9.674  1.00 38.60  ? 428  ASP A CB  1 
ATOM   3061  C  CG  . ASP A  1 428 ? 22.227  -11.774 -10.604 1.00 38.44  ? 428  ASP A CG  1 
ATOM   3062  O  OD1 . ASP A  1 428 ? 20.983  -11.750 -10.482 1.00 39.53  ? 428  ASP A OD1 1 
ATOM   3063  O  OD2 . ASP A  1 428 ? 22.808  -11.105 -11.471 1.00 38.74  ? 428  ASP A OD2 1 
ATOM   3064  N  N   . SER A  1 429 ? 23.325  -15.975 -9.222  1.00 37.53  ? 429  SER A N   1 
ATOM   3065  C  CA  . SER A  1 429 ? 23.475  -17.298 -9.781  1.00 40.28  ? 429  SER A CA  1 
ATOM   3066  C  C   . SER A  1 429 ? 22.539  -18.352 -9.155  1.00 43.81  ? 429  SER A C   1 
ATOM   3067  O  O   . SER A  1 429 ? 22.734  -19.547 -9.362  1.00 41.93  ? 429  SER A O   1 
ATOM   3068  C  CB  . SER A  1 429 ? 24.923  -17.738 -9.631  1.00 42.78  ? 429  SER A CB  1 
ATOM   3069  O  OG  . SER A  1 429 ? 25.325  -17.662 -8.284  1.00 38.37  ? 429  SER A OG  1 
ATOM   3070  N  N   . LEU A  1 430 ? 21.537  -17.910 -8.396  1.00 35.64  ? 430  LEU A N   1 
ATOM   3071  C  CA  . LEU A  1 430 ? 20.446  -18.787 -7.953  1.00 39.07  ? 430  LEU A CA  1 
ATOM   3072  C  C   . LEU A  1 430 ? 19.152  -18.368 -8.614  1.00 45.80  ? 430  LEU A C   1 
ATOM   3073  O  O   . LEU A  1 430 ? 18.932  -17.181 -8.804  1.00 49.04  ? 430  LEU A O   1 
ATOM   3074  C  CB  . LEU A  1 430 ? 20.267  -18.748 -6.440  1.00 34.76  ? 430  LEU A CB  1 
ATOM   3075  C  CG  . LEU A  1 430 ? 21.550  -18.939 -5.653  1.00 39.05  ? 430  LEU A CG  1 
ATOM   3076  C  CD1 . LEU A  1 430 ? 21.278  -18.821 -4.170  1.00 38.76  ? 430  LEU A CD1 1 
ATOM   3077  C  CD2 . LEU A  1 430 ? 22.141  -20.286 -6.004  1.00 48.11  ? 430  LEU A CD2 1 
ATOM   3078  N  N   . ASN A  1 431 ? 18.291  -19.330 -8.940  1.00 41.89  ? 431  ASN A N   1 
ATOM   3079  C  CA  . ASN A  1 431 ? 17.060  -19.050 -9.675  1.00 43.12  ? 431  ASN A CA  1 
ATOM   3080  C  C   . ASN A  1 431 ? 16.177  -17.991 -9.049  1.00 48.33  ? 431  ASN A C   1 
ATOM   3081  O  O   . ASN A  1 431 ? 15.506  -17.244 -9.741  1.00 53.56  ? 431  ASN A O   1 
ATOM   3082  C  CB  . ASN A  1 431 ? 16.217  -20.315 -9.831  1.00 59.53  ? 431  ASN A CB  1 
ATOM   3083  C  CG  . ASN A  1 431 ? 15.069  -20.123 -10.825 1.00 64.96  ? 431  ASN A CG  1 
ATOM   3084  O  OD1 . ASN A  1 431 ? 15.133  -19.259 -11.699 1.00 51.25  ? 431  ASN A OD1 1 
ATOM   3085  N  ND2 . ASN A  1 431 ? 14.021  -20.922 -10.692 1.00 76.05  ? 431  ASN A ND2 1 
ATOM   3086  N  N   . SER A  1 432 ? 16.162  -17.946 -7.730  1.00 46.99  ? 432  SER A N   1 
ATOM   3087  C  CA  . SER A  1 432 ? 15.270  -17.070 -7.005  1.00 41.41  ? 432  SER A CA  1 
ATOM   3088  C  C   . SER A  1 432 ? 15.665  -15.586 -7.063  1.00 47.00  ? 432  SER A C   1 
ATOM   3089  O  O   . SER A  1 432 ? 15.078  -14.757 -6.375  1.00 52.90  ? 432  SER A O   1 
ATOM   3090  C  CB  . SER A  1 432 ? 15.215  -17.526 -5.559  1.00 44.34  ? 432  SER A CB  1 
ATOM   3091  O  OG  . SER A  1 432 ? 16.496  -17.958 -5.138  1.00 41.47  ? 432  SER A OG  1 
ATOM   3092  N  N   . SER A  1 433 ? 16.664  -15.251 -7.868  1.00 41.70  ? 433  SER A N   1 
ATOM   3093  C  CA  . SER A  1 433 ? 17.035  -13.860 -8.068  1.00 48.16  ? 433  SER A CA  1 
ATOM   3094  C  C   . SER A  1 433 ? 15.961  -13.104 -8.871  1.00 51.11  ? 433  SER A C   1 
ATOM   3095  O  O   . SER A  1 433 ? 14.985  -13.688 -9.342  1.00 50.58  ? 433  SER A O   1 
ATOM   3096  C  CB  . SER A  1 433 ? 18.390  -13.773 -8.775  1.00 48.92  ? 433  SER A CB  1 
ATOM   3097  O  OG  . SER A  1 433 ? 18.875  -12.447 -8.785  1.00 46.95  ? 433  SER A OG  1 
ATOM   3098  N  N   . ARG A  1 434 ? 16.148  -11.800 -9.024  1.00 46.33  ? 434  ARG A N   1 
ATOM   3099  C  CA  . ARG A  1 434 ? 15.177  -10.978 -9.734  1.00 43.47  ? 434  ARG A CA  1 
ATOM   3100  C  C   . ARG A  1 434 ? 15.897  -10.072 -10.730 1.00 40.01  ? 434  ARG A C   1 
ATOM   3101  O  O   . ARG A  1 434 ? 17.098  -9.829  -10.595 1.00 36.60  ? 434  ARG A O   1 
ATOM   3102  C  CB  . ARG A  1 434 ? 14.345  -10.162 -8.734  1.00 41.06  ? 434  ARG A CB  1 
ATOM   3103  C  CG  . ARG A  1 434 ? 15.172  -9.285  -7.762  1.00 39.76  ? 434  ARG A CG  1 
ATOM   3104  C  CD  . ARG A  1 434 ? 14.298  -8.216  -7.104  1.00 42.87  ? 434  ARG A CD  1 
ATOM   3105  N  NE  . ARG A  1 434 ? 15.055  -7.141  -6.458  1.00 35.60  ? 434  ARG A NE  1 
ATOM   3106  C  CZ  . ARG A  1 434 ? 15.357  -5.982  -7.041  1.00 43.15  ? 434  ARG A CZ  1 
ATOM   3107  N  NH1 . ARG A  1 434 ? 14.989  -5.738  -8.297  1.00 36.61  ? 434  ARG A NH1 1 
ATOM   3108  N  NH2 . ARG A  1 434 ? 16.044  -5.064  -6.370  1.00 40.66  ? 434  ARG A NH2 1 
ATOM   3109  N  N   . PRO A  1 435 ? 15.185  -9.610  -11.769 1.00 45.10  ? 435  PRO A N   1 
ATOM   3110  C  CA  . PRO A  1 435 ? 15.721  -8.553  -12.640 1.00 38.56  ? 435  PRO A CA  1 
ATOM   3111  C  C   . PRO A  1 435 ? 15.974  -7.283  -11.816 1.00 39.87  ? 435  PRO A C   1 
ATOM   3112  O  O   . PRO A  1 435 ? 15.275  -7.103  -10.814 1.00 37.79  ? 435  PRO A O   1 
ATOM   3113  C  CB  . PRO A  1 435 ? 14.597  -8.321  -13.651 1.00 37.51  ? 435  PRO A CB  1 
ATOM   3114  C  CG  . PRO A  1 435 ? 13.717  -9.513  -13.564 1.00 32.27  ? 435  PRO A CG  1 
ATOM   3115  C  CD  . PRO A  1 435 ? 13.868  -10.095 -12.214 1.00 42.09  ? 435  PRO A CD  1 
ATOM   3116  N  N   . ILE A  1 436 ? 16.929  -6.441  -12.216 1.00 34.21  ? 436  ILE A N   1 
ATOM   3117  C  CA  . ILE A  1 436 ? 17.174  -5.170  -11.542 1.00 38.68  ? 436  ILE A CA  1 
ATOM   3118  C  C   . ILE A  1 436 ? 15.914  -4.316  -11.448 1.00 36.40  ? 436  ILE A C   1 
ATOM   3119  O  O   . ILE A  1 436 ? 15.506  -3.904  -10.377 1.00 34.42  ? 436  ILE A O   1 
ATOM   3120  C  CB  . ILE A  1 436 ? 18.246  -4.347  -12.249 1.00 41.24  ? 436  ILE A CB  1 
ATOM   3121  C  CG1 . ILE A  1 436 ? 19.610  -5.020  -12.108 1.00 41.89  ? 436  ILE A CG1 1 
ATOM   3122  C  CG2 . ILE A  1 436 ? 18.303  -2.943  -11.648 1.00 39.89  ? 436  ILE A CG2 1 
ATOM   3123  C  CD1 . ILE A  1 436 ? 20.778  -4.080  -12.399 1.00 42.56  ? 436  ILE A CD1 1 
ATOM   3124  N  N   . SER A  1 437 ? 15.308  -4.043  -12.585 1.00 40.93  ? 437  SER A N   1 
ATOM   3125  C  CA  . SER A  1 437 ? 14.042  -3.352  -12.589 1.00 39.95  ? 437  SER A CA  1 
ATOM   3126  C  C   . SER A  1 437 ? 12.919  -4.397  -12.606 1.00 41.16  ? 437  SER A C   1 
ATOM   3127  O  O   . SER A  1 437 ? 12.969  -5.356  -13.373 1.00 44.96  ? 437  SER A O   1 
ATOM   3128  C  CB  . SER A  1 437 ? 13.963  -2.407  -13.780 1.00 36.76  ? 437  SER A CB  1 
ATOM   3129  O  OG  . SER A  1 437 ? 12.821  -1.575  -13.679 1.00 45.94  ? 437  SER A OG  1 
ATOM   3130  N  N   . LYS A  1 438 ? 11.920  -4.221  -11.750 1.00 39.24  ? 438  LYS A N   1 
ATOM   3131  C  CA  . LYS A  1 438 ? 10.901  -5.246  -11.529 1.00 38.23  ? 438  LYS A CA  1 
ATOM   3132  C  C   . LYS A  1 438 ? 9.689   -4.637  -10.809 1.00 40.11  ? 438  LYS A C   1 
ATOM   3133  O  O   . LYS A  1 438 ? 9.851   -3.779  -9.951  1.00 36.46  ? 438  LYS A O   1 
ATOM   3134  C  CB  . LYS A  1 438 ? 11.504  -6.392  -10.714 1.00 38.90  ? 438  LYS A CB  1 
ATOM   3135  C  CG  . LYS A  1 438 ? 10.512  -7.424  -10.258 1.00 44.57  ? 438  LYS A CG  1 
ATOM   3136  C  CD  . LYS A  1 438 ? 10.987  -8.150  -9.022  1.00 45.48  ? 438  LYS A CD  1 
ATOM   3137  C  CE  . LYS A  1 438 ? 10.120  -7.783  -7.802  1.00 57.44  ? 438  LYS A CE  1 
ATOM   3138  N  NZ  . LYS A  1 438 ? 10.332  -8.671  -6.602  1.00 59.84  ? 438  LYS A NZ  1 
ATOM   3139  N  N   . PRO A  1 439 ? 8.469   -5.058  -11.169 1.00 47.57  ? 439  PRO A N   1 
ATOM   3140  C  CA  . PRO A  1 439 ? 7.256   -4.527  -10.526 1.00 43.69  ? 439  PRO A CA  1 
ATOM   3141  C  C   . PRO A  1 439 ? 7.257   -4.620  -9.009  1.00 42.36  ? 439  PRO A C   1 
ATOM   3142  O  O   . PRO A  1 439 ? 7.903   -5.501  -8.445  1.00 47.77  ? 439  PRO A O   1 
ATOM   3143  C  CB  . PRO A  1 439 ? 6.148   -5.413  -11.102 1.00 40.51  ? 439  PRO A CB  1 
ATOM   3144  C  CG  . PRO A  1 439 ? 6.644   -5.734  -12.476 1.00 37.80  ? 439  PRO A CG  1 
ATOM   3145  C  CD  . PRO A  1 439 ? 8.142   -5.919  -12.319 1.00 44.37  ? 439  PRO A CD  1 
ATOM   3146  N  N   . ALA A  1 440 ? 6.529   -3.716  -8.360  1.00 44.75  ? 440  ALA A N   1 
ATOM   3147  C  CA  . ALA A  1 440 ? 6.371   -3.726  -6.908  1.00 38.15  ? 440  ALA A CA  1 
ATOM   3148  C  C   . ALA A  1 440 ? 5.188   -2.864  -6.523  1.00 40.39  ? 440  ALA A C   1 
ATOM   3149  O  O   . ALA A  1 440 ? 4.976   -1.804  -7.104  1.00 40.95  ? 440  ALA A O   1 
ATOM   3150  C  CB  . ALA A  1 440 ? 7.632   -3.239  -6.227  1.00 36.96  ? 440  ALA A CB  1 
ATOM   3151  N  N   . GLU A  1 441 ? 4.417   -3.314  -5.546  1.00 39.62  ? 441  GLU A N   1 
ATOM   3152  C  CA  . GLU A  1 441 ? 3.161   -2.652  -5.236  1.00 45.85  ? 441  GLU A CA  1 
ATOM   3153  C  C   . GLU A  1 441 ? 2.948   -2.410  -3.750  1.00 45.16  ? 441  GLU A C   1 
ATOM   3154  O  O   . GLU A  1 441 ? 2.620   -1.308  -3.348  1.00 44.17  ? 441  GLU A O   1 
ATOM   3155  C  CB  . GLU A  1 441 ? 1.980   -3.470  -5.756  1.00 50.30  ? 441  GLU A CB  1 
ATOM   3156  C  CG  . GLU A  1 441 ? 1.673   -3.351  -7.219  1.00 51.07  ? 441  GLU A CG  1 
ATOM   3157  C  CD  . GLU A  1 441 ? 0.316   -3.970  -7.542  1.00 72.60  ? 441  GLU A CD  1 
ATOM   3158  O  OE1 . GLU A  1 441 ? -0.719  -3.318  -7.256  1.00 70.63  ? 441  GLU A OE1 1 
ATOM   3159  O  OE2 . GLU A  1 441 ? 0.282   -5.114  -8.060  1.00 82.78  ? 441  GLU A OE2 1 
ATOM   3160  N  N   . THR A  1 442 ? 3.089   -3.444  -2.935  1.00 42.26  ? 442  THR A N   1 
ATOM   3161  C  CA  . THR A  1 442 ? 2.768   -3.292  -1.517  1.00 43.58  ? 442  THR A CA  1 
ATOM   3162  C  C   . THR A  1 442 ? 3.949   -2.670  -0.801  1.00 43.64  ? 442  THR A C   1 
ATOM   3163  O  O   . THR A  1 442 ? 5.064   -2.645  -1.338  1.00 41.44  ? 442  THR A O   1 
ATOM   3164  C  CB  . THR A  1 442 ? 2.400   -4.645  -0.850  1.00 48.70  ? 442  THR A CB  1 
ATOM   3165  O  OG1 . THR A  1 442 ? 3.550   -5.499  -0.830  1.00 49.84  ? 442  THR A OG1 1 
ATOM   3166  C  CG2 . THR A  1 442 ? 1.254   -5.331  -1.612  1.00 43.02  ? 442  THR A CG2 1 
ATOM   3167  N  N   . PRO A  1 443 ? 3.707   -2.119  0.395   1.00 43.80  ? 443  PRO A N   1 
ATOM   3168  C  CA  . PRO A  1 443 ? 4.844   -1.564  1.128   1.00 41.81  ? 443  PRO A CA  1 
ATOM   3169  C  C   . PRO A  1 443 ? 5.916   -2.621  1.364   1.00 40.45  ? 443  PRO A C   1 
ATOM   3170  O  O   . PRO A  1 443 ? 7.104   -2.327  1.205   1.00 42.02  ? 443  PRO A O   1 
ATOM   3171  C  CB  . PRO A  1 443 ? 4.205   -1.082  2.419   1.00 41.20  ? 443  PRO A CB  1 
ATOM   3172  C  CG  . PRO A  1 443 ? 2.831   -0.672  1.970   1.00 38.23  ? 443  PRO A CG  1 
ATOM   3173  C  CD  . PRO A  1 443 ? 2.423   -1.721  0.996   1.00 39.56  ? 443  PRO A CD  1 
ATOM   3174  N  N   . THR A  1 444 ? 5.509   -3.849  1.660   1.00 42.09  ? 444  THR A N   1 
ATOM   3175  C  CA  . THR A  1 444 ? 6.483   -4.930  1.819   1.00 42.09  ? 444  THR A CA  1 
ATOM   3176  C  C   . THR A  1 444 ? 7.211   -5.248  0.527   1.00 36.20  ? 444  THR A C   1 
ATOM   3177  O  O   . THR A  1 444 ? 8.417   -5.469  0.527   1.00 38.72  ? 444  THR A O   1 
ATOM   3178  C  CB  . THR A  1 444 ? 5.842   -6.208  2.340   1.00 39.07  ? 444  THR A CB  1 
ATOM   3179  O  OG1 . THR A  1 444 ? 5.192   -5.923  3.590   1.00 41.25  ? 444  THR A OG1 1 
ATOM   3180  C  CG2 . THR A  1 444 ? 6.919   -7.260  2.565   1.00 34.93  ? 444  THR A CG2 1 
ATOM   3181  N  N   . GLN A  1 445 ? 6.496   -5.258  -0.582  1.00 35.76  ? 445  GLN A N   1 
ATOM   3182  C  CA  . GLN A  1 445 ? 7.159   -5.503  -1.855  1.00 38.63  ? 445  GLN A CA  1 
ATOM   3183  C  C   . GLN A  1 445 ? 8.166   -4.412  -2.143  1.00 37.96  ? 445  GLN A C   1 
ATOM   3184  O  O   . GLN A  1 445 ? 9.258   -4.676  -2.639  1.00 37.12  ? 445  GLN A O   1 
ATOM   3185  C  CB  . GLN A  1 445 ? 6.149   -5.593  -2.985  1.00 41.69  ? 445  GLN A CB  1 
ATOM   3186  C  CG  . GLN A  1 445 ? 5.445   -6.920  -3.054  1.00 40.34  ? 445  GLN A CG  1 
ATOM   3187  C  CD  . GLN A  1 445 ? 4.169   -6.841  -3.857  1.00 46.32  ? 445  GLN A CD  1 
ATOM   3188  O  OE1 . GLN A  1 445 ? 3.957   -5.902  -4.623  1.00 47.05  ? 445  GLN A OE1 1 
ATOM   3189  N  NE2 . GLN A  1 445 ? 3.303   -7.823  -3.678  1.00 48.63  ? 445  GLN A NE2 1 
ATOM   3190  N  N   . ILE A  1 446 ? 7.791   -3.182  -1.807  1.00 43.00  ? 446  ILE A N   1 
ATOM   3191  C  CA  . ILE A  1 446 ? 8.633   -2.037  -2.086  1.00 43.09  ? 446  ILE A CA  1 
ATOM   3192  C  C   . ILE A  1 446 ? 9.877   -2.123  -1.227  1.00 33.39  ? 446  ILE A C   1 
ATOM   3193  O  O   . ILE A  1 446 ? 10.968  -1.879  -1.697  1.00 34.45  ? 446  ILE A O   1 
ATOM   3194  C  CB  . ILE A  1 446 ? 7.889   -0.707  -1.851  1.00 40.34  ? 446  ILE A CB  1 
ATOM   3195  C  CG1 . ILE A  1 446 ? 6.834   -0.517  -2.936  1.00 39.58  ? 446  ILE A CG1 1 
ATOM   3196  C  CG2 . ILE A  1 446 ? 8.838   0.444   -1.966  1.00 29.94  ? 446  ILE A CG2 1 
ATOM   3197  C  CD1 . ILE A  1 446 ? 5.738   0.404   -2.527  1.00 41.88  ? 446  ILE A CD1 1 
ATOM   3198  N  N   . GLN A  1 447 ? 9.720   -2.499  0.027   1.00 37.90  ? 447  GLN A N   1 
ATOM   3199  C  CA  . GLN A  1 447 ? 10.884  -2.723  0.873   1.00 36.12  ? 447  GLN A CA  1 
ATOM   3200  C  C   . GLN A  1 447 ? 11.810  -3.803  0.309   1.00 34.95  ? 447  GLN A C   1 
ATOM   3201  O  O   . GLN A  1 447 ? 13.035  -3.679  0.338   1.00 34.65  ? 447  GLN A O   1 
ATOM   3202  C  CB  . GLN A  1 447 ? 10.430  -3.075  2.272   1.00 40.74  ? 447  GLN A CB  1 
ATOM   3203  C  CG  . GLN A  1 447 ? 10.375  -1.842  3.153   1.00 41.05  ? 447  GLN A CG  1 
ATOM   3204  C  CD  . GLN A  1 447 ? 9.429   -2.009  4.296   1.00 47.97  ? 447  GLN A CD  1 
ATOM   3205  O  OE1 . GLN A  1 447 ? 8.669   -2.978  4.342   1.00 53.94  ? 447  GLN A OE1 1 
ATOM   3206  N  NE2 . GLN A  1 447 ? 9.447   -1.063  5.227   1.00 48.58  ? 447  GLN A NE2 1 
ATOM   3207  N  N   . GLU A  1 448 ? 11.225  -4.836  -0.265  1.00 33.23  ? 448  GLU A N   1 
ATOM   3208  C  CA  . GLU A  1 448 ? 12.024  -5.917  -0.781  1.00 35.91  ? 448  GLU A CA  1 
ATOM   3209  C  C   . GLU A  1 448 ? 12.910  -5.459  -1.944  1.00 40.21  ? 448  GLU A C   1 
ATOM   3210  O  O   . GLU A  1 448 ? 13.961  -6.063  -2.196  1.00 42.97  ? 448  GLU A O   1 
ATOM   3211  C  CB  . GLU A  1 448 ? 11.119  -7.071  -1.193  1.00 39.21  ? 448  GLU A CB  1 
ATOM   3212  C  CG  . GLU A  1 448 ? 10.509  -7.814  -0.022  1.00 42.21  ? 448  GLU A CG  1 
ATOM   3213  C  CD  . GLU A  1 448 ? 9.824   -9.117  -0.442  1.00 51.42  ? 448  GLU A CD  1 
ATOM   3214  O  OE1 . GLU A  1 448 ? 10.525  -10.146 -0.583  1.00 44.99  ? 448  GLU A OE1 1 
ATOM   3215  O  OE2 . GLU A  1 448 ? 8.583   -9.106  -0.635  1.00 52.12  ? 448  GLU A OE2 1 
ATOM   3216  N  N   . MET A  1 449 ? 12.523  -4.387  -2.634  1.00 37.77  ? 449  MET A N   1 
ATOM   3217  C  CA  . MET A  1 449 ? 13.337  -3.888  -3.756  1.00 34.49  ? 449  MET A CA  1 
ATOM   3218  C  C   . MET A  1 449 ? 14.675  -3.359  -3.285  1.00 32.56  ? 449  MET A C   1 
ATOM   3219  O  O   . MET A  1 449 ? 15.594  -3.215  -4.066  1.00 36.00  ? 449  MET A O   1 
ATOM   3220  C  CB  . MET A  1 449 ? 12.607  -2.794  -4.528  1.00 33.53  ? 449  MET A CB  1 
ATOM   3221  C  CG  . MET A  1 449 ? 11.313  -3.268  -5.164  1.00 38.11  ? 449  MET A CG  1 
ATOM   3222  S  SD  . MET A  1 449 ? 11.635  -4.415  -6.515  1.00 42.98  ? 449  MET A SD  1 
ATOM   3223  C  CE  . MET A  1 449 ? 12.617  -3.434  -7.646  1.00 30.61  ? 449  MET A CE  1 
ATOM   3224  N  N   . PHE A  1 450 ? 14.784  -3.062  -2.002  1.00 32.37  ? 450  PHE A N   1 
ATOM   3225  C  CA  . PHE A  1 450 ? 16.028  -2.532  -1.483  1.00 36.73  ? 450  PHE A CA  1 
ATOM   3226  C  C   . PHE A  1 450 ? 16.920  -3.707  -1.142  1.00 33.99  ? 450  PHE A C   1 
ATOM   3227  O  O   . PHE A  1 450 ? 16.879  -4.238  -0.035  1.00 37.03  ? 450  PHE A O   1 
ATOM   3228  C  CB  . PHE A  1 450 ? 15.788  -1.632  -0.250  1.00 37.36  ? 450  PHE A CB  1 
ATOM   3229  C  CG  . PHE A  1 450 ? 15.127  -0.313  -0.568  1.00 33.57  ? 450  PHE A CG  1 
ATOM   3230  C  CD1 . PHE A  1 450 ? 13.763  -0.227  -0.765  1.00 32.52  ? 450  PHE A CD1 1 
ATOM   3231  C  CD2 . PHE A  1 450 ? 15.872  0.848   -0.636  1.00 35.36  ? 450  PHE A CD2 1 
ATOM   3232  C  CE1 . PHE A  1 450 ? 13.154  0.993   -1.023  1.00 27.52  ? 450  PHE A CE1 1 
ATOM   3233  C  CE2 . PHE A  1 450 ? 15.272  2.077   -0.915  1.00 29.95  ? 450  PHE A CE2 1 
ATOM   3234  C  CZ  . PHE A  1 450 ? 13.915  2.143   -1.112  1.00 26.35  ? 450  PHE A CZ  1 
ATOM   3235  N  N   . ASP A  1 451 ? 17.716  -4.133  -2.108  1.00 35.36  ? 451  ASP A N   1 
ATOM   3236  C  CA  . ASP A  1 451 ? 18.550  -5.306  -1.907  1.00 34.16  ? 451  ASP A CA  1 
ATOM   3237  C  C   . ASP A  1 451 ? 19.802  -5.239  -2.765  1.00 33.62  ? 451  ASP A C   1 
ATOM   3238  O  O   . ASP A  1 451 ? 20.057  -4.229  -3.432  1.00 31.91  ? 451  ASP A O   1 
ATOM   3239  C  CB  . ASP A  1 451 ? 17.764  -6.598  -2.196  1.00 39.86  ? 451  ASP A CB  1 
ATOM   3240  C  CG  . ASP A  1 451 ? 17.280  -6.704  -3.650  1.00 41.33  ? 451  ASP A CG  1 
ATOM   3241  O  OD1 . ASP A  1 451 ? 17.851  -6.041  -4.541  1.00 37.46  ? 451  ASP A OD1 1 
ATOM   3242  O  OD2 . ASP A  1 451 ? 16.327  -7.479  -3.904  1.00 48.15  ? 451  ASP A OD2 1 
ATOM   3243  N  N   . GLU A  1 452 ? 20.565  -6.331  -2.728  1.00 32.25  ? 452  GLU A N   1 
ATOM   3244  C  CA  . GLU A  1 452 ? 21.855  -6.448  -3.384  1.00 31.25  ? 452  GLU A CA  1 
ATOM   3245  C  C   . GLU A  1 452 ? 21.711  -6.309  -4.898  1.00 31.47  ? 452  GLU A C   1 
ATOM   3246  O  O   . GLU A  1 452 ? 22.644  -5.918  -5.599  1.00 32.85  ? 452  GLU A O   1 
ATOM   3247  C  CB  . GLU A  1 452 ? 22.508  -7.779  -3.032  1.00 36.50  ? 452  GLU A CB  1 
ATOM   3248  C  CG  . GLU A  1 452 ? 22.934  -7.927  -1.571  1.00 42.39  ? 452  GLU A CG  1 
ATOM   3249  C  CD  . GLU A  1 452 ? 21.742  -8.055  -0.599  1.00 67.93  ? 452  GLU A CD  1 
ATOM   3250  O  OE1 . GLU A  1 452 ? 20.722  -8.693  -0.983  1.00 53.25  ? 452  GLU A OE1 1 
ATOM   3251  O  OE2 . GLU A  1 452 ? 21.820  -7.508  0.543   1.00 67.22  ? 452  GLU A OE2 1 
ATOM   3252  N  N   . VAL A  1 453 ? 20.524  -6.579  -5.400  1.00 25.38  ? 453  VAL A N   1 
ATOM   3253  C  CA  . VAL A  1 453 ? 20.304  -6.469  -6.824  1.00 30.31  ? 453  VAL A CA  1 
ATOM   3254  C  C   . VAL A  1 453 ? 20.095  -5.014  -7.235  1.00 33.99  ? 453  VAL A C   1 
ATOM   3255  O  O   . VAL A  1 453 ? 20.684  -4.543  -8.227  1.00 36.26  ? 453  VAL A O   1 
ATOM   3256  C  CB  . VAL A  1 453 ? 19.119  -7.341  -7.271  1.00 32.78  ? 453  VAL A CB  1 
ATOM   3257  C  CG1 . VAL A  1 453 ? 18.679  -6.975  -8.658  1.00 31.83  ? 453  VAL A CG1 1 
ATOM   3258  C  CG2 . VAL A  1 453 ? 19.535  -8.817  -7.231  1.00 32.91  ? 453  VAL A CG2 1 
ATOM   3259  N  N   . SER A  1 454 ? 19.289  -4.284  -6.479  1.00 28.21  ? 454  SER A N   1 
ATOM   3260  C  CA  . SER A  1 454 ? 19.134  -2.855  -6.746  1.00 29.72  ? 454  SER A CA  1 
ATOM   3261  C  C   . SER A  1 454 ? 20.405  -2.065  -6.473  1.00 33.56  ? 454  SER A C   1 
ATOM   3262  O  O   . SER A  1 454 ? 20.678  -1.092  -7.169  1.00 33.22  ? 454  SER A O   1 
ATOM   3263  C  CB  . SER A  1 454 ? 17.999  -2.267  -5.920  1.00 30.64  ? 454  SER A CB  1 
ATOM   3264  O  OG  . SER A  1 454 ? 16.762  -2.617  -6.494  1.00 32.81  ? 454  SER A OG  1 
ATOM   3265  N  N   . TYR A  1 455 ? 21.154  -2.442  -5.437  1.00 32.97  ? 455  TYR A N   1 
ATOM   3266  C  CA  . TYR A  1 455 ? 22.362  -1.700  -5.077  1.00 31.03  ? 455  TYR A CA  1 
ATOM   3267  C  C   . TYR A  1 455 ? 23.582  -2.245  -5.842  1.00 32.71  ? 455  TYR A C   1 
ATOM   3268  O  O   . TYR A  1 455 ? 24.089  -1.595  -6.745  1.00 28.74  ? 455  TYR A O   1 
ATOM   3269  C  CB  . TYR A  1 455 ? 22.625  -1.766  -3.568  1.00 32.01  ? 455  TYR A CB  1 
ATOM   3270  C  CG  . TYR A  1 455 ? 21.722  -0.950  -2.646  1.00 30.80  ? 455  TYR A CG  1 
ATOM   3271  C  CD1 . TYR A  1 455 ? 20.388  -1.277  -2.457  1.00 28.47  ? 455  TYR A CD1 1 
ATOM   3272  C  CD2 . TYR A  1 455 ? 22.233  0.126   -1.931  1.00 32.84  ? 455  TYR A CD2 1 
ATOM   3273  C  CE1 . TYR A  1 455 ? 19.582  -0.537  -1.609  1.00 28.41  ? 455  TYR A CE1 1 
ATOM   3274  C  CE2 . TYR A  1 455 ? 21.443  0.869   -1.081  1.00 31.68  ? 455  TYR A CE2 1 
ATOM   3275  C  CZ  . TYR A  1 455 ? 20.121  0.533   -0.915  1.00 32.59  ? 455  TYR A CZ  1 
ATOM   3276  O  OH  . TYR A  1 455 ? 19.352  1.291   -0.059  1.00 31.41  ? 455  TYR A OH  1 
ATOM   3277  N  N   . ASN A  1 456 ? 24.055  -3.433  -5.467  1.00 33.36  ? 456  ASN A N   1 
ATOM   3278  C  CA  . ASN A  1 456 ? 25.328  -3.943  -5.990  1.00 32.30  ? 456  ASN A CA  1 
ATOM   3279  C  C   . ASN A  1 456 ? 25.294  -4.223  -7.489  1.00 30.57  ? 456  ASN A C   1 
ATOM   3280  O  O   . ASN A  1 456 ? 26.226  -3.892  -8.212  1.00 29.08  ? 456  ASN A O   1 
ATOM   3281  C  CB  . ASN A  1 456 ? 25.759  -5.234  -5.276  1.00 35.08  ? 456  ASN A CB  1 
ATOM   3282  C  CG  . ASN A  1 456 ? 25.818  -5.112  -3.747  1.00 36.57  ? 456  ASN A CG  1 
ATOM   3283  O  OD1 . ASN A  1 456 ? 24.883  -4.639  -3.107  1.00 35.33  ? 456  ASN A OD1 1 
ATOM   3284  N  ND2 . ASN A  1 456 ? 26.920  -5.583  -3.163  1.00 31.05  ? 456  ASN A ND2 1 
ATOM   3285  N  N   . LYS A  1 457 ? 24.230  -4.851  -7.969  1.00 33.20  ? 457  LYS A N   1 
ATOM   3286  C  CA  . LYS A  1 457 ? 24.200  -5.191  -9.385  1.00 31.43  ? 457  LYS A CA  1 
ATOM   3287  C  C   . LYS A  1 457 ? 24.021  -3.962  -10.266 1.00 30.64  ? 457  LYS A C   1 
ATOM   3288  O  O   . LYS A  1 457 ? 24.614  -3.880  -11.334 1.00 33.11  ? 457  LYS A O   1 
ATOM   3289  C  CB  . LYS A  1 457 ? 23.106  -6.200  -9.700  1.00 34.15  ? 457  LYS A CB  1 
ATOM   3290  C  CG  . LYS A  1 457 ? 23.095  -6.610  -11.180 1.00 37.65  ? 457  LYS A CG  1 
ATOM   3291  C  CD  . LYS A  1 457 ? 22.093  -7.721  -11.455 1.00 38.31  ? 457  LYS A CD  1 
ATOM   3292  C  CE  . LYS A  1 457 ? 22.108  -8.163  -12.920 1.00 37.24  ? 457  LYS A CE  1 
ATOM   3293  N  NZ  . LYS A  1 457 ? 21.223  -9.370  -13.145 1.00 38.21  ? 457  LYS A NZ  1 
ATOM   3294  N  N   . GLY A  1 458 ? 23.195  -3.021  -9.831  1.00 30.87  ? 458  GLY A N   1 
ATOM   3295  C  CA  . GLY A  1 458 ? 23.039  -1.771  -10.555 1.00 29.94  ? 458  GLY A CA  1 
ATOM   3296  C  C   . GLY A  1 458 ? 24.386  -1.096  -10.666 1.00 32.17  ? 458  GLY A C   1 
ATOM   3297  O  O   . GLY A  1 458 ? 24.781  -0.623  -11.736 1.00 29.67  ? 458  GLY A O   1 
ATOM   3298  N  N   . ALA A  1 459 ? 25.117  -1.098  -9.556  1.00 29.07  ? 459  ALA A N   1 
ATOM   3299  C  CA  . ALA A  1 459 ? 26.426  -0.469  -9.520  1.00 30.88  ? 459  ALA A CA  1 
ATOM   3300  C  C   . ALA A  1 459 ? 27.370  -1.218  -10.427 1.00 34.00  ? 459  ALA A C   1 
ATOM   3301  O  O   . ALA A  1 459 ? 28.120  -0.609  -11.190 1.00 34.27  ? 459  ALA A O   1 
ATOM   3302  C  CB  . ALA A  1 459 ? 26.974  -0.424  -8.083  1.00 34.60  ? 459  ALA A CB  1 
ATOM   3303  N  N   . CYS A  1 460 ? 27.329  -2.548  -10.346 1.00 31.06  ? 460  CYS A N   1 
ATOM   3304  C  CA  . CYS A  1 460 ? 28.210  -3.368  -11.165 1.00 31.45  ? 460  CYS A CA  1 
ATOM   3305  C  C   . CYS A  1 460 ? 27.962  -3.220  -12.670 1.00 33.04  ? 460  CYS A C   1 
ATOM   3306  O  O   . CYS A  1 460 ? 28.916  -3.187  -13.439 1.00 37.59  ? 460  CYS A O   1 
ATOM   3307  C  CB  . CYS A  1 460 ? 28.099  -4.835  -10.763 1.00 32.60  ? 460  CYS A CB  1 
ATOM   3308  S  SG  . CYS A  1 460 ? 28.927  -5.145  -9.197  1.00 37.73  ? 460  CYS A SG  1 
ATOM   3309  N  N   . ILE A  1 461 ? 26.707  -3.129  -13.103 1.00 26.80  ? 461  ILE A N   1 
ATOM   3310  C  CA  . ILE A  1 461 ? 26.477  -2.979  -14.522 1.00 31.49  ? 461  ILE A CA  1 
ATOM   3311  C  C   . ILE A  1 461 ? 26.782  -1.547  -14.980 1.00 35.37  ? 461  ILE A C   1 
ATOM   3312  O  O   . ILE A  1 461 ? 27.173  -1.357  -16.117 1.00 36.61  ? 461  ILE A O   1 
ATOM   3313  C  CB  . ILE A  1 461 ? 25.054  -3.359  -14.942 1.00 35.54  ? 461  ILE A CB  1 
ATOM   3314  C  CG1 . ILE A  1 461 ? 24.042  -2.359  -14.406 1.00 32.00  ? 461  ILE A CG1 1 
ATOM   3315  C  CG2 . ILE A  1 461 ? 24.743  -4.836  -14.577 1.00 29.11  ? 461  ILE A CG2 1 
ATOM   3316  C  CD1 . ILE A  1 461 ? 22.655  -2.531  -14.973 1.00 38.22  ? 461  ILE A CD1 1 
ATOM   3317  N  N   . LEU A  1 462 ? 26.631  -0.561  -14.096 1.00 31.68  ? 462  LEU A N   1 
ATOM   3318  C  CA  . LEU A  1 462 ? 27.088  0.799   -14.373 1.00 34.30  ? 462  LEU A CA  1 
ATOM   3319  C  C   . LEU A  1 462 ? 28.586  0.810   -14.574 1.00 38.33  ? 462  LEU A C   1 
ATOM   3320  O  O   . LEU A  1 462 ? 29.093  1.462   -15.491 1.00 38.23  ? 462  LEU A O   1 
ATOM   3321  C  CB  . LEU A  1 462 ? 26.731  1.765   -13.238 1.00 32.89  ? 462  LEU A CB  1 
ATOM   3322  C  CG  . LEU A  1 462 ? 25.253  2.134   -13.243 1.00 30.68  ? 462  LEU A CG  1 
ATOM   3323  C  CD1 . LEU A  1 462 ? 24.949  3.009   -12.059 1.00 22.85  ? 462  LEU A CD1 1 
ATOM   3324  C  CD2 . LEU A  1 462 ? 24.858  2.783   -14.587 1.00 25.46  ? 462  LEU A CD2 1 
ATOM   3325  N  N   . ASN A  1 463 ? 29.300  0.087   -13.718 1.00 36.80  ? 463  ASN A N   1 
ATOM   3326  C  CA  . ASN A  1 463 ? 30.741  0.056   -13.834 1.00 34.50  ? 463  ASN A CA  1 
ATOM   3327  C  C   . ASN A  1 463 ? 31.143  -0.545  -15.185 1.00 39.53  ? 463  ASN A C   1 
ATOM   3328  O  O   . ASN A  1 463 ? 32.098  -0.114  -15.833 1.00 35.82  ? 463  ASN A O   1 
ATOM   3329  C  CB  . ASN A  1 463 ? 31.347  -0.740  -12.697 1.00 30.87  ? 463  ASN A CB  1 
ATOM   3330  C  CG  . ASN A  1 463 ? 32.846  -0.668  -12.693 1.00 37.09  ? 463  ASN A CG  1 
ATOM   3331  O  OD1 . ASN A  1 463 ? 33.423  0.416   -12.612 1.00 37.91  ? 463  ASN A OD1 1 
ATOM   3332  N  ND2 . ASN A  1 463 ? 33.494  -1.816  -12.821 1.00 37.14  ? 463  ASN A ND2 1 
ATOM   3333  N  N   . MET A  1 464 ? 30.389  -1.553  -15.592 1.00 36.36  ? 464  MET A N   1 
ATOM   3334  C  CA  . MET A  1 464 ? 30.689  -2.282  -16.799 1.00 42.62  ? 464  MET A CA  1 
ATOM   3335  C  C   . MET A  1 464 ? 30.535  -1.341  -17.995 1.00 38.72  ? 464  MET A C   1 
ATOM   3336  O  O   . MET A  1 464 ? 31.388  -1.321  -18.881 1.00 38.33  ? 464  MET A O   1 
ATOM   3337  C  CB  . MET A  1 464 ? 29.781  -3.510  -16.907 1.00 38.68  ? 464  MET A CB  1 
ATOM   3338  C  CG  . MET A  1 464 ? 29.726  -4.091  -18.285 1.00 43.75  ? 464  MET A CG  1 
ATOM   3339  S  SD  . MET A  1 464 ? 29.102  -5.757  -18.344 1.00 37.54  ? 464  MET A SD  1 
ATOM   3340  C  CE  . MET A  1 464 ? 27.354  -5.506  -18.056 1.00 33.79  ? 464  MET A CE  1 
ATOM   3341  N  N   . LEU A  1 465 ? 29.482  -0.523  -17.969 1.00 34.07  ? 465  LEU A N   1 
ATOM   3342  C  CA  . LEU A  1 465 ? 29.206  0.428   -19.032 1.00 36.63  ? 465  LEU A CA  1 
ATOM   3343  C  C   . LEU A  1 465 ? 30.189  1.614   -19.038 1.00 43.67  ? 465  LEU A C   1 
ATOM   3344  O  O   . LEU A  1 465 ? 30.552  2.134   -20.095 1.00 43.05  ? 465  LEU A O   1 
ATOM   3345  C  CB  . LEU A  1 465 ? 27.776  0.941   -18.919 1.00 41.70  ? 465  LEU A CB  1 
ATOM   3346  C  CG  . LEU A  1 465 ? 27.392  2.002   -19.970 1.00 38.32  ? 465  LEU A CG  1 
ATOM   3347  C  CD1 . LEU A  1 465 ? 27.090  1.347   -21.265 1.00 32.81  ? 465  LEU A CD1 1 
ATOM   3348  C  CD2 . LEU A  1 465 ? 26.213  2.846   -19.522 1.00 46.62  ? 465  LEU A CD2 1 
ATOM   3349  N  N   . LYS A  1 466 ? 30.625  2.049   -17.863 1.00 42.08  ? 466  LYS A N   1 
ATOM   3350  C  CA  . LYS A  1 466 ? 31.636  3.093   -17.815 1.00 43.12  ? 466  LYS A CA  1 
ATOM   3351  C  C   . LYS A  1 466 ? 32.915  2.617   -18.509 1.00 44.47  ? 466  LYS A C   1 
ATOM   3352  O  O   . LYS A  1 466 ? 33.604  3.389   -19.178 1.00 37.84  ? 466  LYS A O   1 
ATOM   3353  C  CB  . LYS A  1 466 ? 31.937  3.501   -16.375 1.00 36.01  ? 466  LYS A CB  1 
ATOM   3354  C  CG  . LYS A  1 466 ? 32.979  4.587   -16.275 1.00 42.96  ? 466  LYS A CG  1 
ATOM   3355  C  CD  . LYS A  1 466 ? 33.177  5.051   -14.839 1.00 53.51  ? 466  LYS A CD  1 
ATOM   3356  C  CE  . LYS A  1 466 ? 34.530  4.631   -14.296 1.00 60.59  ? 466  LYS A CE  1 
ATOM   3357  N  NZ  . LYS A  1 466 ? 34.663  3.137   -14.309 1.00 65.33  ? 466  LYS A NZ  1 
ATOM   3358  N  N   . ASP A  1 467 ? 33.224  1.336   -18.332 1.00 41.70  ? 467  ASP A N   1 
ATOM   3359  C  CA  . ASP A  1 467 ? 34.412  0.740   -18.925 1.00 44.33  ? 467  ASP A CA  1 
ATOM   3360  C  C   . ASP A  1 467 ? 34.276  0.716   -20.436 1.00 40.91  ? 467  ASP A C   1 
ATOM   3361  O  O   . ASP A  1 467 ? 35.190  1.075   -21.146 1.00 39.81  ? 467  ASP A O   1 
ATOM   3362  C  CB  . ASP A  1 467 ? 34.636  -0.670  -18.390 1.00 43.89  ? 467  ASP A CB  1 
ATOM   3363  C  CG  . ASP A  1 467 ? 35.969  -1.243  -18.812 1.00 44.47  ? 467  ASP A CG  1 
ATOM   3364  O  OD1 . ASP A  1 467 ? 37.009  -0.705  -18.393 1.00 42.92  ? 467  ASP A OD1 1 
ATOM   3365  O  OD2 . ASP A  1 467 ? 35.973  -2.249  -19.548 1.00 51.99  ? 467  ASP A OD2 1 
ATOM   3366  N  N   . PHE A  1 468 ? 33.106  0.309   -20.904 1.00 37.78  ? 468  PHE A N   1 
ATOM   3367  C  CA  . PHE A  1 468 ? 32.771  0.349   -22.319 1.00 42.31  ? 468  PHE A CA  1 
ATOM   3368  C  C   . PHE A  1 468 ? 32.808  1.752   -22.985 1.00 41.99  ? 468  PHE A C   1 
ATOM   3369  O  O   . PHE A  1 468 ? 33.527  1.957   -23.956 1.00 49.13  ? 468  PHE A O   1 
ATOM   3370  C  CB  . PHE A  1 468 ? 31.389  -0.269  -22.512 1.00 35.99  ? 468  PHE A CB  1 
ATOM   3371  C  CG  . PHE A  1 468 ? 31.043  -0.510  -23.943 1.00 42.88  ? 468  PHE A CG  1 
ATOM   3372  C  CD1 . PHE A  1 468 ? 31.660  -1.536  -24.658 1.00 39.94  ? 468  PHE A CD1 1 
ATOM   3373  C  CD2 . PHE A  1 468 ? 30.116  0.296   -24.588 1.00 41.99  ? 468  PHE A CD2 1 
ATOM   3374  C  CE1 . PHE A  1 468 ? 31.334  -1.757  -26.002 1.00 46.34  ? 468  PHE A CE1 1 
ATOM   3375  C  CE2 . PHE A  1 468 ? 29.779  0.087   -25.925 1.00 41.33  ? 468  PHE A CE2 1 
ATOM   3376  C  CZ  . PHE A  1 468 ? 30.395  -0.943  -26.640 1.00 42.12  ? 468  PHE A CZ  1 
ATOM   3377  N  N   . LEU A  1 469 ? 32.022  2.697   -22.481 1.00 42.77  ? 469  LEU A N   1 
ATOM   3378  C  CA  . LEU A  1 469 ? 31.951  4.046   -23.041 1.00 46.50  ? 469  LEU A CA  1 
ATOM   3379  C  C   . LEU A  1 469 ? 33.171  4.935   -22.741 1.00 46.44  ? 469  LEU A C   1 
ATOM   3380  O  O   . LEU A  1 469 ? 33.391  5.941   -23.417 1.00 46.50  ? 469  LEU A O   1 
ATOM   3381  C  CB  . LEU A  1 469 ? 30.704  4.761   -22.513 1.00 47.70  ? 469  LEU A CB  1 
ATOM   3382  C  CG  . LEU A  1 469 ? 29.332  4.112   -22.686 1.00 47.12  ? 469  LEU A CG  1 
ATOM   3383  C  CD1 . LEU A  1 469 ? 28.286  5.005   -22.045 1.00 45.28  ? 469  LEU A CD1 1 
ATOM   3384  C  CD2 . LEU A  1 469 ? 29.000  3.904   -24.139 1.00 39.65  ? 469  LEU A CD2 1 
ATOM   3385  N  N   . GLY A  1 470 ? 33.943  4.590   -21.719 1.00 39.34  ? 470  GLY A N   1 
ATOM   3386  C  CA  . GLY A  1 470 ? 35.020  5.459   -21.267 1.00 40.24  ? 470  GLY A CA  1 
ATOM   3387  C  C   . GLY A  1 470 ? 34.516  6.532   -20.317 1.00 41.91  ? 470  GLY A C   1 
ATOM   3388  O  O   . GLY A  1 470 ? 33.369  6.981   -20.436 1.00 42.52  ? 470  GLY A O   1 
ATOM   3389  N  N   . GLU A  1 471 ? 35.368  6.942   -19.381 1.00 39.53  ? 471  GLU A N   1 
ATOM   3390  C  CA  . GLU A  1 471 ? 34.991  7.900   -18.342 1.00 39.80  ? 471  GLU A CA  1 
ATOM   3391  C  C   . GLU A  1 471 ? 34.348  9.169   -18.893 1.00 43.46  ? 471  GLU A C   1 
ATOM   3392  O  O   . GLU A  1 471 ? 33.313  9.612   -18.384 1.00 44.06  ? 471  GLU A O   1 
ATOM   3393  C  CB  . GLU A  1 471 ? 36.207  8.282   -17.482 1.00 40.65  ? 471  GLU A CB  1 
ATOM   3394  C  CG  . GLU A  1 471 ? 35.909  9.311   -16.355 1.00 53.90  ? 471  GLU A CG  1 
ATOM   3395  C  CD  . GLU A  1 471 ? 34.765  8.894   -15.387 1.00 52.45  ? 471  GLU A CD  1 
ATOM   3396  O  OE1 . GLU A  1 471 ? 34.647  7.690   -15.063 1.00 61.23  ? 471  GLU A OE1 1 
ATOM   3397  O  OE2 . GLU A  1 471 ? 33.983  9.771   -14.944 1.00 42.35  ? 471  GLU A OE2 1 
ATOM   3398  N  N   . GLU A  1 472 ? 34.938  9.751   -19.930 1.00 45.31  ? 472  GLU A N   1 
ATOM   3399  C  CA  . GLU A  1 472 ? 34.465  11.054  -20.390 1.00 51.53  ? 472  GLU A CA  1 
ATOM   3400  C  C   . GLU A  1 472 ? 33.051  10.956  -20.931 1.00 43.44  ? 472  GLU A C   1 
ATOM   3401  O  O   . GLU A  1 472 ? 32.205  11.803  -20.640 1.00 45.35  ? 472  GLU A O   1 
ATOM   3402  C  CB  . GLU A  1 472 ? 35.397  11.648  -21.444 1.00 44.92  ? 472  GLU A CB  1 
ATOM   3403  C  CG  . GLU A  1 472 ? 36.788  11.981  -20.891 1.00 71.38  ? 472  GLU A CG  1 
ATOM   3404  C  CD  . GLU A  1 472 ? 36.761  12.863  -19.621 1.00 76.79  ? 472  GLU A CD  1 
ATOM   3405  O  OE1 . GLU A  1 472 ? 36.700  14.118  -19.740 1.00 72.76  ? 472  GLU A OE1 1 
ATOM   3406  O  OE2 . GLU A  1 472 ? 36.822  12.296  -18.500 1.00 75.60  ? 472  GLU A OE2 1 
ATOM   3407  N  N   . LYS A  1 473 ? 32.777  9.902   -21.678 1.00 33.57  ? 473  LYS A N   1 
ATOM   3408  C  CA  . LYS A  1 473 ? 31.489  9.814   -22.326 1.00 41.17  ? 473  LYS A CA  1 
ATOM   3409  C  C   . LYS A  1 473 ? 30.443  9.466   -21.297 1.00 42.75  ? 473  LYS A C   1 
ATOM   3410  O  O   . LYS A  1 473 ? 29.279  9.853   -21.410 1.00 43.77  ? 473  LYS A O   1 
ATOM   3411  C  CB  . LYS A  1 473 ? 31.507  8.779   -23.443 1.00 43.77  ? 473  LYS A CB  1 
ATOM   3412  C  CG  . LYS A  1 473 ? 30.294  8.862   -24.301 1.00 44.33  ? 473  LYS A CG  1 
ATOM   3413  C  CD  . LYS A  1 473 ? 30.443  8.053   -25.567 1.00 64.50  ? 473  LYS A CD  1 
ATOM   3414  C  CE  . LYS A  1 473 ? 31.518  8.623   -26.482 1.00 58.31  ? 473  LYS A CE  1 
ATOM   3415  N  NZ  . LYS A  1 473 ? 31.589  7.816   -27.726 1.00 55.99  ? 473  LYS A NZ  1 
ATOM   3416  N  N   . PHE A  1 474 ? 30.890  8.741   -20.278 1.00 43.18  ? 474  PHE A N   1 
ATOM   3417  C  CA  . PHE A  1 474 ? 30.034  8.267   -19.205 1.00 40.17  ? 474  PHE A CA  1 
ATOM   3418  C  C   . PHE A  1 474 ? 29.613  9.388   -18.233 1.00 40.52  ? 474  PHE A C   1 
ATOM   3419  O  O   . PHE A  1 474 ? 28.447  9.473   -17.842 1.00 39.18  ? 474  PHE A O   1 
ATOM   3420  C  CB  . PHE A  1 474 ? 30.751  7.135   -18.472 1.00 37.73  ? 474  PHE A CB  1 
ATOM   3421  C  CG  . PHE A  1 474 ? 29.978  6.564   -17.332 1.00 39.97  ? 474  PHE A CG  1 
ATOM   3422  C  CD1 . PHE A  1 474 ? 29.056  5.554   -17.536 1.00 45.38  ? 474  PHE A CD1 1 
ATOM   3423  C  CD2 . PHE A  1 474 ? 30.171  7.039   -16.043 1.00 41.29  ? 474  PHE A CD2 1 
ATOM   3424  C  CE1 . PHE A  1 474 ? 28.324  5.026   -16.466 1.00 33.77  ? 474  PHE A CE1 1 
ATOM   3425  C  CE2 . PHE A  1 474 ? 29.459  6.508   -14.987 1.00 46.17  ? 474  PHE A CE2 1 
ATOM   3426  C  CZ  . PHE A  1 474 ? 28.535  5.498   -15.207 1.00 40.40  ? 474  PHE A CZ  1 
ATOM   3427  N  N   . GLN A  1 475 ? 30.555  10.242  -17.848 1.00 38.47  ? 475  GLN A N   1 
ATOM   3428  C  CA  . GLN A  1 475 ? 30.226  11.388  -16.997 1.00 40.12  ? 475  GLN A CA  1 
ATOM   3429  C  C   . GLN A  1 475 ? 29.318  12.368  -17.751 1.00 41.09  ? 475  GLN A C   1 
ATOM   3430  O  O   . GLN A  1 475 ? 28.318  12.833  -17.219 1.00 38.17  ? 475  GLN A O   1 
ATOM   3431  C  CB  . GLN A  1 475 ? 31.499  12.084  -16.508 1.00 34.80  ? 475  GLN A CB  1 
ATOM   3432  C  CG  . GLN A  1 475 ? 31.325  13.539  -16.165 1.00 34.60  ? 475  GLN A CG  1 
ATOM   3433  C  CD  . GLN A  1 475 ? 32.619  14.167  -15.673 1.00 34.56  ? 475  GLN A CD  1 
ATOM   3434  O  OE1 . GLN A  1 475 ? 33.710  13.734  -16.038 1.00 45.29  ? 475  GLN A OE1 1 
ATOM   3435  N  NE2 . GLN A  1 475 ? 32.501  15.179  -14.825 1.00 35.54  ? 475  GLN A NE2 1 
ATOM   3436  N  N   . LYS A  1 476 ? 29.663  12.654  -19.000 1.00 37.38  ? 476  LYS A N   1 
ATOM   3437  C  CA  . LYS A  1 476 ? 28.812  13.447  -19.873 1.00 38.75  ? 476  LYS A CA  1 
ATOM   3438  C  C   . LYS A  1 476 ? 27.377  12.888  -19.942 1.00 35.80  ? 476  LYS A C   1 
ATOM   3439  O  O   . LYS A  1 476 ? 26.403  13.628  -19.972 1.00 37.38  ? 476  LYS A O   1 
ATOM   3440  C  CB  . LYS A  1 476 ? 29.434  13.516  -21.286 1.00 44.75  ? 476  LYS A CB  1 
ATOM   3441  C  CG  . LYS A  1 476 ? 29.815  14.912  -21.747 1.00 50.88  ? 476  LYS A CG  1 
ATOM   3442  C  CD  . LYS A  1 476 ? 31.269  15.282  -21.465 1.00 53.72  ? 476  LYS A CD  1 
ATOM   3443  C  CE  . LYS A  1 476 ? 31.479  16.781  -21.725 1.00 68.80  ? 476  LYS A CE  1 
ATOM   3444  N  NZ  . LYS A  1 476 ? 32.878  17.276  -21.499 1.00 70.43  ? 476  LYS A NZ  1 
ATOM   3445  N  N   . GLY A  1 477 ? 27.236  11.574  -19.974 1.00 40.92  ? 477  GLY A N   1 
ATOM   3446  C  CA  . GLY A  1 477 ? 25.908  10.987  -20.003 1.00 39.15  ? 477  GLY A CA  1 
ATOM   3447  C  C   . GLY A  1 477 ? 25.224  11.274  -18.686 1.00 37.01  ? 477  GLY A C   1 
ATOM   3448  O  O   . GLY A  1 477 ? 24.045  11.603  -18.626 1.00 38.57  ? 477  GLY A O   1 
ATOM   3449  N  N   . ILE A  1 478 ? 25.986  11.164  -17.613 1.00 34.17  ? 478  ILE A N   1 
ATOM   3450  C  CA  . ILE A  1 478 ? 25.425  11.410  -16.306 1.00 36.93  ? 478  ILE A CA  1 
ATOM   3451  C  C   . ILE A  1 478 ? 24.907  12.847  -16.188 1.00 33.89  ? 478  ILE A C   1 
ATOM   3452  O  O   . ILE A  1 478 ? 23.752  13.062  -15.833 1.00 34.22  ? 478  ILE A O   1 
ATOM   3453  C  CB  . ILE A  1 478 ? 26.461  11.116  -15.212 1.00 38.05  ? 478  ILE A CB  1 
ATOM   3454  C  CG1 . ILE A  1 478 ? 26.599  9.603   -15.031 1.00 35.59  ? 478  ILE A CG1 1 
ATOM   3455  C  CG2 . ILE A  1 478 ? 26.059  11.767  -13.897 1.00 38.87  ? 478  ILE A CG2 1 
ATOM   3456  C  CD1 . ILE A  1 478 ? 27.646  9.223   -14.047 1.00 35.78  ? 478  ILE A CD1 1 
ATOM   3457  N  N   . ILE A  1 479 ? 25.759  13.812  -16.516 1.00 33.79  ? 479  ILE A N   1 
ATOM   3458  C  CA  . ILE A  1 479 ? 25.421  15.223  -16.432 1.00 29.65  ? 479  ILE A CA  1 
ATOM   3459  C  C   . ILE A  1 479 ? 24.137  15.587  -17.176 1.00 31.48  ? 479  ILE A C   1 
ATOM   3460  O  O   . ILE A  1 479 ? 23.281  16.299  -16.648 1.00 36.45  ? 479  ILE A O   1 
ATOM   3461  C  CB  . ILE A  1 479 ? 26.579  16.085  -16.955 1.00 32.62  ? 479  ILE A CB  1 
ATOM   3462  C  CG1 . ILE A  1 479 ? 27.855  15.795  -16.165 1.00 33.31  ? 479  ILE A CG1 1 
ATOM   3463  C  CG2 . ILE A  1 479 ? 26.258  17.551  -16.874 1.00 30.70  ? 479  ILE A CG2 1 
ATOM   3464  C  CD1 . ILE A  1 479 ? 28.953  16.824  -16.437 1.00 30.31  ? 479  ILE A CD1 1 
ATOM   3465  N  N   . GLN A  1 480 ? 23.962  15.082  -18.382 1.00 32.57  ? 480  GLN A N   1 
ATOM   3466  C  CA  . GLN A  1 480 ? 22.788  15.501  -19.141 1.00 35.43  ? 480  GLN A CA  1 
ATOM   3467  C  C   . GLN A  1 480 ? 21.518  14.807  -18.628 1.00 33.99  ? 480  GLN A C   1 
ATOM   3468  O  O   . GLN A  1 480 ? 20.444  15.403  -18.622 1.00 37.09  ? 480  GLN A O   1 
ATOM   3469  C  CB  . GLN A  1 480 ? 23.005  15.265  -20.645 1.00 38.80  ? 480  GLN A CB  1 
ATOM   3470  C  CG  . GLN A  1 480 ? 24.229  16.044  -21.232 1.00 41.76  ? 480  GLN A CG  1 
ATOM   3471  C  CD  . GLN A  1 480 ? 24.079  17.590  -21.251 1.00 53.25  ? 480  GLN A CD  1 
ATOM   3472  O  OE1 . GLN A  1 480 ? 23.034  18.134  -21.635 1.00 53.36  ? 480  GLN A OE1 1 
ATOM   3473  N  NE2 . GLN A  1 480 ? 25.148  18.297  -20.851 1.00 50.11  ? 480  GLN A NE2 1 
ATOM   3474  N  N   . TYR A  1 481 ? 21.639  13.568  -18.167 1.00 30.06  ? 481  TYR A N   1 
ATOM   3475  C  CA  . TYR A  1 481 ? 20.557  12.911  -17.435 1.00 28.00  ? 481  TYR A CA  1 
ATOM   3476  C  C   . TYR A  1 481 ? 20.086  13.718  -16.192 1.00 36.55  ? 481  TYR A C   1 
ATOM   3477  O  O   . TYR A  1 481 ? 18.896  13.963  -16.008 1.00 35.02  ? 481  TYR A O   1 
ATOM   3478  C  CB  . TYR A  1 481 ? 21.006  11.508  -17.006 1.00 29.62  ? 481  TYR A CB  1 
ATOM   3479  C  CG  . TYR A  1 481 ? 20.038  10.793  -16.092 1.00 30.67  ? 481  TYR A CG  1 
ATOM   3480  C  CD1 . TYR A  1 481 ? 18.837  10.272  -16.583 1.00 33.40  ? 481  TYR A CD1 1 
ATOM   3481  C  CD2 . TYR A  1 481 ? 20.323  10.632  -14.745 1.00 26.69  ? 481  TYR A CD2 1 
ATOM   3482  C  CE1 . TYR A  1 481 ? 17.931  9.623   -15.757 1.00 27.92  ? 481  TYR A CE1 1 
ATOM   3483  C  CE2 . TYR A  1 481 ? 19.438  9.978   -13.910 1.00 33.61  ? 481  TYR A CE2 1 
ATOM   3484  C  CZ  . TYR A  1 481 ? 18.242  9.467   -14.418 1.00 33.22  ? 481  TYR A CZ  1 
ATOM   3485  O  OH  . TYR A  1 481 ? 17.366  8.834   -13.563 1.00 27.51  ? 481  TYR A OH  1 
ATOM   3486  N  N   . LEU A  1 482 ? 21.027  14.126  -15.344 1.00 32.30  ? 482  LEU A N   1 
ATOM   3487  C  CA  . LEU A  1 482 ? 20.700  14.848  -14.124 1.00 31.03  ? 482  LEU A CA  1 
ATOM   3488  C  C   . LEU A  1 482 ? 20.113  16.217  -14.472 1.00 39.33  ? 482  LEU A C   1 
ATOM   3489  O  O   . LEU A  1 482 ? 19.172  16.687  -13.815 1.00 34.85  ? 482  LEU A O   1 
ATOM   3490  C  CB  . LEU A  1 482 ? 21.947  14.991  -13.232 1.00 28.83  ? 482  LEU A CB  1 
ATOM   3491  C  CG  . LEU A  1 482 ? 22.451  13.666  -12.616 1.00 32.10  ? 482  LEU A CG  1 
ATOM   3492  C  CD1 . LEU A  1 482 ? 23.712  13.819  -11.771 1.00 33.72  ? 482  LEU A CD1 1 
ATOM   3493  C  CD2 . LEU A  1 482 ? 21.367  13.024  -11.772 1.00 27.15  ? 482  LEU A CD2 1 
ATOM   3494  N  N   . LYS A  1 483 ? 20.661  16.848  -15.518 1.00 38.52  ? 483  LYS A N   1 
ATOM   3495  C  CA  . LYS A  1 483 ? 20.201  18.173  -15.928 1.00 34.64  ? 483  LYS A CA  1 
ATOM   3496  C  C   . LYS A  1 483 ? 18.810  18.090  -16.531 1.00 31.73  ? 483  LYS A C   1 
ATOM   3497  O  O   . LYS A  1 483 ? 17.943  18.899  -16.221 1.00 35.10  ? 483  LYS A O   1 
ATOM   3498  C  CB  . LYS A  1 483 ? 21.180  18.803  -16.916 1.00 31.98  ? 483  LYS A CB  1 
ATOM   3499  C  CG  . LYS A  1 483 ? 22.415  19.387  -16.241 1.00 41.32  ? 483  LYS A CG  1 
ATOM   3500  C  CD  . LYS A  1 483 ? 23.337  20.081  -17.222 1.00 42.49  ? 483  LYS A CD  1 
ATOM   3501  C  CE  . LYS A  1 483 ? 24.515  20.743  -16.495 1.00 41.63  ? 483  LYS A CE  1 
ATOM   3502  N  NZ  . LYS A  1 483 ? 25.513  21.307  -17.462 1.00 42.26  ? 483  LYS A NZ  1 
ATOM   3503  N  N   . LYS A  1 484 ? 18.589  17.069  -17.349 1.00 33.26  ? 484  LYS A N   1 
ATOM   3504  C  CA  . LYS A  1 484 ? 17.336  16.922  -18.083 1.00 35.43  ? 484  LYS A CA  1 
ATOM   3505  C  C   . LYS A  1 484 ? 16.157  16.532  -17.211 1.00 37.72  ? 484  LYS A C   1 
ATOM   3506  O  O   . LYS A  1 484 ? 15.023  16.800  -17.566 1.00 44.10  ? 484  LYS A O   1 
ATOM   3507  C  CB  . LYS A  1 484 ? 17.516  15.895  -19.190 1.00 35.86  ? 484  LYS A CB  1 
ATOM   3508  C  CG  . LYS A  1 484 ? 16.253  15.484  -19.921 1.00 39.57  ? 484  LYS A CG  1 
ATOM   3509  C  CD  . LYS A  1 484 ? 16.626  14.698  -21.158 1.00 37.32  ? 484  LYS A CD  1 
ATOM   3510  C  CE  . LYS A  1 484 ? 15.405  14.278  -21.939 1.00 45.09  ? 484  LYS A CE  1 
ATOM   3511  N  NZ  . LYS A  1 484 ? 15.822  13.350  -23.027 1.00 55.77  ? 484  LYS A NZ  1 
ATOM   3512  N  N   . PHE A  1 485 ? 16.419  15.905  -16.068 1.00 37.43  ? 485  PHE A N   1 
ATOM   3513  C  CA  . PHE A  1 485 ? 15.349  15.415  -15.204 1.00 34.60  ? 485  PHE A CA  1 
ATOM   3514  C  C   . PHE A  1 485 ? 15.331  16.083  -13.828 1.00 30.95  ? 485  PHE A C   1 
ATOM   3515  O  O   . PHE A  1 485 ? 14.580  15.685  -12.941 1.00 29.71  ? 485  PHE A O   1 
ATOM   3516  C  CB  . PHE A  1 485 ? 15.465  13.891  -15.074 1.00 35.14  ? 485  PHE A CB  1 
ATOM   3517  C  CG  . PHE A  1 485 ? 15.254  13.174  -16.375 1.00 35.04  ? 485  PHE A CG  1 
ATOM   3518  C  CD1 . PHE A  1 485 ? 13.970  12.927  -16.844 1.00 36.28  ? 485  PHE A CD1 1 
ATOM   3519  C  CD2 . PHE A  1 485 ? 16.336  12.780  -17.151 1.00 36.25  ? 485  PHE A CD2 1 
ATOM   3520  C  CE1 . PHE A  1 485 ? 13.766  12.266  -18.058 1.00 39.50  ? 485  PHE A CE1 1 
ATOM   3521  C  CE2 . PHE A  1 485 ? 16.150  12.124  -18.369 1.00 36.64  ? 485  PHE A CE2 1 
ATOM   3522  C  CZ  . PHE A  1 485 ? 14.862  11.863  -18.819 1.00 39.74  ? 485  PHE A CZ  1 
ATOM   3523  N  N   . SER A  1 486 ? 16.170  17.106  -13.678 1.00 34.75  ? 486  SER A N   1 
ATOM   3524  C  CA  . SER A  1 486 ? 16.195  17.950  -12.492 1.00 30.71  ? 486  SER A CA  1 
ATOM   3525  C  C   . SER A  1 486 ? 14.809  18.305  -12.001 1.00 31.72  ? 486  SER A C   1 
ATOM   3526  O  O   . SER A  1 486 ? 13.966  18.724  -12.775 1.00 34.03  ? 486  SER A O   1 
ATOM   3527  C  CB  . SER A  1 486 ? 16.949  19.238  -12.765 1.00 30.28  ? 486  SER A CB  1 
ATOM   3528  O  OG  . SER A  1 486 ? 18.340  19.044  -12.690 1.00 39.11  ? 486  SER A OG  1 
ATOM   3529  N  N   . TYR A  1 487 ? 14.575  18.103  -10.713 1.00 31.08  ? 487  TYR A N   1 
ATOM   3530  C  CA  . TYR A  1 487 ? 13.303  18.416  -10.072 1.00 30.58  ? 487  TYR A CA  1 
ATOM   3531  C  C   . TYR A  1 487 ? 12.085  17.662  -10.604 1.00 31.68  ? 487  TYR A C   1 
ATOM   3532  O  O   . TYR A  1 487 ? 10.972  18.095  -10.393 1.00 33.12  ? 487  TYR A O   1 
ATOM   3533  C  CB  . TYR A  1 487 ? 13.067  19.947  -10.116 1.00 23.95  ? 487  TYR A CB  1 
ATOM   3534  C  CG  . TYR A  1 487 ? 14.241  20.722  -9.552  1.00 26.90  ? 487  TYR A CG  1 
ATOM   3535  C  CD1 . TYR A  1 487 ? 14.503  20.712  -8.185  1.00 26.31  ? 487  TYR A CD1 1 
ATOM   3536  C  CD2 . TYR A  1 487 ? 15.126  21.404  -10.388 1.00 27.50  ? 487  TYR A CD2 1 
ATOM   3537  C  CE1 . TYR A  1 487 ? 15.591  21.395  -7.654  1.00 29.41  ? 487  TYR A CE1 1 
ATOM   3538  C  CE2 . TYR A  1 487 ? 16.228  22.094  -9.876  1.00 25.03  ? 487  TYR A CE2 1 
ATOM   3539  C  CZ  . TYR A  1 487 ? 16.447  22.079  -8.507  1.00 30.33  ? 487  TYR A CZ  1 
ATOM   3540  O  OH  . TYR A  1 487 ? 17.522  22.732  -7.997  1.00 28.31  ? 487  TYR A OH  1 
ATOM   3541  N  N   . ARG A  1 488 ? 12.293  16.500  -11.214 1.00 30.20  ? 488  ARG A N   1 
ATOM   3542  C  CA  . ARG A  1 488 ? 11.196  15.556  -11.488 1.00 38.18  ? 488  ARG A CA  1 
ATOM   3543  C  C   . ARG A  1 488 ? 11.683  14.112  -11.541 1.00 36.59  ? 488  ARG A C   1 
ATOM   3544  O  O   . ARG A  1 488 ? 12.626  13.725  -10.875 1.00 34.22  ? 488  ARG A O   1 
ATOM   3545  C  CB  . ARG A  1 488 ? 10.500  15.930  -12.809 1.00 42.37  ? 488  ARG A CB  1 
ATOM   3546  C  CG  . ARG A  1 488 ? 11.458  16.018  -13.971 1.00 36.41  ? 488  ARG A CG  1 
ATOM   3547  C  CD  . ARG A  1 488 ? 10.954  16.826  -15.186 1.00 47.27  ? 488  ARG A CD  1 
ATOM   3548  N  NE  . ARG A  1 488 ? 11.685  16.668  -16.475 1.00 45.52  ? 488  ARG A NE  1 
ATOM   3549  C  CZ  . ARG A  1 488 ? 11.379  15.764  -17.411 1.00 47.18  ? 488  ARG A CZ  1 
ATOM   3550  N  NH1 . ARG A  1 488 ? 10.393  14.891  -17.204 1.00 38.16  ? 488  ARG A NH1 1 
ATOM   3551  N  NH2 . ARG A  1 488 ? 12.065  15.709  -18.552 1.00 52.97  ? 488  ARG A NH2 1 
ATOM   3552  N  N   . ASN A  1 489 ? 11.051  13.317  -12.383 1.00 40.57  ? 489  ASN A N   1 
ATOM   3553  C  CA  . ASN A  1 489 ? 11.304  11.896  -12.337 1.00 34.64  ? 489  ASN A CA  1 
ATOM   3554  C  C   . ASN A  1 489 ? 11.771  11.206  -13.623 1.00 38.27  ? 489  ASN A C   1 
ATOM   3555  O  O   . ASN A  1 489 ? 11.519  11.653  -14.736 1.00 35.25  ? 489  ASN A O   1 
ATOM   3556  C  CB  . ASN A  1 489 ? 10.049  11.226  -11.801 1.00 37.55  ? 489  ASN A CB  1 
ATOM   3557  C  CG  . ASN A  1 489 ? 9.644   11.780  -10.449 1.00 37.78  ? 489  ASN A CG  1 
ATOM   3558  O  OD1 . ASN A  1 489 ? 9.275   12.943  -10.320 1.00 41.32  ? 489  ASN A OD1 1 
ATOM   3559  N  ND2 . ASN A  1 489 ? 9.738   10.954  -9.433  1.00 36.76  ? 489  ASN A ND2 1 
ATOM   3560  N  N   . ALA A  1 490 ? 12.514  10.125  -13.437 1.00 38.82  ? 490  ALA A N   1 
ATOM   3561  C  CA  . ALA A  1 490 ? 12.929  9.291   -14.552 1.00 38.17  ? 490  ALA A CA  1 
ATOM   3562  C  C   . ALA A  1 490 ? 12.525  7.837   -14.316 1.00 42.68  ? 490  ALA A C   1 
ATOM   3563  O  O   . ALA A  1 490 ? 12.272  7.390   -13.172 1.00 41.80  ? 490  ALA A O   1 
ATOM   3564  C  CB  . ALA A  1 490 ? 14.412  9.395   -14.770 1.00 33.62  ? 490  ALA A CB  1 
ATOM   3565  N  N   . LYS A  1 491 ? 12.439  7.099   -15.411 1.00 42.18  ? 491  LYS A N   1 
ATOM   3566  C  CA  . LYS A  1 491 ? 12.245  5.664   -15.313 1.00 38.38  ? 491  LYS A CA  1 
ATOM   3567  C  C   . LYS A  1 491 ? 13.363  5.000   -16.084 1.00 41.15  ? 491  LYS A C   1 
ATOM   3568  O  O   . LYS A  1 491 ? 14.151  5.676   -16.744 1.00 40.91  ? 491  LYS A O   1 
ATOM   3569  C  CB  . LYS A  1 491 ? 10.876  5.237   -15.830 1.00 43.72  ? 491  LYS A CB  1 
ATOM   3570  C  CG  . LYS A  1 491 ? 10.621  5.507   -17.302 1.00 42.25  ? 491  LYS A CG  1 
ATOM   3571  C  CD  . LYS A  1 491 ? 9.562   4.555   -17.838 1.00 46.38  ? 491  LYS A CD  1 
ATOM   3572  C  CE  . LYS A  1 491 ? 9.123   4.922   -19.242 1.00 49.71  ? 491  LYS A CE  1 
ATOM   3573  N  NZ  . LYS A  1 491 ? 7.921   5.799   -19.177 1.00 65.36  ? 491  LYS A NZ  1 
ATOM   3574  N  N   . ASN A  1 492 ? 13.447  3.682   -15.970 1.00 41.56  ? 492  ASN A N   1 
ATOM   3575  C  CA  . ASN A  1 492 ? 14.594  2.953   -16.469 1.00 40.57  ? 492  ASN A CA  1 
ATOM   3576  C  C   . ASN A  1 492 ? 15.016  3.392   -17.878 1.00 40.93  ? 492  ASN A C   1 
ATOM   3577  O  O   . ASN A  1 492 ? 16.190  3.647   -18.137 1.00 39.69  ? 492  ASN A O   1 
ATOM   3578  C  CB  . ASN A  1 492 ? 14.298  1.453   -16.432 1.00 44.21  ? 492  ASN A CB  1 
ATOM   3579  C  CG  . ASN A  1 492 ? 15.531  0.624   -16.673 1.00 47.52  ? 492  ASN A CG  1 
ATOM   3580  O  OD1 . ASN A  1 492 ? 16.441  0.612   -15.849 1.00 45.76  ? 492  ASN A OD1 1 
ATOM   3581  N  ND2 . ASN A  1 492 ? 15.579  -0.069  -17.810 1.00 48.60  ? 492  ASN A ND2 1 
ATOM   3582  N  N   . ASP A  1 493 ? 14.055  3.539   -18.779 1.00 44.54  ? 493  ASP A N   1 
ATOM   3583  C  CA  . ASP A  1 493 ? 14.396  3.895   -20.154 1.00 43.25  ? 493  ASP A CA  1 
ATOM   3584  C  C   . ASP A  1 493 ? 14.900  5.332   -20.333 1.00 46.58  ? 493  ASP A C   1 
ATOM   3585  O  O   . ASP A  1 493 ? 15.699  5.613   -21.232 1.00 44.96  ? 493  ASP A O   1 
ATOM   3586  C  CB  . ASP A  1 493 ? 13.205  3.678   -21.078 1.00 46.90  ? 493  ASP A CB  1 
ATOM   3587  C  CG  . ASP A  1 493 ? 13.600  3.785   -22.546 1.00 66.01  ? 493  ASP A CG  1 
ATOM   3588  O  OD1 . ASP A  1 493 ? 14.437  2.964   -23.002 1.00 67.67  ? 493  ASP A OD1 1 
ATOM   3589  O  OD2 . ASP A  1 493 ? 13.095  4.702   -23.236 1.00 71.31  ? 493  ASP A OD2 1 
ATOM   3590  N  N   . ASP A  1 494 ? 14.416  6.249   -19.506 1.00 43.84  ? 494  ASP A N   1 
ATOM   3591  C  CA  . ASP A  1 494 ? 14.878  7.616   -19.591 1.00 41.53  ? 494  ASP A CA  1 
ATOM   3592  C  C   . ASP A  1 494 ? 16.375  7.633   -19.370 1.00 41.45  ? 494  ASP A C   1 
ATOM   3593  O  O   . ASP A  1 494 ? 17.121  8.291   -20.098 1.00 44.38  ? 494  ASP A O   1 
ATOM   3594  C  CB  . ASP A  1 494 ? 14.152  8.495   -18.582 1.00 39.10  ? 494  ASP A CB  1 
ATOM   3595  C  CG  . ASP A  1 494 ? 12.765  8.881   -19.054 1.00 48.49  ? 494  ASP A CG  1 
ATOM   3596  O  OD1 . ASP A  1 494 ? 12.634  9.209   -20.267 1.00 47.34  ? 494  ASP A OD1 1 
ATOM   3597  O  OD2 . ASP A  1 494 ? 11.811  8.838   -18.228 1.00 48.19  ? 494  ASP A OD2 1 
ATOM   3598  N  N   . LEU A  1 495 ? 16.816  6.854   -18.397 1.00 36.55  ? 495  LEU A N   1 
ATOM   3599  C  CA  . LEU A  1 495 ? 18.222  6.782   -18.082 1.00 32.71  ? 495  LEU A CA  1 
ATOM   3600  C  C   . LEU A  1 495 ? 19.051  6.186   -19.231 1.00 39.92  ? 495  LEU A C   1 
ATOM   3601  O  O   . LEU A  1 495 ? 20.126  6.696   -19.560 1.00 41.40  ? 495  LEU A O   1 
ATOM   3602  C  CB  . LEU A  1 495 ? 18.440  5.969   -16.797 1.00 33.82  ? 495  LEU A CB  1 
ATOM   3603  C  CG  . LEU A  1 495 ? 19.951  5.946   -16.584 1.00 36.83  ? 495  LEU A CG  1 
ATOM   3604  C  CD1 . LEU A  1 495 ? 20.417  7.064   -15.644 1.00 31.60  ? 495  LEU A CD1 1 
ATOM   3605  C  CD2 . LEU A  1 495 ? 20.475  4.569   -16.216 1.00 39.46  ? 495  LEU A CD2 1 
ATOM   3606  N  N   . TRP A  1 496 ? 18.575  5.107   -19.847 1.00 40.48  ? 496  TRP A N   1 
ATOM   3607  C  CA  . TRP A  1 496 ? 19.378  4.484   -20.902 1.00 39.18  ? 496  TRP A CA  1 
ATOM   3608  C  C   . TRP A  1 496 ? 19.468  5.357   -22.158 1.00 39.50  ? 496  TRP A C   1 
ATOM   3609  O  O   . TRP A  1 496 ? 20.512  5.372   -22.823 1.00 36.17  ? 496  TRP A O   1 
ATOM   3610  C  CB  . TRP A  1 496 ? 18.844  3.085   -21.226 1.00 41.86  ? 496  TRP A CB  1 
ATOM   3611  C  CG  . TRP A  1 496 ? 18.987  2.198   -20.051 1.00 37.77  ? 496  TRP A CG  1 
ATOM   3612  C  CD1 . TRP A  1 496 ? 17.991  1.539   -19.384 1.00 43.18  ? 496  TRP A CD1 1 
ATOM   3613  C  CD2 . TRP A  1 496 ? 20.201  1.916   -19.342 1.00 38.78  ? 496  TRP A CD2 1 
ATOM   3614  N  NE1 . TRP A  1 496 ? 18.517  0.840   -18.318 1.00 42.05  ? 496  TRP A NE1 1 
ATOM   3615  C  CE2 . TRP A  1 496 ? 19.868  1.065   -18.264 1.00 35.97  ? 496  TRP A CE2 1 
ATOM   3616  C  CE3 . TRP A  1 496 ? 21.537  2.296   -19.517 1.00 34.03  ? 496  TRP A CE3 1 
ATOM   3617  C  CZ2 . TRP A  1 496 ? 20.824  0.579   -17.376 1.00 40.51  ? 496  TRP A CZ2 1 
ATOM   3618  C  CZ3 . TRP A  1 496 ? 22.484  1.817   -18.634 1.00 38.52  ? 496  TRP A CZ3 1 
ATOM   3619  C  CH2 . TRP A  1 496 ? 22.126  0.964   -17.572 1.00 36.33  ? 496  TRP A CH2 1 
ATOM   3620  N  N   . SER A  1 497 ? 18.414  6.124   -22.449 1.00 39.23  ? 497  SER A N   1 
ATOM   3621  C  CA  . SER A  1 497 ? 18.472  7.114   -23.538 1.00 39.50  ? 497  SER A CA  1 
ATOM   3622  C  C   . SER A  1 497 ? 19.599  8.129   -23.329 1.00 46.79  ? 497  SER A C   1 
ATOM   3623  O  O   . SER A  1 497 ? 20.431  8.320   -24.219 1.00 52.98  ? 497  SER A O   1 
ATOM   3624  C  CB  . SER A  1 497 ? 17.147  7.867   -23.688 1.00 33.94  ? 497  SER A CB  1 
ATOM   3625  O  OG  . SER A  1 497 ? 16.071  6.972   -23.857 1.00 40.70  ? 497  SER A OG  1 
ATOM   3626  N  N   . SER A  1 498 ? 19.633  8.771   -22.162 1.00 39.27  ? 498  SER A N   1 
ATOM   3627  C  CA  . SER A  1 498 ? 20.643  9.775   -21.898 1.00 39.14  ? 498  SER A CA  1 
ATOM   3628  C  C   . SER A  1 498 ? 22.034  9.177   -21.887 1.00 42.71  ? 498  SER A C   1 
ATOM   3629  O  O   . SER A  1 498 ? 22.983  9.801   -22.365 1.00 51.78  ? 498  SER A O   1 
ATOM   3630  C  CB  . SER A  1 498 ? 20.384  10.482  -20.567 1.00 37.86  ? 498  SER A CB  1 
ATOM   3631  O  OG  . SER A  1 498 ? 19.032  10.879  -20.478 1.00 45.62  ? 498  SER A OG  1 
ATOM   3632  N  N   . LEU A  1 499 ? 22.182  7.982   -21.338 1.00 41.09  ? 499  LEU A N   1 
ATOM   3633  C  CA  . LEU A  1 499 ? 23.517  7.388   -21.295 1.00 47.97  ? 499  LEU A CA  1 
ATOM   3634  C  C   . LEU A  1 499 ? 23.969  6.924   -22.668 1.00 46.58  ? 499  LEU A C   1 
ATOM   3635  O  O   . LEU A  1 499 ? 25.137  7.062   -23.007 1.00 50.74  ? 499  LEU A O   1 
ATOM   3636  C  CB  . LEU A  1 499 ? 23.578  6.227   -20.300 1.00 46.78  ? 499  LEU A CB  1 
ATOM   3637  C  CG  . LEU A  1 499 ? 23.445  6.702   -18.850 1.00 46.89  ? 499  LEU A CG  1 
ATOM   3638  C  CD1 . LEU A  1 499 ? 23.844  5.620   -17.865 1.00 43.19  ? 499  LEU A CD1 1 
ATOM   3639  C  CD2 . LEU A  1 499 ? 24.247  7.974   -18.629 1.00 37.67  ? 499  LEU A CD2 1 
ATOM   3640  N  N   . SER A  1 500 ? 23.054  6.387   -23.467 1.00 41.96  ? 500  SER A N   1 
ATOM   3641  C  CA  . SER A  1 500 ? 23.440  5.935   -24.800 1.00 46.49  ? 500  SER A CA  1 
ATOM   3642  C  C   . SER A  1 500 ? 23.581  7.107   -25.793 1.00 48.58  ? 500  SER A C   1 
ATOM   3643  O  O   . SER A  1 500 ? 24.210  6.948   -26.826 1.00 48.58  ? 500  SER A O   1 
ATOM   3644  C  CB  . SER A  1 500 ? 22.448  4.883   -25.334 1.00 39.73  ? 500  SER A CB  1 
ATOM   3645  O  OG  . SER A  1 500 ? 21.124  5.377   -25.397 1.00 43.22  ? 500  SER A OG  1 
ATOM   3646  N  N   . ASN A  1 501 ? 23.047  8.285   -25.472 1.00 45.89  ? 501  ASN A N   1 
ATOM   3647  C  CA  . ASN A  1 501 ? 23.206  9.441   -26.364 1.00 45.85  ? 501  ASN A CA  1 
ATOM   3648  C  C   . ASN A  1 501 ? 24.207  10.488  -25.899 1.00 46.16  ? 501  ASN A C   1 
ATOM   3649  O  O   . ASN A  1 501 ? 23.974  11.679  -26.075 1.00 50.00  ? 501  ASN A O   1 
ATOM   3650  C  CB  . ASN A  1 501 ? 21.867  10.139  -26.570 1.00 46.25  ? 501  ASN A CB  1 
ATOM   3651  C  CG  . ASN A  1 501 ? 20.828  9.232   -27.191 1.00 55.03  ? 501  ASN A CG  1 
ATOM   3652  O  OD1 . ASN A  1 501 ? 21.159  8.182   -27.751 1.00 57.14  ? 501  ASN A OD1 1 
ATOM   3653  N  ND2 . ASN A  1 501 ? 19.559  9.632   -27.100 1.00 52.11  ? 501  ASN A ND2 1 
ATOM   3654  N  N   . SER A  1 502 ? 25.319  10.070  -25.311 1.00 45.77  ? 502  SER A N   1 
ATOM   3655  C  CA  . SER A  1 502 ? 26.214  11.046  -24.696 1.00 53.38  ? 502  SER A CA  1 
ATOM   3656  C  C   . SER A  1 502 ? 27.284  11.570  -25.636 1.00 57.91  ? 502  SER A C   1 
ATOM   3657  O  O   . SER A  1 502 ? 27.919  10.816  -26.362 1.00 54.86  ? 502  SER A O   1 
ATOM   3658  C  CB  . SER A  1 502 ? 26.883  10.456  -23.464 1.00 46.92  ? 502  SER A CB  1 
ATOM   3659  O  OG  . SER A  1 502 ? 27.404  9.180   -23.778 1.00 58.22  ? 502  SER A OG  1 
ATOM   3660  N  N   . CYS A  1 503 ? 27.500  12.877  -25.570 1.00 65.57  ? 503  CYS A N   1 
ATOM   3661  C  CA  . CYS A  1 503 ? 28.410  13.566  -26.463 1.00 70.89  ? 503  CYS A CA  1 
ATOM   3662  C  C   . CYS A  1 503 ? 29.766  13.859  -25.827 1.00 73.58  ? 503  CYS A C   1 
ATOM   3663  O  O   . CYS A  1 503 ? 29.831  14.598  -24.852 1.00 86.07  ? 503  CYS A O   1 
ATOM   3664  C  CB  . CYS A  1 503 ? 27.766  14.873  -26.920 1.00 83.91  ? 503  CYS A CB  1 
ATOM   3665  S  SG  . CYS A  1 503 ? 26.029  14.710  -27.450 1.00 100.31 ? 503  CYS A SG  1 
ATOM   3666  N  N   . LEU A  1 504 ? 30.842  13.295  -26.380 1.00 70.84  ? 504  LEU A N   1 
ATOM   3667  C  CA  . LEU A  1 504 ? 32.209  13.631  -25.963 1.00 76.21  ? 504  LEU A CA  1 
ATOM   3668  C  C   . LEU A  1 504 ? 32.480  15.113  -26.191 1.00 83.62  ? 504  LEU A C   1 
ATOM   3669  O  O   . LEU A  1 504 ? 31.711  15.776  -26.889 1.00 88.79  ? 504  LEU A O   1 
ATOM   3670  C  CB  . LEU A  1 504 ? 33.239  12.795  -26.736 1.00 71.54  ? 504  LEU A CB  1 
ATOM   3671  C  CG  . LEU A  1 504 ? 34.545  12.288  -26.101 1.00 73.03  ? 504  LEU A CG  1 
ATOM   3672  C  CD1 . LEU A  1 504 ? 35.167  11.297  -27.055 1.00 69.55  ? 504  LEU A CD1 1 
ATOM   3673  C  CD2 . LEU A  1 504 ? 35.579  13.373  -25.729 1.00 71.56  ? 504  LEU A CD2 1 
ATOM   3674  N  N   . GLU A  1 505 ? 33.587  15.609  -25.627 1.00 85.85  ? 505  GLU A N   1 
ATOM   3675  C  CA  . GLU A  1 505 ? 34.103  16.968  -25.850 1.00 90.14  ? 505  GLU A CA  1 
ATOM   3676  C  C   . GLU A  1 505 ? 32.995  17.998  -26.052 1.00 95.66  ? 505  GLU A C   1 
ATOM   3677  O  O   . GLU A  1 505 ? 32.886  18.625  -27.120 1.00 88.28  ? 505  GLU A O   1 
ATOM   3678  C  CB  . GLU A  1 505 ? 35.063  16.983  -27.041 1.00 85.82  ? 505  GLU A CB  1 
ATOM   3679  C  CG  . GLU A  1 505 ? 34.597  16.163  -28.212 1.00 85.18  ? 505  GLU A CG  1 
ATOM   3680  C  CD  . GLU A  1 505 ? 35.568  16.150  -29.338 1.00 85.91  ? 505  GLU A CD  1 
ATOM   3681  O  OE1 . GLU A  1 505 ? 36.743  15.814  -29.092 1.00 89.91  ? 505  GLU A OE1 1 
ATOM   3682  O  OE2 . GLU A  1 505 ? 35.155  16.477  -30.468 1.00 90.21  ? 505  GLU A OE2 1 
ATOM   3683  N  N   . SER A  1 506 ? 32.179  18.136  -25.005 1.00 97.19  ? 506  SER A N   1 
ATOM   3684  C  CA  . SER A  1 506 ? 30.974  18.968  -24.992 1.00 100.41 ? 506  SER A CA  1 
ATOM   3685  C  C   . SER A  1 506 ? 30.081  18.723  -26.217 1.00 96.84  ? 506  SER A C   1 
ATOM   3686  O  O   . SER A  1 506 ? 29.664  17.589  -26.466 1.00 97.25  ? 506  SER A O   1 
ATOM   3687  C  CB  . SER A  1 506 ? 31.347  20.452  -24.878 1.00 98.02  ? 506  SER A CB  1 
ATOM   3688  O  OG  . SER A  1 506 ? 31.925  20.725  -23.614 1.00 90.97  ? 506  SER A OG  1 
ATOM   3689  N  N   . ASP A  1 507 ? 29.795  19.777  -26.977 1.00 93.42  ? 507  ASP A N   1 
ATOM   3690  C  CA  . ASP A  1 507 ? 28.792  19.697  -28.035 1.00 93.16  ? 507  ASP A CA  1 
ATOM   3691  C  C   . ASP A  1 507 ? 29.186  20.380  -29.345 1.00 97.14  ? 507  ASP A C   1 
ATOM   3692  O  O   . ASP A  1 507 ? 28.894  21.568  -29.520 1.00 95.20  ? 507  ASP A O   1 
ATOM   3693  C  CB  . ASP A  1 507 ? 27.471  20.329  -27.566 1.00 86.61  ? 507  ASP A CB  1 
ATOM   3694  C  CG  . ASP A  1 507 ? 26.742  19.503  -26.521 1.00 93.86  ? 507  ASP A CG  1 
ATOM   3695  O  OD1 . ASP A  1 507 ? 27.056  18.301  -26.357 1.00 87.76  ? 507  ASP A OD1 1 
ATOM   3696  O  OD2 . ASP A  1 507 ? 25.830  20.063  -25.873 1.00 98.78  ? 507  ASP A OD2 1 
ATOM   3697  N  N   . PHE A  1 508 ? 29.847  19.694  -30.276 1.00 99.89  ? 508  PHE A N   1 
ATOM   3698  C  CA  . PHE A  1 508 ? 30.677  18.501  -30.106 1.00 93.57  ? 508  PHE A CA  1 
ATOM   3699  C  C   . PHE A  1 508 ? 32.190  18.713  -30.404 1.00 94.12  ? 508  PHE A C   1 
ATOM   3700  O  O   . PHE A  1 508 ? 32.966  17.887  -29.945 1.00 87.91  ? 508  PHE A O   1 
ATOM   3701  C  CB  . PHE A  1 508 ? 30.168  17.366  -31.010 1.00 81.61  ? 508  PHE A CB  1 
ATOM   3702  C  CG  . PHE A  1 508 ? 30.613  15.989  -30.598 1.00 87.11  ? 508  PHE A CG  1 
ATOM   3703  C  CD1 . PHE A  1 508 ? 31.785  15.431  -31.101 1.00 93.41  ? 508  PHE A CD1 1 
ATOM   3704  C  CD2 . PHE A  1 508 ? 29.836  15.228  -29.743 1.00 86.89  ? 508  PHE A CD2 1 
ATOM   3705  C  CE1 . PHE A  1 508 ? 32.188  14.148  -30.729 1.00 86.25  ? 508  PHE A CE1 1 
ATOM   3706  C  CE2 . PHE A  1 508 ? 30.230  13.951  -29.372 1.00 81.97  ? 508  PHE A CE2 1 
ATOM   3707  C  CZ  . PHE A  1 508 ? 31.405  13.410  -29.863 1.00 82.18  ? 508  PHE A CZ  1 
ATOM   3708  N  N   . THR A  1 509 ? 32.644  19.751  -31.142 1.00 91.36  ? 509  THR A N   1 
ATOM   3709  C  CA  . THR A  1 509 ? 31.829  20.843  -31.688 1.00 88.40  ? 509  THR A CA  1 
ATOM   3710  C  C   . THR A  1 509 ? 32.049  21.253  -33.140 1.00 91.86  ? 509  THR A C   1 
ATOM   3711  O  O   . THR A  1 509 ? 33.177  21.424  -33.585 1.00 89.57  ? 509  THR A O   1 
ATOM   3712  C  CB  . THR A  1 509 ? 31.985  22.105  -30.836 1.00 92.92  ? 509  THR A CB  1 
ATOM   3713  O  OG1 . THR A  1 509 ? 31.265  23.196  -31.439 1.00 100.16 ? 509  THR A OG1 1 
ATOM   3714  C  CG2 . THR A  1 509 ? 33.461  22.451  -30.682 1.00 98.55  ? 509  THR A CG2 1 
ATOM   3715  N  N   . SER A  1 510 ? 30.923  21.423  -33.843 1.00 93.96  ? 510  SER A N   1 
ATOM   3716  C  CA  . SER A  1 510 ? 30.830  21.997  -35.201 1.00 94.06  ? 510  SER A CA  1 
ATOM   3717  C  C   . SER A  1 510 ? 31.805  21.449  -36.254 1.00 82.30  ? 510  SER A C   1 
ATOM   3718  O  O   . SER A  1 510 ? 32.991  21.771  -36.249 1.00 89.40  ? 510  SER A O   1 
ATOM   3719  C  CB  . SER A  1 510 ? 31.002  23.512  -35.135 1.00 94.90  ? 510  SER A CB  1 
ATOM   3720  O  OG  . SER A  1 510 ? 31.290  24.038  -36.427 1.00 94.18  ? 510  SER A OG  1 
ATOM   3721  N  N   . GLY A  1 511 ? 31.293  20.649  -37.179 1.00 77.92  ? 511  GLY A N   1 
ATOM   3722  C  CA  . GLY A  1 511 ? 29.901  20.245  -37.168 1.00 85.86  ? 511  GLY A CA  1 
ATOM   3723  C  C   . GLY A  1 511 ? 29.808  18.874  -36.535 1.00 90.13  ? 511  GLY A C   1 
ATOM   3724  O  O   . GLY A  1 511 ? 29.418  17.896  -37.181 1.00 83.62  ? 511  GLY A O   1 
ATOM   3725  N  N   . GLY A  1 512 ? 30.190  18.808  -35.262 1.00 87.98  ? 512  GLY A N   1 
ATOM   3726  C  CA  . GLY A  1 512 ? 30.235  17.558  -34.540 1.00 84.98  ? 512  GLY A CA  1 
ATOM   3727  C  C   . GLY A  1 512 ? 28.849  16.999  -34.352 1.00 77.74  ? 512  GLY A C   1 
ATOM   3728  O  O   . GLY A  1 512 ? 27.851  17.694  -34.562 1.00 72.33  ? 512  GLY A O   1 
ATOM   3729  N  N   . VAL A  1 513 ? 28.802  15.742  -33.934 1.00 73.37  ? 513  VAL A N   1 
ATOM   3730  C  CA  . VAL A  1 513 ? 27.557  14.991  -33.826 1.00 77.54  ? 513  VAL A CA  1 
ATOM   3731  C  C   . VAL A  1 513 ? 26.428  15.695  -33.058 1.00 82.16  ? 513  VAL A C   1 
ATOM   3732  O  O   . VAL A  1 513 ? 25.259  15.633  -33.452 1.00 77.11  ? 513  VAL A O   1 
ATOM   3733  C  CB  . VAL A  1 513 ? 27.818  13.636  -33.171 1.00 77.21  ? 513  VAL A CB  1 
ATOM   3734  C  CG1 . VAL A  1 513 ? 27.100  12.601  -33.940 1.00 76.37  ? 513  VAL A CG1 1 
ATOM   3735  C  CG2 . VAL A  1 513 ? 29.308  13.319  -33.176 1.00 78.27  ? 513  VAL A CG2 1 
ATOM   3736  N  N   . CYS A  1 514 ? 26.779  16.356  -31.959 1.00 87.32  ? 514  CYS A N   1 
ATOM   3737  C  CA  . CYS A  1 514 ? 25.827  17.183  -31.221 1.00 89.50  ? 514  CYS A CA  1 
ATOM   3738  C  C   . CYS A  1 514 ? 26.410  18.592  -31.137 1.00 93.40  ? 514  CYS A C   1 
ATOM   3739  O  O   . CYS A  1 514 ? 27.619  18.737  -31.125 1.00 89.39  ? 514  CYS A O   1 
ATOM   3740  C  CB  . CYS A  1 514 ? 25.560  16.607  -29.820 1.00 94.62  ? 514  CYS A CB  1 
ATOM   3741  S  SG  . CYS A  1 514 ? 26.328  14.976  -29.455 1.00 88.13  ? 514  CYS A SG  1 
ATOM   3742  N  N   . HIS A  1 515 ? 25.583  19.635  -31.135 1.00 99.65  ? 515  HIS A N   1 
ATOM   3743  C  CA  . HIS A  1 515 ? 24.147  19.543  -31.362 1.00 102.36 ? 515  HIS A CA  1 
ATOM   3744  C  C   . HIS A  1 515 ? 23.775  20.379  -32.589 1.00 92.29  ? 515  HIS A C   1 
ATOM   3745  O  O   . HIS A  1 515 ? 23.421  19.825  -33.630 1.00 85.56  ? 515  HIS A O   1 
ATOM   3746  C  CB  . HIS A  1 515 ? 23.361  20.024  -30.131 1.00 95.39  ? 515  HIS A CB  1 
ATOM   3747  C  CG  . HIS A  1 515 ? 21.905  19.665  -30.160 1.00 101.72 ? 515  HIS A CG  1 
ATOM   3748  N  ND1 . HIS A  1 515 ? 21.423  18.565  -30.840 1.00 104.15 ? 515  HIS A ND1 1 
ATOM   3749  C  CD2 . HIS A  1 515 ? 20.826  20.257  -29.592 1.00 108.34 ? 515  HIS A CD2 1 
ATOM   3750  C  CE1 . HIS A  1 515 ? 20.111  18.495  -30.689 1.00 105.33 ? 515  HIS A CE1 1 
ATOM   3751  N  NE2 . HIS A  1 515 ? 19.724  19.511  -29.937 1.00 110.07 ? 515  HIS A NE2 1 
ATOM   3752  N  N   . SER A  1 516 ? 23.889  21.702  -32.420 1.00 92.11  ? 516  SER A N   1 
ATOM   3753  C  CA  . SER A  1 516 ? 23.491  22.758  -33.365 1.00 88.45  ? 516  SER A CA  1 
ATOM   3754  C  C   . SER A  1 516 ? 23.157  22.303  -34.779 1.00 87.47  ? 516  SER A C   1 
ATOM   3755  O  O   . SER A  1 516 ? 22.006  21.975  -35.085 1.00 82.50  ? 516  SER A O   1 
ATOM   3756  C  CB  . SER A  1 516 ? 24.600  23.815  -33.439 1.00 85.73  ? 516  SER A CB  1 
ATOM   3757  O  OG  . SER A  1 516 ? 25.855  23.212  -33.724 1.00 90.07  ? 516  SER A OG  1 
ATOM   3758  N  N   . ASP A  1 517 ? 24.177  22.293  -35.630 1.00 84.24  ? 517  ASP A N   1 
ATOM   3759  C  CA  . ASP A  1 517 ? 24.038  21.899  -37.024 1.00 83.54  ? 517  ASP A CA  1 
ATOM   3760  C  C   . ASP A  1 517 ? 25.159  20.917  -37.379 1.00 86.36  ? 517  ASP A C   1 
ATOM   3761  O  O   . ASP A  1 517 ? 26.257  21.326  -37.779 1.00 85.03  ? 517  ASP A O   1 
ATOM   3762  C  CB  . ASP A  1 517 ? 24.068  23.136  -37.928 1.00 83.72  ? 517  ASP A CB  1 
ATOM   3763  C  CG  . ASP A  1 517 ? 24.005  22.789  -39.403 1.00 82.67  ? 517  ASP A CG  1 
ATOM   3764  O  OD1 . ASP A  1 517 ? 25.084  22.589  -40.008 1.00 80.46  ? 517  ASP A OD1 1 
ATOM   3765  O  OD2 . ASP A  1 517 ? 22.881  22.721  -39.953 1.00 76.81  ? 517  ASP A OD2 1 
ATOM   3766  N  N   . PRO A  1 518 ? 24.892  19.612  -37.213 1.00 81.55  ? 518  PRO A N   1 
ATOM   3767  C  CA  . PRO A  1 518 ? 25.909  18.568  -37.391 1.00 80.10  ? 518  PRO A CA  1 
ATOM   3768  C  C   . PRO A  1 518 ? 26.122  18.164  -38.855 1.00 82.15  ? 518  PRO A C   1 
ATOM   3769  O  O   . PRO A  1 518 ? 25.199  18.261  -39.667 1.00 75.87  ? 518  PRO A O   1 
ATOM   3770  C  CB  . PRO A  1 518 ? 25.340  17.403  -36.585 1.00 77.85  ? 518  PRO A CB  1 
ATOM   3771  C  CG  . PRO A  1 518 ? 23.853  17.569  -36.711 1.00 76.64  ? 518  PRO A CG  1 
ATOM   3772  C  CD  . PRO A  1 518 ? 23.592  19.057  -36.790 1.00 77.64  ? 518  PRO A CD  1 
ATOM   3773  N  N   . LYS A  1 519 ? 27.332  17.707  -39.177 1.00 84.04  ? 519  LYS A N   1 
ATOM   3774  C  CA  . LYS A  1 519 ? 27.675  17.320  -40.547 1.00 79.35  ? 519  LYS A CA  1 
ATOM   3775  C  C   . LYS A  1 519 ? 27.380  15.848  -40.803 1.00 73.83  ? 519  LYS A C   1 
ATOM   3776  O  O   . LYS A  1 519 ? 27.804  14.978  -40.047 1.00 73.67  ? 519  LYS A O   1 
ATOM   3777  C  CB  . LYS A  1 519 ? 29.152  17.624  -40.848 1.00 72.65  ? 519  LYS A CB  1 
ATOM   3778  C  CG  . LYS A  1 519 ? 29.350  18.824  -41.770 1.00 77.40  ? 519  LYS A CG  1 
ATOM   3779  C  CD  . LYS A  1 519 ? 28.383  19.946  -41.402 1.00 79.50  ? 519  LYS A CD  1 
ATOM   3780  C  CE  . LYS A  1 519 ? 28.483  21.132  -42.353 1.00 86.73  ? 519  LYS A CE  1 
ATOM   3781  N  NZ  . LYS A  1 519 ? 27.468  22.196  -42.041 1.00 80.76  ? 519  LYS A NZ  1 
ATOM   3782  N  N   . MET A  1 520 ? 26.654  15.569  -41.876 1.00 71.91  ? 520  MET A N   1 
ATOM   3783  C  CA  . MET A  1 520 ? 26.307  14.193  -42.191 1.00 66.31  ? 520  MET A CA  1 
ATOM   3784  C  C   . MET A  1 520 ? 27.514  13.411  -42.693 1.00 66.39  ? 520  MET A C   1 
ATOM   3785  O  O   . MET A  1 520 ? 27.940  13.558  -43.832 1.00 70.39  ? 520  MET A O   1 
ATOM   3786  C  CB  . MET A  1 520 ? 25.184  14.179  -43.203 1.00 64.99  ? 520  MET A CB  1 
ATOM   3787  C  CG  . MET A  1 520 ? 24.205  15.278  -42.926 1.00 62.70  ? 520  MET A CG  1 
ATOM   3788  S  SD  . MET A  1 520 ? 22.663  15.046  -43.793 1.00 66.11  ? 520  MET A SD  1 
ATOM   3789  C  CE  . MET A  1 520 ? 22.128  16.731  -43.747 1.00 67.95  ? 520  MET A CE  1 
ATOM   3790  N  N   . THR A  1 521 ? 28.049  12.574  -41.814 1.00 67.27  ? 521  THR A N   1 
ATOM   3791  C  CA  . THR A  1 521 ? 29.289  11.848  -42.048 1.00 65.54  ? 521  THR A CA  1 
ATOM   3792  C  C   . THR A  1 521 ? 29.013  10.372  -41.839 1.00 63.30  ? 521  THR A C   1 
ATOM   3793  O  O   . THR A  1 521 ? 27.989  10.018  -41.263 1.00 67.26  ? 521  THR A O   1 
ATOM   3794  C  CB  . THR A  1 521 ? 30.392  12.353  -41.092 1.00 65.96  ? 521  THR A CB  1 
ATOM   3795  O  OG1 . THR A  1 521 ? 30.517  13.769  -41.252 1.00 71.62  ? 521  THR A OG1 1 
ATOM   3796  C  CG2 . THR A  1 521 ? 31.748  11.708  -41.357 1.00 66.55  ? 521  THR A CG2 1 
ATOM   3797  N  N   . SER A  1 522 ? 29.892  9.506   -42.327 1.00 62.57  ? 522  SER A N   1 
ATOM   3798  C  CA  . SER A  1 522 ? 29.799  8.096   -41.981 1.00 68.23  ? 522  SER A CA  1 
ATOM   3799  C  C   . SER A  1 522 ? 30.038  7.961   -40.476 1.00 64.50  ? 522  SER A C   1 
ATOM   3800  O  O   . SER A  1 522 ? 29.439  7.119   -39.808 1.00 61.15  ? 522  SER A O   1 
ATOM   3801  C  CB  . SER A  1 522 ? 30.805  7.262   -42.779 1.00 67.73  ? 522  SER A CB  1 
ATOM   3802  O  OG  . SER A  1 522 ? 32.131  7.648   -42.479 1.00 65.54  ? 522  SER A OG  1 
ATOM   3803  N  N   . ASN A  1 523 ? 30.919  8.813   -39.962 1.00 66.58  ? 523  ASN A N   1 
ATOM   3804  C  CA  . ASN A  1 523 ? 31.167  8.931   -38.533 1.00 69.97  ? 523  ASN A CA  1 
ATOM   3805  C  C   . ASN A  1 523 ? 29.871  9.233   -37.751 1.00 67.52  ? 523  ASN A C   1 
ATOM   3806  O  O   . ASN A  1 523 ? 29.602  8.608   -36.724 1.00 63.88  ? 523  ASN A O   1 
ATOM   3807  C  CB  . ASN A  1 523 ? 32.217  10.017  -38.285 1.00 66.82  ? 523  ASN A CB  1 
ATOM   3808  C  CG  . ASN A  1 523 ? 32.998  9.801   -37.005 1.00 88.19  ? 523  ASN A CG  1 
ATOM   3809  O  OD1 . ASN A  1 523 ? 32.578  9.057   -36.106 1.00 89.64  ? 523  ASN A OD1 1 
ATOM   3810  N  ND2 . ASN A  1 523 ? 34.148  10.461  -36.911 1.00 94.39  ? 523  ASN A ND2 1 
ATOM   3811  N  N   . MET A  1 524 ? 29.074  10.179  -38.248 1.00 61.83  ? 524  MET A N   1 
ATOM   3812  C  CA  . MET A  1 524 ? 27.770  10.484  -37.666 1.00 55.74  ? 524  MET A CA  1 
ATOM   3813  C  C   . MET A  1 524 ? 26.849  9.263   -37.632 1.00 60.84  ? 524  MET A C   1 
ATOM   3814  O  O   . MET A  1 524 ? 26.216  8.988   -36.617 1.00 62.91  ? 524  MET A O   1 
ATOM   3815  C  CB  . MET A  1 524 ? 27.101  11.615  -38.443 1.00 58.42  ? 524  MET A CB  1 
ATOM   3816  C  CG  . MET A  1 524 ? 25.593  11.658  -38.305 1.00 57.37  ? 524  MET A CG  1 
ATOM   3817  S  SD  . MET A  1 524 ? 25.063  11.996  -36.614 1.00 76.17  ? 524  MET A SD  1 
ATOM   3818  C  CE  . MET A  1 524 ? 24.957  13.779  -36.581 1.00 55.76  ? 524  MET A CE  1 
ATOM   3819  N  N   . LEU A  1 525 ? 26.774  8.537   -38.744 1.00 59.95  ? 525  LEU A N   1 
ATOM   3820  C  CA  . LEU A  1 525 ? 25.947  7.332   -38.834 1.00 59.03  ? 525  LEU A CA  1 
ATOM   3821  C  C   . LEU A  1 525 ? 26.432  6.286   -37.851 1.00 54.64  ? 525  LEU A C   1 
ATOM   3822  O  O   . LEU A  1 525 ? 25.639  5.536   -37.273 1.00 55.43  ? 525  LEU A O   1 
ATOM   3823  C  CB  . LEU A  1 525 ? 25.976  6.760   -40.261 1.00 61.32  ? 525  LEU A CB  1 
ATOM   3824  C  CG  . LEU A  1 525 ? 25.179  5.492   -40.592 1.00 53.19  ? 525  LEU A CG  1 
ATOM   3825  C  CD1 . LEU A  1 525 ? 23.682  5.783   -40.725 1.00 48.81  ? 525  LEU A CD1 1 
ATOM   3826  C  CD2 . LEU A  1 525 ? 25.727  4.836   -41.857 1.00 50.13  ? 525  LEU A CD2 1 
ATOM   3827  N  N   . ALA A  1 526 ? 27.749  6.255   -37.674 1.00 52.33  ? 526  ALA A N   1 
ATOM   3828  C  CA  . ALA A  1 526 ? 28.404  5.327   -36.773 1.00 54.97  ? 526  ALA A CA  1 
ATOM   3829  C  C   . ALA A  1 526 ? 27.996  5.617   -35.325 1.00 61.27  ? 526  ALA A C   1 
ATOM   3830  O  O   . ALA A  1 526 ? 27.624  4.712   -34.563 1.00 56.46  ? 526  ALA A O   1 
ATOM   3831  C  CB  . ALA A  1 526 ? 29.909  5.424   -36.940 1.00 46.60  ? 526  ALA A CB  1 
ATOM   3832  N  N   . PHE A  1 527 ? 28.075  6.898   -34.975 1.00 57.42  ? 527  PHE A N   1 
ATOM   3833  C  CA  . PHE A  1 527 ? 27.651  7.421   -33.690 1.00 54.85  ? 527  PHE A CA  1 
ATOM   3834  C  C   . PHE A  1 527 ? 26.222  7.007   -33.364 1.00 56.51  ? 527  PHE A C   1 
ATOM   3835  O  O   . PHE A  1 527 ? 25.970  6.422   -32.314 1.00 50.94  ? 527  PHE A O   1 
ATOM   3836  C  CB  . PHE A  1 527 ? 27.775  8.946   -33.690 1.00 50.35  ? 527  PHE A CB  1 
ATOM   3837  C  CG  . PHE A  1 527 ? 27.348  9.596   -32.406 1.00 62.85  ? 527  PHE A CG  1 
ATOM   3838  C  CD1 . PHE A  1 527 ? 28.217  9.668   -31.329 1.00 59.97  ? 527  PHE A CD1 1 
ATOM   3839  C  CD2 . PHE A  1 527 ? 26.076  10.142  -32.272 1.00 65.44  ? 527  PHE A CD2 1 
ATOM   3840  C  CE1 . PHE A  1 527 ? 27.829  10.278  -30.152 1.00 62.04  ? 527  PHE A CE1 1 
ATOM   3841  C  CE2 . PHE A  1 527 ? 25.687  10.773  -31.097 1.00 59.99  ? 527  PHE A CE2 1 
ATOM   3842  C  CZ  . PHE A  1 527 ? 26.558  10.834  -30.038 1.00 63.62  ? 527  PHE A CZ  1 
ATOM   3843  N  N   . LEU A  1 528 ? 25.302  7.295   -34.283 1.00 56.13  ? 528  LEU A N   1 
ATOM   3844  C  CA  . LEU A  1 528 ? 23.875  7.038   -34.077 1.00 58.10  ? 528  LEU A CA  1 
ATOM   3845  C  C   . LEU A  1 528 ? 23.550  5.571   -33.813 1.00 55.76  ? 528  LEU A C   1 
ATOM   3846  O  O   . LEU A  1 528 ? 22.646  5.251   -33.044 1.00 54.89  ? 528  LEU A O   1 
ATOM   3847  C  CB  . LEU A  1 528 ? 23.075  7.517   -35.291 1.00 59.95  ? 528  LEU A CB  1 
ATOM   3848  C  CG  . LEU A  1 528 ? 23.057  9.027   -35.555 1.00 65.40  ? 528  LEU A CG  1 
ATOM   3849  C  CD1 . LEU A  1 528 ? 22.422  9.329   -36.902 1.00 59.86  ? 528  LEU A CD1 1 
ATOM   3850  C  CD2 . LEU A  1 528 ? 22.313  9.757   -34.437 1.00 56.35  ? 528  LEU A CD2 1 
ATOM   3851  N  N   . GLY A  1 529 ? 24.292  4.681   -34.457 1.00 56.87  ? 529  GLY A N   1 
ATOM   3852  C  CA  . GLY A  1 529 ? 23.981  3.270   -34.391 1.00 49.58  ? 529  GLY A CA  1 
ATOM   3853  C  C   . GLY A  1 529 ? 24.670  2.619   -33.225 1.00 48.76  ? 529  GLY A C   1 
ATOM   3854  O  O   . GLY A  1 529 ? 24.109  1.734   -32.584 1.00 51.08  ? 529  GLY A O   1 
ATOM   3855  N  N   . GLU A  1 530 ? 25.896  3.050   -32.955 1.00 51.20  ? 530  GLU A N   1 
ATOM   3856  C  CA  . GLU A  1 530 ? 26.583  2.658   -31.732 1.00 50.88  ? 530  GLU A CA  1 
ATOM   3857  C  C   . GLU A  1 530 ? 25.753  3.063   -30.490 1.00 54.66  ? 530  GLU A C   1 
ATOM   3858  O  O   . GLU A  1 530 ? 25.650  2.306   -29.518 1.00 53.19  ? 530  GLU A O   1 
ATOM   3859  C  CB  . GLU A  1 530 ? 27.979  3.281   -31.686 1.00 50.69  ? 530  GLU A CB  1 
ATOM   3860  C  CG  . GLU A  1 530 ? 29.048  2.365   -32.256 1.00 57.30  ? 530  GLU A CG  1 
ATOM   3861  C  CD  . GLU A  1 530 ? 30.206  3.112   -32.905 1.00 73.98  ? 530  GLU A CD  1 
ATOM   3862  O  OE1 . GLU A  1 530 ? 30.413  4.307   -32.595 1.00 67.69  ? 530  GLU A OE1 1 
ATOM   3863  O  OE2 . GLU A  1 530 ? 30.908  2.494   -33.740 1.00 79.58  ? 530  GLU A OE2 1 
ATOM   3864  N  N   . ASN A  1 531 ? 25.146  4.245   -30.538 1.00 50.30  ? 531  ASN A N   1 
ATOM   3865  C  CA  . ASN A  1 531 ? 24.245  4.674   -29.484 1.00 44.90  ? 531  ASN A CA  1 
ATOM   3866  C  C   . ASN A  1 531 ? 23.097  3.709   -29.287 1.00 48.68  ? 531  ASN A C   1 
ATOM   3867  O  O   . ASN A  1 531 ? 22.854  3.244   -28.165 1.00 45.04  ? 531  ASN A O   1 
ATOM   3868  C  CB  . ASN A  1 531 ? 23.702  6.059   -29.779 1.00 42.91  ? 531  ASN A CB  1 
ATOM   3869  C  CG  . ASN A  1 531 ? 24.742  7.129   -29.597 1.00 49.34  ? 531  ASN A CG  1 
ATOM   3870  O  OD1 . ASN A  1 531 ? 25.894  6.851   -29.229 1.00 44.50  ? 531  ASN A OD1 1 
ATOM   3871  N  ND2 . ASN A  1 531 ? 24.350  8.363   -29.843 1.00 45.51  ? 531  ASN A ND2 1 
ATOM   3872  N  N   . ALA A  1 532 ? 22.390  3.406   -30.370 1.00 44.97  ? 532  ALA A N   1 
ATOM   3873  C  CA  . ALA A  1 532 ? 21.245  2.510   -30.284 1.00 47.11  ? 532  ALA A CA  1 
ATOM   3874  C  C   . ALA A  1 532 ? 21.663  1.105   -29.820 1.00 48.20  ? 532  ALA A C   1 
ATOM   3875  O  O   . ALA A  1 532 ? 20.879  0.394   -29.197 1.00 43.16  ? 532  ALA A O   1 
ATOM   3876  C  CB  . ALA A  1 532 ? 20.535  2.439   -31.610 1.00 46.42  ? 532  ALA A CB  1 
ATOM   3877  N  N   . GLU A  1 533 ? 22.898  0.717   -30.122 1.00 47.37  ? 533  GLU A N   1 
ATOM   3878  C  CA  A GLU A  1 533 ? 23.470  -0.565  -29.726 0.52 48.17  ? 533  GLU A CA  1 
ATOM   3879  C  CA  B GLU A  1 533 ? 23.338  -0.614  -29.705 0.48 48.17  ? 533  GLU A CA  1 
ATOM   3880  C  C   . GLU A  1 533 ? 23.573  -0.635  -28.204 1.00 49.11  ? 533  GLU A C   1 
ATOM   3881  O  O   . GLU A  1 533 ? 23.214  -1.624  -27.553 1.00 50.78  ? 533  GLU A O   1 
ATOM   3882  C  CB  A GLU A  1 533 ? 24.851  -0.715  -30.380 0.52 49.30  ? 533  GLU A CB  1 
ATOM   3883  C  CB  B GLU A  1 533 ? 24.592  -1.077  -30.455 0.48 49.20  ? 533  GLU A CB  1 
ATOM   3884  C  CG  A GLU A  1 533 ? 25.520  -2.072  -30.290 0.52 53.19  ? 533  GLU A CG  1 
ATOM   3885  C  CG  B GLU A  1 533 ? 25.321  -2.296  -29.828 0.48 53.61  ? 533  GLU A CG  1 
ATOM   3886  C  CD  A GLU A  1 533 ? 26.924  -2.057  -30.887 0.52 51.23  ? 533  GLU A CD  1 
ATOM   3887  C  CD  B GLU A  1 533 ? 24.417  -3.499  -29.503 0.48 50.71  ? 533  GLU A CD  1 
ATOM   3888  O  OE1 A GLU A  1 533 ? 27.715  -1.143  -30.552 0.52 48.47  ? 533  GLU A OE1 1 
ATOM   3889  O  OE1 B GLU A  1 533 ? 23.376  -3.693  -30.167 0.48 50.87  ? 533  GLU A OE1 1 
ATOM   3890  O  OE2 A GLU A  1 533 ? 27.234  -2.964  -31.686 0.52 52.18  ? 533  GLU A OE2 1 
ATOM   3891  O  OE2 B GLU A  1 533 ? 24.757  -4.252  -28.566 0.48 44.52  ? 533  GLU A OE2 1 
ATOM   3892  N  N   . VAL A  1 534 ? 24.100  0.448   -27.648 1.00 48.10  ? 534  VAL A N   1 
ATOM   3893  C  CA  . VAL A  1 534 ? 24.311  0.538   -26.216 1.00 38.88  ? 534  VAL A CA  1 
ATOM   3894  C  C   . VAL A  1 534 ? 22.963  0.541   -25.507 1.00 39.39  ? 534  VAL A C   1 
ATOM   3895  O  O   . VAL A  1 534 ? 22.798  -0.119  -24.492 1.00 46.03  ? 534  VAL A O   1 
ATOM   3896  C  CB  . VAL A  1 534 ? 25.153  1.767   -25.867 1.00 41.28  ? 534  VAL A CB  1 
ATOM   3897  C  CG1 . VAL A  1 534 ? 24.972  2.173   -24.410 1.00 38.71  ? 534  VAL A CG1 1 
ATOM   3898  C  CG2 . VAL A  1 534 ? 26.627  1.478   -26.172 1.00 35.28  ? 534  VAL A CG2 1 
ATOM   3899  N  N   . LYS A  1 535 ? 21.977  1.217   -26.068 1.00 40.42  ? 535  LYS A N   1 
ATOM   3900  C  CA  . LYS A  1 535 ? 20.651  1.184   -25.474 1.00 42.74  ? 535  LYS A CA  1 
ATOM   3901  C  C   . LYS A  1 535 ? 20.062  -0.233  -25.432 1.00 49.67  ? 535  LYS A C   1 
ATOM   3902  O  O   . LYS A  1 535 ? 19.499  -0.648  -24.415 1.00 53.50  ? 535  LYS A O   1 
ATOM   3903  C  CB  . LYS A  1 535 ? 19.709  2.117   -26.224 1.00 38.99  ? 535  LYS A CB  1 
ATOM   3904  C  CG  . LYS A  1 535 ? 18.244  1.948   -25.866 1.00 47.09  ? 535  LYS A CG  1 
ATOM   3905  C  CD  . LYS A  1 535 ? 17.583  3.301   -25.643 1.00 55.55  ? 535  LYS A CD  1 
ATOM   3906  C  CE  . LYS A  1 535 ? 16.063  3.201   -25.684 1.00 62.10  ? 535  LYS A CE  1 
ATOM   3907  N  NZ  . LYS A  1 535 ? 15.450  4.535   -25.939 1.00 65.03  ? 535  LYS A NZ  1 
ATOM   3908  N  N   . GLU A  1 536 ? 20.191  -0.982  -26.520 1.00 46.60  ? 536  GLU A N   1 
ATOM   3909  C  CA  . GLU A  1 536 ? 19.595  -2.313  -26.562 1.00 55.78  ? 536  GLU A CA  1 
ATOM   3910  C  C   . GLU A  1 536 ? 20.301  -3.229  -25.564 1.00 53.09  ? 536  GLU A C   1 
ATOM   3911  O  O   . GLU A  1 536 ? 19.670  -3.993  -24.848 1.00 51.34  ? 536  GLU A O   1 
ATOM   3912  C  CB  . GLU A  1 536 ? 19.652  -2.904  -27.976 1.00 53.32  ? 536  GLU A CB  1 
ATOM   3913  C  CG  . GLU A  1 536 ? 18.445  -3.799  -28.340 1.00 68.08  ? 536  GLU A CG  1 
ATOM   3914  C  CD  . GLU A  1 536 ? 17.101  -3.038  -28.468 1.00 76.61  ? 536  GLU A CD  1 
ATOM   3915  O  OE1 . GLU A  1 536 ? 17.086  -1.781  -28.428 1.00 64.88  ? 536  GLU A OE1 1 
ATOM   3916  O  OE2 . GLU A  1 536 ? 16.048  -3.708  -28.615 1.00 75.95  ? 536  GLU A OE2 1 
ATOM   3917  N  N   . MET A  1 537 ? 21.618  -3.113  -25.508 1.00 49.07  ? 537  MET A N   1 
ATOM   3918  C  CA  . MET A  1 537 ? 22.433  -3.927  -24.625 1.00 43.96  ? 537  MET A CA  1 
ATOM   3919  C  C   . MET A  1 537 ? 22.085  -3.785  -23.131 1.00 50.06  ? 537  MET A C   1 
ATOM   3920  O  O   . MET A  1 537 ? 21.944  -4.785  -22.411 1.00 42.47  ? 537  MET A O   1 
ATOM   3921  C  CB  . MET A  1 537 ? 23.886  -3.555  -24.845 1.00 39.82  ? 537  MET A CB  1 
ATOM   3922  C  CG  . MET A  1 537 ? 24.821  -4.217  -23.911 1.00 40.90  ? 537  MET A CG  1 
ATOM   3923  S  SD  . MET A  1 537 ? 26.442  -3.554  -24.229 1.00 49.89  ? 537  MET A SD  1 
ATOM   3924  C  CE  . MET A  1 537 ? 27.283  -5.059  -24.649 1.00 45.95  ? 537  MET A CE  1 
ATOM   3925  N  N   . MET A  1 538 ? 21.960  -2.534  -22.684 1.00 43.50  ? 538  MET A N   1 
ATOM   3926  C  CA  . MET A  1 538 ? 21.775  -2.228  -21.280 1.00 42.68  ? 538  MET A CA  1 
ATOM   3927  C  C   . MET A  1 538 ? 20.371  -2.552  -20.804 1.00 48.58  ? 538  MET A C   1 
ATOM   3928  O  O   . MET A  1 538 ? 20.172  -2.888  -19.635 1.00 49.10  ? 538  MET A O   1 
ATOM   3929  C  CB  . MET A  1 538 ? 22.095  -0.754  -20.997 1.00 40.59  ? 538  MET A CB  1 
ATOM   3930  C  CG  . MET A  1 538 ? 23.572  -0.371  -21.189 1.00 34.68  ? 538  MET A CG  1 
ATOM   3931  S  SD  . MET A  1 538 ? 24.738  -1.634  -20.590 1.00 43.06  ? 538  MET A SD  1 
ATOM   3932  C  CE  . MET A  1 538 ? 24.227  -1.791  -18.867 1.00 37.70  ? 538  MET A CE  1 
ATOM   3933  N  N   . THR A  1 539 ? 19.387  -2.466  -21.687 1.00 50.20  ? 539  THR A N   1 
ATOM   3934  C  CA  . THR A  1 539 ? 18.042  -2.781  -21.239 1.00 49.99  ? 539  THR A CA  1 
ATOM   3935  C  C   . THR A  1 539 ? 17.955  -4.281  -20.940 1.00 50.45  ? 539  THR A C   1 
ATOM   3936  O  O   . THR A  1 539 ? 17.240  -4.686  -20.017 1.00 51.96  ? 539  THR A O   1 
ATOM   3937  C  CB  . THR A  1 539 ? 16.951  -2.358  -22.258 1.00 51.41  ? 539  THR A CB  1 
ATOM   3938  O  OG1 . THR A  1 539 ? 17.105  -3.101  -23.471 1.00 65.14  ? 539  THR A OG1 1 
ATOM   3939  C  CG2 . THR A  1 539 ? 17.037  -0.866  -22.555 1.00 49.43  ? 539  THR A CG2 1 
ATOM   3940  N  N   . THR A  1 540 ? 18.694  -5.113  -21.676 1.00 49.03  ? 540  THR A N   1 
ATOM   3941  C  CA  . THR A  1 540 ? 18.649  -6.544  -21.369 1.00 46.49  ? 540  THR A CA  1 
ATOM   3942  C  C   . THR A  1 540 ? 19.431  -6.865  -20.074 1.00 46.27  ? 540  THR A C   1 
ATOM   3943  O  O   . THR A  1 540 ? 19.236  -7.916  -19.471 1.00 48.98  ? 540  THR A O   1 
ATOM   3944  C  CB  . THR A  1 540 ? 19.191  -7.431  -22.536 1.00 46.53  ? 540  THR A CB  1 
ATOM   3945  O  OG1 . THR A  1 540 ? 20.616  -7.567  -22.451 1.00 45.20  ? 540  THR A OG1 1 
ATOM   3946  C  CG2 . THR A  1 540 ? 18.806  -6.861  -23.893 1.00 48.91  ? 540  THR A CG2 1 
ATOM   3947  N  N   . TRP A  1 541 ? 20.318  -5.975  -19.642 1.00 41.77  ? 541  TRP A N   1 
ATOM   3948  C  CA  . TRP A  1 541 ? 21.010  -6.214  -18.386 1.00 42.76  ? 541  TRP A CA  1 
ATOM   3949  C  C   . TRP A  1 541 ? 20.098  -5.869  -17.208 1.00 41.13  ? 541  TRP A C   1 
ATOM   3950  O  O   . TRP A  1 541 ? 20.348  -6.283  -16.087 1.00 35.40  ? 541  TRP A O   1 
ATOM   3951  C  CB  . TRP A  1 541 ? 22.306  -5.410  -18.307 1.00 41.91  ? 541  TRP A CB  1 
ATOM   3952  C  CG  . TRP A  1 541 ? 23.438  -6.044  -19.039 1.00 42.12  ? 541  TRP A CG  1 
ATOM   3953  C  CD1 . TRP A  1 541 ? 23.997  -5.626  -20.215 1.00 38.45  ? 541  TRP A CD1 1 
ATOM   3954  C  CD2 . TRP A  1 541 ? 24.161  -7.212  -18.647 1.00 36.09  ? 541  TRP A CD2 1 
ATOM   3955  N  NE1 . TRP A  1 541 ? 25.023  -6.463  -20.575 1.00 33.11  ? 541  TRP A NE1 1 
ATOM   3956  C  CE2 . TRP A  1 541 ? 25.145  -7.444  -19.630 1.00 37.86  ? 541  TRP A CE2 1 
ATOM   3957  C  CE3 . TRP A  1 541 ? 24.089  -8.068  -17.555 1.00 38.00  ? 541  TRP A CE3 1 
ATOM   3958  C  CZ2 . TRP A  1 541 ? 26.040  -8.519  -19.561 1.00 37.42  ? 541  TRP A CZ2 1 
ATOM   3959  C  CZ3 . TRP A  1 541 ? 24.984  -9.140  -17.488 1.00 46.33  ? 541  TRP A CZ3 1 
ATOM   3960  C  CH2 . TRP A  1 541 ? 25.941  -9.354  -18.496 1.00 38.59  ? 541  TRP A CH2 1 
ATOM   3961  N  N   . THR A  1 542 ? 19.030  -5.125  -17.473 1.00 43.58  ? 542  THR A N   1 
ATOM   3962  C  CA  . THR A  1 542 ? 18.150  -4.679  -16.407 1.00 42.37  ? 542  THR A CA  1 
ATOM   3963  C  C   . THR A  1 542 ? 16.835  -5.422  -16.388 1.00 43.37  ? 542  THR A C   1 
ATOM   3964  O  O   . THR A  1 542 ? 16.133  -5.407  -15.383 1.00 48.82  ? 542  THR A O   1 
ATOM   3965  C  CB  . THR A  1 542 ? 17.853  -3.157  -16.489 1.00 46.57  ? 542  THR A CB  1 
ATOM   3966  O  OG1 . THR A  1 542 ? 17.148  -2.852  -17.698 1.00 48.28  ? 542  THR A OG1 1 
ATOM   3967  C  CG2 . THR A  1 542 ? 19.148  -2.344  -16.427 1.00 43.07  ? 542  THR A CG2 1 
ATOM   3968  N  N   . LEU A  1 543 ? 16.484  -6.093  -17.471 1.00 43.62  ? 543  LEU A N   1 
ATOM   3969  C  CA  . LEU A  1 543 ? 15.200  -6.784  -17.469 1.00 45.16  ? 543  LEU A CA  1 
ATOM   3970  C  C   . LEU A  1 543 ? 15.378  -8.294  -17.372 1.00 46.82  ? 543  LEU A C   1 
ATOM   3971  O  O   . LEU A  1 543 ? 14.450  -9.003  -17.005 1.00 45.00  ? 543  LEU A O   1 
ATOM   3972  C  CB  . LEU A  1 543 ? 14.385  -6.404  -18.706 1.00 46.52  ? 543  LEU A CB  1 
ATOM   3973  C  CG  . LEU A  1 543 ? 14.116  -4.896  -18.804 1.00 49.86  ? 543  LEU A CG  1 
ATOM   3974  C  CD1 . LEU A  1 543 ? 13.052  -4.608  -19.818 1.00 51.39  ? 543  LEU A CD1 1 
ATOM   3975  C  CD2 . LEU A  1 543 ? 13.714  -4.303  -17.462 1.00 49.17  ? 543  LEU A CD2 1 
ATOM   3976  N  N   . GLN A  1 544 ? 16.572  -8.784  -17.691 1.00 45.20  ? 544  GLN A N   1 
ATOM   3977  C  CA  . GLN A  1 544 ? 16.899  -10.191 -17.453 1.00 52.88  ? 544  GLN A CA  1 
ATOM   3978  C  C   . GLN A  1 544 ? 17.475  -10.424 -16.055 1.00 43.89  ? 544  GLN A C   1 
ATOM   3979  O  O   . GLN A  1 544 ? 18.463  -9.793  -15.667 1.00 41.70  ? 544  GLN A O   1 
ATOM   3980  C  CB  . GLN A  1 544 ? 17.920  -10.704 -18.469 1.00 45.33  ? 544  GLN A CB  1 
ATOM   3981  C  CG  . GLN A  1 544 ? 17.454  -10.818 -19.877 1.00 47.61  ? 544  GLN A CG  1 
ATOM   3982  C  CD  . GLN A  1 544 ? 18.269  -11.844 -20.624 1.00 46.73  ? 544  GLN A CD  1 
ATOM   3983  O  OE1 . GLN A  1 544 ? 17.726  -12.802 -21.148 1.00 57.09  ? 544  GLN A OE1 1 
ATOM   3984  N  NE2 . GLN A  1 544 ? 19.580  -11.666 -20.650 1.00 44.48  ? 544  GLN A NE2 1 
ATOM   3985  N  N   . LYS A  1 545 ? 16.897  -11.348 -15.308 1.00 40.40  ? 545  LYS A N   1 
ATOM   3986  C  CA  . LYS A  1 545 ? 17.564  -11.787 -14.082 1.00 40.01  ? 545  LYS A CA  1 
ATOM   3987  C  C   . LYS A  1 545 ? 18.812  -12.582 -14.439 1.00 44.22  ? 545  LYS A C   1 
ATOM   3988  O  O   . LYS A  1 545 ? 18.943  -13.084 -15.552 1.00 49.05  ? 545  LYS A O   1 
ATOM   3989  C  CB  . LYS A  1 545 ? 16.654  -12.656 -13.227 1.00 43.24  ? 545  LYS A CB  1 
ATOM   3990  C  CG  . LYS A  1 545 ? 16.445  -14.044 -13.806 1.00 49.65  ? 545  LYS A CG  1 
ATOM   3991  C  CD  . LYS A  1 545 ? 16.012  -15.076 -12.756 1.00 54.43  ? 545  LYS A CD  1 
ATOM   3992  C  CE  . LYS A  1 545 ? 14.532  -14.994 -12.461 1.00 55.50  ? 545  LYS A CE  1 
ATOM   3993  N  NZ  . LYS A  1 545 ? 13.980  -16.303 -12.023 1.00 52.61  ? 545  LYS A NZ  1 
ATOM   3994  N  N   . GLY A  1 546 ? 19.735  -12.698 -13.501 1.00 41.88  ? 546  GLY A N   1 
ATOM   3995  C  CA  . GLY A  1 546 ? 20.870  -13.572 -13.692 1.00 34.12  ? 546  GLY A CA  1 
ATOM   3996  C  C   . GLY A  1 546 ? 22.136  -12.946 -14.224 1.00 34.14  ? 546  GLY A C   1 
ATOM   3997  O  O   . GLY A  1 546 ? 22.163  -11.811 -14.681 1.00 37.67  ? 546  GLY A O   1 
ATOM   3998  N  N   . ILE A  1 547 ? 23.199  -13.725 -14.138 1.00 35.84  ? 547  ILE A N   1 
ATOM   3999  C  CA  . ILE A  1 547 ? 24.502  -13.384 -14.671 1.00 37.78  ? 547  ILE A CA  1 
ATOM   4000  C  C   . ILE A  1 547 ? 24.913  -14.442 -15.705 1.00 43.21  ? 547  ILE A C   1 
ATOM   4001  O  O   . ILE A  1 547 ? 24.610  -15.629 -15.542 1.00 43.35  ? 547  ILE A O   1 
ATOM   4002  C  CB  . ILE A  1 547 ? 25.528  -13.310 -13.530 1.00 36.83  ? 547  ILE A CB  1 
ATOM   4003  C  CG1 . ILE A  1 547 ? 26.937  -13.116 -14.058 1.00 35.37  ? 547  ILE A CG1 1 
ATOM   4004  C  CG2 . ILE A  1 547 ? 25.458  -14.563 -12.700 1.00 36.69  ? 547  ILE A CG2 1 
ATOM   4005  C  CD1 . ILE A  1 547 ? 27.715  -12.079 -13.292 1.00 38.08  ? 547  ILE A CD1 1 
ATOM   4006  N  N   . PRO A  1 548 ? 25.564  -14.025 -16.798 1.00 43.58  ? 548  PRO A N   1 
ATOM   4007  C  CA  . PRO A  1 548 ? 25.984  -15.023 -17.790 1.00 38.03  ? 548  PRO A CA  1 
ATOM   4008  C  C   . PRO A  1 548 ? 27.358  -15.669 -17.543 1.00 39.09  ? 548  PRO A C   1 
ATOM   4009  O  O   . PRO A  1 548 ? 28.283  -15.026 -17.066 1.00 40.08  ? 548  PRO A O   1 
ATOM   4010  C  CB  . PRO A  1 548 ? 26.008  -14.215 -19.089 1.00 40.88  ? 548  PRO A CB  1 
ATOM   4011  C  CG  . PRO A  1 548 ? 26.288  -12.837 -18.675 1.00 33.82  ? 548  PRO A CG  1 
ATOM   4012  C  CD  . PRO A  1 548 ? 25.623  -12.656 -17.333 1.00 41.49  ? 548  PRO A CD  1 
ATOM   4013  N  N   . LEU A  1 549 ? 27.483  -16.951 -17.873 1.00 42.01  ? 549  LEU A N   1 
ATOM   4014  C  CA  . LEU A  1 549 ? 28.786  -17.604 -17.949 1.00 34.02  ? 549  LEU A CA  1 
ATOM   4015  C  C   . LEU A  1 549 ? 29.268  -17.586 -19.397 1.00 47.40  ? 549  LEU A C   1 
ATOM   4016  O  O   . LEU A  1 549 ? 28.531  -17.990 -20.313 1.00 46.00  ? 549  LEU A O   1 
ATOM   4017  C  CB  . LEU A  1 549 ? 28.705  -19.045 -17.439 1.00 39.65  ? 549  LEU A CB  1 
ATOM   4018  C  CG  . LEU A  1 549 ? 29.887  -19.988 -17.692 1.00 39.46  ? 549  LEU A CG  1 
ATOM   4019  C  CD1 . LEU A  1 549 ? 31.124  -19.492 -16.959 1.00 33.72  ? 549  LEU A CD1 1 
ATOM   4020  C  CD2 . LEU A  1 549 ? 29.558  -21.412 -17.274 1.00 40.38  ? 549  LEU A CD2 1 
ATOM   4021  N  N   . LEU A  1 550 ? 30.495  -17.113 -19.594 1.00 40.25  ? 550  LEU A N   1 
ATOM   4022  C  CA  . LEU A  1 550 ? 31.133  -17.100 -20.894 1.00 36.70  ? 550  LEU A CA  1 
ATOM   4023  C  C   . LEU A  1 550 ? 32.110  -18.260 -20.966 1.00 46.12  ? 550  LEU A C   1 
ATOM   4024  O  O   . LEU A  1 550 ? 33.138  -18.260 -20.267 1.00 41.51  ? 550  LEU A O   1 
ATOM   4025  C  CB  . LEU A  1 550 ? 31.872  -15.792 -21.122 1.00 38.62  ? 550  LEU A CB  1 
ATOM   4026  C  CG  . LEU A  1 550 ? 32.788  -15.751 -22.354 1.00 45.94  ? 550  LEU A CG  1 
ATOM   4027  C  CD1 . LEU A  1 550 ? 32.010  -15.508 -23.633 1.00 48.64  ? 550  LEU A CD1 1 
ATOM   4028  C  CD2 . LEU A  1 550 ? 33.854  -14.697 -22.203 1.00 43.06  ? 550  LEU A CD2 1 
ATOM   4029  N  N   . VAL A  1 551 ? 31.789  -19.255 -21.794 1.00 47.92  ? 551  VAL A N   1 
ATOM   4030  C  CA  . VAL A  1 551 ? 32.665  -20.416 -21.953 1.00 45.24  ? 551  VAL A CA  1 
ATOM   4031  C  C   . VAL A  1 551 ? 33.586  -20.244 -23.171 1.00 55.42  ? 551  VAL A C   1 
ATOM   4032  O  O   . VAL A  1 551 ? 33.138  -19.987 -24.297 1.00 47.32  ? 551  VAL A O   1 
ATOM   4033  C  CB  . VAL A  1 551 ? 31.873  -21.711 -22.091 1.00 45.07  ? 551  VAL A CB  1 
ATOM   4034  C  CG1 . VAL A  1 551 ? 32.824  -22.891 -22.159 1.00 52.29  ? 551  VAL A CG1 1 
ATOM   4035  C  CG2 . VAL A  1 551 ? 30.927  -21.875 -20.919 1.00 45.64  ? 551  VAL A CG2 1 
ATOM   4036  N  N   . VAL A  1 552 ? 34.882  -20.390 -22.916 1.00 55.23  ? 552  VAL A N   1 
ATOM   4037  C  CA  . VAL A  1 552 ? 35.919  -20.070 -23.878 1.00 53.85  ? 552  VAL A CA  1 
ATOM   4038  C  C   . VAL A  1 552 ? 36.809  -21.270 -24.200 1.00 61.98  ? 552  VAL A C   1 
ATOM   4039  O  O   . VAL A  1 552 ? 37.546  -21.750 -23.325 1.00 53.43  ? 552  VAL A O   1 
ATOM   4040  C  CB  . VAL A  1 552 ? 36.795  -18.931 -23.347 1.00 52.70  ? 552  VAL A CB  1 
ATOM   4041  C  CG1 . VAL A  1 552 ? 37.948  -18.650 -24.292 1.00 59.33  ? 552  VAL A CG1 1 
ATOM   4042  C  CG2 . VAL A  1 552 ? 35.954  -17.690 -23.151 1.00 52.12  ? 552  VAL A CG2 1 
ATOM   4043  N  N   . LYS A  1 553 ? 36.732  -21.748 -25.451 1.00 68.75  ? 553  LYS A N   1 
ATOM   4044  C  CA  . LYS A  1 553 ? 37.630  -22.800 -25.959 1.00 65.02  ? 553  LYS A CA  1 
ATOM   4045  C  C   . LYS A  1 553 ? 38.652  -22.238 -26.956 1.00 66.92  ? 553  LYS A C   1 
ATOM   4046  O  O   . LYS A  1 553 ? 38.313  -21.470 -27.858 1.00 67.46  ? 553  LYS A O   1 
ATOM   4047  C  CB  . LYS A  1 553 ? 36.846  -23.936 -26.622 1.00 56.27  ? 553  LYS A CB  1 
ATOM   4048  C  CG  . LYS A  1 553 ? 37.730  -25.141 -26.943 1.00 61.21  ? 553  LYS A CG  1 
ATOM   4049  C  CD  . LYS A  1 553 ? 37.028  -26.179 -27.812 1.00 75.27  ? 553  LYS A CD  1 
ATOM   4050  C  CE  . LYS A  1 553 ? 36.092  -27.076 -27.008 1.00 74.41  ? 553  LYS A CE  1 
ATOM   4051  N  NZ  . LYS A  1 553 ? 35.377  -28.085 -27.866 1.00 77.39  ? 553  LYS A NZ  1 
ATOM   4052  N  N   . GLN A  1 554 ? 39.905  -22.634 -26.785 1.00 65.17  ? 554  GLN A N   1 
ATOM   4053  C  CA  . GLN A  1 554 ? 40.992  -22.104 -27.587 1.00 70.65  ? 554  GLN A CA  1 
ATOM   4054  C  C   . GLN A  1 554 ? 41.542  -23.171 -28.513 1.00 79.72  ? 554  GLN A C   1 
ATOM   4055  O  O   . GLN A  1 554 ? 41.902  -24.250 -28.055 1.00 84.70  ? 554  GLN A O   1 
ATOM   4056  C  CB  . GLN A  1 554 ? 42.094  -21.572 -26.676 1.00 72.69  ? 554  GLN A CB  1 
ATOM   4057  C  CG  . GLN A  1 554 ? 43.262  -20.945 -27.395 1.00 76.64  ? 554  GLN A CG  1 
ATOM   4058  C  CD  . GLN A  1 554 ? 44.201  -20.266 -26.434 1.00 70.61  ? 554  GLN A CD  1 
ATOM   4059  O  OE1 . GLN A  1 554 ? 44.227  -20.590 -25.250 1.00 72.53  ? 554  GLN A OE1 1 
ATOM   4060  N  NE2 . GLN A  1 554 ? 44.975  -19.312 -26.932 1.00 78.37  ? 554  GLN A NE2 1 
ATOM   4061  N  N   . ASP A  1 555 ? 41.598  -22.878 -29.810 1.00 83.30  ? 555  ASP A N   1 
ATOM   4062  C  CA  . ASP A  1 555 ? 42.116  -23.833 -30.800 1.00 85.65  ? 555  ASP A CA  1 
ATOM   4063  C  C   . ASP A  1 555 ? 43.247  -23.210 -31.598 1.00 84.52  ? 555  ASP A C   1 
ATOM   4064  O  O   . ASP A  1 555 ? 43.044  -22.729 -32.715 1.00 83.99  ? 555  ASP A O   1 
ATOM   4065  C  CB  . ASP A  1 555 ? 41.011  -24.307 -31.751 1.00 86.08  ? 555  ASP A CB  1 
ATOM   4066  C  CG  . ASP A  1 555 ? 40.266  -25.529 -31.232 1.00 98.21  ? 555  ASP A CG  1 
ATOM   4067  O  OD1 . ASP A  1 555 ? 40.885  -26.363 -30.530 1.00 96.44  ? 555  ASP A OD1 1 
ATOM   4068  O  OD2 . ASP A  1 555 ? 39.057  -25.660 -31.535 1.00 101.48 ? 555  ASP A OD2 1 
ATOM   4069  N  N   . GLY A  1 556 ? 44.440  -23.226 -31.019 1.00 83.17  ? 556  GLY A N   1 
ATOM   4070  C  CA  . GLY A  1 556 ? 45.556  -22.503 -31.585 1.00 87.96  ? 556  GLY A CA  1 
ATOM   4071  C  C   . GLY A  1 556 ? 45.259  -21.014 -31.619 1.00 94.10  ? 556  GLY A C   1 
ATOM   4072  O  O   . GLY A  1 556 ? 45.674  -20.255 -30.736 1.00 98.11  ? 556  GLY A O   1 
ATOM   4073  N  N   . CYS A  1 557 ? 44.527  -20.598 -32.646 1.00 90.57  ? 557  CYS A N   1 
ATOM   4074  C  CA  . CYS A  1 557 ? 44.163  -19.200 -32.813 1.00 91.80  ? 557  CYS A CA  1 
ATOM   4075  C  C   . CYS A  1 557 ? 42.669  -19.111 -33.073 1.00 89.28  ? 557  CYS A C   1 
ATOM   4076  O  O   . CYS A  1 557 ? 42.171  -18.128 -33.626 1.00 94.55  ? 557  CYS A O   1 
ATOM   4077  C  CB  . CYS A  1 557 ? 44.951  -18.569 -33.960 1.00 96.87  ? 557  CYS A CB  1 
ATOM   4078  S  SG  . CYS A  1 557 ? 44.414  -19.081 -35.610 1.00 98.65  ? 557  CYS A SG  1 
ATOM   4079  N  N   . SER A  1 558 ? 41.957  -20.155 -32.669 1.00 82.46  ? 558  SER A N   1 
ATOM   4080  C  CA  . SER A  1 558 ? 40.518  -20.223 -32.868 1.00 86.19  ? 558  SER A CA  1 
ATOM   4081  C  C   . SER A  1 558 ? 39.739  -20.187 -31.536 1.00 87.45  ? 558  SER A C   1 
ATOM   4082  O  O   . SER A  1 558 ? 39.204  -21.208 -31.092 1.00 83.78  ? 558  SER A O   1 
ATOM   4083  C  CB  . SER A  1 558 ? 40.167  -21.485 -33.660 1.00 79.52  ? 558  SER A CB  1 
ATOM   4084  O  OG  . SER A  1 558 ? 38.767  -21.624 -33.823 1.00 82.70  ? 558  SER A OG  1 
ATOM   4085  N  N   . LEU A  1 559 ? 39.673  -19.008 -30.912 1.00 83.57  ? 559  LEU A N   1 
ATOM   4086  C  CA  . LEU A  1 559 ? 38.915  -18.816 -29.670 1.00 74.49  ? 559  LEU A CA  1 
ATOM   4087  C  C   . LEU A  1 559 ? 37.410  -18.858 -29.946 1.00 72.04  ? 559  LEU A C   1 
ATOM   4088  O  O   . LEU A  1 559 ? 36.866  -17.968 -30.607 1.00 75.02  ? 559  LEU A O   1 
ATOM   4089  C  CB  . LEU A  1 559 ? 39.294  -17.485 -29.003 1.00 73.33  ? 559  LEU A CB  1 
ATOM   4090  C  CG  . LEU A  1 559 ? 40.764  -17.202 -28.648 1.00 74.61  ? 559  LEU A CG  1 
ATOM   4091  C  CD1 . LEU A  1 559 ? 40.939  -15.760 -28.220 1.00 76.38  ? 559  LEU A CD1 1 
ATOM   4092  C  CD2 . LEU A  1 559 ? 41.263  -18.117 -27.545 1.00 72.21  ? 559  LEU A CD2 1 
ATOM   4093  N  N   . ARG A  1 560 ? 36.740  -19.895 -29.457 1.00 64.30  ? 560  ARG A N   1 
ATOM   4094  C  CA  . ARG A  1 560 ? 35.306  -20.040 -29.692 1.00 66.41  ? 560  ARG A CA  1 
ATOM   4095  C  C   . ARG A  1 560 ? 34.562  -19.643 -28.430 1.00 66.71  ? 560  ARG A C   1 
ATOM   4096  O  O   . ARG A  1 560 ? 34.962  -20.008 -27.326 1.00 66.42  ? 560  ARG A O   1 
ATOM   4097  C  CB  . ARG A  1 560 ? 34.956  -21.477 -30.112 1.00 69.11  ? 560  ARG A CB  1 
ATOM   4098  C  CG  . ARG A  1 560 ? 35.907  -22.046 -31.188 1.00 84.82  ? 560  ARG A CG  1 
ATOM   4099  C  CD  . ARG A  1 560 ? 35.205  -22.915 -32.245 1.00 84.55  ? 560  ARG A CD  1 
ATOM   4100  N  NE  . ARG A  1 560 ? 35.386  -24.342 -31.994 1.00 88.78  ? 560  ARG A NE  1 
ATOM   4101  C  CZ  . ARG A  1 560 ? 34.414  -25.244 -32.089 1.00 88.37  ? 560  ARG A CZ  1 
ATOM   4102  N  NH1 . ARG A  1 560 ? 33.188  -24.864 -32.434 1.00 81.56  ? 560  ARG A NH1 1 
ATOM   4103  N  NH2 . ARG A  1 560 ? 34.668  -26.522 -31.837 1.00 86.70  ? 560  ARG A NH2 1 
ATOM   4104  N  N   . LEU A  1 561 ? 33.483  -18.893 -28.590 1.00 58.57  ? 561  LEU A N   1 
ATOM   4105  C  CA  . LEU A  1 561 ? 32.793  -18.338 -27.441 1.00 50.77  ? 561  LEU A CA  1 
ATOM   4106  C  C   . LEU A  1 561 ? 31.378  -18.870 -27.319 1.00 57.57  ? 561  LEU A C   1 
ATOM   4107  O  O   . LEU A  1 561 ? 30.646  -18.911 -28.303 1.00 59.74  ? 561  LEU A O   1 
ATOM   4108  C  CB  . LEU A  1 561 ? 32.763  -16.807 -27.532 1.00 51.12  ? 561  LEU A CB  1 
ATOM   4109  C  CG  . LEU A  1 561 ? 34.125  -16.134 -27.740 1.00 53.25  ? 561  LEU A CG  1 
ATOM   4110  C  CD1 . LEU A  1 561 ? 33.955  -14.690 -28.157 1.00 54.54  ? 561  LEU A CD1 1 
ATOM   4111  C  CD2 . LEU A  1 561 ? 35.051  -16.253 -26.513 1.00 51.87  ? 561  LEU A CD2 1 
ATOM   4112  N  N   . GLN A  1 562 ? 30.992  -19.270 -26.108 1.00 52.40  ? 562  GLN A N   1 
ATOM   4113  C  CA  . GLN A  1 562 ? 29.591  -19.553 -25.826 1.00 55.56  ? 562  GLN A CA  1 
ATOM   4114  C  C   . GLN A  1 562 ? 29.136  -18.814 -24.570 1.00 53.75  ? 562  GLN A C   1 
ATOM   4115  O  O   . GLN A  1 562 ? 29.895  -18.680 -23.601 1.00 49.37  ? 562  GLN A O   1 
ATOM   4116  C  CB  . GLN A  1 562 ? 29.351  -21.058 -25.670 1.00 56.63  ? 562  GLN A CB  1 
ATOM   4117  C  CG  . GLN A  1 562 ? 29.256  -21.820 -26.989 1.00 74.17  ? 562  GLN A CG  1 
ATOM   4118  C  CD  . GLN A  1 562 ? 29.503  -23.328 -26.833 1.00 72.52  ? 562  GLN A CD  1 
ATOM   4119  O  OE1 . GLN A  1 562 ? 30.066  -23.783 -25.834 1.00 73.60  ? 562  GLN A OE1 1 
ATOM   4120  N  NE2 . GLN A  1 562 ? 29.088  -24.098 -27.830 1.00 65.87  ? 562  GLN A NE2 1 
ATOM   4121  N  N   . GLN A  1 563 ? 27.893  -18.341 -24.591 1.00 50.61  ? 563  GLN A N   1 
ATOM   4122  C  CA  . GLN A  1 563 ? 27.328  -17.661 -23.444 1.00 49.05  ? 563  GLN A CA  1 
ATOM   4123  C  C   . GLN A  1 563 ? 26.180  -18.480 -22.898 1.00 51.01  ? 563  GLN A C   1 
ATOM   4124  O  O   . GLN A  1 563 ? 25.568  -19.250 -23.610 1.00 49.84  ? 563  GLN A O   1 
ATOM   4125  C  CB  . GLN A  1 563 ? 26.876  -16.242 -23.798 1.00 48.38  ? 563  GLN A CB  1 
ATOM   4126  C  CG  . GLN A  1 563 ? 25.576  -16.156 -24.574 1.00 56.75  ? 563  GLN A CG  1 
ATOM   4127  C  CD  . GLN A  1 563 ? 24.865  -14.828 -24.356 1.00 52.16  ? 563  GLN A CD  1 
ATOM   4128  O  OE1 . GLN A  1 563 ? 24.064  -14.688 -23.428 1.00 53.90  ? 563  GLN A OE1 1 
ATOM   4129  N  NE2 . GLN A  1 563 ? 25.156  -13.845 -25.208 1.00 46.75  ? 563  GLN A NE2 1 
ATOM   4130  N  N   . GLU A  1 564 ? 25.886  -18.291 -21.620 1.00 55.84  ? 564  GLU A N   1 
ATOM   4131  C  CA  . GLU A  1 564 ? 25.107  -19.255 -20.868 1.00 52.88  ? 564  GLU A CA  1 
ATOM   4132  C  C   . GLU A  1 564 ? 24.706  -18.613 -19.551 1.00 50.45  ? 564  GLU A C   1 
ATOM   4133  O  O   . GLU A  1 564 ? 25.476  -17.836 -18.984 1.00 45.18  ? 564  GLU A O   1 
ATOM   4134  C  CB  . GLU A  1 564 ? 25.953  -20.502 -20.628 1.00 48.76  ? 564  GLU A CB  1 
ATOM   4135  C  CG  . GLU A  1 564 ? 25.242  -21.805 -20.424 1.00 56.72  ? 564  GLU A CG  1 
ATOM   4136  C  CD  . GLU A  1 564 ? 26.225  -22.988 -20.529 1.00 61.59  ? 564  GLU A CD  1 
ATOM   4137  O  OE1 . GLU A  1 564 ? 27.152  -23.077 -19.695 1.00 58.22  ? 564  GLU A OE1 1 
ATOM   4138  O  OE2 . GLU A  1 564 ? 26.084  -23.817 -21.459 1.00 59.37  ? 564  GLU A OE2 1 
ATOM   4139  N  N   . ARG A  1 565 ? 23.513  -18.920 -19.060 1.00 49.32  ? 565  ARG A N   1 
ATOM   4140  C  CA  . ARG A  1 565 ? 23.137  -18.444 -17.745 1.00 42.21  ? 565  ARG A CA  1 
ATOM   4141  C  C   . ARG A  1 565 ? 23.947  -19.228 -16.735 1.00 46.00  ? 565  ARG A C   1 
ATOM   4142  O  O   . ARG A  1 565 ? 23.957  -20.463 -16.762 1.00 48.85  ? 565  ARG A O   1 
ATOM   4143  C  CB  . ARG A  1 565 ? 21.644  -18.602 -17.486 1.00 45.40  ? 565  ARG A CB  1 
ATOM   4144  C  CG  . ARG A  1 565 ? 21.158  -17.907 -16.213 1.00 46.14  ? 565  ARG A CG  1 
ATOM   4145  C  CD  . ARG A  1 565 ? 19.656  -18.014 -16.093 1.00 46.32  ? 565  ARG A CD  1 
ATOM   4146  N  NE  . ARG A  1 565 ? 19.206  -17.892 -14.716 1.00 50.67  ? 565  ARG A NE  1 
ATOM   4147  C  CZ  . ARG A  1 565 ? 18.054  -18.372 -14.254 1.00 55.33  ? 565  ARG A CZ  1 
ATOM   4148  N  NH1 . ARG A  1 565 ? 17.226  -19.020 -15.055 1.00 55.57  ? 565  ARG A NH1 1 
ATOM   4149  N  NH2 . ARG A  1 565 ? 17.726  -18.200 -12.981 1.00 62.41  ? 565  ARG A NH2 1 
ATOM   4150  N  N   . PHE A  1 566 ? 24.657  -18.508 -15.873 1.00 44.14  ? 566  PHE A N   1 
ATOM   4151  C  CA  . PHE A  1 566 ? 25.467  -19.144 -14.854 1.00 40.10  ? 566  PHE A CA  1 
ATOM   4152  C  C   . PHE A  1 566 ? 24.559  -19.601 -13.751 1.00 36.93  ? 566  PHE A C   1 
ATOM   4153  O  O   . PHE A  1 566 ? 23.673  -18.871 -13.349 1.00 39.43  ? 566  PHE A O   1 
ATOM   4154  C  CB  . PHE A  1 566 ? 26.526  -18.210 -14.310 1.00 36.06  ? 566  PHE A CB  1 
ATOM   4155  C  CG  . PHE A  1 566 ? 27.333  -18.818 -13.222 1.00 41.53  ? 566  PHE A CG  1 
ATOM   4156  C  CD1 . PHE A  1 566 ? 28.157  -19.901 -13.483 1.00 43.11  ? 566  PHE A CD1 1 
ATOM   4157  C  CD2 . PHE A  1 566 ? 27.258  -18.334 -11.934 1.00 35.57  ? 566  PHE A CD2 1 
ATOM   4158  C  CE1 . PHE A  1 566 ? 28.908  -20.475 -12.479 1.00 39.81  ? 566  PHE A CE1 1 
ATOM   4159  C  CE2 . PHE A  1 566 ? 28.009  -18.898 -10.924 1.00 40.65  ? 566  PHE A CE2 1 
ATOM   4160  C  CZ  . PHE A  1 566 ? 28.835  -19.974 -11.195 1.00 39.97  ? 566  PHE A CZ  1 
ATOM   4161  N  N   . LEU A  1 567 ? 24.762  -20.829 -13.294 1.00 42.13  ? 567  LEU A N   1 
ATOM   4162  C  CA  . LEU A  1 567 ? 23.867  -21.446 -12.322 1.00 46.27  ? 567  LEU A CA  1 
ATOM   4163  C  C   . LEU A  1 567 ? 24.642  -22.207 -11.265 1.00 48.29  ? 567  LEU A C   1 
ATOM   4164  O  O   . LEU A  1 567 ? 25.413  -23.124 -11.556 1.00 53.78  ? 567  LEU A O   1 
ATOM   4165  C  CB  . LEU A  1 567 ? 22.870  -22.380 -12.999 1.00 45.00  ? 567  LEU A CB  1 
ATOM   4166  C  CG  . LEU A  1 567 ? 21.811  -21.737 -13.889 1.00 44.84  ? 567  LEU A CG  1 
ATOM   4167  C  CD1 . LEU A  1 567 ? 20.887  -22.831 -14.389 1.00 50.80  ? 567  LEU A CD1 1 
ATOM   4168  C  CD2 . LEU A  1 567 ? 21.030  -20.664 -13.150 1.00 37.41  ? 567  LEU A CD2 1 
ATOM   4169  N  N   . GLN A  1 568 ? 24.407  -21.809 -10.027 1.00 48.49  ? 568  GLN A N   1 
ATOM   4170  C  CA  . GLN A  1 568 ? 25.109  -22.336 -8.879  1.00 49.80  ? 568  GLN A CA  1 
ATOM   4171  C  C   . GLN A  1 568 ? 24.450  -23.623 -8.363  1.00 56.68  ? 568  GLN A C   1 
ATOM   4172  O  O   . GLN A  1 568 ? 23.250  -23.646 -8.062  1.00 54.54  ? 568  GLN A O   1 
ATOM   4173  C  CB  . GLN A  1 568 ? 25.146  -21.259 -7.804  1.00 47.71  ? 568  GLN A CB  1 
ATOM   4174  C  CG  . GLN A  1 568 ? 26.077  -21.525 -6.693  1.00 51.73  ? 568  GLN A CG  1 
ATOM   4175  C  CD  . GLN A  1 568 ? 27.477  -21.741 -7.160  1.00 49.83  ? 568  GLN A CD  1 
ATOM   4176  O  OE1 . GLN A  1 568 ? 27.982  -22.857 -7.103  1.00 62.20  ? 568  GLN A OE1 1 
ATOM   4177  N  NE2 . GLN A  1 568 ? 28.131  -20.679 -7.601  1.00 44.10  ? 568  GLN A NE2 1 
ATOM   4178  N  N   . GLY A  1 569 ? 25.244  -24.691 -8.289  1.00 57.26  ? 569  GLY A N   1 
ATOM   4179  C  CA  . GLY A  1 569 ? 24.788  -25.975 -7.785  1.00 66.99  ? 569  GLY A CA  1 
ATOM   4180  C  C   . GLY A  1 569 ? 23.834  -26.698 -8.723  1.00 69.72  ? 569  GLY A C   1 
ATOM   4181  O  O   . GLY A  1 569 ? 23.046  -27.547 -8.296  1.00 70.25  ? 569  GLY A O   1 
ATOM   4182  N  N   . VAL A  1 570 ? 23.881  -26.343 -10.001 1.00 63.45  ? 570  VAL A N   1 
ATOM   4183  C  CA  . VAL A  1 570 ? 23.050  -27.005 -10.996 1.00 68.48  ? 570  VAL A CA  1 
ATOM   4184  C  C   . VAL A  1 570 ? 23.956  -27.358 -12.159 1.00 67.98  ? 570  VAL A C   1 
ATOM   4185  O  O   . VAL A  1 570 ? 24.289  -26.498 -12.979 1.00 67.10  ? 570  VAL A O   1 
ATOM   4186  C  CB  . VAL A  1 570 ? 21.866  -26.120 -11.459 1.00 65.64  ? 570  VAL A CB  1 
ATOM   4187  C  CG1 . VAL A  1 570 ? 21.070  -26.820 -12.557 1.00 68.29  ? 570  VAL A CG1 1 
ATOM   4188  C  CG2 . VAL A  1 570 ? 20.955  -25.765 -10.267 1.00 56.01  ? 570  VAL A CG2 1 
ATOM   4189  N  N   . PHE A  1 571 ? 24.368  -28.622 -12.212 1.00 67.28  ? 571  PHE A N   1 
ATOM   4190  C  CA  . PHE A  1 571 ? 25.492  -29.023 -13.052 1.00 72.64  ? 571  PHE A CA  1 
ATOM   4191  C  C   . PHE A  1 571 ? 25.183  -28.947 -14.545 1.00 72.69  ? 571  PHE A C   1 
ATOM   4192  O  O   . PHE A  1 571 ? 24.028  -29.077 -14.965 1.00 67.10  ? 571  PHE A O   1 
ATOM   4193  C  CB  . PHE A  1 571 ? 25.951  -30.429 -12.672 1.00 73.89  ? 571  PHE A CB  1 
ATOM   4194  C  CG  . PHE A  1 571 ? 26.328  -30.559 -11.230 1.00 79.75  ? 571  PHE A CG  1 
ATOM   4195  C  CD1 . PHE A  1 571 ? 27.626  -30.305 -10.815 1.00 79.21  ? 571  PHE A CD1 1 
ATOM   4196  C  CD2 . PHE A  1 571 ? 25.375  -30.913 -10.279 1.00 84.87  ? 571  PHE A CD2 1 
ATOM   4197  C  CE1 . PHE A  1 571 ? 27.974  -30.404 -9.480  1.00 73.93  ? 571  PHE A CE1 1 
ATOM   4198  C  CE2 . PHE A  1 571 ? 25.712  -31.020 -8.938  1.00 82.52  ? 571  PHE A CE2 1 
ATOM   4199  C  CZ  . PHE A  1 571 ? 27.011  -30.759 -8.540  1.00 86.37  ? 571  PHE A CZ  1 
ATOM   4200  N  N   . GLN A  1 572 ? 26.245  -28.712 -15.319 1.00 75.85  ? 572  GLN A N   1 
ATOM   4201  C  CA  . GLN A  1 572 ? 26.205  -28.574 -16.782 1.00 78.79  ? 572  GLN A CA  1 
ATOM   4202  C  C   . GLN A  1 572 ? 25.149  -29.454 -17.461 1.00 81.42  ? 572  GLN A C   1 
ATOM   4203  O  O   . GLN A  1 572 ? 24.471  -29.028 -18.391 1.00 79.32  ? 572  GLN A O   1 
ATOM   4204  C  CB  . GLN A  1 572 ? 27.596  -28.887 -17.359 1.00 78.92  ? 572  GLN A CB  1 
ATOM   4205  C  CG  . GLN A  1 572 ? 28.267  -30.133 -16.739 1.00 83.78  ? 572  GLN A CG  1 
ATOM   4206  C  CD  . GLN A  1 572 ? 29.715  -30.335 -17.191 1.00 86.38  ? 572  GLN A CD  1 
ATOM   4207  O  OE1 . GLN A  1 572 ? 30.225  -29.602 -18.050 1.00 81.00  ? 572  GLN A OE1 1 
ATOM   4208  N  NE2 . GLN A  1 572 ? 30.382  -31.334 -16.609 1.00 78.04  ? 572  GLN A NE2 1 
ATOM   4209  N  N   . GLU A  1 573 ? 25.014  -30.682 -16.977 1.00 84.04  ? 573  GLU A N   1 
ATOM   4210  C  CA  . GLU A  1 573 ? 24.011  -31.595 -17.488 1.00 86.01  ? 573  GLU A CA  1 
ATOM   4211  C  C   . GLU A  1 573 ? 23.182  -32.147 -16.329 1.00 85.16  ? 573  GLU A C   1 
ATOM   4212  O  O   . GLU A  1 573 ? 23.531  -33.147 -15.700 1.00 82.65  ? 573  GLU A O   1 
ATOM   4213  C  CB  . GLU A  1 573 ? 24.674  -32.712 -18.297 1.00 96.15  ? 573  GLU A CB  1 
ATOM   4214  C  CG  . GLU A  1 573 ? 25.389  -32.194 -19.553 1.00 96.91  ? 573  GLU A CG  1 
ATOM   4215  C  CD  . GLU A  1 573 ? 25.903  -33.304 -20.452 1.00 107.39 ? 573  GLU A CD  1 
ATOM   4216  O  OE1 . GLU A  1 573 ? 26.440  -34.305 -19.928 1.00 118.64 ? 573  GLU A OE1 1 
ATOM   4217  O  OE2 . GLU A  1 573 ? 25.769  -33.175 -21.688 1.00 101.29 ? 573  GLU A OE2 1 
ATOM   4218  N  N   . ASP A  1 574 ? 22.079  -31.456 -16.070 1.00 84.54  ? 574  ASP A N   1 
ATOM   4219  C  CA  . ASP A  1 574 ? 21.203  -31.699 -14.933 1.00 85.03  ? 574  ASP A CA  1 
ATOM   4220  C  C   . ASP A  1 574 ? 19.781  -31.573 -15.471 1.00 87.13  ? 574  ASP A C   1 
ATOM   4221  O  O   . ASP A  1 574 ? 19.550  -30.781 -16.386 1.00 85.80  ? 574  ASP A O   1 
ATOM   4222  C  CB  . ASP A  1 574 ? 21.477  -30.674 -13.823 1.00 87.94  ? 574  ASP A CB  1 
ATOM   4223  C  CG  . ASP A  1 574 ? 21.414  -31.266 -12.429 1.00 86.53  ? 574  ASP A CG  1 
ATOM   4224  O  OD1 . ASP A  1 574 ? 20.304  -31.342 -11.861 1.00 89.61  ? 574  ASP A OD1 1 
ATOM   4225  O  OD2 . ASP A  1 574 ? 22.484  -31.616 -11.886 1.00 83.00  ? 574  ASP A OD2 1 
ATOM   4226  N  N   . PRO A  1 575 ? 18.831  -32.353 -14.925 1.00 90.02  ? 575  PRO A N   1 
ATOM   4227  C  CA  . PRO A  1 575 ? 17.436  -32.361 -15.397 1.00 86.72  ? 575  PRO A CA  1 
ATOM   4228  C  C   . PRO A  1 575 ? 16.855  -30.968 -15.658 1.00 88.58  ? 575  PRO A C   1 
ATOM   4229  O  O   . PRO A  1 575 ? 16.304  -30.706 -16.730 1.00 85.35  ? 575  PRO A O   1 
ATOM   4230  C  CB  . PRO A  1 575 ? 16.684  -33.038 -14.244 1.00 87.02  ? 575  PRO A CB  1 
ATOM   4231  C  CG  . PRO A  1 575 ? 17.689  -33.949 -13.626 1.00 90.85  ? 575  PRO A CG  1 
ATOM   4232  C  CD  . PRO A  1 575 ? 19.051  -33.324 -13.836 1.00 92.39  ? 575  PRO A CD  1 
ATOM   4233  N  N   . GLU A  1 576 ? 16.998  -30.083 -14.678 1.00 86.69  ? 576  GLU A N   1 
ATOM   4234  C  CA  . GLU A  1 576 ? 16.364  -28.775 -14.722 1.00 84.32  ? 576  GLU A CA  1 
ATOM   4235  C  C   . GLU A  1 576 ? 17.307  -27.700 -15.256 1.00 80.68  ? 576  GLU A C   1 
ATOM   4236  O  O   . GLU A  1 576 ? 16.920  -26.539 -15.383 1.00 74.78  ? 576  GLU A O   1 
ATOM   4237  C  CB  . GLU A  1 576 ? 15.858  -28.389 -13.327 1.00 82.42  ? 576  GLU A CB  1 
ATOM   4238  C  CG  . GLU A  1 576 ? 16.956  -28.228 -12.277 1.00 87.50  ? 576  GLU A CG  1 
ATOM   4239  C  CD  . GLU A  1 576 ? 17.479  -29.556 -11.728 1.00 98.29  ? 576  GLU A CD  1 
ATOM   4240  O  OE1 . GLU A  1 576 ? 17.735  -30.491 -12.524 1.00 88.71  ? 576  GLU A OE1 1 
ATOM   4241  O  OE2 . GLU A  1 576 ? 17.636  -29.661 -10.487 1.00 101.50 ? 576  GLU A OE2 1 
ATOM   4242  N  N   . TRP A  1 577 ? 18.538  -28.089 -15.580 1.00 83.50  ? 577  TRP A N   1 
ATOM   4243  C  CA  . TRP A  1 577 ? 19.534  -27.128 -16.048 1.00 75.80  ? 577  TRP A CA  1 
ATOM   4244  C  C   . TRP A  1 577 ? 19.140  -26.492 -17.378 1.00 78.59  ? 577  TRP A C   1 
ATOM   4245  O  O   . TRP A  1 577 ? 19.293  -25.279 -17.554 1.00 77.69  ? 577  TRP A O   1 
ATOM   4246  C  CB  . TRP A  1 577 ? 20.913  -27.778 -16.185 1.00 73.63  ? 577  TRP A CB  1 
ATOM   4247  C  CG  . TRP A  1 577 ? 21.987  -26.762 -16.449 1.00 72.85  ? 577  TRP A CG  1 
ATOM   4248  C  CD1 . TRP A  1 577 ? 22.659  -26.019 -15.520 1.00 69.54  ? 577  TRP A CD1 1 
ATOM   4249  C  CD2 . TRP A  1 577 ? 22.491  -26.356 -17.726 1.00 69.73  ? 577  TRP A CD2 1 
ATOM   4250  N  NE1 . TRP A  1 577 ? 23.557  -25.184 -16.137 1.00 67.89  ? 577  TRP A NE1 1 
ATOM   4251  C  CE2 . TRP A  1 577 ? 23.475  -25.371 -17.492 1.00 68.71  ? 577  TRP A CE2 1 
ATOM   4252  C  CE3 . TRP A  1 577 ? 22.208  -26.728 -19.044 1.00 71.27  ? 577  TRP A CE3 1 
ATOM   4253  C  CZ2 . TRP A  1 577 ? 24.182  -24.756 -18.530 1.00 65.68  ? 577  TRP A CZ2 1 
ATOM   4254  C  CZ3 . TRP A  1 577 ? 22.911  -26.116 -20.076 1.00 73.24  ? 577  TRP A CZ3 1 
ATOM   4255  C  CH2 . TRP A  1 577 ? 23.884  -25.142 -19.811 1.00 67.23  ? 577  TRP A CH2 1 
ATOM   4256  N  N   . ARG A  1 578 ? 18.632  -27.298 -18.311 1.00 80.15  ? 578  ARG A N   1 
ATOM   4257  C  CA  . ARG A  1 578 ? 18.282  -26.792 -19.640 1.00 74.85  ? 578  ARG A CA  1 
ATOM   4258  C  C   . ARG A  1 578 ? 17.018  -25.933 -19.604 1.00 73.00  ? 578  ARG A C   1 
ATOM   4259  O  O   . ARG A  1 578 ? 16.862  -24.996 -20.395 1.00 70.70  ? 578  ARG A O   1 
ATOM   4260  C  CB  . ARG A  1 578 ? 18.096  -27.948 -20.611 1.00 77.13  ? 578  ARG A CB  1 
ATOM   4261  C  CG  . ARG A  1 578 ? 18.553  -27.658 -22.028 1.00 85.26  ? 578  ARG A CG  1 
ATOM   4262  C  CD  . ARG A  1 578 ? 18.393  -28.907 -22.869 1.00 91.23  ? 578  ARG A CD  1 
ATOM   4263  N  NE  . ARG A  1 578 ? 16.999  -29.345 -22.880 1.00 101.94 ? 578  ARG A NE  1 
ATOM   4264  C  CZ  . ARG A  1 578 ? 16.577  -30.515 -23.344 1.00 96.02  ? 578  ARG A CZ  1 
ATOM   4265  N  NH1 . ARG A  1 578 ? 17.447  -31.390 -23.836 1.00 84.73  ? 578  ARG A NH1 1 
ATOM   4266  N  NH2 . ARG A  1 578 ? 15.282  -30.807 -23.309 1.00 91.50  ? 578  ARG A NH2 1 
ATOM   4267  N  N   . ALA A  1 579 ? 16.127  -26.252 -18.670 1.00 69.42  ? 579  ALA A N   1 
ATOM   4268  C  CA  . ALA A  1 579 ? 14.888  -25.506 -18.504 1.00 67.11  ? 579  ALA A CA  1 
ATOM   4269  C  C   . ALA A  1 579 ? 15.145  -24.096 -17.953 1.00 76.96  ? 579  ALA A C   1 
ATOM   4270  O  O   . ALA A  1 579 ? 14.353  -23.176 -18.165 1.00 72.81  ? 579  ALA A O   1 
ATOM   4271  C  CB  . ALA A  1 579 ? 13.938  -26.266 -17.594 1.00 66.06  ? 579  ALA A CB  1 
ATOM   4272  N  N   . LEU A  1 580 ? 16.255  -23.932 -17.241 1.00 74.86  ? 580  LEU A N   1 
ATOM   4273  C  CA  . LEU A  1 580 ? 16.613  -22.631 -16.703 1.00 71.71  ? 580  LEU A CA  1 
ATOM   4274  C  C   . LEU A  1 580 ? 17.476  -21.871 -17.697 1.00 68.10  ? 580  LEU A C   1 
ATOM   4275  O  O   . LEU A  1 580 ? 17.863  -20.735 -17.435 1.00 62.94  ? 580  LEU A O   1 
ATOM   4276  C  CB  . LEU A  1 580 ? 17.354  -22.770 -15.371 1.00 67.92  ? 580  LEU A CB  1 
ATOM   4277  C  CG  . LEU A  1 580 ? 16.641  -23.465 -14.213 1.00 72.06  ? 580  LEU A CG  1 
ATOM   4278  C  CD1 . LEU A  1 580 ? 17.662  -24.119 -13.281 1.00 65.50  ? 580  LEU A CD1 1 
ATOM   4279  C  CD2 . LEU A  1 580 ? 15.772  -22.476 -13.458 1.00 69.87  ? 580  LEU A CD2 1 
ATOM   4280  N  N   . GLN A  1 581 ? 17.783  -22.492 -18.835 1.00 68.92  ? 581  GLN A N   1 
ATOM   4281  C  CA  . GLN A  1 581 ? 18.620  -21.831 -19.837 1.00 68.80  ? 581  GLN A CA  1 
ATOM   4282  C  C   . GLN A  1 581 ? 17.825  -20.983 -20.843 1.00 64.87  ? 581  GLN A C   1 
ATOM   4283  O  O   . GLN A  1 581 ? 18.272  -19.908 -21.210 1.00 67.53  ? 581  GLN A O   1 
ATOM   4284  C  CB  . GLN A  1 581 ? 19.477  -22.861 -20.559 1.00 61.47  ? 581  GLN A CB  1 
ATOM   4285  C  CG  . GLN A  1 581 ? 20.626  -23.367 -19.704 1.00 65.22  ? 581  GLN A CG  1 
ATOM   4286  C  CD  . GLN A  1 581 ? 21.515  -22.243 -19.164 1.00 67.23  ? 581  GLN A CD  1 
ATOM   4287  O  OE1 . GLN A  1 581 ? 21.788  -21.247 -19.849 1.00 63.44  ? 581  GLN A OE1 1 
ATOM   4288  N  NE2 . GLN A  1 581 ? 21.971  -22.404 -17.927 1.00 59.21  ? 581  GLN A NE2 1 
ATOM   4289  N  N   . GLU A  1 582 ? 16.657  -21.463 -21.265 1.00 72.40  ? 582  GLU A N   1 
ATOM   4290  C  CA  . GLU A  1 582 ? 15.694  -20.692 -22.072 1.00 76.63  ? 582  GLU A CA  1 
ATOM   4291  C  C   . GLU A  1 582 ? 16.262  -19.737 -23.119 1.00 86.30  ? 582  GLU A C   1 
ATOM   4292  O  O   . GLU A  1 582 ? 17.146  -20.101 -23.908 1.00 91.13  ? 582  GLU A O   1 
ATOM   4293  C  CB  . GLU A  1 582 ? 14.811  -19.870 -21.159 1.00 76.05  ? 582  GLU A CB  1 
ATOM   4294  C  CG  . GLU A  1 582 ? 14.497  -20.566 -19.881 1.00 82.21  ? 582  GLU A CG  1 
ATOM   4295  C  CD  . GLU A  1 582 ? 13.870  -19.634 -18.886 1.00 77.17  ? 582  GLU A CD  1 
ATOM   4296  O  OE1 . GLU A  1 582 ? 13.088  -18.753 -19.320 1.00 86.83  ? 582  GLU A OE1 1 
ATOM   4297  O  OE2 . GLU A  1 582 ? 14.178  -19.775 -17.683 1.00 76.89  ? 582  GLU A OE2 1 
ATOM   4298  N  N   . ARG A  1 583 ? 15.732  -18.514 -23.127 1.00 75.06  ? 583  ARG A N   1 
ATOM   4299  C  CA  . ARG A  1 583 ? 16.244  -17.491 -24.027 1.00 76.22  ? 583  ARG A CA  1 
ATOM   4300  C  C   . ARG A  1 583 ? 17.066  -16.469 -23.241 1.00 72.25  ? 583  ARG A C   1 
ATOM   4301  O  O   . ARG A  1 583 ? 17.116  -15.281 -23.578 1.00 68.19  ? 583  ARG A O   1 
ATOM   4302  C  CB  . ARG A  1 583 ? 15.107  -16.812 -24.817 1.00 96.41  ? 583  ARG A CB  1 
ATOM   4303  C  CG  . ARG A  1 583 ? 14.201  -15.838 -24.051 1.00 102.69 ? 583  ARG A CG  1 
ATOM   4304  C  CD  . ARG A  1 583 ? 13.340  -15.009 -25.023 1.00 106.66 ? 583  ARG A CD  1 
ATOM   4305  N  NE  . ARG A  1 583 ? 12.555  -13.975 -24.346 1.00 109.73 ? 583  ARG A NE  1 
ATOM   4306  C  CZ  . ARG A  1 583 ? 11.512  -13.347 -24.885 1.00 118.71 ? 583  ARG A CZ  1 
ATOM   4307  N  NH1 . ARG A  1 583 ? 11.113  -13.645 -26.118 1.00 122.56 ? 583  ARG A NH1 1 
ATOM   4308  N  NH2 . ARG A  1 583 ? 10.859  -12.423 -24.189 1.00 118.69 ? 583  ARG A NH2 1 
ATOM   4309  N  N   . TYR A  1 584 ? 17.729  -16.941 -22.192 1.00 66.13  ? 584  TYR A N   1 
ATOM   4310  C  CA  . TYR A  1 584 ? 18.686  -16.089 -21.520 1.00 58.47  ? 584  TYR A CA  1 
ATOM   4311  C  C   . TYR A  1 584 ? 19.786  -15.747 -22.508 1.00 58.21  ? 584  TYR A C   1 
ATOM   4312  O  O   . TYR A  1 584 ? 20.664  -16.548 -22.807 1.00 59.91  ? 584  TYR A O   1 
ATOM   4313  C  CB  . TYR A  1 584 ? 19.232  -16.748 -20.251 1.00 55.37  ? 584  TYR A CB  1 
ATOM   4314  C  CG  . TYR A  1 584 ? 18.253  -16.617 -19.101 1.00 60.81  ? 584  TYR A CG  1 
ATOM   4315  C  CD1 . TYR A  1 584 ? 17.254  -17.561 -18.904 1.00 61.00  ? 584  TYR A CD1 1 
ATOM   4316  C  CD2 . TYR A  1 584 ? 18.292  -15.520 -18.251 1.00 51.74  ? 584  TYR A CD2 1 
ATOM   4317  C  CE1 . TYR A  1 584 ? 16.344  -17.437 -17.874 1.00 60.78  ? 584  TYR A CE1 1 
ATOM   4318  C  CE2 . TYR A  1 584 ? 17.380  -15.384 -17.222 1.00 57.73  ? 584  TYR A CE2 1 
ATOM   4319  C  CZ  . TYR A  1 584 ? 16.409  -16.346 -17.033 1.00 62.59  ? 584  TYR A CZ  1 
ATOM   4320  O  OH  . TYR A  1 584 ? 15.498  -16.219 -16.004 1.00 61.24  ? 584  TYR A OH  1 
ATOM   4321  N  N   . LEU A  1 585 ? 19.702  -14.543 -23.046 1.00 48.82  ? 585  LEU A N   1 
ATOM   4322  C  CA  . LEU A  1 585 ? 20.735  -14.065 -23.925 1.00 49.34  ? 585  LEU A CA  1 
ATOM   4323  C  C   . LEU A  1 585 ? 21.100  -12.637 -23.560 1.00 48.26  ? 585  LEU A C   1 
ATOM   4324  O  O   . LEU A  1 585 ? 20.223  -11.800 -23.328 1.00 46.94  ? 585  LEU A O   1 
ATOM   4325  C  CB  . LEU A  1 585 ? 20.263  -14.152 -25.372 1.00 56.18  ? 585  LEU A CB  1 
ATOM   4326  C  CG  . LEU A  1 585 ? 21.346  -13.953 -26.413 1.00 51.01  ? 585  LEU A CG  1 
ATOM   4327  C  CD1 . LEU A  1 585 ? 22.055  -15.268 -26.664 1.00 54.19  ? 585  LEU A CD1 1 
ATOM   4328  C  CD2 . LEU A  1 585 ? 20.739  -13.397 -27.685 1.00 65.43  ? 585  LEU A CD2 1 
ATOM   4329  N  N   . TRP A  1 586 ? 22.394  -12.362 -23.505 1.00 45.24  ? 586  TRP A N   1 
ATOM   4330  C  CA  . TRP A  1 586 ? 22.872  -11.031 -23.152 1.00 44.55  ? 586  TRP A CA  1 
ATOM   4331  C  C   . TRP A  1 586 ? 23.703  -10.430 -24.281 1.00 46.78  ? 586  TRP A C   1 
ATOM   4332  O  O   . TRP A  1 586 ? 24.395  -11.145 -24.995 1.00 42.83  ? 586  TRP A O   1 
ATOM   4333  C  CB  . TRP A  1 586 ? 23.733  -11.080 -21.884 1.00 38.66  ? 586  TRP A CB  1 
ATOM   4334  C  CG  . TRP A  1 586 ? 23.003  -11.211 -20.563 1.00 45.41  ? 586  TRP A CG  1 
ATOM   4335  C  CD1 . TRP A  1 586 ? 22.592  -10.196 -19.765 1.00 40.78  ? 586  TRP A CD1 1 
ATOM   4336  C  CD2 . TRP A  1 586 ? 22.645  -12.430 -19.877 1.00 47.11  ? 586  TRP A CD2 1 
ATOM   4337  N  NE1 . TRP A  1 586 ? 21.976  -10.692 -18.640 1.00 42.01  ? 586  TRP A NE1 1 
ATOM   4338  C  CE2 . TRP A  1 586 ? 21.996  -12.058 -18.681 1.00 44.88  ? 586  TRP A CE2 1 
ATOM   4339  C  CE3 . TRP A  1 586 ? 22.799  -13.792 -20.167 1.00 45.32  ? 586  TRP A CE3 1 
ATOM   4340  C  CZ2 . TRP A  1 586 ? 21.503  -12.991 -17.773 1.00 39.69  ? 586  TRP A CZ2 1 
ATOM   4341  C  CZ3 . TRP A  1 586 ? 22.318  -14.723 -19.260 1.00 47.15  ? 586  TRP A CZ3 1 
ATOM   4342  C  CH2 . TRP A  1 586 ? 21.678  -14.317 -18.075 1.00 46.23  ? 586  TRP A CH2 1 
ATOM   4343  N  N   . HIS A  1 587 ? 23.677  -9.114  -24.428 1.00 47.01  ? 587  HIS A N   1 
ATOM   4344  C  CA  . HIS A  1 587 ? 24.719  -8.484  -25.208 1.00 43.49  ? 587  HIS A CA  1 
ATOM   4345  C  C   . HIS A  1 587 ? 25.834  -8.225  -24.238 1.00 40.27  ? 587  HIS A C   1 
ATOM   4346  O  O   . HIS A  1 587 ? 25.673  -7.427  -23.331 1.00 44.95  ? 587  HIS A O   1 
ATOM   4347  C  CB  . HIS A  1 587 ? 24.237  -7.194  -25.877 1.00 49.59  ? 587  HIS A CB  1 
ATOM   4348  C  CG  . HIS A  1 587 ? 23.196  -7.413  -26.934 1.00 59.82  ? 587  HIS A CG  1 
ATOM   4349  N  ND1 . HIS A  1 587 ? 22.973  -6.519  -27.960 1.00 62.94  ? 587  HIS A ND1 1 
ATOM   4350  C  CD2 . HIS A  1 587 ? 22.323  -8.433  -27.127 1.00 61.42  ? 587  HIS A CD2 1 
ATOM   4351  C  CE1 . HIS A  1 587 ? 22.000  -6.974  -28.733 1.00 60.07  ? 587  HIS A CE1 1 
ATOM   4352  N  NE2 . HIS A  1 587 ? 21.588  -8.133  -28.249 1.00 62.04  ? 587  HIS A NE2 1 
ATOM   4353  N  N   . ILE A  1 588 ? 26.952  -8.920  -24.402 1.00 37.85  ? 588  ILE A N   1 
ATOM   4354  C  CA  . ILE A  1 588 ? 28.029  -8.863  -23.424 1.00 38.65  ? 588  ILE A CA  1 
ATOM   4355  C  C   . ILE A  1 588 ? 29.288  -8.230  -23.985 1.00 39.49  ? 588  ILE A C   1 
ATOM   4356  O  O   . ILE A  1 588 ? 29.943  -8.816  -24.839 1.00 43.80  ? 588  ILE A O   1 
ATOM   4357  C  CB  . ILE A  1 588 ? 28.413  -10.274 -22.906 1.00 37.86  ? 588  ILE A CB  1 
ATOM   4358  C  CG1 . ILE A  1 588 ? 27.202  -11.043 -22.397 1.00 37.39  ? 588  ILE A CG1 1 
ATOM   4359  C  CG2 . ILE A  1 588 ? 29.449  -10.185 -21.805 1.00 33.73  ? 588  ILE A CG2 1 
ATOM   4360  C  CD1 . ILE A  1 588 ? 27.500  -12.529 -22.184 1.00 27.66  ? 588  ILE A CD1 1 
ATOM   4361  N  N   . PRO A  1 589 ? 29.682  -7.066  -23.453 1.00 42.60  ? 589  PRO A N   1 
ATOM   4362  C  CA  . PRO A  1 589 ? 30.887  -6.431  -23.986 1.00 41.05  ? 589  PRO A CA  1 
ATOM   4363  C  C   . PRO A  1 589 ? 32.115  -7.105  -23.429 1.00 41.13  ? 589  PRO A C   1 
ATOM   4364  O  O   . PRO A  1 589 ? 32.629  -6.707  -22.393 1.00 45.52  ? 589  PRO A O   1 
ATOM   4365  C  CB  . PRO A  1 589 ? 30.772  -4.986  -23.495 1.00 40.65  ? 589  PRO A CB  1 
ATOM   4366  C  CG  . PRO A  1 589 ? 29.989  -5.082  -22.212 1.00 31.07  ? 589  PRO A CG  1 
ATOM   4367  C  CD  . PRO A  1 589 ? 29.202  -6.393  -22.233 1.00 39.21  ? 589  PRO A CD  1 
ATOM   4368  N  N   . LEU A  1 590 ? 32.583  -8.134  -24.114 1.00 38.76  ? 590  LEU A N   1 
ATOM   4369  C  CA  . LEU A  1 590 ? 33.757  -8.846  -23.658 1.00 40.99  ? 590  LEU A CA  1 
ATOM   4370  C  C   . LEU A  1 590 ? 34.980  -7.969  -23.696 1.00 42.77  ? 590  LEU A C   1 
ATOM   4371  O  O   . LEU A  1 590 ? 35.003  -6.950  -24.378 1.00 52.76  ? 590  LEU A O   1 
ATOM   4372  C  CB  . LEU A  1 590 ? 33.989  -10.093 -24.508 1.00 43.13  ? 590  LEU A CB  1 
ATOM   4373  C  CG  . LEU A  1 590 ? 32.830  -11.086 -24.484 1.00 44.03  ? 590  LEU A CG  1 
ATOM   4374  C  CD1 . LEU A  1 590 ? 33.199  -12.377 -25.214 1.00 44.10  ? 590  LEU A CD1 1 
ATOM   4375  C  CD2 . LEU A  1 590 ? 32.480  -11.369 -23.036 1.00 46.92  ? 590  LEU A CD2 1 
ATOM   4376  N  N   . THR A  1 591 ? 35.990  -8.362  -22.936 1.00 46.29  ? 591  THR A N   1 
ATOM   4377  C  CA  . THR A  1 591 ? 37.338  -7.854  -23.110 1.00 48.25  ? 591  THR A CA  1 
ATOM   4378  C  C   . THR A  1 591 ? 38.276  -9.041  -22.935 1.00 52.32  ? 591  THR A C   1 
ATOM   4379  O  O   . THR A  1 591 ? 37.878  -10.065 -22.379 1.00 51.51  ? 591  THR A O   1 
ATOM   4380  C  CB  . THR A  1 591 ? 37.696  -6.726  -22.107 1.00 50.48  ? 591  THR A CB  1 
ATOM   4381  O  OG1 . THR A  1 591 ? 37.692  -7.223  -20.755 1.00 50.23  ? 591  THR A OG1 1 
ATOM   4382  C  CG2 . THR A  1 591 ? 36.721  -5.553  -22.230 1.00 48.97  ? 591  THR A CG2 1 
ATOM   4383  N  N   . TYR A  1 592 ? 39.499  -8.917  -23.441 1.00 54.39  ? 592  TYR A N   1 
ATOM   4384  C  CA  . TYR A  1 592 ? 40.565  -9.876  -23.150 1.00 56.41  ? 592  TYR A CA  1 
ATOM   4385  C  C   . TYR A  1 592 ? 41.939  -9.329  -23.498 1.00 56.93  ? 592  TYR A C   1 
ATOM   4386  O  O   . TYR A  1 592 ? 42.083  -8.387  -24.280 1.00 59.54  ? 592  TYR A O   1 
ATOM   4387  C  CB  . TYR A  1 592 ? 40.357  -11.198 -23.884 1.00 58.10  ? 592  TYR A CB  1 
ATOM   4388  C  CG  . TYR A  1 592 ? 40.313  -11.114 -25.399 1.00 60.65  ? 592  TYR A CG  1 
ATOM   4389  C  CD1 . TYR A  1 592 ? 39.122  -10.850 -26.062 1.00 60.28  ? 592  TYR A CD1 1 
ATOM   4390  C  CD2 . TYR A  1 592 ? 41.453  -11.341 -26.168 1.00 64.35  ? 592  TYR A CD2 1 
ATOM   4391  C  CE1 . TYR A  1 592 ? 39.065  -10.787 -27.447 1.00 67.36  ? 592  TYR A CE1 1 
ATOM   4392  C  CE2 . TYR A  1 592 ? 41.406  -11.281 -27.561 1.00 65.22  ? 592  TYR A CE2 1 
ATOM   4393  C  CZ  . TYR A  1 592 ? 40.206  -11.003 -28.193 1.00 74.07  ? 592  TYR A CZ  1 
ATOM   4394  O  OH  . TYR A  1 592 ? 40.134  -10.934 -29.569 1.00 76.36  ? 592  TYR A OH  1 
ATOM   4395  N  N   . SER A  1 593 ? 42.941  -9.906  -22.863 1.00 50.37  ? 593  SER A N   1 
ATOM   4396  C  CA  . SER A  1 593 ? 44.311  -9.697  -23.252 1.00 56.82  ? 593  SER A CA  1 
ATOM   4397  C  C   . SER A  1 593 ? 44.883  -11.099 -23.381 1.00 61.07  ? 593  SER A C   1 
ATOM   4398  O  O   . SER A  1 593 ? 44.184  -12.072 -23.109 1.00 60.23  ? 593  SER A O   1 
ATOM   4399  C  CB  . SER A  1 593 ? 45.062  -8.838  -22.234 1.00 54.17  ? 593  SER A CB  1 
ATOM   4400  O  OG  . SER A  1 593 ? 44.969  -9.379  -20.925 1.00 66.87  ? 593  SER A OG  1 
ATOM   4401  N  N   . THR A  1 594 ? 46.123  -11.229 -23.832 1.00 63.01  ? 594  THR A N   1 
ATOM   4402  C  CA  . THR A  1 594 ? 46.729  -12.553 -23.891 1.00 62.44  ? 594  THR A CA  1 
ATOM   4403  C  C   . THR A  1 594 ? 48.086  -12.570 -23.202 1.00 64.80  ? 594  THR A C   1 
ATOM   4404  O  O   . THR A  1 594 ? 48.542  -11.550 -22.677 1.00 60.78  ? 594  THR A O   1 
ATOM   4405  C  CB  . THR A  1 594 ? 46.905  -13.047 -25.330 1.00 61.07  ? 594  THR A CB  1 
ATOM   4406  O  OG1 . THR A  1 594 ? 47.991  -12.350 -25.947 1.00 61.42  ? 594  THR A OG1 1 
ATOM   4407  C  CG2 . THR A  1 594 ? 45.638  -12.844 -26.126 1.00 64.14  ? 594  THR A CG2 1 
ATOM   4408  N  N   . SER A  1 595 ? 48.719  -13.742 -23.200 1.00 66.92  ? 595  SER A N   1 
ATOM   4409  C  CA  . SER A  1 595 ? 50.033  -13.915 -22.595 1.00 60.51  ? 595  SER A CA  1 
ATOM   4410  C  C   . SER A  1 595 ? 51.108  -13.227 -23.402 1.00 62.13  ? 595  SER A C   1 
ATOM   4411  O  O   . SER A  1 595 ? 52.159  -12.909 -22.870 1.00 66.37  ? 595  SER A O   1 
ATOM   4412  C  CB  . SER A  1 595 ? 50.371  -15.396 -22.456 1.00 66.66  ? 595  SER A CB  1 
ATOM   4413  O  OG  . SER A  1 595 ? 50.251  -16.065 -23.697 1.00 73.50  ? 595  SER A OG  1 
ATOM   4414  N  N   . SER A  1 596 ? 50.841  -13.000 -24.685 1.00 73.11  ? 596  SER A N   1 
ATOM   4415  C  CA  . SER A  1 596 ? 51.820  -12.376 -25.573 1.00 73.42  ? 596  SER A CA  1 
ATOM   4416  C  C   . SER A  1 596 ? 51.491  -10.922 -25.854 1.00 71.97  ? 596  SER A C   1 
ATOM   4417  O  O   . SER A  1 596 ? 52.190  -10.273 -26.625 1.00 85.21  ? 596  SER A O   1 
ATOM   4418  C  CB  . SER A  1 596 ? 51.918  -13.134 -26.902 1.00 77.10  ? 596  SER A CB  1 
ATOM   4419  O  OG  . SER A  1 596 ? 50.956  -12.659 -27.829 1.00 83.89  ? 596  SER A OG  1 
ATOM   4420  N  N   . SER A  1 597 ? 50.432  -10.407 -25.239 1.00 70.37  ? 597  SER A N   1 
ATOM   4421  C  CA  . SER A  1 597 ? 50.039  -9.020  -25.481 1.00 74.92  ? 597  SER A CA  1 
ATOM   4422  C  C   . SER A  1 597 ? 49.114  -8.463  -24.409 1.00 75.08  ? 597  SER A C   1 
ATOM   4423  O  O   . SER A  1 597 ? 48.017  -8.974  -24.198 1.00 72.11  ? 597  SER A O   1 
ATOM   4424  C  CB  . SER A  1 597 ? 49.360  -8.890  -26.847 1.00 76.37  ? 597  SER A CB  1 
ATOM   4425  O  OG  . SER A  1 597 ? 48.885  -7.572  -27.060 1.00 72.90  ? 597  SER A OG  1 
ATOM   4426  N  N   . ASN A  1 598 ? 49.552  -7.391  -23.757 1.00 79.77  ? 598  ASN A N   1 
ATOM   4427  C  CA  . ASN A  1 598 ? 48.738  -6.710  -22.753 1.00 79.97  ? 598  ASN A CA  1 
ATOM   4428  C  C   . ASN A  1 598 ? 47.654  -5.831  -23.365 1.00 77.46  ? 598  ASN A C   1 
ATOM   4429  O  O   . ASN A  1 598 ? 46.791  -5.319  -22.660 1.00 79.13  ? 598  ASN A O   1 
ATOM   4430  C  CB  . ASN A  1 598 ? 49.621  -5.855  -21.854 1.00 81.08  ? 598  ASN A CB  1 
ATOM   4431  C  CG  . ASN A  1 598 ? 50.143  -4.623  -22.560 1.00 90.69  ? 598  ASN A CG  1 
ATOM   4432  O  OD1 . ASN A  1 598 ? 50.133  -4.540  -23.794 1.00 90.97  ? 598  ASN A OD1 1 
ATOM   4433  N  ND2 . ASN A  1 598 ? 50.612  -3.654  -21.780 1.00 93.38  ? 598  ASN A ND2 1 
ATOM   4434  N  N   . VAL A  1 599 ? 47.739  -5.629  -24.675 1.00 77.18  ? 599  VAL A N   1 
ATOM   4435  C  CA  . VAL A  1 599 ? 46.712  -4.919  -25.419 1.00 76.26  ? 599  VAL A CA  1 
ATOM   4436  C  C   . VAL A  1 599 ? 45.328  -5.426  -25.067 1.00 68.78  ? 599  VAL A C   1 
ATOM   4437  O  O   . VAL A  1 599 ? 45.060  -6.622  -25.101 1.00 72.15  ? 599  VAL A O   1 
ATOM   4438  C  CB  . VAL A  1 599 ? 46.906  -5.069  -26.938 1.00 80.91  ? 599  VAL A CB  1 
ATOM   4439  C  CG1 . VAL A  1 599 ? 45.786  -4.358  -27.684 1.00 77.02  ? 599  VAL A CG1 1 
ATOM   4440  C  CG2 . VAL A  1 599 ? 48.263  -4.528  -27.349 1.00 90.33  ? 599  VAL A CG2 1 
ATOM   4441  N  N   . ILE A  1 600 ? 44.440  -4.513  -24.728 1.00 59.39  ? 600  ILE A N   1 
ATOM   4442  C  CA  . ILE A  1 600 ? 43.100  -4.921  -24.402 1.00 59.19  ? 600  ILE A CA  1 
ATOM   4443  C  C   . ILE A  1 600 ? 42.259  -4.935  -25.650 1.00 60.55  ? 600  ILE A C   1 
ATOM   4444  O  O   . ILE A  1 600 ? 42.023  -3.898  -26.257 1.00 65.84  ? 600  ILE A O   1 
ATOM   4445  C  CB  . ILE A  1 600 ? 42.476  -4.003  -23.361 1.00 57.95  ? 600  ILE A CB  1 
ATOM   4446  C  CG1 . ILE A  1 600 ? 43.342  -4.012  -22.102 1.00 58.56  ? 600  ILE A CG1 1 
ATOM   4447  C  CG2 . ILE A  1 600 ? 41.032  -4.426  -23.087 1.00 52.69  ? 600  ILE A CG2 1 
ATOM   4448  C  CD1 . ILE A  1 600 ? 42.884  -3.052  -21.047 1.00 64.53  ? 600  ILE A CD1 1 
ATOM   4449  N  N   . HIS A  1 601 ? 41.811  -6.119  -26.036 1.00 62.44  ? 601  HIS A N   1 
ATOM   4450  C  CA  . HIS A  1 601 ? 40.920  -6.251  -27.175 1.00 61.14  ? 601  HIS A CA  1 
ATOM   4451  C  C   . HIS A  1 601 ? 39.497  -6.346  -26.686 1.00 57.34  ? 601  HIS A C   1 
ATOM   4452  O  O   . HIS A  1 601 ? 39.231  -6.987  -25.678 1.00 61.58  ? 601  HIS A O   1 
ATOM   4453  C  CB  . HIS A  1 601 ? 41.279  -7.479  -28.005 1.00 68.46  ? 601  HIS A CB  1 
ATOM   4454  C  CG  . HIS A  1 601 ? 42.701  -7.496  -28.454 1.00 72.64  ? 601  HIS A CG  1 
ATOM   4455  N  ND1 . HIS A  1 601 ? 43.229  -6.526  -29.279 1.00 75.07  ? 601  HIS A ND1 1 
ATOM   4456  C  CD2 . HIS A  1 601 ? 43.713  -8.352  -28.178 1.00 75.76  ? 601  HIS A CD2 1 
ATOM   4457  C  CE1 . HIS A  1 601 ? 44.505  -6.789  -29.498 1.00 82.47  ? 601  HIS A CE1 1 
ATOM   4458  N  NE2 . HIS A  1 601 ? 44.824  -7.890  -28.840 1.00 84.02  ? 601  HIS A NE2 1 
ATOM   4459  N  N   . ARG A  1 602 ? 38.588  -5.713  -27.411 1.00 51.98  ? 602  ARG A N   1 
ATOM   4460  C  CA  . ARG A  1 602 ? 37.193  -5.645  -27.021 1.00 46.73  ? 602  ARG A CA  1 
ATOM   4461  C  C   . ARG A  1 602 ? 36.327  -6.158  -28.161 1.00 52.37  ? 602  ARG A C   1 
ATOM   4462  O  O   . ARG A  1 602 ? 36.751  -6.106  -29.309 1.00 67.90  ? 602  ARG A O   1 
ATOM   4463  C  CB  . ARG A  1 602 ? 36.825  -4.205  -26.669 1.00 52.06  ? 602  ARG A CB  1 
ATOM   4464  C  CG  . ARG A  1 602 ? 37.874  -3.485  -25.822 1.00 47.76  ? 602  ARG A CG  1 
ATOM   4465  C  CD  . ARG A  1 602 ? 37.393  -2.096  -25.462 1.00 40.11  ? 602  ARG A CD  1 
ATOM   4466  N  NE  . ARG A  1 602 ? 38.162  -1.499  -24.374 1.00 57.79  ? 602  ARG A NE  1 
ATOM   4467  C  CZ  . ARG A  1 602 ? 37.777  -1.495  -23.092 1.00 64.76  ? 602  ARG A CZ  1 
ATOM   4468  N  NH1 . ARG A  1 602 ? 36.626  -2.067  -22.718 1.00 45.99  ? 602  ARG A NH1 1 
ATOM   4469  N  NH2 . ARG A  1 602 ? 38.544  -0.912  -22.174 1.00 63.11  ? 602  ARG A NH2 1 
ATOM   4470  N  N   . HIS A  1 603 ? 35.130  -6.654  -27.854 1.00 42.66  ? 603  HIS A N   1 
ATOM   4471  C  CA  . HIS A  1 603 ? 34.195  -7.137  -28.863 1.00 43.48  ? 603  HIS A CA  1 
ATOM   4472  C  C   . HIS A  1 603 ? 32.888  -7.562  -28.215 1.00 42.72  ? 603  HIS A C   1 
ATOM   4473  O  O   . HIS A  1 603 ? 32.893  -8.287  -27.243 1.00 48.02  ? 603  HIS A O   1 
ATOM   4474  C  CB  . HIS A  1 603 ? 34.797  -8.312  -29.650 1.00 60.23  ? 603  HIS A CB  1 
ATOM   4475  C  CG  . HIS A  1 603 ? 33.788  -9.125  -30.405 1.00 60.73  ? 603  HIS A CG  1 
ATOM   4476  N  ND1 . HIS A  1 603 ? 33.599  -10.471 -30.178 1.00 58.65  ? 603  HIS A ND1 1 
ATOM   4477  C  CD2 . HIS A  1 603 ? 32.914  -8.784  -31.382 1.00 63.27  ? 603  HIS A CD2 1 
ATOM   4478  C  CE1 . HIS A  1 603 ? 32.649  -10.924 -30.977 1.00 61.87  ? 603  HIS A CE1 1 
ATOM   4479  N  NE2 . HIS A  1 603 ? 32.219  -9.922  -31.721 1.00 62.65  ? 603  HIS A NE2 1 
ATOM   4480  N  N   . ILE A  1 604 ? 31.764  -7.128  -28.767 1.00 47.79  ? 604  ILE A N   1 
ATOM   4481  C  CA  . ILE A  1 604 ? 30.467  -7.376  -28.151 1.00 42.02  ? 604  ILE A CA  1 
ATOM   4482  C  C   . ILE A  1 604 ? 29.805  -8.671  -28.600 1.00 52.65  ? 604  ILE A C   1 
ATOM   4483  O  O   . ILE A  1 604 ? 29.371  -8.786  -29.737 1.00 51.26  ? 604  ILE A O   1 
ATOM   4484  C  CB  . ILE A  1 604 ? 29.481  -6.246  -28.446 1.00 39.45  ? 604  ILE A CB  1 
ATOM   4485  C  CG1 . ILE A  1 604 ? 29.992  -4.919  -27.901 1.00 47.12  ? 604  ILE A CG1 1 
ATOM   4486  C  CG2 . ILE A  1 604 ? 28.099  -6.547  -27.864 1.00 43.34  ? 604  ILE A CG2 1 
ATOM   4487  C  CD1 . ILE A  1 604 ? 29.012  -3.796  -28.144 1.00 52.02  ? 604  ILE A CD1 1 
ATOM   4488  N  N   . LEU A  1 605 ? 29.695  -9.629  -27.688 1.00 44.71  ? 605  LEU A N   1 
ATOM   4489  C  CA  . LEU A  1 605 ? 28.981  -10.854 -27.973 1.00 46.07  ? 605  LEU A CA  1 
ATOM   4490  C  C   . LEU A  1 605 ? 27.470  -10.627 -27.934 1.00 48.49  ? 605  LEU A C   1 
ATOM   4491  O  O   . LEU A  1 605 ? 26.895  -10.458 -26.871 1.00 49.51  ? 605  LEU A O   1 
ATOM   4492  C  CB  . LEU A  1 605 ? 29.393  -11.929 -26.968 1.00 47.36  ? 605  LEU A CB  1 
ATOM   4493  C  CG  . LEU A  1 605 ? 28.806  -13.314 -27.174 1.00 50.51  ? 605  LEU A CG  1 
ATOM   4494  C  CD1 . LEU A  1 605 ? 29.171  -13.755 -28.566 1.00 54.40  ? 605  LEU A CD1 1 
ATOM   4495  C  CD2 . LEU A  1 605 ? 29.311  -14.314 -26.119 1.00 50.27  ? 605  LEU A CD2 1 
ATOM   4496  N  N   . LYS A  1 606 ? 26.817  -10.630 -29.090 1.00 56.57  ? 606  LYS A N   1 
ATOM   4497  C  CA  . LYS A  1 606 ? 25.375  -10.378 -29.142 1.00 53.13  ? 606  LYS A CA  1 
ATOM   4498  C  C   . LYS A  1 606 ? 24.560  -11.658 -29.252 1.00 51.19  ? 606  LYS A C   1 
ATOM   4499  O  O   . LYS A  1 606 ? 23.335  -11.627 -29.191 1.00 52.31  ? 606  LYS A O   1 
ATOM   4500  C  CB  . LYS A  1 606 ? 25.030  -9.467  -30.326 1.00 56.32  ? 606  LYS A CB  1 
ATOM   4501  C  CG  . LYS A  1 606 ? 26.023  -8.322  -30.581 1.00 56.82  ? 606  LYS A CG  1 
ATOM   4502  C  CD  . LYS A  1 606 ? 25.421  -7.258  -31.514 1.00 52.85  ? 606  LYS A CD  1 
ATOM   4503  C  CE  . LYS A  1 606 ? 26.314  -6.030  -31.608 1.00 60.53  ? 606  LYS A CE  1 
ATOM   4504  N  NZ  . LYS A  1 606 ? 25.603  -4.841  -32.189 1.00 60.52  ? 606  LYS A NZ  1 
ATOM   4505  N  N   . SER A  1 607 ? 25.236  -12.786 -29.428 1.00 51.38  ? 607  SER A N   1 
ATOM   4506  C  CA  . SER A  1 607 ? 24.526  -14.036 -29.678 1.00 58.44  ? 607  SER A CA  1 
ATOM   4507  C  C   . SER A  1 607 ? 25.045  -15.198 -28.839 1.00 59.86  ? 607  SER A C   1 
ATOM   4508  O  O   . SER A  1 607 ? 26.097  -15.096 -28.198 1.00 57.92  ? 607  SER A O   1 
ATOM   4509  C  CB  . SER A  1 607 ? 24.620  -14.406 -31.155 1.00 57.40  ? 607  SER A CB  1 
ATOM   4510  O  OG  . SER A  1 607 ? 25.974  -14.567 -31.516 1.00 56.17  ? 607  SER A OG  1 
ATOM   4511  N  N   . LYS A  1 608 ? 24.305  -16.307 -28.880 1.00 60.90  ? 608  LYS A N   1 
ATOM   4512  C  CA  . LYS A  1 608 ? 24.590  -17.497 -28.077 1.00 62.13  ? 608  LYS A CA  1 
ATOM   4513  C  C   . LYS A  1 608 ? 25.974  -18.086 -28.361 1.00 59.53  ? 608  LYS A C   1 
ATOM   4514  O  O   . LYS A  1 608 ? 26.605  -18.662 -27.470 1.00 60.64  ? 608  LYS A O   1 
ATOM   4515  C  CB  . LYS A  1 608 ? 23.495  -18.544 -28.310 1.00 56.06  ? 608  LYS A CB  1 
ATOM   4516  C  CG  . LYS A  1 608 ? 23.856  -19.975 -27.951 1.00 64.14  ? 608  LYS A CG  1 
ATOM   4517  C  CD  . LYS A  1 608 ? 24.131  -20.178 -26.465 1.00 69.90  ? 608  LYS A CD  1 
ATOM   4518  C  CE  . LYS A  1 608 ? 24.010  -21.657 -26.066 1.00 74.91  ? 608  LYS A CE  1 
ATOM   4519  N  NZ  . LYS A  1 608 ? 24.637  -22.597 -27.050 1.00 76.32  ? 608  LYS A NZ  1 
ATOM   4520  N  N   . THR A  1 609 ? 26.465  -17.917 -29.583 1.00 55.45  ? 609  THR A N   1 
ATOM   4521  C  CA  . THR A  1 609 ? 27.785  -18.443 -29.915 1.00 61.95  ? 609  THR A CA  1 
ATOM   4522  C  C   . THR A  1 609 ? 28.533  -17.570 -30.922 1.00 59.87  ? 609  THR A C   1 
ATOM   4523  O  O   . THR A  1 609 ? 27.919  -16.789 -31.648 1.00 63.59  ? 609  THR A O   1 
ATOM   4524  C  CB  . THR A  1 609 ? 27.675  -19.872 -30.459 1.00 64.96  ? 609  THR A CB  1 
ATOM   4525  O  OG1 . THR A  1 609 ? 28.977  -20.344 -30.818 1.00 70.62  ? 609  THR A OG1 1 
ATOM   4526  C  CG2 . THR A  1 609 ? 26.757  -19.902 -31.671 1.00 67.34  ? 609  THR A CG2 1 
ATOM   4527  N  N   . ASP A  1 610 ? 29.856  -17.705 -30.954 1.00 51.92  ? 610  ASP A N   1 
ATOM   4528  C  CA  . ASP A  1 610 ? 30.689  -16.836 -31.773 1.00 58.09  ? 610  ASP A CA  1 
ATOM   4529  C  C   . ASP A  1 610 ? 32.162  -17.234 -31.709 1.00 60.68  ? 610  ASP A C   1 
ATOM   4530  O  O   . ASP A  1 610 ? 32.584  -17.979 -30.822 1.00 61.16  ? 610  ASP A O   1 
ATOM   4531  C  CB  . ASP A  1 610 ? 30.525  -15.381 -31.336 1.00 56.37  ? 610  ASP A CB  1 
ATOM   4532  C  CG  . ASP A  1 610 ? 30.931  -14.391 -32.412 1.00 70.28  ? 610  ASP A CG  1 
ATOM   4533  O  OD1 . ASP A  1 610 ? 31.635  -14.797 -33.370 1.00 71.19  ? 610  ASP A OD1 1 
ATOM   4534  O  OD2 . ASP A  1 610 ? 30.548  -13.202 -32.292 1.00 69.93  ? 610  ASP A OD2 1 
ATOM   4535  N  N   . THR A  1 611 ? 32.944  -16.730 -32.659 1.00 59.60  ? 611  THR A N   1 
ATOM   4536  C  CA  . THR A  1 611 ? 34.358  -17.058 -32.719 1.00 62.45  ? 611  THR A CA  1 
ATOM   4537  C  C   . THR A  1 611 ? 35.199  -15.832 -32.999 1.00 61.48  ? 611  THR A C   1 
ATOM   4538  O  O   . THR A  1 611 ? 34.758  -14.905 -33.662 1.00 68.09  ? 611  THR A O   1 
ATOM   4539  C  CB  . THR A  1 611 ? 34.628  -18.110 -33.797 1.00 67.47  ? 611  THR A CB  1 
ATOM   4540  O  OG1 . THR A  1 611 ? 33.677  -17.944 -34.853 1.00 74.55  ? 611  THR A OG1 1 
ATOM   4541  C  CG2 . THR A  1 611 ? 34.454  -19.489 -33.233 1.00 63.05  ? 611  THR A CG2 1 
ATOM   4542  N  N   . LEU A  1 612 ? 36.417  -15.827 -32.484 1.00 66.94  ? 612  LEU A N   1 
ATOM   4543  C  CA  . LEU A  1 612 ? 37.337  -14.727 -32.726 1.00 75.81  ? 612  LEU A CA  1 
ATOM   4544  C  C   . LEU A  1 612 ? 38.702  -15.320 -33.046 1.00 82.20  ? 612  LEU A C   1 
ATOM   4545  O  O   . LEU A  1 612 ? 38.967  -16.483 -32.721 1.00 78.98  ? 612  LEU A O   1 
ATOM   4546  C  CB  . LEU A  1 612 ? 37.408  -13.783 -31.516 1.00 73.76  ? 612  LEU A CB  1 
ATOM   4547  C  CG  . LEU A  1 612 ? 36.170  -12.945 -31.133 1.00 76.85  ? 612  LEU A CG  1 
ATOM   4548  C  CD1 . LEU A  1 612 ? 36.315  -12.365 -29.730 1.00 69.30  ? 612  LEU A CD1 1 
ATOM   4549  C  CD2 . LEU A  1 612 ? 35.905  -11.815 -32.125 1.00 68.48  ? 612  LEU A CD2 1 
ATOM   4550  N  N   . ASP A  1 613 ? 39.567  -14.532 -33.679 1.00 81.65  ? 613  ASP A N   1 
ATOM   4551  C  CA  . ASP A  1 613 ? 40.847  -15.049 -34.148 1.00 84.55  ? 613  ASP A CA  1 
ATOM   4552  C  C   . ASP A  1 613 ? 42.048  -14.403 -33.477 1.00 88.39  ? 613  ASP A C   1 
ATOM   4553  O  O   . ASP A  1 613 ? 42.175  -13.180 -33.430 1.00 90.02  ? 613  ASP A O   1 
ATOM   4554  C  CB  . ASP A  1 613 ? 40.947  -14.880 -35.659 1.00 92.16  ? 613  ASP A CB  1 
ATOM   4555  C  CG  . ASP A  1 613 ? 39.913  -15.695 -36.392 1.00 92.85  ? 613  ASP A CG  1 
ATOM   4556  O  OD1 . ASP A  1 613 ? 40.080  -16.936 -36.450 1.00 88.41  ? 613  ASP A OD1 1 
ATOM   4557  O  OD2 . ASP A  1 613 ? 38.936  -15.098 -36.898 1.00 92.52  ? 613  ASP A OD2 1 
ATOM   4558  N  N   . LEU A  1 614 ? 42.945  -15.251 -32.989 1.00 90.31  ? 614  LEU A N   1 
ATOM   4559  C  CA  . LEU A  1 614 ? 44.049  -14.814 -32.152 1.00 94.68  ? 614  LEU A CA  1 
ATOM   4560  C  C   . LEU A  1 614 ? 45.383  -14.839 -32.893 1.00 99.20  ? 614  LEU A C   1 
ATOM   4561  O  O   . LEU A  1 614 ? 45.987  -15.901 -33.054 1.00 102.75 ? 614  LEU A O   1 
ATOM   4562  C  CB  . LEU A  1 614 ? 44.121  -15.700 -30.900 1.00 91.92  ? 614  LEU A CB  1 
ATOM   4563  C  CG  . LEU A  1 614 ? 44.530  -15.104 -29.549 1.00 87.26  ? 614  LEU A CG  1 
ATOM   4564  C  CD1 . LEU A  1 614 ? 46.007  -15.346 -29.260 1.00 88.67  ? 614  LEU A CD1 1 
ATOM   4565  C  CD2 . LEU A  1 614 ? 44.196  -13.617 -29.487 1.00 80.16  ? 614  LEU A CD2 1 
ATOM   4566  N  N   . PRO A  1 615 ? 45.852  -13.669 -33.349 1.00 98.70  ? 615  PRO A N   1 
ATOM   4567  C  CA  . PRO A  1 615 ? 47.218  -13.648 -33.879 1.00 101.52 ? 615  PRO A CA  1 
ATOM   4568  C  C   . PRO A  1 615 ? 48.235  -14.105 -32.827 1.00 104.62 ? 615  PRO A C   1 
ATOM   4569  O  O   . PRO A  1 615 ? 48.068  -13.798 -31.643 1.00 100.60 ? 615  PRO A O   1 
ATOM   4570  C  CB  . PRO A  1 615 ? 47.430  -12.179 -34.252 1.00 99.88  ? 615  PRO A CB  1 
ATOM   4571  C  CG  . PRO A  1 615 ? 46.442  -11.428 -33.414 1.00 101.12 ? 615  PRO A CG  1 
ATOM   4572  C  CD  . PRO A  1 615 ? 45.246  -12.328 -33.333 1.00 97.07  ? 615  PRO A CD  1 
ATOM   4573  N  N   . GLU A  1 616 ? 49.236  -14.858 -33.284 1.00 106.20 ? 616  GLU A N   1 
ATOM   4574  C  CA  . GLU A  1 616 ? 50.389  -15.330 -32.507 1.00 103.87 ? 616  GLU A CA  1 
ATOM   4575  C  C   . GLU A  1 616 ? 50.160  -16.648 -31.781 1.00 99.21  ? 616  GLU A C   1 
ATOM   4576  O  O   . GLU A  1 616 ? 51.129  -17.262 -31.336 1.00 97.27  ? 616  GLU A O   1 
ATOM   4577  C  CB  . GLU A  1 616 ? 50.855  -14.283 -31.497 1.00 100.83 ? 616  GLU A CB  1 
ATOM   4578  C  CG  . GLU A  1 616 ? 51.309  -12.987 -32.124 1.00 103.27 ? 616  GLU A CG  1 
ATOM   4579  C  CD  . GLU A  1 616 ? 52.050  -12.113 -31.140 1.00 107.14 ? 616  GLU A CD  1 
ATOM   4580  O  OE1 . GLU A  1 616 ? 52.855  -12.663 -30.354 1.00 102.36 ? 616  GLU A OE1 1 
ATOM   4581  O  OE2 . GLU A  1 616 ? 51.822  -10.881 -31.147 1.00 108.98 ? 616  GLU A OE2 1 
ATOM   4582  N  N   . LYS A  1 617 ? 48.904  -17.076 -31.653 1.00 98.57  ? 617  LYS A N   1 
ATOM   4583  C  CA  . LYS A  1 617 ? 48.612  -18.416 -31.142 1.00 98.93  ? 617  LYS A CA  1 
ATOM   4584  C  C   . LYS A  1 617 ? 49.264  -18.642 -29.761 1.00 99.28  ? 617  LYS A C   1 
ATOM   4585  O  O   . LYS A  1 617 ? 49.956  -19.634 -29.533 1.00 105.88 ? 617  LYS A O   1 
ATOM   4586  C  CB  . LYS A  1 617 ? 49.092  -19.453 -32.169 1.00 95.90  ? 617  LYS A CB  1 
ATOM   4587  C  CG  . LYS A  1 617 ? 48.666  -20.895 -31.946 1.00 96.22  ? 617  LYS A CG  1 
ATOM   4588  C  CD  . LYS A  1 617 ? 49.046  -21.746 -33.152 1.00 97.06  ? 617  LYS A CD  1 
ATOM   4589  C  CE  . LYS A  1 617 ? 49.743  -23.033 -32.742 1.00 95.11  ? 617  LYS A CE  1 
ATOM   4590  N  NZ  . LYS A  1 617 ? 50.835  -23.364 -33.698 1.00 98.47  ? 617  LYS A NZ  1 
ATOM   4591  N  N   . THR A  1 618 ? 49.042  -17.708 -28.845 1.00 94.20  ? 618  THR A N   1 
ATOM   4592  C  CA  . THR A  1 618 ? 49.795  -17.659 -27.593 1.00 86.67  ? 618  THR A CA  1 
ATOM   4593  C  C   . THR A  1 618 ? 49.376  -18.698 -26.547 1.00 80.21  ? 618  THR A C   1 
ATOM   4594  O  O   . THR A  1 618 ? 48.517  -19.536 -26.801 1.00 81.13  ? 618  THR A O   1 
ATOM   4595  C  CB  . THR A  1 618 ? 49.667  -16.276 -26.966 1.00 85.38  ? 618  THR A CB  1 
ATOM   4596  O  OG1 . THR A  1 618 ? 50.599  -16.146 -25.882 1.00 82.81  ? 618  THR A OG1 1 
ATOM   4597  C  CG2 . THR A  1 618 ? 48.249  -16.081 -26.467 1.00 79.62  ? 618  THR A CG2 1 
ATOM   4598  N  N   . SER A  1 619 ? 49.988  -18.625 -25.368 1.00 74.16  ? 619  SER A N   1 
ATOM   4599  C  CA  . SER A  1 619 ? 49.725  -19.577 -24.284 1.00 78.35  ? 619  SER A CA  1 
ATOM   4600  C  C   . SER A  1 619 ? 48.326  -19.444 -23.675 1.00 80.33  ? 619  SER A C   1 
ATOM   4601  O  O   . SER A  1 619 ? 47.464  -20.293 -23.899 1.00 85.32  ? 619  SER A O   1 
ATOM   4602  C  CB  . SER A  1 619 ? 50.761  -19.420 -23.171 1.00 75.10  ? 619  SER A CB  1 
ATOM   4603  O  OG  . SER A  1 619 ? 52.061  -19.272 -23.700 1.00 79.76  ? 619  SER A OG  1 
ATOM   4604  N  N   . TRP A  1 620 ? 48.106  -18.397 -22.881 1.00 73.85  ? 620  TRP A N   1 
ATOM   4605  C  CA  . TRP A  1 620 ? 46.795  -18.203 -22.256 1.00 69.48  ? 620  TRP A CA  1 
ATOM   4606  C  C   . TRP A  1 620 ? 46.076  -16.951 -22.737 1.00 63.38  ? 620  TRP A C   1 
ATOM   4607  O  O   . TRP A  1 620 ? 46.692  -15.989 -23.201 1.00 59.42  ? 620  TRP A O   1 
ATOM   4608  C  CB  . TRP A  1 620 ? 46.909  -18.162 -20.723 1.00 60.97  ? 620  TRP A CB  1 
ATOM   4609  C  CG  . TRP A  1 620 ? 47.971  -17.226 -20.161 1.00 57.96  ? 620  TRP A CG  1 
ATOM   4610  C  CD1 . TRP A  1 620 ? 49.217  -17.576 -19.712 1.00 57.72  ? 620  TRP A CD1 1 
ATOM   4611  C  CD2 . TRP A  1 620 ? 47.865  -15.807 -19.969 1.00 52.02  ? 620  TRP A CD2 1 
ATOM   4612  N  NE1 . TRP A  1 620 ? 49.892  -16.463 -19.257 1.00 56.55  ? 620  TRP A NE1 1 
ATOM   4613  C  CE2 . TRP A  1 620 ? 49.085  -15.367 -19.403 1.00 52.20  ? 620  TRP A CE2 1 
ATOM   4614  C  CE3 . TRP A  1 620 ? 46.864  -14.866 -20.225 1.00 56.18  ? 620  TRP A CE3 1 
ATOM   4615  C  CZ2 . TRP A  1 620 ? 49.329  -14.033 -19.102 1.00 48.82  ? 620  TRP A CZ2 1 
ATOM   4616  C  CZ3 . TRP A  1 620 ? 47.107  -13.543 -19.917 1.00 50.16  ? 620  TRP A CZ3 1 
ATOM   4617  C  CH2 . TRP A  1 620 ? 48.331  -13.137 -19.360 1.00 45.13  ? 620  TRP A CH2 1 
ATOM   4618  N  N   . VAL A  1 621 ? 44.756  -16.998 -22.622 1.00 62.72  ? 621  VAL A N   1 
ATOM   4619  C  CA  . VAL A  1 621 ? 43.906  -15.842 -22.858 1.00 66.38  ? 621  VAL A CA  1 
ATOM   4620  C  C   . VAL A  1 621 ? 43.049  -15.560 -21.628 1.00 57.55  ? 621  VAL A C   1 
ATOM   4621  O  O   . VAL A  1 621 ? 42.353  -16.455 -21.140 1.00 54.05  ? 621  VAL A O   1 
ATOM   4622  C  CB  . VAL A  1 621 ? 42.971  -16.053 -24.057 1.00 67.69  ? 621  VAL A CB  1 
ATOM   4623  C  CG1 . VAL A  1 621 ? 42.178  -14.782 -24.317 1.00 63.34  ? 621  VAL A CG1 1 
ATOM   4624  C  CG2 . VAL A  1 621 ? 43.757  -16.475 -25.285 1.00 74.11  ? 621  VAL A CG2 1 
ATOM   4625  N  N   . LYS A  1 622 ? 43.080  -14.320 -21.146 1.00 58.07  ? 622  LYS A N   1 
ATOM   4626  C  CA  . LYS A  1 622 ? 42.321  -13.931 -19.945 1.00 52.62  ? 622  LYS A CA  1 
ATOM   4627  C  C   . LYS A  1 622 ? 41.188  -12.968 -20.291 1.00 56.35  ? 622  LYS A C   1 
ATOM   4628  O  O   . LYS A  1 622 ? 41.408  -11.766 -20.518 1.00 56.94  ? 622  LYS A O   1 
ATOM   4629  C  CB  . LYS A  1 622 ? 43.263  -13.322 -18.889 1.00 51.14  ? 622  LYS A CB  1 
ATOM   4630  C  CG  . LYS A  1 622 ? 42.603  -12.543 -17.758 1.00 56.93  ? 622  LYS A CG  1 
ATOM   4631  C  CD  . LYS A  1 622 ? 41.806  -13.439 -16.838 1.00 55.07  ? 622  LYS A CD  1 
ATOM   4632  C  CE  . LYS A  1 622 ? 41.126  -12.632 -15.763 1.00 46.09  ? 622  LYS A CE  1 
ATOM   4633  N  NZ  . LYS A  1 622 ? 40.100  -11.756 -16.356 1.00 48.34  ? 622  LYS A NZ  1 
ATOM   4634  N  N   . PHE A  1 623 ? 39.972  -13.507 -20.329 1.00 52.38  ? 623  PHE A N   1 
ATOM   4635  C  CA  . PHE A  1 623 ? 38.785  -12.698 -20.576 1.00 52.37  ? 623  PHE A CA  1 
ATOM   4636  C  C   . PHE A  1 623 ? 38.300  -11.888 -19.368 1.00 48.97  ? 623  PHE A C   1 
ATOM   4637  O  O   . PHE A  1 623 ? 38.664  -12.171 -18.225 1.00 48.54  ? 623  PHE A O   1 
ATOM   4638  C  CB  . PHE A  1 623 ? 37.660  -13.585 -21.088 1.00 49.36  ? 623  PHE A CB  1 
ATOM   4639  C  CG  . PHE A  1 623 ? 37.628  -13.678 -22.579 1.00 55.06  ? 623  PHE A CG  1 
ATOM   4640  C  CD1 . PHE A  1 623 ? 38.541  -14.477 -23.255 1.00 58.07  ? 623  PHE A CD1 1 
ATOM   4641  C  CD2 . PHE A  1 623 ? 36.717  -12.935 -23.311 1.00 51.81  ? 623  PHE A CD2 1 
ATOM   4642  C  CE1 . PHE A  1 623 ? 38.533  -14.546 -24.637 1.00 53.32  ? 623  PHE A CE1 1 
ATOM   4643  C  CE2 . PHE A  1 623 ? 36.698  -13.001 -24.690 1.00 55.07  ? 623  PHE A CE2 1 
ATOM   4644  C  CZ  . PHE A  1 623 ? 37.608  -13.809 -25.354 1.00 56.73  ? 623  PHE A CZ  1 
ATOM   4645  N  N   . ASN A  1 624 ? 37.462  -10.888 -19.650 1.00 49.56  ? 624  ASN A N   1 
ATOM   4646  C  CA  . ASN A  1 624 ? 37.029  -9.898  -18.663 1.00 47.04  ? 624  ASN A CA  1 
ATOM   4647  C  C   . ASN A  1 624 ? 38.204  -9.258  -17.937 1.00 46.77  ? 624  ASN A C   1 
ATOM   4648  O  O   . ASN A  1 624 ? 38.478  -9.600  -16.782 1.00 51.93  ? 624  ASN A O   1 
ATOM   4649  C  CB  . ASN A  1 624 ? 36.073  -10.521 -17.629 1.00 46.81  ? 624  ASN A CB  1 
ATOM   4650  C  CG  . ASN A  1 624 ? 35.246  -9.462  -16.880 1.00 47.30  ? 624  ASN A CG  1 
ATOM   4651  O  OD1 . ASN A  1 624 ? 35.316  -8.263  -17.185 1.00 41.37  ? 624  ASN A OD1 1 
ATOM   4652  N  ND2 . ASN A  1 624 ? 34.444  -9.908  -15.919 1.00 39.07  ? 624  ASN A ND2 1 
ATOM   4653  N  N   . VAL A  1 625 ? 38.904  -8.333  -18.586 1.00 44.16  ? 625  VAL A N   1 
ATOM   4654  C  CA  . VAL A  1 625 ? 40.073  -7.735  -17.925 1.00 49.85  ? 625  VAL A CA  1 
ATOM   4655  C  C   . VAL A  1 625 ? 39.672  -6.964  -16.670 1.00 43.06  ? 625  VAL A C   1 
ATOM   4656  O  O   . VAL A  1 625 ? 38.677  -6.239  -16.660 1.00 44.74  ? 625  VAL A O   1 
ATOM   4657  C  CB  . VAL A  1 625 ? 40.857  -6.793  -18.855 1.00 54.29  ? 625  VAL A CB  1 
ATOM   4658  C  CG1 . VAL A  1 625 ? 42.079  -6.251  -18.136 1.00 55.85  ? 625  VAL A CG1 1 
ATOM   4659  C  CG2 . VAL A  1 625 ? 41.285  -7.529  -20.112 1.00 55.08  ? 625  VAL A CG2 1 
ATOM   4660  N  N   . ASP A  1 626 ? 40.429  -7.169  -15.603 1.00 44.49  ? 626  ASP A N   1 
ATOM   4661  C  CA  . ASP A  1 626 ? 40.191  -6.491  -14.334 1.00 46.66  ? 626  ASP A CA  1 
ATOM   4662  C  C   . ASP A  1 626 ? 38.831  -6.827  -13.687 1.00 44.31  ? 626  ASP A C   1 
ATOM   4663  O  O   . ASP A  1 626 ? 38.481  -6.259  -12.661 1.00 38.68  ? 626  ASP A O   1 
ATOM   4664  C  CB  . ASP A  1 626 ? 40.311  -4.973  -14.529 1.00 47.85  ? 626  ASP A CB  1 
ATOM   4665  C  CG  . ASP A  1 626 ? 41.759  -4.484  -14.521 1.00 54.56  ? 626  ASP A CG  1 
ATOM   4666  O  OD1 . ASP A  1 626 ? 42.633  -5.152  -13.911 1.00 51.18  ? 626  ASP A OD1 1 
ATOM   4667  O  OD2 . ASP A  1 626 ? 42.015  -3.411  -15.113 1.00 53.96  ? 626  ASP A OD2 1 
ATOM   4668  N  N   . SER A  1 627 ? 38.083  -7.740  -14.304 1.00 41.61  ? 627  SER A N   1 
ATOM   4669  C  CA  . SER A  1 627 ? 36.741  -8.117  -13.875 1.00 42.10  ? 627  SER A CA  1 
ATOM   4670  C  C   . SER A  1 627 ? 35.726  -6.961  -13.942 1.00 42.00  ? 627  SER A C   1 
ATOM   4671  O  O   . SER A  1 627 ? 34.768  -6.923  -13.178 1.00 44.33  ? 627  SER A O   1 
ATOM   4672  C  CB  . SER A  1 627 ? 36.774  -8.709  -12.462 1.00 41.99  ? 627  SER A CB  1 
ATOM   4673  O  OG  . SER A  1 627 ? 37.209  -10.053 -12.487 1.00 43.91  ? 627  SER A OG  1 
ATOM   4674  N  N   . ASN A  1 628 ? 35.885  -6.063  -14.903 1.00 38.86  ? 628  ASN A N   1 
ATOM   4675  C  CA  . ASN A  1 628 ? 34.916  -4.992  -15.054 1.00 44.17  ? 628  ASN A CA  1 
ATOM   4676  C  C   . ASN A  1 628 ? 33.595  -5.421  -15.651 1.00 42.11  ? 628  ASN A C   1 
ATOM   4677  O  O   . ASN A  1 628 ? 32.656  -4.631  -15.684 1.00 49.78  ? 628  ASN A O   1 
ATOM   4678  C  CB  . ASN A  1 628 ? 35.505  -3.859  -15.887 1.00 39.65  ? 628  ASN A CB  1 
ATOM   4679  C  CG  . ASN A  1 628 ? 36.527  -3.067  -15.115 1.00 47.30  ? 628  ASN A CG  1 
ATOM   4680  O  OD1 . ASN A  1 628 ? 36.433  -2.942  -13.883 1.00 46.23  ? 628  ASN A OD1 1 
ATOM   4681  N  ND2 . ASN A  1 628 ? 37.532  -2.553  -15.816 1.00 52.56  ? 628  ASN A ND2 1 
ATOM   4682  N  N   . GLY A  1 629 ? 33.501  -6.663  -16.104 1.00 38.99  ? 629  GLY A N   1 
ATOM   4683  C  CA  . GLY A  1 629 ? 32.273  -7.137  -16.713 1.00 33.40  ? 629  GLY A CA  1 
ATOM   4684  C  C   . GLY A  1 629 ? 31.457  -8.013  -15.793 1.00 37.69  ? 629  GLY A C   1 
ATOM   4685  O  O   . GLY A  1 629 ? 31.982  -8.819  -15.032 1.00 41.07  ? 629  GLY A O   1 
ATOM   4686  N  N   . TYR A  1 630 ? 30.149  -7.877  -15.877 1.00 37.30  ? 630  TYR A N   1 
ATOM   4687  C  CA  . TYR A  1 630 ? 29.292  -8.665  -15.029 1.00 37.51  ? 630  TYR A CA  1 
ATOM   4688  C  C   . TYR A  1 630 ? 29.056  -10.022 -15.672 1.00 36.70  ? 630  TYR A C   1 
ATOM   4689  O  O   . TYR A  1 630 ? 27.959  -10.319 -16.172 1.00 31.94  ? 630  TYR A O   1 
ATOM   4690  C  CB  . TYR A  1 630 ? 27.981  -7.928  -14.767 1.00 38.17  ? 630  TYR A CB  1 
ATOM   4691  C  CG  . TYR A  1 630 ? 27.179  -8.529  -13.657 1.00 29.38  ? 630  TYR A CG  1 
ATOM   4692  C  CD1 . TYR A  1 630 ? 27.613  -8.450  -12.342 1.00 37.00  ? 630  TYR A CD1 1 
ATOM   4693  C  CD2 . TYR A  1 630 ? 25.984  -9.161  -13.912 1.00 32.33  ? 630  TYR A CD2 1 
ATOM   4694  C  CE1 . TYR A  1 630 ? 26.879  -9.015  -11.309 1.00 31.59  ? 630  TYR A CE1 1 
ATOM   4695  C  CE2 . TYR A  1 630 ? 25.242  -9.717  -12.893 1.00 34.93  ? 630  TYR A CE2 1 
ATOM   4696  C  CZ  . TYR A  1 630 ? 25.696  -9.636  -11.599 1.00 29.85  ? 630  TYR A CZ  1 
ATOM   4697  O  OH  . TYR A  1 630 ? 24.969  -10.199 -10.598 1.00 35.14  ? 630  TYR A OH  1 
ATOM   4698  N  N   . TYR A  1 631 ? 30.110  -10.837 -15.663 1.00 34.68  ? 631  TYR A N   1 
ATOM   4699  C  CA  . TYR A  1 631 ? 30.014  -12.222 -16.133 1.00 36.60  ? 631  TYR A CA  1 
ATOM   4700  C  C   . TYR A  1 631 ? 31.182  -13.103 -15.649 1.00 35.13  ? 631  TYR A C   1 
ATOM   4701  O  O   . TYR A  1 631 ? 32.282  -12.628 -15.396 1.00 33.59  ? 631  TYR A O   1 
ATOM   4702  C  CB  . TYR A  1 631 ? 29.919  -12.263 -17.668 1.00 34.59  ? 631  TYR A CB  1 
ATOM   4703  C  CG  . TYR A  1 631 ? 31.067  -11.570 -18.400 1.00 39.51  ? 631  TYR A CG  1 
ATOM   4704  C  CD1 . TYR A  1 631 ? 31.041  -10.199 -18.650 1.00 37.99  ? 631  TYR A CD1 1 
ATOM   4705  C  CD2 . TYR A  1 631 ? 32.176  -12.290 -18.837 1.00 38.36  ? 631  TYR A CD2 1 
ATOM   4706  C  CE1 . TYR A  1 631 ? 32.092  -9.566  -19.325 1.00 42.26  ? 631  TYR A CE1 1 
ATOM   4707  C  CE2 . TYR A  1 631 ? 33.221  -11.668 -19.505 1.00 42.16  ? 631  TYR A CE2 1 
ATOM   4708  C  CZ  . TYR A  1 631 ? 33.173  -10.307 -19.753 1.00 46.93  ? 631  TYR A CZ  1 
ATOM   4709  O  OH  . TYR A  1 631 ? 34.218  -9.694  -20.420 1.00 43.43  ? 631  TYR A OH  1 
ATOM   4710  N  N   . ILE A  1 632 ? 30.912  -14.396 -15.513 1.00 37.29  ? 632  ILE A N   1 
ATOM   4711  C  CA  . ILE A  1 632 ? 31.929  -15.379 -15.160 1.00 36.15  ? 632  ILE A CA  1 
ATOM   4712  C  C   . ILE A  1 632 ? 32.494  -15.989 -16.439 1.00 35.93  ? 632  ILE A C   1 
ATOM   4713  O  O   . ILE A  1 632 ? 31.773  -16.148 -17.419 1.00 35.19  ? 632  ILE A O   1 
ATOM   4714  C  CB  . ILE A  1 632 ? 31.334  -16.452 -14.227 1.00 40.10  ? 632  ILE A CB  1 
ATOM   4715  C  CG1 . ILE A  1 632 ? 31.078  -15.834 -12.858 1.00 42.22  ? 632  ILE A CG1 1 
ATOM   4716  C  CG2 . ILE A  1 632 ? 32.276  -17.617 -14.031 1.00 41.71  ? 632  ILE A CG2 1 
ATOM   4717  C  CD1 . ILE A  1 632 ? 29.767  -16.217 -12.251 1.00 39.55  ? 632  ILE A CD1 1 
ATOM   4718  N  N   . VAL A  1 633 ? 33.793  -16.270 -16.436 1.00 35.91  ? 633  VAL A N   1 
ATOM   4719  C  CA  . VAL A  1 633 ? 34.462  -16.824 -17.597 1.00 41.29  ? 633  VAL A CA  1 
ATOM   4720  C  C   . VAL A  1 633 ? 35.007  -18.205 -17.265 1.00 42.48  ? 633  VAL A C   1 
ATOM   4721  O  O   . VAL A  1 633 ? 35.738  -18.384 -16.295 1.00 40.66  ? 633  VAL A O   1 
ATOM   4722  C  CB  . VAL A  1 633 ? 35.611  -15.895 -18.137 1.00 45.88  ? 633  VAL A CB  1 
ATOM   4723  C  CG1 . VAL A  1 633 ? 35.055  -14.535 -18.509 1.00 41.76  ? 633  VAL A CG1 1 
ATOM   4724  C  CG2 . VAL A  1 633 ? 36.750  -15.724 -17.125 1.00 55.32  ? 633  VAL A CG2 1 
ATOM   4725  N  N   . HIS A  1 634 ? 34.616  -19.181 -18.083 1.00 43.13  ? 634  HIS A N   1 
ATOM   4726  C  CA  . HIS A  1 634 ? 35.126  -20.541 -17.976 1.00 42.87  ? 634  HIS A CA  1 
ATOM   4727  C  C   . HIS A  1 634 ? 35.962  -20.902 -19.200 1.00 50.17  ? 634  HIS A C   1 
ATOM   4728  O  O   . HIS A  1 634 ? 35.520  -20.741 -20.344 1.00 45.82  ? 634  HIS A O   1 
ATOM   4729  C  CB  . HIS A  1 634 ? 33.986  -21.546 -17.816 1.00 38.26  ? 634  HIS A CB  1 
ATOM   4730  C  CG  . HIS A  1 634 ? 34.462  -22.946 -17.639 1.00 45.33  ? 634  HIS A CG  1 
ATOM   4731  N  ND1 . HIS A  1 634 ? 35.624  -23.245 -16.960 1.00 41.92  ? 634  HIS A ND1 1 
ATOM   4732  C  CD2 . HIS A  1 634 ? 33.955  -24.129 -18.064 1.00 50.01  ? 634  HIS A CD2 1 
ATOM   4733  C  CE1 . HIS A  1 634 ? 35.811  -24.555 -16.973 1.00 49.95  ? 634  HIS A CE1 1 
ATOM   4734  N  NE2 . HIS A  1 634 ? 34.812  -25.115 -17.636 1.00 53.14  ? 634  HIS A NE2 1 
ATOM   4735  N  N   . TYR A  1 635 ? 37.171  -21.394 -18.948 1.00 52.85  ? 635  TYR A N   1 
ATOM   4736  C  CA  . TYR A  1 635 ? 38.065  -21.828 -20.014 1.00 51.66  ? 635  TYR A CA  1 
ATOM   4737  C  C   . TYR A  1 635 ? 38.056  -23.335 -20.159 1.00 52.23  ? 635  TYR A C   1 
ATOM   4738  O  O   . TYR A  1 635 ? 38.264  -24.065 -19.190 1.00 51.53  ? 635  TYR A O   1 
ATOM   4739  C  CB  . TYR A  1 635 ? 39.482  -21.346 -19.747 1.00 48.35  ? 635  TYR A CB  1 
ATOM   4740  C  CG  . TYR A  1 635 ? 39.517  -19.883 -19.456 1.00 51.92  ? 635  TYR A CG  1 
ATOM   4741  C  CD1 . TYR A  1 635 ? 39.534  -18.957 -20.487 1.00 45.85  ? 635  TYR A CD1 1 
ATOM   4742  C  CD2 . TYR A  1 635 ? 39.485  -19.415 -18.147 1.00 55.34  ? 635  TYR A CD2 1 
ATOM   4743  C  CE1 . TYR A  1 635 ? 39.554  -17.611 -20.229 1.00 53.14  ? 635  TYR A CE1 1 
ATOM   4744  C  CE2 . TYR A  1 635 ? 39.495  -18.059 -17.882 1.00 48.50  ? 635  TYR A CE2 1 
ATOM   4745  C  CZ  . TYR A  1 635 ? 39.534  -17.164 -18.927 1.00 51.11  ? 635  TYR A CZ  1 
ATOM   4746  O  OH  . TYR A  1 635 ? 39.547  -15.808 -18.671 1.00 63.34  ? 635  TYR A OH  1 
ATOM   4747  N  N   . GLU A  1 636 ? 37.817  -23.803 -21.377 1.00 58.04  ? 636  GLU A N   1 
ATOM   4748  C  CA  . GLU A  1 636 ? 37.922  -25.235 -21.666 1.00 63.08  ? 636  GLU A CA  1 
ATOM   4749  C  C   . GLU A  1 636 ? 39.354  -25.643 -22.027 1.00 59.64  ? 636  GLU A C   1 
ATOM   4750  O  O   . GLU A  1 636 ? 40.294  -24.837 -21.953 1.00 57.21  ? 636  GLU A O   1 
ATOM   4751  C  CB  . GLU A  1 636 ? 36.959  -25.621 -22.787 1.00 55.85  ? 636  GLU A CB  1 
ATOM   4752  C  CG  . GLU A  1 636 ? 35.599  -26.030 -22.268 1.00 53.05  ? 636  GLU A CG  1 
ATOM   4753  C  CD  . GLU A  1 636 ? 34.503  -25.847 -23.293 1.00 61.22  ? 636  GLU A CD  1 
ATOM   4754  O  OE1 . GLU A  1 636 ? 34.734  -25.138 -24.295 1.00 65.84  ? 636  GLU A OE1 1 
ATOM   4755  O  OE2 . GLU A  1 636 ? 33.405  -26.410 -23.094 1.00 67.08  ? 636  GLU A OE2 1 
ATOM   4756  N  N   . GLY A  1 637 ? 39.520  -26.903 -22.402 1.00 61.06  ? 637  GLY A N   1 
ATOM   4757  C  CA  . GLY A  1 637 ? 40.828  -27.394 -22.787 1.00 67.06  ? 637  GLY A CA  1 
ATOM   4758  C  C   . GLY A  1 637 ? 41.775  -27.308 -21.614 1.00 65.28  ? 637  GLY A C   1 
ATOM   4759  O  O   . GLY A  1 637 ? 41.447  -27.747 -20.518 1.00 62.74  ? 637  GLY A O   1 
ATOM   4760  N  N   . HIS A  1 638 ? 42.949  -26.730 -21.833 1.00 70.27  ? 638  HIS A N   1 
ATOM   4761  C  CA  . HIS A  1 638 ? 43.909  -26.585 -20.747 1.00 72.93  ? 638  HIS A CA  1 
ATOM   4762  C  C   . HIS A  1 638 ? 44.010  -25.123 -20.302 1.00 70.62  ? 638  HIS A C   1 
ATOM   4763  O  O   . HIS A  1 638 ? 44.971  -24.742 -19.630 1.00 69.41  ? 638  HIS A O   1 
ATOM   4764  C  CB  . HIS A  1 638 ? 45.282  -27.135 -21.165 1.00 73.78  ? 638  HIS A CB  1 
ATOM   4765  C  CG  . HIS A  1 638 ? 45.256  -28.582 -21.560 1.00 79.72  ? 638  HIS A CG  1 
ATOM   4766  N  ND1 . HIS A  1 638 ? 45.025  -29.599 -20.657 1.00 84.35  ? 638  HIS A ND1 1 
ATOM   4767  C  CD2 . HIS A  1 638 ? 45.430  -29.183 -22.763 1.00 80.20  ? 638  HIS A CD2 1 
ATOM   4768  C  CE1 . HIS A  1 638 ? 45.052  -30.761 -21.287 1.00 82.76  ? 638  HIS A CE1 1 
ATOM   4769  N  NE2 . HIS A  1 638 ? 45.300  -30.537 -22.565 1.00 80.90  ? 638  HIS A NE2 1 
ATOM   4770  N  N   . GLY A  1 639 ? 43.003  -24.321 -20.669 1.00 66.50  ? 639  GLY A N   1 
ATOM   4771  C  CA  . GLY A  1 639 ? 42.927  -22.914 -20.290 1.00 58.59  ? 639  GLY A CA  1 
ATOM   4772  C  C   . GLY A  1 639 ? 43.165  -22.611 -18.818 1.00 54.11  ? 639  GLY A C   1 
ATOM   4773  O  O   . GLY A  1 639 ? 44.011  -21.778 -18.482 1.00 55.44  ? 639  GLY A O   1 
ATOM   4774  N  N   . TRP A  1 640 ? 42.428  -23.290 -17.942 1.00 48.25  ? 640  TRP A N   1 
ATOM   4775  C  CA  . TRP A  1 640 ? 42.619  -23.128 -16.500 1.00 53.00  ? 640  TRP A CA  1 
ATOM   4776  C  C   . TRP A  1 640 ? 44.007  -23.562 -16.032 1.00 58.14  ? 640  TRP A C   1 
ATOM   4777  O  O   . TRP A  1 640 ? 44.519  -23.039 -15.039 1.00 52.01  ? 640  TRP A O   1 
ATOM   4778  C  CB  . TRP A  1 640 ? 41.556  -23.902 -15.709 1.00 46.59  ? 640  TRP A CB  1 
ATOM   4779  C  CG  . TRP A  1 640 ? 40.250  -23.191 -15.652 1.00 48.54  ? 640  TRP A CG  1 
ATOM   4780  C  CD1 . TRP A  1 640 ? 39.073  -23.589 -16.209 1.00 41.96  ? 640  TRP A CD1 1 
ATOM   4781  C  CD2 . TRP A  1 640 ? 39.990  -21.935 -15.011 1.00 49.76  ? 640  TRP A CD2 1 
ATOM   4782  N  NE1 . TRP A  1 640 ? 38.097  -22.656 -15.960 1.00 46.50  ? 640  TRP A NE1 1 
ATOM   4783  C  CE2 . TRP A  1 640 ? 38.634  -21.633 -15.221 1.00 49.99  ? 640  TRP A CE2 1 
ATOM   4784  C  CE3 . TRP A  1 640 ? 40.778  -21.036 -14.278 1.00 50.47  ? 640  TRP A CE3 1 
ATOM   4785  C  CZ2 . TRP A  1 640 ? 38.044  -20.470 -14.728 1.00 43.61  ? 640  TRP A CZ2 1 
ATOM   4786  C  CZ3 . TRP A  1 640 ? 40.192  -19.881 -13.789 1.00 45.37  ? 640  TRP A CZ3 1 
ATOM   4787  C  CH2 . TRP A  1 640 ? 38.838  -19.610 -14.017 1.00 48.13  ? 640  TRP A CH2 1 
ATOM   4788  N  N   . ASP A  1 641 ? 44.615  -24.516 -16.735 1.00 58.06  ? 641  ASP A N   1 
ATOM   4789  C  CA  . ASP A  1 641 ? 45.950  -24.973 -16.355 1.00 57.72  ? 641  ASP A CA  1 
ATOM   4790  C  C   . ASP A  1 641 ? 47.008  -24.006 -16.880 1.00 59.21  ? 641  ASP A C   1 
ATOM   4791  O  O   . ASP A  1 641 ? 48.034  -23.794 -16.237 1.00 57.92  ? 641  ASP A O   1 
ATOM   4792  C  CB  . ASP A  1 641 ? 46.214  -26.389 -16.863 1.00 64.86  ? 641  ASP A CB  1 
ATOM   4793  C  CG  . ASP A  1 641 ? 45.406  -27.435 -16.119 1.00 72.76  ? 641  ASP A CG  1 
ATOM   4794  O  OD1 . ASP A  1 641 ? 45.835  -27.843 -15.016 1.00 82.26  ? 641  ASP A OD1 1 
ATOM   4795  O  OD2 . ASP A  1 641 ? 44.346  -27.852 -16.636 1.00 69.18  ? 641  ASP A OD2 1 
ATOM   4796  N  N   . GLN A  1 642 ? 46.765  -23.418 -18.046 1.00 54.12  ? 642  GLN A N   1 
ATOM   4797  C  CA  . GLN A  1 642 ? 47.643  -22.361 -18.513 1.00 59.74  ? 642  GLN A CA  1 
ATOM   4798  C  C   . GLN A  1 642 ? 47.671  -21.238 -17.463 1.00 57.60  ? 642  GLN A C   1 
ATOM   4799  O  O   . GLN A  1 642 ? 48.743  -20.803 -17.033 1.00 56.16  ? 642  GLN A O   1 
ATOM   4800  C  CB  . GLN A  1 642 ? 47.195  -21.827 -19.877 1.00 64.00  ? 642  GLN A CB  1 
ATOM   4801  C  CG  . GLN A  1 642 ? 47.100  -22.874 -21.001 1.00 72.31  ? 642  GLN A CG  1 
ATOM   4802  C  CD  . GLN A  1 642 ? 48.398  -23.653 -21.242 1.00 81.92  ? 642  GLN A CD  1 
ATOM   4803  O  OE1 . GLN A  1 642 ? 49.205  -23.300 -22.110 1.00 86.28  ? 642  GLN A OE1 1 
ATOM   4804  N  NE2 . GLN A  1 642 ? 48.586  -24.735 -20.491 1.00 81.27  ? 642  GLN A NE2 1 
ATOM   4805  N  N   . LEU A  1 643 ? 46.490  -20.806 -17.021 1.00 50.00  ? 643  LEU A N   1 
ATOM   4806  C  CA  . LEU A  1 643 ? 46.398  -19.679 -16.110 1.00 47.27  ? 643  LEU A CA  1 
ATOM   4807  C  C   . LEU A  1 643 ? 46.952  -20.038 -14.736 1.00 52.40  ? 643  LEU A C   1 
ATOM   4808  O  O   . LEU A  1 643 ? 47.717  -19.260 -14.156 1.00 52.48  ? 643  LEU A O   1 
ATOM   4809  C  CB  . LEU A  1 643 ? 44.953  -19.189 -16.021 1.00 50.65  ? 643  LEU A CB  1 
ATOM   4810  C  CG  . LEU A  1 643 ? 44.425  -18.622 -17.344 1.00 41.98  ? 643  LEU A CG  1 
ATOM   4811  C  CD1 . LEU A  1 643 ? 42.934  -18.645 -17.404 1.00 37.98  ? 643  LEU A CD1 1 
ATOM   4812  C  CD2 . LEU A  1 643 ? 44.941  -17.216 -17.581 1.00 39.58  ? 643  LEU A CD2 1 
ATOM   4813  N  N   . ILE A  1 644 ? 46.612  -21.219 -14.221 1.00 50.83  ? 644  ILE A N   1 
ATOM   4814  C  CA  . ILE A  1 644 ? 47.188  -21.625 -12.949 1.00 48.59  ? 644  ILE A CA  1 
ATOM   4815  C  C   . ILE A  1 644 ? 48.704  -21.808 -13.064 1.00 53.09  ? 644  ILE A C   1 
ATOM   4816  O  O   . ILE A  1 644 ? 49.440  -21.430 -12.144 1.00 58.91  ? 644  ILE A O   1 
ATOM   4817  C  CB  . ILE A  1 644 ? 46.553  -22.917 -12.396 1.00 53.29  ? 644  ILE A CB  1 
ATOM   4818  C  CG1 . ILE A  1 644 ? 45.054  -22.724 -12.191 1.00 56.24  ? 644  ILE A CG1 1 
ATOM   4819  C  CG2 . ILE A  1 644 ? 47.158  -23.277 -11.034 1.00 38.75  ? 644  ILE A CG2 1 
ATOM   4820  C  CD1 . ILE A  1 644 ? 44.367  -23.904 -11.556 1.00 47.20  ? 644  ILE A CD1 1 
ATOM   4821  N  N   . THR A  1 645 ? 49.182  -22.364 -14.178 1.00 53.44  ? 645  THR A N   1 
ATOM   4822  C  CA  . THR A  1 645 ? 50.632  -22.505 -14.370 1.00 58.87  ? 645  THR A CA  1 
ATOM   4823  C  C   . THR A  1 645 ? 51.270  -21.131 -14.292 1.00 55.23  ? 645  THR A C   1 
ATOM   4824  O  O   . THR A  1 645 ? 52.235  -20.906 -13.546 1.00 56.56  ? 645  THR A O   1 
ATOM   4825  C  CB  . THR A  1 645 ? 51.026  -23.140 -15.726 1.00 56.38  ? 645  THR A CB  1 
ATOM   4826  O  OG1 . THR A  1 645 ? 50.618  -24.504 -15.770 1.00 55.48  ? 645  THR A OG1 1 
ATOM   4827  C  CG2 . THR A  1 645 ? 52.531  -23.094 -15.905 1.00 55.85  ? 645  THR A CG2 1 
ATOM   4828  N  N   . GLN A  1 646 ? 50.704  -20.217 -15.068 1.00 49.93  ? 646  GLN A N   1 
ATOM   4829  C  CA  . GLN A  1 646 ? 51.176  -18.851 -15.118 1.00 54.03  ? 646  GLN A CA  1 
ATOM   4830  C  C   . GLN A  1 646 ? 51.285  -18.228 -13.727 1.00 57.79  ? 646  GLN A C   1 
ATOM   4831  O  O   . GLN A  1 646 ? 52.279  -17.576 -13.416 1.00 59.45  ? 646  GLN A O   1 
ATOM   4832  C  CB  . GLN A  1 646 ? 50.251  -18.014 -15.988 1.00 54.94  ? 646  GLN A CB  1 
ATOM   4833  C  CG  . GLN A  1 646 ? 50.661  -16.563 -16.037 1.00 56.23  ? 646  GLN A CG  1 
ATOM   4834  C  CD  . GLN A  1 646 ? 52.012  -16.366 -16.687 1.00 56.27  ? 646  GLN A CD  1 
ATOM   4835  O  OE1 . GLN A  1 646 ? 52.114  -16.320 -17.907 1.00 55.88  ? 646  GLN A OE1 1 
ATOM   4836  N  NE2 . GLN A  1 646 ? 53.052  -16.229 -15.874 1.00 54.38  ? 646  GLN A NE2 1 
ATOM   4837  N  N   . LEU A  1 647 ? 50.271  -18.448 -12.892 1.00 52.93  ? 647  LEU A N   1 
ATOM   4838  C  CA  . LEU A  1 647 ? 50.234  -17.868 -11.548 1.00 52.13  ? 647  LEU A CA  1 
ATOM   4839  C  C   . LEU A  1 647 ? 51.327  -18.391 -10.630 1.00 54.10  ? 647  LEU A C   1 
ATOM   4840  O  O   . LEU A  1 647 ? 51.926  -17.633 -9.869  1.00 57.17  ? 647  LEU A O   1 
ATOM   4841  C  CB  . LEU A  1 647 ? 48.872  -18.126 -10.904 1.00 54.50  ? 647  LEU A CB  1 
ATOM   4842  C  CG  . LEU A  1 647 ? 47.762  -17.162 -11.322 1.00 51.36  ? 647  LEU A CG  1 
ATOM   4843  C  CD1 . LEU A  1 647 ? 46.406  -17.809 -11.156 1.00 44.82  ? 647  LEU A CD1 1 
ATOM   4844  C  CD2 . LEU A  1 647 ? 47.865  -15.881 -10.514 1.00 44.00  ? 647  LEU A CD2 1 
ATOM   4845  N  N   . ASN A  1 648 ? 51.577  -19.695 -10.683 1.00 62.02  ? 648  ASN A N   1 
ATOM   4846  C  CA  . ASN A  1 648 ? 52.595  -20.291 -9.823  1.00 54.79  ? 648  ASN A CA  1 
ATOM   4847  C  C   . ASN A  1 648 ? 54.009  -19.909 -10.256 1.00 55.34  ? 648  ASN A C   1 
ATOM   4848  O  O   . ASN A  1 648 ? 54.933  -19.913 -9.445  1.00 55.96  ? 648  ASN A O   1 
ATOM   4849  C  CB  . ASN A  1 648 ? 52.431  -21.804 -9.792  1.00 45.52  ? 648  ASN A CB  1 
ATOM   4850  C  CG  . ASN A  1 648 ? 51.296  -22.243 -8.880  1.00 50.01  ? 648  ASN A CG  1 
ATOM   4851  O  OD1 . ASN A  1 648 ? 51.447  -22.303 -7.649  1.00 46.41  ? 648  ASN A OD1 1 
ATOM   4852  N  ND2 . ASN A  1 648 ? 50.154  -22.558 -9.478  1.00 47.84  ? 648  ASN A ND2 1 
ATOM   4853  N  N   . GLN A  1 649 ? 54.168  -19.553 -11.529 1.00 52.47  ? 649  GLN A N   1 
ATOM   4854  C  CA  . GLN A  1 649 ? 55.488  -19.256 -12.067 1.00 56.97  ? 649  GLN A CA  1 
ATOM   4855  C  C   . GLN A  1 649 ? 55.797  -17.765 -12.135 1.00 61.13  ? 649  GLN A C   1 
ATOM   4856  O  O   . GLN A  1 649 ? 56.856  -17.339 -11.689 1.00 66.52  ? 649  GLN A O   1 
ATOM   4857  C  CB  . GLN A  1 649 ? 55.642  -19.898 -13.446 1.00 60.60  ? 649  GLN A CB  1 
ATOM   4858  C  CG  . GLN A  1 649 ? 56.636  -21.054 -13.439 1.00 59.47  ? 649  GLN A CG  1 
ATOM   4859  C  CD  . GLN A  1 649 ? 56.213  -22.192 -14.344 1.00 73.77  ? 649  GLN A CD  1 
ATOM   4860  O  OE1 . GLN A  1 649 ? 55.897  -21.989 -15.521 1.00 71.72  ? 649  GLN A OE1 1 
ATOM   4861  N  NE2 . GLN A  1 649 ? 56.192  -23.403 -13.793 1.00 82.45  ? 649  GLN A NE2 1 
ATOM   4862  N  N   . ASN A  1 650 ? 54.890  -16.974 -12.700 1.00 55.18  ? 650  ASN A N   1 
ATOM   4863  C  CA  . ASN A  1 650 ? 54.987  -15.524 -12.578 1.00 63.71  ? 650  ASN A CA  1 
ATOM   4864  C  C   . ASN A  1 650 ? 53.631  -14.852 -12.520 1.00 61.63  ? 650  ASN A C   1 
ATOM   4865  O  O   . ASN A  1 650 ? 53.098  -14.426 -13.550 1.00 59.18  ? 650  ASN A O   1 
ATOM   4866  C  CB  . ASN A  1 650 ? 55.793  -14.920 -13.719 1.00 68.55  ? 650  ASN A CB  1 
ATOM   4867  C  CG  . ASN A  1 650 ? 56.864  -13.995 -13.221 1.00 76.46  ? 650  ASN A CG  1 
ATOM   4868  O  OD1 . ASN A  1 650 ? 57.038  -13.844 -12.018 1.00 81.01  ? 650  ASN A OD1 1 
ATOM   4869  N  ND2 . ASN A  1 650 ? 57.590  -13.367 -14.138 1.00 92.60  ? 650  ASN A ND2 1 
ATOM   4870  N  N   . HIS A  1 651 ? 53.092  -14.747 -11.305 1.00 59.05  ? 651  HIS A N   1 
ATOM   4871  C  CA  . HIS A  1 651 ? 51.731  -14.267 -11.118 1.00 60.01  ? 651  HIS A CA  1 
ATOM   4872  C  C   . HIS A  1 651 ? 51.587  -12.823 -11.579 1.00 54.91  ? 651  HIS A C   1 
ATOM   4873  O  O   . HIS A  1 651 ? 50.544  -12.441 -12.113 1.00 52.52  ? 651  HIS A O   1 
ATOM   4874  C  CB  . HIS A  1 651 ? 51.290  -14.424 -9.659  1.00 52.28  ? 651  HIS A CB  1 
ATOM   4875  C  CG  . HIS A  1 651 ? 52.062  -13.591 -8.683  1.00 52.53  ? 651  HIS A CG  1 
ATOM   4876  N  ND1 . HIS A  1 651 ? 51.540  -12.459 -8.094  1.00 49.45  ? 651  HIS A ND1 1 
ATOM   4877  C  CD2 . HIS A  1 651 ? 53.297  -13.753 -8.155  1.00 52.80  ? 651  HIS A CD2 1 
ATOM   4878  C  CE1 . HIS A  1 651 ? 52.428  -11.951 -7.260  1.00 53.56  ? 651  HIS A CE1 1 
ATOM   4879  N  NE2 . HIS A  1 651 ? 53.500  -12.722 -7.273  1.00 47.87  ? 651  HIS A NE2 1 
ATOM   4880  N  N   . THR A  1 652 ? 52.655  -12.051 -11.417 1.00 55.38  ? 652  THR A N   1 
ATOM   4881  C  CA  . THR A  1 652 ? 52.687  -10.656 -11.839 1.00 55.50  ? 652  THR A CA  1 
ATOM   4882  C  C   . THR A  1 652 ? 52.361  -10.439 -13.319 1.00 59.02  ? 652  THR A C   1 
ATOM   4883  O  O   . THR A  1 652 ? 51.888  -9.368  -13.690 1.00 63.71  ? 652  THR A O   1 
ATOM   4884  C  CB  . THR A  1 652 ? 54.050  -10.046 -11.546 1.00 61.84  ? 652  THR A CB  1 
ATOM   4885  O  OG1 . THR A  1 652 ? 55.068  -10.972 -11.950 1.00 72.42  ? 652  THR A OG1 1 
ATOM   4886  C  CG2 . THR A  1 652 ? 54.190  -9.763  -10.051 1.00 46.62  ? 652  THR A CG2 1 
ATOM   4887  N  N   . LEU A  1 653 ? 52.590  -11.445 -14.161 1.00 58.85  ? 653  LEU A N   1 
ATOM   4888  C  CA  . LEU A  1 653 ? 52.239  -11.337 -15.583 1.00 61.11  ? 653  LEU A CA  1 
ATOM   4889  C  C   . LEU A  1 653 ? 50.729  -11.299 -15.832 1.00 58.17  ? 653  LEU A C   1 
ATOM   4890  O  O   . LEU A  1 653 ? 50.289  -11.089 -16.958 1.00 63.50  ? 653  LEU A O   1 
ATOM   4891  C  CB  . LEU A  1 653 ? 52.843  -12.494 -16.389 1.00 65.01  ? 653  LEU A CB  1 
ATOM   4892  C  CG  . LEU A  1 653 ? 54.366  -12.663 -16.380 1.00 71.39  ? 653  LEU A CG  1 
ATOM   4893  C  CD1 . LEU A  1 653 ? 54.792  -13.564 -17.532 1.00 67.72  ? 653  LEU A CD1 1 
ATOM   4894  C  CD2 . LEU A  1 653 ? 55.084  -11.323 -16.420 1.00 64.33  ? 653  LEU A CD2 1 
ATOM   4895  N  N   . LEU A  1 654 ? 49.937  -11.540 -14.795 1.00 60.28  ? 654  LEU A N   1 
ATOM   4896  C  CA  . LEU A  1 654 ? 48.506  -11.265 -14.851 1.00 58.55  ? 654  LEU A CA  1 
ATOM   4897  C  C   . LEU A  1 654 ? 48.259  -10.022 -14.002 1.00 51.19  ? 654  LEU A C   1 
ATOM   4898  O  O   . LEU A  1 654 ? 48.919  -9.832  -12.991 1.00 52.68  ? 654  LEU A O   1 
ATOM   4899  C  CB  . LEU A  1 654 ? 47.689  -12.466 -14.361 1.00 50.93  ? 654  LEU A CB  1 
ATOM   4900  C  CG  . LEU A  1 654 ? 47.668  -13.670 -15.309 1.00 49.64  ? 654  LEU A CG  1 
ATOM   4901  C  CD1 . LEU A  1 654 ? 47.481  -14.958 -14.541 1.00 53.89  ? 654  LEU A CD1 1 
ATOM   4902  C  CD2 . LEU A  1 654 ? 46.577  -13.538 -16.341 1.00 53.88  ? 654  LEU A CD2 1 
ATOM   4903  N  N   . ARG A  1 655 ? 47.346  -9.160  -14.431 1.00 52.27  ? 655  ARG A N   1 
ATOM   4904  C  CA  . ARG A  1 655 ? 47.007  -7.951  -13.670 1.00 54.83  ? 655  ARG A CA  1 
ATOM   4905  C  C   . ARG A  1 655 ? 46.427  -8.291  -12.292 1.00 50.43  ? 655  ARG A C   1 
ATOM   4906  O  O   . ARG A  1 655 ? 45.749  -9.314  -12.149 1.00 50.71  ? 655  ARG A O   1 
ATOM   4907  C  CB  . ARG A  1 655 ? 46.020  -7.092  -14.468 1.00 56.90  ? 655  ARG A CB  1 
ATOM   4908  C  CG  . ARG A  1 655 ? 46.513  -6.783  -15.878 1.00 56.26  ? 655  ARG A CG  1 
ATOM   4909  C  CD  . ARG A  1 655 ? 45.426  -6.234  -16.752 1.00 50.39  ? 655  ARG A CD  1 
ATOM   4910  N  NE  . ARG A  1 655 ? 44.807  -5.094  -16.110 1.00 67.37  ? 655  ARG A NE  1 
ATOM   4911  C  CZ  . ARG A  1 655 ? 45.349  -3.882  -16.064 1.00 73.76  ? 655  ARG A CZ  1 
ATOM   4912  N  NH1 . ARG A  1 655 ? 46.526  -3.660  -16.634 1.00 75.21  ? 655  ARG A NH1 1 
ATOM   4913  N  NH2 . ARG A  1 655 ? 44.714  -2.893  -15.440 1.00 71.05  ? 655  ARG A NH2 1 
ATOM   4914  N  N   . PRO A  1 656 ? 46.725  -7.453  -11.270 1.00 47.83  ? 656  PRO A N   1 
ATOM   4915  C  CA  . PRO A  1 656 ? 46.270  -7.673  -9.888  1.00 41.48  ? 656  PRO A CA  1 
ATOM   4916  C  C   . PRO A  1 656 ? 44.790  -7.974  -9.796  1.00 41.98  ? 656  PRO A C   1 
ATOM   4917  O  O   . PRO A  1 656 ? 44.394  -8.847  -9.041  1.00 46.77  ? 656  PRO A O   1 
ATOM   4918  C  CB  . PRO A  1 656 ? 46.600  -6.351  -9.202  1.00 41.08  ? 656  PRO A CB  1 
ATOM   4919  C  CG  . PRO A  1 656 ? 47.813  -5.866  -9.918  1.00 43.66  ? 656  PRO A CG  1 
ATOM   4920  C  CD  . PRO A  1 656 ? 47.693  -6.340  -11.350 1.00 43.85  ? 656  PRO A CD  1 
ATOM   4921  N  N   . LYS A  1 657 ? 43.977  -7.276  -10.570 1.00 44.22  ? 657  LYS A N   1 
ATOM   4922  C  CA  . LYS A  1 657 ? 42.548  -7.530  -10.551 1.00 38.89  ? 657  LYS A CA  1 
ATOM   4923  C  C   . LYS A  1 657 ? 42.176  -8.730  -11.393 1.00 45.76  ? 657  LYS A C   1 
ATOM   4924  O  O   . LYS A  1 657 ? 41.123  -9.334  -11.184 1.00 48.13  ? 657  LYS A O   1 
ATOM   4925  C  CB  . LYS A  1 657 ? 41.784  -6.305  -11.023 1.00 37.50  ? 657  LYS A CB  1 
ATOM   4926  C  CG  . LYS A  1 657 ? 41.683  -5.234  -9.963  1.00 38.02  ? 657  LYS A CG  1 
ATOM   4927  C  CD  . LYS A  1 657 ? 41.040  -3.973  -10.506 1.00 43.66  ? 657  LYS A CD  1 
ATOM   4928  C  CE  . LYS A  1 657 ? 40.686  -3.008  -9.381  1.00 52.66  ? 657  LYS A CE  1 
ATOM   4929  N  NZ  . LYS A  1 657 ? 40.044  -1.752  -9.891  1.00 53.85  ? 657  LYS A NZ  1 
ATOM   4930  N  N   . ASP A  1 658 ? 43.023  -9.075  -12.361 1.00 51.95  ? 658  ASP A N   1 
ATOM   4931  C  CA  . ASP A  1 658 ? 42.805  -10.303 -13.117 1.00 47.71  ? 658  ASP A CA  1 
ATOM   4932  C  C   . ASP A  1 658 ? 42.966  -11.468 -12.123 1.00 45.03  ? 658  ASP A C   1 
ATOM   4933  O  O   . ASP A  1 658 ? 42.156  -12.399 -12.100 1.00 41.57  ? 658  ASP A O   1 
ATOM   4934  C  CB  . ASP A  1 658 ? 43.761  -10.414 -14.315 1.00 52.75  ? 658  ASP A CB  1 
ATOM   4935  C  CG  . ASP A  1 658 ? 43.208  -9.743  -15.598 1.00 56.12  ? 658  ASP A CG  1 
ATOM   4936  O  OD1 . ASP A  1 658 ? 42.020  -9.361  -15.636 1.00 56.90  ? 658  ASP A OD1 1 
ATOM   4937  O  OD2 . ASP A  1 658 ? 43.960  -9.618  -16.588 1.00 56.58  ? 658  ASP A OD2 1 
ATOM   4938  N  N   . ARG A  1 659 ? 43.963  -11.372 -11.252 1.00 40.80  ? 659  ARG A N   1 
ATOM   4939  C  CA  . ARG A  1 659 ? 44.161  -12.400 -10.238 1.00 43.58  ? 659  ARG A CA  1 
ATOM   4940  C  C   . ARG A  1 659 ? 42.963  -12.518 -9.305  1.00 46.40  ? 659  ARG A C   1 
ATOM   4941  O  O   . ARG A  1 659 ? 42.565  -13.628 -8.955  1.00 49.10  ? 659  ARG A O   1 
ATOM   4942  C  CB  . ARG A  1 659 ? 45.416  -12.131 -9.415  1.00 45.85  ? 659  ARG A CB  1 
ATOM   4943  C  CG  . ARG A  1 659 ? 46.694  -12.078 -10.226 1.00 43.00  ? 659  ARG A CG  1 
ATOM   4944  C  CD  . ARG A  1 659 ? 47.871  -11.869 -9.306  1.00 43.91  ? 659  ARG A CD  1 
ATOM   4945  N  NE  . ARG A  1 659 ? 48.679  -10.785 -9.825  1.00 51.77  ? 659  ARG A NE  1 
ATOM   4946  C  CZ  . ARG A  1 659 ? 49.215  -9.821  -9.090  1.00 47.72  ? 659  ARG A CZ  1 
ATOM   4947  N  NH1 . ARG A  1 659 ? 49.048  -9.798  -7.774  1.00 42.23  ? 659  ARG A NH1 1 
ATOM   4948  N  NH2 . ARG A  1 659 ? 49.929  -8.882  -9.687  1.00 50.57  ? 659  ARG A NH2 1 
ATOM   4949  N  N   . VAL A  1 660 ? 42.381  -11.391 -8.904  1.00 43.43  ? 660  VAL A N   1 
ATOM   4950  C  CA  . VAL A  1 660 ? 41.233  -11.435 -8.002  1.00 44.56  ? 660  VAL A CA  1 
ATOM   4951  C  C   . VAL A  1 660 ? 40.052  -12.131 -8.680  1.00 37.67  ? 660  VAL A C   1 
ATOM   4952  O  O   . VAL A  1 660 ? 39.394  -12.965 -8.073  1.00 37.90  ? 660  VAL A O   1 
ATOM   4953  C  CB  . VAL A  1 660 ? 40.819  -10.006 -7.516  1.00 45.91  ? 660  VAL A CB  1 
ATOM   4954  C  CG1 . VAL A  1 660 ? 39.393  -9.990  -7.040  1.00 36.41  ? 660  VAL A CG1 1 
ATOM   4955  C  CG2 . VAL A  1 660 ? 41.719  -9.557  -6.392  1.00 42.50  ? 660  VAL A CG2 1 
ATOM   4956  N  N   . GLY A  1 661 ? 39.818  -11.819 -9.946  1.00 39.27  ? 661  GLY A N   1 
ATOM   4957  C  CA  . GLY A  1 661 ? 38.699  -12.385 -10.678 1.00 35.56  ? 661  GLY A CA  1 
ATOM   4958  C  C   . GLY A  1 661 ? 38.886  -13.856 -10.997 1.00 41.46  ? 661  GLY A C   1 
ATOM   4959  O  O   . GLY A  1 661 ? 37.917  -14.622 -11.034 1.00 41.07  ? 661  GLY A O   1 
ATOM   4960  N  N   . LEU A  1 662 ? 40.132  -14.262 -11.221 1.00 42.55  ? 662  LEU A N   1 
ATOM   4961  C  CA  . LEU A  1 662 ? 40.423  -15.676 -11.485 1.00 42.58  ? 662  LEU A CA  1 
ATOM   4962  C  C   . LEU A  1 662 ? 40.120  -16.510 -10.251 1.00 40.35  ? 662  LEU A C   1 
ATOM   4963  O  O   . LEU A  1 662 ? 39.358  -17.463 -10.294 1.00 34.41  ? 662  LEU A O   1 
ATOM   4964  C  CB  . LEU A  1 662 ? 41.873  -15.861 -11.908 1.00 41.90  ? 662  LEU A CB  1 
ATOM   4965  C  CG  . LEU A  1 662 ? 42.167  -15.246 -13.274 1.00 46.75  ? 662  LEU A CG  1 
ATOM   4966  C  CD1 . LEU A  1 662 ? 43.669  -15.181 -13.511 1.00 43.96  ? 662  LEU A CD1 1 
ATOM   4967  C  CD2 . LEU A  1 662 ? 41.431  -15.996 -14.375 1.00 37.07  ? 662  LEU A CD2 1 
ATOM   4968  N  N   . ILE A  1 663 ? 40.693  -16.102 -9.132  1.00 44.08  ? 663  ILE A N   1 
ATOM   4969  C  CA  . ILE A  1 663 ? 40.424  -16.768 -7.884  1.00 36.81  ? 663  ILE A CA  1 
ATOM   4970  C  C   . ILE A  1 663 ? 38.929  -16.873 -7.641  1.00 37.56  ? 663  ILE A C   1 
ATOM   4971  O  O   . ILE A  1 663 ? 38.423  -17.964 -7.365  1.00 38.46  ? 663  ILE A O   1 
ATOM   4972  C  CB  . ILE A  1 663 ? 41.093  -16.058 -6.758  1.00 37.18  ? 663  ILE A CB  1 
ATOM   4973  C  CG1 . ILE A  1 663 ? 42.593  -16.026 -7.027  1.00 36.10  ? 663  ILE A CG1 1 
ATOM   4974  C  CG2 . ILE A  1 663 ? 40.800  -16.780 -5.463  1.00 39.06  ? 663  ILE A CG2 1 
ATOM   4975  C  CD1 . ILE A  1 663 ? 43.395  -15.213 -6.015  1.00 45.61  ? 663  ILE A CD1 1 
ATOM   4976  N  N   . HIS A  1 664 ? 38.216  -15.762 -7.801  1.00 35.44  ? 664  HIS A N   1 
ATOM   4977  C  CA  . HIS A  1 664 ? 36.768  -15.787 -7.697  1.00 32.97  ? 664  HIS A CA  1 
ATOM   4978  C  C   . HIS A  1 664 ? 36.101  -16.808 -8.638  1.00 35.27  ? 664  HIS A C   1 
ATOM   4979  O  O   . HIS A  1 664 ? 35.355  -17.672 -8.195  1.00 37.23  ? 664  HIS A O   1 
ATOM   4980  C  CB  . HIS A  1 664 ? 36.181  -14.409 -7.979  1.00 32.30  ? 664  HIS A CB  1 
ATOM   4981  C  CG  . HIS A  1 664 ? 34.691  -14.397 -7.924  1.00 28.34  ? 664  HIS A CG  1 
ATOM   4982  N  ND1 . HIS A  1 664 ? 33.907  -14.310 -9.049  1.00 27.05  ? 664  HIS A ND1 1 
ATOM   4983  C  CD2 . HIS A  1 664 ? 33.841  -14.534 -6.881  1.00 26.91  ? 664  HIS A CD2 1 
ATOM   4984  C  CE1 . HIS A  1 664 ? 32.634  -14.364 -8.704  1.00 30.19  ? 664  HIS A CE1 1 
ATOM   4985  N  NE2 . HIS A  1 664 ? 32.567  -14.507 -7.392  1.00 34.97  ? 664  HIS A NE2 1 
ATOM   4986  N  N   . ASP A  1 665 ? 36.368  -16.697 -9.933  1.00 35.87  ? 665  ASP A N   1 
ATOM   4987  C  CA  . ASP A  1 665 ? 35.742  -17.569 -10.913 1.00 38.85  ? 665  ASP A CA  1 
ATOM   4988  C  C   . ASP A  1 665 ? 36.029  -19.075 -10.717 1.00 37.97  ? 665  ASP A C   1 
ATOM   4989  O  O   . ASP A  1 665 ? 35.094  -19.888 -10.818 1.00 35.14  ? 665  ASP A O   1 
ATOM   4990  C  CB  . ASP A  1 665 ? 36.149  -17.142 -12.329 1.00 40.83  ? 665  ASP A CB  1 
ATOM   4991  C  CG  . ASP A  1 665 ? 35.544  -15.795 -12.744 1.00 46.08  ? 665  ASP A CG  1 
ATOM   4992  O  OD1 . ASP A  1 665 ? 34.758  -15.229 -11.942 1.00 46.38  ? 665  ASP A OD1 1 
ATOM   4993  O  OD2 . ASP A  1 665 ? 35.853  -15.311 -13.869 1.00 41.91  ? 665  ASP A OD2 1 
ATOM   4994  N  N   . VAL A  1 666 ? 37.282  -19.444 -10.434 1.00 30.80  ? 666  VAL A N   1 
ATOM   4995  C  CA  . VAL A  1 666 ? 37.622  -20.859 -10.198 1.00 38.60  ? 666  VAL A CA  1 
ATOM   4996  C  C   . VAL A  1 666 ? 36.710  -21.507 -9.153  1.00 43.11  ? 666  VAL A C   1 
ATOM   4997  O  O   . VAL A  1 666 ? 36.176  -22.614 -9.370  1.00 32.41  ? 666  VAL A O   1 
ATOM   4998  C  CB  . VAL A  1 666 ? 39.062  -21.076 -9.693  1.00 44.34  ? 666  VAL A CB  1 
ATOM   4999  C  CG1 . VAL A  1 666 ? 39.461  -22.503 -9.937  1.00 53.63  ? 666  VAL A CG1 1 
ATOM   5000  C  CG2 . VAL A  1 666 ? 40.016  -20.238 -10.425 1.00 49.76  ? 666  VAL A CG2 1 
ATOM   5001  N  N   . PHE A  1 667 ? 36.521  -20.817 -8.025  1.00 35.93  ? 667  PHE A N   1 
ATOM   5002  C  CA  . PHE A  1 667 ? 35.732  -21.413 -6.963  1.00 37.00  ? 667  PHE A CA  1 
ATOM   5003  C  C   . PHE A  1 667 ? 34.240  -21.418 -7.290  1.00 37.31  ? 667  PHE A C   1 
ATOM   5004  O  O   . PHE A  1 667 ? 33.544  -22.353 -6.909  1.00 41.73  ? 667  PHE A O   1 
ATOM   5005  C  CB  . PHE A  1 667 ? 36.003  -20.719 -5.630  1.00 37.24  ? 667  PHE A CB  1 
ATOM   5006  C  CG  . PHE A  1 667 ? 37.273  -21.182 -4.956  1.00 35.83  ? 667  PHE A CG  1 
ATOM   5007  C  CD1 . PHE A  1 667 ? 37.288  -22.343 -4.195  1.00 35.96  ? 667  PHE A CD1 1 
ATOM   5008  C  CD2 . PHE A  1 667 ? 38.447  -20.458 -5.078  1.00 34.06  ? 667  PHE A CD2 1 
ATOM   5009  C  CE1 . PHE A  1 667 ? 38.449  -22.777 -3.562  1.00 38.48  ? 667  PHE A CE1 1 
ATOM   5010  C  CE2 . PHE A  1 667 ? 39.613  -20.881 -4.455  1.00 35.94  ? 667  PHE A CE2 1 
ATOM   5011  C  CZ  . PHE A  1 667 ? 39.617  -22.051 -3.695  1.00 42.26  ? 667  PHE A CZ  1 
ATOM   5012  N  N   . GLN A  1 668 ? 33.751  -20.413 -8.015  1.00 35.00  ? 668  GLN A N   1 
ATOM   5013  C  CA  . GLN A  1 668 ? 32.352  -20.419 -8.430  1.00 34.01  ? 668  GLN A CA  1 
ATOM   5014  C  C   . GLN A  1 668 ? 32.108  -21.601 -9.348  1.00 36.44  ? 668  GLN A C   1 
ATOM   5015  O  O   . GLN A  1 668 ? 31.079  -22.259 -9.289  1.00 39.61  ? 668  GLN A O   1 
ATOM   5016  C  CB  . GLN A  1 668 ? 31.963  -19.138 -9.176  1.00 38.76  ? 668  GLN A CB  1 
ATOM   5017  C  CG  . GLN A  1 668 ? 32.109  -17.863 -8.414  1.00 37.90  ? 668  GLN A CG  1 
ATOM   5018  C  CD  . GLN A  1 668 ? 31.339  -17.884 -7.130  1.00 39.55  ? 668  GLN A CD  1 
ATOM   5019  O  OE1 . GLN A  1 668 ? 30.135  -18.150 -7.115  1.00 44.51  ? 668  GLN A OE1 1 
ATOM   5020  N  NE2 . GLN A  1 668 ? 32.034  -17.618 -6.028  1.00 34.03  ? 668  GLN A NE2 1 
ATOM   5021  N  N   . LEU A  1 669 ? 33.063  -21.846 -10.228 1.00 37.10  ? 669  LEU A N   1 
ATOM   5022  C  CA  . LEU A  1 669 ? 32.887  -22.875 -11.233 1.00 41.76  ? 669  LEU A CA  1 
ATOM   5023  C  C   . LEU A  1 669 ? 32.908  -24.265 -10.604 1.00 40.79  ? 669  LEU A C   1 
ATOM   5024  O  O   . LEU A  1 669 ? 32.179  -25.147 -11.028 1.00 45.62  ? 669  LEU A O   1 
ATOM   5025  C  CB  . LEU A  1 669 ? 33.956  -22.736 -12.309 1.00 39.58  ? 669  LEU A CB  1 
ATOM   5026  C  CG  . LEU A  1 669 ? 33.717  -21.571 -13.258 1.00 37.10  ? 669  LEU A CG  1 
ATOM   5027  C  CD1 . LEU A  1 669 ? 34.935  -21.389 -14.102 1.00 38.77  ? 669  LEU A CD1 1 
ATOM   5028  C  CD2 . LEU A  1 669 ? 32.497  -21.820 -14.121 1.00 36.21  ? 669  LEU A CD2 1 
ATOM   5029  N  N   . VAL A  1 670 ? 33.740  -24.441 -9.587  1.00 37.12  ? 670  VAL A N   1 
ATOM   5030  C  CA  . VAL A  1 670 ? 33.682  -25.637 -8.770  1.00 40.56  ? 670  VAL A CA  1 
ATOM   5031  C  C   . VAL A  1 670 ? 32.247  -25.877 -8.354  1.00 42.15  ? 670  VAL A C   1 
ATOM   5032  O  O   . VAL A  1 670 ? 31.704  -26.963 -8.565  1.00 44.71  ? 670  VAL A O   1 
ATOM   5033  C  CB  . VAL A  1 670 ? 34.578  -25.537 -7.510  1.00 39.18  ? 670  VAL A CB  1 
ATOM   5034  C  CG1 . VAL A  1 670 ? 34.165  -26.565 -6.482  1.00 35.18  ? 670  VAL A CG1 1 
ATOM   5035  C  CG2 . VAL A  1 670 ? 36.030  -25.729 -7.895  1.00 34.55  ? 670  VAL A CG2 1 
ATOM   5036  N  N   . GLY A  1 671 ? 31.622  -24.853 -7.788  1.00 43.64  ? 671  GLY A N   1 
ATOM   5037  C  CA  . GLY A  1 671 ? 30.252  -24.979 -7.329  1.00 42.48  ? 671  GLY A CA  1 
ATOM   5038  C  C   . GLY A  1 671 ? 29.321  -25.237 -8.491  1.00 44.30  ? 671  GLY A C   1 
ATOM   5039  O  O   . GLY A  1 671 ? 28.263  -25.846 -8.339  1.00 47.17  ? 671  GLY A O   1 
ATOM   5040  N  N   . ALA A  1 672 ? 29.726  -24.774 -9.666  1.00 43.18  ? 672  ALA A N   1 
ATOM   5041  C  CA  . ALA A  1 672 ? 28.936  -24.988 -10.870 1.00 51.04  ? 672  ALA A CA  1 
ATOM   5042  C  C   . ALA A  1 672 ? 29.165  -26.391 -11.454 1.00 54.34  ? 672  ALA A C   1 
ATOM   5043  O  O   . ALA A  1 672 ? 28.587  -26.751 -12.483 1.00 56.97  ? 672  ALA A O   1 
ATOM   5044  C  CB  . ALA A  1 672 ? 29.268  -23.920 -11.904 1.00 44.30  ? 672  ALA A CB  1 
ATOM   5045  N  N   . GLY A  1 673 ? 30.014  -27.172 -10.792 1.00 47.17  ? 673  GLY A N   1 
ATOM   5046  C  CA  . GLY A  1 673 ? 30.438  -28.453 -11.322 1.00 51.03  ? 673  GLY A CA  1 
ATOM   5047  C  C   . GLY A  1 673 ? 31.136  -28.407 -12.676 1.00 52.86  ? 673  GLY A C   1 
ATOM   5048  O  O   . GLY A  1 673 ? 31.098  -29.385 -13.417 1.00 58.38  ? 673  GLY A O   1 
ATOM   5049  N  N   . ARG A  1 674 ? 31.776  -27.287 -13.014 1.00 50.03  ? 674  ARG A N   1 
ATOM   5050  C  CA  . ARG A  1 674 ? 32.553  -27.221 -14.253 1.00 52.25  ? 674  ARG A CA  1 
ATOM   5051  C  C   . ARG A  1 674 ? 34.006  -27.557 -13.989 1.00 50.46  ? 674  ARG A C   1 
ATOM   5052  O  O   . ARG A  1 674 ? 34.767  -27.876 -14.905 1.00 52.22  ? 674  ARG A O   1 
ATOM   5053  C  CB  . ARG A  1 674 ? 32.473  -25.839 -14.901 1.00 50.81  ? 674  ARG A CB  1 
ATOM   5054  C  CG  . ARG A  1 674 ? 31.115  -25.467 -15.437 1.00 51.39  ? 674  ARG A CG  1 
ATOM   5055  C  CD  . ARG A  1 674 ? 30.659  -26.365 -16.559 1.00 53.45  ? 674  ARG A CD  1 
ATOM   5056  N  NE  . ARG A  1 674 ? 29.363  -25.906 -17.049 1.00 55.81  ? 674  ARG A NE  1 
ATOM   5057  C  CZ  . ARG A  1 674 ? 29.169  -25.223 -18.173 1.00 50.07  ? 674  ARG A CZ  1 
ATOM   5058  N  NH1 . ARG A  1 674 ? 30.182  -24.918 -18.983 1.00 45.94  ? 674  ARG A NH1 1 
ATOM   5059  N  NH2 . ARG A  1 674 ? 27.942  -24.857 -18.495 1.00 55.75  ? 674  ARG A NH2 1 
ATOM   5060  N  N   . LEU A  1 675 ? 34.391  -27.439 -12.730 1.00 41.55  ? 675  LEU A N   1 
ATOM   5061  C  CA  . LEU A  1 675 ? 35.733  -27.754 -12.311 1.00 40.21  ? 675  LEU A CA  1 
ATOM   5062  C  C   . LEU A  1 675 ? 35.592  -28.578 -11.056 1.00 40.70  ? 675  LEU A C   1 
ATOM   5063  O  O   . LEU A  1 675 ? 34.534  -28.589 -10.447 1.00 43.44  ? 675  LEU A O   1 
ATOM   5064  C  CB  . LEU A  1 675 ? 36.546  -26.493 -12.046 1.00 42.37  ? 675  LEU A CB  1 
ATOM   5065  C  CG  . LEU A  1 675 ? 36.795  -25.671 -13.292 1.00 46.33  ? 675  LEU A CG  1 
ATOM   5066  C  CD1 . LEU A  1 675 ? 37.591  -24.438 -12.978 1.00 38.38  ? 675  LEU A CD1 1 
ATOM   5067  C  CD2 . LEU A  1 675 ? 37.525  -26.545 -14.285 1.00 51.47  ? 675  LEU A CD2 1 
ATOM   5068  N  N   . THR A  1 676 ? 36.653  -29.269 -10.673 1.00 39.89  ? 676  THR A N   1 
ATOM   5069  C  CA  . THR A  1 676 ? 36.659  -29.987 -9.414  1.00 42.90  ? 676  THR A CA  1 
ATOM   5070  C  C   . THR A  1 676 ? 37.428  -29.174 -8.385  1.00 37.24  ? 676  THR A C   1 
ATOM   5071  O  O   . THR A  1 676 ? 38.267  -28.334 -8.729  1.00 42.16  ? 676  THR A O   1 
ATOM   5072  C  CB  . THR A  1 676 ? 37.265  -31.401 -9.569  1.00 41.41  ? 676  THR A CB  1 
ATOM   5073  O  OG1 . THR A  1 676 ? 38.459  -31.325 -10.357 1.00 39.20  ? 676  THR A OG1 1 
ATOM   5074  C  CG2 . THR A  1 676 ? 36.283  -32.294 -10.271 1.00 33.11  ? 676  THR A CG2 1 
ATOM   5075  N  N   . LEU A  1 677 ? 37.132  -29.422 -7.122  1.00 34.29  ? 677  LEU A N   1 
ATOM   5076  C  CA  . LEU A  1 677 ? 37.637  -28.594 -6.043  1.00 32.94  ? 677  LEU A CA  1 
ATOM   5077  C  C   . LEU A  1 677 ? 39.161  -28.565 -5.983  1.00 39.03  ? 677  LEU A C   1 
ATOM   5078  O  O   . LEU A  1 677 ? 39.745  -27.567 -5.567  1.00 42.71  ? 677  LEU A O   1 
ATOM   5079  C  CB  . LEU A  1 677 ? 37.062  -29.063 -4.711  1.00 33.49  ? 677  LEU A CB  1 
ATOM   5080  C  CG  . LEU A  1 677 ? 37.427  -28.190 -3.521  1.00 33.40  ? 677  LEU A CG  1 
ATOM   5081  C  CD1 . LEU A  1 677 ? 36.924  -26.778 -3.795  1.00 34.02  ? 677  LEU A CD1 1 
ATOM   5082  C  CD2 . LEU A  1 677 ? 36.849  -28.746 -2.234  1.00 33.08  ? 677  LEU A CD2 1 
ATOM   5083  N  N   . ASP A  1 678 ? 39.807  -29.637 -6.417  1.00 33.80  ? 678  ASP A N   1 
ATOM   5084  C  CA  . ASP A  1 678 ? 41.265  -29.691 -6.419  1.00 34.19  ? 678  ASP A CA  1 
ATOM   5085  C  C   . ASP A  1 678 ? 41.914  -28.724 -7.422  1.00 41.15  ? 678  ASP A C   1 
ATOM   5086  O  O   . ASP A  1 678 ? 43.083  -28.372 -7.291  1.00 41.42  ? 678  ASP A O   1 
ATOM   5087  C  CB  . ASP A  1 678 ? 41.714  -31.106 -6.725  1.00 39.65  ? 678  ASP A CB  1 
ATOM   5088  C  CG  . ASP A  1 678 ? 41.138  -31.613 -8.024  1.00 46.35  ? 678  ASP A CG  1 
ATOM   5089  O  OD1 . ASP A  1 678 ? 39.891  -31.698 -8.124  1.00 43.27  ? 678  ASP A OD1 1 
ATOM   5090  O  OD2 . ASP A  1 678 ? 41.931  -31.902 -8.949  1.00 47.60  ? 678  ASP A OD2 1 
ATOM   5091  N  N   . LYS A  1 679 ? 41.184  -28.294 -8.437  1.00 37.66  ? 679  LYS A N   1 
ATOM   5092  C  CA  . LYS A  1 679 ? 41.768  -27.290 -9.317  1.00 48.57  ? 679  LYS A CA  1 
ATOM   5093  C  C   . LYS A  1 679 ? 41.875  -25.948 -8.581  1.00 44.49  ? 679  LYS A C   1 
ATOM   5094  O  O   . LYS A  1 679 ? 42.919  -25.301 -8.592  1.00 44.80  ? 679  LYS A O   1 
ATOM   5095  C  CB  . LYS A  1 679 ? 40.951  -27.144 -10.599 1.00 49.78  ? 679  LYS A CB  1 
ATOM   5096  C  CG  . LYS A  1 679 ? 40.816  -28.446 -11.392 1.00 62.91  ? 679  LYS A CG  1 
ATOM   5097  C  CD  . LYS A  1 679 ? 42.108  -28.839 -12.115 1.00 65.72  ? 679  LYS A CD  1 
ATOM   5098  C  CE  . LYS A  1 679 ? 41.874  -30.013 -13.092 1.00 78.98  ? 679  LYS A CE  1 
ATOM   5099  N  NZ  . LYS A  1 679 ? 41.561  -31.354 -12.469 1.00 66.45  ? 679  LYS A NZ  1 
ATOM   5100  N  N   . ALA A  1 680 ? 40.793  -25.553 -7.923  1.00 40.82  ? 680  ALA A N   1 
ATOM   5101  C  CA  . ALA A  1 680 ? 40.759  -24.307 -7.177  1.00 40.01  ? 680  ALA A CA  1 
ATOM   5102  C  C   . ALA A  1 680 ? 41.758  -24.305 -6.011  1.00 45.08  ? 680  ALA A C   1 
ATOM   5103  O  O   . ALA A  1 680 ? 42.522  -23.349 -5.845  1.00 45.99  ? 680  ALA A O   1 
ATOM   5104  C  CB  . ALA A  1 680 ? 39.348  -24.036 -6.674  1.00 36.22  ? 680  ALA A CB  1 
ATOM   5105  N  N   . LEU A  1 681 ? 41.755  -25.364 -5.203  1.00 40.92  ? 681  LEU A N   1 
ATOM   5106  C  CA  . LEU A  1 681 ? 42.725  -25.479 -4.123  1.00 41.83  ? 681  LEU A CA  1 
ATOM   5107  C  C   . LEU A  1 681 ? 44.160  -25.417 -4.664  1.00 44.85  ? 681  LEU A C   1 
ATOM   5108  O  O   . LEU A  1 681 ? 45.034  -24.806 -4.052  1.00 46.37  ? 681  LEU A O   1 
ATOM   5109  C  CB  . LEU A  1 681 ? 42.507  -26.770 -3.332  1.00 40.41  ? 681  LEU A CB  1 
ATOM   5110  C  CG  . LEU A  1 681 ? 41.123  -26.904 -2.705  1.00 37.10  ? 681  LEU A CG  1 
ATOM   5111  C  CD1 . LEU A  1 681 ? 41.101  -28.078 -1.775  1.00 34.08  ? 681  LEU A CD1 1 
ATOM   5112  C  CD2 . LEU A  1 681 ? 40.747  -25.653 -1.967  1.00 34.19  ? 681  LEU A CD2 1 
ATOM   5113  N  N   . ASP A  1 682 ? 44.390  -26.030 -5.819  1.00 42.85  ? 682  ASP A N   1 
ATOM   5114  C  CA  . ASP A  1 682 ? 45.691  -25.973 -6.472  1.00 46.63  ? 682  ASP A CA  1 
ATOM   5115  C  C   . ASP A  1 682 ? 46.140  -24.546 -6.749  1.00 47.75  ? 682  ASP A C   1 
ATOM   5116  O  O   . ASP A  1 682 ? 47.301  -24.203 -6.566  1.00 51.64  ? 682  ASP A O   1 
ATOM   5117  C  CB  . ASP A  1 682 ? 45.657  -26.762 -7.775  1.00 50.34  ? 682  ASP A CB  1 
ATOM   5118  C  CG  . ASP A  1 682 ? 46.192  -28.170 -7.620  1.00 46.17  ? 682  ASP A CG  1 
ATOM   5119  O  OD1 . ASP A  1 682 ? 46.521  -28.565 -6.476  1.00 44.65  ? 682  ASP A OD1 1 
ATOM   5120  O  OD2 . ASP A  1 682 ? 46.262  -28.881 -8.648  1.00 49.15  ? 682  ASP A OD2 1 
ATOM   5121  N  N   . MET A  1 683 ? 45.216  -23.709 -7.185  1.00 49.09  ? 683  MET A N   1 
ATOM   5122  C  CA  . MET A  1 683 ? 45.536  -22.304 -7.387  1.00 50.25  ? 683  MET A CA  1 
ATOM   5123  C  C   . MET A  1 683 ? 46.010  -21.589 -6.114  1.00 48.43  ? 683  MET A C   1 
ATOM   5124  O  O   . MET A  1 683 ? 46.967  -20.813 -6.168  1.00 56.01  ? 683  MET A O   1 
ATOM   5125  C  CB  . MET A  1 683 ? 44.329  -21.577 -7.961  1.00 45.69  ? 683  MET A CB  1 
ATOM   5126  C  CG  . MET A  1 683 ? 44.552  -20.102 -8.116  1.00 44.78  ? 683  MET A CG  1 
ATOM   5127  S  SD  . MET A  1 683 ? 43.163  -19.390 -8.999  1.00 53.24  ? 683  MET A SD  1 
ATOM   5128  C  CE  . MET A  1 683 ? 43.509  -19.854 -10.690 1.00 43.76  ? 683  MET A CE  1 
ATOM   5129  N  N   . THR A  1 684 ? 45.374  -21.858 -4.970  1.00 42.51  ? 684  THR A N   1 
ATOM   5130  C  CA  . THR A  1 684 ? 45.719  -21.145 -3.728  1.00 42.42  ? 684  THR A CA  1 
ATOM   5131  C  C   . THR A  1 684 ? 47.157  -21.354 -3.283  1.00 47.39  ? 684  THR A C   1 
ATOM   5132  O  O   . THR A  1 684 ? 47.608  -20.747 -2.299  1.00 43.18  ? 684  THR A O   1 
ATOM   5133  C  CB  . THR A  1 684 ? 44.829  -21.562 -2.542  1.00 43.48  ? 684  THR A CB  1 
ATOM   5134  O  OG1 . THR A  1 684 ? 45.118  -22.917 -2.170  1.00 43.84  ? 684  THR A OG1 1 
ATOM   5135  C  CG2 . THR A  1 684 ? 43.353  -21.409 -2.881  1.00 45.83  ? 684  THR A CG2 1 
ATOM   5136  N  N   . TYR A  1 685 ? 47.858  -22.238 -3.990  1.00 44.20  ? 685  TYR A N   1 
ATOM   5137  C  CA  . TYR A  1 685 ? 49.261  -22.512 -3.724  1.00 49.37  ? 685  TYR A CA  1 
ATOM   5138  C  C   . TYR A  1 685 ? 50.087  -21.275 -4.017  1.00 45.18  ? 685  TYR A C   1 
ATOM   5139  O  O   . TYR A  1 685 ? 51.042  -20.984 -3.302  1.00 45.41  ? 685  TYR A O   1 
ATOM   5140  C  CB  . TYR A  1 685 ? 49.775  -23.703 -4.567  1.00 48.67  ? 685  TYR A CB  1 
ATOM   5141  C  CG  . TYR A  1 685 ? 49.605  -25.061 -3.927  1.00 44.57  ? 685  TYR A CG  1 
ATOM   5142  C  CD1 . TYR A  1 685 ? 49.770  -25.227 -2.549  1.00 45.66  ? 685  TYR A CD1 1 
ATOM   5143  C  CD2 . TYR A  1 685 ? 49.271  -26.180 -4.696  1.00 47.50  ? 685  TYR A CD2 1 
ATOM   5144  C  CE1 . TYR A  1 685 ? 49.608  -26.472 -1.949  1.00 46.29  ? 685  TYR A CE1 1 
ATOM   5145  C  CE2 . TYR A  1 685 ? 49.115  -27.448 -4.115  1.00 42.48  ? 685  TYR A CE2 1 
ATOM   5146  C  CZ  . TYR A  1 685 ? 49.284  -27.589 -2.736  1.00 54.30  ? 685  TYR A CZ  1 
ATOM   5147  O  OH  . TYR A  1 685 ? 49.133  -28.835 -2.128  1.00 51.01  ? 685  TYR A OH  1 
ATOM   5148  N  N   . TYR A  1 686 ? 49.730  -20.546 -5.069  1.00 43.26  ? 686  TYR A N   1 
ATOM   5149  C  CA  . TYR A  1 686 ? 50.555  -19.402 -5.444  1.00 48.66  ? 686  TYR A CA  1 
ATOM   5150  C  C   . TYR A  1 686 ? 50.463  -18.297 -4.397  1.00 50.11  ? 686  TYR A C   1 
ATOM   5151  O  O   . TYR A  1 686 ? 51.401  -17.516 -4.227  1.00 49.41  ? 686  TYR A O   1 
ATOM   5152  C  CB  . TYR A  1 686 ? 50.169  -18.866 -6.834  1.00 50.20  ? 686  TYR A CB  1 
ATOM   5153  C  CG  . TYR A  1 686 ? 49.231  -17.678 -6.823  1.00 51.09  ? 686  TYR A CG  1 
ATOM   5154  C  CD1 . TYR A  1 686 ? 49.714  -16.381 -6.662  1.00 50.83  ? 686  TYR A CD1 1 
ATOM   5155  C  CD2 . TYR A  1 686 ? 47.867  -17.850 -6.990  1.00 48.56  ? 686  TYR A CD2 1 
ATOM   5156  C  CE1 . TYR A  1 686 ? 48.862  -15.298 -6.643  1.00 50.08  ? 686  TYR A CE1 1 
ATOM   5157  C  CE2 . TYR A  1 686 ? 47.013  -16.772 -6.982  1.00 50.44  ? 686  TYR A CE2 1 
ATOM   5158  C  CZ  . TYR A  1 686 ? 47.515  -15.498 -6.811  1.00 47.07  ? 686  TYR A CZ  1 
ATOM   5159  O  OH  . TYR A  1 686 ? 46.670  -14.425 -6.802  1.00 43.75  ? 686  TYR A OH  1 
ATOM   5160  N  N   . LEU A  1 687 ? 49.350  -18.253 -3.667  1.00 47.99  ? 687  LEU A N   1 
ATOM   5161  C  CA  . LEU A  1 687 ? 49.082  -17.154 -2.742  1.00 44.96  ? 687  LEU A CA  1 
ATOM   5162  C  C   . LEU A  1 687 ? 50.175  -16.959 -1.702  1.00 49.94  ? 687  LEU A C   1 
ATOM   5163  O  O   . LEU A  1 687 ? 50.148  -15.997 -0.935  1.00 49.84  ? 687  LEU A O   1 
ATOM   5164  C  CB  . LEU A  1 687 ? 47.755  -17.369 -2.030  1.00 43.10  ? 687  LEU A CB  1 
ATOM   5165  C  CG  . LEU A  1 687 ? 46.501  -17.240 -2.883  1.00 41.78  ? 687  LEU A CG  1 
ATOM   5166  C  CD1 . LEU A  1 687 ? 45.288  -17.542 -2.036  1.00 38.22  ? 687  LEU A CD1 1 
ATOM   5167  C  CD2 . LEU A  1 687 ? 46.404  -15.849 -3.481  1.00 40.50  ? 687  LEU A CD2 1 
ATOM   5168  N  N   . GLN A  1 688 ? 51.135  -17.875 -1.670  1.00 49.83  ? 688  GLN A N   1 
ATOM   5169  C  CA  . GLN A  1 688 ? 52.232  -17.784 -0.730  1.00 49.84  ? 688  GLN A CA  1 
ATOM   5170  C  C   . GLN A  1 688 ? 53.176  -16.669 -1.176  1.00 49.72  ? 688  GLN A C   1 
ATOM   5171  O  O   . GLN A  1 688 ? 53.816  -16.019 -0.363  1.00 48.41  ? 688  GLN A O   1 
ATOM   5172  C  CB  . GLN A  1 688 ? 52.940  -19.135 -0.616  1.00 50.76  ? 688  GLN A CB  1 
ATOM   5173  C  CG  . GLN A  1 688 ? 54.420  -19.128 -0.907  1.00 58.96  ? 688  GLN A CG  1 
ATOM   5174  C  CD  . GLN A  1 688 ? 54.902  -20.472 -1.424  1.00 65.27  ? 688  GLN A CD  1 
ATOM   5175  O  OE1 . GLN A  1 688 ? 54.944  -20.700 -2.634  1.00 70.07  ? 688  GLN A OE1 1 
ATOM   5176  N  NE2 . GLN A  1 688 ? 55.264  -21.369 -0.511  1.00 59.08  ? 688  GLN A NE2 1 
ATOM   5177  N  N   . HIS A  1 689 ? 53.222  -16.425 -2.474  1.00 51.81  ? 689  HIS A N   1 
ATOM   5178  C  CA  . HIS A  1 689 ? 54.042  -15.354 -3.004  1.00 51.65  ? 689  HIS A CA  1 
ATOM   5179  C  C   . HIS A  1 689 ? 53.254  -14.051 -3.194  1.00 51.85  ? 689  HIS A C   1 
ATOM   5180  O  O   . HIS A  1 689 ? 53.852  -12.992 -3.344  1.00 54.29  ? 689  HIS A O   1 
ATOM   5181  C  CB  . HIS A  1 689 ? 54.659  -15.786 -4.333  1.00 55.07  ? 689  HIS A CB  1 
ATOM   5182  C  CG  . HIS A  1 689 ? 55.300  -17.139 -4.288  1.00 63.12  ? 689  HIS A CG  1 
ATOM   5183  N  ND1 . HIS A  1 689 ? 56.441  -17.398 -3.560  1.00 68.63  ? 689  HIS A ND1 1 
ATOM   5184  C  CD2 . HIS A  1 689 ? 54.959  -18.308 -4.882  1.00 65.26  ? 689  HIS A CD2 1 
ATOM   5185  C  CE1 . HIS A  1 689 ? 56.776  -18.667 -3.707  1.00 69.73  ? 689  HIS A CE1 1 
ATOM   5186  N  NE2 . HIS A  1 689 ? 55.891  -19.243 -4.502  1.00 72.63  ? 689  HIS A NE2 1 
ATOM   5187  N  N   . GLU A  1 690 ? 51.925  -14.127 -3.176  1.00 44.79  ? 690  GLU A N   1 
ATOM   5188  C  CA  . GLU A  1 690 ? 51.068  -12.975 -3.473  1.00 45.09  ? 690  GLU A CA  1 
ATOM   5189  C  C   . GLU A  1 690 ? 51.119  -11.834 -2.440  1.00 52.08  ? 690  GLU A C   1 
ATOM   5190  O  O   . GLU A  1 690 ? 50.808  -12.032 -1.259  1.00 48.60  ? 690  GLU A O   1 
ATOM   5191  C  CB  . GLU A  1 690 ? 49.623  -13.434 -3.618  1.00 46.55  ? 690  GLU A CB  1 
ATOM   5192  C  CG  . GLU A  1 690 ? 48.628  -12.319 -3.843  1.00 40.35  ? 690  GLU A CG  1 
ATOM   5193  C  CD  . GLU A  1 690 ? 48.852  -11.598 -5.147  1.00 43.76  ? 690  GLU A CD  1 
ATOM   5194  O  OE1 . GLU A  1 690 ? 49.747  -10.716 -5.201  1.00 46.96  ? 690  GLU A OE1 1 
ATOM   5195  O  OE2 . GLU A  1 690 ? 48.127  -11.906 -6.118  1.00 43.62  ? 690  GLU A OE2 1 
ATOM   5196  N  N   . THR A  1 691 ? 51.488  -10.638 -2.903  1.00 46.14  ? 691  THR A N   1 
ATOM   5197  C  CA  . THR A  1 691 ? 51.564  -9.463  -2.034  1.00 52.50  ? 691  THR A CA  1 
ATOM   5198  C  C   . THR A  1 691 ? 50.472  -8.424  -2.333  1.00 45.58  ? 691  THR A C   1 
ATOM   5199  O  O   . THR A  1 691 ? 50.280  -7.487  -1.574  1.00 45.87  ? 691  THR A O   1 
ATOM   5200  C  CB  . THR A  1 691 ? 52.931  -8.782  -2.134  1.00 49.02  ? 691  THR A CB  1 
ATOM   5201  O  OG1 . THR A  1 691 ? 53.329  -8.715  -3.511  1.00 54.61  ? 691  THR A OG1 1 
ATOM   5202  C  CG2 . THR A  1 691 ? 53.955  -9.568  -1.338  1.00 42.96  ? 691  THR A CG2 1 
ATOM   5203  N  N   . SER A  1 692 ? 49.755  -8.606  -3.427  1.00 39.28  ? 692  SER A N   1 
ATOM   5204  C  CA  . SER A  1 692 ? 48.569  -7.826  -3.678  1.00 36.20  ? 692  SER A CA  1 
ATOM   5205  C  C   . SER A  1 692 ? 47.450  -8.251  -2.757  1.00 46.56  ? 692  SER A C   1 
ATOM   5206  O  O   . SER A  1 692 ? 46.833  -9.301  -2.977  1.00 44.38  ? 692  SER A O   1 
ATOM   5207  C  CB  . SER A  1 692 ? 48.107  -7.982  -5.110  1.00 38.48  ? 692  SER A CB  1 
ATOM   5208  O  OG  . SER A  1 692 ? 46.850  -7.350  -5.278  1.00 40.07  ? 692  SER A OG  1 
ATOM   5209  N  N   . SER A  1 693 ? 47.166  -7.421  -1.751  1.00 47.97  ? 693  SER A N   1 
ATOM   5210  C  CA  . SER A  1 693 ? 46.250  -7.792  -0.676  1.00 40.66  ? 693  SER A CA  1 
ATOM   5211  C  C   . SER A  1 693 ? 44.875  -8.283  -1.128  1.00 42.05  ? 693  SER A C   1 
ATOM   5212  O  O   . SER A  1 693 ? 44.372  -9.233  -0.555  1.00 47.74  ? 693  SER A O   1 
ATOM   5213  C  CB  . SER A  1 693 ? 46.071  -6.626  0.282   1.00 43.32  ? 693  SER A CB  1 
ATOM   5214  O  OG  . SER A  1 693 ? 47.292  -6.314  0.911   1.00 50.87  ? 693  SER A OG  1 
ATOM   5215  N  N   . PRO A  1 694 ? 44.263  -7.656  -2.149  1.00 40.98  ? 694  PRO A N   1 
ATOM   5216  C  CA  . PRO A  1 694 ? 42.923  -8.145  -2.488  1.00 41.91  ? 694  PRO A CA  1 
ATOM   5217  C  C   . PRO A  1 694 ? 42.864  -9.598  -2.943  1.00 45.84  ? 694  PRO A C   1 
ATOM   5218  O  O   . PRO A  1 694 ? 41.927  -10.309 -2.566  1.00 45.35  ? 694  PRO A O   1 
ATOM   5219  C  CB  . PRO A  1 694 ? 42.498  -7.219  -3.624  1.00 35.94  ? 694  PRO A CB  1 
ATOM   5220  C  CG  . PRO A  1 694 ? 43.205  -5.968  -3.350  1.00 38.49  ? 694  PRO A CG  1 
ATOM   5221  C  CD  . PRO A  1 694 ? 44.549  -6.385  -2.834  1.00 42.22  ? 694  PRO A CD  1 
ATOM   5222  N  N   . ALA A  1 695 ? 43.825  -10.034 -3.750  1.00 47.69  ? 695  ALA A N   1 
ATOM   5223  C  CA  . ALA A  1 695 ? 43.807  -11.412 -4.214  1.00 45.74  ? 695  ALA A CA  1 
ATOM   5224  C  C   . ALA A  1 695 ? 44.179  -12.333 -3.057  1.00 41.58  ? 695  ALA A C   1 
ATOM   5225  O  O   . ALA A  1 695 ? 43.547  -13.378 -2.886  1.00 36.12  ? 695  ALA A O   1 
ATOM   5226  C  CB  . ALA A  1 695 ? 44.732  -11.609 -5.405  1.00 35.93  ? 695  ALA A CB  1 
ATOM   5227  N  N   . LEU A  1 696 ? 45.167  -11.931 -2.255  1.00 36.98  ? 696  LEU A N   1 
ATOM   5228  C  CA  . LEU A  1 696 ? 45.553  -12.716 -1.076  1.00 39.17  ? 696  LEU A CA  1 
ATOM   5229  C  C   . LEU A  1 696 ? 44.352  -12.987 -0.187  1.00 40.43  ? 696  LEU A C   1 
ATOM   5230  O  O   . LEU A  1 696 ? 44.167  -14.105 0.306   1.00 38.12  ? 696  LEU A O   1 
ATOM   5231  C  CB  . LEU A  1 696 ? 46.636  -12.016 -0.241  1.00 40.23  ? 696  LEU A CB  1 
ATOM   5232  C  CG  . LEU A  1 696 ? 47.009  -12.833 1.009   1.00 41.97  ? 696  LEU A CG  1 
ATOM   5233  C  CD1 . LEU A  1 696 ? 47.544  -14.196 0.602   1.00 39.09  ? 696  LEU A CD1 1 
ATOM   5234  C  CD2 . LEU A  1 696 ? 48.011  -12.136 1.923   1.00 40.11  ? 696  LEU A CD2 1 
ATOM   5235  N  N   . LEU A  1 697 ? 43.532  -11.952 0.009   1.00 43.85  ? 697  LEU A N   1 
ATOM   5236  C  CA  . LEU A  1 697 ? 42.391  -12.037 0.916   1.00 40.14  ? 697  LEU A CA  1 
ATOM   5237  C  C   . LEU A  1 697 ? 41.192  -12.747 0.282   1.00 38.25  ? 697  LEU A C   1 
ATOM   5238  O  O   . LEU A  1 697 ? 40.432  -13.443 0.974   1.00 36.68  ? 697  LEU A O   1 
ATOM   5239  C  CB  . LEU A  1 697 ? 41.990  -10.652 1.382   1.00 37.13  ? 697  LEU A CB  1 
ATOM   5240  C  CG  . LEU A  1 697 ? 42.939  -9.927  2.318   1.00 37.80  ? 697  LEU A CG  1 
ATOM   5241  C  CD1 . LEU A  1 697 ? 42.343  -8.562  2.629   1.00 40.77  ? 697  LEU A CD1 1 
ATOM   5242  C  CD2 . LEU A  1 697 ? 43.163  -10.719 3.589   1.00 34.47  ? 697  LEU A CD2 1 
ATOM   5243  N  N   . GLU A  1 698 ? 41.016  -12.568 -1.020  1.00 29.65  ? 698  GLU A N   1 
ATOM   5244  C  CA  . GLU A  1 698 ? 40.052  -13.383 -1.742  1.00 39.68  ? 698  GLU A CA  1 
ATOM   5245  C  C   . GLU A  1 698 ? 40.344  -14.885 -1.507  1.00 43.47  ? 698  GLU A C   1 
ATOM   5246  O  O   . GLU A  1 698 ? 39.484  -15.610 -0.997  1.00 40.99  ? 698  GLU A O   1 
ATOM   5247  C  CB  . GLU A  1 698 ? 40.075  -13.039 -3.233  1.00 37.25  ? 698  GLU A CB  1 
ATOM   5248  C  CG  . GLU A  1 698 ? 38.975  -13.659 -4.077  1.00 37.58  ? 698  GLU A CG  1 
ATOM   5249  C  CD  . GLU A  1 698 ? 37.563  -13.217 -3.689  1.00 49.40  ? 698  GLU A CD  1 
ATOM   5250  O  OE1 . GLU A  1 698 ? 37.406  -12.271 -2.867  1.00 52.24  ? 698  GLU A OE1 1 
ATOM   5251  O  OE2 . GLU A  1 698 ? 36.593  -13.818 -4.221  1.00 48.81  ? 698  GLU A OE2 1 
ATOM   5252  N  N   . GLY A  1 699 ? 41.564  -15.324 -1.831  1.00 39.16  ? 699  GLY A N   1 
ATOM   5253  C  CA  . GLY A  1 699 ? 41.979  -16.707 -1.668  1.00 35.02  ? 699  GLY A CA  1 
ATOM   5254  C  C   . GLY A  1 699 ? 41.808  -17.224 -0.251  1.00 39.00  ? 699  GLY A C   1 
ATOM   5255  O  O   . GLY A  1 699 ? 41.235  -18.284 -0.045  1.00 36.41  ? 699  GLY A O   1 
ATOM   5256  N  N   . LEU A  1 700 ? 42.289  -16.462 0.723   1.00 36.33  ? 700  LEU A N   1 
ATOM   5257  C  CA  . LEU A  1 700 ? 42.181  -16.850 2.121   1.00 36.38  ? 700  LEU A CA  1 
ATOM   5258  C  C   . LEU A  1 700 ? 40.741  -17.056 2.519   1.00 34.90  ? 700  LEU A C   1 
ATOM   5259  O  O   . LEU A  1 700 ? 40.417  -18.011 3.205   1.00 37.89  ? 700  LEU A O   1 
ATOM   5260  C  CB  . LEU A  1 700 ? 42.815  -15.799 3.039   1.00 33.96  ? 700  LEU A CB  1 
ATOM   5261  C  CG  . LEU A  1 700 ? 44.338  -15.892 3.115   1.00 43.09  ? 700  LEU A CG  1 
ATOM   5262  C  CD1 . LEU A  1 700 ? 44.912  -14.740 3.906   1.00 39.17  ? 700  LEU A CD1 1 
ATOM   5263  C  CD2 . LEU A  1 700 ? 44.739  -17.209 3.732   1.00 40.07  ? 700  LEU A CD2 1 
ATOM   5264  N  N   . SER A  1 701 ? 39.876  -16.168 2.061   1.00 34.80  ? 701  SER A N   1 
ATOM   5265  C  CA  . SER A  1 701 ? 38.500  -16.160 2.518   1.00 33.39  ? 701  SER A CA  1 
ATOM   5266  C  C   . SER A  1 701 ? 37.789  -17.449 2.121   1.00 35.84  ? 701  SER A C   1 
ATOM   5267  O  O   . SER A  1 701 ? 36.940  -17.929 2.860   1.00 36.33  ? 701  SER A O   1 
ATOM   5268  C  CB  . SER A  1 701 ? 37.752  -14.921 1.985   1.00 31.86  ? 701  SER A CB  1 
ATOM   5269  O  OG  . SER A  1 701 ? 37.715  -14.893 0.572   1.00 37.97  ? 701  SER A OG  1 
ATOM   5270  N  N   . TYR A  1 702 ? 38.162  -18.025 0.978   1.00 38.83  ? 702  TYR A N   1 
ATOM   5271  C  CA  . TYR A  1 702 ? 37.631  -19.327 0.595   1.00 35.37  ? 702  TYR A CA  1 
ATOM   5272  C  C   . TYR A  1 702 ? 38.131  -20.425 1.543   1.00 39.32  ? 702  TYR A C   1 
ATOM   5273  O  O   . TYR A  1 702 ? 37.330  -21.264 2.008   1.00 38.06  ? 702  TYR A O   1 
ATOM   5274  C  CB  . TYR A  1 702 ? 37.970  -19.638 -0.864  1.00 33.21  ? 702  TYR A CB  1 
ATOM   5275  C  CG  . TYR A  1 702 ? 37.090  -18.855 -1.819  1.00 38.89  ? 702  TYR A CG  1 
ATOM   5276  C  CD1 . TYR A  1 702 ? 35.713  -19.062 -1.854  1.00 46.29  ? 702  TYR A CD1 1 
ATOM   5277  C  CD2 . TYR A  1 702 ? 37.624  -17.896 -2.667  1.00 40.13  ? 702  TYR A CD2 1 
ATOM   5278  C  CE1 . TYR A  1 702 ? 34.893  -18.331 -2.706  1.00 45.83  ? 702  TYR A CE1 1 
ATOM   5279  C  CE2 . TYR A  1 702 ? 36.817  -17.167 -3.530  1.00 35.42  ? 702  TYR A CE2 1 
ATOM   5280  C  CZ  . TYR A  1 702 ? 35.459  -17.380 -3.537  1.00 42.92  ? 702  TYR A CZ  1 
ATOM   5281  O  OH  . TYR A  1 702 ? 34.665  -16.653 -4.388  1.00 45.70  ? 702  TYR A OH  1 
ATOM   5282  N  N   . LEU A  1 703 ? 39.426  -20.411 1.867   1.00 36.34  ? 703  LEU A N   1 
ATOM   5283  C  CA  . LEU A  1 703 ? 39.952  -21.397 2.812   1.00 32.41  ? 703  LEU A CA  1 
ATOM   5284  C  C   . LEU A  1 703 ? 39.295  -21.226 4.176   1.00 37.31  ? 703  LEU A C   1 
ATOM   5285  O  O   . LEU A  1 703 ? 38.937  -22.209 4.849   1.00 39.47  ? 703  LEU A O   1 
ATOM   5286  C  CB  . LEU A  1 703 ? 41.467  -21.291 2.927   1.00 32.59  ? 703  LEU A CB  1 
ATOM   5287  C  CG  . LEU A  1 703 ? 42.209  -21.592 1.619   1.00 38.00  ? 703  LEU A CG  1 
ATOM   5288  C  CD1 . LEU A  1 703 ? 43.705  -21.556 1.845   1.00 43.67  ? 703  LEU A CD1 1 
ATOM   5289  C  CD2 . LEU A  1 703 ? 41.804  -22.926 1.048   1.00 30.37  ? 703  LEU A CD2 1 
ATOM   5290  N  N   . GLU A  1 704 ? 39.107  -19.974 4.580   1.00 35.91  ? 704  GLU A N   1 
ATOM   5291  C  CA  . GLU A  1 704 ? 38.511  -19.710 5.868   1.00 38.26  ? 704  GLU A CA  1 
ATOM   5292  C  C   . GLU A  1 704 ? 37.062  -20.154 5.864   1.00 36.79  ? 704  GLU A C   1 
ATOM   5293  O  O   . GLU A  1 704 ? 36.528  -20.628 6.867   1.00 33.40  ? 704  GLU A O   1 
ATOM   5294  C  CB  . GLU A  1 704 ? 38.601  -18.233 6.211   1.00 42.05  ? 704  GLU A CB  1 
ATOM   5295  C  CG  . GLU A  1 704 ? 38.167  -17.932 7.617   1.00 38.69  ? 704  GLU A CG  1 
ATOM   5296  C  CD  . GLU A  1 704 ? 38.170  -16.448 7.899   1.00 61.59  ? 704  GLU A CD  1 
ATOM   5297  O  OE1 . GLU A  1 704 ? 38.405  -15.663 6.936   1.00 56.75  ? 704  GLU A OE1 1 
ATOM   5298  O  OE2 . GLU A  1 704 ? 37.936  -16.074 9.081   1.00 65.24  ? 704  GLU A OE2 1 
ATOM   5299  N  N   . SER A  1 705 ? 36.432  -20.006 4.715   1.00 30.66  ? 705  SER A N   1 
ATOM   5300  C  CA  . SER A  1 705 ? 35.024  -20.283 4.634   1.00 33.90  ? 705  SER A CA  1 
ATOM   5301  C  C   . SER A  1 705 ? 34.770  -21.769 4.787   1.00 36.14  ? 705  SER A C   1 
ATOM   5302  O  O   . SER A  1 705 ? 33.811  -22.173 5.445   1.00 35.57  ? 705  SER A O   1 
ATOM   5303  C  CB  . SER A  1 705 ? 34.456  -19.785 3.326   1.00 30.80  ? 705  SER A CB  1 
ATOM   5304  O  OG  . SER A  1 705 ? 33.063  -19.621 3.447   1.00 49.79  ? 705  SER A OG  1 
ATOM   5305  N  N   . PHE A  1 706 ? 35.642  -22.571 4.181   1.00 36.86  ? 706  PHE A N   1 
ATOM   5306  C  CA  . PHE A  1 706 ? 35.560  -24.023 4.304   1.00 34.91  ? 706  PHE A CA  1 
ATOM   5307  C  C   . PHE A  1 706 ? 35.766  -24.450 5.739   1.00 36.23  ? 706  PHE A C   1 
ATOM   5308  O  O   . PHE A  1 706 ? 35.074  -25.346 6.213   1.00 37.79  ? 706  PHE A O   1 
ATOM   5309  C  CB  . PHE A  1 706 ? 36.584  -24.721 3.411   1.00 29.17  ? 706  PHE A CB  1 
ATOM   5310  C  CG  . PHE A  1 706 ? 36.421  -24.407 1.958   1.00 31.97  ? 706  PHE A CG  1 
ATOM   5311  C  CD1 . PHE A  1 706 ? 35.195  -23.973 1.461   1.00 33.08  ? 706  PHE A CD1 1 
ATOM   5312  C  CD2 . PHE A  1 706 ? 37.499  -24.502 1.094   1.00 30.86  ? 706  PHE A CD2 1 
ATOM   5313  C  CE1 . PHE A  1 706 ? 35.037  -23.657 0.133   1.00 31.16  ? 706  PHE A CE1 1 
ATOM   5314  C  CE2 . PHE A  1 706 ? 37.349  -24.188 -0.231  1.00 33.15  ? 706  PHE A CE2 1 
ATOM   5315  C  CZ  . PHE A  1 706 ? 36.114  -23.770 -0.713  1.00 37.74  ? 706  PHE A CZ  1 
ATOM   5316  N  N   . TYR A  1 707 ? 36.709  -23.813 6.430   1.00 33.43  ? 707  TYR A N   1 
ATOM   5317  C  CA  . TYR A  1 707 ? 36.984  -24.193 7.813   1.00 36.29  ? 707  TYR A CA  1 
ATOM   5318  C  C   . TYR A  1 707 ? 35.730  -24.009 8.675   1.00 38.08  ? 707  TYR A C   1 
ATOM   5319  O  O   . TYR A  1 707 ? 35.384  -24.876 9.474   1.00 36.39  ? 707  TYR A O   1 
ATOM   5320  C  CB  . TYR A  1 707 ? 38.162  -23.394 8.396   1.00 35.47  ? 707  TYR A CB  1 
ATOM   5321  C  CG  . TYR A  1 707 ? 38.278  -23.550 9.898   1.00 36.16  ? 707  TYR A CG  1 
ATOM   5322  C  CD1 . TYR A  1 707 ? 38.949  -24.636 10.450  1.00 34.59  ? 707  TYR A CD1 1 
ATOM   5323  C  CD2 . TYR A  1 707 ? 37.704  -22.618 10.769  1.00 35.43  ? 707  TYR A CD2 1 
ATOM   5324  C  CE1 . TYR A  1 707 ? 39.058  -24.785 11.821  1.00 38.01  ? 707  TYR A CE1 1 
ATOM   5325  C  CE2 . TYR A  1 707 ? 37.801  -22.766 12.140  1.00 32.03  ? 707  TYR A CE2 1 
ATOM   5326  C  CZ  . TYR A  1 707 ? 38.481  -23.856 12.657  1.00 35.53  ? 707  TYR A CZ  1 
ATOM   5327  O  OH  . TYR A  1 707 ? 38.582  -24.039 14.007  1.00 42.92  ? 707  TYR A OH  1 
ATOM   5328  N  N   . HIS A  1 708 ? 35.034  -22.893 8.495   1.00 36.23  ? 708  HIS A N   1 
ATOM   5329  C  CA  . HIS A  1 708 ? 33.858  -22.658 9.302   1.00 37.79  ? 708  HIS A CA  1 
ATOM   5330  C  C   . HIS A  1 708 ? 32.774  -23.630 8.886   1.00 34.68  ? 708  HIS A C   1 
ATOM   5331  O  O   . HIS A  1 708 ? 32.060  -24.174 9.726   1.00 36.83  ? 708  HIS A O   1 
ATOM   5332  C  CB  . HIS A  1 708 ? 33.398  -21.196 9.192   1.00 36.40  ? 708  HIS A CB  1 
ATOM   5333  C  CG  . HIS A  1 708 ? 34.376  -20.243 9.791   1.00 33.51  ? 708  HIS A CG  1 
ATOM   5334  N  ND1 . HIS A  1 708 ? 34.729  -20.288 11.121  1.00 38.47  ? 708  HIS A ND1 1 
ATOM   5335  C  CD2 . HIS A  1 708 ? 35.135  -19.273 9.235   1.00 35.83  ? 708  HIS A CD2 1 
ATOM   5336  C  CE1 . HIS A  1 708 ? 35.647  -19.372 11.361  1.00 34.37  ? 708  HIS A CE1 1 
ATOM   5337  N  NE2 . HIS A  1 708 ? 35.914  -18.746 10.231  1.00 32.43  ? 708  HIS A NE2 1 
ATOM   5338  N  N   . MET A  1 709 ? 32.670  -23.869 7.592   1.00 34.57  ? 709  MET A N   1 
ATOM   5339  C  CA  . MET A  1 709 ? 31.732  -24.861 7.104   1.00 38.21  ? 709  MET A CA  1 
ATOM   5340  C  C   . MET A  1 709 ? 31.961  -26.220 7.768   1.00 36.58  ? 709  MET A C   1 
ATOM   5341  O  O   . MET A  1 709 ? 31.027  -26.816 8.289   1.00 37.43  ? 709  MET A O   1 
ATOM   5342  C  CB  . MET A  1 709 ? 31.834  -24.995 5.601   1.00 40.67  ? 709  MET A CB  1 
ATOM   5343  C  CG  . MET A  1 709 ? 30.594  -25.603 5.007   1.00 50.63  ? 709  MET A CG  1 
ATOM   5344  S  SD  . MET A  1 709 ? 30.610  -25.549 3.218   1.00 65.49  ? 709  MET A SD  1 
ATOM   5345  C  CE  . MET A  1 709 ? 28.880  -25.947 2.920   1.00 48.81  ? 709  MET A CE  1 
ATOM   5346  N  N   . MET A  1 710 ? 33.204  -26.686 7.772   1.00 32.79  ? 710  MET A N   1 
ATOM   5347  C  CA  . MET A  1 710 ? 33.525  -27.946 8.428   1.00 36.08  ? 710  MET A CA  1 
ATOM   5348  C  C   . MET A  1 710 ? 33.227  -27.843 9.915   1.00 39.09  ? 710  MET A C   1 
ATOM   5349  O  O   . MET A  1 710 ? 32.625  -28.733 10.513  1.00 42.02  ? 710  MET A O   1 
ATOM   5350  C  CB  . MET A  1 710 ? 34.989  -28.336 8.217   1.00 31.05  ? 710  MET A CB  1 
ATOM   5351  C  CG  . MET A  1 710 ? 35.343  -28.589 6.772   1.00 34.88  ? 710  MET A CG  1 
ATOM   5352  S  SD  . MET A  1 710 ? 34.251  -29.795 6.026   1.00 43.43  ? 710  MET A SD  1 
ATOM   5353  C  CE  . MET A  1 710 ? 33.560  -28.868 4.669   1.00 38.14  ? 710  MET A CE  1 
ATOM   5354  N  N   . ASP A  1 711 ? 33.629  -26.732 10.502  1.00 37.37  ? 711  ASP A N   1 
ATOM   5355  C  CA  . ASP A  1 711 ? 33.566  -26.607 11.931  1.00 36.34  ? 711  ASP A CA  1 
ATOM   5356  C  C   . ASP A  1 711 ? 32.125  -26.530 12.399  1.00 37.75  ? 711  ASP A C   1 
ATOM   5357  O  O   . ASP A  1 711 ? 31.797  -26.971 13.495  1.00 42.04  ? 711  ASP A O   1 
ATOM   5358  C  CB  . ASP A  1 711 ? 34.372  -25.394 12.372  1.00 35.76  ? 711  ASP A CB  1 
ATOM   5359  C  CG  . ASP A  1 711 ? 34.632  -25.388 13.849  1.00 46.65  ? 711  ASP A CG  1 
ATOM   5360  O  OD1 . ASP A  1 711 ? 35.379  -26.261 14.334  1.00 47.52  ? 711  ASP A OD1 1 
ATOM   5361  O  OD2 . ASP A  1 711 ? 34.085  -24.501 14.527  1.00 57.91  ? 711  ASP A OD2 1 
ATOM   5362  N  N   . ARG A  1 712 ? 31.263  -25.991 11.555  1.00 38.83  ? 712  ARG A N   1 
ATOM   5363  C  CA  . ARG A  1 712 ? 29.839  -25.908 11.851  1.00 40.91  ? 712  ARG A CA  1 
ATOM   5364  C  C   . ARG A  1 712 ? 29.244  -27.288 12.046  1.00 38.99  ? 712  ARG A C   1 
ATOM   5365  O  O   . ARG A  1 712 ? 28.532  -27.524 13.005  1.00 49.74  ? 712  ARG A O   1 
ATOM   5366  C  CB  . ARG A  1 712 ? 29.105  -25.179 10.731  1.00 39.28  ? 712  ARG A CB  1 
ATOM   5367  C  CG  . ARG A  1 712 ? 28.444  -23.912 11.179  1.00 40.89  ? 712  ARG A CG  1 
ATOM   5368  C  CD  . ARG A  1 712 ? 28.120  -23.012 9.998   1.00 41.00  ? 712  ARG A CD  1 
ATOM   5369  N  NE  . ARG A  1 712 ? 28.668  -21.675 10.207  1.00 42.51  ? 712  ARG A NE  1 
ATOM   5370  C  CZ  . ARG A  1 712 ? 29.420  -21.033 9.317   1.00 46.27  ? 712  ARG A CZ  1 
ATOM   5371  N  NH1 . ARG A  1 712 ? 29.714  -21.595 8.134   1.00 33.53  ? 712  ARG A NH1 1 
ATOM   5372  N  NH2 . ARG A  1 712 ? 29.869  -19.816 9.609   1.00 48.63  ? 712  ARG A NH2 1 
ATOM   5373  N  N   . ARG A  1 713 ? 29.524  -28.190 11.115  1.00 37.90  ? 713  ARG A N   1 
ATOM   5374  C  CA  . ARG A  1 713 ? 29.299  -29.617 11.332  1.00 48.26  ? 713  ARG A CA  1 
ATOM   5375  C  C   . ARG A  1 713 ? 30.397  -30.114 12.283  1.00 47.43  ? 713  ARG A C   1 
ATOM   5376  O  O   . ARG A  1 713 ? 31.124  -29.314 12.834  1.00 54.81  ? 713  ARG A O   1 
ATOM   5377  C  CB  . ARG A  1 713 ? 29.320  -30.350 10.001  1.00 48.00  ? 713  ARG A CB  1 
ATOM   5378  C  CG  . ARG A  1 713 ? 28.718  -29.532 8.861   1.00 39.45  ? 713  ARG A CG  1 
ATOM   5379  C  CD  . ARG A  1 713 ? 27.219  -29.405 9.007   1.00 40.02  ? 713  ARG A CD  1 
ATOM   5380  N  NE  . ARG A  1 713 ? 26.574  -30.710 9.095   1.00 41.63  ? 713  ARG A NE  1 
ATOM   5381  C  CZ  . ARG A  1 713 ? 26.181  -31.424 8.046   1.00 45.98  ? 713  ARG A CZ  1 
ATOM   5382  N  NH1 . ARG A  1 713 ? 26.364  -30.965 6.818   1.00 39.33  ? 713  ARG A NH1 1 
ATOM   5383  N  NH2 . ARG A  1 713 ? 25.598  -32.599 8.234   1.00 52.46  ? 713  ARG A NH2 1 
ATOM   5384  N  N   . ASN A  1 714 ? 30.561  -31.397 12.519  1.00 49.96  ? 714  ASN A N   1 
ATOM   5385  C  CA  . ASN A  1 714 ? 31.708  -31.741 13.371  1.00 50.87  ? 714  ASN A CA  1 
ATOM   5386  C  C   . ASN A  1 714 ? 32.756  -32.453 12.559  1.00 47.36  ? 714  ASN A C   1 
ATOM   5387  O  O   . ASN A  1 714 ? 33.419  -33.367 13.023  1.00 49.73  ? 714  ASN A O   1 
ATOM   5388  C  CB  . ASN A  1 714 ? 31.301  -32.588 14.567  1.00 59.88  ? 714  ASN A CB  1 
ATOM   5389  C  CG  . ASN A  1 714 ? 30.555  -31.799 15.593  1.00 74.37  ? 714  ASN A CG  1 
ATOM   5390  O  OD1 . ASN A  1 714 ? 30.725  -30.590 15.681  1.00 74.78  ? 714  ASN A OD1 1 
ATOM   5391  N  ND2 . ASN A  1 714 ? 29.709  -32.477 16.378  1.00 96.35  ? 714  ASN A ND2 1 
ATOM   5392  N  N   . ILE A  1 715 ? 32.904  -32.021 11.323  1.00 44.05  ? 715  ILE A N   1 
ATOM   5393  C  CA  . ILE A  1 715 ? 33.880  -32.611 10.443  1.00 38.79  ? 715  ILE A CA  1 
ATOM   5394  C  C   . ILE A  1 715 ? 35.279  -32.160 10.875  1.00 39.67  ? 715  ILE A C   1 
ATOM   5395  O  O   . ILE A  1 715 ? 35.978  -31.432 10.187  1.00 33.97  ? 715  ILE A O   1 
ATOM   5396  C  CB  . ILE A  1 715 ? 33.546  -32.236 9.019   1.00 37.58  ? 715  ILE A CB  1 
ATOM   5397  C  CG1 . ILE A  1 715 ? 32.030  -32.367 8.844   1.00 34.06  ? 715  ILE A CG1 1 
ATOM   5398  C  CG2 . ILE A  1 715 ? 34.302  -33.122 8.049   1.00 40.89  ? 715  ILE A CG2 1 
ATOM   5399  C  CD1 . ILE A  1 715 ? 31.510  -32.138 7.443   1.00 38.93  ? 715  ILE A CD1 1 
ATOM   5400  N  N   . SER A  1 716 ? 35.678  -32.621 12.050  1.00 37.79  ? 716  SER A N   1 
ATOM   5401  C  CA  . SER A  1 716 ? 36.822  -32.055 12.727  1.00 38.08  ? 716  SER A CA  1 
ATOM   5402  C  C   . SER A  1 716 ? 38.174  -32.458 12.124  1.00 42.52  ? 716  SER A C   1 
ATOM   5403  O  O   . SER A  1 716 ? 39.160  -31.745 12.301  1.00 42.44  ? 716  SER A O   1 
ATOM   5404  C  CB  . SER A  1 716 ? 36.774  -32.430 14.210  1.00 37.25  ? 716  SER A CB  1 
ATOM   5405  O  OG  . SER A  1 716 ? 37.215  -33.750 14.403  1.00 51.28  ? 716  SER A OG  1 
ATOM   5406  N  N   . ASP A  1 717 ? 38.236  -33.579 11.414  1.00 36.08  ? 717  ASP A N   1 
ATOM   5407  C  CA  . ASP A  1 717 ? 39.510  -33.985 10.816  1.00 41.20  ? 717  ASP A CA  1 
ATOM   5408  C  C   . ASP A  1 717 ? 39.879  -33.109 9.618   1.00 36.11  ? 717  ASP A C   1 
ATOM   5409  O  O   . ASP A  1 717 ? 41.052  -32.893 9.340   1.00 40.13  ? 717  ASP A O   1 
ATOM   5410  C  CB  . ASP A  1 717 ? 39.481  -35.456 10.382  1.00 37.38  ? 717  ASP A CB  1 
ATOM   5411  C  CG  . ASP A  1 717 ? 38.593  -35.694 9.165   1.00 40.63  ? 717  ASP A CG  1 
ATOM   5412  O  OD1 . ASP A  1 717 ? 37.352  -35.565 9.292   1.00 46.18  ? 717  ASP A OD1 1 
ATOM   5413  O  OD2 . ASP A  1 717 ? 39.129  -36.020 8.084   1.00 38.22  ? 717  ASP A OD2 1 
ATOM   5414  N  N   . ILE A  1 718 ? 38.879  -32.628 8.895   1.00 36.85  ? 718  ILE A N   1 
ATOM   5415  C  CA  . ILE A  1 718 ? 39.122  -31.695 7.804   1.00 39.03  ? 718  ILE A CA  1 
ATOM   5416  C  C   . ILE A  1 718 ? 39.336  -30.272 8.344   1.00 40.63  ? 718  ILE A C   1 
ATOM   5417  O  O   . ILE A  1 718 ? 40.241  -29.569 7.896   1.00 39.94  ? 718  ILE A O   1 
ATOM   5418  C  CB  . ILE A  1 718 ? 37.973  -31.699 6.794   1.00 39.12  ? 718  ILE A CB  1 
ATOM   5419  C  CG1 . ILE A  1 718 ? 37.794  -33.113 6.211   1.00 38.42  ? 718  ILE A CG1 1 
ATOM   5420  C  CG2 . ILE A  1 718 ? 38.225  -30.652 5.701   1.00 39.06  ? 718  ILE A CG2 1 
ATOM   5421  C  CD1 . ILE A  1 718 ? 36.656  -33.243 5.224   1.00 36.12  ? 718  ILE A CD1 1 
ATOM   5422  N  N   . SER A  1 719 ? 38.532  -29.850 9.318   1.00 36.82  ? 719  SER A N   1 
ATOM   5423  C  CA  . SER A  1 719 ? 38.715  -28.512 9.844   1.00 36.48  ? 719  SER A CA  1 
ATOM   5424  C  C   . SER A  1 719 ? 40.108  -28.404 10.471  1.00 45.06  ? 719  SER A C   1 
ATOM   5425  O  O   . SER A  1 719 ? 40.772  -27.370 10.326  1.00 42.46  ? 719  SER A O   1 
ATOM   5426  C  CB  . SER A  1 719 ? 37.625  -28.153 10.846  1.00 37.91  ? 719  SER A CB  1 
ATOM   5427  O  OG  . SER A  1 719 ? 37.633  -29.028 11.951  1.00 51.00  ? 719  SER A OG  1 
ATOM   5428  N  N   . GLU A  1 720 ? 40.577  -29.479 11.113  1.00 43.03  ? 720  GLU A N   1 
ATOM   5429  C  CA  . GLU A  1 720 ? 41.907  -29.441 11.711  1.00 41.31  ? 720  GLU A CA  1 
ATOM   5430  C  C   . GLU A  1 720 ? 42.980  -29.369 10.652  1.00 39.75  ? 720  GLU A C   1 
ATOM   5431  O  O   . GLU A  1 720 ? 44.004  -28.714 10.852  1.00 42.96  ? 720  GLU A O   1 
ATOM   5432  C  CB  . GLU A  1 720 ? 42.177  -30.641 12.621  1.00 43.35  ? 720  GLU A CB  1 
ATOM   5433  C  CG  . GLU A  1 720 ? 41.485  -30.610 13.996  1.00 51.03  ? 720  GLU A CG  1 
ATOM   5434  C  CD  . GLU A  1 720 ? 41.688  -29.313 14.771  1.00 61.82  ? 720  GLU A CD  1 
ATOM   5435  O  OE1 . GLU A  1 720 ? 42.857  -28.954 15.051  1.00 69.28  ? 720  GLU A OE1 1 
ATOM   5436  O  OE2 . GLU A  1 720 ? 40.671  -28.658 15.115  1.00 61.21  ? 720  GLU A OE2 1 
ATOM   5437  N  N   . ASN A  1 721 ? 42.774  -30.023 9.517   1.00 38.84  ? 721  ASN A N   1 
ATOM   5438  C  CA  . ASN A  1 721 ? 43.806  -29.947 8.488   1.00 39.55  ? 721  ASN A CA  1 
ATOM   5439  C  C   . ASN A  1 721 ? 43.847  -28.558 7.843   1.00 38.79  ? 721  ASN A C   1 
ATOM   5440  O  O   . ASN A  1 721 ? 44.910  -28.064 7.435   1.00 40.61  ? 721  ASN A O   1 
ATOM   5441  C  CB  . ASN A  1 721 ? 43.598  -31.037 7.437   1.00 44.11  ? 721  ASN A CB  1 
ATOM   5442  C  CG  . ASN A  1 721 ? 44.189  -32.395 7.869   1.00 45.62  ? 721  ASN A CG  1 
ATOM   5443  O  OD1 . ASN A  1 721 ? 45.229  -32.457 8.536   1.00 40.30  ? 721  ASN A OD1 1 
ATOM   5444  N  ND2 . ASN A  1 721 ? 43.522  -33.478 7.483   1.00 31.68  ? 721  ASN A ND2 1 
ATOM   5445  N  N   . LEU A  1 722 ? 42.680  -27.924 7.771   1.00 37.94  ? 722  LEU A N   1 
ATOM   5446  C  CA  . LEU A  1 722 ? 42.587  -26.591 7.209   1.00 43.67  ? 722  LEU A CA  1 
ATOM   5447  C  C   . LEU A  1 722 ? 43.241  -25.619 8.180   1.00 39.78  ? 722  LEU A C   1 
ATOM   5448  O  O   . LEU A  1 722 ? 43.902  -24.675 7.769   1.00 37.24  ? 722  LEU A O   1 
ATOM   5449  C  CB  . LEU A  1 722 ? 41.137  -26.206 6.937   1.00 37.71  ? 722  LEU A CB  1 
ATOM   5450  C  CG  . LEU A  1 722 ? 40.527  -26.681 5.628   1.00 38.34  ? 722  LEU A CG  1 
ATOM   5451  C  CD1 . LEU A  1 722 ? 39.018  -26.537 5.705   1.00 30.44  ? 722  LEU A CD1 1 
ATOM   5452  C  CD2 . LEU A  1 722 ? 41.093  -25.867 4.464   1.00 34.91  ? 722  LEU A CD2 1 
ATOM   5453  N  N   . LYS A  1 723 ? 43.064  -25.879 9.470   1.00 41.47  ? 723  LYS A N   1 
ATOM   5454  C  CA  . LYS A  1 723 ? 43.702  -25.070 10.497  1.00 43.95  ? 723  LYS A CA  1 
ATOM   5455  C  C   . LYS A  1 723 ? 45.212  -25.169 10.304  1.00 45.91  ? 723  LYS A C   1 
ATOM   5456  O  O   . LYS A  1 723 ? 45.902  -24.152 10.194  1.00 48.94  ? 723  LYS A O   1 
ATOM   5457  C  CB  . LYS A  1 723 ? 43.276  -25.516 11.901  1.00 40.28  ? 723  LYS A CB  1 
ATOM   5458  C  CG  . LYS A  1 723 ? 43.586  -24.505 12.989  1.00 43.16  ? 723  LYS A CG  1 
ATOM   5459  C  CD  . LYS A  1 723 ? 43.306  -25.045 14.388  1.00 52.88  ? 723  LYS A CD  1 
ATOM   5460  C  CE  . LYS A  1 723 ? 41.811  -25.238 14.662  1.00 56.57  ? 723  LYS A CE  1 
ATOM   5461  N  NZ  . LYS A  1 723 ? 41.511  -25.471 16.127  1.00 52.71  ? 723  LYS A NZ  1 
ATOM   5462  N  N   . ARG A  1 724 ? 45.721  -26.392 10.207  1.00 45.02  ? 724  ARG A N   1 
ATOM   5463  C  CA  . ARG A  1 724 ? 47.156  -26.577 10.035  1.00 41.42  ? 724  ARG A CA  1 
ATOM   5464  C  C   . ARG A  1 724 ? 47.651  -26.052 8.698   1.00 47.93  ? 724  ARG A C   1 
ATOM   5465  O  O   . ARG A  1 724 ? 48.757  -25.523 8.621   1.00 55.55  ? 724  ARG A O   1 
ATOM   5466  C  CB  . ARG A  1 724 ? 47.537  -28.045 10.185  1.00 46.09  ? 724  ARG A CB  1 
ATOM   5467  C  CG  . ARG A  1 724 ? 47.493  -28.532 11.621  1.00 43.20  ? 724  ARG A CG  1 
ATOM   5468  C  CD  . ARG A  1 724 ? 47.888  -29.999 11.721  1.00 51.07  ? 724  ARG A CD  1 
ATOM   5469  N  NE  . ARG A  1 724 ? 47.215  -30.614 12.853  1.00 55.55  ? 724  ARG A NE  1 
ATOM   5470  C  CZ  . ARG A  1 724 ? 46.080  -31.292 12.754  1.00 55.26  ? 724  ARG A CZ  1 
ATOM   5471  N  NH1 . ARG A  1 724 ? 45.533  -31.468 11.565  1.00 48.65  ? 724  ARG A NH1 1 
ATOM   5472  N  NH2 . ARG A  1 724 ? 45.507  -31.814 13.836  1.00 61.20  ? 724  ARG A NH2 1 
ATOM   5473  N  N   . TYR A  1 725 ? 46.864  -26.182 7.637   1.00 41.02  ? 725  TYR A N   1 
ATOM   5474  C  CA  . TYR A  1 725 ? 47.350  -25.666 6.360   1.00 42.24  ? 725  TYR A CA  1 
ATOM   5475  C  C   . TYR A  1 725 ? 47.441  -24.116 6.324   1.00 45.97  ? 725  TYR A C   1 
ATOM   5476  O  O   . TYR A  1 725 ? 48.335  -23.565 5.676   1.00 43.89  ? 725  TYR A O   1 
ATOM   5477  C  CB  . TYR A  1 725 ? 46.479  -26.188 5.214   1.00 44.59  ? 725  TYR A CB  1 
ATOM   5478  C  CG  . TYR A  1 725 ? 46.874  -25.649 3.866   1.00 37.04  ? 725  TYR A CG  1 
ATOM   5479  C  CD1 . TYR A  1 725 ? 48.100  -25.956 3.291   1.00 39.73  ? 725  TYR A CD1 1 
ATOM   5480  C  CD2 . TYR A  1 725 ? 46.022  -24.804 3.179   1.00 36.31  ? 725  TYR A CD2 1 
ATOM   5481  C  CE1 . TYR A  1 725 ? 48.464  -25.416 2.023   1.00 42.23  ? 725  TYR A CE1 1 
ATOM   5482  C  CE2 . TYR A  1 725 ? 46.352  -24.283 1.944   1.00 43.20  ? 725  TYR A CE2 1 
ATOM   5483  C  CZ  . TYR A  1 725 ? 47.565  -24.579 1.365   1.00 44.73  ? 725  TYR A CZ  1 
ATOM   5484  O  OH  . TYR A  1 725 ? 47.830  -24.012 0.133   1.00 46.37  ? 725  TYR A OH  1 
ATOM   5485  N  N   . LEU A  1 726 ? 46.544  -23.419 7.028   1.00 42.17  ? 726  LEU A N   1 
ATOM   5486  C  CA  . LEU A  1 726 ? 46.531  -21.954 7.000   1.00 42.15  ? 726  LEU A CA  1 
ATOM   5487  C  C   . LEU A  1 726 ? 47.601  -21.336 7.906   1.00 43.37  ? 726  LEU A C   1 
ATOM   5488  O  O   . LEU A  1 726 ? 48.278  -20.411 7.520   1.00 39.63  ? 726  LEU A O   1 
ATOM   5489  C  CB  . LEU A  1 726 ? 45.160  -21.426 7.401   1.00 40.01  ? 726  LEU A CB  1 
ATOM   5490  C  CG  . LEU A  1 726 ? 44.087  -21.598 6.335   1.00 40.76  ? 726  LEU A CG  1 
ATOM   5491  C  CD1 . LEU A  1 726 ? 42.724  -21.390 6.926   1.00 38.67  ? 726  LEU A CD1 1 
ATOM   5492  C  CD2 . LEU A  1 726 ? 44.312  -20.645 5.197   1.00 43.40  ? 726  LEU A CD2 1 
ATOM   5493  N  N   . LEU A  1 727 ? 47.754  -21.856 9.111   1.00 40.98  ? 727  LEU A N   1 
ATOM   5494  C  CA  . LEU A  1 727 ? 48.772  -21.361 10.005  1.00 35.19  ? 727  LEU A CA  1 
ATOM   5495  C  C   . LEU A  1 727 ? 50.182  -21.653 9.493   1.00 45.03  ? 727  LEU A C   1 
ATOM   5496  O  O   . LEU A  1 727 ? 51.116  -20.910 9.778   1.00 49.19  ? 727  LEU A O   1 
ATOM   5497  C  CB  . LEU A  1 727 ? 48.577  -21.964 11.397  1.00 49.80  ? 727  LEU A CB  1 
ATOM   5498  C  CG  . LEU A  1 727 ? 47.239  -21.628 12.075  1.00 42.59  ? 727  LEU A CG  1 
ATOM   5499  C  CD1 . LEU A  1 727 ? 47.187  -22.104 13.515  1.00 38.93  ? 727  LEU A CD1 1 
ATOM   5500  C  CD2 . LEU A  1 727 ? 46.979  -20.136 11.997  1.00 44.47  ? 727  LEU A CD2 1 
ATOM   5501  N  N   . GLN A  1 728 ? 50.339  -22.721 8.718   1.00 52.22  ? 728  GLN A N   1 
ATOM   5502  C  CA  . GLN A  1 728 ? 51.668  -23.144 8.268   1.00 52.84  ? 728  GLN A CA  1 
ATOM   5503  C  C   . GLN A  1 728 ? 52.053  -22.567 6.904   1.00 46.92  ? 728  GLN A C   1 
ATOM   5504  O  O   . GLN A  1 728 ? 53.070  -21.900 6.770   1.00 50.76  ? 728  GLN A O   1 
ATOM   5505  C  CB  . GLN A  1 728 ? 51.748  -24.669 8.234   1.00 47.40  ? 728  GLN A CB  1 
ATOM   5506  C  CG  . GLN A  1 728 ? 53.021  -25.234 7.572   1.00 63.19  ? 728  GLN A CG  1 
ATOM   5507  C  CD  . GLN A  1 728 ? 52.886  -25.467 6.060   1.00 63.47  ? 728  GLN A CD  1 
ATOM   5508  O  OE1 . GLN A  1 728 ? 51.912  -26.068 5.585   1.00 63.35  ? 728  GLN A OE1 1 
ATOM   5509  N  NE2 . GLN A  1 728 ? 53.868  -24.984 5.300   1.00 67.55  ? 728  GLN A NE2 1 
ATOM   5510  N  N   . TYR A  1 729 ? 51.272  -22.892 5.885   1.00 43.66  ? 729  TYR A N   1 
ATOM   5511  C  CA  . TYR A  1 729 ? 51.269  -22.134 4.650   1.00 47.34  ? 729  TYR A CA  1 
ATOM   5512  C  C   . TYR A  1 729 ? 50.600  -20.831 5.016   1.00 53.31  ? 729  TYR A C   1 
ATOM   5513  O  O   . TYR A  1 729 ? 49.443  -20.888 5.369   1.00 62.53  ? 729  TYR A O   1 
ATOM   5514  C  CB  . TYR A  1 729 ? 50.471  -22.862 3.587   1.00 46.38  ? 729  TYR A CB  1 
ATOM   5515  C  CG  . TYR A  1 729 ? 50.952  -22.706 2.169   1.00 48.54  ? 729  TYR A CG  1 
ATOM   5516  C  CD1 . TYR A  1 729 ? 52.011  -23.466 1.697   1.00 48.39  ? 729  TYR A CD1 1 
ATOM   5517  C  CD2 . TYR A  1 729 ? 50.303  -21.842 1.278   1.00 43.82  ? 729  TYR A CD2 1 
ATOM   5518  C  CE1 . TYR A  1 729 ? 52.437  -23.347 0.379   1.00 54.01  ? 729  TYR A CE1 1 
ATOM   5519  C  CE2 . TYR A  1 729 ? 50.721  -21.719 -0.041  1.00 46.41  ? 729  TYR A CE2 1 
ATOM   5520  C  CZ  . TYR A  1 729 ? 51.790  -22.474 -0.485  1.00 52.35  ? 729  TYR A CZ  1 
ATOM   5521  O  OH  . TYR A  1 729 ? 52.232  -22.359 -1.783  1.00 48.70  ? 729  TYR A OH  1 
ATOM   5522  N  N   . PHE A  1 730 ? 51.317  -19.707 4.980   1.00 43.93  ? 730  PHE A N   1 
ATOM   5523  C  CA  . PHE A  1 730 ? 50.857  -18.352 5.399   1.00 51.07  ? 730  PHE A CA  1 
ATOM   5524  C  C   . PHE A  1 730 ? 51.420  -17.975 6.751   1.00 49.88  ? 730  PHE A C   1 
ATOM   5525  O  O   . PHE A  1 730 ? 51.114  -16.906 7.277   1.00 47.69  ? 730  PHE A O   1 
ATOM   5526  C  CB  . PHE A  1 730 ? 49.322  -18.173 5.433   1.00 37.91  ? 730  PHE A CB  1 
ATOM   5527  C  CG  . PHE A  1 730 ? 48.673  -18.379 4.101   1.00 47.36  ? 730  PHE A CG  1 
ATOM   5528  C  CD1 . PHE A  1 730 ? 49.088  -17.642 3.001   1.00 47.21  ? 730  PHE A CD1 1 
ATOM   5529  C  CD2 . PHE A  1 730 ? 47.675  -19.328 3.932   1.00 42.76  ? 730  PHE A CD2 1 
ATOM   5530  C  CE1 . PHE A  1 730 ? 48.522  -17.845 1.760   1.00 44.75  ? 730  PHE A CE1 1 
ATOM   5531  C  CE2 . PHE A  1 730 ? 47.114  -19.535 2.709   1.00 42.87  ? 730  PHE A CE2 1 
ATOM   5532  C  CZ  . PHE A  1 730 ? 47.530  -18.792 1.617   1.00 44.22  ? 730  PHE A CZ  1 
ATOM   5533  N  N   . LYS A  1 731 ? 52.260  -18.834 7.310   1.00 50.11  ? 731  LYS A N   1 
ATOM   5534  C  CA  . LYS A  1 731 ? 52.984  -18.454 8.522   1.00 54.36  ? 731  LYS A CA  1 
ATOM   5535  C  C   . LYS A  1 731 ? 53.843  -17.194 8.290   1.00 54.63  ? 731  LYS A C   1 
ATOM   5536  O  O   . LYS A  1 731 ? 53.861  -16.297 9.143   1.00 53.25  ? 731  LYS A O   1 
ATOM   5537  C  CB  . LYS A  1 731 ? 53.852  -19.609 9.033   1.00 51.21  ? 731  LYS A CB  1 
ATOM   5538  C  CG  . LYS A  1 731 ? 54.628  -19.302 10.305  1.00 51.81  ? 731  LYS A CG  1 
ATOM   5539  C  CD  . LYS A  1 731 ? 55.402  -20.532 10.782  1.00 52.03  ? 731  LYS A CD  1 
ATOM   5540  C  CE  . LYS A  1 731 ? 56.367  -20.181 11.897  1.00 47.84  ? 731  LYS A CE  1 
ATOM   5541  N  NZ  . LYS A  1 731 ? 55.663  -19.528 13.027  1.00 59.12  ? 731  LYS A NZ  1 
ATOM   5542  N  N   . PRO A  1 732 ? 54.556  -17.118 7.146   1.00 49.56  ? 732  PRO A N   1 
ATOM   5543  C  CA  . PRO A  1 732 ? 55.338  -15.899 6.938   1.00 52.65  ? 732  PRO A CA  1 
ATOM   5544  C  C   . PRO A  1 732 ? 54.508  -14.628 7.069   1.00 55.19  ? 732  PRO A C   1 
ATOM   5545  O  O   . PRO A  1 732 ? 54.880  -13.747 7.854   1.00 57.08  ? 732  PRO A O   1 
ATOM   5546  C  CB  . PRO A  1 732 ? 55.877  -16.067 5.514   1.00 50.33  ? 732  PRO A CB  1 
ATOM   5547  C  CG  . PRO A  1 732 ? 55.178  -17.274 4.954   1.00 49.39  ? 732  PRO A CG  1 
ATOM   5548  C  CD  . PRO A  1 732 ? 54.877  -18.122 6.122   1.00 40.05  ? 732  PRO A CD  1 
ATOM   5549  N  N   . VAL A  1 733 ? 53.386  -14.550 6.363   1.00 54.43  ? 733  VAL A N   1 
ATOM   5550  C  CA  . VAL A  1 733 ? 52.576  -13.339 6.404   1.00 54.65  ? 733  VAL A CA  1 
ATOM   5551  C  C   . VAL A  1 733 ? 52.010  -13.067 7.802   1.00 50.78  ? 733  VAL A C   1 
ATOM   5552  O  O   . VAL A  1 733 ? 52.151  -11.967 8.317   1.00 52.87  ? 733  VAL A O   1 
ATOM   5553  C  CB  . VAL A  1 733 ? 51.421  -13.390 5.396   1.00 51.64  ? 733  VAL A CB  1 
ATOM   5554  C  CG1 . VAL A  1 733 ? 51.107  -11.980 4.924   1.00 49.74  ? 733  VAL A CG1 1 
ATOM   5555  C  CG2 . VAL A  1 733 ? 51.798  -14.254 4.215   1.00 63.94  ? 733  VAL A CG2 1 
ATOM   5556  N  N   . ILE A  1 734 ? 51.374  -14.057 8.417   1.00 48.89  ? 734  ILE A N   1 
ATOM   5557  C  CA  . ILE A  1 734 ? 50.794  -13.859 9.739   1.00 46.13  ? 734  ILE A CA  1 
ATOM   5558  C  C   . ILE A  1 734 ? 51.826  -13.389 10.777  1.00 54.69  ? 734  ILE A C   1 
ATOM   5559  O  O   . ILE A  1 734 ? 51.550  -12.524 11.612  1.00 51.45  ? 734  ILE A O   1 
ATOM   5560  C  CB  . ILE A  1 734 ? 50.136  -15.134 10.233  1.00 40.31  ? 734  ILE A CB  1 
ATOM   5561  C  CG1 . ILE A  1 734 ? 48.908  -15.436 9.397   1.00 42.69  ? 734  ILE A CG1 1 
ATOM   5562  C  CG2 . ILE A  1 734 ? 49.706  -15.002 11.689  1.00 44.48  ? 734  ILE A CG2 1 
ATOM   5563  C  CD1 . ILE A  1 734 ? 48.297  -16.776 9.727   1.00 49.45  ? 734  ILE A CD1 1 
ATOM   5564  N  N   . ASP A  1 735 ? 53.023  -13.952 10.733  1.00 56.55  ? 735  ASP A N   1 
ATOM   5565  C  CA  . ASP A  1 735 ? 54.030  -13.550 11.703  1.00 61.04  ? 735  ASP A CA  1 
ATOM   5566  C  C   . ASP A  1 735 ? 54.581  -12.131 11.448  1.00 54.37  ? 735  ASP A C   1 
ATOM   5567  O  O   . ASP A  1 735 ? 55.258  -11.563 12.287  1.00 52.82  ? 735  ASP A O   1 
ATOM   5568  C  CB  . ASP A  1 735 ? 55.163  -14.577 11.721  1.00 53.37  ? 735  ASP A CB  1 
ATOM   5569  C  CG  . ASP A  1 735 ? 54.788  -15.832 12.487  1.00 66.45  ? 735  ASP A CG  1 
ATOM   5570  O  OD1 . ASP A  1 735 ? 53.692  -15.850 13.100  1.00 64.68  ? 735  ASP A OD1 1 
ATOM   5571  O  OD2 . ASP A  1 735 ? 55.592  -16.794 12.493  1.00 72.54  ? 735  ASP A OD2 1 
ATOM   5572  N  N   . ARG A  1 736 ? 54.266  -11.556 10.299  1.00 53.91  ? 736  ARG A N   1 
ATOM   5573  C  CA  . ARG A  1 736 ? 54.856  -10.282 9.891   1.00 56.81  ? 736  ARG A CA  1 
ATOM   5574  C  C   . ARG A  1 736 ? 54.094  -9.089  10.469  1.00 58.83  ? 736  ARG A C   1 
ATOM   5575  O  O   . ARG A  1 736 ? 54.419  -7.934  10.181  1.00 57.23  ? 736  ARG A O   1 
ATOM   5576  C  CB  . ARG A  1 736 ? 54.879  -10.189 8.364   1.00 48.09  ? 736  ARG A CB  1 
ATOM   5577  C  CG  . ARG A  1 736 ? 56.120  -9.610  7.760   1.00 56.76  ? 736  ARG A CG  1 
ATOM   5578  C  CD  . ARG A  1 736 ? 56.080  -9.759  6.229   1.00 59.16  ? 736  ARG A CD  1 
ATOM   5579  N  NE  . ARG A  1 736 ? 56.036  -11.170 5.858   1.00 55.44  ? 736  ARG A NE  1 
ATOM   5580  C  CZ  . ARG A  1 736 ? 55.894  -11.642 4.623   1.00 56.75  ? 736  ARG A CZ  1 
ATOM   5581  N  NH1 . ARG A  1 736 ? 55.766  -10.827 3.581   1.00 55.84  ? 736  ARG A NH1 1 
ATOM   5582  N  NH2 . ARG A  1 736 ? 55.866  -12.953 4.437   1.00 64.30  ? 736  ARG A NH2 1 
ATOM   5583  N  N   . GLN A  1 737 ? 53.092  -9.371  11.294  1.00 49.71  ? 737  GLN A N   1 
ATOM   5584  C  CA  . GLN A  1 737 ? 52.068  -8.379  11.590  1.00 51.08  ? 737  GLN A CA  1 
ATOM   5585  C  C   . GLN A  1 737 ? 52.181  -7.817  12.996  1.00 47.33  ? 737  GLN A C   1 
ATOM   5586  O  O   . GLN A  1 737 ? 52.205  -8.569  13.960  1.00 51.90  ? 737  GLN A O   1 
ATOM   5587  C  CB  . GLN A  1 737 ? 50.682  -9.002  11.381  1.00 44.86  ? 737  GLN A CB  1 
ATOM   5588  C  CG  . GLN A  1 737 ? 50.500  -9.597  10.008  1.00 41.59  ? 737  GLN A CG  1 
ATOM   5589  C  CD  . GLN A  1 737 ? 50.388  -8.545  8.927   1.00 43.09  ? 737  GLN A CD  1 
ATOM   5590  O  OE1 . GLN A  1 737 ? 49.773  -7.503  9.124   1.00 44.81  ? 737  GLN A OE1 1 
ATOM   5591  N  NE2 . GLN A  1 737 ? 50.979  -8.813  7.773   1.00 48.23  ? 737  GLN A NE2 1 
ATOM   5592  N  N   . SER A  1 738 ? 52.238  -6.497  13.120  1.00 44.53  ? 738  SER A N   1 
ATOM   5593  C  CA  . SER A  1 738 ? 52.406  -5.897  14.442  1.00 48.13  ? 738  SER A CA  1 
ATOM   5594  C  C   . SER A  1 738 ? 51.066  -5.794  15.132  1.00 45.86  ? 738  SER A C   1 
ATOM   5595  O  O   . SER A  1 738 ? 50.049  -5.836  14.489  1.00 52.31  ? 738  SER A O   1 
ATOM   5596  C  CB  . SER A  1 738 ? 53.060  -4.518  14.345  1.00 45.34  ? 738  SER A CB  1 
ATOM   5597  O  OG  . SER A  1 738 ? 52.258  -3.605  13.613  1.00 52.91  ? 738  SER A OG  1 
ATOM   5598  N  N   . TRP A  1 739 ? 51.054  -5.689  16.444  1.00 49.71  ? 739  TRP A N   1 
ATOM   5599  C  CA  . TRP A  1 739 ? 49.804  -5.404  17.127  1.00 51.52  ? 739  TRP A CA  1 
ATOM   5600  C  C   . TRP A  1 739 ? 49.746  -3.898  17.355  1.00 47.25  ? 739  TRP A C   1 
ATOM   5601  O  O   . TRP A  1 739 ? 49.793  -3.435  18.486  1.00 47.23  ? 739  TRP A O   1 
ATOM   5602  C  CB  . TRP A  1 739 ? 49.687  -6.208  18.439  1.00 48.09  ? 739  TRP A CB  1 
ATOM   5603  C  CG  . TRP A  1 739 ? 49.384  -7.677  18.161  1.00 52.57  ? 739  TRP A CG  1 
ATOM   5604  C  CD1 . TRP A  1 739 ? 50.207  -8.581  17.555  1.00 50.51  ? 739  TRP A CD1 1 
ATOM   5605  C  CD2 . TRP A  1 739 ? 48.162  -8.374  18.431  1.00 43.70  ? 739  TRP A CD2 1 
ATOM   5606  N  NE1 . TRP A  1 739 ? 49.582  -9.793  17.446  1.00 51.44  ? 739  TRP A NE1 1 
ATOM   5607  C  CE2 . TRP A  1 739 ? 48.326  -9.695  17.979  1.00 47.35  ? 739  TRP A CE2 1 
ATOM   5608  C  CE3 . TRP A  1 739 ? 46.953  -8.010  19.019  1.00 43.29  ? 739  TRP A CE3 1 
ATOM   5609  C  CZ2 . TRP A  1 739 ? 47.324  -10.657 18.095  1.00 49.62  ? 739  TRP A CZ2 1 
ATOM   5610  C  CZ3 . TRP A  1 739 ? 45.957  -8.960  19.138  1.00 49.79  ? 739  TRP A CZ3 1 
ATOM   5611  C  CH2 . TRP A  1 739 ? 46.146  -10.272 18.679  1.00 47.83  ? 739  TRP A CH2 1 
ATOM   5612  N  N   . SER A  1 740 ? 49.639  -3.160  16.251  1.00 44.70  ? 740  SER A N   1 
ATOM   5613  C  CA  . SER A  1 740 ? 49.624  -1.699  16.239  1.00 48.01  ? 740  SER A CA  1 
ATOM   5614  C  C   . SER A  1 740 ? 48.626  -1.113  15.225  1.00 49.61  ? 740  SER A C   1 
ATOM   5615  O  O   . SER A  1 740 ? 47.888  -1.840  14.573  1.00 51.43  ? 740  SER A O   1 
ATOM   5616  C  CB  . SER A  1 740 ? 51.015  -1.170  15.906  1.00 48.46  ? 740  SER A CB  1 
ATOM   5617  O  OG  . SER A  1 740 ? 51.265  -1.321  14.516  1.00 46.98  ? 740  SER A OG  1 
ATOM   5618  N  N   . ASP A  1 741 ? 48.630  0.209   15.077  1.00 55.09  ? 741  ASP A N   1 
ATOM   5619  C  CA  . ASP A  1 741 ? 47.810  0.878   14.063  1.00 50.46  ? 741  ASP A CA  1 
ATOM   5620  C  C   . ASP A  1 741 ? 48.645  1.450   12.929  1.00 52.24  ? 741  ASP A C   1 
ATOM   5621  O  O   . ASP A  1 741 ? 48.201  2.390   12.275  1.00 54.07  ? 741  ASP A O   1 
ATOM   5622  C  CB  . ASP A  1 741 ? 46.984  2.013   14.683  1.00 44.80  ? 741  ASP A CB  1 
ATOM   5623  C  CG  . ASP A  1 741 ? 45.818  1.503   15.523  1.00 52.78  ? 741  ASP A CG  1 
ATOM   5624  O  OD1 . ASP A  1 741 ? 45.279  0.427   15.201  1.00 56.71  ? 741  ASP A OD1 1 
ATOM   5625  O  OD2 . ASP A  1 741 ? 45.429  2.170   16.506  1.00 53.60  ? 741  ASP A OD2 1 
ATOM   5626  N  N   . LYS A  1 742 ? 49.833  0.889   12.683  1.00 50.85  ? 742  LYS A N   1 
ATOM   5627  C  CA  . LYS A  1 742 ? 50.823  1.553   11.820  1.00 51.04  ? 742  LYS A CA  1 
ATOM   5628  C  C   . LYS A  1 742 ? 50.663  1.227   10.347  1.00 48.92  ? 742  LYS A C   1 
ATOM   5629  O  O   . LYS A  1 742 ? 49.850  0.388   9.984   1.00 54.09  ? 742  LYS A O   1 
ATOM   5630  C  CB  . LYS A  1 742 ? 52.238  1.204   12.279  1.00 51.41  ? 742  LYS A CB  1 
ATOM   5631  C  CG  . LYS A  1 742 ? 52.534  1.675   13.698  1.00 48.06  ? 742  LYS A CG  1 
ATOM   5632  C  CD  . LYS A  1 742 ? 53.905  1.189   14.142  1.00 58.27  ? 742  LYS A CD  1 
ATOM   5633  C  CE  . LYS A  1 742 ? 54.141  1.451   15.630  1.00 70.90  ? 742  LYS A CE  1 
ATOM   5634  N  NZ  . LYS A  1 742 ? 55.391  0.798   16.141  1.00 66.34  ? 742  LYS A NZ  1 
ATOM   5635  N  N   . GLY A  1 743 ? 51.425  1.908   9.495   1.00 50.62  ? 743  GLY A N   1 
ATOM   5636  C  CA  . GLY A  1 743 ? 51.390  1.645   8.065   1.00 48.47  ? 743  GLY A CA  1 
ATOM   5637  C  C   . GLY A  1 743 ? 50.202  2.250   7.331   1.00 53.30  ? 743  GLY A C   1 
ATOM   5638  O  O   . GLY A  1 743 ? 49.382  2.958   7.910   1.00 52.04  ? 743  GLY A O   1 
ATOM   5639  N  N   . SER A  1 744 ? 50.108  1.973   6.037   1.00 56.97  ? 744  SER A N   1 
ATOM   5640  C  CA  . SER A  1 744 ? 49.012  2.477   5.220   1.00 51.59  ? 744  SER A CA  1 
ATOM   5641  C  C   . SER A  1 744 ? 47.683  1.819   5.546   1.00 51.54  ? 744  SER A C   1 
ATOM   5642  O  O   . SER A  1 744 ? 47.613  0.896   6.347   1.00 54.57  ? 744  SER A O   1 
ATOM   5643  C  CB  . SER A  1 744 ? 49.304  2.242   3.750   1.00 54.65  ? 744  SER A CB  1 
ATOM   5644  O  OG  . SER A  1 744 ? 48.820  0.963   3.370   1.00 60.81  ? 744  SER A OG  1 
ATOM   5645  N  N   . VAL A  1 745 ? 46.631  2.277   4.885   1.00 55.28  ? 745  VAL A N   1 
ATOM   5646  C  CA  . VAL A  1 745 ? 45.300  1.724   5.096   1.00 57.86  ? 745  VAL A CA  1 
ATOM   5647  C  C   . VAL A  1 745 ? 45.256  0.225   4.805   1.00 59.36  ? 745  VAL A C   1 
ATOM   5648  O  O   . VAL A  1 745 ? 44.733  -0.545  5.624   1.00 57.72  ? 745  VAL A O   1 
ATOM   5649  C  CB  . VAL A  1 745 ? 44.237  2.452   4.238   1.00 59.82  ? 745  VAL A CB  1 
ATOM   5650  C  CG1 . VAL A  1 745 ? 43.013  1.559   4.015   1.00 52.73  ? 745  VAL A CG1 1 
ATOM   5651  C  CG2 . VAL A  1 745 ? 43.835  3.783   4.895   1.00 51.81  ? 745  VAL A CG2 1 
ATOM   5652  N  N   . TRP A  1 746 ? 45.803  -0.200  3.663   1.00 57.68  ? 746  TRP A N   1 
ATOM   5653  C  CA  . TRP A  1 746 ? 45.845  -1.632  3.368   1.00 57.54  ? 746  TRP A CA  1 
ATOM   5654  C  C   . TRP A  1 746 ? 46.618  -2.414  4.433   1.00 56.30  ? 746  TRP A C   1 
ATOM   5655  O  O   . TRP A  1 746 ? 46.135  -3.450  4.895   1.00 56.08  ? 746  TRP A O   1 
ATOM   5656  C  CB  . TRP A  1 746 ? 46.452  -1.912  1.995   1.00 62.10  ? 746  TRP A CB  1 
ATOM   5657  C  CG  . TRP A  1 746 ? 45.431  -2.070  0.901   1.00 63.88  ? 746  TRP A CG  1 
ATOM   5658  C  CD1 . TRP A  1 746 ? 45.395  -1.382  -0.276  1.00 67.83  ? 746  TRP A CD1 1 
ATOM   5659  C  CD2 . TRP A  1 746 ? 44.300  -2.962  0.876   1.00 63.63  ? 746  TRP A CD2 1 
ATOM   5660  N  NE1 . TRP A  1 746 ? 44.315  -1.782  -1.033  1.00 62.95  ? 746  TRP A NE1 1 
ATOM   5661  C  CE2 . TRP A  1 746 ? 43.625  -2.748  -0.351  1.00 66.97  ? 746  TRP A CE2 1 
ATOM   5662  C  CE3 . TRP A  1 746 ? 43.795  -3.920  1.761   1.00 61.35  ? 746  TRP A CE3 1 
ATOM   5663  C  CZ2 . TRP A  1 746 ? 42.466  -3.457  -0.711  1.00 55.94  ? 746  TRP A CZ2 1 
ATOM   5664  C  CZ3 . TRP A  1 746 ? 42.645  -4.618  1.402   1.00 59.15  ? 746  TRP A CZ3 1 
ATOM   5665  C  CH2 . TRP A  1 746 ? 42.001  -4.388  0.167   1.00 54.06  ? 746  TRP A CH2 1 
ATOM   5666  N  N   . ASP A  1 747 ? 47.798  -1.924  4.817   1.00 48.34  ? 747  ASP A N   1 
ATOM   5667  C  CA  . ASP A  1 747 ? 48.582  -2.562  5.869   1.00 48.59  ? 747  ASP A CA  1 
ATOM   5668  C  C   . ASP A  1 747 ? 47.711  -2.798  7.091   1.00 53.63  ? 747  ASP A C   1 
ATOM   5669  O  O   . ASP A  1 747 ? 47.665  -3.915  7.642   1.00 53.89  ? 747  ASP A O   1 
ATOM   5670  C  CB  . ASP A  1 747 ? 49.796  -1.710  6.275   1.00 50.19  ? 747  ASP A CB  1 
ATOM   5671  C  CG  . ASP A  1 747 ? 50.601  -1.215  5.088   1.00 57.85  ? 747  ASP A CG  1 
ATOM   5672  O  OD1 . ASP A  1 747 ? 50.792  -1.985  4.118   1.00 63.00  ? 747  ASP A OD1 1 
ATOM   5673  O  OD2 . ASP A  1 747 ? 51.049  -0.047  5.125   1.00 57.00  ? 747  ASP A OD2 1 
ATOM   5674  N  N   . ARG A  1 748 ? 47.018  -1.736  7.499   1.00 49.25  ? 748  ARG A N   1 
ATOM   5675  C  CA  . ARG A  1 748 ? 46.182  -1.749  8.691   1.00 48.97  ? 748  ARG A CA  1 
ATOM   5676  C  C   . ARG A  1 748 ? 45.059  -2.775  8.569   1.00 49.24  ? 748  ARG A C   1 
ATOM   5677  O  O   . ARG A  1 748 ? 44.690  -3.434  9.551   1.00 51.45  ? 748  ARG A O   1 
ATOM   5678  C  CB  . ARG A  1 748 ? 45.602  -0.351  8.961   1.00 48.61  ? 748  ARG A CB  1 
ATOM   5679  C  CG  . ARG A  1 748 ? 46.645  0.691   9.368   1.00 48.60  ? 748  ARG A CG  1 
ATOM   5680  C  CD  . ARG A  1 748 ? 46.008  1.993   9.847   1.00 49.95  ? 748  ARG A CD  1 
ATOM   5681  N  NE  . ARG A  1 748 ? 45.286  1.823   11.108  1.00 47.91  ? 748  ARG A NE  1 
ATOM   5682  C  CZ  . ARG A  1 748 ? 44.496  2.739   11.667  1.00 44.29  ? 748  ARG A CZ  1 
ATOM   5683  N  NH1 . ARG A  1 748 ? 44.316  3.916   11.089  1.00 50.58  ? 748  ARG A NH1 1 
ATOM   5684  N  NH2 . ARG A  1 748 ? 43.882  2.473   12.814  1.00 48.68  ? 748  ARG A NH2 1 
ATOM   5685  N  N   . MET A  1 749 ? 44.524  -2.924  7.366   1.00 48.04  ? 749  MET A N   1 
ATOM   5686  C  CA  . MET A  1 749 ? 43.434  -3.867  7.156   1.00 52.34  ? 749  MET A CA  1 
ATOM   5687  C  C   . MET A  1 749 ? 43.919  -5.288  6.885   1.00 49.50  ? 749  MET A C   1 
ATOM   5688  O  O   . MET A  1 749 ? 43.207  -6.243  7.185   1.00 50.07  ? 749  MET A O   1 
ATOM   5689  C  CB  . MET A  1 749 ? 42.538  -3.382  6.030   1.00 49.83  ? 749  MET A CB  1 
ATOM   5690  C  CG  . MET A  1 749 ? 41.915  -2.045  6.371   1.00 56.55  ? 749  MET A CG  1 
ATOM   5691  S  SD  . MET A  1 749 ? 40.421  -1.733  5.432   1.00 81.22  ? 749  MET A SD  1 
ATOM   5692  C  CE  . MET A  1 749 ? 41.122  -1.601  3.768   1.00 62.93  ? 749  MET A CE  1 
ATOM   5693  N  N   . LEU A  1 750 ? 45.124  -5.434  6.341   1.00 45.64  ? 750  LEU A N   1 
ATOM   5694  C  CA  . LEU A  1 750 ? 45.723  -6.758  6.216   1.00 45.65  ? 750  LEU A CA  1 
ATOM   5695  C  C   . LEU A  1 750 ? 45.918  -7.341  7.601   1.00 46.90  ? 750  LEU A C   1 
ATOM   5696  O  O   . LEU A  1 750 ? 45.660  -8.517  7.833   1.00 45.16  ? 750  LEU A O   1 
ATOM   5697  C  CB  . LEU A  1 750 ? 47.058  -6.697  5.477   1.00 45.90  ? 750  LEU A CB  1 
ATOM   5698  C  CG  . LEU A  1 750 ? 47.723  -8.012  5.063   1.00 43.60  ? 750  LEU A CG  1 
ATOM   5699  C  CD1 . LEU A  1 750 ? 46.760  -8.856  4.248   1.00 45.62  ? 750  LEU A CD1 1 
ATOM   5700  C  CD2 . LEU A  1 750 ? 48.967  -7.738  4.240   1.00 38.33  ? 750  LEU A CD2 1 
ATOM   5701  N  N   . ARG A  1 751 ? 46.342  -6.481  8.521   1.00 47.86  ? 751  ARG A N   1 
ATOM   5702  C  CA  . ARG A  1 751 ? 46.652  -6.854  9.893   1.00 41.77  ? 751  ARG A CA  1 
ATOM   5703  C  C   . ARG A  1 751 ? 45.437  -7.368  10.666  1.00 43.84  ? 751  ARG A C   1 
ATOM   5704  O  O   . ARG A  1 751 ? 45.497  -8.421  11.310  1.00 44.00  ? 751  ARG A O   1 
ATOM   5705  C  CB  . ARG A  1 751 ? 47.283  -5.648  10.621  1.00 44.35  ? 751  ARG A CB  1 
ATOM   5706  C  CG  . ARG A  1 751 ? 47.030  -5.595  12.120  1.00 40.01  ? 751  ARG A CG  1 
ATOM   5707  C  CD  . ARG A  1 751 ? 47.994  -4.660  12.853  1.00 44.73  ? 751  ARG A CD  1 
ATOM   5708  N  NE  . ARG A  1 751 ? 48.157  -3.337  12.255  1.00 52.28  ? 751  ARG A NE  1 
ATOM   5709  C  CZ  . ARG A  1 751 ? 49.287  -2.888  11.714  1.00 52.95  ? 751  ARG A CZ  1 
ATOM   5710  N  NH1 . ARG A  1 751 ? 50.370  -3.654  11.691  1.00 55.25  ? 751  ARG A NH1 1 
ATOM   5711  N  NH2 . ARG A  1 751 ? 49.332  -1.671  11.192  1.00 53.62  ? 751  ARG A NH2 1 
ATOM   5712  N  N   . SER A  1 752 ? 44.337  -6.631  10.624  1.00 43.85  ? 752  SER A N   1 
ATOM   5713  C  CA  . SER A  1 752 ? 43.192  -7.011  11.439  1.00 46.69  ? 752  SER A CA  1 
ATOM   5714  C  C   . SER A  1 752 ? 42.584  -8.253  10.842  1.00 43.59  ? 752  SER A C   1 
ATOM   5715  O  O   . SER A  1 752 ? 42.024  -9.085  11.535  1.00 43.62  ? 752  SER A O   1 
ATOM   5716  C  CB  . SER A  1 752 ? 42.170  -5.886  11.518  1.00 41.95  ? 752  SER A CB  1 
ATOM   5717  O  OG  . SER A  1 752 ? 42.212  -5.118  10.335  1.00 63.07  ? 752  SER A OG  1 
ATOM   5718  N  N   . ALA A  1 753 ? 42.739  -8.370  9.537   1.00 39.44  ? 753  ALA A N   1 
ATOM   5719  C  CA  . ALA A  1 753 ? 42.264  -9.511  8.802   1.00 39.06  ? 753  ALA A CA  1 
ATOM   5720  C  C   . ALA A  1 753 ? 43.044  -10.755 9.208   1.00 40.36  ? 753  ALA A C   1 
ATOM   5721  O  O   . ALA A  1 753 ? 42.456  -11.721 9.674   1.00 38.63  ? 753  ALA A O   1 
ATOM   5722  C  CB  . ALA A  1 753 ? 42.381  -9.249  7.310   1.00 38.02  ? 753  ALA A CB  1 
ATOM   5723  N  N   . LEU A  1 754 ? 44.366  -10.723 9.052   1.00 39.62  ? 754  LEU A N   1 
ATOM   5724  C  CA  . LEU A  1 754 ? 45.197  -11.882 9.375   1.00 37.32  ? 754  LEU A CA  1 
ATOM   5725  C  C   . LEU A  1 754 ? 45.189  -12.230 10.863  1.00 45.09  ? 754  LEU A C   1 
ATOM   5726  O  O   . LEU A  1 754 ? 45.182  -13.413 11.230  1.00 44.69  ? 754  LEU A O   1 
ATOM   5727  C  CB  . LEU A  1 754 ? 46.631  -11.656 8.899   1.00 40.88  ? 754  LEU A CB  1 
ATOM   5728  C  CG  . LEU A  1 754 ? 46.859  -11.432 7.387   1.00 44.90  ? 754  LEU A CG  1 
ATOM   5729  C  CD1 . LEU A  1 754 ? 48.318  -11.104 7.065   1.00 39.84  ? 754  LEU A CD1 1 
ATOM   5730  C  CD2 . LEU A  1 754 ? 46.397  -12.622 6.568   1.00 39.85  ? 754  LEU A CD2 1 
ATOM   5731  N  N   . LEU A  1 755 ? 45.169  -11.221 11.728  1.00 43.86  ? 755  LEU A N   1 
ATOM   5732  C  CA  . LEU A  1 755 ? 45.256  -11.502 13.149  1.00 38.41  ? 755  LEU A CA  1 
ATOM   5733  C  C   . LEU A  1 755 ? 43.929  -12.028 13.635  1.00 39.47  ? 755  LEU A C   1 
ATOM   5734  O  O   . LEU A  1 755 ? 43.867  -12.807 14.588  1.00 48.31  ? 755  LEU A O   1 
ATOM   5735  C  CB  . LEU A  1 755 ? 45.681  -10.264 13.941  1.00 43.39  ? 755  LEU A CB  1 
ATOM   5736  C  CG  . LEU A  1 755 ? 47.167  -9.895  13.845  1.00 48.60  ? 755  LEU A CG  1 
ATOM   5737  C  CD1 . LEU A  1 755 ? 47.502  -8.702  14.726  1.00 45.83  ? 755  LEU A CD1 1 
ATOM   5738  C  CD2 . LEU A  1 755 ? 48.045  -11.083 14.235  1.00 48.85  ? 755  LEU A CD2 1 
ATOM   5739  N  N   . LYS A  1 756 ? 42.851  -11.621 12.981  1.00 43.46  ? 756  LYS A N   1 
ATOM   5740  C  CA  . LYS A  1 756 ? 41.548  -12.171 13.349  1.00 46.81  ? 756  LYS A CA  1 
ATOM   5741  C  C   . LYS A  1 756 ? 41.562  -13.661 13.016  1.00 44.37  ? 756  LYS A C   1 
ATOM   5742  O  O   . LYS A  1 756 ? 41.169  -14.499 13.821  1.00 46.67  ? 756  LYS A O   1 
ATOM   5743  C  CB  . LYS A  1 756 ? 40.404  -11.458 12.623  1.00 37.37  ? 756  LYS A CB  1 
ATOM   5744  C  CG  . LYS A  1 756 ? 39.045  -11.811 13.167  1.00 44.84  ? 756  LYS A CG  1 
ATOM   5745  C  CD  . LYS A  1 756 ? 37.931  -11.272 12.297  1.00 51.79  ? 756  LYS A CD  1 
ATOM   5746  C  CE  . LYS A  1 756 ? 36.672  -12.083 12.529  1.00 63.12  ? 756  LYS A CE  1 
ATOM   5747  N  NZ  . LYS A  1 756 ? 36.794  -13.476 11.983  1.00 62.02  ? 756  LYS A NZ  1 
ATOM   5748  N  N   . LEU A  1 757 ? 42.068  -13.958 11.825  1.00 42.28  ? 757  LEU A N   1 
ATOM   5749  C  CA  . LEU A  1 757 ? 42.172  -15.302 11.302  1.00 41.67  ? 757  LEU A CA  1 
ATOM   5750  C  C   . LEU A  1 757 ? 43.020  -16.162 12.206  1.00 42.98  ? 757  LEU A C   1 
ATOM   5751  O  O   . LEU A  1 757 ? 42.598  -17.248 12.596  1.00 46.33  ? 757  LEU A O   1 
ATOM   5752  C  CB  . LEU A  1 757 ? 42.755  -15.274 9.886   1.00 47.06  ? 757  LEU A CB  1 
ATOM   5753  C  CG  . LEU A  1 757 ? 43.045  -16.619 9.195   1.00 44.48  ? 757  LEU A CG  1 
ATOM   5754  C  CD1 . LEU A  1 757 ? 41.808  -17.475 9.109   1.00 41.38  ? 757  LEU A CD1 1 
ATOM   5755  C  CD2 . LEU A  1 757 ? 43.605  -16.385 7.810   1.00 46.32  ? 757  LEU A CD2 1 
ATOM   5756  N  N   . ALA A  1 758 ? 44.208  -15.681 12.553  1.00 40.03  ? 758  ALA A N   1 
ATOM   5757  C  CA  . ALA A  1 758 ? 45.069  -16.455 13.440  1.00 43.49  ? 758  ALA A CA  1 
ATOM   5758  C  C   . ALA A  1 758 ? 44.401  -16.708 14.789  1.00 47.64  ? 758  ALA A C   1 
ATOM   5759  O  O   . ALA A  1 758 ? 44.545  -17.782 15.361  1.00 54.59  ? 758  ALA A O   1 
ATOM   5760  C  CB  . ALA A  1 758 ? 46.399  -15.769 13.635  1.00 42.11  ? 758  ALA A CB  1 
ATOM   5761  N  N   . CYS A  1 759 ? 43.658  -15.731 15.296  1.00 51.18  ? 759  CYS A N   1 
ATOM   5762  C  CA  . CYS A  1 759 ? 43.003  -15.897 16.589  1.00 49.73  ? 759  CYS A CA  1 
ATOM   5763  C  C   . CYS A  1 759 ? 41.785  -16.789 16.478  1.00 47.70  ? 759  CYS A C   1 
ATOM   5764  O  O   . CYS A  1 759 ? 41.403  -17.456 17.431  1.00 53.05  ? 759  CYS A O   1 
ATOM   5765  C  CB  . CYS A  1 759 ? 42.612  -14.544 17.175  1.00 47.14  ? 759  CYS A CB  1 
ATOM   5766  S  SG  . CYS A  1 759 ? 43.944  -13.816 18.144  1.00 51.14  ? 759  CYS A SG  1 
ATOM   5767  N  N   . ASP A  1 760 ? 41.169  -16.800 15.310  1.00 47.76  ? 760  ASP A N   1 
ATOM   5768  C  CA  . ASP A  1 760 ? 40.037  -17.680 15.094  1.00 53.31  ? 760  ASP A CA  1 
ATOM   5769  C  C   . ASP A  1 760 ? 40.473  -19.147 15.043  1.00 53.52  ? 760  ASP A C   1 
ATOM   5770  O  O   . ASP A  1 760 ? 39.759  -20.008 15.524  1.00 54.74  ? 760  ASP A O   1 
ATOM   5771  C  CB  . ASP A  1 760 ? 39.301  -17.287 13.819  1.00 47.45  ? 760  ASP A CB  1 
ATOM   5772  C  CG  . ASP A  1 760 ? 38.497  -16.024 13.986  1.00 51.58  ? 760  ASP A CG  1 
ATOM   5773  O  OD1 . ASP A  1 760 ? 38.142  -15.697 15.140  1.00 64.66  ? 760  ASP A OD1 1 
ATOM   5774  O  OD2 . ASP A  1 760 ? 38.215  -15.354 12.968  1.00 58.77  ? 760  ASP A OD2 1 
ATOM   5775  N  N   . LEU A  1 761 ? 41.649  -19.423 14.481  1.00 48.76  ? 761  LEU A N   1 
ATOM   5776  C  CA  . LEU A  1 761 ? 42.173  -20.787 14.432  1.00 49.41  ? 761  LEU A CA  1 
ATOM   5777  C  C   . LEU A  1 761 ? 42.963  -21.136 15.694  1.00 49.54  ? 761  LEU A C   1 
ATOM   5778  O  O   . LEU A  1 761 ? 43.754  -22.078 15.702  1.00 59.22  ? 761  LEU A O   1 
ATOM   5779  C  CB  . LEU A  1 761 ? 43.053  -20.986 13.188  1.00 47.59  ? 761  LEU A CB  1 
ATOM   5780  C  CG  . LEU A  1 761 ? 42.440  -20.498 11.866  1.00 43.33  ? 761  LEU A CG  1 
ATOM   5781  C  CD1 . LEU A  1 761 ? 43.445  -20.528 10.732  1.00 37.97  ? 761  LEU A CD1 1 
ATOM   5782  C  CD2 . LEU A  1 761 ? 41.198  -21.307 11.508  1.00 37.32  ? 761  LEU A CD2 1 
ATOM   5783  N  N   . ASN A  1 762 ? 42.738  -20.379 16.758  1.00 49.67  ? 762  ASN A N   1 
ATOM   5784  C  CA  . ASN A  1 762 ? 43.350  -20.643 18.068  1.00 53.25  ? 762  ASN A CA  1 
ATOM   5785  C  C   . ASN A  1 762 ? 44.869  -20.730 18.052  1.00 52.79  ? 762  ASN A C   1 
ATOM   5786  O  O   . ASN A  1 762 ? 45.465  -21.392 18.908  1.00 51.82  ? 762  ASN A O   1 
ATOM   5787  C  CB  . ASN A  1 762 ? 42.786  -21.926 18.672  1.00 53.14  ? 762  ASN A CB  1 
ATOM   5788  C  CG  . ASN A  1 762 ? 41.640  -21.660 19.623  1.00 66.16  ? 762  ASN A CG  1 
ATOM   5789  O  OD1 . ASN A  1 762 ? 40.516  -22.124 19.409  1.00 68.78  ? 762  ASN A OD1 1 
ATOM   5790  N  ND2 . ASN A  1 762 ? 41.915  -20.898 20.683  1.00 68.74  ? 762  ASN A ND2 1 
ATOM   5791  N  N   . HIS A  1 763 ? 45.477  -20.070 17.072  1.00 45.98  ? 763  HIS A N   1 
ATOM   5792  C  CA  . HIS A  1 763 ? 46.925  -19.971 16.973  1.00 51.42  ? 763  HIS A CA  1 
ATOM   5793  C  C   . HIS A  1 763 ? 47.493  -19.423 18.272  1.00 54.13  ? 763  HIS A C   1 
ATOM   5794  O  O   . HIS A  1 763 ? 47.259  -18.274 18.629  1.00 59.36  ? 763  HIS A O   1 
ATOM   5795  C  CB  . HIS A  1 763 ? 47.315  -19.081 15.793  1.00 57.00  ? 763  HIS A CB  1 
ATOM   5796  C  CG  . HIS A  1 763 ? 48.789  -18.953 15.590  1.00 58.67  ? 763  HIS A CG  1 
ATOM   5797  N  ND1 . HIS A  1 763 ? 49.617  -20.045 15.443  1.00 56.32  ? 763  HIS A ND1 1 
ATOM   5798  C  CD2 . HIS A  1 763 ? 49.585  -17.861 15.498  1.00 62.91  ? 763  HIS A CD2 1 
ATOM   5799  C  CE1 . HIS A  1 763 ? 50.860  -19.632 15.270  1.00 61.19  ? 763  HIS A CE1 1 
ATOM   5800  N  NE2 . HIS A  1 763 ? 50.868  -18.311 15.299  1.00 70.93  ? 763  HIS A NE2 1 
ATOM   5801  N  N   . ALA A  1 764 ? 48.242  -20.258 18.972  1.00 56.06  ? 764  ALA A N   1 
ATOM   5802  C  CA  . ALA A  1 764 ? 48.630  -19.987 20.354  1.00 61.94  ? 764  ALA A CA  1 
ATOM   5803  C  C   . ALA A  1 764 ? 49.290  -18.634 20.619  1.00 55.10  ? 764  ALA A C   1 
ATOM   5804  O  O   . ALA A  1 764 ? 48.912  -17.960 21.575  1.00 56.12  ? 764  ALA A O   1 
ATOM   5805  C  CB  . ALA A  1 764 ? 49.551  -21.113 20.864  1.00 59.18  ? 764  ALA A CB  1 
ATOM   5806  N  N   . PRO A  1 765 ? 50.292  -18.247 19.812  1.00 52.50  ? 765  PRO A N   1 
ATOM   5807  C  CA  . PRO A  1 765 ? 51.014  -17.028 20.185  1.00 52.66  ? 765  PRO A CA  1 
ATOM   5808  C  C   . PRO A  1 765 ? 50.092  -15.826 20.092  1.00 60.49  ? 765  PRO A C   1 
ATOM   5809  O  O   . PRO A  1 765 ? 50.064  -14.944 20.964  1.00 57.51  ? 765  PRO A O   1 
ATOM   5810  C  CB  . PRO A  1 765 ? 52.132  -16.942 19.142  1.00 56.62  ? 765  PRO A CB  1 
ATOM   5811  C  CG  . PRO A  1 765 ? 52.207  -18.297 18.527  1.00 57.36  ? 765  PRO A CG  1 
ATOM   5812  C  CD  . PRO A  1 765 ? 50.829  -18.840 18.578  1.00 54.15  ? 765  PRO A CD  1 
ATOM   5813  N  N   . CYS A  1 766 ? 49.329  -15.826 19.005  1.00 58.18  ? 766  CYS A N   1 
ATOM   5814  C  CA  . CYS A  1 766 ? 48.264  -14.879 18.771  1.00 50.27  ? 766  CYS A CA  1 
ATOM   5815  C  C   . CYS A  1 766 ? 47.325  -14.770 19.967  1.00 52.29  ? 766  CYS A C   1 
ATOM   5816  O  O   . CYS A  1 766 ? 47.152  -13.692 20.536  1.00 53.50  ? 766  CYS A O   1 
ATOM   5817  C  CB  . CYS A  1 766 ? 47.490  -15.305 17.540  1.00 56.60  ? 766  CYS A CB  1 
ATOM   5818  S  SG  . CYS A  1 766 ? 46.537  -14.021 16.781  1.00 72.41  ? 766  CYS A SG  1 
ATOM   5819  N  N   . ILE A  1 767 ? 46.722  -15.891 20.348  1.00 49.33  ? 767  ILE A N   1 
ATOM   5820  C  CA  . ILE A  1 767 ? 45.785  -15.920 21.471  1.00 49.17  ? 767  ILE A CA  1 
ATOM   5821  C  C   . ILE A  1 767 ? 46.452  -15.418 22.742  1.00 50.91  ? 767  ILE A C   1 
ATOM   5822  O  O   . ILE A  1 767 ? 45.830  -14.755 23.564  1.00 54.37  ? 767  ILE A O   1 
ATOM   5823  C  CB  . ILE A  1 767 ? 45.225  -17.336 21.704  1.00 52.61  ? 767  ILE A CB  1 
ATOM   5824  C  CG1 . ILE A  1 767 ? 44.378  -17.779 20.511  1.00 48.75  ? 767  ILE A CG1 1 
ATOM   5825  C  CG2 . ILE A  1 767 ? 44.386  -17.389 22.959  1.00 44.06  ? 767  ILE A CG2 1 
ATOM   5826  C  CD1 . ILE A  1 767 ? 43.230  -16.857 20.201  1.00 43.54  ? 767  ILE A CD1 1 
ATOM   5827  N  N   . GLN A  1 768 ? 47.734  -15.714 22.881  1.00 57.16  ? 768  GLN A N   1 
ATOM   5828  C  CA  . GLN A  1 768 ? 48.507  -15.255 24.025  1.00 57.79  ? 768  GLN A CA  1 
ATOM   5829  C  C   . GLN A  1 768 ? 48.616  -13.739 24.051  1.00 53.11  ? 768  GLN A C   1 
ATOM   5830  O  O   . GLN A  1 768 ? 48.255  -13.098 25.034  1.00 55.92  ? 768  GLN A O   1 
ATOM   5831  C  CB  . GLN A  1 768 ? 49.898  -15.872 23.993  1.00 62.29  ? 768  GLN A CB  1 
ATOM   5832  C  CG  . GLN A  1 768 ? 50.692  -15.671 25.253  1.00 68.02  ? 768  GLN A CG  1 
ATOM   5833  C  CD  . GLN A  1 768 ? 51.594  -16.851 25.513  1.00 80.91  ? 768  GLN A CD  1 
ATOM   5834  O  OE1 . GLN A  1 768 ? 51.711  -17.748 24.674  1.00 75.07  ? 768  GLN A OE1 1 
ATOM   5835  N  NE2 . GLN A  1 768 ? 52.228  -16.871 26.682  1.00 92.77  ? 768  GLN A NE2 1 
ATOM   5836  N  N   . LYS A  1 769 ? 49.123  -13.178 22.963  1.00 52.35  ? 769  LYS A N   1 
ATOM   5837  C  CA  . LYS A  1 769 ? 49.291  -11.733 22.843  1.00 55.03  ? 769  LYS A CA  1 
ATOM   5838  C  C   . LYS A  1 769 ? 48.009  -10.939 23.131  1.00 51.96  ? 769  LYS A C   1 
ATOM   5839  O  O   . LYS A  1 769 ? 48.044  -9.948  23.865  1.00 52.69  ? 769  LYS A O   1 
ATOM   5840  C  CB  . LYS A  1 769 ? 49.806  -11.393 21.445  1.00 52.05  ? 769  LYS A CB  1 
ATOM   5841  C  CG  . LYS A  1 769 ? 49.980  -9.933  21.194  1.00 50.04  ? 769  LYS A CG  1 
ATOM   5842  C  CD  . LYS A  1 769 ? 50.832  -9.284  22.272  1.00 55.01  ? 769  LYS A CD  1 
ATOM   5843  C  CE  . LYS A  1 769 ? 51.105  -7.809  21.947  1.00 51.62  ? 769  LYS A CE  1 
ATOM   5844  N  NZ  . LYS A  1 769 ? 52.037  -7.191  22.930  1.00 58.88  ? 769  LYS A NZ  1 
ATOM   5845  N  N   . ALA A  1 770 ? 46.889  -11.375 22.555  1.00 49.80  ? 770  ALA A N   1 
ATOM   5846  C  CA  . ALA A  1 770 ? 45.617  -10.693 22.752  1.00 48.52  ? 770  ALA A CA  1 
ATOM   5847  C  C   . ALA A  1 770 ? 45.171  -10.779 24.214  1.00 53.44  ? 770  ALA A C   1 
ATOM   5848  O  O   . ALA A  1 770 ? 44.751  -9.779  24.815  1.00 47.38  ? 770  ALA A O   1 
ATOM   5849  C  CB  . ALA A  1 770 ? 44.571  -11.274 21.849  1.00 45.59  ? 770  ALA A CB  1 
ATOM   5850  N  N   . ALA A  1 771 ? 45.267  -11.983 24.768  1.00 47.92  ? 771  ALA A N   1 
ATOM   5851  C  CA  . ALA A  1 771 ? 45.006  -12.221 26.177  1.00 48.71  ? 771  ALA A CA  1 
ATOM   5852  C  C   . ALA A  1 771 ? 45.817  -11.283 27.048  1.00 50.64  ? 771  ALA A C   1 
ATOM   5853  O  O   . ALA A  1 771 ? 45.297  -10.723 28.007  1.00 46.88  ? 771  ALA A O   1 
ATOM   5854  C  CB  . ALA A  1 771 ? 45.314  -13.655 26.532  1.00 52.05  ? 771  ALA A CB  1 
ATOM   5855  N  N   . GLU A  1 772 ? 47.091  -11.107 26.718  1.00 49.67  ? 772  GLU A N   1 
ATOM   5856  C  CA  . GLU A  1 772 ? 47.922  -10.192 27.483  1.00 55.53  ? 772  GLU A CA  1 
ATOM   5857  C  C   . GLU A  1 772 ? 47.371  -8.770  27.380  1.00 57.03  ? 772  GLU A C   1 
ATOM   5858  O  O   . GLU A  1 772 ? 47.070  -8.146  28.406  1.00 55.56  ? 772  GLU A O   1 
ATOM   5859  C  CB  . GLU A  1 772 ? 49.378  -10.231 27.013  1.00 56.04  ? 772  GLU A CB  1 
ATOM   5860  C  CG  . GLU A  1 772 ? 50.226  -9.078  27.550  1.00 62.60  ? 772  GLU A CG  1 
ATOM   5861  C  CD  . GLU A  1 772 ? 51.464  -8.798  26.696  1.00 77.70  ? 772  GLU A CD  1 
ATOM   5862  O  OE1 . GLU A  1 772 ? 52.307  -9.719  26.553  1.00 84.63  ? 772  GLU A OE1 1 
ATOM   5863  O  OE2 . GLU A  1 772 ? 51.587  -7.661  26.163  1.00 71.97  ? 772  GLU A OE2 1 
ATOM   5864  N  N   . LEU A  1 773 ? 47.238  -8.271  26.147  1.00 53.36  ? 773  LEU A N   1 
ATOM   5865  C  CA  . LEU A  1 773 ? 46.694  -6.934  25.907  1.00 45.42  ? 773  LEU A CA  1 
ATOM   5866  C  C   . LEU A  1 773 ? 45.368  -6.722  26.627  1.00 47.31  ? 773  LEU A C   1 
ATOM   5867  O  O   . LEU A  1 773 ? 45.115  -5.656  27.183  1.00 48.97  ? 773  LEU A O   1 
ATOM   5868  C  CB  . LEU A  1 773 ? 46.504  -6.689  24.421  1.00 47.74  ? 773  LEU A CB  1 
ATOM   5869  C  CG  . LEU A  1 773 ? 47.780  -6.423  23.653  1.00 49.38  ? 773  LEU A CG  1 
ATOM   5870  C  CD1 . LEU A  1 773 ? 47.505  -6.376  22.156  1.00 44.94  ? 773  LEU A CD1 1 
ATOM   5871  C  CD2 . LEU A  1 773 ? 48.314  -5.113  24.143  1.00 45.82  ? 773  LEU A CD2 1 
ATOM   5872  N  N   . PHE A  1 774 ? 44.521  -7.741  26.641  1.00 45.20  ? 774  PHE A N   1 
ATOM   5873  C  CA  . PHE A  1 774 ? 43.241  -7.564  27.285  1.00 45.39  ? 774  PHE A CA  1 
ATOM   5874  C  C   . PHE A  1 774 ? 43.426  -7.393  28.774  1.00 49.68  ? 774  PHE A C   1 
ATOM   5875  O  O   . PHE A  1 774 ? 42.814  -6.526  29.385  1.00 48.28  ? 774  PHE A O   1 
ATOM   5876  C  CB  . PHE A  1 774 ? 42.313  -8.727  27.011  1.00 39.14  ? 774  PHE A CB  1 
ATOM   5877  C  CG  . PHE A  1 774 ? 40.957  -8.551  27.625  1.00 44.81  ? 774  PHE A CG  1 
ATOM   5878  C  CD1 . PHE A  1 774 ? 40.027  -7.692  27.042  1.00 42.29  ? 774  PHE A CD1 1 
ATOM   5879  C  CD2 . PHE A  1 774 ? 40.608  -9.230  28.781  1.00 33.97  ? 774  PHE A CD2 1 
ATOM   5880  C  CE1 . PHE A  1 774 ? 38.759  -7.514  27.603  1.00 45.72  ? 774  PHE A CE1 1 
ATOM   5881  C  CE2 . PHE A  1 774 ? 39.348  -9.062  29.341  1.00 42.71  ? 774  PHE A CE2 1 
ATOM   5882  C  CZ  . PHE A  1 774 ? 38.420  -8.196  28.758  1.00 43.98  ? 774  PHE A CZ  1 
ATOM   5883  N  N   . SER A  1 775 ? 44.284  -8.234  29.340  1.00 56.39  ? 775  SER A N   1 
ATOM   5884  C  CA  . SER A  1 775 ? 44.579  -8.206  30.762  1.00 56.37  ? 775  SER A CA  1 
ATOM   5885  C  C   . SER A  1 775 ? 45.117  -6.842  31.181  1.00 57.26  ? 775  SER A C   1 
ATOM   5886  O  O   . SER A  1 775 ? 44.588  -6.234  32.105  1.00 60.64  ? 775  SER A O   1 
ATOM   5887  C  CB  . SER A  1 775 ? 45.581  -9.309  31.131  1.00 56.26  ? 775  SER A CB  1 
ATOM   5888  O  OG  . SER A  1 775 ? 45.865  -9.280  32.523  1.00 66.45  ? 775  SER A OG  1 
ATOM   5889  N  N   . GLN A  1 776 ? 46.158  -6.362  30.502  1.00 51.37  ? 776  GLN A N   1 
ATOM   5890  C  CA  . GLN A  1 776 ? 46.694  -5.030  30.792  1.00 56.68  ? 776  GLN A CA  1 
ATOM   5891  C  C   . GLN A  1 776 ? 45.612  -3.955  30.737  1.00 62.07  ? 776  GLN A C   1 
ATOM   5892  O  O   . GLN A  1 776 ? 45.570  -3.041  31.572  1.00 64.08  ? 776  GLN A O   1 
ATOM   5893  C  CB  . GLN A  1 776 ? 47.813  -4.667  29.818  1.00 55.12  ? 776  GLN A CB  1 
ATOM   5894  C  CG  . GLN A  1 776 ? 49.076  -5.475  29.985  1.00 60.70  ? 776  GLN A CG  1 
ATOM   5895  C  CD  . GLN A  1 776 ? 50.076  -5.180  28.893  1.00 67.86  ? 776  GLN A CD  1 
ATOM   5896  O  OE1 . GLN A  1 776 ? 49.863  -4.282  28.079  1.00 62.84  ? 776  GLN A OE1 1 
ATOM   5897  N  NE2 . GLN A  1 776 ? 51.170  -5.939  28.859  1.00 70.89  ? 776  GLN A NE2 1 
ATOM   5898  N  N   . TRP A  1 777 ? 44.737  -4.067  29.744  1.00 60.81  ? 777  TRP A N   1 
ATOM   5899  C  CA  . TRP A  1 777 ? 43.681  -3.093  29.577  1.00 52.80  ? 777  TRP A CA  1 
ATOM   5900  C  C   . TRP A  1 777 ? 42.742  -3.147  30.780  1.00 57.80  ? 777  TRP A C   1 
ATOM   5901  O  O   . TRP A  1 777 ? 42.515  -2.131  31.447  1.00 59.14  ? 777  TRP A O   1 
ATOM   5902  C  CB  . TRP A  1 777 ? 42.925  -3.342  28.273  1.00 48.92  ? 777  TRP A CB  1 
ATOM   5903  C  CG  . TRP A  1 777 ? 41.735  -2.468  28.104  1.00 48.41  ? 777  TRP A CG  1 
ATOM   5904  C  CD1 . TRP A  1 777 ? 41.726  -1.124  27.832  1.00 48.67  ? 777  TRP A CD1 1 
ATOM   5905  C  CD2 . TRP A  1 777 ? 40.368  -2.869  28.198  1.00 44.28  ? 777  TRP A CD2 1 
ATOM   5906  N  NE1 . TRP A  1 777 ? 40.433  -0.665  27.762  1.00 42.40  ? 777  TRP A NE1 1 
ATOM   5907  C  CE2 . TRP A  1 777 ? 39.578  -1.714  27.984  1.00 42.91  ? 777  TRP A CE2 1 
ATOM   5908  C  CE3 . TRP A  1 777 ? 39.732  -4.088  28.446  1.00 41.36  ? 777  TRP A CE3 1 
ATOM   5909  C  CZ2 . TRP A  1 777 ? 38.186  -1.748  28.003  1.00 36.99  ? 777  TRP A CZ2 1 
ATOM   5910  C  CZ3 . TRP A  1 777 ? 38.338  -4.115  28.489  1.00 45.38  ? 777  TRP A CZ3 1 
ATOM   5911  C  CH2 . TRP A  1 777 ? 37.584  -2.951  28.263  1.00 42.13  ? 777  TRP A CH2 1 
ATOM   5912  N  N   . MET A  1 778 ? 42.218  -4.335  31.072  1.00 49.19  ? 778  MET A N   1 
ATOM   5913  C  CA  . MET A  1 778 ? 41.214  -4.469  32.121  1.00 56.66  ? 778  MET A CA  1 
ATOM   5914  C  C   . MET A  1 778 ? 41.815  -4.121  33.491  1.00 64.19  ? 778  MET A C   1 
ATOM   5915  O  O   . MET A  1 778 ? 41.161  -3.496  34.329  1.00 58.25  ? 778  MET A O   1 
ATOM   5916  C  CB  . MET A  1 778 ? 40.610  -5.881  32.133  1.00 48.06  ? 778  MET A CB  1 
ATOM   5917  C  CG  . MET A  1 778 ? 39.492  -6.028  33.153  1.00 56.64  ? 778  MET A CG  1 
ATOM   5918  S  SD  . MET A  1 778 ? 38.649  -7.628  33.163  1.00 59.54  ? 778  MET A SD  1 
ATOM   5919  C  CE  . MET A  1 778 ? 40.025  -8.751  32.846  1.00 49.86  ? 778  MET A CE  1 
ATOM   5920  N  N   . GLU A  1 779 ? 43.068  -4.502  33.706  1.00 61.46  ? 779  GLU A N   1 
ATOM   5921  C  CA  . GLU A  1 779 ? 43.717  -4.187  34.965  1.00 67.19  ? 779  GLU A CA  1 
ATOM   5922  C  C   . GLU A  1 779 ? 44.002  -2.694  35.084  1.00 66.93  ? 779  GLU A C   1 
ATOM   5923  O  O   . GLU A  1 779 ? 43.971  -2.143  36.181  1.00 72.75  ? 779  GLU A O   1 
ATOM   5924  C  CB  . GLU A  1 779 ? 45.012  -4.984  35.134  1.00 65.44  ? 779  GLU A CB  1 
ATOM   5925  C  CG  . GLU A  1 779 ? 44.819  -6.481  35.200  1.00 59.36  ? 779  GLU A CG  1 
ATOM   5926  C  CD  . GLU A  1 779 ? 43.656  -6.894  36.097  1.00 80.81  ? 779  GLU A CD  1 
ATOM   5927  O  OE1 . GLU A  1 779 ? 43.507  -6.329  37.211  1.00 81.48  ? 779  GLU A OE1 1 
ATOM   5928  O  OE2 . GLU A  1 779 ? 42.890  -7.799  35.682  1.00 84.14  ? 779  GLU A OE2 1 
ATOM   5929  N  N   . SER A  1 780 ? 44.265  -2.031  33.965  1.00 67.43  ? 780  SER A N   1 
ATOM   5930  C  CA  . SER A  1 780 ? 44.577  -0.607  34.021  1.00 66.24  ? 780  SER A CA  1 
ATOM   5931  C  C   . SER A  1 780 ? 43.312  0.230   34.025  1.00 66.43  ? 780  SER A C   1 
ATOM   5932  O  O   . SER A  1 780 ? 43.379  1.450   33.937  1.00 70.74  ? 780  SER A O   1 
ATOM   5933  C  CB  . SER A  1 780 ? 45.460  -0.200  32.851  1.00 69.58  ? 780  SER A CB  1 
ATOM   5934  O  OG  . SER A  1 780 ? 44.700  -0.061  31.662  1.00 76.12  ? 780  SER A OG  1 
ATOM   5935  N  N   . SER A  1 781 ? 42.168  -0.441  34.140  1.00 68.41  ? 781  SER A N   1 
ATOM   5936  C  CA  . SER A  1 781 ? 40.856  0.190   34.024  1.00 70.34  ? 781  SER A CA  1 
ATOM   5937  C  C   . SER A  1 781 ? 40.822  1.156   32.839  1.00 77.15  ? 781  SER A C   1 
ATOM   5938  O  O   . SER A  1 781 ? 40.663  2.375   33.013  1.00 74.38  ? 781  SER A O   1 
ATOM   5939  C  CB  . SER A  1 781 ? 40.490  0.923   35.311  1.00 74.01  ? 781  SER A CB  1 
ATOM   5940  O  OG  . SER A  1 781 ? 41.145  2.177   35.358  1.00 79.71  ? 781  SER A OG  1 
ATOM   5941  N  N   . GLY A  1 782 ? 41.015  0.603   31.642  1.00 72.43  ? 782  GLY A N   1 
ATOM   5942  C  CA  . GLY A  1 782 ? 40.915  1.361   30.406  1.00 74.53  ? 782  GLY A CA  1 
ATOM   5943  C  C   . GLY A  1 782 ? 41.979  2.418   30.160  1.00 76.23  ? 782  GLY A C   1 
ATOM   5944  O  O   . GLY A  1 782 ? 42.010  3.028   29.091  1.00 76.30  ? 782  GLY A O   1 
ATOM   5945  N  N   . LYS A  1 783 ? 42.861  2.634   31.130  1.00 79.40  ? 783  LYS A N   1 
ATOM   5946  C  CA  . LYS A  1 783 ? 43.825  3.728   31.033  1.00 79.53  ? 783  LYS A CA  1 
ATOM   5947  C  C   . LYS A  1 783 ? 44.987  3.390   30.102  1.00 78.97  ? 783  LYS A C   1 
ATOM   5948  O  O   . LYS A  1 783 ? 45.803  4.249   29.780  1.00 83.27  ? 783  LYS A O   1 
ATOM   5949  C  CB  . LYS A  1 783 ? 44.340  4.117   32.425  1.00 75.23  ? 783  LYS A CB  1 
ATOM   5950  C  CG  . LYS A  1 783 ? 43.270  4.782   33.302  1.00 73.76  ? 783  LYS A CG  1 
ATOM   5951  C  CD  . LYS A  1 783 ? 42.383  5.702   32.454  1.00 77.60  ? 783  LYS A CD  1 
ATOM   5952  C  CE  . LYS A  1 783 ? 41.457  6.567   33.296  1.00 83.83  ? 783  LYS A CE  1 
ATOM   5953  N  NZ  . LYS A  1 783 ? 40.873  7.703   32.510  1.00 72.16  ? 783  LYS A NZ  1 
ATOM   5954  N  N   . LEU A  1 784 ? 45.058  2.138   29.669  1.00 76.09  ? 784  LEU A N   1 
ATOM   5955  C  CA  . LEU A  1 784 ? 45.950  1.771   28.580  1.00 82.28  ? 784  LEU A CA  1 
ATOM   5956  C  C   . LEU A  1 784 ? 45.147  1.771   27.282  1.00 81.22  ? 784  LEU A C   1 
ATOM   5957  O  O   . LEU A  1 784 ? 43.916  1.747   27.312  1.00 77.10  ? 784  LEU A O   1 
ATOM   5958  C  CB  . LEU A  1 784 ? 46.593  0.407   28.828  1.00 78.97  ? 784  LEU A CB  1 
ATOM   5959  C  CG  . LEU A  1 784 ? 47.457  0.376   30.088  1.00 78.76  ? 784  LEU A CG  1 
ATOM   5960  C  CD1 . LEU A  1 784 ? 48.069  -0.994  30.302  1.00 77.49  ? 784  LEU A CD1 1 
ATOM   5961  C  CD2 . LEU A  1 784 ? 48.532  1.435   30.013  1.00 82.57  ? 784  LEU A CD2 1 
ATOM   5962  N  N   . ASN A  1 785 ? 45.838  1.820   26.148  1.00 79.86  ? 785  ASN A N   1 
ATOM   5963  C  CA  . ASN A  1 785 ? 45.161  1.886   24.858  1.00 70.65  ? 785  ASN A CA  1 
ATOM   5964  C  C   . ASN A  1 785 ? 45.401  0.630   24.050  1.00 66.96  ? 785  ASN A C   1 
ATOM   5965  O  O   . ASN A  1 785 ? 46.544  0.237   23.807  1.00 65.42  ? 785  ASN A O   1 
ATOM   5966  C  CB  . ASN A  1 785 ? 45.632  3.098   24.045  1.00 76.97  ? 785  ASN A CB  1 
ATOM   5967  C  CG  . ASN A  1 785 ? 45.453  4.414   24.787  1.00 87.89  ? 785  ASN A CG  1 
ATOM   5968  O  OD1 . ASN A  1 785 ? 44.479  5.141   24.567  1.00 85.28  ? 785  ASN A OD1 1 
ATOM   5969  N  ND2 . ASN A  1 785 ? 46.401  4.730   25.666  1.00 90.61  ? 785  ASN A ND2 1 
ATOM   5970  N  N   . ILE A  1 786 ? 44.332  -0.018  23.629  1.00 55.31  ? 786  ILE A N   1 
ATOM   5971  C  CA  . ILE A  1 786 ? 44.519  -1.073  22.664  1.00 49.03  ? 786  ILE A CA  1 
ATOM   5972  C  C   . ILE A  1 786 ? 44.531  -0.408  21.307  1.00 45.41  ? 786  ILE A C   1 
ATOM   5973  O  O   . ILE A  1 786 ? 43.643  0.378   21.013  1.00 52.12  ? 786  ILE A O   1 
ATOM   5974  C  CB  . ILE A  1 786 ? 43.424  -2.120  22.753  1.00 41.63  ? 786  ILE A CB  1 
ATOM   5975  C  CG1 . ILE A  1 786 ? 43.378  -2.675  24.175  1.00 42.38  ? 786  ILE A CG1 1 
ATOM   5976  C  CG2 . ILE A  1 786 ? 43.687  -3.197  21.752  1.00 36.49  ? 786  ILE A CG2 1 
ATOM   5977  C  CD1 . ILE A  1 786 ? 42.041  -3.251  24.592  1.00 42.01  ? 786  ILE A CD1 1 
ATOM   5978  N  N   . PRO A  1 787 ? 45.546  -0.696  20.479  1.00 45.51  ? 787  PRO A N   1 
ATOM   5979  C  CA  . PRO A  1 787 ? 45.532  -0.198  19.090  1.00 35.01  ? 787  PRO A CA  1 
ATOM   5980  C  C   . PRO A  1 787 ? 44.220  -0.595  18.391  1.00 45.50  ? 787  PRO A C   1 
ATOM   5981  O  O   . PRO A  1 787 ? 43.720  -1.704  18.622  1.00 45.48  ? 787  PRO A O   1 
ATOM   5982  C  CB  . PRO A  1 787 ? 46.733  -0.891  18.445  1.00 37.30  ? 787  PRO A CB  1 
ATOM   5983  C  CG  . PRO A  1 787 ? 47.584  -1.365  19.596  1.00 37.30  ? 787  PRO A CG  1 
ATOM   5984  C  CD  . PRO A  1 787 ? 46.653  -1.637  20.737  1.00 38.63  ? 787  PRO A CD  1 
ATOM   5985  N  N   . THR A  1 788 ? 43.667  0.281   17.557  1.00 44.86  ? 788  THR A N   1 
ATOM   5986  C  CA  . THR A  1 788 ? 42.279  0.120   17.127  1.00 41.46  ? 788  THR A CA  1 
ATOM   5987  C  C   . THR A  1 788 ? 42.091  -1.048  16.191  1.00 40.09  ? 788  THR A C   1 
ATOM   5988  O  O   . THR A  1 788 ? 41.037  -1.676  16.180  1.00 41.91  ? 788  THR A O   1 
ATOM   5989  C  CB  . THR A  1 788 ? 41.728  1.395   16.438  1.00 42.14  ? 788  THR A CB  1 
ATOM   5990  O  OG1 . THR A  1 788 ? 42.507  1.721   15.269  1.00 36.34  ? 788  THR A OG1 1 
ATOM   5991  C  CG2 . THR A  1 788 ? 41.722  2.551   17.431  1.00 34.32  ? 788  THR A CG2 1 
ATOM   5992  N  N   . ASP A  1 789 ? 43.123  -1.359  15.432  1.00 35.54  ? 789  ASP A N   1 
ATOM   5993  C  CA  . ASP A  1 789 ? 43.033  -2.400  14.431  1.00 40.61  ? 789  ASP A CA  1 
ATOM   5994  C  C   . ASP A  1 789 ? 42.925  -3.782  15.044  1.00 42.55  ? 789  ASP A C   1 
ATOM   5995  O  O   . ASP A  1 789 ? 42.790  -4.773  14.345  1.00 43.23  ? 789  ASP A O   1 
ATOM   5996  C  CB  . ASP A  1 789 ? 44.252  -2.360  13.518  1.00 42.53  ? 789  ASP A CB  1 
ATOM   5997  C  CG  . ASP A  1 789 ? 44.388  -1.047  12.790  1.00 48.73  ? 789  ASP A CG  1 
ATOM   5998  O  OD1 . ASP A  1 789 ? 43.368  -0.341  12.634  1.00 48.87  ? 789  ASP A OD1 1 
ATOM   5999  O  OD2 . ASP A  1 789 ? 45.519  -0.720  12.377  1.00 53.09  ? 789  ASP A OD2 1 
ATOM   6000  N  N   . VAL A  1 790 ? 42.966  -3.839  16.358  1.00 36.84  ? 790  VAL A N   1 
ATOM   6001  C  CA  . VAL A  1 790 ? 43.283  -5.071  17.039  1.00 37.47  ? 790  VAL A CA  1 
ATOM   6002  C  C   . VAL A  1 790 ? 42.300  -5.170  18.193  1.00 37.89  ? 790  VAL A C   1 
ATOM   6003  O  O   . VAL A  1 790 ? 42.125  -6.204  18.840  1.00 43.60  ? 790  VAL A O   1 
ATOM   6004  C  CB  . VAL A  1 790 ? 44.779  -5.030  17.453  1.00 47.75  ? 790  VAL A CB  1 
ATOM   6005  C  CG1 . VAL A  1 790 ? 45.009  -5.386  18.906  1.00 43.47  ? 790  VAL A CG1 1 
ATOM   6006  C  CG2 . VAL A  1 790 ? 45.636  -5.814  16.468  1.00 37.65  ? 790  VAL A CG2 1 
ATOM   6007  N  N   . LEU A  1 791 ? 41.602  -4.060  18.380  1.00 36.84  ? 791  LEU A N   1 
ATOM   6008  C  CA  . LEU A  1 791 ? 40.607  -3.907  19.414  1.00 36.33  ? 791  LEU A CA  1 
ATOM   6009  C  C   . LEU A  1 791 ? 39.583  -5.032  19.466  1.00 38.07  ? 791  LEU A C   1 
ATOM   6010  O  O   . LEU A  1 791 ? 39.373  -5.640  20.508  1.00 44.66  ? 791  LEU A O   1 
ATOM   6011  C  CB  . LEU A  1 791 ? 39.908  -2.571  19.212  1.00 37.26  ? 791  LEU A CB  1 
ATOM   6012  C  CG  . LEU A  1 791 ? 39.155  -1.953  20.375  1.00 33.55  ? 791  LEU A CG  1 
ATOM   6013  C  CD1 . LEU A  1 791 ? 39.879  -2.170  21.659  1.00 34.15  ? 791  LEU A CD1 1 
ATOM   6014  C  CD2 . LEU A  1 791 ? 39.040  -0.482  20.090  1.00 36.07  ? 791  LEU A CD2 1 
ATOM   6015  N  N   . LYS A  1 792 ? 38.922  -5.296  18.353  1.00 36.83  ? 792  LYS A N   1 
ATOM   6016  C  CA  . LYS A  1 792 ? 37.896  -6.328  18.332  1.00 39.19  ? 792  LYS A CA  1 
ATOM   6017  C  C   . LYS A  1 792 ? 38.485  -7.714  18.680  1.00 41.86  ? 792  LYS A C   1 
ATOM   6018  O  O   . LYS A  1 792 ? 37.884  -8.510  19.409  1.00 35.15  ? 792  LYS A O   1 
ATOM   6019  C  CB  . LYS A  1 792 ? 37.218  -6.346  16.964  1.00 43.87  ? 792  LYS A CB  1 
ATOM   6020  C  CG  . LYS A  1 792 ? 35.904  -7.056  16.977  1.00 42.30  ? 792  LYS A CG  1 
ATOM   6021  C  CD  . LYS A  1 792 ? 34.988  -6.579  15.876  1.00 43.73  ? 792  LYS A CD  1 
ATOM   6022  C  CE  . LYS A  1 792 ? 35.349  -7.189  14.541  1.00 55.76  ? 792  LYS A CE  1 
ATOM   6023  N  NZ  . LYS A  1 792 ? 34.628  -6.516  13.424  1.00 64.45  ? 792  LYS A NZ  1 
ATOM   6024  N  N   . ILE A  1 793 ? 39.682  -7.991  18.182  1.00 40.40  ? 793  ILE A N   1 
ATOM   6025  C  CA  . ILE A  1 793 ? 40.298  -9.273  18.471  1.00 35.58  ? 793  ILE A CA  1 
ATOM   6026  C  C   . ILE A  1 793 ? 40.634  -9.373  19.945  1.00 41.23  ? 793  ILE A C   1 
ATOM   6027  O  O   . ILE A  1 793 ? 40.338  -10.393 20.592  1.00 41.16  ? 793  ILE A O   1 
ATOM   6028  C  CB  . ILE A  1 793 ? 41.556  -9.513  17.637  1.00 34.49  ? 793  ILE A CB  1 
ATOM   6029  C  CG1 . ILE A  1 793 ? 41.205  -9.505  16.152  1.00 29.41  ? 793  ILE A CG1 1 
ATOM   6030  C  CG2 . ILE A  1 793 ? 42.146  -10.869 17.983  1.00 36.21  ? 793  ILE A CG2 1 
ATOM   6031  C  CD1 . ILE A  1 793 ? 42.369  -9.183  15.279  1.00 31.41  ? 793  ILE A CD1 1 
ATOM   6032  N  N   . VAL A  1 794 ? 41.227  -8.313  20.487  1.00 36.56  ? 794  VAL A N   1 
ATOM   6033  C  CA  . VAL A  1 794 ? 41.582  -8.320  21.900  1.00 36.70  ? 794  VAL A CA  1 
ATOM   6034  C  C   . VAL A  1 794 ? 40.336  -8.486  22.766  1.00 37.88  ? 794  VAL A C   1 
ATOM   6035  O  O   . VAL A  1 794 ? 40.332  -9.303  23.690  1.00 40.01  ? 794  VAL A O   1 
ATOM   6036  C  CB  . VAL A  1 794 ? 42.342  -7.043  22.304  1.00 41.98  ? 794  VAL A CB  1 
ATOM   6037  C  CG1 . VAL A  1 794 ? 42.520  -6.965  23.805  1.00 35.75  ? 794  VAL A CG1 1 
ATOM   6038  C  CG2 . VAL A  1 794 ? 43.701  -7.007  21.617  1.00 40.80  ? 794  VAL A CG2 1 
ATOM   6039  N  N   . TYR A  1 795 ? 39.268  -7.757  22.460  1.00 35.90  ? 795  TYR A N   1 
ATOM   6040  C  CA  . TYR A  1 795 ? 38.047  -7.874  23.266  1.00 37.82  ? 795  TYR A CA  1 
ATOM   6041  C  C   . TYR A  1 795 ? 37.461  -9.261  23.209  1.00 38.42  ? 795  TYR A C   1 
ATOM   6042  O  O   . TYR A  1 795 ? 37.029  -9.785  24.239  1.00 42.67  ? 795  TYR A O   1 
ATOM   6043  C  CB  . TYR A  1 795 ? 36.969  -6.875  22.831  1.00 39.19  ? 795  TYR A CB  1 
ATOM   6044  C  CG  . TYR A  1 795 ? 37.197  -5.471  23.307  1.00 41.97  ? 795  TYR A CG  1 
ATOM   6045  C  CD1 . TYR A  1 795 ? 38.061  -5.197  24.363  1.00 42.07  ? 795  TYR A CD1 1 
ATOM   6046  C  CD2 . TYR A  1 795 ? 36.550  -4.410  22.700  1.00 42.85  ? 795  TYR A CD2 1 
ATOM   6047  C  CE1 . TYR A  1 795 ? 38.265  -3.904  24.794  1.00 39.47  ? 795  TYR A CE1 1 
ATOM   6048  C  CE2 . TYR A  1 795 ? 36.743  -3.127  23.125  1.00 38.70  ? 795  TYR A CE2 1 
ATOM   6049  C  CZ  . TYR A  1 795 ? 37.600  -2.875  24.166  1.00 38.64  ? 795  TYR A CZ  1 
ATOM   6050  O  OH  . TYR A  1 795 ? 37.789  -1.576  24.558  1.00 42.23  ? 795  TYR A OH  1 
ATOM   6051  N  N   . SER A  1 796 ? 37.425  -9.862  22.021  1.00 34.57  ? 796  SER A N   1 
ATOM   6052  C  CA  . SER A  1 796 ? 36.807  -11.178 21.923  1.00 39.25  ? 796  SER A CA  1 
ATOM   6053  C  C   . SER A  1 796 ? 37.644  -12.225 22.650  1.00 39.15  ? 796  SER A C   1 
ATOM   6054  O  O   . SER A  1 796 ? 37.079  -13.091 23.321  1.00 41.07  ? 796  SER A O   1 
ATOM   6055  C  CB  . SER A  1 796 ? 36.538  -11.594 20.470  1.00 37.93  ? 796  SER A CB  1 
ATOM   6056  O  OG  . SER A  1 796 ? 37.586  -11.287 19.586  1.00 44.63  ? 796  SER A OG  1 
ATOM   6057  N  N   . VAL A  1 797 ? 38.969  -12.146 22.576  1.00 37.48  ? 797  VAL A N   1 
ATOM   6058  C  CA  . VAL A  1 797 ? 39.757  -13.092 23.367  1.00 39.78  ? 797  VAL A CA  1 
ATOM   6059  C  C   . VAL A  1 797 ? 39.459  -12.832 24.837  1.00 44.71  ? 797  VAL A C   1 
ATOM   6060  O  O   . VAL A  1 797 ? 39.255  -13.756 25.631  1.00 42.95  ? 797  VAL A O   1 
ATOM   6061  C  CB  . VAL A  1 797 ? 41.260  -12.977 23.118  1.00 45.99  ? 797  VAL A CB  1 
ATOM   6062  C  CG1 . VAL A  1 797 ? 42.008  -13.889 24.080  1.00 44.11  ? 797  VAL A CG1 1 
ATOM   6063  C  CG2 . VAL A  1 797 ? 41.591  -13.341 21.677  1.00 43.59  ? 797  VAL A CG2 1 
ATOM   6064  N  N   . GLY A  1 798 ? 39.375  -11.555 25.185  1.00 37.39  ? 798  GLY A N   1 
ATOM   6065  C  CA  . GLY A  1 798 ? 39.052  -11.182 26.543  1.00 36.65  ? 798  GLY A CA  1 
ATOM   6066  C  C   . GLY A  1 798 ? 37.728  -11.717 27.028  1.00 39.05  ? 798  GLY A C   1 
ATOM   6067  O  O   . GLY A  1 798 ? 37.532  -11.895 28.223  1.00 42.79  ? 798  GLY A O   1 
ATOM   6068  N  N   . ALA A  1 799 ? 36.818  -11.973 26.095  1.00 43.05  ? 799  ALA A N   1 
ATOM   6069  C  CA  . ALA A  1 799 ? 35.442  -12.335 26.431  1.00 42.24  ? 799  ALA A CA  1 
ATOM   6070  C  C   . ALA A  1 799 ? 35.292  -13.839 26.658  1.00 43.31  ? 799  ALA A C   1 
ATOM   6071  O  O   . ALA A  1 799 ? 34.194  -14.332 26.926  1.00 42.44  ? 799  ALA A O   1 
ATOM   6072  C  CB  . ALA A  1 799 ? 34.490  -11.871 25.318  1.00 40.16  ? 799  ALA A CB  1 
ATOM   6073  N  N   . GLN A  1 800 ? 36.391  -14.572 26.525  1.00 42.79  ? 800  GLN A N   1 
ATOM   6074  C  CA  . GLN A  1 800 ? 36.338  -16.016 26.679  1.00 44.85  ? 800  GLN A CA  1 
ATOM   6075  C  C   . GLN A  1 800 ? 36.288  -16.424 28.141  1.00 48.26  ? 800  GLN A C   1 
ATOM   6076  O  O   . GLN A  1 800 ? 36.073  -17.599 28.437  1.00 55.12  ? 800  GLN A O   1 
ATOM   6077  C  CB  . GLN A  1 800 ? 37.524  -16.674 25.987  1.00 37.82  ? 800  GLN A CB  1 
ATOM   6078  C  CG  . GLN A  1 800 ? 37.531  -16.464 24.472  1.00 38.45  ? 800  GLN A CG  1 
ATOM   6079  C  CD  . GLN A  1 800 ? 36.152  -16.694 23.838  1.00 47.35  ? 800  GLN A CD  1 
ATOM   6080  O  OE1 . GLN A  1 800 ? 35.342  -15.767 23.734  1.00 49.45  ? 800  GLN A OE1 1 
ATOM   6081  N  NE2 . GLN A  1 800 ? 35.886  -17.929 23.408  1.00 43.42  ? 800  GLN A NE2 1 
ATOM   6082  N  N   . THR A  1 801 ? 36.463  -15.467 29.055  1.00 39.94  ? 801  THR A N   1 
ATOM   6083  C  CA  . THR A  1 801 ? 36.225  -15.751 30.481  1.00 47.99  ? 801  THR A CA  1 
ATOM   6084  C  C   . THR A  1 801 ? 35.098  -14.928 31.051  1.00 48.88  ? 801  THR A C   1 
ATOM   6085  O  O   . THR A  1 801 ? 34.901  -13.763 30.681  1.00 52.58  ? 801  THR A O   1 
ATOM   6086  C  CB  . THR A  1 801 ? 37.445  -15.477 31.383  1.00 46.04  ? 801  THR A CB  1 
ATOM   6087  O  OG1 . THR A  1 801 ? 37.574  -14.061 31.593  1.00 49.28  ? 801  THR A OG1 1 
ATOM   6088  C  CG2 . THR A  1 801 ? 38.720  -16.059 30.790  1.00 41.10  ? 801  THR A CG2 1 
ATOM   6089  N  N   . THR A  1 802 ? 34.387  -15.529 31.988  1.00 48.08  ? 802  THR A N   1 
ATOM   6090  C  CA  . THR A  1 802 ? 33.263  -14.873 32.631  1.00 49.73  ? 802  THR A CA  1 
ATOM   6091  C  C   . THR A  1 802 ? 33.656  -13.517 33.216  1.00 45.59  ? 802  THR A C   1 
ATOM   6092  O  O   . THR A  1 802 ? 32.860  -12.590 33.208  1.00 45.17  ? 802  THR A O   1 
ATOM   6093  C  CB  . THR A  1 802 ? 32.670  -15.793 33.714  1.00 47.98  ? 802  THR A CB  1 
ATOM   6094  O  OG1 . THR A  1 802 ? 32.047  -16.913 33.070  1.00 48.69  ? 802  THR A OG1 1 
ATOM   6095  C  CG2 . THR A  1 802 ? 31.631  -15.064 34.556  1.00 48.97  ? 802  THR A CG2 1 
ATOM   6096  N  N   . ALA A  1 803 ? 34.892  -13.389 33.687  1.00 48.16  ? 803  ALA A N   1 
ATOM   6097  C  CA  . ALA A  1 803 ? 35.338  -12.120 34.262  1.00 49.06  ? 803  ALA A CA  1 
ATOM   6098  C  C   . ALA A  1 803 ? 35.533  -11.087 33.164  1.00 45.52  ? 803  ALA A C   1 
ATOM   6099  O  O   . ALA A  1 803 ? 34.970  -9.999  33.225  1.00 45.56  ? 803  ALA A O   1 
ATOM   6100  C  CB  . ALA A  1 803 ? 36.622  -12.297 35.055  1.00 40.59  ? 803  ALA A CB  1 
ATOM   6101  N  N   . GLY A  1 804 ? 36.332  -11.442 32.160  1.00 50.21  ? 804  GLY A N   1 
ATOM   6102  C  CA  . GLY A  1 804 ? 36.520  -10.606 30.983  1.00 48.09  ? 804  GLY A CA  1 
ATOM   6103  C  C   . GLY A  1 804 ? 35.190  -10.258 30.339  1.00 45.78  ? 804  GLY A C   1 
ATOM   6104  O  O   . GLY A  1 804 ? 34.931  -9.106  30.024  1.00 41.95  ? 804  GLY A O   1 
ATOM   6105  N  N   . TRP A  1 805 ? 34.336  -11.261 30.168  1.00 45.35  ? 805  TRP A N   1 
ATOM   6106  C  CA  . TRP A  1 805 ? 33.040  -11.069 29.533  1.00 43.22  ? 805  TRP A CA  1 
ATOM   6107  C  C   . TRP A  1 805 ? 32.221  -10.053 30.305  1.00 45.22  ? 805  TRP A C   1 
ATOM   6108  O  O   . TRP A  1 805 ? 31.748  -9.063  29.724  1.00 42.60  ? 805  TRP A O   1 
ATOM   6109  C  CB  . TRP A  1 805 ? 32.294  -12.402 29.431  1.00 45.30  ? 805  TRP A CB  1 
ATOM   6110  C  CG  . TRP A  1 805 ? 31.101  -12.410 28.521  1.00 41.90  ? 805  TRP A CG  1 
ATOM   6111  C  CD1 . TRP A  1 805 ? 31.066  -12.831 27.228  1.00 39.73  ? 805  TRP A CD1 1 
ATOM   6112  C  CD2 . TRP A  1 805 ? 29.769  -12.004 28.844  1.00 40.58  ? 805  TRP A CD2 1 
ATOM   6113  N  NE1 . TRP A  1 805 ? 29.799  -12.699 26.715  1.00 36.74  ? 805  TRP A NE1 1 
ATOM   6114  C  CE2 . TRP A  1 805 ? 28.980  -12.200 27.688  1.00 36.93  ? 805  TRP A CE2 1 
ATOM   6115  C  CE3 . TRP A  1 805 ? 29.166  -11.489 29.993  1.00 40.63  ? 805  TRP A CE3 1 
ATOM   6116  C  CZ2 . TRP A  1 805 ? 27.623  -11.908 27.649  1.00 37.81  ? 805  TRP A CZ2 1 
ATOM   6117  C  CZ3 . TRP A  1 805 ? 27.812  -11.192 29.954  1.00 42.26  ? 805  TRP A CZ3 1 
ATOM   6118  C  CH2 . TRP A  1 805 ? 27.054  -11.410 28.793  1.00 42.84  ? 805  TRP A CH2 1 
ATOM   6119  N  N   . ASN A  1 806 ? 32.072  -10.284 31.614  1.00 46.92  ? 806  ASN A N   1 
ATOM   6120  C  CA  . ASN A  1 806 ? 31.345  -9.361  32.496  1.00 42.90  ? 806  ASN A CA  1 
ATOM   6121  C  C   . ASN A  1 806 ? 31.933  -7.962  32.482  1.00 42.26  ? 806  ASN A C   1 
ATOM   6122  O  O   . ASN A  1 806 ? 31.205  -6.970  32.531  1.00 40.41  ? 806  ASN A O   1 
ATOM   6123  C  CB  . ASN A  1 806 ? 31.325  -9.879  33.933  1.00 51.14  ? 806  ASN A CB  1 
ATOM   6124  C  CG  . ASN A  1 806 ? 30.292  -10.971 34.152  1.00 50.51  ? 806  ASN A CG  1 
ATOM   6125  O  OD1 . ASN A  1 806 ? 30.596  -12.008 34.729  1.00 56.90  ? 806  ASN A OD1 1 
ATOM   6126  N  ND2 . ASN A  1 806 ? 29.066  -10.739 33.695  1.00 51.04  ? 806  ASN A ND2 1 
ATOM   6127  N  N   . TYR A  1 807 ? 33.256  -7.883  32.407  1.00 42.22  ? 807  TYR A N   1 
ATOM   6128  C  CA  . TYR A  1 807 ? 33.909  -6.592  32.349  1.00 43.22  ? 807  TYR A CA  1 
ATOM   6129  C  C   . TYR A  1 807 ? 33.563  -5.857  31.052  1.00 46.43  ? 807  TYR A C   1 
ATOM   6130  O  O   . TYR A  1 807 ? 33.311  -4.649  31.059  1.00 49.39  ? 807  TYR A O   1 
ATOM   6131  C  CB  . TYR A  1 807 ? 35.430  -6.735  32.479  1.00 39.82  ? 807  TYR A CB  1 
ATOM   6132  C  CG  . TYR A  1 807 ? 36.096  -5.395  32.664  1.00 46.82  ? 807  TYR A CG  1 
ATOM   6133  C  CD1 . TYR A  1 807 ? 36.034  -4.735  33.883  1.00 51.02  ? 807  TYR A CD1 1 
ATOM   6134  C  CD2 . TYR A  1 807 ? 36.739  -4.761  31.611  1.00 49.43  ? 807  TYR A CD2 1 
ATOM   6135  C  CE1 . TYR A  1 807 ? 36.624  -3.501  34.055  1.00 51.31  ? 807  TYR A CE1 1 
ATOM   6136  C  CE2 . TYR A  1 807 ? 37.338  -3.527  31.774  1.00 48.29  ? 807  TYR A CE2 1 
ATOM   6137  C  CZ  . TYR A  1 807 ? 37.272  -2.901  32.998  1.00 52.65  ? 807  TYR A CZ  1 
ATOM   6138  O  OH  . TYR A  1 807 ? 37.857  -1.669  33.164  1.00 55.93  ? 807  TYR A OH  1 
ATOM   6139  N  N   . LEU A  1 808 ? 33.564  -6.585  29.939  1.00 43.44  ? 808  LEU A N   1 
ATOM   6140  C  CA  . LEU A  1 808 ? 33.257  -5.992  28.640  1.00 40.61  ? 808  LEU A CA  1 
ATOM   6141  C  C   . LEU A  1 808 ? 31.848  -5.448  28.636  1.00 38.57  ? 808  LEU A C   1 
ATOM   6142  O  O   . LEU A  1 808 ? 31.620  -4.330  28.170  1.00 38.99  ? 808  LEU A O   1 
ATOM   6143  C  CB  . LEU A  1 808 ? 33.431  -7.010  27.508  1.00 38.66  ? 808  LEU A CB  1 
ATOM   6144  C  CG  . LEU A  1 808 ? 34.883  -7.135  27.071  1.00 40.56  ? 808  LEU A CG  1 
ATOM   6145  C  CD1 . LEU A  1 808 ? 35.042  -8.269  26.102  1.00 43.32  ? 808  LEU A CD1 1 
ATOM   6146  C  CD2 . LEU A  1 808 ? 35.359  -5.812  26.464  1.00 39.53  ? 808  LEU A CD2 1 
ATOM   6147  N  N   . LEU A  1 809 ? 30.912  -6.224  29.182  1.00 37.06  ? 809  LEU A N   1 
ATOM   6148  C  CA  . LEU A  1 809 ? 29.506  -5.819  29.200  1.00 41.46  ? 809  LEU A CA  1 
ATOM   6149  C  C   . LEU A  1 809 ? 29.313  -4.550  30.005  1.00 42.64  ? 809  LEU A C   1 
ATOM   6150  O  O   . LEU A  1 809 ? 28.455  -3.723  29.704  1.00 46.19  ? 809  LEU A O   1 
ATOM   6151  C  CB  . LEU A  1 809 ? 28.618  -6.922  29.764  1.00 41.00  ? 809  LEU A CB  1 
ATOM   6152  C  CG  . LEU A  1 809 ? 27.127  -6.577  29.713  1.00 47.64  ? 809  LEU A CG  1 
ATOM   6153  C  CD1 . LEU A  1 809 ? 26.667  -6.181  28.281  1.00 36.99  ? 809  LEU A CD1 1 
ATOM   6154  C  CD2 . LEU A  1 809 ? 26.289  -7.730  30.272  1.00 38.76  ? 809  LEU A CD2 1 
ATOM   6155  N  N   . GLU A  1 810 ? 30.136  -4.388  31.025  1.00 43.91  ? 810  GLU A N   1 
ATOM   6156  C  CA  . GLU A  1 810 ? 30.057  -3.204  31.842  1.00 49.53  ? 810  GLU A CA  1 
ATOM   6157  C  C   . GLU A  1 810 ? 30.593  -2.016  31.043  1.00 49.06  ? 810  GLU A C   1 
ATOM   6158  O  O   . GLU A  1 810 ? 29.962  -0.964  31.000  1.00 48.45  ? 810  GLU A O   1 
ATOM   6159  C  CB  . GLU A  1 810 ? 30.827  -3.403  33.151  1.00 53.76  ? 810  GLU A CB  1 
ATOM   6160  C  CG  . GLU A  1 810 ? 30.994  -2.144  33.981  1.00 65.53  ? 810  GLU A CG  1 
ATOM   6161  C  CD  . GLU A  1 810 ? 32.338  -2.082  34.694  1.00 76.58  ? 810  GLU A CD  1 
ATOM   6162  O  OE1 . GLU A  1 810 ? 32.578  -2.920  35.602  1.00 84.13  ? 810  GLU A OE1 1 
ATOM   6163  O  OE2 . GLU A  1 810 ? 33.147  -1.186  34.342  1.00 71.95  ? 810  GLU A OE2 1 
ATOM   6164  N  N   . GLN A  1 811 ? 31.753  -2.182  30.413  1.00 45.06  ? 811  GLN A N   1 
ATOM   6165  C  CA  . GLN A  1 811 ? 32.286  -1.158  29.514  1.00 45.47  ? 811  GLN A CA  1 
ATOM   6166  C  C   . GLN A  1 811 ? 31.279  -0.767  28.439  1.00 43.77  ? 811  GLN A C   1 
ATOM   6167  O  O   . GLN A  1 811 ? 31.239  0.378   27.998  1.00 42.87  ? 811  GLN A O   1 
ATOM   6168  C  CB  . GLN A  1 811 ? 33.573  -1.644  28.844  1.00 42.68  ? 811  GLN A CB  1 
ATOM   6169  C  CG  . GLN A  1 811 ? 34.593  -2.117  29.845  1.00 47.96  ? 811  GLN A CG  1 
ATOM   6170  C  CD  . GLN A  1 811 ? 34.903  -1.053  30.865  1.00 52.86  ? 811  GLN A CD  1 
ATOM   6171  O  OE1 . GLN A  1 811 ? 34.609  -1.202  32.063  1.00 54.43  ? 811  GLN A OE1 1 
ATOM   6172  N  NE2 . GLN A  1 811 ? 35.505  0.037   30.397  1.00 47.25  ? 811  GLN A NE2 1 
ATOM   6173  N  N   . TYR A  1 812 ? 30.471  -1.729  28.007  1.00 43.09  ? 812  TYR A N   1 
ATOM   6174  C  CA  . TYR A  1 812 ? 29.495  -1.459  26.964  1.00 41.77  ? 812  TYR A CA  1 
ATOM   6175  C  C   . TYR A  1 812 ? 28.535  -0.364  27.388  1.00 37.89  ? 812  TYR A C   1 
ATOM   6176  O  O   . TYR A  1 812 ? 28.252  0.546   26.617  1.00 40.46  ? 812  TYR A O   1 
ATOM   6177  C  CB  . TYR A  1 812 ? 28.717  -2.724  26.604  1.00 41.51  ? 812  TYR A CB  1 
ATOM   6178  C  CG  . TYR A  1 812 ? 27.723  -2.519  25.485  1.00 38.25  ? 812  TYR A CG  1 
ATOM   6179  C  CD1 . TYR A  1 812 ? 28.122  -2.624  24.149  1.00 38.19  ? 812  TYR A CD1 1 
ATOM   6180  C  CD2 . TYR A  1 812 ? 26.386  -2.212  25.751  1.00 37.19  ? 812  TYR A CD2 1 
ATOM   6181  C  CE1 . TYR A  1 812 ? 27.220  -2.437  23.109  1.00 33.82  ? 812  TYR A CE1 1 
ATOM   6182  C  CE2 . TYR A  1 812 ? 25.471  -2.027  24.718  1.00 40.89  ? 812  TYR A CE2 1 
ATOM   6183  C  CZ  . TYR A  1 812 ? 25.896  -2.149  23.398  1.00 40.51  ? 812  TYR A CZ  1 
ATOM   6184  O  OH  . TYR A  1 812 ? 25.007  -1.969  22.362  1.00 43.29  ? 812  TYR A OH  1 
ATOM   6185  N  N   . GLU A  1 813 ? 28.042  -0.451  28.618  1.00 41.74  ? 813  GLU A N   1 
ATOM   6186  C  CA  . GLU A  1 813 ? 27.043  0.502   29.112  1.00 44.91  ? 813  GLU A CA  1 
ATOM   6187  C  C   . GLU A  1 813 ? 27.617  1.880   29.417  1.00 44.23  ? 813  GLU A C   1 
ATOM   6188  O  O   . GLU A  1 813 ? 26.870  2.856   29.485  1.00 45.40  ? 813  GLU A O   1 
ATOM   6189  C  CB  . GLU A  1 813 ? 26.366  -0.043  30.356  1.00 43.17  ? 813  GLU A CB  1 
ATOM   6190  C  CG  . GLU A  1 813 ? 25.950  -1.505  30.202  1.00 58.28  ? 813  GLU A CG  1 
ATOM   6191  C  CD  . GLU A  1 813 ? 24.836  -1.905  31.150  1.00 64.51  ? 813  GLU A CD  1 
ATOM   6192  O  OE1 . GLU A  1 813 ? 23.815  -1.176  31.200  1.00 65.63  ? 813  GLU A OE1 1 
ATOM   6193  O  OE2 . GLU A  1 813 ? 24.984  -2.943  31.838  1.00 62.58  ? 813  GLU A OE2 1 
ATOM   6194  N  N   . LEU A  1 814 ? 28.934  1.956   29.588  1.00 37.46  ? 814  LEU A N   1 
ATOM   6195  C  CA  . LEU A  1 814 ? 29.596  3.214   29.901  1.00 42.74  ? 814  LEU A CA  1 
ATOM   6196  C  C   . LEU A  1 814 ? 30.213  3.902   28.680  1.00 44.38  ? 814  LEU A C   1 
ATOM   6197  O  O   . LEU A  1 814 ? 30.504  5.091   28.718  1.00 45.07  ? 814  LEU A O   1 
ATOM   6198  C  CB  . LEU A  1 814 ? 30.682  2.986   30.953  1.00 42.33  ? 814  LEU A CB  1 
ATOM   6199  C  CG  . LEU A  1 814 ? 30.180  2.475   32.309  1.00 48.16  ? 814  LEU A CG  1 
ATOM   6200  C  CD1 . LEU A  1 814 ? 31.332  2.207   33.249  1.00 41.69  ? 814  LEU A CD1 1 
ATOM   6201  C  CD2 . LEU A  1 814 ? 29.222  3.478   32.912  1.00 44.71  ? 814  LEU A CD2 1 
ATOM   6202  N  N   . SER A  1 815 ? 30.415  3.165   27.596  1.00 45.41  ? 815  SER A N   1 
ATOM   6203  C  CA  . SER A  1 815 ? 31.215  3.695   26.498  1.00 41.03  ? 815  SER A CA  1 
ATOM   6204  C  C   . SER A  1 815 ? 30.504  4.804   25.729  1.00 42.80  ? 815  SER A C   1 
ATOM   6205  O  O   . SER A  1 815 ? 29.279  4.827   25.601  1.00 42.96  ? 815  SER A O   1 
ATOM   6206  C  CB  . SER A  1 815 ? 31.607  2.580   25.546  1.00 39.13  ? 815  SER A CB  1 
ATOM   6207  O  OG  . SER A  1 815 ? 32.252  3.094   24.397  1.00 35.54  ? 815  SER A OG  1 
ATOM   6208  N  N   . MET A  1 816 ? 31.300  5.730   25.225  1.00 41.25  ? 816  MET A N   1 
ATOM   6209  C  CA  . MET A  1 816 ? 30.790  6.879   24.514  1.00 40.17  ? 816  MET A CA  1 
ATOM   6210  C  C   . MET A  1 816 ? 31.196  6.794   23.049  1.00 39.46  ? 816  MET A C   1 
ATOM   6211  O  O   . MET A  1 816 ? 30.941  7.716   22.281  1.00 39.65  ? 816  MET A O   1 
ATOM   6212  C  CB  . MET A  1 816 ? 31.309  8.163   25.158  1.00 33.94  ? 816  MET A CB  1 
ATOM   6213  C  CG  . MET A  1 816 ? 30.635  8.464   26.489  1.00 40.22  ? 816  MET A CG  1 
ATOM   6214  S  SD  . MET A  1 816 ? 29.072  9.372   26.320  1.00 51.01  ? 816  MET A SD  1 
ATOM   6215  C  CE  . MET A  1 816 ? 27.976  8.255   27.174  1.00 44.71  ? 816  MET A CE  1 
ATOM   6216  N  N   . SER A  1 817 ? 31.845  5.696   22.671  1.00 30.41  ? 817  SER A N   1 
ATOM   6217  C  CA  . SER A  1 817 ? 32.090  5.417   21.261  1.00 32.16  ? 817  SER A CA  1 
ATOM   6218  C  C   . SER A  1 817 ? 31.208  4.281   20.787  1.00 33.82  ? 817  SER A C   1 
ATOM   6219  O  O   . SER A  1 817 ? 31.357  3.149   21.239  1.00 35.49  ? 817  SER A O   1 
ATOM   6220  C  CB  . SER A  1 817 ? 33.541  5.052   21.006  1.00 34.25  ? 817  SER A CB  1 
ATOM   6221  O  OG  . SER A  1 817 ? 33.730  4.685   19.653  1.00 34.63  ? 817  SER A OG  1 
ATOM   6222  N  N   . SER A  1 818 ? 30.292  4.580   19.877  1.00 33.02  ? 818  SER A N   1 
ATOM   6223  C  CA  . SER A  1 818 ? 29.426  3.555   19.319  1.00 32.90  ? 818  SER A CA  1 
ATOM   6224  C  C   . SER A  1 818 ? 30.222  2.559   18.481  1.00 35.24  ? 818  SER A C   1 
ATOM   6225  O  O   . SER A  1 818 ? 29.852  1.396   18.369  1.00 32.72  ? 818  SER A O   1 
ATOM   6226  C  CB  . SER A  1 818 ? 28.322  4.190   18.489  1.00 30.38  ? 818  SER A CB  1 
ATOM   6227  O  OG  . SER A  1 818 ? 27.434  4.891   19.338  1.00 41.75  ? 818  SER A OG  1 
ATOM   6228  N  N   . ALA A  1 819 ? 31.314  3.018   17.884  1.00 32.96  ? 819  ALA A N   1 
ATOM   6229  C  CA  . ALA A  1 819 ? 32.170  2.099   17.187  1.00 29.36  ? 819  ALA A CA  1 
ATOM   6230  C  C   . ALA A  1 819 ? 32.719  1.112   18.219  1.00 34.08  ? 819  ALA A C   1 
ATOM   6231  O  O   . ALA A  1 819 ? 32.741  -0.083  17.981  1.00 34.06  ? 819  ALA A O   1 
ATOM   6232  C  CB  . ALA A  1 819 ? 33.288  2.831   16.440  1.00 31.52  ? 819  ALA A CB  1 
ATOM   6233  N  N   . GLU A  1 820 ? 33.116  1.602   19.387  1.00 34.95  ? 820  GLU A N   1 
ATOM   6234  C  CA  . GLU A  1 820 ? 33.659  0.706   20.400  1.00 33.20  ? 820  GLU A CA  1 
ATOM   6235  C  C   . GLU A  1 820 ? 32.607  -0.278  20.891  1.00 34.56  ? 820  GLU A C   1 
ATOM   6236  O  O   . GLU A  1 820 ? 32.882  -1.470  21.069  1.00 35.04  ? 820  GLU A O   1 
ATOM   6237  C  CB  . GLU A  1 820 ? 34.221  1.470   21.596  1.00 32.40  ? 820  GLU A CB  1 
ATOM   6238  C  CG  . GLU A  1 820 ? 35.193  0.627   22.393  1.00 35.50  ? 820  GLU A CG  1 
ATOM   6239  C  CD  . GLU A  1 820 ? 35.301  1.027   23.847  1.00 38.29  ? 820  GLU A CD  1 
ATOM   6240  O  OE1 . GLU A  1 820 ? 34.496  1.857   24.314  1.00 35.00  ? 820  GLU A OE1 1 
ATOM   6241  O  OE2 . GLU A  1 820 ? 36.192  0.481   24.533  1.00 42.20  ? 820  GLU A OE2 1 
ATOM   6242  N  N   . GLN A  1 821 ? 31.402  0.228   21.105  1.00 32.53  ? 821  GLN A N   1 
ATOM   6243  C  CA  . GLN A  1 821 ? 30.291  -0.604  21.543  1.00 34.14  ? 821  GLN A CA  1 
ATOM   6244  C  C   . GLN A  1 821 ? 30.019  -1.724  20.565  1.00 32.24  ? 821  GLN A C   1 
ATOM   6245  O  O   . GLN A  1 821 ? 29.680  -2.843  20.949  1.00 31.77  ? 821  GLN A O   1 
ATOM   6246  C  CB  . GLN A  1 821 ? 29.038  0.244   21.711  1.00 34.15  ? 821  GLN A CB  1 
ATOM   6247  C  CG  . GLN A  1 821 ? 29.064  1.139   22.933  1.00 35.66  ? 821  GLN A CG  1 
ATOM   6248  C  CD  . GLN A  1 821 ? 27.905  2.091   22.937  1.00 36.10  ? 821  GLN A CD  1 
ATOM   6249  O  OE1 . GLN A  1 821 ? 27.737  2.878   22.013  1.00 40.09  ? 821  GLN A OE1 1 
ATOM   6250  N  NE2 . GLN A  1 821 ? 27.083  2.016   23.969  1.00 37.58  ? 821  GLN A NE2 1 
ATOM   6251  N  N   . ASN A  1 822 ? 30.183  -1.397  19.291  1.00 32.93  ? 822  ASN A N   1 
ATOM   6252  C  CA  . ASN A  1 822 ? 29.981  -2.333  18.219  1.00 34.14  ? 822  ASN A CA  1 
ATOM   6253  C  C   . ASN A  1 822 ? 30.966  -3.500  18.325  1.00 33.55  ? 822  ASN A C   1 
ATOM   6254  O  O   . ASN A  1 822 ? 30.593  -4.655  18.149  1.00 34.10  ? 822  ASN A O   1 
ATOM   6255  C  CB  . ASN A  1 822 ? 30.101  -1.605  16.884  1.00 40.31  ? 822  ASN A CB  1 
ATOM   6256  C  CG  . ASN A  1 822 ? 29.711  -2.474  15.692  1.00 51.39  ? 822  ASN A CG  1 
ATOM   6257  O  OD1 . ASN A  1 822 ? 28.530  -2.562  15.335  1.00 62.32  ? 822  ASN A OD1 1 
ATOM   6258  N  ND2 . ASN A  1 822 ? 30.709  -3.087  15.049  1.00 43.04  ? 822  ASN A ND2 1 
ATOM   6259  N  N   . LYS A  1 823 ? 32.211  -3.196  18.649  1.00 32.31  ? 823  LYS A N   1 
ATOM   6260  C  CA  . LYS A  1 823 ? 33.228  -4.231  18.739  1.00 31.99  ? 823  LYS A CA  1 
ATOM   6261  C  C   . LYS A  1 823 ? 33.059  -5.057  20.004  1.00 32.11  ? 823  LYS A C   1 
ATOM   6262  O  O   . LYS A  1 823 ? 33.285  -6.256  20.015  1.00 31.78  ? 823  LYS A O   1 
ATOM   6263  C  CB  . LYS A  1 823 ? 34.615  -3.607  18.686  1.00 34.98  ? 823  LYS A CB  1 
ATOM   6264  C  CG  . LYS A  1 823 ? 34.839  -2.731  17.475  1.00 26.66  ? 823  LYS A CG  1 
ATOM   6265  C  CD  . LYS A  1 823 ? 36.314  -2.368  17.339  1.00 34.14  ? 823  LYS A CD  1 
ATOM   6266  C  CE  . LYS A  1 823 ? 36.573  -1.382  16.186  1.00 38.99  ? 823  LYS A CE  1 
ATOM   6267  N  NZ  . LYS A  1 823 ? 35.992  -0.011  16.427  1.00 36.14  ? 823  LYS A NZ  1 
ATOM   6268  N  N   . ILE A  1 824 ? 32.646  -4.402  21.074  1.00 36.41  ? 824  ILE A N   1 
ATOM   6269  C  CA  . ILE A  1 824 ? 32.344  -5.096  22.306  1.00 31.59  ? 824  ILE A CA  1 
ATOM   6270  C  C   . ILE A  1 824 ? 31.224  -6.109  22.108  1.00 34.74  ? 824  ILE A C   1 
ATOM   6271  O  O   . ILE A  1 824 ? 31.299  -7.273  22.545  1.00 34.43  ? 824  ILE A O   1 
ATOM   6272  C  CB  . ILE A  1 824 ? 31.930  -4.105  23.390  1.00 34.99  ? 824  ILE A CB  1 
ATOM   6273  C  CG1 . ILE A  1 824 ? 33.146  -3.298  23.859  1.00 35.35  ? 824  ILE A CG1 1 
ATOM   6274  C  CG2 . ILE A  1 824 ? 31.236  -4.829  24.543  1.00 28.25  ? 824  ILE A CG2 1 
ATOM   6275  C  CD1 . ILE A  1 824 ? 32.785  -2.183  24.764  1.00 32.52  ? 824  ILE A CD1 1 
ATOM   6276  N  N   . LEU A  1 825 ? 30.167  -5.652  21.461  1.00 33.26  ? 825  LEU A N   1 
ATOM   6277  C  CA  . LEU A  1 825 ? 29.016  -6.500  21.277  1.00 35.79  ? 825  LEU A CA  1 
ATOM   6278  C  C   . LEU A  1 825 ? 29.387  -7.680  20.364  1.00 36.59  ? 825  LEU A C   1 
ATOM   6279  O  O   . LEU A  1 825 ? 28.917  -8.786  20.571  1.00 37.78  ? 825  LEU A O   1 
ATOM   6280  C  CB  . LEU A  1 825 ? 27.855  -5.694  20.722  1.00 36.75  ? 825  LEU A CB  1 
ATOM   6281  C  CG  . LEU A  1 825 ? 26.546  -6.452  20.695  1.00 40.00  ? 825  LEU A CG  1 
ATOM   6282  C  CD1 . LEU A  1 825 ? 26.284  -6.957  22.093  1.00 41.72  ? 825  LEU A CD1 1 
ATOM   6283  C  CD2 . LEU A  1 825 ? 25.421  -5.563  20.235  1.00 31.89  ? 825  LEU A CD2 1 
ATOM   6284  N  N   . TYR A  1 826 ? 30.273  -7.472  19.395  1.00 33.03  ? 826  TYR A N   1 
ATOM   6285  C  CA  . TYR A  1 826 ? 30.803  -8.610  18.657  1.00 32.52  ? 826  TYR A CA  1 
ATOM   6286  C  C   . TYR A  1 826 ? 31.514  -9.579  19.603  1.00 36.56  ? 826  TYR A C   1 
ATOM   6287  O  O   . TYR A  1 826 ? 31.259  -10.773 19.574  1.00 41.62  ? 826  TYR A O   1 
ATOM   6288  C  CB  . TYR A  1 826 ? 31.752  -8.154  17.553  1.00 37.86  ? 826  TYR A CB  1 
ATOM   6289  C  CG  . TYR A  1 826 ? 32.558  -9.268  16.912  1.00 38.61  ? 826  TYR A CG  1 
ATOM   6290  C  CD1 . TYR A  1 826 ? 32.034  -10.039 15.887  1.00 47.30  ? 826  TYR A CD1 1 
ATOM   6291  C  CD2 . TYR A  1 826 ? 33.844  -9.548  17.339  1.00 42.29  ? 826  TYR A CD2 1 
ATOM   6292  C  CE1 . TYR A  1 826 ? 32.781  -11.054 15.298  1.00 50.72  ? 826  TYR A CE1 1 
ATOM   6293  C  CE2 . TYR A  1 826 ? 34.596  -10.559 16.764  1.00 41.39  ? 826  TYR A CE2 1 
ATOM   6294  C  CZ  . TYR A  1 826 ? 34.063  -11.308 15.752  1.00 46.32  ? 826  TYR A CZ  1 
ATOM   6295  O  OH  . TYR A  1 826 ? 34.829  -12.309 15.194  1.00 60.15  ? 826  TYR A OH  1 
ATOM   6296  N  N   . ALA A  1 827 ? 32.393  -9.054  20.447  1.00 38.15  ? 827  ALA A N   1 
ATOM   6297  C  CA  . ALA A  1 827 ? 33.188  -9.856  21.370  1.00 34.67  ? 827  ALA A CA  1 
ATOM   6298  C  C   . ALA A  1 827 ? 32.313  -10.707 22.260  1.00 36.12  ? 827  ALA A C   1 
ATOM   6299  O  O   . ALA A  1 827 ? 32.571  -11.900 22.447  1.00 38.93  ? 827  ALA A O   1 
ATOM   6300  C  CB  . ALA A  1 827 ? 34.072  -8.964  22.219  1.00 31.77  ? 827  ALA A CB  1 
ATOM   6301  N  N   . LEU A  1 828 ? 31.291  -10.090 22.837  1.00 37.75  ? 828  LEU A N   1 
ATOM   6302  C  CA  . LEU A  1 828 ? 30.441  -10.811 23.771  1.00 38.48  ? 828  LEU A CA  1 
ATOM   6303  C  C   . LEU A  1 828 ? 29.787  -11.956 23.007  1.00 39.54  ? 828  LEU A C   1 
ATOM   6304  O  O   . LEU A  1 828 ? 29.499  -13.017 23.559  1.00 35.37  ? 828  LEU A O   1 
ATOM   6305  C  CB  . LEU A  1 828 ? 29.388  -9.889  24.403  1.00 34.12  ? 828  LEU A CB  1 
ATOM   6306  C  CG  . LEU A  1 828 ? 29.894  -8.729  25.267  1.00 37.44  ? 828  LEU A CG  1 
ATOM   6307  C  CD1 . LEU A  1 828 ? 28.744  -7.809  25.730  1.00 30.03  ? 828  LEU A CD1 1 
ATOM   6308  C  CD2 . LEU A  1 828 ? 30.666  -9.275  26.445  1.00 36.06  ? 828  LEU A CD2 1 
ATOM   6309  N  N   . SER A  1 829 ? 29.590  -11.743 21.713  1.00 37.06  ? 829  SER A N   1 
ATOM   6310  C  CA  . SER A  1 829 ? 28.892  -12.724 20.912  1.00 41.87  ? 829  SER A CA  1 
ATOM   6311  C  C   . SER A  1 829 ? 29.803  -13.908 20.544  1.00 38.98  ? 829  SER A C   1 
ATOM   6312  O  O   . SER A  1 829 ? 29.317  -14.921 20.054  1.00 37.80  ? 829  SER A O   1 
ATOM   6313  C  CB  . SER A  1 829 ? 28.318  -12.068 19.655  1.00 37.68  ? 829  SER A CB  1 
ATOM   6314  O  OG  . SER A  1 829 ? 29.287  -12.029 18.605  1.00 36.81  ? 829  SER A OG  1 
ATOM   6315  N  N   . THR A  1 830 ? 31.107  -13.799 20.798  1.00 33.86  ? 830  THR A N   1 
ATOM   6316  C  CA  . THR A  1 830 ? 32.013  -14.913 20.507  1.00 38.75  ? 830  THR A CA  1 
ATOM   6317  C  C   . THR A  1 830 ? 32.139  -15.864 21.703  1.00 44.05  ? 830  THR A C   1 
ATOM   6318  O  O   . THR A  1 830 ? 32.992  -16.740 21.726  1.00 43.48  ? 830  THR A O   1 
ATOM   6319  C  CB  . THR A  1 830 ? 33.412  -14.431 20.131  1.00 42.20  ? 830  THR A CB  1 
ATOM   6320  O  OG1 . THR A  1 830 ? 34.058  -13.893 21.291  1.00 36.20  ? 830  THR A OG1 1 
ATOM   6321  C  CG2 . THR A  1 830 ? 33.341  -13.376 19.036  1.00 45.28  ? 830  THR A CG2 1 
ATOM   6322  N  N   . SER A  1 831 ? 31.282  -15.675 22.697  1.00 39.70  ? 831  SER A N   1 
ATOM   6323  C  CA  . SER A  1 831 ? 31.333  -16.457 23.900  1.00 40.87  ? 831  SER A CA  1 
ATOM   6324  C  C   . SER A  1 831 ? 30.932  -17.910 23.646  1.00 47.56  ? 831  SER A C   1 
ATOM   6325  O  O   . SER A  1 831 ? 29.998  -18.177 22.905  1.00 46.88  ? 831  SER A O   1 
ATOM   6326  C  CB  . SER A  1 831 ? 30.417  -15.841 24.953  1.00 39.06  ? 831  SER A CB  1 
ATOM   6327  O  OG  . SER A  1 831 ? 30.340  -16.683 26.085  1.00 47.27  ? 831  SER A OG  1 
ATOM   6328  N  N   . LYS A  1 832 ? 31.632  -18.841 24.283  1.00 44.37  ? 832  LYS A N   1 
ATOM   6329  C  CA  . LYS A  1 832 ? 31.300  -20.260 24.157  1.00 54.14  ? 832  LYS A CA  1 
ATOM   6330  C  C   . LYS A  1 832 ? 30.121  -20.685 25.073  1.00 56.13  ? 832  LYS A C   1 
ATOM   6331  O  O   . LYS A  1 832 ? 29.481  -21.697 24.806  1.00 61.53  ? 832  LYS A O   1 
ATOM   6332  C  CB  . LYS A  1 832 ? 32.537  -21.134 24.453  1.00 52.13  ? 832  LYS A CB  1 
ATOM   6333  C  CG  . LYS A  1 832 ? 33.842  -20.780 23.680  1.00 48.56  ? 832  LYS A CG  1 
ATOM   6334  C  CD  . LYS A  1 832 ? 33.901  -21.426 22.283  1.00 56.89  ? 832  LYS A CD  1 
ATOM   6335  C  CE  . LYS A  1 832 ? 35.277  -21.290 21.575  1.00 58.88  ? 832  LYS A CE  1 
ATOM   6336  N  NZ  . LYS A  1 832 ? 35.527  -19.966 20.886  1.00 51.77  ? 832  LYS A NZ  1 
ATOM   6337  N  N   . HIS A  1 833 ? 29.831  -19.917 26.129  1.00 55.05  ? 833  HIS A N   1 
ATOM   6338  C  CA  . HIS A  1 833 ? 28.740  -20.232 27.069  1.00 50.83  ? 833  HIS A CA  1 
ATOM   6339  C  C   . HIS A  1 833 ? 27.349  -19.840 26.572  1.00 53.39  ? 833  HIS A C   1 
ATOM   6340  O  O   . HIS A  1 833 ? 27.067  -18.670 26.344  1.00 54.51  ? 833  HIS A O   1 
ATOM   6341  C  CB  . HIS A  1 833 ? 28.952  -19.529 28.420  1.00 56.84  ? 833  HIS A CB  1 
ATOM   6342  C  CG  . HIS A  1 833 ? 30.297  -19.761 29.030  1.00 63.06  ? 833  HIS A CG  1 
ATOM   6343  N  ND1 . HIS A  1 833 ? 30.875  -18.868 29.907  1.00 63.79  ? 833  HIS A ND1 1 
ATOM   6344  C  CD2 . HIS A  1 833 ? 31.176  -20.784 28.900  1.00 65.82  ? 833  HIS A CD2 1 
ATOM   6345  C  CE1 . HIS A  1 833 ? 32.057  -19.325 30.283  1.00 65.68  ? 833  HIS A CE1 1 
ATOM   6346  N  NE2 . HIS A  1 833 ? 32.263  -20.487 29.687  1.00 72.54  ? 833  HIS A NE2 1 
ATOM   6347  N  N   . GLN A  1 834 ? 26.465  -20.816 26.457  1.00 58.90  ? 834  GLN A N   1 
ATOM   6348  C  CA  . GLN A  1 834 ? 25.076  -20.574 26.078  1.00 56.33  ? 834  GLN A CA  1 
ATOM   6349  C  C   . GLN A  1 834 ? 24.346  -19.572 26.976  1.00 54.33  ? 834  GLN A C   1 
ATOM   6350  O  O   . GLN A  1 834 ? 23.482  -18.824 26.512  1.00 56.26  ? 834  GLN A O   1 
ATOM   6351  C  CB  . GLN A  1 834 ? 24.314  -21.899 26.083  1.00 59.53  ? 834  GLN A CB  1 
ATOM   6352  C  CG  . GLN A  1 834 ? 25.003  -22.976 25.273  1.00 65.26  ? 834  GLN A CG  1 
ATOM   6353  C  CD  . GLN A  1 834 ? 25.178  -22.560 23.830  1.00 67.22  ? 834  GLN A CD  1 
ATOM   6354  O  OE1 . GLN A  1 834 ? 24.197  -22.310 23.131  1.00 73.35  ? 834  GLN A OE1 1 
ATOM   6355  N  NE2 . GLN A  1 834 ? 26.428  -22.457 23.379  1.00 66.42  ? 834  GLN A NE2 1 
ATOM   6356  N  N   . GLU A  1 835 ? 24.669  -19.578 28.263  1.00 58.24  ? 835  GLU A N   1 
ATOM   6357  C  CA  . GLU A  1 835 ? 24.052  -18.644 29.198  1.00 57.83  ? 835  GLU A CA  1 
ATOM   6358  C  C   . GLU A  1 835 ? 24.301  -17.204 28.755  1.00 55.02  ? 835  GLU A C   1 
ATOM   6359  O  O   . GLU A  1 835 ? 23.429  -16.352 28.886  1.00 56.26  ? 835  GLU A O   1 
ATOM   6360  C  CB  . GLU A  1 835 ? 24.589  -18.852 30.617  1.00 54.13  ? 835  GLU A CB  1 
ATOM   6361  C  CG  . GLU A  1 835 ? 24.742  -20.317 31.025  1.00 67.56  ? 835  GLU A CG  1 
ATOM   6362  C  CD  . GLU A  1 835 ? 26.140  -20.866 30.772  1.00 68.81  ? 835  GLU A CD  1 
ATOM   6363  O  OE1 . GLU A  1 835 ? 27.037  -20.632 31.617  1.00 66.32  ? 835  GLU A OE1 1 
ATOM   6364  O  OE2 . GLU A  1 835 ? 26.339  -21.541 29.734  1.00 63.27  ? 835  GLU A OE2 1 
ATOM   6365  N  N   . LYS A  1 836 ? 25.492  -16.939 28.224  1.00 53.17  ? 836  LYS A N   1 
ATOM   6366  C  CA  . LYS A  1 836 ? 25.859  -15.579 27.841  1.00 53.24  ? 836  LYS A CA  1 
ATOM   6367  C  C   . LYS A  1 836 ? 25.137  -15.142 26.578  1.00 48.39  ? 836  LYS A C   1 
ATOM   6368  O  O   . LYS A  1 836 ? 24.494  -14.092 26.562  1.00 44.04  ? 836  LYS A O   1 
ATOM   6369  C  CB  . LYS A  1 836 ? 27.369  -15.457 27.631  1.00 48.51  ? 836  LYS A CB  1 
ATOM   6370  C  CG  . LYS A  1 836 ? 28.193  -15.948 28.774  1.00 40.21  ? 836  LYS A CG  1 
ATOM   6371  C  CD  . LYS A  1 836 ? 28.397  -14.909 29.821  1.00 50.69  ? 836  LYS A CD  1 
ATOM   6372  C  CE  . LYS A  1 836 ? 29.577  -15.323 30.695  1.00 55.42  ? 836  LYS A CE  1 
ATOM   6373  N  NZ  . LYS A  1 836 ? 30.722  -15.715 29.806  1.00 56.57  ? 836  LYS A NZ  1 
ATOM   6374  N  N   . LEU A  1 837 ? 25.273  -15.950 25.526  1.00 47.66  ? 837  LEU A N   1 
ATOM   6375  C  CA  . LEU A  1 837 ? 24.671  -15.671 24.223  1.00 46.78  ? 837  LEU A CA  1 
ATOM   6376  C  C   . LEU A  1 837 ? 23.162  -15.430 24.334  1.00 51.84  ? 837  LEU A C   1 
ATOM   6377  O  O   . LEU A  1 837 ? 22.609  -14.522 23.700  1.00 48.76  ? 837  LEU A O   1 
ATOM   6378  C  CB  . LEU A  1 837 ? 24.958  -16.821 23.250  1.00 44.45  ? 837  LEU A CB  1 
ATOM   6379  C  CG  . LEU A  1 837 ? 26.440  -17.178 23.070  1.00 43.97  ? 837  LEU A CG  1 
ATOM   6380  C  CD1 . LEU A  1 837 ? 26.626  -18.436 22.228  1.00 35.88  ? 837  LEU A CD1 1 
ATOM   6381  C  CD2 . LEU A  1 837 ? 27.225  -15.991 22.491  1.00 41.67  ? 837  LEU A CD2 1 
ATOM   6382  N  N   . LEU A  1 838 ? 22.503  -16.230 25.163  1.00 52.76  ? 838  LEU A N   1 
ATOM   6383  C  CA  . LEU A  1 838 ? 21.081  -16.050 25.422  1.00 50.58  ? 838  LEU A CA  1 
ATOM   6384  C  C   . LEU A  1 838 ? 20.803  -14.730 26.124  1.00 49.99  ? 838  LEU A C   1 
ATOM   6385  O  O   . LEU A  1 838 ? 19.818  -14.039 25.824  1.00 52.79  ? 838  LEU A O   1 
ATOM   6386  C  CB  . LEU A  1 838 ? 20.551  -17.205 26.258  1.00 60.41  ? 838  LEU A CB  1 
ATOM   6387  C  CG  . LEU A  1 838 ? 19.095  -17.068 26.692  1.00 65.22  ? 838  LEU A CG  1 
ATOM   6388  C  CD1 . LEU A  1 838 ? 18.178  -16.842 25.490  1.00 63.37  ? 838  LEU A CD1 1 
ATOM   6389  C  CD2 . LEU A  1 838 ? 18.669  -18.295 27.492  1.00 69.71  ? 838  LEU A CD2 1 
ATOM   6390  N  N   . LYS A  1 839 ? 21.680  -14.371 27.052  1.00 46.41  ? 839  LYS A N   1 
ATOM   6391  C  CA  . LYS A  1 839 ? 21.536  -13.112 27.766  1.00 46.59  ? 839  LYS A CA  1 
ATOM   6392  C  C   . LYS A  1 839 ? 21.649  -11.945 26.797  1.00 49.27  ? 839  LYS A C   1 
ATOM   6393  O  O   . LYS A  1 839 ? 20.847  -11.008 26.863  1.00 52.13  ? 839  LYS A O   1 
ATOM   6394  C  CB  . LYS A  1 839 ? 22.582  -12.983 28.875  1.00 51.18  ? 839  LYS A CB  1 
ATOM   6395  C  CG  . LYS A  1 839 ? 22.339  -11.830 29.838  1.00 43.26  ? 839  LYS A CG  1 
ATOM   6396  C  CD  . LYS A  1 839 ? 23.566  -11.565 30.678  1.00 55.85  ? 839  LYS A CD  1 
ATOM   6397  C  CE  . LYS A  1 839 ? 23.263  -10.604 31.842  1.00 65.12  ? 839  LYS A CE  1 
ATOM   6398  N  NZ  . LYS A  1 839 ? 24.406  -10.487 32.805  1.00 49.20  ? 839  LYS A NZ  1 
ATOM   6399  N  N   . LEU A  1 840 ? 22.637  -12.004 25.901  1.00 49.03  ? 840  LEU A N   1 
ATOM   6400  C  CA  . LEU A  1 840 ? 22.774  -10.992 24.845  1.00 51.67  ? 840  LEU A CA  1 
ATOM   6401  C  C   . LEU A  1 840 ? 21.469  -10.852 24.096  1.00 45.73  ? 840  LEU A C   1 
ATOM   6402  O  O   . LEU A  1 840 ? 20.943  -9.761  23.965  1.00 47.19  ? 840  LEU A O   1 
ATOM   6403  C  CB  . LEU A  1 840 ? 23.890  -11.350 23.864  1.00 41.49  ? 840  LEU A CB  1 
ATOM   6404  C  CG  . LEU A  1 840 ? 25.250  -11.327 24.529  1.00 38.93  ? 840  LEU A CG  1 
ATOM   6405  C  CD1 . LEU A  1 840 ? 26.334  -11.733 23.565  1.00 38.78  ? 840  LEU A CD1 1 
ATOM   6406  C  CD2 . LEU A  1 840 ? 25.500  -9.966  25.110  1.00 37.69  ? 840  LEU A CD2 1 
ATOM   6407  N  N   . ILE A  1 841 ? 20.947  -11.979 23.631  1.00 47.17  ? 841  ILE A N   1 
ATOM   6408  C  CA  . ILE A  1 841 ? 19.713  -11.998 22.864  1.00 50.48  ? 841  ILE A CA  1 
ATOM   6409  C  C   . ILE A  1 841 ? 18.573  -11.421 23.679  1.00 52.88  ? 841  ILE A C   1 
ATOM   6410  O  O   . ILE A  1 841 ? 17.810  -10.573 23.204  1.00 51.00  ? 841  ILE A O   1 
ATOM   6411  C  CB  . ILE A  1 841 ? 19.358  -13.422 22.419  1.00 47.30  ? 841  ILE A CB  1 
ATOM   6412  C  CG1 . ILE A  1 841 ? 20.341  -13.890 21.344  1.00 43.96  ? 841  ILE A CG1 1 
ATOM   6413  C  CG2 . ILE A  1 841 ? 17.946  -13.476 21.885  1.00 47.21  ? 841  ILE A CG2 1 
ATOM   6414  C  CD1 . ILE A  1 841 ? 20.212  -15.372 20.977  1.00 46.99  ? 841  ILE A CD1 1 
ATOM   6415  N  N   . GLU A  1 842 ? 18.476  -11.869 24.922  1.00 55.18  ? 842  GLU A N   1 
ATOM   6416  C  CA  . GLU A  1 842 ? 17.403  -11.416 25.787  1.00 52.37  ? 842  GLU A CA  1 
ATOM   6417  C  C   . GLU A  1 842 ? 17.508  -9.927  26.101  1.00 52.60  ? 842  GLU A C   1 
ATOM   6418  O  O   . GLU A  1 842 ? 16.499  -9.219  26.115  1.00 54.95  ? 842  GLU A O   1 
ATOM   6419  C  CB  . GLU A  1 842 ? 17.385  -12.253 27.054  1.00 60.18  ? 842  GLU A CB  1 
ATOM   6420  C  CG  . GLU A  1 842 ? 16.684  -13.590 26.817  1.00 67.57  ? 842  GLU A CG  1 
ATOM   6421  C  CD  . GLU A  1 842 ? 16.670  -14.501 28.033  1.00 79.51  ? 842  GLU A CD  1 
ATOM   6422  O  OE1 . GLU A  1 842 ? 17.553  -14.345 28.914  1.00 74.68  ? 842  GLU A OE1 1 
ATOM   6423  O  OE2 . GLU A  1 842 ? 15.779  -15.384 28.096  1.00 87.15  ? 842  GLU A OE2 1 
ATOM   6424  N  N   . LEU A  1 843 ? 18.726  -9.442  26.319  1.00 51.94  ? 843  LEU A N   1 
ATOM   6425  C  CA  . LEU A  1 843 ? 18.944  -8.010  26.507  1.00 46.67  ? 843  LEU A CA  1 
ATOM   6426  C  C   . LEU A  1 843 ? 18.440  -7.240  25.296  1.00 54.96  ? 843  LEU A C   1 
ATOM   6427  O  O   . LEU A  1 843 ? 17.735  -6.242  25.441  1.00 56.21  ? 843  LEU A O   1 
ATOM   6428  C  CB  . LEU A  1 843 ? 20.424  -7.711  26.734  1.00 42.24  ? 843  LEU A CB  1 
ATOM   6429  C  CG  . LEU A  1 843 ? 21.017  -8.113  28.075  1.00 47.91  ? 843  LEU A CG  1 
ATOM   6430  C  CD1 . LEU A  1 843 ? 22.495  -8.361  27.932  1.00 48.97  ? 843  LEU A CD1 1 
ATOM   6431  C  CD2 . LEU A  1 843 ? 20.763  -7.019  29.082  1.00 44.84  ? 843  LEU A CD2 1 
ATOM   6432  N  N   . GLY A  1 844 ? 18.805  -7.714  24.101  1.00 53.65  ? 844  GLY A N   1 
ATOM   6433  C  CA  . GLY A  1 844 ? 18.417  -7.070  22.858  1.00 50.91  ? 844  GLY A CA  1 
ATOM   6434  C  C   . GLY A  1 844 ? 16.917  -7.072  22.612  1.00 55.35  ? 844  GLY A C   1 
ATOM   6435  O  O   . GLY A  1 844 ? 16.390  -6.198  21.934  1.00 58.02  ? 844  GLY A O   1 
ATOM   6436  N  N   . MET A  1 845 ? 16.221  -8.062  23.150  1.00 54.89  ? 845  MET A N   1 
ATOM   6437  C  CA  . MET A  1 845 ? 14.766  -8.046  23.102  1.00 61.25  ? 845  MET A CA  1 
ATOM   6438  C  C   . MET A  1 845 ? 14.228  -6.855  23.900  1.00 63.24  ? 845  MET A C   1 
ATOM   6439  O  O   . MET A  1 845 ? 13.354  -6.137  23.418  1.00 69.81  ? 845  MET A O   1 
ATOM   6440  C  CB  . MET A  1 845 ? 14.184  -9.363  23.633  1.00 62.89  ? 845  MET A CB  1 
ATOM   6441  C  CG  . MET A  1 845 ? 14.400  -10.558 22.706  1.00 49.57  ? 845  MET A CG  1 
ATOM   6442  S  SD  . MET A  1 845 ? 13.876  -10.173 21.021  1.00 64.83  ? 845  MET A SD  1 
ATOM   6443  C  CE  . MET A  1 845 ? 12.095  -10.351 21.089  1.00 64.53  ? 845  MET A CE  1 
ATOM   6444  N  N   . GLU A  1 846 ? 14.767  -6.645  25.105  1.00 61.01  ? 846  GLU A N   1 
ATOM   6445  C  CA  . GLU A  1 846 ? 14.405  -5.506  25.964  1.00 57.21  ? 846  GLU A CA  1 
ATOM   6446  C  C   . GLU A  1 846 ? 14.654  -4.152  25.307  1.00 60.73  ? 846  GLU A C   1 
ATOM   6447  O  O   . GLU A  1 846 ? 13.902  -3.201  25.508  1.00 59.54  ? 846  GLU A O   1 
ATOM   6448  C  CB  . GLU A  1 846 ? 15.190  -5.541  27.278  1.00 66.37  ? 846  GLU A CB  1 
ATOM   6449  C  CG  . GLU A  1 846 ? 14.513  -6.203  28.461  1.00 72.60  ? 846  GLU A CG  1 
ATOM   6450  C  CD  . GLU A  1 846 ? 15.347  -6.079  29.729  1.00 77.44  ? 846  GLU A CD  1 
ATOM   6451  O  OE1 . GLU A  1 846 ? 15.999  -5.026  29.906  1.00 69.15  ? 846  GLU A OE1 1 
ATOM   6452  O  OE2 . GLU A  1 846 ? 15.362  -7.035  30.538  1.00 88.91  ? 846  GLU A OE2 1 
ATOM   6453  N  N   . GLY A  1 847 ? 15.729  -4.052  24.539  1.00 60.02  ? 847  GLY A N   1 
ATOM   6454  C  CA  . GLY A  1 847 ? 16.067  -2.792  23.915  1.00 57.59  ? 847  GLY A CA  1 
ATOM   6455  C  C   . GLY A  1 847 ? 16.521  -1.727  24.902  1.00 59.04  ? 847  GLY A C   1 
ATOM   6456  O  O   . GLY A  1 847 ? 16.637  -0.564  24.537  1.00 59.74  ? 847  GLY A O   1 
ATOM   6457  N  N   . LYS A  1 848 ? 16.789  -2.111  26.146  1.00 59.59  ? 848  LYS A N   1 
ATOM   6458  C  CA  . LYS A  1 848 ? 17.228  -1.133  27.143  1.00 65.70  ? 848  LYS A CA  1 
ATOM   6459  C  C   . LYS A  1 848 ? 18.750  -0.987  27.125  1.00 56.94  ? 848  LYS A C   1 
ATOM   6460  O  O   . LYS A  1 848 ? 19.276  0.009   26.645  1.00 57.21  ? 848  LYS A O   1 
ATOM   6461  C  CB  . LYS A  1 848 ? 16.734  -1.525  28.547  1.00 66.40  ? 848  LYS A CB  1 
ATOM   6462  C  CG  . LYS A  1 848 ? 15.235  -1.290  28.771  1.00 65.37  ? 848  LYS A CG  1 
ATOM   6463  C  CD  . LYS A  1 848 ? 14.811  -1.589  30.210  1.00 72.09  ? 848  LYS A CD  1 
ATOM   6464  C  CE  . LYS A  1 848 ? 13.987  -0.440  30.796  1.00 82.17  ? 848  LYS A CE  1 
ATOM   6465  N  NZ  . LYS A  1 848 ? 13.383  -0.741  32.133  1.00 75.24  ? 848  LYS A NZ  1 
ATOM   6466  N  N   . VAL A  1 849 ? 19.446  -1.991  27.645  1.00 54.88  ? 849  VAL A N   1 
ATOM   6467  C  CA  . VAL A  1 849 ? 20.901  -2.018  27.628  1.00 50.99  ? 849  VAL A CA  1 
ATOM   6468  C  C   . VAL A  1 849 ? 21.464  -2.061  26.213  1.00 53.57  ? 849  VAL A C   1 
ATOM   6469  O  O   . VAL A  1 849 ? 22.294  -1.240  25.830  1.00 54.69  ? 849  VAL A O   1 
ATOM   6470  C  CB  . VAL A  1 849 ? 21.435  -3.233  28.375  1.00 53.98  ? 849  VAL A CB  1 
ATOM   6471  C  CG1 . VAL A  1 849 ? 22.879  -3.009  28.740  1.00 53.29  ? 849  VAL A CG1 1 
ATOM   6472  C  CG2 . VAL A  1 849 ? 20.607  -3.505  29.607  1.00 55.45  ? 849  VAL A CG2 1 
ATOM   6473  N  N   . ILE A  1 850 ? 21.033  -3.060  25.457  1.00 51.45  ? 850  ILE A N   1 
ATOM   6474  C  CA  . ILE A  1 850 ? 21.386  -3.178  24.052  1.00 47.48  ? 850  ILE A CA  1 
ATOM   6475  C  C   . ILE A  1 850 ? 20.203  -2.766  23.189  1.00 42.93  ? 850  ILE A C   1 
ATOM   6476  O  O   . ILE A  1 850 ? 19.144  -3.377  23.250  1.00 43.19  ? 850  ILE A O   1 
ATOM   6477  C  CB  . ILE A  1 850 ? 21.800  -4.603  23.691  1.00 39.21  ? 850  ILE A CB  1 
ATOM   6478  C  CG1 . ILE A  1 850 ? 23.050  -5.002  24.478  1.00 40.91  ? 850  ILE A CG1 1 
ATOM   6479  C  CG2 . ILE A  1 850 ? 22.070  -4.672  22.234  1.00 39.09  ? 850  ILE A CG2 1 
ATOM   6480  C  CD1 . ILE A  1 850 ? 23.398  -6.456  24.334  1.00 37.67  ? 850  ILE A CD1 1 
ATOM   6481  N  N   . LYS A  1 851 ? 20.392  -1.719  22.396  1.00 49.16  ? 851  LYS A N   1 
ATOM   6482  C  CA  . LYS A  1 851 ? 19.301  -1.115  21.636  1.00 49.76  ? 851  LYS A CA  1 
ATOM   6483  C  C   . LYS A  1 851 ? 18.793  -2.064  20.553  1.00 51.49  ? 851  LYS A C   1 
ATOM   6484  O  O   . LYS A  1 851 ? 19.559  -2.894  20.054  1.00 47.17  ? 851  LYS A O   1 
ATOM   6485  C  CB  . LYS A  1 851 ? 19.763  0.201   21.019  1.00 47.66  ? 851  LYS A CB  1 
ATOM   6486  C  CG  . LYS A  1 851 ? 20.379  1.166   22.027  1.00 61.89  ? 851  LYS A CG  1 
ATOM   6487  C  CD  . LYS A  1 851 ? 19.474  2.373   22.306  1.00 60.98  ? 851  LYS A CD  1 
ATOM   6488  C  CE  . LYS A  1 851 ? 20.116  3.665   21.811  1.00 49.86  ? 851  LYS A CE  1 
ATOM   6489  N  NZ  . LYS A  1 851 ? 19.214  4.830   22.027  1.00 46.91  ? 851  LYS A NZ  1 
ATOM   6490  N  N   . THR A  1 852 ? 17.517  -1.943  20.185  1.00 47.72  ? 852  THR A N   1 
ATOM   6491  C  CA  . THR A  1 852 ? 16.916  -2.904  19.268  1.00 52.85  ? 852  THR A CA  1 
ATOM   6492  C  C   . THR A  1 852 ? 17.399  -2.735  17.815  1.00 47.08  ? 852  THR A C   1 
ATOM   6493  O  O   . THR A  1 852 ? 17.323  -3.669  17.024  1.00 44.93  ? 852  THR A O   1 
ATOM   6494  C  CB  . THR A  1 852 ? 15.386  -2.843  19.321  1.00 53.92  ? 852  THR A CB  1 
ATOM   6495  O  OG1 . THR A  1 852 ? 14.960  -1.486  19.200  1.00 66.23  ? 852  THR A OG1 1 
ATOM   6496  C  CG2 . THR A  1 852 ? 14.875  -3.416  20.637  1.00 57.33  ? 852  THR A CG2 1 
ATOM   6497  N  N   . GLN A  1 853 ? 17.958  -1.580  17.475  1.00 50.10  ? 853  GLN A N   1 
ATOM   6498  C  CA  . GLN A  1 853 ? 18.623  -1.436  16.177  1.00 44.35  ? 853  GLN A CA  1 
ATOM   6499  C  C   . GLN A  1 853 ? 19.827  -2.397  16.066  1.00 38.17  ? 853  GLN A C   1 
ATOM   6500  O  O   . GLN A  1 853 ? 20.492  -2.444  15.048  1.00 39.90  ? 853  GLN A O   1 
ATOM   6501  C  CB  . GLN A  1 853 ? 19.063  0.028   15.946  1.00 39.34  ? 853  GLN A CB  1 
ATOM   6502  C  CG  . GLN A  1 853 ? 20.410  0.428   16.585  1.00 44.75  ? 853  GLN A CG  1 
ATOM   6503  C  CD  . GLN A  1 853 ? 20.659  1.965   16.697  1.00 44.85  ? 853  GLN A CD  1 
ATOM   6504  O  OE1 . GLN A  1 853 ? 20.126  2.775   15.937  1.00 40.23  ? 853  GLN A OE1 1 
ATOM   6505  N  NE2 . GLN A  1 853 ? 21.481  2.346   17.672  1.00 53.23  ? 853  GLN A NE2 1 
ATOM   6506  N  N   . ASN A  1 854 ? 20.112  -3.174  17.103  1.00 41.66  ? 854  ASN A N   1 
ATOM   6507  C  CA  . ASN A  1 854 ? 21.247  -4.086  17.016  1.00 44.59  ? 854  ASN A CA  1 
ATOM   6508  C  C   . ASN A  1 854 ? 20.871  -5.546  17.098  1.00 39.05  ? 854  ASN A C   1 
ATOM   6509  O  O   . ASN A  1 854 ? 21.727  -6.413  16.938  1.00 42.03  ? 854  ASN A O   1 
ATOM   6510  C  CB  . ASN A  1 854 ? 22.260  -3.772  18.098  1.00 40.96  ? 854  ASN A CB  1 
ATOM   6511  C  CG  . ASN A  1 854 ? 22.821  -2.387  17.958  1.00 45.18  ? 854  ASN A CG  1 
ATOM   6512  O  OD1 . ASN A  1 854 ? 23.152  -1.938  16.857  1.00 45.53  ? 854  ASN A OD1 1 
ATOM   6513  N  ND2 . ASN A  1 854 ? 22.899  -1.684  19.063  1.00 41.46  ? 854  ASN A ND2 1 
ATOM   6514  N  N   . LEU A  1 855 ? 19.588  -5.809  17.311  1.00 37.48  ? 855  LEU A N   1 
ATOM   6515  C  CA  . LEU A  1 855 ? 19.103  -7.160  17.555  1.00 40.59  ? 855  LEU A CA  1 
ATOM   6516  C  C   . LEU A  1 855 ? 19.347  -8.072  16.349  1.00 39.26  ? 855  LEU A C   1 
ATOM   6517  O  O   . LEU A  1 855 ? 19.870  -9.189  16.472  1.00 38.39  ? 855  LEU A O   1 
ATOM   6518  C  CB  . LEU A  1 855 ? 17.617  -7.115  17.913  1.00 42.38  ? 855  LEU A CB  1 
ATOM   6519  C  CG  . LEU A  1 855 ? 16.955  -8.464  18.175  1.00 48.71  ? 855  LEU A CG  1 
ATOM   6520  C  CD1 . LEU A  1 855 ? 17.718  -9.241  19.231  1.00 40.79  ? 855  LEU A CD1 1 
ATOM   6521  C  CD2 . LEU A  1 855 ? 15.519  -8.249  18.584  1.00 48.35  ? 855  LEU A CD2 1 
ATOM   6522  N  N   . ALA A  1 856 ? 18.998  -7.587  15.172  1.00 37.61  ? 856  ALA A N   1 
ATOM   6523  C  CA  . ALA A  1 856 ? 19.271  -8.349  13.963  1.00 34.84  ? 856  ALA A CA  1 
ATOM   6524  C  C   . ALA A  1 856 ? 20.768  -8.672  13.791  1.00 35.70  ? 856  ALA A C   1 
ATOM   6525  O  O   . ALA A  1 856 ? 21.128  -9.795  13.457  1.00 39.04  ? 856  ALA A O   1 
ATOM   6526  C  CB  . ALA A  1 856 ? 18.746  -7.608  12.771  1.00 28.57  ? 856  ALA A CB  1 
ATOM   6527  N  N   . ALA A  1 857 ? 21.640  -7.695  14.022  1.00 36.06  ? 857  ALA A N   1 
ATOM   6528  C  CA  . ALA A  1 857 ? 23.068  -7.910  13.844  1.00 40.48  ? 857  ALA A CA  1 
ATOM   6529  C  C   . ALA A  1 857 ? 23.589  -8.908  14.892  1.00 42.76  ? 857  ALA A C   1 
ATOM   6530  O  O   . ALA A  1 857 ? 24.445  -9.746  14.611  1.00 35.58  ? 857  ALA A O   1 
ATOM   6531  C  CB  . ALA A  1 857 ? 23.824  -6.584  13.930  1.00 43.85  ? 857  ALA A CB  1 
ATOM   6532  N  N   . LEU A  1 858 ? 23.038  -8.817  16.095  1.00 33.84  ? 858  LEU A N   1 
ATOM   6533  C  CA  . LEU A  1 858 ? 23.438  -9.673  17.182  1.00 33.09  ? 858  LEU A CA  1 
ATOM   6534  C  C   . LEU A  1 858 ? 23.058  -11.152 16.951  1.00 39.88  ? 858  LEU A C   1 
ATOM   6535  O  O   . LEU A  1 858 ? 23.857  -12.059 17.208  1.00 40.33  ? 858  LEU A O   1 
ATOM   6536  C  CB  . LEU A  1 858 ? 22.815  -9.147  18.479  1.00 37.70  ? 858  LEU A CB  1 
ATOM   6537  C  CG  . LEU A  1 858 ? 23.156  -9.859  19.785  1.00 42.29  ? 858  LEU A CG  1 
ATOM   6538  C  CD1 . LEU A  1 858 ? 24.664  -10.021 19.925  1.00 41.66  ? 858  LEU A CD1 1 
ATOM   6539  C  CD2 . LEU A  1 858 ? 22.574  -9.086  20.963  1.00 42.51  ? 858  LEU A CD2 1 
ATOM   6540  N  N   . LEU A  1 859 ? 21.839  -11.401 16.486  1.00 37.70  ? 859  LEU A N   1 
ATOM   6541  C  CA  . LEU A  1 859 ? 21.417  -12.768 16.202  1.00 40.85  ? 859  LEU A CA  1 
ATOM   6542  C  C   . LEU A  1 859 ? 22.275  -13.340 15.088  1.00 42.46  ? 859  LEU A C   1 
ATOM   6543  O  O   . LEU A  1 859 ? 22.575  -14.538 15.073  1.00 39.44  ? 859  LEU A O   1 
ATOM   6544  C  CB  . LEU A  1 859 ? 19.936  -12.827 15.818  1.00 34.70  ? 859  LEU A CB  1 
ATOM   6545  C  CG  . LEU A  1 859 ? 19.019  -12.514 16.999  1.00 41.29  ? 859  LEU A CG  1 
ATOM   6546  C  CD1 . LEU A  1 859 ? 17.600  -12.173 16.564  1.00 41.04  ? 859  LEU A CD1 1 
ATOM   6547  C  CD2 . LEU A  1 859 ? 19.013  -13.682 17.966  1.00 35.89  ? 859  LEU A CD2 1 
ATOM   6548  N  N   . HIS A  1 860 ? 22.666  -12.475 14.157  1.00 36.63  ? 860  HIS A N   1 
ATOM   6549  C  CA  . HIS A  1 860 ? 23.487  -12.877 13.018  1.00 39.04  ? 860  HIS A CA  1 
ATOM   6550  C  C   . HIS A  1 860 ? 24.872  -13.310 13.489  1.00 39.87  ? 860  HIS A C   1 
ATOM   6551  O  O   . HIS A  1 860 ? 25.481  -14.230 12.943  1.00 44.11  ? 860  HIS A O   1 
ATOM   6552  C  CB  . HIS A  1 860 ? 23.593  -11.707 12.028  1.00 45.65  ? 860  HIS A CB  1 
ATOM   6553  C  CG  . HIS A  1 860 ? 24.239  -12.047 10.722  1.00 38.81  ? 860  HIS A CG  1 
ATOM   6554  N  ND1 . HIS A  1 860 ? 25.550  -12.460 10.617  1.00 53.65  ? 860  HIS A ND1 1 
ATOM   6555  C  CD2 . HIS A  1 860 ? 23.765  -11.987 9.456   1.00 42.48  ? 860  HIS A CD2 1 
ATOM   6556  C  CE1 . HIS A  1 860 ? 25.848  -12.673 9.349   1.00 47.50  ? 860  HIS A CE1 1 
ATOM   6557  N  NE2 . HIS A  1 860 ? 24.782  -12.391 8.622   1.00 49.70  ? 860  HIS A NE2 1 
ATOM   6558  N  N   . ALA A  1 861 ? 25.365  -12.629 14.512  1.00 36.84  ? 861  ALA A N   1 
ATOM   6559  C  CA  . ALA A  1 861 ? 26.726  -12.815 14.976  1.00 45.47  ? 861  ALA A CA  1 
ATOM   6560  C  C   . ALA A  1 861 ? 26.807  -14.098 15.788  1.00 42.73  ? 861  ALA A C   1 
ATOM   6561  O  O   . ALA A  1 861 ? 27.757  -14.871 15.671  1.00 41.19  ? 861  ALA A O   1 
ATOM   6562  C  CB  . ALA A  1 861 ? 27.177  -11.610 15.812  1.00 43.48  ? 861  ALA A CB  1 
ATOM   6563  N  N   . ILE A  1 862 ? 25.800  -14.290 16.627  1.00 35.30  ? 862  ILE A N   1 
ATOM   6564  C  CA  . ILE A  1 862 ? 25.674  -15.490 17.409  1.00 36.73  ? 862  ILE A CA  1 
ATOM   6565  C  C   . ILE A  1 862 ? 25.463  -16.698 16.504  1.00 37.32  ? 862  ILE A C   1 
ATOM   6566  O  O   . ILE A  1 862 ? 26.085  -17.739 16.694  1.00 38.71  ? 862  ILE A O   1 
ATOM   6567  C  CB  . ILE A  1 862 ? 24.522  -15.347 18.409  1.00 37.85  ? 862  ILE A CB  1 
ATOM   6568  C  CG1 . ILE A  1 862 ? 24.867  -14.252 19.417  1.00 36.15  ? 862  ILE A CG1 1 
ATOM   6569  C  CG2 . ILE A  1 862 ? 24.268  -16.643 19.109  1.00 34.71  ? 862  ILE A CG2 1 
ATOM   6570  C  CD1 . ILE A  1 862 ? 23.760  -13.902 20.368  1.00 37.20  ? 862  ILE A CD1 1 
ATOM   6571  N  N   . ALA A  1 863 ? 24.626  -16.554 15.485  1.00 38.34  ? 863  ALA A N   1 
ATOM   6572  C  CA  . ALA A  1 863 ? 24.211  -17.721 14.701  1.00 39.44  ? 863  ALA A CA  1 
ATOM   6573  C  C   . ALA A  1 863 ? 25.327  -18.356 13.881  1.00 41.11  ? 863  ALA A C   1 
ATOM   6574  O  O   . ALA A  1 863 ? 25.252  -19.532 13.548  1.00 43.79  ? 863  ALA A O   1 
ATOM   6575  C  CB  . ALA A  1 863 ? 23.053  -17.355 13.779  1.00 36.86  ? 863  ALA A CB  1 
ATOM   6576  N  N   . ARG A  1 864 ? 26.361  -17.600 13.549  1.00 39.36  ? 864  ARG A N   1 
ATOM   6577  C  CA  . ARG A  1 864 ? 27.338  -18.111 12.585  1.00 44.68  ? 864  ARG A CA  1 
ATOM   6578  C  C   . ARG A  1 864 ? 28.479  -18.825 13.274  1.00 44.06  ? 864  ARG A C   1 
ATOM   6579  O  O   . ARG A  1 864 ? 29.392  -19.312 12.608  1.00 47.20  ? 864  ARG A O   1 
ATOM   6580  C  CB  . ARG A  1 864 ? 27.896  -16.983 11.708  1.00 47.94  ? 864  ARG A CB  1 
ATOM   6581  C  CG  . ARG A  1 864 ? 28.474  -15.822 12.515  1.00 49.54  ? 864  ARG A CG  1 
ATOM   6582  C  CD  . ARG A  1 864 ? 28.892  -14.670 11.616  1.00 57.59  ? 864  ARG A CD  1 
ATOM   6583  N  NE  . ARG A  1 864 ? 28.960  -13.404 12.353  1.00 72.92  ? 864  ARG A NE  1 
ATOM   6584  C  CZ  . ARG A  1 864 ? 29.453  -12.268 11.864  1.00 71.58  ? 864  ARG A CZ  1 
ATOM   6585  N  NH1 . ARG A  1 864 ? 29.937  -12.231 10.629  1.00 84.56  ? 864  ARG A NH1 1 
ATOM   6586  N  NH2 . ARG A  1 864 ? 29.463  -11.174 12.616  1.00 76.84  ? 864  ARG A NH2 1 
ATOM   6587  N  N   . ARG A  1 865 ? 28.440  -18.873 14.603  1.00 41.56  ? 865  ARG A N   1 
ATOM   6588  C  CA  . ARG A  1 865 ? 29.425  -19.644 15.346  1.00 42.82  ? 865  ARG A CA  1 
ATOM   6589  C  C   . ARG A  1 865 ? 28.785  -20.928 15.840  1.00 38.98  ? 865  ARG A C   1 
ATOM   6590  O  O   . ARG A  1 865 ? 27.613  -20.931 16.194  1.00 44.62  ? 865  ARG A O   1 
ATOM   6591  C  CB  . ARG A  1 865 ? 29.978  -18.835 16.502  1.00 43.66  ? 865  ARG A CB  1 
ATOM   6592  C  CG  . ARG A  1 865 ? 30.391  -17.463 16.115  1.00 44.45  ? 865  ARG A CG  1 
ATOM   6593  C  CD  . ARG A  1 865 ? 31.011  -16.728 17.288  1.00 49.56  ? 865  ARG A CD  1 
ATOM   6594  N  NE  . ARG A  1 865 ? 32.465  -16.683 17.162  1.00 56.74  ? 865  ARG A NE  1 
ATOM   6595  C  CZ  . ARG A  1 865 ? 33.317  -17.333 17.951  1.00 62.55  ? 865  ARG A CZ  1 
ATOM   6596  N  NH1 . ARG A  1 865 ? 32.869  -18.086 18.961  1.00 54.64  ? 865  ARG A NH1 1 
ATOM   6597  N  NH2 . ARG A  1 865 ? 34.626  -17.214 17.731  1.00 64.07  ? 865  ARG A NH2 1 
ATOM   6598  N  N   . PRO A  1 866 ? 29.539  -22.027 15.835  1.00 37.35  ? 866  PRO A N   1 
ATOM   6599  C  CA  . PRO A  1 866 ? 28.993  -23.340 16.198  1.00 44.06  ? 866  PRO A CA  1 
ATOM   6600  C  C   . PRO A  1 866 ? 28.207  -23.359 17.493  1.00 45.34  ? 866  PRO A C   1 
ATOM   6601  O  O   . PRO A  1 866 ? 27.116  -23.926 17.535  1.00 43.61  ? 866  PRO A O   1 
ATOM   6602  C  CB  . PRO A  1 866 ? 30.244  -24.195 16.314  1.00 47.22  ? 866  PRO A CB  1 
ATOM   6603  C  CG  . PRO A  1 866 ? 31.100  -23.662 15.190  1.00 49.38  ? 866  PRO A CG  1 
ATOM   6604  C  CD  . PRO A  1 866 ? 30.867  -22.151 15.211  1.00 47.83  ? 866  PRO A CD  1 
ATOM   6605  N  N   . LYS A  1 867 ? 28.745  -22.720 18.523  1.00 46.98  ? 867  LYS A N   1 
ATOM   6606  C  CA  . LYS A  1 867 ? 28.091  -22.673 19.820  1.00 44.94  ? 867  LYS A CA  1 
ATOM   6607  C  C   . LYS A  1 867 ? 26.794  -21.887 19.796  1.00 49.14  ? 867  LYS A C   1 
ATOM   6608  O  O   . LYS A  1 867 ? 25.980  -22.006 20.714  1.00 45.71  ? 867  LYS A O   1 
ATOM   6609  C  CB  . LYS A  1 867 ? 29.034  -22.069 20.854  1.00 52.04  ? 867  LYS A CB  1 
ATOM   6610  C  CG  . LYS A  1 867 ? 30.158  -23.007 21.254  1.00 62.01  ? 867  LYS A CG  1 
ATOM   6611  C  CD  . LYS A  1 867 ? 29.639  -24.140 22.136  1.00 59.95  ? 867  LYS A CD  1 
ATOM   6612  C  CE  . LYS A  1 867 ? 30.775  -25.037 22.611  1.00 59.19  ? 867  LYS A CE  1 
ATOM   6613  N  NZ  . LYS A  1 867 ? 30.328  -25.909 23.728  1.00 64.21  ? 867  LYS A NZ  1 
ATOM   6614  N  N   . GLY A  1 868 ? 26.598  -21.084 18.752  1.00 40.12  ? 868  GLY A N   1 
ATOM   6615  C  CA  . GLY A  1 868 ? 25.445  -20.216 18.720  1.00 38.75  ? 868  GLY A CA  1 
ATOM   6616  C  C   . GLY A  1 868 ? 24.361  -20.579 17.732  1.00 40.08  ? 868  GLY A C   1 
ATOM   6617  O  O   . GLY A  1 868 ? 23.247  -20.104 17.864  1.00 45.67  ? 868  GLY A O   1 
ATOM   6618  N  N   . GLN A  1 869 ? 24.655  -21.411 16.745  1.00 39.64  ? 869  GLN A N   1 
ATOM   6619  C  CA  . GLN A  1 869 ? 23.718  -21.539 15.633  1.00 41.89  ? 869  GLN A CA  1 
ATOM   6620  C  C   . GLN A  1 869 ? 22.387  -22.106 16.065  1.00 40.25  ? 869  GLN A C   1 
ATOM   6621  O  O   . GLN A  1 869 ? 21.356  -21.588 15.671  1.00 44.04  ? 869  GLN A O   1 
ATOM   6622  C  CB  . GLN A  1 869 ? 24.300  -22.387 14.506  1.00 40.56  ? 869  GLN A CB  1 
ATOM   6623  C  CG  . GLN A  1 869 ? 24.682  -23.798 14.882  1.00 49.59  ? 869  GLN A CG  1 
ATOM   6624  C  CD  . GLN A  1 869 ? 25.493  -24.483 13.797  1.00 52.60  ? 869  GLN A CD  1 
ATOM   6625  O  OE1 . GLN A  1 869 ? 25.605  -23.968 12.678  1.00 49.76  ? 869  GLN A OE1 1 
ATOM   6626  N  NE2 . GLN A  1 869 ? 26.075  -25.644 14.124  1.00 56.87  ? 869  GLN A NE2 1 
ATOM   6627  N  N   . GLN A  1 870 ? 22.411  -23.140 16.896  1.00 43.03  ? 870  GLN A N   1 
ATOM   6628  C  CA  . GLN A  1 870 ? 21.198  -23.845 17.289  1.00 40.57  ? 870  GLN A CA  1 
ATOM   6629  C  C   . GLN A  1 870 ? 20.351  -22.951 18.164  1.00 41.58  ? 870  GLN A C   1 
ATOM   6630  O  O   . GLN A  1 870 ? 19.151  -22.774 17.911  1.00 42.75  ? 870  GLN A O   1 
ATOM   6631  C  CB  . GLN A  1 870 ? 21.542  -25.150 18.026  1.00 48.25  ? 870  GLN A CB  1 
ATOM   6632  C  CG  . GLN A  1 870 ? 20.332  -25.958 18.530  1.00 40.90  ? 870  GLN A CG  1 
ATOM   6633  C  CD  . GLN A  1 870 ? 19.476  -26.522 17.407  1.00 44.56  ? 870  GLN A CD  1 
ATOM   6634  O  OE1 . GLN A  1 870 ? 19.974  -27.209 16.516  1.00 50.24  ? 870  GLN A OE1 1 
ATOM   6635  N  NE2 . GLN A  1 870 ? 18.182  -26.218 17.436  1.00 42.54  ? 870  GLN A NE2 1 
ATOM   6636  N  N   . LEU A  1 871 ? 20.989  -22.390 19.190  1.00 35.67  ? 871  LEU A N   1 
ATOM   6637  C  CA  . LEU A  1 871 ? 20.362  -21.431 20.096  1.00 39.00  ? 871  LEU A CA  1 
ATOM   6638  C  C   . LEU A  1 871 ? 19.641  -20.288 19.364  1.00 43.91  ? 871  LEU A C   1 
ATOM   6639  O  O   . LEU A  1 871 ? 18.493  -19.952 19.661  1.00 44.39  ? 871  LEU A O   1 
ATOM   6640  C  CB  . LEU A  1 871 ? 21.422  -20.862 21.037  1.00 44.34  ? 871  LEU A CB  1 
ATOM   6641  C  CG  . LEU A  1 871 ? 21.040  -19.639 21.867  1.00 47.54  ? 871  LEU A CG  1 
ATOM   6642  C  CD1 . LEU A  1 871 ? 19.852  -19.969 22.746  1.00 49.70  ? 871  LEU A CD1 1 
ATOM   6643  C  CD2 . LEU A  1 871 ? 22.226  -19.194 22.705  1.00 51.67  ? 871  LEU A CD2 1 
ATOM   6644  N  N   . ALA A  1 872 ? 20.337  -19.696 18.408  1.00 37.03  ? 872  ALA A N   1 
ATOM   6645  C  CA  . ALA A  1 872 ? 19.779  -18.645 17.584  1.00 43.17  ? 872  ALA A CA  1 
ATOM   6646  C  C   . ALA A  1 872 ? 18.603  -19.152 16.723  1.00 44.69  ? 872  ALA A C   1 
ATOM   6647  O  O   . ALA A  1 872 ? 17.552  -18.511 16.646  1.00 46.70  ? 872  ALA A O   1 
ATOM   6648  C  CB  . ALA A  1 872 ? 20.888  -18.027 16.700  1.00 31.70  ? 872  ALA A CB  1 
ATOM   6649  N  N   . TRP A  1 873 ? 18.777  -20.284 16.059  1.00 40.45  ? 873  TRP A N   1 
ATOM   6650  C  CA  . TRP A  1 873 ? 17.680  -20.876 15.286  1.00 42.86  ? 873  TRP A CA  1 
ATOM   6651  C  C   . TRP A  1 873 ? 16.467  -21.177 16.176  1.00 42.73  ? 873  TRP A C   1 
ATOM   6652  O  O   . TRP A  1 873 ? 15.330  -20.900 15.792  1.00 42.51  ? 873  TRP A O   1 
ATOM   6653  C  CB  . TRP A  1 873 ? 18.174  -22.142 14.583  1.00 41.58  ? 873  TRP A CB  1 
ATOM   6654  C  CG  . TRP A  1 873 ? 17.171  -22.944 13.761  1.00 43.95  ? 873  TRP A CG  1 
ATOM   6655  C  CD1 . TRP A  1 873 ? 17.018  -24.300 13.772  1.00 36.55  ? 873  TRP A CD1 1 
ATOM   6656  C  CD2 . TRP A  1 873 ? 16.248  -22.449 12.778  1.00 47.65  ? 873  TRP A CD2 1 
ATOM   6657  N  NE1 . TRP A  1 873 ? 16.053  -24.682 12.873  1.00 40.18  ? 873  TRP A NE1 1 
ATOM   6658  C  CE2 . TRP A  1 873 ? 15.559  -23.568 12.251  1.00 43.21  ? 873  TRP A CE2 1 
ATOM   6659  C  CE3 . TRP A  1 873 ? 15.934  -21.174 12.292  1.00 39.43  ? 873  TRP A CE3 1 
ATOM   6660  C  CZ2 . TRP A  1 873 ? 14.577  -23.449 11.268  1.00 41.17  ? 873  TRP A CZ2 1 
ATOM   6661  C  CZ3 . TRP A  1 873 ? 14.941  -21.056 11.332  1.00 37.75  ? 873  TRP A CZ3 1 
ATOM   6662  C  CH2 . TRP A  1 873 ? 14.280  -22.187 10.825  1.00 44.93  ? 873  TRP A CH2 1 
ATOM   6663  N  N   . ASP A  1 874 ? 16.704  -21.720 17.369  1.00 37.57  ? 874  ASP A N   1 
ATOM   6664  C  CA  . ASP A  1 874 ? 15.593  -21.965 18.289  1.00 46.86  ? 874  ASP A CA  1 
ATOM   6665  C  C   . ASP A  1 874 ? 14.934  -20.654 18.685  1.00 46.93  ? 874  ASP A C   1 
ATOM   6666  O  O   . ASP A  1 874 ? 13.702  -20.537 18.672  1.00 48.03  ? 874  ASP A O   1 
ATOM   6667  C  CB  . ASP A  1 874 ? 16.044  -22.715 19.546  1.00 46.32  ? 874  ASP A CB  1 
ATOM   6668  C  CG  . ASP A  1 874 ? 16.460  -24.150 19.257  1.00 48.00  ? 874  ASP A CG  1 
ATOM   6669  O  OD1 . ASP A  1 874 ? 16.120  -24.654 18.162  1.00 42.13  ? 874  ASP A OD1 1 
ATOM   6670  O  OD2 . ASP A  1 874 ? 17.135  -24.763 20.121  1.00 47.79  ? 874  ASP A OD2 1 
ATOM   6671  N  N   . PHE A  1 875 ? 15.753  -19.665 19.025  1.00 43.94  ? 875  PHE A N   1 
ATOM   6672  C  CA  . PHE A  1 875 ? 15.200  -18.407 19.475  1.00 43.55  ? 875  PHE A CA  1 
ATOM   6673  C  C   . PHE A  1 875 ? 14.269  -17.809 18.425  1.00 46.45  ? 875  PHE A C   1 
ATOM   6674  O  O   . PHE A  1 875 ? 13.141  -17.446 18.737  1.00 52.06  ? 875  PHE A O   1 
ATOM   6675  C  CB  . PHE A  1 875 ? 16.278  -17.391 19.823  1.00 40.91  ? 875  PHE A CB  1 
ATOM   6676  C  CG  . PHE A  1 875 ? 15.708  -16.044 20.104  1.00 48.72  ? 875  PHE A CG  1 
ATOM   6677  C  CD1 . PHE A  1 875 ? 15.150  -15.769 21.338  1.00 48.24  ? 875  PHE A CD1 1 
ATOM   6678  C  CD2 . PHE A  1 875 ? 15.647  -15.079 19.112  1.00 48.20  ? 875  PHE A CD2 1 
ATOM   6679  C  CE1 . PHE A  1 875 ? 14.589  -14.556 21.590  1.00 48.47  ? 875  PHE A CE1 1 
ATOM   6680  C  CE2 . PHE A  1 875 ? 15.072  -13.861 19.362  1.00 50.78  ? 875  PHE A CE2 1 
ATOM   6681  C  CZ  . PHE A  1 875 ? 14.543  -13.600 20.600  1.00 48.09  ? 875  PHE A CZ  1 
ATOM   6682  N  N   . VAL A  1 876 ? 14.737  -17.704 17.189  1.00 42.65  ? 876  VAL A N   1 
ATOM   6683  C  CA  . VAL A  1 876 ? 13.921  -17.132 16.122  1.00 46.90  ? 876  VAL A CA  1 
ATOM   6684  C  C   . VAL A  1 876 ? 12.601  -17.878 15.921  1.00 46.56  ? 876  VAL A C   1 
ATOM   6685  O  O   . VAL A  1 876 ? 11.562  -17.255 15.725  1.00 46.26  ? 876  VAL A O   1 
ATOM   6686  C  CB  . VAL A  1 876 ? 14.688  -17.088 14.771  1.00 47.08  ? 876  VAL A CB  1 
ATOM   6687  C  CG1 . VAL A  1 876 ? 13.763  -16.675 13.638  1.00 38.69  ? 876  VAL A CG1 1 
ATOM   6688  C  CG2 . VAL A  1 876 ? 15.852  -16.110 14.858  1.00 45.36  ? 876  VAL A CG2 1 
ATOM   6689  N  N   . ARG A  1 877 ? 12.609  -19.203 15.982  1.00 50.78  ? 877  ARG A N   1 
ATOM   6690  C  CA  . ARG A  1 877 ? 11.342  -19.918 15.795  1.00 51.14  ? 877  ARG A CA  1 
ATOM   6691  C  C   . ARG A  1 877 ? 10.399  -19.814 16.997  1.00 47.76  ? 877  ARG A C   1 
ATOM   6692  O  O   . ARG A  1 877 ? 9.191   -19.770 16.829  1.00 50.40  ? 877  ARG A O   1 
ATOM   6693  C  CB  . ARG A  1 877 ? 11.602  -21.378 15.474  1.00 47.59  ? 877  ARG A CB  1 
ATOM   6694  C  CG  . ARG A  1 877 ? 12.188  -21.585 14.105  1.00 49.78  ? 877  ARG A CG  1 
ATOM   6695  C  CD  . ARG A  1 877 ? 12.459  -23.041 13.860  1.00 42.99  ? 877  ARG A CD  1 
ATOM   6696  N  NE  . ARG A  1 877 ? 13.304  -23.616 14.896  1.00 41.97  ? 877  ARG A NE  1 
ATOM   6697  C  CZ  . ARG A  1 877 ? 13.708  -24.882 14.908  1.00 46.73  ? 877  ARG A CZ  1 
ATOM   6698  N  NH1 . ARG A  1 877 ? 13.351  -25.702 13.925  1.00 44.78  ? 877  ARG A NH1 1 
ATOM   6699  N  NH2 . ARG A  1 877 ? 14.481  -25.329 15.893  1.00 44.48  ? 877  ARG A NH2 1 
ATOM   6700  N  N   . GLU A  1 878 ? 10.946  -19.752 18.202  1.00 45.30  ? 878  GLU A N   1 
ATOM   6701  C  CA  . GLU A  1 878 ? 10.111  -19.699 19.404  1.00 49.69  ? 878  GLU A CA  1 
ATOM   6702  C  C   . GLU A  1 878 ? 9.703   -18.285 19.798  1.00 49.54  ? 878  GLU A C   1 
ATOM   6703  O  O   . GLU A  1 878 ? 9.091   -18.094 20.838  1.00 57.26  ? 878  GLU A O   1 
ATOM   6704  C  CB  . GLU A  1 878 ? 10.837  -20.365 20.585  1.00 48.51  ? 878  GLU A CB  1 
ATOM   6705  C  CG  . GLU A  1 878 ? 10.759  -21.890 20.561  1.00 62.57  ? 878  GLU A CG  1 
ATOM   6706  C  CD  . GLU A  1 878 ? 12.026  -22.586 21.047  1.00 64.50  ? 878  GLU A CD  1 
ATOM   6707  O  OE1 . GLU A  1 878 ? 12.556  -22.231 22.128  1.00 55.55  ? 878  GLU A OE1 1 
ATOM   6708  O  OE2 . GLU A  1 878 ? 12.486  -23.506 20.332  1.00 70.82  ? 878  GLU A OE2 1 
ATOM   6709  N  N   . ASN A  1 879 ? 10.054  -17.293 18.986  1.00 51.01  ? 879  ASN A N   1 
ATOM   6710  C  CA  . ASN A  1 879 ? 9.741   -15.893 19.299  1.00 55.95  ? 879  ASN A CA  1 
ATOM   6711  C  C   . ASN A  1 879 ? 9.435   -15.069 18.065  1.00 54.27  ? 879  ASN A C   1 
ATOM   6712  O  O   . ASN A  1 879 ? 9.640   -13.857 18.065  1.00 54.26  ? 879  ASN A O   1 
ATOM   6713  C  CB  . ASN A  1 879 ? 10.896  -15.211 20.046  1.00 52.31  ? 879  ASN A CB  1 
ATOM   6714  C  CG  . ASN A  1 879 ? 11.154  -15.808 21.412  1.00 53.92  ? 879  ASN A CG  1 
ATOM   6715  O  OD1 . ASN A  1 879 ? 10.601  -15.350 22.414  1.00 59.12  ? 879  ASN A OD1 1 
ATOM   6716  N  ND2 . ASN A  1 879 ? 12.011  -16.825 21.463  1.00 47.61  ? 879  ASN A ND2 1 
ATOM   6717  N  N   . TRP A  1 880 ? 8.955   -15.727 17.018  1.00 55.70  ? 880  TRP A N   1 
ATOM   6718  C  CA  . TRP A  1 880 ? 8.737   -15.079 15.728  1.00 52.74  ? 880  TRP A CA  1 
ATOM   6719  C  C   . TRP A  1 880 ? 7.676   -13.986 15.839  1.00 54.12  ? 880  TRP A C   1 
ATOM   6720  O  O   . TRP A  1 880 ? 7.844   -12.877 15.328  1.00 50.81  ? 880  TRP A O   1 
ATOM   6721  C  CB  . TRP A  1 880 ? 8.340   -16.126 14.674  1.00 51.28  ? 880  TRP A CB  1 
ATOM   6722  C  CG  . TRP A  1 880 ? 7.884   -15.537 13.393  1.00 51.53  ? 880  TRP A CG  1 
ATOM   6723  C  CD1 . TRP A  1 880 ? 6.614   -15.515 12.917  1.00 56.91  ? 880  TRP A CD1 1 
ATOM   6724  C  CD2 . TRP A  1 880 ? 8.692   -14.865 12.418  1.00 48.52  ? 880  TRP A CD2 1 
ATOM   6725  N  NE1 . TRP A  1 880 ? 6.573   -14.871 11.696  1.00 51.02  ? 880  TRP A NE1 1 
ATOM   6726  C  CE2 . TRP A  1 880 ? 7.838   -14.462 11.370  1.00 52.19  ? 880  TRP A CE2 1 
ATOM   6727  C  CE3 . TRP A  1 880 ? 10.053  -14.561 12.329  1.00 54.06  ? 880  TRP A CE3 1 
ATOM   6728  C  CZ2 . TRP A  1 880 ? 8.303   -13.764 10.242  1.00 50.45  ? 880  TRP A CZ2 1 
ATOM   6729  C  CZ3 . TRP A  1 880 ? 10.514  -13.869 11.205  1.00 52.65  ? 880  TRP A CZ3 1 
ATOM   6730  C  CH2 . TRP A  1 880 ? 9.638   -13.476 10.184  1.00 48.55  ? 880  TRP A CH2 1 
ATOM   6731  N  N   . THR A  1 881 ? 6.591   -14.308 16.532  1.00 54.99  ? 881  THR A N   1 
ATOM   6732  C  CA  . THR A  1 881 ? 5.483   -13.387 16.705  1.00 54.46  ? 881  THR A CA  1 
ATOM   6733  C  C   . THR A  1 881 ? 5.985   -12.118 17.391  1.00 59.12  ? 881  THR A C   1 
ATOM   6734  O  O   . THR A  1 881 ? 5.580   -11.000 17.046  1.00 52.92  ? 881  THR A O   1 
ATOM   6735  C  CB  . THR A  1 881 ? 4.353   -14.036 17.522  1.00 60.73  ? 881  THR A CB  1 
ATOM   6736  O  OG1 . THR A  1 881 ? 4.825   -14.294 18.849  1.00 72.89  ? 881  THR A OG1 1 
ATOM   6737  C  CG2 . THR A  1 881 ? 3.923   -15.366 16.891  1.00 53.08  ? 881  THR A CG2 1 
ATOM   6738  N  N   . HIS A  1 882 ? 6.908   -12.297 18.332  1.00 55.87  ? 882  HIS A N   1 
ATOM   6739  C  CA  . HIS A  1 882 ? 7.456   -11.179 19.088  1.00 56.01  ? 882  HIS A CA  1 
ATOM   6740  C  C   . HIS A  1 882 ? 8.398   -10.333 18.231  1.00 59.32  ? 882  HIS A C   1 
ATOM   6741  O  O   . HIS A  1 882 ? 8.373   -9.104  18.295  1.00 63.14  ? 882  HIS A O   1 
ATOM   6742  C  CB  . HIS A  1 882 ? 8.178   -11.679 20.335  1.00 56.92  ? 882  HIS A CB  1 
ATOM   6743  C  CG  . HIS A  1 882 ? 7.435   -12.747 21.080  1.00 69.16  ? 882  HIS A CG  1 
ATOM   6744  N  ND1 . HIS A  1 882 ? 7.104   -13.963 20.514  1.00 68.94  ? 882  HIS A ND1 1 
ATOM   6745  C  CD2 . HIS A  1 882 ? 6.963   -12.785 22.349  1.00 76.83  ? 882  HIS A CD2 1 
ATOM   6746  C  CE1 . HIS A  1 882 ? 6.460   -14.702 21.400  1.00 71.40  ? 882  HIS A CE1 1 
ATOM   6747  N  NE2 . HIS A  1 882 ? 6.361   -14.011 22.523  1.00 87.43  ? 882  HIS A NE2 1 
ATOM   6748  N  N   . LEU A  1 883 ? 9.218   -10.989 17.415  1.00 62.35  ? 883  LEU A N   1 
ATOM   6749  C  CA  . LEU A  1 883 ? 10.136  -10.281 16.528  1.00 54.48  ? 883  LEU A CA  1 
ATOM   6750  C  C   . LEU A  1 883 ? 9.361   -9.369  15.590  1.00 53.60  ? 883  LEU A C   1 
ATOM   6751  O  O   . LEU A  1 883 ? 9.817   -8.271  15.245  1.00 55.03  ? 883  LEU A O   1 
ATOM   6752  C  CB  . LEU A  1 883 ? 10.991  -11.273 15.734  1.00 50.15  ? 883  LEU A CB  1 
ATOM   6753  C  CG  . LEU A  1 883 ? 12.080  -11.963 16.562  1.00 54.02  ? 883  LEU A CG  1 
ATOM   6754  C  CD1 . LEU A  1 883 ? 12.560  -13.263 15.918  1.00 47.00  ? 883  LEU A CD1 1 
ATOM   6755  C  CD2 . LEU A  1 883 ? 13.251  -11.014 16.813  1.00 49.04  ? 883  LEU A CD2 1 
ATOM   6756  N  N   . LEU A  1 884 ? 8.175   -9.821  15.197  1.00 54.38  ? 884  LEU A N   1 
ATOM   6757  C  CA  . LEU A  1 884 ? 7.357   -9.082  14.240  1.00 55.97  ? 884  LEU A CA  1 
ATOM   6758  C  C   . LEU A  1 884 ? 6.693   -7.862  14.837  1.00 59.60  ? 884  LEU A C   1 
ATOM   6759  O  O   . LEU A  1 884 ? 6.333   -6.956  14.097  1.00 65.93  ? 884  LEU A O   1 
ATOM   6760  C  CB  . LEU A  1 884 ? 6.283   -9.977  13.643  1.00 55.39  ? 884  LEU A CB  1 
ATOM   6761  C  CG  . LEU A  1 884 ? 6.643   -10.637 12.316  1.00 54.49  ? 884  LEU A CG  1 
ATOM   6762  C  CD1 . LEU A  1 884 ? 5.471   -11.485 11.810  1.00 55.41  ? 884  LEU A CD1 1 
ATOM   6763  C  CD2 . LEU A  1 884 ? 7.072   -9.598  11.297  1.00 57.13  ? 884  LEU A CD2 1 
ATOM   6764  N  N   . LYS A  1 885 ? 6.502   -7.840  16.157  1.00 55.62  ? 885  LYS A N   1 
ATOM   6765  C  CA  . LYS A  1 885 ? 5.958   -6.648  16.806  1.00 62.66  ? 885  LYS A CA  1 
ATOM   6766  C  C   . LYS A  1 885 ? 7.013   -5.549  16.793  1.00 63.04  ? 885  LYS A C   1 
ATOM   6767  O  O   . LYS A  1 885 ? 6.689   -4.357  16.784  1.00 61.77  ? 885  LYS A O   1 
ATOM   6768  C  CB  . LYS A  1 885 ? 5.495   -6.933  18.245  1.00 60.28  ? 885  LYS A CB  1 
ATOM   6769  C  CG  . LYS A  1 885 ? 4.275   -7.859  18.338  1.00 74.85  ? 885  LYS A CG  1 
ATOM   6770  C  CD  . LYS A  1 885 ? 3.479   -7.694  19.645  1.00 79.25  ? 885  LYS A CD  1 
ATOM   6771  C  CE  . LYS A  1 885 ? 2.256   -6.792  19.455  1.00 90.35  ? 885  LYS A CE  1 
ATOM   6772  N  NZ  . LYS A  1 885 ? 1.348   -6.753  20.646  1.00 89.38  ? 885  LYS A NZ  1 
ATOM   6773  N  N   . LYS A  1 886 ? 8.278   -5.955  16.780  1.00 57.29  ? 886  LYS A N   1 
ATOM   6774  C  CA  . LYS A  1 886 ? 9.366   -4.992  16.755  1.00 52.73  ? 886  LYS A CA  1 
ATOM   6775  C  C   . LYS A  1 886 ? 9.670   -4.493  15.336  1.00 57.37  ? 886  LYS A C   1 
ATOM   6776  O  O   . LYS A  1 886 ? 9.999   -3.322  15.171  1.00 59.90  ? 886  LYS A O   1 
ATOM   6777  C  CB  . LYS A  1 886 ? 10.630  -5.589  17.376  1.00 57.03  ? 886  LYS A CB  1 
ATOM   6778  C  CG  . LYS A  1 886 ? 10.402  -6.354  18.689  1.00 60.72  ? 886  LYS A CG  1 
ATOM   6779  C  CD  . LYS A  1 886 ? 11.289  -5.824  19.822  1.00 58.42  ? 886  LYS A CD  1 
ATOM   6780  C  CE  . LYS A  1 886 ? 11.417  -6.825  20.965  1.00 73.96  ? 886  LYS A CE  1 
ATOM   6781  N  NZ  . LYS A  1 886 ? 10.114  -7.393  21.444  1.00 78.88  ? 886  LYS A NZ  1 
ATOM   6782  N  N   . PHE A  1 887 ? 9.561   -5.355  14.316  1.00 60.21  ? 887  PHE A N   1 
ATOM   6783  C  CA  . PHE A  1 887 ? 9.960   -4.962  12.952  1.00 51.03  ? 887  PHE A CA  1 
ATOM   6784  C  C   . PHE A  1 887 ? 8.920   -5.190  11.857  1.00 53.84  ? 887  PHE A C   1 
ATOM   6785  O  O   . PHE A  1 887 ? 8.100   -6.104  11.947  1.00 56.99  ? 887  PHE A O   1 
ATOM   6786  C  CB  . PHE A  1 887 ? 11.223  -5.710  12.528  1.00 48.83  ? 887  PHE A CB  1 
ATOM   6787  C  CG  . PHE A  1 887 ? 12.352  -5.611  13.496  1.00 49.70  ? 887  PHE A CG  1 
ATOM   6788  C  CD1 . PHE A  1 887 ? 13.130  -4.470  13.557  1.00 50.74  ? 887  PHE A CD1 1 
ATOM   6789  C  CD2 . PHE A  1 887 ? 12.665  -6.679  14.320  1.00 50.07  ? 887  PHE A CD2 1 
ATOM   6790  C  CE1 . PHE A  1 887 ? 14.187  -4.377  14.446  1.00 49.04  ? 887  PHE A CE1 1 
ATOM   6791  C  CE2 . PHE A  1 887 ? 13.720  -6.598  15.206  1.00 49.82  ? 887  PHE A CE2 1 
ATOM   6792  C  CZ  . PHE A  1 887 ? 14.481  -5.443  15.271  1.00 51.27  ? 887  PHE A CZ  1 
ATOM   6793  N  N   . ASP A  1 888 ? 8.999   -4.376  10.801  1.00 57.66  ? 888  ASP A N   1 
ATOM   6794  C  CA  . ASP A  1 888 ? 8.288   -4.636  9.534   1.00 59.73  ? 888  ASP A CA  1 
ATOM   6795  C  C   . ASP A  1 888 ? 8.746   -5.966  8.898   1.00 51.36  ? 888  ASP A C   1 
ATOM   6796  O  O   . ASP A  1 888 ? 9.862   -6.415  9.140   1.00 48.26  ? 888  ASP A O   1 
ATOM   6797  C  CB  . ASP A  1 888 ? 8.507   -3.485  8.532   1.00 60.49  ? 888  ASP A CB  1 
ATOM   6798  C  CG  . ASP A  1 888 ? 7.870   -2.161  8.979   1.00 67.29  ? 888  ASP A CG  1 
ATOM   6799  O  OD1 . ASP A  1 888 ? 7.425   -2.051  10.154  1.00 58.29  ? 888  ASP A OD1 1 
ATOM   6800  O  OD2 . ASP A  1 888 ? 7.840   -1.222  8.138   1.00 63.40  ? 888  ASP A OD2 1 
ATOM   6801  N  N   . LEU A  1 889 ? 7.905   -6.565  8.057   1.00 50.86  ? 889  LEU A N   1 
ATOM   6802  C  CA  . LEU A  1 889 ? 8.159   -7.916  7.557   1.00 47.73  ? 889  LEU A CA  1 
ATOM   6803  C  C   . LEU A  1 889 ? 9.269   -8.175  6.509   1.00 45.60  ? 889  LEU A C   1 
ATOM   6804  O  O   . LEU A  1 889 ? 9.988   -9.145  6.666   1.00 50.02  ? 889  LEU A O   1 
ATOM   6805  C  CB  . LEU A  1 889 ? 6.869   -8.501  6.988   1.00 42.77  ? 889  LEU A CB  1 
ATOM   6806  C  CG  . LEU A  1 889 ? 6.964   -9.993  6.615   1.00 47.63  ? 889  LEU A CG  1 
ATOM   6807  C  CD1 . LEU A  1 889 ? 6.913   -10.938 7.817   1.00 46.90  ? 889  LEU A CD1 1 
ATOM   6808  C  CD2 . LEU A  1 889 ? 5.905   -10.391 5.595   1.00 56.35  ? 889  LEU A CD2 1 
ATOM   6809  N  N   . GLY A  1 890 ? 9.508   -7.354  5.493   1.00 44.08  ? 890  GLY A N   1 
ATOM   6810  C  CA  . GLY A  1 890 ? 9.365   -5.935  5.490   1.00 40.14  ? 890  GLY A CA  1 
ATOM   6811  C  C   . GLY A  1 890 ? 10.803  -5.485  5.721   1.00 49.72  ? 890  GLY A C   1 
ATOM   6812  O  O   . GLY A  1 890 ? 11.621  -5.388  4.787   1.00 41.81  ? 890  GLY A O   1 
ATOM   6813  N  N   . SER A  1 891 ? 11.128  -5.257  6.988   1.00 50.52  ? 891  SER A N   1 
ATOM   6814  C  CA  . SER A  1 891 ? 12.365  -4.580  7.375   1.00 51.64  ? 891  SER A CA  1 
ATOM   6815  C  C   . SER A  1 891 ? 13.621  -5.317  6.924   1.00 46.32  ? 891  SER A C   1 
ATOM   6816  O  O   . SER A  1 891 ? 13.591  -6.524  6.718   1.00 45.51  ? 891  SER A O   1 
ATOM   6817  C  CB  . SER A  1 891 ? 12.397  -4.390  8.902   1.00 47.96  ? 891  SER A CB  1 
ATOM   6818  O  OG  . SER A  1 891 ? 12.253  -5.628  9.580   1.00 41.16  ? 891  SER A OG  1 
ATOM   6819  N  N   . TYR A  1 892 ? 14.728  -4.587  6.800   1.00 45.49  ? 892  TYR A N   1 
ATOM   6820  C  CA  . TYR A  1 892 ? 16.022  -5.217  6.575   1.00 46.46  ? 892  TYR A CA  1 
ATOM   6821  C  C   . TYR A  1 892 ? 16.348  -6.117  7.746   1.00 48.08  ? 892  TYR A C   1 
ATOM   6822  O  O   . TYR A  1 892 ? 17.059  -7.109  7.587   1.00 50.12  ? 892  TYR A O   1 
ATOM   6823  C  CB  . TYR A  1 892 ? 17.135  -4.183  6.390   1.00 46.76  ? 892  TYR A CB  1 
ATOM   6824  C  CG  . TYR A  1 892 ? 18.477  -4.761  5.957   1.00 59.13  ? 892  TYR A CG  1 
ATOM   6825  C  CD1 . TYR A  1 892 ? 18.613  -5.456  4.748   1.00 58.49  ? 892  TYR A CD1 1 
ATOM   6826  C  CD2 . TYR A  1 892 ? 19.619  -4.598  6.748   1.00 60.78  ? 892  TYR A CD2 1 
ATOM   6827  C  CE1 . TYR A  1 892 ? 19.856  -5.972  4.340   1.00 61.62  ? 892  TYR A CE1 1 
ATOM   6828  C  CE2 . TYR A  1 892 ? 20.866  -5.116  6.351   1.00 63.52  ? 892  TYR A CE2 1 
ATOM   6829  C  CZ  . TYR A  1 892 ? 20.978  -5.802  5.152   1.00 67.28  ? 892  TYR A CZ  1 
ATOM   6830  O  OH  . TYR A  1 892 ? 22.209  -6.315  4.775   1.00 66.90  ? 892  TYR A OH  1 
ATOM   6831  N  N   . ASP A  1 893 ? 15.832  -5.759  8.920   1.00 43.57  ? 893  ASP A N   1 
ATOM   6832  C  CA  . ASP A  1 893 ? 16.065  -6.511  10.144  1.00 43.52  ? 893  ASP A CA  1 
ATOM   6833  C  C   . ASP A  1 893 ? 15.506  -7.934  10.050  1.00 44.04  ? 893  ASP A C   1 
ATOM   6834  O  O   . ASP A  1 893 ? 16.239  -8.888  10.268  1.00 43.76  ? 893  ASP A O   1 
ATOM   6835  C  CB  . ASP A  1 893 ? 15.455  -5.776  11.338  1.00 46.32  ? 893  ASP A CB  1 
ATOM   6836  C  CG  . ASP A  1 893 ? 15.957  -4.360  11.457  1.00 53.13  ? 893  ASP A CG  1 
ATOM   6837  O  OD1 . ASP A  1 893 ? 15.398  -3.464  10.773  1.00 58.45  ? 893  ASP A OD1 1 
ATOM   6838  O  OD2 . ASP A  1 893 ? 16.924  -4.139  12.221  1.00 55.76  ? 893  ASP A OD2 1 
ATOM   6839  N  N   . ILE A  1 894 ? 14.228  -8.080  9.708   1.00 42.14  ? 894  ILE A N   1 
ATOM   6840  C  CA  . ILE A  1 894 ? 13.640  -9.408  9.533   1.00 43.32  ? 894  ILE A CA  1 
ATOM   6841  C  C   . ILE A  1 894 ? 14.357  -10.241 8.440   1.00 41.12  ? 894  ILE A C   1 
ATOM   6842  O  O   . ILE A  1 894 ? 14.559  -11.455 8.583   1.00 44.53  ? 894  ILE A O   1 
ATOM   6843  C  CB  . ILE A  1 894 ? 12.138  -9.304  9.197   1.00 41.53  ? 894  ILE A CB  1 
ATOM   6844  C  CG1 . ILE A  1 894 ? 11.375  -8.716  10.379  1.00 47.80  ? 894  ILE A CG1 1 
ATOM   6845  C  CG2 . ILE A  1 894 ? 11.562  -10.676 8.844   1.00 43.08  ? 894  ILE A CG2 1 
ATOM   6846  C  CD1 . ILE A  1 894 ? 11.382  -9.577  11.633  1.00 41.05  ? 894  ILE A CD1 1 
ATOM   6847  N  N   . ARG A  1 895 ? 14.739  -9.588  7.355   1.00 36.37  ? 895  ARG A N   1 
ATOM   6848  C  CA  . ARG A  1 895 ? 15.472  -10.256 6.301   1.00 37.65  ? 895  ARG A CA  1 
ATOM   6849  C  C   . ARG A  1 895 ? 16.847  -10.708 6.789   1.00 43.50  ? 895  ARG A C   1 
ATOM   6850  O  O   . ARG A  1 895 ? 17.351  -11.747 6.367   1.00 42.43  ? 895  ARG A O   1 
ATOM   6851  C  CB  . ARG A  1 895 ? 15.617  -9.343  5.088   1.00 43.63  ? 895  ARG A CB  1 
ATOM   6852  C  CG  . ARG A  1 895 ? 16.181  -10.017 3.830   1.00 47.89  ? 895  ARG A CG  1 
ATOM   6853  C  CD  . ARG A  1 895 ? 16.313  -9.012  2.695   1.00 45.05  ? 895  ARG A CD  1 
ATOM   6854  N  NE  . ARG A  1 895 ? 15.283  -7.981  2.807   1.00 46.55  ? 895  ARG A NE  1 
ATOM   6855  C  CZ  . ARG A  1 895 ? 15.270  -6.848  2.110   1.00 50.22  ? 895  ARG A CZ  1 
ATOM   6856  N  NH1 . ARG A  1 895 ? 16.229  -6.590  1.232   1.00 43.65  ? 895  ARG A NH1 1 
ATOM   6857  N  NH2 . ARG A  1 895 ? 14.296  -5.973  2.292   1.00 44.13  ? 895  ARG A NH2 1 
ATOM   6858  N  N   . MET A  1 896 ? 17.461  -9.930  7.674   1.00 43.36  ? 896  MET A N   1 
ATOM   6859  C  CA  . MET A  1 896 ? 18.770  -10.300 8.188   1.00 43.54  ? 896  MET A CA  1 
ATOM   6860  C  C   . MET A  1 896 ? 18.611  -11.395 9.240   1.00 41.44  ? 896  MET A C   1 
ATOM   6861  O  O   . MET A  1 896 ? 19.411  -12.321 9.315   1.00 42.11  ? 896  MET A O   1 
ATOM   6862  C  CB  . MET A  1 896 ? 19.498  -9.082  8.771   1.00 46.72  ? 896  MET A CB  1 
ATOM   6863  C  CG  . MET A  1 896 ? 21.020  -9.087  8.556   1.00 55.26  ? 896  MET A CG  1 
ATOM   6864  S  SD  . MET A  1 896 ? 21.994  -8.234  9.854   1.00 70.43  ? 896  MET A SD  1 
ATOM   6865  C  CE  . MET A  1 896 ? 21.778  -6.511  9.412   1.00 58.99  ? 896  MET A CE  1 
ATOM   6866  N  N   . ILE A  1 897 ? 17.576  -11.283 10.057  1.00 37.58  ? 897  ILE A N   1 
ATOM   6867  C  CA  . ILE A  1 897 ? 17.325  -12.268 11.090  1.00 39.62  ? 897  ILE A CA  1 
ATOM   6868  C  C   . ILE A  1 897 ? 17.062  -13.640 10.474  1.00 42.01  ? 897  ILE A C   1 
ATOM   6869  O  O   . ILE A  1 897 ? 17.616  -14.646 10.914  1.00 41.91  ? 897  ILE A O   1 
ATOM   6870  C  CB  . ILE A  1 897 ? 16.149  -11.846 11.972  1.00 37.83  ? 897  ILE A CB  1 
ATOM   6871  C  CG1 . ILE A  1 897 ? 16.549  -10.652 12.842  1.00 34.50  ? 897  ILE A CG1 1 
ATOM   6872  C  CG2 . ILE A  1 897 ? 15.727  -12.983 12.851  1.00 38.25  ? 897  ILE A CG2 1 
ATOM   6873  C  CD1 . ILE A  1 897 ? 15.412  -10.105 13.662  1.00 29.37  ? 897  ILE A CD1 1 
ATOM   6874  N  N   . ILE A  1 898 ? 16.245  -13.670 9.429   1.00 38.98  ? 898  ILE A N   1 
ATOM   6875  C  CA  . ILE A  1 898 ? 15.948  -14.915 8.738   1.00 39.21  ? 898  ILE A CA  1 
ATOM   6876  C  C   . ILE A  1 898 ? 17.178  -15.525 8.062   1.00 37.84  ? 898  ILE A C   1 
ATOM   6877  O  O   . ILE A  1 898 ? 17.575  -16.631 8.388   1.00 45.56  ? 898  ILE A O   1 
ATOM   6878  C  CB  . ILE A  1 898 ? 14.856  -14.706 7.697   1.00 41.98  ? 898  ILE A CB  1 
ATOM   6879  C  CG1 . ILE A  1 898 ? 13.511  -14.454 8.391   1.00 44.49  ? 898  ILE A CG1 1 
ATOM   6880  C  CG2 . ILE A  1 898 ? 14.791  -15.899 6.777   1.00 40.74  ? 898  ILE A CG2 1 
ATOM   6881  C  CD1 . ILE A  1 898 ? 12.378  -14.126 7.441   1.00 47.08  ? 898  ILE A CD1 1 
ATOM   6882  N  N   . SER A  1 899 ? 17.795  -14.807 7.134   1.00 38.07  ? 899  SER A N   1 
ATOM   6883  C  CA  . SER A  1 899 ? 18.981  -15.314 6.465   1.00 40.11  ? 899  SER A CA  1 
ATOM   6884  C  C   . SER A  1 899 ? 20.141  -15.547 7.431   1.00 39.53  ? 899  SER A C   1 
ATOM   6885  O  O   . SER A  1 899 ? 20.913  -16.489 7.264   1.00 44.21  ? 899  SER A O   1 
ATOM   6886  C  CB  . SER A  1 899 ? 19.415  -14.359 5.359   1.00 38.59  ? 899  SER A CB  1 
ATOM   6887  O  OG  . SER A  1 899 ? 20.014  -13.212 5.917   1.00 46.55  ? 899  SER A OG  1 
ATOM   6888  N  N   . GLY A  1 900 ? 20.255  -14.703 8.447   1.00 39.11  ? 900  GLY A N   1 
ATOM   6889  C  CA  . GLY A  1 900 ? 21.360  -14.795 9.385   1.00 33.66  ? 900  GLY A CA  1 
ATOM   6890  C  C   . GLY A  1 900 ? 21.293  -16.036 10.234  1.00 36.56  ? 900  GLY A C   1 
ATOM   6891  O  O   . GLY A  1 900 ? 22.297  -16.517 10.727  1.00 42.26  ? 900  GLY A O   1 
ATOM   6892  N  N   . THR A  1 901 ? 20.106  -16.585 10.412  1.00 40.00  ? 901  THR A N   1 
ATOM   6893  C  CA  . THR A  1 901 ? 20.007  -17.735 11.292  1.00 38.37  ? 901  THR A CA  1 
ATOM   6894  C  C   . THR A  1 901 ? 19.876  -19.050 10.532  1.00 38.08  ? 901  THR A C   1 
ATOM   6895  O  O   . THR A  1 901 ? 19.983  -20.122 11.134  1.00 42.60  ? 901  THR A O   1 
ATOM   6896  C  CB  . THR A  1 901 ? 18.832  -17.576 12.284  1.00 42.55  ? 901  THR A CB  1 
ATOM   6897  O  OG1 . THR A  1 901 ? 17.588  -17.490 11.585  1.00 41.06  ? 901  THR A OG1 1 
ATOM   6898  C  CG2 . THR A  1 901 ? 19.020  -16.301 13.108  1.00 40.13  ? 901  THR A CG2 1 
ATOM   6899  N  N   . THR A  1 902 ? 19.708  -18.976 9.213   1.00 39.62  ? 902  THR A N   1 
ATOM   6900  C  CA  . THR A  1 902 ? 19.442  -20.171 8.402   1.00 39.85  ? 902  THR A CA  1 
ATOM   6901  C  C   . THR A  1 902 ? 20.405  -20.437 7.235   1.00 41.96  ? 902  THR A C   1 
ATOM   6902  O  O   . THR A  1 902 ? 20.654  -21.607 6.882   1.00 40.63  ? 902  THR A O   1 
ATOM   6903  C  CB  . THR A  1 902 ? 18.022  -20.114 7.787   1.00 41.14  ? 902  THR A CB  1 
ATOM   6904  O  OG1 . THR A  1 902 ? 17.852  -18.878 7.074   1.00 44.83  ? 902  THR A OG1 1 
ATOM   6905  C  CG2 . THR A  1 902 ? 16.979  -20.208 8.845   1.00 35.82  ? 902  THR A CG2 1 
ATOM   6906  N  N   . ALA A  1 903 ? 20.926  -19.375 6.616   1.00 37.98  ? 903  ALA A N   1 
ATOM   6907  C  CA  . ALA A  1 903 ? 21.613  -19.528 5.329   1.00 34.13  ? 903  ALA A CA  1 
ATOM   6908  C  C   . ALA A  1 903 ? 22.905  -20.319 5.444   1.00 32.60  ? 903  ALA A C   1 
ATOM   6909  O  O   . ALA A  1 903 ? 23.408  -20.829 4.456   1.00 36.66  ? 903  ALA A O   1 
ATOM   6910  C  CB  . ALA A  1 903 ? 21.891  -18.172 4.709   1.00 37.47  ? 903  ALA A CB  1 
ATOM   6911  N  N   . HIS A  1 904 ? 23.452  -20.426 6.644   1.00 30.58  ? 904  HIS A N   1 
ATOM   6912  C  CA  . HIS A  1 904 ? 24.693  -21.169 6.816   1.00 35.36  ? 904  HIS A CA  1 
ATOM   6913  C  C   . HIS A  1 904 ? 24.450  -22.693 6.957   1.00 36.99  ? 904  HIS A C   1 
ATOM   6914  O  O   . HIS A  1 904 ? 25.403  -23.479 6.918   1.00 36.45  ? 904  HIS A O   1 
ATOM   6915  C  CB  . HIS A  1 904 ? 25.478  -20.626 8.016   1.00 29.58  ? 904  HIS A CB  1 
ATOM   6916  C  CG  . HIS A  1 904 ? 24.666  -20.501 9.268   1.00 36.06  ? 904  HIS A CG  1 
ATOM   6917  N  ND1 . HIS A  1 904 ? 23.967  -19.361 9.590   1.00 40.90  ? 904  HIS A ND1 1 
ATOM   6918  C  CD2 . HIS A  1 904 ? 24.439  -21.377 10.275  1.00 43.81  ? 904  HIS A CD2 1 
ATOM   6919  C  CE1 . HIS A  1 904 ? 23.352  -19.534 10.746  1.00 40.89  ? 904  HIS A CE1 1 
ATOM   6920  N  NE2 . HIS A  1 904 ? 23.614  -20.754 11.178  1.00 42.73  ? 904  HIS A NE2 1 
ATOM   6921  N  N   . PHE A  1 905 ? 23.186  -23.101 7.078   1.00 32.04  ? 905  PHE A N   1 
ATOM   6922  C  CA  . PHE A  1 905 ? 22.835  -24.519 7.192   1.00 30.66  ? 905  PHE A CA  1 
ATOM   6923  C  C   . PHE A  1 905 ? 23.229  -25.300 5.933   1.00 34.50  ? 905  PHE A C   1 
ATOM   6924  O  O   . PHE A  1 905 ? 23.160  -24.776 4.811   1.00 30.32  ? 905  PHE A O   1 
ATOM   6925  C  CB  . PHE A  1 905 ? 21.336  -24.673 7.480   1.00 33.10  ? 905  PHE A CB  1 
ATOM   6926  C  CG  . PHE A  1 905 ? 20.949  -24.290 8.881   1.00 27.56  ? 905  PHE A CG  1 
ATOM   6927  C  CD1 . PHE A  1 905 ? 21.802  -24.546 9.941   1.00 28.83  ? 905  PHE A CD1 1 
ATOM   6928  C  CD2 . PHE A  1 905 ? 19.731  -23.698 9.138   1.00 28.25  ? 905  PHE A CD2 1 
ATOM   6929  C  CE1 . PHE A  1 905 ? 21.454  -24.202 11.235  1.00 35.12  ? 905  PHE A CE1 1 
ATOM   6930  C  CE2 . PHE A  1 905 ? 19.376  -23.348 10.431  1.00 34.40  ? 905  PHE A CE2 1 
ATOM   6931  C  CZ  . PHE A  1 905 ? 20.237  -23.598 11.480  1.00 29.93  ? 905  PHE A CZ  1 
ATOM   6932  N  N   . SER A  1 906 ? 23.656  -26.549 6.120   1.00 33.62  ? 906  SER A N   1 
ATOM   6933  C  CA  . SER A  1 906 ? 24.181  -27.344 5.015   1.00 29.33  ? 906  SER A CA  1 
ATOM   6934  C  C   . SER A  1 906 ? 23.841  -28.853 5.110   1.00 42.55  ? 906  SER A C   1 
ATOM   6935  O  O   . SER A  1 906 ? 24.490  -29.707 4.456   1.00 34.97  ? 906  SER A O   1 
ATOM   6936  C  CB  . SER A  1 906 ? 25.687  -27.175 4.964   1.00 30.26  ? 906  SER A CB  1 
ATOM   6937  O  OG  . SER A  1 906 ? 26.227  -27.675 6.179   1.00 39.52  ? 906  SER A OG  1 
ATOM   6938  N  N   . SER A  1 907 ? 22.850  -29.186 5.935   1.00 40.62  ? 907  SER A N   1 
ATOM   6939  C  CA  . SER A  1 907 ? 22.416  -30.571 6.070   1.00 39.30  ? 907  SER A CA  1 
ATOM   6940  C  C   . SER A  1 907 ? 20.970  -30.723 5.622   1.00 41.45  ? 907  SER A C   1 
ATOM   6941  O  O   . SER A  1 907 ? 20.176  -29.788 5.729   1.00 39.91  ? 907  SER A O   1 
ATOM   6942  C  CB  . SER A  1 907 ? 22.552  -31.037 7.506   1.00 40.51  ? 907  SER A CB  1 
ATOM   6943  O  OG  . SER A  1 907 ? 21.521  -30.459 8.285   1.00 46.00  ? 907  SER A OG  1 
ATOM   6944  N  N   . LYS A  1 908 ? 20.624  -31.912 5.139   1.00 45.32  ? 908  LYS A N   1 
ATOM   6945  C  CA  . LYS A  1 908 ? 19.251  -32.206 4.755   1.00 39.23  ? 908  LYS A CA  1 
ATOM   6946  C  C   . LYS A  1 908 ? 18.303  -32.023 5.939   1.00 39.23  ? 908  LYS A C   1 
ATOM   6947  O  O   . LYS A  1 908 ? 17.192  -31.521 5.775   1.00 38.51  ? 908  LYS A O   1 
ATOM   6948  C  CB  . LYS A  1 908 ? 19.150  -33.625 4.215   1.00 48.07  ? 908  LYS A CB  1 
ATOM   6949  C  CG  . LYS A  1 908 ? 20.128  -33.936 3.110   1.00 48.97  ? 908  LYS A CG  1 
ATOM   6950  C  CD  . LYS A  1 908 ? 19.450  -33.967 1.761   1.00 53.44  ? 908  LYS A CD  1 
ATOM   6951  C  CE  . LYS A  1 908 ? 19.703  -35.291 1.074   1.00 45.07  ? 908  LYS A CE  1 
ATOM   6952  N  NZ  . LYS A  1 908 ? 19.156  -36.417 1.903   1.00 62.25  ? 908  LYS A NZ  1 
ATOM   6953  N  N   . ASP A  1 909 ? 18.746  -32.433 7.127   1.00 38.78  ? 909  ASP A N   1 
ATOM   6954  C  CA  . ASP A  1 909 ? 18.020  -32.162 8.371   1.00 44.09  ? 909  ASP A CA  1 
ATOM   6955  C  C   . ASP A  1 909 ? 17.548  -30.710 8.507   1.00 46.04  ? 909  ASP A C   1 
ATOM   6956  O  O   . ASP A  1 909 ? 16.350  -30.427 8.646   1.00 42.40  ? 909  ASP A O   1 
ATOM   6957  C  CB  . ASP A  1 909 ? 18.900  -32.502 9.572   1.00 44.48  ? 909  ASP A CB  1 
ATOM   6958  C  CG  . ASP A  1 909 ? 18.707  -33.923 10.056  1.00 63.67  ? 909  ASP A CG  1 
ATOM   6959  O  OD1 . ASP A  1 909 ? 18.203  -34.764 9.270   1.00 65.20  ? 909  ASP A OD1 1 
ATOM   6960  O  OD2 . ASP A  1 909 ? 19.059  -34.203 11.227  1.00 66.56  ? 909  ASP A OD2 1 
ATOM   6961  N  N   . LYS A  1 910 ? 18.506  -29.791 8.474   1.00 42.39  ? 910  LYS A N   1 
ATOM   6962  C  CA  . LYS A  1 910 ? 18.186  -28.389 8.635   1.00 43.27  ? 910  LYS A CA  1 
ATOM   6963  C  C   . LYS A  1 910 ? 17.320  -27.895 7.482   1.00 40.57  ? 910  LYS A C   1 
ATOM   6964  O  O   . LYS A  1 910 ? 16.383  -27.116 7.693   1.00 42.57  ? 910  LYS A O   1 
ATOM   6965  C  CB  . LYS A  1 910 ? 19.459  -27.555 8.753   1.00 38.51  ? 910  LYS A CB  1 
ATOM   6966  C  CG  . LYS A  1 910 ? 20.269  -27.830 10.006  1.00 40.42  ? 910  LYS A CG  1 
ATOM   6967  C  CD  . LYS A  1 910 ? 19.585  -27.346 11.274  1.00 42.75  ? 910  LYS A CD  1 
ATOM   6968  C  CE  . LYS A  1 910 ? 20.407  -27.773 12.483  1.00 46.35  ? 910  LYS A CE  1 
ATOM   6969  N  NZ  . LYS A  1 910 ? 19.565  -27.944 13.699  1.00 54.97  ? 910  LYS A NZ  1 
ATOM   6970  N  N   . LEU A  1 911 ? 17.612  -28.349 6.270   1.00 35.80  ? 911  LEU A N   1 
ATOM   6971  C  CA  . LEU A  1 911 ? 16.767  -27.974 5.132   1.00 42.46  ? 911  LEU A CA  1 
ATOM   6972  C  C   . LEU A  1 911 ? 15.283  -28.210 5.429   1.00 47.73  ? 911  LEU A C   1 
ATOM   6973  O  O   . LEU A  1 911 ? 14.441  -27.335 5.205   1.00 45.60  ? 911  LEU A O   1 
ATOM   6974  C  CB  . LEU A  1 911 ? 17.160  -28.748 3.885   1.00 36.17  ? 911  LEU A CB  1 
ATOM   6975  C  CG  . LEU A  1 911 ? 16.305  -28.398 2.665   1.00 44.66  ? 911  LEU A CG  1 
ATOM   6976  C  CD1 . LEU A  1 911 ? 16.230  -26.884 2.420   1.00 38.97  ? 911  LEU A CD1 1 
ATOM   6977  C  CD2 . LEU A  1 911 ? 16.822  -29.113 1.428   1.00 36.18  ? 911  LEU A CD2 1 
ATOM   6978  N  N   . GLN A  1 912 ? 14.999  -29.401 5.954   1.00 48.50  ? 912  GLN A N   1 
ATOM   6979  C  CA  . GLN A  1 912 ? 13.665  -29.816 6.346   1.00 46.79  ? 912  GLN A CA  1 
ATOM   6980  C  C   . GLN A  1 912 ? 13.031  -28.790 7.284   1.00 46.28  ? 912  GLN A C   1 
ATOM   6981  O  O   . GLN A  1 912 ? 11.967  -28.237 6.989   1.00 44.61  ? 912  GLN A O   1 
ATOM   6982  C  CB  . GLN A  1 912 ? 13.746  -31.185 7.022   1.00 47.62  ? 912  GLN A CB  1 
ATOM   6983  C  CG  . GLN A  1 912 ? 12.620  -32.154 6.760   1.00 48.18  ? 912  GLN A CG  1 
ATOM   6984  C  CD  . GLN A  1 912 ? 12.810  -33.469 7.547   1.00 57.91  ? 912  GLN A CD  1 
ATOM   6985  O  OE1 . GLN A  1 912 ? 12.314  -33.610 8.667   1.00 66.95  ? 912  GLN A OE1 1 
ATOM   6986  N  NE2 . GLN A  1 912 ? 13.537  -34.421 6.964   1.00 49.93  ? 912  GLN A NE2 1 
ATOM   6987  N  N   . GLU A  1 913 ? 13.693  -28.543 8.413   1.00 45.32  ? 913  GLU A N   1 
ATOM   6988  C  CA  . GLU A  1 913 ? 13.176  -27.620 9.427   1.00 45.06  ? 913  GLU A CA  1 
ATOM   6989  C  C   . GLU A  1 913 ? 12.885  -26.248 8.861   1.00 45.30  ? 913  GLU A C   1 
ATOM   6990  O  O   . GLU A  1 913 ? 11.906  -25.603 9.237   1.00 50.31  ? 913  GLU A O   1 
ATOM   6991  C  CB  . GLU A  1 913 ? 14.160  -27.477 10.580  1.00 43.64  ? 913  GLU A CB  1 
ATOM   6992  C  CG  . GLU A  1 913 ? 14.873  -28.757 10.966  1.00 45.20  ? 913  GLU A CG  1 
ATOM   6993  C  CD  . GLU A  1 913 ? 15.694  -28.577 12.231  1.00 55.57  ? 913  GLU A CD  1 
ATOM   6994  O  OE1 . GLU A  1 913 ? 15.512  -27.534 12.898  1.00 51.83  ? 913  GLU A OE1 1 
ATOM   6995  O  OE2 . GLU A  1 913 ? 16.517  -29.466 12.560  1.00 66.06  ? 913  GLU A OE2 1 
ATOM   6996  N  N   . VAL A  1 914 ? 13.737  -25.804 7.948   1.00 44.64  ? 914  VAL A N   1 
ATOM   6997  C  CA  . VAL A  1 914 ? 13.615  -24.461 7.427   1.00 48.06  ? 914  VAL A CA  1 
ATOM   6998  C  C   . VAL A  1 914 ? 12.512  -24.427 6.379   1.00 46.93  ? 914  VAL A C   1 
ATOM   6999  O  O   . VAL A  1 914 ? 11.808  -23.427 6.229   1.00 53.33  ? 914  VAL A O   1 
ATOM   7000  C  CB  . VAL A  1 914 ? 14.961  -23.956 6.848   1.00 43.33  ? 914  VAL A CB  1 
ATOM   7001  C  CG1 . VAL A  1 914 ? 14.796  -22.597 6.257   1.00 38.63  ? 914  VAL A CG1 1 
ATOM   7002  C  CG2 . VAL A  1 914 ? 16.011  -23.894 7.944   1.00 41.27  ? 914  VAL A CG2 1 
ATOM   7003  N  N   . LYS A  1 915 ? 12.337  -25.526 5.665   1.00 45.52  ? 915  LYS A N   1 
ATOM   7004  C  CA  . LYS A  1 915 ? 11.256  -25.581 4.688   1.00 54.02  ? 915  LYS A CA  1 
ATOM   7005  C  C   . LYS A  1 915 ? 9.937   -25.525 5.463   1.00 49.94  ? 915  LYS A C   1 
ATOM   7006  O  O   . LYS A  1 915 ? 9.008   -24.812 5.093   1.00 50.70  ? 915  LYS A O   1 
ATOM   7007  C  CB  . LYS A  1 915 ? 11.354  -26.837 3.809   1.00 46.02  ? 915  LYS A CB  1 
ATOM   7008  C  CG  . LYS A  1 915 ? 10.678  -26.685 2.460   1.00 51.57  ? 915  LYS A CG  1 
ATOM   7009  C  CD  . LYS A  1 915 ? 10.679  -27.999 1.662   1.00 66.47  ? 915  LYS A CD  1 
ATOM   7010  C  CE  . LYS A  1 915 ? 12.094  -28.436 1.243   1.00 72.19  ? 915  LYS A CE  1 
ATOM   7011  N  NZ  . LYS A  1 915 ? 12.153  -29.754 0.502   1.00 64.64  ? 915  LYS A NZ  1 
ATOM   7012  N  N   . LEU A  1 916 ? 9.903   -26.244 6.576   1.00 47.39  ? 916  LEU A N   1 
ATOM   7013  C  CA  . LEU A  1 916 ? 8.737   -26.307 7.444   1.00 52.25  ? 916  LEU A CA  1 
ATOM   7014  C  C   . LEU A  1 916 ? 8.413   -24.978 8.115   1.00 52.91  ? 916  LEU A C   1 
ATOM   7015  O  O   . LEU A  1 916 ? 7.249   -24.614 8.293   1.00 54.01  ? 916  LEU A O   1 
ATOM   7016  C  CB  . LEU A  1 916 ? 8.963   -27.357 8.518   1.00 55.13  ? 916  LEU A CB  1 
ATOM   7017  C  CG  . LEU A  1 916 ? 7.665   -27.980 8.996   1.00 64.44  ? 916  LEU A CG  1 
ATOM   7018  C  CD1 . LEU A  1 916 ? 7.175   -28.926 7.913   1.00 52.46  ? 916  LEU A CD1 1 
ATOM   7019  C  CD2 . LEU A  1 916 ? 7.860   -28.683 10.341  1.00 62.83  ? 916  LEU A CD2 1 
ATOM   7020  N  N   . PHE A  1 917 ? 9.453   -24.257 8.507   1.00 53.72  ? 917  PHE A N   1 
ATOM   7021  C  CA  . PHE A  1 917 ? 9.264   -22.956 9.127   1.00 53.17  ? 917  PHE A CA  1 
ATOM   7022  C  C   . PHE A  1 917 ? 8.740   -21.923 8.121   1.00 50.35  ? 917  PHE A C   1 
ATOM   7023  O  O   . PHE A  1 917 ? 7.853   -21.142 8.433   1.00 51.85  ? 917  PHE A O   1 
ATOM   7024  C  CB  . PHE A  1 917 ? 10.575  -22.487 9.762   1.00 52.26  ? 917  PHE A CB  1 
ATOM   7025  C  CG  . PHE A  1 917 ? 10.459  -21.187 10.499  1.00 52.27  ? 917  PHE A CG  1 
ATOM   7026  C  CD1 . PHE A  1 917 ? 9.640   -21.084 11.616  1.00 49.84  ? 917  PHE A CD1 1 
ATOM   7027  C  CD2 . PHE A  1 917 ? 11.179  -20.066 10.080  1.00 47.75  ? 917  PHE A CD2 1 
ATOM   7028  C  CE1 . PHE A  1 917 ? 9.524   -19.880 12.294  1.00 56.17  ? 917  PHE A CE1 1 
ATOM   7029  C  CE2 . PHE A  1 917 ? 11.077  -18.864 10.761  1.00 46.36  ? 917  PHE A CE2 1 
ATOM   7030  C  CZ  . PHE A  1 917 ? 10.251  -18.766 11.864  1.00 51.25  ? 917  PHE A CZ  1 
ATOM   7031  N  N   . PHE A  1 918 ? 9.271   -21.924 6.907   1.00 50.64  ? 918  PHE A N   1 
ATOM   7032  C  CA  . PHE A  1 918 ? 8.786   -20.968 5.916   1.00 55.61  ? 918  PHE A CA  1 
ATOM   7033  C  C   . PHE A  1 918 ? 7.357   -21.299 5.490   1.00 57.97  ? 918  PHE A C   1 
ATOM   7034  O  O   . PHE A  1 918 ? 6.521   -20.406 5.372   1.00 59.08  ? 918  PHE A O   1 
ATOM   7035  C  CB  . PHE A  1 918 ? 9.700   -20.926 4.689   1.00 52.36  ? 918  PHE A CB  1 
ATOM   7036  C  CG  . PHE A  1 918 ? 11.071  -20.380 4.967   1.00 46.63  ? 918  PHE A CG  1 
ATOM   7037  C  CD1 . PHE A  1 918 ? 11.332  -19.678 6.126   1.00 47.65  ? 918  PHE A CD1 1 
ATOM   7038  C  CD2 . PHE A  1 918 ? 12.100  -20.577 4.067   1.00 43.52  ? 918  PHE A CD2 1 
ATOM   7039  C  CE1 . PHE A  1 918 ? 12.600  -19.188 6.378   1.00 45.30  ? 918  PHE A CE1 1 
ATOM   7040  C  CE2 . PHE A  1 918 ? 13.355  -20.082 4.313   1.00 40.97  ? 918  PHE A CE2 1 
ATOM   7041  C  CZ  . PHE A  1 918 ? 13.604  -19.383 5.467   1.00 39.72  ? 918  PHE A CZ  1 
ATOM   7042  N  N   . GLU A  1 919 ? 7.081   -22.579 5.252   1.00 62.24  ? 919  GLU A N   1 
ATOM   7043  C  CA  . GLU A  1 919 ? 5.724   -23.020 4.915   1.00 61.37  ? 919  GLU A CA  1 
ATOM   7044  C  C   . GLU A  1 919 ? 4.737   -22.563 5.972   1.00 60.20  ? 919  GLU A C   1 
ATOM   7045  O  O   . GLU A  1 919 ? 3.597   -22.230 5.667   1.00 61.84  ? 919  GLU A O   1 
ATOM   7046  C  CB  . GLU A  1 919 ? 5.654   -24.538 4.782   1.00 57.72  ? 919  GLU A CB  1 
ATOM   7047  C  CG  . GLU A  1 919 ? 6.234   -25.105 3.498   1.00 62.88  ? 919  GLU A CG  1 
ATOM   7048  C  CD  . GLU A  1 919 ? 6.464   -26.601 3.612   1.00 66.97  ? 919  GLU A CD  1 
ATOM   7049  O  OE1 . GLU A  1 919 ? 6.237   -27.144 4.720   1.00 62.12  ? 919  GLU A OE1 1 
ATOM   7050  O  OE2 . GLU A  1 919 ? 6.871   -27.231 2.608   1.00 75.51  ? 919  GLU A OE2 1 
ATOM   7051  N  N   . SER A  1 920 ? 5.201   -22.541 7.217   1.00 55.57  ? 920  SER A N   1 
ATOM   7052  C  CA  . SER A  1 920 ? 4.386   -22.117 8.330   1.00 54.45  ? 920  SER A CA  1 
ATOM   7053  C  C   . SER A  1 920 ? 4.195   -20.613 8.364   1.00 60.65  ? 920  SER A C   1 
ATOM   7054  O  O   . SER A  1 920 ? 3.127   -20.135 8.740   1.00 67.31  ? 920  SER A O   1 
ATOM   7055  C  CB  . SER A  1 920 ? 5.005   -22.595 9.646   1.00 56.66  ? 920  SER A CB  1 
ATOM   7056  O  OG  . SER A  1 920 ? 4.433   -21.904 10.739  1.00 61.26  ? 920  SER A OG  1 
ATOM   7057  N  N   . LEU A  1 921 ? 5.225   -19.853 8.002   1.00 59.17  ? 921  LEU A N   1 
ATOM   7058  C  CA  . LEU A  1 921 ? 5.079   -18.400 8.005   1.00 60.69  ? 921  LEU A CA  1 
ATOM   7059  C  C   . LEU A  1 921 ? 4.099   -18.007 6.917   1.00 64.49  ? 921  LEU A C   1 
ATOM   7060  O  O   . LEU A  1 921 ? 3.365   -17.046 7.073   1.00 65.23  ? 921  LEU A O   1 
ATOM   7061  C  CB  . LEU A  1 921 ? 6.413   -17.677 7.807   1.00 53.66  ? 921  LEU A CB  1 
ATOM   7062  C  CG  . LEU A  1 921 ? 7.438   -17.902 8.910   1.00 48.80  ? 921  LEU A CG  1 
ATOM   7063  C  CD1 . LEU A  1 921 ? 8.597   -16.948 8.764   1.00 42.81  ? 921  LEU A CD1 1 
ATOM   7064  C  CD2 . LEU A  1 921 ? 6.788   -17.778 10.267  1.00 49.89  ? 921  LEU A CD2 1 
ATOM   7065  N  N   . GLU A  1 922 ? 4.099   -18.745 5.813   1.00 62.85  ? 922  GLU A N   1 
ATOM   7066  C  CA  . GLU A  1 922 ? 3.017   -18.646 4.840   1.00 70.63  ? 922  GLU A CA  1 
ATOM   7067  C  C   . GLU A  1 922 ? 1.760   -19.161 5.545   1.00 75.54  ? 922  GLU A C   1 
ATOM   7068  O  O   . GLU A  1 922 ? 1.777   -20.274 6.076   1.00 76.87  ? 922  GLU A O   1 
ATOM   7069  C  CB  . GLU A  1 922 ? 3.324   -19.462 3.583   1.00 65.62  ? 922  GLU A CB  1 
ATOM   7070  C  CG  . GLU A  1 922 ? 4.718   -19.251 3.002   1.00 62.79  ? 922  GLU A CG  1 
ATOM   7071  C  CD  . GLU A  1 922 ? 4.780   -18.162 1.933   1.00 70.45  ? 922  GLU A CD  1 
ATOM   7072  O  OE1 . GLU A  1 922 ? 3.987   -17.191 2.005   1.00 70.07  ? 922  GLU A OE1 1 
ATOM   7073  O  OE2 . GLU A  1 922 ? 5.634   -18.286 1.021   1.00 62.45  ? 922  GLU A OE2 1 
ATOM   7074  N  N   . ALA A  1 923 ? 0.687   -18.367 5.549   1.00 77.46  ? 923  ALA A N   1 
ATOM   7075  C  CA  . ALA A  1 923 ? -0.447  -18.556 6.476   1.00 73.80  ? 923  ALA A CA  1 
ATOM   7076  C  C   . ALA A  1 923 ? 0.082   -18.431 7.896   1.00 67.93  ? 923  ALA A C   1 
ATOM   7077  O  O   . ALA A  1 923 ? 0.480   -19.426 8.482   1.00 77.43  ? 923  ALA A O   1 
ATOM   7078  C  CB  . ALA A  1 923 ? -1.146  -19.893 6.263   1.00 80.70  ? 923  ALA A CB  1 
ATOM   7079  N  N   . GLN A  1 924 ? 0.113   -17.226 8.465   1.00 73.13  ? 924  GLN A N   1 
ATOM   7080  C  CA  . GLN A  1 924 ? -0.400  -15.983 7.878   1.00 74.11  ? 924  GLN A CA  1 
ATOM   7081  C  C   . GLN A  1 924 ? 0.214   -15.585 6.532   1.00 74.48  ? 924  GLN A C   1 
ATOM   7082  O  O   . GLN A  1 924 ? 1.234   -16.125 6.116   1.00 75.79  ? 924  GLN A O   1 
ATOM   7083  C  CB  . GLN A  1 924 ? -0.180  -14.843 8.876   1.00 70.40  ? 924  GLN A CB  1 
ATOM   7084  C  CG  . GLN A  1 924 ? -0.930  -13.552 8.578   1.00 75.59  ? 924  GLN A CG  1 
ATOM   7085  C  CD  . GLN A  1 924 ? -0.111  -12.324 8.913   1.00 80.69  ? 924  GLN A CD  1 
ATOM   7086  O  OE1 . GLN A  1 924 ? 0.138   -12.036 10.084  1.00 91.41  ? 924  GLN A OE1 1 
ATOM   7087  N  NE2 . GLN A  1 924 ? 0.325   -11.597 7.885   1.00 70.33  ? 924  GLN A NE2 1 
ATOM   7088  N  N   . GLY A  1 925 ? -0.431  -14.667 5.827   1.00 80.17  ? 925  GLY A N   1 
ATOM   7089  C  CA  . GLY A  1 925 ? 0.145   -14.097 4.626   1.00 73.70  ? 925  GLY A CA  1 
ATOM   7090  C  C   . GLY A  1 925 ? 1.471   -13.417 4.906   1.00 71.85  ? 925  GLY A C   1 
ATOM   7091  O  O   . GLY A  1 925 ? 1.600   -12.189 4.763   1.00 69.54  ? 925  GLY A O   1 
ATOM   7092  N  N   . SER A  1 926 ? 2.449   -14.219 5.327   1.00 68.05  ? 926  SER A N   1 
ATOM   7093  C  CA  . SER A  1 926 ? 3.827   -13.773 5.443   1.00 64.15  ? 926  SER A CA  1 
ATOM   7094  C  C   . SER A  1 926 ? 4.618   -14.338 4.277   1.00 62.16  ? 926  SER A C   1 
ATOM   7095  O  O   . SER A  1 926 ? 5.037   -15.499 4.302   1.00 63.79  ? 926  SER A O   1 
ATOM   7096  C  CB  . SER A  1 926 ? 4.449   -14.202 6.769   1.00 62.26  ? 926  SER A CB  1 
ATOM   7097  O  OG  . SER A  1 926 ? 3.844   -13.537 7.858   1.00 69.56  ? 926  SER A OG  1 
ATOM   7098  N  N   . HIS A  1 927 ? 4.787   -13.524 3.240   1.00 58.69  ? 927  HIS A N   1 
ATOM   7099  C  CA  . HIS A  1 927 ? 5.607   -13.918 2.114   1.00 53.95  ? 927  HIS A CA  1 
ATOM   7100  C  C   . HIS A  1 927 ? 6.806   -12.999 1.959   1.00 55.03  ? 927  HIS A C   1 
ATOM   7101  O  O   . HIS A  1 927 ? 6.675   -11.776 1.981   1.00 53.66  ? 927  HIS A O   1 
ATOM   7102  C  CB  . HIS A  1 927 ? 4.806   -13.919 0.821   1.00 52.53  ? 927  HIS A CB  1 
ATOM   7103  C  CG  . HIS A  1 927 ? 5.638   -14.215 -0.388  1.00 57.80  ? 927  HIS A CG  1 
ATOM   7104  N  ND1 . HIS A  1 927 ? 6.143   -15.471 -0.657  1.00 60.38  ? 927  HIS A ND1 1 
ATOM   7105  C  CD2 . HIS A  1 927 ? 6.085   -13.411 -1.382  1.00 56.77  ? 927  HIS A CD2 1 
ATOM   7106  C  CE1 . HIS A  1 927 ? 6.842   -15.433 -1.777  1.00 55.29  ? 927  HIS A CE1 1 
ATOM   7107  N  NE2 . HIS A  1 927 ? 6.822   -14.195 -2.237  1.00 57.12  ? 927  HIS A NE2 1 
ATOM   7108  N  N   . LEU A  1 928 ? 7.975   -13.606 1.808   1.00 48.69  ? 928  LEU A N   1 
ATOM   7109  C  CA  . LEU A  1 928 ? 9.170   -12.884 1.419   1.00 49.24  ? 928  LEU A CA  1 
ATOM   7110  C  C   . LEU A  1 928 ? 9.903   -13.670 0.341   1.00 44.94  ? 928  LEU A C   1 
ATOM   7111  O  O   . LEU A  1 928 ? 9.880   -14.901 0.330   1.00 42.37  ? 928  LEU A O   1 
ATOM   7112  C  CB  . LEU A  1 928 ? 10.092  -12.655 2.614   1.00 41.65  ? 928  LEU A CB  1 
ATOM   7113  C  CG  . LEU A  1 928 ? 9.566   -11.808 3.762   1.00 43.01  ? 928  LEU A CG  1 
ATOM   7114  C  CD1 . LEU A  1 928 ? 10.608  -11.770 4.841   1.00 41.05  ? 928  LEU A CD1 1 
ATOM   7115  C  CD2 . LEU A  1 928 ? 9.202   -10.387 3.318   1.00 45.61  ? 928  LEU A CD2 1 
ATOM   7116  N  N   . ASP A  1 929 ? 10.559  -12.951 -0.558  1.00 43.45  ? 929  ASP A N   1 
ATOM   7117  C  CA  . ASP A  1 929 ? 11.413  -13.584 -1.535  1.00 42.95  ? 929  ASP A CA  1 
ATOM   7118  C  C   . ASP A  1 929 ? 12.569  -14.291 -0.833  1.00 45.78  ? 929  ASP A C   1 
ATOM   7119  O  O   . ASP A  1 929 ? 13.135  -15.248 -1.357  1.00 42.38  ? 929  ASP A O   1 
ATOM   7120  C  CB  . ASP A  1 929 ? 11.948  -12.560 -2.531  1.00 47.45  ? 929  ASP A CB  1 
ATOM   7121  C  CG  . ASP A  1 929 ? 10.874  -12.026 -3.443  1.00 53.34  ? 929  ASP A CG  1 
ATOM   7122  O  OD1 . ASP A  1 929 ? 9.827   -12.694 -3.536  1.00 47.85  ? 929  ASP A OD1 1 
ATOM   7123  O  OD2 . ASP A  1 929 ? 11.080  -10.951 -4.065  1.00 59.23  ? 929  ASP A OD2 1 
ATOM   7124  N  N   . ILE A  1 930 ? 12.926  -13.815 0.356   1.00 42.63  ? 930  ILE A N   1 
ATOM   7125  C  CA  . ILE A  1 930 ? 14.099  -14.340 1.035   1.00 38.55  ? 930  ILE A CA  1 
ATOM   7126  C  C   . ILE A  1 930 ? 13.869  -15.808 1.468   1.00 43.13  ? 930  ILE A C   1 
ATOM   7127  O  O   . ILE A  1 930 ? 14.823  -16.537 1.741   1.00 40.39  ? 930  ILE A O   1 
ATOM   7128  C  CB  . ILE A  1 930 ? 14.477  -13.458 2.248   1.00 38.37  ? 930  ILE A CB  1 
ATOM   7129  C  CG1 . ILE A  1 930 ? 15.886  -13.769 2.771   1.00 38.12  ? 930  ILE A CG1 1 
ATOM   7130  C  CG2 . ILE A  1 930 ? 13.479  -13.634 3.367   1.00 43.27  ? 930  ILE A CG2 1 
ATOM   7131  C  CD1 . ILE A  1 930 ? 16.964  -13.803 1.731   1.00 36.78  ? 930  ILE A CD1 1 
ATOM   7132  N  N   . PHE A  1 931 ? 12.616  -16.257 1.512   1.00 41.24  ? 931  PHE A N   1 
ATOM   7133  C  CA  . PHE A  1 931 ? 12.364  -17.671 1.823   1.00 41.82  ? 931  PHE A CA  1 
ATOM   7134  C  C   . PHE A  1 931 ? 12.972  -18.596 0.770   1.00 41.44  ? 931  PHE A C   1 
ATOM   7135  O  O   . PHE A  1 931 ? 13.682  -19.555 1.095   1.00 41.89  ? 931  PHE A O   1 
ATOM   7136  C  CB  . PHE A  1 931 ? 10.879  -17.962 1.921   1.00 38.52  ? 931  PHE A CB  1 
ATOM   7137  C  CG  . PHE A  1 931 ? 10.197  -17.234 3.006   1.00 44.57  ? 931  PHE A CG  1 
ATOM   7138  C  CD1 . PHE A  1 931 ? 10.920  -16.651 4.030   1.00 43.24  ? 931  PHE A CD1 1 
ATOM   7139  C  CD2 . PHE A  1 931 ? 8.812   -17.143 3.018   1.00 48.84  ? 931  PHE A CD2 1 
ATOM   7140  C  CE1 . PHE A  1 931 ? 10.274  -15.982 5.037   1.00 43.48  ? 931  PHE A CE1 1 
ATOM   7141  C  CE2 . PHE A  1 931 ? 8.166   -16.479 4.024   1.00 48.47  ? 931  PHE A CE2 1 
ATOM   7142  C  CZ  . PHE A  1 931 ? 8.894   -15.896 5.032   1.00 43.34  ? 931  PHE A CZ  1 
ATOM   7143  N  N   . GLN A  1 932 ? 12.668  -18.308 -0.491  1.00 40.00  ? 932  GLN A N   1 
ATOM   7144  C  CA  . GLN A  1 932 ? 13.170  -19.106 -1.601  1.00 45.25  ? 932  GLN A CA  1 
ATOM   7145  C  C   . GLN A  1 932 ? 14.673  -19.025 -1.638  1.00 42.66  ? 932  GLN A C   1 
ATOM   7146  O  O   . GLN A  1 932 ? 15.356  -20.025 -1.846  1.00 37.13  ? 932  GLN A O   1 
ATOM   7147  C  CB  . GLN A  1 932 ? 12.581  -18.625 -2.939  1.00 38.61  ? 932  GLN A CB  1 
ATOM   7148  C  CG  . GLN A  1 932 ? 12.552  -19.669 -4.041  1.00 39.92  ? 932  GLN A CG  1 
ATOM   7149  C  CD  . GLN A  1 932 ? 12.081  -21.040 -3.552  1.00 56.19  ? 932  GLN A CD  1 
ATOM   7150  O  OE1 . GLN A  1 932 ? 12.671  -22.073 -3.908  1.00 53.85  ? 932  GLN A OE1 1 
ATOM   7151  N  NE2 . GLN A  1 932 ? 11.018  -21.059 -2.734  1.00 52.71  ? 932  GLN A NE2 1 
ATOM   7152  N  N   . THR A  1 933 ? 15.178  -17.820 -1.406  1.00 37.65  ? 933  THR A N   1 
ATOM   7153  C  CA  . THR A  1 933 ? 16.597  -17.564 -1.525  1.00 36.52  ? 933  THR A CA  1 
ATOM   7154  C  C   . THR A  1 933 ? 17.349  -18.393 -0.500  1.00 32.87  ? 933  THR A C   1 
ATOM   7155  O  O   . THR A  1 933 ? 18.411  -18.917 -0.791  1.00 33.38  ? 933  THR A O   1 
ATOM   7156  C  CB  . THR A  1 933 ? 16.892  -16.039 -1.377  1.00 32.09  ? 933  THR A CB  1 
ATOM   7157  O  OG1 . THR A  1 933 ? 16.492  -15.397 -2.585  1.00 39.11  ? 933  THR A OG1 1 
ATOM   7158  C  CG2 . THR A  1 933 ? 18.358  -15.756 -1.180  1.00 18.86  ? 933  THR A CG2 1 
ATOM   7159  N  N   . VAL A  1 934 ? 16.774  -18.532 0.686   1.00 30.04  ? 934  VAL A N   1 
ATOM   7160  C  CA  . VAL A  1 934 ? 17.423  -19.242 1.762   1.00 31.14  ? 934  VAL A CA  1 
ATOM   7161  C  C   . VAL A  1 934 ? 17.448  -20.729 1.429   1.00 37.73  ? 934  VAL A C   1 
ATOM   7162  O  O   . VAL A  1 934 ? 18.503  -21.383 1.517   1.00 35.83  ? 934  VAL A O   1 
ATOM   7163  C  CB  . VAL A  1 934 ? 16.714  -18.993 3.108   1.00 42.02  ? 934  VAL A CB  1 
ATOM   7164  C  CG1 . VAL A  1 934 ? 16.925  -20.172 4.085   1.00 33.48  ? 934  VAL A CG1 1 
ATOM   7165  C  CG2 . VAL A  1 934 ? 17.158  -17.653 3.704   1.00 36.98  ? 934  VAL A CG2 1 
ATOM   7166  N  N   . LEU A  1 935 ? 16.293  -21.243 1.008   1.00 35.74  ? 935  LEU A N   1 
ATOM   7167  C  CA  . LEU A  1 935 ? 16.154  -22.660 0.647   1.00 36.46  ? 935  LEU A CA  1 
ATOM   7168  C  C   . LEU A  1 935 ? 17.099  -23.075 -0.471  1.00 34.14  ? 935  LEU A C   1 
ATOM   7169  O  O   . LEU A  1 935 ? 17.758  -24.107 -0.381  1.00 36.92  ? 935  LEU A O   1 
ATOM   7170  C  CB  . LEU A  1 935 ? 14.706  -22.973 0.263   1.00 39.42  ? 935  LEU A CB  1 
ATOM   7171  C  CG  . LEU A  1 935 ? 13.738  -22.860 1.452   1.00 40.32  ? 935  LEU A CG  1 
ATOM   7172  C  CD1 . LEU A  1 935 ? 12.299  -23.039 1.018   1.00 36.04  ? 935  LEU A CD1 1 
ATOM   7173  C  CD2 . LEU A  1 935 ? 14.114  -23.843 2.589   1.00 37.49  ? 935  LEU A CD2 1 
ATOM   7174  N  N   . GLU A  1 936 ? 17.194  -22.259 -1.511  1.00 36.55  ? 936  GLU A N   1 
ATOM   7175  C  CA  . GLU A  1 936 ? 18.138  -22.530 -2.589  1.00 31.88  ? 936  GLU A CA  1 
ATOM   7176  C  C   . GLU A  1 936 ? 19.583  -22.429 -2.115  1.00 38.29  ? 936  GLU A C   1 
ATOM   7177  O  O   . GLU A  1 936 ? 20.448  -23.160 -2.608  1.00 38.49  ? 936  GLU A O   1 
ATOM   7178  C  CB  . GLU A  1 936 ? 17.882  -21.594 -3.764  1.00 34.03  ? 936  GLU A CB  1 
ATOM   7179  C  CG  . GLU A  1 936 ? 16.441  -21.743 -4.283  1.00 47.57  ? 936  GLU A CG  1 
ATOM   7180  C  CD  . GLU A  1 936 ? 16.195  -21.074 -5.622  1.00 53.55  ? 936  GLU A CD  1 
ATOM   7181  O  OE1 . GLU A  1 936 ? 17.181  -20.882 -6.362  1.00 58.57  ? 936  GLU A OE1 1 
ATOM   7182  O  OE2 . GLU A  1 936 ? 15.015  -20.757 -5.933  1.00 55.83  ? 936  GLU A OE2 1 
ATOM   7183  N  N   . THR A  1 937 ? 19.837  -21.562 -1.138  1.00 33.17  ? 937  THR A N   1 
ATOM   7184  C  CA  . THR A  1 937 ? 21.174  -21.417 -0.579  1.00 32.39  ? 937  THR A CA  1 
ATOM   7185  C  C   . THR A  1 937 ? 21.575  -22.654 0.237   1.00 35.56  ? 937  THR A C   1 
ATOM   7186  O  O   . THR A  1 937 ? 22.709  -23.150 0.131   1.00 35.29  ? 937  THR A O   1 
ATOM   7187  C  CB  . THR A  1 937 ? 21.265  -20.136 0.310   1.00 31.40  ? 937  THR A CB  1 
ATOM   7188  O  OG1 . THR A  1 937 ? 21.136  -18.991 -0.520  1.00 40.43  ? 937  THR A OG1 1 
ATOM   7189  C  CG2 . THR A  1 937 ? 22.582  -20.038 1.026   1.00 28.30  ? 937  THR A CG2 1 
ATOM   7190  N  N   . ILE A  1 938 ? 20.653  -23.129 1.071   1.00 30.79  ? 938  ILE A N   1 
ATOM   7191  C  CA  . ILE A  1 938 ? 20.897  -24.316 1.874   1.00 33.28  ? 938  ILE A CA  1 
ATOM   7192  C  C   . ILE A  1 938 ? 21.069  -25.532 0.972   1.00 35.08  ? 938  ILE A C   1 
ATOM   7193  O  O   . ILE A  1 938 ? 21.912  -26.394 1.189   1.00 38.92  ? 938  ILE A O   1 
ATOM   7194  C  CB  . ILE A  1 938 ? 19.748  -24.577 2.856   1.00 33.91  ? 938  ILE A CB  1 
ATOM   7195  C  CG1 . ILE A  1 938 ? 19.678  -23.455 3.873   1.00 29.27  ? 938  ILE A CG1 1 
ATOM   7196  C  CG2 . ILE A  1 938 ? 19.934  -25.919 3.550   1.00 32.29  ? 938  ILE A CG2 1 
ATOM   7197  C  CD1 . ILE A  1 938 ? 18.468  -23.484 4.747   1.00 36.24  ? 938  ILE A CD1 1 
ATOM   7198  N  N   . THR A  1 939 ? 20.249  -25.586 -0.055  1.00 34.58  ? 939  THR A N   1 
ATOM   7199  C  CA  . THR A  1 939 ? 20.340  -26.639 -1.040  1.00 37.81  ? 939  THR A CA  1 
ATOM   7200  C  C   . THR A  1 939 ? 21.696  -26.601 -1.768  1.00 38.82  ? 939  THR A C   1 
ATOM   7201  O  O   . THR A  1 939 ? 22.356  -27.637 -1.922  1.00 38.45  ? 939  THR A O   1 
ATOM   7202  C  CB  . THR A  1 939 ? 19.167  -26.518 -2.018  1.00 42.32  ? 939  THR A CB  1 
ATOM   7203  O  OG1 . THR A  1 939 ? 17.938  -26.738 -1.297  1.00 38.86  ? 939  THR A OG1 1 
ATOM   7204  C  CG2 . THR A  1 939 ? 19.302  -27.493 -3.163  1.00 28.54  ? 939  THR A CG2 1 
ATOM   7205  N  N   . LYS A  1 940 ? 22.109  -25.405 -2.186  1.00 35.21  ? 940  LYS A N   1 
ATOM   7206  C  CA  . LYS A  1 940 ? 23.427  -25.188 -2.776  1.00 32.78  ? 940  LYS A CA  1 
ATOM   7207  C  C   . LYS A  1 940 ? 24.515  -25.793 -1.898  1.00 38.65  ? 940  LYS A C   1 
ATOM   7208  O  O   . LYS A  1 940 ? 25.413  -26.465 -2.397  1.00 34.67  ? 940  LYS A O   1 
ATOM   7209  C  CB  . LYS A  1 940 ? 23.691  -23.693 -2.966  1.00 34.10  ? 940  LYS A CB  1 
ATOM   7210  C  CG  . LYS A  1 940 ? 24.939  -23.360 -3.777  1.00 44.26  ? 940  LYS A CG  1 
ATOM   7211  C  CD  . LYS A  1 940 ? 25.641  -22.129 -3.251  1.00 43.18  ? 940  LYS A CD  1 
ATOM   7212  C  CE  . LYS A  1 940 ? 24.726  -20.924 -3.199  1.00 46.44  ? 940  LYS A CE  1 
ATOM   7213  N  NZ  . LYS A  1 940 ? 25.063  -19.861 -4.221  1.00 53.29  ? 940  LYS A NZ  1 
ATOM   7214  N  N   . ASN A  1 941 ? 24.414  -25.559 -0.585  1.00 38.63  ? 941  ASN A N   1 
ATOM   7215  C  CA  . ASN A  1 941 ? 25.446  -25.973 0.361   1.00 35.27  ? 941  ASN A CA  1 
ATOM   7216  C  C   . ASN A  1 941 ? 25.487  -27.479 0.493   1.00 39.70  ? 941  ASN A C   1 
ATOM   7217  O  O   . ASN A  1 941 ? 26.560  -28.083 0.647   1.00 36.83  ? 941  ASN A O   1 
ATOM   7218  C  CB  . ASN A  1 941 ? 25.211  -25.358 1.739   1.00 37.73  ? 941  ASN A CB  1 
ATOM   7219  C  CG  . ASN A  1 941 ? 25.336  -23.848 1.740   1.00 39.82  ? 941  ASN A CG  1 
ATOM   7220  O  OD1 . ASN A  1 941 ? 25.956  -23.274 0.844   1.00 41.01  ? 941  ASN A OD1 1 
ATOM   7221  N  ND2 . ASN A  1 941 ? 24.768  -23.196 2.763   1.00 32.76  ? 941  ASN A ND2 1 
ATOM   7222  N  N   . ILE A  1 942 ? 24.302  -28.080 0.451   1.00 40.21  ? 942  ILE A N   1 
ATOM   7223  C  CA  . ILE A  1 942 ? 24.192  -29.515 0.598   1.00 38.02  ? 942  ILE A CA  1 
ATOM   7224  C  C   . ILE A  1 942 ? 24.837  -30.163 -0.614  1.00 38.07  ? 942  ILE A C   1 
ATOM   7225  O  O   . ILE A  1 942 ? 25.698  -31.037 -0.466  1.00 38.78  ? 942  ILE A O   1 
ATOM   7226  C  CB  . ILE A  1 942 ? 22.732  -29.976 0.753   1.00 39.20  ? 942  ILE A CB  1 
ATOM   7227  C  CG1 . ILE A  1 942 ? 22.165  -29.507 2.097   1.00 34.33  ? 942  ILE A CG1 1 
ATOM   7228  C  CG2 . ILE A  1 942 ? 22.646  -31.501 0.653   1.00 38.53  ? 942  ILE A CG2 1 
ATOM   7229  C  CD1 . ILE A  1 942 ? 20.672  -29.406 2.127   1.00 29.13  ? 942  ILE A CD1 1 
ATOM   7230  N  N   . LYS A  1 943 ? 24.457  -29.709 -1.806  1.00 38.50  ? 943  LYS A N   1 
ATOM   7231  C  CA  . LYS A  1 943 ? 24.994  -30.297 -3.026  1.00 36.83  ? 943  LYS A CA  1 
ATOM   7232  C  C   . LYS A  1 943 ? 26.500  -30.095 -3.067  1.00 37.61  ? 943  LYS A C   1 
ATOM   7233  O  O   . LYS A  1 943 ? 27.232  -30.983 -3.495  1.00 42.74  ? 943  LYS A O   1 
ATOM   7234  C  CB  . LYS A  1 943 ? 24.311  -29.727 -4.277  1.00 42.76  ? 943  LYS A CB  1 
ATOM   7235  C  CG  . LYS A  1 943 ? 22.793  -30.040 -4.350  1.00 43.26  ? 943  LYS A CG  1 
ATOM   7236  C  CD  . LYS A  1 943 ? 22.163  -29.725 -5.725  1.00 56.46  ? 943  LYS A CD  1 
ATOM   7237  C  CE  . LYS A  1 943 ? 20.615  -29.811 -5.675  1.00 57.76  ? 943  LYS A CE  1 
ATOM   7238  N  NZ  . LYS A  1 943 ? 19.961  -30.768 -6.640  1.00 49.66  ? 943  LYS A NZ  1 
ATOM   7239  N  N   . TRP A  1 944 ? 26.968  -28.968 -2.548  1.00 34.89  ? 944  TRP A N   1 
ATOM   7240  C  CA  . TRP A  1 944 ? 28.401  -28.682 -2.522  1.00 36.79  ? 944  TRP A CA  1 
ATOM   7241  C  C   . TRP A  1 944 ? 29.181  -29.671 -1.665  1.00 33.66  ? 944  TRP A C   1 
ATOM   7242  O  O   . TRP A  1 944 ? 30.260  -30.122 -2.035  1.00 37.30  ? 944  TRP A O   1 
ATOM   7243  C  CB  . TRP A  1 944 ? 28.665  -27.260 -2.007  1.00 28.22  ? 944  TRP A CB  1 
ATOM   7244  C  CG  . TRP A  1 944 ? 30.018  -26.780 -2.376  1.00 31.06  ? 944  TRP A CG  1 
ATOM   7245  C  CD1 . TRP A  1 944 ? 30.356  -26.081 -3.503  1.00 29.02  ? 944  TRP A CD1 1 
ATOM   7246  C  CD2 . TRP A  1 944 ? 31.236  -26.979 -1.647  1.00 29.83  ? 944  TRP A CD2 1 
ATOM   7247  N  NE1 . TRP A  1 944 ? 31.699  -25.814 -3.502  1.00 30.08  ? 944  TRP A NE1 1 
ATOM   7248  C  CE2 . TRP A  1 944 ? 32.264  -26.347 -2.375  1.00 27.86  ? 944  TRP A CE2 1 
ATOM   7249  C  CE3 . TRP A  1 944 ? 31.554  -27.613 -0.442  1.00 35.85  ? 944  TRP A CE3 1 
ATOM   7250  C  CZ2 . TRP A  1 944 ? 33.583  -26.340 -1.953  1.00 29.47  ? 944  TRP A CZ2 1 
ATOM   7251  C  CZ3 . TRP A  1 944 ? 32.878  -27.605 -0.014  1.00 37.03  ? 944  TRP A CZ3 1 
ATOM   7252  C  CH2 . TRP A  1 944 ? 33.876  -26.975 -0.773  1.00 33.48  ? 944  TRP A CH2 1 
ATOM   7253  N  N   . LEU A  1 945 ? 28.640  -29.979 -0.502  1.00 33.45  ? 945  LEU A N   1 
ATOM   7254  C  CA  . LEU A  1 945 ? 29.288  -30.909 0.394   1.00 36.10  ? 945  LEU A CA  1 
ATOM   7255  C  C   . LEU A  1 945 ? 29.333  -32.300 -0.212  1.00 37.07  ? 945  LEU A C   1 
ATOM   7256  O  O   . LEU A  1 945 ? 30.368  -32.951 -0.188  1.00 37.36  ? 945  LEU A O   1 
ATOM   7257  C  CB  . LEU A  1 945 ? 28.576  -30.946 1.743   1.00 32.88  ? 945  LEU A CB  1 
ATOM   7258  C  CG  . LEU A  1 945 ? 28.913  -29.743 2.600   1.00 32.46  ? 945  LEU A CG  1 
ATOM   7259  C  CD1 . LEU A  1 945 ? 28.141  -29.761 3.902   1.00 31.53  ? 945  LEU A CD1 1 
ATOM   7260  C  CD2 . LEU A  1 945 ? 30.405  -29.761 2.853   1.00 37.37  ? 945  LEU A CD2 1 
ATOM   7261  N  N   . GLU A  1 946 ? 28.231  -32.774 -0.768  1.00 37.91  ? 946  GLU A N   1 
ATOM   7262  C  CA  . GLU A  1 946 ? 28.269  -34.153 -1.233  1.00 43.69  ? 946  GLU A CA  1 
ATOM   7263  C  C   . GLU A  1 946 ? 29.061  -34.266 -2.528  1.00 40.51  ? 946  GLU A C   1 
ATOM   7264  O  O   . GLU A  1 946 ? 29.448  -35.355 -2.920  1.00 50.07  ? 946  GLU A O   1 
ATOM   7265  C  CB  . GLU A  1 946 ? 26.861  -34.740 -1.382  1.00 38.71  ? 946  GLU A CB  1 
ATOM   7266  C  CG  . GLU A  1 946 ? 25.826  -33.886 -2.053  1.00 46.78  ? 946  GLU A CG  1 
ATOM   7267  C  CD  . GLU A  1 946 ? 24.403  -34.284 -1.646  1.00 52.80  ? 946  GLU A CD  1 
ATOM   7268  O  OE1 . GLU A  1 946 ? 24.232  -34.926 -0.578  1.00 52.87  ? 946  GLU A OE1 1 
ATOM   7269  O  OE2 . GLU A  1 946 ? 23.450  -33.945 -2.388  1.00 56.97  ? 946  GLU A OE2 1 
ATOM   7270  N  N   . LYS A  1 947 ? 29.356  -33.137 -3.155  1.00 42.06  ? 947  LYS A N   1 
ATOM   7271  C  CA  . LYS A  1 947 ? 30.092  -33.140 -4.423  1.00 40.32  ? 947  LYS A CA  1 
ATOM   7272  C  C   . LYS A  1 947 ? 31.588  -33.009 -4.223  1.00 40.28  ? 947  LYS A C   1 
ATOM   7273  O  O   . LYS A  1 947 ? 32.367  -33.574 -4.983  1.00 44.67  ? 947  LYS A O   1 
ATOM   7274  C  CB  . LYS A  1 947 ? 29.618  -32.007 -5.324  1.00 36.09  ? 947  LYS A CB  1 
ATOM   7275  C  CG  . LYS A  1 947 ? 29.302  -32.438 -6.728  1.00 51.51  ? 947  LYS A CG  1 
ATOM   7276  C  CD  . LYS A  1 947 ? 28.094  -33.350 -6.740  1.00 59.59  ? 947  LYS A CD  1 
ATOM   7277  C  CE  . LYS A  1 947 ? 28.021  -34.159 -8.034  1.00 73.11  ? 947  LYS A CE  1 
ATOM   7278  N  NZ  . LYS A  1 947 ? 27.048  -35.295 -7.934  1.00 72.16  ? 947  LYS A NZ  1 
ATOM   7279  N  N   . ASN A  1 948 ? 31.986  -32.264 -3.195  1.00 37.43  ? 948  ASN A N   1 
ATOM   7280  C  CA  . ASN A  1 948 ? 33.361  -31.806 -3.095  1.00 34.18  ? 948  ASN A CA  1 
ATOM   7281  C  C   . ASN A  1 948 ? 34.033  -32.105 -1.779  1.00 32.24  ? 948  ASN A C   1 
ATOM   7282  O  O   . ASN A  1 948 ? 35.238  -31.938 -1.668  1.00 37.68  ? 948  ASN A O   1 
ATOM   7283  C  CB  . ASN A  1 948 ? 33.434  -30.296 -3.336  1.00 36.65  ? 948  ASN A CB  1 
ATOM   7284  C  CG  . ASN A  1 948 ? 32.665  -29.868 -4.547  1.00 33.50  ? 948  ASN A CG  1 
ATOM   7285  O  OD1 . ASN A  1 948 ? 32.828  -30.424 -5.633  1.00 41.23  ? 948  ASN A OD1 1 
ATOM   7286  N  ND2 . ASN A  1 948 ? 31.794  -28.890 -4.368  1.00 34.59  ? 948  ASN A ND2 1 
ATOM   7287  N  N   . LEU A  1 949 ? 33.267  -32.518 -0.779  1.00 34.20  ? 949  LEU A N   1 
ATOM   7288  C  CA  . LEU A  1 949 ? 33.831  -32.805 0.534   1.00 37.27  ? 949  LEU A CA  1 
ATOM   7289  C  C   . LEU A  1 949 ? 34.956  -33.856 0.469   1.00 39.14  ? 949  LEU A C   1 
ATOM   7290  O  O   . LEU A  1 949 ? 36.044  -33.623 1.031   1.00 35.55  ? 949  LEU A O   1 
ATOM   7291  C  CB  . LEU A  1 949 ? 32.733  -33.246 1.507   1.00 37.13  ? 949  LEU A CB  1 
ATOM   7292  C  CG  . LEU A  1 949 ? 33.052  -33.577 2.967   1.00 41.96  ? 949  LEU A CG  1 
ATOM   7293  C  CD1 . LEU A  1 949 ? 33.574  -32.376 3.697   1.00 44.68  ? 949  LEU A CD1 1 
ATOM   7294  C  CD2 . LEU A  1 949 ? 31.808  -34.084 3.656   1.00 37.80  ? 949  LEU A CD2 1 
ATOM   7295  N  N   . PRO A  1 950 ? 34.722  -34.999 -0.222  1.00 41.30  ? 950  PRO A N   1 
ATOM   7296  C  CA  . PRO A  1 950 ? 35.826  -35.969 -0.240  1.00 35.58  ? 950  PRO A CA  1 
ATOM   7297  C  C   . PRO A  1 950 ? 37.023  -35.393 -0.961  1.00 35.45  ? 950  PRO A C   1 
ATOM   7298  O  O   . PRO A  1 950 ? 38.156  -35.619 -0.541  1.00 37.30  ? 950  PRO A O   1 
ATOM   7299  C  CB  . PRO A  1 950 ? 35.238  -37.167 -0.988  1.00 35.65  ? 950  PRO A CB  1 
ATOM   7300  C  CG  . PRO A  1 950 ? 33.746  -37.027 -0.778  1.00 38.46  ? 950  PRO A CG  1 
ATOM   7301  C  CD  . PRO A  1 950 ? 33.523  -35.545 -0.887  1.00 38.50  ? 950  PRO A CD  1 
ATOM   7302  N  N   . THR A  1 951 ? 36.778  -34.616 -2.006  1.00 31.18  ? 951  THR A N   1 
ATOM   7303  C  CA  . THR A  1 951 ? 37.884  -33.980 -2.714  1.00 31.20  ? 951  THR A CA  1 
ATOM   7304  C  C   . THR A  1 951 ? 38.672  -33.056 -1.779  1.00 35.93  ? 951  THR A C   1 
ATOM   7305  O  O   . THR A  1 951 ? 39.896  -33.041 -1.790  1.00 36.92  ? 951  THR A O   1 
ATOM   7306  C  CB  . THR A  1 951 ? 37.372  -33.228 -3.930  1.00 39.29  ? 951  THR A CB  1 
ATOM   7307  O  OG1 . THR A  1 951 ? 36.642  -34.151 -4.766  1.00 38.25  ? 951  THR A OG1 1 
ATOM   7308  C  CG2 . THR A  1 951 ? 38.530  -32.619 -4.714  1.00 37.71  ? 951  THR A CG2 1 
ATOM   7309  N  N   . LEU A  1 952 ? 37.964  -32.325 -0.928  1.00 38.26  ? 952  LEU A N   1 
ATOM   7310  C  CA  . LEU A  1 952 ? 38.605  -31.452 0.038   1.00 28.74  ? 952  LEU A CA  1 
ATOM   7311  C  C   . LEU A  1 952 ? 39.434  -32.250 1.046   1.00 34.38  ? 952  LEU A C   1 
ATOM   7312  O  O   . LEU A  1 952 ? 40.606  -31.931 1.275   1.00 30.53  ? 952  LEU A O   1 
ATOM   7313  C  CB  . LEU A  1 952 ? 37.549  -30.609 0.749   1.00 29.77  ? 952  LEU A CB  1 
ATOM   7314  C  CG  . LEU A  1 952 ? 38.049  -29.703 1.880   1.00 32.26  ? 952  LEU A CG  1 
ATOM   7315  C  CD1 . LEU A  1 952 ? 38.915  -28.581 1.350   1.00 29.31  ? 952  LEU A CD1 1 
ATOM   7316  C  CD2 . LEU A  1 952 ? 36.874  -29.163 2.634   1.00 33.94  ? 952  LEU A CD2 1 
ATOM   7317  N  N   . ARG A  1 953 ? 38.821  -33.281 1.648   1.00 36.03  ? 953  ARG A N   1 
ATOM   7318  C  CA  . ARG A  1 953 ? 39.521  -34.186 2.575   1.00 35.08  ? 953  ARG A CA  1 
ATOM   7319  C  C   . ARG A  1 953 ? 40.814  -34.696 1.947   1.00 37.01  ? 953  ARG A C   1 
ATOM   7320  O  O   . ARG A  1 953 ? 41.887  -34.642 2.544   1.00 42.07  ? 953  ARG A O   1 
ATOM   7321  C  CB  . ARG A  1 953 ? 38.635  -35.379 2.984   1.00 33.10  ? 953  ARG A CB  1 
ATOM   7322  C  CG  . ARG A  1 953 ? 39.354  -36.463 3.830   1.00 36.70  ? 953  ARG A CG  1 
ATOM   7323  C  CD  . ARG A  1 953 ? 38.571  -36.899 5.091   1.00 36.50  ? 953  ARG A CD  1 
ATOM   7324  N  NE  . ARG A  1 953 ? 37.125  -36.915 4.860   1.00 44.59  ? 953  ARG A NE  1 
ATOM   7325  C  CZ  . ARG A  1 953 ? 36.191  -36.733 5.794   1.00 41.43  ? 953  ARG A CZ  1 
ATOM   7326  N  NH1 . ARG A  1 953 ? 36.525  -36.533 7.060   1.00 40.52  ? 953  ARG A NH1 1 
ATOM   7327  N  NH2 . ARG A  1 953 ? 34.906  -36.748 5.457   1.00 45.67  ? 953  ARG A NH2 1 
ATOM   7328  N  N   . THR A  1 954 ? 40.714  -35.131 0.705   1.00 35.39  ? 954  THR A N   1 
ATOM   7329  C  CA  . THR A  1 954 ? 41.837  -35.746 0.045   1.00 34.32  ? 954  THR A CA  1 
ATOM   7330  C  C   . THR A  1 954 ? 42.919  -34.755 -0.282  1.00 31.32  ? 954  THR A C   1 
ATOM   7331  O  O   . THR A  1 954 ? 44.086  -35.023 -0.051  1.00 37.11  ? 954  THR A O   1 
ATOM   7332  C  CB  . THR A  1 954 ? 41.372  -36.448 -1.211  1.00 38.26  ? 954  THR A CB  1 
ATOM   7333  O  OG1 . THR A  1 954 ? 40.613  -37.581 -0.812  1.00 39.31  ? 954  THR A OG1 1 
ATOM   7334  C  CG2 . THR A  1 954 ? 42.547  -36.900 -2.060  1.00 35.67  ? 954  THR A CG2 1 
ATOM   7335  N  N   . TRP A  1 955 ? 42.530  -33.603 -0.805  1.00 34.54  ? 955  TRP A N   1 
ATOM   7336  C  CA  . TRP A  1 955 ? 43.491  -32.577 -1.173  1.00 30.03  ? 955  TRP A CA  1 
ATOM   7337  C  C   . TRP A  1 955 ? 44.350  -32.155 0.031   1.00 35.18  ? 955  TRP A C   1 
ATOM   7338  O  O   . TRP A  1 955 ? 45.575  -32.000 -0.067  1.00 33.32  ? 955  TRP A O   1 
ATOM   7339  C  CB  . TRP A  1 955 ? 42.761  -31.380 -1.775  1.00 33.11  ? 955  TRP A CB  1 
ATOM   7340  C  CG  . TRP A  1 955 ? 43.700  -30.396 -2.364  1.00 34.63  ? 955  TRP A CG  1 
ATOM   7341  C  CD1 . TRP A  1 955 ? 44.089  -30.310 -3.665  1.00 37.99  ? 955  TRP A CD1 1 
ATOM   7342  C  CD2 . TRP A  1 955 ? 44.385  -29.353 -1.665  1.00 32.89  ? 955  TRP A CD2 1 
ATOM   7343  N  NE1 . TRP A  1 955 ? 44.983  -29.274 -3.826  1.00 39.30  ? 955  TRP A NE1 1 
ATOM   7344  C  CE2 . TRP A  1 955 ? 45.176  -28.668 -2.610  1.00 39.31  ? 955  TRP A CE2 1 
ATOM   7345  C  CE3 . TRP A  1 955 ? 44.395  -28.923 -0.334  1.00 34.47  ? 955  TRP A CE3 1 
ATOM   7346  C  CZ2 . TRP A  1 955 ? 45.975  -27.581 -2.266  1.00 38.29  ? 955  TRP A CZ2 1 
ATOM   7347  C  CZ3 . TRP A  1 955 ? 45.196  -27.852 0.008   1.00 40.25  ? 955  TRP A CZ3 1 
ATOM   7348  C  CH2 . TRP A  1 955 ? 45.974  -27.189 -0.957  1.00 39.46  ? 955  TRP A CH2 1 
ATOM   7349  N  N   . LEU A  1 956 ? 43.715  -32.006 1.184   1.00 33.26  ? 956  LEU A N   1 
ATOM   7350  C  CA  . LEU A  1 956 ? 44.449  -31.654 2.396   1.00 34.10  ? 956  LEU A CA  1 
ATOM   7351  C  C   . LEU A  1 956 ? 45.379  -32.775 2.872   1.00 38.82  ? 956  LEU A C   1 
ATOM   7352  O  O   . LEU A  1 956 ? 46.506  -32.521 3.335   1.00 36.03  ? 956  LEU A O   1 
ATOM   7353  C  CB  . LEU A  1 956 ? 43.475  -31.288 3.507   1.00 31.17  ? 956  LEU A CB  1 
ATOM   7354  C  CG  . LEU A  1 956 ? 42.667  -30.011 3.301   1.00 37.51  ? 956  LEU A CG  1 
ATOM   7355  C  CD1 . LEU A  1 956 ? 41.485  -29.971 4.258   1.00 37.71  ? 956  LEU A CD1 1 
ATOM   7356  C  CD2 . LEU A  1 956 ? 43.573  -28.787 3.503   1.00 40.38  ? 956  LEU A CD2 1 
ATOM   7357  N  N   . MET A  1 957 ? 44.917  -34.017 2.766   1.00 35.44  ? 957  MET A N   1 
ATOM   7358  C  CA  . MET A  1 957 ? 45.758  -35.129 3.189   1.00 34.65  ? 957  MET A CA  1 
ATOM   7359  C  C   . MET A  1 957 ? 46.971  -35.209 2.276   1.00 36.15  ? 957  MET A C   1 
ATOM   7360  O  O   . MET A  1 957 ? 48.095  -35.313 2.757   1.00 35.59  ? 957  MET A O   1 
ATOM   7361  C  CB  . MET A  1 957 ? 44.963  -36.432 3.202   1.00 39.52  ? 957  MET A CB  1 
ATOM   7362  C  CG  . MET A  1 957 ? 44.083  -36.585 4.453   1.00 36.35  ? 957  MET A CG  1 
ATOM   7363  S  SD  . MET A  1 957 ? 45.019  -36.305 5.976   1.00 39.54  ? 957  MET A SD  1 
ATOM   7364  C  CE  . MET A  1 957 ? 45.865  -37.872 6.151   1.00 38.22  ? 957  MET A CE  1 
ATOM   7365  N  N   . VAL A  1 958 ? 46.735  -35.111 0.964   1.00 36.79  ? 958  VAL A N   1 
ATOM   7366  C  CA  . VAL A  1 958 ? 47.807  -35.043 -0.034  1.00 31.86  ? 958  VAL A CA  1 
ATOM   7367  C  C   . VAL A  1 958 ? 48.799  -33.905 0.229   1.00 44.55  ? 958  VAL A C   1 
ATOM   7368  O  O   . VAL A  1 958 ? 50.003  -34.089 0.083   1.00 51.78  ? 958  VAL A O   1 
ATOM   7369  C  CB  . VAL A  1 958 ? 47.249  -34.860 -1.461  1.00 35.08  ? 958  VAL A CB  1 
ATOM   7370  C  CG1 . VAL A  1 958 ? 48.373  -34.713 -2.461  1.00 35.36  ? 958  VAL A CG1 1 
ATOM   7371  C  CG2 . VAL A  1 958 ? 46.339  -36.015 -1.874  1.00 31.06  ? 958  VAL A CG2 1 
ATOM   7372  N  N   . ASN A  1 959 ? 48.304  -32.726 0.604   1.00 39.19  ? 959  ASN A N   1 
ATOM   7373  C  CA  . ASN A  1 959 ? 49.190  -31.592 0.828   1.00 38.87  ? 959  ASN A CA  1 
ATOM   7374  C  C   . ASN A  1 959 ? 50.155  -31.861 2.004   1.00 43.80  ? 959  ASN A C   1 
ATOM   7375  O  O   . ASN A  1 959 ? 51.334  -31.504 1.933   1.00 49.01  ? 959  ASN A O   1 
ATOM   7376  C  CB  . ASN A  1 959 ? 48.353  -30.304 1.033   1.00 44.18  ? 959  ASN A CB  1 
ATOM   7377  C  CG  . ASN A  1 959 ? 49.174  -29.135 1.560   1.00 39.80  ? 959  ASN A CG  1 
ATOM   7378  O  OD1 . ASN A  1 959 ? 49.850  -28.436 0.803   1.00 44.24  ? 959  ASN A OD1 1 
ATOM   7379  N  ND2 . ASN A  1 959 ? 49.128  -28.927 2.869   1.00 39.16  ? 959  ASN A ND2 1 
ATOM   7380  N  N   . THR A  1 960 ? 49.652  -32.505 3.063   1.00 45.25  ? 960  THR A N   1 
ATOM   7381  C  CA  . THR A  1 960 ? 50.456  -33.011 4.200   1.00 39.44  ? 960  THR A CA  1 
ATOM   7382  C  C   . THR A  1 960 ? 51.718  -33.789 3.809   1.00 47.99  ? 960  THR A C   1 
ATOM   7383  O  O   . THR A  1 960 ? 52.759  -33.684 4.466   1.00 54.85  ? 960  THR A O   1 
ATOM   7384  C  CB  . THR A  1 960 ? 49.598  -33.946 5.104   1.00 48.58  ? 960  THR A CB  1 
ATOM   7385  O  OG1 . THR A  1 960 ? 48.638  -33.177 5.845   1.00 53.67  ? 960  THR A OG1 1 
ATOM   7386  C  CG2 . THR A  1 960 ? 50.457  -34.722 6.080   1.00 61.19  ? 960  THR A CG2 1 
ATOM   7387  N  N   . ARG A  1 961 ? 51.624  -34.561 2.731   1.00 47.54  ? 961  ARG A N   1 
ATOM   7388  C  CA  . ARG A  1 961 ? 52.703  -35.437 2.302   1.00 44.80  ? 961  ARG A CA  1 
ATOM   7389  C  C   . ARG A  1 961 ? 53.753  -34.676 1.495   1.00 59.46  ? 961  ARG A C   1 
ATOM   7390  O  O   . ARG A  1 961 ? 54.812  -34.364 2.015   1.00 74.86  ? 961  ARG A O   1 
ATOM   7391  C  CB  . ARG A  1 961 ? 52.126  -36.603 1.505   1.00 38.91  ? 961  ARG A CB  1 
ATOM   7392  C  CG  . ARG A  1 961 ? 51.279  -37.521 2.389   1.00 38.70  ? 961  ARG A CG  1 
ATOM   7393  C  CD  . ARG A  1 961 ? 50.594  -38.596 1.591   1.00 37.08  ? 961  ARG A CD  1 
ATOM   7394  N  NE  . ARG A  1 961 ? 49.746  -39.472 2.393   1.00 31.51  ? 961  ARG A NE  1 
ATOM   7395  C  CZ  . ARG A  1 961 ? 50.164  -40.585 2.999   1.00 31.89  ? 961  ARG A CZ  1 
ATOM   7396  N  NH1 . ARG A  1 961 ? 51.438  -40.951 2.940   1.00 23.32  ? 961  ARG A NH1 1 
ATOM   7397  N  NH2 . ARG A  1 961 ? 49.304  -41.325 3.696   1.00 28.01  ? 961  ARG A NH2 1 
ATOM   7398  N  N   . HIS A  1 962 ? 53.454  -34.376 0.234   1.00 58.32  ? 962  HIS A N   1 
ATOM   7399  C  CA  A HIS A  1 962 ? 54.346  -33.592 -0.626  0.56 66.21  ? 962  HIS A CA  1 
ATOM   7400  C  CA  B HIS A  1 962 ? 54.350  -33.591 -0.603  0.44 65.38  ? 962  HIS A CA  1 
ATOM   7401  C  C   . HIS A  1 962 ? 53.748  -32.215 -0.911  1.00 65.05  ? 962  HIS A C   1 
ATOM   7402  O  O   . HIS A  1 962 ? 52.836  -32.092 -1.724  1.00 67.57  ? 962  HIS A O   1 
ATOM   7403  C  CB  A HIS A  1 962 ? 54.622  -34.326 -1.952  0.56 63.79  ? 962  HIS A CB  1 
ATOM   7404  C  CB  B HIS A  1 962 ? 54.681  -34.355 -1.896  0.44 64.61  ? 962  HIS A CB  1 
ATOM   7405  C  CG  A HIS A  1 962 ? 55.400  -33.516 -2.951  0.56 63.73  ? 962  HIS A CG  1 
ATOM   7406  C  CG  B HIS A  1 962 ? 53.498  -34.618 -2.768  0.44 58.61  ? 962  HIS A CG  1 
ATOM   7407  N  ND1 A HIS A  1 962 ? 56.592  -32.895 -2.647  0.56 66.72  ? 962  HIS A ND1 1 
ATOM   7408  N  ND1 B HIS A  1 962 ? 52.455  -35.433 -2.386  0.44 50.36  ? 962  HIS A ND1 1 
ATOM   7409  C  CD2 A HIS A  1 962 ? 55.162  -33.254 -4.258  0.56 60.05  ? 962  HIS A CD2 1 
ATOM   7410  C  CD2 B HIS A  1 962 ? 53.188  -34.158 -4.001  0.44 58.67  ? 962  HIS A CD2 1 
ATOM   7411  C  CE1 A HIS A  1 962 ? 57.049  -32.273 -3.721  0.56 62.59  ? 962  HIS A CE1 1 
ATOM   7412  C  CE1 B HIS A  1 962 ? 51.558  -35.472 -3.352  0.44 53.63  ? 962  HIS A CE1 1 
ATOM   7413  N  NE2 A HIS A  1 962 ? 56.200  -32.475 -4.711  0.56 57.09  ? 962  HIS A NE2 1 
ATOM   7414  N  NE2 B HIS A  1 962 ? 51.977  -34.704 -4.343  0.44 57.76  ? 962  HIS A NE2 1 
ATOM   7415  N  N   . HIS A  1 963 ? 54.228  -31.171 -0.234  1.00 72.88  ? 963  HIS A N   1 
ATOM   7416  C  CA  . HIS A  1 963 ? 55.227  -31.238 0.839   1.00 78.01  ? 963  HIS A CA  1 
ATOM   7417  C  C   . HIS A  1 963 ? 54.933  -30.068 1.786   1.00 83.17  ? 963  HIS A C   1 
ATOM   7418  O  O   . HIS A  1 963 ? 54.483  -29.004 1.320   1.00 79.92  ? 963  HIS A O   1 
ATOM   7419  C  CB  . HIS A  1 963 ? 56.668  -31.138 0.293   1.00 86.56  ? 963  HIS A CB  1 
ATOM   7420  C  CG  . HIS A  1 963 ? 57.578  -32.238 0.753   1.00 87.12  ? 963  HIS A CG  1 
ATOM   7421  N  ND1 . HIS A  1 963 ? 58.437  -32.902 -0.100  1.00 88.84  ? 963  HIS A ND1 1 
ATOM   7422  C  CD2 . HIS A  1 963 ? 57.758  -32.792 1.976   1.00 88.94  ? 963  HIS A CD2 1 
ATOM   7423  C  CE1 . HIS A  1 963 ? 59.103  -33.824 0.579   1.00 90.25  ? 963  HIS A CE1 1 
ATOM   7424  N  NE2 . HIS A  1 963 ? 58.711  -33.776 1.840   1.00 93.38  ? 963  HIS A NE2 1 
ATOM   7425  N  N   . HIS A  1 964 ? 55.116  -30.136 3.010   1.00 78.25  ? 964  HIS A N   1 
ATOM   7426  N  N   . PRO B  1 54  ? 52.879  5.688   65.189  1.00 85.83  ? 54   PRO C N   1 
ATOM   7427  C  CA  . PRO B  1 54  ? 51.440  5.942   65.046  1.00 87.80  ? 54   PRO C CA  1 
ATOM   7428  C  C   . PRO B  1 54  ? 51.070  6.624   63.725  1.00 82.47  ? 54   PRO C C   1 
ATOM   7429  O  O   . PRO B  1 54  ? 50.164  7.462   63.753  1.00 72.53  ? 54   PRO C O   1 
ATOM   7430  C  CB  . PRO B  1 54  ? 51.137  6.875   66.228  1.00 83.48  ? 54   PRO C CB  1 
ATOM   7431  C  CG  . PRO B  1 54  ? 52.438  7.584   66.490  1.00 73.58  ? 54   PRO C CG  1 
ATOM   7432  C  CD  . PRO B  1 54  ? 53.508  6.570   66.193  1.00 81.97  ? 54   PRO C CD  1 
ATOM   7433  N  N   . VAL B  1 55  ? 51.772  6.314   62.620  1.00 83.48  ? 55   VAL C N   1 
ATOM   7434  C  CA  . VAL B  1 55  ? 51.719  7.143   61.397  1.00 78.78  ? 55   VAL C CA  1 
ATOM   7435  C  C   . VAL B  1 55  ? 51.885  6.529   59.976  1.00 78.57  ? 55   VAL C C   1 
ATOM   7436  O  O   . VAL B  1 55  ? 52.672  5.606   59.765  1.00 80.70  ? 55   VAL C O   1 
ATOM   7437  C  CB  . VAL B  1 55  ? 52.798  8.227   61.448  1.00 80.67  ? 55   VAL C CB  1 
ATOM   7438  C  CG1 . VAL B  1 55  ? 52.398  9.361   60.544  1.00 82.57  ? 55   VAL C CG1 1 
ATOM   7439  C  CG2 . VAL B  1 55  ? 53.023  8.717   62.858  1.00 80.74  ? 55   VAL C CG2 1 
ATOM   7440  N  N   . ALA B  1 56  ? 51.150  7.118   59.020  1.00 75.80  ? 56   ALA C N   1 
ATOM   7441  C  CA  . ALA B  1 56  ? 51.294  6.969   57.558  1.00 84.15  ? 56   ALA C CA  1 
ATOM   7442  C  C   . ALA B  1 56  ? 51.246  8.429   56.957  1.00 82.46  ? 56   ALA C C   1 
ATOM   7443  O  O   . ALA B  1 56  ? 51.432  9.369   57.740  1.00 79.84  ? 56   ALA C O   1 
ATOM   7444  C  CB  . ALA B  1 56  ? 50.187  6.045   57.019  1.00 77.65  ? 56   ALA C CB  1 
ATOM   7445  N  N   . THR B  1 57  ? 51.047  8.717   55.655  1.00 70.87  ? 57   THR C N   1 
ATOM   7446  C  CA  . THR B  1 57  ? 50.978  7.854   54.474  1.00 71.91  ? 57   THR C CA  1 
ATOM   7447  C  C   . THR B  1 57  ? 52.179  8.041   53.552  1.00 74.57  ? 57   THR C C   1 
ATOM   7448  O  O   . THR B  1 57  ? 52.293  7.378   52.529  1.00 74.14  ? 57   THR C O   1 
ATOM   7449  C  CB  . THR B  1 57  ? 49.730  8.150   53.630  1.00 68.71  ? 57   THR C CB  1 
ATOM   7450  O  OG1 . THR B  1 57  ? 49.714  9.545   53.297  1.00 71.45  ? 57   THR C OG1 1 
ATOM   7451  C  CG2 . THR B  1 57  ? 48.475  7.812   54.379  1.00 66.64  ? 57   THR C CG2 1 
ATOM   7452  N  N   . ASN B  1 58  ? 53.052  8.975   53.893  1.00 76.36  ? 58   ASN C N   1 
ATOM   7453  C  CA  . ASN B  1 58  ? 54.264  9.182   53.121  1.00 77.86  ? 58   ASN C CA  1 
ATOM   7454  C  C   . ASN B  1 58  ? 55.483  8.795   53.944  1.00 81.26  ? 58   ASN C C   1 
ATOM   7455  O  O   . ASN B  1 58  ? 56.561  9.370   53.777  1.00 83.77  ? 58   ASN C O   1 
ATOM   7456  C  CB  . ASN B  1 58  ? 54.368  10.639  52.679  1.00 79.80  ? 58   ASN C CB  1 
ATOM   7457  C  CG  . ASN B  1 58  ? 54.503  11.589  53.852  1.00 78.95  ? 58   ASN C CG  1 
ATOM   7458  O  OD1 . ASN B  1 58  ? 54.201  11.231  54.994  1.00 76.22  ? 58   ASN C OD1 1 
ATOM   7459  N  ND2 . ASN B  1 58  ? 54.966  12.804  53.578  1.00 72.30  ? 58   ASN C ND2 1 
ATOM   7460  N  N   . GLY B  1 59  ? 55.309  7.811   54.824  1.00 78.97  ? 59   GLY C N   1 
ATOM   7461  C  CA  . GLY B  1 59  ? 56.261  7.585   55.894  1.00 74.62  ? 59   GLY C CA  1 
ATOM   7462  C  C   . GLY B  1 59  ? 56.022  8.753   56.821  1.00 77.60  ? 59   GLY C C   1 
ATOM   7463  O  O   . GLY B  1 59  ? 54.911  9.278   56.855  1.00 84.98  ? 59   GLY C O   1 
ATOM   7464  N  N   . GLU B  1 60  ? 57.042  9.165   57.562  1.00 78.55  ? 60   GLU C N   1 
ATOM   7465  C  CA  . GLU B  1 60  ? 56.973  10.392  58.356  1.00 81.33  ? 60   GLU C CA  1 
ATOM   7466  C  C   . GLU B  1 60  ? 55.932  10.313  59.486  1.00 84.29  ? 60   GLU C C   1 
ATOM   7467  O  O   . GLU B  1 60  ? 55.083  9.433   59.489  1.00 76.43  ? 60   GLU C O   1 
ATOM   7468  C  CB  . GLU B  1 60  ? 56.689  11.585  57.442  1.00 80.60  ? 60   GLU C CB  1 
ATOM   7469  C  CG  . GLU B  1 60  ? 56.992  12.932  58.065  1.00 85.49  ? 60   GLU C CG  1 
ATOM   7470  C  CD  . GLU B  1 60  ? 57.112  14.021  57.034  1.00 84.20  ? 60   GLU C CD  1 
ATOM   7471  O  OE1 . GLU B  1 60  ? 57.366  13.684  55.857  1.00 83.12  ? 60   GLU C OE1 1 
ATOM   7472  O  OE2 . GLU B  1 60  ? 56.949  15.208  57.399  1.00 89.20  ? 60   GLU C OE2 1 
ATOM   7473  N  N   . ARG B  1 61  ? 56.017  11.233  60.446  1.00 86.49  ? 61   ARG C N   1 
ATOM   7474  C  CA  . ARG B  1 61  ? 55.277  11.119  61.699  1.00 79.78  ? 61   ARG C CA  1 
ATOM   7475  C  C   . ARG B  1 61  ? 54.148  12.138  61.858  1.00 80.13  ? 61   ARG C C   1 
ATOM   7476  O  O   . ARG B  1 61  ? 54.328  13.334  61.617  1.00 86.18  ? 61   ARG C O   1 
ATOM   7477  C  CB  . ARG B  1 61  ? 56.242  11.239  62.886  1.00 84.08  ? 61   ARG C CB  1 
ATOM   7478  C  CG  . ARG B  1 61  ? 57.206  10.062  63.056  1.00 91.37  ? 61   ARG C CG  1 
ATOM   7479  C  CD  . ARG B  1 61  ? 56.460  8.761   63.351  1.00 92.74  ? 61   ARG C CD  1 
ATOM   7480  N  NE  . ARG B  1 61  ? 57.165  7.886   64.290  1.00 100.72 ? 61   ARG C NE  1 
ATOM   7481  C  CZ  . ARG B  1 61  ? 57.845  6.795   63.943  1.00 102.53 ? 61   ARG C CZ  1 
ATOM   7482  N  NH1 . ARG B  1 61  ? 57.924  6.428   62.670  1.00 103.14 ? 61   ARG C NH1 1 
ATOM   7483  N  NH2 . ARG B  1 61  ? 58.450  6.067   64.873  1.00 98.32  ? 61   ARG C NH2 1 
ATOM   7484  N  N   . PHE B  1 62  ? 52.996  11.644  62.306  1.00 74.50  ? 62   PHE C N   1 
ATOM   7485  C  CA  . PHE B  1 62  ? 51.773  12.416  62.464  1.00 74.17  ? 62   PHE C CA  1 
ATOM   7486  C  C   . PHE B  1 62  ? 51.732  12.974  63.859  1.00 70.70  ? 62   PHE C C   1 
ATOM   7487  O  O   . PHE B  1 62  ? 51.667  12.224  64.823  1.00 73.72  ? 62   PHE C O   1 
ATOM   7488  C  CB  . PHE B  1 62  ? 50.532  11.549  62.214  1.00 72.25  ? 62   PHE C CB  1 
ATOM   7489  C  CG  . PHE B  1 62  ? 49.344  12.308  61.699  1.00 68.50  ? 62   PHE C CG  1 
ATOM   7490  C  CD1 . PHE B  1 62  ? 49.257  12.664  60.360  1.00 68.43  ? 62   PHE C CD1 1 
ATOM   7491  C  CD2 . PHE B  1 62  ? 48.305  12.651  62.545  1.00 67.23  ? 62   PHE C CD2 1 
ATOM   7492  C  CE1 . PHE B  1 62  ? 48.156  13.361  59.881  1.00 66.03  ? 62   PHE C CE1 1 
ATOM   7493  C  CE2 . PHE B  1 62  ? 47.200  13.349  62.072  1.00 66.16  ? 62   PHE C CE2 1 
ATOM   7494  C  CZ  . PHE B  1 62  ? 47.126  13.705  60.744  1.00 64.97  ? 62   PHE C CZ  1 
ATOM   7495  N  N   . PRO B  1 63  ? 51.734  14.299  63.969  1.00 69.13  ? 63   PRO C N   1 
ATOM   7496  C  CA  . PRO B  1 63  ? 51.840  15.005  65.246  1.00 74.57  ? 63   PRO C CA  1 
ATOM   7497  C  C   . PRO B  1 63  ? 50.609  14.838  66.138  1.00 71.94  ? 63   PRO C C   1 
ATOM   7498  O  O   . PRO B  1 63  ? 50.314  15.749  66.926  1.00 68.12  ? 63   PRO C O   1 
ATOM   7499  C  CB  . PRO B  1 63  ? 51.989  16.476  64.826  1.00 75.08  ? 63   PRO C CB  1 
ATOM   7500  C  CG  . PRO B  1 63  ? 52.202  16.466  63.344  1.00 77.55  ? 63   PRO C CG  1 
ATOM   7501  C  CD  . PRO B  1 63  ? 51.573  15.221  62.837  1.00 69.37  ? 63   PRO C CD  1 
ATOM   7502  N  N   . TRP B  1 64  ? 49.905  13.714  66.020  1.00 66.30  ? 64   TRP C N   1 
ATOM   7503  C  CA  . TRP B  1 64  ? 48.655  13.520  66.757  1.00 67.60  ? 64   TRP C CA  1 
ATOM   7504  C  C   . TRP B  1 64  ? 48.161  12.093  66.658  1.00 70.55  ? 64   TRP C C   1 
ATOM   7505  O  O   . TRP B  1 64  ? 48.076  11.530  65.565  1.00 71.63  ? 64   TRP C O   1 
ATOM   7506  C  CB  . TRP B  1 64  ? 47.585  14.462  66.234  1.00 62.32  ? 64   TRP C CB  1 
ATOM   7507  C  CG  . TRP B  1 64  ? 46.389  14.621  67.102  1.00 63.00  ? 64   TRP C CG  1 
ATOM   7508  C  CD1 . TRP B  1 64  ? 45.145  14.126  66.869  1.00 65.10  ? 64   TRP C CD1 1 
ATOM   7509  C  CD2 . TRP B  1 64  ? 46.305  15.361  68.327  1.00 65.39  ? 64   TRP C CD2 1 
ATOM   7510  N  NE1 . TRP B  1 64  ? 44.285  14.508  67.872  1.00 67.91  ? 64   TRP C NE1 1 
ATOM   7511  C  CE2 . TRP B  1 64  ? 44.974  15.265  68.781  1.00 65.02  ? 64   TRP C CE2 1 
ATOM   7512  C  CE3 . TRP B  1 64  ? 47.227  16.082  69.090  1.00 57.87  ? 64   TRP C CE3 1 
ATOM   7513  C  CZ2 . TRP B  1 64  ? 44.542  15.865  69.958  1.00 65.82  ? 64   TRP C CZ2 1 
ATOM   7514  C  CZ3 . TRP B  1 64  ? 46.795  16.681  70.257  1.00 61.37  ? 64   TRP C CZ3 1 
ATOM   7515  C  CH2 . TRP B  1 64  ? 45.465  16.571  70.680  1.00 65.60  ? 64   TRP C CH2 1 
ATOM   7516  N  N   . GLN B  1 65  ? 47.821  11.509  67.802  1.00 71.23  ? 65   GLN C N   1 
ATOM   7517  C  CA  . GLN B  1 65  ? 47.353  10.131  67.821  1.00 69.00  ? 65   GLN C CA  1 
ATOM   7518  C  C   . GLN B  1 65  ? 45.899  10.021  68.266  1.00 66.60  ? 65   GLN C C   1 
ATOM   7519  O  O   . GLN B  1 65  ? 45.261  9.001   68.018  1.00 68.60  ? 65   GLN C O   1 
ATOM   7520  C  CB  . GLN B  1 65  ? 48.254  9.267   68.718  1.00 68.23  ? 65   GLN C CB  1 
ATOM   7521  C  CG  . GLN B  1 65  ? 48.637  9.908   70.036  1.00 72.93  ? 65   GLN C CG  1 
ATOM   7522  C  CD  . GLN B  1 65  ? 50.117  9.735   70.374  1.00 82.44  ? 65   GLN C CD  1 
ATOM   7523  O  OE1 . GLN B  1 65  ? 50.644  8.615   70.379  1.00 64.98  ? 65   GLN C OE1 1 
ATOM   7524  N  NE2 . GLN B  1 65  ? 50.795  10.854  70.659  1.00 80.86  ? 65   GLN C NE2 1 
ATOM   7525  N  N   A GLU B  1 66  ? 45.370  11.054  68.913  0.48 65.32  ? 66   GLU C N   1 
ATOM   7526  N  N   B GLU B  1 66  ? 45.386  11.071  68.907  0.52 64.70  ? 66   GLU C N   1 
ATOM   7527  C  CA  A GLU B  1 66  ? 44.009  10.966  69.433  0.48 64.51  ? 66   GLU C CA  1 
ATOM   7528  C  CA  B GLU B  1 66  ? 44.012  11.081  69.407  0.52 64.62  ? 66   GLU C CA  1 
ATOM   7529  C  C   A GLU B  1 66  ? 42.965  11.166  68.336  0.48 65.56  ? 66   GLU C C   1 
ATOM   7530  C  C   B GLU B  1 66  ? 42.999  11.106  68.257  0.52 66.44  ? 66   GLU C C   1 
ATOM   7531  O  O   A GLU B  1 66  ? 43.133  11.984  67.427  0.48 66.47  ? 66   GLU C O   1 
ATOM   7532  O  O   B GLU B  1 66  ? 43.228  11.748  67.225  0.52 66.46  ? 66   GLU C O   1 
ATOM   7533  C  CB  A GLU B  1 66  ? 43.792  11.971  70.567  0.48 65.85  ? 66   GLU C CB  1 
ATOM   7534  C  CB  B GLU B  1 66  ? 43.782  12.282  70.342  0.52 65.63  ? 66   GLU C CB  1 
ATOM   7535  C  CG  A GLU B  1 66  ? 44.465  11.572  71.881  0.48 65.27  ? 66   GLU C CG  1 
ATOM   7536  C  CG  B GLU B  1 66  ? 44.429  12.155  71.734  0.52 65.84  ? 66   GLU C CG  1 
ATOM   7537  C  CD  A GLU B  1 66  ? 44.382  10.078  72.154  0.48 63.70  ? 66   GLU C CD  1 
ATOM   7538  C  CD  B GLU B  1 66  ? 44.107  13.329  72.658  0.52 63.59  ? 66   GLU C CD  1 
ATOM   7539  O  OE1 A GLU B  1 66  ? 43.262  9.553   72.334  0.48 59.91  ? 66   GLU C OE1 1 
ATOM   7540  O  OE1 B GLU B  1 66  ? 42.927  13.726  72.732  0.52 62.40  ? 66   GLU C OE1 1 
ATOM   7541  O  OE2 A GLU B  1 66  ? 45.447  9.426   72.181  0.48 64.83  ? 66   GLU C OE2 1 
ATOM   7542  O  OE2 B GLU B  1 66  ? 45.034  13.858  73.312  0.52 60.39  ? 66   GLU C OE2 1 
ATOM   7543  N  N   . LEU B  1 67  ? 41.887  10.396  68.436  1.00 63.53  ? 67   LEU C N   1 
ATOM   7544  C  CA  . LEU B  1 67  ? 40.817  10.399  67.454  1.00 55.66  ? 67   LEU C CA  1 
ATOM   7545  C  C   . LEU B  1 67  ? 40.021  11.698  67.503  1.00 54.98  ? 67   LEU C C   1 
ATOM   7546  O  O   . LEU B  1 67  ? 39.400  12.089  66.526  1.00 57.49  ? 67   LEU C O   1 
ATOM   7547  C  CB  . LEU B  1 67  ? 39.893  9.215   67.686  1.00 58.57  ? 67   LEU C CB  1 
ATOM   7548  C  CG  . LEU B  1 67  ? 38.834  9.025   66.619  1.00 57.17  ? 67   LEU C CG  1 
ATOM   7549  C  CD1 . LEU B  1 67  ? 39.496  8.405   65.412  1.00 57.99  ? 67   LEU C CD1 1 
ATOM   7550  C  CD2 . LEU B  1 67  ? 37.701  8.168   67.137  1.00 57.34  ? 67   LEU C CD2 1 
ATOM   7551  N  N   . ARG B  1 68  ? 40.023  12.364  68.648  1.00 54.01  ? 68   ARG C N   1 
ATOM   7552  C  CA  . ARG B  1 68  ? 39.459  13.696  68.705  1.00 55.90  ? 68   ARG C CA  1 
ATOM   7553  C  C   . ARG B  1 68  ? 40.522  14.675  68.262  1.00 59.32  ? 68   ARG C C   1 
ATOM   7554  O  O   . ARG B  1 68  ? 41.718  14.399  68.367  1.00 59.49  ? 68   ARG C O   1 
ATOM   7555  C  CB  . ARG B  1 68  ? 38.965  14.047  70.106  1.00 52.15  ? 68   ARG C CB  1 
ATOM   7556  C  CG  . ARG B  1 68  ? 37.815  13.199  70.588  1.00 50.51  ? 68   ARG C CG  1 
ATOM   7557  C  CD  . ARG B  1 68  ? 36.519  13.551  69.884  1.00 48.00  ? 68   ARG C CD  1 
ATOM   7558  N  NE  . ARG B  1 68  ? 35.887  14.736  70.451  1.00 50.03  ? 68   ARG C NE  1 
ATOM   7559  C  CZ  . ARG B  1 68  ? 35.201  14.745  71.592  1.00 51.05  ? 68   ARG C CZ  1 
ATOM   7560  N  NH1 . ARG B  1 68  ? 35.054  13.634  72.308  1.00 45.17  ? 68   ARG C NH1 1 
ATOM   7561  N  NH2 . ARG B  1 68  ? 34.658  15.875  72.020  1.00 52.77  ? 68   ARG C NH2 1 
ATOM   7562  N  N   . LEU B  1 69  ? 40.073  15.817  67.758  1.00 61.69  ? 69   LEU C N   1 
ATOM   7563  C  CA  . LEU B  1 69  ? 40.968  16.880  67.323  1.00 63.05  ? 69   LEU C CA  1 
ATOM   7564  C  C   . LEU B  1 69  ? 41.600  17.553  68.529  1.00 64.51  ? 69   LEU C C   1 
ATOM   7565  O  O   . LEU B  1 69  ? 41.052  17.497  69.631  1.00 59.31  ? 69   LEU C O   1 
ATOM   7566  C  CB  . LEU B  1 69  ? 40.210  17.921  66.481  1.00 57.28  ? 69   LEU C CB  1 
ATOM   7567  C  CG  . LEU B  1 69  ? 39.673  17.479  65.111  1.00 58.86  ? 69   LEU C CG  1 
ATOM   7568  C  CD1 . LEU B  1 69  ? 38.883  18.594  64.426  1.00 48.34  ? 69   LEU C CD1 1 
ATOM   7569  C  CD2 . LEU B  1 69  ? 40.791  16.958  64.192  1.00 52.17  ? 69   LEU C CD2 1 
ATOM   7570  N  N   . PRO B  1 70  ? 42.755  18.196  68.322  1.00 63.91  ? 70   PRO C N   1 
ATOM   7571  C  CA  . PRO B  1 70  ? 43.271  19.105  69.339  1.00 58.25  ? 70   PRO C CA  1 
ATOM   7572  C  C   . PRO B  1 70  ? 42.245  20.191  69.617  1.00 61.80  ? 70   PRO C C   1 
ATOM   7573  O  O   . PRO B  1 70  ? 41.376  20.431  68.786  1.00 62.84  ? 70   PRO C O   1 
ATOM   7574  C  CB  . PRO B  1 70  ? 44.532  19.683  68.695  1.00 57.70  ? 70   PRO C CB  1 
ATOM   7575  C  CG  . PRO B  1 70  ? 44.934  18.684  67.668  1.00 61.97  ? 70   PRO C CG  1 
ATOM   7576  C  CD  . PRO B  1 70  ? 43.652  18.101  67.157  1.00 66.45  ? 70   PRO C CD  1 
ATOM   7577  N  N   . SER B  1 71  ? 42.324  20.824  70.779  1.00 68.33  ? 71   SER C N   1 
ATOM   7578  C  CA  . SER B  1 71  ? 41.392  21.888  71.111  1.00 68.35  ? 71   SER C CA  1 
ATOM   7579  C  C   . SER B  1 71  ? 42.084  23.230  70.888  1.00 70.89  ? 71   SER C C   1 
ATOM   7580  O  O   . SER B  1 71  ? 41.456  24.291  70.917  1.00 71.46  ? 71   SER C O   1 
ATOM   7581  C  CB  . SER B  1 71  ? 40.903  21.746  72.555  1.00 68.19  ? 71   SER C CB  1 
ATOM   7582  O  OG  . SER B  1 71  ? 39.917  22.722  72.840  1.00 68.88  ? 71   SER C OG  1 
ATOM   7583  N  N   . VAL B  1 72  ? 43.388  23.150  70.642  1.00 70.89  ? 72   VAL C N   1 
ATOM   7584  C  CA  . VAL B  1 72  ? 44.266  24.305  70.491  1.00 75.49  ? 72   VAL C CA  1 
ATOM   7585  C  C   . VAL B  1 72  ? 43.841  25.307  69.396  1.00 77.15  ? 72   VAL C C   1 
ATOM   7586  O  O   . VAL B  1 72  ? 43.777  26.517  69.640  1.00 76.79  ? 72   VAL C O   1 
ATOM   7587  C  CB  . VAL B  1 72  ? 45.707  23.820  70.205  1.00 76.66  ? 72   VAL C CB  1 
ATOM   7588  C  CG1 . VAL B  1 72  ? 46.542  24.939  69.620  1.00 82.43  ? 72   VAL C CG1 1 
ATOM   7589  C  CG2 . VAL B  1 72  ? 46.344  23.253  71.477  1.00 73.61  ? 72   VAL C CG2 1 
ATOM   7590  N  N   . VAL B  1 73  ? 43.550  24.799  68.199  1.00 76.48  ? 73   VAL C N   1 
ATOM   7591  C  CA  . VAL B  1 73  ? 43.241  25.637  67.038  1.00 69.45  ? 73   VAL C CA  1 
ATOM   7592  C  C   . VAL B  1 73  ? 41.737  25.687  66.763  1.00 63.76  ? 73   VAL C C   1 
ATOM   7593  O  O   . VAL B  1 73  ? 41.111  24.653  66.529  1.00 66.70  ? 73   VAL C O   1 
ATOM   7594  C  CB  . VAL B  1 73  ? 43.981  25.119  65.795  1.00 70.60  ? 73   VAL C CB  1 
ATOM   7595  C  CG1 . VAL B  1 73  ? 43.425  25.749  64.534  1.00 69.71  ? 73   VAL C CG1 1 
ATOM   7596  C  CG2 . VAL B  1 73  ? 45.488  25.356  65.922  1.00 71.50  ? 73   VAL C CG2 1 
ATOM   7597  N  N   . ILE B  1 74  ? 41.163  26.885  66.786  1.00 58.55  ? 74   ILE C N   1 
ATOM   7598  C  CA  . ILE B  1 74  ? 39.705  27.043  66.775  1.00 60.81  ? 74   ILE C CA  1 
ATOM   7599  C  C   . ILE B  1 74  ? 39.147  27.789  65.565  1.00 60.39  ? 74   ILE C C   1 
ATOM   7600  O  O   . ILE B  1 74  ? 39.382  28.985  65.406  1.00 61.84  ? 74   ILE C O   1 
ATOM   7601  C  CB  . ILE B  1 74  ? 39.220  27.795  68.032  1.00 60.56  ? 74   ILE C CB  1 
ATOM   7602  C  CG1 . ILE B  1 74  ? 39.496  26.970  69.290  1.00 68.80  ? 74   ILE C CG1 1 
ATOM   7603  C  CG2 . ILE B  1 74  ? 37.739  28.136  67.916  1.00 51.50  ? 74   ILE C CG2 1 
ATOM   7604  C  CD1 . ILE B  1 74  ? 40.361  27.686  70.318  1.00 68.32  ? 74   ILE C CD1 1 
ATOM   7605  N  N   . PRO B  1 75  ? 38.380  27.088  64.718  1.00 63.12  ? 75   PRO C N   1 
ATOM   7606  C  CA  . PRO B  1 75  ? 37.726  27.690  63.543  1.00 60.60  ? 75   PRO C CA  1 
ATOM   7607  C  C   . PRO B  1 75  ? 36.675  28.718  63.903  1.00 48.11  ? 75   PRO C C   1 
ATOM   7608  O  O   . PRO B  1 75  ? 35.839  28.469  64.749  1.00 47.67  ? 75   PRO C O   1 
ATOM   7609  C  CB  . PRO B  1 75  ? 37.066  26.487  62.843  1.00 58.53  ? 75   PRO C CB  1 
ATOM   7610  C  CG  . PRO B  1 75  ? 36.931  25.449  63.913  1.00 56.23  ? 75   PRO C CG  1 
ATOM   7611  C  CD  . PRO B  1 75  ? 38.163  25.632  64.773  1.00 60.43  ? 75   PRO C CD  1 
ATOM   7612  N  N   . LEU B  1 76  ? 36.709  29.857  63.231  1.00 54.90  ? 76   LEU C N   1 
ATOM   7613  C  CA  . LEU B  1 76  ? 35.726  30.900  63.451  1.00 52.96  ? 76   LEU C CA  1 
ATOM   7614  C  C   . LEU B  1 76  ? 34.871  31.089  62.206  1.00 51.02  ? 76   LEU C C   1 
ATOM   7615  O  O   . LEU B  1 76  ? 33.661  31.365  62.292  1.00 46.16  ? 76   LEU C O   1 
ATOM   7616  C  CB  . LEU B  1 76  ? 36.422  32.212  63.829  1.00 55.39  ? 76   LEU C CB  1 
ATOM   7617  C  CG  . LEU B  1 76  ? 37.485  32.083  64.928  1.00 59.50  ? 76   LEU C CG  1 
ATOM   7618  C  CD1 . LEU B  1 76  ? 38.221  33.393  65.171  1.00 61.60  ? 76   LEU C CD1 1 
ATOM   7619  C  CD2 . LEU B  1 76  ? 36.841  31.607  66.208  1.00 58.13  ? 76   LEU C CD2 1 
ATOM   7620  N  N   . HIS B  1 77  ? 35.510  30.943  61.044  1.00 50.65  ? 77   HIS C N   1 
ATOM   7621  C  CA  . HIS B  1 77  ? 34.854  31.246  59.763  1.00 53.96  ? 77   HIS C CA  1 
ATOM   7622  C  C   . HIS B  1 77  ? 35.384  30.425  58.562  1.00 47.59  ? 77   HIS C C   1 
ATOM   7623  O  O   . HIS B  1 77  ? 36.600  30.301  58.353  1.00 43.41  ? 77   HIS C O   1 
ATOM   7624  C  CB  . HIS B  1 77  ? 34.977  32.750  59.459  1.00 46.66  ? 77   HIS C CB  1 
ATOM   7625  C  CG  . HIS B  1 77  ? 34.204  33.180  58.251  1.00 47.65  ? 77   HIS C CG  1 
ATOM   7626  N  ND1 . HIS B  1 77  ? 32.907  33.644  58.324  1.00 49.67  ? 77   HIS C ND1 1 
ATOM   7627  C  CD2 . HIS B  1 77  ? 34.535  33.193  56.938  1.00 44.78  ? 77   HIS C CD2 1 
ATOM   7628  C  CE1 . HIS B  1 77  ? 32.475  33.930  57.109  1.00 48.08  ? 77   HIS C CE1 1 
ATOM   7629  N  NE2 . HIS B  1 77  ? 33.445  33.670  56.250  1.00 45.82  ? 77   HIS C NE2 1 
ATOM   7630  N  N   . TYR B  1 78  ? 34.448  29.857  57.801  1.00 44.79  ? 78   TYR C N   1 
ATOM   7631  C  CA  . TYR B  1 78  ? 34.754  29.141  56.552  1.00 47.59  ? 78   TYR C CA  1 
ATOM   7632  C  C   . TYR B  1 78  ? 34.300  29.933  55.342  1.00 41.31  ? 78   TYR C C   1 
ATOM   7633  O  O   . TYR B  1 78  ? 33.110  30.231  55.188  1.00 39.69  ? 78   TYR C O   1 
ATOM   7634  C  CB  . TYR B  1 78  ? 34.066  27.767  56.481  1.00 49.05  ? 78   TYR C CB  1 
ATOM   7635  C  CG  . TYR B  1 78  ? 34.560  26.716  57.447  1.00 49.33  ? 78   TYR C CG  1 
ATOM   7636  C  CD1 . TYR B  1 78  ? 34.070  26.664  58.744  1.00 43.22  ? 78   TYR C CD1 1 
ATOM   7637  C  CD2 . TYR B  1 78  ? 35.505  25.761  57.056  1.00 43.07  ? 78   TYR C CD2 1 
ATOM   7638  C  CE1 . TYR B  1 78  ? 34.504  25.694  59.633  1.00 46.81  ? 78   TYR C CE1 1 
ATOM   7639  C  CE2 . TYR B  1 78  ? 35.960  24.793  57.949  1.00 44.18  ? 78   TYR C CE2 1 
ATOM   7640  C  CZ  . TYR B  1 78  ? 35.449  24.766  59.241  1.00 41.25  ? 78   TYR C CZ  1 
ATOM   7641  O  OH  . TYR B  1 78  ? 35.868  23.817  60.154  1.00 40.46  ? 78   TYR C OH  1 
ATOM   7642  N  N   . ASP B  1 79  ? 35.243  30.279  54.480  1.00 44.45  ? 79   ASP C N   1 
ATOM   7643  C  CA  . ASP B  1 79  ? 34.895  30.723  53.133  1.00 44.60  ? 79   ASP C CA  1 
ATOM   7644  C  C   . ASP B  1 79  ? 34.911  29.501  52.211  1.00 40.35  ? 79   ASP C C   1 
ATOM   7645  O  O   . ASP B  1 79  ? 35.978  28.921  51.978  1.00 38.69  ? 79   ASP C O   1 
ATOM   7646  C  CB  . ASP B  1 79  ? 35.874  31.786  52.640  1.00 45.67  ? 79   ASP C CB  1 
ATOM   7647  C  CG  . ASP B  1 79  ? 35.561  33.159  53.186  1.00 54.11  ? 79   ASP C CG  1 
ATOM   7648  O  OD1 . ASP B  1 79  ? 34.365  33.530  53.201  1.00 57.93  ? 79   ASP C OD1 1 
ATOM   7649  O  OD2 . ASP B  1 79  ? 36.506  33.864  53.608  1.00 60.98  ? 79   ASP C OD2 1 
ATOM   7650  N  N   . LEU B  1 80  ? 33.751  29.081  51.713  1.00 29.43  ? 80   LEU C N   1 
ATOM   7651  C  CA  . LEU B  1 80  ? 33.744  27.867  50.901  1.00 35.91  ? 80   LEU C CA  1 
ATOM   7652  C  C   . LEU B  1 80  ? 33.276  28.061  49.452  1.00 38.89  ? 80   LEU C C   1 
ATOM   7653  O  O   . LEU B  1 80  ? 32.175  28.575  49.207  1.00 33.36  ? 80   LEU C O   1 
ATOM   7654  C  CB  . LEU B  1 80  ? 32.883  26.804  51.561  1.00 32.32  ? 80   LEU C CB  1 
ATOM   7655  C  CG  . LEU B  1 80  ? 32.820  25.503  50.764  1.00 37.49  ? 80   LEU C CG  1 
ATOM   7656  C  CD1 . LEU B  1 80  ? 34.149  24.715  50.845  1.00 38.97  ? 80   LEU C CD1 1 
ATOM   7657  C  CD2 . LEU B  1 80  ? 31.633  24.659  51.193  1.00 35.18  ? 80   LEU C CD2 1 
ATOM   7658  N  N   . PHE B  1 81  ? 34.097  27.616  48.498  1.00 30.68  ? 81   PHE C N   1 
ATOM   7659  C  CA  . PHE B  1 81  ? 33.703  27.672  47.092  1.00 37.01  ? 81   PHE C CA  1 
ATOM   7660  C  C   . PHE B  1 81  ? 33.623  26.275  46.461  1.00 38.96  ? 81   PHE C C   1 
ATOM   7661  O  O   . PHE B  1 81  ? 34.608  25.529  46.439  1.00 33.38  ? 81   PHE C O   1 
ATOM   7662  C  CB  . PHE B  1 81  ? 34.672  28.559  46.295  1.00 37.14  ? 81   PHE C CB  1 
ATOM   7663  C  CG  . PHE B  1 81  ? 34.567  28.385  44.809  1.00 40.16  ? 81   PHE C CG  1 
ATOM   7664  C  CD1 . PHE B  1 81  ? 33.499  28.947  44.099  1.00 36.66  ? 81   PHE C CD1 1 
ATOM   7665  C  CD2 . PHE B  1 81  ? 35.522  27.644  44.115  1.00 38.46  ? 81   PHE C CD2 1 
ATOM   7666  C  CE1 . PHE B  1 81  ? 33.389  28.780  42.723  1.00 37.15  ? 81   PHE C CE1 1 
ATOM   7667  C  CE2 . PHE B  1 81  ? 35.429  27.482  42.729  1.00 43.47  ? 81   PHE C CE2 1 
ATOM   7668  C  CZ  . PHE B  1 81  ? 34.361  28.054  42.034  1.00 42.40  ? 81   PHE C CZ  1 
ATOM   7669  N  N   . VAL B  1 82  ? 32.450  25.933  45.932  1.00 35.95  ? 82   VAL C N   1 
ATOM   7670  C  CA  . VAL B  1 82  ? 32.254  24.621  45.337  1.00 38.97  ? 82   VAL C CA  1 
ATOM   7671  C  C   . VAL B  1 82  ? 31.946  24.742  43.845  1.00 39.55  ? 82   VAL C C   1 
ATOM   7672  O  O   . VAL B  1 82  ? 31.051  25.490  43.443  1.00 35.18  ? 82   VAL C O   1 
ATOM   7673  C  CB  . VAL B  1 82  ? 31.113  23.832  46.035  1.00 38.15  ? 82   VAL C CB  1 
ATOM   7674  C  CG1 . VAL B  1 82  ? 30.996  22.415  45.444  1.00 31.18  ? 82   VAL C CG1 1 
ATOM   7675  C  CG2 . VAL B  1 82  ? 31.362  23.752  47.532  1.00 40.34  ? 82   VAL C CG2 1 
ATOM   7676  N  N   . HIS B  1 83  ? 32.693  23.996  43.035  1.00 36.04  ? 83   HIS C N   1 
ATOM   7677  C  CA  . HIS B  1 83  ? 32.472  23.976  41.597  1.00 37.68  ? 83   HIS C CA  1 
ATOM   7678  C  C   . HIS B  1 83  ? 32.207  22.549  41.134  1.00 40.87  ? 83   HIS C C   1 
ATOM   7679  O  O   . HIS B  1 83  ? 33.122  21.836  40.688  1.00 38.51  ? 83   HIS C O   1 
ATOM   7680  C  CB  . HIS B  1 83  ? 33.667  24.553  40.868  1.00 34.98  ? 83   HIS C CB  1 
ATOM   7681  C  CG  . HIS B  1 83  ? 33.480  24.650  39.392  1.00 42.30  ? 83   HIS C CG  1 
ATOM   7682  N  ND1 . HIS B  1 83  ? 34.522  24.906  38.524  1.00 41.33  ? 83   HIS C ND1 1 
ATOM   7683  C  CD2 . HIS B  1 83  ? 32.370  24.542  38.625  1.00 43.05  ? 83   HIS C CD2 1 
ATOM   7684  C  CE1 . HIS B  1 83  ? 34.060  24.951  37.290  1.00 38.17  ? 83   HIS C CE1 1 
ATOM   7685  N  NE2 . HIS B  1 83  ? 32.758  24.737  37.323  1.00 34.43  ? 83   HIS C NE2 1 
ATOM   7686  N  N   . PRO B  1 84  ? 30.952  22.115  41.271  1.00 35.72  ? 84   PRO C N   1 
ATOM   7687  C  CA  . PRO B  1 84  ? 30.541  20.789  40.814  1.00 37.33  ? 84   PRO C CA  1 
ATOM   7688  C  C   . PRO B  1 84  ? 30.266  20.762  39.307  1.00 37.74  ? 84   PRO C C   1 
ATOM   7689  O  O   . PRO B  1 84  ? 29.770  21.733  38.726  1.00 33.02  ? 84   PRO C O   1 
ATOM   7690  C  CB  . PRO B  1 84  ? 29.257  20.519  41.616  1.00 29.50  ? 84   PRO C CB  1 
ATOM   7691  C  CG  . PRO B  1 84  ? 28.748  21.856  42.010  1.00 27.90  ? 84   PRO C CG  1 
ATOM   7692  C  CD  . PRO B  1 84  ? 29.815  22.902  41.758  1.00 28.93  ? 84   PRO C CD  1 
ATOM   7693  N  N   . ASN B  1 85  ? 30.590  19.639  38.683  1.00 34.31  ? 85   ASN C N   1 
ATOM   7694  C  CA  . ASN B  1 85  ? 30.149  19.407  37.321  1.00 32.83  ? 85   ASN C CA  1 
ATOM   7695  C  C   . ASN B  1 85  ? 29.289  18.139  37.227  1.00 28.16  ? 85   ASN C C   1 
ATOM   7696  O  O   . ASN B  1 85  ? 29.751  17.041  37.502  1.00 33.72  ? 85   ASN C O   1 
ATOM   7697  C  CB  . ASN B  1 85  ? 31.345  19.318  36.372  1.00 35.15  ? 85   ASN C CB  1 
ATOM   7698  C  CG  . ASN B  1 85  ? 30.916  19.381  34.934  1.00 35.70  ? 85   ASN C CG  1 
ATOM   7699  O  OD1 . ASN B  1 85  ? 30.235  18.472  34.439  1.00 37.99  ? 85   ASN C OD1 1 
ATOM   7700  N  ND2 . ASN B  1 85  ? 31.286  20.443  34.256  1.00 31.80  ? 85   ASN C ND2 1 
ATOM   7701  N  N   . LEU B  1 86  ? 28.040  18.295  36.823  1.00 26.10  ? 86   LEU C N   1 
ATOM   7702  C  CA  . LEU B  1 86  ? 27.123  17.167  36.815  1.00 34.04  ? 86   LEU C CA  1 
ATOM   7703  C  C   . LEU B  1 86  ? 27.178  16.437  35.484  1.00 42.76  ? 86   LEU C C   1 
ATOM   7704  O  O   . LEU B  1 86  ? 26.424  15.489  35.281  1.00 47.06  ? 86   LEU C O   1 
ATOM   7705  C  CB  . LEU B  1 86  ? 25.673  17.591  37.114  1.00 36.31  ? 86   LEU C CB  1 
ATOM   7706  C  CG  . LEU B  1 86  ? 25.380  18.608  38.247  1.00 40.66  ? 86   LEU C CG  1 
ATOM   7707  C  CD1 . LEU B  1 86  ? 23.938  18.518  38.726  1.00 28.15  ? 86   LEU C CD1 1 
ATOM   7708  C  CD2 . LEU B  1 86  ? 26.331  18.517  39.413  1.00 32.69  ? 86   LEU C CD2 1 
ATOM   7709  N  N   . THR B  1 87  ? 28.053  16.862  34.571  1.00 39.58  ? 87   THR C N   1 
ATOM   7710  C  CA  . THR B  1 87  ? 28.274  16.077  33.356  1.00 33.61  ? 87   THR C CA  1 
ATOM   7711  C  C   . THR B  1 87  ? 29.443  15.112  33.591  1.00 37.96  ? 87   THR C C   1 
ATOM   7712  O  O   . THR B  1 87  ? 29.291  13.910  33.417  1.00 39.77  ? 87   THR C O   1 
ATOM   7713  C  CB  . THR B  1 87  ? 28.538  16.980  32.133  1.00 38.46  ? 87   THR C CB  1 
ATOM   7714  O  OG1 . THR B  1 87  ? 27.355  17.749  31.854  1.00 42.44  ? 87   THR C OG1 1 
ATOM   7715  C  CG2 . THR B  1 87  ? 28.926  16.159  30.915  1.00 34.09  ? 87   THR C CG2 1 
ATOM   7716  N  N   . SER B  1 88  ? 30.599  15.622  34.012  1.00 35.08  ? 88   SER C N   1 
ATOM   7717  C  CA  . SER B  1 88  ? 31.715  14.742  34.333  1.00 33.74  ? 88   SER C CA  1 
ATOM   7718  C  C   . SER B  1 88  ? 31.634  14.176  35.766  1.00 34.71  ? 88   SER C C   1 
ATOM   7719  O  O   . SER B  1 88  ? 32.560  13.514  36.232  1.00 32.74  ? 88   SER C O   1 
ATOM   7720  C  CB  . SER B  1 88  ? 33.044  15.470  34.137  1.00 35.60  ? 88   SER C CB  1 
ATOM   7721  O  OG  . SER B  1 88  ? 33.302  16.396  35.178  1.00 41.71  ? 88   SER C OG  1 
ATOM   7722  N  N   . LEU B  1 89  ? 30.534  14.454  36.461  1.00 36.50  ? 89   LEU C N   1 
ATOM   7723  C  CA  . LEU B  1 89  ? 30.293  13.895  37.797  1.00 41.78  ? 89   LEU C CA  1 
ATOM   7724  C  C   . LEU B  1 89  ? 31.410  14.073  38.851  1.00 36.66  ? 89   LEU C C   1 
ATOM   7725  O  O   . LEU B  1 89  ? 31.645  13.185  39.665  1.00 35.73  ? 89   LEU C O   1 
ATOM   7726  C  CB  . LEU B  1 89  ? 29.984  12.399  37.660  1.00 37.14  ? 89   LEU C CB  1 
ATOM   7727  C  CG  . LEU B  1 89  ? 28.808  12.055  36.741  1.00 36.35  ? 89   LEU C CG  1 
ATOM   7728  C  CD1 . LEU B  1 89  ? 28.400  10.619  36.944  1.00 39.83  ? 89   LEU C CD1 1 
ATOM   7729  C  CD2 . LEU B  1 89  ? 27.637  12.978  36.995  1.00 38.87  ? 89   LEU C CD2 1 
ATOM   7730  N  N   . ASP B  1 90  ? 32.080  15.217  38.851  1.00 36.38  ? 90   ASP C N   1 
ATOM   7731  C  CA  . ASP B  1 90  ? 33.087  15.505  39.879  1.00 37.07  ? 90   ASP C CA  1 
ATOM   7732  C  C   . ASP B  1 90  ? 32.989  16.961  40.339  1.00 35.43  ? 90   ASP C C   1 
ATOM   7733  O  O   . ASP B  1 90  ? 32.089  17.710  39.930  1.00 32.95  ? 90   ASP C O   1 
ATOM   7734  C  CB  . ASP B  1 90  ? 34.493  15.206  39.356  1.00 35.11  ? 90   ASP C CB  1 
ATOM   7735  C  CG  . ASP B  1 90  ? 34.740  15.805  37.989  1.00 41.23  ? 90   ASP C CG  1 
ATOM   7736  O  OD1 . ASP B  1 90  ? 33.990  16.726  37.605  1.00 42.29  ? 90   ASP C OD1 1 
ATOM   7737  O  OD2 . ASP B  1 90  ? 35.670  15.359  37.285  1.00 44.13  ? 90   ASP C OD2 1 
ATOM   7738  N  N   . PHE B  1 91  ? 33.915  17.385  41.179  1.00 31.36  ? 91   PHE C N   1 
ATOM   7739  C  CA  . PHE B  1 91  ? 33.885  18.777  41.573  1.00 31.71  ? 91   PHE C CA  1 
ATOM   7740  C  C   . PHE B  1 91  ? 35.268  19.245  41.920  1.00 33.38  ? 91   PHE C C   1 
ATOM   7741  O  O   . PHE B  1 91  ? 36.149  18.438  42.230  1.00 32.34  ? 91   PHE C O   1 
ATOM   7742  C  CB  . PHE B  1 91  ? 32.942  18.995  42.762  1.00 33.38  ? 91   PHE C CB  1 
ATOM   7743  C  CG  . PHE B  1 91  ? 33.427  18.378  44.046  1.00 34.20  ? 91   PHE C CG  1 
ATOM   7744  C  CD1 . PHE B  1 91  ? 33.085  17.068  44.376  1.00 34.00  ? 91   PHE C CD1 1 
ATOM   7745  C  CD2 . PHE B  1 91  ? 34.213  19.108  44.935  1.00 35.85  ? 91   PHE C CD2 1 
ATOM   7746  C  CE1 . PHE B  1 91  ? 33.530  16.485  45.549  1.00 34.81  ? 91   PHE C CE1 1 
ATOM   7747  C  CE2 . PHE B  1 91  ? 34.656  18.531  46.124  1.00 38.77  ? 91   PHE C CE2 1 
ATOM   7748  C  CZ  . PHE B  1 91  ? 34.313  17.215  46.429  1.00 37.77  ? 91   PHE C CZ  1 
ATOM   7749  N  N   . VAL B  1 92  ? 35.452  20.556  41.846  1.00 31.77  ? 92   VAL C N   1 
ATOM   7750  C  CA  . VAL B  1 92  ? 36.636  21.197  42.389  1.00 34.49  ? 92   VAL C CA  1 
ATOM   7751  C  C   . VAL B  1 92  ? 36.138  22.255  43.357  1.00 31.93  ? 92   VAL C C   1 
ATOM   7752  O  O   . VAL B  1 92  ? 35.025  22.794  43.222  1.00 30.76  ? 92   VAL C O   1 
ATOM   7753  C  CB  . VAL B  1 92  ? 37.554  21.840  41.290  1.00 39.63  ? 92   VAL C CB  1 
ATOM   7754  C  CG1 . VAL B  1 92  ? 38.065  20.780  40.302  1.00 35.42  ? 92   VAL C CG1 1 
ATOM   7755  C  CG2 . VAL B  1 92  ? 36.817  22.935  40.551  1.00 29.69  ? 92   VAL C CG2 1 
ATOM   7756  N  N   . ALA B  1 93  ? 36.968  22.547  44.344  1.00 34.41  ? 93   ALA C N   1 
ATOM   7757  C  CA  . ALA B  1 93  ? 36.565  23.437  45.420  1.00 37.11  ? 93   ALA C CA  1 
ATOM   7758  C  C   . ALA B  1 93  ? 37.770  24.010  46.124  1.00 38.88  ? 93   ALA C C   1 
ATOM   7759  O  O   . ALA B  1 93  ? 38.874  23.444  46.097  1.00 42.82  ? 93   ALA C O   1 
ATOM   7760  C  CB  . ALA B  1 93  ? 35.678  22.708  46.413  1.00 30.86  ? 93   ALA C CB  1 
ATOM   7761  N  N   . SER B  1 94  ? 37.554  25.151  46.751  1.00 38.06  ? 94   SER C N   1 
ATOM   7762  C  CA  . SER B  1 94  ? 38.570  25.719  47.618  1.00 42.32  ? 94   SER C CA  1 
ATOM   7763  C  C   . SER B  1 94  ? 37.915  26.278  48.860  1.00 37.83  ? 94   SER C C   1 
ATOM   7764  O  O   . SER B  1 94  ? 36.719  26.623  48.864  1.00 36.34  ? 94   SER C O   1 
ATOM   7765  C  CB  . SER B  1 94  ? 39.378  26.804  46.896  1.00 37.21  ? 94   SER C CB  1 
ATOM   7766  O  OG  . SER B  1 94  ? 38.513  27.770  46.345  1.00 48.11  ? 94   SER C OG  1 
ATOM   7767  N  N   . GLU B  1 95  ? 38.697  26.366  49.923  1.00 41.13  ? 95   GLU C N   1 
ATOM   7768  C  CA  . GLU B  1 95  ? 38.196  26.999  51.138  1.00 41.28  ? 95   GLU C CA  1 
ATOM   7769  C  C   . GLU B  1 95  ? 39.273  27.862  51.774  1.00 37.93  ? 95   GLU C C   1 
ATOM   7770  O  O   . GLU B  1 95  ? 40.475  27.581  51.656  1.00 37.91  ? 95   GLU C O   1 
ATOM   7771  C  CB  . GLU B  1 95  ? 37.701  25.947  52.135  1.00 36.81  ? 95   GLU C CB  1 
ATOM   7772  C  CG  . GLU B  1 95  ? 38.824  25.094  52.691  1.00 37.80  ? 95   GLU C CG  1 
ATOM   7773  C  CD  . GLU B  1 95  ? 38.364  24.081  53.716  1.00 43.78  ? 95   GLU C CD  1 
ATOM   7774  O  OE1 . GLU B  1 95  ? 37.144  24.033  54.007  1.00 41.41  ? 95   GLU C OE1 1 
ATOM   7775  O  OE2 . GLU B  1 95  ? 39.233  23.336  54.230  1.00 46.03  ? 95   GLU C OE2 1 
ATOM   7776  N  N   . LYS B  1 96  ? 38.829  28.926  52.429  1.00 42.75  ? 96   LYS C N   1 
ATOM   7777  C  CA  . LYS B  1 96  ? 39.681  29.665  53.356  1.00 49.45  ? 96   LYS C CA  1 
ATOM   7778  C  C   . LYS B  1 96  ? 39.061  29.600  54.771  1.00 43.06  ? 96   LYS C C   1 
ATOM   7779  O  O   . LYS B  1 96  ? 37.892  29.987  54.971  1.00 39.95  ? 96   LYS C O   1 
ATOM   7780  C  CB  . LYS B  1 96  ? 39.868  31.112  52.886  1.00 51.05  ? 96   LYS C CB  1 
ATOM   7781  C  CG  . LYS B  1 96  ? 40.920  31.879  53.697  1.00 61.73  ? 96   LYS C CG  1 
ATOM   7782  C  CD  . LYS B  1 96  ? 41.380  33.173  53.023  1.00 60.38  ? 96   LYS C CD  1 
ATOM   7783  C  CE  . LYS B  1 96  ? 40.220  34.139  52.802  1.00 75.50  ? 96   LYS C CE  1 
ATOM   7784  N  NZ  . LYS B  1 96  ? 39.581  34.615  54.076  1.00 66.19  ? 96   LYS C NZ  1 
ATOM   7785  N  N   . ILE B  1 97  ? 39.816  29.075  55.737  1.00 39.65  ? 97   ILE C N   1 
ATOM   7786  C  CA  . ILE B  1 97  ? 39.289  28.937  57.118  1.00 57.32  ? 97   ILE C CA  1 
ATOM   7787  C  C   . ILE B  1 97  ? 39.908  29.927  58.120  1.00 53.92  ? 97   ILE C C   1 
ATOM   7788  O  O   . ILE B  1 97  ? 41.128  29.907  58.382  1.00 46.84  ? 97   ILE C O   1 
ATOM   7789  C  CB  . ILE B  1 97  ? 39.492  27.512  57.723  1.00 50.21  ? 97   ILE C CB  1 
ATOM   7790  C  CG1 . ILE B  1 97  ? 38.963  26.420  56.808  1.00 43.23  ? 97   ILE C CG1 1 
ATOM   7791  C  CG2 . ILE B  1 97  ? 38.775  27.407  59.066  1.00 45.49  ? 97   ILE C CG2 1 
ATOM   7792  C  CD1 . ILE B  1 97  ? 39.345  25.026  57.297  1.00 47.24  ? 97   ILE C CD1 1 
ATOM   7793  N  N   . GLU B  1 98  ? 39.052  30.776  58.683  1.00 51.38  ? 98   GLU C N   1 
ATOM   7794  C  CA  . GLU B  1 98  ? 39.473  31.698  59.728  1.00 57.21  ? 98   GLU C CA  1 
ATOM   7795  C  C   . GLU B  1 98  ? 39.630  31.010  61.094  1.00 53.65  ? 98   GLU C C   1 
ATOM   7796  O  O   . GLU B  1 98  ? 38.665  30.552  61.698  1.00 53.98  ? 98   GLU C O   1 
ATOM   7797  C  CB  . GLU B  1 98  ? 38.495  32.855  59.845  1.00 57.66  ? 98   GLU C CB  1 
ATOM   7798  C  CG  . GLU B  1 98  ? 38.824  33.778  61.000  1.00 64.87  ? 98   GLU C CG  1 
ATOM   7799  C  CD  . GLU B  1 98  ? 38.183  35.125  60.853  1.00 69.91  ? 98   GLU C CD  1 
ATOM   7800  O  OE1 . GLU B  1 98  ? 37.105  35.192  60.227  1.00 69.33  ? 98   GLU C OE1 1 
ATOM   7801  O  OE2 . GLU B  1 98  ? 38.755  36.114  61.362  1.00 80.48  ? 98   GLU C OE2 1 
ATOM   7802  N  N   . VAL B  1 99  ? 40.862  30.968  61.572  1.00 52.94  ? 99   VAL C N   1 
ATOM   7803  C  CA  . VAL B  1 99  ? 41.221  30.202  62.749  1.00 59.45  ? 99   VAL C CA  1 
ATOM   7804  C  C   . VAL B  1 99  ? 41.879  31.057  63.857  1.00 67.88  ? 99   VAL C C   1 
ATOM   7805  O  O   . VAL B  1 99  ? 42.730  31.905  63.582  1.00 72.94  ? 99   VAL C O   1 
ATOM   7806  C  CB  . VAL B  1 99  ? 42.162  29.058  62.328  1.00 59.06  ? 99   VAL C CB  1 
ATOM   7807  C  CG1 . VAL B  1 99  ? 43.298  28.883  63.309  1.00 69.15  ? 99   VAL C CG1 1 
ATOM   7808  C  CG2 . VAL B  1 99  ? 41.379  27.774  62.126  1.00 61.10  ? 99   VAL C CG2 1 
ATOM   7809  N  N   . LEU B  1 100 ? 41.474  30.843  65.107  1.00 71.52  ? 100  LEU C N   1 
ATOM   7810  C  CA  . LEU B  1 100 ? 42.161  31.450  66.247  1.00 67.52  ? 100  LEU C CA  1 
ATOM   7811  C  C   . LEU B  1 100 ? 43.041  30.436  66.968  1.00 69.71  ? 100  LEU C C   1 
ATOM   7812  O  O   . LEU B  1 100 ? 42.556  29.398  67.399  1.00 71.99  ? 100  LEU C O   1 
ATOM   7813  C  CB  . LEU B  1 100 ? 41.165  32.032  67.240  1.00 66.04  ? 100  LEU C CB  1 
ATOM   7814  C  CG  . LEU B  1 100 ? 41.929  32.469  68.489  1.00 73.15  ? 100  LEU C CG  1 
ATOM   7815  C  CD1 . LEU B  1 100 ? 42.292  33.947  68.375  1.00 73.51  ? 100  LEU C CD1 1 
ATOM   7816  C  CD2 . LEU B  1 100 ? 41.176  32.146  69.772  1.00 63.86  ? 100  LEU C CD2 1 
ATOM   7817  N  N   . VAL B  1 101 ? 44.328  30.734  67.113  1.00 73.81  ? 101  VAL C N   1 
ATOM   7818  C  CA  . VAL B  1 101 ? 45.224  29.829  67.833  1.00 76.99  ? 101  VAL C CA  1 
ATOM   7819  C  C   . VAL B  1 101 ? 45.316  30.211  69.310  1.00 81.07  ? 101  VAL C C   1 
ATOM   7820  O  O   . VAL B  1 101 ? 45.785  31.294  69.646  1.00 83.50  ? 101  VAL C O   1 
ATOM   7821  C  CB  . VAL B  1 101 ? 46.633  29.819  67.214  1.00 81.79  ? 101  VAL C CB  1 
ATOM   7822  C  CG1 . VAL B  1 101 ? 47.607  29.084  68.118  1.00 83.39  ? 101  VAL C CG1 1 
ATOM   7823  C  CG2 . VAL B  1 101 ? 46.601  29.175  65.830  1.00 82.68  ? 101  VAL C CG2 1 
ATOM   7824  N  N   . SER B  1 102 ? 44.866  29.324  70.194  1.00 84.83  ? 102  SER C N   1 
ATOM   7825  C  CA  . SER B  1 102 ? 44.792  29.656  71.617  1.00 84.93  ? 102  SER C CA  1 
ATOM   7826  C  C   . SER B  1 102 ? 45.883  28.959  72.436  1.00 84.34  ? 102  SER C C   1 
ATOM   7827  O  O   . SER B  1 102 ? 45.755  28.811  73.648  1.00 90.20  ? 102  SER C O   1 
ATOM   7828  C  CB  . SER B  1 102 ? 43.407  29.309  72.171  1.00 81.55  ? 102  SER C CB  1 
ATOM   7829  O  OG  . SER B  1 102 ? 43.161  27.915  72.112  1.00 79.25  ? 102  SER C OG  1 
ATOM   7830  N  N   . ASN B  1 103 ? 46.953  28.558  71.757  1.00 80.61  ? 103  ASN C N   1 
ATOM   7831  C  CA  . ASN B  1 103 ? 48.107  27.905  72.362  1.00 80.34  ? 103  ASN C CA  1 
ATOM   7832  C  C   . ASN B  1 103 ? 49.094  27.588  71.254  1.00 79.34  ? 103  ASN C C   1 
ATOM   7833  O  O   . ASN B  1 103 ? 48.698  27.093  70.215  1.00 87.00  ? 103  ASN C O   1 
ATOM   7834  C  CB  . ASN B  1 103 ? 47.709  26.625  73.113  1.00 89.71  ? 103  ASN C CB  1 
ATOM   7835  C  CG  . ASN B  1 103 ? 47.955  26.726  74.619  1.00 98.80  ? 103  ASN C CG  1 
ATOM   7836  O  OD1 . ASN B  1 103 ? 48.624  27.647  75.087  1.00 101.46 ? 103  ASN C OD1 1 
ATOM   7837  N  ND2 . ASN B  1 103 ? 47.414  25.773  75.380  1.00 103.62 ? 103  ASN C ND2 1 
ATOM   7838  N  N   . ALA B  1 104 ? 50.372  27.871  71.460  1.00 79.13  ? 104  ALA C N   1 
ATOM   7839  C  CA  . ALA B  1 104 ? 51.364  27.710  70.394  1.00 81.88  ? 104  ALA C CA  1 
ATOM   7840  C  C   . ALA B  1 104 ? 51.491  26.271  69.897  1.00 81.45  ? 104  ALA C C   1 
ATOM   7841  O  O   . ALA B  1 104 ? 51.598  25.342  70.687  1.00 77.29  ? 104  ALA C O   1 
ATOM   7842  C  CB  . ALA B  1 104 ? 52.716  28.213  70.858  1.00 83.82  ? 104  ALA C CB  1 
ATOM   7843  N  N   . THR B  1 105 ? 51.479  26.104  68.578  1.00 84.45  ? 105  THR C N   1 
ATOM   7844  C  CA  . THR B  1 105 ? 51.610  24.790  67.947  1.00 82.52  ? 105  THR C CA  1 
ATOM   7845  C  C   . THR B  1 105 ? 52.426  24.848  66.663  1.00 82.30  ? 105  THR C C   1 
ATOM   7846  O  O   . THR B  1 105 ? 52.516  25.888  66.007  1.00 79.37  ? 105  THR C O   1 
ATOM   7847  C  CB  . THR B  1 105 ? 50.236  24.171  67.596  1.00 80.88  ? 105  THR C CB  1 
ATOM   7848  O  OG1 . THR B  1 105 ? 49.327  25.209  67.206  1.00 84.63  ? 105  THR C OG1 1 
ATOM   7849  C  CG2 . THR B  1 105 ? 49.658  23.416  68.781  1.00 88.27  ? 105  THR C CG2 1 
ATOM   7850  N  N   . GLN B  1 106 ? 53.007  23.714  66.300  1.00 81.68  ? 106  GLN C N   1 
ATOM   7851  C  CA  . GLN B  1 106 ? 53.689  23.597  65.023  1.00 84.03  ? 106  GLN C CA  1 
ATOM   7852  C  C   . GLN B  1 106 ? 52.817  22.874  64.003  1.00 81.73  ? 106  GLN C C   1 
ATOM   7853  O  O   . GLN B  1 106 ? 53.286  22.517  62.922  1.00 81.81  ? 106  GLN C O   1 
ATOM   7854  C  CB  . GLN B  1 106 ? 55.014  22.855  65.176  1.00 87.19  ? 106  GLN C CB  1 
ATOM   7855  C  CG  . GLN B  1 106 ? 55.823  23.267  66.378  1.00 92.80  ? 106  GLN C CG  1 
ATOM   7856  C  CD  . GLN B  1 106 ? 57.301  23.026  66.177  1.00 96.23  ? 106  GLN C CD  1 
ATOM   7857  O  OE1 . GLN B  1 106 ? 57.861  23.374  65.134  1.00 99.26  ? 106  GLN C OE1 1 
ATOM   7858  N  NE2 . GLN B  1 106 ? 57.942  22.417  67.168  1.00 89.08  ? 106  GLN C NE2 1 
ATOM   7859  N  N   . PHE B  1 107 ? 51.552  22.654  64.342  1.00 80.23  ? 107  PHE C N   1 
ATOM   7860  C  CA  . PHE B  1 107 ? 50.667  21.948  63.431  1.00 77.92  ? 107  PHE C CA  1 
ATOM   7861  C  C   . PHE B  1 107 ? 49.183  22.190  63.696  1.00 73.00  ? 107  PHE C C   1 
ATOM   7862  O  O   . PHE B  1 107 ? 48.752  22.338  64.842  1.00 73.41  ? 107  PHE C O   1 
ATOM   7863  C  CB  . PHE B  1 107 ? 50.969  20.443  63.468  1.00 77.51  ? 107  PHE C CB  1 
ATOM   7864  C  CG  . PHE B  1 107 ? 51.115  19.882  64.855  1.00 83.59  ? 107  PHE C CG  1 
ATOM   7865  C  CD1 . PHE B  1 107 ? 52.353  19.856  65.479  1.00 86.44  ? 107  PHE C CD1 1 
ATOM   7866  C  CD2 . PHE B  1 107 ? 50.019  19.369  65.529  1.00 83.38  ? 107  PHE C CD2 1 
ATOM   7867  C  CE1 . PHE B  1 107 ? 52.494  19.340  66.753  1.00 83.04  ? 107  PHE C CE1 1 
ATOM   7868  C  CE2 . PHE B  1 107 ? 50.152  18.846  66.799  1.00 80.16  ? 107  PHE C CE2 1 
ATOM   7869  C  CZ  . PHE B  1 107 ? 51.392  18.831  67.412  1.00 85.70  ? 107  PHE C CZ  1 
ATOM   7870  N  N   . ILE B  1 108 ? 48.416  22.239  62.609  1.00 70.50  ? 108  ILE C N   1 
ATOM   7871  C  CA  . ILE B  1 108 ? 46.962  22.232  62.687  1.00 69.30  ? 108  ILE C CA  1 
ATOM   7872  C  C   . ILE B  1 108 ? 46.431  20.863  62.237  1.00 64.50  ? 108  ILE C C   1 
ATOM   7873  O  O   . ILE B  1 108 ? 46.898  20.304  61.247  1.00 60.25  ? 108  ILE C O   1 
ATOM   7874  C  CB  . ILE B  1 108 ? 46.342  23.344  61.832  1.00 62.15  ? 108  ILE C CB  1 
ATOM   7875  C  CG1 . ILE B  1 108 ? 47.108  24.657  62.032  1.00 62.63  ? 108  ILE C CG1 1 
ATOM   7876  C  CG2 . ILE B  1 108 ? 44.879  23.513  62.181  1.00 61.13  ? 108  ILE C CG2 1 
ATOM   7877  C  CD1 . ILE B  1 108 ? 46.292  25.924  61.786  1.00 54.47  ? 108  ILE C CD1 1 
ATOM   7878  N  N   . ILE B  1 109 ? 45.481  20.312  62.989  1.00 66.18  ? 109  ILE C N   1 
ATOM   7879  C  CA  . ILE B  1 109 ? 44.887  19.026  62.635  1.00 63.11  ? 109  ILE C CA  1 
ATOM   7880  C  C   . ILE B  1 109 ? 43.413  19.228  62.315  1.00 57.45  ? 109  ILE C C   1 
ATOM   7881  O  O   . ILE B  1 109 ? 42.726  20.032  62.949  1.00 55.14  ? 109  ILE C O   1 
ATOM   7882  C  CB  . ILE B  1 109 ? 45.057  17.977  63.756  1.00 65.46  ? 109  ILE C CB  1 
ATOM   7883  C  CG1 . ILE B  1 109 ? 46.513  17.901  64.182  1.00 68.37  ? 109  ILE C CG1 1 
ATOM   7884  C  CG2 . ILE B  1 109 ? 44.670  16.590  63.274  1.00 57.68  ? 109  ILE C CG2 1 
ATOM   7885  C  CD1 . ILE B  1 109 ? 47.393  17.291  63.132  1.00 67.18  ? 109  ILE C CD1 1 
ATOM   7886  N  N   . LEU B  1 110 ? 42.947  18.478  61.322  1.00 52.44  ? 110  LEU C N   1 
ATOM   7887  C  CA  . LEU B  1 110 ? 41.653  18.686  60.690  1.00 46.93  ? 110  LEU C CA  1 
ATOM   7888  C  C   . LEU B  1 110 ? 41.129  17.370  60.217  1.00 44.39  ? 110  LEU C C   1 
ATOM   7889  O  O   . LEU B  1 110 ? 41.909  16.444  60.033  1.00 45.61  ? 110  LEU C O   1 
ATOM   7890  C  CB  . LEU B  1 110 ? 41.788  19.576  59.468  1.00 54.55  ? 110  LEU C CB  1 
ATOM   7891  C  CG  . LEU B  1 110 ? 41.717  21.073  59.515  1.00 53.15  ? 110  LEU C CG  1 
ATOM   7892  C  CD1 . LEU B  1 110 ? 41.938  21.493  58.121  1.00 53.06  ? 110  LEU C CD1 1 
ATOM   7893  C  CD2 . LEU B  1 110 ? 40.349  21.452  59.927  1.00 53.58  ? 110  LEU C CD2 1 
ATOM   7894  N  N   . HIS B  1 111 ? 39.835  17.300  59.934  1.00 40.69  ? 111  HIS C N   1 
ATOM   7895  C  CA  . HIS B  1 111 ? 39.314  16.129  59.227  1.00 43.34  ? 111  HIS C CA  1 
ATOM   7896  C  C   . HIS B  1 111 ? 39.331  16.313  57.700  1.00 49.82  ? 111  HIS C C   1 
ATOM   7897  O  O   . HIS B  1 111 ? 39.175  17.435  57.180  1.00 47.88  ? 111  HIS C O   1 
ATOM   7898  C  CB  . HIS B  1 111 ? 37.890  15.809  59.660  1.00 40.09  ? 111  HIS C CB  1 
ATOM   7899  C  CG  . HIS B  1 111 ? 37.759  15.440  61.101  1.00 47.48  ? 111  HIS C CG  1 
ATOM   7900  N  ND1 . HIS B  1 111 ? 37.283  16.317  62.051  1.00 40.68  ? 111  HIS C ND1 1 
ATOM   7901  C  CD2 . HIS B  1 111 ? 38.036  14.287  61.755  1.00 44.63  ? 111  HIS C CD2 1 
ATOM   7902  C  CE1 . HIS B  1 111 ? 37.262  15.715  63.226  1.00 44.21  ? 111  HIS C CE1 1 
ATOM   7903  N  NE2 . HIS B  1 111 ? 37.713  14.484  63.075  1.00 42.27  ? 111  HIS C NE2 1 
ATOM   7904  N  N   . SER B  1 112 ? 39.504  15.199  56.996  1.00 42.56  ? 112  SER C N   1 
ATOM   7905  C  CA  . SER B  1 112 ? 39.413  15.161  55.547  1.00 45.44  ? 112  SER C CA  1 
ATOM   7906  C  C   . SER B  1 112 ? 39.398  13.710  55.091  1.00 46.31  ? 112  SER C C   1 
ATOM   7907  O  O   . SER B  1 112 ? 40.160  12.891  55.609  1.00 38.87  ? 112  SER C O   1 
ATOM   7908  C  CB  . SER B  1 112 ? 40.580  15.915  54.902  1.00 49.39  ? 112  SER C CB  1 
ATOM   7909  O  OG  . SER B  1 112 ? 40.379  16.059  53.514  1.00 47.85  ? 112  SER C OG  1 
ATOM   7910  N  N   . LYS B  1 113 ? 38.530  13.398  54.131  1.00 39.53  ? 113  LYS C N   1 
ATOM   7911  C  CA  . LYS B  1 113 ? 38.387  12.029  53.668  1.00 42.62  ? 113  LYS C CA  1 
ATOM   7912  C  C   . LYS B  1 113 ? 38.037  11.993  52.181  1.00 42.28  ? 113  LYS C C   1 
ATOM   7913  O  O   . LYS B  1 113 ? 37.122  12.687  51.732  1.00 44.61  ? 113  LYS C O   1 
ATOM   7914  C  CB  . LYS B  1 113 ? 37.323  11.307  54.503  1.00 43.09  ? 113  LYS C CB  1 
ATOM   7915  C  CG  . LYS B  1 113 ? 37.107  9.825   54.175  1.00 39.34  ? 113  LYS C CG  1 
ATOM   7916  C  CD  . LYS B  1 113 ? 36.037  9.286   55.119  1.00 49.81  ? 113  LYS C CD  1 
ATOM   7917  C  CE  . LYS B  1 113 ? 36.068  7.776   55.260  1.00 50.10  ? 113  LYS C CE  1 
ATOM   7918  N  NZ  . LYS B  1 113 ? 35.393  7.096   54.129  1.00 66.14  ? 113  LYS C NZ  1 
ATOM   7919  N  N   . ASP B  1 114 ? 38.786  11.193  51.426  1.00 40.71  ? 114  ASP C N   1 
ATOM   7920  C  CA  . ASP B  1 114 ? 38.563  11.026  49.993  1.00 42.48  ? 114  ASP C CA  1 
ATOM   7921  C  C   . ASP B  1 114 ? 38.590  12.345  49.224  1.00 44.43  ? 114  ASP C C   1 
ATOM   7922  O  O   . ASP B  1 114 ? 37.798  12.564  48.306  1.00 42.44  ? 114  ASP C O   1 
ATOM   7923  C  CB  . ASP B  1 114 ? 37.237  10.316  49.755  1.00 46.89  ? 114  ASP C CB  1 
ATOM   7924  C  CG  . ASP B  1 114 ? 37.197  8.959   50.410  1.00 49.08  ? 114  ASP C CG  1 
ATOM   7925  O  OD1 . ASP B  1 114 ? 38.294  8.403   50.649  1.00 44.07  ? 114  ASP C OD1 1 
ATOM   7926  O  OD2 . ASP B  1 114 ? 36.084  8.458   50.688  1.00 51.47  ? 114  ASP C OD2 1 
ATOM   7927  N  N   . LEU B  1 115 ? 39.499  13.225  49.620  1.00 42.49  ? 115  LEU C N   1 
ATOM   7928  C  CA  . LEU B  1 115 ? 39.645  14.513  48.984  1.00 42.49  ? 115  LEU C CA  1 
ATOM   7929  C  C   . LEU B  1 115 ? 41.077  14.636  48.550  1.00 44.72  ? 115  LEU C C   1 
ATOM   7930  O  O   . LEU B  1 115 ? 41.984  14.321  49.308  1.00 45.14  ? 115  LEU C O   1 
ATOM   7931  C  CB  . LEU B  1 115 ? 39.279  15.652  49.929  1.00 37.89  ? 115  LEU C CB  1 
ATOM   7932  C  CG  . LEU B  1 115 ? 37.815  15.877  50.271  1.00 38.86  ? 115  LEU C CG  1 
ATOM   7933  C  CD1 . LEU B  1 115 ? 37.648  17.091  51.196  1.00 34.62  ? 115  LEU C CD1 1 
ATOM   7934  C  CD2 . LEU B  1 115 ? 37.020  16.047  49.003  1.00 38.80  ? 115  LEU C CD2 1 
ATOM   7935  N  N   . GLU B  1 116 ? 41.288  15.073  47.320  1.00 50.58  ? 116  GLU C N   1 
ATOM   7936  C  CA  . GLU B  1 116 ? 42.640  15.329  46.875  1.00 48.76  ? 116  GLU C CA  1 
ATOM   7937  C  C   . GLU B  1 116 ? 42.931  16.761  47.275  1.00 44.43  ? 116  GLU C C   1 
ATOM   7938  O  O   . GLU B  1 116 ? 42.274  17.681  46.803  1.00 47.18  ? 116  GLU C O   1 
ATOM   7939  C  CB  . GLU B  1 116 ? 42.775  15.099  45.367  1.00 49.70  ? 116  GLU C CB  1 
ATOM   7940  C  CG  . GLU B  1 116 ? 44.166  14.703  44.895  1.00 59.65  ? 116  GLU C CG  1 
ATOM   7941  C  CD  . GLU B  1 116 ? 44.332  14.779  43.372  1.00 64.22  ? 116  GLU C CD  1 
ATOM   7942  O  OE1 . GLU B  1 116 ? 43.389  14.410  42.639  1.00 63.24  ? 116  GLU C OE1 1 
ATOM   7943  O  OE2 . GLU B  1 116 ? 45.407  15.220  42.908  1.00 71.10  ? 116  GLU C OE2 1 
ATOM   7944  N  N   . ILE B  1 117 ? 43.863  16.948  48.201  1.00 45.92  ? 117  ILE C N   1 
ATOM   7945  C  CA  . ILE B  1 117 ? 44.284  18.294  48.585  1.00 50.40  ? 117  ILE C CA  1 
ATOM   7946  C  C   . ILE B  1 117 ? 45.467  18.718  47.743  1.00 52.46  ? 117  ILE C C   1 
ATOM   7947  O  O   . ILE B  1 117 ? 46.517  18.060  47.786  1.00 48.33  ? 117  ILE C O   1 
ATOM   7948  C  CB  . ILE B  1 117 ? 44.708  18.394  50.057  1.00 51.01  ? 117  ILE C CB  1 
ATOM   7949  C  CG1 . ILE B  1 117 ? 43.707  17.688  50.982  1.00 54.82  ? 117  ILE C CG1 1 
ATOM   7950  C  CG2 . ILE B  1 117 ? 44.927  19.859  50.422  1.00 48.74  ? 117  ILE C CG2 1 
ATOM   7951  C  CD1 . ILE B  1 117 ? 42.479  18.494  51.297  1.00 52.59  ? 117  ILE C CD1 1 
ATOM   7952  N  N   . THR B  1 118 ? 45.325  19.821  47.009  1.00 48.48  ? 118  THR C N   1 
ATOM   7953  C  CA  . THR B  1 118 ? 46.342  20.169  46.008  1.00 58.95  ? 118  THR C CA  1 
ATOM   7954  C  C   . THR B  1 118 ? 47.131  21.437  46.353  1.00 58.27  ? 118  THR C C   1 
ATOM   7955  O  O   . THR B  1 118 ? 48.302  21.569  45.996  1.00 64.34  ? 118  THR C O   1 
ATOM   7956  C  CB  . THR B  1 118 ? 45.708  20.314  44.600  1.00 54.55  ? 118  THR C CB  1 
ATOM   7957  O  OG1 . THR B  1 118 ? 44.654  21.284  44.637  1.00 53.55  ? 118  THR C OG1 1 
ATOM   7958  C  CG2 . THR B  1 118 ? 45.121  18.988  44.151  1.00 49.74  ? 118  THR C CG2 1 
ATOM   7959  N  N   . ASN B  1 119 ? 46.499  22.353  47.066  1.00 53.50  ? 119  ASN C N   1 
ATOM   7960  C  CA  . ASN B  1 119 ? 47.158  23.582  47.478  1.00 61.98  ? 119  ASN C CA  1 
ATOM   7961  C  C   . ASN B  1 119 ? 46.724  23.863  48.903  1.00 67.35  ? 119  ASN C C   1 
ATOM   7962  O  O   . ASN B  1 119 ? 45.549  23.699  49.217  1.00 60.33  ? 119  ASN C O   1 
ATOM   7963  C  CB  . ASN B  1 119 ? 46.785  24.749  46.551  1.00 65.27  ? 119  ASN C CB  1 
ATOM   7964  C  CG  . ASN B  1 119 ? 47.995  25.527  46.045  1.00 69.11  ? 119  ASN C CG  1 
ATOM   7965  O  OD1 . ASN B  1 119 ? 48.982  24.947  45.587  1.00 70.72  ? 119  ASN C OD1 1 
ATOM   7966  N  ND2 . ASN B  1 119 ? 47.913  26.855  46.117  1.00 69.58  ? 119  ASN C ND2 1 
ATOM   7967  N  N   . ALA B  1 120 ? 47.663  24.269  49.758  1.00 67.77  ? 120  ALA C N   1 
ATOM   7968  C  CA  . ALA B  1 120 ? 47.366  24.549  51.162  1.00 58.58  ? 120  ALA C CA  1 
ATOM   7969  C  C   . ALA B  1 120 ? 48.306  25.616  51.721  1.00 60.74  ? 120  ALA C C   1 
ATOM   7970  O  O   . ALA B  1 120 ? 49.529  25.447  51.758  1.00 56.38  ? 120  ALA C O   1 
ATOM   7971  C  CB  . ALA B  1 120 ? 47.462  23.279  51.986  1.00 61.44  ? 120  ALA C CB  1 
ATOM   7972  N  N   . THR B  1 121 ? 47.723  26.719  52.167  1.00 64.08  ? 121  THR C N   1 
ATOM   7973  C  CA  . THR B  1 121 ? 48.515  27.861  52.602  1.00 65.38  ? 121  THR C CA  1 
ATOM   7974  C  C   . THR B  1 121 ? 48.032  28.443  53.918  1.00 64.49  ? 121  THR C C   1 
ATOM   7975  O  O   . THR B  1 121 ? 46.850  28.377  54.241  1.00 62.00  ? 121  THR C O   1 
ATOM   7976  C  CB  . THR B  1 121 ? 48.484  28.991  51.563  1.00 65.51  ? 121  THR C CB  1 
ATOM   7977  O  OG1 . THR B  1 121 ? 47.143  29.488  51.465  1.00 55.72  ? 121  THR C OG1 1 
ATOM   7978  C  CG2 . THR B  1 121 ? 48.968  28.502  50.191  1.00 51.61  ? 121  THR C CG2 1 
ATOM   7979  N  N   . LEU B  1 122 ? 48.953  29.035  54.667  1.00 73.28  ? 122  LEU C N   1 
ATOM   7980  C  CA  . LEU B  1 122 ? 48.582  29.803  55.846  1.00 72.47  ? 122  LEU C CA  1 
ATOM   7981  C  C   . LEU B  1 122 ? 48.872  31.265  55.585  1.00 74.84  ? 122  LEU C C   1 
ATOM   7982  O  O   . LEU B  1 122 ? 49.936  31.618  55.097  1.00 72.47  ? 122  LEU C O   1 
ATOM   7983  C  CB  . LEU B  1 122 ? 49.332  29.321  57.080  1.00 73.58  ? 122  LEU C CB  1 
ATOM   7984  C  CG  . LEU B  1 122 ? 48.639  29.624  58.408  1.00 74.56  ? 122  LEU C CG  1 
ATOM   7985  C  CD1 . LEU B  1 122 ? 47.292  28.917  58.510  1.00 63.79  ? 122  LEU C CD1 1 
ATOM   7986  C  CD2 . LEU B  1 122 ? 49.542  29.213  59.553  1.00 83.08  ? 122  LEU C CD2 1 
ATOM   7987  N  N   . GLN B  1 123 ? 47.906  32.107  55.903  1.00 75.10  ? 123  GLN C N   1 
ATOM   7988  C  CA  . GLN B  1 123 ? 48.011  33.521  55.633  1.00 76.13  ? 123  GLN C CA  1 
ATOM   7989  C  C   . GLN B  1 123 ? 47.603  34.232  56.908  1.00 82.20  ? 123  GLN C C   1 
ATOM   7990  O  O   . GLN B  1 123 ? 46.497  34.028  57.401  1.00 80.91  ? 123  GLN C O   1 
ATOM   7991  C  CB  . GLN B  1 123 ? 47.119  33.917  54.451  1.00 72.59  ? 123  GLN C CB  1 
ATOM   7992  C  CG  . GLN B  1 123 ? 47.378  35.306  53.889  1.00 84.84  ? 123  GLN C CG  1 
ATOM   7993  C  CD  . GLN B  1 123 ? 46.527  35.630  52.659  1.00 87.12  ? 123  GLN C CD  1 
ATOM   7994  O  OE1 . GLN B  1 123 ? 46.967  35.453  51.522  1.00 92.70  ? 123  GLN C OE1 1 
ATOM   7995  N  NE2 . GLN B  1 123 ? 45.311  36.122  52.886  1.00 73.34  ? 123  GLN C NE2 1 
ATOM   7996  N  N   . SER B  1 124 ? 48.494  35.046  57.466  1.00 86.19  ? 124  SER C N   1 
ATOM   7997  C  CA  . SER B  1 124 ? 48.149  35.766  58.683  1.00 86.41  ? 124  SER C CA  1 
ATOM   7998  C  C   . SER B  1 124 ? 48.016  37.267  58.470  1.00 86.35  ? 124  SER C C   1 
ATOM   7999  O  O   . SER B  1 124 ? 48.711  37.869  57.647  1.00 82.86  ? 124  SER C O   1 
ATOM   8000  C  CB  . SER B  1 124 ? 49.175  35.500  59.782  1.00 86.68  ? 124  SER C CB  1 
ATOM   8001  O  OG  . SER B  1 124 ? 48.631  35.837  61.045  1.00 82.56  ? 124  SER C OG  1 
ATOM   8002  N  N   . GLU B  1 125 ? 47.109  37.848  59.246  1.00 83.81  ? 125  GLU C N   1 
ATOM   8003  C  CA  . GLU B  1 125 ? 46.811  39.267  59.207  1.00 83.48  ? 125  GLU C CA  1 
ATOM   8004  C  C   . GLU B  1 125 ? 47.217  39.901  60.550  1.00 87.40  ? 125  GLU C C   1 
ATOM   8005  O  O   . GLU B  1 125 ? 46.962  41.077  60.808  1.00 82.21  ? 125  GLU C O   1 
ATOM   8006  C  CB  . GLU B  1 125 ? 45.324  39.465  58.912  1.00 82.48  ? 125  GLU C CB  1 
ATOM   8007  C  CG  . GLU B  1 125 ? 44.908  40.863  58.510  1.00 90.57  ? 125  GLU C CG  1 
ATOM   8008  C  CD  . GLU B  1 125 ? 43.396  41.036  58.516  1.00 101.00 ? 125  GLU C CD  1 
ATOM   8009  O  OE1 . GLU B  1 125 ? 42.741  40.587  57.547  1.00 103.14 ? 125  GLU C OE1 1 
ATOM   8010  O  OE2 . GLU B  1 125 ? 42.863  41.617  59.490  1.00 95.42  ? 125  GLU C OE2 1 
ATOM   8011  N  N   . GLU B  1 126 ? 47.851  39.099  61.407  1.00 90.32  ? 126  GLU C N   1 
ATOM   8012  C  CA  . GLU B  1 126 ? 48.344  39.565  62.702  1.00 79.29  ? 126  GLU C CA  1 
ATOM   8013  C  C   . GLU B  1 126 ? 49.799  39.138  62.906  1.00 79.71  ? 126  GLU C C   1 
ATOM   8014  O  O   . GLU B  1 126 ? 50.676  39.980  63.066  1.00 84.61  ? 126  GLU C O   1 
ATOM   8015  C  CB  . GLU B  1 126 ? 47.458  39.048  63.841  1.00 76.87  ? 126  GLU C CB  1 
ATOM   8016  C  CG  . GLU B  1 126 ? 46.040  39.610  63.820  1.00 76.00  ? 126  GLU C CG  1 
ATOM   8017  C  CD  . GLU B  1 126 ? 45.147  39.031  64.913  1.00 84.68  ? 126  GLU C CD  1 
ATOM   8018  O  OE1 . GLU B  1 126 ? 45.641  38.239  65.743  1.00 85.83  ? 126  GLU C OE1 1 
ATOM   8019  O  OE2 . GLU B  1 126 ? 43.941  39.370  64.941  1.00 81.90  ? 126  GLU C OE2 1 
ATOM   8020  N  N   . ASP B  1 127 ? 50.066  37.838  62.904  1.00 81.79  ? 127  ASP C N   1 
ATOM   8021  C  CA  . ASP B  1 127 ? 51.450  37.376  62.928  1.00 82.45  ? 127  ASP C CA  1 
ATOM   8022  C  C   . ASP B  1 127 ? 52.027  37.596  61.550  1.00 85.21  ? 127  ASP C C   1 
ATOM   8023  O  O   . ASP B  1 127 ? 51.967  36.716  60.696  1.00 87.56  ? 127  ASP C O   1 
ATOM   8024  C  CB  . ASP B  1 127 ? 51.559  35.902  63.329  1.00 85.14  ? 127  ASP C CB  1 
ATOM   8025  C  CG  . ASP B  1 127 ? 52.999  35.379  63.290  1.00 91.69  ? 127  ASP C CG  1 
ATOM   8026  O  OD1 . ASP B  1 127 ? 53.938  36.198  63.177  1.00 95.22  ? 127  ASP C OD1 1 
ATOM   8027  O  OD2 . ASP B  1 127 ? 53.195  34.143  63.381  1.00 89.01  ? 127  ASP C OD2 1 
ATOM   8028  N  N   . SER B  1 128 ? 52.607  38.773  61.347  1.00 90.67  ? 128  SER C N   1 
ATOM   8029  C  CA  . SER B  1 128 ? 53.079  39.200  60.030  1.00 91.96  ? 128  SER C CA  1 
ATOM   8030  C  C   . SER B  1 128 ? 54.225  38.348  59.498  1.00 92.93  ? 128  SER C C   1 
ATOM   8031  O  O   . SER B  1 128 ? 54.841  38.689  58.487  1.00 95.44  ? 128  SER C O   1 
ATOM   8032  C  CB  . SER B  1 128 ? 53.514  40.663  60.076  1.00 92.96  ? 128  SER C CB  1 
ATOM   8033  O  OG  . SER B  1 128 ? 52.520  41.469  60.683  1.00 93.43  ? 128  SER C OG  1 
ATOM   8034  N  N   . ARG B  1 129 ? 54.513  37.249  60.187  1.00 89.08  ? 129  ARG C N   1 
ATOM   8035  C  CA  . ARG B  1 129 ? 55.442  36.250  59.684  1.00 92.23  ? 129  ARG C CA  1 
ATOM   8036  C  C   . ARG B  1 129 ? 54.745  35.385  58.618  1.00 96.85  ? 129  ARG C C   1 
ATOM   8037  O  O   . ARG B  1 129 ? 55.401  34.765  57.765  1.00 92.86  ? 129  ARG C O   1 
ATOM   8038  C  CB  . ARG B  1 129 ? 55.967  35.396  60.838  1.00 90.17  ? 129  ARG C CB  1 
ATOM   8039  C  CG  . ARG B  1 129 ? 56.879  34.272  60.418  1.00 93.73  ? 129  ARG C CG  1 
ATOM   8040  C  CD  . ARG B  1 129 ? 56.747  33.125  61.380  1.00 93.85  ? 129  ARG C CD  1 
ATOM   8041  N  NE  . ARG B  1 129 ? 57.303  33.465  62.679  1.00 89.82  ? 129  ARG C NE  1 
ATOM   8042  C  CZ  . ARG B  1 129 ? 56.830  33.010  63.833  1.00 96.75  ? 129  ARG C CZ  1 
ATOM   8043  N  NH1 . ARG B  1 129 ? 55.778  32.206  63.858  1.00 93.50  ? 129  ARG C NH1 1 
ATOM   8044  N  NH2 . ARG B  1 129 ? 57.406  33.369  64.970  1.00 111.48 ? 129  ARG C NH2 1 
ATOM   8045  N  N   . TYR B  1 130 ? 53.412  35.352  58.676  1.00 93.48  ? 130  TYR C N   1 
ATOM   8046  C  CA  . TYR B  1 130 ? 52.599  34.677  57.660  1.00 95.90  ? 130  TYR C CA  1 
ATOM   8047  C  C   . TYR B  1 130 ? 51.764  35.705  56.892  1.00 95.79  ? 130  TYR C C   1 
ATOM   8048  O  O   . TYR B  1 130 ? 50.805  35.345  56.200  1.00 90.87  ? 130  TYR C O   1 
ATOM   8049  C  CB  . TYR B  1 130 ? 51.691  33.597  58.284  1.00 89.57  ? 130  TYR C CB  1 
ATOM   8050  C  CG  . TYR B  1 130 ? 52.449  32.415  58.847  1.00 84.03  ? 130  TYR C CG  1 
ATOM   8051  C  CD1 . TYR B  1 130 ? 52.982  31.448  58.011  1.00 84.75  ? 130  TYR C CD1 1 
ATOM   8052  C  CD2 . TYR B  1 130 ? 52.647  32.278  60.212  1.00 86.95  ? 130  TYR C CD2 1 
ATOM   8053  C  CE1 . TYR B  1 130 ? 53.688  30.378  58.518  1.00 84.02  ? 130  TYR C CE1 1 
ATOM   8054  C  CE2 . TYR B  1 130 ? 53.350  31.214  60.726  1.00 85.28  ? 130  TYR C CE2 1 
ATOM   8055  C  CZ  . TYR B  1 130 ? 53.865  30.266  59.876  1.00 84.81  ? 130  TYR C CZ  1 
ATOM   8056  O  OH  . TYR B  1 130 ? 54.566  29.200  60.384  1.00 87.02  ? 130  TYR C OH  1 
ATOM   8057  N  N   . MET B  1 131 ? 52.132  36.980  57.043  1.00 94.72  ? 131  MET C N   1 
ATOM   8058  C  CA  . MET B  1 131 ? 51.621  38.072  56.212  1.00 94.65  ? 131  MET C CA  1 
ATOM   8059  C  C   . MET B  1 131 ? 51.636  37.638  54.742  1.00 91.16  ? 131  MET C C   1 
ATOM   8060  O  O   . MET B  1 131 ? 52.588  36.991  54.292  1.00 86.39  ? 131  MET C O   1 
ATOM   8061  C  CB  . MET B  1 131 ? 52.464  39.341  56.434  1.00 91.94  ? 131  MET C CB  1 
ATOM   8062  C  CG  . MET B  1 131 ? 52.285  40.456  55.402  1.00 100.72 ? 131  MET C CG  1 
ATOM   8063  S  SD  . MET B  1 131 ? 53.630  41.684  55.420  1.00 105.26 ? 131  MET C SD  1 
ATOM   8064  C  CE  . MET B  1 131 ? 53.402  42.432  57.032  1.00 79.20  ? 131  MET C CE  1 
ATOM   8065  N  N   . LYS B  1 132 ? 50.579  37.981  54.009  1.00 86.06  ? 132  LYS C N   1 
ATOM   8066  C  CA  . LYS B  1 132 ? 50.324  37.408  52.684  1.00 91.64  ? 132  LYS C CA  1 
ATOM   8067  C  C   . LYS B  1 132 ? 51.456  37.638  51.680  1.00 92.20  ? 132  LYS C C   1 
ATOM   8068  O  O   . LYS B  1 132 ? 52.188  38.621  51.779  1.00 92.30  ? 132  LYS C O   1 
ATOM   8069  C  CB  . LYS B  1 132 ? 49.013  37.963  52.127  1.00 91.07  ? 132  LYS C CB  1 
ATOM   8070  C  CG  . LYS B  1 132 ? 49.030  39.430  51.804  1.00 88.39  ? 132  LYS C CG  1 
ATOM   8071  C  CD  . LYS B  1 132 ? 47.826  39.780  50.953  1.00 90.86  ? 132  LYS C CD  1 
ATOM   8072  C  CE  . LYS B  1 132 ? 47.736  38.872  49.728  1.00 99.03  ? 132  LYS C CE  1 
ATOM   8073  N  NZ  . LYS B  1 132 ? 48.963  38.912  48.873  1.00 94.67  ? 132  LYS C NZ  1 
ATOM   8074  N  N   . PRO B  1 133 ? 51.591  36.740  50.687  1.00 93.66  ? 133  PRO C N   1 
ATOM   8075  C  CA  . PRO B  1 133 ? 50.703  35.623  50.334  1.00 90.76  ? 133  PRO C CA  1 
ATOM   8076  C  C   . PRO B  1 133 ? 50.936  34.316  51.097  1.00 90.81  ? 133  PRO C C   1 
ATOM   8077  O  O   . PRO B  1 133 ? 49.957  33.706  51.527  1.00 85.90  ? 133  PRO C O   1 
ATOM   8078  C  CB  . PRO B  1 133 ? 51.006  35.417  48.852  1.00 91.46  ? 133  PRO C CB  1 
ATOM   8079  C  CG  . PRO B  1 133 ? 52.455  35.758  48.732  1.00 85.25  ? 133  PRO C CG  1 
ATOM   8080  C  CD  . PRO B  1 133 ? 52.720  36.852  49.745  1.00 90.18  ? 133  PRO C CD  1 
ATOM   8081  N  N   . GLY B  1 134 ? 52.199  33.905  51.241  1.00 94.16  ? 134  GLY C N   1 
ATOM   8082  C  CA  . GLY B  1 134 ? 52.578  32.602  51.771  1.00 81.75  ? 134  GLY C CA  1 
ATOM   8083  C  C   . GLY B  1 134 ? 52.087  32.377  53.179  1.00 81.67  ? 134  GLY C C   1 
ATOM   8084  O  O   . GLY B  1 134 ? 51.501  33.283  53.765  1.00 88.44  ? 134  GLY C O   1 
ATOM   8085  N  N   . LYS B  1 135 ? 52.365  31.204  53.750  1.00 81.05  ? 135  LYS C N   1 
ATOM   8086  C  CA  . LYS B  1 135 ? 53.321  30.256  53.180  1.00 82.79  ? 135  LYS C CA  1 
ATOM   8087  C  C   . LYS B  1 135 ? 52.747  28.855  52.929  1.00 73.57  ? 135  LYS C C   1 
ATOM   8088  O  O   . LYS B  1 135 ? 51.769  28.442  53.556  1.00 70.38  ? 135  LYS C O   1 
ATOM   8089  C  CB  . LYS B  1 135 ? 54.539  30.143  54.105  1.00 81.66  ? 135  LYS C CB  1 
ATOM   8090  C  CG  . LYS B  1 135 ? 55.165  31.476  54.467  1.00 82.83  ? 135  LYS C CG  1 
ATOM   8091  C  CD  . LYS B  1 135 ? 56.361  31.302  55.387  1.00 93.10  ? 135  LYS C CD  1 
ATOM   8092  C  CE  . LYS B  1 135 ? 56.900  32.657  55.837  1.00 97.80  ? 135  LYS C CE  1 
ATOM   8093  N  NZ  . LYS B  1 135 ? 58.039  32.543  56.788  1.00 98.10  ? 135  LYS C NZ  1 
ATOM   8094  N  N   . GLU B  1 136 ? 53.384  28.126  52.018  1.00 64.41  ? 136  GLU C N   1 
ATOM   8095  C  CA  . GLU B  1 136 ? 52.985  26.762  51.688  1.00 67.02  ? 136  GLU C CA  1 
ATOM   8096  C  C   . GLU B  1 136 ? 53.071  25.795  52.875  1.00 74.24  ? 136  GLU C C   1 
ATOM   8097  O  O   . GLU B  1 136 ? 54.080  25.751  53.588  1.00 70.30  ? 136  GLU C O   1 
ATOM   8098  C  CB  . GLU B  1 136 ? 53.844  26.229  50.540  1.00 68.69  ? 136  GLU C CB  1 
ATOM   8099  C  CG  . GLU B  1 136 ? 53.170  26.298  49.179  1.00 79.83  ? 136  GLU C CG  1 
ATOM   8100  C  CD  . GLU B  1 136 ? 53.859  25.438  48.130  1.00 89.28  ? 136  GLU C CD  1 
ATOM   8101  O  OE1 . GLU B  1 136 ? 54.581  24.487  48.511  1.00 89.90  ? 136  GLU C OE1 1 
ATOM   8102  O  OE2 . GLU B  1 136 ? 53.676  25.718  46.924  1.00 89.14  ? 136  GLU C OE2 1 
ATOM   8103  N  N   . LEU B  1 137 ? 52.019  25.000  53.060  1.00 69.80  ? 137  LEU C N   1 
ATOM   8104  C  CA  . LEU B  1 137 ? 51.927  24.102  54.205  1.00 64.47  ? 137  LEU C CA  1 
ATOM   8105  C  C   . LEU B  1 137 ? 52.074  22.639  53.832  1.00 63.54  ? 137  LEU C C   1 
ATOM   8106  O  O   . LEU B  1 137 ? 51.304  22.123  53.034  1.00 73.44  ? 137  LEU C O   1 
ATOM   8107  C  CB  . LEU B  1 137 ? 50.596  24.300  54.922  1.00 63.41  ? 137  LEU C CB  1 
ATOM   8108  C  CG  . LEU B  1 137 ? 50.334  25.737  55.347  1.00 66.09  ? 137  LEU C CG  1 
ATOM   8109  C  CD1 . LEU B  1 137 ? 49.047  25.837  56.138  1.00 64.05  ? 137  LEU C CD1 1 
ATOM   8110  C  CD2 . LEU B  1 137 ? 51.512  26.245  56.158  1.00 73.63  ? 137  LEU C CD2 1 
ATOM   8111  N  N   . LYS B  1 138 ? 53.059  21.979  54.432  1.00 64.94  ? 138  LYS C N   1 
ATOM   8112  C  CA  . LYS B  1 138 ? 53.228  20.533  54.329  1.00 70.73  ? 138  LYS C CA  1 
ATOM   8113  C  C   . LYS B  1 138 ? 51.994  19.809  54.856  1.00 67.97  ? 138  LYS C C   1 
ATOM   8114  O  O   . LYS B  1 138 ? 51.476  20.153  55.922  1.00 69.70  ? 138  LYS C O   1 
ATOM   8115  C  CB  . LYS B  1 138 ? 54.466  20.096  55.105  1.00 74.15  ? 138  LYS C CB  1 
ATOM   8116  C  CG  . LYS B  1 138 ? 54.963  18.699  54.805  1.00 79.52  ? 138  LYS C CG  1 
ATOM   8117  C  CD  . LYS B  1 138 ? 56.232  18.438  55.609  1.00 89.18  ? 138  LYS C CD  1 
ATOM   8118  C  CE  . LYS B  1 138 ? 57.164  19.656  55.552  1.00 90.39  ? 138  LYS C CE  1 
ATOM   8119  N  NZ  . LYS B  1 138 ? 57.814  19.959  56.856  1.00 86.36  ? 138  LYS C NZ  1 
ATOM   8120  N  N   . VAL B  1 139 ? 51.512  18.816  54.115  1.00 63.54  ? 139  VAL C N   1 
ATOM   8121  C  CA  . VAL B  1 139 ? 50.278  18.150  54.508  1.00 65.43  ? 139  VAL C CA  1 
ATOM   8122  C  C   . VAL B  1 139 ? 50.422  16.647  54.652  1.00 62.66  ? 139  VAL C C   1 
ATOM   8123  O  O   . VAL B  1 139 ? 50.693  15.940  53.684  1.00 57.20  ? 139  VAL C O   1 
ATOM   8124  C  CB  . VAL B  1 139 ? 49.144  18.420  53.521  1.00 60.74  ? 139  VAL C CB  1 
ATOM   8125  C  CG1 . VAL B  1 139 ? 47.915  17.594  53.909  1.00 57.93  ? 139  VAL C CG1 1 
ATOM   8126  C  CG2 . VAL B  1 139 ? 48.816  19.897  53.498  1.00 63.52  ? 139  VAL C CG2 1 
ATOM   8127  N  N   . LEU B  1 140 ? 50.208  16.164  55.870  1.00 62.13  ? 140  LEU C N   1 
ATOM   8128  C  CA  . LEU B  1 140 ? 50.225  14.734  56.133  1.00 59.75  ? 140  LEU C CA  1 
ATOM   8129  C  C   . LEU B  1 140 ? 48.814  14.178  56.198  1.00 56.95  ? 140  LEU C C   1 
ATOM   8130  O  O   . LEU B  1 140 ? 47.896  14.841  56.686  1.00 59.84  ? 140  LEU C O   1 
ATOM   8131  C  CB  . LEU B  1 140 ? 50.960  14.443  57.434  1.00 61.22  ? 140  LEU C CB  1 
ATOM   8132  C  CG  . LEU B  1 140 ? 52.466  14.625  57.351  1.00 69.33  ? 140  LEU C CG  1 
ATOM   8133  C  CD1 . LEU B  1 140 ? 53.124  14.359  58.706  1.00 68.47  ? 140  LEU C CD1 1 
ATOM   8134  C  CD2 . LEU B  1 140 ? 53.000  13.689  56.280  1.00 67.01  ? 140  LEU C CD2 1 
ATOM   8135  N  N   . SER B  1 141 ? 48.647  12.962  55.693  1.00 58.43  ? 141  SER C N   1 
ATOM   8136  C  CA  . SER B  1 141 ? 47.385  12.242  55.809  1.00 57.31  ? 141  SER C CA  1 
ATOM   8137  C  C   . SER B  1 141 ? 47.495  11.141  56.820  1.00 56.39  ? 141  SER C C   1 
ATOM   8138  O  O   . SER B  1 141 ? 48.353  10.267  56.694  1.00 55.69  ? 141  SER C O   1 
ATOM   8139  C  CB  . SER B  1 141 ? 46.955  11.628  54.480  1.00 52.17  ? 141  SER C CB  1 
ATOM   8140  O  OG  . SER B  1 141 ? 46.389  12.612  53.644  1.00 71.48  ? 141  SER C OG  1 
ATOM   8141  N  N   . TYR B  1 142 ? 46.625  11.174  57.821  1.00 57.73  ? 142  TYR C N   1 
ATOM   8142  C  CA  . TYR B  1 142 ? 46.419  9.980   58.621  1.00 59.58  ? 142  TYR C CA  1 
ATOM   8143  C  C   . TYR B  1 142 ? 44.977  9.493   58.451  1.00 55.36  ? 142  TYR C C   1 
ATOM   8144  O  O   . TYR B  1 142 ? 44.077  9.904   59.185  1.00 55.67  ? 142  TYR C O   1 
ATOM   8145  C  CB  . TYR B  1 142 ? 46.745  10.225  60.093  1.00 63.72  ? 142  TYR C CB  1 
ATOM   8146  C  CG  . TYR B  1 142 ? 46.768  8.935   60.870  1.00 62.05  ? 142  TYR C CG  1 
ATOM   8147  C  CD1 . TYR B  1 142 ? 47.374  7.807   60.334  1.00 60.04  ? 142  TYR C CD1 1 
ATOM   8148  C  CD2 . TYR B  1 142 ? 46.169  8.835   62.123  1.00 64.27  ? 142  TYR C CD2 1 
ATOM   8149  C  CE1 . TYR B  1 142 ? 47.397  6.612   61.019  1.00 67.35  ? 142  TYR C CE1 1 
ATOM   8150  C  CE2 . TYR B  1 142 ? 46.188  7.636   62.826  1.00 65.38  ? 142  TYR C CE2 1 
ATOM   8151  C  CZ  . TYR B  1 142 ? 46.805  6.531   62.263  1.00 71.21  ? 142  TYR C CZ  1 
ATOM   8152  O  OH  . TYR B  1 142 ? 46.836  5.337   62.933  1.00 78.98  ? 142  TYR C OH  1 
ATOM   8153  N  N   . PRO B  1 143 ? 44.757  8.617   57.466  1.00 47.62  ? 143  PRO C N   1 
ATOM   8154  C  CA  . PRO B  1 143 ? 43.404  8.196   57.090  1.00 51.75  ? 143  PRO C CA  1 
ATOM   8155  C  C   . PRO B  1 143 ? 42.743  7.242   58.095  1.00 56.45  ? 143  PRO C C   1 
ATOM   8156  O  O   . PRO B  1 143 ? 41.546  6.985   57.990  1.00 60.24  ? 143  PRO C O   1 
ATOM   8157  C  CB  . PRO B  1 143 ? 43.613  7.512   55.735  1.00 45.80  ? 143  PRO C CB  1 
ATOM   8158  C  CG  . PRO B  1 143 ? 45.035  7.139   55.695  1.00 46.57  ? 143  PRO C CG  1 
ATOM   8159  C  CD  . PRO B  1 143 ? 45.793  8.062   56.586  1.00 45.64  ? 143  PRO C CD  1 
ATOM   8160  N  N   . ALA B  1 144 ? 43.499  6.730   59.058  1.00 57.26  ? 144  ALA C N   1 
ATOM   8161  C  CA  . ALA B  1 144 ? 42.908  5.881   60.092  1.00 62.42  ? 144  ALA C CA  1 
ATOM   8162  C  C   . ALA B  1 144 ? 42.099  6.700   61.097  1.00 58.30  ? 144  ALA C C   1 
ATOM   8163  O  O   . ALA B  1 144 ? 41.200  6.180   61.763  1.00 60.02  ? 144  ALA C O   1 
ATOM   8164  C  CB  . ALA B  1 144 ? 43.988  5.081   60.812  1.00 62.41  ? 144  ALA C CB  1 
ATOM   8165  N  N   . HIS B  1 145 ? 42.426  7.978   61.219  1.00 53.12  ? 145  HIS C N   1 
ATOM   8166  C  CA  . HIS B  1 145 ? 41.661  8.851   62.090  1.00 57.66  ? 145  HIS C CA  1 
ATOM   8167  C  C   . HIS B  1 145 ? 40.853  9.809   61.240  1.00 54.37  ? 145  HIS C C   1 
ATOM   8168  O  O   . HIS B  1 145 ? 40.149  10.686  61.765  1.00 51.24  ? 145  HIS C O   1 
ATOM   8169  C  CB  . HIS B  1 145 ? 42.577  9.618   63.049  1.00 60.33  ? 145  HIS C CB  1 
ATOM   8170  C  CG  . HIS B  1 145 ? 42.983  8.833   64.256  1.00 60.98  ? 145  HIS C CG  1 
ATOM   8171  N  ND1 . HIS B  1 145 ? 42.549  7.544   64.487  1.00 65.17  ? 145  HIS C ND1 1 
ATOM   8172  C  CD2 . HIS B  1 145 ? 43.785  9.154   65.299  1.00 61.83  ? 145  HIS C CD2 1 
ATOM   8173  C  CE1 . HIS B  1 145 ? 43.066  7.104   65.621  1.00 62.45  ? 145  HIS C CE1 1 
ATOM   8174  N  NE2 . HIS B  1 145 ? 43.819  8.062   66.133  1.00 63.80  ? 145  HIS C NE2 1 
ATOM   8175  N  N   . GLU B  1 146 ? 40.954  9.611   59.923  1.00 54.82  ? 146  GLU C N   1 
ATOM   8176  C  CA  . GLU B  1 146 ? 40.362  10.511  58.930  1.00 49.78  ? 146  GLU C CA  1 
ATOM   8177  C  C   . GLU B  1 146 ? 40.762  11.954  59.200  1.00 48.94  ? 146  GLU C C   1 
ATOM   8178  O  O   . GLU B  1 146 ? 39.909  12.841  59.220  1.00 50.04  ? 146  GLU C O   1 
ATOM   8179  C  CB  . GLU B  1 146 ? 38.836  10.379  58.907  1.00 46.36  ? 146  GLU C CB  1 
ATOM   8180  C  CG  . GLU B  1 146 ? 38.353  8.950   58.676  1.00 48.62  ? 146  GLU C CG  1 
ATOM   8181  C  CD  . GLU B  1 146 ? 36.839  8.812   58.732  1.00 48.24  ? 146  GLU C CD  1 
ATOM   8182  O  OE1 . GLU B  1 146 ? 36.138  9.793   59.099  1.00 45.38  ? 146  GLU C OE1 1 
ATOM   8183  O  OE2 . GLU B  1 146 ? 36.354  7.706   58.404  1.00 47.89  ? 146  GLU C OE2 1 
ATOM   8184  N  N   . GLN B  1 147 ? 42.063  12.169  59.407  1.00 52.91  ? 147  GLN C N   1 
ATOM   8185  C  CA  . GLN B  1 147 ? 42.623  13.483  59.731  1.00 49.37  ? 147  GLN C CA  1 
ATOM   8186  C  C   . GLN B  1 147 ? 43.801  13.873  58.848  1.00 51.29  ? 147  GLN C C   1 
ATOM   8187  O  O   . GLN B  1 147 ? 44.553  13.026  58.342  1.00 54.43  ? 147  GLN C O   1 
ATOM   8188  C  CB  . GLN B  1 147 ? 43.095  13.530  61.192  1.00 54.06  ? 147  GLN C CB  1 
ATOM   8189  C  CG  . GLN B  1 147 ? 42.008  13.481  62.258  1.00 52.70  ? 147  GLN C CG  1 
ATOM   8190  C  CD  . GLN B  1 147 ? 42.570  13.130  63.633  1.00 55.02  ? 147  GLN C CD  1 
ATOM   8191  O  OE1 . GLN B  1 147 ? 43.731  12.748  63.755  1.00 55.94  ? 147  GLN C OE1 1 
ATOM   8192  N  NE2 . GLN B  1 147 ? 41.746  13.259  64.671  1.00 56.86  ? 147  GLN C NE2 1 
ATOM   8193  N  N   . ILE B  1 148 ? 43.992  15.171  58.698  1.00 51.64  ? 148  ILE C N   1 
ATOM   8194  C  CA  . ILE B  1 148 ? 45.194  15.659  58.039  1.00 61.82  ? 148  ILE C CA  1 
ATOM   8195  C  C   . ILE B  1 148 ? 46.026  16.507  58.986  1.00 63.62  ? 148  ILE C C   1 
ATOM   8196  O  O   . ILE B  1 148 ? 45.501  17.149  59.908  1.00 59.50  ? 148  ILE C O   1 
ATOM   8197  C  CB  . ILE B  1 148 ? 44.877  16.495  56.788  1.00 59.60  ? 148  ILE C CB  1 
ATOM   8198  C  CG1 . ILE B  1 148 ? 43.868  17.598  57.145  1.00 53.47  ? 148  ILE C CG1 1 
ATOM   8199  C  CG2 . ILE B  1 148 ? 44.394  15.588  55.652  1.00 52.86  ? 148  ILE C CG2 1 
ATOM   8200  C  CD1 . ILE B  1 148 ? 43.457  18.466  55.992  1.00 46.71  ? 148  ILE C CD1 1 
ATOM   8201  N  N   . ALA B  1 149 ? 47.331  16.494  58.750  1.00 65.03  ? 149  ALA C N   1 
ATOM   8202  C  CA  . ALA B  1 149 ? 48.248  17.357  59.478  1.00 67.08  ? 149  ALA C CA  1 
ATOM   8203  C  C   . ALA B  1 149 ? 48.757  18.450  58.551  1.00 65.80  ? 149  ALA C C   1 
ATOM   8204  O  O   . ALA B  1 149 ? 49.304  18.173  57.469  1.00 57.74  ? 149  ALA C O   1 
ATOM   8205  C  CB  . ALA B  1 149 ? 49.407  16.554  60.054  1.00 64.78  ? 149  ALA C CB  1 
ATOM   8206  N  N   . LEU B  1 150 ? 48.533  19.687  58.975  1.00 64.29  ? 150  LEU C N   1 
ATOM   8207  C  CA  . LEU B  1 150 ? 49.071  20.865  58.310  1.00 63.03  ? 150  LEU C CA  1 
ATOM   8208  C  C   . LEU B  1 150 ? 50.270  21.360  59.102  1.00 64.05  ? 150  LEU C C   1 
ATOM   8209  O  O   . LEU B  1 150 ? 50.108  22.034  60.114  1.00 61.79  ? 150  LEU C O   1 
ATOM   8210  C  CB  . LEU B  1 150 ? 48.016  21.964  58.212  1.00 61.97  ? 150  LEU C CB  1 
ATOM   8211  C  CG  . LEU B  1 150 ? 46.653  21.567  57.651  1.00 60.06  ? 150  LEU C CG  1 
ATOM   8212  C  CD1 . LEU B  1 150 ? 45.682  22.729  57.743  1.00 54.10  ? 150  LEU C CD1 1 
ATOM   8213  C  CD2 . LEU B  1 150 ? 46.793  21.095  56.219  1.00 53.47  ? 150  LEU C CD2 1 
ATOM   8214  N  N   . LEU B  1 151 ? 51.467  21.004  58.659  1.00 64.96  ? 151  LEU C N   1 
ATOM   8215  C  CA  . LEU B  1 151 ? 52.678  21.380  59.379  1.00 71.69  ? 151  LEU C CA  1 
ATOM   8216  C  C   . LEU B  1 151 ? 53.104  22.802  59.029  1.00 77.09  ? 151  LEU C C   1 
ATOM   8217  O  O   . LEU B  1 151 ? 53.416  23.088  57.873  1.00 76.73  ? 151  LEU C O   1 
ATOM   8218  C  CB  . LEU B  1 151 ? 53.816  20.408  59.058  1.00 75.38  ? 151  LEU C CB  1 
ATOM   8219  C  CG  . LEU B  1 151 ? 53.523  18.907  58.958  1.00 71.83  ? 151  LEU C CG  1 
ATOM   8220  C  CD1 . LEU B  1 151 ? 54.825  18.130  58.809  1.00 75.68  ? 151  LEU C CD1 1 
ATOM   8221  C  CD2 . LEU B  1 151 ? 52.723  18.385  60.141  1.00 69.61  ? 151  LEU C CD2 1 
ATOM   8222  N  N   . VAL B  1 152 ? 53.120  23.694  60.015  1.00 77.13  ? 152  VAL C N   1 
ATOM   8223  C  CA  . VAL B  1 152 ? 53.516  25.076  59.765  1.00 80.18  ? 152  VAL C CA  1 
ATOM   8224  C  C   . VAL B  1 152 ? 55.031  25.236  59.894  1.00 86.25  ? 152  VAL C C   1 
ATOM   8225  O  O   . VAL B  1 152 ? 55.667  24.490  60.640  1.00 81.23  ? 152  VAL C O   1 
ATOM   8226  C  CB  . VAL B  1 152 ? 52.810  26.053  60.719  1.00 78.55  ? 152  VAL C CB  1 
ATOM   8227  C  CG1 . VAL B  1 152 ? 51.311  25.978  60.526  1.00 75.68  ? 152  VAL C CG1 1 
ATOM   8228  C  CG2 . VAL B  1 152 ? 53.192  25.766  62.159  1.00 81.12  ? 152  VAL C CG2 1 
ATOM   8229  N  N   . PRO B  1 153 ? 55.613  26.198  59.145  1.00 94.52  ? 153  PRO C N   1 
ATOM   8230  C  CA  . PRO B  1 153 ? 57.057  26.472  59.155  1.00 93.03  ? 153  PRO C CA  1 
ATOM   8231  C  C   . PRO B  1 153 ? 57.561  26.963  60.507  1.00 92.24  ? 153  PRO C C   1 
ATOM   8232  O  O   . PRO B  1 153 ? 58.671  26.618  60.913  1.00 91.06  ? 153  PRO C O   1 
ATOM   8233  C  CB  . PRO B  1 153 ? 57.219  27.574  58.100  1.00 92.17  ? 153  PRO C CB  1 
ATOM   8234  C  CG  . PRO B  1 153 ? 56.021  27.478  57.245  1.00 90.11  ? 153  PRO C CG  1 
ATOM   8235  C  CD  . PRO B  1 153 ? 54.915  27.025  58.141  1.00 90.89  ? 153  PRO C CD  1 
ATOM   8236  N  N   . GLU B  1 154 ? 56.756  27.774  61.183  1.00 90.14  ? 154  GLU C N   1 
ATOM   8237  C  CA  . GLU B  1 154 ? 57.125  28.299  62.490  1.00 92.11  ? 154  GLU C CA  1 
ATOM   8238  C  C   . GLU B  1 154 ? 55.912  28.351  63.414  1.00 92.46  ? 154  GLU C C   1 
ATOM   8239  O  O   . GLU B  1 154 ? 54.814  28.719  62.987  1.00 94.94  ? 154  GLU C O   1 
ATOM   8240  C  CB  . GLU B  1 154 ? 57.756  29.688  62.356  1.00 99.69  ? 154  GLU C CB  1 
ATOM   8241  C  CG  . GLU B  1 154 ? 59.192  29.680  61.839  1.00 99.01  ? 154  GLU C CG  1 
ATOM   8242  C  CD  . GLU B  1 154 ? 59.287  30.006  60.361  1.00 104.61 ? 154  GLU C CD  1 
ATOM   8243  O  OE1 . GLU B  1 154 ? 58.632  30.981  59.927  1.00 103.63 ? 154  GLU C OE1 1 
ATOM   8244  O  OE2 . GLU B  1 154 ? 60.017  29.291  59.635  1.00 105.42 ? 154  GLU C OE2 1 
ATOM   8245  N  N   . LYS B  1 155 ? 56.128  27.985  64.676  1.00 88.53  ? 155  LYS C N   1 
ATOM   8246  C  CA  . LYS B  1 155 ? 55.054  27.825  65.652  1.00 87.74  ? 155  LYS C CA  1 
ATOM   8247  C  C   . LYS B  1 155 ? 54.094  28.993  65.651  1.00 85.36  ? 155  LYS C C   1 
ATOM   8248  O  O   . LYS B  1 155 ? 54.500  30.140  65.795  1.00 88.77  ? 155  LYS C O   1 
ATOM   8249  C  CB  . LYS B  1 155 ? 55.626  27.643  67.057  1.00 94.78  ? 155  LYS C CB  1 
ATOM   8250  C  CG  . LYS B  1 155 ? 56.599  26.481  67.186  1.00 93.64  ? 155  LYS C CG  1 
ATOM   8251  C  CD  . LYS B  1 155 ? 57.038  26.276  68.633  1.00 98.31  ? 155  LYS C CD  1 
ATOM   8252  C  CE  . LYS B  1 155 ? 55.842  26.117  69.564  1.00 89.92  ? 155  LYS C CE  1 
ATOM   8253  N  NZ  . LYS B  1 155 ? 56.273  25.958  70.980  1.00 95.44  ? 155  LYS C NZ  1 
ATOM   8254  N  N   . LEU B  1 156 ? 52.817  28.690  65.469  1.00 88.63  ? 156  LEU C N   1 
ATOM   8255  C  CA  . LEU B  1 156 ? 51.803  29.727  65.447  1.00 86.96  ? 156  LEU C CA  1 
ATOM   8256  C  C   . LEU B  1 156 ? 51.791  30.406  66.798  1.00 82.71  ? 156  LEU C C   1 
ATOM   8257  O  O   . LEU B  1 156 ? 52.181  29.817  67.802  1.00 82.49  ? 156  LEU C O   1 
ATOM   8258  C  CB  . LEU B  1 156 ? 50.431  29.151  65.098  1.00 86.29  ? 156  LEU C CB  1 
ATOM   8259  C  CG  . LEU B  1 156 ? 50.439  28.291  63.831  1.00 86.01  ? 156  LEU C CG  1 
ATOM   8260  C  CD1 . LEU B  1 156 ? 49.027  27.926  63.411  1.00 82.60  ? 156  LEU C CD1 1 
ATOM   8261  C  CD2 . LEU B  1 156 ? 51.186  28.996  62.704  1.00 84.27  ? 156  LEU C CD2 1 
ATOM   8262  N  N   . THR B  1 157 ? 51.357  31.656  66.810  1.00 86.32  ? 157  THR C N   1 
ATOM   8263  C  CA  . THR B  1 157 ? 51.453  32.476  67.998  1.00 86.09  ? 157  THR C CA  1 
ATOM   8264  C  C   . THR B  1 157 ? 50.091  32.673  68.650  1.00 84.38  ? 157  THR C C   1 
ATOM   8265  O  O   . THR B  1 157 ? 49.146  33.136  68.007  1.00 79.17  ? 157  THR C O   1 
ATOM   8266  C  CB  . THR B  1 157 ? 52.074  33.834  67.658  1.00 90.98  ? 157  THR C CB  1 
ATOM   8267  O  OG1 . THR B  1 157 ? 53.304  33.627  66.949  1.00 91.09  ? 157  THR C OG1 1 
ATOM   8268  C  CG2 . THR B  1 157 ? 52.325  34.645  68.921  1.00 81.91  ? 157  THR C CG2 1 
ATOM   8269  N  N   . PRO B  1 158 ? 49.995  32.311  69.938  1.00 85.22  ? 158  PRO C N   1 
ATOM   8270  C  CA  . PRO B  1 158 ? 48.768  32.363  70.738  1.00 84.19  ? 158  PRO C CA  1 
ATOM   8271  C  C   . PRO B  1 158 ? 47.984  33.654  70.593  1.00 77.94  ? 158  PRO C C   1 
ATOM   8272  O  O   . PRO B  1 158 ? 48.568  34.723  70.479  1.00 77.58  ? 158  PRO C O   1 
ATOM   8273  C  CB  . PRO B  1 158 ? 49.290  32.199  72.160  1.00 82.59  ? 158  PRO C CB  1 
ATOM   8274  C  CG  . PRO B  1 158 ? 50.449  31.266  71.981  1.00 84.05  ? 158  PRO C CG  1 
ATOM   8275  C  CD  . PRO B  1 158 ? 51.099  31.676  70.681  1.00 84.24  ? 158  PRO C CD  1 
ATOM   8276  N  N   . HIS B  1 159 ? 46.663  33.506  70.553  1.00 81.72  ? 159  HIS C N   1 
ATOM   8277  C  CA  . HIS B  1 159 ? 45.692  34.597  70.498  1.00 78.15  ? 159  HIS C CA  1 
ATOM   8278  C  C   . HIS B  1 159 ? 45.716  35.313  69.145  1.00 80.88  ? 159  HIS C C   1 
ATOM   8279  O  O   . HIS B  1 159 ? 44.974  36.278  68.923  1.00 76.55  ? 159  HIS C O   1 
ATOM   8280  C  CB  . HIS B  1 159 ? 45.926  35.578  71.650  1.00 72.33  ? 159  HIS C CB  1 
ATOM   8281  C  CG  . HIS B  1 159 ? 45.842  34.946  73.007  1.00 85.95  ? 159  HIS C CG  1 
ATOM   8282  N  ND1 . HIS B  1 159 ? 45.844  33.579  73.197  1.00 91.37  ? 159  HIS C ND1 1 
ATOM   8283  C  CD2 . HIS B  1 159 ? 45.748  35.494  74.241  1.00 87.98  ? 159  HIS C CD2 1 
ATOM   8284  C  CE1 . HIS B  1 159 ? 45.757  33.312  74.487  1.00 86.57  ? 159  HIS C CE1 1 
ATOM   8285  N  NE2 . HIS B  1 159 ? 45.699  34.458  75.144  1.00 91.29  ? 159  HIS C NE2 1 
ATOM   8286  N  N   . LEU B  1 160 ? 46.547  34.815  68.231  1.00 76.72  ? 160  LEU C N   1 
ATOM   8287  C  CA  . LEU B  1 160 ? 46.609  35.376  66.889  1.00 83.05  ? 160  LEU C CA  1 
ATOM   8288  C  C   . LEU B  1 160 ? 45.777  34.575  65.874  1.00 87.16  ? 160  LEU C C   1 
ATOM   8289  O  O   . LEU B  1 160 ? 45.716  33.336  65.917  1.00 76.50  ? 160  LEU C O   1 
ATOM   8290  C  CB  . LEU B  1 160 ? 48.062  35.476  66.416  1.00 84.58  ? 160  LEU C CB  1 
ATOM   8291  C  CG  . LEU B  1 160 ? 48.945  36.493  67.144  1.00 84.00  ? 160  LEU C CG  1 
ATOM   8292  C  CD1 . LEU B  1 160 ? 50.304  36.573  66.494  1.00 83.74  ? 160  LEU C CD1 1 
ATOM   8293  C  CD2 . LEU B  1 160 ? 48.304  37.872  67.170  1.00 74.12  ? 160  LEU C CD2 1 
ATOM   8294  N  N   . LYS B  1 161 ? 45.138  35.310  64.965  1.00 83.49  ? 161  LYS C N   1 
ATOM   8295  C  CA  . LYS B  1 161 ? 44.345  34.729  63.889  1.00 76.33  ? 161  LYS C CA  1 
ATOM   8296  C  C   . LYS B  1 161 ? 45.187  34.352  62.661  1.00 77.34  ? 161  LYS C C   1 
ATOM   8297  O  O   . LYS B  1 161 ? 46.004  35.137  62.177  1.00 79.97  ? 161  LYS C O   1 
ATOM   8298  C  CB  . LYS B  1 161 ? 43.243  35.699  63.468  1.00 70.16  ? 161  LYS C CB  1 
ATOM   8299  C  CG  . LYS B  1 161 ? 42.242  35.981  64.542  1.00 67.89  ? 161  LYS C CG  1 
ATOM   8300  C  CD  . LYS B  1 161 ? 41.120  36.829  63.997  1.00 63.68  ? 161  LYS C CD  1 
ATOM   8301  C  CE  . LYS B  1 161 ? 39.961  36.849  64.978  1.00 67.95  ? 161  LYS C CE  1 
ATOM   8302  N  NZ  . LYS B  1 161 ? 38.803  37.644  64.478  1.00 77.26  ? 161  LYS C NZ  1 
ATOM   8303  N  N   . TYR B  1 162 ? 44.970  33.141  62.162  1.00 66.22  ? 162  TYR C N   1 
ATOM   8304  C  CA  . TYR B  1 162 ? 45.583  32.697  60.923  1.00 73.39  ? 162  TYR C CA  1 
ATOM   8305  C  C   . TYR B  1 162 ? 44.486  32.266  59.943  1.00 67.87  ? 162  TYR C C   1 
ATOM   8306  O  O   . TYR B  1 162 ? 43.351  32.005  60.340  1.00 62.67  ? 162  TYR C O   1 
ATOM   8307  C  CB  . TYR B  1 162 ? 46.557  31.544  61.178  1.00 75.24  ? 162  TYR C CB  1 
ATOM   8308  C  CG  . TYR B  1 162 ? 47.689  31.874  62.122  1.00 76.88  ? 162  TYR C CG  1 
ATOM   8309  C  CD1 . TYR B  1 162 ? 47.498  31.870  63.496  1.00 84.42  ? 162  TYR C CD1 1 
ATOM   8310  C  CD2 . TYR B  1 162 ? 48.954  32.166  61.638  1.00 80.60  ? 162  TYR C CD2 1 
ATOM   8311  C  CE1 . TYR B  1 162 ? 48.536  32.163  64.363  1.00 85.99  ? 162  TYR C CE1 1 
ATOM   8312  C  CE2 . TYR B  1 162 ? 49.999  32.458  62.491  1.00 83.76  ? 162  TYR C CE2 1 
ATOM   8313  C  CZ  . TYR B  1 162 ? 49.785  32.456  63.854  1.00 87.31  ? 162  TYR C CZ  1 
ATOM   8314  O  OH  . TYR B  1 162 ? 50.823  32.748  64.711  1.00 88.07  ? 162  TYR C OH  1 
ATOM   8315  N  N   . TYR B  1 163 ? 44.816  32.197  58.662  1.00 64.98  ? 163  TYR C N   1 
ATOM   8316  C  CA  . TYR B  1 163 ? 43.833  31.781  57.668  1.00 65.20  ? 163  TYR C CA  1 
ATOM   8317  C  C   . TYR B  1 163 ? 44.340  30.555  56.951  1.00 63.10  ? 163  TYR C C   1 
ATOM   8318  O  O   . TYR B  1 163 ? 45.413  30.568  56.344  1.00 64.02  ? 163  TYR C O   1 
ATOM   8319  C  CB  . TYR B  1 163 ? 43.526  32.915  56.683  1.00 63.11  ? 163  TYR C CB  1 
ATOM   8320  C  CG  . TYR B  1 163 ? 42.800  34.056  57.356  1.00 61.16  ? 163  TYR C CG  1 
ATOM   8321  C  CD1 . TYR B  1 163 ? 43.480  34.937  58.192  1.00 65.54  ? 163  TYR C CD1 1 
ATOM   8322  C  CD2 . TYR B  1 163 ? 41.432  34.230  57.189  1.00 57.25  ? 163  TYR C CD2 1 
ATOM   8323  C  CE1 . TYR B  1 163 ? 42.823  35.969  58.833  1.00 69.75  ? 163  TYR C CE1 1 
ATOM   8324  C  CE2 . TYR B  1 163 ? 40.762  35.258  57.815  1.00 60.97  ? 163  TYR C CE2 1 
ATOM   8325  C  CZ  . TYR B  1 163 ? 41.462  36.129  58.642  1.00 74.52  ? 163  TYR C CZ  1 
ATOM   8326  O  OH  . TYR B  1 163 ? 40.807  37.162  59.280  1.00 75.19  ? 163  TYR C OH  1 
ATOM   8327  N  N   . VAL B  1 164 ? 43.580  29.476  57.072  1.00 60.09  ? 164  VAL C N   1 
ATOM   8328  C  CA  . VAL B  1 164 ? 43.911  28.242  56.378  1.00 57.46  ? 164  VAL C CA  1 
ATOM   8329  C  C   . VAL B  1 164 ? 43.155  28.211  55.067  1.00 53.29  ? 164  VAL C C   1 
ATOM   8330  O  O   . VAL B  1 164 ? 41.923  28.181  55.059  1.00 50.61  ? 164  VAL C O   1 
ATOM   8331  C  CB  . VAL B  1 164 ? 43.550  26.999  57.195  1.00 57.37  ? 164  VAL C CB  1 
ATOM   8332  C  CG1 . VAL B  1 164 ? 44.197  25.782  56.577  1.00 52.23  ? 164  VAL C CG1 1 
ATOM   8333  C  CG2 . VAL B  1 164 ? 43.988  27.166  58.653  1.00 59.95  ? 164  VAL C CG2 1 
ATOM   8334  N  N   . ALA B  1 165 ? 43.894  28.252  53.966  1.00 55.75  ? 165  ALA C N   1 
ATOM   8335  C  CA  . ALA B  1 165 ? 43.303  28.172  52.635  1.00 54.65  ? 165  ALA C CA  1 
ATOM   8336  C  C   . ALA B  1 165 ? 43.721  26.884  51.943  1.00 49.26  ? 165  ALA C C   1 
ATOM   8337  O  O   . ALA B  1 165 ? 44.883  26.460  52.031  1.00 48.50  ? 165  ALA C O   1 
ATOM   8338  C  CB  . ALA B  1 165 ? 43.701  29.385  51.794  1.00 47.97  ? 165  ALA C CB  1 
ATOM   8339  N  N   . MET B  1 166 ? 42.783  26.235  51.268  1.00 46.37  ? 166  MET C N   1 
ATOM   8340  C  CA  . MET B  1 166 ? 43.202  25.128  50.409  1.00 53.80  ? 166  MET C CA  1 
ATOM   8341  C  C   . MET B  1 166 ? 42.260  24.851  49.255  1.00 49.40  ? 166  MET C C   1 
ATOM   8342  O  O   . MET B  1 166 ? 41.081  25.216  49.294  1.00 47.66  ? 166  MET C O   1 
ATOM   8343  C  CB  . MET B  1 166 ? 43.411  23.828  51.211  1.00 54.20  ? 166  MET C CB  1 
ATOM   8344  C  CG  . MET B  1 166 ? 42.723  23.730  52.549  1.00 59.16  ? 166  MET C CG  1 
ATOM   8345  S  SD  . MET B  1 166 ? 43.238  22.272  53.498  1.00 67.95  ? 166  MET C SD  1 
ATOM   8346  C  CE  . MET B  1 166 ? 42.275  22.615  54.958  1.00 49.03  ? 166  MET C CE  1 
ATOM   8347  N  N   . ASP B  1 167 ? 42.832  24.219  48.229  1.00 46.70  ? 167  ASP C N   1 
ATOM   8348  C  CA  . ASP B  1 167 ? 42.126  23.727  47.052  1.00 43.35  ? 167  ASP C CA  1 
ATOM   8349  C  C   . ASP B  1 167 ? 42.004  22.224  47.142  1.00 46.11  ? 167  ASP C C   1 
ATOM   8350  O  O   . ASP B  1 167 ? 42.946  21.541  47.556  1.00 47.78  ? 167  ASP C O   1 
ATOM   8351  C  CB  . ASP B  1 167 ? 42.877  24.070  45.770  1.00 44.32  ? 167  ASP C CB  1 
ATOM   8352  C  CG  . ASP B  1 167 ? 43.104  25.543  45.604  1.00 53.61  ? 167  ASP C CG  1 
ATOM   8353  O  OD1 . ASP B  1 167 ? 42.165  26.325  45.853  1.00 51.05  ? 167  ASP C OD1 1 
ATOM   8354  O  OD2 . ASP B  1 167 ? 44.228  25.919  45.214  1.00 64.55  ? 167  ASP C OD2 1 
ATOM   8355  N  N   . PHE B  1 168 ? 40.872  21.694  46.709  1.00 38.98  ? 168  PHE C N   1 
ATOM   8356  C  CA  . PHE B  1 168 ? 40.670  20.257  46.766  1.00 43.78  ? 168  PHE C CA  1 
ATOM   8357  C  C   . PHE B  1 168 ? 39.627  19.840  45.736  1.00 42.36  ? 168  PHE C C   1 
ATOM   8358  O  O   . PHE B  1 168 ? 38.839  20.661  45.255  1.00 37.98  ? 168  PHE C O   1 
ATOM   8359  C  CB  . PHE B  1 168 ? 40.247  19.821  48.183  1.00 43.70  ? 168  PHE C CB  1 
ATOM   8360  C  CG  . PHE B  1 168 ? 39.135  20.656  48.756  1.00 41.49  ? 168  PHE C CG  1 
ATOM   8361  C  CD1 . PHE B  1 168 ? 39.400  21.900  49.322  1.00 39.50  ? 168  PHE C CD1 1 
ATOM   8362  C  CD2 . PHE B  1 168 ? 37.821  20.221  48.700  1.00 42.10  ? 168  PHE C CD2 1 
ATOM   8363  C  CE1 . PHE B  1 168 ? 38.384  22.685  49.826  1.00 35.40  ? 168  PHE C CE1 1 
ATOM   8364  C  CE2 . PHE B  1 168 ? 36.792  21.017  49.224  1.00 39.72  ? 168  PHE C CE2 1 
ATOM   8365  C  CZ  . PHE B  1 168 ? 37.087  22.253  49.773  1.00 36.09  ? 168  PHE C CZ  1 
ATOM   8366  N  N   . GLN B  1 169 ? 39.623  18.558  45.414  1.00 37.51  ? 169  GLN C N   1 
ATOM   8367  C  CA  . GLN B  1 169 ? 38.739  18.053  44.394  1.00 41.54  ? 169  GLN C CA  1 
ATOM   8368  C  C   . GLN B  1 169 ? 38.436  16.575  44.639  1.00 37.09  ? 169  GLN C C   1 
ATOM   8369  O  O   . GLN B  1 169 ? 39.173  15.899  45.368  1.00 37.80  ? 169  GLN C O   1 
ATOM   8370  C  CB  . GLN B  1 169 ? 39.379  18.256  43.028  1.00 37.99  ? 169  GLN C CB  1 
ATOM   8371  C  CG  . GLN B  1 169 ? 40.570  17.372  42.848  1.00 41.91  ? 169  GLN C CG  1 
ATOM   8372  C  CD  . GLN B  1 169 ? 41.515  17.900  41.815  1.00 51.50  ? 169  GLN C CD  1 
ATOM   8373  O  OE1 . GLN B  1 169 ? 41.523  19.097  41.520  1.00 54.33  ? 169  GLN C OE1 1 
ATOM   8374  N  NE2 . GLN B  1 169 ? 42.328  17.016  41.254  1.00 46.02  ? 169  GLN C NE2 1 
ATOM   8375  N  N   . ALA B  1 170 ? 37.342  16.101  44.049  1.00 29.28  ? 170  ALA C N   1 
ATOM   8376  C  CA  . ALA B  1 170 ? 36.965  14.690  44.104  1.00 37.46  ? 170  ALA C CA  1 
ATOM   8377  C  C   . ALA B  1 170 ? 35.788  14.408  43.174  1.00 36.28  ? 170  ALA C C   1 
ATOM   8378  O  O   . ALA B  1 170 ? 35.145  15.325  42.647  1.00 33.01  ? 170  ALA C O   1 
ATOM   8379  C  CB  . ALA B  1 170 ? 36.621  14.252  45.549  1.00 33.83  ? 170  ALA C CB  1 
ATOM   8380  N  N   . LYS B  1 171 ? 35.537  13.124  42.948  1.00 37.33  ? 171  LYS C N   1 
ATOM   8381  C  CA  . LYS B  1 171 ? 34.373  12.702  42.190  1.00 35.96  ? 171  LYS C CA  1 
ATOM   8382  C  C   . LYS B  1 171 ? 33.189  12.886  43.082  1.00 33.88  ? 171  LYS C C   1 
ATOM   8383  O  O   . LYS B  1 171 ? 33.332  12.771  44.291  1.00 40.20  ? 171  LYS C O   1 
ATOM   8384  C  CB  . LYS B  1 171 ? 34.475  11.244  41.762  1.00 34.43  ? 171  LYS C CB  1 
ATOM   8385  C  CG  . LYS B  1 171 ? 35.570  10.959  40.749  1.00 48.04  ? 171  LYS C CG  1 
ATOM   8386  C  CD  . LYS B  1 171 ? 35.647  9.465   40.476  1.00 50.00  ? 171  LYS C CD  1 
ATOM   8387  C  CE  . LYS B  1 171 ? 36.610  9.119   39.382  1.00 50.37  ? 171  LYS C CE  1 
ATOM   8388  N  NZ  . LYS B  1 171 ? 36.846  7.646   39.410  1.00 67.77  ? 171  LYS C NZ  1 
ATOM   8389  N  N   . LEU B  1 172 ? 32.025  13.182  42.511  1.00 33.00  ? 172  LEU C N   1 
ATOM   8390  C  CA  . LEU B  1 172 ? 30.810  13.137  43.290  1.00 30.85  ? 172  LEU C CA  1 
ATOM   8391  C  C   . LEU B  1 172 ? 30.654  11.757  43.907  1.00 40.73  ? 172  LEU C C   1 
ATOM   8392  O  O   . LEU B  1 172 ? 31.086  10.752  43.335  1.00 43.89  ? 172  LEU C O   1 
ATOM   8393  C  CB  . LEU B  1 172 ? 29.603  13.479  42.446  1.00 31.86  ? 172  LEU C CB  1 
ATOM   8394  C  CG  . LEU B  1 172 ? 29.497  14.957  42.153  1.00 35.56  ? 172  LEU C CG  1 
ATOM   8395  C  CD1 . LEU B  1 172 ? 28.337  15.155  41.241  1.00 32.20  ? 172  LEU C CD1 1 
ATOM   8396  C  CD2 . LEU B  1 172 ? 29.332  15.781  43.455  1.00 27.76  ? 172  LEU C CD2 1 
ATOM   8397  N  N   . GLY B  1 173 ? 30.061  11.724  45.095  1.00 42.39  ? 173  GLY C N   1 
ATOM   8398  C  CA  . GLY B  1 173 ? 29.887  10.500  45.838  1.00 33.45  ? 173  GLY C CA  1 
ATOM   8399  C  C   . GLY B  1 173 ? 29.100  9.427   45.104  1.00 42.62  ? 173  GLY C C   1 
ATOM   8400  O  O   . GLY B  1 173 ? 28.153  9.708   44.373  1.00 35.01  ? 173  GLY C O   1 
ATOM   8401  N  N   . ASP B  1 174 ? 29.518  8.186   45.342  1.00 53.60  ? 174  ASP C N   1 
ATOM   8402  C  CA  . ASP B  1 174 ? 28.924  6.978   44.790  1.00 50.93  ? 174  ASP C CA  1 
ATOM   8403  C  C   . ASP B  1 174 ? 27.665  6.542   45.516  1.00 49.62  ? 174  ASP C C   1 
ATOM   8404  O  O   . ASP B  1 174 ? 26.835  5.847   44.950  1.00 49.88  ? 174  ASP C O   1 
ATOM   8405  C  CB  . ASP B  1 174 ? 29.942  5.832   44.859  1.00 58.59  ? 174  ASP C CB  1 
ATOM   8406  C  CG  . ASP B  1 174 ? 30.519  5.481   43.504  1.00 70.54  ? 174  ASP C CG  1 
ATOM   8407  O  OD1 . ASP B  1 174 ? 29.799  5.670   42.498  1.00 72.70  ? 174  ASP C OD1 1 
ATOM   8408  O  OD2 . ASP B  1 174 ? 31.683  5.015   43.447  1.00 68.79  ? 174  ASP C OD2 1 
ATOM   8409  N  N   . GLY B  1 175 ? 27.540  6.902   46.789  1.00 49.44  ? 175  GLY C N   1 
ATOM   8410  C  CA  . GLY B  1 175 ? 26.464  6.340   47.569  1.00 46.01  ? 175  GLY C CA  1 
ATOM   8411  C  C   . GLY B  1 175 ? 25.998  7.021   48.832  1.00 52.71  ? 175  GLY C C   1 
ATOM   8412  O  O   . GLY B  1 175 ? 26.462  6.676   49.920  1.00 57.54  ? 175  GLY C O   1 
ATOM   8413  N  N   . PHE B  1 176 ? 25.068  7.965   48.685  1.00 49.04  ? 176  PHE C N   1 
ATOM   8414  C  CA  . PHE B  1 176 ? 24.297  8.504   49.820  1.00 47.67  ? 176  PHE C CA  1 
ATOM   8415  C  C   . PHE B  1 176 ? 25.038  9.404   50.814  1.00 44.08  ? 176  PHE C C   1 
ATOM   8416  O  O   . PHE B  1 176 ? 24.473  9.783   51.835  1.00 48.00  ? 176  PHE C O   1 
ATOM   8417  C  CB  . PHE B  1 176 ? 23.682  7.356   50.635  1.00 48.20  ? 176  PHE C CB  1 
ATOM   8418  C  CG  . PHE B  1 176 ? 22.724  6.495   49.866  1.00 59.67  ? 176  PHE C CG  1 
ATOM   8419  C  CD1 . PHE B  1 176 ? 22.013  7.010   48.785  1.00 59.88  ? 176  PHE C CD1 1 
ATOM   8420  C  CD2 . PHE B  1 176 ? 22.521  5.163   50.238  1.00 59.14  ? 176  PHE C CD2 1 
ATOM   8421  C  CE1 . PHE B  1 176 ? 21.114  6.206   48.084  1.00 67.62  ? 176  PHE C CE1 1 
ATOM   8422  C  CE2 . PHE B  1 176 ? 21.624  4.359   49.554  1.00 60.99  ? 176  PHE C CE2 1 
ATOM   8423  C  CZ  . PHE B  1 176 ? 20.922  4.879   48.468  1.00 66.82  ? 176  PHE C CZ  1 
ATOM   8424  N  N   . GLU B  1 177 ? 26.284  9.754   50.546  1.00 42.33  ? 177  GLU C N   1 
ATOM   8425  C  CA  . GLU B  1 177 ? 27.092  10.341  51.598  1.00 40.36  ? 177  GLU C CA  1 
ATOM   8426  C  C   . GLU B  1 177 ? 28.015  11.418  51.096  1.00 36.98  ? 177  GLU C C   1 
ATOM   8427  O  O   . GLU B  1 177 ? 28.601  11.260  50.037  1.00 32.45  ? 177  GLU C O   1 
ATOM   8428  C  CB  . GLU B  1 177 ? 27.929  9.256   52.270  1.00 45.64  ? 177  GLU C CB  1 
ATOM   8429  C  CG  . GLU B  1 177 ? 27.495  8.909   53.646  1.00 52.68  ? 177  GLU C CG  1 
ATOM   8430  C  CD  . GLU B  1 177 ? 28.190  7.668   54.140  1.00 60.74  ? 177  GLU C CD  1 
ATOM   8431  O  OE1 . GLU B  1 177 ? 29.402  7.740   54.449  1.00 62.83  ? 177  GLU C OE1 1 
ATOM   8432  O  OE2 . GLU B  1 177 ? 27.521  6.614   54.192  1.00 67.23  ? 177  GLU C OE2 1 
ATOM   8433  N  N   . GLY B  1 178 ? 28.201  12.473  51.894  1.00 34.35  ? 178  GLY C N   1 
ATOM   8434  C  CA  . GLY B  1 178 ? 29.053  13.583  51.503  1.00 37.68  ? 178  GLY C CA  1 
ATOM   8435  C  C   . GLY B  1 178 ? 28.370  14.369  50.394  1.00 33.68  ? 178  GLY C C   1 
ATOM   8436  O  O   . GLY B  1 178 ? 27.141  14.514  50.421  1.00 31.39  ? 178  GLY C O   1 
ATOM   8437  N  N   . PHE B  1 179 ? 29.158  14.842  49.421  1.00 32.55  ? 179  PHE C N   1 
ATOM   8438  C  CA  . PHE B  1 179 ? 28.631  15.473  48.194  1.00 32.95  ? 179  PHE C CA  1 
ATOM   8439  C  C   . PHE B  1 179 ? 28.419  14.406  47.156  1.00 28.82  ? 179  PHE C C   1 
ATOM   8440  O  O   . PHE B  1 179 ? 29.387  13.905  46.603  1.00 31.21  ? 179  PHE C O   1 
ATOM   8441  C  CB  . PHE B  1 179 ? 29.594  16.510  47.637  1.00 27.51  ? 179  PHE C CB  1 
ATOM   8442  C  CG  . PHE B  1 179 ? 28.945  17.524  46.745  1.00 29.42  ? 179  PHE C CG  1 
ATOM   8443  C  CD1 . PHE B  1 179 ? 27.565  17.643  46.692  1.00 30.23  ? 179  PHE C CD1 1 
ATOM   8444  C  CD2 . PHE B  1 179 ? 29.720  18.390  45.973  1.00 25.06  ? 179  PHE C CD2 1 
ATOM   8445  C  CE1 . PHE B  1 179 ? 26.966  18.586  45.880  1.00 28.47  ? 179  PHE C CE1 1 
ATOM   8446  C  CE2 . PHE B  1 179 ? 29.122  19.353  45.167  1.00 23.81  ? 179  PHE C CE2 1 
ATOM   8447  C  CZ  . PHE B  1 179 ? 27.749  19.452  45.118  1.00 23.22  ? 179  PHE C CZ  1 
ATOM   8448  N  N   . TYR B  1 180 ? 27.170  14.035  46.902  1.00 31.84  ? 180  TYR C N   1 
ATOM   8449  C  CA  . TYR B  1 180 ? 26.900  12.839  46.086  1.00 36.35  ? 180  TYR C CA  1 
ATOM   8450  C  C   . TYR B  1 180 ? 25.831  13.059  45.025  1.00 37.01  ? 180  TYR C C   1 
ATOM   8451  O  O   . TYR B  1 180 ? 25.016  13.974  45.120  1.00 36.38  ? 180  TYR C O   1 
ATOM   8452  C  CB  . TYR B  1 180 ? 26.500  11.639  46.973  1.00 33.48  ? 180  TYR C CB  1 
ATOM   8453  C  CG  . TYR B  1 180 ? 25.080  11.669  47.534  1.00 37.69  ? 180  TYR C CG  1 
ATOM   8454  C  CD1 . TYR B  1 180 ? 23.998  11.189  46.788  1.00 33.02  ? 180  TYR C CD1 1 
ATOM   8455  C  CD2 . TYR B  1 180 ? 24.824  12.152  48.814  1.00 33.72  ? 180  TYR C CD2 1 
ATOM   8456  C  CE1 . TYR B  1 180 ? 22.714  11.209  47.291  1.00 32.36  ? 180  TYR C CE1 1 
ATOM   8457  C  CE2 . TYR B  1 180 ? 23.538  12.176  49.318  1.00 34.11  ? 180  TYR C CE2 1 
ATOM   8458  C  CZ  . TYR B  1 180 ? 22.495  11.703  48.555  1.00 34.13  ? 180  TYR C CZ  1 
ATOM   8459  O  OH  . TYR B  1 180 ? 21.223  11.718  49.057  1.00 39.25  ? 180  TYR C OH  1 
ATOM   8460  N  N   . LYS B  1 181 ? 25.834  12.200  44.013  1.00 37.77  ? 181  LYS C N   1 
ATOM   8461  C  CA  . LYS B  1 181 ? 24.929  12.368  42.887  1.00 35.51  ? 181  LYS C CA  1 
ATOM   8462  C  C   . LYS B  1 181 ? 23.665  11.513  43.033  1.00 35.94  ? 181  LYS C C   1 
ATOM   8463  O  O   . LYS B  1 181 ? 23.661  10.465  43.662  1.00 30.06  ? 181  LYS C O   1 
ATOM   8464  C  CB  . LYS B  1 181 ? 25.641  12.024  41.579  1.00 40.35  ? 181  LYS C CB  1 
ATOM   8465  C  CG  . LYS B  1 181 ? 25.980  10.534  41.450  1.00 46.14  ? 181  LYS C CG  1 
ATOM   8466  C  CD  . LYS B  1 181 ? 26.526  10.176  40.072  1.00 48.55  ? 181  LYS C CD  1 
ATOM   8467  C  CE  . LYS B  1 181 ? 27.071  8.750   40.044  1.00 52.91  ? 181  LYS C CE  1 
ATOM   8468  N  NZ  . LYS B  1 181 ? 28.228  8.585   40.981  1.00 53.57  ? 181  LYS C NZ  1 
ATOM   8469  N  N   . SER B  1 182 ? 22.592  11.990  42.431  1.00 35.63  ? 182  SER C N   1 
ATOM   8470  C  CA  . SER B  1 182 ? 21.302  11.349  42.522  1.00 36.55  ? 182  SER C CA  1 
ATOM   8471  C  C   . SER B  1 182 ? 20.584  11.553  41.196  1.00 37.30  ? 182  SER C C   1 
ATOM   8472  O  O   . SER B  1 182 ? 20.875  12.512  40.465  1.00 37.63  ? 182  SER C O   1 
ATOM   8473  C  CB  . SER B  1 182 ? 20.501  11.932  43.687  1.00 37.03  ? 182  SER C CB  1 
ATOM   8474  O  OG  . SER B  1 182 ? 19.203  11.370  43.755  1.00 43.76  ? 182  SER C OG  1 
ATOM   8475  N  N   . THR B  1 183 ? 19.648  10.663  40.885  1.00 34.12  ? 183  THR C N   1 
ATOM   8476  C  CA  . THR B  1 183 ? 18.898  10.761  39.632  1.00 44.03  ? 183  THR C CA  1 
ATOM   8477  C  C   . THR B  1 183 ? 17.391  10.645  39.815  1.00 44.26  ? 183  THR C C   1 
ATOM   8478  O  O   . THR B  1 183 ? 16.928  9.976   40.723  1.00 50.60  ? 183  THR C O   1 
ATOM   8479  C  CB  . THR B  1 183 ? 19.307  9.668   38.646  1.00 48.46  ? 183  THR C CB  1 
ATOM   8480  O  OG1 . THR B  1 183 ? 19.156  8.383   39.279  1.00 50.54  ? 183  THR C OG1 1 
ATOM   8481  C  CG2 . THR B  1 183 ? 20.744  9.870   38.161  1.00 38.13  ? 183  THR C CG2 1 
ATOM   8482  N  N   . TYR B  1 184 ? 16.629  11.283  38.936  1.00 46.22  ? 184  TYR C N   1 
ATOM   8483  C  CA  . TYR B  1 184 ? 15.197  11.046  38.871  1.00 48.63  ? 184  TYR C CA  1 
ATOM   8484  C  C   . TYR B  1 184 ? 14.705  10.848  37.443  1.00 47.95  ? 184  TYR C C   1 
ATOM   8485  O  O   . TYR B  1 184 ? 15.326  11.334  36.509  1.00 37.81  ? 184  TYR C O   1 
ATOM   8486  C  CB  . TYR B  1 184 ? 14.435  12.189  39.505  1.00 41.24  ? 184  TYR C CB  1 
ATOM   8487  C  CG  . TYR B  1 184 ? 14.542  13.517  38.807  1.00 40.39  ? 184  TYR C CG  1 
ATOM   8488  C  CD1 . TYR B  1 184 ? 15.665  14.306  38.951  1.00 44.23  ? 184  TYR C CD1 1 
ATOM   8489  C  CD2 . TYR B  1 184 ? 13.497  14.003  38.039  1.00 44.76  ? 184  TYR C CD2 1 
ATOM   8490  C  CE1 . TYR B  1 184 ? 15.757  15.552  38.330  1.00 45.47  ? 184  TYR C CE1 1 
ATOM   8491  C  CE2 . TYR B  1 184 ? 13.575  15.236  37.416  1.00 46.93  ? 184  TYR C CE2 1 
ATOM   8492  C  CZ  . TYR B  1 184 ? 14.705  16.011  37.568  1.00 49.41  ? 184  TYR C CZ  1 
ATOM   8493  O  OH  . TYR B  1 184 ? 14.778  17.248  36.959  1.00 51.82  ? 184  TYR C OH  1 
ATOM   8494  N  N   . ARG B  1 185 ? 13.593  10.118  37.317  1.00 52.24  ? 185  ARG C N   1 
ATOM   8495  C  CA  . ARG B  1 185 ? 12.850  9.938   36.074  1.00 50.20  ? 185  ARG C CA  1 
ATOM   8496  C  C   . ARG B  1 185 ? 11.921  11.135  35.826  1.00 51.36  ? 185  ARG C C   1 
ATOM   8497  O  O   . ARG B  1 185 ? 11.427  11.747  36.763  1.00 50.96  ? 185  ARG C O   1 
ATOM   8498  C  CB  . ARG B  1 185 ? 12.038  8.636   36.114  1.00 51.92  ? 185  ARG C CB  1 
ATOM   8499  C  CG  . ARG B  1 185 ? 11.443  8.207   34.764  1.00 59.98  ? 185  ARG C CG  1 
ATOM   8500  C  CD  . ARG B  1 185 ? 10.144  7.406   34.920  1.00 62.22  ? 185  ARG C CD  1 
ATOM   8501  N  NE  . ARG B  1 185 ? 9.670   6.843   33.653  1.00 65.77  ? 185  ARG C NE  1 
ATOM   8502  C  CZ  . ARG B  1 185 ? 8.694   7.353   32.900  1.00 68.16  ? 185  ARG C CZ  1 
ATOM   8503  N  NH1 . ARG B  1 185 ? 8.057   8.456   33.269  1.00 66.79  ? 185  ARG C NH1 1 
ATOM   8504  N  NH2 . ARG B  1 185 ? 8.348   6.751   31.766  1.00 66.07  ? 185  ARG C NH2 1 
ATOM   8505  N  N   . THR B  1 186 ? 11.712  11.492  34.562  1.00 54.24  ? 186  THR C N   1 
ATOM   8506  C  CA  . THR B  1 186 ? 10.741  12.530  34.218  1.00 53.63  ? 186  THR C CA  1 
ATOM   8507  C  C   . THR B  1 186 ? 9.460   11.902  33.677  1.00 57.85  ? 186  THR C C   1 
ATOM   8508  O  O   . THR B  1 186 ? 9.430   10.712  33.346  1.00 55.69  ? 186  THR C O   1 
ATOM   8509  C  CB  . THR B  1 186 ? 11.286  13.505  33.173  1.00 48.30  ? 186  THR C CB  1 
ATOM   8510  O  OG1 . THR B  1 186 ? 11.497  12.811  31.934  1.00 50.38  ? 186  THR C OG1 1 
ATOM   8511  C  CG2 . THR B  1 186 ? 12.590  14.122  33.635  1.00 48.95  ? 186  THR C CG2 1 
ATOM   8512  N  N   . LEU B  1 187 ? 8.410   12.711  33.565  1.00 58.81  ? 187  LEU C N   1 
ATOM   8513  C  CA  . LEU B  1 187 ? 7.147   12.244  32.990  1.00 57.63  ? 187  LEU C CA  1 
ATOM   8514  C  C   . LEU B  1 187 ? 7.345   11.650  31.613  1.00 55.10  ? 187  LEU C C   1 
ATOM   8515  O  O   . LEU B  1 187 ? 6.577   10.787  31.198  1.00 65.40  ? 187  LEU C O   1 
ATOM   8516  C  CB  . LEU B  1 187 ? 6.127   13.380  32.912  1.00 60.09  ? 187  LEU C CB  1 
ATOM   8517  C  CG  . LEU B  1 187 ? 4.785   13.054  32.263  1.00 55.85  ? 187  LEU C CG  1 
ATOM   8518  C  CD1 . LEU B  1 187 ? 4.177   11.822  32.908  1.00 57.45  ? 187  LEU C CD1 1 
ATOM   8519  C  CD2 . LEU B  1 187 ? 3.856   14.243  32.385  1.00 54.85  ? 187  LEU C CD2 1 
ATOM   8520  N  N   . GLY B  1 188 ? 8.383   12.099  30.909  1.00 57.29  ? 188  GLY C N   1 
ATOM   8521  C  CA  . GLY B  1 188 ? 8.663   11.619  29.563  1.00 50.51  ? 188  GLY C CA  1 
ATOM   8522  C  C   . GLY B  1 188 ? 9.582   10.409  29.525  1.00 55.27  ? 188  GLY C C   1 
ATOM   8523  O  O   . GLY B  1 188 ? 9.792   9.803   28.476  1.00 50.12  ? 188  GLY C O   1 
ATOM   8524  N  N   . GLY B  1 189 ? 10.142  10.044  30.671  1.00 54.82  ? 189  GLY C N   1 
ATOM   8525  C  CA  . GLY B  1 189 ? 11.088  8.951   30.686  1.00 50.30  ? 189  GLY C CA  1 
ATOM   8526  C  C   . GLY B  1 189 ? 12.533  9.393   30.570  1.00 45.66  ? 189  GLY C C   1 
ATOM   8527  O  O   . GLY B  1 189 ? 13.424  8.561   30.426  1.00 49.33  ? 189  GLY C O   1 
ATOM   8528  N  N   . GLU B  1 190 ? 12.778  10.697  30.639  1.00 46.62  ? 190  GLU C N   1 
ATOM   8529  C  CA  . GLU B  1 190 ? 14.147  11.197  30.674  1.00 45.26  ? 190  GLU C CA  1 
ATOM   8530  C  C   . GLU B  1 190 ? 14.688  10.998  32.072  1.00 51.17  ? 190  GLU C C   1 
ATOM   8531  O  O   . GLU B  1 190 ? 13.923  10.843  33.022  1.00 56.74  ? 190  GLU C O   1 
ATOM   8532  C  CB  . GLU B  1 190 ? 14.226  12.682  30.285  1.00 46.64  ? 190  GLU C CB  1 
ATOM   8533  C  CG  . GLU B  1 190 ? 14.066  13.004  28.782  1.00 41.29  ? 190  GLU C CG  1 
ATOM   8534  C  CD  . GLU B  1 190 ? 14.598  14.398  28.417  1.00 48.14  ? 190  GLU C CD  1 
ATOM   8535  O  OE1 . GLU B  1 190 ? 14.242  15.385  29.103  1.00 53.52  ? 190  GLU C OE1 1 
ATOM   8536  O  OE2 . GLU B  1 190 ? 15.376  14.518  27.443  1.00 47.05  ? 190  GLU C OE2 1 
ATOM   8537  N  N   . THR B  1 191 ? 16.003  10.992  32.223  1.00 51.89  ? 191  THR C N   1 
ATOM   8538  C  CA  . THR B  1 191 ? 16.562  11.051  33.559  1.00 43.68  ? 191  THR C CA  1 
ATOM   8539  C  C   . THR B  1 191 ? 17.523  12.236  33.707  1.00 53.25  ? 191  THR C C   1 
ATOM   8540  O  O   . THR B  1 191 ? 18.372  12.470  32.834  1.00 50.11  ? 191  THR C O   1 
ATOM   8541  C  CB  . THR B  1 191 ? 17.289  9.775   33.922  1.00 41.68  ? 191  THR C CB  1 
ATOM   8542  O  OG1 . THR B  1 191 ? 18.514  9.701   33.193  1.00 53.53  ? 191  THR C OG1 1 
ATOM   8543  C  CG2 . THR B  1 191 ? 16.436  8.573   33.619  1.00 51.55  ? 191  THR C CG2 1 
ATOM   8544  N  N   . ARG B  1 192 ? 17.374  12.988  34.805  1.00 46.45  ? 192  ARG C N   1 
ATOM   8545  C  CA  . ARG B  1 192 ? 18.297  14.075  35.119  1.00 42.24  ? 192  ARG C CA  1 
ATOM   8546  C  C   . ARG B  1 192 ? 19.119  13.785  36.377  1.00 44.37  ? 192  ARG C C   1 
ATOM   8547  O  O   . ARG B  1 192 ? 18.736  12.984  37.240  1.00 44.48  ? 192  ARG C O   1 
ATOM   8548  C  CB  . ARG B  1 192 ? 17.548  15.383  35.291  1.00 44.23  ? 192  ARG C CB  1 
ATOM   8549  C  CG  . ARG B  1 192 ? 16.368  15.535  34.377  1.00 47.43  ? 192  ARG C CG  1 
ATOM   8550  C  CD  . ARG B  1 192 ? 16.629  16.559  33.302  1.00 50.23  ? 192  ARG C CD  1 
ATOM   8551  N  NE  . ARG B  1 192 ? 15.555  16.545  32.318  1.00 52.95  ? 192  ARG C NE  1 
ATOM   8552  C  CZ  . ARG B  1 192 ? 14.391  17.163  32.482  1.00 60.93  ? 192  ARG C CZ  1 
ATOM   8553  N  NH1 . ARG B  1 192 ? 14.145  17.845  33.600  1.00 63.77  ? 192  ARG C NH1 1 
ATOM   8554  N  NH2 . ARG B  1 192 ? 13.469  17.098  31.531  1.00 58.75  ? 192  ARG C NH2 1 
ATOM   8555  N  N   . ILE B  1 193 ? 20.266  14.440  36.459  1.00 39.36  ? 193  ILE C N   1 
ATOM   8556  C  CA  . ILE B  1 193 ? 21.171  14.259  37.570  1.00 36.07  ? 193  ILE C CA  1 
ATOM   8557  C  C   . ILE B  1 193 ? 21.060  15.428  38.542  1.00 35.00  ? 193  ILE C C   1 
ATOM   8558  O  O   . ILE B  1 193 ? 20.475  16.441  38.229  1.00 33.07  ? 193  ILE C O   1 
ATOM   8559  C  CB  . ILE B  1 193 ? 22.575  14.040  37.042  1.00 34.57  ? 193  ILE C CB  1 
ATOM   8560  C  CG1 . ILE B  1 193 ? 22.693  12.566  36.706  1.00 43.48  ? 193  ILE C CG1 1 
ATOM   8561  C  CG2 . ILE B  1 193 ? 23.669  14.358  38.054  1.00 36.23  ? 193  ILE C CG2 1 
ATOM   8562  C  CD1 . ILE B  1 193 ? 24.067  12.177  36.344  1.00 52.73  ? 193  ILE C CD1 1 
ATOM   8563  N  N   . LEU B  1 194 ? 21.572  15.219  39.747  1.00 39.80  ? 194  LEU C N   1 
ATOM   8564  C  CA  . LEU B  1 194 ? 21.353  16.043  40.903  1.00 34.48  ? 194  LEU C CA  1 
ATOM   8565  C  C   . LEU B  1 194 ? 22.614  15.950  41.731  1.00 35.88  ? 194  LEU C C   1 
ATOM   8566  O  O   . LEU B  1 194 ? 23.092  14.849  41.939  1.00 37.00  ? 194  LEU C O   1 
ATOM   8567  C  CB  . LEU B  1 194 ? 20.187  15.469  41.678  1.00 46.95  ? 194  LEU C CB  1 
ATOM   8568  C  CG  . LEU B  1 194 ? 18.923  16.176  42.100  1.00 51.88  ? 194  LEU C CG  1 
ATOM   8569  C  CD1 . LEU B  1 194 ? 17.778  15.351  41.551  1.00 47.89  ? 194  LEU C CD1 1 
ATOM   8570  C  CD2 . LEU B  1 194 ? 18.876  16.185  43.612  1.00 38.35  ? 194  LEU C CD2 1 
ATOM   8571  N  N   . ALA B  1 195 ? 23.170  17.044  42.230  1.00 35.73  ? 195  ALA C N   1 
ATOM   8572  C  CA  . ALA B  1 195 ? 24.248  16.877  43.206  1.00 31.48  ? 195  ALA C CA  1 
ATOM   8573  C  C   . ALA B  1 195 ? 23.835  17.399  44.609  1.00 39.05  ? 195  ALA C C   1 
ATOM   8574  O  O   . ALA B  1 195 ? 23.452  18.572  44.769  1.00 32.41  ? 195  ALA C O   1 
ATOM   8575  C  CB  . ALA B  1 195 ? 25.498  17.548  42.730  1.00 29.70  ? 195  ALA C CB  1 
ATOM   8576  N  N   . VAL B  1 196 ? 23.906  16.503  45.610  1.00 39.80  ? 196  VAL C N   1 
ATOM   8577  C  CA  . VAL B  1 196 ? 23.385  16.741  46.973  1.00 30.14  ? 196  VAL C CA  1 
ATOM   8578  C  C   . VAL B  1 196 ? 24.367  16.429  48.090  1.00 30.34  ? 196  VAL C C   1 
ATOM   8579  O  O   . VAL B  1 196 ? 25.177  15.509  47.998  1.00 30.68  ? 196  VAL C O   1 
ATOM   8580  C  CB  . VAL B  1 196 ? 22.150  15.901  47.268  1.00 34.23  ? 196  VAL C CB  1 
ATOM   8581  C  CG1 . VAL B  1 196 ? 21.313  16.580  48.325  1.00 38.45  ? 196  VAL C CG1 1 
ATOM   8582  C  CG2 . VAL B  1 196 ? 21.353  15.694  46.030  1.00 36.98  ? 196  VAL C CG2 1 
ATOM   8583  N  N   . THR B  1 197 ? 24.264  17.183  49.171  1.00 32.34  ? 197  THR C N   1 
ATOM   8584  C  CA  . THR B  1 197 ? 25.074  16.920  50.359  1.00 36.27  ? 197  THR C CA  1 
ATOM   8585  C  C   . THR B  1 197 ? 24.297  16.155  51.419  1.00 34.13  ? 197  THR C C   1 
ATOM   8586  O  O   . THR B  1 197 ? 23.072  16.245  51.492  1.00 33.35  ? 197  THR C O   1 
ATOM   8587  C  CB  . THR B  1 197 ? 25.583  18.216  51.008  1.00 29.98  ? 197  THR C CB  1 
ATOM   8588  O  OG1 . THR B  1 197 ? 24.461  19.042  51.317  1.00 35.28  ? 197  THR C OG1 1 
ATOM   8589  C  CG2 . THR B  1 197 ? 26.472  18.955  50.078  1.00 30.17  ? 197  THR C CG2 1 
ATOM   8590  N  N   . ASP B  1 198 ? 25.022  15.412  52.246  1.00 33.42  ? 198  ASP C N   1 
ATOM   8591  C  CA  . ASP B  1 198 ? 24.443  14.837  53.449  1.00 33.45  ? 198  ASP C CA  1 
ATOM   8592  C  C   . ASP B  1 198 ? 25.571  14.455  54.401  1.00 35.79  ? 198  ASP C C   1 
ATOM   8593  O  O   . ASP B  1 198 ? 26.409  13.613  54.090  1.00 32.41  ? 198  ASP C O   1 
ATOM   8594  C  CB  . ASP B  1 198 ? 23.569  13.637  53.124  1.00 34.84  ? 198  ASP C CB  1 
ATOM   8595  C  CG  . ASP B  1 198 ? 22.916  13.069  54.352  1.00 40.30  ? 198  ASP C CG  1 
ATOM   8596  O  OD1 . ASP B  1 198 ? 21.882  13.612  54.796  1.00 43.37  ? 198  ASP C OD1 1 
ATOM   8597  O  OD2 . ASP B  1 198 ? 23.455  12.089  54.889  1.00 45.55  ? 198  ASP C OD2 1 
ATOM   8598  N  N   . PHE B  1 199 ? 25.605  15.097  55.565  1.00 39.53  ? 199  PHE C N   1 
ATOM   8599  C  CA  . PHE B  1 199 ? 26.837  15.122  56.329  1.00 36.64  ? 199  PHE C CA  1 
ATOM   8600  C  C   . PHE B  1 199 ? 26.734  14.465  57.691  1.00 33.96  ? 199  PHE C C   1 
ATOM   8601  O  O   . PHE B  1 199 ? 27.752  14.060  58.238  1.00 33.68  ? 199  PHE C O   1 
ATOM   8602  C  CB  . PHE B  1 199 ? 27.316  16.564  56.500  1.00 32.41  ? 199  PHE C CB  1 
ATOM   8603  C  CG  . PHE B  1 199 ? 27.833  17.167  55.253  1.00 33.78  ? 199  PHE C CG  1 
ATOM   8604  C  CD1 . PHE B  1 199 ? 28.274  16.363  54.221  1.00 37.09  ? 199  PHE C CD1 1 
ATOM   8605  C  CD2 . PHE B  1 199 ? 27.864  18.538  55.095  1.00 34.28  ? 199  PHE C CD2 1 
ATOM   8606  C  CE1 . PHE B  1 199 ? 28.755  16.906  53.062  1.00 33.36  ? 199  PHE C CE1 1 
ATOM   8607  C  CE2 . PHE B  1 199 ? 28.339  19.101  53.942  1.00 36.46  ? 199  PHE C CE2 1 
ATOM   8608  C  CZ  . PHE B  1 199 ? 28.785  18.293  52.918  1.00 36.94  ? 199  PHE C CZ  1 
ATOM   8609  N  N   . GLU B  1 200 ? 25.533  14.371  58.242  1.00 24.01  ? 200  GLU C N   1 
ATOM   8610  C  CA  . GLU B  1 200 ? 25.425  13.861  59.601  1.00 38.48  ? 200  GLU C CA  1 
ATOM   8611  C  C   . GLU B  1 200 ? 25.688  12.350  59.643  1.00 41.01  ? 200  GLU C C   1 
ATOM   8612  O  O   . GLU B  1 200 ? 25.060  11.570  58.939  1.00 37.40  ? 200  GLU C O   1 
ATOM   8613  C  CB  . GLU B  1 200 ? 24.057  14.177  60.228  1.00 41.53  ? 200  GLU C CB  1 
ATOM   8614  C  CG  . GLU B  1 200 ? 24.075  13.993  61.742  1.00 37.40  ? 200  GLU C CG  1 
ATOM   8615  C  CD  . GLU B  1 200 ? 22.780  14.316  62.438  1.00 41.43  ? 200  GLU C CD  1 
ATOM   8616  O  OE1 . GLU B  1 200 ? 21.691  14.155  61.845  1.00 39.76  ? 200  GLU C OE1 1 
ATOM   8617  O  OE2 . GLU B  1 200 ? 22.860  14.710  63.620  1.00 42.84  ? 200  GLU C OE2 1 
ATOM   8618  N  N   . PRO B  1 201 ? 26.605  11.937  60.517  1.00 42.68  ? 201  PRO C N   1 
ATOM   8619  C  CA  . PRO B  1 201 ? 27.231  12.833  61.486  1.00 34.66  ? 201  PRO C CA  1 
ATOM   8620  C  C   . PRO B  1 201 ? 28.647  13.255  61.166  1.00 30.34  ? 201  PRO C C   1 
ATOM   8621  O  O   . PRO B  1 201 ? 29.076  14.304  61.625  1.00 32.73  ? 201  PRO C O   1 
ATOM   8622  C  CB  . PRO B  1 201 ? 27.212  11.994  62.760  1.00 36.77  ? 201  PRO C CB  1 
ATOM   8623  C  CG  . PRO B  1 201 ? 27.380  10.626  62.270  1.00 40.52  ? 201  PRO C CG  1 
ATOM   8624  C  CD  . PRO B  1 201 ? 26.785  10.530  60.889  1.00 44.84  ? 201  PRO C CD  1 
ATOM   8625  N  N   . THR B  1 202 ? 29.374  12.448  60.419  1.00 29.90  ? 202  THR C N   1 
ATOM   8626  C  CA  . THR B  1 202 ? 30.787  12.708  60.217  1.00 31.68  ? 202  THR C CA  1 
ATOM   8627  C  C   . THR B  1 202 ? 31.189  12.710  58.743  1.00 35.94  ? 202  THR C C   1 
ATOM   8628  O  O   . THR B  1 202 ? 32.319  12.341  58.418  1.00 34.55  ? 202  THR C O   1 
ATOM   8629  C  CB  . THR B  1 202 ? 31.654  11.652  60.957  1.00 39.27  ? 202  THR C CB  1 
ATOM   8630  O  OG1 . THR B  1 202 ? 31.211  10.346  60.588  1.00 41.92  ? 202  THR C OG1 1 
ATOM   8631  C  CG2 . THR B  1 202 ? 31.533  11.782  62.481  1.00 35.79  ? 202  THR C CG2 1 
ATOM   8632  N  N   . GLN B  1 203 ? 30.296  13.126  57.843  1.00 33.53  ? 203  GLN C N   1 
ATOM   8633  C  CA  . GLN B  1 203 ? 30.683  13.138  56.422  1.00 39.36  ? 203  GLN C CA  1 
ATOM   8634  C  C   . GLN B  1 203 ? 30.999  14.517  55.825  1.00 37.65  ? 203  GLN C C   1 
ATOM   8635  O  O   . GLN B  1 203 ? 31.385  14.583  54.655  1.00 39.69  ? 203  GLN C O   1 
ATOM   8636  C  CB  . GLN B  1 203 ? 29.612  12.476  55.549  1.00 40.39  ? 203  GLN C CB  1 
ATOM   8637  C  CG  . GLN B  1 203 ? 29.351  11.029  55.881  1.00 39.17  ? 203  GLN C CG  1 
ATOM   8638  C  CD  . GLN B  1 203 ? 28.243  10.888  56.909  1.00 48.74  ? 203  GLN C CD  1 
ATOM   8639  O  OE1 . GLN B  1 203 ? 28.480  10.436  58.052  1.00 45.08  ? 203  GLN C OE1 1 
ATOM   8640  N  NE2 . GLN B  1 203 ? 27.012  11.282  56.513  1.00 40.20  ? 203  GLN C NE2 1 
ATOM   8641  N  N   . ALA B  1 204 ? 30.864  15.602  56.592  1.00 32.48  ? 204  ALA C N   1 
ATOM   8642  C  CA  . ALA B  1 204 ? 31.260  16.917  56.072  1.00 35.34  ? 204  ALA C CA  1 
ATOM   8643  C  C   . ALA B  1 204 ? 32.668  16.840  55.520  1.00 37.51  ? 204  ALA C C   1 
ATOM   8644  O  O   . ALA B  1 204 ? 32.982  17.456  54.515  1.00 38.22  ? 204  ALA C O   1 
ATOM   8645  C  CB  . ALA B  1 204 ? 31.185  17.979  57.127  1.00 36.08  ? 204  ALA C CB  1 
ATOM   8646  N  N   . ARG B  1 205 ? 33.494  16.041  56.185  1.00 35.30  ? 205  ARG C N   1 
ATOM   8647  C  CA  . ARG B  1 205 ? 34.891  15.885  55.841  1.00 38.16  ? 205  ARG C CA  1 
ATOM   8648  C  C   . ARG B  1 205 ? 35.111  15.174  54.497  1.00 42.61  ? 205  ARG C C   1 
ATOM   8649  O  O   . ARG B  1 205 ? 36.254  15.075  54.010  1.00 39.82  ? 205  ARG C O   1 
ATOM   8650  C  CB  . ARG B  1 205 ? 35.599  15.116  56.963  1.00 44.51  ? 205  ARG C CB  1 
ATOM   8651  C  CG  . ARG B  1 205 ? 35.056  13.692  57.204  1.00 40.40  ? 205  ARG C CG  1 
ATOM   8652  C  CD  . ARG B  1 205 ? 35.598  13.053  58.498  1.00 36.36  ? 205  ARG C CD  1 
ATOM   8653  N  NE  . ARG B  1 205 ? 35.010  13.669  59.685  1.00 41.26  ? 205  ARG C NE  1 
ATOM   8654  C  CZ  . ARG B  1 205 ? 35.123  13.181  60.923  1.00 41.53  ? 205  ARG C CZ  1 
ATOM   8655  N  NH1 . ARG B  1 205 ? 35.803  12.064  61.148  1.00 39.57  ? 205  ARG C NH1 1 
ATOM   8656  N  NH2 . ARG B  1 205 ? 34.561  13.814  61.937  1.00 33.17  ? 205  ARG C NH2 1 
ATOM   8657  N  N   . MET B  1 206 ? 34.039  14.649  53.906  1.00 39.92  ? 206  MET C N   1 
ATOM   8658  C  CA  . MET B  1 206 ? 34.165  14.018  52.588  1.00 39.50  ? 206  MET C CA  1 
ATOM   8659  C  C   . MET B  1 206 ? 34.001  15.068  51.505  1.00 37.97  ? 206  MET C C   1 
ATOM   8660  O  O   . MET B  1 206 ? 34.330  14.824  50.346  1.00 42.94  ? 206  MET C O   1 
ATOM   8661  C  CB  . MET B  1 206 ? 33.136  12.900  52.397  1.00 37.48  ? 206  MET C CB  1 
ATOM   8662  C  CG  . MET B  1 206 ? 33.392  11.646  53.232  1.00 39.94  ? 206  MET C CG  1 
ATOM   8663  S  SD  . MET B  1 206 ? 32.044  10.465  53.042  1.00 50.71  ? 206  MET C SD  1 
ATOM   8664  C  CE  . MET B  1 206 ? 32.832  8.945   53.575  1.00 56.04  ? 206  MET C CE  1 
ATOM   8665  N  N   . ALA B  1 207 ? 33.503  16.238  51.902  1.00 34.15  ? 207  ALA C N   1 
ATOM   8666  C  CA  . ALA B  1 207 ? 33.158  17.298  50.971  1.00 35.78  ? 207  ALA C CA  1 
ATOM   8667  C  C   . ALA B  1 207 ? 34.100  18.488  51.042  1.00 37.72  ? 207  ALA C C   1 
ATOM   8668  O  O   . ALA B  1 207 ? 34.291  19.186  50.056  1.00 46.74  ? 207  ALA C O   1 
ATOM   8669  C  CB  . ALA B  1 207 ? 31.747  17.752  51.210  1.00 33.26  ? 207  ALA C CB  1 
ATOM   8670  N  N   . PHE B  1 208 ? 34.660  18.747  52.208  1.00 38.61  ? 208  PHE C N   1 
ATOM   8671  C  CA  . PHE B  1 208 ? 35.638  19.817  52.356  1.00 40.56  ? 208  PHE C CA  1 
ATOM   8672  C  C   . PHE B  1 208 ? 36.333  19.603  53.662  1.00 40.97  ? 208  PHE C C   1 
ATOM   8673  O  O   . PHE B  1 208 ? 35.699  19.190  54.625  1.00 40.20  ? 208  PHE C O   1 
ATOM   8674  C  CB  . PHE B  1 208 ? 34.994  21.212  52.316  1.00 35.26  ? 208  PHE C CB  1 
ATOM   8675  C  CG  . PHE B  1 208 ? 33.947  21.441  53.361  1.00 37.15  ? 208  PHE C CG  1 
ATOM   8676  C  CD1 . PHE B  1 208 ? 32.622  21.130  53.109  1.00 39.12  ? 208  PHE C CD1 1 
ATOM   8677  C  CD2 . PHE B  1 208 ? 34.276  22.014  54.589  1.00 40.57  ? 208  PHE C CD2 1 
ATOM   8678  C  CE1 . PHE B  1 208 ? 31.633  21.360  54.074  1.00 40.17  ? 208  PHE C CE1 1 
ATOM   8679  C  CE2 . PHE B  1 208 ? 33.296  22.251  55.564  1.00 36.72  ? 208  PHE C CE2 1 
ATOM   8680  C  CZ  . PHE B  1 208 ? 31.974  21.917  55.306  1.00 37.94  ? 208  PHE C CZ  1 
ATOM   8681  N  N   . PRO B  1 209 ? 37.640  19.879  53.706  1.00 44.14  ? 209  PRO C N   1 
ATOM   8682  C  CA  . PRO B  1 209 ? 38.349  19.702  54.975  1.00 42.22  ? 209  PRO C CA  1 
ATOM   8683  C  C   . PRO B  1 209 ? 37.762  20.642  56.006  1.00 42.29  ? 209  PRO C C   1 
ATOM   8684  O  O   . PRO B  1 209 ? 37.443  21.777  55.679  1.00 41.30  ? 209  PRO C O   1 
ATOM   8685  C  CB  . PRO B  1 209 ? 39.796  20.065  54.635  1.00 46.15  ? 209  PRO C CB  1 
ATOM   8686  C  CG  . PRO B  1 209 ? 39.878  19.973  53.135  1.00 45.85  ? 209  PRO C CG  1 
ATOM   8687  C  CD  . PRO B  1 209 ? 38.518  20.405  52.648  1.00 39.62  ? 209  PRO C CD  1 
ATOM   8688  N  N   . CYS B  1 210 ? 37.557  20.152  57.220  1.00 47.89  ? 210  CYS C N   1 
ATOM   8689  C  CA  . CYS B  1 210 ? 36.998  20.980  58.271  1.00 39.91  ? 210  CYS C CA  1 
ATOM   8690  C  C   . CYS B  1 210 ? 37.328  20.370  59.613  1.00 43.63  ? 210  CYS C C   1 
ATOM   8691  O  O   . CYS B  1 210 ? 37.879  19.258  59.688  1.00 44.75  ? 210  CYS C O   1 
ATOM   8692  C  CB  . CYS B  1 210 ? 35.480  21.137  58.103  1.00 40.59  ? 210  CYS C CB  1 
ATOM   8693  S  SG  . CYS B  1 210 ? 34.561  19.571  57.890  1.00 44.34  ? 210  CYS C SG  1 
ATOM   8694  N  N   . PHE B  1 211 ? 37.058  21.135  60.671  1.00 46.33  ? 211  PHE C N   1 
ATOM   8695  C  CA  . PHE B  1 211 ? 37.090  20.622  62.037  1.00 42.61  ? 211  PHE C CA  1 
ATOM   8696  C  C   . PHE B  1 211 ? 35.728  19.988  62.228  1.00 40.77  ? 211  PHE C C   1 
ATOM   8697  O  O   . PHE B  1 211 ? 34.770  20.655  62.644  1.00 38.78  ? 211  PHE C O   1 
ATOM   8698  C  CB  . PHE B  1 211 ? 37.356  21.731  63.067  1.00 49.06  ? 211  PHE C CB  1 
ATOM   8699  C  CG  . PHE B  1 211 ? 38.670  22.455  62.870  1.00 50.93  ? 211  PHE C CG  1 
ATOM   8700  C  CD1 . PHE B  1 211 ? 38.756  23.550  62.027  1.00 52.52  ? 211  PHE C CD1 1 
ATOM   8701  C  CD2 . PHE B  1 211 ? 39.815  22.039  63.534  1.00 51.63  ? 211  PHE C CD2 1 
ATOM   8702  C  CE1 . PHE B  1 211 ? 39.960  24.220  61.853  1.00 55.37  ? 211  PHE C CE1 1 
ATOM   8703  C  CE2 . PHE B  1 211 ? 41.022  22.701  63.361  1.00 50.39  ? 211  PHE C CE2 1 
ATOM   8704  C  CZ  . PHE B  1 211 ? 41.095  23.788  62.519  1.00 55.20  ? 211  PHE C CZ  1 
ATOM   8705  N  N   . ASP B  1 212 ? 35.642  18.710  61.863  1.00 37.52  ? 212  ASP C N   1 
ATOM   8706  C  CA  . ASP B  1 212 ? 34.366  18.038  61.683  1.00 38.24  ? 212  ASP C CA  1 
ATOM   8707  C  C   . ASP B  1 212 ? 33.916  17.378  62.988  1.00 41.93  ? 212  ASP C C   1 
ATOM   8708  O  O   . ASP B  1 212 ? 33.710  16.150  63.034  1.00 34.82  ? 212  ASP C O   1 
ATOM   8709  C  CB  . ASP B  1 212 ? 34.474  17.001  60.559  1.00 37.99  ? 212  ASP C CB  1 
ATOM   8710  C  CG  . ASP B  1 212 ? 33.112  16.563  60.015  1.00 35.44  ? 212  ASP C CG  1 
ATOM   8711  O  OD1 . ASP B  1 212 ? 32.097  17.209  60.333  1.00 34.75  ? 212  ASP C OD1 1 
ATOM   8712  O  OD2 . ASP B  1 212 ? 33.064  15.583  59.247  1.00 34.63  ? 212  ASP C OD2 1 
ATOM   8713  N  N   . GLU B  1 213 ? 33.801  18.207  64.035  1.00 41.91  ? 213  GLU C N   1 
ATOM   8714  C  CA  . GLU B  1 213 ? 33.212  17.854  65.341  1.00 41.12  ? 213  GLU C CA  1 
ATOM   8715  C  C   . GLU B  1 213 ? 32.230  18.943  65.701  1.00 42.92  ? 213  GLU C C   1 
ATOM   8716  O  O   . GLU B  1 213 ? 32.542  20.125  65.573  1.00 46.06  ? 213  GLU C O   1 
ATOM   8717  C  CB  . GLU B  1 213 ? 34.279  17.712  66.427  1.00 37.97  ? 213  GLU C CB  1 
ATOM   8718  C  CG  . GLU B  1 213 ? 34.973  16.357  66.410  1.00 41.41  ? 213  GLU C CG  1 
ATOM   8719  C  CD  . GLU B  1 213 ? 36.220  16.313  67.267  1.00 46.57  ? 213  GLU C CD  1 
ATOM   8720  O  OE1 . GLU B  1 213 ? 36.340  17.127  68.197  1.00 47.01  ? 213  GLU C OE1 1 
ATOM   8721  O  OE2 . GLU B  1 213 ? 37.088  15.452  67.013  1.00 52.18  ? 213  GLU C OE2 1 
ATOM   8722  N  N   . PRO B  1 214 ? 31.026  18.557  66.125  1.00 37.62  ? 214  PRO C N   1 
ATOM   8723  C  CA  . PRO B  1 214 ? 29.899  19.491  66.305  1.00 36.98  ? 214  PRO C CA  1 
ATOM   8724  C  C   . PRO B  1 214 ? 30.212  20.703  67.198  1.00 48.66  ? 214  PRO C C   1 
ATOM   8725  O  O   . PRO B  1 214 ? 29.634  21.781  67.007  1.00 41.46  ? 214  PRO C O   1 
ATOM   8726  C  CB  . PRO B  1 214 ? 28.811  18.614  66.946  1.00 37.55  ? 214  PRO C CB  1 
ATOM   8727  C  CG  . PRO B  1 214 ? 29.503  17.300  67.298  1.00 43.61  ? 214  PRO C CG  1 
ATOM   8728  C  CD  . PRO B  1 214 ? 30.633  17.158  66.324  1.00 32.12  ? 214  PRO C CD  1 
ATOM   8729  N  N   . LEU B  1 215 ? 31.106  20.515  68.168  1.00 50.61  ? 215  LEU C N   1 
ATOM   8730  C  CA  . LEU B  1 215 ? 31.549  21.592  69.046  1.00 49.31  ? 215  LEU C CA  1 
ATOM   8731  C  C   . LEU B  1 215 ? 32.143  22.783  68.276  1.00 53.98  ? 215  LEU C C   1 
ATOM   8732  O  O   . LEU B  1 215 ? 31.944  23.949  68.647  1.00 53.44  ? 215  LEU C O   1 
ATOM   8733  C  CB  . LEU B  1 215 ? 32.583  21.060  70.044  1.00 53.41  ? 215  LEU C CB  1 
ATOM   8734  C  CG  . LEU B  1 215 ? 32.963  21.957  71.239  1.00 60.77  ? 215  LEU C CG  1 
ATOM   8735  C  CD1 . LEU B  1 215 ? 31.724  22.367  72.031  1.00 48.03  ? 215  LEU C CD1 1 
ATOM   8736  C  CD2 . LEU B  1 215 ? 33.995  21.264  72.147  1.00 53.45  ? 215  LEU C CD2 1 
ATOM   8737  N  N   . PHE B  1 216 ? 32.875  22.489  67.207  1.00 48.65  ? 216  PHE C N   1 
ATOM   8738  C  CA  . PHE B  1 216 ? 33.579  23.527  66.473  1.00 44.95  ? 216  PHE C CA  1 
ATOM   8739  C  C   . PHE B  1 216 ? 32.683  24.315  65.528  1.00 40.64  ? 216  PHE C C   1 
ATOM   8740  O  O   . PHE B  1 216 ? 32.958  24.367  64.347  1.00 45.91  ? 216  PHE C O   1 
ATOM   8741  C  CB  . PHE B  1 216 ? 34.715  22.921  65.670  1.00 40.11  ? 216  PHE C CB  1 
ATOM   8742  C  CG  . PHE B  1 216 ? 35.768  22.274  66.499  1.00 44.71  ? 216  PHE C CG  1 
ATOM   8743  C  CD1 . PHE B  1 216 ? 35.574  21.013  67.030  1.00 52.17  ? 216  PHE C CD1 1 
ATOM   8744  C  CD2 . PHE B  1 216 ? 36.978  22.910  66.721  1.00 46.94  ? 216  PHE C CD2 1 
ATOM   8745  C  CE1 . PHE B  1 216 ? 36.564  20.398  67.793  1.00 54.65  ? 216  PHE C CE1 1 
ATOM   8746  C  CE2 . PHE B  1 216 ? 37.978  22.298  67.464  1.00 56.30  ? 216  PHE C CE2 1 
ATOM   8747  C  CZ  . PHE B  1 216 ? 37.766  21.038  68.007  1.00 58.99  ? 216  PHE C CZ  1 
ATOM   8748  N  N   . LYS B  1 217 ? 31.635  24.939  66.045  1.00 39.35  ? 217  LYS C N   1 
ATOM   8749  C  CA  . LYS B  1 217 ? 30.802  25.825  65.236  1.00 44.42  ? 217  LYS C CA  1 
ATOM   8750  C  C   . LYS B  1 217 ? 31.567  26.994  64.601  1.00 47.32  ? 217  LYS C C   1 
ATOM   8751  O  O   . LYS B  1 217 ? 32.641  27.401  65.056  1.00 41.05  ? 217  LYS C O   1 
ATOM   8752  C  CB  . LYS B  1 217 ? 29.645  26.385  66.065  1.00 46.10  ? 217  LYS C CB  1 
ATOM   8753  C  CG  . LYS B  1 217 ? 28.808  25.329  66.756  1.00 40.70  ? 217  LYS C CG  1 
ATOM   8754  C  CD  . LYS B  1 217 ? 27.409  25.844  66.961  1.00 45.25  ? 217  LYS C CD  1 
ATOM   8755  C  CE  . LYS B  1 217 ? 26.536  24.806  67.646  1.00 49.04  ? 217  LYS C CE  1 
ATOM   8756  N  NZ  . LYS B  1 217 ? 25.083  25.133  67.546  1.00 44.70  ? 217  LYS C NZ  1 
ATOM   8757  N  N   . ALA B  1 218 ? 30.981  27.523  63.535  1.00 49.07  ? 218  ALA C N   1 
ATOM   8758  C  CA  . ALA B  1 218 ? 31.615  28.533  62.713  1.00 47.30  ? 218  ALA C CA  1 
ATOM   8759  C  C   . ALA B  1 218 ? 30.580  29.150  61.805  1.00 46.65  ? 218  ALA C C   1 
ATOM   8760  O  O   . ALA B  1 218 ? 29.489  28.617  61.665  1.00 43.21  ? 218  ALA C O   1 
ATOM   8761  C  CB  . ALA B  1 218 ? 32.758  27.933  61.892  1.00 44.15  ? 218  ALA C CB  1 
ATOM   8762  N  N   . ASN B  1 219 ? 30.916  30.296  61.221  1.00 49.20  ? 219  ASN C N   1 
ATOM   8763  C  CA  . ASN B  1 219 ? 30.109  30.876  60.162  1.00 46.45  ? 219  ASN C CA  1 
ATOM   8764  C  C   . ASN B  1 219 ? 30.519  30.300  58.787  1.00 43.34  ? 219  ASN C C   1 
ATOM   8765  O  O   . ASN B  1 219 ? 31.712  30.081  58.517  1.00 42.55  ? 219  ASN C O   1 
ATOM   8766  C  CB  . ASN B  1 219 ? 30.256  32.406  60.112  1.00 48.86  ? 219  ASN C CB  1 
ATOM   8767  C  CG  . ASN B  1 219 ? 29.911  33.121  61.416  1.00 48.89  ? 219  ASN C CG  1 
ATOM   8768  O  OD1 . ASN B  1 219 ? 30.724  33.184  62.336  1.00 49.01  ? 219  ASN C OD1 1 
ATOM   8769  N  ND2 . ASN B  1 219 ? 28.711  33.703  61.473  1.00 46.69  ? 219  ASN C ND2 1 
ATOM   8770  N  N   . PHE B  1 220 ? 29.553  30.101  57.897  1.00 40.32  ? 220  PHE C N   1 
ATOM   8771  C  CA  . PHE B  1 220 ? 29.892  29.609  56.556  1.00 45.67  ? 220  PHE C CA  1 
ATOM   8772  C  C   . PHE B  1 220 ? 29.445  30.545  55.433  1.00 43.39  ? 220  PHE C C   1 
ATOM   8773  O  O   . PHE B  1 220 ? 28.256  30.862  55.291  1.00 43.33  ? 220  PHE C O   1 
ATOM   8774  C  CB  . PHE B  1 220 ? 29.302  28.205  56.325  1.00 44.94  ? 220  PHE C CB  1 
ATOM   8775  C  CG  . PHE B  1 220 ? 29.916  27.149  57.199  1.00 42.55  ? 220  PHE C CG  1 
ATOM   8776  C  CD1 . PHE B  1 220 ? 29.514  27.002  58.533  1.00 43.20  ? 220  PHE C CD1 1 
ATOM   8777  C  CD2 . PHE B  1 220 ? 30.904  26.331  56.711  1.00 38.66  ? 220  PHE C CD2 1 
ATOM   8778  C  CE1 . PHE B  1 220 ? 30.096  26.048  59.355  1.00 40.42  ? 220  PHE C CE1 1 
ATOM   8779  C  CE2 . PHE B  1 220 ? 31.480  25.370  57.508  1.00 44.43  ? 220  PHE C CE2 1 
ATOM   8780  C  CZ  . PHE B  1 220 ? 31.080  25.230  58.843  1.00 45.56  ? 220  PHE C CZ  1 
ATOM   8781  N  N   . SER B  1 221 ? 30.421  30.981  54.643  1.00 38.52  ? 221  SER C N   1 
ATOM   8782  C  CA  . SER B  1 221 ? 30.156  31.701  53.395  1.00 44.44  ? 221  SER C CA  1 
ATOM   8783  C  C   . SER B  1 221 ? 30.251  30.770  52.154  1.00 35.68  ? 221  SER C C   1 
ATOM   8784  O  O   . SER B  1 221 ? 31.339  30.309  51.798  1.00 31.42  ? 221  SER C O   1 
ATOM   8785  C  CB  . SER B  1 221 ? 31.131  32.869  53.272  1.00 40.66  ? 221  SER C CB  1 
ATOM   8786  O  OG  . SER B  1 221 ? 31.076  33.657  54.442  1.00 46.19  ? 221  SER C OG  1 
ATOM   8787  N  N   . ILE B  1 222 ? 29.112  30.487  51.527  1.00 29.74  ? 222  ILE C N   1 
ATOM   8788  C  CA  . ILE B  1 222 ? 29.057  29.518  50.431  1.00 40.90  ? 222  ILE C CA  1 
ATOM   8789  C  C   . ILE B  1 222 ? 28.891  30.135  49.025  1.00 40.38  ? 222  ILE C C   1 
ATOM   8790  O  O   . ILE B  1 222 ? 27.903  30.812  48.742  1.00 43.65  ? 222  ILE C O   1 
ATOM   8791  C  CB  . ILE B  1 222 ? 27.883  28.498  50.611  1.00 41.23  ? 222  ILE C CB  1 
ATOM   8792  C  CG1 . ILE B  1 222 ? 27.993  27.715  51.919  1.00 45.82  ? 222  ILE C CG1 1 
ATOM   8793  C  CG2 . ILE B  1 222 ? 27.835  27.506  49.445  1.00 39.12  ? 222  ILE C CG2 1 
ATOM   8794  C  CD1 . ILE B  1 222 ? 29.357  27.152  52.143  1.00 48.66  ? 222  ILE C CD1 1 
ATOM   8795  N  N   . LYS B  1 223 ? 29.837  29.851  48.138  1.00 40.55  ? 223  LYS C N   1 
ATOM   8796  C  CA  . LYS B  1 223 ? 29.652  30.110  46.700  1.00 47.61  ? 223  LYS C CA  1 
ATOM   8797  C  C   . LYS B  1 223 ? 29.597  28.812  45.863  1.00 43.79  ? 223  LYS C C   1 
ATOM   8798  O  O   . LYS B  1 223 ? 30.465  27.941  45.977  1.00 38.18  ? 223  LYS C O   1 
ATOM   8799  C  CB  . LYS B  1 223 ? 30.764  31.013  46.188  1.00 41.13  ? 223  LYS C CB  1 
ATOM   8800  C  CG  . LYS B  1 223 ? 30.940  32.231  47.063  1.00 49.26  ? 223  LYS C CG  1 
ATOM   8801  C  CD  . LYS B  1 223 ? 31.994  33.190  46.552  1.00 57.64  ? 223  LYS C CD  1 
ATOM   8802  C  CE  . LYS B  1 223 ? 32.102  34.423  47.457  1.00 61.66  ? 223  LYS C CE  1 
ATOM   8803  N  NZ  . LYS B  1 223 ? 32.987  35.506  46.906  1.00 61.39  ? 223  LYS C NZ  1 
ATOM   8804  N  N   . ILE B  1 224 ? 28.559  28.695  45.040  1.00 37.97  ? 224  ILE C N   1 
ATOM   8805  C  CA  . ILE B  1 224 ? 28.442  27.605  44.097  1.00 42.26  ? 224  ILE C CA  1 
ATOM   8806  C  C   . ILE B  1 224 ? 28.506  28.084  42.628  1.00 46.31  ? 224  ILE C C   1 
ATOM   8807  O  O   . ILE B  1 224 ? 27.764  28.980  42.231  1.00 46.47  ? 224  ILE C O   1 
ATOM   8808  C  CB  . ILE B  1 224 ? 27.120  26.826  44.289  1.00 45.32  ? 224  ILE C CB  1 
ATOM   8809  C  CG1 . ILE B  1 224 ? 26.920  26.417  45.752  1.00 34.37  ? 224  ILE C CG1 1 
ATOM   8810  C  CG2 . ILE B  1 224 ? 27.100  25.595  43.362  1.00 37.56  ? 224  ILE C CG2 1 
ATOM   8811  C  CD1 . ILE B  1 224 ? 27.819  25.291  46.186  1.00 41.17  ? 224  ILE C CD1 1 
ATOM   8812  N  N   . ARG B  1 225 ? 29.374  27.461  41.830  1.00 45.17  ? 225  ARG C N   1 
ATOM   8813  C  CA  . ARG B  1 225 ? 29.425  27.687  40.387  1.00 40.18  ? 225  ARG C CA  1 
ATOM   8814  C  C   . ARG B  1 225 ? 28.617  26.641  39.618  1.00 43.61  ? 225  ARG C C   1 
ATOM   8815  O  O   . ARG B  1 225 ? 28.751  25.439  39.835  1.00 46.34  ? 225  ARG C O   1 
ATOM   8816  C  CB  . ARG B  1 225 ? 30.871  27.692  39.901  1.00 40.63  ? 225  ARG C CB  1 
ATOM   8817  C  CG  . ARG B  1 225 ? 31.031  28.190  38.471  1.00 43.03  ? 225  ARG C CG  1 
ATOM   8818  C  CD  . ARG B  1 225 ? 32.509  28.272  38.061  1.00 44.52  ? 225  ARG C CD  1 
ATOM   8819  N  NE  . ARG B  1 225 ? 33.199  29.394  38.693  1.00 45.73  ? 225  ARG C NE  1 
ATOM   8820  C  CZ  . ARG B  1 225 ? 34.507  29.600  38.625  1.00 47.24  ? 225  ARG C CZ  1 
ATOM   8821  N  NH1 . ARG B  1 225 ? 35.267  28.755  37.954  1.00 47.57  ? 225  ARG C NH1 1 
ATOM   8822  N  NH2 . ARG B  1 225 ? 35.051  30.641  39.242  1.00 45.40  ? 225  ARG C NH2 1 
ATOM   8823  N  N   . ARG B  1 226 ? 27.778  27.090  38.703  1.00 45.37  ? 226  ARG C N   1 
ATOM   8824  C  CA  . ARG B  1 226 ? 26.882  26.171  38.023  1.00 41.49  ? 226  ARG C CA  1 
ATOM   8825  C  C   . ARG B  1 226 ? 26.600  26.587  36.580  1.00 41.26  ? 226  ARG C C   1 
ATOM   8826  O  O   . ARG B  1 226 ? 27.060  27.643  36.117  1.00 43.09  ? 226  ARG C O   1 
ATOM   8827  C  CB  . ARG B  1 226 ? 25.568  26.090  38.781  1.00 32.81  ? 226  ARG C CB  1 
ATOM   8828  C  CG  . ARG B  1 226 ? 24.975  27.469  38.946  1.00 41.05  ? 226  ARG C CG  1 
ATOM   8829  C  CD  . ARG B  1 226 ? 23.503  27.465  39.256  1.00 43.08  ? 226  ARG C CD  1 
ATOM   8830  N  NE  . ARG B  1 226 ? 23.077  28.848  39.409  1.00 52.18  ? 226  ARG C NE  1 
ATOM   8831  C  CZ  . ARG B  1 226 ? 22.549  29.565  38.428  1.00 49.65  ? 226  ARG C CZ  1 
ATOM   8832  N  NH1 . ARG B  1 226 ? 22.351  28.999  37.247  1.00 46.74  ? 226  ARG C NH1 1 
ATOM   8833  N  NH2 . ARG B  1 226 ? 22.200  30.827  38.639  1.00 50.24  ? 226  ARG C NH2 1 
ATOM   8834  N  N   . GLU B  1 227 ? 25.821  25.747  35.903  1.00 36.60  ? 227  GLU C N   1 
ATOM   8835  C  CA  . GLU B  1 227 ? 25.347  25.977  34.543  1.00 41.04  ? 227  GLU C CA  1 
ATOM   8836  C  C   . GLU B  1 227 ? 23.959  26.554  34.620  1.00 42.13  ? 227  GLU C C   1 
ATOM   8837  O  O   . GLU B  1 227 ? 23.359  26.548  35.686  1.00 47.19  ? 227  GLU C O   1 
ATOM   8838  C  CB  . GLU B  1 227 ? 25.327  24.683  33.741  1.00 32.85  ? 227  GLU C CB  1 
ATOM   8839  C  CG  . GLU B  1 227 ? 26.683  24.156  33.390  1.00 28.32  ? 227  GLU C CG  1 
ATOM   8840  C  CD  . GLU B  1 227 ? 26.616  22.736  32.892  1.00 38.47  ? 227  GLU C CD  1 
ATOM   8841  O  OE1 . GLU B  1 227 ? 25.500  22.309  32.532  1.00 42.23  ? 227  GLU C OE1 1 
ATOM   8842  O  OE2 . GLU B  1 227 ? 27.662  22.035  32.884  1.00 42.89  ? 227  GLU C OE2 1 
ATOM   8843  N  N   . SER B  1 228 ? 23.436  27.025  33.494  1.00 38.64  ? 228  SER C N   1 
ATOM   8844  C  CA  . SER B  1 228 ? 22.200  27.807  33.507  1.00 38.77  ? 228  SER C CA  1 
ATOM   8845  C  C   . SER B  1 228 ? 21.000  26.887  33.535  1.00 37.76  ? 228  SER C C   1 
ATOM   8846  O  O   . SER B  1 228 ? 19.895  27.295  33.884  1.00 44.39  ? 228  SER C O   1 
ATOM   8847  C  CB  . SER B  1 228 ? 22.134  28.740  32.291  1.00 40.40  ? 228  SER C CB  1 
ATOM   8848  O  OG  . SER B  1 228 ? 21.870  28.008  31.111  1.00 44.98  ? 228  SER C OG  1 
ATOM   8849  N  N   . ARG B  1 229 ? 21.233  25.633  33.172  1.00 33.62  ? 229  ARG C N   1 
ATOM   8850  C  CA  . ARG B  1 229 ? 20.201  24.608  33.217  1.00 38.52  ? 229  ARG C CA  1 
ATOM   8851  C  C   . ARG B  1 229 ? 19.884  24.205  34.675  1.00 43.68  ? 229  ARG C C   1 
ATOM   8852  O  O   . ARG B  1 229 ? 18.918  23.480  34.932  1.00 40.56  ? 229  ARG C O   1 
ATOM   8853  C  CB  . ARG B  1 229 ? 20.645  23.368  32.406  1.00 34.25  ? 229  ARG C CB  1 
ATOM   8854  C  CG  . ARG B  1 229 ? 21.884  22.688  33.000  1.00 41.71  ? 229  ARG C CG  1 
ATOM   8855  C  CD  . ARG B  1 229 ? 22.489  21.622  32.083  1.00 36.84  ? 229  ARG C CD  1 
ATOM   8856  N  NE  . ARG B  1 229 ? 21.802  20.345  32.197  1.00 43.66  ? 229  ARG C NE  1 
ATOM   8857  C  CZ  . ARG B  1 229 ? 22.381  19.189  32.524  1.00 39.41  ? 229  ARG C CZ  1 
ATOM   8858  N  NH1 . ARG B  1 229 ? 23.696  19.118  32.775  1.00 30.44  ? 229  ARG C NH1 1 
ATOM   8859  N  NH2 . ARG B  1 229 ? 21.629  18.099  32.592  1.00 36.28  ? 229  ARG C NH2 1 
ATOM   8860  N  N   . HIS B  1 230 ? 20.703  24.672  35.617  1.00 38.23  ? 230  HIS C N   1 
ATOM   8861  C  CA  . HIS B  1 230 ? 20.552  24.298  37.018  1.00 40.15  ? 230  HIS C CA  1 
ATOM   8862  C  C   . HIS B  1 230 ? 20.220  25.504  37.904  1.00 41.25  ? 230  HIS C C   1 
ATOM   8863  O  O   . HIS B  1 230 ? 20.457  26.645  37.506  1.00 45.65  ? 230  HIS C O   1 
ATOM   8864  C  CB  . HIS B  1 230 ? 21.842  23.633  37.555  1.00 34.36  ? 230  HIS C CB  1 
ATOM   8865  C  CG  . HIS B  1 230 ? 22.258  22.386  36.829  1.00 35.75  ? 230  HIS C CG  1 
ATOM   8866  N  ND1 . HIS B  1 230 ? 21.386  21.355  36.544  1.00 37.16  ? 230  HIS C ND1 1 
ATOM   8867  C  CD2 . HIS B  1 230 ? 23.473  21.992  36.369  1.00 31.14  ? 230  HIS C CD2 1 
ATOM   8868  C  CE1 . HIS B  1 230 ? 22.040  20.386  35.923  1.00 34.26  ? 230  HIS C CE1 1 
ATOM   8869  N  NE2 . HIS B  1 230 ? 23.307  20.744  35.813  1.00 32.02  ? 230  HIS C NE2 1 
ATOM   8870  N  N   . ILE B  1 231 ? 19.676  25.226  39.097  1.00 39.32  ? 231  ILE C N   1 
ATOM   8871  C  CA  . ILE B  1 231 ? 19.755  26.116  40.270  1.00 32.96  ? 231  ILE C CA  1 
ATOM   8872  C  C   . ILE B  1 231 ? 20.733  25.508  41.299  1.00 36.60  ? 231  ILE C C   1 
ATOM   8873  O  O   . ILE B  1 231 ? 20.940  24.286  41.344  1.00 40.61  ? 231  ILE C O   1 
ATOM   8874  C  CB  . ILE B  1 231 ? 18.382  26.325  40.981  1.00 33.34  ? 231  ILE C CB  1 
ATOM   8875  C  CG1 . ILE B  1 231 ? 17.837  24.979  41.496  1.00 38.28  ? 231  ILE C CG1 1 
ATOM   8876  C  CG2 . ILE B  1 231 ? 17.367  27.009  40.086  1.00 23.19  ? 231  ILE C CG2 1 
ATOM   8877  C  CD1 . ILE B  1 231 ? 16.539  25.043  42.258  1.00 32.59  ? 231  ILE C CD1 1 
ATOM   8878  N  N   . ALA B  1 232 ? 21.352  26.362  42.097  1.00 28.58  ? 232  ALA C N   1 
ATOM   8879  C  CA  . ALA B  1 232 ? 22.076  25.949  43.267  1.00 36.00  ? 232  ALA C CA  1 
ATOM   8880  C  C   . ALA B  1 232 ? 21.278  26.404  44.492  1.00 39.59  ? 232  ALA C C   1 
ATOM   8881  O  O   . ALA B  1 232 ? 20.660  27.458  44.453  1.00 39.69  ? 232  ALA C O   1 
ATOM   8882  C  CB  . ALA B  1 232 ? 23.481  26.540  43.270  1.00 38.75  ? 232  ALA C CB  1 
ATOM   8883  N  N   . LEU B  1 233 ? 21.259  25.588  45.549  1.00 41.34  ? 233  LEU C N   1 
ATOM   8884  C  CA  . LEU B  1 233 ? 20.620  25.934  46.827  1.00 35.02  ? 233  LEU C CA  1 
ATOM   8885  C  C   . LEU B  1 233 ? 21.575  25.646  47.964  1.00 40.77  ? 233  LEU C C   1 
ATOM   8886  O  O   . LEU B  1 233 ? 22.372  24.701  47.878  1.00 42.85  ? 233  LEU C O   1 
ATOM   8887  C  CB  . LEU B  1 233 ? 19.337  25.145  47.053  1.00 35.10  ? 233  LEU C CB  1 
ATOM   8888  C  CG  . LEU B  1 233 ? 18.142  25.306  46.123  1.00 40.73  ? 233  LEU C CG  1 
ATOM   8889  C  CD1 . LEU B  1 233 ? 17.181  24.155  46.287  1.00 29.95  ? 233  LEU C CD1 1 
ATOM   8890  C  CD2 . LEU B  1 233 ? 17.426  26.627  46.378  1.00 44.67  ? 233  LEU C CD2 1 
ATOM   8891  N  N   . SER B  1 234 ? 21.498  26.443  49.028  1.00 39.39  ? 234  SER C N   1 
ATOM   8892  C  CA  . SER B  1 234 ? 22.303  26.206  50.228  1.00 35.48  ? 234  SER C CA  1 
ATOM   8893  C  C   . SER B  1 234 ? 21.502  26.497  51.513  1.00 37.48  ? 234  SER C C   1 
ATOM   8894  O  O   . SER B  1 234 ? 20.270  26.554  51.506  1.00 38.93  ? 234  SER C O   1 
ATOM   8895  C  CB  . SER B  1 234 ? 23.580  27.052  50.175  1.00 34.59  ? 234  SER C CB  1 
ATOM   8896  O  OG  . SER B  1 234 ? 24.573  26.595  51.083  1.00 35.17  ? 234  SER C OG  1 
ATOM   8897  N  N   . ASN B  1 235 ? 22.205  26.644  52.626  1.00 42.75  ? 235  ASN C N   1 
ATOM   8898  C  CA  . ASN B  1 235 ? 21.562  26.923  53.906  1.00 40.69  ? 235  ASN C CA  1 
ATOM   8899  C  C   . ASN B  1 235 ? 20.886  28.283  53.912  1.00 47.12  ? 235  ASN C C   1 
ATOM   8900  O  O   . ASN B  1 235 ? 19.677  28.383  54.088  1.00 47.12  ? 235  ASN C O   1 
ATOM   8901  C  CB  . ASN B  1 235 ? 22.581  26.884  55.026  1.00 40.94  ? 235  ASN C CB  1 
ATOM   8902  C  CG  . ASN B  1 235 ? 23.272  25.553  55.139  1.00 42.66  ? 235  ASN C CG  1 
ATOM   8903  O  OD1 . ASN B  1 235 ? 24.200  25.253  54.382  1.00 38.64  ? 235  ASN C OD1 1 
ATOM   8904  N  ND2 . ASN B  1 235 ? 22.847  24.749  56.113  1.00 39.71  ? 235  ASN C ND2 1 
ATOM   8905  N  N   . MET B  1 236 ? 21.706  29.317  53.724  1.00 44.99  ? 236  MET C N   1 
ATOM   8906  C  CA  . MET B  1 236 ? 21.276  30.710  53.649  1.00 46.27  ? 236  MET C CA  1 
ATOM   8907  C  C   . MET B  1 236 ? 20.676  31.076  52.298  1.00 45.39  ? 236  MET C C   1 
ATOM   8908  O  O   . MET B  1 236 ? 20.899  30.369  51.316  1.00 52.46  ? 236  MET C O   1 
ATOM   8909  C  CB  . MET B  1 236 ? 22.470  31.619  53.931  1.00 45.68  ? 236  MET C CB  1 
ATOM   8910  C  CG  . MET B  1 236 ? 23.083  31.393  55.312  1.00 53.20  ? 236  MET C CG  1 
ATOM   8911  S  SD  . MET B  1 236 ? 21.877  31.615  56.630  1.00 51.08  ? 236  MET C SD  1 
ATOM   8912  C  CE  . MET B  1 236 ? 21.651  33.385  56.473  1.00 53.29  ? 236  MET C CE  1 
ATOM   8913  N  N   . PRO B  1 237 ? 19.924  32.188  52.238  1.00 45.79  ? 237  PRO C N   1 
ATOM   8914  C  CA  . PRO B  1 237 ? 19.434  32.759  50.965  1.00 48.74  ? 237  PRO C CA  1 
ATOM   8915  C  C   . PRO B  1 237 ? 20.545  33.176  49.976  1.00 42.65  ? 237  PRO C C   1 
ATOM   8916  O  O   . PRO B  1 237 ? 21.709  33.401  50.334  1.00 39.29  ? 237  PRO C O   1 
ATOM   8917  C  CB  . PRO B  1 237 ? 18.640  33.999  51.410  1.00 52.58  ? 237  PRO C CB  1 
ATOM   8918  C  CG  . PRO B  1 237 ? 18.267  33.740  52.839  1.00 52.10  ? 237  PRO C CG  1 
ATOM   8919  C  CD  . PRO B  1 237 ? 19.332  32.848  53.418  1.00 51.02  ? 237  PRO C CD  1 
ATOM   8920  N  N   . LYS B  1 238 ? 20.173  33.272  48.708  1.00 40.84  ? 238  LYS C N   1 
ATOM   8921  C  CA  . LYS B  1 238 ? 21.118  33.702  47.695  1.00 46.17  ? 238  LYS C CA  1 
ATOM   8922  C  C   . LYS B  1 238 ? 21.184  35.213  47.692  1.00 47.81  ? 238  LYS C C   1 
ATOM   8923  O  O   . LYS B  1 238 ? 20.163  35.863  47.508  1.00 50.28  ? 238  LYS C O   1 
ATOM   8924  C  CB  . LYS B  1 238 ? 20.704  33.189  46.315  1.00 52.12  ? 238  LYS C CB  1 
ATOM   8925  C  CG  . LYS B  1 238 ? 21.793  33.295  45.244  1.00 48.34  ? 238  LYS C CG  1 
ATOM   8926  C  CD  . LYS B  1 238 ? 21.285  32.849  43.861  1.00 48.94  ? 238  LYS C CD  1 
ATOM   8927  C  CE  . LYS B  1 238 ? 20.265  33.811  43.262  1.00 57.61  ? 238  LYS C CE  1 
ATOM   8928  N  NZ  . LYS B  1 238 ? 20.045  33.583  41.792  1.00 61.55  ? 238  LYS C NZ  1 
ATOM   8929  N  N   . VAL B  1 239 ? 22.373  35.763  47.919  1.00 50.84  ? 239  VAL C N   1 
ATOM   8930  C  CA  . VAL B  1 239 ? 22.609  37.201  47.773  1.00 55.79  ? 239  VAL C CA  1 
ATOM   8931  C  C   . VAL B  1 239 ? 22.494  37.609  46.301  1.00 61.43  ? 239  VAL C C   1 
ATOM   8932  O  O   . VAL B  1 239 ? 21.556  38.302  45.905  1.00 63.85  ? 239  VAL C O   1 
ATOM   8933  C  CB  . VAL B  1 239 ? 24.007  37.610  48.304  1.00 55.44  ? 239  VAL C CB  1 
ATOM   8934  C  CG1 . VAL B  1 239 ? 24.299  39.039  47.958  1.00 56.57  ? 239  VAL C CG1 1 
ATOM   8935  C  CG2 . VAL B  1 239 ? 24.098  37.413  49.801  1.00 53.03  ? 239  VAL C CG2 1 
ATOM   8936  N  N   . LYS B  1 240 ? 23.444  37.149  45.491  1.00 58.26  ? 240  LYS C N   1 
ATOM   8937  C  CA  . LYS B  1 240 ? 23.452  37.470  44.076  1.00 59.77  ? 240  LYS C CA  1 
ATOM   8938  C  C   . LYS B  1 240 ? 23.908  36.320  43.189  1.00 57.42  ? 240  LYS C C   1 
ATOM   8939  O  O   . LYS B  1 240 ? 24.286  35.246  43.655  1.00 55.70  ? 240  LYS C O   1 
ATOM   8940  C  CB  . LYS B  1 240 ? 24.356  38.676  43.816  1.00 57.21  ? 240  LYS C CB  1 
ATOM   8941  C  CG  . LYS B  1 240 ? 25.783  38.487  44.299  1.00 56.96  ? 240  LYS C CG  1 
ATOM   8942  C  CD  . LYS B  1 240 ? 26.739  39.325  43.470  1.00 52.50  ? 240  LYS C CD  1 
ATOM   8943  C  CE  . LYS B  1 240 ? 27.931  39.853  44.292  1.00 60.55  ? 240  LYS C CE  1 
ATOM   8944  N  NZ  . LYS B  1 240 ? 28.795  40.811  43.492  1.00 53.65  ? 240  LYS C NZ  1 
ATOM   8945  N  N   . THR B  1 241 ? 23.879  36.590  41.892  1.00 62.49  ? 241  THR C N   1 
ATOM   8946  C  CA  . THR B  1 241 ? 24.390  35.699  40.866  1.00 54.97  ? 241  THR C CA  1 
ATOM   8947  C  C   . THR B  1 241 ? 25.238  36.492  39.892  1.00 55.80  ? 241  THR C C   1 
ATOM   8948  O  O   . THR B  1 241 ? 24.721  37.372  39.210  1.00 54.57  ? 241  THR C O   1 
ATOM   8949  C  CB  . THR B  1 241 ? 23.270  35.044  40.080  1.00 55.66  ? 241  THR C CB  1 
ATOM   8950  O  OG1 . THR B  1 241 ? 22.339  34.429  40.981  1.00 53.79  ? 241  THR C OG1 1 
ATOM   8951  C  CG2 . THR B  1 241 ? 23.847  34.019  39.079  1.00 57.55  ? 241  THR C CG2 1 
ATOM   8952  N  N   . ILE B  1 242 ? 26.530  36.204  39.831  1.00 52.69  ? 242  ILE C N   1 
ATOM   8953  C  CA  . ILE B  1 242 ? 27.357  36.837  38.830  1.00 51.47  ? 242  ILE C CA  1 
ATOM   8954  C  C   . ILE B  1 242 ? 27.438  35.943  37.607  1.00 52.82  ? 242  ILE C C   1 
ATOM   8955  O  O   . ILE B  1 242 ? 27.453  34.721  37.725  1.00 52.28  ? 242  ILE C O   1 
ATOM   8956  C  CB  . ILE B  1 242 ? 28.754  37.142  39.361  1.00 57.89  ? 242  ILE C CB  1 
ATOM   8957  C  CG1 . ILE B  1 242 ? 29.364  35.897  39.990  1.00 59.02  ? 242  ILE C CG1 1 
ATOM   8958  C  CG2 . ILE B  1 242 ? 28.694  38.257  40.399  1.00 58.66  ? 242  ILE C CG2 1 
ATOM   8959  C  CD1 . ILE B  1 242 ? 30.756  36.126  40.549  1.00 63.45  ? 242  ILE C CD1 1 
ATOM   8960  N  N   . GLU B  1 243 ? 27.449  36.563  36.430  1.00 56.48  ? 243  GLU C N   1 
ATOM   8961  C  CA  . GLU B  1 243 ? 27.625  35.848  35.174  1.00 51.91  ? 243  GLU C CA  1 
ATOM   8962  C  C   . GLU B  1 243 ? 29.098  35.816  34.819  1.00 52.71  ? 243  GLU C C   1 
ATOM   8963  O  O   . GLU B  1 243 ? 29.810  36.794  34.995  1.00 54.17  ? 243  GLU C O   1 
ATOM   8964  C  CB  . GLU B  1 243 ? 26.820  36.489  34.050  1.00 56.20  ? 243  GLU C CB  1 
ATOM   8965  C  CG  . GLU B  1 243 ? 25.311  36.350  34.200  1.00 64.82  ? 243  GLU C CG  1 
ATOM   8966  C  CD  . GLU B  1 243 ? 24.520  36.975  33.045  1.00 80.89  ? 243  GLU C CD  1 
ATOM   8967  O  OE1 . GLU B  1 243 ? 25.025  37.920  32.386  1.00 76.76  ? 243  GLU C OE1 1 
ATOM   8968  O  OE2 . GLU B  1 243 ? 23.380  36.519  32.804  1.00 83.05  ? 243  GLU C OE2 1 
ATOM   8969  N  N   . LEU B  1 244 ? 29.561  34.677  34.335  1.00 55.09  ? 244  LEU C N   1 
ATOM   8970  C  CA  . LEU B  1 244 ? 30.981  34.496  34.102  1.00 56.56  ? 244  LEU C CA  1 
ATOM   8971  C  C   . LEU B  1 244 ? 31.266  34.476  32.610  1.00 64.39  ? 244  LEU C C   1 
ATOM   8972  O  O   . LEU B  1 244 ? 30.384  34.154  31.807  1.00 65.42  ? 244  LEU C O   1 
ATOM   8973  C  CB  . LEU B  1 244 ? 31.472  33.207  34.761  1.00 57.92  ? 244  LEU C CB  1 
ATOM   8974  C  CG  . LEU B  1 244 ? 31.175  33.001  36.251  1.00 54.52  ? 244  LEU C CG  1 
ATOM   8975  C  CD1 . LEU B  1 244 ? 31.654  31.609  36.677  1.00 54.70  ? 244  LEU C CD1 1 
ATOM   8976  C  CD2 . LEU B  1 244 ? 31.815  34.083  37.124  1.00 49.05  ? 244  LEU C CD2 1 
ATOM   8977  N  N   . GLU B  1 245 ? 32.502  34.814  32.254  1.00 67.51  ? 245  GLU C N   1 
ATOM   8978  C  CA  . GLU B  1 245 ? 32.883  35.020  30.863  1.00 73.21  ? 245  GLU C CA  1 
ATOM   8979  C  C   . GLU B  1 245 ? 32.440  33.897  29.931  1.00 71.56  ? 245  GLU C C   1 
ATOM   8980  O  O   . GLU B  1 245 ? 31.959  34.157  28.828  1.00 83.62  ? 245  GLU C O   1 
ATOM   8981  C  CB  . GLU B  1 245 ? 34.402  35.210  30.741  1.00 74.69  ? 245  GLU C CB  1 
ATOM   8982  C  CG  . GLU B  1 245 ? 34.869  35.507  29.308  1.00 80.68  ? 245  GLU C CG  1 
ATOM   8983  C  CD  . GLU B  1 245 ? 35.767  36.734  29.211  1.00 84.39  ? 245  GLU C CD  1 
ATOM   8984  O  OE1 . GLU B  1 245 ? 36.980  36.604  29.485  1.00 84.21  ? 245  GLU C OE1 1 
ATOM   8985  O  OE2 . GLU B  1 245 ? 35.259  37.825  28.859  1.00 89.32  ? 245  GLU C OE2 1 
ATOM   8986  N  N   . GLY B  1 246 ? 32.575  32.656  30.373  1.00 54.78  ? 246  GLY C N   1 
ATOM   8987  C  CA  . GLY B  1 246 ? 32.381  31.547  29.461  1.00 60.19  ? 246  GLY C CA  1 
ATOM   8988  C  C   . GLY B  1 246 ? 30.968  31.010  29.423  1.00 58.07  ? 246  GLY C C   1 
ATOM   8989  O  O   . GLY B  1 246 ? 30.704  30.017  28.747  1.00 55.96  ? 246  GLY C O   1 
ATOM   8990  N  N   . GLY B  1 247 ? 30.063  31.642  30.161  1.00 53.93  ? 247  GLY C N   1 
ATOM   8991  C  CA  . GLY B  1 247 ? 28.686  31.182  30.201  1.00 53.80  ? 247  GLY C CA  1 
ATOM   8992  C  C   . GLY B  1 247 ? 28.200  30.529  31.494  1.00 51.55  ? 247  GLY C C   1 
ATOM   8993  O  O   . GLY B  1 247 ? 26.999  30.296  31.654  1.00 47.42  ? 247  GLY C O   1 
ATOM   8994  N  N   . LEU B  1 248 ? 29.112  30.214  32.408  1.00 41.37  ? 248  LEU C N   1 
ATOM   8995  C  CA  . LEU B  1 248 ? 28.706  29.645  33.691  1.00 48.90  ? 248  LEU C CA  1 
ATOM   8996  C  C   . LEU B  1 248 ? 28.165  30.742  34.619  1.00 54.36  ? 248  LEU C C   1 
ATOM   8997  O  O   . LEU B  1 248 ? 28.340  31.946  34.355  1.00 50.12  ? 248  LEU C O   1 
ATOM   8998  C  CB  . LEU B  1 248 ? 29.873  28.919  34.360  1.00 40.08  ? 248  LEU C CB  1 
ATOM   8999  C  CG  . LEU B  1 248 ? 30.412  27.739  33.549  1.00 41.06  ? 248  LEU C CG  1 
ATOM   9000  C  CD1 . LEU B  1 248 ? 31.703  27.183  34.160  1.00 33.99  ? 248  LEU C CD1 1 
ATOM   9001  C  CD2 . LEU B  1 248 ? 29.346  26.664  33.412  1.00 40.21  ? 248  LEU C CD2 1 
ATOM   9002  N  N   . LEU B  1 249 ? 27.506  30.320  35.697  1.00 45.64  ? 249  LEU C N   1 
ATOM   9003  C  CA  . LEU B  1 249 ? 26.989  31.255  36.690  1.00 43.75  ? 249  LEU C CA  1 
ATOM   9004  C  C   . LEU B  1 249 ? 27.629  30.974  38.031  1.00 48.90  ? 249  LEU C C   1 
ATOM   9005  O  O   . LEU B  1 249 ? 28.147  29.880  38.271  1.00 53.31  ? 249  LEU C O   1 
ATOM   9006  C  CB  . LEU B  1 249 ? 25.468  31.159  36.798  1.00 40.81  ? 249  LEU C CB  1 
ATOM   9007  C  CG  . LEU B  1 249 ? 24.790  31.579  35.498  1.00 43.96  ? 249  LEU C CG  1 
ATOM   9008  C  CD1 . LEU B  1 249 ? 23.281  31.456  35.534  1.00 48.28  ? 249  LEU C CD1 1 
ATOM   9009  C  CD2 . LEU B  1 249 ? 25.178  33.004  35.216  1.00 50.98  ? 249  LEU C CD2 1 
ATOM   9010  N  N   . GLU B  1 250 ? 27.596  31.957  38.908  1.00 46.00  ? 250  GLU C N   1 
ATOM   9011  C  CA  . GLU B  1 250 ? 28.096  31.753  40.252  1.00 49.49  ? 250  GLU C CA  1 
ATOM   9012  C  C   . GLU B  1 250 ? 27.095  32.335  41.245  1.00 54.53  ? 250  GLU C C   1 
ATOM   9013  O  O   . GLU B  1 250 ? 26.893  33.545  41.286  1.00 54.21  ? 250  GLU C O   1 
ATOM   9014  C  CB  . GLU B  1 250 ? 29.468  32.393  40.403  1.00 46.15  ? 250  GLU C CB  1 
ATOM   9015  C  CG  . GLU B  1 250 ? 30.339  31.733  41.422  1.00 50.58  ? 250  GLU C CG  1 
ATOM   9016  C  CD  . GLU B  1 250 ? 31.800  32.113  41.272  1.00 62.13  ? 250  GLU C CD  1 
ATOM   9017  O  OE1 . GLU B  1 250 ? 32.214  33.119  41.898  1.00 72.50  ? 250  GLU C OE1 1 
ATOM   9018  O  OE2 . GLU B  1 250 ? 32.532  31.399  40.538  1.00 54.96  ? 250  GLU C OE2 1 
ATOM   9019  N  N   . ASP B  1 251 ? 26.434  31.474  42.017  1.00 53.28  ? 251  ASP C N   1 
ATOM   9020  C  CA  . ASP B  1 251 ? 25.494  31.956  43.028  1.00 49.60  ? 251  ASP C CA  1 
ATOM   9021  C  C   . ASP B  1 251 ? 26.255  32.213  44.323  1.00 50.20  ? 251  ASP C C   1 
ATOM   9022  O  O   . ASP B  1 251 ? 27.046  31.376  44.768  1.00 47.35  ? 251  ASP C O   1 
ATOM   9023  C  CB  . ASP B  1 251 ? 24.347  30.966  43.269  1.00 44.79  ? 251  ASP C CB  1 
ATOM   9024  C  CG  . ASP B  1 251 ? 23.377  30.872  42.089  1.00 52.83  ? 251  ASP C CG  1 
ATOM   9025  O  OD1 . ASP B  1 251 ? 23.463  31.715  41.166  1.00 50.54  ? 251  ASP C OD1 1 
ATOM   9026  O  OD2 . ASP B  1 251 ? 22.506  29.962  42.100  1.00 49.54  ? 251  ASP C OD2 1 
ATOM   9027  N  N   . HIS B  1 252 ? 26.039  33.391  44.905  1.00 54.32  ? 252  HIS C N   1 
ATOM   9028  C  CA  . HIS B  1 252 ? 26.661  33.750  46.178  1.00 52.23  ? 252  HIS C CA  1 
ATOM   9029  C  C   . HIS B  1 252 ? 25.615  33.683  47.272  1.00 47.67  ? 252  HIS C C   1 
ATOM   9030  O  O   . HIS B  1 252 ? 24.480  34.135  47.097  1.00 50.20  ? 252  HIS C O   1 
ATOM   9031  C  CB  . HIS B  1 252 ? 27.290  35.144  46.114  1.00 58.39  ? 252  HIS C CB  1 
ATOM   9032  C  CG  . HIS B  1 252 ? 28.450  35.240  45.172  1.00 58.13  ? 252  HIS C CG  1 
ATOM   9033  N  ND1 . HIS B  1 252 ? 29.706  35.641  45.575  1.00 56.80  ? 252  HIS C ND1 1 
ATOM   9034  C  CD2 . HIS B  1 252 ? 28.546  34.971  43.847  1.00 56.89  ? 252  HIS C CD2 1 
ATOM   9035  C  CE1 . HIS B  1 252 ? 30.527  35.613  44.538  1.00 66.17  ? 252  HIS C CE1 1 
ATOM   9036  N  NE2 . HIS B  1 252 ? 29.849  35.208  43.478  1.00 61.73  ? 252  HIS C NE2 1 
ATOM   9037  N  N   . PHE B  1 253 ? 25.992  33.086  48.390  1.00 45.45  ? 253  PHE C N   1 
ATOM   9038  C  CA  . PHE B  1 253 ? 25.051  32.871  49.476  1.00 46.53  ? 253  PHE C CA  1 
ATOM   9039  C  C   . PHE B  1 253 ? 25.404  33.692  50.706  1.00 45.80  ? 253  PHE C C   1 
ATOM   9040  O  O   . PHE B  1 253 ? 26.584  33.824  51.069  1.00 39.34  ? 253  PHE C O   1 
ATOM   9041  C  CB  . PHE B  1 253 ? 24.988  31.385  49.822  1.00 39.30  ? 253  PHE C CB  1 
ATOM   9042  C  CG  . PHE B  1 253 ? 24.355  30.565  48.752  1.00 39.33  ? 253  PHE C CG  1 
ATOM   9043  C  CD1 . PHE B  1 253 ? 22.975  30.506  48.637  1.00 40.37  ? 253  PHE C CD1 1 
ATOM   9044  C  CD2 . PHE B  1 253 ? 25.127  29.890  47.834  1.00 37.92  ? 253  PHE C CD2 1 
ATOM   9045  C  CE1 . PHE B  1 253 ? 22.377  29.780  47.629  1.00 36.95  ? 253  PHE C CE1 1 
ATOM   9046  C  CE2 . PHE B  1 253 ? 24.533  29.158  46.824  1.00 33.85  ? 253  PHE C CE2 1 
ATOM   9047  C  CZ  . PHE B  1 253 ? 23.157  29.104  46.723  1.00 35.00  ? 253  PHE C CZ  1 
ATOM   9048  N  N   . GLU B  1 254 ? 24.367  34.262  51.319  1.00 43.87  ? 254  GLU C N   1 
ATOM   9049  C  CA  . GLU B  1 254 ? 24.469  34.942  52.618  1.00 50.59  ? 254  GLU C CA  1 
ATOM   9050  C  C   . GLU B  1 254 ? 25.270  34.114  53.632  1.00 48.27  ? 254  GLU C C   1 
ATOM   9051  O  O   . GLU B  1 254 ? 25.192  32.884  53.648  1.00 47.34  ? 254  GLU C O   1 
ATOM   9052  C  CB  . GLU B  1 254 ? 23.059  35.235  53.157  1.00 51.19  ? 254  GLU C CB  1 
ATOM   9053  C  CG  . GLU B  1 254 ? 22.984  36.091  54.405  1.00 59.65  ? 254  GLU C CG  1 
ATOM   9054  C  CD  . GLU B  1 254 ? 21.546  36.567  54.721  1.00 72.81  ? 254  GLU C CD  1 
ATOM   9055  O  OE1 . GLU B  1 254 ? 20.661  36.429  53.840  1.00 60.42  ? 254  GLU C OE1 1 
ATOM   9056  O  OE2 . GLU B  1 254 ? 21.307  37.084  55.849  1.00 79.05  ? 254  GLU C OE2 1 
ATOM   9057  N  N   . THR B  1 255 ? 26.061  34.777  54.463  1.00 46.66  ? 255  THR C N   1 
ATOM   9058  C  CA  . THR B  1 255 ? 26.824  34.050  55.462  1.00 48.47  ? 255  THR C CA  1 
ATOM   9059  C  C   . THR B  1 255 ? 25.876  33.402  56.497  1.00 54.76  ? 255  THR C C   1 
ATOM   9060  O  O   . THR B  1 255 ? 24.764  33.893  56.742  1.00 50.67  ? 255  THR C O   1 
ATOM   9061  C  CB  . THR B  1 255 ? 27.846  34.973  56.128  1.00 43.61  ? 255  THR C CB  1 
ATOM   9062  O  OG1 . THR B  1 255 ? 28.879  35.254  55.188  1.00 43.53  ? 255  THR C OG1 1 
ATOM   9063  C  CG2 . THR B  1 255 ? 28.486  34.331  57.346  1.00 48.03  ? 255  THR C CG2 1 
ATOM   9064  N  N   . THR B  1 256 ? 26.285  32.260  57.047  1.00 50.55  ? 256  THR C N   1 
ATOM   9065  C  CA  . THR B  1 256 ? 25.478  31.606  58.069  1.00 55.27  ? 256  THR C CA  1 
ATOM   9066  C  C   . THR B  1 256 ? 25.733  32.144  59.467  1.00 47.35  ? 256  THR C C   1 
ATOM   9067  O  O   . THR B  1 256 ? 26.754  32.780  59.753  1.00 40.69  ? 256  THR C O   1 
ATOM   9068  C  CB  . THR B  1 256 ? 25.733  30.086  58.140  1.00 37.51  ? 256  THR C CB  1 
ATOM   9069  O  OG1 . THR B  1 256 ? 27.120  29.864  58.425  1.00 39.60  ? 256  THR C OG1 1 
ATOM   9070  C  CG2 . THR B  1 256 ? 25.378  29.411  56.839  1.00 48.13  ? 256  THR C CG2 1 
ATOM   9071  N  N   . VAL B  1 257 ? 24.787  31.819  60.335  1.00 51.33  ? 257  VAL C N   1 
ATOM   9072  C  CA  . VAL B  1 257 ? 24.992  31.760  61.775  1.00 45.35  ? 257  VAL C CA  1 
ATOM   9073  C  C   . VAL B  1 257 ? 26.147  30.845  62.219  1.00 47.10  ? 257  VAL C C   1 
ATOM   9074  O  O   . VAL B  1 257 ? 26.726  30.098  61.413  1.00 49.70  ? 257  VAL C O   1 
ATOM   9075  C  CB  . VAL B  1 257 ? 23.733  31.263  62.406  1.00 44.42  ? 257  VAL C CB  1 
ATOM   9076  C  CG1 . VAL B  1 257 ? 23.548  31.936  63.685  1.00 63.84  ? 257  VAL C CG1 1 
ATOM   9077  C  CG2 . VAL B  1 257 ? 22.569  31.606  61.493  1.00 58.45  ? 257  VAL C CG2 1 
ATOM   9078  N  N   . LYS B  1 258 ? 26.489  30.885  63.502  1.00 47.46  ? 258  LYS C N   1 
ATOM   9079  C  CA  . LYS B  1 258 ? 27.385  29.859  64.041  1.00 51.93  ? 258  LYS C CA  1 
ATOM   9080  C  C   . LYS B  1 258 ? 26.666  28.506  64.006  1.00 44.14  ? 258  LYS C C   1 
ATOM   9081  O  O   . LYS B  1 258 ? 25.544  28.370  64.491  1.00 47.39  ? 258  LYS C O   1 
ATOM   9082  C  CB  . LYS B  1 258 ? 27.829  30.192  65.467  1.00 55.46  ? 258  LYS C CB  1 
ATOM   9083  C  CG  . LYS B  1 258 ? 28.716  31.421  65.584  1.00 54.71  ? 258  LYS C CG  1 
ATOM   9084  C  CD  . LYS B  1 258 ? 30.116  31.181  65.064  1.00 49.62  ? 258  LYS C CD  1 
ATOM   9085  C  CE  . LYS B  1 258 ? 30.958  32.428  65.274  1.00 45.00  ? 258  LYS C CE  1 
ATOM   9086  N  NZ  . LYS B  1 258 ? 32.159  32.487  64.403  1.00 54.45  ? 258  LYS C NZ  1 
ATOM   9087  N  N   . MET B  1 259 ? 27.288  27.510  63.395  1.00 48.78  ? 259  MET C N   1 
ATOM   9088  C  CA  . MET B  1 259 ? 26.642  26.203  63.288  1.00 49.67  ? 259  MET C CA  1 
ATOM   9089  C  C   . MET B  1 259 ? 27.689  25.130  63.155  1.00 43.11  ? 259  MET C C   1 
ATOM   9090  O  O   . MET B  1 259 ? 28.861  25.427  62.974  1.00 44.01  ? 259  MET C O   1 
ATOM   9091  C  CB  . MET B  1 259 ? 25.671  26.140  62.102  1.00 40.75  ? 259  MET C CB  1 
ATOM   9092  C  CG  . MET B  1 259 ? 26.270  26.639  60.799  1.00 42.33  ? 259  MET C CG  1 
ATOM   9093  S  SD  . MET B  1 259 ? 25.359  26.083  59.348  1.00 47.61  ? 259  MET C SD  1 
ATOM   9094  C  CE  . MET B  1 259 ? 23.746  26.788  59.572  1.00 51.13  ? 259  MET C CE  1 
ATOM   9095  N  N   . SER B  1 260 ? 27.256  23.881  63.254  1.00 38.36  ? 260  SER C N   1 
ATOM   9096  C  CA  . SER B  1 260 ? 28.167  22.758  63.159  1.00 35.30  ? 260  SER C CA  1 
ATOM   9097  C  C   . SER B  1 260 ? 28.343  22.383  61.681  1.00 35.95  ? 260  SER C C   1 
ATOM   9098  O  O   . SER B  1 260 ? 27.447  22.593  60.861  1.00 35.21  ? 260  SER C O   1 
ATOM   9099  C  CB  . SER B  1 260 ? 27.631  21.574  63.977  1.00 39.16  ? 260  SER C CB  1 
ATOM   9100  O  OG  . SER B  1 260 ? 27.452  21.897  65.352  1.00 41.81  ? 260  SER C OG  1 
ATOM   9101  N  N   . THR B  1 261 ? 29.496  21.829  61.349  1.00 30.65  ? 261  THR C N   1 
ATOM   9102  C  CA  . THR B  1 261 ? 29.783  21.418  59.993  1.00 29.29  ? 261  THR C CA  1 
ATOM   9103  C  C   . THR B  1 261 ? 28.745  20.453  59.433  1.00 36.16  ? 261  THR C C   1 
ATOM   9104  O  O   . THR B  1 261 ? 28.518  20.447  58.233  1.00 38.75  ? 261  THR C O   1 
ATOM   9105  C  CB  . THR B  1 261 ? 31.175  20.740  59.882  1.00 37.62  ? 261  THR C CB  1 
ATOM   9106  O  OG1 . THR B  1 261 ? 31.347  19.777  60.940  1.00 39.92  ? 261  THR C OG1 1 
ATOM   9107  C  CG2 . THR B  1 261 ? 32.269  21.752  59.961  1.00 36.12  ? 261  THR C CG2 1 
ATOM   9108  N  N   . TYR B  1 262 ? 28.107  19.636  60.262  1.00 32.32  ? 262  TYR C N   1 
ATOM   9109  C  CA  . TYR B  1 262 ? 27.309  18.558  59.686  1.00 33.01  ? 262  TYR C CA  1 
ATOM   9110  C  C   . TYR B  1 262 ? 26.000  19.101  59.130  1.00 36.25  ? 262  TYR C C   1 
ATOM   9111  O  O   . TYR B  1 262 ? 25.268  18.380  58.441  1.00 34.01  ? 262  TYR C O   1 
ATOM   9112  C  CB  . TYR B  1 262 ? 27.045  17.428  60.703  1.00 38.99  ? 262  TYR C CB  1 
ATOM   9113  C  CG  . TYR B  1 262 ? 26.116  17.783  61.842  1.00 34.82  ? 262  TYR C CG  1 
ATOM   9114  C  CD1 . TYR B  1 262 ? 26.605  18.376  62.994  1.00 37.34  ? 262  TYR C CD1 1 
ATOM   9115  C  CD2 . TYR B  1 262 ? 24.756  17.526  61.765  1.00 33.16  ? 262  TYR C CD2 1 
ATOM   9116  C  CE1 . TYR B  1 262 ? 25.758  18.710  64.041  1.00 41.52  ? 262  TYR C CE1 1 
ATOM   9117  C  CE2 . TYR B  1 262 ? 23.899  17.853  62.803  1.00 32.81  ? 262  TYR C CE2 1 
ATOM   9118  C  CZ  . TYR B  1 262 ? 24.407  18.447  63.941  1.00 36.17  ? 262  TYR C CZ  1 
ATOM   9119  O  OH  . TYR B  1 262 ? 23.581  18.786  64.991  1.00 37.58  ? 262  TYR C OH  1 
ATOM   9120  N  N   . LEU B  1 263 ? 25.726  20.381  59.369  1.00 29.93  ? 263  LEU C N   1 
ATOM   9121  C  CA  . LEU B  1 263 ? 24.470  20.947  58.889  1.00 31.06  ? 263  LEU C CA  1 
ATOM   9122  C  C   . LEU B  1 263 ? 24.647  21.799  57.654  1.00 33.70  ? 263  LEU C C   1 
ATOM   9123  O  O   . LEU B  1 263 ? 23.655  22.312  57.096  1.00 31.86  ? 263  LEU C O   1 
ATOM   9124  C  CB  . LEU B  1 263 ? 23.799  21.769  59.979  1.00 38.37  ? 263  LEU C CB  1 
ATOM   9125  C  CG  . LEU B  1 263 ? 23.336  20.911  61.164  1.00 38.00  ? 263  LEU C CG  1 
ATOM   9126  C  CD1 . LEU B  1 263 ? 23.273  21.777  62.392  1.00 41.94  ? 263  LEU C CD1 1 
ATOM   9127  C  CD2 . LEU B  1 263 ? 21.990  20.227  60.891  1.00 31.74  ? 263  LEU C CD2 1 
ATOM   9128  N  N   . VAL B  1 264 ? 25.901  21.947  57.223  1.00 29.09  ? 264  VAL C N   1 
ATOM   9129  C  CA  . VAL B  1 264 ? 26.160  22.632  55.971  1.00 40.49  ? 264  VAL C CA  1 
ATOM   9130  C  C   . VAL B  1 264 ? 25.514  21.838  54.835  1.00 38.48  ? 264  VAL C C   1 
ATOM   9131  O  O   . VAL B  1 264 ? 25.517  20.604  54.838  1.00 35.08  ? 264  VAL C O   1 
ATOM   9132  C  CB  . VAL B  1 264 ? 27.661  22.820  55.711  1.00 39.15  ? 264  VAL C CB  1 
ATOM   9133  C  CG1 . VAL B  1 264 ? 27.849  23.619  54.455  1.00 28.30  ? 264  VAL C CG1 1 
ATOM   9134  C  CG2 . VAL B  1 264 ? 28.307  23.547  56.899  1.00 38.70  ? 264  VAL C CG2 1 
ATOM   9135  N  N   . ALA B  1 265 ? 24.928  22.538  53.879  1.00 35.93  ? 265  ALA C N   1 
ATOM   9136  C  CA  . ALA B  1 265 ? 24.291  21.843  52.778  1.00 32.74  ? 265  ALA C CA  1 
ATOM   9137  C  C   . ALA B  1 265 ? 24.394  22.641  51.477  1.00 34.72  ? 265  ALA C C   1 
ATOM   9138  O  O   . ALA B  1 265 ? 24.484  23.859  51.505  1.00 38.03  ? 265  ALA C O   1 
ATOM   9139  C  CB  . ALA B  1 265 ? 22.853  21.555  53.125  1.00 29.21  ? 265  ALA C CB  1 
ATOM   9140  N  N   . TYR B  1 266 ? 24.420  21.958  50.339  1.00 34.33  ? 266  TYR C N   1 
ATOM   9141  C  CA  . TYR B  1 266 ? 24.220  22.635  49.051  1.00 36.17  ? 266  TYR C CA  1 
ATOM   9142  C  C   . TYR B  1 266 ? 23.788  21.653  48.003  1.00 38.54  ? 266  TYR C C   1 
ATOM   9143  O  O   . TYR B  1 266 ? 24.288  20.538  47.940  1.00 37.56  ? 266  TYR C O   1 
ATOM   9144  C  CB  . TYR B  1 266 ? 25.464  23.368  48.572  1.00 29.60  ? 266  TYR C CB  1 
ATOM   9145  C  CG  . TYR B  1 266 ? 26.753  22.683  48.908  1.00 35.95  ? 266  TYR C CG  1 
ATOM   9146  C  CD1 . TYR B  1 266 ? 27.335  21.744  48.043  1.00 32.36  ? 266  TYR C CD1 1 
ATOM   9147  C  CD2 . TYR B  1 266 ? 27.402  22.975  50.099  1.00 38.56  ? 266  TYR C CD2 1 
ATOM   9148  C  CE1 . TYR B  1 266 ? 28.558  21.135  48.372  1.00 33.07  ? 266  TYR C CE1 1 
ATOM   9149  C  CE2 . TYR B  1 266 ? 28.594  22.376  50.441  1.00 32.74  ? 266  TYR C CE2 1 
ATOM   9150  C  CZ  . TYR B  1 266 ? 29.168  21.464  49.597  1.00 32.54  ? 266  TYR C CZ  1 
ATOM   9151  O  OH  . TYR B  1 266 ? 30.355  20.912  50.009  1.00 32.36  ? 266  TYR C OH  1 
ATOM   9152  N  N   . ILE B  1 267 ? 22.847  22.081  47.179  1.00 37.51  ? 267  ILE C N   1 
ATOM   9153  C  CA  . ILE B  1 267 ? 22.261  21.210  46.181  1.00 35.80  ? 267  ILE C CA  1 
ATOM   9154  C  C   . ILE B  1 267 ? 22.291  21.880  44.799  1.00 40.20  ? 267  ILE C C   1 
ATOM   9155  O  O   . ILE B  1 267 ? 21.949  23.056  44.656  1.00 37.52  ? 267  ILE C O   1 
ATOM   9156  C  CB  . ILE B  1 267 ? 20.828  20.842  46.586  1.00 32.96  ? 267  ILE C CB  1 
ATOM   9157  C  CG1 . ILE B  1 267 ? 20.865  20.049  47.884  1.00 30.99  ? 267  ILE C CG1 1 
ATOM   9158  C  CG2 . ILE B  1 267 ? 20.103  20.064  45.493  1.00 31.69  ? 267  ILE C CG2 1 
ATOM   9159  C  CD1 . ILE B  1 267 ? 19.493  19.629  48.371  1.00 36.98  ? 267  ILE C CD1 1 
ATOM   9160  N  N   . VAL B  1 268 ? 22.751  21.144  43.793  1.00 37.65  ? 268  VAL C N   1 
ATOM   9161  C  CA  . VAL B  1 268 ? 22.631  21.601  42.423  1.00 30.12  ? 268  VAL C CA  1 
ATOM   9162  C  C   . VAL B  1 268 ? 21.642  20.709  41.698  1.00 33.38  ? 268  VAL C C   1 
ATOM   9163  O  O   . VAL B  1 268 ? 21.859  19.503  41.578  1.00 39.05  ? 268  VAL C O   1 
ATOM   9164  C  CB  . VAL B  1 268 ? 23.960  21.596  41.701  1.00 35.05  ? 268  VAL C CB  1 
ATOM   9165  C  CG1 . VAL B  1 268 ? 23.741  21.995  40.265  1.00 39.27  ? 268  VAL C CG1 1 
ATOM   9166  C  CG2 . VAL B  1 268 ? 24.927  22.557  42.352  1.00 34.28  ? 268  VAL C CG2 1 
ATOM   9167  N  N   . CYS B  1 269 ? 20.538  21.302  41.252  1.00 33.37  ? 269  CYS C N   1 
ATOM   9168  C  CA  . CYS B  1 269 ? 19.468  20.560  40.597  1.00 38.28  ? 269  CYS C CA  1 
ATOM   9169  C  C   . CYS B  1 269 ? 18.670  21.474  39.670  1.00 39.17  ? 269  CYS C C   1 
ATOM   9170  O  O   . CYS B  1 269 ? 18.987  22.652  39.540  1.00 37.50  ? 269  CYS C O   1 
ATOM   9171  C  CB  . CYS B  1 269 ? 18.534  19.927  41.633  1.00 35.07  ? 269  CYS C CB  1 
ATOM   9172  S  SG  . CYS B  1 269 ? 17.583  21.139  42.584  1.00 48.45  ? 269  CYS C SG  1 
ATOM   9173  N  N   . ASP B  1 270 ? 17.620  20.940  39.056  1.00 37.92  ? 270  ASP C N   1 
ATOM   9174  C  CA  . ASP B  1 270 ? 16.774  21.741  38.184  1.00 41.19  ? 270  ASP C CA  1 
ATOM   9175  C  C   . ASP B  1 270 ? 15.334  21.769  38.660  1.00 45.22  ? 270  ASP C C   1 
ATOM   9176  O  O   . ASP B  1 270 ? 14.407  21.816  37.866  1.00 54.37  ? 270  ASP C O   1 
ATOM   9177  C  CB  . ASP B  1 270 ? 16.834  21.211  36.750  1.00 44.98  ? 270  ASP C CB  1 
ATOM   9178  C  CG  . ASP B  1 270 ? 16.420  19.743  36.636  1.00 52.90  ? 270  ASP C CG  1 
ATOM   9179  O  OD1 . ASP B  1 270 ? 16.106  19.103  37.671  1.00 52.36  ? 270  ASP C OD1 1 
ATOM   9180  O  OD2 . ASP B  1 270 ? 16.417  19.223  35.494  1.00 55.68  ? 270  ASP C OD2 1 
ATOM   9181  N  N   . PHE B  1 271 ? 15.149  21.745  39.965  1.00 47.53  ? 271  PHE C N   1 
ATOM   9182  C  CA  . PHE B  1 271 ? 13.822  21.597  40.548  1.00 48.19  ? 271  PHE C CA  1 
ATOM   9183  C  C   . PHE B  1 271 ? 12.969  22.861  40.486  1.00 46.81  ? 271  PHE C C   1 
ATOM   9184  O  O   . PHE B  1 271 ? 13.493  23.970  40.471  1.00 56.88  ? 271  PHE C O   1 
ATOM   9185  C  CB  . PHE B  1 271 ? 13.965  21.167  42.008  1.00 48.57  ? 271  PHE C CB  1 
ATOM   9186  C  CG  . PHE B  1 271 ? 14.250  19.719  42.193  1.00 47.13  ? 271  PHE C CG  1 
ATOM   9187  C  CD1 . PHE B  1 271 ? 14.539  18.909  41.114  1.00 46.04  ? 271  PHE C CD1 1 
ATOM   9188  C  CD2 . PHE B  1 271 ? 14.199  19.159  43.460  1.00 46.14  ? 271  PHE C CD2 1 
ATOM   9189  C  CE1 . PHE B  1 271 ? 14.794  17.564  41.294  1.00 44.56  ? 271  PHE C CE1 1 
ATOM   9190  C  CE2 . PHE B  1 271 ? 14.442  17.818  43.646  1.00 46.32  ? 271  PHE C CE2 1 
ATOM   9191  C  CZ  . PHE B  1 271 ? 14.738  17.015  42.557  1.00 45.95  ? 271  PHE C CZ  1 
ATOM   9192  N  N   . HIS B  1 272 ? 11.652  22.700  40.511  1.00 53.35  ? 272  HIS C N   1 
ATOM   9193  C  CA  . HIS B  1 272 ? 10.755  23.847  40.696  1.00 58.46  ? 272  HIS C CA  1 
ATOM   9194  C  C   . HIS B  1 272 ? 10.339  24.033  42.164  1.00 59.55  ? 272  HIS C C   1 
ATOM   9195  O  O   . HIS B  1 272 ? 10.850  23.358  43.057  1.00 56.32  ? 272  HIS C O   1 
ATOM   9196  C  CB  . HIS B  1 272 ? 9.517   23.691  39.816  1.00 63.46  ? 272  HIS C CB  1 
ATOM   9197  C  CG  . HIS B  1 272 ? 9.812   23.766  38.350  1.00 67.77  ? 272  HIS C CG  1 
ATOM   9198  N  ND1 . HIS B  1 272 ? 9.008   23.178  37.398  1.00 72.18  ? 272  HIS C ND1 1 
ATOM   9199  C  CD2 . HIS B  1 272 ? 10.821  24.365  37.675  1.00 58.67  ? 272  HIS C CD2 1 
ATOM   9200  C  CE1 . HIS B  1 272 ? 9.512   23.409  36.199  1.00 70.99  ? 272  HIS C CE1 1 
ATOM   9201  N  NE2 . HIS B  1 272 ? 10.610  24.128  36.340  1.00 70.67  ? 272  HIS C NE2 1 
ATOM   9202  N  N   . SER B  1 273 ? 9.414   24.951  42.417  1.00 58.27  ? 273  SER C N   1 
ATOM   9203  C  CA  . SER B  1 273 ? 8.990   25.194  43.782  1.00 54.85  ? 273  SER C CA  1 
ATOM   9204  C  C   . SER B  1 273 ? 7.677   25.965  43.921  1.00 66.23  ? 273  SER C C   1 
ATOM   9205  O  O   . SER B  1 273 ? 7.266   26.709  43.030  1.00 71.65  ? 273  SER C O   1 
ATOM   9206  C  CB  . SER B  1 273 ? 10.090  25.932  44.548  1.00 57.80  ? 273  SER C CB  1 
ATOM   9207  O  OG  . SER B  1 273 ? 10.735  26.900  43.743  1.00 62.02  ? 273  SER C OG  1 
ATOM   9208  N  N   . LEU B  1 274 ? 7.023   25.741  45.056  1.00 65.01  ? 274  LEU C N   1 
ATOM   9209  C  CA  . LEU B  1 274 ? 5.859   26.491  45.481  1.00 59.86  ? 274  LEU C CA  1 
ATOM   9210  C  C   . LEU B  1 274 ? 6.228   27.066  46.820  1.00 59.63  ? 274  LEU C C   1 
ATOM   9211  O  O   . LEU B  1 274 ? 6.881   26.392  47.612  1.00 61.02  ? 274  LEU C O   1 
ATOM   9212  C  CB  . LEU B  1 274 ? 4.624   25.608  45.574  1.00 63.73  ? 274  LEU C CB  1 
ATOM   9213  C  CG  . LEU B  1 274 ? 4.225   24.960  44.246  1.00 63.40  ? 274  LEU C CG  1 
ATOM   9214  C  CD1 . LEU B  1 274 ? 2.992   24.089  44.424  1.00 65.77  ? 274  LEU C CD1 1 
ATOM   9215  C  CD2 . LEU B  1 274 ? 3.991   25.999  43.166  1.00 63.74  ? 274  LEU C CD2 1 
ATOM   9216  N  N   . SER B  1 275 ? 5.835   28.308  47.071  1.00 59.08  ? 275  SER C N   1 
ATOM   9217  C  CA  . SER B  1 275 ? 6.394   29.049  48.198  1.00 61.34  ? 275  SER C CA  1 
ATOM   9218  C  C   . SER B  1 275 ? 5.350   29.827  49.001  1.00 64.27  ? 275  SER C C   1 
ATOM   9219  O  O   . SER B  1 275 ? 4.267   30.163  48.505  1.00 61.78  ? 275  SER C O   1 
ATOM   9220  C  CB  . SER B  1 275 ? 7.475   30.009  47.695  1.00 62.63  ? 275  SER C CB  1 
ATOM   9221  O  OG  . SER B  1 275 ? 8.141   29.469  46.563  1.00 65.27  ? 275  SER C OG  1 
ATOM   9222  N  N   . GLY B  1 276 ? 5.696   30.121  50.248  1.00 61.38  ? 276  GLY C N   1 
ATOM   9223  C  CA  . GLY B  1 276 ? 4.774   30.764  51.154  1.00 54.02  ? 276  GLY C CA  1 
ATOM   9224  C  C   . GLY B  1 276 ? 5.508   31.512  52.247  1.00 63.25  ? 276  GLY C C   1 
ATOM   9225  O  O   . GLY B  1 276 ? 6.745   31.494  52.300  1.00 63.57  ? 276  GLY C O   1 
ATOM   9226  N  N   . PHE B  1 277 ? 4.742   32.164  53.123  1.00 63.99  ? 277  PHE C N   1 
ATOM   9227  C  CA  . PHE B  1 277 ? 5.312   32.982  54.182  1.00 60.03  ? 277  PHE C CA  1 
ATOM   9228  C  C   . PHE B  1 277 ? 4.696   32.709  55.539  1.00 59.81  ? 277  PHE C C   1 
ATOM   9229  O  O   . PHE B  1 277 ? 3.505   32.423  55.660  1.00 63.70  ? 277  PHE C O   1 
ATOM   9230  C  CB  . PHE B  1 277 ? 5.149   34.467  53.854  1.00 56.68  ? 277  PHE C CB  1 
ATOM   9231  C  CG  . PHE B  1 277 ? 6.188   34.987  52.932  1.00 56.86  ? 277  PHE C CG  1 
ATOM   9232  C  CD1 . PHE B  1 277 ? 7.382   35.485  53.436  1.00 55.14  ? 277  PHE C CD1 1 
ATOM   9233  C  CD2 . PHE B  1 277 ? 5.985   34.970  51.549  1.00 54.60  ? 277  PHE C CD2 1 
ATOM   9234  C  CE1 . PHE B  1 277 ? 8.367   35.961  52.569  1.00 60.30  ? 277  PHE C CE1 1 
ATOM   9235  C  CE2 . PHE B  1 277 ? 6.960   35.449  50.680  1.00 46.90  ? 277  PHE C CE2 1 
ATOM   9236  C  CZ  . PHE B  1 277 ? 8.156   35.939  51.187  1.00 44.29  ? 277  PHE C CZ  1 
ATOM   9237  N  N   . THR B  1 278 ? 5.524   32.802  56.566  1.00 56.25  ? 278  THR C N   1 
ATOM   9238  C  CA  . THR B  1 278 ? 5.009   32.814  57.917  1.00 62.54  ? 278  THR C CA  1 
ATOM   9239  C  C   . THR B  1 278 ? 4.862   34.275  58.361  1.00 66.81  ? 278  THR C C   1 
ATOM   9240  O  O   . THR B  1 278 ? 5.387   35.205  57.724  1.00 59.49  ? 278  THR C O   1 
ATOM   9241  C  CB  . THR B  1 278 ? 5.921   32.033  58.897  1.00 60.08  ? 278  THR C CB  1 
ATOM   9242  O  OG1 . THR B  1 278 ? 7.153   32.738  59.085  1.00 62.01  ? 278  THR C OG1 1 
ATOM   9243  C  CG2 . THR B  1 278 ? 6.226   30.658  58.358  1.00 60.48  ? 278  THR C CG2 1 
ATOM   9244  N  N   . SER B  1 279 ? 4.127   34.469  59.447  1.00 64.97  ? 279  SER C N   1 
ATOM   9245  C  CA  . SER B  1 279 ? 3.905   35.788  60.002  1.00 64.94  ? 279  SER C CA  1 
ATOM   9246  C  C   . SER B  1 279 ? 5.203   36.439  60.463  1.00 64.48  ? 279  SER C C   1 
ATOM   9247  O  O   . SER B  1 279 ? 5.278   37.659  60.572  1.00 71.36  ? 279  SER C O   1 
ATOM   9248  C  CB  . SER B  1 279 ? 2.927   35.702  61.168  1.00 77.41  ? 279  SER C CB  1 
ATOM   9249  O  OG  . SER B  1 279 ? 3.369   34.744  62.113  1.00 79.19  ? 279  SER C OG  1 
ATOM   9250  N  N   . SER B  1 280 ? 6.222   35.632  60.738  1.00 59.07  ? 280  SER C N   1 
ATOM   9251  C  CA  . SER B  1 280 ? 7.498   36.166  61.210  1.00 63.48  ? 280  SER C CA  1 
ATOM   9252  C  C   . SER B  1 280 ? 8.359   36.638  60.044  1.00 65.07  ? 280  SER C C   1 
ATOM   9253  O  O   . SER B  1 280 ? 9.455   37.177  60.236  1.00 64.69  ? 280  SER C O   1 
ATOM   9254  C  CB  . SER B  1 280 ? 8.254   35.120  62.027  1.00 66.78  ? 280  SER C CB  1 
ATOM   9255  O  OG  . SER B  1 280 ? 8.385   33.910  61.299  1.00 63.17  ? 280  SER C OG  1 
ATOM   9256  N  N   . GLY B  1 281 ? 7.859   36.426  58.833  1.00 61.05  ? 281  GLY C N   1 
ATOM   9257  C  CA  . GLY B  1 281 ? 8.566   36.856  57.649  1.00 64.14  ? 281  GLY C CA  1 
ATOM   9258  C  C   . GLY B  1 281 ? 9.649   35.888  57.222  1.00 67.82  ? 281  GLY C C   1 
ATOM   9259  O  O   . GLY B  1 281 ? 10.707  36.318  56.750  1.00 69.52  ? 281  GLY C O   1 
ATOM   9260  N  N   . VAL B  1 282 ? 9.391   34.589  57.405  1.00 67.76  ? 282  VAL C N   1 
ATOM   9261  C  CA  . VAL B  1 282 ? 10.237  33.534  56.846  1.00 56.46  ? 282  VAL C CA  1 
ATOM   9262  C  C   . VAL B  1 282 ? 9.574   33.005  55.589  1.00 55.94  ? 282  VAL C C   1 
ATOM   9263  O  O   . VAL B  1 282 ? 8.407   32.599  55.620  1.00 52.16  ? 282  VAL C O   1 
ATOM   9264  C  CB  . VAL B  1 282 ? 10.482  32.350  57.834  1.00 61.02  ? 282  VAL C CB  1 
ATOM   9265  C  CG1 . VAL B  1 282 ? 11.398  31.292  57.195  1.00 49.41  ? 282  VAL C CG1 1 
ATOM   9266  C  CG2 . VAL B  1 282 ? 11.091  32.845  59.131  1.00 59.64  ? 282  VAL C CG2 1 
ATOM   9267  N  N   . LYS B  1 283 ? 10.318  33.036  54.482  1.00 53.75  ? 283  LYS C N   1 
ATOM   9268  C  CA  . LYS B  1 283 ? 9.859   32.472  53.225  1.00 49.28  ? 283  LYS C CA  1 
ATOM   9269  C  C   . LYS B  1 283 ? 10.107  30.949  53.184  1.00 51.39  ? 283  LYS C C   1 
ATOM   9270  O  O   . LYS B  1 283 ? 11.246  30.484  53.332  1.00 42.94  ? 283  LYS C O   1 
ATOM   9271  C  CB  . LYS B  1 283 ? 10.564  33.163  52.071  1.00 51.00  ? 283  LYS C CB  1 
ATOM   9272  C  CG  . LYS B  1 283 ? 10.020  32.844  50.690  1.00 47.87  ? 283  LYS C CG  1 
ATOM   9273  C  CD  . LYS B  1 283 ? 11.057  33.231  49.644  1.00 40.29  ? 283  LYS C CD  1 
ATOM   9274  C  CE  . LYS B  1 283 ? 10.433  33.552  48.292  1.00 44.97  ? 283  LYS C CE  1 
ATOM   9275  N  NZ  . LYS B  1 283 ? 9.583   32.474  47.726  1.00 53.37  ? 283  LYS C NZ  1 
ATOM   9276  N  N   . VAL B  1 284 ? 9.036   30.188  52.975  1.00 49.23  ? 284  VAL C N   1 
ATOM   9277  C  CA  . VAL B  1 284 ? 9.091   28.733  53.043  1.00 53.66  ? 284  VAL C CA  1 
ATOM   9278  C  C   . VAL B  1 284 ? 8.716   28.081  51.726  1.00 55.63  ? 284  VAL C C   1 
ATOM   9279  O  O   . VAL B  1 284 ? 7.589   28.219  51.262  1.00 58.37  ? 284  VAL C O   1 
ATOM   9280  C  CB  . VAL B  1 284 ? 8.164   28.187  54.142  1.00 53.04  ? 284  VAL C CB  1 
ATOM   9281  C  CG1 . VAL B  1 284 ? 7.992   26.694  54.001  1.00 55.73  ? 284  VAL C CG1 1 
ATOM   9282  C  CG2 . VAL B  1 284 ? 8.715   28.544  55.512  1.00 54.67  ? 284  VAL C CG2 1 
ATOM   9283  N  N   . SER B  1 285 ? 9.663   27.338  51.154  1.00 55.78  ? 285  SER C N   1 
ATOM   9284  C  CA  . SER B  1 285 ? 9.541   26.826  49.792  1.00 48.75  ? 285  SER C CA  1 
ATOM   9285  C  C   . SER B  1 285 ? 9.708   25.312  49.700  1.00 48.77  ? 285  SER C C   1 
ATOM   9286  O  O   . SER B  1 285 ? 10.614  24.732  50.305  1.00 51.98  ? 285  SER C O   1 
ATOM   9287  C  CB  . SER B  1 285 ? 10.574  27.524  48.917  1.00 53.00  ? 285  SER C CB  1 
ATOM   9288  O  OG  . SER B  1 285 ? 11.008  28.731  49.545  1.00 58.36  ? 285  SER C OG  1 
ATOM   9289  N  N   . ILE B  1 286 ? 8.830   24.668  48.940  1.00 49.81  ? 286  ILE C N   1 
ATOM   9290  C  CA  . ILE B  1 286 ? 8.923   23.222  48.743  1.00 45.87  ? 286  ILE C CA  1 
ATOM   9291  C  C   . ILE B  1 286 ? 9.393   22.856  47.321  1.00 56.26  ? 286  ILE C C   1 
ATOM   9292  O  O   . ILE B  1 286 ? 8.647   22.984  46.338  1.00 53.87  ? 286  ILE C O   1 
ATOM   9293  C  CB  . ILE B  1 286 ? 7.586   22.518  49.011  1.00 45.28  ? 286  ILE C CB  1 
ATOM   9294  C  CG1 . ILE B  1 286 ? 6.963   23.013  50.316  1.00 52.09  ? 286  ILE C CG1 1 
ATOM   9295  C  CG2 . ILE B  1 286 ? 7.794   21.030  49.061  1.00 46.18  ? 286  ILE C CG2 1 
ATOM   9296  C  CD1 . ILE B  1 286 ? 7.926   23.051  51.505  1.00 54.32  ? 286  ILE C CD1 1 
ATOM   9297  N  N   . TYR B  1 287 ? 10.639  22.392  47.238  1.00 51.62  ? 287  TYR C N   1 
ATOM   9298  C  CA  . TYR B  1 287 ? 11.270  22.003  45.987  1.00 44.49  ? 287  TYR C CA  1 
ATOM   9299  C  C   . TYR B  1 287 ? 11.090  20.526  45.657  1.00 47.40  ? 287  TYR C C   1 
ATOM   9300  O  O   . TYR B  1 287 ? 11.128  19.659  46.533  1.00 41.59  ? 287  TYR C O   1 
ATOM   9301  C  CB  . TYR B  1 287 ? 12.755  22.327  46.038  1.00 43.73  ? 287  TYR C CB  1 
ATOM   9302  C  CG  . TYR B  1 287 ? 13.078  23.806  45.980  1.00 47.82  ? 287  TYR C CG  1 
ATOM   9303  C  CD1 . TYR B  1 287 ? 13.028  24.592  47.121  1.00 39.78  ? 287  TYR C CD1 1 
ATOM   9304  C  CD2 . TYR B  1 287 ? 13.455  24.411  44.775  1.00 49.26  ? 287  TYR C CD2 1 
ATOM   9305  C  CE1 . TYR B  1 287 ? 13.342  25.944  47.082  1.00 46.11  ? 287  TYR C CE1 1 
ATOM   9306  C  CE2 . TYR B  1 287 ? 13.773  25.768  44.717  1.00 45.29  ? 287  TYR C CE2 1 
ATOM   9307  C  CZ  . TYR B  1 287 ? 13.716  26.525  45.870  1.00 52.36  ? 287  TYR C CZ  1 
ATOM   9308  O  OH  . TYR B  1 287 ? 14.029  27.862  45.821  1.00 51.22  ? 287  TYR C OH  1 
ATOM   9309  N  N   . ALA B  1 288 ? 10.924  20.246  44.371  1.00 45.74  ? 288  ALA C N   1 
ATOM   9310  C  CA  . ALA B  1 288 ? 10.753  18.879  43.907  1.00 44.16  ? 288  ALA C CA  1 
ATOM   9311  C  C   . ALA B  1 288 ? 11.027  18.730  42.398  1.00 48.56  ? 288  ALA C C   1 
ATOM   9312  O  O   . ALA B  1 288 ? 11.177  19.724  41.684  1.00 50.66  ? 288  ALA C O   1 
ATOM   9313  C  CB  . ALA B  1 288 ? 9.350   18.402  44.243  1.00 38.37  ? 288  ALA C CB  1 
ATOM   9314  N  N   . SER B  1 289 ? 11.112  17.485  41.928  1.00 49.12  ? 289  SER C N   1 
ATOM   9315  C  CA  . SER B  1 289 ? 10.973  17.189  40.500  1.00 49.90  ? 289  SER C CA  1 
ATOM   9316  C  C   . SER B  1 289 ? 9.911   18.087  39.878  1.00 57.42  ? 289  SER C C   1 
ATOM   9317  O  O   . SER B  1 289 ? 8.847   18.297  40.472  1.00 57.54  ? 289  SER C O   1 
ATOM   9318  C  CB  . SER B  1 289 ? 10.572  15.728  40.262  1.00 48.69  ? 289  SER C CB  1 
ATOM   9319  O  OG  . SER B  1 289 ? 11.575  14.812  40.652  1.00 58.29  ? 289  SER C OG  1 
ATOM   9320  N  N   . PRO B  1 290 ? 10.189  18.619  38.678  1.00 64.66  ? 290  PRO C N   1 
ATOM   9321  C  CA  . PRO B  1 290 ? 9.230   19.523  38.032  1.00 64.82  ? 290  PRO C CA  1 
ATOM   9322  C  C   . PRO B  1 290 ? 7.929   18.809  37.697  1.00 57.15  ? 290  PRO C C   1 
ATOM   9323  O  O   . PRO B  1 290 ? 6.881   19.434  37.686  1.00 59.34  ? 290  PRO C O   1 
ATOM   9324  C  CB  . PRO B  1 290 ? 9.967   19.975  36.767  1.00 68.22  ? 290  PRO C CB  1 
ATOM   9325  C  CG  . PRO B  1 290 ? 11.425  19.735  37.071  1.00 63.89  ? 290  PRO C CG  1 
ATOM   9326  C  CD  . PRO B  1 290 ? 11.424  18.479  37.889  1.00 60.78  ? 290  PRO C CD  1 
ATOM   9327  N  N   . ASP B  1 291 ? 7.995   17.506  37.467  1.00 60.23  ? 291  ASP C N   1 
ATOM   9328  C  CA  . ASP B  1 291 ? 6.796   16.743  37.158  1.00 61.48  ? 291  ASP C CA  1 
ATOM   9329  C  C   . ASP B  1 291 ? 6.092   16.302  38.425  1.00 62.85  ? 291  ASP C C   1 
ATOM   9330  O  O   . ASP B  1 291 ? 5.138   15.529  38.366  1.00 67.53  ? 291  ASP C O   1 
ATOM   9331  C  CB  . ASP B  1 291 ? 7.137   15.533  36.284  1.00 60.20  ? 291  ASP C CB  1 
ATOM   9332  C  CG  . ASP B  1 291 ? 7.708   15.945  34.931  1.00 69.52  ? 291  ASP C CG  1 
ATOM   9333  O  OD1 . ASP B  1 291 ? 7.592   17.146  34.617  1.00 64.74  ? 291  ASP C OD1 1 
ATOM   9334  O  OD2 . ASP B  1 291 ? 8.269   15.097  34.189  1.00 61.93  ? 291  ASP C OD2 1 
ATOM   9335  N  N   . LYS B  1 292 ? 6.567   16.785  39.570  1.00 58.99  ? 292  LYS C N   1 
ATOM   9336  C  CA  . LYS B  1 292 ? 5.963   16.425  40.852  1.00 60.87  ? 292  LYS C CA  1 
ATOM   9337  C  C   . LYS B  1 292 ? 5.571   17.654  41.676  1.00 61.81  ? 292  LYS C C   1 
ATOM   9338  O  O   . LYS B  1 292 ? 5.267   17.545  42.864  1.00 63.13  ? 292  LYS C O   1 
ATOM   9339  C  CB  . LYS B  1 292 ? 6.912   15.528  41.657  1.00 55.73  ? 292  LYS C CB  1 
ATOM   9340  C  CG  . LYS B  1 292 ? 7.063   14.129  41.075  1.00 55.17  ? 292  LYS C CG  1 
ATOM   9341  C  CD  . LYS B  1 292 ? 7.939   13.231  41.930  1.00 46.43  ? 292  LYS C CD  1 
ATOM   9342  C  CE  . LYS B  1 292 ? 7.906   11.802  41.427  1.00 41.42  ? 292  LYS C CE  1 
ATOM   9343  N  NZ  . LYS B  1 292 ? 8.772   10.902  42.218  1.00 50.70  ? 292  LYS C NZ  1 
ATOM   9344  N  N   . ARG B  1 293 ? 5.565   18.819  41.037  1.00 63.50  ? 293  ARG C N   1 
ATOM   9345  C  CA  . ARG B  1 293 ? 5.244   20.069  41.717  1.00 64.88  ? 293  ARG C CA  1 
ATOM   9346  C  C   . ARG B  1 293 ? 3.861   20.036  42.366  1.00 59.85  ? 293  ARG C C   1 
ATOM   9347  O  O   . ARG B  1 293 ? 3.655   20.617  43.424  1.00 54.94  ? 293  ARG C O   1 
ATOM   9348  C  CB  . ARG B  1 293 ? 5.339   21.244  40.735  1.00 70.05  ? 293  ARG C CB  1 
ATOM   9349  C  CG  . ARG B  1 293 ? 5.081   22.613  41.363  1.00 73.53  ? 293  ARG C CG  1 
ATOM   9350  C  CD  . ARG B  1 293 ? 5.567   23.733  40.467  1.00 78.27  ? 293  ARG C CD  1 
ATOM   9351  N  NE  . ARG B  1 293 ? 5.096   23.576  39.090  1.00 92.26  ? 293  ARG C NE  1 
ATOM   9352  C  CZ  . ARG B  1 293 ? 4.026   24.188  38.593  1.00 96.94  ? 293  ARG C CZ  1 
ATOM   9353  N  NH1 . ARG B  1 293 ? 3.316   25.004  39.365  1.00 99.58  ? 293  ARG C NH1 1 
ATOM   9354  N  NH2 . ARG B  1 293 ? 3.669   23.990  37.328  1.00 90.23  ? 293  ARG C NH2 1 
ATOM   9355  N  N   . ASN B  1 294 ? 2.921   19.345  41.728  1.00 63.90  ? 294  ASN C N   1 
ATOM   9356  C  CA  . ASN B  1 294 ? 1.572   19.205  42.266  1.00 70.39  ? 294  ASN C CA  1 
ATOM   9357  C  C   . ASN B  1 294 ? 1.549   18.547  43.638  1.00 67.69  ? 294  ASN C C   1 
ATOM   9358  O  O   . ASN B  1 294 ? 0.688   18.848  44.467  1.00 65.96  ? 294  ASN C O   1 
ATOM   9359  C  CB  . ASN B  1 294 ? 0.696   18.403  41.302  1.00 75.31  ? 294  ASN C CB  1 
ATOM   9360  C  CG  . ASN B  1 294 ? 0.001   19.284  40.287  1.00 94.13  ? 294  ASN C CG  1 
ATOM   9361  O  OD1 . ASN B  1 294 ? 0.233   20.494  40.245  1.00 90.96  ? 294  ASN C OD1 1 
ATOM   9362  N  ND2 . ASN B  1 294 ? -0.857  18.690  39.461  1.00 106.84 ? 294  ASN C ND2 1 
ATOM   9363  N  N   . GLN B  1 295 ? 2.505   17.655  43.876  1.00 59.47  ? 295  GLN C N   1 
ATOM   9364  C  CA  . GLN B  1 295 ? 2.520   16.879  45.105  1.00 59.50  ? 295  GLN C CA  1 
ATOM   9365  C  C   . GLN B  1 295 ? 3.081   17.637  46.303  1.00 61.25  ? 295  GLN C C   1 
ATOM   9366  O  O   . GLN B  1 295 ? 3.177   17.067  47.392  1.00 57.88  ? 295  GLN C O   1 
ATOM   9367  C  CB  . GLN B  1 295 ? 3.332   15.610  44.914  1.00 57.96  ? 295  GLN C CB  1 
ATOM   9368  C  CG  . GLN B  1 295 ? 2.841   14.718  43.810  1.00 58.64  ? 295  GLN C CG  1 
ATOM   9369  C  CD  . GLN B  1 295 ? 3.679   13.474  43.699  1.00 56.15  ? 295  GLN C CD  1 
ATOM   9370  O  OE1 . GLN B  1 295 ? 4.445   13.154  44.610  1.00 60.93  ? 295  GLN C OE1 1 
ATOM   9371  N  NE2 . GLN B  1 295 ? 3.559   12.771  42.578  1.00 57.33  ? 295  GLN C NE2 1 
ATOM   9372  N  N   . THR B  1 296 ? 3.442   18.907  46.119  1.00 52.08  ? 296  THR C N   1 
ATOM   9373  C  CA  . THR B  1 296 ? 4.155   19.633  47.161  1.00 50.94  ? 296  THR C CA  1 
ATOM   9374  C  C   . THR B  1 296 ? 3.250   20.505  48.022  1.00 56.91  ? 296  THR C C   1 
ATOM   9375  O  O   . THR B  1 296 ? 3.736   21.276  48.853  1.00 55.32  ? 296  THR C O   1 
ATOM   9376  C  CB  . THR B  1 296 ? 5.257   20.523  46.563  1.00 56.18  ? 296  THR C CB  1 
ATOM   9377  O  OG1 . THR B  1 296 ? 4.672   21.475  45.665  1.00 56.11  ? 296  THR C OG1 1 
ATOM   9378  C  CG2 . THR B  1 296 ? 6.279   19.672  45.810  1.00 53.28  ? 296  THR C CG2 1 
ATOM   9379  N  N   . HIS B  1 297 ? 1.940   20.367  47.844  1.00 58.32  ? 297  HIS C N   1 
ATOM   9380  C  CA  . HIS B  1 297 ? 1.007   21.330  48.412  1.00 59.90  ? 297  HIS C CA  1 
ATOM   9381  C  C   . HIS B  1 297 ? 0.806   21.150  49.890  1.00 62.27  ? 297  HIS C C   1 
ATOM   9382  O  O   . HIS B  1 297 ? 0.870   22.125  50.659  1.00 61.99  ? 297  HIS C O   1 
ATOM   9383  C  CB  . HIS B  1 297 ? -0.332  21.260  47.691  1.00 59.99  ? 297  HIS C CB  1 
ATOM   9384  C  CG  . HIS B  1 297 ? -0.354  22.056  46.427  1.00 70.21  ? 297  HIS C CG  1 
ATOM   9385  N  ND1 . HIS B  1 297 ? -0.733  21.521  45.213  1.00 72.30  ? 297  HIS C ND1 1 
ATOM   9386  C  CD2 . HIS B  1 297 ? -0.009  23.345  46.184  1.00 60.52  ? 297  HIS C CD2 1 
ATOM   9387  C  CE1 . HIS B  1 297 ? -0.636  22.454  44.280  1.00 76.01  ? 297  HIS C CE1 1 
ATOM   9388  N  NE2 . HIS B  1 297 ? -0.197  23.568  44.843  1.00 61.05  ? 297  HIS C NE2 1 
ATOM   9389  N  N   . TYR B  1 298 ? 0.573   19.907  50.288  1.00 58.87  ? 298  TYR C N   1 
ATOM   9390  C  CA  . TYR B  1 298 ? 0.300   19.633  51.680  1.00 56.91  ? 298  TYR C CA  1 
ATOM   9391  C  C   . TYR B  1 298 ? 1.473   20.054  52.536  1.00 59.55  ? 298  TYR C C   1 
ATOM   9392  O  O   . TYR B  1 298 ? 1.300   20.618  53.624  1.00 57.43  ? 298  TYR C O   1 
ATOM   9393  C  CB  . TYR B  1 298 ? 0.003   18.161  51.910  1.00 55.45  ? 298  TYR C CB  1 
ATOM   9394  C  CG  . TYR B  1 298 ? -0.135  17.889  53.377  1.00 67.14  ? 298  TYR C CG  1 
ATOM   9395  C  CD1 . TYR B  1 298 ? -1.217  18.385  54.087  1.00 66.74  ? 298  TYR C CD1 1 
ATOM   9396  C  CD2 . TYR B  1 298 ? 0.841   17.184  54.069  1.00 66.02  ? 298  TYR C CD2 1 
ATOM   9397  C  CE1 . TYR B  1 298 ? -1.335  18.170  55.441  1.00 70.59  ? 298  TYR C CE1 1 
ATOM   9398  C  CE2 . TYR B  1 298 ? 0.726   16.957  55.418  1.00 65.19  ? 298  TYR C CE2 1 
ATOM   9399  C  CZ  . TYR B  1 298 ? -0.367  17.449  56.100  1.00 69.32  ? 298  TYR C CZ  1 
ATOM   9400  O  OH  . TYR B  1 298 ? -0.491  17.221  57.450  1.00 76.10  ? 298  TYR C OH  1 
ATOM   9401  N  N   . ALA B  1 299 ? 2.671   19.784  52.033  1.00 59.03  ? 299  ALA C N   1 
ATOM   9402  C  CA  . ALA B  1 299 ? 3.875   20.111  52.772  1.00 57.61  ? 299  ALA C CA  1 
ATOM   9403  C  C   . ALA B  1 299 ? 3.926   21.597  53.035  1.00 57.11  ? 299  ALA C C   1 
ATOM   9404  O  O   . ALA B  1 299 ? 4.190   22.009  54.156  1.00 54.03  ? 299  ALA C O   1 
ATOM   9405  C  CB  . ALA B  1 299 ? 5.106   19.658  52.029  1.00 56.29  ? 299  ALA C CB  1 
ATOM   9406  N  N   . LEU B  1 300 ? 3.643   22.404  52.014  1.00 61.59  ? 300  LEU C N   1 
ATOM   9407  C  CA  . LEU B  1 300 ? 3.714   23.854  52.183  1.00 60.59  ? 300  LEU C CA  1 
ATOM   9408  C  C   . LEU B  1 300 ? 2.736   24.292  53.265  1.00 60.15  ? 300  LEU C C   1 
ATOM   9409  O  O   . LEU B  1 300 ? 3.129   24.967  54.225  1.00 59.44  ? 300  LEU C O   1 
ATOM   9410  C  CB  . LEU B  1 300 ? 3.434   24.594  50.872  1.00 58.18  ? 300  LEU C CB  1 
ATOM   9411  C  CG  . LEU B  1 300 ? 3.612   26.124  50.944  1.00 59.66  ? 300  LEU C CG  1 
ATOM   9412  C  CD1 . LEU B  1 300 ? 4.987   26.527  51.498  1.00 52.82  ? 300  LEU C CD1 1 
ATOM   9413  C  CD2 . LEU B  1 300 ? 3.346   26.808  49.594  1.00 52.85  ? 300  LEU C CD2 1 
ATOM   9414  N  N   . GLN B  1 301 ? 1.476   23.884  53.120  1.00 57.38  ? 301  GLN C N   1 
ATOM   9415  C  CA  . GLN B  1 301 ? 0.457   24.170  54.128  1.00 59.98  ? 301  GLN C CA  1 
ATOM   9416  C  C   . GLN B  1 301 ? 0.941   23.773  55.524  1.00 62.41  ? 301  GLN C C   1 
ATOM   9417  O  O   . GLN B  1 301 ? 1.114   24.634  56.400  1.00 56.23  ? 301  GLN C O   1 
ATOM   9418  C  CB  . GLN B  1 301 ? -0.849  23.446  53.789  1.00 61.93  ? 301  GLN C CB  1 
ATOM   9419  C  CG  . GLN B  1 301 ? -1.830  23.367  54.953  1.00 70.61  ? 301  GLN C CG  1 
ATOM   9420  C  CD  . GLN B  1 301 ? -2.940  22.357  54.704  1.00 78.76  ? 301  GLN C CD  1 
ATOM   9421  O  OE1 . GLN B  1 301 ? -3.159  21.926  53.565  1.00 79.79  ? 301  GLN C OE1 1 
ATOM   9422  N  NE2 . GLN B  1 301 ? -3.642  21.969  55.768  1.00 71.35  ? 301  GLN C NE2 1 
ATOM   9423  N  N   . ALA B  1 302 ? 1.204   22.475  55.697  1.00 62.34  ? 302  ALA C N   1 
ATOM   9424  C  CA  . ALA B  1 302 ? 1.640   21.916  56.973  1.00 56.42  ? 302  ALA C CA  1 
ATOM   9425  C  C   . ALA B  1 302 ? 2.969   22.500  57.452  1.00 57.99  ? 302  ALA C C   1 
ATOM   9426  O  O   . ALA B  1 302 ? 3.156   22.737  58.647  1.00 61.22  ? 302  ALA C O   1 
ATOM   9427  C  CB  . ALA B  1 302 ? 1.745   20.406  56.873  1.00 58.60  ? 302  ALA C CB  1 
ATOM   9428  N  N   . SER B  1 303 ? 3.893   22.731  56.529  1.00 57.79  ? 303  SER C N   1 
ATOM   9429  C  CA  . SER B  1 303 ? 5.169   23.318  56.900  1.00 56.22  ? 303  SER C CA  1 
ATOM   9430  C  C   . SER B  1 303 ? 4.933   24.678  57.552  1.00 59.72  ? 303  SER C C   1 
ATOM   9431  O  O   . SER B  1 303 ? 5.582   25.025  58.548  1.00 51.83  ? 303  SER C O   1 
ATOM   9432  C  CB  . SER B  1 303 ? 6.072   23.466  55.676  1.00 53.65  ? 303  SER C CB  1 
ATOM   9433  O  OG  . SER B  1 303 ? 7.400   23.720  56.069  1.00 64.58  ? 303  SER C OG  1 
ATOM   9434  N  N   . LEU B  1 304 ? 3.995   25.438  56.982  1.00 57.54  ? 304  LEU C N   1 
ATOM   9435  C  CA  . LEU B  1 304 ? 3.703   26.786  57.457  1.00 59.88  ? 304  LEU C CA  1 
ATOM   9436  C  C   . LEU B  1 304 ? 3.135   26.770  58.879  1.00 59.01  ? 304  LEU C C   1 
ATOM   9437  O  O   . LEU B  1 304 ? 3.606   27.502  59.750  1.00 58.30  ? 304  LEU C O   1 
ATOM   9438  C  CB  . LEU B  1 304 ? 2.749   27.488  56.483  1.00 59.73  ? 304  LEU C CB  1 
ATOM   9439  C  CG  . LEU B  1 304 ? 3.474   28.112  55.273  1.00 56.42  ? 304  LEU C CG  1 
ATOM   9440  C  CD1 . LEU B  1 304 ? 2.538   28.453  54.116  1.00 45.57  ? 304  LEU C CD1 1 
ATOM   9441  C  CD2 . LEU B  1 304 ? 4.247   29.343  55.713  1.00 53.04  ? 304  LEU C CD2 1 
ATOM   9442  N  N   . LYS B  1 305 ? 2.141   25.919  59.115  1.00 60.06  ? 305  LYS C N   1 
ATOM   9443  C  CA  . LYS B  1 305 ? 1.552   25.781  60.436  1.00 57.55  ? 305  LYS C CA  1 
ATOM   9444  C  C   . LYS B  1 305 ? 2.607   25.393  61.473  1.00 63.80  ? 305  LYS C C   1 
ATOM   9445  O  O   . LYS B  1 305 ? 2.771   26.062  62.502  1.00 60.25  ? 305  LYS C O   1 
ATOM   9446  C  CB  . LYS B  1 305 ? 0.437   24.741  60.411  1.00 57.13  ? 305  LYS C CB  1 
ATOM   9447  C  CG  . LYS B  1 305 ? -0.720  25.095  59.522  1.00 58.95  ? 305  LYS C CG  1 
ATOM   9448  C  CD  . LYS B  1 305 ? -1.928  24.223  59.820  1.00 74.25  ? 305  LYS C CD  1 
ATOM   9449  C  CE  . LYS B  1 305 ? -3.140  24.646  58.985  1.00 81.29  ? 305  LYS C CE  1 
ATOM   9450  N  NZ  . LYS B  1 305 ? -4.235  23.624  58.995  1.00 77.38  ? 305  LYS C NZ  1 
ATOM   9451  N  N   . LEU B  1 306 ? 3.332   24.315  61.201  1.00 58.75  ? 306  LEU C N   1 
ATOM   9452  C  CA  . LEU B  1 306 ? 4.289   23.816  62.177  1.00 60.00  ? 306  LEU C CA  1 
ATOM   9453  C  C   . LEU B  1 306 ? 5.372   24.841  62.472  1.00 56.31  ? 306  LEU C C   1 
ATOM   9454  O  O   . LEU B  1 306 ? 5.790   24.983  63.618  1.00 58.33  ? 306  LEU C O   1 
ATOM   9455  C  CB  . LEU B  1 306 ? 4.902   22.495  61.703  1.00 52.50  ? 306  LEU C CB  1 
ATOM   9456  C  CG  . LEU B  1 306 ? 3.917   21.340  61.880  1.00 55.47  ? 306  LEU C CG  1 
ATOM   9457  C  CD1 . LEU B  1 306 ? 4.268   20.173  60.983  1.00 51.14  ? 306  LEU C CD1 1 
ATOM   9458  C  CD2 . LEU B  1 306 ? 3.873   20.910  63.362  1.00 58.90  ? 306  LEU C CD2 1 
ATOM   9459  N  N   . LEU B  1 307 ? 5.805   25.583  61.462  1.00 53.02  ? 307  LEU C N   1 
ATOM   9460  C  CA  . LEU B  1 307 ? 6.950   26.470  61.665  1.00 55.67  ? 307  LEU C CA  1 
ATOM   9461  C  C   . LEU B  1 307 ? 6.647   27.576  62.664  1.00 64.76  ? 307  LEU C C   1 
ATOM   9462  O  O   . LEU B  1 307 ? 7.434   27.814  63.589  1.00 61.71  ? 307  LEU C O   1 
ATOM   9463  C  CB  . LEU B  1 307 ? 7.430   27.104  60.355  1.00 48.06  ? 307  LEU C CB  1 
ATOM   9464  C  CG  . LEU B  1 307 ? 8.718   27.876  60.661  1.00 49.68  ? 307  LEU C CG  1 
ATOM   9465  C  CD1 . LEU B  1 307 ? 9.818   26.932  61.180  1.00 48.06  ? 307  LEU C CD1 1 
ATOM   9466  C  CD2 . LEU B  1 307 ? 9.210   28.665  59.476  1.00 55.71  ? 307  LEU C CD2 1 
ATOM   9467  N  N   . ASP B  1 308 ? 5.516   28.258  62.477  1.00 65.36  ? 308  ASP C N   1 
ATOM   9468  C  CA  . ASP B  1 308 ? 5.199   29.392  63.343  1.00 73.58  ? 308  ASP C CA  1 
ATOM   9469  C  C   . ASP B  1 308 ? 4.888   28.906  64.763  1.00 68.14  ? 308  ASP C C   1 
ATOM   9470  O  O   . ASP B  1 308 ? 5.283   29.551  65.741  1.00 63.31  ? 308  ASP C O   1 
ATOM   9471  C  CB  . ASP B  1 308 ? 4.041   30.240  62.770  1.00 77.46  ? 308  ASP C CB  1 
ATOM   9472  C  CG  . ASP B  1 308 ? 2.747   29.442  62.557  1.00 80.56  ? 308  ASP C CG  1 
ATOM   9473  O  OD1 . ASP B  1 308 ? 2.261   28.789  63.517  1.00 78.16  ? 308  ASP C OD1 1 
ATOM   9474  O  OD2 . ASP B  1 308 ? 2.208   29.496  61.420  1.00 73.92  ? 308  ASP C OD2 1 
ATOM   9475  N  N   . PHE B  1 309 ? 4.206   27.762  64.861  1.00 69.47  ? 309  PHE C N   1 
ATOM   9476  C  CA  . PHE B  1 309 ? 3.867   27.175  66.151  1.00 63.80  ? 309  PHE C CA  1 
ATOM   9477  C  C   . PHE B  1 309 ? 5.099   27.061  67.035  1.00 66.30  ? 309  PHE C C   1 
ATOM   9478  O  O   . PHE B  1 309 ? 5.046   27.348  68.227  1.00 71.46  ? 309  PHE C O   1 
ATOM   9479  C  CB  . PHE B  1 309 ? 3.231   25.800  65.987  1.00 61.19  ? 309  PHE C CB  1 
ATOM   9480  C  CG  . PHE B  1 309 ? 3.327   24.953  67.223  1.00 69.11  ? 309  PHE C CG  1 
ATOM   9481  C  CD1 . PHE B  1 309 ? 2.405   25.098  68.252  1.00 74.24  ? 309  PHE C CD1 1 
ATOM   9482  C  CD2 . PHE B  1 309 ? 4.357   24.035  67.377  1.00 64.92  ? 309  PHE C CD2 1 
ATOM   9483  C  CE1 . PHE B  1 309 ? 2.496   24.331  69.409  1.00 70.01  ? 309  PHE C CE1 1 
ATOM   9484  C  CE2 . PHE B  1 309 ? 4.458   23.267  68.528  1.00 71.45  ? 309  PHE C CE2 1 
ATOM   9485  C  CZ  . PHE B  1 309 ? 3.523   23.415  69.550  1.00 73.15  ? 309  PHE C CZ  1 
ATOM   9486  N  N   . TYR B  1 310 ? 6.212   26.649  66.445  1.00 64.71  ? 310  TYR C N   1 
ATOM   9487  C  CA  . TYR B  1 310 ? 7.427   26.445  67.218  1.00 65.15  ? 310  TYR C CA  1 
ATOM   9488  C  C   . TYR B  1 310 ? 8.004   27.770  67.738  1.00 64.92  ? 310  TYR C C   1 
ATOM   9489  O  O   . TYR B  1 310 ? 8.481   27.829  68.877  1.00 65.53  ? 310  TYR C O   1 
ATOM   9490  C  CB  . TYR B  1 310 ? 8.483   25.709  66.385  1.00 65.12  ? 310  TYR C CB  1 
ATOM   9491  C  CG  . TYR B  1 310 ? 8.311   24.198  66.225  1.00 63.87  ? 310  TYR C CG  1 
ATOM   9492  C  CD1 . TYR B  1 310 ? 8.340   23.345  67.330  1.00 59.45  ? 310  TYR C CD1 1 
ATOM   9493  C  CD2 . TYR B  1 310 ? 8.193   23.620  64.950  1.00 56.10  ? 310  TYR C CD2 1 
ATOM   9494  C  CE1 . TYR B  1 310 ? 8.211   21.964  67.171  1.00 58.15  ? 310  TYR C CE1 1 
ATOM   9495  C  CE2 . TYR B  1 310 ? 8.060   22.244  64.782  1.00 49.03  ? 310  TYR C CE2 1 
ATOM   9496  C  CZ  . TYR B  1 310 ? 8.075   21.424  65.890  1.00 54.34  ? 310  TYR C CZ  1 
ATOM   9497  O  OH  . TYR B  1 310 ? 7.961   20.064  65.727  1.00 45.23  ? 310  TYR C OH  1 
ATOM   9498  N  N   . GLU B  1 311 ? 7.958   28.818  66.907  1.00 65.87  ? 311  GLU C N   1 
ATOM   9499  C  CA  . GLU B  1 311 ? 8.550   30.132  67.227  1.00 64.33  ? 311  GLU C CA  1 
ATOM   9500  C  C   . GLU B  1 311 ? 7.937   30.790  68.488  1.00 70.58  ? 311  GLU C C   1 
ATOM   9501  O  O   . GLU B  1 311 ? 8.654   31.347  69.338  1.00 64.81  ? 311  GLU C O   1 
ATOM   9502  C  CB  . GLU B  1 311 ? 8.418   31.081  66.025  1.00 59.21  ? 311  GLU C CB  1 
ATOM   9503  C  CG  . GLU B  1 311 ? 9.157   30.617  64.769  1.00 65.00  ? 311  GLU C CG  1 
ATOM   9504  C  CD  . GLU B  1 311 ? 9.375   31.723  63.739  1.00 60.47  ? 311  GLU C CD  1 
ATOM   9505  O  OE1 . GLU B  1 311 ? 8.471   31.965  62.905  1.00 57.00  ? 311  GLU C OE1 1 
ATOM   9506  O  OE2 . GLU B  1 311 ? 10.463  32.331  63.749  1.00 59.58  ? 311  GLU C OE2 1 
ATOM   9507  N  N   . LYS B  1 312 ? 6.617   30.730  68.615  1.00 67.23  ? 312  LYS C N   1 
ATOM   9508  C  CA  . LYS B  1 312 ? 5.996   31.172  69.849  1.00 72.59  ? 312  LYS C CA  1 
ATOM   9509  C  C   . LYS B  1 312 ? 6.301   30.160  70.955  1.00 69.42  ? 312  LYS C C   1 
ATOM   9510  O  O   . LYS B  1 312 ? 6.833   30.540  72.001  1.00 65.33  ? 312  LYS C O   1 
ATOM   9511  C  CB  . LYS B  1 312 ? 4.484   31.376  69.677  1.00 78.78  ? 312  LYS C CB  1 
ATOM   9512  C  CG  . LYS B  1 312 ? 3.687   30.162  69.191  1.00 74.49  ? 312  LYS C CG  1 
ATOM   9513  C  CD  . LYS B  1 312 ? 2.312   30.596  68.701  1.00 80.89  ? 312  LYS C CD  1 
ATOM   9514  C  CE  . LYS B  1 312 ? 1.622   31.492  69.725  1.00 81.98  ? 312  LYS C CE  1 
ATOM   9515  N  NZ  . LYS B  1 312 ? 0.719   32.474  69.072  1.00 82.63  ? 312  LYS C NZ  1 
ATOM   9516  N  N   . TYR B  1 313 ? 6.008   28.880  70.706  1.00 69.09  ? 313  TYR C N   1 
ATOM   9517  C  CA  . TYR B  1 313 ? 6.134   27.832  71.722  1.00 61.08  ? 313  TYR C CA  1 
ATOM   9518  C  C   . TYR B  1 313 ? 7.543   27.798  72.312  1.00 63.49  ? 313  TYR C C   1 
ATOM   9519  O  O   . TYR B  1 313 ? 7.717   27.548  73.502  1.00 66.71  ? 313  TYR C O   1 
ATOM   9520  C  CB  . TYR B  1 313 ? 5.758   26.468  71.137  1.00 64.49  ? 313  TYR C CB  1 
ATOM   9521  C  CG  . TYR B  1 313 ? 5.708   25.356  72.159  1.00 71.45  ? 313  TYR C CG  1 
ATOM   9522  C  CD1 . TYR B  1 313 ? 6.852   24.628  72.484  1.00 70.92  ? 313  TYR C CD1 1 
ATOM   9523  C  CD2 . TYR B  1 313 ? 4.520   25.030  72.804  1.00 71.52  ? 313  TYR C CD2 1 
ATOM   9524  C  CE1 . TYR B  1 313 ? 6.815   23.610  73.431  1.00 69.68  ? 313  TYR C CE1 1 
ATOM   9525  C  CE2 . TYR B  1 313 ? 4.471   24.016  73.756  1.00 71.56  ? 313  TYR C CE2 1 
ATOM   9526  C  CZ  . TYR B  1 313 ? 5.621   23.309  74.063  1.00 72.96  ? 313  TYR C CZ  1 
ATOM   9527  O  OH  . TYR B  1 313 ? 5.577   22.300  75.000  1.00 72.61  ? 313  TYR C OH  1 
ATOM   9528  N  N   . PHE B  1 314 ? 8.549   28.083  71.494  1.00 61.74  ? 314  PHE C N   1 
ATOM   9529  C  CA  . PHE B  1 314 ? 9.916   28.175  71.995  1.00 62.85  ? 314  PHE C CA  1 
ATOM   9530  C  C   . PHE B  1 314 ? 10.246  29.582  72.471  1.00 61.14  ? 314  PHE C C   1 
ATOM   9531  O  O   . PHE B  1 314 ? 11.288  29.800  73.096  1.00 59.51  ? 314  PHE C O   1 
ATOM   9532  C  CB  . PHE B  1 314 ? 10.926  27.759  70.914  1.00 61.45  ? 314  PHE C CB  1 
ATOM   9533  C  CG  . PHE B  1 314 ? 10.903  26.298  70.585  1.00 61.43  ? 314  PHE C CG  1 
ATOM   9534  C  CD1 . PHE B  1 314 ? 10.698  25.347  71.576  1.00 66.20  ? 314  PHE C CD1 1 
ATOM   9535  C  CD2 . PHE B  1 314 ? 11.081  25.870  69.279  1.00 61.09  ? 314  PHE C CD2 1 
ATOM   9536  C  CE1 . PHE B  1 314 ? 10.677  23.988  71.272  1.00 60.59  ? 314  PHE C CE1 1 
ATOM   9537  C  CE2 . PHE B  1 314 ? 11.057  24.521  68.967  1.00 59.99  ? 314  PHE C CE2 1 
ATOM   9538  C  CZ  . PHE B  1 314 ? 10.854  23.580  69.966  1.00 62.39  ? 314  PHE C CZ  1 
ATOM   9539  N  N   . ASP B  1 315 ? 9.363   30.531  72.151  1.00 64.45  ? 315  ASP C N   1 
ATOM   9540  C  CA  . ASP B  1 315 ? 9.629   31.969  72.298  1.00 62.44  ? 315  ASP C CA  1 
ATOM   9541  C  C   . ASP B  1 315 ? 10.924  32.385  71.594  1.00 63.85  ? 315  ASP C C   1 
ATOM   9542  O  O   . ASP B  1 315 ? 11.570  33.361  71.986  1.00 65.48  ? 315  ASP C O   1 
ATOM   9543  C  CB  . ASP B  1 315 ? 9.695   32.374  73.777  1.00 63.95  ? 315  ASP C CB  1 
ATOM   9544  C  CG  . ASP B  1 315 ? 9.508   33.875  73.984  1.00 61.31  ? 315  ASP C CG  1 
ATOM   9545  O  OD1 . ASP B  1 315 ? 8.494   34.412  73.484  1.00 61.45  ? 315  ASP C OD1 1 
ATOM   9546  O  OD2 . ASP B  1 315 ? 10.379  34.511  74.623  1.00 52.61  ? 315  ASP C OD2 1 
ATOM   9547  N  N   . ILE B  1 316 ? 11.319  31.629  70.570  1.00 64.63  ? 316  ILE C N   1 
ATOM   9548  C  CA  . ILE B  1 316 ? 12.497  31.978  69.774  1.00 62.63  ? 316  ILE C CA  1 
ATOM   9549  C  C   . ILE B  1 316 ? 12.177  31.944  68.292  1.00 56.25  ? 316  ILE C C   1 
ATOM   9550  O  O   . ILE B  1 316 ? 11.575  30.994  67.809  1.00 57.85  ? 316  ILE C O   1 
ATOM   9551  C  CB  . ILE B  1 316 ? 13.667  31.043  70.040  1.00 56.14  ? 316  ILE C CB  1 
ATOM   9552  C  CG1 . ILE B  1 316 ? 13.929  30.956  71.534  1.00 58.46  ? 316  ILE C CG1 1 
ATOM   9553  C  CG2 . ILE B  1 316 ? 14.917  31.530  69.305  1.00 52.77  ? 316  ILE C CG2 1 
ATOM   9554  C  CD1 . ILE B  1 316 ? 15.054  30.053  71.874  1.00 57.69  ? 316  ILE C CD1 1 
ATOM   9555  N  N   . TYR B  1 317 ? 12.566  32.999  67.587  1.00 50.84  ? 317  TYR C N   1 
ATOM   9556  C  CA  . TYR B  1 317 ? 12.295  33.123  66.166  1.00 57.10  ? 317  TYR C CA  1 
ATOM   9557  C  C   . TYR B  1 317 ? 13.233  32.252  65.315  1.00 56.02  ? 317  TYR C C   1 
ATOM   9558  O  O   . TYR B  1 317 ? 14.432  32.189  65.588  1.00 57.43  ? 317  TYR C O   1 
ATOM   9559  C  CB  . TYR B  1 317 ? 12.425  34.590  65.750  1.00 57.16  ? 317  TYR C CB  1 
ATOM   9560  C  CG  . TYR B  1 317 ? 11.171  35.418  65.943  1.00 61.01  ? 317  TYR C CG  1 
ATOM   9561  C  CD1 . TYR B  1 317 ? 9.972   35.032  65.348  1.00 57.73  ? 317  TYR C CD1 1 
ATOM   9562  C  CD2 . TYR B  1 317 ? 11.192  36.604  66.694  1.00 57.98  ? 317  TYR C CD2 1 
ATOM   9563  C  CE1 . TYR B  1 317 ? 8.821   35.779  65.502  1.00 63.07  ? 317  TYR C CE1 1 
ATOM   9564  C  CE2 . TYR B  1 317 ? 10.039  37.366  66.855  1.00 61.23  ? 317  TYR C CE2 1 
ATOM   9565  C  CZ  . TYR B  1 317 ? 8.855   36.942  66.253  1.00 68.75  ? 317  TYR C CZ  1 
ATOM   9566  O  OH  . TYR B  1 317 ? 7.689   37.659  66.384  1.00 68.92  ? 317  TYR C OH  1 
ATOM   9567  N  N   . TYR B  1 318 ? 12.697  31.579  64.299  1.00 54.55  ? 318  TYR C N   1 
ATOM   9568  C  CA  . TYR B  1 318 ? 13.550  30.968  63.280  1.00 52.70  ? 318  TYR C CA  1 
ATOM   9569  C  C   . TYR B  1 318 ? 14.354  32.100  62.670  1.00 53.24  ? 318  TYR C C   1 
ATOM   9570  O  O   . TYR B  1 318 ? 13.779  32.983  62.046  1.00 59.48  ? 318  TYR C O   1 
ATOM   9571  C  CB  . TYR B  1 318 ? 12.721  30.234  62.219  1.00 57.89  ? 318  TYR C CB  1 
ATOM   9572  C  CG  . TYR B  1 318 ? 13.542  29.635  61.075  1.00 60.96  ? 318  TYR C CG  1 
ATOM   9573  C  CD1 . TYR B  1 318 ? 14.202  28.399  61.211  1.00 56.95  ? 318  TYR C CD1 1 
ATOM   9574  C  CD2 . TYR B  1 318 ? 13.643  30.294  59.865  1.00 52.44  ? 318  TYR C CD2 1 
ATOM   9575  C  CE1 . TYR B  1 318 ? 14.948  27.862  60.173  1.00 46.78  ? 318  TYR C CE1 1 
ATOM   9576  C  CE2 . TYR B  1 318 ? 14.379  29.774  58.826  1.00 53.36  ? 318  TYR C CE2 1 
ATOM   9577  C  CZ  . TYR B  1 318 ? 15.024  28.563  58.975  1.00 56.50  ? 318  TYR C CZ  1 
ATOM   9578  O  OH  . TYR B  1 318 ? 15.747  28.087  57.911  1.00 49.78  ? 318  TYR C OH  1 
ATOM   9579  N  N   . PRO B  1 319 ? 15.684  32.091  62.863  1.00 51.21  ? 319  PRO C N   1 
ATOM   9580  C  CA  . PRO B  1 319 ? 16.524  33.268  62.617  1.00 50.23  ? 319  PRO C CA  1 
ATOM   9581  C  C   . PRO B  1 319 ? 17.077  33.395  61.179  1.00 49.85  ? 319  PRO C C   1 
ATOM   9582  O  O   . PRO B  1 319 ? 18.110  34.027  60.982  1.00 47.65  ? 319  PRO C O   1 
ATOM   9583  C  CB  . PRO B  1 319 ? 17.668  33.070  63.626  1.00 50.41  ? 319  PRO C CB  1 
ATOM   9584  C  CG  . PRO B  1 319 ? 17.855  31.582  63.655  1.00 51.39  ? 319  PRO C CG  1 
ATOM   9585  C  CD  . PRO B  1 319 ? 16.491  30.949  63.326  1.00 51.52  ? 319  PRO C CD  1 
ATOM   9586  N  N   . LEU B  1 320 ? 16.400  32.810  60.198  1.00 50.95  ? 320  LEU C N   1 
ATOM   9587  C  CA  . LEU B  1 320 ? 16.816  32.912  58.800  1.00 48.71  ? 320  LEU C CA  1 
ATOM   9588  C  C   . LEU B  1 320 ? 15.599  33.338  57.996  1.00 52.85  ? 320  LEU C C   1 
ATOM   9589  O  O   . LEU B  1 320 ? 14.467  33.026  58.373  1.00 53.60  ? 320  LEU C O   1 
ATOM   9590  C  CB  . LEU B  1 320 ? 17.368  31.583  58.269  1.00 44.78  ? 320  LEU C CB  1 
ATOM   9591  C  CG  . LEU B  1 320 ? 18.307  30.731  59.118  1.00 43.44  ? 320  LEU C CG  1 
ATOM   9592  C  CD1 . LEU B  1 320 ? 18.684  29.456  58.355  1.00 41.32  ? 320  LEU C CD1 1 
ATOM   9593  C  CD2 . LEU B  1 320 ? 19.553  31.503  59.546  1.00 43.63  ? 320  LEU C CD2 1 
ATOM   9594  N  N   . SER B  1 321 ? 15.813  34.039  56.889  1.00 56.48  ? 321  SER C N   1 
ATOM   9595  C  CA  . SER B  1 321 ? 14.692  34.658  56.181  1.00 54.04  ? 321  SER C CA  1 
ATOM   9596  C  C   . SER B  1 321 ? 13.969  33.681  55.287  1.00 49.85  ? 321  SER C C   1 
ATOM   9597  O  O   . SER B  1 321 ? 12.798  33.872  54.948  1.00 55.06  ? 321  SER C O   1 
ATOM   9598  C  CB  . SER B  1 321 ? 15.178  35.851  55.364  1.00 59.58  ? 321  SER C CB  1 
ATOM   9599  O  OG  . SER B  1 321 ? 16.365  35.529  54.668  1.00 71.44  ? 321  SER C OG  1 
ATOM   9600  N  N   . LYS B  1 322 ? 14.671  32.629  54.891  1.00 52.16  ? 322  LYS C N   1 
ATOM   9601  C  CA  . LYS B  1 322 ? 14.057  31.577  54.081  1.00 51.52  ? 322  LYS C CA  1 
ATOM   9602  C  C   . LYS B  1 322 ? 14.299  30.218  54.725  1.00 45.17  ? 322  LYS C C   1 
ATOM   9603  O  O   . LYS B  1 322 ? 15.341  29.986  55.346  1.00 38.31  ? 322  LYS C O   1 
ATOM   9604  C  CB  . LYS B  1 322 ? 14.603  31.596  52.640  1.00 43.72  ? 322  LYS C CB  1 
ATOM   9605  C  CG  . LYS B  1 322 ? 16.054  31.093  52.476  1.00 47.69  ? 322  LYS C CG  1 
ATOM   9606  C  CD  . LYS B  1 322 ? 16.118  29.587  52.099  1.00 47.32  ? 322  LYS C CD  1 
ATOM   9607  C  CE  . LYS B  1 322 ? 17.556  29.075  52.000  1.00 45.47  ? 322  LYS C CE  1 
ATOM   9608  N  NZ  . LYS B  1 322 ? 17.641  27.642  51.561  1.00 49.14  ? 322  LYS C NZ  1 
ATOM   9609  N  N   . LEU B  1 323 ? 13.337  29.322  54.571  1.00 46.47  ? 323  LEU C N   1 
ATOM   9610  C  CA  . LEU B  1 323 ? 13.568  27.933  54.919  1.00 47.80  ? 323  LEU C CA  1 
ATOM   9611  C  C   . LEU B  1 323 ? 13.030  27.100  53.797  1.00 46.11  ? 323  LEU C C   1 
ATOM   9612  O  O   . LEU B  1 323 ? 11.838  27.191  53.498  1.00 46.36  ? 323  LEU C O   1 
ATOM   9613  C  CB  . LEU B  1 323 ? 12.905  27.546  56.256  1.00 51.42  ? 323  LEU C CB  1 
ATOM   9614  C  CG  . LEU B  1 323 ? 12.819  26.042  56.607  1.00 52.90  ? 323  LEU C CG  1 
ATOM   9615  C  CD1 . LEU B  1 323 ? 14.147  25.308  56.386  1.00 43.41  ? 323  LEU C CD1 1 
ATOM   9616  C  CD2 . LEU B  1 323 ? 12.345  25.834  58.041  1.00 47.46  ? 323  LEU C CD2 1 
ATOM   9617  N  N   . ASP B  1 324 ? 13.904  26.284  53.188  1.00 41.90  ? 324  ASP C N   1 
ATOM   9618  C  CA  . ASP B  1 324 ? 13.487  25.408  52.082  1.00 49.70  ? 324  ASP C CA  1 
ATOM   9619  C  C   . ASP B  1 324 ? 13.398  23.924  52.480  1.00 45.13  ? 324  ASP C C   1 
ATOM   9620  O  O   . ASP B  1 324 ? 14.236  23.406  53.217  1.00 43.62  ? 324  ASP C O   1 
ATOM   9621  C  CB  . ASP B  1 324 ? 14.445  25.518  50.884  1.00 48.09  ? 324  ASP C CB  1 
ATOM   9622  C  CG  . ASP B  1 324 ? 14.682  26.940  50.426  1.00 49.70  ? 324  ASP C CG  1 
ATOM   9623  O  OD1 . ASP B  1 324 ? 13.735  27.764  50.392  1.00 55.50  ? 324  ASP C OD1 1 
ATOM   9624  O  OD2 . ASP B  1 324 ? 15.847  27.223  50.087  1.00 46.36  ? 324  ASP C OD2 1 
ATOM   9625  N  N   . LEU B  1 325 ? 12.390  23.250  51.945  1.00 43.62  ? 325  LEU C N   1 
ATOM   9626  C  CA  . LEU B  1 325 ? 12.258  21.810  52.064  1.00 41.16  ? 325  LEU C CA  1 
ATOM   9627  C  C   . LEU B  1 325 ? 12.336  21.214  50.660  1.00 44.36  ? 325  LEU C C   1 
ATOM   9628  O  O   . LEU B  1 325 ? 11.596  21.648  49.773  1.00 47.05  ? 325  LEU C O   1 
ATOM   9629  C  CB  . LEU B  1 325 ? 10.929  21.430  52.718  1.00 43.00  ? 325  LEU C CB  1 
ATOM   9630  C  CG  . LEU B  1 325 ? 10.569  21.774  54.169  1.00 48.45  ? 325  LEU C CG  1 
ATOM   9631  C  CD1 . LEU B  1 325 ? 10.558  23.260  54.484  1.00 42.24  ? 325  LEU C CD1 1 
ATOM   9632  C  CD2 . LEU B  1 325 ? 9.203   21.183  54.471  1.00 50.91  ? 325  LEU C CD2 1 
ATOM   9633  N  N   . ILE B  1 326 ? 13.199  20.221  50.451  1.00 37.96  ? 326  ILE C N   1 
ATOM   9634  C  CA  . ILE B  1 326 ? 13.371  19.642  49.111  1.00 40.21  ? 326  ILE C CA  1 
ATOM   9635  C  C   . ILE B  1 326 ? 13.255  18.094  49.061  1.00 38.30  ? 326  ILE C C   1 
ATOM   9636  O  O   . ILE B  1 326 ? 13.930  17.377  49.798  1.00 40.63  ? 326  ILE C O   1 
ATOM   9637  C  CB  . ILE B  1 326 ? 14.717  20.111  48.523  1.00 38.29  ? 326  ILE C CB  1 
ATOM   9638  C  CG1 . ILE B  1 326 ? 14.946  19.547  47.133  1.00 40.62  ? 326  ILE C CG1 1 
ATOM   9639  C  CG2 . ILE B  1 326 ? 15.880  19.796  49.453  1.00 38.87  ? 326  ILE C CG2 1 
ATOM   9640  C  CD1 . ILE B  1 326 ? 16.191  20.130  46.485  1.00 38.65  ? 326  ILE C CD1 1 
ATOM   9641  N  N   . ALA B  1 327 ? 12.360  17.597  48.208  1.00 37.11  ? 327  ALA C N   1 
ATOM   9642  C  CA  . ALA B  1 327 ? 12.109  16.165  48.043  1.00 36.67  ? 327  ALA C CA  1 
ATOM   9643  C  C   . ALA B  1 327 ? 13.151  15.490  47.154  1.00 38.76  ? 327  ALA C C   1 
ATOM   9644  O  O   . ALA B  1 327 ? 13.209  15.767  45.973  1.00 39.76  ? 327  ALA C O   1 
ATOM   9645  C  CB  . ALA B  1 327 ? 10.729  15.947  47.459  1.00 38.07  ? 327  ALA C CB  1 
ATOM   9646  N  N   . ILE B  1 328 ? 13.933  14.568  47.701  1.00 38.92  ? 328  ILE C N   1 
ATOM   9647  C  CA  . ILE B  1 328 ? 15.071  14.053  46.967  1.00 38.39  ? 328  ILE C CA  1 
ATOM   9648  C  C   . ILE B  1 328 ? 14.972  12.560  46.689  1.00 42.48  ? 328  ILE C C   1 
ATOM   9649  O  O   . ILE B  1 328 ? 14.814  11.754  47.587  1.00 47.36  ? 328  ILE C O   1 
ATOM   9650  C  CB  . ILE B  1 328 ? 16.347  14.397  47.714  1.00 42.26  ? 328  ILE C CB  1 
ATOM   9651  C  CG1 . ILE B  1 328 ? 16.482  15.926  47.709  1.00 38.40  ? 328  ILE C CG1 1 
ATOM   9652  C  CG2 . ILE B  1 328 ? 17.548  13.653  47.136  1.00 38.29  ? 328  ILE C CG2 1 
ATOM   9653  C  CD1 . ILE B  1 328 ? 17.817  16.448  48.072  1.00 40.91  ? 328  ILE C CD1 1 
ATOM   9654  N  N   . PRO B  1 329 ? 15.021  12.200  45.405  1.00 50.87  ? 329  PRO C N   1 
ATOM   9655  C  CA  . PRO B  1 329 ? 14.856  10.865  44.811  1.00 50.23  ? 329  PRO C CA  1 
ATOM   9656  C  C   . PRO B  1 329 ? 15.631  9.743   45.500  1.00 45.40  ? 329  PRO C C   1 
ATOM   9657  O  O   . PRO B  1 329 ? 15.035  8.769   45.950  1.00 51.51  ? 329  PRO C O   1 
ATOM   9658  C  CB  . PRO B  1 329 ? 15.391  11.066  43.393  1.00 55.87  ? 329  PRO C CB  1 
ATOM   9659  C  CG  . PRO B  1 329 ? 15.084  12.483  43.094  1.00 49.90  ? 329  PRO C CG  1 
ATOM   9660  C  CD  . PRO B  1 329 ? 15.290  13.222  44.379  1.00 48.60  ? 329  PRO C CD  1 
ATOM   9661  N  N   . ASP B  1 330 ? 16.951  9.885   45.566  1.00 45.37  ? 330  ASP C N   1 
ATOM   9662  C  CA  . ASP B  1 330 ? 17.815  8.905   46.219  1.00 46.74  ? 330  ASP C CA  1 
ATOM   9663  C  C   . ASP B  1 330 ? 18.303  9.439   47.534  1.00 51.44  ? 330  ASP C C   1 
ATOM   9664  O  O   . ASP B  1 330 ? 19.304  10.174  47.587  1.00 47.94  ? 330  ASP C O   1 
ATOM   9665  C  CB  . ASP B  1 330 ? 19.022  8.558   45.357  1.00 50.43  ? 330  ASP C CB  1 
ATOM   9666  C  CG  . ASP B  1 330 ? 18.633  8.028   44.013  1.00 52.40  ? 330  ASP C CG  1 
ATOM   9667  O  OD1 . ASP B  1 330 ? 18.294  6.827   43.929  1.00 57.62  ? 330  ASP C OD1 1 
ATOM   9668  O  OD2 . ASP B  1 330 ? 18.672  8.815   43.046  1.00 53.06  ? 330  ASP C OD2 1 
ATOM   9669  N  N   . PHE B  1 331 ? 17.606  9.077   48.601  1.00 47.24  ? 331  PHE C N   1 
ATOM   9670  C  CA  . PHE B  1 331 ? 17.937  9.666   49.872  1.00 47.49  ? 331  PHE C CA  1 
ATOM   9671  C  C   . PHE B  1 331 ? 17.890  8.600   50.957  1.00 46.80  ? 331  PHE C C   1 
ATOM   9672  O  O   . PHE B  1 331 ? 16.850  7.997   51.198  1.00 47.32  ? 331  PHE C O   1 
ATOM   9673  C  CB  . PHE B  1 331 ? 17.004  10.861  50.161  1.00 47.54  ? 331  PHE C CB  1 
ATOM   9674  C  CG  . PHE B  1 331 ? 17.569  11.826  51.156  1.00 42.87  ? 331  PHE C CG  1 
ATOM   9675  C  CD1 . PHE B  1 331 ? 18.657  12.612  50.829  1.00 37.32  ? 331  PHE C CD1 1 
ATOM   9676  C  CD2 . PHE B  1 331 ? 17.036  11.917  52.437  1.00 45.12  ? 331  PHE C CD2 1 
ATOM   9677  C  CE1 . PHE B  1 331 ? 19.192  13.475  51.741  1.00 30.76  ? 331  PHE C CE1 1 
ATOM   9678  C  CE2 . PHE B  1 331 ? 17.579  12.783  53.355  1.00 38.47  ? 331  PHE C CE2 1 
ATOM   9679  C  CZ  . PHE B  1 331 ? 18.662  13.549  53.002  1.00 35.59  ? 331  PHE C CZ  1 
ATOM   9680  N  N   . ALA B  1 332 ? 19.046  8.361   51.575  1.00 40.85  ? 332  ALA C N   1 
ATOM   9681  C  CA  . ALA B  1 332 ? 19.196  7.279   52.525  1.00 41.68  ? 332  ALA C CA  1 
ATOM   9682  C  C   . ALA B  1 332 ? 18.422  7.542   53.800  1.00 43.07  ? 332  ALA C C   1 
ATOM   9683  O  O   . ALA B  1 332 ? 17.581  6.720   54.145  1.00 48.67  ? 332  ALA C O   1 
ATOM   9684  C  CB  . ALA B  1 332 ? 20.655  7.026   52.830  1.00 46.54  ? 332  ALA C CB  1 
ATOM   9685  N  N   . PRO B  1 333 ? 18.665  8.686   54.494  1.00 43.71  ? 333  PRO C N   1 
ATOM   9686  C  CA  . PRO B  1 333 ? 17.811  8.953   55.662  1.00 42.66  ? 333  PRO C CA  1 
ATOM   9687  C  C   . PRO B  1 333 ? 16.364  9.155   55.253  1.00 43.80  ? 333  PRO C C   1 
ATOM   9688  O  O   . PRO B  1 333 ? 16.090  9.315   54.071  1.00 43.24  ? 333  PRO C O   1 
ATOM   9689  C  CB  . PRO B  1 333 ? 18.381  10.257  56.237  1.00 41.12  ? 333  PRO C CB  1 
ATOM   9690  C  CG  . PRO B  1 333 ? 19.718  10.412  55.611  1.00 40.51  ? 333  PRO C CG  1 
ATOM   9691  C  CD  . PRO B  1 333 ? 19.590  9.813   54.260  1.00 40.25  ? 333  PRO C CD  1 
ATOM   9692  N  N   . GLY B  1 334 ? 15.451  9.163   56.212  1.00 49.93  ? 334  GLY C N   1 
ATOM   9693  C  CA  . GLY B  1 334 ? 14.079  9.533   55.915  1.00 52.16  ? 334  GLY C CA  1 
ATOM   9694  C  C   . GLY B  1 334 ? 13.963  11.023  55.615  1.00 47.98  ? 334  GLY C C   1 
ATOM   9695  O  O   . GLY B  1 334 ? 13.046  11.450  54.908  1.00 45.06  ? 334  GLY C O   1 
ATOM   9696  N  N   . ALA B  1 335 ? 14.904  11.794  56.163  1.00 40.70  ? 335  ALA C N   1 
ATOM   9697  C  CA  . ALA B  1 335 ? 14.971  13.242  56.028  1.00 37.46  ? 335  ALA C CA  1 
ATOM   9698  C  C   . ALA B  1 335 ? 16.228  13.708  56.741  1.00 39.55  ? 335  ALA C C   1 
ATOM   9699  O  O   . ALA B  1 335 ? 16.863  12.905  57.419  1.00 45.00  ? 335  ALA C O   1 
ATOM   9700  C  CB  . ALA B  1 335 ? 13.757  13.901  56.604  1.00 36.57  ? 335  ALA C CB  1 
ATOM   9701  N  N   . MET B  1 336 ? 16.601  14.974  56.587  1.00 31.60  ? 336  MET C N   1 
ATOM   9702  C  CA  . MET B  1 336 ? 17.775  15.515  57.283  1.00 33.88  ? 336  MET C CA  1 
ATOM   9703  C  C   . MET B  1 336 ? 17.606  17.013  57.476  1.00 38.47  ? 336  MET C C   1 
ATOM   9704  O  O   . MET B  1 336 ? 17.096  17.687  56.590  1.00 41.24  ? 336  MET C O   1 
ATOM   9705  C  CB  . MET B  1 336 ? 19.062  15.240  56.515  1.00 38.10  ? 336  MET C CB  1 
ATOM   9706  C  CG  . MET B  1 336 ? 20.281  15.915  57.118  1.00 38.42  ? 336  MET C CG  1 
ATOM   9707  S  SD  . MET B  1 336 ? 20.574  15.341  58.819  1.00 40.59  ? 336  MET C SD  1 
ATOM   9708  C  CE  . MET B  1 336 ? 21.493  16.718  59.508  1.00 35.04  ? 336  MET C CE  1 
ATOM   9709  N  N   . GLU B  1 337 ? 18.061  17.539  58.609  1.00 36.46  ? 337  GLU C N   1 
ATOM   9710  C  CA  . GLU B  1 337 ? 17.587  18.847  59.079  1.00 38.44  ? 337  GLU C CA  1 
ATOM   9711  C  C   . GLU B  1 337 ? 18.516  20.028  58.796  1.00 39.10  ? 337  GLU C C   1 
ATOM   9712  O  O   . GLU B  1 337 ? 18.541  20.981  59.564  1.00 40.96  ? 337  GLU C O   1 
ATOM   9713  C  CB  . GLU B  1 337 ? 17.325  18.793  60.586  1.00 34.55  ? 337  GLU C CB  1 
ATOM   9714  C  CG  . GLU B  1 337 ? 18.592  18.650  61.430  1.00 39.42  ? 337  GLU C CG  1 
ATOM   9715  C  CD  . GLU B  1 337 ? 18.898  17.221  61.852  1.00 41.47  ? 337  GLU C CD  1 
ATOM   9716  O  OE1 . GLU B  1 337 ? 18.287  16.273  61.304  1.00 44.50  ? 337  GLU C OE1 1 
ATOM   9717  O  OE2 . GLU B  1 337 ? 19.764  17.050  62.739  1.00 38.89  ? 337  GLU C OE2 1 
ATOM   9718  N  N   . ASN B  1 338 ? 19.284  19.962  57.714  1.00 38.32  ? 338  ASN C N   1 
ATOM   9719  C  CA  . ASN B  1 338 ? 20.187  21.046  57.362  1.00 37.46  ? 338  ASN C CA  1 
ATOM   9720  C  C   . ASN B  1 338 ? 19.486  22.402  57.505  1.00 36.94  ? 338  ASN C C   1 
ATOM   9721  O  O   . ASN B  1 338 ? 18.378  22.603  57.011  1.00 36.19  ? 338  ASN C O   1 
ATOM   9722  C  CB  . ASN B  1 338 ? 20.711  20.835  55.947  1.00 39.63  ? 338  ASN C CB  1 
ATOM   9723  C  CG  . ASN B  1 338 ? 21.004  19.360  55.651  1.00 40.56  ? 338  ASN C CG  1 
ATOM   9724  O  OD1 . ASN B  1 338 ? 21.974  18.792  56.174  1.00 40.66  ? 338  ASN C OD1 1 
ATOM   9725  N  ND2 . ASN B  1 338 ? 20.167  18.738  54.811  1.00 31.66  ? 338  ASN C ND2 1 
ATOM   9726  N  N   . TRP B  1 339 ? 20.120  23.296  58.245  1.00 38.45  ? 339  TRP C N   1 
ATOM   9727  C  CA  . TRP B  1 339 ? 19.504  24.552  58.655  1.00 39.92  ? 339  TRP C CA  1 
ATOM   9728  C  C   . TRP B  1 339 ? 19.175  25.389  57.419  1.00 40.80  ? 339  TRP C C   1 
ATOM   9729  O  O   . TRP B  1 339 ? 20.086  25.856  56.740  1.00 35.95  ? 339  TRP C O   1 
ATOM   9730  C  CB  . TRP B  1 339 ? 20.451  25.292  59.600  1.00 38.23  ? 339  TRP C CB  1 
ATOM   9731  C  CG  . TRP B  1 339 ? 19.800  26.187  60.652  1.00 44.30  ? 339  TRP C CG  1 
ATOM   9732  C  CD1 . TRP B  1 339 ? 18.510  26.633  60.678  1.00 42.25  ? 339  TRP C CD1 1 
ATOM   9733  C  CD2 . TRP B  1 339 ? 20.439  26.741  61.820  1.00 41.80  ? 339  TRP C CD2 1 
ATOM   9734  N  NE1 . TRP B  1 339 ? 18.310  27.427  61.784  1.00 40.29  ? 339  TRP C NE1 1 
ATOM   9735  C  CE2 . TRP B  1 339 ? 19.475  27.503  62.501  1.00 40.96  ? 339  TRP C CE2 1 
ATOM   9736  C  CE3 . TRP B  1 339 ? 21.732  26.659  62.352  1.00 41.25  ? 339  TRP C CE3 1 
ATOM   9737  C  CZ2 . TRP B  1 339 ? 19.762  28.175  63.692  1.00 45.84  ? 339  TRP C CZ2 1 
ATOM   9738  C  CZ3 . TRP B  1 339 ? 22.019  27.336  63.527  1.00 43.68  ? 339  TRP C CZ3 1 
ATOM   9739  C  CH2 . TRP B  1 339 ? 21.044  28.083  64.183  1.00 46.06  ? 339  TRP C CH2 1 
ATOM   9740  N  N   . GLY B  1 340 ? 17.882  25.542  57.115  1.00 34.89  ? 340  GLY C N   1 
ATOM   9741  C  CA  . GLY B  1 340 ? 17.462  26.342  55.981  1.00 38.40  ? 340  GLY C CA  1 
ATOM   9742  C  C   . GLY B  1 340 ? 17.125  25.544  54.731  1.00 46.78  ? 340  GLY C C   1 
ATOM   9743  O  O   . GLY B  1 340 ? 16.331  25.989  53.873  1.00 39.18  ? 340  GLY C O   1 
ATOM   9744  N  N   . LEU B  1 341 ? 17.707  24.348  54.650  1.00 42.09  ? 341  LEU C N   1 
ATOM   9745  C  CA  . LEU B  1 341 ? 17.556  23.485  53.493  1.00 40.07  ? 341  LEU C CA  1 
ATOM   9746  C  C   . LEU B  1 341 ? 17.330  22.038  53.900  1.00 44.26  ? 341  LEU C C   1 
ATOM   9747  O  O   . LEU B  1 341 ? 18.293  21.275  54.069  1.00 38.59  ? 341  LEU C O   1 
ATOM   9748  C  CB  . LEU B  1 341 ? 18.802  23.590  52.627  1.00 38.98  ? 341  LEU C CB  1 
ATOM   9749  C  CG  . LEU B  1 341 ? 18.770  22.826  51.321  1.00 39.11  ? 341  LEU C CG  1 
ATOM   9750  C  CD1 . LEU B  1 341 ? 17.571  23.221  50.505  1.00 35.62  ? 341  LEU C CD1 1 
ATOM   9751  C  CD2 . LEU B  1 341 ? 20.065  23.085  50.594  1.00 37.40  ? 341  LEU C CD2 1 
ATOM   9752  N  N   . ILE B  1 342 ? 16.069  21.646  54.037  1.00 40.65  ? 342  ILE C N   1 
ATOM   9753  C  CA  . ILE B  1 342 ? 15.793  20.347  54.601  1.00 38.28  ? 342  ILE C CA  1 
ATOM   9754  C  C   . ILE B  1 342 ? 15.517  19.337  53.508  1.00 39.41  ? 342  ILE C C   1 
ATOM   9755  O  O   . ILE B  1 342 ? 14.626  19.520  52.678  1.00 40.93  ? 342  ILE C O   1 
ATOM   9756  C  CB  . ILE B  1 342 ? 14.600  20.387  55.586  1.00 48.79  ? 342  ILE C CB  1 
ATOM   9757  C  CG1 . ILE B  1 342 ? 14.805  21.478  56.651  1.00 42.36  ? 342  ILE C CG1 1 
ATOM   9758  C  CG2 . ILE B  1 342 ? 14.416  19.021  56.253  1.00 37.11  ? 342  ILE C CG2 1 
ATOM   9759  C  CD1 . ILE B  1 342 ? 13.536  21.867  57.332  1.00 38.03  ? 342  ILE C CD1 1 
ATOM   9760  N  N   . THR B  1 343 ? 16.286  18.256  53.544  1.00 34.80  ? 343  THR C N   1 
ATOM   9761  C  CA  . THR B  1 343 ? 16.219  17.197  52.551  1.00 39.04  ? 343  THR C CA  1 
ATOM   9762  C  C   . THR B  1 343 ? 15.347  16.024  53.016  1.00 39.90  ? 343  THR C C   1 
ATOM   9763  O  O   . THR B  1 343 ? 15.539  15.531  54.110  1.00 43.17  ? 343  THR C O   1 
ATOM   9764  C  CB  . THR B  1 343 ? 17.637  16.679  52.224  1.00 39.18  ? 343  THR C CB  1 
ATOM   9765  O  OG1 . THR B  1 343 ? 18.353  16.434  53.443  1.00 35.98  ? 343  THR C OG1 1 
ATOM   9766  C  CG2 . THR B  1 343 ? 18.398  17.695  51.439  1.00 36.83  ? 343  THR C CG2 1 
ATOM   9767  N  N   . TYR B  1 344 ? 14.412  15.593  52.170  1.00 38.99  ? 344  TYR C N   1 
ATOM   9768  C  CA  . TYR B  1 344 ? 13.459  14.527  52.459  1.00 36.99  ? 344  TYR C CA  1 
ATOM   9769  C  C   . TYR B  1 344 ? 13.480  13.439  51.392  1.00 46.02  ? 344  TYR C C   1 
ATOM   9770  O  O   . TYR B  1 344 ? 13.698  13.726  50.199  1.00 40.36  ? 344  TYR C O   1 
ATOM   9771  C  CB  . TYR B  1 344 ? 12.031  15.066  52.501  1.00 41.04  ? 344  TYR C CB  1 
ATOM   9772  C  CG  . TYR B  1 344 ? 11.725  16.068  53.575  1.00 42.21  ? 344  TYR C CG  1 
ATOM   9773  C  CD1 . TYR B  1 344 ? 12.132  17.392  53.456  1.00 45.50  ? 344  TYR C CD1 1 
ATOM   9774  C  CD2 . TYR B  1 344 ? 10.977  15.705  54.687  1.00 40.29  ? 344  TYR C CD2 1 
ATOM   9775  C  CE1 . TYR B  1 344 ? 11.830  18.319  54.428  1.00 44.42  ? 344  TYR C CE1 1 
ATOM   9776  C  CE2 . TYR B  1 344 ? 10.682  16.611  55.661  1.00 40.32  ? 344  TYR C CE2 1 
ATOM   9777  C  CZ  . TYR B  1 344 ? 11.111  17.921  55.535  1.00 48.19  ? 344  TYR C CZ  1 
ATOM   9778  O  OH  . TYR B  1 344 ? 10.812  18.834  56.527  1.00 51.01  ? 344  TYR C OH  1 
ATOM   9779  N  N   . ARG B  1 345 ? 13.213  12.202  51.809  1.00 42.02  ? 345  ARG C N   1 
ATOM   9780  C  CA  . ARG B  1 345 ? 12.719  11.199  50.884  1.00 40.58  ? 345  ARG C CA  1 
ATOM   9781  C  C   . ARG B  1 345 ? 11.460  11.756  50.276  1.00 42.36  ? 345  ARG C C   1 
ATOM   9782  O  O   . ARG B  1 345 ? 10.778  12.565  50.894  1.00 44.77  ? 345  ARG C O   1 
ATOM   9783  C  CB  . ARG B  1 345 ? 12.411  9.884   51.580  1.00 44.85  ? 345  ARG C CB  1 
ATOM   9784  C  CG  . ARG B  1 345 ? 13.434  8.817   51.348  1.00 47.19  ? 345  ARG C CG  1 
ATOM   9785  C  CD  . ARG B  1 345 ? 13.183  7.651   52.240  1.00 52.01  ? 345  ARG C CD  1 
ATOM   9786  N  NE  . ARG B  1 345 ? 14.414  6.927   52.524  1.00 53.97  ? 345  ARG C NE  1 
ATOM   9787  C  CZ  . ARG B  1 345 ? 14.664  5.698   52.105  1.00 49.16  ? 345  ARG C CZ  1 
ATOM   9788  N  NH1 . ARG B  1 345 ? 13.760  5.055   51.383  1.00 52.00  ? 345  ARG C NH1 1 
ATOM   9789  N  NH2 . ARG B  1 345 ? 15.810  5.123   52.419  1.00 44.50  ? 345  ARG C NH2 1 
ATOM   9790  N  N   . GLU B  1 346 ? 11.140  11.329  49.070  1.00 45.15  ? 346  GLU C N   1 
ATOM   9791  C  CA  . GLU B  1 346 ? 9.950   11.823  48.421  1.00 43.85  ? 346  GLU C CA  1 
ATOM   9792  C  C   . GLU B  1 346 ? 8.759   11.321  49.190  1.00 43.56  ? 346  GLU C C   1 
ATOM   9793  O  O   . GLU B  1 346 ? 7.828   12.076  49.448  1.00 48.82  ? 346  GLU C O   1 
ATOM   9794  C  CB  . GLU B  1 346 ? 9.904   11.382  46.958  1.00 42.55  ? 346  GLU C CB  1 
ATOM   9795  C  CG  . GLU B  1 346 ? 11.215  11.709  46.244  1.00 53.71  ? 346  GLU C CG  1 
ATOM   9796  C  CD  . GLU B  1 346 ? 11.093  11.787  44.741  1.00 54.31  ? 346  GLU C CD  1 
ATOM   9797  O  OE1 . GLU B  1 346 ? 10.458  12.746  44.242  1.00 51.88  ? 346  GLU C OE1 1 
ATOM   9798  O  OE2 . GLU B  1 346 ? 11.647  10.893  44.063  1.00 59.14  ? 346  GLU C OE2 1 
ATOM   9799  N  N   . THR B  1 347 ? 8.816   10.052  49.582  1.00 37.90  ? 347  THR C N   1 
ATOM   9800  C  CA  . THR B  1 347 ? 7.750   9.406   50.334  1.00 39.49  ? 347  THR C CA  1 
ATOM   9801  C  C   . THR B  1 347 ? 7.474   10.073  51.700  1.00 48.04  ? 347  THR C C   1 
ATOM   9802  O  O   . THR B  1 347 ? 6.431   9.859   52.307  1.00 55.30  ? 347  THR C O   1 
ATOM   9803  C  CB  . THR B  1 347 ? 8.095   7.932   50.568  1.00 44.66  ? 347  THR C CB  1 
ATOM   9804  O  OG1 . THR B  1 347 ? 9.466   7.847   50.963  1.00 49.61  ? 347  THR C OG1 1 
ATOM   9805  C  CG2 . THR B  1 347 ? 7.924   7.134   49.299  1.00 43.76  ? 347  THR C CG2 1 
ATOM   9806  N  N   . SER B  1 348 ? 8.440   10.821  52.200  1.00 39.66  ? 348  SER C N   1 
ATOM   9807  C  CA  . SER B  1 348 ? 8.267   11.494  53.464  1.00 38.00  ? 348  SER C CA  1 
ATOM   9808  C  C   . SER B  1 348 ? 7.988   12.992  53.337  1.00 47.38  ? 348  SER C C   1 
ATOM   9809  O  O   . SER B  1 348 ? 7.857   13.678  54.333  1.00 42.57  ? 348  SER C O   1 
ATOM   9810  C  CB  . SER B  1 348 ? 9.449   11.197  54.393  1.00 44.91  ? 348  SER C CB  1 
ATOM   9811  O  OG  . SER B  1 348 ? 10.521  12.079  54.190  1.00 41.84  ? 348  SER C OG  1 
ATOM   9812  N  N   . LEU B  1 349 ? 7.929   13.506  52.115  1.00 47.38  ? 349  LEU C N   1 
ATOM   9813  C  CA  . LEU B  1 349 ? 7.566   14.906  51.910  1.00 43.08  ? 349  LEU C CA  1 
ATOM   9814  C  C   . LEU B  1 349 ? 6.410   15.155  50.945  1.00 41.78  ? 349  LEU C C   1 
ATOM   9815  O  O   . LEU B  1 349 ? 5.715   16.147  51.050  1.00 50.19  ? 349  LEU C O   1 
ATOM   9816  C  CB  . LEU B  1 349 ? 8.786   15.731  51.495  1.00 43.17  ? 349  LEU C CB  1 
ATOM   9817  C  CG  . LEU B  1 349 ? 8.605   17.245  51.423  1.00 43.56  ? 349  LEU C CG  1 
ATOM   9818  C  CD1 . LEU B  1 349 ? 8.805   17.893  52.780  1.00 40.06  ? 349  LEU C CD1 1 
ATOM   9819  C  CD2 . LEU B  1 349 ? 9.529   17.860  50.396  1.00 30.02  ? 349  LEU C CD2 1 
ATOM   9820  N  N   . LEU B  1 350 ? 6.206   14.250  50.006  1.00 42.41  ? 350  LEU C N   1 
ATOM   9821  C  CA  . LEU B  1 350 ? 5.298   14.513  48.907  1.00 46.20  ? 350  LEU C CA  1 
ATOM   9822  C  C   . LEU B  1 350 ? 3.995   13.768  49.053  1.00 52.76  ? 350  LEU C C   1 
ATOM   9823  O  O   . LEU B  1 350 ? 3.974   12.572  49.304  1.00 56.06  ? 350  LEU C O   1 
ATOM   9824  C  CB  . LEU B  1 350 ? 5.949   14.145  47.578  1.00 51.60  ? 350  LEU C CB  1 
ATOM   9825  C  CG  . LEU B  1 350 ? 7.135   14.988  47.121  1.00 49.52  ? 350  LEU C CG  1 
ATOM   9826  C  CD1 . LEU B  1 350 ? 7.658   14.472  45.798  1.00 48.08  ? 350  LEU C CD1 1 
ATOM   9827  C  CD2 . LEU B  1 350 ? 6.741   16.445  47.004  1.00 46.81  ? 350  LEU C CD2 1 
ATOM   9828  N  N   . PHE B  1 351 ? 2.898   14.487  48.897  1.00 55.62  ? 351  PHE C N   1 
ATOM   9829  C  CA  . PHE B  1 351 ? 1.597   13.888  49.136  1.00 54.72  ? 351  PHE C CA  1 
ATOM   9830  C  C   . PHE B  1 351 ? 0.694   14.068  47.929  1.00 55.02  ? 351  PHE C C   1 
ATOM   9831  O  O   . PHE B  1 351 ? 0.405   15.180  47.528  1.00 58.92  ? 351  PHE C O   1 
ATOM   9832  C  CB  . PHE B  1 351 ? 0.944   14.491  50.388  1.00 57.97  ? 351  PHE C CB  1 
ATOM   9833  C  CG  . PHE B  1 351 ? -0.434  13.962  50.662  1.00 61.24  ? 351  PHE C CG  1 
ATOM   9834  C  CD1 . PHE B  1 351 ? -0.609  12.718  51.240  1.00 66.88  ? 351  PHE C CD1 1 
ATOM   9835  C  CD2 . PHE B  1 351 ? -1.557  14.706  50.339  1.00 61.27  ? 351  PHE C CD2 1 
ATOM   9836  C  CE1 . PHE B  1 351 ? -1.881  12.216  51.486  1.00 69.05  ? 351  PHE C CE1 1 
ATOM   9837  C  CE2 . PHE B  1 351 ? -2.826  14.210  50.576  1.00 65.43  ? 351  PHE C CE2 1 
ATOM   9838  C  CZ  . PHE B  1 351 ? -2.986  12.963  51.149  1.00 73.57  ? 351  PHE C CZ  1 
ATOM   9839  N  N   . ASP B  1 352 ? 0.258   12.955  47.357  1.00 63.11  ? 352  ASP C N   1 
ATOM   9840  C  CA  . ASP B  1 352 ? -0.645  12.958  46.216  1.00 66.45  ? 352  ASP C CA  1 
ATOM   9841  C  C   . ASP B  1 352 ? -1.900  12.145  46.530  1.00 71.76  ? 352  ASP C C   1 
ATOM   9842  O  O   . ASP B  1 352 ? -1.878  10.908  46.511  1.00 68.39  ? 352  ASP C O   1 
ATOM   9843  C  CB  . ASP B  1 352 ? 0.046   12.398  44.973  1.00 66.26  ? 352  ASP C CB  1 
ATOM   9844  C  CG  . ASP B  1 352 ? -0.936  12.078  43.863  1.00 75.48  ? 352  ASP C CG  1 
ATOM   9845  O  OD1 . ASP B  1 352 ? -1.866  12.888  43.646  1.00 75.57  ? 352  ASP C OD1 1 
ATOM   9846  O  OD2 . ASP B  1 352 ? -0.790  11.012  43.223  1.00 77.09  ? 352  ASP C OD2 1 
ATOM   9847  N  N   . PRO B  1 353 ? -3.009  12.847  46.780  1.00 68.77  ? 353  PRO C N   1 
ATOM   9848  C  CA  . PRO B  1 353 ? -4.269  12.322  47.322  1.00 71.79  ? 353  PRO C CA  1 
ATOM   9849  C  C   . PRO B  1 353 ? -4.979  11.280  46.454  1.00 74.07  ? 353  PRO C C   1 
ATOM   9850  O  O   . PRO B  1 353 ? -6.141  10.978  46.714  1.00 75.75  ? 353  PRO C O   1 
ATOM   9851  C  CB  . PRO B  1 353 ? -5.142  13.578  47.448  1.00 79.35  ? 353  PRO C CB  1 
ATOM   9852  C  CG  . PRO B  1 353 ? -4.176  14.743  47.395  1.00 78.68  ? 353  PRO C CG  1 
ATOM   9853  C  CD  . PRO B  1 353 ? -3.085  14.289  46.498  1.00 69.39  ? 353  PRO C CD  1 
ATOM   9854  N  N   . LYS B  1 354 ? -4.306  10.739  45.446  1.00 76.00  ? 354  LYS C N   1 
ATOM   9855  C  CA  . LYS B  1 354 ? -4.920  9.723   44.602  1.00 72.55  ? 354  LYS C CA  1 
ATOM   9856  C  C   . LYS B  1 354 ? -4.293  8.362   44.898  1.00 72.45  ? 354  LYS C C   1 
ATOM   9857  O  O   . LYS B  1 354 ? -4.896  7.315   44.681  1.00 76.25  ? 354  LYS C O   1 
ATOM   9858  C  CB  . LYS B  1 354 ? -4.768  10.097  43.124  1.00 72.93  ? 354  LYS C CB  1 
ATOM   9859  C  CG  . LYS B  1 354 ? -5.401  9.111   42.158  1.00 82.02  ? 354  LYS C CG  1 
ATOM   9860  C  CD  . LYS B  1 354 ? -5.341  9.609   40.726  1.00 86.97  ? 354  LYS C CD  1 
ATOM   9861  C  CE  . LYS B  1 354 ? -5.844  8.554   39.755  1.00 92.70  ? 354  LYS C CE  1 
ATOM   9862  N  NZ  . LYS B  1 354 ? -5.841  9.062   38.355  1.00 99.27  ? 354  LYS C NZ  1 
ATOM   9863  N  N   . THR B  1 355 ? -3.075  8.395   45.422  1.00 74.43  ? 355  THR C N   1 
ATOM   9864  C  CA  . THR B  1 355 ? -2.308  7.188   45.697  1.00 71.51  ? 355  THR C CA  1 
ATOM   9865  C  C   . THR B  1 355 ? -1.716  7.242   47.098  1.00 77.80  ? 355  THR C C   1 
ATOM   9866  O  O   . THR B  1 355 ? -1.090  6.278   47.552  1.00 80.20  ? 355  THR C O   1 
ATOM   9867  C  CB  . THR B  1 355 ? -1.166  7.003   44.683  1.00 77.50  ? 355  THR C CB  1 
ATOM   9868  O  OG1 . THR B  1 355 ? -0.405  8.221   44.603  1.00 74.36  ? 355  THR C OG1 1 
ATOM   9869  C  CG2 . THR B  1 355 ? -1.720  6.645   43.301  1.00 70.56  ? 355  THR C CG2 1 
ATOM   9870  N  N   . SER B  1 356 ? -1.898  8.379   47.768  1.00 68.66  ? 356  SER C N   1 
ATOM   9871  C  CA  . SER B  1 356 ? -1.439  8.544   49.140  1.00 69.50  ? 356  SER C CA  1 
ATOM   9872  C  C   . SER B  1 356 ? -2.611  8.423   50.128  1.00 74.94  ? 356  SER C C   1 
ATOM   9873  O  O   . SER B  1 356 ? -3.698  8.953   49.891  1.00 79.92  ? 356  SER C O   1 
ATOM   9874  C  CB  . SER B  1 356 ? -0.729  9.889   49.311  1.00 70.19  ? 356  SER C CB  1 
ATOM   9875  O  OG  . SER B  1 356 ? 0.563   9.886   48.733  1.00 60.96  ? 356  SER C OG  1 
ATOM   9876  N  N   . SER B  1 357 ? -2.376  7.732   51.239  1.00 68.36  ? 357  SER C N   1 
ATOM   9877  C  CA  . SER B  1 357 ? -3.431  7.413   52.189  1.00 66.56  ? 357  SER C CA  1 
ATOM   9878  C  C   . SER B  1 357 ? -3.349  8.226   53.473  1.00 67.75  ? 357  SER C C   1 
ATOM   9879  O  O   . SER B  1 357 ? -2.540  9.150   53.604  1.00 65.30  ? 357  SER C O   1 
ATOM   9880  C  CB  . SER B  1 357 ? -3.384  5.935   52.535  1.00 67.56  ? 357  SER C CB  1 
ATOM   9881  O  OG  . SER B  1 357 ? -2.180  5.643   53.212  1.00 66.56  ? 357  SER C OG  1 
ATOM   9882  N  N   . ALA B  1 358 ? -4.194  7.858   54.426  1.00 71.87  ? 358  ALA C N   1 
ATOM   9883  C  CA  . ALA B  1 358 ? -4.251  8.538   55.715  1.00 73.15  ? 358  ALA C CA  1 
ATOM   9884  C  C   . ALA B  1 358 ? -2.967  8.353   56.525  1.00 63.79  ? 358  ALA C C   1 
ATOM   9885  O  O   . ALA B  1 358 ? -2.459  9.311   57.123  1.00 57.49  ? 358  ALA C O   1 
ATOM   9886  C  CB  . ALA B  1 358 ? -5.451  8.045   56.506  1.00 78.73  ? 358  ALA C CB  1 
ATOM   9887  N  N   . SER B  1 359 ? -2.446  7.125   56.541  1.00 60.77  ? 359  SER C N   1 
ATOM   9888  C  CA  . SER B  1 359 ? -1.196  6.855   57.238  1.00 64.19  ? 359  SER C CA  1 
ATOM   9889  C  C   . SER B  1 359 ? -0.101  7.689   56.595  1.00 63.77  ? 359  SER C C   1 
ATOM   9890  O  O   . SER B  1 359 ? 0.667   8.372   57.287  1.00 58.84  ? 359  SER C O   1 
ATOM   9891  C  CB  . SER B  1 359 ? -0.836  5.369   57.200  1.00 67.44  ? 359  SER C CB  1 
ATOM   9892  O  OG  . SER B  1 359 ? -0.588  4.938   55.872  1.00 76.75  ? 359  SER C OG  1 
ATOM   9893  N  N   . ASP B  1 360 ? -0.055  7.648   55.265  1.00 61.41  ? 360  ASP C N   1 
ATOM   9894  C  CA  . ASP B  1 360 ? 0.892   8.451   54.510  1.00 59.31  ? 360  ASP C CA  1 
ATOM   9895  C  C   . ASP B  1 360 ? 0.870   9.899   54.965  1.00 53.05  ? 360  ASP C C   1 
ATOM   9896  O  O   . ASP B  1 360 ? 1.903   10.438  55.355  1.00 49.47  ? 360  ASP C O   1 
ATOM   9897  C  CB  . ASP B  1 360 ? 0.595   8.362   53.021  1.00 64.23  ? 360  ASP C CB  1 
ATOM   9898  C  CG  . ASP B  1 360 ? 1.017   7.043   52.431  1.00 68.74  ? 360  ASP C CG  1 
ATOM   9899  O  OD1 . ASP B  1 360 ? 1.906   6.384   53.016  1.00 79.10  ? 360  ASP C OD1 1 
ATOM   9900  O  OD2 . ASP B  1 360 ? 0.461   6.660   51.385  1.00 70.47  ? 360  ASP C OD2 1 
ATOM   9901  N  N   . LYS B  1 361 ? -0.312  10.509  54.937  1.00 54.32  ? 361  LYS C N   1 
ATOM   9902  C  CA  . LYS B  1 361 ? -0.482  11.881  55.400  1.00 54.42  ? 361  LYS C CA  1 
ATOM   9903  C  C   . LYS B  1 361 ? 0.135   12.080  56.777  1.00 58.01  ? 361  LYS C C   1 
ATOM   9904  O  O   . LYS B  1 361 ? 0.849   13.070  57.034  1.00 54.41  ? 361  LYS C O   1 
ATOM   9905  C  CB  . LYS B  1 361 ? -1.961  12.254  55.438  1.00 59.32  ? 361  LYS C CB  1 
ATOM   9906  C  CG  . LYS B  1 361 ? -2.218  13.755  55.558  1.00 62.18  ? 361  LYS C CG  1 
ATOM   9907  C  CD  . LYS B  1 361 ? -3.189  14.186  54.476  1.00 66.94  ? 361  LYS C CD  1 
ATOM   9908  C  CE  . LYS B  1 361 ? -3.308  15.690  54.399  1.00 73.87  ? 361  LYS C CE  1 
ATOM   9909  N  NZ  . LYS B  1 361 ? -3.770  16.300  55.680  1.00 73.30  ? 361  LYS C NZ  1 
ATOM   9910  N  N   . LEU B  1 362 ? -0.141  11.121  57.657  1.00 54.52  ? 362  LEU C N   1 
ATOM   9911  C  CA  . LEU B  1 362 ? 0.392   11.147  59.009  1.00 56.62  ? 362  LEU C CA  1 
ATOM   9912  C  C   . LEU B  1 362 ? 1.912   11.067  59.003  1.00 54.71  ? 362  LEU C C   1 
ATOM   9913  O  O   . LEU B  1 362 ? 2.597   11.790  59.735  1.00 49.19  ? 362  LEU C O   1 
ATOM   9914  C  CB  . LEU B  1 362 ? -0.197  10.002  59.820  1.00 58.45  ? 362  LEU C CB  1 
ATOM   9915  C  CG  . LEU B  1 362 ? 0.234   9.866   61.271  1.00 63.79  ? 362  LEU C CG  1 
ATOM   9916  C  CD1 . LEU B  1 362 ? 0.090   11.190  62.049  1.00 60.73  ? 362  LEU C CD1 1 
ATOM   9917  C  CD2 . LEU B  1 362 ? -0.595  8.763   61.896  1.00 64.99  ? 362  LEU C CD2 1 
ATOM   9918  N  N   . TRP B  1 363 ? 2.441   10.197  58.152  1.00 57.50  ? 363  TRP C N   1 
ATOM   9919  C  CA  . TRP B  1 363 ? 3.882   10.050  58.055  1.00 53.55  ? 363  TRP C CA  1 
ATOM   9920  C  C   . TRP B  1 363 ? 4.530   11.344  57.581  1.00 51.00  ? 363  TRP C C   1 
ATOM   9921  O  O   . TRP B  1 363 ? 5.564   11.755  58.110  1.00 55.34  ? 363  TRP C O   1 
ATOM   9922  C  CB  . TRP B  1 363 ? 4.249   8.897   57.131  1.00 49.87  ? 363  TRP C CB  1 
ATOM   9923  C  CG  . TRP B  1 363 ? 5.718   8.746   56.964  1.00 56.48  ? 363  TRP C CG  1 
ATOM   9924  C  CD1 . TRP B  1 363 ? 6.414   8.807   55.798  1.00 57.18  ? 363  TRP C CD1 1 
ATOM   9925  C  CD2 . TRP B  1 363 ? 6.687   8.521   57.997  1.00 63.56  ? 363  TRP C CD2 1 
ATOM   9926  N  NE1 . TRP B  1 363 ? 7.750   8.627   56.034  1.00 55.57  ? 363  TRP C NE1 1 
ATOM   9927  C  CE2 . TRP B  1 363 ? 7.947   8.448   57.377  1.00 62.20  ? 363  TRP C CE2 1 
ATOM   9928  C  CE3 . TRP B  1 363 ? 6.611   8.367   59.383  1.00 61.21  ? 363  TRP C CE3 1 
ATOM   9929  C  CZ2 . TRP B  1 363 ? 9.124   8.232   58.096  1.00 60.01  ? 363  TRP C CZ2 1 
ATOM   9930  C  CZ3 . TRP B  1 363 ? 7.778   8.159   60.093  1.00 57.26  ? 363  TRP C CZ3 1 
ATOM   9931  C  CH2 . TRP B  1 363 ? 9.015   8.091   59.450  1.00 61.10  ? 363  TRP C CH2 1 
ATOM   9932  N  N   . VAL B  1 364 ? 3.917   12.008  56.612  1.00 44.78  ? 364  VAL C N   1 
ATOM   9933  C  CA  . VAL B  1 364 ? 4.492   13.257  56.118  1.00 53.52  ? 364  VAL C CA  1 
ATOM   9934  C  C   . VAL B  1 364 ? 4.500   14.324  57.205  1.00 49.87  ? 364  VAL C C   1 
ATOM   9935  O  O   . VAL B  1 364 ? 5.519   15.000  57.462  1.00 44.54  ? 364  VAL C O   1 
ATOM   9936  C  CB  . VAL B  1 364 ? 3.735   13.774  54.890  1.00 51.73  ? 364  VAL C CB  1 
ATOM   9937  C  CG1 . VAL B  1 364 ? 4.033   15.240  54.656  1.00 46.82  ? 364  VAL C CG1 1 
ATOM   9938  C  CG2 . VAL B  1 364 ? 4.119   12.949  53.685  1.00 47.15  ? 364  VAL C CG2 1 
ATOM   9939  N  N   . THR B  1 365 ? 3.361   14.438  57.870  1.00 55.68  ? 365  THR C N   1 
ATOM   9940  C  CA  . THR B  1 365 ? 3.198   15.432  58.915  1.00 53.32  ? 365  THR C CA  1 
ATOM   9941  C  C   . THR B  1 365 ? 4.172   15.212  60.083  1.00 49.64  ? 365  THR C C   1 
ATOM   9942  O  O   . THR B  1 365 ? 4.694   16.186  60.653  1.00 47.03  ? 365  THR C O   1 
ATOM   9943  C  CB  . THR B  1 365 ? 1.761   15.433  59.409  1.00 52.54  ? 365  THR C CB  1 
ATOM   9944  O  OG1 . THR B  1 365 ? 0.883   15.149  58.308  1.00 52.03  ? 365  THR C OG1 1 
ATOM   9945  C  CG2 . THR B  1 365 ? 1.421   16.775  59.991  1.00 52.36  ? 365  THR C CG2 1 
ATOM   9946  N  N   . ARG B  1 366 ? 4.442   13.949  60.424  1.00 47.10  ? 366  ARG C N   1 
ATOM   9947  C  CA  . ARG B  1 366 ? 5.437   13.647  61.471  1.00 47.65  ? 366  ARG C CA  1 
ATOM   9948  C  C   . ARG B  1 366 ? 6.806   14.170  61.093  1.00 47.24  ? 366  ARG C C   1 
ATOM   9949  O  O   . ARG B  1 366 ? 7.444   14.925  61.865  1.00 41.69  ? 366  ARG C O   1 
ATOM   9950  C  CB  . ARG B  1 366 ? 5.566   12.142  61.736  1.00 56.48  ? 366  ARG C CB  1 
ATOM   9951  C  CG  . ARG B  1 366 ? 4.454   11.503  62.517  1.00 57.53  ? 366  ARG C CG  1 
ATOM   9952  C  CD  . ARG B  1 366 ? 4.737   10.017  62.678  1.00 68.25  ? 366  ARG C CD  1 
ATOM   9953  N  NE  . ARG B  1 366 ? 5.677   9.739   63.764  1.00 74.13  ? 366  ARG C NE  1 
ATOM   9954  C  CZ  . ARG B  1 366 ? 6.165   8.531   64.038  0.98 78.88  ? 366  ARG C CZ  1 
ATOM   9955  N  NH1 . ARG B  1 366 ? 5.815   7.479   63.304  1.00 77.19  ? 366  ARG C NH1 1 
ATOM   9956  N  NH2 . ARG B  1 366 ? 6.998   8.362   65.054  1.00 75.07  ? 366  ARG C NH2 1 
ATOM   9957  N  N   . VAL B  1 367 ? 7.249   13.748  59.902  1.00 46.28  ? 367  VAL C N   1 
ATOM   9958  C  CA  . VAL B  1 367 ? 8.602   14.028  59.439  1.00 41.43  ? 367  VAL C CA  1 
ATOM   9959  C  C   . VAL B  1 367 ? 8.811   15.520  59.324  1.00 40.87  ? 367  VAL C C   1 
ATOM   9960  O  O   . VAL B  1 367 ? 9.841   16.030  59.754  1.00 42.95  ? 367  VAL C O   1 
ATOM   9961  C  CB  . VAL B  1 367 ? 8.924   13.365  58.077  1.00 46.05  ? 367  VAL C CB  1 
ATOM   9962  C  CG1 . VAL B  1 367 ? 10.366  13.682  57.678  1.00 40.80  ? 367  VAL C CG1 1 
ATOM   9963  C  CG2 . VAL B  1 367 ? 8.707   11.857  58.135  1.00 41.45  ? 367  VAL C CG2 1 
ATOM   9964  N  N   . ILE B  1 368 ? 7.842   16.233  58.764  1.00 43.07  ? 368  ILE C N   1 
ATOM   9965  C  CA  . ILE B  1 368 ? 7.995   17.681  58.706  1.00 49.00  ? 368  ILE C CA  1 
ATOM   9966  C  C   . ILE B  1 368 ? 8.135   18.240  60.121  1.00 42.42  ? 368  ILE C C   1 
ATOM   9967  O  O   . ILE B  1 368 ? 9.076   18.987  60.416  1.00 45.91  ? 368  ILE C O   1 
ATOM   9968  C  CB  . ILE B  1 368 ? 6.825   18.372  57.989  1.00 50.45  ? 368  ILE C CB  1 
ATOM   9969  C  CG1 . ILE B  1 368 ? 6.711   17.869  56.545  1.00 43.54  ? 368  ILE C CG1 1 
ATOM   9970  C  CG2 . ILE B  1 368 ? 7.028   19.886  58.024  1.00 44.33  ? 368  ILE C CG2 1 
ATOM   9971  C  CD1 . ILE B  1 368 ? 5.531   18.437  55.794  1.00 47.40  ? 368  ILE C CD1 1 
ATOM   9972  N  N   . ALA B  1 369 ? 7.218   17.851  61.001  1.00 45.34  ? 369  ALA C N   1 
ATOM   9973  C  CA  . ALA B  1 369 ? 7.264   18.297  62.391  1.00 44.81  ? 369  ALA C CA  1 
ATOM   9974  C  C   . ALA B  1 369 ? 8.600   17.938  63.029  1.00 42.01  ? 369  ALA C C   1 
ATOM   9975  O  O   . ALA B  1 369 ? 9.209   18.759  63.709  1.00 42.89  ? 369  ALA C O   1 
ATOM   9976  C  CB  . ALA B  1 369 ? 6.132   17.693  63.172  1.00 49.86  ? 369  ALA C CB  1 
ATOM   9977  N  N   . HIS B  1 370 ? 9.060   16.712  62.796  1.00 43.71  ? 370  HIS C N   1 
ATOM   9978  C  CA  . HIS B  1 370 ? 10.348  16.275  63.343  1.00 46.41  ? 370  HIS C CA  1 
ATOM   9979  C  C   . HIS B  1 370 ? 11.465  17.189  62.841  1.00 44.86  ? 370  HIS C C   1 
ATOM   9980  O  O   . HIS B  1 370 ? 12.306  17.648  63.615  1.00 46.36  ? 370  HIS C O   1 
ATOM   9981  C  CB  . HIS B  1 370 ? 10.634  14.802  62.970  1.00 35.83  ? 370  HIS C CB  1 
ATOM   9982  C  CG  . HIS B  1 370 ? 11.943  14.285  63.482  1.00 38.20  ? 370  HIS C CG  1 
ATOM   9983  N  ND1 . HIS B  1 370 ? 12.032  13.432  64.561  1.00 49.79  ? 370  HIS C ND1 1 
ATOM   9984  C  CD2 . HIS B  1 370 ? 13.215  14.503  63.073  1.00 40.01  ? 370  HIS C CD2 1 
ATOM   9985  C  CE1 . HIS B  1 370 ? 13.302  13.142  64.788  1.00 42.32  ? 370  HIS C CE1 1 
ATOM   9986  N  NE2 . HIS B  1 370 ? 14.037  13.770  63.892  1.00 34.28  ? 370  HIS C NE2 1 
ATOM   9987  N  N   . GLU B  1 371 ? 11.450  17.478  61.545  1.00 37.92  ? 371  GLU C N   1 
ATOM   9988  C  CA  . GLU B  1 371 ? 12.558  18.194  60.934  1.00 41.46  ? 371  GLU C CA  1 
ATOM   9989  C  C   . GLU B  1 371 ? 12.557  19.667  61.300  1.00 38.38  ? 371  GLU C C   1 
ATOM   9990  O  O   . GLU B  1 371 ? 13.628  20.256  61.490  1.00 37.89  ? 371  GLU C O   1 
ATOM   9991  C  CB  . GLU B  1 371 ? 12.546  18.020  59.395  1.00 37.55  ? 371  GLU C CB  1 
ATOM   9992  C  CG  . GLU B  1 371 ? 12.829  16.592  58.964  1.00 34.60  ? 371  GLU C CG  1 
ATOM   9993  C  CD  . GLU B  1 371 ? 14.108  16.035  59.592  1.00 41.35  ? 371  GLU C CD  1 
ATOM   9994  O  OE1 . GLU B  1 371 ? 15.139  16.744  59.572  1.00 42.59  ? 371  GLU C OE1 1 
ATOM   9995  O  OE2 . GLU B  1 371 ? 14.089  14.897  60.114  1.00 38.44  ? 371  GLU C OE2 1 
ATOM   9996  N  N   . LEU B  1 372 ? 11.379  20.277  61.388  1.00 38.10  ? 372  LEU C N   1 
ATOM   9997  C  CA  . LEU B  1 372 ? 11.360  21.691  61.760  1.00 46.54  ? 372  LEU C CA  1 
ATOM   9998  C  C   . LEU B  1 372 ? 11.836  21.847  63.216  1.00 40.20  ? 372  LEU C C   1 
ATOM   9999  O  O   . LEU B  1 372 ? 12.635  22.740  63.515  1.00 35.32  ? 372  LEU C O   1 
ATOM   10000 C  CB  . LEU B  1 372 ? 9.972   22.304  61.542  1.00 46.69  ? 372  LEU C CB  1 
ATOM   10001 C  CG  . LEU B  1 372 ? 9.491   22.298  60.082  1.00 53.58  ? 372  LEU C CG  1 
ATOM   10002 C  CD1 . LEU B  1 372 ? 8.125   22.956  59.901  1.00 46.96  ? 372  LEU C CD1 1 
ATOM   10003 C  CD2 . LEU B  1 372 ? 10.513  22.964  59.181  1.00 52.02  ? 372  LEU C CD2 1 
ATOM   10004 N  N   . ALA B  1 373 ? 11.399  20.933  64.090  1.00 39.33  ? 373  ALA C N   1 
ATOM   10005 C  CA  . ALA B  1 373 ? 11.760  20.964  65.516  1.00 44.54  ? 373  ALA C CA  1 
ATOM   10006 C  C   . ALA B  1 373 ? 13.274  20.948  65.721  1.00 45.67  ? 373  ALA C C   1 
ATOM   10007 O  O   . ALA B  1 373 ? 13.826  21.581  66.650  1.00 39.89  ? 373  ALA C O   1 
ATOM   10008 C  CB  . ALA B  1 373 ? 11.121  19.790  66.249  1.00 43.40  ? 373  ALA C CB  1 
ATOM   10009 N  N   . HIS B  1 374 ? 13.936  20.203  64.838  1.00 43.80  ? 374  HIS C N   1 
ATOM   10010 C  CA  . HIS B  1 374 ? 15.389  20.154  64.788  1.00 36.95  ? 374  HIS C CA  1 
ATOM   10011 C  C   . HIS B  1 374 ? 16.054  21.532  64.557  1.00 42.79  ? 374  HIS C C   1 
ATOM   10012 O  O   . HIS B  1 374 ? 17.218  21.748  64.972  1.00 38.23  ? 374  HIS C O   1 
ATOM   10013 C  CB  . HIS B  1 374 ? 15.806  19.219  63.677  1.00 38.21  ? 374  HIS C CB  1 
ATOM   10014 C  CG  . HIS B  1 374 ? 16.178  17.838  64.112  1.00 41.27  ? 374  HIS C CG  1 
ATOM   10015 N  ND1 . HIS B  1 374 ? 17.096  17.588  65.110  1.00 49.00  ? 374  HIS C ND1 1 
ATOM   10016 C  CD2 . HIS B  1 374 ? 15.819  16.629  63.620  1.00 37.94  ? 374  HIS C CD2 1 
ATOM   10017 C  CE1 . HIS B  1 374 ? 17.259  16.284  65.236  1.00 44.47  ? 374  HIS C CE1 1 
ATOM   10018 N  NE2 . HIS B  1 374 ? 16.511  15.683  64.330  1.00 39.06  ? 374  HIS C NE2 1 
ATOM   10019 N  N   . GLN B  1 375 ? 15.347  22.453  63.881  1.00 33.49  ? 375  GLN C N   1 
ATOM   10020 C  CA  . GLN B  1 375 ? 15.937  23.760  63.622  1.00 40.49  ? 375  GLN C CA  1 
ATOM   10021 C  C   . GLN B  1 375 ? 16.383  24.410  64.943  1.00 42.85  ? 375  GLN C C   1 
ATOM   10022 O  O   . GLN B  1 375 ? 17.407  25.099  65.000  1.00 37.87  ? 375  GLN C O   1 
ATOM   10023 C  CB  . GLN B  1 375 ? 14.967  24.663  62.857  1.00 43.35  ? 375  GLN C CB  1 
ATOM   10024 C  CG  . GLN B  1 375 ? 14.580  24.155  61.452  1.00 41.75  ? 375  GLN C CG  1 
ATOM   10025 C  CD  . GLN B  1 375 ? 15.787  23.809  60.561  1.00 41.11  ? 375  GLN C CD  1 
ATOM   10026 O  OE1 . GLN B  1 375 ? 16.501  24.691  60.084  1.00 48.10  ? 375  GLN C OE1 1 
ATOM   10027 N  NE2 . GLN B  1 375 ? 16.004  22.523  60.335  1.00 35.19  ? 375  GLN C NE2 1 
ATOM   10028 N  N   . TRP B  1 376 ? 15.646  24.125  66.017  1.00 47.82  ? 376  TRP C N   1 
ATOM   10029 C  CA  . TRP B  1 376 ? 16.031  24.557  67.364  1.00 46.14  ? 376  TRP C CA  1 
ATOM   10030 C  C   . TRP B  1 376 ? 16.804  23.476  68.151  1.00 42.19  ? 376  TRP C C   1 
ATOM   10031 O  O   . TRP B  1 376 ? 17.920  23.717  68.646  1.00 38.89  ? 376  TRP C O   1 
ATOM   10032 C  CB  . TRP B  1 376 ? 14.789  24.969  68.146  1.00 53.45  ? 376  TRP C CB  1 
ATOM   10033 C  CG  . TRP B  1 376 ? 14.116  26.234  67.680  1.00 48.88  ? 376  TRP C CG  1 
ATOM   10034 C  CD1 . TRP B  1 376 ? 14.249  27.481  68.225  1.00 52.37  ? 376  TRP C CD1 1 
ATOM   10035 C  CD2 . TRP B  1 376 ? 13.168  26.363  66.620  1.00 50.64  ? 376  TRP C CD2 1 
ATOM   10036 N  NE1 . TRP B  1 376 ? 13.455  28.380  67.562  1.00 50.04  ? 376  TRP C NE1 1 
ATOM   10037 C  CE2 . TRP B  1 376 ? 12.780  27.723  66.571  1.00 54.27  ? 376  TRP C CE2 1 
ATOM   10038 C  CE3 . TRP B  1 376 ? 12.626  25.473  65.692  1.00 48.13  ? 376  TRP C CE3 1 
ATOM   10039 C  CZ2 . TRP B  1 376 ? 11.869  28.204  65.638  1.00 54.41  ? 376  TRP C CZ2 1 
ATOM   10040 C  CZ3 . TRP B  1 376 ? 11.716  25.954  64.765  1.00 52.74  ? 376  TRP C CZ3 1 
ATOM   10041 C  CH2 . TRP B  1 376 ? 11.345  27.305  64.747  1.00 59.56  ? 376  TRP C CH2 1 
ATOM   10042 N  N   . PHE B  1 377 ? 16.209  22.287  68.261  1.00 44.55  ? 377  PHE C N   1 
ATOM   10043 C  CA  . PHE B  1 377 ? 16.849  21.164  68.964  1.00 44.74  ? 377  PHE C CA  1 
ATOM   10044 C  C   . PHE B  1 377 ? 17.749  20.397  68.032  1.00 45.44  ? 377  PHE C C   1 
ATOM   10045 O  O   . PHE B  1 377 ? 17.338  19.383  67.442  1.00 40.56  ? 377  PHE C O   1 
ATOM   10046 C  CB  . PHE B  1 377 ? 15.829  20.183  69.549  1.00 47.21  ? 377  PHE C CB  1 
ATOM   10047 C  CG  . PHE B  1 377 ? 15.029  20.735  70.667  1.00 47.01  ? 377  PHE C CG  1 
ATOM   10048 C  CD1 . PHE B  1 377 ? 15.633  21.058  71.866  1.00 47.79  ? 377  PHE C CD1 1 
ATOM   10049 C  CD2 . PHE B  1 377 ? 13.663  20.914  70.523  1.00 51.29  ? 377  PHE C CD2 1 
ATOM   10050 C  CE1 . PHE B  1 377 ? 14.892  21.576  72.899  1.00 58.56  ? 377  PHE C CE1 1 
ATOM   10051 C  CE2 . PHE B  1 377 ? 12.911  21.426  71.549  1.00 58.49  ? 377  PHE C CE2 1 
ATOM   10052 C  CZ  . PHE B  1 377 ? 13.524  21.767  72.741  1.00 61.38  ? 377  PHE C CZ  1 
ATOM   10053 N  N   . GLY B  1 378 ? 18.981  20.861  67.915  1.00 42.52  ? 378  GLY C N   1 
ATOM   10054 C  CA  . GLY B  1 378 ? 19.875  20.336  66.912  1.00 38.71  ? 378  GLY C CA  1 
ATOM   10055 C  C   . GLY B  1 378 ? 20.661  21.459  66.273  1.00 43.79  ? 378  GLY C C   1 
ATOM   10056 O  O   . GLY B  1 378 ? 21.889  21.499  66.415  1.00 43.81  ? 378  GLY C O   1 
ATOM   10057 N  N   . ASN B  1 379 ? 19.976  22.376  65.581  1.00 40.07  ? 379  ASN C N   1 
ATOM   10058 C  CA  . ASN B  1 379 ? 20.695  23.422  64.852  1.00 48.88  ? 379  ASN C CA  1 
ATOM   10059 C  C   . ASN B  1 379 ? 21.016  24.613  65.747  1.00 44.91  ? 379  ASN C C   1 
ATOM   10060 O  O   . ASN B  1 379 ? 22.193  24.912  65.985  1.00 44.10  ? 379  ASN C O   1 
ATOM   10061 C  CB  . ASN B  1 379 ? 19.913  23.873  63.613  1.00 47.46  ? 379  ASN C CB  1 
ATOM   10062 C  CG  . ASN B  1 379 ? 19.575  22.719  62.700  1.00 44.62  ? 379  ASN C CG  1 
ATOM   10063 O  OD1 . ASN B  1 379 ? 20.045  21.609  62.924  1.00 50.87  ? 379  ASN C OD1 1 
ATOM   10064 N  ND2 . ASN B  1 379 ? 18.741  22.959  61.682  1.00 40.39  ? 379  ASN C ND2 1 
ATOM   10065 N  N   . LEU B  1 380 ? 19.968  25.278  66.236  1.00 46.77  ? 380  LEU C N   1 
ATOM   10066 C  CA  . LEU B  1 380 ? 20.110  26.314  67.262  1.00 42.19  ? 380  LEU C CA  1 
ATOM   10067 C  C   . LEU B  1 380 ? 20.831  25.755  68.475  1.00 43.10  ? 380  LEU C C   1 
ATOM   10068 O  O   . LEU B  1 380 ? 21.871  26.283  68.869  1.00 42.11  ? 380  LEU C O   1 
ATOM   10069 C  CB  . LEU B  1 380 ? 18.750  26.873  67.662  1.00 43.45  ? 380  LEU C CB  1 
ATOM   10070 C  CG  . LEU B  1 380 ? 18.782  28.030  68.671  1.00 49.72  ? 380  LEU C CG  1 
ATOM   10071 C  CD1 . LEU B  1 380 ? 19.623  29.215  68.186  1.00 44.62  ? 380  LEU C CD1 1 
ATOM   10072 C  CD2 . LEU B  1 380 ? 17.358  28.469  69.012  1.00 47.38  ? 380  LEU C CD2 1 
ATOM   10073 N  N   . VAL B  1 381 ? 20.316  24.662  69.042  1.00 43.43  ? 381  VAL C N   1 
ATOM   10074 C  CA  . VAL B  1 381 ? 21.031  24.010  70.137  1.00 42.21  ? 381  VAL C CA  1 
ATOM   10075 C  C   . VAL B  1 381 ? 21.626  22.654  69.763  1.00 41.66  ? 381  VAL C C   1 
ATOM   10076 O  O   . VAL B  1 381 ? 20.930  21.766  69.300  1.00 40.44  ? 381  VAL C O   1 
ATOM   10077 C  CB  . VAL B  1 381 ? 20.135  23.822  71.358  1.00 46.92  ? 381  VAL C CB  1 
ATOM   10078 C  CG1 . VAL B  1 381 ? 20.938  23.204  72.477  1.00 42.31  ? 381  VAL C CG1 1 
ATOM   10079 C  CG2 . VAL B  1 381 ? 19.545  25.174  71.792  1.00 48.20  ? 381  VAL C CG2 1 
ATOM   10080 N  N   . THR B  1 382 ? 22.918  22.482  70.000  1.00 38.18  ? 382  THR C N   1 
ATOM   10081 C  CA  . THR B  1 382 ? 23.587  21.279  69.553  1.00 44.52  ? 382  THR C CA  1 
ATOM   10082 C  C   . THR B  1 382 ? 24.313  20.587  70.720  1.00 53.44  ? 382  THR C C   1 
ATOM   10083 O  O   . THR B  1 382 ? 24.990  21.246  71.519  1.00 49.17  ? 382  THR C O   1 
ATOM   10084 C  CB  . THR B  1 382 ? 24.618  21.589  68.394  1.00 46.86  ? 382  THR C CB  1 
ATOM   10085 O  OG1 . THR B  1 382 ? 24.028  22.441  67.403  1.00 48.93  ? 382  THR C OG1 1 
ATOM   10086 C  CG2 . THR B  1 382 ? 25.071  20.320  67.712  1.00 47.30  ? 382  THR C CG2 1 
ATOM   10087 N  N   . MET B  1 383 ? 24.183  19.261  70.806  1.00 45.14  ? 383  MET C N   1 
ATOM   10088 C  CA  . MET B  1 383 ? 24.948  18.492  71.782  1.00 48.60  ? 383  MET C CA  1 
ATOM   10089 C  C   . MET B  1 383 ? 26.432  18.821  71.650  1.00 51.19  ? 383  MET C C   1 
ATOM   10090 O  O   . MET B  1 383 ? 26.918  19.162  70.576  1.00 48.37  ? 383  MET C O   1 
ATOM   10091 C  CB  . MET B  1 383 ? 24.726  16.971  71.615  1.00 47.23  ? 383  MET C CB  1 
ATOM   10092 C  CG  . MET B  1 383 ? 25.366  16.336  70.365  1.00 44.53  ? 383  MET C CG  1 
ATOM   10093 S  SD  . MET B  1 383 ? 24.355  16.550  68.877  1.00 48.59  ? 383  MET C SD  1 
ATOM   10094 C  CE  . MET B  1 383 ? 25.614  16.895  67.656  1.00 43.95  ? 383  MET C CE  1 
ATOM   10095 N  N   . GLU B  1 384 ? 27.158  18.731  72.750  1.00 51.78  ? 384  GLU C N   1 
ATOM   10096 C  CA  . GLU B  1 384 ? 28.578  18.998  72.685  1.00 51.71  ? 384  GLU C CA  1 
ATOM   10097 C  C   . GLU B  1 384 ? 29.315  17.903  71.910  1.00 46.22  ? 384  GLU C C   1 
ATOM   10098 O  O   . GLU B  1 384 ? 30.145  18.192  71.044  1.00 44.71  ? 384  GLU C O   1 
ATOM   10099 C  CB  . GLU B  1 384 ? 29.143  19.148  74.090  1.00 52.80  ? 384  GLU C CB  1 
ATOM   10100 C  CG  . GLU B  1 384 ? 30.655  19.110  74.147  1.00 57.32  ? 384  GLU C CG  1 
ATOM   10101 C  CD  . GLU B  1 384 ? 31.174  19.467  75.522  1.00 64.96  ? 384  GLU C CD  1 
ATOM   10102 O  OE1 . GLU B  1 384 ? 30.491  20.253  76.222  1.00 68.13  ? 384  GLU C OE1 1 
ATOM   10103 O  OE2 . GLU B  1 384 ? 32.258  18.962  75.896  1.00 67.88  ? 384  GLU C OE2 1 
ATOM   10104 N  N   . TRP B  1 385 ? 29.011  16.648  72.222  1.00 44.65  ? 385  TRP C N   1 
ATOM   10105 C  CA  . TRP B  1 385 ? 29.608  15.533  71.502  1.00 43.07  ? 385  TRP C CA  1 
ATOM   10106 C  C   . TRP B  1 385 ? 28.545  14.465  71.283  1.00 43.46  ? 385  TRP C C   1 
ATOM   10107 O  O   . TRP B  1 385 ? 27.461  14.548  71.843  1.00 44.31  ? 385  TRP C O   1 
ATOM   10108 C  CB  . TRP B  1 385 ? 30.823  14.998  72.261  1.00 44.95  ? 385  TRP C CB  1 
ATOM   10109 C  CG  . TRP B  1 385 ? 31.470  13.789  71.651  1.00 44.90  ? 385  TRP C CG  1 
ATOM   10110 C  CD1 . TRP B  1 385 ? 31.549  12.541  72.190  1.00 43.69  ? 385  TRP C CD1 1 
ATOM   10111 C  CD2 . TRP B  1 385 ? 32.121  13.716  70.382  1.00 45.95  ? 385  TRP C CD2 1 
ATOM   10112 N  NE1 . TRP B  1 385 ? 32.223  11.695  71.342  1.00 43.26  ? 385  TRP C NE1 1 
ATOM   10113 C  CE2 . TRP B  1 385 ? 32.580  12.392  70.221  1.00 45.91  ? 385  TRP C CE2 1 
ATOM   10114 C  CE3 . TRP B  1 385 ? 32.353  14.640  69.355  1.00 48.49  ? 385  TRP C CE3 1 
ATOM   10115 C  CZ2 . TRP B  1 385 ? 33.263  11.972  69.078  1.00 50.16  ? 385  TRP C CZ2 1 
ATOM   10116 C  CZ3 . TRP B  1 385 ? 33.030  14.222  68.224  1.00 40.83  ? 385  TRP C CZ3 1 
ATOM   10117 C  CH2 . TRP B  1 385 ? 33.476  12.901  68.094  1.00 46.21  ? 385  TRP C CH2 1 
ATOM   10118 N  N   . TRP B  1 386 ? 28.843  13.476  70.449  1.00 45.36  ? 386  TRP C N   1 
ATOM   10119 C  CA  . TRP B  1 386 ? 27.829  12.537  69.964  1.00 44.78  ? 386  TRP C CA  1 
ATOM   10120 C  C   . TRP B  1 386 ? 27.276  11.595  71.040  1.00 44.81  ? 386  TRP C C   1 
ATOM   10121 O  O   . TRP B  1 386 ? 26.250  10.937  70.835  1.00 45.14  ? 386  TRP C O   1 
ATOM   10122 C  CB  . TRP B  1 386 ? 28.403  11.725  68.799  1.00 41.20  ? 386  TRP C CB  1 
ATOM   10123 C  CG  . TRP B  1 386 ? 28.816  12.593  67.637  1.00 41.51  ? 386  TRP C CG  1 
ATOM   10124 C  CD1 . TRP B  1 386 ? 30.089  12.880  67.238  1.00 39.70  ? 386  TRP C CD1 1 
ATOM   10125 C  CD2 . TRP B  1 386 ? 27.950  13.304  66.748  1.00 37.67  ? 386  TRP C CD2 1 
ATOM   10126 N  NE1 . TRP B  1 386 ? 30.068  13.721  66.157  1.00 38.37  ? 386  TRP C NE1 1 
ATOM   10127 C  CE2 . TRP B  1 386 ? 28.767  13.997  65.836  1.00 41.14  ? 386  TRP C CE2 1 
ATOM   10128 C  CE3 . TRP B  1 386 ? 26.564  13.419  66.629  1.00 38.37  ? 386  TRP C CE3 1 
ATOM   10129 C  CZ2 . TRP B  1 386 ? 28.241  14.784  64.820  1.00 32.81  ? 386  TRP C CZ2 1 
ATOM   10130 C  CZ3 . TRP B  1 386 ? 26.053  14.201  65.621  1.00 40.40  ? 386  TRP C CZ3 1 
ATOM   10131 C  CH2 . TRP B  1 386 ? 26.884  14.865  64.729  1.00 32.10  ? 386  TRP C CH2 1 
ATOM   10132 N  N   . ASN B  1 387 ? 27.954  11.540  72.181  1.00 50.44  ? 387  ASN C N   1 
ATOM   10133 C  CA  . ASN B  1 387 ? 27.492  10.759  73.333  1.00 50.28  ? 387  ASN C CA  1 
ATOM   10134 C  C   . ASN B  1 387 ? 26.131  11.232  73.804  1.00 47.43  ? 387  ASN C C   1 
ATOM   10135 O  O   . ASN B  1 387 ? 25.341  10.470  74.361  1.00 49.20  ? 387  ASN C O   1 
ATOM   10136 C  CB  . ASN B  1 387 ? 28.494  10.852  74.478  1.00 45.02  ? 387  ASN C CB  1 
ATOM   10137 C  CG  . ASN B  1 387 ? 28.864  12.278  74.791  1.00 49.39  ? 387  ASN C CG  1 
ATOM   10138 O  OD1 . ASN B  1 387 ? 28.039  13.175  74.677  1.00 52.61  ? 387  ASN C OD1 1 
ATOM   10139 N  ND2 . ASN B  1 387 ? 30.116  12.503  75.160  1.00 57.71  ? 387  ASN C ND2 1 
ATOM   10140 N  N   . ASP B  1 388 ? 25.866  12.508  73.565  1.00 45.72  ? 388  ASP C N   1 
ATOM   10141 C  CA  . ASP B  1 388 ? 24.598  13.089  73.949  1.00 47.21  ? 388  ASP C CA  1 
ATOM   10142 C  C   . ASP B  1 388 ? 23.748  13.416  72.728  1.00 50.34  ? 388  ASP C C   1 
ATOM   10143 O  O   . ASP B  1 388 ? 23.036  14.428  72.704  1.00 44.11  ? 388  ASP C O   1 
ATOM   10144 C  CB  . ASP B  1 388 ? 24.835  14.334  74.810  1.00 52.62  ? 388  ASP C CB  1 
ATOM   10145 C  CG  . ASP B  1 388 ? 25.331  13.982  76.208  1.00 55.99  ? 388  ASP C CG  1 
ATOM   10146 O  OD1 . ASP B  1 388 ? 25.051  12.841  76.665  1.00 50.32  ? 388  ASP C OD1 1 
ATOM   10147 O  OD2 . ASP B  1 388 ? 25.999  14.835  76.840  1.00 52.49  ? 388  ASP C OD2 1 
ATOM   10148 N  N   . ILE B  1 389 ? 23.806  12.537  71.727  1.00 43.39  ? 389  ILE C N   1 
ATOM   10149 C  CA  . ILE B  1 389 ? 22.980  12.692  70.551  1.00 35.91  ? 389  ILE C CA  1 
ATOM   10150 C  C   . ILE B  1 389 ? 21.486  12.748  70.881  1.00 41.79  ? 389  ILE C C   1 
ATOM   10151 O  O   . ILE B  1 389 ? 20.693  13.319  70.122  1.00 47.90  ? 389  ILE C O   1 
ATOM   10152 C  CB  . ILE B  1 389 ? 23.234  11.558  69.541  1.00 39.26  ? 389  ILE C CB  1 
ATOM   10153 C  CG1 . ILE B  1 389 ? 22.465  11.820  68.234  1.00 43.78  ? 389  ILE C CG1 1 
ATOM   10154 C  CG2 . ILE B  1 389 ? 22.871  10.204  70.123  1.00 40.00  ? 389  ILE C CG2 1 
ATOM   10155 C  CD1 . ILE B  1 389 ? 22.686  13.221  67.643  1.00 31.97  ? 389  ILE C CD1 1 
ATOM   10156 N  N   . TRP B  1 390 ? 21.088  12.170  72.007  1.00 41.21  ? 390  TRP C N   1 
ATOM   10157 C  CA  . TRP B  1 390 ? 19.669  12.140  72.342  1.00 46.10  ? 390  TRP C CA  1 
ATOM   10158 C  C   . TRP B  1 390 ? 19.108  13.556  72.526  1.00 45.57  ? 390  TRP C C   1 
ATOM   10159 O  O   . TRP B  1 390 ? 17.935  13.807  72.224  1.00 43.92  ? 390  TRP C O   1 
ATOM   10160 C  CB  . TRP B  1 390 ? 19.430  11.296  73.591  1.00 50.49  ? 390  TRP C CB  1 
ATOM   10161 C  CG  . TRP B  1 390 ? 19.595  12.049  74.872  1.00 48.18  ? 390  TRP C CG  1 
ATOM   10162 C  CD1 . TRP B  1 390 ? 20.734  12.172  75.616  1.00 45.39  ? 390  TRP C CD1 1 
ATOM   10163 C  CD2 . TRP B  1 390 ? 18.577  12.771  75.569  1.00 45.27  ? 390  TRP C CD2 1 
ATOM   10164 N  NE1 . TRP B  1 390 ? 20.485  12.935  76.730  1.00 50.88  ? 390  TRP C NE1 1 
ATOM   10165 C  CE2 . TRP B  1 390 ? 19.167  13.315  76.723  1.00 51.06  ? 390  TRP C CE2 1 
ATOM   10166 C  CE3 . TRP B  1 390 ? 17.225  13.023  75.317  1.00 50.40  ? 390  TRP C CE3 1 
ATOM   10167 C  CZ2 . TRP B  1 390 ? 18.454  14.093  77.625  1.00 52.06  ? 390  TRP C CZ2 1 
ATOM   10168 C  CZ3 . TRP B  1 390 ? 16.518  13.789  76.208  1.00 51.55  ? 390  TRP C CZ3 1 
ATOM   10169 C  CH2 . TRP B  1 390 ? 17.130  14.318  77.348  1.00 52.87  ? 390  TRP C CH2 1 
ATOM   10170 N  N   . LEU B  1 391 ? 19.951  14.471  73.002  1.00 43.92  ? 391  LEU C N   1 
ATOM   10171 C  CA  . LEU B  1 391 ? 19.565  15.878  73.144  1.00 47.94  ? 391  LEU C CA  1 
ATOM   10172 C  C   . LEU B  1 391 ? 18.864  16.396  71.899  1.00 47.47  ? 391  LEU C C   1 
ATOM   10173 O  O   . LEU B  1 391 ? 17.737  16.912  71.985  1.00 45.80  ? 391  LEU C O   1 
ATOM   10174 C  CB  . LEU B  1 391 ? 20.782  16.747  73.445  1.00 48.41  ? 391  LEU C CB  1 
ATOM   10175 C  CG  . LEU B  1 391 ? 21.471  16.447  74.778  1.00 47.63  ? 391  LEU C CG  1 
ATOM   10176 C  CD1 . LEU B  1 391 ? 22.572  17.464  75.029  1.00 45.36  ? 391  LEU C CD1 1 
ATOM   10177 C  CD2 . LEU B  1 391 ? 20.461  16.449  75.897  1.00 43.32  ? 391  LEU C CD2 1 
ATOM   10178 N  N   . ASN B  1 392 ? 19.527  16.232  70.747  1.00 46.97  ? 392  ASN C N   1 
ATOM   10179 C  CA  . ASN B  1 392 ? 18.910  16.484  69.437  1.00 46.19  ? 392  ASN C CA  1 
ATOM   10180 C  C   . ASN B  1 392 ? 17.680  15.595  69.185  1.00 45.72  ? 392  ASN C C   1 
ATOM   10181 O  O   . ASN B  1 392 ? 16.576  16.081  68.905  1.00 40.65  ? 392  ASN C O   1 
ATOM   10182 C  CB  . ASN B  1 392 ? 19.904  16.246  68.281  1.00 47.97  ? 392  ASN C CB  1 
ATOM   10183 C  CG  . ASN B  1 392 ? 21.064  17.247  68.240  1.00 42.82  ? 392  ASN C CG  1 
ATOM   10184 O  OD1 . ASN B  1 392 ? 21.491  17.777  69.259  1.00 56.11  ? 392  ASN C OD1 1 
ATOM   10185 N  ND2 . ASN B  1 392 ? 21.603  17.467  67.051  1.00 48.86  ? 392  ASN C ND2 1 
ATOM   10186 N  N   . GLU B  1 393 ? 17.880  14.284  69.282  1.00 42.20  ? 393  GLU C N   1 
ATOM   10187 C  CA  . GLU B  1 393 ? 16.918  13.347  68.707  1.00 43.53  ? 393  GLU C CA  1 
ATOM   10188 C  C   . GLU B  1 393 ? 15.735  13.000  69.602  1.00 43.31  ? 393  GLU C C   1 
ATOM   10189 O  O   . GLU B  1 393 ? 14.607  12.849  69.115  1.00 43.44  ? 393  GLU C O   1 
ATOM   10190 C  CB  . GLU B  1 393 ? 17.645  12.071  68.280  1.00 47.74  ? 393  GLU C CB  1 
ATOM   10191 C  CG  . GLU B  1 393 ? 18.646  12.287  67.132  1.00 45.17  ? 393  GLU C CG  1 
ATOM   10192 C  CD  . GLU B  1 393 ? 18.000  12.866  65.869  1.00 45.58  ? 393  GLU C CD  1 
ATOM   10193 O  OE1 . GLU B  1 393 ? 16.744  12.844  65.779  1.00 44.00  ? 393  GLU C OE1 1 
ATOM   10194 O  OE2 . GLU B  1 393 ? 18.752  13.322  64.968  1.00 39.05  ? 393  GLU C OE2 1 
ATOM   10195 N  N   . GLY B  1 394 ? 15.990  12.879  70.902  1.00 45.43  ? 394  GLY C N   1 
ATOM   10196 C  CA  . GLY B  1 394 ? 14.921  12.689  71.858  1.00 43.45  ? 394  GLY C CA  1 
ATOM   10197 C  C   . GLY B  1 394 ? 13.964  13.865  71.814  1.00 40.54  ? 394  GLY C C   1 
ATOM   10198 O  O   . GLY B  1 394 ? 12.747  13.696  71.766  1.00 42.31  ? 394  GLY C O   1 
ATOM   10199 N  N   . PHE B  1 395 ? 14.510  15.070  71.809  1.00 35.36  ? 395  PHE C N   1 
ATOM   10200 C  CA  . PHE B  1 395 ? 13.654  16.246  71.774  1.00 44.56  ? 395  PHE C CA  1 
ATOM   10201 C  C   . PHE B  1 395 ? 12.917  16.412  70.439  1.00 50.46  ? 395  PHE C C   1 
ATOM   10202 O  O   . PHE B  1 395 ? 11.729  16.767  70.427  1.00 49.09  ? 395  PHE C O   1 
ATOM   10203 C  CB  . PHE B  1 395 ? 14.469  17.491  72.077  1.00 47.00  ? 395  PHE C CB  1 
ATOM   10204 C  CG  . PHE B  1 395 ? 14.217  18.039  73.435  1.00 60.71  ? 395  PHE C CG  1 
ATOM   10205 C  CD1 . PHE B  1 395 ? 13.019  18.672  73.725  1.00 60.57  ? 395  PHE C CD1 1 
ATOM   10206 C  CD2 . PHE B  1 395 ? 15.165  17.910  74.435  1.00 61.94  ? 395  PHE C CD2 1 
ATOM   10207 C  CE1 . PHE B  1 395 ? 12.780  19.181  74.979  1.00 57.35  ? 395  PHE C CE1 1 
ATOM   10208 C  CE2 . PHE B  1 395 ? 14.934  18.423  75.687  1.00 61.38  ? 395  PHE C CE2 1 
ATOM   10209 C  CZ  . PHE B  1 395 ? 13.736  19.057  75.960  1.00 64.00  ? 395  PHE C CZ  1 
ATOM   10210 N  N   . ALA B  1 396 ? 13.613  16.162  69.324  1.00 40.87  ? 396  ALA C N   1 
ATOM   10211 C  CA  . ALA B  1 396 ? 12.966  16.183  68.015  1.00 43.15  ? 396  ALA C CA  1 
ATOM   10212 C  C   . ALA B  1 396 ? 11.838  15.176  67.992  1.00 44.64  ? 396  ALA C C   1 
ATOM   10213 O  O   . ALA B  1 396 ? 10.710  15.511  67.625  1.00 44.83  ? 396  ALA C O   1 
ATOM   10214 C  CB  . ALA B  1 396 ? 13.969  15.894  66.891  1.00 47.71  ? 396  ALA C CB  1 
ATOM   10215 N  N   . LYS B  1 397 ? 12.135  13.945  68.405  1.00 44.18  ? 397  LYS C N   1 
ATOM   10216 C  CA  . LYS B  1 397 ? 11.116  12.908  68.402  1.00 43.00  ? 397  LYS C CA  1 
ATOM   10217 C  C   . LYS B  1 397 ? 9.954   13.357  69.287  1.00 51.87  ? 397  LYS C C   1 
ATOM   10218 O  O   . LYS B  1 397 ? 8.790   13.306  68.880  1.00 47.74  ? 397  LYS C O   1 
ATOM   10219 C  CB  . LYS B  1 397 ? 11.691  11.578  68.880  1.00 39.34  ? 397  LYS C CB  1 
ATOM   10220 C  CG  . LYS B  1 397 ? 10.668  10.464  68.988  1.00 41.62  ? 397  LYS C CG  1 
ATOM   10221 C  CD  . LYS B  1 397 ? 10.185  9.953   67.647  1.00 48.24  ? 397  LYS C CD  1 
ATOM   10222 C  CE  . LYS B  1 397 ? 10.227  8.422   67.625  1.00 53.60  ? 397  LYS C CE  1 
ATOM   10223 N  NZ  . LYS B  1 397 ? 9.083   7.808   66.888  1.00 52.37  ? 397  LYS C NZ  1 
ATOM   10224 N  N   . TYR B  1 398 ? 10.289  13.844  70.481  1.00 49.46  ? 398  TYR C N   1 
ATOM   10225 C  CA  . TYR B  1 398 ? 9.289   14.273  71.437  1.00 53.32  ? 398  TYR C CA  1 
ATOM   10226 C  C   . TYR B  1 398 ? 8.447   15.436  70.916  1.00 54.30  ? 398  TYR C C   1 
ATOM   10227 O  O   . TYR B  1 398 ? 7.220   15.415  71.063  1.00 54.56  ? 398  TYR C O   1 
ATOM   10228 C  CB  . TYR B  1 398 ? 9.955   14.654  72.762  1.00 57.86  ? 398  TYR C CB  1 
ATOM   10229 C  CG  . TYR B  1 398 ? 9.000   15.245  73.774  1.00 65.08  ? 398  TYR C CG  1 
ATOM   10230 C  CD1 . TYR B  1 398 ? 7.914   14.510  74.256  1.00 63.60  ? 398  TYR C CD1 1 
ATOM   10231 C  CD2 . TYR B  1 398 ? 9.185   16.538  74.254  1.00 65.66  ? 398  TYR C CD2 1 
ATOM   10232 C  CE1 . TYR B  1 398 ? 7.036   15.058  75.184  1.00 65.37  ? 398  TYR C CE1 1 
ATOM   10233 C  CE2 . TYR B  1 398 ? 8.324   17.087  75.182  1.00 65.99  ? 398  TYR C CE2 1 
ATOM   10234 C  CZ  . TYR B  1 398 ? 7.251   16.348  75.647  1.00 69.55  ? 398  TYR C CZ  1 
ATOM   10235 O  OH  . TYR B  1 398 ? 6.389   16.915  76.568  1.00 75.43  ? 398  TYR C OH  1 
ATOM   10236 N  N   . MET B  1 399 ? 9.086   16.437  70.300  1.00 51.04  ? 399  MET C N   1 
ATOM   10237 C  CA  . MET B  1 399 ? 8.333   17.602  69.805  1.00 50.80  ? 399  MET C CA  1 
ATOM   10238 C  C   . MET B  1 399 ? 7.314   17.232  68.738  1.00 47.32  ? 399  MET C C   1 
ATOM   10239 O  O   . MET B  1 399 ? 6.403   18.003  68.474  1.00 46.57  ? 399  MET C O   1 
ATOM   10240 C  CB  . MET B  1 399 ? 9.260   18.678  69.252  1.00 48.51  ? 399  MET C CB  1 
ATOM   10241 C  CG  . MET B  1 399 ? 10.019  19.463  70.312  1.00 54.88  ? 399  MET C CG  1 
ATOM   10242 S  SD  . MET B  1 399 ? 8.928   19.947  71.661  1.00 58.77  ? 399  MET C SD  1 
ATOM   10243 C  CE  . MET B  1 399 ? 7.762   21.019  70.813  1.00 60.27  ? 399  MET C CE  1 
ATOM   10244 N  N   . GLU B  1 400 ? 7.471   16.057  68.130  1.00 47.60  ? 400  GLU C N   1 
ATOM   10245 C  CA  . GLU B  1 400 ? 6.528   15.588  67.127  1.00 52.66  ? 400  GLU C CA  1 
ATOM   10246 C  C   . GLU B  1 400 ? 5.148   15.615  67.731  1.00 53.86  ? 400  GLU C C   1 
ATOM   10247 O  O   . GLU B  1 400 ? 4.247   16.273  67.223  1.00 54.72  ? 400  GLU C O   1 
ATOM   10248 C  CB  . GLU B  1 400 ? 6.871   14.171  66.632  1.00 54.87  ? 400  GLU C CB  1 
ATOM   10249 C  CG  . GLU B  1 400 ? 8.125   14.095  65.762  1.00 53.12  ? 400  GLU C CG  1 
ATOM   10250 C  CD  . GLU B  1 400 ? 8.449   12.676  65.283  1.00 53.74  ? 400  GLU C CD  1 
ATOM   10251 O  OE1 . GLU B  1 400 ? 7.502   11.930  64.947  1.00 64.14  ? 400  GLU C OE1 1 
ATOM   10252 O  OE2 . GLU B  1 400 ? 9.649   12.314  65.238  1.00 43.17  ? 400  GLU C OE2 1 
ATOM   10253 N  N   . LEU B  1 401 ? 5.011   14.897  68.837  1.00 60.86  ? 401  LEU C N   1 
ATOM   10254 C  CA  . LEU B  1 401 ? 3.791   14.879  69.624  1.00 55.68  ? 401  LEU C CA  1 
ATOM   10255 C  C   . LEU B  1 401 ? 3.381   16.290  70.020  1.00 57.38  ? 401  LEU C C   1 
ATOM   10256 O  O   . LEU B  1 401 ? 2.270   16.737  69.734  1.00 58.11  ? 401  LEU C O   1 
ATOM   10257 C  CB  . LEU B  1 401 ? 4.005   14.016  70.863  1.00 63.56  ? 401  LEU C CB  1 
ATOM   10258 C  CG  . LEU B  1 401 ? 2.902   13.956  71.917  1.00 70.70  ? 401  LEU C CG  1 
ATOM   10259 C  CD1 . LEU B  1 401 ? 1.843   12.935  71.504  1.00 73.84  ? 401  LEU C CD1 1 
ATOM   10260 C  CD2 . LEU B  1 401 ? 3.493   13.653  73.301  1.00 61.29  ? 401  LEU C CD2 1 
ATOM   10261 N  N   . ILE B  1 402 ? 4.300   17.004  70.658  1.00 55.69  ? 402  ILE C N   1 
ATOM   10262 C  CA  . ILE B  1 402 ? 3.982   18.317  71.202  1.00 57.70  ? 402  ILE C CA  1 
ATOM   10263 C  C   . ILE B  1 402 ? 3.708   19.336  70.091  1.00 65.08  ? 402  ILE C C   1 
ATOM   10264 O  O   . ILE B  1 402 ? 3.121   20.389  70.351  1.00 66.69  ? 402  ILE C O   1 
ATOM   10265 C  CB  . ILE B  1 402 ? 5.111   18.816  72.134  1.00 63.30  ? 402  ILE C CB  1 
ATOM   10266 C  CG1 . ILE B  1 402 ? 5.427   17.751  73.181  1.00 64.47  ? 402  ILE C CG1 1 
ATOM   10267 C  CG2 . ILE B  1 402 ? 4.702   20.075  72.868  1.00 65.00  ? 402  ILE C CG2 1 
ATOM   10268 C  CD1 . ILE B  1 402 ? 4.221   17.340  74.015  1.00 60.63  ? 402  ILE C CD1 1 
ATOM   10269 N  N   . ALA B  1 403 ? 4.073   19.011  68.845  1.00 62.45  ? 403  ALA C N   1 
ATOM   10270 C  CA  . ALA B  1 403 ? 3.781   19.911  67.726  1.00 58.38  ? 403  ALA C CA  1 
ATOM   10271 C  C   . ALA B  1 403 ? 2.624   19.436  66.860  1.00 59.67  ? 403  ALA C C   1 
ATOM   10272 O  O   . ALA B  1 403 ? 1.715   20.207  66.572  1.00 66.56  ? 403  ALA C O   1 
ATOM   10273 C  CB  . ALA B  1 403 ? 5.005   20.115  66.873  1.00 63.41  ? 403  ALA C CB  1 
ATOM   10274 N  N   . VAL B  1 404 ? 2.656   18.181  66.437  1.00 60.64  ? 404  VAL C N   1 
ATOM   10275 C  CA  . VAL B  1 404 ? 1.591   17.659  65.596  1.00 59.41  ? 404  VAL C CA  1 
ATOM   10276 C  C   . VAL B  1 404 ? 0.256   17.796  66.283  1.00 73.12  ? 404  VAL C C   1 
ATOM   10277 O  O   . VAL B  1 404 ? -0.690  18.328  65.701  1.00 74.83  ? 404  VAL C O   1 
ATOM   10278 C  CB  . VAL B  1 404 ? 1.798   16.197  65.249  1.00 62.83  ? 404  VAL C CB  1 
ATOM   10279 C  CG1 . VAL B  1 404 ? 0.551   15.642  64.577  1.00 67.64  ? 404  VAL C CG1 1 
ATOM   10280 C  CG2 . VAL B  1 404 ? 3.012   16.044  64.355  1.00 63.23  ? 404  VAL C CG2 1 
ATOM   10281 N  N   . ASN B  1 405 ? 0.206   17.333  67.534  1.00 72.39  ? 405  ASN C N   1 
ATOM   10282 C  CA  . ASN B  1 405 ? -1.027  17.275  68.312  1.00 75.93  ? 405  ASN C CA  1 
ATOM   10283 C  C   . ASN B  1 405 ? -1.740  18.618  68.399  1.00 79.17  ? 405  ASN C C   1 
ATOM   10284 O  O   . ASN B  1 405 ? -2.971  18.673  68.410  1.00 82.83  ? 405  ASN C O   1 
ATOM   10285 C  CB  . ASN B  1 405 ? -0.742  16.761  69.728  1.00 83.29  ? 405  ASN C CB  1 
ATOM   10286 C  CG  . ASN B  1 405 ? -1.893  17.008  70.666  1.00 82.73  ? 405  ASN C CG  1 
ATOM   10287 O  OD1 . ASN B  1 405 ? -2.956  16.411  70.509  1.00 83.27  ? 405  ASN C OD1 1 
ATOM   10288 N  ND2 . ASN B  1 405 ? -1.703  17.886  71.647  1.00 86.91  ? 405  ASN C ND2 1 
ATOM   10289 N  N   . ALA B  1 406 ? -0.960  19.695  68.456  1.00 73.74  ? 406  ALA C N   1 
ATOM   10290 C  CA  . ALA B  1 406 ? -1.504  21.049  68.530  1.00 76.25  ? 406  ALA C CA  1 
ATOM   10291 C  C   . ALA B  1 406 ? -2.013  21.502  67.176  1.00 79.66  ? 406  ALA C C   1 
ATOM   10292 O  O   . ALA B  1 406 ? -3.196  21.788  67.000  1.00 80.63  ? 406  ALA C O   1 
ATOM   10293 C  CB  . ALA B  1 406 ? -0.449  22.021  69.036  1.00 66.13  ? 406  ALA C CB  1 
ATOM   10294 N  N   . THR B  1 407 ? -1.089  21.557  66.224  1.00 78.52  ? 407  THR C N   1 
ATOM   10295 C  CA  . THR B  1 407 ? -1.335  22.112  64.905  1.00 73.89  ? 407  THR C CA  1 
ATOM   10296 C  C   . THR B  1 407 ? -2.245  21.234  64.057  1.00 72.51  ? 407  THR C C   1 
ATOM   10297 O  O   . THR B  1 407 ? -2.960  21.721  63.181  1.00 77.69  ? 407  THR C O   1 
ATOM   10298 C  CB  . THR B  1 407 ? -0.012  22.322  64.174  1.00 72.01  ? 407  THR C CB  1 
ATOM   10299 O  OG1 . THR B  1 407 ? 0.658   21.061  64.050  1.00 75.84  ? 407  THR C OG1 1 
ATOM   10300 C  CG2 . THR B  1 407 ? 0.872   23.283  64.966  1.00 67.42  ? 407  THR C CG2 1 
ATOM   10301 N  N   . TYR B  1 408 ? -2.207  19.935  64.314  1.00 74.42  ? 408  TYR C N   1 
ATOM   10302 C  CA  . TYR B  1 408 ? -3.030  18.988  63.567  1.00 82.74  ? 408  TYR C CA  1 
ATOM   10303 C  C   . TYR B  1 408 ? -3.632  17.946  64.496  1.00 77.81  ? 408  TYR C C   1 
ATOM   10304 O  O   . TYR B  1 408 ? -3.217  16.791  64.482  1.00 77.65  ? 408  TYR C O   1 
ATOM   10305 C  CB  . TYR B  1 408 ? -2.212  18.279  62.476  1.00 81.84  ? 408  TYR C CB  1 
ATOM   10306 C  CG  . TYR B  1 408 ? -2.043  19.038  61.176  1.00 76.79  ? 408  TYR C CG  1 
ATOM   10307 C  CD1 . TYR B  1 408 ? -3.023  18.994  60.190  1.00 77.94  ? 408  TYR C CD1 1 
ATOM   10308 C  CD2 . TYR B  1 408 ? -0.892  19.766  60.922  1.00 73.25  ? 408  TYR C CD2 1 
ATOM   10309 C  CE1 . TYR B  1 408 ? -2.873  19.667  58.998  1.00 72.49  ? 408  TYR C CE1 1 
ATOM   10310 C  CE2 . TYR B  1 408 ? -0.728  20.447  59.732  1.00 74.79  ? 408  TYR C CE2 1 
ATOM   10311 C  CZ  . TYR B  1 408 ? -1.723  20.397  58.772  1.00 77.16  ? 408  TYR C CZ  1 
ATOM   10312 O  OH  . TYR B  1 408 ? -1.565  21.075  57.582  1.00 72.68  ? 408  TYR C OH  1 
ATOM   10313 N  N   . PRO B  1 409 ? -4.605  18.351  65.319  1.00 82.75  ? 409  PRO C N   1 
ATOM   10314 C  CA  . PRO B  1 409 ? -5.211  17.376  66.230  1.00 83.83  ? 409  PRO C CA  1 
ATOM   10315 C  C   . PRO B  1 409 ? -6.018  16.345  65.453  1.00 86.30  ? 409  PRO C C   1 
ATOM   10316 O  O   . PRO B  1 409 ? -6.143  15.190  65.870  1.00 89.09  ? 409  PRO C O   1 
ATOM   10317 C  CB  . PRO B  1 409 ? -6.113  18.232  67.122  1.00 82.40  ? 409  PRO C CB  1 
ATOM   10318 C  CG  . PRO B  1 409 ? -5.603  19.633  66.967  1.00 83.81  ? 409  PRO C CG  1 
ATOM   10319 C  CD  . PRO B  1 409 ? -5.091  19.718  65.566  1.00 82.65  ? 409  PRO C CD  1 
ATOM   10320 N  N   . GLU B  1 410 ? -6.531  16.773  64.305  1.00 80.05  ? 410  GLU C N   1 
ATOM   10321 C  CA  . GLU B  1 410 ? -7.384  15.950  63.459  1.00 83.73  ? 410  GLU C CA  1 
ATOM   10322 C  C   . GLU B  1 410 ? -6.712  14.643  63.036  1.00 89.04  ? 410  GLU C C   1 
ATOM   10323 O  O   . GLU B  1 410 ? -7.375  13.717  62.566  1.00 88.69  ? 410  GLU C O   1 
ATOM   10324 C  CB  . GLU B  1 410 ? -7.810  16.755  62.225  1.00 84.33  ? 410  GLU C CB  1 
ATOM   10325 C  CG  . GLU B  1 410 ? -6.692  17.603  61.592  1.00 86.69  ? 410  GLU C CG  1 
ATOM   10326 C  CD  . GLU B  1 410 ? -6.486  18.943  62.288  1.00 83.54  ? 410  GLU C CD  1 
ATOM   10327 O  OE1 . GLU B  1 410 ? -7.096  19.141  63.357  1.00 82.56  ? 410  GLU C OE1 1 
ATOM   10328 O  OE2 . GLU B  1 410 ? -5.721  19.791  61.771  1.00 80.22  ? 410  GLU C OE2 1 
ATOM   10329 N  N   . LEU B  1 411 ? -5.395  14.580  63.216  1.00 89.85  ? 411  LEU C N   1 
ATOM   10330 C  CA  . LEU B  1 411 ? -4.599  13.420  62.827  1.00 90.49  ? 411  LEU C CA  1 
ATOM   10331 C  C   . LEU B  1 411 ? -4.477  12.405  63.961  1.00 89.48  ? 411  LEU C C   1 
ATOM   10332 O  O   . LEU B  1 411 ? -3.838  11.358  63.801  1.00 81.14  ? 411  LEU C O   1 
ATOM   10333 C  CB  . LEU B  1 411 ? -3.212  13.865  62.367  1.00 84.21  ? 411  LEU C CB  1 
ATOM   10334 C  CG  . LEU B  1 411 ? -3.251  14.791  61.151  1.00 86.87  ? 411  LEU C CG  1 
ATOM   10335 C  CD1 . LEU B  1 411 ? -1.845  15.182  60.709  1.00 82.81  ? 411  LEU C CD1 1 
ATOM   10336 C  CD2 . LEU B  1 411 ? -4.027  14.141  60.009  1.00 74.09  ? 411  LEU C CD2 1 
ATOM   10337 N  N   . GLN B  1 412 ? -5.083  12.741  65.099  1.00 88.21  ? 412  GLN C N   1 
ATOM   10338 C  CA  . GLN B  1 412 ? -5.262  11.814  66.214  1.00 92.54  ? 412  GLN C CA  1 
ATOM   10339 C  C   . GLN B  1 412 ? -3.955  11.174  66.658  1.00 88.06  ? 412  GLN C C   1 
ATOM   10340 O  O   . GLN B  1 412 ? -3.903  9.983   66.951  1.00 90.74  ? 412  GLN C O   1 
ATOM   10341 C  CB  . GLN B  1 412 ? -6.268  10.727  65.830  1.00 97.44  ? 412  GLN C CB  1 
ATOM   10342 C  CG  . GLN B  1 412 ? -7.607  11.257  65.311  1.00 103.34 ? 412  GLN C CG  1 
ATOM   10343 C  CD  . GLN B  1 412 ? -8.799  10.727  66.104  1.00 113.27 ? 412  GLN C CD  1 
ATOM   10344 O  OE1 . GLN B  1 412 ? -8.725  10.561  67.324  1.00 109.59 ? 412  GLN C OE1 1 
ATOM   10345 N  NE2 . GLN B  1 412 ? -9.896  10.441  65.406  1.00 115.35 ? 412  GLN C NE2 1 
ATOM   10346 N  N   . PHE B  1 413 ? -2.907  11.984  66.715  1.00 84.72  ? 413  PHE C N   1 
ATOM   10347 C  CA  . PHE B  1 413 ? -1.556  11.486  66.909  1.00 83.52  ? 413  PHE C CA  1 
ATOM   10348 C  C   . PHE B  1 413 ? -1.229  11.190  68.378  1.00 87.73  ? 413  PHE C C   1 
ATOM   10349 O  O   . PHE B  1 413 ? -0.189  10.602  68.681  1.00 87.75  ? 413  PHE C O   1 
ATOM   10350 C  CB  . PHE B  1 413 ? -0.555  12.493  66.327  1.00 79.60  ? 413  PHE C CB  1 
ATOM   10351 C  CG  . PHE B  1 413 ? 0.812   11.926  66.103  1.00 78.85  ? 413  PHE C CG  1 
ATOM   10352 C  CD1 . PHE B  1 413 ? 0.977   10.730  65.413  1.00 85.44  ? 413  PHE C CD1 1 
ATOM   10353 C  CD2 . PHE B  1 413 ? 1.932   12.579  66.580  1.00 71.84  ? 413  PHE C CD2 1 
ATOM   10354 C  CE1 . PHE B  1 413 ? 2.241   10.194  65.209  1.00 83.64  ? 413  PHE C CE1 1 
ATOM   10355 C  CE2 . PHE B  1 413 ? 3.198   12.048  66.382  1.00 73.78  ? 413  PHE C CE2 1 
ATOM   10356 C  CZ  . PHE B  1 413 ? 3.352   10.854  65.698  1.00 76.99  ? 413  PHE C CZ  1 
ATOM   10357 N  N   . ASP B  1 414 ? -2.118  11.576  69.289  1.00 91.03  ? 414  ASP C N   1 
ATOM   10358 C  CA  . ASP B  1 414 ? -1.860  11.371  70.716  1.00 95.01  ? 414  ASP C CA  1 
ATOM   10359 C  C   . ASP B  1 414 ? -2.002  9.902   71.111  1.00 91.91  ? 414  ASP C C   1 
ATOM   10360 O  O   . ASP B  1 414 ? -1.464  9.469   72.129  1.00 87.25  ? 414  ASP C O   1 
ATOM   10361 C  CB  . ASP B  1 414 ? -2.797  12.228  71.570  1.00 92.93  ? 414  ASP C CB  1 
ATOM   10362 C  CG  . ASP B  1 414 ? -2.281  12.424  72.986  1.00 95.97  ? 414  ASP C CG  1 
ATOM   10363 O  OD1 . ASP B  1 414 ? -1.102  12.802  73.141  1.00 92.72  ? 414  ASP C OD1 1 
ATOM   10364 O  OD2 . ASP B  1 414 ? -3.050  12.199  73.947  1.00 98.43  ? 414  ASP C OD2 1 
ATOM   10365 N  N   . ASP B  1 415 ? -2.717  9.136   70.297  1.00 91.29  ? 415  ASP C N   1 
ATOM   10366 C  CA  . ASP B  1 415 ? -2.987  7.741   70.617  1.00 89.27  ? 415  ASP C CA  1 
ATOM   10367 C  C   . ASP B  1 415 ? -1.867  6.838   70.108  1.00 89.18  ? 415  ASP C C   1 
ATOM   10368 O  O   . ASP B  1 415 ? -1.799  5.649   70.429  1.00 89.11  ? 415  ASP C O   1 
ATOM   10369 C  CB  . ASP B  1 415 ? -4.334  7.329   70.026  1.00 95.57  ? 415  ASP C CB  1 
ATOM   10370 C  CG  . ASP B  1 415 ? -5.452  8.295   70.397  1.00 96.14  ? 415  ASP C CG  1 
ATOM   10371 O  OD1 . ASP B  1 415 ? -5.336  8.972   71.442  1.00 99.87  ? 415  ASP C OD1 1 
ATOM   10372 O  OD2 . ASP B  1 415 ? -6.448  8.380   69.649  1.00 97.49  ? 415  ASP C OD2 1 
ATOM   10373 N  N   . TYR B  1 416 ? -0.980  7.429   69.320  1.00 88.50  ? 416  TYR C N   1 
ATOM   10374 C  CA  . TYR B  1 416 ? 0.119   6.705   68.699  1.00 90.09  ? 416  TYR C CA  1 
ATOM   10375 C  C   . TYR B  1 416 ? 1.311   6.663   69.651  1.00 79.98  ? 416  TYR C C   1 
ATOM   10376 O  O   . TYR B  1 416 ? 2.024   5.663   69.746  1.00 76.44  ? 416  TYR C O   1 
ATOM   10377 C  CB  . TYR B  1 416 ? 0.501   7.384   67.371  1.00 91.73  ? 416  TYR C CB  1 
ATOM   10378 C  CG  . TYR B  1 416 ? 1.045   6.477   66.278  1.00 94.66  ? 416  TYR C CG  1 
ATOM   10379 C  CD1 . TYR B  1 416 ? 0.223   5.557   65.633  1.00 99.11  ? 416  TYR C CD1 1 
ATOM   10380 C  CD2 . TYR B  1 416 ? 2.371   6.577   65.856  1.00 94.83  ? 416  TYR C CD2 1 
ATOM   10381 C  CE1 . TYR B  1 416 ? 0.715   4.736   64.618  1.00 106.28 ? 416  TYR C CE1 1 
ATOM   10382 C  CE2 . TYR B  1 416 ? 2.873   5.763   64.840  1.00 96.10  ? 416  TYR C CE2 1 
ATOM   10383 C  CZ  . TYR B  1 416 ? 2.041   4.846   64.226  1.00 104.39 ? 416  TYR C CZ  1 
ATOM   10384 O  OH  . TYR B  1 416 ? 2.530   4.036   63.223  1.00 103.22 ? 416  TYR C OH  1 
ATOM   10385 N  N   . PHE B  1 417 ? 1.497   7.757   70.378  1.00 78.82  ? 417  PHE C N   1 
ATOM   10386 C  CA  . PHE B  1 417 ? 2.754   8.022   71.067  1.00 75.54  ? 417  PHE C CA  1 
ATOM   10387 C  C   . PHE B  1 417 ? 3.239   6.918   72.024  1.00 73.79  ? 417  PHE C C   1 
ATOM   10388 O  O   . PHE B  1 417 ? 4.436   6.794   72.265  1.00 71.13  ? 417  PHE C O   1 
ATOM   10389 C  CB  . PHE B  1 417 ? 2.648   9.341   71.832  1.00 70.86  ? 417  PHE C CB  1 
ATOM   10390 C  CG  . PHE B  1 417 ? 3.895   9.703   72.584  1.00 73.26  ? 417  PHE C CG  1 
ATOM   10391 C  CD1 . PHE B  1 417 ? 4.962   10.309  71.934  1.00 73.92  ? 417  PHE C CD1 1 
ATOM   10392 C  CD2 . PHE B  1 417 ? 4.009   9.425   73.936  1.00 67.82  ? 417  PHE C CD2 1 
ATOM   10393 C  CE1 . PHE B  1 417 ? 6.116   10.639  72.622  1.00 66.35  ? 417  PHE C CE1 1 
ATOM   10394 C  CE2 . PHE B  1 417 ? 5.156   9.750   74.627  1.00 68.79  ? 417  PHE C CE2 1 
ATOM   10395 C  CZ  . PHE B  1 417 ? 6.210   10.358  73.973  1.00 69.96  ? 417  PHE C CZ  1 
ATOM   10396 N  N   . LEU B  1 418 ? 2.335   6.117   72.576  1.00 74.35  ? 418  LEU C N   1 
ATOM   10397 C  CA  . LEU B  1 418 ? 2.775   5.098   73.525  1.00 66.53  ? 418  LEU C CA  1 
ATOM   10398 C  C   . LEU B  1 418 ? 3.516   3.961   72.814  1.00 63.89  ? 418  LEU C C   1 
ATOM   10399 O  O   . LEU B  1 418 ? 4.385   3.317   73.404  1.00 58.27  ? 418  LEU C O   1 
ATOM   10400 C  CB  . LEU B  1 418 ? 1.589   4.565   74.332  1.00 69.58  ? 418  LEU C CB  1 
ATOM   10401 C  CG  . LEU B  1 418 ? 1.230   5.409   75.559  1.00 67.77  ? 418  LEU C CG  1 
ATOM   10402 C  CD1 . LEU B  1 418 ? 0.005   4.840   76.252  1.00 75.58  ? 418  LEU C CD1 1 
ATOM   10403 C  CD2 . LEU B  1 418 ? 2.413   5.505   76.530  1.00 65.37  ? 418  LEU C CD2 1 
ATOM   10404 N  N   . ASN B  1 419 ? 3.177   3.736   71.546  1.00 64.47  ? 419  ASN C N   1 
ATOM   10405 C  CA  . ASN B  1 419 ? 3.947   2.851   70.683  1.00 61.00  ? 419  ASN C CA  1 
ATOM   10406 C  C   . ASN B  1 419 ? 5.416   3.218   70.651  1.00 60.78  ? 419  ASN C C   1 
ATOM   10407 O  O   . ASN B  1 419 ? 6.272   2.338   70.628  1.00 63.24  ? 419  ASN C O   1 
ATOM   10408 C  CB  . ASN B  1 419 ? 3.401   2.871   69.262  1.00 61.51  ? 419  ASN C CB  1 
ATOM   10409 C  CG  . ASN B  1 419 ? 2.003   2.322   69.177  1.00 74.74  ? 419  ASN C CG  1 
ATOM   10410 O  OD1 . ASN B  1 419 ? 1.797   1.106   69.239  1.00 73.09  ? 419  ASN C OD1 1 
ATOM   10411 N  ND2 . ASN B  1 419 ? 1.025   3.212   69.038  1.00 79.55  ? 419  ASN C ND2 1 
ATOM   10412 N  N   . VAL B  1 420 ? 5.697   4.517   70.635  1.00 53.24  ? 420  VAL C N   1 
ATOM   10413 C  CA  . VAL B  1 420 ? 7.067   5.011   70.704  1.00 60.90  ? 420  VAL C CA  1 
ATOM   10414 C  C   . VAL B  1 420 ? 7.818   4.363   71.877  1.00 59.28  ? 420  VAL C C   1 
ATOM   10415 O  O   . VAL B  1 420 ? 8.923   3.829   71.726  1.00 53.65  ? 420  VAL C O   1 
ATOM   10416 C  CB  . VAL B  1 420 ? 7.099   6.551   70.856  1.00 59.26  ? 420  VAL C CB  1 
ATOM   10417 C  CG1 . VAL B  1 420 ? 8.514   7.056   70.864  1.00 56.05  ? 420  VAL C CG1 1 
ATOM   10418 C  CG2 . VAL B  1 420 ? 6.305   7.218   69.751  1.00 56.05  ? 420  VAL C CG2 1 
ATOM   10419 N  N   . CYS B  1 421 ? 7.178   4.393   73.039  1.00 62.05  ? 421  CYS C N   1 
ATOM   10420 C  CA  . CYS B  1 421 ? 7.739   3.852   74.270  1.00 58.91  ? 421  CYS C CA  1 
ATOM   10421 C  C   . CYS B  1 421 ? 7.752   2.330   74.269  1.00 52.35  ? 421  CYS C C   1 
ATOM   10422 O  O   . CYS B  1 421 ? 8.759   1.711   74.642  1.00 50.10  ? 421  CYS C O   1 
ATOM   10423 C  CB  . CYS B  1 421 ? 6.948   4.378   75.474  1.00 63.11  ? 421  CYS C CB  1 
ATOM   10424 S  SG  . CYS B  1 421 ? 6.560   6.157   75.320  1.00 70.00  ? 421  CYS C SG  1 
ATOM   10425 N  N   . PHE B  1 422 ? 6.639   1.735   73.845  1.00 48.28  ? 422  PHE C N   1 
ATOM   10426 C  CA  . PHE B  1 422 ? 6.507   0.283   73.834  1.00 57.04  ? 422  PHE C CA  1 
ATOM   10427 C  C   . PHE B  1 422 ? 7.625   -0.332  72.998  1.00 59.26  ? 422  PHE C C   1 
ATOM   10428 O  O   . PHE B  1 422 ? 8.244   -1.328  73.396  1.00 57.45  ? 422  PHE C O   1 
ATOM   10429 C  CB  . PHE B  1 422 ? 5.137   -0.140  73.294  1.00 59.18  ? 422  PHE C CB  1 
ATOM   10430 C  CG  . PHE B  1 422 ? 3.977   0.188   74.214  1.00 62.41  ? 422  PHE C CG  1 
ATOM   10431 C  CD1 . PHE B  1 422 ? 4.191   0.598   75.534  1.00 68.30  ? 422  PHE C CD1 1 
ATOM   10432 C  CD2 . PHE B  1 422 ? 2.667   0.072   73.763  1.00 60.36  ? 422  PHE C CD2 1 
ATOM   10433 C  CE1 . PHE B  1 422 ? 3.111   0.898   76.378  1.00 66.33  ? 422  PHE C CE1 1 
ATOM   10434 C  CE2 . PHE B  1 422 ? 1.588   0.368   74.597  1.00 65.06  ? 422  PHE C CE2 1 
ATOM   10435 C  CZ  . PHE B  1 422 ? 1.811   0.786   75.905  1.00 67.13  ? 422  PHE C CZ  1 
ATOM   10436 N  N   . GLU B  1 423 ? 7.905   0.296   71.857  1.00 58.71  ? 423  GLU C N   1 
ATOM   10437 C  CA  . GLU B  1 423 ? 8.901   -0.219  70.930  1.00 59.99  ? 423  GLU C CA  1 
ATOM   10438 C  C   . GLU B  1 423 ? 10.317  -0.215  71.502  1.00 59.99  ? 423  GLU C C   1 
ATOM   10439 O  O   . GLU B  1 423 ? 11.138  -1.045  71.122  1.00 65.06  ? 423  GLU C O   1 
ATOM   10440 C  CB  . GLU B  1 423 ? 8.865   0.569   69.620  1.00 66.38  ? 423  GLU C CB  1 
ATOM   10441 C  CG  . GLU B  1 423 ? 7.694   0.195   68.708  1.00 74.76  ? 423  GLU C CG  1 
ATOM   10442 C  CD  . GLU B  1 423 ? 7.652   1.021   67.428  1.00 86.01  ? 423  GLU C CD  1 
ATOM   10443 O  OE1 . GLU B  1 423 ? 8.078   2.199   67.462  1.00 85.63  ? 423  GLU C OE1 1 
ATOM   10444 O  OE2 . GLU B  1 423 ? 7.198   0.490   66.386  1.00 81.21  ? 423  GLU C OE2 1 
ATOM   10445 N  N   . VAL B  1 424 ? 10.616  0.697   72.418  1.00 51.69  ? 424  VAL C N   1 
ATOM   10446 C  CA  . VAL B  1 424 ? 11.965  0.721   72.975  1.00 59.43  ? 424  VAL C CA  1 
ATOM   10447 C  C   . VAL B  1 424 ? 12.068  -0.040  74.281  1.00 58.45  ? 424  VAL C C   1 
ATOM   10448 O  O   . VAL B  1 424 ? 13.144  -0.501  74.643  1.00 57.13  ? 424  VAL C O   1 
ATOM   10449 C  CB  . VAL B  1 424 ? 12.438  2.149   73.151  1.00 59.39  ? 424  VAL C CB  1 
ATOM   10450 C  CG1 . VAL B  1 424 ? 13.864  2.216   73.689  1.00 51.56  ? 424  VAL C CG1 1 
ATOM   10451 C  CG2 . VAL B  1 424 ? 12.440  2.722   71.820  1.00 68.12  ? 424  VAL C CG2 1 
ATOM   10452 N  N   . ILE B  1 425 ? 10.948  -0.202  74.970  1.00 57.62  ? 425  ILE C N   1 
ATOM   10453 C  CA  . ILE B  1 425 ? 10.920  -1.125  76.092  1.00 60.19  ? 425  ILE C CA  1 
ATOM   10454 C  C   . ILE B  1 425 ? 11.409  -2.499  75.608  1.00 60.96  ? 425  ILE C C   1 
ATOM   10455 O  O   . ILE B  1 425 ? 12.162  -3.166  76.307  1.00 55.91  ? 425  ILE C O   1 
ATOM   10456 C  CB  . ILE B  1 425 ? 9.517   -1.221  76.714  1.00 59.51  ? 425  ILE C CB  1 
ATOM   10457 C  CG1 . ILE B  1 425 ? 9.163   0.100   77.421  1.00 56.56  ? 425  ILE C CG1 1 
ATOM   10458 C  CG2 . ILE B  1 425 ? 9.462   -2.365  77.702  1.00 62.46  ? 425  ILE C CG2 1 
ATOM   10459 C  CD1 . ILE B  1 425 ? 7.679   0.459   77.377  1.00 52.23  ? 425  ILE C CD1 1 
ATOM   10460 N  N   . THR B  1 426 ? 11.017  -2.888  74.393  1.00 65.47  ? 426  THR C N   1 
ATOM   10461 C  CA  . THR B  1 426 ? 11.531  -4.114  73.783  1.00 64.25  ? 426  THR C CA  1 
ATOM   10462 C  C   . THR B  1 426 ? 13.062  -4.185  73.866  1.00 67.49  ? 426  THR C C   1 
ATOM   10463 O  O   . THR B  1 426 ? 13.631  -5.103  74.459  1.00 66.01  ? 426  THR C O   1 
ATOM   10464 C  CB  . THR B  1 426 ? 11.122  -4.239  72.303  1.00 62.44  ? 426  THR C CB  1 
ATOM   10465 O  OG1 . THR B  1 426 ? 9.695   -4.187  72.182  1.00 68.40  ? 426  THR C OG1 1 
ATOM   10466 C  CG2 . THR B  1 426 ? 11.621  -5.555  71.737  1.00 59.35  ? 426  THR C CG2 1 
ATOM   10467 N  N   . LYS B  1 427 ? 13.726  -3.206  73.268  1.00 67.75  ? 427  LYS C N   1 
ATOM   10468 C  CA  . LYS B  1 427 ? 15.167  -3.109  73.380  1.00 60.84  ? 427  LYS C CA  1 
ATOM   10469 C  C   . LYS B  1 427 ? 15.615  -2.967  74.845  1.00 60.69  ? 427  LYS C C   1 
ATOM   10470 O  O   . LYS B  1 427 ? 16.554  -3.634  75.283  1.00 53.18  ? 427  LYS C O   1 
ATOM   10471 C  CB  . LYS B  1 427 ? 15.667  -1.932  72.548  1.00 59.93  ? 427  LYS C CB  1 
ATOM   10472 C  CG  . LYS B  1 427 ? 15.220  -1.976  71.089  1.00 72.67  ? 427  LYS C CG  1 
ATOM   10473 C  CD  . LYS B  1 427 ? 16.408  -2.235  70.156  1.00 81.12  ? 427  LYS C CD  1 
ATOM   10474 C  CE  . LYS B  1 427 ? 15.973  -2.581  68.734  1.00 70.71  ? 427  LYS C CE  1 
ATOM   10475 N  NZ  . LYS B  1 427 ? 17.142  -2.595  67.794  1.00 75.95  ? 427  LYS C NZ  1 
ATOM   10476 N  N   . ASP B  1 428 ? 14.934  -2.112  75.605  1.00 59.10  ? 428  ASP C N   1 
ATOM   10477 C  CA  . ASP B  1 428 ? 15.408  -1.725  76.939  1.00 65.04  ? 428  ASP C CA  1 
ATOM   10478 C  C   . ASP B  1 428 ? 15.301  -2.860  77.969  1.00 68.70  ? 428  ASP C C   1 
ATOM   10479 O  O   . ASP B  1 428 ? 15.970  -2.839  79.018  1.00 68.68  ? 428  ASP C O   1 
ATOM   10480 C  CB  . ASP B  1 428 ? 14.645  -0.496  77.453  1.00 57.73  ? 428  ASP C CB  1 
ATOM   10481 C  CG  . ASP B  1 428 ? 15.566  0.575   78.011  1.00 57.36  ? 428  ASP C CG  1 
ATOM   10482 O  OD1 . ASP B  1 428 ? 16.794  0.367   78.084  1.00 51.07  ? 428  ASP C OD1 1 
ATOM   10483 O  OD2 . ASP B  1 428 ? 15.053  1.640   78.389  1.00 63.26  ? 428  ASP C OD2 1 
ATOM   10484 N  N   . SER B  1 429 ? 14.465  -3.846  77.666  1.00 63.52  ? 429  SER C N   1 
ATOM   10485 C  CA  . SER B  1 429 ? 14.249  -4.962  78.565  1.00 64.27  ? 429  SER C CA  1 
ATOM   10486 C  C   . SER B  1 429 ? 15.356  -6.016  78.426  1.00 63.57  ? 429  SER C C   1 
ATOM   10487 O  O   . SER B  1 429 ? 15.466  -6.922  79.251  1.00 69.06  ? 429  SER C O   1 
ATOM   10488 C  CB  . SER B  1 429 ? 12.885  -5.581  78.296  1.00 65.16  ? 429  SER C CB  1 
ATOM   10489 O  OG  . SER B  1 429 ? 12.899  -6.221  77.035  1.00 63.22  ? 429  SER C OG  1 
ATOM   10490 N  N   . LEU B  1 430 ? 16.179  -5.890  77.390  1.00 62.33  ? 430  LEU C N   1 
ATOM   10491 C  CA  . LEU B  1 430 ? 17.298  -6.807  77.180  1.00 60.13  ? 430  LEU C CA  1 
ATOM   10492 C  C   . LEU B  1 430 ? 18.609  -6.249  77.717  1.00 61.62  ? 430  LEU C C   1 
ATOM   10493 O  O   . LEU B  1 430 ? 18.801  -5.030  77.788  1.00 64.71  ? 430  LEU C O   1 
ATOM   10494 C  CB  . LEU B  1 430 ? 17.465  -7.137  75.701  1.00 57.83  ? 430  LEU C CB  1 
ATOM   10495 C  CG  . LEU B  1 430 ? 16.250  -7.681  74.970  1.00 57.55  ? 430  LEU C CG  1 
ATOM   10496 C  CD1 . LEU B  1 430 ? 16.706  -8.226  73.636  1.00 60.67  ? 430  LEU C CD1 1 
ATOM   10497 C  CD2 . LEU B  1 430 ? 15.568  -8.753  75.803  1.00 60.20  ? 430  LEU C CD2 1 
ATOM   10498 N  N   . ASN B  1 431 ? 19.517  -7.151  78.071  1.00 61.88  ? 431  ASN C N   1 
ATOM   10499 C  CA  . ASN B  1 431 ? 20.792  -6.769  78.648  1.00 67.12  ? 431  ASN C CA  1 
ATOM   10500 C  C   . ASN B  1 431 ? 21.614  -5.875  77.725  1.00 69.76  ? 431  ASN C C   1 
ATOM   10501 O  O   . ASN B  1 431 ? 22.351  -5.010  78.191  1.00 73.11  ? 431  ASN C O   1 
ATOM   10502 C  CB  . ASN B  1 431 ? 21.609  -8.005  79.006  1.00 74.45  ? 431  ASN C CB  1 
ATOM   10503 C  CG  . ASN B  1 431 ? 22.926  -7.647  79.646  1.00 82.35  ? 431  ASN C CG  1 
ATOM   10504 O  OD1 . ASN B  1 431 ? 22.965  -6.853  80.589  1.00 81.35  ? 431  ASN C OD1 1 
ATOM   10505 N  ND2 . ASN B  1 431 ? 24.019  -8.216  79.131  1.00 85.05  ? 431  ASN C ND2 1 
ATOM   10506 N  N   . SER B  1 432 ? 21.473  -6.080  76.417  1.00 71.47  ? 432  SER C N   1 
ATOM   10507 C  CA  . SER B  1 432 ? 22.305  -5.392  75.422  1.00 68.84  ? 432  SER C CA  1 
ATOM   10508 C  C   . SER B  1 432 ? 21.897  -3.934  75.110  1.00 60.23  ? 432  SER C C   1 
ATOM   10509 O  O   . SER B  1 432 ? 22.448  -3.327  74.196  1.00 60.11  ? 432  SER C O   1 
ATOM   10510 C  CB  . SER B  1 432 ? 22.325  -6.204  74.118  1.00 64.55  ? 432  SER C CB  1 
ATOM   10511 O  OG  . SER B  1 432 ? 21.014  -6.362  73.592  1.00 62.27  ? 432  SER C OG  1 
ATOM   10512 N  N   . SER B  1 433 ? 20.946  -3.366  75.848  1.00 55.73  ? 433  SER C N   1 
ATOM   10513 C  CA  . SER B  1 433 ? 20.685  -1.934  75.696  1.00 51.43  ? 433  SER C CA  1 
ATOM   10514 C  C   . SER B  1 433 ? 21.833  -1.146  76.274  1.00 51.70  ? 433  SER C C   1 
ATOM   10515 O  O   . SER B  1 433 ? 22.892  -1.682  76.637  1.00 52.71  ? 433  SER C O   1 
ATOM   10516 C  CB  . SER B  1 433 ? 19.395  -1.482  76.378  1.00 46.10  ? 433  SER C CB  1 
ATOM   10517 O  OG  . SER B  1 433 ? 18.319  -2.303  75.985  1.00 62.86  ? 433  SER C OG  1 
ATOM   10518 N  N   . ARG B  1 434 ? 21.604  0.147   76.373  1.00 44.01  ? 434  ARG C N   1 
ATOM   10519 C  CA  . ARG B  1 434 ? 22.638  1.045   76.797  1.00 44.15  ? 434  ARG C CA  1 
ATOM   10520 C  C   . ARG B  1 434 ? 21.965  2.239   77.438  1.00 47.96  ? 434  ARG C C   1 
ATOM   10521 O  O   . ARG B  1 434 ? 20.772  2.503   77.197  1.00 43.30  ? 434  ARG C O   1 
ATOM   10522 C  CB  . ARG B  1 434 ? 23.498  1.468   75.609  1.00 47.76  ? 434  ARG C CB  1 
ATOM   10523 C  CG  . ARG B  1 434 ? 22.705  2.251   74.589  1.00 46.96  ? 434  ARG C CG  1 
ATOM   10524 C  CD  . ARG B  1 434 ? 23.583  2.891   73.537  1.00 54.66  ? 434  ARG C CD  1 
ATOM   10525 N  NE  . ARG B  1 434 ? 22.768  3.631   72.581  1.00 57.36  ? 434  ARG C NE  1 
ATOM   10526 C  CZ  . ARG B  1 434 ? 22.370  4.885   72.763  1.00 55.59  ? 434  ARG C CZ  1 
ATOM   10527 N  NH1 . ARG B  1 434 ? 22.729  5.541   73.864  1.00 49.90  ? 434  ARG C NH1 1 
ATOM   10528 N  NH2 . ARG B  1 434 ? 21.624  5.483   71.840  1.00 53.60  ? 434  ARG C NH2 1 
ATOM   10529 N  N   . PRO B  1 435 ? 22.715  2.947   78.283  1.00 45.19  ? 435  PRO C N   1 
ATOM   10530 C  CA  . PRO B  1 435 ? 22.266  4.246   78.796  1.00 53.62  ? 435  PRO C CA  1 
ATOM   10531 C  C   . PRO B  1 435 ? 22.175  5.265   77.654  1.00 50.71  ? 435  PRO C C   1 
ATOM   10532 O  O   . PRO B  1 435 ? 23.100  5.305   76.851  1.00 43.90  ? 435  PRO C O   1 
ATOM   10533 C  CB  . PRO B  1 435 ? 23.359  4.625   79.809  1.00 51.87  ? 435  PRO C CB  1 
ATOM   10534 C  CG  . PRO B  1 435 ? 24.570  3.835   79.397  1.00 46.49  ? 435  PRO C CG  1 
ATOM   10535 C  CD  . PRO B  1 435 ? 24.038  2.560   78.799  1.00 42.71  ? 435  PRO C CD  1 
ATOM   10536 N  N   . ILE B  1 436 ? 21.112  6.073   77.601  1.00 52.10  ? 436  ILE C N   1 
ATOM   10537 C  CA  . ILE B  1 436 ? 20.865  6.929   76.445  1.00 54.84  ? 436  ILE C CA  1 
ATOM   10538 C  C   . ILE B  1 436 ? 21.949  7.968   76.248  1.00 49.65  ? 436  ILE C C   1 
ATOM   10539 O  O   . ILE B  1 436 ? 22.122  8.475   75.152  1.00 53.76  ? 436  ILE C O   1 
ATOM   10540 C  CB  . ILE B  1 436 ? 19.506  7.646   76.528  1.00 54.61  ? 436  ILE C CB  1 
ATOM   10541 C  CG1 . ILE B  1 436 ? 19.601  8.931   77.322  1.00 53.97  ? 436  ILE C CG1 1 
ATOM   10542 C  CG2 . ILE B  1 436 ? 18.469  6.755   77.141  1.00 60.15  ? 436  ILE C CG2 1 
ATOM   10543 C  CD1 . ILE B  1 436 ? 18.250  9.582   77.488  1.00 61.38  ? 436  ILE C CD1 1 
ATOM   10544 N  N   . SER B  1 437 ? 22.669  8.295   77.305  1.00 44.03  ? 437  SER C N   1 
ATOM   10545 C  CA  . SER B  1 437 ? 23.889  9.054   77.156  1.00 44.06  ? 437  SER C CA  1 
ATOM   10546 C  C   . SER B  1 437 ? 25.014  8.070   77.374  1.00 47.33  ? 437  SER C C   1 
ATOM   10547 O  O   . SER B  1 437 ? 24.931  7.247   78.277  1.00 52.57  ? 437  SER C O   1 
ATOM   10548 C  CB  . SER B  1 437 ? 23.951  10.211  78.146  1.00 46.62  ? 437  SER C CB  1 
ATOM   10549 O  OG  . SER B  1 437 ? 25.281  10.655  78.313  1.00 46.09  ? 437  SER C OG  1 
ATOM   10550 N  N   . LYS B  1 438 ? 26.053  8.133   76.551  1.00 45.47  ? 438  LYS C N   1 
ATOM   10551 C  CA  . LYS B  1 438 ? 27.071  7.085   76.545  1.00 50.90  ? 438  LYS C CA  1 
ATOM   10552 C  C   . LYS B  1 438 ? 28.150  7.378   75.515  1.00 52.10  ? 438  LYS C C   1 
ATOM   10553 O  O   . LYS B  1 438 ? 27.844  7.639   74.361  1.00 53.31  ? 438  LYS C O   1 
ATOM   10554 C  CB  . LYS B  1 438 ? 26.441  5.714   76.243  1.00 49.23  ? 438  LYS C CB  1 
ATOM   10555 C  CG  . LYS B  1 438 ? 27.423  4.674   75.741  1.00 51.06  ? 438  LYS C CG  1 
ATOM   10556 C  CD  . LYS B  1 438 ? 26.752  3.659   74.836  1.00 51.83  ? 438  LYS C CD  1 
ATOM   10557 C  CE  . LYS B  1 438 ? 27.790  2.791   74.122  1.00 66.35  ? 438  LYS C CE  1 
ATOM   10558 N  NZ  . LYS B  1 438 ? 27.201  1.887   73.078  1.00 67.91  ? 438  LYS C NZ  1 
ATOM   10559 N  N   . PRO B  1 439 ? 29.419  7.296   75.925  1.00 54.36  ? 439  PRO C N   1 
ATOM   10560 C  CA  . PRO B  1 439 ? 30.547  7.609   75.045  1.00 55.43  ? 439  PRO C CA  1 
ATOM   10561 C  C   . PRO B  1 439 ? 30.433  6.976   73.659  1.00 53.10  ? 439  PRO C C   1 
ATOM   10562 O  O   . PRO B  1 439 ? 29.832  5.912   73.511  1.00 49.70  ? 439  PRO C O   1 
ATOM   10563 C  CB  . PRO B  1 439 ? 31.754  7.044   75.813  1.00 50.64  ? 439  PRO C CB  1 
ATOM   10564 C  CG  . PRO B  1 439 ? 31.358  7.186   77.249  1.00 54.52  ? 439  PRO C CG  1 
ATOM   10565 C  CD  . PRO B  1 439 ? 29.867  6.890   77.272  1.00 55.00  ? 439  PRO C CD  1 
ATOM   10566 N  N   . ALA B  1 440 ? 30.966  7.681   72.661  1.00 52.72  ? 440  ALA C N   1 
ATOM   10567 C  CA  . ALA B  1 440 ? 31.091  7.178   71.297  1.00 51.51  ? 440  ALA C CA  1 
ATOM   10568 C  C   . ALA B  1 440 ? 32.235  7.913   70.603  1.00 50.12  ? 440  ALA C C   1 
ATOM   10569 O  O   . ALA B  1 440 ? 32.324  9.153   70.667  1.00 44.91  ? 440  ALA C O   1 
ATOM   10570 C  CB  . ALA B  1 440 ? 29.791  7.347   70.534  1.00 45.95  ? 440  ALA C CB  1 
ATOM   10571 N  N   . GLU B  1 441 ? 33.108  7.138   69.958  1.00 48.47  ? 441  GLU C N   1 
ATOM   10572 C  CA  A GLU B  1 441 ? 34.263  7.742   69.311  0.60 51.33  ? 441  GLU C CA  1 
ATOM   10573 C  CA  B GLU B  1 441 ? 34.341  7.600   69.310  0.40 51.37  ? 441  GLU C CA  1 
ATOM   10574 C  C   . GLU B  1 441 ? 34.261  7.509   67.794  1.00 52.72  ? 441  GLU C C   1 
ATOM   10575 O  O   . GLU B  1 441 ? 34.081  8.482   67.072  1.00 58.92  ? 441  GLU C O   1 
ATOM   10576 C  CB  A GLU B  1 441 ? 35.565  7.248   69.957  0.60 51.23  ? 441  GLU C CB  1 
ATOM   10577 C  CB  B GLU B  1 441 ? 35.537  6.735   69.735  0.40 51.47  ? 441  GLU C CB  1 
ATOM   10578 C  CG  A GLU B  1 441 ? 35.799  7.807   71.379  0.60 54.01  ? 441  GLU C CG  1 
ATOM   10579 C  CG  B GLU B  1 441 ? 36.320  7.119   70.959  0.40 52.95  ? 441  GLU C CG  1 
ATOM   10580 C  CD  A GLU B  1 441 ? 36.376  9.230   71.405  0.60 53.93  ? 441  GLU C CD  1 
ATOM   10581 C  CD  B GLU B  1 441 ? 37.555  6.240   71.109  0.40 52.86  ? 441  GLU C CD  1 
ATOM   10582 O  OE1 A GLU B  1 441 ? 37.553  9.405   71.017  0.60 54.61  ? 441  GLU C OE1 1 
ATOM   10583 O  OE1 B GLU B  1 441 ? 37.596  5.157   70.479  0.40 51.92  ? 441  GLU C OE1 1 
ATOM   10584 O  OE2 A GLU B  1 441 ? 35.660  10.170  71.823  0.60 52.17  ? 441  GLU C OE2 1 
ATOM   10585 O  OE2 B GLU B  1 441 ? 38.489  6.629   71.840  0.40 55.88  ? 441  GLU C OE2 1 
ATOM   10586 N  N   . THR B  1 442 ? 34.430  6.267   67.323  1.00 49.55  ? 442  THR C N   1 
ATOM   10587 C  CA  . THR B  1 442 ? 34.535  5.969   65.898  1.00 47.82  ? 442  THR C CA  1 
ATOM   10588 C  C   . THR B  1 442 ? 33.262  6.352   65.167  1.00 50.71  ? 442  THR C C   1 
ATOM   10589 O  O   . THR B  1 442 ? 32.201  6.452   65.787  1.00 50.64  ? 442  THR C O   1 
ATOM   10590 C  CB  . THR B  1 442 ? 34.827  4.461   65.622  1.00 48.57  ? 442  THR C CB  1 
ATOM   10591 O  OG1 . THR B  1 442 ? 33.674  3.675   65.920  1.00 43.59  ? 442  THR C OG1 1 
ATOM   10592 C  CG2 . THR B  1 442 ? 36.010  3.972   66.421  1.00 46.26  ? 442  THR C CG2 1 
ATOM   10593 N  N   . PRO B  1 443 ? 33.365  6.577   63.845  1.00 44.27  ? 443  PRO C N   1 
ATOM   10594 C  CA  . PRO B  1 443 ? 32.193  6.958   63.046  1.00 51.06  ? 443  PRO C CA  1 
ATOM   10595 C  C   . PRO B  1 443 ? 31.060  5.940   63.147  1.00 46.56  ? 443  PRO C C   1 
ATOM   10596 O  O   . PRO B  1 443 ? 29.878  6.303   63.219  1.00 39.88  ? 443  PRO C O   1 
ATOM   10597 C  CB  . PRO B  1 443 ? 32.751  7.029   61.619  1.00 50.24  ? 443  PRO C CB  1 
ATOM   10598 C  CG  . PRO B  1 443 ? 34.189  7.421   61.815  1.00 49.75  ? 443  PRO C CG  1 
ATOM   10599 C  CD  . PRO B  1 443 ? 34.620  6.717   63.082  1.00 48.81  ? 443  PRO C CD  1 
ATOM   10600 N  N   . THR B  1 444 ? 31.422  4.668   63.173  1.00 46.76  ? 444  THR C N   1 
ATOM   10601 C  CA  . THR B  1 444 ? 30.407  3.630   63.275  1.00 50.47  ? 444  THR C CA  1 
ATOM   10602 C  C   . THR B  1 444 ? 29.727  3.708   64.637  1.00 45.32  ? 444  THR C C   1 
ATOM   10603 O  O   . THR B  1 444 ? 28.505  3.595   64.735  1.00 42.44  ? 444  THR C O   1 
ATOM   10604 C  CB  . THR B  1 444 ? 31.008  2.249   63.042  1.00 48.78  ? 444  THR C CB  1 
ATOM   10605 O  OG1 . THR B  1 444 ? 31.718  2.275   61.805  1.00 50.86  ? 444  THR C OG1 1 
ATOM   10606 C  CG2 . THR B  1 444 ? 29.928  1.183   62.955  1.00 55.30  ? 444  THR C CG2 1 
ATOM   10607 N  N   . GLN B  1 445 ? 30.507  3.946   65.687  1.00 47.62  ? 445  GLN C N   1 
ATOM   10608 C  CA  . GLN B  1 445 ? 29.921  4.051   67.025  1.00 50.58  ? 445  GLN C CA  1 
ATOM   10609 C  C   . GLN B  1 445 ? 28.921  5.180   67.078  1.00 46.76  ? 445  GLN C C   1 
ATOM   10610 O  O   . GLN B  1 445 ? 27.851  5.029   67.648  1.00 49.77  ? 445  GLN C O   1 
ATOM   10611 C  CB  . GLN B  1 445 ? 30.989  4.272   68.087  1.00 49.16  ? 445  GLN C CB  1 
ATOM   10612 C  CG  . GLN B  1 445 ? 31.787  3.046   68.415  1.00 48.59  ? 445  GLN C CG  1 
ATOM   10613 C  CD  . GLN B  1 445 ? 33.063  3.388   69.138  1.00 55.25  ? 445  GLN C CD  1 
ATOM   10614 O  OE1 . GLN B  1 445 ? 33.326  4.556   69.424  1.00 53.04  ? 445  GLN C OE1 1 
ATOM   10615 N  NE2 . GLN B  1 445 ? 33.877  2.375   69.423  1.00 55.88  ? 445  GLN C NE2 1 
ATOM   10616 N  N   . ILE B  1 446 ? 29.290  6.302   66.466  1.00 45.61  ? 446  ILE C N   1 
ATOM   10617 C  CA  . ILE B  1 446 ? 28.476  7.503   66.440  1.00 42.36  ? 446  ILE C CA  1 
ATOM   10618 C  C   . ILE B  1 446 ? 27.159  7.251   65.710  1.00 41.09  ? 446  ILE C C   1 
ATOM   10619 O  O   . ILE B  1 446 ? 26.127  7.827   66.039  1.00 40.38  ? 446  ILE C O   1 
ATOM   10620 C  CB  . ILE B  1 446 ? 29.243  8.663   65.771  1.00 45.44  ? 446  ILE C CB  1 
ATOM   10621 C  CG1 . ILE B  1 446 ? 30.535  8.955   66.540  1.00 45.05  ? 446  ILE C CG1 1 
ATOM   10622 C  CG2 . ILE B  1 446 ? 28.368  9.910   65.674  1.00 40.13  ? 446  ILE C CG2 1 
ATOM   10623 C  CD1 . ILE B  1 446 ? 31.442  9.977   65.864  1.00 45.82  ? 446  ILE C CD1 1 
ATOM   10624 N  N   . GLN B  1 447 ? 27.181  6.374   64.723  1.00 43.55  ? 447  GLN C N   1 
ATOM   10625 C  CA  . GLN B  1 447 ? 25.960  6.067   63.997  1.00 45.73  ? 447  GLN C CA  1 
ATOM   10626 C  C   . GLN B  1 447 ? 25.081  5.118   64.783  1.00 43.59  ? 447  GLN C C   1 
ATOM   10627 O  O   . GLN B  1 447 ? 23.857  5.139   64.657  1.00 46.10  ? 447  GLN C O   1 
ATOM   10628 C  CB  . GLN B  1 447 ? 26.291  5.473   62.637  1.00 49.37  ? 447  GLN C CB  1 
ATOM   10629 C  CG  . GLN B  1 447 ? 27.202  6.350   61.855  1.00 55.77  ? 447  GLN C CG  1 
ATOM   10630 C  CD  . GLN B  1 447 ? 27.505  5.787   60.499  1.00 58.30  ? 447  GLN C CD  1 
ATOM   10631 O  OE1 . GLN B  1 447 ? 28.303  4.858   60.360  1.00 57.98  ? 447  GLN C OE1 1 
ATOM   10632 N  NE2 . GLN B  1 447 ? 26.862  6.339   59.484  1.00 52.12  ? 447  GLN C NE2 1 
ATOM   10633 N  N   . GLU B  1 448 ? 25.714  4.279   65.595  1.00 42.61  ? 448  GLU C N   1 
ATOM   10634 C  CA  . GLU B  1 448 ? 24.971  3.359   66.445  1.00 42.87  ? 448  GLU C CA  1 
ATOM   10635 C  C   . GLU B  1 448 ? 24.135  4.139   67.456  1.00 41.47  ? 448  GLU C C   1 
ATOM   10636 O  O   . GLU B  1 448 ? 23.072  3.686   67.896  1.00 41.35  ? 448  GLU C O   1 
ATOM   10637 C  CB  . GLU B  1 448 ? 25.934  2.389   67.132  1.00 45.26  ? 448  GLU C CB  1 
ATOM   10638 C  CG  . GLU B  1 448 ? 26.585  1.451   66.129  1.00 51.50  ? 448  GLU C CG  1 
ATOM   10639 C  CD  . GLU B  1 448 ? 27.488  0.416   66.748  1.00 53.30  ? 448  GLU C CD  1 
ATOM   10640 O  OE1 . GLU B  1 448 ? 28.692  0.715   66.929  1.00 52.45  ? 448  GLU C OE1 1 
ATOM   10641 O  OE2 . GLU B  1 448 ? 26.995  -0.705  67.018  1.00 54.08  ? 448  GLU C OE2 1 
ATOM   10642 N  N   . MET B  1 449 ? 24.619  5.332   67.792  1.00 37.74  ? 449  MET C N   1 
ATOM   10643 C  CA  . MET B  1 449 ? 23.938  6.234   68.705  1.00 41.34  ? 449  MET C CA  1 
ATOM   10644 C  C   . MET B  1 449 ? 22.576  6.701   68.205  1.00 40.27  ? 449  MET C C   1 
ATOM   10645 O  O   . MET B  1 449 ? 21.767  7.173   68.980  1.00 41.22  ? 449  MET C O   1 
ATOM   10646 C  CB  . MET B  1 449 ? 24.823  7.445   68.982  1.00 41.24  ? 449  MET C CB  1 
ATOM   10647 C  CG  . MET B  1 449 ? 26.088  7.108   69.760  1.00 51.80  ? 449  MET C CG  1 
ATOM   10648 S  SD  . MET B  1 449 ? 25.757  6.275   71.343  1.00 53.44  ? 449  MET C SD  1 
ATOM   10649 C  CE  . MET B  1 449 ? 24.798  7.512   72.216  1.00 44.27  ? 449  MET C CE  1 
ATOM   10650 N  N   . PHE B  1 450 ? 22.331  6.585   66.908  1.00 42.91  ? 450  PHE C N   1 
ATOM   10651 C  CA  . PHE B  1 450 ? 21.075  7.047   66.336  1.00 46.89  ? 450  PHE C CA  1 
ATOM   10652 C  C   . PHE B  1 450 ? 20.089  5.905   66.364  1.00 46.53  ? 450  PHE C C   1 
ATOM   10653 O  O   . PHE B  1 450 ? 19.863  5.273   65.334  1.00 44.98  ? 450  PHE C O   1 
ATOM   10654 C  CB  . PHE B  1 450 ? 21.267  7.548   64.894  1.00 44.99  ? 450  PHE C CB  1 
ATOM   10655 C  CG  . PHE B  1 450 ? 21.915  8.895   64.797  1.00 41.87  ? 450  PHE C CG  1 
ATOM   10656 C  CD1 . PHE B  1 450 ? 23.289  9.028   64.899  1.00 41.76  ? 450  PHE C CD1 1 
ATOM   10657 C  CD2 . PHE B  1 450 ? 21.150  10.034  64.595  1.00 37.51  ? 450  PHE C CD2 1 
ATOM   10658 C  CE1 . PHE B  1 450 ? 23.889  10.279  64.808  1.00 39.52  ? 450  PHE C CE1 1 
ATOM   10659 C  CE2 . PHE B  1 450 ? 21.740  11.282  64.514  1.00 37.03  ? 450  PHE C CE2 1 
ATOM   10660 C  CZ  . PHE B  1 450 ? 23.107  11.413  64.617  1.00 36.50  ? 450  PHE C CZ  1 
ATOM   10661 N  N   . ASP B  1 451 ? 19.515  5.625   67.536  1.00 47.40  ? 451  ASP C N   1 
ATOM   10662 C  CA  . ASP B  1 451 ? 18.684  4.425   67.691  1.00 49.21  ? 451  ASP C CA  1 
ATOM   10663 C  C   . ASP B  1 451 ? 17.438  4.657   68.495  1.00 49.30  ? 451  ASP C C   1 
ATOM   10664 O  O   . ASP B  1 451 ? 17.142  5.780   68.888  1.00 49.30  ? 451  ASP C O   1 
ATOM   10665 C  CB  . ASP B  1 451 ? 19.478  3.280   68.329  1.00 44.18  ? 451  ASP C CB  1 
ATOM   10666 C  CG  . ASP B  1 451 ? 20.022  3.621   69.707  1.00 52.24  ? 451  ASP C CG  1 
ATOM   10667 O  OD1 . ASP B  1 451 ? 19.692  4.697   70.255  1.00 51.60  ? 451  ASP C OD1 1 
ATOM   10668 O  OD2 . ASP B  1 451 ? 20.789  2.792   70.255  1.00 57.43  ? 451  ASP C OD2 1 
ATOM   10669 N  N   . GLU B  1 452 ? 16.716  3.572   68.746  1.00 53.43  ? 452  GLU C N   1 
ATOM   10670 C  CA  . GLU B  1 452 ? 15.450  3.633   69.464  1.00 53.18  ? 452  GLU C CA  1 
ATOM   10671 C  C   . GLU B  1 452 ? 15.644  4.217   70.862  1.00 48.26  ? 452  GLU C C   1 
ATOM   10672 O  O   . GLU B  1 452 ? 14.755  4.874   71.412  1.00 46.04  ? 452  GLU C O   1 
ATOM   10673 C  CB  . GLU B  1 452 ? 14.825  2.243   69.542  1.00 56.50  ? 452  GLU C CB  1 
ATOM   10674 C  CG  . GLU B  1 452 ? 14.239  1.714   68.222  1.00 63.91  ? 452  GLU C CG  1 
ATOM   10675 C  CD  . GLU B  1 452 ? 15.176  0.754   67.484  1.00 75.17  ? 452  GLU C CD  1 
ATOM   10676 O  OE1 . GLU B  1 452 ? 16.269  0.439   68.014  1.00 69.37  ? 452  GLU C OE1 1 
ATOM   10677 O  OE2 . GLU B  1 452 ? 14.821  0.321   66.360  1.00 82.83  ? 452  GLU C OE2 1 
ATOM   10678 N  N   . VAL B  1 453 ? 16.827  4.001   71.418  1.00 39.81  ? 453  VAL C N   1 
ATOM   10679 C  CA  . VAL B  1 453 ? 17.127  4.478   72.751  1.00 48.25  ? 453  VAL C CA  1 
ATOM   10680 C  C   . VAL B  1 453 ? 17.256  6.010   72.764  1.00 52.41  ? 453  VAL C C   1 
ATOM   10681 O  O   . VAL B  1 453 ? 16.637  6.696   73.600  1.00 49.15  ? 453  VAL C O   1 
ATOM   10682 C  CB  . VAL B  1 453 ? 18.413  3.801   73.302  1.00 45.91  ? 453  VAL C CB  1 
ATOM   10683 C  CG1 . VAL B  1 453 ? 19.029  4.621   74.419  1.00 50.37  ? 453  VAL C CG1 1 
ATOM   10684 C  CG2 . VAL B  1 453 ? 18.086  2.432   73.818  1.00 43.59  ? 453  VAL C CG2 1 
ATOM   10685 N  N   . SER B  1 454 ? 18.049  6.536   71.830  1.00 48.20  ? 454  SER C N   1 
ATOM   10686 C  CA  . SER B  1 454 ? 18.214  7.974   71.677  1.00 46.74  ? 454  SER C CA  1 
ATOM   10687 C  C   . SER B  1 454 ? 16.914  8.684   71.312  1.00 46.34  ? 454  SER C C   1 
ATOM   10688 O  O   . SER B  1 454 ? 16.584  9.715   71.879  1.00 49.10  ? 454  SER C O   1 
ATOM   10689 C  CB  . SER B  1 454 ? 19.264  8.265   70.621  1.00 43.40  ? 454  SER C CB  1 
ATOM   10690 O  OG  . SER B  1 454 ? 20.554  8.032   71.139  1.00 46.88  ? 454  SER C OG  1 
ATOM   10691 N  N   . TYR B  1 455 ? 16.177  8.126   70.366  1.00 46.20  ? 455  TYR C N   1 
ATOM   10692 C  CA  . TYR B  1 455 ? 15.008  8.805   69.837  1.00 50.59  ? 455  TYR C CA  1 
ATOM   10693 C  C   . TYR B  1 455 ? 13.837  8.653   70.773  1.00 49.17  ? 455  TYR C C   1 
ATOM   10694 O  O   . TYR B  1 455 ? 13.352  9.636   71.329  1.00 46.35  ? 455  TYR C O   1 
ATOM   10695 C  CB  . TYR B  1 455 ? 14.628  8.266   68.451  1.00 48.81  ? 455  TYR C CB  1 
ATOM   10696 C  CG  . TYR B  1 455 ? 15.467  8.795   67.297  1.00 52.66  ? 455  TYR C CG  1 
ATOM   10697 C  CD1 . TYR B  1 455 ? 16.821  8.495   67.194  1.00 47.19  ? 455  TYR C CD1 1 
ATOM   10698 C  CD2 . TYR B  1 455 ? 14.889  9.565   66.285  1.00 55.57  ? 455  TYR C CD2 1 
ATOM   10699 C  CE1 . TYR B  1 455 ? 17.577  8.965   66.141  1.00 50.49  ? 455  TYR C CE1 1 
ATOM   10700 C  CE2 . TYR B  1 455 ? 15.642  10.039  65.215  1.00 45.30  ? 455  TYR C CE2 1 
ATOM   10701 C  CZ  . TYR B  1 455 ? 16.984  9.734   65.152  1.00 46.88  ? 455  TYR C CZ  1 
ATOM   10702 O  OH  . TYR B  1 455 ? 17.744  10.199  64.108  1.00 41.52  ? 455  TYR C OH  1 
ATOM   10703 N  N   . ASN B  1 456 ? 13.403  7.406   70.935  1.00 51.89  ? 456  ASN C N   1 
ATOM   10704 C  CA  . ASN B  1 456 ? 12.151  7.079   71.605  1.00 54.91  ? 456  ASN C CA  1 
ATOM   10705 C  C   . ASN B  1 456 ? 12.248  7.161   73.130  1.00 53.90  ? 456  ASN C C   1 
ATOM   10706 O  O   . ASN B  1 456 ? 11.394  7.766   73.780  1.00 51.41  ? 456  ASN C O   1 
ATOM   10707 C  CB  . ASN B  1 456 ? 11.667  5.675   71.240  1.00 51.38  ? 456  ASN C CB  1 
ATOM   10708 C  CG  . ASN B  1 456 ? 11.577  5.401   69.715  1.00 61.90  ? 456  ASN C CG  1 
ATOM   10709 O  OD1 . ASN B  1 456 ? 12.486  5.709   68.933  1.00 55.46  ? 456  ASN C OD1 1 
ATOM   10710 N  ND2 . ASN B  1 456 ? 10.476  4.767   69.310  1.00 58.69  ? 456  ASN C ND2 1 
ATOM   10711 N  N   . LYS B  1 457 ? 13.274  6.537   73.700  1.00 51.13  ? 457  LYS C N   1 
ATOM   10712 C  CA  . LYS B  1 457 ? 13.409  6.536   75.140  1.00 48.75  ? 457  LYS C CA  1 
ATOM   10713 C  C   . LYS B  1 457 ? 13.731  7.944   75.583  1.00 56.21  ? 457  LYS C C   1 
ATOM   10714 O  O   . LYS B  1 457 ? 13.252  8.415   76.624  1.00 49.52  ? 457  LYS C O   1 
ATOM   10715 C  CB  . LYS B  1 457 ? 14.486  5.573   75.612  1.00 51.98  ? 457  LYS C CB  1 
ATOM   10716 C  CG  . LYS B  1 457 ? 14.754  5.697   77.098  1.00 46.16  ? 457  LYS C CG  1 
ATOM   10717 C  CD  . LYS B  1 457 ? 15.760  4.690   77.585  1.00 55.06  ? 457  LYS C CD  1 
ATOM   10718 C  CE  . LYS B  1 457 ? 15.874  4.762   79.110  1.00 56.24  ? 457  LYS C CE  1 
ATOM   10719 N  NZ  . LYS B  1 457 ? 16.747  3.694   79.649  1.00 56.47  ? 457  LYS C NZ  1 
ATOM   10720 N  N   . GLY B  1 458 ? 14.547  8.612   74.772  1.00 53.55  ? 458  GLY C N   1 
ATOM   10721 C  CA  . GLY B  1 458 ? 14.816  10.019  74.961  1.00 48.01  ? 458  GLY C CA  1 
ATOM   10722 C  C   . GLY B  1 458 ? 13.517  10.802  74.942  1.00 51.11  ? 458  GLY C C   1 
ATOM   10723 O  O   . GLY B  1 458 ? 13.362  11.779  75.662  1.00 56.39  ? 458  GLY C O   1 
ATOM   10724 N  N   . ALA B  1 459 ? 12.563  10.369  74.131  1.00 48.38  ? 459  ALA C N   1 
ATOM   10725 C  CA  . ALA B  1 459 ? 11.342  11.138  73.997  1.00 52.97  ? 459  ALA C CA  1 
ATOM   10726 C  C   . ALA B  1 459 ? 10.393  10.801  75.133  1.00 57.45  ? 459  ALA C C   1 
ATOM   10727 O  O   . ALA B  1 459 ? 9.696   11.669  75.636  1.00 60.42  ? 459  ALA C O   1 
ATOM   10728 C  CB  . ALA B  1 459 ? 10.689  10.886  72.645  1.00 47.48  ? 459  ALA C CB  1 
ATOM   10729 N  N   . CYS B  1 460 ? 10.386  9.536   75.543  1.00 59.94  ? 460  CYS C N   1 
ATOM   10730 C  CA  . CYS B  1 460 ? 9.491   9.062   76.591  1.00 55.36  ? 460  CYS C CA  1 
ATOM   10731 C  C   . CYS B  1 460 ? 9.886   9.584   77.967  1.00 60.71  ? 460  CYS C C   1 
ATOM   10732 O  O   . CYS B  1 460 ? 9.028   10.024  78.731  1.00 61.04  ? 460  CYS C O   1 
ATOM   10733 C  CB  . CYS B  1 460 ? 9.450   7.538   76.604  1.00 54.53  ? 460  CYS C CB  1 
ATOM   10734 S  SG  . CYS B  1 460 ? 8.468   6.855   75.209  1.00 63.94  ? 460  CYS C SG  1 
ATOM   10735 N  N   . ILE B  1 461 ? 11.177  9.556   78.283  1.00 54.91  ? 461  ILE C N   1 
ATOM   10736 C  CA  . ILE B  1 461 ? 11.609  10.065  79.574  1.00 52.75  ? 461  ILE C CA  1 
ATOM   10737 C  C   . ILE B  1 461 ? 11.491  11.578  79.596  1.00 58.63  ? 461  ILE C C   1 
ATOM   10738 O  O   . ILE B  1 461 ? 11.427  12.178  80.658  1.00 62.52  ? 461  ILE C O   1 
ATOM   10739 C  CB  . ILE B  1 461 ? 13.060  9.657   79.939  1.00 56.92  ? 461  ILE C CB  1 
ATOM   10740 C  CG1 . ILE B  1 461 ? 14.086  10.347  79.036  1.00 52.16  ? 461  ILE C CG1 1 
ATOM   10741 C  CG2 . ILE B  1 461 ? 13.215  8.125   79.966  1.00 59.65  ? 461  ILE C CG2 1 
ATOM   10742 C  CD1 . ILE B  1 461 ? 15.489  10.420  79.659  1.00 52.95  ? 461  ILE C CD1 1 
ATOM   10743 N  N   . LEU B  1 462 ? 11.462  12.202  78.426  1.00 62.15  ? 462  LEU C N   1 
ATOM   10744 C  CA  . LEU B  1 462 ? 11.130  13.613  78.373  1.00 57.97  ? 462  LEU C CA  1 
ATOM   10745 C  C   . LEU B  1 462 ? 9.658   13.768  78.682  1.00 63.05  ? 462  LEU C C   1 
ATOM   10746 O  O   . LEU B  1 462 ? 9.259   14.736  79.315  1.00 66.81  ? 462  LEU C O   1 
ATOM   10747 C  CB  . LEU B  1 462 ? 11.447  14.225  77.014  1.00 57.63  ? 462  LEU C CB  1 
ATOM   10748 C  CG  . LEU B  1 462 ? 12.862  14.764  76.838  1.00 61.02  ? 462  LEU C CG  1 
ATOM   10749 C  CD1 . LEU B  1 462 ? 13.052  15.289  75.407  1.00 59.66  ? 462  LEU C CD1 1 
ATOM   10750 C  CD2 . LEU B  1 462 ? 13.165  15.843  77.865  1.00 54.68  ? 462  LEU C CD2 1 
ATOM   10751 N  N   . ASN B  1 463 ? 8.851   12.815  78.230  1.00 59.23  ? 463  ASN C N   1 
ATOM   10752 C  CA  . ASN B  1 463 ? 7.422   12.878  78.489  1.00 65.03  ? 463  ASN C CA  1 
ATOM   10753 C  C   . ASN B  1 463 ? 7.137   12.710  79.985  1.00 69.75  ? 463  ASN C C   1 
ATOM   10754 O  O   . ASN B  1 463 ? 6.312   13.425  80.564  1.00 74.62  ? 463  ASN C O   1 
ATOM   10755 C  CB  . ASN B  1 463 ? 6.682   11.813  77.688  1.00 60.81  ? 463  ASN C CB  1 
ATOM   10756 C  CG  . ASN B  1 463 ? 5.203   12.084  77.605  1.00 65.24  ? 463  ASN C CG  1 
ATOM   10757 O  OD1 . ASN B  1 463 ? 4.776   13.234  77.550  1.00 64.05  ? 463  ASN C OD1 1 
ATOM   10758 N  ND2 . ASN B  1 463 ? 4.409   11.025  77.599  1.00 71.17  ? 463  ASN C ND2 1 
ATOM   10759 N  N   . MET B  1 464 ? 7.836   11.758  80.596  1.00 63.85  ? 464  MET C N   1 
ATOM   10760 C  CA  . MET B  1 464 ? 7.718   11.483  82.020  1.00 62.52  ? 464  MET C CA  1 
ATOM   10761 C  C   . MET B  1 464 ? 7.898   12.775  82.809  1.00 65.08  ? 464  MET C C   1 
ATOM   10762 O  O   . MET B  1 464 ? 6.987   13.215  83.501  1.00 63.96  ? 464  MET C O   1 
ATOM   10763 C  CB  . MET B  1 464 ? 8.753   10.431  82.441  1.00 54.75  ? 464  MET C CB  1 
ATOM   10764 C  CG  . MET B  1 464 ? 8.467   9.719   83.738  1.00 51.38  ? 464  MET C CG  1 
ATOM   10765 S  SD  . MET B  1 464 ? 9.492   8.245   83.952  1.00 61.61  ? 464  MET C SD  1 
ATOM   10766 C  CE  . MET B  1 464 ? 11.120  8.953   84.151  1.00 59.15  ? 464  MET C CE  1 
ATOM   10767 N  N   . LEU B  1 465 ? 9.057   13.403  82.656  1.00 61.43  ? 465  LEU C N   1 
ATOM   10768 C  CA  . LEU B  1 465 ? 9.394   14.583  83.438  1.00 63.72  ? 465  LEU C CA  1 
ATOM   10769 C  C   . LEU B  1 465 ? 8.510   15.777  83.108  1.00 67.96  ? 465  LEU C C   1 
ATOM   10770 O  O   . LEU B  1 465 ? 8.383   16.697  83.909  1.00 69.87  ? 465  LEU C O   1 
ATOM   10771 C  CB  . LEU B  1 465 ? 10.855  14.953  83.230  1.00 63.06  ? 465  LEU C CB  1 
ATOM   10772 C  CG  . LEU B  1 465 ? 11.331  16.149  84.047  1.00 67.36  ? 465  LEU C CG  1 
ATOM   10773 C  CD1 . LEU B  1 465 ? 11.102  15.905  85.522  1.00 66.26  ? 465  LEU C CD1 1 
ATOM   10774 C  CD2 . LEU B  1 465 ? 12.785  16.461  83.762  1.00 64.06  ? 465  LEU C CD2 1 
ATOM   10775 N  N   . LYS B  1 466 ? 7.887   15.769  81.937  1.00 64.69  ? 466  LYS C N   1 
ATOM   10776 C  CA  . LYS B  1 466 ? 6.976   16.848  81.611  1.00 68.97  ? 466  LYS C CA  1 
ATOM   10777 C  C   . LYS B  1 466 ? 5.737   16.701  82.458  1.00 70.02  ? 466  LYS C C   1 
ATOM   10778 O  O   . LYS B  1 466 ? 5.242   17.684  83.005  1.00 75.66  ? 466  LYS C O   1 
ATOM   10779 C  CB  . LYS B  1 466 ? 6.593   16.862  80.135  1.00 71.30  ? 466  LYS C CB  1 
ATOM   10780 C  CG  . LYS B  1 466 ? 5.334   17.668  79.852  1.00 66.29  ? 466  LYS C CG  1 
ATOM   10781 C  CD  . LYS B  1 466 ? 4.313   16.829  79.102  1.00 71.98  ? 466  LYS C CD  1 
ATOM   10782 C  CE  . LYS B  1 466 ? 2.936   17.449  79.174  1.00 76.85  ? 466  LYS C CE  1 
ATOM   10783 N  NZ  . LYS B  1 466 ? 2.063   16.976  78.069  1.00 83.08  ? 466  LYS C NZ  1 
ATOM   10784 N  N   . ASP B  1 467 ? 5.238   15.474  82.563  1.00 66.03  ? 467  ASP C N   1 
ATOM   10785 C  CA  . ASP B  1 467 ? 4.072   15.197  83.400  1.00 73.54  ? 467  ASP C CA  1 
ATOM   10786 C  C   . ASP B  1 467 ? 4.343   15.521  84.880  1.00 75.49  ? 467  ASP C C   1 
ATOM   10787 O  O   . ASP B  1 467 ? 3.480   16.034  85.593  1.00 74.76  ? 467  ASP C O   1 
ATOM   10788 C  CB  . ASP B  1 467 ? 3.661   13.737  83.255  1.00 69.80  ? 467  ASP C CB  1 
ATOM   10789 C  CG  . ASP B  1 467 ? 2.254   13.488  83.720  1.00 72.72  ? 467  ASP C CG  1 
ATOM   10790 O  OD1 . ASP B  1 467 ? 1.350   14.230  83.275  1.00 74.12  ? 467  ASP C OD1 1 
ATOM   10791 O  OD2 . ASP B  1 467 ? 2.058   12.554  84.529  1.00 75.03  ? 467  ASP C OD2 1 
ATOM   10792 N  N   . PHE B  1 468 ? 5.568   15.231  85.305  1.00 71.52  ? 468  PHE C N   1 
ATOM   10793 C  CA  . PHE B  1 468 ? 6.015   15.360  86.681  1.00 65.55  ? 468  PHE C CA  1 
ATOM   10794 C  C   . PHE B  1 468 ? 6.193   16.813  87.107  1.00 71.39  ? 468  PHE C C   1 
ATOM   10795 O  O   . PHE B  1 468 ? 6.126   17.123  88.297  1.00 73.41  ? 468  PHE C O   1 
ATOM   10796 C  CB  . PHE B  1 468 ? 7.330   14.587  86.851  1.00 69.56  ? 468  PHE C CB  1 
ATOM   10797 C  CG  . PHE B  1 468 ? 8.033   14.829  88.163  1.00 77.00  ? 468  PHE C CG  1 
ATOM   10798 C  CD1 . PHE B  1 468 ? 8.965   15.854  88.292  1.00 69.10  ? 468  PHE C CD1 1 
ATOM   10799 C  CD2 . PHE B  1 468 ? 7.790   14.011  89.256  1.00 74.66  ? 468  PHE C CD2 1 
ATOM   10800 C  CE1 . PHE B  1 468 ? 9.617   16.075  89.486  1.00 73.37  ? 468  PHE C CE1 1 
ATOM   10801 C  CE2 . PHE B  1 468 ? 8.443   14.227  90.456  1.00 72.76  ? 468  PHE C CE2 1 
ATOM   10802 C  CZ  . PHE B  1 468 ? 9.356   15.258  90.573  1.00 76.12  ? 468  PHE C CZ  1 
ATOM   10803 N  N   . LEU B  1 469 ? 6.432   17.695  86.142  1.00 63.69  ? 469  LEU C N   1 
ATOM   10804 C  CA  . LEU B  1 469 ? 6.624   19.114  86.432  1.00 64.73  ? 469  LEU C CA  1 
ATOM   10805 C  C   . LEU B  1 469 ? 5.478   19.972  85.886  1.00 65.90  ? 469  LEU C C   1 
ATOM   10806 O  O   . LEU B  1 469 ? 5.495   21.200  86.020  1.00 70.31  ? 469  LEU C O   1 
ATOM   10807 C  CB  . LEU B  1 469 ? 7.950   19.614  85.850  1.00 64.50  ? 469  LEU C CB  1 
ATOM   10808 C  CG  . LEU B  1 469 ? 9.294   18.970  86.203  1.00 67.22  ? 469  LEU C CG  1 
ATOM   10809 C  CD1 . LEU B  1 469 ? 10.366  19.472  85.240  1.00 67.52  ? 469  LEU C CD1 1 
ATOM   10810 C  CD2 . LEU B  1 469 ? 9.726   19.236  87.640  1.00 62.93  ? 469  LEU C CD2 1 
ATOM   10811 N  N   . GLY B  1 470 ? 4.491   19.330  85.266  1.00 62.06  ? 470  GLY C N   1 
ATOM   10812 C  CA  . GLY B  1 470 ? 3.417   20.040  84.587  1.00 66.38  ? 470  GLY C CA  1 
ATOM   10813 C  C   . GLY B  1 470 ? 3.837   20.695  83.275  1.00 73.18  ? 470  GLY C C   1 
ATOM   10814 O  O   . GLY B  1 470 ? 5.001   21.062  83.098  1.00 68.51  ? 470  GLY C O   1 
ATOM   10815 N  N   . GLU B  1 471 ? 2.886   20.843  82.353  1.00 74.99  ? 471  GLU C N   1 
ATOM   10816 C  CA  A GLU B  1 471 ? 3.190   21.471  81.069  0.52 73.46  ? 471  GLU C CA  1 
ATOM   10817 C  CA  B GLU B  1 471 ? 3.107   21.515  81.073  0.48 73.46  ? 471  GLU C CA  1 
ATOM   10818 C  C   . GLU B  1 471 ? 3.817   22.851  81.254  1.00 76.93  ? 471  GLU C C   1 
ATOM   10819 O  O   . GLU B  1 471 ? 4.727   23.214  80.506  1.00 77.01  ? 471  GLU C O   1 
ATOM   10820 C  CB  A GLU B  1 471 ? 1.937   21.576  80.194  0.52 73.64  ? 471  GLU C CB  1 
ATOM   10821 C  CB  B GLU B  1 471 ? 1.771   21.748  80.352  0.48 73.61  ? 471  GLU C CB  1 
ATOM   10822 C  CG  A GLU B  1 471 ? 2.184   22.178  78.803  0.52 76.61  ? 471  GLU C CG  1 
ATOM   10823 C  CG  B GLU B  1 471 ? 1.057   20.486  79.871  0.48 76.27  ? 471  GLU C CG  1 
ATOM   10824 C  CD  A GLU B  1 471 ? 3.271   21.456  77.999  0.52 77.15  ? 471  GLU C CD  1 
ATOM   10825 C  CD  B GLU B  1 471 ? 0.195   19.826  80.939  0.48 77.24  ? 471  GLU C CD  1 
ATOM   10826 O  OE1 A GLU B  1 471 ? 3.089   20.269  77.640  0.52 77.83  ? 471  GLU C OE1 1 
ATOM   10827 O  OE1 B GLU B  1 471 ? 0.023   20.410  82.028  0.48 74.92  ? 471  GLU C OE1 1 
ATOM   10828 O  OE2 A GLU B  1 471 ? 4.311   22.087  77.715  0.52 72.45  ? 471  GLU C OE2 1 
ATOM   10829 O  OE2 B GLU B  1 471 ? -0.317  18.715  80.682  0.48 80.73  ? 471  GLU C OE2 1 
ATOM   10830 N  N   . GLU B  1 472 ? 3.365   23.590  82.260  1.00 78.54  ? 472  GLU C N   1 
ATOM   10831 C  CA  . GLU B  1 472 ? 3.837   24.950  82.487  1.00 77.64  ? 472  GLU C CA  1 
ATOM   10832 C  C   . GLU B  1 472 ? 5.335   25.051  82.738  1.00 72.24  ? 472  GLU C C   1 
ATOM   10833 O  O   . GLU B  1 472 ? 6.047   25.692  81.977  1.00 69.96  ? 472  GLU C O   1 
ATOM   10834 C  CB  . GLU B  1 472 ? 3.090   25.575  83.665  1.00 80.23  ? 472  GLU C CB  1 
ATOM   10835 C  CG  . GLU B  1 472 ? 3.419   27.038  83.865  1.00 84.79  ? 472  GLU C CG  1 
ATOM   10836 C  CD  . GLU B  1 472 ? 3.593   27.410  85.320  1.00 88.66  ? 472  GLU C CD  1 
ATOM   10837 O  OE1 . GLU B  1 472 ? 3.548   26.506  86.187  1.00 88.89  ? 472  GLU C OE1 1 
ATOM   10838 O  OE2 . GLU B  1 472 ? 3.780   28.613  85.592  1.00 90.82  ? 472  GLU C OE2 1 
ATOM   10839 N  N   . LYS B  1 473 ? 5.809   24.430  83.814  1.00 78.03  ? 473  LYS C N   1 
ATOM   10840 C  CA  . LYS B  1 473 ? 7.204   24.584  84.213  1.00 77.95  ? 473  LYS C CA  1 
ATOM   10841 C  C   . LYS B  1 473 ? 8.122   24.043  83.127  1.00 72.72  ? 473  LYS C C   1 
ATOM   10842 O  O   . LYS B  1 473 ? 9.243   24.521  82.954  1.00 70.44  ? 473  LYS C O   1 
ATOM   10843 C  CB  . LYS B  1 473 ? 7.480   23.881  85.553  1.00 75.17  ? 473  LYS C CB  1 
ATOM   10844 C  CG  . LYS B  1 473 ? 8.855   24.201  86.163  1.00 73.71  ? 473  LYS C CG  1 
ATOM   10845 C  CD  . LYS B  1 473 ? 9.017   25.703  86.429  1.00 83.32  ? 473  LYS C CD  1 
ATOM   10846 C  CE  . LYS B  1 473 ? 8.040   26.189  87.512  1.00 85.71  ? 473  LYS C CE  1 
ATOM   10847 N  NZ  . LYS B  1 473 ? 7.821   27.671  87.527  1.00 75.49  ? 473  LYS C NZ  1 
ATOM   10848 N  N   . PHE B  1 474 ? 7.622   23.053  82.393  1.00 72.24  ? 474  PHE C N   1 
ATOM   10849 C  CA  . PHE B  1 474 ? 8.366   22.409  81.304  1.00 75.99  ? 474  PHE C CA  1 
ATOM   10850 C  C   . PHE B  1 474 ? 8.722   23.369  80.154  1.00 70.51  ? 474  PHE C C   1 
ATOM   10851 O  O   . PHE B  1 474 ? 9.889   23.492  79.753  1.00 59.19  ? 474  PHE C O   1 
ATOM   10852 C  CB  . PHE B  1 474 ? 7.556   21.233  80.760  1.00 70.48  ? 474  PHE C CB  1 
ATOM   10853 C  CG  . PHE B  1 474 ? 8.385   20.202  80.078  1.00 73.28  ? 474  PHE C CG  1 
ATOM   10854 C  CD1 . PHE B  1 474 ? 9.514   19.691  80.699  1.00 71.52  ? 474  PHE C CD1 1 
ATOM   10855 C  CD2 . PHE B  1 474 ? 8.036   19.732  78.822  1.00 75.86  ? 474  PHE C CD2 1 
ATOM   10856 C  CE1 . PHE B  1 474 ? 10.286  18.743  80.080  1.00 71.58  ? 474  PHE C CE1 1 
ATOM   10857 C  CE2 . PHE B  1 474 ? 8.798   18.776  78.197  1.00 69.37  ? 474  PHE C CE2 1 
ATOM   10858 C  CZ  . PHE B  1 474 ? 9.929   18.281  78.827  1.00 74.21  ? 474  PHE C CZ  1 
ATOM   10859 N  N   . GLN B  1 475 ? 7.698   24.034  79.632  1.00 67.13  ? 475  GLN C N   1 
ATOM   10860 C  CA  . GLN B  1 475 ? 7.858   25.023  78.584  1.00 66.35  ? 475  GLN C CA  1 
ATOM   10861 C  C   . GLN B  1 475 ? 8.878   26.099  78.970  1.00 70.50  ? 475  GLN C C   1 
ATOM   10862 O  O   . GLN B  1 475 ? 9.754   26.435  78.171  1.00 71.23  ? 475  GLN C O   1 
ATOM   10863 C  CB  . GLN B  1 475 ? 6.497   25.640  78.263  1.00 66.88  ? 475  GLN C CB  1 
ATOM   10864 C  CG  . GLN B  1 475 ? 6.495   26.695  77.187  1.00 62.49  ? 475  GLN C CG  1 
ATOM   10865 C  CD  . GLN B  1 475 ? 5.141   26.793  76.515  1.00 69.81  ? 475  GLN C CD  1 
ATOM   10866 O  OE1 . GLN B  1 475 ? 4.238   26.007  76.805  1.00 72.51  ? 475  GLN C OE1 1 
ATOM   10867 N  NE2 . GLN B  1 475 ? 4.994   27.754  75.607  1.00 65.65  ? 475  GLN C NE2 1 
ATOM   10868 N  N   . LYS B  1 476 ? 8.771   26.618  80.194  1.00 68.82  ? 476  LYS C N   1 
ATOM   10869 C  CA  . LYS B  1 476 ? 9.719   27.603  80.728  1.00 68.02  ? 476  LYS C CA  1 
ATOM   10870 C  C   . LYS B  1 476 ? 11.152  27.077  80.755  1.00 69.02  ? 476  LYS C C   1 
ATOM   10871 O  O   . LYS B  1 476 ? 12.102  27.793  80.405  1.00 66.98  ? 476  LYS C O   1 
ATOM   10872 C  CB  . LYS B  1 476 ? 9.303   28.029  82.149  1.00 74.74  ? 476  LYS C CB  1 
ATOM   10873 C  CG  . LYS B  1 476 ? 10.382  28.754  82.980  1.00 70.41  ? 476  LYS C CG  1 
ATOM   10874 C  CD  . LYS B  1 476 ? 9.768   29.377  84.251  1.00 80.30  ? 476  LYS C CD  1 
ATOM   10875 C  CE  . LYS B  1 476 ? 10.707  30.358  84.951  1.00 71.64  ? 476  LYS C CE  1 
ATOM   10876 N  NZ  . LYS B  1 476 ? 11.584  29.711  85.964  1.00 68.92  ? 476  LYS C NZ  1 
ATOM   10877 N  N   . GLY B  1 477 ? 11.303  25.830  81.195  1.00 68.91  ? 477  GLY C N   1 
ATOM   10878 C  CA  . GLY B  1 477 ? 12.609  25.198  81.278  1.00 73.15  ? 477  GLY C CA  1 
ATOM   10879 C  C   . GLY B  1 477 ? 13.214  25.036  79.896  1.00 68.55  ? 477  GLY C C   1 
ATOM   10880 O  O   . GLY B  1 477 ? 14.398  25.325  79.682  1.00 66.44  ? 477  GLY C O   1 
ATOM   10881 N  N   . ILE B  1 478 ? 12.379  24.576  78.964  1.00 61.80  ? 478  ILE C N   1 
ATOM   10882 C  CA  . ILE B  1 478 ? 12.740  24.448  77.553  1.00 67.55  ? 478  ILE C CA  1 
ATOM   10883 C  C   . ILE B  1 478 ? 13.242  25.776  76.969  1.00 63.53  ? 478  ILE C C   1 
ATOM   10884 O  O   . ILE B  1 478 ? 14.367  25.862  76.459  1.00 58.30  ? 478  ILE C O   1 
ATOM   10885 C  CB  . ILE B  1 478 ? 11.533  23.932  76.722  1.00 62.53  ? 478  ILE C CB  1 
ATOM   10886 C  CG1 . ILE B  1 478 ? 11.352  22.421  76.923  1.00 55.95  ? 478  ILE C CG1 1 
ATOM   10887 C  CG2 . ILE B  1 478 ? 11.727  24.240  75.258  1.00 58.52  ? 478  ILE C CG2 1 
ATOM   10888 C  CD1 . ILE B  1 478 ? 10.063  21.871  76.361  1.00 55.26  ? 478  ILE C CD1 1 
ATOM   10889 N  N   . ILE B  1 479 ? 12.408  26.808  77.071  1.00 60.53  ? 479  ILE C N   1 
ATOM   10890 C  CA  . ILE B  1 479 ? 12.732  28.129  76.554  1.00 59.23  ? 479  ILE C CA  1 
ATOM   10891 C  C   . ILE B  1 479 ? 14.005  28.687  77.205  1.00 62.24  ? 479  ILE C C   1 
ATOM   10892 O  O   . ILE B  1 479 ? 14.787  29.404  76.565  1.00 60.99  ? 479  ILE C O   1 
ATOM   10893 C  CB  . ILE B  1 479 ? 11.544  29.083  76.760  1.00 56.28  ? 479  ILE C CB  1 
ATOM   10894 C  CG1 . ILE B  1 479 ? 10.336  28.560  75.982  1.00 56.82  ? 479  ILE C CG1 1 
ATOM   10895 C  CG2 . ILE B  1 479 ? 11.894  30.496  76.330  1.00 55.50  ? 479  ILE C CG2 1 
ATOM   10896 C  CD1 . ILE B  1 479 ? 9.141   29.445  76.049  1.00 50.95  ? 479  ILE C CD1 1 
ATOM   10897 N  N   . GLN B  1 480 ? 14.227  28.335  78.469  1.00 64.34  ? 480  GLN C N   1 
ATOM   10898 C  CA  . GLN B  1 480 ? 15.429  28.772  79.184  1.00 68.23  ? 480  GLN C CA  1 
ATOM   10899 C  C   . GLN B  1 480 ? 16.678  28.050  78.651  1.00 66.52  ? 480  GLN C C   1 
ATOM   10900 O  O   . GLN B  1 480 ? 17.759  28.645  78.529  1.00 59.23  ? 480  GLN C O   1 
ATOM   10901 C  CB  . GLN B  1 480 ? 15.279  28.533  80.690  1.00 66.39  ? 480  GLN C CB  1 
ATOM   10902 C  CG  . GLN B  1 480 ? 16.503  28.940  81.491  1.00 68.86  ? 480  GLN C CG  1 
ATOM   10903 C  CD  . GLN B  1 480 ? 16.490  28.380  82.901  1.00 81.41  ? 480  GLN C CD  1 
ATOM   10904 O  OE1 . GLN B  1 480 ? 15.474  27.861  83.369  1.00 78.75  ? 480  GLN C OE1 1 
ATOM   10905 N  NE2 . GLN B  1 480 ? 17.627  28.477  83.585  1.00 85.43  ? 480  GLN C NE2 1 
ATOM   10906 N  N   . TYR B  1 481 ? 16.506  26.766  78.337  1.00 63.79  ? 481  TYR C N   1 
ATOM   10907 C  CA  . TYR B  1 481 ? 17.562  25.925  77.771  1.00 58.60  ? 481  TYR C CA  1 
ATOM   10908 C  C   . TYR B  1 481 ? 18.004  26.418  76.404  1.00 57.95  ? 481  TYR C C   1 
ATOM   10909 O  O   . TYR B  1 481 ? 19.202  26.555  76.116  1.00 55.50  ? 481  TYR C O   1 
ATOM   10910 C  CB  . TYR B  1 481 ? 17.066  24.486  77.662  1.00 54.07  ? 481  TYR C CB  1 
ATOM   10911 C  CG  . TYR B  1 481 ? 18.023  23.538  76.988  1.00 54.69  ? 481  TYR C CG  1 
ATOM   10912 C  CD1 . TYR B  1 481 ? 19.283  23.296  77.524  1.00 54.04  ? 481  TYR C CD1 1 
ATOM   10913 C  CD2 . TYR B  1 481 ? 17.655  22.865  75.822  1.00 52.14  ? 481  TYR C CD2 1 
ATOM   10914 C  CE1 . TYR B  1 481 ? 20.157  22.420  76.913  1.00 56.04  ? 481  TYR C CE1 1 
ATOM   10915 C  CE2 . TYR B  1 481 ? 18.516  21.983  75.206  1.00 47.26  ? 481  TYR C CE2 1 
ATOM   10916 C  CZ  . TYR B  1 481 ? 19.769  21.760  75.754  1.00 52.79  ? 481  TYR C CZ  1 
ATOM   10917 O  OH  . TYR B  1 481 ? 20.636  20.875  75.148  1.00 41.76  ? 481  TYR C OH  1 
ATOM   10918 N  N   . LEU B  1 482 ? 17.015  26.669  75.558  1.00 51.18  ? 482  LEU C N   1 
ATOM   10919 C  CA  . LEU B  1 482 ? 17.267  27.138  74.217  1.00 49.78  ? 482  LEU C CA  1 
ATOM   10920 C  C   . LEU B  1 482 ? 18.044  28.443  74.219  1.00 56.31  ? 482  LEU C C   1 
ATOM   10921 O  O   . LEU B  1 482 ? 19.114  28.545  73.602  1.00 49.60  ? 482  LEU C O   1 
ATOM   10922 C  CB  . LEU B  1 482 ? 15.953  27.317  73.482  1.00 52.30  ? 482  LEU C CB  1 
ATOM   10923 C  CG  . LEU B  1 482 ? 15.118  26.073  73.197  1.00 54.88  ? 482  LEU C CG  1 
ATOM   10924 C  CD1 . LEU B  1 482 ? 13.844  26.505  72.496  1.00 54.95  ? 482  LEU C CD1 1 
ATOM   10925 C  CD2 . LEU B  1 482 ? 15.895  25.044  72.368  1.00 41.88  ? 482  LEU C CD2 1 
ATOM   10926 N  N   . LYS B  1 483 ? 17.507  29.434  74.932  1.00 57.42  ? 483  LYS C N   1 
ATOM   10927 C  CA  . LYS B  1 483 ? 18.080  30.766  74.914  1.00 50.49  ? 483  LYS C CA  1 
ATOM   10928 C  C   . LYS B  1 483 ? 19.458  30.770  75.551  1.00 50.68  ? 483  LYS C C   1 
ATOM   10929 O  O   . LYS B  1 483 ? 20.370  31.440  75.074  1.00 53.71  ? 483  LYS C O   1 
ATOM   10930 C  CB  . LYS B  1 483 ? 17.152  31.757  75.609  1.00 60.98  ? 483  LYS C CB  1 
ATOM   10931 C  CG  . LYS B  1 483 ? 15.834  31.978  74.870  1.00 59.48  ? 483  LYS C CG  1 
ATOM   10932 C  CD  . LYS B  1 483 ? 15.085  33.182  75.426  1.00 60.06  ? 483  LYS C CD  1 
ATOM   10933 C  CE  . LYS B  1 483 ? 13.767  33.401  74.690  1.00 63.73  ? 483  LYS C CE  1 
ATOM   10934 N  NZ  . LYS B  1 483 ? 12.985  34.530  75.266  1.00 58.95  ? 483  LYS C NZ  1 
ATOM   10935 N  N   . LYS B  1 484 ? 19.625  29.997  76.611  1.00 54.74  ? 484  LYS C N   1 
ATOM   10936 C  CA  . LYS B  1 484 ? 20.906  29.976  77.301  1.00 61.27  ? 484  LYS C CA  1 
ATOM   10937 C  C   . LYS B  1 484 ? 21.999  29.412  76.388  1.00 61.45  ? 484  LYS C C   1 
ATOM   10938 O  O   . LYS B  1 484 ? 23.159  29.825  76.464  1.00 59.63  ? 484  LYS C O   1 
ATOM   10939 C  CB  . LYS B  1 484 ? 20.816  29.163  78.608  1.00 55.54  ? 484  LYS C CB  1 
ATOM   10940 C  CG  . LYS B  1 484 ? 22.141  29.108  79.388  1.00 64.26  ? 484  LYS C CG  1 
ATOM   10941 C  CD  . LYS B  1 484 ? 22.052  28.347  80.707  1.00 64.62  ? 484  LYS C CD  1 
ATOM   10942 C  CE  . LYS B  1 484 ? 23.451  28.033  81.221  1.00 63.79  ? 484  LYS C CE  1 
ATOM   10943 N  NZ  . LYS B  1 484 ? 23.439  27.508  82.613  1.00 72.23  ? 484  LYS C NZ  1 
ATOM   10944 N  N   . PHE B  1 485 ? 21.616  28.479  75.517  1.00 61.90  ? 485  PHE C N   1 
ATOM   10945 C  CA  . PHE B  1 485 ? 22.590  27.734  74.722  1.00 60.71  ? 485  PHE C CA  1 
ATOM   10946 C  C   . PHE B  1 485 ? 22.485  27.938  73.203  1.00 57.01  ? 485  PHE C C   1 
ATOM   10947 O  O   . PHE B  1 485 ? 23.116  27.208  72.440  1.00 60.48  ? 485  PHE C O   1 
ATOM   10948 C  CB  . PHE B  1 485 ? 22.469  26.240  75.031  1.00 60.32  ? 485  PHE C CB  1 
ATOM   10949 C  CG  . PHE B  1 485 ? 22.894  25.874  76.417  1.00 63.70  ? 485  PHE C CG  1 
ATOM   10950 C  CD1 . PHE B  1 485 ? 24.223  25.584  76.692  1.00 64.68  ? 485  PHE C CD1 1 
ATOM   10951 C  CD2 . PHE B  1 485 ? 21.968  25.819  77.447  1.00 60.30  ? 485  PHE C CD2 1 
ATOM   10952 C  CE1 . PHE B  1 485 ? 24.622  25.241  77.973  1.00 64.28  ? 485  PHE C CE1 1 
ATOM   10953 C  CE2 . PHE B  1 485 ? 22.357  25.476  78.725  1.00 62.92  ? 485  PHE C CE2 1 
ATOM   10954 C  CZ  . PHE B  1 485 ? 23.685  25.189  78.992  1.00 65.01  ? 485  PHE C CZ  1 
ATOM   10955 N  N   . SER B  1 486 ? 21.689  28.908  72.764  1.00 55.36  ? 486  SER C N   1 
ATOM   10956 C  CA  . SER B  1 486 ? 21.647  29.279  71.350  1.00 54.11  ? 486  SER C CA  1 
ATOM   10957 C  C   . SER B  1 486 ? 23.051  29.478  70.753  1.00 55.90  ? 486  SER C C   1 
ATOM   10958 O  O   . SER B  1 486 ? 23.931  30.081  71.393  1.00 51.01  ? 486  SER C O   1 
ATOM   10959 C  CB  . SER B  1 486 ? 20.815  30.540  71.179  1.00 46.65  ? 486  SER C CB  1 
ATOM   10960 O  OG  . SER B  1 486 ? 19.485  30.282  71.603  1.00 46.72  ? 486  SER C OG  1 
ATOM   10961 N  N   . TYR B  1 487 ? 23.257  28.931  69.551  1.00 43.59  ? 487  TYR C N   1 
ATOM   10962 C  CA  . TYR B  1 487 ? 24.506  29.097  68.810  1.00 41.36  ? 487  TYR C CA  1 
ATOM   10963 C  C   . TYR B  1 487 ? 25.698  28.521  69.585  1.00 49.72  ? 487  TYR C C   1 
ATOM   10964 O  O   . TYR B  1 487 ? 26.857  28.889  69.353  1.00 45.27  ? 487  TYR C O   1 
ATOM   10965 C  CB  . TYR B  1 487 ? 24.719  30.578  68.456  1.00 48.67  ? 487  TYR C CB  1 
ATOM   10966 C  CG  . TYR B  1 487 ? 23.480  31.198  67.822  1.00 55.85  ? 487  TYR C CG  1 
ATOM   10967 C  CD1 . TYR B  1 487 ? 22.866  30.593  66.733  1.00 54.23  ? 487  TYR C CD1 1 
ATOM   10968 C  CD2 . TYR B  1 487 ? 22.897  32.357  68.333  1.00 53.73  ? 487  TYR C CD2 1 
ATOM   10969 C  CE1 . TYR B  1 487 ? 21.724  31.128  66.148  1.00 52.23  ? 487  TYR C CE1 1 
ATOM   10970 C  CE2 . TYR B  1 487 ? 21.743  32.901  67.744  1.00 55.96  ? 487  TYR C CE2 1 
ATOM   10971 C  CZ  . TYR B  1 487 ? 21.172  32.279  66.645  1.00 57.41  ? 487  TYR C CZ  1 
ATOM   10972 O  OH  . TYR B  1 487 ? 20.037  32.772  66.033  1.00 59.39  ? 487  TYR C OH  1 
ATOM   10973 N  N   . ARG B  1 488 ? 25.400  27.559  70.459  1.00 53.51  ? 488  ARG C N   1 
ATOM   10974 C  CA  . ARG B  1 488 ? 26.387  26.981  71.362  1.00 54.56  ? 488  ARG C CA  1 
ATOM   10975 C  C   . ARG B  1 488 ? 26.139  25.483  71.569  1.00 49.27  ? 488  ARG C C   1 
ATOM   10976 O  O   . ARG B  1 488 ? 25.222  24.925  70.998  1.00 49.17  ? 488  ARG C O   1 
ATOM   10977 C  CB  . ARG B  1 488 ? 26.335  27.725  72.690  1.00 56.69  ? 488  ARG C CB  1 
ATOM   10978 C  CG  . ARG B  1 488 ? 27.610  27.771  73.479  1.00 61.96  ? 488  ARG C CG  1 
ATOM   10979 C  CD  . ARG B  1 488 ? 27.400  28.679  74.696  1.00 72.84  ? 488  ARG C CD  1 
ATOM   10980 N  NE  . ARG B  1 488 ? 28.077  28.174  75.889  1.00 76.36  ? 488  ARG C NE  1 
ATOM   10981 C  CZ  . ARG B  1 488 ? 27.506  28.068  77.083  1.00 77.33  ? 488  ARG C CZ  1 
ATOM   10982 N  NH1 . ARG B  1 488 ? 26.241  28.441  77.251  1.00 79.16  ? 488  ARG C NH1 1 
ATOM   10983 N  NH2 . ARG B  1 488 ? 28.202  27.595  78.109  1.00 86.71  ? 488  ARG C NH2 1 
ATOM   10984 N  N   . ASN B  1 489 ? 26.943  24.836  72.403  1.00 53.28  ? 489  ASN C N   1 
ATOM   10985 C  CA  . ASN B  1 489 ? 26.796  23.398  72.638  1.00 52.79  ? 489  ASN C CA  1 
ATOM   10986 C  C   . ASN B  1 489 ? 26.416  23.026  74.091  1.00 56.02  ? 489  ASN C C   1 
ATOM   10987 O  O   . ASN B  1 489 ? 26.899  23.627  75.056  1.00 50.86  ? 489  ASN C O   1 
ATOM   10988 C  CB  . ASN B  1 489 ? 28.090  22.682  72.218  1.00 51.55  ? 489  ASN C CB  1 
ATOM   10989 C  CG  . ASN B  1 489 ? 28.499  23.003  70.764  1.00 56.17  ? 489  ASN C CG  1 
ATOM   10990 O  OD1 . ASN B  1 489 ? 28.966  24.116  70.460  1.00 53.20  ? 489  ASN C OD1 1 
ATOM   10991 N  ND2 . ASN B  1 489 ? 28.321  22.027  69.866  1.00 46.43  ? 489  ASN C ND2 1 
ATOM   10992 N  N   . ALA B  1 490 ? 25.540  22.030  74.228  1.00 58.96  ? 490  ALA C N   1 
ATOM   10993 C  CA  . ALA B  1 490 ? 25.042  21.576  75.532  1.00 50.69  ? 490  ALA C CA  1 
ATOM   10994 C  C   . ALA B  1 490 ? 25.359  20.107  75.776  1.00 50.35  ? 490  ALA C C   1 
ATOM   10995 O  O   . ALA B  1 490 ? 25.438  19.321  74.837  1.00 55.35  ? 490  ALA C O   1 
ATOM   10996 C  CB  . ALA B  1 490 ? 23.538  21.806  75.638  1.00 50.05  ? 490  ALA C CB  1 
ATOM   10997 N  N   . LYS B  1 491 ? 25.550  19.740  77.038  1.00 50.29  ? 491  LYS C N   1 
ATOM   10998 C  CA  . LYS B  1 491 ? 25.776  18.345  77.381  1.00 54.42  ? 491  LYS C CA  1 
ATOM   10999 C  C   . LYS B  1 491 ? 24.604  17.875  78.234  1.00 55.14  ? 491  LYS C C   1 
ATOM   11000 O  O   . LYS B  1 491 ? 23.781  18.697  78.643  1.00 55.65  ? 491  LYS C O   1 
ATOM   11001 C  CB  . LYS B  1 491 ? 27.116  18.158  78.100  1.00 58.31  ? 491  LYS C CB  1 
ATOM   11002 C  CG  . LYS B  1 491 ? 27.368  19.152  79.232  1.00 65.67  ? 491  LYS C CG  1 
ATOM   11003 C  CD  . LYS B  1 491 ? 28.617  18.789  80.039  1.00 70.01  ? 491  LYS C CD  1 
ATOM   11004 C  CE  . LYS B  1 491 ? 29.876  18.788  79.173  1.00 76.27  ? 491  LYS C CE  1 
ATOM   11005 N  NZ  . LYS B  1 491 ? 31.116  18.550  79.979  1.00 71.25  ? 491  LYS C NZ  1 
ATOM   11006 N  N   . ASN B  1 492 ? 24.517  16.564  78.470  1.00 54.96  ? 492  ASN C N   1 
ATOM   11007 C  CA  . ASN B  1 492 ? 23.396  15.953  79.197  1.00 53.49  ? 492  ASN C CA  1 
ATOM   11008 C  C   . ASN B  1 492 ? 23.042  16.698  80.504  1.00 55.13  ? 492  ASN C C   1 
ATOM   11009 O  O   . ASN B  1 492 ? 21.877  17.018  80.758  1.00 56.04  ? 492  ASN C O   1 
ATOM   11010 C  CB  . ASN B  1 492 ? 23.713  14.476  79.480  1.00 40.24  ? 492  ASN C CB  1 
ATOM   11011 C  CG  . ASN B  1 492 ? 22.577  13.751  80.201  1.00 55.39  ? 492  ASN C CG  1 
ATOM   11012 O  OD1 . ASN B  1 492 ? 21.417  13.817  79.789  1.00 53.14  ? 492  ASN C OD1 1 
ATOM   11013 N  ND2 . ASN B  1 492 ? 22.910  13.067  81.299  1.00 54.89  ? 492  ASN C ND2 1 
ATOM   11014 N  N   . ASP B  1 493 ? 24.055  17.005  81.308  1.00 55.53  ? 493  ASP C N   1 
ATOM   11015 C  CA  . ASP B  1 493 ? 23.852  17.728  82.567  1.00 61.26  ? 493  ASP C CA  1 
ATOM   11016 C  C   . ASP B  1 493 ? 23.119  19.061  82.358  1.00 63.67  ? 493  ASP C C   1 
ATOM   11017 O  O   . ASP B  1 493 ? 22.163  19.365  83.075  1.00 61.58  ? 493  ASP C O   1 
ATOM   11018 C  CB  . ASP B  1 493 ? 25.200  17.969  83.263  1.00 60.72  ? 493  ASP C CB  1 
ATOM   11019 C  CG  . ASP B  1 493 ? 25.070  18.822  84.519  1.00 77.53  ? 493  ASP C CG  1 
ATOM   11020 O  OD1 . ASP B  1 493 ? 25.081  20.077  84.409  1.00 71.40  ? 493  ASP C OD1 1 
ATOM   11021 O  OD2 . ASP B  1 493 ? 24.954  18.230  85.620  1.00 82.75  ? 493  ASP C OD2 1 
ATOM   11022 N  N   . ASP B  1 494 ? 23.569  19.834  81.365  1.00 63.23  ? 494  ASP C N   1 
ATOM   11023 C  CA  . ASP B  1 494 ? 23.025  21.166  81.072  1.00 60.38  ? 494  ASP C CA  1 
ATOM   11024 C  C   . ASP B  1 494 ? 21.528  21.147  80.802  1.00 59.58  ? 494  ASP C C   1 
ATOM   11025 O  O   . ASP B  1 494 ? 20.838  22.115  81.073  1.00 64.95  ? 494  ASP C O   1 
ATOM   11026 C  CB  . ASP B  1 494 ? 23.732  21.805  79.860  1.00 56.23  ? 494  ASP C CB  1 
ATOM   11027 C  CG  . ASP B  1 494 ? 25.181  22.176  80.141  1.00 63.39  ? 494  ASP C CG  1 
ATOM   11028 O  OD1 . ASP B  1 494 ? 25.509  22.489  81.309  1.00 75.40  ? 494  ASP C OD1 1 
ATOM   11029 O  OD2 . ASP B  1 494 ? 25.996  22.161  79.193  1.00 60.32  ? 494  ASP C OD2 1 
ATOM   11030 N  N   . LEU B  1 495 ? 21.017  20.062  80.243  1.00 61.97  ? 495  LEU C N   1 
ATOM   11031 C  CA  . LEU B  1 495 ? 19.611  20.068  79.890  1.00 61.50  ? 495  LEU C CA  1 
ATOM   11032 C  C   . LEU B  1 495 ? 18.739  20.101  81.131  1.00 65.31  ? 495  LEU C C   1 
ATOM   11033 O  O   . LEU B  1 495 ? 17.901  20.991  81.285  1.00 63.04  ? 495  LEU C O   1 
ATOM   11034 C  CB  . LEU B  1 495 ? 19.232  18.858  79.049  1.00 57.23  ? 495  LEU C CB  1 
ATOM   11035 C  CG  . LEU B  1 495 ? 17.705  18.884  78.909  1.00 59.96  ? 495  LEU C CG  1 
ATOM   11036 C  CD1 . LEU B  1 495 ? 17.231  20.106  78.104  1.00 55.25  ? 495  LEU C CD1 1 
ATOM   11037 C  CD2 . LEU B  1 495 ? 17.171  17.594  78.343  1.00 59.45  ? 495  LEU C CD2 1 
ATOM   11038 N  N   . TRP B  1 496 ? 18.925  19.118  82.008  1.00 69.54  ? 496  TRP C N   1 
ATOM   11039 C  CA  . TRP B  1 496 ? 18.065  19.000  83.176  1.00 68.56  ? 496  TRP C CA  1 
ATOM   11040 C  C   . TRP B  1 496 ? 18.372  20.080  84.211  1.00 64.30  ? 496  TRP C C   1 
ATOM   11041 O  O   . TRP B  1 496 ? 17.494  20.496  84.962  1.00 65.19  ? 496  TRP C O   1 
ATOM   11042 C  CB  . TRP B  1 496 ? 18.202  17.631  83.807  1.00 62.89  ? 496  TRP C CB  1 
ATOM   11043 C  CG  . TRP B  1 496 ? 18.265  16.480  82.863  1.00 55.52  ? 496  TRP C CG  1 
ATOM   11044 C  CD1 . TRP B  1 496 ? 19.380  15.782  82.500  1.00 54.96  ? 496  TRP C CD1 1 
ATOM   11045 C  CD2 . TRP B  1 496 ? 17.167  15.847  82.208  1.00 53.89  ? 496  TRP C CD2 1 
ATOM   11046 N  NE1 . TRP B  1 496 ? 19.044  14.761  81.647  1.00 49.30  ? 496  TRP C NE1 1 
ATOM   11047 C  CE2 . TRP B  1 496 ? 17.690  14.781  81.450  1.00 50.43  ? 496  TRP C CE2 1 
ATOM   11048 C  CE3 . TRP B  1 496 ? 15.795  16.081  82.178  1.00 58.75  ? 496  TRP C CE3 1 
ATOM   11049 C  CZ2 . TRP B  1 496 ? 16.889  13.956  80.673  1.00 49.99  ? 496  TRP C CZ2 1 
ATOM   11050 C  CZ3 . TRP B  1 496 ? 14.997  15.253  81.402  1.00 59.97  ? 496  TRP C CZ3 1 
ATOM   11051 C  CH2 . TRP B  1 496 ? 15.547  14.203  80.665  1.00 54.23  ? 496  TRP C CH2 1 
ATOM   11052 N  N   . SER B  1 497 ? 19.621  20.532  84.226  1.00 69.24  ? 497  SER C N   1 
ATOM   11053 C  CA  . SER B  1 497 ? 20.033  21.695  85.013  1.00 66.04  ? 497  SER C CA  1 
ATOM   11054 C  C   . SER B  1 497 ? 19.189  22.934  84.674  1.00 67.51  ? 497  SER C C   1 
ATOM   11055 O  O   . SER B  1 497 ? 18.980  23.795  85.517  1.00 80.47  ? 497  SER C O   1 
ATOM   11056 C  CB  . SER B  1 497 ? 21.528  21.973  84.783  1.00 66.29  ? 497  SER C CB  1 
ATOM   11057 O  OG  . SER B  1 497 ? 22.036  22.980  85.642  1.00 65.73  ? 497  SER C OG  1 
ATOM   11058 N  N   . SER B  1 498 ? 18.693  23.013  83.443  1.00 70.76  ? 498  SER C N   1 
ATOM   11059 C  CA  . SER B  1 498 ? 17.848  24.128  83.016  1.00 69.66  ? 498  SER C CA  1 
ATOM   11060 C  C   . SER B  1 498 ? 16.368  23.805  83.173  1.00 72.01  ? 498  SER C C   1 
ATOM   11061 O  O   . SER B  1 498 ? 15.538  24.705  83.258  1.00 75.80  ? 498  SER C O   1 
ATOM   11062 C  CB  . SER B  1 498 ? 18.136  24.504  81.550  1.00 63.00  ? 498  SER C CB  1 
ATOM   11063 O  OG  . SER B  1 498 ? 19.452  25.019  81.381  1.00 60.52  ? 498  SER C OG  1 
ATOM   11064 N  N   . LEU B  1 499 ? 16.045  22.516  83.213  1.00 72.33  ? 499  LEU C N   1 
ATOM   11065 C  CA  . LEU B  1 499 ? 14.654  22.066  83.143  1.00 72.20  ? 499  LEU C CA  1 
ATOM   11066 C  C   . LEU B  1 499 ? 13.919  22.167  84.476  1.00 79.32  ? 499  LEU C C   1 
ATOM   11067 O  O   . LEU B  1 499 ? 12.687  22.083  84.524  1.00 84.13  ? 499  LEU C O   1 
ATOM   11068 C  CB  . LEU B  1 499 ? 14.591  20.627  82.626  1.00 69.22  ? 499  LEU C CB  1 
ATOM   11069 C  CG  . LEU B  1 499 ? 14.314  20.453  81.130  1.00 69.92  ? 499  LEU C CG  1 
ATOM   11070 C  CD1 . LEU B  1 499 ? 14.402  18.993  80.730  1.00 67.99  ? 499  LEU C CD1 1 
ATOM   11071 C  CD2 . LEU B  1 499 ? 12.944  21.021  80.770  1.00 72.13  ? 499  LEU C CD2 1 
ATOM   11072 N  N   . SER B  1 500 ? 14.670  22.334  85.558  1.00 77.55  ? 500  SER C N   1 
ATOM   11073 C  CA  . SER B  1 500 ? 14.061  22.640  86.846  1.00 84.63  ? 500  SER C CA  1 
ATOM   11074 C  C   . SER B  1 500 ? 13.841  24.146  86.936  1.00 89.85  ? 500  SER C C   1 
ATOM   11075 O  O   . SER B  1 500 ? 12.705  24.608  87.101  1.00 90.76  ? 500  SER C O   1 
ATOM   11076 C  CB  . SER B  1 500 ? 14.927  22.136  88.008  1.00 88.15  ? 500  SER C CB  1 
ATOM   11077 O  OG  . SER B  1 500 ? 16.313  22.221  87.714  1.00 89.29  ? 500  SER C OG  1 
ATOM   11078 N  N   . ASN B  1 501 ? 14.933  24.899  86.795  1.00 89.36  ? 501  ASN C N   1 
ATOM   11079 C  CA  . ASN B  1 501 ? 14.892  26.359  86.817  1.00 86.74  ? 501  ASN C CA  1 
ATOM   11080 C  C   . ASN B  1 501 ? 13.862  26.901  85.831  1.00 87.54  ? 501  ASN C C   1 
ATOM   11081 O  O   . ASN B  1 501 ? 12.945  27.627  86.211  1.00 95.07  ? 501  ASN C O   1 
ATOM   11082 C  CB  . ASN B  1 501 ? 16.275  26.947  86.499  1.00 85.44  ? 501  ASN C CB  1 
ATOM   11083 C  CG  . ASN B  1 501 ? 17.405  26.252  87.253  1.00 89.00  ? 501  ASN C CG  1 
ATOM   11084 O  OD1 . ASN B  1 501 ? 17.177  25.543  88.233  1.00 89.19  ? 501  ASN C OD1 1 
ATOM   11085 N  ND2 . ASN B  1 501 ? 18.635  26.465  86.797  1.00 86.99  ? 501  ASN C ND2 1 
ATOM   11086 N  N   . GLY B  1 529 ? 15.640  20.446  98.218  1.00 93.38  ? 529  GLY C N   1 
ATOM   11087 C  CA  . GLY B  1 529 ? 14.290  20.939  98.008  1.00 101.58 ? 529  GLY C CA  1 
ATOM   11088 C  C   . GLY B  1 529 ? 14.002  21.328  96.567  1.00 101.42 ? 529  GLY C C   1 
ATOM   11089 O  O   . GLY B  1 529 ? 13.799  22.513  96.280  1.00 100.01 ? 529  GLY C O   1 
ATOM   11090 N  N   . GLU B  1 530 ? 13.979  20.317  95.690  1.00 98.09  ? 530  GLU C N   1 
ATOM   11091 C  CA  . GLU B  1 530 ? 13.783  20.439  94.231  1.00 97.63  ? 530  GLU C CA  1 
ATOM   11092 C  C   . GLU B  1 530 ? 15.102  20.825  93.544  1.00 95.03  ? 530  GLU C C   1 
ATOM   11093 O  O   . GLU B  1 530 ? 16.044  21.270  94.208  1.00 93.47  ? 530  GLU C O   1 
ATOM   11094 C  CB  . GLU B  1 530 ? 12.654  21.438  93.895  1.00 101.56 ? 530  GLU C CB  1 
ATOM   11095 C  CG  . GLU B  1 530 ? 12.235  21.530  92.426  1.00 103.11 ? 530  GLU C CG  1 
ATOM   11096 C  CD  . GLU B  1 530 ? 11.693  20.225  91.860  1.00 100.37 ? 530  GLU C CD  1 
ATOM   11097 O  OE1 . GLU B  1 530 ? 11.191  19.377  92.630  1.00 93.21  ? 530  GLU C OE1 1 
ATOM   11098 O  OE2 . GLU B  1 530 ? 11.771  20.054  90.628  1.00 103.79 ? 530  GLU C OE2 1 
ATOM   11099 N  N   . ASN B  1 531 ? 15.152  20.623  92.223  1.00 89.26  ? 531  ASN C N   1 
ATOM   11100 C  CA  . ASN B  1 531 ? 16.345  20.791  91.379  1.00 84.77  ? 531  ASN C CA  1 
ATOM   11101 C  C   . ASN B  1 531 ? 17.399  19.716  91.634  1.00 83.54  ? 531  ASN C C   1 
ATOM   11102 O  O   . ASN B  1 531 ? 17.753  18.967  90.722  1.00 83.81  ? 531  ASN C O   1 
ATOM   11103 C  CB  . ASN B  1 531 ? 16.989  22.173  91.539  1.00 87.04  ? 531  ASN C CB  1 
ATOM   11104 C  CG  . ASN B  1 531 ? 18.055  22.445  90.474  1.00 86.93  ? 531  ASN C CG  1 
ATOM   11105 O  OD1 . ASN B  1 531 ? 17.759  23.014  89.422  1.00 96.27  ? 531  ASN C OD1 1 
ATOM   11106 N  ND2 . ASN B  1 531 ? 19.291  22.023  90.736  1.00 77.98  ? 531  ASN C ND2 1 
ATOM   11107 N  N   . ALA B  1 532 ? 17.922  19.639  92.854  1.00 88.79  ? 532  ALA C N   1 
ATOM   11108 C  CA  . ALA B  1 532 ? 18.809  18.530  93.186  1.00 82.40  ? 532  ALA C CA  1 
ATOM   11109 C  C   . ALA B  1 532 ? 18.010  17.229  93.079  1.00 75.59  ? 532  ALA C C   1 
ATOM   11110 O  O   . ALA B  1 532 ? 18.552  16.199  92.688  1.00 73.20  ? 532  ALA C O   1 
ATOM   11111 C  CB  . ALA B  1 532 ? 19.417  18.696  94.573  1.00 76.44  ? 532  ALA C CB  1 
ATOM   11112 N  N   . GLU B  1 533 ? 16.715  17.294  93.391  1.00 70.82  ? 533  GLU C N   1 
ATOM   11113 C  CA  . GLU B  1 533 ? 15.834  16.143  93.221  1.00 74.92  ? 533  GLU C CA  1 
ATOM   11114 C  C   . GLU B  1 533 ? 15.756  15.739  91.743  1.00 75.86  ? 533  GLU C C   1 
ATOM   11115 O  O   . GLU B  1 533 ? 15.908  14.557  91.402  1.00 69.15  ? 533  GLU C O   1 
ATOM   11116 C  CB  . GLU B  1 533 ? 14.429  16.442  93.765  1.00 78.25  ? 533  GLU C CB  1 
ATOM   11117 C  CG  . GLU B  1 533 ? 13.552  15.197  93.951  1.00 79.34  ? 533  GLU C CG  1 
ATOM   11118 C  CD  . GLU B  1 533 ? 12.231  15.490  94.661  1.00 84.85  ? 533  GLU C CD  1 
ATOM   11119 O  OE1 . GLU B  1 533 ? 11.501  16.401  94.216  1.00 91.87  ? 533  GLU C OE1 1 
ATOM   11120 O  OE2 . GLU B  1 533 ? 11.918  14.809  95.666  1.00 82.80  ? 533  GLU C OE2 1 
ATOM   11121 N  N   . VAL B  1 534 ? 15.532  16.727  90.873  1.00 75.51  ? 534  VAL C N   1 
ATOM   11122 C  CA  . VAL B  1 534 ? 15.368  16.489  89.436  1.00 70.61  ? 534  VAL C CA  1 
ATOM   11123 C  C   . VAL B  1 534 ? 16.653  15.933  88.827  1.00 62.57  ? 534  VAL C C   1 
ATOM   11124 O  O   . VAL B  1 534 ? 16.639  14.882  88.187  1.00 50.50  ? 534  VAL C O   1 
ATOM   11125 C  CB  . VAL B  1 534 ? 14.930  17.782  88.692  1.00 67.43  ? 534  VAL C CB  1 
ATOM   11126 C  CG1 . VAL B  1 534 ? 15.473  17.826  87.271  1.00 67.33  ? 534  VAL C CG1 1 
ATOM   11127 C  CG2 . VAL B  1 534 ? 13.421  17.896  88.682  1.00 67.80  ? 534  VAL C CG2 1 
ATOM   11128 N  N   . LYS B  1 535 ? 17.767  16.616  89.058  1.00 63.21  ? 535  LYS C N   1 
ATOM   11129 C  CA  . LYS B  1 535 ? 19.027  16.181  88.487  1.00 61.54  ? 535  LYS C CA  1 
ATOM   11130 C  C   . LYS B  1 535 ? 19.375  14.761  88.947  1.00 62.79  ? 535  LYS C C   1 
ATOM   11131 O  O   . LYS B  1 535 ? 19.789  13.930  88.134  1.00 60.88  ? 535  LYS C O   1 
ATOM   11132 C  CB  . LYS B  1 535 ? 20.140  17.175  88.829  1.00 61.63  ? 535  LYS C CB  1 
ATOM   11133 C  CG  . LYS B  1 535 ? 19.898  18.563  88.226  1.00 67.67  ? 535  LYS C CG  1 
ATOM   11134 C  CD  . LYS B  1 535 ? 21.107  19.489  88.357  1.00 75.29  ? 535  LYS C CD  1 
ATOM   11135 C  CE  . LYS B  1 535 ? 22.103  19.309  87.210  1.00 70.95  ? 535  LYS C CE  1 
ATOM   11136 N  NZ  . LYS B  1 535 ? 23.297  20.205  87.331  1.00 74.86  ? 535  LYS C NZ  1 
ATOM   11137 N  N   . GLU B  1 536 ? 19.167  14.471  90.231  1.00 66.36  ? 536  GLU C N   1 
ATOM   11138 C  CA  . GLU B  1 536 ? 19.443  13.136  90.772  1.00 62.94  ? 536  GLU C CA  1 
ATOM   11139 C  C   . GLU B  1 536 ? 18.585  12.036  90.134  1.00 60.72  ? 536  GLU C C   1 
ATOM   11140 O  O   . GLU B  1 536 ? 19.106  10.981  89.749  1.00 49.21  ? 536  GLU C O   1 
ATOM   11141 C  CB  . GLU B  1 536 ? 19.235  13.117  92.285  1.00 67.69  ? 536  GLU C CB  1 
ATOM   11142 C  CG  . GLU B  1 536 ? 20.444  13.557  93.093  1.00 70.84  ? 536  GLU C CG  1 
ATOM   11143 C  CD  . GLU B  1 536 ? 20.232  13.396  94.593  1.00 68.45  ? 536  GLU C CD  1 
ATOM   11144 O  OE1 . GLU B  1 536 ? 19.249  12.727  94.994  1.00 63.72  ? 536  GLU C OE1 1 
ATOM   11145 O  OE2 . GLU B  1 536 ? 21.054  13.937  95.368  1.00 75.59  ? 536  GLU C OE2 1 
ATOM   11146 N  N   . MET B  1 537 ? 17.279  12.285  90.041  1.00 57.77  ? 537  MET C N   1 
ATOM   11147 C  CA  . MET B  1 537 ? 16.340  11.320  89.480  1.00 57.29  ? 537  MET C CA  1 
ATOM   11148 C  C   . MET B  1 537 ? 16.697  10.986  88.039  1.00 64.99  ? 537  MET C C   1 
ATOM   11149 O  O   . MET B  1 537 ? 16.770  9.808   87.658  1.00 66.50  ? 537  MET C O   1 
ATOM   11150 C  CB  . MET B  1 537 ? 14.921  11.869  89.562  1.00 63.52  ? 537  MET C CB  1 
ATOM   11151 C  CG  . MET B  1 537 ? 13.928  11.247  88.616  1.00 57.36  ? 537  MET C CG  1 
ATOM   11152 S  SD  . MET B  1 537 ? 12.407  12.214  88.680  1.00 72.92  ? 537  MET C SD  1 
ATOM   11153 C  CE  . MET B  1 537 ? 11.542  11.343  89.956  1.00 75.23  ? 537  MET C CE  1 
ATOM   11154 N  N   . MET B  1 538 ? 16.951  12.029  87.251  1.00 60.52  ? 538  MET C N   1 
ATOM   11155 C  CA  . MET B  1 538 ? 17.273  11.866  85.842  1.00 59.27  ? 538  MET C CA  1 
ATOM   11156 C  C   . MET B  1 538 ? 18.594  11.143  85.639  1.00 60.84  ? 538  MET C C   1 
ATOM   11157 O  O   . MET B  1 538 ? 18.795  10.480  84.620  1.00 62.51  ? 538  MET C O   1 
ATOM   11158 C  CB  . MET B  1 538 ? 17.285  13.227  85.146  1.00 56.53  ? 538  MET C CB  1 
ATOM   11159 C  CG  . MET B  1 538 ? 15.882  13.735  84.933  1.00 53.34  ? 538  MET C CG  1 
ATOM   11160 S  SD  . MET B  1 538 ? 14.859  12.335  84.448  1.00 69.36  ? 538  MET C SD  1 
ATOM   11161 C  CE  . MET B  1 538 ? 13.228  12.988  84.701  1.00 65.85  ? 538  MET C CE  1 
ATOM   11162 N  N   . THR B  1 539 ? 19.483  11.240  86.620  1.00 55.64  ? 539  THR C N   1 
ATOM   11163 C  CA  . THR B  1 539 ? 20.762  10.545  86.544  1.00 54.30  ? 539  THR C CA  1 
ATOM   11164 C  C   . THR B  1 539 ? 20.561  9.034   86.543  1.00 58.68  ? 539  THR C C   1 
ATOM   11165 O  O   . THR B  1 539 ? 21.459  8.264   86.183  1.00 57.36  ? 539  THR C O   1 
ATOM   11166 C  CB  . THR B  1 539 ? 21.671  10.951  87.700  1.00 55.02  ? 539  THR C CB  1 
ATOM   11167 O  OG1 . THR B  1 539 ? 21.643  12.375  87.824  1.00 56.03  ? 539  THR C OG1 1 
ATOM   11168 C  CG2 . THR B  1 539 ? 23.113  10.492  87.464  1.00 56.46  ? 539  THR C CG2 1 
ATOM   11169 N  N   . THR B  1 540 ? 19.368  8.607   86.929  1.00 58.48  ? 540  THR C N   1 
ATOM   11170 C  CA  . THR B  1 540 ? 19.056  7.184   86.942  1.00 66.20  ? 540  THR C CA  1 
ATOM   11171 C  C   . THR B  1 540 ? 18.389  6.761   85.636  1.00 57.19  ? 540  THR C C   1 
ATOM   11172 O  O   . THR B  1 540 ? 18.280  5.573   85.333  1.00 56.10  ? 540  THR C O   1 
ATOM   11173 C  CB  . THR B  1 540 ? 18.151  6.840   88.139  1.00 61.58  ? 540  THR C CB  1 
ATOM   11174 O  OG1 . THR B  1 540 ? 16.941  7.615   88.068  1.00 58.30  ? 540  THR C OG1 1 
ATOM   11175 C  CG2 . THR B  1 540 ? 18.885  7.164   89.432  1.00 57.02  ? 540  THR C CG2 1 
ATOM   11176 N  N   . TRP B  1 541 ? 17.936  7.755   84.880  1.00 59.21  ? 541  TRP C N   1 
ATOM   11177 C  CA  . TRP B  1 541 ? 17.232  7.530   83.627  1.00 62.74  ? 541  TRP C CA  1 
ATOM   11178 C  C   . TRP B  1 541 ? 18.138  7.753   82.414  1.00 61.81  ? 541  TRP C C   1 
ATOM   11179 O  O   . TRP B  1 541 ? 17.850  7.276   81.310  1.00 64.03  ? 541  TRP C O   1 
ATOM   11180 C  CB  . TRP B  1 541 ? 16.005  8.441   83.543  1.00 60.46  ? 541  TRP C CB  1 
ATOM   11181 C  CG  . TRP B  1 541 ? 14.974  8.086   84.536  1.00 65.88  ? 541  TRP C CG  1 
ATOM   11182 C  CD1 . TRP B  1 541 ? 14.653  8.780   85.658  1.00 65.48  ? 541  TRP C CD1 1 
ATOM   11183 C  CD2 . TRP B  1 541 ? 14.133  6.924   84.522  1.00 68.52  ? 541  TRP C CD2 1 
ATOM   11184 N  NE1 . TRP B  1 541 ? 13.655  8.135   86.342  1.00 67.33  ? 541  TRP C NE1 1 
ATOM   11185 C  CE2 . TRP B  1 541 ? 13.321  6.988   85.671  1.00 66.84  ? 541  TRP C CE2 1 
ATOM   11186 C  CE3 . TRP B  1 541 ? 13.988  5.838   83.650  1.00 66.05  ? 541  TRP C CE3 1 
ATOM   11187 C  CZ2 . TRP B  1 541 ? 12.368  6.015   85.971  1.00 65.06  ? 541  TRP C CZ2 1 
ATOM   11188 C  CZ3 . TRP B  1 541 ? 13.044  4.868   83.952  1.00 65.67  ? 541  TRP C CZ3 1 
ATOM   11189 C  CH2 . TRP B  1 541 ? 12.245  4.966   85.104  1.00 65.18  ? 541  TRP C CH2 1 
ATOM   11190 N  N   . THR B  1 542 ? 19.243  8.457   82.624  1.00 53.92  ? 542  THR C N   1 
ATOM   11191 C  CA  . THR B  1 542 ? 20.098  8.826   81.507  1.00 55.01  ? 542  THR C CA  1 
ATOM   11192 C  C   . THR B  1 542 ? 21.507  8.235   81.607  1.00 52.95  ? 542  THR C C   1 
ATOM   11193 O  O   . THR B  1 542 ? 22.252  8.273   80.633  1.00 48.20  ? 542  THR C O   1 
ATOM   11194 C  CB  . THR B  1 542 ? 20.203  10.365  81.380  1.00 56.96  ? 542  THR C CB  1 
ATOM   11195 O  OG1 . THR B  1 542 ? 20.921  10.895  82.503  1.00 54.48  ? 542  THR C OG1 1 
ATOM   11196 C  CG2 . THR B  1 542 ? 18.810  11.002  81.323  1.00 50.62  ? 542  THR C CG2 1 
ATOM   11197 N  N   . LEU B  1 543 ? 21.892  7.691   82.763  1.00 47.48  ? 543  LEU C N   1 
ATOM   11198 C  CA  . LEU B  1 543 ? 23.262  7.196   82.883  1.00 40.21  ? 543  LEU C CA  1 
ATOM   11199 C  C   . LEU B  1 543 ? 23.357  5.693   83.108  1.00 44.43  ? 543  LEU C C   1 
ATOM   11200 O  O   . LEU B  1 543 ? 24.458  5.150   83.174  1.00 46.02  ? 543  LEU C O   1 
ATOM   11201 C  CB  . LEU B  1 543 ? 24.005  7.920   83.993  1.00 45.67  ? 543  LEU C CB  1 
ATOM   11202 C  CG  . LEU B  1 543 ? 24.115  9.449   83.953  1.00 52.10  ? 543  LEU C CG  1 
ATOM   11203 C  CD1 . LEU B  1 543 ? 25.379  9.884   84.669  1.00 60.55  ? 543  LEU C CD1 1 
ATOM   11204 C  CD2 . LEU B  1 543 ? 24.103  10.029  82.550  1.00 59.31  ? 543  LEU C CD2 1 
ATOM   11205 N  N   . GLN B  1 544 ? 22.213  5.020   83.195  1.00 47.81  ? 544  GLN C N   1 
ATOM   11206 C  CA  . GLN B  1 544 ? 22.183  3.560   83.313  1.00 54.14  ? 544  GLN C CA  1 
ATOM   11207 C  C   . GLN B  1 544 ? 21.126  3.011   82.352  1.00 49.10  ? 544  GLN C C   1 
ATOM   11208 O  O   . GLN B  1 544 ? 20.155  3.698   82.039  1.00 41.63  ? 544  GLN C O   1 
ATOM   11209 C  CB  . GLN B  1 544 ? 21.910  3.107   84.778  1.00 56.51  ? 544  GLN C CB  1 
ATOM   11210 C  CG  . GLN B  1 544 ? 20.430  3.019   85.212  1.00 55.22  ? 544  GLN C CG  1 
ATOM   11211 C  CD  . GLN B  1 544 ? 20.226  2.778   86.735  1.00 69.53  ? 544  GLN C CD  1 
ATOM   11212 O  OE1 . GLN B  1 544 ? 21.075  2.196   87.426  1.00 68.37  ? 544  GLN C OE1 1 
ATOM   11213 N  NE2 . GLN B  1 544 ? 19.085  3.229   87.248  1.00 63.20  ? 544  GLN C NE2 1 
ATOM   11214 N  N   . LYS B  1 545 ? 21.310  1.776   81.886  1.00 51.12  ? 545  LYS C N   1 
ATOM   11215 C  CA  . LYS B  1 545 ? 20.407  1.226   80.875  1.00 52.47  ? 545  LYS C CA  1 
ATOM   11216 C  C   . LYS B  1 545 ? 19.181  0.619   81.495  1.00 53.86  ? 545  LYS C C   1 
ATOM   11217 O  O   . LYS B  1 545 ? 19.161  0.368   82.689  1.00 64.78  ? 545  LYS C O   1 
ATOM   11218 C  CB  . LYS B  1 545 ? 21.110  0.178   80.010  1.00 49.26  ? 545  LYS C CB  1 
ATOM   11219 C  CG  . LYS B  1 545 ? 21.926  -0.848  80.761  1.00 59.65  ? 545  LYS C CG  1 
ATOM   11220 C  CD  . LYS B  1 545 ? 22.111  -2.088  79.900  1.00 56.46  ? 545  LYS C CD  1 
ATOM   11221 C  CE  . LYS B  1 545 ? 23.151  -3.004  80.489  1.00 63.14  ? 545  LYS C CE  1 
ATOM   11222 N  NZ  . LYS B  1 545 ? 24.467  -2.342  80.512  1.00 70.35  ? 545  LYS C NZ  1 
ATOM   11223 N  N   . GLY B  1 546 ? 18.149  0.404   80.689  1.00 55.05  ? 546  GLY C N   1 
ATOM   11224 C  CA  . GLY B  1 546 ? 17.013  -0.390  81.121  1.00 55.17  ? 546  GLY C CA  1 
ATOM   11225 C  C   . GLY B  1 546 ? 15.775  0.364   81.568  1.00 55.88  ? 546  GLY C C   1 
ATOM   11226 O  O   . GLY B  1 546 ? 15.790  1.580   81.746  1.00 59.66  ? 546  GLY C O   1 
ATOM   11227 N  N   . ILE B  1 547 ? 14.688  -0.382  81.729  1.00 60.23  ? 547  ILE C N   1 
ATOM   11228 C  CA  . ILE B  1 547 ? 13.451  0.112   82.320  1.00 58.74  ? 547  ILE C CA  1 
ATOM   11229 C  C   . ILE B  1 547 ? 13.207  -0.624  83.647  1.00 64.43  ? 547  ILE C C   1 
ATOM   11230 O  O   . ILE B  1 547 ? 13.440  -1.833  83.752  1.00 59.48  ? 547  ILE C O   1 
ATOM   11231 C  CB  . ILE B  1 547 ? 12.250  -0.076  81.353  1.00 62.70  ? 547  ILE C CB  1 
ATOM   11232 C  CG1 . ILE B  1 547 ? 10.950  0.473   81.952  1.00 61.39  ? 547  ILE C CG1 1 
ATOM   11233 C  CG2 . ILE B  1 547 ? 12.102  -1.540  80.930  1.00 60.23  ? 547  ILE C CG2 1 
ATOM   11234 C  CD1 . ILE B  1 547 ? 9.849   0.677   80.938  1.00 52.64  ? 547  ILE C CD1 1 
ATOM   11235 N  N   . PRO B  1 548 ? 12.774  0.106   84.686  1.00 65.97  ? 548  PRO C N   1 
ATOM   11236 C  CA  . PRO B  1 548 ? 12.497  -0.607  85.934  1.00 65.73  ? 548  PRO C CA  1 
ATOM   11237 C  C   . PRO B  1 548 ? 11.156  -1.329  85.906  1.00 63.72  ? 548  PRO C C   1 
ATOM   11238 O  O   . PRO B  1 548 ? 10.296  -1.057  85.068  1.00 61.77  ? 548  PRO C O   1 
ATOM   11239 C  CB  . PRO B  1 548 ? 12.497  0.510   86.977  1.00 61.92  ? 548  PRO C CB  1 
ATOM   11240 C  CG  . PRO B  1 548 ? 12.048  1.697   86.232  1.00 64.20  ? 548  PRO C CG  1 
ATOM   11241 C  CD  . PRO B  1 548 ? 12.652  1.561   84.851  1.00 64.00  ? 548  PRO C CD  1 
ATOM   11242 N  N   . LEU B  1 549 ? 11.003  -2.265  86.832  1.00 70.98  ? 549  LEU C N   1 
ATOM   11243 C  CA  . LEU B  1 549 ? 9.734   -2.936  87.067  1.00 69.44  ? 549  LEU C CA  1 
ATOM   11244 C  C   . LEU B  1 549 ? 9.197   -2.527  88.435  1.00 74.32  ? 549  LEU C C   1 
ATOM   11245 O  O   . LEU B  1 549 ? 9.944   -2.503  89.422  1.00 72.29  ? 549  LEU C O   1 
ATOM   11246 C  CB  . LEU B  1 549 ? 9.906   -4.448  86.988  1.00 70.93  ? 549  LEU C CB  1 
ATOM   11247 C  CG  . LEU B  1 549 ? 8.766   -5.300  87.540  1.00 74.53  ? 549  LEU C CG  1 
ATOM   11248 C  CD1 . LEU B  1 549 ? 7.517   -5.119  86.688  1.00 71.27  ? 549  LEU C CD1 1 
ATOM   11249 C  CD2 . LEU B  1 549 ? 9.193   -6.771  87.640  1.00 70.68  ? 549  LEU C CD2 1 
ATOM   11250 N  N   . LEU B  1 550 ? 7.912   -2.185  88.491  1.00 79.85  ? 550  LEU C N   1 
ATOM   11251 C  CA  . LEU B  1 550 ? 7.280   -1.776  89.747  1.00 80.75  ? 550  LEU C CA  1 
ATOM   11252 C  C   . LEU B  1 550 ? 6.404   -2.888  90.318  1.00 82.68  ? 550  LEU C C   1 
ATOM   11253 O  O   . LEU B  1 550 ? 5.310   -3.150  89.804  1.00 80.29  ? 550  LEU C O   1 
ATOM   11254 C  CB  . LEU B  1 550 ? 6.441   -0.514  89.544  1.00 76.40  ? 550  LEU C CB  1 
ATOM   11255 C  CG  . LEU B  1 550 ? 5.661   -0.002  90.758  1.00 80.82  ? 550  LEU C CG  1 
ATOM   11256 C  CD1 . LEU B  1 550 ? 6.584   0.625   91.807  1.00 74.82  ? 550  LEU C CD1 1 
ATOM   11257 C  CD2 . LEU B  1 550 ? 4.571   0.976   90.326  1.00 85.51  ? 550  LEU C CD2 1 
ATOM   11258 N  N   . VAL B  1 551 ? 6.895   -3.536  91.376  1.00 77.59  ? 551  VAL C N   1 
ATOM   11259 C  CA  . VAL B  1 551 ? 6.145   -4.578  92.074  1.00 81.84  ? 551  VAL C CA  1 
ATOM   11260 C  C   . VAL B  1 551 ? 5.257   -3.989  93.178  1.00 77.59  ? 551  VAL C C   1 
ATOM   11261 O  O   . VAL B  1 551 ? 5.734   -3.330  94.103  1.00 72.19  ? 551  VAL C O   1 
ATOM   11262 C  CB  . VAL B  1 551 ? 7.088   -5.637  92.672  1.00 79.46  ? 551  VAL C CB  1 
ATOM   11263 C  CG1 . VAL B  1 551 ? 6.334   -6.557  93.597  1.00 83.05  ? 551  VAL C CG1 1 
ATOM   11264 C  CG2 . VAL B  1 551 ? 7.738   -6.439  91.560  1.00 80.89  ? 551  VAL C CG2 1 
ATOM   11265 N  N   . VAL B  1 552 ? 3.956   -4.225  93.045  1.00 78.49  ? 552  VAL C N   1 
ATOM   11266 C  CA  . VAL B  1 552 ? 2.960   -3.735  93.985  1.00 82.78  ? 552  VAL C CA  1 
ATOM   11267 C  C   . VAL B  1 552 ? 2.209   -4.886  94.647  1.00 90.89  ? 552  VAL C C   1 
ATOM   11268 O  O   . VAL B  1 552 ? 1.446   -5.595  93.988  1.00 88.50  ? 552  VAL C O   1 
ATOM   11269 C  CB  . VAL B  1 552 ? 1.928   -2.820  93.293  1.00 82.47  ? 552  VAL C CB  1 
ATOM   11270 C  CG1 . VAL B  1 552 ? 0.782   -2.488  94.238  1.00 83.94  ? 552  VAL C CG1 1 
ATOM   11271 C  CG2 . VAL B  1 552 ? 2.588   -1.562  92.776  1.00 78.05  ? 552  VAL C CG2 1 
ATOM   11272 N  N   . LYS B  1 553 ? 2.446   -5.075  95.945  1.00 96.07  ? 553  LYS C N   1 
ATOM   11273 C  CA  . LYS B  1 553 ? 1.606   -5.939  96.769  1.00 92.90  ? 553  LYS C CA  1 
ATOM   11274 C  C   . LYS B  1 553 ? 0.733   -5.039  97.629  1.00 94.12  ? 553  LYS C C   1 
ATOM   11275 O  O   . LYS B  1 553 ? 1.248   -4.224  98.392  1.00 91.04  ? 553  LYS C O   1 
ATOM   11276 C  CB  . LYS B  1 553 ? 2.448   -6.880  97.636  1.00 91.99  ? 553  LYS C CB  1 
ATOM   11277 C  CG  . LYS B  1 553 ? 1.706   -8.137  98.078  1.00 96.03  ? 553  LYS C CG  1 
ATOM   11278 C  CD  . LYS B  1 553 ? 2.657   -9.214  98.590  1.00 95.53  ? 553  LYS C CD  1 
ATOM   11279 C  CE  . LYS B  1 553 ? 1.905   -10.458 99.064  1.00 102.81 ? 553  LYS C CE  1 
ATOM   11280 N  NZ  . LYS B  1 553 ? 1.072   -11.080 97.989  1.00 94.39  ? 553  LYS C NZ  1 
ATOM   11281 N  N   . GLN B  1 554 ? -0.583  -5.163  97.482  1.00 99.36  ? 554  GLN C N   1 
ATOM   11282 C  CA  . GLN B  1 554 ? -1.518  -4.307  98.212  1.00 101.00 ? 554  GLN C CA  1 
ATOM   11283 C  C   . GLN B  1 554 ? -2.286  -5.086  99.290  1.00 106.79 ? 554  GLN C C   1 
ATOM   11284 O  O   . GLN B  1 554 ? -2.952  -6.081  98.992  1.00 104.20 ? 554  GLN C O   1 
ATOM   11285 C  CB  . GLN B  1 554 ? -2.503  -3.646  97.242  1.00 96.83  ? 554  GLN C CB  1 
ATOM   11286 C  CG  . GLN B  1 554 ? -3.479  -2.688  97.900  1.00 107.63 ? 554  GLN C CG  1 
ATOM   11287 C  CD  . GLN B  1 554 ? -4.818  -2.639  97.192  1.00 107.64 ? 554  GLN C CD  1 
ATOM   11288 O  OE1 . GLN B  1 554 ? -5.073  -3.417  96.277  1.00 102.07 ? 554  GLN C OE1 1 
ATOM   11289 N  NE2 . GLN B  1 554 ? -5.685  -1.726  97.620  1.00 108.62 ? 554  GLN C NE2 1 
ATOM   11290 N  N   . ASP B  1 555 ? -2.179  -4.625  100.538 1.00 109.10 ? 555  ASP C N   1 
ATOM   11291 C  CA  . ASP B  1 555 ? -2.879  -5.226  101.674 1.00 105.76 ? 555  ASP C CA  1 
ATOM   11292 C  C   . ASP B  1 555 ? -4.038  -4.353  102.143 1.00 104.94 ? 555  ASP C C   1 
ATOM   11293 O  O   . ASP B  1 555 ? -3.912  -3.627  103.123 1.00 100.43 ? 555  ASP C O   1 
ATOM   11294 C  CB  . ASP B  1 555 ? -1.918  -5.464  102.841 1.00 105.26 ? 555  ASP C CB  1 
ATOM   11295 C  CG  . ASP B  1 555 ? -1.476  -6.917  102.957 1.00 114.02 ? 555  ASP C CG  1 
ATOM   11296 O  OD1 . ASP B  1 555 ? -2.156  -7.810  102.399 1.00 115.30 ? 555  ASP C OD1 1 
ATOM   11297 O  OD2 . ASP B  1 555 ? -0.448  -7.166  103.621 1.00 110.75 ? 555  ASP C OD2 1 
ATOM   11298 N  N   . GLY B  1 556 ? -5.166  -4.437  101.446 1.00 106.81 ? 556  GLY C N   1 
ATOM   11299 C  CA  . GLY B  1 556 ? -6.328  -3.635  101.776 1.00 105.53 ? 556  GLY C CA  1 
ATOM   11300 C  C   . GLY B  1 556 ? -6.162  -2.190  101.351 1.00 111.33 ? 556  GLY C C   1 
ATOM   11301 O  O   . GLY B  1 556 ? -6.297  -1.860  100.172 1.00 116.07 ? 556  GLY C O   1 
ATOM   11302 N  N   . CYS B  1 557 ? -5.870  -1.324  102.317 1.00 115.87 ? 557  CYS C N   1 
ATOM   11303 C  CA  . CYS B  1 557 ? -5.658  0.098   102.048 1.00 118.25 ? 557  CYS C CA  1 
ATOM   11304 C  C   . CYS B  1 557 ? -4.168  0.436   102.074 1.00 114.55 ? 557  CYS C C   1 
ATOM   11305 O  O   . CYS B  1 557 ? -3.763  1.554   101.762 1.00 113.97 ? 557  CYS C O   1 
ATOM   11306 C  CB  . CYS B  1 557 ? -6.427  0.961   103.058 1.00 120.31 ? 557  CYS C CB  1 
ATOM   11307 S  SG  . CYS B  1 557 ? -6.405  0.350   104.771 1.00 122.52 ? 557  CYS C SG  1 
ATOM   11308 N  N   . SER B  1 558 ? -3.354  -0.546  102.443 1.00 110.71 ? 558  SER C N   1 
ATOM   11309 C  CA  . SER B  1 558 ? -1.906  -0.394  102.411 1.00 109.44 ? 558  SER C CA  1 
ATOM   11310 C  C   . SER B  1 558 ? -1.330  -1.072  101.172 1.00 105.12 ? 558  SER C C   1 
ATOM   11311 O  O   . SER B  1 558 ? -1.840  -2.100  100.732 1.00 102.50 ? 558  SER C O   1 
ATOM   11312 C  CB  . SER B  1 558 ? -1.276  -0.976  103.676 1.00 107.29 ? 558  SER C CB  1 
ATOM   11313 O  OG  . SER B  1 558 ? 0.134   -1.030  103.560 1.00 109.09 ? 558  SER C OG  1 
ATOM   11314 N  N   . LEU B  1 559 ? -0.273  -0.489  100.613 1.00 105.70 ? 559  LEU C N   1 
ATOM   11315 C  CA  . LEU B  1 559 ? 0.366   -1.027  99.413  1.00 99.56  ? 559  LEU C CA  1 
ATOM   11316 C  C   . LEU B  1 559 ? 1.883   -0.955  99.526  1.00 92.77  ? 559  LEU C C   1 
ATOM   11317 O  O   . LEU B  1 559 ? 2.442   0.092   99.845  1.00 91.83  ? 559  LEU C O   1 
ATOM   11318 C  CB  . LEU B  1 559 ? -0.111  -0.278  98.165  1.00 100.17 ? 559  LEU C CB  1 
ATOM   11319 C  CG  . LEU B  1 559 ? -0.140  1.258   98.206  1.00 105.35 ? 559  LEU C CG  1 
ATOM   11320 C  CD1 . LEU B  1 559 ? 1.137   1.879   97.643  1.00 98.87  ? 559  LEU C CD1 1 
ATOM   11321 C  CD2 . LEU B  1 559 ? -1.365  1.796   97.471  1.00 108.76 ? 559  LEU C CD2 1 
ATOM   11322 N  N   . ARG B  1 560 ? 2.548   -2.078  99.280  1.00 91.29  ? 560  ARG C N   1 
ATOM   11323 C  CA  . ARG B  1 560 ? 4.000   -2.105  99.355  1.00 84.63  ? 560  ARG C CA  1 
ATOM   11324 C  C   . ARG B  1 560 ? 4.621   -2.130  97.971  1.00 88.86  ? 560  ARG C C   1 
ATOM   11325 O  O   . ARG B  1 560 ? 4.302   -2.987  97.140  1.00 85.48  ? 560  ARG C O   1 
ATOM   11326 C  CB  . ARG B  1 560 ? 4.493   -3.301  100.153 1.00 83.25  ? 560  ARG C CB  1 
ATOM   11327 C  CG  . ARG B  1 560 ? 5.997   -3.311  100.301 1.00 86.05  ? 560  ARG C CG  1 
ATOM   11328 C  CD  . ARG B  1 560 ? 6.448   -4.478  101.128 1.00 86.79  ? 560  ARG C CD  1 
ATOM   11329 N  NE  . ARG B  1 560 ? 6.108   -5.735  100.482 1.00 100.29 ? 560  ARG C NE  1 
ATOM   11330 C  CZ  . ARG B  1 560 ? 6.995   -6.524  99.891  1.00 104.57 ? 560  ARG C CZ  1 
ATOM   11331 N  NH1 . ARG B  1 560 ? 8.278   -6.178  99.878  1.00 97.23  ? 560  ARG C NH1 1 
ATOM   11332 N  NH2 . ARG B  1 560 ? 6.600   -7.657  99.324  1.00 93.21  ? 560  ARG C NH2 1 
ATOM   11333 N  N   . LEU B  1 561 ? 5.526   -1.186  97.747  1.00 84.66  ? 561  LEU C N   1 
ATOM   11334 C  CA  . LEU B  1 561 ? 6.140   -0.985  96.449  1.00 80.44  ? 561  LEU C CA  1 
ATOM   11335 C  C   . LEU B  1 561 ? 7.596   -1.432  96.476  1.00 79.36  ? 561  LEU C C   1 
ATOM   11336 O  O   . LEU B  1 561 ? 8.316   -1.187  97.445  1.00 71.54  ? 561  LEU C O   1 
ATOM   11337 C  CB  . LEU B  1 561 ? 6.031   0.489   96.038  1.00 79.27  ? 561  LEU C CB  1 
ATOM   11338 C  CG  . LEU B  1 561 ? 4.657   1.150   96.216  1.00 72.37  ? 561  LEU C CG  1 
ATOM   11339 C  CD1 . LEU B  1 561 ? 4.737   2.658   96.115  1.00 77.09  ? 561  LEU C CD1 1 
ATOM   11340 C  CD2 . LEU B  1 561 ? 3.675   0.627   95.217  1.00 75.84  ? 561  LEU C CD2 1 
ATOM   11341 N  N   . GLN B  1 562 ? 8.011   -2.100  95.404  1.00 79.49  ? 562  GLN C N   1 
ATOM   11342 C  CA  . GLN B  1 562 ? 9.394   -2.522  95.232  1.00 76.93  ? 562  GLN C CA  1 
ATOM   11343 C  C   . GLN B  1 562 ? 9.840   -2.290  93.782  1.00 83.25  ? 562  GLN C C   1 
ATOM   11344 O  O   . GLN B  1 562 ? 9.013   -2.288  92.863  1.00 84.93  ? 562  GLN C O   1 
ATOM   11345 C  CB  . GLN B  1 562 ? 9.550   -3.995  95.615  1.00 79.55  ? 562  GLN C CB  1 
ATOM   11346 C  CG  . GLN B  1 562 ? 10.986  -4.499  95.616  1.00 79.41  ? 562  GLN C CG  1 
ATOM   11347 C  CD  . GLN B  1 562 ? 11.138  -5.831  94.901  1.00 90.52  ? 562  GLN C CD  1 
ATOM   11348 O  OE1 . GLN B  1 562 ? 10.150  -6.511  94.607  1.00 93.59  ? 562  GLN C OE1 1 
ATOM   11349 N  NE2 . GLN B  1 562 ? 12.382  -6.208  94.615  1.00 87.97  ? 562  GLN C NE2 1 
ATOM   11350 N  N   . GLN B  1 563 ? 11.138  -2.090  93.566  1.00 78.09  ? 563  GLN C N   1 
ATOM   11351 C  CA  . GLN B  1 563 ? 11.631  -1.893  92.209  1.00 77.68  ? 563  GLN C CA  1 
ATOM   11352 C  C   . GLN B  1 563 ? 12.791  -2.821  91.886  1.00 78.28  ? 563  GLN C C   1 
ATOM   11353 O  O   . GLN B  1 563 ? 13.565  -3.210  92.763  1.00 71.14  ? 563  GLN C O   1 
ATOM   11354 C  CB  . GLN B  1 563 ? 12.048  -0.433  91.987  1.00 77.97  ? 563  GLN C CB  1 
ATOM   11355 C  CG  . GLN B  1 563 ? 13.096  0.077   92.962  1.00 76.53  ? 563  GLN C CG  1 
ATOM   11356 C  CD  . GLN B  1 563 ? 14.077  1.026   92.307  1.00 72.38  ? 563  GLN C CD  1 
ATOM   11357 O  OE1 . GLN B  1 563 ? 15.019  0.600   91.632  1.00 77.48  ? 563  GLN C OE1 1 
ATOM   11358 N  NE2 . GLN B  1 563 ? 13.860  2.318   92.496  1.00 63.30  ? 563  GLN C NE2 1 
ATOM   11359 N  N   . GLU B  1 564 ? 12.889  -3.182  90.611  1.00 79.82  ? 564  GLU C N   1 
ATOM   11360 C  CA  . GLU B  1 564 ? 13.983  -4.007  90.123  1.00 76.25  ? 564  GLU C CA  1 
ATOM   11361 C  C   . GLU B  1 564 ? 14.189  -3.760  88.638  1.00 75.17  ? 564  GLU C C   1 
ATOM   11362 O  O   . GLU B  1 564 ? 13.295  -3.260  87.957  1.00 76.51  ? 564  GLU C O   1 
ATOM   11363 C  CB  . GLU B  1 564 ? 13.710  -5.486  90.394  1.00 77.32  ? 564  GLU C CB  1 
ATOM   11364 C  CG  . GLU B  1 564 ? 12.269  -5.937  90.149  1.00 79.82  ? 564  GLU C CG  1 
ATOM   11365 C  CD  . GLU B  1 564 ? 11.967  -7.298  90.786  1.00 89.17  ? 564  GLU C CD  1 
ATOM   11366 O  OE1 . GLU B  1 564 ? 12.903  -7.934  91.322  1.00 87.53  ? 564  GLU C OE1 1 
ATOM   11367 O  OE2 . GLU B  1 564 ? 10.793  -7.728  90.760  1.00 90.69  ? 564  GLU C OE2 1 
ATOM   11368 N  N   . ARG B  1 565 ? 15.370  -4.090  88.133  1.00 69.00  ? 565  ARG C N   1 
ATOM   11369 C  CA  . ARG B  1 565 ? 15.596  -4.008  86.701  1.00 71.08  ? 565  ARG C CA  1 
ATOM   11370 C  C   . ARG B  1 565 ? 14.710  -5.030  85.995  1.00 71.03  ? 565  ARG C C   1 
ATOM   11371 O  O   . ARG B  1 565 ? 14.896  -6.226  86.166  1.00 75.26  ? 565  ARG C O   1 
ATOM   11372 C  CB  . ARG B  1 565 ? 17.072  -4.246  86.379  1.00 75.68  ? 565  ARG C CB  1 
ATOM   11373 C  CG  . ARG B  1 565 ? 17.486  -3.964  84.930  1.00 68.38  ? 565  ARG C CG  1 
ATOM   11374 C  CD  . ARG B  1 565 ? 18.968  -4.247  84.766  1.00 67.87  ? 565  ARG C CD  1 
ATOM   11375 N  NE  . ARG B  1 565 ? 19.377  -4.317  83.371  1.00 70.10  ? 565  ARG C NE  1 
ATOM   11376 C  CZ  . ARG B  1 565 ? 20.486  -4.915  82.942  1.00 73.85  ? 565  ARG C CZ  1 
ATOM   11377 N  NH1 . ARG B  1 565 ? 21.306  -5.517  83.797  1.00 75.53  ? 565  ARG C NH1 1 
ATOM   11378 N  NH2 . ARG B  1 565 ? 20.771  -4.922  81.647  1.00 70.16  ? 565  ARG C NH2 1 
ATOM   11379 N  N   . PHE B  1 566 ? 13.738  -4.559  85.216  1.00 74.10  ? 566  PHE C N   1 
ATOM   11380 C  CA  . PHE B  1 566 ? 12.847  -5.457  84.465  1.00 71.31  ? 566  PHE C CA  1 
ATOM   11381 C  C   . PHE B  1 566 ? 13.582  -6.148  83.328  1.00 69.62  ? 566  PHE C C   1 
ATOM   11382 O  O   . PHE B  1 566 ? 13.875  -5.527  82.312  1.00 80.07  ? 566  PHE C O   1 
ATOM   11383 C  CB  . PHE B  1 566 ? 11.642  -4.684  83.907  1.00 66.15  ? 566  PHE C CB  1 
ATOM   11384 C  CG  . PHE B  1 566 ? 10.741  -5.506  83.033  1.00 68.94  ? 566  PHE C CG  1 
ATOM   11385 C  CD1 . PHE B  1 566 ? 9.771   -6.323  83.587  1.00 75.39  ? 566  PHE C CD1 1 
ATOM   11386 C  CD2 . PHE B  1 566 ? 10.848  -5.451  81.652  1.00 69.84  ? 566  PHE C CD2 1 
ATOM   11387 C  CE1 . PHE B  1 566 ? 8.931   -7.085  82.773  1.00 78.03  ? 566  PHE C CE1 1 
ATOM   11388 C  CE2 . PHE B  1 566 ? 10.016  -6.211  80.834  1.00 70.67  ? 566  PHE C CE2 1 
ATOM   11389 C  CZ  . PHE B  1 566 ? 9.059   -7.024  81.392  1.00 72.88  ? 566  PHE C CZ  1 
ATOM   11390 N  N   . LEU B  1 567 ? 13.894  -7.428  83.492  1.00 73.82  ? 567  LEU C N   1 
ATOM   11391 C  CA  . LEU B  1 567 ? 14.473  -8.204  82.394  1.00 72.30  ? 567  LEU C CA  1 
ATOM   11392 C  C   . LEU B  1 567 ? 13.374  -8.753  81.489  1.00 74.66  ? 567  LEU C C   1 
ATOM   11393 O  O   . LEU B  1 567 ? 12.211  -8.363  81.610  1.00 77.67  ? 567  LEU C O   1 
ATOM   11394 C  CB  . LEU B  1 567 ? 15.340  -9.342  82.921  1.00 73.99  ? 567  LEU C CB  1 
ATOM   11395 C  CG  . LEU B  1 567 ? 16.843  -9.091  82.832  1.00 77.57  ? 567  LEU C CG  1 
ATOM   11396 C  CD1 . LEU B  1 567 ? 17.285  -9.001  81.374  1.00 71.89  ? 567  LEU C CD1 1 
ATOM   11397 C  CD2 . LEU B  1 567 ? 17.205  -7.829  83.590  1.00 75.77  ? 567  LEU C CD2 1 
ATOM   11398 N  N   . GLN B  1 568 ? 13.740  -9.654  80.582  1.00 77.03  ? 568  GLN C N   1 
ATOM   11399 C  CA  . GLN B  1 568 ? 12.779  -10.189 79.623  1.00 73.90  ? 568  GLN C CA  1 
ATOM   11400 C  C   . GLN B  1 568 ? 13.242  -11.536 79.106  1.00 81.12  ? 568  GLN C C   1 
ATOM   11401 O  O   . GLN B  1 568 ? 14.096  -11.612 78.227  1.00 85.37  ? 568  GLN C O   1 
ATOM   11402 C  CB  . GLN B  1 568 ? 12.579  -9.212  78.466  1.00 73.37  ? 568  GLN C CB  1 
ATOM   11403 C  CG  . GLN B  1 568 ? 11.586  -9.659  77.414  1.00 71.26  ? 568  GLN C CG  1 
ATOM   11404 C  CD  . GLN B  1 568 ? 10.165  -9.713  77.922  1.00 74.32  ? 568  GLN C CD  1 
ATOM   11405 O  OE1 . GLN B  1 568 ? 9.672   -10.776 78.297  1.00 81.97  ? 568  GLN C OE1 1 
ATOM   11406 N  NE2 . GLN B  1 568 ? 9.487   -8.567  77.920  1.00 74.50  ? 568  GLN C NE2 1 
ATOM   11407 N  N   . GLY B  1 569 ? 12.671  -12.600 79.662  1.00 90.01  ? 569  GLY C N   1 
ATOM   11408 C  CA  . GLY B  1 569 ? 13.112  -13.950 79.363  1.00 93.06  ? 569  GLY C CA  1 
ATOM   11409 C  C   . GLY B  1 569 ? 14.080  -14.472 80.407  1.00 93.63  ? 569  GLY C C   1 
ATOM   11410 O  O   . GLY B  1 569 ? 14.545  -15.606 80.320  1.00 100.55 ? 569  GLY C O   1 
ATOM   11411 N  N   . VAL B  1 570 ? 14.395  -13.635 81.392  1.00 94.54  ? 570  VAL C N   1 
ATOM   11412 C  CA  . VAL B  1 570 ? 15.270  -14.032 82.492  1.00 99.48  ? 570  VAL C CA  1 
ATOM   11413 C  C   . VAL B  1 570 ? 14.469  -14.046 83.788  1.00 104.40 ? 570  VAL C C   1 
ATOM   11414 O  O   . VAL B  1 570 ? 14.396  -13.041 84.494  1.00 104.37 ? 570  VAL C O   1 
ATOM   11415 C  CB  . VAL B  1 570 ? 16.482  -13.089 82.643  1.00 96.92  ? 570  VAL C CB  1 
ATOM   11416 C  CG1 . VAL B  1 570 ? 17.534  -13.715 83.553  1.00 103.18 ? 570  VAL C CG1 1 
ATOM   11417 C  CG2 . VAL B  1 570 ? 17.078  -12.770 81.281  1.00 94.30  ? 570  VAL C CG2 1 
ATOM   11418 N  N   . PHE B  1 571 ? 13.868  -15.195 84.088  1.00 110.44 ? 571  PHE C N   1 
ATOM   11419 C  CA  . PHE B  1 571 ? 12.966  -15.342 85.227  1.00 109.29 ? 571  PHE C CA  1 
ATOM   11420 C  C   . PHE B  1 571 ? 13.720  -15.263 86.555  1.00 109.52 ? 571  PHE C C   1 
ATOM   11421 O  O   . PHE B  1 571 ? 14.919  -15.551 86.618  1.00 107.41 ? 571  PHE C O   1 
ATOM   11422 C  CB  . PHE B  1 571 ? 12.204  -16.668 85.131  1.00 109.11 ? 571  PHE C CB  1 
ATOM   11423 C  CG  . PHE B  1 571 ? 12.006  -17.163 83.718  1.00 107.26 ? 571  PHE C CG  1 
ATOM   11424 C  CD1 . PHE B  1 571 ? 12.966  -17.962 83.105  1.00 106.57 ? 571  PHE C CD1 1 
ATOM   11425 C  CD2 . PHE B  1 571 ? 10.855  -16.847 83.010  1.00 98.49  ? 571  PHE C CD2 1 
ATOM   11426 C  CE1 . PHE B  1 571 ? 12.792  -18.424 81.813  1.00 97.79  ? 571  PHE C CE1 1 
ATOM   11427 C  CE2 . PHE B  1 571 ? 10.673  -17.307 81.715  1.00 97.83  ? 571  PHE C CE2 1 
ATOM   11428 C  CZ  . PHE B  1 571 ? 11.646  -18.097 81.118  1.00 99.44  ? 571  PHE C CZ  1 
ATOM   11429 N  N   . GLN B  1 572 ? 13.007  -14.875 87.610  1.00 104.83 ? 572  GLN C N   1 
ATOM   11430 C  CA  . GLN B  1 572 ? 13.604  -14.698 88.930  1.00 106.34 ? 572  GLN C CA  1 
ATOM   11431 C  C   . GLN B  1 572 ? 14.318  -15.964 89.370  1.00 108.45 ? 572  GLN C C   1 
ATOM   11432 O  O   . GLN B  1 572 ? 15.350  -15.915 90.038  1.00 108.49 ? 572  GLN C O   1 
ATOM   11433 C  CB  . GLN B  1 572 ? 12.533  -14.314 89.943  1.00 105.58 ? 572  GLN C CB  1 
ATOM   11434 C  CG  . GLN B  1 572 ? 13.054  -13.561 91.147  1.00 101.68 ? 572  GLN C CG  1 
ATOM   11435 C  CD  . GLN B  1 572 ? 11.967  -12.736 91.796  1.00 104.77 ? 572  GLN C CD  1 
ATOM   11436 O  OE1 . GLN B  1 572 ? 10.781  -13.045 91.665  1.00 107.80 ? 572  GLN C OE1 1 
ATOM   11437 N  NE2 . GLN B  1 572 ? 12.360  -11.669 92.485  1.00 102.21 ? 572  GLN C NE2 1 
ATOM   11438 N  N   . GLU B  1 573 ? 13.745  -17.093 88.971  1.00 112.64 ? 573  GLU C N   1 
ATOM   11439 C  CA  . GLU B  1 573 ? 14.320  -18.414 89.181  1.00 112.53 ? 573  GLU C CA  1 
ATOM   11440 C  C   . GLU B  1 573 ? 15.735  -18.509 88.624  1.00 117.41 ? 573  GLU C C   1 
ATOM   11441 O  O   . GLU B  1 573 ? 16.649  -18.952 89.319  1.00 121.54 ? 573  GLU C O   1 
ATOM   11442 C  CB  . GLU B  1 573 ? 13.443  -19.487 88.523  1.00 108.58 ? 573  GLU C CB  1 
ATOM   11443 C  CG  . GLU B  1 573 ? 12.001  -19.536 89.000  1.00 107.93 ? 573  GLU C CG  1 
ATOM   11444 C  CD  . GLU B  1 573 ? 11.125  -18.450 88.398  1.00 112.15 ? 573  GLU C CD  1 
ATOM   11445 O  OE1 . GLU B  1 573 ? 11.621  -17.327 88.160  1.00 113.02 ? 573  GLU C OE1 1 
ATOM   11446 O  OE2 . GLU B  1 573 ? 9.927   -18.721 88.174  1.00 114.16 ? 573  GLU C OE2 1 
ATOM   11447 N  N   . ASP B  1 574 ? 15.900  -18.101 87.365  1.00 120.19 ? 574  ASP C N   1 
ATOM   11448 C  CA  . ASP B  1 574 ? 17.178  -18.223 86.663  1.00 122.05 ? 574  ASP C CA  1 
ATOM   11449 C  C   . ASP B  1 574 ? 18.296  -17.540 87.441  1.00 122.93 ? 574  ASP C C   1 
ATOM   11450 O  O   . ASP B  1 574 ? 18.099  -16.460 88.003  1.00 119.60 ? 574  ASP C O   1 
ATOM   11451 C  CB  . ASP B  1 574 ? 17.076  -17.643 85.249  1.00 119.40 ? 574  ASP C CB  1 
ATOM   11452 C  CG  . ASP B  1 574 ? 16.207  -18.490 84.334  1.00 121.19 ? 574  ASP C CG  1 
ATOM   11453 O  OD1 . ASP B  1 574 ? 15.263  -19.131 84.841  1.00 117.23 ? 574  ASP C OD1 1 
ATOM   11454 O  OD2 . ASP B  1 574 ? 16.468  -18.521 83.109  1.00 125.08 ? 574  ASP C OD2 1 
ATOM   11455 N  N   . PRO B  1 575 ? 19.473  -18.184 87.488  1.00 126.06 ? 575  PRO C N   1 
ATOM   11456 C  CA  . PRO B  1 575 ? 20.590  -17.711 88.316  1.00 128.03 ? 575  PRO C CA  1 
ATOM   11457 C  C   . PRO B  1 575 ? 21.119  -16.350 87.857  1.00 126.52 ? 575  PRO C C   1 
ATOM   11458 O  O   . PRO B  1 575 ? 21.401  -15.476 88.687  1.00 121.30 ? 575  PRO C O   1 
ATOM   11459 C  CB  . PRO B  1 575 ? 21.646  -18.809 88.136  1.00 130.24 ? 575  PRO C CB  1 
ATOM   11460 C  CG  . PRO B  1 575 ? 21.313  -19.449 86.819  1.00 124.54 ? 575  PRO C CG  1 
ATOM   11461 C  CD  . PRO B  1 575 ? 19.821  -19.390 86.712  1.00 121.72 ? 575  PRO C CD  1 
ATOM   11462 N  N   . GLU B  1 576 ? 21.227  -16.184 86.540  1.00 127.02 ? 576  GLU C N   1 
ATOM   11463 C  CA  . GLU B  1 576 ? 21.747  -14.966 85.934  1.00 119.22 ? 576  GLU C CA  1 
ATOM   11464 C  C   . GLU B  1 576 ? 20.951  -13.756 86.372  1.00 112.41 ? 576  GLU C C   1 
ATOM   11465 O  O   . GLU B  1 576 ? 21.497  -12.663 86.486  1.00 111.76 ? 576  GLU C O   1 
ATOM   11466 C  CB  . GLU B  1 576 ? 21.724  -15.067 84.406  1.00 122.57 ? 576  GLU C CB  1 
ATOM   11467 C  CG  . GLU B  1 576 ? 22.469  -16.265 83.832  1.00 127.04 ? 576  GLU C CG  1 
ATOM   11468 C  CD  . GLU B  1 576 ? 21.656  -17.543 83.894  1.00 130.45 ? 576  GLU C CD  1 
ATOM   11469 O  OE1 . GLU B  1 576 ? 20.444  -17.464 84.191  1.00 131.20 ? 576  GLU C OE1 1 
ATOM   11470 O  OE2 . GLU B  1 576 ? 22.230  -18.624 83.650  1.00 136.35 ? 576  GLU C OE2 1 
ATOM   11471 N  N   . TRP B  1 577 ? 19.663  -13.967 86.625  1.00 112.81 ? 577  TRP C N   1 
ATOM   11472 C  CA  . TRP B  1 577 ? 18.745  -12.886 86.972  1.00 113.37 ? 577  TRP C CA  1 
ATOM   11473 C  C   . TRP B  1 577 ? 19.248  -11.986 88.097  1.00 109.37 ? 577  TRP C C   1 
ATOM   11474 O  O   . TRP B  1 577 ? 19.211  -10.765 87.978  1.00 106.24 ? 577  TRP C O   1 
ATOM   11475 C  CB  . TRP B  1 577 ? 17.377  -13.447 87.362  1.00 110.80 ? 577  TRP C CB  1 
ATOM   11476 C  CG  . TRP B  1 577 ? 16.398  -12.374 87.743  1.00 104.33 ? 577  TRP C CG  1 
ATOM   11477 C  CD1 . TRP B  1 577 ? 15.586  -11.671 86.905  1.00 101.61 ? 577  TRP C CD1 1 
ATOM   11478 C  CD2 . TRP B  1 577 ? 16.135  -11.881 89.060  1.00 101.25 ? 577  TRP C CD2 1 
ATOM   11479 N  NE1 . TRP B  1 577 ? 14.830  -10.773 87.618  1.00 99.59  ? 577  TRP C NE1 1 
ATOM   11480 C  CE2 . TRP B  1 577 ? 15.149  -10.883 88.944  1.00 99.51  ? 577  TRP C CE2 1 
ATOM   11481 C  CE3 . TRP B  1 577 ? 16.632  -12.192 90.325  1.00 105.58 ? 577  TRP C CE3 1 
ATOM   11482 C  CZ2 . TRP B  1 577 ? 14.657  -10.189 90.044  1.00 96.36  ? 577  TRP C CZ2 1 
ATOM   11483 C  CZ3 . TRP B  1 577 ? 16.146  -11.503 91.417  1.00 104.02 ? 577  TRP C CZ3 1 
ATOM   11484 C  CH2 . TRP B  1 577 ? 15.167  -10.513 91.270  1.00 102.67 ? 577  TRP C CH2 1 
ATOM   11485 N  N   . ARG B  1 578 ? 19.698  -12.575 89.196  1.00 109.29 ? 578  ARG C N   1 
ATOM   11486 C  CA  . ARG B  1 578 ? 20.215  -11.761 90.286  1.00 111.07 ? 578  ARG C CA  1 
ATOM   11487 C  C   . ARG B  1 578 ? 21.724  -11.815 90.285  1.00 113.20 ? 578  ARG C C   1 
ATOM   11488 O  O   . ARG B  1 578 ? 22.313  -12.775 89.779  1.00 115.74 ? 578  ARG C O   1 
ATOM   11489 C  CB  . ARG B  1 578 ? 19.667  -12.221 91.636  1.00 114.58 ? 578  ARG C CB  1 
ATOM   11490 C  CG  . ARG B  1 578 ? 19.515  -11.103 92.664  1.00 112.28 ? 578  ARG C CG  1 
ATOM   11491 C  CD  . ARG B  1 578 ? 18.658  -11.568 93.832  1.00 113.95 ? 578  ARG C CD  1 
ATOM   11492 N  NE  . ARG B  1 578 ? 19.035  -12.914 94.258  1.00 114.49 ? 578  ARG C NE  1 
ATOM   11493 C  CZ  . ARG B  1 578 ? 18.172  -13.875 94.565  1.00 107.52 ? 578  ARG C CZ  1 
ATOM   11494 N  NH1 . ARG B  1 578 ? 16.869  -13.642 94.499  1.00 102.60 ? 578  ARG C NH1 1 
ATOM   11495 N  NH2 . ARG B  1 578 ? 18.615  -15.069 94.937  1.00 108.48 ? 578  ARG C NH2 1 
ATOM   11496 N  N   . ALA B  1 579 ? 22.329  -10.780 90.864  1.00 113.27 ? 579  ALA C N   1 
ATOM   11497 C  CA  . ALA B  1 579 ? 23.778  -10.579 90.873  1.00 118.96 ? 579  ALA C CA  1 
ATOM   11498 C  C   . ALA B  1 579 ? 24.309  -10.370 89.451  1.00 116.39 ? 579  ALA C C   1 
ATOM   11499 O  O   . ALA B  1 579 ? 24.032  -11.158 88.539  1.00 110.53 ? 579  ALA C O   1 
ATOM   11500 C  CB  . ALA B  1 579 ? 24.496  -11.748 91.563  1.00 116.45 ? 579  ALA C CB  1 
ATOM   11501 N  N   . LEU B  1 580 ? 25.074  -9.292  89.284  1.00 117.47 ? 580  LEU C N   1 
ATOM   11502 C  CA  . LEU B  1 580 ? 25.550  -8.854  87.977  1.00 110.99 ? 580  LEU C CA  1 
ATOM   11503 C  C   . LEU B  1 580 ? 24.362  -8.743  87.026  1.00 104.93 ? 580  LEU C C   1 
ATOM   11504 O  O   . LEU B  1 580 ? 24.433  -9.156  85.868  1.00 106.79 ? 580  LEU C O   1 
ATOM   11505 C  CB  . LEU B  1 580 ? 26.617  -9.808  87.426  1.00 117.25 ? 580  LEU C CB  1 
ATOM   11506 C  CG  . LEU B  1 580 ? 27.792  -10.157 88.350  1.00 116.70 ? 580  LEU C CG  1 
ATOM   11507 C  CD1 . LEU B  1 580 ? 28.898  -10.867 87.571  1.00 118.06 ? 580  LEU C CD1 1 
ATOM   11508 C  CD2 . LEU B  1 580 ? 28.332  -8.926  89.080  1.00 108.07 ? 580  LEU C CD2 1 
ATOM   11509 N  N   . GLN B  1 581 ? 23.267  -8.190  87.540  1.00 101.92 ? 581  GLN C N   1 
ATOM   11510 C  CA  . GLN B  1 581 ? 22.056  -8.010  86.762  1.00 97.25  ? 581  GLN C CA  1 
ATOM   11511 C  C   . GLN B  1 581 ? 21.071  -7.116  87.486  1.00 92.43  ? 581  GLN C C   1 
ATOM   11512 O  O   . GLN B  1 581 ? 20.364  -6.333  86.860  1.00 90.96  ? 581  GLN C O   1 
ATOM   11513 C  CB  . GLN B  1 581 ? 21.406  -9.350  86.469  1.00 100.39 ? 581  GLN C CB  1 
ATOM   11514 C  CG  . GLN B  1 581 ? 20.377  -9.296  85.369  1.00 98.22  ? 581  GLN C CG  1 
ATOM   11515 C  CD  . GLN B  1 581 ? 20.986  -9.522  84.006  1.00 93.67  ? 581  GLN C CD  1 
ATOM   11516 O  OE1 . GLN B  1 581 ? 22.070  -9.023  83.703  1.00 93.03  ? 581  GLN C OE1 1 
ATOM   11517 N  NE2 . GLN B  1 581 ? 20.297  -10.294 83.178  1.00 97.15  ? 581  GLN C NE2 1 
ATOM   11518 N  N   . GLU B  1 582 ? 21.028  -7.238  88.808  1.00 91.99  ? 582  GLU C N   1 
ATOM   11519 C  CA  . GLU B  1 582 ? 20.092  -6.460  89.610  1.00 92.11  ? 582  GLU C CA  1 
ATOM   11520 C  C   . GLU B  1 582 ? 20.765  -5.309  90.353  1.00 91.04  ? 582  GLU C C   1 
ATOM   11521 O  O   . GLU B  1 582 ? 20.307  -4.913  91.422  1.00 90.39  ? 582  GLU C O   1 
ATOM   11522 C  CB  . GLU B  1 582 ? 19.381  -7.360  90.619  1.00 97.23  ? 582  GLU C CB  1 
ATOM   11523 C  CG  . GLU B  1 582 ? 18.511  -8.424  89.999  1.00 97.14  ? 582  GLU C CG  1 
ATOM   11524 C  CD  . GLU B  1 582 ? 17.369  -7.847  89.197  1.00 90.03  ? 582  GLU C CD  1 
ATOM   11525 O  OE1 . GLU B  1 582 ? 16.569  -7.069  89.760  1.00 84.83  ? 582  GLU C OE1 1 
ATOM   11526 O  OE2 . GLU B  1 582 ? 17.273  -8.176  87.998  1.00 90.30  ? 582  GLU C OE2 1 
ATOM   11527 N  N   . ARG B  1 583 ? 21.832  -4.757  89.785  1.00 90.43  ? 583  ARG C N   1 
ATOM   11528 C  CA  . ARG B  1 583 ? 22.600  -3.717  90.474  1.00 91.97  ? 583  ARG C CA  1 
ATOM   11529 C  C   . ARG B  1 583 ? 22.045  -2.326  90.161  1.00 87.83  ? 583  ARG C C   1 
ATOM   11530 O  O   . ARG B  1 583 ? 22.687  -1.298  90.397  1.00 87.57  ? 583  ARG C O   1 
ATOM   11531 C  CB  . ARG B  1 583 ? 24.076  -3.807  90.091  1.00 87.01  ? 583  ARG C CB  1 
ATOM   11532 C  CG  . ARG B  1 583 ? 24.641  -5.218  90.162  1.00 94.51  ? 583  ARG C CG  1 
ATOM   11533 C  CD  . ARG B  1 583 ? 24.080  -5.993  91.349  1.00 94.67  ? 583  ARG C CD  1 
ATOM   11534 N  NE  . ARG B  1 583 ? 24.853  -7.185  91.672  1.00 101.25 ? 583  ARG C NE  1 
ATOM   11535 C  CZ  . ARG B  1 583 ? 25.453  -7.383  92.842  1.00 99.00  ? 583  ARG C CZ  1 
ATOM   11536 N  NH1 . ARG B  1 583 ? 25.363  -6.462  93.800  1.00 82.22  ? 583  ARG C NH1 1 
ATOM   11537 N  NH2 . ARG B  1 583 ? 26.136  -8.503  93.056  1.00 102.08 ? 583  ARG C NH2 1 
ATOM   11538 N  N   . TYR B  1 584 ? 20.820  -2.322  89.654  1.00 83.12  ? 584  TYR C N   1 
ATOM   11539 C  CA  . TYR B  1 584 ? 20.196  -1.130  89.124  1.00 79.20  ? 584  TYR C CA  1 
ATOM   11540 C  C   . TYR B  1 584 ? 19.161  -0.542  90.088  1.00 76.57  ? 584  TYR C C   1 
ATOM   11541 O  O   . TYR B  1 584 ? 18.489  -1.257  90.825  1.00 79.09  ? 584  TYR C O   1 
ATOM   11542 C  CB  . TYR B  1 584 ? 19.562  -1.455  87.765  1.00 78.09  ? 584  TYR C CB  1 
ATOM   11543 C  CG  . TYR B  1 584 ? 20.581  -1.778  86.677  1.00 78.30  ? 584  TYR C CG  1 
ATOM   11544 C  CD1 . TYR B  1 584 ? 21.396  -2.904  86.765  1.00 79.29  ? 584  TYR C CD1 1 
ATOM   11545 C  CD2 . TYR B  1 584 ? 20.722  -0.962  85.564  1.00 67.00  ? 584  TYR C CD2 1 
ATOM   11546 C  CE1 . TYR B  1 584 ? 22.327  -3.198  85.787  1.00 80.56  ? 584  TYR C CE1 1 
ATOM   11547 C  CE2 . TYR B  1 584 ? 21.656  -1.251  84.573  1.00 71.83  ? 584  TYR C CE2 1 
ATOM   11548 C  CZ  . TYR B  1 584 ? 22.455  -2.371  84.687  1.00 76.00  ? 584  TYR C CZ  1 
ATOM   11549 O  OH  . TYR B  1 584 ? 23.380  -2.674  83.702  1.00 68.87  ? 584  TYR C OH  1 
ATOM   11550 N  N   . LEU B  1 585 ? 19.035  0.776   90.071  1.00 73.11  ? 585  LEU C N   1 
ATOM   11551 C  CA  . LEU B  1 585 ? 18.136  1.458   90.978  1.00 63.92  ? 585  LEU C CA  1 
ATOM   11552 C  C   . LEU B  1 585 ? 17.677  2.795   90.397  1.00 66.04  ? 585  LEU C C   1 
ATOM   11553 O  O   . LEU B  1 585 ? 18.497  3.587   89.939  1.00 65.32  ? 585  LEU C O   1 
ATOM   11554 C  CB  . LEU B  1 585 ? 18.832  1.676   92.312  1.00 60.39  ? 585  LEU C CB  1 
ATOM   11555 C  CG  . LEU B  1 585 ? 18.127  2.693   93.195  1.00 59.55  ? 585  LEU C CG  1 
ATOM   11556 C  CD1 . LEU B  1 585 ? 17.090  1.985   94.054  1.00 64.25  ? 585  LEU C CD1 1 
ATOM   11557 C  CD2 . LEU B  1 585 ? 19.130  3.510   94.021  1.00 55.28  ? 585  LEU C CD2 1 
ATOM   11558 N  N   . TRP B  1 586 ? 16.373  3.055   90.428  1.00 66.50  ? 586  TRP C N   1 
ATOM   11559 C  CA  . TRP B  1 586 ? 15.824  4.293   89.873  1.00 64.04  ? 586  TRP C CA  1 
ATOM   11560 C  C   . TRP B  1 586 ? 15.132  5.155   90.921  1.00 62.13  ? 586  TRP C C   1 
ATOM   11561 O  O   . TRP B  1 586 ? 14.669  4.652   91.927  1.00 68.76  ? 586  TRP C O   1 
ATOM   11562 C  CB  . TRP B  1 586 ? 14.813  3.986   88.753  1.00 65.68  ? 586  TRP C CB  1 
ATOM   11563 C  CG  . TRP B  1 586 ? 15.413  3.441   87.485  1.00 68.41  ? 586  TRP C CG  1 
ATOM   11564 C  CD1 . TRP B  1 586 ? 15.694  4.141   86.339  1.00 67.48  ? 586  TRP C CD1 1 
ATOM   11565 C  CD2 . TRP B  1 586 ? 15.806  2.084   87.233  1.00 65.96  ? 586  TRP C CD2 1 
ATOM   11566 N  NE1 . TRP B  1 586 ? 16.238  3.299   85.393  1.00 66.33  ? 586  TRP C NE1 1 
ATOM   11567 C  CE2 . TRP B  1 586 ? 16.316  2.034   85.915  1.00 64.40  ? 586  TRP C CE2 1 
ATOM   11568 C  CE3 . TRP B  1 586 ? 15.783  0.911   87.993  1.00 64.84  ? 586  TRP C CE3 1 
ATOM   11569 C  CZ2 . TRP B  1 586 ? 16.795  0.857   85.344  1.00 63.19  ? 586  TRP C CZ2 1 
ATOM   11570 C  CZ3 . TRP B  1 586 ? 16.254  -0.263  87.421  1.00 66.45  ? 586  TRP C CZ3 1 
ATOM   11571 C  CH2 . TRP B  1 586 ? 16.752  -0.280  86.110  1.00 70.01  ? 586  TRP C CH2 1 
ATOM   11572 N  N   . HIS B  1 587 ? 15.079  6.460   90.677  1.00 64.17  ? 587  HIS C N   1 
ATOM   11573 C  CA  . HIS B  1 587 ? 14.104  7.319   91.320  1.00 62.72  ? 587  HIS C CA  1 
ATOM   11574 C  C   . HIS B  1 587 ? 12.925  7.402   90.368  1.00 61.95  ? 587  HIS C C   1 
ATOM   11575 O  O   . HIS B  1 587 ? 12.866  8.270   89.503  1.00 65.34  ? 587  HIS C O   1 
ATOM   11576 C  CB  . HIS B  1 587 ? 14.647  8.726   91.623  1.00 65.51  ? 587  HIS C CB  1 
ATOM   11577 C  CG  . HIS B  1 587 ? 15.814  8.751   92.567  1.00 66.36  ? 587  HIS C CG  1 
ATOM   11578 N  ND1 . HIS B  1 587 ? 16.382  9.928   93.013  1.00 60.82  ? 587  HIS C ND1 1 
ATOM   11579 C  CD2 . HIS B  1 587 ? 16.524  7.749   93.139  1.00 63.08  ? 587  HIS C CD2 1 
ATOM   11580 C  CE1 . HIS B  1 587 ? 17.396  9.650   93.813  1.00 63.74  ? 587  HIS C CE1 1 
ATOM   11581 N  NE2 . HIS B  1 587 ? 17.501  8.335   93.910  1.00 66.14  ? 587  HIS C NE2 1 
ATOM   11582 N  N   . ILE B  1 588 ? 11.992  6.479   90.516  1.00 62.21  ? 588  ILE C N   1 
ATOM   11583 C  CA  . ILE B  1 588 ? 10.814  6.464   89.673  1.00 62.75  ? 588  ILE C CA  1 
ATOM   11584 C  C   . ILE B  1 588 ? 9.741   7.447   90.147  1.00 68.04  ? 588  ILE C C   1 
ATOM   11585 O  O   . ILE B  1 588 ? 9.230   7.331   91.260  1.00 68.55  ? 588  ILE C O   1 
ATOM   11586 C  CB  . ILE B  1 588 ? 10.206  5.066   89.628  1.00 56.03  ? 588  ILE C CB  1 
ATOM   11587 C  CG1 . ILE B  1 588 ? 11.294  4.016   89.420  1.00 56.14  ? 588  ILE C CG1 1 
ATOM   11588 C  CG2 . ILE B  1 588 ? 9.135   5.003   88.594  1.00 52.93  ? 588  ILE C CG2 1 
ATOM   11589 C  CD1 . ILE B  1 588 ? 10.785  2.609   89.537  1.00 66.02  ? 588  ILE C CD1 1 
ATOM   11590 N  N   . PRO B  1 589 ? 9.386   8.417   89.296  1.00 71.65  ? 589  PRO C N   1 
ATOM   11591 C  CA  . PRO B  1 589 ? 8.246   9.282   89.611  1.00 68.70  ? 589  PRO C CA  1 
ATOM   11592 C  C   . PRO B  1 589 ? 6.924   8.569   89.341  1.00 70.45  ? 589  PRO C C   1 
ATOM   11593 O  O   . PRO B  1 589 ? 6.438   8.581   88.211  1.00 70.99  ? 589  PRO C O   1 
ATOM   11594 C  CB  . PRO B  1 589 ? 8.438   10.472  88.667  1.00 70.97  ? 589  PRO C CB  1 
ATOM   11595 C  CG  . PRO B  1 589 ? 9.198   9.919   87.518  1.00 63.22  ? 589  PRO C CG  1 
ATOM   11596 C  CD  . PRO B  1 589 ? 10.045  8.792   88.034  1.00 63.59  ? 589  PRO C CD  1 
ATOM   11597 N  N   . LEU B  1 590 ? 6.353   7.961   90.376  1.00 72.85  ? 590  LEU C N   1 
ATOM   11598 C  CA  . LEU B  1 590 ? 5.132   7.161   90.240  1.00 74.71  ? 590  LEU C CA  1 
ATOM   11599 C  C   . LEU B  1 590 ? 3.845   7.978   90.220  1.00 74.69  ? 590  LEU C C   1 
ATOM   11600 O  O   . LEU B  1 590 ? 3.796   9.103   90.711  1.00 77.07  ? 590  LEU C O   1 
ATOM   11601 C  CB  . LEU B  1 590 ? 5.035   6.155   91.381  1.00 74.97  ? 590  LEU C CB  1 
ATOM   11602 C  CG  . LEU B  1 590 ? 6.247   5.280   91.653  1.00 75.34  ? 590  LEU C CG  1 
ATOM   11603 C  CD1 . LEU B  1 590 ? 6.144   4.661   93.048  1.00 74.93  ? 590  LEU C CD1 1 
ATOM   11604 C  CD2 . LEU B  1 590 ? 6.315   4.209   90.581  1.00 77.20  ? 590  LEU C CD2 1 
ATOM   11605 N  N   . THR B  1 591 ? 2.802   7.382   89.653  1.00 76.77  ? 591  THR C N   1 
ATOM   11606 C  CA  . THR B  1 591 ? 1.451   7.933   89.678  1.00 79.99  ? 591  THR C CA  1 
ATOM   11607 C  C   . THR B  1 591 ? 0.471   6.790   89.876  1.00 85.71  ? 591  THR C C   1 
ATOM   11608 O  O   . THR B  1 591 ? 0.757   5.661   89.465  1.00 87.86  ? 591  THR C O   1 
ATOM   11609 C  CB  . THR B  1 591 ? 1.079   8.672   88.373  1.00 80.94  ? 591  THR C CB  1 
ATOM   11610 O  OG1 . THR B  1 591 ? 1.149   7.759   87.264  1.00 81.54  ? 591  THR C OG1 1 
ATOM   11611 C  CG2 . THR B  1 591 ? 1.999   9.876   88.130  1.00 80.62  ? 591  THR C CG2 1 
ATOM   11612 N  N   . TYR B  1 592 ? -0.669  7.071   90.505  1.00 85.51  ? 592  TYR C N   1 
ATOM   11613 C  CA  . TYR B  1 592 ? -1.785  6.126   90.499  1.00 91.13  ? 592  TYR C CA  1 
ATOM   11614 C  C   . TYR B  1 592 ? -3.119  6.798   90.775  1.00 91.53  ? 592  TYR C C   1 
ATOM   11615 O  O   . TYR B  1 592 ? -3.189  7.952   91.202  1.00 90.69  ? 592  TYR C O   1 
ATOM   11616 C  CB  . TYR B  1 592 ? -1.568  4.986   91.510  1.00 93.92  ? 592  TYR C CB  1 
ATOM   11617 C  CG  . TYR B  1 592 ? -1.472  5.396   92.969  1.00 95.69  ? 592  TYR C CG  1 
ATOM   11618 C  CD1 . TYR B  1 592 ? -2.614  5.649   93.729  1.00 99.72  ? 592  TYR C CD1 1 
ATOM   11619 C  CD2 . TYR B  1 592 ? -0.238  5.496   93.597  1.00 98.54  ? 592  TYR C CD2 1 
ATOM   11620 C  CE1 . TYR B  1 592 ? -2.519  6.011   95.069  1.00 99.43  ? 592  TYR C CE1 1 
ATOM   11621 C  CE2 . TYR B  1 592 ? -0.133  5.856   94.933  1.00 101.08 ? 592  TYR C CE2 1 
ATOM   11622 C  CZ  . TYR B  1 592 ? -1.274  6.113   95.662  1.00 101.54 ? 592  TYR C CZ  1 
ATOM   11623 O  OH  . TYR B  1 592 ? -1.159  6.468   96.984  1.00 100.43 ? 592  TYR C OH  1 
ATOM   11624 N  N   . SER B  1 593 ? -4.177  6.050   90.500  1.00 90.58  ? 593  SER C N   1 
ATOM   11625 C  CA  . SER B  1 593 ? -5.517  6.410   90.916  1.00 96.38  ? 593  SER C CA  1 
ATOM   11626 C  C   . SER B  1 593 ? -6.215  5.111   91.309  1.00 100.01 ? 593  SER C C   1 
ATOM   11627 O  O   . SER B  1 593 ? -5.924  4.050   90.753  1.00 99.03  ? 593  SER C O   1 
ATOM   11628 C  CB  . SER B  1 593 ? -6.273  7.149   89.808  1.00 95.60  ? 593  SER C CB  1 
ATOM   11629 O  OG  . SER B  1 593 ? -6.869  6.244   88.898  1.00 96.11  ? 593  SER C OG  1 
ATOM   11630 N  N   . THR B  1 594 ? -7.119  5.193   92.280  1.00 104.17 ? 594  THR C N   1 
ATOM   11631 C  CA  . THR B  1 594 ? -7.771  4.007   92.822  1.00 104.65 ? 594  THR C CA  1 
ATOM   11632 C  C   . THR B  1 594 ? -9.037  3.660   92.045  1.00 103.82 ? 594  THR C C   1 
ATOM   11633 O  O   . THR B  1 594 ? -9.355  4.305   91.045  1.00 102.37 ? 594  THR C O   1 
ATOM   11634 C  CB  . THR B  1 594 ? -8.125  4.197   94.303  1.00 101.59 ? 594  THR C CB  1 
ATOM   11635 O  OG1 . THR B  1 594 ? -9.252  5.073   94.415  1.00 102.33 ? 594  THR C OG1 1 
ATOM   11636 C  CG2 . THR B  1 594 ? -6.948  4.792   95.052  1.00 101.81 ? 594  THR C CG2 1 
ATOM   11637 N  N   . SER B  1 595 ? -9.758  2.650   92.527  1.00 102.69 ? 595  SER C N   1 
ATOM   11638 C  CA  . SER B  1 595 ? -10.943 2.135   91.848  1.00 102.98 ? 595  SER C CA  1 
ATOM   11639 C  C   . SER B  1 595 ? -11.967 3.216   91.509  1.00 105.12 ? 595  SER C C   1 
ATOM   11640 O  O   . SER B  1 595 ? -12.339 3.371   90.346  1.00 107.27 ? 595  SER C O   1 
ATOM   11641 C  CB  . SER B  1 595 ? -11.608 1.051   92.696  1.00 104.95 ? 595  SER C CB  1 
ATOM   11642 O  OG  . SER B  1 595 ? -12.263 1.606   93.822  1.00 106.17 ? 595  SER C OG  1 
ATOM   11643 N  N   . SER B  1 596 ? -12.421 3.966   92.509  1.00 106.44 ? 596  SER C N   1 
ATOM   11644 C  CA  . SER B  1 596 ? -13.438 4.984   92.260  1.00 109.04 ? 596  SER C CA  1 
ATOM   11645 C  C   . SER B  1 596 ? -12.906 6.419   92.376  1.00 114.31 ? 596  SER C C   1 
ATOM   11646 O  O   . SER B  1 596 ? -13.573 7.364   91.941  1.00 115.38 ? 596  SER C O   1 
ATOM   11647 C  CB  . SER B  1 596 ? -14.622 4.792   93.209  1.00 111.48 ? 596  SER C CB  1 
ATOM   11648 O  OG  . SER B  1 596 ? -15.707 5.629   92.840  1.00 110.91 ? 596  SER C OG  1 
ATOM   11649 N  N   . SER B  1 597 ? -11.714 6.580   92.951  1.00 110.23 ? 597  SER C N   1 
ATOM   11650 C  CA  . SER B  1 597 ? -11.096 7.900   93.100  1.00 105.09 ? 597  SER C CA  1 
ATOM   11651 C  C   . SER B  1 597 ? -10.122 8.211   91.954  1.00 105.47 ? 597  SER C C   1 
ATOM   11652 O  O   . SER B  1 597 ? -8.935  7.889   92.028  1.00 103.73 ? 597  SER C O   1 
ATOM   11653 C  CB  . SER B  1 597 ? -10.378 7.997   94.448  1.00 98.44  ? 597  SER C CB  1 
ATOM   11654 O  OG  . SER B  1 597 ? -9.671  9.217   94.562  1.00 91.65  ? 597  SER C OG  1 
ATOM   11655 N  N   . ASN B  1 598 ? -10.634 8.854   90.905  1.00 103.94 ? 598  ASN C N   1 
ATOM   11656 C  CA  . ASN B  1 598 ? -9.871  9.112   89.685  1.00 102.98 ? 598  ASN C CA  1 
ATOM   11657 C  C   . ASN B  1 598 ? -8.711  10.096  89.859  1.00 107.36 ? 598  ASN C C   1 
ATOM   11658 O  O   . ASN B  1 598 ? -7.792  10.134  89.037  1.00 108.57 ? 598  ASN C O   1 
ATOM   11659 C  CB  . ASN B  1 598 ? -10.805 9.622   88.585  1.00 98.62  ? 598  ASN C CB  1 
ATOM   11660 C  CG  . ASN B  1 598 ? -11.470 10.942  88.939  1.00 102.25 ? 598  ASN C CG  1 
ATOM   11661 O  OD1 . ASN B  1 598 ? -11.044 11.651  89.851  1.00 103.03 ? 598  ASN C OD1 1 
ATOM   11662 N  ND2 . ASN B  1 598 ? -12.522 11.281  88.206  1.00 105.02 ? 598  ASN C ND2 1 
ATOM   11663 N  N   . VAL B  1 599 ? -8.782  10.906  90.912  1.00 103.82 ? 599  VAL C N   1 
ATOM   11664 C  CA  . VAL B  1 599 ? -7.731  11.864  91.230  1.00 100.90 ? 599  VAL C CA  1 
ATOM   11665 C  C   . VAL B  1 599 ? -6.375  11.169  91.242  1.00 99.59  ? 599  VAL C C   1 
ATOM   11666 O  O   . VAL B  1 599 ? -6.209  10.108  91.844  1.00 98.87  ? 599  VAL C O   1 
ATOM   11667 C  CB  . VAL B  1 599 ? -7.991  12.553  92.591  1.00 103.99 ? 599  VAL C CB  1 
ATOM   11668 C  CG1 . VAL B  1 599 ? -6.714  13.160  93.153  1.00 105.12 ? 599  VAL C CG1 1 
ATOM   11669 C  CG2 . VAL B  1 599 ? -9.078  13.611  92.452  1.00 97.94  ? 599  VAL C CG2 1 
ATOM   11670 N  N   . ILE B  1 600 ? -5.414  11.759  90.545  1.00 96.52  ? 600  ILE C N   1 
ATOM   11671 C  CA  . ILE B  1 600 ? -4.123  11.121  90.361  1.00 100.29 ? 600  ILE C CA  1 
ATOM   11672 C  C   . ILE B  1 600 ? -3.186  11.423  91.522  1.00 97.67  ? 600  ILE C C   1 
ATOM   11673 O  O   . ILE B  1 600 ? -2.806  12.571  91.749  1.00 96.88  ? 600  ILE C O   1 
ATOM   11674 C  CB  . ILE B  1 600 ? -3.476  11.562  89.035  1.00 98.65  ? 600  ILE C CB  1 
ATOM   11675 C  CG1 . ILE B  1 600 ? -4.320  11.083  87.857  1.00 91.99  ? 600  ILE C CG1 1 
ATOM   11676 C  CG2 . ILE B  1 600 ? -2.072  11.012  88.910  1.00 93.68  ? 600  ILE C CG2 1 
ATOM   11677 C  CD1 . ILE B  1 600 ? -3.836  11.593  86.541  1.00 91.45  ? 600  ILE C CD1 1 
ATOM   11678 N  N   . HIS B  1 601 ? -2.827  10.380  92.263  1.00 96.39  ? 601  HIS C N   1 
ATOM   11679 C  CA  . HIS B  1 601 ? -1.892  10.517  93.373  1.00 98.41  ? 601  HIS C CA  1 
ATOM   11680 C  C   . HIS B  1 601 ? -0.471  10.330  92.851  1.00 87.63  ? 601  HIS C C   1 
ATOM   11681 O  O   . HIS B  1 601 ? -0.244  9.542   91.945  1.00 89.35  ? 601  HIS C O   1 
ATOM   11682 C  CB  . HIS B  1 601 ? -2.211  9.507   94.486  1.00 100.51 ? 601  HIS C CB  1 
ATOM   11683 C  CG  . HIS B  1 601 ? -3.604  9.626   95.034  1.00 105.57 ? 601  HIS C CG  1 
ATOM   11684 N  ND1 . HIS B  1 601 ? -4.364  8.530   95.387  1.00 106.98 ? 601  HIS C ND1 1 
ATOM   11685 C  CD2 . HIS B  1 601 ? -4.373  10.712  95.290  1.00 103.45 ? 601  HIS C CD2 1 
ATOM   11686 C  CE1 . HIS B  1 601 ? -5.541  8.934   95.833  1.00 105.27 ? 601  HIS C CE1 1 
ATOM   11687 N  NE2 . HIS B  1 601 ? -5.572  10.254  95.785  1.00 107.08 ? 601  HIS C NE2 1 
ATOM   11688 N  N   . ARG B  1 602 ? 0.479   11.048  93.437  1.00 81.43  ? 602  ARG C N   1 
ATOM   11689 C  CA  . ARG B  1 602 ? 1.839   11.110  92.919  1.00 76.32  ? 602  ARG C CA  1 
ATOM   11690 C  C   . ARG B  1 602 ? 2.878   10.847  94.015  1.00 77.17  ? 602  ARG C C   1 
ATOM   11691 O  O   . ARG B  1 602 ? 2.778   11.406  95.102  1.00 85.18  ? 602  ARG C O   1 
ATOM   11692 C  CB  . ARG B  1 602 ? 2.069   12.489  92.293  1.00 86.97  ? 602  ARG C CB  1 
ATOM   11693 C  CG  . ARG B  1 602 ? 2.831   12.509  90.986  1.00 88.91  ? 602  ARG C CG  1 
ATOM   11694 C  CD  . ARG B  1 602 ? 2.757   13.899  90.354  1.00 93.43  ? 602  ARG C CD  1 
ATOM   11695 N  NE  . ARG B  1 602 ? 1.377   14.301  90.081  1.00 95.19  ? 602  ARG C NE  1 
ATOM   11696 C  CZ  . ARG B  1 602 ? 0.785   14.191  88.894  1.00 90.50  ? 602  ARG C CZ  1 
ATOM   11697 N  NH1 . ARG B  1 602 ? 1.454   13.696  87.857  1.00 76.18  ? 602  ARG C NH1 1 
ATOM   11698 N  NH2 . ARG B  1 602 ? -0.476  14.580  88.746  1.00 85.36  ? 602  ARG C NH2 1 
ATOM   11699 N  N   . HIS B  1 603 ? 3.871   10.007  93.739  1.00 73.79  ? 603  HIS C N   1 
ATOM   11700 C  CA  . HIS B  1 603 ? 4.944   9.760   94.708  1.00 76.99  ? 603  HIS C CA  1 
ATOM   11701 C  C   . HIS B  1 603 ? 6.231   9.269   94.050  1.00 74.75  ? 603  HIS C C   1 
ATOM   11702 O  O   . HIS B  1 603 ? 6.210   8.421   93.162  1.00 74.93  ? 603  HIS C O   1 
ATOM   11703 C  CB  . HIS B  1 603 ? 4.493   8.741   95.771  1.00 84.56  ? 603  HIS C CB  1 
ATOM   11704 C  CG  . HIS B  1 603 ? 5.592   8.289   96.693  1.00 86.65  ? 603  HIS C CG  1 
ATOM   11705 N  ND1 . HIS B  1 603 ? 6.341   9.165   97.453  1.00 86.34  ? 603  HIS C ND1 1 
ATOM   11706 C  CD2 . HIS B  1 603 ? 6.062   7.050   96.980  1.00 84.95  ? 603  HIS C CD2 1 
ATOM   11707 C  CE1 . HIS B  1 603 ? 7.224   8.486   98.165  1.00 80.65  ? 603  HIS C CE1 1 
ATOM   11708 N  NE2 . HIS B  1 603 ? 7.076   7.201   97.896  1.00 83.21  ? 603  HIS C NE2 1 
ATOM   11709 N  N   . ILE B  1 604 ? 7.356   9.797   94.505  1.00 71.10  ? 604  ILE C N   1 
ATOM   11710 C  CA  . ILE B  1 604 ? 8.644   9.420   93.947  1.00 70.09  ? 604  ILE C CA  1 
ATOM   11711 C  C   . ILE B  1 604 ? 9.218   8.222   94.686  1.00 72.84  ? 604  ILE C C   1 
ATOM   11712 O  O   . ILE B  1 604 ? 9.501   8.319   95.879  1.00 74.30  ? 604  ILE C O   1 
ATOM   11713 C  CB  . ILE B  1 604 ? 9.655   10.584  94.029  1.00 72.21  ? 604  ILE C CB  1 
ATOM   11714 C  CG1 . ILE B  1 604 ? 8.990   11.912  93.650  1.00 75.90  ? 604  ILE C CG1 1 
ATOM   11715 C  CG2 . ILE B  1 604 ? 10.878  10.289  93.176  1.00 66.02  ? 604  ILE C CG2 1 
ATOM   11716 C  CD1 . ILE B  1 604 ? 9.520   13.109  94.423  1.00 76.50  ? 604  ILE C CD1 1 
ATOM   11717 N  N   . LEU B  1 605 ? 9.390   7.099   93.994  1.00 63.67  ? 605  LEU C N   1 
ATOM   11718 C  CA  . LEU B  1 605 ? 10.012  5.936   94.616  1.00 62.74  ? 605  LEU C CA  1 
ATOM   11719 C  C   . LEU B  1 605 ? 11.526  6.057   94.508  1.00 67.72  ? 605  LEU C C   1 
ATOM   11720 O  O   . LEU B  1 605 ? 12.087  5.875   93.434  1.00 69.57  ? 605  LEU C O   1 
ATOM   11721 C  CB  . LEU B  1 605 ? 9.522   4.642   93.968  1.00 67.28  ? 605  LEU C CB  1 
ATOM   11722 C  CG  . LEU B  1 605 ? 10.154  3.312   94.395  1.00 71.74  ? 605  LEU C CG  1 
ATOM   11723 C  CD1 . LEU B  1 605 ? 10.259  3.207   95.898  1.00 68.40  ? 605  LEU C CD1 1 
ATOM   11724 C  CD2 . LEU B  1 605 ? 9.341   2.144   93.845  1.00 73.98  ? 605  LEU C CD2 1 
ATOM   11725 N  N   . LYS B  1 606 ? 12.189  6.365   95.616  1.00 66.30  ? 606  LYS C N   1 
ATOM   11726 C  CA  . LYS B  1 606 ? 13.609  6.688   95.566  1.00 61.41  ? 606  LYS C CA  1 
ATOM   11727 C  C   . LYS B  1 606 ? 14.491  5.580   96.135  1.00 61.29  ? 606  LYS C C   1 
ATOM   11728 O  O   . LYS B  1 606 ? 15.683  5.786   96.366  1.00 62.83  ? 606  LYS C O   1 
ATOM   11729 C  CB  . LYS B  1 606 ? 13.880  8.000   96.316  1.00 64.93  ? 606  LYS C CB  1 
ATOM   11730 C  CG  . LYS B  1 606 ? 12.886  9.128   96.020  1.00 63.09  ? 606  LYS C CG  1 
ATOM   11731 C  CD  . LYS B  1 606 ? 13.439  10.483  96.457  1.00 60.62  ? 606  LYS C CD  1 
ATOM   11732 C  CE  . LYS B  1 606 ? 12.487  11.630  96.143  1.00 72.63  ? 606  LYS C CE  1 
ATOM   11733 N  NZ  . LYS B  1 606 ? 11.236  11.618  96.970  1.00 82.22  ? 606  LYS C NZ  1 
ATOM   11734 N  N   . SER B  1 607 ? 13.918  4.405   96.363  1.00 63.13  ? 607  SER C N   1 
ATOM   11735 C  CA  . SER B  1 607 ? 14.693  3.306   96.949  1.00 73.56  ? 607  SER C CA  1 
ATOM   11736 C  C   . SER B  1 607 ? 14.098  1.912   96.699  1.00 67.87  ? 607  SER C C   1 
ATOM   11737 O  O   . SER B  1 607 ? 12.950  1.776   96.267  1.00 61.08  ? 607  SER C O   1 
ATOM   11738 C  CB  . SER B  1 607 ? 14.864  3.529   98.459  1.00 69.37  ? 607  SER C CB  1 
ATOM   11739 O  OG  . SER B  1 607 ? 13.621  3.833   99.062  1.00 74.27  ? 607  SER C OG  1 
ATOM   11740 N  N   . LYS B  1 608 ? 14.904  0.891   96.993  1.00 62.52  ? 608  LYS C N   1 
ATOM   11741 C  CA  . LYS B  1 608 ? 14.602  -0.500  96.664  1.00 72.20  ? 608  LYS C CA  1 
ATOM   11742 C  C   . LYS B  1 608 ? 13.196  -0.938  97.075  1.00 75.06  ? 608  LYS C C   1 
ATOM   11743 O  O   . LYS B  1 608 ? 12.533  -1.698  96.359  1.00 68.45  ? 608  LYS C O   1 
ATOM   11744 C  CB  . LYS B  1 608 ? 15.643  -1.421  97.312  1.00 69.94  ? 608  LYS C CB  1 
ATOM   11745 C  CG  . LYS B  1 608 ? 16.841  -1.764  96.421  1.00 74.76  ? 608  LYS C CG  1 
ATOM   11746 C  CD  . LYS B  1 608 ? 16.402  -2.542  95.176  1.00 75.18  ? 608  LYS C CD  1 
ATOM   11747 C  CE  . LYS B  1 608 ? 17.502  -3.451  94.639  1.00 72.95  ? 608  LYS C CE  1 
ATOM   11748 N  NZ  . LYS B  1 608 ? 16.949  -4.426  93.658  1.00 76.53  ? 608  LYS C NZ  1 
ATOM   11749 N  N   . THR B  1 609 ? 12.751  -0.435  98.225  1.00 79.94  ? 609  THR C N   1 
ATOM   11750 C  CA  . THR B  1 609 ? 11.447  -0.768  98.791  1.00 78.72  ? 609  THR C CA  1 
ATOM   11751 C  C   . THR B  1 609 ? 10.767  0.499   99.295  1.00 67.81  ? 609  THR C C   1 
ATOM   11752 O  O   . THR B  1 609 ? 11.435  1.500   99.518  1.00 73.90  ? 609  THR C O   1 
ATOM   11753 C  CB  . THR B  1 609 ? 11.594  -1.780  99.940  1.00 76.27  ? 609  THR C CB  1 
ATOM   11754 O  OG1 . THR B  1 609 ? 12.817  -1.511  100.630 1.00 78.55  ? 609  THR C OG1 1 
ATOM   11755 C  CG2 . THR B  1 609 ? 11.653  -3.204  99.401  1.00 74.68  ? 609  THR C CG2 1 
ATOM   11756 N  N   . ASP B  1 610 ? 9.447   0.455   99.456  1.00 72.24  ? 610  ASP C N   1 
ATOM   11757 C  CA  . ASP B  1 610 ? 8.691   1.569   100.034 1.00 79.07  ? 610  ASP C CA  1 
ATOM   11758 C  C   . ASP B  1 610 ? 7.228   1.175   100.260 1.00 85.01  ? 610  ASP C C   1 
ATOM   11759 O  O   . ASP B  1 610 ? 6.756   0.182   99.703  1.00 85.74  ? 610  ASP C O   1 
ATOM   11760 C  CB  . ASP B  1 610 ? 8.766   2.803   99.133  1.00 83.07  ? 610  ASP C CB  1 
ATOM   11761 C  CG  . ASP B  1 610 ? 8.567   4.098   99.895  1.00 86.28  ? 610  ASP C CG  1 
ATOM   11762 O  OD1 . ASP B  1 610 ? 8.015   4.045   101.012 1.00 91.02  ? 610  ASP C OD1 1 
ATOM   11763 O  OD2 . ASP B  1 610 ? 8.956   5.169   99.373  1.00 86.73  ? 610  ASP C OD2 1 
ATOM   11764 N  N   . THR B  1 611 ? 6.515   1.951   101.078 1.00 87.62  ? 611  THR C N   1 
ATOM   11765 C  CA  . THR B  1 611 ? 5.102   1.683   101.362 1.00 92.22  ? 611  THR C CA  1 
ATOM   11766 C  C   . THR B  1 611 ? 4.287   2.971   101.374 1.00 88.51  ? 611  THR C C   1 
ATOM   11767 O  O   . THR B  1 611 ? 4.794   4.025   101.737 1.00 90.98  ? 611  THR C O   1 
ATOM   11768 C  CB  . THR B  1 611 ? 4.905   0.969   102.730 1.00 92.44  ? 611  THR C CB  1 
ATOM   11769 O  OG1 . THR B  1 611 ? 5.816   -0.131  102.859 1.00 86.32  ? 611  THR C OG1 1 
ATOM   11770 C  CG2 . THR B  1 611 ? 3.484   0.451   102.869 1.00 96.75  ? 611  THR C CG2 1 
ATOM   11771 N  N   . LEU B  1 612 ? 3.024   2.880   100.973 1.00 93.91  ? 612  LEU C N   1 
ATOM   11772 C  CA  . LEU B  1 612 ? 2.107   4.008   101.079 1.00 100.95 ? 612  LEU C CA  1 
ATOM   11773 C  C   . LEU B  1 612 ? 0.742   3.549   101.587 1.00 105.60 ? 612  LEU C C   1 
ATOM   11774 O  O   . LEU B  1 612 ? 0.443   2.351   101.602 1.00 102.14 ? 612  LEU C O   1 
ATOM   11775 C  CB  . LEU B  1 612 ? 1.961   4.722   99.733  1.00 105.09 ? 612  LEU C CB  1 
ATOM   11776 C  CG  . LEU B  1 612 ? 3.109   5.650   99.338  1.00 99.79  ? 612  LEU C CG  1 
ATOM   11777 C  CD1 . LEU B  1 612 ? 2.774   6.376   98.045  1.00 96.17  ? 612  LEU C CD1 1 
ATOM   11778 C  CD2 . LEU B  1 612 ? 3.403   6.637   100.460 1.00 95.43  ? 612  LEU C CD2 1 
ATOM   11779 N  N   . ASP B  1 613 ? -0.080  4.509   102.002 1.00 109.82 ? 613  ASP C N   1 
ATOM   11780 C  CA  . ASP B  1 613 ? -1.367  4.199   102.616 1.00 113.70 ? 613  ASP C CA  1 
ATOM   11781 C  C   . ASP B  1 613 ? -2.532  4.870   101.903 1.00 114.49 ? 613  ASP C C   1 
ATOM   11782 O  O   . ASP B  1 613 ? -2.646  6.099   101.898 1.00 109.58 ? 613  ASP C O   1 
ATOM   11783 C  CB  . ASP B  1 613 ? -1.366  4.614   104.089 1.00 116.31 ? 613  ASP C CB  1 
ATOM   11784 C  CG  . ASP B  1 613 ? -0.156  4.096   104.840 1.00 111.85 ? 613  ASP C CG  1 
ATOM   11785 O  OD1 . ASP B  1 613 ? -0.008  2.860   104.948 1.00 107.48 ? 613  ASP C OD1 1 
ATOM   11786 O  OD2 . ASP B  1 613 ? 0.642   4.926   105.326 1.00 113.25 ? 613  ASP C OD2 1 
ATOM   11787 N  N   . LEU B  1 614 ? -3.397  4.052   101.309 1.00 118.54 ? 614  LEU C N   1 
ATOM   11788 C  CA  . LEU B  1 614 ? -4.630  4.546   100.708 1.00 122.63 ? 614  LEU C CA  1 
ATOM   11789 C  C   . LEU B  1 614 ? -5.524  5.162   101.776 1.00 124.91 ? 614  LEU C C   1 
ATOM   11790 O  O   . LEU B  1 614 ? -5.663  4.606   102.870 1.00 125.58 ? 614  LEU C O   1 
ATOM   11791 C  CB  . LEU B  1 614 ? -5.386  3.420   99.992  1.00 120.13 ? 614  LEU C CB  1 
ATOM   11792 C  CG  . LEU B  1 614 ? -4.702  2.698   98.830  1.00 118.96 ? 614  LEU C CG  1 
ATOM   11793 C  CD1 . LEU B  1 614 ? -5.474  1.440   98.470  1.00 118.60 ? 614  LEU C CD1 1 
ATOM   11794 C  CD2 . LEU B  1 614 ? -4.576  3.617   97.622  1.00 113.74 ? 614  LEU C CD2 1 
ATOM   11795 N  N   . PRO B  1 615 ? -6.133  6.317   101.462 1.00 122.47 ? 615  PRO C N   1 
ATOM   11796 C  CA  . PRO B  1 615 ? -7.142  6.910   102.345 1.00 122.29 ? 615  PRO C CA  1 
ATOM   11797 C  C   . PRO B  1 615 ? -8.255  5.913   102.679 1.00 125.45 ? 615  PRO C C   1 
ATOM   11798 O  O   . PRO B  1 615 ? -8.742  5.877   103.811 1.00 128.13 ? 615  PRO C O   1 
ATOM   11799 C  CB  . PRO B  1 615 ? -7.680  8.092   101.524 1.00 122.21 ? 615  PRO C CB  1 
ATOM   11800 C  CG  . PRO B  1 615 ? -7.220  7.847   100.111 1.00 115.34 ? 615  PRO C CG  1 
ATOM   11801 C  CD  . PRO B  1 615 ? -5.925  7.119   100.245 1.00 118.82 ? 615  PRO C CD  1 
ATOM   11802 N  N   . GLU B  1 616 ? -8.629  5.097   101.698 1.00 124.76 ? 616  GLU C N   1 
ATOM   11803 C  CA  . GLU B  1 616 ? -9.694  4.120   101.868 1.00 121.23 ? 616  GLU C CA  1 
ATOM   11804 C  C   . GLU B  1 616 ? -9.382  2.822   101.140 1.00 121.45 ? 616  GLU C C   1 
ATOM   11805 O  O   . GLU B  1 616 ? -8.599  2.801   100.191 1.00 121.73 ? 616  GLU C O   1 
ATOM   11806 C  CB  . GLU B  1 616 ? -11.021 4.692   101.363 1.00 121.67 ? 616  GLU C CB  1 
ATOM   11807 C  CG  . GLU B  1 616 ? -10.970 5.171   99.918  1.00 119.12 ? 616  GLU C CG  1 
ATOM   11808 C  CD  . GLU B  1 616 ? -12.125 6.096   99.558  1.00 113.93 ? 616  GLU C CD  1 
ATOM   11809 O  OE1 . GLU B  1 616 ? -13.271 5.613   99.449  1.00 108.05 ? 616  GLU C OE1 1 
ATOM   11810 O  OE2 . GLU B  1 616 ? -11.882 7.306   99.379  1.00 111.94 ? 616  GLU C OE2 1 
ATOM   11811 N  N   . LYS B  1 617 ? -9.996  1.738   101.597 1.00 120.68 ? 617  LYS C N   1 
ATOM   11812 C  CA  . LYS B  1 617 ? -9.950  0.478   100.874 1.00 118.01 ? 617  LYS C CA  1 
ATOM   11813 C  C   . LYS B  1 617 ? -10.740 0.626   99.577  1.00 118.63 ? 617  LYS C C   1 
ATOM   11814 O  O   . LYS B  1 617 ? -11.789 1.274   99.551  1.00 116.48 ? 617  LYS C O   1 
ATOM   11815 C  CB  . LYS B  1 617 ? -10.510 -0.659  101.735 1.00 117.93 ? 617  LYS C CB  1 
ATOM   11816 C  CG  . LYS B  1 617 ? -10.537 -2.037  101.070 1.00 113.45 ? 617  LYS C CG  1 
ATOM   11817 C  CD  . LYS B  1 617 ? -11.836 -2.278  100.308 1.00 108.67 ? 617  LYS C CD  1 
ATOM   11818 C  CE  . LYS B  1 617 ? -12.056 -3.748  100.052 1.00 105.41 ? 617  LYS C CE  1 
ATOM   11819 N  NZ  . LYS B  1 617 ? -12.319 -4.454  101.332 1.00 101.36 ? 617  LYS C NZ  1 
ATOM   11820 N  N   . THR B  1 618 ? -10.236 0.015   98.508  1.00 118.43 ? 618  THR C N   1 
ATOM   11821 C  CA  . THR B  1 618 ? -10.886 0.069   97.202  1.00 111.86 ? 618  THR C CA  1 
ATOM   11822 C  C   . THR B  1 618 ? -10.713 -1.251  96.469  1.00 105.83 ? 618  THR C C   1 
ATOM   11823 O  O   . THR B  1 618 ? -9.905  -2.081  96.874  1.00 106.70 ? 618  THR C O   1 
ATOM   11824 C  CB  . THR B  1 618 ? -10.323 1.210   96.345  1.00 111.52 ? 618  THR C CB  1 
ATOM   11825 O  OG1 . THR B  1 618 ? -8.912  1.320   96.574  1.00 112.59 ? 618  THR C OG1 1 
ATOM   11826 C  CG2 . THR B  1 618 ? -10.990 2.532   96.709  1.00 112.87 ? 618  THR C CG2 1 
ATOM   11827 N  N   . SER B  1 619 ? -11.465 -1.443  95.390  1.00 105.49 ? 619  SER C N   1 
ATOM   11828 C  CA  . SER B  1 619 ? -11.442 -2.721  94.681  1.00 110.23 ? 619  SER C CA  1 
ATOM   11829 C  C   . SER B  1 619 ? -10.187 -2.890  93.811  1.00 111.70 ? 619  SER C C   1 
ATOM   11830 O  O   . SER B  1 619 ? -9.560  -3.948  93.846  1.00 107.38 ? 619  SER C O   1 
ATOM   11831 C  CB  . SER B  1 619 ? -12.712 -2.898  93.836  1.00 110.22 ? 619  SER C CB  1 
ATOM   11832 O  OG  . SER B  1 619 ? -12.990 -1.760  93.044  1.00 108.17 ? 619  SER C OG  1 
ATOM   11833 N  N   . TRP B  1 620 ? -9.811  -1.869  93.038  1.00 110.18 ? 620  TRP C N   1 
ATOM   11834 C  CA  . TRP B  1 620 ? -8.529  -1.912  92.323  1.00 103.32 ? 620  TRP C CA  1 
ATOM   11835 C  C   . TRP B  1 620 ? -7.764  -0.610  92.421  1.00 100.39 ? 620  TRP C C   1 
ATOM   11836 O  O   . TRP B  1 620 ? -8.326  0.432   92.762  1.00 100.10 ? 620  TRP C O   1 
ATOM   11837 C  CB  . TRP B  1 620 ? -8.715  -2.267  90.843  1.00 98.16  ? 620  TRP C CB  1 
ATOM   11838 C  CG  . TRP B  1 620 ? -9.603  -1.337  90.065  1.00 99.98  ? 620  TRP C CG  1 
ATOM   11839 C  CD1 . TRP B  1 620 ? -10.868 -1.598  89.624  1.00 98.61  ? 620  TRP C CD1 1 
ATOM   11840 C  CD2 . TRP B  1 620 ? -9.290  -0.008  89.614  1.00 101.57 ? 620  TRP C CD2 1 
ATOM   11841 N  NE1 . TRP B  1 620 ? -11.365 -0.520  88.937  1.00 97.94  ? 620  TRP C NE1 1 
ATOM   11842 C  CE2 . TRP B  1 620 ? -10.416 0.469   88.913  1.00 100.85 ? 620  TRP C CE2 1 
ATOM   11843 C  CE3 . TRP B  1 620 ? -8.168  0.822   89.729  1.00 96.37  ? 620  TRP C CE3 1 
ATOM   11844 C  CZ2 . TRP B  1 620 ? -10.455 1.739   88.343  1.00 96.59  ? 620  TRP C CZ2 1 
ATOM   11845 C  CZ3 . TRP B  1 620 ? -8.210  2.077   89.170  1.00 92.45  ? 620  TRP C CZ3 1 
ATOM   11846 C  CH2 . TRP B  1 620 ? -9.345  2.526   88.483  1.00 96.02  ? 620  TRP C CH2 1 
ATOM   11847 N  N   . VAL B  1 621 ? -6.475  -0.679  92.104  1.00 98.46  ? 621  VAL C N   1 
ATOM   11848 C  CA  . VAL B  1 621 ? -5.639  0.511   91.993  1.00 100.76 ? 621  VAL C CA  1 
ATOM   11849 C  C   . VAL B  1 621 ? -4.697  0.367   90.802  1.00 97.58  ? 621  VAL C C   1 
ATOM   11850 O  O   . VAL B  1 621 ? -3.866  -0.545  90.769  1.00 92.94  ? 621  VAL C O   1 
ATOM   11851 C  CB  . VAL B  1 621 ? -4.818  0.767   93.275  1.00 100.84 ? 621  VAL C CB  1 
ATOM   11852 C  CG1 . VAL B  1 621 ? -3.721  1.788   93.011  1.00 102.13 ? 621  VAL C CG1 1 
ATOM   11853 C  CG2 . VAL B  1 621 ? -5.719  1.249   94.396  1.00 105.17 ? 621  VAL C CG2 1 
ATOM   11854 N  N   . LYS B  1 622 ? -4.835  1.261   89.825  1.00 97.22  ? 622  LYS C N   1 
ATOM   11855 C  CA  . LYS B  1 622 ? -3.982  1.239   88.634  1.00 92.96  ? 622  LYS C CA  1 
ATOM   11856 C  C   . LYS B  1 622 ? -2.812  2.213   88.752  1.00 89.55  ? 622  LYS C C   1 
ATOM   11857 O  O   . LYS B  1 622 ? -3.007  3.417   88.937  1.00 88.81  ? 622  LYS C O   1 
ATOM   11858 C  CB  . LYS B  1 622 ? -4.796  1.561   87.378  1.00 90.86  ? 622  LYS C CB  1 
ATOM   11859 C  CG  . LYS B  1 622 ? -3.953  1.710   86.126  1.00 87.71  ? 622  LYS C CG  1 
ATOM   11860 C  CD  . LYS B  1 622 ? -3.226  0.420   85.801  1.00 89.01  ? 622  LYS C CD  1 
ATOM   11861 C  CE  . LYS B  1 622 ? -2.180  0.628   84.715  1.00 89.19  ? 622  LYS C CE  1 
ATOM   11862 N  NZ  . LYS B  1 622 ? -2.474  1.825   83.867  1.00 90.18  ? 622  LYS C NZ  1 
ATOM   11863 N  N   . PHE B  1 623 ? -1.598  1.678   88.649  1.00 87.68  ? 623  PHE C N   1 
ATOM   11864 C  CA  . PHE B  1 623 ? -0.378  2.483   88.696  1.00 86.41  ? 623  PHE C CA  1 
ATOM   11865 C  C   . PHE B  1 623 ? 0.039   2.938   87.303  1.00 86.44  ? 623  PHE C C   1 
ATOM   11866 O  O   . PHE B  1 623 ? -0.362  2.335   86.312  1.00 87.23  ? 623  PHE C O   1 
ATOM   11867 C  CB  . PHE B  1 623 ? 0.759   1.694   89.341  1.00 92.72  ? 623  PHE C CB  1 
ATOM   11868 C  CG  . PHE B  1 623 ? 0.898   1.926   90.812  1.00 92.06  ? 623  PHE C CG  1 
ATOM   11869 C  CD1 . PHE B  1 623 ? 0.186   1.155   91.720  1.00 94.59  ? 623  PHE C CD1 1 
ATOM   11870 C  CD2 . PHE B  1 623 ? 1.740   2.915   91.289  1.00 87.76  ? 623  PHE C CD2 1 
ATOM   11871 C  CE1 . PHE B  1 623 ? 0.313   1.370   93.079  1.00 92.65  ? 623  PHE C CE1 1 
ATOM   11872 C  CE2 . PHE B  1 623 ? 1.872   3.133   92.642  1.00 91.06  ? 623  PHE C CE2 1 
ATOM   11873 C  CZ  . PHE B  1 623 ? 1.156   2.364   93.540  1.00 93.48  ? 623  PHE C CZ  1 
ATOM   11874 N  N   . ASN B  1 624 ? 0.848   3.996   87.238  1.00 85.06  ? 624  ASN C N   1 
ATOM   11875 C  CA  . ASN B  1 624 ? 1.257   4.589   85.963  1.00 82.14  ? 624  ASN C CA  1 
ATOM   11876 C  C   . ASN B  1 624 ? 0.052   5.061   85.148  1.00 81.80  ? 624  ASN C C   1 
ATOM   11877 O  O   . ASN B  1 624 ? -0.377  4.394   84.198  1.00 78.07  ? 624  ASN C O   1 
ATOM   11878 C  CB  . ASN B  1 624 ? 2.084   3.591   85.148  1.00 79.91  ? 624  ASN C CB  1 
ATOM   11879 C  CG  . ASN B  1 624 ? 3.108   4.266   84.270  1.00 75.22  ? 624  ASN C CG  1 
ATOM   11880 O  OD1 . ASN B  1 624 ? 3.271   5.485   84.328  1.00 78.11  ? 624  ASN C OD1 1 
ATOM   11881 N  ND2 . ASN B  1 624 ? 3.822   3.478   83.464  1.00 68.72  ? 624  ASN C ND2 1 
ATOM   11882 N  N   . VAL B  1 625 ? -0.494  6.211   85.531  1.00 76.08  ? 625  VAL C N   1 
ATOM   11883 C  CA  . VAL B  1 625 ? -1.696  6.732   84.893  1.00 83.22  ? 625  VAL C CA  1 
ATOM   11884 C  C   . VAL B  1 625 ? -1.426  7.208   83.474  1.00 79.99  ? 625  VAL C C   1 
ATOM   11885 O  O   . VAL B  1 625 ? -0.542  8.034   83.260  1.00 74.83  ? 625  VAL C O   1 
ATOM   11886 C  CB  . VAL B  1 625 ? -2.290  7.906   85.681  1.00 85.71  ? 625  VAL C CB  1 
ATOM   11887 C  CG1 . VAL B  1 625 ? -3.702  8.212   85.179  1.00 84.69  ? 625  VAL C CG1 1 
ATOM   11888 C  CG2 . VAL B  1 625 ? -2.282  7.606   87.175  1.00 83.45  ? 625  VAL C CG2 1 
ATOM   11889 N  N   . ASP B  1 626 ? -2.202  6.687   82.523  1.00 82.02  ? 626  ASP C N   1 
ATOM   11890 C  CA  . ASP B  1 626 ? -2.084  7.001   81.089  1.00 80.84  ? 626  ASP C CA  1 
ATOM   11891 C  C   . ASP B  1 626 ? -0.765  6.516   80.468  1.00 73.85  ? 626  ASP C C   1 
ATOM   11892 O  O   . ASP B  1 626 ? -0.530  6.721   79.280  1.00 72.82  ? 626  ASP C O   1 
ATOM   11893 C  CB  . ASP B  1 626 ? -2.250  8.508   80.846  1.00 83.50  ? 626  ASP C CB  1 
ATOM   11894 C  CG  . ASP B  1 626 ? -3.710  8.939   80.764  1.00 88.00  ? 626  ASP C CG  1 
ATOM   11895 O  OD1 . ASP B  1 626 ? -4.578  8.077   80.505  1.00 86.40  ? 626  ASP C OD1 1 
ATOM   11896 O  OD2 . ASP B  1 626 ? -3.988  10.148  80.939  1.00 91.38  ? 626  ASP C OD2 1 
ATOM   11897 N  N   . SER B  1 627 ? 0.069   5.883   81.295  1.00 74.99  ? 627  SER C N   1 
ATOM   11898 C  CA  . SER B  1 627 ? 1.351   5.275   80.922  1.00 71.95  ? 627  SER C CA  1 
ATOM   11899 C  C   . SER B  1 627 ? 2.474   6.298   80.661  1.00 69.76  ? 627  SER C C   1 
ATOM   11900 O  O   . SER B  1 627 ? 3.424   6.011   79.929  1.00 70.77  ? 627  SER C O   1 
ATOM   11901 C  CB  . SER B  1 627 ? 1.172   4.360   79.703  1.00 73.00  ? 627  SER C CB  1 
ATOM   11902 O  OG  . SER B  1 627 ? 0.051   3.503   79.873  1.00 72.69  ? 627  SER C OG  1 
ATOM   11903 N  N   . ASN B  1 628 ? 2.388   7.462   81.301  1.00 61.00  ? 628  ASN C N   1 
ATOM   11904 C  CA  . ASN B  1 628 ? 3.361   8.536   81.093  1.00 66.61  ? 628  ASN C CA  1 
ATOM   11905 C  C   . ASN B  1 628 ? 4.718   8.262   81.706  1.00 58.24  ? 628  ASN C C   1 
ATOM   11906 O  O   . ASN B  1 628 ? 5.641   9.069   81.598  1.00 57.56  ? 628  ASN C O   1 
ATOM   11907 C  CB  . ASN B  1 628 ? 2.843   9.856   81.663  1.00 62.87  ? 628  ASN C CB  1 
ATOM   11908 C  CG  . ASN B  1 628 ? 1.537   10.274  81.054  1.00 70.39  ? 628  ASN C CG  1 
ATOM   11909 O  OD1 . ASN B  1 628 ? 1.254   9.979   79.889  1.00 70.59  ? 628  ASN C OD1 1 
ATOM   11910 N  ND2 . ASN B  1 628 ? 0.723   10.976  81.839  1.00 77.61  ? 628  ASN C ND2 1 
ATOM   11911 N  N   . GLY B  1 629 ? 4.838   7.137   82.378  1.00 52.67  ? 629  GLY C N   1 
ATOM   11912 C  CA  . GLY B  1 629 ? 6.075   6.842   83.057  1.00 55.88  ? 629  GLY C CA  1 
ATOM   11913 C  C   . GLY B  1 629 ? 6.762   5.686   82.389  1.00 60.39  ? 629  GLY C C   1 
ATOM   11914 O  O   . GLY B  1 629 ? 6.123   4.737   81.931  1.00 60.15  ? 629  GLY C O   1 
ATOM   11915 N  N   . TYR B  1 630 ? 8.082   5.770   82.335  1.00 61.30  ? 630  TYR C N   1 
ATOM   11916 C  CA  . TYR B  1 630 ? 8.860   4.720   81.712  1.00 64.12  ? 630  TYR C CA  1 
ATOM   11917 C  C   . TYR B  1 630 ? 9.150   3.615   82.716  1.00 60.56  ? 630  TYR C C   1 
ATOM   11918 O  O   . TYR B  1 630 ? 10.296  3.430   83.137  1.00 59.36  ? 630  TYR C O   1 
ATOM   11919 C  CB  . TYR B  1 630 ? 10.157  5.285   81.130  1.00 59.51  ? 630  TYR C CB  1 
ATOM   11920 C  CG  . TYR B  1 630 ? 10.797  4.378   80.104  1.00 56.99  ? 630  TYR C CG  1 
ATOM   11921 C  CD1 . TYR B  1 630 ? 10.230  4.204   78.839  1.00 51.49  ? 630  TYR C CD1 1 
ATOM   11922 C  CD2 . TYR B  1 630 ? 11.969  3.694   80.397  1.00 56.87  ? 630  TYR C CD2 1 
ATOM   11923 C  CE1 . TYR B  1 630 ? 10.811  3.371   77.912  1.00 51.50  ? 630  TYR C CE1 1 
ATOM   11924 C  CE2 . TYR B  1 630 ? 12.554  2.865   79.475  1.00 54.63  ? 630  TYR C CE2 1 
ATOM   11925 C  CZ  . TYR B  1 630 ? 11.978  2.704   78.238  1.00 52.97  ? 630  TYR C CZ  1 
ATOM   11926 O  OH  . TYR B  1 630 ? 12.587  1.865   77.341  1.00 53.69  ? 630  TYR C OH  1 
ATOM   11927 N  N   . TYR B  1 631 ? 8.097   2.894   83.101  1.00 63.31  ? 631  TYR C N   1 
ATOM   11928 C  CA  . TYR B  1 631 ? 8.228   1.699   83.945  1.00 65.68  ? 631  TYR C CA  1 
ATOM   11929 C  C   . TYR B  1 631 ? 7.030   0.774   83.767  1.00 65.31  ? 631  TYR C C   1 
ATOM   11930 O  O   . TYR B  1 631 ? 5.940   1.209   83.396  1.00 71.03  ? 631  TYR C O   1 
ATOM   11931 C  CB  . TYR B  1 631 ? 8.387   2.077   85.426  1.00 65.50  ? 631  TYR C CB  1 
ATOM   11932 C  CG  . TYR B  1 631 ? 7.292   2.971   85.969  1.00 61.87  ? 631  TYR C CG  1 
ATOM   11933 C  CD1 . TYR B  1 631 ? 7.391   4.359   85.883  1.00 64.82  ? 631  TYR C CD1 1 
ATOM   11934 C  CD2 . TYR B  1 631 ? 6.160   2.435   86.559  1.00 65.10  ? 631  TYR C CD2 1 
ATOM   11935 C  CE1 . TYR B  1 631 ? 6.392   5.190   86.379  1.00 64.69  ? 631  TYR C CE1 1 
ATOM   11936 C  CE2 . TYR B  1 631 ? 5.151   3.257   87.053  1.00 70.88  ? 631  TYR C CE2 1 
ATOM   11937 C  CZ  . TYR B  1 631 ? 5.273   4.633   86.961  1.00 70.75  ? 631  TYR C CZ  1 
ATOM   11938 O  OH  . TYR B  1 631 ? 4.273   5.445   87.451  1.00 75.11  ? 631  TYR C OH  1 
ATOM   11939 N  N   . ILE B  1 632 ? 7.238   -0.506  84.040  1.00 68.10  ? 632  ILE C N   1 
ATOM   11940 C  CA  . ILE B  1 632 ? 6.164   -1.494  83.973  1.00 75.60  ? 632  ILE C CA  1 
ATOM   11941 C  C   . ILE B  1 632 ? 5.529   -1.703  85.362  1.00 74.53  ? 632  ILE C C   1 
ATOM   11942 O  O   . ILE B  1 632 ? 6.176   -1.462  86.382  1.00 73.78  ? 632  ILE C O   1 
ATOM   11943 C  CB  . ILE B  1 632 ? 6.705   -2.824  83.415  1.00 70.01  ? 632  ILE C CB  1 
ATOM   11944 C  CG1 . ILE B  1 632 ? 7.720   -2.530  82.306  1.00 65.82  ? 632  ILE C CG1 1 
ATOM   11945 C  CG2 . ILE B  1 632 ? 5.570   -3.729  82.952  1.00 74.50  ? 632  ILE C CG2 1 
ATOM   11946 C  CD1 . ILE B  1 632 ? 7.754   -3.540  81.177  1.00 68.63  ? 632  ILE C CD1 1 
ATOM   11947 N  N   . VAL B  1 633 ? 4.267   -2.127  85.407  1.00 73.64  ? 633  VAL C N   1 
ATOM   11948 C  CA  . VAL B  1 633 ? 3.610   -2.407  86.689  1.00 79.65  ? 633  VAL C CA  1 
ATOM   11949 C  C   . VAL B  1 633 ? 3.237   -3.880  86.846  1.00 75.63  ? 633  VAL C C   1 
ATOM   11950 O  O   . VAL B  1 633 ? 2.625   -4.472  85.961  1.00 76.36  ? 633  VAL C O   1 
ATOM   11951 C  CB  . VAL B  1 633 ? 2.329   -1.548  86.889  1.00 78.93  ? 633  VAL C CB  1 
ATOM   11952 C  CG1 . VAL B  1 633 ? 2.698   -0.088  87.025  1.00 78.81  ? 633  VAL C CG1 1 
ATOM   11953 C  CG2 . VAL B  1 633 ? 1.308   -1.765  85.752  1.00 74.18  ? 633  VAL C CG2 1 
ATOM   11954 N  N   . HIS B  1 634 ? 3.617   -4.468  87.978  1.00 79.52  ? 634  HIS C N   1 
ATOM   11955 C  CA  . HIS B  1 634 ? 3.204   -5.836  88.317  1.00 85.12  ? 634  HIS C CA  1 
ATOM   11956 C  C   . HIS B  1 634 ? 2.466   -5.912  89.657  1.00 86.11  ? 634  HIS C C   1 
ATOM   11957 O  O   . HIS B  1 634 ? 3.028   -5.586  90.706  1.00 81.98  ? 634  HIS C O   1 
ATOM   11958 C  CB  . HIS B  1 634 ? 4.410   -6.771  88.360  1.00 78.48  ? 634  HIS C CB  1 
ATOM   11959 C  CG  . HIS B  1 634 ? 4.057   -8.189  88.682  1.00 82.21  ? 634  HIS C CG  1 
ATOM   11960 N  ND1 . HIS B  1 634 ? 2.786   -8.694  88.513  1.00 83.23  ? 634  HIS C ND1 1 
ATOM   11961 C  CD2 . HIS B  1 634 ? 4.807   -9.209  89.165  1.00 83.32  ? 634  HIS C CD2 1 
ATOM   11962 C  CE1 . HIS B  1 634 ? 2.768   -9.965  88.875  1.00 84.46  ? 634  HIS C CE1 1 
ATOM   11963 N  NE2 . HIS B  1 634 ? 3.981   -10.302 89.274  1.00 84.28  ? 634  HIS C NE2 1 
ATOM   11964 N  N   . TYR B  1 635 ? 1.217   -6.366  89.620  1.00 88.45  ? 635  TYR C N   1 
ATOM   11965 C  CA  . TYR B  1 635 ? 0.405   -6.465  90.834  1.00 88.97  ? 635  TYR C CA  1 
ATOM   11966 C  C   . TYR B  1 635 ? 0.460   -7.877  91.418  1.00 91.66  ? 635  TYR C C   1 
ATOM   11967 O  O   . TYR B  1 635 ? -0.027  -8.835  90.812  1.00 96.41  ? 635  TYR C O   1 
ATOM   11968 C  CB  . TYR B  1 635 ? -1.040  -6.058  90.543  1.00 83.30  ? 635  TYR C CB  1 
ATOM   11969 C  CG  . TYR B  1 635 ? -1.137  -4.727  89.845  1.00 85.81  ? 635  TYR C CG  1 
ATOM   11970 C  CD1 . TYR B  1 635 ? -1.051  -4.640  88.462  1.00 88.37  ? 635  TYR C CD1 1 
ATOM   11971 C  CD2 . TYR B  1 635 ? -1.293  -3.552  90.565  1.00 84.23  ? 635  TYR C CD2 1 
ATOM   11972 C  CE1 . TYR B  1 635 ? -1.121  -3.414  87.809  1.00 89.63  ? 635  TYR C CE1 1 
ATOM   11973 C  CE2 . TYR B  1 635 ? -1.375  -2.320  89.924  1.00 89.78  ? 635  TYR C CE2 1 
ATOM   11974 C  CZ  . TYR B  1 635 ? -1.290  -2.258  88.543  1.00 89.36  ? 635  TYR C CZ  1 
ATOM   11975 O  OH  . TYR B  1 635 ? -1.365  -1.045  87.895  1.00 85.77  ? 635  TYR C OH  1 
ATOM   11976 N  N   . GLU B  1 636 ? 1.065   -8.001  92.595  1.00 93.00  ? 636  GLU C N   1 
ATOM   11977 C  CA  . GLU B  1 636 ? 1.203   -9.298  93.245  1.00 96.41  ? 636  GLU C CA  1 
ATOM   11978 C  C   . GLU B  1 636 ? -0.132  -9.794  93.778  1.00 92.82  ? 636  GLU C C   1 
ATOM   11979 O  O   . GLU B  1 636 ? -1.045  -9.004  94.042  1.00 81.43  ? 636  GLU C O   1 
ATOM   11980 C  CB  . GLU B  1 636 ? 2.227   -9.229  94.380  1.00 97.50  ? 636  GLU C CB  1 
ATOM   11981 C  CG  . GLU B  1 636 ? 3.646   -9.565  93.949  1.00 93.47  ? 636  GLU C CG  1 
ATOM   11982 C  CD  . GLU B  1 636 ? 4.649   -9.404  95.074  1.00 95.87  ? 636  GLU C CD  1 
ATOM   11983 O  OE1 . GLU B  1 636 ? 4.392   -8.606  95.998  1.00 95.76  ? 636  GLU C OE1 1 
ATOM   11984 O  OE2 . GLU B  1 636 ? 5.702   -10.070 95.030  1.00 97.90  ? 636  GLU C OE2 1 
ATOM   11985 N  N   . GLY B  1 637 ? -0.227  -11.111 93.928  1.00 95.52  ? 637  GLY C N   1 
ATOM   11986 C  CA  . GLY B  1 637 ? -1.441  -11.743 94.397  1.00 98.43  ? 637  GLY C CA  1 
ATOM   11987 C  C   . GLY B  1 637 ? -2.648  -11.412 93.542  1.00 99.42  ? 637  GLY C C   1 
ATOM   11988 O  O   . GLY B  1 637 ? -2.656  -11.652 92.334  1.00 93.57  ? 637  GLY C O   1 
ATOM   11989 N  N   . HIS B  1 638 ? -3.660  -10.830 94.179  1.00 102.33 ? 638  HIS C N   1 
ATOM   11990 C  CA  . HIS B  1 638 ? -4.978  -10.662 93.572  1.00 105.31 ? 638  HIS C CA  1 
ATOM   11991 C  C   . HIS B  1 638 ? -5.170  -9.285  92.948  1.00 105.31 ? 638  HIS C C   1 
ATOM   11992 O  O   . HIS B  1 638 ? -6.275  -8.739  92.956  1.00 106.62 ? 638  HIS C O   1 
ATOM   11993 C  CB  . HIS B  1 638 ? -6.071  -10.914 94.619  1.00 110.07 ? 638  HIS C CB  1 
ATOM   11994 C  CG  . HIS B  1 638 ? -5.914  -12.210 95.355  1.00 115.19 ? 638  HIS C CG  1 
ATOM   11995 N  ND1 . HIS B  1 638 ? -6.342  -13.416 94.841  1.00 113.37 ? 638  HIS C ND1 1 
ATOM   11996 C  CD2 . HIS B  1 638 ? -5.365  -12.489 96.562  1.00 114.83 ? 638  HIS C CD2 1 
ATOM   11997 C  CE1 . HIS B  1 638 ? -6.067  -14.381 95.701  1.00 114.60 ? 638  HIS C CE1 1 
ATOM   11998 N  NE2 . HIS B  1 638 ? -5.474  -13.846 96.753  1.00 115.04 ? 638  HIS C NE2 1 
ATOM   11999 N  N   . GLY B  1 639 ? -4.096  -8.726  92.406  1.00 98.94  ? 639  GLY C N   1 
ATOM   12000 C  CA  . GLY B  1 639 ? -4.167  -7.411  91.800  1.00 94.81  ? 639  GLY C CA  1 
ATOM   12001 C  C   . GLY B  1 639 ? -4.655  -7.443  90.364  1.00 98.23  ? 639  GLY C C   1 
ATOM   12002 O  O   . GLY B  1 639 ? -5.518  -6.651  89.978  1.00 93.75  ? 639  GLY C O   1 
ATOM   12003 N  N   . TRP B  1 640 ? -4.104  -8.362  89.573  1.00 98.07  ? 640  TRP C N   1 
ATOM   12004 C  CA  . TRP B  1 640 ? -4.415  -8.429  88.148  1.00 90.55  ? 640  TRP C CA  1 
ATOM   12005 C  C   . TRP B  1 640 ? -5.855  -8.837  87.891  1.00 93.04  ? 640  TRP C C   1 
ATOM   12006 O  O   . TRP B  1 640 ? -6.523  -8.243  87.048  1.00 90.43  ? 640  TRP C O   1 
ATOM   12007 C  CB  . TRP B  1 640 ? -3.467  -9.394  87.437  1.00 89.38  ? 640  TRP C CB  1 
ATOM   12008 C  CG  . TRP B  1 640 ? -2.098  -8.820  87.218  1.00 91.95  ? 640  TRP C CG  1 
ATOM   12009 C  CD1 . TRP B  1 640 ? -0.940  -9.182  87.849  1.00 91.45  ? 640  TRP C CD1 1 
ATOM   12010 C  CD2 . TRP B  1 640 ? -1.746  -7.776  86.307  1.00 85.69  ? 640  TRP C CD2 1 
ATOM   12011 N  NE1 . TRP B  1 640 ? 0.112   -8.425  87.384  1.00 81.29  ? 640  TRP C NE1 1 
ATOM   12012 C  CE2 . TRP B  1 640 ? -0.359  -7.554  86.438  1.00 86.19  ? 640  TRP C CE2 1 
ATOM   12013 C  CE3 . TRP B  1 640 ? -2.470  -7.000  85.397  1.00 83.24  ? 640  TRP C CE3 1 
ATOM   12014 C  CZ2 . TRP B  1 640 ? 0.315   -6.596  85.688  1.00 87.49  ? 640  TRP C CZ2 1 
ATOM   12015 C  CZ3 . TRP B  1 640 ? -1.799  -6.046  84.657  1.00 81.03  ? 640  TRP C CZ3 1 
ATOM   12016 C  CH2 . TRP B  1 640 ? -0.421  -5.853  84.804  1.00 83.83  ? 640  TRP C CH2 1 
ATOM   12017 N  N   . ASP B  1 641 ? -6.328  -9.841  88.629  1.00 95.99  ? 641  ASP C N   1 
ATOM   12018 C  CA  . ASP B  1 641 ? -7.675  -10.380 88.442  1.00 94.47  ? 641  ASP C CA  1 
ATOM   12019 C  C   . ASP B  1 641 ? -8.741  -9.306  88.617  1.00 94.29  ? 641  ASP C C   1 
ATOM   12020 O  O   . ASP B  1 641 ? -9.773  -9.328  87.952  1.00 92.91  ? 641  ASP C O   1 
ATOM   12021 C  CB  . ASP B  1 641 ? -7.943  -11.530 89.418  1.00 93.47  ? 641  ASP C CB  1 
ATOM   12022 C  CG  . ASP B  1 641 ? -6.884  -12.614 89.358  1.00 95.15  ? 641  ASP C CG  1 
ATOM   12023 O  OD1 . ASP B  1 641 ? -6.942  -13.463 88.438  1.00 101.50 ? 641  ASP C OD1 1 
ATOM   12024 O  OD2 . ASP B  1 641 ? -5.999  -12.622 90.241  1.00 93.57  ? 641  ASP C OD2 1 
ATOM   12025 N  N   . GLN B  1 642 ? -8.486  -8.365  89.518  1.00 95.18  ? 642  GLN C N   1 
ATOM   12026 C  CA  . GLN B  1 642 ? -9.427  -7.279  89.761  1.00 101.42 ? 642  GLN C CA  1 
ATOM   12027 C  C   . GLN B  1 642 ? -9.340  -6.240  88.661  1.00 103.15 ? 642  GLN C C   1 
ATOM   12028 O  O   . GLN B  1 642 ? -10.336 -5.599  88.315  1.00 105.72 ? 642  GLN C O   1 
ATOM   12029 C  CB  . GLN B  1 642 ? -9.168  -6.625  91.118  1.00 104.28 ? 642  GLN C CB  1 
ATOM   12030 C  CG  . GLN B  1 642 ? -9.877  -7.295  92.275  1.00 106.05 ? 642  GLN C CG  1 
ATOM   12031 C  CD  . GLN B  1 642 ? -9.402  -6.767  93.602  1.00 113.37 ? 642  GLN C CD  1 
ATOM   12032 O  OE1 . GLN B  1 642 ? -8.221  -6.457  93.769  1.00 113.95 ? 642  GLN C OE1 1 
ATOM   12033 N  NE2 . GLN B  1 642 ? -10.323 -6.628  94.552  1.00 111.19 ? 642  GLN C NE2 1 
ATOM   12034 N  N   . LEU B  1 643 ? -8.141  -6.064  88.118  1.00 102.31 ? 643  LEU C N   1 
ATOM   12035 C  CA  . LEU B  1 643 ? -7.958  -5.143  87.007  1.00 100.86 ? 643  LEU C CA  1 
ATOM   12036 C  C   . LEU B  1 643 ? -8.586  -5.730  85.749  1.00 100.19 ? 643  LEU C C   1 
ATOM   12037 O  O   . LEU B  1 643 ? -9.269  -5.022  85.005  1.00 102.71 ? 643  LEU C O   1 
ATOM   12038 C  CB  . LEU B  1 643 ? -6.478  -4.838  86.793  1.00 91.87  ? 643  LEU C CB  1 
ATOM   12039 C  CG  . LEU B  1 643 ? -5.929  -3.833  87.798  1.00 86.97  ? 643  LEU C CG  1 
ATOM   12040 C  CD1 . LEU B  1 643 ? -4.426  -3.893  87.811  1.00 76.84  ? 643  LEU C CD1 1 
ATOM   12041 C  CD2 . LEU B  1 643 ? -6.417  -2.432  87.457  1.00 90.63  ? 643  LEU C CD2 1 
ATOM   12042 N  N   . ILE B  1 644 ? -8.370  -7.024  85.526  1.00 90.92  ? 644  ILE C N   1 
ATOM   12043 C  CA  . ILE B  1 644 ? -8.995  -7.703  84.403  1.00 92.32  ? 644  ILE C CA  1 
ATOM   12044 C  C   . ILE B  1 644 ? -10.500 -7.579  84.530  1.00 97.51  ? 644  ILE C C   1 
ATOM   12045 O  O   . ILE B  1 644 ? -11.151 -6.959  83.689  1.00 95.96  ? 644  ILE C O   1 
ATOM   12046 C  CB  . ILE B  1 644 ? -8.613  -9.193  84.329  1.00 89.80  ? 644  ILE C CB  1 
ATOM   12047 C  CG1 . ILE B  1 644 ? -7.099  -9.359  84.167  1.00 90.84  ? 644  ILE C CG1 1 
ATOM   12048 C  CG2 . ILE B  1 644 ? -9.358  -9.863  83.187  1.00 81.55  ? 644  ILE C CG2 1 
ATOM   12049 C  CD1 . ILE B  1 644 ? -6.595  -10.775 84.401  1.00 92.22  ? 644  ILE C CD1 1 
ATOM   12050 N  N   . THR B  1 645 ? -11.033 -8.132  85.620  1.00 100.91 ? 645  THR C N   1 
ATOM   12051 C  CA  . THR B  1 645 ? -12.474 -8.238  85.832  1.00 101.86 ? 645  THR C CA  1 
ATOM   12052 C  C   . THR B  1 645 ? -13.171 -6.887  85.746  1.00 102.93 ? 645  THR C C   1 
ATOM   12053 O  O   . THR B  1 645 ? -14.349 -6.813  85.390  1.00 105.43 ? 645  THR C O   1 
ATOM   12054 C  CB  . THR B  1 645 ? -12.796 -8.877  87.194  1.00 101.49 ? 645  THR C CB  1 
ATOM   12055 O  OG1 . THR B  1 645 ? -11.820 -9.880  87.492  1.00 96.58  ? 645  THR C OG1 1 
ATOM   12056 C  CG2 . THR B  1 645 ? -14.185 -9.510  87.175  1.00 103.16 ? 645  THR C CG2 1 
ATOM   12057 N  N   . GLN B  1 646 ? -12.440 -5.822  86.063  1.00 103.83 ? 646  GLN C N   1 
ATOM   12058 C  CA  . GLN B  1 646 ? -12.983 -4.473  85.959  1.00 102.90 ? 646  GLN C CA  1 
ATOM   12059 C  C   . GLN B  1 646 ? -13.242 -4.111  84.501  1.00 101.42 ? 646  GLN C C   1 
ATOM   12060 O  O   . GLN B  1 646 ? -14.189 -3.383  84.191  1.00 93.26  ? 646  GLN C O   1 
ATOM   12061 C  CB  . GLN B  1 646 ? -12.043 -3.453  86.604  1.00 98.07  ? 646  GLN C CB  1 
ATOM   12062 C  CG  . GLN B  1 646 ? -12.316 -2.006  86.208  1.00 101.89 ? 646  GLN C CG  1 
ATOM   12063 C  CD  . GLN B  1 646 ? -13.648 -1.472  86.713  1.00 98.54  ? 646  GLN C CD  1 
ATOM   12064 O  OE1 . GLN B  1 646 ? -13.681 -0.636  87.611  1.00 97.04  ? 646  GLN C OE1 1 
ATOM   12065 N  NE2 . GLN B  1 646 ? -14.748 -1.930  86.119  1.00 95.47  ? 646  GLN C NE2 1 
ATOM   12066 N  N   . LEU B  1 647 ? -12.406 -4.640  83.611  1.00 100.99 ? 647  LEU C N   1 
ATOM   12067 C  CA  . LEU B  1 647 ? -12.549 -4.389  82.183  1.00 101.83 ? 647  LEU C CA  1 
ATOM   12068 C  C   . LEU B  1 647 ? -13.580 -5.310  81.548  1.00 101.06 ? 647  LEU C C   1 
ATOM   12069 O  O   . LEU B  1 647 ? -14.363 -4.875  80.706  1.00 102.31 ? 647  LEU C O   1 
ATOM   12070 C  CB  . LEU B  1 647 ? -11.205 -4.550  81.465  1.00 105.61 ? 647  LEU C CB  1 
ATOM   12071 C  CG  . LEU B  1 647 ? -10.130 -3.473  81.665  1.00 104.87 ? 647  LEU C CG  1 
ATOM   12072 C  CD1 . LEU B  1 647 ? -8.781  -3.981  81.176  1.00 97.84  ? 647  LEU C CD1 1 
ATOM   12073 C  CD2 . LEU B  1 647 ? -10.490 -2.157  80.969  1.00 99.37  ? 647  LEU C CD2 1 
ATOM   12074 N  N   . ASN B  1 648 ? -13.574 -6.580  81.948  1.00 101.23 ? 648  ASN C N   1 
ATOM   12075 C  CA  . ASN B  1 648 ? -14.496 -7.573  81.389  1.00 105.56 ? 648  ASN C CA  1 
ATOM   12076 C  C   . ASN B  1 648 ? -15.955 -7.143  81.542  1.00 105.51 ? 648  ASN C C   1 
ATOM   12077 O  O   . ASN B  1 648 ? -16.798 -7.440  80.693  1.00 100.17 ? 648  ASN C O   1 
ATOM   12078 C  CB  . ASN B  1 648 ? -14.282 -8.939  82.053  1.00 101.48 ? 648  ASN C CB  1 
ATOM   12079 C  CG  . ASN B  1 648 ? -12.845 -9.415  81.967  1.00 96.42  ? 648  ASN C CG  1 
ATOM   12080 O  OD1 . ASN B  1 648 ? -11.938 -8.625  81.728  1.00 98.03  ? 648  ASN C OD1 1 
ATOM   12081 N  ND2 . ASN B  1 648 ? -12.630 -10.709 82.168  1.00 96.88  ? 648  ASN C ND2 1 
ATOM   12082 N  N   . GLN B  1 649 ? -16.233 -6.440  82.636  1.00 105.76 ? 649  GLN C N   1 
ATOM   12083 C  CA  . GLN B  1 649 ? -17.544 -5.851  82.882  1.00 106.88 ? 649  GLN C CA  1 
ATOM   12084 C  C   . GLN B  1 649 ? -17.648 -4.489  82.203  1.00 108.31 ? 649  GLN C C   1 
ATOM   12085 O  O   . GLN B  1 649 ? -18.009 -4.399  81.028  1.00 110.78 ? 649  GLN C O   1 
ATOM   12086 C  CB  . GLN B  1 649 ? -17.797 -5.708  84.386  1.00 112.43 ? 649  GLN C CB  1 
ATOM   12087 C  CG  . GLN B  1 649 ? -17.562 -6.981  85.192  1.00 114.59 ? 649  GLN C CG  1 
ATOM   12088 C  CD  . GLN B  1 649 ? -17.626 -6.748  86.693  1.00 115.03 ? 649  GLN C CD  1 
ATOM   12089 O  OE1 . GLN B  1 649 ? -17.081 -7.528  87.476  1.00 113.89 ? 649  GLN C OE1 1 
ATOM   12090 N  NE2 . GLN B  1 649 ? -18.295 -5.675  87.101  1.00 114.76 ? 649  GLN C NE2 1 
ATOM   12091 N  N   . ASN B  1 650 ? -17.318 -3.437  82.952  1.00 108.98 ? 650  ASN C N   1 
ATOM   12092 C  CA  . ASN B  1 650 ? -17.349 -2.059  82.460  1.00 104.37 ? 650  ASN C CA  1 
ATOM   12093 C  C   . ASN B  1 650 ? -15.952 -1.494  82.256  1.00 105.82 ? 650  ASN C C   1 
ATOM   12094 O  O   . ASN B  1 650 ? -15.328 -1.040  83.213  1.00 108.96 ? 650  ASN C O   1 
ATOM   12095 C  CB  . ASN B  1 650 ? -18.094 -1.151  83.439  1.00 106.88 ? 650  ASN C CB  1 
ATOM   12096 C  CG  . ASN B  1 650 ? -19.351 -0.527  82.846  1.00 114.68 ? 650  ASN C CG  1 
ATOM   12097 O  OD1 . ASN B  1 650 ? -20.120 -1.186  82.145  1.00 114.03 ? 650  ASN C OD1 1 
ATOM   12098 N  ND2 . ASN B  1 650 ? -19.553 0.762   83.141  1.00 116.05 ? 650  ASN C ND2 1 
ATOM   12099 N  N   . HIS B  1 651 ? -15.470 -1.488  81.018  1.00 105.17 ? 651  HIS C N   1 
ATOM   12100 C  CA  . HIS B  1 651 ? -14.104 -1.044  80.748  1.00 101.97 ? 651  HIS C CA  1 
ATOM   12101 C  C   . HIS B  1 651 ? -13.946 0.471   80.763  1.00 96.96  ? 651  HIS C C   1 
ATOM   12102 O  O   . HIS B  1 651 ? -12.867 0.989   81.063  1.00 92.18  ? 651  HIS C O   1 
ATOM   12103 C  CB  . HIS B  1 651 ? -13.624 -1.584  79.402  1.00 102.10 ? 651  HIS C CB  1 
ATOM   12104 C  CG  . HIS B  1 651 ? -14.405 -1.086  78.226  1.00 99.26  ? 651  HIS C CG  1 
ATOM   12105 N  ND1 . HIS B  1 651 ? -14.329 0.213   77.773  1.00 97.97  ? 651  HIS C ND1 1 
ATOM   12106 C  CD2 . HIS B  1 651 ? -15.259 -1.725  77.393  1.00 102.23 ? 651  HIS C CD2 1 
ATOM   12107 C  CE1 . HIS B  1 651 ? -15.113 0.357   76.720  1.00 100.88 ? 651  HIS C CE1 1 
ATOM   12108 N  NE2 . HIS B  1 651 ? -15.689 -0.804  76.469  1.00 105.74 ? 651  HIS C NE2 1 
ATOM   12109 N  N   . THR B  1 652 ? -15.033 1.170   80.449  1.00 96.09  ? 652  THR C N   1 
ATOM   12110 C  CA  . THR B  1 652 ? -15.032 2.624   80.318  1.00 95.23  ? 652  THR C CA  1 
ATOM   12111 C  C   . THR B  1 652 ? -14.631 3.307   81.614  1.00 96.28  ? 652  THR C C   1 
ATOM   12112 O  O   . THR B  1 652 ? -14.237 4.474   81.617  1.00 95.49  ? 652  THR C O   1 
ATOM   12113 C  CB  . THR B  1 652 ? -16.414 3.141   79.897  1.00 99.88  ? 652  THR C CB  1 
ATOM   12114 O  OG1 . THR B  1 652 ? -17.402 2.589   80.774  1.00 111.40 ? 652  THR C OG1 1 
ATOM   12115 C  CG2 . THR B  1 652 ? -16.732 2.727   78.466  1.00 93.41  ? 652  THR C CG2 1 
ATOM   12116 N  N   . LEU B  1 653 ? -14.744 2.576   82.717  1.00 100.43 ? 653  LEU C N   1 
ATOM   12117 C  CA  . LEU B  1 653 ? -14.371 3.104   84.021  1.00 98.36  ? 653  LEU C CA  1 
ATOM   12118 C  C   . LEU B  1 653 ? -12.868 3.353   84.053  1.00 95.42  ? 653  LEU C C   1 
ATOM   12119 O  O   . LEU B  1 653 ? -12.413 4.362   84.588  1.00 95.39  ? 653  LEU C O   1 
ATOM   12120 C  CB  . LEU B  1 653 ? -14.796 2.147   85.140  1.00 102.66 ? 653  LEU C CB  1 
ATOM   12121 C  CG  . LEU B  1 653 ? -16.206 1.549   85.012  1.00 106.80 ? 653  LEU C CG  1 
ATOM   12122 C  CD1 . LEU B  1 653 ? -16.574 0.724   86.247  1.00 106.12 ? 653  LEU C CD1 1 
ATOM   12123 C  CD2 . LEU B  1 653 ? -17.258 2.621   84.737  1.00 104.05 ? 653  LEU C CD2 1 
ATOM   12124 N  N   . LEU B  1 654 ? -12.108 2.437   83.453  1.00 98.52  ? 654  LEU C N   1 
ATOM   12125 C  CA  . LEU B  1 654 ? -10.658 2.589   83.290  1.00 97.99  ? 654  LEU C CA  1 
ATOM   12126 C  C   . LEU B  1 654 ? -10.316 3.499   82.105  1.00 92.06  ? 654  LEU C C   1 
ATOM   12127 O  O   . LEU B  1 654 ? -10.930 3.376   81.046  1.00 95.97  ? 654  LEU C O   1 
ATOM   12128 C  CB  . LEU B  1 654 ? -10.002 1.219   83.099  1.00 94.43  ? 654  LEU C CB  1 
ATOM   12129 C  CG  . LEU B  1 654 ? -9.497  0.530   84.362  1.00 88.62  ? 654  LEU C CG  1 
ATOM   12130 C  CD1 . LEU B  1 654 ? -9.055  -0.877  84.042  1.00 82.33  ? 654  LEU C CD1 1 
ATOM   12131 C  CD2 . LEU B  1 654 ? -8.350  1.331   84.965  1.00 89.00  ? 654  LEU C CD2 1 
ATOM   12132 N  N   . ARG B  1 655 ? -9.342  4.396   82.283  1.00 87.44  ? 655  ARG C N   1 
ATOM   12133 C  CA  . ARG B  1 655 ? -8.936  5.331   81.222  1.00 88.02  ? 655  ARG C CA  1 
ATOM   12134 C  C   . ARG B  1 655 ? -8.504  4.608   79.936  1.00 89.60  ? 655  ARG C C   1 
ATOM   12135 O  O   . ARG B  1 655 ? -7.907  3.527   79.995  1.00 84.85  ? 655  ARG C O   1 
ATOM   12136 C  CB  . ARG B  1 655 ? -7.801  6.242   81.706  1.00 77.03  ? 655  ARG C CB  1 
ATOM   12137 C  CG  . ARG B  1 655 ? -8.219  7.258   82.742  1.00 78.05  ? 655  ARG C CG  1 
ATOM   12138 C  CD  . ARG B  1 655 ? -7.218  8.395   82.850  1.00 79.97  ? 655  ARG C CD  1 
ATOM   12139 N  NE  . ARG B  1 655 ? -7.858  9.681   82.561  1.00 92.20  ? 655  ARG C NE  1 
ATOM   12140 C  CZ  . ARG B  1 655 ? -7.215  10.813  82.265  1.00 93.14  ? 655  ARG C CZ  1 
ATOM   12141 N  NH1 . ARG B  1 655 ? -5.889  10.850  82.204  1.00 89.67  ? 655  ARG C NH1 1 
ATOM   12142 N  NH2 . ARG B  1 655 ? -7.907  11.919  82.023  1.00 91.52  ? 655  ARG C NH2 1 
ATOM   12143 N  N   . PRO B  1 656 ? -8.816  5.203   78.770  1.00 91.38  ? 656  PRO C N   1 
ATOM   12144 C  CA  . PRO B  1 656 ? -8.475  4.639   77.457  1.00 85.30  ? 656  PRO C CA  1 
ATOM   12145 C  C   . PRO B  1 656 ? -6.985  4.374   77.297  1.00 82.22  ? 656  PRO C C   1 
ATOM   12146 O  O   . PRO B  1 656 ? -6.608  3.342   76.740  1.00 80.40  ? 656  PRO C O   1 
ATOM   12147 C  CB  . PRO B  1 656 ? -8.940  5.721   76.482  1.00 85.49  ? 656  PRO C CB  1 
ATOM   12148 C  CG  . PRO B  1 656 ? -10.021 6.433   77.203  1.00 88.01  ? 656  PRO C CG  1 
ATOM   12149 C  CD  . PRO B  1 656 ? -9.590  6.451   78.641  1.00 88.97  ? 656  PRO C CD  1 
ATOM   12150 N  N   . LYS B  1 657 ? -6.155  5.291   77.790  1.00 82.46  ? 657  LYS C N   1 
ATOM   12151 C  CA  . LYS B  1 657 ? -4.704  5.128   77.730  1.00 83.87  ? 657  LYS C CA  1 
ATOM   12152 C  C   . LYS B  1 657 ? -4.177  4.200   78.818  1.00 85.97  ? 657  LYS C C   1 
ATOM   12153 O  O   . LYS B  1 657 ? -3.007  3.812   78.794  1.00 86.91  ? 657  LYS C O   1 
ATOM   12154 C  CB  . LYS B  1 657 ? -4.009  6.484   77.830  1.00 82.90  ? 657  LYS C CB  1 
ATOM   12155 C  CG  . LYS B  1 657 ? -4.072  7.288   76.547  1.00 82.17  ? 657  LYS C CG  1 
ATOM   12156 C  CD  . LYS B  1 657 ? -3.516  8.687   76.734  1.00 84.66  ? 657  LYS C CD  1 
ATOM   12157 C  CE  . LYS B  1 657 ? -3.557  9.454   75.431  1.00 77.08  ? 657  LYS C CE  1 
ATOM   12158 N  NZ  . LYS B  1 657 ? -4.880  9.300   74.762  1.00 83.84  ? 657  LYS C NZ  1 
ATOM   12159 N  N   . ASP B  1 658 ? -5.040  3.862   79.776  1.00 89.15  ? 658  ASP C N   1 
ATOM   12160 C  CA  . ASP B  1 658 ? -4.709  2.888   80.817  1.00 87.84  ? 658  ASP C CA  1 
ATOM   12161 C  C   . ASP B  1 658 ? -5.023  1.478   80.326  1.00 81.64  ? 658  ASP C C   1 
ATOM   12162 O  O   . ASP B  1 658 ? -4.282  0.538   80.601  1.00 80.71  ? 658  ASP C O   1 
ATOM   12163 C  CB  . ASP B  1 658 ? -5.464  3.192   82.121  1.00 92.39  ? 658  ASP C CB  1 
ATOM   12164 C  CG  . ASP B  1 658 ? -4.704  4.148   83.033  1.00 90.41  ? 658  ASP C CG  1 
ATOM   12165 O  OD1 . ASP B  1 658 ? -3.533  3.849   83.368  1.00 90.70  ? 658  ASP C OD1 1 
ATOM   12166 O  OD2 . ASP B  1 658 ? -5.274  5.199   83.406  1.00 87.96  ? 658  ASP C OD2 1 
ATOM   12167 N  N   . ARG B  1 659 ? -6.127  1.347   79.597  1.00 81.54  ? 659  ARG C N   1 
ATOM   12168 C  CA  . ARG B  1 659 ? -6.461  0.104   78.915  1.00 80.22  ? 659  ARG C CA  1 
ATOM   12169 C  C   . ARG B  1 659 ? -5.278  -0.360  78.083  1.00 82.73  ? 659  ARG C C   1 
ATOM   12170 O  O   . ARG B  1 659 ? -4.841  -1.508  78.182  1.00 80.24  ? 659  ARG C O   1 
ATOM   12171 C  CB  . ARG B  1 659 ? -7.690  0.295   78.030  1.00 80.65  ? 659  ARG C CB  1 
ATOM   12172 C  CG  . ARG B  1 659 ? -8.981  0.472   78.796  1.00 85.07  ? 659  ARG C CG  1 
ATOM   12173 C  CD  . ARG B  1 659 ? -10.118 0.875   77.884  1.00 84.48  ? 659  ARG C CD  1 
ATOM   12174 N  NE  . ARG B  1 659 ? -10.778 2.078   78.376  1.00 88.29  ? 659  ARG C NE  1 
ATOM   12175 C  CZ  . ARG B  1 659 ? -11.529 2.880   77.627  1.00 92.38  ? 659  ARG C CZ  1 
ATOM   12176 N  NH1 . ARG B  1 659 ? -11.714 2.612   76.340  1.00 94.66  ? 659  ARG C NH1 1 
ATOM   12177 N  NH2 . ARG B  1 659 ? -12.090 3.959   78.163  1.00 87.32  ? 659  ARG C NH2 1 
ATOM   12178 N  N   . VAL B  1 660 ? -4.759  0.557   77.272  1.00 86.22  ? 660  VAL C N   1 
ATOM   12179 C  CA  . VAL B  1 660 ? -3.582  0.291   76.461  1.00 84.37  ? 660  VAL C CA  1 
ATOM   12180 C  C   . VAL B  1 660 ? -2.449  -0.163  77.359  1.00 75.70  ? 660  VAL C C   1 
ATOM   12181 O  O   . VAL B  1 660 ? -1.947  -1.277  77.217  1.00 71.30  ? 660  VAL C O   1 
ATOM   12182 C  CB  . VAL B  1 660 ? -3.138  1.533   75.663  1.00 83.31  ? 660  VAL C CB  1 
ATOM   12183 C  CG1 . VAL B  1 660 ? -1.930  1.198   74.798  1.00 77.80  ? 660  VAL C CG1 1 
ATOM   12184 C  CG2 . VAL B  1 660 ? -4.287  2.059   74.814  1.00 73.84  ? 660  VAL C CG2 1 
ATOM   12185 N  N   . GLY B  1 661 ? -2.079  0.704   78.301  1.00 76.63  ? 661  GLY C N   1 
ATOM   12186 C  CA  . GLY B  1 661 ? -1.002  0.427   79.235  1.00 77.91  ? 661  GLY C CA  1 
ATOM   12187 C  C   . GLY B  1 661 ? -1.080  -0.964  79.834  1.00 80.31  ? 661  GLY C C   1 
ATOM   12188 O  O   . GLY B  1 661 ? -0.088  -1.698  79.859  1.00 77.25  ? 661  GLY C O   1 
ATOM   12189 N  N   . LEU B  1 662 ? -2.277  -1.337  80.282  1.00 85.12  ? 662  LEU C N   1 
ATOM   12190 C  CA  . LEU B  1 662 ? -2.497  -2.616  80.956  1.00 82.77  ? 662  LEU C CA  1 
ATOM   12191 C  C   . LEU B  1 662 ? -2.334  -3.803  80.014  1.00 75.62  ? 662  LEU C C   1 
ATOM   12192 O  O   . LEU B  1 662 ? -1.697  -4.792  80.379  1.00 72.72  ? 662  LEU C O   1 
ATOM   12193 C  CB  . LEU B  1 662 ? -3.886  -2.645  81.614  1.00 85.11  ? 662  LEU C CB  1 
ATOM   12194 C  CG  . LEU B  1 662 ? -4.011  -1.902  82.953  1.00 82.08  ? 662  LEU C CG  1 
ATOM   12195 C  CD1 . LEU B  1 662 ? -5.459  -1.573  83.263  1.00 84.52  ? 662  LEU C CD1 1 
ATOM   12196 C  CD2 . LEU B  1 662 ? -3.389  -2.706  84.091  1.00 76.75  ? 662  LEU C CD2 1 
ATOM   12197 N  N   . ILE B  1 663 ? -2.897  -3.717  78.811  1.00 75.35  ? 663  ILE C N   1 
ATOM   12198 C  CA  . ILE B  1 663 ? -2.711  -4.801  77.849  1.00 79.23  ? 663  ILE C CA  1 
ATOM   12199 C  C   . ILE B  1 663 ? -1.224  -4.993  77.600  1.00 72.79  ? 663  ILE C C   1 
ATOM   12200 O  O   . ILE B  1 663 ? -0.725  -6.116  77.588  1.00 69.40  ? 663  ILE C O   1 
ATOM   12201 C  CB  . ILE B  1 663 ? -3.407  -4.534  76.505  1.00 78.46  ? 663  ILE C CB  1 
ATOM   12202 C  CG1 . ILE B  1 663 ? -4.881  -4.196  76.722  1.00 80.98  ? 663  ILE C CG1 1 
ATOM   12203 C  CG2 . ILE B  1 663 ? -3.234  -5.735  75.573  1.00 62.90  ? 663  ILE C CG2 1 
ATOM   12204 C  CD1 . ILE B  1 663 ? -5.508  -3.447  75.569  1.00 82.55  ? 663  ILE C CD1 1 
ATOM   12205 N  N   . HIS B  1 664 ? -0.522  -3.879  77.422  1.00 70.70  ? 664  HIS C N   1 
ATOM   12206 C  CA  . HIS B  1 664 ? 0.899   -3.923  77.137  1.00 69.44  ? 664  HIS C CA  1 
ATOM   12207 C  C   . HIS B  1 664 ? 1.663   -4.626  78.233  1.00 72.20  ? 664  HIS C C   1 
ATOM   12208 O  O   . HIS B  1 664 ? 2.377   -5.595  77.976  1.00 72.43  ? 664  HIS C O   1 
ATOM   12209 C  CB  . HIS B  1 664 ? 1.471   -2.526  76.965  1.00 68.91  ? 664  HIS C CB  1 
ATOM   12210 C  CG  . HIS B  1 664 ? 2.967   -2.500  76.937  1.00 67.39  ? 664  HIS C CG  1 
ATOM   12211 N  ND1 . HIS B  1 664 ? 3.699   -2.916  75.843  1.00 67.94  ? 664  HIS C ND1 1 
ATOM   12212 C  CD2 . HIS B  1 664 ? 3.869   -2.131  77.876  1.00 59.39  ? 664  HIS C CD2 1 
ATOM   12213 C  CE1 . HIS B  1 664 ? 4.988   -2.789  76.105  1.00 66.94  ? 664  HIS C CE1 1 
ATOM   12214 N  NE2 . HIS B  1 664 ? 5.119   -2.316  77.333  1.00 61.47  ? 664  HIS C NE2 1 
ATOM   12215 N  N   . ASP B  1 665 ? 1.508   -4.127  79.457  1.00 71.00  ? 665  ASP C N   1 
ATOM   12216 C  CA  . ASP B  1 665 ? 2.251   -4.643  80.591  1.00 70.07  ? 665  ASP C CA  1 
ATOM   12217 C  C   . ASP B  1 665 ? 1.896   -6.100  80.881  1.00 70.20  ? 665  ASP C C   1 
ATOM   12218 O  O   . ASP B  1 665 ? 2.739   -6.868  81.352  1.00 69.81  ? 665  ASP C O   1 
ATOM   12219 C  CB  . ASP B  1 665 ? 1.996   -3.778  81.830  1.00 78.51  ? 665  ASP C CB  1 
ATOM   12220 C  CG  . ASP B  1 665 ? 2.633   -2.397  81.729  1.00 79.16  ? 665  ASP C CG  1 
ATOM   12221 O  OD1 . ASP B  1 665 ? 3.609   -2.231  80.965  1.00 79.29  ? 665  ASP C OD1 1 
ATOM   12222 O  OD2 . ASP B  1 665 ? 2.161   -1.473  82.430  1.00 84.13  ? 665  ASP C OD2 1 
ATOM   12223 N  N   . VAL B  1 666 ? 0.652   -6.472  80.591  1.00 68.88  ? 666  VAL C N   1 
ATOM   12224 C  CA  . VAL B  1 666 ? 0.170   -7.839  80.814  1.00 77.90  ? 666  VAL C CA  1 
ATOM   12225 C  C   . VAL B  1 666 ? 1.072   -8.885  80.153  1.00 75.51  ? 666  VAL C C   1 
ATOM   12226 O  O   . VAL B  1 666 ? 1.543   -9.809  80.824  1.00 72.96  ? 666  VAL C O   1 
ATOM   12227 C  CB  . VAL B  1 666 ? -1.299  -8.007  80.312  1.00 80.93  ? 666  VAL C CB  1 
ATOM   12228 C  CG1 . VAL B  1 666 ? -1.520  -9.352  79.678  1.00 78.35  ? 666  VAL C CG1 1 
ATOM   12229 C  CG2 . VAL B  1 666 ? -2.285  -7.809  81.459  1.00 75.66  ? 666  VAL C CG2 1 
ATOM   12230 N  N   . PHE B  1 667 ? 1.342   -8.724  78.858  1.00 71.65  ? 667  PHE C N   1 
ATOM   12231 C  CA  . PHE B  1 667 ? 2.127   -9.712  78.122  1.00 69.27  ? 667  PHE C CA  1 
ATOM   12232 C  C   . PHE B  1 667 ? 3.610   -9.559  78.397  1.00 67.27  ? 667  PHE C C   1 
ATOM   12233 O  O   . PHE B  1 667 ? 4.359   -10.534 78.369  1.00 65.10  ? 667  PHE C O   1 
ATOM   12234 C  CB  . PHE B  1 667 ? 1.884   -9.593  76.625  1.00 70.32  ? 667  PHE C CB  1 
ATOM   12235 C  CG  . PHE B  1 667 ? 0.484   -9.913  76.207  1.00 68.66  ? 667  PHE C CG  1 
ATOM   12236 C  CD1 . PHE B  1 667 ? -0.515  -8.965  76.315  1.00 69.53  ? 667  PHE C CD1 1 
ATOM   12237 C  CD2 . PHE B  1 667 ? 0.175   -11.152 75.675  1.00 71.38  ? 667  PHE C CD2 1 
ATOM   12238 C  CE1 . PHE B  1 667 ? -1.801  -9.251  75.921  1.00 72.39  ? 667  PHE C CE1 1 
ATOM   12239 C  CE2 . PHE B  1 667 ? -1.116  -11.447 75.274  1.00 73.39  ? 667  PHE C CE2 1 
ATOM   12240 C  CZ  . PHE B  1 667 ? -2.104  -10.500 75.397  1.00 70.66  ? 667  PHE C CZ  1 
ATOM   12241 N  N   . GLN B  1 668 ? 4.032   -8.321  78.640  1.00 68.20  ? 668  GLN C N   1 
ATOM   12242 C  CA  . GLN B  1 668 ? 5.426   -8.038  78.969  1.00 70.50  ? 668  GLN C CA  1 
ATOM   12243 C  C   . GLN B  1 668 ? 5.848   -8.882  80.162  1.00 71.56  ? 668  GLN C C   1 
ATOM   12244 O  O   . GLN B  1 668 ? 6.936   -9.462  80.182  1.00 69.51  ? 668  GLN C O   1 
ATOM   12245 C  CB  . GLN B  1 668 ? 5.631   -6.548  79.267  1.00 69.41  ? 668  GLN C CB  1 
ATOM   12246 C  CG  . GLN B  1 668 ? 5.432   -5.638  78.069  1.00 62.63  ? 668  GLN C CG  1 
ATOM   12247 C  CD  . GLN B  1 668 ? 6.131   -6.155  76.838  1.00 64.08  ? 668  GLN C CD  1 
ATOM   12248 O  OE1 . GLN B  1 668 ? 5.500   -6.409  75.802  1.00 52.23  ? 668  GLN C OE1 1 
ATOM   12249 N  NE2 . GLN B  1 668 ? 7.447   -6.335  76.944  1.00 64.57  ? 668  GLN C NE2 1 
ATOM   12250 N  N   . LEU B  1 669 ? 4.956   -8.962  81.143  1.00 73.69  ? 669  LEU C N   1 
ATOM   12251 C  CA  . LEU B  1 669 ? 5.188   -9.753  82.337  1.00 75.77  ? 669  LEU C CA  1 
ATOM   12252 C  C   . LEU B  1 669 ? 5.030   -11.250 82.070  1.00 77.74  ? 669  LEU C C   1 
ATOM   12253 O  O   . LEU B  1 669 ? 5.699   -12.069 82.710  1.00 77.77  ? 669  LEU C O   1 
ATOM   12254 C  CB  . LEU B  1 669 ? 4.248   -9.297  83.449  1.00 75.64  ? 669  LEU C CB  1 
ATOM   12255 C  CG  . LEU B  1 669 ? 4.702   -7.982  84.087  1.00 81.79  ? 669  LEU C CG  1 
ATOM   12256 C  CD1 . LEU B  1 669 ? 3.593   -7.362  84.922  1.00 79.89  ? 669  LEU C CD1 1 
ATOM   12257 C  CD2 . LEU B  1 669 ? 5.964   -8.190  84.926  1.00 76.91  ? 669  LEU C CD2 1 
ATOM   12258 N  N   . VAL B  1 670 ? 4.157   -11.605 81.126  1.00 73.97  ? 670  VAL C N   1 
ATOM   12259 C  CA  . VAL B  1 670 ? 4.052   -12.992 80.689  1.00 68.76  ? 670  VAL C CA  1 
ATOM   12260 C  C   . VAL B  1 670 ? 5.423   -13.497 80.256  1.00 73.08  ? 670  VAL C C   1 
ATOM   12261 O  O   . VAL B  1 670 ? 5.833   -14.599 80.626  1.00 77.55  ? 670  VAL C O   1 
ATOM   12262 C  CB  . VAL B  1 670 ? 3.051   -13.152 79.538  1.00 72.09  ? 670  VAL C CB  1 
ATOM   12263 C  CG1 . VAL B  1 670 ? 3.227   -14.489 78.868  1.00 68.95  ? 670  VAL C CG1 1 
ATOM   12264 C  CG2 . VAL B  1 670 ? 1.639   -12.998 80.052  1.00 74.87  ? 670  VAL C CG2 1 
ATOM   12265 N  N   . GLY B  1 671 ? 6.140   -12.673 79.497  1.00 72.33  ? 671  GLY C N   1 
ATOM   12266 C  CA  . GLY B  1 671 ? 7.474   -13.019 79.041  1.00 72.60  ? 671  GLY C CA  1 
ATOM   12267 C  C   . GLY B  1 671 ? 8.481   -13.149 80.169  1.00 74.30  ? 671  GLY C C   1 
ATOM   12268 O  O   . GLY B  1 671 ? 9.409   -13.945 80.093  1.00 79.30  ? 671  GLY C O   1 
ATOM   12269 N  N   . ALA B  1 672 ? 8.290   -12.375 81.229  1.00 77.73  ? 672  ALA C N   1 
ATOM   12270 C  CA  . ALA B  1 672 ? 9.206   -12.404 82.367  1.00 80.60  ? 672  ALA C CA  1 
ATOM   12271 C  C   . ALA B  1 672 ? 8.974   -13.611 83.275  1.00 86.90  ? 672  ALA C C   1 
ATOM   12272 O  O   . ALA B  1 672 ? 9.882   -14.054 83.982  1.00 92.40  ? 672  ALA C O   1 
ATOM   12273 C  CB  . ALA B  1 672 ? 9.082   -11.125 83.169  1.00 77.82  ? 672  ALA C CB  1 
ATOM   12274 N  N   . GLY B  1 673 ? 7.754   -14.133 83.262  1.00 80.86  ? 673  GLY C N   1 
ATOM   12275 C  CA  . GLY B  1 673 ? 7.395   -15.213 84.158  1.00 80.69  ? 673  GLY C CA  1 
ATOM   12276 C  C   . GLY B  1 673 ? 6.623   -14.718 85.369  1.00 84.94  ? 673  GLY C C   1 
ATOM   12277 O  O   . GLY B  1 673 ? 6.358   -15.475 86.297  1.00 93.20  ? 673  GLY C O   1 
ATOM   12278 N  N   . ARG B  1 674 ? 6.250   -13.446 85.367  1.00 82.22  ? 674  ARG C N   1 
ATOM   12279 C  CA  . ARG B  1 674 ? 5.542   -12.873 86.506  1.00 87.45  ? 674  ARG C CA  1 
ATOM   12280 C  C   . ARG B  1 674 ? 4.038   -12.896 86.257  1.00 84.50  ? 674  ARG C C   1 
ATOM   12281 O  O   . ARG B  1 674 ? 3.261   -12.311 87.011  1.00 82.64  ? 674  ARG C O   1 
ATOM   12282 C  CB  . ARG B  1 674 ? 6.023   -11.446 86.779  1.00 85.95  ? 674  ARG C CB  1 
ATOM   12283 C  CG  . ARG B  1 674 ? 7.524   -11.281 86.635  1.00 87.98  ? 674  ARG C CG  1 
ATOM   12284 C  CD  . ARG B  1 674 ? 8.269   -12.087 87.671  1.00 86.93  ? 674  ARG C CD  1 
ATOM   12285 N  NE  . ARG B  1 674 ? 8.768   -11.226 88.736  1.00 89.67  ? 674  ARG C NE  1 
ATOM   12286 C  CZ  . ARG B  1 674 ? 9.946   -10.615 88.698  1.00 90.82  ? 674  ARG C CZ  1 
ATOM   12287 N  NH1 . ARG B  1 674 ? 10.743  -10.777 87.646  1.00 89.60  ? 674  ARG C NH1 1 
ATOM   12288 N  NH2 . ARG B  1 674 ? 10.331  -9.849  89.707  1.00 82.95  ? 674  ARG C NH2 1 
ATOM   12289 N  N   . LEU B  1 675 ? 3.652   -13.560 85.173  1.00 80.02  ? 675  LEU C N   1 
ATOM   12290 C  CA  . LEU B  1 675 ? 2.260   -13.867 84.870  1.00 76.74  ? 675  LEU C CA  1 
ATOM   12291 C  C   . LEU B  1 675 ? 2.275   -15.005 83.875  1.00 73.30  ? 675  LEU C C   1 
ATOM   12292 O  O   . LEU B  1 675 ? 3.260   -15.200 83.168  1.00 68.16  ? 675  LEU C O   1 
ATOM   12293 C  CB  . LEU B  1 675 ? 1.502   -12.662 84.304  1.00 76.81  ? 675  LEU C CB  1 
ATOM   12294 C  CG  . LEU B  1 675 ? 0.867   -11.674 85.291  1.00 84.14  ? 675  LEU C CG  1 
ATOM   12295 C  CD1 . LEU B  1 675 ? 0.047   -10.603 84.582  1.00 78.40  ? 675  LEU C CD1 1 
ATOM   12296 C  CD2 . LEU B  1 675 ? 0.024   -12.413 86.321  1.00 86.61  ? 675  LEU C CD2 1 
ATOM   12297 N  N   . THR B  1 676 ? 1.191   -15.767 83.840  1.00 76.84  ? 676  THR C N   1 
ATOM   12298 C  CA  . THR B  1 676 ? 1.094   -16.913 82.952  1.00 81.13  ? 676  THR C CA  1 
ATOM   12299 C  C   . THR B  1 676 ? 0.340   -16.487 81.701  1.00 78.52  ? 676  THR C C   1 
ATOM   12300 O  O   . THR B  1 676 ? -0.458  -15.548 81.752  1.00 80.72  ? 676  THR C O   1 
ATOM   12301 C  CB  . THR B  1 676 ? 0.386   -18.108 83.642  1.00 83.20  ? 676  THR C CB  1 
ATOM   12302 O  OG1 . THR B  1 676 ? 0.483   -19.278 82.818  1.00 90.82  ? 676  THR C OG1 1 
ATOM   12303 C  CG2 . THR B  1 676 ? -1.087  -17.785 83.917  1.00 79.08  ? 676  THR C CG2 1 
ATOM   12304 N  N   . LEU B  1 677 ? 0.586   -17.164 80.582  1.00 76.85  ? 677  LEU C N   1 
ATOM   12305 C  CA  . LEU B  1 677 ? -0.041  -16.769 79.322  1.00 79.43  ? 677  LEU C CA  1 
ATOM   12306 C  C   . LEU B  1 677 ? -1.572  -16.753 79.395  1.00 86.75  ? 677  LEU C C   1 
ATOM   12307 O  O   . LEU B  1 677 ? -2.224  -15.971 78.698  1.00 87.55  ? 677  LEU C O   1 
ATOM   12308 C  CB  . LEU B  1 677 ? 0.408   -17.687 78.189  1.00 84.42  ? 677  LEU C CB  1 
ATOM   12309 C  CG  . LEU B  1 677 ? 0.010   -17.203 76.791  1.00 85.08  ? 677  LEU C CG  1 
ATOM   12310 C  CD1 . LEU B  1 677 ? 0.648   -15.853 76.480  1.00 82.32  ? 677  LEU C CD1 1 
ATOM   12311 C  CD2 . LEU B  1 677 ? 0.385   -18.213 75.743  1.00 81.02  ? 677  LEU C CD2 1 
ATOM   12312 N  N   . ASP B  1 678 ? -2.130  -17.615 80.243  1.00 92.38  ? 678  ASP C N   1 
ATOM   12313 C  CA  . ASP B  1 678 ? -3.574  -17.692 80.481  1.00 89.45  ? 678  ASP C CA  1 
ATOM   12314 C  C   . ASP B  1 678 ? -4.227  -16.340 80.707  1.00 95.11  ? 678  ASP C C   1 
ATOM   12315 O  O   . ASP B  1 678 ? -5.147  -15.956 79.981  1.00 97.39  ? 678  ASP C O   1 
ATOM   12316 C  CB  . ASP B  1 678 ? -3.858  -18.568 81.696  1.00 86.72  ? 678  ASP C CB  1 
ATOM   12317 C  CG  . ASP B  1 678 ? -3.235  -19.928 81.575  1.00 98.03  ? 678  ASP C CG  1 
ATOM   12318 O  OD1 . ASP B  1 678 ? -3.410  -20.560 80.509  1.00 100.43 ? 678  ASP C OD1 1 
ATOM   12319 O  OD2 . ASP B  1 678 ? -2.563  -20.359 82.538  1.00 95.14  ? 678  ASP C OD2 1 
ATOM   12320 N  N   . LYS B  1 679 ? -3.748  -15.638 81.733  1.00 95.18  ? 679  LYS C N   1 
ATOM   12321 C  CA  . LYS B  1 679 ? -4.309  -14.359 82.151  1.00 95.58  ? 679  LYS C CA  1 
ATOM   12322 C  C   . LYS B  1 679 ? -4.305  -13.377 80.999  1.00 98.57  ? 679  LYS C C   1 
ATOM   12323 O  O   . LYS B  1 679 ? -5.277  -12.645 80.783  1.00 97.07  ? 679  LYS C O   1 
ATOM   12324 C  CB  . LYS B  1 679 ? -3.516  -13.773 83.324  1.00 92.44  ? 679  LYS C CB  1 
ATOM   12325 C  CG  . LYS B  1 679 ? -3.344  -14.701 84.506  1.00 92.56  ? 679  LYS C CG  1 
ATOM   12326 C  CD  . LYS B  1 679 ? -4.127  -14.203 85.707  1.00 97.87  ? 679  LYS C CD  1 
ATOM   12327 C  CE  . LYS B  1 679 ? -3.694  -14.933 86.962  1.00 101.07 ? 679  LYS C CE  1 
ATOM   12328 N  NZ  . LYS B  1 679 ? -2.213  -14.860 87.146  1.00 98.93  ? 679  LYS C NZ  1 
ATOM   12329 N  N   . ALA B  1 680 ? -3.191  -13.381 80.268  1.00 100.45 ? 680  ALA C N   1 
ATOM   12330 C  CA  . ALA B  1 680 ? -2.964  -12.463 79.159  1.00 93.74  ? 680  ALA C CA  1 
ATOM   12331 C  C   . ALA B  1 680 ? -4.038  -12.598 78.093  1.00 91.23  ? 680  ALA C C   1 
ATOM   12332 O  O   . ALA B  1 680 ? -4.640  -11.617 77.675  1.00 93.14  ? 680  ALA C O   1 
ATOM   12333 C  CB  . ALA B  1 680 ? -1.586  -12.703 78.556  1.00 87.31  ? 680  ALA C CB  1 
ATOM   12334 N  N   . LEU B  1 681 ? -4.277  -13.822 77.657  1.00 87.05  ? 681  LEU C N   1 
ATOM   12335 C  CA  . LEU B  1 681 ? -5.283  -14.060 76.643  1.00 93.72  ? 681  LEU C CA  1 
ATOM   12336 C  C   . LEU B  1 681 ? -6.667  -13.694 77.170  1.00 95.13  ? 681  LEU C C   1 
ATOM   12337 O  O   . LEU B  1 681 ? -7.479  -13.114 76.454  1.00 94.04  ? 681  LEU C O   1 
ATOM   12338 C  CB  . LEU B  1 681 ? -5.213  -15.511 76.199  1.00 88.45  ? 681  LEU C CB  1 
ATOM   12339 C  CG  . LEU B  1 681 ? -3.790  -15.816 75.751  1.00 87.54  ? 681  LEU C CG  1 
ATOM   12340 C  CD1 . LEU B  1 681 ? -3.552  -17.300 75.535  1.00 89.04  ? 681  LEU C CD1 1 
ATOM   12341 C  CD2 . LEU B  1 681 ? -3.514  -15.018 74.485  1.00 86.37  ? 681  LEU C CD2 1 
ATOM   12342 N  N   . ASP B  1 682 ? -6.912  -14.012 78.438  1.00 96.71  ? 682  ASP C N   1 
ATOM   12343 C  CA  . ASP B  1 682 ? -8.162  -13.656 79.107  1.00 100.44 ? 682  ASP C CA  1 
ATOM   12344 C  C   . ASP B  1 682 ? -8.394  -12.146 79.063  1.00 97.67  ? 682  ASP C C   1 
ATOM   12345 O  O   . ASP B  1 682 ? -9.529  -11.677 79.078  1.00 98.11  ? 682  ASP C O   1 
ATOM   12346 C  CB  . ASP B  1 682 ? -8.157  -14.147 80.562  1.00 101.03 ? 682  ASP C CB  1 
ATOM   12347 C  CG  . ASP B  1 682 ? -8.357  -15.653 80.681  1.00 102.35 ? 682  ASP C CG  1 
ATOM   12348 O  OD1 . ASP B  1 682 ? -8.270  -16.355 79.649  1.00 102.67 ? 682  ASP C OD1 1 
ATOM   12349 O  OD2 . ASP B  1 682 ? -8.595  -16.135 81.813  1.00 100.50 ? 682  ASP C OD2 1 
ATOM   12350 N  N   . MET B  1 683 ? -7.300  -11.395 79.009  1.00 97.33  ? 683  MET C N   1 
ATOM   12351 C  CA  . MET B  1 683 ? -7.346  -9.944  78.886  1.00 98.69  ? 683  MET C CA  1 
ATOM   12352 C  C   . MET B  1 683 ? -7.934  -9.513  77.538  1.00 98.09  ? 683  MET C C   1 
ATOM   12353 O  O   . MET B  1 683 ? -8.537  -8.447  77.418  1.00 94.95  ? 683  MET C O   1 
ATOM   12354 C  CB  . MET B  1 683 ? -5.938  -9.368  79.067  1.00 96.17  ? 683  MET C CB  1 
ATOM   12355 C  CG  . MET B  1 683 ? -5.811  -7.879  78.869  1.00 93.56  ? 683  MET C CG  1 
ATOM   12356 S  SD  . MET B  1 683 ? -6.470  -6.988  80.277  1.00 93.30  ? 683  MET C SD  1 
ATOM   12357 C  CE  . MET B  1 683 ? -5.775  -5.367  79.998  1.00 94.80  ? 683  MET C CE  1 
ATOM   12358 N  N   . THR B  1 684 ? -7.767  -10.357 76.527  1.00 98.34  ? 684  THR C N   1 
ATOM   12359 C  CA  . THR B  1 684 ? -8.197  -10.018 75.176  1.00 100.83 ? 684  THR C CA  1 
ATOM   12360 C  C   . THR B  1 684 ? -9.711  -9.988  75.009  1.00 105.24 ? 684  THR C C   1 
ATOM   12361 O  O   . THR B  1 684 ? -10.230 -9.211  74.207  1.00 105.32 ? 684  THR C O   1 
ATOM   12362 C  CB  . THR B  1 684 ? -7.637  -11.005 74.147  1.00 100.01 ? 684  THR C CB  1 
ATOM   12363 O  OG1 . THR B  1 684 ? -8.188  -12.302 74.396  1.00 95.41  ? 684  THR C OG1 1 
ATOM   12364 C  CG2 . THR B  1 684 ? -6.125  -11.072 74.247  1.00 97.15  ? 684  THR C CG2 1 
ATOM   12365 N  N   . TYR B  1 685 ? -10.413 -10.843 75.749  1.00 104.36 ? 685  TYR C N   1 
ATOM   12366 C  CA  . TYR B  1 685 ? -11.860 -10.957 75.608  1.00 102.34 ? 685  TYR C CA  1 
ATOM   12367 C  C   . TYR B  1 685 ? -12.550 -9.599  75.705  1.00 99.56  ? 685  TYR C C   1 
ATOM   12368 O  O   . TYR B  1 685 ? -13.505 -9.324  74.980  1.00 102.07 ? 685  TYR C O   1 
ATOM   12369 C  CB  . TYR B  1 685 ? -12.426 -11.905 76.661  1.00 100.50 ? 685  TYR C CB  1 
ATOM   12370 C  CG  . TYR B  1 685 ? -12.356 -13.369 76.289  1.00 102.24 ? 685  TYR C CG  1 
ATOM   12371 C  CD1 . TYR B  1 685 ? -13.039 -13.861 75.178  1.00 104.65 ? 685  TYR C CD1 1 
ATOM   12372 C  CD2 . TYR B  1 685 ? -11.630 -14.267 77.062  1.00 102.25 ? 685  TYR C CD2 1 
ATOM   12373 C  CE1 . TYR B  1 685 ? -12.985 -15.208 74.841  1.00 102.67 ? 685  TYR C CE1 1 
ATOM   12374 C  CE2 . TYR B  1 685 ? -11.579 -15.608 76.741  1.00 99.57  ? 685  TYR C CE2 1 
ATOM   12375 C  CZ  . TYR B  1 685 ? -12.247 -16.075 75.628  1.00 104.42 ? 685  TYR C CZ  1 
ATOM   12376 O  OH  . TYR B  1 685 ? -12.179 -17.415 75.318  1.00 106.33 ? 685  TYR C OH  1 
ATOM   12377 N  N   . TYR B  1 686 ? -12.030 -8.738  76.572  1.00 97.32  ? 686  TYR C N   1 
ATOM   12378 C  CA  . TYR B  1 686 ? -12.635 -7.431  76.803  1.00 104.32 ? 686  TYR C CA  1 
ATOM   12379 C  C   . TYR B  1 686 ? -12.540 -6.505  75.591  1.00 107.54 ? 686  TYR C C   1 
ATOM   12380 O  O   . TYR B  1 686 ? -13.271 -5.518  75.507  1.00 110.52 ? 686  TYR C O   1 
ATOM   12381 C  CB  . TYR B  1 686 ? -11.994 -6.757  78.031  1.00 105.77 ? 686  TYR C CB  1 
ATOM   12382 C  CG  . TYR B  1 686 ? -11.072 -5.586  77.733  1.00 103.02 ? 686  TYR C CG  1 
ATOM   12383 C  CD1 . TYR B  1 686 ? -11.578 -4.303  77.534  1.00 105.64 ? 686  TYR C CD1 1 
ATOM   12384 C  CD2 . TYR B  1 686 ? -9.696  -5.754  77.690  1.00 98.56  ? 686  TYR C CD2 1 
ATOM   12385 C  CE1 . TYR B  1 686 ? -10.744 -3.236  77.261  1.00 104.75 ? 686  TYR C CE1 1 
ATOM   12386 C  CE2 . TYR B  1 686 ? -8.852  -4.688  77.431  1.00 98.33  ? 686  TYR C CE2 1 
ATOM   12387 C  CZ  . TYR B  1 686 ? -9.382  -3.429  77.217  1.00 99.17  ? 686  TYR C CZ  1 
ATOM   12388 O  OH  . TYR B  1 686 ? -8.559  -2.357  76.955  1.00 88.91  ? 686  TYR C OH  1 
ATOM   12389 N  N   . LEU B  1 687 ? -11.640 -6.805  74.662  1.00 109.42 ? 687  LEU C N   1 
ATOM   12390 C  CA  . LEU B  1 687 ? -11.410 -5.906  73.533  1.00 105.33 ? 687  LEU C CA  1 
ATOM   12391 C  C   . LEU B  1 687 ? -12.626 -5.798  72.640  1.00 107.13 ? 687  LEU C C   1 
ATOM   12392 O  O   . LEU B  1 687 ? -12.948 -4.721  72.149  1.00 108.37 ? 687  LEU C O   1 
ATOM   12393 C  CB  . LEU B  1 687 ? -10.208 -6.361  72.725  1.00 100.04 ? 687  LEU C CB  1 
ATOM   12394 C  CG  . LEU B  1 687 ? -8.917  -6.084  73.487  1.00 101.42 ? 687  LEU C CG  1 
ATOM   12395 C  CD1 . LEU B  1 687 ? -7.728  -6.456  72.640  1.00 100.09 ? 687  LEU C CD1 1 
ATOM   12396 C  CD2 . LEU B  1 687 ? -8.855  -4.623  73.912  1.00 99.41  ? 687  LEU C CD2 1 
ATOM   12397 N  N   . GLN B  1 688 ? -13.295 -6.917  72.413  1.00 108.19 ? 688  GLN C N   1 
ATOM   12398 C  CA  . GLN B  1 688 ? -14.639 -6.836  71.892  1.00 108.76 ? 688  GLN C CA  1 
ATOM   12399 C  C   . GLN B  1 688 ? -15.416 -6.056  72.931  1.00 112.27 ? 688  GLN C C   1 
ATOM   12400 O  O   . GLN B  1 688 ? -15.257 -6.329  74.113  1.00 114.01 ? 688  GLN C O   1 
ATOM   12401 C  CB  . GLN B  1 688 ? -15.242 -8.215  71.668  1.00 110.55 ? 688  GLN C CB  1 
ATOM   12402 C  CG  . GLN B  1 688 ? -16.727 -8.167  71.404  1.00 118.68 ? 688  GLN C CG  1 
ATOM   12403 C  CD  . GLN B  1 688 ? -17.094 -7.138  70.350  1.00 116.17 ? 688  GLN C CD  1 
ATOM   12404 O  OE1 . GLN B  1 688 ? -17.499 -6.018  70.668  1.00 112.05 ? 688  GLN C OE1 1 
ATOM   12405 N  NE2 . GLN B  1 688 ? -16.949 -7.514  69.087  1.00 116.10 ? 688  GLN C NE2 1 
ATOM   12406 N  N   . HIS B  1 689 ? -16.226 -5.099  72.470  1.00 111.87 ? 689  HIS C N   1 
ATOM   12407 C  CA  . HIS B  1 689 ? -16.996 -4.116  73.267  1.00 118.20 ? 689  HIS C CA  1 
ATOM   12408 C  C   . HIS B  1 689 ? -16.215 -2.802  73.434  1.00 115.70 ? 689  HIS C C   1 
ATOM   12409 O  O   . HIS B  1 689 ? -16.683 -1.888  74.109  1.00 115.08 ? 689  HIS C O   1 
ATOM   12410 C  CB  . HIS B  1 689 ? -17.407 -4.625  74.672  1.00 120.46 ? 689  HIS C CB  1 
ATOM   12411 C  CG  . HIS B  1 689 ? -18.010 -6.004  74.693  1.00 127.57 ? 689  HIS C CG  1 
ATOM   12412 N  ND1 . HIS B  1 689 ? -18.737 -6.526  73.645  1.00 128.77 ? 689  HIS C ND1 1 
ATOM   12413 C  CD2 . HIS B  1 689 ? -17.972 -6.971  75.643  1.00 123.86 ? 689  HIS C CD2 1 
ATOM   12414 C  CE1 . HIS B  1 689 ? -19.127 -7.754  73.950  1.00 125.67 ? 689  HIS C CE1 1 
ATOM   12415 N  NE2 . HIS B  1 689 ? -18.675 -8.047  75.155  1.00 123.95 ? 689  HIS C NE2 1 
ATOM   12416 N  N   . GLU B  1 690 ? -15.035 -2.703  72.821  1.00 115.86 ? 690  GLU C N   1 
ATOM   12417 C  CA  . GLU B  1 690 ? -14.206 -1.493  72.929  1.00 110.65 ? 690  GLU C CA  1 
ATOM   12418 C  C   . GLU B  1 690 ? -14.274 -0.634  71.670  1.00 105.52 ? 690  GLU C C   1 
ATOM   12419 O  O   . GLU B  1 690 ? -13.928 -1.092  70.582  1.00 101.80 ? 690  GLU C O   1 
ATOM   12420 C  CB  . GLU B  1 690 ? -12.745 -1.863  73.216  1.00 106.31 ? 690  GLU C CB  1 
ATOM   12421 C  CG  . GLU B  1 690 ? -11.770 -0.691  73.149  1.00 99.32  ? 690  GLU C CG  1 
ATOM   12422 C  CD  . GLU B  1 690 ? -11.405 -0.143  74.520  1.00 98.72  ? 690  GLU C CD  1 
ATOM   12423 O  OE1 . GLU B  1 690 ? -10.601 -0.792  75.220  1.00 96.88  ? 690  GLU C OE1 1 
ATOM   12424 O  OE2 . GLU B  1 690 ? -11.920 0.931   74.900  1.00 91.64  ? 690  GLU C OE2 1 
ATOM   12425 N  N   . THR B  1 691 ? -14.716 0.611   71.819  1.00 103.01 ? 691  THR C N   1 
ATOM   12426 C  CA  . THR B  1 691 ? -14.763 1.537   70.689  1.00 106.87 ? 691  THR C CA  1 
ATOM   12427 C  C   . THR B  1 691 ? -13.379 2.131   70.439  1.00 106.43 ? 691  THR C C   1 
ATOM   12428 O  O   . THR B  1 691 ? -12.928 2.198   69.292  1.00 105.32 ? 691  THR C O   1 
ATOM   12429 C  CB  . THR B  1 691 ? -15.792 2.675   70.913  1.00 108.58 ? 691  THR C CB  1 
ATOM   12430 O  OG1 . THR B  1 691 ? -17.115 2.179   70.677  1.00 109.25 ? 691  THR C OG1 1 
ATOM   12431 C  CG2 . THR B  1 691 ? -15.540 3.832   69.962  1.00 98.07  ? 691  THR C CG2 1 
ATOM   12432 N  N   . SER B  1 692 ? -12.715 2.547   71.519  1.00 104.08 ? 692  SER C N   1 
ATOM   12433 C  CA  . SER B  1 692 ? -11.353 3.089   71.467  1.00 99.16  ? 692  SER C CA  1 
ATOM   12434 C  C   . SER B  1 692 ? -10.392 2.200   70.682  1.00 98.58  ? 692  SER C C   1 
ATOM   12435 O  O   . SER B  1 692 ? -10.076 1.090   71.104  1.00 98.95  ? 692  SER C O   1 
ATOM   12436 C  CB  . SER B  1 692 ? -10.811 3.298   72.883  1.00 97.08  ? 692  SER C CB  1 
ATOM   12437 O  OG  . SER B  1 692 ? -9.392  3.327   72.891  1.00 94.02  ? 692  SER C OG  1 
ATOM   12438 N  N   . SER B  1 693 ? -9.922  2.705   69.545  1.00 94.99  ? 693  SER C N   1 
ATOM   12439 C  CA  . SER B  1 693 ? -9.104  1.924   68.618  1.00 95.09  ? 693  SER C CA  1 
ATOM   12440 C  C   . SER B  1 693 ? -7.676  1.567   69.090  1.00 95.88  ? 693  SER C C   1 
ATOM   12441 O  O   . SER B  1 693 ? -7.278  0.402   68.970  1.00 92.48  ? 693  SER C O   1 
ATOM   12442 C  CB  . SER B  1 693 ? -9.024  2.655   67.277  1.00 96.91  ? 693  SER C CB  1 
ATOM   12443 O  OG  . SER B  1 693 ? -10.315 3.024   66.827  1.00 99.82  ? 693  SER C OG  1 
ATOM   12444 N  N   . PRO B  1 694 ? -6.896  2.549   69.611  1.00 96.81  ? 694  PRO C N   1 
ATOM   12445 C  CA  . PRO B  1 694 ? -5.522  2.220   70.033  1.00 94.00  ? 694  PRO C CA  1 
ATOM   12446 C  C   . PRO B  1 694 ? -5.455  1.101   71.068  1.00 92.30  ? 694  PRO C C   1 
ATOM   12447 O  O   . PRO B  1 694 ? -4.559  0.256   71.016  1.00 87.39  ? 694  PRO C O   1 
ATOM   12448 C  CB  . PRO B  1 694 ? -5.011  3.536   70.637  1.00 88.51  ? 694  PRO C CB  1 
ATOM   12449 C  CG  . PRO B  1 694 ? -6.232  4.306   70.965  1.00 89.73  ? 694  PRO C CG  1 
ATOM   12450 C  CD  . PRO B  1 694 ? -7.204  3.964   69.887  1.00 93.86  ? 694  PRO C CD  1 
ATOM   12451 N  N   . ALA B  1 695 ? -6.402  1.104   71.999  1.00 96.17  ? 695  ALA C N   1 
ATOM   12452 C  CA  . ALA B  1 695 ? -6.523  0.011   72.947  1.00 92.66  ? 695  ALA C CA  1 
ATOM   12453 C  C   . ALA B  1 695 ? -6.883  -1.272  72.210  1.00 85.72  ? 695  ALA C C   1 
ATOM   12454 O  O   . ALA B  1 695 ? -6.346  -2.333  72.517  1.00 86.59  ? 695  ALA C O   1 
ATOM   12455 C  CB  . ALA B  1 695 ? -7.559  0.334   74.014  1.00 92.13  ? 695  ALA C CB  1 
ATOM   12456 N  N   . LEU B  1 696 ? -7.774  -1.172  71.227  1.00 81.64  ? 696  LEU C N   1 
ATOM   12457 C  CA  . LEU B  1 696 ? -8.191  -2.352  70.478  1.00 88.53  ? 696  LEU C CA  1 
ATOM   12458 C  C   . LEU B  1 696 ? -7.035  -2.989  69.712  1.00 88.93  ? 696  LEU C C   1 
ATOM   12459 O  O   . LEU B  1 696 ? -6.731  -4.170  69.900  1.00 85.22  ? 696  LEU C O   1 
ATOM   12460 C  CB  . LEU B  1 696 ? -9.321  -2.017  69.502  1.00 91.11  ? 696  LEU C CB  1 
ATOM   12461 C  CG  . LEU B  1 696 ? -9.712  -3.171  68.563  1.00 88.07  ? 696  LEU C CG  1 
ATOM   12462 C  CD1 . LEU B  1 696 ? -10.051 -4.434  69.329  1.00 88.44  ? 696  LEU C CD1 1 
ATOM   12463 C  CD2 . LEU B  1 696 ? -10.880 -2.784  67.677  1.00 92.06  ? 696  LEU C CD2 1 
ATOM   12464 N  N   . LEU B  1 697 ? -6.389  -2.206  68.855  1.00 87.94  ? 697  LEU C N   1 
ATOM   12465 C  CA  . LEU B  1 697 ? -5.352  -2.743  67.979  1.00 87.89  ? 697  LEU C CA  1 
ATOM   12466 C  C   . LEU B  1 697 ? -4.139  -3.255  68.749  1.00 79.87  ? 697  LEU C C   1 
ATOM   12467 O  O   . LEU B  1 697 ? -3.484  -4.191  68.312  1.00 78.67  ? 697  LEU C O   1 
ATOM   12468 C  CB  . LEU B  1 697 ? -4.922  -1.685  66.968  1.00 89.43  ? 697  LEU C CB  1 
ATOM   12469 C  CG  . LEU B  1 697 ? -6.093  -1.049  66.213  1.00 94.12  ? 697  LEU C CG  1 
ATOM   12470 C  CD1 . LEU B  1 697 ? -5.604  -0.011  65.219  1.00 91.09  ? 697  LEU C CD1 1 
ATOM   12471 C  CD2 . LEU B  1 697 ? -6.937  -2.106  65.519  1.00 82.80  ? 697  LEU C CD2 1 
ATOM   12472 N  N   . GLU B  1 698 ? -3.855  -2.642  69.894  1.00 83.12  ? 698  GLU C N   1 
ATOM   12473 C  CA  . GLU B  1 698 ? -2.736  -3.055  70.748  1.00 86.40  ? 698  GLU C CA  1 
ATOM   12474 C  C   . GLU B  1 698 ? -2.881  -4.508  71.207  1.00 81.13  ? 698  GLU C C   1 
ATOM   12475 O  O   . GLU B  1 698 ? -1.892  -5.240  71.327  1.00 74.93  ? 698  GLU C O   1 
ATOM   12476 C  CB  . GLU B  1 698 ? -2.619  -2.121  71.965  1.00 83.26  ? 698  GLU C CB  1 
ATOM   12477 C  CG  . GLU B  1 698 ? -1.683  -2.613  73.079  1.00 78.89  ? 698  GLU C CG  1 
ATOM   12478 C  CD  . GLU B  1 698 ? -0.209  -2.624  72.683  1.00 79.30  ? 698  GLU C CD  1 
ATOM   12479 O  OE1 . GLU B  1 698 ? 0.149   -2.001  71.662  1.00 82.43  ? 698  GLU C OE1 1 
ATOM   12480 O  OE2 . GLU B  1 698 ? 0.600   -3.255  73.401  1.00 81.35  ? 698  GLU C OE2 1 
ATOM   12481 N  N   . GLY B  1 699 ? -4.119  -4.916  71.467  1.00 82.16  ? 699  GLY C N   1 
ATOM   12482 C  CA  . GLY B  1 699 ? -4.400  -6.297  71.806  1.00 83.46  ? 699  GLY C CA  1 
ATOM   12483 C  C   . GLY B  1 699 ? -4.492  -7.141  70.553  1.00 80.59  ? 699  GLY C C   1 
ATOM   12484 O  O   . GLY B  1 699 ? -3.990  -8.261  70.509  1.00 76.78  ? 699  GLY C O   1 
ATOM   12485 N  N   . LEU B  1 700 ? -5.131  -6.591  69.527  1.00 80.30  ? 700  LEU C N   1 
ATOM   12486 C  CA  . LEU B  1 700 ? -5.176  -7.241  68.224  1.00 79.92  ? 700  LEU C CA  1 
ATOM   12487 C  C   . LEU B  1 700 ? -3.782  -7.597  67.730  1.00 76.61  ? 700  LEU C C   1 
ATOM   12488 O  O   . LEU B  1 700 ? -3.559  -8.687  67.213  1.00 78.26  ? 700  LEU C O   1 
ATOM   12489 C  CB  . LEU B  1 700 ? -5.867  -6.345  67.197  1.00 78.97  ? 700  LEU C CB  1 
ATOM   12490 C  CG  . LEU B  1 700 ? -7.330  -6.005  67.464  1.00 84.16  ? 700  LEU C CG  1 
ATOM   12491 C  CD1 . LEU B  1 700 ? -7.978  -5.426  66.228  1.00 83.17  ? 700  LEU C CD1 1 
ATOM   12492 C  CD2 . LEU B  1 700 ? -8.088  -7.230  67.941  1.00 86.38  ? 700  LEU C CD2 1 
ATOM   12493 N  N   . SER B  1 701 ? -2.847  -6.669  67.901  1.00 76.01  ? 701  SER C N   1 
ATOM   12494 C  CA  . SER B  1 701 ? -1.495  -6.823  67.377  1.00 77.95  ? 701  SER C CA  1 
ATOM   12495 C  C   . SER B  1 701 ? -0.792  -8.015  67.992  1.00 75.74  ? 701  SER C C   1 
ATOM   12496 O  O   . SER B  1 701 ? -0.181  -8.830  67.297  1.00 74.26  ? 701  SER C O   1 
ATOM   12497 C  CB  . SER B  1 701 ? -0.675  -5.570  67.649  1.00 72.65  ? 701  SER C CB  1 
ATOM   12498 O  OG  . SER B  1 701 ? -0.347  -5.505  69.024  1.00 76.56  ? 701  SER C OG  1 
ATOM   12499 N  N   . TYR B  1 702 ? -0.875  -8.088  69.314  1.00 80.34  ? 702  TYR C N   1 
ATOM   12500 C  CA  . TYR B  1 702 ? -0.264  -9.161  70.077  1.00 77.76  ? 702  TYR C CA  1 
ATOM   12501 C  C   . TYR B  1 702 ? -0.722  -10.540 69.612  1.00 77.36  ? 702  TYR C C   1 
ATOM   12502 O  O   . TYR B  1 702 ? 0.089   -11.457 69.509  1.00 78.31  ? 702  TYR C O   1 
ATOM   12503 C  CB  . TYR B  1 702 ? -0.571  -8.977  71.556  1.00 76.87  ? 702  TYR C CB  1 
ATOM   12504 C  CG  . TYR B  1 702 ? 0.454   -8.159  72.288  1.00 75.21  ? 702  TYR C CG  1 
ATOM   12505 C  CD1 . TYR B  1 702 ? 1.734   -8.657  72.502  1.00 76.99  ? 702  TYR C CD1 1 
ATOM   12506 C  CD2 . TYR B  1 702 ? 0.142   -6.905  72.783  1.00 69.16  ? 702  TYR C CD2 1 
ATOM   12507 C  CE1 . TYR B  1 702 ? 2.678   -7.920  73.180  1.00 74.08  ? 702  TYR C CE1 1 
ATOM   12508 C  CE2 . TYR B  1 702 ? 1.076   -6.160  73.466  1.00 72.43  ? 702  TYR C CE2 1 
ATOM   12509 C  CZ  . TYR B  1 702 ? 2.345   -6.669  73.663  1.00 77.19  ? 702  TYR C CZ  1 
ATOM   12510 O  OH  . TYR B  1 702 ? 3.288   -5.930  74.347  1.00 80.54  ? 702  TYR C OH  1 
ATOM   12511 N  N   . LEU B  1 703 ? -2.017  -10.679 69.330  1.00 75.73  ? 703  LEU C N   1 
ATOM   12512 C  CA  . LEU B  1 703 ? -2.568  -11.932 68.807  1.00 78.85  ? 703  LEU C CA  1 
ATOM   12513 C  C   . LEU B  1 703 ? -2.032  -12.239 67.414  1.00 77.95  ? 703  LEU C C   1 
ATOM   12514 O  O   . LEU B  1 703 ? -1.673  -13.374 67.106  1.00 80.79  ? 703  LEU C O   1 
ATOM   12515 C  CB  . LEU B  1 703 ? -4.100  -11.881 68.774  1.00 79.22  ? 703  LEU C CB  1 
ATOM   12516 C  CG  . LEU B  1 703 ? -4.802  -11.942 70.134  1.00 83.42  ? 703  LEU C CG  1 
ATOM   12517 C  CD1 . LEU B  1 703 ? -6.321  -11.777 70.012  1.00 82.89  ? 703  LEU C CD1 1 
ATOM   12518 C  CD2 . LEU B  1 703 ? -4.446  -13.242 70.852  1.00 76.24  ? 703  LEU C CD2 1 
ATOM   12519 N  N   . GLU B  1 704 ? -1.979  -11.214 66.574  1.00 79.07  ? 704  GLU C N   1 
ATOM   12520 C  CA  . GLU B  1 704 ? -1.499  -11.370 65.213  1.00 80.78  ? 704  GLU C CA  1 
ATOM   12521 C  C   . GLU B  1 704 ? -0.023  -11.776 65.191  1.00 78.04  ? 704  GLU C C   1 
ATOM   12522 O  O   . GLU B  1 704 ? 0.412   -12.550 64.334  1.00 71.91  ? 704  GLU C O   1 
ATOM   12523 C  CB  . GLU B  1 704 ? -1.718  -10.073 64.439  1.00 81.14  ? 704  GLU C CB  1 
ATOM   12524 C  CG  . GLU B  1 704 ? -1.616  -10.233 62.941  1.00 76.67  ? 704  GLU C CG  1 
ATOM   12525 C  CD  . GLU B  1 704 ? -0.527  -9.372  62.359  1.00 85.75  ? 704  GLU C CD  1 
ATOM   12526 O  OE1 . GLU B  1 704 ? -0.269  -8.283  62.924  1.00 89.26  ? 704  GLU C OE1 1 
ATOM   12527 O  OE2 . GLU B  1 704 ? 0.073   -9.788  61.344  1.00 88.68  ? 704  GLU C OE2 1 
ATOM   12528 N  N   . SER B  1 705 ? 0.738   -11.249 66.146  1.00 80.14  ? 705  SER C N   1 
ATOM   12529 C  CA  . SER B  1 705 ? 2.138   -11.611 66.294  1.00 79.76  ? 705  SER C CA  1 
ATOM   12530 C  C   . SER B  1 705 ? 2.272   -13.100 66.573  1.00 78.26  ? 705  SER C C   1 
ATOM   12531 O  O   . SER B  1 705 ? 3.108   -13.773 65.972  1.00 79.89  ? 705  SER C O   1 
ATOM   12532 C  CB  . SER B  1 705 ? 2.793   -10.801 67.414  1.00 78.90  ? 705  SER C CB  1 
ATOM   12533 O  OG  . SER B  1 705 ? 4.109   -11.269 67.673  1.00 87.00  ? 705  SER C OG  1 
ATOM   12534 N  N   . PHE B  1 706 ? 1.440   -13.604 67.486  1.00 84.56  ? 706  PHE C N   1 
ATOM   12535 C  CA  . PHE B  1 706 ? 1.412   -15.030 67.831  1.00 79.81  ? 706  PHE C CA  1 
ATOM   12536 C  C   . PHE B  1 706 ? 1.203   -15.893 66.591  1.00 79.20  ? 706  PHE C C   1 
ATOM   12537 O  O   . PHE B  1 706 ? 1.859   -16.919 66.429  1.00 78.22  ? 706  PHE C O   1 
ATOM   12538 C  CB  . PHE B  1 706 ? 0.308   -15.331 68.853  1.00 77.20  ? 706  PHE C CB  1 
ATOM   12539 C  CG  . PHE B  1 706 ? 0.457   -14.596 70.146  1.00 74.49  ? 706  PHE C CG  1 
ATOM   12540 C  CD1 . PHE B  1 706 ? 1.704   -14.402 70.715  1.00 79.68  ? 706  PHE C CD1 1 
ATOM   12541 C  CD2 . PHE B  1 706 ? -0.656  -14.089 70.795  1.00 82.04  ? 706  PHE C CD2 1 
ATOM   12542 C  CE1 . PHE B  1 706 ? 1.837   -13.706 71.918  1.00 81.89  ? 706  PHE C CE1 1 
ATOM   12543 C  CE2 . PHE B  1 706 ? -0.531  -13.388 71.998  1.00 82.72  ? 706  PHE C CE2 1 
ATOM   12544 C  CZ  . PHE B  1 706 ? 0.715   -13.200 72.561  1.00 76.12  ? 706  PHE C CZ  1 
ATOM   12545 N  N   . TYR B  1 707 ? 0.288   -15.465 65.723  1.00 77.05  ? 707  TYR C N   1 
ATOM   12546 C  CA  . TYR B  1 707 ? 0.047   -16.135 64.447  1.00 83.31  ? 707  TYR C CA  1 
ATOM   12547 C  C   . TYR B  1 707 ? 1.336   -16.376 63.671  1.00 83.72  ? 707  TYR C C   1 
ATOM   12548 O  O   . TYR B  1 707 ? 1.724   -17.522 63.432  1.00 81.96  ? 707  TYR C O   1 
ATOM   12549 C  CB  . TYR B  1 707 ? -0.919  -15.310 63.592  1.00 85.66  ? 707  TYR C CB  1 
ATOM   12550 C  CG  . TYR B  1 707 ? -1.352  -15.963 62.289  1.00 87.88  ? 707  TYR C CG  1 
ATOM   12551 C  CD1 . TYR B  1 707 ? -0.516  -15.989 61.179  1.00 82.84  ? 707  TYR C CD1 1 
ATOM   12552 C  CD2 . TYR B  1 707 ? -2.616  -16.525 62.163  1.00 92.62  ? 707  TYR C CD2 1 
ATOM   12553 C  CE1 . TYR B  1 707 ? -0.920  -16.574 59.998  1.00 84.54  ? 707  TYR C CE1 1 
ATOM   12554 C  CE2 . TYR B  1 707 ? -3.025  -17.109 60.980  1.00 89.94  ? 707  TYR C CE2 1 
ATOM   12555 C  CZ  . TYR B  1 707 ? -2.175  -17.129 59.905  1.00 80.51  ? 707  TYR C CZ  1 
ATOM   12556 O  OH  . TYR B  1 707 ? -2.585  -17.707 58.732  1.00 93.99  ? 707  TYR C OH  1 
ATOM   12557 N  N   . HIS B  1 708 ? 1.995   -15.288 63.282  1.00 81.34  ? 708  HIS C N   1 
ATOM   12558 C  CA  . HIS B  1 708 ? 3.142   -15.379 62.387  1.00 82.67  ? 708  HIS C CA  1 
ATOM   12559 C  C   . HIS B  1 708 ? 4.336   -16.086 63.003  1.00 79.23  ? 708  HIS C C   1 
ATOM   12560 O  O   . HIS B  1 708 ? 5.174   -16.617 62.291  1.00 81.37  ? 708  HIS C O   1 
ATOM   12561 C  CB  . HIS B  1 708 ? 3.553   -13.989 61.926  1.00 78.22  ? 708  HIS C CB  1 
ATOM   12562 C  CG  . HIS B  1 708 ? 2.532   -13.320 61.063  1.00 76.10  ? 708  HIS C CG  1 
ATOM   12563 N  ND1 . HIS B  1 708 ? 2.242   -13.748 59.784  1.00 75.44  ? 708  HIS C ND1 1 
ATOM   12564 C  CD2 . HIS B  1 708 ? 1.730   -12.255 61.295  1.00 77.37  ? 708  HIS C CD2 1 
ATOM   12565 C  CE1 . HIS B  1 708 ? 1.308   -12.971 59.264  1.00 79.20  ? 708  HIS C CE1 1 
ATOM   12566 N  NE2 . HIS B  1 708 ? 0.979   -12.058 60.161  1.00 74.00  ? 708  HIS C NE2 1 
ATOM   12567 N  N   . MET B  1 709 ? 4.419   -16.089 64.325  1.00 81.21  ? 709  MET C N   1 
ATOM   12568 C  CA  . MET B  1 709 ? 5.493   -16.815 64.980  1.00 84.80  ? 709  MET C CA  1 
ATOM   12569 C  C   . MET B  1 709 ? 5.281   -18.301 64.785  1.00 84.32  ? 709  MET C C   1 
ATOM   12570 O  O   . MET B  1 709 ? 6.227   -19.042 64.546  1.00 84.65  ? 709  MET C O   1 
ATOM   12571 C  CB  . MET B  1 709 ? 5.570   -16.485 66.469  1.00 81.70  ? 709  MET C CB  1 
ATOM   12572 C  CG  . MET B  1 709 ? 6.670   -17.252 67.184  1.00 79.66  ? 709  MET C CG  1 
ATOM   12573 S  SD  . MET B  1 709 ? 7.209   -16.453 68.701  1.00 93.50  ? 709  MET C SD  1 
ATOM   12574 C  CE  . MET B  1 709 ? 7.670   -14.843 68.053  1.00 91.95  ? 709  MET C CE  1 
ATOM   12575 N  N   . MET B  1 710 ? 4.028   -18.728 64.889  1.00 88.18  ? 710  MET C N   1 
ATOM   12576 C  CA  . MET B  1 710 ? 3.676   -20.123 64.651  1.00 89.66  ? 710  MET C CA  1 
ATOM   12577 C  C   . MET B  1 710 ? 3.802   -20.432 63.170  1.00 89.60  ? 710  MET C C   1 
ATOM   12578 O  O   . MET B  1 710 ? 4.364   -21.450 62.783  1.00 90.49  ? 710  MET C O   1 
ATOM   12579 C  CB  . MET B  1 710 ? 2.251   -20.426 65.135  1.00 87.66  ? 710  MET C CB  1 
ATOM   12580 C  CG  . MET B  1 710 ? 1.935   -20.000 66.572  1.00 85.18  ? 710  MET C CG  1 
ATOM   12581 S  SD  . MET B  1 710 ? 2.720   -20.967 67.886  1.00 93.72  ? 710  MET C SD  1 
ATOM   12582 C  CE  . MET B  1 710 ? 4.347   -20.218 68.032  1.00 87.11  ? 710  MET C CE  1 
ATOM   12583 N  N   . ASP B  1 711 ? 3.289   -19.522 62.352  1.00 89.75  ? 711  ASP C N   1 
ATOM   12584 C  CA  . ASP B  1 711 ? 3.225   -19.711 60.910  1.00 89.75  ? 711  ASP C CA  1 
ATOM   12585 C  C   . ASP B  1 711 ? 4.591   -19.578 60.216  1.00 93.01  ? 711  ASP C C   1 
ATOM   12586 O  O   . ASP B  1 711 ? 4.762   -20.058 59.092  1.00 94.35  ? 711  ASP C O   1 
ATOM   12587 C  CB  . ASP B  1 711 ? 2.224   -18.719 60.315  1.00 85.43  ? 711  ASP C CB  1 
ATOM   12588 C  CG  . ASP B  1 711 ? 1.763   -19.122 58.941  1.00 87.34  ? 711  ASP C CG  1 
ATOM   12589 O  OD1 . ASP B  1 711 ? 2.094   -20.246 58.522  1.00 91.10  ? 711  ASP C OD1 1 
ATOM   12590 O  OD2 . ASP B  1 711 ? 1.068   -18.324 58.280  1.00 91.35  ? 711  ASP C OD2 1 
ATOM   12591 N  N   . ARG B  1 712 ? 5.557   -18.934 60.874  1.00 93.86  ? 712  ARG C N   1 
ATOM   12592 C  CA  . ARG B  1 712 ? 6.941   -18.907 60.378  1.00 95.99  ? 712  ARG C CA  1 
ATOM   12593 C  C   . ARG B  1 712 ? 7.497   -20.312 60.464  1.00 96.25  ? 712  ARG C C   1 
ATOM   12594 O  O   . ARG B  1 712 ? 8.182   -20.797 59.558  1.00 94.46  ? 712  ARG C O   1 
ATOM   12595 C  CB  . ARG B  1 712 ? 7.817   -17.949 61.184  1.00 89.19  ? 712  ARG C CB  1 
ATOM   12596 C  CG  . ARG B  1 712 ? 8.152   -16.666 60.468  1.00 87.23  ? 712  ARG C CG  1 
ATOM   12597 C  CD  . ARG B  1 712 ? 9.085   -15.815 61.311  1.00 85.91  ? 712  ARG C CD  1 
ATOM   12598 N  NE  . ARG B  1 712 ? 8.387   -15.158 62.405  1.00 83.06  ? 712  ARG C NE  1 
ATOM   12599 C  CZ  . ARG B  1 712 ? 7.734   -14.009 62.281  1.00 83.21  ? 712  ARG C CZ  1 
ATOM   12600 N  NH1 . ARG B  1 712 ? 7.692   -13.398 61.103  1.00 83.28  ? 712  ARG C NH1 1 
ATOM   12601 N  NH2 . ARG B  1 712 ? 7.121   -13.474 63.331  1.00 77.43  ? 712  ARG C NH2 1 
ATOM   12602 N  N   . ARG B  1 713 ? 7.196   -20.944 61.590  1.00 89.53  ? 713  ARG C N   1 
ATOM   12603 C  CA  . ARG B  1 713 ? 7.322   -22.374 61.730  1.00 92.05  ? 713  ARG C CA  1 
ATOM   12604 C  C   . ARG B  1 713 ? 6.122   -23.014 61.032  1.00 95.79  ? 713  ARG C C   1 
ATOM   12605 O  O   . ARG B  1 713 ? 5.324   -22.316 60.417  1.00 94.66  ? 713  ARG C O   1 
ATOM   12606 C  CB  . ARG B  1 713 ? 7.370   -22.752 63.195  1.00 91.57  ? 713  ARG C CB  1 
ATOM   12607 C  CG  . ARG B  1 713 ? 8.273   -21.878 64.039  1.00 82.96  ? 713  ARG C CG  1 
ATOM   12608 C  CD  . ARG B  1 713 ? 8.190   -22.417 65.442  1.00 85.77  ? 713  ARG C CD  1 
ATOM   12609 N  NE  . ARG B  1 713 ? 9.278   -22.059 66.342  1.00 83.21  ? 713  ARG C NE  1 
ATOM   12610 C  CZ  . ARG B  1 713 ? 10.545  -22.424 66.193  1.00 78.08  ? 713  ARG C CZ  1 
ATOM   12611 N  NH1 . ARG B  1 713 ? 10.930  -23.118 65.130  1.00 75.36  ? 713  ARG C NH1 1 
ATOM   12612 N  NH2 . ARG B  1 713 ? 11.436  -22.057 67.106  1.00 72.89  ? 713  ARG C NH2 1 
ATOM   12613 N  N   . ASN B  1 714 ? 5.968   -24.329 61.124  1.00 101.46 ? 714  ASN C N   1 
ATOM   12614 C  CA  . ASN B  1 714 ? 4.864   -24.978 60.418  1.00 98.70  ? 714  ASN C CA  1 
ATOM   12615 C  C   . ASN B  1 714 ? 3.743   -25.396 61.380  1.00 94.40  ? 714  ASN C C   1 
ATOM   12616 O  O   . ASN B  1 714 ? 2.765   -26.018 60.958  1.00 86.85  ? 714  ASN C O   1 
ATOM   12617 C  CB  . ASN B  1 714 ? 5.375   -26.184 59.606  1.00 102.69 ? 714  ASN C CB  1 
ATOM   12618 C  CG  . ASN B  1 714 ? 6.441   -25.796 58.568  1.00 106.55 ? 714  ASN C CG  1 
ATOM   12619 O  OD1 . ASN B  1 714 ? 7.079   -24.752 58.684  1.00 104.75 ? 714  ASN C OD1 1 
ATOM   12620 N  ND2 . ASN B  1 714 ? 6.631   -26.643 57.553  1.00 114.07 ? 714  ASN C ND2 1 
ATOM   12621 N  N   . ILE B  1 715 ? 3.771   -24.853 62.589  1.00 92.80  ? 715  ILE C N   1 
ATOM   12622 C  CA  . ILE B  1 715 ? 2.950   -25.360 63.665  1.00 89.31  ? 715  ILE C CA  1 
ATOM   12623 C  C   . ILE B  1 715 ? 1.539   -24.892 63.409  1.00 90.46  ? 715  ILE C C   1 
ATOM   12624 O  O   . ILE B  1 715 ? 1.064   -23.909 63.959  1.00 92.48  ? 715  ILE C O   1 
ATOM   12625 C  CB  . ILE B  1 715 ? 3.395   -24.786 65.015  1.00 93.27  ? 715  ILE C CB  1 
ATOM   12626 C  CG1 . ILE B  1 715 ? 4.913   -24.636 65.058  1.00 91.26  ? 715  ILE C CG1 1 
ATOM   12627 C  CG2 . ILE B  1 715 ? 2.914   -25.664 66.155  1.00 92.40  ? 715  ILE C CG2 1 
ATOM   12628 C  CD1 . ILE B  1 715 ? 5.396   -23.643 66.089  1.00 91.16  ? 715  ILE C CD1 1 
ATOM   12629 N  N   . SER B  1 716 ? 0.888   -25.655 62.542  1.00 94.79  ? 716  SER C N   1 
ATOM   12630 C  CA  . SER B  1 716 ? -0.453  -25.405 62.044  1.00 94.29  ? 716  SER C CA  1 
ATOM   12631 C  C   . SER B  1 716 ? -1.514  -25.442 63.132  1.00 89.40  ? 716  SER C C   1 
ATOM   12632 O  O   . SER B  1 716 ? -2.514  -24.739 63.048  1.00 84.29  ? 716  SER C O   1 
ATOM   12633 C  CB  . SER B  1 716 ? -0.794  -26.393 60.927  1.00 85.58  ? 716  SER C CB  1 
ATOM   12634 O  OG  . SER B  1 716 ? -0.307  -25.935 59.682  1.00 74.65  ? 716  SER C OG  1 
ATOM   12635 N  N   . ASP B  1 717 ? -1.321  -26.297 64.128  1.00 88.94  ? 717  ASP C N   1 
ATOM   12636 C  CA  . ASP B  1 717 ? -2.348  -26.501 65.134  1.00 89.43  ? 717  ASP C CA  1 
ATOM   12637 C  C   . ASP B  1 717 ? -2.672  -25.211 65.875  1.00 95.34  ? 717  ASP C C   1 
ATOM   12638 O  O   . ASP B  1 717 ? -3.841  -24.886 66.065  1.00 95.17  ? 717  ASP C O   1 
ATOM   12639 C  CB  . ASP B  1 717 ? -1.883  -27.562 66.138  1.00 90.87  ? 717  ASP C CB  1 
ATOM   12640 C  CG  . ASP B  1 717 ? -2.769  -27.636 67.368  1.00 94.30  ? 717  ASP C CG  1 
ATOM   12641 O  OD1 . ASP B  1 717 ? -3.993  -27.472 67.210  1.00 95.46  ? 717  ASP C OD1 1 
ATOM   12642 O  OD2 . ASP B  1 717 ? -2.245  -27.831 68.482  1.00 85.27  ? 717  ASP C OD2 1 
ATOM   12643 N  N   . ILE B  1 718 ? -1.653  -24.464 66.276  1.00 92.14  ? 718  ILE C N   1 
ATOM   12644 C  CA  . ILE B  1 718 ? -1.901  -23.215 66.976  1.00 94.51  ? 718  ILE C CA  1 
ATOM   12645 C  C   . ILE B  1 718 ? -2.217  -22.091 65.986  1.00 94.21  ? 718  ILE C C   1 
ATOM   12646 O  O   . ILE B  1 718 ? -2.976  -21.175 66.306  1.00 96.80  ? 718  ILE C O   1 
ATOM   12647 C  CB  . ILE B  1 718 ? -0.701  -22.842 67.882  1.00 99.13  ? 718  ILE C CB  1 
ATOM   12648 C  CG1 . ILE B  1 718 ? -0.504  -23.925 68.953  1.00 98.37  ? 718  ILE C CG1 1 
ATOM   12649 C  CG2 . ILE B  1 718 ? -0.912  -21.473 68.548  1.00 92.06  ? 718  ILE C CG2 1 
ATOM   12650 C  CD1 . ILE B  1 718 ? 0.933   -24.351 69.172  1.00 92.82  ? 718  ILE C CD1 1 
ATOM   12651 N  N   . SER B  1 719 ? -1.680  -22.179 64.774  1.00 87.33  ? 719  SER C N   1 
ATOM   12652 C  CA  . SER B  1 719 ? -1.920  -21.130 63.794  1.00 89.14  ? 719  SER C CA  1 
ATOM   12653 C  C   . SER B  1 719 ? -3.400  -21.034 63.401  1.00 92.41  ? 719  SER C C   1 
ATOM   12654 O  O   . SER B  1 719 ? -3.993  -19.953 63.464  1.00 90.10  ? 719  SER C O   1 
ATOM   12655 C  CB  . SER B  1 719 ? -1.058  -21.351 62.554  1.00 91.29  ? 719  SER C CB  1 
ATOM   12656 O  OG  . SER B  1 719 ? -1.523  -22.462 61.810  1.00 99.17  ? 719  SER C OG  1 
ATOM   12657 N  N   . GLU B  1 720 ? -3.998  -22.161 63.009  1.00 96.08  ? 720  GLU C N   1 
ATOM   12658 C  CA  A GLU B  1 720 ? -5.384  -22.129 62.544  0.37 94.80  ? 720  GLU C CA  1 
ATOM   12659 C  CA  B GLU B  1 720 ? -5.400  -22.223 62.578  0.63 94.88  ? 720  GLU C CA  1 
ATOM   12660 C  C   . GLU B  1 720 ? -6.356  -21.781 63.678  1.00 93.13  ? 720  GLU C C   1 
ATOM   12661 O  O   . GLU B  1 720 ? -7.366  -21.115 63.433  1.00 92.23  ? 720  GLU C O   1 
ATOM   12662 C  CB  A GLU B  1 720 ? -5.772  -23.460 61.879  0.37 93.02  ? 720  GLU C CB  1 
ATOM   12663 C  CB  B GLU B  1 720 ? -5.765  -23.648 62.141  0.63 93.13  ? 720  GLU C CB  1 
ATOM   12664 C  CG  A GLU B  1 720 ? -5.777  -24.677 62.789  0.37 91.14  ? 720  GLU C CG  1 
ATOM   12665 C  CG  B GLU B  1 720 ? -4.991  -24.166 60.954  0.63 90.59  ? 720  GLU C CG  1 
ATOM   12666 C  CD  A GLU B  1 720 ? -5.946  -25.973 62.017  0.37 87.80  ? 720  GLU C CD  1 
ATOM   12667 C  CD  B GLU B  1 720 ? -5.291  -23.392 59.707  0.63 89.36  ? 720  GLU C CD  1 
ATOM   12668 O  OE1 A GLU B  1 720 ? -7.090  -26.311 61.648  0.37 87.59  ? 720  GLU C OE1 1 
ATOM   12669 O  OE1 B GLU B  1 720 ? -6.449  -22.953 59.548  0.63 90.58  ? 720  GLU C OE1 1 
ATOM   12670 O  OE2 A GLU B  1 720 ? -4.930  -26.653 61.774  0.37 85.29  ? 720  GLU C OE2 1 
ATOM   12671 O  OE2 B GLU B  1 720 ? -4.367  -23.217 58.892  0.63 94.19  ? 720  GLU C OE2 1 
ATOM   12672 N  N   . ASN B  1 721 ? -6.044  -22.197 64.903  1.00 93.86  ? 721  ASN C N   1 
ATOM   12673 C  CA  . ASN B  1 721 ? -6.859  -21.849 66.062  1.00 93.20  ? 721  ASN C CA  1 
ATOM   12674 C  C   . ASN B  1 721 ? -6.916  -20.335 66.234  1.00 95.46  ? 721  ASN C C   1 
ATOM   12675 O  O   . ASN B  1 721 ? -7.978  -19.775 66.516  1.00 90.13  ? 721  ASN C O   1 
ATOM   12676 C  CB  . ASN B  1 721 ? -6.315  -22.516 67.329  1.00 92.32  ? 721  ASN C CB  1 
ATOM   12677 C  CG  . ASN B  1 721 ? -6.715  -23.983 67.437  1.00 96.72  ? 721  ASN C CG  1 
ATOM   12678 O  OD1 . ASN B  1 721 ? -7.863  -24.339 67.180  1.00 97.59  ? 721  ASN C OD1 1 
ATOM   12679 N  ND2 . ASN B  1 721 ? -5.764  -24.839 67.811  1.00 91.06  ? 721  ASN C ND2 1 
ATOM   12680 N  N   . LEU B  1 722 ? -5.772  -19.681 66.032  1.00 95.41  ? 722  LEU C N   1 
ATOM   12681 C  CA  . LEU B  1 722 ? -5.678  -18.225 66.100  1.00 91.40  ? 722  LEU C CA  1 
ATOM   12682 C  C   . LEU B  1 722 ? -6.516  -17.557 65.008  1.00 96.97  ? 722  LEU C C   1 
ATOM   12683 O  O   . LEU B  1 722 ? -7.186  -16.545 65.254  1.00 88.69  ? 722  LEU C O   1 
ATOM   12684 C  CB  . LEU B  1 722 ? -4.218  -17.786 65.994  1.00 87.34  ? 722  LEU C CB  1 
ATOM   12685 C  CG  . LEU B  1 722 ? -3.326  -18.127 67.190  1.00 91.90  ? 722  LEU C CG  1 
ATOM   12686 C  CD1 . LEU B  1 722 ? -1.855  -18.173 66.805  1.00 89.04  ? 722  LEU C CD1 1 
ATOM   12687 C  CD2 . LEU B  1 722 ? -3.540  -17.133 68.313  1.00 89.08  ? 722  LEU C CD2 1 
ATOM   12688 N  N   . LYS B  1 723 ? -6.489  -18.136 63.810  1.00 95.11  ? 723  LYS C N   1 
ATOM   12689 C  CA  . LYS B  1 723 ? -7.236  -17.601 62.675  1.00 98.27  ? 723  LYS C CA  1 
ATOM   12690 C  C   . LYS B  1 723 ? -8.750  -17.658 62.886  1.00 100.88 ? 723  LYS C C   1 
ATOM   12691 O  O   . LYS B  1 723 ? -9.451  -16.664 62.678  1.00 103.91 ? 723  LYS C O   1 
ATOM   12692 C  CB  . LYS B  1 723 ? -6.857  -18.354 61.400  1.00 99.61  ? 723  LYS C CB  1 
ATOM   12693 C  CG  . LYS B  1 723 ? -7.589  -17.893 60.155  1.00 101.10 ? 723  LYS C CG  1 
ATOM   12694 C  CD  . LYS B  1 723 ? -7.026  -18.586 58.930  1.00 105.79 ? 723  LYS C CD  1 
ATOM   12695 C  CE  . LYS B  1 723 ? -8.010  -18.555 57.775  1.00 108.88 ? 723  LYS C CE  1 
ATOM   12696 N  NZ  . LYS B  1 723 ? -7.545  -19.406 56.643  1.00 110.25 ? 723  LYS C NZ  1 
ATOM   12697 N  N   . ARG B  1 724 ? -9.242  -18.828 63.290  1.00 96.77  ? 724  ARG C N   1 
ATOM   12698 C  CA  . ARG B  1 724 ? -10.665 -19.033 63.541  1.00 100.60 ? 724  ARG C CA  1 
ATOM   12699 C  C   . ARG B  1 724 ? -11.174 -18.036 64.572  1.00 96.75  ? 724  ARG C C   1 
ATOM   12700 O  O   . ARG B  1 724 ? -12.173 -17.351 64.347  1.00 97.07  ? 724  ARG C O   1 
ATOM   12701 C  CB  . ARG B  1 724 ? -10.923 -20.478 64.009  1.00 104.88 ? 724  ARG C CB  1 
ATOM   12702 C  CG  . ARG B  1 724 ? -12.348 -20.762 64.515  1.00 100.10 ? 724  ARG C CG  1 
ATOM   12703 C  CD  . ARG B  1 724 ? -12.543 -22.233 64.905  1.00 96.88  ? 724  ARG C CD  1 
ATOM   12704 N  NE  . ARG B  1 724 ? -12.710 -23.109 63.740  1.00 106.90 ? 724  ARG C NE  1 
ATOM   12705 C  CZ  . ARG B  1 724 ? -13.758 -23.907 63.540  1.00 100.54 ? 724  ARG C CZ  1 
ATOM   12706 N  NH1 . ARG B  1 724 ? -14.743 -23.957 64.431  1.00 101.76 ? 724  ARG C NH1 1 
ATOM   12707 N  NH2 . ARG B  1 724 ? -13.819 -24.662 62.452  1.00 87.64  ? 724  ARG C NH2 1 
ATOM   12708 N  N   . TYR B  1 725 ? -10.460 -17.953 65.691  1.00 93.95  ? 725  TYR C N   1 
ATOM   12709 C  CA  . TYR B  1 725 ? -10.857 -17.111 66.811  1.00 95.61  ? 725  TYR C CA  1 
ATOM   12710 C  C   . TYR B  1 725 ? -10.981 -15.655 66.421  1.00 102.08 ? 725  TYR C C   1 
ATOM   12711 O  O   . TYR B  1 725 ? -11.921 -14.987 66.839  1.00 103.99 ? 725  TYR C O   1 
ATOM   12712 C  CB  . TYR B  1 725 ? -9.862  -17.232 67.963  1.00 95.59  ? 725  TYR C CB  1 
ATOM   12713 C  CG  . TYR B  1 725 ? -10.206 -16.362 69.154  1.00 95.80  ? 725  TYR C CG  1 
ATOM   12714 C  CD1 . TYR B  1 725 ? -11.297 -16.654 69.957  1.00 98.21  ? 725  TYR C CD1 1 
ATOM   12715 C  CD2 . TYR B  1 725 ? -9.438  -15.255 69.476  1.00 99.45  ? 725  TYR C CD2 1 
ATOM   12716 C  CE1 . TYR B  1 725 ? -11.618 -15.865 71.045  1.00 101.14 ? 725  TYR C CE1 1 
ATOM   12717 C  CE2 . TYR B  1 725 ? -9.748  -14.460 70.564  1.00 102.32 ? 725  TYR C CE2 1 
ATOM   12718 C  CZ  . TYR B  1 725 ? -10.840 -14.771 71.345  1.00 102.67 ? 725  TYR C CZ  1 
ATOM   12719 O  OH  . TYR B  1 725 ? -11.160 -13.987 72.428  1.00 102.81 ? 725  TYR C OH  1 
ATOM   12720 N  N   . LEU B  1 726 ? -10.034 -15.173 65.618  1.00 102.95 ? 726  LEU C N   1 
ATOM   12721 C  CA  . LEU B  1 726 ? -9.988  -13.762 65.226  1.00 103.14 ? 726  LEU C CA  1 
ATOM   12722 C  C   . LEU B  1 726 ? -11.076 -13.377 64.221  1.00 104.03 ? 726  LEU C C   1 
ATOM   12723 O  O   . LEU B  1 726 ? -11.502 -12.221 64.166  1.00 100.00 ? 726  LEU C O   1 
ATOM   12724 C  CB  . LEU B  1 726 ? -8.613  -13.414 64.651  1.00 97.49  ? 726  LEU C CB  1 
ATOM   12725 C  CG  . LEU B  1 726 ? -7.497  -13.216 65.675  1.00 92.31  ? 726  LEU C CG  1 
ATOM   12726 C  CD1 . LEU B  1 726 ? -6.252  -12.678 65.000  1.00 93.85  ? 726  LEU C CD1 1 
ATOM   12727 C  CD2 . LEU B  1 726 ? -7.953  -12.289 66.792  1.00 96.45  ? 726  LEU C CD2 1 
ATOM   12728 N  N   . LEU B  1 727 ? -11.521 -14.339 63.422  1.00 105.55 ? 727  LEU C N   1 
ATOM   12729 C  CA  . LEU B  1 727 ? -12.625 -14.090 62.507  1.00 107.72 ? 727  LEU C CA  1 
ATOM   12730 C  C   . LEU B  1 727 ? -13.922 -13.967 63.295  1.00 108.72 ? 727  LEU C C   1 
ATOM   12731 O  O   . LEU B  1 727 ? -14.525 -12.893 63.343  1.00 104.09 ? 727  LEU C O   1 
ATOM   12732 C  CB  . LEU B  1 727 ? -12.716 -15.199 61.465  1.00 109.01 ? 727  LEU C CB  1 
ATOM   12733 C  CG  . LEU B  1 727 ? -11.467 -15.227 60.588  1.00 108.75 ? 727  LEU C CG  1 
ATOM   12734 C  CD1 . LEU B  1 727 ? -11.536 -16.338 59.558  1.00 114.29 ? 727  LEU C CD1 1 
ATOM   12735 C  CD2 . LEU B  1 727 ? -11.287 -13.874 59.918  1.00 109.93 ? 727  LEU C CD2 1 
ATOM   12736 N  N   . GLN B  1 728 ? -14.331 -15.070 63.919  1.00 107.95 ? 728  GLN C N   1 
ATOM   12737 C  CA  . GLN B  1 728 ? -15.501 -15.088 64.788  1.00 107.23 ? 728  GLN C CA  1 
ATOM   12738 C  C   . GLN B  1 728 ? -15.391 -14.005 65.853  1.00 107.73 ? 728  GLN C C   1 
ATOM   12739 O  O   . GLN B  1 728 ? -16.062 -12.981 65.766  1.00 107.53 ? 728  GLN C O   1 
ATOM   12740 C  CB  . GLN B  1 728 ? -15.670 -16.460 65.443  1.00 105.36 ? 728  GLN C CB  1 
ATOM   12741 C  CG  . GLN B  1 728 ? -15.974 -17.592 64.470  1.00 108.99 ? 728  GLN C CG  1 
ATOM   12742 C  CD  . GLN B  1 728 ? -17.449 -17.691 64.109  1.00 108.33 ? 728  GLN C CD  1 
ATOM   12743 O  OE1 . GLN B  1 728 ? -18.070 -16.709 63.695  1.00 106.98 ? 728  GLN C OE1 1 
ATOM   12744 N  NE2 . GLN B  1 728 ? -18.018 -18.884 64.269  1.00 104.54 ? 728  GLN C NE2 1 
ATOM   12745 N  N   . TYR B  1 729 ? -14.549 -14.220 66.859  1.00 105.84 ? 729  TYR C N   1 
ATOM   12746 C  CA  . TYR B  1 729 ? -14.319 -13.173 67.846  1.00 106.09 ? 729  TYR C CA  1 
ATOM   12747 C  C   . TYR B  1 729 ? -13.608 -12.026 67.125  1.00 108.78 ? 729  TYR C C   1 
ATOM   12748 O  O   . TYR B  1 729 ? -12.497 -12.207 66.633  1.00 108.77 ? 729  TYR C O   1 
ATOM   12749 C  CB  . TYR B  1 729 ? -13.506 -13.698 69.035  1.00 103.88 ? 729  TYR C CB  1 
ATOM   12750 C  CG  . TYR B  1 729 ? -13.847 -13.044 70.361  1.00 109.11 ? 729  TYR C CG  1 
ATOM   12751 C  CD1 . TYR B  1 729 ? -14.980 -13.419 71.075  1.00 103.05 ? 729  TYR C CD1 1 
ATOM   12752 C  CD2 . TYR B  1 729 ? -13.032 -12.053 70.900  1.00 108.87 ? 729  TYR C CD2 1 
ATOM   12753 C  CE1 . TYR B  1 729 ? -15.290 -12.823 72.281  1.00 101.78 ? 729  TYR C CE1 1 
ATOM   12754 C  CE2 . TYR B  1 729 ? -13.334 -11.452 72.106  1.00 106.16 ? 729  TYR C CE2 1 
ATOM   12755 C  CZ  . TYR B  1 729 ? -14.462 -11.839 72.792  1.00 104.33 ? 729  TYR C CZ  1 
ATOM   12756 O  OH  . TYR B  1 729 ? -14.755 -11.237 73.992  1.00 94.22  ? 729  TYR C OH  1 
ATOM   12757 N  N   . PHE B  1 730 ? -14.280 -10.870 67.067  1.00 108.86 ? 730  PHE C N   1 
ATOM   12758 C  CA  . PHE B  1 730 ? -13.947 -9.700  66.227  1.00 107.13 ? 730  PHE C CA  1 
ATOM   12759 C  C   . PHE B  1 730 ? -14.492 -9.879  64.807  1.00 104.13 ? 730  PHE C C   1 
ATOM   12760 O  O   . PHE B  1 730 ? -13.830 -9.554  63.828  1.00 103.83 ? 730  PHE C O   1 
ATOM   12761 C  CB  . PHE B  1 730 ? -12.439 -9.408  66.175  1.00 101.31 ? 730  PHE C CB  1 
ATOM   12762 C  CG  . PHE B  1 730 ? -11.805 -9.230  67.526  1.00 100.48 ? 730  PHE C CG  1 
ATOM   12763 C  CD1 . PHE B  1 730 ? -12.219 -8.214  68.376  1.00 102.82 ? 730  PHE C CD1 1 
ATOM   12764 C  CD2 . PHE B  1 730 ? -10.787 -10.073 67.943  1.00 100.55 ? 730  PHE C CD2 1 
ATOM   12765 C  CE1 . PHE B  1 730 ? -11.637 -8.047  69.626  1.00 103.99 ? 730  PHE C CE1 1 
ATOM   12766 C  CE2 . PHE B  1 730 ? -10.200 -9.914  69.190  1.00 106.28 ? 730  PHE C CE2 1 
ATOM   12767 C  CZ  . PHE B  1 730 ? -10.625 -8.897  70.032  1.00 104.77 ? 730  PHE C CZ  1 
ATOM   12768 N  N   . LYS B  1 731 ? -15.708 -10.404 64.715  1.00 106.17 ? 731  LYS C N   1 
ATOM   12769 C  CA  . LYS B  1 731 ? -16.461 -10.433 63.464  1.00 105.86 ? 731  LYS C CA  1 
ATOM   12770 C  C   . LYS B  1 731 ? -17.276 -9.158  63.200  1.00 104.83 ? 731  LYS C C   1 
ATOM   12771 O  O   . LYS B  1 731 ? -17.322 -8.700  62.063  1.00 104.80 ? 731  LYS C O   1 
ATOM   12772 C  CB  . LYS B  1 731 ? -17.401 -11.639 63.440  1.00 106.33 ? 731  LYS C CB  1 
ATOM   12773 C  CG  . LYS B  1 731 ? -18.119 -11.864 62.125  1.00 110.23 ? 731  LYS C CG  1 
ATOM   12774 C  CD  . LYS B  1 731 ? -17.164 -12.351 61.056  1.00 109.52 ? 731  LYS C CD  1 
ATOM   12775 C  CE  . LYS B  1 731 ? -17.908 -12.939 59.878  1.00 101.37 ? 731  LYS C CE  1 
ATOM   12776 N  NZ  . LYS B  1 731 ? -16.992 -13.815 59.105  1.00 109.25 ? 731  LYS C NZ  1 
ATOM   12777 N  N   . PRO B  1 732 ? -17.938 -8.586  64.234  1.00 110.61 ? 732  PRO C N   1 
ATOM   12778 C  CA  . PRO B  1 732 ? -18.762 -7.406  63.934  1.00 110.58 ? 732  PRO C CA  1 
ATOM   12779 C  C   . PRO B  1 732 ? -17.965 -6.184  63.493  1.00 109.89 ? 732  PRO C C   1 
ATOM   12780 O  O   . PRO B  1 732 ? -18.543 -5.265  62.910  1.00 106.46 ? 732  PRO C O   1 
ATOM   12781 C  CB  . PRO B  1 732 ? -19.460 -7.117  65.268  1.00 109.64 ? 732  PRO C CB  1 
ATOM   12782 C  CG  . PRO B  1 732 ? -18.569 -7.710  66.294  1.00 108.57 ? 732  PRO C CG  1 
ATOM   12783 C  CD  . PRO B  1 732 ? -18.055 -8.962  65.658  1.00 111.75 ? 732  PRO C CD  1 
ATOM   12784 N  N   . VAL B  1 733 ? -16.665 -6.179  63.773  1.00 111.70 ? 733  VAL C N   1 
ATOM   12785 C  CA  . VAL B  1 733 ? -15.815 -5.030  63.479  1.00 107.93 ? 733  VAL C CA  1 
ATOM   12786 C  C   . VAL B  1 733 ? -14.967 -5.275  62.220  1.00 104.06 ? 733  VAL C C   1 
ATOM   12787 O  O   . VAL B  1 733 ? -14.449 -4.338  61.609  1.00 101.06 ? 733  VAL C O   1 
ATOM   12788 C  CB  . VAL B  1 733 ? -14.918 -4.694  64.688  1.00 106.62 ? 733  VAL C CB  1 
ATOM   12789 C  CG1 . VAL B  1 733 ? -13.829 -5.743  64.857  1.00 105.06 ? 733  VAL C CG1 1 
ATOM   12790 C  CG2 . VAL B  1 733 ? -14.334 -3.296  64.556  1.00 102.99 ? 733  VAL C CG2 1 
ATOM   12791 N  N   . ILE B  1 734 ? -14.839 -6.539  61.831  1.00 102.00 ? 734  ILE C N   1 
ATOM   12792 C  CA  . ILE B  1 734 ? -14.330 -6.871  60.510  1.00 102.54 ? 734  ILE C CA  1 
ATOM   12793 C  C   . ILE B  1 734 ? -15.380 -6.494  59.473  1.00 101.65 ? 734  ILE C C   1 
ATOM   12794 O  O   . ILE B  1 734 ? -15.105 -5.762  58.529  1.00 99.47  ? 734  ILE C O   1 
ATOM   12795 C  CB  . ILE B  1 734 ? -13.990 -8.376  60.371  1.00 106.90 ? 734  ILE C CB  1 
ATOM   12796 C  CG1 . ILE B  1 734 ? -12.641 -8.692  61.016  1.00 101.21 ? 734  ILE C CG1 1 
ATOM   12797 C  CG2 . ILE B  1 734 ? -13.978 -8.799  58.903  1.00 97.75  ? 734  ILE C CG2 1 
ATOM   12798 C  CD1 . ILE B  1 734 ? -12.225 -10.137 60.852  1.00 88.24  ? 734  ILE C CD1 1 
ATOM   12799 N  N   . ASP B  1 735 ? -16.597 -6.979  59.681  1.00 102.68 ? 735  ASP C N   1 
ATOM   12800 C  CA  . ASP B  1 735 ? -17.641 -6.907  58.670  1.00 103.01 ? 735  ASP C CA  1 
ATOM   12801 C  C   . ASP B  1 735 ? -18.098 -5.487  58.364  1.00 101.02 ? 735  ASP C C   1 
ATOM   12802 O  O   . ASP B  1 735 ? -18.539 -5.201  57.250  1.00 100.08 ? 735  ASP C O   1 
ATOM   12803 C  CB  . ASP B  1 735 ? -18.836 -7.750  59.107  1.00 104.39 ? 735  ASP C CB  1 
ATOM   12804 C  CG  . ASP B  1 735 ? -18.471 -9.205  59.322  1.00 111.55 ? 735  ASP C CG  1 
ATOM   12805 O  OD1 . ASP B  1 735 ? -17.457 -9.656  58.743  1.00 112.90 ? 735  ASP C OD1 1 
ATOM   12806 O  OD2 . ASP B  1 735 ? -19.199 -9.896  60.068  1.00 111.88 ? 735  ASP C OD2 1 
ATOM   12807 N  N   . ARG B  1 736 ? -17.993 -4.602  59.348  1.00 100.06 ? 736  ARG C N   1 
ATOM   12808 C  CA  . ARG B  1 736 ? -18.466 -3.231  59.189  1.00 99.39  ? 736  ARG C CA  1 
ATOM   12809 C  C   . ARG B  1 736 ? -17.692 -2.460  58.113  1.00 103.69 ? 736  ARG C C   1 
ATOM   12810 O  O   . ARG B  1 736 ? -18.289 -1.765  57.287  1.00 100.21 ? 736  ARG C O   1 
ATOM   12811 C  CB  . ARG B  1 736 ? -18.387 -2.485  60.527  1.00 99.52  ? 736  ARG C CB  1 
ATOM   12812 C  CG  . ARG B  1 736 ? -19.659 -2.574  61.358  1.00 103.87 ? 736  ARG C CG  1 
ATOM   12813 C  CD  . ARG B  1 736 ? -19.545 -1.821  62.680  1.00 103.93 ? 736  ARG C CD  1 
ATOM   12814 N  NE  . ARG B  1 736 ? -19.017 -2.658  63.755  1.00 106.60 ? 736  ARG C NE  1 
ATOM   12815 C  CZ  . ARG B  1 736 ? -19.165 -2.391  65.048  1.00 99.65  ? 736  ARG C CZ  1 
ATOM   12816 N  NH1 . ARG B  1 736 ? -19.835 -1.312  65.429  1.00 96.38  ? 736  ARG C NH1 1 
ATOM   12817 N  NH2 . ARG B  1 736 ? -18.650 -3.204  65.959  1.00 99.55  ? 736  ARG C NH2 1 
ATOM   12818 N  N   . GLN B  1 737 ? -16.370 -2.621  58.117  1.00 104.37 ? 737  GLN C N   1 
ATOM   12819 C  CA  . GLN B  1 737 ? -15.450 -1.820  57.305  1.00 97.49  ? 737  GLN C CA  1 
ATOM   12820 C  C   . GLN B  1 737 ? -15.779 -1.703  55.815  1.00 97.53  ? 737  GLN C C   1 
ATOM   12821 O  O   . GLN B  1 737 ? -15.837 -2.700  55.097  1.00 94.06  ? 737  GLN C O   1 
ATOM   12822 C  CB  . GLN B  1 737 ? -14.037 -2.380  57.452  1.00 98.95  ? 737  GLN C CB  1 
ATOM   12823 C  CG  . GLN B  1 737 ? -13.526 -2.385  58.885  1.00 103.46 ? 737  GLN C CG  1 
ATOM   12824 C  CD  . GLN B  1 737 ? -13.494 -0.998  59.499  1.00 99.63  ? 737  GLN C CD  1 
ATOM   12825 O  OE1 . GLN B  1 737 ? -13.330 0.004   58.800  1.00 99.16  ? 737  GLN C OE1 1 
ATOM   12826 N  NE2 . GLN B  1 737 ? -13.654 -0.933  60.814  1.00 98.65  ? 737  GLN C NE2 1 
ATOM   12827 N  N   . SER B  1 738 ? -15.970 -0.464  55.367  1.00 102.01 ? 738  SER C N   1 
ATOM   12828 C  CA  . SER B  1 738 ? -16.188 -0.153  53.957  1.00 101.16 ? 738  SER C CA  1 
ATOM   12829 C  C   . SER B  1 738 ? -14.872 -0.171  53.186  1.00 101.39 ? 738  SER C C   1 
ATOM   12830 O  O   . SER B  1 738 ? -13.801 -0.146  53.783  1.00 100.46 ? 738  SER C O   1 
ATOM   12831 C  CB  . SER B  1 738 ? -16.872 1.211   53.810  1.00 93.90  ? 738  SER C CB  1 
ATOM   12832 O  OG  . SER B  1 738 ? -16.322 2.167   54.700  1.00 87.57  ? 738  SER C OG  1 
ATOM   12833 N  N   . TRP B  1 739 ? -14.951 -0.225  51.860  1.00 102.51 ? 739  TRP C N   1 
ATOM   12834 C  CA  . TRP B  1 739 ? -13.747 -0.216  51.033  1.00 98.16  ? 739  TRP C CA  1 
ATOM   12835 C  C   . TRP B  1 739 ? -13.656 1.110   50.289  1.00 98.90  ? 739  TRP C C   1 
ATOM   12836 O  O   . TRP B  1 739 ? -13.872 1.189   49.077  1.00 94.84  ? 739  TRP C O   1 
ATOM   12837 C  CB  . TRP B  1 739 ? -13.738 -1.412  50.073  1.00 99.09  ? 739  TRP C CB  1 
ATOM   12838 C  CG  . TRP B  1 739 ? -13.486 -2.720  50.798  1.00 103.83 ? 739  TRP C CG  1 
ATOM   12839 C  CD1 . TRP B  1 739 ? -14.198 -3.221  51.850  1.00 102.90 ? 739  TRP C CD1 1 
ATOM   12840 C  CD2 . TRP B  1 739 ? -12.448 -3.674  50.532  1.00 102.31 ? 739  TRP C CD2 1 
ATOM   12841 N  NE1 . TRP B  1 739 ? -13.672 -4.423  52.252  1.00 103.94 ? 739  TRP C NE1 1 
ATOM   12842 C  CE2 . TRP B  1 739 ? -12.599 -4.726  51.458  1.00 102.62 ? 739  TRP C CE2 1 
ATOM   12843 C  CE3 . TRP B  1 739 ? -11.412 -3.745  49.600  1.00 102.76 ? 739  TRP C CE3 1 
ATOM   12844 C  CZ2 . TRP B  1 739 ? -11.752 -5.832  51.480  1.00 101.30 ? 739  TRP C CZ2 1 
ATOM   12845 C  CZ3 . TRP B  1 739 ? -10.569 -4.847  49.628  1.00 104.72 ? 739  TRP C CZ3 1 
ATOM   12846 C  CH2 . TRP B  1 739 ? -10.745 -5.872  50.561  1.00 101.62 ? 739  TRP C CH2 1 
ATOM   12847 N  N   . SER B  1 740 ? -13.341 2.153   51.054  1.00 97.65  ? 740  SER C N   1 
ATOM   12848 C  CA  . SER B  1 740 ? -13.250 3.517   50.551  1.00 91.85  ? 740  SER C CA  1 
ATOM   12849 C  C   . SER B  1 740 ? -12.318 4.327   51.437  1.00 90.07  ? 740  SER C C   1 
ATOM   12850 O  O   . SER B  1 740 ? -11.676 3.781   52.332  1.00 89.75  ? 740  SER C O   1 
ATOM   12851 C  CB  . SER B  1 740 ? -14.620 4.174   50.525  1.00 95.86  ? 740  SER C CB  1 
ATOM   12852 O  OG  . SER B  1 740 ? -15.082 4.357   51.852  1.00 92.08  ? 740  SER C OG  1 
ATOM   12853 N  N   . ASP B  1 741 ? -12.268 5.634   51.203  1.00 87.83  ? 741  ASP C N   1 
ATOM   12854 C  CA  . ASP B  1 741 ? -11.409 6.513   51.987  1.00 83.07  ? 741  ASP C CA  1 
ATOM   12855 C  C   . ASP B  1 741 ? -12.263 7.447   52.852  1.00 85.44  ? 741  ASP C C   1 
ATOM   12856 O  O   . ASP B  1 741 ? -11.802 8.500   53.296  1.00 86.05  ? 741  ASP C O   1 
ATOM   12857 C  CB  . ASP B  1 741 ? -10.473 7.315   51.067  1.00 82.22  ? 741  ASP C CB  1 
ATOM   12858 C  CG  . ASP B  1 741 ? -9.732  6.431   50.045  1.00 91.17  ? 741  ASP C CG  1 
ATOM   12859 O  OD1 . ASP B  1 741 ? -9.272  5.333   50.423  1.00 94.64  ? 741  ASP C OD1 1 
ATOM   12860 O  OD2 . ASP B  1 741 ? -9.611  6.827   48.860  1.00 86.01  ? 741  ASP C OD2 1 
ATOM   12861 N  N   . LYS B  1 742 ? -13.509 7.045   53.097  1.00 84.99  ? 742  LYS C N   1 
ATOM   12862 C  CA  . LYS B  1 742 ? -14.467 7.868   53.841  1.00 88.69  ? 742  LYS C CA  1 
ATOM   12863 C  C   . LYS B  1 742 ? -14.212 7.860   55.348  1.00 87.12  ? 742  LYS C C   1 
ATOM   12864 O  O   . LYS B  1 742 ? -13.472 7.021   55.862  1.00 89.12  ? 742  LYS C O   1 
ATOM   12865 C  CB  . LYS B  1 742 ? -15.901 7.393   53.574  1.00 86.61  ? 742  LYS C CB  1 
ATOM   12866 C  CG  . LYS B  1 742 ? -16.278 7.262   52.105  1.00 80.65  ? 742  LYS C CG  1 
ATOM   12867 C  CD  . LYS B  1 742 ? -17.660 6.642   51.952  1.00 81.60  ? 742  LYS C CD  1 
ATOM   12868 C  CE  . LYS B  1 742 ? -17.918 6.201   50.518  1.00 91.80  ? 742  LYS C CE  1 
ATOM   12869 N  NZ  . LYS B  1 742 ? -19.163 5.394   50.393  1.00 95.37  ? 742  LYS C NZ  1 
ATOM   12870 N  N   . GLY B  1 743 ? -14.841 8.790   56.055  1.00 83.98  ? 743  GLY C N   1 
ATOM   12871 C  CA  . GLY B  1 743 ? -14.720 8.846   57.499  1.00 89.48  ? 743  GLY C CA  1 
ATOM   12872 C  C   . GLY B  1 743 ? -13.489 9.591   57.977  1.00 90.49  ? 743  GLY C C   1 
ATOM   12873 O  O   . GLY B  1 743 ? -12.664 10.034  57.182  1.00 91.84  ? 743  GLY C O   1 
ATOM   12874 N  N   . SER B  1 744 ? -13.371 9.723   59.293  1.00 96.19  ? 744  SER C N   1 
ATOM   12875 C  CA  . SER B  1 744 ? -12.262 10.434  59.917  1.00 98.67  ? 744  SER C CA  1 
ATOM   12876 C  C   . SER B  1 744 ? -10.930 9.720   59.731  1.00 94.67  ? 744  SER C C   1 
ATOM   12877 O  O   . SER B  1 744 ? -10.832 8.738   59.001  1.00 95.64  ? 744  SER C O   1 
ATOM   12878 C  CB  . SER B  1 744 ? -12.534 10.628  61.413  1.00 104.06 ? 744  SER C CB  1 
ATOM   12879 O  OG  . SER B  1 744 ? -13.730 11.362  61.633  1.00 105.25 ? 744  SER C OG  1 
ATOM   12880 N  N   . VAL B  1 745 ? -9.903  10.220  60.406  1.00 92.55  ? 745  VAL C N   1 
ATOM   12881 C  CA  . VAL B  1 745 ? -8.565  9.672   60.253  1.00 94.65  ? 745  VAL C CA  1 
ATOM   12882 C  C   . VAL B  1 745 ? -8.461  8.302   60.905  1.00 97.94  ? 745  VAL C C   1 
ATOM   12883 O  O   . VAL B  1 745 ? -8.025  7.345   60.266  1.00 95.62  ? 745  VAL C O   1 
ATOM   12884 C  CB  . VAL B  1 745 ? -7.501  10.609  60.844  1.00 97.94  ? 745  VAL C CB  1 
ATOM   12885 C  CG1 . VAL B  1 745 ? -6.148  9.927   60.848  1.00 91.36  ? 745  VAL C CG1 1 
ATOM   12886 C  CG2 . VAL B  1 745 ? -7.442  11.907  60.044  1.00 93.36  ? 745  VAL C CG2 1 
ATOM   12887 N  N   . TRP B  1 746 ? -8.868  8.207   62.172  1.00 106.00 ? 746  TRP C N   1 
ATOM   12888 C  CA  . TRP B  1 746 ? -8.918  6.911   62.852  1.00 104.72 ? 746  TRP C CA  1 
ATOM   12889 C  C   . TRP B  1 746 ? -9.898  6.007   62.130  1.00 101.34 ? 746  TRP C C   1 
ATOM   12890 O  O   . TRP B  1 746 ? -9.731  4.791   62.122  1.00 104.02 ? 746  TRP C O   1 
ATOM   12891 C  CB  . TRP B  1 746 ? -9.319  7.040   64.331  1.00 106.03 ? 746  TRP C CB  1 
ATOM   12892 C  CG  . TRP B  1 746 ? -8.160  6.898   65.309  1.00 109.68 ? 746  TRP C CG  1 
ATOM   12893 C  CD1 . TRP B  1 746 ? -7.750  7.820   66.228  1.00 110.04 ? 746  TRP C CD1 1 
ATOM   12894 C  CD2 . TRP B  1 746 ? -7.271  5.774   65.454  1.00 106.30 ? 746  TRP C CD2 1 
ATOM   12895 N  NE1 . TRP B  1 746 ? -6.664  7.348   66.933  1.00 108.67 ? 746  TRP C NE1 1 
ATOM   12896 C  CE2 . TRP B  1 746 ? -6.351  6.095   66.477  1.00 103.50 ? 746  TRP C CE2 1 
ATOM   12897 C  CE3 . TRP B  1 746 ? -7.162  4.534   64.819  1.00 98.77  ? 746  TRP C CE3 1 
ATOM   12898 C  CZ2 . TRP B  1 746 ? -5.340  5.224   66.876  1.00 94.83  ? 746  TRP C CZ2 1 
ATOM   12899 C  CZ3 . TRP B  1 746 ? -6.157  3.671   65.219  1.00 95.79  ? 746  TRP C CZ3 1 
ATOM   12900 C  CH2 . TRP B  1 746 ? -5.261  4.020   66.238  1.00 95.32  ? 746  TRP C CH2 1 
ATOM   12901 N  N   . ASP B  1 747 ? -10.922 6.605   61.529  1.00 96.96  ? 747  ASP C N   1 
ATOM   12902 C  CA  . ASP B  1 747 ? -11.851 5.846   60.708  1.00 98.64  ? 747  ASP C CA  1 
ATOM   12903 C  C   . ASP B  1 747 ? -11.104 5.204   59.543  1.00 99.23  ? 747  ASP C C   1 
ATOM   12904 O  O   . ASP B  1 747 ? -11.221 4.002   59.303  1.00 96.30  ? 747  ASP C O   1 
ATOM   12905 C  CB  . ASP B  1 747 ? -12.978 6.737   60.186  1.00 100.46 ? 747  ASP C CB  1 
ATOM   12906 C  CG  . ASP B  1 747 ? -14.083 6.949   61.206  1.00 107.19 ? 747  ASP C CG  1 
ATOM   12907 O  OD1 . ASP B  1 747 ? -13.856 6.691   62.409  1.00 107.87 ? 747  ASP C OD1 1 
ATOM   12908 O  OD2 . ASP B  1 747 ? -15.184 7.381   60.799  1.00 107.26 ? 747  ASP C OD2 1 
ATOM   12909 N  N   . ARG B  1 748 ? -10.325 6.017   58.835  1.00 99.86  ? 748  ARG C N   1 
ATOM   12910 C  CA  . ARG B  1 748 ? -9.607  5.564   57.648  1.00 97.13  ? 748  ARG C CA  1 
ATOM   12911 C  C   . ARG B  1 748 ? -8.600  4.463   57.969  1.00 95.62  ? 748  ARG C C   1 
ATOM   12912 O  O   . ARG B  1 748 ? -8.641  3.376   57.387  1.00 96.11  ? 748  ARG C O   1 
ATOM   12913 C  CB  . ARG B  1 748 ? -8.891  6.741   56.975  1.00 95.23  ? 748  ARG C CB  1 
ATOM   12914 C  CG  . ARG B  1 748 ? -9.805  7.663   56.182  1.00 92.15  ? 748  ARG C CG  1 
ATOM   12915 C  CD  . ARG B  1 748 ? -9.018  8.695   55.370  1.00 90.26  ? 748  ARG C CD  1 
ATOM   12916 N  NE  . ARG B  1 748 ? -8.198  8.094   54.317  1.00 81.17  ? 748  ARG C NE  1 
ATOM   12917 C  CZ  . ARG B  1 748 ? -7.765  8.753   53.245  1.00 86.26  ? 748  ARG C CZ  1 
ATOM   12918 N  NH1 . ARG B  1 748 ? -8.079  10.032  53.079  1.00 91.57  ? 748  ARG C NH1 1 
ATOM   12919 N  NH2 . ARG B  1 748 ? -7.023  8.139   52.333  1.00 83.15  ? 748  ARG C NH2 1 
ATOM   12920 N  N   . MET B  1 749 ? -7.698  4.755   58.898  1.00 97.02  ? 749  MET C N   1 
ATOM   12921 C  CA  . MET B  1 749 ? -6.629  3.829   59.237  1.00 98.51  ? 749  MET C CA  1 
ATOM   12922 C  C   . MET B  1 749 ? -7.169  2.477   59.675  1.00 97.29  ? 749  MET C C   1 
ATOM   12923 O  O   . MET B  1 749 ? -6.816  1.451   59.095  1.00 96.82  ? 749  MET C O   1 
ATOM   12924 C  CB  . MET B  1 749 ? -5.741  4.424   60.327  1.00 93.63  ? 749  MET C CB  1 
ATOM   12925 C  CG  . MET B  1 749 ? -4.873  5.561   59.831  1.00 90.80  ? 749  MET C CG  1 
ATOM   12926 S  SD  . MET B  1 749 ? -3.483  5.844   60.934  1.00 111.20 ? 749  MET C SD  1 
ATOM   12927 C  CE  . MET B  1 749 ? -2.796  4.191   61.041  1.00 84.63  ? 749  MET C CE  1 
ATOM   12928 N  N   . LEU B  1 750 ? -8.044  2.494   60.677  1.00 98.76  ? 750  LEU C N   1 
ATOM   12929 C  CA  . LEU B  1 750 ? -8.624  1.284   61.264  1.00 98.65  ? 750  LEU C CA  1 
ATOM   12930 C  C   . LEU B  1 750 ? -9.065  0.262   60.226  1.00 96.91  ? 750  LEU C C   1 
ATOM   12931 O  O   . LEU B  1 750 ? -8.976  -0.945  60.458  1.00 96.80  ? 750  LEU C O   1 
ATOM   12932 C  CB  . LEU B  1 750 ? -9.817  1.653   62.149  1.00 104.37 ? 750  LEU C CB  1 
ATOM   12933 C  CG  . LEU B  1 750 ? -10.559 0.506   62.840  1.00 104.67 ? 750  LEU C CG  1 
ATOM   12934 C  CD1 . LEU B  1 750 ? -9.693  -0.113  63.924  1.00 100.95 ? 750  LEU C CD1 1 
ATOM   12935 C  CD2 . LEU B  1 750 ? -11.894 0.980   63.405  1.00 98.46  ? 750  LEU C CD2 1 
ATOM   12936 N  N   . ARG B  1 751 ? -9.528  0.764   59.083  1.00 95.76  ? 751  ARG C N   1 
ATOM   12937 C  CA  . ARG B  1 751 ? -9.994  -0.065  57.978  1.00 94.94  ? 751  ARG C CA  1 
ATOM   12938 C  C   . ARG B  1 751 ? -8.831  -0.742  57.253  1.00 98.04  ? 751  ARG C C   1 
ATOM   12939 O  O   . ARG B  1 751 ? -8.909  -1.916  56.877  1.00 94.77  ? 751  ARG C O   1 
ATOM   12940 C  CB  . ARG B  1 751 ? -10.818 0.785   57.002  1.00 96.75  ? 751  ARG C CB  1 
ATOM   12941 C  CG  . ARG B  1 751 ? -10.542 0.527   55.531  1.00 96.54  ? 751  ARG C CG  1 
ATOM   12942 C  CD  . ARG B  1 751 ? -11.390 1.420   54.644  1.00 93.65  ? 751  ARG C CD  1 
ATOM   12943 N  NE  . ARG B  1 751 ? -11.507 2.775   55.172  1.00 93.19  ? 751  ARG C NE  1 
ATOM   12944 C  CZ  . ARG B  1 751 ? -12.634 3.476   55.179  1.00 89.88  ? 751  ARG C CZ  1 
ATOM   12945 N  NH1 . ARG B  1 751 ? -13.748 2.952   54.689  1.00 96.50  ? 751  ARG C NH1 1 
ATOM   12946 N  NH2 . ARG B  1 751 ? -12.649 4.702   55.674  1.00 90.93  ? 751  ARG C NH2 1 
ATOM   12947 N  N   . SER B  1 752 ? -7.744  0.000   57.069  1.00 99.31  ? 752  SER C N   1 
ATOM   12948 C  CA  . SER B  1 752 ? -6.585  -0.531  56.368  1.00 95.85  ? 752  SER C CA  1 
ATOM   12949 C  C   . SER B  1 752 ? -5.805  -1.466  57.264  1.00 90.04  ? 752  SER C C   1 
ATOM   12950 O  O   . SER B  1 752 ? -4.974  -2.229  56.799  1.00 91.96  ? 752  SER C O   1 
ATOM   12951 C  CB  . SER B  1 752 ? -5.676  0.594   55.884  1.00 97.05  ? 752  SER C CB  1 
ATOM   12952 O  OG  . SER B  1 752 ? -4.581  0.064   55.156  1.00 107.71 ? 752  SER C OG  1 
ATOM   12953 N  N   . ALA B  1 753 ? -6.070  -1.380  58.559  1.00 94.60  ? 753  ALA C N   1 
ATOM   12954 C  CA  . ALA B  1 753 ? -5.386  -2.195  59.543  1.00 87.48  ? 753  ALA C CA  1 
ATOM   12955 C  C   . ALA B  1 753 ? -6.125  -3.494  59.690  1.00 89.40  ? 753  ALA C C   1 
ATOM   12956 O  O   . ALA B  1 753 ? -5.536  -4.529  59.986  1.00 92.57  ? 753  ALA C O   1 
ATOM   12957 C  CB  . ALA B  1 753 ? -5.309  -1.480  60.861  1.00 87.08  ? 753  ALA C CB  1 
ATOM   12958 N  N   . LEU B  1 754 ? -7.431  -3.423  59.474  1.00 96.51  ? 754  LEU C N   1 
ATOM   12959 C  CA  . LEU B  1 754 ? -8.294  -4.587  59.585  1.00 99.82  ? 754  LEU C CA  1 
ATOM   12960 C  C   . LEU B  1 754 ? -8.334  -5.364  58.278  1.00 95.88  ? 754  LEU C C   1 
ATOM   12961 O  O   . LEU B  1 754 ? -8.187  -6.581  58.278  1.00 98.73  ? 754  LEU C O   1 
ATOM   12962 C  CB  . LEU B  1 754 ? -9.707  -4.167  60.005  1.00 100.25 ? 754  LEU C CB  1 
ATOM   12963 C  CG  . LEU B  1 754 ? -9.956  -3.970  61.506  1.00 99.40  ? 754  LEU C CG  1 
ATOM   12964 C  CD1 . LEU B  1 754 ? -11.228 -3.178  61.751  1.00 99.30  ? 754  LEU C CD1 1 
ATOM   12965 C  CD2 . LEU B  1 754 ? -10.038 -5.314  62.206  1.00 97.71  ? 754  LEU C CD2 1 
ATOM   12966 N  N   . LEU B  1 755 ? -8.526  -4.665  57.163  1.00 97.21  ? 755  LEU C N   1 
ATOM   12967 C  CA  . LEU B  1 755 ? -8.628  -5.334  55.868  1.00 98.75  ? 755  LEU C CA  1 
ATOM   12968 C  C   . LEU B  1 755 ? -7.294  -5.948  55.457  1.00 100.89 ? 755  LEU C C   1 
ATOM   12969 O  O   . LEU B  1 755 ? -7.245  -6.888  54.662  1.00 100.83 ? 755  LEU C O   1 
ATOM   12970 C  CB  . LEU B  1 755 ? -9.112  -4.363  54.796  1.00 98.62  ? 755  LEU C CB  1 
ATOM   12971 C  CG  . LEU B  1 755 ? -10.551 -3.872  54.927  1.00 99.96  ? 755  LEU C CG  1 
ATOM   12972 C  CD1 . LEU B  1 755 ? -10.861 -2.830  53.860  1.00 105.17 ? 755  LEU C CD1 1 
ATOM   12973 C  CD2 . LEU B  1 755 ? -11.509 -5.038  54.828  1.00 98.18  ? 755  LEU C CD2 1 
ATOM   12974 N  N   . LYS B  1 756 ? -6.210  -5.405  55.998  1.00 102.55 ? 756  LYS C N   1 
ATOM   12975 C  CA  . LYS B  1 756 ? -4.897  -6.010  55.831  1.00 102.02 ? 756  LYS C CA  1 
ATOM   12976 C  C   . LYS B  1 756 ? -4.871  -7.311  56.613  1.00 103.55 ? 756  LYS C C   1 
ATOM   12977 O  O   . LYS B  1 756 ? -4.262  -8.293  56.197  1.00 104.57 ? 756  LYS C O   1 
ATOM   12978 C  CB  . LYS B  1 756 ? -3.793  -5.065  56.310  1.00 98.79  ? 756  LYS C CB  1 
ATOM   12979 C  CG  . LYS B  1 756 ? -2.393  -5.632  56.219  1.00 102.06 ? 756  LYS C CG  1 
ATOM   12980 C  CD  . LYS B  1 756 ? -2.136  -6.260  54.861  1.00 104.90 ? 756  LYS C CD  1 
ATOM   12981 C  CE  . LYS B  1 756 ? -0.708  -6.726  54.777  1.00 101.84 ? 756  LYS C CE  1 
ATOM   12982 N  NZ  . LYS B  1 756 ? -0.255  -7.241  56.099  1.00 99.47  ? 756  LYS C NZ  1 
ATOM   12983 N  N   . LEU B  1 757 ? -5.558  -7.303  57.749  1.00 104.44 ? 757  LEU C N   1 
ATOM   12984 C  CA  . LEU B  1 757 ? -5.611  -8.457  58.632  1.00 101.84 ? 757  LEU C CA  1 
ATOM   12985 C  C   . LEU B  1 757 ? -6.557  -9.523  58.093  1.00 101.27 ? 757  LEU C C   1 
ATOM   12986 O  O   . LEU B  1 757 ? -6.290  -10.715 58.206  1.00 99.27  ? 757  LEU C O   1 
ATOM   12987 C  CB  . LEU B  1 757 ? -6.036  -8.020  60.030  1.00 95.75  ? 757  LEU C CB  1 
ATOM   12988 C  CG  . LEU B  1 757 ? -6.104  -9.115  61.087  1.00 101.98 ? 757  LEU C CG  1 
ATOM   12989 C  CD1 . LEU B  1 757 ? -4.795  -9.888  61.155  1.00 98.26  ? 757  LEU C CD1 1 
ATOM   12990 C  CD2 . LEU B  1 757 ? -6.439  -8.490  62.428  1.00 103.37 ? 757  LEU C CD2 1 
ATOM   12991 N  N   . ALA B  1 758 ? -7.658  -9.086  57.498  1.00 100.97 ? 758  ALA C N   1 
ATOM   12992 C  CA  . ALA B  1 758 ? -8.614  -10.008 56.906  1.00 101.28 ? 758  ALA C CA  1 
ATOM   12993 C  C   . ALA B  1 758 ? -7.989  -10.749 55.732  1.00 106.52 ? 758  ALA C C   1 
ATOM   12994 O  O   . ALA B  1 758 ? -8.190  -11.948 55.565  1.00 109.20 ? 758  ALA C O   1 
ATOM   12995 C  CB  . ALA B  1 758 ? -9.861  -9.265  56.461  1.00 100.24 ? 758  ALA C CB  1 
ATOM   12996 N  N   . CYS B  1 759 ? -7.221  -10.033 54.922  1.00 109.77 ? 759  CYS C N   1 
ATOM   12997 C  CA  . CYS B  1 759 ? -6.621  -10.627 53.733  1.00 111.68 ? 759  CYS C CA  1 
ATOM   12998 C  C   . CYS B  1 759 ? -5.428  -11.499 54.081  1.00 112.41 ? 759  CYS C C   1 
ATOM   12999 O  O   . CYS B  1 759 ? -5.198  -12.527 53.444  1.00 114.59 ? 759  CYS C O   1 
ATOM   13000 C  CB  . CYS B  1 759 ? -6.193  -9.543  52.743  1.00 111.96 ? 759  CYS C CB  1 
ATOM   13001 S  SG  . CYS B  1 759 ? -7.450  -9.099  51.523  1.00 126.70 ? 759  CYS C SG  1 
ATOM   13002 N  N   . ASP B  1 760 ? -4.667  -11.084 55.089  1.00 108.95 ? 760  ASP C N   1 
ATOM   13003 C  CA  . ASP B  1 760 ? -3.458  -11.805 55.469  1.00 113.92 ? 760  ASP C CA  1 
ATOM   13004 C  C   . ASP B  1 760 ? -3.802  -13.097 56.191  1.00 113.66 ? 760  ASP C C   1 
ATOM   13005 O  O   . ASP B  1 760 ? -2.942  -13.958 56.392  1.00 112.41 ? 760  ASP C O   1 
ATOM   13006 C  CB  . ASP B  1 760 ? -2.554  -10.933 56.343  1.00 108.79 ? 760  ASP C CB  1 
ATOM   13007 C  CG  . ASP B  1 760 ? -1.605  -10.071 55.525  1.00 115.17 ? 760  ASP C CG  1 
ATOM   13008 O  OD1 . ASP B  1 760 ? -1.880  -9.836  54.322  1.00 113.01 ? 760  ASP C OD1 1 
ATOM   13009 O  OD2 . ASP B  1 760 ? -0.581  -9.629  56.091  1.00 114.83 ? 760  ASP C OD2 1 
ATOM   13010 N  N   . LEU B  1 761 ? -5.065  -13.228 56.581  1.00 111.20 ? 761  LEU C N   1 
ATOM   13011 C  CA  . LEU B  1 761 ? -5.534  -14.457 57.199  1.00 108.61 ? 761  LEU C CA  1 
ATOM   13012 C  C   . LEU B  1 761 ? -6.061  -15.436 56.155  1.00 113.19 ? 761  LEU C C   1 
ATOM   13013 O  O   . LEU B  1 761 ? -6.025  -16.641 56.383  1.00 116.69 ? 761  LEU C O   1 
ATOM   13014 C  CB  . LEU B  1 761 ? -6.619  -14.159 58.234  1.00 106.37 ? 761  LEU C CB  1 
ATOM   13015 C  CG  . LEU B  1 761 ? -6.132  -13.544 59.548  1.00 103.28 ? 761  LEU C CG  1 
ATOM   13016 C  CD1 . LEU B  1 761 ? -7.272  -13.387 60.536  1.00 99.63  ? 761  LEU C CD1 1 
ATOM   13017 C  CD2 . LEU B  1 761 ? -5.029  -14.385 60.141  1.00 98.59  ? 761  LEU C CD2 1 
ATOM   13018 N  N   . ASN B  1 762 ? -6.506  -14.892 55.016  1.00 111.62 ? 762  ASN C N   1 
ATOM   13019 C  CA  . ASN B  1 762 ? -7.250  -15.591 53.946  1.00 113.11 ? 762  ASN C CA  1 
ATOM   13020 C  C   . ASN B  1 762 ? -8.740  -15.683 54.277  1.00 116.03 ? 762  ASN C C   1 
ATOM   13021 O  O   . ASN B  1 762 ? -9.210  -16.661 54.860  1.00 115.22 ? 762  ASN C O   1 
ATOM   13022 C  CB  . ASN B  1 762 ? -6.693  -16.993 53.651  1.00 112.24 ? 762  ASN C CB  1 
ATOM   13023 C  CG  . ASN B  1 762 ? -5.454  -16.961 52.784  1.00 116.37 ? 762  ASN C CG  1 
ATOM   13024 O  OD1 . ASN B  1 762 ? -5.507  -16.548 51.624  1.00 116.76 ? 762  ASN C OD1 1 
ATOM   13025 N  ND2 . ASN B  1 762 ? -4.329  -17.409 53.337  1.00 116.57 ? 762  ASN C ND2 1 
ATOM   13026 N  N   . HIS B  1 763 ? -9.472  -14.646 53.879  1.00 116.09 ? 763  HIS C N   1 
ATOM   13027 C  CA  . HIS B  1 763 ? -10.885 -14.486 54.200  1.00 113.71 ? 763  HIS C CA  1 
ATOM   13028 C  C   . HIS B  1 763 ? -11.634 -14.140 52.916  1.00 110.66 ? 763  HIS C C   1 
ATOM   13029 O  O   . HIS B  1 763 ? -11.311 -13.151 52.266  1.00 113.24 ? 763  HIS C O   1 
ATOM   13030 C  CB  . HIS B  1 763 ? -11.057 -13.388 55.262  1.00 112.01 ? 763  HIS C CB  1 
ATOM   13031 C  CG  . HIS B  1 763 ? -12.290 -13.521 56.104  1.00 113.08 ? 763  HIS C CG  1 
ATOM   13032 N  ND1 . HIS B  1 763 ? -13.149 -12.467 56.335  1.00 116.58 ? 763  HIS C ND1 1 
ATOM   13033 C  CD2 . HIS B  1 763 ? -12.798 -14.575 56.787  1.00 116.40 ? 763  HIS C CD2 1 
ATOM   13034 C  CE1 . HIS B  1 763 ? -14.137 -12.868 57.116  1.00 115.57 ? 763  HIS C CE1 1 
ATOM   13035 N  NE2 . HIS B  1 763 ? -13.948 -14.143 57.405  1.00 116.02 ? 763  HIS C NE2 1 
ATOM   13036 N  N   . ALA B  1 764 ? -12.616 -14.963 52.553  1.00 106.90 ? 764  ALA C N   1 
ATOM   13037 C  CA  . ALA B  1 764 ? -13.339 -14.827 51.283  1.00 108.80 ? 764  ALA C CA  1 
ATOM   13038 C  C   . ALA B  1 764 ? -13.827 -13.408 50.955  1.00 114.38 ? 764  ALA C C   1 
ATOM   13039 O  O   . ALA B  1 764 ? -13.659 -12.959 49.815  1.00 114.48 ? 764  ALA C O   1 
ATOM   13040 C  CB  . ALA B  1 764 ? -14.517 -15.795 51.246  1.00 106.70 ? 764  ALA C CB  1 
ATOM   13041 N  N   . PRO B  1 765 ? -14.437 -12.698 51.929  1.00 118.50 ? 765  PRO C N   1 
ATOM   13042 C  CA  . PRO B  1 765 ? -14.857 -11.328 51.598  1.00 118.96 ? 765  PRO C CA  1 
ATOM   13043 C  C   . PRO B  1 765 ? -13.703 -10.410 51.194  1.00 117.98 ? 765  PRO C C   1 
ATOM   13044 O  O   . PRO B  1 765 ? -13.785 -9.763  50.147  1.00 117.68 ? 765  PRO C O   1 
ATOM   13045 C  CB  . PRO B  1 765 ? -15.503 -10.832 52.900  1.00 120.16 ? 765  PRO C CB  1 
ATOM   13046 C  CG  . PRO B  1 765 ? -15.937 -12.066 53.600  1.00 114.70 ? 765  PRO C CG  1 
ATOM   13047 C  CD  . PRO B  1 765 ? -14.885 -13.084 53.281  1.00 113.45 ? 765  PRO C CD  1 
ATOM   13048 N  N   . CYS B  1 766 ? -12.649 -10.363 52.007  1.00 116.49 ? 766  CYS C N   1 
ATOM   13049 C  CA  . CYS B  1 766 ? -11.503 -9.498  51.732  1.00 116.71 ? 766  CYS C CA  1 
ATOM   13050 C  C   . CYS B  1 766 ? -10.830 -9.847  50.403  1.00 116.66 ? 766  CYS C C   1 
ATOM   13051 O  O   . CYS B  1 766 ? -10.720 -9.000  49.511  1.00 117.23 ? 766  CYS C O   1 
ATOM   13052 C  CB  . CYS B  1 766 ? -10.479 -9.579  52.870  1.00 115.64 ? 766  CYS C CB  1 
ATOM   13053 S  SG  . CYS B  1 766 ? -9.025  -8.489  52.657  1.00 122.62 ? 766  CYS C SG  1 
ATOM   13054 N  N   . ILE B  1 767 ? -10.391 -11.095 50.277  1.00 115.04 ? 767  ILE C N   1 
ATOM   13055 C  CA  . ILE B  1 767 ? -9.656  -11.540 49.100  1.00 109.49 ? 767  ILE C CA  1 
ATOM   13056 C  C   . ILE B  1 767 ? -10.417 -11.286 47.802  1.00 106.89 ? 767  ILE C C   1 
ATOM   13057 O  O   . ILE B  1 767 ? -9.839  -10.819 46.824  1.00 108.06 ? 767  ILE C O   1 
ATOM   13058 C  CB  . ILE B  1 767 ? -9.317  -13.028 49.202  1.00 103.64 ? 767  ILE C CB  1 
ATOM   13059 C  CG1 . ILE B  1 767 ? -8.507  -13.293 50.472  1.00 108.21 ? 767  ILE C CG1 1 
ATOM   13060 C  CG2 . ILE B  1 767 ? -8.557  -13.480 47.979  1.00 100.01 ? 767  ILE C CG2 1 
ATOM   13061 C  CD1 . ILE B  1 767 ? -7.171  -12.583 50.514  1.00 110.27 ? 767  ILE C CD1 1 
ATOM   13062 N  N   . GLN B  1 768 ? -11.715 -11.572 47.796  1.00 106.93 ? 768  GLN C N   1 
ATOM   13063 C  CA  . GLN B  1 768 ? -12.509 -11.400 46.584  1.00 108.74 ? 768  GLN C CA  1 
ATOM   13064 C  C   . GLN B  1 768 ? -12.787 -9.926  46.264  1.00 111.85 ? 768  GLN C C   1 
ATOM   13065 O  O   . GLN B  1 768 ? -12.760 -9.530  45.094  1.00 111.38 ? 768  GLN C O   1 
ATOM   13066 C  CB  . GLN B  1 768 ? -13.828 -12.173 46.688  1.00 109.38 ? 768  GLN C CB  1 
ATOM   13067 C  CG  . GLN B  1 768 ? -14.840 -11.858 45.575  1.00 112.12 ? 768  GLN C CG  1 
ATOM   13068 C  CD  . GLN B  1 768 ? -14.301 -12.099 44.164  1.00 111.88 ? 768  GLN C CD  1 
ATOM   13069 O  OE1 . GLN B  1 768 ? -13.360 -12.870 43.962  1.00 108.62 ? 768  GLN C OE1 1 
ATOM   13070 N  NE2 . GLN B  1 768 ? -14.906 -11.434 43.179  1.00 110.69 ? 768  GLN C NE2 1 
ATOM   13071 N  N   . LYS B  1 769 ? -13.055 -9.116  47.287  1.00 109.77 ? 769  LYS C N   1 
ATOM   13072 C  CA  . LYS B  1 769 ? -13.287 -7.687  47.070  1.00 107.29 ? 769  LYS C CA  1 
ATOM   13073 C  C   . LYS B  1 769 ? -12.002 -7.028  46.584  1.00 107.41 ? 769  LYS C C   1 
ATOM   13074 O  O   . LYS B  1 769 ? -12.030 -6.070  45.810  1.00 105.82 ? 769  LYS C O   1 
ATOM   13075 C  CB  . LYS B  1 769 ? -13.793 -7.005  48.344  1.00 102.55 ? 769  LYS C CB  1 
ATOM   13076 C  CG  . LYS B  1 769 ? -14.074 -5.504  48.199  1.00 102.44 ? 769  LYS C CG  1 
ATOM   13077 C  CD  . LYS B  1 769 ? -15.049 -5.197  47.061  1.00 99.01  ? 769  LYS C CD  1 
ATOM   13078 C  CE  . LYS B  1 769 ? -15.490 -3.735  47.069  1.00 96.00  ? 769  LYS C CE  1 
ATOM   13079 N  NZ  . LYS B  1 769 ? -16.420 -3.415  45.945  1.00 87.45  ? 769  LYS C NZ  1 
ATOM   13080 N  N   . ALA B  1 770 ? -10.873 -7.557  47.041  1.00 106.12 ? 770  ALA C N   1 
ATOM   13081 C  CA  . ALA B  1 770 ? -9.580  -7.111  46.555  1.00 103.51 ? 770  ALA C CA  1 
ATOM   13082 C  C   . ALA B  1 770 ? -9.405  -7.532  45.103  1.00 103.08 ? 770  ALA C C   1 
ATOM   13083 O  O   . ALA B  1 770 ? -9.138  -6.701  44.238  1.00 107.06 ? 770  ALA C O   1 
ATOM   13084 C  CB  . ALA B  1 770 ? -8.462  -7.675  47.416  1.00 100.46 ? 770  ALA C CB  1 
ATOM   13085 N  N   . ALA B  1 771 ? -9.569  -8.826  44.848  1.00 101.67 ? 771  ALA C N   1 
ATOM   13086 C  CA  . ALA B  1 771 ? -9.389  -9.388  43.518  1.00 101.48 ? 771  ALA C CA  1 
ATOM   13087 C  C   . ALA B  1 771 ? -10.248 -8.668  42.492  1.00 104.84 ? 771  ALA C C   1 
ATOM   13088 O  O   . ALA B  1 771 ? -9.810  -8.420  41.366  1.00 103.37 ? 771  ALA C O   1 
ATOM   13089 C  CB  . ALA B  1 771 ? -9.709  -10.872 43.526  1.00 99.72  ? 771  ALA C CB  1 
ATOM   13090 N  N   . GLU B  1 772 ? -11.470 -8.323  42.890  1.00 105.41 ? 772  GLU C N   1 
ATOM   13091 C  CA  . GLU B  1 772 ? -12.385 -7.633  41.990  1.00 113.23 ? 772  GLU C CA  1 
ATOM   13092 C  C   . GLU B  1 772 ? -11.844 -6.241  41.683  1.00 113.87 ? 772  GLU C C   1 
ATOM   13093 O  O   . GLU B  1 772 ? -11.814 -5.823  40.521  1.00 113.74 ? 772  GLU C O   1 
ATOM   13094 C  CB  . GLU B  1 772 ? -13.794 -7.545  42.587  1.00 111.73 ? 772  GLU C CB  1 
ATOM   13095 C  CG  . GLU B  1 772 ? -14.905 -7.641  41.546  1.00 113.28 ? 772  GLU C CG  1 
ATOM   13096 C  CD  . GLU B  1 772 ? -16.213 -7.044  42.025  1.00 116.60 ? 772  GLU C CD  1 
ATOM   13097 O  OE1 . GLU B  1 772 ? -16.173 -6.090  42.830  1.00 116.34 ? 772  GLU C OE1 1 
ATOM   13098 O  OE2 . GLU B  1 772 ? -17.281 -7.527  41.593  1.00 116.69 ? 772  GLU C OE2 1 
ATOM   13099 N  N   . LEU B  1 773 ? -11.400 -5.547  42.733  1.00 111.44 ? 773  LEU C N   1 
ATOM   13100 C  CA  . LEU B  1 773 ? -10.835 -4.197  42.632  1.00 106.01 ? 773  LEU C CA  1 
ATOM   13101 C  C   . LEU B  1 773 ? -9.531  -4.145  41.834  1.00 104.05 ? 773  LEU C C   1 
ATOM   13102 O  O   . LEU B  1 773 ? -9.330  -3.236  41.033  1.00 100.80 ? 773  LEU C O   1 
ATOM   13103 C  CB  . LEU B  1 773 ? -10.595 -3.620  44.029  1.00 100.43 ? 773  LEU C CB  1 
ATOM   13104 C  CG  . LEU B  1 773 ? -11.661 -2.695  44.610  1.00 97.00  ? 773  LEU C CG  1 
ATOM   13105 C  CD1 . LEU B  1 773 ? -13.038 -3.319  44.490  1.00 106.50 ? 773  LEU C CD1 1 
ATOM   13106 C  CD2 . LEU B  1 773 ? -11.340 -2.378  46.057  1.00 92.85  ? 773  LEU C CD2 1 
ATOM   13107 N  N   . PHE B  1 774 ? -8.644  -5.110  42.067  1.00 102.62 ? 774  PHE C N   1 
ATOM   13108 C  CA  . PHE B  1 774 ? -7.391  -5.189  41.322  1.00 104.25 ? 774  PHE C CA  1 
ATOM   13109 C  C   . PHE B  1 774 ? -7.681  -5.370  39.839  1.00 107.48 ? 774  PHE C C   1 
ATOM   13110 O  O   . PHE B  1 774 ? -7.035  -4.756  38.988  1.00 108.87 ? 774  PHE C O   1 
ATOM   13111 C  CB  . PHE B  1 774 ? -6.512  -6.338  41.839  1.00 101.42 ? 774  PHE C CB  1 
ATOM   13112 C  CG  . PHE B  1 774 ? -5.141  -6.390  41.207  1.00 101.18 ? 774  PHE C CG  1 
ATOM   13113 C  CD1 . PHE B  1 774 ? -4.153  -5.492  41.582  1.00 98.08  ? 774  PHE C CD1 1 
ATOM   13114 C  CD2 . PHE B  1 774 ? -4.839  -7.341  40.245  1.00 97.64  ? 774  PHE C CD2 1 
ATOM   13115 C  CE1 . PHE B  1 774 ? -2.893  -5.537  41.002  1.00 92.74  ? 774  PHE C CE1 1 
ATOM   13116 C  CE2 . PHE B  1 774 ? -3.579  -7.392  39.670  1.00 93.60  ? 774  PHE C CE2 1 
ATOM   13117 C  CZ  . PHE B  1 774 ? -2.607  -6.486  40.049  1.00 87.71  ? 774  PHE C CZ  1 
ATOM   13118 N  N   . SER B  1 775 ? -8.665  -6.209  39.536  1.00 110.09 ? 775  SER C N   1 
ATOM   13119 C  CA  . SER B  1 775 ? -9.054  -6.457  38.156  1.00 110.37 ? 775  SER C CA  1 
ATOM   13120 C  C   . SER B  1 775 ? -9.591  -5.190  37.493  1.00 110.44 ? 775  SER C C   1 
ATOM   13121 O  O   . SER B  1 775 ? -9.103  -4.783  36.441  1.00 111.69 ? 775  SER C O   1 
ATOM   13122 C  CB  . SER B  1 775 ? -10.091 -7.574  38.095  1.00 106.52 ? 775  SER C CB  1 
ATOM   13123 O  OG  . SER B  1 775 ? -9.563  -8.760  38.658  1.00 102.63 ? 775  SER C OG  1 
ATOM   13124 N  N   . GLN B  1 776 ? -10.570 -4.550  38.125  1.00 108.30 ? 776  GLN C N   1 
ATOM   13125 C  CA  . GLN B  1 776 ? -11.242 -3.398  37.526  1.00 110.95 ? 776  GLN C CA  1 
ATOM   13126 C  C   . GLN B  1 776 ? -10.332 -2.170  37.354  1.00 111.03 ? 776  GLN C C   1 
ATOM   13127 O  O   . GLN B  1 776 ? -10.683 -1.226  36.646  1.00 113.73 ? 776  GLN C O   1 
ATOM   13128 C  CB  . GLN B  1 776 ? -12.478 -3.027  38.355  1.00 117.18 ? 776  GLN C CB  1 
ATOM   13129 C  CG  . GLN B  1 776 ? -13.521 -4.151  38.449  1.00 121.61 ? 776  GLN C CG  1 
ATOM   13130 C  CD  . GLN B  1 776 ? -14.843 -3.692  39.049  1.00 124.82 ? 776  GLN C CD  1 
ATOM   13131 O  OE1 . GLN B  1 776 ? -15.656 -3.061  38.373  1.00 129.34 ? 776  GLN C OE1 1 
ATOM   13132 N  NE2 . GLN B  1 776 ? -15.064 -4.011  40.323  1.00 118.72 ? 776  GLN C NE2 1 
ATOM   13133 N  N   . TRP B  1 777 ? -9.164  -2.189  37.987  1.00 110.37 ? 777  TRP C N   1 
ATOM   13134 C  CA  . TRP B  1 777 ? -8.186  -1.114  37.832  1.00 108.47 ? 777  TRP C CA  1 
ATOM   13135 C  C   . TRP B  1 777 ? -7.144  -1.503  36.784  1.00 106.95 ? 777  TRP C C   1 
ATOM   13136 O  O   . TRP B  1 777 ? -6.701  -0.670  35.993  1.00 106.20 ? 777  TRP C O   1 
ATOM   13137 C  CB  . TRP B  1 777 ? -7.528  -0.798  39.184  1.00 108.68 ? 777  TRP C CB  1 
ATOM   13138 C  CG  . TRP B  1 777 ? -6.229  -0.020  39.135  1.00 105.66 ? 777  TRP C CG  1 
ATOM   13139 C  CD1 . TRP B  1 777 ? -6.078  1.344   39.112  1.00 103.58 ? 777  TRP C CD1 1 
ATOM   13140 C  CD2 . TRP B  1 777 ? -4.904  -0.568  39.147  1.00 100.83 ? 777  TRP C CD2 1 
ATOM   13141 N  NE1 . TRP B  1 777 ? -4.742  1.671   39.090  1.00 101.40 ? 777  TRP C NE1 1 
ATOM   13142 C  CE2 . TRP B  1 777 ? -4.002  0.516   39.110  1.00 102.04 ? 777  TRP C CE2 1 
ATOM   13143 C  CE3 . TRP B  1 777 ? -4.394  -1.872  39.174  1.00 94.79  ? 777  TRP C CE3 1 
ATOM   13144 C  CZ2 . TRP B  1 777 ? -2.621  0.334   39.097  1.00 95.81  ? 777  TRP C CZ2 1 
ATOM   13145 C  CZ3 . TRP B  1 777 ? -3.025  -2.051  39.163  1.00 89.81  ? 777  TRP C CZ3 1 
ATOM   13146 C  CH2 . TRP B  1 777 ? -2.154  -0.953  39.124  1.00 93.83  ? 777  TRP C CH2 1 
ATOM   13147 N  N   . MET B  1 778 ? -6.771  -2.779  36.778  1.00 102.96 ? 778  MET C N   1 
ATOM   13148 C  CA  . MET B  1 778 ? -5.804  -3.291  35.817  1.00 102.29 ? 778  MET C CA  1 
ATOM   13149 C  C   . MET B  1 778 ? -6.423  -3.420  34.428  1.00 107.74 ? 778  MET C C   1 
ATOM   13150 O  O   . MET B  1 778 ? -5.782  -3.107  33.424  1.00 107.30 ? 778  MET C O   1 
ATOM   13151 C  CB  . MET B  1 778 ? -5.258  -4.641  36.281  1.00 95.77  ? 778  MET C CB  1 
ATOM   13152 C  CG  . MET B  1 778 ? -4.347  -5.329  35.279  1.00 92.56  ? 778  MET C CG  1 
ATOM   13153 S  SD  . MET B  1 778 ? -3.708  -6.897  35.913  1.00 97.40  ? 778  MET C SD  1 
ATOM   13154 C  CE  . MET B  1 778 ? -2.820  -7.537  34.490  1.00 88.84  ? 778  MET C CE  1 
ATOM   13155 N  N   . GLU B  1 779 ? -7.670  -3.881  34.376  1.00 108.02 ? 779  GLU C N   1 
ATOM   13156 C  CA  . GLU B  1 779 ? -8.381  -4.025  33.112  1.00 109.46 ? 779  GLU C CA  1 
ATOM   13157 C  C   . GLU B  1 779 ? -8.550  -2.681  32.424  1.00 108.76 ? 779  GLU C C   1 
ATOM   13158 O  O   . GLU B  1 779 ? -8.460  -2.580  31.199  1.00 108.01 ? 779  GLU C O   1 
ATOM   13159 C  CB  . GLU B  1 779 ? -9.750  -4.671  33.328  1.00 111.12 ? 779  GLU C CB  1 
ATOM   13160 C  CG  . GLU B  1 779 ? -9.702  -6.152  33.670  1.00 117.05 ? 779  GLU C CG  1 
ATOM   13161 C  CD  . GLU B  1 779 ? -11.085 -6.789  33.708  1.00 125.84 ? 779  GLU C CD  1 
ATOM   13162 O  OE1 . GLU B  1 779 ? -11.702 -6.929  32.629  1.00 125.99 ? 779  GLU C OE1 1 
ATOM   13163 O  OE2 . GLU B  1 779 ? -11.553 -7.150  34.813  1.00 127.60 ? 779  GLU C OE2 1 
ATOM   13164 N  N   . SER B  1 780 ? -8.790  -1.647  33.224  1.00 107.52 ? 780  SER C N   1 
ATOM   13165 C  CA  . SER B  1 780 ? -8.963  -0.301  32.700  1.00 110.12 ? 780  SER C CA  1 
ATOM   13166 C  C   . SER B  1 780 ? -7.623  0.296   32.284  1.00 115.90 ? 780  SER C C   1 
ATOM   13167 O  O   . SER B  1 780 ? -7.573  1.349   31.645  1.00 115.40 ? 780  SER C O   1 
ATOM   13168 C  CB  . SER B  1 780 ? -9.636  0.595   33.737  1.00 109.77 ? 780  SER C CB  1 
ATOM   13169 O  OG  . SER B  1 780 ? -8.789  0.809   34.852  1.00 111.35 ? 780  SER C OG  1 
ATOM   13170 N  N   . SER B  1 781 ? -6.544  -0.394  32.653  1.00 114.83 ? 781  SER C N   1 
ATOM   13171 C  CA  . SER B  1 781 ? -5.177  0.058   32.396  1.00 113.47 ? 781  SER C CA  1 
ATOM   13172 C  C   . SER B  1 781 ? -4.881  1.365   33.143  1.00 113.41 ? 781  SER C C   1 
ATOM   13173 O  O   . SER B  1 781 ? -4.137  2.217   32.659  1.00 116.32 ? 781  SER C O   1 
ATOM   13174 C  CB  . SER B  1 781 ? -4.933  0.221   30.888  1.00 111.05 ? 781  SER C CB  1 
ATOM   13175 O  OG  . SER B  1 781 ? -5.401  -0.908  30.165  1.00 99.46  ? 781  SER C OG  1 
ATOM   13176 N  N   . GLY B  1 782 ? -5.472  1.510   34.328  1.00 113.93 ? 782  GLY C N   1 
ATOM   13177 C  CA  . GLY B  1 782 ? -5.198  2.643   35.194  1.00 109.60 ? 782  GLY C CA  1 
ATOM   13178 C  C   . GLY B  1 782 ? -6.346  3.619   35.379  1.00 111.03 ? 782  GLY C C   1 
ATOM   13179 O  O   . GLY B  1 782 ? -6.297  4.479   36.262  1.00 109.02 ? 782  GLY C O   1 
ATOM   13180 N  N   . LYS B  1 783 ? -7.383  3.488   34.556  1.00 112.62 ? 783  LYS C N   1 
ATOM   13181 C  CA  . LYS B  1 783 ? -8.459  4.477   34.519  1.00 112.58 ? 783  LYS C CA  1 
ATOM   13182 C  C   . LYS B  1 783 ? -9.227  4.570   35.837  1.00 112.59 ? 783  LYS C C   1 
ATOM   13183 O  O   . LYS B  1 783 ? -9.438  5.666   36.353  1.00 109.14 ? 783  LYS C O   1 
ATOM   13184 C  CB  . LYS B  1 783 ? -9.432  4.173   33.376  1.00 109.95 ? 783  LYS C CB  1 
ATOM   13185 C  CG  . LYS B  1 783 ? -8.790  4.089   31.993  1.00 109.60 ? 783  LYS C CG  1 
ATOM   13186 C  CD  . LYS B  1 783 ? -8.041  5.361   31.607  1.00 111.38 ? 783  LYS C CD  1 
ATOM   13187 C  CE  . LYS B  1 783 ? -7.396  5.227   30.224  1.00 109.08 ? 783  LYS C CE  1 
ATOM   13188 N  NZ  . LYS B  1 783 ? -6.720  6.481   29.767  1.00 97.89  ? 783  LYS C NZ  1 
ATOM   13189 N  N   . LEU B  1 784 ? -9.640  3.427   36.382  1.00 110.95 ? 784  LEU C N   1 
ATOM   13190 C  CA  . LEU B  1 784 ? -10.409 3.413   37.628  1.00 111.28 ? 784  LEU C CA  1 
ATOM   13191 C  C   . LEU B  1 784 ? -9.564  3.710   38.866  1.00 110.92 ? 784  LEU C C   1 
ATOM   13192 O  O   . LEU B  1 784 ? -8.350  3.500   38.881  1.00 111.93 ? 784  LEU C O   1 
ATOM   13193 C  CB  . LEU B  1 784 ? -11.110 2.067   37.817  1.00 107.75 ? 784  LEU C CB  1 
ATOM   13194 C  CG  . LEU B  1 784 ? -12.304 1.778   36.908  1.00 113.73 ? 784  LEU C CG  1 
ATOM   13195 C  CD1 . LEU B  1 784 ? -13.183 0.687   37.514  1.00 113.29 ? 784  LEU C CD1 1 
ATOM   13196 C  CD2 . LEU B  1 784 ? -13.110 3.042   36.638  1.00 112.67 ? 784  LEU C CD2 1 
ATOM   13197 N  N   . ASN B  1 785 ? -10.222 4.191   39.912  1.00 106.08 ? 785  ASN C N   1 
ATOM   13198 C  CA  . ASN B  1 785 ? -9.537  4.478   41.162  1.00 106.33 ? 785  ASN C CA  1 
ATOM   13199 C  C   . ASN B  1 785 ? -9.717  3.364   42.178  1.00 102.82 ? 785  ASN C C   1 
ATOM   13200 O  O   . ASN B  1 785 ? -10.798 2.793   42.310  1.00 104.35 ? 785  ASN C O   1 
ATOM   13201 C  CB  . ASN B  1 785 ? -10.032 5.797   41.754  1.00 104.79 ? 785  ASN C CB  1 
ATOM   13202 C  CG  . ASN B  1 785 ? -9.758  6.975   40.852  1.00 103.05 ? 785  ASN C CG  1 
ATOM   13203 O  OD1 . ASN B  1 785 ? -8.732  7.024   40.171  1.00 99.12  ? 785  ASN C OD1 1 
ATOM   13204 N  ND2 . ASN B  1 785 ? -10.677 7.934   40.836  1.00 104.67 ? 785  ASN C ND2 1 
ATOM   13205 N  N   . ILE B  1 786 ? -8.641  3.052   42.886  1.00 98.21  ? 786  ILE C N   1 
ATOM   13206 C  CA  . ILE B  1 786 ? -8.716  2.173   44.042  1.00 94.69  ? 786  ILE C CA  1 
ATOM   13207 C  C   . ILE B  1 786 ? -8.406  2.972   45.282  1.00 91.75  ? 786  ILE C C   1 
ATOM   13208 O  O   . ILE B  1 786 ? -7.306  3.491   45.408  1.00 96.61  ? 786  ILE C O   1 
ATOM   13209 C  CB  . ILE B  1 786 ? -7.728  1.023   43.961  1.00 91.28  ? 786  ILE C CB  1 
ATOM   13210 C  CG1 . ILE B  1 786 ? -8.028  0.146   42.751  1.00 92.74  ? 786  ILE C CG1 1 
ATOM   13211 C  CG2 . ILE B  1 786 ? -7.761  0.227   45.249  1.00 91.78  ? 786  ILE C CG2 1 
ATOM   13212 C  CD1 . ILE B  1 786 ? -7.130  -1.052  42.669  1.00 97.23  ? 786  ILE C CD1 1 
ATOM   13213 N  N   . PRO B  1 787 ? -9.369  3.069   46.202  1.00 87.59  ? 787  PRO C N   1 
ATOM   13214 C  CA  . PRO B  1 787 ? -9.239  3.897   47.407  1.00 91.22  ? 787  PRO C CA  1 
ATOM   13215 C  C   . PRO B  1 787 ? -7.876  3.743   48.079  1.00 87.64  ? 787  PRO C C   1 
ATOM   13216 O  O   . PRO B  1 787 ? -7.350  2.637   48.190  1.00 86.09  ? 787  PRO C O   1 
ATOM   13217 C  CB  . PRO B  1 787 ? -10.363 3.380   48.302  1.00 92.76  ? 787  PRO C CB  1 
ATOM   13218 C  CG  . PRO B  1 787 ? -11.401 2.913   47.338  1.00 97.12  ? 787  PRO C CG  1 
ATOM   13219 C  CD  . PRO B  1 787 ? -10.639 2.329   46.173  1.00 91.76  ? 787  PRO C CD  1 
ATOM   13220 N  N   . THR B  1 788 ? -7.302  4.864   48.491  1.00 85.86  ? 788  THR C N   1 
ATOM   13221 C  CA  . THR B  1 788 ? -5.932  4.886   48.984  1.00 85.14  ? 788  THR C CA  1 
ATOM   13222 C  C   . THR B  1 788 ? -5.744  4.032   50.237  1.00 81.92  ? 788  THR C C   1 
ATOM   13223 O  O   . THR B  1 788 ? -4.679  3.462   50.457  1.00 85.14  ? 788  THR C O   1 
ATOM   13224 C  CB  . THR B  1 788 ? -5.483  6.324   49.289  1.00 80.44  ? 788  THR C CB  1 
ATOM   13225 O  OG1 . THR B  1 788 ? -6.121  6.782   50.489  1.00 76.88  ? 788  THR C OG1 1 
ATOM   13226 C  CG2 . THR B  1 788 ? -5.846  7.242   48.138  1.00 76.22  ? 788  THR C CG2 1 
ATOM   13227 N  N   . ASP B  1 789 ? -6.782  3.940   51.055  1.00 84.09  ? 789  ASP C N   1 
ATOM   13228 C  CA  . ASP B  1 789 ? -6.702  3.165   52.285  1.00 85.13  ? 789  ASP C CA  1 
ATOM   13229 C  C   . ASP B  1 789 ? -6.599  1.676   51.999  1.00 84.26  ? 789  ASP C C   1 
ATOM   13230 O  O   . ASP B  1 789 ? -6.201  0.898   52.856  1.00 83.82  ? 789  ASP C O   1 
ATOM   13231 C  CB  . ASP B  1 789 ? -7.914  3.439   53.171  1.00 81.53  ? 789  ASP C CB  1 
ATOM   13232 C  CG  . ASP B  1 789 ? -7.945  4.862   53.696  1.00 83.75  ? 789  ASP C CG  1 
ATOM   13233 O  OD1 . ASP B  1 789 ? -6.937  5.582   53.543  1.00 85.96  ? 789  ASP C OD1 1 
ATOM   13234 O  OD2 . ASP B  1 789 ? -8.976  5.260   54.278  1.00 86.69  ? 789  ASP C OD2 1 
ATOM   13235 N  N   . VAL B  1 790 ? -6.952  1.280   50.786  1.00 80.46  ? 790  VAL C N   1 
ATOM   13236 C  CA  . VAL B  1 790 ? -6.992  -0.130  50.455  1.00 82.93  ? 790  VAL C CA  1 
ATOM   13237 C  C   . VAL B  1 790 ? -5.892  -0.485  49.477  1.00 83.93  ? 790  VAL C C   1 
ATOM   13238 O  O   . VAL B  1 790 ? -5.591  -1.655  49.264  1.00 84.98  ? 790  VAL C O   1 
ATOM   13239 C  CB  . VAL B  1 790 ? -8.350  -0.523  49.849  1.00 87.38  ? 790  VAL C CB  1 
ATOM   13240 C  CG1 . VAL B  1 790 ? -8.566  -2.009  49.994  1.00 93.05  ? 790  VAL C CG1 1 
ATOM   13241 C  CG2 . VAL B  1 790 ? -9.465  0.228   50.535  1.00 87.90  ? 790  VAL C CG2 1 
ATOM   13242 N  N   . LEU B  1 791 ? -5.284  0.541   48.898  1.00 85.73  ? 791  LEU C N   1 
ATOM   13243 C  CA  . LEU B  1 791 ? -4.383  0.374   47.764  1.00 83.16  ? 791  LEU C CA  1 
ATOM   13244 C  C   . LEU B  1 791 ? -3.328  -0.715  47.954  1.00 74.31  ? 791  LEU C C   1 
ATOM   13245 O  O   . LEU B  1 791 ? -3.156  -1.581  47.097  1.00 73.56  ? 791  LEU C O   1 
ATOM   13246 C  CB  . LEU B  1 791 ? -3.700  1.708   47.465  1.00 84.28  ? 791  LEU C CB  1 
ATOM   13247 C  CG  . LEU B  1 791 ? -3.037  1.792   46.095  1.00 78.95  ? 791  LEU C CG  1 
ATOM   13248 C  CD1 . LEU B  1 791 ? -3.959  1.209   45.050  1.00 83.26  ? 791  LEU C CD1 1 
ATOM   13249 C  CD2 . LEU B  1 791 ? -2.719  3.234   45.773  1.00 82.03  ? 791  LEU C CD2 1 
ATOM   13250 N  N   . LYS B  1 792 ? -2.634  -0.672  49.085  1.00 74.32  ? 792  LYS C N   1 
ATOM   13251 C  CA  . LYS B  1 792 ? -1.548  -1.604  49.340  1.00 72.93  ? 792  LYS C CA  1 
ATOM   13252 C  C   . LYS B  1 792 ? -2.114  -3.008  49.483  1.00 75.07  ? 792  LYS C C   1 
ATOM   13253 O  O   . LYS B  1 792 ? -1.485  -3.982  49.076  1.00 73.50  ? 792  LYS C O   1 
ATOM   13254 C  CB  . LYS B  1 792 ? -0.757  -1.195  50.590  1.00 70.04  ? 792  LYS C CB  1 
ATOM   13255 C  CG  . LYS B  1 792 ? 0.659   -1.757  50.634  1.00 70.99  ? 792  LYS C CG  1 
ATOM   13256 C  CD  . LYS B  1 792 ? 1.268   -1.702  52.025  1.00 72.18  ? 792  LYS C CD  1 
ATOM   13257 C  CE  . LYS B  1 792 ? 1.518   -0.280  52.466  1.00 78.21  ? 792  LYS C CE  1 
ATOM   13258 N  NZ  . LYS B  1 792 ? 0.814   0.031   53.737  1.00 78.72  ? 792  LYS C NZ  1 
ATOM   13259 N  N   . ILE B  1 793 ? -3.319  -3.095  50.042  1.00 80.76  ? 793  ILE C N   1 
ATOM   13260 C  CA  . ILE B  1 793 ? -4.017  -4.371  50.226  1.00 85.39  ? 793  ILE C CA  1 
ATOM   13261 C  C   . ILE B  1 793 ? -4.326  -5.027  48.895  1.00 76.63  ? 793  ILE C C   1 
ATOM   13262 O  O   . ILE B  1 793 ? -4.033  -6.199  48.683  1.00 77.03  ? 793  ILE C O   1 
ATOM   13263 C  CB  . ILE B  1 793 ? -5.338  -4.181  51.011  1.00 87.85  ? 793  ILE C CB  1 
ATOM   13264 C  CG1 . ILE B  1 793 ? -5.049  -3.870  52.476  1.00 85.82  ? 793  ILE C CG1 1 
ATOM   13265 C  CG2 . ILE B  1 793 ? -6.230  -5.408  50.892  1.00 91.08  ? 793  ILE C CG2 1 
ATOM   13266 C  CD1 . ILE B  1 793 ? -6.172  -3.144  53.152  1.00 91.89  ? 793  ILE C CD1 1 
ATOM   13267 N  N   . VAL B  1 794 ? -4.924  -4.243  48.009  1.00 80.67  ? 794  VAL C N   1 
ATOM   13268 C  CA  . VAL B  1 794 ? -5.257  -4.673  46.658  1.00 87.08  ? 794  VAL C CA  1 
ATOM   13269 C  C   . VAL B  1 794 ? -4.046  -5.194  45.895  1.00 85.98  ? 794  VAL C C   1 
ATOM   13270 O  O   . VAL B  1 794 ? -4.032  -6.344  45.457  1.00 84.12  ? 794  VAL C O   1 
ATOM   13271 C  CB  . VAL B  1 794 ? -5.877  -3.524  45.850  1.00 86.53  ? 794  VAL C CB  1 
ATOM   13272 C  CG1 . VAL B  1 794 ? -6.140  -3.971  44.437  1.00 82.98  ? 794  VAL C CG1 1 
ATOM   13273 C  CG2 . VAL B  1 794 ? -7.153  -3.029  46.521  1.00 87.74  ? 794  VAL C CG2 1 
ATOM   13274 N  N   . TYR B  1 795 ? -3.039  -4.337  45.736  1.00 84.62  ? 795  TYR C N   1 
ATOM   13275 C  CA  . TYR B  1 795 ? -1.819  -4.696  45.017  1.00 81.18  ? 795  TYR C CA  1 
ATOM   13276 C  C   . TYR B  1 795 ? -1.204  -5.953  45.586  1.00 79.48  ? 795  TYR C C   1 
ATOM   13277 O  O   . TYR B  1 795 ? -0.666  -6.780  44.854  1.00 78.41  ? 795  TYR C O   1 
ATOM   13278 C  CB  . TYR B  1 795 ? -0.794  -3.568  45.079  1.00 77.94  ? 795  TYR C CB  1 
ATOM   13279 C  CG  . TYR B  1 795 ? -1.136  -2.367  44.252  1.00 78.44  ? 795  TYR C CG  1 
ATOM   13280 C  CD1 . TYR B  1 795 ? -2.046  -2.451  43.212  1.00 77.39  ? 795  TYR C CD1 1 
ATOM   13281 C  CD2 . TYR B  1 795 ? -0.547  -1.142  44.513  1.00 74.38  ? 795  TYR C CD2 1 
ATOM   13282 C  CE1 . TYR B  1 795 ? -2.357  -1.345  42.460  1.00 83.55  ? 795  TYR C CE1 1 
ATOM   13283 C  CE2 . TYR B  1 795 ? -0.851  -0.036  43.765  1.00 75.35  ? 795  TYR C CE2 1 
ATOM   13284 C  CZ  . TYR B  1 795 ? -1.751  -0.140  42.741  1.00 75.54  ? 795  TYR C CZ  1 
ATOM   13285 O  OH  . TYR B  1 795 ? -2.048  0.970   42.001  1.00 76.39  ? 795  TYR C OH  1 
ATOM   13286 N  N   . SER B  1 796 ? -1.279  -6.080  46.905  1.00 78.61  ? 796  SER C N   1 
ATOM   13287 C  CA  . SER B  1 796 ? -0.732  -7.238  47.588  1.00 76.18  ? 796  SER C CA  1 
ATOM   13288 C  C   . SER B  1 796 ? -1.442  -8.488  47.112  1.00 78.01  ? 796  SER C C   1 
ATOM   13289 O  O   . SER B  1 796 ? -0.806  -9.497  46.816  1.00 81.60  ? 796  SER C O   1 
ATOM   13290 C  CB  . SER B  1 796 ? -0.869  -7.090  49.104  1.00 82.65  ? 796  SER C CB  1 
ATOM   13291 O  OG  . SER B  1 796 ? -0.405  -5.822  49.537  1.00 79.42  ? 796  SER C OG  1 
ATOM   13292 N  N   . VAL B  1 797 ? -2.765  -8.413  47.028  1.00 81.32  ? 797  VAL C N   1 
ATOM   13293 C  CA  . VAL B  1 797 ? -3.560  -9.568  46.621  1.00 90.54  ? 797  VAL C CA  1 
ATOM   13294 C  C   . VAL B  1 797 ? -3.359  -9.860  45.135  1.00 84.22  ? 797  VAL C C   1 
ATOM   13295 O  O   . VAL B  1 797 ? -3.112  -11.001 44.741  1.00 84.13  ? 797  VAL C O   1 
ATOM   13296 C  CB  . VAL B  1 797 ? -5.067  -9.357  46.921  1.00 90.92  ? 797  VAL C CB  1 
ATOM   13297 C  CG1 . VAL B  1 797 ? -5.896  -10.512 46.368  1.00 84.29  ? 797  VAL C CG1 1 
ATOM   13298 C  CG2 . VAL B  1 797 ? -5.294  -9.209  48.426  1.00 93.03  ? 797  VAL C CG2 1 
ATOM   13299 N  N   . GLY B  1 798 ? -3.432  -8.816  44.317  1.00 85.26  ? 798  GLY C N   1 
ATOM   13300 C  CA  . GLY B  1 798 ? -3.281  -8.952  42.880  1.00 87.69  ? 798  GLY C CA  1 
ATOM   13301 C  C   . GLY B  1 798 ? -1.863  -9.268  42.450  1.00 86.40  ? 798  GLY C C   1 
ATOM   13302 O  O   . GLY B  1 798 ? -1.539  -9.228  41.269  1.00 82.74  ? 798  GLY C O   1 
ATOM   13303 N  N   . ALA B  1 799 ? -1.014  -9.586  43.415  1.00 85.11  ? 799  ALA C N   1 
ATOM   13304 C  CA  . ALA B  1 799 ? 0.367   -9.914  43.124  1.00 85.04  ? 799  ALA C CA  1 
ATOM   13305 C  C   . ALA B  1 799 ? 0.606   -11.386 43.387  1.00 83.53  ? 799  ALA C C   1 
ATOM   13306 O  O   . ALA B  1 799 ? 1.735   -11.869 43.295  1.00 84.91  ? 799  ALA C O   1 
ATOM   13307 C  CB  . ALA B  1 799 ? 1.311   -9.057  43.957  1.00 85.18  ? 799  ALA C CB  1 
ATOM   13308 N  N   . GLN B  1 800 ? -0.466  -12.100 43.713  1.00 87.88  ? 800  GLN C N   1 
ATOM   13309 C  CA  . GLN B  1 800 ? -0.366  -13.534 43.981  1.00 89.52  ? 800  GLN C CA  1 
ATOM   13310 C  C   . GLN B  1 800 ? -0.481  -14.340 42.681  1.00 87.81  ? 800  GLN C C   1 
ATOM   13311 O  O   . GLN B  1 800 ? -0.437  -15.570 42.696  1.00 83.18  ? 800  GLN C O   1 
ATOM   13312 C  CB  . GLN B  1 800 ? -1.435  -13.971 44.989  1.00 85.55  ? 800  GLN C CB  1 
ATOM   13313 C  CG  . GLN B  1 800 ? -1.501  -13.119 46.255  1.00 79.12  ? 800  GLN C CG  1 
ATOM   13314 C  CD  . GLN B  1 800 ? -0.148  -12.946 46.928  1.00 83.61  ? 800  GLN C CD  1 
ATOM   13315 O  OE1 . GLN B  1 800 ? 0.607   -13.909 47.096  1.00 80.34  ? 800  GLN C OE1 1 
ATOM   13316 N  NE2 . GLN B  1 800 ? 0.167   -11.709 47.312  1.00 77.02  ? 800  GLN C NE2 1 
ATOM   13317 N  N   . THR B  1 801 ? -0.618  -13.626 41.564  1.00 90.64  ? 801  THR C N   1 
ATOM   13318 C  CA  . THR B  1 801 ? -0.656  -14.226 40.231  1.00 89.66  ? 801  THR C CA  1 
ATOM   13319 C  C   . THR B  1 801 ? 0.412   -13.605 39.330  1.00 93.50  ? 801  THR C C   1 
ATOM   13320 O  O   . THR B  1 801 ? 0.593   -12.383 39.331  1.00 93.18  ? 801  THR C O   1 
ATOM   13321 C  CB  . THR B  1 801 ? -2.041  -14.059 39.590  1.00 89.61  ? 801  THR C CB  1 
ATOM   13322 O  OG1 . THR B  1 801 ? -2.901  -15.098 40.070  1.00 99.31  ? 801  THR C OG1 1 
ATOM   13323 C  CG2 . THR B  1 801 ? -1.964  -14.142 38.067  1.00 95.42  ? 801  THR C CG2 1 
ATOM   13324 N  N   . THR B  1 802 ? 1.107   -14.452 38.567  1.00 86.36  ? 802  THR C N   1 
ATOM   13325 C  CA  . THR B  1 802 ? 2.246   -14.036 37.749  1.00 83.61  ? 802  THR C CA  1 
ATOM   13326 C  C   . THR B  1 802 ? 1.901   -12.946 36.731  1.00 81.23  ? 802  THR C C   1 
ATOM   13327 O  O   . THR B  1 802 ? 2.774   -12.219 36.269  1.00 81.71  ? 802  THR C O   1 
ATOM   13328 C  CB  . THR B  1 802 ? 2.851   -15.241 37.004  1.00 83.18  ? 802  THR C CB  1 
ATOM   13329 O  OG1 . THR B  1 802 ? 2.917   -16.364 37.892  1.00 83.67  ? 802  THR C OG1 1 
ATOM   13330 C  CG2 . THR B  1 802 ? 4.254   -14.923 36.496  1.00 84.47  ? 802  THR C CG2 1 
ATOM   13331 N  N   . ALA B  1 803 ? 0.629   -12.818 36.386  1.00 82.02  ? 803  ALA C N   1 
ATOM   13332 C  CA  . ALA B  1 803 ? 0.236   -11.778 35.453  1.00 80.84  ? 803  ALA C CA  1 
ATOM   13333 C  C   . ALA B  1 803 ? 0.096   -10.449 36.184  1.00 83.44  ? 803  ALA C C   1 
ATOM   13334 O  O   . ALA B  1 803 ? 0.456   -9.397  35.656  1.00 83.46  ? 803  ALA C O   1 
ATOM   13335 C  CB  . ALA B  1 803 ? -1.054  -12.149 34.754  1.00 83.74  ? 803  ALA C CB  1 
ATOM   13336 N  N   . GLY B  1 804 ? -0.422  -10.504 37.407  1.00 87.98  ? 804  GLY C N   1 
ATOM   13337 C  CA  . GLY B  1 804 ? -0.597  -9.307  38.215  1.00 87.42  ? 804  GLY C CA  1 
ATOM   13338 C  C   . GLY B  1 804 ? 0.699   -8.807  38.837  1.00 85.35  ? 804  GLY C C   1 
ATOM   13339 O  O   . GLY B  1 804 ? 0.922   -7.598  38.942  1.00 84.89  ? 804  GLY C O   1 
ATOM   13340 N  N   . TRP B  1 805 ? 1.541   -9.745  39.266  1.00 82.80  ? 805  TRP C N   1 
ATOM   13341 C  CA  . TRP B  1 805 ? 2.871   -9.443  39.786  1.00 80.88  ? 805  TRP C CA  1 
ATOM   13342 C  C   . TRP B  1 805 ? 3.674   -8.684  38.753  1.00 82.76  ? 805  TRP C C   1 
ATOM   13343 O  O   . TRP B  1 805 ? 4.271   -7.641  39.039  1.00 79.12  ? 805  TRP C O   1 
ATOM   13344 C  CB  . TRP B  1 805 ? 3.592   -10.735 40.156  1.00 80.89  ? 805  TRP C CB  1 
ATOM   13345 C  CG  . TRP B  1 805 ? 4.902   -10.568 40.864  1.00 81.60  ? 805  TRP C CG  1 
ATOM   13346 C  CD1 . TRP B  1 805 ? 5.143   -10.776 42.193  1.00 79.73  ? 805  TRP C CD1 1 
ATOM   13347 C  CD2 . TRP B  1 805 ? 6.160   -10.197 40.283  1.00 81.58  ? 805  TRP C CD2 1 
ATOM   13348 N  NE1 . TRP B  1 805 ? 6.468   -10.551 42.475  1.00 80.49  ? 805  TRP C NE1 1 
ATOM   13349 C  CE2 . TRP B  1 805 ? 7.115   -10.194 41.320  1.00 81.81  ? 805  TRP C CE2 1 
ATOM   13350 C  CE3 . TRP B  1 805 ? 6.571   -9.864  38.992  1.00 77.29  ? 805  TRP C CE3 1 
ATOM   13351 C  CZ2 . TRP B  1 805 ? 8.452   -9.870  41.104  1.00 74.71  ? 805  TRP C CZ2 1 
ATOM   13352 C  CZ3 . TRP B  1 805 ? 7.892   -9.540  38.782  1.00 82.11  ? 805  TRP C CZ3 1 
ATOM   13353 C  CH2 . TRP B  1 805 ? 8.819   -9.544  39.833  1.00 78.46  ? 805  TRP C CH2 1 
ATOM   13354 N  N   . ASN B  1 806 ? 3.690   -9.243  37.546  1.00 84.91  ? 806  ASN C N   1 
ATOM   13355 C  CA  . ASN B  1 806 ? 4.400   -8.663  36.427  1.00 78.31  ? 806  ASN C CA  1 
ATOM   13356 C  C   . ASN B  1 806 ? 3.784   -7.344  36.030  1.00 78.50  ? 806  ASN C C   1 
ATOM   13357 O  O   . ASN B  1 806 ? 4.492   -6.419  35.635  1.00 79.65  ? 806  ASN C O   1 
ATOM   13358 C  CB  . ASN B  1 806 ? 4.408   -9.621  35.238  1.00 76.94  ? 806  ASN C CB  1 
ATOM   13359 C  CG  . ASN B  1 806 ? 5.556   -10.607 35.296  1.00 87.58  ? 806  ASN C CG  1 
ATOM   13360 O  OD1 . ASN B  1 806 ? 6.570   -10.367 35.957  1.00 88.54  ? 806  ASN C OD1 1 
ATOM   13361 N  ND2 . ASN B  1 806 ? 5.408   -11.724 34.594  1.00 92.78  ? 806  ASN C ND2 1 
ATOM   13362 N  N   . TYR B  1 807 ? 2.465   -7.250  36.143  1.00 76.99  ? 807  TYR C N   1 
ATOM   13363 C  CA  . TYR B  1 807 ? 1.793   -6.029  35.742  1.00 79.97  ? 807  TYR C CA  1 
ATOM   13364 C  C   . TYR B  1 807 ? 2.194   -4.899  36.656  1.00 80.53  ? 807  TYR C C   1 
ATOM   13365 O  O   . TYR B  1 807 ? 2.379   -3.764  36.221  1.00 82.50  ? 807  TYR C O   1 
ATOM   13366 C  CB  . TYR B  1 807 ? 0.282   -6.184  35.764  1.00 80.95  ? 807  TYR C CB  1 
ATOM   13367 C  CG  . TYR B  1 807 ? -0.427  -4.935  35.291  1.00 84.16  ? 807  TYR C CG  1 
ATOM   13368 C  CD1 . TYR B  1 807 ? -0.574  -4.666  33.939  1.00 79.59  ? 807  TYR C CD1 1 
ATOM   13369 C  CD2 . TYR B  1 807 ? -0.939  -4.018  36.197  1.00 83.36  ? 807  TYR C CD2 1 
ATOM   13370 C  CE1 . TYR B  1 807 ? -1.219  -3.526  33.504  1.00 84.84  ? 807  TYR C CE1 1 
ATOM   13371 C  CE2 . TYR B  1 807 ? -1.585  -2.876  35.770  1.00 86.68  ? 807  TYR C CE2 1 
ATOM   13372 C  CZ  . TYR B  1 807 ? -1.721  -2.634  34.424  1.00 86.93  ? 807  TYR C CZ  1 
ATOM   13373 O  OH  . TYR B  1 807 ? -2.366  -1.496  33.998  1.00 94.14  ? 807  TYR C OH  1 
ATOM   13374 N  N   . LEU B  1 808 ? 2.320   -5.225  37.935  1.00 83.56  ? 808  LEU C N   1 
ATOM   13375 C  CA  . LEU B  1 808 ? 2.624   -4.237  38.958  1.00 82.14  ? 808  LEU C CA  1 
ATOM   13376 C  C   . LEU B  1 808 ? 4.075   -3.761  38.869  1.00 79.00  ? 808  LEU C C   1 
ATOM   13377 O  O   . LEU B  1 808 ? 4.351   -2.567  38.999  1.00 73.93  ? 808  LEU C O   1 
ATOM   13378 C  CB  . LEU B  1 808 ? 2.326   -4.813  40.341  1.00 82.84  ? 808  LEU C CB  1 
ATOM   13379 C  CG  . LEU B  1 808 ? 0.846   -4.897  40.720  1.00 82.53  ? 808  LEU C CG  1 
ATOM   13380 C  CD1 . LEU B  1 808 ? 0.673   -5.725  41.980  1.00 77.34  ? 808  LEU C CD1 1 
ATOM   13381 C  CD2 . LEU B  1 808 ? 0.260   -3.496  40.899  1.00 79.17  ? 808  LEU C CD2 1 
ATOM   13382 N  N   . LEU B  1 809 ? 4.993   -4.699  38.646  1.00 76.90  ? 809  LEU C N   1 
ATOM   13383 C  CA  . LEU B  1 809 ? 6.398   -4.366  38.471  1.00 75.11  ? 809  LEU C CA  1 
ATOM   13384 C  C   . LEU B  1 809 ? 6.562   -3.436  37.274  1.00 79.91  ? 809  LEU C C   1 
ATOM   13385 O  O   . LEU B  1 809 ? 7.383   -2.518  37.280  1.00 80.72  ? 809  LEU C O   1 
ATOM   13386 C  CB  . LEU B  1 809 ? 7.231   -5.629  38.288  1.00 76.13  ? 809  LEU C CB  1 
ATOM   13387 C  CG  . LEU B  1 809 ? 8.696   -5.357  37.964  1.00 75.27  ? 809  LEU C CG  1 
ATOM   13388 C  CD1 . LEU B  1 809 ? 9.317   -4.485  39.040  1.00 60.56  ? 809  LEU C CD1 1 
ATOM   13389 C  CD2 . LEU B  1 809 ? 9.456   -6.666  37.821  1.00 73.31  ? 809  LEU C CD2 1 
ATOM   13390 N  N   . GLU B  1 810 ? 5.761   -3.674  36.248  1.00 78.84  ? 810  GLU C N   1 
ATOM   13391 C  CA  . GLU B  1 810 ? 5.735   -2.790  35.100  1.00 79.55  ? 810  GLU C CA  1 
ATOM   13392 C  C   . GLU B  1 810 ? 5.143   -1.452  35.516  1.00 75.23  ? 810  GLU C C   1 
ATOM   13393 O  O   . GLU B  1 810 ? 5.593   -0.397  35.068  1.00 79.04  ? 810  GLU C O   1 
ATOM   13394 C  CB  . GLU B  1 810 ? 4.935   -3.427  33.956  1.00 87.52  ? 810  GLU C CB  1 
ATOM   13395 C  CG  . GLU B  1 810 ? 4.301   -2.443  32.980  1.00 89.43  ? 810  GLU C CG  1 
ATOM   13396 C  CD  . GLU B  1 810 ? 3.060   -3.019  32.305  1.00 94.03  ? 810  GLU C CD  1 
ATOM   13397 O  OE1 . GLU B  1 810 ? 3.196   -3.993  31.534  1.00 95.55  ? 810  GLU C OE1 1 
ATOM   13398 O  OE2 . GLU B  1 810 ? 1.946   -2.499  32.549  1.00 94.14  ? 810  GLU C OE2 1 
ATOM   13399 N  N   . GLN B  1 811 ? 4.146   -1.494  36.395  1.00 78.88  ? 811  GLN C N   1 
ATOM   13400 C  CA  . GLN B  1 811 ? 3.474   -0.272  36.833  1.00 81.11  ? 811  GLN C CA  1 
ATOM   13401 C  C   . GLN B  1 811 ? 4.392   0.562   37.721  1.00 79.51  ? 811  GLN C C   1 
ATOM   13402 O  O   . GLN B  1 811 ? 4.301   1.798   37.757  1.00 78.76  ? 811  GLN C O   1 
ATOM   13403 C  CB  . GLN B  1 811 ? 2.176   -0.596  37.575  1.00 80.49  ? 811  GLN C CB  1 
ATOM   13404 C  CG  . GLN B  1 811 ? 1.163   0.537   37.522  1.00 86.60  ? 811  GLN C CG  1 
ATOM   13405 C  CD  . GLN B  1 811 ? 0.777   0.894   36.095  1.00 93.45  ? 811  GLN C CD  1 
ATOM   13406 O  OE1 . GLN B  1 811 ? 0.490   0.013   35.278  1.00 91.55  ? 811  GLN C OE1 1 
ATOM   13407 N  NE2 . GLN B  1 811 ? 0.780   2.187   35.783  1.00 94.53  ? 811  GLN C NE2 1 
ATOM   13408 N  N   . TYR B  1 812 ? 5.276   -0.135  38.429  1.00 72.21  ? 812  TYR C N   1 
ATOM   13409 C  CA  . TYR B  1 812 ? 6.246   0.488   39.316  1.00 71.06  ? 812  TYR C CA  1 
ATOM   13410 C  C   . TYR B  1 812 ? 7.134   1.479   38.567  1.00 72.50  ? 812  TYR C C   1 
ATOM   13411 O  O   . TYR B  1 812 ? 7.290   2.627   38.988  1.00 69.72  ? 812  TYR C O   1 
ATOM   13412 C  CB  . TYR B  1 812 ? 7.100   -0.592  39.989  1.00 71.19  ? 812  TYR C CB  1 
ATOM   13413 C  CG  . TYR B  1 812 ? 8.044   -0.092  41.063  1.00 67.45  ? 812  TYR C CG  1 
ATOM   13414 C  CD1 . TYR B  1 812 ? 7.592   0.155   42.353  1.00 70.49  ? 812  TYR C CD1 1 
ATOM   13415 C  CD2 . TYR B  1 812 ? 9.390   0.112   40.792  1.00 71.37  ? 812  TYR C CD2 1 
ATOM   13416 C  CE1 . TYR B  1 812 ? 8.453   0.597   43.335  1.00 71.98  ? 812  TYR C CE1 1 
ATOM   13417 C  CE2 . TYR B  1 812 ? 10.264  0.556   41.771  1.00 69.30  ? 812  TYR C CE2 1 
ATOM   13418 C  CZ  . TYR B  1 812 ? 9.789   0.798   43.039  1.00 73.30  ? 812  TYR C CZ  1 
ATOM   13419 O  OH  . TYR B  1 812 ? 10.656  1.241   44.016  1.00 75.99  ? 812  TYR C OH  1 
ATOM   13420 N  N   . GLU B  1 813 ? 7.689   1.027   37.443  1.00 73.76  ? 813  GLU C N   1 
ATOM   13421 C  CA  . GLU B  1 813 ? 8.677   1.792   36.696  1.00 66.03  ? 813  GLU C CA  1 
ATOM   13422 C  C   . GLU B  1 813 ? 8.084   2.989   35.997  1.00 69.70  ? 813  GLU C C   1 
ATOM   13423 O  O   . GLU B  1 813 ? 8.808   3.874   35.550  1.00 79.00  ? 813  GLU C O   1 
ATOM   13424 C  CB  . GLU B  1 813 ? 9.365   0.915   35.658  1.00 68.93  ? 813  GLU C CB  1 
ATOM   13425 C  CG  . GLU B  1 813 ? 9.782   -0.436  36.163  1.00 74.07  ? 813  GLU C CG  1 
ATOM   13426 C  CD  . GLU B  1 813 ? 10.613  -1.179  35.145  1.00 75.00  ? 813  GLU C CD  1 
ATOM   13427 O  OE1 . GLU B  1 813 ? 11.181  -0.511  34.256  1.00 79.27  ? 813  GLU C OE1 1 
ATOM   13428 O  OE2 . GLU B  1 813 ? 10.692  -2.426  35.228  1.00 73.90  ? 813  GLU C OE2 1 
ATOM   13429 N  N   . LEU B  1 814 ? 6.767   3.027   35.890  1.00 72.67  ? 814  LEU C N   1 
ATOM   13430 C  CA  . LEU B  1 814 ? 6.142   4.099   35.136  1.00 73.33  ? 814  LEU C CA  1 
ATOM   13431 C  C   . LEU B  1 814 ? 5.464   5.124   36.032  1.00 70.10  ? 814  LEU C C   1 
ATOM   13432 O  O   . LEU B  1 814 ? 5.128   6.209   35.582  1.00 72.14  ? 814  LEU C O   1 
ATOM   13433 C  CB  . LEU B  1 814 ? 5.138   3.515   34.141  1.00 83.42  ? 814  LEU C CB  1 
ATOM   13434 C  CG  . LEU B  1 814 ? 5.780   2.686   33.023  1.00 81.91  ? 814  LEU C CG  1 
ATOM   13435 C  CD1 . LEU B  1 814 ? 4.730   2.133   32.065  1.00 84.02  ? 814  LEU C CD1 1 
ATOM   13436 C  CD2 . LEU B  1 814 ? 6.808   3.525   32.274  1.00 73.80  ? 814  LEU C CD2 1 
ATOM   13437 N  N   . SER B  1 815 ? 5.274   4.786   37.302  1.00 71.55  ? 815  SER C N   1 
ATOM   13438 C  CA  . SER B  1 815 ? 4.537   5.663   38.196  1.00 67.42  ? 815  SER C CA  1 
ATOM   13439 C  C   . SER B  1 815 ? 5.295   6.933   38.530  1.00 66.30  ? 815  SER C C   1 
ATOM   13440 O  O   . SER B  1 815 ? 6.517   6.939   38.541  1.00 68.85  ? 815  SER C O   1 
ATOM   13441 C  CB  . SER B  1 815 ? 4.189   4.940   39.491  1.00 69.54  ? 815  SER C CB  1 
ATOM   13442 O  OG  . SER B  1 815 ? 3.814   5.882   40.485  1.00 62.81  ? 815  SER C OG  1 
ATOM   13443 N  N   . MET B  1 816 ? 4.552   7.996   38.828  1.00 69.32  ? 816  MET C N   1 
ATOM   13444 C  CA  . MET B  1 816 ? 5.126   9.254   39.301  1.00 62.63  ? 816  MET C CA  1 
ATOM   13445 C  C   . MET B  1 816 ? 4.852   9.501   40.785  1.00 59.26  ? 816  MET C C   1 
ATOM   13446 O  O   . MET B  1 816 ? 5.109   10.593  41.309  1.00 55.50  ? 816  MET C O   1 
ATOM   13447 C  CB  . MET B  1 816 ? 4.586   10.425  38.479  1.00 60.40  ? 816  MET C CB  1 
ATOM   13448 C  CG  . MET B  1 816 ? 4.974   10.386  37.007  1.00 66.94  ? 816  MET C CG  1 
ATOM   13449 S  SD  . MET B  1 816 ? 6.658   10.949  36.682  1.00 66.98  ? 816  MET C SD  1 
ATOM   13450 C  CE  . MET B  1 816 ? 7.523   9.371   36.581  1.00 58.06  ? 816  MET C CE  1 
ATOM   13451 N  N   . SER B  1 817 ? 4.324   8.492   41.467  1.00 64.55  ? 817  SER C N   1 
ATOM   13452 C  CA  . SER B  1 817 ? 4.117   8.605   42.912  1.00 69.01  ? 817  SER C CA  1 
ATOM   13453 C  C   . SER B  1 817 ? 4.976   7.626   43.693  1.00 63.62  ? 817  SER C C   1 
ATOM   13454 O  O   . SER B  1 817 ? 4.733   6.422   43.672  1.00 66.07  ? 817  SER C O   1 
ATOM   13455 C  CB  . SER B  1 817 ? 2.653   8.383   43.281  1.00 69.51  ? 817  SER C CB  1 
ATOM   13456 O  OG  . SER B  1 817 ? 2.456   8.574   44.677  1.00 71.97  ? 817  SER C OG  1 
ATOM   13457 N  N   . SER B  1 818 ? 5.977   8.149   44.390  1.00 62.24  ? 818  SER C N   1 
ATOM   13458 C  CA  . SER B  1 818 ? 6.830   7.310   45.216  1.00 65.16  ? 818  SER C CA  1 
ATOM   13459 C  C   . SER B  1 818 ? 6.006   6.620   46.306  1.00 63.86  ? 818  SER C C   1 
ATOM   13460 O  O   . SER B  1 818 ? 6.354   5.539   46.778  1.00 58.23  ? 818  SER C O   1 
ATOM   13461 C  CB  . SER B  1 818 ? 7.963   8.139   45.815  1.00 54.50  ? 818  SER C CB  1 
ATOM   13462 O  OG  . SER B  1 818 ? 8.944   8.399   44.820  1.00 56.20  ? 818  SER C OG  1 
ATOM   13463 N  N   . ALA B  1 819 ? 4.898   7.249   46.679  1.00 65.87  ? 819  ALA C N   1 
ATOM   13464 C  CA  . ALA B  1 819 ? 3.967   6.656   47.612  1.00 60.30  ? 819  ALA C CA  1 
ATOM   13465 C  C   . ALA B  1 819 ? 3.339   5.421   47.000  1.00 64.88  ? 819  ALA C C   1 
ATOM   13466 O  O   . ALA B  1 819 ? 3.229   4.385   47.656  1.00 71.51  ? 819  ALA C O   1 
ATOM   13467 C  CB  . ALA B  1 819 ? 2.908   7.649   48.008  1.00 68.20  ? 819  ALA C CB  1 
ATOM   13468 N  N   . GLU B  1 820 ? 2.933   5.523   45.742  1.00 62.78  ? 820  GLU C N   1 
ATOM   13469 C  CA  . GLU B  1 820 ? 2.373   4.368   45.057  1.00 66.98  ? 820  GLU C CA  1 
ATOM   13470 C  C   . GLU B  1 820 ? 3.465   3.324   44.852  1.00 63.43  ? 820  GLU C C   1 
ATOM   13471 O  O   . GLU B  1 820 ? 3.206   2.127   44.871  1.00 69.28  ? 820  GLU C O   1 
ATOM   13472 C  CB  . GLU B  1 820 ? 1.746   4.760   43.712  1.00 70.18  ? 820  GLU C CB  1 
ATOM   13473 C  CG  . GLU B  1 820 ? 0.768   3.715   43.168  1.00 76.69  ? 820  GLU C CG  1 
ATOM   13474 C  CD  . GLU B  1 820 ? 0.429   3.909   41.699  1.00 78.40  ? 820  GLU C CD  1 
ATOM   13475 O  OE1 . GLU B  1 820 ? 1.268   4.462   40.962  1.00 76.17  ? 820  GLU C OE1 1 
ATOM   13476 O  OE2 . GLU B  1 820 ? -0.676  3.504   41.276  1.00 85.17  ? 820  GLU C OE2 1 
ATOM   13477 N  N   . GLN B  1 821 ? 4.694   3.783   44.673  1.00 60.99  ? 821  GLN C N   1 
ATOM   13478 C  CA  . GLN B  1 821 ? 5.800   2.869   44.451  1.00 65.09  ? 821  GLN C CA  1 
ATOM   13479 C  C   . GLN B  1 821 ? 6.103   2.055   45.703  1.00 61.86  ? 821  GLN C C   1 
ATOM   13480 O  O   . GLN B  1 821 ? 6.371   0.859   45.630  1.00 59.34  ? 821  GLN C O   1 
ATOM   13481 C  CB  . GLN B  1 821 ? 7.030   3.641   43.985  1.00 65.65  ? 821  GLN C CB  1 
ATOM   13482 C  CG  . GLN B  1 821 ? 6.858   4.208   42.584  1.00 69.01  ? 821  GLN C CG  1 
ATOM   13483 C  CD  . GLN B  1 821 ? 8.087   4.925   42.071  1.00 65.08  ? 821  GLN C CD  1 
ATOM   13484 O  OE1 . GLN B  1 821 ? 8.554   5.886   42.674  1.00 59.02  ? 821  GLN C OE1 1 
ATOM   13485 N  NE2 . GLN B  1 821 ? 8.620   4.455   40.950  1.00 68.43  ? 821  GLN C NE2 1 
ATOM   13486 N  N   . ASN B  1 822 ? 6.044   2.707   46.854  1.00 62.96  ? 822  ASN C N   1 
ATOM   13487 C  CA  . ASN B  1 822 ? 6.273   2.016   48.105  1.00 64.32  ? 822  ASN C CA  1 
ATOM   13488 C  C   . ASN B  1 822 ? 5.261   0.872   48.263  1.00 66.30  ? 822  ASN C C   1 
ATOM   13489 O  O   . ASN B  1 822 ? 5.640   -0.239  48.634  1.00 62.51  ? 822  ASN C O   1 
ATOM   13490 C  CB  . ASN B  1 822 ? 6.201   2.998   49.275  1.00 65.98  ? 822  ASN C CB  1 
ATOM   13491 C  CG  . ASN B  1 822 ? 6.724   2.405   50.580  1.00 77.77  ? 822  ASN C CG  1 
ATOM   13492 O  OD1 . ASN B  1 822 ? 5.957   1.873   51.384  1.00 80.01  ? 822  ASN C OD1 1 
ATOM   13493 N  ND2 . ASN B  1 822 ? 8.034   2.500   50.795  1.00 78.75  ? 822  ASN C ND2 1 
ATOM   13494 N  N   . LYS B  1 823 ? 3.994   1.144   47.941  1.00 67.01  ? 823  LYS C N   1 
ATOM   13495 C  CA  . LYS B  1 823 ? 2.920   0.138   47.993  1.00 66.54  ? 823  LYS C CA  1 
ATOM   13496 C  C   . LYS B  1 823 ? 3.146   -1.021  47.015  1.00 68.36  ? 823  LYS C C   1 
ATOM   13497 O  O   . LYS B  1 823 ? 3.151   -2.202  47.401  1.00 64.35  ? 823  LYS C O   1 
ATOM   13498 C  CB  . LYS B  1 823 ? 1.560   0.772   47.687  1.00 62.64  ? 823  LYS C CB  1 
ATOM   13499 C  CG  . LYS B  1 823 ? 1.285   2.112   48.353  1.00 72.41  ? 823  LYS C CG  1 
ATOM   13500 C  CD  . LYS B  1 823 ? 1.116   2.022   49.859  1.00 68.87  ? 823  LYS C CD  1 
ATOM   13501 C  CE  . LYS B  1 823 ? 0.059   3.019   50.322  1.00 76.29  ? 823  LYS C CE  1 
ATOM   13502 N  NZ  . LYS B  1 823 ? 0.201   4.350   49.654  1.00 66.37  ? 823  LYS C NZ  1 
ATOM   13503 N  N   . ILE B  1 824 ? 3.309   -0.667  45.743  1.00 65.59  ? 824  ILE C N   1 
ATOM   13504 C  CA  . ILE B  1 824 ? 3.570   -1.640  44.689  1.00 67.91  ? 824  ILE C CA  1 
ATOM   13505 C  C   . ILE B  1 824 ? 4.749   -2.542  45.022  1.00 62.27  ? 824  ILE C C   1 
ATOM   13506 O  O   . ILE B  1 824 ? 4.680   -3.758  44.866  1.00 69.64  ? 824  ILE C O   1 
ATOM   13507 C  CB  . ILE B  1 824 ? 3.836   -0.936  43.362  1.00 66.69  ? 824  ILE C CB  1 
ATOM   13508 C  CG1 . ILE B  1 824 ? 2.575   -0.201  42.917  1.00 68.64  ? 824  ILE C CG1 1 
ATOM   13509 C  CG2 . ILE B  1 824 ? 4.275   -1.935  42.313  1.00 66.97  ? 824  ILE C CG2 1 
ATOM   13510 C  CD1 . ILE B  1 824 ? 2.823   0.878   41.900  1.00 76.97  ? 824  ILE C CD1 1 
ATOM   13511 N  N   . LEU B  1 825 ? 5.820   -1.934  45.507  1.00 61.04  ? 825  LEU C N   1 
ATOM   13512 C  CA  . LEU B  1 825 ? 7.024   -2.665  45.845  1.00 67.15  ? 825  LEU C CA  1 
ATOM   13513 C  C   . LEU B  1 825 ? 6.734   -3.669  46.949  1.00 68.13  ? 825  LEU C C   1 
ATOM   13514 O  O   . LEU B  1 825 ? 7.152   -4.827  46.870  1.00 68.82  ? 825  LEU C O   1 
ATOM   13515 C  CB  . LEU B  1 825 ? 8.135   -1.697  46.259  1.00 66.16  ? 825  LEU C CB  1 
ATOM   13516 C  CG  . LEU B  1 825 ? 9.487   -2.289  46.651  1.00 66.84  ? 825  LEU C CG  1 
ATOM   13517 C  CD1 . LEU B  1 825 ? 9.930   -3.368  45.678  1.00 68.84  ? 825  LEU C CD1 1 
ATOM   13518 C  CD2 . LEU B  1 825 ? 10.515  -1.182  46.703  1.00 70.39  ? 825  LEU C CD2 1 
ATOM   13519 N  N   . TYR B  1 826 ? 6.001   -3.222  47.964  1.00 66.75  ? 826  TYR C N   1 
ATOM   13520 C  CA  . TYR B  1 826 ? 5.559   -4.103  49.035  1.00 69.97  ? 826  TYR C CA  1 
ATOM   13521 C  C   . TYR B  1 826 ? 4.732   -5.253  48.499  1.00 73.17  ? 826  TYR C C   1 
ATOM   13522 O  O   . TYR B  1 826 ? 4.943   -6.412  48.870  1.00 68.59  ? 826  TYR C O   1 
ATOM   13523 C  CB  . TYR B  1 826 ? 4.731   -3.342  50.061  1.00 76.84  ? 826  TYR C CB  1 
ATOM   13524 C  CG  . TYR B  1 826 ? 4.041   -4.254  51.044  1.00 78.28  ? 826  TYR C CG  1 
ATOM   13525 C  CD1 . TYR B  1 826 ? 4.698   -4.702  52.179  1.00 79.65  ? 826  TYR C CD1 1 
ATOM   13526 C  CD2 . TYR B  1 826 ? 2.733   -4.676  50.832  1.00 82.42  ? 826  TYR C CD2 1 
ATOM   13527 C  CE1 . TYR B  1 826 ? 4.074   -5.542  53.077  1.00 84.84  ? 826  TYR C CE1 1 
ATOM   13528 C  CE2 . TYR B  1 826 ? 2.100   -5.519  51.722  1.00 85.80  ? 826  TYR C CE2 1 
ATOM   13529 C  CZ  . TYR B  1 826 ? 2.775   -5.946  52.844  1.00 89.38  ? 826  TYR C CZ  1 
ATOM   13530 O  OH  . TYR B  1 826 ? 2.153   -6.782  53.737  1.00 96.60  ? 826  TYR C OH  1 
ATOM   13531 N  N   . ALA B  1 827 ? 3.766   -4.902  47.655  1.00 71.40  ? 827  ALA C N   1 
ATOM   13532 C  CA  . ALA B  1 827 ? 2.886   -5.866  47.025  1.00 67.89  ? 827  ALA C CA  1 
ATOM   13533 C  C   . ALA B  1 827 ? 3.691   -7.005  46.451  1.00 70.25  ? 827  ALA C C   1 
ATOM   13534 O  O   . ALA B  1 827 ? 3.436   -8.171  46.745  1.00 68.81  ? 827  ALA C O   1 
ATOM   13535 C  CB  . ALA B  1 827 ? 2.075   -5.206  45.947  1.00 63.10  ? 827  ALA C CB  1 
ATOM   13536 N  N   . LEU B  1 828 ? 4.691   -6.647  45.654  1.00 70.41  ? 828  LEU C N   1 
ATOM   13537 C  CA  . LEU B  1 828 ? 5.525   -7.628  44.981  1.00 68.06  ? 828  LEU C CA  1 
ATOM   13538 C  C   . LEU B  1 828 ? 6.293   -8.530  45.936  1.00 65.61  ? 828  LEU C C   1 
ATOM   13539 O  O   . LEU B  1 828 ? 6.636   -9.639  45.581  1.00 74.00  ? 828  LEU C O   1 
ATOM   13540 C  CB  . LEU B  1 828 ? 6.506   -6.918  44.062  1.00 69.77  ? 828  LEU C CB  1 
ATOM   13541 C  CG  . LEU B  1 828 ? 5.878   -6.159  42.906  1.00 69.24  ? 828  LEU C CG  1 
ATOM   13542 C  CD1 . LEU B  1 828 ? 6.940   -5.421  42.115  1.00 73.05  ? 828  LEU C CD1 1 
ATOM   13543 C  CD2 . LEU B  1 828 ? 5.146   -7.134  42.034  1.00 74.83  ? 828  LEU C CD2 1 
ATOM   13544 N  N   . SER B  1 829 ? 6.574   -8.054  47.142  1.00 70.15  ? 829  SER C N   1 
ATOM   13545 C  CA  . SER B  1 829 ? 7.389   -8.815  48.086  1.00 70.99  ? 829  SER C CA  1 
ATOM   13546 C  C   . SER B  1 829 ? 6.585   -9.863  48.852  1.00 76.94  ? 829  SER C C   1 
ATOM   13547 O  O   . SER B  1 829 ? 7.103   -10.532 49.747  1.00 74.94  ? 829  SER C O   1 
ATOM   13548 C  CB  . SER B  1 829 ? 8.050   -7.872  49.074  1.00 73.47  ? 829  SER C CB  1 
ATOM   13549 O  OG  . SER B  1 829 ? 7.051   -7.139  49.758  1.00 79.44  ? 829  SER C OG  1 
ATOM   13550 N  N   . THR B  1 830 ? 5.314   -9.999  48.502  1.00 79.74  ? 830  THR C N   1 
ATOM   13551 C  CA  . THR B  1 830 ? 4.444   -10.944 49.181  1.00 78.30  ? 830  THR C CA  1 
ATOM   13552 C  C   . THR B  1 830 ? 4.327   -12.240 48.399  1.00 80.31  ? 830  THR C C   1 
ATOM   13553 O  O   . THR B  1 830 ? 3.834   -13.239 48.915  1.00 83.89  ? 830  THR C O   1 
ATOM   13554 C  CB  . THR B  1 830 ? 3.040   -10.373 49.383  1.00 77.30  ? 830  THR C CB  1 
ATOM   13555 O  OG1 . THR B  1 830 ? 2.413   -10.218 48.106  1.00 79.49  ? 830  THR C OG1 1 
ATOM   13556 C  CG2 . THR B  1 830 ? 3.097   -9.026  50.095  1.00 73.65  ? 830  THR C CG2 1 
ATOM   13557 N  N   . SER B  1 831 ? 4.784   -12.217 47.152  1.00 81.01  ? 831  SER C N   1 
ATOM   13558 C  CA  . SER B  1 831 ? 4.647   -13.362 46.258  1.00 82.94  ? 831  SER C CA  1 
ATOM   13559 C  C   . SER B  1 831 ? 5.315   -14.620 46.814  1.00 84.27  ? 831  SER C C   1 
ATOM   13560 O  O   . SER B  1 831 ? 6.352   -14.547 47.478  1.00 77.98  ? 831  SER C O   1 
ATOM   13561 C  CB  . SER B  1 831 ? 5.221   -13.029 44.883  1.00 79.65  ? 831  SER C CB  1 
ATOM   13562 O  OG  . SER B  1 831 ? 5.089   -14.123 43.993  1.00 89.26  ? 831  SER C OG  1 
ATOM   13563 N  N   . LYS B  1 832 ? 4.696   -15.767 46.531  1.00 90.66  ? 832  LYS C N   1 
ATOM   13564 C  CA  . LYS B  1 832 ? 5.127   -17.071 47.044  1.00 91.33  ? 832  LYS C CA  1 
ATOM   13565 C  C   . LYS B  1 832 ? 6.300   -17.661 46.261  1.00 91.95  ? 832  LYS C C   1 
ATOM   13566 O  O   . LYS B  1 832 ? 7.008   -18.543 46.759  1.00 91.00  ? 832  LYS C O   1 
ATOM   13567 C  CB  . LYS B  1 832 ? 3.954   -18.054 47.019  1.00 91.58  ? 832  LYS C CB  1 
ATOM   13568 C  CG  . LYS B  1 832 ? 3.175   -18.024 45.702  1.00 101.72 ? 832  LYS C CG  1 
ATOM   13569 C  CD  . LYS B  1 832 ? 2.806   -19.423 45.206  1.00 104.73 ? 832  LYS C CD  1 
ATOM   13570 C  CE  . LYS B  1 832 ? 2.025   -19.355 43.894  1.00 97.69  ? 832  LYS C CE  1 
ATOM   13571 N  NZ  . LYS B  1 832 ? 1.671   -20.703 43.360  1.00 108.04 ? 832  LYS C NZ  1 
ATOM   13572 N  N   . HIS B  1 833 ? 6.488   -17.179 45.033  1.00 88.91  ? 833  HIS C N   1 
ATOM   13573 C  CA  . HIS B  1 833 ? 7.564   -17.648 44.164  1.00 88.69  ? 833  HIS C CA  1 
ATOM   13574 C  C   . HIS B  1 833 ? 8.919   -17.201 44.666  1.00 89.22  ? 833  HIS C C   1 
ATOM   13575 O  O   . HIS B  1 833 ? 9.193   -16.000 44.715  1.00 88.44  ? 833  HIS C O   1 
ATOM   13576 C  CB  . HIS B  1 833 ? 7.386   -17.131 42.738  1.00 89.80  ? 833  HIS C CB  1 
ATOM   13577 C  CG  . HIS B  1 833 ? 6.070   -17.482 42.125  1.00 92.87  ? 833  HIS C CG  1 
ATOM   13578 N  ND1 . HIS B  1 833 ? 5.723   -17.096 40.849  1.00 95.17  ? 833  HIS C ND1 1 
ATOM   13579 C  CD2 . HIS B  1 833 ? 5.019   -18.183 42.609  1.00 93.58  ? 833  HIS C CD2 1 
ATOM   13580 C  CE1 . HIS B  1 833 ? 4.510   -17.543 40.573  1.00 99.82  ? 833  HIS C CE1 1 
ATOM   13581 N  NE2 . HIS B  1 833 ? 4.061   -18.205 41.624  1.00 103.46 ? 833  HIS C NE2 1 
ATOM   13582 N  N   . GLN B  1 834 ? 9.763   -18.165 45.019  1.00 89.18  ? 834  GLN C N   1 
ATOM   13583 C  CA  . GLN B  1 834 ? 11.148  -17.881 45.365  1.00 83.90  ? 834  GLN C CA  1 
ATOM   13584 C  C   . GLN B  1 834 ? 11.804  -17.061 44.271  1.00 85.88  ? 834  GLN C C   1 
ATOM   13585 O  O   . GLN B  1 834 ? 12.546  -16.120 44.551  1.00 87.88  ? 834  GLN C O   1 
ATOM   13586 C  CB  . GLN B  1 834 ? 11.930  -19.174 45.581  1.00 81.35  ? 834  GLN C CB  1 
ATOM   13587 C  CG  . GLN B  1 834 ? 11.425  -19.993 46.738  1.00 86.22  ? 834  GLN C CG  1 
ATOM   13588 C  CD  . GLN B  1 834 ? 11.577  -19.267 48.050  1.00 86.75  ? 834  GLN C CD  1 
ATOM   13589 O  OE1 . GLN B  1 834 ? 10.682  -18.536 48.476  1.00 92.44  ? 834  GLN C OE1 1 
ATOM   13590 N  NE2 . GLN B  1 834 ? 12.720  -19.453 48.699  1.00 85.49  ? 834  GLN C NE2 1 
ATOM   13591 N  N   . GLU B  1 835 ? 11.508  -17.414 43.025  1.00 84.11  ? 835  GLU C N   1 
ATOM   13592 C  CA  . GLU B  1 835 ? 12.172  -16.806 41.882  1.00 84.19  ? 835  GLU C CA  1 
ATOM   13593 C  C   . GLU B  1 835 ? 11.776  -15.344 41.700  1.00 82.86  ? 835  GLU C C   1 
ATOM   13594 O  O   . GLU B  1 835 ? 12.603  -14.518 41.301  1.00 74.95  ? 835  GLU C O   1 
ATOM   13595 C  CB  . GLU B  1 835 ? 11.869  -17.599 40.605  1.00 82.65  ? 835  GLU C CB  1 
ATOM   13596 C  CG  . GLU B  1 835 ? 10.394  -17.634 40.211  1.00 87.27  ? 835  GLU C CG  1 
ATOM   13597 C  CD  . GLU B  1 835 ? 10.206  -17.763 38.710  1.00 95.01  ? 835  GLU C CD  1 
ATOM   13598 O  OE1 . GLU B  1 835 ? 11.018  -18.474 38.077  1.00 100.92 ? 835  GLU C OE1 1 
ATOM   13599 O  OE2 . GLU B  1 835 ? 9.261   -17.149 38.160  1.00 93.43  ? 835  GLU C OE2 1 
ATOM   13600 N  N   . LYS B  1 836 ? 10.517  -15.019 41.988  1.00 82.87  ? 836  LYS C N   1 
ATOM   13601 C  CA  . LYS B  1 836 ? 10.065  -13.640 41.843  1.00 82.99  ? 836  LYS C CA  1 
ATOM   13602 C  C   . LYS B  1 836 ? 10.569  -12.794 43.009  1.00 78.81  ? 836  LYS C C   1 
ATOM   13603 O  O   . LYS B  1 836 ? 10.789  -11.593 42.859  1.00 75.92  ? 836  LYS C O   1 
ATOM   13604 C  CB  . LYS B  1 836 ? 8.537   -13.565 41.733  1.00 84.20  ? 836  LYS C CB  1 
ATOM   13605 C  CG  . LYS B  1 836 ? 8.007   -13.884 40.339  1.00 82.84  ? 836  LYS C CG  1 
ATOM   13606 C  CD  . LYS B  1 836 ? 8.898   -13.270 39.252  1.00 85.41  ? 836  LYS C CD  1 
ATOM   13607 C  CE  . LYS B  1 836 ? 8.502   -13.729 37.848  1.00 85.31  ? 836  LYS C CE  1 
ATOM   13608 N  NZ  . LYS B  1 836 ? 9.307   -13.040 36.796  1.00 88.17  ? 836  LYS C NZ  1 
ATOM   13609 N  N   . LEU B  1 837 ? 10.766  -13.436 44.158  1.00 74.09  ? 837  LEU C N   1 
ATOM   13610 C  CA  . LEU B  1 837 ? 11.275  -12.760 45.338  1.00 71.56  ? 837  LEU C CA  1 
ATOM   13611 C  C   . LEU B  1 837 ? 12.757  -12.463 45.191  1.00 75.55  ? 837  LEU C C   1 
ATOM   13612 O  O   . LEU B  1 837 ? 13.259  -11.497 45.763  1.00 79.56  ? 837  LEU C O   1 
ATOM   13613 C  CB  . LEU B  1 837 ? 11.026  -13.596 46.596  1.00 72.33  ? 837  LEU C CB  1 
ATOM   13614 C  CG  . LEU B  1 837 ? 9.575   -13.775 47.064  1.00 76.56  ? 837  LEU C CG  1 
ATOM   13615 C  CD1 . LEU B  1 837 ? 9.512   -14.729 48.248  1.00 82.95  ? 837  LEU C CD1 1 
ATOM   13616 C  CD2 . LEU B  1 837 ? 8.893   -12.444 47.404  1.00 76.03  ? 837  LEU C CD2 1 
ATOM   13617 N  N   . LEU B  1 838 ? 13.456  -13.291 44.424  1.00 73.30  ? 838  LEU C N   1 
ATOM   13618 C  CA  . LEU B  1 838 ? 14.874  -13.067 44.163  1.00 75.54  ? 838  LEU C CA  1 
ATOM   13619 C  C   . LEU B  1 838 ? 15.081  -12.044 43.062  1.00 75.70  ? 838  LEU C C   1 
ATOM   13620 O  O   . LEU B  1 838 ? 16.099  -11.359 43.028  1.00 79.07  ? 838  LEU C O   1 
ATOM   13621 C  CB  . LEU B  1 838 ? 15.581  -14.375 43.792  1.00 83.13  ? 838  LEU C CB  1 
ATOM   13622 C  CG  . LEU B  1 838 ? 16.245  -15.088 44.973  1.00 83.54  ? 838  LEU C CG  1 
ATOM   13623 C  CD1 . LEU B  1 838 ? 16.933  -16.393 44.583  1.00 75.50  ? 838  LEU C CD1 1 
ATOM   13624 C  CD2 . LEU B  1 838 ? 17.223  -14.145 45.643  1.00 86.11  ? 838  LEU C CD2 1 
ATOM   13625 N  N   . LYS B  1 839 ? 14.115  -11.939 42.159  1.00 74.74  ? 839  LYS C N   1 
ATOM   13626 C  CA  . LYS B  1 839 ? 14.198  -10.954 41.087  1.00 75.90  ? 839  LYS C CA  1 
ATOM   13627 C  C   . LYS B  1 839 ? 14.132  -9.548  41.672  1.00 76.72  ? 839  LYS C C   1 
ATOM   13628 O  O   . LYS B  1 839 ? 14.986  -8.706  41.381  1.00 75.57  ? 839  LYS C O   1 
ATOM   13629 C  CB  . LYS B  1 839 ? 13.078  -11.161 40.064  1.00 72.42  ? 839  LYS C CB  1 
ATOM   13630 C  CG  . LYS B  1 839 ? 13.209  -10.322 38.797  1.00 69.28  ? 839  LYS C CG  1 
ATOM   13631 C  CD  . LYS B  1 839 ? 12.064  -10.623 37.842  1.00 75.33  ? 839  LYS C CD  1 
ATOM   13632 C  CE  . LYS B  1 839 ? 11.849  -9.503  36.839  1.00 76.73  ? 839  LYS C CE  1 
ATOM   13633 N  NZ  . LYS B  1 839 ? 10.629  -9.753  36.011  1.00 86.05  ? 839  LYS C NZ  1 
ATOM   13634 N  N   . LEU B  1 840 ? 13.109  -9.308  42.489  1.00 74.10  ? 840  LEU C N   1 
ATOM   13635 C  CA  . LEU B  1 840 ? 12.990  -8.066  43.232  1.00 72.58  ? 840  LEU C CA  1 
ATOM   13636 C  C   . LEU B  1 840 ? 14.300  -7.734  43.907  1.00 75.03  ? 840  LEU C C   1 
ATOM   13637 O  O   . LEU B  1 840 ? 14.812  -6.627  43.764  1.00 70.98  ? 840  LEU C O   1 
ATOM   13638 C  CB  . LEU B  1 840 ? 11.900  -8.165  44.283  1.00 71.13  ? 840  LEU C CB  1 
ATOM   13639 C  CG  . LEU B  1 840 ? 10.485  -8.321  43.770  1.00 73.82  ? 840  LEU C CG  1 
ATOM   13640 C  CD1 . LEU B  1 840 ? 9.567   -8.380  44.976  1.00 73.78  ? 840  LEU C CD1 1 
ATOM   13641 C  CD2 . LEU B  1 840 ? 10.136  -7.169  42.835  1.00 65.49  ? 840  LEU C CD2 1 
ATOM   13642 N  N   . ILE B  1 841 ? 14.834  -8.712  44.638  1.00 74.68  ? 841  ILE C N   1 
ATOM   13643 C  CA  . ILE B  1 841 ? 16.088  -8.542  45.359  1.00 73.14  ? 841  ILE C CA  1 
ATOM   13644 C  C   . ILE B  1 841 ? 17.232  -8.149  44.436  1.00 72.49  ? 841  ILE C C   1 
ATOM   13645 O  O   . ILE B  1 841 ? 18.022  -7.267  44.769  1.00 72.80  ? 841  ILE C O   1 
ATOM   13646 C  CB  . ILE B  1 841 ? 16.479  -9.816  46.116  1.00 68.48  ? 841  ILE C CB  1 
ATOM   13647 C  CG1 . ILE B  1 841 ? 15.519  -10.045 47.274  1.00 68.15  ? 841  ILE C CG1 1 
ATOM   13648 C  CG2 . ILE B  1 841 ? 17.878  -9.694  46.676  1.00 66.58  ? 841  ILE C CG2 1 
ATOM   13649 C  CD1 . ILE B  1 841 ? 15.891  -11.203 48.138  1.00 68.60  ? 841  ILE C CD1 1 
ATOM   13650 N  N   . GLU B  1 842 ? 17.308  -8.792  43.272  1.00 77.25  ? 842  GLU C N   1 
ATOM   13651 C  CA  . GLU B  1 842 ? 18.399  -8.546  42.327  1.00 76.17  ? 842  GLU C CA  1 
ATOM   13652 C  C   . GLU B  1 842 ? 18.356  -7.114  41.780  1.00 72.44  ? 842  GLU C C   1 
ATOM   13653 O  O   . GLU B  1 842 ? 19.378  -6.421  41.747  1.00 70.41  ? 842  GLU C O   1 
ATOM   13654 C  CB  . GLU B  1 842 ? 18.357  -9.576  41.184  1.00 76.78  ? 842  GLU C CB  1 
ATOM   13655 C  CG  . GLU B  1 842 ? 18.866  -10.976 41.594  1.00 84.32  ? 842  GLU C CG  1 
ATOM   13656 C  CD  . GLU B  1 842 ? 18.540  -12.089 40.587  1.00 87.65  ? 842  GLU C CD  1 
ATOM   13657 O  OE1 . GLU B  1 842 ? 19.010  -12.029 39.428  1.00 78.71  ? 842  GLU C OE1 1 
ATOM   13658 O  OE2 . GLU B  1 842 ? 17.816  -13.038 40.967  1.00 90.06  ? 842  GLU C OE2 1 
ATOM   13659 N  N   . LEU B  1 843 ? 17.166  -6.680  41.374  1.00 68.70  ? 843  LEU C N   1 
ATOM   13660 C  CA  . LEU B  1 843 ? 16.946  -5.333  40.858  1.00 66.64  ? 843  LEU C CA  1 
ATOM   13661 C  C   . LEU B  1 843 ? 17.378  -4.247  41.840  1.00 68.29  ? 843  LEU C C   1 
ATOM   13662 O  O   . LEU B  1 843 ? 17.919  -3.214  41.453  1.00 67.71  ? 843  LEU C O   1 
ATOM   13663 C  CB  . LEU B  1 843 ? 15.472  -5.150  40.517  1.00 67.68  ? 843  LEU C CB  1 
ATOM   13664 C  CG  . LEU B  1 843 ? 14.888  -6.122  39.497  1.00 70.85  ? 843  LEU C CG  1 
ATOM   13665 C  CD1 . LEU B  1 843 ? 13.407  -6.335  39.765  1.00 67.98  ? 843  LEU C CD1 1 
ATOM   13666 C  CD2 . LEU B  1 843 ? 15.122  -5.587  38.090  1.00 57.09  ? 843  LEU C CD2 1 
ATOM   13667 N  N   . GLY B  1 844 ? 17.110  -4.482  43.117  1.00 71.15  ? 844  GLY C N   1 
ATOM   13668 C  CA  . GLY B  1 844 ? 17.496  -3.551  44.155  1.00 71.18  ? 844  GLY C CA  1 
ATOM   13669 C  C   . GLY B  1 844 ? 19.001  -3.571  44.343  1.00 72.90  ? 844  GLY C C   1 
ATOM   13670 O  O   . GLY B  1 844 ? 19.607  -2.543  44.646  1.00 69.49  ? 844  GLY C O   1 
ATOM   13671 N  N   . MET B  1 845 ? 19.603  -4.744  44.157  1.00 68.64  ? 845  MET C N   1 
ATOM   13672 C  CA  . MET B  1 845 ? 21.050  -4.889  44.247  1.00 66.75  ? 845  MET C CA  1 
ATOM   13673 C  C   . MET B  1 845 ? 21.750  -4.298  43.026  1.00 71.57  ? 845  MET C C   1 
ATOM   13674 O  O   . MET B  1 845 ? 22.973  -4.148  43.022  1.00 72.62  ? 845  MET C O   1 
ATOM   13675 C  CB  . MET B  1 845 ? 21.437  -6.354  44.400  1.00 63.27  ? 845  MET C CB  1 
ATOM   13676 C  CG  . MET B  1 845 ? 21.692  -6.785  45.824  1.00 61.60  ? 845  MET C CG  1 
ATOM   13677 S  SD  . MET B  1 845 ? 23.272  -6.170  46.439  1.00 69.49  ? 845  MET C SD  1 
ATOM   13678 C  CE  . MET B  1 845 ? 24.293  -6.389  44.977  1.00 73.70  ? 845  MET C CE  1 
ATOM   13679 N  N   . GLU B  1 846 ? 20.985  -3.966  41.991  1.00 63.99  ? 846  GLU C N   1 
ATOM   13680 C  CA  . GLU B  1 846 ? 21.571  -3.292  40.839  1.00 72.53  ? 846  GLU C CA  1 
ATOM   13681 C  C   . GLU B  1 846 ? 21.264  -1.791  40.847  1.00 66.61  ? 846  GLU C C   1 
ATOM   13682 O  O   . GLU B  1 846 ? 21.933  -1.020  40.176  1.00 70.16  ? 846  GLU C O   1 
ATOM   13683 C  CB  . GLU B  1 846 ? 21.091  -3.928  39.527  1.00 78.43  ? 846  GLU C CB  1 
ATOM   13684 C  CG  . GLU B  1 846 ? 19.775  -3.378  38.973  1.00 79.08  ? 846  GLU C CG  1 
ATOM   13685 C  CD  . GLU B  1 846 ? 19.476  -3.873  37.557  1.00 83.64  ? 846  GLU C CD  1 
ATOM   13686 O  OE1 . GLU B  1 846 ? 20.427  -4.226  36.823  1.00 75.42  ? 846  GLU C OE1 1 
ATOM   13687 O  OE2 . GLU B  1 846 ? 18.283  -3.905  37.181  1.00 87.55  ? 846  GLU C OE2 1 
ATOM   13688 N  N   . GLY B  1 847 ? 20.250  -1.380  41.598  1.00 66.63  ? 847  GLY C N   1 
ATOM   13689 C  CA  . GLY B  1 847 ? 19.988  0.035   41.805  1.00 63.41  ? 847  GLY C CA  1 
ATOM   13690 C  C   . GLY B  1 847 ? 19.415  0.798   40.630  1.00 71.43  ? 847  GLY C C   1 
ATOM   13691 O  O   . GLY B  1 847 ? 19.201  2.011   40.706  1.00 73.43  ? 847  GLY C O   1 
ATOM   13692 N  N   . LYS B  1 848 ? 19.152  0.098   39.535  1.00 74.66  ? 848  LYS C N   1 
ATOM   13693 C  CA  . LYS B  1 848 ? 18.637  0.759   38.350  1.00 68.29  ? 848  LYS C CA  1 
ATOM   13694 C  C   . LYS B  1 848 ? 17.108  0.843   38.398  1.00 63.99  ? 848  LYS C C   1 
ATOM   13695 O  O   . LYS B  1 848 ? 16.542  1.931   38.434  1.00 65.39  ? 848  LYS C O   1 
ATOM   13696 C  CB  . LYS B  1 848 ? 19.108  0.029   37.091  1.00 74.48  ? 848  LYS C CB  1 
ATOM   13697 C  CG  . LYS B  1 848 ? 19.584  0.946   35.965  1.00 87.01  ? 848  LYS C CG  1 
ATOM   13698 C  CD  . LYS B  1 848 ? 21.108  1.128   35.956  1.00 92.89  ? 848  LYS C CD  1 
ATOM   13699 C  CE  . LYS B  1 848 ? 21.545  2.084   34.838  1.00 98.84  ? 848  LYS C CE  1 
ATOM   13700 N  NZ  . LYS B  1 848 ? 23.027  2.273   34.730  1.00 94.96  ? 848  LYS C NZ  1 
ATOM   13701 N  N   . VAL B  1 849 ? 16.449  -0.310  38.417  1.00 67.37  ? 849  VAL C N   1 
ATOM   13702 C  CA  . VAL B  1 849 ? 14.988  -0.373  38.387  1.00 69.56  ? 849  VAL C CA  1 
ATOM   13703 C  C   . VAL B  1 849 ? 14.350  -0.009  39.726  1.00 67.16  ? 849  VAL C C   1 
ATOM   13704 O  O   . VAL B  1 849 ? 13.392  0.767   39.786  1.00 69.75  ? 849  VAL C O   1 
ATOM   13705 C  CB  . VAL B  1 849 ? 14.524  -1.775  37.990  1.00 74.73  ? 849  VAL C CB  1 
ATOM   13706 C  CG1 . VAL B  1 849 ? 13.028  -1.780  37.707  1.00 73.76  ? 849  VAL C CG1 1 
ATOM   13707 C  CG2 . VAL B  1 849 ? 15.309  -2.240  36.792  1.00 57.30  ? 849  VAL C CG2 1 
ATOM   13708 N  N   . ILE B  1 850 ? 14.884  -0.594  40.791  1.00 65.16  ? 850  ILE C N   1 
ATOM   13709 C  CA  . ILE B  1 850 ? 14.506  -0.264  42.159  1.00 63.49  ? 850  ILE C CA  1 
ATOM   13710 C  C   . ILE B  1 850 ? 15.684  0.412   42.857  1.00 60.42  ? 850  ILE C C   1 
ATOM   13711 O  O   . ILE B  1 850 ? 16.739  -0.200  42.993  1.00 54.91  ? 850  ILE C O   1 
ATOM   13712 C  CB  . ILE B  1 850 ? 14.104  -1.530  42.935  1.00 59.97  ? 850  ILE C CB  1 
ATOM   13713 C  CG1 . ILE B  1 850 ? 12.787  -2.075  42.397  1.00 60.30  ? 850  ILE C CG1 1 
ATOM   13714 C  CG2 . ILE B  1 850 ? 14.010  -1.254  44.417  1.00 56.58  ? 850  ILE C CG2 1 
ATOM   13715 C  CD1 . ILE B  1 850 ? 12.539  -3.496  42.794  1.00 61.64  ? 850  ILE C CD1 1 
ATOM   13716 N  N   . LYS B  1 851 ? 15.514  1.660   43.295  1.00 60.05  ? 851  LYS C N   1 
ATOM   13717 C  CA  . LYS B  1 851 ? 16.605  2.388   43.951  1.00 53.97  ? 851  LYS C CA  1 
ATOM   13718 C  C   . LYS B  1 851 ? 17.161  1.585   45.117  1.00 56.69  ? 851  LYS C C   1 
ATOM   13719 O  O   . LYS B  1 851 ? 16.442  0.792   45.724  1.00 58.91  ? 851  LYS C O   1 
ATOM   13720 C  CB  . LYS B  1 851 ? 16.133  3.740   44.456  1.00 59.53  ? 851  LYS C CB  1 
ATOM   13721 C  CG  . LYS B  1 851 ? 15.192  4.476   43.527  1.00 64.10  ? 851  LYS C CG  1 
ATOM   13722 C  CD  . LYS B  1 851 ? 15.957  5.153   42.425  1.00 67.00  ? 851  LYS C CD  1 
ATOM   13723 C  CE  . LYS B  1 851 ? 15.551  6.622   42.293  1.00 59.70  ? 851  LYS C CE  1 
ATOM   13724 N  NZ  . LYS B  1 851 ? 16.493  7.310   41.368  1.00 46.73  ? 851  LYS C NZ  1 
ATOM   13725 N  N   . THR B  1 852 ? 18.433  1.771   45.443  1.00 57.51  ? 852  THR C N   1 
ATOM   13726 C  CA  . THR B  1 852 ? 19.015  1.010   46.550  1.00 60.37  ? 852  THR C CA  1 
ATOM   13727 C  C   . THR B  1 852 ? 18.607  1.582   47.921  1.00 57.74  ? 852  THR C C   1 
ATOM   13728 O  O   . THR B  1 852 ? 18.762  0.921   48.956  1.00 56.04  ? 852  THR C O   1 
ATOM   13729 C  CB  . THR B  1 852 ? 20.545  0.957   46.447  1.00 59.22  ? 852  THR C CB  1 
ATOM   13730 O  OG1 . THR B  1 852 ? 21.075  2.282   46.545  1.00 67.99  ? 852  THR C OG1 1 
ATOM   13731 C  CG2 . THR B  1 852 ? 20.961  0.365   45.124  1.00 61.05  ? 852  THR C CG2 1 
ATOM   13732 N  N   . GLN B  1 853 ? 18.058  2.796   47.921  1.00 54.72  ? 853  GLN C N   1 
ATOM   13733 C  CA  . GLN B  1 853 ? 17.443  3.369   49.129  1.00 59.86  ? 853  GLN C CA  1 
ATOM   13734 C  C   . GLN B  1 853 ? 16.256  2.507   49.601  1.00 58.56  ? 853  GLN C C   1 
ATOM   13735 O  O   . GLN B  1 853 ? 15.703  2.722   50.683  1.00 56.30  ? 853  GLN C O   1 
ATOM   13736 C  CB  . GLN B  1 853 ? 16.977  4.827   48.889  1.00 52.91  ? 853  GLN C CB  1 
ATOM   13737 C  CG  . GLN B  1 853 ? 15.712  4.958   48.036  1.00 54.46  ? 853  GLN C CG  1 
ATOM   13738 C  CD  . GLN B  1 853 ? 15.175  6.386   47.915  1.00 58.89  ? 853  GLN C CD  1 
ATOM   13739 O  OE1 . GLN B  1 853 ? 15.743  7.345   48.448  1.00 57.32  ? 853  GLN C OE1 1 
ATOM   13740 N  NE2 . GLN B  1 853 ? 14.069  6.526   47.197  1.00 55.40  ? 853  GLN C NE2 1 
ATOM   13741 N  N   . ASN B  1 854 ? 15.864  1.537   48.779  1.00 55.41  ? 854  ASN C N   1 
ATOM   13742 C  CA  . ASN B  1 854 ? 14.765  0.653   49.121  1.00 53.64  ? 854  ASN C CA  1 
ATOM   13743 C  C   . ASN B  1 854 ? 15.237  -0.756  49.396  1.00 52.24  ? 854  ASN C C   1 
ATOM   13744 O  O   . ASN B  1 854 ? 14.446  -1.590  49.823  1.00 57.99  ? 854  ASN C O   1 
ATOM   13745 C  CB  . ASN B  1 854 ? 13.721  0.630   48.007  1.00 48.92  ? 854  ASN C CB  1 
ATOM   13746 C  CG  . ASN B  1 854 ? 13.056  1.973   47.808  1.00 54.02  ? 854  ASN C CG  1 
ATOM   13747 O  OD1 . ASN B  1 854 ? 13.049  2.818   48.705  1.00 53.79  ? 854  ASN C OD1 1 
ATOM   13748 N  ND2 . ASN B  1 854 ? 12.482  2.176   46.634  1.00 54.85  ? 854  ASN C ND2 1 
ATOM   13749 N  N   . LEU B  1 855 ? 16.518  -1.023  49.165  1.00 49.67  ? 855  LEU C N   1 
ATOM   13750 C  CA  . LEU B  1 855 ? 17.007  -2.395  49.215  1.00 53.57  ? 855  LEU C CA  1 
ATOM   13751 C  C   . LEU B  1 855 ? 16.736  -3.027  50.566  1.00 55.90  ? 855  LEU C C   1 
ATOM   13752 O  O   . LEU B  1 855 ? 16.113  -4.081  50.651  1.00 54.62  ? 855  LEU C O   1 
ATOM   13753 C  CB  . LEU B  1 855 ? 18.496  -2.468  48.908  1.00 51.03  ? 855  LEU C CB  1 
ATOM   13754 C  CG  . LEU B  1 855 ? 18.966  -3.919  48.911  1.00 55.41  ? 855  LEU C CG  1 
ATOM   13755 C  CD1 . LEU B  1 855 ? 18.200  -4.713  47.868  1.00 58.39  ? 855  LEU C CD1 1 
ATOM   13756 C  CD2 . LEU B  1 855 ? 20.452  -4.026  48.670  1.00 50.27  ? 855  LEU C CD2 1 
ATOM   13757 N  N   . ALA B  1 856 ? 17.176  -2.351  51.621  1.00 59.40  ? 856  ALA C N   1 
ATOM   13758 C  CA  . ALA B  1 856 ? 16.991  -2.829  52.991  1.00 59.59  ? 856  ALA C CA  1 
ATOM   13759 C  C   . ALA B  1 856 ? 15.527  -3.144  53.323  1.00 57.53  ? 856  ALA C C   1 
ATOM   13760 O  O   . ALA B  1 856 ? 15.208  -4.238  53.780  1.00 62.92  ? 856  ALA C O   1 
ATOM   13761 C  CB  . ALA B  1 856 ? 17.540  -1.812  53.961  1.00 54.08  ? 856  ALA C CB  1 
ATOM   13762 N  N   . ALA B  1 857 ? 14.645  -2.186  53.081  1.00 56.31  ? 857  ALA C N   1 
ATOM   13763 C  CA  . ALA B  1 857 ? 13.236  -2.354  53.388  1.00 61.49  ? 857  ALA C CA  1 
ATOM   13764 C  C   . ALA B  1 857 ? 12.645  -3.501  52.591  1.00 61.30  ? 857  ALA C C   1 
ATOM   13765 O  O   . ALA B  1 857 ? 11.644  -4.087  52.988  1.00 61.01  ? 857  ALA C O   1 
ATOM   13766 C  CB  . ALA B  1 857 ? 12.477  -1.074  53.108  1.00 60.99  ? 857  ALA C CB  1 
ATOM   13767 N  N   . LEU B  1 858 ? 13.259  -3.812  51.459  1.00 57.80  ? 858  LEU C N   1 
ATOM   13768 C  CA  . LEU B  1 858 ? 12.776  -4.904  50.633  1.00 62.92  ? 858  LEU C CA  1 
ATOM   13769 C  C   . LEU B  1 858 ? 13.177  -6.242  51.272  1.00 66.98  ? 858  LEU C C   1 
ATOM   13770 O  O   . LEU B  1 858 ? 12.339  -7.143  51.414  1.00 66.79  ? 858  LEU C O   1 
ATOM   13771 C  CB  . LEU B  1 858 ? 13.308  -4.776  49.204  1.00 56.67  ? 858  LEU C CB  1 
ATOM   13772 C  CG  . LEU B  1 858 ? 12.805  -5.746  48.134  1.00 67.52  ? 858  LEU C CG  1 
ATOM   13773 C  CD1 . LEU B  1 858 ? 11.321  -6.014  48.268  1.00 70.52  ? 858  LEU C CD1 1 
ATOM   13774 C  CD2 . LEU B  1 858 ? 13.104  -5.196  46.750  1.00 63.57  ? 858  LEU C CD2 1 
ATOM   13775 N  N   . LEU B  1 859 ? 14.440  -6.362  51.682  1.00 57.62  ? 859  LEU C N   1 
ATOM   13776 C  CA  . LEU B  1 859 ? 14.894  -7.565  52.360  1.00 56.77  ? 859  LEU C CA  1 
ATOM   13777 C  C   . LEU B  1 859 ? 14.033  -7.805  53.587  1.00 66.57  ? 859  LEU C C   1 
ATOM   13778 O  O   . LEU B  1 859 ? 13.507  -8.902  53.785  1.00 70.74  ? 859  LEU C O   1 
ATOM   13779 C  CB  . LEU B  1 859 ? 16.374  -7.471  52.753  1.00 56.54  ? 859  LEU C CB  1 
ATOM   13780 C  CG  . LEU B  1 859 ? 17.397  -7.871  51.677  1.00 57.09  ? 859  LEU C CG  1 
ATOM   13781 C  CD1 . LEU B  1 859 ? 17.503  -6.788  50.671  1.00 60.09  ? 859  LEU C CD1 1 
ATOM   13782 C  CD2 . LEU B  1 859 ? 18.779  -8.159  52.232  1.00 58.58  ? 859  LEU C CD2 1 
ATOM   13783 N  N   . HIS B  1 860 ? 13.872  -6.755  54.387  1.00 66.63  ? 860  HIS C N   1 
ATOM   13784 C  CA  . HIS B  1 860 ? 13.046  -6.788  55.588  1.00 63.65  ? 860  HIS C CA  1 
ATOM   13785 C  C   . HIS B  1 860 ? 11.609  -7.223  55.314  1.00 65.73  ? 860  HIS C C   1 
ATOM   13786 O  O   . HIS B  1 860 ? 10.975  -7.860  56.153  1.00 66.39  ? 860  HIS C O   1 
ATOM   13787 C  CB  . HIS B  1 860 ? 13.040  -5.410  56.245  1.00 65.73  ? 860  HIS C CB  1 
ATOM   13788 C  CG  . HIS B  1 860 ? 12.349  -5.375  57.572  1.00 63.41  ? 860  HIS C CG  1 
ATOM   13789 N  ND1 . HIS B  1 860 ? 10.978  -5.366  57.698  1.00 65.59  ? 860  HIS C ND1 1 
ATOM   13790 C  CD2 . HIS B  1 860 ? 12.843  -5.334  58.833  1.00 67.82  ? 860  HIS C CD2 1 
ATOM   13791 C  CE1 . HIS B  1 860 ? 10.656  -5.326  58.979  1.00 66.49  ? 860  HIS C CE1 1 
ATOM   13792 N  NE2 . HIS B  1 860 ? 11.769  -5.303  59.689  1.00 65.16  ? 860  HIS C NE2 1 
ATOM   13793 N  N   . ALA B  1 861 ? 11.094  -6.863  54.143  1.00 64.71  ? 861  ALA C N   1 
ATOM   13794 C  CA  . ALA B  1 861 ? 9.723   -7.184  53.789  1.00 64.11  ? 861  ALA C CA  1 
ATOM   13795 C  C   . ALA B  1 861 ? 9.599   -8.650  53.410  1.00 67.64  ? 861  ALA C C   1 
ATOM   13796 O  O   . ALA B  1 861 ? 8.629   -9.312  53.763  1.00 66.09  ? 861  ALA C O   1 
ATOM   13797 C  CB  . ALA B  1 861 ? 9.245   -6.294  52.657  1.00 59.96  ? 861  ALA C CB  1 
ATOM   13798 N  N   . ILE B  1 862 ? 10.595  -9.144  52.686  1.00 70.07  ? 862  ILE C N   1 
ATOM   13799 C  CA  . ILE B  1 862 ? 10.603  -10.518 52.210  1.00 68.67  ? 862  ILE C CA  1 
ATOM   13800 C  C   . ILE B  1 862 ? 10.903  -11.510 53.337  1.00 73.55  ? 862  ILE C C   1 
ATOM   13801 O  O   . ILE B  1 862 ? 10.245  -12.545 53.456  1.00 73.74  ? 862  ILE C O   1 
ATOM   13802 C  CB  . ILE B  1 862 ? 11.633  -10.701 51.097  1.00 66.22  ? 862  ILE C CB  1 
ATOM   13803 C  CG1 . ILE B  1 862 ? 11.321  -9.775  49.935  1.00 63.34  ? 862  ILE C CG1 1 
ATOM   13804 C  CG2 . ILE B  1 862 ? 11.652  -12.126 50.614  1.00 66.00  ? 862  ILE C CG2 1 
ATOM   13805 C  CD1 . ILE B  1 862 ? 12.448  -9.688  48.962  1.00 59.59  ? 862  ILE C CD1 1 
ATOM   13806 N  N   . ALA B  1 863 ? 11.887  -11.180 54.171  1.00 71.74  ? 863  ALA C N   1 
ATOM   13807 C  CA  . ALA B  1 863 ? 12.256  -12.017 55.312  1.00 73.33  ? 863  ALA C CA  1 
ATOM   13808 C  C   . ALA B  1 863 ? 11.114  -12.147 56.318  1.00 73.37  ? 863  ALA C C   1 
ATOM   13809 O  O   . ALA B  1 863 ? 11.162  -12.995 57.217  1.00 69.05  ? 863  ALA C O   1 
ATOM   13810 C  CB  . ALA B  1 863 ? 13.492  -11.450 56.000  1.00 66.90  ? 863  ALA C CB  1 
ATOM   13811 N  N   . ARG B  1 864 ? 10.102  -11.295 56.149  1.00 71.85  ? 864  ARG C N   1 
ATOM   13812 C  CA  . ARG B  1 864 ? 8.981   -11.153 57.078  1.00 75.99  ? 864  ARG C CA  1 
ATOM   13813 C  C   . ARG B  1 864 ? 7.956   -12.262 56.920  1.00 80.11  ? 864  ARG C C   1 
ATOM   13814 O  O   . ARG B  1 864 ? 7.280   -12.639 57.877  1.00 78.53  ? 864  ARG C O   1 
ATOM   13815 C  CB  . ARG B  1 864 ? 8.300   -9.802  56.867  1.00 74.38  ? 864  ARG C CB  1 
ATOM   13816 C  CG  . ARG B  1 864 ? 8.162   -8.975  58.122  1.00 74.03  ? 864  ARG C CG  1 
ATOM   13817 C  CD  . ARG B  1 864 ? 8.325   -7.508  57.803  1.00 73.30  ? 864  ARG C CD  1 
ATOM   13818 N  NE  . ARG B  1 864 ? 7.178   -6.939  57.105  1.00 75.59  ? 864  ARG C NE  1 
ATOM   13819 C  CZ  . ARG B  1 864 ? 7.205   -5.773  56.462  1.00 84.04  ? 864  ARG C CZ  1 
ATOM   13820 N  NH1 . ARG B  1 864 ? 8.325   -5.064  56.411  1.00 85.17  ? 864  ARG C NH1 1 
ATOM   13821 N  NH2 . ARG B  1 864 ? 6.117   -5.319  55.857  1.00 89.34  ? 864  ARG C NH2 1 
ATOM   13822 N  N   . ARG B  1 865 ? 7.837   -12.756 55.691  1.00 82.31  ? 865  ARG C N   1 
ATOM   13823 C  CA  . ARG B  1 865 ? 7.004   -13.907 55.381  1.00 77.21  ? 865  ARG C CA  1 
ATOM   13824 C  C   . ARG B  1 865 ? 7.841   -15.173 55.495  1.00 83.40  ? 865  ARG C C   1 
ATOM   13825 O  O   . ARG B  1 865 ? 9.060   -15.124 55.333  1.00 85.48  ? 865  ARG C O   1 
ATOM   13826 C  CB  . ARG B  1 865 ? 6.414   -13.776 53.980  1.00 76.06  ? 865  ARG C CB  1 
ATOM   13827 C  CG  . ARG B  1 865 ? 5.599   -12.513 53.789  1.00 78.64  ? 865  ARG C CG  1 
ATOM   13828 C  CD  . ARG B  1 865 ? 5.060   -12.423 52.381  1.00 85.70  ? 865  ARG C CD  1 
ATOM   13829 N  NE  . ARG B  1 865 ? 3.813   -11.667 52.320  1.00 83.48  ? 865  ARG C NE  1 
ATOM   13830 C  CZ  . ARG B  1 865 ? 2.607   -12.214 52.420  1.00 83.85  ? 865  ARG C CZ  1 
ATOM   13831 N  NH1 . ARG B  1 865 ? 2.489   -13.527 52.591  1.00 85.15  ? 865  ARG C NH1 1 
ATOM   13832 N  NH2 . ARG B  1 865 ? 1.523   -11.449 52.354  1.00 82.16  ? 865  ARG C NH2 1 
ATOM   13833 N  N   . PRO B  1 866 ? 7.198   -16.310 55.794  1.00 86.90  ? 866  PRO C N   1 
ATOM   13834 C  CA  . PRO B  1 866 ? 7.969   -17.553 55.918  1.00 88.59  ? 866  PRO C CA  1 
ATOM   13835 C  C   . PRO B  1 866 ? 8.490   -18.055 54.571  1.00 86.22  ? 866  PRO C C   1 
ATOM   13836 O  O   . PRO B  1 866 ? 9.529   -18.725 54.530  1.00 83.81  ? 866  PRO C O   1 
ATOM   13837 C  CB  . PRO B  1 866 ? 6.961   -18.535 56.520  1.00 85.11  ? 866  PRO C CB  1 
ATOM   13838 C  CG  . PRO B  1 866 ? 5.902   -17.680 57.124  1.00 87.23  ? 866  PRO C CG  1 
ATOM   13839 C  CD  . PRO B  1 866 ? 5.809   -16.480 56.244  1.00 82.79  ? 866  PRO C CD  1 
ATOM   13840 N  N   . LYS B  1 867 ? 7.790   -17.730 53.487  1.00 80.57  ? 867  LYS C N   1 
ATOM   13841 C  CA  . LYS B  1 867 ? 8.241   -18.173 52.174  1.00 88.44  ? 867  LYS C CA  1 
ATOM   13842 C  C   . LYS B  1 867 ? 9.565   -17.517 51.784  1.00 90.40  ? 867  LYS C C   1 
ATOM   13843 O  O   . LYS B  1 867 ? 10.465  -18.180 51.257  1.00 85.95  ? 867  LYS C O   1 
ATOM   13844 C  CB  . LYS B  1 867 ? 7.191   -17.889 51.103  1.00 88.65  ? 867  LYS C CB  1 
ATOM   13845 C  CG  . LYS B  1 867 ? 7.526   -18.547 49.767  1.00 90.73  ? 867  LYS C CG  1 
ATOM   13846 C  CD  . LYS B  1 867 ? 7.863   -20.021 49.985  1.00 97.01  ? 867  LYS C CD  1 
ATOM   13847 C  CE  . LYS B  1 867 ? 8.374   -20.723 48.730  1.00 88.67  ? 867  LYS C CE  1 
ATOM   13848 N  NZ  . LYS B  1 867 ? 8.931   -22.060 49.090  1.00 73.11  ? 867  LYS C NZ  1 
ATOM   13849 N  N   . GLY B  1 868 ? 9.687   -16.218 52.048  1.00 86.46  ? 868  GLY C N   1 
ATOM   13850 C  CA  . GLY B  1 868 ? 10.898  -15.493 51.704  1.00 84.53  ? 868  GLY C CA  1 
ATOM   13851 C  C   . GLY B  1 868 ? 11.959  -15.522 52.789  1.00 79.15  ? 868  GLY C C   1 
ATOM   13852 O  O   . GLY B  1 868 ? 13.096  -15.107 52.574  1.00 78.62  ? 868  GLY C O   1 
ATOM   13853 N  N   . GLN B  1 869 ? 11.584  -16.037 53.952  1.00 81.28  ? 869  GLN C N   1 
ATOM   13854 C  CA  . GLN B  1 869 ? 12.429  -16.005 55.143  1.00 80.48  ? 869  GLN C CA  1 
ATOM   13855 C  C   . GLN B  1 869 ? 13.799  -16.661 54.997  1.00 75.99  ? 869  GLN C C   1 
ATOM   13856 O  O   . GLN B  1 869 ? 14.803  -16.115 55.467  1.00 72.78  ? 869  GLN C O   1 
ATOM   13857 C  CB  . GLN B  1 869 ? 11.692  -16.666 56.302  1.00 81.21  ? 869  GLN C CB  1 
ATOM   13858 C  CG  . GLN B  1 869 ? 12.594  -17.078 57.446  1.00 89.34  ? 869  GLN C CG  1 
ATOM   13859 C  CD  . GLN B  1 869 ? 11.808  -17.411 58.687  1.00 87.97  ? 869  GLN C CD  1 
ATOM   13860 O  OE1 . GLN B  1 869 ? 10.818  -16.750 58.995  1.00 84.89  ? 869  GLN C OE1 1 
ATOM   13861 N  NE2 . GLN B  1 869 ? 12.231  -18.447 59.400  1.00 85.76  ? 869  GLN C NE2 1 
ATOM   13862 N  N   . GLN B  1 870 ? 13.841  -17.835 54.373  1.00 78.75  ? 870  GLN C N   1 
ATOM   13863 C  CA  . GLN B  1 870 ? 15.104  -18.558 54.241  1.00 78.24  ? 870  GLN C CA  1 
ATOM   13864 C  C   . GLN B  1 870 ? 15.931  -17.921 53.139  1.00 67.55  ? 870  GLN C C   1 
ATOM   13865 O  O   . GLN B  1 870 ? 17.157  -17.896 53.195  1.00 65.97  ? 870  GLN C O   1 
ATOM   13866 C  CB  . GLN B  1 870 ? 14.870  -20.046 53.946  1.00 71.40  ? 870  GLN C CB  1 
ATOM   13867 C  CG  . GLN B  1 870 ? 16.157  -20.856 53.799  1.00 63.24  ? 870  GLN C CG  1 
ATOM   13868 C  CD  . GLN B  1 870 ? 16.914  -21.010 55.106  1.00 70.35  ? 870  GLN C CD  1 
ATOM   13869 O  OE1 . GLN B  1 870 ? 16.334  -21.335 56.145  1.00 72.05  ? 870  GLN C OE1 1 
ATOM   13870 N  NE2 . GLN B  1 870 ? 18.221  -20.775 55.062  1.00 73.92  ? 870  GLN C NE2 1 
ATOM   13871 N  N   . LEU B  1 871 ? 15.234  -17.393 52.146  1.00 65.89  ? 871  LEU C N   1 
ATOM   13872 C  CA  . LEU B  1 871 ? 15.861  -16.754 51.001  1.00 73.46  ? 871  LEU C CA  1 
ATOM   13873 C  C   . LEU B  1 871 ? 16.648  -15.483 51.364  1.00 73.29  ? 871  LEU C C   1 
ATOM   13874 O  O   . LEU B  1 871 ? 17.815  -15.339 50.995  1.00 67.94  ? 871  LEU C O   1 
ATOM   13875 C  CB  . LEU B  1 871 ? 14.790  -16.426 49.972  1.00 74.48  ? 871  LEU C CB  1 
ATOM   13876 C  CG  . LEU B  1 871 ? 15.310  -15.715 48.742  1.00 77.36  ? 871  LEU C CG  1 
ATOM   13877 C  CD1 . LEU B  1 871 ? 16.473  -16.518 48.196  1.00 83.39  ? 871  LEU C CD1 1 
ATOM   13878 C  CD2 . LEU B  1 871 ? 14.181  -15.593 47.730  1.00 80.78  ? 871  LEU C CD2 1 
ATOM   13879 N  N   . ALA B  1 872 ? 15.993  -14.568 52.074  1.00 69.63  ? 872  ALA C N   1 
ATOM   13880 C  CA  . ALA B  1 872 ? 16.629  -13.339 52.552  1.00 73.88  ? 872  ALA C CA  1 
ATOM   13881 C  C   . ALA B  1 872 ? 17.836  -13.634 53.430  1.00 65.69  ? 872  ALA C C   1 
ATOM   13882 O  O   . ALA B  1 872 ? 18.878  -12.996 53.312  1.00 54.43  ? 872  ALA C O   1 
ATOM   13883 C  CB  . ALA B  1 872 ? 15.622  -12.480 53.326  1.00 72.18  ? 872  ALA C CB  1 
ATOM   13884 N  N   . TRP B  1 873 ? 17.680  -14.609 54.314  1.00 68.55  ? 873  TRP C N   1 
ATOM   13885 C  CA  . TRP B  1 873 ? 18.734  -14.960 55.244  1.00 63.98  ? 873  TRP C CA  1 
ATOM   13886 C  C   . TRP B  1 873 ? 19.927  -15.545 54.513  1.00 65.81  ? 873  TRP C C   1 
ATOM   13887 O  O   . TRP B  1 873 ? 21.071  -15.193 54.804  1.00 64.17  ? 873  TRP C O   1 
ATOM   13888 C  CB  . TRP B  1 873 ? 18.205  -15.932 56.290  1.00 65.49  ? 873  TRP C CB  1 
ATOM   13889 C  CG  . TRP B  1 873 ? 19.241  -16.501 57.201  1.00 62.71  ? 873  TRP C CG  1 
ATOM   13890 C  CD1 . TRP B  1 873 ? 19.329  -17.789 57.602  1.00 67.31  ? 873  TRP C CD1 1 
ATOM   13891 C  CD2 . TRP B  1 873 ? 20.333  -15.810 57.829  1.00 69.29  ? 873  TRP C CD2 1 
ATOM   13892 N  NE1 . TRP B  1 873 ? 20.398  -17.956 58.441  1.00 69.64  ? 873  TRP C NE1 1 
ATOM   13893 C  CE2 . TRP B  1 873 ? 21.032  -16.755 58.599  1.00 71.45  ? 873  TRP C CE2 1 
ATOM   13894 C  CE3 . TRP B  1 873 ? 20.779  -14.486 57.826  1.00 68.48  ? 873  TRP C CE3 1 
ATOM   13895 C  CZ2 . TRP B  1 873 ? 22.157  -16.423 59.355  1.00 73.27  ? 873  TRP C CZ2 1 
ATOM   13896 C  CZ3 . TRP B  1 873 ? 21.896  -14.161 58.569  1.00 67.28  ? 873  TRP C CZ3 1 
ATOM   13897 C  CH2 . TRP B  1 873 ? 22.572  -15.125 59.326  1.00 71.45  ? 873  TRP C CH2 1 
ATOM   13898 N  N   . ASP B  1 874 ? 19.648  -16.435 53.561  1.00 66.18  ? 874  ASP C N   1 
ATOM   13899 C  CA  . ASP B  1 874 ? 20.685  -16.970 52.685  1.00 70.16  ? 874  ASP C CA  1 
ATOM   13900 C  C   . ASP B  1 874 ? 21.400  -15.815 51.993  1.00 68.93  ? 874  ASP C C   1 
ATOM   13901 O  O   . ASP B  1 874 ? 22.620  -15.702 52.059  1.00 65.82  ? 874  ASP C O   1 
ATOM   13902 C  CB  . ASP B  1 874 ? 20.103  -17.929 51.631  1.00 73.12  ? 874  ASP C CB  1 
ATOM   13903 C  CG  . ASP B  1 874 ? 19.719  -19.295 52.207  1.00 77.61  ? 874  ASP C CG  1 
ATOM   13904 O  OD1 . ASP B  1 874 ? 20.177  -19.623 53.326  1.00 75.11  ? 874  ASP C OD1 1 
ATOM   13905 O  OD2 . ASP B  1 874 ? 18.966  -20.041 51.527  1.00 70.81  ? 874  ASP C OD2 1 
ATOM   13906 N  N   . PHE B  1 875 ? 20.616  -14.950 51.357  1.00 64.81  ? 875  PHE C N   1 
ATOM   13907 C  CA  . PHE B  1 875 ? 21.141  -13.839 50.571  1.00 64.29  ? 875  PHE C CA  1 
ATOM   13908 C  C   . PHE B  1 875 ? 22.083  -12.908 51.318  1.00 65.70  ? 875  PHE C C   1 
ATOM   13909 O  O   . PHE B  1 875 ? 23.141  -12.554 50.808  1.00 67.36  ? 875  PHE C O   1 
ATOM   13910 C  CB  . PHE B  1 875 ? 20.008  -13.005 50.017  1.00 56.58  ? 875  PHE C CB  1 
ATOM   13911 C  CG  . PHE B  1 875 ? 20.458  -12.024 48.994  1.00 70.01  ? 875  PHE C CG  1 
ATOM   13912 C  CD1 . PHE B  1 875 ? 20.934  -10.782 49.365  1.00 72.32  ? 875  PHE C CD1 1 
ATOM   13913 C  CD2 . PHE B  1 875 ? 20.427  -12.351 47.655  1.00 71.49  ? 875  PHE C CD2 1 
ATOM   13914 C  CE1 . PHE B  1 875 ? 21.361  -9.888  48.416  1.00 69.71  ? 875  PHE C CE1 1 
ATOM   13915 C  CE2 . PHE B  1 875 ? 20.844  -11.457 46.705  1.00 63.37  ? 875  PHE C CE2 1 
ATOM   13916 C  CZ  . PHE B  1 875 ? 21.315  -10.228 47.087  1.00 65.85  ? 875  PHE C CZ  1 
ATOM   13917 N  N   . VAL B  1 876 ? 21.670  -12.473 52.502  1.00 67.50  ? 876  VAL C N   1 
ATOM   13918 C  CA  . VAL B  1 876 ? 22.498  -11.615 53.337  1.00 64.33  ? 876  VAL C CA  1 
ATOM   13919 C  C   . VAL B  1 876 ? 23.803  -12.328 53.674  1.00 70.56  ? 876  VAL C C   1 
ATOM   13920 O  O   . VAL B  1 876 ? 24.867  -11.962 53.177  1.00 69.21  ? 876  VAL C O   1 
ATOM   13921 C  CB  . VAL B  1 876 ? 21.772  -11.217 54.644  1.00 60.66  ? 876  VAL C CB  1 
ATOM   13922 C  CG1 . VAL B  1 876 ? 22.705  -10.448 55.571  1.00 64.57  ? 876  VAL C CG1 1 
ATOM   13923 C  CG2 . VAL B  1 876 ? 20.529  -10.413 54.339  1.00 55.72  ? 876  VAL C CG2 1 
ATOM   13924 N  N   . ARG B  1 877 ? 23.696  -13.364 54.504  1.00 72.03  ? 877  ARG C N   1 
ATOM   13925 C  CA  . ARG B  1 877 ? 24.820  -14.198 54.923  1.00 73.56  ? 877  ARG C CA  1 
ATOM   13926 C  C   . ARG B  1 877 ? 25.732  -14.606 53.748  1.00 76.11  ? 877  ARG C C   1 
ATOM   13927 O  O   . ARG B  1 877 ? 26.928  -14.853 53.936  1.00 75.13  ? 877  ARG C O   1 
ATOM   13928 C  CB  . ARG B  1 877 ? 24.273  -15.433 55.652  1.00 73.01  ? 877  ARG C CB  1 
ATOM   13929 C  CG  . ARG B  1 877 ? 25.308  -16.296 56.341  1.00 77.02  ? 877  ARG C CG  1 
ATOM   13930 C  CD  . ARG B  1 877 ? 24.635  -17.425 57.117  1.00 79.59  ? 877  ARG C CD  1 
ATOM   13931 N  NE  . ARG B  1 877 ? 23.496  -17.983 56.385  1.00 84.87  ? 877  ARG C NE  1 
ATOM   13932 C  CZ  . ARG B  1 877 ? 22.827  -19.077 56.747  1.00 75.61  ? 877  ARG C CZ  1 
ATOM   13933 N  NH1 . ARG B  1 877 ? 23.178  -19.743 57.842  1.00 73.71  ? 877  ARG C NH1 1 
ATOM   13934 N  NH2 . ARG B  1 877 ? 21.805  -19.502 56.013  1.00 68.61  ? 877  ARG C NH2 1 
ATOM   13935 N  N   . GLU B  1 878 ? 25.151  -14.650 52.545  1.00 73.60  ? 878  GLU C N   1 
ATOM   13936 C  CA  . GLU B  1 878 ? 25.866  -14.899 51.291  1.00 73.39  ? 878  GLU C CA  1 
ATOM   13937 C  C   . GLU B  1 878 ? 26.642  -13.689 50.789  1.00 75.20  ? 878  GLU C C   1 
ATOM   13938 O  O   . GLU B  1 878 ? 27.868  -13.699 50.769  1.00 80.87  ? 878  GLU C O   1 
ATOM   13939 C  CB  . GLU B  1 878 ? 24.880  -15.314 50.206  1.00 77.34  ? 878  GLU C CB  1 
ATOM   13940 C  CG  . GLU B  1 878 ? 25.319  -16.444 49.308  1.00 81.60  ? 878  GLU C CG  1 
ATOM   13941 C  CD  . GLU B  1 878 ? 24.194  -16.880 48.383  1.00 90.46  ? 878  GLU C CD  1 
ATOM   13942 O  OE1 . GLU B  1 878 ? 23.204  -17.468 48.873  1.00 89.13  ? 878  GLU C OE1 1 
ATOM   13943 O  OE2 . GLU B  1 878 ? 24.285  -16.610 47.167  1.00 100.10 ? 878  GLU C OE2 1 
ATOM   13944 N  N   . ASN B  1 879 ? 25.906  -12.653 50.381  1.00 78.22  ? 879  ASN C N   1 
ATOM   13945 C  CA  . ASN B  1 879 ? 26.456  -11.493 49.666  1.00 75.22  ? 879  ASN C CA  1 
ATOM   13946 C  C   . ASN B  1 879 ? 26.949  -10.344 50.528  1.00 70.63  ? 879  ASN C C   1 
ATOM   13947 O  O   . ASN B  1 879 ? 27.117  -9.236  50.028  1.00 72.71  ? 879  ASN C O   1 
ATOM   13948 C  CB  . ASN B  1 879 ? 25.405  -10.918 48.722  1.00 74.27  ? 879  ASN C CB  1 
ATOM   13949 C  CG  . ASN B  1 879 ? 24.847  -11.943 47.778  1.00 78.13  ? 879  ASN C CG  1 
ATOM   13950 O  OD1 . ASN B  1 879 ? 25.188  -11.954 46.597  1.00 84.47  ? 879  ASN C OD1 1 
ATOM   13951 N  ND2 . ASN B  1 879 ? 23.970  -12.809 48.286  1.00 76.75  ? 879  ASN C ND2 1 
ATOM   13952 N  N   . TRP B  1 880 ? 27.164  -10.604 51.810  1.00 72.13  ? 880  TRP C N   1 
ATOM   13953 C  CA  . TRP B  1 880 ? 27.484  -9.565  52.790  1.00 73.95  ? 880  TRP C CA  1 
ATOM   13954 C  C   . TRP B  1 880 ? 28.454  -8.514  52.280  1.00 69.87  ? 880  TRP C C   1 
ATOM   13955 O  O   . TRP B  1 880 ? 28.228  -7.317  52.423  1.00 69.58  ? 880  TRP C O   1 
ATOM   13956 C  CB  . TRP B  1 880 ? 28.066  -10.203 54.052  1.00 72.40  ? 880  TRP C CB  1 
ATOM   13957 C  CG  . TRP B  1 880 ? 28.597  -9.205  55.027  1.00 66.06  ? 880  TRP C CG  1 
ATOM   13958 C  CD1 . TRP B  1 880 ? 29.904  -8.864  55.222  1.00 63.00  ? 880  TRP C CD1 1 
ATOM   13959 C  CD2 . TRP B  1 880 ? 27.831  -8.407  55.939  1.00 71.68  ? 880  TRP C CD2 1 
ATOM   13960 N  NE1 . TRP B  1 880 ? 30.002  -7.909  56.203  1.00 68.05  ? 880  TRP C NE1 1 
ATOM   13961 C  CE2 . TRP B  1 880 ? 28.743  -7.609  56.661  1.00 71.31  ? 880  TRP C CE2 1 
ATOM   13962 C  CE3 . TRP B  1 880 ? 26.464  -8.292  56.221  1.00 64.73  ? 880  TRP C CE3 1 
ATOM   13963 C  CZ2 . TRP B  1 880 ? 28.330  -6.705  57.645  1.00 57.70  ? 880  TRP C CZ2 1 
ATOM   13964 C  CZ3 . TRP B  1 880 ? 26.062  -7.389  57.196  1.00 61.31  ? 880  TRP C CZ3 1 
ATOM   13965 C  CH2 . TRP B  1 880 ? 26.991  -6.608  57.890  1.00 50.71  ? 880  TRP C CH2 1 
ATOM   13966 N  N   . THR B  1 881 ? 29.532  -8.989  51.679  1.00 74.87  ? 881  THR C N   1 
ATOM   13967 C  CA  . THR B  1 881 ? 30.596  -8.129  51.200  1.00 74.86  ? 881  THR C CA  1 
ATOM   13968 C  C   . THR B  1 881 ? 30.062  -7.098  50.213  1.00 77.19  ? 881  THR C C   1 
ATOM   13969 O  O   . THR B  1 881 ? 30.408  -5.913  50.285  1.00 73.38  ? 881  THR C O   1 
ATOM   13970 C  CB  . THR B  1 881 ? 31.690  -8.962  50.548  1.00 73.38  ? 881  THR C CB  1 
ATOM   13971 O  OG1 . THR B  1 881 ? 31.090  -9.833  49.582  1.00 84.51  ? 881  THR C OG1 1 
ATOM   13972 C  CG2 . THR B  1 881 ? 32.397  -9.809  51.605  1.00 69.93  ? 881  THR C CG2 1 
ATOM   13973 N  N   . HIS B  1 882 ? 29.195  -7.554  49.314  1.00 73.37  ? 882  HIS C N   1 
ATOM   13974 C  CA  . HIS B  1 882 ? 28.596  -6.692  48.300  1.00 69.98  ? 882  HIS C CA  1 
ATOM   13975 C  C   . HIS B  1 882 ? 27.680  -5.634  48.916  1.00 71.78  ? 882  HIS C C   1 
ATOM   13976 O  O   . HIS B  1 882 ? 27.667  -4.480  48.485  1.00 73.55  ? 882  HIS C O   1 
ATOM   13977 C  CB  . HIS B  1 882 ? 27.829  -7.542  47.288  1.00 71.53  ? 882  HIS C CB  1 
ATOM   13978 C  CG  . HIS B  1 882 ? 28.641  -8.664  46.706  1.00 84.61  ? 882  HIS C CG  1 
ATOM   13979 N  ND1 . HIS B  1 882 ? 28.931  -9.817  47.407  1.00 78.91  ? 882  HIS C ND1 1 
ATOM   13980 C  CD2 . HIS B  1 882 ? 29.239  -8.798  45.498  1.00 77.88  ? 882  HIS C CD2 1 
ATOM   13981 C  CE1 . HIS B  1 882 ? 29.664  -10.616 46.653  1.00 78.12  ? 882  HIS C CE1 1 
ATOM   13982 N  NE2 . HIS B  1 882 ? 29.864  -10.022 45.490  1.00 82.21  ? 882  HIS C NE2 1 
ATOM   13983 N  N   . LEU B  1 883 ? 26.922  -6.032  49.931  1.00 67.56  ? 883  LEU C N   1 
ATOM   13984 C  CA  . LEU B  1 883 ? 26.043  -5.114  50.633  1.00 61.80  ? 883  LEU C CA  1 
ATOM   13985 C  C   . LEU B  1 883 ? 26.839  -4.083  51.413  1.00 64.02  ? 883  LEU C C   1 
ATOM   13986 O  O   . LEU B  1 883 ? 26.409  -2.945  51.585  1.00 63.78  ? 883  LEU C O   1 
ATOM   13987 C  CB  . LEU B  1 883 ? 25.128  -5.880  51.577  1.00 60.56  ? 883  LEU C CB  1 
ATOM   13988 C  CG  . LEU B  1 883 ? 24.092  -6.749  50.878  1.00 64.29  ? 883  LEU C CG  1 
ATOM   13989 C  CD1 . LEU B  1 883 ? 23.327  -7.619  51.896  1.00 63.76  ? 883  LEU C CD1 1 
ATOM   13990 C  CD2 . LEU B  1 883 ? 23.161  -5.846  50.103  1.00 54.65  ? 883  LEU C CD2 1 
ATOM   13991 N  N   . LEU B  1 884 ? 28.000  -4.500  51.898  1.00 62.79  ? 884  LEU C N   1 
ATOM   13992 C  CA  . LEU B  1 884 ? 28.849  -3.634  52.694  1.00 63.43  ? 884  LEU C CA  1 
ATOM   13993 C  C   . LEU B  1 884 ? 29.572  -2.595  51.833  1.00 68.11  ? 884  LEU C C   1 
ATOM   13994 O  O   . LEU B  1 884 ? 29.977  -1.551  52.328  1.00 67.70  ? 884  LEU C O   1 
ATOM   13995 C  CB  . LEU B  1 884 ? 29.865  -4.471  53.465  1.00 66.06  ? 884  LEU C CB  1 
ATOM   13996 C  CG  . LEU B  1 884 ? 30.463  -3.781  54.686  1.00 71.07  ? 884  LEU C CG  1 
ATOM   13997 C  CD1 . LEU B  1 884 ? 29.461  -3.793  55.831  1.00 66.00  ? 884  LEU C CD1 1 
ATOM   13998 C  CD2 . LEU B  1 884 ? 31.770  -4.438  55.086  1.00 69.82  ? 884  LEU C CD2 1 
ATOM   13999 N  N   . LYS B  1 885 ? 29.748  -2.899  50.549  1.00 70.58  ? 885  LYS C N   1 
ATOM   14000 C  CA  . LYS B  1 885 ? 30.327  -1.950  49.607  1.00 68.38  ? 885  LYS C CA  1 
ATOM   14001 C  C   . LYS B  1 885 ? 29.304  -0.881  49.298  1.00 67.55  ? 885  LYS C C   1 
ATOM   14002 O  O   . LYS B  1 885 ? 29.644  0.213   48.869  1.00 69.89  ? 885  LYS C O   1 
ATOM   14003 C  CB  . LYS B  1 885 ? 30.763  -2.632  48.307  1.00 75.00  ? 885  LYS C CB  1 
ATOM   14004 C  CG  . LYS B  1 885 ? 31.785  -3.748  48.462  1.00 81.38  ? 885  LYS C CG  1 
ATOM   14005 C  CD  . LYS B  1 885 ? 32.026  -4.467  47.133  1.00 82.42  ? 885  LYS C CD  1 
ATOM   14006 C  CE  . LYS B  1 885 ? 32.683  -3.543  46.117  1.00 87.23  ? 885  LYS C CE  1 
ATOM   14007 N  NZ  . LYS B  1 885 ? 34.007  -3.055  46.594  1.00 84.82  ? 885  LYS C NZ  1 
ATOM   14008 N  N   . LYS B  1 886 ? 28.040  -1.221  49.510  1.00 64.62  ? 886  LYS C N   1 
ATOM   14009 C  CA  . LYS B  1 886 ? 26.946  -0.300  49.277  1.00 58.52  ? 886  LYS C CA  1 
ATOM   14010 C  C   . LYS B  1 886 ? 26.632  0.553   50.509  1.00 58.22  ? 886  LYS C C   1 
ATOM   14011 O  O   . LYS B  1 886 ? 26.115  1.664   50.381  1.00 57.82  ? 886  LYS C O   1 
ATOM   14012 C  CB  . LYS B  1 886 ? 25.702  -1.073  48.845  1.00 57.53  ? 886  LYS C CB  1 
ATOM   14013 C  CG  . LYS B  1 886 ? 25.285  -0.791  47.426  1.00 62.20  ? 886  LYS C CG  1 
ATOM   14014 C  CD  . LYS B  1 886 ? 24.753  -2.040  46.731  1.00 75.27  ? 886  LYS C CD  1 
ATOM   14015 C  CE  . LYS B  1 886 ? 24.650  -1.816  45.219  1.00 74.83  ? 886  LYS C CE  1 
ATOM   14016 N  NZ  . LYS B  1 886 ? 24.404  -3.092  44.475  1.00 70.60  ? 886  LYS C NZ  1 
ATOM   14017 N  N   . PHE B  1 887 ? 26.946  0.041   51.697  1.00 60.66  ? 887  PHE C N   1 
ATOM   14018 C  CA  . PHE B  1 887 ? 26.538  0.702   52.939  1.00 56.45  ? 887  PHE C CA  1 
ATOM   14019 C  C   . PHE B  1 887 ? 27.645  0.854   54.010  1.00 62.36  ? 887  PHE C C   1 
ATOM   14020 O  O   . PHE B  1 887 ? 28.644  0.130   54.012  1.00 65.56  ? 887  PHE C O   1 
ATOM   14021 C  CB  . PHE B  1 887 ? 25.366  -0.058  53.555  1.00 52.81  ? 887  PHE C CB  1 
ATOM   14022 C  CG  . PHE B  1 887 ? 24.147  -0.142  52.670  1.00 55.31  ? 887  PHE C CG  1 
ATOM   14023 C  CD1 . PHE B  1 887 ? 23.411  0.988   52.364  1.00 54.29  ? 887  PHE C CD1 1 
ATOM   14024 C  CD2 . PHE B  1 887 ? 23.717  -1.365  52.174  1.00 55.08  ? 887  PHE C CD2 1 
ATOM   14025 C  CE1 . PHE B  1 887 ? 22.282  0.901   51.569  1.00 50.98  ? 887  PHE C CE1 1 
ATOM   14026 C  CE2 . PHE B  1 887 ? 22.591  -1.456  51.380  1.00 48.27  ? 887  PHE C CE2 1 
ATOM   14027 C  CZ  . PHE B  1 887 ? 21.873  -0.324  51.079  1.00 51.03  ? 887  PHE C CZ  1 
ATOM   14028 N  N   . ASP B  1 888 ? 27.444  1.814   54.913  1.00 62.30  ? 888  ASP C N   1 
ATOM   14029 C  CA  . ASP B  1 888 ? 28.198  1.921   56.169  1.00 62.49  ? 888  ASP C CA  1 
ATOM   14030 C  C   . ASP B  1 888 ? 27.866  0.778   57.129  1.00 58.58  ? 888  ASP C C   1 
ATOM   14031 O  O   . ASP B  1 888 ? 26.732  0.320   57.182  1.00 56.87  ? 888  ASP C O   1 
ATOM   14032 C  CB  . ASP B  1 888 ? 27.891  3.250   56.874  1.00 67.31  ? 888  ASP C CB  1 
ATOM   14033 C  CG  . ASP B  1 888 ? 28.493  4.446   56.171  1.00 66.10  ? 888  ASP C CG  1 
ATOM   14034 O  OD1 . ASP B  1 888 ? 28.790  4.328   54.965  1.00 65.95  ? 888  ASP C OD1 1 
ATOM   14035 O  OD2 . ASP B  1 888 ? 28.668  5.503   56.828  1.00 63.52  ? 888  ASP C OD2 1 
ATOM   14036 N  N   . LEU B  1 889 ? 28.842  0.388   57.939  1.00 59.25  ? 889  LEU C N   1 
ATOM   14037 C  CA  . LEU B  1 889 ? 28.719  -0.762  58.831  1.00 57.56  ? 889  LEU C CA  1 
ATOM   14038 C  C   . LEU B  1 889 ? 27.468  -0.919  59.724  1.00 56.74  ? 889  LEU C C   1 
ATOM   14039 O  O   . LEU B  1 889 ? 26.962  -2.020  59.788  1.00 66.46  ? 889  LEU C O   1 
ATOM   14040 C  CB  . LEU B  1 889 ? 29.948  -0.838  59.741  1.00 62.28  ? 889  LEU C CB  1 
ATOM   14041 C  CG  . LEU B  1 889 ? 30.016  -2.114  60.595  1.00 58.95  ? 889  LEU C CG  1 
ATOM   14042 C  CD1 . LEU B  1 889 ? 29.793  -3.346  59.728  1.00 52.22  ? 889  LEU C CD1 1 
ATOM   14043 C  CD2 . LEU B  1 889 ? 31.330  -2.210  61.344  1.00 55.78  ? 889  LEU C CD2 1 
ATOM   14044 N  N   . GLY B  1 890 ? 26.936  0.082   60.420  1.00 56.26  ? 890  GLY C N   1 
ATOM   14045 C  CA  . GLY B  1 890 ? 27.249  1.481   60.344  1.00 53.42  ? 890  GLY C CA  1 
ATOM   14046 C  C   . GLY B  1 890 ? 25.871  2.063   60.082  1.00 61.67  ? 890  GLY C C   1 
ATOM   14047 O  O   . GLY B  1 890 ? 25.192  2.566   60.989  1.00 52.18  ? 890  GLY C O   1 
ATOM   14048 N  N   . SER B  1 891 ? 25.437  1.929   58.833  1.00 54.36  ? 891  SER C N   1 
ATOM   14049 C  CA  . SER B  1 891 ? 24.179  2.489   58.390  1.00 51.22  ? 891  SER C CA  1 
ATOM   14050 C  C   . SER B  1 891 ? 22.977  1.909   59.089  1.00 54.85  ? 891  SER C C   1 
ATOM   14051 O  O   . SER B  1 891 ? 23.047  0.850   59.699  1.00 63.12  ? 891  SER C O   1 
ATOM   14052 C  CB  . SER B  1 891 ? 24.022  2.279   56.891  1.00 54.14  ? 891  SER C CB  1 
ATOM   14053 O  OG  . SER B  1 891 ? 24.238  0.922   56.567  1.00 57.53  ? 891  SER C OG  1 
ATOM   14054 N  N   . TYR B  1 892 ? 21.864  2.619   58.977  1.00 57.59  ? 892  TYR C N   1 
ATOM   14055 C  CA  . TYR B  1 892 ? 20.569  2.104   59.381  1.00 61.52  ? 892  TYR C CA  1 
ATOM   14056 C  C   . TYR B  1 892 ? 20.207  0.966   58.452  1.00 60.74  ? 892  TYR C C   1 
ATOM   14057 O  O   . TYR B  1 892 ? 19.448  0.067   58.819  1.00 58.62  ? 892  TYR C O   1 
ATOM   14058 C  CB  . TYR B  1 892 ? 19.516  3.200   59.313  1.00 64.45  ? 892  TYR C CB  1 
ATOM   14059 C  CG  . TYR B  1 892 ? 18.169  2.838   59.897  1.00 74.70  ? 892  TYR C CG  1 
ATOM   14060 C  CD1 . TYR B  1 892 ? 17.972  2.829   61.274  1.00 75.49  ? 892  TYR C CD1 1 
ATOM   14061 C  CD2 . TYR B  1 892 ? 17.082  2.533   59.072  1.00 77.40  ? 892  TYR C CD2 1 
ATOM   14062 C  CE1 . TYR B  1 892 ? 16.731  2.522   61.827  1.00 80.64  ? 892  TYR C CE1 1 
ATOM   14063 C  CE2 . TYR B  1 892 ? 15.831  2.218   59.616  1.00 82.98  ? 892  TYR C CE2 1 
ATOM   14064 C  CZ  . TYR B  1 892 ? 15.665  2.216   61.000  1.00 82.72  ? 892  TYR C CZ  1 
ATOM   14065 O  OH  . TYR B  1 892 ? 14.445  1.911   61.566  1.00 81.15  ? 892  TYR C OH  1 
ATOM   14066 N  N   . ASP B  1 893 ? 20.762  1.040   57.239  1.00 56.98  ? 893  ASP C N   1 
ATOM   14067 C  CA  . ASP B  1 893 ? 20.550  0.064   56.170  1.00 55.23  ? 893  ASP C CA  1 
ATOM   14068 C  C   . ASP B  1 893 ? 21.033  -1.324  56.563  1.00 53.96  ? 893  ASP C C   1 
ATOM   14069 O  O   . ASP B  1 893 ? 20.297  -2.299  56.463  1.00 49.42  ? 893  ASP C O   1 
ATOM   14070 C  CB  . ASP B  1 893 ? 21.283  0.488   54.894  1.00 52.41  ? 893  ASP C CB  1 
ATOM   14071 C  CG  . ASP B  1 893 ? 20.750  1.783   54.294  1.00 57.12  ? 893  ASP C CG  1 
ATOM   14072 O  OD1 . ASP B  1 893 ? 19.772  1.707   53.518  1.00 57.35  ? 893  ASP C OD1 1 
ATOM   14073 O  OD2 . ASP B  1 893 ? 21.331  2.865   54.569  1.00 55.40  ? 893  ASP C OD2 1 
ATOM   14074 N  N   . ILE B  1 894 ? 22.290  -1.401  56.982  1.00 50.67  ? 894  ILE C N   1 
ATOM   14075 C  CA  . ILE B  1 894 ? 22.862  -2.656  57.414  1.00 53.92  ? 894  ILE C CA  1 
ATOM   14076 C  C   . ILE B  1 894 ? 22.119  -3.177  58.631  1.00 57.78  ? 894  ILE C C   1 
ATOM   14077 O  O   . ILE B  1 894 ? 21.810  -4.357  58.720  1.00 59.05  ? 894  ILE C O   1 
ATOM   14078 C  CB  . ILE B  1 894 ? 24.343  -2.517  57.760  1.00 56.78  ? 894  ILE C CB  1 
ATOM   14079 C  CG1 . ILE B  1 894 ? 25.158  -2.227  56.501  1.00 58.13  ? 894  ILE C CG1 1 
ATOM   14080 C  CG2 . ILE B  1 894 ? 24.837  -3.797  58.432  1.00 57.89  ? 894  ILE C CG2 1 
ATOM   14081 C  CD1 . ILE B  1 894 ? 25.010  -3.288  55.410  1.00 55.59  ? 894  ILE C CD1 1 
ATOM   14082 N  N   . ARG B  1 895 ? 21.813  -2.284  59.560  1.00 57.98  ? 895  ARG C N   1 
ATOM   14083 C  CA  . ARG B  1 895 ? 21.161  -2.694  60.785  1.00 58.96  ? 895  ARG C CA  1 
ATOM   14084 C  C   . ARG B  1 895 ? 19.755  -3.220  60.505  1.00 57.96  ? 895  ARG C C   1 
ATOM   14085 O  O   . ARG B  1 895 ? 19.280  -4.118  61.201  1.00 57.72  ? 895  ARG C O   1 
ATOM   14086 C  CB  . ARG B  1 895 ? 21.133  -1.535  61.787  1.00 59.67  ? 895  ARG C CB  1 
ATOM   14087 C  CG  . ARG B  1 895 ? 22.384  -1.459  62.665  1.00 59.03  ? 895  ARG C CG  1 
ATOM   14088 C  CD  . ARG B  1 895 ? 22.600  -0.066  63.246  1.00 67.73  ? 895  ARG C CD  1 
ATOM   14089 N  NE  . ARG B  1 895 ? 21.364  0.506   63.789  1.00 73.25  ? 895  ARG C NE  1 
ATOM   14090 C  CZ  . ARG B  1 895 ? 21.197  1.791   64.105  1.00 62.73  ? 895  ARG C CZ  1 
ATOM   14091 N  NH1 . ARG B  1 895 ? 22.188  2.672   63.934  1.00 53.88  ? 895  ARG C NH1 1 
ATOM   14092 N  NH2 . ARG B  1 895 ? 20.025  2.195   64.585  1.00 64.05  ? 895  ARG C NH2 1 
ATOM   14093 N  N   . MET B  1 896 ? 19.096  -2.677  59.486  1.00 52.17  ? 896  MET C N   1 
ATOM   14094 C  CA  . MET B  1 896 ? 17.758  -3.144  59.141  1.00 56.95  ? 896  MET C CA  1 
ATOM   14095 C  C   . MET B  1 896 ? 17.877  -4.467  58.397  1.00 60.67  ? 896  MET C C   1 
ATOM   14096 O  O   . MET B  1 896 ? 17.000  -5.318  58.496  1.00 61.24  ? 896  MET C O   1 
ATOM   14097 C  CB  . MET B  1 896 ? 16.987  -2.112  58.299  1.00 57.11  ? 896  MET C CB  1 
ATOM   14098 C  CG  . MET B  1 896 ? 15.699  -2.655  57.650  1.00 55.72  ? 896  MET C CG  1 
ATOM   14099 S  SD  . MET B  1 896 ? 14.352  -1.473  57.287  1.00 79.31  ? 896  MET C SD  1 
ATOM   14100 C  CE  . MET B  1 896 ? 15.131  -0.279  56.198  1.00 58.97  ? 896  MET C CE  1 
ATOM   14101 N  N   . ILE B  1 897 ? 18.974  -4.641  57.664  1.00 55.52  ? 897  ILE C N   1 
ATOM   14102 C  CA  . ILE B  1 897 ? 19.204  -5.877  56.927  1.00 58.54  ? 897  ILE C CA  1 
ATOM   14103 C  C   . ILE B  1 897 ? 19.570  -7.023  57.877  1.00 60.52  ? 897  ILE C C   1 
ATOM   14104 O  O   . ILE B  1 897 ? 19.102  -8.154  57.732  1.00 61.57  ? 897  ILE C O   1 
ATOM   14105 C  CB  . ILE B  1 897 ? 20.315  -5.717  55.874  1.00 55.21  ? 897  ILE C CB  1 
ATOM   14106 C  CG1 . ILE B  1 897 ? 19.849  -4.829  54.726  1.00 53.22  ? 897  ILE C CG1 1 
ATOM   14107 C  CG2 . ILE B  1 897 ? 20.679  -7.056  55.282  1.00 54.76  ? 897  ILE C CG2 1 
ATOM   14108 C  CD1 . ILE B  1 897 ? 20.878  -4.688  53.650  1.00 52.12  ? 897  ILE C CD1 1 
ATOM   14109 N  N   . ILE B  1 898 ? 20.402  -6.719  58.857  1.00 56.73  ? 898  ILE C N   1 
ATOM   14110 C  CA  . ILE B  1 898 ? 20.800  -7.717  59.822  1.00 57.55  ? 898  ILE C CA  1 
ATOM   14111 C  C   . ILE B  1 898 ? 19.628  -8.158  60.687  1.00 61.09  ? 898  ILE C C   1 
ATOM   14112 O  O   . ILE B  1 898 ? 19.281  -9.331  60.701  1.00 67.90  ? 898  ILE C O   1 
ATOM   14113 C  CB  . ILE B  1 898 ? 21.920  -7.206  60.715  1.00 59.75  ? 898  ILE C CB  1 
ATOM   14114 C  CG1 . ILE B  1 898 ? 23.207  -7.080  59.898  1.00 56.20  ? 898  ILE C CG1 1 
ATOM   14115 C  CG2 . ILE B  1 898 ? 22.103  -8.137  61.921  1.00 52.15  ? 898  ILE C CG2 1 
ATOM   14116 C  CD1 . ILE B  1 898 ? 24.399  -6.706  60.727  1.00 63.89  ? 898  ILE C CD1 1 
ATOM   14117 N  N   . SER B  1 899 ? 19.010  -7.223  61.395  1.00 62.47  ? 899  SER C N   1 
ATOM   14118 C  CA  . SER B  1 899 ? 17.933  -7.564  62.321  1.00 58.80  ? 899  SER C CA  1 
ATOM   14119 C  C   . SER B  1 899 ? 16.663  -7.916  61.579  1.00 57.33  ? 899  SER C C   1 
ATOM   14120 O  O   . SER B  1 899 ? 15.787  -8.575  62.121  1.00 56.38  ? 899  SER C O   1 
ATOM   14121 C  CB  . SER B  1 899 ? 17.654  -6.408  63.285  1.00 61.92  ? 899  SER C CB  1 
ATOM   14122 O  OG  . SER B  1 899 ? 16.647  -5.551  62.774  1.00 60.90  ? 899  SER C OG  1 
ATOM   14123 N  N   . GLY B  1 900 ? 16.557  -7.469  60.335  1.00 58.68  ? 900  GLY C N   1 
ATOM   14124 C  CA  . GLY B  1 900 ? 15.340  -7.694  59.583  1.00 57.92  ? 900  GLY C CA  1 
ATOM   14125 C  C   . GLY B  1 900 ? 15.311  -9.098  59.036  1.00 62.64  ? 900  GLY C C   1 
ATOM   14126 O  O   . GLY B  1 900 ? 14.279  -9.562  58.555  1.00 69.20  ? 900  GLY C O   1 
ATOM   14127 N  N   . THR B  1 901 ? 16.445  -9.783  59.108  1.00 57.26  ? 901  THR C N   1 
ATOM   14128 C  CA  . THR B  1 901 ? 16.550  -11.093 58.494  1.00 63.59  ? 901  THR C CA  1 
ATOM   14129 C  C   . THR B  1 901 ? 16.992  -12.128 59.501  1.00 64.17  ? 901  THR C C   1 
ATOM   14130 O  O   . THR B  1 901 ? 17.321  -13.254 59.137  1.00 66.45  ? 901  THR C O   1 
ATOM   14131 C  CB  . THR B  1 901 ? 17.540  -11.107 57.289  1.00 65.97  ? 901  THR C CB  1 
ATOM   14132 O  OG1 . THR B  1 901 ? 18.800  -10.543 57.674  1.00 60.60  ? 901  THR C OG1 1 
ATOM   14133 C  CG2 . THR B  1 901 ? 16.980  -10.325 56.117  1.00 64.29  ? 901  THR C CG2 1 
ATOM   14134 N  N   . THR B  1 902 ? 17.003  -11.754 60.772  1.00 61.93  ? 902  THR C N   1 
ATOM   14135 C  CA  . THR B  1 902 ? 17.437  -12.693 61.795  1.00 66.86  ? 902  THR C CA  1 
ATOM   14136 C  C   . THR B  1 902 ? 16.644  -12.632 63.104  1.00 70.92  ? 902  THR C C   1 
ATOM   14137 O  O   . THR B  1 902 ? 16.647  -13.601 63.866  1.00 69.09  ? 902  THR C O   1 
ATOM   14138 C  CB  . THR B  1 902 ? 18.930  -12.494 62.153  1.00 66.41  ? 902  THR C CB  1 
ATOM   14139 O  OG1 . THR B  1 902 ? 19.150  -11.152 62.601  1.00 64.77  ? 902  THR C OG1 1 
ATOM   14140 C  CG2 . THR B  1 902 ? 19.825  -12.792 60.970  1.00 64.29  ? 902  THR C CG2 1 
ATOM   14141 N  N   . ALA B  1 903 ? 15.979  -11.511 63.378  1.00 64.87  ? 903  ALA C N   1 
ATOM   14142 C  CA  . ALA B  1 903 ? 15.368  -11.323 64.691  1.00 64.41  ? 903  ALA C CA  1 
ATOM   14143 C  C   . ALA B  1 903 ? 14.065  -12.094 64.836  1.00 72.35  ? 903  ALA C C   1 
ATOM   14144 O  O   . ALA B  1 903 ? 13.630  -12.379 65.956  1.00 67.21  ? 903  ALA C O   1 
ATOM   14145 C  CB  . ALA B  1 903 ? 15.132  -9.843  64.972  1.00 56.18  ? 903  ALA C CB  1 
ATOM   14146 N  N   . HIS B  1 904 ? 13.438  -12.421 63.710  1.00 69.35  ? 904  HIS C N   1 
ATOM   14147 C  CA  . HIS B  1 904 ? 12.174  -13.147 63.740  1.00 71.48  ? 904  HIS C CA  1 
ATOM   14148 C  C   . HIS B  1 904 ? 12.387  -14.599 64.168  1.00 75.96  ? 904  HIS C C   1 
ATOM   14149 O  O   . HIS B  1 904 ? 11.474  -15.239 64.698  1.00 78.00  ? 904  HIS C O   1 
ATOM   14150 C  CB  . HIS B  1 904 ? 11.477  -13.087 62.375  1.00 73.64  ? 904  HIS C CB  1 
ATOM   14151 C  CG  . HIS B  1 904 ? 12.394  -13.302 61.208  1.00 74.19  ? 904  HIS C CG  1 
ATOM   14152 N  ND1 . HIS B  1 904 ? 13.223  -12.315 60.720  1.00 72.18  ? 904  HIS C ND1 1 
ATOM   14153 C  CD2 . HIS B  1 904 ? 12.591  -14.383 60.415  1.00 82.63  ? 904  HIS C CD2 1 
ATOM   14154 C  CE1 . HIS B  1 904 ? 13.900  -12.783 59.686  1.00 77.08  ? 904  HIS C CE1 1 
ATOM   14155 N  NE2 . HIS B  1 904 ? 13.532  -14.035 59.476  1.00 79.41  ? 904  HIS C NE2 1 
ATOM   14156 N  N   . PHE B  1 905 ? 13.600  -15.102 63.949  1.00 72.71  ? 905  PHE C N   1 
ATOM   14157 C  CA  . PHE B  1 905 ? 13.948  -16.485 64.257  1.00 68.27  ? 905  PHE C CA  1 
ATOM   14158 C  C   . PHE B  1 905 ? 13.666  -16.810 65.711  1.00 70.59  ? 905  PHE C C   1 
ATOM   14159 O  O   . PHE B  1 905 ? 13.679  -15.920 66.561  1.00 73.30  ? 905  PHE C O   1 
ATOM   14160 C  CB  . PHE B  1 905 ? 15.417  -16.752 63.926  1.00 68.67  ? 905  PHE C CB  1 
ATOM   14161 C  CG  . PHE B  1 905 ? 15.714  -16.750 62.455  1.00 62.35  ? 905  PHE C CG  1 
ATOM   14162 C  CD1 . PHE B  1 905 ? 14.715  -17.018 61.531  1.00 67.54  ? 905  PHE C CD1 1 
ATOM   14163 C  CD2 . PHE B  1 905 ? 16.993  -16.482 61.992  1.00 67.04  ? 905  PHE C CD2 1 
ATOM   14164 C  CE1 . PHE B  1 905 ? 14.986  -17.015 60.168  1.00 70.06  ? 905  PHE C CE1 1 
ATOM   14165 C  CE2 . PHE B  1 905 ? 17.271  -16.476 60.632  1.00 64.96  ? 905  PHE C CE2 1 
ATOM   14166 C  CZ  . PHE B  1 905 ? 16.265  -16.742 59.720  1.00 64.60  ? 905  PHE C CZ  1 
ATOM   14167 N  N   . SER B  1 906 ? 13.398  -18.086 65.991  1.00 74.67  ? 906  SER C N   1 
ATOM   14168 C  CA  . SER B  1 906 ? 12.957  -18.507 67.325  1.00 73.87  ? 906  SER C CA  1 
ATOM   14169 C  C   . SER B  1 906 ? 13.393  -19.928 67.728  1.00 74.20  ? 906  SER C C   1 
ATOM   14170 O  O   . SER B  1 906 ? 13.022  -20.421 68.796  1.00 75.18  ? 906  SER C O   1 
ATOM   14171 C  CB  . SER B  1 906 ? 11.430  -18.398 67.419  1.00 71.96  ? 906  SER C CB  1 
ATOM   14172 O  OG  . SER B  1 906 ? 10.798  -18.994 66.300  1.00 73.03  ? 906  SER C OG  1 
ATOM   14173 N  N   . SER B  1 907 ? 14.169  -20.591 66.876  1.00 76.99  ? 907  SER C N   1 
ATOM   14174 C  CA  . SER B  1 907 ? 14.645  -21.938 67.179  1.00 72.60  ? 907  SER C CA  1 
ATOM   14175 C  C   . SER B  1 907 ? 16.052  -21.886 67.747  1.00 73.95  ? 907  SER C C   1 
ATOM   14176 O  O   . SER B  1 907 ? 16.695  -20.841 67.724  1.00 72.13  ? 907  SER C O   1 
ATOM   14177 C  CB  . SER B  1 907 ? 14.608  -22.820 65.934  1.00 68.26  ? 907  SER C CB  1 
ATOM   14178 O  OG  . SER B  1 907 ? 15.639  -22.468 65.036  1.00 69.68  ? 907  SER C OG  1 
ATOM   14179 N  N   . LYS B  1 908 ? 16.530  -23.017 68.256  1.00 78.22  ? 908  LYS C N   1 
ATOM   14180 C  CA  . LYS B  1 908 ? 17.849  -23.066 68.871  1.00 73.69  ? 908  LYS C CA  1 
ATOM   14181 C  C   . LYS B  1 908 ? 18.912  -23.273 67.804  1.00 77.27  ? 908  LYS C C   1 
ATOM   14182 O  O   . LYS B  1 908 ? 20.093  -23.012 68.037  1.00 82.26  ? 908  LYS C O   1 
ATOM   14183 C  CB  . LYS B  1 908 ? 17.926  -24.180 69.925  1.00 81.41  ? 908  LYS C CB  1 
ATOM   14184 C  CG  . LYS B  1 908 ? 16.693  -24.312 70.833  1.00 79.87  ? 908  LYS C CG  1 
ATOM   14185 C  CD  . LYS B  1 908 ? 16.940  -25.318 71.967  1.00 86.72  ? 908  LYS C CD  1 
ATOM   14186 C  CE  . LYS B  1 908 ? 15.635  -25.789 72.643  1.00 90.84  ? 908  LYS C CE  1 
ATOM   14187 N  NZ  . LYS B  1 908 ? 15.171  -24.961 73.814  1.00 72.68  ? 908  LYS C NZ  1 
ATOM   14188 N  N   . ASP B  1 909 ? 18.496  -23.740 66.630  1.00 73.59  ? 909  ASP C N   1 
ATOM   14189 C  CA  . ASP B  1 909 ? 19.450  -24.026 65.563  1.00 78.32  ? 909  ASP C CA  1 
ATOM   14190 C  C   . ASP B  1 909 ? 19.624  -22.824 64.636  1.00 82.48  ? 909  ASP C C   1 
ATOM   14191 O  O   . ASP B  1 909 ? 20.690  -22.633 64.042  1.00 81.91  ? 909  ASP C O   1 
ATOM   14192 C  CB  . ASP B  1 909 ? 19.023  -25.263 64.760  1.00 77.06  ? 909  ASP C CB  1 
ATOM   14193 C  CG  . ASP B  1 909 ? 17.743  -25.043 63.978  1.00 84.46  ? 909  ASP C CG  1 
ATOM   14194 O  OD1 . ASP B  1 909 ? 16.652  -25.206 64.575  1.00 88.85  ? 909  ASP C OD1 1 
ATOM   14195 O  OD2 . ASP B  1 909 ? 17.830  -24.719 62.767  1.00 81.27  ? 909  ASP C OD2 1 
ATOM   14196 N  N   . LYS B  1 910 ? 18.580  -22.012 64.504  1.00 81.85  ? 910  LYS C N   1 
ATOM   14197 C  CA  . LYS B  1 910 ? 18.725  -20.757 63.786  1.00 76.39  ? 910  LYS C CA  1 
ATOM   14198 C  C   . LYS B  1 910 ? 19.585  -19.812 64.632  1.00 75.80  ? 910  LYS C C   1 
ATOM   14199 O  O   . LYS B  1 910 ? 20.467  -19.135 64.108  1.00 78.02  ? 910  LYS C O   1 
ATOM   14200 C  CB  . LYS B  1 910 ? 17.363  -20.147 63.457  1.00 69.49  ? 910  LYS C CB  1 
ATOM   14201 C  CG  . LYS B  1 910 ? 16.768  -20.680 62.166  1.00 72.42  ? 910  LYS C CG  1 
ATOM   14202 C  CD  . LYS B  1 910 ? 17.792  -20.634 61.042  1.00 75.68  ? 910  LYS C CD  1 
ATOM   14203 C  CE  . LYS B  1 910 ? 17.198  -21.073 59.700  1.00 81.52  ? 910  LYS C CE  1 
ATOM   14204 N  NZ  . LYS B  1 910 ? 16.756  -22.499 59.712  1.00 89.08  ? 910  LYS C NZ  1 
ATOM   14205 N  N   . LEU B  1 911 ? 19.366  -19.808 65.944  1.00 71.36  ? 911  LEU C N   1 
ATOM   14206 C  CA  . LEU B  1 911 ? 20.181  -18.999 66.847  1.00 72.48  ? 911  LEU C CA  1 
ATOM   14207 C  C   . LEU B  1 911 ? 21.662  -19.320 66.685  1.00 75.33  ? 911  LEU C C   1 
ATOM   14208 O  O   . LEU B  1 911 ? 22.531  -18.497 66.972  1.00 77.69  ? 911  LEU C O   1 
ATOM   14209 C  CB  . LEU B  1 911 ? 19.762  -19.210 68.304  1.00 72.56  ? 911  LEU C CB  1 
ATOM   14210 C  CG  . LEU B  1 911 ? 20.515  -18.318 69.302  1.00 72.69  ? 911  LEU C CG  1 
ATOM   14211 C  CD1 . LEU B  1 911 ? 20.309  -16.839 68.982  1.00 66.25  ? 911  LEU C CD1 1 
ATOM   14212 C  CD2 . LEU B  1 911 ? 20.126  -18.620 70.730  1.00 59.00  ? 911  LEU C CD2 1 
ATOM   14213 N  N   . GLN B  1 912 ? 21.942  -20.523 66.209  1.00 76.88  ? 912  GLN C N   1 
ATOM   14214 C  CA  . GLN B  1 912 ? 23.308  -20.946 65.968  1.00 80.69  ? 912  GLN C CA  1 
ATOM   14215 C  C   . GLN B  1 912 ? 23.847  -20.325 64.684  1.00 79.22  ? 912  GLN C C   1 
ATOM   14216 O  O   . GLN B  1 912 ? 24.926  -19.726 64.690  1.00 80.60  ? 912  GLN C O   1 
ATOM   14217 C  CB  . GLN B  1 912 ? 23.386  -22.475 65.904  1.00 85.19  ? 912  GLN C CB  1 
ATOM   14218 C  CG  . GLN B  1 912 ? 24.726  -23.028 65.437  1.00 85.30  ? 912  GLN C CG  1 
ATOM   14219 C  CD  . GLN B  1 912 ? 25.856  -22.785 66.428  1.00 84.68  ? 912  GLN C CD  1 
ATOM   14220 O  OE1 . GLN B  1 912 ? 25.659  -22.190 67.494  1.00 73.21  ? 912  GLN C OE1 1 
ATOM   14221 N  NE2 . GLN B  1 912 ? 27.055  -23.253 66.075  1.00 83.16  ? 912  GLN C NE2 1 
ATOM   14222 N  N   . GLU B  1 913 ? 23.095  -20.462 63.591  1.00 73.04  ? 913  GLU C N   1 
ATOM   14223 C  CA  . GLU B  1 913 ? 23.493  -19.893 62.303  1.00 76.91  ? 913  GLU C CA  1 
ATOM   14224 C  C   . GLU B  1 913 ? 23.723  -18.386 62.409  1.00 79.90  ? 913  GLU C C   1 
ATOM   14225 O  O   . GLU B  1 913 ? 24.612  -17.836 61.757  1.00 78.41  ? 913  GLU C O   1 
ATOM   14226 C  CB  . GLU B  1 913 ? 22.436  -20.170 61.237  1.00 77.97  ? 913  GLU C CB  1 
ATOM   14227 C  CG  . GLU B  1 913 ? 22.163  -21.628 60.963  1.00 74.58  ? 913  GLU C CG  1 
ATOM   14228 C  CD  . GLU B  1 913 ? 20.908  -21.815 60.146  1.00 75.89  ? 913  GLU C CD  1 
ATOM   14229 O  OE1 . GLU B  1 913 ? 20.611  -20.923 59.325  1.00 67.53  ? 913  GLU C OE1 1 
ATOM   14230 O  OE2 . GLU B  1 913 ? 20.216  -22.844 60.328  1.00 79.04  ? 913  GLU C OE2 1 
ATOM   14231 N  N   . VAL B  1 914 ? 22.906  -17.734 63.234  1.00 78.89  ? 914  VAL C N   1 
ATOM   14232 C  CA  . VAL B  1 914 ? 22.992  -16.301 63.456  1.00 72.81  ? 914  VAL C CA  1 
ATOM   14233 C  C   . VAL B  1 914 ? 24.235  -15.984 64.265  1.00 77.45  ? 914  VAL C C   1 
ATOM   14234 O  O   . VAL B  1 914 ? 24.959  -15.036 63.964  1.00 76.12  ? 914  VAL C O   1 
ATOM   14235 C  CB  . VAL B  1 914 ? 21.736  -15.767 64.173  1.00 71.28  ? 914  VAL C CB  1 
ATOM   14236 C  CG1 . VAL B  1 914 ? 22.041  -14.483 64.943  1.00 73.85  ? 914  VAL C CG1 1 
ATOM   14237 C  CG2 . VAL B  1 914 ? 20.619  -15.550 63.176  1.00 68.96  ? 914  VAL C CG2 1 
ATOM   14238 N  N   . LYS B  1 915 ? 24.485  -16.785 65.293  1.00 79.97  ? 915  LYS C N   1 
ATOM   14239 C  CA  . LYS B  1 915 ? 25.718  -16.659 66.059  1.00 80.12  ? 915  LYS C CA  1 
ATOM   14240 C  C   . LYS B  1 915 ? 26.928  -16.927 65.178  1.00 76.63  ? 915  LYS C C   1 
ATOM   14241 O  O   . LYS B  1 915 ? 27.926  -16.227 65.256  1.00 72.98  ? 915  LYS C O   1 
ATOM   14242 C  CB  . LYS B  1 915 ? 25.717  -17.618 67.244  1.00 79.05  ? 915  LYS C CB  1 
ATOM   14243 C  CG  . LYS B  1 915 ? 27.091  -17.851 67.852  1.00 87.41  ? 915  LYS C CG  1 
ATOM   14244 C  CD  . LYS B  1 915 ? 27.578  -16.644 68.626  1.00 84.80  ? 915  LYS C CD  1 
ATOM   14245 C  CE  . LYS B  1 915 ? 28.798  -16.987 69.472  1.00 91.72  ? 915  LYS C CE  1 
ATOM   14246 N  NZ  . LYS B  1 915 ? 29.286  -15.800 70.244  1.00 92.52  ? 915  LYS C NZ  1 
ATOM   14247 N  N   . LEU B  1 916 ? 26.825  -17.952 64.341  1.00 78.81  ? 916  LEU C N   1 
ATOM   14248 C  CA  . LEU B  1 916 ? 27.917  -18.321 63.449  1.00 83.37  ? 916  LEU C CA  1 
ATOM   14249 C  C   . LEU B  1 916 ? 28.278  -17.147 62.549  1.00 79.91  ? 916  LEU C C   1 
ATOM   14250 O  O   . LEU B  1 916 ? 29.438  -16.734 62.479  1.00 76.50  ? 916  LEU C O   1 
ATOM   14251 C  CB  . LEU B  1 916 ? 27.533  -19.547 62.610  1.00 85.83  ? 916  LEU C CB  1 
ATOM   14252 C  CG  . LEU B  1 916 ? 28.639  -20.327 61.886  1.00 88.71  ? 916  LEU C CG  1 
ATOM   14253 C  CD1 . LEU B  1 916 ? 29.819  -20.626 62.807  1.00 77.50  ? 916  LEU C CD1 1 
ATOM   14254 C  CD2 . LEU B  1 916 ? 28.066  -21.621 61.311  1.00 89.18  ? 916  LEU C CD2 1 
ATOM   14255 N  N   . PHE B  1 917 ? 27.257  -16.600 61.895  1.00 79.25  ? 917  PHE C N   1 
ATOM   14256 C  CA  . PHE B  1 917 ? 27.424  -15.520 60.935  1.00 74.07  ? 917  PHE C CA  1 
ATOM   14257 C  C   . PHE B  1 917 ? 28.006  -14.257 61.557  1.00 70.25  ? 917  PHE C C   1 
ATOM   14258 O  O   . PHE B  1 917 ? 28.970  -13.708 61.031  1.00 68.66  ? 917  PHE C O   1 
ATOM   14259 C  CB  . PHE B  1 917 ? 26.091  -15.202 60.273  1.00 74.62  ? 917  PHE C CB  1 
ATOM   14260 C  CG  . PHE B  1 917 ? 26.162  -14.069 59.306  1.00 77.73  ? 917  PHE C CG  1 
ATOM   14261 C  CD1 . PHE B  1 917 ? 27.044  -14.111 58.243  1.00 76.05  ? 917  PHE C CD1 1 
ATOM   14262 C  CD2 . PHE B  1 917 ? 25.353  -12.958 59.460  1.00 69.57  ? 917  PHE C CD2 1 
ATOM   14263 C  CE1 . PHE B  1 917 ? 27.112  -13.067 57.349  1.00 72.19  ? 917  PHE C CE1 1 
ATOM   14264 C  CE2 . PHE B  1 917 ? 25.417  -11.921 58.570  1.00 65.37  ? 917  PHE C CE2 1 
ATOM   14265 C  CZ  . PHE B  1 917 ? 26.300  -11.973 57.512  1.00 71.51  ? 917  PHE C CZ  1 
ATOM   14266 N  N   . PHE B  1 918 ? 27.419  -13.804 62.665  1.00 68.62  ? 918  PHE C N   1 
ATOM   14267 C  CA  . PHE B  1 918 ? 27.920  -12.643 63.404  1.00 67.25  ? 918  PHE C CA  1 
ATOM   14268 C  C   . PHE B  1 918 ? 29.381  -12.836 63.784  1.00 75.88  ? 918  PHE C C   1 
ATOM   14269 O  O   . PHE B  1 918 ? 30.157  -11.887 63.776  1.00 79.89  ? 918  PHE C O   1 
ATOM   14270 C  CB  . PHE B  1 918 ? 27.107  -12.378 64.680  1.00 64.28  ? 918  PHE C CB  1 
ATOM   14271 C  CG  . PHE B  1 918 ? 25.720  -11.831 64.439  1.00 60.65  ? 918  PHE C CG  1 
ATOM   14272 C  CD1 . PHE B  1 918 ? 25.312  -11.438 63.177  1.00 55.91  ? 918  PHE C CD1 1 
ATOM   14273 C  CD2 . PHE B  1 918 ? 24.825  -11.705 65.497  1.00 58.54  ? 918  PHE C CD2 1 
ATOM   14274 C  CE1 . PHE B  1 918 ? 24.035  -10.942 62.972  1.00 55.62  ? 918  PHE C CE1 1 
ATOM   14275 C  CE2 . PHE B  1 918 ? 23.549  -11.206 65.297  1.00 59.13  ? 918  PHE C CE2 1 
ATOM   14276 C  CZ  . PHE B  1 918 ? 23.156  -10.820 64.033  1.00 58.95  ? 918  PHE C CZ  1 
ATOM   14277 N  N   . GLU B  1 919 ? 29.751  -14.068 64.120  1.00 79.65  ? 919  GLU C N   1 
ATOM   14278 C  CA  . GLU B  1 919 ? 31.133  -14.373 64.476  1.00 80.74  ? 919  GLU C CA  1 
ATOM   14279 C  C   . GLU B  1 919 ? 32.060  -14.325 63.262  1.00 81.95  ? 919  GLU C C   1 
ATOM   14280 O  O   . GLU B  1 919 ? 33.225  -13.948 63.388  1.00 81.43  ? 919  GLU C O   1 
ATOM   14281 C  CB  . GLU B  1 919 ? 31.236  -15.744 65.156  1.00 83.82  ? 919  GLU C CB  1 
ATOM   14282 C  CG  . GLU B  1 919 ? 30.644  -15.810 66.572  1.00 87.54  ? 919  GLU C CG  1 
ATOM   14283 C  CD  . GLU B  1 919 ? 30.626  -14.463 67.303  1.00 90.37  ? 919  GLU C CD  1 
ATOM   14284 O  OE1 . GLU B  1 919 ? 31.682  -13.797 67.400  1.00 92.71  ? 919  GLU C OE1 1 
ATOM   14285 O  OE2 . GLU B  1 919 ? 29.543  -14.073 67.796  1.00 88.96  ? 919  GLU C OE2 1 
ATOM   14286 N  N   . SER B  1 920 ? 31.550  -14.709 62.093  1.00 80.65  ? 920  SER C N   1 
ATOM   14287 C  CA  . SER B  1 920 ? 32.300  -14.549 60.848  1.00 74.82  ? 920  SER C CA  1 
ATOM   14288 C  C   . SER B  1 920 ? 32.568  -13.071 60.592  1.00 82.33  ? 920  SER C C   1 
ATOM   14289 O  O   . SER B  1 920 ? 33.664  -12.692 60.174  1.00 85.06  ? 920  SER C O   1 
ATOM   14290 C  CB  . SER B  1 920 ? 31.544  -15.161 59.671  1.00 76.79  ? 920  SER C CB  1 
ATOM   14291 O  OG  . SER B  1 920 ? 32.111  -14.754 58.438  1.00 87.38  ? 920  SER C OG  1 
ATOM   14292 N  N   . LEU B  1 921 ? 31.560  -12.242 60.857  1.00 80.33  ? 921  LEU C N   1 
ATOM   14293 C  CA  . LEU B  1 921 ? 31.689  -10.800 60.699  1.00 77.06  ? 921  LEU C CA  1 
ATOM   14294 C  C   . LEU B  1 921 ? 32.675  -10.219 61.701  1.00 79.99  ? 921  LEU C C   1 
ATOM   14295 O  O   . LEU B  1 921 ? 33.320  -9.223  61.409  1.00 80.44  ? 921  LEU C O   1 
ATOM   14296 C  CB  . LEU B  1 921 ? 30.334  -10.103 60.852  1.00 70.10  ? 921  LEU C CB  1 
ATOM   14297 C  CG  . LEU B  1 921 ? 29.191  -10.534 59.940  1.00 64.41  ? 921  LEU C CG  1 
ATOM   14298 C  CD1 . LEU B  1 921 ? 27.972  -9.682  60.197  1.00 62.49  ? 921  LEU C CD1 1 
ATOM   14299 C  CD2 . LEU B  1 921 ? 29.602  -10.473 58.487  1.00 63.02  ? 921  LEU C CD2 1 
ATOM   14300 N  N   . GLU B  1 922 ? 32.817  -10.832 62.875  1.00 84.92  ? 922  GLU C N   1 
ATOM   14301 C  CA  . GLU B  1 922 ? 33.739  -10.272 63.871  1.00 84.41  ? 922  GLU C CA  1 
ATOM   14302 C  C   . GLU B  1 922 ? 35.194  -10.394 63.403  1.00 85.36  ? 922  GLU C C   1 
ATOM   14303 O  O   . GLU B  1 922 ? 36.108  -9.909  64.050  1.00 86.50  ? 922  GLU C O   1 
ATOM   14304 C  CB  . GLU B  1 922 ? 33.541  -10.913 65.255  1.00 81.36  ? 922  GLU C CB  1 
ATOM   14305 C  CG  . GLU B  1 922 ? 32.103  -10.821 65.830  1.00 86.85  ? 922  GLU C CG  1 
ATOM   14306 C  CD  . GLU B  1 922 ? 31.871  -9.705  66.871  1.00 94.34  ? 922  GLU C CD  1 
ATOM   14307 O  OE1 . GLU B  1 922 ? 32.720  -8.794  67.026  1.00 89.89  ? 922  GLU C OE1 1 
ATOM   14308 O  OE2 . GLU B  1 922 ? 30.809  -9.744  67.538  1.00 90.97  ? 922  GLU C OE2 1 
ATOM   14309 N  N   . ALA B  1 923 ? 35.389  -11.036 62.258  1.00 84.72  ? 923  ALA C N   1 
ATOM   14310 C  CA  . ALA B  1 923 ? 36.650  -10.989 61.527  1.00 83.54  ? 923  ALA C CA  1 
ATOM   14311 C  C   . ALA B  1 923 ? 36.581  -9.837  60.523  1.00 91.69  ? 923  ALA C C   1 
ATOM   14312 O  O   . ALA B  1 923 ? 36.036  -10.011 59.423  1.00 88.68  ? 923  ALA C O   1 
ATOM   14313 C  CB  . ALA B  1 923 ? 36.905  -12.313 60.827  1.00 84.36  ? 923  ALA C CB  1 
ATOM   14314 N  N   . GLN B  1 924 ? 37.136  -8.688  60.935  1.00 95.83  ? 924  GLN C N   1 
ATOM   14315 C  CA  . GLN B  1 924 ? 37.045  -7.384  60.268  1.00 93.15  ? 924  GLN C CA  1 
ATOM   14316 C  C   . GLN B  1 924 ? 35.658  -6.771  60.466  1.00 96.53  ? 924  GLN C C   1 
ATOM   14317 O  O   . GLN B  1 924 ? 35.477  -5.850  61.286  1.00 91.38  ? 924  GLN C O   1 
ATOM   14318 C  CB  . GLN B  1 924 ? 37.373  -7.466  58.758  1.00 96.01  ? 924  GLN C CB  1 
ATOM   14319 C  CG  . GLN B  1 924 ? 37.304  -6.094  58.040  1.00 103.94 ? 924  GLN C CG  1 
ATOM   14320 C  CD  . GLN B  1 924 ? 37.221  -6.179  56.521  1.00 111.32 ? 924  GLN C CD  1 
ATOM   14321 O  OE1 . GLN B  1 924 ? 37.069  -7.264  55.949  1.00 114.35 ? 924  GLN C OE1 1 
ATOM   14322 N  NE2 . GLN B  1 924 ? 37.316  -5.022  55.860  1.00 102.99 ? 924  GLN C NE2 1 
ATOM   14323 N  N   . GLY B  1 925 ? 34.695  -7.288  59.698  1.00 97.99  ? 925  GLY C N   1 
ATOM   14324 C  CA  . GLY B  1 925 ? 33.350  -6.731  59.579  1.00 88.70  ? 925  GLY C CA  1 
ATOM   14325 C  C   . GLY B  1 925 ? 32.703  -6.185  60.832  1.00 79.64  ? 925  GLY C C   1 
ATOM   14326 O  O   . GLY B  1 925 ? 31.943  -5.249  60.740  1.00 88.96  ? 925  GLY C O   1 
ATOM   14327 N  N   . SER B  1 926 ? 33.007  -6.756  61.991  1.00 86.91  ? 926  SER C N   1 
ATOM   14328 C  CA  . SER B  1 926 ? 32.448  -6.277  63.252  1.00 85.96  ? 926  SER C CA  1 
ATOM   14329 C  C   . SER B  1 926 ? 32.856  -4.820  63.470  1.00 86.43  ? 926  SER C C   1 
ATOM   14330 O  O   . SER B  1 926 ? 33.786  -4.350  62.817  1.00 92.62  ? 926  SER C O   1 
ATOM   14331 C  CB  . SER B  1 926 ? 32.921  -7.161  64.402  1.00 90.77  ? 926  SER C CB  1 
ATOM   14332 O  OG  . SER B  1 926 ? 34.289  -6.937  64.693  1.00 100.50 ? 926  SER C OG  1 
ATOM   14333 N  N   . HIS B  1 927 ? 32.211  -4.098  64.387  1.00 85.67  ? 927  HIS C N   1 
ATOM   14334 C  CA  . HIS B  1 927 ? 31.308  -4.633  65.390  1.00 74.30  ? 927  HIS C CA  1 
ATOM   14335 C  C   . HIS B  1 927 ? 30.081  -3.775  65.564  1.00 74.85  ? 927  HIS C C   1 
ATOM   14336 O  O   . HIS B  1 927 ? 30.172  -2.554  65.720  1.00 79.07  ? 927  HIS C O   1 
ATOM   14337 C  CB  . HIS B  1 927 ? 32.056  -4.761  66.714  1.00 79.91  ? 927  HIS C CB  1 
ATOM   14338 C  CG  . HIS B  1 927 ? 31.167  -4.897  67.908  1.00 83.07  ? 927  HIS C CG  1 
ATOM   14339 N  ND1 . HIS B  1 927 ? 30.745  -6.119  68.387  1.00 81.44  ? 927  HIS C ND1 1 
ATOM   14340 C  CD2 . HIS B  1 927 ? 30.633  -3.963  68.733  1.00 78.48  ? 927  HIS C CD2 1 
ATOM   14341 C  CE1 . HIS B  1 927 ? 29.981  -5.932  69.449  1.00 78.68  ? 927  HIS C CE1 1 
ATOM   14342 N  NE2 . HIS B  1 927 ? 29.898  -4.633  69.680  1.00 81.36  ? 927  HIS C NE2 1 
ATOM   14343 N  N   . LEU B  1 928 ? 28.928  -4.423  65.546  1.00 71.57  ? 928  LEU C N   1 
ATOM   14344 C  CA  . LEU B  1 928 ? 27.679  -3.746  65.845  1.00 67.97  ? 928  LEU C CA  1 
ATOM   14345 C  C   . LEU B  1 928 ? 27.087  -4.281  67.136  1.00 64.98  ? 928  LEU C C   1 
ATOM   14346 O  O   . LEU B  1 928 ? 27.028  -5.492  67.350  1.00 65.64  ? 928  LEU C O   1 
ATOM   14347 C  CB  . LEU B  1 928 ? 26.688  -3.923  64.696  1.00 62.02  ? 928  LEU C CB  1 
ATOM   14348 C  CG  . LEU B  1 928 ? 27.252  -3.467  63.349  1.00 66.72  ? 928  LEU C CG  1 
ATOM   14349 C  CD1 . LEU B  1 928 ? 26.339  -3.896  62.200  1.00 45.96  ? 928  LEU C CD1 1 
ATOM   14350 C  CD2 . LEU B  1 928 ? 27.486  -1.954  63.358  1.00 55.48  ? 928  LEU C CD2 1 
ATOM   14351 N  N   . ASP B  1 929 ? 26.637  -3.377  67.994  1.00 60.97  ? 929  ASP C N   1 
ATOM   14352 C  CA  . ASP B  1 929 ? 25.842  -3.767  69.143  1.00 54.47  ? 929  ASP C CA  1 
ATOM   14353 C  C   . ASP B  1 929 ? 24.615  -4.583  68.735  1.00 58.67  ? 929  ASP C C   1 
ATOM   14354 O  O   . ASP B  1 929 ? 24.066  -5.330  69.540  1.00 63.95  ? 929  ASP C O   1 
ATOM   14355 C  CB  . ASP B  1 929 ? 25.401  -2.535  69.921  1.00 57.04  ? 929  ASP C CB  1 
ATOM   14356 C  CG  . ASP B  1 929 ? 26.566  -1.709  70.407  1.00 59.69  ? 929  ASP C CG  1 
ATOM   14357 O  OD1 . ASP B  1 929 ? 27.710  -2.219  70.391  1.00 57.94  ? 929  ASP C OD1 1 
ATOM   14358 O  OD2 . ASP B  1 929 ? 26.329  -0.550  70.812  1.00 63.57  ? 929  ASP C OD2 1 
ATOM   14359 N  N   . ILE B  1 930 ? 24.185  -4.442  67.484  1.00 59.37  ? 930  ILE C N   1 
ATOM   14360 C  CA  . ILE B  1 930 ? 23.005  -5.152  67.007  1.00 60.34  ? 930  ILE C CA  1 
ATOM   14361 C  C   . ILE B  1 930 ? 23.280  -6.662  66.918  1.00 62.03  ? 930  ILE C C   1 
ATOM   14362 O  O   . ILE B  1 930 ? 22.356  -7.466  66.773  1.00 61.17  ? 930  ILE C O   1 
ATOM   14363 C  CB  . ILE B  1 930 ? 22.534  -4.613  65.627  1.00 53.90  ? 930  ILE C CB  1 
ATOM   14364 C  CG1 . ILE B  1 930 ? 21.010  -4.668  65.510  1.00 50.37  ? 930  ILE C CG1 1 
ATOM   14365 C  CG2 . ILE B  1 930 ? 23.170  -5.392  64.495  1.00 52.63  ? 930  ILE C CG2 1 
ATOM   14366 C  CD1 . ILE B  1 930 ? 20.290  -4.072  66.689  1.00 53.37  ? 930  ILE C CD1 1 
ATOM   14367 N  N   . PHE B  1 931 ? 24.547  -7.056  67.000  1.00 55.27  ? 931  PHE C N   1 
ATOM   14368 C  CA  . PHE B  1 931 ? 24.850  -8.478  67.061  1.00 60.26  ? 931  PHE C CA  1 
ATOM   14369 C  C   . PHE B  1 931 ? 24.357  -9.023  68.397  1.00 60.95  ? 931  PHE C C   1 
ATOM   14370 O  O   . PHE B  1 931 ? 23.491  -9.898  68.459  1.00 56.37  ? 931  PHE C O   1 
ATOM   14371 C  CB  . PHE B  1 931 ? 26.349  -8.750  66.907  1.00 58.81  ? 931  PHE C CB  1 
ATOM   14372 C  CG  . PHE B  1 931 ? 26.903  -8.358  65.582  1.00 61.21  ? 931  PHE C CG  1 
ATOM   14373 C  CD1 . PHE B  1 931 ? 26.076  -8.232  64.480  1.00 64.56  ? 931  PHE C CD1 1 
ATOM   14374 C  CD2 . PHE B  1 931 ? 28.253  -8.108  65.434  1.00 67.05  ? 931  PHE C CD2 1 
ATOM   14375 C  CE1 . PHE B  1 931 ? 26.587  -7.865  63.257  1.00 59.47  ? 931  PHE C CE1 1 
ATOM   14376 C  CE2 . PHE B  1 931 ? 28.774  -7.741  64.212  1.00 66.71  ? 931  PHE C CE2 1 
ATOM   14377 C  CZ  . PHE B  1 931 ? 27.939  -7.618  63.123  1.00 63.06  ? 931  PHE C CZ  1 
ATOM   14378 N  N   . GLN B  1 932 ? 24.915  -8.472  69.468  1.00 62.82  ? 932  GLN C N   1 
ATOM   14379 C  CA  . GLN B  1 932 ? 24.586  -8.904  70.810  1.00 63.29  ? 932  GLN C CA  1 
ATOM   14380 C  C   . GLN B  1 932 ? 23.099  -8.719  71.076  1.00 62.48  ? 932  GLN C C   1 
ATOM   14381 O  O   . GLN B  1 932 ? 22.512  -9.452  71.856  1.00 66.47  ? 932  GLN C O   1 
ATOM   14382 C  CB  . GLN B  1 932 ? 25.428  -8.142  71.831  1.00 61.58  ? 932  GLN C CB  1 
ATOM   14383 C  CG  . GLN B  1 932 ? 25.625  -8.880  73.136  1.00 67.61  ? 932  GLN C CG  1 
ATOM   14384 C  CD  . GLN B  1 932 ? 26.093  -10.321 72.938  1.00 81.79  ? 932  GLN C CD  1 
ATOM   14385 O  OE1 . GLN B  1 932 ? 26.999  -10.595 72.144  1.00 81.70  ? 932  GLN C OE1 1 
ATOM   14386 N  NE2 . GLN B  1 932 ? 25.465  -11.250 73.658  1.00 74.51  ? 932  GLN C NE2 1 
ATOM   14387 N  N   . THR B  1 933 ? 22.485  -7.761  70.398  1.00 58.00  ? 933  THR C N   1 
ATOM   14388 C  CA  . THR B  1 933 ? 21.053  -7.539  70.536  1.00 61.83  ? 933  THR C CA  1 
ATOM   14389 C  C   . THR B  1 933 ? 20.210  -8.621  69.847  1.00 61.46  ? 933  THR C C   1 
ATOM   14390 O  O   . THR B  1 933 ? 19.253  -9.137  70.426  1.00 58.47  ? 933  THR C O   1 
ATOM   14391 C  CB  . THR B  1 933 ? 20.667  -6.169  69.967  1.00 54.68  ? 933  THR C CB  1 
ATOM   14392 O  OG1 . THR B  1 933 ? 21.384  -5.152  70.669  1.00 58.25  ? 933  THR C OG1 1 
ATOM   14393 C  CG2 . THR B  1 933 ? 19.173  -5.932  70.094  1.00 46.90  ? 933  THR C CG2 1 
ATOM   14394 N  N   . VAL B  1 934 ? 20.563  -8.933  68.602  1.00 58.15  ? 934  VAL C N   1 
ATOM   14395 C  CA  . VAL B  1 934 ? 19.823  -9.886  67.790  1.00 59.19  ? 934  VAL C CA  1 
ATOM   14396 C  C   . VAL B  1 934 ? 19.967  -11.271 68.403  1.00 64.52  ? 934  VAL C C   1 
ATOM   14397 O  O   . VAL B  1 934 ? 19.007  -12.045 68.466  1.00 62.28  ? 934  VAL C O   1 
ATOM   14398 C  CB  . VAL B  1 934 ? 20.324  -9.900  66.331  1.00 63.83  ? 934  VAL C CB  1 
ATOM   14399 C  CG1 . VAL B  1 934 ? 19.909  -11.182 65.629  1.00 62.83  ? 934  VAL C CG1 1 
ATOM   14400 C  CG2 . VAL B  1 934 ? 19.803  -8.690  65.572  1.00 63.31  ? 934  VAL C CG2 1 
ATOM   14401 N  N   . LEU B  1 935 ? 21.181  -11.573 68.852  1.00 60.81  ? 935  LEU C N   1 
ATOM   14402 C  CA  . LEU B  1 935 ? 21.422  -12.766 69.642  1.00 60.74  ? 935  LEU C CA  1 
ATOM   14403 C  C   . LEU B  1 935 ? 20.388  -12.847 70.754  1.00 65.25  ? 935  LEU C C   1 
ATOM   14404 O  O   . LEU B  1 935 ? 19.546  -13.746 70.773  1.00 67.39  ? 935  LEU C O   1 
ATOM   14405 C  CB  . LEU B  1 935 ? 22.836  -12.763 70.238  1.00 59.30  ? 935  LEU C CB  1 
ATOM   14406 C  CG  . LEU B  1 935 ? 24.006  -13.173 69.340  1.00 57.61  ? 935  LEU C CG  1 
ATOM   14407 C  CD1 . LEU B  1 935 ? 25.194  -13.632 70.179  1.00 57.93  ? 935  LEU C CD1 1 
ATOM   14408 C  CD2 . LEU B  1 935 ? 23.580  -14.241 68.336  1.00 57.10  ? 935  LEU C CD2 1 
ATOM   14409 N  N   . GLU B  1 936 ? 20.430  -11.872 71.653  1.00 61.44  ? 936  GLU C N   1 
ATOM   14410 C  CA  . GLU B  1 936 ? 19.564  -11.879 72.815  1.00 60.89  ? 936  GLU C CA  1 
ATOM   14411 C  C   . GLU B  1 936 ? 18.085  -11.888 72.432  1.00 60.65  ? 936  GLU C C   1 
ATOM   14412 O  O   . GLU B  1 936 ? 17.237  -12.268 73.237  1.00 65.89  ? 936  GLU C O   1 
ATOM   14413 C  CB  . GLU B  1 936 ? 19.881  -10.677 73.712  1.00 59.78  ? 936  GLU C CB  1 
ATOM   14414 C  CG  . GLU B  1 936 ? 21.261  -10.744 74.366  1.00 62.67  ? 936  GLU C CG  1 
ATOM   14415 C  CD  . GLU B  1 936 ? 21.588  -9.505  75.198  1.00 76.63  ? 936  GLU C CD  1 
ATOM   14416 O  OE1 . GLU B  1 936 ? 20.697  -8.629  75.328  1.00 77.04  ? 936  GLU C OE1 1 
ATOM   14417 O  OE2 . GLU B  1 936 ? 22.730  -9.406  75.718  1.00 72.13  ? 936  GLU C OE2 1 
ATOM   14418 N  N   . THR B  1 937 ? 17.764  -11.497 71.205  1.00 60.51  ? 937  THR C N   1 
ATOM   14419 C  CA  . THR B  1 937 ? 16.358  -11.394 70.832  1.00 65.62  ? 937  THR C CA  1 
ATOM   14420 C  C   . THR B  1 937 ? 15.794  -12.738 70.374  1.00 65.07  ? 937  THR C C   1 
ATOM   14421 O  O   . THR B  1 937 ? 14.653  -13.078 70.692  1.00 64.58  ? 937  THR C O   1 
ATOM   14422 C  CB  . THR B  1 937 ? 16.131  -10.331 69.743  1.00 62.52  ? 937  THR C CB  1 
ATOM   14423 O  OG1 . THR B  1 937 ? 16.627  -9.071  70.212  1.00 57.65  ? 937  THR C OG1 1 
ATOM   14424 C  CG2 . THR B  1 937 ? 14.639  -10.195 69.437  1.00 55.35  ? 937  THR C CG2 1 
ATOM   14425 N  N   . ILE B  1 938 ? 16.586  -13.514 69.650  1.00 62.85  ? 938  ILE C N   1 
ATOM   14426 C  CA  . ILE B  1 938 ? 16.148  -14.853 69.294  1.00 69.97  ? 938  ILE C CA  1 
ATOM   14427 C  C   . ILE B  1 938 ? 16.052  -15.718 70.560  1.00 70.09  ? 938  ILE C C   1 
ATOM   14428 O  O   . ILE B  1 938 ? 15.074  -16.437 70.758  1.00 68.89  ? 938  ILE C O   1 
ATOM   14429 C  CB  . ILE B  1 938 ? 17.090  -15.491 68.283  1.00 68.23  ? 938  ILE C CB  1 
ATOM   14430 C  CG1 . ILE B  1 938 ? 17.462  -14.472 67.210  1.00 64.06  ? 938  ILE C CG1 1 
ATOM   14431 C  CG2 . ILE B  1 938 ? 16.442  -16.714 67.653  1.00 69.13  ? 938  ILE C CG2 1 
ATOM   14432 C  CD1 . ILE B  1 938 ? 18.634  -14.897 66.337  1.00 68.85  ? 938  ILE C CD1 1 
ATOM   14433 N  N   . THR B  1 939 ? 17.064  -15.614 71.418  1.00 65.49  ? 939  THR C N   1 
ATOM   14434 C  CA  . THR B  1 939 ? 17.081  -16.298 72.711  1.00 71.56  ? 939  THR C CA  1 
ATOM   14435 C  C   . THR B  1 939 ? 15.812  -16.038 73.543  1.00 76.28  ? 939  THR C C   1 
ATOM   14436 O  O   . THR B  1 939 ? 15.254  -16.956 74.150  1.00 77.84  ? 939  THR C O   1 
ATOM   14437 C  CB  . THR B  1 939 ? 18.317  -15.876 73.538  1.00 74.72  ? 939  THR C CB  1 
ATOM   14438 O  OG1 . THR B  1 939 ? 19.516  -16.199 72.817  1.00 62.16  ? 939  THR C OG1 1 
ATOM   14439 C  CG2 . THR B  1 939 ? 18.324  -16.572 74.901  1.00 71.35  ? 939  THR C CG2 1 
ATOM   14440 N  N   . LYS B  1 940 ? 15.369  -14.783 73.567  1.00 76.99  ? 940  LYS C N   1 
ATOM   14441 C  CA  . LYS B  1 940 ? 14.109  -14.398 74.205  1.00 74.42  ? 940  LYS C CA  1 
ATOM   14442 C  C   . LYS B  1 940 ? 12.902  -15.094 73.552  1.00 69.54  ? 940  LYS C C   1 
ATOM   14443 O  O   . LYS B  1 940 ? 12.016  -15.603 74.244  1.00 64.93  ? 940  LYS C O   1 
ATOM   14444 C  CB  . LYS B  1 940 ? 13.945  -12.873 74.145  1.00 72.94  ? 940  LYS C CB  1 
ATOM   14445 C  CG  . LYS B  1 940 ? 12.605  -12.351 74.655  1.00 75.46  ? 940  LYS C CG  1 
ATOM   14446 C  CD  . LYS B  1 940 ? 12.389  -10.902 74.253  1.00 70.48  ? 940  LYS C CD  1 
ATOM   14447 C  CE  . LYS B  1 940 ? 12.228  -10.738 72.746  1.00 70.10  ? 940  LYS C CE  1 
ATOM   14448 N  NZ  . LYS B  1 940 ? 10.889  -11.178 72.257  1.00 70.17  ? 940  LYS C NZ  1 
ATOM   14449 N  N   . ASN B  1 941 ? 12.889  -15.104 72.219  1.00 71.81  ? 941  ASN C N   1 
ATOM   14450 C  CA  . ASN B  1 941 ? 11.849  -15.756 71.424  1.00 66.63  ? 941  ASN C CA  1 
ATOM   14451 C  C   . ASN B  1 941 ? 11.765  -17.245 71.692  1.00 74.11  ? 941  ASN C C   1 
ATOM   14452 O  O   . ASN B  1 941 ? 10.692  -17.848 71.599  1.00 71.18  ? 941  ASN C O   1 
ATOM   14453 C  CB  . ASN B  1 941 ? 12.104  -15.526 69.938  1.00 70.87  ? 941  ASN C CB  1 
ATOM   14454 C  CG  . ASN B  1 941 ? 11.602  -14.178 69.461  1.00 65.52  ? 941  ASN C CG  1 
ATOM   14455 O  OD1 . ASN B  1 941 ? 10.679  -14.102 68.659  1.00 66.21  ? 941  ASN C OD1 1 
ATOM   14456 N  ND2 . ASN B  1 941 ? 12.195  -13.112 69.968  1.00 62.32  ? 941  ASN C ND2 1 
ATOM   14457 N  N   . ILE B  1 942 ? 12.917  -17.824 72.018  1.00 74.90  ? 942  ILE C N   1 
ATOM   14458 C  CA  . ILE B  1 942 ? 13.026  -19.233 72.346  1.00 71.68  ? 942  ILE C CA  1 
ATOM   14459 C  C   . ILE B  1 942 ? 12.367  -19.549 73.678  1.00 71.79  ? 942  ILE C C   1 
ATOM   14460 O  O   . ILE B  1 942 ? 11.444  -20.364 73.755  1.00 69.31  ? 942  ILE C O   1 
ATOM   14461 C  CB  . ILE B  1 942 ? 14.491  -19.666 72.414  1.00 70.51  ? 942  ILE C CB  1 
ATOM   14462 C  CG1 . ILE B  1 942 ? 15.145  -19.549 71.040  1.00 70.53  ? 942  ILE C CG1 1 
ATOM   14463 C  CG2 . ILE B  1 942 ? 14.599  -21.088 72.969  1.00 67.46  ? 942  ILE C CG2 1 
ATOM   14464 C  CD1 . ILE B  1 942 ? 16.612  -19.934 71.026  1.00 67.76  ? 942  ILE C CD1 1 
ATOM   14465 N  N   . LYS B  1 943 ? 12.865  -18.900 74.726  1.00 71.27  ? 943  LYS C N   1 
ATOM   14466 C  CA  . LYS B  1 943 ? 12.383  -19.128 76.077  1.00 69.20  ? 943  LYS C CA  1 
ATOM   14467 C  C   . LYS B  1 943 ? 10.897  -18.856 76.165  1.00 72.17  ? 943  LYS C C   1 
ATOM   14468 O  O   . LYS B  1 943 ? 10.196  -19.472 76.960  1.00 79.74  ? 943  LYS C O   1 
ATOM   14469 C  CB  . LYS B  1 943 ? 13.136  -18.256 77.079  1.00 72.14  ? 943  LYS C CB  1 
ATOM   14470 C  CG  . LYS B  1 943 ? 14.624  -18.565 77.190  1.00 81.13  ? 943  LYS C CG  1 
ATOM   14471 C  CD  . LYS B  1 943 ? 15.331  -17.493 78.010  1.00 92.28  ? 943  LYS C CD  1 
ATOM   14472 C  CE  . LYS B  1 943 ? 16.799  -17.814 78.258  1.00 97.98  ? 943  LYS C CE  1 
ATOM   14473 N  NZ  . LYS B  1 943 ? 17.469  -16.749 79.070  1.00 101.59 ? 943  LYS C NZ  1 
ATOM   14474 N  N   . TRP B  1 944 ? 10.412  -17.942 75.334  1.00 72.22  ? 944  TRP C N   1 
ATOM   14475 C  CA  . TRP B  1 944 ? 9.005   -17.575 75.379  1.00 74.86  ? 944  TRP C CA  1 
ATOM   14476 C  C   . TRP B  1 944 ? 8.120   -18.701 74.838  1.00 75.86  ? 944  TRP C C   1 
ATOM   14477 O  O   . TRP B  1 944 ? 6.954   -18.822 75.224  1.00 75.94  ? 944  TRP C O   1 
ATOM   14478 C  CB  . TRP B  1 944 ? 8.759   -16.281 74.607  1.00 67.91  ? 944  TRP C CB  1 
ATOM   14479 C  CG  . TRP B  1 944 ? 7.379   -15.764 74.800  1.00 68.12  ? 944  TRP C CG  1 
ATOM   14480 C  CD1 . TRP B  1 944 ? 6.972   -14.842 75.719  1.00 64.14  ? 944  TRP C CD1 1 
ATOM   14481 C  CD2 . TRP B  1 944 ? 6.205   -16.155 74.070  1.00 70.80  ? 944  TRP C CD2 1 
ATOM   14482 N  NE1 . TRP B  1 944 ? 5.622   -14.626 75.601  1.00 70.00  ? 944  TRP C NE1 1 
ATOM   14483 C  CE2 . TRP B  1 944 ? 5.126   -15.422 74.600  1.00 72.02  ? 944  TRP C CE2 1 
ATOM   14484 C  CE3 . TRP B  1 944 ? 5.965   -17.050 73.019  1.00 69.55  ? 944  TRP C CE3 1 
ATOM   14485 C  CZ2 . TRP B  1 944 ? 3.821   -15.557 74.112  1.00 71.34  ? 944  TRP C CZ2 1 
ATOM   14486 C  CZ3 . TRP B  1 944 ? 4.672   -17.181 72.536  1.00 69.53  ? 944  TRP C CZ3 1 
ATOM   14487 C  CH2 . TRP B  1 944 ? 3.617   -16.437 73.079  1.00 70.34  ? 944  TRP C CH2 1 
ATOM   14488 N  N   . LEU B  1 945 ? 8.674   -19.524 73.951  1.00 78.19  ? 945  LEU C N   1 
ATOM   14489 C  CA  . LEU B  1 945 ? 7.965   -20.712 73.468  1.00 80.48  ? 945  LEU C CA  1 
ATOM   14490 C  C   . LEU B  1 945 ? 7.973   -21.837 74.519  1.00 81.56  ? 945  LEU C C   1 
ATOM   14491 O  O   . LEU B  1 945 ? 6.921   -22.409 74.829  1.00 78.47  ? 945  LEU C O   1 
ATOM   14492 C  CB  . LEU B  1 945 ? 8.573   -21.193 72.152  1.00 76.93  ? 945  LEU C CB  1 
ATOM   14493 C  CG  . LEU B  1 945 ? 8.299   -20.228 70.999  1.00 75.74  ? 945  LEU C CG  1 
ATOM   14494 C  CD1 . LEU B  1 945 ? 9.021   -20.652 69.742  1.00 71.52  ? 945  LEU C CD1 1 
ATOM   14495 C  CD2 . LEU B  1 945 ? 6.806   -20.132 70.754  1.00 77.26  ? 945  LEU C CD2 1 
ATOM   14496 N  N   . GLU B  1 946 ? 9.151   -22.124 75.079  1.00 77.30  ? 946  GLU C N   1 
ATOM   14497 C  CA  . GLU B  1 946 ? 9.306   -23.086 76.176  1.00 75.11  ? 946  GLU C CA  1 
ATOM   14498 C  C   . GLU B  1 946 ? 8.327   -22.905 77.339  1.00 78.45  ? 946  GLU C C   1 
ATOM   14499 O  O   . GLU B  1 946 ? 7.986   -23.870 78.020  1.00 88.53  ? 946  GLU C O   1 
ATOM   14500 C  CB  . GLU B  1 946 ? 10.716  -23.012 76.759  1.00 75.87  ? 946  GLU C CB  1 
ATOM   14501 C  CG  . GLU B  1 946 ? 11.860  -23.050 75.768  1.00 76.09  ? 946  GLU C CG  1 
ATOM   14502 C  CD  . GLU B  1 946 ? 13.199  -22.808 76.462  1.00 76.55  ? 946  GLU C CD  1 
ATOM   14503 O  OE1 . GLU B  1 946 ? 13.177  -22.305 77.604  1.00 80.79  ? 946  GLU C OE1 1 
ATOM   14504 O  OE2 . GLU B  1 946 ? 14.260  -23.119 75.881  1.00 74.62  ? 946  GLU C OE2 1 
ATOM   14505 N  N   . LYS B  1 947 ? 7.897   -21.673 77.586  1.00 78.72  ? 947  LYS C N   1 
ATOM   14506 C  CA  . LYS B  1 947 ? 7.147   -21.372 78.799  1.00 79.74  ? 947  LYS C CA  1 
ATOM   14507 C  C   . LYS B  1 947 ? 5.660   -21.108 78.567  1.00 77.03  ? 947  LYS C C   1 
ATOM   14508 O  O   . LYS B  1 947 ? 4.861   -21.197 79.501  1.00 80.77  ? 947  LYS C O   1 
ATOM   14509 C  CB  . LYS B  1 947 ? 7.771   -20.168 79.513  1.00 82.72  ? 947  LYS C CB  1 
ATOM   14510 C  CG  . LYS B  1 947 ? 9.201   -20.389 79.994  1.00 82.57  ? 947  LYS C CG  1 
ATOM   14511 C  CD  . LYS B  1 947 ? 9.267   -21.334 81.187  1.00 84.74  ? 947  LYS C CD  1 
ATOM   14512 C  CE  . LYS B  1 947 ? 10.710  -21.563 81.616  1.00 90.35  ? 947  LYS C CE  1 
ATOM   14513 N  NZ  . LYS B  1 947 ? 10.863  -22.584 82.695  1.00 81.07  ? 947  LYS C NZ  1 
ATOM   14514 N  N   . ASN B  1 948 ? 5.278   -20.786 77.339  1.00 73.36  ? 948  ASN C N   1 
ATOM   14515 C  CA  . ASN B  1 948 ? 3.890   -20.414 77.087  1.00 78.55  ? 948  ASN C CA  1 
ATOM   14516 C  C   . ASN B  1 948 ? 3.254   -21.104 75.886  1.00 83.85  ? 948  ASN C C   1 
ATOM   14517 O  O   . ASN B  1 948 ? 2.066   -20.931 75.639  1.00 86.24  ? 948  ASN C O   1 
ATOM   14518 C  CB  . ASN B  1 948 ? 3.769   -18.896 76.906  1.00 80.16  ? 948  ASN C CB  1 
ATOM   14519 C  CG  . ASN B  1 948 ? 4.152   -18.119 78.158  1.00 82.95  ? 948  ASN C CG  1 
ATOM   14520 O  OD1 . ASN B  1 948 ? 3.491   -18.227 79.203  1.00 80.04  ? 948  ASN C OD1 1 
ATOM   14521 N  ND2 . ASN B  1 948 ? 5.216   -17.314 78.055  1.00 75.31  ? 948  ASN C ND2 1 
ATOM   14522 N  N   . LEU B  1 949 ? 4.023   -21.880 75.133  1.00 83.69  ? 949  LEU C N   1 
ATOM   14523 C  CA  . LEU B  1 949 ? 3.447   -22.535 73.963  1.00 85.94  ? 949  LEU C CA  1 
ATOM   14524 C  C   . LEU B  1 949 ? 2.342   -23.545 74.321  1.00 89.06  ? 949  LEU C C   1 
ATOM   14525 O  O   . LEU B  1 949 ? 1.260   -23.493 73.728  1.00 87.37  ? 949  LEU C O   1 
ATOM   14526 C  CB  . LEU B  1 949 ? 4.534   -23.219 73.131  1.00 87.67  ? 949  LEU C CB  1 
ATOM   14527 C  CG  . LEU B  1 949 ? 4.032   -23.660 71.761  1.00 88.55  ? 949  LEU C CG  1 
ATOM   14528 C  CD1 . LEU B  1 949 ? 3.300   -22.501 71.115  1.00 91.30  ? 949  LEU C CD1 1 
ATOM   14529 C  CD2 . LEU B  1 949 ? 5.186   -24.129 70.892  1.00 88.14  ? 949  LEU C CD2 1 
ATOM   14530 N  N   . PRO B  1 950 ? 2.600   -24.466 75.281  1.00 84.69  ? 950  PRO C N   1 
ATOM   14531 C  CA  . PRO B  1 950 ? 1.515   -25.410 75.584  1.00 86.67  ? 950  PRO C CA  1 
ATOM   14532 C  C   . PRO B  1 950 ? 0.329   -24.706 76.217  1.00 85.70  ? 950  PRO C C   1 
ATOM   14533 O  O   . PRO B  1 950 ? -0.823  -25.005 75.903  1.00 85.82  ? 950  PRO C O   1 
ATOM   14534 C  CB  . PRO B  1 950 ? 2.158   -26.396 76.566  1.00 80.46  ? 950  PRO C CB  1 
ATOM   14535 C  CG  . PRO B  1 950 ? 3.312   -25.675 77.143  1.00 84.43  ? 950  PRO C CG  1 
ATOM   14536 C  CD  . PRO B  1 950 ? 3.809   -24.749 76.080  1.00 84.38  ? 950  PRO C CD  1 
ATOM   14537 N  N   . THR B  1 951 ? 0.635   -23.765 77.102  1.00 83.11  ? 951  THR C N   1 
ATOM   14538 C  CA  . THR B  1 951 ? -0.357  -22.876 77.686  1.00 86.15  ? 951  THR C CA  1 
ATOM   14539 C  C   . THR B  1 951 ? -1.195  -22.210 76.585  1.00 90.94  ? 951  THR C C   1 
ATOM   14540 O  O   . THR B  1 951 ? -2.390  -21.937 76.776  1.00 87.76  ? 951  THR C O   1 
ATOM   14541 C  CB  . THR B  1 951 ? 0.330   -21.795 78.561  1.00 86.20  ? 951  THR C CB  1 
ATOM   14542 O  OG1 . THR B  1 951 ? 1.232   -22.421 79.485  1.00 76.76  ? 951  THR C OG1 1 
ATOM   14543 C  CG2 . THR B  1 951 ? -0.687  -20.976 79.328  1.00 85.91  ? 951  THR C CG2 1 
ATOM   14544 N  N   . LEU B  1 952 ? -0.559  -21.969 75.432  1.00 92.64  ? 952  LEU C N   1 
ATOM   14545 C  CA  . LEU B  1 952 ? -1.225  -21.384 74.262  1.00 91.30  ? 952  LEU C CA  1 
ATOM   14546 C  C   . LEU B  1 952 ? -2.077  -22.418 73.522  1.00 89.98  ? 952  LEU C C   1 
ATOM   14547 O  O   . LEU B  1 952 ? -3.177  -22.100 73.064  1.00 90.94  ? 952  LEU C O   1 
ATOM   14548 C  CB  . LEU B  1 952 ? -0.197  -20.764 73.301  1.00 88.44  ? 952  LEU C CB  1 
ATOM   14549 C  CG  . LEU B  1 952 ? -0.720  -19.946 72.108  1.00 80.54  ? 952  LEU C CG  1 
ATOM   14550 C  CD1 . LEU B  1 952 ? -1.630  -18.823 72.549  1.00 80.43  ? 952  LEU C CD1 1 
ATOM   14551 C  CD2 . LEU B  1 952 ? 0.426   -19.389 71.291  1.00 83.57  ? 952  LEU C CD2 1 
ATOM   14552 N  N   . ARG B  1 953 ? -1.572  -23.646 73.403  1.00 84.38  ? 953  ARG C N   1 
ATOM   14553 C  CA  . ARG B  1 953 ? -2.367  -24.732 72.838  1.00 89.59  ? 953  ARG C CA  1 
ATOM   14554 C  C   . ARG B  1 953 ? -3.681  -24.849 73.584  1.00 92.11  ? 953  ARG C C   1 
ATOM   14555 O  O   . ARG B  1 953 ? -4.758  -24.964 72.984  1.00 89.16  ? 953  ARG C O   1 
ATOM   14556 C  CB  . ARG B  1 953 ? -1.633  -26.069 72.924  1.00 91.33  ? 953  ARG C CB  1 
ATOM   14557 C  CG  . ARG B  1 953 ? -0.321  -26.155 72.201  1.00 89.31  ? 953  ARG C CG  1 
ATOM   14558 C  CD  . ARG B  1 953 ? 0.173   -27.587 72.245  1.00 88.38  ? 953  ARG C CD  1 
ATOM   14559 N  NE  . ARG B  1 953 ? 1.161   -27.865 71.209  1.00 98.03  ? 953  ARG C NE  1 
ATOM   14560 C  CZ  . ARG B  1 953 ? 0.868   -28.017 69.919  1.00 103.49 ? 953  ARG C CZ  1 
ATOM   14561 N  NH1 . ARG B  1 953 ? -0.388  -27.908 69.507  1.00 103.58 ? 953  ARG C NH1 1 
ATOM   14562 N  NH2 . ARG B  1 953 ? 1.830   -28.274 69.039  1.00 104.05 ? 953  ARG C NH2 1 
ATOM   14563 N  N   . THR B  1 954 ? -3.558  -24.810 74.911  1.00 94.64  ? 954  THR C N   1 
ATOM   14564 C  CA  . THR B  1 954 ? -4.653  -25.072 75.836  1.00 91.89  ? 954  THR C CA  1 
ATOM   14565 C  C   . THR B  1 954 ? -5.698  -23.972 75.837  1.00 89.63  ? 954  THR C C   1 
ATOM   14566 O  O   . THR B  1 954 ? -6.889  -24.237 75.719  1.00 88.92  ? 954  THR C O   1 
ATOM   14567 C  CB  . THR B  1 954 ? -4.138  -25.240 77.278  1.00 90.73  ? 954  THR C CB  1 
ATOM   14568 O  OG1 . THR B  1 954 ? -3.214  -26.335 77.347  1.00 88.50  ? 954  THR C OG1 1 
ATOM   14569 C  CG2 . THR B  1 954 ? -5.296  -25.497 78.216  1.00 90.27  ? 954  THR C CG2 1 
ATOM   14570 N  N   . TRP B  1 955 ? -5.246  -22.734 75.985  1.00 92.77  ? 955  TRP C N   1 
ATOM   14571 C  CA  . TRP B  1 955 ? -6.168  -21.612 76.061  1.00 95.36  ? 955  TRP C CA  1 
ATOM   14572 C  C   . TRP B  1 955 ? -6.924  -21.412 74.752  1.00 96.52  ? 955  TRP C C   1 
ATOM   14573 O  O   . TRP B  1 955 ? -8.077  -20.979 74.750  1.00 96.80  ? 955  TRP C O   1 
ATOM   14574 C  CB  . TRP B  1 955 ? -5.429  -20.331 76.428  1.00 92.22  ? 955  TRP C CB  1 
ATOM   14575 C  CG  . TRP B  1 955 ? -6.363  -19.232 76.813  1.00 95.97  ? 955  TRP C CG  1 
ATOM   14576 C  CD1 . TRP B  1 955 ? -6.764  -18.902 78.078  1.00 99.76  ? 955  TRP C CD1 1 
ATOM   14577 C  CD2 . TRP B  1 955 ? -7.040  -18.327 75.930  1.00 96.78  ? 955  TRP C CD2 1 
ATOM   14578 N  NE1 . TRP B  1 955 ? -7.637  -17.842 78.039  1.00 98.50  ? 955  TRP C NE1 1 
ATOM   14579 C  CE2 . TRP B  1 955 ? -7.826  -17.471 76.733  1.00 97.66  ? 955  TRP C CE2 1 
ATOM   14580 C  CE3 . TRP B  1 955 ? -7.047  -18.145 74.542  1.00 92.49  ? 955  TRP C CE3 1 
ATOM   14581 C  CZ2 . TRP B  1 955 ? -8.601  -16.452 76.196  1.00 95.83  ? 955  TRP C CZ2 1 
ATOM   14582 C  CZ3 . TRP B  1 955 ? -7.829  -17.136 74.008  1.00 95.24  ? 955  TRP C CZ3 1 
ATOM   14583 C  CH2 . TRP B  1 955 ? -8.595  -16.301 74.835  1.00 99.57  ? 955  TRP C CH2 1 
ATOM   14584 N  N   . LEU B  1 956 ? -6.269  -21.729 73.641  1.00 94.65  ? 956  LEU C N   1 
ATOM   14585 C  CA  . LEU B  1 956 ? -6.876  -21.570 72.326  1.00 94.56  ? 956  LEU C CA  1 
ATOM   14586 C  C   . LEU B  1 956 ? -7.940  -22.616 72.063  1.00 96.93  ? 956  LEU C C   1 
ATOM   14587 O  O   . LEU B  1 956 ? -9.032  -22.292 71.587  1.00 96.18  ? 956  LEU C O   1 
ATOM   14588 C  CB  . LEU B  1 956 ? -5.813  -21.644 71.236  1.00 97.05  ? 956  LEU C CB  1 
ATOM   14589 C  CG  . LEU B  1 956 ? -5.414  -20.293 70.654  1.00 93.77  ? 956  LEU C CG  1 
ATOM   14590 C  CD1 . LEU B  1 956 ? -5.104  -19.306 71.767  1.00 97.67  ? 956  LEU C CD1 1 
ATOM   14591 C  CD2 . LEU B  1 956 ? -4.218  -20.469 69.739  1.00 98.27  ? 956  LEU C CD2 1 
ATOM   14592 N  N   . MET B  1 957 ? -7.611  -23.869 72.372  1.00 100.18 ? 957  MET C N   1 
ATOM   14593 C  CA  . MET B  1 957 ? -8.522  -24.981 72.134  1.00 96.29  ? 957  MET C CA  1 
ATOM   14594 C  C   . MET B  1 957 ? -9.825  -24.822 72.937  1.00 97.12  ? 957  MET C C   1 
ATOM   14595 O  O   . MET B  1 957 ? -10.880 -25.270 72.491  1.00 99.42  ? 957  MET C O   1 
ATOM   14596 C  CB  . MET B  1 957 ? -7.841  -26.315 72.451  1.00 87.87  ? 957  MET C CB  1 
ATOM   14597 C  CG  . MET B  1 957 ? -7.790  -26.681 73.924  1.00 96.74  ? 957  MET C CG  1 
ATOM   14598 S  SD  . MET B  1 957 ? -8.260  -28.401 74.229  1.00 85.08  ? 957  MET C SD  1 
ATOM   14599 C  CE  . MET B  1 957 ? -10.040 -28.265 74.465  1.00 82.11  ? 957  MET C CE  1 
ATOM   14600 N  N   . VAL B  1 958 ? -9.747  -24.167 74.099  1.00 95.91  ? 958  VAL C N   1 
ATOM   14601 C  CA  . VAL B  1 958 ? -10.927 -23.809 74.893  1.00 95.35  ? 958  VAL C CA  1 
ATOM   14602 C  C   . VAL B  1 958 ? -11.966 -23.073 74.037  1.00 98.11  ? 958  VAL C C   1 
ATOM   14603 O  O   . VAL B  1 958 ? -13.173 -23.294 74.170  1.00 100.85 ? 958  VAL C O   1 
ATOM   14604 C  CB  . VAL B  1 958 ? -10.546 -22.919 76.125  1.00 98.76  ? 958  VAL C CB  1 
ATOM   14605 C  CG1 . VAL B  1 958 ? -11.789 -22.492 76.918  1.00 100.07 ? 958  VAL C CG1 1 
ATOM   14606 C  CG2 . VAL B  1 958 ? -9.571  -23.642 77.039  1.00 93.08  ? 958  VAL C CG2 1 
ATOM   14607 N  N   . ASN B  1 959 ? -11.491 -22.212 73.143  1.00 99.64  ? 959  ASN C N   1 
ATOM   14608 C  CA  . ASN B  1 959 ? -12.383 -21.463 72.270  1.00 95.41  ? 959  ASN C CA  1 
ATOM   14609 C  C   . ASN B  1 959 ? -12.762 -22.173 70.985  1.00 99.44  ? 959  ASN C C   1 
ATOM   14610 O  O   . ASN B  1 959 ? -13.403 -21.573 70.122  1.00 97.25  ? 959  ASN C O   1 
ATOM   14611 C  CB  . ASN B  1 959 ? -11.756 -20.129 71.930  1.00 89.57  ? 959  ASN C CB  1 
ATOM   14612 C  CG  . ASN B  1 959 ? -11.989 -19.115 73.005  1.00 96.45  ? 959  ASN C CG  1 
ATOM   14613 O  OD1 . ASN B  1 959 ? -12.912 -18.306 72.913  1.00 97.03  ? 959  ASN C OD1 1 
ATOM   14614 N  ND2 . ASN B  1 959 ? -11.176 -19.166 74.060  1.00 90.72  ? 959  ASN C ND2 1 
ATOM   14615 N  N   . THR B  1 960 ? -12.389 -23.437 71.014  1.00 100.51 ? 960  THR C N   1 
ATOM   14616 C  CA  . THR B  1 960 ? -12.507 -24.406 69.987  1.00 101.75 ? 960  THR C CA  1 
ATOM   14617 C  C   . THR B  1 960 ? -13.941 -24.873 69.931  1.00 102.19 ? 960  THR C C   1 
ATOM   14618 O  O   . THR B  1 960 ? -14.430 -25.548 70.834  1.00 95.62  ? 960  THR C O   1 
ATOM   14619 C  CB  . THR B  1 960 ? -11.592 -25.571 70.386  1.00 99.75  ? 960  THR C CB  1 
ATOM   14620 O  OG1 . THR B  1 960 ? -10.844 -25.180 71.548  1.00 95.29  ? 960  THR C OG1 1 
ATOM   14621 C  CG2 . THR B  1 960 ? -10.625 -25.887 69.285  1.00 92.11  ? 960  THR C CG2 1 
ATOM   14622 N  N   . ARG B  1 961 ? -14.622 -24.498 68.861  1.00 101.09 ? 961  ARG C N   1 
ATOM   14623 C  CA  . ARG B  1 961 ? -15.920 -25.064 68.576  1.00 98.58  ? 961  ARG C CA  1 
ATOM   14624 C  C   . ARG B  1 961 ? -15.653 -26.445 68.043  1.00 97.31  ? 961  ARG C C   1 
ATOM   14625 O  O   . ARG B  1 961 ? -15.243 -26.498 66.843  1.00 96.82  ? 961  ARG C O   1 
ATOM   14626 C  CB  . ARG B  1 961 ? -16.646 -24.248 67.524  1.00 84.94  ? 961  ARG C CB  1 
ATOM   14627 C  CG  . ARG B  1 961 ? -17.885 -24.906 66.986  1.00 85.95  ? 961  ARG C CG  1 
ATOM   14628 C  CD  . ARG B  1 961 ? -19.103 -24.087 67.341  1.00 95.84  ? 961  ARG C CD  1 
ATOM   14629 N  NE  . ARG B  1 961 ? -20.087 -24.042 66.268  1.00 102.14 ? 961  ARG C NE  1 
ATOM   14630 C  CZ  . ARG B  1 961 ? -20.144 -23.085 65.356  1.00 100.31 ? 961  ARG C CZ  1 
ATOM   14631 N  NH1 . ARG B  1 961 ? -19.275 -22.095 65.391  1.00 96.35  ? 961  ARG C NH1 1 
ATOM   14632 N  NH2 . ARG B  1 961 ? -21.065 -23.123 64.409  1.00 100.79 ? 961  ARG C NH2 1 
ATOM   14633 N  N   . HIS B  1 962 ? -15.832 -27.425 68.833  1.00 30.00  ? 962  HIS C N   1 
HETATM 14634 C  C6  . 2X0 C  2 1   ? 16.632  3.589   3.140   1.00 36.33  ? 1    2X0 E C6  1 
HETATM 14635 C  C8  . 2X0 C  2 1   ? 15.740  2.346   3.210   1.00 42.56  ? 1    2X0 E C8  1 
HETATM 14636 C  C3  . 2X0 C  2 1   ? 18.331  4.630   1.866   1.00 32.47  ? 1    2X0 E C3  1 
HETATM 14637 O  O11 . 2X0 C  2 1   ? 20.804  5.674   1.812   1.00 24.04  ? 1    2X0 E O11 1 
HETATM 14638 P  P11 . 2X0 C  2 1   ? 20.100  4.411   1.886   1.00 31.25  ? 1    2X0 E P11 1 
HETATM 14639 O  O12 . 2X0 C  2 1   ? 20.542  3.509   0.847   1.00 26.03  ? 1    2X0 E O12 1 
HETATM 14640 N  N10 . 2X0 C  2 1   ? 17.880  5.265   0.845   1.00 26.26  ? 1    2X0 E N10 1 
HETATM 14641 C  C1  . 2X0 C  2 1   ? 17.710  3.422   2.063   1.00 33.43  ? 1    2X0 E C1  1 
HETATM 14642 C  C17 . 2X0 C  2 1   ? 16.019  1.189   3.930   1.00 50.77  ? 1    2X0 E C17 1 
HETATM 14643 C  C18 . 2X0 C  2 1   ? 15.112  0.107   3.930   1.00 44.32  ? 1    2X0 E C18 1 
HETATM 14644 C  C19 . 2X0 C  2 1   ? 13.936  0.130   3.263   1.00 39.97  ? 1    2X0 E C19 1 
HETATM 14645 C  C20 . 2X0 C  2 1   ? 13.639  1.296   2.541   1.00 45.40  ? 1    2X0 E C20 1 
HETATM 14646 C  C21 . 2X0 C  2 1   ? 14.538  2.384   2.528   1.00 36.35  ? 1    2X0 E C21 1 
HETATM 14647 C  CA  . 7GA C  2 2   ? 21.538  2.667   3.158   1.00 38.77  ? 2    7GA E CA  1 
HETATM 14648 C  C   . 7GA C  2 2   ? 21.285  1.709   4.315   1.00 45.74  ? 2    7GA E C   1 
HETATM 14649 O  O   . 7GA C  2 2   ? 22.091  1.609   5.207   1.00 47.80  ? 2    7GA E O   1 
HETATM 14650 C  C8  . 7GA C  2 2   ? 22.889  3.427   3.438   1.00 35.93  ? 2    7GA E C8  1 
HETATM 14651 C  C9  . 7GA C  2 2   ? 24.188  2.641   3.246   1.00 37.11  ? 2    7GA E C9  1 
HETATM 14652 C  C10 . 7GA C  2 2   ? 25.391  3.560   3.152   1.00 30.68  ? 2    7GA E C10 1 
HETATM 14653 C  C11 . 7GA C  2 2   ? 24.025  1.881   1.920   1.00 43.87  ? 2    7GA E C11 1 
HETATM 14654 C  C6  . 7GA C  2 2   ? 20.425  3.741   3.287   1.00 35.32  ? 2    7GA E C6  1 
ATOM   14655 N  N   . LYS C  2 3   ? 20.057  0.964   4.334   1.00 56.56  ? 3    LYS E N   1 
ATOM   14656 C  CA  . LYS C  2 3   ? 19.784  -0.025  5.404   1.00 68.47  ? 3    LYS E CA  1 
ATOM   14657 C  C   . LYS C  2 3   ? 20.885  -1.073  5.432   1.00 65.93  ? 3    LYS E C   1 
ATOM   14658 O  O   . LYS C  2 3   ? 21.096  -1.723  6.453   1.00 66.67  ? 3    LYS E O   1 
ATOM   14659 C  CB  . LYS C  2 3   ? 18.416  -0.716  5.250   1.00 60.10  ? 3    LYS E CB  1 
ATOM   14660 C  CG  . LYS C  2 3   ? 18.093  -1.212  3.845   1.00 55.37  ? 3    LYS E CG  1 
ATOM   14661 C  CD  . LYS C  2 3   ? 18.705  -2.528  3.539   1.00 60.48  ? 3    LYS E CD  1 
ATOM   14662 C  CE  . LYS C  2 3   ? 18.517  -2.851  2.085   1.00 59.13  ? 3    LYS E CE  1 
ATOM   14663 N  NZ  . LYS C  2 3   ? 18.802  -1.623  1.289   1.00 52.47  ? 3    LYS E NZ  1 
ATOM   14664 N  N   . HIS C  2 4   ? 21.598  -1.208  4.314   1.00 64.69  ? 4    HIS E N   1 
ATOM   14665 C  CA  . HIS C  2 4   ? 22.893  -1.861  4.270   1.00 67.40  ? 4    HIS E CA  1 
ATOM   14666 C  C   . HIS C  2 4   ? 23.816  -1.308  5.360   1.00 65.01  ? 4    HIS E C   1 
ATOM   14667 O  O   . HIS C  2 4   ? 25.003  -1.118  5.126   1.00 68.48  ? 4    HIS E O   1 
ATOM   14668 C  CB  . HIS C  2 4   ? 23.553  -1.680  2.884   1.00 75.16  ? 4    HIS E CB  1 
ATOM   14669 C  CG  . HIS C  2 4   ? 22.873  -2.431  1.773   1.00 66.86  ? 4    HIS E CG  1 
ATOM   14670 N  ND1 . HIS C  2 4   ? 21.671  -2.032  1.227   1.00 57.41  ? 4    HIS E ND1 1 
ATOM   14671 C  CD2 . HIS C  2 4   ? 23.233  -3.556  1.102   1.00 70.40  ? 4    HIS E CD2 1 
ATOM   14672 C  CE1 . HIS C  2 4   ? 21.313  -2.886  0.279   1.00 55.49  ? 4    HIS E CE1 1 
ATOM   14673 N  NE2 . HIS C  2 4   ? 22.245  -3.818  0.180   1.00 55.44  ? 4    HIS E NE2 1 
ATOM   14674 N  N   . HIS C  2 5   ? 23.263  -1.064  6.549   1.00 63.38  ? 5    HIS E N   1 
ATOM   14675 C  CA  . HIS C  2 5   ? 24.018  -0.906  7.782   1.00 64.07  ? 5    HIS E CA  1 
ATOM   14676 C  C   . HIS C  2 5   ? 24.986  -2.066  7.942   1.00 70.67  ? 5    HIS E C   1 
ATOM   14677 O  O   . HIS C  2 5   ? 25.929  -1.965  8.709   1.00 72.75  ? 5    HIS E O   1 
ATOM   14678 C  CB  . HIS C  2 5   ? 23.091  -0.839  9.007   1.00 57.91  ? 5    HIS E CB  1 
ATOM   14679 C  CG  . HIS C  2 5   ? 23.774  -1.184  10.296  1.00 67.90  ? 5    HIS E CG  1 
ATOM   14680 N  ND1 . HIS C  2 5   ? 24.901  -0.517  10.741  1.00 64.91  ? 5    HIS E ND1 1 
ATOM   14681 C  CD2 . HIS C  2 5   ? 23.517  -2.147  11.218  1.00 66.69  ? 5    HIS E CD2 1 
ATOM   14682 C  CE1 . HIS C  2 5   ? 25.294  -1.041  11.891  1.00 64.77  ? 5    HIS E CE1 1 
ATOM   14683 N  NE2 . HIS C  2 5   ? 24.470  -2.030  12.203  1.00 64.30  ? 5    HIS E NE2 1 
ATOM   14684 N  N   . ALA C  2 6   ? 24.742  -3.161  7.223   1.00 69.90  ? 6    ALA E N   1 
ATOM   14685 C  CA  . ALA C  2 6   ? 25.607  -4.336  7.261   1.00 82.02  ? 6    ALA E CA  1 
ATOM   14686 C  C   . ALA C  2 6   ? 26.861  -4.257  6.354   1.00 90.04  ? 6    ALA E C   1 
ATOM   14687 O  O   . ALA C  2 6   ? 26.703  -4.272  5.121   1.00 87.80  ? 6    ALA E O   1 
ATOM   14688 C  CB  . ALA C  2 6   ? 24.787  -5.606  6.910   1.00 77.25  ? 6    ALA E CB  1 
ATOM   14689 N  N   . PHE C  2 7   ? 28.097  -4.160  6.890   1.00 82.62  ? 7    PHE E N   1 
ATOM   14690 C  CA  . PHE C  2 7   ? 28.539  -3.771  8.264   1.00 79.63  ? 7    PHE E CA  1 
ATOM   14691 C  C   . PHE C  2 7   ? 27.668  -4.140  9.506   1.00 82.92  ? 7    PHE E C   1 
ATOM   14692 O  O   . PHE C  2 7   ? 27.521  -3.342  10.433  1.00 81.42  ? 7    PHE E O   1 
ATOM   14693 C  CB  . PHE C  2 7   ? 28.787  -2.245  8.229   1.00 65.89  ? 7    PHE E CB  1 
ATOM   14694 C  CG  . PHE C  2 7   ? 29.638  -1.689  9.369   1.00 59.77  ? 7    PHE E CG  1 
ATOM   14695 C  CD1 . PHE C  2 7   ? 31.022  -1.885  9.392   1.00 59.67  ? 7    PHE E CD1 1 
ATOM   14696 C  CD2 . PHE C  2 7   ? 29.053  -0.890  10.369  1.00 56.48  ? 7    PHE E CD2 1 
ATOM   14697 C  CE1 . PHE C  2 7   ? 31.809  -1.333  10.419  1.00 61.58  ? 7    PHE E CE1 1 
ATOM   14698 C  CE2 . PHE C  2 7   ? 29.818  -0.335  11.410  1.00 50.02  ? 7    PHE E CE2 1 
ATOM   14699 C  CZ  . PHE C  2 7   ? 31.201  -0.552  11.436  1.00 56.53  ? 7    PHE E CZ  1 
ATOM   14700 N  N   . SER C  2 8   ? 27.097  -5.344  9.532   1.00 84.81  ? 8    SER E N   1 
ATOM   14701 C  CA  . SER C  2 8   ? 26.205  -5.714  10.627  1.00 79.73  ? 8    SER E CA  1 
ATOM   14702 C  C   . SER C  2 8   ? 27.100  -5.863  11.848  1.00 88.67  ? 8    SER E C   1 
ATOM   14703 O  O   . SER C  2 8   ? 26.948  -5.140  12.844  1.00 85.92  ? 8    SER E O   1 
ATOM   14704 C  CB  . SER C  2 8   ? 25.423  -7.000  10.314  1.00 83.58  ? 8    SER E CB  1 
ATOM   14705 O  OG  . SER C  2 8   ? 25.975  -7.703  9.206   1.00 80.01  ? 8    SER E OG  1 
ATOM   14706 N  N   . PHE C  2 9   ? 28.050  -6.789  11.733  1.00 87.06  ? 9    PHE E N   1 
ATOM   14707 C  CA  . PHE C  2 9   ? 29.227  -6.842  12.593  1.00 86.29  ? 9    PHE E CA  1 
ATOM   14708 C  C   . PHE C  2 9   ? 30.428  -7.231  11.741  1.00 97.42  ? 9    PHE E C   1 
ATOM   14709 O  O   . PHE C  2 9   ? 30.671  -6.602  10.703  1.00 91.48  ? 9    PHE E O   1 
ATOM   14710 C  CB  . PHE C  2 9   ? 29.030  -7.819  13.751  1.00 73.68  ? 9    PHE E CB  1 
ATOM   14711 C  CG  . PHE C  2 9   ? 28.303  -7.219  14.909  1.00 62.92  ? 9    PHE E CG  1 
ATOM   14712 C  CD1 . PHE C  2 9   ? 28.505  -5.900  15.246  1.00 60.77  ? 9    PHE E CD1 1 
ATOM   14713 C  CD2 . PHE C  2 9   ? 27.409  -7.961  15.649  1.00 57.36  ? 9    PHE E CD2 1 
ATOM   14714 C  CE1 . PHE C  2 9   ? 27.828  -5.335  16.293  1.00 58.84  ? 9    PHE E CE1 1 
ATOM   14715 C  CE2 . PHE C  2 9   ? 26.738  -7.402  16.702  1.00 41.99  ? 9    PHE E CE2 1 
ATOM   14716 C  CZ  . PHE C  2 9   ? 26.940  -6.092  17.022  1.00 54.68  ? 9    PHE E CZ  1 
HETATM 14717 N  N   . LYN C  2 10  ? 31.167  -8.259  12.169  1.00 107.09 ? 10   LYN E N   1 
HETATM 14718 C  CA  . LYN C  2 10  ? 32.346  -8.765  11.388  1.00 100.94 ? 10   LYN E CA  1 
HETATM 14719 C  CB  . LYN C  2 10  ? 33.488  -9.227  12.309  1.00 82.15  ? 10   LYN E CB  1 
HETATM 14720 C  CG  . LYN C  2 10  ? 34.879  -9.201  11.647  1.00 80.49  ? 10   LYN E CG  1 
HETATM 14721 C  CD  . LYN C  2 10  ? 35.043  -8.112  10.573  1.00 83.54  ? 10   LYN E CD  1 
HETATM 14722 C  CE  . LYN C  2 10  ? 35.234  -8.710  9.170   1.00 76.66  ? 10   LYN E CE  1 
HETATM 14723 N  NZ  . LYN C  2 10  ? 36.672  -9.026  8.922   1.00 64.98  ? 10   LYN E NZ  1 
HETATM 14724 C  C   . LYN C  2 10  ? 31.944  -9.840  10.402  1.00 105.56 ? 10   LYN E C   1 
HETATM 14725 O  O   . LYN C  2 10  ? 30.992  -9.643  9.649   1.00 109.03 ? 10   LYN E O   1 
HETATM 14726 N  NT  . LYN C  2 10  ? 32.668  -11.068 10.345  1.00 100.14 ? 10   LYN E NT  1 
HETATM 14727 C  C6  . 2X0 D  2 1   ? 20.135  11.187  59.988  1.00 53.47  ? 1    2X0 F C6  1 
HETATM 14728 C  C8  . 2X0 D  2 1   ? 21.167  10.119  60.369  1.00 47.12  ? 1    2X0 F C8  1 
HETATM 14729 C  C3  . 2X0 D  2 1   ? 18.535  12.663  61.035  1.00 44.32  ? 1    2X0 F C3  1 
HETATM 14730 O  O11 . 2X0 D  2 1   ? 16.220  13.854  61.302  1.00 42.22  ? 1    2X0 F O11 1 
HETATM 14731 P  P11 . 2X0 D  2 1   ? 16.785  12.511  61.318  1.00 44.92  ? 1    2X0 F P11 1 
HETATM 14732 O  O12 . 2X0 D  2 1   ? 16.466  11.853  62.569  1.00 51.53  ? 1    2X0 F O12 1 
HETATM 14733 N  N10 . 2X0 D  2 1   ? 19.039  13.628  61.733  1.00 36.52  ? 1    2X0 F N10 1 
HETATM 14734 C  C1  . 2X0 D  2 1   ? 19.194  11.466  61.176  1.00 48.15  ? 1    2X0 F C1  1 
HETATM 14735 C  C17 . 2X0 D  2 1   ? 21.022  8.758   60.174  1.00 55.48  ? 1    2X0 F C17 1 
HETATM 14736 C  C18 . 2X0 D  2 1   ? 22.028  7.896   60.632  1.00 50.99  ? 1    2X0 F C18 1 
HETATM 14737 C  C19 . 2X0 D  2 1   ? 23.169  8.320   61.244  1.00 43.34  ? 1    2X0 F C19 1 
HETATM 14738 C  C20 . 2X0 D  2 1   ? 23.336  9.689   61.438  1.00 38.89  ? 1    2X0 F C20 1 
HETATM 14739 C  C21 . 2X0 D  2 1   ? 22.324  10.554  61.000  1.00 45.28  ? 1    2X0 F C21 1 
HETATM 14740 C  CA  . 7GA D  2 2   ? 15.079  10.671  60.622  1.00 54.87  ? 2    7GA F CA  1 
HETATM 14741 C  C   . 7GA D  2 2   ? 15.225  9.370   59.838  1.00 65.92  ? 2    7GA F C   1 
HETATM 14742 O  O   . 7GA D  2 2   ? 14.274  8.856   59.284  1.00 66.04  ? 2    7GA F O   1 
HETATM 14743 C  C8  . 7GA D  2 2   ? 13.665  11.287  60.366  1.00 54.35  ? 2    7GA F C8  1 
HETATM 14744 C  C9  . 7GA D  2 2   ? 12.498  10.558  61.049  1.00 51.32  ? 2    7GA F C9  1 
HETATM 14745 C  C10 . 7GA D  2 2   ? 11.226  11.388  61.074  1.00 50.73  ? 2    7GA F C10 1 
HETATM 14746 C  C11 . 7GA D  2 2   ? 12.904  10.187  62.473  1.00 54.77  ? 2    7GA F C11 1 
HETATM 14747 C  C6  . 7GA D  2 2   ? 16.152  11.677  60.115  1.00 50.33  ? 2    7GA F C6  1 
ATOM   14748 N  N   . LYS D  2 3   ? 16.521  8.779   59.783  1.00 73.38  ? 3    LYS F N   1 
ATOM   14749 C  CA  . LYS D  2 3   ? 16.755  7.440   59.220  1.00 80.39  ? 3    LYS F CA  1 
ATOM   14750 C  C   . LYS D  2 3   ? 15.692  6.483   59.721  1.00 83.90  ? 3    LYS F C   1 
ATOM   14751 O  O   . LYS D  2 3   ? 15.292  5.568   58.994  1.00 86.34  ? 3    LYS F O   1 
ATOM   14752 C  CB  . LYS D  2 3   ? 18.141  6.904   59.589  1.00 71.09  ? 3    LYS F CB  1 
ATOM   14753 C  CG  . LYS D  2 3   ? 18.494  7.179   61.035  1.00 70.50  ? 3    LYS F CG  1 
ATOM   14754 C  CD  . LYS D  2 3   ? 19.044  5.976   61.730  1.00 70.36  ? 3    LYS F CD  1 
ATOM   14755 C  CE  . LYS D  2 3   ? 18.166  5.721   62.915  1.00 72.22  ? 3    LYS F CE  1 
ATOM   14756 N  NZ  . LYS D  2 3   ? 17.572  7.022   63.352  1.00 68.78  ? 3    LYS F NZ  1 
ATOM   14757 N  N   . HIS D  2 4   ? 15.238  6.685   60.961  1.00 82.44  ? 4    HIS F N   1 
ATOM   14758 C  CA  . HIS D  2 4   ? 13.966  6.133   61.419  1.00 84.83  ? 4    HIS F CA  1 
ATOM   14759 C  C   . HIS D  2 4   ? 12.875  6.425   60.375  1.00 81.77  ? 4    HIS F C   1 
ATOM   14760 O  O   . HIS D  2 4   ? 11.876  7.097   60.642  1.00 78.10  ? 4    HIS F O   1 
ATOM   14761 C  CB  . HIS D  2 4   ? 13.594  6.686   62.805  1.00 78.80  ? 4    HIS F CB  1 
ATOM   14762 C  CG  . HIS D  2 4   ? 14.038  5.808   63.940  1.00 88.90  ? 4    HIS F CG  1 
ATOM   14763 N  ND1 . HIS D  2 4   ? 15.356  5.453   64.132  1.00 80.60  ? 4    HIS F ND1 1 
ATOM   14764 C  CD2 . HIS D  2 4   ? 13.336  5.193   64.925  1.00 81.67  ? 4    HIS F CD2 1 
ATOM   14765 C  CE1 . HIS D  2 4   ? 15.451  4.665   65.189  1.00 77.64  ? 4    HIS F CE1 1 
ATOM   14766 N  NE2 . HIS D  2 4   ? 14.239  4.490   65.687  1.00 76.77  ? 4    HIS F NE2 1 
ATOM   14767 N  N   . HIS D  2 5   ? 13.133  5.907   59.175  1.00 82.71  ? 5    HIS F N   1 
ATOM   14768 C  CA  . HIS D  2 5   ? 12.212  5.789   58.069  1.00 82.66  ? 5    HIS F CA  1 
ATOM   14769 C  C   . HIS D  2 5   ? 11.505  4.452   58.295  1.00 85.47  ? 5    HIS F C   1 
ATOM   14770 O  O   . HIS D  2 5   ? 11.374  3.631   57.385  1.00 84.67  ? 5    HIS F O   1 
ATOM   14771 C  CB  . HIS D  2 5   ? 12.979  5.853   56.736  1.00 73.77  ? 5    HIS F CB  1 
ATOM   14772 C  CG  . HIS D  2 5   ? 12.112  5.723   55.524  1.00 72.59  ? 5    HIS F CG  1 
ATOM   14773 N  ND1 . HIS D  2 5   ? 11.170  6.666   55.176  1.00 71.96  ? 5    HIS F ND1 1 
ATOM   14774 C  CD2 . HIS D  2 5   ? 12.043  4.754   54.580  1.00 73.41  ? 5    HIS F CD2 1 
ATOM   14775 C  CE1 . HIS D  2 5   ? 10.555  6.283   54.071  1.00 74.23  ? 5    HIS F CE1 1 
ATOM   14776 N  NE2 . HIS D  2 5   ? 11.064  5.125   53.690  1.00 79.16  ? 5    HIS F NE2 1 
ATOM   14777 N  N   . ALA D  2 6   ? 11.074  4.250   59.546  1.00 91.48  ? 6    ALA F N   1 
ATOM   14778 C  CA  . ALA D  2 6   ? 10.456  3.008   60.012  1.00 98.49  ? 6    ALA F CA  1 
ATOM   14779 C  C   . ALA D  2 6   ? 9.002   2.913   59.547  1.00 101.61 ? 6    ALA F C   1 
ATOM   14780 O  O   . ALA D  2 6   ? 8.243   2.046   59.992  1.00 102.70 ? 6    ALA F O   1 
ATOM   14781 C  CB  . ALA D  2 6   ? 10.546  2.902   61.539  1.00 94.23  ? 6    ALA F CB  1 
ATOM   14782 N  N   . PHE D  2 7   ? 8.625   3.830   58.659  1.00 95.20  ? 7    PHE F N   1 
ATOM   14783 C  CA  . PHE D  2 7   ? 7.397   3.710   57.888  1.00 93.53  ? 7    PHE F CA  1 
ATOM   14784 C  C   . PHE D  2 7   ? 7.750   3.113   56.513  1.00 100.33 ? 7    PHE F C   1 
ATOM   14785 O  O   . PHE D  2 7   ? 6.935   3.111   55.582  1.00 99.96  ? 7    PHE F O   1 
ATOM   14786 C  CB  . PHE D  2 7   ? 6.697   5.071   57.760  1.00 84.69  ? 7    PHE F CB  1 
ATOM   14787 C  CG  . PHE D  2 7   ? 5.408   5.023   56.979  1.00 87.83  ? 7    PHE F CG  1 
ATOM   14788 C  CD1 . PHE D  2 7   ? 4.264   4.455   57.532  1.00 91.22  ? 7    PHE F CD1 1 
ATOM   14789 C  CD2 . PHE D  2 7   ? 5.343   5.540   55.688  1.00 84.39  ? 7    PHE F CD2 1 
ATOM   14790 C  CE1 . PHE D  2 7   ? 3.080   4.400   56.814  1.00 88.89  ? 7    PHE F CE1 1 
ATOM   14791 C  CE2 . PHE D  2 7   ? 4.168   5.491   54.962  1.00 86.50  ? 7    PHE F CE2 1 
ATOM   14792 C  CZ  . PHE D  2 7   ? 3.031   4.920   55.525  1.00 87.67  ? 7    PHE F CZ  1 
ATOM   14793 N  N   . SER D  2 8   ? 8.983   2.610   56.406  1.00 97.74  ? 8    SER F N   1 
ATOM   14794 C  CA  . SER D  2 8   ? 9.431   1.830   55.251  1.00 94.36  ? 8    SER F CA  1 
ATOM   14795 C  C   . SER D  2 8   ? 8.340   0.862   54.794  1.00 96.56  ? 8    SER F C   1 
ATOM   14796 O  O   . SER D  2 8   ? 7.746   1.037   53.725  1.00 96.89  ? 8    SER F O   1 
ATOM   14797 C  CB  . SER D  2 8   ? 10.702  1.053   55.594  1.00 92.72  ? 8    SER F CB  1 
ATOM   14798 O  OG  . SER D  2 8   ? 10.441  0.087   56.598  1.00 90.83  ? 8    SER F OG  1 
ATOM   14799 N  N   . PHE D  2 9   ? 8.092   -0.152  55.620  1.00 96.38  ? 9    PHE F N   1 
ATOM   14800 C  CA  . PHE D  2 9   ? 6.922   -1.019  55.489  1.00 101.96 ? 9    PHE F CA  1 
ATOM   14801 C  C   . PHE D  2 9   ? 6.385   -1.320  56.898  1.00 106.52 ? 9    PHE F C   1 
ATOM   14802 O  O   . PHE D  2 9   ? 6.953   -0.858  57.894  1.00 102.09 ? 9    PHE F O   1 
ATOM   14803 C  CB  . PHE D  2 9   ? 7.249   -2.328  54.741  1.00 93.96  ? 9    PHE F CB  1 
ATOM   14804 C  CG  . PHE D  2 9   ? 7.722   -2.128  53.311  1.00 94.28  ? 9    PHE F CG  1 
ATOM   14805 C  CD1 . PHE D  2 9   ? 6.936   -1.466  52.382  1.00 85.94  ? 9    PHE F CD1 1 
ATOM   14806 C  CD2 . PHE D  2 9   ? 8.954   -2.619  52.897  1.00 88.25  ? 9    PHE F CD2 1 
ATOM   14807 C  CE1 . PHE D  2 9   ? 7.382   -1.280  51.078  1.00 85.45  ? 9    PHE F CE1 1 
ATOM   14808 C  CE2 . PHE D  2 9   ? 9.397   -2.437  51.588  1.00 79.75  ? 9    PHE F CE2 1 
ATOM   14809 C  CZ  . PHE D  2 9   ? 8.613   -1.773  50.682  1.00 76.17  ? 9    PHE F CZ  1 
HETATM 14810 N  N   . LYN D  2 10  ? 5.288   -2.078  56.971  1.00 122.18 ? 10   LYN F N   1 
HETATM 14811 C  CA  . LYN D  2 10  ? 4.652   -2.487  58.271  1.00 105.31 ? 10   LYN F CA  1 
HETATM 14812 C  CB  . LYN D  2 10  ? 3.796   -1.364  58.853  1.00 102.96 ? 10   LYN F CB  1 
HETATM 14813 C  CG  . LYN D  2 10  ? 3.188   -1.678  60.220  1.00 91.90  ? 10   LYN F CG  1 
HETATM 14814 C  CD  . LYN D  2 10  ? 2.376   -0.470  60.701  1.00 91.97  ? 10   LYN F CD  1 
HETATM 14815 C  CE  . LYN D  2 10  ? 1.723   -0.721  62.064  1.00 87.12  ? 10   LYN F CE  1 
HETATM 14816 N  NZ  . LYN D  2 10  ? 1.369   0.602   62.666  1.00 87.63  ? 10   LYN F NZ  1 
HETATM 14817 C  C   . LYN D  2 10  ? 3.796   -3.694  58.032  1.00 104.49 ? 10   LYN F C   1 
HETATM 14818 O  O   . LYN D  2 10  ? 3.678   -4.548  58.900  1.00 106.41 ? 10   LYN F O   1 
HETATM 14819 N  NT  . LYN D  2 10  ? 3.125   -3.823  56.781  1.00 102.04 ? 10   LYN F NT  1 
HETATM 14820 ZN ZN  . ZN  E  3 .   ? 21.058  4.698   -0.763  1.00 23.80  ? 1008 ZN  A ZN  1 
HETATM 14821 C  C1  . NAG F  4 .   ? -9.524  14.225  -18.453 1.00 93.04  ? 1069 NAG A C1  1 
HETATM 14822 C  C2  . NAG F  4 .   ? -8.285  14.274  -19.359 1.00 99.15  ? 1069 NAG A C2  1 
HETATM 14823 C  C3  . NAG F  4 .   ? -8.350  13.152  -20.394 1.00 98.18  ? 1069 NAG A C3  1 
HETATM 14824 C  C4  . NAG F  4 .   ? -8.571  11.818  -19.695 1.00 99.59  ? 1069 NAG A C4  1 
HETATM 14825 C  C5  . NAG F  4 .   ? -9.941  11.825  -19.013 1.00 101.44 ? 1069 NAG A C5  1 
HETATM 14826 C  C6  . NAG F  4 .   ? -9.966  11.226  -17.620 1.00 88.53  ? 1069 NAG A C6  1 
HETATM 14827 C  C7  . NAG F  4 .   ? -7.807  16.687  -19.347 1.00 98.63  ? 1069 NAG A C7  1 
HETATM 14828 C  C8  . NAG F  4 .   ? -7.747  17.944  -20.165 1.00 92.45  ? 1069 NAG A C8  1 
HETATM 14829 N  N2  . NAG F  4 .   ? -8.166  15.571  -20.003 1.00 99.63  ? 1069 NAG A N2  1 
HETATM 14830 O  O3  . NAG F  4 .   ? -7.156  13.129  -21.172 1.00 98.02  ? 1069 NAG A O3  1 
HETATM 14831 O  O4  . NAG F  4 .   ? -8.504  10.749  -20.636 1.00 90.63  ? 1069 NAG A O4  1 
HETATM 14832 O  O5  . NAG F  4 .   ? -10.455 13.169  -18.919 1.00 99.63  ? 1069 NAG A O5  1 
HETATM 14833 O  O6  . NAG F  4 .   ? -8.724  11.350  -16.942 1.00 84.05  ? 1069 NAG A O6  1 
HETATM 14834 O  O7  . NAG F  4 .   ? -7.536  16.678  -18.147 1.00 91.33  ? 1069 NAG A O7  1 
HETATM 14835 C  C1  . NAG G  4 .   ? 12.895  -20.809 -11.590 1.00 84.06  ? 1070 NAG A C1  1 
HETATM 14836 C  C2  . NAG G  4 .   ? 11.862  -21.928 -11.356 1.00 85.18  ? 1070 NAG A C2  1 
HETATM 14837 C  C3  . NAG G  4 .   ? 10.655  -21.743 -12.270 1.00 86.53  ? 1070 NAG A C3  1 
HETATM 14838 C  C4  . NAG G  4 .   ? 10.072  -20.347 -12.110 1.00 91.49  ? 1070 NAG A C4  1 
HETATM 14839 C  C5  . NAG G  4 .   ? 11.155  -19.303 -12.374 1.00 80.41  ? 1070 NAG A C5  1 
HETATM 14840 C  C6  . NAG G  4 .   ? 10.681  -17.885 -12.148 1.00 83.04  ? 1070 NAG A C6  1 
HETATM 14841 C  C7  . NAG G  4 .   ? 13.112  -23.919 -10.622 1.00 88.22  ? 1070 NAG A C7  1 
HETATM 14842 C  C8  . NAG G  4 .   ? 13.654  -25.257 -11.033 1.00 81.33  ? 1070 NAG A C8  1 
HETATM 14843 N  N2  . NAG G  4 .   ? 12.457  -23.238 -11.569 1.00 89.78  ? 1070 NAG A N2  1 
HETATM 14844 O  O3  . NAG G  4 .   ? 9.671   -22.717 -11.943 1.00 97.80  ? 1070 NAG A O3  1 
HETATM 14845 O  O4  . NAG G  4 .   ? 8.991   -20.178 -13.021 1.00 96.96  ? 1070 NAG A O4  1 
HETATM 14846 O  O5  . NAG G  4 .   ? 12.253  -19.514 -11.474 1.00 76.46  ? 1070 NAG A O5  1 
HETATM 14847 O  O6  . NAG G  4 .   ? 11.300  -16.971 -13.045 1.00 72.50  ? 1070 NAG A O6  1 
HETATM 14848 O  O7  . NAG G  4 .   ? 13.268  -23.473 -9.489  1.00 86.64  ? 1070 NAG A O7  1 
HETATM 14849 C  C1  . NAG H  4 .   ? 4.702   19.971  26.600  1.00 51.36  ? 1071 NAG A C1  1 
HETATM 14850 C  C2  . NAG H  4 .   ? 4.906   21.452  26.360  1.00 49.17  ? 1071 NAG A C2  1 
HETATM 14851 C  C3  . NAG H  4 .   ? 5.352   22.165  27.647  1.00 58.19  ? 1071 NAG A C3  1 
HETATM 14852 C  C4  . NAG H  4 .   ? 4.462   21.800  28.831  1.00 65.80  ? 1071 NAG A C4  1 
HETATM 14853 C  C5  . NAG H  4 .   ? 4.270   20.285  28.902  1.00 59.57  ? 1071 NAG A C5  1 
HETATM 14854 C  C6  . NAG H  4 .   ? 3.277   19.864  29.956  1.00 59.66  ? 1071 NAG A C6  1 
HETATM 14855 C  C7  . NAG H  4 .   ? 5.547   21.919  24.039  1.00 47.85  ? 1071 NAG A C7  1 
HETATM 14856 C  C8  . NAG H  4 .   ? 6.689   22.160  23.103  1.00 48.70  ? 1071 NAG A C8  1 
HETATM 14857 N  N2  . NAG H  4 .   ? 5.880   21.664  25.307  1.00 50.69  ? 1071 NAG A N2  1 
HETATM 14858 O  O3  . NAG H  4 .   ? 5.345   23.580  27.455  1.00 52.54  ? 1071 NAG A O3  1 
HETATM 14859 O  O4  . NAG H  4 .   ? 5.114   22.222  30.026  1.00 76.81  ? 1071 NAG A O4  1 
HETATM 14860 O  O5  . NAG H  4 .   ? 3.783   19.786  27.646  1.00 63.20  ? 1071 NAG A O5  1 
HETATM 14861 O  O6  . NAG H  4 .   ? 3.895   19.012  30.909  1.00 76.49  ? 1071 NAG A O6  1 
HETATM 14862 O  O7  . NAG H  4 .   ? 4.378   21.950  23.666  1.00 44.85  ? 1071 NAG A O7  1 
HETATM 14863 C  C1  . NAG I  4 .   ? 4.384   23.109  30.904  1.00 75.06  ? 1072 NAG A C1  1 
HETATM 14864 C  C2  . NAG I  4 .   ? 5.257   23.234  32.148  1.00 78.49  ? 1072 NAG A C2  1 
HETATM 14865 C  C3  . NAG I  4 .   ? 4.643   24.217  33.144  1.00 81.03  ? 1072 NAG A C3  1 
HETATM 14866 C  C4  . NAG I  4 .   ? 4.309   25.539  32.468  1.00 82.14  ? 1072 NAG A C4  1 
HETATM 14867 C  C5  . NAG I  4 .   ? 3.505   25.307  31.191  1.00 85.51  ? 1072 NAG A C5  1 
HETATM 14868 C  C6  . NAG I  4 .   ? 3.317   26.571  30.385  1.00 88.15  ? 1072 NAG A C6  1 
HETATM 14869 C  C7  . NAG I  4 .   ? 6.682   21.502  33.133  1.00 77.77  ? 1072 NAG A C7  1 
HETATM 14870 C  C8  . NAG I  4 .   ? 6.734   20.148  33.766  1.00 73.36  ? 1072 NAG A C8  1 
HETATM 14871 N  N2  . NAG I  4 .   ? 5.469   21.938  32.773  1.00 69.86  ? 1072 NAG A N2  1 
HETATM 14872 O  O3  . NAG I  4 .   ? 5.582   24.452  34.187  1.00 82.20  ? 1072 NAG A O3  1 
HETATM 14873 O  O4  . NAG I  4 .   ? 3.557   26.359  33.359  1.00 85.53  ? 1072 NAG A O4  1 
HETATM 14874 O  O5  . NAG I  4 .   ? 4.190   24.381  30.335  1.00 82.27  ? 1072 NAG A O5  1 
HETATM 14875 O  O6  . NAG I  4 .   ? 4.568   27.160  30.057  1.00 88.84  ? 1072 NAG A O6  1 
HETATM 14876 O  O7  . NAG I  4 .   ? 7.692   22.175  32.957  1.00 83.12  ? 1072 NAG A O7  1 
HETATM 14877 C  C1  . NAG J  4 .   ? 9.090   25.147  -5.713  1.00 37.14  ? 1073 NAG A C1  1 
HETATM 14878 C  C2  . NAG J  4 .   ? 9.093   26.694  -5.679  1.00 37.14  ? 1073 NAG A C2  1 
HETATM 14879 C  C3  . NAG J  4 .   ? 9.631   27.277  -6.986  1.00 47.01  ? 1073 NAG A C3  1 
HETATM 14880 C  C4  . NAG J  4 .   ? 10.962  26.647  -7.362  1.00 45.19  ? 1073 NAG A C4  1 
HETATM 14881 C  C5  . NAG J  4 .   ? 10.844  25.129  -7.362  1.00 39.32  ? 1073 NAG A C5  1 
HETATM 14882 C  C6  . NAG J  4 .   ? 12.176  24.455  -7.605  1.00 37.47  ? 1073 NAG A C6  1 
HETATM 14883 C  C7  . NAG J  4 .   ? 7.422   27.702  -4.215  1.00 37.43  ? 1073 NAG A C7  1 
HETATM 14884 C  C8  . NAG J  4 .   ? 6.004   28.148  -4.057  1.00 36.10  ? 1073 NAG A C8  1 
HETATM 14885 N  N2  . NAG J  4 .   ? 7.758   27.197  -5.404  1.00 33.71  ? 1073 NAG A N2  1 
HETATM 14886 O  O3  . NAG J  4 .   ? 9.815   28.683  -6.845  1.00 48.33  ? 1073 NAG A O3  1 
HETATM 14887 O  O4  . NAG J  4 .   ? 11.308  27.059  -8.679  1.00 55.04  ? 1073 NAG A O4  1 
HETATM 14888 O  O5  . NAG J  4 .   ? 10.375  24.672  -6.085  1.00 37.35  ? 1073 NAG A O5  1 
HETATM 14889 O  O6  . NAG J  4 .   ? 12.019  23.069  -7.885  1.00 42.54  ? 1073 NAG A O6  1 
HETATM 14890 O  O7  . NAG J  4 .   ? 8.231   27.806  -3.315  1.00 44.39  ? 1073 NAG A O7  1 
HETATM 14891 C  C1  . NAG K  4 .   ? 12.332  28.060  -8.663  1.00 55.75  ? 1074 NAG A C1  1 
HETATM 14892 C  C2  . NAG K  4 .   ? 12.972  28.092  -10.045 1.00 60.79  ? 1074 NAG A C2  1 
HETATM 14893 C  C3  . NAG K  4 .   ? 14.030  29.193  -10.116 1.00 68.56  ? 1074 NAG A C3  1 
HETATM 14894 C  C4  . NAG K  4 .   ? 13.470  30.526  -9.636  1.00 67.22  ? 1074 NAG A C4  1 
HETATM 14895 C  C5  . NAG K  4 .   ? 12.751  30.362  -8.298  1.00 61.98  ? 1074 NAG A C5  1 
HETATM 14896 C  C6  . NAG K  4 .   ? 11.998  31.602  -7.880  1.00 61.90  ? 1074 NAG A C6  1 
HETATM 14897 C  C7  . NAG K  4 .   ? 12.912  25.889  -11.104 1.00 58.21  ? 1074 NAG A C7  1 
HETATM 14898 C  C8  . NAG K  4 .   ? 13.662  24.625  -11.380 1.00 52.59  ? 1074 NAG A C8  1 
HETATM 14899 N  N2  . NAG K  4 .   ? 13.557  26.806  -10.383 1.00 55.76  ? 1074 NAG A N2  1 
HETATM 14900 O  O3  . NAG K  4 .   ? 14.510  29.317  -11.451 1.00 70.73  ? 1074 NAG A O3  1 
HETATM 14901 O  O4  . NAG K  4 .   ? 14.561  31.418  -9.442  1.00 88.33  ? 1074 NAG A O4  1 
HETATM 14902 O  O5  . NAG K  4 .   ? 11.780  29.308  -8.376  1.00 59.18  ? 1074 NAG A O5  1 
HETATM 14903 O  O6  . NAG K  4 .   ? 10.883  31.827  -8.733  1.00 67.45  ? 1074 NAG A O6  1 
HETATM 14904 O  O7  . NAG K  4 .   ? 11.768  26.071  -11.507 1.00 65.35  ? 1074 NAG A O7  1 
HETATM 14905 C  C1  . BMA L  5 .   ? 14.553  32.598  -10.283 1.00 89.67  ? 1075 BMA A C1  1 
HETATM 14906 C  C2  . BMA L  5 .   ? 15.328  33.682  -9.497  1.00 95.18  ? 1075 BMA A C2  1 
HETATM 14907 C  C3  . BMA L  5 .   ? 15.495  34.934  -10.333 1.00 100.78 ? 1075 BMA A C3  1 
HETATM 14908 C  C4  . BMA L  5 .   ? 16.192  34.572  -11.648 1.00 98.20  ? 1075 BMA A C4  1 
HETATM 14909 C  C5  . BMA L  5 .   ? 15.344  33.526  -12.411 1.00 95.19  ? 1075 BMA A C5  1 
HETATM 14910 C  C6  . BMA L  5 .   ? 16.026  33.016  -13.673 1.00 99.45  ? 1075 BMA A C6  1 
HETATM 14911 O  O2  . BMA L  5 .   ? 16.672  33.246  -9.228  1.00 94.73  ? 1075 BMA A O2  1 
HETATM 14912 O  O3  . BMA L  5 .   ? 16.220  35.959  -9.630  1.00 97.53  ? 1075 BMA A O3  1 
HETATM 14913 O  O4  . BMA L  5 .   ? 16.348  35.739  -12.438 1.00 102.39 ? 1075 BMA A O4  1 
HETATM 14914 O  O5  . BMA L  5 .   ? 15.097  32.365  -11.567 1.00 87.11  ? 1075 BMA A O5  1 
HETATM 14915 O  O6  . BMA L  5 .   ? 16.541  31.703  -13.405 1.00 98.23  ? 1075 BMA A O6  1 
HETATM 14916 C  C1  . NAG M  4 .   ? 40.531  6.455   -9.564  1.00 58.04  ? 1076 NAG A C1  1 
HETATM 14917 C  C2  . NAG M  4 .   ? 39.884  6.093   -10.901 1.00 63.83  ? 1076 NAG A C2  1 
HETATM 14918 C  C3  . NAG M  4 .   ? 40.931  6.046   -12.007 1.00 71.85  ? 1076 NAG A C3  1 
HETATM 14919 C  C4  . NAG M  4 .   ? 41.706  7.353   -12.083 1.00 81.42  ? 1076 NAG A C4  1 
HETATM 14920 C  C5  . NAG M  4 .   ? 42.323  7.622   -10.706 1.00 73.62  ? 1076 NAG A C5  1 
HETATM 14921 C  C6  . NAG M  4 .   ? 43.041  8.946   -10.590 1.00 74.38  ? 1076 NAG A C6  1 
HETATM 14922 C  C7  . NAG M  4 .   ? 37.885  4.677   -11.061 1.00 58.74  ? 1076 NAG A C7  1 
HETATM 14923 C  C8  . NAG M  4 .   ? 37.338  3.288   -10.941 1.00 58.55  ? 1076 NAG A C8  1 
HETATM 14924 N  N2  . NAG M  4 .   ? 39.191  4.818   -10.816 1.00 55.83  ? 1076 NAG A N2  1 
HETATM 14925 O  O3  . NAG M  4 .   ? 40.309  5.767   -13.255 1.00 74.12  ? 1076 NAG A O3  1 
HETATM 14926 O  O4  . NAG M  4 .   ? 42.671  7.169   -13.121 1.00 96.31  ? 1076 NAG A O4  1 
HETATM 14927 O  O5  . NAG M  4 .   ? 41.290  7.649   -9.705  1.00 68.14  ? 1076 NAG A O5  1 
HETATM 14928 O  O6  . NAG M  4 .   ? 43.018  9.406   -9.246  1.00 77.82  ? 1076 NAG A O6  1 
HETATM 14929 O  O7  . NAG M  4 .   ? 37.173  5.631   -11.354 1.00 67.35  ? 1076 NAG A O7  1 
HETATM 14930 C  C1  . NAG N  4 .   ? 43.294  8.293   -13.801 1.00 95.35  ? 1077 NAG A C1  1 
HETATM 14931 C  C2  . NAG N  4 .   ? 44.649  7.792   -14.316 1.00 99.14  ? 1077 NAG A C2  1 
HETATM 14932 C  C3  . NAG N  4 .   ? 44.826  8.137   -15.787 1.00 110.65 ? 1077 NAG A C3  1 
HETATM 14933 C  C4  . NAG N  4 .   ? 43.626  7.645   -16.582 1.00 110.96 ? 1077 NAG A C4  1 
HETATM 14934 C  C5  . NAG N  4 .   ? 42.381  8.418   -16.152 1.00 104.84 ? 1077 NAG A C5  1 
HETATM 14935 C  C6  . NAG N  4 .   ? 41.148  7.555   -16.024 1.00 94.90  ? 1077 NAG A C6  1 
HETATM 14936 C  C7  . NAG N  4 .   ? 46.392  7.600   -12.609 1.00 93.76  ? 1077 NAG A C7  1 
HETATM 14937 C  C8  . NAG N  4 .   ? 47.511  8.294   -11.893 1.00 103.51 ? 1077 NAG A C8  1 
HETATM 14938 N  N2  . NAG N  4 .   ? 45.748  8.323   -13.530 1.00 95.54  ? 1077 NAG A N2  1 
HETATM 14939 O  O3  . NAG N  4 .   ? 46.014  7.515   -16.266 1.00 117.68 ? 1077 NAG A O3  1 
HETATM 14940 O  O4  . NAG N  4 .   ? 43.854  7.686   -17.994 1.00 117.72 ? 1077 NAG A O4  1 
HETATM 14941 O  O5  . NAG N  4 .   ? 42.587  9.059   -14.877 1.00 99.87  ? 1077 NAG A O5  1 
HETATM 14942 O  O6  . NAG N  4 .   ? 40.012  8.219   -16.562 1.00 87.44  ? 1077 NAG A O6  1 
HETATM 14943 O  O7  . NAG N  4 .   ? 46.083  6.439   -12.365 1.00 89.96  ? 1077 NAG A O7  1 
HETATM 14944 C  C1  . BMA O  5 .   ? 44.119  8.953   -18.672 1.00 117.26 ? 1078 BMA A C1  1 
HETATM 14945 C  C2  . BMA O  5 .   ? 45.680  9.230   -18.942 1.00 117.38 ? 1078 BMA A C2  1 
HETATM 14946 C  C3  . BMA O  5 .   ? 46.031  9.280   -20.408 1.00 121.34 ? 1078 BMA A C3  1 
HETATM 14947 C  C4  . BMA O  5 .   ? 45.158  8.311   -21.169 1.00 121.35 ? 1078 BMA A C4  1 
HETATM 14948 C  C5  . BMA O  5 .   ? 43.779  8.937   -21.210 1.00 123.03 ? 1078 BMA A C5  1 
HETATM 14949 C  C6  . BMA O  5 .   ? 42.781  8.123   -22.027 1.00 116.93 ? 1078 BMA A C6  1 
HETATM 14950 O  O2  . BMA O  5 .   ? 46.508  8.175   -18.448 1.00 119.96 ? 1078 BMA A O2  1 
HETATM 14951 O  O3  . BMA O  5 .   ? 47.409  8.987   -20.613 1.00 125.94 ? 1078 BMA A O3  1 
HETATM 14952 O  O4  . BMA O  5 .   ? 45.642  8.131   -22.496 1.00 121.45 ? 1078 BMA A O4  1 
HETATM 14953 O  O5  . BMA O  5 .   ? 43.247  9.129   -19.828 1.00 118.04 ? 1078 BMA A O5  1 
HETATM 14954 O  O6  . BMA O  5 .   ? 42.325  7.047   -21.225 1.00 118.55 ? 1078 BMA A O6  1 
HETATM 14955 C  C1  . NAG P  4 .   ? 58.707  -12.488 -13.821 1.00 99.07  ? 1079 NAG A C1  1 
HETATM 14956 C  C2  . NAG P  4 .   ? 58.667  -11.035 -14.212 1.00 99.76  ? 1079 NAG A C2  1 
HETATM 14957 C  C3  . NAG P  4 .   ? 59.957  -10.310 -13.775 1.00 101.96 ? 1079 NAG A C3  1 
HETATM 14958 C  C4  . NAG P  4 .   ? 61.082  -11.248 -13.302 1.00 109.83 ? 1079 NAG A C4  1 
HETATM 14959 C  C5  . NAG P  4 .   ? 60.606  -12.530 -12.607 1.00 104.16 ? 1079 NAG A C5  1 
HETATM 14960 C  C6  . NAG P  4 .   ? 61.103  -12.712 -11.192 1.00 102.06 ? 1079 NAG A C6  1 
HETATM 14961 C  C7  . NAG P  4 .   ? 58.399  -9.729  -16.300 1.00 111.70 ? 1079 NAG A C7  1 
HETATM 14962 C  C8  . NAG P  4 .   ? 58.098  -9.814  -17.776 1.00 107.54 ? 1079 NAG A C8  1 
HETATM 14963 N  N2  . NAG P  4 .   ? 58.441  -10.889 -15.645 1.00 105.30 ? 1079 NAG A N2  1 
HETATM 14964 O  O3  . NAG P  4 .   ? 59.670  -9.326  -12.795 1.00 101.54 ? 1079 NAG A O3  1 
HETATM 14965 O  O4  . NAG P  4 .   ? 61.869  -11.632 -14.418 1.00 118.28 ? 1079 NAG A O4  1 
HETATM 14966 O  O5  . NAG P  4 .   ? 59.182  -12.605 -12.568 1.00 99.63  ? 1079 NAG A O5  1 
HETATM 14967 O  O6  . NAG P  4 .   ? 60.793  -14.028 -10.748 1.00 89.28  ? 1079 NAG A O6  1 
HETATM 14968 O  O7  . NAG P  4 .   ? 58.599  -8.647  -15.748 1.00 110.82 ? 1079 NAG A O7  1 
HETATM 14969 C  C1  . NAG Q  4 .   ? 62.904  -10.693 -14.789 1.00 117.46 ? 1080 NAG A C1  1 
HETATM 14970 C  C2  . NAG Q  4 .   ? 62.538  -9.962  -16.082 1.00 116.64 ? 1080 NAG A C2  1 
HETATM 14971 C  C3  . NAG Q  4 .   ? 63.730  -9.150  -16.584 1.00 116.07 ? 1080 NAG A C3  1 
HETATM 14972 C  C4  . NAG Q  4 .   ? 64.308  -8.274  -15.479 1.00 120.31 ? 1080 NAG A C4  1 
HETATM 14973 C  C5  . NAG Q  4 .   ? 64.548  -9.080  -14.202 1.00 121.26 ? 1080 NAG A C5  1 
HETATM 14974 C  C6  . NAG Q  4 .   ? 64.985  -8.223  -13.034 1.00 122.30 ? 1080 NAG A C6  1 
HETATM 14975 C  C7  . NAG Q  4 .   ? 61.354  -10.555 -18.156 1.00 116.05 ? 1080 NAG A C7  1 
HETATM 14976 C  C8  . NAG Q  4 .   ? 60.969  -11.665 -19.088 1.00 105.62 ? 1080 NAG A C8  1 
HETATM 14977 N  N2  . NAG Q  4 .   ? 62.095  -10.906 -17.096 1.00 119.95 ? 1080 NAG A N2  1 
HETATM 14978 O  O3  . NAG Q  4 .   ? 63.303  -8.317  -17.655 1.00 114.53 ? 1080 NAG A O3  1 
HETATM 14979 O  O4  . NAG Q  4 .   ? 65.542  -7.707  -15.909 1.00 119.74 ? 1080 NAG A O4  1 
HETATM 14980 O  O5  . NAG Q  4 .   ? 63.340  -9.750  -13.807 1.00 120.22 ? 1080 NAG A O5  1 
HETATM 14981 O  O6  . NAG Q  4 .   ? 64.382  -8.642  -11.816 1.00 121.89 ? 1080 NAG A O6  1 
HETATM 14982 O  O7  . NAG Q  4 .   ? 61.021  -9.389  -18.361 1.00 112.62 ? 1080 NAG A O7  1 
HETATM 14983 C  C1  . NAG R  4 .   ? -11.500 22.861  13.367  1.00 98.32  ? 1081 NAG A C1  1 
HETATM 14984 C  C2  . NAG R  4 .   ? -12.571 22.422  14.371  1.00 103.84 ? 1081 NAG A C2  1 
HETATM 14985 C  C3  . NAG R  4 .   ? -13.110 23.633  15.133  1.00 108.49 ? 1081 NAG A C3  1 
HETATM 14986 C  C4  . NAG R  4 .   ? -11.970 24.369  15.821  1.00 105.72 ? 1081 NAG A C4  1 
HETATM 14987 C  C5  . NAG R  4 .   ? -10.926 24.789  14.790  1.00 103.34 ? 1081 NAG A C5  1 
HETATM 14988 C  C6  . NAG R  4 .   ? -9.702  25.409  15.425  1.00 97.48  ? 1081 NAG A C6  1 
HETATM 14989 C  C7  . NAG R  4 .   ? -13.825 20.381  13.817  1.00 97.30  ? 1081 NAG A C7  1 
HETATM 14990 C  C8  . NAG R  4 .   ? -14.997 19.807  13.075  1.00 88.52  ? 1081 NAG A C8  1 
HETATM 14991 N  N2  . NAG R  4 .   ? -13.655 21.705  13.713  1.00 104.44 ? 1081 NAG A N2  1 
HETATM 14992 O  O3  . NAG R  4 .   ? -14.067 23.213  16.100  1.00 112.64 ? 1081 NAG A O3  1 
HETATM 14993 O  O4  . NAG R  4 .   ? -12.463 25.521  16.498  1.00 106.31 ? 1081 NAG A O4  1 
HETATM 14994 O  O5  . NAG R  4 .   ? -10.471 23.642  14.053  1.00 98.13  ? 1081 NAG A O5  1 
HETATM 14995 O  O6  . NAG R  4 .   ? -8.906  26.094  14.470  1.00 103.85 ? 1081 NAG A O6  1 
HETATM 14996 O  O7  . NAG R  4 .   ? -13.066 19.679  14.477  1.00 96.01  ? 1081 NAG A O7  1 
HETATM 14997 C  C1  . NAG S  4 .   ? 28.876  -31.944 17.449  1.00 95.84  ? 1082 NAG A C1  1 
HETATM 14998 C  C2  . NAG S  4 .   ? 29.340  -32.384 18.841  1.00 96.50  ? 1082 NAG A C2  1 
HETATM 14999 C  C3  . NAG S  4 .   ? 28.305  -31.966 19.890  1.00 105.46 ? 1082 NAG A C3  1 
HETATM 15000 C  C4  . NAG S  4 .   ? 28.018  -30.471 19.791  1.00 106.91 ? 1082 NAG A C4  1 
HETATM 15001 C  C5  . NAG S  4 .   ? 27.632  -30.084 18.360  1.00 103.05 ? 1082 NAG A C5  1 
HETATM 15002 C  C6  . NAG S  4 .   ? 27.471  -28.585 18.176  1.00 99.05  ? 1082 NAG A C6  1 
HETATM 15003 C  C7  . NAG S  4 .   ? 30.769  -34.394 18.723  1.00 96.96  ? 1082 NAG A C7  1 
HETATM 15004 C  C8  . NAG S  4 .   ? 30.804  -35.893 18.797  1.00 83.52  ? 1082 NAG A C8  1 
HETATM 15005 N  N2  . NAG S  4 .   ? 29.567  -33.822 18.886  1.00 100.85 ? 1082 NAG A N2  1 
HETATM 15006 O  O3  . NAG S  4 .   ? 28.765  -32.294 21.199  1.00 103.69 ? 1082 NAG A O3  1 
HETATM 15007 O  O4  . NAG S  4 .   ? 26.975  -30.111 20.693  1.00 104.08 ? 1082 NAG A O4  1 
HETATM 15008 O  O5  . NAG S  4 .   ? 28.650  -30.520 17.440  1.00 97.42  ? 1082 NAG A O5  1 
HETATM 15009 O  O6  . NAG S  4 .   ? 27.607  -28.161 16.824  1.00 86.20  ? 1082 NAG A O6  1 
HETATM 15010 O  O7  . NAG S  4 .   ? 31.783  -33.733 18.527  1.00 98.31  ? 1082 NAG A O7  1 
HETATM 15011 C  C1  . EDO T  6 .   ? 3.281   29.679  0.993   1.00 61.65  ? 1964 EDO A C1  1 
HETATM 15012 O  O1  . EDO T  6 .   ? 2.405   30.810  1.134   1.00 62.05  ? 1964 EDO A O1  1 
HETATM 15013 C  C2  . EDO T  6 .   ? 4.351   29.669  2.083   1.00 57.48  ? 1964 EDO A C2  1 
HETATM 15014 O  O2  . EDO T  6 .   ? 3.781   29.213  3.326   1.00 62.66  ? 1964 EDO A O2  1 
HETATM 15015 C  C1  . EDO U  6 .   ? 23.552  26.302  11.801  1.00 56.67  ? 1965 EDO A C1  1 
HETATM 15016 O  O1  . EDO U  6 .   ? 24.461  25.601  12.651  1.00 61.99  ? 1965 EDO A O1  1 
HETATM 15017 C  C2  . EDO U  6 .   ? 22.430  26.892  12.621  1.00 59.47  ? 1965 EDO A C2  1 
HETATM 15018 O  O2  . EDO U  6 .   ? 22.956  27.223  13.908  1.00 74.18  ? 1965 EDO A O2  1 
HETATM 15019 O  O1  . MES V  7 .   ? 19.751  25.718  -13.035 1.00 93.79  ? 2002 MES A O1  1 
HETATM 15020 C  C2  . MES V  7 .   ? 20.015  26.723  -14.027 1.00 98.63  ? 2002 MES A C2  1 
HETATM 15021 C  C3  . MES V  7 .   ? 19.151  27.976  -13.824 1.00 93.85  ? 2002 MES A C3  1 
HETATM 15022 N  N4  . MES V  7 .   ? 17.768  27.517  -13.681 1.00 100.38 ? 2002 MES A N4  1 
HETATM 15023 C  C5  . MES V  7 .   ? 17.485  26.501  -12.669 1.00 96.26  ? 2002 MES A C5  1 
HETATM 15024 C  C6  . MES V  7 .   ? 18.383  25.297  -12.968 1.00 87.47  ? 2002 MES A C6  1 
HETATM 15025 C  C7  . MES V  7 .   ? 16.687  28.400  -14.130 1.00 99.35  ? 2002 MES A C7  1 
HETATM 15026 C  C8  . MES V  7 .   ? 16.186  27.797  -15.450 1.00 106.63 ? 2002 MES A C8  1 
HETATM 15027 S  S   . MES V  7 .   ? 14.774  26.930  -15.277 1.00 140.26 ? 2002 MES A S   1 
HETATM 15028 O  O1S . MES V  7 .   ? 14.427  26.287  -16.573 1.00 123.41 ? 2002 MES A O1S 1 
HETATM 15029 O  O2S . MES V  7 .   ? 13.678  27.832  -14.851 1.00 89.92  ? 2002 MES A O2S 1 
HETATM 15030 O  O3S . MES V  7 .   ? 14.947  25.857  -14.269 1.00 111.09 ? 2002 MES A O3S 1 
HETATM 15031 C  C1  . BMA W  5 .   ? 32.514  25.665  24.266  1.00 67.78  ? 1001 BMA C C1  1 
HETATM 15032 C  C2  . BMA W  5 .   ? 33.676  25.002  23.721  1.00 64.16  ? 1001 BMA C C2  1 
HETATM 15033 C  C3  . BMA W  5 .   ? 34.632  25.982  23.240  1.00 76.59  ? 1001 BMA C C3  1 
HETATM 15034 C  C4  . BMA W  5 .   ? 33.981  26.869  22.150  1.00 73.55  ? 1001 BMA C C4  1 
HETATM 15035 C  C5  . BMA W  5 .   ? 32.639  27.471  22.634  1.00 71.33  ? 1001 BMA C C5  1 
HETATM 15036 C  C6  . BMA W  5 .   ? 31.780  27.986  21.488  1.00 70.16  ? 1001 BMA C C6  1 
HETATM 15037 O  O2  . BMA W  5 .   ? 33.251  24.330  22.548  1.00 70.80  ? 1001 BMA C O2  1 
HETATM 15038 O  O3  . BMA W  5 .   ? 35.764  25.281  22.717  1.00 85.40  ? 1001 BMA C O3  1 
HETATM 15039 O  O4  . BMA W  5 .   ? 34.875  27.891  21.678  1.00 84.94  ? 1001 BMA C O4  1 
HETATM 15040 O  O5  . BMA W  5 .   ? 31.849  26.423  23.286  1.00 68.94  ? 1001 BMA C O5  1 
HETATM 15041 O  O6  . BMA W  5 .   ? 30.636  27.080  21.319  1.00 71.36  ? 1001 BMA C O6  1 
HETATM 15042 C  C1  . BMA X  5 .   ? 35.728  28.459  22.695  1.00 88.25  ? 1002 BMA C C1  1 
HETATM 15043 C  C2  . BMA X  5 .   ? 37.203  27.976  22.554  1.00 88.65  ? 1002 BMA C C2  1 
HETATM 15044 C  C3  . BMA X  5 .   ? 37.945  28.489  23.741  1.00 91.89  ? 1002 BMA C C3  1 
HETATM 15045 C  C4  . BMA X  5 .   ? 37.930  30.038  23.698  1.00 99.72  ? 1002 BMA C C4  1 
HETATM 15046 C  C5  . BMA X  5 .   ? 36.454  30.576  23.673  1.00 98.12  ? 1002 BMA C C5  1 
HETATM 15047 C  C6  . BMA X  5 .   ? 36.346  32.058  23.314  1.00 97.91  ? 1002 BMA C C6  1 
HETATM 15048 O  O2  . BMA X  5 .   ? 37.865  28.520  21.395  1.00 81.73  ? 1002 BMA C O2  1 
HETATM 15049 O  O3  . BMA X  5 .   ? 39.268  27.966  23.788  1.00 93.47  ? 1002 BMA C O3  1 
HETATM 15050 O  O4  . BMA X  5 .   ? 38.639  30.583  24.820  1.00 100.91 ? 1002 BMA C O4  1 
HETATM 15051 O  O5  . BMA X  5 .   ? 35.638  29.857  22.701  1.00 93.77  ? 1002 BMA C O5  1 
HETATM 15052 O  O6  . BMA X  5 .   ? 35.098  32.267  22.636  1.00 94.04  ? 1002 BMA C O6  1 
HETATM 15053 C  C1  . NAG Y  4 .   ? 30.882  20.631  32.885  1.00 35.64  ? 1003 NAG C C1  1 
HETATM 15054 C  C2  . NAG Y  4 .   ? 30.818  22.123  32.647  1.00 37.36  ? 1003 NAG C C2  1 
HETATM 15055 C  C3  . NAG Y  4 .   ? 30.271  22.427  31.263  1.00 40.78  ? 1003 NAG C C3  1 
HETATM 15056 C  C4  . NAG Y  4 .   ? 31.047  21.647  30.209  1.00 41.72  ? 1003 NAG C C4  1 
HETATM 15057 C  C5  . NAG Y  4 .   ? 31.069  20.173  30.591  1.00 42.03  ? 1003 NAG C C5  1 
HETATM 15058 C  C6  . NAG Y  4 .   ? 31.819  19.293  29.618  1.00 32.42  ? 1003 NAG C C6  1 
HETATM 15059 C  C7  . NAG Y  4 .   ? 30.594  23.404  34.705  1.00 36.53  ? 1003 NAG C C7  1 
HETATM 15060 C  C8  . NAG Y  4 .   ? 32.084  23.407  34.722  1.00 32.74  ? 1003 NAG C C8  1 
HETATM 15061 N  N2  . NAG Y  4 .   ? 30.026  22.775  33.674  1.00 34.76  ? 1003 NAG C N2  1 
HETATM 15062 O  O3  . NAG Y  4 .   ? 30.376  23.830  31.039  1.00 40.47  ? 1003 NAG C O3  1 
HETATM 15063 O  O4  . NAG Y  4 .   ? 30.362  21.765  28.976  1.00 41.58  ? 1003 NAG C O4  1 
HETATM 15064 O  O5  . NAG Y  4 .   ? 31.678  20.029  31.884  1.00 38.13  ? 1003 NAG C O5  1 
HETATM 15065 O  O6  . NAG Y  4 .   ? 33.120  19.804  29.370  1.00 47.51  ? 1003 NAG C O6  1 
HETATM 15066 O  O7  . NAG Y  4 .   ? 29.933  23.941  35.585  1.00 42.67  ? 1003 NAG C O7  1 
HETATM 15067 C  C1  . NAG Z  4 .   ? 31.196  22.176  27.897  1.00 45.86  ? 1004 NAG C C1  1 
HETATM 15068 C  C2  . NAG Z  4 .   ? 30.176  22.064  26.775  1.00 46.54  ? 1004 NAG C C2  1 
HETATM 15069 C  C3  . NAG Z  4 .   ? 30.670  22.752  25.524  1.00 47.99  ? 1004 NAG C C3  1 
HETATM 15070 C  C4  . NAG Z  4 .   ? 31.209  24.146  25.796  1.00 54.19  ? 1004 NAG C C4  1 
HETATM 15071 C  C5  . NAG Z  4 .   ? 32.133  24.169  27.018  1.00 55.69  ? 1004 NAG C C5  1 
HETATM 15072 C  C6  . NAG Z  4 .   ? 32.363  25.567  27.538  1.00 57.72  ? 1004 NAG C C6  1 
HETATM 15073 C  C7  . NAG Z  4 .   ? 28.649  20.168  26.412  1.00 38.69  ? 1004 NAG C C7  1 
HETATM 15074 C  C8  . NAG Z  4 .   ? 28.559  18.703  26.102  1.00 42.84  ? 1004 NAG C C8  1 
HETATM 15075 N  N2  . NAG Z  4 .   ? 29.887  20.669  26.487  1.00 39.16  ? 1004 NAG C N2  1 
HETATM 15076 O  O3  . NAG Z  4 .   ? 29.569  22.878  24.635  1.00 55.50  ? 1004 NAG C O3  1 
HETATM 15077 O  O4  . NAG Z  4 .   ? 31.870  24.437  24.572  1.00 62.91  ? 1004 NAG C O4  1 
HETATM 15078 O  O5  . NAG Z  4 .   ? 31.507  23.488  28.112  1.00 47.76  ? 1004 NAG C O5  1 
HETATM 15079 O  O6  . NAG Z  4 .   ? 31.130  26.098  28.003  1.00 60.55  ? 1004 NAG C O6  1 
HETATM 15080 O  O7  . NAG Z  4 .   ? 27.646  20.864  26.588  1.00 35.82  ? 1004 NAG C O7  1 
HETATM 15081 C  C1  . BMA AA 5 .   ? 30.734  26.215  20.150  1.00 69.66  ? 1005 BMA C C1  1 
HETATM 15082 C  C2  . BMA AA 5 .   ? 29.310  25.949  19.565  1.00 70.74  ? 1005 BMA C C2  1 
HETATM 15083 C  C3  . BMA AA 5 .   ? 29.359  25.105  18.261  1.00 69.43  ? 1005 BMA C C3  1 
HETATM 15084 C  C4  . BMA AA 5 .   ? 30.496  25.564  17.310  1.00 67.49  ? 1005 BMA C C4  1 
HETATM 15085 C  C5  . BMA AA 5 .   ? 31.824  25.648  18.040  1.00 74.40  ? 1005 BMA C C5  1 
HETATM 15086 C  C6  . BMA AA 5 .   ? 32.950  26.109  17.114  1.00 64.69  ? 1005 BMA C C6  1 
HETATM 15087 O  O2  . BMA AA 5 .   ? 28.646  27.163  19.205  1.00 72.41  ? 1005 BMA C O2  1 
HETATM 15088 O  O3  . BMA AA 5 .   ? 28.104  25.161  17.572  1.00 61.86  ? 1005 BMA C O3  1 
HETATM 15089 O  O4  . BMA AA 5 .   ? 30.660  24.668  16.255  1.00 70.43  ? 1005 BMA C O4  1 
HETATM 15090 O  O5  . BMA AA 5 .   ? 31.682  26.599  19.139  1.00 76.77  ? 1005 BMA C O5  1 
HETATM 15091 O  O6  . BMA AA 5 .   ? 32.635  27.442  16.703  1.00 72.15  ? 1005 BMA C O6  1 
HETATM 15092 C  C1  . NAG BA 4 .   ? 47.561  25.711  76.821  1.00 110.04 ? 1006 NAG C C1  1 
HETATM 15093 C  C2  . NAG BA 4 .   ? 46.370  26.330  77.586  1.00 109.55 ? 1006 NAG C C2  1 
HETATM 15094 C  C3  . NAG BA 4 .   ? 46.509  26.091  79.090  1.00 108.19 ? 1006 NAG C C3  1 
HETATM 15095 C  C4  . NAG BA 4 .   ? 46.698  24.608  79.375  1.00 107.89 ? 1006 NAG C C4  1 
HETATM 15096 C  C5  . NAG BA 4 .   ? 47.940  24.131  78.640  1.00 107.97 ? 1006 NAG C C5  1 
HETATM 15097 C  C6  . NAG BA 4 .   ? 48.220  22.663  78.851  1.00 113.82 ? 1006 NAG C C6  1 
HETATM 15098 C  C7  . NAG BA 4 .   ? 45.131  28.322  76.845  1.00 106.00 ? 1006 NAG C C7  1 
HETATM 15099 C  C8  . NAG BA 4 .   ? 45.190  29.807  76.622  1.00 96.37  ? 1006 NAG C C8  1 
HETATM 15100 N  N2  . NAG BA 4 .   ? 46.250  27.754  77.310  1.00 107.71 ? 1006 NAG C N2  1 
HETATM 15101 O  O3  . NAG BA 4 .   ? 45.348  26.577  79.754  1.00 113.77 ? 1006 NAG C O3  1 
HETATM 15102 O  O4  . NAG BA 4 .   ? 46.835  24.362  80.770  1.00 105.42 ? 1006 NAG C O4  1 
HETATM 15103 O  O5  . NAG BA 4 .   ? 47.747  24.322  77.231  1.00 108.46 ? 1006 NAG C O5  1 
HETATM 15104 O  O6  . NAG BA 4 .   ? 47.213  21.858  78.256  1.00 123.01 ? 1006 NAG C O6  1 
HETATM 15105 O  O7  . NAG BA 4 .   ? 44.119  27.668  76.609  1.00 101.98 ? 1006 NAG C O7  1 
HETATM 15106 C  C1  . NAG CA 4 .   ? 28.244  34.506  62.575  1.00 52.62  ? 1007 NAG C C1  1 
HETATM 15107 C  C2  . NAG CA 4 .   ? 28.058  35.910  61.987  1.00 58.91  ? 1007 NAG C C2  1 
HETATM 15108 C  C3  . NAG CA 4 .   ? 27.645  36.914  63.065  1.00 61.19  ? 1007 NAG C C3  1 
HETATM 15109 C  C4  . NAG CA 4 .   ? 26.501  36.376  63.921  1.00 65.82  ? 1007 NAG C C4  1 
HETATM 15110 C  C5  . NAG CA 4 .   ? 26.779  34.932  64.358  1.00 56.69  ? 1007 NAG C C5  1 
HETATM 15111 C  C6  . NAG CA 4 .   ? 25.617  34.284  65.073  1.00 50.53  ? 1007 NAG C C6  1 
HETATM 15112 C  C7  . NAG CA 4 .   ? 29.249  36.833  60.065  1.00 50.66  ? 1007 NAG C C7  1 
HETATM 15113 C  C8  . NAG CA 4 .   ? 30.580  37.221  59.491  1.00 42.12  ? 1007 NAG C C8  1 
HETATM 15114 N  N2  . NAG CA 4 .   ? 29.265  36.352  61.310  1.00 47.67  ? 1007 NAG C N2  1 
HETATM 15115 O  O3  . NAG CA 4 .   ? 27.222  38.087  62.375  1.00 63.03  ? 1007 NAG C O3  1 
HETATM 15116 O  O4  . NAG CA 4 .   ? 26.296  37.200  65.070  1.00 65.79  ? 1007 NAG C O4  1 
HETATM 15117 O  O5  . NAG CA 4 .   ? 27.068  34.110  63.215  1.00 56.31  ? 1007 NAG C O5  1 
HETATM 15118 O  O6  . NAG CA 4 .   ? 25.914  32.932  65.399  1.00 55.69  ? 1007 NAG C O6  1 
HETATM 15119 O  O7  . NAG CA 4 .   ? 28.203  36.956  59.433  1.00 50.47  ? 1007 NAG C O7  1 
HETATM 15120 C  C1  . NAG DA 4 .   ? 25.380  38.308  64.834  1.00 70.39  ? 1008 NAG C C1  1 
HETATM 15121 C  C2  . NAG DA 4 .   ? 24.547  38.630  66.074  1.00 70.62  ? 1008 NAG C C2  1 
HETATM 15122 C  C3  . NAG DA 4 .   ? 23.641  39.838  65.808  1.00 78.16  ? 1008 NAG C C3  1 
HETATM 15123 C  C4  . NAG DA 4 .   ? 24.438  41.014  65.261  1.00 82.03  ? 1008 NAG C C4  1 
HETATM 15124 C  C5  . NAG DA 4 .   ? 25.294  40.586  64.072  1.00 76.95  ? 1008 NAG C C5  1 
HETATM 15125 C  C6  . NAG DA 4 .   ? 26.248  41.670  63.624  1.00 77.65  ? 1008 NAG C C6  1 
HETATM 15126 C  C7  . NAG DA 4 .   ? 24.111  36.646  67.475  1.00 69.86  ? 1008 NAG C C7  1 
HETATM 15127 C  C8  . NAG DA 4 .   ? 25.434  36.920  68.133  1.00 57.48  ? 1008 NAG C C8  1 
HETATM 15128 N  N2  . NAG DA 4 .   ? 23.752  37.485  66.492  1.00 63.92  ? 1008 NAG C N2  1 
HETATM 15129 O  O3  . NAG DA 4 .   ? 23.023  40.257  67.017  1.00 71.09  ? 1008 NAG C O3  1 
HETATM 15130 O  O4  . NAG DA 4 .   ? 23.533  42.041  64.870  1.00 87.36  ? 1008 NAG C O4  1 
HETATM 15131 O  O5  . NAG DA 4 .   ? 26.109  39.464  64.440  1.00 76.40  ? 1008 NAG C O5  1 
HETATM 15132 O  O6  . NAG DA 4 .   ? 27.357  41.777  64.508  1.00 79.57  ? 1008 NAG C O6  1 
HETATM 15133 O  O7  . NAG DA 4 .   ? 23.401  35.698  67.809  1.00 70.95  ? 1008 NAG C O7  1 
HETATM 15134 C  C1  . NAG EA 4 .   ? 25.356  -7.951  79.620  1.00 90.58  ? 1009 NAG C C1  1 
HETATM 15135 C  C2  . NAG EA 4 .   ? 25.816  -6.496  79.336  1.00 94.45  ? 1009 NAG C C2  1 
HETATM 15136 C  C3  . NAG EA 4 .   ? 26.584  -5.862  80.526  1.00 92.31  ? 1009 NAG C C3  1 
HETATM 15137 C  C4  . NAG EA 4 .   ? 27.466  -6.838  81.311  1.00 95.23  ? 1009 NAG C C4  1 
HETATM 15138 C  C5  . NAG EA 4 .   ? 26.956  -8.273  81.257  1.00 97.71  ? 1009 NAG C C5  1 
HETATM 15139 C  C6  . NAG EA 4 .   ? 27.108  -9.012  82.564  1.00 97.58  ? 1009 NAG C C6  1 
HETATM 15140 C  C7  . NAG EA 4 .   ? 26.421  -5.433  77.195  1.00 96.87  ? 1009 NAG C C7  1 
HETATM 15141 C  C8  . NAG EA 4 .   ? 27.286  -5.521  75.974  1.00 87.30  ? 1009 NAG C C8  1 
HETATM 15142 N  N2  . NAG EA 4 .   ? 26.585  -6.408  78.101  1.00 104.30 ? 1009 NAG C N2  1 
HETATM 15143 O  O3  . NAG EA 4 .   ? 25.686  -5.174  81.391  1.00 90.19  ? 1009 NAG C O3  1 
HETATM 15144 O  O4  . NAG EA 4 .   ? 28.823  -6.763  80.886  1.00 92.20  ? 1009 NAG C O4  1 
HETATM 15145 O  O5  . NAG EA 4 .   ? 25.560  -8.257  80.956  1.00 96.15  ? 1009 NAG C O5  1 
HETATM 15146 O  O6  . NAG EA 4 .   ? 25.990  -9.857  82.799  1.00 99.56  ? 1009 NAG C O6  1 
HETATM 15147 O  O7  . NAG EA 4 .   ? 25.619  -4.513  77.361  1.00 90.28  ? 1009 NAG C O7  1 
HETATM 15148 C  C1  . NAG FA 4 .   ? -1.529  19.504  38.475  1.00 113.70 ? 1010 NAG C C1  1 
HETATM 15149 C  C2  . NAG FA 4 .   ? -2.019  18.742  37.249  1.00 115.86 ? 1010 NAG C C2  1 
HETATM 15150 C  C3  . NAG FA 4 .   ? -2.537  19.730  36.206  1.00 115.78 ? 1010 NAG C C3  1 
HETATM 15151 C  C4  . NAG FA 4 .   ? -3.606  20.632  36.813  1.00 118.51 ? 1010 NAG C C4  1 
HETATM 15152 C  C5  . NAG FA 4 .   ? -3.102  21.289  38.100  1.00 114.79 ? 1010 NAG C C5  1 
HETATM 15153 C  C6  . NAG FA 4 .   ? -4.188  22.042  38.835  1.00 105.65 ? 1010 NAG C C6  1 
HETATM 15154 C  C7  . NAG FA 4 .   ? -0.712  16.656  37.108  1.00 118.13 ? 1010 NAG C C7  1 
HETATM 15155 C  C8  . NAG FA 4 .   ? 0.401   15.943  36.399  1.00 111.85 ? 1010 NAG C C8  1 
HETATM 15156 N  N2  . NAG FA 4 .   ? -0.971  17.902  36.687  1.00 120.09 ? 1010 NAG C N2  1 
HETATM 15157 O  O3  . NAG FA 4 .   ? -3.067  19.025  35.088  1.00 122.94 ? 1010 NAG C O3  1 
HETATM 15158 O  O4  . NAG FA 4 .   ? -3.969  21.647  35.884  1.00 120.53 ? 1010 NAG C O4  1 
HETATM 15159 O  O5  . NAG FA 4 .   ? -2.604  20.296  39.011  1.00 115.49 ? 1010 NAG C O5  1 
HETATM 15160 O  O6  . NAG FA 4 .   ? -4.150  23.428  38.530  1.00 106.18 ? 1010 NAG C O6  1 
HETATM 15161 O  O7  . NAG FA 4 .   ? -1.344  16.128  38.022  1.00 109.38 ? 1010 NAG C O7  1 
HETATM 15162 C  C1  . NAG GA 4 .   ? -2.874  18.076  72.468  1.00 98.36  ? 1011 NAG C C1  1 
HETATM 15163 C  C2  . NAG GA 4 .   ? -2.883  17.762  73.948  1.00 97.49  ? 1011 NAG C C2  1 
HETATM 15164 C  C3  . NAG GA 4 .   ? -4.329  17.599  74.415  1.00 100.22 ? 1011 NAG C C3  1 
HETATM 15165 C  C4  . NAG GA 4 .   ? -5.198  18.766  73.950  1.00 102.02 ? 1011 NAG C C4  1 
HETATM 15166 C  C5  . NAG GA 4 .   ? -4.932  19.167  72.494  1.00 100.27 ? 1011 NAG C C5  1 
HETATM 15167 C  C6  . NAG GA 4 .   ? -5.550  20.494  72.122  1.00 103.45 ? 1011 NAG C C6  1 
HETATM 15168 C  C7  . NAG GA 4 .   ? -0.852  16.607  74.705  1.00 91.58  ? 1011 NAG C C7  1 
HETATM 15169 C  C8  . NAG GA 4 .   ? -0.203  15.279  74.957  1.00 89.49  ? 1011 NAG C C8  1 
HETATM 15170 N  N2  . NAG GA 4 .   ? -2.108  16.568  74.244  1.00 92.48  ? 1011 NAG C N2  1 
HETATM 15171 O  O3  . NAG GA 4 .   ? -4.376  17.503  75.835  1.00 102.52 ? 1011 NAG C O3  1 
HETATM 15172 O  O4  . NAG GA 4 .   ? -6.565  18.381  74.047  1.00 111.68 ? 1011 NAG C O4  1 
HETATM 15173 O  O5  . NAG GA 4 .   ? -3.525  19.290  72.248  1.00 101.70 ? 1011 NAG C O5  1 
HETATM 15174 O  O6  . NAG GA 4 .   ? -5.578  21.380  73.233  1.00 105.15 ? 1011 NAG C O6  1 
HETATM 15175 O  O7  . NAG GA 4 .   ? -0.266  17.666  74.908  1.00 88.32  ? 1011 NAG C O7  1 
HETATM 15176 C  C1  . NAG HA 4 .   ? 7.603   -26.396 56.505  1.00 110.92 ? 1012 NAG C C1  1 
HETATM 15177 C  C2  . NAG HA 4 .   ? 7.557   -27.461 55.404  1.00 115.01 ? 1012 NAG C C2  1 
HETATM 15178 C  C3  . NAG HA 4 .   ? 8.616   -27.172 54.336  1.00 116.32 ? 1012 NAG C C3  1 
HETATM 15179 C  C4  . NAG HA 4 .   ? 8.506   -25.740 53.829  1.00 111.91 ? 1012 NAG C C4  1 
HETATM 15180 C  C5  . NAG HA 4 .   ? 8.504   -24.755 54.996  1.00 112.69 ? 1012 NAG C C5  1 
HETATM 15181 C  C6  . NAG HA 4 .   ? 8.253   -23.326 54.564  1.00 110.42 ? 1012 NAG C C6  1 
HETATM 15182 C  C7  . NAG HA 4 .   ? 6.964   -29.840 55.664  1.00 114.22 ? 1012 NAG C C7  1 
HETATM 15183 C  C8  . NAG HA 4 .   ? 5.836   -29.574 54.710  1.00 114.10 ? 1012 NAG C C8  1 
HETATM 15184 N  N2  . NAG HA 4 .   ? 7.747   -28.794 55.959  1.00 117.66 ? 1012 NAG C N2  1 
HETATM 15185 O  O3  . NAG HA 4 .   ? 8.457   -28.077 53.249  1.00 115.46 ? 1012 NAG C O3  1 
HETATM 15186 O  O4  . NAG HA 4 .   ? 9.610   -25.457 52.976  1.00 106.97 ? 1012 NAG C O4  1 
HETATM 15187 O  O5  . NAG HA 4 .   ? 7.461   -25.095 55.922  1.00 108.23 ? 1012 NAG C O5  1 
HETATM 15188 O  O6  . NAG HA 4 .   ? 9.194   -22.888 53.593  1.00 101.72 ? 1012 NAG C O6  1 
HETATM 15189 O  O7  . NAG HA 4 .   ? 7.156   -30.951 56.149  1.00 105.65 ? 1012 NAG C O7  1 
HETATM 15190 C  C1  . NAG IA 4 .   ? -20.591 1.721   82.825  1.00 118.16 ? 1013 NAG C C1  1 
HETATM 15191 C  C2  . NAG IA 4 .   ? -21.875 1.300   82.064  1.00 119.51 ? 1013 NAG C C2  1 
HETATM 15192 C  C3  . NAG IA 4 .   ? -22.906 2.435   82.068  1.00 121.99 ? 1013 NAG C C3  1 
HETATM 15193 C  C4  . NAG IA 4 .   ? -23.167 2.928   83.487  1.00 127.29 ? 1013 NAG C C4  1 
HETATM 15194 C  C5  . NAG IA 4 .   ? -21.853 3.376   84.111  1.00 125.33 ? 1013 NAG C C5  1 
HETATM 15195 C  C6  . NAG IA 4 .   ? -22.004 3.824   85.547  1.00 126.80 ? 1013 NAG C C6  1 
HETATM 15196 C  C7  . NAG IA 4 .   ? -22.045 -0.185  80.100  1.00 124.83 ? 1013 NAG C C7  1 
HETATM 15197 C  C8  . NAG IA 4 .   ? -21.617 -0.413  78.676  1.00 108.98 ? 1013 NAG C C8  1 
HETATM 15198 N  N2  . NAG IA 4 .   ? -21.561 0.916   80.689  1.00 124.55 ? 1013 NAG C N2  1 
HETATM 15199 O  O3  . NAG IA 4 .   ? -24.122 1.995   81.476  1.00 121.87 ? 1013 NAG C O3  1 
HETATM 15200 O  O4  . NAG IA 4 .   ? -24.090 4.011   83.476  1.00 119.17 ? 1013 NAG C O4  1 
HETATM 15201 O  O5  . NAG IA 4 .   ? -20.949 2.266   84.128  1.00 122.21 ? 1013 NAG C O5  1 
HETATM 15202 O  O6  . NAG IA 4 .   ? -20.754 4.178   86.125  1.00 126.24 ? 1013 NAG C O6  1 
HETATM 15203 O  O7  . NAG IA 4 .   ? -22.784 -0.970  80.688  1.00 126.55 ? 1013 NAG C O7  1 
HETATM 15204 ZN ZN  . ZN  JA 3 .   ? 16.052  13.739  64.046  1.00 39.86  ? 1020 ZN  C ZN  1 
HETATM 15205 C  C1  . EDO KA 6 .   ? 13.014  35.838  60.021  1.00 61.97  ? 1962 EDO C C1  1 
HETATM 15206 O  O1  . EDO KA 6 .   ? 12.825  36.916  59.095  1.00 62.68  ? 1962 EDO C O1  1 
HETATM 15207 C  C2  . EDO KA 6 .   ? 14.501  35.672  60.323  1.00 57.05  ? 1962 EDO C C2  1 
HETATM 15208 O  O2  . EDO KA 6 .   ? 15.027  36.864  60.921  1.00 71.27  ? 1962 EDO C O2  1 
HETATM 15209 C  C1  . EDO LA 6 .   ? -20.894 -17.219 65.183  1.00 89.98  ? 1963 EDO C C1  1 
HETATM 15210 O  O1  . EDO LA 6 .   ? -20.895 -17.115 63.749  1.00 99.73  ? 1963 EDO C O1  1 
HETATM 15211 C  C2  . EDO LA 6 .   ? -21.749 -18.425 65.564  1.00 91.12  ? 1963 EDO C C2  1 
HETATM 15212 O  O2  . EDO LA 6 .   ? -21.827 -18.456 66.999  1.00 96.77  ? 1963 EDO C O2  1 
HETATM 15213 O  O   . HOH MA 8 .   ? -14.415 0.530   -3.716  1.00 73.92  ? 3001 HOH A O   1 
HETATM 15214 O  O   . HOH MA 8 .   ? -13.916 5.873   7.216   1.00 62.15  ? 3002 HOH A O   1 
HETATM 15215 O  O   . HOH MA 8 .   ? -19.379 6.742   -0.594  1.00 66.84  ? 3003 HOH A O   1 
HETATM 15216 O  O   . HOH MA 8 .   ? -3.560  -3.069  -8.213  1.00 56.63  ? 3004 HOH A O   1 
HETATM 15217 O  O   . HOH MA 8 .   ? 0.059   4.211   -3.731  1.00 49.73  ? 3005 HOH A O   1 
HETATM 15218 O  O   . HOH MA 8 .   ? 2.275   7.193   -8.687  1.00 44.62  ? 3006 HOH A O   1 
HETATM 15219 O  O   . HOH MA 8 .   ? 4.926   1.332   -12.781 1.00 54.44  ? 3007 HOH A O   1 
HETATM 15220 O  O   . HOH MA 8 .   ? 2.744   16.525  -7.730  1.00 40.42  ? 3008 HOH A O   1 
HETATM 15221 O  O   . HOH MA 8 .   ? 4.280   20.098  -8.406  1.00 42.51  ? 3009 HOH A O   1 
HETATM 15222 O  O   . HOH MA 8 .   ? 2.969   14.544  -2.744  1.00 57.84  ? 3010 HOH A O   1 
HETATM 15223 O  O   . HOH MA 8 .   ? 1.134   18.991  21.292  1.00 52.37  ? 3011 HOH A O   1 
HETATM 15224 O  O   . HOH MA 8 .   ? 8.503   20.168  20.287  1.00 36.94  ? 3012 HOH A O   1 
HETATM 15225 O  O   . HOH MA 8 .   ? 1.720   20.099  24.078  1.00 48.21  ? 3013 HOH A O   1 
HETATM 15226 O  O   . HOH MA 8 .   ? 4.789   10.590  28.731  1.00 47.99  ? 3014 HOH A O   1 
HETATM 15227 O  O   . HOH MA 8 .   ? 0.324   16.942  21.598  1.00 69.22  ? 3015 HOH A O   1 
HETATM 15228 O  O   . HOH MA 8 .   ? -7.120  12.025  -5.403  1.00 50.61  ? 3016 HOH A O   1 
HETATM 15229 O  O   . HOH MA 8 .   ? -5.884  7.841   8.982   1.00 51.28  ? 3017 HOH A O   1 
HETATM 15230 O  O   . HOH MA 8 .   ? 0.868   7.768   13.194  1.00 41.77  ? 3018 HOH A O   1 
HETATM 15231 O  O   . HOH MA 8 .   ? -3.570  3.519   15.178  1.00 50.40  ? 3019 HOH A O   1 
HETATM 15232 O  O   . HOH MA 8 .   ? -8.743  10.116  11.461  1.00 54.21  ? 3020 HOH A O   1 
HETATM 15233 O  O   . HOH MA 8 .   ? -9.601  19.866  15.918  1.00 65.33  ? 3021 HOH A O   1 
HETATM 15234 O  O   . HOH MA 8 .   ? -9.055  24.557  3.292   1.00 53.63  ? 3022 HOH A O   1 
HETATM 15235 O  O   . HOH MA 8 .   ? -12.700 32.888  -4.214  1.00 56.74  ? 3023 HOH A O   1 
HETATM 15236 O  O   . HOH MA 8 .   ? -8.027  34.379  -7.749  1.00 48.81  ? 3024 HOH A O   1 
HETATM 15237 O  O   . HOH MA 8 .   ? -15.567 30.542  -9.730  1.00 59.40  ? 3025 HOH A O   1 
HETATM 15238 O  O   . HOH MA 8 .   ? -4.717  28.275  -12.619 1.00 49.90  ? 3026 HOH A O   1 
HETATM 15239 O  O   . HOH MA 8 .   ? -16.535 26.692  -10.796 1.00 52.53  ? 3027 HOH A O   1 
HETATM 15240 O  O   . HOH MA 8 .   ? 19.065  24.839  10.589  1.00 40.79  ? 3028 HOH A O   1 
HETATM 15241 O  O   . HOH MA 8 .   ? 21.064  27.222  8.083   1.00 36.25  ? 3029 HOH A O   1 
HETATM 15242 O  O   . HOH MA 8 .   ? -15.801 13.081  8.218   1.00 60.63  ? 3030 HOH A O   1 
HETATM 15243 O  O   . HOH MA 8 .   ? 14.361  27.702  -5.510  1.00 48.80  ? 3031 HOH A O   1 
HETATM 15244 O  O   . HOH MA 8 .   ? 3.284   2.149   4.689   1.00 44.03  ? 3032 HOH A O   1 
HETATM 15245 O  O   . HOH MA 8 .   ? 36.036  23.159  8.828   1.00 51.63  ? 3033 HOH A O   1 
HETATM 15246 O  O   . HOH MA 8 .   ? -4.793  29.623  -5.707  1.00 54.71  ? 3034 HOH A O   1 
HETATM 15247 O  O   . HOH MA 8 .   ? 29.260  23.725  -10.784 1.00 44.04  ? 3035 HOH A O   1 
HETATM 15248 O  O   . HOH MA 8 .   ? 21.873  26.033  -7.510  1.00 43.70  ? 3036 HOH A O   1 
HETATM 15249 O  O   . HOH MA 8 .   ? 4.078   3.215   17.182  1.00 53.35  ? 3037 HOH A O   1 
HETATM 15250 O  O   . HOH MA 8 .   ? 15.221  4.888   11.841  1.00 40.04  ? 3038 HOH A O   1 
HETATM 15251 O  O   . HOH MA 8 .   ? 4.893   9.262   12.480  1.00 39.38  ? 3039 HOH A O   1 
HETATM 15252 O  O   . HOH MA 8 .   ? 17.989  15.486  22.513  1.00 35.08  ? 3040 HOH A O   1 
HETATM 15253 O  O   . HOH MA 8 .   ? 25.928  11.978  24.419  1.00 48.60  ? 3041 HOH A O   1 
HETATM 15254 O  O   . HOH MA 8 .   ? 27.002  5.611   27.738  1.00 52.12  ? 3042 HOH A O   1 
HETATM 15255 O  O   . HOH MA 8 .   ? 24.304  8.858   36.333  1.00 47.43  ? 3043 HOH A O   1 
HETATM 15256 O  O   . HOH MA 8 .   ? 5.245   -1.595  -12.812 1.00 47.74  ? 3044 HOH A O   1 
HETATM 15257 O  O   . HOH MA 8 .   ? 14.403  16.133  25.361  1.00 40.57  ? 3045 HOH A O   1 
HETATM 15258 O  O   . HOH MA 8 .   ? 12.186  11.842  7.197   1.00 32.48  ? 3046 HOH A O   1 
HETATM 15259 O  O   . HOH MA 8 .   ? 15.278  9.872   8.493   1.00 26.36  ? 3047 HOH A O   1 
HETATM 15260 O  O   . HOH MA 8 .   ? 10.854  4.333   6.581   1.00 40.57  ? 3048 HOH A O   1 
HETATM 15261 O  O   . HOH MA 8 .   ? 14.173  5.706   5.458   1.00 34.93  ? 3049 HOH A O   1 
HETATM 15262 O  O   . HOH MA 8 .   ? 12.985  9.730   5.064   1.00 29.86  ? 3050 HOH A O   1 
HETATM 15263 O  O   . HOH MA 8 .   ? 7.158   8.206   2.551   1.00 29.47  ? 3051 HOH A O   1 
HETATM 15264 O  O   . HOH MA 8 .   ? 16.100  6.162   -2.163  1.00 36.19  ? 3052 HOH A O   1 
HETATM 15265 O  O   . HOH MA 8 .   ? 6.444   7.582   -0.936  1.00 30.69  ? 3053 HOH A O   1 
HETATM 15266 O  O   . HOH MA 8 .   ? 2.685   3.342   -2.395  1.00 37.44  ? 3054 HOH A O   1 
HETATM 15267 O  O   . HOH MA 8 .   ? 6.280   12.773  -3.383  1.00 32.75  ? 3055 HOH A O   1 
HETATM 15268 O  O   . HOH MA 8 .   ? 5.430   7.896   -7.855  1.00 35.67  ? 3056 HOH A O   1 
HETATM 15269 O  O   . HOH MA 8 .   ? 7.483   9.913   -2.239  1.00 31.21  ? 3057 HOH A O   1 
HETATM 15270 O  O   . HOH MA 8 .   ? 3.576   16.075  -10.518 1.00 43.97  ? 3058 HOH A O   1 
HETATM 15271 O  O   . HOH MA 8 .   ? 12.345  14.317  -4.641  1.00 25.48  ? 3059 HOH A O   1 
HETATM 15272 O  O   . HOH MA 8 .   ? 13.309  17.107  -7.201  1.00 28.83  ? 3060 HOH A O   1 
HETATM 15273 O  O   . HOH MA 8 .   ? 10.194  24.081  4.610   1.00 42.82  ? 3061 HOH A O   1 
HETATM 15274 O  O   . HOH MA 8 .   ? 2.313   28.772  12.507  1.00 49.87  ? 3062 HOH A O   1 
HETATM 15275 O  O   . HOH MA 8 .   ? 15.406  28.821  22.168  1.00 42.06  ? 3063 HOH A O   1 
HETATM 15276 O  O   . HOH MA 8 .   ? 15.479  30.250  19.593  1.00 47.17  ? 3064 HOH A O   1 
HETATM 15277 O  O   . HOH MA 8 .   ? 7.718   10.099  -21.046 1.00 58.28  ? 3065 HOH A O   1 
HETATM 15278 O  O   . HOH MA 8 .   ? 9.798   27.237  26.195  1.00 49.62  ? 3066 HOH A O   1 
HETATM 15279 O  O   . HOH MA 8 .   ? 16.724  26.657  27.537  1.00 42.48  ? 3067 HOH A O   1 
HETATM 15280 O  O   . HOH MA 8 .   ? 16.704  18.105  27.024  1.00 64.35  ? 3068 HOH A O   1 
HETATM 15281 O  O   . HOH MA 8 .   ? 16.028  25.599  16.281  1.00 42.25  ? 3069 HOH A O   1 
HETATM 15282 O  O   . HOH MA 8 .   ? 17.475  25.254  13.006  1.00 32.49  ? 3070 HOH A O   1 
HETATM 15283 O  O   . HOH MA 8 .   ? 17.326  23.203  9.690   1.00 29.50  ? 3071 HOH A O   1 
HETATM 15284 O  O   . HOH MA 8 .   ? 12.341  22.136  5.268   1.00 40.79  ? 3072 HOH A O   1 
HETATM 15285 O  O   . HOH MA 8 .   ? 19.464  22.929  3.138   1.00 38.16  ? 3073 HOH A O   1 
HETATM 15286 O  O   . HOH MA 8 .   ? 19.352  27.022  9.828   1.00 41.64  ? 3074 HOH A O   1 
HETATM 15287 O  O   . HOH MA 8 .   ? 9.855   37.048  18.148  1.00 58.89  ? 3075 HOH A O   1 
HETATM 15288 O  O   . HOH MA 8 .   ? 6.095   34.782  27.633  1.00 54.94  ? 3076 HOH A O   1 
HETATM 15289 O  O   . HOH MA 8 .   ? 18.270  27.084  0.141   1.00 43.94  ? 3077 HOH A O   1 
HETATM 15290 O  O   . HOH MA 8 .   ? 10.765  30.423  1.936   1.00 37.98  ? 3078 HOH A O   1 
HETATM 15291 O  O   . HOH MA 8 .   ? 13.108  27.245  -2.785  1.00 46.76  ? 3079 HOH A O   1 
HETATM 15292 O  O   . HOH MA 8 .   ? 9.480   30.630  3.812   1.00 65.83  ? 3080 HOH A O   1 
HETATM 15293 O  O   . HOH MA 8 .   ? 21.985  -20.046 -24.132 1.00 55.59  ? 3081 HOH A O   1 
HETATM 15294 O  O   . HOH MA 8 .   ? 16.804  9.801   -2.569  1.00 28.97  ? 3082 HOH A O   1 
HETATM 15295 O  O   . HOH MA 8 .   ? 23.596  23.794  17.805  1.00 53.21  ? 3083 HOH A O   1 
HETATM 15296 O  O   . HOH MA 8 .   ? 25.743  23.622  18.523  1.00 44.00  ? 3084 HOH A O   1 
HETATM 15297 O  O   . HOH MA 8 .   ? 34.449  24.461  11.062  1.00 54.07  ? 3085 HOH A O   1 
HETATM 15298 O  O   . HOH MA 8 .   ? 34.869  26.715  6.435   1.00 46.92  ? 3086 HOH A O   1 
HETATM 15299 O  O   . HOH MA 8 .   ? 25.563  29.054  2.503   1.00 36.81  ? 3087 HOH A O   1 
HETATM 15300 O  O   . HOH MA 8 .   ? 24.447  23.706  8.133   1.00 31.74  ? 3088 HOH A O   1 
HETATM 15301 O  O   . HOH MA 8 .   ? 26.348  31.094  9.485   1.00 54.42  ? 3089 HOH A O   1 
HETATM 15302 O  O   . HOH MA 8 .   ? 20.954  23.861  10.728  1.00 40.79  ? 3090 HOH A O   1 
HETATM 15303 O  O   . HOH MA 8 .   ? 32.748  -21.647 -2.689  1.00 41.43  ? 3091 HOH A O   1 
HETATM 15304 O  O   . HOH MA 8 .   ? 24.505  11.462  18.485  1.00 34.10  ? 3092 HOH A O   1 
HETATM 15305 O  O   . HOH MA 8 .   ? 24.095  9.539   21.441  1.00 41.34  ? 3093 HOH A O   1 
HETATM 15306 O  O   . HOH MA 8 .   ? 32.132  17.625  23.622  1.00 46.26  ? 3094 HOH A O   1 
HETATM 15307 O  O   . HOH MA 8 .   ? 30.386  16.268  27.423  1.00 35.77  ? 3095 HOH A O   1 
HETATM 15308 O  O   . HOH MA 8 .   ? 29.732  7.259   19.119  1.00 36.90  ? 3096 HOH A O   1 
HETATM 15309 O  O   . HOH MA 8 .   ? 27.734  5.457   22.705  1.00 37.64  ? 3097 HOH A O   1 
HETATM 15310 O  O   . HOH MA 8 .   ? 41.692  -35.889 -10.529 1.00 54.11  ? 3098 HOH A O   1 
HETATM 15311 O  O   . HOH MA 8 .   ? 34.660  19.692  19.586  1.00 43.29  ? 3099 HOH A O   1 
HETATM 15312 O  O   . HOH MA 8 .   ? 38.016  17.348  23.220  1.00 54.57  ? 3100 HOH A O   1 
HETATM 15313 O  O   . HOH MA 8 .   ? 33.106  12.020  12.209  1.00 31.38  ? 3101 HOH A O   1 
HETATM 15314 O  O   . HOH MA 8 .   ? 36.301  12.753  14.186  1.00 36.38  ? 3102 HOH A O   1 
HETATM 15315 O  O   . HOH MA 8 .   ? 33.177  6.887   17.360  1.00 41.56  ? 3103 HOH A O   1 
HETATM 15316 O  O   . HOH MA 8 .   ? 34.033  -17.624 6.574   1.00 50.15  ? 3104 HOH A O   1 
HETATM 15317 O  O   . HOH MA 8 .   ? 36.555  20.615  8.069   1.00 39.22  ? 3105 HOH A O   1 
HETATM 15318 O  O   . HOH MA 8 .   ? 36.346  17.671  -3.189  1.00 37.85  ? 3106 HOH A O   1 
HETATM 15319 O  O   . HOH MA 8 .   ? 55.979  -23.468 2.688   1.00 72.27  ? 3107 HOH A O   1 
HETATM 15320 O  O   . HOH MA 8 .   ? 31.248  23.614  -9.632  1.00 45.38  ? 3108 HOH A O   1 
HETATM 15321 O  O   . HOH MA 8 .   ? 32.096  21.421  -13.345 1.00 49.25  ? 3109 HOH A O   1 
HETATM 15322 O  O   . HOH MA 8 .   ? 27.272  24.240  -11.899 1.00 65.14  ? 3110 HOH A O   1 
HETATM 15323 O  O   . HOH MA 8 .   ? 28.881  24.965  -13.173 1.00 58.44  ? 3111 HOH A O   1 
HETATM 15324 O  O   . HOH MA 8 .   ? 24.006  23.953  -11.164 1.00 44.10  ? 3112 HOH A O   1 
HETATM 15325 O  O   . HOH MA 8 .   ? 21.589  23.518  -8.667  1.00 37.96  ? 3113 HOH A O   1 
HETATM 15326 O  O   . HOH MA 8 .   ? 32.345  27.192  -9.017  1.00 49.95  ? 3114 HOH A O   1 
HETATM 15327 O  O   . HOH MA 8 .   ? 21.140  27.992  -1.970  1.00 35.52  ? 3115 HOH A O   1 
HETATM 15328 O  O   . HOH MA 8 .   ? 20.547  30.592  5.474   1.00 62.21  ? 3116 HOH A O   1 
HETATM 15329 O  O   . HOH MA 8 .   ? 21.779  28.703  5.651   1.00 32.70  ? 3117 HOH A O   1 
HETATM 15330 O  O   . HOH MA 8 .   ? 53.234  -21.279 21.563  1.00 70.54  ? 3118 HOH A O   1 
HETATM 15331 O  O   . HOH MA 8 .   ? 22.329  25.095  9.199   1.00 63.72  ? 3119 HOH A O   1 
HETATM 15332 O  O   . HOH MA 8 .   ? 32.821  -18.174 37.213  1.00 60.31  ? 3120 HOH A O   1 
HETATM 15333 O  O   . HOH MA 8 .   ? 25.121  3.428   16.074  1.00 32.06  ? 3121 HOH A O   1 
HETATM 15334 O  O   . HOH MA 8 .   ? 30.781  5.816   16.264  1.00 44.82  ? 3122 HOH A O   1 
HETATM 15335 O  O   . HOH MA 8 .   ? 26.840  1.885   10.863  1.00 32.02  ? 3123 HOH A O   1 
HETATM 15336 O  O   . HOH MA 8 .   ? 33.710  5.413   13.770  1.00 28.45  ? 3124 HOH A O   1 
HETATM 15337 O  O   . HOH MA 8 .   ? 42.005  5.099   13.006  1.00 52.35  ? 3125 HOH A O   1 
HETATM 15338 O  O   . HOH MA 8 .   ? 37.013  -2.971  13.131  1.00 57.25  ? 3126 HOH A O   1 
HETATM 15339 O  O   . HOH MA 8 .   ? 32.008  0.282   14.263  1.00 49.46  ? 3127 HOH A O   1 
HETATM 15340 O  O   . HOH MA 8 .   ? 33.559  -1.075  14.710  1.00 44.65  ? 3128 HOH A O   1 
HETATM 15341 O  O   . HOH MA 8 .   ? 13.988  -17.818 25.610  1.00 62.67  ? 3129 HOH A O   1 
HETATM 15342 O  O   . HOH MA 8 .   ? 25.405  -0.153  0.035   1.00 47.63  ? 3130 HOH A O   1 
HETATM 15343 O  O   . HOH MA 8 .   ? 9.638   -11.017 26.567  1.00 58.41  ? 3131 HOH A O   1 
HETATM 15344 O  O   . HOH MA 8 .   ? 4.828   -18.862 13.813  1.00 70.08  ? 3132 HOH A O   1 
HETATM 15345 O  O   . HOH MA 8 .   ? 16.955  8.712   -8.958  1.00 32.32  ? 3133 HOH A O   1 
HETATM 15346 O  O   . HOH MA 8 .   ? 7.917   -21.171 1.204   1.00 70.11  ? 3134 HOH A O   1 
HETATM 15347 O  O   . HOH MA 8 .   ? 9.767   3.773   -12.812 1.00 43.00  ? 3135 HOH A O   1 
HETATM 15348 O  O   . HOH MA 8 .   ? 5.500   -1.510  -10.390 1.00 41.74  ? 3136 HOH A O   1 
HETATM 15349 O  O   . HOH MA 8 .   ? 8.501   1.539   -15.555 1.00 49.52  ? 3137 HOH A O   1 
HETATM 15350 O  O   . HOH MA 8 .   ? 9.318   -2.844  -13.869 1.00 37.72  ? 3138 HOH A O   1 
HETATM 15351 O  O   . HOH MA 8 .   ? 10.346  1.161   -16.279 1.00 43.76  ? 3139 HOH A O   1 
HETATM 15352 O  O   . HOH MA 8 .   ? 18.537  8.497   -10.954 1.00 32.43  ? 3140 HOH A O   1 
HETATM 15353 O  O   . HOH MA 8 .   ? 42.954  0.156   -7.970  1.00 50.07  ? 3141 HOH A O   1 
HETATM 15354 O  O   . HOH MA 8 .   ? 38.744  -8.685  -3.019  1.00 53.55  ? 3142 HOH A O   1 
HETATM 15355 O  O   . HOH MA 8 .   ? 31.045  -6.866  -12.371 1.00 58.99  ? 3143 HOH A O   1 
HETATM 15356 O  O   . HOH MA 8 .   ? 22.292  -16.929 -13.382 1.00 44.88  ? 3144 HOH A O   1 
HETATM 15357 O  O   . HOH MA 8 .   ? 19.275  -9.863  -11.512 1.00 43.41  ? 3145 HOH A O   1 
HETATM 15358 O  O   . HOH MA 8 .   ? 19.026  -7.436  -14.193 1.00 31.08  ? 3146 HOH A O   1 
HETATM 15359 O  O   . HOH MA 8 .   ? 11.529  -0.932  -16.380 1.00 47.82  ? 3147 HOH A O   1 
HETATM 15360 O  O   . HOH MA 8 .   ? 10.016  -7.715  -4.697  1.00 48.36  ? 3148 HOH A O   1 
HETATM 15361 O  O   . HOH MA 8 .   ? 11.416  1.172   6.466   1.00 42.67  ? 3149 HOH A O   1 
HETATM 15362 O  O   . HOH MA 8 .   ? 14.355  -9.073  -2.664  1.00 57.46  ? 3150 HOH A O   1 
HETATM 15363 O  O   . HOH MA 8 .   ? 12.919  -10.910 0.623   1.00 48.66  ? 3151 HOH A O   1 
HETATM 15364 O  O   . HOH MA 8 .   ? 6.181   -10.246 -0.425  1.00 61.31  ? 3152 HOH A O   1 
HETATM 15365 O  O   . HOH MA 8 .   ? 25.304  -2.534  -0.634  1.00 48.55  ? 3153 HOH A O   1 
HETATM 15366 O  O   . HOH MA 8 .   ? 20.677  -9.665  -15.984 1.00 38.67  ? 3154 HOH A O   1 
HETATM 15367 O  O   . HOH MA 8 .   ? 31.657  -4.974  -13.222 1.00 53.89  ? 3155 HOH A O   1 
HETATM 15368 O  O   . HOH MA 8 .   ? 37.552  2.489   -20.902 1.00 47.04  ? 3156 HOH A O   1 
HETATM 15369 O  O   . HOH MA 8 .   ? 38.461  -3.172  -19.164 1.00 52.16  ? 3157 HOH A O   1 
HETATM 15370 O  O   . HOH MA 8 .   ? 35.300  8.326   -23.164 1.00 41.06  ? 3158 HOH A O   1 
HETATM 15371 O  O   . HOH MA 8 .   ? 35.422  15.596  -19.759 1.00 66.59  ? 3159 HOH A O   1 
HETATM 15372 O  O   . HOH MA 8 .   ? 31.702  5.301   -26.936 1.00 43.93  ? 3160 HOH A O   1 
HETATM 15373 O  O   . HOH MA 8 .   ? 27.016  20.121  -19.834 1.00 44.91  ? 3161 HOH A O   1 
HETATM 15374 O  O   . HOH MA 8 .   ? 17.256  12.023  -24.904 1.00 47.62  ? 3162 HOH A O   1 
HETATM 15375 O  O   . HOH MA 8 .   ? 19.553  22.626  -10.994 1.00 52.07  ? 3163 HOH A O   1 
HETATM 15376 O  O   . HOH MA 8 .   ? 7.844   13.410  -18.183 1.00 58.54  ? 3164 HOH A O   1 
HETATM 15377 O  O   . HOH MA 8 .   ? 8.628   13.668  -14.388 1.00 62.08  ? 3165 HOH A O   1 
HETATM 15378 O  O   . HOH MA 8 .   ? 11.258  2.116   -18.285 1.00 45.37  ? 3166 HOH A O   1 
HETATM 15379 O  O   . HOH MA 8 .   ? 13.503  -0.219  -19.758 1.00 46.63  ? 3167 HOH A O   1 
HETATM 15380 O  O   . HOH MA 8 .   ? 14.141  9.804   -21.905 1.00 45.81  ? 3168 HOH A O   1 
HETATM 15381 O  O   . HOH MA 8 .   ? 10.765  10.994  -20.552 1.00 50.96  ? 3169 HOH A O   1 
HETATM 15382 O  O   . HOH MA 8 .   ? 27.089  8.586   -27.018 1.00 46.70  ? 3170 HOH A O   1 
HETATM 15383 O  O   . HOH MA 8 .   ? 21.755  8.874   -30.805 1.00 49.39  ? 3171 HOH A O   1 
HETATM 15384 O  O   . HOH MA 8 .   ? 19.865  22.186  -34.563 1.00 74.30  ? 3172 HOH A O   1 
HETATM 15385 O  O   . HOH MA 8 .   ? 17.652  6.508   -27.214 1.00 64.47  ? 3173 HOH A O   1 
HETATM 15386 O  O   . HOH MA 8 .   ? 11.792  -7.984  -16.521 1.00 53.12  ? 3174 HOH A O   1 
HETATM 15387 O  O   . HOH MA 8 .   ? 33.638  -22.807 -26.728 1.00 62.19  ? 3175 HOH A O   1 
HETATM 15388 O  O   . HOH MA 8 .   ? 31.565  -25.794 -29.900 1.00 72.25  ? 3176 HOH A O   1 
HETATM 15389 O  O   . HOH MA 8 .   ? 26.669  -25.423 -28.166 1.00 59.59  ? 3177 HOH A O   1 
HETATM 15390 O  O   . HOH MA 8 .   ? 23.131  -16.382 -22.833 1.00 57.35  ? 3178 HOH A O   1 
HETATM 15391 O  O   . HOH MA 8 .   ? 26.850  -23.260 -14.915 1.00 54.64  ? 3179 HOH A O   1 
HETATM 15392 O  O   . HOH MA 8 .   ? 27.025  -25.445 -14.788 1.00 58.86  ? 3180 HOH A O   1 
HETATM 15393 O  O   . HOH MA 8 .   ? 31.293  -31.436 -19.458 1.00 62.26  ? 3181 HOH A O   1 
HETATM 15394 O  O   . HOH MA 8 .   ? 32.622  -29.225 -17.492 1.00 60.74  ? 3182 HOH A O   1 
HETATM 15395 O  O   . HOH MA 8 .   ? 16.525  -28.627 -9.081  1.00 75.97  ? 3183 HOH A O   1 
HETATM 15396 O  O   . HOH MA 8 .   ? 19.829  -19.278 -24.060 1.00 59.64  ? 3184 HOH A O   1 
HETATM 15397 O  O   . HOH MA 8 .   ? 35.426  -7.131  -19.441 1.00 41.45  ? 3185 HOH A O   1 
HETATM 15398 O  O   . HOH MA 8 .   ? 34.588  -2.698  -23.397 1.00 51.58  ? 3186 HOH A O   1 
HETATM 15399 O  O   . HOH MA 8 .   ? 31.241  -18.775 -35.114 1.00 59.54  ? 3187 HOH A O   1 
HETATM 15400 O  O   . HOH MA 8 .   ? 55.583  -13.708 -29.184 1.00 75.82  ? 3188 HOH A O   1 
HETATM 15401 O  O   . HOH MA 8 .   ? 48.800  -21.278 -36.782 1.00 71.51  ? 3189 HOH A O   1 
HETATM 15402 O  O   . HOH MA 8 .   ? 43.481  -19.314 -20.694 1.00 52.04  ? 3190 HOH A O   1 
HETATM 15403 O  O   . HOH MA 8 .   ? 44.980  -4.873  -11.817 1.00 46.07  ? 3191 HOH A O   1 
HETATM 15404 O  O   . HOH MA 8 .   ? 39.930  -0.979  -14.789 1.00 53.76  ? 3192 HOH A O   1 
HETATM 15405 O  O   . HOH MA 8 .   ? 38.015  -28.487 -21.418 1.00 64.65  ? 3193 HOH A O   1 
HETATM 15406 O  O   . HOH MA 8 .   ? 54.101  -25.146 -12.345 1.00 55.05  ? 3194 HOH A O   1 
HETATM 15407 O  O   . HOH MA 8 .   ? 51.342  -6.710  -12.478 1.00 50.82  ? 3195 HOH A O   1 
HETATM 15408 O  O   . HOH MA 8 .   ? 46.529  -9.749  -17.014 1.00 56.41  ? 3196 HOH A O   1 
HETATM 15409 O  O   . HOH MA 8 .   ? 44.889  -7.849  -6.054  1.00 47.13  ? 3197 HOH A O   1 
HETATM 15410 O  O   . HOH MA 8 .   ? 51.590  -6.950  -9.690  1.00 46.27  ? 3198 HOH A O   1 
HETATM 15411 O  O   . HOH MA 8 .   ? 36.780  -13.332 -14.175 1.00 46.82  ? 3199 HOH A O   1 
HETATM 15412 O  O   . HOH MA 8 .   ? 33.709  -23.662 -4.154  1.00 39.63  ? 3200 HOH A O   1 
HETATM 15413 O  O   . HOH MA 8 .   ? 26.963  -26.572 -5.275  1.00 41.54  ? 3201 HOH A O   1 
HETATM 15414 O  O   . HOH MA 8 .   ? 35.418  -31.777 -6.717  1.00 45.59  ? 3202 HOH A O   1 
HETATM 15415 O  O   . HOH MA 8 .   ? 42.123  -33.811 -10.566 1.00 64.81  ? 3203 HOH A O   1 
HETATM 15416 O  O   . HOH MA 8 .   ? 47.228  -31.065 -2.140  1.00 38.44  ? 3204 HOH A O   1 
HETATM 15417 O  O   . HOH MA 8 .   ? 54.981  -13.283 1.298   1.00 56.59  ? 3205 HOH A O   1 
HETATM 15418 O  O   . HOH MA 8 .   ? 48.391  -4.219  -0.905  1.00 48.83  ? 3206 HOH A O   1 
HETATM 15419 O  O   . HOH MA 8 .   ? 33.955  -13.122 -2.533  1.00 54.27  ? 3207 HOH A O   1 
HETATM 15420 O  O   . HOH MA 8 .   ? 35.331  -16.367 5.260   1.00 47.63  ? 3208 HOH A O   1 
HETATM 15421 O  O   . HOH MA 8 .   ? 30.942  -20.882 6.211   1.00 43.96  ? 3209 HOH A O   1 
HETATM 15422 O  O   . HOH MA 8 .   ? 33.913  -21.558 13.156  1.00 46.98  ? 3210 HOH A O   1 
HETATM 15423 O  O   . HOH MA 8 .   ? 31.798  -27.981 16.103  1.00 47.27  ? 3211 HOH A O   1 
HETATM 15424 O  O   . HOH MA 8 .   ? 27.054  -21.394 12.406  1.00 45.78  ? 3212 HOH A O   1 
HETATM 15425 O  O   . HOH MA 8 .   ? 26.850  -32.340 10.565  1.00 49.25  ? 3213 HOH A O   1 
HETATM 15426 O  O   . HOH MA 8 .   ? 25.031  -32.891 4.053   1.00 48.24  ? 3214 HOH A O   1 
HETATM 15427 O  O   . HOH MA 8 .   ? 23.244  -35.113 7.277   1.00 60.16  ? 3215 HOH A O   1 
HETATM 15428 O  O   . HOH MA 8 .   ? 35.600  -36.252 11.693  1.00 49.50  ? 3216 HOH A O   1 
HETATM 15429 O  O   . HOH MA 8 .   ? 39.346  -27.815 14.118  1.00 54.35  ? 3217 HOH A O   1 
HETATM 15430 O  O   . HOH MA 8 .   ? 41.641  -33.970 5.477   1.00 38.46  ? 3218 HOH A O   1 
HETATM 15431 O  O   . HOH MA 8 .   ? 43.562  -33.799 14.704  1.00 54.46  ? 3219 HOH A O   1 
HETATM 15432 O  O   . HOH MA 8 .   ? 55.861  -21.686 5.090   1.00 58.04  ? 3220 HOH A O   1 
HETATM 15433 O  O   . HOH MA 8 .   ? 57.383  -13.861 8.524   1.00 52.70  ? 3221 HOH A O   1 
HETATM 15434 O  O   . HOH MA 8 .   ? 51.872  -12.065 15.162  1.00 44.43  ? 3222 HOH A O   1 
HETATM 15435 O  O   . HOH MA 8 .   ? 58.387  -12.060 11.425  1.00 50.30  ? 3223 HOH A O   1 
HETATM 15436 O  O   . HOH MA 8 .   ? 50.065  -5.584  7.153   1.00 42.73  ? 3224 HOH A O   1 
HETATM 15437 O  O   . HOH MA 8 .   ? 51.908  -5.133  10.208  1.00 50.42  ? 3225 HOH A O   1 
HETATM 15438 O  O   . HOH MA 8 .   ? 53.974  -3.468  11.468  1.00 49.88  ? 3226 HOH A O   1 
HETATM 15439 O  O   . HOH MA 8 .   ? 50.949  -12.745 17.299  1.00 55.01  ? 3227 HOH A O   1 
HETATM 15440 O  O   . HOH MA 8 .   ? 49.137  3.831   10.066  1.00 47.36  ? 3228 HOH A O   1 
HETATM 15441 O  O   . HOH MA 8 .   ? 51.583  -0.695  2.290   1.00 55.18  ? 3229 HOH A O   1 
HETATM 15442 O  O   . HOH MA 8 .   ? 42.232  5.916   11.101  1.00 45.39  ? 3230 HOH A O   1 
HETATM 15443 O  O   . HOH MA 8 .   ? 41.304  -2.116  10.689  1.00 47.58  ? 3231 HOH A O   1 
HETATM 15444 O  O   . HOH MA 8 .   ? 34.063  -13.175 12.150  1.00 61.10  ? 3232 HOH A O   1 
HETATM 15445 O  O   . HOH MA 8 .   ? 52.645  -19.530 22.547  1.00 60.72  ? 3233 HOH A O   1 
HETATM 15446 O  O   . HOH MA 8 .   ? 37.038  2.389   33.382  1.00 60.53  ? 3234 HOH A O   1 
HETATM 15447 O  O   . HOH MA 8 .   ? 39.353  -3.636  15.711  1.00 41.78  ? 3235 HOH A O   1 
HETATM 15448 O  O   . HOH MA 8 .   ? 30.570  -18.585 35.620  1.00 48.83  ? 3236 HOH A O   1 
HETATM 15449 O  O   . HOH MA 8 .   ? 27.996  -7.349  33.576  1.00 50.53  ? 3237 HOH A O   1 
HETATM 15450 O  O   . HOH MA 8 .   ? 26.997  -9.110  33.613  1.00 51.51  ? 3238 HOH A O   1 
HETATM 15451 O  O   . HOH MA 8 .   ? 34.558  0.492   33.564  1.00 58.94  ? 3239 HOH A O   1 
HETATM 15452 O  O   . HOH MA 8 .   ? 35.463  0.815   28.235  1.00 53.72  ? 3240 HOH A O   1 
HETATM 15453 O  O   . HOH MA 8 .   ? 33.957  6.202   26.293  1.00 40.95  ? 3241 HOH A O   1 
HETATM 15454 O  O   . HOH MA 8 .   ? 30.486  -13.720 16.595  1.00 71.81  ? 3242 HOH A O   1 
HETATM 15455 O  O   . HOH MA 8 .   ? 27.563  -23.372 28.062  1.00 63.38  ? 3243 HOH A O   1 
HETATM 15456 O  O   . HOH MA 8 .   ? 23.638  -23.465 20.182  1.00 45.12  ? 3244 HOH A O   1 
HETATM 15457 O  O   . HOH MA 8 .   ? 17.262  -12.197 30.138  1.00 54.53  ? 3245 HOH A O   1 
HETATM 15458 O  O   . HOH MA 8 .   ? 17.981  -3.927  27.174  1.00 56.95  ? 3246 HOH A O   1 
HETATM 15459 O  O   . HOH MA 8 .   ? 18.030  -4.947  14.577  1.00 44.79  ? 3247 HOH A O   1 
HETATM 15460 O  O   . HOH MA 8 .   ? 33.605  -18.559 14.270  1.00 58.96  ? 3248 HOH A O   1 
HETATM 15461 O  O   . HOH MA 8 .   ? 24.969  -24.382 17.927  1.00 48.19  ? 3249 HOH A O   1 
HETATM 15462 O  O   . HOH MA 8 .   ? 24.189  -27.972 12.281  1.00 59.78  ? 3250 HOH A O   1 
HETATM 15463 O  O   . HOH MA 8 .   ? 12.816  -19.105 24.009  1.00 56.92  ? 3251 HOH A O   1 
HETATM 15464 O  O   . HOH MA 8 .   ? 10.145  -25.549 20.174  1.00 64.20  ? 3252 HOH A O   1 
HETATM 15465 O  O   . HOH MA 8 .   ? 3.168   -16.751 19.785  1.00 66.06  ? 3253 HOH A O   1 
HETATM 15466 O  O   . HOH MA 8 .   ? 9.477   -10.081 23.418  1.00 66.41  ? 3254 HOH A O   1 
HETATM 15467 O  O   . HOH MA 8 .   ? 13.287  -9.084  2.962   1.00 46.20  ? 3255 HOH A O   1 
HETATM 15468 O  O   . HOH MA 8 .   ? 25.732  -19.283 2.737   1.00 64.02  ? 3256 HOH A O   1 
HETATM 15469 O  O   . HOH MA 8 .   ? 23.604  -27.947 9.135   1.00 32.59  ? 3257 HOH A O   1 
HETATM 15470 O  O   . HOH MA 8 .   ? 21.274  -34.390 7.641   1.00 48.42  ? 3258 HOH A O   1 
HETATM 15471 O  O   . HOH MA 8 .   ? 3.981   -27.797 7.097   1.00 56.29  ? 3259 HOH A O   1 
HETATM 15472 O  O   . HOH MA 8 .   ? 5.850   -20.987 13.382  1.00 64.70  ? 3260 HOH A O   1 
HETATM 15473 O  O   . HOH MA 8 .   ? 1.527   -17.011 10.516  1.00 64.29  ? 3261 HOH A O   1 
HETATM 15474 O  O   . HOH MA 8 .   ? 12.742  -25.334 -4.088  1.00 52.29  ? 3262 HOH A O   1 
HETATM 15475 O  O   . HOH MA 8 .   ? 8.740   -19.955 -0.608  1.00 52.07  ? 3263 HOH A O   1 
HETATM 15476 O  O   . HOH MA 8 .   ? 28.269  -23.638 -0.550  1.00 41.46  ? 3264 HOH A O   1 
HETATM 15477 O  O   . HOH MA 8 .   ? 34.686  -34.933 -3.939  1.00 40.07  ? 3265 HOH A O   1 
HETATM 15478 O  O   . HOH MA 8 .   ? 47.497  -29.940 4.629   1.00 41.72  ? 3266 HOH A O   1 
HETATM 15479 O  O   . HOH MA 8 .   ? 52.267  -27.273 1.996   1.00 55.84  ? 3267 HOH A O   1 
HETATM 15480 O  O   . HOH MA 8 .   ? 53.672  -29.443 4.427   1.00 64.49  ? 3268 HOH A O   1 
HETATM 15481 O  O   . HOH MA 8 .   ? -9.874  9.099   -20.475 1.00 78.21  ? 3269 HOH A O   1 
HETATM 15482 O  O   . HOH MA 8 .   ? -7.995  14.507  -23.443 1.00 63.63  ? 3270 HOH A O   1 
HETATM 15483 O  O   . HOH MA 8 .   ? 11.046  23.010  -10.044 1.00 38.78  ? 3271 HOH A O   1 
HETATM 15484 O  O   . HOH MA 8 .   ? 9.086   29.437  -10.400 1.00 70.76  ? 3272 HOH A O   1 
HETATM 15485 O  O   . HOH MA 8 .   ? 65.759  -5.732  -17.361 1.00 74.49  ? 3273 HOH A O   1 
HETATM 15486 O  O   . HOH MA 8 .   ? 25.302  -30.270 23.233  1.00 75.54  ? 3274 HOH A O   1 
HETATM 15487 O  O   . HOH MA 8 .   ? 16.312  37.369  -7.661  1.00 70.81  ? 3275 HOH A O   1 
HETATM 15488 O  O   . HOH MA 8 .   ? 14.435  26.769  -19.128 1.00 76.38  ? 3276 HOH A O   1 
HETATM 15489 O  O   . HOH MA 8 .   ? 11.027  28.225  -14.972 1.00 69.27  ? 3277 HOH A O   1 
HETATM 15490 O  O   . HOH MA 8 .   ? 51.679  -20.098 -37.766 1.00 73.71  ? 3278 HOH A O   1 
HETATM 15491 O  O   . HOH NA 8 .   ? 50.754  11.550  54.044  1.00 63.12  ? 3001 HOH C O   1 
HETATM 15492 O  O   . HOH NA 8 .   ? 36.946  13.448  65.986  1.00 57.29  ? 3002 HOH C O   1 
HETATM 15493 O  O   . HOH NA 8 .   ? 34.959  18.176  70.090  1.00 50.07  ? 3003 HOH C O   1 
HETATM 15494 O  O   . HOH NA 8 .   ? 34.484  22.929  62.336  1.00 44.27  ? 3004 HOH C O   1 
HETATM 15495 O  O   . HOH NA 8 .   ? 34.480  21.345  37.867  1.00 45.01  ? 3005 HOH C O   1 
HETATM 15496 O  O   . HOH NA 8 .   ? 36.759  26.274  38.778  1.00 58.55  ? 3006 HOH C O   1 
HETATM 15497 O  O   . HOH NA 8 .   ? 37.286  22.751  36.850  1.00 48.56  ? 3007 HOH C O   1 
HETATM 15498 O  O   . HOH NA 8 .   ? 27.436  22.809  38.928  1.00 31.30  ? 3008 HOH C O   1 
HETATM 15499 O  O   . HOH NA 8 .   ? 34.205  21.307  35.342  1.00 45.88  ? 3009 HOH C O   1 
HETATM 15500 O  O   . HOH NA 8 .   ? 27.255  20.713  35.975  1.00 48.42  ? 3010 HOH C O   1 
HETATM 15501 O  O   . HOH NA 8 .   ? 36.821  16.122  35.698  1.00 55.39  ? 3011 HOH C O   1 
HETATM 15502 O  O   . HOH NA 8 .   ? 35.124  19.287  38.274  1.00 37.65  ? 3012 HOH C O   1 
HETATM 15503 O  O   . HOH NA 8 .   ? 40.652  22.955  43.496  1.00 41.26  ? 3013 HOH C O   1 
HETATM 15504 O  O   . HOH NA 8 .   ? 41.786  33.384  60.511  1.00 62.20  ? 3014 HOH C O   1 
HETATM 15505 O  O   . HOH NA 8 .   ? 53.673  21.651  68.578  1.00 70.65  ? 3015 HOH C O   1 
HETATM 15506 O  O   . HOH NA 8 .   ? 41.138  10.711  55.493  1.00 47.59  ? 3016 HOH C O   1 
HETATM 15507 O  O   . HOH NA 8 .   ? 42.523  13.318  52.478  1.00 40.65  ? 3017 HOH C O   1 
HETATM 15508 O  O   . HOH NA 8 .   ? 35.144  12.614  48.865  1.00 39.27  ? 3018 HOH C O   1 
HETATM 15509 O  O   . HOH NA 8 .   ? 42.643  20.761  44.033  1.00 47.06  ? 3019 HOH C O   1 
HETATM 15510 O  O   . HOH NA 8 .   ? 46.281  30.853  53.327  1.00 61.35  ? 3020 HOH C O   1 
HETATM 15511 O  O   . HOH NA 8 .   ? 43.329  38.220  67.724  1.00 60.33  ? 3021 HOH C O   1 
HETATM 15512 O  O   . HOH NA 8 .   ? 17.793  30.200  47.216  1.00 45.85  ? 3022 HOH C O   1 
HETATM 15513 O  O   . HOH NA 8 .   ? 16.040  33.349  49.501  1.00 49.95  ? 3023 HOH C O   1 
HETATM 15514 O  O   . HOH NA 8 .   ? 33.303  9.231   58.316  1.00 41.26  ? 3024 HOH C O   1 
HETATM 15515 O  O   . HOH NA 8 .   ? 37.074  10.782  44.262  1.00 44.55  ? 3025 HOH C O   1 
HETATM 15516 O  O   . HOH NA 8 .   ? 32.967  3.219   45.240  1.00 55.53  ? 3026 HOH C O   1 
HETATM 15517 O  O   . HOH NA 8 .   ? 33.650  4.801   43.821  1.00 60.29  ? 3027 HOH C O   1 
HETATM 15518 O  O   . HOH NA 8 .   ? 21.279  10.269  51.620  1.00 42.01  ? 3028 HOH C O   1 
HETATM 15519 O  O   . HOH NA 8 .   ? 31.195  7.309   56.848  1.00 57.04  ? 3029 HOH C O   1 
HETATM 15520 O  O   . HOH NA 8 .   ? 31.994  13.619  48.886  1.00 40.86  ? 3030 HOH C O   1 
HETATM 15521 O  O   . HOH NA 8 .   ? 21.236  16.199  53.311  1.00 32.80  ? 3031 HOH C O   1 
HETATM 15522 O  O   . HOH NA 8 .   ? 24.183  18.439  53.716  1.00 32.03  ? 3032 HOH C O   1 
HETATM 15523 O  O   . HOH NA 8 .   ? 22.210  12.688  57.053  1.00 45.44  ? 3033 HOH C O   1 
HETATM 15524 O  O   . HOH NA 8 .   ? 23.593  11.091  56.740  1.00 41.63  ? 3034 HOH C O   1 
HETATM 15525 O  O   . HOH NA 8 .   ? 23.799  16.515  56.562  1.00 37.23  ? 3035 HOH C O   1 
HETATM 15526 O  O   . HOH NA 8 .   ? 29.831  16.175  59.215  1.00 31.29  ? 3036 HOH C O   1 
HETATM 15527 O  O   . HOH NA 8 .   ? 20.561  15.225  64.646  1.00 41.47  ? 3037 HOH C O   1 
HETATM 15528 O  O   . HOH NA 8 .   ? 30.689  16.336  62.735  1.00 41.39  ? 3038 HOH C O   1 
HETATM 15529 O  O   . HOH NA 8 .   ? 36.426  9.986   63.526  1.00 52.00  ? 3039 HOH C O   1 
HETATM 15530 O  O   . HOH NA 8 .   ? 31.514  22.032  63.862  1.00 39.64  ? 3040 HOH C O   1 
HETATM 15531 O  O   . HOH NA 8 .   ? 24.376  27.096  66.483  1.00 40.55  ? 3041 HOH C O   1 
HETATM 15532 O  O   . HOH NA 8 .   ? 25.120  23.761  64.626  1.00 45.34  ? 3042 HOH C O   1 
HETATM 15533 O  O   . HOH NA 8 .   ? 23.379  25.698  70.570  1.00 52.60  ? 3043 HOH C O   1 
HETATM 15534 O  O   . HOH NA 8 .   ? 32.225  35.859  62.522  1.00 58.34  ? 3044 HOH C O   1 
HETATM 15535 O  O   . HOH NA 8 .   ? 27.076  31.031  53.259  1.00 42.43  ? 3045 HOH C O   1 
HETATM 15536 O  O   . HOH NA 8 .   ? 20.038  32.772  37.509  1.00 51.00  ? 3046 HOH C O   1 
HETATM 15537 O  O   . HOH NA 8 .   ? 25.817  28.096  31.557  1.00 43.41  ? 3047 HOH C O   1 
HETATM 15538 O  O   . HOH NA 8 .   ? 23.706  29.452  28.930  1.00 44.29  ? 3048 HOH C O   1 
HETATM 15539 O  O   . HOH NA 8 .   ? 18.614  29.863  44.845  1.00 45.87  ? 3049 HOH C O   1 
HETATM 15540 O  O   . HOH NA 8 .   ? 17.763  32.968  48.368  1.00 44.55  ? 3050 HOH C O   1 
HETATM 15541 O  O   . HOH NA 8 .   ? 21.721  38.771  41.350  1.00 54.76  ? 3051 HOH C O   1 
HETATM 15542 O  O   . HOH NA 8 .   ? 32.494  37.640  35.635  1.00 65.47  ? 3052 HOH C O   1 
HETATM 15543 O  O   . HOH NA 8 .   ? 34.623  32.187  31.763  1.00 54.76  ? 3053 HOH C O   1 
HETATM 15544 O  O   . HOH NA 8 .   ? 31.866  30.407  32.352  1.00 45.12  ? 3054 HOH C O   1 
HETATM 15545 O  O   . HOH NA 8 .   ? 31.252  28.987  25.285  1.00 63.20  ? 3055 HOH C O   1 
HETATM 15546 O  O   . HOH NA 8 .   ? 26.106  37.299  54.526  1.00 57.19  ? 3056 HOH C O   1 
HETATM 15547 O  O   . HOH NA 8 .   ? 21.263  19.147  64.183  1.00 34.69  ? 3057 HOH C O   1 
HETATM 15548 O  O   . HOH NA 8 .   ? 11.952  27.452  41.209  1.00 57.64  ? 3058 HOH C O   1 
HETATM 15549 O  O   . HOH NA 8 .   ? 1.875   32.869  52.652  1.00 54.75  ? 3059 HOH C O   1 
HETATM 15550 O  O   . HOH NA 8 .   ? 15.046  28.769  47.734  1.00 45.06  ? 3060 HOH C O   1 
HETATM 15551 O  O   . HOH NA 8 .   ? 11.356  15.743  43.648  1.00 42.25  ? 3061 HOH C O   1 
HETATM 15552 O  O   . HOH NA 8 .   ? 8.189   8.243   41.445  1.00 60.30  ? 3062 HOH C O   1 
HETATM 15553 O  O   . HOH NA 8 .   ? 14.155  31.094  49.387  1.00 54.69  ? 3063 HOH C O   1 
HETATM 15554 O  O   . HOH NA 8 .   ? 18.914  5.155   45.951  1.00 50.62  ? 3064 HOH C O   1 
HETATM 15555 O  O   . HOH NA 8 .   ? 19.898  4.878   55.892  1.00 51.18  ? 3065 HOH C O   1 
HETATM 15556 O  O   . HOH NA 8 .   ? 19.516  -15.376 36.447  1.00 72.13  ? 3066 HOH C O   1 
HETATM 15557 O  O   . HOH NA 8 .   ? 6.380   6.069   65.383  1.00 69.33  ? 3067 HOH C O   1 
HETATM 15558 O  O   . HOH NA 8 .   ? 10.080  10.054  64.351  1.00 52.42  ? 3068 HOH C O   1 
HETATM 15559 O  O   . HOH NA 8 .   ? 34.738  18.478  75.161  1.00 46.10  ? 3069 HOH C O   1 
HETATM 15560 O  O   . HOH NA 8 .   ? 27.826  15.864  75.302  1.00 46.77  ? 3070 HOH C O   1 
HETATM 15561 O  O   . HOH NA 8 .   ? 32.891  14.255  75.412  1.00 65.51  ? 3071 HOH C O   1 
HETATM 15562 O  O   . HOH NA 8 .   ? 28.146  14.302  78.774  1.00 53.42  ? 3072 HOH C O   1 
HETATM 15563 O  O   . HOH NA 8 .   ? 1.046   19.222  69.281  1.00 68.79  ? 3073 HOH C O   1 
HETATM 15564 O  O   . HOH NA 8 .   ? 6.273   6.041   78.609  1.00 59.50  ? 3074 HOH C O   1 
HETATM 15565 O  O   . HOH NA 8 .   ? 19.863  5.577   79.852  1.00 50.47  ? 3075 HOH C O   1 
HETATM 15566 O  O   . HOH NA 8 .   ? 28.038  2.889   70.783  1.00 52.97  ? 3076 HOH C O   1 
HETATM 15567 O  O   . HOH NA 8 .   ? 36.901  2.089   69.840  1.00 54.92  ? 3077 HOH C O   1 
HETATM 15568 O  O   . HOH NA 8 .   ? 33.868  1.582   65.722  1.00 59.22  ? 3078 HOH C O   1 
HETATM 15569 O  O   . HOH NA 8 .   ? 34.168  3.216   62.117  1.00 51.44  ? 3079 HOH C O   1 
HETATM 15570 O  O   . HOH NA 8 .   ? 24.234  -1.698  66.487  1.00 51.59  ? 3080 HOH C O   1 
HETATM 15571 O  O   . HOH NA 8 .   ? 16.321  1.185   65.064  1.00 62.33  ? 3081 HOH C O   1 
HETATM 15572 O  O   . HOH NA 8 .   ? 17.354  3.955   82.742  1.00 52.29  ? 3082 HOH C O   1 
HETATM 15573 O  O   . HOH NA 8 .   ? 1.441   26.202  75.009  1.00 59.26  ? 3083 HOH C O   1 
HETATM 15574 O  O   . HOH NA 8 .   ? 15.025  11.690  93.195  1.00 58.52  ? 3084 HOH C O   1 
HETATM 15575 O  O   . HOH NA 8 .   ? 11.315  16.829  97.859  1.00 74.53  ? 3085 HOH C O   1 
HETATM 15576 O  O   . HOH NA 8 .   ? 18.775  10.911  97.847  1.00 47.35  ? 3086 HOH C O   1 
HETATM 15577 O  O   . HOH NA 8 .   ? -1.904  -5.607  95.123  1.00 75.87  ? 3087 HOH C O   1 
HETATM 15578 O  O   . HOH NA 8 .   ? 11.474  6.167   98.600  1.00 64.05  ? 3088 HOH C O   1 
HETATM 15579 O  O   . HOH NA 8 .   ? -5.934  -15.593 89.107  1.00 72.86  ? 3089 HOH C O   1 
HETATM 15580 O  O   . HOH NA 8 .   ? -11.747 7.206   84.124  1.00 70.28  ? 3090 HOH C O   1 
HETATM 15581 O  O   . HOH NA 8 .   ? 1.128   0.929   82.682  1.00 72.88  ? 3091 HOH C O   1 
HETATM 15582 O  O   . HOH NA 8 .   ? 4.853   -16.731 83.231  1.00 60.74  ? 3092 HOH C O   1 
HETATM 15583 O  O   . HOH NA 8 .   ? 7.422   -16.052 80.320  1.00 66.78  ? 3093 HOH C O   1 
HETATM 15584 O  O   . HOH NA 8 .   ? 6.664   -12.384 66.078  1.00 70.72  ? 3094 HOH C O   1 
HETATM 15585 O  O   . HOH NA 8 .   ? 12.006  -23.970 68.838  1.00 54.55  ? 3095 HOH C O   1 
HETATM 15586 O  O   . HOH NA 8 .   ? -3.163  -27.971 61.146  1.00 69.55  ? 3096 HOH C O   1 
HETATM 15587 O  O   . HOH NA 8 .   ? -12.509 -14.987 43.284  1.00 71.78  ? 3097 HOH C O   1 
HETATM 15588 O  O   . HOH NA 8 .   ? 0.880   -0.112  32.382  1.00 70.50  ? 3098 HOH C O   1 
HETATM 15589 O  O   . HOH NA 8 .   ? 8.293   -21.084 40.716  1.00 68.38  ? 3099 HOH C O   1 
HETATM 15590 O  O   . HOH NA 8 .   ? 7.976   -21.372 43.620  1.00 64.02  ? 3100 HOH C O   1 
HETATM 15591 O  O   . HOH NA 8 .   ? 12.867  -20.204 37.358  1.00 65.49  ? 3101 HOH C O   1 
HETATM 15592 O  O   . HOH NA 8 .   ? 11.457  -21.052 40.746  1.00 69.21  ? 3102 HOH C O   1 
HETATM 15593 O  O   . HOH NA 8 .   ? 20.114  -13.544 37.192  1.00 62.62  ? 3103 HOH C O   1 
HETATM 15594 O  O   . HOH NA 8 .   ? 17.385  4.958   39.231  1.00 48.45  ? 3104 HOH C O   1 
HETATM 15595 O  O   . HOH NA 8 .   ? 11.878  3.335   39.224  1.00 63.23  ? 3105 HOH C O   1 
HETATM 15596 O  O   . HOH NA 8 .   ? 18.138  0.514   51.715  1.00 51.39  ? 3106 HOH C O   1 
HETATM 15597 O  O   . HOH NA 8 .   ? 14.232  -5.133  62.226  1.00 60.19  ? 3107 HOH C O   1 
HETATM 15598 O  O   . HOH NA 8 .   ? 30.174  -12.799 51.168  1.00 70.97  ? 3108 HOH C O   1 
HETATM 15599 O  O   . HOH NA 8 .   ? 20.973  5.824   57.595  1.00 53.83  ? 3109 HOH C O   1 
HETATM 15600 O  O   . HOH NA 8 .   ? 13.221  -19.990 63.915  1.00 59.69  ? 3110 HOH C O   1 
HETATM 15601 O  O   . HOH NA 8 .   ? 20.936  -25.293 61.047  1.00 54.90  ? 3111 HOH C O   1 
HETATM 15602 O  O   . HOH NA 8 .   ? 34.360  -13.912 65.152  1.00 74.73  ? 3112 HOH C O   1 
HETATM 15603 O  O   . HOH NA 8 .   ? 11.126  -14.572 76.804  1.00 67.28  ? 3113 HOH C O   1 
HETATM 15604 O  O   . HOH NA 8 .   ? 9.057   -12.500 72.702  1.00 65.32  ? 3114 HOH C O   1 
HETATM 15605 O  O   . HOH NA 8 .   ? 3.166   -23.145 79.103  1.00 72.90  ? 3115 HOH C O   1 
HETATM 15606 O  O   . HOH NA 8 .   ? 6.144   -22.418 81.715  1.00 69.56  ? 3116 HOH C O   1 
HETATM 15607 O  O   . HOH NA 8 .   ? 30.329  28.390  18.039  1.00 62.03  ? 3117 HOH C O   1 
HETATM 15608 O  O   . HOH NA 8 .   ? 32.615  25.230  31.218  1.00 40.79  ? 3118 HOH C O   1 
HETATM 15609 O  O   . HOH NA 8 .   ? 32.028  18.595  25.936  1.00 39.89  ? 3119 HOH C O   1 
HETATM 15610 O  O   . HOH NA 8 .   ? 21.016  36.870  66.175  1.00 63.47  ? 3120 HOH C O   1 
HETATM 15611 O  O   . HOH NA 8 .   ? -3.255  19.847  31.447  1.00 63.14  ? 3121 HOH C O   1 
HETATM 15612 O  O   . HOH NA 8 .   ? 28.558  29.785  19.043  1.00 59.15  ? 3122 HOH C O   1 
HETATM 15613 O  O   . HOH NA 8 .   ? 8.922   -28.186 50.760  1.00 75.67  ? 3123 HOH C O   1 
HETATM 15614 O  O   . HOH NA 8 .   ? 16.889  38.093  60.910  1.00 63.84  ? 3124 HOH C O   1 
HETATM 15615 O  O   . HOH NA 8 .   ? -1.093  22.276  31.358  1.00 58.03  ? 3125 HOH C O   1 
# 
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   1   ?   ?   ?   A . n 
A 1 2   PHE 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   ?   ?   ?   A . n 
A 1 7   MET 7   7   ?   ?   ?   A . n 
A 1 8   VAL 8   8   ?   ?   ?   A . n 
A 1 9   ASN 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  HIS 11  11  ?   ?   ?   A . n 
A 1 12  ARG 12  12  ?   ?   ?   A . n 
A 1 13  LYS 13  13  ?   ?   ?   A . n 
A 1 14  PRO 14  14  ?   ?   ?   A . n 
A 1 15  MET 15  15  ?   ?   ?   A . n 
A 1 16  PHE 16  16  ?   ?   ?   A . n 
A 1 17  ASN 17  17  ?   ?   ?   A . n 
A 1 18  ILE 18  18  ?   ?   ?   A . n 
A 1 19  HIS 19  19  ?   ?   ?   A . n 
A 1 20  ARG 20  20  ?   ?   ?   A . n 
A 1 21  GLY 21  21  ?   ?   ?   A . n 
A 1 22  PHE 22  22  ?   ?   ?   A . n 
A 1 23  TYR 23  23  ?   ?   ?   A . n 
A 1 24  CYS 24  24  ?   ?   ?   A . n 
A 1 25  LEU 25  25  ?   ?   ?   A . n 
A 1 26  THR 26  26  ?   ?   ?   A . n 
A 1 27  ALA 27  27  ?   ?   ?   A . n 
A 1 28  ILE 28  28  ?   ?   ?   A . n 
A 1 29  LEU 29  29  ?   ?   ?   A . n 
A 1 30  PRO 30  30  ?   ?   ?   A . n 
A 1 31  GLN 31  31  ?   ?   ?   A . n 
A 1 32  ILE 32  32  ?   ?   ?   A . n 
A 1 33  CYS 33  33  ?   ?   ?   A . n 
A 1 34  ILE 34  34  ?   ?   ?   A . n 
A 1 35  CYS 35  35  ?   ?   ?   A . n 
A 1 36  SER 36  36  ?   ?   ?   A . n 
A 1 37  GLN 37  37  ?   ?   ?   A . n 
A 1 38  PHE 38  38  ?   ?   ?   A . n 
A 1 39  SER 39  39  ?   ?   ?   A . n 
A 1 40  VAL 40  40  ?   ?   ?   A . n 
A 1 41  PRO 41  41  ?   ?   ?   A . n 
A 1 42  SER 42  42  ?   ?   ?   A . n 
A 1 43  SER 43  43  ?   ?   ?   A . n 
A 1 44  TYR 44  44  ?   ?   ?   A . n 
A 1 45  HIS 45  45  ?   ?   ?   A . n 
A 1 46  PHE 46  46  ?   ?   ?   A . n 
A 1 47  THR 47  47  ?   ?   ?   A . n 
A 1 48  GLU 48  48  ?   ?   ?   A . n 
A 1 49  ASP 49  49  ?   ?   ?   A . n 
A 1 50  PRO 50  50  ?   ?   ?   A . n 
A 1 51  GLY 51  51  ?   ?   ?   A . n 
A 1 52  ALA 52  52  ?   ?   ?   A . n 
A 1 53  PHE 53  53  ?   ?   ?   A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  TRP 64  64  64  TRP TRP A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  HIS 83  83  83  HIS HIS A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 GLN 106 106 106 GLN GLN A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 TYR 142 142 142 TYR TYR A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 HIS 145 145 145 HIS HIS A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 THR 183 183 183 THR THR A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 ILE 193 193 193 ILE ILE A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 MET 206 206 206 MET MET A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 CYS 210 210 210 CYS CYS A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 HIS 230 230 230 HIS HIS A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 HIS 252 252 252 HIS HIS A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 THR 256 256 256 THR THR A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 MET 259 259 259 MET MET A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 TYR 266 266 266 TYR TYR A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 CYS 269 269 269 CYS CYS A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 HIS 272 272 272 HIS HIS A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 PHE 277 277 277 PHE PHE A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 ASN 294 294 294 ASN ASN A . n 
A 1 295 GLN 295 295 295 GLN GLN A . n 
A 1 296 THR 296 296 296 THR THR A . n 
A 1 297 HIS 297 297 297 HIS HIS A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 GLN 301 301 301 GLN GLN A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 ASP 308 308 308 ASP ASP A . n 
A 1 309 PHE 309 309 309 PHE PHE A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 TYR 313 313 313 TYR TYR A . n 
A 1 314 PHE 314 314 314 PHE PHE A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 PRO 319 319 319 PRO PRO A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 ASP 330 330 330 ASP ASP A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 PRO 333 333 333 PRO PRO A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 MET 336 336 336 MET MET A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 TRP 339 339 339 TRP TRP A . n 
A 1 340 GLY 340 340 340 GLY GLY A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 TYR 344 344 344 TYR TYR A . n 
A 1 345 ARG 345 345 345 ARG ARG A . n 
A 1 346 GLU 346 346 346 GLU GLU A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 PRO 353 353 353 PRO PRO A . n 
A 1 354 LYS 354 354 354 LYS LYS A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 ASP 360 360 360 ASP ASP A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 TRP 363 363 363 TRP TRP A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 ARG 366 366 366 ARG ARG A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 HIS 370 370 370 HIS HIS A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 ALA 373 373 373 ALA ALA A . n 
A 1 374 HIS 374 374 374 HIS HIS A . n 
A 1 375 GLN 375 375 375 GLN GLN A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 PHE 377 377 377 PHE PHE A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 ASN 379 379 379 ASN ASN A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 MET 383 383 383 MET MET A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 TRP 385 385 385 TRP TRP A . n 
A 1 386 TRP 386 386 386 TRP TRP A . n 
A 1 387 ASN 387 387 387 ASN ASN A . n 
A 1 388 ASP 388 388 388 ASP ASP A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 TRP 390 390 390 TRP TRP A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 ASN 392 392 392 ASN ASN A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 PHE 395 395 395 PHE PHE A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 LYS 397 397 397 LYS LYS A . n 
A 1 398 TYR 398 398 398 TYR TYR A . n 
A 1 399 MET 399 399 399 MET MET A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 ALA 403 403 403 ALA ALA A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ASN 405 405 405 ASN ASN A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TYR 408 408 408 TYR TYR A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 GLU 410 410 410 GLU GLU A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 GLN 412 412 412 GLN GLN A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 TYR 416 416 416 TYR TYR A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 VAL 420 420 420 VAL VAL A . n 
A 1 421 CYS 421 421 421 CYS CYS A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 THR 426 426 426 THR THR A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 SER 429 429 429 SER SER A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 ASN 431 431 431 ASN ASN A . n 
A 1 432 SER 432 432 432 SER SER A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 PRO 435 435 435 PRO PRO A . n 
A 1 436 ILE 436 436 436 ILE ILE A . n 
A 1 437 SER 437 437 437 SER SER A . n 
A 1 438 LYS 438 438 438 LYS LYS A . n 
A 1 439 PRO 439 439 439 PRO PRO A . n 
A 1 440 ALA 440 440 440 ALA ALA A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 PRO 443 443 443 PRO PRO A . n 
A 1 444 THR 444 444 444 THR THR A . n 
A 1 445 GLN 445 445 445 GLN GLN A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 GLN 447 447 447 GLN GLN A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 MET 449 449 449 MET MET A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 ASP 451 451 451 ASP ASP A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 VAL 453 453 453 VAL VAL A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 TYR 455 455 455 TYR TYR A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 GLY 458 458 458 GLY GLY A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 CYS 460 460 460 CYS CYS A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 LEU 462 462 462 LEU LEU A . n 
A 1 463 ASN 463 463 463 ASN ASN A . n 
A 1 464 MET 464 464 464 MET MET A . n 
A 1 465 LEU 465 465 465 LEU LEU A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 ASP 467 467 467 ASP ASP A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 LEU 469 469 469 LEU LEU A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 GLU 471 471 471 GLU GLU A . n 
A 1 472 GLU 472 472 472 GLU GLU A . n 
A 1 473 LYS 473 473 473 LYS LYS A . n 
A 1 474 PHE 474 474 474 PHE PHE A . n 
A 1 475 GLN 475 475 475 GLN GLN A . n 
A 1 476 LYS 476 476 476 LYS LYS A . n 
A 1 477 GLY 477 477 477 GLY GLY A . n 
A 1 478 ILE 478 478 478 ILE ILE A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 GLN 480 480 480 GLN GLN A . n 
A 1 481 TYR 481 481 481 TYR TYR A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 LYS 483 483 483 LYS LYS A . n 
A 1 484 LYS 484 484 484 LYS LYS A . n 
A 1 485 PHE 485 485 485 PHE PHE A . n 
A 1 486 SER 486 486 486 SER SER A . n 
A 1 487 TYR 487 487 487 TYR TYR A . n 
A 1 488 ARG 488 488 488 ARG ARG A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 ALA 490 490 490 ALA ALA A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 ASN 492 492 492 ASN ASN A . n 
A 1 493 ASP 493 493 493 ASP ASP A . n 
A 1 494 ASP 494 494 494 ASP ASP A . n 
A 1 495 LEU 495 495 495 LEU LEU A . n 
A 1 496 TRP 496 496 496 TRP TRP A . n 
A 1 497 SER 497 497 497 SER SER A . n 
A 1 498 SER 498 498 498 SER SER A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 SER 500 500 500 SER SER A . n 
A 1 501 ASN 501 501 501 ASN ASN A . n 
A 1 502 SER 502 502 502 SER SER A . n 
A 1 503 CYS 503 503 503 CYS CYS A . n 
A 1 504 LEU 504 504 504 LEU LEU A . n 
A 1 505 GLU 505 505 505 GLU GLU A . n 
A 1 506 SER 506 506 506 SER SER A . n 
A 1 507 ASP 507 507 507 ASP ASP A . n 
A 1 508 PHE 508 508 508 PHE PHE A . n 
A 1 509 THR 509 509 509 THR THR A . n 
A 1 510 SER 510 510 510 SER SER A . n 
A 1 511 GLY 511 511 511 GLY GLY A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 VAL 513 513 513 VAL VAL A . n 
A 1 514 CYS 514 514 514 CYS CYS A . n 
A 1 515 HIS 515 515 515 HIS HIS A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 ASP 517 517 517 ASP ASP A . n 
A 1 518 PRO 518 518 518 PRO PRO A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 MET 520 520 520 MET MET A . n 
A 1 521 THR 521 521 521 THR THR A . n 
A 1 522 SER 522 522 522 SER SER A . n 
A 1 523 ASN 523 523 523 ASN ASN A . n 
A 1 524 MET 524 524 524 MET MET A . n 
A 1 525 LEU 525 525 525 LEU LEU A . n 
A 1 526 ALA 526 526 526 ALA ALA A . n 
A 1 527 PHE 527 527 527 PHE PHE A . n 
A 1 528 LEU 528 528 528 LEU LEU A . n 
A 1 529 GLY 529 529 529 GLY GLY A . n 
A 1 530 GLU 530 530 530 GLU GLU A . n 
A 1 531 ASN 531 531 531 ASN ASN A . n 
A 1 532 ALA 532 532 532 ALA ALA A . n 
A 1 533 GLU 533 533 533 GLU GLU A . n 
A 1 534 VAL 534 534 534 VAL VAL A . n 
A 1 535 LYS 535 535 535 LYS LYS A . n 
A 1 536 GLU 536 536 536 GLU GLU A . n 
A 1 537 MET 537 537 537 MET MET A . n 
A 1 538 MET 538 538 538 MET MET A . n 
A 1 539 THR 539 539 539 THR THR A . n 
A 1 540 THR 540 540 540 THR THR A . n 
A 1 541 TRP 541 541 541 TRP TRP A . n 
A 1 542 THR 542 542 542 THR THR A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 GLN 544 544 544 GLN GLN A . n 
A 1 545 LYS 545 545 545 LYS LYS A . n 
A 1 546 GLY 546 546 546 GLY GLY A . n 
A 1 547 ILE 547 547 547 ILE ILE A . n 
A 1 548 PRO 548 548 548 PRO PRO A . n 
A 1 549 LEU 549 549 549 LEU LEU A . n 
A 1 550 LEU 550 550 550 LEU LEU A . n 
A 1 551 VAL 551 551 551 VAL VAL A . n 
A 1 552 VAL 552 552 552 VAL VAL A . n 
A 1 553 LYS 553 553 553 LYS LYS A . n 
A 1 554 GLN 554 554 554 GLN GLN A . n 
A 1 555 ASP 555 555 555 ASP ASP A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 CYS 557 557 557 CYS CYS A . n 
A 1 558 SER 558 558 558 SER SER A . n 
A 1 559 LEU 559 559 559 LEU LEU A . n 
A 1 560 ARG 560 560 560 ARG ARG A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 GLN 562 562 562 GLN GLN A . n 
A 1 563 GLN 563 563 563 GLN GLN A . n 
A 1 564 GLU 564 564 564 GLU GLU A . n 
A 1 565 ARG 565 565 565 ARG ARG A . n 
A 1 566 PHE 566 566 566 PHE PHE A . n 
A 1 567 LEU 567 567 567 LEU LEU A . n 
A 1 568 GLN 568 568 568 GLN GLN A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 VAL 570 570 570 VAL VAL A . n 
A 1 571 PHE 571 571 571 PHE PHE A . n 
A 1 572 GLN 572 572 572 GLN GLN A . n 
A 1 573 GLU 573 573 573 GLU GLU A . n 
A 1 574 ASP 574 574 574 ASP ASP A . n 
A 1 575 PRO 575 575 575 PRO PRO A . n 
A 1 576 GLU 576 576 576 GLU GLU A . n 
A 1 577 TRP 577 577 577 TRP TRP A . n 
A 1 578 ARG 578 578 578 ARG ARG A . n 
A 1 579 ALA 579 579 579 ALA ALA A . n 
A 1 580 LEU 580 580 580 LEU LEU A . n 
A 1 581 GLN 581 581 581 GLN GLN A . n 
A 1 582 GLU 582 582 582 GLU GLU A . n 
A 1 583 ARG 583 583 583 ARG ARG A . n 
A 1 584 TYR 584 584 584 TYR TYR A . n 
A 1 585 LEU 585 585 585 LEU LEU A . n 
A 1 586 TRP 586 586 586 TRP TRP A . n 
A 1 587 HIS 587 587 587 HIS HIS A . n 
A 1 588 ILE 588 588 588 ILE ILE A . n 
A 1 589 PRO 589 589 589 PRO PRO A . n 
A 1 590 LEU 590 590 590 LEU LEU A . n 
A 1 591 THR 591 591 591 THR THR A . n 
A 1 592 TYR 592 592 592 TYR TYR A . n 
A 1 593 SER 593 593 593 SER SER A . n 
A 1 594 THR 594 594 594 THR THR A . n 
A 1 595 SER 595 595 595 SER SER A . n 
A 1 596 SER 596 596 596 SER SER A . n 
A 1 597 SER 597 597 597 SER SER A . n 
A 1 598 ASN 598 598 598 ASN ASN A . n 
A 1 599 VAL 599 599 599 VAL VAL A . n 
A 1 600 ILE 600 600 600 ILE ILE A . n 
A 1 601 HIS 601 601 601 HIS HIS A . n 
A 1 602 ARG 602 602 602 ARG ARG A . n 
A 1 603 HIS 603 603 603 HIS HIS A . n 
A 1 604 ILE 604 604 604 ILE ILE A . n 
A 1 605 LEU 605 605 605 LEU LEU A . n 
A 1 606 LYS 606 606 606 LYS LYS A . n 
A 1 607 SER 607 607 607 SER SER A . n 
A 1 608 LYS 608 608 608 LYS LYS A . n 
A 1 609 THR 609 609 609 THR THR A . n 
A 1 610 ASP 610 610 610 ASP ASP A . n 
A 1 611 THR 611 611 611 THR THR A . n 
A 1 612 LEU 612 612 612 LEU LEU A . n 
A 1 613 ASP 613 613 613 ASP ASP A . n 
A 1 614 LEU 614 614 614 LEU LEU A . n 
A 1 615 PRO 615 615 615 PRO PRO A . n 
A 1 616 GLU 616 616 616 GLU GLU A . n 
A 1 617 LYS 617 617 617 LYS LYS A . n 
A 1 618 THR 618 618 618 THR THR A . n 
A 1 619 SER 619 619 619 SER SER A . n 
A 1 620 TRP 620 620 620 TRP TRP A . n 
A 1 621 VAL 621 621 621 VAL VAL A . n 
A 1 622 LYS 622 622 622 LYS LYS A . n 
A 1 623 PHE 623 623 623 PHE PHE A . n 
A 1 624 ASN 624 624 624 ASN ASN A . n 
A 1 625 VAL 625 625 625 VAL VAL A . n 
A 1 626 ASP 626 626 626 ASP ASP A . n 
A 1 627 SER 627 627 627 SER SER A . n 
A 1 628 ASN 628 628 628 ASN ASN A . n 
A 1 629 GLY 629 629 629 GLY GLY A . n 
A 1 630 TYR 630 630 630 TYR TYR A . n 
A 1 631 TYR 631 631 631 TYR TYR A . n 
A 1 632 ILE 632 632 632 ILE ILE A . n 
A 1 633 VAL 633 633 633 VAL VAL A . n 
A 1 634 HIS 634 634 634 HIS HIS A . n 
A 1 635 TYR 635 635 635 TYR TYR A . n 
A 1 636 GLU 636 636 636 GLU GLU A . n 
A 1 637 GLY 637 637 637 GLY GLY A . n 
A 1 638 HIS 638 638 638 HIS HIS A . n 
A 1 639 GLY 639 639 639 GLY GLY A . n 
A 1 640 TRP 640 640 640 TRP TRP A . n 
A 1 641 ASP 641 641 641 ASP ASP A . n 
A 1 642 GLN 642 642 642 GLN GLN A . n 
A 1 643 LEU 643 643 643 LEU LEU A . n 
A 1 644 ILE 644 644 644 ILE ILE A . n 
A 1 645 THR 645 645 645 THR THR A . n 
A 1 646 GLN 646 646 646 GLN GLN A . n 
A 1 647 LEU 647 647 647 LEU LEU A . n 
A 1 648 ASN 648 648 648 ASN ASN A . n 
A 1 649 GLN 649 649 649 GLN GLN A . n 
A 1 650 ASN 650 650 650 ASN ASN A . n 
A 1 651 HIS 651 651 651 HIS HIS A . n 
A 1 652 THR 652 652 652 THR THR A . n 
A 1 653 LEU 653 653 653 LEU LEU A . n 
A 1 654 LEU 654 654 654 LEU LEU A . n 
A 1 655 ARG 655 655 655 ARG ARG A . n 
A 1 656 PRO 656 656 656 PRO PRO A . n 
A 1 657 LYS 657 657 657 LYS LYS A . n 
A 1 658 ASP 658 658 658 ASP ASP A . n 
A 1 659 ARG 659 659 659 ARG ARG A . n 
A 1 660 VAL 660 660 660 VAL VAL A . n 
A 1 661 GLY 661 661 661 GLY GLY A . n 
A 1 662 LEU 662 662 662 LEU LEU A . n 
A 1 663 ILE 663 663 663 ILE ILE A . n 
A 1 664 HIS 664 664 664 HIS HIS A . n 
A 1 665 ASP 665 665 665 ASP ASP A . n 
A 1 666 VAL 666 666 666 VAL VAL A . n 
A 1 667 PHE 667 667 667 PHE PHE A . n 
A 1 668 GLN 668 668 668 GLN GLN A . n 
A 1 669 LEU 669 669 669 LEU LEU A . n 
A 1 670 VAL 670 670 670 VAL VAL A . n 
A 1 671 GLY 671 671 671 GLY GLY A . n 
A 1 672 ALA 672 672 672 ALA ALA A . n 
A 1 673 GLY 673 673 673 GLY GLY A . n 
A 1 674 ARG 674 674 674 ARG ARG A . n 
A 1 675 LEU 675 675 675 LEU LEU A . n 
A 1 676 THR 676 676 676 THR THR A . n 
A 1 677 LEU 677 677 677 LEU LEU A . n 
A 1 678 ASP 678 678 678 ASP ASP A . n 
A 1 679 LYS 679 679 679 LYS LYS A . n 
A 1 680 ALA 680 680 680 ALA ALA A . n 
A 1 681 LEU 681 681 681 LEU LEU A . n 
A 1 682 ASP 682 682 682 ASP ASP A . n 
A 1 683 MET 683 683 683 MET MET A . n 
A 1 684 THR 684 684 684 THR THR A . n 
A 1 685 TYR 685 685 685 TYR TYR A . n 
A 1 686 TYR 686 686 686 TYR TYR A . n 
A 1 687 LEU 687 687 687 LEU LEU A . n 
A 1 688 GLN 688 688 688 GLN GLN A . n 
A 1 689 HIS 689 689 689 HIS HIS A . n 
A 1 690 GLU 690 690 690 GLU GLU A . n 
A 1 691 THR 691 691 691 THR THR A . n 
A 1 692 SER 692 692 692 SER SER A . n 
A 1 693 SER 693 693 693 SER SER A . n 
A 1 694 PRO 694 694 694 PRO PRO A . n 
A 1 695 ALA 695 695 695 ALA ALA A . n 
A 1 696 LEU 696 696 696 LEU LEU A . n 
A 1 697 LEU 697 697 697 LEU LEU A . n 
A 1 698 GLU 698 698 698 GLU GLU A . n 
A 1 699 GLY 699 699 699 GLY GLY A . n 
A 1 700 LEU 700 700 700 LEU LEU A . n 
A 1 701 SER 701 701 701 SER SER A . n 
A 1 702 TYR 702 702 702 TYR TYR A . n 
A 1 703 LEU 703 703 703 LEU LEU A . n 
A 1 704 GLU 704 704 704 GLU GLU A . n 
A 1 705 SER 705 705 705 SER SER A . n 
A 1 706 PHE 706 706 706 PHE PHE A . n 
A 1 707 TYR 707 707 707 TYR TYR A . n 
A 1 708 HIS 708 708 708 HIS HIS A . n 
A 1 709 MET 709 709 709 MET MET A . n 
A 1 710 MET 710 710 710 MET MET A . n 
A 1 711 ASP 711 711 711 ASP ASP A . n 
A 1 712 ARG 712 712 712 ARG ARG A . n 
A 1 713 ARG 713 713 713 ARG ARG A . n 
A 1 714 ASN 714 714 714 ASN ASN A . n 
A 1 715 ILE 715 715 715 ILE ILE A . n 
A 1 716 SER 716 716 716 SER SER A . n 
A 1 717 ASP 717 717 717 ASP ASP A . n 
A 1 718 ILE 718 718 718 ILE ILE A . n 
A 1 719 SER 719 719 719 SER SER A . n 
A 1 720 GLU 720 720 720 GLU GLU A . n 
A 1 721 ASN 721 721 721 ASN ASN A . n 
A 1 722 LEU 722 722 722 LEU LEU A . n 
A 1 723 LYS 723 723 723 LYS LYS A . n 
A 1 724 ARG 724 724 724 ARG ARG A . n 
A 1 725 TYR 725 725 725 TYR TYR A . n 
A 1 726 LEU 726 726 726 LEU LEU A . n 
A 1 727 LEU 727 727 727 LEU LEU A . n 
A 1 728 GLN 728 728 728 GLN GLN A . n 
A 1 729 TYR 729 729 729 TYR TYR A . n 
A 1 730 PHE 730 730 730 PHE PHE A . n 
A 1 731 LYS 731 731 731 LYS LYS A . n 
A 1 732 PRO 732 732 732 PRO PRO A . n 
A 1 733 VAL 733 733 733 VAL VAL A . n 
A 1 734 ILE 734 734 734 ILE ILE A . n 
A 1 735 ASP 735 735 735 ASP ASP A . n 
A 1 736 ARG 736 736 736 ARG ARG A . n 
A 1 737 GLN 737 737 737 GLN GLN A . n 
A 1 738 SER 738 738 738 SER SER A . n 
A 1 739 TRP 739 739 739 TRP TRP A . n 
A 1 740 SER 740 740 740 SER SER A . n 
A 1 741 ASP 741 741 741 ASP ASP A . n 
A 1 742 LYS 742 742 742 LYS LYS A . n 
A 1 743 GLY 743 743 743 GLY GLY A . n 
A 1 744 SER 744 744 744 SER SER A . n 
A 1 745 VAL 745 745 745 VAL VAL A . n 
A 1 746 TRP 746 746 746 TRP TRP A . n 
A 1 747 ASP 747 747 747 ASP ASP A . n 
A 1 748 ARG 748 748 748 ARG ARG A . n 
A 1 749 MET 749 749 749 MET MET A . n 
A 1 750 LEU 750 750 750 LEU LEU A . n 
A 1 751 ARG 751 751 751 ARG ARG A . n 
A 1 752 SER 752 752 752 SER SER A . n 
A 1 753 ALA 753 753 753 ALA ALA A . n 
A 1 754 LEU 754 754 754 LEU LEU A . n 
A 1 755 LEU 755 755 755 LEU LEU A . n 
A 1 756 LYS 756 756 756 LYS LYS A . n 
A 1 757 LEU 757 757 757 LEU LEU A . n 
A 1 758 ALA 758 758 758 ALA ALA A . n 
A 1 759 CYS 759 759 759 CYS CYS A . n 
A 1 760 ASP 760 760 760 ASP ASP A . n 
A 1 761 LEU 761 761 761 LEU LEU A . n 
A 1 762 ASN 762 762 762 ASN ASN A . n 
A 1 763 HIS 763 763 763 HIS HIS A . n 
A 1 764 ALA 764 764 764 ALA ALA A . n 
A 1 765 PRO 765 765 765 PRO PRO A . n 
A 1 766 CYS 766 766 766 CYS CYS A . n 
A 1 767 ILE 767 767 767 ILE ILE A . n 
A 1 768 GLN 768 768 768 GLN GLN A . n 
A 1 769 LYS 769 769 769 LYS LYS A . n 
A 1 770 ALA 770 770 770 ALA ALA A . n 
A 1 771 ALA 771 771 771 ALA ALA A . n 
A 1 772 GLU 772 772 772 GLU GLU A . n 
A 1 773 LEU 773 773 773 LEU LEU A . n 
A 1 774 PHE 774 774 774 PHE PHE A . n 
A 1 775 SER 775 775 775 SER SER A . n 
A 1 776 GLN 776 776 776 GLN GLN A . n 
A 1 777 TRP 777 777 777 TRP TRP A . n 
A 1 778 MET 778 778 778 MET MET A . n 
A 1 779 GLU 779 779 779 GLU GLU A . n 
A 1 780 SER 780 780 780 SER SER A . n 
A 1 781 SER 781 781 781 SER SER A . n 
A 1 782 GLY 782 782 782 GLY GLY A . n 
A 1 783 LYS 783 783 783 LYS LYS A . n 
A 1 784 LEU 784 784 784 LEU LEU A . n 
A 1 785 ASN 785 785 785 ASN ASN A . n 
A 1 786 ILE 786 786 786 ILE ILE A . n 
A 1 787 PRO 787 787 787 PRO PRO A . n 
A 1 788 THR 788 788 788 THR THR A . n 
A 1 789 ASP 789 789 789 ASP ASP A . n 
A 1 790 VAL 790 790 790 VAL VAL A . n 
A 1 791 LEU 791 791 791 LEU LEU A . n 
A 1 792 LYS 792 792 792 LYS LYS A . n 
A 1 793 ILE 793 793 793 ILE ILE A . n 
A 1 794 VAL 794 794 794 VAL VAL A . n 
A 1 795 TYR 795 795 795 TYR TYR A . n 
A 1 796 SER 796 796 796 SER SER A . n 
A 1 797 VAL 797 797 797 VAL VAL A . n 
A 1 798 GLY 798 798 798 GLY GLY A . n 
A 1 799 ALA 799 799 799 ALA ALA A . n 
A 1 800 GLN 800 800 800 GLN GLN A . n 
A 1 801 THR 801 801 801 THR THR A . n 
A 1 802 THR 802 802 802 THR THR A . n 
A 1 803 ALA 803 803 803 ALA ALA A . n 
A 1 804 GLY 804 804 804 GLY GLY A . n 
A 1 805 TRP 805 805 805 TRP TRP A . n 
A 1 806 ASN 806 806 806 ASN ASN A . n 
A 1 807 TYR 807 807 807 TYR TYR A . n 
A 1 808 LEU 808 808 808 LEU LEU A . n 
A 1 809 LEU 809 809 809 LEU LEU A . n 
A 1 810 GLU 810 810 810 GLU GLU A . n 
A 1 811 GLN 811 811 811 GLN GLN A . n 
A 1 812 TYR 812 812 812 TYR TYR A . n 
A 1 813 GLU 813 813 813 GLU GLU A . n 
A 1 814 LEU 814 814 814 LEU LEU A . n 
A 1 815 SER 815 815 815 SER SER A . n 
A 1 816 MET 816 816 816 MET MET A . n 
A 1 817 SER 817 817 817 SER SER A . n 
A 1 818 SER 818 818 818 SER SER A . n 
A 1 819 ALA 819 819 819 ALA ALA A . n 
A 1 820 GLU 820 820 820 GLU GLU A . n 
A 1 821 GLN 821 821 821 GLN GLN A . n 
A 1 822 ASN 822 822 822 ASN ASN A . n 
A 1 823 LYS 823 823 823 LYS LYS A . n 
A 1 824 ILE 824 824 824 ILE ILE A . n 
A 1 825 LEU 825 825 825 LEU LEU A . n 
A 1 826 TYR 826 826 826 TYR TYR A . n 
A 1 827 ALA 827 827 827 ALA ALA A . n 
A 1 828 LEU 828 828 828 LEU LEU A . n 
A 1 829 SER 829 829 829 SER SER A . n 
A 1 830 THR 830 830 830 THR THR A . n 
A 1 831 SER 831 831 831 SER SER A . n 
A 1 832 LYS 832 832 832 LYS LYS A . n 
A 1 833 HIS 833 833 833 HIS HIS A . n 
A 1 834 GLN 834 834 834 GLN GLN A . n 
A 1 835 GLU 835 835 835 GLU GLU A . n 
A 1 836 LYS 836 836 836 LYS LYS A . n 
A 1 837 LEU 837 837 837 LEU LEU A . n 
A 1 838 LEU 838 838 838 LEU LEU A . n 
A 1 839 LYS 839 839 839 LYS LYS A . n 
A 1 840 LEU 840 840 840 LEU LEU A . n 
A 1 841 ILE 841 841 841 ILE ILE A . n 
A 1 842 GLU 842 842 842 GLU GLU A . n 
A 1 843 LEU 843 843 843 LEU LEU A . n 
A 1 844 GLY 844 844 844 GLY GLY A . n 
A 1 845 MET 845 845 845 MET MET A . n 
A 1 846 GLU 846 846 846 GLU GLU A . n 
A 1 847 GLY 847 847 847 GLY GLY A . n 
A 1 848 LYS 848 848 848 LYS LYS A . n 
A 1 849 VAL 849 849 849 VAL VAL A . n 
A 1 850 ILE 850 850 850 ILE ILE A . n 
A 1 851 LYS 851 851 851 LYS LYS A . n 
A 1 852 THR 852 852 852 THR THR A . n 
A 1 853 GLN 853 853 853 GLN GLN A . n 
A 1 854 ASN 854 854 854 ASN ASN A . n 
A 1 855 LEU 855 855 855 LEU LEU A . n 
A 1 856 ALA 856 856 856 ALA ALA A . n 
A 1 857 ALA 857 857 857 ALA ALA A . n 
A 1 858 LEU 858 858 858 LEU LEU A . n 
A 1 859 LEU 859 859 859 LEU LEU A . n 
A 1 860 HIS 860 860 860 HIS HIS A . n 
A 1 861 ALA 861 861 861 ALA ALA A . n 
A 1 862 ILE 862 862 862 ILE ILE A . n 
A 1 863 ALA 863 863 863 ALA ALA A . n 
A 1 864 ARG 864 864 864 ARG ARG A . n 
A 1 865 ARG 865 865 865 ARG ARG A . n 
A 1 866 PRO 866 866 866 PRO PRO A . n 
A 1 867 LYS 867 867 867 LYS LYS A . n 
A 1 868 GLY 868 868 868 GLY GLY A . n 
A 1 869 GLN 869 869 869 GLN GLN A . n 
A 1 870 GLN 870 870 870 GLN GLN A . n 
A 1 871 LEU 871 871 871 LEU LEU A . n 
A 1 872 ALA 872 872 872 ALA ALA A . n 
A 1 873 TRP 873 873 873 TRP TRP A . n 
A 1 874 ASP 874 874 874 ASP ASP A . n 
A 1 875 PHE 875 875 875 PHE PHE A . n 
A 1 876 VAL 876 876 876 VAL VAL A . n 
A 1 877 ARG 877 877 877 ARG ARG A . n 
A 1 878 GLU 878 878 878 GLU GLU A . n 
A 1 879 ASN 879 879 879 ASN ASN A . n 
A 1 880 TRP 880 880 880 TRP TRP A . n 
A 1 881 THR 881 881 881 THR THR A . n 
A 1 882 HIS 882 882 882 HIS HIS A . n 
A 1 883 LEU 883 883 883 LEU LEU A . n 
A 1 884 LEU 884 884 884 LEU LEU A . n 
A 1 885 LYS 885 885 885 LYS LYS A . n 
A 1 886 LYS 886 886 886 LYS LYS A . n 
A 1 887 PHE 887 887 887 PHE PHE A . n 
A 1 888 ASP 888 888 888 ASP ASP A . n 
A 1 889 LEU 889 889 889 LEU LEU A . n 
A 1 890 GLY 890 890 890 GLY GLY A . n 
A 1 891 SER 891 891 891 SER SER A . n 
A 1 892 TYR 892 892 892 TYR TYR A . n 
A 1 893 ASP 893 893 893 ASP ASP A . n 
A 1 894 ILE 894 894 894 ILE ILE A . n 
A 1 895 ARG 895 895 895 ARG ARG A . n 
A 1 896 MET 896 896 896 MET MET A . n 
A 1 897 ILE 897 897 897 ILE ILE A . n 
A 1 898 ILE 898 898 898 ILE ILE A . n 
A 1 899 SER 899 899 899 SER SER A . n 
A 1 900 GLY 900 900 900 GLY GLY A . n 
A 1 901 THR 901 901 901 THR THR A . n 
A 1 902 THR 902 902 902 THR THR A . n 
A 1 903 ALA 903 903 903 ALA ALA A . n 
A 1 904 HIS 904 904 904 HIS HIS A . n 
A 1 905 PHE 905 905 905 PHE PHE A . n 
A 1 906 SER 906 906 906 SER SER A . n 
A 1 907 SER 907 907 907 SER SER A . n 
A 1 908 LYS 908 908 908 LYS LYS A . n 
A 1 909 ASP 909 909 909 ASP ASP A . n 
A 1 910 LYS 910 910 910 LYS LYS A . n 
A 1 911 LEU 911 911 911 LEU LEU A . n 
A 1 912 GLN 912 912 912 GLN GLN A . n 
A 1 913 GLU 913 913 913 GLU GLU A . n 
A 1 914 VAL 914 914 914 VAL VAL A . n 
A 1 915 LYS 915 915 915 LYS LYS A . n 
A 1 916 LEU 916 916 916 LEU LEU A . n 
A 1 917 PHE 917 917 917 PHE PHE A . n 
A 1 918 PHE 918 918 918 PHE PHE A . n 
A 1 919 GLU 919 919 919 GLU GLU A . n 
A 1 920 SER 920 920 920 SER SER A . n 
A 1 921 LEU 921 921 921 LEU LEU A . n 
A 1 922 GLU 922 922 922 GLU GLU A . n 
A 1 923 ALA 923 923 923 ALA ALA A . n 
A 1 924 GLN 924 924 924 GLN GLN A . n 
A 1 925 GLY 925 925 925 GLY GLY A . n 
A 1 926 SER 926 926 926 SER SER A . n 
A 1 927 HIS 927 927 927 HIS HIS A . n 
A 1 928 LEU 928 928 928 LEU LEU A . n 
A 1 929 ASP 929 929 929 ASP ASP A . n 
A 1 930 ILE 930 930 930 ILE ILE A . n 
A 1 931 PHE 931 931 931 PHE PHE A . n 
A 1 932 GLN 932 932 932 GLN GLN A . n 
A 1 933 THR 933 933 933 THR THR A . n 
A 1 934 VAL 934 934 934 VAL VAL A . n 
A 1 935 LEU 935 935 935 LEU LEU A . n 
A 1 936 GLU 936 936 936 GLU GLU A . n 
A 1 937 THR 937 937 937 THR THR A . n 
A 1 938 ILE 938 938 938 ILE ILE A . n 
A 1 939 THR 939 939 939 THR THR A . n 
A 1 940 LYS 940 940 940 LYS LYS A . n 
A 1 941 ASN 941 941 941 ASN ASN A . n 
A 1 942 ILE 942 942 942 ILE ILE A . n 
A 1 943 LYS 943 943 943 LYS LYS A . n 
A 1 944 TRP 944 944 944 TRP TRP A . n 
A 1 945 LEU 945 945 945 LEU LEU A . n 
A 1 946 GLU 946 946 946 GLU GLU A . n 
A 1 947 LYS 947 947 947 LYS LYS A . n 
A 1 948 ASN 948 948 948 ASN ASN A . n 
A 1 949 LEU 949 949 949 LEU LEU A . n 
A 1 950 PRO 950 950 950 PRO PRO A . n 
A 1 951 THR 951 951 951 THR THR A . n 
A 1 952 LEU 952 952 952 LEU LEU A . n 
A 1 953 ARG 953 953 953 ARG ARG A . n 
A 1 954 THR 954 954 954 THR THR A . n 
A 1 955 TRP 955 955 955 TRP TRP A . n 
A 1 956 LEU 956 956 956 LEU LEU A . n 
A 1 957 MET 957 957 957 MET MET A . n 
A 1 958 VAL 958 958 958 VAL VAL A . n 
A 1 959 ASN 959 959 959 ASN ASN A . n 
A 1 960 THR 960 960 960 THR THR A . n 
A 1 961 ARG 961 961 961 ARG ARG A . n 
A 1 962 HIS 962 962 962 HIS HIS A . n 
A 1 963 HIS 963 963 963 HIS HIS A . n 
A 1 964 HIS 964 964 964 HIS HIS A . n 
A 1 965 HIS 965 965 ?   ?   ?   A . n 
A 1 966 HIS 966 966 ?   ?   ?   A . n 
A 1 967 HIS 967 967 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   C . n 
B 1 2   PHE 2   2   ?   ?   ?   C . n 
B 1 3   HIS 3   3   ?   ?   ?   C . n 
B 1 4   SER 4   4   ?   ?   ?   C . n 
B 1 5   SER 5   5   ?   ?   ?   C . n 
B 1 6   ALA 6   6   ?   ?   ?   C . n 
B 1 7   MET 7   7   ?   ?   ?   C . n 
B 1 8   VAL 8   8   ?   ?   ?   C . n 
B 1 9   ASN 9   9   ?   ?   ?   C . n 
B 1 10  SER 10  10  ?   ?   ?   C . n 
B 1 11  HIS 11  11  ?   ?   ?   C . n 
B 1 12  ARG 12  12  ?   ?   ?   C . n 
B 1 13  LYS 13  13  ?   ?   ?   C . n 
B 1 14  PRO 14  14  ?   ?   ?   C . n 
B 1 15  MET 15  15  ?   ?   ?   C . n 
B 1 16  PHE 16  16  ?   ?   ?   C . n 
B 1 17  ASN 17  17  ?   ?   ?   C . n 
B 1 18  ILE 18  18  ?   ?   ?   C . n 
B 1 19  HIS 19  19  ?   ?   ?   C . n 
B 1 20  ARG 20  20  ?   ?   ?   C . n 
B 1 21  GLY 21  21  ?   ?   ?   C . n 
B 1 22  PHE 22  22  ?   ?   ?   C . n 
B 1 23  TYR 23  23  ?   ?   ?   C . n 
B 1 24  CYS 24  24  ?   ?   ?   C . n 
B 1 25  LEU 25  25  ?   ?   ?   C . n 
B 1 26  THR 26  26  ?   ?   ?   C . n 
B 1 27  ALA 27  27  ?   ?   ?   C . n 
B 1 28  ILE 28  28  ?   ?   ?   C . n 
B 1 29  LEU 29  29  ?   ?   ?   C . n 
B 1 30  PRO 30  30  ?   ?   ?   C . n 
B 1 31  GLN 31  31  ?   ?   ?   C . n 
B 1 32  ILE 32  32  ?   ?   ?   C . n 
B 1 33  CYS 33  33  ?   ?   ?   C . n 
B 1 34  ILE 34  34  ?   ?   ?   C . n 
B 1 35  CYS 35  35  ?   ?   ?   C . n 
B 1 36  SER 36  36  ?   ?   ?   C . n 
B 1 37  GLN 37  37  ?   ?   ?   C . n 
B 1 38  PHE 38  38  ?   ?   ?   C . n 
B 1 39  SER 39  39  ?   ?   ?   C . n 
B 1 40  VAL 40  40  ?   ?   ?   C . n 
B 1 41  PRO 41  41  ?   ?   ?   C . n 
B 1 42  SER 42  42  ?   ?   ?   C . n 
B 1 43  SER 43  43  ?   ?   ?   C . n 
B 1 44  TYR 44  44  ?   ?   ?   C . n 
B 1 45  HIS 45  45  ?   ?   ?   C . n 
B 1 46  PHE 46  46  ?   ?   ?   C . n 
B 1 47  THR 47  47  ?   ?   ?   C . n 
B 1 48  GLU 48  48  ?   ?   ?   C . n 
B 1 49  ASP 49  49  ?   ?   ?   C . n 
B 1 50  PRO 50  50  ?   ?   ?   C . n 
B 1 51  GLY 51  51  ?   ?   ?   C . n 
B 1 52  ALA 52  52  ?   ?   ?   C . n 
B 1 53  PHE 53  53  ?   ?   ?   C . n 
B 1 54  PRO 54  54  54  PRO PRO C . n 
B 1 55  VAL 55  55  55  VAL VAL C . n 
B 1 56  ALA 56  56  56  ALA ALA C . n 
B 1 57  THR 57  57  57  THR THR C . n 
B 1 58  ASN 58  58  58  ASN ASN C . n 
B 1 59  GLY 59  59  59  GLY GLY C . n 
B 1 60  GLU 60  60  60  GLU GLU C . n 
B 1 61  ARG 61  61  61  ARG ARG C . n 
B 1 62  PHE 62  62  62  PHE PHE C . n 
B 1 63  PRO 63  63  63  PRO PRO C . n 
B 1 64  TRP 64  64  64  TRP TRP C . n 
B 1 65  GLN 65  65  65  GLN GLN C . n 
B 1 66  GLU 66  66  66  GLU GLU C . n 
B 1 67  LEU 67  67  67  LEU LEU C . n 
B 1 68  ARG 68  68  68  ARG ARG C . n 
B 1 69  LEU 69  69  69  LEU LEU C . n 
B 1 70  PRO 70  70  70  PRO PRO C . n 
B 1 71  SER 71  71  71  SER SER C . n 
B 1 72  VAL 72  72  72  VAL VAL C . n 
B 1 73  VAL 73  73  73  VAL VAL C . n 
B 1 74  ILE 74  74  74  ILE ILE C . n 
B 1 75  PRO 75  75  75  PRO PRO C . n 
B 1 76  LEU 76  76  76  LEU LEU C . n 
B 1 77  HIS 77  77  77  HIS HIS C . n 
B 1 78  TYR 78  78  78  TYR TYR C . n 
B 1 79  ASP 79  79  79  ASP ASP C . n 
B 1 80  LEU 80  80  80  LEU LEU C . n 
B 1 81  PHE 81  81  81  PHE PHE C . n 
B 1 82  VAL 82  82  82  VAL VAL C . n 
B 1 83  HIS 83  83  83  HIS HIS C . n 
B 1 84  PRO 84  84  84  PRO PRO C . n 
B 1 85  ASN 85  85  85  ASN ASN C . n 
B 1 86  LEU 86  86  86  LEU LEU C . n 
B 1 87  THR 87  87  87  THR THR C . n 
B 1 88  SER 88  88  88  SER SER C . n 
B 1 89  LEU 89  89  89  LEU LEU C . n 
B 1 90  ASP 90  90  90  ASP ASP C . n 
B 1 91  PHE 91  91  91  PHE PHE C . n 
B 1 92  VAL 92  92  92  VAL VAL C . n 
B 1 93  ALA 93  93  93  ALA ALA C . n 
B 1 94  SER 94  94  94  SER SER C . n 
B 1 95  GLU 95  95  95  GLU GLU C . n 
B 1 96  LYS 96  96  96  LYS LYS C . n 
B 1 97  ILE 97  97  97  ILE ILE C . n 
B 1 98  GLU 98  98  98  GLU GLU C . n 
B 1 99  VAL 99  99  99  VAL VAL C . n 
B 1 100 LEU 100 100 100 LEU LEU C . n 
B 1 101 VAL 101 101 101 VAL VAL C . n 
B 1 102 SER 102 102 102 SER SER C . n 
B 1 103 ASN 103 103 103 ASN ASN C . n 
B 1 104 ALA 104 104 104 ALA ALA C . n 
B 1 105 THR 105 105 105 THR THR C . n 
B 1 106 GLN 106 106 106 GLN GLN C . n 
B 1 107 PHE 107 107 107 PHE PHE C . n 
B 1 108 ILE 108 108 108 ILE ILE C . n 
B 1 109 ILE 109 109 109 ILE ILE C . n 
B 1 110 LEU 110 110 110 LEU LEU C . n 
B 1 111 HIS 111 111 111 HIS HIS C . n 
B 1 112 SER 112 112 112 SER SER C . n 
B 1 113 LYS 113 113 113 LYS LYS C . n 
B 1 114 ASP 114 114 114 ASP ASP C . n 
B 1 115 LEU 115 115 115 LEU LEU C . n 
B 1 116 GLU 116 116 116 GLU GLU C . n 
B 1 117 ILE 117 117 117 ILE ILE C . n 
B 1 118 THR 118 118 118 THR THR C . n 
B 1 119 ASN 119 119 119 ASN ASN C . n 
B 1 120 ALA 120 120 120 ALA ALA C . n 
B 1 121 THR 121 121 121 THR THR C . n 
B 1 122 LEU 122 122 122 LEU LEU C . n 
B 1 123 GLN 123 123 123 GLN GLN C . n 
B 1 124 SER 124 124 124 SER SER C . n 
B 1 125 GLU 125 125 125 GLU GLU C . n 
B 1 126 GLU 126 126 126 GLU GLU C . n 
B 1 127 ASP 127 127 127 ASP ASP C . n 
B 1 128 SER 128 128 128 SER SER C . n 
B 1 129 ARG 129 129 129 ARG ARG C . n 
B 1 130 TYR 130 130 130 TYR TYR C . n 
B 1 131 MET 131 131 131 MET MET C . n 
B 1 132 LYS 132 132 132 LYS LYS C . n 
B 1 133 PRO 133 133 133 PRO PRO C . n 
B 1 134 GLY 134 134 134 GLY GLY C . n 
B 1 135 LYS 135 135 135 LYS LYS C . n 
B 1 136 GLU 136 136 136 GLU GLU C . n 
B 1 137 LEU 137 137 137 LEU LEU C . n 
B 1 138 LYS 138 138 138 LYS LYS C . n 
B 1 139 VAL 139 139 139 VAL VAL C . n 
B 1 140 LEU 140 140 140 LEU LEU C . n 
B 1 141 SER 141 141 141 SER SER C . n 
B 1 142 TYR 142 142 142 TYR TYR C . n 
B 1 143 PRO 143 143 143 PRO PRO C . n 
B 1 144 ALA 144 144 144 ALA ALA C . n 
B 1 145 HIS 145 145 145 HIS HIS C . n 
B 1 146 GLU 146 146 146 GLU GLU C . n 
B 1 147 GLN 147 147 147 GLN GLN C . n 
B 1 148 ILE 148 148 148 ILE ILE C . n 
B 1 149 ALA 149 149 149 ALA ALA C . n 
B 1 150 LEU 150 150 150 LEU LEU C . n 
B 1 151 LEU 151 151 151 LEU LEU C . n 
B 1 152 VAL 152 152 152 VAL VAL C . n 
B 1 153 PRO 153 153 153 PRO PRO C . n 
B 1 154 GLU 154 154 154 GLU GLU C . n 
B 1 155 LYS 155 155 155 LYS LYS C . n 
B 1 156 LEU 156 156 156 LEU LEU C . n 
B 1 157 THR 157 157 157 THR THR C . n 
B 1 158 PRO 158 158 158 PRO PRO C . n 
B 1 159 HIS 159 159 159 HIS HIS C . n 
B 1 160 LEU 160 160 160 LEU LEU C . n 
B 1 161 LYS 161 161 161 LYS LYS C . n 
B 1 162 TYR 162 162 162 TYR TYR C . n 
B 1 163 TYR 163 163 163 TYR TYR C . n 
B 1 164 VAL 164 164 164 VAL VAL C . n 
B 1 165 ALA 165 165 165 ALA ALA C . n 
B 1 166 MET 166 166 166 MET MET C . n 
B 1 167 ASP 167 167 167 ASP ASP C . n 
B 1 168 PHE 168 168 168 PHE PHE C . n 
B 1 169 GLN 169 169 169 GLN GLN C . n 
B 1 170 ALA 170 170 170 ALA ALA C . n 
B 1 171 LYS 171 171 171 LYS LYS C . n 
B 1 172 LEU 172 172 172 LEU LEU C . n 
B 1 173 GLY 173 173 173 GLY GLY C . n 
B 1 174 ASP 174 174 174 ASP ASP C . n 
B 1 175 GLY 175 175 175 GLY GLY C . n 
B 1 176 PHE 176 176 176 PHE PHE C . n 
B 1 177 GLU 177 177 177 GLU GLU C . n 
B 1 178 GLY 178 178 178 GLY GLY C . n 
B 1 179 PHE 179 179 179 PHE PHE C . n 
B 1 180 TYR 180 180 180 TYR TYR C . n 
B 1 181 LYS 181 181 181 LYS LYS C . n 
B 1 182 SER 182 182 182 SER SER C . n 
B 1 183 THR 183 183 183 THR THR C . n 
B 1 184 TYR 184 184 184 TYR TYR C . n 
B 1 185 ARG 185 185 185 ARG ARG C . n 
B 1 186 THR 186 186 186 THR THR C . n 
B 1 187 LEU 187 187 187 LEU LEU C . n 
B 1 188 GLY 188 188 188 GLY GLY C . n 
B 1 189 GLY 189 189 189 GLY GLY C . n 
B 1 190 GLU 190 190 190 GLU GLU C . n 
B 1 191 THR 191 191 191 THR THR C . n 
B 1 192 ARG 192 192 192 ARG ARG C . n 
B 1 193 ILE 193 193 193 ILE ILE C . n 
B 1 194 LEU 194 194 194 LEU LEU C . n 
B 1 195 ALA 195 195 195 ALA ALA C . n 
B 1 196 VAL 196 196 196 VAL VAL C . n 
B 1 197 THR 197 197 197 THR THR C . n 
B 1 198 ASP 198 198 198 ASP ASP C . n 
B 1 199 PHE 199 199 199 PHE PHE C . n 
B 1 200 GLU 200 200 200 GLU GLU C . n 
B 1 201 PRO 201 201 201 PRO PRO C . n 
B 1 202 THR 202 202 202 THR THR C . n 
B 1 203 GLN 203 203 203 GLN GLN C . n 
B 1 204 ALA 204 204 204 ALA ALA C . n 
B 1 205 ARG 205 205 205 ARG ARG C . n 
B 1 206 MET 206 206 206 MET MET C . n 
B 1 207 ALA 207 207 207 ALA ALA C . n 
B 1 208 PHE 208 208 208 PHE PHE C . n 
B 1 209 PRO 209 209 209 PRO PRO C . n 
B 1 210 CYS 210 210 210 CYS CYS C . n 
B 1 211 PHE 211 211 211 PHE PHE C . n 
B 1 212 ASP 212 212 212 ASP ASP C . n 
B 1 213 GLU 213 213 213 GLU GLU C . n 
B 1 214 PRO 214 214 214 PRO PRO C . n 
B 1 215 LEU 215 215 215 LEU LEU C . n 
B 1 216 PHE 216 216 216 PHE PHE C . n 
B 1 217 LYS 217 217 217 LYS LYS C . n 
B 1 218 ALA 218 218 218 ALA ALA C . n 
B 1 219 ASN 219 219 219 ASN ASN C . n 
B 1 220 PHE 220 220 220 PHE PHE C . n 
B 1 221 SER 221 221 221 SER SER C . n 
B 1 222 ILE 222 222 222 ILE ILE C . n 
B 1 223 LYS 223 223 223 LYS LYS C . n 
B 1 224 ILE 224 224 224 ILE ILE C . n 
B 1 225 ARG 225 225 225 ARG ARG C . n 
B 1 226 ARG 226 226 226 ARG ARG C . n 
B 1 227 GLU 227 227 227 GLU GLU C . n 
B 1 228 SER 228 228 228 SER SER C . n 
B 1 229 ARG 229 229 229 ARG ARG C . n 
B 1 230 HIS 230 230 230 HIS HIS C . n 
B 1 231 ILE 231 231 231 ILE ILE C . n 
B 1 232 ALA 232 232 232 ALA ALA C . n 
B 1 233 LEU 233 233 233 LEU LEU C . n 
B 1 234 SER 234 234 234 SER SER C . n 
B 1 235 ASN 235 235 235 ASN ASN C . n 
B 1 236 MET 236 236 236 MET MET C . n 
B 1 237 PRO 237 237 237 PRO PRO C . n 
B 1 238 LYS 238 238 238 LYS LYS C . n 
B 1 239 VAL 239 239 239 VAL VAL C . n 
B 1 240 LYS 240 240 240 LYS LYS C . n 
B 1 241 THR 241 241 241 THR THR C . n 
B 1 242 ILE 242 242 242 ILE ILE C . n 
B 1 243 GLU 243 243 243 GLU GLU C . n 
B 1 244 LEU 244 244 244 LEU LEU C . n 
B 1 245 GLU 245 245 245 GLU GLU C . n 
B 1 246 GLY 246 246 246 GLY GLY C . n 
B 1 247 GLY 247 247 247 GLY GLY C . n 
B 1 248 LEU 248 248 248 LEU LEU C . n 
B 1 249 LEU 249 249 249 LEU LEU C . n 
B 1 250 GLU 250 250 250 GLU GLU C . n 
B 1 251 ASP 251 251 251 ASP ASP C . n 
B 1 252 HIS 252 252 252 HIS HIS C . n 
B 1 253 PHE 253 253 253 PHE PHE C . n 
B 1 254 GLU 254 254 254 GLU GLU C . n 
B 1 255 THR 255 255 255 THR THR C . n 
B 1 256 THR 256 256 256 THR THR C . n 
B 1 257 VAL 257 257 257 VAL VAL C . n 
B 1 258 LYS 258 258 258 LYS LYS C . n 
B 1 259 MET 259 259 259 MET MET C . n 
B 1 260 SER 260 260 260 SER SER C . n 
B 1 261 THR 261 261 261 THR THR C . n 
B 1 262 TYR 262 262 262 TYR TYR C . n 
B 1 263 LEU 263 263 263 LEU LEU C . n 
B 1 264 VAL 264 264 264 VAL VAL C . n 
B 1 265 ALA 265 265 265 ALA ALA C . n 
B 1 266 TYR 266 266 266 TYR TYR C . n 
B 1 267 ILE 267 267 267 ILE ILE C . n 
B 1 268 VAL 268 268 268 VAL VAL C . n 
B 1 269 CYS 269 269 269 CYS CYS C . n 
B 1 270 ASP 270 270 270 ASP ASP C . n 
B 1 271 PHE 271 271 271 PHE PHE C . n 
B 1 272 HIS 272 272 272 HIS HIS C . n 
B 1 273 SER 273 273 273 SER SER C . n 
B 1 274 LEU 274 274 274 LEU LEU C . n 
B 1 275 SER 275 275 275 SER SER C . n 
B 1 276 GLY 276 276 276 GLY GLY C . n 
B 1 277 PHE 277 277 277 PHE PHE C . n 
B 1 278 THR 278 278 278 THR THR C . n 
B 1 279 SER 279 279 279 SER SER C . n 
B 1 280 SER 280 280 280 SER SER C . n 
B 1 281 GLY 281 281 281 GLY GLY C . n 
B 1 282 VAL 282 282 282 VAL VAL C . n 
B 1 283 LYS 283 283 283 LYS LYS C . n 
B 1 284 VAL 284 284 284 VAL VAL C . n 
B 1 285 SER 285 285 285 SER SER C . n 
B 1 286 ILE 286 286 286 ILE ILE C . n 
B 1 287 TYR 287 287 287 TYR TYR C . n 
B 1 288 ALA 288 288 288 ALA ALA C . n 
B 1 289 SER 289 289 289 SER SER C . n 
B 1 290 PRO 290 290 290 PRO PRO C . n 
B 1 291 ASP 291 291 291 ASP ASP C . n 
B 1 292 LYS 292 292 292 LYS LYS C . n 
B 1 293 ARG 293 293 293 ARG ARG C . n 
B 1 294 ASN 294 294 294 ASN ASN C . n 
B 1 295 GLN 295 295 295 GLN GLN C . n 
B 1 296 THR 296 296 296 THR THR C . n 
B 1 297 HIS 297 297 297 HIS HIS C . n 
B 1 298 TYR 298 298 298 TYR TYR C . n 
B 1 299 ALA 299 299 299 ALA ALA C . n 
B 1 300 LEU 300 300 300 LEU LEU C . n 
B 1 301 GLN 301 301 301 GLN GLN C . n 
B 1 302 ALA 302 302 302 ALA ALA C . n 
B 1 303 SER 303 303 303 SER SER C . n 
B 1 304 LEU 304 304 304 LEU LEU C . n 
B 1 305 LYS 305 305 305 LYS LYS C . n 
B 1 306 LEU 306 306 306 LEU LEU C . n 
B 1 307 LEU 307 307 307 LEU LEU C . n 
B 1 308 ASP 308 308 308 ASP ASP C . n 
B 1 309 PHE 309 309 309 PHE PHE C . n 
B 1 310 TYR 310 310 310 TYR TYR C . n 
B 1 311 GLU 311 311 311 GLU GLU C . n 
B 1 312 LYS 312 312 312 LYS LYS C . n 
B 1 313 TYR 313 313 313 TYR TYR C . n 
B 1 314 PHE 314 314 314 PHE PHE C . n 
B 1 315 ASP 315 315 315 ASP ASP C . n 
B 1 316 ILE 316 316 316 ILE ILE C . n 
B 1 317 TYR 317 317 317 TYR TYR C . n 
B 1 318 TYR 318 318 318 TYR TYR C . n 
B 1 319 PRO 319 319 319 PRO PRO C . n 
B 1 320 LEU 320 320 320 LEU LEU C . n 
B 1 321 SER 321 321 321 SER SER C . n 
B 1 322 LYS 322 322 322 LYS LYS C . n 
B 1 323 LEU 323 323 323 LEU LEU C . n 
B 1 324 ASP 324 324 324 ASP ASP C . n 
B 1 325 LEU 325 325 325 LEU LEU C . n 
B 1 326 ILE 326 326 326 ILE ILE C . n 
B 1 327 ALA 327 327 327 ALA ALA C . n 
B 1 328 ILE 328 328 328 ILE ILE C . n 
B 1 329 PRO 329 329 329 PRO PRO C . n 
B 1 330 ASP 330 330 330 ASP ASP C . n 
B 1 331 PHE 331 331 331 PHE PHE C . n 
B 1 332 ALA 332 332 332 ALA ALA C . n 
B 1 333 PRO 333 333 333 PRO PRO C . n 
B 1 334 GLY 334 334 334 GLY GLY C . n 
B 1 335 ALA 335 335 335 ALA ALA C . n 
B 1 336 MET 336 336 336 MET MET C . n 
B 1 337 GLU 337 337 337 GLU GLU C . n 
B 1 338 ASN 338 338 338 ASN ASN C . n 
B 1 339 TRP 339 339 339 TRP TRP C . n 
B 1 340 GLY 340 340 340 GLY GLY C . n 
B 1 341 LEU 341 341 341 LEU LEU C . n 
B 1 342 ILE 342 342 342 ILE ILE C . n 
B 1 343 THR 343 343 343 THR THR C . n 
B 1 344 TYR 344 344 344 TYR TYR C . n 
B 1 345 ARG 345 345 345 ARG ARG C . n 
B 1 346 GLU 346 346 346 GLU GLU C . n 
B 1 347 THR 347 347 347 THR THR C . n 
B 1 348 SER 348 348 348 SER SER C . n 
B 1 349 LEU 349 349 349 LEU LEU C . n 
B 1 350 LEU 350 350 350 LEU LEU C . n 
B 1 351 PHE 351 351 351 PHE PHE C . n 
B 1 352 ASP 352 352 352 ASP ASP C . n 
B 1 353 PRO 353 353 353 PRO PRO C . n 
B 1 354 LYS 354 354 354 LYS LYS C . n 
B 1 355 THR 355 355 355 THR THR C . n 
B 1 356 SER 356 356 356 SER SER C . n 
B 1 357 SER 357 357 357 SER SER C . n 
B 1 358 ALA 358 358 358 ALA ALA C . n 
B 1 359 SER 359 359 359 SER SER C . n 
B 1 360 ASP 360 360 360 ASP ASP C . n 
B 1 361 LYS 361 361 361 LYS LYS C . n 
B 1 362 LEU 362 362 362 LEU LEU C . n 
B 1 363 TRP 363 363 363 TRP TRP C . n 
B 1 364 VAL 364 364 364 VAL VAL C . n 
B 1 365 THR 365 365 365 THR THR C . n 
B 1 366 ARG 366 366 366 ARG ARG C . n 
B 1 367 VAL 367 367 367 VAL VAL C . n 
B 1 368 ILE 368 368 368 ILE ILE C . n 
B 1 369 ALA 369 369 369 ALA ALA C . n 
B 1 370 HIS 370 370 370 HIS HIS C . n 
B 1 371 GLU 371 371 371 GLU GLU C . n 
B 1 372 LEU 372 372 372 LEU LEU C . n 
B 1 373 ALA 373 373 373 ALA ALA C . n 
B 1 374 HIS 374 374 374 HIS HIS C . n 
B 1 375 GLN 375 375 375 GLN GLN C . n 
B 1 376 TRP 376 376 376 TRP TRP C . n 
B 1 377 PHE 377 377 377 PHE PHE C . n 
B 1 378 GLY 378 378 378 GLY GLY C . n 
B 1 379 ASN 379 379 379 ASN ASN C . n 
B 1 380 LEU 380 380 380 LEU LEU C . n 
B 1 381 VAL 381 381 381 VAL VAL C . n 
B 1 382 THR 382 382 382 THR THR C . n 
B 1 383 MET 383 383 383 MET MET C . n 
B 1 384 GLU 384 384 384 GLU GLU C . n 
B 1 385 TRP 385 385 385 TRP TRP C . n 
B 1 386 TRP 386 386 386 TRP TRP C . n 
B 1 387 ASN 387 387 387 ASN ASN C . n 
B 1 388 ASP 388 388 388 ASP ASP C . n 
B 1 389 ILE 389 389 389 ILE ILE C . n 
B 1 390 TRP 390 390 390 TRP TRP C . n 
B 1 391 LEU 391 391 391 LEU LEU C . n 
B 1 392 ASN 392 392 392 ASN ASN C . n 
B 1 393 GLU 393 393 393 GLU GLU C . n 
B 1 394 GLY 394 394 394 GLY GLY C . n 
B 1 395 PHE 395 395 395 PHE PHE C . n 
B 1 396 ALA 396 396 396 ALA ALA C . n 
B 1 397 LYS 397 397 397 LYS LYS C . n 
B 1 398 TYR 398 398 398 TYR TYR C . n 
B 1 399 MET 399 399 399 MET MET C . n 
B 1 400 GLU 400 400 400 GLU GLU C . n 
B 1 401 LEU 401 401 401 LEU LEU C . n 
B 1 402 ILE 402 402 402 ILE ILE C . n 
B 1 403 ALA 403 403 403 ALA ALA C . n 
B 1 404 VAL 404 404 404 VAL VAL C . n 
B 1 405 ASN 405 405 405 ASN ASN C . n 
B 1 406 ALA 406 406 406 ALA ALA C . n 
B 1 407 THR 407 407 407 THR THR C . n 
B 1 408 TYR 408 408 408 TYR TYR C . n 
B 1 409 PRO 409 409 409 PRO PRO C . n 
B 1 410 GLU 410 410 410 GLU GLU C . n 
B 1 411 LEU 411 411 411 LEU LEU C . n 
B 1 412 GLN 412 412 412 GLN GLN C . n 
B 1 413 PHE 413 413 413 PHE PHE C . n 
B 1 414 ASP 414 414 414 ASP ASP C . n 
B 1 415 ASP 415 415 415 ASP ASP C . n 
B 1 416 TYR 416 416 416 TYR TYR C . n 
B 1 417 PHE 417 417 417 PHE PHE C . n 
B 1 418 LEU 418 418 418 LEU LEU C . n 
B 1 419 ASN 419 419 419 ASN ASN C . n 
B 1 420 VAL 420 420 420 VAL VAL C . n 
B 1 421 CYS 421 421 421 CYS CYS C . n 
B 1 422 PHE 422 422 422 PHE PHE C . n 
B 1 423 GLU 423 423 423 GLU GLU C . n 
B 1 424 VAL 424 424 424 VAL VAL C . n 
B 1 425 ILE 425 425 425 ILE ILE C . n 
B 1 426 THR 426 426 426 THR THR C . n 
B 1 427 LYS 427 427 427 LYS LYS C . n 
B 1 428 ASP 428 428 428 ASP ASP C . n 
B 1 429 SER 429 429 429 SER SER C . n 
B 1 430 LEU 430 430 430 LEU LEU C . n 
B 1 431 ASN 431 431 431 ASN ASN C . n 
B 1 432 SER 432 432 432 SER SER C . n 
B 1 433 SER 433 433 433 SER SER C . n 
B 1 434 ARG 434 434 434 ARG ARG C . n 
B 1 435 PRO 435 435 435 PRO PRO C . n 
B 1 436 ILE 436 436 436 ILE ILE C . n 
B 1 437 SER 437 437 437 SER SER C . n 
B 1 438 LYS 438 438 438 LYS LYS C . n 
B 1 439 PRO 439 439 439 PRO PRO C . n 
B 1 440 ALA 440 440 440 ALA ALA C . n 
B 1 441 GLU 441 441 441 GLU GLU C . n 
B 1 442 THR 442 442 442 THR THR C . n 
B 1 443 PRO 443 443 443 PRO PRO C . n 
B 1 444 THR 444 444 444 THR THR C . n 
B 1 445 GLN 445 445 445 GLN GLN C . n 
B 1 446 ILE 446 446 446 ILE ILE C . n 
B 1 447 GLN 447 447 447 GLN GLN C . n 
B 1 448 GLU 448 448 448 GLU GLU C . n 
B 1 449 MET 449 449 449 MET MET C . n 
B 1 450 PHE 450 450 450 PHE PHE C . n 
B 1 451 ASP 451 451 451 ASP ASP C . n 
B 1 452 GLU 452 452 452 GLU GLU C . n 
B 1 453 VAL 453 453 453 VAL VAL C . n 
B 1 454 SER 454 454 454 SER SER C . n 
B 1 455 TYR 455 455 455 TYR TYR C . n 
B 1 456 ASN 456 456 456 ASN ASN C . n 
B 1 457 LYS 457 457 457 LYS LYS C . n 
B 1 458 GLY 458 458 458 GLY GLY C . n 
B 1 459 ALA 459 459 459 ALA ALA C . n 
B 1 460 CYS 460 460 460 CYS CYS C . n 
B 1 461 ILE 461 461 461 ILE ILE C . n 
B 1 462 LEU 462 462 462 LEU LEU C . n 
B 1 463 ASN 463 463 463 ASN ASN C . n 
B 1 464 MET 464 464 464 MET MET C . n 
B 1 465 LEU 465 465 465 LEU LEU C . n 
B 1 466 LYS 466 466 466 LYS LYS C . n 
B 1 467 ASP 467 467 467 ASP ASP C . n 
B 1 468 PHE 468 468 468 PHE PHE C . n 
B 1 469 LEU 469 469 469 LEU LEU C . n 
B 1 470 GLY 470 470 470 GLY GLY C . n 
B 1 471 GLU 471 471 471 GLU GLU C . n 
B 1 472 GLU 472 472 472 GLU GLU C . n 
B 1 473 LYS 473 473 473 LYS LYS C . n 
B 1 474 PHE 474 474 474 PHE PHE C . n 
B 1 475 GLN 475 475 475 GLN GLN C . n 
B 1 476 LYS 476 476 476 LYS LYS C . n 
B 1 477 GLY 477 477 477 GLY GLY C . n 
B 1 478 ILE 478 478 478 ILE ILE C . n 
B 1 479 ILE 479 479 479 ILE ILE C . n 
B 1 480 GLN 480 480 480 GLN GLN C . n 
B 1 481 TYR 481 481 481 TYR TYR C . n 
B 1 482 LEU 482 482 482 LEU LEU C . n 
B 1 483 LYS 483 483 483 LYS LYS C . n 
B 1 484 LYS 484 484 484 LYS LYS C . n 
B 1 485 PHE 485 485 485 PHE PHE C . n 
B 1 486 SER 486 486 486 SER SER C . n 
B 1 487 TYR 487 487 487 TYR TYR C . n 
B 1 488 ARG 488 488 488 ARG ARG C . n 
B 1 489 ASN 489 489 489 ASN ASN C . n 
B 1 490 ALA 490 490 490 ALA ALA C . n 
B 1 491 LYS 491 491 491 LYS LYS C . n 
B 1 492 ASN 492 492 492 ASN ASN C . n 
B 1 493 ASP 493 493 493 ASP ASP C . n 
B 1 494 ASP 494 494 494 ASP ASP C . n 
B 1 495 LEU 495 495 495 LEU LEU C . n 
B 1 496 TRP 496 496 496 TRP TRP C . n 
B 1 497 SER 497 497 497 SER SER C . n 
B 1 498 SER 498 498 498 SER SER C . n 
B 1 499 LEU 499 499 499 LEU LEU C . n 
B 1 500 SER 500 500 500 SER SER C . n 
B 1 501 ASN 501 501 501 ASN ASN C . n 
B 1 502 SER 502 502 ?   ?   ?   C . n 
B 1 503 CYS 503 503 ?   ?   ?   C . n 
B 1 504 LEU 504 504 ?   ?   ?   C . n 
B 1 505 GLU 505 505 ?   ?   ?   C . n 
B 1 506 SER 506 506 ?   ?   ?   C . n 
B 1 507 ASP 507 507 ?   ?   ?   C . n 
B 1 508 PHE 508 508 ?   ?   ?   C . n 
B 1 509 THR 509 509 ?   ?   ?   C . n 
B 1 510 SER 510 510 ?   ?   ?   C . n 
B 1 511 GLY 511 511 ?   ?   ?   C . n 
B 1 512 GLY 512 512 ?   ?   ?   C . n 
B 1 513 VAL 513 513 ?   ?   ?   C . n 
B 1 514 CYS 514 514 ?   ?   ?   C . n 
B 1 515 HIS 515 515 ?   ?   ?   C . n 
B 1 516 SER 516 516 ?   ?   ?   C . n 
B 1 517 ASP 517 517 ?   ?   ?   C . n 
B 1 518 PRO 518 518 ?   ?   ?   C . n 
B 1 519 LYS 519 519 ?   ?   ?   C . n 
B 1 520 MET 520 520 ?   ?   ?   C . n 
B 1 521 THR 521 521 ?   ?   ?   C . n 
B 1 522 SER 522 522 ?   ?   ?   C . n 
B 1 523 ASN 523 523 ?   ?   ?   C . n 
B 1 524 MET 524 524 ?   ?   ?   C . n 
B 1 525 LEU 525 525 ?   ?   ?   C . n 
B 1 526 ALA 526 526 ?   ?   ?   C . n 
B 1 527 PHE 527 527 ?   ?   ?   C . n 
B 1 528 LEU 528 528 ?   ?   ?   C . n 
B 1 529 GLY 529 529 529 GLY GLY C . n 
B 1 530 GLU 530 530 530 GLU GLU C . n 
B 1 531 ASN 531 531 531 ASN ASN C . n 
B 1 532 ALA 532 532 532 ALA ALA C . n 
B 1 533 GLU 533 533 533 GLU GLU C . n 
B 1 534 VAL 534 534 534 VAL VAL C . n 
B 1 535 LYS 535 535 535 LYS LYS C . n 
B 1 536 GLU 536 536 536 GLU GLU C . n 
B 1 537 MET 537 537 537 MET MET C . n 
B 1 538 MET 538 538 538 MET MET C . n 
B 1 539 THR 539 539 539 THR THR C . n 
B 1 540 THR 540 540 540 THR THR C . n 
B 1 541 TRP 541 541 541 TRP TRP C . n 
B 1 542 THR 542 542 542 THR THR C . n 
B 1 543 LEU 543 543 543 LEU LEU C . n 
B 1 544 GLN 544 544 544 GLN GLN C . n 
B 1 545 LYS 545 545 545 LYS LYS C . n 
B 1 546 GLY 546 546 546 GLY GLY C . n 
B 1 547 ILE 547 547 547 ILE ILE C . n 
B 1 548 PRO 548 548 548 PRO PRO C . n 
B 1 549 LEU 549 549 549 LEU LEU C . n 
B 1 550 LEU 550 550 550 LEU LEU C . n 
B 1 551 VAL 551 551 551 VAL VAL C . n 
B 1 552 VAL 552 552 552 VAL VAL C . n 
B 1 553 LYS 553 553 553 LYS LYS C . n 
B 1 554 GLN 554 554 554 GLN GLN C . n 
B 1 555 ASP 555 555 555 ASP ASP C . n 
B 1 556 GLY 556 556 556 GLY GLY C . n 
B 1 557 CYS 557 557 557 CYS CYS C . n 
B 1 558 SER 558 558 558 SER SER C . n 
B 1 559 LEU 559 559 559 LEU LEU C . n 
B 1 560 ARG 560 560 560 ARG ARG C . n 
B 1 561 LEU 561 561 561 LEU LEU C . n 
B 1 562 GLN 562 562 562 GLN GLN C . n 
B 1 563 GLN 563 563 563 GLN GLN C . n 
B 1 564 GLU 564 564 564 GLU GLU C . n 
B 1 565 ARG 565 565 565 ARG ARG C . n 
B 1 566 PHE 566 566 566 PHE PHE C . n 
B 1 567 LEU 567 567 567 LEU LEU C . n 
B 1 568 GLN 568 568 568 GLN GLN C . n 
B 1 569 GLY 569 569 569 GLY GLY C . n 
B 1 570 VAL 570 570 570 VAL VAL C . n 
B 1 571 PHE 571 571 571 PHE PHE C . n 
B 1 572 GLN 572 572 572 GLN GLN C . n 
B 1 573 GLU 573 573 573 GLU GLU C . n 
B 1 574 ASP 574 574 574 ASP ASP C . n 
B 1 575 PRO 575 575 575 PRO PRO C . n 
B 1 576 GLU 576 576 576 GLU GLU C . n 
B 1 577 TRP 577 577 577 TRP TRP C . n 
B 1 578 ARG 578 578 578 ARG ARG C . n 
B 1 579 ALA 579 579 579 ALA ALA C . n 
B 1 580 LEU 580 580 580 LEU LEU C . n 
B 1 581 GLN 581 581 581 GLN GLN C . n 
B 1 582 GLU 582 582 582 GLU GLU C . n 
B 1 583 ARG 583 583 583 ARG ARG C . n 
B 1 584 TYR 584 584 584 TYR TYR C . n 
B 1 585 LEU 585 585 585 LEU LEU C . n 
B 1 586 TRP 586 586 586 TRP TRP C . n 
B 1 587 HIS 587 587 587 HIS HIS C . n 
B 1 588 ILE 588 588 588 ILE ILE C . n 
B 1 589 PRO 589 589 589 PRO PRO C . n 
B 1 590 LEU 590 590 590 LEU LEU C . n 
B 1 591 THR 591 591 591 THR THR C . n 
B 1 592 TYR 592 592 592 TYR TYR C . n 
B 1 593 SER 593 593 593 SER SER C . n 
B 1 594 THR 594 594 594 THR THR C . n 
B 1 595 SER 595 595 595 SER SER C . n 
B 1 596 SER 596 596 596 SER SER C . n 
B 1 597 SER 597 597 597 SER SER C . n 
B 1 598 ASN 598 598 598 ASN ASN C . n 
B 1 599 VAL 599 599 599 VAL VAL C . n 
B 1 600 ILE 600 600 600 ILE ILE C . n 
B 1 601 HIS 601 601 601 HIS HIS C . n 
B 1 602 ARG 602 602 602 ARG ARG C . n 
B 1 603 HIS 603 603 603 HIS HIS C . n 
B 1 604 ILE 604 604 604 ILE ILE C . n 
B 1 605 LEU 605 605 605 LEU LEU C . n 
B 1 606 LYS 606 606 606 LYS LYS C . n 
B 1 607 SER 607 607 607 SER SER C . n 
B 1 608 LYS 608 608 608 LYS LYS C . n 
B 1 609 THR 609 609 609 THR THR C . n 
B 1 610 ASP 610 610 610 ASP ASP C . n 
B 1 611 THR 611 611 611 THR THR C . n 
B 1 612 LEU 612 612 612 LEU LEU C . n 
B 1 613 ASP 613 613 613 ASP ASP C . n 
B 1 614 LEU 614 614 614 LEU LEU C . n 
B 1 615 PRO 615 615 615 PRO PRO C . n 
B 1 616 GLU 616 616 616 GLU GLU C . n 
B 1 617 LYS 617 617 617 LYS LYS C . n 
B 1 618 THR 618 618 618 THR THR C . n 
B 1 619 SER 619 619 619 SER SER C . n 
B 1 620 TRP 620 620 620 TRP TRP C . n 
B 1 621 VAL 621 621 621 VAL VAL C . n 
B 1 622 LYS 622 622 622 LYS LYS C . n 
B 1 623 PHE 623 623 623 PHE PHE C . n 
B 1 624 ASN 624 624 624 ASN ASN C . n 
B 1 625 VAL 625 625 625 VAL VAL C . n 
B 1 626 ASP 626 626 626 ASP ASP C . n 
B 1 627 SER 627 627 627 SER SER C . n 
B 1 628 ASN 628 628 628 ASN ASN C . n 
B 1 629 GLY 629 629 629 GLY GLY C . n 
B 1 630 TYR 630 630 630 TYR TYR C . n 
B 1 631 TYR 631 631 631 TYR TYR C . n 
B 1 632 ILE 632 632 632 ILE ILE C . n 
B 1 633 VAL 633 633 633 VAL VAL C . n 
B 1 634 HIS 634 634 634 HIS HIS C . n 
B 1 635 TYR 635 635 635 TYR TYR C . n 
B 1 636 GLU 636 636 636 GLU GLU C . n 
B 1 637 GLY 637 637 637 GLY GLY C . n 
B 1 638 HIS 638 638 638 HIS HIS C . n 
B 1 639 GLY 639 639 639 GLY GLY C . n 
B 1 640 TRP 640 640 640 TRP TRP C . n 
B 1 641 ASP 641 641 641 ASP ASP C . n 
B 1 642 GLN 642 642 642 GLN GLN C . n 
B 1 643 LEU 643 643 643 LEU LEU C . n 
B 1 644 ILE 644 644 644 ILE ILE C . n 
B 1 645 THR 645 645 645 THR THR C . n 
B 1 646 GLN 646 646 646 GLN GLN C . n 
B 1 647 LEU 647 647 647 LEU LEU C . n 
B 1 648 ASN 648 648 648 ASN ASN C . n 
B 1 649 GLN 649 649 649 GLN GLN C . n 
B 1 650 ASN 650 650 650 ASN ASN C . n 
B 1 651 HIS 651 651 651 HIS HIS C . n 
B 1 652 THR 652 652 652 THR THR C . n 
B 1 653 LEU 653 653 653 LEU LEU C . n 
B 1 654 LEU 654 654 654 LEU LEU C . n 
B 1 655 ARG 655 655 655 ARG ARG C . n 
B 1 656 PRO 656 656 656 PRO PRO C . n 
B 1 657 LYS 657 657 657 LYS LYS C . n 
B 1 658 ASP 658 658 658 ASP ASP C . n 
B 1 659 ARG 659 659 659 ARG ARG C . n 
B 1 660 VAL 660 660 660 VAL VAL C . n 
B 1 661 GLY 661 661 661 GLY GLY C . n 
B 1 662 LEU 662 662 662 LEU LEU C . n 
B 1 663 ILE 663 663 663 ILE ILE C . n 
B 1 664 HIS 664 664 664 HIS HIS C . n 
B 1 665 ASP 665 665 665 ASP ASP C . n 
B 1 666 VAL 666 666 666 VAL VAL C . n 
B 1 667 PHE 667 667 667 PHE PHE C . n 
B 1 668 GLN 668 668 668 GLN GLN C . n 
B 1 669 LEU 669 669 669 LEU LEU C . n 
B 1 670 VAL 670 670 670 VAL VAL C . n 
B 1 671 GLY 671 671 671 GLY GLY C . n 
B 1 672 ALA 672 672 672 ALA ALA C . n 
B 1 673 GLY 673 673 673 GLY GLY C . n 
B 1 674 ARG 674 674 674 ARG ARG C . n 
B 1 675 LEU 675 675 675 LEU LEU C . n 
B 1 676 THR 676 676 676 THR THR C . n 
B 1 677 LEU 677 677 677 LEU LEU C . n 
B 1 678 ASP 678 678 678 ASP ASP C . n 
B 1 679 LYS 679 679 679 LYS LYS C . n 
B 1 680 ALA 680 680 680 ALA ALA C . n 
B 1 681 LEU 681 681 681 LEU LEU C . n 
B 1 682 ASP 682 682 682 ASP ASP C . n 
B 1 683 MET 683 683 683 MET MET C . n 
B 1 684 THR 684 684 684 THR THR C . n 
B 1 685 TYR 685 685 685 TYR TYR C . n 
B 1 686 TYR 686 686 686 TYR TYR C . n 
B 1 687 LEU 687 687 687 LEU LEU C . n 
B 1 688 GLN 688 688 688 GLN GLN C . n 
B 1 689 HIS 689 689 689 HIS HIS C . n 
B 1 690 GLU 690 690 690 GLU GLU C . n 
B 1 691 THR 691 691 691 THR THR C . n 
B 1 692 SER 692 692 692 SER SER C . n 
B 1 693 SER 693 693 693 SER SER C . n 
B 1 694 PRO 694 694 694 PRO PRO C . n 
B 1 695 ALA 695 695 695 ALA ALA C . n 
B 1 696 LEU 696 696 696 LEU LEU C . n 
B 1 697 LEU 697 697 697 LEU LEU C . n 
B 1 698 GLU 698 698 698 GLU GLU C . n 
B 1 699 GLY 699 699 699 GLY GLY C . n 
B 1 700 LEU 700 700 700 LEU LEU C . n 
B 1 701 SER 701 701 701 SER SER C . n 
B 1 702 TYR 702 702 702 TYR TYR C . n 
B 1 703 LEU 703 703 703 LEU LEU C . n 
B 1 704 GLU 704 704 704 GLU GLU C . n 
B 1 705 SER 705 705 705 SER SER C . n 
B 1 706 PHE 706 706 706 PHE PHE C . n 
B 1 707 TYR 707 707 707 TYR TYR C . n 
B 1 708 HIS 708 708 708 HIS HIS C . n 
B 1 709 MET 709 709 709 MET MET C . n 
B 1 710 MET 710 710 710 MET MET C . n 
B 1 711 ASP 711 711 711 ASP ASP C . n 
B 1 712 ARG 712 712 712 ARG ARG C . n 
B 1 713 ARG 713 713 713 ARG ARG C . n 
B 1 714 ASN 714 714 714 ASN ASN C . n 
B 1 715 ILE 715 715 715 ILE ILE C . n 
B 1 716 SER 716 716 716 SER SER C . n 
B 1 717 ASP 717 717 717 ASP ASP C . n 
B 1 718 ILE 718 718 718 ILE ILE C . n 
B 1 719 SER 719 719 719 SER SER C . n 
B 1 720 GLU 720 720 720 GLU GLU C . n 
B 1 721 ASN 721 721 721 ASN ASN C . n 
B 1 722 LEU 722 722 722 LEU LEU C . n 
B 1 723 LYS 723 723 723 LYS LYS C . n 
B 1 724 ARG 724 724 724 ARG ARG C . n 
B 1 725 TYR 725 725 725 TYR TYR C . n 
B 1 726 LEU 726 726 726 LEU LEU C . n 
B 1 727 LEU 727 727 727 LEU LEU C . n 
B 1 728 GLN 728 728 728 GLN GLN C . n 
B 1 729 TYR 729 729 729 TYR TYR C . n 
B 1 730 PHE 730 730 730 PHE PHE C . n 
B 1 731 LYS 731 731 731 LYS LYS C . n 
B 1 732 PRO 732 732 732 PRO PRO C . n 
B 1 733 VAL 733 733 733 VAL VAL C . n 
B 1 734 ILE 734 734 734 ILE ILE C . n 
B 1 735 ASP 735 735 735 ASP ASP C . n 
B 1 736 ARG 736 736 736 ARG ARG C . n 
B 1 737 GLN 737 737 737 GLN GLN C . n 
B 1 738 SER 738 738 738 SER SER C . n 
B 1 739 TRP 739 739 739 TRP TRP C . n 
B 1 740 SER 740 740 740 SER SER C . n 
B 1 741 ASP 741 741 741 ASP ASP C . n 
B 1 742 LYS 742 742 742 LYS LYS C . n 
B 1 743 GLY 743 743 743 GLY GLY C . n 
B 1 744 SER 744 744 744 SER SER C . n 
B 1 745 VAL 745 745 745 VAL VAL C . n 
B 1 746 TRP 746 746 746 TRP TRP C . n 
B 1 747 ASP 747 747 747 ASP ASP C . n 
B 1 748 ARG 748 748 748 ARG ARG C . n 
B 1 749 MET 749 749 749 MET MET C . n 
B 1 750 LEU 750 750 750 LEU LEU C . n 
B 1 751 ARG 751 751 751 ARG ARG C . n 
B 1 752 SER 752 752 752 SER SER C . n 
B 1 753 ALA 753 753 753 ALA ALA C . n 
B 1 754 LEU 754 754 754 LEU LEU C . n 
B 1 755 LEU 755 755 755 LEU LEU C . n 
B 1 756 LYS 756 756 756 LYS LYS C . n 
B 1 757 LEU 757 757 757 LEU LEU C . n 
B 1 758 ALA 758 758 758 ALA ALA C . n 
B 1 759 CYS 759 759 759 CYS CYS C . n 
B 1 760 ASP 760 760 760 ASP ASP C . n 
B 1 761 LEU 761 761 761 LEU LEU C . n 
B 1 762 ASN 762 762 762 ASN ASN C . n 
B 1 763 HIS 763 763 763 HIS HIS C . n 
B 1 764 ALA 764 764 764 ALA ALA C . n 
B 1 765 PRO 765 765 765 PRO PRO C . n 
B 1 766 CYS 766 766 766 CYS CYS C . n 
B 1 767 ILE 767 767 767 ILE ILE C . n 
B 1 768 GLN 768 768 768 GLN GLN C . n 
B 1 769 LYS 769 769 769 LYS LYS C . n 
B 1 770 ALA 770 770 770 ALA ALA C . n 
B 1 771 ALA 771 771 771 ALA ALA C . n 
B 1 772 GLU 772 772 772 GLU GLU C . n 
B 1 773 LEU 773 773 773 LEU LEU C . n 
B 1 774 PHE 774 774 774 PHE PHE C . n 
B 1 775 SER 775 775 775 SER SER C . n 
B 1 776 GLN 776 776 776 GLN GLN C . n 
B 1 777 TRP 777 777 777 TRP TRP C . n 
B 1 778 MET 778 778 778 MET MET C . n 
B 1 779 GLU 779 779 779 GLU GLU C . n 
B 1 780 SER 780 780 780 SER SER C . n 
B 1 781 SER 781 781 781 SER SER C . n 
B 1 782 GLY 782 782 782 GLY GLY C . n 
B 1 783 LYS 783 783 783 LYS LYS C . n 
B 1 784 LEU 784 784 784 LEU LEU C . n 
B 1 785 ASN 785 785 785 ASN ASN C . n 
B 1 786 ILE 786 786 786 ILE ILE C . n 
B 1 787 PRO 787 787 787 PRO PRO C . n 
B 1 788 THR 788 788 788 THR THR C . n 
B 1 789 ASP 789 789 789 ASP ASP C . n 
B 1 790 VAL 790 790 790 VAL VAL C . n 
B 1 791 LEU 791 791 791 LEU LEU C . n 
B 1 792 LYS 792 792 792 LYS LYS C . n 
B 1 793 ILE 793 793 793 ILE ILE C . n 
B 1 794 VAL 794 794 794 VAL VAL C . n 
B 1 795 TYR 795 795 795 TYR TYR C . n 
B 1 796 SER 796 796 796 SER SER C . n 
B 1 797 VAL 797 797 797 VAL VAL C . n 
B 1 798 GLY 798 798 798 GLY GLY C . n 
B 1 799 ALA 799 799 799 ALA ALA C . n 
B 1 800 GLN 800 800 800 GLN GLN C . n 
B 1 801 THR 801 801 801 THR THR C . n 
B 1 802 THR 802 802 802 THR THR C . n 
B 1 803 ALA 803 803 803 ALA ALA C . n 
B 1 804 GLY 804 804 804 GLY GLY C . n 
B 1 805 TRP 805 805 805 TRP TRP C . n 
B 1 806 ASN 806 806 806 ASN ASN C . n 
B 1 807 TYR 807 807 807 TYR TYR C . n 
B 1 808 LEU 808 808 808 LEU LEU C . n 
B 1 809 LEU 809 809 809 LEU LEU C . n 
B 1 810 GLU 810 810 810 GLU GLU C . n 
B 1 811 GLN 811 811 811 GLN GLN C . n 
B 1 812 TYR 812 812 812 TYR TYR C . n 
B 1 813 GLU 813 813 813 GLU GLU C . n 
B 1 814 LEU 814 814 814 LEU LEU C . n 
B 1 815 SER 815 815 815 SER SER C . n 
B 1 816 MET 816 816 816 MET MET C . n 
B 1 817 SER 817 817 817 SER SER C . n 
B 1 818 SER 818 818 818 SER SER C . n 
B 1 819 ALA 819 819 819 ALA ALA C . n 
B 1 820 GLU 820 820 820 GLU GLU C . n 
B 1 821 GLN 821 821 821 GLN GLN C . n 
B 1 822 ASN 822 822 822 ASN ASN C . n 
B 1 823 LYS 823 823 823 LYS LYS C . n 
B 1 824 ILE 824 824 824 ILE ILE C . n 
B 1 825 LEU 825 825 825 LEU LEU C . n 
B 1 826 TYR 826 826 826 TYR TYR C . n 
B 1 827 ALA 827 827 827 ALA ALA C . n 
B 1 828 LEU 828 828 828 LEU LEU C . n 
B 1 829 SER 829 829 829 SER SER C . n 
B 1 830 THR 830 830 830 THR THR C . n 
B 1 831 SER 831 831 831 SER SER C . n 
B 1 832 LYS 832 832 832 LYS LYS C . n 
B 1 833 HIS 833 833 833 HIS HIS C . n 
B 1 834 GLN 834 834 834 GLN GLN C . n 
B 1 835 GLU 835 835 835 GLU GLU C . n 
B 1 836 LYS 836 836 836 LYS LYS C . n 
B 1 837 LEU 837 837 837 LEU LEU C . n 
B 1 838 LEU 838 838 838 LEU LEU C . n 
B 1 839 LYS 839 839 839 LYS LYS C . n 
B 1 840 LEU 840 840 840 LEU LEU C . n 
B 1 841 ILE 841 841 841 ILE ILE C . n 
B 1 842 GLU 842 842 842 GLU GLU C . n 
B 1 843 LEU 843 843 843 LEU LEU C . n 
B 1 844 GLY 844 844 844 GLY GLY C . n 
B 1 845 MET 845 845 845 MET MET C . n 
B 1 846 GLU 846 846 846 GLU GLU C . n 
B 1 847 GLY 847 847 847 GLY GLY C . n 
B 1 848 LYS 848 848 848 LYS LYS C . n 
B 1 849 VAL 849 849 849 VAL VAL C . n 
B 1 850 ILE 850 850 850 ILE ILE C . n 
B 1 851 LYS 851 851 851 LYS LYS C . n 
B 1 852 THR 852 852 852 THR THR C . n 
B 1 853 GLN 853 853 853 GLN GLN C . n 
B 1 854 ASN 854 854 854 ASN ASN C . n 
B 1 855 LEU 855 855 855 LEU LEU C . n 
B 1 856 ALA 856 856 856 ALA ALA C . n 
B 1 857 ALA 857 857 857 ALA ALA C . n 
B 1 858 LEU 858 858 858 LEU LEU C . n 
B 1 859 LEU 859 859 859 LEU LEU C . n 
B 1 860 HIS 860 860 860 HIS HIS C . n 
B 1 861 ALA 861 861 861 ALA ALA C . n 
B 1 862 ILE 862 862 862 ILE ILE C . n 
B 1 863 ALA 863 863 863 ALA ALA C . n 
B 1 864 ARG 864 864 864 ARG ARG C . n 
B 1 865 ARG 865 865 865 ARG ARG C . n 
B 1 866 PRO 866 866 866 PRO PRO C . n 
B 1 867 LYS 867 867 867 LYS LYS C . n 
B 1 868 GLY 868 868 868 GLY GLY C . n 
B 1 869 GLN 869 869 869 GLN GLN C . n 
B 1 870 GLN 870 870 870 GLN GLN C . n 
B 1 871 LEU 871 871 871 LEU LEU C . n 
B 1 872 ALA 872 872 872 ALA ALA C . n 
B 1 873 TRP 873 873 873 TRP TRP C . n 
B 1 874 ASP 874 874 874 ASP ASP C . n 
B 1 875 PHE 875 875 875 PHE PHE C . n 
B 1 876 VAL 876 876 876 VAL VAL C . n 
B 1 877 ARG 877 877 877 ARG ARG C . n 
B 1 878 GLU 878 878 878 GLU GLU C . n 
B 1 879 ASN 879 879 879 ASN ASN C . n 
B 1 880 TRP 880 880 880 TRP TRP C . n 
B 1 881 THR 881 881 881 THR THR C . n 
B 1 882 HIS 882 882 882 HIS HIS C . n 
B 1 883 LEU 883 883 883 LEU LEU C . n 
B 1 884 LEU 884 884 884 LEU LEU C . n 
B 1 885 LYS 885 885 885 LYS LYS C . n 
B 1 886 LYS 886 886 886 LYS LYS C . n 
B 1 887 PHE 887 887 887 PHE PHE C . n 
B 1 888 ASP 888 888 888 ASP ASP C . n 
B 1 889 LEU 889 889 889 LEU LEU C . n 
B 1 890 GLY 890 890 890 GLY GLY C . n 
B 1 891 SER 891 891 891 SER SER C . n 
B 1 892 TYR 892 892 892 TYR TYR C . n 
B 1 893 ASP 893 893 893 ASP ASP C . n 
B 1 894 ILE 894 894 894 ILE ILE C . n 
B 1 895 ARG 895 895 895 ARG ARG C . n 
B 1 896 MET 896 896 896 MET MET C . n 
B 1 897 ILE 897 897 897 ILE ILE C . n 
B 1 898 ILE 898 898 898 ILE ILE C . n 
B 1 899 SER 899 899 899 SER SER C . n 
B 1 900 GLY 900 900 900 GLY GLY C . n 
B 1 901 THR 901 901 901 THR THR C . n 
B 1 902 THR 902 902 902 THR THR C . n 
B 1 903 ALA 903 903 903 ALA ALA C . n 
B 1 904 HIS 904 904 904 HIS HIS C . n 
B 1 905 PHE 905 905 905 PHE PHE C . n 
B 1 906 SER 906 906 906 SER SER C . n 
B 1 907 SER 907 907 907 SER SER C . n 
B 1 908 LYS 908 908 908 LYS LYS C . n 
B 1 909 ASP 909 909 909 ASP ASP C . n 
B 1 910 LYS 910 910 910 LYS LYS C . n 
B 1 911 LEU 911 911 911 LEU LEU C . n 
B 1 912 GLN 912 912 912 GLN GLN C . n 
B 1 913 GLU 913 913 913 GLU GLU C . n 
B 1 914 VAL 914 914 914 VAL VAL C . n 
B 1 915 LYS 915 915 915 LYS LYS C . n 
B 1 916 LEU 916 916 916 LEU LEU C . n 
B 1 917 PHE 917 917 917 PHE PHE C . n 
B 1 918 PHE 918 918 918 PHE PHE C . n 
B 1 919 GLU 919 919 919 GLU GLU C . n 
B 1 920 SER 920 920 920 SER SER C . n 
B 1 921 LEU 921 921 921 LEU LEU C . n 
B 1 922 GLU 922 922 922 GLU GLU C . n 
B 1 923 ALA 923 923 923 ALA ALA C . n 
B 1 924 GLN 924 924 924 GLN GLN C . n 
B 1 925 GLY 925 925 925 GLY GLY C . n 
B 1 926 SER 926 926 926 SER SER C . n 
B 1 927 HIS 927 927 927 HIS HIS C . n 
B 1 928 LEU 928 928 928 LEU LEU C . n 
B 1 929 ASP 929 929 929 ASP ASP C . n 
B 1 930 ILE 930 930 930 ILE ILE C . n 
B 1 931 PHE 931 931 931 PHE PHE C . n 
B 1 932 GLN 932 932 932 GLN GLN C . n 
B 1 933 THR 933 933 933 THR THR C . n 
B 1 934 VAL 934 934 934 VAL VAL C . n 
B 1 935 LEU 935 935 935 LEU LEU C . n 
B 1 936 GLU 936 936 936 GLU GLU C . n 
B 1 937 THR 937 937 937 THR THR C . n 
B 1 938 ILE 938 938 938 ILE ILE C . n 
B 1 939 THR 939 939 939 THR THR C . n 
B 1 940 LYS 940 940 940 LYS LYS C . n 
B 1 941 ASN 941 941 941 ASN ASN C . n 
B 1 942 ILE 942 942 942 ILE ILE C . n 
B 1 943 LYS 943 943 943 LYS LYS C . n 
B 1 944 TRP 944 944 944 TRP TRP C . n 
B 1 945 LEU 945 945 945 LEU LEU C . n 
B 1 946 GLU 946 946 946 GLU GLU C . n 
B 1 947 LYS 947 947 947 LYS LYS C . n 
B 1 948 ASN 948 948 948 ASN ASN C . n 
B 1 949 LEU 949 949 949 LEU LEU C . n 
B 1 950 PRO 950 950 950 PRO PRO C . n 
B 1 951 THR 951 951 951 THR THR C . n 
B 1 952 LEU 952 952 952 LEU LEU C . n 
B 1 953 ARG 953 953 953 ARG ARG C . n 
B 1 954 THR 954 954 954 THR THR C . n 
B 1 955 TRP 955 955 955 TRP TRP C . n 
B 1 956 LEU 956 956 956 LEU LEU C . n 
B 1 957 MET 957 957 957 MET MET C . n 
B 1 958 VAL 958 958 958 VAL VAL C . n 
B 1 959 ASN 959 959 959 ASN ASN C . n 
B 1 960 THR 960 960 960 THR THR C . n 
B 1 961 ARG 961 961 961 ARG ARG C . n 
B 1 962 HIS 962 962 962 HIS HIS C . n 
B 1 963 HIS 963 963 ?   ?   ?   C . n 
B 1 964 HIS 964 964 ?   ?   ?   C . n 
B 1 965 HIS 965 965 ?   ?   ?   C . n 
B 1 966 HIS 966 966 ?   ?   ?   C . n 
B 1 967 HIS 967 967 ?   ?   ?   C . n 
C 2 1   2X0 1   1   1   2X0 2X0 E . n 
C 2 2   7GA 2   2   2   7GA 7GA E . n 
C 2 3   LYS 3   3   3   LYS LYS E . n 
C 2 4   HIS 4   4   4   HIS HIS E . n 
C 2 5   HIS 5   5   5   HIS HIS E . n 
C 2 6   ALA 6   6   6   ALA ALA E . n 
C 2 7   PHE 7   7   7   PHE PHE E . n 
C 2 8   SER 8   8   8   SER SER E . n 
C 2 9   PHE 9   9   9   PHE PHE E . n 
C 2 10  LYN 10  10  10  LYN LYN E . n 
D 2 1   2X0 1   1   1   2X0 2X0 F . n 
D 2 2   7GA 2   2   2   7GA 7GA F . n 
D 2 3   LYS 3   3   3   LYS LYS F . n 
D 2 4   HIS 4   4   4   HIS HIS F . n 
D 2 5   HIS 5   5   5   HIS HIS F . n 
D 2 6   ALA 6   6   6   ALA ALA F . n 
D 2 7   PHE 7   7   7   PHE PHE F . n 
D 2 8   SER 8   8   8   SER SER F . n 
D 2 9   PHE 9   9   9   PHE PHE F . n 
D 2 10  LYN 10  10  10  LYN LYN F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  3 ZN  1   1008 1008 ZN  ZN  A . 
F  4 NAG 1   1069 1069 NAG NAG A . 
G  4 NAG 1   1070 1070 NAG NAG A . 
H  4 NAG 1   1071 1071 NAG NAG A . 
I  4 NAG 2   1072 1072 NAG NAG A . 
J  4 NAG 1   1073 1073 NAG NAG A . 
K  4 NAG 2   1074 1074 NAG NAG A . 
L  5 BMA 3   1075 1075 BMA BMA A . 
M  4 NAG 1   1076 1076 NAG NAG A . 
N  4 NAG 2   1077 1077 NAG NAG A . 
O  5 BMA 3   1078 1078 BMA BMA A . 
P  4 NAG 1   1079 1079 NAG NAG A . 
Q  4 NAG 2   1080 1080 NAG NAG A . 
R  4 NAG 1   1081 1081 NAG NAG A . 
S  4 NAG 1   1082 1082 NAG NAG A . 
T  6 EDO 1   1964 1964 EDO EDO A . 
U  6 EDO 1   1965 1965 EDO EDO A . 
V  7 MES 1   2002 2002 MES MES A . 
W  5 BMA 1   1001 1001 BMA BMA C . 
X  5 BMA 2   1002 1002 BMA BMA C . 
Y  4 NAG 3   1003 1003 NAG NAG C . 
Z  4 NAG 4   1004 1004 NAG NAG C . 
AA 5 BMA 5   1005 1005 BMA BMA C . 
BA 4 NAG 1   1006 1006 NAG NAG C . 
CA 4 NAG 1   1007 1007 NAG NAG C . 
DA 4 NAG 2   1008 1008 NAG NAG C . 
EA 4 NAG 1   1009 1009 NAG NAG C . 
FA 4 NAG 1   1010 1010 NAG NAG C . 
GA 4 NAG 1   1011 1011 NAG NAG C . 
HA 4 NAG 1   1012 1012 NAG NAG C . 
IA 4 NAG 1   1013 1013 NAG NAG C . 
JA 3 ZN  1   1020 1020 ZN  ZN  C . 
KA 6 EDO 1   1962 1962 EDO EDO C . 
LA 6 EDO 1   1963 1963 EDO EDO C . 
MA 8 HOH 1   3001 3001 HOH HOH A . 
MA 8 HOH 2   3002 3002 HOH HOH A . 
MA 8 HOH 3   3003 3003 HOH HOH A . 
MA 8 HOH 4   3004 3004 HOH HOH A . 
MA 8 HOH 5   3005 3005 HOH HOH A . 
MA 8 HOH 6   3006 3006 HOH HOH A . 
MA 8 HOH 7   3007 3007 HOH HOH A . 
MA 8 HOH 8   3008 3008 HOH HOH A . 
MA 8 HOH 9   3009 3009 HOH HOH A . 
MA 8 HOH 10  3010 3010 HOH HOH A . 
MA 8 HOH 11  3011 3011 HOH HOH A . 
MA 8 HOH 12  3012 3012 HOH HOH A . 
MA 8 HOH 13  3013 3013 HOH HOH A . 
MA 8 HOH 14  3014 3014 HOH HOH A . 
MA 8 HOH 15  3015 3015 HOH HOH A . 
MA 8 HOH 16  3016 3016 HOH HOH A . 
MA 8 HOH 17  3017 3017 HOH HOH A . 
MA 8 HOH 18  3018 3018 HOH HOH A . 
MA 8 HOH 19  3019 3019 HOH HOH A . 
MA 8 HOH 20  3020 3020 HOH HOH A . 
MA 8 HOH 21  3021 3021 HOH HOH A . 
MA 8 HOH 22  3022 3022 HOH HOH A . 
MA 8 HOH 23  3023 3023 HOH HOH A . 
MA 8 HOH 24  3024 3024 HOH HOH A . 
MA 8 HOH 25  3025 3025 HOH HOH A . 
MA 8 HOH 26  3026 3026 HOH HOH A . 
MA 8 HOH 27  3027 3027 HOH HOH A . 
MA 8 HOH 28  3028 3028 HOH HOH A . 
MA 8 HOH 29  3029 3029 HOH HOH A . 
MA 8 HOH 30  3030 3030 HOH HOH A . 
MA 8 HOH 31  3031 3031 HOH HOH A . 
MA 8 HOH 32  3032 3032 HOH HOH A . 
MA 8 HOH 33  3033 3033 HOH HOH A . 
MA 8 HOH 34  3034 3034 HOH HOH A . 
MA 8 HOH 35  3035 3035 HOH HOH A . 
MA 8 HOH 36  3036 3036 HOH HOH A . 
MA 8 HOH 37  3037 3037 HOH HOH A . 
MA 8 HOH 38  3038 3038 HOH HOH A . 
MA 8 HOH 39  3039 3039 HOH HOH A . 
MA 8 HOH 40  3040 3040 HOH HOH A . 
MA 8 HOH 41  3041 3041 HOH HOH A . 
MA 8 HOH 42  3042 3042 HOH HOH A . 
MA 8 HOH 43  3043 3043 HOH HOH A . 
MA 8 HOH 44  3044 3044 HOH HOH A . 
MA 8 HOH 45  3045 3045 HOH HOH A . 
MA 8 HOH 46  3046 3046 HOH HOH A . 
MA 8 HOH 47  3047 3047 HOH HOH A . 
MA 8 HOH 48  3048 3048 HOH HOH A . 
MA 8 HOH 49  3049 3049 HOH HOH A . 
MA 8 HOH 50  3050 3050 HOH HOH A . 
MA 8 HOH 51  3051 3051 HOH HOH A . 
MA 8 HOH 52  3052 3052 HOH HOH A . 
MA 8 HOH 53  3053 3053 HOH HOH A . 
MA 8 HOH 54  3054 3054 HOH HOH A . 
MA 8 HOH 55  3055 3055 HOH HOH A . 
MA 8 HOH 56  3056 3056 HOH HOH A . 
MA 8 HOH 57  3057 3057 HOH HOH A . 
MA 8 HOH 58  3058 3058 HOH HOH A . 
MA 8 HOH 59  3059 3059 HOH HOH A . 
MA 8 HOH 60  3060 3060 HOH HOH A . 
MA 8 HOH 61  3061 3061 HOH HOH A . 
MA 8 HOH 62  3062 3062 HOH HOH A . 
MA 8 HOH 63  3063 3063 HOH HOH A . 
MA 8 HOH 64  3064 3064 HOH HOH A . 
MA 8 HOH 65  3065 3065 HOH HOH A . 
MA 8 HOH 66  3066 3066 HOH HOH A . 
MA 8 HOH 67  3067 3067 HOH HOH A . 
MA 8 HOH 68  3068 3068 HOH HOH A . 
MA 8 HOH 69  3069 3069 HOH HOH A . 
MA 8 HOH 70  3070 3070 HOH HOH A . 
MA 8 HOH 71  3071 3071 HOH HOH A . 
MA 8 HOH 72  3072 3072 HOH HOH A . 
MA 8 HOH 73  3073 3073 HOH HOH A . 
MA 8 HOH 74  3074 3074 HOH HOH A . 
MA 8 HOH 75  3075 3075 HOH HOH A . 
MA 8 HOH 76  3076 3076 HOH HOH A . 
MA 8 HOH 77  3077 3077 HOH HOH A . 
MA 8 HOH 78  3078 3078 HOH HOH A . 
MA 8 HOH 79  3079 3079 HOH HOH A . 
MA 8 HOH 80  3080 3080 HOH HOH A . 
MA 8 HOH 81  3081 3081 HOH HOH A . 
MA 8 HOH 82  3082 3082 HOH HOH A . 
MA 8 HOH 83  3083 3083 HOH HOH A . 
MA 8 HOH 84  3084 3084 HOH HOH A . 
MA 8 HOH 85  3085 3085 HOH HOH A . 
MA 8 HOH 86  3086 3086 HOH HOH A . 
MA 8 HOH 87  3087 3087 HOH HOH A . 
MA 8 HOH 88  3088 3088 HOH HOH A . 
MA 8 HOH 89  3089 3089 HOH HOH A . 
MA 8 HOH 90  3090 3090 HOH HOH A . 
MA 8 HOH 91  3091 3091 HOH HOH A . 
MA 8 HOH 92  3092 3092 HOH HOH A . 
MA 8 HOH 93  3093 3093 HOH HOH A . 
MA 8 HOH 94  3094 3094 HOH HOH A . 
MA 8 HOH 95  3095 3095 HOH HOH A . 
MA 8 HOH 96  3096 3096 HOH HOH A . 
MA 8 HOH 97  3097 3097 HOH HOH A . 
MA 8 HOH 98  3098 3098 HOH HOH A . 
MA 8 HOH 99  3099 3099 HOH HOH A . 
MA 8 HOH 100 3100 3100 HOH HOH A . 
MA 8 HOH 101 3101 3101 HOH HOH A . 
MA 8 HOH 102 3102 3102 HOH HOH A . 
MA 8 HOH 103 3103 3103 HOH HOH A . 
MA 8 HOH 104 3104 3104 HOH HOH A . 
MA 8 HOH 105 3105 3105 HOH HOH A . 
MA 8 HOH 106 3106 3106 HOH HOH A . 
MA 8 HOH 107 3107 3107 HOH HOH A . 
MA 8 HOH 108 3108 3108 HOH HOH A . 
MA 8 HOH 109 3109 3109 HOH HOH A . 
MA 8 HOH 110 3110 3110 HOH HOH A . 
MA 8 HOH 111 3111 3111 HOH HOH A . 
MA 8 HOH 112 3112 3112 HOH HOH A . 
MA 8 HOH 113 3113 3113 HOH HOH A . 
MA 8 HOH 114 3114 3114 HOH HOH A . 
MA 8 HOH 115 3115 3115 HOH HOH A . 
MA 8 HOH 116 3116 3116 HOH HOH A . 
MA 8 HOH 117 3117 3117 HOH HOH A . 
MA 8 HOH 118 3118 3118 HOH HOH A . 
MA 8 HOH 119 3119 3119 HOH HOH A . 
MA 8 HOH 120 3120 3120 HOH HOH A . 
MA 8 HOH 121 3121 3121 HOH HOH A . 
MA 8 HOH 122 3122 3122 HOH HOH A . 
MA 8 HOH 123 3123 3123 HOH HOH A . 
MA 8 HOH 124 3124 3124 HOH HOH A . 
MA 8 HOH 125 3125 3125 HOH HOH A . 
MA 8 HOH 126 3126 3126 HOH HOH A . 
MA 8 HOH 127 3127 3127 HOH HOH A . 
MA 8 HOH 128 3128 3128 HOH HOH A . 
MA 8 HOH 129 3129 3129 HOH HOH A . 
MA 8 HOH 130 3130 3130 HOH HOH A . 
MA 8 HOH 131 3131 3131 HOH HOH A . 
MA 8 HOH 132 3132 3132 HOH HOH A . 
MA 8 HOH 133 3133 3133 HOH HOH A . 
MA 8 HOH 134 3134 3134 HOH HOH A . 
MA 8 HOH 135 3135 3135 HOH HOH A . 
MA 8 HOH 136 3136 3136 HOH HOH A . 
MA 8 HOH 137 3137 3137 HOH HOH A . 
MA 8 HOH 138 3138 3138 HOH HOH A . 
MA 8 HOH 139 3139 3139 HOH HOH A . 
MA 8 HOH 140 3140 3140 HOH HOH A . 
MA 8 HOH 141 3141 3141 HOH HOH A . 
MA 8 HOH 142 3142 3142 HOH HOH A . 
MA 8 HOH 143 3143 3143 HOH HOH A . 
MA 8 HOH 144 3144 3144 HOH HOH A . 
MA 8 HOH 145 3145 3145 HOH HOH A . 
MA 8 HOH 146 3146 3146 HOH HOH A . 
MA 8 HOH 147 3147 3147 HOH HOH A . 
MA 8 HOH 148 3148 3148 HOH HOH A . 
MA 8 HOH 149 3149 3149 HOH HOH A . 
MA 8 HOH 150 3150 3150 HOH HOH A . 
MA 8 HOH 151 3151 3151 HOH HOH A . 
MA 8 HOH 152 3152 3152 HOH HOH A . 
MA 8 HOH 153 3153 3153 HOH HOH A . 
MA 8 HOH 154 3154 3154 HOH HOH A . 
MA 8 HOH 155 3155 3155 HOH HOH A . 
MA 8 HOH 156 3156 3156 HOH HOH A . 
MA 8 HOH 157 3157 3157 HOH HOH A . 
MA 8 HOH 158 3158 3158 HOH HOH A . 
MA 8 HOH 159 3159 3159 HOH HOH A . 
MA 8 HOH 160 3160 3160 HOH HOH A . 
MA 8 HOH 161 3161 3161 HOH HOH A . 
MA 8 HOH 162 3162 3162 HOH HOH A . 
MA 8 HOH 163 3163 3163 HOH HOH A . 
MA 8 HOH 164 3164 3164 HOH HOH A . 
MA 8 HOH 165 3165 3165 HOH HOH A . 
MA 8 HOH 166 3166 3166 HOH HOH A . 
MA 8 HOH 167 3167 3167 HOH HOH A . 
MA 8 HOH 168 3168 3168 HOH HOH A . 
MA 8 HOH 169 3169 3169 HOH HOH A . 
MA 8 HOH 170 3170 3170 HOH HOH A . 
MA 8 HOH 171 3171 3171 HOH HOH A . 
MA 8 HOH 172 3172 3172 HOH HOH A . 
MA 8 HOH 173 3173 3173 HOH HOH A . 
MA 8 HOH 174 3174 3174 HOH HOH A . 
MA 8 HOH 175 3175 3175 HOH HOH A . 
MA 8 HOH 176 3176 3176 HOH HOH A . 
MA 8 HOH 177 3177 3177 HOH HOH A . 
MA 8 HOH 178 3178 3178 HOH HOH A . 
MA 8 HOH 179 3179 3179 HOH HOH A . 
MA 8 HOH 180 3180 3180 HOH HOH A . 
MA 8 HOH 181 3181 3181 HOH HOH A . 
MA 8 HOH 182 3182 3182 HOH HOH A . 
MA 8 HOH 183 3183 3183 HOH HOH A . 
MA 8 HOH 184 3184 3184 HOH HOH A . 
MA 8 HOH 185 3185 3185 HOH HOH A . 
MA 8 HOH 186 3186 3186 HOH HOH A . 
MA 8 HOH 187 3187 3187 HOH HOH A . 
MA 8 HOH 188 3188 3188 HOH HOH A . 
MA 8 HOH 189 3189 3189 HOH HOH A . 
MA 8 HOH 190 3190 3190 HOH HOH A . 
MA 8 HOH 191 3191 3191 HOH HOH A . 
MA 8 HOH 192 3192 3192 HOH HOH A . 
MA 8 HOH 193 3193 3193 HOH HOH A . 
MA 8 HOH 194 3194 3194 HOH HOH A . 
MA 8 HOH 195 3195 3195 HOH HOH A . 
MA 8 HOH 196 3196 3196 HOH HOH A . 
MA 8 HOH 197 3197 3197 HOH HOH A . 
MA 8 HOH 198 3198 3198 HOH HOH A . 
MA 8 HOH 199 3199 3199 HOH HOH A . 
MA 8 HOH 200 3200 3200 HOH HOH A . 
MA 8 HOH 201 3201 3201 HOH HOH A . 
MA 8 HOH 202 3202 3202 HOH HOH A . 
MA 8 HOH 203 3203 3203 HOH HOH A . 
MA 8 HOH 204 3204 3204 HOH HOH A . 
MA 8 HOH 205 3205 3205 HOH HOH A . 
MA 8 HOH 206 3206 3206 HOH HOH A . 
MA 8 HOH 207 3207 3207 HOH HOH A . 
MA 8 HOH 208 3208 3208 HOH HOH A . 
MA 8 HOH 209 3209 3209 HOH HOH A . 
MA 8 HOH 210 3210 3210 HOH HOH A . 
MA 8 HOH 211 3211 3211 HOH HOH A . 
MA 8 HOH 212 3212 3212 HOH HOH A . 
MA 8 HOH 213 3213 3213 HOH HOH A . 
MA 8 HOH 214 3214 3214 HOH HOH A . 
MA 8 HOH 215 3215 3215 HOH HOH A . 
MA 8 HOH 216 3216 3216 HOH HOH A . 
MA 8 HOH 217 3217 3217 HOH HOH A . 
MA 8 HOH 218 3218 3218 HOH HOH A . 
MA 8 HOH 219 3219 3219 HOH HOH A . 
MA 8 HOH 220 3220 3220 HOH HOH A . 
MA 8 HOH 221 3221 3221 HOH HOH A . 
MA 8 HOH 222 3222 3222 HOH HOH A . 
MA 8 HOH 223 3223 3223 HOH HOH A . 
MA 8 HOH 224 3224 3224 HOH HOH A . 
MA 8 HOH 225 3225 3225 HOH HOH A . 
MA 8 HOH 226 3226 3226 HOH HOH A . 
MA 8 HOH 227 3227 3227 HOH HOH A . 
MA 8 HOH 228 3228 3228 HOH HOH A . 
MA 8 HOH 229 3229 3229 HOH HOH A . 
MA 8 HOH 230 3230 3230 HOH HOH A . 
MA 8 HOH 231 3231 3231 HOH HOH A . 
MA 8 HOH 232 3232 3232 HOH HOH A . 
MA 8 HOH 233 3233 3233 HOH HOH A . 
MA 8 HOH 234 3234 3234 HOH HOH A . 
MA 8 HOH 235 3235 3235 HOH HOH A . 
MA 8 HOH 236 3236 3236 HOH HOH A . 
MA 8 HOH 237 3237 3237 HOH HOH A . 
MA 8 HOH 238 3238 3238 HOH HOH A . 
MA 8 HOH 239 3239 3239 HOH HOH A . 
MA 8 HOH 240 3240 3240 HOH HOH A . 
MA 8 HOH 241 3241 3241 HOH HOH A . 
MA 8 HOH 242 3242 3242 HOH HOH A . 
MA 8 HOH 243 3243 3243 HOH HOH A . 
MA 8 HOH 244 3244 3244 HOH HOH A . 
MA 8 HOH 245 3245 3245 HOH HOH A . 
MA 8 HOH 246 3246 3246 HOH HOH A . 
MA 8 HOH 247 3247 3247 HOH HOH A . 
MA 8 HOH 248 3248 3248 HOH HOH A . 
MA 8 HOH 249 3249 3249 HOH HOH A . 
MA 8 HOH 250 3250 3250 HOH HOH A . 
MA 8 HOH 251 3251 3251 HOH HOH A . 
MA 8 HOH 252 3252 3252 HOH HOH A . 
MA 8 HOH 253 3253 3253 HOH HOH A . 
MA 8 HOH 254 3254 3254 HOH HOH A . 
MA 8 HOH 255 3255 3255 HOH HOH A . 
MA 8 HOH 256 3256 3256 HOH HOH A . 
MA 8 HOH 257 3257 3257 HOH HOH A . 
MA 8 HOH 258 3258 3258 HOH HOH A . 
MA 8 HOH 259 3259 3259 HOH HOH A . 
MA 8 HOH 260 3260 3260 HOH HOH A . 
MA 8 HOH 261 3261 3261 HOH HOH A . 
MA 8 HOH 262 3262 3262 HOH HOH A . 
MA 8 HOH 263 3263 3263 HOH HOH A . 
MA 8 HOH 264 3264 3264 HOH HOH A . 
MA 8 HOH 265 3265 3265 HOH HOH A . 
MA 8 HOH 266 3266 3266 HOH HOH A . 
MA 8 HOH 267 3267 3267 HOH HOH A . 
MA 8 HOH 268 3268 3268 HOH HOH A . 
MA 8 HOH 269 3269 3269 HOH HOH A . 
MA 8 HOH 270 3270 3270 HOH HOH A . 
MA 8 HOH 271 3271 3271 HOH HOH A . 
MA 8 HOH 272 3272 3272 HOH HOH A . 
MA 8 HOH 273 3273 3273 HOH HOH A . 
MA 8 HOH 274 3274 3274 HOH HOH A . 
MA 8 HOH 275 3275 3275 HOH HOH A . 
MA 8 HOH 276 3276 3276 HOH HOH A . 
MA 8 HOH 277 3277 3277 HOH HOH A . 
MA 8 HOH 278 3278 3278 HOH HOH A . 
NA 8 HOH 1   3001 3001 HOH HOH C . 
NA 8 HOH 2   3002 3002 HOH HOH C . 
NA 8 HOH 3   3003 3003 HOH HOH C . 
NA 8 HOH 4   3004 3004 HOH HOH C . 
NA 8 HOH 5   3005 3005 HOH HOH C . 
NA 8 HOH 6   3006 3006 HOH HOH C . 
NA 8 HOH 7   3007 3007 HOH HOH C . 
NA 8 HOH 8   3008 3008 HOH HOH C . 
NA 8 HOH 9   3009 3009 HOH HOH C . 
NA 8 HOH 10  3010 3010 HOH HOH C . 
NA 8 HOH 11  3011 3011 HOH HOH C . 
NA 8 HOH 12  3012 3012 HOH HOH C . 
NA 8 HOH 13  3013 3013 HOH HOH C . 
NA 8 HOH 14  3014 3014 HOH HOH C . 
NA 8 HOH 15  3015 3015 HOH HOH C . 
NA 8 HOH 16  3016 3016 HOH HOH C . 
NA 8 HOH 17  3017 3017 HOH HOH C . 
NA 8 HOH 18  3018 3018 HOH HOH C . 
NA 8 HOH 19  3019 3019 HOH HOH C . 
NA 8 HOH 20  3020 3020 HOH HOH C . 
NA 8 HOH 21  3021 3021 HOH HOH C . 
NA 8 HOH 22  3022 3022 HOH HOH C . 
NA 8 HOH 23  3023 3023 HOH HOH C . 
NA 8 HOH 24  3024 3024 HOH HOH C . 
NA 8 HOH 25  3025 3025 HOH HOH C . 
NA 8 HOH 26  3026 3026 HOH HOH C . 
NA 8 HOH 27  3027 3027 HOH HOH C . 
NA 8 HOH 28  3028 3028 HOH HOH C . 
NA 8 HOH 29  3029 3029 HOH HOH C . 
NA 8 HOH 30  3030 3030 HOH HOH C . 
NA 8 HOH 31  3031 3031 HOH HOH C . 
NA 8 HOH 32  3032 3032 HOH HOH C . 
NA 8 HOH 33  3033 3033 HOH HOH C . 
NA 8 HOH 34  3034 3034 HOH HOH C . 
NA 8 HOH 35  3035 3035 HOH HOH C . 
NA 8 HOH 36  3036 3036 HOH HOH C . 
NA 8 HOH 37  3037 3037 HOH HOH C . 
NA 8 HOH 38  3038 3038 HOH HOH C . 
NA 8 HOH 39  3039 3039 HOH HOH C . 
NA 8 HOH 40  3040 3040 HOH HOH C . 
NA 8 HOH 41  3041 3041 HOH HOH C . 
NA 8 HOH 42  3042 3042 HOH HOH C . 
NA 8 HOH 43  3043 3043 HOH HOH C . 
NA 8 HOH 44  3044 3044 HOH HOH C . 
NA 8 HOH 45  3045 3045 HOH HOH C . 
NA 8 HOH 46  3046 3046 HOH HOH C . 
NA 8 HOH 47  3047 3047 HOH HOH C . 
NA 8 HOH 48  3048 3048 HOH HOH C . 
NA 8 HOH 49  3049 3049 HOH HOH C . 
NA 8 HOH 50  3050 3050 HOH HOH C . 
NA 8 HOH 51  3051 3051 HOH HOH C . 
NA 8 HOH 52  3052 3052 HOH HOH C . 
NA 8 HOH 53  3053 3053 HOH HOH C . 
NA 8 HOH 54  3054 3054 HOH HOH C . 
NA 8 HOH 55  3055 3055 HOH HOH C . 
NA 8 HOH 56  3056 3056 HOH HOH C . 
NA 8 HOH 57  3057 3057 HOH HOH C . 
NA 8 HOH 58  3058 3058 HOH HOH C . 
NA 8 HOH 59  3059 3059 HOH HOH C . 
NA 8 HOH 60  3060 3060 HOH HOH C . 
NA 8 HOH 61  3061 3061 HOH HOH C . 
NA 8 HOH 62  3062 3062 HOH HOH C . 
NA 8 HOH 63  3063 3063 HOH HOH C . 
NA 8 HOH 64  3064 3064 HOH HOH C . 
NA 8 HOH 65  3065 3065 HOH HOH C . 
NA 8 HOH 66  3066 3066 HOH HOH C . 
NA 8 HOH 67  3067 3067 HOH HOH C . 
NA 8 HOH 68  3068 3068 HOH HOH C . 
NA 8 HOH 69  3069 3069 HOH HOH C . 
NA 8 HOH 70  3070 3070 HOH HOH C . 
NA 8 HOH 71  3071 3071 HOH HOH C . 
NA 8 HOH 72  3072 3072 HOH HOH C . 
NA 8 HOH 73  3073 3073 HOH HOH C . 
NA 8 HOH 74  3074 3074 HOH HOH C . 
NA 8 HOH 75  3075 3075 HOH HOH C . 
NA 8 HOH 76  3076 3076 HOH HOH C . 
NA 8 HOH 77  3077 3077 HOH HOH C . 
NA 8 HOH 78  3078 3078 HOH HOH C . 
NA 8 HOH 79  3079 3079 HOH HOH C . 
NA 8 HOH 80  3080 3080 HOH HOH C . 
NA 8 HOH 81  3081 3081 HOH HOH C . 
NA 8 HOH 82  3082 3082 HOH HOH C . 
NA 8 HOH 83  3083 3083 HOH HOH C . 
NA 8 HOH 84  3084 3084 HOH HOH C . 
NA 8 HOH 85  3085 3085 HOH HOH C . 
NA 8 HOH 86  3086 3086 HOH HOH C . 
NA 8 HOH 87  3087 3087 HOH HOH C . 
NA 8 HOH 88  3088 3088 HOH HOH C . 
NA 8 HOH 89  3089 3089 HOH HOH C . 
NA 8 HOH 90  3090 3090 HOH HOH C . 
NA 8 HOH 91  3091 3091 HOH HOH C . 
NA 8 HOH 92  3092 3092 HOH HOH C . 
NA 8 HOH 93  3093 3093 HOH HOH C . 
NA 8 HOH 94  3094 3094 HOH HOH C . 
NA 8 HOH 95  3095 3095 HOH HOH C . 
NA 8 HOH 96  3096 3096 HOH HOH C . 
NA 8 HOH 97  3097 3097 HOH HOH C . 
NA 8 HOH 98  3098 3098 HOH HOH C . 
NA 8 HOH 99  3099 3099 HOH HOH C . 
NA 8 HOH 100 3100 3100 HOH HOH C . 
NA 8 HOH 101 3101 3101 HOH HOH C . 
NA 8 HOH 102 3102 3102 HOH HOH C . 
NA 8 HOH 103 3103 3103 HOH HOH C . 
NA 8 HOH 104 3104 3104 HOH HOH C . 
NA 8 HOH 105 3105 3105 HOH HOH C . 
NA 8 HOH 106 3106 3106 HOH HOH C . 
NA 8 HOH 107 3107 3107 HOH HOH C . 
NA 8 HOH 108 3108 3108 HOH HOH C . 
NA 8 HOH 109 3109 3109 HOH HOH C . 
NA 8 HOH 110 3110 3110 HOH HOH C . 
NA 8 HOH 111 3111 3111 HOH HOH C . 
NA 8 HOH 112 3112 3112 HOH HOH C . 
NA 8 HOH 113 3113 3113 HOH HOH C . 
NA 8 HOH 114 3114 3114 HOH HOH C . 
NA 8 HOH 115 3115 3115 HOH HOH C . 
NA 8 HOH 116 3116 3116 HOH HOH C . 
NA 8 HOH 117 3117 3117 HOH HOH C . 
NA 8 HOH 118 3118 3118 HOH HOH C . 
NA 8 HOH 119 3119 3119 HOH HOH C . 
NA 8 HOH 120 3120 3120 HOH HOH C . 
NA 8 HOH 121 3121 3121 HOH HOH C . 
NA 8 HOH 122 3122 3122 HOH HOH C . 
NA 8 HOH 123 3123 3123 HOH HOH C . 
NA 8 HOH 124 3124 3124 HOH HOH C . 
NA 8 HOH 125 3125 3125 HOH HOH C . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A ASN 85  A ASN 85  ? ASN 'GLYCOSYLATION SITE'              
2  A ASN 103 A ASN 103 ? ASN 'GLYCOSYLATION SITE'              
3  A ASN 119 A ASN 119 ? ASN 'GLYCOSYLATION SITE'              
4  A ASN 219 A ASN 219 ? ASN 'GLYCOSYLATION SITE'              
5  A ASN 405 A ASN 405 ? ASN 'GLYCOSYLATION SITE'              
6  A ASN 431 A ASN 431 ? ASN 'GLYCOSYLATION SITE'              
7  A ASN 650 A ASN 650 ? ASN 'GLYCOSYLATION SITE'              
8  A ASN 714 A ASN 714 ? ASN 'GLYCOSYLATION SITE'              
9  B ASN 85  C ASN 85  ? ASN 'GLYCOSYLATION SITE'              
10 B ASN 103 C ASN 103 ? ASN 'GLYCOSYLATION SITE'              
11 B ASN 219 C ASN 219 ? ASN 'GLYCOSYLATION SITE'              
12 B ASN 294 C ASN 294 ? ASN 'GLYCOSYLATION SITE'              
13 B ASN 405 C ASN 405 ? ASN 'GLYCOSYLATION SITE'              
14 B ASN 431 C ASN 431 ? ASN 'GLYCOSYLATION SITE'              
15 B ASN 650 C ASN 650 ? ASN 'GLYCOSYLATION SITE'              
16 B ASN 714 C ASN 714 ? ASN 'GLYCOSYLATION SITE'              
17 C LYN 10  E LYN 10  ? LYS '2,6-DIAMINO-HEXANOIC ACID AMIDE' 
18 D LYN 10  F LYN 10  ? LYS '2,6-DIAMINO-HEXANOIC ACID AMIDE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,MA         
2 1 B,D,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,NA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5850  ? 
1 MORE         -3.8  ? 
1 'SSA (A^2)'  37630 ? 
2 'ABSA (A^2)' 5160  ? 
2 MORE         -11.5 ? 
2 'SSA (A^2)'  35400 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 370 ? A HIS 370 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 OE1 ? A GLU 393 ? A GLU 393 ? 1_555 86.9  ? 
2  NE2 ? A HIS 370 ? A HIS 370 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 NE2 ? A HIS 374 ? A HIS 374 ? 1_555 105.8 ? 
3  OE1 ? A GLU 393 ? A GLU 393 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 NE2 ? A HIS 374 ? A HIS 374 ? 1_555 95.0  ? 
4  NE2 ? A HIS 370 ? A HIS 370 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 OE2 ? A GLU 393 ? A GLU 393 ? 1_555 141.8 ? 
5  OE1 ? A GLU 393 ? A GLU 393 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 OE2 ? A GLU 393 ? A GLU 393 ? 1_555 60.6  ? 
6  NE2 ? A HIS 374 ? A HIS 374 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 OE2 ? A GLU 393 ? A GLU 393 ? 1_555 97.1  ? 
7  NE2 ? A HIS 370 ? A HIS 370 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 O12 ? C 2X0 1   ? E 2X0 1   ? 1_555 103.4 ? 
8  OE1 ? A GLU 393 ? A GLU 393 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 O12 ? C 2X0 1   ? E 2X0 1   ? 1_555 110.5 ? 
9  NE2 ? A HIS 374 ? A HIS 374 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 O12 ? C 2X0 1   ? E 2X0 1   ? 1_555 142.0 ? 
10 OE2 ? A GLU 393 ? A GLU 393 ? 1_555 ZN ? E  ZN . ? A ZN 1008 ? 1_555 O12 ? C 2X0 1   ? E 2X0 1   ? 1_555 73.4  ? 
11 NE2 ? B HIS 374 ? C HIS 374 ? 1_555 ZN ? JA ZN . ? C ZN 1020 ? 1_555 OE1 ? B GLU 393 ? C GLU 393 ? 1_555 102.9 ? 
12 NE2 ? B HIS 374 ? C HIS 374 ? 1_555 ZN ? JA ZN . ? C ZN 1020 ? 1_555 NE2 ? B HIS 370 ? C HIS 370 ? 1_555 102.9 ? 
13 OE1 ? B GLU 393 ? C GLU 393 ? 1_555 ZN ? JA ZN . ? C ZN 1020 ? 1_555 NE2 ? B HIS 370 ? C HIS 370 ? 1_555 113.8 ? 
14 NE2 ? B HIS 374 ? C HIS 374 ? 1_555 ZN ? JA ZN . ? C ZN 1020 ? 1_555 O12 ? D 2X0 1   ? F 2X0 1   ? 1_555 142.6 ? 
15 OE1 ? B GLU 393 ? C GLU 393 ? 1_555 ZN ? JA ZN . ? C ZN 1020 ? 1_555 O12 ? D 2X0 1   ? F 2X0 1   ? 1_555 96.7  ? 
16 NE2 ? B HIS 370 ? C HIS 370 ? 1_555 ZN ? JA ZN . ? C ZN 1020 ? 1_555 O12 ? D 2X0 1   ? F 2X0 1   ? 1_555 97.8  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-09-30 
2 'Structure model' 1 1 2015-11-11 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
PHENIX refinement       '(PHENIX.REFINE)' ? 1 
XDS    'data reduction' .                 ? 2 
XDS    'data scaling'   .                 ? 3 
MOLREP phasing          .                 ? 4 
# 
_pdbx_entry_details.entry_id             5AB0 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     'CORRESPONDS TO VARIANT RS2549782' 
# 
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   C MET 957  ? ? OG1 C THR 960  ? ? 0.95 
2  1 C   C MET 957  ? ? OG1 C THR 960  ? ? 1.76 
3  1 OE2 A GLU 720  ? ? O   A HOH 3217 ? ? 1.86 
4  1 OD1 A ASP 291  ? ? O   A HOH 3095 ? ? 1.95 
5  1 OE1 A GLU 472  ? ? O   A HOH 3159 ? ? 1.95 
6  1 OE1 A GLU 213  ? ? O   A HOH 3006 ? ? 2.01 
7  1 OD2 C ASP 174  ? ? O   C HOH 3027 ? ? 2.01 
8  1 O   A HOH 3137 ? ? O   A HOH 3139 ? ? 2.02 
9  1 OE1 A GLN 563  ? ? O   A HOH 3178 ? ? 2.02 
10 1 O   A HOH 3237 ? ? O   A HOH 3238 ? ? 2.02 
11 1 O   C ARG 488  ? ? O   C HOH 3043 ? ? 2.04 
12 1 O   C HOH 3066 ? ? O   C HOH 3103 ? ? 2.07 
13 1 OE2 A GLU 576  ? ? O   A HOH 3183 ? ? 2.07 
14 1 C2  C BMA 1001 ? ? O4  C NAG 1004 ? ? 2.07 
15 1 O   A HOH 3125 ? ? O   A HOH 3230 ? ? 2.09 
16 1 O   A HOH 3118 ? ? O   A HOH 3233 ? ? 2.09 
17 1 O   C TYR 162  ? ? O   C HOH 3014 ? ? 2.09 
18 1 O   C HOH 3023 ? ? O   C HOH 3050 ? ? 2.10 
19 1 O   C GLU 919  ? ? O   C HOH 3112 ? ? 2.10 
20 1 OG1 C THR 951  ? ? O   C HOH 3115 ? ? 2.10 
21 1 OD2 C ASP 90   ? ? O   C HOH 3011 ? ? 2.10 
22 1 OD2 C ASP 198  ? ? O   C HOH 3034 ? ? 2.11 
23 1 O   A HOH 3127 ? ? O   A HOH 3128 ? ? 2.11 
24 1 OG1 C THR 442  ? ? O   C HOH 3078 ? ? 2.11 
25 1 OD2 C ASP 717  ? ? NH1 C ARG 953  ? ? 2.12 
26 1 O   A HOH 3098 ? ? O   A HOH 3203 ? ? 2.12 
27 1 O   A HOH 3215 ? ? O   A HOH 3258 ? ? 2.13 
28 1 O   A HOH 3028 ? ? O   A HOH 3090 ? ? 2.13 
29 1 O   C HOH 3033 ? ? O   C HOH 3034 ? ? 2.14 
30 1 N   A HIS 964  ? ? O   A HOH 3268 ? ? 2.14 
31 1 O4  A NAG 1069 ? ? O   A HOH 3269 ? ? 2.15 
32 1 OD2 A ASP 414  ? ? O   A HOH 3141 ? ? 2.15 
33 1 NZ  A LYS 438  ? ? O   A HOH 3148 ? ? 2.15 
34 1 OE2 C GLU 452  ? ? O   C HOH 3081 ? ? 2.16 
35 1 O   A HOH 3143 ? ? O   A HOH 3155 ? ? 2.16 
36 1 OG1 C THR 118  ? ? O   C HOH 3019 ? ? 2.16 
37 1 OG  A SER 692  ? ? O   A HOH 3197 ? ? 2.17 
38 1 O   C ASP 641  ? ? OG1 C THR 645  ? ? 2.17 
39 1 O   C VAL 670  ? ? O   C HOH 3093 ? ? 2.17 
40 1 OE2 A GLU 200  ? ? O   A HOH 3052 ? ? 2.17 
41 1 O   A HOH 3110 ? ? O   A HOH 3111 ? ? 2.18 
42 1 O   C LYS 792  ? ? OG  C SER 796  ? ? 2.18 
43 1 O   F LYS 3    ? ? N   F HIS 5    ? ? 2.19 
44 1 O   C HOH 3005 ? ? O   C HOH 3012 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ILE 
_pdbx_validate_rmsd_angle.auth_seq_id_1              328 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              329 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              329 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                129.01 
_pdbx_validate_rmsd_angle.angle_target_value         119.30 
_pdbx_validate_rmsd_angle.angle_deviation            9.71 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 58  ? ? -85.08  45.01   
2  1 ASN A 58  ? ? -92.06  53.56   
3  1 GLU A 60  ? ? 65.74   125.67  
4  1 PRO A 63  ? ? -56.88  -2.40   
5  1 LYS A 132 ? ? -37.56  132.02  
6  1 LYS A 155 ? ? -33.62  119.88  
7  1 PHE A 176 ? ? 69.55   -6.41   
8  1 GLU A 245 ? A -43.21  -74.44  
9  1 ASN A 338 ? ? -39.47  127.29  
10 1 LEU A 349 ? ? -131.03 -42.37  
11 1 ASN A 379 ? ? -92.41  -63.38  
12 1 TYR A 408 ? ? -141.40 55.59   
13 1 GLU A 441 ? ? -133.69 -51.78  
14 1 TYR A 455 ? ? -88.48  -72.45  
15 1 ARG A 488 ? ? -152.16 -146.81 
16 1 GLU A 505 ? ? 34.05   61.78   
17 1 SER A 506 ? ? 48.55   -123.02 
18 1 SER A 510 ? ? 48.06   106.67  
19 1 HIS A 515 ? ? -120.16 -69.24  
20 1 SER A 516 ? ? -12.28  -90.64  
21 1 SER A 558 ? ? -113.63 74.07   
22 1 GLU A 582 ? ? 36.69   -132.85 
23 1 HIS A 603 ? ? -176.59 132.59  
24 1 GLU A 616 ? ? 87.61   -15.20  
25 1 SER A 619 ? ? -68.87  -74.12  
26 1 ASN A 624 ? ? 51.81   76.56   
27 1 LEU A 687 ? ? -56.58  -7.06   
28 1 GLN A 728 ? ? -93.12  -60.73  
29 1 PHE A 730 ? ? 103.17  3.37    
30 1 LYS A 848 ? ? -88.81  -73.43  
31 1 ASN A 879 ? ? -145.50 26.65   
32 1 SER A 906 ? ? -145.02 17.52   
33 1 ALA A 923 ? ? 60.32   89.04   
34 1 ARG A 961 ? ? -82.26  -76.67  
35 1 GLU C 60  ? ? 65.06   164.35  
36 1 PRO C 63  ? ? -68.34  29.19   
37 1 TRP C 64  ? ? -170.05 130.98  
38 1 ASN C 103 ? ? 179.06  134.48  
39 1 GLU C 126 ? ? -130.91 -60.52  
40 1 SER C 128 ? ? -65.18  8.96    
41 1 ASP C 198 ? ? -161.33 116.65  
42 1 ASP C 212 ? ? -90.80  57.37   
43 1 VAL C 257 ? ? -55.05  171.63  
44 1 SER C 289 ? ? -37.60  137.38  
45 1 PRO C 353 ? ? -62.51  13.14   
46 1 LYS C 438 ? ? 179.69  130.63  
47 1 GLU C 441 ? ? -110.45 -77.67  
48 1 GLU C 530 ? ? 81.20   162.91  
49 1 ASN C 531 ? ? 70.17   -61.29  
50 1 ALA C 579 ? ? 64.00   128.60  
51 1 GLN C 581 ? ? -168.48 -35.94  
52 1 ASN C 624 ? ? 59.10   77.81   
53 1 HIS C 638 ? ? -96.40  33.84   
54 1 GLN C 649 ? ? -85.11  -92.66  
55 1 HIS C 689 ? ? 93.71   2.81    
56 1 GLN C 728 ? ? -53.41  -74.92  
57 1 PHE C 730 ? ? 82.90   41.06   
58 1 TRP C 739 ? ? -110.08 72.15   
59 1 SER C 744 ? ? -67.46  -172.16 
60 1 ASN C 762 ? ? 82.46   88.04   
61 1 THR C 902 ? ? -141.69 -21.81  
62 1 GLN C 924 ? ? 74.33   -77.18  
63 1 HIS E 4   ? ? -49.77  40.09   
64 1 PHE E 7   ? ? 33.92   40.50   
65 1 PHE E 9   ? ? -140.88 -127.92 
66 1 HIS F 4   ? ? -47.81  59.57   
67 1 HIS F 5   ? ? -87.48  46.55   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    889 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    890 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            33.26 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       3131 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.00 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 HIS 964 ? CA  ? A HIS 964 CA  
2  1 Y 1 A HIS 964 ? C   ? A HIS 964 C   
3  1 Y 1 A HIS 964 ? O   ? A HIS 964 O   
4  1 Y 1 A HIS 964 ? CB  ? A HIS 964 CB  
5  1 Y 1 A HIS 964 ? CG  ? A HIS 964 CG  
6  1 Y 1 A HIS 964 ? ND1 ? A HIS 964 ND1 
7  1 Y 1 A HIS 964 ? CD2 ? A HIS 964 CD2 
8  1 Y 1 A HIS 964 ? CE1 ? A HIS 964 CE1 
9  1 Y 1 A HIS 964 ? NE2 ? A HIS 964 NE2 
10 1 Y 1 C HIS 962 ? CA  ? B HIS 962 CA  
11 1 Y 1 C HIS 962 ? C   ? B HIS 962 C   
12 1 Y 1 C HIS 962 ? O   ? B HIS 962 O   
13 1 Y 1 C HIS 962 ? CB  ? B HIS 962 CB  
14 1 Y 1 C HIS 962 ? CG  ? B HIS 962 CG  
15 1 Y 1 C HIS 962 ? ND1 ? B HIS 962 ND1 
16 1 Y 1 C HIS 962 ? CD2 ? B HIS 962 CD2 
17 1 Y 1 C HIS 962 ? CE1 ? B HIS 962 CE1 
18 1 Y 1 C HIS 962 ? NE2 ? B HIS 962 NE2 
# 
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 1   ? A MET 1   
2   1 Y 1 A PHE 2   ? A PHE 2   
3   1 Y 1 A HIS 3   ? A HIS 3   
4   1 Y 1 A SER 4   ? A SER 4   
5   1 Y 1 A SER 5   ? A SER 5   
6   1 Y 1 A ALA 6   ? A ALA 6   
7   1 Y 1 A MET 7   ? A MET 7   
8   1 Y 1 A VAL 8   ? A VAL 8   
9   1 Y 1 A ASN 9   ? A ASN 9   
10  1 Y 1 A SER 10  ? A SER 10  
11  1 Y 1 A HIS 11  ? A HIS 11  
12  1 Y 1 A ARG 12  ? A ARG 12  
13  1 Y 1 A LYS 13  ? A LYS 13  
14  1 Y 1 A PRO 14  ? A PRO 14  
15  1 Y 1 A MET 15  ? A MET 15  
16  1 Y 1 A PHE 16  ? A PHE 16  
17  1 Y 1 A ASN 17  ? A ASN 17  
18  1 Y 1 A ILE 18  ? A ILE 18  
19  1 Y 1 A HIS 19  ? A HIS 19  
20  1 Y 1 A ARG 20  ? A ARG 20  
21  1 Y 1 A GLY 21  ? A GLY 21  
22  1 Y 1 A PHE 22  ? A PHE 22  
23  1 Y 1 A TYR 23  ? A TYR 23  
24  1 Y 1 A CYS 24  ? A CYS 24  
25  1 Y 1 A LEU 25  ? A LEU 25  
26  1 Y 1 A THR 26  ? A THR 26  
27  1 Y 1 A ALA 27  ? A ALA 27  
28  1 Y 1 A ILE 28  ? A ILE 28  
29  1 Y 1 A LEU 29  ? A LEU 29  
30  1 Y 1 A PRO 30  ? A PRO 30  
31  1 Y 1 A GLN 31  ? A GLN 31  
32  1 Y 1 A ILE 32  ? A ILE 32  
33  1 Y 1 A CYS 33  ? A CYS 33  
34  1 Y 1 A ILE 34  ? A ILE 34  
35  1 Y 1 A CYS 35  ? A CYS 35  
36  1 Y 1 A SER 36  ? A SER 36  
37  1 Y 1 A GLN 37  ? A GLN 37  
38  1 Y 1 A PHE 38  ? A PHE 38  
39  1 Y 1 A SER 39  ? A SER 39  
40  1 Y 1 A VAL 40  ? A VAL 40  
41  1 Y 1 A PRO 41  ? A PRO 41  
42  1 Y 1 A SER 42  ? A SER 42  
43  1 Y 1 A SER 43  ? A SER 43  
44  1 Y 1 A TYR 44  ? A TYR 44  
45  1 Y 1 A HIS 45  ? A HIS 45  
46  1 Y 1 A PHE 46  ? A PHE 46  
47  1 Y 1 A THR 47  ? A THR 47  
48  1 Y 1 A GLU 48  ? A GLU 48  
49  1 Y 1 A ASP 49  ? A ASP 49  
50  1 Y 1 A PRO 50  ? A PRO 50  
51  1 Y 1 A GLY 51  ? A GLY 51  
52  1 Y 1 A ALA 52  ? A ALA 52  
53  1 Y 1 A PHE 53  ? A PHE 53  
54  1 Y 1 A HIS 965 ? A HIS 965 
55  1 Y 1 A HIS 966 ? A HIS 966 
56  1 Y 1 A HIS 967 ? A HIS 967 
57  1 Y 1 C MET 1   ? B MET 1   
58  1 Y 1 C PHE 2   ? B PHE 2   
59  1 Y 1 C HIS 3   ? B HIS 3   
60  1 Y 1 C SER 4   ? B SER 4   
61  1 Y 1 C SER 5   ? B SER 5   
62  1 Y 1 C ALA 6   ? B ALA 6   
63  1 Y 1 C MET 7   ? B MET 7   
64  1 Y 1 C VAL 8   ? B VAL 8   
65  1 Y 1 C ASN 9   ? B ASN 9   
66  1 Y 1 C SER 10  ? B SER 10  
67  1 Y 1 C HIS 11  ? B HIS 11  
68  1 Y 1 C ARG 12  ? B ARG 12  
69  1 Y 1 C LYS 13  ? B LYS 13  
70  1 Y 1 C PRO 14  ? B PRO 14  
71  1 Y 1 C MET 15  ? B MET 15  
72  1 Y 1 C PHE 16  ? B PHE 16  
73  1 Y 1 C ASN 17  ? B ASN 17  
74  1 Y 1 C ILE 18  ? B ILE 18  
75  1 Y 1 C HIS 19  ? B HIS 19  
76  1 Y 1 C ARG 20  ? B ARG 20  
77  1 Y 1 C GLY 21  ? B GLY 21  
78  1 Y 1 C PHE 22  ? B PHE 22  
79  1 Y 1 C TYR 23  ? B TYR 23  
80  1 Y 1 C CYS 24  ? B CYS 24  
81  1 Y 1 C LEU 25  ? B LEU 25  
82  1 Y 1 C THR 26  ? B THR 26  
83  1 Y 1 C ALA 27  ? B ALA 27  
84  1 Y 1 C ILE 28  ? B ILE 28  
85  1 Y 1 C LEU 29  ? B LEU 29  
86  1 Y 1 C PRO 30  ? B PRO 30  
87  1 Y 1 C GLN 31  ? B GLN 31  
88  1 Y 1 C ILE 32  ? B ILE 32  
89  1 Y 1 C CYS 33  ? B CYS 33  
90  1 Y 1 C ILE 34  ? B ILE 34  
91  1 Y 1 C CYS 35  ? B CYS 35  
92  1 Y 1 C SER 36  ? B SER 36  
93  1 Y 1 C GLN 37  ? B GLN 37  
94  1 Y 1 C PHE 38  ? B PHE 38  
95  1 Y 1 C SER 39  ? B SER 39  
96  1 Y 1 C VAL 40  ? B VAL 40  
97  1 Y 1 C PRO 41  ? B PRO 41  
98  1 Y 1 C SER 42  ? B SER 42  
99  1 Y 1 C SER 43  ? B SER 43  
100 1 Y 1 C TYR 44  ? B TYR 44  
101 1 Y 1 C HIS 45  ? B HIS 45  
102 1 Y 1 C PHE 46  ? B PHE 46  
103 1 Y 1 C THR 47  ? B THR 47  
104 1 Y 1 C GLU 48  ? B GLU 48  
105 1 Y 1 C ASP 49  ? B ASP 49  
106 1 Y 1 C PRO 50  ? B PRO 50  
107 1 Y 1 C GLY 51  ? B GLY 51  
108 1 Y 1 C ALA 52  ? B ALA 52  
109 1 Y 1 C PHE 53  ? B PHE 53  
110 1 Y 1 C SER 502 ? B SER 502 
111 1 Y 1 C CYS 503 ? B CYS 503 
112 1 Y 1 C LEU 504 ? B LEU 504 
113 1 Y 1 C GLU 505 ? B GLU 505 
114 1 Y 1 C SER 506 ? B SER 506 
115 1 Y 1 C ASP 507 ? B ASP 507 
116 1 Y 1 C PHE 508 ? B PHE 508 
117 1 Y 1 C THR 509 ? B THR 509 
118 1 Y 1 C SER 510 ? B SER 510 
119 1 Y 1 C GLY 511 ? B GLY 511 
120 1 Y 1 C GLY 512 ? B GLY 512 
121 1 Y 1 C VAL 513 ? B VAL 513 
122 1 Y 1 C CYS 514 ? B CYS 514 
123 1 Y 1 C HIS 515 ? B HIS 515 
124 1 Y 1 C SER 516 ? B SER 516 
125 1 Y 1 C ASP 517 ? B ASP 517 
126 1 Y 1 C PRO 518 ? B PRO 518 
127 1 Y 1 C LYS 519 ? B LYS 519 
128 1 Y 1 C MET 520 ? B MET 520 
129 1 Y 1 C THR 521 ? B THR 521 
130 1 Y 1 C SER 522 ? B SER 522 
131 1 Y 1 C ASN 523 ? B ASN 523 
132 1 Y 1 C MET 524 ? B MET 524 
133 1 Y 1 C LEU 525 ? B LEU 525 
134 1 Y 1 C ALA 526 ? B ALA 526 
135 1 Y 1 C PHE 527 ? B PHE 527 
136 1 Y 1 C LEU 528 ? B LEU 528 
137 1 Y 1 C HIS 963 ? B HIS 963 
138 1 Y 1 C HIS 964 ? B HIS 964 
139 1 Y 1 C HIS 965 ? B HIS 965 
140 1 Y 1 C HIS 966 ? B HIS 966 
141 1 Y 1 C HIS 967 ? B HIS 967 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'ZINC ION'                             ZN  
4 N-ACETYL-D-GLUCOSAMINE                 NAG 
5 BETA-D-MANNOSE                         BMA 
6 1,2-ETHANEDIOL                         EDO 
7 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
8 water                                  HOH 
# 
