data_3CTT
# 
_entry.id   3CTT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3CTT         
RCSB  RCSB047200   
WWPDB D_1000047200 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2qly 'Apo enzyme'                           unspecified 
PDB 2qmj 'Same enzyme in complex with Acarbose' unspecified 
# 
_pdbx_database_status.entry_id                        3CTT 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2008-04-14 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Sim, L.'    1 
'Rose, D.R.' 2 
# 
_citation.id                        primary 
_citation.title                     
;Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families
;
_citation.journal_abbrev            Chemistry 
_citation.journal_volume            15 
_citation.page_first                1627 
_citation.page_last                 1636 
_citation.year                      2009 
_citation.journal_id_ASTM           ? 
_citation.country                   GE 
_citation.journal_id_ISSN           0947-6539 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19123216 
_citation.pdbx_database_id_DOI      10.1002/chem.200801578 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Cardona, F.'     1  
primary 'Parmeggiani, C.' 2  
primary 'Faggi, E.'       3  
primary 'Bonaccini, C.'   4  
primary 'Gratteri, P.'    5  
primary 'Sim, L.'         6  
primary 'Gloster, T.M.'   7  
primary 'Roberts, S.'     8  
primary 'Davies, G.J.'    9  
primary 'Rose, D.R.'      10 
primary 'Goti, A.'        11 
# 
_cell.length_a           86.692 
_cell.length_b           109.131 
_cell.length_c           109.438 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           3CTT 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              4 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.entry_id                         3CTT 
_symmetry.Int_Tables_number                19 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
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 Maltase-glucoamylase   98585.992 1   3.2.1.20 ? 'N-terminal subunit (UNP residues 87-954)' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   2   ?        ? ?                                          ? 
3 non-polymer syn 'SULFATE ION'          96.063    1   ?        ? ?                                          ? 
4 non-polymer syn CASUARINE              205.208   1   ?        ? ?                                          ? 
5 non-polymer syn GLYCEROL               92.094    9   ?        ? ?                                          ? 
6 water       nat water                  18.015    352 ?        ? ?                                          ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ALA n 
1 3   GLU n 
1 4   CYS n 
1 5   PRO n 
1 6   VAL n 
1 7   VAL n 
1 8   ASN n 
1 9   GLU n 
1 10  LEU n 
1 11  GLU n 
1 12  ARG n 
1 13  ILE n 
1 14  ASN n 
1 15  CYS n 
1 16  ILE n 
1 17  PRO n 
1 18  ASP n 
1 19  GLN n 
1 20  PRO n 
1 21  PRO n 
1 22  THR n 
1 23  LYS n 
1 24  ALA n 
1 25  THR n 
1 26  CYS n 
1 27  ASP n 
1 28  GLN n 
1 29  ARG n 
1 30  GLY n 
1 31  CYS n 
1 32  CYS n 
1 33  TRP n 
1 34  ASN n 
1 35  PRO n 
1 36  GLN n 
1 37  GLY n 
1 38  ALA n 
1 39  VAL n 
1 40  SER n 
1 41  VAL n 
1 42  PRO n 
1 43  TRP n 
1 44  CYS n 
1 45  TYR n 
1 46  TYR n 
1 47  SER n 
1 48  LYS n 
1 49  ASN n 
1 50  HIS n 
1 51  SER n 
1 52  TYR n 
1 53  HIS n 
1 54  VAL n 
1 55  GLU n 
1 56  GLY n 
1 57  ASN n 
1 58  LEU n 
1 59  VAL n 
1 60  ASN n 
1 61  THR n 
1 62  ASN n 
1 63  ALA n 
1 64  GLY n 
1 65  PHE n 
1 66  THR n 
1 67  ALA n 
1 68  ARG n 
1 69  LEU n 
1 70  LYS n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  SER n 
1 76  PRO n 
1 77  VAL n 
1 78  PHE n 
1 79  GLY n 
1 80  SER n 
1 81  ASN n 
1 82  VAL n 
1 83  ASP n 
1 84  ASN n 
1 85  VAL n 
1 86  LEU n 
1 87  LEU n 
1 88  THR n 
1 89  ALA n 
1 90  GLU n 
1 91  TYR n 
1 92  GLN n 
1 93  THR n 
1 94  SER n 
1 95  ASN n 
1 96  ARG n 
1 97  PHE n 
1 98  HIS n 
1 99  PHE n 
1 100 LYS n 
1 101 LEU n 
1 102 THR n 
1 103 ASP n 
1 104 GLN n 
1 105 THR n 
1 106 ASN n 
1 107 ASN n 
1 108 ARG n 
1 109 PHE n 
1 110 GLU n 
1 111 VAL n 
1 112 PRO n 
1 113 HIS n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 GLN n 
1 118 SER n 
1 119 PHE n 
1 120 SER n 
1 121 GLY n 
1 122 ASN n 
1 123 ALA n 
1 124 ALA n 
1 125 ALA n 
1 126 SER n 
1 127 LEU n 
1 128 THR n 
1 129 TYR n 
1 130 GLN n 
1 131 VAL n 
1 132 GLU n 
1 133 ILE n 
1 134 SER n 
1 135 ARG n 
1 136 GLN n 
1 137 PRO n 
1 138 PHE n 
1 139 SER n 
1 140 ILE n 
1 141 LYS n 
1 142 VAL n 
1 143 THR n 
1 144 ARG n 
1 145 ARG n 
1 146 SER n 
1 147 ASN n 
1 148 ASN n 
1 149 ARG n 
1 150 VAL n 
1 151 LEU n 
1 152 PHE n 
1 153 ASP n 
1 154 SER n 
1 155 SER n 
1 156 ILE n 
1 157 GLY n 
1 158 PRO n 
1 159 LEU n 
1 160 LEU n 
1 161 PHE n 
1 162 ALA n 
1 163 ASP n 
1 164 GLN n 
1 165 PHE n 
1 166 LEU n 
1 167 GLN n 
1 168 LEU n 
1 169 SER n 
1 170 THR n 
1 171 ARG n 
1 172 LEU n 
1 173 PRO n 
1 174 SER n 
1 175 THR n 
1 176 ASN n 
1 177 VAL n 
1 178 TYR n 
1 179 GLY n 
1 180 LEU n 
1 181 GLY n 
1 182 GLU n 
1 183 HIS n 
1 184 VAL n 
1 185 HIS n 
1 186 GLN n 
1 187 GLN n 
1 188 TYR n 
1 189 ARG n 
1 190 HIS n 
1 191 ASP n 
1 192 MET n 
1 193 ASN n 
1 194 TRP n 
1 195 LYS n 
1 196 THR n 
1 197 TRP n 
1 198 PRO n 
1 199 ILE n 
1 200 PHE n 
1 201 ASN n 
1 202 ARG n 
1 203 ASP n 
1 204 THR n 
1 205 THR n 
1 206 PRO n 
1 207 ASN n 
1 208 GLY n 
1 209 ASN n 
1 210 GLY n 
1 211 THR n 
1 212 ASN n 
1 213 LEU n 
1 214 TYR n 
1 215 GLY n 
1 216 ALA n 
1 217 GLN n 
1 218 THR n 
1 219 PHE n 
1 220 PHE n 
1 221 LEU n 
1 222 CYS n 
1 223 LEU n 
1 224 GLU n 
1 225 ASP n 
1 226 ALA n 
1 227 SER n 
1 228 GLY n 
1 229 LEU n 
1 230 SER n 
1 231 PHE n 
1 232 GLY n 
1 233 VAL n 
1 234 PHE n 
1 235 LEU n 
1 236 MET n 
1 237 ASN n 
1 238 SER n 
1 239 ASN n 
1 240 ALA n 
1 241 MET n 
1 242 GLU n 
1 243 VAL n 
1 244 VAL n 
1 245 LEU n 
1 246 GLN n 
1 247 PRO n 
1 248 ALA n 
1 249 PRO n 
1 250 ALA n 
1 251 ILE n 
1 252 THR n 
1 253 TYR n 
1 254 ARG n 
1 255 THR n 
1 256 ILE n 
1 257 GLY n 
1 258 GLY n 
1 259 ILE n 
1 260 LEU n 
1 261 ASP n 
1 262 PHE n 
1 263 TYR n 
1 264 VAL n 
1 265 PHE n 
1 266 LEU n 
1 267 GLY n 
1 268 ASN n 
1 269 THR n 
1 270 PRO n 
1 271 GLU n 
1 272 GLN n 
1 273 VAL n 
1 274 VAL n 
1 275 GLN n 
1 276 GLU n 
1 277 TYR n 
1 278 LEU n 
1 279 GLU n 
1 280 LEU n 
1 281 ILE n 
1 282 GLY n 
1 283 ARG n 
1 284 PRO n 
1 285 ALA n 
1 286 LEU n 
1 287 PRO n 
1 288 SER n 
1 289 TYR n 
1 290 TRP n 
1 291 ALA n 
1 292 LEU n 
1 293 GLY n 
1 294 PHE n 
1 295 HIS n 
1 296 LEU n 
1 297 SER n 
1 298 ARG n 
1 299 TYR n 
1 300 GLU n 
1 301 TYR n 
1 302 GLY n 
1 303 THR n 
1 304 LEU n 
1 305 ASP n 
1 306 ASN n 
1 307 MET n 
1 308 ARG n 
1 309 GLU n 
1 310 VAL n 
1 311 VAL n 
1 312 GLU n 
1 313 ARG n 
1 314 ASN n 
1 315 ARG n 
1 316 ALA n 
1 317 ALA n 
1 318 GLN n 
1 319 LEU n 
1 320 PRO n 
1 321 TYR n 
1 322 ASP n 
1 323 VAL n 
1 324 GLN n 
1 325 HIS n 
1 326 ALA n 
1 327 ASP n 
1 328 ILE n 
1 329 ASP n 
1 330 TYR n 
1 331 MET n 
1 332 ASP n 
1 333 GLU n 
1 334 ARG n 
1 335 ARG n 
1 336 ASP n 
1 337 PHE n 
1 338 THR n 
1 339 TYR n 
1 340 ASP n 
1 341 SER n 
1 342 VAL n 
1 343 ASP n 
1 344 PHE n 
1 345 LYS n 
1 346 GLY n 
1 347 PHE n 
1 348 PRO n 
1 349 GLU n 
1 350 PHE n 
1 351 VAL n 
1 352 ASN n 
1 353 GLU n 
1 354 LEU n 
1 355 HIS n 
1 356 ASN n 
1 357 ASN n 
1 358 GLY n 
1 359 GLN n 
1 360 LYS n 
1 361 LEU n 
1 362 VAL n 
1 363 ILE n 
1 364 ILE n 
1 365 VAL n 
1 366 ASP n 
1 367 PRO n 
1 368 ALA n 
1 369 ILE n 
1 370 SER n 
1 371 ASN n 
1 372 ASN n 
1 373 SER n 
1 374 SER n 
1 375 SER n 
1 376 SER n 
1 377 LYS n 
1 378 PRO n 
1 379 TYR n 
1 380 GLY n 
1 381 PRO n 
1 382 TYR n 
1 383 ASP n 
1 384 ARG n 
1 385 GLY n 
1 386 SER n 
1 387 ASP n 
1 388 MET n 
1 389 LYS n 
1 390 ILE n 
1 391 TRP n 
1 392 VAL n 
1 393 ASN n 
1 394 SER n 
1 395 SER n 
1 396 ASP n 
1 397 GLY n 
1 398 VAL n 
1 399 THR n 
1 400 PRO n 
1 401 LEU n 
1 402 ILE n 
1 403 GLY n 
1 404 GLU n 
1 405 VAL n 
1 406 TRP n 
1 407 PRO n 
1 408 GLY n 
1 409 GLN n 
1 410 THR n 
1 411 VAL n 
1 412 PHE n 
1 413 PRO n 
1 414 ASP n 
1 415 TYR n 
1 416 THR n 
1 417 ASN n 
1 418 PRO n 
1 419 ASN n 
1 420 CYS n 
1 421 ALA n 
1 422 VAL n 
1 423 TRP n 
1 424 TRP n 
1 425 THR n 
1 426 LYS n 
1 427 GLU n 
1 428 PHE n 
1 429 GLU n 
1 430 LEU n 
1 431 PHE n 
1 432 HIS n 
1 433 ASN n 
1 434 GLN n 
1 435 VAL n 
1 436 GLU n 
1 437 PHE n 
1 438 ASP n 
1 439 GLY n 
1 440 ILE n 
1 441 TRP n 
1 442 ILE n 
1 443 ASP n 
1 444 MET n 
1 445 ASN n 
1 446 GLU n 
1 447 VAL n 
1 448 SER n 
1 449 ASN n 
1 450 PHE n 
1 451 VAL n 
1 452 ASP n 
1 453 GLY n 
1 454 SER n 
1 455 VAL n 
1 456 SER n 
1 457 GLY n 
1 458 CYS n 
1 459 SER n 
1 460 THR n 
1 461 ASN n 
1 462 ASN n 
1 463 LEU n 
1 464 ASN n 
1 465 ASN n 
1 466 PRO n 
1 467 PRO n 
1 468 PHE n 
1 469 THR n 
1 470 PRO n 
1 471 ARG n 
1 472 ILE n 
1 473 LEU n 
1 474 ASP n 
1 475 GLY n 
1 476 TYR n 
1 477 LEU n 
1 478 PHE n 
1 479 CYS n 
1 480 LYS n 
1 481 THR n 
1 482 LEU n 
1 483 CYS n 
1 484 MET n 
1 485 ASP n 
1 486 ALA n 
1 487 VAL n 
1 488 GLN n 
1 489 HIS n 
1 490 TRP n 
1 491 GLY n 
1 492 LYS n 
1 493 GLN n 
1 494 TYR n 
1 495 ASP n 
1 496 ILE n 
1 497 HIS n 
1 498 ASN n 
1 499 LEU n 
1 500 TYR n 
1 501 GLY n 
1 502 TYR n 
1 503 SER n 
1 504 MET n 
1 505 ALA n 
1 506 VAL n 
1 507 ALA n 
1 508 THR n 
1 509 ALA n 
1 510 GLU n 
1 511 ALA n 
1 512 ALA n 
1 513 LYS n 
1 514 THR n 
1 515 VAL n 
1 516 PHE n 
1 517 PRO n 
1 518 ASN n 
1 519 LYS n 
1 520 ARG n 
1 521 SER n 
1 522 PHE n 
1 523 ILE n 
1 524 LEU n 
1 525 THR n 
1 526 ARG n 
1 527 SER n 
1 528 THR n 
1 529 PHE n 
1 530 ALA n 
1 531 GLY n 
1 532 SER n 
1 533 GLY n 
1 534 LYS n 
1 535 PHE n 
1 536 ALA n 
1 537 ALA n 
1 538 HIS n 
1 539 TRP n 
1 540 LEU n 
1 541 GLY n 
1 542 ASP n 
1 543 ASN n 
1 544 THR n 
1 545 ALA n 
1 546 THR n 
1 547 TRP n 
1 548 ASP n 
1 549 ASP n 
1 550 LEU n 
1 551 ARG n 
1 552 TRP n 
1 553 SER n 
1 554 ILE n 
1 555 PRO n 
1 556 GLY n 
1 557 VAL n 
1 558 LEU n 
1 559 GLU n 
1 560 PHE n 
1 561 ASN n 
1 562 LEU n 
1 563 PHE n 
1 564 GLY n 
1 565 ILE n 
1 566 PRO n 
1 567 MET n 
1 568 VAL n 
1 569 GLY n 
1 570 PRO n 
1 571 ASP n 
1 572 ILE n 
1 573 CYS n 
1 574 GLY n 
1 575 PHE n 
1 576 ALA n 
1 577 LEU n 
1 578 ASP n 
1 579 THR n 
1 580 PRO n 
1 581 GLU n 
1 582 GLU n 
1 583 LEU n 
1 584 CYS n 
1 585 ARG n 
1 586 ARG n 
1 587 TRP n 
1 588 MET n 
1 589 GLN n 
1 590 LEU n 
1 591 GLY n 
1 592 ALA n 
1 593 PHE n 
1 594 TYR n 
1 595 PRO n 
1 596 PHE n 
1 597 SER n 
1 598 ARG n 
1 599 ASN n 
1 600 HIS n 
1 601 ASN n 
1 602 GLY n 
1 603 GLN n 
1 604 GLY n 
1 605 TYR n 
1 606 LYS n 
1 607 ASP n 
1 608 GLN n 
1 609 ASP n 
1 610 PRO n 
1 611 ALA n 
1 612 SER n 
1 613 PHE n 
1 614 GLY n 
1 615 ALA n 
1 616 ASP n 
1 617 SER n 
1 618 LEU n 
1 619 LEU n 
1 620 LEU n 
1 621 ASN n 
1 622 SER n 
1 623 SER n 
1 624 ARG n 
1 625 HIS n 
1 626 TYR n 
1 627 LEU n 
1 628 ASN n 
1 629 ILE n 
1 630 ARG n 
1 631 TYR n 
1 632 THR n 
1 633 LEU n 
1 634 LEU n 
1 635 PRO n 
1 636 TYR n 
1 637 LEU n 
1 638 TYR n 
1 639 THR n 
1 640 LEU n 
1 641 PHE n 
1 642 PHE n 
1 643 ARG n 
1 644 ALA n 
1 645 HIS n 
1 646 SER n 
1 647 ARG n 
1 648 GLY n 
1 649 ASP n 
1 650 THR n 
1 651 VAL n 
1 652 ALA n 
1 653 ARG n 
1 654 PRO n 
1 655 LEU n 
1 656 LEU n 
1 657 HIS n 
1 658 GLU n 
1 659 PHE n 
1 660 TYR n 
1 661 GLU n 
1 662 ASP n 
1 663 ASN n 
1 664 SER n 
1 665 THR n 
1 666 TRP n 
1 667 ASP n 
1 668 VAL n 
1 669 HIS n 
1 670 GLN n 
1 671 GLN n 
1 672 PHE n 
1 673 LEU n 
1 674 TRP n 
1 675 GLY n 
1 676 PRO n 
1 677 GLY n 
1 678 LEU n 
1 679 LEU n 
1 680 ILE n 
1 681 THR n 
1 682 PRO n 
1 683 VAL n 
1 684 LEU n 
1 685 ASP n 
1 686 GLU n 
1 687 GLY n 
1 688 ALA n 
1 689 GLU n 
1 690 LYS n 
1 691 VAL n 
1 692 MET n 
1 693 ALA n 
1 694 TYR n 
1 695 VAL n 
1 696 PRO n 
1 697 ASP n 
1 698 ALA n 
1 699 VAL n 
1 700 TRP n 
1 701 TYR n 
1 702 ASP n 
1 703 TYR n 
1 704 GLU n 
1 705 THR n 
1 706 GLY n 
1 707 SER n 
1 708 GLN n 
1 709 VAL n 
1 710 ARG n 
1 711 TRP n 
1 712 ARG n 
1 713 LYS n 
1 714 GLN n 
1 715 LYS n 
1 716 VAL n 
1 717 GLU n 
1 718 MET n 
1 719 GLU n 
1 720 LEU n 
1 721 PRO n 
1 722 GLY n 
1 723 ASP n 
1 724 LYS n 
1 725 ILE n 
1 726 GLY n 
1 727 LEU n 
1 728 HIS n 
1 729 LEU n 
1 730 ARG n 
1 731 GLY n 
1 732 GLY n 
1 733 TYR n 
1 734 ILE n 
1 735 PHE n 
1 736 PRO n 
1 737 THR n 
1 738 GLN n 
1 739 GLN n 
1 740 PRO n 
1 741 ASN n 
1 742 THR n 
1 743 THR n 
1 744 THR n 
1 745 LEU n 
1 746 ALA n 
1 747 SER n 
1 748 ARG n 
1 749 LYS n 
1 750 ASN n 
1 751 PRO n 
1 752 LEU n 
1 753 GLY n 
1 754 LEU n 
1 755 ILE n 
1 756 ILE n 
1 757 ALA n 
1 758 LEU n 
1 759 ASP n 
1 760 GLU n 
1 761 ASN n 
1 762 LYS n 
1 763 GLU n 
1 764 ALA n 
1 765 LYS n 
1 766 GLY n 
1 767 GLU n 
1 768 LEU n 
1 769 PHE n 
1 770 TRP n 
1 771 ASP n 
1 772 ASP n 
1 773 GLY n 
1 774 GLU n 
1 775 THR n 
1 776 LYS n 
1 777 ASP n 
1 778 THR n 
1 779 VAL n 
1 780 ALA n 
1 781 ASN n 
1 782 LYS n 
1 783 VAL n 
1 784 TYR n 
1 785 LEU n 
1 786 LEU n 
1 787 CYS n 
1 788 GLU n 
1 789 PHE n 
1 790 SER n 
1 791 VAL n 
1 792 THR n 
1 793 GLN n 
1 794 ASN n 
1 795 ARG n 
1 796 LEU n 
1 797 GLU n 
1 798 VAL n 
1 799 ASN n 
1 800 ILE n 
1 801 SER n 
1 802 GLN n 
1 803 SER n 
1 804 THR n 
1 805 TYR n 
1 806 LYS n 
1 807 ASP n 
1 808 PRO n 
1 809 ASN n 
1 810 ASN n 
1 811 LEU n 
1 812 ALA n 
1 813 PHE n 
1 814 ASN n 
1 815 GLU n 
1 816 ILE n 
1 817 LYS n 
1 818 ILE n 
1 819 LEU n 
1 820 GLY n 
1 821 THR n 
1 822 GLU n 
1 823 GLU n 
1 824 PRO n 
1 825 SER n 
1 826 ASN n 
1 827 VAL n 
1 828 THR n 
1 829 VAL n 
1 830 LYS n 
1 831 HIS n 
1 832 ASN n 
1 833 GLY n 
1 834 VAL n 
1 835 PRO n 
1 836 SER n 
1 837 GLN n 
1 838 THR n 
1 839 SER n 
1 840 PRO n 
1 841 THR n 
1 842 VAL n 
1 843 THR n 
1 844 TYR n 
1 845 ASP n 
1 846 SER n 
1 847 ASN n 
1 848 LEU n 
1 849 LYS n 
1 850 VAL n 
1 851 ALA n 
1 852 ILE n 
1 853 ILE n 
1 854 THR n 
1 855 ASP n 
1 856 ILE n 
1 857 ASP n 
1 858 LEU n 
1 859 LEU n 
1 860 LEU n 
1 861 GLY n 
1 862 GLU n 
1 863 ALA n 
1 864 TYR n 
1 865 THR n 
1 866 VAL n 
1 867 GLU n 
1 868 TRP n 
1 869 ALA n 
1 870 HIS 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                 'MGAM, MGA, MGAML' 
_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     ? 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'S2 cells' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          'Stable Transfection Plasmid' 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMT-BiP-V5-His 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MGA_HUMAN 
_struct_ref.pdbx_db_accession          O43451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEW
;
_struct_ref.pdbx_align_begin           87 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3CTT 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 868 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O43451 
_struct_ref_seq.db_align_beg                  87 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  954 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       868 
# 
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 3CTT ALA A 869 ? UNP O43451 ? ? 'EXPRESSION TAG' 869 1 
1 3CTT HIS A 870 ? UNP O43451 ? ? 'EXPRESSION TAG' 870 2 
# 
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 
3CU non-polymer         . CASUARINE              '(1R,2R,3R,6S,7S,7aR)-3-(hydroxymethyl)hexahydro-1H-pyrrolizine-1,2,6,7-tetrol' 
'C8 H15 N O5'    205.208 
ALA 'L-peptide linking' y ALANINE                ?                                                                               
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ?                                                                               
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ?                                                                               
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ?                                                                               
'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ?                                                                               
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ?                                                                               
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ?                                                                               
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ?                                                                               
'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL               'GLYCERIN; PROPANE-1,2,3-TRIOL'                                                 
'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE              ?                                                                               
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ?                                                                               
'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ?                                                                               
'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ?                                                                               
'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ?                                                                               
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ?                                                                               
'C5 H11 N O2 S'  149.211 
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 
SO4 non-polymer         . 'SULFATE ION'          ?                                                                               
'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE              ?                                                                               
'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ?                                                                               
'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ?                                                                               
'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ?                                                                               
'C5 H11 N O2'    117.146 
# 
_exptl.crystals_number   1 
_exptl.entry_id          3CTT 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.63 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   53.15 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'20% PEG 3350, 0.2M sodium sulfate, 4% 1,1,1,3,3,3-hexafluoro-2-propanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2007-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9175 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE F1' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9175 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
# 
_reflns.entry_id                     3CTT 
_reflns.d_resolution_high            2.100 
_reflns.d_resolution_low             20.000 
_reflns.number_obs                   58131 
_reflns.pdbx_Rmerge_I_obs            0.118 
_reflns.pdbx_netI_over_sigmaI        11.900 
_reflns.pdbx_chi_squared             1.036 
_reflns.percent_possible_obs         95.600 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.3 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.10 
_reflns_shell.d_res_low              2.15 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.432 
_reflns_shell.meanI_over_sigI_obs    4.96 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       0.937 
_reflns_shell.pdbx_redundancy        5.5 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3891 
_reflns_shell.percent_possible_all   97.40 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3CTT 
_refine.ls_d_res_high                            2.100 
_refine.ls_d_res_low                             15.650 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    94.590 
_refine.ls_number_reflns_obs                     57768 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.ls_R_factor_obs                          0.228 
_refine.ls_R_factor_R_work                       0.225 
_refine.ls_R_factor_R_free                       0.278 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  2932 
_refine.B_iso_mean                               22.542 
_refine.aniso_B[1][1]                            0.060 
_refine.aniso_B[2][2]                            -0.020 
_refine.aniso_B[3][3]                            -0.030 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.901 
_refine.correlation_coeff_Fo_to_Fc_free          0.865 
_refine.pdbx_overall_ESU_R                       0.263 
_refine.pdbx_overall_ESU_R_Free                  0.222 
_refine.overall_SU_ML                            0.138 
_refine.overall_SU_B                             4.969 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 2QMJ' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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        6905 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         101 
_refine_hist.number_atoms_solvent             352 
_refine_hist.number_atoms_total               7358 
_refine_hist.d_res_high                       2.100 
_refine_hist.d_res_low                        15.650 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         7200 0.014  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      9810 1.527  1.946  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   860  6.843  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   363  35.313 24.325 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   1091 14.431 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   38   17.846 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           1047 0.106  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     5607 0.006  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            3530 0.213  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          4846 0.313  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    519  0.164  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   82   0.214  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 12   0.133  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              4411 0.866  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             6967 1.413  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              3228 2.224  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             2843 3.275  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               95.970 
_refine_ls_shell.number_reflns_R_work             4012 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.259 
_refine_ls_shell.R_factor_R_free                  0.359 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             207 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                4219 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3CTT 
_struct.title                     'Crystal complex of N-terminal Human Maltase-Glucoamylase with Casuarine' 
_struct.pdbx_descriptor           'Maltase-glucoamylase (E.C.3.2.1.20)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3CTT 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Glycosyl Hydrolase Family 31, alpha-glucosidase, Glycoprotein, Glycosidase, Membrane, Multifunctional enzyme, Signal-anchor, Sulfation, Transmembrane, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   Monomer 
# 
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  ASN A 8   ? ARG A 12  ? ASN A 8   ARG A 12  5 ? 5  
HELX_P HELX_P2  2  THR A 22  ? ARG A 29  ? THR A 22  ARG A 29  1 ? 8  
HELX_P HELX_P3  3  SER A 155 ? GLY A 157 ? SER A 155 GLY A 157 5 ? 3  
HELX_P HELX_P4  4  THR A 269 ? GLY A 282 ? THR A 269 GLY A 282 1 ? 14 
HELX_P HELX_P5  5  SER A 288 ? LEU A 292 ? SER A 288 LEU A 292 5 ? 5  
HELX_P HELX_P6  6  THR A 303 ? ALA A 317 ? THR A 303 ALA A 317 1 ? 15 
HELX_P HELX_P7  7  ASP A 327 ? MET A 331 ? ASP A 327 MET A 331 5 ? 5  
HELX_P HELX_P8  8  GLY A 346 ? ASN A 357 ? GLY A 346 ASN A 357 1 ? 12 
HELX_P HELX_P9  9  TYR A 379 ? LYS A 389 ? TYR A 379 LYS A 389 1 ? 11 
HELX_P HELX_P10 10 ASN A 417 ? ASN A 433 ? ASN A 417 ASN A 433 1 ? 17 
HELX_P HELX_P11 11 ILE A 472 ? TYR A 476 ? ILE A 472 TYR A 476 5 ? 5  
HELX_P HELX_P12 12 GLN A 493 ? HIS A 497 ? GLN A 493 HIS A 497 1 ? 5  
HELX_P HELX_P13 13 LEU A 499 ? PHE A 516 ? LEU A 499 PHE A 516 1 ? 18 
HELX_P HELX_P14 14 GLY A 531 ? PHE A 535 ? GLY A 531 PHE A 535 5 ? 5  
HELX_P HELX_P15 15 THR A 546 ? PHE A 563 ? THR A 546 PHE A 563 1 ? 18 
HELX_P HELX_P16 16 PRO A 580 ? ALA A 592 ? PRO A 580 ALA A 592 1 ? 13 
HELX_P HELX_P17 17 ASP A 609 ? GLY A 614 ? ASP A 609 GLY A 614 5 ? 6  
HELX_P HELX_P18 18 SER A 617 ? LEU A 633 ? SER A 617 LEU A 633 1 ? 17 
HELX_P HELX_P19 19 LEU A 633 ? ARG A 647 ? LEU A 633 ARG A 647 1 ? 15 
HELX_P HELX_P20 20 LEU A 655 ? TYR A 660 ? LEU A 655 TYR A 660 1 ? 6  
HELX_P HELX_P21 21 ASP A 662 ? TRP A 666 ? ASP A 662 TRP A 666 5 ? 5  
HELX_P HELX_P22 22 THR A 743 ? ARG A 748 ? THR A 743 ARG A 748 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 15  SG  ? ? ? 1_555 A CYS 31  SG ? ? A CYS 15  A CYS 31   1_555 ? ? ? ? ? ? ? 2.063 ? 
disulf2 disulf ? ? A CYS 573 SG  ? ? ? 1_555 A CYS 584 SG ? ? A CYS 573 A CYS 584  1_555 ? ? ? ? ? ? ? 2.062 ? 
covale1 covale ? ? A ASN 393 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 393 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale2 covale ? ? A ASN 741 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 741 A NAG 2001 1_555 ? ? ? ? ? ? ? 1.455 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 GLN 136 A . ? GLN 136 A PRO 137 A ? PRO 137 A 1 2.31   
2 GLY 181 A . ? GLY 181 A GLU 182 A ? GLU 182 A 1 -0.67  
3 ALA 248 A . ? ALA 248 A PRO 249 A ? PRO 249 A 1 -4.56  
4 GLU 446 A . ? GLU 446 A VAL 447 A ? VAL 447 A 1 1.79   
5 PRO 835 A . ? PRO 835 A SER 836 A ? SER 836 A 1 -10.14 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 8  ? 
C ? 3  ? 
D ? 5  ? 
E ? 9  ? 
F ? 3  ? 
G ? 2  ? 
H ? 5  ? 
I ? 2  ? 
J ? 10 ? 
K ? 9  ? 
# 
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 
A 1 2  ? anti-parallel 
B 1 2  ? anti-parallel 
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? anti-parallel 
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
D 1 2  ? anti-parallel 
D 2 3  ? anti-parallel 
D 3 4  ? anti-parallel 
D 4 5  ? anti-parallel 
E 1 2  ? parallel      
E 2 3  ? parallel      
E 3 4  ? parallel      
E 4 5  ? parallel      
E 5 6  ? parallel      
E 6 7  ? parallel      
E 7 8  ? parallel      
E 8 9  ? parallel      
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
G 1 2  ? anti-parallel 
H 1 2  ? anti-parallel 
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? anti-parallel 
I 1 2  ? anti-parallel 
J 1 2  ? anti-parallel 
J 2 3  ? anti-parallel 
J 3 4  ? anti-parallel 
J 4 5  ? anti-parallel 
J 5 6  ? parallel      
J 6 7  ? anti-parallel 
J 7 8  ? parallel      
J 8 9  ? anti-parallel 
J 9 10 ? anti-parallel 
K 1 2  ? anti-parallel 
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? anti-parallel 
K 5 6  ? parallel      
K 6 7  ? anti-parallel 
K 7 8  ? parallel      
K 8 9  ? 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 
A 1  CYS A 32  ? TRP A 33  ? CYS A 32  TRP A 33  
A 2  CYS A 44  ? TYR A 45  ? CYS A 44  TYR A 45  
B 1  TYR A 52  ? ASN A 60  ? TYR A 52  ASN A 60  
B 2  GLY A 64  ? ASN A 71  ? GLY A 64  ASN A 71  
B 3  ASN A 84  ? THR A 93  ? ASN A 84  THR A 93  
B 4  ARG A 96  ? ASP A 103 ? ARG A 96  ASP A 103 
B 5  LEU A 260 ? GLY A 267 ? LEU A 260 GLY A 267 
B 6  SER A 230 ? LEU A 235 ? SER A 230 LEU A 235 
B 7  GLN A 217 ? LEU A 223 ? GLN A 217 LEU A 223 
B 8  VAL A 177 ? GLY A 181 ? VAL A 177 GLY A 181 
C 1  TYR A 129 ? SER A 134 ? TYR A 129 SER A 134 
C 2  SER A 139 ? ARG A 144 ? SER A 139 ARG A 144 
C 3  VAL A 150 ? ASP A 153 ? VAL A 150 ASP A 153 
D 1  LEU A 160 ? ALA A 162 ? LEU A 160 ALA A 162 
D 2  PHE A 165 ? ARG A 171 ? PHE A 165 ARG A 171 
D 3  ALA A 250 ? THR A 255 ? ALA A 250 THR A 255 
D 4  MET A 241 ? GLN A 246 ? MET A 241 GLN A 246 
D 5  LYS A 195 ? ILE A 199 ? LYS A 195 ILE A 199 
E 1  VAL A 568 ? GLY A 569 ? VAL A 568 GLY A 569 
E 2  ALA A 537 ? TRP A 539 ? ALA A 537 TRP A 539 
E 3  ILE A 523 ? THR A 525 ? ILE A 523 THR A 525 
E 4  GLY A 439 ? ILE A 442 ? GLY A 439 ILE A 442 
E 5  LYS A 360 ? VAL A 365 ? LYS A 360 VAL A 365 
E 6  VAL A 323 ? ALA A 326 ? VAL A 323 ALA A 326 
E 7  PHE A 294 ? LEU A 296 ? PHE A 294 LEU A 296 
E 8  SER A 597 ? ASN A 599 ? SER A 597 ASN A 599 
E 9  ASP A 571 ? ILE A 572 ? ASP A 571 ILE A 572 
F 1  ILE A 369 ? SER A 370 ? ILE A 369 SER A 370 
F 2  GLY A 408 ? VAL A 411 ? GLY A 408 VAL A 411 
F 3  GLY A 403 ? VAL A 405 ? GLY A 403 VAL A 405 
G 1  VAL A 487 ? GLN A 488 ? VAL A 487 GLN A 488 
G 2  GLY A 491 ? LYS A 492 ? GLY A 491 LYS A 492 
H 1  ALA A 652 ? ARG A 653 ? ALA A 652 ARG A 653 
H 2  PHE A 672 ? TRP A 674 ? PHE A 672 TRP A 674 
H 3  LEU A 678 ? THR A 681 ? LEU A 678 THR A 681 
H 4  GLY A 726 ? ARG A 730 ? GLY A 726 ARG A 730 
H 5  TRP A 700 ? ASP A 702 ? TRP A 700 ASP A 702 
I 1  LYS A 690 ? VAL A 695 ? LYS A 690 VAL A 695 
I 2  GLN A 714 ? GLU A 719 ? GLN A 714 GLU A 719 
J 1  SER A 825 ? LYS A 830 ? SER A 825 LYS A 830 
J 2  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
J 3  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
J 4  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
J 5  GLU A 763 ? TRP A 770 ? GLU A 763 TRP A 770 
J 6  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
J 7  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
J 8  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
J 9  VAL A 850 ? THR A 854 ? VAL A 850 THR A 854 
J 10 THR A 841 ? ASP A 845 ? THR A 841 ASP A 845 
K 1  SER A 825 ? LYS A 830 ? SER A 825 LYS A 830 
K 2  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
K 3  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
K 4  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
K 5  GLU A 763 ? TRP A 770 ? GLU A 763 TRP A 770 
K 6  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
K 7  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
K 8  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
K 9  LEU A 858 ? LEU A 859 ? LEU A 858 LEU A 859 
# 
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 
A 1 2  N CYS A 32  ? N CYS A 32  O TYR A 45  ? O TYR A 45  
B 1 2  N GLU A 55  ? N GLU A 55  O ARG A 68  ? O ARG A 68  
B 2 3  N LEU A 69  ? N LEU A 69  O VAL A 85  ? O VAL A 85  
B 3 4  N GLU A 90  ? N GLU A 90  O HIS A 98  ? O HIS A 98  
B 4 5  N PHE A 99  ? N PHE A 99  O PHE A 262 ? O PHE A 262 
B 5 6  O PHE A 265 ? O PHE A 265 N GLY A 232 ? N GLY A 232 
B 6 7  O PHE A 231 ? O PHE A 231 N CYS A 222 ? N CYS A 222 
B 7 8  O PHE A 219 ? O PHE A 219 N LEU A 180 ? N LEU A 180 
C 1 2  N GLN A 130 ? N GLN A 130 O THR A 143 ? O THR A 143 
C 2 3  N VAL A 142 ? N VAL A 142 O PHE A 152 ? O PHE A 152 
D 1 2  N ALA A 162 ? N ALA A 162 O PHE A 165 ? O PHE A 165 
D 2 3  N LEU A 166 ? N LEU A 166 O THR A 255 ? O THR A 255 
D 3 4  O THR A 252 ? O THR A 252 N VAL A 244 ? N VAL A 244 
D 4 5  O LEU A 245 ? O LEU A 245 N LYS A 195 ? N LYS A 195 
E 1 2  O GLY A 569 ? O GLY A 569 N HIS A 538 ? N HIS A 538 
E 2 3  O ALA A 537 ? O ALA A 537 N THR A 525 ? N THR A 525 
E 3 4  O LEU A 524 ? O LEU A 524 N ILE A 442 ? N ILE A 442 
E 4 5  O TRP A 441 ? O TRP A 441 N ILE A 363 ? N ILE A 363 
E 5 6  O VAL A 362 ? O VAL A 362 N ALA A 326 ? N ALA A 326 
E 6 7  O HIS A 325 ? O HIS A 325 N LEU A 296 ? N LEU A 296 
E 7 8  N HIS A 295 ? N HIS A 295 O SER A 597 ? O SER A 597 
E 8 9  O ARG A 598 ? O ARG A 598 N ILE A 572 ? N ILE A 572 
F 1 2  N ILE A 369 ? N ILE A 369 O VAL A 411 ? O VAL A 411 
F 2 3  O THR A 410 ? O THR A 410 N GLY A 403 ? N GLY A 403 
G 1 2  N GLN A 488 ? N GLN A 488 O GLY A 491 ? O GLY A 491 
H 1 2  N ARG A 653 ? N ARG A 653 O LEU A 673 ? O LEU A 673 
H 2 3  N PHE A 672 ? N PHE A 672 O ILE A 680 ? O ILE A 680 
H 3 4  N LEU A 679 ? N LEU A 679 O HIS A 728 ? O HIS A 728 
H 4 5  O LEU A 729 ? O LEU A 729 N TYR A 701 ? N TYR A 701 
I 1 2  N VAL A 691 ? N VAL A 691 O MET A 718 ? O MET A 718 
J 1 2  N LYS A 830 ? N LYS A 830 O THR A 865 ? O THR A 865 
J 2 3  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
J 3 4  O ASN A 799 ? O ASN A 799 N GLU A 788 ? N GLU A 788 
J 4 5  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
J 5 6  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
J 6 7  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
J 7 8  N ILE A 756 ? N ILE A 756 O LEU A 819 ? O LEU A 819 
J 8 9  N ILE A 816 ? N ILE A 816 O ILE A 853 ? O ILE A 853 
J 9 10 O THR A 854 ? O THR A 854 N THR A 841 ? N THR A 841 
K 1 2  N LYS A 830 ? N LYS A 830 O THR A 865 ? O THR A 865 
K 2 3  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
K 3 4  O ASN A 799 ? O ASN A 799 N GLU A 788 ? N GLU A 788 
K 4 5  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
K 5 6  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
K 6 7  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
K 7 8  N ILE A 756 ? N ILE A 756 O LEU A 819 ? O LEU A 819 
K 8 9  N PHE A 813 ? N PHE A 813 O LEU A 858 ? O LEU A 858 
# 
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 ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG A 2001' 
AC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG A 2002' 
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 A 4001' 
AC4 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE 3CU A 1001' 
AC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3001' 
AC6 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE GOL A 3002' 
AC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE GOL A 3003' 
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3004' 
AC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3005' 
BC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3006' 
BC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3007' 
BC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3008' 
BC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3009' 
# 
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 9  SER A 146 ? SER A 146  . ? 2_454 ? 
2  AC1 9  ASN A 147 ? ASN A 147  . ? 2_454 ? 
3  AC1 9  ASN A 148 ? ASN A 148  . ? 2_454 ? 
4  AC1 9  ASN A 741 ? ASN A 741  . ? 1_555 ? 
5  AC1 9  ALA A 746 ? ALA A 746  . ? 1_555 ? 
6  AC1 9  ASN A 750 ? ASN A 750  . ? 1_555 ? 
7  AC1 9  HOH O .   ? HOH A 4101 . ? 1_555 ? 
8  AC1 9  HOH O .   ? HOH A 4221 . ? 2_454 ? 
9  AC1 9  HOH O .   ? HOH A 4282 . ? 1_555 ? 
10 AC2 7  LYS A 389 ? LYS A 389  . ? 1_555 ? 
11 AC2 7  ASN A 393 ? ASN A 393  . ? 1_555 ? 
12 AC2 7  GLY A 397 ? GLY A 397  . ? 1_555 ? 
13 AC2 7  GLN A 488 ? GLN A 488  . ? 1_555 ? 
14 AC2 7  HIS A 489 ? HIS A 489  . ? 1_555 ? 
15 AC2 7  HOH O .   ? HOH A 4184 . ? 1_555 ? 
16 AC2 7  HOH O .   ? HOH A 4273 . ? 1_555 ? 
17 AC3 5  SER A 126 ? SER A 126  . ? 2_454 ? 
18 AC3 5  ARG A 145 ? ARG A 145  . ? 2_454 ? 
19 AC3 5  HIS A 625 ? HIS A 625  . ? 1_555 ? 
20 AC3 5  ASN A 628 ? ASN A 628  . ? 1_555 ? 
21 AC3 5  HOH O .   ? HOH A 4069 . ? 1_555 ? 
22 AC4 11 TYR A 299 ? TYR A 299  . ? 1_555 ? 
23 AC4 11 ASP A 327 ? ASP A 327  . ? 1_555 ? 
24 AC4 11 ILE A 364 ? ILE A 364  . ? 1_555 ? 
25 AC4 11 TRP A 441 ? TRP A 441  . ? 1_555 ? 
26 AC4 11 ASP A 443 ? ASP A 443  . ? 1_555 ? 
27 AC4 11 ARG A 526 ? ARG A 526  . ? 1_555 ? 
28 AC4 11 TRP A 539 ? TRP A 539  . ? 1_555 ? 
29 AC4 11 ASP A 542 ? ASP A 542  . ? 1_555 ? 
30 AC4 11 PHE A 575 ? PHE A 575  . ? 1_555 ? 
31 AC4 11 HIS A 600 ? HIS A 600  . ? 1_555 ? 
32 AC4 11 HOH O .   ? HOH A 4353 . ? 1_555 ? 
33 AC5 4  ASP A 203 ? ASP A 203  . ? 1_555 ? 
34 AC5 4  ARG A 526 ? ARG A 526  . ? 1_555 ? 
35 AC5 4  ASP A 542 ? ASP A 542  . ? 1_555 ? 
36 AC5 4  HOH O .   ? HOH A 4265 . ? 1_555 ? 
37 AC6 8  ALA A 285 ? ALA A 285  . ? 1_555 ? 
38 AC6 8  PRO A 287 ? PRO A 287  . ? 1_555 ? 
39 AC6 8  PHE A 522 ? PHE A 522  . ? 1_555 ? 
40 AC6 8  ILE A 523 ? ILE A 523  . ? 1_555 ? 
41 AC6 8  PHE A 535 ? PHE A 535  . ? 1_555 ? 
42 AC6 8  ALA A 536 ? ALA A 536  . ? 1_555 ? 
43 AC6 8  ALA A 537 ? ALA A 537  . ? 1_555 ? 
44 AC6 8  HOH O .   ? HOH A 4117 . ? 1_555 ? 
45 AC7 6  ASN A 306 ? ASN A 306  . ? 1_555 ? 
46 AC7 6  GLU A 309 ? GLU A 309  . ? 1_555 ? 
47 AC7 6  ARG A 313 ? ARG A 313  . ? 1_555 ? 
48 AC7 6  ASP A 607 ? ASP A 607  . ? 1_555 ? 
49 AC7 6  HOH O .   ? HOH A 4056 . ? 1_555 ? 
50 AC7 6  HOH O .   ? HOH A 4237 . ? 1_555 ? 
51 AC8 5  LEU A 58  ? LEU A 58   . ? 1_555 ? 
52 AC8 5  GLU A 132 ? GLU A 132  . ? 1_555 ? 
53 AC8 5  ILE A 133 ? ILE A 133  . ? 1_555 ? 
54 AC8 5  THR A 843 ? THR A 843  . ? 2_455 ? 
55 AC8 5  THR A 854 ? THR A 854  . ? 2_455 ? 
56 AC9 4  ASP A 153 ? ASP A 153  . ? 1_555 ? 
57 AC9 4  ARG A 171 ? ARG A 171  . ? 1_555 ? 
58 AC9 4  HOH O .   ? HOH A 4169 . ? 1_555 ? 
59 AC9 4  HOH O .   ? HOH A 4313 . ? 1_555 ? 
60 BC1 5  ALA A 24  ? ALA A 24   . ? 3_555 ? 
61 BC1 5  GLU A 312 ? GLU A 312  . ? 1_555 ? 
62 BC1 5  GLU A 353 ? GLU A 353  . ? 1_555 ? 
63 BC1 5  HOH O .   ? HOH A 4145 . ? 1_555 ? 
64 BC1 5  HOH O .   ? HOH A 4232 . ? 3_555 ? 
65 BC2 4  ASP A 772 ? ASP A 772  . ? 1_555 ? 
66 BC2 4  THR A 775 ? THR A 775  . ? 1_555 ? 
67 BC2 4  THR A 778 ? THR A 778  . ? 1_555 ? 
68 BC2 4  HOH O .   ? HOH A 4010 . ? 1_555 ? 
69 BC3 4  ARG A 145 ? ARG A 145  . ? 2_454 ? 
70 BC3 4  GLN A 739 ? GLN A 739  . ? 1_555 ? 
71 BC3 4  PRO A 740 ? PRO A 740  . ? 1_555 ? 
72 BC3 4  HOH O .   ? HOH A 4275 . ? 2_454 ? 
73 BC4 5  GLN A 130 ? GLN A 130  . ? 1_555 ? 
74 BC4 5  GLU A 132 ? GLU A 132  . ? 1_555 ? 
75 BC4 5  ASN A 814 ? ASN A 814  . ? 2_455 ? 
76 BC4 5  THR A 854 ? THR A 854  . ? 2_455 ? 
77 BC4 5  ASP A 855 ? ASP A 855  . ? 2_455 ? 
# 
_atom_sites.entry_id                    3CTT 
_atom_sites.fract_transf_matrix[1][1]   0.011535 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009163 
_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]   0.009138 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . VAL A 1 7   ? -12.891 -36.819 63.371 1.00 36.61 ? 7    VAL A N   1 
ATOM   2    C CA  . VAL A 1 7   ? -12.698 -35.868 62.230 1.00 36.68 ? 7    VAL A CA  1 
ATOM   3    C C   . VAL A 1 7   ? -13.675 -36.252 61.113 1.00 35.83 ? 7    VAL A C   1 
ATOM   4    O O   . VAL A 1 7   ? -13.525 -37.299 60.477 1.00 36.66 ? 7    VAL A O   1 
ATOM   5    C CB  . VAL A 1 7   ? -11.212 -35.873 61.686 1.00 36.72 ? 7    VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 7   ? -10.977 -34.742 60.684 1.00 37.32 ? 7    VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 7   ? -10.220 -35.734 62.802 1.00 37.16 ? 7    VAL A CG2 1 
ATOM   8    N N   . ASN A 1 8   ? -14.696 -35.423 60.898 1.00 34.56 ? 8    ASN A N   1 
ATOM   9    C CA  . ASN A 1 8   ? -15.486 -35.489 59.671 1.00 32.30 ? 8    ASN A CA  1 
ATOM   10   C C   . ASN A 1 8   ? -14.488 -35.601 58.507 1.00 30.82 ? 8    ASN A C   1 
ATOM   11   O O   . ASN A 1 8   ? -13.516 -34.847 58.441 1.00 30.30 ? 8    ASN A O   1 
ATOM   12   C CB  . ASN A 1 8   ? -16.380 -34.241 59.596 1.00 32.83 ? 8    ASN A CB  1 
ATOM   13   C CG  . ASN A 1 8   ? -16.890 -33.908 58.174 1.00 33.99 ? 8    ASN A CG  1 
ATOM   14   O OD1 . ASN A 1 8   ? -16.883 -34.738 57.251 1.00 34.69 ? 8    ASN A OD1 1 
ATOM   15   N ND2 . ASN A 1 8   ? -17.362 -32.666 58.014 1.00 35.67 ? 8    ASN A ND2 1 
ATOM   16   N N   . GLU A 1 9   ? -14.694 -36.583 57.634 1.00 28.87 ? 9    GLU A N   1 
ATOM   17   C CA  . GLU A 1 9   ? -13.795 -36.814 56.498 1.00 28.08 ? 9    GLU A CA  1 
ATOM   18   C C   . GLU A 1 9   ? -13.613 -35.625 55.509 1.00 26.14 ? 9    GLU A C   1 
ATOM   19   O O   . GLU A 1 9   ? -12.575 -35.531 54.869 1.00 25.95 ? 9    GLU A O   1 
ATOM   20   C CB  . GLU A 1 9   ? -14.100 -38.148 55.795 1.00 28.43 ? 9    GLU A CB  1 
ATOM   21   C CG  . GLU A 1 9   ? -15.435 -38.290 55.116 1.00 29.72 ? 9    GLU A CG  1 
ATOM   22   C CD  . GLU A 1 9   ? -15.607 -39.671 54.468 1.00 31.14 ? 9    GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 9   ? -15.548 -40.711 55.176 1.00 34.68 ? 9    GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 9   ? -15.829 -39.723 53.234 1.00 34.79 ? 9    GLU A OE2 1 
ATOM   25   N N   . LEU A 1 10  ? -14.583 -34.705 55.432 1.00 23.42 ? 10   LEU A N   1 
ATOM   26   C CA  . LEU A 1 10  ? -14.463 -33.505 54.590 1.00 22.02 ? 10   LEU A CA  1 
ATOM   27   C C   . LEU A 1 10  ? -13.471 -32.519 55.168 1.00 20.83 ? 10   LEU A C   1 
ATOM   28   O O   . LEU A 1 10  ? -13.008 -31.641 54.461 1.00 20.40 ? 10   LEU A O   1 
ATOM   29   C CB  . LEU A 1 10  ? -15.825 -32.802 54.375 1.00 21.45 ? 10   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 10  ? -16.923 -33.697 53.804 1.00 23.24 ? 10   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 10  ? -18.254 -32.949 53.546 1.00 23.72 ? 10   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 10  ? -16.464 -34.433 52.559 1.00 23.45 ? 10   LEU A CD2 1 
ATOM   33   N N   . GLU A 1 11  ? -13.152 -32.681 56.453 1.00 20.13 ? 11   GLU A N   1 
ATOM   34   C CA  . GLU A 1 11  ? -12.265 -31.791 57.156 1.00 21.50 ? 11   GLU A CA  1 
ATOM   35   C C   . GLU A 1 11  ? -10.822 -32.315 57.244 1.00 19.96 ? 11   GLU A C   1 
ATOM   36   O O   . GLU A 1 11  ? -9.948  -31.624 57.773 1.00 19.54 ? 11   GLU A O   1 
ATOM   37   C CB  . GLU A 1 11  ? -12.803 -31.473 58.553 1.00 21.03 ? 11   GLU A CB  1 
ATOM   38   C CG  . GLU A 1 11  ? -14.091 -30.682 58.573 1.00 24.99 ? 11   GLU A CG  1 
ATOM   39   C CD  . GLU A 1 11  ? -14.625 -30.473 59.986 1.00 26.49 ? 11   GLU A CD  1 
ATOM   40   O OE1 . GLU A 1 11  ? -13.851 -30.606 60.966 1.00 32.48 ? 11   GLU A OE1 1 
ATOM   41   O OE2 . GLU A 1 11  ? -15.833 -30.168 60.116 1.00 33.21 ? 11   GLU A OE2 1 
ATOM   42   N N   . ARG A 1 12  ? -10.580 -33.511 56.702 1.00 19.04 ? 12   ARG A N   1 
ATOM   43   C CA  . ARG A 1 12  ? -9.232  -34.104 56.680 1.00 19.29 ? 12   ARG A CA  1 
ATOM   44   C C   . ARG A 1 12  ? -8.282  -33.308 55.802 1.00 18.02 ? 12   ARG A C   1 
ATOM   45   O O   . ARG A 1 12  ? -8.623  -32.959 54.687 1.00 18.44 ? 12   ARG A O   1 
ATOM   46   C CB  . ARG A 1 12  ? -9.290  -35.549 56.187 1.00 19.23 ? 12   ARG A CB  1 
ATOM   47   C CG  . ARG A 1 12  ? -9.869  -36.542 57.169 1.00 20.84 ? 12   ARG A CG  1 
ATOM   48   C CD  . ARG A 1 12  ? -9.905  -37.874 56.495 1.00 23.97 ? 12   ARG A CD  1 
ATOM   49   N NE  . ARG A 1 12  ? -10.792 -38.835 57.117 1.00 29.17 ? 12   ARG A NE  1 
ATOM   50   C CZ  . ARG A 1 12  ? -10.834 -40.123 56.769 1.00 30.15 ? 12   ARG A CZ  1 
ATOM   51   N NH1 . ARG A 1 12  ? -10.014 -40.618 55.811 1.00 25.49 ? 12   ARG A NH1 1 
ATOM   52   N NH2 . ARG A 1 12  ? -11.703 -40.906 57.378 1.00 30.43 ? 12   ARG A NH2 1 
ATOM   53   N N   . ILE A 1 13  ? -7.094  -33.031 56.314 1.00 17.44 ? 13   ILE A N   1 
ATOM   54   C CA  . ILE A 1 13  ? -6.079  -32.262 55.593 1.00 16.21 ? 13   ILE A CA  1 
ATOM   55   C C   . ILE A 1 13  ? -4.982  -33.261 55.195 1.00 16.70 ? 13   ILE A C   1 
ATOM   56   O O   . ILE A 1 13  ? -4.316  -33.832 56.058 1.00 15.89 ? 13   ILE A O   1 
ATOM   57   C CB  . ILE A 1 13  ? -5.530  -31.073 56.443 1.00 15.95 ? 13   ILE A CB  1 
ATOM   58   C CG1 . ILE A 1 13  ? -6.667  -30.117 56.872 1.00 15.59 ? 13   ILE A CG1 1 
ATOM   59   C CG2 . ILE A 1 13  ? -4.419  -30.294 55.704 1.00 16.02 ? 13   ILE A CG2 1 
ATOM   60   C CD1 . ILE A 1 13  ? -7.211  -29.249 55.729 1.00 16.08 ? 13   ILE A CD1 1 
ATOM   61   N N   . ASN A 1 14  ? -4.830  -33.459 53.886 1.00 16.16 ? 14   ASN A N   1 
ATOM   62   C CA  . ASN A 1 14  ? -4.000  -34.495 53.318 1.00 17.20 ? 14   ASN A CA  1 
ATOM   63   C C   . ASN A 1 14  ? -2.540  -34.273 53.736 1.00 17.27 ? 14   ASN A C   1 
ATOM   64   O O   . ASN A 1 14  ? -1.965  -33.211 53.486 1.00 15.94 ? 14   ASN A O   1 
ATOM   65   C CB  . ASN A 1 14  ? -4.120  -34.469 51.793 1.00 16.96 ? 14   ASN A CB  1 
ATOM   66   C CG  . ASN A 1 14  ? -3.278  -35.564 51.087 1.00 18.08 ? 14   ASN A CG  1 
ATOM   67   O OD1 . ASN A 1 14  ? -2.826  -36.519 51.705 1.00 16.15 ? 14   ASN A OD1 1 
ATOM   68   N ND2 . ASN A 1 14  ? -3.083  -35.406 49.774 1.00 17.89 ? 14   ASN A ND2 1 
ATOM   69   N N   . CYS A 1 15  ? -1.993  -35.303 54.367 1.00 18.95 ? 15   CYS A N   1 
ATOM   70   C CA  . CYS A 1 15  ? -0.613  -35.369 54.850 1.00 19.77 ? 15   CYS A CA  1 
ATOM   71   C C   . CYS A 1 15  ? 0.317   -36.015 53.829 1.00 20.49 ? 15   CYS A C   1 
ATOM   72   O O   . CYS A 1 15  ? 1.571   -36.008 54.006 1.00 20.06 ? 15   CYS A O   1 
ATOM   73   C CB  . CYS A 1 15  ? -0.590  -36.155 56.190 1.00 19.84 ? 15   CYS A CB  1 
ATOM   74   S SG  . CYS A 1 15  ? 1.071   -36.543 56.828 1.00 22.46 ? 15   CYS A SG  1 
ATOM   75   N N   . ILE A 1 16  ? -0.278  -36.597 52.776 1.00 19.95 ? 16   ILE A N   1 
ATOM   76   C CA  . ILE A 1 16  ? 0.512   -37.173 51.665 1.00 20.28 ? 16   ILE A CA  1 
ATOM   77   C C   . ILE A 1 16  ? 0.108   -36.577 50.289 1.00 21.64 ? 16   ILE A C   1 
ATOM   78   O O   . ILE A 1 16  ? -0.557  -37.258 49.485 1.00 21.65 ? 16   ILE A O   1 
ATOM   79   C CB  . ILE A 1 16  ? 0.465   -38.759 51.620 1.00 19.69 ? 16   ILE A CB  1 
ATOM   80   C CG1 . ILE A 1 16  ? 0.893   -39.381 52.955 1.00 19.42 ? 16   ILE A CG1 1 
ATOM   81   C CG2 . ILE A 1 16  ? 1.401   -39.278 50.555 1.00 19.66 ? 16   ILE A CG2 1 
ATOM   82   C CD1 . ILE A 1 16  ? 0.786   -40.910 53.036 1.00 18.34 ? 16   ILE A CD1 1 
ATOM   83   N N   . PRO A 1 17  ? 0.518   -35.323 50.006 1.00 22.81 ? 17   PRO A N   1 
ATOM   84   C CA  . PRO A 1 17  ? 0.187   -34.646 48.736 1.00 24.45 ? 17   PRO A CA  1 
ATOM   85   C C   . PRO A 1 17  ? 1.100   -35.028 47.578 1.00 25.70 ? 17   PRO A C   1 
ATOM   86   O O   . PRO A 1 17  ? 0.797   -34.710 46.423 1.00 26.49 ? 17   PRO A O   1 
ATOM   87   C CB  . PRO A 1 17  ? 0.435   -33.178 49.073 1.00 24.35 ? 17   PRO A CB  1 
ATOM   88   C CG  . PRO A 1 17  ? 1.512   -33.202 50.070 1.00 23.09 ? 17   PRO A CG  1 
ATOM   89   C CD  . PRO A 1 17  ? 1.310   -34.445 50.885 1.00 23.30 ? 17   PRO A CD  1 
ATOM   90   N N   . ASP A 1 18  ? 2.192   -35.719 47.915 1.00 26.00 ? 18   ASP A N   1 
ATOM   91   C CA  . ASP A 1 18  ? 3.351   -35.946 47.052 1.00 27.05 ? 18   ASP A CA  1 
ATOM   92   C C   . ASP A 1 18  ? 3.431   -37.337 46.427 1.00 27.19 ? 18   ASP A C   1 
ATOM   93   O O   . ASP A 1 18  ? 4.290   -37.585 45.578 1.00 27.38 ? 18   ASP A O   1 
ATOM   94   C CB  . ASP A 1 18  ? 4.644   -35.684 47.850 1.00 26.36 ? 18   ASP A CB  1 
ATOM   95   C CG  . ASP A 1 18  ? 4.671   -36.392 49.235 1.00 28.29 ? 18   ASP A CG  1 
ATOM   96   O OD1 . ASP A 1 18  ? 3.663   -36.395 49.995 1.00 27.64 ? 18   ASP A OD1 1 
ATOM   97   O OD2 . ASP A 1 18  ? 5.734   -36.945 49.589 1.00 29.15 ? 18   ASP A OD2 1 
ATOM   98   N N   . GLN A 1 19  ? 2.556   -38.248 46.845 1.00 27.38 ? 19   GLN A N   1 
ATOM   99   C CA  . GLN A 1 19  ? 2.632   -39.633 46.383 1.00 27.77 ? 19   GLN A CA  1 
ATOM   100  C C   . GLN A 1 19  ? 1.321   -40.394 46.603 1.00 27.46 ? 19   GLN A C   1 
ATOM   101  O O   . GLN A 1 19  ? 0.451   -39.900 47.311 1.00 27.26 ? 19   GLN A O   1 
ATOM   102  C CB  . GLN A 1 19  ? 3.829   -40.346 47.043 1.00 27.61 ? 19   GLN A CB  1 
ATOM   103  C CG  . GLN A 1 19  ? 3.709   -40.608 48.517 1.00 27.30 ? 19   GLN A CG  1 
ATOM   104  C CD  . GLN A 1 19  ? 5.042   -40.883 49.202 1.00 28.04 ? 19   GLN A CD  1 
ATOM   105  O OE1 . GLN A 1 19  ? 6.083   -40.390 48.779 1.00 31.42 ? 19   GLN A OE1 1 
ATOM   106  N NE2 . GLN A 1 19  ? 5.009   -41.664 50.277 1.00 24.21 ? 19   GLN A NE2 1 
ATOM   107  N N   . PRO A 1 20  ? 1.160   -41.585 45.966 1.00 27.33 ? 20   PRO A N   1 
ATOM   108  C CA  . PRO A 1 20  ? 0.048   -42.460 46.379 1.00 26.56 ? 20   PRO A CA  1 
ATOM   109  C C   . PRO A 1 20  ? 0.146   -42.816 47.880 1.00 25.24 ? 20   PRO A C   1 
ATOM   110  O O   . PRO A 1 20  ? 1.221   -43.179 48.342 1.00 24.33 ? 20   PRO A O   1 
ATOM   111  C CB  . PRO A 1 20  ? 0.211   -43.701 45.492 1.00 26.34 ? 20   PRO A CB  1 
ATOM   112  C CG  . PRO A 1 20  ? 1.630   -43.639 44.962 1.00 27.24 ? 20   PRO A CG  1 
ATOM   113  C CD  . PRO A 1 20  ? 1.936   -42.176 44.853 1.00 27.78 ? 20   PRO A CD  1 
ATOM   114  N N   . PRO A 1 21  ? -0.969  -42.659 48.634 1.00 24.26 ? 21   PRO A N   1 
ATOM   115  C CA  . PRO A 1 21  ? -0.984  -42.778 50.103 1.00 23.90 ? 21   PRO A CA  1 
ATOM   116  C C   . PRO A 1 21  ? -0.648  -44.186 50.610 1.00 23.45 ? 21   PRO A C   1 
ATOM   117  O O   . PRO A 1 21  ? -1.253  -45.160 50.157 1.00 24.15 ? 21   PRO A O   1 
ATOM   118  C CB  . PRO A 1 21  ? -2.429  -42.407 50.482 1.00 23.35 ? 21   PRO A CB  1 
ATOM   119  C CG  . PRO A 1 21  ? -3.226  -42.599 49.248 1.00 25.23 ? 21   PRO A CG  1 
ATOM   120  C CD  . PRO A 1 21  ? -2.291  -42.308 48.094 1.00 24.73 ? 21   PRO A CD  1 
ATOM   121  N N   . THR A 1 22  ? 0.314   -44.307 51.522 1.00 22.46 ? 22   THR A N   1 
ATOM   122  C CA  . THR A 1 22  ? 0.544   -45.604 52.171 1.00 21.26 ? 22   THR A CA  1 
ATOM   123  C C   . THR A 1 22  ? 0.554   -45.457 53.679 1.00 21.46 ? 22   THR A C   1 
ATOM   124  O O   . THR A 1 22  ? 0.887   -44.395 54.182 1.00 21.49 ? 22   THR A O   1 
ATOM   125  C CB  . THR A 1 22  ? 1.880   -46.259 51.740 1.00 20.69 ? 22   THR A CB  1 
ATOM   126  O OG1 . THR A 1 22  ? 2.959   -45.411 52.123 1.00 20.35 ? 22   THR A OG1 1 
ATOM   127  C CG2 . THR A 1 22  ? 1.916   -46.476 50.244 1.00 19.53 ? 22   THR A CG2 1 
ATOM   128  N N   . LYS A 1 23  ? 0.209   -46.527 54.391 1.00 21.55 ? 23   LYS A N   1 
ATOM   129  C CA  . LYS A 1 23  ? 0.296   -46.533 55.841 1.00 22.74 ? 23   LYS A CA  1 
ATOM   130  C C   . LYS A 1 23  ? 1.740   -46.348 56.343 1.00 22.78 ? 23   LYS A C   1 
ATOM   131  O O   . LYS A 1 23  ? 1.956   -45.637 57.302 1.00 22.91 ? 23   LYS A O   1 
ATOM   132  C CB  . LYS A 1 23  ? -0.351  -47.795 56.448 1.00 23.57 ? 23   LYS A CB  1 
ATOM   133  C CG  . LYS A 1 23  ? -0.552  -47.678 57.975 1.00 24.92 ? 23   LYS A CG  1 
ATOM   134  C CD  . LYS A 1 23  ? -1.061  -48.943 58.617 1.00 24.65 ? 23   LYS A CD  1 
ATOM   135  C CE  . LYS A 1 23  ? -1.400  -48.710 60.110 1.00 27.44 ? 23   LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 23  ? -0.219  -48.372 60.983 1.00 29.12 ? 23   LYS A NZ  1 
ATOM   137  N N   . ALA A 1 24  ? 2.728   -46.941 55.677 1.00 22.92 ? 24   ALA A N   1 
ATOM   138  C CA  . ALA A 1 24  ? 4.129   -46.752 56.072 1.00 23.23 ? 24   ALA A CA  1 
ATOM   139  C C   . ALA A 1 24  ? 4.597   -45.290 56.005 1.00 23.22 ? 24   ALA A C   1 
ATOM   140  O O   . ALA A 1 24  ? 5.236   -44.793 56.921 1.00 24.08 ? 24   ALA A O   1 
ATOM   141  C CB  . ALA A 1 24  ? 5.053   -47.670 55.236 1.00 23.68 ? 24   ALA A CB  1 
ATOM   142  N N   . THR A 1 25  ? 4.304   -44.596 54.916 1.00 22.91 ? 25   THR A N   1 
ATOM   143  C CA  . THR A 1 25  ? 4.611   -43.177 54.864 1.00 22.81 ? 25   THR A CA  1 
ATOM   144  C C   . THR A 1 25  ? 3.751   -42.418 55.892 1.00 22.54 ? 25   THR A C   1 
ATOM   145  O O   . THR A 1 25  ? 4.211   -41.502 56.551 1.00 21.02 ? 25   THR A O   1 
ATOM   146  C CB  . THR A 1 25  ? 4.361   -42.622 53.466 1.00 23.36 ? 25   THR A CB  1 
ATOM   147  O OG1 . THR A 1 25  ? 5.259   -43.240 52.537 1.00 22.86 ? 25   THR A OG1 1 
ATOM   148  C CG2 . THR A 1 25  ? 4.564   -41.134 53.441 1.00 22.93 ? 25   THR A CG2 1 
ATOM   149  N N   . CYS A 1 26  ? 2.489   -42.806 56.008 1.00 23.75 ? 26   CYS A N   1 
ATOM   150  C CA  . CYS A 1 26  ? 1.623   -42.188 56.985 1.00 24.18 ? 26   CYS A CA  1 
ATOM   151  C C   . CYS A 1 26  ? 2.213   -42.253 58.400 1.00 24.13 ? 26   CYS A C   1 
ATOM   152  O O   . CYS A 1 26  ? 2.270   -41.244 59.089 1.00 24.31 ? 26   CYS A O   1 
ATOM   153  C CB  . CYS A 1 26  ? 0.253   -42.845 56.969 1.00 24.23 ? 26   CYS A CB  1 
ATOM   154  S SG  . CYS A 1 26  ? -0.799  -42.132 58.268 1.00 27.94 ? 26   CYS A SG  1 
ATOM   155  N N   . ASP A 1 27  ? 2.646   -43.445 58.816 1.00 24.40 ? 27   ASP A N   1 
ATOM   156  C CA  . ASP A 1 27  ? 3.226   -43.669 60.145 1.00 24.83 ? 27   ASP A CA  1 
ATOM   157  C C   . ASP A 1 27  ? 4.558   -42.919 60.328 1.00 24.87 ? 27   ASP A C   1 
ATOM   158  O O   . ASP A 1 27  ? 4.797   -42.351 61.390 1.00 25.12 ? 27   ASP A O   1 
ATOM   159  C CB  . ASP A 1 27  ? 3.405   -45.165 60.408 1.00 24.99 ? 27   ASP A CB  1 
ATOM   160  C CG  . ASP A 1 27  ? 2.075   -45.905 60.562 1.00 27.60 ? 27   ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 27  ? 0.999   -45.270 60.659 1.00 30.45 ? 27   ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 27  ? 2.106   -47.146 60.591 1.00 31.52 ? 27   ASP A OD2 1 
ATOM   163  N N   . GLN A 1 28  ? 5.391   -42.879 59.291 1.00 24.26 ? 28   GLN A N   1 
ATOM   164  C CA  . GLN A 1 28  ? 6.683   -42.161 59.367 1.00 25.15 ? 28   GLN A CA  1 
ATOM   165  C C   . GLN A 1 28  ? 6.491   -40.657 59.597 1.00 24.87 ? 28   GLN A C   1 
ATOM   166  O O   . GLN A 1 28  ? 7.285   -40.011 60.299 1.00 24.48 ? 28   GLN A O   1 
ATOM   167  C CB  . GLN A 1 28  ? 7.551   -42.440 58.119 1.00 25.24 ? 28   GLN A CB  1 
ATOM   168  C CG  . GLN A 1 28  ? 8.829   -41.592 58.002 1.00 27.51 ? 28   GLN A CG  1 
ATOM   169  C CD  . GLN A 1 28  ? 9.755   -41.718 59.224 1.00 31.60 ? 28   GLN A CD  1 
ATOM   170  O OE1 . GLN A 1 28  ? 10.252  -40.717 59.748 1.00 35.42 ? 28   GLN A OE1 1 
ATOM   171  N NE2 . GLN A 1 28  ? 9.973   -42.941 59.682 1.00 32.35 ? 28   GLN A NE2 1 
ATOM   172  N N   . ARG A 1 29  ? 5.417   -40.113 59.027 1.00 24.73 ? 29   ARG A N   1 
ATOM   173  C CA  . ARG A 1 29  ? 5.110   -38.692 59.160 1.00 24.56 ? 29   ARG A CA  1 
ATOM   174  C C   . ARG A 1 29  ? 4.292   -38.339 60.391 1.00 24.04 ? 29   ARG A C   1 
ATOM   175  O O   . ARG A 1 29  ? 4.045   -37.171 60.635 1.00 23.85 ? 29   ARG A O   1 
ATOM   176  C CB  . ARG A 1 29  ? 4.399   -38.178 57.896 1.00 25.37 ? 29   ARG A CB  1 
ATOM   177  C CG  . ARG A 1 29  ? 5.285   -38.280 56.667 1.00 25.02 ? 29   ARG A CG  1 
ATOM   178  C CD  . ARG A 1 29  ? 4.608   -37.760 55.420 1.00 26.53 ? 29   ARG A CD  1 
ATOM   179  N NE  . ARG A 1 29  ? 5.475   -38.036 54.276 1.00 23.51 ? 29   ARG A NE  1 
ATOM   180  C CZ  . ARG A 1 29  ? 5.179   -37.755 53.021 1.00 23.23 ? 29   ARG A CZ  1 
ATOM   181  N NH1 . ARG A 1 29  ? 4.028   -37.160 52.711 1.00 18.81 ? 29   ARG A NH1 1 
ATOM   182  N NH2 . ARG A 1 29  ? 6.042   -38.074 52.078 1.00 22.10 ? 29   ARG A NH2 1 
ATOM   183  N N   . GLY A 1 30  ? 3.872   -39.341 61.158 1.00 23.70 ? 30   GLY A N   1 
ATOM   184  C CA  . GLY A 1 30  ? 3.090   -39.113 62.360 1.00 23.12 ? 30   GLY A CA  1 
ATOM   185  C C   . GLY A 1 30  ? 1.665   -38.653 62.054 1.00 23.60 ? 30   GLY A C   1 
ATOM   186  O O   . GLY A 1 30  ? 1.101   -37.859 62.790 1.00 23.71 ? 30   GLY A O   1 
ATOM   187  N N   . CYS A 1 31  ? 1.075   -39.158 60.979 1.00 23.07 ? 31   CYS A N   1 
ATOM   188  C CA  . CYS A 1 31  ? -0.263  -38.688 60.560 1.00 23.35 ? 31   CYS A CA  1 
ATOM   189  C C   . CYS A 1 31  ? -1.327  -39.748 60.826 1.00 23.04 ? 31   CYS A C   1 
ATOM   190  O O   . CYS A 1 31  ? -1.025  -40.764 61.424 1.00 23.26 ? 31   CYS A O   1 
ATOM   191  C CB  . CYS A 1 31  ? -0.219  -38.229 59.098 1.00 23.12 ? 31   CYS A CB  1 
ATOM   192  S SG  . CYS A 1 31  ? 0.791   -36.694 58.866 1.00 24.45 ? 31   CYS A SG  1 
ATOM   193  N N   . CYS A 1 32  ? -2.568  -39.514 60.407 1.00 23.78 ? 32   CYS A N   1 
ATOM   194  C CA  . CYS A 1 32  ? -3.675  -40.426 60.718 1.00 24.04 ? 32   CYS A CA  1 
ATOM   195  C C   . CYS A 1 32  ? -4.053  -41.240 59.496 1.00 23.83 ? 32   CYS A C   1 
ATOM   196  O O   . CYS A 1 32  ? -4.068  -40.718 58.387 1.00 23.36 ? 32   CYS A O   1 
ATOM   197  C CB  . CYS A 1 32  ? -4.898  -39.644 61.170 1.00 24.46 ? 32   CYS A CB  1 
ATOM   198  S SG  . CYS A 1 32  ? -4.639  -38.638 62.607 1.00 26.55 ? 32   CYS A SG  1 
ATOM   199  N N   . TRP A 1 33  ? -4.378  -42.510 59.699 1.00 23.57 ? 33   TRP A N   1 
ATOM   200  C CA  . TRP A 1 33  ? -4.659  -43.412 58.595 1.00 24.49 ? 33   TRP A CA  1 
ATOM   201  C C   . TRP A 1 33  ? -6.099  -43.920 58.680 1.00 25.37 ? 33   TRP A C   1 
ATOM   202  O O   . TRP A 1 33  ? -6.514  -44.447 59.707 1.00 24.55 ? 33   TRP A O   1 
ATOM   203  C CB  . TRP A 1 33  ? -3.674  -44.582 58.618 1.00 23.77 ? 33   TRP A CB  1 
ATOM   204  C CG  . TRP A 1 33  ? -3.831  -45.546 57.498 1.00 23.79 ? 33   TRP A CG  1 
ATOM   205  C CD1 . TRP A 1 33  ? -4.360  -46.811 57.561 1.00 23.63 ? 33   TRP A CD1 1 
ATOM   206  C CD2 . TRP A 1 33  ? -3.464  -45.331 56.124 1.00 23.85 ? 33   TRP A CD2 1 
ATOM   207  N NE1 . TRP A 1 33  ? -4.335  -47.393 56.313 1.00 23.16 ? 33   TRP A NE1 1 
ATOM   208  C CE2 . TRP A 1 33  ? -3.790  -46.508 55.416 1.00 23.12 ? 33   TRP A CE2 1 
ATOM   209  C CE3 . TRP A 1 33  ? -2.870  -44.261 55.429 1.00 22.19 ? 33   TRP A CE3 1 
ATOM   210  C CZ2 . TRP A 1 33  ? -3.549  -46.647 54.050 1.00 23.08 ? 33   TRP A CZ2 1 
ATOM   211  C CZ3 . TRP A 1 33  ? -2.628  -44.407 54.078 1.00 23.38 ? 33   TRP A CZ3 1 
ATOM   212  C CH2 . TRP A 1 33  ? -2.974  -45.593 53.403 1.00 22.98 ? 33   TRP A CH2 1 
ATOM   213  N N   . ASN A 1 34  ? -6.853  -43.715 57.606 1.00 26.90 ? 34   ASN A N   1 
ATOM   214  C CA  . ASN A 1 34  ? -8.230  -44.198 57.492 1.00 28.70 ? 34   ASN A CA  1 
ATOM   215  C C   . ASN A 1 34  ? -8.589  -44.292 56.017 1.00 30.37 ? 34   ASN A C   1 
ATOM   216  O O   . ASN A 1 34  ? -9.056  -43.317 55.427 1.00 30.26 ? 34   ASN A O   1 
ATOM   217  C CB  . ASN A 1 34  ? -9.202  -43.291 58.258 1.00 28.34 ? 34   ASN A CB  1 
ATOM   218  C CG  . ASN A 1 34  ? -10.665 -43.800 58.225 1.00 30.37 ? 34   ASN A CG  1 
ATOM   219  O OD1 . ASN A 1 34  ? -11.023 -44.676 57.444 1.00 32.50 ? 34   ASN A OD1 1 
ATOM   220  N ND2 . ASN A 1 34  ? -11.497 -43.245 59.088 1.00 27.86 ? 34   ASN A ND2 1 
ATOM   221  N N   . PRO A 1 35  ? -8.322  -45.456 55.390 1.00 32.44 ? 35   PRO A N   1 
ATOM   222  C CA  . PRO A 1 35  ? -8.652  -45.602 53.974 1.00 34.04 ? 35   PRO A CA  1 
ATOM   223  C C   . PRO A 1 35  ? -10.141 -45.716 53.644 1.00 35.97 ? 35   PRO A C   1 
ATOM   224  O O   . PRO A 1 35  ? -10.461 -45.991 52.495 1.00 37.81 ? 35   PRO A O   1 
ATOM   225  C CB  . PRO A 1 35  ? -7.931  -46.900 53.563 1.00 33.66 ? 35   PRO A CB  1 
ATOM   226  C CG  . PRO A 1 35  ? -7.034  -47.243 54.696 1.00 33.07 ? 35   PRO A CG  1 
ATOM   227  C CD  . PRO A 1 35  ? -7.647  -46.655 55.912 1.00 32.69 ? 35   PRO A CD  1 
ATOM   228  N N   . GLN A 1 36  ? -11.041 -45.507 54.596 1.00 37.92 ? 36   GLN A N   1 
ATOM   229  C CA  . GLN A 1 36  ? -12.477 -45.751 54.331 1.00 40.55 ? 36   GLN A CA  1 
ATOM   230  C C   . GLN A 1 36  ? -13.376 -44.511 54.042 1.00 41.09 ? 36   GLN A C   1 
ATOM   231  O O   . GLN A 1 36  ? -14.599 -44.552 54.264 1.00 42.07 ? 36   GLN A O   1 
ATOM   232  C CB  . GLN A 1 36  ? -13.091 -46.644 55.429 1.00 41.18 ? 36   GLN A CB  1 
ATOM   233  C CG  . GLN A 1 36  ? -12.305 -47.941 55.752 1.00 43.67 ? 36   GLN A CG  1 
ATOM   234  C CD  . GLN A 1 36  ? -12.400 -49.029 54.672 1.00 47.33 ? 36   GLN A CD  1 
ATOM   235  O OE1 . GLN A 1 36  ? -13.037 -48.851 53.628 1.00 47.90 ? 36   GLN A OE1 1 
ATOM   236  N NE2 . GLN A 1 36  ? -11.750 -50.167 54.927 1.00 49.05 ? 36   GLN A NE2 1 
ATOM   237  N N   . GLY A 1 37  ? -12.791 -43.425 53.539 1.00 40.98 ? 37   GLY A N   1 
ATOM   238  C CA  . GLY A 1 37  ? -13.599 -42.298 53.042 1.00 40.77 ? 37   GLY A CA  1 
ATOM   239  C C   . GLY A 1 37  ? -14.048 -42.504 51.597 1.00 40.63 ? 37   GLY A C   1 
ATOM   240  O O   . GLY A 1 37  ? -13.735 -43.543 50.984 1.00 41.53 ? 37   GLY A O   1 
ATOM   241  N N   . ALA A 1 38  ? -14.777 -41.526 51.041 1.00 39.60 ? 38   ALA A N   1 
ATOM   242  C CA  . ALA A 1 38  ? -15.182 -41.545 49.619 1.00 38.26 ? 38   ALA A CA  1 
ATOM   243  C C   . ALA A 1 38  ? -14.022 -41.139 48.694 1.00 37.35 ? 38   ALA A C   1 
ATOM   244  O O   . ALA A 1 38  ? -12.908 -40.896 49.163 1.00 37.13 ? 38   ALA A O   1 
ATOM   245  C CB  . ALA A 1 38  ? -16.363 -40.621 49.405 1.00 38.34 ? 38   ALA A CB  1 
ATOM   246  N N   . VAL A 1 39  ? -14.287 -41.057 47.389 1.00 35.63 ? 39   VAL A N   1 
ATOM   247  C CA  . VAL A 1 39  ? -13.265 -40.644 46.408 1.00 33.91 ? 39   VAL A CA  1 
ATOM   248  C C   . VAL A 1 39  ? -12.615 -39.295 46.748 1.00 32.68 ? 39   VAL A C   1 
ATOM   249  O O   . VAL A 1 39  ? -13.308 -38.322 47.064 1.00 32.05 ? 39   VAL A O   1 
ATOM   250  C CB  . VAL A 1 39  ? -13.793 -40.659 44.932 1.00 33.97 ? 39   VAL A CB  1 
ATOM   251  C CG1 . VAL A 1 39  ? -14.850 -39.593 44.682 1.00 33.95 ? 39   VAL A CG1 1 
ATOM   252  C CG2 . VAL A 1 39  ? -12.641 -40.521 43.946 1.00 34.13 ? 39   VAL A CG2 1 
ATOM   253  N N   . SER A 1 40  ? -11.281 -39.280 46.715 1.00 30.84 ? 40   SER A N   1 
ATOM   254  C CA  . SER A 1 40  ? -10.466 -38.069 46.950 1.00 29.57 ? 40   SER A CA  1 
ATOM   255  C C   . SER A 1 40  ? -10.334 -37.714 48.432 1.00 27.45 ? 40   SER A C   1 
ATOM   256  O O   . SER A 1 40  ? -9.483  -36.918 48.784 1.00 26.99 ? 40   SER A O   1 
ATOM   257  C CB  . SER A 1 40  ? -10.972 -36.851 46.151 1.00 29.35 ? 40   SER A CB  1 
ATOM   258  O OG  . SER A 1 40  ? -11.072 -37.108 44.757 1.00 30.70 ? 40   SER A OG  1 
ATOM   259  N N   . VAL A 1 41  ? -11.158 -38.303 49.295 1.00 25.77 ? 41   VAL A N   1 
ATOM   260  C CA  . VAL A 1 41  ? -10.968 -38.141 50.749 1.00 25.10 ? 41   VAL A CA  1 
ATOM   261  C C   . VAL A 1 41  ? -9.573  -38.706 51.116 1.00 24.16 ? 41   VAL A C   1 
ATOM   262  O O   . VAL A 1 41  ? -9.277  -39.850 50.790 1.00 24.33 ? 41   VAL A O   1 
ATOM   263  C CB  . VAL A 1 41  ? -12.089 -38.816 51.567 1.00 24.90 ? 41   VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 41  ? -11.767 -38.788 53.071 1.00 24.98 ? 41   VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 41  ? -13.396 -38.126 51.331 1.00 24.99 ? 41   VAL A CG2 1 
ATOM   266  N N   . PRO A 1 42  ? -8.700  -37.895 51.750 1.00 23.58 ? 42   PRO A N   1 
ATOM   267  C CA  . PRO A 1 42  ? -7.328  -38.363 51.976 1.00 22.93 ? 42   PRO A CA  1 
ATOM   268  C C   . PRO A 1 42  ? -7.277  -39.545 52.928 1.00 22.80 ? 42   PRO A C   1 
ATOM   269  O O   . PRO A 1 42  ? -7.868  -39.508 54.009 1.00 22.90 ? 42   PRO A O   1 
ATOM   270  C CB  . PRO A 1 42  ? -6.645  -37.160 52.642 1.00 23.47 ? 42   PRO A CB  1 
ATOM   271  C CG  . PRO A 1 42  ? -7.535  -36.040 52.466 1.00 22.27 ? 42   PRO A CG  1 
ATOM   272  C CD  . PRO A 1 42  ? -8.903  -36.543 52.286 1.00 22.93 ? 42   PRO A CD  1 
ATOM   273  N N   . TRP A 1 43  ? -6.554  -40.587 52.534 1.00 22.55 ? 43   TRP A N   1 
ATOM   274  C CA  . TRP A 1 43  ? -6.400  -41.761 53.372 1.00 21.99 ? 43   TRP A CA  1 
ATOM   275  C C   . TRP A 1 43  ? -5.486  -41.410 54.542 1.00 21.56 ? 43   TRP A C   1 
ATOM   276  O O   . TRP A 1 43  ? -5.591  -41.969 55.617 1.00 21.25 ? 43   TRP A O   1 
ATOM   277  C CB  . TRP A 1 43  ? -5.797  -42.894 52.536 1.00 23.20 ? 43   TRP A CB  1 
ATOM   278  C CG  . TRP A 1 43  ? -6.771  -43.534 51.625 1.00 23.37 ? 43   TRP A CG  1 
ATOM   279  C CD1 . TRP A 1 43  ? -8.051  -43.126 51.381 1.00 24.49 ? 43   TRP A CD1 1 
ATOM   280  C CD2 . TRP A 1 43  ? -6.559  -44.696 50.812 1.00 25.42 ? 43   TRP A CD2 1 
ATOM   281  N NE1 . TRP A 1 43  ? -8.647  -43.957 50.482 1.00 25.09 ? 43   TRP A NE1 1 
ATOM   282  C CE2 . TRP A 1 43  ? -7.761  -44.932 50.109 1.00 24.00 ? 43   TRP A CE2 1 
ATOM   283  C CE3 . TRP A 1 43  ? -5.473  -45.563 50.614 1.00 24.96 ? 43   TRP A CE3 1 
ATOM   284  C CZ2 . TRP A 1 43  ? -7.919  -45.997 49.219 1.00 24.32 ? 43   TRP A CZ2 1 
ATOM   285  C CZ3 . TRP A 1 43  ? -5.619  -46.622 49.719 1.00 25.53 ? 43   TRP A CZ3 1 
ATOM   286  C CH2 . TRP A 1 43  ? -6.853  -46.837 49.044 1.00 25.87 ? 43   TRP A CH2 1 
ATOM   287  N N   . CYS A 1 44  ? -4.580  -40.477 54.301 1.00 21.19 ? 44   CYS A N   1 
ATOM   288  C CA  . CYS A 1 44  ? -3.610  -40.055 55.298 1.00 20.84 ? 44   CYS A CA  1 
ATOM   289  C C   . CYS A 1 44  ? -3.747  -38.543 55.548 1.00 20.45 ? 44   CYS A C   1 
ATOM   290  O O   . CYS A 1 44  ? -3.594  -37.732 54.638 1.00 19.92 ? 44   CYS A O   1 
ATOM   291  C CB  . CYS A 1 44  ? -2.209  -40.424 54.849 1.00 20.23 ? 44   CYS A CB  1 
ATOM   292  S SG  . CYS A 1 44  ? -0.974  -39.813 55.983 1.00 22.68 ? 44   CYS A SG  1 
ATOM   293  N N   . TYR A 1 45  ? -4.063  -38.178 56.781 1.00 20.71 ? 45   TYR A N   1 
ATOM   294  C CA  . TYR A 1 45  ? -4.366  -36.791 57.121 1.00 20.80 ? 45   TYR A CA  1 
ATOM   295  C C   . TYR A 1 45  ? -3.672  -36.377 58.404 1.00 20.63 ? 45   TYR A C   1 
ATOM   296  O O   . TYR A 1 45  ? -3.238  -37.223 59.176 1.00 19.96 ? 45   TYR A O   1 
ATOM   297  C CB  . TYR A 1 45  ? -5.899  -36.543 57.175 1.00 20.78 ? 45   TYR A CB  1 
ATOM   298  C CG  . TYR A 1 45  ? -6.640  -37.441 58.133 1.00 21.89 ? 45   TYR A CG  1 
ATOM   299  C CD1 . TYR A 1 45  ? -7.020  -36.984 59.396 1.00 20.27 ? 45   TYR A CD1 1 
ATOM   300  C CD2 . TYR A 1 45  ? -6.976  -38.754 57.776 1.00 20.94 ? 45   TYR A CD2 1 
ATOM   301  C CE1 . TYR A 1 45  ? -7.703  -37.814 60.279 1.00 21.46 ? 45   TYR A CE1 1 
ATOM   302  C CE2 . TYR A 1 45  ? -7.633  -39.594 58.663 1.00 20.51 ? 45   TYR A CE2 1 
ATOM   303  C CZ  . TYR A 1 45  ? -7.993  -39.124 59.904 1.00 21.78 ? 45   TYR A CZ  1 
ATOM   304  O OH  . TYR A 1 45  ? -8.665  -39.960 60.769 1.00 25.05 ? 45   TYR A OH  1 
ATOM   305  N N   . TYR A 1 46  ? -3.518  -35.078 58.620 1.00 21.15 ? 46   TYR A N   1 
ATOM   306  C CA  . TYR A 1 46  ? -2.767  -34.626 59.780 1.00 23.36 ? 46   TYR A CA  1 
ATOM   307  C C   . TYR A 1 46  ? -3.535  -34.879 61.054 1.00 25.11 ? 46   TYR A C   1 
ATOM   308  O O   . TYR A 1 46  ? -4.769  -34.809 61.065 1.00 24.28 ? 46   TYR A O   1 
ATOM   309  C CB  . TYR A 1 46  ? -2.386  -33.146 59.690 1.00 22.51 ? 46   TYR A CB  1 
ATOM   310  C CG  . TYR A 1 46  ? -1.374  -32.869 58.619 1.00 21.00 ? 46   TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 46  ? -0.006  -33.149 58.827 1.00 18.25 ? 46   TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 46  ? -1.765  -32.325 57.396 1.00 17.52 ? 46   TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 46  ? 0.926   -32.894 57.826 1.00 19.33 ? 46   TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 46  ? -0.833  -32.058 56.396 1.00 17.30 ? 46   TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 46  ? 0.513   -32.356 56.621 1.00 20.96 ? 46   TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 46  ? 1.453   -32.119 55.634 1.00 23.14 ? 46   TYR A OH  1 
ATOM   317  N N   . SER A 1 47  ? -2.780  -35.205 62.105 1.00 27.92 ? 47   SER A N   1 
ATOM   318  C CA  . SER A 1 47  ? -3.307  -35.381 63.469 1.00 30.96 ? 47   SER A CA  1 
ATOM   319  C C   . SER A 1 47  ? -3.599  -34.029 64.102 1.00 33.66 ? 47   SER A C   1 
ATOM   320  O O   . SER A 1 47  ? -3.084  -33.008 63.636 1.00 33.88 ? 47   SER A O   1 
ATOM   321  C CB  . SER A 1 47  ? -2.309  -36.148 64.325 1.00 30.31 ? 47   SER A CB  1 
ATOM   322  O OG  . SER A 1 47  ? -1.086  -35.440 64.407 1.00 30.15 ? 47   SER A OG  1 
ATOM   323  N N   . LYS A 1 48  ? -4.397  -34.044 65.178 1.00 37.22 ? 48   LYS A N   1 
ATOM   324  C CA  . LYS A 1 48  ? -5.014  -32.839 65.777 1.00 40.67 ? 48   LYS A CA  1 
ATOM   325  C C   . LYS A 1 48  ? -4.052  -31.946 66.552 1.00 41.80 ? 48   LYS A C   1 
ATOM   326  O O   . LYS A 1 48  ? -4.398  -30.818 66.938 1.00 42.69 ? 48   LYS A O   1 
ATOM   327  C CB  . LYS A 1 48  ? -6.224  -33.207 66.658 1.00 40.56 ? 48   LYS A CB  1 
ATOM   328  C CG  . LYS A 1 48  ? -7.539  -33.351 65.884 1.00 42.06 ? 48   LYS A CG  1 
ATOM   329  C CD  . LYS A 1 48  ? -8.672  -33.903 66.768 1.00 42.77 ? 48   LYS A CD  1 
ATOM   330  C CE  . LYS A 1 48  ? -9.682  -32.825 67.206 1.00 45.70 ? 48   LYS A CE  1 
ATOM   331  N NZ  . LYS A 1 48  ? -10.992 -32.852 66.439 1.00 46.28 ? 48   LYS A NZ  1 
ATOM   332  N N   . ASN A 1 49  ? -2.845  -32.450 66.759 1.00 43.15 ? 49   ASN A N   1 
ATOM   333  C CA  . ASN A 1 49  ? -1.828  -31.736 67.486 1.00 44.45 ? 49   ASN A CA  1 
ATOM   334  C C   . ASN A 1 49  ? -0.510  -32.236 66.919 1.00 44.84 ? 49   ASN A C   1 
ATOM   335  O O   . ASN A 1 49  ? -0.229  -33.433 66.912 1.00 45.58 ? 49   ASN A O   1 
ATOM   336  C CB  . ASN A 1 49  ? -1.966  -32.003 68.996 1.00 45.16 ? 49   ASN A CB  1 
ATOM   337  C CG  . ASN A 1 49  ? -1.720  -30.754 69.852 1.00 46.50 ? 49   ASN A CG  1 
ATOM   338  O OD1 . ASN A 1 49  ? -0.672  -30.102 69.747 1.00 48.81 ? 49   ASN A OD1 1 
ATOM   339  N ND2 . ASN A 1 49  ? -2.680  -30.434 70.726 1.00 46.92 ? 49   ASN A ND2 1 
ATOM   340  N N   . HIS A 1 50  ? 0.297   -31.278 66.487 1.00 45.20 ? 50   HIS A N   1 
ATOM   341  C CA  . HIS A 1 50  ? 1.287   -31.391 65.412 1.00 44.82 ? 50   HIS A CA  1 
ATOM   342  C C   . HIS A 1 50  ? 1.327   -29.904 65.071 1.00 43.77 ? 50   HIS A C   1 
ATOM   343  O O   . HIS A 1 50  ? 0.367   -29.164 65.392 1.00 44.64 ? 50   HIS A O   1 
ATOM   344  C CB  . HIS A 1 50  ? 0.739   -32.201 64.207 1.00 45.56 ? 50   HIS A CB  1 
ATOM   345  C CG  . HIS A 1 50  ? 1.620   -32.206 62.972 1.00 47.76 ? 50   HIS A CG  1 
ATOM   346  N ND1 . HIS A 1 50  ? 2.120   -33.372 62.418 1.00 48.77 ? 50   HIS A ND1 1 
ATOM   347  C CD2 . HIS A 1 50  ? 2.051   -31.201 62.166 1.00 48.59 ? 50   HIS A CD2 1 
ATOM   348  C CE1 . HIS A 1 50  ? 2.842   -33.082 61.347 1.00 48.83 ? 50   HIS A CE1 1 
ATOM   349  N NE2 . HIS A 1 50  ? 2.820   -31.772 61.174 1.00 49.31 ? 50   HIS A NE2 1 
ATOM   350  N N   . SER A 1 51  ? 2.416   -29.467 64.446 1.00 41.15 ? 51   SER A N   1 
ATOM   351  C CA  . SER A 1 51  ? 2.605   -28.083 63.996 1.00 38.38 ? 51   SER A CA  1 
ATOM   352  C C   . SER A 1 51  ? 3.290   -27.222 65.055 1.00 35.84 ? 51   SER A C   1 
ATOM   353  O O   . SER A 1 51  ? 4.274   -27.636 65.664 1.00 36.86 ? 51   SER A O   1 
ATOM   354  C CB  . SER A 1 51  ? 1.310   -27.439 63.432 1.00 38.61 ? 51   SER A CB  1 
ATOM   355  O OG  . SER A 1 51  ? 0.382   -27.106 64.436 1.00 38.57 ? 51   SER A OG  1 
ATOM   356  N N   . TYR A 1 52  ? 2.795   -26.014 65.252 1.00 32.19 ? 52   TYR A N   1 
ATOM   357  C CA  . TYR A 1 52  ? 3.495   -25.051 66.065 1.00 28.38 ? 52   TYR A CA  1 
ATOM   358  C C   . TYR A 1 52  ? 2.728   -24.740 67.335 1.00 27.44 ? 52   TYR A C   1 
ATOM   359  O O   . TYR A 1 52  ? 1.518   -24.969 67.417 1.00 26.54 ? 52   TYR A O   1 
ATOM   360  C CB  . TYR A 1 52  ? 3.725   -23.803 65.230 1.00 27.07 ? 52   TYR A CB  1 
ATOM   361  C CG  . TYR A 1 52  ? 4.832   -23.977 64.217 1.00 25.47 ? 52   TYR A CG  1 
ATOM   362  C CD1 . TYR A 1 52  ? 4.616   -24.650 63.008 1.00 22.24 ? 52   TYR A CD1 1 
ATOM   363  C CD2 . TYR A 1 52  ? 6.108   -23.478 64.475 1.00 23.56 ? 52   TYR A CD2 1 
ATOM   364  C CE1 . TYR A 1 52  ? 5.658   -24.817 62.069 1.00 23.00 ? 52   TYR A CE1 1 
ATOM   365  C CE2 . TYR A 1 52  ? 7.138   -23.638 63.547 1.00 23.80 ? 52   TYR A CE2 1 
ATOM   366  C CZ  . TYR A 1 52  ? 6.908   -24.308 62.363 1.00 23.23 ? 52   TYR A CZ  1 
ATOM   367  O OH  . TYR A 1 52  ? 7.946   -24.426 61.483 1.00 25.30 ? 52   TYR A OH  1 
ATOM   368  N N   . HIS A 1 53  ? 3.440   -24.255 68.342 1.00 26.43 ? 53   HIS A N   1 
ATOM   369  C CA  . HIS A 1 53  ? 2.771   -23.718 69.526 1.00 26.29 ? 53   HIS A CA  1 
ATOM   370  C C   . HIS A 1 53  ? 3.273   -22.316 69.785 1.00 25.26 ? 53   HIS A C   1 
ATOM   371  O O   . HIS A 1 53  ? 4.407   -21.977 69.430 1.00 24.78 ? 53   HIS A O   1 
ATOM   372  C CB  . HIS A 1 53  ? 2.911   -24.651 70.754 1.00 26.99 ? 53   HIS A CB  1 
ATOM   373  C CG  . HIS A 1 53  ? 4.316   -24.839 71.220 1.00 28.27 ? 53   HIS A CG  1 
ATOM   374  N ND1 . HIS A 1 53  ? 4.844   -24.145 72.287 1.00 33.47 ? 53   HIS A ND1 1 
ATOM   375  C CD2 . HIS A 1 53  ? 5.315   -25.622 70.751 1.00 30.89 ? 53   HIS A CD2 1 
ATOM   376  C CE1 . HIS A 1 53  ? 6.106   -24.497 72.461 1.00 31.53 ? 53   HIS A CE1 1 
ATOM   377  N NE2 . HIS A 1 53  ? 6.419   -25.391 71.539 1.00 31.31 ? 53   HIS A NE2 1 
ATOM   378  N N   . VAL A 1 54  ? 2.414   -21.484 70.364 1.00 24.82 ? 54   VAL A N   1 
ATOM   379  C CA  . VAL A 1 54  ? 2.822   -20.147 70.759 1.00 24.16 ? 54   VAL A CA  1 
ATOM   380  C C   . VAL A 1 54  ? 3.758   -20.343 71.947 1.00 24.72 ? 54   VAL A C   1 
ATOM   381  O O   . VAL A 1 54  ? 3.431   -21.079 72.874 1.00 24.91 ? 54   VAL A O   1 
ATOM   382  C CB  . VAL A 1 54  ? 1.609   -19.234 71.148 1.00 24.04 ? 54   VAL A CB  1 
ATOM   383  C CG1 . VAL A 1 54  ? 2.092   -17.903 71.641 1.00 22.78 ? 54   VAL A CG1 1 
ATOM   384  C CG2 . VAL A 1 54  ? 0.626   -19.012 69.943 1.00 22.06 ? 54   VAL A CG2 1 
ATOM   385  N N   . GLU A 1 55  ? 4.935   -19.726 71.896 1.00 24.98 ? 55   GLU A N   1 
ATOM   386  C CA  . GLU A 1 55  ? 5.803   -19.707 73.044 1.00 25.74 ? 55   GLU A CA  1 
ATOM   387  C C   . GLU A 1 55  ? 5.669   -18.358 73.775 1.00 24.79 ? 55   GLU A C   1 
ATOM   388  O O   . GLU A 1 55  ? 5.914   -17.295 73.189 1.00 24.91 ? 55   GLU A O   1 
ATOM   389  C CB  . GLU A 1 55  ? 7.251   -19.974 72.613 1.00 27.04 ? 55   GLU A CB  1 
ATOM   390  C CG  . GLU A 1 55  ? 8.219   -20.242 73.773 1.00 32.32 ? 55   GLU A CG  1 
ATOM   391  C CD  . GLU A 1 55  ? 7.956   -21.551 74.499 1.00 37.05 ? 55   GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 55  ? 8.242   -22.631 73.931 1.00 40.44 ? 55   GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 55  ? 7.484   -21.500 75.659 1.00 40.08 ? 55   GLU A OE2 1 
ATOM   394  N N   . GLY A 1 56  ? 5.274   -18.396 75.045 1.00 22.92 ? 56   GLY A N   1 
ATOM   395  C CA  . GLY A 1 56  ? 5.245   -17.183 75.861 1.00 22.86 ? 56   GLY A CA  1 
ATOM   396  C C   . GLY A 1 56  ? 3.989   -16.367 75.573 1.00 23.13 ? 56   GLY A C   1 
ATOM   397  O O   . GLY A 1 56  ? 2.981   -16.916 75.131 1.00 21.87 ? 56   GLY A O   1 
ATOM   398  N N   . ASN A 1 57  ? 4.073   -15.064 75.807 1.00 22.98 ? 57   ASN A N   1 
ATOM   399  C CA  . ASN A 1 57  ? 2.976   -14.140 75.540 1.00 23.16 ? 57   ASN A CA  1 
ATOM   400  C C   . ASN A 1 57  ? 3.070   -13.456 74.172 1.00 22.62 ? 57   ASN A C   1 
ATOM   401  O O   . ASN A 1 57  ? 4.158   -13.257 73.606 1.00 22.26 ? 57   ASN A O   1 
ATOM   402  C CB  . ASN A 1 57  ? 2.821   -13.084 76.660 1.00 23.21 ? 57   ASN A CB  1 
ATOM   403  C CG  . ASN A 1 57  ? 2.648   -13.700 78.049 1.00 22.39 ? 57   ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 57  ? 2.204   -14.823 78.192 1.00 24.47 ? 57   ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 57  ? 3.021   -12.951 79.073 1.00 24.02 ? 57   ASN A ND2 1 
ATOM   406  N N   . LEU A 1 58  ? 1.899   -13.134 73.637 1.00 21.39 ? 58   LEU A N   1 
ATOM   407  C CA  . LEU A 1 58  ? 1.768   -12.204 72.533 1.00 21.09 ? 58   LEU A CA  1 
ATOM   408  C C   . LEU A 1 58  ? 2.176   -10.834 73.024 1.00 20.45 ? 58   LEU A C   1 
ATOM   409  O O   . LEU A 1 58  ? 1.967   -10.489 74.183 1.00 20.66 ? 58   LEU A O   1 
ATOM   410  C CB  . LEU A 1 58  ? 0.314   -12.179 71.988 1.00 21.20 ? 58   LEU A CB  1 
ATOM   411  C CG  . LEU A 1 58  ? -0.072  -13.134 70.860 1.00 21.09 ? 58   LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 58  ? 0.462   -14.516 71.123 1.00 22.16 ? 58   LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 58  ? -1.589  -13.200 70.686 1.00 21.12 ? 58   LEU A CD2 1 
ATOM   414  N N   . VAL A 1 59  ? 2.766   -10.054 72.136 1.00 20.57 ? 59   VAL A N   1 
ATOM   415  C CA  . VAL A 1 59  ? 3.270   -8.739  72.468 1.00 20.45 ? 59   VAL A CA  1 
ATOM   416  C C   . VAL A 1 59  ? 2.495   -7.730  71.633 1.00 20.62 ? 59   VAL A C   1 
ATOM   417  O O   . VAL A 1 59  ? 2.524   -7.809  70.431 1.00 19.94 ? 59   VAL A O   1 
ATOM   418  C CB  . VAL A 1 59  ? 4.790   -8.624  72.107 1.00 20.82 ? 59   VAL A CB  1 
ATOM   419  C CG1 . VAL A 1 59  ? 5.306   -7.228  72.389 1.00 21.11 ? 59   VAL A CG1 1 
ATOM   420  C CG2 . VAL A 1 59  ? 5.612   -9.671  72.872 1.00 20.49 ? 59   VAL A CG2 1 
ATOM   421  N N   . ASN A 1 60  ? 1.822   -6.774  72.274 1.00 20.95 ? 60   ASN A N   1 
ATOM   422  C CA  . ASN A 1 60  ? 1.249   -5.647  71.559 1.00 20.87 ? 60   ASN A CA  1 
ATOM   423  C C   . ASN A 1 60  ? 2.279   -4.754  70.894 1.00 21.43 ? 60   ASN A C   1 
ATOM   424  O O   . ASN A 1 60  ? 3.292   -4.403  71.503 1.00 20.99 ? 60   ASN A O   1 
ATOM   425  C CB  . ASN A 1 60  ? 0.413   -4.802  72.505 1.00 20.88 ? 60   ASN A CB  1 
ATOM   426  C CG  . ASN A 1 60  ? -0.853  -5.496  72.918 1.00 21.71 ? 60   ASN A CG  1 
ATOM   427  O OD1 . ASN A 1 60  ? -1.860  -5.443  72.211 1.00 23.94 ? 60   ASN A OD1 1 
ATOM   428  N ND2 . ASN A 1 60  ? -0.821  -6.145  74.073 1.00 20.05 ? 60   ASN A ND2 1 
ATOM   429  N N   . THR A 1 61  ? 1.991   -4.361  69.650 1.00 21.50 ? 61   THR A N   1 
ATOM   430  C CA  . THR A 1 61  ? 2.802   -3.413  68.907 1.00 22.32 ? 61   THR A CA  1 
ATOM   431  C C   . THR A 1 61  ? 1.870   -2.245  68.553 1.00 23.00 ? 61   THR A C   1 
ATOM   432  O O   . THR A 1 61  ? 0.669   -2.327  68.818 1.00 22.56 ? 61   THR A O   1 
ATOM   433  C CB  . THR A 1 61  ? 3.313   -4.046  67.606 1.00 22.51 ? 61   THR A CB  1 
ATOM   434  O OG1 . THR A 1 61  ? 2.180   -4.502  66.837 1.00 22.78 ? 61   THR A OG1 1 
ATOM   435  C CG2 . THR A 1 61  ? 4.275   -5.226  67.894 1.00 20.16 ? 61   THR A CG2 1 
ATOM   436  N N   . ASN A 1 62  ? 2.407   -1.176  67.956 1.00 23.46 ? 62   ASN A N   1 
ATOM   437  C CA  . ASN A 1 62  ? 1.560   -0.055  67.454 1.00 24.33 ? 62   ASN A CA  1 
ATOM   438  C C   . ASN A 1 62  ? 0.536   -0.506  66.406 1.00 23.23 ? 62   ASN A C   1 
ATOM   439  O O   . ASN A 1 62  ? -0.620  -0.035  66.401 1.00 23.58 ? 62   ASN A O   1 
ATOM   440  C CB  . ASN A 1 62  ? 2.424   1.091   66.899 1.00 24.94 ? 62   ASN A CB  1 
ATOM   441  C CG  . ASN A 1 62  ? 3.238   1.825   68.000 1.00 28.66 ? 62   ASN A CG  1 
ATOM   442  O OD1 . ASN A 1 62  ? 4.363   2.293   67.760 1.00 32.21 ? 62   ASN A OD1 1 
ATOM   443  N ND2 . ASN A 1 62  ? 2.667   1.929   69.190 1.00 30.06 ? 62   ASN A ND2 1 
ATOM   444  N N   . ALA A 1 63  ? 0.960   -1.451  65.561 1.00 21.94 ? 63   ALA A N   1 
ATOM   445  C CA  . ALA A 1 63  ? 0.178   -1.973  64.444 1.00 21.38 ? 63   ALA A CA  1 
ATOM   446  C C   . ALA A 1 63  ? -0.820  -3.089  64.791 1.00 20.71 ? 63   ALA A C   1 
ATOM   447  O O   . ALA A 1 63  ? -1.829  -3.265  64.090 1.00 20.74 ? 63   ALA A O   1 
ATOM   448  C CB  . ALA A 1 63  ? 1.127   -2.454  63.342 1.00 21.49 ? 63   ALA A CB  1 
ATOM   449  N N   . GLY A 1 64  ? -0.512  -3.848  65.842 1.00 19.58 ? 64   GLY A N   1 
ATOM   450  C CA  . GLY A 1 64  ? -1.231  -5.041  66.226 1.00 18.83 ? 64   GLY A CA  1 
ATOM   451  C C   . GLY A 1 64  ? -0.493  -5.807  67.311 1.00 18.81 ? 64   GLY A C   1 
ATOM   452  O O   . GLY A 1 64  ? -0.488  -5.403  68.473 1.00 19.01 ? 64   GLY A O   1 
ATOM   453  N N   . PHE A 1 65  ? 0.102   -6.936  66.936 1.00 18.61 ? 65   PHE A N   1 
ATOM   454  C CA  . PHE A 1 65  ? 0.831   -7.791  67.857 1.00 18.66 ? 65   PHE A CA  1 
ATOM   455  C C   . PHE A 1 65  ? 1.780   -8.742  67.113 1.00 18.75 ? 65   PHE A C   1 
ATOM   456  O O   . PHE A 1 65  ? 1.644   -8.953  65.914 1.00 18.07 ? 65   PHE A O   1 
ATOM   457  C CB  . PHE A 1 65  ? -0.122  -8.620  68.722 1.00 18.78 ? 65   PHE A CB  1 
ATOM   458  C CG  . PHE A 1 65  ? -0.952  -9.617  67.935 1.00 20.40 ? 65   PHE A CG  1 
ATOM   459  C CD1 . PHE A 1 65  ? -0.472  -10.905 67.691 1.00 18.95 ? 65   PHE A CD1 1 
ATOM   460  C CD2 . PHE A 1 65  ? -2.212  -9.259  67.448 1.00 21.33 ? 65   PHE A CD2 1 
ATOM   461  C CE1 . PHE A 1 65  ? -1.234  -11.824 66.982 1.00 19.18 ? 65   PHE A CE1 1 
ATOM   462  C CE2 . PHE A 1 65  ? -2.992  -10.165 66.756 1.00 20.96 ? 65   PHE A CE2 1 
ATOM   463  C CZ  . PHE A 1 65  ? -2.496  -11.449 66.505 1.00 20.04 ? 65   PHE A CZ  1 
ATOM   464  N N   . THR A 1 66  ? 2.733   -9.292  67.861 1.00 18.57 ? 66   THR A N   1 
ATOM   465  C CA  . THR A 1 66  ? 3.625   -10.350 67.392 1.00 20.10 ? 66   THR A CA  1 
ATOM   466  C C   . THR A 1 66  ? 3.522   -11.541 68.350 1.00 20.33 ? 66   THR A C   1 
ATOM   467  O O   . THR A 1 66  ? 3.134   -11.387 69.516 1.00 21.25 ? 66   THR A O   1 
ATOM   468  C CB  . THR A 1 66  ? 5.128   -9.857  67.331 1.00 20.31 ? 66   THR A CB  1 
ATOM   469  O OG1 . THR A 1 66  ? 5.525   -9.371  68.612 1.00 20.97 ? 66   THR A OG1 1 
ATOM   470  C CG2 . THR A 1 66  ? 5.287   -8.720  66.343 1.00 19.93 ? 66   THR A CG2 1 
ATOM   471  N N   . ALA A 1 67  ? 3.859   -12.732 67.860 1.00 20.12 ? 67   ALA A N   1 
ATOM   472  C CA  . ALA A 1 67  ? 3.880   -13.931 68.673 1.00 20.36 ? 67   ALA A CA  1 
ATOM   473  C C   . ALA A 1 67  ? 5.048   -14.776 68.228 1.00 21.08 ? 67   ALA A C   1 
ATOM   474  O O   . ALA A 1 67  ? 5.349   -14.844 67.048 1.00 20.24 ? 67   ALA A O   1 
ATOM   475  C CB  . ALA A 1 67  ? 2.608   -14.723 68.478 1.00 19.32 ? 67   ALA A CB  1 
ATOM   476  N N   . ARG A 1 68  ? 5.673   -15.456 69.174 1.00 22.65 ? 68   ARG A N   1 
ATOM   477  C CA  . ARG A 1 68  ? 6.718   -16.412 68.824 1.00 24.01 ? 68   ARG A CA  1 
ATOM   478  C C   . ARG A 1 68  ? 6.100   -17.782 68.750 1.00 23.83 ? 68   ARG A C   1 
ATOM   479  O O   . ARG A 1 68  ? 5.416   -18.210 69.695 1.00 23.51 ? 68   ARG A O   1 
ATOM   480  C CB  . ARG A 1 68  ? 7.853   -16.363 69.835 1.00 24.59 ? 68   ARG A CB  1 
ATOM   481  C CG  . ARG A 1 68  ? 8.563   -15.024 69.836 1.00 28.16 ? 68   ARG A CG  1 
ATOM   482  C CD  . ARG A 1 68  ? 9.249   -14.721 71.192 1.00 34.92 ? 68   ARG A CD  1 
ATOM   483  N NE  . ARG A 1 68  ? 10.410  -13.833 71.036 1.00 41.79 ? 68   ARG A NE  1 
ATOM   484  C CZ  . ARG A 1 68  ? 11.000  -13.148 72.022 1.00 44.02 ? 68   ARG A CZ  1 
ATOM   485  N NH1 . ARG A 1 68  ? 10.544  -13.217 73.272 1.00 44.40 ? 68   ARG A NH1 1 
ATOM   486  N NH2 . ARG A 1 68  ? 12.048  -12.375 71.748 1.00 44.07 ? 68   ARG A NH2 1 
ATOM   487  N N   . LEU A 1 69  ? 6.298   -18.443 67.607 1.00 23.48 ? 69   LEU A N   1 
ATOM   488  C CA  . LEU A 1 69  ? 5.861   -19.814 67.429 1.00 24.88 ? 69   LEU A CA  1 
ATOM   489  C C   . LEU A 1 69  ? 7.073   -20.751 67.431 1.00 26.42 ? 69   LEU A C   1 
ATOM   490  O O   . LEU A 1 69  ? 8.099   -20.455 66.821 1.00 25.71 ? 69   LEU A O   1 
ATOM   491  C CB  . LEU A 1 69  ? 5.041   -19.986 66.146 1.00 24.57 ? 69   LEU A CB  1 
ATOM   492  C CG  . LEU A 1 69  ? 4.019   -18.921 65.737 1.00 24.51 ? 69   LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 69  ? 3.072   -19.493 64.675 1.00 24.25 ? 69   LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 69  ? 3.261   -18.430 66.949 1.00 23.83 ? 69   LEU A CD2 1 
ATOM   495  N N   . LYS A 1 70  ? 6.950   -21.857 68.152 1.00 28.35 ? 70   LYS A N   1 
ATOM   496  C CA  . LYS A 1 70  ? 8.020   -22.820 68.259 1.00 31.68 ? 70   LYS A CA  1 
ATOM   497  C C   . LYS A 1 70  ? 7.521   -24.112 67.627 1.00 32.95 ? 70   LYS A C   1 
ATOM   498  O O   . LYS A 1 70  ? 6.400   -24.541 67.893 1.00 32.08 ? 70   LYS A O   1 
ATOM   499  C CB  . LYS A 1 70  ? 8.394   -23.023 69.740 1.00 31.67 ? 70   LYS A CB  1 
ATOM   500  C CG  . LYS A 1 70  ? 9.848   -23.509 70.043 1.00 33.63 ? 70   LYS A CG  1 
ATOM   501  C CD  . LYS A 1 70  ? 10.213  -23.176 71.510 1.00 33.18 ? 70   LYS A CD  1 
ATOM   502  C CE  . LYS A 1 70  ? 11.254  -24.146 72.122 1.00 38.82 ? 70   LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 70  ? 11.231  -24.149 73.628 1.00 37.96 ? 70   LYS A NZ  1 
ATOM   504  N N   . ASN A 1 71  ? 8.349   -24.708 66.768 1.00 35.37 ? 71   ASN A N   1 
ATOM   505  C CA  . ASN A 1 71  ? 8.047   -25.999 66.153 1.00 38.32 ? 71   ASN A CA  1 
ATOM   506  C C   . ASN A 1 71  ? 7.965   -27.122 67.201 1.00 40.26 ? 71   ASN A C   1 
ATOM   507  O O   . ASN A 1 71  ? 8.904   -27.323 67.982 1.00 40.40 ? 71   ASN A O   1 
ATOM   508  C CB  . ASN A 1 71  ? 9.114   -26.323 65.086 1.00 38.35 ? 71   ASN A CB  1 
ATOM   509  C CG  . ASN A 1 71  ? 8.726   -27.478 64.173 1.00 39.77 ? 71   ASN A CG  1 
ATOM   510  O OD1 . ASN A 1 71  ? 7.598   -27.558 63.675 1.00 40.10 ? 71   ASN A OD1 1 
ATOM   511  N ND2 . ASN A 1 71  ? 9.686   -28.379 63.927 1.00 41.72 ? 71   ASN A ND2 1 
ATOM   512  N N   . LEU A 1 72  ? 6.838   -27.835 67.220 1.00 42.54 ? 72   LEU A N   1 
ATOM   513  C CA  . LEU A 1 72  ? 6.731   -29.099 67.938 1.00 44.92 ? 72   LEU A CA  1 
ATOM   514  C C   . LEU A 1 72  ? 7.442   -30.136 67.077 1.00 46.59 ? 72   LEU A C   1 
ATOM   515  O O   . LEU A 1 72  ? 6.948   -30.472 65.999 1.00 46.81 ? 72   LEU A O   1 
ATOM   516  C CB  . LEU A 1 72  ? 5.270   -29.540 68.097 1.00 45.23 ? 72   LEU A CB  1 
ATOM   517  C CG  . LEU A 1 72  ? 4.263   -29.083 69.162 1.00 45.81 ? 72   LEU A CG  1 
ATOM   518  C CD1 . LEU A 1 72  ? 4.900   -28.851 70.542 1.00 46.52 ? 72   LEU A CD1 1 
ATOM   519  C CD2 . LEU A 1 72  ? 3.487   -27.883 68.685 1.00 45.20 ? 72   LEU A CD2 1 
ATOM   520  N N   . PRO A 1 73  ? 8.604   -30.644 67.529 1.00 48.29 ? 73   PRO A N   1 
ATOM   521  C CA  . PRO A 1 73  ? 9.370   -31.540 66.652 1.00 49.31 ? 73   PRO A CA  1 
ATOM   522  C C   . PRO A 1 73  ? 8.495   -32.586 65.957 1.00 49.92 ? 73   PRO A C   1 
ATOM   523  O O   . PRO A 1 73  ? 7.608   -33.181 66.588 1.00 50.08 ? 73   PRO A O   1 
ATOM   524  C CB  . PRO A 1 73  ? 10.355  -32.203 67.615 1.00 49.42 ? 73   PRO A CB  1 
ATOM   525  C CG  . PRO A 1 73  ? 10.626  -31.137 68.618 1.00 49.60 ? 73   PRO A CG  1 
ATOM   526  C CD  . PRO A 1 73  ? 9.279   -30.451 68.828 1.00 48.72 ? 73   PRO A CD  1 
ATOM   527  N N   . SER A 1 74  ? 8.720   -32.751 64.657 1.00 50.18 ? 74   SER A N   1 
ATOM   528  C CA  . SER A 1 74  ? 8.089   -33.808 63.875 1.00 50.79 ? 74   SER A CA  1 
ATOM   529  C C   . SER A 1 74  ? 9.002   -34.194 62.720 1.00 50.97 ? 74   SER A C   1 
ATOM   530  O O   . SER A 1 74  ? 10.119  -33.685 62.621 1.00 50.81 ? 74   SER A O   1 
ATOM   531  C CB  . SER A 1 74  ? 6.713   -33.386 63.349 1.00 50.96 ? 74   SER A CB  1 
ATOM   532  O OG  . SER A 1 74  ? 5.995   -34.529 62.902 1.00 51.20 ? 74   SER A OG  1 
ATOM   533  N N   . SER A 1 75  ? 8.511   -35.083 61.853 1.00 51.22 ? 75   SER A N   1 
ATOM   534  C CA  . SER A 1 75  ? 9.278   -35.599 60.719 1.00 51.24 ? 75   SER A CA  1 
ATOM   535  C C   . SER A 1 75  ? 9.674   -34.520 59.720 1.00 51.08 ? 75   SER A C   1 
ATOM   536  O O   . SER A 1 75  ? 8.860   -33.658 59.386 1.00 51.53 ? 75   SER A O   1 
ATOM   537  C CB  . SER A 1 75  ? 8.511   -36.719 60.012 1.00 51.17 ? 75   SER A CB  1 
ATOM   538  O OG  . SER A 1 75  ? 8.707   -37.946 60.691 1.00 51.28 ? 75   SER A OG  1 
ATOM   539  N N   . PRO A 1 76  ? 10.943  -34.554 59.263 1.00 50.84 ? 76   PRO A N   1 
ATOM   540  C CA  . PRO A 1 76  ? 11.424  -33.674 58.206 1.00 50.26 ? 76   PRO A CA  1 
ATOM   541  C C   . PRO A 1 76  ? 11.155  -34.279 56.820 1.00 49.61 ? 76   PRO A C   1 
ATOM   542  O O   . PRO A 1 76  ? 12.020  -34.967 56.248 1.00 50.02 ? 76   PRO A O   1 
ATOM   543  C CB  . PRO A 1 76  ? 12.932  -33.569 58.492 1.00 50.32 ? 76   PRO A CB  1 
ATOM   544  C CG  . PRO A 1 76  ? 13.236  -34.607 59.537 1.00 50.56 ? 76   PRO A CG  1 
ATOM   545  C CD  . PRO A 1 76  ? 12.015  -35.438 59.743 1.00 50.90 ? 76   PRO A CD  1 
ATOM   546  N N   . VAL A 1 77  ? 9.958   -34.017 56.293 1.00 48.49 ? 77   VAL A N   1 
ATOM   547  C CA  . VAL A 1 77  ? 9.500   -34.606 55.032 1.00 47.29 ? 77   VAL A CA  1 
ATOM   548  C C   . VAL A 1 77  ? 10.058  -33.894 53.799 1.00 46.41 ? 77   VAL A C   1 
ATOM   549  O O   . VAL A 1 77  ? 10.663  -34.523 52.915 1.00 46.58 ? 77   VAL A O   1 
ATOM   550  C CB  . VAL A 1 77  ? 7.961   -34.614 54.955 1.00 47.53 ? 77   VAL A CB  1 
ATOM   551  C CG1 . VAL A 1 77  ? 7.493   -35.216 53.641 1.00 47.56 ? 77   VAL A CG1 1 
ATOM   552  C CG2 . VAL A 1 77  ? 7.381   -35.374 56.132 1.00 47.92 ? 77   VAL A CG2 1 
ATOM   553  N N   . PHE A 1 78  ? 9.840   -32.586 53.725 1.00 44.58 ? 78   PHE A N   1 
ATOM   554  C CA  . PHE A 1 78  ? 10.283  -31.827 52.567 1.00 42.87 ? 78   PHE A CA  1 
ATOM   555  C C   . PHE A 1 78  ? 11.421  -30.896 52.947 1.00 42.59 ? 78   PHE A C   1 
ATOM   556  O O   . PHE A 1 78  ? 11.481  -29.738 52.531 1.00 42.24 ? 78   PHE A O   1 
ATOM   557  C CB  . PHE A 1 78  ? 9.117   -31.091 51.920 1.00 41.56 ? 78   PHE A CB  1 
ATOM   558  C CG  . PHE A 1 78  ? 7.967   -31.982 51.569 1.00 39.67 ? 78   PHE A CG  1 
ATOM   559  C CD1 . PHE A 1 78  ? 6.731   -31.802 52.169 1.00 36.68 ? 78   PHE A CD1 1 
ATOM   560  C CD2 . PHE A 1 78  ? 8.120   -33.010 50.647 1.00 36.94 ? 78   PHE A CD2 1 
ATOM   561  C CE1 . PHE A 1 78  ? 5.646   -32.624 51.840 1.00 38.75 ? 78   PHE A CE1 1 
ATOM   562  C CE2 . PHE A 1 78  ? 7.051   -33.829 50.316 1.00 37.35 ? 78   PHE A CE2 1 
ATOM   563  C CZ  . PHE A 1 78  ? 5.809   -33.634 50.919 1.00 38.00 ? 78   PHE A CZ  1 
ATOM   564  N N   . GLY A 1 79  ? 12.317  -31.429 53.766 1.00 42.80 ? 79   GLY A N   1 
ATOM   565  C CA  . GLY A 1 79  ? 13.567  -30.762 54.090 1.00 42.56 ? 79   GLY A CA  1 
ATOM   566  C C   . GLY A 1 79  ? 13.583  -29.877 55.318 1.00 42.31 ? 79   GLY A C   1 
ATOM   567  O O   . GLY A 1 79  ? 12.762  -30.026 56.235 1.00 42.81 ? 79   GLY A O   1 
ATOM   568  N N   . SER A 1 80  ? 14.541  -28.952 55.290 1.00 42.13 ? 80   SER A N   1 
ATOM   569  C CA  . SER A 1 80  ? 14.939  -28.071 56.385 1.00 41.18 ? 80   SER A CA  1 
ATOM   570  C C   . SER A 1 80  ? 13.800  -27.207 56.967 1.00 40.22 ? 80   SER A C   1 
ATOM   571  O O   . SER A 1 80  ? 13.453  -26.155 56.426 1.00 39.54 ? 80   SER A O   1 
ATOM   572  C CB  . SER A 1 80  ? 16.109  -27.195 55.908 1.00 41.66 ? 80   SER A CB  1 
ATOM   573  O OG  . SER A 1 80  ? 16.982  -26.875 56.977 1.00 43.09 ? 80   SER A OG  1 
ATOM   574  N N   . ASN A 1 81  ? 13.271  -27.678 58.096 1.00 38.76 ? 81   ASN A N   1 
ATOM   575  C CA  . ASN A 1 81  ? 12.171  -27.078 58.829 1.00 37.87 ? 81   ASN A CA  1 
ATOM   576  C C   . ASN A 1 81  ? 12.579  -25.808 59.611 1.00 37.24 ? 81   ASN A C   1 
ATOM   577  O O   . ASN A 1 81  ? 13.762  -25.604 59.932 1.00 36.63 ? 81   ASN A O   1 
ATOM   578  C CB  . ASN A 1 81  ? 11.603  -28.145 59.759 1.00 37.94 ? 81   ASN A CB  1 
ATOM   579  C CG  . ASN A 1 81  ? 10.246  -27.796 60.302 1.00 39.06 ? 81   ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 81  ? 10.132  -27.017 61.242 1.00 40.32 ? 81   ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 81  ? 9.197   -28.415 59.745 1.00 41.34 ? 81   ASN A ND2 1 
ATOM   582  N N   . VAL A 1 82  ? 11.593  -24.953 59.892 1.00 35.83 ? 82   VAL A N   1 
ATOM   583  C CA  . VAL A 1 82  ? 11.829  -23.670 60.560 1.00 34.43 ? 82   VAL A CA  1 
ATOM   584  C C   . VAL A 1 82  ? 11.350  -23.748 62.008 1.00 34.12 ? 82   VAL A C   1 
ATOM   585  O O   . VAL A 1 82  ? 10.133  -23.810 62.279 1.00 34.02 ? 82   VAL A O   1 
ATOM   586  C CB  . VAL A 1 82  ? 11.231  -22.478 59.749 1.00 34.47 ? 82   VAL A CB  1 
ATOM   587  C CG1 . VAL A 1 82  ? 11.225  -21.193 60.547 1.00 33.27 ? 82   VAL A CG1 1 
ATOM   588  C CG2 . VAL A 1 82  ? 12.005  -22.285 58.440 1.00 32.89 ? 82   VAL A CG2 1 
ATOM   589  N N   . ASP A 1 83  ? 12.326  -23.789 62.922 1.00 32.84 ? 83   ASP A N   1 
ATOM   590  C CA  . ASP A 1 83  ? 12.084  -24.059 64.352 1.00 33.11 ? 83   ASP A CA  1 
ATOM   591  C C   . ASP A 1 83  ? 11.438  -22.905 65.105 1.00 31.52 ? 83   ASP A C   1 
ATOM   592  O O   . ASP A 1 83  ? 10.615  -23.130 65.981 1.00 32.12 ? 83   ASP A O   1 
ATOM   593  C CB  . ASP A 1 83  ? 13.375  -24.435 65.094 1.00 33.26 ? 83   ASP A CB  1 
ATOM   594  C CG  . ASP A 1 83  ? 13.892  -25.821 64.730 1.00 36.93 ? 83   ASP A CG  1 
ATOM   595  O OD1 . ASP A 1 83  ? 13.101  -26.680 64.254 1.00 37.41 ? 83   ASP A OD1 1 
ATOM   596  O OD2 . ASP A 1 83  ? 15.117  -26.043 64.934 1.00 40.08 ? 83   ASP A OD2 1 
ATOM   597  N N   . ASN A 1 84  ? 11.848  -21.682 64.801 1.00 29.84 ? 84   ASN A N   1 
ATOM   598  C CA  . ASN A 1 84  ? 11.257  -20.505 65.444 1.00 28.81 ? 84   ASN A CA  1 
ATOM   599  C C   . ASN A 1 84  ? 10.654  -19.554 64.439 1.00 26.79 ? 84   ASN A C   1 
ATOM   600  O O   . ASN A 1 84  ? 11.374  -18.901 63.680 1.00 26.10 ? 84   ASN A O   1 
ATOM   601  C CB  . ASN A 1 84  ? 12.277  -19.786 66.322 1.00 29.18 ? 84   ASN A CB  1 
ATOM   602  C CG  . ASN A 1 84  ? 12.701  -20.622 67.505 1.00 31.23 ? 84   ASN A CG  1 
ATOM   603  O OD1 . ASN A 1 84  ? 13.780  -21.210 67.499 1.00 36.61 ? 84   ASN A OD1 1 
ATOM   604  N ND2 . ASN A 1 84  ? 11.849  -20.703 68.514 1.00 33.66 ? 84   ASN A ND2 1 
ATOM   605  N N   . VAL A 1 85  ? 9.324   -19.501 64.447 1.00 24.84 ? 85   VAL A N   1 
ATOM   606  C CA  . VAL A 1 85  ? 8.535   -18.687 63.509 1.00 23.27 ? 85   VAL A CA  1 
ATOM   607  C C   . VAL A 1 85  ? 7.991   -17.438 64.230 1.00 22.55 ? 85   VAL A C   1 
ATOM   608  O O   . VAL A 1 85  ? 7.660   -17.508 65.405 1.00 22.19 ? 85   VAL A O   1 
ATOM   609  C CB  . VAL A 1 85  ? 7.358   -19.533 62.881 1.00 23.44 ? 85   VAL A CB  1 
ATOM   610  C CG1 . VAL A 1 85  ? 6.359   -18.652 62.141 1.00 21.35 ? 85   VAL A CG1 1 
ATOM   611  C CG2 . VAL A 1 85  ? 7.915   -20.552 61.908 1.00 22.31 ? 85   VAL A CG2 1 
ATOM   612  N N   . LEU A 1 86  ? 7.957   -16.300 63.533 1.00 21.05 ? 86   LEU A N   1 
ATOM   613  C CA  . LEU A 1 86  ? 7.426   -15.086 64.081 1.00 20.22 ? 86   LEU A CA  1 
ATOM   614  C C   . LEU A 1 86  ? 6.096   -14.802 63.398 1.00 19.96 ? 86   LEU A C   1 
ATOM   615  O O   . LEU A 1 86  ? 5.995   -14.767 62.180 1.00 20.21 ? 86   LEU A O   1 
ATOM   616  C CB  . LEU A 1 86  ? 8.392   -13.900 63.901 1.00 20.12 ? 86   LEU A CB  1 
ATOM   617  C CG  . LEU A 1 86  ? 7.977   -12.559 64.512 1.00 19.84 ? 86   LEU A CG  1 
ATOM   618  C CD1 . LEU A 1 86  ? 8.112   -12.526 66.031 1.00 21.08 ? 86   LEU A CD1 1 
ATOM   619  C CD2 . LEU A 1 86  ? 8.737   -11.395 63.885 1.00 20.20 ? 86   LEU A CD2 1 
ATOM   620  N N   . LEU A 1 87  ? 5.069   -14.627 64.197 1.00 18.70 ? 87   LEU A N   1 
ATOM   621  C CA  . LEU A 1 87  ? 3.831   -14.110 63.673 1.00 17.85 ? 87   LEU A CA  1 
ATOM   622  C C   . LEU A 1 87  ? 3.801   -12.608 63.938 1.00 17.31 ? 87   LEU A C   1 
ATOM   623  O O   . LEU A 1 87  ? 3.986   -12.177 65.061 1.00 16.59 ? 87   LEU A O   1 
ATOM   624  C CB  . LEU A 1 87  ? 2.659   -14.836 64.346 1.00 17.40 ? 87   LEU A CB  1 
ATOM   625  C CG  . LEU A 1 87  ? 1.286   -14.183 64.138 1.00 17.32 ? 87   LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 87  ? 0.859   -14.268 62.672 1.00 14.83 ? 87   LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 87  ? 0.312   -14.898 65.042 1.00 15.34 ? 87   LEU A CD2 1 
ATOM   628  N N   . THR A 1 88  ? 3.598   -11.823 62.886 1.00 18.09 ? 88   THR A N   1 
ATOM   629  C CA  . THR A 1 88  ? 3.433   -10.392 62.973 1.00 18.90 ? 88   THR A CA  1 
ATOM   630  C C   . THR A 1 88  ? 2.045   -10.102 62.397 1.00 19.58 ? 88   THR A C   1 
ATOM   631  O O   . THR A 1 88  ? 1.772   -10.444 61.241 1.00 19.68 ? 88   THR A O   1 
ATOM   632  C CB  . THR A 1 88  ? 4.532   -9.697  62.156 1.00 19.05 ? 88   THR A CB  1 
ATOM   633  O OG1 . THR A 1 88  ? 5.810   -10.120 62.655 1.00 21.87 ? 88   THR A OG1 1 
ATOM   634  C CG2 . THR A 1 88  ? 4.453   -8.171  62.245 1.00 20.75 ? 88   THR A CG2 1 
ATOM   635  N N   . ALA A 1 89  ? 1.165   -9.534  63.220 1.00 19.73 ? 89   ALA A N   1 
ATOM   636  C CA  . ALA A 1 89  ? -0.200  -9.192  62.814 1.00 19.06 ? 89   ALA A CA  1 
ATOM   637  C C   . ALA A 1 89  ? -0.420  -7.697  62.845 1.00 19.45 ? 89   ALA A C   1 
ATOM   638  O O   . ALA A 1 89  ? -0.049  -7.022  63.824 1.00 19.29 ? 89   ALA A O   1 
ATOM   639  C CB  . ALA A 1 89  ? -1.217  -9.911  63.707 1.00 19.68 ? 89   ALA A CB  1 
ATOM   640  N N   . GLU A 1 90  ? -1.010  -7.163  61.766 1.00 18.84 ? 90   GLU A N   1 
ATOM   641  C CA  . GLU A 1 90  ? -1.209  -5.730  61.625 1.00 18.51 ? 90   GLU A CA  1 
ATOM   642  C C   . GLU A 1 90  ? -2.684  -5.427  61.303 1.00 18.39 ? 90   GLU A C   1 
ATOM   643  O O   . GLU A 1 90  ? -3.222  -5.892  60.313 1.00 16.97 ? 90   GLU A O   1 
ATOM   644  C CB  . GLU A 1 90  ? -0.276  -5.140  60.564 1.00 17.78 ? 90   GLU A CB  1 
ATOM   645  C CG  . GLU A 1 90  ? 1.219   -5.212  60.960 1.00 19.69 ? 90   GLU A CG  1 
ATOM   646  C CD  . GLU A 1 90  ? 2.173   -4.837  59.841 1.00 21.63 ? 90   GLU A CD  1 
ATOM   647  O OE1 . GLU A 1 90  ? 1.768   -4.939  58.663 1.00 25.40 ? 90   GLU A OE1 1 
ATOM   648  O OE2 . GLU A 1 90  ? 3.340   -4.433  60.140 1.00 27.12 ? 90   GLU A OE2 1 
ATOM   649  N N   . TYR A 1 91  ? -3.303  -4.653  62.176 1.00 17.64 ? 91   TYR A N   1 
ATOM   650  C CA  . TYR A 1 91  ? -4.683  -4.179  62.031 1.00 18.08 ? 91   TYR A CA  1 
ATOM   651  C C   . TYR A 1 91  ? -4.674  -2.964  61.109 1.00 16.21 ? 91   TYR A C   1 
ATOM   652  O O   . TYR A 1 91  ? -4.713  -1.824  61.554 1.00 17.22 ? 91   TYR A O   1 
ATOM   653  C CB  . TYR A 1 91  ? -5.195  -3.809  63.420 1.00 18.68 ? 91   TYR A CB  1 
ATOM   654  C CG  . TYR A 1 91  ? -5.352  -4.989  64.376 1.00 20.59 ? 91   TYR A CG  1 
ATOM   655  C CD1 . TYR A 1 91  ? -6.295  -5.976  64.142 1.00 22.03 ? 91   TYR A CD1 1 
ATOM   656  C CD2 . TYR A 1 91  ? -4.618  -5.065  65.559 1.00 22.92 ? 91   TYR A CD2 1 
ATOM   657  C CE1 . TYR A 1 91  ? -6.459  -7.055  65.024 1.00 21.94 ? 91   TYR A CE1 1 
ATOM   658  C CE2 . TYR A 1 91  ? -4.794  -6.144  66.465 1.00 22.54 ? 91   TYR A CE2 1 
ATOM   659  C CZ  . TYR A 1 91  ? -5.709  -7.129  66.174 1.00 20.98 ? 91   TYR A CZ  1 
ATOM   660  O OH  . TYR A 1 91  ? -5.918  -8.182  67.036 1.00 21.79 ? 91   TYR A OH  1 
ATOM   661  N N   . GLN A 1 92  ? -4.573  -3.191  59.811 1.00 16.09 ? 92   GLN A N   1 
ATOM   662  C CA  . GLN A 1 92  ? -4.129  -2.127  58.912 1.00 15.75 ? 92   GLN A CA  1 
ATOM   663  C C   . GLN A 1 92  ? -5.222  -1.086  58.646 1.00 15.84 ? 92   GLN A C   1 
ATOM   664  O O   . GLN A 1 92  ? -4.952  0.089   58.606 1.00 15.42 ? 92   GLN A O   1 
ATOM   665  C CB  . GLN A 1 92  ? -3.614  -2.710  57.600 1.00 15.74 ? 92   GLN A CB  1 
ATOM   666  C CG  . GLN A 1 92  ? -2.231  -3.377  57.737 1.00 15.51 ? 92   GLN A CG  1 
ATOM   667  C CD  . GLN A 1 92  ? -1.571  -3.692  56.392 1.00 16.13 ? 92   GLN A CD  1 
ATOM   668  O OE1 . GLN A 1 92  ? -2.211  -3.665  55.337 1.00 13.01 ? 92   GLN A OE1 1 
ATOM   669  N NE2 . GLN A 1 92  ? -0.265  -3.999  56.436 1.00 15.85 ? 92   GLN A NE2 1 
ATOM   670  N N   . THR A 1 93  ? -6.454  -1.545  58.471 1.00 16.12 ? 93   THR A N   1 
ATOM   671  C CA  . THR A 1 93  ? -7.599  -0.650  58.271 1.00 16.18 ? 93   THR A CA  1 
ATOM   672  C C   . THR A 1 93  ? -8.774  -1.325  58.924 1.00 16.47 ? 93   THR A C   1 
ATOM   673  O O   . THR A 1 93  ? -8.671  -2.460  59.340 1.00 17.05 ? 93   THR A O   1 
ATOM   674  C CB  . THR A 1 93  ? -7.865  -0.354  56.764 1.00 16.78 ? 93   THR A CB  1 
ATOM   675  O OG1 . THR A 1 93  ? -8.634  -1.403  56.176 1.00 17.88 ? 93   THR A OG1 1 
ATOM   676  C CG2 . THR A 1 93  ? -6.546  -0.198  55.948 1.00 16.65 ? 93   THR A CG2 1 
ATOM   677  N N   . SER A 1 94  ? -9.918  -0.652  59.011 1.00 16.73 ? 94   SER A N   1 
ATOM   678  C CA  . SER A 1 94  ? -11.102 -1.286  59.539 1.00 16.73 ? 94   SER A CA  1 
ATOM   679  C C   . SER A 1 94  ? -11.493 -2.535  58.768 1.00 15.81 ? 94   SER A C   1 
ATOM   680  O O   . SER A 1 94  ? -12.181 -3.401  59.304 1.00 16.18 ? 94   SER A O   1 
ATOM   681  C CB  . SER A 1 94  ? -12.248 -0.271  59.522 1.00 17.55 ? 94   SER A CB  1 
ATOM   682  O OG  . SER A 1 94  ? -11.917 0.758   60.433 1.00 22.36 ? 94   SER A OG  1 
ATOM   683  N N   . ASN A 1 95  ? -11.060 -2.639  57.510 1.00 14.97 ? 95   ASN A N   1 
ATOM   684  C CA  . ASN A 1 95  ? -11.494 -3.736  56.663 1.00 15.87 ? 95   ASN A CA  1 
ATOM   685  C C   . ASN A 1 95  ? -10.409 -4.667  56.135 1.00 16.50 ? 95   ASN A C   1 
ATOM   686  O O   . ASN A 1 95  ? -10.708 -5.595  55.410 1.00 17.63 ? 95   ASN A O   1 
ATOM   687  C CB  . ASN A 1 95  ? -12.315 -3.180  55.511 1.00 16.58 ? 95   ASN A CB  1 
ATOM   688  C CG  . ASN A 1 95  ? -13.577 -2.542  55.990 1.00 18.80 ? 95   ASN A CG  1 
ATOM   689  O OD1 . ASN A 1 95  ? -14.551 -3.231  56.271 1.00 26.84 ? 95   ASN A OD1 1 
ATOM   690  N ND2 . ASN A 1 95  ? -13.570 -1.240  56.114 1.00 20.13 ? 95   ASN A ND2 1 
ATOM   691  N N   . ARG A 1 96  ? -9.159  -4.403  56.497 1.00 15.68 ? 96   ARG A N   1 
ATOM   692  C CA  . ARG A 1 96  ? -8.030  -5.168  55.979 1.00 15.23 ? 96   ARG A CA  1 
ATOM   693  C C   . ARG A 1 96  ? -7.159  -5.571  57.143 1.00 14.43 ? 96   ARG A C   1 
ATOM   694  O O   . ARG A 1 96  ? -6.669  -4.715  57.892 1.00 15.20 ? 96   ARG A O   1 
ATOM   695  C CB  . ARG A 1 96  ? -7.213  -4.369  54.957 1.00 14.58 ? 96   ARG A CB  1 
ATOM   696  C CG  . ARG A 1 96  ? -5.961  -5.153  54.438 1.00 15.87 ? 96   ARG A CG  1 
ATOM   697  C CD  . ARG A 1 96  ? -5.227  -4.408  53.345 1.00 13.99 ? 96   ARG A CD  1 
ATOM   698  N NE  . ARG A 1 96  ? -4.469  -3.267  53.833 1.00 15.67 ? 96   ARG A NE  1 
ATOM   699  C CZ  . ARG A 1 96  ? -4.621  -2.032  53.391 1.00 19.49 ? 96   ARG A CZ  1 
ATOM   700  N NH1 . ARG A 1 96  ? -5.558  -1.757  52.487 1.00 17.99 ? 96   ARG A NH1 1 
ATOM   701  N NH2 . ARG A 1 96  ? -3.838  -1.061  53.855 1.00 20.66 ? 96   ARG A NH2 1 
ATOM   702  N N   . PHE A 1 97  ? -7.031  -6.876  57.321 1.00 14.77 ? 97   PHE A N   1 
ATOM   703  C CA  . PHE A 1 97  ? -6.149  -7.461  58.306 1.00 15.16 ? 97   PHE A CA  1 
ATOM   704  C C   . PHE A 1 97  ? -4.949  -8.029  57.549 1.00 15.75 ? 97   PHE A C   1 
ATOM   705  O O   . PHE A 1 97  ? -5.115  -8.639  56.479 1.00 13.91 ? 97   PHE A O   1 
ATOM   706  C CB  . PHE A 1 97  ? -6.874  -8.577  59.074 1.00 14.93 ? 97   PHE A CB  1 
ATOM   707  C CG  . PHE A 1 97  ? -6.009  -9.270  60.094 1.00 17.25 ? 97   PHE A CG  1 
ATOM   708  C CD1 . PHE A 1 97  ? -5.380  -8.541  61.114 1.00 18.75 ? 97   PHE A CD1 1 
ATOM   709  C CD2 . PHE A 1 97  ? -5.759  -10.633 59.994 1.00 15.79 ? 97   PHE A CD2 1 
ATOM   710  C CE1 . PHE A 1 97  ? -4.539  -9.170  62.033 1.00 16.87 ? 97   PHE A CE1 1 
ATOM   711  C CE2 . PHE A 1 97  ? -4.958  -11.269 60.911 1.00 16.89 ? 97   PHE A CE2 1 
ATOM   712  C CZ  . PHE A 1 97  ? -4.343  -10.546 61.933 1.00 16.21 ? 97   PHE A CZ  1 
ATOM   713  N N   . HIS A 1 98  ? -3.756  -7.829  58.106 1.00 16.61 ? 98   HIS A N   1 
ATOM   714  C CA  . HIS A 1 98  ? -2.522  -8.340  57.527 1.00 17.17 ? 98   HIS A CA  1 
ATOM   715  C C   . HIS A 1 98  ? -1.791  -9.219  58.567 1.00 17.75 ? 98   HIS A C   1 
ATOM   716  O O   . HIS A 1 98  ? -1.591  -8.813  59.711 1.00 17.60 ? 98   HIS A O   1 
ATOM   717  C CB  . HIS A 1 98  ? -1.651  -7.158  57.062 1.00 17.90 ? 98   HIS A CB  1 
ATOM   718  C CG  . HIS A 1 98  ? -0.273  -7.536  56.599 1.00 17.92 ? 98   HIS A CG  1 
ATOM   719  N ND1 . HIS A 1 98  ? -0.040  -8.547  55.692 1.00 18.90 ? 98   HIS A ND1 1 
ATOM   720  C CD2 . HIS A 1 98  ? 0.947   -7.031  56.916 1.00 20.09 ? 98   HIS A CD2 1 
ATOM   721  C CE1 . HIS A 1 98  ? 1.263   -8.656  55.476 1.00 19.73 ? 98   HIS A CE1 1 
ATOM   722  N NE2 . HIS A 1 98  ? 1.883   -7.738  56.195 1.00 21.12 ? 98   HIS A NE2 1 
ATOM   723  N N   . PHE A 1 99  ? -1.428  -10.444 58.195 1.00 18.11 ? 99   PHE A N   1 
ATOM   724  C CA  . PHE A 1 99  ? -0.524  -11.220 59.052 1.00 18.90 ? 99   PHE A CA  1 
ATOM   725  C C   . PHE A 1 99  ? 0.560   -11.934 58.259 1.00 19.19 ? 99   PHE A C   1 
ATOM   726  O O   . PHE A 1 99  ? 0.363   -12.327 57.113 1.00 18.59 ? 99   PHE A O   1 
ATOM   727  C CB  . PHE A 1 99  ? -1.263  -12.164 60.022 1.00 19.12 ? 99   PHE A CB  1 
ATOM   728  C CG  . PHE A 1 99  ? -1.801  -13.429 59.390 1.00 20.45 ? 99   PHE A CG  1 
ATOM   729  C CD1 . PHE A 1 99  ? -1.036  -14.600 59.372 1.00 18.93 ? 99   PHE A CD1 1 
ATOM   730  C CD2 . PHE A 1 99  ? -3.092  -13.461 58.880 1.00 20.54 ? 99   PHE A CD2 1 
ATOM   731  C CE1 . PHE A 1 99  ? -1.530  -15.757 58.812 1.00 20.91 ? 99   PHE A CE1 1 
ATOM   732  C CE2 . PHE A 1 99  ? -3.611  -14.633 58.325 1.00 20.56 ? 99   PHE A CE2 1 
ATOM   733  C CZ  . PHE A 1 99  ? -2.844  -15.773 58.296 1.00 21.20 ? 99   PHE A CZ  1 
ATOM   734  N N   . LYS A 1 100 ? 1.730   -12.052 58.863 1.00 20.25 ? 100  LYS A N   1 
ATOM   735  C CA  . LYS A 1 100 ? 2.826   -12.758 58.218 1.00 20.87 ? 100  LYS A CA  1 
ATOM   736  C C   . LYS A 1 100 ? 3.555   -13.660 59.200 1.00 20.62 ? 100  LYS A C   1 
ATOM   737  O O   . LYS A 1 100 ? 3.691   -13.341 60.389 1.00 19.87 ? 100  LYS A O   1 
ATOM   738  C CB  . LYS A 1 100 ? 3.755   -11.806 57.446 1.00 21.18 ? 100  LYS A CB  1 
ATOM   739  C CG  . LYS A 1 100 ? 4.689   -10.931 58.224 1.00 23.79 ? 100  LYS A CG  1 
ATOM   740  C CD  . LYS A 1 100 ? 5.497   -10.046 57.250 1.00 23.52 ? 100  LYS A CD  1 
ATOM   741  C CE  . LYS A 1 100 ? 6.059   -8.787  57.937 1.00 29.85 ? 100  LYS A CE  1 
ATOM   742  N NZ  . LYS A 1 100 ? 7.340   -8.971  58.700 1.00 31.96 ? 100  LYS A NZ  1 
ATOM   743  N N   . LEU A 1 101 ? 3.960   -14.819 58.681 1.00 20.07 ? 101  LEU A N   1 
ATOM   744  C CA  . LEU A 1 101 ? 4.735   -15.814 59.402 1.00 20.35 ? 101  LEU A CA  1 
ATOM   745  C C   . LEU A 1 101 ? 6.129   -15.804 58.769 1.00 20.74 ? 101  LEU A C   1 
ATOM   746  O O   . LEU A 1 101 ? 6.273   -15.966 57.566 1.00 19.85 ? 101  LEU A O   1 
ATOM   747  C CB  . LEU A 1 101 ? 4.064   -17.189 59.299 1.00 19.29 ? 101  LEU A CB  1 
ATOM   748  C CG  . LEU A 1 101 ? 2.678   -17.174 59.988 1.00 18.53 ? 101  LEU A CG  1 
ATOM   749  C CD1 . LEU A 1 101 ? 1.811   -18.274 59.472 1.00 19.09 ? 101  LEU A CD1 1 
ATOM   750  C CD2 . LEU A 1 101 ? 2.801   -17.256 61.527 1.00 15.15 ? 101  LEU A CD2 1 
ATOM   751  N N   . THR A 1 102 ? 7.143   -15.534 59.567 1.00 20.92 ? 102  THR A N   1 
ATOM   752  C CA  . THR A 1 102 ? 8.476   -15.402 59.009 1.00 22.18 ? 102  THR A CA  1 
ATOM   753  C C   . THR A 1 102 ? 9.378   -16.253 59.887 1.00 22.25 ? 102  THR A C   1 
ATOM   754  O O   . THR A 1 102 ? 8.955   -16.740 60.922 1.00 21.97 ? 102  THR A O   1 
ATOM   755  C CB  . THR A 1 102 ? 8.931   -13.912 58.956 1.00 22.04 ? 102  THR A CB  1 
ATOM   756  O OG1 . THR A 1 102 ? 8.949   -13.372 60.274 1.00 22.07 ? 102  THR A OG1 1 
ATOM   757  C CG2 . THR A 1 102 ? 7.956   -13.056 58.140 1.00 23.48 ? 102  THR A CG2 1 
ATOM   758  N N   . ASP A 1 103 ? 10.601  -16.475 59.449 1.00 23.82 ? 103  ASP A N   1 
ATOM   759  C CA  . ASP A 1 103 ? 11.575  -17.194 60.252 1.00 24.74 ? 103  ASP A CA  1 
ATOM   760  C C   . ASP A 1 103 ? 12.127  -16.181 61.241 1.00 25.48 ? 103  ASP A C   1 
ATOM   761  O O   . ASP A 1 103 ? 12.598  -15.127 60.855 1.00 25.20 ? 103  ASP A O   1 
ATOM   762  C CB  . ASP A 1 103 ? 12.677  -17.748 59.343 1.00 24.74 ? 103  ASP A CB  1 
ATOM   763  C CG  . ASP A 1 103 ? 13.703  -18.593 60.091 1.00 26.28 ? 103  ASP A CG  1 
ATOM   764  O OD1 . ASP A 1 103 ? 13.725  -18.566 61.339 1.00 25.59 ? 103  ASP A OD1 1 
ATOM   765  O OD2 . ASP A 1 103 ? 14.504  -19.271 59.411 1.00 27.92 ? 103  ASP A OD2 1 
ATOM   766  N N   . GLN A 1 104 ? 12.049  -16.489 62.527 1.00 27.64 ? 104  GLN A N   1 
ATOM   767  C CA  . GLN A 1 104 ? 12.474  -15.533 63.548 1.00 30.20 ? 104  GLN A CA  1 
ATOM   768  C C   . GLN A 1 104 ? 13.944  -15.124 63.480 1.00 31.72 ? 104  GLN A C   1 
ATOM   769  O O   . GLN A 1 104 ? 14.299  -13.979 63.812 1.00 32.31 ? 104  GLN A O   1 
ATOM   770  C CB  . GLN A 1 104 ? 12.146  -16.063 64.936 1.00 30.23 ? 104  GLN A CB  1 
ATOM   771  C CG  . GLN A 1 104 ? 11.807  -14.964 65.877 1.00 32.38 ? 104  GLN A CG  1 
ATOM   772  C CD  . GLN A 1 104 ? 11.535  -15.447 67.260 1.00 35.94 ? 104  GLN A CD  1 
ATOM   773  O OE1 . GLN A 1 104 ? 11.567  -16.657 67.547 1.00 35.96 ? 104  GLN A OE1 1 
ATOM   774  N NE2 . GLN A 1 104 ? 11.255  -14.498 68.153 1.00 38.36 ? 104  GLN A NE2 1 
ATOM   775  N N   . THR A 1 105 ? 14.794  -16.047 63.031 1.00 33.42 ? 105  THR A N   1 
ATOM   776  C CA  . THR A 1 105 ? 16.246  -15.835 63.081 1.00 34.76 ? 105  THR A CA  1 
ATOM   777  C C   . THR A 1 105 ? 16.927  -15.786 61.707 1.00 35.14 ? 105  THR A C   1 
ATOM   778  O O   . THR A 1 105 ? 18.156  -15.818 61.626 1.00 36.24 ? 105  THR A O   1 
ATOM   779  C CB  . THR A 1 105 ? 16.937  -16.910 63.943 1.00 34.85 ? 105  THR A CB  1 
ATOM   780  O OG1 . THR A 1 105 ? 16.670  -18.203 63.394 1.00 36.15 ? 105  THR A OG1 1 
ATOM   781  C CG2 . THR A 1 105 ? 16.455  -16.865 65.393 1.00 35.96 ? 105  THR A CG2 1 
ATOM   782  N N   . ASN A 1 106 ? 16.137  -15.716 60.634 1.00 34.62 ? 106  ASN A N   1 
ATOM   783  C CA  . ASN A 1 106 ? 16.665  -15.654 59.270 1.00 34.11 ? 106  ASN A CA  1 
ATOM   784  C C   . ASN A 1 106 ? 15.729  -14.857 58.357 1.00 33.15 ? 106  ASN A C   1 
ATOM   785  O O   . ASN A 1 106 ? 14.519  -15.081 58.354 1.00 32.46 ? 106  ASN A O   1 
ATOM   786  C CB  . ASN A 1 106 ? 16.858  -17.067 58.680 1.00 34.10 ? 106  ASN A CB  1 
ATOM   787  C CG  . ASN A 1 106 ? 17.912  -17.898 59.420 1.00 36.32 ? 106  ASN A CG  1 
ATOM   788  O OD1 . ASN A 1 106 ? 17.614  -18.992 59.922 1.00 34.77 ? 106  ASN A OD1 1 
ATOM   789  N ND2 . ASN A 1 106 ? 19.153  -17.390 59.480 1.00 37.06 ? 106  ASN A ND2 1 
ATOM   790  N N   . ASN A 1 107 ? 16.302  -13.933 57.595 1.00 32.57 ? 107  ASN A N   1 
ATOM   791  C CA  . ASN A 1 107 ? 15.594  -13.180 56.558 1.00 31.72 ? 107  ASN A CA  1 
ATOM   792  C C   . ASN A 1 107 ? 15.195  -14.115 55.405 1.00 29.96 ? 107  ASN A C   1 
ATOM   793  O O   . ASN A 1 107 ? 15.992  -14.909 54.947 1.00 30.55 ? 107  ASN A O   1 
ATOM   794  C CB  . ASN A 1 107 ? 16.488  -12.049 56.025 1.00 32.58 ? 107  ASN A CB  1 
ATOM   795  C CG  . ASN A 1 107 ? 16.481  -10.777 56.903 1.00 35.56 ? 107  ASN A CG  1 
ATOM   796  O OD1 . ASN A 1 107 ? 17.396  -9.948  56.796 1.00 40.56 ? 107  ASN A OD1 1 
ATOM   797  N ND2 . ASN A 1 107 ? 15.448  -10.595 57.724 1.00 38.34 ? 107  ASN A ND2 1 
ATOM   798  N N   . ARG A 1 108 ? 13.949  -14.070 54.954 1.00 27.43 ? 108  ARG A N   1 
ATOM   799  C CA  . ARG A 1 108 ? 13.552  -14.925 53.827 1.00 24.20 ? 108  ARG A CA  1 
ATOM   800  C C   . ARG A 1 108 ? 13.079  -14.064 52.667 1.00 23.57 ? 108  ARG A C   1 
ATOM   801  O O   . ARG A 1 108 ? 12.845  -12.868 52.850 1.00 23.05 ? 108  ARG A O   1 
ATOM   802  C CB  . ARG A 1 108 ? 12.491  -15.948 54.251 1.00 24.40 ? 108  ARG A CB  1 
ATOM   803  C CG  . ARG A 1 108 ? 12.933  -16.880 55.383 1.00 20.79 ? 108  ARG A CG  1 
ATOM   804  C CD  . ARG A 1 108 ? 11.839  -17.886 55.752 1.00 22.24 ? 108  ARG A CD  1 
ATOM   805  N NE  . ARG A 1 108 ? 11.269  -18.508 54.567 1.00 17.58 ? 108  ARG A NE  1 
ATOM   806  C CZ  . ARG A 1 108 ? 11.702  -19.643 54.036 1.00 20.28 ? 108  ARG A CZ  1 
ATOM   807  N NH1 . ARG A 1 108 ? 12.696  -20.333 54.604 1.00 20.38 ? 108  ARG A NH1 1 
ATOM   808  N NH2 . ARG A 1 108 ? 11.139  -20.101 52.942 1.00 16.99 ? 108  ARG A NH2 1 
ATOM   809  N N   . PHE A 1 109 ? 12.977  -14.646 51.469 1.00 22.13 ? 109  PHE A N   1 
ATOM   810  C CA  . PHE A 1 109 ? 12.546  -13.886 50.325 1.00 20.83 ? 109  PHE A CA  1 
ATOM   811  C C   . PHE A 1 109 ? 11.114  -13.376 50.552 1.00 20.83 ? 109  PHE A C   1 
ATOM   812  O O   . PHE A 1 109 ? 10.247  -14.135 50.990 1.00 19.72 ? 109  PHE A O   1 
ATOM   813  C CB  . PHE A 1 109 ? 12.584  -14.701 49.027 1.00 20.32 ? 109  PHE A CB  1 
ATOM   814  C CG  . PHE A 1 109 ? 11.966  -13.962 47.861 1.00 19.32 ? 109  PHE A CG  1 
ATOM   815  C CD1 . PHE A 1 109 ? 12.697  -13.012 47.166 1.00 18.34 ? 109  PHE A CD1 1 
ATOM   816  C CD2 . PHE A 1 109 ? 10.638  -14.172 47.509 1.00 17.54 ? 109  PHE A CD2 1 
ATOM   817  C CE1 . PHE A 1 109 ? 12.137  -12.296 46.121 1.00 19.44 ? 109  PHE A CE1 1 
ATOM   818  C CE2 . PHE A 1 109 ? 10.068  -13.468 46.468 1.00 17.60 ? 109  PHE A CE2 1 
ATOM   819  C CZ  . PHE A 1 109 ? 10.808  -12.534 45.764 1.00 19.11 ? 109  PHE A CZ  1 
ATOM   820  N N   . GLU A 1 110 ? 10.897  -12.094 50.278 1.00 21.18 ? 110  GLU A N   1 
ATOM   821  C CA  . GLU A 1 110 ? 9.560   -11.484 50.352 1.00 23.29 ? 110  GLU A CA  1 
ATOM   822  C C   . GLU A 1 110 ? 9.347   -10.716 49.062 1.00 22.63 ? 110  GLU A C   1 
ATOM   823  O O   . GLU A 1 110 ? 10.263  -10.031 48.572 1.00 21.61 ? 110  GLU A O   1 
ATOM   824  C CB  . GLU A 1 110 ? 9.454   -10.539 51.554 1.00 23.37 ? 110  GLU A CB  1 
ATOM   825  C CG  . GLU A 1 110 ? 9.634   -11.205 52.907 1.00 26.10 ? 110  GLU A CG  1 
ATOM   826  C CD  . GLU A 1 110 ? 9.529   -10.213 54.055 1.00 28.00 ? 110  GLU A CD  1 
ATOM   827  O OE1 . GLU A 1 110 ? 8.425   -9.643  54.262 1.00 33.30 ? 110  GLU A OE1 1 
ATOM   828  O OE2 . GLU A 1 110 ? 10.551  -10.009 54.753 1.00 33.61 ? 110  GLU A OE2 1 
ATOM   829  N N   . VAL A 1 111 ? 8.136   -10.821 48.506 1.00 22.30 ? 111  VAL A N   1 
ATOM   830  C CA  . VAL A 1 111 ? 7.847   -10.222 47.212 1.00 21.67 ? 111  VAL A CA  1 
ATOM   831  C C   . VAL A 1 111 ? 8.149   -8.738  47.263 1.00 23.41 ? 111  VAL A C   1 
ATOM   832  O O   . VAL A 1 111 ? 7.605   -8.047  48.104 1.00 23.64 ? 111  VAL A O   1 
ATOM   833  C CB  . VAL A 1 111 ? 6.369   -10.412 46.825 1.00 21.52 ? 111  VAL A CB  1 
ATOM   834  C CG1 . VAL A 1 111 ? 6.091   -9.782  45.496 1.00 17.00 ? 111  VAL A CG1 1 
ATOM   835  C CG2 . VAL A 1 111 ? 6.021   -11.895 46.838 1.00 19.02 ? 111  VAL A CG2 1 
ATOM   836  N N   . PRO A 1 112 ? 9.019   -8.249  46.360 1.00 24.68 ? 112  PRO A N   1 
ATOM   837  C CA  . PRO A 1 112 ? 9.346   -6.832  46.276 1.00 25.56 ? 112  PRO A CA  1 
ATOM   838  C C   . PRO A 1 112 ? 8.297   -6.064  45.445 1.00 26.65 ? 112  PRO A C   1 
ATOM   839  O O   . PRO A 1 112 ? 8.639   -5.467  44.438 1.00 26.45 ? 112  PRO A O   1 
ATOM   840  C CB  . PRO A 1 112 ? 10.722  -6.831  45.600 1.00 25.57 ? 112  PRO A CB  1 
ATOM   841  C CG  . PRO A 1 112 ? 10.819  -8.103  44.868 1.00 25.17 ? 112  PRO A CG  1 
ATOM   842  C CD  . PRO A 1 112 ? 9.743   -9.043  45.346 1.00 25.02 ? 112  PRO A CD  1 
ATOM   843  N N   . HIS A 1 113 ? 7.031   -6.102  45.880 1.00 26.88 ? 113  HIS A N   1 
ATOM   844  C CA  . HIS A 1 113 ? 5.911   -5.512  45.129 1.00 28.07 ? 113  HIS A CA  1 
ATOM   845  C C   . HIS A 1 113 ? 6.077   -4.002  44.954 1.00 29.08 ? 113  HIS A C   1 
ATOM   846  O O   . HIS A 1 113 ? 6.473   -3.302  45.900 1.00 29.65 ? 113  HIS A O   1 
ATOM   847  C CB  . HIS A 1 113 ? 4.589   -5.796  45.842 1.00 27.28 ? 113  HIS A CB  1 
ATOM   848  C CG  . HIS A 1 113 ? 3.398   -5.850  44.923 1.00 28.31 ? 113  HIS A CG  1 
ATOM   849  N ND1 . HIS A 1 113 ? 2.595   -4.756  44.681 1.00 28.07 ? 113  HIS A ND1 1 
ATOM   850  C CD2 . HIS A 1 113 ? 2.874   -6.868  44.199 1.00 25.97 ? 113  HIS A CD2 1 
ATOM   851  C CE1 . HIS A 1 113 ? 1.631   -5.095  43.840 1.00 28.51 ? 113  HIS A CE1 1 
ATOM   852  N NE2 . HIS A 1 113 ? 1.773   -6.374  43.538 1.00 27.18 ? 113  HIS A NE2 1 
ATOM   853  N N   . GLU A 1 114 ? 5.765   -3.509  43.758 1.00 30.99 ? 114  GLU A N   1 
ATOM   854  C CA  . GLU A 1 114 ? 5.945   -2.083  43.408 1.00 32.28 ? 114  GLU A CA  1 
ATOM   855  C C   . GLU A 1 114 ? 4.941   -1.182  44.137 1.00 32.87 ? 114  GLU A C   1 
ATOM   856  O O   . GLU A 1 114 ? 5.296   -0.091  44.601 1.00 33.44 ? 114  GLU A O   1 
ATOM   857  C CB  . GLU A 1 114 ? 5.866   -1.875  41.880 1.00 32.37 ? 114  GLU A CB  1 
ATOM   858  C CG  . GLU A 1 114 ? 6.118   -0.440  41.359 1.00 32.76 ? 114  GLU A CG  1 
ATOM   859  C CD  . GLU A 1 114 ? 4.855   0.434   41.173 1.00 35.91 ? 114  GLU A CD  1 
ATOM   860  O OE1 . GLU A 1 114 ? 3.702   0.038   41.511 1.00 34.46 ? 114  GLU A OE1 1 
ATOM   861  O OE2 . GLU A 1 114 ? 5.037   1.557   40.659 1.00 38.11 ? 114  GLU A OE2 1 
ATOM   862  N N   . HIS A 1 115 ? 3.694   -1.643  44.249 1.00 33.23 ? 115  HIS A N   1 
ATOM   863  C CA  . HIS A 1 115 ? 2.647   -0.832  44.874 1.00 33.42 ? 115  HIS A CA  1 
ATOM   864  C C   . HIS A 1 115 ? 2.603   -0.977  46.396 1.00 33.69 ? 115  HIS A C   1 
ATOM   865  O O   . HIS A 1 115 ? 2.675   0.027   47.119 1.00 33.89 ? 115  HIS A O   1 
ATOM   866  C CB  . HIS A 1 115 ? 1.276   -1.123  44.256 1.00 33.64 ? 115  HIS A CB  1 
ATOM   867  C CG  . HIS A 1 115 ? 0.223   -0.128  44.637 1.00 34.02 ? 115  HIS A CG  1 
ATOM   868  N ND1 . HIS A 1 115 ? 0.060   1.070   43.977 1.00 35.30 ? 115  HIS A ND1 1 
ATOM   869  C CD2 . HIS A 1 115 ? -0.712  -0.146  45.615 1.00 34.36 ? 115  HIS A CD2 1 
ATOM   870  C CE1 . HIS A 1 115 ? -0.934  1.747   44.527 1.00 35.19 ? 115  HIS A CE1 1 
ATOM   871  N NE2 . HIS A 1 115 ? -1.421  1.031   45.524 1.00 35.15 ? 115  HIS A NE2 1 
ATOM   872  N N   . VAL A 1 116 ? 2.508   -2.216  46.879 1.00 33.90 ? 116  VAL A N   1 
ATOM   873  C CA  . VAL A 1 116 ? 2.329   -2.480  48.303 1.00 34.60 ? 116  VAL A CA  1 
ATOM   874  C C   . VAL A 1 116 ? 3.508   -1.974  49.124 1.00 35.47 ? 116  VAL A C   1 
ATOM   875  O O   . VAL A 1 116 ? 4.667   -2.253  48.819 1.00 35.45 ? 116  VAL A O   1 
ATOM   876  C CB  . VAL A 1 116 ? 2.061   -3.975  48.591 1.00 34.53 ? 116  VAL A CB  1 
ATOM   877  C CG1 . VAL A 1 116 ? 2.090   -4.269  50.090 1.00 34.49 ? 116  VAL A CG1 1 
ATOM   878  C CG2 . VAL A 1 116 ? 0.728   -4.372  48.019 1.00 33.53 ? 116  VAL A CG2 1 
ATOM   879  N N   . GLN A 1 117 ? 3.190   -1.195  50.154 1.00 36.61 ? 117  GLN A N   1 
ATOM   880  C CA  . GLN A 1 117 ? 4.203   -0.659  51.054 1.00 37.78 ? 117  GLN A CA  1 
ATOM   881  C C   . GLN A 1 117 ? 4.126   -1.355  52.394 1.00 37.71 ? 117  GLN A C   1 
ATOM   882  O O   . GLN A 1 117 ? 3.046   -1.748  52.852 1.00 37.57 ? 117  GLN A O   1 
ATOM   883  C CB  . GLN A 1 117 ? 3.998   0.835   51.282 1.00 37.48 ? 117  GLN A CB  1 
ATOM   884  C CG  . GLN A 1 117 ? 4.361   1.729   50.137 1.00 40.57 ? 117  GLN A CG  1 
ATOM   885  C CD  . GLN A 1 117 ? 4.433   3.175   50.584 1.00 44.09 ? 117  GLN A CD  1 
ATOM   886  O OE1 . GLN A 1 117 ? 3.405   3.803   50.873 1.00 47.49 ? 117  GLN A OE1 1 
ATOM   887  N NE2 . GLN A 1 117 ? 5.652   3.705   50.681 1.00 44.39 ? 117  GLN A NE2 1 
ATOM   888  N N   . SER A 1 118 ? 5.279   -1.474  53.036 1.00 38.34 ? 118  SER A N   1 
ATOM   889  C CA  . SER A 1 118 ? 5.330   -1.892  54.435 1.00 38.79 ? 118  SER A CA  1 
ATOM   890  C C   . SER A 1 118 ? 4.447   -0.977  55.288 1.00 38.15 ? 118  SER A C   1 
ATOM   891  O O   . SER A 1 118 ? 4.228   0.202   54.972 1.00 38.11 ? 118  SER A O   1 
ATOM   892  C CB  . SER A 1 118 ? 6.770   -1.859  54.944 1.00 39.05 ? 118  SER A CB  1 
ATOM   893  O OG  . SER A 1 118 ? 7.382   -0.634  54.563 1.00 41.16 ? 118  SER A OG  1 
ATOM   894  N N   . PHE A 1 119 ? 3.931   -1.534  56.370 1.00 37.66 ? 119  PHE A N   1 
ATOM   895  C CA  . PHE A 1 119 ? 3.018   -0.798  57.205 1.00 37.22 ? 119  PHE A CA  1 
ATOM   896  C C   . PHE A 1 119 ? 3.750   -0.163  58.370 1.00 37.52 ? 119  PHE A C   1 
ATOM   897  O O   . PHE A 1 119 ? 4.411   -0.850  59.147 1.00 37.71 ? 119  PHE A O   1 
ATOM   898  C CB  . PHE A 1 119 ? 1.927   -1.723  57.714 1.00 36.47 ? 119  PHE A CB  1 
ATOM   899  C CG  . PHE A 1 119 ? 0.874   -1.037  58.501 1.00 33.73 ? 119  PHE A CG  1 
ATOM   900  C CD1 . PHE A 1 119 ? -0.048  -0.202  57.876 1.00 33.31 ? 119  PHE A CD1 1 
ATOM   901  C CD2 . PHE A 1 119 ? 0.770   -1.250  59.862 1.00 33.33 ? 119  PHE A CD2 1 
ATOM   902  C CE1 . PHE A 1 119 ? -1.043  0.420   58.603 1.00 29.64 ? 119  PHE A CE1 1 
ATOM   903  C CE2 . PHE A 1 119 ? -0.227  -0.624  60.597 1.00 33.14 ? 119  PHE A CE2 1 
ATOM   904  C CZ  . PHE A 1 119 ? -1.135  0.213   59.955 1.00 32.48 ? 119  PHE A CZ  1 
ATOM   905  N N   . SER A 1 120 ? 3.631   1.157   58.457 1.00 38.03 ? 120  SER A N   1 
ATOM   906  C CA  . SER A 1 120 ? 4.045   1.922   59.627 1.00 38.60 ? 120  SER A CA  1 
ATOM   907  C C   . SER A 1 120 ? 2.860   2.792   60.001 1.00 38.36 ? 120  SER A C   1 
ATOM   908  O O   . SER A 1 120 ? 2.779   3.963   59.644 1.00 39.60 ? 120  SER A O   1 
ATOM   909  C CB  . SER A 1 120 ? 5.289   2.778   59.345 1.00 38.72 ? 120  SER A CB  1 
ATOM   910  O OG  . SER A 1 120 ? 5.024   3.774   58.364 1.00 39.80 ? 120  SER A OG  1 
ATOM   911  N N   . GLY A 1 121 ? 1.902   2.186   60.669 1.00 37.79 ? 121  GLY A N   1 
ATOM   912  C CA  . GLY A 1 121 ? 0.807   2.935   61.239 1.00 36.71 ? 121  GLY A CA  1 
ATOM   913  C C   . GLY A 1 121 ? 0.529   2.384   62.617 1.00 35.82 ? 121  GLY A C   1 
ATOM   914  O O   . GLY A 1 121 ? 1.236   1.482   63.103 1.00 35.38 ? 121  GLY A O   1 
ATOM   915  N N   . ASN A 1 122 ? -0.478  2.971   63.255 1.00 34.88 ? 122  ASN A N   1 
ATOM   916  C CA  . ASN A 1 122 ? -1.099  2.407   64.427 1.00 34.08 ? 122  ASN A CA  1 
ATOM   917  C C   . ASN A 1 122 ? -2.267  1.522   64.005 1.00 31.92 ? 122  ASN A C   1 
ATOM   918  O O   . ASN A 1 122 ? -2.890  1.786   62.989 1.00 32.15 ? 122  ASN A O   1 
ATOM   919  C CB  . ASN A 1 122 ? -1.609  3.533   65.343 1.00 35.17 ? 122  ASN A CB  1 
ATOM   920  C CG  . ASN A 1 122 ? -0.483  4.256   66.060 1.00 37.35 ? 122  ASN A CG  1 
ATOM   921  O OD1 . ASN A 1 122 ? 0.684   3.881   65.942 1.00 39.92 ? 122  ASN A OD1 1 
ATOM   922  N ND2 . ASN A 1 122 ? -0.831  5.293   66.820 1.00 40.91 ? 122  ASN A ND2 1 
ATOM   923  N N   . ALA A 1 123 ? -2.562  0.496   64.793 1.00 29.72 ? 123  ALA A N   1 
ATOM   924  C CA  . ALA A 1 123 ? -3.755  -0.313  64.611 1.00 28.11 ? 123  ALA A CA  1 
ATOM   925  C C   . ALA A 1 123 ? -4.952  0.590   64.319 1.00 27.77 ? 123  ALA A C   1 
ATOM   926  O O   . ALA A 1 123 ? -5.148  1.615   64.981 1.00 26.65 ? 123  ALA A O   1 
ATOM   927  C CB  . ALA A 1 123 ? -4.010  -1.132  65.848 1.00 28.39 ? 123  ALA A CB  1 
ATOM   928  N N   . ALA A 1 124 ? -5.729  0.217   63.306 1.00 26.50 ? 124  ALA A N   1 
ATOM   929  C CA  . ALA A 1 124 ? -6.869  0.999   62.897 1.00 26.13 ? 124  ALA A CA  1 
ATOM   930  C C   . ALA A 1 124 ? -7.940  0.895   63.956 1.00 25.91 ? 124  ALA A C   1 
ATOM   931  O O   . ALA A 1 124 ? -8.000  -0.085  64.696 1.00 25.96 ? 124  ALA A O   1 
ATOM   932  C CB  . ALA A 1 124 ? -7.400  0.496   61.599 1.00 25.65 ? 124  ALA A CB  1 
ATOM   933  N N   . ALA A 1 125 ? -8.786  1.909   64.009 1.00 26.24 ? 125  ALA A N   1 
ATOM   934  C CA  . ALA A 1 125 ? -9.923  1.919   64.905 1.00 26.53 ? 125  ALA A CA  1 
ATOM   935  C C   . ALA A 1 125 ? -11.130 1.325   64.203 1.00 26.89 ? 125  ALA A C   1 
ATOM   936  O O   . ALA A 1 125 ? -11.118 1.140   62.972 1.00 27.76 ? 125  ALA A O   1 
ATOM   937  C CB  . ALA A 1 125 ? -10.213 3.336   65.328 1.00 27.07 ? 125  ALA A CB  1 
ATOM   938  N N   . SER A 1 126 ? -12.177 1.047   64.982 1.00 26.89 ? 126  SER A N   1 
ATOM   939  C CA  . SER A 1 126 ? -13.485 0.606   64.471 1.00 26.51 ? 126  SER A CA  1 
ATOM   940  C C   . SER A 1 126 ? -13.371 -0.560  63.501 1.00 25.96 ? 126  SER A C   1 
ATOM   941  O O   . SER A 1 126 ? -13.842 -0.490  62.357 1.00 27.35 ? 126  SER A O   1 
ATOM   942  C CB  . SER A 1 126 ? -14.230 1.765   63.811 1.00 27.00 ? 126  SER A CB  1 
ATOM   943  O OG  . SER A 1 126 ? -14.098 2.941   64.588 1.00 29.65 ? 126  SER A OG  1 
ATOM   944  N N   . LEU A 1 127 ? -12.760 -1.640  63.962 1.00 24.62 ? 127  LEU A N   1 
ATOM   945  C CA  . LEU A 1 127 ? -12.514 -2.820  63.129 1.00 22.79 ? 127  LEU A CA  1 
ATOM   946  C C   . LEU A 1 127 ? -13.803 -3.592  62.881 1.00 22.40 ? 127  LEU A C   1 
ATOM   947  O O   . LEU A 1 127 ? -14.608 -3.787  63.805 1.00 21.98 ? 127  LEU A O   1 
ATOM   948  C CB  . LEU A 1 127 ? -11.503 -3.740  63.820 1.00 22.33 ? 127  LEU A CB  1 
ATOM   949  C CG  . LEU A 1 127 ? -10.106 -3.187  64.146 1.00 20.85 ? 127  LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 127 ? -9.273  -4.253  64.837 1.00 20.88 ? 127  LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 127 ? -9.431  -2.713  62.883 1.00 17.24 ? 127  LEU A CD2 1 
ATOM   952  N N   . THR A 1 128 ? -13.987 -4.049  61.640 1.00 21.18 ? 128  THR A N   1 
ATOM   953  C CA  . THR A 1 128 ? -15.138 -4.868  61.274 1.00 20.27 ? 128  THR A CA  1 
ATOM   954  C C   . THR A 1 128 ? -14.834 -6.332  61.536 1.00 19.46 ? 128  THR A C   1 
ATOM   955  O O   . THR A 1 128 ? -15.688 -7.180  61.342 1.00 17.84 ? 128  THR A O   1 
ATOM   956  C CB  . THR A 1 128 ? -15.503 -4.695  59.769 1.00 20.61 ? 128  THR A CB  1 
ATOM   957  O OG1 . THR A 1 128 ? -14.461 -5.231  58.958 1.00 22.09 ? 128  THR A OG1 1 
ATOM   958  C CG2 . THR A 1 128 ? -15.691 -3.233  59.420 1.00 21.22 ? 128  THR A CG2 1 
ATOM   959  N N   . TYR A 1 129 ? -13.586 -6.624  61.934 1.00 18.03 ? 129  TYR A N   1 
ATOM   960  C CA  . TYR A 1 129 ? -13.144 -7.990  62.216 1.00 17.58 ? 129  TYR A CA  1 
ATOM   961  C C   . TYR A 1 129 ? -12.496 -8.121  63.626 1.00 17.15 ? 129  TYR A C   1 
ATOM   962  O O   . TYR A 1 129 ? -12.074 -7.135  64.222 1.00 15.02 ? 129  TYR A O   1 
ATOM   963  C CB  . TYR A 1 129 ? -12.161 -8.472  61.141 1.00 17.10 ? 129  TYR A CB  1 
ATOM   964  C CG  . TYR A 1 129 ? -10.931 -7.618  61.063 1.00 14.58 ? 129  TYR A CG  1 
ATOM   965  C CD1 . TYR A 1 129 ? -9.791  -7.911  61.813 1.00 16.19 ? 129  TYR A CD1 1 
ATOM   966  C CD2 . TYR A 1 129 ? -10.897 -6.528  60.227 1.00 13.74 ? 129  TYR A CD2 1 
ATOM   967  C CE1 . TYR A 1 129 ? -8.656  -7.088  61.727 1.00 13.83 ? 129  TYR A CE1 1 
ATOM   968  C CE2 . TYR A 1 129 ? -9.815  -5.714  60.160 1.00 13.93 ? 129  TYR A CE2 1 
ATOM   969  C CZ  . TYR A 1 129 ? -8.678  -6.018  60.887 1.00 12.93 ? 129  TYR A CZ  1 
ATOM   970  O OH  . TYR A 1 129 ? -7.626  -5.151  60.792 1.00 14.73 ? 129  TYR A OH  1 
ATOM   971  N N   . GLN A 1 130 ? -12.455 -9.347  64.132 1.00 17.48 ? 130  GLN A N   1 
ATOM   972  C CA  . GLN A 1 130 ? -11.718 -9.687  65.350 1.00 19.48 ? 130  GLN A CA  1 
ATOM   973  C C   . GLN A 1 130 ? -10.720 -10.841 65.035 1.00 18.21 ? 130  GLN A C   1 
ATOM   974  O O   . GLN A 1 130 ? -10.991 -11.689 64.196 1.00 18.56 ? 130  GLN A O   1 
ATOM   975  C CB  . GLN A 1 130 ? -12.703 -10.073 66.449 1.00 19.19 ? 130  GLN A CB  1 
ATOM   976  C CG  . GLN A 1 130 ? -12.093 -10.321 67.833 1.00 22.23 ? 130  GLN A CG  1 
ATOM   977  C CD  . GLN A 1 130 ? -13.152 -10.636 68.893 1.00 24.58 ? 130  GLN A CD  1 
ATOM   978  O OE1 . GLN A 1 130 ? -14.364 -10.671 68.607 1.00 30.83 ? 130  GLN A OE1 1 
ATOM   979  N NE2 . GLN A 1 130 ? -12.702 -10.848 70.126 1.00 28.54 ? 130  GLN A NE2 1 
ATOM   980  N N   . VAL A 1 131 ? -9.574  -10.837 65.700 1.00 17.79 ? 131  VAL A N   1 
ATOM   981  C CA  . VAL A 1 131 ? -8.528  -11.844 65.526 1.00 17.06 ? 131  VAL A CA  1 
ATOM   982  C C   . VAL A 1 131 ? -8.340  -12.619 66.828 1.00 17.78 ? 131  VAL A C   1 
ATOM   983  O O   . VAL A 1 131 ? -8.183  -12.040 67.902 1.00 17.48 ? 131  VAL A O   1 
ATOM   984  C CB  . VAL A 1 131 ? -7.214  -11.190 65.115 1.00 16.89 ? 131  VAL A CB  1 
ATOM   985  C CG1 . VAL A 1 131 ? -6.095  -12.258 64.841 1.00 15.32 ? 131  VAL A CG1 1 
ATOM   986  C CG2 . VAL A 1 131 ? -7.443  -10.287 63.906 1.00 15.05 ? 131  VAL A CG2 1 
ATOM   987  N N   . GLU A 1 132 ? -8.394  -13.937 66.728 1.00 17.89 ? 132  GLU A N   1 
ATOM   988  C CA  . GLU A 1 132 ? -8.319  -14.816 67.880 1.00 19.24 ? 132  GLU A CA  1 
ATOM   989  C C   . GLU A 1 132 ? -7.112  -15.720 67.622 1.00 18.76 ? 132  GLU A C   1 
ATOM   990  O O   . GLU A 1 132 ? -7.028  -16.320 66.560 1.00 18.31 ? 132  GLU A O   1 
ATOM   991  C CB  . GLU A 1 132 ? -9.591  -15.682 67.953 1.00 19.93 ? 132  GLU A CB  1 
ATOM   992  C CG  . GLU A 1 132 ? -10.919 -14.887 68.211 1.00 25.52 ? 132  GLU A CG  1 
ATOM   993  C CD  . GLU A 1 132 ? -11.641 -14.299 66.979 1.00 31.38 ? 132  GLU A CD  1 
ATOM   994  O OE1 . GLU A 1 132 ? -11.343 -14.625 65.807 1.00 32.21 ? 132  GLU A OE1 1 
ATOM   995  O OE2 . GLU A 1 132 ? -12.577 -13.503 67.210 1.00 35.53 ? 132  GLU A OE2 1 
ATOM   996  N N   . ILE A 1 133 ? -6.208  -15.819 68.580 1.00 18.03 ? 133  ILE A N   1 
ATOM   997  C CA  . ILE A 1 133 ? -5.032  -16.694 68.479 1.00 18.48 ? 133  ILE A CA  1 
ATOM   998  C C   . ILE A 1 133 ? -5.105  -17.783 69.513 1.00 18.93 ? 133  ILE A C   1 
ATOM   999  O O   . ILE A 1 133 ? -5.385  -17.509 70.658 1.00 18.76 ? 133  ILE A O   1 
ATOM   1000 C CB  . ILE A 1 133 ? -3.745  -15.890 68.703 1.00 18.02 ? 133  ILE A CB  1 
ATOM   1001 C CG1 . ILE A 1 133 ? -3.687  -14.727 67.722 1.00 19.08 ? 133  ILE A CG1 1 
ATOM   1002 C CG2 . ILE A 1 133 ? -2.447  -16.797 68.691 1.00 18.32 ? 133  ILE A CG2 1 
ATOM   1003 C CD1 . ILE A 1 133 ? -3.714  -15.126 66.260 1.00 20.55 ? 133  ILE A CD1 1 
ATOM   1004 N N   . SER A 1 134 ? -4.872  -19.023 69.096 1.00 20.62 ? 134  SER A N   1 
ATOM   1005 C CA  . SER A 1 134 ? -4.805  -20.148 70.002 1.00 22.44 ? 134  SER A CA  1 
ATOM   1006 C C   . SER A 1 134 ? -3.353  -20.556 70.114 1.00 24.03 ? 134  SER A C   1 
ATOM   1007 O O   . SER A 1 134 ? -2.591  -20.395 69.164 1.00 24.19 ? 134  SER A O   1 
ATOM   1008 C CB  . SER A 1 134 ? -5.670  -21.291 69.500 1.00 22.78 ? 134  SER A CB  1 
ATOM   1009 O OG  . SER A 1 134 ? -7.019  -20.860 69.489 1.00 25.15 ? 134  SER A OG  1 
ATOM   1010 N N   . ARG A 1 135 ? -2.971  -21.044 71.286 1.00 25.31 ? 135  ARG A N   1 
ATOM   1011 C CA  . ARG A 1 135 ? -1.571  -21.178 71.656 1.00 26.89 ? 135  ARG A CA  1 
ATOM   1012 C C   . ARG A 1 135 ? -1.106  -22.600 71.434 1.00 26.80 ? 135  ARG A C   1 
ATOM   1013 O O   . ARG A 1 135 ? 0.005   -22.827 70.982 1.00 26.40 ? 135  ARG A O   1 
ATOM   1014 C CB  . ARG A 1 135 ? -1.377  -20.886 73.167 1.00 28.59 ? 135  ARG A CB  1 
ATOM   1015 C CG  . ARG A 1 135 ? -1.031  -19.476 73.616 1.00 30.94 ? 135  ARG A CG  1 
ATOM   1016 C CD  . ARG A 1 135 ? -0.129  -19.583 74.874 1.00 35.52 ? 135  ARG A CD  1 
ATOM   1017 N NE  . ARG A 1 135 ? 0.189   -18.297 75.539 1.00 38.51 ? 135  ARG A NE  1 
ATOM   1018 C CZ  . ARG A 1 135 ? 0.281   -17.106 74.940 1.00 35.65 ? 135  ARG A CZ  1 
ATOM   1019 N NH1 . ARG A 1 135 ? 0.121   -16.974 73.634 1.00 38.51 ? 135  ARG A NH1 1 
ATOM   1020 N NH2 . ARG A 1 135 ? 0.570   -16.041 75.653 1.00 36.55 ? 135  ARG A NH2 1 
ATOM   1021 N N   . GLN A 1 136 ? -1.946  -23.560 71.818 1.00 27.54 ? 136  GLN A N   1 
ATOM   1022 C CA  . GLN A 1 136 ? -1.509  -24.955 71.941 1.00 27.93 ? 136  GLN A CA  1 
ATOM   1023 C C   . GLN A 1 136 ? -2.542  -25.927 71.351 1.00 27.61 ? 136  GLN A C   1 
ATOM   1024 O O   . GLN A 1 136 ? -3.419  -26.412 72.063 1.00 28.61 ? 136  GLN A O   1 
ATOM   1025 C CB  . GLN A 1 136 ? -1.163  -25.296 73.401 1.00 28.02 ? 136  GLN A CB  1 
ATOM   1026 C CG  . GLN A 1 136 ? -0.560  -24.137 74.261 1.00 30.42 ? 136  GLN A CG  1 
ATOM   1027 C CD  . GLN A 1 136 ? 0.938   -23.863 73.998 1.00 36.03 ? 136  GLN A CD  1 
ATOM   1028 O OE1 . GLN A 1 136 ? 1.738   -24.793 73.852 1.00 37.15 ? 136  GLN A OE1 1 
ATOM   1029 N NE2 . GLN A 1 136 ? 1.319   -22.575 73.966 1.00 35.20 ? 136  GLN A NE2 1 
ATOM   1030 N N   . PRO A 1 137 ? -2.450  -26.218 70.035 1.00 26.97 ? 137  PRO A N   1 
ATOM   1031 C CA  . PRO A 1 137 ? -1.438  -25.748 69.086 1.00 26.39 ? 137  PRO A CA  1 
ATOM   1032 C C   . PRO A 1 137 ? -1.849  -24.414 68.433 1.00 25.47 ? 137  PRO A C   1 
ATOM   1033 O O   . PRO A 1 137 ? -2.997  -23.975 68.585 1.00 25.56 ? 137  PRO A O   1 
ATOM   1034 C CB  . PRO A 1 137 ? -1.412  -26.870 68.054 1.00 26.68 ? 137  PRO A CB  1 
ATOM   1035 C CG  . PRO A 1 137 ? -2.837  -27.384 68.029 1.00 27.32 ? 137  PRO A CG  1 
ATOM   1036 C CD  . PRO A 1 137 ? -3.455  -27.077 69.373 1.00 26.55 ? 137  PRO A CD  1 
ATOM   1037 N N   . PHE A 1 138 ? -0.912  -23.784 67.731 1.00 24.02 ? 138  PHE A N   1 
ATOM   1038 C CA  . PHE A 1 138 ? -1.153  -22.520 67.056 1.00 22.90 ? 138  PHE A CA  1 
ATOM   1039 C C   . PHE A 1 138 ? -2.299  -22.586 66.046 1.00 22.65 ? 138  PHE A C   1 
ATOM   1040 O O   . PHE A 1 138 ? -2.371  -23.498 65.218 1.00 22.08 ? 138  PHE A O   1 
ATOM   1041 C CB  . PHE A 1 138 ? 0.106   -21.995 66.356 1.00 21.29 ? 138  PHE A CB  1 
ATOM   1042 C CG  . PHE A 1 138 ? -0.152  -20.812 65.457 1.00 21.57 ? 138  PHE A CG  1 
ATOM   1043 C CD1 . PHE A 1 138 ? -0.167  -20.960 64.069 1.00 20.64 ? 138  PHE A CD1 1 
ATOM   1044 C CD2 . PHE A 1 138 ? -0.406  -19.550 65.999 1.00 19.99 ? 138  PHE A CD2 1 
ATOM   1045 C CE1 . PHE A 1 138 ? -0.430  -19.882 63.244 1.00 20.58 ? 138  PHE A CE1 1 
ATOM   1046 C CE2 . PHE A 1 138 ? -0.664  -18.465 65.174 1.00 21.76 ? 138  PHE A CE2 1 
ATOM   1047 C CZ  . PHE A 1 138 ? -0.676  -18.637 63.789 1.00 21.69 ? 138  PHE A CZ  1 
ATOM   1048 N N   . SER A 1 139 ? -3.192  -21.605 66.135 1.00 22.33 ? 139  SER A N   1 
ATOM   1049 C CA  . SER A 1 139 ? -4.151  -21.353 65.067 1.00 21.60 ? 139  SER A CA  1 
ATOM   1050 C C   . SER A 1 139 ? -4.495  -19.867 65.079 1.00 20.88 ? 139  SER A C   1 
ATOM   1051 O O   . SER A 1 139 ? -4.333  -19.218 66.098 1.00 20.84 ? 139  SER A O   1 
ATOM   1052 C CB  . SER A 1 139 ? -5.371  -22.286 65.150 1.00 22.28 ? 139  SER A CB  1 
ATOM   1053 O OG  . SER A 1 139 ? -6.330  -21.825 66.081 1.00 23.90 ? 139  SER A OG  1 
ATOM   1054 N N   . ILE A 1 140 ? -4.840  -19.321 63.913 1.00 19.95 ? 140  ILE A N   1 
ATOM   1055 C CA  . ILE A 1 140 ? -5.263  -17.933 63.762 1.00 19.73 ? 140  ILE A CA  1 
ATOM   1056 C C   . ILE A 1 140 ? -6.663  -17.939 63.177 1.00 19.68 ? 140  ILE A C   1 
ATOM   1057 O O   . ILE A 1 140 ? -6.933  -18.664 62.230 1.00 18.64 ? 140  ILE A O   1 
ATOM   1058 C CB  . ILE A 1 140 ? -4.284  -17.080 62.882 1.00 19.60 ? 140  ILE A CB  1 
ATOM   1059 C CG1 . ILE A 1 140 ? -4.767  -15.629 62.734 1.00 19.67 ? 140  ILE A CG1 1 
ATOM   1060 C CG2 . ILE A 1 140 ? -4.098  -17.682 61.488 1.00 18.66 ? 140  ILE A CG2 1 
ATOM   1061 C CD1 . ILE A 1 140 ? -3.609  -14.591 62.533 1.00 20.07 ? 140  ILE A CD1 1 
ATOM   1062 N N   . LYS A 1 141 ? -7.547  -17.147 63.762 1.00 19.92 ? 141  LYS A N   1 
ATOM   1063 C CA  . LYS A 1 141 ? -8.946  -17.097 63.343 1.00 20.50 ? 141  LYS A CA  1 
ATOM   1064 C C   . LYS A 1 141 ? -9.285  -15.628 63.131 1.00 19.99 ? 141  LYS A C   1 
ATOM   1065 O O   . LYS A 1 141 ? -8.857  -14.766 63.903 1.00 19.14 ? 141  LYS A O   1 
ATOM   1066 C CB  . LYS A 1 141 ? -9.849  -17.711 64.422 1.00 20.51 ? 141  LYS A CB  1 
ATOM   1067 C CG  . LYS A 1 141 ? -11.248 -18.109 63.944 1.00 25.73 ? 141  LYS A CG  1 
ATOM   1068 C CD  . LYS A 1 141 ? -12.314 -18.052 65.052 1.00 27.67 ? 141  LYS A CD  1 
ATOM   1069 C CE  . LYS A 1 141 ? -12.225 -19.212 66.032 1.00 30.79 ? 141  LYS A CE  1 
ATOM   1070 N NZ  . LYS A 1 141 ? -13.336 -19.188 67.076 1.00 31.02 ? 141  LYS A NZ  1 
ATOM   1071 N N   . VAL A 1 142 ? -10.005 -15.334 62.055 1.00 18.88 ? 142  VAL A N   1 
ATOM   1072 C CA  . VAL A 1 142 ? -10.459 -13.977 61.795 1.00 18.06 ? 142  VAL A CA  1 
ATOM   1073 C C   . VAL A 1 142 ? -11.969 -14.073 61.690 1.00 18.39 ? 142  VAL A C   1 
ATOM   1074 O O   . VAL A 1 142 ? -12.502 -14.848 60.904 1.00 17.42 ? 142  VAL A O   1 
ATOM   1075 C CB  . VAL A 1 142 ? -9.857  -13.335 60.512 1.00 18.25 ? 142  VAL A CB  1 
ATOM   1076 C CG1 . VAL A 1 142 ? -10.375 -11.911 60.332 1.00 17.53 ? 142  VAL A CG1 1 
ATOM   1077 C CG2 . VAL A 1 142 ? -8.299  -13.324 60.537 1.00 16.45 ? 142  VAL A CG2 1 
ATOM   1078 N N   . THR A 1 143 ? -12.650 -13.290 62.521 1.00 18.82 ? 143  THR A N   1 
ATOM   1079 C CA  . THR A 1 143 ? -14.100 -13.329 62.603 1.00 18.80 ? 143  THR A CA  1 
ATOM   1080 C C   . THR A 1 143 ? -14.711 -11.983 62.205 1.00 18.85 ? 143  THR A C   1 
ATOM   1081 O O   . THR A 1 143 ? -14.093 -10.939 62.329 1.00 19.92 ? 143  THR A O   1 
ATOM   1082 C CB  . THR A 1 143 ? -14.581 -13.756 64.003 1.00 18.91 ? 143  THR A CB  1 
ATOM   1083 O OG1 . THR A 1 143 ? -13.942 -12.942 65.003 1.00 22.17 ? 143  THR A OG1 1 
ATOM   1084 C CG2 . THR A 1 143 ? -14.250 -15.176 64.259 1.00 16.04 ? 143  THR A CG2 1 
ATOM   1085 N N   . ARG A 1 144 ? -15.908 -12.023 61.651 1.00 18.89 ? 144  ARG A N   1 
ATOM   1086 C CA  . ARG A 1 144 ? -16.662 -10.811 61.414 1.00 18.05 ? 144  ARG A CA  1 
ATOM   1087 C C   . ARG A 1 144 ? -17.317 -10.422 62.750 1.00 17.81 ? 144  ARG A C   1 
ATOM   1088 O O   . ARG A 1 144 ? -17.985 -11.224 63.378 1.00 16.31 ? 144  ARG A O   1 
ATOM   1089 C CB  . ARG A 1 144 ? -17.705 -11.046 60.312 1.00 18.32 ? 144  ARG A CB  1 
ATOM   1090 C CG  . ARG A 1 144 ? -18.553 -9.829  60.021 1.00 17.91 ? 144  ARG A CG  1 
ATOM   1091 C CD  . ARG A 1 144 ? -19.466 -10.059 58.823 1.00 17.99 ? 144  ARG A CD  1 
ATOM   1092 N NE  . ARG A 1 144 ? -18.737 -10.180 57.571 1.00 19.84 ? 144  ARG A NE  1 
ATOM   1093 C CZ  . ARG A 1 144 ? -18.274 -9.154  56.861 1.00 16.41 ? 144  ARG A CZ  1 
ATOM   1094 N NH1 . ARG A 1 144 ? -18.472 -7.911  57.270 1.00 16.90 ? 144  ARG A NH1 1 
ATOM   1095 N NH2 . ARG A 1 144 ? -17.634 -9.382  55.730 1.00 14.99 ? 144  ARG A NH2 1 
ATOM   1096 N N   . ARG A 1 145 ? -17.063 -9.200  63.194 1.00 18.72 ? 145  ARG A N   1 
ATOM   1097 C CA  . ARG A 1 145 ? -17.533 -8.687  64.468 1.00 20.25 ? 145  ARG A CA  1 
ATOM   1098 C C   . ARG A 1 145 ? -19.080 -8.654  64.540 1.00 21.09 ? 145  ARG A C   1 
ATOM   1099 O O   . ARG A 1 145 ? -19.661 -9.097  65.542 1.00 21.30 ? 145  ARG A O   1 
ATOM   1100 C CB  . ARG A 1 145 ? -16.956 -7.282  64.642 1.00 20.22 ? 145  ARG A CB  1 
ATOM   1101 C CG  . ARG A 1 145 ? -16.596 -6.905  66.036 1.00 25.97 ? 145  ARG A CG  1 
ATOM   1102 C CD  . ARG A 1 145 ? -15.558 -5.790  66.041 1.00 30.65 ? 145  ARG A CD  1 
ATOM   1103 N NE  . ARG A 1 145 ? -15.662 -4.965  67.234 1.00 34.14 ? 145  ARG A NE  1 
ATOM   1104 C CZ  . ARG A 1 145 ? -15.899 -3.650  67.256 1.00 35.97 ? 145  ARG A CZ  1 
ATOM   1105 N NH1 . ARG A 1 145 ? -16.053 -2.946  66.147 1.00 36.66 ? 145  ARG A NH1 1 
ATOM   1106 N NH2 . ARG A 1 145 ? -15.970 -3.025  68.423 1.00 38.50 ? 145  ARG A NH2 1 
ATOM   1107 N N   . SER A 1 146 ? -19.726 -8.143  63.489 1.00 21.22 ? 146  SER A N   1 
ATOM   1108 C CA  . SER A 1 146 ? -21.197 -7.977  63.473 1.00 22.58 ? 146  SER A CA  1 
ATOM   1109 C C   . SER A 1 146 ? -21.907 -9.271  63.871 1.00 23.05 ? 146  SER A C   1 
ATOM   1110 O O   . SER A 1 146 ? -22.651 -9.271  64.821 1.00 23.88 ? 146  SER A O   1 
ATOM   1111 C CB  . SER A 1 146 ? -21.711 -7.429  62.130 1.00 22.66 ? 146  SER A CB  1 
ATOM   1112 O OG  . SER A 1 146 ? -21.337 -8.251  61.028 1.00 22.23 ? 146  SER A OG  1 
ATOM   1113 N N   . ASN A 1 147 ? -21.583 -10.378 63.210 1.00 23.61 ? 147  ASN A N   1 
ATOM   1114 C CA  . ASN A 1 147 ? -22.249 -11.662 63.438 1.00 23.51 ? 147  ASN A CA  1 
ATOM   1115 C C   . ASN A 1 147 ? -21.335 -12.796 63.963 1.00 23.03 ? 147  ASN A C   1 
ATOM   1116 O O   . ASN A 1 147 ? -21.745 -13.949 64.049 1.00 23.58 ? 147  ASN A O   1 
ATOM   1117 C CB  . ASN A 1 147 ? -22.984 -12.095 62.164 1.00 23.13 ? 147  ASN A CB  1 
ATOM   1118 C CG  . ASN A 1 147 ? -22.062 -12.238 60.962 1.00 24.57 ? 147  ASN A CG  1 
ATOM   1119 O OD1 . ASN A 1 147 ? -20.820 -12.089 61.063 1.00 21.61 ? 147  ASN A OD1 1 
ATOM   1120 N ND2 . ASN A 1 147 ? -22.662 -12.529 59.812 1.00 19.35 ? 147  ASN A ND2 1 
ATOM   1121 N N   . ASN A 1 148 ? -20.104 -12.456 64.319 1.00 22.10 ? 148  ASN A N   1 
ATOM   1122 C CA  . ASN A 1 148 ? -19.093 -13.446 64.714 1.00 21.09 ? 148  ASN A CA  1 
ATOM   1123 C C   . ASN A 1 148 ? -18.961 -14.615 63.742 1.00 19.56 ? 148  ASN A C   1 
ATOM   1124 O O   . ASN A 1 148 ? -18.692 -15.739 64.160 1.00 20.43 ? 148  ASN A O   1 
ATOM   1125 C CB  . ASN A 1 148 ? -19.357 -13.963 66.148 1.00 22.19 ? 148  ASN A CB  1 
ATOM   1126 C CG  . ASN A 1 148 ? -19.008 -12.923 67.231 1.00 23.98 ? 148  ASN A CG  1 
ATOM   1127 O OD1 . ASN A 1 148 ? -19.528 -12.979 68.335 1.00 29.73 ? 148  ASN A OD1 1 
ATOM   1128 N ND2 . ASN A 1 148 ? -18.117 -12.000 66.914 1.00 23.57 ? 148  ASN A ND2 1 
ATOM   1129 N N   . ARG A 1 149 ? -19.153 -14.357 62.451 1.00 17.73 ? 149  ARG A N   1 
ATOM   1130 C CA  . ARG A 1 149 ? -19.000 -15.409 61.431 1.00 16.30 ? 149  ARG A CA  1 
ATOM   1131 C C   . ARG A 1 149 ? -17.507 -15.664 61.351 1.00 15.28 ? 149  ARG A C   1 
ATOM   1132 O O   . ARG A 1 149 ? -16.734 -14.744 61.197 1.00 14.83 ? 149  ARG A O   1 
ATOM   1133 C CB  . ARG A 1 149 ? -19.511 -14.935 60.089 1.00 15.46 ? 149  ARG A CB  1 
ATOM   1134 C CG  . ARG A 1 149 ? -19.283 -15.884 58.876 1.00 20.91 ? 149  ARG A CG  1 
ATOM   1135 C CD  . ARG A 1 149 ? -20.473 -16.759 58.600 1.00 27.15 ? 149  ARG A CD  1 
ATOM   1136 N NE  . ARG A 1 149 ? -21.668 -15.958 58.341 1.00 31.18 ? 149  ARG A NE  1 
ATOM   1137 C CZ  . ARG A 1 149 ? -22.884 -16.471 58.179 1.00 35.75 ? 149  ARG A CZ  1 
ATOM   1138 N NH1 . ARG A 1 149 ? -23.066 -17.794 58.240 1.00 37.21 ? 149  ARG A NH1 1 
ATOM   1139 N NH2 . ARG A 1 149 ? -23.916 -15.661 57.958 1.00 35.13 ? 149  ARG A NH2 1 
ATOM   1140 N N   . VAL A 1 150 ? -17.113 -16.908 61.472 1.00 15.79 ? 150  VAL A N   1 
ATOM   1141 C CA  . VAL A 1 150 ? -15.700 -17.239 61.352 1.00 15.70 ? 150  VAL A CA  1 
ATOM   1142 C C   . VAL A 1 150 ? -15.359 -17.175 59.875 1.00 15.47 ? 150  VAL A C   1 
ATOM   1143 O O   . VAL A 1 150 ? -15.931 -17.921 59.077 1.00 14.09 ? 150  VAL A O   1 
ATOM   1144 C CB  . VAL A 1 150 ? -15.428 -18.651 61.855 1.00 16.17 ? 150  VAL A CB  1 
ATOM   1145 C CG1 . VAL A 1 150 ? -13.949 -19.007 61.583 1.00 17.24 ? 150  VAL A CG1 1 
ATOM   1146 C CG2 . VAL A 1 150 ? -15.768 -18.759 63.357 1.00 15.83 ? 150  VAL A CG2 1 
ATOM   1147 N N   . LEU A 1 151 ? -14.415 -16.305 59.510 1.00 15.63 ? 151  LEU A N   1 
ATOM   1148 C CA  . LEU A 1 151 ? -14.027 -16.159 58.105 1.00 16.09 ? 151  LEU A CA  1 
ATOM   1149 C C   . LEU A 1 151 ? -12.744 -16.966 57.738 1.00 17.13 ? 151  LEU A C   1 
ATOM   1150 O O   . LEU A 1 151 ? -12.789 -17.806 56.856 1.00 17.52 ? 151  LEU A O   1 
ATOM   1151 C CB  . LEU A 1 151 ? -13.897 -14.673 57.737 1.00 15.05 ? 151  LEU A CB  1 
ATOM   1152 C CG  . LEU A 1 151 ? -15.100 -13.775 58.066 1.00 14.13 ? 151  LEU A CG  1 
ATOM   1153 C CD1 . LEU A 1 151 ? -14.761 -12.350 57.774 1.00 13.10 ? 151  LEU A CD1 1 
ATOM   1154 C CD2 . LEU A 1 151 ? -16.351 -14.202 57.306 1.00 12.70 ? 151  LEU A CD2 1 
ATOM   1155 N N   . PHE A 1 152 ? -11.620 -16.650 58.384 1.00 17.62 ? 152  PHE A N   1 
ATOM   1156 C CA  . PHE A 1 152 ? -10.341 -17.368 58.263 1.00 18.53 ? 152  PHE A CA  1 
ATOM   1157 C C   . PHE A 1 152 ? -10.202 -18.164 59.552 1.00 19.29 ? 152  PHE A C   1 
ATOM   1158 O O   . PHE A 1 152 ? -10.453 -17.630 60.624 1.00 19.20 ? 152  PHE A O   1 
ATOM   1159 C CB  . PHE A 1 152 ? -9.189  -16.348 58.212 1.00 18.27 ? 152  PHE A CB  1 
ATOM   1160 C CG  . PHE A 1 152 ? -7.895  -16.879 57.639 1.00 19.60 ? 152  PHE A CG  1 
ATOM   1161 C CD1 . PHE A 1 152 ? -7.594  -16.700 56.291 1.00 19.43 ? 152  PHE A CD1 1 
ATOM   1162 C CD2 . PHE A 1 152 ? -6.966  -17.541 58.449 1.00 19.04 ? 152  PHE A CD2 1 
ATOM   1163 C CE1 . PHE A 1 152 ? -6.373  -17.172 55.748 1.00 19.69 ? 152  PHE A CE1 1 
ATOM   1164 C CE2 . PHE A 1 152 ? -5.750  -18.022 57.916 1.00 19.69 ? 152  PHE A CE2 1 
ATOM   1165 C CZ  . PHE A 1 152 ? -5.461  -17.844 56.560 1.00 18.16 ? 152  PHE A CZ  1 
ATOM   1166 N N   . ASP A 1 153 ? -9.813  -19.432 59.461 1.00 19.92 ? 153  ASP A N   1 
ATOM   1167 C CA  . ASP A 1 153 ? -9.617  -20.257 60.643 1.00 20.00 ? 153  ASP A CA  1 
ATOM   1168 C C   . ASP A 1 153 ? -8.595  -21.316 60.311 1.00 19.32 ? 153  ASP A C   1 
ATOM   1169 O O   . ASP A 1 153 ? -8.937  -22.333 59.709 1.00 19.20 ? 153  ASP A O   1 
ATOM   1170 C CB  . ASP A 1 153 ? -10.948 -20.905 61.089 1.00 20.14 ? 153  ASP A CB  1 
ATOM   1171 C CG  . ASP A 1 153 ? -10.796 -21.788 62.315 1.00 23.22 ? 153  ASP A CG  1 
ATOM   1172 O OD1 . ASP A 1 153 ? -9.691  -21.843 62.927 1.00 25.92 ? 153  ASP A OD1 1 
ATOM   1173 O OD2 . ASP A 1 153 ? -11.787 -22.466 62.670 1.00 28.57 ? 153  ASP A OD2 1 
ATOM   1174 N N   . SER A 1 154 ? -7.334  -21.070 60.664 1.00 18.99 ? 154  SER A N   1 
ATOM   1175 C CA  . SER A 1 154 ? -6.272  -22.040 60.365 1.00 18.89 ? 154  SER A CA  1 
ATOM   1176 C C   . SER A 1 154 ? -6.348  -23.359 61.152 1.00 19.49 ? 154  SER A C   1 
ATOM   1177 O O   . SER A 1 154 ? -5.611  -24.303 60.812 1.00 20.26 ? 154  SER A O   1 
ATOM   1178 C CB  . SER A 1 154 ? -4.885  -21.410 60.528 1.00 19.00 ? 154  SER A CB  1 
ATOM   1179 O OG  . SER A 1 154 ? -4.654  -21.126 61.883 1.00 18.32 ? 154  SER A OG  1 
ATOM   1180 N N   . SER A 1 155 ? -7.249  -23.453 62.150 1.00 19.69 ? 155  SER A N   1 
ATOM   1181 C CA  . SER A 1 155 ? -7.294  -24.601 63.088 1.00 19.36 ? 155  SER A CA  1 
ATOM   1182 C C   . SER A 1 155 ? -7.672  -25.929 62.462 1.00 18.89 ? 155  SER A C   1 
ATOM   1183 O O   . SER A 1 155 ? -7.499  -26.981 63.105 1.00 19.13 ? 155  SER A O   1 
ATOM   1184 C CB  . SER A 1 155 ? -8.215  -24.338 64.299 1.00 19.61 ? 155  SER A CB  1 
ATOM   1185 O OG  . SER A 1 155 ? -9.595  -24.389 63.917 1.00 22.14 ? 155  SER A OG  1 
ATOM   1186 N N   . ILE A 1 156 ? -8.188  -25.905 61.230 1.00 17.93 ? 156  ILE A N   1 
ATOM   1187 C CA  . ILE A 1 156 ? -8.481  -27.159 60.501 1.00 17.03 ? 156  ILE A CA  1 
ATOM   1188 C C   . ILE A 1 156 ? -7.220  -28.013 60.201 1.00 16.91 ? 156  ILE A C   1 
ATOM   1189 O O   . ILE A 1 156 ? -7.272  -29.256 60.143 1.00 17.32 ? 156  ILE A O   1 
ATOM   1190 C CB  . ILE A 1 156 ? -9.290  -26.894 59.199 1.00 17.68 ? 156  ILE A CB  1 
ATOM   1191 C CG1 . ILE A 1 156 ? -9.919  -28.184 58.682 1.00 14.82 ? 156  ILE A CG1 1 
ATOM   1192 C CG2 . ILE A 1 156 ? -8.431  -26.120 58.148 1.00 16.07 ? 156  ILE A CG2 1 
ATOM   1193 C CD1 . ILE A 1 156 ? -11.102 -27.973 57.641 1.00 17.08 ? 156  ILE A CD1 1 
ATOM   1194 N N   . GLY A 1 157 ? -6.077  -27.363 60.063 1.00 16.43 ? 157  GLY A N   1 
ATOM   1195 C CA  . GLY A 1 157 ? -4.863  -28.098 59.787 1.00 15.64 ? 157  GLY A CA  1 
ATOM   1196 C C   . GLY A 1 157 ? -3.641  -27.473 60.421 1.00 15.76 ? 157  GLY A C   1 
ATOM   1197 O O   . GLY A 1 157 ? -3.715  -26.480 61.140 1.00 14.69 ? 157  GLY A O   1 
ATOM   1198 N N   . PRO A 1 158 ? -2.488  -28.080 60.180 1.00 16.11 ? 158  PRO A N   1 
ATOM   1199 C CA  . PRO A 1 158 ? -1.258  -27.556 60.751 1.00 16.08 ? 158  PRO A CA  1 
ATOM   1200 C C   . PRO A 1 158 ? -0.745  -26.292 60.058 1.00 16.37 ? 158  PRO A C   1 
ATOM   1201 O O   . PRO A 1 158 ? -1.193  -25.944 58.963 1.00 17.60 ? 158  PRO A O   1 
ATOM   1202 C CB  . PRO A 1 158 ? -0.280  -28.713 60.525 1.00 16.77 ? 158  PRO A CB  1 
ATOM   1203 C CG  . PRO A 1 158 ? -0.698  -29.290 59.203 1.00 15.35 ? 158  PRO A CG  1 
ATOM   1204 C CD  . PRO A 1 158 ? -2.252  -29.287 59.354 1.00 16.93 ? 158  PRO A CD  1 
ATOM   1205 N N   . LEU A 1 159 ? 0.181   -25.596 60.710 1.00 17.17 ? 159  LEU A N   1 
ATOM   1206 C CA  . LEU A 1 159 ? 1.116   -24.756 60.026 1.00 16.37 ? 159  LEU A CA  1 
ATOM   1207 C C   . LEU A 1 159 ? 2.361   -25.584 59.740 1.00 18.54 ? 159  LEU A C   1 
ATOM   1208 O O   . LEU A 1 159 ? 2.948   -26.164 60.652 1.00 18.23 ? 159  LEU A O   1 
ATOM   1209 C CB  . LEU A 1 159 ? 1.521   -23.548 60.875 1.00 16.97 ? 159  LEU A CB  1 
ATOM   1210 C CG  . LEU A 1 159 ? 2.825   -22.817 60.453 1.00 14.25 ? 159  LEU A CG  1 
ATOM   1211 C CD1 . LEU A 1 159 ? 2.719   -22.056 59.113 1.00 9.18  ? 159  LEU A CD1 1 
ATOM   1212 C CD2 . LEU A 1 159 ? 3.243   -21.858 61.556 1.00 13.69 ? 159  LEU A CD2 1 
ATOM   1213 N N   . LEU A 1 160 ? 2.776   -25.607 58.471 1.00 18.88 ? 160  LEU A N   1 
ATOM   1214 C CA  . LEU A 1 160 ? 4.017   -26.249 58.087 1.00 19.37 ? 160  LEU A CA  1 
ATOM   1215 C C   . LEU A 1 160 ? 4.937   -25.162 57.551 1.00 19.46 ? 160  LEU A C   1 
ATOM   1216 O O   . LEU A 1 160 ? 4.492   -24.257 56.838 1.00 19.50 ? 160  LEU A O   1 
ATOM   1217 C CB  . LEU A 1 160 ? 3.752   -27.391 57.083 1.00 19.29 ? 160  LEU A CB  1 
ATOM   1218 C CG  . LEU A 1 160 ? 2.707   -28.396 57.618 1.00 19.99 ? 160  LEU A CG  1 
ATOM   1219 C CD1 . LEU A 1 160 ? 2.186   -29.341 56.578 1.00 20.47 ? 160  LEU A CD1 1 
ATOM   1220 C CD2 . LEU A 1 160 ? 3.239   -29.183 58.819 1.00 22.64 ? 160  LEU A CD2 1 
ATOM   1221 N N   . PHE A 1 161 ? 6.201   -25.196 57.949 1.00 19.06 ? 161  PHE A N   1 
ATOM   1222 C CA  . PHE A 1 161 ? 7.122   -24.142 57.561 1.00 19.31 ? 161  PHE A CA  1 
ATOM   1223 C C   . PHE A 1 161 ? 8.552   -24.683 57.480 1.00 20.39 ? 161  PHE A C   1 
ATOM   1224 O O   . PHE A 1 161 ? 9.359   -24.494 58.399 1.00 19.06 ? 161  PHE A O   1 
ATOM   1225 C CB  . PHE A 1 161 ? 7.029   -22.956 58.524 1.00 19.85 ? 161  PHE A CB  1 
ATOM   1226 C CG  . PHE A 1 161 ? 7.578   -21.640 57.971 1.00 20.69 ? 161  PHE A CG  1 
ATOM   1227 C CD1 . PHE A 1 161 ? 6.919   -20.448 58.224 1.00 23.39 ? 161  PHE A CD1 1 
ATOM   1228 C CD2 . PHE A 1 161 ? 8.767   -21.598 57.224 1.00 23.42 ? 161  PHE A CD2 1 
ATOM   1229 C CE1 . PHE A 1 161 ? 7.402   -19.239 57.734 1.00 23.76 ? 161  PHE A CE1 1 
ATOM   1230 C CE2 . PHE A 1 161 ? 9.283   -20.399 56.740 1.00 21.43 ? 161  PHE A CE2 1 
ATOM   1231 C CZ  . PHE A 1 161 ? 8.597   -19.204 56.997 1.00 23.62 ? 161  PHE A CZ  1 
ATOM   1232 N N   . ALA A 1 162 ? 8.851   -25.329 56.359 1.00 20.60 ? 162  ALA A N   1 
ATOM   1233 C CA  . ALA A 1 162 ? 10.225  -25.684 56.016 1.00 20.67 ? 162  ALA A CA  1 
ATOM   1234 C C   . ALA A 1 162 ? 10.752  -24.700 54.973 1.00 20.75 ? 162  ALA A C   1 
ATOM   1235 O O   . ALA A 1 162 ? 9.988   -23.961 54.358 1.00 20.08 ? 162  ALA A O   1 
ATOM   1236 C CB  . ALA A 1 162 ? 10.269  -27.093 55.515 1.00 20.58 ? 162  ALA A CB  1 
ATOM   1237 N N   . ASP A 1 163 ? 12.067  -24.665 54.788 1.00 20.49 ? 163  ASP A N   1 
ATOM   1238 C CA  . ASP A 1 163 ? 12.675  -23.754 53.843 1.00 20.77 ? 163  ASP A CA  1 
ATOM   1239 C C   . ASP A 1 163 ? 11.992  -23.785 52.454 1.00 20.62 ? 163  ASP A C   1 
ATOM   1240 O O   . ASP A 1 163 ? 11.889  -22.747 51.794 1.00 21.17 ? 163  ASP A O   1 
ATOM   1241 C CB  . ASP A 1 163 ? 14.192  -24.039 53.770 1.00 21.92 ? 163  ASP A CB  1 
ATOM   1242 C CG  . ASP A 1 163 ? 14.928  -23.109 52.839 1.00 24.16 ? 163  ASP A CG  1 
ATOM   1243 O OD1 . ASP A 1 163 ? 14.732  -21.869 52.874 1.00 27.87 ? 163  ASP A OD1 1 
ATOM   1244 O OD2 . ASP A 1 163 ? 15.751  -23.633 52.072 1.00 31.23 ? 163  ASP A OD2 1 
ATOM   1245 N N   . GLN A 1 164 ? 11.507  -24.955 52.029 1.00 20.28 ? 164  GLN A N   1 
ATOM   1246 C CA  . GLN A 1 164 ? 10.932  -25.122 50.683 1.00 19.42 ? 164  GLN A CA  1 
ATOM   1247 C C   . GLN A 1 164 ? 9.609   -25.852 50.718 1.00 19.37 ? 164  GLN A C   1 
ATOM   1248 O O   . GLN A 1 164 ? 9.236   -26.542 49.756 1.00 18.35 ? 164  GLN A O   1 
ATOM   1249 C CB  . GLN A 1 164 ? 11.915  -25.866 49.746 1.00 19.75 ? 164  GLN A CB  1 
ATOM   1250 C CG  . GLN A 1 164 ? 13.187  -25.092 49.450 1.00 18.55 ? 164  GLN A CG  1 
ATOM   1251 C CD  . GLN A 1 164 ? 14.084  -25.816 48.476 1.00 18.96 ? 164  GLN A CD  1 
ATOM   1252 O OE1 . GLN A 1 164 ? 13.912  -25.723 47.270 1.00 22.23 ? 164  GLN A OE1 1 
ATOM   1253 N NE2 . GLN A 1 164 ? 15.027  -26.547 48.994 1.00 18.18 ? 164  GLN A NE2 1 
ATOM   1254 N N   . PHE A 1 165 ? 8.900   -25.705 51.836 1.00 19.46 ? 165  PHE A N   1 
ATOM   1255 C CA  . PHE A 1 165 ? 7.547   -26.211 51.960 1.00 20.18 ? 165  PHE A CA  1 
ATOM   1256 C C   . PHE A 1 165 ? 6.804   -25.454 53.060 1.00 20.09 ? 165  PHE A C   1 
ATOM   1257 O O   . PHE A 1 165 ? 7.101   -25.622 54.255 1.00 19.77 ? 165  PHE A O   1 
ATOM   1258 C CB  . PHE A 1 165 ? 7.504   -27.696 52.258 1.00 20.23 ? 165  PHE A CB  1 
ATOM   1259 C CG  . PHE A 1 165 ? 6.129   -28.289 52.140 1.00 22.53 ? 165  PHE A CG  1 
ATOM   1260 C CD1 . PHE A 1 165 ? 5.654   -28.736 50.914 1.00 23.60 ? 165  PHE A CD1 1 
ATOM   1261 C CD2 . PHE A 1 165 ? 5.304   -28.391 53.243 1.00 23.99 ? 165  PHE A CD2 1 
ATOM   1262 C CE1 . PHE A 1 165 ? 4.396   -29.279 50.806 1.00 24.78 ? 165  PHE A CE1 1 
ATOM   1263 C CE2 . PHE A 1 165 ? 4.034   -28.944 53.137 1.00 23.45 ? 165  PHE A CE2 1 
ATOM   1264 C CZ  . PHE A 1 165 ? 3.589   -29.395 51.921 1.00 24.59 ? 165  PHE A CZ  1 
ATOM   1265 N N   . LEU A 1 166 ? 5.863   -24.613 52.641 1.00 18.30 ? 166  LEU A N   1 
ATOM   1266 C CA  . LEU A 1 166 ? 5.080   -23.809 53.582 1.00 18.41 ? 166  LEU A CA  1 
ATOM   1267 C C   . LEU A 1 166 ? 3.633   -24.111 53.311 1.00 17.77 ? 166  LEU A C   1 
ATOM   1268 O O   . LEU A 1 166 ? 3.226   -24.152 52.168 1.00 17.75 ? 166  LEU A O   1 
ATOM   1269 C CB  . LEU A 1 166 ? 5.339   -22.318 53.397 1.00 17.16 ? 166  LEU A CB  1 
ATOM   1270 C CG  . LEU A 1 166 ? 6.706   -21.709 53.760 1.00 19.69 ? 166  LEU A CG  1 
ATOM   1271 C CD1 . LEU A 1 166 ? 7.739   -22.034 52.713 1.00 17.69 ? 166  LEU A CD1 1 
ATOM   1272 C CD2 . LEU A 1 166 ? 6.539   -20.211 53.845 1.00 20.19 ? 166  LEU A CD2 1 
ATOM   1273 N N   . GLN A 1 167 ? 2.862   -24.335 54.361 1.00 17.58 ? 167  GLN A N   1 
ATOM   1274 C CA  . GLN A 1 167 ? 1.457   -24.658 54.175 1.00 16.70 ? 167  GLN A CA  1 
ATOM   1275 C C   . GLN A 1 167 ? 0.612   -24.085 55.327 1.00 16.56 ? 167  GLN A C   1 
ATOM   1276 O O   . GLN A 1 167 ? 0.956   -24.224 56.502 1.00 15.08 ? 167  GLN A O   1 
ATOM   1277 C CB  . GLN A 1 167 ? 1.252   -26.178 54.076 1.00 17.12 ? 167  GLN A CB  1 
ATOM   1278 C CG  . GLN A 1 167 ? -0.220  -26.578 53.937 1.00 15.78 ? 167  GLN A CG  1 
ATOM   1279 C CD  . GLN A 1 167 ? -0.450  -28.076 53.767 1.00 17.26 ? 167  GLN A CD  1 
ATOM   1280 O OE1 . GLN A 1 167 ? -1.236  -28.693 54.511 1.00 20.07 ? 167  GLN A OE1 1 
ATOM   1281 N NE2 . GLN A 1 167 ? 0.197   -28.657 52.801 1.00 14.87 ? 167  GLN A NE2 1 
ATOM   1282 N N   . LEU A 1 168 ? -0.486  -23.429 54.968 1.00 15.48 ? 168  LEU A N   1 
ATOM   1283 C CA  . LEU A 1 168 ? -1.477  -23.056 55.935 1.00 15.38 ? 168  LEU A CA  1 
ATOM   1284 C C   . LEU A 1 168 ? -2.836  -23.290 55.304 1.00 15.37 ? 168  LEU A C   1 
ATOM   1285 O O   . LEU A 1 168 ? -3.020  -23.023 54.123 1.00 16.05 ? 168  LEU A O   1 
ATOM   1286 C CB  . LEU A 1 168 ? -1.334  -21.582 56.349 1.00 15.15 ? 168  LEU A CB  1 
ATOM   1287 C CG  . LEU A 1 168 ? -2.124  -21.180 57.615 1.00 15.40 ? 168  LEU A CG  1 
ATOM   1288 C CD1 . LEU A 1 168 ? -1.642  -21.893 58.881 1.00 13.78 ? 168  LEU A CD1 1 
ATOM   1289 C CD2 . LEU A 1 168 ? -2.102  -19.720 57.822 1.00 15.01 ? 168  LEU A CD2 1 
ATOM   1290 N N   . SER A 1 169 ? -3.781  -23.773 56.099 1.00 15.33 ? 169  SER A N   1 
ATOM   1291 C CA  . SER A 1 169 ? -5.150  -23.998 55.631 1.00 15.19 ? 169  SER A CA  1 
ATOM   1292 C C   . SER A 1 169 ? -6.076  -23.001 56.285 1.00 15.53 ? 169  SER A C   1 
ATOM   1293 O O   . SER A 1 169 ? -5.687  -22.352 57.227 1.00 16.23 ? 169  SER A O   1 
ATOM   1294 C CB  . SER A 1 169 ? -5.610  -25.412 55.960 1.00 14.56 ? 169  SER A CB  1 
ATOM   1295 O OG  . SER A 1 169 ? -4.583  -26.351 55.712 1.00 16.91 ? 169  SER A OG  1 
ATOM   1296 N N   . THR A 1 170 ? -7.289  -22.844 55.744 1.00 16.65 ? 170  THR A N   1 
ATOM   1297 C CA  . THR A 1 170 ? -8.352  -22.091 56.413 1.00 17.14 ? 170  THR A CA  1 
ATOM   1298 C C   . THR A 1 170 ? -9.677  -22.757 56.103 1.00 16.98 ? 170  THR A C   1 
ATOM   1299 O O   . THR A 1 170 ? -9.928  -23.137 54.964 1.00 17.05 ? 170  THR A O   1 
ATOM   1300 C CB  . THR A 1 170 ? -8.425  -20.575 56.015 1.00 17.05 ? 170  THR A CB  1 
ATOM   1301 O OG1 . THR A 1 170 ? -9.532  -19.952 56.684 1.00 19.45 ? 170  THR A OG1 1 
ATOM   1302 C CG2 . THR A 1 170 ? -8.601  -20.357 54.501 1.00 18.83 ? 170  THR A CG2 1 
ATOM   1303 N N   . ARG A 1 171 ? -10.502 -22.937 57.123 1.00 16.84 ? 171  ARG A N   1 
ATOM   1304 C CA  . ARG A 1 171 ? -11.931 -23.124 56.874 1.00 17.49 ? 171  ARG A CA  1 
ATOM   1305 C C   . ARG A 1 171 ? -12.501 -21.903 56.160 1.00 17.59 ? 171  ARG A C   1 
ATOM   1306 O O   . ARG A 1 171 ? -11.918 -20.795 56.218 1.00 18.62 ? 171  ARG A O   1 
ATOM   1307 C CB  . ARG A 1 171 ? -12.677 -23.338 58.168 1.00 17.81 ? 171  ARG A CB  1 
ATOM   1308 C CG  . ARG A 1 171 ? -12.135 -24.457 59.026 1.00 19.17 ? 171  ARG A CG  1 
ATOM   1309 C CD  . ARG A 1 171 ? -13.023 -24.703 60.243 1.00 23.73 ? 171  ARG A CD  1 
ATOM   1310 N NE  . ARG A 1 171 ? -12.183 -24.960 61.411 1.00 25.67 ? 171  ARG A NE  1 
ATOM   1311 C CZ  . ARG A 1 171 ? -11.903 -26.158 61.882 1.00 25.58 ? 171  ARG A CZ  1 
ATOM   1312 N NH1 . ARG A 1 171 ? -12.448 -27.228 61.325 1.00 29.97 ? 171  ARG A NH1 1 
ATOM   1313 N NH2 . ARG A 1 171 ? -11.114 -26.275 62.941 1.00 28.08 ? 171  ARG A NH2 1 
ATOM   1314 N N   . LEU A 1 172 ? -13.642 -22.120 55.512 1.00 17.61 ? 172  LEU A N   1 
ATOM   1315 C CA  . LEU A 1 172 ? -14.360 -21.130 54.721 1.00 18.40 ? 172  LEU A CA  1 
ATOM   1316 C C   . LEU A 1 172 ? -15.806 -21.166 55.185 1.00 18.20 ? 172  LEU A C   1 
ATOM   1317 O O   . LEU A 1 172 ? -16.301 -22.246 55.516 1.00 17.70 ? 172  LEU A O   1 
ATOM   1318 C CB  . LEU A 1 172 ? -14.263 -21.454 53.205 1.00 18.08 ? 172  LEU A CB  1 
ATOM   1319 C CG  . LEU A 1 172 ? -12.896 -21.177 52.566 1.00 19.69 ? 172  LEU A CG  1 
ATOM   1320 C CD1 . LEU A 1 172 ? -12.774 -21.603 51.087 1.00 17.87 ? 172  LEU A CD1 1 
ATOM   1321 C CD2 . LEU A 1 172 ? -12.561 -19.697 52.723 1.00 18.03 ? 172  LEU A CD2 1 
ATOM   1322 N N   . PRO A 1 173 ? -16.471 -19.988 55.271 1.00 18.71 ? 173  PRO A N   1 
ATOM   1323 C CA  . PRO A 1 173 ? -17.882 -19.908 55.716 1.00 18.91 ? 173  PRO A CA  1 
ATOM   1324 C C   . PRO A 1 173 ? -18.940 -20.353 54.724 1.00 20.35 ? 173  PRO A C   1 
ATOM   1325 O O   . PRO A 1 173 ? -20.131 -20.449 55.092 1.00 21.26 ? 173  PRO A O   1 
ATOM   1326 C CB  . PRO A 1 173 ? -18.058 -18.409 56.038 1.00 18.00 ? 173  PRO A CB  1 
ATOM   1327 C CG  . PRO A 1 173 ? -17.188 -17.735 55.155 1.00 17.28 ? 173  PRO A CG  1 
ATOM   1328 C CD  . PRO A 1 173 ? -15.920 -18.636 55.070 1.00 18.97 ? 173  PRO A CD  1 
ATOM   1329 N N   . SER A 1 174 ? -18.530 -20.608 53.478 1.00 20.70 ? 174  SER A N   1 
ATOM   1330 C CA  . SER A 1 174 ? -19.427 -21.001 52.410 1.00 20.44 ? 174  SER A CA  1 
ATOM   1331 C C   . SER A 1 174 ? -18.676 -21.666 51.264 1.00 20.44 ? 174  SER A C   1 
ATOM   1332 O O   . SER A 1 174 ? -17.439 -21.653 51.203 1.00 20.28 ? 174  SER A O   1 
ATOM   1333 C CB  . SER A 1 174 ? -20.202 -19.792 51.869 1.00 20.71 ? 174  SER A CB  1 
ATOM   1334 O OG  . SER A 1 174 ? -19.351 -18.969 51.077 1.00 22.12 ? 174  SER A OG  1 
ATOM   1335 N N   . THR A 1 175 ? -19.440 -22.233 50.343 1.00 19.56 ? 175  THR A N   1 
ATOM   1336 C CA  . THR A 1 175 ? -18.873 -22.758 49.117 1.00 19.86 ? 175  THR A CA  1 
ATOM   1337 C C   . THR A 1 175 ? -18.958 -21.739 47.988 1.00 19.01 ? 175  THR A C   1 
ATOM   1338 O O   . THR A 1 175 ? -18.711 -22.088 46.852 1.00 20.16 ? 175  THR A O   1 
ATOM   1339 C CB  . THR A 1 175 ? -19.549 -24.072 48.688 1.00 20.01 ? 175  THR A CB  1 
ATOM   1340 O OG1 . THR A 1 175 ? -20.961 -23.850 48.566 1.00 19.94 ? 175  THR A OG1 1 
ATOM   1341 C CG2 . THR A 1 175 ? -19.254 -25.205 49.714 1.00 20.09 ? 175  THR A CG2 1 
ATOM   1342 N N   . ASN A 1 176 ? -19.316 -20.485 48.291 1.00 18.02 ? 176  ASN A N   1 
ATOM   1343 C CA  . ASN A 1 176 ? -19.395 -19.447 47.273 1.00 17.41 ? 176  ASN A CA  1 
ATOM   1344 C C   . ASN A 1 176 ? -18.030 -18.796 47.112 1.00 16.11 ? 176  ASN A C   1 
ATOM   1345 O O   . ASN A 1 176 ? -17.799 -17.715 47.582 1.00 16.88 ? 176  ASN A O   1 
ATOM   1346 C CB  . ASN A 1 176 ? -20.478 -18.393 47.594 1.00 17.30 ? 176  ASN A CB  1 
ATOM   1347 C CG  . ASN A 1 176 ? -21.839 -19.012 47.857 1.00 19.44 ? 176  ASN A CG  1 
ATOM   1348 O OD1 . ASN A 1 176 ? -22.230 -19.933 47.179 1.00 19.64 ? 176  ASN A OD1 1 
ATOM   1349 N ND2 . ASN A 1 176 ? -22.554 -18.510 48.872 1.00 23.05 ? 176  ASN A ND2 1 
ATOM   1350 N N   . VAL A 1 177 ? -17.128 -19.491 46.448 1.00 16.45 ? 177  VAL A N   1 
ATOM   1351 C CA  . VAL A 1 177 ? -15.707 -19.103 46.366 1.00 14.70 ? 177  VAL A CA  1 
ATOM   1352 C C   . VAL A 1 177 ? -15.376 -18.791 44.904 1.00 13.83 ? 177  VAL A C   1 
ATOM   1353 O O   . VAL A 1 177 ? -15.637 -19.599 44.040 1.00 14.24 ? 177  VAL A O   1 
ATOM   1354 C CB  . VAL A 1 177 ? -14.809 -20.243 46.906 1.00 15.16 ? 177  VAL A CB  1 
ATOM   1355 C CG1 . VAL A 1 177 ? -13.289 -19.971 46.616 1.00 13.87 ? 177  VAL A CG1 1 
ATOM   1356 C CG2 . VAL A 1 177 ? -15.043 -20.450 48.406 1.00 16.54 ? 177  VAL A CG2 1 
ATOM   1357 N N   . TYR A 1 178 ? -14.780 -17.630 44.640 1.00 13.79 ? 178  TYR A N   1 
ATOM   1358 C CA  . TYR A 1 178 ? -14.490 -17.169 43.273 1.00 13.49 ? 178  TYR A CA  1 
ATOM   1359 C C   . TYR A 1 178 ? -13.069 -16.646 43.236 1.00 13.72 ? 178  TYR A C   1 
ATOM   1360 O O   . TYR A 1 178 ? -12.634 -15.996 44.167 1.00 14.43 ? 178  TYR A O   1 
ATOM   1361 C CB  . TYR A 1 178 ? -15.442 -16.029 42.894 1.00 12.64 ? 178  TYR A CB  1 
ATOM   1362 C CG  . TYR A 1 178 ? -16.876 -16.359 43.247 1.00 13.37 ? 178  TYR A CG  1 
ATOM   1363 C CD1 . TYR A 1 178 ? -17.687 -17.030 42.347 1.00 12.69 ? 178  TYR A CD1 1 
ATOM   1364 C CD2 . TYR A 1 178 ? -17.416 -16.000 44.478 1.00 12.84 ? 178  TYR A CD2 1 
ATOM   1365 C CE1 . TYR A 1 178 ? -19.004 -17.352 42.665 1.00 13.47 ? 178  TYR A CE1 1 
ATOM   1366 C CE2 . TYR A 1 178 ? -18.749 -16.316 44.798 1.00 12.76 ? 178  TYR A CE2 1 
ATOM   1367 C CZ  . TYR A 1 178 ? -19.508 -17.016 43.885 1.00 11.82 ? 178  TYR A CZ  1 
ATOM   1368 O OH  . TYR A 1 178 ? -20.811 -17.346 44.154 1.00 17.62 ? 178  TYR A OH  1 
ATOM   1369 N N   . GLY A 1 179 ? -12.321 -16.928 42.173 1.00 14.09 ? 179  GLY A N   1 
ATOM   1370 C CA  . GLY A 1 179 ? -10.937 -16.457 42.165 1.00 13.90 ? 179  GLY A CA  1 
ATOM   1371 C C   . GLY A 1 179 ? -9.900  -17.505 41.869 1.00 13.85 ? 179  GLY A C   1 
ATOM   1372 O O   . GLY A 1 179 ? -10.215 -18.554 41.293 1.00 14.29 ? 179  GLY A O   1 
ATOM   1373 N N   . LEU A 1 180 ? -8.662  -17.174 42.221 1.00 14.08 ? 180  LEU A N   1 
ATOM   1374 C CA  . LEU A 1 180 ? -7.447  -17.938 41.867 1.00 14.89 ? 180  LEU A CA  1 
ATOM   1375 C C   . LEU A 1 180 ? -7.169  -17.950 40.380 1.00 14.41 ? 180  LEU A C   1 
ATOM   1376 O O   . LEU A 1 180 ? -8.083  -17.926 39.565 1.00 14.34 ? 180  LEU A O   1 
ATOM   1377 C CB  . LEU A 1 180 ? -7.480  -19.376 42.394 1.00 14.99 ? 180  LEU A CB  1 
ATOM   1378 C CG  . LEU A 1 180 ? -7.924  -19.558 43.845 1.00 17.61 ? 180  LEU A CG  1 
ATOM   1379 C CD1 . LEU A 1 180 ? -8.480  -20.994 44.028 1.00 16.35 ? 180  LEU A CD1 1 
ATOM   1380 C CD2 . LEU A 1 180 ? -6.821  -19.158 44.870 1.00 17.63 ? 180  LEU A CD2 1 
ATOM   1381 N N   . GLY A 1 181 ? -5.891  -17.965 40.021 1.00 13.76 ? 181  GLY A N   1 
ATOM   1382 C CA  . GLY A 1 181 ? -5.505  -18.026 38.635 1.00 13.65 ? 181  GLY A CA  1 
ATOM   1383 C C   . GLY A 1 181 ? -3.996  -18.124 38.473 1.00 14.32 ? 181  GLY A C   1 
ATOM   1384 O O   . GLY A 1 181 ? -3.277  -18.108 39.460 1.00 14.69 ? 181  GLY A O   1 
ATOM   1385 N N   . GLU A 1 182 ? -3.525  -18.206 37.236 1.00 15.12 ? 182  GLU A N   1 
ATOM   1386 C CA  . GLU A 1 182 ? -4.406  -18.219 36.049 1.00 15.31 ? 182  GLU A CA  1 
ATOM   1387 C C   . GLU A 1 182 ? -4.740  -19.624 35.600 1.00 15.91 ? 182  GLU A C   1 
ATOM   1388 O O   . GLU A 1 182 ? -3.841  -20.485 35.457 1.00 15.74 ? 182  GLU A O   1 
ATOM   1389 C CB  . GLU A 1 182 ? -3.747  -17.450 34.918 1.00 16.50 ? 182  GLU A CB  1 
ATOM   1390 C CG  . GLU A 1 182 ? -4.632  -17.232 33.713 1.00 14.64 ? 182  GLU A CG  1 
ATOM   1391 C CD  . GLU A 1 182 ? -3.977  -16.314 32.724 1.00 20.09 ? 182  GLU A CD  1 
ATOM   1392 O OE1 . GLU A 1 182 ? -2.766  -15.969 32.921 1.00 17.58 ? 182  GLU A OE1 1 
ATOM   1393 O OE2 . GLU A 1 182 ? -4.668  -15.931 31.761 1.00 19.51 ? 182  GLU A OE2 1 
ATOM   1394 N N   . HIS A 1 183 ? -6.039  -19.885 35.437 1.00 14.92 ? 183  HIS A N   1 
ATOM   1395 C CA  . HIS A 1 183 ? -6.496  -21.192 35.000 1.00 15.34 ? 183  HIS A CA  1 
ATOM   1396 C C   . HIS A 1 183 ? -7.753  -21.058 34.122 1.00 15.39 ? 183  HIS A C   1 
ATOM   1397 O O   . HIS A 1 183 ? -8.403  -20.003 34.112 1.00 15.39 ? 183  HIS A O   1 
ATOM   1398 C CB  . HIS A 1 183 ? -6.873  -22.133 36.172 1.00 14.40 ? 183  HIS A CB  1 
ATOM   1399 C CG  . HIS A 1 183 ? -6.058  -21.985 37.417 1.00 14.35 ? 183  HIS A CG  1 
ATOM   1400 N ND1 . HIS A 1 183 ? -4.782  -22.517 37.552 1.00 13.88 ? 183  HIS A ND1 1 
ATOM   1401 C CD2 . HIS A 1 183 ? -6.390  -21.495 38.634 1.00 8.42  ? 183  HIS A CD2 1 
ATOM   1402 C CE1 . HIS A 1 183 ? -4.325  -22.250 38.760 1.00 8.72  ? 183  HIS A CE1 1 
ATOM   1403 N NE2 . HIS A 1 183 ? -5.281  -21.640 39.440 1.00 15.20 ? 183  HIS A NE2 1 
ATOM   1404 N N   . VAL A 1 184 ? -8.088  -22.142 33.423 1.00 14.91 ? 184  VAL A N   1 
ATOM   1405 C CA  . VAL A 1 184 ? -9.434  -22.334 32.865 1.00 15.61 ? 184  VAL A CA  1 
ATOM   1406 C C   . VAL A 1 184 ? -10.218 -23.180 33.873 1.00 15.94 ? 184  VAL A C   1 
ATOM   1407 O O   . VAL A 1 184 ? -10.099 -24.403 33.923 1.00 15.61 ? 184  VAL A O   1 
ATOM   1408 C CB  . VAL A 1 184 ? -9.378  -23.011 31.483 1.00 15.33 ? 184  VAL A CB  1 
ATOM   1409 C CG1 . VAL A 1 184 ? -10.770 -23.367 30.967 1.00 16.31 ? 184  VAL A CG1 1 
ATOM   1410 C CG2 . VAL A 1 184 ? -8.601  -22.154 30.478 1.00 13.74 ? 184  VAL A CG2 1 
ATOM   1411 N N   . HIS A 1 185 ? -10.995 -22.520 34.722 1.00 17.78 ? 185  HIS A N   1 
ATOM   1412 C CA  . HIS A 1 185 ? -11.759 -23.226 35.738 1.00 17.51 ? 185  HIS A CA  1 
ATOM   1413 C C   . HIS A 1 185 ? -13.048 -23.824 35.151 1.00 18.90 ? 185  HIS A C   1 
ATOM   1414 O O   . HIS A 1 185 ? -13.660 -24.672 35.791 1.00 19.10 ? 185  HIS A O   1 
ATOM   1415 C CB  . HIS A 1 185 ? -12.127 -22.292 36.917 1.00 17.86 ? 185  HIS A CB  1 
ATOM   1416 C CG  . HIS A 1 185 ? -10.944 -21.723 37.637 1.00 15.90 ? 185  HIS A CG  1 
ATOM   1417 N ND1 . HIS A 1 185 ? -10.901 -20.418 38.075 1.00 13.45 ? 185  HIS A ND1 1 
ATOM   1418 C CD2 . HIS A 1 185 ? -9.756  -22.280 37.991 1.00 16.35 ? 185  HIS A CD2 1 
ATOM   1419 C CE1 . HIS A 1 185 ? -9.735  -20.196 38.662 1.00 19.22 ? 185  HIS A CE1 1 
ATOM   1420 N NE2 . HIS A 1 185 ? -9.021  -21.306 38.618 1.00 13.86 ? 185  HIS A NE2 1 
ATOM   1421 N N   . GLN A 1 186 ? -13.463 -23.346 33.975 1.00 19.49 ? 186  GLN A N   1 
ATOM   1422 C CA  . GLN A 1 186 ? -14.669 -23.823 33.247 1.00 20.77 ? 186  GLN A CA  1 
ATOM   1423 C C   . GLN A 1 186 ? -15.980 -23.326 33.858 1.00 20.84 ? 186  GLN A C   1 
ATOM   1424 O O   . GLN A 1 186 ? -16.852 -22.847 33.142 1.00 21.91 ? 186  GLN A O   1 
ATOM   1425 C CB  . GLN A 1 186 ? -14.677 -25.346 33.063 1.00 20.24 ? 186  GLN A CB  1 
ATOM   1426 C CG  . GLN A 1 186 ? -13.385 -25.873 32.390 1.00 21.95 ? 186  GLN A CG  1 
ATOM   1427 C CD  . GLN A 1 186 ? -13.448 -27.349 32.076 1.00 22.67 ? 186  GLN A CD  1 
ATOM   1428 O OE1 . GLN A 1 186 ? -14.531 -27.910 31.891 1.00 24.91 ? 186  GLN A OE1 1 
ATOM   1429 N NE2 . GLN A 1 186 ? -12.284 -27.986 32.002 1.00 24.08 ? 186  GLN A NE2 1 
ATOM   1430 N N   . GLN A 1 187 ? -16.108 -23.427 35.170 1.00 20.22 ? 187  GLN A N   1 
ATOM   1431 C CA  . GLN A 1 187 ? -17.169 -22.725 35.893 1.00 20.85 ? 187  GLN A CA  1 
ATOM   1432 C C   . GLN A 1 187 ? -16.597 -21.531 36.662 1.00 18.99 ? 187  GLN A C   1 
ATOM   1433 O O   . GLN A 1 187 ? -15.399 -21.419 36.803 1.00 18.01 ? 187  GLN A O   1 
ATOM   1434 C CB  . GLN A 1 187 ? -17.872 -23.688 36.826 1.00 22.01 ? 187  GLN A CB  1 
ATOM   1435 C CG  . GLN A 1 187 ? -18.768 -24.677 36.100 1.00 27.39 ? 187  GLN A CG  1 
ATOM   1436 C CD  . GLN A 1 187 ? -19.331 -25.710 37.042 1.00 36.97 ? 187  GLN A CD  1 
ATOM   1437 O OE1 . GLN A 1 187 ? -18.614 -26.222 37.923 1.00 41.67 ? 187  GLN A OE1 1 
ATOM   1438 N NE2 . GLN A 1 187 ? -20.629 -26.038 36.871 1.00 40.37 ? 187  GLN A NE2 1 
ATOM   1439 N N   . TYR A 1 188 ? -17.447 -20.630 37.144 1.00 17.91 ? 188  TYR A N   1 
ATOM   1440 C CA  . TYR A 1 188 ? -16.949 -19.472 37.882 1.00 16.95 ? 188  TYR A CA  1 
ATOM   1441 C C   . TYR A 1 188 ? -16.952 -19.742 39.408 1.00 17.25 ? 188  TYR A C   1 
ATOM   1442 O O   . TYR A 1 188 ? -15.963 -19.469 40.099 1.00 16.09 ? 188  TYR A O   1 
ATOM   1443 C CB  . TYR A 1 188 ? -17.729 -18.197 37.491 1.00 16.61 ? 188  TYR A CB  1 
ATOM   1444 C CG  . TYR A 1 188 ? -17.313 -16.939 38.211 1.00 14.21 ? 188  TYR A CG  1 
ATOM   1445 C CD1 . TYR A 1 188 ? -16.016 -16.432 38.083 1.00 14.20 ? 188  TYR A CD1 1 
ATOM   1446 C CD2 . TYR A 1 188 ? -18.210 -16.251 39.014 1.00 14.12 ? 188  TYR A CD2 1 
ATOM   1447 C CE1 . TYR A 1 188 ? -15.622 -15.298 38.734 1.00 12.65 ? 188  TYR A CE1 1 
ATOM   1448 C CE2 . TYR A 1 188 ? -17.811 -15.104 39.679 1.00 14.08 ? 188  TYR A CE2 1 
ATOM   1449 C CZ  . TYR A 1 188 ? -16.525 -14.634 39.528 1.00 13.87 ? 188  TYR A CZ  1 
ATOM   1450 O OH  . TYR A 1 188 ? -16.126 -13.490 40.184 1.00 15.37 ? 188  TYR A OH  1 
ATOM   1451 N N   . ARG A 1 189 ? -18.053 -20.288 39.931 1.00 17.12 ? 189  ARG A N   1 
ATOM   1452 C CA  . ARG A 1 189 ? -18.059 -20.703 41.318 1.00 17.61 ? 189  ARG A CA  1 
ATOM   1453 C C   . ARG A 1 189 ? -17.219 -21.953 41.494 1.00 18.83 ? 189  ARG A C   1 
ATOM   1454 O O   . ARG A 1 189 ? -17.398 -22.962 40.814 1.00 17.97 ? 189  ARG A O   1 
ATOM   1455 C CB  . ARG A 1 189 ? -19.455 -20.873 41.914 1.00 18.31 ? 189  ARG A CB  1 
ATOM   1456 C CG  . ARG A 1 189 ? -19.398 -21.087 43.429 1.00 16.80 ? 189  ARG A CG  1 
ATOM   1457 C CD  . ARG A 1 189 ? -20.768 -21.159 44.059 1.00 22.84 ? 189  ARG A CD  1 
ATOM   1458 N NE  . ARG A 1 189 ? -21.552 -22.274 43.550 1.00 23.65 ? 189  ARG A NE  1 
ATOM   1459 C CZ  . ARG A 1 189 ? -21.611 -23.486 44.099 1.00 28.01 ? 189  ARG A CZ  1 
ATOM   1460 N NH1 . ARG A 1 189 ? -20.944 -23.765 45.210 1.00 28.26 ? 189  ARG A NH1 1 
ATOM   1461 N NH2 . ARG A 1 189 ? -22.364 -24.429 43.538 1.00 30.29 ? 189  ARG A NH2 1 
ATOM   1462 N N   . HIS A 1 190 ? -16.242 -21.865 42.382 1.00 20.84 ? 190  HIS A N   1 
ATOM   1463 C CA  . HIS A 1 190 ? -15.361 -23.004 42.580 1.00 23.00 ? 190  HIS A CA  1 
ATOM   1464 C C   . HIS A 1 190 ? -16.053 -24.198 43.135 1.00 25.21 ? 190  HIS A C   1 
ATOM   1465 O O   . HIS A 1 190 ? -16.675 -24.121 44.188 1.00 25.35 ? 190  HIS A O   1 
ATOM   1466 C CB  . HIS A 1 190 ? -14.214 -22.653 43.494 1.00 23.07 ? 190  HIS A CB  1 
ATOM   1467 C CG  . HIS A 1 190 ? -13.032 -22.172 42.746 1.00 22.20 ? 190  HIS A CG  1 
ATOM   1468 N ND1 . HIS A 1 190 ? -12.761 -20.836 42.576 1.00 25.13 ? 190  HIS A ND1 1 
ATOM   1469 C CD2 . HIS A 1 190 ? -12.100 -22.843 42.041 1.00 23.46 ? 190  HIS A CD2 1 
ATOM   1470 C CE1 . HIS A 1 190 ? -11.662 -20.702 41.859 1.00 23.91 ? 190  HIS A CE1 1 
ATOM   1471 N NE2 . HIS A 1 190 ? -11.239 -21.907 41.525 1.00 26.13 ? 190  HIS A NE2 1 
ATOM   1472 N N   . ASP A 1 191 ? -15.978 -25.263 42.333 1.00 28.41 ? 191  ASP A N   1 
ATOM   1473 C CA  . ASP A 1 191 ? -15.986 -26.644 42.762 1.00 30.20 ? 191  ASP A CA  1 
ATOM   1474 C C   . ASP A 1 191 ? -15.077 -26.830 43.995 1.00 29.95 ? 191  ASP A C   1 
ATOM   1475 O O   . ASP A 1 191 ? -13.841 -27.052 43.852 1.00 29.32 ? 191  ASP A O   1 
ATOM   1476 C CB  . ASP A 1 191 ? -15.491 -27.525 41.600 1.00 31.51 ? 191  ASP A CB  1 
ATOM   1477 C CG  . ASP A 1 191 ? -15.664 -28.992 41.889 1.00 34.22 ? 191  ASP A CG  1 
ATOM   1478 O OD1 . ASP A 1 191 ? -16.198 -29.265 42.987 1.00 36.01 ? 191  ASP A OD1 1 
ATOM   1479 O OD2 . ASP A 1 191 ? -15.307 -29.854 41.037 1.00 36.90 ? 191  ASP A OD2 1 
ATOM   1480 N N   . MET A 1 192 ? -15.712 -26.711 45.179 1.00 29.32 ? 192  MET A N   1 
ATOM   1481 C CA  . MET A 1 192 ? -15.091 -26.942 46.493 1.00 28.72 ? 192  MET A CA  1 
ATOM   1482 C C   . MET A 1 192 ? -14.954 -28.418 46.782 1.00 29.02 ? 192  MET A C   1 
ATOM   1483 O O   . MET A 1 192 ? -14.544 -28.809 47.856 1.00 29.52 ? 192  MET A O   1 
ATOM   1484 C CB  . MET A 1 192 ? -15.871 -26.279 47.639 1.00 28.83 ? 192  MET A CB  1 
ATOM   1485 C CG  . MET A 1 192 ? -15.801 -24.747 47.695 1.00 26.66 ? 192  MET A CG  1 
ATOM   1486 S SD  . MET A 1 192 ? -14.122 -24.117 47.498 1.00 22.69 ? 192  MET A SD  1 
ATOM   1487 C CE  . MET A 1 192 ? -13.410 -24.650 49.059 1.00 20.84 ? 192  MET A CE  1 
ATOM   1488 N N   . ASN A 1 193 ? -15.273 -29.255 45.813 1.00 29.02 ? 193  ASN A N   1 
ATOM   1489 C CA  . ASN A 1 193 ? -14.971 -30.634 45.972 1.00 28.92 ? 193  ASN A CA  1 
ATOM   1490 C C   . ASN A 1 193 ? -13.456 -30.727 45.821 1.00 28.09 ? 193  ASN A C   1 
ATOM   1491 O O   . ASN A 1 193 ? -12.791 -29.740 45.440 1.00 28.91 ? 193  ASN A O   1 
ATOM   1492 C CB  . ASN A 1 193 ? -15.787 -31.509 45.007 1.00 30.62 ? 193  ASN A CB  1 
ATOM   1493 C CG  . ASN A 1 193 ? -17.275 -31.631 45.426 1.00 33.88 ? 193  ASN A CG  1 
ATOM   1494 O OD1 . ASN A 1 193 ? -18.087 -32.208 44.690 1.00 41.19 ? 193  ASN A OD1 1 
ATOM   1495 N ND2 . ASN A 1 193 ? -17.631 -31.093 46.606 1.00 34.67 ? 193  ASN A ND2 1 
ATOM   1496 N N   . TRP A 1 194 ? -12.908 -31.867 46.188 1.00 25.07 ? 194  TRP A N   1 
ATOM   1497 C CA  . TRP A 1 194 ? -11.462 -32.041 46.306 1.00 22.90 ? 194  TRP A CA  1 
ATOM   1498 C C   . TRP A 1 194 ? -10.786 -31.663 45.000 1.00 22.46 ? 194  TRP A C   1 
ATOM   1499 O O   . TRP A 1 194 ? -10.933 -32.375 44.012 1.00 23.53 ? 194  TRP A O   1 
ATOM   1500 C CB  . TRP A 1 194 ? -11.187 -33.504 46.680 1.00 20.59 ? 194  TRP A CB  1 
ATOM   1501 C CG  . TRP A 1 194 ? -11.955 -33.931 47.925 1.00 18.12 ? 194  TRP A CG  1 
ATOM   1502 C CD1 . TRP A 1 194 ? -13.240 -34.433 47.983 1.00 19.02 ? 194  TRP A CD1 1 
ATOM   1503 C CD2 . TRP A 1 194 ? -11.486 -33.882 49.270 1.00 17.69 ? 194  TRP A CD2 1 
ATOM   1504 N NE1 . TRP A 1 194 ? -13.584 -34.689 49.286 1.00 18.65 ? 194  TRP A NE1 1 
ATOM   1505 C CE2 . TRP A 1 194 ? -12.528 -34.367 50.097 1.00 15.93 ? 194  TRP A CE2 1 
ATOM   1506 C CE3 . TRP A 1 194 ? -10.271 -33.490 49.862 1.00 12.61 ? 194  TRP A CE3 1 
ATOM   1507 C CZ2 . TRP A 1 194 ? -12.399 -34.464 51.476 1.00 15.27 ? 194  TRP A CZ2 1 
ATOM   1508 C CZ3 . TRP A 1 194 ? -10.146 -33.586 51.227 1.00 15.92 ? 194  TRP A CZ3 1 
ATOM   1509 C CH2 . TRP A 1 194 ? -11.213 -34.055 52.026 1.00 16.79 ? 194  TRP A CH2 1 
ATOM   1510 N N   . LYS A 1 195 ? -10.100 -30.517 44.986 1.00 21.92 ? 195  LYS A N   1 
ATOM   1511 C CA  . LYS A 1 195 ? -9.454  -29.963 43.771 1.00 20.97 ? 195  LYS A CA  1 
ATOM   1512 C C   . LYS A 1 195 ? -8.212  -29.200 44.120 1.00 19.45 ? 195  LYS A C   1 
ATOM   1513 O O   . LYS A 1 195 ? -8.235  -28.354 45.011 1.00 19.99 ? 195  LYS A O   1 
ATOM   1514 C CB  . LYS A 1 195 ? -10.382 -29.018 42.978 1.00 21.57 ? 195  LYS A CB  1 
ATOM   1515 C CG  . LYS A 1 195 ? -10.814 -29.521 41.593 1.00 24.34 ? 195  LYS A CG  1 
ATOM   1516 C CD  . LYS A 1 195 ? -9.676  -30.091 40.708 1.00 29.34 ? 195  LYS A CD  1 
ATOM   1517 C CE  . LYS A 1 195 ? -9.070  -29.091 39.736 1.00 28.20 ? 195  LYS A CE  1 
ATOM   1518 N NZ  . LYS A 1 195 ? -8.584  -29.737 38.461 1.00 29.88 ? 195  LYS A NZ  1 
ATOM   1519 N N   . THR A 1 196 ? -7.129  -29.506 43.427 1.00 17.41 ? 196  THR A N   1 
ATOM   1520 C CA  . THR A 1 196 ? -5.880  -28.763 43.550 1.00 15.80 ? 196  THR A CA  1 
ATOM   1521 C C   . THR A 1 196 ? -5.652  -27.941 42.287 1.00 15.35 ? 196  THR A C   1 
ATOM   1522 O O   . THR A 1 196 ? -5.716  -28.478 41.155 1.00 15.87 ? 196  THR A O   1 
ATOM   1523 C CB  . THR A 1 196 ? -4.683  -29.739 43.796 1.00 15.84 ? 196  THR A CB  1 
ATOM   1524 O OG1 . THR A 1 196 ? -4.975  -30.570 44.927 1.00 14.61 ? 196  THR A OG1 1 
ATOM   1525 C CG2 . THR A 1 196 ? -3.388  -28.980 44.074 1.00 16.37 ? 196  THR A CG2 1 
ATOM   1526 N N   . TRP A 1 197 ? -5.406  -26.643 42.478 1.00 14.48 ? 197  TRP A N   1 
ATOM   1527 C CA  . TRP A 1 197 ? -5.047  -25.726 41.404 1.00 13.75 ? 197  TRP A CA  1 
ATOM   1528 C C   . TRP A 1 197 ? -3.622  -25.288 41.597 1.00 13.62 ? 197  TRP A C   1 
ATOM   1529 O O   . TRP A 1 197 ? -3.335  -24.603 42.581 1.00 13.73 ? 197  TRP A O   1 
ATOM   1530 C CB  . TRP A 1 197 ? -5.962  -24.498 41.418 1.00 13.23 ? 197  TRP A CB  1 
ATOM   1531 C CG  . TRP A 1 197 ? -7.378  -24.864 41.095 1.00 13.32 ? 197  TRP A CG  1 
ATOM   1532 C CD1 . TRP A 1 197 ? -8.400  -25.050 41.985 1.00 15.90 ? 197  TRP A CD1 1 
ATOM   1533 C CD2 . TRP A 1 197 ? -7.908  -25.156 39.803 1.00 13.98 ? 197  TRP A CD2 1 
ATOM   1534 N NE1 . TRP A 1 197 ? -9.561  -25.421 41.311 1.00 16.48 ? 197  TRP A NE1 1 
ATOM   1535 C CE2 . TRP A 1 197 ? -9.281  -25.493 39.974 1.00 15.03 ? 197  TRP A CE2 1 
ATOM   1536 C CE3 . TRP A 1 197 ? -7.357  -25.184 38.506 1.00 12.50 ? 197  TRP A CE3 1 
ATOM   1537 C CZ2 . TRP A 1 197 ? -10.109 -25.810 38.901 1.00 15.28 ? 197  TRP A CZ2 1 
ATOM   1538 C CZ3 . TRP A 1 197 ? -8.182  -25.501 37.438 1.00 14.09 ? 197  TRP A CZ3 1 
ATOM   1539 C CH2 . TRP A 1 197 ? -9.553  -25.793 37.643 1.00 14.74 ? 197  TRP A CH2 1 
ATOM   1540 N N   . PRO A 1 198 ? -2.729  -25.681 40.668 1.00 14.43 ? 198  PRO A N   1 
ATOM   1541 C CA  . PRO A 1 198 ? -1.353  -25.227 40.700 1.00 14.69 ? 198  PRO A CA  1 
ATOM   1542 C C   . PRO A 1 198 ? -1.200  -23.828 40.126 1.00 15.35 ? 198  PRO A C   1 
ATOM   1543 O O   . PRO A 1 198 ? -1.934  -23.437 39.198 1.00 16.32 ? 198  PRO A O   1 
ATOM   1544 C CB  . PRO A 1 198 ? -0.633  -26.254 39.819 1.00 15.11 ? 198  PRO A CB  1 
ATOM   1545 C CG  . PRO A 1 198 ? -1.663  -26.640 38.792 1.00 14.90 ? 198  PRO A CG  1 
ATOM   1546 C CD  . PRO A 1 198 ? -2.974  -26.624 39.548 1.00 13.98 ? 198  PRO A CD  1 
ATOM   1547 N N   . ILE A 1 199 ? -0.264  -23.074 40.694 1.00 15.07 ? 199  ILE A N   1 
ATOM   1548 C CA  . ILE A 1 199 ? 0.011   -21.706 40.299 1.00 14.86 ? 199  ILE A CA  1 
ATOM   1549 C C   . ILE A 1 199 ? 1.538   -21.518 40.075 1.00 15.94 ? 199  ILE A C   1 
ATOM   1550 O O   . ILE A 1 199 ? 2.320   -21.537 41.002 1.00 15.06 ? 199  ILE A O   1 
ATOM   1551 C CB  . ILE A 1 199 ? -0.543  -20.689 41.354 1.00 15.24 ? 199  ILE A CB  1 
ATOM   1552 C CG1 . ILE A 1 199 ? -2.073  -20.862 41.543 1.00 15.12 ? 199  ILE A CG1 1 
ATOM   1553 C CG2 . ILE A 1 199 ? -0.244  -19.244 40.934 1.00 14.64 ? 199  ILE A CG2 1 
ATOM   1554 C CD1 . ILE A 1 199 ? -2.673  -19.972 42.638 1.00 14.25 ? 199  ILE A CD1 1 
ATOM   1555 N N   . PHE A 1 200 ? 1.932   -21.350 38.819 1.00 16.82 ? 200  PHE A N   1 
ATOM   1556 C CA  . PHE A 1 200 ? 3.320   -21.050 38.453 1.00 17.37 ? 200  PHE A CA  1 
ATOM   1557 C C   . PHE A 1 200 ? 3.275   -20.633 37.015 1.00 16.36 ? 200  PHE A C   1 
ATOM   1558 O O   . PHE A 1 200 ? 2.810   -21.398 36.169 1.00 17.40 ? 200  PHE A O   1 
ATOM   1559 C CB  . PHE A 1 200 ? 4.196   -22.310 38.629 1.00 17.31 ? 200  PHE A CB  1 
ATOM   1560 C CG  . PHE A 1 200 ? 5.664   -22.068 38.491 1.00 20.05 ? 200  PHE A CG  1 
ATOM   1561 C CD1 . PHE A 1 200 ? 6.355   -21.330 39.441 1.00 19.24 ? 200  PHE A CD1 1 
ATOM   1562 C CD2 . PHE A 1 200 ? 6.367   -22.629 37.427 1.00 20.26 ? 200  PHE A CD2 1 
ATOM   1563 C CE1 . PHE A 1 200 ? 7.728   -21.142 39.334 1.00 20.37 ? 200  PHE A CE1 1 
ATOM   1564 C CE2 . PHE A 1 200 ? 7.737   -22.429 37.310 1.00 19.33 ? 200  PHE A CE2 1 
ATOM   1565 C CZ  . PHE A 1 200 ? 8.408   -21.691 38.259 1.00 18.98 ? 200  PHE A CZ  1 
ATOM   1566 N N   . ASN A 1 201 ? 3.754   -19.419 36.737 1.00 16.54 ? 201  ASN A N   1 
ATOM   1567 C CA  . ASN A 1 201 ? 3.647   -18.817 35.421 1.00 16.23 ? 201  ASN A CA  1 
ATOM   1568 C C   . ASN A 1 201 ? 4.282   -19.696 34.364 1.00 16.80 ? 201  ASN A C   1 
ATOM   1569 O O   . ASN A 1 201 ? 5.511   -20.006 34.390 1.00 15.93 ? 201  ASN A O   1 
ATOM   1570 C CB  . ASN A 1 201 ? 4.222   -17.392 35.422 1.00 15.98 ? 201  ASN A CB  1 
ATOM   1571 C CG  . ASN A 1 201 ? 3.398   -16.447 36.301 1.00 18.11 ? 201  ASN A CG  1 
ATOM   1572 O OD1 . ASN A 1 201 ? 2.393   -16.868 36.909 1.00 17.40 ? 201  ASN A OD1 1 
ATOM   1573 N ND2 . ASN A 1 201 ? 3.790   -15.183 36.355 1.00 14.37 ? 201  ASN A ND2 1 
ATOM   1574 N N   . ARG A 1 202 ? 3.443   -20.116 33.443 1.00 15.19 ? 202  ARG A N   1 
ATOM   1575 C CA  . ARG A 1 202 ? 3.864   -21.116 32.454 1.00 15.55 ? 202  ARG A CA  1 
ATOM   1576 C C   . ARG A 1 202 ? 3.199   -20.874 31.102 1.00 16.44 ? 202  ARG A C   1 
ATOM   1577 O O   . ARG A 1 202 ? 1.972   -20.588 31.010 1.00 14.97 ? 202  ARG A O   1 
ATOM   1578 C CB  . ARG A 1 202 ? 3.547   -22.527 32.994 1.00 15.45 ? 202  ARG A CB  1 
ATOM   1579 C CG  . ARG A 1 202 ? 3.537   -23.667 32.015 1.00 14.44 ? 202  ARG A CG  1 
ATOM   1580 C CD  . ARG A 1 202 ? 4.948   -24.050 31.546 1.00 18.26 ? 202  ARG A CD  1 
ATOM   1581 N NE  . ARG A 1 202 ? 4.907   -24.922 30.363 1.00 18.73 ? 202  ARG A NE  1 
ATOM   1582 C CZ  . ARG A 1 202 ? 5.000   -26.245 30.422 1.00 19.91 ? 202  ARG A CZ  1 
ATOM   1583 N NH1 . ARG A 1 202 ? 5.126   -26.827 31.602 1.00 18.84 ? 202  ARG A NH1 1 
ATOM   1584 N NH2 . ARG A 1 202 ? 4.957   -26.981 29.309 1.00 18.80 ? 202  ARG A NH2 1 
ATOM   1585 N N   . ASP A 1 203 ? 4.018   -21.001 30.057 1.00 17.10 ? 203  ASP A N   1 
ATOM   1586 C CA  . ASP A 1 203 ? 3.549   -21.077 28.685 1.00 18.18 ? 203  ASP A CA  1 
ATOM   1587 C C   . ASP A 1 203 ? 2.868   -22.415 28.455 1.00 19.14 ? 203  ASP A C   1 
ATOM   1588 O O   . ASP A 1 203 ? 3.534   -23.453 28.313 1.00 18.05 ? 203  ASP A O   1 
ATOM   1589 C CB  . ASP A 1 203 ? 4.733   -20.884 27.732 1.00 18.57 ? 203  ASP A CB  1 
ATOM   1590 C CG  . ASP A 1 203 ? 4.316   -20.741 26.283 1.00 20.09 ? 203  ASP A CG  1 
ATOM   1591 O OD1 . ASP A 1 203 ? 3.200   -21.186 25.915 1.00 24.10 ? 203  ASP A OD1 1 
ATOM   1592 O OD2 . ASP A 1 203 ? 5.123   -20.189 25.499 1.00 20.95 ? 203  ASP A OD2 1 
ATOM   1593 N N   . THR A 1 204 ? 1.529   -22.391 28.469 1.00 19.85 ? 204  THR A N   1 
ATOM   1594 C CA  . THR A 1 204 ? 0.708   -23.584 28.309 1.00 21.83 ? 204  THR A CA  1 
ATOM   1595 C C   . THR A 1 204 ? -0.649  -23.213 27.760 1.00 21.37 ? 204  THR A C   1 
ATOM   1596 O O   . THR A 1 204 ? -1.055  -22.068 27.837 1.00 22.08 ? 204  THR A O   1 
ATOM   1597 C CB  . THR A 1 204 ? 0.447   -24.362 29.620 1.00 21.83 ? 204  THR A CB  1 
ATOM   1598 O OG1 . THR A 1 204 ? -0.516  -23.681 30.426 1.00 28.81 ? 204  THR A OG1 1 
ATOM   1599 C CG2 . THR A 1 204 ? 1.675   -24.549 30.411 1.00 25.70 ? 204  THR A CG2 1 
ATOM   1600 N N   . THR A 1 205 ? -1.355  -24.201 27.232 1.00 21.36 ? 205  THR A N   1 
ATOM   1601 C CA  . THR A 1 205 ? -2.597  -23.966 26.547 1.00 21.70 ? 205  THR A CA  1 
ATOM   1602 C C   . THR A 1 205 ? -3.771  -23.852 27.521 1.00 21.27 ? 205  THR A C   1 
ATOM   1603 O O   . THR A 1 205 ? -4.018  -24.749 28.306 1.00 20.16 ? 205  THR A O   1 
ATOM   1604 C CB  . THR A 1 205 ? -2.883  -25.081 25.512 1.00 22.13 ? 205  THR A CB  1 
ATOM   1605 O OG1 . THR A 1 205 ? -1.726  -25.275 24.684 1.00 24.00 ? 205  THR A OG1 1 
ATOM   1606 C CG2 . THR A 1 205 ? -4.105  -24.723 24.639 1.00 18.94 ? 205  THR A CG2 1 
ATOM   1607 N N   . PRO A 1 206 ? -4.511  -22.745 27.450 1.00 21.91 ? 206  PRO A N   1 
ATOM   1608 C CA  . PRO A 1 206 ? -5.782  -22.749 28.179 1.00 22.14 ? 206  PRO A CA  1 
ATOM   1609 C C   . PRO A 1 206 ? -6.734  -23.757 27.579 1.00 22.23 ? 206  PRO A C   1 
ATOM   1610 O O   . PRO A 1 206 ? -7.403  -23.458 26.614 1.00 24.35 ? 206  PRO A O   1 
ATOM   1611 C CB  . PRO A 1 206 ? -6.303  -21.308 28.018 1.00 21.97 ? 206  PRO A CB  1 
ATOM   1612 C CG  . PRO A 1 206 ? -5.585  -20.753 26.819 1.00 22.65 ? 206  PRO A CG  1 
ATOM   1613 C CD  . PRO A 1 206 ? -4.247  -21.466 26.764 1.00 22.41 ? 206  PRO A CD  1 
ATOM   1614 N N   . ASN A 1 207 ? -6.788  -24.956 28.143 1.00 22.71 ? 207  ASN A N   1 
ATOM   1615 C CA  . ASN A 1 207 ? -7.711  -25.988 27.667 1.00 22.46 ? 207  ASN A CA  1 
ATOM   1616 C C   . ASN A 1 207 ? -8.472  -26.596 28.834 1.00 22.69 ? 207  ASN A C   1 
ATOM   1617 O O   . ASN A 1 207 ? -8.424  -26.075 29.954 1.00 22.63 ? 207  ASN A O   1 
ATOM   1618 C CB  . ASN A 1 207 ? -6.965  -27.072 26.881 1.00 22.78 ? 207  ASN A CB  1 
ATOM   1619 C CG  . ASN A 1 207 ? -5.750  -27.630 27.632 1.00 22.02 ? 207  ASN A CG  1 
ATOM   1620 O OD1 . ASN A 1 207 ? -5.683  -27.600 28.858 1.00 22.96 ? 207  ASN A OD1 1 
ATOM   1621 N ND2 . ASN A 1 207 ? -4.802  -28.153 26.892 1.00 22.07 ? 207  ASN A ND2 1 
ATOM   1622 N N   . GLY A 1 208 ? -9.164  -27.696 28.571 1.00 22.66 ? 208  GLY A N   1 
ATOM   1623 C CA  . GLY A 1 208 ? -9.877  -28.460 29.598 1.00 22.28 ? 208  GLY A CA  1 
ATOM   1624 C C   . GLY A 1 208 ? -9.057  -29.163 30.671 1.00 22.25 ? 208  GLY A C   1 
ATOM   1625 O O   . GLY A 1 208 ? -9.631  -29.746 31.578 1.00 22.07 ? 208  GLY A O   1 
ATOM   1626 N N   . ASN A 1 209 ? -7.723  -29.105 30.600 1.00 22.83 ? 209  ASN A N   1 
ATOM   1627 C CA  . ASN A 1 209 ? -6.880  -29.825 31.578 1.00 22.77 ? 209  ASN A CA  1 
ATOM   1628 C C   . ASN A 1 209 ? -6.688  -29.189 32.964 1.00 22.53 ? 209  ASN A C   1 
ATOM   1629 O O   . ASN A 1 209 ? -6.196  -29.842 33.899 1.00 23.54 ? 209  ASN A O   1 
ATOM   1630 C CB  . ASN A 1 209 ? -5.527  -30.245 30.963 1.00 23.53 ? 209  ASN A CB  1 
ATOM   1631 C CG  . ASN A 1 209 ? -5.642  -31.498 30.088 1.00 26.38 ? 209  ASN A CG  1 
ATOM   1632 O OD1 . ASN A 1 209 ? -6.019  -32.575 30.574 1.00 28.53 ? 209  ASN A OD1 1 
ATOM   1633 N ND2 . ASN A 1 209 ? -5.306  -31.368 28.793 1.00 27.68 ? 209  ASN A ND2 1 
ATOM   1634 N N   . GLY A 1 210 ? -7.051  -27.922 33.115 1.00 21.59 ? 210  GLY A N   1 
ATOM   1635 C CA  . GLY A 1 210 ? -6.928  -27.269 34.416 1.00 20.08 ? 210  GLY A CA  1 
ATOM   1636 C C   . GLY A 1 210 ? -5.495  -27.108 34.928 1.00 19.59 ? 210  GLY A C   1 
ATOM   1637 O O   . GLY A 1 210 ? -5.248  -27.229 36.134 1.00 19.77 ? 210  GLY A O   1 
ATOM   1638 N N   . THR A 1 211 ? -4.555  -26.824 34.033 1.00 17.97 ? 211  THR A N   1 
ATOM   1639 C CA  . THR A 1 211 ? -3.151  -26.640 34.447 1.00 17.37 ? 211  THR A CA  1 
ATOM   1640 C C   . THR A 1 211 ? -2.896  -25.198 34.899 1.00 16.73 ? 211  THR A C   1 
ATOM   1641 O O   . THR A 1 211 ? -3.745  -24.301 34.700 1.00 15.21 ? 211  THR A O   1 
ATOM   1642 C CB  . THR A 1 211 ? -2.162  -26.957 33.303 1.00 16.44 ? 211  THR A CB  1 
ATOM   1643 O OG1 . THR A 1 211 ? -2.325  -25.985 32.270 1.00 19.55 ? 211  THR A OG1 1 
ATOM   1644 C CG2 . THR A 1 211 ? -2.410  -28.289 32.706 1.00 17.38 ? 211  THR A CG2 1 
ATOM   1645 N N   . ASN A 1 212 ? -1.708  -24.972 35.473 1.00 15.13 ? 212  ASN A N   1 
ATOM   1646 C CA  . ASN A 1 212 ? -1.230  -23.636 35.668 1.00 15.18 ? 212  ASN A CA  1 
ATOM   1647 C C   . ASN A 1 212 ? -1.046  -22.969 34.300 1.00 14.90 ? 212  ASN A C   1 
ATOM   1648 O O   . ASN A 1 212 ? -0.652  -23.623 33.330 1.00 16.45 ? 212  ASN A O   1 
ATOM   1649 C CB  . ASN A 1 212 ? 0.078   -23.639 36.457 1.00 14.90 ? 212  ASN A CB  1 
ATOM   1650 C CG  . ASN A 1 212 ? 1.086   -24.630 35.920 1.00 15.90 ? 212  ASN A CG  1 
ATOM   1651 O OD1 . ASN A 1 212 ? 0.792   -25.822 35.799 1.00 13.49 ? 212  ASN A OD1 1 
ATOM   1652 N ND2 . ASN A 1 212 ? 2.297   -24.156 35.659 1.00 13.84 ? 212  ASN A ND2 1 
ATOM   1653 N N   . LEU A 1 213 ? -1.364  -21.682 34.203 1.00 13.48 ? 213  LEU A N   1 
ATOM   1654 C CA  . LEU A 1 213 ? -1.205  -20.955 32.953 1.00 13.05 ? 213  LEU A CA  1 
ATOM   1655 C C   . LEU A 1 213 ? -0.214  -19.794 33.105 1.00 14.19 ? 213  LEU A C   1 
ATOM   1656 O O   . LEU A 1 213 ? 0.737   -19.876 33.895 1.00 14.46 ? 213  LEU A O   1 
ATOM   1657 C CB  . LEU A 1 213 ? -2.595  -20.578 32.343 1.00 14.10 ? 213  LEU A CB  1 
ATOM   1658 C CG  . LEU A 1 213 ? -3.569  -21.754 32.116 1.00 9.05  ? 213  LEU A CG  1 
ATOM   1659 C CD1 . LEU A 1 213 ? -5.041  -21.259 31.738 1.00 11.85 ? 213  LEU A CD1 1 
ATOM   1660 C CD2 . LEU A 1 213 ? -3.113  -22.755 31.096 1.00 9.51  ? 213  LEU A CD2 1 
ATOM   1661 N N   . TYR A 1 214 ? -0.422  -18.724 32.357 1.00 14.46 ? 214  TYR A N   1 
ATOM   1662 C CA  . TYR A 1 214 ? 0.539   -17.639 32.206 1.00 14.28 ? 214  TYR A CA  1 
ATOM   1663 C C   . TYR A 1 214 ? 0.785   -16.717 33.401 1.00 14.29 ? 214  TYR A C   1 
ATOM   1664 O O   . TYR A 1 214 ? 1.921   -16.177 33.568 1.00 13.56 ? 214  TYR A O   1 
ATOM   1665 C CB  . TYR A 1 214 ? 0.128   -16.757 31.029 1.00 14.53 ? 214  TYR A CB  1 
ATOM   1666 C CG  . TYR A 1 214 ? -0.360  -17.503 29.836 1.00 15.31 ? 214  TYR A CG  1 
ATOM   1667 C CD1 . TYR A 1 214 ? 0.514   -18.213 29.030 1.00 15.82 ? 214  TYR A CD1 1 
ATOM   1668 C CD2 . TYR A 1 214 ? -1.702  -17.474 29.495 1.00 15.18 ? 214  TYR A CD2 1 
ATOM   1669 C CE1 . TYR A 1 214 ? 0.062   -18.889 27.914 1.00 16.61 ? 214  TYR A CE1 1 
ATOM   1670 C CE2 . TYR A 1 214 ? -2.163  -18.133 28.399 1.00 16.22 ? 214  TYR A CE2 1 
ATOM   1671 C CZ  . TYR A 1 214 ? -1.291  -18.840 27.616 1.00 16.49 ? 214  TYR A CZ  1 
ATOM   1672 O OH  . TYR A 1 214 ? -1.777  -19.478 26.500 1.00 17.61 ? 214  TYR A OH  1 
ATOM   1673 N N   . GLY A 1 215 ? -0.256  -16.536 34.218 1.00 12.34 ? 215  GLY A N   1 
ATOM   1674 C CA  . GLY A 1 215 ? -0.218  -15.657 35.376 1.00 11.70 ? 215  GLY A CA  1 
ATOM   1675 C C   . GLY A 1 215 ? -0.374  -16.324 36.723 1.00 11.57 ? 215  GLY A C   1 
ATOM   1676 O O   . GLY A 1 215 ? -0.691  -17.491 36.816 1.00 12.68 ? 215  GLY A O   1 
ATOM   1677 N N   . ALA A 1 216 ? -0.136  -15.561 37.775 1.00 12.58 ? 216  ALA A N   1 
ATOM   1678 C CA  . ALA A 1 216 ? -0.170  -16.036 39.139 1.00 13.95 ? 216  ALA A CA  1 
ATOM   1679 C C   . ALA A 1 216 ? -1.079  -15.107 39.924 1.00 14.01 ? 216  ALA A C   1 
ATOM   1680 O O   . ALA A 1 216 ? -0.790  -13.933 40.093 1.00 15.11 ? 216  ALA A O   1 
ATOM   1681 C CB  . ALA A 1 216 ? 1.231   -16.021 39.764 1.00 13.60 ? 216  ALA A CB  1 
ATOM   1682 N N   . GLN A 1 217 ? -2.185  -15.647 40.388 1.00 14.78 ? 217  GLN A N   1 
ATOM   1683 C CA  . GLN A 1 217 ? -3.230  -14.832 41.071 1.00 14.46 ? 217  GLN A CA  1 
ATOM   1684 C C   . GLN A 1 217 ? -3.742  -15.627 42.267 1.00 14.14 ? 217  GLN A C   1 
ATOM   1685 O O   . GLN A 1 217 ? -4.439  -16.603 42.108 1.00 14.97 ? 217  GLN A O   1 
ATOM   1686 C CB  . GLN A 1 217 ? -4.354  -14.493 40.092 1.00 14.48 ? 217  GLN A CB  1 
ATOM   1687 C CG  . GLN A 1 217 ? -3.910  -13.691 38.816 1.00 14.70 ? 217  GLN A CG  1 
ATOM   1688 C CD  . GLN A 1 217 ? -3.390  -12.285 39.140 1.00 14.52 ? 217  GLN A CD  1 
ATOM   1689 O OE1 . GLN A 1 217 ? -3.631  -11.754 40.218 1.00 17.59 ? 217  GLN A OE1 1 
ATOM   1690 N NE2 . GLN A 1 217 ? -2.671  -11.687 38.210 1.00 16.53 ? 217  GLN A NE2 1 
ATOM   1691 N N   . THR A 1 218 ? -3.369  -15.227 43.473 1.00 15.69 ? 218  THR A N   1 
ATOM   1692 C CA  . THR A 1 218 ? -3.741  -16.009 44.652 1.00 16.41 ? 218  THR A CA  1 
ATOM   1693 C C   . THR A 1 218 ? -5.036  -15.497 45.295 1.00 16.80 ? 218  THR A C   1 
ATOM   1694 O O   . THR A 1 218 ? -5.575  -16.137 46.189 1.00 17.90 ? 218  THR A O   1 
ATOM   1695 C CB  . THR A 1 218 ? -2.641  -15.983 45.697 1.00 16.14 ? 218  THR A CB  1 
ATOM   1696 O OG1 . THR A 1 218 ? -2.465  -14.645 46.156 1.00 18.47 ? 218  THR A OG1 1 
ATOM   1697 C CG2 . THR A 1 218 ? -1.313  -16.470 45.110 1.00 14.89 ? 218  THR A CG2 1 
ATOM   1698 N N   . PHE A 1 219 ? -5.531  -14.358 44.835 1.00 16.39 ? 219  PHE A N   1 
ATOM   1699 C CA  . PHE A 1 219 ? -6.762  -13.780 45.401 1.00 15.09 ? 219  PHE A CA  1 
ATOM   1700 C C   . PHE A 1 219 ? -7.985  -14.678 45.182 1.00 15.40 ? 219  PHE A C   1 
ATOM   1701 O O   . PHE A 1 219 ? -8.213  -15.199 44.088 1.00 14.58 ? 219  PHE A O   1 
ATOM   1702 C CB  . PHE A 1 219 ? -7.013  -12.378 44.830 1.00 14.59 ? 219  PHE A CB  1 
ATOM   1703 C CG  . PHE A 1 219 ? -8.269  -11.701 45.370 1.00 15.12 ? 219  PHE A CG  1 
ATOM   1704 C CD1 . PHE A 1 219 ? -8.319  -11.254 46.693 1.00 14.01 ? 219  PHE A CD1 1 
ATOM   1705 C CD2 . PHE A 1 219 ? -9.401  -11.553 44.569 1.00 12.97 ? 219  PHE A CD2 1 
ATOM   1706 C CE1 . PHE A 1 219 ? -9.474  -10.647 47.204 1.00 15.93 ? 219  PHE A CE1 1 
ATOM   1707 C CE2 . PHE A 1 219 ? -10.556 -10.945 45.074 1.00 13.05 ? 219  PHE A CE2 1 
ATOM   1708 C CZ  . PHE A 1 219 ? -10.590 -10.498 46.382 1.00 13.52 ? 219  PHE A CZ  1 
ATOM   1709 N N   . PHE A 1 220 ? -8.768  -14.847 46.245 1.00 15.59 ? 220  PHE A N   1 
ATOM   1710 C CA  . PHE A 1 220 ? -10.112 -15.357 46.132 1.00 16.36 ? 220  PHE A CA  1 
ATOM   1711 C C   . PHE A 1 220 ? -11.036 -14.537 47.005 1.00 16.42 ? 220  PHE A C   1 
ATOM   1712 O O   . PHE A 1 220 ? -10.600 -13.944 47.996 1.00 17.27 ? 220  PHE A O   1 
ATOM   1713 C CB  . PHE A 1 220 ? -10.215 -16.857 46.452 1.00 16.41 ? 220  PHE A CB  1 
ATOM   1714 C CG  . PHE A 1 220 ? -10.144 -17.184 47.928 1.00 16.61 ? 220  PHE A CG  1 
ATOM   1715 C CD1 . PHE A 1 220 ? -11.299 -17.218 48.712 1.00 17.57 ? 220  PHE A CD1 1 
ATOM   1716 C CD2 . PHE A 1 220 ? -8.930  -17.466 48.525 1.00 14.59 ? 220  PHE A CD2 1 
ATOM   1717 C CE1 . PHE A 1 220 ? -11.248 -17.500 50.066 1.00 15.31 ? 220  PHE A CE1 1 
ATOM   1718 C CE2 . PHE A 1 220 ? -8.871  -17.762 49.875 1.00 14.59 ? 220  PHE A CE2 1 
ATOM   1719 C CZ  . PHE A 1 220 ? -10.050 -17.796 50.646 1.00 17.34 ? 220  PHE A CZ  1 
ATOM   1720 N N   . LEU A 1 221 ? -12.301 -14.527 46.608 1.00 16.08 ? 221  LEU A N   1 
ATOM   1721 C CA  . LEU A 1 221 ? -13.399 -13.815 47.266 1.00 15.92 ? 221  LEU A CA  1 
ATOM   1722 C C   . LEU A 1 221 ? -14.408 -14.890 47.669 1.00 15.57 ? 221  LEU A C   1 
ATOM   1723 O O   . LEU A 1 221 ? -14.624 -15.843 46.936 1.00 13.78 ? 221  LEU A O   1 
ATOM   1724 C CB  . LEU A 1 221 ? -14.060 -12.819 46.271 1.00 15.07 ? 221  LEU A CB  1 
ATOM   1725 C CG  . LEU A 1 221 ? -15.296 -11.946 46.598 1.00 17.05 ? 221  LEU A CG  1 
ATOM   1726 C CD1 . LEU A 1 221 ? -15.291 -10.729 45.675 1.00 17.75 ? 221  LEU A CD1 1 
ATOM   1727 C CD2 . LEU A 1 221 ? -16.636 -12.708 46.441 1.00 15.91 ? 221  LEU A CD2 1 
ATOM   1728 N N   . CYS A 1 222 ? -15.041 -14.710 48.831 1.00 16.64 ? 222  CYS A N   1 
ATOM   1729 C CA  . CYS A 1 222 ? -16.058 -15.640 49.302 1.00 16.19 ? 222  CYS A CA  1 
ATOM   1730 C C   . CYS A 1 222 ? -17.335 -14.848 49.623 1.00 15.69 ? 222  CYS A C   1 
ATOM   1731 O O   . CYS A 1 222 ? -17.312 -13.943 50.425 1.00 15.41 ? 222  CYS A O   1 
ATOM   1732 C CB  . CYS A 1 222 ? -15.557 -16.392 50.534 1.00 16.67 ? 222  CYS A CB  1 
ATOM   1733 S SG  . CYS A 1 222 ? -16.724 -17.551 51.274 1.00 18.69 ? 222  CYS A SG  1 
ATOM   1734 N N   . LEU A 1 223 ? -18.428 -15.179 48.963 1.00 15.21 ? 223  LEU A N   1 
ATOM   1735 C CA  . LEU A 1 223 ? -19.723 -14.620 49.368 1.00 14.74 ? 223  LEU A CA  1 
ATOM   1736 C C   . LEU A 1 223 ? -20.247 -15.465 50.541 1.00 14.34 ? 223  LEU A C   1 
ATOM   1737 O O   . LEU A 1 223 ? -20.600 -16.622 50.376 1.00 13.53 ? 223  LEU A O   1 
ATOM   1738 C CB  . LEU A 1 223 ? -20.698 -14.571 48.184 1.00 13.76 ? 223  LEU A CB  1 
ATOM   1739 C CG  . LEU A 1 223 ? -22.175 -14.273 48.552 1.00 14.23 ? 223  LEU A CG  1 
ATOM   1740 C CD1 . LEU A 1 223 ? -22.364 -12.874 49.069 1.00 9.01  ? 223  LEU A CD1 1 
ATOM   1741 C CD2 . LEU A 1 223 ? -23.087 -14.530 47.370 1.00 14.35 ? 223  LEU A CD2 1 
ATOM   1742 N N   . GLU A 1 224 ? -20.268 -14.875 51.728 1.00 15.56 ? 224  GLU A N   1 
ATOM   1743 C CA  . GLU A 1 224 ? -20.643 -15.583 52.957 1.00 17.45 ? 224  GLU A CA  1 
ATOM   1744 C C   . GLU A 1 224 ? -22.087 -16.074 52.967 1.00 17.79 ? 224  GLU A C   1 
ATOM   1745 O O   . GLU A 1 224 ? -22.336 -17.206 53.353 1.00 17.69 ? 224  GLU A O   1 
ATOM   1746 C CB  . GLU A 1 224 ? -20.401 -14.687 54.180 1.00 17.76 ? 224  GLU A CB  1 
ATOM   1747 C CG  . GLU A 1 224 ? -18.920 -14.335 54.338 1.00 18.07 ? 224  GLU A CG  1 
ATOM   1748 C CD  . GLU A 1 224 ? -18.691 -13.127 55.193 1.00 19.51 ? 224  GLU A CD  1 
ATOM   1749 O OE1 . GLU A 1 224 ? -19.329 -12.968 56.273 1.00 19.37 ? 224  GLU A OE1 1 
ATOM   1750 O OE2 . GLU A 1 224 ? -17.816 -12.344 54.792 1.00 22.46 ? 224  GLU A OE2 1 
ATOM   1751 N N   . ASP A 1 225 ? -23.017 -15.210 52.552 1.00 20.12 ? 225  ASP A N   1 
ATOM   1752 C CA  . ASP A 1 225 ? -24.473 -15.488 52.585 1.00 20.48 ? 225  ASP A CA  1 
ATOM   1753 C C   . ASP A 1 225 ? -25.284 -14.503 51.713 1.00 19.84 ? 225  ASP A C   1 
ATOM   1754 O O   . ASP A 1 225 ? -24.720 -13.614 51.078 1.00 17.94 ? 225  ASP A O   1 
ATOM   1755 C CB  . ASP A 1 225 ? -24.988 -15.535 54.055 1.00 22.47 ? 225  ASP A CB  1 
ATOM   1756 C CG  . ASP A 1 225 ? -24.779 -14.227 54.833 1.00 25.82 ? 225  ASP A CG  1 
ATOM   1757 O OD1 . ASP A 1 225 ? -25.245 -13.138 54.392 1.00 28.15 ? 225  ASP A OD1 1 
ATOM   1758 O OD2 . ASP A 1 225 ? -24.174 -14.279 55.941 1.00 30.94 ? 225  ASP A OD2 1 
ATOM   1759 N N   . ALA A 1 226 ? -26.613 -14.660 51.682 1.00 19.84 ? 226  ALA A N   1 
ATOM   1760 C CA  . ALA A 1 226 ? -27.473 -13.831 50.837 1.00 19.31 ? 226  ALA A CA  1 
ATOM   1761 C C   . ALA A 1 226 ? -27.504 -12.353 51.241 1.00 19.43 ? 226  ALA A C   1 
ATOM   1762 O O   . ALA A 1 226 ? -27.933 -11.507 50.476 1.00 19.09 ? 226  ALA A O   1 
ATOM   1763 C CB  . ALA A 1 226 ? -28.949 -14.437 50.782 1.00 19.66 ? 226  ALA A CB  1 
ATOM   1764 N N   . SER A 1 227 ? -27.046 -12.014 52.437 1.00 19.59 ? 227  SER A N   1 
ATOM   1765 C CA  . SER A 1 227 ? -26.957 -10.606 52.804 1.00 20.24 ? 227  SER A CA  1 
ATOM   1766 C C   . SER A 1 227 ? -25.969 -9.803  51.961 1.00 19.62 ? 227  SER A C   1 
ATOM   1767 O O   . SER A 1 227 ? -26.057 -8.573  51.924 1.00 18.96 ? 227  SER A O   1 
ATOM   1768 C CB  . SER A 1 227 ? -26.647 -10.413 54.291 1.00 20.82 ? 227  SER A CB  1 
ATOM   1769 O OG  . SER A 1 227 ? -25.359 -10.908 54.609 1.00 24.52 ? 227  SER A OG  1 
ATOM   1770 N N   . GLY A 1 228 ? -25.041 -10.493 51.284 1.00 19.69 ? 228  GLY A N   1 
ATOM   1771 C CA  . GLY A 1 228 ? -23.982 -9.821  50.541 1.00 18.02 ? 228  GLY A CA  1 
ATOM   1772 C C   . GLY A 1 228 ? -22.650 -9.809  51.254 1.00 17.98 ? 228  GLY A C   1 
ATOM   1773 O O   . GLY A 1 228 ? -21.607 -9.616  50.619 1.00 15.86 ? 228  GLY A O   1 
ATOM   1774 N N   . LEU A 1 229 ? -22.668 -10.023 52.572 1.00 17.90 ? 229  LEU A N   1 
ATOM   1775 C CA  . LEU A 1 229 ? -21.416 -10.069 53.342 1.00 16.43 ? 229  LEU A CA  1 
ATOM   1776 C C   . LEU A 1 229 ? -20.473 -11.086 52.701 1.00 15.40 ? 229  LEU A C   1 
ATOM   1777 O O   . LEU A 1 229 ? -20.851 -12.211 52.347 1.00 14.86 ? 229  LEU A O   1 
ATOM   1778 C CB  . LEU A 1 229 ? -21.621 -10.363 54.844 1.00 16.54 ? 229  LEU A CB  1 
ATOM   1779 C CG  . LEU A 1 229 ? -22.527 -9.422  55.665 1.00 17.66 ? 229  LEU A CG  1 
ATOM   1780 C CD1 . LEU A 1 229 ? -22.737 -9.950  57.085 1.00 16.89 ? 229  LEU A CD1 1 
ATOM   1781 C CD2 . LEU A 1 229 ? -22.017 -7.997  55.731 1.00 17.98 ? 229  LEU A CD2 1 
ATOM   1782 N N   . SER A 1 230 ? -19.238 -10.654 52.549 1.00 14.08 ? 230  SER A N   1 
ATOM   1783 C CA  . SER A 1 230 ? -18.274 -11.296 51.667 1.00 13.62 ? 230  SER A CA  1 
ATOM   1784 C C   . SER A 1 230 ? -16.924 -10.946 52.257 1.00 13.22 ? 230  SER A C   1 
ATOM   1785 O O   . SER A 1 230 ? -16.829 -9.995  52.984 1.00 11.68 ? 230  SER A O   1 
ATOM   1786 C CB  . SER A 1 230 ? -18.363 -10.657 50.283 1.00 12.98 ? 230  SER A CB  1 
ATOM   1787 O OG  . SER A 1 230 ? -19.467 -11.119 49.560 1.00 15.63 ? 230  SER A OG  1 
ATOM   1788 N N   . PHE A 1 231 ? -15.889 -11.729 51.964 1.00 13.94 ? 231  PHE A N   1 
ATOM   1789 C CA  . PHE A 1 231 ? -14.552 -11.364 52.392 1.00 13.37 ? 231  PHE A CA  1 
ATOM   1790 C C   . PHE A 1 231 ? -13.607 -11.942 51.360 1.00 13.40 ? 231  PHE A C   1 
ATOM   1791 O O   . PHE A 1 231 ? -14.042 -12.652 50.450 1.00 12.75 ? 231  PHE A O   1 
ATOM   1792 C CB  . PHE A 1 231 ? -14.246 -11.878 53.811 1.00 14.34 ? 231  PHE A CB  1 
ATOM   1793 C CG  . PHE A 1 231 ? -13.897 -13.334 53.856 1.00 14.42 ? 231  PHE A CG  1 
ATOM   1794 C CD1 . PHE A 1 231 ? -12.565 -13.733 53.973 1.00 14.66 ? 231  PHE A CD1 1 
ATOM   1795 C CD2 . PHE A 1 231 ? -14.902 -14.310 53.761 1.00 13.88 ? 231  PHE A CD2 1 
ATOM   1796 C CE1 . PHE A 1 231 ? -12.227 -15.086 53.967 1.00 15.80 ? 231  PHE A CE1 1 
ATOM   1797 C CE2 . PHE A 1 231 ? -14.585 -15.637 53.802 1.00 16.77 ? 231  PHE A CE2 1 
ATOM   1798 C CZ  . PHE A 1 231 ? -13.232 -16.044 53.897 1.00 15.75 ? 231  PHE A CZ  1 
ATOM   1799 N N   . GLY A 1 232 ? -12.339 -11.539 51.422 1.00 12.42 ? 232  GLY A N   1 
ATOM   1800 C CA  . GLY A 1 232 ? -11.377 -12.043 50.452 1.00 11.81 ? 232  GLY A CA  1 
ATOM   1801 C C   . GLY A 1 232 ? -10.057 -12.340 51.133 1.00 11.73 ? 232  GLY A C   1 
ATOM   1802 O O   . GLY A 1 232 ? -9.817  -11.878 52.232 1.00 11.31 ? 232  GLY A O   1 
ATOM   1803 N N   . VAL A 1 233 ? -9.229  -13.167 50.508 1.00 12.09 ? 233  VAL A N   1 
ATOM   1804 C CA  . VAL A 1 233 ? -7.912  -13.517 51.068 1.00 12.69 ? 233  VAL A CA  1 
ATOM   1805 C C   . VAL A 1 233 ? -6.915  -13.352 49.950 1.00 13.14 ? 233  VAL A C   1 
ATOM   1806 O O   . VAL A 1 233 ? -7.188  -13.777 48.816 1.00 12.23 ? 233  VAL A O   1 
ATOM   1807 C CB  . VAL A 1 233 ? -7.849  -14.978 51.634 1.00 13.26 ? 233  VAL A CB  1 
ATOM   1808 C CG1 . VAL A 1 233 ? -6.423  -15.350 52.059 1.00 11.65 ? 233  VAL A CG1 1 
ATOM   1809 C CG2 . VAL A 1 233 ? -8.768  -15.143 52.824 1.00 11.59 ? 233  VAL A CG2 1 
ATOM   1810 N N   . PHE A 1 234 ? -5.776  -12.733 50.267 1.00 13.61 ? 234  PHE A N   1 
ATOM   1811 C CA  . PHE A 1 234 ? -4.659  -12.636 49.347 1.00 13.03 ? 234  PHE A CA  1 
ATOM   1812 C C   . PHE A 1 234 ? -3.339  -13.149 49.999 1.00 13.54 ? 234  PHE A C   1 
ATOM   1813 O O   . PHE A 1 234 ? -2.944  -12.701 51.085 1.00 11.82 ? 234  PHE A O   1 
ATOM   1814 C CB  . PHE A 1 234 ? -4.474  -11.183 48.906 1.00 13.53 ? 234  PHE A CB  1 
ATOM   1815 C CG  . PHE A 1 234 ? -3.243  -10.950 48.052 1.00 13.90 ? 234  PHE A CG  1 
ATOM   1816 C CD1 . PHE A 1 234 ? -3.108  -11.592 46.844 1.00 14.36 ? 234  PHE A CD1 1 
ATOM   1817 C CD2 . PHE A 1 234 ? -2.228  -10.096 48.482 1.00 13.95 ? 234  PHE A CD2 1 
ATOM   1818 C CE1 . PHE A 1 234 ? -1.977  -11.415 46.047 1.00 17.15 ? 234  PHE A CE1 1 
ATOM   1819 C CE2 . PHE A 1 234 ? -1.088  -9.897  47.700 1.00 15.64 ? 234  PHE A CE2 1 
ATOM   1820 C CZ  . PHE A 1 234 ? -0.963  -10.571 46.465 1.00 13.06 ? 234  PHE A CZ  1 
ATOM   1821 N N   . LEU A 1 235 ? -2.687  -14.093 49.323 1.00 12.40 ? 235  LEU A N   1 
ATOM   1822 C CA  . LEU A 1 235 ? -1.367  -14.565 49.734 1.00 12.72 ? 235  LEU A CA  1 
ATOM   1823 C C   . LEU A 1 235 ? -0.327  -13.853 48.863 1.00 12.64 ? 235  LEU A C   1 
ATOM   1824 O O   . LEU A 1 235 ? -0.317  -14.026 47.647 1.00 13.48 ? 235  LEU A O   1 
ATOM   1825 C CB  . LEU A 1 235 ? -1.246  -16.101 49.648 1.00 12.93 ? 235  LEU A CB  1 
ATOM   1826 C CG  . LEU A 1 235 ? 0.182   -16.686 49.824 1.00 11.96 ? 235  LEU A CG  1 
ATOM   1827 C CD1 . LEU A 1 235 ? 0.713   -16.283 51.168 1.00 6.52  ? 235  LEU A CD1 1 
ATOM   1828 C CD2 . LEU A 1 235 ? 0.228   -18.208 49.654 1.00 11.35 ? 235  LEU A CD2 1 
ATOM   1829 N N   . MET A 1 236 ? 0.476   -12.998 49.499 1.00 13.94 ? 236  MET A N   1 
ATOM   1830 C CA  . MET A 1 236 ? 1.614   -12.310 48.890 1.00 14.86 ? 236  MET A CA  1 
ATOM   1831 C C   . MET A 1 236 ? 2.858   -13.217 48.892 1.00 15.95 ? 236  MET A C   1 
ATOM   1832 O O   . MET A 1 236 ? 3.686   -13.182 49.804 1.00 15.82 ? 236  MET A O   1 
ATOM   1833 C CB  . MET A 1 236 ? 1.915   -11.010 49.640 1.00 14.62 ? 236  MET A CB  1 
ATOM   1834 C CG  . MET A 1 236 ? 3.066   -10.161 49.014 1.00 16.10 ? 236  MET A CG  1 
ATOM   1835 S SD  . MET A 1 236 ? 2.792   -9.519  47.345 1.00 21.51 ? 236  MET A SD  1 
ATOM   1836 C CE  . MET A 1 236 ? 2.218   -7.909  47.887 1.00 17.52 ? 236  MET A CE  1 
ATOM   1837 N N   . ASN A 1 237 ? 2.951   -14.043 47.856 1.00 17.17 ? 237  ASN A N   1 
ATOM   1838 C CA  . ASN A 1 237 ? 4.022   -15.035 47.719 1.00 16.36 ? 237  ASN A CA  1 
ATOM   1839 C C   . ASN A 1 237 ? 4.149   -15.276 46.212 1.00 16.96 ? 237  ASN A C   1 
ATOM   1840 O O   . ASN A 1 237 ? 3.143   -15.446 45.514 1.00 16.31 ? 237  ASN A O   1 
ATOM   1841 C CB  . ASN A 1 237 ? 3.643   -16.306 48.512 1.00 16.38 ? 237  ASN A CB  1 
ATOM   1842 C CG  . ASN A 1 237 ? 4.725   -17.396 48.503 1.00 15.36 ? 237  ASN A CG  1 
ATOM   1843 O OD1 . ASN A 1 237 ? 4.861   -18.122 47.544 1.00 14.34 ? 237  ASN A OD1 1 
ATOM   1844 N ND2 . ASN A 1 237 ? 5.360   -17.608 49.643 1.00 13.96 ? 237  ASN A ND2 1 
ATOM   1845 N N   . SER A 1 238 ? 5.381   -15.208 45.701 1.00 16.43 ? 238  SER A N   1 
ATOM   1846 C CA  . SER A 1 238 ? 5.647   -15.407 44.284 1.00 16.83 ? 238  SER A CA  1 
ATOM   1847 C C   . SER A 1 238 ? 6.299   -16.781 43.910 1.00 17.87 ? 238  SER A C   1 
ATOM   1848 O O   . SER A 1 238 ? 6.751   -16.971 42.780 1.00 17.67 ? 238  SER A O   1 
ATOM   1849 C CB  . SER A 1 238 ? 6.552   -14.273 43.784 1.00 17.19 ? 238  SER A CB  1 
ATOM   1850 O OG  . SER A 1 238 ? 7.760   -14.224 44.522 1.00 15.96 ? 238  SER A OG  1 
ATOM   1851 N N   . ASN A 1 239 ? 6.382   -17.705 44.866 1.00 16.48 ? 239  ASN A N   1 
ATOM   1852 C CA  . ASN A 1 239 ? 6.937   -19.014 44.597 1.00 16.27 ? 239  ASN A CA  1 
ATOM   1853 C C   . ASN A 1 239 ? 5.892   -19.931 43.995 1.00 16.23 ? 239  ASN A C   1 
ATOM   1854 O O   . ASN A 1 239 ? 4.673   -19.614 44.057 1.00 15.89 ? 239  ASN A O   1 
ATOM   1855 C CB  . ASN A 1 239 ? 7.520   -19.603 45.891 1.00 16.16 ? 239  ASN A CB  1 
ATOM   1856 C CG  . ASN A 1 239 ? 8.773   -18.861 46.336 1.00 17.41 ? 239  ASN A CG  1 
ATOM   1857 O OD1 . ASN A 1 239 ? 9.890   -19.275 46.037 1.00 22.01 ? 239  ASN A OD1 1 
ATOM   1858 N ND2 . ASN A 1 239 ? 8.595   -17.759 47.026 1.00 15.99 ? 239  ASN A ND2 1 
ATOM   1859 N N   . ALA A 1 240 ? 6.339   -21.030 43.391 1.00 15.35 ? 240  ALA A N   1 
ATOM   1860 C CA  . ALA A 1 240 ? 5.403   -22.065 42.908 1.00 15.81 ? 240  ALA A CA  1 
ATOM   1861 C C   . ALA A 1 240 ? 4.550   -22.549 44.060 1.00 16.02 ? 240  ALA A C   1 
ATOM   1862 O O   . ALA A 1 240 ? 5.019   -22.706 45.163 1.00 16.10 ? 240  ALA A O   1 
ATOM   1863 C CB  . ALA A 1 240 ? 6.119   -23.247 42.270 1.00 16.23 ? 240  ALA A CB  1 
ATOM   1864 N N   . MET A 1 241 ? 3.296   -22.835 43.778 1.00 16.14 ? 241  MET A N   1 
ATOM   1865 C CA  . MET A 1 241 ? 2.398   -23.194 44.835 1.00 17.06 ? 241  MET A CA  1 
ATOM   1866 C C   . MET A 1 241 ? 1.212   -23.910 44.249 1.00 16.52 ? 241  MET A C   1 
ATOM   1867 O O   . MET A 1 241 ? 1.056   -23.987 43.029 1.00 15.85 ? 241  MET A O   1 
ATOM   1868 C CB  . MET A 1 241 ? 1.935   -21.926 45.557 1.00 17.00 ? 241  MET A CB  1 
ATOM   1869 C CG  . MET A 1 241 ? 0.775   -21.177 44.854 1.00 18.74 ? 241  MET A CG  1 
ATOM   1870 S SD  . MET A 1 241 ? 0.122   -19.847 45.889 1.00 19.46 ? 241  MET A SD  1 
ATOM   1871 C CE  . MET A 1 241 ? 1.597   -18.821 46.030 1.00 16.30 ? 241  MET A CE  1 
ATOM   1872 N N   . GLU A 1 242 ? 0.389   -24.453 45.134 1.00 17.56 ? 242  GLU A N   1 
ATOM   1873 C CA  . GLU A 1 242 ? -0.909  -24.943 44.742 1.00 17.40 ? 242  GLU A CA  1 
ATOM   1874 C C   . GLU A 1 242 ? -1.950  -24.656 45.812 1.00 17.76 ? 242  GLU A C   1 
ATOM   1875 O O   . GLU A 1 242 ? -1.642  -24.436 46.979 1.00 18.44 ? 242  GLU A O   1 
ATOM   1876 C CB  . GLU A 1 242 ? -0.849  -26.418 44.348 1.00 17.63 ? 242  GLU A CB  1 
ATOM   1877 C CG  . GLU A 1 242 ? -0.444  -27.379 45.447 1.00 19.97 ? 242  GLU A CG  1 
ATOM   1878 C CD  . GLU A 1 242 ? -0.025  -28.725 44.887 1.00 23.55 ? 242  GLU A CD  1 
ATOM   1879 O OE1 . GLU A 1 242 ? -0.013  -28.862 43.640 1.00 23.92 ? 242  GLU A OE1 1 
ATOM   1880 O OE2 . GLU A 1 242 ? 0.277   -29.648 45.681 1.00 24.74 ? 242  GLU A OE2 1 
ATOM   1881 N N   . VAL A 1 243 ? -3.198  -24.614 45.389 1.00 17.28 ? 243  VAL A N   1 
ATOM   1882 C CA  . VAL A 1 243 ? -4.273  -24.270 46.282 1.00 16.52 ? 243  VAL A CA  1 
ATOM   1883 C C   . VAL A 1 243 ? -5.164  -25.476 46.260 1.00 15.92 ? 243  VAL A C   1 
ATOM   1884 O O   . VAL A 1 243 ? -5.611  -25.922 45.206 1.00 15.13 ? 243  VAL A O   1 
ATOM   1885 C CB  . VAL A 1 243 ? -4.990  -22.985 45.795 1.00 17.61 ? 243  VAL A CB  1 
ATOM   1886 C CG1 . VAL A 1 243 ? -6.392  -22.862 46.401 1.00 19.81 ? 243  VAL A CG1 1 
ATOM   1887 C CG2 . VAL A 1 243 ? -4.166  -21.792 46.143 1.00 17.16 ? 243  VAL A CG2 1 
ATOM   1888 N N   . VAL A 1 244 ? -5.417  -26.014 47.438 1.00 15.57 ? 244  VAL A N   1 
ATOM   1889 C CA  . VAL A 1 244 ? -6.153  -27.234 47.548 1.00 15.20 ? 244  VAL A CA  1 
ATOM   1890 C C   . VAL A 1 244 ? -7.510  -26.863 48.107 1.00 15.01 ? 244  VAL A C   1 
ATOM   1891 O O   . VAL A 1 244 ? -7.602  -26.235 49.141 1.00 15.19 ? 244  VAL A O   1 
ATOM   1892 C CB  . VAL A 1 244 ? -5.435  -28.215 48.484 1.00 15.53 ? 244  VAL A CB  1 
ATOM   1893 C CG1 . VAL A 1 244 ? -6.169  -29.554 48.529 1.00 14.59 ? 244  VAL A CG1 1 
ATOM   1894 C CG2 . VAL A 1 244 ? -3.954  -28.388 48.055 1.00 17.73 ? 244  VAL A CG2 1 
ATOM   1895 N N   . LEU A 1 245 ? -8.559  -27.285 47.436 1.00 15.41 ? 245  LEU A N   1 
ATOM   1896 C CA  . LEU A 1 245 ? -9.926  -26.915 47.833 1.00 16.31 ? 245  LEU A CA  1 
ATOM   1897 C C   . LEU A 1 245 ? -10.594 -28.184 48.256 1.00 16.54 ? 245  LEU A C   1 
ATOM   1898 O O   . LEU A 1 245 ? -10.415 -29.209 47.609 1.00 16.68 ? 245  LEU A O   1 
ATOM   1899 C CB  . LEU A 1 245 ? -10.692 -26.274 46.663 1.00 15.65 ? 245  LEU A CB  1 
ATOM   1900 C CG  . LEU A 1 245 ? -10.097 -25.056 45.906 1.00 17.49 ? 245  LEU A CG  1 
ATOM   1901 C CD1 . LEU A 1 245 ? -11.146 -24.523 44.914 1.00 18.50 ? 245  LEU A CD1 1 
ATOM   1902 C CD2 . LEU A 1 245 ? -9.708  -23.918 46.820 1.00 18.88 ? 245  LEU A CD2 1 
ATOM   1903 N N   . GLN A 1 246 ? -11.362 -28.140 49.340 1.00 16.77 ? 246  GLN A N   1 
ATOM   1904 C CA  . GLN A 1 246 ? -12.063 -29.331 49.797 1.00 17.01 ? 246  GLN A CA  1 
ATOM   1905 C C   . GLN A 1 246 ? -13.454 -28.988 50.403 1.00 17.79 ? 246  GLN A C   1 
ATOM   1906 O O   . GLN A 1 246 ? -13.669 -27.860 50.810 1.00 18.04 ? 246  GLN A O   1 
ATOM   1907 C CB  . GLN A 1 246 ? -11.199 -30.098 50.770 1.00 17.16 ? 246  GLN A CB  1 
ATOM   1908 C CG  . GLN A 1 246 ? -11.100 -29.549 52.180 1.00 15.89 ? 246  GLN A CG  1 
ATOM   1909 C CD  . GLN A 1 246 ? -10.016 -30.293 52.929 1.00 16.91 ? 246  GLN A CD  1 
ATOM   1910 O OE1 . GLN A 1 246 ? -8.840  -30.170 52.586 1.00 16.52 ? 246  GLN A OE1 1 
ATOM   1911 N NE2 . GLN A 1 246 ? -10.405 -31.086 53.939 1.00 15.32 ? 246  GLN A NE2 1 
ATOM   1912 N N   . PRO A 1 247 ? -14.373 -29.962 50.478 1.00 18.21 ? 247  PRO A N   1 
ATOM   1913 C CA  . PRO A 1 247 ? -15.788 -29.671 50.784 1.00 19.42 ? 247  PRO A CA  1 
ATOM   1914 C C   . PRO A 1 247 ? -16.078 -29.341 52.225 1.00 19.84 ? 247  PRO A C   1 
ATOM   1915 O O   . PRO A 1 247 ? -17.225 -29.083 52.550 1.00 21.09 ? 247  PRO A O   1 
ATOM   1916 C CB  . PRO A 1 247 ? -16.517 -30.970 50.401 1.00 19.03 ? 247  PRO A CB  1 
ATOM   1917 C CG  . PRO A 1 247 ? -15.507 -31.801 49.701 1.00 19.09 ? 247  PRO A CG  1 
ATOM   1918 C CD  . PRO A 1 247 ? -14.183 -31.391 50.253 1.00 18.97 ? 247  PRO A CD  1 
ATOM   1919 N N   . ALA A 1 248 ? -15.062 -29.324 53.094 1.00 20.09 ? 248  ALA A N   1 
ATOM   1920 C CA  . ALA A 1 248 ? -15.268 -28.951 54.499 1.00 18.91 ? 248  ALA A CA  1 
ATOM   1921 C C   . ALA A 1 248 ? -16.309 -27.834 54.749 1.00 20.32 ? 248  ALA A C   1 
ATOM   1922 O O   . ALA A 1 248 ? -17.075 -27.952 55.724 1.00 19.24 ? 248  ALA A O   1 
ATOM   1923 C CB  . ALA A 1 248 ? -13.963 -28.602 55.161 1.00 19.02 ? 248  ALA A CB  1 
ATOM   1924 N N   . PRO A 1 249 ? -16.274 -26.685 53.957 1.00 19.30 ? 249  PRO A N   1 
ATOM   1925 C CA  . PRO A 1 249 ? -15.345 -26.252 52.922 1.00 17.88 ? 249  PRO A CA  1 
ATOM   1926 C C   . PRO A 1 249 ? -14.065 -25.647 53.500 1.00 17.45 ? 249  PRO A C   1 
ATOM   1927 O O   . PRO A 1 249 ? -14.078 -25.077 54.579 1.00 16.89 ? 249  PRO A O   1 
ATOM   1928 C CB  . PRO A 1 249 ? -16.137 -25.179 52.184 1.00 17.96 ? 249  PRO A CB  1 
ATOM   1929 C CG  . PRO A 1 249 ? -16.911 -24.548 53.232 1.00 18.36 ? 249  PRO A CG  1 
ATOM   1930 C CD  . PRO A 1 249 ? -17.323 -25.669 54.161 1.00 18.79 ? 249  PRO A CD  1 
ATOM   1931 N N   . ALA A 1 250 ? -12.956 -25.795 52.786 1.00 17.15 ? 250  ALA A N   1 
ATOM   1932 C CA  . ALA A 1 250 ? -11.682 -25.291 53.303 1.00 16.76 ? 250  ALA A CA  1 
ATOM   1933 C C   . ALA A 1 250 ? -10.739 -25.057 52.156 1.00 16.71 ? 250  ALA A C   1 
ATOM   1934 O O   . ALA A 1 250 ? -10.931 -25.638 51.089 1.00 15.14 ? 250  ALA A O   1 
ATOM   1935 C CB  . ALA A 1 250 ? -11.084 -26.316 54.269 1.00 16.76 ? 250  ALA A CB  1 
ATOM   1936 N N   . ILE A 1 251 ? -9.710  -24.223 52.375 1.00 16.75 ? 251  ILE A N   1 
ATOM   1937 C CA  . ILE A 1 251 ? -8.699  -23.979 51.357 1.00 16.87 ? 251  ILE A CA  1 
ATOM   1938 C C   . ILE A 1 251 ? -7.322  -24.083 51.999 1.00 17.13 ? 251  ILE A C   1 
ATOM   1939 O O   . ILE A 1 251 ? -7.136  -23.656 53.140 1.00 16.84 ? 251  ILE A O   1 
ATOM   1940 C CB  . ILE A 1 251 ? -8.926  -22.637 50.548 1.00 17.54 ? 251  ILE A CB  1 
ATOM   1941 C CG1 . ILE A 1 251 ? -7.713  -22.284 49.670 1.00 15.38 ? 251  ILE A CG1 1 
ATOM   1942 C CG2 . ILE A 1 251 ? -9.305  -21.486 51.477 1.00 19.35 ? 251  ILE A CG2 1 
ATOM   1943 C CD1 . ILE A 1 251 ? -7.954  -21.120 48.654 1.00 17.60 ? 251  ILE A CD1 1 
ATOM   1944 N N   . THR A 1 252 ? -6.397  -24.733 51.298 1.00 16.63 ? 252  THR A N   1 
ATOM   1945 C CA  . THR A 1 252 ? -5.023  -24.914 51.784 1.00 18.06 ? 252  THR A CA  1 
ATOM   1946 C C   . THR A 1 252 ? -4.097  -24.297 50.752 1.00 18.20 ? 252  THR A C   1 
ATOM   1947 O O   . THR A 1 252 ? -4.225  -24.588 49.555 1.00 18.26 ? 252  THR A O   1 
ATOM   1948 C CB  . THR A 1 252 ? -4.678  -26.407 51.974 1.00 18.07 ? 252  THR A CB  1 
ATOM   1949 O OG1 . THR A 1 252 ? -5.580  -26.996 52.916 1.00 19.43 ? 252  THR A OG1 1 
ATOM   1950 C CG2 . THR A 1 252 ? -3.209  -26.607 52.494 1.00 17.91 ? 252  THR A CG2 1 
ATOM   1951 N N   . TYR A 1 253 ? -3.217  -23.411 51.210 1.00 19.12 ? 253  TYR A N   1 
ATOM   1952 C CA  . TYR A 1 253 ? -2.172  -22.814 50.379 1.00 20.04 ? 253  TYR A CA  1 
ATOM   1953 C C   . TYR A 1 253 ? -0.893  -23.609 50.646 1.00 19.87 ? 253  TYR A C   1 
ATOM   1954 O O   . TYR A 1 253 ? -0.541  -23.804 51.791 1.00 19.77 ? 253  TYR A O   1 
ATOM   1955 C CB  . TYR A 1 253 ? -1.949  -21.338 50.750 1.00 21.39 ? 253  TYR A CB  1 
ATOM   1956 C CG  . TYR A 1 253 ? -3.015  -20.356 50.275 1.00 21.52 ? 253  TYR A CG  1 
ATOM   1957 C CD1 . TYR A 1 253 ? -2.921  -19.755 49.029 1.00 23.85 ? 253  TYR A CD1 1 
ATOM   1958 C CD2 . TYR A 1 253 ? -4.104  -20.018 51.079 1.00 24.85 ? 253  TYR A CD2 1 
ATOM   1959 C CE1 . TYR A 1 253 ? -3.898  -18.824 48.574 1.00 24.73 ? 253  TYR A CE1 1 
ATOM   1960 C CE2 . TYR A 1 253 ? -5.093  -19.097 50.635 1.00 23.33 ? 253  TYR A CE2 1 
ATOM   1961 C CZ  . TYR A 1 253 ? -4.976  -18.508 49.384 1.00 26.06 ? 253  TYR A CZ  1 
ATOM   1962 O OH  . TYR A 1 253 ? -5.937  -17.582 48.903 1.00 26.80 ? 253  TYR A OH  1 
ATOM   1963 N N   . ARG A 1 254 ? -0.216  -24.064 49.595 1.00 19.16 ? 254  ARG A N   1 
ATOM   1964 C CA  . ARG A 1 254 ? 0.937   -24.938 49.727 1.00 19.41 ? 254  ARG A CA  1 
ATOM   1965 C C   . ARG A 1 254 ? 2.030   -24.364 48.830 1.00 18.99 ? 254  ARG A C   1 
ATOM   1966 O O   . ARG A 1 254 ? 1.946   -24.507 47.626 1.00 19.22 ? 254  ARG A O   1 
ATOM   1967 C CB  . ARG A 1 254 ? 0.532   -26.320 49.237 1.00 19.57 ? 254  ARG A CB  1 
ATOM   1968 C CG  . ARG A 1 254 ? 1.441   -27.474 49.689 1.00 20.34 ? 254  ARG A CG  1 
ATOM   1969 C CD  . ARG A 1 254 ? 0.921   -28.763 49.123 1.00 16.24 ? 254  ARG A CD  1 
ATOM   1970 N NE  . ARG A 1 254 ? -0.117  -29.397 49.944 1.00 17.91 ? 254  ARG A NE  1 
ATOM   1971 C CZ  . ARG A 1 254 ? -1.114  -30.110 49.442 1.00 16.32 ? 254  ARG A CZ  1 
ATOM   1972 N NH1 . ARG A 1 254 ? -1.236  -30.238 48.136 1.00 19.00 ? 254  ARG A NH1 1 
ATOM   1973 N NH2 . ARG A 1 254 ? -1.984  -30.703 50.233 1.00 20.08 ? 254  ARG A NH2 1 
ATOM   1974 N N   . THR A 1 255 ? 3.025   -23.702 49.410 1.00 17.74 ? 255  THR A N   1 
ATOM   1975 C CA  . THR A 1 255 ? 4.043   -23.010 48.616 1.00 17.84 ? 255  THR A CA  1 
ATOM   1976 C C   . THR A 1 255 ? 5.482   -23.537 48.913 1.00 17.77 ? 255  THR A C   1 
ATOM   1977 O O   . THR A 1 255 ? 5.720   -24.141 49.944 1.00 17.87 ? 255  THR A O   1 
ATOM   1978 C CB  . THR A 1 255 ? 3.897   -21.479 48.784 1.00 17.64 ? 255  THR A CB  1 
ATOM   1979 O OG1 . THR A 1 255 ? 4.788   -20.798 47.893 1.00 20.09 ? 255  THR A OG1 1 
ATOM   1980 C CG2 . THR A 1 255 ? 4.116   -21.028 50.231 1.00 16.33 ? 255  THR A CG2 1 
ATOM   1981 N N   . ILE A 1 256 ? 6.417   -23.349 47.987 1.00 17.49 ? 256  ILE A N   1 
ATOM   1982 C CA  . ILE A 1 256 ? 7.750   -23.960 48.127 1.00 17.07 ? 256  ILE A CA  1 
ATOM   1983 C C   . ILE A 1 256 ? 8.844   -22.916 48.370 1.00 17.11 ? 256  ILE A C   1 
ATOM   1984 O O   . ILE A 1 256 ? 10.044  -23.170 48.179 1.00 18.47 ? 256  ILE A O   1 
ATOM   1985 C CB  . ILE A 1 256 ? 8.106   -24.903 46.922 1.00 17.03 ? 256  ILE A CB  1 
ATOM   1986 C CG1 . ILE A 1 256 ? 8.286   -24.108 45.626 1.00 15.47 ? 256  ILE A CG1 1 
ATOM   1987 C CG2 . ILE A 1 256 ? 7.056   -26.027 46.767 1.00 14.10 ? 256  ILE A CG2 1 
ATOM   1988 C CD1 . ILE A 1 256 ? 8.633   -24.947 44.417 1.00 17.48 ? 256  ILE A CD1 1 
ATOM   1989 N N   . GLY A 1 257 ? 8.438   -21.730 48.791 1.00 16.78 ? 257  GLY A N   1 
ATOM   1990 C CA  . GLY A 1 257 ? 9.412   -20.784 49.297 1.00 15.94 ? 257  GLY A CA  1 
ATOM   1991 C C   . GLY A 1 257 ? 8.788   -19.563 49.890 1.00 16.19 ? 257  GLY A C   1 
ATOM   1992 O O   . GLY A 1 257 ? 7.556   -19.478 50.061 1.00 14.86 ? 257  GLY A O   1 
ATOM   1993 N N   . GLY A 1 258 ? 9.661   -18.597 50.153 1.00 15.12 ? 258  GLY A N   1 
ATOM   1994 C CA  . GLY A 1 258 ? 9.298   -17.290 50.601 1.00 14.90 ? 258  GLY A CA  1 
ATOM   1995 C C   . GLY A 1 258 ? 8.684   -17.349 51.963 1.00 16.29 ? 258  GLY A C   1 
ATOM   1996 O O   . GLY A 1 258 ? 9.141   -18.100 52.827 1.00 14.99 ? 258  GLY A O   1 
ATOM   1997 N N   . ILE A 1 259 ? 7.614   -16.561 52.155 1.00 16.45 ? 259  ILE A N   1 
ATOM   1998 C CA  . ILE A 1 259 ? 6.946   -16.531 53.442 1.00 17.13 ? 259  ILE A CA  1 
ATOM   1999 C C   . ILE A 1 259 ? 5.436   -16.539 53.233 1.00 17.59 ? 259  ILE A C   1 
ATOM   2000 O O   . ILE A 1 259 ? 4.939   -16.333 52.112 1.00 16.70 ? 259  ILE A O   1 
ATOM   2001 C CB  . ILE A 1 259 ? 7.365   -15.291 54.358 1.00 17.65 ? 259  ILE A CB  1 
ATOM   2002 C CG1 . ILE A 1 259 ? 7.124   -13.948 53.667 1.00 17.12 ? 259  ILE A CG1 1 
ATOM   2003 C CG2 . ILE A 1 259 ? 8.802   -15.367 54.775 1.00 18.35 ? 259  ILE A CG2 1 
ATOM   2004 C CD1 . ILE A 1 259 ? 6.831   -12.758 54.646 1.00 17.27 ? 259  ILE A CD1 1 
ATOM   2005 N N   . LEU A 1 260 ? 4.737   -16.810 54.321 1.00 18.31 ? 260  LEU A N   1 
ATOM   2006 C CA  . LEU A 1 260 ? 3.301   -16.792 54.337 1.00 20.09 ? 260  LEU A CA  1 
ATOM   2007 C C   . LEU A 1 260 ? 2.934   -15.397 54.770 1.00 20.28 ? 260  LEU A C   1 
ATOM   2008 O O   . LEU A 1 260 ? 3.037   -15.065 55.928 1.00 21.37 ? 260  LEU A O   1 
ATOM   2009 C CB  . LEU A 1 260 ? 2.756   -17.853 55.295 1.00 20.07 ? 260  LEU A CB  1 
ATOM   2010 C CG  . LEU A 1 260 ? 2.797   -19.287 54.778 1.00 21.62 ? 260  LEU A CG  1 
ATOM   2011 C CD1 . LEU A 1 260 ? 2.225   -20.235 55.844 1.00 20.55 ? 260  LEU A CD1 1 
ATOM   2012 C CD2 . LEU A 1 260 ? 2.043   -19.425 53.416 1.00 21.34 ? 260  LEU A CD2 1 
ATOM   2013 N N   . ASP A 1 261 ? 2.569   -14.578 53.790 1.00 20.97 ? 261  ASP A N   1 
ATOM   2014 C CA  . ASP A 1 261 ? 2.277   -13.174 53.966 1.00 20.96 ? 261  ASP A CA  1 
ATOM   2015 C C   . ASP A 1 261 ? 0.843   -13.000 53.481 1.00 20.91 ? 261  ASP A C   1 
ATOM   2016 O O   . ASP A 1 261 ? 0.604   -12.925 52.268 1.00 21.54 ? 261  ASP A O   1 
ATOM   2017 C CB  . ASP A 1 261 ? 3.245   -12.341 53.117 1.00 20.97 ? 261  ASP A CB  1 
ATOM   2018 C CG  . ASP A 1 261 ? 3.117   -10.836 53.364 1.00 24.17 ? 261  ASP A CG  1 
ATOM   2019 O OD1 . ASP A 1 261 ? 2.162   -10.431 54.038 1.00 27.63 ? 261  ASP A OD1 1 
ATOM   2020 O OD2 . ASP A 1 261 ? 3.976   -10.049 52.893 1.00 25.07 ? 261  ASP A OD2 1 
ATOM   2021 N N   . PHE A 1 262 ? -0.097  -12.933 54.430 1.00 19.37 ? 262  PHE A N   1 
ATOM   2022 C CA  . PHE A 1 262 ? -1.542  -13.027 54.158 1.00 18.61 ? 262  PHE A CA  1 
ATOM   2023 C C   . PHE A 1 262 ? -2.274  -11.705 54.417 1.00 18.02 ? 262  PHE A C   1 
ATOM   2024 O O   . PHE A 1 262 ? -1.924  -10.970 55.343 1.00 17.49 ? 262  PHE A O   1 
ATOM   2025 C CB  . PHE A 1 262 ? -2.192  -14.116 55.035 1.00 17.78 ? 262  PHE A CB  1 
ATOM   2026 C CG  . PHE A 1 262 ? -2.118  -15.515 54.463 1.00 18.60 ? 262  PHE A CG  1 
ATOM   2027 C CD1 . PHE A 1 262 ? -2.888  -15.882 53.357 1.00 15.49 ? 262  PHE A CD1 1 
ATOM   2028 C CD2 . PHE A 1 262 ? -1.290  -16.480 55.047 1.00 16.64 ? 262  PHE A CD2 1 
ATOM   2029 C CE1 . PHE A 1 262 ? -2.813  -17.171 52.836 1.00 16.76 ? 262  PHE A CE1 1 
ATOM   2030 C CE2 . PHE A 1 262 ? -1.223  -17.777 54.514 1.00 16.84 ? 262  PHE A CE2 1 
ATOM   2031 C CZ  . PHE A 1 262 ? -1.977  -18.117 53.420 1.00 16.55 ? 262  PHE A CZ  1 
ATOM   2032 N N   . TYR A 1 263 ? -3.277  -11.417 53.586 1.00 16.90 ? 263  TYR A N   1 
ATOM   2033 C CA  . TYR A 1 263 ? -4.184  -10.274 53.755 1.00 17.22 ? 263  TYR A CA  1 
ATOM   2034 C C   . TYR A 1 263 ? -5.619  -10.806 53.776 1.00 16.96 ? 263  TYR A C   1 
ATOM   2035 O O   . TYR A 1 263 ? -5.938  -11.682 52.990 1.00 16.05 ? 263  TYR A O   1 
ATOM   2036 C CB  . TYR A 1 263 ? -4.022  -9.295  52.581 1.00 17.38 ? 263  TYR A CB  1 
ATOM   2037 C CG  . TYR A 1 263 ? -2.696  -8.543  52.599 1.00 17.96 ? 263  TYR A CG  1 
ATOM   2038 C CD1 . TYR A 1 263 ? -2.580  -7.330  53.274 1.00 20.19 ? 263  TYR A CD1 1 
ATOM   2039 C CD2 . TYR A 1 263 ? -1.570  -9.069  52.003 1.00 17.81 ? 263  TYR A CD2 1 
ATOM   2040 C CE1 . TYR A 1 263 ? -1.379  -6.633  53.303 1.00 19.56 ? 263  TYR A CE1 1 
ATOM   2041 C CE2 . TYR A 1 263 ? -0.345  -8.389  52.036 1.00 19.15 ? 263  TYR A CE2 1 
ATOM   2042 C CZ  . TYR A 1 263 ? -0.271  -7.167  52.676 1.00 17.52 ? 263  TYR A CZ  1 
ATOM   2043 O OH  . TYR A 1 263 ? 0.896   -6.473  52.736 1.00 15.46 ? 263  TYR A OH  1 
ATOM   2044 N N   . VAL A 1 264 ? -6.456  -10.297 54.686 1.00 16.29 ? 264  VAL A N   1 
ATOM   2045 C CA  . VAL A 1 264 ? -7.857  -10.702 54.786 1.00 15.70 ? 264  VAL A CA  1 
ATOM   2046 C C   . VAL A 1 264 ? -8.682  -9.413  54.689 1.00 16.11 ? 264  VAL A C   1 
ATOM   2047 O O   . VAL A 1 264 ? -8.448  -8.459  55.442 1.00 16.20 ? 264  VAL A O   1 
ATOM   2048 C CB  . VAL A 1 264 ? -8.188  -11.534 56.090 1.00 16.38 ? 264  VAL A CB  1 
ATOM   2049 C CG1 . VAL A 1 264 ? -9.655  -12.014 56.106 1.00 14.33 ? 264  VAL A CG1 1 
ATOM   2050 C CG2 . VAL A 1 264 ? -7.251  -12.753 56.231 1.00 15.31 ? 264  VAL A CG2 1 
ATOM   2051 N N   . PHE A 1 265 ? -9.607  -9.380  53.733 1.00 15.63 ? 265  PHE A N   1 
ATOM   2052 C CA  . PHE A 1 265 ? -10.364 -8.173  53.387 1.00 15.92 ? 265  PHE A CA  1 
ATOM   2053 C C   . PHE A 1 265 ? -11.806 -8.481  53.755 1.00 16.23 ? 265  PHE A C   1 
ATOM   2054 O O   . PHE A 1 265 ? -12.293 -9.551  53.425 1.00 16.20 ? 265  PHE A O   1 
ATOM   2055 C CB  . PHE A 1 265 ? -10.299 -7.877  51.862 1.00 15.67 ? 265  PHE A CB  1 
ATOM   2056 C CG  . PHE A 1 265 ? -8.887  -7.852  51.293 1.00 16.68 ? 265  PHE A CG  1 
ATOM   2057 C CD1 . PHE A 1 265 ? -8.064  -6.768  51.511 1.00 15.30 ? 265  PHE A CD1 1 
ATOM   2058 C CD2 . PHE A 1 265 ? -8.381  -8.952  50.590 1.00 17.29 ? 265  PHE A CD2 1 
ATOM   2059 C CE1 . PHE A 1 265 ? -6.740  -6.758  51.039 1.00 16.56 ? 265  PHE A CE1 1 
ATOM   2060 C CE2 . PHE A 1 265 ? -7.085  -8.957  50.104 1.00 18.03 ? 265  PHE A CE2 1 
ATOM   2061 C CZ  . PHE A 1 265 ? -6.260  -7.843  50.311 1.00 15.50 ? 265  PHE A CZ  1 
ATOM   2062 N N   . LEU A 1 266 ? -12.485 -7.552  54.421 1.00 17.09 ? 266  LEU A N   1 
ATOM   2063 C CA  . LEU A 1 266 ? -13.907 -7.709  54.662 1.00 18.00 ? 266  LEU A CA  1 
ATOM   2064 C C   . LEU A 1 266 ? -14.659 -6.631  53.928 1.00 17.86 ? 266  LEU A C   1 
ATOM   2065 O O   . LEU A 1 266 ? -14.176 -5.527  53.788 1.00 18.62 ? 266  LEU A O   1 
ATOM   2066 C CB  . LEU A 1 266 ? -14.246 -7.664  56.153 1.00 17.79 ? 266  LEU A CB  1 
ATOM   2067 C CG  . LEU A 1 266 ? -13.979 -8.893  57.018 1.00 18.85 ? 266  LEU A CG  1 
ATOM   2068 C CD1 . LEU A 1 266 ? -12.507 -8.978  57.378 1.00 19.32 ? 266  LEU A CD1 1 
ATOM   2069 C CD2 . LEU A 1 266 ? -14.825 -8.747  58.302 1.00 19.31 ? 266  LEU A CD2 1 
ATOM   2070 N N   . GLY A 1 267 ? -15.827 -6.980  53.421 1.00 17.59 ? 267  GLY A N   1 
ATOM   2071 C CA  . GLY A 1 267 ? -16.672 -6.019  52.733 1.00 17.40 ? 267  GLY A CA  1 
ATOM   2072 C C   . GLY A 1 267 ? -18.132 -6.330  53.007 1.00 16.20 ? 267  GLY A C   1 
ATOM   2073 O O   . GLY A 1 267 ? -18.461 -7.414  53.438 1.00 16.15 ? 267  GLY A O   1 
ATOM   2074 N N   . ASN A 1 268 ? -19.028 -5.386  52.744 1.00 17.65 ? 268  ASN A N   1 
ATOM   2075 C CA  . ASN A 1 268 ? -20.476 -5.667  52.928 1.00 16.68 ? 268  ASN A CA  1 
ATOM   2076 C C   . ASN A 1 268 ? -21.126 -6.265  51.705 1.00 16.81 ? 268  ASN A C   1 
ATOM   2077 O O   . ASN A 1 268 ? -22.284 -6.756  51.761 1.00 17.07 ? 268  ASN A O   1 
ATOM   2078 C CB  . ASN A 1 268 ? -21.226 -4.390  53.338 1.00 17.62 ? 268  ASN A CB  1 
ATOM   2079 C CG  . ASN A 1 268 ? -20.796 -3.882  54.691 1.00 20.20 ? 268  ASN A CG  1 
ATOM   2080 O OD1 . ASN A 1 268 ? -20.451 -4.662  55.572 1.00 26.35 ? 268  ASN A OD1 1 
ATOM   2081 N ND2 . ASN A 1 268 ? -20.791 -2.563  54.862 1.00 21.66 ? 268  ASN A ND2 1 
ATOM   2082 N N   . THR A 1 269 ? -20.397 -6.196  50.594 1.00 16.31 ? 269  THR A N   1 
ATOM   2083 C CA  . THR A 1 269 ? -20.807 -6.734  49.302 1.00 15.81 ? 269  THR A CA  1 
ATOM   2084 C C   . THR A 1 269 ? -19.572 -7.336  48.618 1.00 15.38 ? 269  THR A C   1 
ATOM   2085 O O   . THR A 1 269 ? -18.447 -6.993  48.976 1.00 15.43 ? 269  THR A O   1 
ATOM   2086 C CB  . THR A 1 269 ? -21.333 -5.626  48.380 1.00 15.70 ? 269  THR A CB  1 
ATOM   2087 O OG1 . THR A 1 269 ? -20.319 -4.640  48.209 1.00 14.63 ? 269  THR A OG1 1 
ATOM   2088 C CG2 . THR A 1 269 ? -22.604 -4.951  48.930 1.00 16.40 ? 269  THR A CG2 1 
ATOM   2089 N N   . PRO A 1 270 ? -19.784 -8.226  47.629 1.00 14.79 ? 270  PRO A N   1 
ATOM   2090 C CA  . PRO A 1 270 ? -18.667 -8.744  46.851 1.00 14.10 ? 270  PRO A CA  1 
ATOM   2091 C C   . PRO A 1 270 ? -17.838 -7.648  46.211 1.00 14.96 ? 270  PRO A C   1 
ATOM   2092 O O   . PRO A 1 270 ? -16.593 -7.723  46.255 1.00 13.01 ? 270  PRO A O   1 
ATOM   2093 C CB  . PRO A 1 270 ? -19.344 -9.650  45.806 1.00 13.95 ? 270  PRO A CB  1 
ATOM   2094 C CG  . PRO A 1 270 ? -20.644 -10.037 46.422 1.00 13.61 ? 270  PRO A CG  1 
ATOM   2095 C CD  . PRO A 1 270 ? -21.073 -8.832  47.213 1.00 14.06 ? 270  PRO A CD  1 
ATOM   2096 N N   . GLU A 1 271 ? -18.498 -6.621  45.659 1.00 13.06 ? 271  GLU A N   1 
ATOM   2097 C CA  . GLU A 1 271 ? -17.809 -5.458  45.092 1.00 13.63 ? 271  GLU A CA  1 
ATOM   2098 C C   . GLU A 1 271 ? -16.853 -4.738  46.061 1.00 14.24 ? 271  GLU A C   1 
ATOM   2099 O O   . GLU A 1 271 ? -15.718 -4.325  45.664 1.00 12.04 ? 271  GLU A O   1 
ATOM   2100 C CB  . GLU A 1 271 ? -18.819 -4.446  44.517 1.00 14.35 ? 271  GLU A CB  1 
ATOM   2101 C CG  . GLU A 1 271 ? -19.355 -4.819  43.122 1.00 16.09 ? 271  GLU A CG  1 
ATOM   2102 C CD  . GLU A 1 271 ? -18.262 -4.808  42.055 1.00 21.64 ? 271  GLU A CD  1 
ATOM   2103 O OE1 . GLU A 1 271 ? -17.725 -3.709  41.754 1.00 22.04 ? 271  GLU A OE1 1 
ATOM   2104 O OE2 . GLU A 1 271 ? -17.927 -5.904  41.542 1.00 23.19 ? 271  GLU A OE2 1 
ATOM   2105 N N   . GLN A 1 272 ? -17.306 -4.558  47.313 1.00 14.39 ? 272  GLN A N   1 
ATOM   2106 C CA  . GLN A 1 272 ? -16.462 -3.942  48.339 1.00 16.09 ? 272  GLN A CA  1 
ATOM   2107 C C   . GLN A 1 272 ? -15.207 -4.759  48.692 1.00 15.74 ? 272  GLN A C   1 
ATOM   2108 O O   . GLN A 1 272 ? -14.190 -4.182  49.059 1.00 16.50 ? 272  GLN A O   1 
ATOM   2109 C CB  . GLN A 1 272 ? -17.234 -3.648  49.599 1.00 16.16 ? 272  GLN A CB  1 
ATOM   2110 C CG  . GLN A 1 272 ? -18.271 -2.543  49.444 1.00 20.37 ? 272  GLN A CG  1 
ATOM   2111 C CD  . GLN A 1 272 ? -18.956 -2.223  50.738 1.00 25.99 ? 272  GLN A CD  1 
ATOM   2112 O OE1 . GLN A 1 272 ? -18.472 -2.602  51.820 1.00 27.64 ? 272  GLN A OE1 1 
ATOM   2113 N NE2 . GLN A 1 272 ? -20.102 -1.529  50.649 1.00 27.34 ? 272  GLN A NE2 1 
ATOM   2114 N N   . VAL A 1 273 ? -15.318 -6.085  48.642 1.00 15.67 ? 273  VAL A N   1 
ATOM   2115 C CA  . VAL A 1 273 ? -14.154 -6.961  48.772 1.00 15.15 ? 273  VAL A CA  1 
ATOM   2116 C C   . VAL A 1 273 ? -13.167 -6.731  47.657 1.00 14.81 ? 273  VAL A C   1 
ATOM   2117 O O   . VAL A 1 273 ? -11.986 -6.581  47.919 1.00 15.12 ? 273  VAL A O   1 
ATOM   2118 C CB  . VAL A 1 273 ? -14.518 -8.432  48.873 1.00 14.64 ? 273  VAL A CB  1 
ATOM   2119 C CG1 . VAL A 1 273 ? -13.207 -9.319  48.862 1.00 12.19 ? 273  VAL A CG1 1 
ATOM   2120 C CG2 . VAL A 1 273 ? -15.305 -8.636  50.139 1.00 13.81 ? 273  VAL A CG2 1 
ATOM   2121 N N   . VAL A 1 274 ? -13.651 -6.663  46.419 1.00 14.87 ? 274  VAL A N   1 
ATOM   2122 C CA  . VAL A 1 274 ? -12.772 -6.343  45.303 1.00 14.13 ? 274  VAL A CA  1 
ATOM   2123 C C   . VAL A 1 274 ? -12.134 -4.969  45.484 1.00 14.24 ? 274  VAL A C   1 
ATOM   2124 O O   . VAL A 1 274 ? -10.876 -4.831  45.305 1.00 12.14 ? 274  VAL A O   1 
ATOM   2125 C CB  . VAL A 1 274 ? -13.434 -6.540  43.903 1.00 15.11 ? 274  VAL A CB  1 
ATOM   2126 C CG1 . VAL A 1 274 ? -12.444 -6.150  42.790 1.00 12.52 ? 274  VAL A CG1 1 
ATOM   2127 C CG2 . VAL A 1 274 ? -13.882 -7.968  43.751 1.00 13.60 ? 274  VAL A CG2 1 
ATOM   2128 N N   . GLN A 1 275 ? -12.943 -3.970  45.884 1.00 12.82 ? 275  GLN A N   1 
ATOM   2129 C CA  . GLN A 1 275 ? -12.421 -2.608  46.204 1.00 14.11 ? 275  GLN A CA  1 
ATOM   2130 C C   . GLN A 1 275 ? -11.314 -2.614  47.291 1.00 13.81 ? 275  GLN A C   1 
ATOM   2131 O O   . GLN A 1 275 ? -10.324 -1.909  47.148 1.00 14.00 ? 275  GLN A O   1 
ATOM   2132 C CB  . GLN A 1 275 ? -13.547 -1.618  46.610 1.00 14.05 ? 275  GLN A CB  1 
ATOM   2133 C CG  . GLN A 1 275 ? -14.573 -1.328  45.503 1.00 14.40 ? 275  GLN A CG  1 
ATOM   2134 C CD  . GLN A 1 275 ? -15.872 -0.671  46.022 1.00 15.58 ? 275  GLN A CD  1 
ATOM   2135 O OE1 . GLN A 1 275 ? -16.119 -0.612  47.213 1.00 18.45 ? 275  GLN A OE1 1 
ATOM   2136 N NE2 . GLN A 1 275 ? -16.680 -0.189  45.117 1.00 15.86 ? 275  GLN A NE2 1 
ATOM   2137 N N   . GLU A 1 276 ? -11.516 -3.374  48.380 1.00 13.80 ? 276  GLU A N   1 
ATOM   2138 C CA  . GLU A 1 276 ? -10.515 -3.551  49.448 1.00 14.46 ? 276  GLU A CA  1 
ATOM   2139 C C   . GLU A 1 276 ? -9.229  -4.219  48.953 1.00 14.04 ? 276  GLU A C   1 
ATOM   2140 O O   . GLU A 1 276 ? -8.130  -3.778  49.287 1.00 14.45 ? 276  GLU A O   1 
ATOM   2141 C CB  . GLU A 1 276 ? -11.084 -4.386  50.619 1.00 15.55 ? 276  GLU A CB  1 
ATOM   2142 C CG  . GLU A 1 276 ? -12.151 -3.708  51.465 1.00 17.48 ? 276  GLU A CG  1 
ATOM   2143 C CD  . GLU A 1 276 ? -11.702 -2.388  52.074 1.00 23.43 ? 276  GLU A CD  1 
ATOM   2144 O OE1 . GLU A 1 276 ? -10.475 -2.194  52.288 1.00 24.38 ? 276  GLU A OE1 1 
ATOM   2145 O OE2 . GLU A 1 276 ? -12.592 -1.546  52.374 1.00 26.39 ? 276  GLU A OE2 1 
ATOM   2146 N N   . TYR A 1 277 ? -9.373  -5.276  48.152 1.00 13.96 ? 277  TYR A N   1 
ATOM   2147 C CA  . TYR A 1 277 ? -8.216  -5.923  47.517 1.00 13.15 ? 277  TYR A CA  1 
ATOM   2148 C C   . TYR A 1 277 ? -7.428  -4.972  46.639 1.00 13.58 ? 277  TYR A C   1 
ATOM   2149 O O   . TYR A 1 277 ? -6.192  -4.872  46.781 1.00 11.73 ? 277  TYR A O   1 
ATOM   2150 C CB  . TYR A 1 277 ? -8.632  -7.148  46.704 1.00 14.52 ? 277  TYR A CB  1 
ATOM   2151 C CG  . TYR A 1 277 ? -7.507  -7.811  45.911 1.00 14.03 ? 277  TYR A CG  1 
ATOM   2152 C CD1 . TYR A 1 277 ? -6.335  -8.267  46.540 1.00 14.54 ? 277  TYR A CD1 1 
ATOM   2153 C CD2 . TYR A 1 277 ? -7.623  -7.980  44.545 1.00 15.70 ? 277  TYR A CD2 1 
ATOM   2154 C CE1 . TYR A 1 277 ? -5.302  -8.885  45.800 1.00 14.58 ? 277  TYR A CE1 1 
ATOM   2155 C CE2 . TYR A 1 277 ? -6.625  -8.605  43.809 1.00 15.63 ? 277  TYR A CE2 1 
ATOM   2156 C CZ  . TYR A 1 277 ? -5.470  -9.041  44.433 1.00 16.72 ? 277  TYR A CZ  1 
ATOM   2157 O OH  . TYR A 1 277 ? -4.490  -9.627  43.645 1.00 18.46 ? 277  TYR A OH  1 
ATOM   2158 N N   . LEU A 1 278 ? -8.124  -4.272  45.733 1.00 12.52 ? 278  LEU A N   1 
ATOM   2159 C CA  . LEU A 1 278 ? -7.461  -3.366  44.792 1.00 13.94 ? 278  LEU A CA  1 
ATOM   2160 C C   . LEU A 1 278 ? -6.900  -2.125  45.461 1.00 14.07 ? 278  LEU A C   1 
ATOM   2161 O O   . LEU A 1 278 ? -5.935  -1.542  44.965 1.00 15.07 ? 278  LEU A O   1 
ATOM   2162 C CB  . LEU A 1 278 ? -8.360  -3.023  43.577 1.00 13.59 ? 278  LEU A CB  1 
ATOM   2163 C CG  . LEU A 1 278 ? -8.831  -4.269  42.801 1.00 13.89 ? 278  LEU A CG  1 
ATOM   2164 C CD1 . LEU A 1 278 ? -9.687  -3.822  41.620 1.00 11.74 ? 278  LEU A CD1 1 
ATOM   2165 C CD2 . LEU A 1 278 ? -7.611  -5.099  42.358 1.00 13.07 ? 278  LEU A CD2 1 
ATOM   2166 N N   . GLU A 1 279 ? -7.493  -1.716  46.583 1.00 15.08 ? 279  GLU A N   1 
ATOM   2167 C CA  . GLU A 1 279 ? -6.885  -0.687  47.432 1.00 16.63 ? 279  GLU A CA  1 
ATOM   2168 C C   . GLU A 1 279 ? -5.475  -1.100  47.882 1.00 16.38 ? 279  GLU A C   1 
ATOM   2169 O O   . GLU A 1 279 ? -4.551  -0.283  47.907 1.00 16.68 ? 279  GLU A O   1 
ATOM   2170 C CB  . GLU A 1 279 ? -7.752  -0.345  48.647 1.00 17.10 ? 279  GLU A CB  1 
ATOM   2171 C CG  . GLU A 1 279 ? -7.064  0.523   49.740 1.00 20.17 ? 279  GLU A CG  1 
ATOM   2172 C CD  . GLU A 1 279 ? -6.650  1.920   49.279 1.00 27.70 ? 279  GLU A CD  1 
ATOM   2173 O OE1 . GLU A 1 279 ? -7.191  2.408   48.265 1.00 32.30 ? 279  GLU A OE1 1 
ATOM   2174 O OE2 . GLU A 1 279 ? -5.793  2.557   49.947 1.00 29.32 ? 279  GLU A OE2 1 
ATOM   2175 N N   . LEU A 1 280 ? -5.330  -2.354  48.263 1.00 16.95 ? 280  LEU A N   1 
ATOM   2176 C CA  . LEU A 1 280 ? -4.008  -2.864  48.648 1.00 17.32 ? 280  LEU A CA  1 
ATOM   2177 C C   . LEU A 1 280 ? -3.063  -3.039  47.440 1.00 17.21 ? 280  LEU A C   1 
ATOM   2178 O O   . LEU A 1 280 ? -2.011  -2.422  47.382 1.00 17.40 ? 280  LEU A O   1 
ATOM   2179 C CB  . LEU A 1 280 ? -4.136  -4.161  49.477 1.00 16.17 ? 280  LEU A CB  1 
ATOM   2180 C CG  . LEU A 1 280 ? -2.752  -4.787  49.764 1.00 17.07 ? 280  LEU A CG  1 
ATOM   2181 C CD1 . LEU A 1 280 ? -1.953  -4.044  50.862 1.00 14.42 ? 280  LEU A CD1 1 
ATOM   2182 C CD2 . LEU A 1 280 ? -2.913  -6.249  50.031 1.00 17.61 ? 280  LEU A CD2 1 
ATOM   2183 N N   . ILE A 1 281 ? -3.422  -3.866  46.467 1.00 17.43 ? 281  ILE A N   1 
ATOM   2184 C CA  . ILE A 1 281 ? -2.446  -4.212  45.416 1.00 17.93 ? 281  ILE A CA  1 
ATOM   2185 C C   . ILE A 1 281 ? -2.301  -3.184  44.295 1.00 17.98 ? 281  ILE A C   1 
ATOM   2186 O O   . ILE A 1 281 ? -1.305  -3.230  43.552 1.00 18.83 ? 281  ILE A O   1 
ATOM   2187 C CB  . ILE A 1 281 ? -2.732  -5.572  44.724 1.00 18.31 ? 281  ILE A CB  1 
ATOM   2188 C CG1 . ILE A 1 281 ? -4.149  -5.572  44.185 1.00 17.32 ? 281  ILE A CG1 1 
ATOM   2189 C CG2 . ILE A 1 281 ? -2.404  -6.770  45.629 1.00 21.53 ? 281  ILE A CG2 1 
ATOM   2190 C CD1 . ILE A 1 281 ? -4.209  -5.976  42.789 1.00 17.23 ? 281  ILE A CD1 1 
ATOM   2191 N N   . GLY A 1 282 ? -3.274  -2.279  44.140 1.00 16.94 ? 282  GLY A N   1 
ATOM   2192 C CA  . GLY A 1 282 ? -3.218  -1.326  43.025 1.00 16.19 ? 282  GLY A CA  1 
ATOM   2193 C C   . GLY A 1 282 ? -4.427  -1.440  42.099 1.00 16.39 ? 282  GLY A C   1 
ATOM   2194 O O   . GLY A 1 282 ? -4.718  -2.496  41.555 1.00 14.24 ? 282  GLY A O   1 
ATOM   2195 N N   . ARG A 1 283 ? -5.115  -0.320  41.920 1.00 16.85 ? 283  ARG A N   1 
ATOM   2196 C CA  . ARG A 1 283 ? -6.270  -0.263  41.039 1.00 17.60 ? 283  ARG A CA  1 
ATOM   2197 C C   . ARG A 1 283 ? -5.789  -0.193  39.611 1.00 17.82 ? 283  ARG A C   1 
ATOM   2198 O O   . ARG A 1 283 ? -4.701  0.317   39.355 1.00 19.32 ? 283  ARG A O   1 
ATOM   2199 C CB  . ARG A 1 283 ? -7.172  0.923   41.401 1.00 16.29 ? 283  ARG A CB  1 
ATOM   2200 C CG  . ARG A 1 283 ? -8.000  0.634   42.619 1.00 15.86 ? 283  ARG A CG  1 
ATOM   2201 C CD  . ARG A 1 283 ? -8.949  1.805   43.018 1.00 18.52 ? 283  ARG A CD  1 
ATOM   2202 N NE  . ARG A 1 283 ? -8.214  3.004   43.393 1.00 20.61 ? 283  ARG A NE  1 
ATOM   2203 C CZ  . ARG A 1 283 ? -7.796  3.302   44.618 1.00 23.26 ? 283  ARG A CZ  1 
ATOM   2204 N NH1 . ARG A 1 283 ? -8.035  2.500   45.638 1.00 24.76 ? 283  ARG A NH1 1 
ATOM   2205 N NH2 . ARG A 1 283 ? -7.136  4.425   44.826 1.00 25.32 ? 283  ARG A NH2 1 
ATOM   2206 N N   . PRO A 1 284 ? -6.581  -0.745  38.682 1.00 18.52 ? 284  PRO A N   1 
ATOM   2207 C CA  . PRO A 1 284 ? -6.217  -0.772  37.261 1.00 18.23 ? 284  PRO A CA  1 
ATOM   2208 C C   . PRO A 1 284 ? -6.052  0.613   36.667 1.00 18.71 ? 284  PRO A C   1 
ATOM   2209 O O   . PRO A 1 284 ? -6.743  1.564   37.090 1.00 18.73 ? 284  PRO A O   1 
ATOM   2210 C CB  . PRO A 1 284 ? -7.413  -1.453  36.601 1.00 18.67 ? 284  PRO A CB  1 
ATOM   2211 C CG  . PRO A 1 284 ? -8.535  -1.363  37.609 1.00 17.83 ? 284  PRO A CG  1 
ATOM   2212 C CD  . PRO A 1 284 ? -7.887  -1.385  38.938 1.00 17.94 ? 284  PRO A CD  1 
ATOM   2213 N N   . ALA A 1 285 ? -5.130  0.723   35.703 1.00 18.12 ? 285  ALA A N   1 
ATOM   2214 C CA  . ALA A 1 285 ? -4.932  1.936   34.934 1.00 17.58 ? 285  ALA A CA  1 
ATOM   2215 C C   . ALA A 1 285 ? -6.232  2.289   34.232 1.00 17.27 ? 285  ALA A C   1 
ATOM   2216 O O   . ALA A 1 285 ? -6.953  1.389   33.796 1.00 17.62 ? 285  ALA A O   1 
ATOM   2217 C CB  . ALA A 1 285 ? -3.871  1.700   33.899 1.00 17.73 ? 285  ALA A CB  1 
ATOM   2218 N N   . LEU A 1 286 ? -6.524  3.575   34.094 1.00 16.52 ? 286  LEU A N   1 
ATOM   2219 C CA  . LEU A 1 286 ? -7.638  3.980   33.228 1.00 16.61 ? 286  LEU A CA  1 
ATOM   2220 C C   . LEU A 1 286 ? -7.112  3.785   31.810 1.00 16.11 ? 286  LEU A C   1 
ATOM   2221 O O   . LEU A 1 286 ? -6.049  4.294   31.483 1.00 16.32 ? 286  LEU A O   1 
ATOM   2222 C CB  . LEU A 1 286 ? -8.018  5.447   33.487 1.00 16.65 ? 286  LEU A CB  1 
ATOM   2223 C CG  . LEU A 1 286 ? -9.194  6.072   32.709 1.00 17.13 ? 286  LEU A CG  1 
ATOM   2224 C CD1 . LEU A 1 286 ? -10.547 5.431   33.084 1.00 18.91 ? 286  LEU A CD1 1 
ATOM   2225 C CD2 . LEU A 1 286 ? -9.227  7.562   33.026 1.00 16.58 ? 286  LEU A CD2 1 
ATOM   2226 N N   . PRO A 1 287 ? -7.817  3.015   30.971 1.00 16.33 ? 287  PRO A N   1 
ATOM   2227 C CA  . PRO A 1 287 ? -7.205  2.844   29.651 1.00 16.29 ? 287  PRO A CA  1 
ATOM   2228 C C   . PRO A 1 287 ? -7.399  4.061   28.743 1.00 16.16 ? 287  PRO A C   1 
ATOM   2229 O O   . PRO A 1 287 ? -8.199  4.972   29.049 1.00 16.36 ? 287  PRO A O   1 
ATOM   2230 C CB  . PRO A 1 287 ? -7.942  1.649   29.079 1.00 16.84 ? 287  PRO A CB  1 
ATOM   2231 C CG  . PRO A 1 287 ? -9.320  1.740   29.694 1.00 16.41 ? 287  PRO A CG  1 
ATOM   2232 C CD  . PRO A 1 287 ? -9.108  2.313   31.085 1.00 16.11 ? 287  PRO A CD  1 
ATOM   2233 N N   . SER A 1 288 ? -6.661  4.076   27.639 1.00 15.32 ? 288  SER A N   1 
ATOM   2234 C CA  . SER A 1 288 ? -6.904  5.025   26.587 1.00 15.04 ? 288  SER A CA  1 
ATOM   2235 C C   . SER A 1 288 ? -8.335  4.714   26.088 1.00 15.62 ? 288  SER A C   1 
ATOM   2236 O O   . SER A 1 288 ? -8.783  3.561   26.075 1.00 14.35 ? 288  SER A O   1 
ATOM   2237 C CB  . SER A 1 288 ? -5.884  4.876   25.470 1.00 15.34 ? 288  SER A CB  1 
ATOM   2238 O OG  . SER A 1 288 ? -4.552  5.239   25.884 1.00 14.23 ? 288  SER A OG  1 
ATOM   2239 N N   . TYR A 1 289 ? -9.075  5.741   25.710 1.00 15.52 ? 289  TYR A N   1 
ATOM   2240 C CA  . TYR A 1 289 ? -10.445 5.481   25.288 1.00 15.84 ? 289  TYR A CA  1 
ATOM   2241 C C   . TYR A 1 289 ? -10.463 4.625   23.999 1.00 15.26 ? 289  TYR A C   1 
ATOM   2242 O O   . TYR A 1 289 ? -11.362 3.802   23.796 1.00 14.45 ? 289  TYR A O   1 
ATOM   2243 C CB  . TYR A 1 289 ? -11.139 6.812   25.107 1.00 16.31 ? 289  TYR A CB  1 
ATOM   2244 C CG  . TYR A 1 289 ? -12.626 6.765   24.940 1.00 15.94 ? 289  TYR A CG  1 
ATOM   2245 C CD1 . TYR A 1 289 ? -13.457 7.077   25.990 1.00 16.50 ? 289  TYR A CD1 1 
ATOM   2246 C CD2 . TYR A 1 289 ? -13.202 6.490   23.711 1.00 18.66 ? 289  TYR A CD2 1 
ATOM   2247 C CE1 . TYR A 1 289 ? -14.867 7.117   25.822 1.00 13.52 ? 289  TYR A CE1 1 
ATOM   2248 C CE2 . TYR A 1 289 ? -14.590 6.534   23.526 1.00 17.64 ? 289  TYR A CE2 1 
ATOM   2249 C CZ  . TYR A 1 289 ? -15.408 6.840   24.597 1.00 15.54 ? 289  TYR A CZ  1 
ATOM   2250 O OH  . TYR A 1 289 ? -16.779 6.864   24.428 1.00 18.00 ? 289  TYR A OH  1 
ATOM   2251 N N   . TRP A 1 290 ? -9.459  4.783   23.132 1.00 15.15 ? 290  TRP A N   1 
ATOM   2252 C CA  . TRP A 1 290 ? -9.382  3.941   21.903 1.00 15.35 ? 290  TRP A CA  1 
ATOM   2253 C C   . TRP A 1 290 ? -9.167  2.435   22.129 1.00 15.54 ? 290  TRP A C   1 
ATOM   2254 O O   . TRP A 1 290 ? -9.590  1.603   21.308 1.00 15.49 ? 290  TRP A O   1 
ATOM   2255 C CB  . TRP A 1 290 ? -8.346  4.469   20.932 1.00 16.40 ? 290  TRP A CB  1 
ATOM   2256 C CG  . TRP A 1 290 ? -6.941  4.569   21.447 1.00 15.29 ? 290  TRP A CG  1 
ATOM   2257 C CD1 . TRP A 1 290 ? -6.334  5.674   21.926 1.00 15.88 ? 290  TRP A CD1 1 
ATOM   2258 C CD2 . TRP A 1 290 ? -5.956  3.519   21.468 1.00 15.36 ? 290  TRP A CD2 1 
ATOM   2259 N NE1 . TRP A 1 290 ? -5.007  5.396   22.232 1.00 16.60 ? 290  TRP A NE1 1 
ATOM   2260 C CE2 . TRP A 1 290 ? -4.756  4.079   21.963 1.00 17.19 ? 290  TRP A CE2 1 
ATOM   2261 C CE3 . TRP A 1 290 ? -5.974  2.163   21.115 1.00 13.75 ? 290  TRP A CE3 1 
ATOM   2262 C CZ2 . TRP A 1 290 ? -3.586  3.323   22.135 1.00 15.13 ? 290  TRP A CZ2 1 
ATOM   2263 C CZ3 . TRP A 1 290 ? -4.796  1.421   21.254 1.00 16.60 ? 290  TRP A CZ3 1 
ATOM   2264 C CH2 . TRP A 1 290 ? -3.630  2.010   21.770 1.00 15.93 ? 290  TRP A CH2 1 
ATOM   2265 N N   . ALA A 1 291 ? -8.522  2.080   23.244 1.00 14.63 ? 291  ALA A N   1 
ATOM   2266 C CA  . ALA A 1 291 ? -8.325  0.656   23.616 1.00 14.25 ? 291  ALA A CA  1 
ATOM   2267 C C   . ALA A 1 291 ? -9.668  -0.075  23.900 1.00 13.89 ? 291  ALA A C   1 
ATOM   2268 O O   . ALA A 1 291 ? -9.756  -1.314  23.917 1.00 12.95 ? 291  ALA A O   1 
ATOM   2269 C CB  . ALA A 1 291 ? -7.428  0.571   24.793 1.00 12.75 ? 291  ALA A CB  1 
ATOM   2270 N N   . LEU A 1 292 ? -10.709 0.704   24.105 1.00 14.83 ? 292  LEU A N   1 
ATOM   2271 C CA  . LEU A 1 292 ? -12.049 0.158   24.384 1.00 15.81 ? 292  LEU A CA  1 
ATOM   2272 C C   . LEU A 1 292 ? -12.678 -0.266  23.096 1.00 15.95 ? 292  LEU A C   1 
ATOM   2273 O O   . LEU A 1 292 ? -13.685 -0.974  23.090 1.00 17.23 ? 292  LEU A O   1 
ATOM   2274 C CB  . LEU A 1 292 ? -12.949 1.203   25.060 1.00 16.51 ? 292  LEU A CB  1 
ATOM   2275 C CG  . LEU A 1 292 ? -12.521 1.808   26.402 1.00 20.45 ? 292  LEU A CG  1 
ATOM   2276 C CD1 . LEU A 1 292 ? -13.596 2.806   26.889 1.00 21.77 ? 292  LEU A CD1 1 
ATOM   2277 C CD2 . LEU A 1 292 ? -12.337 0.745   27.402 1.00 21.53 ? 292  LEU A CD2 1 
ATOM   2278 N N   . GLY A 1 293 ? -12.111 0.205   21.991 1.00 16.24 ? 293  GLY A N   1 
ATOM   2279 C CA  . GLY A 1 293 ? -12.544 -0.209  20.665 1.00 14.88 ? 293  GLY A CA  1 
ATOM   2280 C C   . GLY A 1 293 ? -12.243 -1.641  20.301 1.00 15.02 ? 293  GLY A C   1 
ATOM   2281 O O   . GLY A 1 293 ? -11.699 -2.441  21.108 1.00 14.08 ? 293  GLY A O   1 
ATOM   2282 N N   . PHE A 1 294 ? -12.626 -1.989  19.076 1.00 14.50 ? 294  PHE A N   1 
ATOM   2283 C CA  . PHE A 1 294 ? -12.470 -3.335  18.608 1.00 13.93 ? 294  PHE A CA  1 
ATOM   2284 C C   . PHE A 1 294 ? -11.068 -3.444  18.043 1.00 14.65 ? 294  PHE A C   1 
ATOM   2285 O O   . PHE A 1 294 ? -10.620 -2.539  17.344 1.00 14.41 ? 294  PHE A O   1 
ATOM   2286 C CB  . PHE A 1 294 ? -13.499 -3.649  17.547 1.00 14.10 ? 294  PHE A CB  1 
ATOM   2287 C CG  . PHE A 1 294 ? -13.354 -5.011  16.946 1.00 15.20 ? 294  PHE A CG  1 
ATOM   2288 C CD1 . PHE A 1 294 ? -13.546 -6.150  17.721 1.00 15.07 ? 294  PHE A CD1 1 
ATOM   2289 C CD2 . PHE A 1 294 ? -13.026 -5.151  15.600 1.00 17.35 ? 294  PHE A CD2 1 
ATOM   2290 C CE1 . PHE A 1 294 ? -13.400 -7.412  17.168 1.00 17.29 ? 294  PHE A CE1 1 
ATOM   2291 C CE2 . PHE A 1 294 ? -12.896 -6.408  15.023 1.00 19.37 ? 294  PHE A CE2 1 
ATOM   2292 C CZ  . PHE A 1 294 ? -13.093 -7.549  15.813 1.00 17.67 ? 294  PHE A CZ  1 
ATOM   2293 N N   . HIS A 1 295 ? -10.372 -4.526  18.385 1.00 14.44 ? 295  HIS A N   1 
ATOM   2294 C CA  . HIS A 1 295 ? -8.966  -4.731  17.950 1.00 13.47 ? 295  HIS A CA  1 
ATOM   2295 C C   . HIS A 1 295 ? -8.952  -5.904  16.934 1.00 14.26 ? 295  HIS A C   1 
ATOM   2296 O O   . HIS A 1 295 ? -9.653  -6.892  17.107 1.00 13.41 ? 295  HIS A O   1 
ATOM   2297 C CB  . HIS A 1 295 ? -8.106  -5.145  19.159 1.00 13.71 ? 295  HIS A CB  1 
ATOM   2298 C CG  . HIS A 1 295 ? -7.914  -4.093  20.214 1.00 12.85 ? 295  HIS A CG  1 
ATOM   2299 N ND1 . HIS A 1 295 ? -8.953  -3.568  20.963 1.00 15.28 ? 295  HIS A ND1 1 
ATOM   2300 C CD2 . HIS A 1 295 ? -6.786  -3.536  20.705 1.00 9.39  ? 295  HIS A CD2 1 
ATOM   2301 C CE1 . HIS A 1 295 ? -8.472  -2.699  21.836 1.00 12.20 ? 295  HIS A CE1 1 
ATOM   2302 N NE2 . HIS A 1 295 ? -7.155  -2.667  21.704 1.00 15.79 ? 295  HIS A NE2 1 
ATOM   2303 N N   . LEU A 1 296 ? -8.150  -5.817  15.886 1.00 15.44 ? 296  LEU A N   1 
ATOM   2304 C CA  . LEU A 1 296 ? -8.063  -6.885  14.892 1.00 16.16 ? 296  LEU A CA  1 
ATOM   2305 C C   . LEU A 1 296 ? -6.608  -7.348  14.798 1.00 17.43 ? 296  LEU A C   1 
ATOM   2306 O O   . LEU A 1 296 ? -5.674  -6.555  14.842 1.00 17.70 ? 296  LEU A O   1 
ATOM   2307 C CB  . LEU A 1 296 ? -8.600  -6.416  13.511 1.00 16.52 ? 296  LEU A CB  1 
ATOM   2308 C CG  . LEU A 1 296 ? -8.876  -7.516  12.457 1.00 18.19 ? 296  LEU A CG  1 
ATOM   2309 C CD1 . LEU A 1 296 ? -9.828  -8.576  13.012 1.00 13.19 ? 296  LEU A CD1 1 
ATOM   2310 C CD2 . LEU A 1 296 ? -9.393  -6.978  11.140 1.00 15.99 ? 296  LEU A CD2 1 
ATOM   2311 N N   . SER A 1 297 ? -6.410  -8.644  14.640 1.00 19.40 ? 297  SER A N   1 
ATOM   2312 C CA  . SER A 1 297 ? -5.062  -9.200  14.693 1.00 20.30 ? 297  SER A CA  1 
ATOM   2313 C C   . SER A 1 297 ? -5.037  -10.551 13.999 1.00 20.06 ? 297  SER A C   1 
ATOM   2314 O O   . SER A 1 297 ? -6.087  -11.199 13.834 1.00 20.01 ? 297  SER A O   1 
ATOM   2315 C CB  . SER A 1 297 ? -4.679  -9.399  16.173 1.00 20.45 ? 297  SER A CB  1 
ATOM   2316 O OG  . SER A 1 297 ? -3.327  -9.838  16.347 1.00 24.23 ? 297  SER A OG  1 
ATOM   2317 N N   . ARG A 1 298 ? -3.829  -10.994 13.647 1.00 19.58 ? 298  ARG A N   1 
ATOM   2318 C CA  . ARG A 1 298 ? -3.576  -12.408 13.394 1.00 19.56 ? 298  ARG A CA  1 
ATOM   2319 C C   . ARG A 1 298 ? -2.086  -12.697 13.409 1.00 19.78 ? 298  ARG A C   1 
ATOM   2320 O O   . ARG A 1 298 ? -1.245  -11.807 13.231 1.00 19.70 ? 298  ARG A O   1 
ATOM   2321 C CB  . ARG A 1 298 ? -4.234  -12.942 12.104 1.00 19.56 ? 298  ARG A CB  1 
ATOM   2322 C CG  . ARG A 1 298 ? -3.379  -12.813 10.866 1.00 20.74 ? 298  ARG A CG  1 
ATOM   2323 C CD  . ARG A 1 298 ? -3.762  -13.729 9.748  1.00 21.16 ? 298  ARG A CD  1 
ATOM   2324 N NE  . ARG A 1 298 ? -3.482  -15.139 10.009 1.00 21.55 ? 298  ARG A NE  1 
ATOM   2325 C CZ  . ARG A 1 298 ? -4.220  -16.123 9.514  1.00 21.52 ? 298  ARG A CZ  1 
ATOM   2326 N NH1 . ARG A 1 298 ? -5.271  -15.840 8.760  1.00 20.44 ? 298  ARG A NH1 1 
ATOM   2327 N NH2 . ARG A 1 298 ? -3.936  -17.387 9.788  1.00 22.90 ? 298  ARG A NH2 1 
ATOM   2328 N N   . TYR A 1 299 ? -1.779  -13.948 13.692 1.00 20.15 ? 299  TYR A N   1 
ATOM   2329 C CA  . TYR A 1 299 ? -0.428  -14.455 13.619 1.00 21.20 ? 299  TYR A CA  1 
ATOM   2330 C C   . TYR A 1 299 ? -0.166  -14.767 12.139 1.00 21.38 ? 299  TYR A C   1 
ATOM   2331 O O   . TYR A 1 299 ? -0.881  -15.540 11.523 1.00 21.26 ? 299  TYR A O   1 
ATOM   2332 C CB  . TYR A 1 299 ? -0.339  -15.681 14.545 1.00 21.82 ? 299  TYR A CB  1 
ATOM   2333 C CG  . TYR A 1 299 ? 1.031   -16.303 14.739 1.00 21.43 ? 299  TYR A CG  1 
ATOM   2334 C CD1 . TYR A 1 299 ? 1.158   -17.524 15.395 1.00 21.39 ? 299  TYR A CD1 1 
ATOM   2335 C CD2 . TYR A 1 299 ? 2.186   -15.698 14.246 1.00 21.85 ? 299  TYR A CD2 1 
ATOM   2336 C CE1 . TYR A 1 299 ? 2.421   -18.134 15.575 1.00 21.64 ? 299  TYR A CE1 1 
ATOM   2337 C CE2 . TYR A 1 299 ? 3.436   -16.294 14.416 1.00 22.66 ? 299  TYR A CE2 1 
ATOM   2338 C CZ  . TYR A 1 299 ? 3.544   -17.507 15.069 1.00 22.02 ? 299  TYR A CZ  1 
ATOM   2339 O OH  . TYR A 1 299 ? 4.791   -18.069 15.228 1.00 23.70 ? 299  TYR A OH  1 
ATOM   2340 N N   . GLU A 1 300 ? 0.811   -14.086 11.549 1.00 21.74 ? 300  GLU A N   1 
ATOM   2341 C CA  . GLU A 1 300 ? 1.211   -14.348 10.170 1.00 22.31 ? 300  GLU A CA  1 
ATOM   2342 C C   . GLU A 1 300 ? 0.208   -13.883 9.099  1.00 21.68 ? 300  GLU A C   1 
ATOM   2343 O O   . GLU A 1 300 ? -0.437  -14.698 8.430  1.00 21.69 ? 300  GLU A O   1 
ATOM   2344 C CB  . GLU A 1 300 ? 1.613   -15.817 9.953  1.00 22.58 ? 300  GLU A CB  1 
ATOM   2345 C CG  . GLU A 1 300 ? 2.820   -16.263 10.755 1.00 26.28 ? 300  GLU A CG  1 
ATOM   2346 C CD  . GLU A 1 300 ? 4.161   -15.728 10.236 1.00 28.99 ? 300  GLU A CD  1 
ATOM   2347 O OE1 . GLU A 1 300 ? 4.288   -15.458 9.015  1.00 31.50 ? 300  GLU A OE1 1 
ATOM   2348 O OE2 . GLU A 1 300 ? 5.092   -15.590 11.075 1.00 31.23 ? 300  GLU A OE2 1 
ATOM   2349 N N   . TYR A 1 301 ? 0.081   -12.573 8.949  1.00 21.82 ? 301  TYR A N   1 
ATOM   2350 C CA  . TYR A 1 301 ? -0.404  -12.015 7.696  1.00 21.03 ? 301  TYR A CA  1 
ATOM   2351 C C   . TYR A 1 301 ? 0.644   -12.354 6.647  1.00 21.63 ? 301  TYR A C   1 
ATOM   2352 O O   . TYR A 1 301 ? 0.315   -12.670 5.508  1.00 21.25 ? 301  TYR A O   1 
ATOM   2353 C CB  . TYR A 1 301 ? -0.590  -10.510 7.815  1.00 20.71 ? 301  TYR A CB  1 
ATOM   2354 C CG  . TYR A 1 301 ? -1.763  -10.103 8.684  1.00 20.93 ? 301  TYR A CG  1 
ATOM   2355 C CD1 . TYR A 1 301 ? -3.078  -10.276 8.230  1.00 20.61 ? 301  TYR A CD1 1 
ATOM   2356 C CD2 . TYR A 1 301 ? -1.565  -9.528  9.947  1.00 20.44 ? 301  TYR A CD2 1 
ATOM   2357 C CE1 . TYR A 1 301 ? -4.164  -9.892  9.008  1.00 20.78 ? 301  TYR A CE1 1 
ATOM   2358 C CE2 . TYR A 1 301 ? -2.669  -9.130  10.745 1.00 20.36 ? 301  TYR A CE2 1 
ATOM   2359 C CZ  . TYR A 1 301 ? -3.957  -9.326  10.263 1.00 19.47 ? 301  TYR A CZ  1 
ATOM   2360 O OH  . TYR A 1 301 ? -5.062  -8.968  11.016 1.00 19.99 ? 301  TYR A OH  1 
ATOM   2361 N N   . GLY A 1 302 ? 1.913   -12.318 7.057  1.00 22.36 ? 302  GLY A N   1 
ATOM   2362 C CA  . GLY A 1 302 ? 3.002   -12.841 6.237  1.00 23.12 ? 302  GLY A CA  1 
ATOM   2363 C C   . GLY A 1 302 ? 3.679   -11.702 5.518  1.00 23.66 ? 302  GLY A C   1 
ATOM   2364 O O   . GLY A 1 302 ? 4.912   -11.612 5.470  1.00 24.18 ? 302  GLY A O   1 
ATOM   2365 N N   . THR A 1 303 ? 2.853   -10.840 4.942  1.00 23.68 ? 303  THR A N   1 
ATOM   2366 C CA  . THR A 1 303 ? 3.298   -9.626  4.270  1.00 24.15 ? 303  THR A CA  1 
ATOM   2367 C C   . THR A 1 303 ? 2.404   -8.453  4.672  1.00 24.53 ? 303  THR A C   1 
ATOM   2368 O O   . THR A 1 303 ? 1.229   -8.642  5.064  1.00 23.26 ? 303  THR A O   1 
ATOM   2369 C CB  . THR A 1 303 ? 3.254   -9.737  2.712  1.00 24.30 ? 303  THR A CB  1 
ATOM   2370 O OG1 . THR A 1 303 ? 1.901   -9.886  2.277  1.00 25.02 ? 303  THR A OG1 1 
ATOM   2371 C CG2 . THR A 1 303 ? 4.063   -10.914 2.201  1.00 23.21 ? 303  THR A CG2 1 
ATOM   2372 N N   . LEU A 1 304 ? 2.974   -7.252  4.569  1.00 24.46 ? 304  LEU A N   1 
ATOM   2373 C CA  . LEU A 1 304 ? 2.226   -6.019  4.765  1.00 25.04 ? 304  LEU A CA  1 
ATOM   2374 C C   . LEU A 1 304 ? 1.037   -5.892  3.827  1.00 25.14 ? 304  LEU A C   1 
ATOM   2375 O O   . LEU A 1 304 ? -0.021  -5.444  4.255  1.00 25.71 ? 304  LEU A O   1 
ATOM   2376 C CB  . LEU A 1 304 ? 3.121   -4.795  4.634  1.00 24.40 ? 304  LEU A CB  1 
ATOM   2377 C CG  . LEU A 1 304 ? 2.465   -3.462  5.005  1.00 23.96 ? 304  LEU A CG  1 
ATOM   2378 C CD1 . LEU A 1 304 ? 1.851   -3.520  6.417  1.00 23.57 ? 304  LEU A CD1 1 
ATOM   2379 C CD2 . LEU A 1 304 ? 3.458   -2.321  4.919  1.00 25.22 ? 304  LEU A CD2 1 
ATOM   2380 N N   . ASP A 1 305 ? 1.217   -6.284  2.562  1.00 25.86 ? 305  ASP A N   1 
ATOM   2381 C CA  . ASP A 1 305 ? 0.145   -6.306  1.565  1.00 25.79 ? 305  ASP A CA  1 
ATOM   2382 C C   . ASP A 1 305 ? -1.042  -7.172  2.016  1.00 25.35 ? 305  ASP A C   1 
ATOM   2383 O O   . ASP A 1 305 ? -2.204  -6.865  1.713  1.00 24.14 ? 305  ASP A O   1 
ATOM   2384 C CB  . ASP A 1 305 ? 0.666   -6.851  0.241  1.00 27.17 ? 305  ASP A CB  1 
ATOM   2385 C CG  . ASP A 1 305 ? 1.655   -5.900  -0.473 1.00 30.36 ? 305  ASP A CG  1 
ATOM   2386 O OD1 . ASP A 1 305 ? 1.935   -4.776  0.007  1.00 33.88 ? 305  ASP A OD1 1 
ATOM   2387 O OD2 . ASP A 1 305 ? 2.150   -6.295  -1.552 1.00 33.85 ? 305  ASP A OD2 1 
ATOM   2388 N N   . ASN A 1 306 ? -0.732  -8.278  2.691  1.00 24.75 ? 306  ASN A N   1 
ATOM   2389 C CA  . ASN A 1 306 ? -1.756  -9.176  3.238  1.00 25.16 ? 306  ASN A CA  1 
ATOM   2390 C C   . ASN A 1 306 ? -2.509  -8.519  4.397  1.00 25.16 ? 306  ASN A C   1 
ATOM   2391 O O   . ASN A 1 306 ? -3.758  -8.589  4.454  1.00 25.42 ? 306  ASN A O   1 
ATOM   2392 C CB  . ASN A 1 306 ? -1.139  -10.515 3.663  1.00 25.27 ? 306  ASN A CB  1 
ATOM   2393 C CG  . ASN A 1 306 ? -0.897  -11.464 2.479  1.00 26.21 ? 306  ASN A CG  1 
ATOM   2394 O OD1 . ASN A 1 306 ? -1.415  -11.263 1.379  1.00 26.76 ? 306  ASN A OD1 1 
ATOM   2395 N ND2 . ASN A 1 306 ? -0.092  -12.500 2.709  1.00 28.87 ? 306  ASN A ND2 1 
ATOM   2396 N N   . MET A 1 307 ? -1.755  -7.870  5.293  1.00 24.68 ? 307  MET A N   1 
ATOM   2397 C CA  . MET A 1 307 ? -2.317  -7.088  6.409  1.00 25.37 ? 307  MET A CA  1 
ATOM   2398 C C   . MET A 1 307 ? -3.179  -5.945  5.884  1.00 25.28 ? 307  MET A C   1 
ATOM   2399 O O   . MET A 1 307 ? -4.330  -5.794  6.317  1.00 25.62 ? 307  MET A O   1 
ATOM   2400 C CB  . MET A 1 307 ? -1.209  -6.559  7.339  1.00 25.25 ? 307  MET A CB  1 
ATOM   2401 C CG  . MET A 1 307 ? -1.710  -5.809  8.603  1.00 25.06 ? 307  MET A CG  1 
ATOM   2402 S SD  . MET A 1 307 ? -0.374  -5.139  9.592  1.00 28.05 ? 307  MET A SD  1 
ATOM   2403 C CE  . MET A 1 307 ? 0.378   -6.591  10.300 1.00 27.55 ? 307  MET A CE  1 
ATOM   2404 N N   . ARG A 1 308 ? -2.631  -5.160  4.946  1.00 24.59 ? 308  ARG A N   1 
ATOM   2405 C CA  . ARG A 1 308 ? -3.342  -4.050  4.313  1.00 24.53 ? 308  ARG A CA  1 
ATOM   2406 C C   . ARG A 1 308 ? -4.656  -4.515  3.701  1.00 24.02 ? 308  ARG A C   1 
ATOM   2407 O O   . ARG A 1 308 ? -5.664  -3.836  3.823  1.00 23.40 ? 308  ARG A O   1 
ATOM   2408 C CB  . ARG A 1 308 ? -2.500  -3.395  3.212  1.00 25.37 ? 308  ARG A CB  1 
ATOM   2409 C CG  . ARG A 1 308 ? -1.445  -2.390  3.642  1.00 28.35 ? 308  ARG A CG  1 
ATOM   2410 C CD  . ARG A 1 308 ? -1.159  -1.401  2.476  1.00 34.28 ? 308  ARG A CD  1 
ATOM   2411 N NE  . ARG A 1 308 ? -0.171  -0.369  2.810  1.00 37.66 ? 308  ARG A NE  1 
ATOM   2412 C CZ  . ARG A 1 308 ? 1.109   -0.416  2.436  1.00 39.76 ? 308  ARG A CZ  1 
ATOM   2413 N NH1 . ARG A 1 308 ? 1.545   -1.438  1.715  1.00 41.20 ? 308  ARG A NH1 1 
ATOM   2414 N NH2 . ARG A 1 308 ? 1.953   0.556   2.766  1.00 40.22 ? 308  ARG A NH2 1 
ATOM   2415 N N   . GLU A 1 309 ? -4.631  -5.660  3.032  1.00 23.57 ? 309  GLU A N   1 
ATOM   2416 C CA  . GLU A 1 309 ? -5.821  -6.226  2.427  1.00 25.37 ? 309  GLU A CA  1 
ATOM   2417 C C   . GLU A 1 309 ? -6.921  -6.580  3.450  1.00 23.88 ? 309  GLU A C   1 
ATOM   2418 O O   . GLU A 1 309 ? -8.116  -6.386  3.189  1.00 23.73 ? 309  GLU A O   1 
ATOM   2419 C CB  . GLU A 1 309 ? -5.472  -7.458  1.575  1.00 25.44 ? 309  GLU A CB  1 
ATOM   2420 C CG  . GLU A 1 309 ? -6.706  -7.992  0.827  1.00 28.24 ? 309  GLU A CG  1 
ATOM   2421 C CD  . GLU A 1 309 ? -6.497  -9.328  0.137  1.00 30.06 ? 309  GLU A CD  1 
ATOM   2422 O OE1 . GLU A 1 309 ? -5.329  -9.689  -0.169 1.00 34.92 ? 309  GLU A OE1 1 
ATOM   2423 O OE2 . GLU A 1 309 ? -7.529  -10.019 -0.111 1.00 36.38 ? 309  GLU A OE2 1 
ATOM   2424 N N   . VAL A 1 310 ? -6.517  -7.134  4.589  1.00 22.61 ? 310  VAL A N   1 
ATOM   2425 C CA  . VAL A 1 310 ? -7.453  -7.415  5.676  1.00 21.77 ? 310  VAL A CA  1 
ATOM   2426 C C   . VAL A 1 310 ? -8.016  -6.115  6.284  1.00 21.45 ? 310  VAL A C   1 
ATOM   2427 O O   . VAL A 1 310 ? -9.230  -6.000  6.469  1.00 21.85 ? 310  VAL A O   1 
ATOM   2428 C CB  . VAL A 1 310 ? -6.815  -8.353  6.760  1.00 22.30 ? 310  VAL A CB  1 
ATOM   2429 C CG1 . VAL A 1 310 ? -7.818  -8.625  7.934  1.00 22.12 ? 310  VAL A CG1 1 
ATOM   2430 C CG2 . VAL A 1 310 ? -6.359  -9.674  6.105  1.00 21.13 ? 310  VAL A CG2 1 
ATOM   2431 N N   . VAL A 1 311 ? -7.140  -5.146  6.561  1.00 21.09 ? 311  VAL A N   1 
ATOM   2432 C CA  . VAL A 1 311 ? -7.512  -3.839  7.102  1.00 22.23 ? 311  VAL A CA  1 
ATOM   2433 C C   . VAL A 1 311 ? -8.589  -3.200  6.215  1.00 22.96 ? 311  VAL A C   1 
ATOM   2434 O O   . VAL A 1 311 ? -9.634  -2.785  6.702  1.00 23.06 ? 311  VAL A O   1 
ATOM   2435 C CB  . VAL A 1 311 ? -6.280  -2.873  7.248  1.00 22.31 ? 311  VAL A CB  1 
ATOM   2436 C CG1 . VAL A 1 311 ? -6.727  -1.437  7.631  1.00 22.43 ? 311  VAL A CG1 1 
ATOM   2437 C CG2 . VAL A 1 311 ? -5.278  -3.394  8.266  1.00 20.93 ? 311  VAL A CG2 1 
ATOM   2438 N N   . GLU A 1 312 ? -8.348  -3.192  4.905  1.00 23.03 ? 312  GLU A N   1 
ATOM   2439 C CA  . GLU A 1 312 ? -9.193  -2.459  3.986  1.00 23.74 ? 312  GLU A CA  1 
ATOM   2440 C C   . GLU A 1 312 ? -10.545 -3.129  3.718  1.00 22.75 ? 312  GLU A C   1 
ATOM   2441 O O   . GLU A 1 312 ? -11.525 -2.428  3.577  1.00 22.94 ? 312  GLU A O   1 
ATOM   2442 C CB  . GLU A 1 312 ? -8.430  -2.090  2.708  1.00 24.98 ? 312  GLU A CB  1 
ATOM   2443 C CG  . GLU A 1 312 ? -7.393  -0.957  2.936  1.00 29.80 ? 312  GLU A CG  1 
ATOM   2444 C CD  . GLU A 1 312 ? -7.964  0.322   3.606  1.00 36.79 ? 312  GLU A CD  1 
ATOM   2445 O OE1 . GLU A 1 312 ? -8.987  0.859   3.100  1.00 39.66 ? 312  GLU A OE1 1 
ATOM   2446 O OE2 . GLU A 1 312 ? -7.367  0.805   4.619  1.00 37.30 ? 312  GLU A OE2 1 
ATOM   2447 N N   . ARG A 1 313 ? -10.614 -4.460  3.697  1.00 21.93 ? 313  ARG A N   1 
ATOM   2448 C CA  . ARG A 1 313 ? -11.927 -5.118  3.597  1.00 21.96 ? 313  ARG A CA  1 
ATOM   2449 C C   . ARG A 1 313 ? -12.790 -4.887  4.860  1.00 21.23 ? 313  ARG A C   1 
ATOM   2450 O O   . ARG A 1 313 ? -13.996 -4.752  4.758  1.00 21.28 ? 313  ARG A O   1 
ATOM   2451 C CB  . ARG A 1 313 ? -11.850 -6.613  3.184  1.00 21.77 ? 313  ARG A CB  1 
ATOM   2452 C CG  . ARG A 1 313 ? -11.214 -7.587  4.194  1.00 21.93 ? 313  ARG A CG  1 
ATOM   2453 C CD  . ARG A 1 313 ? -11.535 -9.029  3.841  1.00 22.38 ? 313  ARG A CD  1 
ATOM   2454 N NE  . ARG A 1 313 ? -10.820 -9.968  4.701  1.00 26.16 ? 313  ARG A NE  1 
ATOM   2455 C CZ  . ARG A 1 313 ? -9.986  -10.914 4.274  1.00 25.90 ? 313  ARG A CZ  1 
ATOM   2456 N NH1 . ARG A 1 313 ? -9.745  -11.077 2.979  1.00 28.63 ? 313  ARG A NH1 1 
ATOM   2457 N NH2 . ARG A 1 313 ? -9.395  -11.708 5.146  1.00 25.75 ? 313  ARG A NH2 1 
ATOM   2458 N N   . ASN A 1 314 ? -12.171 -4.807  6.031  1.00 20.38 ? 314  ASN A N   1 
ATOM   2459 C CA  . ASN A 1 314 ? -12.936 -4.526  7.252  1.00 20.89 ? 314  ASN A CA  1 
ATOM   2460 C C   . ASN A 1 314 ? -13.383 -3.075  7.362  1.00 20.69 ? 314  ASN A C   1 
ATOM   2461 O O   . ASN A 1 314 ? -14.521 -2.800  7.730  1.00 20.45 ? 314  ASN A O   1 
ATOM   2462 C CB  . ASN A 1 314 ? -12.214 -5.042  8.502  1.00 20.41 ? 314  ASN A CB  1 
ATOM   2463 C CG  . ASN A 1 314 ? -12.270 -6.545  8.597  1.00 21.29 ? 314  ASN A CG  1 
ATOM   2464 O OD1 . ASN A 1 314 ? -13.265 -7.105  9.047  1.00 24.92 ? 314  ASN A OD1 1 
ATOM   2465 N ND2 . ASN A 1 314 ? -11.224 -7.217  8.130  1.00 21.74 ? 314  ASN A ND2 1 
ATOM   2466 N N   . ARG A 1 315 ? -12.487 -2.166  6.999  1.00 20.77 ? 315  ARG A N   1 
ATOM   2467 C CA  . ARG A 1 315 ? -12.807 -0.759  6.812  1.00 21.67 ? 315  ARG A CA  1 
ATOM   2468 C C   . ARG A 1 315 ? -13.852 -0.524  5.729  1.00 22.15 ? 315  ARG A C   1 
ATOM   2469 O O   . ARG A 1 315 ? -14.741 0.319   5.907  1.00 22.02 ? 315  ARG A O   1 
ATOM   2470 C CB  . ARG A 1 315 ? -11.548 0.031   6.487  1.00 21.93 ? 315  ARG A CB  1 
ATOM   2471 C CG  . ARG A 1 315 ? -10.791 0.422   7.703  1.00 21.00 ? 315  ARG A CG  1 
ATOM   2472 C CD  . ARG A 1 315 ? -9.667  1.350   7.337  1.00 21.92 ? 315  ARG A CD  1 
ATOM   2473 N NE  . ARG A 1 315 ? -10.087 2.736   7.342  1.00 22.45 ? 315  ARG A NE  1 
ATOM   2474 C CZ  . ARG A 1 315 ? -10.382 3.457   6.262  1.00 27.94 ? 315  ARG A CZ  1 
ATOM   2475 N NH1 . ARG A 1 315 ? -10.332 2.932   5.031  1.00 26.63 ? 315  ARG A NH1 1 
ATOM   2476 N NH2 . ARG A 1 315 ? -10.733 4.724   6.418  1.00 29.52 ? 315  ARG A NH2 1 
ATOM   2477 N N   . ALA A 1 316 ? -13.761 -1.274  4.624  1.00 22.76 ? 316  ALA A N   1 
ATOM   2478 C CA  . ALA A 1 316 ? -14.748 -1.176  3.557  1.00 23.30 ? 316  ALA A CA  1 
ATOM   2479 C C   . ALA A 1 316 ? -16.127 -1.644  4.038  1.00 23.73 ? 316  ALA A C   1 
ATOM   2480 O O   . ALA A 1 316 ? -17.152 -1.168  3.550  1.00 24.35 ? 316  ALA A O   1 
ATOM   2481 C CB  . ALA A 1 316 ? -14.311 -1.982  2.311  1.00 23.48 ? 316  ALA A CB  1 
ATOM   2482 N N   . ALA A 1 317 ? -16.145 -2.557  5.012  1.00 23.49 ? 317  ALA A N   1 
ATOM   2483 C CA  . ALA A 1 317 ? -17.393 -3.074  5.569  1.00 23.93 ? 317  ALA A CA  1 
ATOM   2484 C C   . ALA A 1 317 ? -18.050 -2.178  6.639  1.00 23.78 ? 317  ALA A C   1 
ATOM   2485 O O   . ALA A 1 317 ? -19.119 -2.522  7.155  1.00 24.48 ? 317  ALA A O   1 
ATOM   2486 C CB  . ALA A 1 317 ? -17.170 -4.468  6.118  1.00 23.80 ? 317  ALA A CB  1 
ATOM   2487 N N   . GLN A 1 318 ? -17.414 -1.049  6.945  1.00 23.14 ? 318  GLN A N   1 
ATOM   2488 C CA  . GLN A 1 318 ? -17.856 -0.089  7.961  1.00 24.19 ? 318  GLN A CA  1 
ATOM   2489 C C   . GLN A 1 318 ? -17.880 -0.731  9.354  1.00 24.10 ? 318  GLN A C   1 
ATOM   2490 O O   . GLN A 1 318 ? -18.815 -0.525  10.144 1.00 24.64 ? 318  GLN A O   1 
ATOM   2491 C CB  . GLN A 1 318 ? -19.208 0.580   7.591  1.00 24.98 ? 318  GLN A CB  1 
ATOM   2492 C CG  . GLN A 1 318 ? -19.214 1.342   6.228  1.00 26.73 ? 318  GLN A CG  1 
ATOM   2493 C CD  . GLN A 1 318 ? -18.060 2.353   6.101  1.00 28.56 ? 318  GLN A CD  1 
ATOM   2494 O OE1 . GLN A 1 318 ? -17.842 3.181   6.981  1.00 30.70 ? 318  GLN A OE1 1 
ATOM   2495 N NE2 . GLN A 1 318 ? -17.334 2.287   4.999  1.00 30.65 ? 318  GLN A NE2 1 
ATOM   2496 N N   . LEU A 1 319 ? -16.848 -1.534  9.625  1.00 23.24 ? 319  LEU A N   1 
ATOM   2497 C CA  . LEU A 1 319 ? -16.708 -2.231  10.902 1.00 22.31 ? 319  LEU A CA  1 
ATOM   2498 C C   . LEU A 1 319 ? -16.138 -1.267  11.910 1.00 21.57 ? 319  LEU A C   1 
ATOM   2499 O O   . LEU A 1 319 ? -15.154 -0.584  11.615 1.00 22.63 ? 319  LEU A O   1 
ATOM   2500 C CB  . LEU A 1 319 ? -15.794 -3.458  10.771 1.00 22.02 ? 319  LEU A CB  1 
ATOM   2501 C CG  . LEU A 1 319 ? -15.807 -4.450  11.950 1.00 22.29 ? 319  LEU A CG  1 
ATOM   2502 C CD1 . LEU A 1 319 ? -17.079 -5.291  11.996 1.00 19.91 ? 319  LEU A CD1 1 
ATOM   2503 C CD2 . LEU A 1 319 ? -14.566 -5.357  11.954 1.00 20.80 ? 319  LEU A CD2 1 
ATOM   2504 N N   . PRO A 1 320 ? -16.773 -1.162  13.095 1.00 21.22 ? 320  PRO A N   1 
ATOM   2505 C CA  . PRO A 1 320 ? -16.138 -0.396  14.131 1.00 19.88 ? 320  PRO A CA  1 
ATOM   2506 C C   . PRO A 1 320 ? -14.860 -1.151  14.442 1.00 18.51 ? 320  PRO A C   1 
ATOM   2507 O O   . PRO A 1 320 ? -14.888 -2.360  14.644 1.00 17.60 ? 320  PRO A O   1 
ATOM   2508 C CB  . PRO A 1 320 ? -17.136 -0.495  15.283 1.00 19.89 ? 320  PRO A CB  1 
ATOM   2509 C CG  . PRO A 1 320 ? -18.429 -0.744  14.630 1.00 20.48 ? 320  PRO A CG  1 
ATOM   2510 C CD  . PRO A 1 320 ? -18.055 -1.718  13.571 1.00 20.69 ? 320  PRO A CD  1 
ATOM   2511 N N   . TYR A 1 321 ? -13.748 -0.435  14.461 1.00 17.76 ? 321  TYR A N   1 
ATOM   2512 C CA  . TYR A 1 321 ? -12.453 -1.079  14.322 1.00 17.79 ? 321  TYR A CA  1 
ATOM   2513 C C   . TYR A 1 321 ? -11.444 0.000   14.631 1.00 17.08 ? 321  TYR A C   1 
ATOM   2514 O O   . TYR A 1 321 ? -11.187 0.834   13.807 1.00 17.96 ? 321  TYR A O   1 
ATOM   2515 C CB  . TYR A 1 321 ? -12.379 -1.574  12.862 1.00 18.43 ? 321  TYR A CB  1 
ATOM   2516 C CG  . TYR A 1 321 ? -11.060 -2.089  12.299 1.00 18.79 ? 321  TYR A CG  1 
ATOM   2517 C CD1 . TYR A 1 321 ? -9.984  -2.464  13.127 1.00 18.89 ? 321  TYR A CD1 1 
ATOM   2518 C CD2 . TYR A 1 321 ? -10.930 -2.261  10.928 1.00 16.30 ? 321  TYR A CD2 1 
ATOM   2519 C CE1 . TYR A 1 321 ? -8.785  -2.954  12.573 1.00 17.88 ? 321  TYR A CE1 1 
ATOM   2520 C CE2 . TYR A 1 321 ? -9.769  -2.756  10.372 1.00 20.53 ? 321  TYR A CE2 1 
ATOM   2521 C CZ  . TYR A 1 321 ? -8.699  -3.099  11.193 1.00 19.96 ? 321  TYR A CZ  1 
ATOM   2522 O OH  . TYR A 1 321 ? -7.559  -3.576  10.614 1.00 19.12 ? 321  TYR A OH  1 
ATOM   2523 N N   . ASP A 1 322 ? -10.905 0.010   15.843 1.00 17.04 ? 322  ASP A N   1 
ATOM   2524 C CA  . ASP A 1 322 ? -9.986  1.046   16.269 1.00 17.90 ? 322  ASP A CA  1 
ATOM   2525 C C   . ASP A 1 322 ? -8.531  0.659   16.166 1.00 18.14 ? 322  ASP A C   1 
ATOM   2526 O O   . ASP A 1 322 ? -7.695  1.528   15.964 1.00 18.67 ? 322  ASP A O   1 
ATOM   2527 C CB  . ASP A 1 322 ? -10.247 1.450   17.719 1.00 17.72 ? 322  ASP A CB  1 
ATOM   2528 C CG  . ASP A 1 322 ? -11.204 2.577   17.824 1.00 20.59 ? 322  ASP A CG  1 
ATOM   2529 O OD1 . ASP A 1 322 ? -10.731 3.707   18.090 1.00 19.75 ? 322  ASP A OD1 1 
ATOM   2530 O OD2 . ASP A 1 322 ? -12.420 2.315   17.605 1.00 18.24 ? 322  ASP A OD2 1 
ATOM   2531 N N   . VAL A 1 323 ? -8.226  -0.622  16.369 1.00 18.29 ? 323  VAL A N   1 
ATOM   2532 C CA  . VAL A 1 323 ? -6.834  -1.035  16.588 1.00 18.43 ? 323  VAL A CA  1 
ATOM   2533 C C   . VAL A 1 323 ? -6.448  -2.200  15.674 1.00 18.31 ? 323  VAL A C   1 
ATOM   2534 O O   . VAL A 1 323 ? -7.204  -3.142  15.505 1.00 18.35 ? 323  VAL A O   1 
ATOM   2535 C CB  . VAL A 1 323 ? -6.568  -1.395  18.084 1.00 18.07 ? 323  VAL A CB  1 
ATOM   2536 C CG1 . VAL A 1 323 ? -5.056  -1.501  18.404 1.00 16.98 ? 323  VAL A CG1 1 
ATOM   2537 C CG2 . VAL A 1 323 ? -7.235  -0.381  19.030 1.00 15.74 ? 323  VAL A CG2 1 
ATOM   2538 N N   . GLN A 1 324 ? -5.267  -2.104  15.067 1.00 18.69 ? 324  GLN A N   1 
ATOM   2539 C CA  . GLN A 1 324 ? -4.683  -3.194  14.282 1.00 18.48 ? 324  GLN A CA  1 
ATOM   2540 C C   . GLN A 1 324 ? -3.449  -3.681  15.037 1.00 18.70 ? 324  GLN A C   1 
ATOM   2541 O O   . GLN A 1 324 ? -2.589  -2.869  15.395 1.00 17.54 ? 324  GLN A O   1 
ATOM   2542 C CB  . GLN A 1 324 ? -4.238  -2.700  12.886 1.00 19.00 ? 324  GLN A CB  1 
ATOM   2543 C CG  . GLN A 1 324 ? -3.650  -3.800  11.996 1.00 17.55 ? 324  GLN A CG  1 
ATOM   2544 C CD  . GLN A 1 324 ? -4.567  -5.029  11.859 1.00 19.74 ? 324  GLN A CD  1 
ATOM   2545 O OE1 . GLN A 1 324 ? -5.808  -4.915  11.678 1.00 16.05 ? 324  GLN A OE1 1 
ATOM   2546 N NE2 . GLN A 1 324 ? -3.961  -6.216  11.944 1.00 19.31 ? 324  GLN A NE2 1 
ATOM   2547 N N   . HIS A 1 325 ? -3.357  -4.994  15.270 1.00 18.83 ? 325  HIS A N   1 
ATOM   2548 C CA  . HIS A 1 325 ? -2.184  -5.549  15.952 1.00 18.57 ? 325  HIS A CA  1 
ATOM   2549 C C   . HIS A 1 325 ? -1.244  -6.134  14.908 1.00 18.95 ? 325  HIS A C   1 
ATOM   2550 O O   . HIS A 1 325 ? -1.686  -6.715  13.914 1.00 20.19 ? 325  HIS A O   1 
ATOM   2551 C CB  . HIS A 1 325 ? -2.579  -6.604  17.017 1.00 18.78 ? 325  HIS A CB  1 
ATOM   2552 C CG  . HIS A 1 325 ? -3.364  -6.037  18.170 1.00 18.13 ? 325  HIS A CG  1 
ATOM   2553 N ND1 . HIS A 1 325 ? -3.219  -6.484  19.460 1.00 15.98 ? 325  HIS A ND1 1 
ATOM   2554 C CD2 . HIS A 1 325 ? -4.293  -5.050  18.222 1.00 16.91 ? 325  HIS A CD2 1 
ATOM   2555 C CE1 . HIS A 1 325 ? -3.991  -5.777  20.267 1.00 15.99 ? 325  HIS A CE1 1 
ATOM   2556 N NE2 . HIS A 1 325 ? -4.675  -4.918  19.535 1.00 18.16 ? 325  HIS A NE2 1 
ATOM   2557 N N   . ALA A 1 326 ? 0.048   -5.940  15.115 1.00 18.46 ? 326  ALA A N   1 
ATOM   2558 C CA  . ALA A 1 326 ? 1.067   -6.505  14.211 1.00 18.70 ? 326  ALA A CA  1 
ATOM   2559 C C   . ALA A 1 326 ? 1.810   -7.562  15.033 1.00 18.06 ? 326  ALA A C   1 
ATOM   2560 O O   . ALA A 1 326 ? 2.455   -7.218  16.012 1.00 17.73 ? 326  ALA A O   1 
ATOM   2561 C CB  . ALA A 1 326 ? 2.044   -5.381  13.717 1.00 17.62 ? 326  ALA A CB  1 
ATOM   2562 N N   . ASP A 1 327 ? 1.664   -8.830  14.648 1.00 18.43 ? 327  ASP A N   1 
ATOM   2563 C CA  . ASP A 1 327 ? 2.277   -9.959  15.334 1.00 19.60 ? 327  ASP A CA  1 
ATOM   2564 C C   . ASP A 1 327 ? 3.761   -10.118 14.888 1.00 20.31 ? 327  ASP A C   1 
ATOM   2565 O O   . ASP A 1 327 ? 4.280   -9.264  14.186 1.00 20.64 ? 327  ASP A O   1 
ATOM   2566 C CB  . ASP A 1 327 ? 1.455   -11.222 15.070 1.00 19.13 ? 327  ASP A CB  1 
ATOM   2567 C CG  . ASP A 1 327 ? 1.584   -12.256 16.165 1.00 18.47 ? 327  ASP A CG  1 
ATOM   2568 O OD1 . ASP A 1 327 ? 2.668   -12.401 16.771 1.00 19.35 ? 327  ASP A OD1 1 
ATOM   2569 O OD2 . ASP A 1 327 ? 0.614   -12.991 16.379 1.00 17.92 ? 327  ASP A OD2 1 
ATOM   2570 N N   . ILE A 1 328 ? 4.431   -11.199 15.267 1.00 21.21 ? 328  ILE A N   1 
ATOM   2571 C CA  . ILE A 1 328 ? 5.885   -11.318 14.970 1.00 22.04 ? 328  ILE A CA  1 
ATOM   2572 C C   . ILE A 1 328 ? 6.260   -11.352 13.474 1.00 22.58 ? 328  ILE A C   1 
ATOM   2573 O O   . ILE A 1 328 ? 7.428   -11.142 13.152 1.00 22.76 ? 328  ILE A O   1 
ATOM   2574 C CB  . ILE A 1 328 ? 6.595   -12.496 15.727 1.00 21.97 ? 328  ILE A CB  1 
ATOM   2575 C CG1 . ILE A 1 328 ? 5.885   -13.830 15.458 1.00 21.77 ? 328  ILE A CG1 1 
ATOM   2576 C CG2 . ILE A 1 328 ? 6.700   -12.189 17.198 1.00 21.06 ? 328  ILE A CG2 1 
ATOM   2577 C CD1 . ILE A 1 328 ? 6.512   -15.049 16.162 1.00 22.57 ? 328  ILE A CD1 1 
ATOM   2578 N N   . ASP A 1 329 ? 5.304   -11.597 12.563 1.00 22.00 ? 329  ASP A N   1 
ATOM   2579 C CA  . ASP A 1 329 ? 5.631   -11.483 11.131 1.00 22.49 ? 329  ASP A CA  1 
ATOM   2580 C C   . ASP A 1 329 ? 6.113   -10.116 10.641 1.00 22.03 ? 329  ASP A C   1 
ATOM   2581 O O   . ASP A 1 329 ? 6.727   -10.084 9.593  1.00 22.79 ? 329  ASP A O   1 
ATOM   2582 C CB  . ASP A 1 329 ? 4.558   -12.069 10.188 1.00 23.11 ? 329  ASP A CB  1 
ATOM   2583 C CG  . ASP A 1 329 ? 3.138   -11.683 10.582 1.00 24.92 ? 329  ASP A CG  1 
ATOM   2584 O OD1 . ASP A 1 329 ? 2.773   -11.773 11.791 1.00 25.58 ? 329  ASP A OD1 1 
ATOM   2585 O OD2 . ASP A 1 329 ? 2.372   -11.345 9.664  1.00 28.97 ? 329  ASP A OD2 1 
ATOM   2586 N N   . TYR A 1 330 ? 5.872   -9.013  11.383 1.00 21.95 ? 330  TYR A N   1 
ATOM   2587 C CA  . TYR A 1 330 ? 6.396   -7.663  11.010 1.00 21.13 ? 330  TYR A CA  1 
ATOM   2588 C C   . TYR A 1 330 ? 7.920   -7.549  11.146 1.00 21.30 ? 330  TYR A C   1 
ATOM   2589 O O   . TYR A 1 330 ? 8.557   -6.747  10.464 1.00 20.47 ? 330  TYR A O   1 
ATOM   2590 C CB  . TYR A 1 330 ? 5.691   -6.488  11.743 1.00 20.43 ? 330  TYR A CB  1 
ATOM   2591 C CG  . TYR A 1 330 ? 6.177   -6.172  13.163 1.00 20.19 ? 330  TYR A CG  1 
ATOM   2592 C CD1 . TYR A 1 330 ? 7.368   -5.468  13.382 1.00 18.68 ? 330  TYR A CD1 1 
ATOM   2593 C CD2 . TYR A 1 330 ? 5.446   -6.583  14.281 1.00 18.12 ? 330  TYR A CD2 1 
ATOM   2594 C CE1 . TYR A 1 330 ? 7.834   -5.205  14.674 1.00 19.61 ? 330  TYR A CE1 1 
ATOM   2595 C CE2 . TYR A 1 330 ? 5.901   -6.329  15.588 1.00 17.78 ? 330  TYR A CE2 1 
ATOM   2596 C CZ  . TYR A 1 330 ? 7.083   -5.625  15.772 1.00 18.66 ? 330  TYR A CZ  1 
ATOM   2597 O OH  . TYR A 1 330 ? 7.536   -5.360  17.034 1.00 18.88 ? 330  TYR A OH  1 
ATOM   2598 N N   . MET A 1 331 ? 8.484   -8.359  12.026 1.00 21.12 ? 331  MET A N   1 
ATOM   2599 C CA  . MET A 1 331 ? 9.876   -8.264  12.384 1.00 21.79 ? 331  MET A CA  1 
ATOM   2600 C C   . MET A 1 331 ? 10.785  -8.850  11.302 1.00 21.90 ? 331  MET A C   1 
ATOM   2601 O O   . MET A 1 331 ? 10.360  -9.627  10.460 1.00 22.12 ? 331  MET A O   1 
ATOM   2602 C CB  . MET A 1 331 ? 10.121  -8.990  13.711 1.00 21.42 ? 331  MET A CB  1 
ATOM   2603 C CG  . MET A 1 331 ? 9.226   -8.564  14.885 1.00 22.34 ? 331  MET A CG  1 
ATOM   2604 S SD  . MET A 1 331 ? 9.535   -9.607  16.305 1.00 22.91 ? 331  MET A SD  1 
ATOM   2605 C CE  . MET A 1 331 ? 8.519   -8.785  17.575 1.00 21.66 ? 331  MET A CE  1 
ATOM   2606 N N   . ASP A 1 332 ? 12.055  -8.484  11.357 1.00 23.65 ? 332  ASP A N   1 
ATOM   2607 C CA  . ASP A 1 332 ? 13.053  -9.079  10.482 1.00 24.52 ? 332  ASP A CA  1 
ATOM   2608 C C   . ASP A 1 332 ? 13.503  -10.357 11.175 1.00 24.60 ? 332  ASP A C   1 
ATOM   2609 O O   . ASP A 1 332 ? 14.250  -10.309 12.147 1.00 24.71 ? 332  ASP A O   1 
ATOM   2610 C CB  . ASP A 1 332 ? 14.227  -8.116  10.315 1.00 25.41 ? 332  ASP A CB  1 
ATOM   2611 C CG  . ASP A 1 332 ? 15.298  -8.636  9.360  1.00 28.17 ? 332  ASP A CG  1 
ATOM   2612 O OD1 . ASP A 1 332 ? 15.094  -9.689  8.704  1.00 28.74 ? 332  ASP A OD1 1 
ATOM   2613 O OD2 . ASP A 1 332 ? 16.343  -7.947  9.266  1.00 33.97 ? 332  ASP A OD2 1 
ATOM   2614 N N   . GLU A 1 333 ? 13.020  -11.496 10.693 1.00 25.39 ? 333  GLU A N   1 
ATOM   2615 C CA  . GLU A 1 333 ? 13.408  -12.806 11.261 1.00 26.18 ? 333  GLU A CA  1 
ATOM   2616 C C   . GLU A 1 333 ? 13.061  -12.923 12.756 1.00 24.82 ? 333  GLU A C   1 
ATOM   2617 O O   . GLU A 1 333 ? 13.833  -13.465 13.566 1.00 23.46 ? 333  GLU A O   1 
ATOM   2618 C CB  . GLU A 1 333 ? 14.901  -13.108 11.014 1.00 27.24 ? 333  GLU A CB  1 
ATOM   2619 C CG  . GLU A 1 333 ? 15.331  -13.047 9.544  1.00 31.99 ? 333  GLU A CG  1 
ATOM   2620 C CD  . GLU A 1 333 ? 14.905  -14.258 8.745  1.00 39.66 ? 333  GLU A CD  1 
ATOM   2621 O OE1 . GLU A 1 333 ? 13.784  -14.794 8.980  1.00 41.23 ? 333  GLU A OE1 1 
ATOM   2622 O OE2 . GLU A 1 333 ? 15.693  -14.669 7.854  1.00 41.45 ? 333  GLU A OE2 1 
ATOM   2623 N N   . ARG A 1 334 ? 11.889  -12.389 13.100 1.00 23.53 ? 334  ARG A N   1 
ATOM   2624 C CA  . ARG A 1 334 ? 11.311  -12.547 14.424 1.00 23.21 ? 334  ARG A CA  1 
ATOM   2625 C C   . ARG A 1 334 ? 12.138  -11.933 15.533 1.00 22.61 ? 334  ARG A C   1 
ATOM   2626 O O   . ARG A 1 334 ? 12.125  -12.397 16.671 1.00 22.35 ? 334  ARG A O   1 
ATOM   2627 C CB  . ARG A 1 334 ? 10.991  -14.031 14.661 1.00 23.35 ? 334  ARG A CB  1 
ATOM   2628 C CG  . ARG A 1 334 ? 9.843   -14.481 13.731 1.00 24.02 ? 334  ARG A CG  1 
ATOM   2629 C CD  . ARG A 1 334 ? 9.686   -15.979 13.571 1.00 26.39 ? 334  ARG A CD  1 
ATOM   2630 N NE  . ARG A 1 334 ? 8.327   -16.278 13.102 1.00 29.03 ? 334  ARG A NE  1 
ATOM   2631 C CZ  . ARG A 1 334 ? 7.705   -17.447 13.281 1.00 30.02 ? 334  ARG A CZ  1 
ATOM   2632 N NH1 . ARG A 1 334 ? 8.318   -18.456 13.909 1.00 28.35 ? 334  ARG A NH1 1 
ATOM   2633 N NH2 . ARG A 1 334 ? 6.474   -17.611 12.828 1.00 27.69 ? 334  ARG A NH2 1 
ATOM   2634 N N   . ARG A 1 335 ? 12.848  -10.862 15.197 1.00 22.81 ? 335  ARG A N   1 
ATOM   2635 C CA  . ARG A 1 335 ? 13.723  -10.170 16.150 1.00 22.64 ? 335  ARG A CA  1 
ATOM   2636 C C   . ARG A 1 335 ? 13.126  -8.821  16.525 1.00 22.07 ? 335  ARG A C   1 
ATOM   2637 O O   . ARG A 1 335 ? 12.693  -8.076  15.636 1.00 21.74 ? 335  ARG A O   1 
ATOM   2638 C CB  . ARG A 1 335 ? 15.118  -9.951  15.546 1.00 22.18 ? 335  ARG A CB  1 
ATOM   2639 C CG  . ARG A 1 335 ? 15.980  -11.197 15.426 1.00 23.68 ? 335  ARG A CG  1 
ATOM   2640 C CD  . ARG A 1 335 ? 17.394  -10.833 14.984 1.00 24.83 ? 335  ARG A CD  1 
ATOM   2641 N NE  . ARG A 1 335 ? 17.324  -10.154 13.702 1.00 32.88 ? 335  ARG A NE  1 
ATOM   2642 C CZ  . ARG A 1 335 ? 18.349  -9.578  13.096 1.00 37.54 ? 335  ARG A CZ  1 
ATOM   2643 N NH1 . ARG A 1 335 ? 18.138  -8.984  11.920 1.00 37.86 ? 335  ARG A NH1 1 
ATOM   2644 N NH2 . ARG A 1 335 ? 19.569  -9.597  13.658 1.00 34.21 ? 335  ARG A NH2 1 
ATOM   2645 N N   . ASP A 1 336 ? 13.088  -8.515  17.828 1.00 21.48 ? 336  ASP A N   1 
ATOM   2646 C CA  . ASP A 1 336 ? 12.576  -7.229  18.329 1.00 21.49 ? 336  ASP A CA  1 
ATOM   2647 C C   . ASP A 1 336 ? 13.259  -6.057  17.654 1.00 21.80 ? 336  ASP A C   1 
ATOM   2648 O O   . ASP A 1 336 ? 14.477  -6.134  17.312 1.00 21.96 ? 336  ASP A O   1 
ATOM   2649 C CB  . ASP A 1 336 ? 12.828  -7.073  19.829 1.00 21.07 ? 336  ASP A CB  1 
ATOM   2650 C CG  . ASP A 1 336 ? 11.858  -7.852  20.690 1.00 23.72 ? 336  ASP A CG  1 
ATOM   2651 O OD1 . ASP A 1 336 ? 10.802  -8.320  20.174 1.00 19.81 ? 336  ASP A OD1 1 
ATOM   2652 O OD2 . ASP A 1 336 ? 12.168  -7.969  21.914 1.00 23.60 ? 336  ASP A OD2 1 
ATOM   2653 N N   . PHE A 1 337 ? 12.488  -4.976  17.499 1.00 21.04 ? 337  PHE A N   1 
ATOM   2654 C CA  . PHE A 1 337 ? 12.988  -3.630  17.142 1.00 21.60 ? 337  PHE A CA  1 
ATOM   2655 C C   . PHE A 1 337 ? 13.578  -3.518  15.726 1.00 21.44 ? 337  PHE A C   1 
ATOM   2656 O O   . PHE A 1 337 ? 14.428  -2.660  15.453 1.00 22.11 ? 337  PHE A O   1 
ATOM   2657 C CB  . PHE A 1 337 ? 13.945  -3.055  18.200 1.00 20.52 ? 337  PHE A CB  1 
ATOM   2658 C CG  . PHE A 1 337 ? 13.448  -3.198  19.606 1.00 21.56 ? 337  PHE A CG  1 
ATOM   2659 C CD1 . PHE A 1 337 ? 12.228  -2.611  20.002 1.00 18.86 ? 337  PHE A CD1 1 
ATOM   2660 C CD2 . PHE A 1 337 ? 14.178  -3.938  20.536 1.00 18.30 ? 337  PHE A CD2 1 
ATOM   2661 C CE1 . PHE A 1 337 ? 11.765  -2.762  21.320 1.00 19.12 ? 337  PHE A CE1 1 
ATOM   2662 C CE2 . PHE A 1 337 ? 13.708  -4.106  21.839 1.00 19.89 ? 337  PHE A CE2 1 
ATOM   2663 C CZ  . PHE A 1 337 ? 12.487  -3.508  22.218 1.00 19.52 ? 337  PHE A CZ  1 
ATOM   2664 N N   . THR A 1 338 ? 13.084  -4.394  14.859 1.00 21.74 ? 338  THR A N   1 
ATOM   2665 C CA  . THR A 1 338 ? 13.294  -4.377  13.432 1.00 22.27 ? 338  THR A CA  1 
ATOM   2666 C C   . THR A 1 338 ? 11.947  -4.588  12.754 1.00 22.87 ? 338  THR A C   1 
ATOM   2667 O O   . THR A 1 338 ? 10.999  -5.060  13.385 1.00 22.84 ? 338  THR A O   1 
ATOM   2668 C CB  . THR A 1 338 ? 14.152  -5.562  12.995 1.00 22.23 ? 338  THR A CB  1 
ATOM   2669 O OG1 . THR A 1 338 ? 13.439  -6.777  13.250 1.00 22.51 ? 338  THR A OG1 1 
ATOM   2670 C CG2 . THR A 1 338 ? 15.523  -5.582  13.734 1.00 22.57 ? 338  THR A CG2 1 
ATOM   2671 N N   . TYR A 1 339 ? 11.871  -4.273  11.465 1.00 23.99 ? 339  TYR A N   1 
ATOM   2672 C CA  . TYR A 1 339 ? 10.801  -4.823  10.631 1.00 24.57 ? 339  TYR A CA  1 
ATOM   2673 C C   . TYR A 1 339 ? 11.358  -5.436  9.327  1.00 25.00 ? 339  TYR A C   1 
ATOM   2674 O O   . TYR A 1 339 ? 12.465  -5.101  8.905  1.00 24.65 ? 339  TYR A O   1 
ATOM   2675 C CB  . TYR A 1 339 ? 9.688   -3.793  10.399 1.00 24.70 ? 339  TYR A CB  1 
ATOM   2676 C CG  . TYR A 1 339 ? 10.053  -2.587  9.561  1.00 24.73 ? 339  TYR A CG  1 
ATOM   2677 C CD1 . TYR A 1 339 ? 9.940   -2.632  8.176  1.00 26.11 ? 339  TYR A CD1 1 
ATOM   2678 C CD2 . TYR A 1 339 ? 10.466  -1.394  10.144 1.00 24.54 ? 339  TYR A CD2 1 
ATOM   2679 C CE1 . TYR A 1 339 ? 10.264  -1.546  7.392  1.00 26.18 ? 339  TYR A CE1 1 
ATOM   2680 C CE2 . TYR A 1 339 ? 10.800  -0.283  9.351  1.00 23.89 ? 339  TYR A CE2 1 
ATOM   2681 C CZ  . TYR A 1 339 ? 10.674  -0.379  7.976  1.00 24.81 ? 339  TYR A CZ  1 
ATOM   2682 O OH  . TYR A 1 339 ? 10.968  0.682   7.139  1.00 27.87 ? 339  TYR A OH  1 
ATOM   2683 N N   . ASP A 1 340 ? 10.596  -6.332  8.699  1.00 25.39 ? 340  ASP A N   1 
ATOM   2684 C CA  . ASP A 1 340 ? 11.045  -7.014  7.486  1.00 26.04 ? 340  ASP A CA  1 
ATOM   2685 C C   . ASP A 1 340 ? 11.012  -6.037  6.299  1.00 26.46 ? 340  ASP A C   1 
ATOM   2686 O O   . ASP A 1 340 ? 9.946   -5.653  5.816  1.00 25.85 ? 340  ASP A O   1 
ATOM   2687 C CB  . ASP A 1 340 ? 10.194  -8.262  7.247  1.00 26.34 ? 340  ASP A CB  1 
ATOM   2688 C CG  . ASP A 1 340 ? 10.734  -9.156  6.130  1.00 27.62 ? 340  ASP A CG  1 
ATOM   2689 O OD1 . ASP A 1 340 ? 11.245  -8.654  5.112  1.00 31.56 ? 340  ASP A OD1 1 
ATOM   2690 O OD2 . ASP A 1 340 ? 10.618  -10.382 6.248  1.00 31.67 ? 340  ASP A OD2 1 
ATOM   2691 N N   . SER A 1 341 ? 12.200  -5.632  5.851  1.00 27.24 ? 341  SER A N   1 
ATOM   2692 C CA  . SER A 1 341 ? 12.375  -4.592  4.833  1.00 28.13 ? 341  SER A CA  1 
ATOM   2693 C C   . SER A 1 341 ? 11.882  -4.995  3.447  1.00 28.23 ? 341  SER A C   1 
ATOM   2694 O O   . SER A 1 341 ? 11.783  -4.153  2.575  1.00 29.58 ? 341  SER A O   1 
ATOM   2695 C CB  . SER A 1 341 ? 13.855  -4.173  4.764  1.00 29.08 ? 341  SER A CB  1 
ATOM   2696 O OG  . SER A 1 341 ? 14.650  -5.288  4.365  1.00 32.17 ? 341  SER A OG  1 
ATOM   2697 N N   . VAL A 1 342 ? 11.561  -6.275  3.256  1.00 28.27 ? 342  VAL A N   1 
ATOM   2698 C CA  . VAL A 1 342 ? 10.974  -6.805  2.022  1.00 27.91 ? 342  VAL A CA  1 
ATOM   2699 C C   . VAL A 1 342 ? 9.468   -7.136  2.187  1.00 28.11 ? 342  VAL A C   1 
ATOM   2700 O O   . VAL A 1 342 ? 8.618   -6.565  1.516  1.00 27.80 ? 342  VAL A O   1 
ATOM   2701 C CB  . VAL A 1 342 ? 11.759  -8.060  1.535  1.00 27.97 ? 342  VAL A CB  1 
ATOM   2702 C CG1 . VAL A 1 342 ? 11.082  -8.699  0.332  1.00 28.57 ? 342  VAL A CG1 1 
ATOM   2703 C CG2 . VAL A 1 342 ? 13.233  -7.686  1.212  1.00 27.88 ? 342  VAL A CG2 1 
ATOM   2704 N N   . ASP A 1 343 ? 9.145   -8.058  3.081  1.00 27.70 ? 343  ASP A N   1 
ATOM   2705 C CA  . ASP A 1 343 ? 7.751   -8.433  3.315  1.00 27.81 ? 343  ASP A CA  1 
ATOM   2706 C C   . ASP A 1 343 ? 6.902   -7.307  3.928  1.00 26.88 ? 343  ASP A C   1 
ATOM   2707 O O   . ASP A 1 343 ? 5.682   -7.236  3.700  1.00 28.04 ? 343  ASP A O   1 
ATOM   2708 C CB  . ASP A 1 343 ? 7.701   -9.708  4.164  1.00 28.01 ? 343  ASP A CB  1 
ATOM   2709 C CG  . ASP A 1 343 ? 8.087   -10.963 3.364  1.00 30.26 ? 343  ASP A CG  1 
ATOM   2710 O OD1 . ASP A 1 343 ? 8.235   -10.871 2.125  1.00 32.06 ? 343  ASP A OD1 1 
ATOM   2711 O OD2 . ASP A 1 343 ? 8.212   -12.052 3.976  1.00 31.26 ? 343  ASP A OD2 1 
ATOM   2712 N N   . PHE A 1 344 ? 7.550   -6.427  4.681  1.00 25.53 ? 344  PHE A N   1 
ATOM   2713 C CA  . PHE A 1 344 ? 6.897   -5.295  5.333  1.00 25.16 ? 344  PHE A CA  1 
ATOM   2714 C C   . PHE A 1 344 ? 7.514   -3.967  4.917  1.00 25.25 ? 344  PHE A C   1 
ATOM   2715 O O   . PHE A 1 344 ? 7.538   -3.019  5.694  1.00 24.84 ? 344  PHE A O   1 
ATOM   2716 C CB  . PHE A 1 344 ? 6.872   -5.456  6.865  1.00 24.44 ? 344  PHE A CB  1 
ATOM   2717 C CG  . PHE A 1 344 ? 5.755   -6.358  7.352  1.00 23.18 ? 344  PHE A CG  1 
ATOM   2718 C CD1 . PHE A 1 344 ? 5.858   -7.747  7.240  1.00 22.15 ? 344  PHE A CD1 1 
ATOM   2719 C CD2 . PHE A 1 344 ? 4.587   -5.817  7.906  1.00 23.61 ? 344  PHE A CD2 1 
ATOM   2720 C CE1 . PHE A 1 344 ? 4.806   -8.587  7.680  1.00 22.09 ? 344  PHE A CE1 1 
ATOM   2721 C CE2 . PHE A 1 344 ? 3.533   -6.659  8.345  1.00 21.05 ? 344  PHE A CE2 1 
ATOM   2722 C CZ  . PHE A 1 344 ? 3.649   -8.028  8.222  1.00 21.25 ? 344  PHE A CZ  1 
ATOM   2723 N N   . LYS A 1 345 ? 7.959   -3.895  3.658  1.00 25.86 ? 345  LYS A N   1 
ATOM   2724 C CA  . LYS A 1 345 ? 8.492   -2.649  3.095  1.00 26.72 ? 345  LYS A CA  1 
ATOM   2725 C C   . LYS A 1 345 ? 7.346   -1.656  3.003  1.00 26.63 ? 345  LYS A C   1 
ATOM   2726 O O   . LYS A 1 345 ? 6.256   -1.982  2.501  1.00 25.95 ? 345  LYS A O   1 
ATOM   2727 C CB  . LYS A 1 345 ? 9.106   -2.892  1.708  1.00 27.16 ? 345  LYS A CB  1 
ATOM   2728 C CG  . LYS A 1 345 ? 9.586   -1.612  1.003  1.00 28.31 ? 345  LYS A CG  1 
ATOM   2729 C CD  . LYS A 1 345 ? 9.804   -1.844  -0.507 1.00 28.10 ? 345  LYS A CD  1 
ATOM   2730 C CE  . LYS A 1 345 ? 10.323  -0.577  -1.193 1.00 30.05 ? 345  LYS A CE  1 
ATOM   2731 N NZ  . LYS A 1 345 ? 10.301  -0.702  -2.693 1.00 31.24 ? 345  LYS A NZ  1 
ATOM   2732 N N   . GLY A 1 346 ? 7.575   -0.449  3.499  1.00 26.68 ? 346  GLY A N   1 
ATOM   2733 C CA  . GLY A 1 346 ? 6.491   0.528   3.531  1.00 27.08 ? 346  GLY A CA  1 
ATOM   2734 C C   . GLY A 1 346 ? 5.675   0.470   4.800  1.00 26.90 ? 346  GLY A C   1 
ATOM   2735 O O   . GLY A 1 346 ? 4.602   1.065   4.871  1.00 28.21 ? 346  GLY A O   1 
ATOM   2736 N N   . PHE A 1 347 ? 6.165   -0.257  5.805  1.00 26.64 ? 347  PHE A N   1 
ATOM   2737 C CA  . PHE A 1 347 ? 5.533   -0.267  7.146  1.00 25.86 ? 347  PHE A CA  1 
ATOM   2738 C C   . PHE A 1 347 ? 5.249   1.148   7.696  1.00 25.49 ? 347  PHE A C   1 
ATOM   2739 O O   . PHE A 1 347 ? 4.114   1.398   8.156  1.00 25.89 ? 347  PHE A O   1 
ATOM   2740 C CB  . PHE A 1 347 ? 6.317   -1.146  8.165  1.00 25.54 ? 347  PHE A CB  1 
ATOM   2741 C CG  . PHE A 1 347 ? 5.466   -1.721  9.298  1.00 25.42 ? 347  PHE A CG  1 
ATOM   2742 C CD1 . PHE A 1 347 ? 4.082   -1.910  9.154  1.00 25.08 ? 347  PHE A CD1 1 
ATOM   2743 C CD2 . PHE A 1 347 ? 6.067   -2.131  10.480 1.00 23.96 ? 347  PHE A CD2 1 
ATOM   2744 C CE1 . PHE A 1 347 ? 3.309   -2.452  10.201 1.00 25.85 ? 347  PHE A CE1 1 
ATOM   2745 C CE2 . PHE A 1 347 ? 5.309   -2.677  11.531 1.00 25.74 ? 347  PHE A CE2 1 
ATOM   2746 C CZ  . PHE A 1 347 ? 3.928   -2.835  11.386 1.00 25.57 ? 347  PHE A CZ  1 
ATOM   2747 N N   . PRO A 1 348 ? 6.247   2.082   7.645  1.00 24.22 ? 348  PRO A N   1 
ATOM   2748 C CA  . PRO A 1 348 ? 5.936   3.418   8.154  1.00 23.24 ? 348  PRO A CA  1 
ATOM   2749 C C   . PRO A 1 348 ? 4.784   4.125   7.414  1.00 23.07 ? 348  PRO A C   1 
ATOM   2750 O O   . PRO A 1 348 ? 4.028   4.844   8.076  1.00 22.57 ? 348  PRO A O   1 
ATOM   2751 C CB  . PRO A 1 348 ? 7.242   4.182   7.959  1.00 23.73 ? 348  PRO A CB  1 
ATOM   2752 C CG  . PRO A 1 348 ? 8.307   3.109   7.913  1.00 23.40 ? 348  PRO A CG  1 
ATOM   2753 C CD  . PRO A 1 348 ? 7.642   2.015   7.162  1.00 24.13 ? 348  PRO A CD  1 
ATOM   2754 N N   . GLU A 1 349 ? 4.667   3.930   6.092  1.00 22.01 ? 349  GLU A N   1 
ATOM   2755 C CA  . GLU A 1 349 ? 3.602   4.539   5.277  1.00 23.42 ? 349  GLU A CA  1 
ATOM   2756 C C   . GLU A 1 349 ? 2.221   3.960   5.684  1.00 22.69 ? 349  GLU A C   1 
ATOM   2757 O O   . GLU A 1 349 ? 1.231   4.679   5.724  1.00 22.81 ? 349  GLU A O   1 
ATOM   2758 C CB  . GLU A 1 349 ? 3.827   4.310   3.766  1.00 23.64 ? 349  GLU A CB  1 
ATOM   2759 C CG  . GLU A 1 349 ? 4.995   5.090   3.076  1.00 27.41 ? 349  GLU A CG  1 
ATOM   2760 C CD  . GLU A 1 349 ? 6.295   4.279   2.977  1.00 31.96 ? 349  GLU A CD  1 
ATOM   2761 O OE1 . GLU A 1 349 ? 6.817   3.860   4.042  1.00 31.12 ? 349  GLU A OE1 1 
ATOM   2762 O OE2 . GLU A 1 349 ? 6.786   4.057   1.830  1.00 32.51 ? 349  GLU A OE2 1 
ATOM   2763 N N   . PHE A 1 350 ? 2.181   2.654   5.936  1.00 22.68 ? 350  PHE A N   1 
ATOM   2764 C CA  . PHE A 1 350 ? 0.985   1.946   6.440  1.00 23.32 ? 350  PHE A CA  1 
ATOM   2765 C C   . PHE A 1 350 ? 0.579   2.474   7.825  1.00 23.20 ? 350  PHE A C   1 
ATOM   2766 O O   . PHE A 1 350 ? -0.606  2.634   8.117  1.00 23.51 ? 350  PHE A O   1 
ATOM   2767 C CB  . PHE A 1 350 ? 1.222   0.426   6.453  1.00 23.31 ? 350  PHE A CB  1 
ATOM   2768 C CG  . PHE A 1 350 ? 0.212   -0.357  7.264  1.00 23.76 ? 350  PHE A CG  1 
ATOM   2769 C CD1 . PHE A 1 350 ? -1.012  -0.735  6.705  1.00 25.35 ? 350  PHE A CD1 1 
ATOM   2770 C CD2 . PHE A 1 350 ? 0.493   -0.726  8.584  1.00 22.05 ? 350  PHE A CD2 1 
ATOM   2771 C CE1 . PHE A 1 350 ? -1.951  -1.477  7.453  1.00 25.18 ? 350  PHE A CE1 1 
ATOM   2772 C CE2 . PHE A 1 350 ? -0.429  -1.462  9.330  1.00 24.60 ? 350  PHE A CE2 1 
ATOM   2773 C CZ  . PHE A 1 350 ? -1.648  -1.841  8.764  1.00 23.75 ? 350  PHE A CZ  1 
ATOM   2774 N N   . VAL A 1 351 ? 1.561   2.769   8.666  1.00 22.62 ? 351  VAL A N   1 
ATOM   2775 C CA  . VAL A 1 351 ? 1.296   3.403   9.958  1.00 22.79 ? 351  VAL A CA  1 
ATOM   2776 C C   . VAL A 1 351 ? 0.581   4.767   9.807  1.00 22.55 ? 351  VAL A C   1 
ATOM   2777 O O   . VAL A 1 351 ? -0.417  5.013   10.503 1.00 23.02 ? 351  VAL A O   1 
ATOM   2778 C CB  . VAL A 1 351 ? 2.565   3.464   10.821 1.00 22.38 ? 351  VAL A CB  1 
ATOM   2779 C CG1 . VAL A 1 351 ? 2.405   4.403   11.993 1.00 23.44 ? 351  VAL A CG1 1 
ATOM   2780 C CG2 . VAL A 1 351 ? 2.879   2.080   11.328 1.00 23.72 ? 351  VAL A CG2 1 
ATOM   2781 N N   . ASN A 1 352 ? 1.054   5.606   8.872  1.00 21.38 ? 352  ASN A N   1 
ATOM   2782 C CA  . ASN A 1 352 ? 0.382   6.866   8.523  1.00 20.81 ? 352  ASN A CA  1 
ATOM   2783 C C   . ASN A 1 352 ? -1.037  6.651   7.998  1.00 20.22 ? 352  ASN A C   1 
ATOM   2784 O O   . ASN A 1 352 ? -1.897  7.482   8.246  1.00 19.64 ? 352  ASN A O   1 
ATOM   2785 C CB  . ASN A 1 352 ? 1.136   7.655   7.450  1.00 20.01 ? 352  ASN A CB  1 
ATOM   2786 C CG  . ASN A 1 352 ? 2.428   8.302   7.951  1.00 22.82 ? 352  ASN A CG  1 
ATOM   2787 O OD1 . ASN A 1 352 ? 2.785   8.257   9.136  1.00 22.97 ? 352  ASN A OD1 1 
ATOM   2788 N ND2 . ASN A 1 352 ? 3.133   8.935   7.022  1.00 24.68 ? 352  ASN A ND2 1 
ATOM   2789 N N   . GLU A 1 353 ? -1.246  5.594   7.212  1.00 19.69 ? 353  GLU A N   1 
ATOM   2790 C CA  . GLU A 1 353 ? -2.578  5.228   6.700  1.00 20.75 ? 353  GLU A CA  1 
ATOM   2791 C C   . GLU A 1 353 ? -3.554  4.897   7.833  1.00 20.95 ? 353  GLU A C   1 
ATOM   2792 O O   . GLU A 1 353 ? -4.700  5.382   7.835  1.00 21.13 ? 353  GLU A O   1 
ATOM   2793 C CB  . GLU A 1 353 ? -2.505  4.053   5.693  1.00 18.95 ? 353  GLU A CB  1 
ATOM   2794 C CG  . GLU A 1 353 ? -1.727  4.391   4.444  1.00 22.26 ? 353  GLU A CG  1 
ATOM   2795 C CD  . GLU A 1 353 ? -1.416  3.200   3.550  1.00 22.47 ? 353  GLU A CD  1 
ATOM   2796 O OE1 . GLU A 1 353 ? -1.428  2.046   4.029  1.00 25.73 ? 353  GLU A OE1 1 
ATOM   2797 O OE2 . GLU A 1 353 ? -1.156  3.445   2.353  1.00 25.91 ? 353  GLU A OE2 1 
ATOM   2798 N N   . LEU A 1 354 ? -3.117  4.029   8.755  1.00 20.59 ? 354  LEU A N   1 
ATOM   2799 C CA  . LEU A 1 354 ? -3.882  3.727   9.973  1.00 20.33 ? 354  LEU A CA  1 
ATOM   2800 C C   . LEU A 1 354 ? -4.257  5.009   10.718 1.00 20.61 ? 354  LEU A C   1 
ATOM   2801 O O   . LEU A 1 354 ? -5.442  5.240   11.012 1.00 20.35 ? 354  LEU A O   1 
ATOM   2802 C CB  . LEU A 1 354 ? -3.108  2.774   10.913 1.00 20.72 ? 354  LEU A CB  1 
ATOM   2803 C CG  . LEU A 1 354 ? -2.956  1.300   10.534 1.00 20.06 ? 354  LEU A CG  1 
ATOM   2804 C CD1 . LEU A 1 354 ? -2.094  0.660   11.578 1.00 20.27 ? 354  LEU A CD1 1 
ATOM   2805 C CD2 . LEU A 1 354 ? -4.314  0.547   10.441 1.00 20.62 ? 354  LEU A CD2 1 
ATOM   2806 N N   . HIS A 1 355 ? -3.257  5.851   10.984 1.00 19.93 ? 355  HIS A N   1 
ATOM   2807 C CA  . HIS A 1 355 ? -3.452  7.074   11.727 1.00 20.60 ? 355  HIS A CA  1 
ATOM   2808 C C   . HIS A 1 355 ? -4.422  8.056   11.074 1.00 21.14 ? 355  HIS A C   1 
ATOM   2809 O O   . HIS A 1 355 ? -5.225  8.690   11.765 1.00 21.26 ? 355  HIS A O   1 
ATOM   2810 C CB  . HIS A 1 355 ? -2.096  7.716   12.021 1.00 20.96 ? 355  HIS A CB  1 
ATOM   2811 C CG  . HIS A 1 355 ? -1.287  6.948   13.021 1.00 22.21 ? 355  HIS A CG  1 
ATOM   2812 N ND1 . HIS A 1 355 ? 0.068   7.142   13.192 1.00 22.76 ? 355  HIS A ND1 1 
ATOM   2813 C CD2 . HIS A 1 355 ? -1.643  5.979   13.903 1.00 21.99 ? 355  HIS A CD2 1 
ATOM   2814 C CE1 . HIS A 1 355 ? 0.509   6.342   14.148 1.00 22.39 ? 355  HIS A CE1 1 
ATOM   2815 N NE2 . HIS A 1 355 ? -0.503  5.619   14.591 1.00 23.11 ? 355  HIS A NE2 1 
ATOM   2816 N N   . ASN A 1 356 ? -4.330  8.175   9.749  1.00 21.17 ? 356  ASN A N   1 
ATOM   2817 C CA  . ASN A 1 356 ? -5.224  9.010   8.966  1.00 22.05 ? 356  ASN A CA  1 
ATOM   2818 C C   . ASN A 1 356 ? -6.661  8.458   8.938  1.00 22.11 ? 356  ASN A C   1 
ATOM   2819 O O   . ASN A 1 356 ? -7.585  9.227   8.723  1.00 21.98 ? 356  ASN A O   1 
ATOM   2820 C CB  . ASN A 1 356 ? -4.706  9.156   7.532  1.00 22.34 ? 356  ASN A CB  1 
ATOM   2821 C CG  . ASN A 1 356 ? -5.529  10.130  6.714  1.00 24.27 ? 356  ASN A CG  1 
ATOM   2822 O OD1 . ASN A 1 356 ? -5.803  11.252  7.156  1.00 28.90 ? 356  ASN A OD1 1 
ATOM   2823 N ND2 . ASN A 1 356 ? -5.941  9.709   5.523  1.00 26.30 ? 356  ASN A ND2 1 
ATOM   2824 N N   . ASN A 1 357 ? -6.813  7.137   9.109  1.00 22.12 ? 357  ASN A N   1 
ATOM   2825 C CA  . ASN A 1 357 ? -8.117  6.443   9.189  1.00 22.16 ? 357  ASN A CA  1 
ATOM   2826 C C   . ASN A 1 357 ? -8.753  6.563   10.578 1.00 22.16 ? 357  ASN A C   1 
ATOM   2827 O O   . ASN A 1 357 ? -9.876  6.053   10.808 1.00 23.13 ? 357  ASN A O   1 
ATOM   2828 C CB  . ASN A 1 357 ? -7.994  4.925   8.899  1.00 22.21 ? 357  ASN A CB  1 
ATOM   2829 C CG  . ASN A 1 357 ? -7.570  4.577   7.468  1.00 22.69 ? 357  ASN A CG  1 
ATOM   2830 O OD1 . ASN A 1 357 ? -7.277  3.412   7.197  1.00 29.26 ? 357  ASN A OD1 1 
ATOM   2831 N ND2 . ASN A 1 357 ? -7.557  5.538   6.566  1.00 23.54 ? 357  ASN A ND2 1 
ATOM   2832 N N   . GLY A 1 358 ? -8.043  7.208   11.498 1.00 21.64 ? 358  GLY A N   1 
ATOM   2833 C CA  . GLY A 1 358 ? -8.426  7.276   12.911 1.00 21.24 ? 358  GLY A CA  1 
ATOM   2834 C C   . GLY A 1 358 ? -8.088  6.054   13.759 1.00 20.96 ? 358  GLY A C   1 
ATOM   2835 O O   . GLY A 1 358 ? -8.635  5.886   14.847 1.00 21.24 ? 358  GLY A O   1 
ATOM   2836 N N   . GLN A 1 359 ? -7.155  5.226   13.284 1.00 19.88 ? 359  GLN A N   1 
ATOM   2837 C CA  . GLN A 1 359 ? -6.843  3.947   13.891 1.00 18.76 ? 359  GLN A CA  1 
ATOM   2838 C C   . GLN A 1 359 ? -5.478  3.906   14.556 1.00 19.05 ? 359  GLN A C   1 
ATOM   2839 O O   . GLN A 1 359 ? -4.662  4.830   14.400 1.00 19.48 ? 359  GLN A O   1 
ATOM   2840 C CB  . GLN A 1 359 ? -6.940  2.845   12.849 1.00 18.42 ? 359  GLN A CB  1 
ATOM   2841 C CG  . GLN A 1 359 ? -8.337  2.565   12.356 1.00 20.03 ? 359  GLN A CG  1 
ATOM   2842 C CD  . GLN A 1 359 ? -8.331  1.585   11.210 1.00 22.09 ? 359  GLN A CD  1 
ATOM   2843 O OE1 . GLN A 1 359 ? -7.644  1.800   10.224 1.00 22.59 ? 359  GLN A OE1 1 
ATOM   2844 N NE2 . GLN A 1 359 ? -9.094  0.499   11.333 1.00 22.26 ? 359  GLN A NE2 1 
ATOM   2845 N N   . LYS A 1 360 ? -5.255  2.847   15.340 1.00 18.86 ? 360  LYS A N   1 
ATOM   2846 C CA  . LYS A 1 360 ? -4.040  2.709   16.137 1.00 18.72 ? 360  LYS A CA  1 
ATOM   2847 C C   . LYS A 1 360 ? -3.290  1.433   15.788 1.00 17.72 ? 360  LYS A C   1 
ATOM   2848 O O   . LYS A 1 360 ? -3.880  0.495   15.317 1.00 17.22 ? 360  LYS A O   1 
ATOM   2849 C CB  . LYS A 1 360 ? -4.401  2.760   17.619 1.00 19.36 ? 360  LYS A CB  1 
ATOM   2850 C CG  . LYS A 1 360 ? -5.243  4.018   18.004 1.00 20.48 ? 360  LYS A CG  1 
ATOM   2851 C CD  . LYS A 1 360 ? -4.380  5.274   18.186 1.00 21.13 ? 360  LYS A CD  1 
ATOM   2852 C CE  . LYS A 1 360 ? -5.228  6.511   18.393 1.00 23.01 ? 360  LYS A CE  1 
ATOM   2853 N NZ  . LYS A 1 360 ? -4.444  7.682   18.964 1.00 28.63 ? 360  LYS A NZ  1 
ATOM   2854 N N   . LEU A 1 361 ? -1.975  1.421   15.966 1.00 18.32 ? 361  LEU A N   1 
ATOM   2855 C CA  . LEU A 1 361 ? -1.185  0.216   15.709 1.00 18.37 ? 361  LEU A CA  1 
ATOM   2856 C C   . LEU A 1 361 ? -0.668  -0.270  17.047 1.00 17.99 ? 361  LEU A C   1 
ATOM   2857 O O   . LEU A 1 361 ? -0.090  0.480   17.793 1.00 18.67 ? 361  LEU A O   1 
ATOM   2858 C CB  . LEU A 1 361 ? 0.004   0.499   14.764 1.00 18.89 ? 361  LEU A CB  1 
ATOM   2859 C CG  . LEU A 1 361 ? 1.043   -0.617  14.571 1.00 18.84 ? 361  LEU A CG  1 
ATOM   2860 C CD1 . LEU A 1 361 ? 0.426   -1.805  13.851 1.00 19.00 ? 361  LEU A CD1 1 
ATOM   2861 C CD2 . LEU A 1 361 ? 2.327   -0.135  13.852 1.00 20.87 ? 361  LEU A CD2 1 
ATOM   2862 N N   . VAL A 1 362 ? -0.888  -1.540  17.350 1.00 18.23 ? 362  VAL A N   1 
ATOM   2863 C CA  . VAL A 1 362 ? -0.261  -2.155  18.497 1.00 17.11 ? 362  VAL A CA  1 
ATOM   2864 C C   . VAL A 1 362 ? 0.752   -3.170  17.957 1.00 16.71 ? 362  VAL A C   1 
ATOM   2865 O O   . VAL A 1 362 ? 0.413   -4.006  17.132 1.00 16.54 ? 362  VAL A O   1 
ATOM   2866 C CB  . VAL A 1 362 ? -1.327  -2.790  19.441 1.00 17.23 ? 362  VAL A CB  1 
ATOM   2867 C CG1 . VAL A 1 362 ? -0.656  -3.682  20.490 1.00 17.51 ? 362  VAL A CG1 1 
ATOM   2868 C CG2 . VAL A 1 362 ? -2.131  -1.668  20.123 1.00 15.33 ? 362  VAL A CG2 1 
ATOM   2869 N N   . ILE A 1 363 ? 2.008   -3.068  18.390 1.00 16.59 ? 363  ILE A N   1 
ATOM   2870 C CA  . ILE A 1 363 ? 3.014   -4.052  17.970 1.00 15.94 ? 363  ILE A CA  1 
ATOM   2871 C C   . ILE A 1 363 ? 3.306   -5.011  19.098 1.00 14.94 ? 363  ILE A C   1 
ATOM   2872 O O   . ILE A 1 363 ? 3.322   -4.619  20.265 1.00 13.25 ? 363  ILE A O   1 
ATOM   2873 C CB  . ILE A 1 363 ? 4.381   -3.393  17.519 1.00 16.53 ? 363  ILE A CB  1 
ATOM   2874 C CG1 . ILE A 1 363 ? 4.904   -2.387  18.560 1.00 16.00 ? 363  ILE A CG1 1 
ATOM   2875 C CG2 . ILE A 1 363 ? 4.220   -2.729  16.147 1.00 18.17 ? 363  ILE A CG2 1 
ATOM   2876 C CD1 . ILE A 1 363 ? 6.445   -2.061  18.443 1.00 16.44 ? 363  ILE A CD1 1 
ATOM   2877 N N   . ILE A 1 364 ? 3.541   -6.266  18.738 1.00 14.88 ? 364  ILE A N   1 
ATOM   2878 C CA  . ILE A 1 364 ? 3.998   -7.265  19.674 1.00 16.63 ? 364  ILE A CA  1 
ATOM   2879 C C   . ILE A 1 364 ? 5.511   -7.022  19.866 1.00 17.31 ? 364  ILE A C   1 
ATOM   2880 O O   . ILE A 1 364 ? 6.209   -6.621  18.926 1.00 15.47 ? 364  ILE A O   1 
ATOM   2881 C CB  . ILE A 1 364 ? 3.692   -8.712  19.166 1.00 16.27 ? 364  ILE A CB  1 
ATOM   2882 C CG1 . ILE A 1 364 ? 3.623   -9.704  20.324 1.00 18.51 ? 364  ILE A CG1 1 
ATOM   2883 C CG2 . ILE A 1 364 ? 4.705   -9.186  18.115 1.00 17.32 ? 364  ILE A CG2 1 
ATOM   2884 C CD1 . ILE A 1 364 ? 2.884   -11.032 19.992 1.00 17.84 ? 364  ILE A CD1 1 
ATOM   2885 N N   . VAL A 1 365 ? 5.962   -7.186  21.102 1.00 18.15 ? 365  VAL A N   1 
ATOM   2886 C CA  . VAL A 1 365 ? 7.377   -7.201  21.441 1.00 19.81 ? 365  VAL A CA  1 
ATOM   2887 C C   . VAL A 1 365 ? 7.562   -8.382  22.399 1.00 20.26 ? 365  VAL A C   1 
ATOM   2888 O O   . VAL A 1 365 ? 6.675   -8.688  23.220 1.00 19.03 ? 365  VAL A O   1 
ATOM   2889 C CB  . VAL A 1 365 ? 7.897   -5.860  22.087 1.00 20.22 ? 365  VAL A CB  1 
ATOM   2890 C CG1 . VAL A 1 365 ? 9.445   -5.858  22.217 1.00 22.00 ? 365  VAL A CG1 1 
ATOM   2891 C CG2 . VAL A 1 365 ? 7.517   -4.662  21.259 1.00 20.75 ? 365  VAL A CG2 1 
ATOM   2892 N N   . ASP A 1 366 ? 8.714   -9.045  22.265 1.00 20.13 ? 366  ASP A N   1 
ATOM   2893 C CA  . ASP A 1 366 ? 9.046   -10.218 23.047 1.00 20.42 ? 366  ASP A CA  1 
ATOM   2894 C C   . ASP A 1 366 ? 10.162  -9.801  23.986 1.00 20.67 ? 366  ASP A C   1 
ATOM   2895 O O   . ASP A 1 366 ? 10.912  -8.905  23.679 1.00 21.24 ? 366  ASP A O   1 
ATOM   2896 C CB  . ASP A 1 366 ? 9.502   -11.389 22.137 1.00 20.58 ? 366  ASP A CB  1 
ATOM   2897 C CG  . ASP A 1 366 ? 8.408   -11.877 21.179 1.00 22.67 ? 366  ASP A CG  1 
ATOM   2898 O OD1 . ASP A 1 366 ? 7.250   -12.157 21.621 1.00 21.14 ? 366  ASP A OD1 1 
ATOM   2899 O OD2 . ASP A 1 366 ? 8.722   -12.025 19.973 1.00 23.33 ? 366  ASP A OD2 1 
ATOM   2900 N N   . PRO A 1 367 ? 10.246  -10.416 25.169 1.00 21.12 ? 367  PRO A N   1 
ATOM   2901 C CA  . PRO A 1 367 ? 11.363  -10.123 26.060 1.00 21.77 ? 367  PRO A CA  1 
ATOM   2902 C C   . PRO A 1 367 ? 12.712  -10.603 25.521 1.00 22.64 ? 367  PRO A C   1 
ATOM   2903 O O   . PRO A 1 367 ? 13.710  -9.903  25.678 1.00 22.91 ? 367  PRO A O   1 
ATOM   2904 C CB  . PRO A 1 367 ? 11.024  -10.898 27.333 1.00 21.45 ? 367  PRO A CB  1 
ATOM   2905 C CG  . PRO A 1 367 ? 9.947   -11.821 26.994 1.00 21.62 ? 367  PRO A CG  1 
ATOM   2906 C CD  . PRO A 1 367 ? 9.300   -11.388 25.729 1.00 20.26 ? 367  PRO A CD  1 
ATOM   2907 N N   . ALA A 1 368 ? 12.735  -11.785 24.910 1.00 22.70 ? 368  ALA A N   1 
ATOM   2908 C CA  . ALA A 1 368 ? 14.000  -12.445 24.614 1.00 23.29 ? 368  ALA A CA  1 
ATOM   2909 C C   . ALA A 1 368 ? 14.623  -11.813 23.395 1.00 22.78 ? 368  ALA A C   1 
ATOM   2910 O O   . ALA A 1 368 ? 13.966  -11.610 22.369 1.00 23.35 ? 368  ALA A O   1 
ATOM   2911 C CB  . ALA A 1 368 ? 13.817  -13.943 24.409 1.00 22.61 ? 368  ALA A CB  1 
ATOM   2912 N N   . ILE A 1 369 ? 15.902  -11.517 23.536 1.00 22.29 ? 369  ILE A N   1 
ATOM   2913 C CA  . ILE A 1 369 ? 16.666  -10.757 22.563 1.00 22.47 ? 369  ILE A CA  1 
ATOM   2914 C C   . ILE A 1 369 ? 17.701  -11.692 21.923 1.00 23.07 ? 369  ILE A C   1 
ATOM   2915 O O   . ILE A 1 369 ? 18.455  -12.351 22.625 1.00 23.02 ? 369  ILE A O   1 
ATOM   2916 C CB  . ILE A 1 369 ? 17.404  -9.566  23.256 1.00 21.52 ? 369  ILE A CB  1 
ATOM   2917 C CG1 . ILE A 1 369 ? 16.401  -8.651  24.000 1.00 21.80 ? 369  ILE A CG1 1 
ATOM   2918 C CG2 . ILE A 1 369 ? 18.207  -8.753  22.231 1.00 21.68 ? 369  ILE A CG2 1 
ATOM   2919 C CD1 . ILE A 1 369 ? 15.352  -7.961  23.105 1.00 21.12 ? 369  ILE A CD1 1 
ATOM   2920 N N   . SER A 1 370 ? 17.707  -11.748 20.595 1.00 24.18 ? 370  SER A N   1 
ATOM   2921 C CA  . SER A 1 370 ? 18.704  -12.499 19.827 1.00 25.28 ? 370  SER A CA  1 
ATOM   2922 C C   . SER A 1 370 ? 20.115  -12.148 20.255 1.00 25.22 ? 370  SER A C   1 
ATOM   2923 O O   . SER A 1 370 ? 20.462  -10.977 20.282 1.00 24.88 ? 370  SER A O   1 
ATOM   2924 C CB  . SER A 1 370 ? 18.574  -12.162 18.346 1.00 24.45 ? 370  SER A CB  1 
ATOM   2925 O OG  . SER A 1 370 ? 19.477  -12.953 17.582 1.00 26.96 ? 370  SER A OG  1 
ATOM   2926 N N   . ASN A 1 371 ? 20.921  -13.147 20.601 1.00 26.46 ? 371  ASN A N   1 
ATOM   2927 C CA  . ASN A 1 371 ? 22.355  -12.893 20.809 1.00 27.39 ? 371  ASN A CA  1 
ATOM   2928 C C   . ASN A 1 371 ? 23.189  -13.011 19.528 1.00 28.65 ? 371  ASN A C   1 
ATOM   2929 O O   . ASN A 1 371 ? 24.419  -13.139 19.603 1.00 28.41 ? 371  ASN A O   1 
ATOM   2930 C CB  . ASN A 1 371 ? 22.943  -13.801 21.901 1.00 26.72 ? 371  ASN A CB  1 
ATOM   2931 C CG  . ASN A 1 371 ? 22.970  -15.268 21.507 1.00 27.19 ? 371  ASN A CG  1 
ATOM   2932 O OD1 . ASN A 1 371 ? 22.388  -15.685 20.489 1.00 24.41 ? 371  ASN A OD1 1 
ATOM   2933 N ND2 . ASN A 1 371 ? 23.615  -16.071 22.340 1.00 27.02 ? 371  ASN A ND2 1 
ATOM   2934 N N   . ASN A 1 372 ? 22.537  -13.004 18.367 1.00 29.52 ? 372  ASN A N   1 
ATOM   2935 C CA  . ASN A 1 372 ? 23.277  -13.098 17.097 1.00 31.00 ? 372  ASN A CA  1 
ATOM   2936 C C   . ASN A 1 372 ? 23.648  -11.706 16.585 1.00 31.73 ? 372  ASN A C   1 
ATOM   2937 O O   . ASN A 1 372 ? 22.866  -11.056 15.907 1.00 30.96 ? 372  ASN A O   1 
ATOM   2938 C CB  . ASN A 1 372 ? 22.528  -13.923 16.029 1.00 31.38 ? 372  ASN A CB  1 
ATOM   2939 C CG  . ASN A 1 372 ? 23.438  -14.331 14.837 1.00 33.11 ? 372  ASN A CG  1 
ATOM   2940 O OD1 . ASN A 1 372 ? 24.560  -13.833 14.704 1.00 35.68 ? 372  ASN A OD1 1 
ATOM   2941 N ND2 . ASN A 1 372 ? 22.953  -15.238 13.986 1.00 33.97 ? 372  ASN A ND2 1 
ATOM   2942 N N   . SER A 1 373 ? 24.852  -11.261 16.944 1.00 33.03 ? 373  SER A N   1 
ATOM   2943 C CA  . SER A 1 373 ? 25.378  -9.962  16.542 1.00 34.41 ? 373  SER A CA  1 
ATOM   2944 C C   . SER A 1 373 ? 26.876  -10.092 16.312 1.00 35.90 ? 373  SER A C   1 
ATOM   2945 O O   . SER A 1 373 ? 27.566  -10.756 17.087 1.00 35.95 ? 373  SER A O   1 
ATOM   2946 C CB  . SER A 1 373 ? 25.148  -8.931  17.641 1.00 34.37 ? 373  SER A CB  1 
ATOM   2947 O OG  . SER A 1 373 ? 25.564  -7.627  17.254 1.00 33.57 ? 373  SER A OG  1 
ATOM   2948 N N   . SER A 1 374 ? 27.366  -9.466  15.248 1.00 37.58 ? 374  SER A N   1 
ATOM   2949 C CA  . SER A 1 374 ? 28.805  -9.437  14.952 1.00 39.98 ? 374  SER A CA  1 
ATOM   2950 C C   . SER A 1 374 ? 29.209  -8.068  14.409 1.00 40.97 ? 374  SER A C   1 
ATOM   2951 O O   . SER A 1 374 ? 28.348  -7.212  14.184 1.00 41.67 ? 374  SER A O   1 
ATOM   2952 C CB  . SER A 1 374 ? 29.188  -10.560 13.971 1.00 39.94 ? 374  SER A CB  1 
ATOM   2953 O OG  . SER A 1 374 ? 28.334  -10.582 12.837 1.00 41.56 ? 374  SER A OG  1 
ATOM   2954 N N   . SER A 1 375 ? 30.507  -7.846  14.208 1.00 42.08 ? 375  SER A N   1 
ATOM   2955 C CA  . SER A 1 375 ? 30.972  -6.608  13.569 1.00 42.59 ? 375  SER A CA  1 
ATOM   2956 C C   . SER A 1 375 ? 30.330  -6.404  12.197 1.00 42.69 ? 375  SER A C   1 
ATOM   2957 O O   . SER A 1 375 ? 29.936  -5.287  11.846 1.00 43.63 ? 375  SER A O   1 
ATOM   2958 C CB  . SER A 1 375 ? 32.506  -6.596  13.437 1.00 43.21 ? 375  SER A CB  1 
ATOM   2959 O OG  . SER A 1 375 ? 33.136  -6.298  14.680 1.00 44.16 ? 375  SER A OG  1 
ATOM   2960 N N   . SER A 1 376 ? 30.211  -7.490  11.438 1.00 42.39 ? 376  SER A N   1 
ATOM   2961 C CA  . SER A 1 376 ? 29.712  -7.446  10.067 1.00 42.32 ? 376  SER A CA  1 
ATOM   2962 C C   . SER A 1 376 ? 28.186  -7.300  9.967  1.00 41.88 ? 376  SER A C   1 
ATOM   2963 O O   . SER A 1 376 ? 27.659  -6.975  8.894  1.00 41.84 ? 376  SER A O   1 
ATOM   2964 C CB  . SER A 1 376 ? 30.167  -8.702  9.317  1.00 42.33 ? 376  SER A CB  1 
ATOM   2965 O OG  . SER A 1 376 ? 29.274  -9.027  8.258  1.00 44.76 ? 376  SER A OG  1 
ATOM   2966 N N   . LYS A 1 377 ? 27.484  -7.570  11.074 1.00 40.77 ? 377  LYS A N   1 
ATOM   2967 C CA  . LYS A 1 377 ? 26.022  -7.567  11.094 1.00 39.60 ? 377  LYS A CA  1 
ATOM   2968 C C   . LYS A 1 377 ? 25.492  -7.285  12.526 1.00 37.73 ? 377  LYS A C   1 
ATOM   2969 O O   . LYS A 1 377 ? 24.938  -8.178  13.181 1.00 37.12 ? 377  LYS A O   1 
ATOM   2970 C CB  . LYS A 1 377 ? 25.513  -8.914  10.568 1.00 40.19 ? 377  LYS A CB  1 
ATOM   2971 C CG  . LYS A 1 377 ? 24.363  -8.821  9.580  1.00 42.36 ? 377  LYS A CG  1 
ATOM   2972 C CD  . LYS A 1 377 ? 24.826  -8.563  8.149  1.00 43.35 ? 377  LYS A CD  1 
ATOM   2973 C CE  . LYS A 1 377 ? 23.679  -8.000  7.293  1.00 45.42 ? 377  LYS A CE  1 
ATOM   2974 N NZ  . LYS A 1 377 ? 24.066  -7.766  5.870  1.00 45.07 ? 377  LYS A NZ  1 
ATOM   2975 N N   . PRO A 1 378 ? 25.697  -6.050  13.027 1.00 36.23 ? 378  PRO A N   1 
ATOM   2976 C CA  . PRO A 1 378 ? 25.336  -5.743  14.412 1.00 34.73 ? 378  PRO A CA  1 
ATOM   2977 C C   . PRO A 1 378 ? 23.834  -5.865  14.655 1.00 32.92 ? 378  PRO A C   1 
ATOM   2978 O O   . PRO A 1 378 ? 23.039  -5.550  13.771 1.00 32.74 ? 378  PRO A O   1 
ATOM   2979 C CB  . PRO A 1 378 ? 25.749  -4.273  14.566 1.00 35.14 ? 378  PRO A CB  1 
ATOM   2980 C CG  . PRO A 1 378 ? 25.822  -3.736  13.193 1.00 35.21 ? 378  PRO A CG  1 
ATOM   2981 C CD  . PRO A 1 378 ? 26.282  -4.876  12.350 1.00 36.04 ? 378  PRO A CD  1 
ATOM   2982 N N   . TYR A 1 379 ? 23.458  -6.334  15.841 1.00 30.97 ? 379  TYR A N   1 
ATOM   2983 C CA  . TYR A 1 379 ? 22.056  -6.270  16.254 1.00 28.57 ? 379  TYR A CA  1 
ATOM   2984 C C   . TYR A 1 379 ? 22.039  -5.376  17.455 1.00 27.41 ? 379  TYR A C   1 
ATOM   2985 O O   . TYR A 1 379 ? 22.408  -5.808  18.549 1.00 28.58 ? 379  TYR A O   1 
ATOM   2986 C CB  . TYR A 1 379 ? 21.493  -7.659  16.582 1.00 27.92 ? 379  TYR A CB  1 
ATOM   2987 C CG  . TYR A 1 379 ? 20.040  -7.655  17.052 1.00 26.19 ? 379  TYR A CG  1 
ATOM   2988 C CD1 . TYR A 1 379 ? 19.024  -7.070  16.275 1.00 24.89 ? 379  TYR A CD1 1 
ATOM   2989 C CD2 . TYR A 1 379 ? 19.678  -8.263  18.246 1.00 25.75 ? 379  TYR A CD2 1 
ATOM   2990 C CE1 . TYR A 1 379 ? 17.667  -7.081  16.708 1.00 25.20 ? 379  TYR A CE1 1 
ATOM   2991 C CE2 . TYR A 1 379 ? 18.323  -8.289  18.683 1.00 24.88 ? 379  TYR A CE2 1 
ATOM   2992 C CZ  . TYR A 1 379 ? 17.334  -7.697  17.907 1.00 24.74 ? 379  TYR A CZ  1 
ATOM   2993 O OH  . TYR A 1 379 ? 16.018  -7.710  18.351 1.00 26.65 ? 379  TYR A OH  1 
ATOM   2994 N N   . GLY A 1 380 ? 21.674  -4.117  17.224 1.00 25.86 ? 380  GLY A N   1 
ATOM   2995 C CA  . GLY A 1 380 ? 21.656  -3.063  18.247 1.00 24.85 ? 380  GLY A CA  1 
ATOM   2996 C C   . GLY A 1 380 ? 21.046  -3.383  19.604 1.00 23.68 ? 380  GLY A C   1 
ATOM   2997 O O   . GLY A 1 380 ? 21.705  -3.183  20.615 1.00 23.01 ? 380  GLY A O   1 
ATOM   2998 N N   . PRO A 1 381 ? 19.772  -3.881  19.646 1.00 23.92 ? 381  PRO A N   1 
ATOM   2999 C CA  . PRO A 1 381 ? 19.172  -4.188  20.961 1.00 23.12 ? 381  PRO A CA  1 
ATOM   3000 C C   . PRO A 1 381 ? 20.089  -5.067  21.850 1.00 23.07 ? 381  PRO A C   1 
ATOM   3001 O O   . PRO A 1 381 ? 20.174  -4.849  23.045 1.00 22.27 ? 381  PRO A O   1 
ATOM   3002 C CB  . PRO A 1 381 ? 17.882  -4.933  20.588 1.00 23.51 ? 381  PRO A CB  1 
ATOM   3003 C CG  . PRO A 1 381 ? 17.481  -4.340  19.271 1.00 23.66 ? 381  PRO A CG  1 
ATOM   3004 C CD  . PRO A 1 381 ? 18.834  -4.172  18.548 1.00 23.52 ? 381  PRO A CD  1 
ATOM   3005 N N   . TYR A 1 382 ? 20.754  -6.053  21.247 1.00 23.24 ? 382  TYR A N   1 
ATOM   3006 C CA  . TYR A 1 382 ? 21.633  -6.967  21.972 1.00 23.55 ? 382  TYR A CA  1 
ATOM   3007 C C   . TYR A 1 382 ? 22.933  -6.273  22.379 1.00 23.97 ? 382  TYR A C   1 
ATOM   3008 O O   . TYR A 1 382 ? 23.408  -6.454  23.507 1.00 25.29 ? 382  TYR A O   1 
ATOM   3009 C CB  . TYR A 1 382 ? 21.936  -8.224  21.139 1.00 23.46 ? 382  TYR A CB  1 
ATOM   3010 C CG  . TYR A 1 382 ? 22.971  -9.124  21.791 1.00 23.67 ? 382  TYR A CG  1 
ATOM   3011 C CD1 . TYR A 1 382 ? 22.652  -9.847  22.935 1.00 23.32 ? 382  TYR A CD1 1 
ATOM   3012 C CD2 . TYR A 1 382 ? 24.288  -9.207  21.295 1.00 22.39 ? 382  TYR A CD2 1 
ATOM   3013 C CE1 . TYR A 1 382 ? 23.580  -10.662 23.571 1.00 24.46 ? 382  TYR A CE1 1 
ATOM   3014 C CE2 . TYR A 1 382 ? 25.246  -10.028 21.941 1.00 23.17 ? 382  TYR A CE2 1 
ATOM   3015 C CZ  . TYR A 1 382 ? 24.870  -10.752 23.082 1.00 24.10 ? 382  TYR A CZ  1 
ATOM   3016 O OH  . TYR A 1 382 ? 25.760  -11.574 23.757 1.00 25.27 ? 382  TYR A OH  1 
ATOM   3017 N N   . ASP A 1 383 ? 23.509  -5.491  21.466 1.00 24.31 ? 383  ASP A N   1 
ATOM   3018 C CA  . ASP A 1 383 ? 24.769  -4.794  21.759 1.00 25.43 ? 383  ASP A CA  1 
ATOM   3019 C C   . ASP A 1 383 ? 24.549  -3.793  22.880 1.00 25.22 ? 383  ASP A C   1 
ATOM   3020 O O   . ASP A 1 383 ? 25.289  -3.757  23.843 1.00 25.33 ? 383  ASP A O   1 
ATOM   3021 C CB  . ASP A 1 383 ? 25.286  -4.062  20.515 1.00 25.56 ? 383  ASP A CB  1 
ATOM   3022 C CG  . ASP A 1 383 ? 25.670  -5.004  19.390 1.00 26.31 ? 383  ASP A CG  1 
ATOM   3023 O OD1 . ASP A 1 383 ? 25.804  -6.227  19.613 1.00 25.76 ? 383  ASP A OD1 1 
ATOM   3024 O OD2 . ASP A 1 383 ? 25.827  -4.503  18.261 1.00 29.88 ? 383  ASP A OD2 1 
ATOM   3025 N N   . ARG A 1 384 ? 23.495  -2.994  22.745 1.00 25.25 ? 384  ARG A N   1 
ATOM   3026 C CA  . ARG A 1 384 ? 23.163  -1.997  23.738 1.00 25.05 ? 384  ARG A CA  1 
ATOM   3027 C C   . ARG A 1 384 ? 22.869  -2.661  25.064 1.00 24.25 ? 384  ARG A C   1 
ATOM   3028 O O   . ARG A 1 384 ? 23.211  -2.104  26.094 1.00 23.70 ? 384  ARG A O   1 
ATOM   3029 C CB  . ARG A 1 384 ? 21.982  -1.108  23.277 1.00 25.10 ? 384  ARG A CB  1 
ATOM   3030 C CG  . ARG A 1 384 ? 22.347  -0.046  22.216 1.00 25.99 ? 384  ARG A CG  1 
ATOM   3031 C CD  . ARG A 1 384 ? 21.148  0.818   21.800 1.00 26.63 ? 384  ARG A CD  1 
ATOM   3032 N NE  . ARG A 1 384 ? 20.186  0.078   20.974 1.00 27.84 ? 384  ARG A NE  1 
ATOM   3033 C CZ  . ARG A 1 384 ? 20.175  0.043   19.645 1.00 27.44 ? 384  ARG A CZ  1 
ATOM   3034 N NH1 . ARG A 1 384 ? 21.064  0.717   18.941 1.00 30.40 ? 384  ARG A NH1 1 
ATOM   3035 N NH2 . ARG A 1 384 ? 19.256  -0.668  19.011 1.00 30.26 ? 384  ARG A NH2 1 
ATOM   3036 N N   . GLY A 1 385 ? 22.224  -3.840  25.050 1.00 23.79 ? 385  GLY A N   1 
ATOM   3037 C CA  . GLY A 1 385 ? 21.869  -4.543  26.305 1.00 23.57 ? 385  GLY A CA  1 
ATOM   3038 C C   . GLY A 1 385 ? 23.046  -5.176  27.032 1.00 24.49 ? 385  GLY A C   1 
ATOM   3039 O O   . GLY A 1 385 ? 23.118  -5.160  28.274 1.00 24.00 ? 385  GLY A O   1 
ATOM   3040 N N   . SER A 1 386 ? 23.962  -5.744  26.249 1.00 25.40 ? 386  SER A N   1 
ATOM   3041 C CA  . SER A 1 386 ? 25.227  -6.289  26.767 1.00 26.92 ? 386  SER A CA  1 
ATOM   3042 C C   . SER A 1 386 ? 26.084  -5.200  27.372 1.00 27.42 ? 386  SER A C   1 
ATOM   3043 O O   . SER A 1 386 ? 26.535  -5.354  28.478 1.00 28.08 ? 386  SER A O   1 
ATOM   3044 C CB  . SER A 1 386 ? 25.994  -7.016  25.660 1.00 26.25 ? 386  SER A CB  1 
ATOM   3045 O OG  . SER A 1 386 ? 25.162  -7.995  25.080 1.00 26.69 ? 386  SER A OG  1 
ATOM   3046 N N   . ASP A 1 387 ? 26.285  -4.098  26.646 1.00 29.73 ? 387  ASP A N   1 
ATOM   3047 C CA  . ASP A 1 387 ? 27.005  -2.920  27.160 1.00 31.09 ? 387  ASP A CA  1 
ATOM   3048 C C   . ASP A 1 387 ? 26.474  -2.520  28.553 1.00 31.77 ? 387  ASP A C   1 
ATOM   3049 O O   . ASP A 1 387 ? 27.249  -2.254  29.485 1.00 31.32 ? 387  ASP A O   1 
ATOM   3050 C CB  . ASP A 1 387 ? 26.863  -1.722  26.204 1.00 32.06 ? 387  ASP A CB  1 
ATOM   3051 C CG  . ASP A 1 387 ? 27.579  -1.910  24.847 1.00 34.47 ? 387  ASP A CG  1 
ATOM   3052 O OD1 . ASP A 1 387 ? 28.191  -2.974  24.561 1.00 36.95 ? 387  ASP A OD1 1 
ATOM   3053 O OD2 . ASP A 1 387 ? 27.513  -0.953  24.042 1.00 37.56 ? 387  ASP A OD2 1 
ATOM   3054 N N   . MET A 1 388 ? 25.143  -2.483  28.694 1.00 31.92 ? 388  MET A N   1 
ATOM   3055 C CA  . MET A 1 388 ? 24.521  -2.099  29.960 1.00 32.47 ? 388  MET A CA  1 
ATOM   3056 C C   . MET A 1 388 ? 24.478  -3.205  31.013 1.00 30.43 ? 388  MET A C   1 
ATOM   3057 O O   . MET A 1 388 ? 24.232  -2.941  32.186 1.00 30.59 ? 388  MET A O   1 
ATOM   3058 C CB  . MET A 1 388 ? 23.132  -1.493  29.723 1.00 32.39 ? 388  MET A CB  1 
ATOM   3059 C CG  . MET A 1 388 ? 23.196  -0.075  29.145 1.00 34.59 ? 388  MET A CG  1 
ATOM   3060 S SD  . MET A 1 388 ? 21.572  0.643   28.827 1.00 38.37 ? 388  MET A SD  1 
ATOM   3061 C CE  . MET A 1 388 ? 20.978  0.823   30.505 1.00 35.42 ? 388  MET A CE  1 
ATOM   3062 N N   . LYS A 1 389 ? 24.733  -4.441  30.594 1.00 28.84 ? 389  LYS A N   1 
ATOM   3063 C CA  . LYS A 1 389 ? 24.767  -5.606  31.511 1.00 27.51 ? 389  LYS A CA  1 
ATOM   3064 C C   . LYS A 1 389 ? 23.415  -5.915  32.207 1.00 25.76 ? 389  LYS A C   1 
ATOM   3065 O O   . LYS A 1 389 ? 23.345  -6.218  33.406 1.00 24.53 ? 389  LYS A O   1 
ATOM   3066 C CB  . LYS A 1 389 ? 25.932  -5.496  32.507 1.00 27.96 ? 389  LYS A CB  1 
ATOM   3067 C CG  . LYS A 1 389 ? 27.271  -5.160  31.825 1.00 29.31 ? 389  LYS A CG  1 
ATOM   3068 C CD  . LYS A 1 389 ? 28.370  -6.126  32.210 1.00 32.49 ? 389  LYS A CD  1 
ATOM   3069 C CE  . LYS A 1 389 ? 29.553  -6.042  31.238 1.00 35.43 ? 389  LYS A CE  1 
ATOM   3070 N NZ  . LYS A 1 389 ? 30.414  -7.275  31.266 1.00 35.12 ? 389  LYS A NZ  1 
ATOM   3071 N N   . ILE A 1 390 ? 22.354  -5.866  31.424 1.00 24.15 ? 390  ILE A N   1 
ATOM   3072 C CA  . ILE A 1 390 ? 21.002  -5.965  31.977 1.00 23.08 ? 390  ILE A CA  1 
ATOM   3073 C C   . ILE A 1 390 ? 20.318  -7.302  31.691 1.00 22.94 ? 390  ILE A C   1 
ATOM   3074 O O   . ILE A 1 390 ? 19.097  -7.387  31.789 1.00 21.77 ? 390  ILE A O   1 
ATOM   3075 C CB  . ILE A 1 390 ? 20.096  -4.797  31.479 1.00 22.99 ? 390  ILE A CB  1 
ATOM   3076 C CG1 . ILE A 1 390 ? 20.243  -4.567  29.973 1.00 23.54 ? 390  ILE A CG1 1 
ATOM   3077 C CG2 . ILE A 1 390 ? 20.378  -3.532  32.257 1.00 23.18 ? 390  ILE A CG2 1 
ATOM   3078 C CD1 . ILE A 1 390 ? 19.512  -5.541  29.074 1.00 20.98 ? 390  ILE A CD1 1 
ATOM   3079 N N   . TRP A 1 391 ? 21.093  -8.336  31.327 1.00 22.21 ? 391  TRP A N   1 
ATOM   3080 C CA  . TRP A 1 391 ? 20.519  -9.680  31.108 1.00 21.68 ? 391  TRP A CA  1 
ATOM   3081 C C   . TRP A 1 391 ? 20.367  -10.502 32.412 1.00 21.06 ? 391  TRP A C   1 
ATOM   3082 O O   . TRP A 1 391 ? 21.050  -10.237 33.411 1.00 21.51 ? 391  TRP A O   1 
ATOM   3083 C CB  . TRP A 1 391 ? 21.324  -10.474 30.067 1.00 20.84 ? 391  TRP A CB  1 
ATOM   3084 C CG  . TRP A 1 391 ? 21.734  -9.724  28.828 1.00 20.12 ? 391  TRP A CG  1 
ATOM   3085 C CD1 . TRP A 1 391 ? 23.024  -9.530  28.380 1.00 19.87 ? 391  TRP A CD1 1 
ATOM   3086 C CD2 . TRP A 1 391 ? 20.876  -9.109  27.851 1.00 18.74 ? 391  TRP A CD2 1 
ATOM   3087 N NE1 . TRP A 1 391 ? 23.010  -8.833  27.195 1.00 20.76 ? 391  TRP A NE1 1 
ATOM   3088 C CE2 . TRP A 1 391 ? 21.711  -8.565  26.845 1.00 17.55 ? 391  TRP A CE2 1 
ATOM   3089 C CE3 . TRP A 1 391 ? 19.486  -8.981  27.719 1.00 18.79 ? 391  TRP A CE3 1 
ATOM   3090 C CZ2 . TRP A 1 391 ? 21.202  -7.875  25.739 1.00 20.97 ? 391  TRP A CZ2 1 
ATOM   3091 C CZ3 . TRP A 1 391 ? 18.975  -8.298  26.607 1.00 20.40 ? 391  TRP A CZ3 1 
ATOM   3092 C CH2 . TRP A 1 391 ? 19.820  -7.762  25.633 1.00 21.38 ? 391  TRP A CH2 1 
ATOM   3093 N N   . VAL A 1 392 ? 19.458  -11.479 32.385 1.00 20.50 ? 392  VAL A N   1 
ATOM   3094 C CA  . VAL A 1 392 ? 19.341  -12.500 33.426 1.00 19.43 ? 392  VAL A CA  1 
ATOM   3095 C C   . VAL A 1 392 ? 20.586  -13.366 33.339 1.00 20.26 ? 392  VAL A C   1 
ATOM   3096 O O   . VAL A 1 392 ? 20.933  -13.851 32.265 1.00 19.76 ? 392  VAL A O   1 
ATOM   3097 C CB  . VAL A 1 392 ? 18.113  -13.444 33.231 1.00 19.02 ? 392  VAL A CB  1 
ATOM   3098 C CG1 . VAL A 1 392 ? 18.122  -14.547 34.295 1.00 15.42 ? 392  VAL A CG1 1 
ATOM   3099 C CG2 . VAL A 1 392 ? 16.769  -12.652 33.228 1.00 16.39 ? 392  VAL A CG2 1 
ATOM   3100 N N   . ASN A 1 393 ? 21.239  -13.570 34.470 1.00 22.25 ? 393  ASN A N   1 
ATOM   3101 C CA  . ASN A 1 393 ? 22.481  -14.350 34.502 1.00 23.34 ? 393  ASN A CA  1 
ATOM   3102 C C   . ASN A 1 393 ? 22.190  -15.785 34.909 1.00 24.45 ? 393  ASN A C   1 
ATOM   3103 O O   . ASN A 1 393 ? 21.186  -16.070 35.583 1.00 24.31 ? 393  ASN A O   1 
ATOM   3104 C CB  . ASN A 1 393 ? 23.506  -13.700 35.457 1.00 23.77 ? 393  ASN A CB  1 
ATOM   3105 C CG  . ASN A 1 393 ? 24.007  -12.336 34.960 1.00 23.48 ? 393  ASN A CG  1 
ATOM   3106 O OD1 . ASN A 1 393 ? 23.899  -12.012 33.776 1.00 22.95 ? 393  ASN A OD1 1 
ATOM   3107 N ND2 . ASN A 1 393 ? 24.556  -11.535 35.885 1.00 25.12 ? 393  ASN A ND2 1 
ATOM   3108 N N   . SER A 1 394 ? 23.049  -16.695 34.456 1.00 25.53 ? 394  SER A N   1 
ATOM   3109 C CA  . SER A 1 394 ? 23.117  -18.050 34.994 1.00 26.61 ? 394  SER A CA  1 
ATOM   3110 C C   . SER A 1 394 ? 23.531  -17.969 36.454 1.00 26.42 ? 394  SER A C   1 
ATOM   3111 O O   . SER A 1 394 ? 23.905  -16.898 36.935 1.00 26.46 ? 394  SER A O   1 
ATOM   3112 C CB  . SER A 1 394 ? 24.135  -18.888 34.210 1.00 26.88 ? 394  SER A CB  1 
ATOM   3113 O OG  . SER A 1 394 ? 23.723  -19.030 32.862 1.00 30.60 ? 394  SER A OG  1 
ATOM   3114 N N   . SER A 1 395 ? 23.475  -19.098 37.153 1.00 27.19 ? 395  SER A N   1 
ATOM   3115 C CA  . SER A 1 395 ? 23.721  -19.130 38.599 1.00 28.88 ? 395  SER A CA  1 
ATOM   3116 C C   . SER A 1 395 ? 25.120  -18.684 39.050 1.00 29.44 ? 395  SER A C   1 
ATOM   3117 O O   . SER A 1 395 ? 25.308  -18.392 40.229 1.00 30.45 ? 395  SER A O   1 
ATOM   3118 C CB  . SER A 1 395 ? 23.437  -20.525 39.147 1.00 28.68 ? 395  SER A CB  1 
ATOM   3119 O OG  . SER A 1 395 ? 24.445  -21.426 38.717 1.00 30.67 ? 395  SER A OG  1 
ATOM   3120 N N   . ASP A 1 396 ? 26.094  -18.622 38.138 1.00 30.13 ? 396  ASP A N   1 
ATOM   3121 C CA  . ASP A 1 396 ? 27.439  -18.104 38.503 1.00 30.42 ? 396  ASP A CA  1 
ATOM   3122 C C   . ASP A 1 396 ? 27.393  -16.599 38.813 1.00 30.32 ? 396  ASP A C   1 
ATOM   3123 O O   . ASP A 1 396 ? 28.345  -16.016 39.346 1.00 29.69 ? 396  ASP A O   1 
ATOM   3124 C CB  . ASP A 1 396 ? 28.497  -18.441 37.437 1.00 30.57 ? 396  ASP A CB  1 
ATOM   3125 C CG  . ASP A 1 396 ? 28.255  -17.756 36.102 1.00 32.19 ? 396  ASP A CG  1 
ATOM   3126 O OD1 . ASP A 1 396 ? 27.309  -16.928 35.985 1.00 34.53 ? 396  ASP A OD1 1 
ATOM   3127 O OD2 . ASP A 1 396 ? 29.030  -18.045 35.153 1.00 32.32 ? 396  ASP A OD2 1 
ATOM   3128 N N   . GLY A 1 397 ? 26.251  -15.993 38.471 1.00 30.01 ? 397  GLY A N   1 
ATOM   3129 C CA  . GLY A 1 397 ? 25.989  -14.591 38.725 1.00 28.87 ? 397  GLY A CA  1 
ATOM   3130 C C   . GLY A 1 397 ? 26.662  -13.603 37.795 1.00 28.26 ? 397  GLY A C   1 
ATOM   3131 O O   . GLY A 1 397 ? 26.571  -12.411 38.025 1.00 28.36 ? 397  GLY A O   1 
ATOM   3132 N N   . VAL A 1 398 ? 27.337  -14.073 36.748 1.00 28.12 ? 398  VAL A N   1 
ATOM   3133 C CA  . VAL A 1 398 ? 28.079  -13.149 35.858 1.00 28.06 ? 398  VAL A CA  1 
ATOM   3134 C C   . VAL A 1 398 ? 27.904  -13.404 34.352 1.00 27.21 ? 398  VAL A C   1 
ATOM   3135 O O   . VAL A 1 398 ? 28.111  -12.514 33.524 1.00 27.39 ? 398  VAL A O   1 
ATOM   3136 C CB  . VAL A 1 398 ? 29.605  -13.027 36.237 1.00 28.96 ? 398  VAL A CB  1 
ATOM   3137 C CG1 . VAL A 1 398 ? 29.775  -12.179 37.485 1.00 29.27 ? 398  VAL A CG1 1 
ATOM   3138 C CG2 . VAL A 1 398 ? 30.238  -14.400 36.443 1.00 29.06 ? 398  VAL A CG2 1 
ATOM   3139 N N   . THR A 1 399 ? 27.488  -14.610 34.008 1.00 26.63 ? 399  THR A N   1 
ATOM   3140 C CA  . THR A 1 399 ? 27.343  -14.997 32.624 1.00 26.99 ? 399  THR A CA  1 
ATOM   3141 C C   . THR A 1 399 ? 25.854  -14.983 32.209 1.00 25.82 ? 399  THR A C   1 
ATOM   3142 O O   . THR A 1 399 ? 25.071  -15.736 32.763 1.00 25.24 ? 399  THR A O   1 
ATOM   3143 C CB  . THR A 1 399 ? 27.940  -16.415 32.397 1.00 26.87 ? 399  THR A CB  1 
ATOM   3144 O OG1 . THR A 1 399 ? 29.276  -16.467 32.938 1.00 28.99 ? 399  THR A OG1 1 
ATOM   3145 C CG2 . THR A 1 399 ? 27.973  -16.760 30.924 1.00 27.72 ? 399  THR A CG2 1 
ATOM   3146 N N   . PRO A 1 400 ? 25.487  -14.158 31.206 1.00 25.54 ? 400  PRO A N   1 
ATOM   3147 C CA  . PRO A 1 400 ? 24.087  -14.103 30.754 1.00 25.06 ? 400  PRO A CA  1 
ATOM   3148 C C   . PRO A 1 400 ? 23.540  -15.496 30.404 1.00 24.75 ? 400  PRO A C   1 
ATOM   3149 O O   . PRO A 1 400 ? 24.234  -16.292 29.765 1.00 24.55 ? 400  PRO A O   1 
ATOM   3150 C CB  . PRO A 1 400 ? 24.154  -13.223 29.493 1.00 25.68 ? 400  PRO A CB  1 
ATOM   3151 C CG  . PRO A 1 400 ? 25.339  -12.383 29.660 1.00 26.39 ? 400  PRO A CG  1 
ATOM   3152 C CD  . PRO A 1 400 ? 26.347  -13.234 30.437 1.00 25.01 ? 400  PRO A CD  1 
ATOM   3153 N N   . LEU A 1 401 ? 22.321  -15.804 30.845 1.00 22.91 ? 401  LEU A N   1 
ATOM   3154 C CA  . LEU A 1 401 ? 21.736  -17.099 30.559 1.00 21.66 ? 401  LEU A CA  1 
ATOM   3155 C C   . LEU A 1 401 ? 21.257  -17.138 29.103 1.00 21.51 ? 401  LEU A C   1 
ATOM   3156 O O   . LEU A 1 401 ? 20.651  -16.180 28.611 1.00 20.88 ? 401  LEU A O   1 
ATOM   3157 C CB  . LEU A 1 401 ? 20.592  -17.398 31.546 1.00 21.91 ? 401  LEU A CB  1 
ATOM   3158 C CG  . LEU A 1 401 ? 19.954  -18.782 31.476 1.00 21.19 ? 401  LEU A CG  1 
ATOM   3159 C CD1 . LEU A 1 401 ? 19.411  -19.153 32.819 1.00 18.91 ? 401  LEU A CD1 1 
ATOM   3160 C CD2 . LEU A 1 401 ? 18.850  -18.799 30.403 1.00 21.02 ? 401  LEU A CD2 1 
ATOM   3161 N N   . ILE A 1 402 ? 21.529  -18.247 28.422 1.00 21.49 ? 402  ILE A N   1 
ATOM   3162 C CA  . ILE A 1 402 ? 21.241  -18.366 27.011 1.00 22.12 ? 402  ILE A CA  1 
ATOM   3163 C C   . ILE A 1 402 ? 20.102  -19.361 26.852 1.00 21.79 ? 402  ILE A C   1 
ATOM   3164 O O   . ILE A 1 402 ? 20.179  -20.483 27.333 1.00 20.94 ? 402  ILE A O   1 
ATOM   3165 C CB  . ILE A 1 402 ? 22.476  -18.865 26.168 1.00 22.93 ? 402  ILE A CB  1 
ATOM   3166 C CG1 . ILE A 1 402 ? 23.730  -17.988 26.365 1.00 24.40 ? 402  ILE A CG1 1 
ATOM   3167 C CG2 . ILE A 1 402 ? 22.095  -19.010 24.679 1.00 22.46 ? 402  ILE A CG2 1 
ATOM   3168 C CD1 . ILE A 1 402 ? 23.557  -16.497 26.149 1.00 25.62 ? 402  ILE A CD1 1 
ATOM   3169 N N   . GLY A 1 403 ? 19.032  -18.926 26.192 1.00 21.79 ? 403  GLY A N   1 
ATOM   3170 C CA  . GLY A 1 403 ? 17.906  -19.810 25.922 1.00 22.09 ? 403  GLY A CA  1 
ATOM   3171 C C   . GLY A 1 403 ? 17.609  -19.791 24.441 1.00 22.36 ? 403  GLY A C   1 
ATOM   3172 O O   . GLY A 1 403 ? 18.472  -19.481 23.627 1.00 22.54 ? 403  GLY A O   1 
ATOM   3173 N N   . GLU A 1 404 ? 16.386  -20.141 24.082 1.00 22.76 ? 404  GLU A N   1 
ATOM   3174 C CA  . GLU A 1 404 ? 16.002  -20.145 22.701 1.00 23.05 ? 404  GLU A CA  1 
ATOM   3175 C C   . GLU A 1 404 ? 14.551  -19.697 22.588 1.00 22.36 ? 404  GLU A C   1 
ATOM   3176 O O   . GLU A 1 404 ? 13.675  -20.312 23.188 1.00 22.71 ? 404  GLU A O   1 
ATOM   3177 C CB  . GLU A 1 404 ? 16.152  -21.562 22.123 1.00 23.54 ? 404  GLU A CB  1 
ATOM   3178 C CG  . GLU A 1 404 ? 15.915  -21.626 20.608 1.00 28.35 ? 404  GLU A CG  1 
ATOM   3179 C CD  . GLU A 1 404 ? 15.577  -23.009 20.104 1.00 36.03 ? 404  GLU A CD  1 
ATOM   3180 O OE1 . GLU A 1 404 ? 16.032  -24.000 20.735 1.00 39.28 ? 404  GLU A OE1 1 
ATOM   3181 O OE2 . GLU A 1 404 ? 14.864  -23.100 19.065 1.00 38.67 ? 404  GLU A OE2 1 
ATOM   3182 N N   . VAL A 1 405 ? 14.288  -18.647 21.823 1.00 21.24 ? 405  VAL A N   1 
ATOM   3183 C CA  . VAL A 1 405 ? 12.881  -18.301 21.486 1.00 20.90 ? 405  VAL A CA  1 
ATOM   3184 C C   . VAL A 1 405 ? 12.795  -18.096 19.969 1.00 21.46 ? 405  VAL A C   1 
ATOM   3185 O O   . VAL A 1 405 ? 13.536  -18.748 19.246 1.00 21.54 ? 405  VAL A O   1 
ATOM   3186 C CB  . VAL A 1 405 ? 12.262  -17.159 22.368 1.00 20.07 ? 405  VAL A CB  1 
ATOM   3187 C CG1 . VAL A 1 405 ? 10.704  -17.300 22.415 1.00 18.51 ? 405  VAL A CG1 1 
ATOM   3188 C CG2 . VAL A 1 405 ? 12.767  -17.278 23.799 1.00 18.94 ? 405  VAL A CG2 1 
ATOM   3189 N N   . TRP A 1 406 ? 11.919  -17.212 19.495 1.00 21.08 ? 406  TRP A N   1 
ATOM   3190 C CA  . TRP A 1 406 ? 11.631  -17.034 18.071 1.00 21.88 ? 406  TRP A CA  1 
ATOM   3191 C C   . TRP A 1 406 ? 12.871  -16.855 17.154 1.00 22.43 ? 406  TRP A C   1 
ATOM   3192 O O   . TRP A 1 406 ? 12.949  -17.468 16.096 1.00 22.58 ? 406  TRP A O   1 
ATOM   3193 C CB  . TRP A 1 406 ? 10.665  -15.855 17.880 1.00 22.04 ? 406  TRP A CB  1 
ATOM   3194 C CG  . TRP A 1 406 ? 9.341   -16.013 18.581 1.00 20.99 ? 406  TRP A CG  1 
ATOM   3195 C CD1 . TRP A 1 406 ? 8.804   -15.193 19.533 1.00 22.60 ? 406  TRP A CD1 1 
ATOM   3196 C CD2 . TRP A 1 406 ? 8.393   -17.065 18.374 1.00 21.55 ? 406  TRP A CD2 1 
ATOM   3197 N NE1 . TRP A 1 406 ? 7.567   -15.678 19.935 1.00 21.24 ? 406  TRP A NE1 1 
ATOM   3198 C CE2 . TRP A 1 406 ? 7.288   -16.815 19.226 1.00 20.56 ? 406  TRP A CE2 1 
ATOM   3199 C CE3 . TRP A 1 406 ? 8.354   -18.185 17.528 1.00 22.20 ? 406  TRP A CE3 1 
ATOM   3200 C CZ2 . TRP A 1 406 ? 6.174   -17.652 19.270 1.00 21.25 ? 406  TRP A CZ2 1 
ATOM   3201 C CZ3 . TRP A 1 406 ? 7.237   -19.024 17.579 1.00 22.60 ? 406  TRP A CZ3 1 
ATOM   3202 C CH2 . TRP A 1 406 ? 6.170   -18.751 18.454 1.00 21.29 ? 406  TRP A CH2 1 
ATOM   3203 N N   . PRO A 1 407 ? 13.822  -16.004 17.545 1.00 22.61 ? 407  PRO A N   1 
ATOM   3204 C CA  . PRO A 1 407 ? 14.880  -15.755 16.590 1.00 23.68 ? 407  PRO A CA  1 
ATOM   3205 C C   . PRO A 1 407 ? 16.052  -16.761 16.667 1.00 24.60 ? 407  PRO A C   1 
ATOM   3206 O O   . PRO A 1 407 ? 17.074  -16.570 15.998 1.00 26.18 ? 407  PRO A O   1 
ATOM   3207 C CB  . PRO A 1 407 ? 15.344  -14.341 16.967 1.00 23.27 ? 407  PRO A CB  1 
ATOM   3208 C CG  . PRO A 1 407 ? 14.801  -14.057 18.324 1.00 21.52 ? 407  PRO A CG  1 
ATOM   3209 C CD  . PRO A 1 407 ? 14.030  -15.239 18.787 1.00 22.92 ? 407  PRO A CD  1 
ATOM   3210 N N   . GLY A 1 408 ? 15.905  -17.811 17.471 1.00 24.17 ? 408  GLY A N   1 
ATOM   3211 C CA  . GLY A 1 408 ? 17.011  -18.720 17.774 1.00 23.35 ? 408  GLY A CA  1 
ATOM   3212 C C   . GLY A 1 408 ? 17.496  -18.459 19.188 1.00 22.67 ? 408  GLY A C   1 
ATOM   3213 O O   . GLY A 1 408 ? 16.699  -18.111 20.060 1.00 22.18 ? 408  GLY A O   1 
ATOM   3214 N N   . GLN A 1 409 ? 18.797  -18.615 19.417 1.00 21.58 ? 409  GLN A N   1 
ATOM   3215 C CA  . GLN A 1 409 ? 19.404  -18.359 20.727 1.00 20.71 ? 409  GLN A CA  1 
ATOM   3216 C C   . GLN A 1 409 ? 19.196  -16.937 21.191 1.00 20.18 ? 409  GLN A C   1 
ATOM   3217 O O   . GLN A 1 409 ? 19.219  -16.005 20.400 1.00 20.19 ? 409  GLN A O   1 
ATOM   3218 C CB  . GLN A 1 409 ? 20.906  -18.646 20.695 1.00 21.21 ? 409  GLN A CB  1 
ATOM   3219 C CG  . GLN A 1 409 ? 21.247  -20.078 20.917 1.00 24.08 ? 409  GLN A CG  1 
ATOM   3220 C CD  . GLN A 1 409 ? 22.735  -20.282 21.171 1.00 27.03 ? 409  GLN A CD  1 
ATOM   3221 O OE1 . GLN A 1 409 ? 23.503  -19.319 21.279 1.00 30.10 ? 409  GLN A OE1 1 
ATOM   3222 N NE2 . GLN A 1 409 ? 23.141  -21.539 21.294 1.00 27.13 ? 409  GLN A NE2 1 
ATOM   3223 N N   . THR A 1 410 ? 19.014  -16.762 22.489 1.00 20.52 ? 410  THR A N   1 
ATOM   3224 C CA  . THR A 1 410 ? 18.628  -15.451 23.011 1.00 20.47 ? 410  THR A CA  1 
ATOM   3225 C C   . THR A 1 410 ? 19.092  -15.289 24.414 1.00 19.21 ? 410  THR A C   1 
ATOM   3226 O O   . THR A 1 410 ? 19.216  -16.252 25.136 1.00 20.14 ? 410  THR A O   1 
ATOM   3227 C CB  . THR A 1 410 ? 17.075  -15.301 23.130 1.00 20.44 ? 410  THR A CB  1 
ATOM   3228 O OG1 . THR A 1 410 ? 16.556  -16.392 23.900 1.00 22.58 ? 410  THR A OG1 1 
ATOM   3229 C CG2 . THR A 1 410 ? 16.407  -15.251 21.805 1.00 20.54 ? 410  THR A CG2 1 
ATOM   3230 N N   . VAL A 1 411 ? 19.279  -14.042 24.804 1.00 19.20 ? 411  VAL A N   1 
ATOM   3231 C CA  . VAL A 1 411 ? 19.406  -13.641 26.192 1.00 19.00 ? 411  VAL A CA  1 
ATOM   3232 C C   . VAL A 1 411 ? 18.054  -13.024 26.667 1.00 18.97 ? 411  VAL A C   1 
ATOM   3233 O O   . VAL A 1 411 ? 17.209  -12.698 25.863 1.00 19.66 ? 411  VAL A O   1 
ATOM   3234 C CB  . VAL A 1 411 ? 20.545  -12.613 26.334 1.00 18.81 ? 411  VAL A CB  1 
ATOM   3235 C CG1 . VAL A 1 411 ? 21.927  -13.314 26.295 1.00 20.20 ? 411  VAL A CG1 1 
ATOM   3236 C CG2 . VAL A 1 411 ? 20.448  -11.610 25.230 1.00 19.13 ? 411  VAL A CG2 1 
ATOM   3237 N N   . PHE A 1 412 ? 17.876  -12.852 27.969 1.00 19.65 ? 412  PHE A N   1 
ATOM   3238 C CA  . PHE A 1 412 ? 16.585  -12.435 28.540 1.00 19.51 ? 412  PHE A CA  1 
ATOM   3239 C C   . PHE A 1 412 ? 16.815  -11.183 29.383 1.00 19.13 ? 412  PHE A C   1 
ATOM   3240 O O   . PHE A 1 412 ? 17.676  -11.200 30.259 1.00 19.98 ? 412  PHE A O   1 
ATOM   3241 C CB  . PHE A 1 412 ? 16.007  -13.576 29.412 1.00 18.97 ? 412  PHE A CB  1 
ATOM   3242 C CG  . PHE A 1 412 ? 15.728  -14.841 28.647 1.00 18.07 ? 412  PHE A CG  1 
ATOM   3243 C CD1 . PHE A 1 412 ? 14.489  -15.056 28.069 1.00 19.18 ? 412  PHE A CD1 1 
ATOM   3244 C CD2 . PHE A 1 412 ? 16.723  -15.815 28.482 1.00 17.81 ? 412  PHE A CD2 1 
ATOM   3245 C CE1 . PHE A 1 412 ? 14.227  -16.230 27.345 1.00 18.26 ? 412  PHE A CE1 1 
ATOM   3246 C CE2 . PHE A 1 412 ? 16.465  -16.972 27.762 1.00 16.74 ? 412  PHE A CE2 1 
ATOM   3247 C CZ  . PHE A 1 412 ? 15.210  -17.176 27.195 1.00 20.23 ? 412  PHE A CZ  1 
ATOM   3248 N N   . PRO A 1 413 ? 16.066  -10.089 29.122 1.00 18.66 ? 413  PRO A N   1 
ATOM   3249 C CA  . PRO A 1 413 ? 16.259  -8.900  29.946 1.00 18.91 ? 413  PRO A CA  1 
ATOM   3250 C C   . PRO A 1 413 ? 15.879  -9.164  31.372 1.00 19.17 ? 413  PRO A C   1 
ATOM   3251 O O   . PRO A 1 413 ? 14.906  -9.888  31.622 1.00 18.76 ? 413  PRO A O   1 
ATOM   3252 C CB  . PRO A 1 413 ? 15.299  -7.870  29.324 1.00 18.23 ? 413  PRO A CB  1 
ATOM   3253 C CG  . PRO A 1 413 ? 15.111  -8.356  27.922 1.00 17.76 ? 413  PRO A CG  1 
ATOM   3254 C CD  . PRO A 1 413 ? 15.084  -9.843  28.055 1.00 18.34 ? 413  PRO A CD  1 
ATOM   3255 N N   . ASP A 1 414 ? 16.646  -8.590  32.297 1.00 18.84 ? 414  ASP A N   1 
ATOM   3256 C CA  . ASP A 1 414 ? 16.272  -8.594  33.704 1.00 19.52 ? 414  ASP A CA  1 
ATOM   3257 C C   . ASP A 1 414 ? 15.513  -7.305  34.032 1.00 19.84 ? 414  ASP A C   1 
ATOM   3258 O O   . ASP A 1 414 ? 16.092  -6.260  34.323 1.00 18.54 ? 414  ASP A O   1 
ATOM   3259 C CB  . ASP A 1 414 ? 17.473  -8.816  34.643 1.00 19.78 ? 414  ASP A CB  1 
ATOM   3260 C CG  . ASP A 1 414 ? 17.144  -8.550  36.115 1.00 20.29 ? 414  ASP A CG  1 
ATOM   3261 O OD1 . ASP A 1 414 ? 15.960  -8.707  36.539 1.00 22.71 ? 414  ASP A OD1 1 
ATOM   3262 O OD2 . ASP A 1 414 ? 18.076  -8.215  36.884 1.00 19.83 ? 414  ASP A OD2 1 
ATOM   3263 N N   . TYR A 1 415 ? 14.191  -7.389  33.978 1.00 20.01 ? 415  TYR A N   1 
ATOM   3264 C CA  . TYR A 1 415 ? 13.381  -6.175  34.107 1.00 19.62 ? 415  TYR A CA  1 
ATOM   3265 C C   . TYR A 1 415 ? 13.290  -5.713  35.546 1.00 20.84 ? 415  TYR A C   1 
ATOM   3266 O O   . TYR A 1 415 ? 12.793  -4.623  35.812 1.00 21.55 ? 415  TYR A O   1 
ATOM   3267 C CB  . TYR A 1 415 ? 11.981  -6.362  33.498 1.00 19.21 ? 415  TYR A CB  1 
ATOM   3268 C CG  . TYR A 1 415 ? 11.952  -6.535  32.002 1.00 16.10 ? 415  TYR A CG  1 
ATOM   3269 C CD1 . TYR A 1 415 ? 12.126  -5.457  31.143 1.00 15.91 ? 415  TYR A CD1 1 
ATOM   3270 C CD2 . TYR A 1 415 ? 11.688  -7.769  31.443 1.00 13.86 ? 415  TYR A CD2 1 
ATOM   3271 C CE1 . TYR A 1 415 ? 12.076  -5.630  29.781 1.00 13.05 ? 415  TYR A CE1 1 
ATOM   3272 C CE2 . TYR A 1 415 ? 11.662  -7.943  30.081 1.00 15.54 ? 415  TYR A CE2 1 
ATOM   3273 C CZ  . TYR A 1 415 ? 11.865  -6.871  29.260 1.00 16.89 ? 415  TYR A CZ  1 
ATOM   3274 O OH  . TYR A 1 415 ? 11.789  -7.056  27.902 1.00 19.31 ? 415  TYR A OH  1 
ATOM   3275 N N   . THR A 1 416 ? 13.807  -6.512  36.480 1.00 22.24 ? 416  THR A N   1 
ATOM   3276 C CA  . THR A 1 416 ? 13.872  -6.107  37.885 1.00 22.81 ? 416  THR A CA  1 
ATOM   3277 C C   . THR A 1 416 ? 14.985  -5.106  38.162 1.00 23.93 ? 416  THR A C   1 
ATOM   3278 O O   . THR A 1 416 ? 14.920  -4.377  39.139 1.00 23.65 ? 416  THR A O   1 
ATOM   3279 C CB  . THR A 1 416 ? 13.983  -7.316  38.872 1.00 23.50 ? 416  THR A CB  1 
ATOM   3280 O OG1 . THR A 1 416 ? 15.331  -7.829  38.913 1.00 23.93 ? 416  THR A OG1 1 
ATOM   3281 C CG2 . THR A 1 416 ? 13.010  -8.386  38.501 1.00 22.14 ? 416  THR A CG2 1 
ATOM   3282 N N   . ASN A 1 417 ? 16.006  -5.087  37.302 1.00 24.82 ? 417  ASN A N   1 
ATOM   3283 C CA  . ASN A 1 417 ? 17.034  -4.064  37.311 1.00 25.46 ? 417  ASN A CA  1 
ATOM   3284 C C   . ASN A 1 417 ? 16.494  -2.720  36.768 1.00 26.55 ? 417  ASN A C   1 
ATOM   3285 O O   . ASN A 1 417 ? 16.074  -2.657  35.621 1.00 26.29 ? 417  ASN A O   1 
ATOM   3286 C CB  . ASN A 1 417 ? 18.187  -4.551  36.426 1.00 25.61 ? 417  ASN A CB  1 
ATOM   3287 C CG  . ASN A 1 417 ? 19.433  -3.698  36.542 1.00 24.36 ? 417  ASN A CG  1 
ATOM   3288 O OD1 . ASN A 1 417 ? 19.366  -2.518  36.868 1.00 23.41 ? 417  ASN A OD1 1 
ATOM   3289 N ND2 . ASN A 1 417 ? 20.587  -4.304  36.263 1.00 21.74 ? 417  ASN A ND2 1 
ATOM   3290 N N   . PRO A 1 418 ? 16.520  -1.636  37.584 1.00 27.99 ? 418  PRO A N   1 
ATOM   3291 C CA  . PRO A 1 418 ? 16.108  -0.297  37.095 1.00 28.63 ? 418  PRO A CA  1 
ATOM   3292 C C   . PRO A 1 418 ? 16.764  0.107   35.766 1.00 29.20 ? 418  PRO A C   1 
ATOM   3293 O O   . PRO A 1 418 ? 16.116  0.715   34.916 1.00 29.14 ? 418  PRO A O   1 
ATOM   3294 C CB  . PRO A 1 418 ? 16.590  0.652   38.207 1.00 29.08 ? 418  PRO A CB  1 
ATOM   3295 C CG  . PRO A 1 418 ? 16.672  -0.184  39.429 1.00 28.85 ? 418  PRO A CG  1 
ATOM   3296 C CD  . PRO A 1 418 ? 16.941  -1.603  38.998 1.00 28.06 ? 418  PRO A CD  1 
ATOM   3297 N N   . ASN A 1 419 ? 18.043  -0.239  35.603 1.00 29.38 ? 419  ASN A N   1 
ATOM   3298 C CA  . ASN A 1 419 ? 18.790  0.041   34.388 1.00 29.83 ? 419  ASN A CA  1 
ATOM   3299 C C   . ASN A 1 419 ? 18.220  -0.645  33.155 1.00 28.75 ? 419  ASN A C   1 
ATOM   3300 O O   . ASN A 1 419 ? 18.385  -0.162  32.033 1.00 28.37 ? 419  ASN A O   1 
ATOM   3301 C CB  . ASN A 1 419 ? 20.238  -0.418  34.566 1.00 30.94 ? 419  ASN A CB  1 
ATOM   3302 C CG  . ASN A 1 419 ? 21.202  0.730   34.588 1.00 34.65 ? 419  ASN A CG  1 
ATOM   3303 O OD1 . ASN A 1 419 ? 21.351  1.444   33.590 1.00 38.44 ? 419  ASN A OD1 1 
ATOM   3304 N ND2 . ASN A 1 419 ? 21.858  0.931   35.729 1.00 37.39 ? 419  ASN A ND2 1 
ATOM   3305 N N   . CYS A 1 420 ? 17.581  -1.791  33.359 1.00 27.55 ? 420  CYS A N   1 
ATOM   3306 C CA  . CYS A 1 420 ? 17.024  -2.532  32.237 1.00 27.24 ? 420  CYS A CA  1 
ATOM   3307 C C   . CYS A 1 420 ? 15.903  -1.715  31.614 1.00 26.95 ? 420  CYS A C   1 
ATOM   3308 O O   . CYS A 1 420 ? 15.820  -1.631  30.398 1.00 27.62 ? 420  CYS A O   1 
ATOM   3309 C CB  . CYS A 1 420 ? 16.543  -3.910  32.669 1.00 27.42 ? 420  CYS A CB  1 
ATOM   3310 S SG  . CYS A 1 420 ? 15.949  -4.913  31.304 1.00 26.70 ? 420  CYS A SG  1 
ATOM   3311 N N   . ALA A 1 421 ? 15.089  -1.061  32.448 1.00 26.81 ? 421  ALA A N   1 
ATOM   3312 C CA  . ALA A 1 421 ? 14.038  -0.170  31.941 1.00 26.48 ? 421  ALA A CA  1 
ATOM   3313 C C   . ALA A 1 421 ? 14.601  1.006   31.137 1.00 25.97 ? 421  ALA A C   1 
ATOM   3314 O O   . ALA A 1 421 ? 14.035  1.375   30.139 1.00 26.52 ? 421  ALA A O   1 
ATOM   3315 C CB  . ALA A 1 421 ? 13.137  0.314   33.065 1.00 26.34 ? 421  ALA A CB  1 
ATOM   3316 N N   . VAL A 1 422 ? 15.727  1.574   31.553 1.00 25.99 ? 422  VAL A N   1 
ATOM   3317 C CA  . VAL A 1 422 ? 16.442  2.581   30.744 1.00 25.26 ? 422  VAL A CA  1 
ATOM   3318 C C   . VAL A 1 422 ? 16.775  2.006   29.358 1.00 24.29 ? 422  VAL A C   1 
ATOM   3319 O O   . VAL A 1 422 ? 16.436  2.585   28.331 1.00 24.62 ? 422  VAL A O   1 
ATOM   3320 C CB  . VAL A 1 422 ? 17.732  3.050   31.451 1.00 25.71 ? 422  VAL A CB  1 
ATOM   3321 C CG1 . VAL A 1 422 ? 18.517  4.040   30.589 1.00 25.86 ? 422  VAL A CG1 1 
ATOM   3322 C CG2 . VAL A 1 422 ? 17.410  3.629   32.847 1.00 25.78 ? 422  VAL A CG2 1 
ATOM   3323 N N   . TRP A 1 423 ? 17.382  0.830   29.340 1.00 23.27 ? 423  TRP A N   1 
ATOM   3324 C CA  . TRP A 1 423 ? 17.731  0.145   28.095 1.00 22.37 ? 423  TRP A CA  1 
ATOM   3325 C C   . TRP A 1 423 ? 16.496  -0.107  27.235 1.00 21.22 ? 423  TRP A C   1 
ATOM   3326 O O   . TRP A 1 423 ? 16.503  0.143   26.044 1.00 20.20 ? 423  TRP A O   1 
ATOM   3327 C CB  . TRP A 1 423 ? 18.401  -1.205  28.398 1.00 22.75 ? 423  TRP A CB  1 
ATOM   3328 C CG  . TRP A 1 423 ? 18.426  -2.162  27.205 1.00 23.75 ? 423  TRP A CG  1 
ATOM   3329 C CD1 . TRP A 1 423 ? 19.310  -2.145  26.164 1.00 24.96 ? 423  TRP A CD1 1 
ATOM   3330 C CD2 . TRP A 1 423 ? 17.556  -3.286  26.970 1.00 24.85 ? 423  TRP A CD2 1 
ATOM   3331 N NE1 . TRP A 1 423 ? 19.020  -3.158  25.279 1.00 25.41 ? 423  TRP A NE1 1 
ATOM   3332 C CE2 . TRP A 1 423 ? 17.960  -3.880  25.754 1.00 24.55 ? 423  TRP A CE2 1 
ATOM   3333 C CE3 . TRP A 1 423 ? 16.462  -3.839  27.664 1.00 24.13 ? 423  TRP A CE3 1 
ATOM   3334 C CZ2 . TRP A 1 423 ? 17.307  -4.994  25.206 1.00 23.77 ? 423  TRP A CZ2 1 
ATOM   3335 C CZ3 . TRP A 1 423 ? 15.818  -4.941  27.123 1.00 24.23 ? 423  TRP A CZ3 1 
ATOM   3336 C CH2 . TRP A 1 423 ? 16.241  -5.507  25.905 1.00 24.25 ? 423  TRP A CH2 1 
ATOM   3337 N N   . TRP A 1 424 ? 15.448  -0.634  27.863 1.00 20.67 ? 424  TRP A N   1 
ATOM   3338 C CA  . TRP A 1 424 ? 14.202  -0.988  27.188 1.00 20.45 ? 424  TRP A CA  1 
ATOM   3339 C C   . TRP A 1 424 ? 13.586  0.278   26.606 1.00 20.14 ? 424  TRP A C   1 
ATOM   3340 O O   . TRP A 1 424 ? 13.079  0.278   25.504 1.00 20.60 ? 424  TRP A O   1 
ATOM   3341 C CB  . TRP A 1 424 ? 13.283  -1.600  28.251 1.00 19.40 ? 424  TRP A CB  1 
ATOM   3342 C CG  . TRP A 1 424 ? 11.999  -2.303  27.853 1.00 19.29 ? 424  TRP A CG  1 
ATOM   3343 C CD1 . TRP A 1 424 ? 10.752  -2.079  28.403 1.00 16.25 ? 424  TRP A CD1 1 
ATOM   3344 C CD2 . TRP A 1 424 ? 11.839  -3.396  26.936 1.00 18.34 ? 424  TRP A CD2 1 
ATOM   3345 N NE1 . TRP A 1 424 ? 9.833   -2.934  27.863 1.00 17.71 ? 424  TRP A NE1 1 
ATOM   3346 C CE2 . TRP A 1 424 ? 10.461  -3.762  26.966 1.00 19.31 ? 424  TRP A CE2 1 
ATOM   3347 C CE3 . TRP A 1 424 ? 12.712  -4.100  26.084 1.00 18.48 ? 424  TRP A CE3 1 
ATOM   3348 C CZ2 . TRP A 1 424 ? 9.945   -4.773  26.172 1.00 17.30 ? 424  TRP A CZ2 1 
ATOM   3349 C CZ3 . TRP A 1 424 ? 12.198  -5.117  25.312 1.00 17.79 ? 424  TRP A CZ3 1 
ATOM   3350 C CH2 . TRP A 1 424 ? 10.829  -5.456  25.372 1.00 19.49 ? 424  TRP A CH2 1 
ATOM   3351 N N   . THR A 1 425 ? 13.624  1.362   27.366 1.00 21.44 ? 425  THR A N   1 
ATOM   3352 C CA  . THR A 1 425 ? 13.026  2.631   26.931 1.00 22.56 ? 425  THR A CA  1 
ATOM   3353 C C   . THR A 1 425 ? 13.681  3.127   25.635 1.00 23.38 ? 425  THR A C   1 
ATOM   3354 O O   . THR A 1 425 ? 13.001  3.450   24.663 1.00 24.41 ? 425  THR A O   1 
ATOM   3355 C CB  . THR A 1 425 ? 13.091  3.683   28.076 1.00 22.71 ? 425  THR A CB  1 
ATOM   3356 O OG1 . THR A 1 425 ? 12.334  3.198   29.195 1.00 20.94 ? 425  THR A OG1 1 
ATOM   3357 C CG2 . THR A 1 425 ? 12.582  5.053   27.629 1.00 21.85 ? 425  THR A CG2 1 
ATOM   3358 N N   . LYS A 1 426 ? 15.009  3.149   25.626 1.00 24.83 ? 426  LYS A N   1 
ATOM   3359 C CA  . LYS A 1 426 ? 15.790  3.568   24.466 1.00 25.06 ? 426  LYS A CA  1 
ATOM   3360 C C   . LYS A 1 426 ? 15.555  2.695   23.254 1.00 24.76 ? 426  LYS A C   1 
ATOM   3361 O O   . LYS A 1 426 ? 15.567  3.194   22.126 1.00 24.88 ? 426  LYS A O   1 
ATOM   3362 C CB  . LYS A 1 426 ? 17.279  3.606   24.815 1.00 25.89 ? 426  LYS A CB  1 
ATOM   3363 C CG  . LYS A 1 426 ? 18.195  4.100   23.692 1.00 29.83 ? 426  LYS A CG  1 
ATOM   3364 C CD  . LYS A 1 426 ? 17.881  5.543   23.319 1.00 34.35 ? 426  LYS A CD  1 
ATOM   3365 C CE  . LYS A 1 426 ? 19.100  6.230   22.706 1.00 36.44 ? 426  LYS A CE  1 
ATOM   3366 N NZ  . LYS A 1 426 ? 18.851  7.689   22.455 1.00 37.52 ? 426  LYS A NZ  1 
ATOM   3367 N N   . GLU A 1 427 ? 15.334  1.399   23.469 1.00 23.74 ? 427  GLU A N   1 
ATOM   3368 C CA  . GLU A 1 427 ? 15.048  0.514   22.351 1.00 23.92 ? 427  GLU A CA  1 
ATOM   3369 C C   . GLU A 1 427 ? 13.701  0.893   21.730 1.00 23.14 ? 427  GLU A C   1 
ATOM   3370 O O   . GLU A 1 427 ? 13.560  0.903   20.516 1.00 22.32 ? 427  GLU A O   1 
ATOM   3371 C CB  . GLU A 1 427 ? 15.040  -0.960  22.769 1.00 23.36 ? 427  GLU A CB  1 
ATOM   3372 C CG  . GLU A 1 427 ? 16.390  -1.543  23.166 1.00 25.56 ? 427  GLU A CG  1 
ATOM   3373 C CD  . GLU A 1 427 ? 17.498  -1.337  22.120 1.00 25.14 ? 427  GLU A CD  1 
ATOM   3374 O OE1 . GLU A 1 427 ? 17.228  -1.384  20.901 1.00 26.96 ? 427  GLU A OE1 1 
ATOM   3375 O OE2 . GLU A 1 427 ? 18.654  -1.112  22.532 1.00 27.10 ? 427  GLU A OE2 1 
ATOM   3376 N N   . PHE A 1 428 ? 12.722  1.209   22.571 1.00 23.57 ? 428  PHE A N   1 
ATOM   3377 C CA  . PHE A 1 428 ? 11.404  1.657   22.057 1.00 23.98 ? 428  PHE A CA  1 
ATOM   3378 C C   . PHE A 1 428 ? 11.451  3.015   21.393 1.00 24.27 ? 428  PHE A C   1 
ATOM   3379 O O   . PHE A 1 428 ? 10.798  3.210   20.400 1.00 25.61 ? 428  PHE A O   1 
ATOM   3380 C CB  . PHE A 1 428 ? 10.358  1.656   23.159 1.00 23.19 ? 428  PHE A CB  1 
ATOM   3381 C CG  . PHE A 1 428 ? 9.758   0.322   23.388 1.00 23.06 ? 428  PHE A CG  1 
ATOM   3382 C CD1 . PHE A 1 428 ? 8.850   -0.204  22.482 1.00 24.58 ? 428  PHE A CD1 1 
ATOM   3383 C CD2 . PHE A 1 428 ? 10.111  -0.425  24.496 1.00 23.56 ? 428  PHE A CD2 1 
ATOM   3384 C CE1 . PHE A 1 428 ? 8.306   -1.446  22.691 1.00 24.99 ? 428  PHE A CE1 1 
ATOM   3385 C CE2 . PHE A 1 428 ? 9.566   -1.665  24.706 1.00 24.18 ? 428  PHE A CE2 1 
ATOM   3386 C CZ  . PHE A 1 428 ? 8.661   -2.174  23.814 1.00 24.31 ? 428  PHE A CZ  1 
ATOM   3387 N N   . GLU A 1 429 ? 12.209  3.943   21.982 1.00 26.02 ? 429  GLU A N   1 
ATOM   3388 C CA  . GLU A 1 429 ? 12.519  5.261   21.425 1.00 27.12 ? 429  GLU A CA  1 
ATOM   3389 C C   . GLU A 1 429 ? 13.056  5.113   20.017 1.00 26.72 ? 429  GLU A C   1 
ATOM   3390 O O   . GLU A 1 429 ? 12.482  5.637   19.076 1.00 26.70 ? 429  GLU A O   1 
ATOM   3391 C CB  . GLU A 1 429 ? 13.574  5.939   22.324 1.00 28.08 ? 429  GLU A CB  1 
ATOM   3392 C CG  . GLU A 1 429 ? 13.751  7.445   22.165 1.00 32.39 ? 429  GLU A CG  1 
ATOM   3393 C CD  . GLU A 1 429 ? 14.132  8.135   23.484 1.00 37.25 ? 429  GLU A CD  1 
ATOM   3394 O OE1 . GLU A 1 429 ? 14.539  7.444   24.457 1.00 39.95 ? 429  GLU A OE1 1 
ATOM   3395 O OE2 . GLU A 1 429 ? 14.012  9.379   23.552 1.00 40.24 ? 429  GLU A OE2 1 
ATOM   3396 N N   . LEU A 1 430 ? 14.166  4.390   19.873 1.00 26.45 ? 430  LEU A N   1 
ATOM   3397 C CA  . LEU A 1 430 ? 14.745  4.137   18.556 1.00 26.09 ? 430  LEU A CA  1 
ATOM   3398 C C   . LEU A 1 430 ? 13.786  3.479   17.568 1.00 25.43 ? 430  LEU A C   1 
ATOM   3399 O O   . LEU A 1 430 ? 13.703  3.896   16.415 1.00 25.34 ? 430  LEU A O   1 
ATOM   3400 C CB  . LEU A 1 430 ? 16.022  3.312   18.681 1.00 26.84 ? 430  LEU A CB  1 
ATOM   3401 C CG  . LEU A 1 430 ? 17.143  3.985   19.475 1.00 26.92 ? 430  LEU A CG  1 
ATOM   3402 C CD1 . LEU A 1 430 ? 18.144  2.946   19.915 1.00 30.09 ? 430  LEU A CD1 1 
ATOM   3403 C CD2 . LEU A 1 430 ? 17.805  5.104   18.649 1.00 31.12 ? 430  LEU A CD2 1 
ATOM   3404 N N   . PHE A 1 431 ? 13.056  2.457   18.004 1.00 25.18 ? 431  PHE A N   1 
ATOM   3405 C CA  . PHE A 1 431 ? 12.097  1.816   17.099 1.00 24.65 ? 431  PHE A CA  1 
ATOM   3406 C C   . PHE A 1 431 ? 10.911  2.730   16.737 1.00 24.41 ? 431  PHE A C   1 
ATOM   3407 O O   . PHE A 1 431 ? 10.425  2.709   15.599 1.00 23.22 ? 431  PHE A O   1 
ATOM   3408 C CB  . PHE A 1 431 ? 11.618  0.460   17.638 1.00 24.81 ? 431  PHE A CB  1 
ATOM   3409 C CG  . PHE A 1 431 ? 11.010  -0.420  16.576 1.00 26.20 ? 431  PHE A CG  1 
ATOM   3410 C CD1 . PHE A 1 431 ? 11.724  -0.712  15.412 1.00 24.99 ? 431  PHE A CD1 1 
ATOM   3411 C CD2 . PHE A 1 431 ? 9.719   -0.937  16.726 1.00 26.69 ? 431  PHE A CD2 1 
ATOM   3412 C CE1 . PHE A 1 431 ? 11.174  -1.506  14.436 1.00 26.34 ? 431  PHE A CE1 1 
ATOM   3413 C CE2 . PHE A 1 431 ? 9.156   -1.740  15.751 1.00 25.02 ? 431  PHE A CE2 1 
ATOM   3414 C CZ  . PHE A 1 431 ? 9.879   -2.025  14.600 1.00 26.81 ? 431  PHE A CZ  1 
ATOM   3415 N N   . HIS A 1 432 ? 10.457  3.532   17.699 1.00 25.13 ? 432  HIS A N   1 
ATOM   3416 C CA  . HIS A 1 432 ? 9.314   4.432   17.467 1.00 26.73 ? 432  HIS A CA  1 
ATOM   3417 C C   . HIS A 1 432 ? 9.622   5.483   16.398 1.00 27.33 ? 432  HIS A C   1 
ATOM   3418 O O   . HIS A 1 432 ? 8.729   5.937   15.683 1.00 26.74 ? 432  HIS A O   1 
ATOM   3419 C CB  . HIS A 1 432 ? 8.872   5.120   18.766 1.00 26.34 ? 432  HIS A CB  1 
ATOM   3420 C CG  . HIS A 1 432 ? 7.525   5.770   18.671 1.00 27.68 ? 432  HIS A CG  1 
ATOM   3421 N ND1 . HIS A 1 432 ? 7.359   7.130   18.497 1.00 28.48 ? 432  HIS A ND1 1 
ATOM   3422 C CD2 . HIS A 1 432 ? 6.276   5.242   18.704 1.00 26.63 ? 432  HIS A CD2 1 
ATOM   3423 C CE1 . HIS A 1 432 ? 6.070   7.408   18.429 1.00 25.99 ? 432  HIS A CE1 1 
ATOM   3424 N NE2 . HIS A 1 432 ? 5.393   6.283   18.563 1.00 26.13 ? 432  HIS A NE2 1 
ATOM   3425 N N   . ASN A 1 433 ? 10.899  5.852   16.297 1.00 28.20 ? 433  ASN A N   1 
ATOM   3426 C CA  . ASN A 1 433 ? 11.365  6.779   15.258 1.00 29.45 ? 433  ASN A CA  1 
ATOM   3427 C C   . ASN A 1 433 ? 11.192  6.228   13.854 1.00 29.31 ? 433  ASN A C   1 
ATOM   3428 O O   . ASN A 1 433 ? 11.140  6.987   12.895 1.00 30.48 ? 433  ASN A O   1 
ATOM   3429 C CB  . ASN A 1 433 ? 12.829  7.172   15.514 1.00 29.42 ? 433  ASN A CB  1 
ATOM   3430 C CG  . ASN A 1 433 ? 12.981  8.037   16.736 1.00 31.96 ? 433  ASN A CG  1 
ATOM   3431 O OD1 . ASN A 1 433 ? 12.003  8.620   17.227 1.00 35.01 ? 433  ASN A OD1 1 
ATOM   3432 N ND2 . ASN A 1 433 ? 14.203  8.131   17.249 1.00 33.80 ? 433  ASN A ND2 1 
ATOM   3433 N N   . GLN A 1 434 ? 11.095  4.903   13.743 1.00 29.16 ? 434  GLN A N   1 
ATOM   3434 C CA  . GLN A 1 434 ? 10.915  4.212   12.470 1.00 29.08 ? 434  GLN A CA  1 
ATOM   3435 C C   . GLN A 1 434 ? 9.436   3.872   12.183 1.00 28.37 ? 434  GLN A C   1 
ATOM   3436 O O   . GLN A 1 434 ? 8.918   4.165   11.105 1.00 27.99 ? 434  GLN A O   1 
ATOM   3437 C CB  . GLN A 1 434 ? 11.755  2.936   12.453 1.00 29.01 ? 434  GLN A CB  1 
ATOM   3438 C CG  . GLN A 1 434 ? 13.243  3.155   12.833 1.00 31.38 ? 434  GLN A CG  1 
ATOM   3439 C CD  . GLN A 1 434 ? 14.011  1.843   12.936 1.00 31.84 ? 434  GLN A CD  1 
ATOM   3440 O OE1 . GLN A 1 434 ? 14.505  1.469   14.013 1.00 35.96 ? 434  GLN A OE1 1 
ATOM   3441 N NE2 . GLN A 1 434 ? 14.097  1.123   11.816 1.00 36.04 ? 434  GLN A NE2 1 
ATOM   3442 N N   . VAL A 1 435 ? 8.784   3.226   13.148 1.00 27.73 ? 435  VAL A N   1 
ATOM   3443 C CA  . VAL A 1 435 ? 7.378   2.803   13.049 1.00 27.09 ? 435  VAL A CA  1 
ATOM   3444 C C   . VAL A 1 435 ? 6.678   3.478   14.225 1.00 26.73 ? 435  VAL A C   1 
ATOM   3445 O O   . VAL A 1 435 ? 6.977   3.170   15.370 1.00 26.27 ? 435  VAL A O   1 
ATOM   3446 C CB  . VAL A 1 435 ? 7.252   1.260   13.180 1.00 27.24 ? 435  VAL A CB  1 
ATOM   3447 C CG1 . VAL A 1 435 ? 5.820   0.778   12.929 1.00 25.76 ? 435  VAL A CG1 1 
ATOM   3448 C CG2 . VAL A 1 435 ? 8.234   0.547   12.259 1.00 27.75 ? 435  VAL A CG2 1 
ATOM   3449 N N   . GLU A 1 436 ? 5.785   4.427   13.954 1.00 27.02 ? 436  GLU A N   1 
ATOM   3450 C CA  . GLU A 1 436 ? 5.078   5.171   15.014 1.00 27.44 ? 436  GLU A CA  1 
ATOM   3451 C C   . GLU A 1 436 ? 3.847   4.419   15.564 1.00 25.79 ? 436  GLU A C   1 
ATOM   3452 O O   . GLU A 1 436 ? 2.687   4.856   15.389 1.00 25.61 ? 436  GLU A O   1 
ATOM   3453 C CB  . GLU A 1 436 ? 4.638   6.547   14.513 1.00 27.72 ? 436  GLU A CB  1 
ATOM   3454 C CG  . GLU A 1 436 ? 5.732   7.576   14.269 1.00 30.93 ? 436  GLU A CG  1 
ATOM   3455 C CD  . GLU A 1 436 ? 5.186   8.894   13.680 1.00 32.06 ? 436  GLU A CD  1 
ATOM   3456 O OE1 . GLU A 1 436 ? 4.073   8.903   13.079 1.00 37.46 ? 436  GLU A OE1 1 
ATOM   3457 O OE2 . GLU A 1 436 ? 5.874   9.933   13.821 1.00 37.80 ? 436  GLU A OE2 1 
ATOM   3458 N N   . PHE A 1 437 ? 4.117   3.306   16.242 1.00 24.09 ? 437  PHE A N   1 
ATOM   3459 C CA  . PHE A 1 437 ? 3.101   2.466   16.896 1.00 22.60 ? 437  PHE A CA  1 
ATOM   3460 C C   . PHE A 1 437 ? 2.504   3.197   18.093 1.00 22.22 ? 437  PHE A C   1 
ATOM   3461 O O   . PHE A 1 437 ? 3.084   4.142   18.621 1.00 22.11 ? 437  PHE A O   1 
ATOM   3462 C CB  . PHE A 1 437 ? 3.702   1.123   17.349 1.00 21.42 ? 437  PHE A CB  1 
ATOM   3463 C CG  . PHE A 1 437 ? 4.835   1.282   18.315 1.00 19.80 ? 437  PHE A CG  1 
ATOM   3464 C CD1 . PHE A 1 437 ? 4.599   1.363   19.674 1.00 16.76 ? 437  PHE A CD1 1 
ATOM   3465 C CD2 . PHE A 1 437 ? 6.140   1.409   17.854 1.00 19.65 ? 437  PHE A CD2 1 
ATOM   3466 C CE1 . PHE A 1 437 ? 5.631   1.552   20.573 1.00 17.98 ? 437  PHE A CE1 1 
ATOM   3467 C CE2 . PHE A 1 437 ? 7.191   1.585   18.747 1.00 16.01 ? 437  PHE A CE2 1 
ATOM   3468 C CZ  . PHE A 1 437 ? 6.948   1.681   20.096 1.00 18.20 ? 437  PHE A CZ  1 
ATOM   3469 N N   . ASP A 1 438 ? 1.331   2.740   18.522 1.00 21.94 ? 438  ASP A N   1 
ATOM   3470 C CA  . ASP A 1 438 ? 0.552   3.459   19.532 1.00 20.53 ? 438  ASP A CA  1 
ATOM   3471 C C   . ASP A 1 438 ? 0.530   2.718   20.846 1.00 19.55 ? 438  ASP A C   1 
ATOM   3472 O O   . ASP A 1 438 ? 0.346   3.315   21.893 1.00 19.97 ? 438  ASP A O   1 
ATOM   3473 C CB  . ASP A 1 438 ? -0.858  3.659   18.994 1.00 20.30 ? 438  ASP A CB  1 
ATOM   3474 C CG  . ASP A 1 438 ? -0.865  4.554   17.789 1.00 19.57 ? 438  ASP A CG  1 
ATOM   3475 O OD1 . ASP A 1 438 ? -0.641  5.763   17.984 1.00 20.47 ? 438  ASP A OD1 1 
ATOM   3476 O OD2 . ASP A 1 438 ? -1.038  4.056   16.661 1.00 19.56 ? 438  ASP A OD2 1 
ATOM   3477 N N   . GLY A 1 439 ? 0.711   1.407   20.772 1.00 18.82 ? 439  GLY A N   1 
ATOM   3478 C CA  . GLY A 1 439 ? 0.727   0.577   21.951 1.00 17.89 ? 439  GLY A CA  1 
ATOM   3479 C C   . GLY A 1 439 ? 1.588   -0.651  21.774 1.00 17.32 ? 439  GLY A C   1 
ATOM   3480 O O   . GLY A 1 439 ? 2.098   -0.920  20.683 1.00 16.87 ? 439  GLY A O   1 
ATOM   3481 N N   . ILE A 1 440 ? 1.727   -1.394  22.864 1.00 16.64 ? 440  ILE A N   1 
ATOM   3482 C CA  . ILE A 1 440 ? 2.647   -2.500  22.941 1.00 16.53 ? 440  ILE A CA  1 
ATOM   3483 C C   . ILE A 1 440 ? 1.961   -3.732  23.497 1.00 16.15 ? 440  ILE A C   1 
ATOM   3484 O O   . ILE A 1 440 ? 1.301   -3.681  24.512 1.00 16.19 ? 440  ILE A O   1 
ATOM   3485 C CB  . ILE A 1 440 ? 3.898   -2.135  23.811 1.00 16.17 ? 440  ILE A CB  1 
ATOM   3486 C CG1 . ILE A 1 440 ? 4.662   -0.959  23.175 1.00 17.42 ? 440  ILE A CG1 1 
ATOM   3487 C CG2 . ILE A 1 440 ? 4.872   -3.268  23.842 1.00 16.51 ? 440  ILE A CG2 1 
ATOM   3488 C CD1 . ILE A 1 440 ? 5.271   0.009   24.170 1.00 17.98 ? 440  ILE A CD1 1 
ATOM   3489 N N   . TRP A 1 441 ? 2.178   -4.849  22.820 1.00 15.96 ? 441  TRP A N   1 
ATOM   3490 C CA  . TRP A 1 441 ? 1.677   -6.139  23.232 1.00 15.83 ? 441  TRP A CA  1 
ATOM   3491 C C   . TRP A 1 441 ? 2.919   -6.962  23.653 1.00 16.35 ? 441  TRP A C   1 
ATOM   3492 O O   . TRP A 1 441 ? 3.739   -7.342  22.825 1.00 14.66 ? 441  TRP A O   1 
ATOM   3493 C CB  . TRP A 1 441 ? 0.810   -6.712  22.084 1.00 15.51 ? 441  TRP A CB  1 
ATOM   3494 C CG  . TRP A 1 441 ? 0.492   -8.168  22.086 1.00 14.34 ? 441  TRP A CG  1 
ATOM   3495 C CD1 . TRP A 1 441 ? 0.462   -8.997  23.148 1.00 15.65 ? 441  TRP A CD1 1 
ATOM   3496 C CD2 . TRP A 1 441 ? 0.101   -8.951  20.952 1.00 15.68 ? 441  TRP A CD2 1 
ATOM   3497 N NE1 . TRP A 1 441 ? 0.127   -10.260 22.749 1.00 15.94 ? 441  TRP A NE1 1 
ATOM   3498 C CE2 . TRP A 1 441 ? -0.115  -10.252 21.402 1.00 14.49 ? 441  TRP A CE2 1 
ATOM   3499 C CE3 . TRP A 1 441 ? -0.082  -8.666  19.590 1.00 17.32 ? 441  TRP A CE3 1 
ATOM   3500 C CZ2 . TRP A 1 441 ? -0.489  -11.287 20.547 1.00 16.69 ? 441  TRP A CZ2 1 
ATOM   3501 C CZ3 . TRP A 1 441 ? -0.437  -9.668  18.747 1.00 15.09 ? 441  TRP A CZ3 1 
ATOM   3502 C CH2 . TRP A 1 441 ? -0.647  -10.974 19.219 1.00 16.82 ? 441  TRP A CH2 1 
ATOM   3503 N N   . ILE A 1 442 ? 3.068   -7.146  24.975 1.00 16.30 ? 442  ILE A N   1 
ATOM   3504 C CA  . ILE A 1 442 ? 4.169   -7.903  25.551 1.00 17.49 ? 442  ILE A CA  1 
ATOM   3505 C C   . ILE A 1 442 ? 3.783   -9.371  25.760 1.00 17.61 ? 442  ILE A C   1 
ATOM   3506 O O   . ILE A 1 442 ? 2.801   -9.698  26.437 1.00 18.04 ? 442  ILE A O   1 
ATOM   3507 C CB  . ILE A 1 442 ? 4.810   -7.178  26.786 1.00 18.34 ? 442  ILE A CB  1 
ATOM   3508 C CG1 . ILE A 1 442 ? 3.760   -6.827  27.869 1.00 18.33 ? 442  ILE A CG1 1 
ATOM   3509 C CG2 . ILE A 1 442 ? 5.523   -5.898  26.302 1.00 16.58 ? 442  ILE A CG2 1 
ATOM   3510 C CD1 . ILE A 1 442 ? 4.335   -6.505  29.262 1.00 17.07 ? 442  ILE A CD1 1 
ATOM   3511 N N   . ASP A 1 443 ? 4.535   -10.245 25.087 1.00 17.29 ? 443  ASP A N   1 
ATOM   3512 C CA  . ASP A 1 443 ? 4.203   -11.642 24.944 1.00 17.61 ? 443  ASP A CA  1 
ATOM   3513 C C   . ASP A 1 443 ? 5.325   -12.519 25.508 1.00 18.07 ? 443  ASP A C   1 
ATOM   3514 O O   . ASP A 1 443 ? 6.458   -12.054 25.694 1.00 17.54 ? 443  ASP A O   1 
ATOM   3515 C CB  . ASP A 1 443 ? 3.986   -11.953 23.459 1.00 16.77 ? 443  ASP A CB  1 
ATOM   3516 C CG  . ASP A 1 443 ? 3.349   -13.327 23.208 1.00 17.66 ? 443  ASP A CG  1 
ATOM   3517 O OD1 . ASP A 1 443 ? 2.670   -13.848 24.112 1.00 20.97 ? 443  ASP A OD1 1 
ATOM   3518 O OD2 . ASP A 1 443 ? 3.554   -13.896 22.105 1.00 14.13 ? 443  ASP A OD2 1 
ATOM   3519 N N   . MET A 1 444 ? 4.992   -13.784 25.775 1.00 18.61 ? 444  MET A N   1 
ATOM   3520 C CA  . MET A 1 444 ? 5.985   -14.810 26.087 1.00 19.00 ? 444  MET A CA  1 
ATOM   3521 C C   . MET A 1 444 ? 6.794   -14.445 27.306 1.00 18.37 ? 444  MET A C   1 
ATOM   3522 O O   . MET A 1 444 ? 7.952   -14.841 27.417 1.00 18.21 ? 444  MET A O   1 
ATOM   3523 C CB  . MET A 1 444 ? 6.939   -14.983 24.890 1.00 19.81 ? 444  MET A CB  1 
ATOM   3524 C CG  . MET A 1 444 ? 6.235   -15.305 23.584 1.00 18.52 ? 444  MET A CG  1 
ATOM   3525 S SD  . MET A 1 444 ? 5.840   -17.014 23.539 1.00 22.28 ? 444  MET A SD  1 
ATOM   3526 C CE  . MET A 1 444 ? 7.495   -17.766 23.353 1.00 19.00 ? 444  MET A CE  1 
ATOM   3527 N N   . ASN A 1 445 ? 6.171   -13.703 28.228 1.00 17.90 ? 445  ASN A N   1 
ATOM   3528 C CA  . ASN A 1 445 ? 6.877   -13.072 29.345 1.00 17.22 ? 445  ASN A CA  1 
ATOM   3529 C C   . ASN A 1 445 ? 6.722   -13.737 30.711 1.00 18.25 ? 445  ASN A C   1 
ATOM   3530 O O   . ASN A 1 445 ? 6.821   -13.071 31.746 1.00 17.49 ? 445  ASN A O   1 
ATOM   3531 C CB  . ASN A 1 445 ? 6.534   -11.579 29.428 1.00 16.09 ? 445  ASN A CB  1 
ATOM   3532 C CG  . ASN A 1 445 ? 5.011   -11.324 29.518 1.00 17.21 ? 445  ASN A CG  1 
ATOM   3533 O OD1 . ASN A 1 445 ? 4.212   -12.235 29.372 1.00 12.83 ? 445  ASN A OD1 1 
ATOM   3534 N ND2 . ASN A 1 445 ? 4.637   -10.103 29.747 1.00 18.05 ? 445  ASN A ND2 1 
ATOM   3535 N N   . GLU A 1 446 ? 6.538   -15.058 30.694 1.00 19.09 ? 446  GLU A N   1 
ATOM   3536 C CA  . GLU A 1 446 ? 6.493   -15.892 31.914 1.00 20.24 ? 446  GLU A CA  1 
ATOM   3537 C C   . GLU A 1 446 ? 7.746   -16.027 32.766 1.00 21.38 ? 446  GLU A C   1 
ATOM   3538 O O   . GLU A 1 446 ? 7.588   -16.168 33.974 1.00 22.74 ? 446  GLU A O   1 
ATOM   3539 C CB  . GLU A 1 446 ? 6.010   -17.305 31.600 1.00 20.32 ? 446  GLU A CB  1 
ATOM   3540 C CG  . GLU A 1 446 ? 4.553   -17.404 31.220 1.00 20.73 ? 446  GLU A CG  1 
ATOM   3541 C CD  . GLU A 1 446 ? 4.241   -16.820 29.840 1.00 24.51 ? 446  GLU A CD  1 
ATOM   3542 O OE1 . GLU A 1 446 ? 5.115   -16.896 28.942 1.00 23.95 ? 446  GLU A OE1 1 
ATOM   3543 O OE2 . GLU A 1 446 ? 3.101   -16.309 29.651 1.00 22.00 ? 446  GLU A OE2 1 
ATOM   3544 N N   . VAL A 1 447 ? 8.982   -16.029 32.232 1.00 21.27 ? 447  VAL A N   1 
ATOM   3545 C CA  . VAL A 1 447 ? 9.354   -15.876 30.838 1.00 20.47 ? 447  VAL A CA  1 
ATOM   3546 C C   . VAL A 1 447 ? 9.416   -17.238 30.158 1.00 21.02 ? 447  VAL A C   1 
ATOM   3547 O O   . VAL A 1 447 ? 9.669   -18.257 30.788 1.00 21.04 ? 447  VAL A O   1 
ATOM   3548 C CB  . VAL A 1 447 ? 10.701  -15.108 30.692 1.00 20.75 ? 447  VAL A CB  1 
ATOM   3549 C CG1 . VAL A 1 447 ? 11.869  -15.972 31.137 1.00 19.78 ? 447  VAL A CG1 1 
ATOM   3550 C CG2 . VAL A 1 447 ? 10.911  -14.621 29.262 1.00 19.19 ? 447  VAL A CG2 1 
ATOM   3551 N N   . SER A 1 448 ? 9.096   -17.259 28.871 1.00 21.58 ? 448  SER A N   1 
ATOM   3552 C CA  . SER A 1 448 ? 8.937   -18.502 28.131 1.00 21.01 ? 448  SER A CA  1 
ATOM   3553 C C   . SER A 1 448 ? 10.227  -18.821 27.377 1.00 20.29 ? 448  SER A C   1 
ATOM   3554 O O   . SER A 1 448 ? 10.897  -17.916 26.882 1.00 20.36 ? 448  SER A O   1 
ATOM   3555 C CB  . SER A 1 448 ? 7.763   -18.374 27.169 1.00 20.92 ? 448  SER A CB  1 
ATOM   3556 O OG  . SER A 1 448 ? 7.557   -19.560 26.428 1.00 23.49 ? 448  SER A OG  1 
ATOM   3557 N N   . ASN A 1 449 ? 10.569  -20.105 27.314 1.00 18.91 ? 449  ASN A N   1 
ATOM   3558 C CA  . ASN A 1 449 ? 11.841  -20.557 26.702 1.00 18.71 ? 449  ASN A CA  1 
ATOM   3559 C C   . ASN A 1 449 ? 11.560  -21.822 25.872 1.00 18.66 ? 449  ASN A C   1 
ATOM   3560 O O   . ASN A 1 449 ? 10.926  -22.753 26.352 1.00 18.68 ? 449  ASN A O   1 
ATOM   3561 C CB  . ASN A 1 449 ? 12.858  -20.818 27.827 1.00 17.79 ? 449  ASN A CB  1 
ATOM   3562 C CG  . ASN A 1 449 ? 14.328  -20.920 27.344 1.00 17.97 ? 449  ASN A CG  1 
ATOM   3563 O OD1 . ASN A 1 449 ? 14.628  -20.755 26.176 1.00 19.67 ? 449  ASN A OD1 1 
ATOM   3564 N ND2 . ASN A 1 449 ? 15.235  -21.217 28.278 1.00 14.91 ? 449  ASN A ND2 1 
ATOM   3565 N N   . PHE A 1 450 ? 11.974  -21.854 24.613 1.00 18.85 ? 450  PHE A N   1 
ATOM   3566 C CA  . PHE A 1 450 ? 11.755  -23.053 23.804 1.00 19.80 ? 450  PHE A CA  1 
ATOM   3567 C C   . PHE A 1 450 ? 12.649  -24.241 24.213 1.00 20.94 ? 450  PHE A C   1 
ATOM   3568 O O   . PHE A 1 450 ? 12.443  -25.373 23.758 1.00 22.27 ? 450  PHE A O   1 
ATOM   3569 C CB  . PHE A 1 450 ? 11.936  -22.746 22.318 1.00 19.92 ? 450  PHE A CB  1 
ATOM   3570 C CG  . PHE A 1 450 ? 10.892  -21.829 21.752 1.00 19.13 ? 450  PHE A CG  1 
ATOM   3571 C CD1 . PHE A 1 450 ? 9.652   -21.646 22.408 1.00 20.01 ? 450  PHE A CD1 1 
ATOM   3572 C CD2 . PHE A 1 450 ? 11.102  -21.204 20.539 1.00 17.42 ? 450  PHE A CD2 1 
ATOM   3573 C CE1 . PHE A 1 450 ? 8.677   -20.811 21.877 1.00 16.56 ? 450  PHE A CE1 1 
ATOM   3574 C CE2 . PHE A 1 450 ? 10.124  -20.366 20.001 1.00 20.65 ? 450  PHE A CE2 1 
ATOM   3575 C CZ  . PHE A 1 450 ? 8.900   -20.181 20.678 1.00 18.07 ? 450  PHE A CZ  1 
ATOM   3576 N N   . VAL A 1 451 ? 13.629  -23.982 25.072 1.00 20.53 ? 451  VAL A N   1 
ATOM   3577 C CA  . VAL A 1 451 ? 14.400  -25.045 25.699 1.00 21.33 ? 451  VAL A CA  1 
ATOM   3578 C C   . VAL A 1 451 ? 14.094  -25.023 27.197 1.00 21.72 ? 451  VAL A C   1 
ATOM   3579 O O   . VAL A 1 451 ? 13.641  -24.016 27.723 1.00 21.63 ? 451  VAL A O   1 
ATOM   3580 C CB  . VAL A 1 451 ? 15.947  -24.904 25.444 1.00 20.08 ? 451  VAL A CB  1 
ATOM   3581 C CG1 . VAL A 1 451 ? 16.246  -25.101 23.988 1.00 22.62 ? 451  VAL A CG1 1 
ATOM   3582 C CG2 . VAL A 1 451 ? 16.457  -23.568 25.883 1.00 19.19 ? 451  VAL A CG2 1 
ATOM   3583 N N   . ASP A 1 452 ? 14.325  -26.141 27.870 1.00 22.28 ? 452  ASP A N   1 
ATOM   3584 C CA  . ASP A 1 452 ? 14.057  -26.244 29.291 1.00 23.43 ? 452  ASP A CA  1 
ATOM   3585 C C   . ASP A 1 452 ? 15.259  -25.726 30.087 1.00 23.52 ? 452  ASP A C   1 
ATOM   3586 O O   . ASP A 1 452 ? 16.312  -26.365 30.115 1.00 25.15 ? 452  ASP A O   1 
ATOM   3587 C CB  . ASP A 1 452 ? 13.717  -27.701 29.660 1.00 23.19 ? 452  ASP A CB  1 
ATOM   3588 C CG  . ASP A 1 452 ? 12.349  -28.157 29.124 1.00 25.86 ? 452  ASP A CG  1 
ATOM   3589 O OD1 . ASP A 1 452 ? 11.485  -27.307 28.756 1.00 26.74 ? 452  ASP A OD1 1 
ATOM   3590 O OD2 . ASP A 1 452 ? 12.130  -29.383 29.075 1.00 28.29 ? 452  ASP A OD2 1 
ATOM   3591 N N   . GLY A 1 453 ? 15.113  -24.556 30.708 1.00 23.59 ? 453  GLY A N   1 
ATOM   3592 C CA  . GLY A 1 453 ? 16.157  -24.001 31.555 1.00 23.50 ? 453  GLY A CA  1 
ATOM   3593 C C   . GLY A 1 453 ? 17.071  -23.089 30.771 1.00 24.36 ? 453  GLY A C   1 
ATOM   3594 O O   . GLY A 1 453 ? 17.009  -21.865 30.891 1.00 24.43 ? 453  GLY A O   1 
ATOM   3595 N N   . SER A 1 454 ? 17.947  -23.700 29.985 1.00 24.43 ? 454  SER A N   1 
ATOM   3596 C CA  . SER A 1 454 ? 18.899  -22.976 29.160 1.00 24.54 ? 454  SER A CA  1 
ATOM   3597 C C   . SER A 1 454 ? 19.335  -23.925 28.051 1.00 24.55 ? 454  SER A C   1 
ATOM   3598 O O   . SER A 1 454 ? 18.947  -25.105 28.044 1.00 25.00 ? 454  SER A O   1 
ATOM   3599 C CB  . SER A 1 454 ? 20.125  -22.557 29.987 1.00 24.60 ? 454  SER A CB  1 
ATOM   3600 O OG  . SER A 1 454 ? 20.903  -23.692 30.334 1.00 23.89 ? 454  SER A OG  1 
ATOM   3601 N N   . VAL A 1 455 ? 20.142  -23.425 27.118 1.00 24.86 ? 455  VAL A N   1 
ATOM   3602 C CA  . VAL A 1 455 ? 20.678  -24.285 26.049 1.00 24.27 ? 455  VAL A CA  1 
ATOM   3603 C C   . VAL A 1 455 ? 21.529  -25.454 26.572 1.00 25.07 ? 455  VAL A C   1 
ATOM   3604 O O   . VAL A 1 455 ? 21.690  -26.467 25.892 1.00 25.55 ? 455  VAL A O   1 
ATOM   3605 C CB  . VAL A 1 455 ? 21.384  -23.502 24.911 1.00 24.31 ? 455  VAL A CB  1 
ATOM   3606 C CG1 . VAL A 1 455 ? 20.400  -22.597 24.219 1.00 21.21 ? 455  VAL A CG1 1 
ATOM   3607 C CG2 . VAL A 1 455 ? 22.627  -22.747 25.392 1.00 22.30 ? 455  VAL A CG2 1 
ATOM   3608 N N   . SER A 1 456 ? 22.019  -25.341 27.794 1.00 25.78 ? 456  SER A N   1 
ATOM   3609 C CA  . SER A 1 456 ? 22.684  -26.481 28.424 1.00 27.44 ? 456  SER A CA  1 
ATOM   3610 C C   . SER A 1 456 ? 21.945  -27.052 29.645 1.00 26.90 ? 456  SER A C   1 
ATOM   3611 O O   . SER A 1 456 ? 22.563  -27.610 30.539 1.00 28.25 ? 456  SER A O   1 
ATOM   3612 C CB  . SER A 1 456 ? 24.137  -26.131 28.733 1.00 27.04 ? 456  SER A CB  1 
ATOM   3613 O OG  . SER A 1 456 ? 24.180  -25.101 29.688 1.00 31.51 ? 456  SER A OG  1 
ATOM   3614 N N   . GLY A 1 457 ? 20.615  -26.923 29.662 1.00 26.90 ? 457  GLY A N   1 
ATOM   3615 C CA  . GLY A 1 457 ? 19.794  -27.417 30.768 1.00 26.47 ? 457  GLY A CA  1 
ATOM   3616 C C   . GLY A 1 457 ? 20.072  -26.693 32.076 1.00 26.54 ? 457  GLY A C   1 
ATOM   3617 O O   . GLY A 1 457 ? 20.531  -25.554 32.076 1.00 27.31 ? 457  GLY A O   1 
ATOM   3618 N N   . CYS A 1 458 ? 19.806  -27.368 33.188 1.00 26.46 ? 458  CYS A N   1 
ATOM   3619 C CA  . CYS A 1 458 ? 20.003  -26.822 34.522 1.00 26.94 ? 458  CYS A CA  1 
ATOM   3620 C C   . CYS A 1 458 ? 20.707  -27.844 35.379 1.00 26.60 ? 458  CYS A C   1 
ATOM   3621 O O   . CYS A 1 458 ? 20.460  -29.036 35.255 1.00 26.49 ? 458  CYS A O   1 
ATOM   3622 C CB  . CYS A 1 458 ? 18.657  -26.591 35.211 1.00 27.18 ? 458  CYS A CB  1 
ATOM   3623 S SG  . CYS A 1 458 ? 17.381  -25.951 34.208 1.00 31.68 ? 458  CYS A SG  1 
ATOM   3624 N N   . SER A 1 459 ? 21.521  -27.368 36.299 1.00 26.90 ? 459  SER A N   1 
ATOM   3625 C CA  . SER A 1 459 ? 22.125  -28.263 37.279 1.00 27.75 ? 459  SER A CA  1 
ATOM   3626 C C   . SER A 1 459 ? 21.059  -28.864 38.182 1.00 27.00 ? 459  SER A C   1 
ATOM   3627 O O   . SER A 1 459 ? 20.050  -28.224 38.507 1.00 26.70 ? 459  SER A O   1 
ATOM   3628 C CB  . SER A 1 459 ? 23.156  -27.518 38.123 1.00 27.66 ? 459  SER A CB  1 
ATOM   3629 O OG  . SER A 1 459 ? 23.956  -26.710 37.282 1.00 29.99 ? 459  SER A OG  1 
ATOM   3630 N N   . THR A 1 460 ? 21.297  -30.112 38.557 1.00 26.48 ? 460  THR A N   1 
ATOM   3631 C CA  . THR A 1 460 ? 20.562  -30.782 39.609 1.00 26.17 ? 460  THR A CA  1 
ATOM   3632 C C   . THR A 1 460 ? 20.973  -30.145 40.930 1.00 25.91 ? 460  THR A C   1 
ATOM   3633 O O   . THR A 1 460 ? 22.150  -30.181 41.334 1.00 25.66 ? 460  THR A O   1 
ATOM   3634 C CB  . THR A 1 460 ? 20.856  -32.291 39.576 1.00 25.98 ? 460  THR A CB  1 
ATOM   3635 O OG1 . THR A 1 460 ? 20.540  -32.791 38.268 1.00 25.07 ? 460  THR A OG1 1 
ATOM   3636 C CG2 . THR A 1 460 ? 20.044  -33.037 40.622 1.00 27.77 ? 460  THR A CG2 1 
ATOM   3637 N N   . ASN A 1 461 ? 19.995  -29.505 41.570 1.00 24.30 ? 461  ASN A N   1 
ATOM   3638 C CA  . ASN A 1 461 ? 20.157  -28.861 42.865 1.00 23.24 ? 461  ASN A CA  1 
ATOM   3639 C C   . ASN A 1 461 ? 18.755  -28.616 43.442 1.00 23.25 ? 461  ASN A C   1 
ATOM   3640 O O   . ASN A 1 461 ? 17.770  -28.914 42.770 1.00 21.78 ? 461  ASN A O   1 
ATOM   3641 C CB  . ASN A 1 461 ? 20.993  -27.567 42.777 1.00 23.31 ? 461  ASN A CB  1 
ATOM   3642 C CG  . ASN A 1 461 ? 20.380  -26.522 41.889 1.00 24.39 ? 461  ASN A CG  1 
ATOM   3643 O OD1 . ASN A 1 461 ? 19.158  -26.266 41.950 1.00 23.93 ? 461  ASN A OD1 1 
ATOM   3644 N ND2 . ASN A 1 461 ? 21.220  -25.866 41.075 1.00 20.37 ? 461  ASN A ND2 1 
ATOM   3645 N N   . ASN A 1 462 ? 18.675  -28.107 44.673 1.00 22.76 ? 462  ASN A N   1 
ATOM   3646 C CA  . ASN A 1 462 ? 17.393  -27.936 45.367 1.00 24.04 ? 462  ASN A CA  1 
ATOM   3647 C C   . ASN A 1 462 ? 16.440  -26.870 44.779 1.00 22.91 ? 462  ASN A C   1 
ATOM   3648 O O   . ASN A 1 462 ? 15.248  -26.837 45.123 1.00 23.51 ? 462  ASN A O   1 
ATOM   3649 C CB  . ASN A 1 462 ? 17.613  -27.683 46.861 1.00 24.96 ? 462  ASN A CB  1 
ATOM   3650 C CG  . ASN A 1 462 ? 18.279  -26.349 47.141 1.00 29.07 ? 462  ASN A CG  1 
ATOM   3651 O OD1 . ASN A 1 462 ? 19.424  -26.096 46.709 1.00 30.86 ? 462  ASN A OD1 1 
ATOM   3652 N ND2 . ASN A 1 462 ? 17.575  -25.480 47.894 1.00 32.72 ? 462  ASN A ND2 1 
ATOM   3653 N N   . LEU A 1 463 ? 16.975  -25.986 43.941 1.00 21.89 ? 463  LEU A N   1 
ATOM   3654 C CA  . LEU A 1 463 ? 16.173  -24.945 43.279 1.00 21.71 ? 463  LEU A CA  1 
ATOM   3655 C C   . LEU A 1 463 ? 15.516  -25.544 42.047 1.00 21.27 ? 463  LEU A C   1 
ATOM   3656 O O   . LEU A 1 463 ? 14.279  -25.469 41.878 1.00 20.17 ? 463  LEU A O   1 
ATOM   3657 C CB  . LEU A 1 463 ? 17.016  -23.709 42.922 1.00 21.17 ? 463  LEU A CB  1 
ATOM   3658 C CG  . LEU A 1 463 ? 17.585  -22.929 44.120 1.00 22.26 ? 463  LEU A CG  1 
ATOM   3659 C CD1 . LEU A 1 463 ? 18.030  -21.517 43.717 1.00 20.21 ? 463  LEU A CD1 1 
ATOM   3660 C CD2 . LEU A 1 463 ? 16.546  -22.832 45.234 1.00 22.15 ? 463  LEU A CD2 1 
ATOM   3661 N N   . ASN A 1 464 ? 16.334  -26.211 41.231 1.00 19.88 ? 464  ASN A N   1 
ATOM   3662 C CA  . ASN A 1 464 ? 15.859  -26.845 39.987 1.00 19.80 ? 464  ASN A CA  1 
ATOM   3663 C C   . ASN A 1 464 ? 15.098  -28.106 40.270 1.00 18.71 ? 464  ASN A C   1 
ATOM   3664 O O   . ASN A 1 464 ? 14.215  -28.498 39.520 1.00 18.49 ? 464  ASN A O   1 
ATOM   3665 C CB  . ASN A 1 464 ? 17.036  -27.167 39.048 1.00 18.61 ? 464  ASN A CB  1 
ATOM   3666 C CG  . ASN A 1 464 ? 17.628  -25.943 38.420 1.00 21.36 ? 464  ASN A CG  1 
ATOM   3667 O OD1 . ASN A 1 464 ? 18.875  -25.793 38.337 1.00 22.53 ? 464  ASN A OD1 1 
ATOM   3668 N ND2 . ASN A 1 464 ? 16.760  -25.053 37.936 1.00 18.27 ? 464  ASN A ND2 1 
ATOM   3669 N N   . ASN A 1 465 ? 15.464  -28.751 41.366 1.00 19.49 ? 465  ASN A N   1 
ATOM   3670 C CA  . ASN A 1 465 ? 14.847  -30.006 41.764 1.00 20.03 ? 465  ASN A CA  1 
ATOM   3671 C C   . ASN A 1 465 ? 14.499  -30.002 43.252 1.00 20.01 ? 465  ASN A C   1 
ATOM   3672 O O   . ASN A 1 465 ? 15.192  -30.619 44.050 1.00 20.08 ? 465  ASN A O   1 
ATOM   3673 C CB  . ASN A 1 465 ? 15.714  -31.224 41.355 1.00 20.21 ? 465  ASN A CB  1 
ATOM   3674 C CG  . ASN A 1 465 ? 16.074  -31.218 39.870 1.00 21.34 ? 465  ASN A CG  1 
ATOM   3675 O OD1 . ASN A 1 465 ? 15.404  -31.854 39.042 1.00 22.91 ? 465  ASN A OD1 1 
ATOM   3676 N ND2 . ASN A 1 465 ? 17.131  -30.493 39.525 1.00 20.04 ? 465  ASN A ND2 1 
ATOM   3677 N N   . PRO A 1 466 ? 13.376  -29.322 43.625 1.00 19.92 ? 466  PRO A N   1 
ATOM   3678 C CA  . PRO A 1 466 ? 13.062  -29.108 45.042 1.00 19.33 ? 466  PRO A CA  1 
ATOM   3679 C C   . PRO A 1 466 ? 12.498  -30.353 45.730 1.00 19.37 ? 466  PRO A C   1 
ATOM   3680 O O   . PRO A 1 466 ? 12.062  -31.298 45.039 1.00 19.77 ? 466  PRO A O   1 
ATOM   3681 C CB  . PRO A 1 466 ? 12.004  -27.974 44.994 1.00 19.66 ? 466  PRO A CB  1 
ATOM   3682 C CG  . PRO A 1 466 ? 11.297  -28.177 43.691 1.00 19.12 ? 466  PRO A CG  1 
ATOM   3683 C CD  . PRO A 1 466 ? 12.347  -28.733 42.729 1.00 19.81 ? 466  PRO A CD  1 
ATOM   3684 N N   . PRO A 1 467 ? 12.468  -30.363 47.085 1.00 18.81 ? 467  PRO A N   1 
ATOM   3685 C CA  . PRO A 1 467 ? 11.955  -31.561 47.765 1.00 18.54 ? 467  PRO A CA  1 
ATOM   3686 C C   . PRO A 1 467 ? 10.467  -31.826 47.432 1.00 19.20 ? 467  PRO A C   1 
ATOM   3687 O O   . PRO A 1 467 ? 10.033  -32.992 47.359 1.00 19.34 ? 467  PRO A O   1 
ATOM   3688 C CB  . PRO A 1 467 ? 12.107  -31.236 49.256 1.00 18.68 ? 467  PRO A CB  1 
ATOM   3689 C CG  . PRO A 1 467 ? 12.826  -29.957 49.350 1.00 19.48 ? 467  PRO A CG  1 
ATOM   3690 C CD  . PRO A 1 467 ? 12.865  -29.293 48.016 1.00 17.84 ? 467  PRO A CD  1 
ATOM   3691 N N   . PHE A 1 468 ? 9.696   -30.752 47.231 1.00 18.46 ? 468  PHE A N   1 
ATOM   3692 C CA  . PHE A 1 468 ? 8.295   -30.884 46.792 1.00 18.00 ? 468  PHE A CA  1 
ATOM   3693 C C   . PHE A 1 468 ? 8.035   -29.997 45.568 1.00 18.13 ? 468  PHE A C   1 
ATOM   3694 O O   . PHE A 1 468 ? 8.458   -28.832 45.526 1.00 17.27 ? 468  PHE A O   1 
ATOM   3695 C CB  . PHE A 1 468 ? 7.365   -30.498 47.935 1.00 17.78 ? 468  PHE A CB  1 
ATOM   3696 C CG  . PHE A 1 468 ? 5.907   -30.498 47.575 1.00 17.08 ? 468  PHE A CG  1 
ATOM   3697 C CD1 . PHE A 1 468 ? 5.168   -31.662 47.662 1.00 17.70 ? 468  PHE A CD1 1 
ATOM   3698 C CD2 . PHE A 1 468 ? 5.271   -29.321 47.153 1.00 17.74 ? 468  PHE A CD2 1 
ATOM   3699 C CE1 . PHE A 1 468 ? 3.789   -31.659 47.354 1.00 21.60 ? 468  PHE A CE1 1 
ATOM   3700 C CE2 . PHE A 1 468 ? 3.895   -29.306 46.847 1.00 17.40 ? 468  PHE A CE2 1 
ATOM   3701 C CZ  . PHE A 1 468 ? 3.169   -30.479 46.931 1.00 18.83 ? 468  PHE A CZ  1 
ATOM   3702 N N   . THR A 1 469 ? 7.337   -30.558 44.585 1.00 18.39 ? 469  THR A N   1 
ATOM   3703 C CA  . THR A 1 469 ? 6.941   -29.843 43.391 1.00 18.71 ? 469  THR A CA  1 
ATOM   3704 C C   . THR A 1 469 ? 5.402   -29.877 43.381 1.00 19.53 ? 469  THR A C   1 
ATOM   3705 O O   . THR A 1 469 ? 4.818   -30.970 43.494 1.00 18.09 ? 469  THR A O   1 
ATOM   3706 C CB  . THR A 1 469 ? 7.496   -30.521 42.101 1.00 20.76 ? 469  THR A CB  1 
ATOM   3707 O OG1 . THR A 1 469 ? 8.916   -30.751 42.228 1.00 19.57 ? 469  THR A OG1 1 
ATOM   3708 C CG2 . THR A 1 469 ? 7.235   -29.611 40.851 1.00 18.53 ? 469  THR A CG2 1 
ATOM   3709 N N   . PRO A 1 470 ? 4.743   -28.684 43.321 1.00 19.62 ? 470  PRO A N   1 
ATOM   3710 C CA  . PRO A 1 470 ? 3.268   -28.694 43.151 1.00 20.67 ? 470  PRO A CA  1 
ATOM   3711 C C   . PRO A 1 470 ? 2.966   -29.341 41.819 1.00 20.96 ? 470  PRO A C   1 
ATOM   3712 O O   . PRO A 1 470 ? 3.890   -29.559 41.051 1.00 21.23 ? 470  PRO A O   1 
ATOM   3713 C CB  . PRO A 1 470 ? 2.884   -27.214 43.113 1.00 20.04 ? 470  PRO A CB  1 
ATOM   3714 C CG  . PRO A 1 470 ? 4.038   -26.480 43.679 1.00 21.22 ? 470  PRO A CG  1 
ATOM   3715 C CD  . PRO A 1 470 ? 5.282   -27.313 43.411 1.00 19.39 ? 470  PRO A CD  1 
ATOM   3716 N N   . ARG A 1 471 ? 1.702   -29.652 41.544 1.00 21.60 ? 471  ARG A N   1 
ATOM   3717 C CA  . ARG A 1 471 ? 1.371   -30.403 40.348 1.00 22.42 ? 471  ARG A CA  1 
ATOM   3718 C C   . ARG A 1 471 ? 1.307   -29.502 39.120 1.00 21.90 ? 471  ARG A C   1 
ATOM   3719 O O   . ARG A 1 471 ? 0.352   -29.533 38.351 1.00 22.20 ? 471  ARG A O   1 
ATOM   3720 C CB  . ARG A 1 471 ? 0.070   -31.191 40.537 1.00 23.29 ? 471  ARG A CB  1 
ATOM   3721 C CG  . ARG A 1 471 ? -1.129  -30.331 40.840 1.00 26.50 ? 471  ARG A CG  1 
ATOM   3722 C CD  . ARG A 1 471 ? -2.386  -31.138 40.676 1.00 32.89 ? 471  ARG A CD  1 
ATOM   3723 N NE  . ARG A 1 471 ? -2.488  -32.191 41.685 1.00 34.98 ? 471  ARG A NE  1 
ATOM   3724 C CZ  . ARG A 1 471 ? -3.580  -32.926 41.889 1.00 36.80 ? 471  ARG A CZ  1 
ATOM   3725 N NH1 . ARG A 1 471 ? -4.681  -32.726 41.151 1.00 34.20 ? 471  ARG A NH1 1 
ATOM   3726 N NH2 . ARG A 1 471 ? -3.571  -33.849 42.848 1.00 38.06 ? 471  ARG A NH2 1 
ATOM   3727 N N   . ILE A 1 472 ? 2.356   -28.714 38.936 1.00 21.57 ? 472  ILE A N   1 
ATOM   3728 C CA  . ILE A 1 472 ? 2.514   -27.889 37.747 1.00 20.57 ? 472  ILE A CA  1 
ATOM   3729 C C   . ILE A 1 472 ? 2.655   -28.770 36.501 1.00 20.97 ? 472  ILE A C   1 
ATOM   3730 O O   . ILE A 1 472 ? 3.161   -29.910 36.581 1.00 20.77 ? 472  ILE A O   1 
ATOM   3731 C CB  . ILE A 1 472 ? 3.707   -26.913 37.913 1.00 20.33 ? 472  ILE A CB  1 
ATOM   3732 C CG1 . ILE A 1 472 ? 5.014   -27.678 38.151 1.00 20.42 ? 472  ILE A CG1 1 
ATOM   3733 C CG2 . ILE A 1 472 ? 3.426   -25.940 39.081 1.00 18.81 ? 472  ILE A CG2 1 
ATOM   3734 C CD1 . ILE A 1 472 ? 6.281   -26.919 37.799 1.00 21.81 ? 472  ILE A CD1 1 
ATOM   3735 N N   . LEU A 1 473 ? 2.183   -28.256 35.359 1.00 20.60 ? 473  LEU A N   1 
ATOM   3736 C CA  . LEU A 1 473 ? 2.299   -28.935 34.081 1.00 20.25 ? 473  LEU A CA  1 
ATOM   3737 C C   . LEU A 1 473 ? 3.735   -29.421 33.885 1.00 20.56 ? 473  LEU A C   1 
ATOM   3738 O O   . LEU A 1 473 ? 4.684   -28.641 34.065 1.00 19.70 ? 473  LEU A O   1 
ATOM   3739 C CB  . LEU A 1 473 ? 1.928   -27.990 32.934 1.00 19.59 ? 473  LEU A CB  1 
ATOM   3740 C CG  . LEU A 1 473 ? 1.933   -28.633 31.522 1.00 20.82 ? 473  LEU A CG  1 
ATOM   3741 C CD1 . LEU A 1 473 ? 1.128   -29.918 31.400 1.00 21.81 ? 473  LEU A CD1 1 
ATOM   3742 C CD2 . LEU A 1 473 ? 1.509   -27.635 30.483 1.00 20.29 ? 473  LEU A CD2 1 
ATOM   3743 N N   . ASP A 1 474 ? 3.866   -30.698 33.524 1.00 21.06 ? 474  ASP A N   1 
ATOM   3744 C CA  . ASP A 1 474 ? 5.151   -31.382 33.286 1.00 21.75 ? 474  ASP A CA  1 
ATOM   3745 C C   . ASP A 1 474 ? 5.924   -31.791 34.541 1.00 21.10 ? 474  ASP A C   1 
ATOM   3746 O O   . ASP A 1 474 ? 6.780   -32.675 34.477 1.00 22.75 ? 474  ASP A O   1 
ATOM   3747 C CB  . ASP A 1 474 ? 6.050   -30.607 32.300 1.00 21.94 ? 474  ASP A CB  1 
ATOM   3748 C CG  . ASP A 1 474 ? 5.434   -30.489 30.919 1.00 25.40 ? 474  ASP A CG  1 
ATOM   3749 O OD1 . ASP A 1 474 ? 4.660   -31.396 30.519 1.00 29.50 ? 474  ASP A OD1 1 
ATOM   3750 O OD2 . ASP A 1 474 ? 5.720   -29.486 30.215 1.00 29.42 ? 474  ASP A OD2 1 
ATOM   3751 N N   . GLY A 1 475 ? 5.674   -31.121 35.662 1.00 20.70 ? 475  GLY A N   1 
ATOM   3752 C CA  . GLY A 1 475 ? 6.236   -31.499 36.956 1.00 19.94 ? 475  GLY A CA  1 
ATOM   3753 C C   . GLY A 1 475 ? 7.679   -31.073 37.230 1.00 20.09 ? 475  GLY A C   1 
ATOM   3754 O O   . GLY A 1 475 ? 8.293   -31.554 38.174 1.00 20.43 ? 475  GLY A O   1 
ATOM   3755 N N   . TYR A 1 476 ? 8.228   -30.188 36.409 1.00 19.63 ? 476  TYR A N   1 
ATOM   3756 C CA  . TYR A 1 476 ? 9.541   -29.582 36.693 1.00 20.42 ? 476  TYR A CA  1 
ATOM   3757 C C   . TYR A 1 476 ? 9.388   -28.090 36.554 1.00 19.97 ? 476  TYR A C   1 
ATOM   3758 O O   . TYR A 1 476 ? 8.788   -27.621 35.595 1.00 19.57 ? 476  TYR A O   1 
ATOM   3759 C CB  . TYR A 1 476 ? 10.647  -30.097 35.727 1.00 21.86 ? 476  TYR A CB  1 
ATOM   3760 C CG  . TYR A 1 476 ? 10.871  -31.589 35.819 1.00 22.47 ? 476  TYR A CG  1 
ATOM   3761 C CD1 . TYR A 1 476 ? 11.966  -32.100 36.526 1.00 26.00 ? 476  TYR A CD1 1 
ATOM   3762 C CD2 . TYR A 1 476 ? 10.006  -32.490 35.199 1.00 22.73 ? 476  TYR A CD2 1 
ATOM   3763 C CE1 . TYR A 1 476 ? 12.171  -33.461 36.633 1.00 25.16 ? 476  TYR A CE1 1 
ATOM   3764 C CE2 . TYR A 1 476 ? 10.198  -33.866 35.311 1.00 23.51 ? 476  TYR A CE2 1 
ATOM   3765 C CZ  . TYR A 1 476 ? 11.292  -34.338 36.028 1.00 25.14 ? 476  TYR A CZ  1 
ATOM   3766 O OH  . TYR A 1 476 ? 11.526  -35.702 36.149 1.00 26.25 ? 476  TYR A OH  1 
ATOM   3767 N N   . LEU A 1 477 ? 9.936   -27.350 37.512 1.00 19.92 ? 477  LEU A N   1 
ATOM   3768 C CA  . LEU A 1 477 ? 9.870   -25.888 37.519 1.00 20.15 ? 477  LEU A CA  1 
ATOM   3769 C C   . LEU A 1 477 ? 10.430  -25.231 36.272 1.00 20.55 ? 477  LEU A C   1 
ATOM   3770 O O   . LEU A 1 477 ? 9.878   -24.236 35.787 1.00 20.07 ? 477  LEU A O   1 
ATOM   3771 C CB  . LEU A 1 477 ? 10.576  -25.318 38.754 1.00 19.33 ? 477  LEU A CB  1 
ATOM   3772 C CG  . LEU A 1 477 ? 9.939   -25.709 40.089 1.00 19.41 ? 477  LEU A CG  1 
ATOM   3773 C CD1 . LEU A 1 477 ? 10.850  -25.338 41.255 1.00 16.64 ? 477  LEU A CD1 1 
ATOM   3774 C CD2 . LEU A 1 477 ? 8.532   -25.080 40.233 1.00 16.01 ? 477  LEU A CD2 1 
ATOM   3775 N N   . PHE A 1 478 ? 11.525  -25.784 35.752 1.00 20.46 ? 478  PHE A N   1 
ATOM   3776 C CA  . PHE A 1 478 ? 12.246  -25.120 34.676 1.00 20.27 ? 478  PHE A CA  1 
ATOM   3777 C C   . PHE A 1 478 ? 11.684  -25.394 33.302 1.00 19.89 ? 478  PHE A C   1 
ATOM   3778 O O   . PHE A 1 478 ? 12.182  -24.858 32.337 1.00 19.48 ? 478  PHE A O   1 
ATOM   3779 C CB  . PHE A 1 478 ? 13.714  -25.526 34.700 1.00 20.88 ? 478  PHE A CB  1 
ATOM   3780 C CG  . PHE A 1 478 ? 13.918  -26.990 34.871 1.00 19.77 ? 478  PHE A CG  1 
ATOM   3781 C CD1 . PHE A 1 478 ? 13.906  -27.838 33.780 1.00 20.23 ? 478  PHE A CD1 1 
ATOM   3782 C CD2 . PHE A 1 478 ? 14.116  -27.524 36.132 1.00 17.71 ? 478  PHE A CD2 1 
ATOM   3783 C CE1 . PHE A 1 478 ? 14.069  -29.206 33.958 1.00 19.42 ? 478  PHE A CE1 1 
ATOM   3784 C CE2 . PHE A 1 478 ? 14.292  -28.882 36.300 1.00 18.78 ? 478  PHE A CE2 1 
ATOM   3785 C CZ  . PHE A 1 478 ? 14.266  -29.716 35.210 1.00 16.85 ? 478  PHE A CZ  1 
ATOM   3786 N N   . CYS A 1 479 ? 10.689  -26.267 33.201 1.00 20.78 ? 479  CYS A N   1 
ATOM   3787 C CA  . CYS A 1 479 ? 10.089  -26.584 31.901 1.00 22.64 ? 479  CYS A CA  1 
ATOM   3788 C C   . CYS A 1 479 ? 9.633   -25.339 31.196 1.00 21.59 ? 479  CYS A C   1 
ATOM   3789 O O   . CYS A 1 479 ? 8.891   -24.543 31.756 1.00 22.14 ? 479  CYS A O   1 
ATOM   3790 C CB  . CYS A 1 479 ? 8.915   -27.560 32.016 1.00 23.02 ? 479  CYS A CB  1 
ATOM   3791 S SG  . CYS A 1 479 ? 9.424   -29.167 32.510 1.00 31.97 ? 479  CYS A SG  1 
ATOM   3792 N N   . LYS A 1 480 ? 10.110  -25.196 29.964 1.00 21.39 ? 480  LYS A N   1 
ATOM   3793 C CA  . LYS A 1 480 ? 9.825   -24.078 29.076 1.00 20.90 ? 480  LYS A CA  1 
ATOM   3794 C C   . LYS A 1 480 ? 10.070  -22.702 29.708 1.00 19.98 ? 480  LYS A C   1 
ATOM   3795 O O   . LYS A 1 480 ? 9.377   -21.737 29.398 1.00 19.30 ? 480  LYS A O   1 
ATOM   3796 C CB  . LYS A 1 480 ? 8.399   -24.202 28.509 1.00 22.16 ? 480  LYS A CB  1 
ATOM   3797 C CG  . LYS A 1 480 ? 8.106   -25.543 27.794 1.00 22.28 ? 480  LYS A CG  1 
ATOM   3798 C CD  . LYS A 1 480 ? 9.058   -25.806 26.613 1.00 24.85 ? 480  LYS A CD  1 
ATOM   3799 C CE  . LYS A 1 480 ? 8.908   -27.233 26.050 1.00 27.05 ? 480  LYS A CE  1 
ATOM   3800 N NZ  . LYS A 1 480 ? 10.261  -27.855 25.745 1.00 31.97 ? 480  LYS A NZ  1 
ATOM   3801 N N   . THR A 1 481 ? 11.043  -22.609 30.611 1.00 18.10 ? 481  THR A N   1 
ATOM   3802 C CA  . THR A 1 481 ? 11.376  -21.308 31.184 1.00 16.52 ? 481  THR A CA  1 
ATOM   3803 C C   . THR A 1 481 ? 12.861  -21.297 31.570 1.00 16.82 ? 481  THR A C   1 
ATOM   3804 O O   . THR A 1 481 ? 13.626  -22.061 30.998 1.00 16.37 ? 481  THR A O   1 
ATOM   3805 C CB  . THR A 1 481 ? 10.384  -20.839 32.327 1.00 15.16 ? 481  THR A CB  1 
ATOM   3806 O OG1 . THR A 1 481 ? 10.698  -19.504 32.718 1.00 13.83 ? 481  THR A OG1 1 
ATOM   3807 C CG2 . THR A 1 481 ? 10.436  -21.716 33.544 1.00 14.69 ? 481  THR A CG2 1 
ATOM   3808 N N   . LEU A 1 482 ? 13.278  -20.423 32.485 1.00 17.31 ? 482  LEU A N   1 
ATOM   3809 C CA  . LEU A 1 482 ? 14.716  -20.340 32.830 1.00 18.41 ? 482  LEU A CA  1 
ATOM   3810 C C   . LEU A 1 482 ? 15.045  -21.269 33.998 1.00 19.11 ? 482  LEU A C   1 
ATOM   3811 O O   . LEU A 1 482 ? 14.147  -21.693 34.743 1.00 19.22 ? 482  LEU A O   1 
ATOM   3812 C CB  . LEU A 1 482 ? 15.129  -18.894 33.148 1.00 18.09 ? 482  LEU A CB  1 
ATOM   3813 C CG  . LEU A 1 482 ? 14.676  -17.786 32.185 1.00 20.15 ? 482  LEU A CG  1 
ATOM   3814 C CD1 . LEU A 1 482 ? 15.191  -16.418 32.628 1.00 21.44 ? 482  LEU A CD1 1 
ATOM   3815 C CD2 . LEU A 1 482 ? 15.127  -18.093 30.776 1.00 22.53 ? 482  LEU A CD2 1 
ATOM   3816 N N   . CYS A 1 483 ? 16.331  -21.626 34.141 1.00 19.93 ? 483  CYS A N   1 
ATOM   3817 C CA  . CYS A 1 483 ? 16.810  -22.279 35.340 1.00 19.91 ? 483  CYS A CA  1 
ATOM   3818 C C   . CYS A 1 483 ? 16.330  -21.495 36.571 1.00 19.60 ? 483  CYS A C   1 
ATOM   3819 O O   . CYS A 1 483 ? 16.384  -20.257 36.603 1.00 20.04 ? 483  CYS A O   1 
ATOM   3820 C CB  . CYS A 1 483 ? 18.354  -22.305 35.339 1.00 21.18 ? 483  CYS A CB  1 
ATOM   3821 S SG  . CYS A 1 483 ? 19.036  -23.073 33.882 1.00 27.19 ? 483  CYS A SG  1 
ATOM   3822 N N   . MET A 1 484 ? 15.844  -22.232 37.569 1.00 18.77 ? 484  MET A N   1 
ATOM   3823 C CA  . MET A 1 484 ? 15.474  -21.705 38.883 1.00 17.55 ? 484  MET A CA  1 
ATOM   3824 C C   . MET A 1 484 ? 16.660  -21.086 39.637 1.00 17.64 ? 484  MET A C   1 
ATOM   3825 O O   . MET A 1 484 ? 16.474  -20.250 40.503 1.00 16.48 ? 484  MET A O   1 
ATOM   3826 C CB  . MET A 1 484 ? 14.833  -22.827 39.697 1.00 17.96 ? 484  MET A CB  1 
ATOM   3827 C CG  . MET A 1 484 ? 13.513  -23.335 39.055 1.00 17.86 ? 484  MET A CG  1 
ATOM   3828 S SD  . MET A 1 484 ? 12.376  -21.920 39.099 1.00 24.36 ? 484  MET A SD  1 
ATOM   3829 C CE  . MET A 1 484 ? 11.905  -21.751 37.384 1.00 21.86 ? 484  MET A CE  1 
ATOM   3830 N N   . ASP A 1 485 ? 17.883  -21.486 39.301 1.00 17.30 ? 485  ASP A N   1 
ATOM   3831 C CA  . ASP A 1 485 ? 19.039  -20.826 39.920 1.00 17.22 ? 485  ASP A CA  1 
ATOM   3832 C C   . ASP A 1 485 ? 19.573  -19.619 39.117 1.00 17.56 ? 485  ASP A C   1 
ATOM   3833 O O   . ASP A 1 485 ? 20.546  -18.963 39.526 1.00 15.76 ? 485  ASP A O   1 
ATOM   3834 C CB  . ASP A 1 485 ? 20.127  -21.834 40.318 1.00 17.88 ? 485  ASP A CB  1 
ATOM   3835 C CG  . ASP A 1 485 ? 20.567  -22.751 39.180 1.00 17.42 ? 485  ASP A CG  1 
ATOM   3836 O OD1 . ASP A 1 485 ? 20.179  -22.516 38.027 1.00 15.63 ? 485  ASP A OD1 1 
ATOM   3837 O OD2 . ASP A 1 485 ? 21.335  -23.725 39.451 1.00 18.63 ? 485  ASP A OD2 1 
ATOM   3838 N N   . ALA A 1 486 ? 18.900  -19.292 38.004 1.00 17.79 ? 486  ALA A N   1 
ATOM   3839 C CA  . ALA A 1 486 ? 19.166  -18.042 37.293 1.00 18.95 ? 486  ALA A CA  1 
ATOM   3840 C C   . ALA A 1 486 ? 19.013  -16.846 38.236 1.00 20.06 ? 486  ALA A C   1 
ATOM   3841 O O   . ALA A 1 486 ? 18.240  -16.895 39.204 1.00 19.66 ? 486  ALA A O   1 
ATOM   3842 C CB  . ALA A 1 486 ? 18.275  -17.886 36.082 1.00 20.09 ? 486  ALA A CB  1 
ATOM   3843 N N   . VAL A 1 487 ? 19.787  -15.791 37.958 1.00 19.85 ? 487  VAL A N   1 
ATOM   3844 C CA  . VAL A 1 487 ? 19.968  -14.691 38.878 1.00 19.56 ? 487  VAL A CA  1 
ATOM   3845 C C   . VAL A 1 487 ? 19.603  -13.343 38.252 1.00 18.88 ? 487  VAL A C   1 
ATOM   3846 O O   . VAL A 1 487 ? 19.913  -13.047 37.107 1.00 18.66 ? 487  VAL A O   1 
ATOM   3847 C CB  . VAL A 1 487 ? 21.433  -14.732 39.471 1.00 20.31 ? 487  VAL A CB  1 
ATOM   3848 C CG1 . VAL A 1 487 ? 21.978  -13.380 39.677 1.00 20.62 ? 487  VAL A CG1 1 
ATOM   3849 C CG2 . VAL A 1 487 ? 21.425  -15.533 40.793 1.00 20.24 ? 487  VAL A CG2 1 
ATOM   3850 N N   . GLN A 1 488 ? 18.909  -12.536 39.038 1.00 19.10 ? 488  GLN A N   1 
ATOM   3851 C CA  . GLN A 1 488 ? 18.343  -11.284 38.596 1.00 19.46 ? 488  GLN A CA  1 
ATOM   3852 C C   . GLN A 1 488 ? 18.483  -10.315 39.754 1.00 19.75 ? 488  GLN A C   1 
ATOM   3853 O O   . GLN A 1 488 ? 18.780  -10.724 40.877 1.00 19.49 ? 488  GLN A O   1 
ATOM   3854 C CB  . GLN A 1 488 ? 16.860  -11.481 38.280 1.00 19.65 ? 488  GLN A CB  1 
ATOM   3855 C CG  . GLN A 1 488 ? 16.590  -11.921 36.881 1.00 19.25 ? 488  GLN A CG  1 
ATOM   3856 C CD  . GLN A 1 488 ? 15.101  -11.921 36.537 1.00 22.48 ? 488  GLN A CD  1 
ATOM   3857 O OE1 . GLN A 1 488 ? 14.582  -10.966 35.955 1.00 24.35 ? 488  GLN A OE1 1 
ATOM   3858 N NE2 . GLN A 1 488 ? 14.431  -13.000 36.860 1.00 19.87 ? 488  GLN A NE2 1 
ATOM   3859 N N   . HIS A 1 489 ? 18.239  -9.039  39.498 1.00 20.58 ? 489  HIS A N   1 
ATOM   3860 C CA  . HIS A 1 489 ? 18.321  -8.027  40.559 1.00 21.26 ? 489  HIS A CA  1 
ATOM   3861 C C   . HIS A 1 489 ? 17.492  -8.326  41.841 1.00 21.42 ? 489  HIS A C   1 
ATOM   3862 O O   . HIS A 1 489 ? 18.028  -8.245  42.962 1.00 19.71 ? 489  HIS A O   1 
ATOM   3863 C CB  . HIS A 1 489 ? 17.997  -6.641  40.005 1.00 21.68 ? 489  HIS A CB  1 
ATOM   3864 C CG  . HIS A 1 489 ? 18.262  -5.550  40.984 1.00 24.60 ? 489  HIS A CG  1 
ATOM   3865 N ND1 . HIS A 1 489 ? 17.290  -4.669  41.393 1.00 24.86 ? 489  HIS A ND1 1 
ATOM   3866 C CD2 . HIS A 1 489 ? 19.380  -5.236  41.686 1.00 26.49 ? 489  HIS A CD2 1 
ATOM   3867 C CE1 . HIS A 1 489 ? 17.799  -3.841  42.289 1.00 27.31 ? 489  HIS A CE1 1 
ATOM   3868 N NE2 . HIS A 1 489 ? 19.067  -4.168  42.489 1.00 27.60 ? 489  HIS A NE2 1 
ATOM   3869 N N   . TRP A 1 490 ? 16.208  -8.696  41.667 1.00 21.38 ? 490  TRP A N   1 
ATOM   3870 C CA  . TRP A 1 490 ? 15.326  -8.995  42.799 1.00 22.08 ? 490  TRP A CA  1 
ATOM   3871 C C   . TRP A 1 490 ? 15.552  -10.366 43.436 1.00 22.37 ? 490  TRP A C   1 
ATOM   3872 O O   . TRP A 1 490 ? 15.006  -10.649 44.507 1.00 23.02 ? 490  TRP A O   1 
ATOM   3873 C CB  . TRP A 1 490 ? 13.832  -8.892  42.421 1.00 22.03 ? 490  TRP A CB  1 
ATOM   3874 C CG  . TRP A 1 490 ? 13.297  -7.532  42.181 1.00 22.16 ? 490  TRP A CG  1 
ATOM   3875 C CD1 . TRP A 1 490 ? 13.934  -6.327  42.381 1.00 21.96 ? 490  TRP A CD1 1 
ATOM   3876 C CD2 . TRP A 1 490 ? 11.975  -7.215  41.726 1.00 22.38 ? 490  TRP A CD2 1 
ATOM   3877 N NE1 . TRP A 1 490 ? 13.096  -5.299  42.047 1.00 22.08 ? 490  TRP A NE1 1 
ATOM   3878 C CE2 . TRP A 1 490 ? 11.889  -5.816  41.642 1.00 23.40 ? 490  TRP A CE2 1 
ATOM   3879 C CE3 . TRP A 1 490 ? 10.860  -7.991  41.356 1.00 24.23 ? 490  TRP A CE3 1 
ATOM   3880 C CZ2 . TRP A 1 490 ? 10.723  -5.161  41.208 1.00 23.75 ? 490  TRP A CZ2 1 
ATOM   3881 C CZ3 . TRP A 1 490 ? 9.700   -7.344  40.938 1.00 22.77 ? 490  TRP A CZ3 1 
ATOM   3882 C CH2 . TRP A 1 490 ? 9.648   -5.935  40.875 1.00 23.21 ? 490  TRP A CH2 1 
ATOM   3883 N N   . GLY A 1 491 ? 16.277  -11.246 42.748 1.00 22.97 ? 491  GLY A N   1 
ATOM   3884 C CA  . GLY A 1 491 ? 16.771  -12.484 43.355 1.00 22.31 ? 491  GLY A CA  1 
ATOM   3885 C C   . GLY A 1 491 ? 16.929  -13.643 42.393 1.00 21.66 ? 491  GLY A C   1 
ATOM   3886 O O   . GLY A 1 491 ? 17.087  -13.453 41.198 1.00 21.86 ? 491  GLY A O   1 
ATOM   3887 N N   . LYS A 1 492 ? 16.884  -14.852 42.931 1.00 21.66 ? 492  LYS A N   1 
ATOM   3888 C CA  . LYS A 1 492 ? 16.961  -16.062 42.122 1.00 21.45 ? 492  LYS A CA  1 
ATOM   3889 C C   . LYS A 1 492 ? 15.602  -16.356 41.476 1.00 20.94 ? 492  LYS A C   1 
ATOM   3890 O O   . LYS A 1 492 ? 14.565  -16.059 42.056 1.00 19.43 ? 492  LYS A O   1 
ATOM   3891 C CB  . LYS A 1 492 ? 17.471  -17.239 42.967 1.00 21.59 ? 492  LYS A CB  1 
ATOM   3892 C CG  . LYS A 1 492 ? 18.927  -17.039 43.439 1.00 25.42 ? 492  LYS A CG  1 
ATOM   3893 C CD  . LYS A 1 492 ? 19.742  -18.330 43.396 1.00 29.15 ? 492  LYS A CD  1 
ATOM   3894 C CE  . LYS A 1 492 ? 21.262  -18.049 43.310 1.00 31.67 ? 492  LYS A CE  1 
ATOM   3895 N NZ  . LYS A 1 492 ? 21.883  -18.912 42.240 1.00 32.75 ? 492  LYS A NZ  1 
ATOM   3896 N N   . GLN A 1 493 ? 15.641  -16.905 40.267 1.00 19.76 ? 493  GLN A N   1 
ATOM   3897 C CA  . GLN A 1 493 ? 14.455  -17.217 39.492 1.00 20.41 ? 493  GLN A CA  1 
ATOM   3898 C C   . GLN A 1 493 ? 13.412  -18.063 40.266 1.00 19.78 ? 493  GLN A C   1 
ATOM   3899 O O   . GLN A 1 493 ? 12.226  -17.847 40.105 1.00 18.24 ? 493  GLN A O   1 
ATOM   3900 C CB  . GLN A 1 493 ? 14.890  -17.878 38.190 1.00 20.79 ? 493  GLN A CB  1 
ATOM   3901 C CG  . GLN A 1 493 ? 13.808  -18.441 37.319 1.00 21.42 ? 493  GLN A CG  1 
ATOM   3902 C CD  . GLN A 1 493 ? 13.106  -17.411 36.436 1.00 22.54 ? 493  GLN A CD  1 
ATOM   3903 O OE1 . GLN A 1 493 ? 13.368  -16.202 36.473 1.00 22.78 ? 493  GLN A OE1 1 
ATOM   3904 N NE2 . GLN A 1 493 ? 12.202  -17.908 35.634 1.00 22.45 ? 493  GLN A NE2 1 
ATOM   3905 N N   . TYR A 1 494 ? 13.881  -19.009 41.084 1.00 18.06 ? 494  TYR A N   1 
ATOM   3906 C CA  . TYR A 1 494 ? 13.057  -19.771 42.028 1.00 18.54 ? 494  TYR A CA  1 
ATOM   3907 C C   . TYR A 1 494 ? 12.042  -18.917 42.787 1.00 19.36 ? 494  TYR A C   1 
ATOM   3908 O O   . TYR A 1 494 ? 10.929  -19.373 43.049 1.00 17.97 ? 494  TYR A O   1 
ATOM   3909 C CB  . TYR A 1 494 ? 13.921  -20.428 43.094 1.00 16.88 ? 494  TYR A CB  1 
ATOM   3910 C CG  . TYR A 1 494 ? 13.234  -21.453 43.955 1.00 17.23 ? 494  TYR A CG  1 
ATOM   3911 C CD1 . TYR A 1 494 ? 12.977  -22.751 43.475 1.00 14.84 ? 494  TYR A CD1 1 
ATOM   3912 C CD2 . TYR A 1 494 ? 12.853  -21.144 45.262 1.00 15.96 ? 494  TYR A CD2 1 
ATOM   3913 C CE1 . TYR A 1 494 ? 12.378  -23.731 44.279 1.00 13.89 ? 494  TYR A CE1 1 
ATOM   3914 C CE2 . TYR A 1 494 ? 12.214  -22.093 46.055 1.00 17.20 ? 494  TYR A CE2 1 
ATOM   3915 C CZ  . TYR A 1 494 ? 11.979  -23.383 45.563 1.00 15.79 ? 494  TYR A CZ  1 
ATOM   3916 O OH  . TYR A 1 494 ? 11.381  -24.304 46.395 1.00 15.60 ? 494  TYR A OH  1 
ATOM   3917 N N   . ASP A 1 495 ? 12.505  -17.747 43.221 1.00 19.15 ? 495  ASP A N   1 
ATOM   3918 C CA  . ASP A 1 495 ? 11.713  -16.837 44.017 1.00 20.05 ? 495  ASP A CA  1 
ATOM   3919 C C   . ASP A 1 495 ? 10.935  -15.842 43.159 1.00 20.53 ? 495  ASP A C   1 
ATOM   3920 O O   . ASP A 1 495 ? 9.809   -15.488 43.508 1.00 19.47 ? 495  ASP A O   1 
ATOM   3921 C CB  . ASP A 1 495 ? 12.593  -16.083 45.015 1.00 19.95 ? 495  ASP A CB  1 
ATOM   3922 C CG  . ASP A 1 495 ? 13.091  -16.971 46.142 1.00 22.17 ? 495  ASP A CG  1 
ATOM   3923 O OD1 . ASP A 1 495 ? 12.299  -17.828 46.657 1.00 24.09 ? 495  ASP A OD1 1 
ATOM   3924 O OD2 . ASP A 1 495 ? 14.263  -16.768 46.543 1.00 21.93 ? 495  ASP A OD2 1 
ATOM   3925 N N   . ILE A 1 496 ? 11.526  -15.398 42.042 1.00 19.53 ? 496  ILE A N   1 
ATOM   3926 C CA  . ILE A 1 496 ? 10.935  -14.272 41.297 1.00 19.66 ? 496  ILE A CA  1 
ATOM   3927 C C   . ILE A 1 496 ? 10.406  -14.624 39.924 1.00 17.99 ? 496  ILE A C   1 
ATOM   3928 O O   . ILE A 1 496 ? 10.047  -13.735 39.184 1.00 18.09 ? 496  ILE A O   1 
ATOM   3929 C CB  . ILE A 1 496 ? 11.903  -13.087 41.178 1.00 20.33 ? 496  ILE A CB  1 
ATOM   3930 C CG1 . ILE A 1 496 ? 13.022  -13.392 40.181 1.00 21.86 ? 496  ILE A CG1 1 
ATOM   3931 C CG2 . ILE A 1 496 ? 12.435  -12.664 42.575 1.00 20.75 ? 496  ILE A CG2 1 
ATOM   3932 C CD1 . ILE A 1 496 ? 14.022  -12.256 40.110 1.00 23.99 ? 496  ILE A CD1 1 
ATOM   3933 N N   . HIS A 1 497 ? 10.351  -15.919 39.600 1.00 16.98 ? 497  HIS A N   1 
ATOM   3934 C CA  . HIS A 1 497 ? 9.841   -16.370 38.311 1.00 17.06 ? 497  HIS A CA  1 
ATOM   3935 C C   . HIS A 1 497 ? 8.457   -15.756 38.015 1.00 16.54 ? 497  HIS A C   1 
ATOM   3936 O O   . HIS A 1 497 ? 8.242   -15.189 36.935 1.00 17.84 ? 497  HIS A O   1 
ATOM   3937 C CB  . HIS A 1 497 ? 9.764   -17.895 38.265 1.00 16.38 ? 497  HIS A CB  1 
ATOM   3938 C CG  . HIS A 1 497 ? 9.038   -18.437 37.071 1.00 16.41 ? 497  HIS A CG  1 
ATOM   3939 N ND1 . HIS A 1 497 ? 7.673   -18.649 37.069 1.00 17.29 ? 497  HIS A ND1 1 
ATOM   3940 C CD2 . HIS A 1 497 ? 9.479   -18.819 35.853 1.00 13.67 ? 497  HIS A CD2 1 
ATOM   3941 C CE1 . HIS A 1 497 ? 7.307   -19.121 35.898 1.00 15.08 ? 497  HIS A CE1 1 
ATOM   3942 N NE2 . HIS A 1 497 ? 8.383   -19.245 35.146 1.00 19.04 ? 497  HIS A NE2 1 
ATOM   3943 N N   . ASN A 1 498 ? 7.536   -15.889 38.961 1.00 16.83 ? 498  ASN A N   1 
ATOM   3944 C CA  . ASN A 1 498 ? 6.161   -15.407 38.795 1.00 17.33 ? 498  ASN A CA  1 
ATOM   3945 C C   . ASN A 1 498 ? 6.093   -13.877 38.624 1.00 18.03 ? 498  ASN A C   1 
ATOM   3946 O O   . ASN A 1 498 ? 5.059   -13.332 38.276 1.00 18.72 ? 498  ASN A O   1 
ATOM   3947 C CB  . ASN A 1 498 ? 5.278   -15.888 39.972 1.00 16.72 ? 498  ASN A CB  1 
ATOM   3948 C CG  . ASN A 1 498 ? 4.826   -17.329 39.828 1.00 16.36 ? 498  ASN A CG  1 
ATOM   3949 O OD1 . ASN A 1 498 ? 4.291   -17.922 40.758 1.00 20.93 ? 498  ASN A OD1 1 
ATOM   3950 N ND2 . ASN A 1 498 ? 4.992   -17.884 38.654 1.00 18.33 ? 498  ASN A ND2 1 
ATOM   3951 N N   . LEU A 1 499 ? 7.229   -13.199 38.820 1.00 18.71 ? 499  LEU A N   1 
ATOM   3952 C CA  . LEU A 1 499 ? 7.284   -11.747 38.749 1.00 19.15 ? 499  LEU A CA  1 
ATOM   3953 C C   . LEU A 1 499 ? 7.862   -11.188 37.471 1.00 19.46 ? 499  LEU A C   1 
ATOM   3954 O O   . LEU A 1 499 ? 7.988   -9.980  37.364 1.00 20.35 ? 499  LEU A O   1 
ATOM   3955 C CB  . LEU A 1 499 ? 8.091   -11.192 39.939 1.00 20.00 ? 499  LEU A CB  1 
ATOM   3956 C CG  . LEU A 1 499 ? 7.579   -11.544 41.333 1.00 20.38 ? 499  LEU A CG  1 
ATOM   3957 C CD1 . LEU A 1 499 ? 8.475   -10.969 42.444 1.00 17.76 ? 499  LEU A CD1 1 
ATOM   3958 C CD2 . LEU A 1 499 ? 6.117   -11.072 41.469 1.00 17.73 ? 499  LEU A CD2 1 
ATOM   3959 N N   . TYR A 1 500 ? 8.250   -12.045 36.514 1.00 18.97 ? 500  TYR A N   1 
ATOM   3960 C CA  . TYR A 1 500 ? 8.884   -11.561 35.284 1.00 17.90 ? 500  TYR A CA  1 
ATOM   3961 C C   . TYR A 1 500 ? 7.899   -10.721 34.429 1.00 17.64 ? 500  TYR A C   1 
ATOM   3962 O O   . TYR A 1 500 ? 8.227   -9.622  33.969 1.00 19.23 ? 500  TYR A O   1 
ATOM   3963 C CB  . TYR A 1 500 ? 9.420   -12.734 34.451 1.00 17.04 ? 500  TYR A CB  1 
ATOM   3964 C CG  . TYR A 1 500 ? 10.347  -12.292 33.334 1.00 17.66 ? 500  TYR A CG  1 
ATOM   3965 C CD1 . TYR A 1 500 ? 11.717  -12.396 33.484 1.00 17.17 ? 500  TYR A CD1 1 
ATOM   3966 C CD2 . TYR A 1 500 ? 9.853   -11.759 32.148 1.00 12.83 ? 500  TYR A CD2 1 
ATOM   3967 C CE1 . TYR A 1 500 ? 12.600  -11.976 32.457 1.00 17.32 ? 500  TYR A CE1 1 
ATOM   3968 C CE2 . TYR A 1 500 ? 10.694  -11.335 31.142 1.00 14.85 ? 500  TYR A CE2 1 
ATOM   3969 C CZ  . TYR A 1 500 ? 12.082  -11.455 31.309 1.00 17.12 ? 500  TYR A CZ  1 
ATOM   3970 O OH  . TYR A 1 500 ? 12.924  -11.059 30.301 1.00 19.32 ? 500  TYR A OH  1 
ATOM   3971 N N   . GLY A 1 501 ? 6.704   -11.248 34.184 1.00 16.66 ? 501  GLY A N   1 
ATOM   3972 C CA  . GLY A 1 501 ? 5.708   -10.501 33.395 1.00 15.75 ? 501  GLY A CA  1 
ATOM   3973 C C   . GLY A 1 501 ? 5.286   -9.218  34.054 1.00 14.27 ? 501  GLY A C   1 
ATOM   3974 O O   . GLY A 1 501 ? 5.208   -8.179  33.422 1.00 15.44 ? 501  GLY A O   1 
ATOM   3975 N N   . TYR A 1 502 ? 5.067   -9.273  35.352 1.00 14.80 ? 502  TYR A N   1 
ATOM   3976 C CA  . TYR A 1 502 ? 4.810   -8.061  36.146 1.00 15.80 ? 502  TYR A CA  1 
ATOM   3977 C C   . TYR A 1 502 ? 5.951   -6.996  36.015 1.00 16.16 ? 502  TYR A C   1 
ATOM   3978 O O   . TYR A 1 502 ? 5.719   -5.817  35.690 1.00 15.78 ? 502  TYR A O   1 
ATOM   3979 C CB  . TYR A 1 502 ? 4.598   -8.499  37.596 1.00 16.75 ? 502  TYR A CB  1 
ATOM   3980 C CG  . TYR A 1 502 ? 4.523   -7.361  38.575 1.00 19.66 ? 502  TYR A CG  1 
ATOM   3981 C CD1 . TYR A 1 502 ? 3.336   -6.685  38.781 1.00 19.40 ? 502  TYR A CD1 1 
ATOM   3982 C CD2 . TYR A 1 502 ? 5.661   -6.959  39.297 1.00 21.22 ? 502  TYR A CD2 1 
ATOM   3983 C CE1 . TYR A 1 502 ? 3.259   -5.626  39.665 1.00 21.21 ? 502  TYR A CE1 1 
ATOM   3984 C CE2 . TYR A 1 502 ? 5.601   -5.902  40.193 1.00 23.20 ? 502  TYR A CE2 1 
ATOM   3985 C CZ  . TYR A 1 502 ? 4.388   -5.244  40.377 1.00 22.34 ? 502  TYR A CZ  1 
ATOM   3986 O OH  . TYR A 1 502 ? 4.296   -4.204  41.267 1.00 23.48 ? 502  TYR A OH  1 
ATOM   3987 N N   . SER A 1 503 ? 7.193   -7.434  36.208 1.00 15.46 ? 503  SER A N   1 
ATOM   3988 C CA  . SER A 1 503 ? 8.354   -6.523  36.117 1.00 16.00 ? 503  SER A CA  1 
ATOM   3989 C C   . SER A 1 503 ? 8.472   -5.969  34.687 1.00 16.24 ? 503  SER A C   1 
ATOM   3990 O O   . SER A 1 503 ? 8.739   -4.783  34.473 1.00 16.67 ? 503  SER A O   1 
ATOM   3991 C CB  . SER A 1 503 ? 9.618   -7.275  36.556 1.00 16.16 ? 503  SER A CB  1 
ATOM   3992 O OG  . SER A 1 503 ? 9.880   -8.359  35.662 1.00 16.78 ? 503  SER A OG  1 
ATOM   3993 N N   . MET A 1 504 ? 8.200   -6.815  33.701 1.00 17.36 ? 504  MET A N   1 
ATOM   3994 C CA  . MET A 1 504 ? 8.201   -6.381  32.314 1.00 17.70 ? 504  MET A CA  1 
ATOM   3995 C C   . MET A 1 504 ? 7.087   -5.347  32.044 1.00 17.66 ? 504  MET A C   1 
ATOM   3996 O O   . MET A 1 504 ? 7.322   -4.367  31.356 1.00 17.18 ? 504  MET A O   1 
ATOM   3997 C CB  . MET A 1 504 ? 8.082   -7.580  31.357 1.00 17.80 ? 504  MET A CB  1 
ATOM   3998 C CG  . MET A 1 504 ? 8.364   -7.238  29.905 1.00 16.37 ? 504  MET A CG  1 
ATOM   3999 S SD  . MET A 1 504 ? 8.147   -8.689  28.882 1.00 18.99 ? 504  MET A SD  1 
ATOM   4000 C CE  . MET A 1 504 ? 8.335   -7.965  27.258 1.00 16.85 ? 504  MET A CE  1 
ATOM   4001 N N   . ALA A 1 505 ? 5.886   -5.561  32.582 1.00 17.42 ? 505  ALA A N   1 
ATOM   4002 C CA  . ALA A 1 505 ? 4.806   -4.545  32.434 1.00 17.32 ? 505  ALA A CA  1 
ATOM   4003 C C   . ALA A 1 505 ? 5.206   -3.227  33.082 1.00 17.27 ? 505  ALA A C   1 
ATOM   4004 O O   . ALA A 1 505 ? 4.984   -2.158  32.475 1.00 16.81 ? 505  ALA A O   1 
ATOM   4005 C CB  . ALA A 1 505 ? 3.469   -5.036  33.023 1.00 16.10 ? 505  ALA A CB  1 
ATOM   4006 N N   . VAL A 1 506 ? 5.816   -3.294  34.279 1.00 17.02 ? 506  VAL A N   1 
ATOM   4007 C CA  . VAL A 1 506 ? 6.244   -2.064  34.994 1.00 17.55 ? 506  VAL A CA  1 
ATOM   4008 C C   . VAL A 1 506 ? 7.236   -1.283  34.106 1.00 18.16 ? 506  VAL A C   1 
ATOM   4009 O O   . VAL A 1 506 ? 7.124   -0.060  33.947 1.00 17.01 ? 506  VAL A O   1 
ATOM   4010 C CB  . VAL A 1 506 ? 6.817   -2.355  36.394 1.00 18.37 ? 506  VAL A CB  1 
ATOM   4011 C CG1 . VAL A 1 506 ? 7.392   -1.092  37.062 1.00 19.03 ? 506  VAL A CG1 1 
ATOM   4012 C CG2 . VAL A 1 506 ? 5.739   -3.018  37.316 1.00 17.51 ? 506  VAL A CG2 1 
ATOM   4013 N N   . ALA A 1 507 ? 8.173   -2.018  33.494 1.00 18.85 ? 507  ALA A N   1 
ATOM   4014 C CA  . ALA A 1 507 ? 9.259   -1.425  32.675 1.00 18.77 ? 507  ALA A CA  1 
ATOM   4015 C C   . ALA A 1 507 ? 8.740   -0.890  31.381 1.00 18.12 ? 507  ALA A C   1 
ATOM   4016 O O   . ALA A 1 507 ? 9.274   0.068   30.842 1.00 18.91 ? 507  ALA A O   1 
ATOM   4017 C CB  . ALA A 1 507 ? 10.319  -2.469  32.389 1.00 18.35 ? 507  ALA A CB  1 
ATOM   4018 N N   . THR A 1 508 ? 7.716   -1.536  30.833 1.00 19.50 ? 508  THR A N   1 
ATOM   4019 C CA  . THR A 1 508 ? 7.134   -1.104  29.569 1.00 19.35 ? 508  THR A CA  1 
ATOM   4020 C C   . THR A 1 508 ? 6.312   0.185   29.734 1.00 20.32 ? 508  THR A C   1 
ATOM   4021 O O   . THR A 1 508 ? 6.313   1.057   28.844 1.00 19.27 ? 508  THR A O   1 
ATOM   4022 C CB  . THR A 1 508 ? 6.348   -2.256  28.901 1.00 20.58 ? 508  THR A CB  1 
ATOM   4023 O OG1 . THR A 1 508 ? 7.216   -3.389  28.783 1.00 18.62 ? 508  THR A OG1 1 
ATOM   4024 C CG2 . THR A 1 508 ? 5.897   -1.872  27.511 1.00 17.99 ? 508  THR A CG2 1 
ATOM   4025 N N   . ALA A 1 509 ? 5.632   0.308   30.878 1.00 20.85 ? 509  ALA A N   1 
ATOM   4026 C CA  . ALA A 1 509 ? 4.940   1.552   31.276 1.00 21.88 ? 509  ALA A CA  1 
ATOM   4027 C C   . ALA A 1 509 ? 5.915   2.712   31.542 1.00 23.02 ? 509  ALA A C   1 
ATOM   4028 O O   . ALA A 1 509 ? 5.693   3.835   31.086 1.00 23.48 ? 509  ALA A O   1 
ATOM   4029 C CB  . ALA A 1 509 ? 4.056   1.306   32.496 1.00 21.01 ? 509  ALA A CB  1 
ATOM   4030 N N   . GLU A 1 510 ? 7.007   2.436   32.255 1.00 23.99 ? 510  GLU A N   1 
ATOM   4031 C CA  . GLU A 1 510 ? 8.118   3.394   32.352 1.00 24.61 ? 510  GLU A CA  1 
ATOM   4032 C C   . GLU A 1 510 ? 8.556   3.922   30.987 1.00 23.96 ? 510  GLU A C   1 
ATOM   4033 O O   . GLU A 1 510 ? 8.646   5.128   30.800 1.00 23.29 ? 510  GLU A O   1 
ATOM   4034 C CB  . GLU A 1 510 ? 9.305   2.798   33.140 1.00 25.85 ? 510  GLU A CB  1 
ATOM   4035 C CG  . GLU A 1 510 ? 10.516  3.731   33.281 1.00 30.46 ? 510  GLU A CG  1 
ATOM   4036 C CD  . GLU A 1 510 ? 10.323  4.894   34.288 1.00 37.81 ? 510  GLU A CD  1 
ATOM   4037 O OE1 . GLU A 1 510 ? 9.284   4.946   35.007 1.00 38.42 ? 510  GLU A OE1 1 
ATOM   4038 O OE2 . GLU A 1 510 ? 11.237  5.768   34.354 1.00 39.31 ? 510  GLU A OE2 1 
ATOM   4039 N N   . ALA A 1 511 ? 8.803   3.016   30.039 1.00 23.96 ? 511  ALA A N   1 
ATOM   4040 C CA  . ALA A 1 511 ? 9.165   3.351   28.667 1.00 23.36 ? 511  ALA A CA  1 
ATOM   4041 C C   . ALA A 1 511 ? 8.132   4.243   27.954 1.00 23.63 ? 511  ALA A C   1 
ATOM   4042 O O   . ALA A 1 511 ? 8.487   5.165   27.192 1.00 23.53 ? 511  ALA A O   1 
ATOM   4043 C CB  . ALA A 1 511 ? 9.380   2.076   27.880 1.00 22.96 ? 511  ALA A CB  1 
ATOM   4044 N N   . ALA A 1 512 ? 6.859   3.934   28.169 1.00 22.79 ? 512  ALA A N   1 
ATOM   4045 C CA  . ALA A 1 512 ? 5.757   4.746   27.658 1.00 23.28 ? 512  ALA A CA  1 
ATOM   4046 C C   . ALA A 1 512 ? 5.861   6.207   28.143 1.00 23.07 ? 512  ALA A C   1 
ATOM   4047 O O   . ALA A 1 512 ? 5.521   7.110   27.398 1.00 23.03 ? 512  ALA A O   1 
ATOM   4048 C CB  . ALA A 1 512 ? 4.406   4.118   28.054 1.00 22.79 ? 512  ALA A CB  1 
ATOM   4049 N N   . LYS A 1 513 ? 6.366   6.430   29.358 1.00 23.88 ? 513  LYS A N   1 
ATOM   4050 C CA  . LYS A 1 513 ? 6.626   7.806   29.865 1.00 26.02 ? 513  LYS A CA  1 
ATOM   4051 C C   . LYS A 1 513 ? 7.442   8.663   28.899 1.00 26.00 ? 513  LYS A C   1 
ATOM   4052 O O   . LYS A 1 513 ? 7.239   9.870   28.799 1.00 26.25 ? 513  LYS A O   1 
ATOM   4053 C CB  . LYS A 1 513 ? 7.341   7.789   31.226 1.00 25.96 ? 513  LYS A CB  1 
ATOM   4054 C CG  . LYS A 1 513 ? 6.474   7.265   32.357 1.00 27.70 ? 513  LYS A CG  1 
ATOM   4055 C CD  . LYS A 1 513 ? 7.189   7.281   33.679 1.00 29.08 ? 513  LYS A CD  1 
ATOM   4056 C CE  . LYS A 1 513 ? 6.452   6.375   34.649 1.00 32.80 ? 513  LYS A CE  1 
ATOM   4057 N NZ  . LYS A 1 513 ? 7.082   6.334   36.011 1.00 33.19 ? 513  LYS A NZ  1 
ATOM   4058 N N   . THR A 1 514 ? 8.376   8.021   28.209 1.00 26.60 ? 514  THR A N   1 
ATOM   4059 C CA  . THR A 1 514 ? 9.304   8.703   27.300 1.00 26.14 ? 514  THR A CA  1 
ATOM   4060 C C   . THR A 1 514 ? 8.770   8.627   25.888 1.00 25.72 ? 514  THR A C   1 
ATOM   4061 O O   . THR A 1 514 ? 8.817   9.599   25.156 1.00 25.36 ? 514  THR A O   1 
ATOM   4062 C CB  . THR A 1 514 ? 10.719  8.064   27.362 1.00 26.57 ? 514  THR A CB  1 
ATOM   4063 O OG1 . THR A 1 514 ? 11.288  8.295   28.658 1.00 27.19 ? 514  THR A OG1 1 
ATOM   4064 C CG2 . THR A 1 514 ? 11.651  8.653   26.293 1.00 25.91 ? 514  THR A CG2 1 
ATOM   4065 N N   . VAL A 1 515 ? 8.235   7.469   25.517 1.00 25.04 ? 515  VAL A N   1 
ATOM   4066 C CA  . VAL A 1 515 ? 7.867   7.215   24.135 1.00 25.31 ? 515  VAL A CA  1 
ATOM   4067 C C   . VAL A 1 515 ? 6.547   7.905   23.766 1.00 25.08 ? 515  VAL A C   1 
ATOM   4068 O O   . VAL A 1 515 ? 6.373   8.371   22.631 1.00 25.27 ? 515  VAL A O   1 
ATOM   4069 C CB  . VAL A 1 515 ? 7.810   5.709   23.877 1.00 25.04 ? 515  VAL A CB  1 
ATOM   4070 C CG1 . VAL A 1 515 ? 7.280   5.405   22.493 1.00 25.87 ? 515  VAL A CG1 1 
ATOM   4071 C CG2 . VAL A 1 515 ? 9.210   5.115   24.059 1.00 25.69 ? 515  VAL A CG2 1 
ATOM   4072 N N   . PHE A 1 516 ? 5.652   7.987   24.747 1.00 24.86 ? 516  PHE A N   1 
ATOM   4073 C CA  . PHE A 1 516 ? 4.339   8.623   24.609 1.00 25.12 ? 516  PHE A CA  1 
ATOM   4074 C C   . PHE A 1 516 ? 4.107   9.639   25.735 1.00 25.93 ? 516  PHE A C   1 
ATOM   4075 O O   . PHE A 1 516 ? 3.257   9.402   26.616 1.00 26.23 ? 516  PHE A O   1 
ATOM   4076 C CB  . PHE A 1 516 ? 3.236   7.551   24.692 1.00 24.54 ? 516  PHE A CB  1 
ATOM   4077 C CG  . PHE A 1 516 ? 3.443   6.401   23.764 1.00 24.11 ? 516  PHE A CG  1 
ATOM   4078 C CD1 . PHE A 1 516 ? 3.346   6.572   22.395 1.00 24.74 ? 516  PHE A CD1 1 
ATOM   4079 C CD2 . PHE A 1 516 ? 3.739   5.137   24.259 1.00 22.38 ? 516  PHE A CD2 1 
ATOM   4080 C CE1 . PHE A 1 516 ? 3.544   5.492   21.529 1.00 24.16 ? 516  PHE A CE1 1 
ATOM   4081 C CE2 . PHE A 1 516 ? 3.924   4.069   23.402 1.00 24.28 ? 516  PHE A CE2 1 
ATOM   4082 C CZ  . PHE A 1 516 ? 3.807   4.245   22.038 1.00 22.25 ? 516  PHE A CZ  1 
ATOM   4083 N N   . PRO A 1 517 ? 4.849   10.772  25.728 1.00 26.33 ? 517  PRO A N   1 
ATOM   4084 C CA  . PRO A 1 517 ? 4.831   11.641  26.912 1.00 26.67 ? 517  PRO A CA  1 
ATOM   4085 C C   . PRO A 1 517 ? 3.437   12.133  27.324 1.00 26.18 ? 517  PRO A C   1 
ATOM   4086 O O   . PRO A 1 517 ? 2.674   12.624  26.493 1.00 26.23 ? 517  PRO A O   1 
ATOM   4087 C CB  . PRO A 1 517 ? 5.733   12.822  26.501 1.00 26.68 ? 517  PRO A CB  1 
ATOM   4088 C CG  . PRO A 1 517 ? 6.654   12.241  25.464 1.00 27.20 ? 517  PRO A CG  1 
ATOM   4089 C CD  . PRO A 1 517 ? 5.744   11.306  24.680 1.00 26.80 ? 517  PRO A CD  1 
ATOM   4090 N N   . ASN A 1 518 ? 3.133   11.961  28.607 1.00 26.52 ? 518  ASN A N   1 
ATOM   4091 C CA  . ASN A 1 518 ? 1.812   12.237  29.199 1.00 26.45 ? 518  ASN A CA  1 
ATOM   4092 C C   . ASN A 1 518 ? 0.602   11.507  28.615 1.00 25.33 ? 518  ASN A C   1 
ATOM   4093 O O   . ASN A 1 518 ? -0.522  11.911  28.906 1.00 25.57 ? 518  ASN A O   1 
ATOM   4094 C CB  . ASN A 1 518 ? 1.513   13.748  29.200 1.00 27.44 ? 518  ASN A CB  1 
ATOM   4095 C CG  . ASN A 1 518 ? 2.580   14.558  29.898 1.00 30.88 ? 518  ASN A CG  1 
ATOM   4096 O OD1 . ASN A 1 518 ? 3.079   14.173  30.979 1.00 34.73 ? 518  ASN A OD1 1 
ATOM   4097 N ND2 . ASN A 1 518 ? 2.942   15.702  29.289 1.00 32.68 ? 518  ASN A ND2 1 
ATOM   4098 N N   . LYS A 1 519 ? 0.820   10.471  27.794 1.00 23.83 ? 519  LYS A N   1 
ATOM   4099 C CA  . LYS A 1 519 ? -0.276  9.610   27.306 1.00 22.08 ? 519  LYS A CA  1 
ATOM   4100 C C   . LYS A 1 519 ? -0.273  8.270   28.040 1.00 20.77 ? 519  LYS A C   1 
ATOM   4101 O O   . LYS A 1 519 ? 0.778   7.792   28.526 1.00 19.65 ? 519  LYS A O   1 
ATOM   4102 C CB  . LYS A 1 519 ? -0.240  9.372   25.772 1.00 22.66 ? 519  LYS A CB  1 
ATOM   4103 C CG  . LYS A 1 519 ? -0.157  10.613  24.854 1.00 23.93 ? 519  LYS A CG  1 
ATOM   4104 C CD  . LYS A 1 519 ? -1.370  11.535  24.976 1.00 28.52 ? 519  LYS A CD  1 
ATOM   4105 C CE  . LYS A 1 519 ? -1.239  12.768  24.079 1.00 27.24 ? 519  LYS A CE  1 
ATOM   4106 N NZ  . LYS A 1 519 ? -1.607  13.992  24.856 1.00 31.48 ? 519  LYS A NZ  1 
ATOM   4107 N N   . ARG A 1 520 ? -1.465  7.679   28.129 1.00 18.30 ? 520  ARG A N   1 
ATOM   4108 C CA  . ARG A 1 520 ? -1.680  6.357   28.719 1.00 17.14 ? 520  ARG A CA  1 
ATOM   4109 C C   . ARG A 1 520 ? -1.138  5.259   27.823 1.00 17.57 ? 520  ARG A C   1 
ATOM   4110 O O   . ARG A 1 520 ? -0.606  4.256   28.320 1.00 16.48 ? 520  ARG A O   1 
ATOM   4111 C CB  . ARG A 1 520 ? -3.183  6.093   28.897 1.00 17.47 ? 520  ARG A CB  1 
ATOM   4112 C CG  . ARG A 1 520 ? -3.847  7.071   29.847 1.00 13.91 ? 520  ARG A CG  1 
ATOM   4113 C CD  . ARG A 1 520 ? -5.360  6.989   29.696 1.00 12.62 ? 520  ARG A CD  1 
ATOM   4114 N NE  . ARG A 1 520 ? -5.912  8.251   30.161 1.00 10.82 ? 520  ARG A NE  1 
ATOM   4115 C CZ  . ARG A 1 520 ? -7.195  8.570   30.146 1.00 12.06 ? 520  ARG A CZ  1 
ATOM   4116 N NH1 . ARG A 1 520 ? -8.106  7.687   29.734 1.00 8.58  ? 520  ARG A NH1 1 
ATOM   4117 N NH2 . ARG A 1 520 ? -7.537  9.783   30.549 1.00 11.71 ? 520  ARG A NH2 1 
ATOM   4118 N N   . SER A 1 521 ? -1.326  5.441   26.510 1.00 17.19 ? 521  SER A N   1 
ATOM   4119 C CA  . SER A 1 521 ? -1.006  4.411   25.510 1.00 17.55 ? 521  SER A CA  1 
ATOM   4120 C C   . SER A 1 521 ? -1.819  3.133   25.820 1.00 17.83 ? 521  SER A C   1 
ATOM   4121 O O   . SER A 1 521 ? -2.970  3.228   26.255 1.00 17.84 ? 521  SER A O   1 
ATOM   4122 C CB  . SER A 1 521 ? 0.531   4.177   25.474 1.00 17.68 ? 521  SER A CB  1 
ATOM   4123 O OG  . SER A 1 521 ? 0.940   3.224   24.491 1.00 17.27 ? 521  SER A OG  1 
ATOM   4124 N N   . PHE A 1 522 ? -1.223  1.959   25.619 1.00 16.90 ? 522  PHE A N   1 
ATOM   4125 C CA  . PHE A 1 522 ? -1.897  0.677   25.825 1.00 17.35 ? 522  PHE A CA  1 
ATOM   4126 C C   . PHE A 1 522 ? -0.816  -0.385  25.922 1.00 17.23 ? 522  PHE A C   1 
ATOM   4127 O O   . PHE A 1 522 ? 0.082   -0.410  25.089 1.00 17.13 ? 522  PHE A O   1 
ATOM   4128 C CB  . PHE A 1 522 ? -2.823  0.361   24.640 1.00 15.86 ? 522  PHE A CB  1 
ATOM   4129 C CG  . PHE A 1 522 ? -3.383  -1.046  24.638 1.00 17.01 ? 522  PHE A CG  1 
ATOM   4130 C CD1 . PHE A 1 522 ? -4.437  -1.395  25.482 1.00 16.95 ? 522  PHE A CD1 1 
ATOM   4131 C CD2 . PHE A 1 522 ? -2.890  -2.009  23.751 1.00 15.01 ? 522  PHE A CD2 1 
ATOM   4132 C CE1 . PHE A 1 522 ? -4.972  -2.698  25.471 1.00 18.24 ? 522  PHE A CE1 1 
ATOM   4133 C CE2 . PHE A 1 522 ? -3.418  -3.308  23.741 1.00 17.13 ? 522  PHE A CE2 1 
ATOM   4134 C CZ  . PHE A 1 522 ? -4.471  -3.641  24.600 1.00 17.05 ? 522  PHE A CZ  1 
ATOM   4135 N N   . ILE A 1 523 ? -0.896  -1.233  26.951 1.00 17.38 ? 523  ILE A N   1 
ATOM   4136 C CA  . ILE A 1 523 ? 0.003   -2.380  27.101 1.00 16.43 ? 523  ILE A CA  1 
ATOM   4137 C C   . ILE A 1 523 ? -0.849  -3.597  27.326 1.00 16.30 ? 523  ILE A C   1 
ATOM   4138 O O   . ILE A 1 523 ? -1.660  -3.586  28.219 1.00 16.93 ? 523  ILE A O   1 
ATOM   4139 C CB  . ILE A 1 523 ? 0.921   -2.233  28.299 1.00 16.01 ? 523  ILE A CB  1 
ATOM   4140 C CG1 . ILE A 1 523 ? 1.883   -1.044  28.102 1.00 16.64 ? 523  ILE A CG1 1 
ATOM   4141 C CG2 . ILE A 1 523 ? 1.700   -3.535  28.509 1.00 15.30 ? 523  ILE A CG2 1 
ATOM   4142 C CD1 . ILE A 1 523 ? 2.671   -0.712  29.337 1.00 15.40 ? 523  ILE A CD1 1 
ATOM   4143 N N   . LEU A 1 524 ? -0.678  -4.617  26.485 1.00 16.28 ? 524  LEU A N   1 
ATOM   4144 C CA  . LEU A 1 524 ? -1.296  -5.928  26.630 1.00 15.77 ? 524  LEU A CA  1 
ATOM   4145 C C   . LEU A 1 524 ? -0.236  -6.946  27.030 1.00 16.37 ? 524  LEU A C   1 
ATOM   4146 O O   . LEU A 1 524 ? 0.771   -7.095  26.323 1.00 16.88 ? 524  LEU A O   1 
ATOM   4147 C CB  . LEU A 1 524 ? -1.936  -6.345  25.315 1.00 14.86 ? 524  LEU A CB  1 
ATOM   4148 C CG  . LEU A 1 524 ? -2.729  -7.655  25.295 1.00 16.49 ? 524  LEU A CG  1 
ATOM   4149 C CD1 . LEU A 1 524 ? -4.053  -7.520  26.098 1.00 13.08 ? 524  LEU A CD1 1 
ATOM   4150 C CD2 . LEU A 1 524 ? -2.996  -8.049  23.858 1.00 14.94 ? 524  LEU A CD2 1 
ATOM   4151 N N   . THR A 1 525 ? -0.450  -7.628  28.160 1.00 16.43 ? 525  THR A N   1 
ATOM   4152 C CA  . THR A 1 525 ? 0.507   -8.623  28.717 1.00 16.57 ? 525  THR A CA  1 
ATOM   4153 C C   . THR A 1 525 ? -0.077  -10.028 28.801 1.00 17.33 ? 525  THR A C   1 
ATOM   4154 O O   . THR A 1 525 ? -1.296  -10.225 29.045 1.00 17.19 ? 525  THR A O   1 
ATOM   4155 C CB  . THR A 1 525 ? 1.103   -8.192  30.083 1.00 17.02 ? 525  THR A CB  1 
ATOM   4156 O OG1 . THR A 1 525 ? 2.238   -9.018  30.410 1.00 16.62 ? 525  THR A OG1 1 
ATOM   4157 C CG2 . THR A 1 525 ? 0.043   -8.253  31.204 1.00 16.35 ? 525  THR A CG2 1 
ATOM   4158 N N   . ARG A 1 526 ? 0.775   -11.015 28.531 1.00 17.22 ? 526  ARG A N   1 
ATOM   4159 C CA  . ARG A 1 526 ? 0.361   -12.405 28.695 1.00 16.53 ? 526  ARG A CA  1 
ATOM   4160 C C   . ARG A 1 526 ? 0.473   -12.800 30.162 1.00 16.42 ? 526  ARG A C   1 
ATOM   4161 O O   . ARG A 1 526 ? -0.528  -13.181 30.801 1.00 16.36 ? 526  ARG A O   1 
ATOM   4162 C CB  . ARG A 1 526 ? 1.181   -13.373 27.813 1.00 15.76 ? 526  ARG A CB  1 
ATOM   4163 C CG  . ARG A 1 526 ? 0.487   -14.709 27.735 1.00 15.70 ? 526  ARG A CG  1 
ATOM   4164 C CD  . ARG A 1 526 ? 0.974   -15.565 26.663 1.00 15.91 ? 526  ARG A CD  1 
ATOM   4165 N NE  . ARG A 1 526 ? 2.226   -16.187 27.055 1.00 20.41 ? 526  ARG A NE  1 
ATOM   4166 C CZ  . ARG A 1 526 ? 2.852   -17.100 26.332 1.00 21.56 ? 526  ARG A CZ  1 
ATOM   4167 N NH1 . ARG A 1 526 ? 2.344   -17.486 25.166 1.00 23.45 ? 526  ARG A NH1 1 
ATOM   4168 N NH2 . ARG A 1 526 ? 3.978   -17.606 26.770 1.00 20.71 ? 526  ARG A NH2 1 
ATOM   4169 N N   . SER A 1 527 ? 1.694   -12.708 30.685 1.00 14.99 ? 527  SER A N   1 
ATOM   4170 C CA  . SER A 1 527 ? 1.971   -13.101 32.065 1.00 16.01 ? 527  SER A CA  1 
ATOM   4171 C C   . SER A 1 527 ? 1.640   -11.966 33.045 1.00 15.73 ? 527  SER A C   1 
ATOM   4172 O O   . SER A 1 527 ? 1.931   -10.789 32.765 1.00 17.67 ? 527  SER A O   1 
ATOM   4173 C CB  . SER A 1 527 ? 3.436   -13.551 32.182 1.00 16.49 ? 527  SER A CB  1 
ATOM   4174 O OG  . SER A 1 527 ? 3.771   -13.942 33.504 1.00 19.11 ? 527  SER A OG  1 
ATOM   4175 N N   . THR A 1 528 ? 1.029   -12.299 34.181 1.00 14.56 ? 528  THR A N   1 
ATOM   4176 C CA  . THR A 1 528 ? 0.615   -11.280 35.157 1.00 13.75 ? 528  THR A CA  1 
ATOM   4177 C C   . THR A 1 528 ? 0.901   -11.786 36.545 1.00 13.06 ? 528  THR A C   1 
ATOM   4178 O O   . THR A 1 528 ? 1.074   -12.970 36.767 1.00 13.50 ? 528  THR A O   1 
ATOM   4179 C CB  . THR A 1 528 ? -0.926  -11.006 35.130 1.00 14.40 ? 528  THR A CB  1 
ATOM   4180 O OG1 . THR A 1 528 ? -1.585  -12.199 35.517 1.00 14.04 ? 528  THR A OG1 1 
ATOM   4181 C CG2 . THR A 1 528 ? -1.405  -10.567 33.762 1.00 11.67 ? 528  THR A CG2 1 
ATOM   4182 N N   . PHE A 1 529 ? 0.882   -10.872 37.495 1.00 13.15 ? 529  PHE A N   1 
ATOM   4183 C CA  . PHE A 1 529 ? 0.981   -11.200 38.888 1.00 14.27 ? 529  PHE A CA  1 
ATOM   4184 C C   . PHE A 1 529 ? -0.021  -10.261 39.522 1.00 14.18 ? 529  PHE A C   1 
ATOM   4185 O O   . PHE A 1 529 ? -0.581  -9.419  38.826 1.00 16.64 ? 529  PHE A O   1 
ATOM   4186 C CB  . PHE A 1 529 ? 2.395   -10.915 39.423 1.00 14.02 ? 529  PHE A CB  1 
ATOM   4187 C CG  . PHE A 1 529 ? 2.604   -11.359 40.865 1.00 15.34 ? 529  PHE A CG  1 
ATOM   4188 C CD1 . PHE A 1 529 ? 2.677   -12.701 41.186 1.00 18.07 ? 529  PHE A CD1 1 
ATOM   4189 C CD2 . PHE A 1 529 ? 2.742   -10.434 41.868 1.00 15.88 ? 529  PHE A CD2 1 
ATOM   4190 C CE1 . PHE A 1 529 ? 2.864   -13.123 42.510 1.00 18.28 ? 529  PHE A CE1 1 
ATOM   4191 C CE2 . PHE A 1 529 ? 2.937   -10.828 43.189 1.00 16.69 ? 529  PHE A CE2 1 
ATOM   4192 C CZ  . PHE A 1 529 ? 2.995   -12.179 43.509 1.00 16.63 ? 529  PHE A CZ  1 
ATOM   4193 N N   . ALA A 1 530 ? -0.263  -10.404 40.812 1.00 14.01 ? 530  ALA A N   1 
ATOM   4194 C CA  . ALA A 1 530 ? -1.145  -9.493  41.543 1.00 15.26 ? 530  ALA A CA  1 
ATOM   4195 C C   . ALA A 1 530 ? -0.661  -8.066  41.378 1.00 16.52 ? 530  ALA A C   1 
ATOM   4196 O O   . ALA A 1 530 ? 0.493   -7.712  41.716 1.00 17.34 ? 530  ALA A O   1 
ATOM   4197 C CB  . ALA A 1 530 ? -1.219  -9.864  42.991 1.00 14.78 ? 530  ALA A CB  1 
ATOM   4198 N N   . GLY A 1 531 ? -1.525  -7.262  40.769 1.00 16.57 ? 531  GLY A N   1 
ATOM   4199 C CA  . GLY A 1 531 ? -1.225  -5.871  40.563 1.00 15.06 ? 531  GLY A CA  1 
ATOM   4200 C C   . GLY A 1 531 ? -0.886  -5.435  39.169 1.00 14.82 ? 531  GLY A C   1 
ATOM   4201 O O   . GLY A 1 531 ? -0.735  -4.249  38.950 1.00 15.97 ? 531  GLY A O   1 
ATOM   4202 N N   . SER A 1 532 ? -0.749  -6.382  38.233 1.00 14.48 ? 532  SER A N   1 
ATOM   4203 C CA  . SER A 1 532 ? -0.397  -6.093  36.836 1.00 13.83 ? 532  SER A CA  1 
ATOM   4204 C C   . SER A 1 532 ? -1.374  -5.178  36.135 1.00 14.10 ? 532  SER A C   1 
ATOM   4205 O O   . SER A 1 532 ? -1.020  -4.471  35.171 1.00 12.77 ? 532  SER A O   1 
ATOM   4206 C CB  . SER A 1 532 ? -0.315  -7.388  36.034 1.00 12.55 ? 532  SER A CB  1 
ATOM   4207 O OG  . SER A 1 532 ? 0.815   -8.139  36.395 1.00 15.95 ? 532  SER A OG  1 
ATOM   4208 N N   . GLY A 1 533 ? -2.622  -5.226  36.596 1.00 13.65 ? 533  GLY A N   1 
ATOM   4209 C CA  . GLY A 1 533 ? -3.646  -4.315  36.076 1.00 14.51 ? 533  GLY A CA  1 
ATOM   4210 C C   . GLY A 1 533 ? -3.373  -2.839  36.220 1.00 14.29 ? 533  GLY A C   1 
ATOM   4211 O O   . GLY A 1 533 ? -3.869  -2.021  35.440 1.00 14.16 ? 533  GLY A O   1 
ATOM   4212 N N   . LYS A 1 534 ? -2.570  -2.472  37.211 1.00 15.77 ? 534  LYS A N   1 
ATOM   4213 C CA  . LYS A 1 534 ? -2.098  -1.098  37.302 1.00 16.62 ? 534  LYS A CA  1 
ATOM   4214 C C   . LYS A 1 534 ? -1.439  -0.667  35.981 1.00 16.77 ? 534  LYS A C   1 
ATOM   4215 O O   . LYS A 1 534 ? -1.531  0.491   35.578 1.00 17.26 ? 534  LYS A O   1 
ATOM   4216 C CB  . LYS A 1 534 ? -1.145  -0.969  38.475 1.00 17.46 ? 534  LYS A CB  1 
ATOM   4217 C CG  . LYS A 1 534 ? -0.937  0.418   38.972 1.00 19.96 ? 534  LYS A CG  1 
ATOM   4218 C CD  . LYS A 1 534 ? -0.047  0.426   40.217 1.00 22.24 ? 534  LYS A CD  1 
ATOM   4219 C CE  . LYS A 1 534 ? 0.441   1.853   40.451 1.00 26.50 ? 534  LYS A CE  1 
ATOM   4220 N NZ  . LYS A 1 534 ? 0.987   2.026   41.810 1.00 29.14 ? 534  LYS A NZ  1 
ATOM   4221 N N   . PHE A 1 535 ? -0.853  -1.625  35.266 1.00 17.31 ? 535  PHE A N   1 
ATOM   4222 C CA  . PHE A 1 535 ? 0.022   -1.334  34.119 1.00 16.81 ? 535  PHE A CA  1 
ATOM   4223 C C   . PHE A 1 535 ? -0.477  -1.834  32.796 1.00 16.29 ? 535  PHE A C   1 
ATOM   4224 O O   . PHE A 1 535 ? -0.196  -1.233  31.757 1.00 16.90 ? 535  PHE A O   1 
ATOM   4225 C CB  . PHE A 1 535 ? 1.440   -1.887  34.374 1.00 17.51 ? 535  PHE A CB  1 
ATOM   4226 C CG  . PHE A 1 535 ? 1.991   -1.499  35.707 1.00 19.27 ? 535  PHE A CG  1 
ATOM   4227 C CD1 . PHE A 1 535 ? 2.574   -0.253  35.894 1.00 18.34 ? 535  PHE A CD1 1 
ATOM   4228 C CD2 . PHE A 1 535 ? 1.912   -2.370  36.784 1.00 20.18 ? 535  PHE A CD2 1 
ATOM   4229 C CE1 . PHE A 1 535 ? 3.057   0.121   37.135 1.00 18.82 ? 535  PHE A CE1 1 
ATOM   4230 C CE2 . PHE A 1 535 ? 2.397   -1.986  38.038 1.00 19.73 ? 535  PHE A CE2 1 
ATOM   4231 C CZ  . PHE A 1 535 ? 2.974   -0.746  38.200 1.00 17.93 ? 535  PHE A CZ  1 
ATOM   4232 N N   . ALA A 1 536 ? -1.279  -2.893  32.806 1.00 15.91 ? 536  ALA A N   1 
ATOM   4233 C CA  . ALA A 1 536 ? -1.584  -3.563  31.564 1.00 15.17 ? 536  ALA A CA  1 
ATOM   4234 C C   . ALA A 1 536 ? -2.948  -4.239  31.524 1.00 15.33 ? 536  ALA A C   1 
ATOM   4235 O O   . ALA A 1 536 ? -3.486  -4.599  32.548 1.00 14.84 ? 536  ALA A O   1 
ATOM   4236 C CB  . ALA A 1 536 ? -0.509  -4.605  31.313 1.00 15.31 ? 536  ALA A CB  1 
ATOM   4237 N N   . ALA A 1 537 ? -3.436  -4.435  30.308 1.00 14.14 ? 537  ALA A N   1 
ATOM   4238 C CA  . ALA A 1 537 ? -4.520  -5.342  29.979 1.00 14.52 ? 537  ALA A CA  1 
ATOM   4239 C C   . ALA A 1 537 ? -3.991  -6.757  29.795 1.00 14.15 ? 537  ALA A C   1 
ATOM   4240 O O   . ALA A 1 537 ? -2.766  -6.987  29.693 1.00 14.53 ? 537  ALA A O   1 
ATOM   4241 C CB  . ALA A 1 537 ? -5.217  -4.870  28.694 1.00 13.61 ? 537  ALA A CB  1 
ATOM   4242 N N   . HIS A 1 538 ? -4.908  -7.706  29.714 1.00 14.04 ? 538  HIS A N   1 
ATOM   4243 C CA  . HIS A 1 538 ? -4.533  -9.107  29.578 1.00 14.93 ? 538  HIS A CA  1 
ATOM   4244 C C   . HIS A 1 538 ? -5.404  -9.762  28.535 1.00 15.36 ? 538  HIS A C   1 
ATOM   4245 O O   . HIS A 1 538 ? -6.584  -9.421  28.390 1.00 15.39 ? 538  HIS A O   1 
ATOM   4246 C CB  . HIS A 1 538 ? -4.648  -9.801  30.960 1.00 14.91 ? 538  HIS A CB  1 
ATOM   4247 C CG  . HIS A 1 538 ? -4.408  -11.278 30.936 1.00 15.99 ? 538  HIS A CG  1 
ATOM   4248 N ND1 . HIS A 1 538 ? -3.176  -11.836 30.632 1.00 13.99 ? 538  HIS A ND1 1 
ATOM   4249 C CD2 . HIS A 1 538 ? -5.240  -12.314 31.209 1.00 13.11 ? 538  HIS A CD2 1 
ATOM   4250 C CE1 . HIS A 1 538 ? -3.268  -13.148 30.695 1.00 13.74 ? 538  HIS A CE1 1 
ATOM   4251 N NE2 . HIS A 1 538 ? -4.505  -13.467 31.049 1.00 18.08 ? 538  HIS A NE2 1 
ATOM   4252 N N   . TRP A 1 539 ? -4.849  -10.710 27.784 1.00 15.20 ? 539  TRP A N   1 
ATOM   4253 C CA  . TRP A 1 539 ? -5.731  -11.595 27.025 1.00 15.34 ? 539  TRP A CA  1 
ATOM   4254 C C   . TRP A 1 539 ? -5.504  -13.041 27.476 1.00 16.14 ? 539  TRP A C   1 
ATOM   4255 O O   . TRP A 1 539 ? -4.408  -13.377 27.950 1.00 16.04 ? 539  TRP A O   1 
ATOM   4256 C CB  . TRP A 1 539 ? -5.582  -11.404 25.507 1.00 14.87 ? 539  TRP A CB  1 
ATOM   4257 C CG  . TRP A 1 539 ? -4.563  -12.306 24.853 1.00 14.73 ? 539  TRP A CG  1 
ATOM   4258 C CD1 . TRP A 1 539 ? -4.821  -13.355 24.027 1.00 13.56 ? 539  TRP A CD1 1 
ATOM   4259 C CD2 . TRP A 1 539 ? -3.128  -12.224 24.971 1.00 14.23 ? 539  TRP A CD2 1 
ATOM   4260 N NE1 . TRP A 1 539 ? -3.625  -13.935 23.612 1.00 13.82 ? 539  TRP A NE1 1 
ATOM   4261 C CE2 . TRP A 1 539 ? -2.580  -13.255 24.178 1.00 14.45 ? 539  TRP A CE2 1 
ATOM   4262 C CE3 . TRP A 1 539 ? -2.261  -11.382 25.667 1.00 14.38 ? 539  TRP A CE3 1 
ATOM   4263 C CZ2 . TRP A 1 539 ? -1.202  -13.475 24.074 1.00 15.84 ? 539  TRP A CZ2 1 
ATOM   4264 C CZ3 . TRP A 1 539 ? -0.888  -11.583 25.544 1.00 15.17 ? 539  TRP A CZ3 1 
ATOM   4265 C CH2 . TRP A 1 539 ? -0.373  -12.634 24.773 1.00 14.44 ? 539  TRP A CH2 1 
ATOM   4266 N N   . LEU A 1 540 ? -6.516  -13.891 27.296 1.00 15.56 ? 540  LEU A N   1 
ATOM   4267 C CA  . LEU A 1 540 ? -6.528  -15.208 27.947 1.00 16.30 ? 540  LEU A CA  1 
ATOM   4268 C C   . LEU A 1 540 ? -5.665  -16.264 27.243 1.00 16.49 ? 540  LEU A C   1 
ATOM   4269 O O   . LEU A 1 540 ? -5.677  -17.433 27.615 1.00 16.86 ? 540  LEU A O   1 
ATOM   4270 C CB  . LEU A 1 540 ? -7.965  -15.705 28.145 1.00 15.53 ? 540  LEU A CB  1 
ATOM   4271 C CG  . LEU A 1 540 ? -8.754  -14.709 28.978 1.00 16.09 ? 540  LEU A CG  1 
ATOM   4272 C CD1 . LEU A 1 540 ? -10.250 -14.949 28.886 1.00 14.24 ? 540  LEU A CD1 1 
ATOM   4273 C CD2 . LEU A 1 540 ? -8.245  -14.776 30.421 1.00 15.45 ? 540  LEU A CD2 1 
ATOM   4274 N N   . GLY A 1 541 ? -4.926  -15.851 26.225 1.00 16.59 ? 541  GLY A N   1 
ATOM   4275 C CA  . GLY A 1 541 ? -3.940  -16.725 25.597 1.00 17.69 ? 541  GLY A CA  1 
ATOM   4276 C C   . GLY A 1 541 ? -4.457  -17.525 24.438 1.00 17.64 ? 541  GLY A C   1 
ATOM   4277 O O   . GLY A 1 541 ? -5.452  -17.151 23.788 1.00 18.21 ? 541  GLY A O   1 
ATOM   4278 N N   . ASP A 1 542 ? -3.790  -18.651 24.197 1.00 17.87 ? 542  ASP A N   1 
ATOM   4279 C CA  . ASP A 1 542 ? -3.988  -19.454 22.994 1.00 17.21 ? 542  ASP A CA  1 
ATOM   4280 C C   . ASP A 1 542 ? -5.129  -20.416 23.133 1.00 17.17 ? 542  ASP A C   1 
ATOM   4281 O O   . ASP A 1 542 ? -4.918  -21.624 23.324 1.00 16.18 ? 542  ASP A O   1 
ATOM   4282 C CB  . ASP A 1 542 ? -2.702  -20.213 22.653 1.00 18.07 ? 542  ASP A CB  1 
ATOM   4283 C CG  . ASP A 1 542 ? -1.641  -19.310 22.108 1.00 18.66 ? 542  ASP A CG  1 
ATOM   4284 O OD1 . ASP A 1 542 ? -1.979  -18.133 21.870 1.00 22.40 ? 542  ASP A OD1 1 
ATOM   4285 O OD2 . ASP A 1 542 ? -0.472  -19.750 21.940 1.00 21.36 ? 542  ASP A OD2 1 
ATOM   4286 N N   . ASN A 1 543 ? -6.350  -19.884 23.030 1.00 16.98 ? 543  ASN A N   1 
ATOM   4287 C CA  . ASN A 1 543 ? -7.522  -20.724 22.992 1.00 16.52 ? 543  ASN A CA  1 
ATOM   4288 C C   . ASN A 1 543 ? -7.673  -21.425 21.629 1.00 17.57 ? 543  ASN A C   1 
ATOM   4289 O O   . ASN A 1 543 ? -6.782  -21.402 20.783 1.00 17.91 ? 543  ASN A O   1 
ATOM   4290 C CB  . ASN A 1 543 ? -8.796  -19.931 23.390 1.00 15.76 ? 543  ASN A CB  1 
ATOM   4291 C CG  . ASN A 1 543 ? -9.148  -18.843 22.395 1.00 16.24 ? 543  ASN A CG  1 
ATOM   4292 O OD1 . ASN A 1 543 ? -8.382  -18.575 21.464 1.00 18.36 ? 543  ASN A OD1 1 
ATOM   4293 N ND2 . ASN A 1 543 ? -10.321 -18.215 22.569 1.00 15.00 ? 543  ASN A ND2 1 
ATOM   4294 N N   . THR A 1 544 ? -8.829  -22.033 21.428 1.00 18.61 ? 544  THR A N   1 
ATOM   4295 C CA  . THR A 1 544 ? -9.081  -22.874 20.297 1.00 20.03 ? 544  THR A CA  1 
ATOM   4296 C C   . THR A 1 544 ? -10.473 -22.523 19.813 1.00 20.01 ? 544  THR A C   1 
ATOM   4297 O O   . THR A 1 544 ? -11.322 -22.075 20.596 1.00 19.59 ? 544  THR A O   1 
ATOM   4298 C CB  . THR A 1 544 ? -8.924  -24.368 20.690 1.00 20.65 ? 544  THR A CB  1 
ATOM   4299 O OG1 . THR A 1 544 ? -7.605  -24.547 21.217 1.00 24.08 ? 544  THR A OG1 1 
ATOM   4300 C CG2 . THR A 1 544 ? -9.065  -25.309 19.473 1.00 21.58 ? 544  THR A CG2 1 
ATOM   4301 N N   . ALA A 1 545 ? -10.685 -22.664 18.507 1.00 19.59 ? 545  ALA A N   1 
ATOM   4302 C CA  . ALA A 1 545 ? -11.970 -22.365 17.917 1.00 19.53 ? 545  ALA A CA  1 
ATOM   4303 C C   . ALA A 1 545 ? -12.949 -23.503 18.191 1.00 19.31 ? 545  ALA A C   1 
ATOM   4304 O O   . ALA A 1 545 ? -13.272 -24.280 17.299 1.00 18.75 ? 545  ALA A O   1 
ATOM   4305 C CB  . ALA A 1 545 ? -11.795 -22.118 16.431 1.00 19.83 ? 545  ALA A CB  1 
ATOM   4306 N N   . THR A 1 546 ? -13.360 -23.642 19.457 1.00 18.80 ? 546  THR A N   1 
ATOM   4307 C CA  . THR A 1 546 ? -14.384 -24.619 19.839 1.00 18.22 ? 546  THR A CA  1 
ATOM   4308 C C   . THR A 1 546 ? -15.470 -23.964 20.693 1.00 17.22 ? 546  THR A C   1 
ATOM   4309 O O   . THR A 1 546 ? -15.266 -22.911 21.279 1.00 14.16 ? 546  THR A O   1 
ATOM   4310 C CB  . THR A 1 546 ? -13.836 -25.840 20.649 1.00 18.90 ? 546  THR A CB  1 
ATOM   4311 O OG1 . THR A 1 546 ? -13.530 -25.441 21.994 1.00 21.40 ? 546  THR A OG1 1 
ATOM   4312 C CG2 . THR A 1 546 ? -12.576 -26.470 20.000 1.00 19.89 ? 546  THR A CG2 1 
ATOM   4313 N N   . TRP A 1 547 ? -16.617 -24.627 20.773 1.00 17.23 ? 547  TRP A N   1 
ATOM   4314 C CA  . TRP A 1 547 ? -17.714 -24.188 21.630 1.00 17.52 ? 547  TRP A CA  1 
ATOM   4315 C C   . TRP A 1 547 ? -17.358 -24.206 23.136 1.00 18.07 ? 547  TRP A C   1 
ATOM   4316 O O   . TRP A 1 547 ? -17.757 -23.309 23.877 1.00 16.55 ? 547  TRP A O   1 
ATOM   4317 C CB  . TRP A 1 547 ? -18.966 -25.005 21.312 1.00 17.99 ? 547  TRP A CB  1 
ATOM   4318 C CG  . TRP A 1 547 ? -19.517 -24.637 19.981 1.00 18.24 ? 547  TRP A CG  1 
ATOM   4319 C CD1 . TRP A 1 547 ? -19.224 -25.224 18.776 1.00 19.47 ? 547  TRP A CD1 1 
ATOM   4320 C CD2 . TRP A 1 547 ? -20.405 -23.562 19.699 1.00 18.16 ? 547  TRP A CD2 1 
ATOM   4321 N NE1 . TRP A 1 547 ? -19.912 -24.591 17.769 1.00 20.39 ? 547  TRP A NE1 1 
ATOM   4322 C CE2 . TRP A 1 547 ? -20.639 -23.564 18.309 1.00 19.62 ? 547  TRP A CE2 1 
ATOM   4323 C CE3 . TRP A 1 547 ? -21.039 -22.597 20.486 1.00 18.36 ? 547  TRP A CE3 1 
ATOM   4324 C CZ2 . TRP A 1 547 ? -21.501 -22.654 17.696 1.00 19.31 ? 547  TRP A CZ2 1 
ATOM   4325 C CZ3 . TRP A 1 547 ? -21.878 -21.675 19.865 1.00 18.32 ? 547  TRP A CZ3 1 
ATOM   4326 C CH2 . TRP A 1 547 ? -22.102 -21.716 18.491 1.00 18.15 ? 547  TRP A CH2 1 
ATOM   4327 N N   . ASP A 1 548 ? -16.584 -25.204 23.563 1.00 19.02 ? 548  ASP A N   1 
ATOM   4328 C CA  . ASP A 1 548 ? -16.025 -25.259 24.928 1.00 19.45 ? 548  ASP A CA  1 
ATOM   4329 C C   . ASP A 1 548 ? -15.257 -23.987 25.265 1.00 19.22 ? 548  ASP A C   1 
ATOM   4330 O O   . ASP A 1 548 ? -15.567 -23.350 26.270 1.00 19.58 ? 548  ASP A O   1 
ATOM   4331 C CB  . ASP A 1 548 ? -15.115 -26.471 25.110 1.00 20.28 ? 548  ASP A CB  1 
ATOM   4332 C CG  . ASP A 1 548 ? -15.872 -27.738 25.444 1.00 23.15 ? 548  ASP A CG  1 
ATOM   4333 O OD1 . ASP A 1 548 ? -16.937 -27.673 26.091 1.00 25.44 ? 548  ASP A OD1 1 
ATOM   4334 O OD2 . ASP A 1 548 ? -15.364 -28.816 25.081 1.00 26.86 ? 548  ASP A OD2 1 
ATOM   4335 N N   . ASP A 1 549 ? -14.277 -23.613 24.431 1.00 18.72 ? 549  ASP A N   1 
ATOM   4336 C CA  . ASP A 1 549 ? -13.532 -22.348 24.617 1.00 18.94 ? 549  ASP A CA  1 
ATOM   4337 C C   . ASP A 1 549 ? -14.396 -21.060 24.658 1.00 18.15 ? 549  ASP A C   1 
ATOM   4338 O O   . ASP A 1 549 ? -14.102 -20.124 25.397 1.00 18.43 ? 549  ASP A O   1 
ATOM   4339 C CB  . ASP A 1 549 ? -12.413 -22.180 23.577 1.00 18.87 ? 549  ASP A CB  1 
ATOM   4340 C CG  . ASP A 1 549 ? -11.308 -23.229 23.701 1.00 21.35 ? 549  ASP A CG  1 
ATOM   4341 O OD1 . ASP A 1 549 ? -10.186 -22.878 24.102 1.00 23.90 ? 549  ASP A OD1 1 
ATOM   4342 O OD2 . ASP A 1 549 ? -11.538 -24.407 23.351 1.00 25.73 ? 549  ASP A OD2 1 
ATOM   4343 N N   . LEU A 1 550 ? -15.439 -20.989 23.845 1.00 17.75 ? 550  LEU A N   1 
ATOM   4344 C CA  . LEU A 1 550 ? -16.364 -19.859 23.920 1.00 16.74 ? 550  LEU A CA  1 
ATOM   4345 C C   . LEU A 1 550 ? -16.977 -19.781 25.321 1.00 16.19 ? 550  LEU A C   1 
ATOM   4346 O O   . LEU A 1 550 ? -16.934 -18.731 25.980 1.00 15.26 ? 550  LEU A O   1 
ATOM   4347 C CB  . LEU A 1 550 ? -17.423 -19.964 22.802 1.00 17.16 ? 550  LEU A CB  1 
ATOM   4348 C CG  . LEU A 1 550 ? -18.676 -19.077 22.882 1.00 17.33 ? 550  LEU A CG  1 
ATOM   4349 C CD1 . LEU A 1 550 ? -18.348 -17.630 22.733 1.00 16.47 ? 550  LEU A CD1 1 
ATOM   4350 C CD2 . LEU A 1 550 ? -19.659 -19.486 21.831 1.00 17.39 ? 550  LEU A CD2 1 
ATOM   4351 N N   . ARG A 1 551 ? -17.533 -20.899 25.790 1.00 16.87 ? 551  ARG A N   1 
ATOM   4352 C CA  . ARG A 1 551 ? -18.065 -20.999 27.158 1.00 16.38 ? 551  ARG A CA  1 
ATOM   4353 C C   . ARG A 1 551 ? -17.041 -20.692 28.281 1.00 16.44 ? 551  ARG A C   1 
ATOM   4354 O O   . ARG A 1 551 ? -17.321 -19.915 29.211 1.00 16.80 ? 551  ARG A O   1 
ATOM   4355 C CB  . ARG A 1 551 ? -18.710 -22.370 27.358 1.00 17.08 ? 551  ARG A CB  1 
ATOM   4356 C CG  . ARG A 1 551 ? -20.011 -22.560 26.546 1.00 18.18 ? 551  ARG A CG  1 
ATOM   4357 C CD  . ARG A 1 551 ? -20.717 -23.837 26.938 1.00 20.65 ? 551  ARG A CD  1 
ATOM   4358 N NE  . ARG A 1 551 ? -20.053 -25.049 26.475 1.00 19.99 ? 551  ARG A NE  1 
ATOM   4359 C CZ  . ARG A 1 551 ? -20.204 -25.598 25.265 1.00 22.75 ? 551  ARG A CZ  1 
ATOM   4360 N NH1 . ARG A 1 551 ? -20.974 -25.018 24.350 1.00 26.01 ? 551  ARG A NH1 1 
ATOM   4361 N NH2 . ARG A 1 551 ? -19.564 -26.721 24.960 1.00 20.18 ? 551  ARG A NH2 1 
ATOM   4362 N N   . TRP A 1 552 ? -15.851 -21.261 28.190 1.00 16.56 ? 552  TRP A N   1 
ATOM   4363 C CA  . TRP A 1 552 ? -14.806 -21.005 29.215 1.00 16.64 ? 552  TRP A CA  1 
ATOM   4364 C C   . TRP A 1 552 ? -14.315 -19.568 29.278 1.00 16.76 ? 552  TRP A C   1 
ATOM   4365 O O   . TRP A 1 552 ? -13.778 -19.155 30.307 1.00 17.45 ? 552  TRP A O   1 
ATOM   4366 C CB  . TRP A 1 552 ? -13.633 -21.969 29.055 1.00 17.25 ? 552  TRP A CB  1 
ATOM   4367 C CG  . TRP A 1 552 ? -14.049 -23.421 29.068 1.00 17.52 ? 552  TRP A CG  1 
ATOM   4368 C CD1 . TRP A 1 552 ? -15.202 -23.954 29.617 1.00 16.92 ? 552  TRP A CD1 1 
ATOM   4369 C CD2 . TRP A 1 552 ? -13.319 -24.526 28.518 1.00 17.08 ? 552  TRP A CD2 1 
ATOM   4370 N NE1 . TRP A 1 552 ? -15.228 -25.308 29.417 1.00 17.47 ? 552  TRP A NE1 1 
ATOM   4371 C CE2 . TRP A 1 552 ? -14.078 -25.683 28.755 1.00 18.62 ? 552  TRP A CE2 1 
ATOM   4372 C CE3 . TRP A 1 552 ? -12.094 -24.643 27.847 1.00 19.09 ? 552  TRP A CE3 1 
ATOM   4373 C CZ2 . TRP A 1 552 ? -13.648 -26.950 28.341 1.00 20.07 ? 552  TRP A CZ2 1 
ATOM   4374 C CZ3 . TRP A 1 552 ? -11.667 -25.897 27.440 1.00 17.77 ? 552  TRP A CZ3 1 
ATOM   4375 C CH2 . TRP A 1 552 ? -12.437 -27.029 27.696 1.00 18.68 ? 552  TRP A CH2 1 
ATOM   4376 N N   . SER A 1 553 ? -14.515 -18.793 28.211 1.00 16.36 ? 553  SER A N   1 
ATOM   4377 C CA  . SER A 1 553 ? -14.090 -17.377 28.192 1.00 17.23 ? 553  SER A CA  1 
ATOM   4378 C C   . SER A 1 553 ? -14.724 -16.555 29.300 1.00 16.93 ? 553  SER A C   1 
ATOM   4379 O O   . SER A 1 553 ? -14.073 -15.694 29.880 1.00 16.61 ? 553  SER A O   1 
ATOM   4380 C CB  . SER A 1 553 ? -14.367 -16.695 26.835 1.00 16.52 ? 553  SER A CB  1 
ATOM   4381 O OG  . SER A 1 553 ? -15.765 -16.613 26.573 1.00 19.34 ? 553  SER A OG  1 
ATOM   4382 N N   . ILE A 1 554 ? -16.000 -16.818 29.592 1.00 16.87 ? 554  ILE A N   1 
ATOM   4383 C CA  . ILE A 1 554 ? -16.712 -15.966 30.534 1.00 15.88 ? 554  ILE A CA  1 
ATOM   4384 C C   . ILE A 1 554 ? -16.164 -15.960 31.978 1.00 15.23 ? 554  ILE A C   1 
ATOM   4385 O O   . ILE A 1 554 ? -15.949 -14.904 32.495 1.00 16.36 ? 554  ILE A O   1 
ATOM   4386 C CB  . ILE A 1 554 ? -18.280 -16.131 30.478 1.00 15.50 ? 554  ILE A CB  1 
ATOM   4387 C CG1 . ILE A 1 554 ? -18.804 -15.781 29.072 1.00 16.34 ? 554  ILE A CG1 1 
ATOM   4388 C CG2 . ILE A 1 554 ? -18.894 -15.229 31.519 1.00 12.64 ? 554  ILE A CG2 1 
ATOM   4389 C CD1 . ILE A 1 554 ? -20.344 -15.916 28.858 1.00 17.22 ? 554  ILE A CD1 1 
ATOM   4390 N N   . PRO A 1 555 ? -15.961 -17.127 32.629 1.00 14.15 ? 555  PRO A N   1 
ATOM   4391 C CA  . PRO A 1 555 ? -15.407 -17.087 33.996 1.00 14.74 ? 555  PRO A CA  1 
ATOM   4392 C C   . PRO A 1 555 ? -13.977 -16.522 34.022 1.00 14.43 ? 555  PRO A C   1 
ATOM   4393 O O   . PRO A 1 555 ? -13.614 -15.850 34.975 1.00 13.98 ? 555  PRO A O   1 
ATOM   4394 C CB  . PRO A 1 555 ? -15.383 -18.565 34.432 1.00 13.60 ? 555  PRO A CB  1 
ATOM   4395 C CG  . PRO A 1 555 ? -16.183 -19.284 33.496 1.00 13.50 ? 555  PRO A CG  1 
ATOM   4396 C CD  . PRO A 1 555 ? -16.264 -18.503 32.213 1.00 15.08 ? 555  PRO A CD  1 
ATOM   4397 N N   . GLY A 1 556 ? -13.209 -16.758 32.961 1.00 14.66 ? 556  GLY A N   1 
ATOM   4398 C CA  . GLY A 1 556 ? -11.838 -16.200 32.843 1.00 13.67 ? 556  GLY A CA  1 
ATOM   4399 C C   . GLY A 1 556 ? -11.831 -14.688 32.826 1.00 14.04 ? 556  GLY A C   1 
ATOM   4400 O O   . GLY A 1 556 ? -11.012 -14.055 33.496 1.00 15.44 ? 556  GLY A O   1 
ATOM   4401 N N   . VAL A 1 557 ? -12.743 -14.104 32.048 1.00 13.99 ? 557  VAL A N   1 
ATOM   4402 C CA  . VAL A 1 557 ? -12.973 -12.662 32.051 1.00 13.15 ? 557  VAL A CA  1 
ATOM   4403 C C   . VAL A 1 557 ? -13.390 -12.117 33.433 1.00 12.91 ? 557  VAL A C   1 
ATOM   4404 O O   . VAL A 1 557 ? -12.806 -11.125 33.907 1.00 11.44 ? 557  VAL A O   1 
ATOM   4405 C CB  . VAL A 1 557 ? -13.985 -12.237 30.908 1.00 14.10 ? 557  VAL A CB  1 
ATOM   4406 C CG1 . VAL A 1 557 ? -14.604 -10.862 31.168 1.00 11.92 ? 557  VAL A CG1 1 
ATOM   4407 C CG2 . VAL A 1 557 ? -13.285 -12.239 29.553 1.00 11.65 ? 557  VAL A CG2 1 
ATOM   4408 N N   . LEU A 1 558 ? -14.422 -12.733 34.050 1.00 13.08 ? 558  LEU A N   1 
ATOM   4409 C CA  . LEU A 1 558 ? -14.900 -12.361 35.399 1.00 12.08 ? 558  LEU A CA  1 
ATOM   4410 C C   . LEU A 1 558 ? -13.788 -12.475 36.457 1.00 12.75 ? 558  LEU A C   1 
ATOM   4411 O O   . LEU A 1 558 ? -13.684 -11.658 37.329 1.00 12.93 ? 558  LEU A O   1 
ATOM   4412 C CB  . LEU A 1 558 ? -16.054 -13.261 35.804 1.00 12.12 ? 558  LEU A CB  1 
ATOM   4413 C CG  . LEU A 1 558 ? -17.302 -13.081 34.917 1.00 10.89 ? 558  LEU A CG  1 
ATOM   4414 C CD1 . LEU A 1 558 ? -18.416 -13.855 35.496 1.00 11.32 ? 558  LEU A CD1 1 
ATOM   4415 C CD2 . LEU A 1 558 ? -17.632 -11.569 34.821 1.00 11.55 ? 558  LEU A CD2 1 
ATOM   4416 N N   . GLU A 1 559 ? -12.992 -13.523 36.389 1.00 12.73 ? 559  GLU A N   1 
ATOM   4417 C CA  . GLU A 1 559 ? -11.918 -13.702 37.354 1.00 13.76 ? 559  GLU A CA  1 
ATOM   4418 C C   . GLU A 1 559 ? -10.878 -12.591 37.228 1.00 12.72 ? 559  GLU A C   1 
ATOM   4419 O O   . GLU A 1 559 ? -10.475 -12.065 38.225 1.00 13.35 ? 559  GLU A O   1 
ATOM   4420 C CB  . GLU A 1 559 ? -11.285 -15.089 37.213 1.00 14.42 ? 559  GLU A CB  1 
ATOM   4421 C CG  . GLU A 1 559 ? -12.209 -16.218 37.698 1.00 15.45 ? 559  GLU A CG  1 
ATOM   4422 C CD  . GLU A 1 559 ? -11.855 -17.557 37.075 1.00 21.00 ? 559  GLU A CD  1 
ATOM   4423 O OE1 . GLU A 1 559 ? -11.003 -17.575 36.151 1.00 22.39 ? 559  GLU A OE1 1 
ATOM   4424 O OE2 . GLU A 1 559 ? -12.401 -18.589 37.526 1.00 18.37 ? 559  GLU A OE2 1 
ATOM   4425 N N   . PHE A 1 560 ? -10.512 -12.172 36.025 1.00 12.18 ? 560  PHE A N   1 
ATOM   4426 C CA  . PHE A 1 560 ? -9.501  -11.102 35.929 1.00 13.33 ? 560  PHE A CA  1 
ATOM   4427 C C   . PHE A 1 560 ? -10.003 -9.739  36.380 1.00 12.95 ? 560  PHE A C   1 
ATOM   4428 O O   . PHE A 1 560 ? -9.195  -8.899  36.752 1.00 11.75 ? 560  PHE A O   1 
ATOM   4429 C CB  . PHE A 1 560 ? -8.850  -11.061 34.551 1.00 13.19 ? 560  PHE A CB  1 
ATOM   4430 C CG  . PHE A 1 560 ? -7.709  -12.009 34.449 1.00 14.01 ? 560  PHE A CG  1 
ATOM   4431 C CD1 . PHE A 1 560 ? -7.929  -13.330 34.139 1.00 15.60 ? 560  PHE A CD1 1 
ATOM   4432 C CD2 . PHE A 1 560 ? -6.405  -11.593 34.790 1.00 15.35 ? 560  PHE A CD2 1 
ATOM   4433 C CE1 . PHE A 1 560 ? -6.862  -14.239 34.112 1.00 18.88 ? 560  PHE A CE1 1 
ATOM   4434 C CE2 . PHE A 1 560 ? -5.349  -12.491 34.776 1.00 15.09 ? 560  PHE A CE2 1 
ATOM   4435 C CZ  . PHE A 1 560 ? -5.565  -13.795 34.424 1.00 14.80 ? 560  PHE A CZ  1 
ATOM   4436 N N   . ASN A 1 561 ? -11.330 -9.534  36.316 1.00 11.88 ? 561  ASN A N   1 
ATOM   4437 C CA  . ASN A 1 561 ? -11.986 -8.329  36.882 1.00 12.69 ? 561  ASN A CA  1 
ATOM   4438 C C   . ASN A 1 561 ? -11.839 -8.310  38.437 1.00 12.96 ? 561  ASN A C   1 
ATOM   4439 O O   . ASN A 1 561 ? -11.541 -7.279  39.029 1.00 15.87 ? 561  ASN A O   1 
ATOM   4440 C CB  . ASN A 1 561 ? -13.471 -8.210  36.362 1.00 11.26 ? 561  ASN A CB  1 
ATOM   4441 C CG  . ASN A 1 561 ? -13.584 -7.411  35.059 1.00 11.79 ? 561  ASN A CG  1 
ATOM   4442 O OD1 . ASN A 1 561 ? -13.916 -6.226  35.073 1.00 10.98 ? 561  ASN A OD1 1 
ATOM   4443 N ND2 . ASN A 1 561 ? -13.296 -8.054  33.929 1.00 12.77 ? 561  ASN A ND2 1 
ATOM   4444 N N   . LEU A 1 562 ? -11.947 -9.460  39.098 1.00 13.61 ? 562  LEU A N   1 
ATOM   4445 C CA  . LEU A 1 562 ? -11.567 -9.568  40.514 1.00 12.94 ? 562  LEU A CA  1 
ATOM   4446 C C   . LEU A 1 562 ? -10.090 -9.275  40.777 1.00 13.62 ? 562  LEU A C   1 
ATOM   4447 O O   . LEU A 1 562 ? -9.756  -8.707  41.793 1.00 14.43 ? 562  LEU A O   1 
ATOM   4448 C CB  . LEU A 1 562 ? -11.838 -10.963 41.030 1.00 13.47 ? 562  LEU A CB  1 
ATOM   4449 C CG  . LEU A 1 562 ? -13.180 -11.665 40.846 1.00 16.46 ? 562  LEU A CG  1 
ATOM   4450 C CD1 . LEU A 1 562 ? -13.034 -13.055 41.473 1.00 14.40 ? 562  LEU A CD1 1 
ATOM   4451 C CD2 . LEU A 1 562 ? -14.303 -10.865 41.522 1.00 14.17 ? 562  LEU A CD2 1 
ATOM   4452 N N   . PHE A 1 563 ? -9.212  -9.673  39.863 1.00 13.18 ? 563  PHE A N   1 
ATOM   4453 C CA  . PHE A 1 563 ? -7.760  -9.487  40.056 1.00 13.29 ? 563  PHE A CA  1 
ATOM   4454 C C   . PHE A 1 563 ? -7.326  -8.060  39.702 1.00 13.80 ? 563  PHE A C   1 
ATOM   4455 O O   . PHE A 1 563 ? -6.138  -7.697  39.790 1.00 13.90 ? 563  PHE A O   1 
ATOM   4456 C CB  . PHE A 1 563 ? -6.989  -10.496 39.187 1.00 13.08 ? 563  PHE A CB  1 
ATOM   4457 C CG  . PHE A 1 563 ? -7.374  -11.939 39.421 1.00 11.77 ? 563  PHE A CG  1 
ATOM   4458 C CD1 . PHE A 1 563 ? -7.777  -12.393 40.685 1.00 12.86 ? 563  PHE A CD1 1 
ATOM   4459 C CD2 . PHE A 1 563 ? -7.302  -12.849 38.377 1.00 11.11 ? 563  PHE A CD2 1 
ATOM   4460 C CE1 . PHE A 1 563 ? -8.105  -13.704 40.883 1.00 11.91 ? 563  PHE A CE1 1 
ATOM   4461 C CE2 . PHE A 1 563 ? -7.597  -14.154 38.554 1.00 13.57 ? 563  PHE A CE2 1 
ATOM   4462 C CZ  . PHE A 1 563 ? -8.025  -14.602 39.822 1.00 13.68 ? 563  PHE A CZ  1 
ATOM   4463 N N   . GLY A 1 564 ? -8.297  -7.243  39.285 1.00 13.12 ? 564  GLY A N   1 
ATOM   4464 C CA  . GLY A 1 564 ? -8.040  -5.857  38.916 1.00 12.47 ? 564  GLY A CA  1 
ATOM   4465 C C   . GLY A 1 564 ? -7.419  -5.645  37.557 1.00 12.64 ? 564  GLY A C   1 
ATOM   4466 O O   . GLY A 1 564 ? -6.710  -4.678  37.353 1.00 13.11 ? 564  GLY A O   1 
ATOM   4467 N N   . ILE A 1 565 ? -7.644  -6.576  36.639 1.00 12.33 ? 565  ILE A N   1 
ATOM   4468 C CA  . ILE A 1 565 ? -7.254  -6.429  35.253 1.00 12.64 ? 565  ILE A CA  1 
ATOM   4469 C C   . ILE A 1 565 ? -8.563  -6.480  34.467 1.00 13.21 ? 565  ILE A C   1 
ATOM   4470 O O   . ILE A 1 565 ? -8.838  -7.473  33.826 1.00 13.40 ? 565  ILE A O   1 
ATOM   4471 C CB  . ILE A 1 565 ? -6.328  -7.608  34.844 1.00 13.20 ? 565  ILE A CB  1 
ATOM   4472 C CG1 . ILE A 1 565 ? -5.173  -7.717  35.845 1.00 12.99 ? 565  ILE A CG1 1 
ATOM   4473 C CG2 . ILE A 1 565 ? -5.843  -7.456  33.418 1.00 13.03 ? 565  ILE A CG2 1 
ATOM   4474 C CD1 . ILE A 1 565 ? -4.206  -8.818  35.564 1.00 18.08 ? 565  ILE A CD1 1 
ATOM   4475 N N   . PRO A 1 566 ? -9.386  -5.410  34.561 1.00 13.28 ? 566  PRO A N   1 
ATOM   4476 C CA  . PRO A 1 566 ? -10.710 -5.489  33.966 1.00 13.79 ? 566  PRO A CA  1 
ATOM   4477 C C   . PRO A 1 566 ? -10.692 -5.532  32.447 1.00 13.93 ? 566  PRO A C   1 
ATOM   4478 O O   . PRO A 1 566 ? -11.665 -6.007  31.847 1.00 13.20 ? 566  PRO A O   1 
ATOM   4479 C CB  . PRO A 1 566 ? -11.399 -4.213  34.471 1.00 12.42 ? 566  PRO A CB  1 
ATOM   4480 C CG  . PRO A 1 566 ? -10.330 -3.257  34.682 1.00 13.02 ? 566  PRO A CG  1 
ATOM   4481 C CD  . PRO A 1 566 ? -9.162  -4.098  35.205 1.00 12.81 ? 566  PRO A CD  1 
ATOM   4482 N N   . MET A 1 567 ? -9.629  -4.996  31.837 1.00 14.28 ? 567  MET A N   1 
ATOM   4483 C CA  . MET A 1 567 ? -9.474  -5.033  30.394 1.00 15.11 ? 567  MET A CA  1 
ATOM   4484 C C   . MET A 1 567 ? -8.876  -6.379  29.974 1.00 14.25 ? 567  MET A C   1 
ATOM   4485 O O   . MET A 1 567 ? -7.626  -6.569  29.902 1.00 13.89 ? 567  MET A O   1 
ATOM   4486 C CB  . MET A 1 567 ? -8.672  -3.827  29.868 1.00 14.85 ? 567  MET A CB  1 
ATOM   4487 C CG  . MET A 1 567 ? -8.627  -3.801  28.332 1.00 17.02 ? 567  MET A CG  1 
ATOM   4488 S SD  . MET A 1 567 ? -8.156  -2.257  27.588 1.00 21.25 ? 567  MET A SD  1 
ATOM   4489 C CE  . MET A 1 567 ? -9.716  -1.386  27.505 1.00 19.12 ? 567  MET A CE  1 
ATOM   4490 N N   . VAL A 1 568 ? -9.780  -7.328  29.739 1.00 12.35 ? 568  VAL A N   1 
ATOM   4491 C CA  . VAL A 1 568 ? -9.434  -8.716  29.530 1.00 13.21 ? 568  VAL A CA  1 
ATOM   4492 C C   . VAL A 1 568 ? -10.448 -9.295  28.573 1.00 13.90 ? 568  VAL A C   1 
ATOM   4493 O O   . VAL A 1 568 ? -11.640 -8.969  28.639 1.00 14.39 ? 568  VAL A O   1 
ATOM   4494 C CB  . VAL A 1 568 ? -9.363  -9.521  30.931 1.00 13.51 ? 568  VAL A CB  1 
ATOM   4495 C CG1 . VAL A 1 568 ? -10.682 -9.467  31.683 1.00 11.60 ? 568  VAL A CG1 1 
ATOM   4496 C CG2 . VAL A 1 568 ? -8.881  -10.995 30.780 1.00 12.00 ? 568  VAL A CG2 1 
ATOM   4497 N N   . GLY A 1 569 ? -9.977  -10.148 27.673 1.00 14.43 ? 569  GLY A N   1 
ATOM   4498 C CA  . GLY A 1 569 ? -10.854 -11.005 26.894 1.00 13.78 ? 569  GLY A CA  1 
ATOM   4499 C C   . GLY A 1 569 ? -10.051 -12.097 26.203 1.00 14.83 ? 569  GLY A C   1 
ATOM   4500 O O   . GLY A 1 569 ? -8.806  -12.119 26.309 1.00 14.64 ? 569  GLY A O   1 
ATOM   4501 N N   . PRO A 1 570 ? -10.741 -13.020 25.524 1.00 14.57 ? 570  PRO A N   1 
ATOM   4502 C CA  . PRO A 1 570 ? -10.030 -14.024 24.755 1.00 15.94 ? 570  PRO A CA  1 
ATOM   4503 C C   . PRO A 1 570 ? -9.710  -13.549 23.316 1.00 16.20 ? 570  PRO A C   1 
ATOM   4504 O O   . PRO A 1 570 ? -9.932  -12.361 22.946 1.00 16.51 ? 570  PRO A O   1 
ATOM   4505 C CB  . PRO A 1 570 ? -11.028 -15.172 24.709 1.00 14.87 ? 570  PRO A CB  1 
ATOM   4506 C CG  . PRO A 1 570 ? -12.402 -14.417 24.545 1.00 14.78 ? 570  PRO A CG  1 
ATOM   4507 C CD  . PRO A 1 570 ? -12.219 -13.197 25.445 1.00 16.12 ? 570  PRO A CD  1 
ATOM   4508 N N   . ASP A 1 571 ? -9.178  -14.473 22.528 1.00 16.83 ? 571  ASP A N   1 
ATOM   4509 C CA  . ASP A 1 571 ? -9.097  -14.323 21.079 1.00 16.96 ? 571  ASP A CA  1 
ATOM   4510 C C   . ASP A 1 571 ? -10.468 -14.737 20.570 1.00 17.08 ? 571  ASP A C   1 
ATOM   4511 O O   . ASP A 1 571 ? -10.827 -15.909 20.636 1.00 17.36 ? 571  ASP A O   1 
ATOM   4512 C CB  . ASP A 1 571 ? -8.015  -15.235 20.515 1.00 16.45 ? 571  ASP A CB  1 
ATOM   4513 C CG  . ASP A 1 571 ? -6.596  -14.746 20.840 1.00 17.93 ? 571  ASP A CG  1 
ATOM   4514 O OD1 . ASP A 1 571 ? -6.438  -13.598 21.282 1.00 18.67 ? 571  ASP A OD1 1 
ATOM   4515 O OD2 . ASP A 1 571 ? -5.630  -15.524 20.686 1.00 18.26 ? 571  ASP A OD2 1 
ATOM   4516 N N   . ILE A 1 572 ? -11.239 -13.751 20.124 1.00 17.39 ? 572  ILE A N   1 
ATOM   4517 C CA  . ILE A 1 572 ? -12.571 -13.952 19.613 1.00 17.82 ? 572  ILE A CA  1 
ATOM   4518 C C   . ILE A 1 572 ? -12.420 -14.807 18.372 1.00 18.43 ? 572  ILE A C   1 
ATOM   4519 O O   . ILE A 1 572 ? -11.515 -14.565 17.546 1.00 17.44 ? 572  ILE A O   1 
ATOM   4520 C CB  . ILE A 1 572 ? -13.289 -12.623 19.240 1.00 18.01 ? 572  ILE A CB  1 
ATOM   4521 C CG1 . ILE A 1 572 ? -13.508 -11.742 20.470 1.00 17.47 ? 572  ILE A CG1 1 
ATOM   4522 C CG2 . ILE A 1 572 ? -14.633 -12.922 18.542 1.00 19.34 ? 572  ILE A CG2 1 
ATOM   4523 C CD1 . ILE A 1 572 ? -14.233 -10.415 20.188 1.00 17.27 ? 572  ILE A CD1 1 
ATOM   4524 N N   . CYS A 1 573 ? -13.295 -15.812 18.280 1.00 18.01 ? 573  CYS A N   1 
ATOM   4525 C CA  . CYS A 1 573 ? -13.319 -16.812 17.210 1.00 18.91 ? 573  CYS A CA  1 
ATOM   4526 C C   . CYS A 1 573 ? -12.302 -17.939 17.401 1.00 18.31 ? 573  CYS A C   1 
ATOM   4527 O O   . CYS A 1 573 ? -12.392 -18.972 16.758 1.00 18.98 ? 573  CYS A O   1 
ATOM   4528 C CB  . CYS A 1 573 ? -13.276 -16.195 15.805 1.00 19.40 ? 573  CYS A CB  1 
ATOM   4529 S SG  . CYS A 1 573 ? -14.727 -15.125 15.551 1.00 21.24 ? 573  CYS A SG  1 
ATOM   4530 N N   . GLY A 1 574 ? -11.395 -17.767 18.343 1.00 17.66 ? 574  GLY A N   1 
ATOM   4531 C CA  . GLY A 1 574 ? -10.519 -18.850 18.711 1.00 17.68 ? 574  GLY A CA  1 
ATOM   4532 C C   . GLY A 1 574 ? -9.237  -18.751 17.941 1.00 17.63 ? 574  GLY A C   1 
ATOM   4533 O O   . GLY A 1 574 ? -9.242  -18.680 16.725 1.00 18.68 ? 574  GLY A O   1 
ATOM   4534 N N   . PHE A 1 575 ? -8.143  -18.718 18.674 1.00 17.50 ? 575  PHE A N   1 
ATOM   4535 C CA  . PHE A 1 575 ? -6.814  -18.681 18.094 1.00 17.63 ? 575  PHE A CA  1 
ATOM   4536 C C   . PHE A 1 575 ? -6.511  -19.903 17.209 1.00 18.35 ? 575  PHE A C   1 
ATOM   4537 O O   . PHE A 1 575 ? -6.375  -19.767 16.008 1.00 18.59 ? 575  PHE A O   1 
ATOM   4538 C CB  . PHE A 1 575 ? -5.827  -18.573 19.234 1.00 17.17 ? 575  PHE A CB  1 
ATOM   4539 C CG  . PHE A 1 575 ? -4.390  -18.502 18.814 1.00 17.13 ? 575  PHE A CG  1 
ATOM   4540 C CD1 . PHE A 1 575 ? -3.871  -17.351 18.234 1.00 15.46 ? 575  PHE A CD1 1 
ATOM   4541 C CD2 . PHE A 1 575 ? -3.546  -19.569 19.067 1.00 16.70 ? 575  PHE A CD2 1 
ATOM   4542 C CE1 . PHE A 1 575 ? -2.532  -17.271 17.900 1.00 18.35 ? 575  PHE A CE1 1 
ATOM   4543 C CE2 . PHE A 1 575 ? -2.203  -19.511 18.710 1.00 16.47 ? 575  PHE A CE2 1 
ATOM   4544 C CZ  . PHE A 1 575 ? -1.689  -18.362 18.140 1.00 16.84 ? 575  PHE A CZ  1 
ATOM   4545 N N   . ALA A 1 576 ? -6.426  -21.091 17.802 1.00 19.15 ? 576  ALA A N   1 
ATOM   4546 C CA  . ALA A 1 576 ? -6.044  -22.285 17.059 1.00 20.20 ? 576  ALA A CA  1 
ATOM   4547 C C   . ALA A 1 576 ? -7.245  -22.845 16.319 1.00 20.76 ? 576  ALA A C   1 
ATOM   4548 O O   . ALA A 1 576 ? -8.366  -22.787 16.827 1.00 20.46 ? 576  ALA A O   1 
ATOM   4549 C CB  . ALA A 1 576 ? -5.464  -23.345 18.001 1.00 19.69 ? 576  ALA A CB  1 
ATOM   4550 N N   . LEU A 1 577 ? -6.987  -23.358 15.114 1.00 21.41 ? 577  LEU A N   1 
ATOM   4551 C CA  . LEU A 1 577 ? -7.972  -24.054 14.296 1.00 22.12 ? 577  LEU A CA  1 
ATOM   4552 C C   . LEU A 1 577 ? -8.749  -23.099 13.400 1.00 22.20 ? 577  LEU A C   1 
ATOM   4553 O O   . LEU A 1 577 ? -8.835  -21.907 13.685 1.00 22.04 ? 577  LEU A O   1 
ATOM   4554 C CB  . LEU A 1 577 ? -8.938  -24.888 15.166 1.00 21.95 ? 577  LEU A CB  1 
ATOM   4555 C CG  . LEU A 1 577 ? -8.570  -26.320 15.530 1.00 23.60 ? 577  LEU A CG  1 
ATOM   4556 C CD1 . LEU A 1 577 ? -7.089  -26.548 15.747 1.00 24.47 ? 577  LEU A CD1 1 
ATOM   4557 C CD2 . LEU A 1 577 ? -9.402  -26.820 16.687 1.00 23.20 ? 577  LEU A CD2 1 
ATOM   4558 N N   . ASP A 1 578 ? -9.309  -23.643 12.318 1.00 21.80 ? 578  ASP A N   1 
ATOM   4559 C CA  . ASP A 1 578 ? -10.213 -22.916 11.448 1.00 22.33 ? 578  ASP A CA  1 
ATOM   4560 C C   . ASP A 1 578 ? -11.521 -22.769 12.228 1.00 21.90 ? 578  ASP A C   1 
ATOM   4561 O O   . ASP A 1 578 ? -11.970 -23.732 12.834 1.00 21.55 ? 578  ASP A O   1 
ATOM   4562 C CB  . ASP A 1 578 ? -10.488 -23.715 10.164 1.00 22.28 ? 578  ASP A CB  1 
ATOM   4563 C CG  . ASP A 1 578 ? -9.242  -23.878 9.275  1.00 24.23 ? 578  ASP A CG  1 
ATOM   4564 O OD1 . ASP A 1 578 ? -8.242  -23.146 9.438  1.00 25.09 ? 578  ASP A OD1 1 
ATOM   4565 O OD2 . ASP A 1 578 ? -9.267  -24.749 8.392  1.00 26.75 ? 578  ASP A OD2 1 
ATOM   4566 N N   . THR A 1 579 ? -12.108 -21.578 12.236 1.00 20.98 ? 579  THR A N   1 
ATOM   4567 C CA  . THR A 1 579 ? -13.308 -21.357 13.042 1.00 22.01 ? 579  THR A CA  1 
ATOM   4568 C C   . THR A 1 579 ? -14.565 -21.580 12.211 1.00 21.55 ? 579  THR A C   1 
ATOM   4569 O O   . THR A 1 579 ? -14.684 -21.023 11.140 1.00 21.35 ? 579  THR A O   1 
ATOM   4570 C CB  . THR A 1 579 ? -13.313 -19.947 13.694 1.00 22.10 ? 579  THR A CB  1 
ATOM   4571 O OG1 . THR A 1 579 ? -14.247 -19.915 14.776 1.00 24.18 ? 579  THR A OG1 1 
ATOM   4572 C CG2 . THR A 1 579 ? -13.657 -18.847 12.682 1.00 21.99 ? 579  THR A CG2 1 
ATOM   4573 N N   . PRO A 1 580 ? -15.500 -22.410 12.698 1.00 22.31 ? 580  PRO A N   1 
ATOM   4574 C CA  . PRO A 1 580 ? -16.776 -22.552 11.967 1.00 21.94 ? 580  PRO A CA  1 
ATOM   4575 C C   . PRO A 1 580 ? -17.518 -21.223 11.916 1.00 21.51 ? 580  PRO A C   1 
ATOM   4576 O O   . PRO A 1 580 ? -17.484 -20.452 12.874 1.00 20.95 ? 580  PRO A O   1 
ATOM   4577 C CB  . PRO A 1 580 ? -17.574 -23.522 12.832 1.00 22.66 ? 580  PRO A CB  1 
ATOM   4578 C CG  . PRO A 1 580 ? -16.540 -24.222 13.677 1.00 22.23 ? 580  PRO A CG  1 
ATOM   4579 C CD  . PRO A 1 580 ? -15.472 -23.230 13.922 1.00 21.87 ? 580  PRO A CD  1 
ATOM   4580 N N   . GLU A 1 581 ? -18.180 -20.936 10.810 1.00 21.00 ? 581  GLU A N   1 
ATOM   4581 C CA  . GLU A 1 581 ? -18.961 -19.707 10.740 1.00 21.24 ? 581  GLU A CA  1 
ATOM   4582 C C   . GLU A 1 581 ? -19.913 -19.490 11.961 1.00 20.52 ? 581  GLU A C   1 
ATOM   4583 O O   . GLU A 1 581 ? -20.036 -18.374 12.457 1.00 19.70 ? 581  GLU A O   1 
ATOM   4584 C CB  . GLU A 1 581 ? -19.712 -19.638 9.416  1.00 20.80 ? 581  GLU A CB  1 
ATOM   4585 C CG  . GLU A 1 581 ? -20.335 -18.285 9.139  1.00 21.88 ? 581  GLU A CG  1 
ATOM   4586 C CD  . GLU A 1 581 ? -21.740 -18.143 9.716  1.00 24.47 ? 581  GLU A CD  1 
ATOM   4587 O OE1 . GLU A 1 581 ? -22.334 -19.126 10.230 1.00 25.60 ? 581  GLU A OE1 1 
ATOM   4588 O OE2 . GLU A 1 581 ? -22.254 -17.019 9.675  1.00 26.36 ? 581  GLU A OE2 1 
ATOM   4589 N N   . GLU A 1 582 ? -20.596 -20.534 12.431 1.00 20.59 ? 582  GLU A N   1 
ATOM   4590 C CA  . GLU A 1 582 ? -21.647 -20.325 13.441 1.00 21.08 ? 582  GLU A CA  1 
ATOM   4591 C C   . GLU A 1 582 ? -21.007 -19.966 14.785 1.00 20.41 ? 582  GLU A C   1 
ATOM   4592 O O   . GLU A 1 582 ? -21.472 -19.058 15.479 1.00 19.36 ? 582  GLU A O   1 
ATOM   4593 C CB  . GLU A 1 582 ? -22.561 -21.545 13.585 1.00 21.15 ? 582  GLU A CB  1 
ATOM   4594 C CG  . GLU A 1 582 ? -23.643 -21.448 14.672 1.00 20.47 ? 582  GLU A CG  1 
ATOM   4595 C CD  . GLU A 1 582 ? -24.186 -22.814 15.073 1.00 23.29 ? 582  GLU A CD  1 
ATOM   4596 O OE1 . GLU A 1 582 ? -23.768 -23.841 14.476 1.00 26.63 ? 582  GLU A OE1 1 
ATOM   4597 O OE2 . GLU A 1 582 ? -25.007 -22.890 16.015 1.00 24.97 ? 582  GLU A OE2 1 
ATOM   4598 N N   . LEU A 1 583 ? -19.918 -20.662 15.106 1.00 19.89 ? 583  LEU A N   1 
ATOM   4599 C CA  . LEU A 1 583 ? -19.141 -20.375 16.294 1.00 19.75 ? 583  LEU A CA  1 
ATOM   4600 C C   . LEU A 1 583 ? -18.629 -18.934 16.256 1.00 19.75 ? 583  LEU A C   1 
ATOM   4601 O O   . LEU A 1 583 ? -18.895 -18.173 17.174 1.00 20.42 ? 583  LEU A O   1 
ATOM   4602 C CB  . LEU A 1 583 ? -17.967 -21.382 16.464 1.00 18.90 ? 583  LEU A CB  1 
ATOM   4603 C CG  . LEU A 1 583 ? -16.988 -21.069 17.608 1.00 18.89 ? 583  LEU A CG  1 
ATOM   4604 C CD1 . LEU A 1 583 ? -17.622 -21.153 18.979 1.00 17.84 ? 583  LEU A CD1 1 
ATOM   4605 C CD2 . LEU A 1 583 ? -15.692 -21.920 17.538 1.00 18.77 ? 583  LEU A CD2 1 
ATOM   4606 N N   . CYS A 1 584 ? -17.946 -18.547 15.176 1.00 20.58 ? 584  CYS A N   1 
ATOM   4607 C CA  . CYS A 1 584 ? -17.366 -17.206 15.066 1.00 19.95 ? 584  CYS A CA  1 
ATOM   4608 C C   . CYS A 1 584 ? -18.448 -16.130 15.123 1.00 19.17 ? 584  CYS A C   1 
ATOM   4609 O O   . CYS A 1 584 ? -18.282 -15.118 15.749 1.00 19.46 ? 584  CYS A O   1 
ATOM   4610 C CB  . CYS A 1 584 ? -16.507 -17.065 13.804 1.00 20.03 ? 584  CYS A CB  1 
ATOM   4611 S SG  . CYS A 1 584 ? -15.461 -15.576 13.678 1.00 22.54 ? 584  CYS A SG  1 
ATOM   4612 N N   . ARG A 1 585 ? -19.584 -16.381 14.506 1.00 19.02 ? 585  ARG A N   1 
ATOM   4613 C CA  . ARG A 1 585 ? -20.702 -15.463 14.626 1.00 17.85 ? 585  ARG A CA  1 
ATOM   4614 C C   . ARG A 1 585 ? -21.180 -15.248 16.071 1.00 17.62 ? 585  ARG A C   1 
ATOM   4615 O O   . ARG A 1 585 ? -21.382 -14.107 16.483 1.00 17.95 ? 585  ARG A O   1 
ATOM   4616 C CB  . ARG A 1 585 ? -21.848 -15.953 13.749 1.00 18.25 ? 585  ARG A CB  1 
ATOM   4617 C CG  . ARG A 1 585 ? -23.107 -15.096 13.845 1.00 17.67 ? 585  ARG A CG  1 
ATOM   4618 C CD  . ARG A 1 585 ? -24.001 -15.292 12.626 1.00 17.03 ? 585  ARG A CD  1 
ATOM   4619 N NE  . ARG A 1 585 ? -24.030 -16.668 12.147 1.00 17.45 ? 585  ARG A NE  1 
ATOM   4620 C CZ  . ARG A 1 585 ? -24.776 -17.644 12.660 1.00 19.11 ? 585  ARG A CZ  1 
ATOM   4621 N NH1 . ARG A 1 585 ? -25.576 -17.416 13.703 1.00 24.92 ? 585  ARG A NH1 1 
ATOM   4622 N NH2 . ARG A 1 585 ? -24.715 -18.856 12.136 1.00 18.37 ? 585  ARG A NH2 1 
ATOM   4623 N N   . ARG A 1 586 ? -21.387 -16.335 16.819 1.00 17.29 ? 586  ARG A N   1 
ATOM   4624 C CA  . ARG A 1 586 ? -21.783 -16.255 18.244 1.00 15.92 ? 586  ARG A CA  1 
ATOM   4625 C C   . ARG A 1 586 ? -20.650 -15.683 19.083 1.00 15.78 ? 586  ARG A C   1 
ATOM   4626 O O   . ARG A 1 586 ? -20.871 -14.916 20.026 1.00 14.61 ? 586  ARG A O   1 
ATOM   4627 C CB  . ARG A 1 586 ? -22.198 -17.629 18.787 1.00 15.78 ? 586  ARG A CB  1 
ATOM   4628 C CG  . ARG A 1 586 ? -23.473 -18.210 18.202 1.00 15.85 ? 586  ARG A CG  1 
ATOM   4629 C CD  . ARG A 1 586 ? -24.593 -17.223 18.161 1.00 16.85 ? 586  ARG A CD  1 
ATOM   4630 N NE  . ARG A 1 586 ? -25.861 -17.914 18.026 1.00 16.55 ? 586  ARG A NE  1 
ATOM   4631 C CZ  . ARG A 1 586 ? -27.040 -17.309 18.010 1.00 16.47 ? 586  ARG A CZ  1 
ATOM   4632 N NH1 . ARG A 1 586 ? -27.093 -16.007 18.112 1.00 13.97 ? 586  ARG A NH1 1 
ATOM   4633 N NH2 . ARG A 1 586 ? -28.167 -18.028 17.895 1.00 18.08 ? 586  ARG A NH2 1 
ATOM   4634 N N   . TRP A 1 587 ? -19.412 -16.051 18.731 1.00 16.19 ? 587  TRP A N   1 
ATOM   4635 C CA  . TRP A 1 587 ? -18.281 -15.504 19.421 1.00 15.20 ? 587  TRP A CA  1 
ATOM   4636 C C   . TRP A 1 587 ? -18.153 -14.017 19.176 1.00 15.36 ? 587  TRP A C   1 
ATOM   4637 O O   . TRP A 1 587 ? -17.874 -13.280 20.099 1.00 16.42 ? 587  TRP A O   1 
ATOM   4638 C CB  . TRP A 1 587 ? -16.969 -16.254 19.070 1.00 15.44 ? 587  TRP A CB  1 
ATOM   4639 C CG  . TRP A 1 587 ? -16.043 -16.356 20.260 1.00 15.37 ? 587  TRP A CG  1 
ATOM   4640 C CD1 . TRP A 1 587 ? -15.897 -15.445 21.302 1.00 15.75 ? 587  TRP A CD1 1 
ATOM   4641 C CD2 . TRP A 1 587 ? -15.142 -17.424 20.538 1.00 15.82 ? 587  TRP A CD2 1 
ATOM   4642 N NE1 . TRP A 1 587 ? -14.950 -15.899 22.201 1.00 14.02 ? 587  TRP A NE1 1 
ATOM   4643 C CE2 . TRP A 1 587 ? -14.468 -17.107 21.750 1.00 15.89 ? 587  TRP A CE2 1 
ATOM   4644 C CE3 . TRP A 1 587 ? -14.849 -18.634 19.890 1.00 13.53 ? 587  TRP A CE3 1 
ATOM   4645 C CZ2 . TRP A 1 587 ? -13.499 -17.957 22.311 1.00 14.78 ? 587  TRP A CZ2 1 
ATOM   4646 C CZ3 . TRP A 1 587 ? -13.866 -19.474 20.448 1.00 15.71 ? 587  TRP A CZ3 1 
ATOM   4647 C CH2 . TRP A 1 587 ? -13.217 -19.126 21.643 1.00 15.37 ? 587  TRP A CH2 1 
ATOM   4648 N N   . MET A 1 588 ? -18.377 -13.541 17.951 1.00 16.09 ? 588  MET A N   1 
ATOM   4649 C CA  . MET A 1 588 ? -18.352 -12.079 17.706 1.00 15.49 ? 588  MET A CA  1 
ATOM   4650 C C   . MET A 1 588 ? -19.505 -11.323 18.392 1.00 15.24 ? 588  MET A C   1 
ATOM   4651 O O   . MET A 1 588 ? -19.342 -10.201 18.854 1.00 13.98 ? 588  MET A O   1 
ATOM   4652 C CB  . MET A 1 588 ? -18.345 -11.764 16.199 1.00 15.89 ? 588  MET A CB  1 
ATOM   4653 C CG  . MET A 1 588 ? -17.016 -11.943 15.498 1.00 16.51 ? 588  MET A CG  1 
ATOM   4654 S SD  . MET A 1 588 ? -15.727 -10.776 16.008 1.00 16.06 ? 588  MET A SD  1 
ATOM   4655 C CE  . MET A 1 588 ? -16.304 -9.127  15.652 1.00 15.86 ? 588  MET A CE  1 
ATOM   4656 N N   . GLN A 1 589 ? -20.684 -11.926 18.443 1.00 14.67 ? 589  GLN A N   1 
ATOM   4657 C CA  . GLN A 1 589 ? -21.806 -11.320 19.200 1.00 15.23 ? 589  GLN A CA  1 
ATOM   4658 C C   . GLN A 1 589 ? -21.510 -11.106 20.677 1.00 15.49 ? 589  GLN A C   1 
ATOM   4659 O O   . GLN A 1 589 ? -21.748 -10.013 21.209 1.00 16.00 ? 589  GLN A O   1 
ATOM   4660 C CB  . GLN A 1 589 ? -23.053 -12.193 19.064 1.00 15.07 ? 589  GLN A CB  1 
ATOM   4661 C CG  . GLN A 1 589 ? -23.578 -12.159 17.653 1.00 15.91 ? 589  GLN A CG  1 
ATOM   4662 C CD  . GLN A 1 589 ? -24.626 -13.227 17.371 1.00 18.20 ? 589  GLN A CD  1 
ATOM   4663 O OE1 . GLN A 1 589 ? -24.957 -14.061 18.225 1.00 15.22 ? 589  GLN A OE1 1 
ATOM   4664 N NE2 . GLN A 1 589 ? -25.155 -13.195 16.173 1.00 19.63 ? 589  GLN A NE2 1 
ATOM   4665 N N   . LEU A 1 590 ? -20.996 -12.152 21.328 1.00 15.75 ? 590  LEU A N   1 
ATOM   4666 C CA  . LEU A 1 590 ? -20.496 -12.086 22.700 1.00 16.35 ? 590  LEU A CA  1 
ATOM   4667 C C   . LEU A 1 590 ? -19.285 -11.163 22.794 1.00 15.68 ? 590  LEU A C   1 
ATOM   4668 O O   . LEU A 1 590 ? -19.197 -10.340 23.706 1.00 16.28 ? 590  LEU A O   1 
ATOM   4669 C CB  . LEU A 1 590 ? -20.109 -13.486 23.233 1.00 15.43 ? 590  LEU A CB  1 
ATOM   4670 C CG  . LEU A 1 590 ? -19.393 -13.531 24.594 1.00 16.35 ? 590  LEU A CG  1 
ATOM   4671 C CD1 . LEU A 1 590 ? -20.164 -12.840 25.741 1.00 12.06 ? 590  LEU A CD1 1 
ATOM   4672 C CD2 . LEU A 1 590 ? -19.018 -14.923 25.017 1.00 17.25 ? 590  LEU A CD2 1 
ATOM   4673 N N   . GLY A 1 591 ? -18.358 -11.324 21.859 1.00 15.75 ? 591  GLY A N   1 
ATOM   4674 C CA  . GLY A 1 591 ? -17.058 -10.611 21.886 1.00 14.77 ? 591  GLY A CA  1 
ATOM   4675 C C   . GLY A 1 591 ? -17.125 -9.096  21.799 1.00 14.61 ? 591  GLY A C   1 
ATOM   4676 O O   . GLY A 1 591 ? -16.176 -8.388  22.209 1.00 13.31 ? 591  GLY A O   1 
ATOM   4677 N N   . ALA A 1 592 ? -18.245 -8.576  21.270 1.00 13.67 ? 592  ALA A N   1 
ATOM   4678 C CA  . ALA A 1 592 ? -18.475 -7.134  21.241 1.00 13.08 ? 592  ALA A CA  1 
ATOM   4679 C C   . ALA A 1 592 ? -18.642 -6.595  22.664 1.00 13.51 ? 592  ALA A C   1 
ATOM   4680 O O   . ALA A 1 592 ? -18.579 -5.386  22.905 1.00 13.23 ? 592  ALA A O   1 
ATOM   4681 C CB  . ALA A 1 592 ? -19.720 -6.800  20.360 1.00 14.02 ? 592  ALA A CB  1 
ATOM   4682 N N   . PHE A 1 593 ? -18.837 -7.498  23.620 1.00 13.38 ? 593  PHE A N   1 
ATOM   4683 C CA  . PHE A 1 593 ? -19.039 -7.110  25.021 1.00 14.14 ? 593  PHE A CA  1 
ATOM   4684 C C   . PHE A 1 593 ? -17.947 -7.540  26.018 1.00 14.34 ? 593  PHE A C   1 
ATOM   4685 O O   . PHE A 1 593 ? -18.088 -7.338  27.219 1.00 14.46 ? 593  PHE A O   1 
ATOM   4686 C CB  . PHE A 1 593 ? -20.462 -7.534  25.444 1.00 14.82 ? 593  PHE A CB  1 
ATOM   4687 C CG  . PHE A 1 593 ? -21.497 -6.881  24.597 1.00 14.41 ? 593  PHE A CG  1 
ATOM   4688 C CD1 . PHE A 1 593 ? -21.890 -5.559  24.861 1.00 16.01 ? 593  PHE A CD1 1 
ATOM   4689 C CD2 . PHE A 1 593 ? -21.979 -7.520  23.463 1.00 14.43 ? 593  PHE A CD2 1 
ATOM   4690 C CE1 . PHE A 1 593 ? -22.795 -4.896  24.038 1.00 12.38 ? 593  PHE A CE1 1 
ATOM   4691 C CE2 . PHE A 1 593 ? -22.899 -6.876  22.630 1.00 14.98 ? 593  PHE A CE2 1 
ATOM   4692 C CZ  . PHE A 1 593 ? -23.296 -5.553  22.918 1.00 15.75 ? 593  PHE A CZ  1 
ATOM   4693 N N   . TYR A 1 594 ? -16.858 -8.138  25.526 1.00 14.38 ? 594  TYR A N   1 
ATOM   4694 C CA  . TYR A 1 594 ? -15.682 -8.375  26.386 1.00 14.52 ? 594  TYR A CA  1 
ATOM   4695 C C   . TYR A 1 594 ? -15.060 -7.020  26.650 1.00 15.27 ? 594  TYR A C   1 
ATOM   4696 O O   . TYR A 1 594 ? -14.989 -6.203  25.738 1.00 17.49 ? 594  TYR A O   1 
ATOM   4697 C CB  . TYR A 1 594 ? -14.643 -9.253  25.688 1.00 12.45 ? 594  TYR A CB  1 
ATOM   4698 C CG  . TYR A 1 594 ? -14.996 -10.712 25.507 1.00 10.95 ? 594  TYR A CG  1 
ATOM   4699 C CD1 . TYR A 1 594 ? -15.469 -11.504 26.561 1.00 11.45 ? 594  TYR A CD1 1 
ATOM   4700 C CD2 . TYR A 1 594 ? -14.778 -11.313 24.290 1.00 9.12  ? 594  TYR A CD2 1 
ATOM   4701 C CE1 . TYR A 1 594 ? -15.720 -12.889 26.361 1.00 7.93  ? 594  TYR A CE1 1 
ATOM   4702 C CE2 . TYR A 1 594 ? -15.025 -12.641 24.081 1.00 8.67  ? 594  TYR A CE2 1 
ATOM   4703 C CZ  . TYR A 1 594 ? -15.496 -13.412 25.096 1.00 8.11  ? 594  TYR A CZ  1 
ATOM   4704 O OH  . TYR A 1 594 ? -15.722 -14.717 24.787 1.00 11.22 ? 594  TYR A OH  1 
ATOM   4705 N N   . PRO A 1 595 ? -14.605 -6.760  27.881 1.00 15.69 ? 595  PRO A N   1 
ATOM   4706 C CA  . PRO A 1 595 ? -14.039 -5.432  28.098 1.00 15.97 ? 595  PRO A CA  1 
ATOM   4707 C C   . PRO A 1 595 ? -12.798 -5.162  27.196 1.00 16.59 ? 595  PRO A C   1 
ATOM   4708 O O   . PRO A 1 595 ? -12.579 -4.029  26.771 1.00 17.57 ? 595  PRO A O   1 
ATOM   4709 C CB  . PRO A 1 595 ? -13.691 -5.424  29.600 1.00 15.57 ? 595  PRO A CB  1 
ATOM   4710 C CG  . PRO A 1 595 ? -14.272 -6.655  30.182 1.00 14.64 ? 595  PRO A CG  1 
ATOM   4711 C CD  . PRO A 1 595 ? -14.532 -7.629  29.077 1.00 15.28 ? 595  PRO A CD  1 
ATOM   4712 N N   . PHE A 1 596 ? -12.021 -6.203  26.894 1.00 16.71 ? 596  PHE A N   1 
ATOM   4713 C CA  . PHE A 1 596 ? -10.986 -6.164  25.844 1.00 16.20 ? 596  PHE A CA  1 
ATOM   4714 C C   . PHE A 1 596 ? -11.468 -7.019  24.699 1.00 15.76 ? 596  PHE A C   1 
ATOM   4715 O O   . PHE A 1 596 ? -11.691 -8.216  24.860 1.00 15.92 ? 596  PHE A O   1 
ATOM   4716 C CB  . PHE A 1 596 ? -9.639  -6.726  26.332 1.00 15.59 ? 596  PHE A CB  1 
ATOM   4717 C CG  . PHE A 1 596 ? -8.613  -6.851  25.248 1.00 15.68 ? 596  PHE A CG  1 
ATOM   4718 C CD1 . PHE A 1 596 ? -8.218  -5.729  24.522 1.00 14.75 ? 596  PHE A CD1 1 
ATOM   4719 C CD2 . PHE A 1 596 ? -8.059  -8.080  24.922 1.00 15.13 ? 596  PHE A CD2 1 
ATOM   4720 C CE1 . PHE A 1 596 ? -7.266  -5.834  23.511 1.00 15.08 ? 596  PHE A CE1 1 
ATOM   4721 C CE2 . PHE A 1 596 ? -7.080  -8.180  23.908 1.00 15.21 ? 596  PHE A CE2 1 
ATOM   4722 C CZ  . PHE A 1 596 ? -6.701  -7.046  23.202 1.00 11.18 ? 596  PHE A CZ  1 
ATOM   4723 N N   . SER A 1 597 ? -11.638 -6.403  23.539 1.00 15.85 ? 597  SER A N   1 
ATOM   4724 C CA  . SER A 1 597 ? -12.352 -7.042  22.437 1.00 16.69 ? 597  SER A CA  1 
ATOM   4725 C C   . SER A 1 597 ? -11.436 -7.170  21.232 1.00 15.70 ? 597  SER A C   1 
ATOM   4726 O O   . SER A 1 597 ? -11.228 -6.220  20.516 1.00 15.64 ? 597  SER A O   1 
ATOM   4727 C CB  . SER A 1 597 ? -13.598 -6.201  22.094 1.00 16.36 ? 597  SER A CB  1 
ATOM   4728 O OG  . SER A 1 597 ? -14.322 -6.757  21.026 1.00 16.73 ? 597  SER A OG  1 
ATOM   4729 N N   . ARG A 1 598 ? -10.880 -8.352  21.022 1.00 16.23 ? 598  ARG A N   1 
ATOM   4730 C CA  . ARG A 1 598 ? -9.934  -8.558  19.936 1.00 15.76 ? 598  ARG A CA  1 
ATOM   4731 C C   . ARG A 1 598 ? -10.200 -9.883  19.233 1.00 15.74 ? 598  ARG A C   1 
ATOM   4732 O O   . ARG A 1 598 ? -10.265 -10.935 19.868 1.00 15.79 ? 598  ARG A O   1 
ATOM   4733 C CB  . ARG A 1 598 ? -8.470  -8.463  20.448 1.00 15.35 ? 598  ARG A CB  1 
ATOM   4734 C CG  . ARG A 1 598 ? -7.452  -8.792  19.367 1.00 14.26 ? 598  ARG A CG  1 
ATOM   4735 C CD  . ARG A 1 598 ? -5.998  -8.622  19.799 1.00 16.27 ? 598  ARG A CD  1 
ATOM   4736 N NE  . ARG A 1 598 ? -5.574  -9.806  20.526 1.00 19.21 ? 598  ARG A NE  1 
ATOM   4737 C CZ  . ARG A 1 598 ? -4.315  -10.170 20.723 1.00 21.00 ? 598  ARG A CZ  1 
ATOM   4738 N NH1 . ARG A 1 598 ? -3.310  -9.433  20.237 1.00 18.73 ? 598  ARG A NH1 1 
ATOM   4739 N NH2 . ARG A 1 598 ? -4.081  -11.286 21.413 1.00 21.37 ? 598  ARG A NH2 1 
ATOM   4740 N N   . ASN A 1 599 ? -10.421 -9.819  17.920 1.00 15.93 ? 599  ASN A N   1 
ATOM   4741 C CA  . ASN A 1 599 ? -10.451 -11.004 17.067 1.00 15.89 ? 599  ASN A CA  1 
ATOM   4742 C C   . ASN A 1 599 ? -8.984  -11.277 16.684 1.00 16.01 ? 599  ASN A C   1 
ATOM   4743 O O   . ASN A 1 599 ? -8.380  -10.483 15.972 1.00 16.26 ? 599  ASN A O   1 
ATOM   4744 C CB  . ASN A 1 599 ? -11.338 -10.745 15.829 1.00 15.35 ? 599  ASN A CB  1 
ATOM   4745 C CG  . ASN A 1 599 ? -11.450 -11.947 14.866 1.00 16.20 ? 599  ASN A CG  1 
ATOM   4746 O OD1 . ASN A 1 599 ? -10.458 -12.575 14.482 1.00 17.85 ? 599  ASN A OD1 1 
ATOM   4747 N ND2 . ASN A 1 599 ? -12.671 -12.206 14.399 1.00 15.60 ? 599  ASN A ND2 1 
ATOM   4748 N N   . HIS A 1 600 ? -8.426  -12.385 17.171 1.00 16.47 ? 600  HIS A N   1 
ATOM   4749 C CA  . HIS A 1 600 ? -7.055  -12.798 16.837 1.00 16.01 ? 600  HIS A CA  1 
ATOM   4750 C C   . HIS A 1 600 ? -7.042  -14.273 16.378 1.00 16.94 ? 600  HIS A C   1 
ATOM   4751 O O   . HIS A 1 600 ? -7.899  -15.048 16.765 1.00 16.96 ? 600  HIS A O   1 
ATOM   4752 C CB  . HIS A 1 600 ? -6.118  -12.513 18.015 1.00 16.40 ? 600  HIS A CB  1 
ATOM   4753 C CG  . HIS A 1 600 ? -4.684  -12.911 17.795 1.00 15.39 ? 600  HIS A CG  1 
ATOM   4754 N ND1 . HIS A 1 600 ? -3.919  -12.418 16.768 1.00 17.63 ? 600  HIS A ND1 1 
ATOM   4755 C CD2 . HIS A 1 600 ? -3.863  -13.709 18.513 1.00 16.64 ? 600  HIS A CD2 1 
ATOM   4756 C CE1 . HIS A 1 600 ? -2.695  -12.920 16.836 1.00 18.00 ? 600  HIS A CE1 1 
ATOM   4757 N NE2 . HIS A 1 600 ? -2.636  -13.715 17.884 1.00 16.18 ? 600  HIS A NE2 1 
ATOM   4758 N N   . ASN A 1 601 ? -6.069  -14.652 15.546 1.00 16.90 ? 601  ASN A N   1 
ATOM   4759 C CA  . ASN A 1 601 ? -6.065  -15.935 14.850 1.00 17.55 ? 601  ASN A CA  1 
ATOM   4760 C C   . ASN A 1 601 ? -4.617  -16.444 14.829 1.00 18.06 ? 601  ASN A C   1 
ATOM   4761 O O   . ASN A 1 601 ? -3.691  -15.653 14.682 1.00 17.36 ? 601  ASN A O   1 
ATOM   4762 C CB  . ASN A 1 601 ? -6.544  -15.737 13.399 1.00 16.78 ? 601  ASN A CB  1 
ATOM   4763 C CG  . ASN A 1 601 ? -6.939  -17.047 12.686 1.00 16.09 ? 601  ASN A CG  1 
ATOM   4764 O OD1 . ASN A 1 601 ? -7.081  -18.096 13.292 1.00 17.50 ? 601  ASN A OD1 1 
ATOM   4765 N ND2 . ASN A 1 601 ? -7.134  -16.961 11.377 1.00 13.87 ? 601  ASN A ND2 1 
ATOM   4766 N N   . GLY A 1 602 ? -4.438  -17.757 14.937 1.00 18.93 ? 602  GLY A N   1 
ATOM   4767 C CA  . GLY A 1 602 ? -3.094  -18.351 14.894 1.00 19.72 ? 602  GLY A CA  1 
ATOM   4768 C C   . GLY A 1 602 ? -2.574  -18.521 13.478 1.00 20.96 ? 602  GLY A C   1 
ATOM   4769 O O   . GLY A 1 602 ? -3.263  -18.213 12.502 1.00 20.69 ? 602  GLY A O   1 
ATOM   4770 N N   . GLN A 1 603 ? -1.351  -19.029 13.378 1.00 21.88 ? 603  GLN A N   1 
ATOM   4771 C CA  . GLN A 1 603 ? -0.625  -19.128 12.125 1.00 23.46 ? 603  GLN A CA  1 
ATOM   4772 C C   . GLN A 1 603 ? -1.238  -20.177 11.208 1.00 24.03 ? 603  GLN A C   1 
ATOM   4773 O O   . GLN A 1 603 ? -1.550  -21.295 11.643 1.00 25.49 ? 603  GLN A O   1 
ATOM   4774 C CB  . GLN A 1 603 ? 0.831   -19.495 12.446 1.00 23.62 ? 603  GLN A CB  1 
ATOM   4775 C CG  . GLN A 1 603 ? 1.817   -19.372 11.302 1.00 25.62 ? 603  GLN A CG  1 
ATOM   4776 C CD  . GLN A 1 603 ? 3.243   -19.811 11.718 1.00 25.67 ? 603  GLN A CD  1 
ATOM   4777 O OE1 . GLN A 1 603 ? 3.422   -20.616 12.638 1.00 28.82 ? 603  GLN A OE1 1 
ATOM   4778 N NE2 . GLN A 1 603 ? 4.244   -19.282 11.038 1.00 31.23 ? 603  GLN A NE2 1 
ATOM   4779 N N   . GLY A 1 604 ? -1.438  -19.809 9.946  1.00 23.65 ? 604  GLY A N   1 
ATOM   4780 C CA  . GLY A 1 604 ? -1.812  -20.775 8.938  1.00 24.47 ? 604  GLY A CA  1 
ATOM   4781 C C   . GLY A 1 604 ? -3.297  -21.086 8.842  1.00 24.94 ? 604  GLY A C   1 
ATOM   4782 O O   . GLY A 1 604 ? -3.722  -21.680 7.856  1.00 25.23 ? 604  GLY A O   1 
ATOM   4783 N N   . TYR A 1 605 ? -4.097  -20.703 9.842  1.00 24.48 ? 605  TYR A N   1 
ATOM   4784 C CA  . TYR A 1 605 ? -5.524  -21.073 9.825  1.00 24.33 ? 605  TYR A CA  1 
ATOM   4785 C C   . TYR A 1 605 ? -6.326  -20.162 8.903  1.00 24.00 ? 605  TYR A C   1 
ATOM   4786 O O   . TYR A 1 605 ? -5.850  -19.092 8.533  1.00 23.39 ? 605  TYR A O   1 
ATOM   4787 C CB  . TYR A 1 605 ? -6.127  -21.145 11.237 1.00 24.63 ? 605  TYR A CB  1 
ATOM   4788 C CG  . TYR A 1 605 ? -5.318  -22.010 12.198 1.00 24.84 ? 605  TYR A CG  1 
ATOM   4789 C CD1 . TYR A 1 605 ? -5.232  -23.397 12.035 1.00 23.28 ? 605  TYR A CD1 1 
ATOM   4790 C CD2 . TYR A 1 605 ? -4.658  -21.436 13.265 1.00 24.32 ? 605  TYR A CD2 1 
ATOM   4791 C CE1 . TYR A 1 605 ? -4.491  -24.180 12.924 1.00 26.86 ? 605  TYR A CE1 1 
ATOM   4792 C CE2 . TYR A 1 605 ? -3.898  -22.194 14.145 1.00 26.64 ? 605  TYR A CE2 1 
ATOM   4793 C CZ  . TYR A 1 605 ? -3.817  -23.558 13.979 1.00 27.04 ? 605  TYR A CZ  1 
ATOM   4794 O OH  . TYR A 1 605 ? -3.077  -24.274 14.891 1.00 26.27 ? 605  TYR A OH  1 
ATOM   4795 N N   . LYS A 1 606 ? -7.528  -20.599 8.511  1.00 23.74 ? 606  LYS A N   1 
ATOM   4796 C CA  . LYS A 1 606 ? -8.346  -19.822 7.576  1.00 24.74 ? 606  LYS A CA  1 
ATOM   4797 C C   . LYS A 1 606 ? -8.618  -18.442 8.195  1.00 23.51 ? 606  LYS A C   1 
ATOM   4798 O O   . LYS A 1 606 ? -8.562  -18.287 9.409  1.00 23.28 ? 606  LYS A O   1 
ATOM   4799 C CB  . LYS A 1 606 ? -9.643  -20.572 7.166  1.00 24.64 ? 606  LYS A CB  1 
ATOM   4800 C CG  . LYS A 1 606 ? -10.872 -20.308 8.010  1.00 28.20 ? 606  LYS A CG  1 
ATOM   4801 C CD  . LYS A 1 606 ? -12.147 -21.042 7.478  1.00 27.91 ? 606  LYS A CD  1 
ATOM   4802 C CE  . LYS A 1 606 ? -13.444 -20.323 7.901  1.00 33.25 ? 606  LYS A CE  1 
ATOM   4803 N NZ  . LYS A 1 606 ? -14.725 -21.044 7.494  1.00 32.68 ? 606  LYS A NZ  1 
ATOM   4804 N N   . ASP A 1 607 ? -8.848  -17.439 7.358  1.00 22.99 ? 607  ASP A N   1 
ATOM   4805 C CA  . ASP A 1 607 ? -9.137  -16.082 7.824  1.00 22.43 ? 607  ASP A CA  1 
ATOM   4806 C C   . ASP A 1 607 ? -10.385 -16.078 8.708  1.00 21.22 ? 607  ASP A C   1 
ATOM   4807 O O   . ASP A 1 607 ? -11.360 -16.808 8.431  1.00 20.20 ? 607  ASP A O   1 
ATOM   4808 C CB  . ASP A 1 607 ? -9.351  -15.139 6.628  1.00 22.86 ? 607  ASP A CB  1 
ATOM   4809 C CG  . ASP A 1 607 ? -8.078  -14.862 5.863  1.00 26.46 ? 607  ASP A CG  1 
ATOM   4810 O OD1 . ASP A 1 607 ? -6.974  -15.102 6.416  1.00 28.88 ? 607  ASP A OD1 1 
ATOM   4811 O OD2 . ASP A 1 607 ? -8.183  -14.405 4.707  1.00 29.62 ? 607  ASP A OD2 1 
ATOM   4812 N N   . GLN A 1 608 ? -10.345 -15.264 9.769  1.00 20.46 ? 608  GLN A N   1 
ATOM   4813 C CA  . GLN A 1 608 ? -11.492 -15.129 10.678 1.00 19.66 ? 608  GLN A CA  1 
ATOM   4814 C C   . GLN A 1 608 ? -11.846 -13.705 11.053 1.00 19.50 ? 608  GLN A C   1 
ATOM   4815 O O   . GLN A 1 608 ? -12.706 -13.498 11.917 1.00 19.97 ? 608  GLN A O   1 
ATOM   4816 C CB  . GLN A 1 608 ? -11.360 -16.030 11.925 1.00 19.88 ? 608  GLN A CB  1 
ATOM   4817 C CG  . GLN A 1 608 ? -10.214 -15.714 12.865 1.00 18.92 ? 608  GLN A CG  1 
ATOM   4818 C CD  . GLN A 1 608 ? -10.033 -16.808 13.907 1.00 17.88 ? 608  GLN A CD  1 
ATOM   4819 O OE1 . GLN A 1 608 ? -10.173 -18.002 13.608 1.00 17.82 ? 608  GLN A OE1 1 
ATOM   4820 N NE2 . GLN A 1 608 ? -9.740  -16.410 15.128 1.00 15.22 ? 608  GLN A NE2 1 
ATOM   4821 N N   . ASP A 1 609 ? -11.229 -12.743 10.362 1.00 18.06 ? 609  ASP A N   1 
ATOM   4822 C CA  . ASP A 1 609 ? -11.593 -11.356 10.464 1.00 18.14 ? 609  ASP A CA  1 
ATOM   4823 C C   . ASP A 1 609 ? -13.030 -11.221 9.964  1.00 18.65 ? 609  ASP A C   1 
ATOM   4824 O O   . ASP A 1 609 ? -13.428 -11.928 9.031  1.00 18.43 ? 609  ASP A O   1 
ATOM   4825 C CB  . ASP A 1 609 ? -10.636 -10.457 9.694  1.00 18.02 ? 609  ASP A CB  1 
ATOM   4826 C CG  . ASP A 1 609 ? -10.521 -10.813 8.233  1.00 19.33 ? 609  ASP A CG  1 
ATOM   4827 O OD1 . ASP A 1 609 ? -9.902  -11.854 7.889  1.00 18.36 ? 609  ASP A OD1 1 
ATOM   4828 O OD2 . ASP A 1 609 ? -11.008 -10.013 7.422  1.00 21.06 ? 609  ASP A OD2 1 
ATOM   4829 N N   . PRO A 1 610 ? -13.824 -10.382 10.627 1.00 18.04 ? 610  PRO A N   1 
ATOM   4830 C CA  . PRO A 1 610 ? -15.254 -10.310 10.294 1.00 19.47 ? 610  PRO A CA  1 
ATOM   4831 C C   . PRO A 1 610 ? -15.592 -10.206 8.786  1.00 19.61 ? 610  PRO A C   1 
ATOM   4832 O O   . PRO A 1 610 ? -16.433 -10.949 8.319  1.00 19.85 ? 610  PRO A O   1 
ATOM   4833 C CB  . PRO A 1 610 ? -15.750 -9.111  11.109 1.00 18.73 ? 610  PRO A CB  1 
ATOM   4834 C CG  . PRO A 1 610 ? -14.771 -9.007  12.255 1.00 18.81 ? 610  PRO A CG  1 
ATOM   4835 C CD  . PRO A 1 610 ? -13.464 -9.535  11.783 1.00 19.47 ? 610  PRO A CD  1 
ATOM   4836 N N   . ALA A 1 611 ? -14.922 -9.332  8.033  1.00 20.64 ? 611  ALA A N   1 
ATOM   4837 C CA  . ALA A 1 611 ? -15.249 -9.127  6.612  1.00 21.53 ? 611  ALA A CA  1 
ATOM   4838 C C   . ALA A 1 611 ? -14.801 -10.266 5.684  1.00 22.42 ? 611  ALA A C   1 
ATOM   4839 O O   . ALA A 1 611 ? -15.108 -10.231 4.491  1.00 22.85 ? 611  ALA A O   1 
ATOM   4840 C CB  . ALA A 1 611 ? -14.688 -7.781  6.109  1.00 20.50 ? 611  ALA A CB  1 
ATOM   4841 N N   . SER A 1 612 ? -14.067 -11.258 6.215  1.00 23.49 ? 612  SER A N   1 
ATOM   4842 C CA  . SER A 1 612 ? -13.599 -12.395 5.395  1.00 24.50 ? 612  SER A CA  1 
ATOM   4843 C C   . SER A 1 612 ? -14.722 -13.401 5.139  1.00 25.13 ? 612  SER A C   1 
ATOM   4844 O O   . SER A 1 612 ? -14.601 -14.259 4.251  1.00 24.77 ? 612  SER A O   1 
ATOM   4845 C CB  . SER A 1 612 ? -12.356 -13.080 5.990  1.00 24.59 ? 612  SER A CB  1 
ATOM   4846 O OG  . SER A 1 612 ? -12.633 -13.710 7.234  1.00 25.77 ? 612  SER A OG  1 
ATOM   4847 N N   . PHE A 1 613 ? -15.814 -13.278 5.909  1.00 24.95 ? 613  PHE A N   1 
ATOM   4848 C CA  . PHE A 1 613 ? -16.966 -14.160 5.775  1.00 24.62 ? 613  PHE A CA  1 
ATOM   4849 C C   . PHE A 1 613 ? -17.947 -13.691 4.710  1.00 25.11 ? 613  PHE A C   1 
ATOM   4850 O O   . PHE A 1 613 ? -18.897 -14.403 4.389  1.00 26.08 ? 613  PHE A O   1 
ATOM   4851 C CB  . PHE A 1 613 ? -17.680 -14.327 7.120  1.00 24.64 ? 613  PHE A CB  1 
ATOM   4852 C CG  . PHE A 1 613 ? -16.881 -15.089 8.138  1.00 23.03 ? 613  PHE A CG  1 
ATOM   4853 C CD1 . PHE A 1 613 ? -17.165 -16.414 8.393  1.00 22.17 ? 613  PHE A CD1 1 
ATOM   4854 C CD2 . PHE A 1 613 ? -15.821 -14.471 8.833  1.00 23.20 ? 613  PHE A CD2 1 
ATOM   4855 C CE1 . PHE A 1 613 ? -16.421 -17.135 9.331  1.00 23.50 ? 613  PHE A CE1 1 
ATOM   4856 C CE2 . PHE A 1 613 ? -15.072 -15.171 9.773  1.00 21.07 ? 613  PHE A CE2 1 
ATOM   4857 C CZ  . PHE A 1 613 ? -15.361 -16.512 10.015 1.00 22.11 ? 613  PHE A CZ  1 
ATOM   4858 N N   . GLY A 1 614 ? -17.722 -12.490 4.176  1.00 25.26 ? 614  GLY A N   1 
ATOM   4859 C CA  . GLY A 1 614 ? -18.475 -11.988 3.047  1.00 24.75 ? 614  GLY A CA  1 
ATOM   4860 C C   . GLY A 1 614 ? -19.039 -10.619 3.325  1.00 24.67 ? 614  GLY A C   1 
ATOM   4861 O O   . GLY A 1 614 ? -19.557 -10.367 4.408  1.00 23.74 ? 614  GLY A O   1 
ATOM   4862 N N   . ALA A 1 615 ? -18.933 -9.746  2.332  1.00 25.26 ? 615  ALA A N   1 
ATOM   4863 C CA  . ALA A 1 615 ? -19.370 -8.370  2.421  1.00 26.35 ? 615  ALA A CA  1 
ATOM   4864 C C   . ALA A 1 615 ? -20.828 -8.294  2.826  1.00 26.86 ? 615  ALA A C   1 
ATOM   4865 O O   . ALA A 1 615 ? -21.251 -7.301  3.406  1.00 28.04 ? 615  ALA A O   1 
ATOM   4866 C CB  . ALA A 1 615 ? -19.186 -7.688  1.081  1.00 27.15 ? 615  ALA A CB  1 
ATOM   4867 N N   . ASP A 1 616 ? -21.579 -9.355  2.536  1.00 27.33 ? 616  ASP A N   1 
ATOM   4868 C CA  . ASP A 1 616 ? -23.011 -9.414  2.838  1.00 27.72 ? 616  ASP A CA  1 
ATOM   4869 C C   . ASP A 1 616 ? -23.399 -10.530 3.803  1.00 26.30 ? 616  ASP A C   1 
ATOM   4870 O O   . ASP A 1 616 ? -24.587 -10.796 3.981  1.00 26.14 ? 616  ASP A O   1 
ATOM   4871 C CB  . ASP A 1 616 ? -23.831 -9.530  1.545  1.00 28.07 ? 616  ASP A CB  1 
ATOM   4872 C CG  . ASP A 1 616 ? -23.854 -8.231  0.753  1.00 32.44 ? 616  ASP A CG  1 
ATOM   4873 O OD1 . ASP A 1 616 ? -23.660 -8.294  -0.487 1.00 36.58 ? 616  ASP A OD1 1 
ATOM   4874 O OD2 . ASP A 1 616 ? -24.056 -7.143  1.364  1.00 35.83 ? 616  ASP A OD2 1 
ATOM   4875 N N   . SER A 1 617 ? -22.409 -11.155 4.444  1.00 24.47 ? 617  SER A N   1 
ATOM   4876 C CA  . SER A 1 617 ? -22.663 -12.320 5.305  1.00 22.83 ? 617  SER A CA  1 
ATOM   4877 C C   . SER A 1 617 ? -23.444 -11.990 6.586  1.00 21.93 ? 617  SER A C   1 
ATOM   4878 O O   . SER A 1 617 ? -23.353 -10.884 7.086  1.00 21.66 ? 617  SER A O   1 
ATOM   4879 C CB  . SER A 1 617 ? -21.344 -12.965 5.695  1.00 22.52 ? 617  SER A CB  1 
ATOM   4880 O OG  . SER A 1 617 ? -20.568 -12.072 6.479  1.00 21.40 ? 617  SER A OG  1 
ATOM   4881 N N   . LEU A 1 618 ? -24.174 -12.968 7.138  1.00 22.60 ? 618  LEU A N   1 
ATOM   4882 C CA  . LEU A 1 618 ? -24.883 -12.776 8.415  1.00 22.23 ? 618  LEU A CA  1 
ATOM   4883 C C   . LEU A 1 618 ? -23.897 -12.436 9.519  1.00 21.79 ? 618  LEU A C   1 
ATOM   4884 O O   . LEU A 1 618 ? -24.206 -11.663 10.421 1.00 21.43 ? 618  LEU A O   1 
ATOM   4885 C CB  . LEU A 1 618 ? -25.713 -14.003 8.823  1.00 21.98 ? 618  LEU A CB  1 
ATOM   4886 C CG  . LEU A 1 618 ? -26.511 -13.838 10.121 1.00 22.67 ? 618  LEU A CG  1 
ATOM   4887 C CD1 . LEU A 1 618 ? -27.533 -12.682 10.021 1.00 23.27 ? 618  LEU A CD1 1 
ATOM   4888 C CD2 . LEU A 1 618 ? -27.220 -15.122 10.471 1.00 24.75 ? 618  LEU A CD2 1 
ATOM   4889 N N   . LEU A 1 619 ? -22.698 -13.003 9.429  1.00 21.50 ? 619  LEU A N   1 
ATOM   4890 C CA  . LEU A 1 619 ? -21.683 -12.777 10.452 1.00 20.56 ? 619  LEU A CA  1 
ATOM   4891 C C   . LEU A 1 619 ? -21.154 -11.359 10.460 1.00 20.46 ? 619  LEU A C   1 
ATOM   4892 O O   . LEU A 1 619 ? -20.983 -10.771 11.521 1.00 19.41 ? 619  LEU A O   1 
ATOM   4893 C CB  . LEU A 1 619 ? -20.532 -13.776 10.321 1.00 20.25 ? 619  LEU A CB  1 
ATOM   4894 C CG  . LEU A 1 619 ? -19.416 -13.663 11.371 1.00 20.62 ? 619  LEU A CG  1 
ATOM   4895 C CD1 . LEU A 1 619 ? -18.730 -14.987 11.554 1.00 17.56 ? 619  LEU A CD1 1 
ATOM   4896 C CD2 . LEU A 1 619 ? -18.380 -12.564 11.033 1.00 20.05 ? 619  LEU A CD2 1 
ATOM   4897 N N   . LEU A 1 620 ? -20.862 -10.808 9.281  1.00 20.98 ? 620  LEU A N   1 
ATOM   4898 C CA  . LEU A 1 620 ? -20.344 -9.446  9.195  1.00 20.61 ? 620  LEU A CA  1 
ATOM   4899 C C   . LEU A 1 620 ? -21.395 -8.458  9.641  1.00 20.97 ? 620  LEU A C   1 
ATOM   4900 O O   . LEU A 1 620 ? -21.109 -7.540  10.416 1.00 21.27 ? 620  LEU A O   1 
ATOM   4901 C CB  . LEU A 1 620 ? -19.904 -9.108  7.759  1.00 20.92 ? 620  LEU A CB  1 
ATOM   4902 C CG  . LEU A 1 620 ? -19.410 -7.675  7.564  1.00 20.86 ? 620  LEU A CG  1 
ATOM   4903 C CD1 . LEU A 1 620 ? -18.145 -7.418  8.392  1.00 20.79 ? 620  LEU A CD1 1 
ATOM   4904 C CD2 . LEU A 1 620 ? -19.187 -7.347  6.083  1.00 21.13 ? 620  LEU A CD2 1 
ATOM   4905 N N   . ASN A 1 621 ? -22.599 -8.637  9.114  1.00 20.75 ? 621  ASN A N   1 
ATOM   4906 C CA  . ASN A 1 621 ? -23.769 -7.842  9.489  1.00 22.14 ? 621  ASN A CA  1 
ATOM   4907 C C   . ASN A 1 621 ? -24.040 -7.839  10.990 1.00 21.02 ? 621  ASN A C   1 
ATOM   4908 O O   . ASN A 1 621 ? -24.141 -6.789  11.586 1.00 21.68 ? 621  ASN A O   1 
ATOM   4909 C CB  . ASN A 1 621 ? -25.010 -8.307  8.701  1.00 22.16 ? 621  ASN A CB  1 
ATOM   4910 C CG  . ASN A 1 621 ? -24.983 -7.853  7.233  1.00 28.59 ? 621  ASN A CG  1 
ATOM   4911 O OD1 . ASN A 1 621 ? -24.060 -7.144  6.781  1.00 31.59 ? 621  ASN A OD1 1 
ATOM   4912 N ND2 . ASN A 1 621 ? -26.014 -8.248  6.479  1.00 33.39 ? 621  ASN A ND2 1 
ATOM   4913 N N   . SER A 1 622 ? -24.130 -9.015  11.598 1.00 21.22 ? 622  SER A N   1 
ATOM   4914 C CA  . SER A 1 622 ? -24.283 -9.144  13.063 1.00 20.20 ? 622  SER A CA  1 
ATOM   4915 C C   . SER A 1 622 ? -23.084 -8.552  13.834 1.00 19.98 ? 622  SER A C   1 
ATOM   4916 O O   . SER A 1 622 ? -23.257 -7.831  14.822 1.00 19.75 ? 622  SER A O   1 
ATOM   4917 C CB  . SER A 1 622 ? -24.449 -10.606 13.417 1.00 20.29 ? 622  SER A CB  1 
ATOM   4918 O OG  . SER A 1 622 ? -24.737 -10.762 14.794 1.00 23.46 ? 622  SER A OG  1 
ATOM   4919 N N   . SER A 1 623 ? -21.868 -8.831  13.370 1.00 18.13 ? 623  SER A N   1 
ATOM   4920 C CA  . SER A 1 623 ? -20.697 -8.269  14.022 1.00 17.84 ? 623  SER A CA  1 
ATOM   4921 C C   . SER A 1 623 ? -20.722 -6.772  14.060 1.00 17.08 ? 623  SER A C   1 
ATOM   4922 O O   . SER A 1 623 ? -20.468 -6.177  15.094 1.00 17.08 ? 623  SER A O   1 
ATOM   4923 C CB  . SER A 1 623 ? -19.426 -8.729  13.323 1.00 17.32 ? 623  SER A CB  1 
ATOM   4924 O OG  . SER A 1 623 ? -19.396 -10.122 13.420 1.00 18.15 ? 623  SER A OG  1 
ATOM   4925 N N   . ARG A 1 624 ? -21.015 -6.167  12.913 1.00 16.91 ? 624  ARG A N   1 
ATOM   4926 C CA  . ARG A 1 624 ? -21.088 -4.739  12.801 1.00 16.29 ? 624  ARG A CA  1 
ATOM   4927 C C   . ARG A 1 624 ? -22.202 -4.211  13.680 1.00 15.51 ? 624  ARG A C   1 
ATOM   4928 O O   . ARG A 1 624 ? -22.003 -3.243  14.371 1.00 14.68 ? 624  ARG A O   1 
ATOM   4929 C CB  . ARG A 1 624 ? -21.284 -4.304  11.321 1.00 16.75 ? 624  ARG A CB  1 
ATOM   4930 C CG  . ARG A 1 624 ? -21.271 -2.796  11.072 1.00 16.13 ? 624  ARG A CG  1 
ATOM   4931 C CD  . ARG A 1 624 ? -21.504 -2.437  9.555  1.00 18.58 ? 624  ARG A CD  1 
ATOM   4932 N NE  . ARG A 1 624 ? -22.543 -3.289  8.990  1.00 22.04 ? 624  ARG A NE  1 
ATOM   4933 C CZ  . ARG A 1 624 ? -22.433 -4.006  7.880  1.00 24.00 ? 624  ARG A CZ  1 
ATOM   4934 N NH1 . ARG A 1 624 ? -21.334 -3.958  7.134  1.00 24.07 ? 624  ARG A NH1 1 
ATOM   4935 N NH2 . ARG A 1 624 ? -23.466 -4.747  7.496  1.00 24.78 ? 624  ARG A NH2 1 
ATOM   4936 N N   . HIS A 1 625 ? -23.369 -4.857  13.650 1.00 15.51 ? 625  HIS A N   1 
ATOM   4937 C CA  . HIS A 1 625 ? -24.499 -4.450  14.504 1.00 15.37 ? 625  HIS A CA  1 
ATOM   4938 C C   . HIS A 1 625 ? -24.139 -4.358  15.996 1.00 14.41 ? 625  HIS A C   1 
ATOM   4939 O O   . HIS A 1 625 ? -24.313 -3.331  16.614 1.00 14.18 ? 625  HIS A O   1 
ATOM   4940 C CB  . HIS A 1 625 ? -25.682 -5.411  14.280 1.00 15.38 ? 625  HIS A CB  1 
ATOM   4941 C CG  . HIS A 1 625 ? -26.934 -5.003  14.996 1.00 18.91 ? 625  HIS A CG  1 
ATOM   4942 N ND1 . HIS A 1 625 ? -27.480 -5.740  16.019 1.00 21.09 ? 625  HIS A ND1 1 
ATOM   4943 C CD2 . HIS A 1 625 ? -27.747 -3.935  14.830 1.00 22.88 ? 625  HIS A CD2 1 
ATOM   4944 C CE1 . HIS A 1 625 ? -28.571 -5.142  16.460 1.00 23.68 ? 625  HIS A CE1 1 
ATOM   4945 N NE2 . HIS A 1 625 ? -28.757 -4.042  15.753 1.00 24.48 ? 625  HIS A NE2 1 
ATOM   4946 N N   . TYR A 1 626 ? -23.604 -5.433  16.565 1.00 14.80 ? 626  TYR A N   1 
ATOM   4947 C CA  . TYR A 1 626 ? -23.316 -5.468  17.989 1.00 14.73 ? 626  TYR A CA  1 
ATOM   4948 C C   . TYR A 1 626 ? -22.072 -4.697  18.359 1.00 14.49 ? 626  TYR A C   1 
ATOM   4949 O O   . TYR A 1 626 ? -21.973 -4.178  19.474 1.00 13.90 ? 626  TYR A O   1 
ATOM   4950 C CB  . TYR A 1 626 ? -23.261 -6.918  18.496 1.00 15.52 ? 626  TYR A CB  1 
ATOM   4951 C CG  . TYR A 1 626 ? -24.650 -7.477  18.577 1.00 15.60 ? 626  TYR A CG  1 
ATOM   4952 C CD1 . TYR A 1 626 ? -25.080 -8.451  17.693 1.00 16.91 ? 626  TYR A CD1 1 
ATOM   4953 C CD2 . TYR A 1 626 ? -25.563 -6.960  19.499 1.00 15.04 ? 626  TYR A CD2 1 
ATOM   4954 C CE1 . TYR A 1 626 ? -26.395 -8.938  17.761 1.00 18.35 ? 626  TYR A CE1 1 
ATOM   4955 C CE2 . TYR A 1 626 ? -26.867 -7.438  19.569 1.00 16.09 ? 626  TYR A CE2 1 
ATOM   4956 C CZ  . TYR A 1 626 ? -27.262 -8.422  18.706 1.00 15.91 ? 626  TYR A CZ  1 
ATOM   4957 O OH  . TYR A 1 626 ? -28.555 -8.882  18.771 1.00 19.17 ? 626  TYR A OH  1 
ATOM   4958 N N   . LEU A 1 627 ? -21.155 -4.565  17.413 1.00 14.31 ? 627  LEU A N   1 
ATOM   4959 C CA  . LEU A 1 627 ? -20.028 -3.666  17.651 1.00 15.34 ? 627  LEU A CA  1 
ATOM   4960 C C   . LEU A 1 627 ? -20.512 -2.233  17.641 1.00 15.93 ? 627  LEU A C   1 
ATOM   4961 O O   . LEU A 1 627 ? -19.952 -1.401  18.342 1.00 16.48 ? 627  LEU A O   1 
ATOM   4962 C CB  . LEU A 1 627 ? -18.915 -3.888  16.637 1.00 14.63 ? 627  LEU A CB  1 
ATOM   4963 C CG  . LEU A 1 627 ? -17.954 -5.041  16.977 1.00 18.74 ? 627  LEU A CG  1 
ATOM   4964 C CD1 . LEU A 1 627 ? -17.077 -5.329  15.784 1.00 19.95 ? 627  LEU A CD1 1 
ATOM   4965 C CD2 . LEU A 1 627 ? -17.079 -4.694  18.197 1.00 19.27 ? 627  LEU A CD2 1 
ATOM   4966 N N   . ASN A 1 628 ? -21.557 -1.927  16.855 1.00 15.24 ? 628  ASN A N   1 
ATOM   4967 C CA  . ASN A 1 628 ? -22.052 -0.550  16.860 1.00 15.67 ? 628  ASN A CA  1 
ATOM   4968 C C   . ASN A 1 628 ? -22.747 -0.248  18.165 1.00 14.38 ? 628  ASN A C   1 
ATOM   4969 O O   . ASN A 1 628 ? -22.714 0.881   18.659 1.00 14.16 ? 628  ASN A O   1 
ATOM   4970 C CB  . ASN A 1 628 ? -22.952 -0.253  15.657 1.00 15.87 ? 628  ASN A CB  1 
ATOM   4971 C CG  . ASN A 1 628 ? -22.179 0.297   14.494 1.00 18.18 ? 628  ASN A CG  1 
ATOM   4972 O OD1 . ASN A 1 628 ? -22.410 -0.076  13.326 1.00 21.93 ? 628  ASN A OD1 1 
ATOM   4973 N ND2 . ASN A 1 628 ? -21.243 1.184   14.795 1.00 18.19 ? 628  ASN A ND2 1 
ATOM   4974 N N   . ILE A 1 629 ? -23.332 -1.288  18.745 1.00 14.35 ? 629  ILE A N   1 
ATOM   4975 C CA  . ILE A 1 629 ? -23.921 -1.203  20.096 1.00 14.30 ? 629  ILE A CA  1 
ATOM   4976 C C   . ILE A 1 629 ? -22.861 -1.042  21.168 1.00 13.78 ? 629  ILE A C   1 
ATOM   4977 O O   . ILE A 1 629 ? -22.992 -0.191  22.020 1.00 14.78 ? 629  ILE A O   1 
ATOM   4978 C CB  . ILE A 1 629 ? -24.814 -2.395  20.399 1.00 14.57 ? 629  ILE A CB  1 
ATOM   4979 C CG1 . ILE A 1 629 ? -26.086 -2.307  19.535 1.00 13.78 ? 629  ILE A CG1 1 
ATOM   4980 C CG2 . ILE A 1 629 ? -25.165 -2.418  21.935 1.00 15.88 ? 629  ILE A CG2 1 
ATOM   4981 C CD1 . ILE A 1 629 ? -26.832 -3.601  19.500 1.00 15.87 ? 629  ILE A CD1 1 
ATOM   4982 N N   . ARG A 1 630 ? -21.792 -1.836  21.119 1.00 13.86 ? 630  ARG A N   1 
ATOM   4983 C CA  . ARG A 1 630 ? -20.652 -1.606  22.021 1.00 13.40 ? 630  ARG A CA  1 
ATOM   4984 C C   . ARG A 1 630 ? -20.196 -0.160  21.962 1.00 13.82 ? 630  ARG A C   1 
ATOM   4985 O O   . ARG A 1 630 ? -20.009 0.493   23.012 1.00 12.64 ? 630  ARG A O   1 
ATOM   4986 C CB  . ARG A 1 630 ? -19.454 -2.520  21.654 1.00 13.28 ? 630  ARG A CB  1 
ATOM   4987 C CG  . ARG A 1 630 ? -18.162 -2.202  22.485 1.00 11.24 ? 630  ARG A CG  1 
ATOM   4988 C CD  . ARG A 1 630 ? -16.900 -2.838  21.873 1.00 14.19 ? 630  ARG A CD  1 
ATOM   4989 N NE  . ARG A 1 630 ? -15.751 -2.700  22.787 1.00 12.27 ? 630  ARG A NE  1 
ATOM   4990 C CZ  . ARG A 1 630 ? -15.475 -3.547  23.779 1.00 12.99 ? 630  ARG A CZ  1 
ATOM   4991 N NH1 . ARG A 1 630 ? -16.240 -4.612  23.996 1.00 13.13 ? 630  ARG A NH1 1 
ATOM   4992 N NH2 . ARG A 1 630 ? -14.439 -3.335  24.573 1.00 14.08 ? 630  ARG A NH2 1 
ATOM   4993 N N   . TYR A 1 631 ? -19.979 0.343   20.737 1.00 14.45 ? 631  TYR A N   1 
ATOM   4994 C CA  . TYR A 1 631 ? -19.459 1.727   20.554 1.00 14.40 ? 631  TYR A CA  1 
ATOM   4995 C C   . TYR A 1 631 ? -20.446 2.793   21.063 1.00 14.25 ? 631  TYR A C   1 
ATOM   4996 O O   . TYR A 1 631 ? -20.067 3.797   21.666 1.00 14.01 ? 631  TYR A O   1 
ATOM   4997 C CB  . TYR A 1 631 ? -19.100 1.964   19.083 1.00 14.42 ? 631  TYR A CB  1 
ATOM   4998 C CG  . TYR A 1 631 ? -17.694 1.518   18.716 1.00 16.39 ? 631  TYR A CG  1 
ATOM   4999 C CD1 . TYR A 1 631 ? -17.261 0.218   18.954 1.00 17.55 ? 631  TYR A CD1 1 
ATOM   5000 C CD2 . TYR A 1 631 ? -16.785 2.423   18.133 1.00 19.13 ? 631  TYR A CD2 1 
ATOM   5001 C CE1 . TYR A 1 631 ? -15.940 -0.196  18.617 1.00 17.40 ? 631  TYR A CE1 1 
ATOM   5002 C CE2 . TYR A 1 631 ? -15.472 2.016   17.776 1.00 18.30 ? 631  TYR A CE2 1 
ATOM   5003 C CZ  . TYR A 1 631 ? -15.071 0.718   18.035 1.00 16.02 ? 631  TYR A CZ  1 
ATOM   5004 O OH  . TYR A 1 631 ? -13.820 0.316   17.681 1.00 14.86 ? 631  TYR A OH  1 
ATOM   5005 N N   . THR A 1 632 ? -21.727 2.566   20.824 1.00 13.84 ? 632  THR A N   1 
ATOM   5006 C CA  . THR A 1 632 ? -22.767 3.417   21.419 1.00 14.31 ? 632  THR A CA  1 
ATOM   5007 C C   . THR A 1 632 ? -22.628 3.507   22.934 1.00 14.54 ? 632  THR A C   1 
ATOM   5008 O O   . THR A 1 632 ? -22.832 4.558   23.509 1.00 15.53 ? 632  THR A O   1 
ATOM   5009 C CB  . THR A 1 632 ? -24.175 2.868   21.067 1.00 13.85 ? 632  THR A CB  1 
ATOM   5010 O OG1 . THR A 1 632 ? -24.294 2.757   19.649 1.00 13.31 ? 632  THR A OG1 1 
ATOM   5011 C CG2 . THR A 1 632 ? -25.271 3.808   21.559 1.00 14.93 ? 632  THR A CG2 1 
ATOM   5012 N N   . LEU A 1 633 ? -22.258 2.407   23.590 1.00 14.96 ? 633  LEU A N   1 
ATOM   5013 C CA  . LEU A 1 633 ? -22.269 2.358   25.052 1.00 15.90 ? 633  LEU A CA  1 
ATOM   5014 C C   . LEU A 1 633 ? -20.895 2.604   25.585 1.00 15.46 ? 633  LEU A C   1 
ATOM   5015 O O   . LEU A 1 633 ? -20.664 2.363   26.758 1.00 15.81 ? 633  LEU A O   1 
ATOM   5016 C CB  . LEU A 1 633 ? -22.795 0.991   25.581 1.00 15.31 ? 633  LEU A CB  1 
ATOM   5017 C CG  . LEU A 1 633 ? -24.277 0.688   25.347 1.00 18.17 ? 633  LEU A CG  1 
ATOM   5018 C CD1 . LEU A 1 633 ? -24.536 -0.809  25.482 1.00 17.36 ? 633  LEU A CD1 1 
ATOM   5019 C CD2 . LEU A 1 633 ? -25.172 1.490   26.307 1.00 19.58 ? 633  LEU A CD2 1 
ATOM   5020 N N   . LEU A 1 634 ? -19.975 3.078   24.744 1.00 15.40 ? 634  LEU A N   1 
ATOM   5021 C CA  . LEU A 1 634 ? -18.610 3.392   25.245 1.00 15.23 ? 634  LEU A CA  1 
ATOM   5022 C C   . LEU A 1 634 ? -18.534 4.450   26.346 1.00 14.60 ? 634  LEU A C   1 
ATOM   5023 O O   . LEU A 1 634 ? -17.720 4.332   27.223 1.00 13.44 ? 634  LEU A O   1 
ATOM   5024 C CB  . LEU A 1 634 ? -17.649 3.733   24.114 1.00 15.95 ? 634  LEU A CB  1 
ATOM   5025 C CG  . LEU A 1 634 ? -17.309 2.602   23.153 1.00 17.88 ? 634  LEU A CG  1 
ATOM   5026 C CD1 . LEU A 1 634 ? -16.423 3.085   22.021 1.00 17.94 ? 634  LEU A CD1 1 
ATOM   5027 C CD2 . LEU A 1 634 ? -16.719 1.398   23.853 1.00 19.84 ? 634  LEU A CD2 1 
ATOM   5028 N N   . PRO A 1 635 ? -19.363 5.526   26.302 1.00 14.24 ? 635  PRO A N   1 
ATOM   5029 C CA  . PRO A 1 635 ? -19.302 6.363   27.496 1.00 13.23 ? 635  PRO A CA  1 
ATOM   5030 C C   . PRO A 1 635 ? -19.674 5.665   28.817 1.00 12.89 ? 635  PRO A C   1 
ATOM   5031 O O   . PRO A 1 635 ? -19.107 5.972   29.845 1.00 12.82 ? 635  PRO A O   1 
ATOM   5032 C CB  . PRO A 1 635 ? -20.264 7.522   27.155 1.00 15.04 ? 635  PRO A CB  1 
ATOM   5033 C CG  . PRO A 1 635 ? -20.223 7.609   25.661 1.00 13.43 ? 635  PRO A CG  1 
ATOM   5034 C CD  . PRO A 1 635 ? -20.218 6.129   25.259 1.00 14.51 ? 635  PRO A CD  1 
ATOM   5035 N N   . TYR A 1 636 ? -20.662 4.772   28.784 1.00 13.20 ? 636  TYR A N   1 
ATOM   5036 C CA  . TYR A 1 636 ? -20.984 3.892   29.904 1.00 12.60 ? 636  TYR A CA  1 
ATOM   5037 C C   . TYR A 1 636 ? -19.792 2.975   30.271 1.00 12.28 ? 636  TYR A C   1 
ATOM   5038 O O   . TYR A 1 636 ? -19.422 2.916   31.403 1.00 11.89 ? 636  TYR A O   1 
ATOM   5039 C CB  . TYR A 1 636 ? -22.211 3.040   29.559 1.00 11.91 ? 636  TYR A CB  1 
ATOM   5040 C CG  . TYR A 1 636 ? -22.627 2.058   30.648 1.00 13.19 ? 636  TYR A CG  1 
ATOM   5041 C CD1 . TYR A 1 636 ? -22.965 2.496   31.915 1.00 13.17 ? 636  TYR A CD1 1 
ATOM   5042 C CD2 . TYR A 1 636 ? -22.727 0.702   30.382 1.00 10.46 ? 636  TYR A CD2 1 
ATOM   5043 C CE1 . TYR A 1 636 ? -23.347 1.609   32.907 1.00 13.52 ? 636  TYR A CE1 1 
ATOM   5044 C CE2 . TYR A 1 636 ? -23.118 -0.187  31.367 1.00 11.67 ? 636  TYR A CE2 1 
ATOM   5045 C CZ  . TYR A 1 636 ? -23.417 0.276   32.621 1.00 11.46 ? 636  TYR A CZ  1 
ATOM   5046 O OH  . TYR A 1 636 ? -23.791 -0.608  33.585 1.00 14.66 ? 636  TYR A OH  1 
ATOM   5047 N N   . LEU A 1 637 ? -19.251 2.229   29.318 1.00 12.79 ? 637  LEU A N   1 
ATOM   5048 C CA  . LEU A 1 637 ? -18.058 1.384   29.584 1.00 13.69 ? 637  LEU A CA  1 
ATOM   5049 C C   . LEU A 1 637 ? -16.898 2.171   30.153 1.00 14.22 ? 637  LEU A C   1 
ATOM   5050 O O   . LEU A 1 637 ? -16.219 1.725   31.095 1.00 15.04 ? 637  LEU A O   1 
ATOM   5051 C CB  . LEU A 1 637 ? -17.626 0.632   28.322 1.00 13.50 ? 637  LEU A CB  1 
ATOM   5052 C CG  . LEU A 1 637 ? -16.568 -0.466  28.483 1.00 13.34 ? 637  LEU A CG  1 
ATOM   5053 C CD1 . LEU A 1 637 ? -17.172 -1.613  29.362 1.00 11.23 ? 637  LEU A CD1 1 
ATOM   5054 C CD2 . LEU A 1 637 ? -16.221 -0.957  27.116 1.00 11.21 ? 637  LEU A CD2 1 
ATOM   5055 N N   . TYR A 1 638 ? -16.646 3.341   29.580 1.00 14.70 ? 638  TYR A N   1 
ATOM   5056 C CA  . TYR A 1 638 ? -15.519 4.168   30.015 1.00 14.67 ? 638  TYR A CA  1 
ATOM   5057 C C   . TYR A 1 638 ? -15.680 4.661   31.462 1.00 14.29 ? 638  TYR A C   1 
ATOM   5058 O O   . TYR A 1 638 ? -14.722 4.703   32.235 1.00 13.71 ? 638  TYR A O   1 
ATOM   5059 C CB  . TYR A 1 638 ? -15.362 5.370   29.064 1.00 15.10 ? 638  TYR A CB  1 
ATOM   5060 C CG  . TYR A 1 638 ? -14.077 6.164   29.246 1.00 13.11 ? 638  TYR A CG  1 
ATOM   5061 C CD1 . TYR A 1 638 ? -12.827 5.542   29.136 1.00 14.70 ? 638  TYR A CD1 1 
ATOM   5062 C CD2 . TYR A 1 638 ? -14.111 7.526   29.493 1.00 12.83 ? 638  TYR A CD2 1 
ATOM   5063 C CE1 . TYR A 1 638 ? -11.629 6.254   29.288 1.00 15.10 ? 638  TYR A CE1 1 
ATOM   5064 C CE2 . TYR A 1 638 ? -12.902 8.263   29.635 1.00 12.99 ? 638  TYR A CE2 1 
ATOM   5065 C CZ  . TYR A 1 638 ? -11.681 7.612   29.532 1.00 15.65 ? 638  TYR A CZ  1 
ATOM   5066 O OH  . TYR A 1 638 ? -10.503 8.346   29.654 1.00 14.68 ? 638  TYR A OH  1 
ATOM   5067 N N   . THR A 1 639 ? -16.908 5.031   31.826 1.00 13.90 ? 639  THR A N   1 
ATOM   5068 C CA  . THR A 1 639 ? -17.204 5.425   33.193 1.00 13.23 ? 639  THR A CA  1 
ATOM   5069 C C   . THR A 1 639 ? -16.975 4.253   34.169 1.00 12.71 ? 639  THR A C   1 
ATOM   5070 O O   . THR A 1 639 ? -16.481 4.462   35.266 1.00 13.48 ? 639  THR A O   1 
ATOM   5071 C CB  . THR A 1 639 ? -18.645 5.997   33.306 1.00 12.72 ? 639  THR A CB  1 
ATOM   5072 O OG1 . THR A 1 639 ? -18.770 7.076   32.380 1.00 13.85 ? 639  THR A OG1 1 
ATOM   5073 C CG2 . THR A 1 639 ? -18.964 6.479   34.731 1.00 13.75 ? 639  THR A CG2 1 
ATOM   5074 N N   . LEU A 1 640 ? -17.332 3.038   33.756 1.00 12.49 ? 640  LEU A N   1 
ATOM   5075 C CA  . LEU A 1 640 ? -17.086 1.822   34.549 1.00 11.89 ? 640  LEU A CA  1 
ATOM   5076 C C   . LEU A 1 640 ? -15.591 1.620   34.779 1.00 11.84 ? 640  LEU A C   1 
ATOM   5077 O O   . LEU A 1 640 ? -15.178 1.220   35.862 1.00 12.96 ? 640  LEU A O   1 
ATOM   5078 C CB  . LEU A 1 640 ? -17.653 0.595   33.835 1.00 10.94 ? 640  LEU A CB  1 
ATOM   5079 C CG  . LEU A 1 640 ? -19.184 0.519   33.701 1.00 9.77  ? 640  LEU A CG  1 
ATOM   5080 C CD1 . LEU A 1 640 ? -19.560 -0.817  33.097 1.00 10.18 ? 640  LEU A CD1 1 
ATOM   5081 C CD2 . LEU A 1 640 ? -19.815 0.711   35.045 1.00 10.48 ? 640  LEU A CD2 1 
ATOM   5082 N N   . PHE A 1 641 ? -14.802 1.872   33.753 1.00 11.70 ? 641  PHE A N   1 
ATOM   5083 C CA  . PHE A 1 641 ? -13.308 1.859   33.882 1.00 12.99 ? 641  PHE A CA  1 
ATOM   5084 C C   . PHE A 1 641 ? -12.837 2.968   34.782 1.00 12.96 ? 641  PHE A C   1 
ATOM   5085 O O   . PHE A 1 641 ? -11.873 2.798   35.520 1.00 14.12 ? 641  PHE A O   1 
ATOM   5086 C CB  . PHE A 1 641 ? -12.647 1.951   32.493 1.00 12.19 ? 641  PHE A CB  1 
ATOM   5087 C CG  . PHE A 1 641 ? -12.481 0.620   31.817 1.00 13.34 ? 641  PHE A CG  1 
ATOM   5088 C CD1 . PHE A 1 641 ? -11.401 -0.220  32.152 1.00 13.13 ? 641  PHE A CD1 1 
ATOM   5089 C CD2 . PHE A 1 641 ? -13.338 0.221   30.825 1.00 11.97 ? 641  PHE A CD2 1 
ATOM   5090 C CE1 . PHE A 1 641 ? -11.243 -1.450  31.537 1.00 11.32 ? 641  PHE A CE1 1 
ATOM   5091 C CE2 . PHE A 1 641 ? -13.183 -0.999  30.196 1.00 14.20 ? 641  PHE A CE2 1 
ATOM   5092 C CZ  . PHE A 1 641 ? -12.114 -1.846  30.562 1.00 14.69 ? 641  PHE A CZ  1 
ATOM   5093 N N   . PHE A 1 642 ? -13.525 4.124   34.752 1.00 13.17 ? 642  PHE A N   1 
ATOM   5094 C CA  . PHE A 1 642 ? -13.149 5.206   35.644 1.00 12.72 ? 642  PHE A CA  1 
ATOM   5095 C C   . PHE A 1 642 ? -13.396 4.766   37.071 1.00 13.00 ? 642  PHE A C   1 
ATOM   5096 O O   . PHE A 1 642 ? -12.562 5.028   37.962 1.00 13.03 ? 642  PHE A O   1 
ATOM   5097 C CB  . PHE A 1 642 ? -13.824 6.557   35.321 1.00 13.01 ? 642  PHE A CB  1 
ATOM   5098 C CG  . PHE A 1 642 ? -13.901 7.505   36.506 1.00 12.26 ? 642  PHE A CG  1 
ATOM   5099 C CD1 . PHE A 1 642 ? -12.761 8.169   36.965 1.00 11.86 ? 642  PHE A CD1 1 
ATOM   5100 C CD2 . PHE A 1 642 ? -15.130 7.726   37.164 1.00 13.76 ? 642  PHE A CD2 1 
ATOM   5101 C CE1 . PHE A 1 642 ? -12.826 9.054   38.054 1.00 15.01 ? 642  PHE A CE1 1 
ATOM   5102 C CE2 . PHE A 1 642 ? -15.208 8.602   38.257 1.00 16.17 ? 642  PHE A CE2 1 
ATOM   5103 C CZ  . PHE A 1 642 ? -14.049 9.263   38.711 1.00 15.22 ? 642  PHE A CZ  1 
ATOM   5104 N N   . ARG A 1 643 ? -14.487 4.031   37.295 1.00 12.38 ? 643  ARG A N   1 
ATOM   5105 C CA  . ARG A 1 643 ? -14.778 3.563   38.650 1.00 11.83 ? 643  ARG A CA  1 
ATOM   5106 C C   . ARG A 1 643 ? -13.845 2.436   39.072 1.00 11.89 ? 643  ARG A C   1 
ATOM   5107 O O   . ARG A 1 643 ? -13.492 2.365   40.233 1.00 12.81 ? 643  ARG A O   1 
ATOM   5108 C CB  . ARG A 1 643 ? -16.268 3.206   38.856 1.00 12.01 ? 643  ARG A CB  1 
ATOM   5109 C CG  . ARG A 1 643 ? -17.236 4.440   38.856 1.00 13.96 ? 643  ARG A CG  1 
ATOM   5110 C CD  . ARG A 1 643 ? -16.858 5.515   39.873 1.00 17.74 ? 643  ARG A CD  1 
ATOM   5111 N NE  . ARG A 1 643 ? -17.972 6.439   40.089 1.00 23.64 ? 643  ARG A NE  1 
ATOM   5112 C CZ  . ARG A 1 643 ? -17.948 7.520   40.867 1.00 23.86 ? 643  ARG A CZ  1 
ATOM   5113 N NH1 . ARG A 1 643 ? -16.862 7.862   41.532 1.00 27.89 ? 643  ARG A NH1 1 
ATOM   5114 N NH2 . ARG A 1 643 ? -19.032 8.268   40.974 1.00 25.11 ? 643  ARG A NH2 1 
ATOM   5115 N N   . ALA A 1 644 ? -13.454 1.564   38.144 1.00 10.29 ? 644  ALA A N   1 
ATOM   5116 C CA  . ALA A 1 644 ? -12.473 0.517   38.419 1.00 11.70 ? 644  ALA A CA  1 
ATOM   5117 C C   . ALA A 1 644 ? -11.097 1.134   38.809 1.00 11.80 ? 644  ALA A C   1 
ATOM   5118 O O   . ALA A 1 644 ? -10.472 0.753   39.799 1.00 11.90 ? 644  ALA A O   1 
ATOM   5119 C CB  . ALA A 1 644 ? -12.337 -0.439  37.159 1.00 11.03 ? 644  ALA A CB  1 
ATOM   5120 N N   . HIS A 1 645 ? -10.674 2.133   38.055 1.00 12.48 ? 645  HIS A N   1 
ATOM   5121 C CA  . HIS A 1 645 ? -9.477  2.908   38.365 1.00 13.43 ? 645  HIS A CA  1 
ATOM   5122 C C   . HIS A 1 645 ? -9.491  3.738   39.672 1.00 15.07 ? 645  HIS A C   1 
ATOM   5123 O O   . HIS A 1 645 ? -8.501  3.746   40.406 1.00 16.40 ? 645  HIS A O   1 
ATOM   5124 C CB  . HIS A 1 645 ? -9.107  3.815   37.178 1.00 13.67 ? 645  HIS A CB  1 
ATOM   5125 C CG  . HIS A 1 645 ? -7.981  4.754   37.492 1.00 17.04 ? 645  HIS A CG  1 
ATOM   5126 N ND1 . HIS A 1 645 ? -6.686  4.319   37.651 1.00 19.27 ? 645  HIS A ND1 1 
ATOM   5127 C CD2 . HIS A 1 645 ? -7.964  6.082   37.761 1.00 20.54 ? 645  HIS A CD2 1 
ATOM   5128 C CE1 . HIS A 1 645 ? -5.907  5.339   37.971 1.00 19.19 ? 645  HIS A CE1 1 
ATOM   5129 N NE2 . HIS A 1 645 ? -6.660  6.422   38.048 1.00 22.71 ? 645  HIS A NE2 1 
ATOM   5130 N N   . SER A 1 646 ? -10.599 4.415   39.991 1.00 15.29 ? 646  SER A N   1 
ATOM   5131 C CA  . SER A 1 646 ? -10.628 5.350   41.112 1.00 16.11 ? 646  SER A CA  1 
ATOM   5132 C C   . SER A 1 646 ? -11.131 4.738   42.428 1.00 16.62 ? 646  SER A C   1 
ATOM   5133 O O   . SER A 1 646 ? -10.855 5.247   43.513 1.00 16.64 ? 646  SER A O   1 
ATOM   5134 C CB  . SER A 1 646 ? -11.457 6.595   40.743 1.00 16.92 ? 646  SER A CB  1 
ATOM   5135 O OG  . SER A 1 646 ? -12.797 6.232   40.420 1.00 17.12 ? 646  SER A OG  1 
ATOM   5136 N N   . ARG A 1 647 ? -11.844 3.629   42.335 1.00 16.91 ? 647  ARG A N   1 
ATOM   5137 C CA  . ARG A 1 647 ? -12.542 3.104   43.490 1.00 17.51 ? 647  ARG A CA  1 
ATOM   5138 C C   . ARG A 1 647 ? -12.344 1.614   43.627 1.00 16.38 ? 647  ARG A C   1 
ATOM   5139 O O   . ARG A 1 647 ? -12.369 1.083   44.728 1.00 16.24 ? 647  ARG A O   1 
ATOM   5140 C CB  . ARG A 1 647 ? -14.040 3.451   43.377 1.00 17.09 ? 647  ARG A CB  1 
ATOM   5141 C CG  . ARG A 1 647 ? -14.869 2.983   44.531 1.00 20.40 ? 647  ARG A CG  1 
ATOM   5142 C CD  . ARG A 1 647 ? -16.247 3.685   44.514 1.00 23.11 ? 647  ARG A CD  1 
ATOM   5143 N NE  . ARG A 1 647 ? -17.140 3.167   43.479 1.00 22.21 ? 647  ARG A NE  1 
ATOM   5144 C CZ  . ARG A 1 647 ? -18.190 3.822   42.973 1.00 24.35 ? 647  ARG A CZ  1 
ATOM   5145 N NH1 . ARG A 1 647 ? -18.509 5.040   43.392 1.00 25.53 ? 647  ARG A NH1 1 
ATOM   5146 N NH2 . ARG A 1 647 ? -18.927 3.262   42.030 1.00 23.57 ? 647  ARG A NH2 1 
ATOM   5147 N N   . GLY A 1 648 ? -12.149 0.944   42.495 1.00 16.31 ? 648  GLY A N   1 
ATOM   5148 C CA  . GLY A 1 648 ? -11.863 -0.483  42.479 1.00 16.77 ? 648  GLY A CA  1 
ATOM   5149 C C   . GLY A 1 648 ? -13.035 -1.381  42.136 1.00 17.07 ? 648  GLY A C   1 
ATOM   5150 O O   . GLY A 1 648 ? -13.017 -2.549  42.480 1.00 16.89 ? 648  GLY A O   1 
ATOM   5151 N N   . ASP A 1 649 ? -14.055 -0.843  41.473 1.00 17.80 ? 649  ASP A N   1 
ATOM   5152 C CA  . ASP A 1 649 ? -15.163 -1.654  40.992 1.00 18.55 ? 649  ASP A CA  1 
ATOM   5153 C C   . ASP A 1 649 ? -14.733 -2.575  39.846 1.00 19.18 ? 649  ASP A C   1 
ATOM   5154 O O   . ASP A 1 649 ? -13.815 -2.255  39.083 1.00 21.35 ? 649  ASP A O   1 
ATOM   5155 C CB  . ASP A 1 649 ? -16.348 -0.778  40.514 1.00 19.10 ? 649  ASP A CB  1 
ATOM   5156 C CG  . ASP A 1 649 ? -16.705 0.339   41.470 1.00 20.42 ? 649  ASP A CG  1 
ATOM   5157 O OD1 . ASP A 1 649 ? -15.888 0.729   42.318 1.00 25.30 ? 649  ASP A OD1 1 
ATOM   5158 O OD2 . ASP A 1 649 ? -17.816 0.876   41.353 1.00 25.55 ? 649  ASP A OD2 1 
ATOM   5159 N N   . THR A 1 650 ? -15.409 -3.714  39.700 1.00 18.51 ? 650  THR A N   1 
ATOM   5160 C CA  . THR A 1 650 ? -15.254 -4.550  38.507 1.00 17.24 ? 650  THR A CA  1 
ATOM   5161 C C   . THR A 1 650 ? -15.877 -3.854  37.284 1.00 16.48 ? 650  THR A C   1 
ATOM   5162 O O   . THR A 1 650 ? -16.670 -2.929  37.456 1.00 18.43 ? 650  THR A O   1 
ATOM   5163 C CB  . THR A 1 650 ? -15.908 -5.927  38.706 1.00 17.22 ? 650  THR A CB  1 
ATOM   5164 O OG1 . THR A 1 650 ? -17.317 -5.778  39.028 1.00 17.22 ? 650  THR A OG1 1 
ATOM   5165 C CG2 . THR A 1 650 ? -15.209 -6.672  39.823 1.00 16.73 ? 650  THR A CG2 1 
ATOM   5166 N N   . VAL A 1 651 ? -15.534 -4.291  36.073 1.00 15.16 ? 651  VAL A N   1 
ATOM   5167 C CA  . VAL A 1 651 ? -16.112 -3.762  34.845 1.00 14.17 ? 651  VAL A CA  1 
ATOM   5168 C C   . VAL A 1 651 ? -17.057 -4.811  34.280 1.00 15.37 ? 651  VAL A C   1 
ATOM   5169 O O   . VAL A 1 651 ? -18.255 -4.563  34.274 1.00 14.45 ? 651  VAL A O   1 
ATOM   5170 C CB  . VAL A 1 651 ? -15.084 -3.248  33.800 1.00 15.36 ? 651  VAL A CB  1 
ATOM   5171 C CG1 . VAL A 1 651 ? -15.784 -2.854  32.511 1.00 14.58 ? 651  VAL A CG1 1 
ATOM   5172 C CG2 . VAL A 1 651 ? -14.290 -2.075  34.339 1.00 11.96 ? 651  VAL A CG2 1 
ATOM   5173 N N   . ALA A 1 652 ? -16.529 -5.957  33.819 1.00 15.29 ? 652  ALA A N   1 
ATOM   5174 C CA  . ALA A 1 652 ? -17.354 -7.137  33.555 1.00 15.63 ? 652  ALA A CA  1 
ATOM   5175 C C   . ALA A 1 652 ? -17.585 -7.744  34.944 1.00 16.00 ? 652  ALA A C   1 
ATOM   5176 O O   . ALA A 1 652 ? -16.633 -8.002  35.687 1.00 13.95 ? 652  ALA A O   1 
ATOM   5177 C CB  . ALA A 1 652 ? -16.624 -8.145  32.642 1.00 16.13 ? 652  ALA A CB  1 
ATOM   5178 N N   . ARG A 1 653 ? -18.856 -7.932  35.291 1.00 14.57 ? 653  ARG A N   1 
ATOM   5179 C CA  . ARG A 1 653 ? -19.258 -8.219  36.641 1.00 13.93 ? 653  ARG A CA  1 
ATOM   5180 C C   . ARG A 1 653 ? -20.149 -9.468  36.668 1.00 14.53 ? 653  ARG A C   1 
ATOM   5181 O O   . ARG A 1 653 ? -21.040 -9.643  35.797 1.00 14.21 ? 653  ARG A O   1 
ATOM   5182 C CB  . ARG A 1 653 ? -20.010 -6.986  37.207 1.00 14.64 ? 653  ARG A CB  1 
ATOM   5183 C CG  . ARG A 1 653 ? -20.173 -6.947  38.719 1.00 12.84 ? 653  ARG A CG  1 
ATOM   5184 C CD  . ARG A 1 653 ? -20.828 -5.665  39.150 1.00 14.15 ? 653  ARG A CD  1 
ATOM   5185 N NE  . ARG A 1 653 ? -19.924 -4.540  38.943 1.00 11.08 ? 653  ARG A NE  1 
ATOM   5186 C CZ  . ARG A 1 653 ? -20.246 -3.268  39.113 1.00 13.87 ? 653  ARG A CZ  1 
ATOM   5187 N NH1 . ARG A 1 653 ? -21.482 -2.885  39.496 1.00 12.62 ? 653  ARG A NH1 1 
ATOM   5188 N NH2 . ARG A 1 653 ? -19.314 -2.370  38.889 1.00 13.76 ? 653  ARG A NH2 1 
ATOM   5189 N N   . PRO A 1 654 ? -19.925 -10.349 37.677 1.00 14.11 ? 654  PRO A N   1 
ATOM   5190 C CA  . PRO A 1 654 ? -20.819 -11.480 37.870 1.00 13.41 ? 654  PRO A CA  1 
ATOM   5191 C C   . PRO A 1 654 ? -22.188 -10.947 38.255 1.00 13.47 ? 654  PRO A C   1 
ATOM   5192 O O   . PRO A 1 654 ? -22.270 -9.914  38.911 1.00 13.24 ? 654  PRO A O   1 
ATOM   5193 C CB  . PRO A 1 654 ? -20.198 -12.213 39.052 1.00 13.92 ? 654  PRO A CB  1 
ATOM   5194 C CG  . PRO A 1 654 ? -18.678 -11.753 39.044 1.00 12.70 ? 654  PRO A CG  1 
ATOM   5195 C CD  . PRO A 1 654 ? -18.850 -10.313 38.684 1.00 13.94 ? 654  PRO A CD  1 
ATOM   5196 N N   . LEU A 1 655 ? -23.243 -11.625 37.818 1.00 13.60 ? 655  LEU A N   1 
ATOM   5197 C CA  . LEU A 1 655 ? -24.610 -11.334 38.289 1.00 14.12 ? 655  LEU A CA  1 
ATOM   5198 C C   . LEU A 1 655 ? -24.715 -11.316 39.799 1.00 14.37 ? 655  LEU A C   1 
ATOM   5199 O O   . LEU A 1 655 ? -25.424 -10.491 40.349 1.00 14.78 ? 655  LEU A O   1 
ATOM   5200 C CB  . LEU A 1 655 ? -25.606 -12.364 37.738 1.00 14.35 ? 655  LEU A CB  1 
ATOM   5201 C CG  . LEU A 1 655 ? -26.295 -12.070 36.407 1.00 13.59 ? 655  LEU A CG  1 
ATOM   5202 C CD1 . LEU A 1 655 ? -25.293 -11.874 35.296 1.00 15.76 ? 655  LEU A CD1 1 
ATOM   5203 C CD2 . LEU A 1 655 ? -27.249 -13.257 36.043 1.00 14.42 ? 655  LEU A CD2 1 
ATOM   5204 N N   . LEU A 1 656 ? -23.977 -12.201 40.479 1.00 14.92 ? 656  LEU A N   1 
ATOM   5205 C CA  . LEU A 1 656 ? -24.077 -12.312 41.935 1.00 15.08 ? 656  LEU A CA  1 
ATOM   5206 C C   . LEU A 1 656 ? -23.553 -11.067 42.677 1.00 15.66 ? 656  LEU A C   1 
ATOM   5207 O O   . LEU A 1 656 ? -23.885 -10.854 43.843 1.00 16.67 ? 656  LEU A O   1 
ATOM   5208 C CB  . LEU A 1 656 ? -23.374 -13.588 42.443 1.00 15.40 ? 656  LEU A CB  1 
ATOM   5209 C CG  . LEU A 1 656 ? -21.839 -13.568 42.361 1.00 16.95 ? 656  LEU A CG  1 
ATOM   5210 C CD1 . LEU A 1 656 ? -21.219 -13.254 43.753 1.00 18.81 ? 656  LEU A CD1 1 
ATOM   5211 C CD2 . LEU A 1 656 ? -21.339 -14.888 41.816 1.00 17.68 ? 656  LEU A CD2 1 
ATOM   5212 N N   . HIS A 1 657 ? -22.740 -10.247 42.012 1.00 14.99 ? 657  HIS A N   1 
ATOM   5213 C CA  . HIS A 1 657 ? -22.224 -9.034  42.637 1.00 14.46 ? 657  HIS A CA  1 
ATOM   5214 C C   . HIS A 1 657 ? -23.298 -7.968  42.767 1.00 13.99 ? 657  HIS A C   1 
ATOM   5215 O O   . HIS A 1 657 ? -23.221 -7.115  43.646 1.00 13.01 ? 657  HIS A O   1 
ATOM   5216 C CB  . HIS A 1 657 ? -21.045 -8.488  41.847 1.00 14.93 ? 657  HIS A CB  1 
ATOM   5217 C CG  . HIS A 1 657 ? -19.771 -9.217  42.107 1.00 13.60 ? 657  HIS A CG  1 
ATOM   5218 N ND1 . HIS A 1 657 ? -18.551 -8.580  42.137 1.00 11.15 ? 657  HIS A ND1 1 
ATOM   5219 C CD2 . HIS A 1 657 ? -19.529 -10.515 42.394 1.00 14.11 ? 657  HIS A CD2 1 
ATOM   5220 C CE1 . HIS A 1 657 ? -17.604 -9.460  42.417 1.00 15.13 ? 657  HIS A CE1 1 
ATOM   5221 N NE2 . HIS A 1 657 ? -18.172 -10.638 42.591 1.00 16.09 ? 657  HIS A NE2 1 
ATOM   5222 N N   . GLU A 1 658 ? -24.321 -8.070  41.920 1.00 13.81 ? 658  GLU A N   1 
ATOM   5223 C CA  . GLU A 1 658 ? -25.445 -7.167  41.957 1.00 14.92 ? 658  GLU A CA  1 
ATOM   5224 C C   . GLU A 1 658 ? -26.658 -7.828  42.612 1.00 15.12 ? 658  GLU A C   1 
ATOM   5225 O O   . GLU A 1 658 ? -27.482 -7.142  43.195 1.00 16.89 ? 658  GLU A O   1 
ATOM   5226 C CB  . GLU A 1 658 ? -25.800 -6.684  40.533 1.00 14.98 ? 658  GLU A CB  1 
ATOM   5227 C CG  . GLU A 1 658 ? -24.816 -5.648  39.918 1.00 16.43 ? 658  GLU A CG  1 
ATOM   5228 C CD  . GLU A 1 658 ? -24.673 -4.410  40.766 1.00 18.56 ? 658  GLU A CD  1 
ATOM   5229 O OE1 . GLU A 1 658 ? -25.714 -3.819  41.172 1.00 18.94 ? 658  GLU A OE1 1 
ATOM   5230 O OE2 . GLU A 1 658 ? -23.514 -4.018  41.037 1.00 20.78 ? 658  GLU A OE2 1 
ATOM   5231 N N   . PHE A 1 659 ? -26.743 -9.147  42.524 1.00 15.08 ? 659  PHE A N   1 
ATOM   5232 C CA  . PHE A 1 659 ? -27.949 -9.902  42.910 1.00 15.71 ? 659  PHE A CA  1 
ATOM   5233 C C   . PHE A 1 659 ? -27.655 -11.041 43.890 1.00 15.78 ? 659  PHE A C   1 
ATOM   5234 O O   . PHE A 1 659 ? -28.325 -12.089 43.863 1.00 14.78 ? 659  PHE A O   1 
ATOM   5235 C CB  . PHE A 1 659 ? -28.671 -10.405 41.645 1.00 14.35 ? 659  PHE A CB  1 
ATOM   5236 C CG  . PHE A 1 659 ? -29.004 -9.305  40.677 1.00 14.32 ? 659  PHE A CG  1 
ATOM   5237 C CD1 . PHE A 1 659 ? -30.026 -8.408  40.963 1.00 17.63 ? 659  PHE A CD1 1 
ATOM   5238 C CD2 . PHE A 1 659 ? -28.306 -9.169  39.468 1.00 15.84 ? 659  PHE A CD2 1 
ATOM   5239 C CE1 . PHE A 1 659 ? -30.348 -7.383  40.075 1.00 14.87 ? 659  PHE A CE1 1 
ATOM   5240 C CE2 . PHE A 1 659 ? -28.641 -8.135  38.569 1.00 14.16 ? 659  PHE A CE2 1 
ATOM   5241 C CZ  . PHE A 1 659 ? -29.647 -7.249  38.897 1.00 14.29 ? 659  PHE A CZ  1 
ATOM   5242 N N   . TYR A 1 660 ? -26.660 -10.806 44.762 1.00 15.88 ? 660  TYR A N   1 
ATOM   5243 C CA  . TYR A 1 660 ? -26.185 -11.778 45.785 1.00 17.06 ? 660  TYR A CA  1 
ATOM   5244 C C   . TYR A 1 660 ? -27.269 -12.231 46.739 1.00 17.65 ? 660  TYR A C   1 
ATOM   5245 O O   . TYR A 1 660 ? -27.130 -13.273 47.344 1.00 16.88 ? 660  TYR A O   1 
ATOM   5246 C CB  . TYR A 1 660 ? -25.016 -11.200 46.612 1.00 15.98 ? 660  TYR A CB  1 
ATOM   5247 C CG  . TYR A 1 660 ? -25.242 -9.768  46.990 1.00 17.76 ? 660  TYR A CG  1 
ATOM   5248 C CD1 . TYR A 1 660 ? -26.064 -9.423  48.066 1.00 16.31 ? 660  TYR A CD1 1 
ATOM   5249 C CD2 . TYR A 1 660 ? -24.656 -8.738  46.251 1.00 19.48 ? 660  TYR A CD2 1 
ATOM   5250 C CE1 . TYR A 1 660 ? -26.298 -8.095  48.402 1.00 18.44 ? 660  TYR A CE1 1 
ATOM   5251 C CE2 . TYR A 1 660 ? -24.895 -7.413  46.572 1.00 19.72 ? 660  TYR A CE2 1 
ATOM   5252 C CZ  . TYR A 1 660 ? -25.703 -7.099  47.654 1.00 18.45 ? 660  TYR A CZ  1 
ATOM   5253 O OH  . TYR A 1 660 ? -25.900 -5.777  47.980 1.00 19.49 ? 660  TYR A OH  1 
ATOM   5254 N N   . GLU A 1 661 ? -28.344 -11.447 46.862 1.00 19.91 ? 661  GLU A N   1 
ATOM   5255 C CA  . GLU A 1 661 ? -29.500 -11.808 47.705 1.00 21.94 ? 661  GLU A CA  1 
ATOM   5256 C C   . GLU A 1 661 ? -30.240 -12.989 47.097 1.00 21.02 ? 661  GLU A C   1 
ATOM   5257 O O   . GLU A 1 661 ? -31.020 -13.675 47.777 1.00 21.70 ? 661  GLU A O   1 
ATOM   5258 C CB  . GLU A 1 661 ? -30.462 -10.618 47.915 1.00 21.50 ? 661  GLU A CB  1 
ATOM   5259 C CG  . GLU A 1 661 ? -29.902 -9.517  48.847 1.00 26.09 ? 661  GLU A CG  1 
ATOM   5260 C CD  . GLU A 1 661 ? -30.906 -8.418  49.218 1.00 27.30 ? 661  GLU A CD  1 
ATOM   5261 O OE1 . GLU A 1 661 ? -32.004 -8.337  48.606 1.00 35.84 ? 661  GLU A OE1 1 
ATOM   5262 O OE2 . GLU A 1 661 ? -30.605 -7.623  50.142 1.00 35.51 ? 661  GLU A OE2 1 
ATOM   5263 N N   . ASP A 1 662 ? -29.954 -13.230 45.823 1.00 19.98 ? 662  ASP A N   1 
ATOM   5264 C CA  . ASP A 1 662 ? -30.596 -14.257 45.025 1.00 19.13 ? 662  ASP A CA  1 
ATOM   5265 C C   . ASP A 1 662 ? -29.651 -15.422 44.732 1.00 19.18 ? 662  ASP A C   1 
ATOM   5266 O O   . ASP A 1 662 ? -28.851 -15.352 43.809 1.00 17.95 ? 662  ASP A O   1 
ATOM   5267 C CB  . ASP A 1 662 ? -31.084 -13.603 43.724 1.00 18.38 ? 662  ASP A CB  1 
ATOM   5268 C CG  . ASP A 1 662 ? -31.879 -14.538 42.845 1.00 17.52 ? 662  ASP A CG  1 
ATOM   5269 O OD1 . ASP A 1 662 ? -31.956 -15.732 43.173 1.00 15.77 ? 662  ASP A OD1 1 
ATOM   5270 O OD2 . ASP A 1 662 ? -32.448 -14.056 41.829 1.00 16.90 ? 662  ASP A OD2 1 
ATOM   5271 N N   . ASN A 1 663 ? -29.765 -16.511 45.504 1.00 20.16 ? 663  ASN A N   1 
ATOM   5272 C CA  . ASN A 1 663 ? -28.856 -17.653 45.387 1.00 20.75 ? 663  ASN A CA  1 
ATOM   5273 C C   . ASN A 1 663 ? -28.802 -18.314 43.989 1.00 20.34 ? 663  ASN A C   1 
ATOM   5274 O O   . ASN A 1 663 ? -27.804 -18.969 43.652 1.00 19.84 ? 663  ASN A O   1 
ATOM   5275 C CB  . ASN A 1 663 ? -29.129 -18.709 46.490 1.00 21.62 ? 663  ASN A CB  1 
ATOM   5276 C CG  . ASN A 1 663 ? -30.382 -19.528 46.220 1.00 24.13 ? 663  ASN A CG  1 
ATOM   5277 O OD1 . ASN A 1 663 ? -31.438 -18.988 45.853 1.00 27.28 ? 663  ASN A OD1 1 
ATOM   5278 N ND2 . ASN A 1 663 ? -30.269 -20.846 46.387 1.00 27.49 ? 663  ASN A ND2 1 
ATOM   5279 N N   . SER A 1 664 ? -29.848 -18.123 43.175 1.00 19.84 ? 664  SER A N   1 
ATOM   5280 C CA  . SER A 1 664 ? -29.843 -18.614 41.785 1.00 20.12 ? 664  SER A CA  1 
ATOM   5281 C C   . SER A 1 664 ? -28.776 -17.954 40.923 1.00 19.24 ? 664  SER A C   1 
ATOM   5282 O O   . SER A 1 664 ? -28.489 -18.436 39.837 1.00 19.74 ? 664  SER A O   1 
ATOM   5283 C CB  . SER A 1 664 ? -31.198 -18.405 41.091 1.00 20.31 ? 664  SER A CB  1 
ATOM   5284 O OG  . SER A 1 664 ? -32.179 -19.216 41.662 1.00 19.23 ? 664  SER A OG  1 
ATOM   5285 N N   . THR A 1 665 ? -28.214 -16.844 41.393 1.00 18.87 ? 665  THR A N   1 
ATOM   5286 C CA  . THR A 1 665 ? -27.206 -16.135 40.624 1.00 18.46 ? 665  THR A CA  1 
ATOM   5287 C C   . THR A 1 665 ? -25.778 -16.584 41.052 1.00 18.72 ? 665  THR A C   1 
ATOM   5288 O O   . THR A 1 665 ? -24.818 -16.189 40.430 1.00 19.21 ? 665  THR A O   1 
ATOM   5289 C CB  . THR A 1 665 ? -27.309 -14.621 40.799 1.00 17.94 ? 665  THR A CB  1 
ATOM   5290 O OG1 . THR A 1 665 ? -26.963 -14.281 42.149 1.00 19.61 ? 665  THR A OG1 1 
ATOM   5291 C CG2 . THR A 1 665 ? -28.719 -14.052 40.427 1.00 18.23 ? 665  THR A CG2 1 
ATOM   5292 N N   . TRP A 1 666 ? -25.658 -17.378 42.123 1.00 18.51 ? 666  TRP A N   1 
ATOM   5293 C CA  . TRP A 1 666 ? -24.363 -17.685 42.747 1.00 18.59 ? 666  TRP A CA  1 
ATOM   5294 C C   . TRP A 1 666 ? -23.390 -18.522 41.874 1.00 18.58 ? 666  TRP A C   1 
ATOM   5295 O O   . TRP A 1 666 ? -22.180 -18.472 42.041 1.00 19.12 ? 666  TRP A O   1 
ATOM   5296 C CB  . TRP A 1 666 ? -24.544 -18.346 44.127 1.00 18.04 ? 666  TRP A CB  1 
ATOM   5297 C CG  . TRP A 1 666 ? -25.112 -17.441 45.258 1.00 18.24 ? 666  TRP A CG  1 
ATOM   5298 C CD1 . TRP A 1 666 ? -25.417 -16.109 45.193 1.00 17.56 ? 666  TRP A CD1 1 
ATOM   5299 C CD2 . TRP A 1 666 ? -25.397 -17.847 46.605 1.00 16.82 ? 666  TRP A CD2 1 
ATOM   5300 N NE1 . TRP A 1 666 ? -25.913 -15.671 46.410 1.00 17.48 ? 666  TRP A NE1 1 
ATOM   5301 C CE2 . TRP A 1 666 ? -25.898 -16.721 47.291 1.00 18.44 ? 666  TRP A CE2 1 
ATOM   5302 C CE3 . TRP A 1 666 ? -25.313 -19.071 47.289 1.00 19.75 ? 666  TRP A CE3 1 
ATOM   5303 C CZ2 . TRP A 1 666 ? -26.291 -16.775 48.634 1.00 19.05 ? 666  TRP A CZ2 1 
ATOM   5304 C CZ3 . TRP A 1 666 ? -25.705 -19.120 48.629 1.00 18.17 ? 666  TRP A CZ3 1 
ATOM   5305 C CH2 . TRP A 1 666 ? -26.175 -17.975 49.283 1.00 18.28 ? 666  TRP A CH2 1 
ATOM   5306 N N   . ASP A 1 667 ? -23.925 -19.293 40.956 1.00 19.08 ? 667  ASP A N   1 
ATOM   5307 C CA  . ASP A 1 667 ? -23.078 -20.051 40.083 1.00 20.45 ? 667  ASP A CA  1 
ATOM   5308 C C   . ASP A 1 667 ? -23.291 -19.714 38.628 1.00 19.75 ? 667  ASP A C   1 
ATOM   5309 O O   . ASP A 1 667 ? -22.839 -20.459 37.772 1.00 20.07 ? 667  ASP A O   1 
ATOM   5310 C CB  . ASP A 1 667 ? -23.246 -21.544 40.332 1.00 21.99 ? 667  ASP A CB  1 
ATOM   5311 C CG  . ASP A 1 667 ? -24.650 -22.026 40.047 1.00 26.97 ? 667  ASP A CG  1 
ATOM   5312 O OD1 . ASP A 1 667 ? -25.503 -21.182 39.645 1.00 32.41 ? 667  ASP A OD1 1 
ATOM   5313 O OD2 . ASP A 1 667 ? -24.873 -23.252 40.200 1.00 31.44 ? 667  ASP A OD2 1 
ATOM   5314 N N   . VAL A 1 668 ? -23.982 -18.602 38.344 1.00 19.03 ? 668  VAL A N   1 
ATOM   5315 C CA  . VAL A 1 668 ? -24.214 -18.185 36.964 1.00 18.65 ? 668  VAL A CA  1 
ATOM   5316 C C   . VAL A 1 668 ? -22.912 -17.709 36.362 1.00 18.97 ? 668  VAL A C   1 
ATOM   5317 O O   . VAL A 1 668 ? -22.276 -16.822 36.904 1.00 19.72 ? 668  VAL A O   1 
ATOM   5318 C CB  . VAL A 1 668 ? -25.309 -17.112 36.857 1.00 19.07 ? 668  VAL A CB  1 
ATOM   5319 C CG1 . VAL A 1 668 ? -25.293 -16.452 35.492 1.00 17.00 ? 668  VAL A CG1 1 
ATOM   5320 C CG2 . VAL A 1 668 ? -26.642 -17.769 37.120 1.00 19.20 ? 668  VAL A CG2 1 
ATOM   5321 N N   . HIS A 1 669 ? -22.528 -18.325 35.249 1.00 19.80 ? 669  HIS A N   1 
ATOM   5322 C CA  . HIS A 1 669 ? -21.256 -18.059 34.572 1.00 21.38 ? 669  HIS A CA  1 
ATOM   5323 C C   . HIS A 1 669 ? -21.430 -18.040 33.038 1.00 20.89 ? 669  HIS A C   1 
ATOM   5324 O O   . HIS A 1 669 ? -20.457 -17.996 32.302 1.00 20.63 ? 669  HIS A O   1 
ATOM   5325 C CB  . HIS A 1 669 ? -20.213 -19.113 34.989 1.00 21.20 ? 669  HIS A CB  1 
ATOM   5326 C CG  . HIS A 1 669 ? -20.613 -20.520 34.673 1.00 23.10 ? 669  HIS A CG  1 
ATOM   5327 N ND1 . HIS A 1 669 ? -20.262 -21.147 33.496 1.00 26.53 ? 669  HIS A ND1 1 
ATOM   5328 C CD2 . HIS A 1 669 ? -21.348 -21.418 35.367 1.00 24.91 ? 669  HIS A CD2 1 
ATOM   5329 C CE1 . HIS A 1 669 ? -20.769 -22.366 33.478 1.00 26.10 ? 669  HIS A CE1 1 
ATOM   5330 N NE2 . HIS A 1 669 ? -21.422 -22.560 34.607 1.00 25.87 ? 669  HIS A NE2 1 
ATOM   5331 N N   . GLN A 1 670 ? -22.672 -18.114 32.572 1.00 19.99 ? 670  GLN A N   1 
ATOM   5332 C CA  . GLN A 1 670 ? -22.985 -18.089 31.134 1.00 20.68 ? 670  GLN A CA  1 
ATOM   5333 C C   . GLN A 1 670 ? -23.561 -16.729 30.695 1.00 18.90 ? 670  GLN A C   1 
ATOM   5334 O O   . GLN A 1 670 ? -23.822 -16.487 29.510 1.00 17.83 ? 670  GLN A O   1 
ATOM   5335 C CB  . GLN A 1 670 ? -23.916 -19.273 30.752 1.00 21.16 ? 670  GLN A CB  1 
ATOM   5336 C CG  . GLN A 1 670 ? -23.142 -20.616 30.645 1.00 22.85 ? 670  GLN A CG  1 
ATOM   5337 C CD  . GLN A 1 670 ? -23.853 -21.729 29.829 1.00 25.02 ? 670  GLN A CD  1 
ATOM   5338 O OE1 . GLN A 1 670 ? -23.223 -22.745 29.500 1.00 30.73 ? 670  GLN A OE1 1 
ATOM   5339 N NE2 . GLN A 1 670 ? -25.148 -21.546 29.512 1.00 28.27 ? 670  GLN A NE2 1 
ATOM   5340 N N   . GLN A 1 671 ? -23.725 -15.846 31.678 1.00 17.62 ? 671  GLN A N   1 
ATOM   5341 C CA  . GLN A 1 671 ? -24.148 -14.477 31.477 1.00 17.17 ? 671  GLN A CA  1 
ATOM   5342 C C   . GLN A 1 671 ? -23.238 -13.625 32.323 1.00 16.66 ? 671  GLN A C   1 
ATOM   5343 O O   . GLN A 1 671 ? -22.630 -14.125 33.262 1.00 17.52 ? 671  GLN A O   1 
ATOM   5344 C CB  . GLN A 1 671 ? -25.585 -14.286 31.988 1.00 17.10 ? 671  GLN A CB  1 
ATOM   5345 C CG  . GLN A 1 671 ? -26.633 -15.049 31.221 1.00 18.02 ? 671  GLN A CG  1 
ATOM   5346 C CD  . GLN A 1 671 ? -27.979 -14.960 31.912 1.00 17.91 ? 671  GLN A CD  1 
ATOM   5347 O OE1 . GLN A 1 671 ? -28.283 -15.741 32.830 1.00 17.66 ? 671  GLN A OE1 1 
ATOM   5348 N NE2 . GLN A 1 671 ? -28.781 -13.995 31.495 1.00 17.98 ? 671  GLN A NE2 1 
ATOM   5349 N N   . PHE A 1 672 ? -23.137 -12.344 32.000 1.00 15.92 ? 672  PHE A N   1 
ATOM   5350 C CA  . PHE A 1 672 ? -22.458 -11.398 32.874 1.00 15.53 ? 672  PHE A CA  1 
ATOM   5351 C C   . PHE A 1 672 ? -23.039 -10.002 32.700 1.00 15.81 ? 672  PHE A C   1 
ATOM   5352 O O   . PHE A 1 672 ? -23.897 -9.760  31.840 1.00 15.88 ? 672  PHE A O   1 
ATOM   5353 C CB  . PHE A 1 672 ? -20.924 -11.434 32.721 1.00 15.51 ? 672  PHE A CB  1 
ATOM   5354 C CG  . PHE A 1 672 ? -20.435 -10.961 31.398 1.00 16.13 ? 672  PHE A CG  1 
ATOM   5355 C CD1 . PHE A 1 672 ? -19.851 -9.716  31.273 1.00 14.16 ? 672  PHE A CD1 1 
ATOM   5356 C CD2 . PHE A 1 672 ? -20.512 -11.780 30.288 1.00 15.16 ? 672  PHE A CD2 1 
ATOM   5357 C CE1 . PHE A 1 672 ? -19.408 -9.274  30.057 1.00 12.00 ? 672  PHE A CE1 1 
ATOM   5358 C CE2 . PHE A 1 672 ? -20.069 -11.349 29.069 1.00 15.83 ? 672  PHE A CE2 1 
ATOM   5359 C CZ  . PHE A 1 672 ? -19.525 -10.070 28.954 1.00 15.18 ? 672  PHE A CZ  1 
ATOM   5360 N N   . LEU A 1 673 ? -22.604 -9.089  33.552 1.00 15.61 ? 673  LEU A N   1 
ATOM   5361 C CA  . LEU A 1 673 ? -23.000 -7.707  33.430 1.00 15.15 ? 673  LEU A CA  1 
ATOM   5362 C C   . LEU A 1 673 ? -21.849 -6.807  32.990 1.00 14.93 ? 673  LEU A C   1 
ATOM   5363 O O   . LEU A 1 673 ? -20.679 -7.078  33.285 1.00 14.51 ? 673  LEU A O   1 
ATOM   5364 C CB  . LEU A 1 673 ? -23.515 -7.224  34.772 1.00 15.74 ? 673  LEU A CB  1 
ATOM   5365 C CG  . LEU A 1 673 ? -24.413 -8.145  35.598 1.00 16.22 ? 673  LEU A CG  1 
ATOM   5366 C CD1 . LEU A 1 673 ? -24.414 -7.618  36.997 1.00 15.36 ? 673  LEU A CD1 1 
ATOM   5367 C CD2 . LEU A 1 673 ? -25.814 -8.109  35.039 1.00 18.88 ? 673  LEU A CD2 1 
ATOM   5368 N N   . TRP A 1 674 ? -22.176 -5.736  32.284 1.00 14.57 ? 674  TRP A N   1 
ATOM   5369 C CA  . TRP A 1 674 ? -21.288 -4.577  32.270 1.00 15.03 ? 674  TRP A CA  1 
ATOM   5370 C C   . TRP A 1 674 ? -21.689 -3.735  33.456 1.00 16.12 ? 674  TRP A C   1 
ATOM   5371 O O   . TRP A 1 674 ? -22.814 -3.212  33.469 1.00 16.56 ? 674  TRP A O   1 
ATOM   5372 C CB  . TRP A 1 674 ? -21.503 -3.733  31.027 1.00 14.62 ? 674  TRP A CB  1 
ATOM   5373 C CG  . TRP A 1 674 ? -20.707 -4.123  29.837 1.00 13.71 ? 674  TRP A CG  1 
ATOM   5374 C CD1 . TRP A 1 674 ? -20.063 -5.307  29.621 1.00 15.45 ? 674  TRP A CD1 1 
ATOM   5375 C CD2 . TRP A 1 674 ? -20.484 -3.322  28.669 1.00 14.69 ? 674  TRP A CD2 1 
ATOM   5376 N NE1 . TRP A 1 674 ? -19.449 -5.290  28.396 1.00 15.47 ? 674  TRP A NE1 1 
ATOM   5377 C CE2 . TRP A 1 674 ? -19.686 -4.082  27.791 1.00 12.92 ? 674  TRP A CE2 1 
ATOM   5378 C CE3 . TRP A 1 674 ? -20.896 -2.039  28.276 1.00 15.36 ? 674  TRP A CE3 1 
ATOM   5379 C CZ2 . TRP A 1 674 ? -19.301 -3.613  26.536 1.00 12.86 ? 674  TRP A CZ2 1 
ATOM   5380 C CZ3 . TRP A 1 674 ? -20.506 -1.569  27.033 1.00 14.15 ? 674  TRP A CZ3 1 
ATOM   5381 C CH2 . TRP A 1 674 ? -19.692 -2.350  26.187 1.00 15.25 ? 674  TRP A CH2 1 
ATOM   5382 N N   . GLY A 1 675 ? -20.811 -3.598  34.455 1.00 15.42 ? 675  GLY A N   1 
ATOM   5383 C CA  . GLY A 1 675 ? -21.168 -2.759  35.591 1.00 16.04 ? 675  GLY A CA  1 
ATOM   5384 C C   . GLY A 1 675 ? -22.531 -3.177  36.166 1.00 16.37 ? 675  GLY A C   1 
ATOM   5385 O O   . GLY A 1 675 ? -22.903 -4.344  36.107 1.00 14.80 ? 675  GLY A O   1 
ATOM   5386 N N   . PRO A 1 676 ? -23.250 -2.234  36.776 1.00 16.94 ? 676  PRO A N   1 
ATOM   5387 C CA  . PRO A 1 676 ? -24.445 -2.650  37.473 1.00 18.26 ? 676  PRO A CA  1 
ATOM   5388 C C   . PRO A 1 676 ? -25.689 -2.883  36.574 1.00 18.55 ? 676  PRO A C   1 
ATOM   5389 O O   . PRO A 1 676 ? -26.633 -3.562  37.000 1.00 19.13 ? 676  PRO A O   1 
ATOM   5390 C CB  . PRO A 1 676 ? -24.663 -1.502  38.456 1.00 19.26 ? 676  PRO A CB  1 
ATOM   5391 C CG  . PRO A 1 676 ? -24.156 -0.291  37.701 1.00 18.23 ? 676  PRO A CG  1 
ATOM   5392 C CD  . PRO A 1 676 ? -22.984 -0.788  36.908 1.00 17.26 ? 676  PRO A CD  1 
ATOM   5393 N N   . GLY A 1 677 ? -25.676 -2.392  35.334 1.00 18.67 ? 677  GLY A N   1 
ATOM   5394 C CA  . GLY A 1 677 ? -26.960 -2.206  34.604 1.00 18.16 ? 677  GLY A CA  1 
ATOM   5395 C C   . GLY A 1 677 ? -27.239 -2.879  33.268 1.00 17.61 ? 677  GLY A C   1 
ATOM   5396 O O   . GLY A 1 677 ? -28.384 -2.850  32.787 1.00 17.58 ? 677  GLY A O   1 
ATOM   5397 N N   . LEU A 1 678 ? -26.214 -3.466  32.654 1.00 17.42 ? 678  LEU A N   1 
ATOM   5398 C CA  . LEU A 1 678 ? -26.360 -4.177  31.359 1.00 16.74 ? 678  LEU A CA  1 
ATOM   5399 C C   . LEU A 1 678 ? -26.094 -5.681  31.461 1.00 16.57 ? 678  LEU A C   1 
ATOM   5400 O O   . LEU A 1 678 ? -24.954 -6.129  31.727 1.00 16.28 ? 678  LEU A O   1 
ATOM   5401 C CB  . LEU A 1 678 ? -25.469 -3.560  30.271 1.00 16.99 ? 678  LEU A CB  1 
ATOM   5402 C CG  . LEU A 1 678 ? -25.385 -4.257  28.897 1.00 16.87 ? 678  LEU A CG  1 
ATOM   5403 C CD1 . LEU A 1 678 ? -26.653 -4.014  28.075 1.00 15.78 ? 678  LEU A CD1 1 
ATOM   5404 C CD2 . LEU A 1 678 ? -24.205 -3.727  28.151 1.00 15.12 ? 678  LEU A CD2 1 
ATOM   5405 N N   . LEU A 1 679 ? -27.147 -6.448  31.207 1.00 15.38 ? 679  LEU A N   1 
ATOM   5406 C CA  . LEU A 1 679 ? -27.108 -7.894  31.238 1.00 14.83 ? 679  LEU A CA  1 
ATOM   5407 C C   . LEU A 1 679 ? -26.893 -8.501  29.851 1.00 15.12 ? 679  LEU A C   1 
ATOM   5408 O O   . LEU A 1 679 ? -27.667 -8.261  28.938 1.00 14.04 ? 679  LEU A O   1 
ATOM   5409 C CB  . LEU A 1 679 ? -28.432 -8.392  31.844 1.00 14.44 ? 679  LEU A CB  1 
ATOM   5410 C CG  . LEU A 1 679 ? -28.657 -9.885  31.801 1.00 13.85 ? 679  LEU A CG  1 
ATOM   5411 C CD1 . LEU A 1 679 ? -27.629 -10.580 32.722 1.00 10.43 ? 679  LEU A CD1 1 
ATOM   5412 C CD2 . LEU A 1 679 ? -30.098 -10.220 32.206 1.00 13.96 ? 679  LEU A CD2 1 
ATOM   5413 N N   . ILE A 1 680 ? -25.818 -9.286  29.703 1.00 16.17 ? 680  ILE A N   1 
ATOM   5414 C CA  . ILE A 1 680 ? -25.405 -9.874  28.436 1.00 16.63 ? 680  ILE A CA  1 
ATOM   5415 C C   . ILE A 1 680 ? -25.686 -11.372 28.513 1.00 16.77 ? 680  ILE A C   1 
ATOM   5416 O O   . ILE A 1 680 ? -25.143 -12.058 29.382 1.00 16.77 ? 680  ILE A O   1 
ATOM   5417 C CB  . ILE A 1 680 ? -23.856 -9.576  28.124 1.00 17.20 ? 680  ILE A CB  1 
ATOM   5418 C CG1 . ILE A 1 680 ? -23.648 -8.067  27.947 1.00 19.21 ? 680  ILE A CG1 1 
ATOM   5419 C CG2 . ILE A 1 680 ? -23.425 -10.210 26.834 1.00 16.20 ? 680  ILE A CG2 1 
ATOM   5420 C CD1 . ILE A 1 680 ? -22.483 -7.493  28.696 1.00 17.23 ? 680  ILE A CD1 1 
ATOM   5421 N N   . THR A 1 681 ? -26.519 -11.865 27.593 1.00 16.16 ? 681  THR A N   1 
ATOM   5422 C CA  . THR A 1 681 ? -26.912 -13.270 27.520 1.00 16.31 ? 681  THR A CA  1 
ATOM   5423 C C   . THR A 1 681 ? -26.569 -13.878 26.147 1.00 15.98 ? 681  THR A C   1 
ATOM   5424 O O   . THR A 1 681 ? -27.382 -13.818 25.205 1.00 16.07 ? 681  THR A O   1 
ATOM   5425 C CB  . THR A 1 681 ? -28.451 -13.425 27.846 1.00 16.23 ? 681  THR A CB  1 
ATOM   5426 O OG1 . THR A 1 681 ? -28.737 -12.764 29.085 1.00 18.28 ? 681  THR A OG1 1 
ATOM   5427 C CG2 . THR A 1 681 ? -28.818 -14.850 28.009 1.00 17.71 ? 681  THR A CG2 1 
ATOM   5428 N N   . PRO A 1 682 ? -25.339 -14.434 26.001 1.00 15.67 ? 682  PRO A N   1 
ATOM   5429 C CA  . PRO A 1 682 ? -24.946 -15.094 24.764 1.00 15.49 ? 682  PRO A CA  1 
ATOM   5430 C C   . PRO A 1 682 ? -25.538 -16.486 24.554 1.00 15.66 ? 682  PRO A C   1 
ATOM   5431 O O   . PRO A 1 682 ? -25.769 -17.226 25.516 1.00 16.05 ? 682  PRO A O   1 
ATOM   5432 C CB  . PRO A 1 682 ? -23.412 -15.226 24.895 1.00 15.64 ? 682  PRO A CB  1 
ATOM   5433 C CG  . PRO A 1 682 ? -23.183 -15.291 26.357 1.00 15.95 ? 682  PRO A CG  1 
ATOM   5434 C CD  . PRO A 1 682 ? -24.253 -14.424 26.992 1.00 16.05 ? 682  PRO A CD  1 
ATOM   5435 N N   . VAL A 1 683 ? -25.735 -16.844 23.287 1.00 16.62 ? 683  VAL A N   1 
ATOM   5436 C CA  . VAL A 1 683 ? -25.984 -18.228 22.898 1.00 17.12 ? 683  VAL A CA  1 
ATOM   5437 C C   . VAL A 1 683 ? -24.607 -18.890 22.884 1.00 18.35 ? 683  VAL A C   1 
ATOM   5438 O O   . VAL A 1 683 ? -23.677 -18.401 22.236 1.00 17.95 ? 683  VAL A O   1 
ATOM   5439 C CB  . VAL A 1 683 ? -26.668 -18.331 21.528 1.00 16.31 ? 683  VAL A CB  1 
ATOM   5440 C CG1 . VAL A 1 683 ? -26.649 -19.774 21.034 1.00 17.05 ? 683  VAL A CG1 1 
ATOM   5441 C CG2 . VAL A 1 683 ? -28.131 -17.847 21.635 1.00 18.43 ? 683  VAL A CG2 1 
ATOM   5442 N N   . LEU A 1 684 ? -24.488 -19.981 23.626 1.00 18.98 ? 684  LEU A N   1 
ATOM   5443 C CA  . LEU A 1 684 ? -23.205 -20.593 23.877 1.00 20.84 ? 684  LEU A CA  1 
ATOM   5444 C C   . LEU A 1 684 ? -23.138 -22.031 23.379 1.00 22.21 ? 684  LEU A C   1 
ATOM   5445 O O   . LEU A 1 684 ? -22.106 -22.696 23.548 1.00 22.34 ? 684  LEU A O   1 
ATOM   5446 C CB  . LEU A 1 684 ? -22.922 -20.555 25.377 1.00 19.99 ? 684  LEU A CB  1 
ATOM   5447 C CG  . LEU A 1 684 ? -22.675 -19.134 25.854 1.00 19.27 ? 684  LEU A CG  1 
ATOM   5448 C CD1 . LEU A 1 684 ? -22.658 -19.082 27.345 1.00 18.66 ? 684  LEU A CD1 1 
ATOM   5449 C CD2 . LEU A 1 684 ? -21.387 -18.534 25.278 1.00 16.14 ? 684  LEU A CD2 1 
ATOM   5450 N N   . ASP A 1 685 ? -24.241 -22.497 22.785 1.00 22.99 ? 685  ASP A N   1 
ATOM   5451 C CA  . ASP A 1 685 ? -24.383 -23.906 22.359 1.00 24.34 ? 685  ASP A CA  1 
ATOM   5452 C C   . ASP A 1 685 ? -24.560 -24.064 20.845 1.00 23.99 ? 685  ASP A C   1 
ATOM   5453 O O   . ASP A 1 685 ? -25.359 -23.347 20.249 1.00 22.56 ? 685  ASP A O   1 
ATOM   5454 C CB  . ASP A 1 685 ? -25.558 -24.530 23.096 1.00 25.29 ? 685  ASP A CB  1 
ATOM   5455 C CG  . ASP A 1 685 ? -25.333 -24.580 24.581 1.00 28.69 ? 685  ASP A CG  1 
ATOM   5456 O OD1 . ASP A 1 685 ? -24.297 -25.140 24.996 1.00 32.49 ? 685  ASP A OD1 1 
ATOM   5457 O OD2 . ASP A 1 685 ? -26.188 -24.064 25.336 1.00 33.11 ? 685  ASP A OD2 1 
ATOM   5458 N N   . GLU A 1 686 ? -23.799 -24.984 20.237 1.00 24.84 ? 686  GLU A N   1 
ATOM   5459 C CA  . GLU A 1 686 ? -23.841 -25.233 18.781 1.00 25.93 ? 686  GLU A CA  1 
ATOM   5460 C C   . GLU A 1 686 ? -25.246 -25.582 18.315 1.00 26.07 ? 686  GLU A C   1 
ATOM   5461 O O   . GLU A 1 686 ? -25.891 -26.449 18.893 1.00 26.15 ? 686  GLU A O   1 
ATOM   5462 C CB  . GLU A 1 686 ? -22.884 -26.356 18.363 1.00 26.00 ? 686  GLU A CB  1 
ATOM   5463 C CG  . GLU A 1 686 ? -22.656 -26.460 16.834 1.00 27.83 ? 686  GLU A CG  1 
ATOM   5464 C CD  . GLU A 1 686 ? -21.652 -27.555 16.406 1.00 28.64 ? 686  GLU A CD  1 
ATOM   5465 O OE1 . GLU A 1 686 ? -20.843 -27.990 17.247 1.00 30.14 ? 686  GLU A OE1 1 
ATOM   5466 O OE2 . GLU A 1 686 ? -21.684 -27.992 15.219 1.00 32.50 ? 686  GLU A OE2 1 
ATOM   5467 N N   . GLY A 1 687 ? -25.709 -24.901 17.271 1.00 26.35 ? 687  GLY A N   1 
ATOM   5468 C CA  . GLY A 1 687 ? -27.005 -25.206 16.667 1.00 27.14 ? 687  GLY A CA  1 
ATOM   5469 C C   . GLY A 1 687 ? -28.126 -24.443 17.322 1.00 27.36 ? 687  GLY A C   1 
ATOM   5470 O O   . GLY A 1 687 ? -29.261 -24.511 16.868 1.00 28.05 ? 687  GLY A O   1 
ATOM   5471 N N   . ALA A 1 688 ? -27.804 -23.709 18.389 1.00 27.09 ? 688  ALA A N   1 
ATOM   5472 C CA  . ALA A 1 688 ? -28.819 -23.078 19.233 1.00 26.80 ? 688  ALA A CA  1 
ATOM   5473 C C   . ALA A 1 688 ? -29.350 -21.724 18.749 1.00 26.70 ? 688  ALA A C   1 
ATOM   5474 O O   . ALA A 1 688 ? -28.599 -20.870 18.266 1.00 25.16 ? 688  ALA A O   1 
ATOM   5475 C CB  . ALA A 1 688 ? -28.330 -22.991 20.706 1.00 26.52 ? 688  ALA A CB  1 
ATOM   5476 N N   . GLU A 1 689 ? -30.665 -21.545 18.878 1.00 27.19 ? 689  GLU A N   1 
ATOM   5477 C CA  . GLU A 1 689 ? -31.292 -20.257 18.641 1.00 29.12 ? 689  GLU A CA  1 
ATOM   5478 C C   . GLU A 1 689 ? -32.144 -19.870 19.867 1.00 28.79 ? 689  GLU A C   1 
ATOM   5479 O O   . GLU A 1 689 ? -33.126 -19.112 19.795 1.00 27.60 ? 689  GLU A O   1 
ATOM   5480 C CB  . GLU A 1 689 ? -32.052 -20.231 17.306 1.00 29.75 ? 689  GLU A CB  1 
ATOM   5481 C CG  . GLU A 1 689 ? -31.131 -20.177 16.049 1.00 30.96 ? 689  GLU A CG  1 
ATOM   5482 C CD  . GLU A 1 689 ? -31.906 -20.011 14.727 1.00 33.13 ? 689  GLU A CD  1 
ATOM   5483 O OE1 . GLU A 1 689 ? -32.738 -20.902 14.421 1.00 36.31 ? 689  GLU A OE1 1 
ATOM   5484 O OE2 . GLU A 1 689 ? -31.661 -19.009 13.984 1.00 37.21 ? 689  GLU A OE2 1 
ATOM   5485 N N   . LYS A 1 690 ? -31.676 -20.381 20.998 1.00 28.92 ? 690  LYS A N   1 
ATOM   5486 C CA  . LYS A 1 690 ? -32.281 -20.246 22.299 1.00 30.07 ? 690  LYS A CA  1 
ATOM   5487 C C   . LYS A 1 690 ? -31.139 -20.269 23.308 1.00 30.35 ? 690  LYS A C   1 
ATOM   5488 O O   . LYS A 1 690 ? -30.110 -20.913 23.088 1.00 29.82 ? 690  LYS A O   1 
ATOM   5489 C CB  . LYS A 1 690 ? -33.180 -21.442 22.603 1.00 30.34 ? 690  LYS A CB  1 
ATOM   5490 C CG  . LYS A 1 690 ? -34.641 -21.314 22.154 1.00 33.40 ? 690  LYS A CG  1 
ATOM   5491 C CD  . LYS A 1 690 ? -35.305 -22.671 22.270 1.00 35.05 ? 690  LYS A CD  1 
ATOM   5492 C CE  . LYS A 1 690 ? -36.661 -22.718 21.576 1.00 39.12 ? 690  LYS A CE  1 
ATOM   5493 N NZ  . LYS A 1 690 ? -37.223 -24.119 21.572 1.00 38.30 ? 690  LYS A NZ  1 
ATOM   5494 N N   . VAL A 1 691 ? -31.322 -19.575 24.423 1.00 30.02 ? 691  VAL A N   1 
ATOM   5495 C CA  . VAL A 1 691 ? -30.406 -19.752 25.527 1.00 30.34 ? 691  VAL A CA  1 
ATOM   5496 C C   . VAL A 1 691 ? -31.243 -19.913 26.798 1.00 29.74 ? 691  VAL A C   1 
ATOM   5497 O O   . VAL A 1 691 ? -32.240 -19.201 26.991 1.00 29.10 ? 691  VAL A O   1 
ATOM   5498 C CB  . VAL A 1 691 ? -29.401 -18.592 25.593 1.00 29.91 ? 691  VAL A CB  1 
ATOM   5499 C CG1 . VAL A 1 691 ? -29.892 -17.505 26.499 1.00 31.73 ? 691  VAL A CG1 1 
ATOM   5500 C CG2 . VAL A 1 691 ? -28.061 -19.078 26.061 1.00 32.55 ? 691  VAL A CG2 1 
ATOM   5501 N N   . MET A 1 692 ? -30.871 -20.891 27.618 1.00 29.79 ? 692  MET A N   1 
ATOM   5502 C CA  . MET A 1 692 ? -31.424 -21.024 28.971 1.00 29.70 ? 692  MET A CA  1 
ATOM   5503 C C   . MET A 1 692 ? -30.686 -20.011 29.847 1.00 27.91 ? 692  MET A C   1 
ATOM   5504 O O   . MET A 1 692 ? -29.485 -20.136 30.080 1.00 28.16 ? 692  MET A O   1 
ATOM   5505 C CB  . MET A 1 692 ? -31.293 -22.458 29.505 1.00 31.31 ? 692  MET A CB  1 
ATOM   5506 C CG  . MET A 1 692 ? -32.386 -23.422 29.007 1.00 35.01 ? 692  MET A CG  1 
ATOM   5507 S SD  . MET A 1 692 ? -34.024 -23.134 29.776 1.00 44.92 ? 692  MET A SD  1 
ATOM   5508 C CE  . MET A 1 692 ? -35.109 -23.896 28.580 1.00 39.55 ? 692  MET A CE  1 
ATOM   5509 N N   . ALA A 1 693 ? -31.417 -19.005 30.306 1.00 25.63 ? 693  ALA A N   1 
ATOM   5510 C CA  . ALA A 1 693 ? -30.841 -17.825 30.936 1.00 24.25 ? 693  ALA A CA  1 
ATOM   5511 C C   . ALA A 1 693 ? -31.478 -17.532 32.268 1.00 23.59 ? 693  ALA A C   1 
ATOM   5512 O O   . ALA A 1 693 ? -32.628 -17.868 32.494 1.00 23.76 ? 693  ALA A O   1 
ATOM   5513 C CB  . ALA A 1 693 ? -30.992 -16.607 30.022 1.00 23.75 ? 693  ALA A CB  1 
ATOM   5514 N N   . TYR A 1 694 ? -30.728 -16.877 33.148 1.00 22.26 ? 694  TYR A N   1 
ATOM   5515 C CA  . TYR A 1 694 ? -31.302 -16.379 34.366 1.00 20.82 ? 694  TYR A CA  1 
ATOM   5516 C C   . TYR A 1 694 ? -31.618 -14.879 34.295 1.00 20.19 ? 694  TYR A C   1 
ATOM   5517 O O   . TYR A 1 694 ? -30.779 -14.051 33.926 1.00 20.64 ? 694  TYR A O   1 
ATOM   5518 C CB  . TYR A 1 694 ? -30.501 -16.814 35.610 1.00 20.89 ? 694  TYR A CB  1 
ATOM   5519 C CG  . TYR A 1 694 ? -31.290 -16.576 36.866 1.00 20.51 ? 694  TYR A CG  1 
ATOM   5520 C CD1 . TYR A 1 694 ? -32.397 -17.374 37.186 1.00 21.97 ? 694  TYR A CD1 1 
ATOM   5521 C CD2 . TYR A 1 694 ? -30.993 -15.513 37.688 1.00 20.49 ? 694  TYR A CD2 1 
ATOM   5522 C CE1 . TYR A 1 694 ? -33.152 -17.115 38.325 1.00 19.63 ? 694  TYR A CE1 1 
ATOM   5523 C CE2 . TYR A 1 694 ? -31.736 -15.253 38.824 1.00 19.63 ? 694  TYR A CE2 1 
ATOM   5524 C CZ  . TYR A 1 694 ? -32.798 -16.061 39.137 1.00 21.08 ? 694  TYR A CZ  1 
ATOM   5525 O OH  . TYR A 1 694 ? -33.509 -15.767 40.267 1.00 20.38 ? 694  TYR A OH  1 
ATOM   5526 N N   . VAL A 1 695 ? -32.869 -14.540 34.586 1.00 18.57 ? 695  VAL A N   1 
ATOM   5527 C CA  . VAL A 1 695 ? -33.253 -13.139 34.687 1.00 18.15 ? 695  VAL A CA  1 
ATOM   5528 C C   . VAL A 1 695 ? -33.357 -12.712 36.166 1.00 18.19 ? 695  VAL A C   1 
ATOM   5529 O O   . VAL A 1 695 ? -34.272 -13.132 36.876 1.00 18.05 ? 695  VAL A O   1 
ATOM   5530 C CB  . VAL A 1 695 ? -34.558 -12.832 33.922 1.00 17.84 ? 695  VAL A CB  1 
ATOM   5531 C CG1 . VAL A 1 695 ? -34.758 -11.369 33.844 1.00 16.04 ? 695  VAL A CG1 1 
ATOM   5532 C CG2 . VAL A 1 695 ? -34.531 -13.436 32.497 1.00 17.64 ? 695  VAL A CG2 1 
ATOM   5533 N N   . PRO A 1 696 ? -32.392 -11.911 36.643 1.00 18.37 ? 696  PRO A N   1 
ATOM   5534 C CA  . PRO A 1 696 ? -32.382 -11.442 38.024 1.00 18.82 ? 696  PRO A CA  1 
ATOM   5535 C C   . PRO A 1 696 ? -33.602 -10.645 38.494 1.00 20.30 ? 696  PRO A C   1 
ATOM   5536 O O   . PRO A 1 696 ? -34.484 -10.258 37.686 1.00 19.70 ? 696  PRO A O   1 
ATOM   5537 C CB  . PRO A 1 696 ? -31.114 -10.590 38.077 1.00 18.94 ? 696  PRO A CB  1 
ATOM   5538 C CG  . PRO A 1 696 ? -30.223 -11.219 37.057 1.00 18.58 ? 696  PRO A CG  1 
ATOM   5539 C CD  . PRO A 1 696 ? -31.185 -11.455 35.930 1.00 18.78 ? 696  PRO A CD  1 
ATOM   5540 N N   . ASP A 1 697 ? -33.641 -10.434 39.810 1.00 20.66 ? 697  ASP A N   1 
ATOM   5541 C CA  . ASP A 1 697 ? -34.699 -9.699  40.497 1.00 21.06 ? 697  ASP A CA  1 
ATOM   5542 C C   . ASP A 1 697 ? -34.634 -8.189  40.261 1.00 20.97 ? 697  ASP A C   1 
ATOM   5543 O O   . ASP A 1 697 ? -34.154 -7.424  41.110 1.00 21.31 ? 697  ASP A O   1 
ATOM   5544 C CB  . ASP A 1 697 ? -34.637 -10.019 41.993 1.00 21.62 ? 697  ASP A CB  1 
ATOM   5545 C CG  . ASP A 1 697 ? -35.905 -9.621  42.742 1.00 23.61 ? 697  ASP A CG  1 
ATOM   5546 O OD1 . ASP A 1 697 ? -36.861 -9.100  42.122 1.00 24.46 ? 697  ASP A OD1 1 
ATOM   5547 O OD2 . ASP A 1 697 ? -35.925 -9.811  43.974 1.00 25.87 ? 697  ASP A OD2 1 
ATOM   5548 N N   . ALA A 1 698 ? -35.139 -7.768  39.097 1.00 19.94 ? 698  ALA A N   1 
ATOM   5549 C CA  . ALA A 1 698 ? -35.138 -6.369  38.680 1.00 18.57 ? 698  ALA A CA  1 
ATOM   5550 C C   . ALA A 1 698 ? -36.086 -6.230  37.523 1.00 17.64 ? 698  ALA A C   1 
ATOM   5551 O O   . ALA A 1 698 ? -36.464 -7.208  36.898 1.00 18.53 ? 698  ALA A O   1 
ATOM   5552 C CB  . ALA A 1 698 ? -33.700 -5.916  38.228 1.00 17.95 ? 698  ALA A CB  1 
ATOM   5553 N N   . VAL A 1 699 ? -36.448 -5.003  37.221 1.00 17.86 ? 699  VAL A N   1 
ATOM   5554 C CA  . VAL A 1 699 ? -37.085 -4.673  35.951 1.00 18.41 ? 699  VAL A CA  1 
ATOM   5555 C C   . VAL A 1 699 ? -36.014 -4.719  34.860 1.00 17.72 ? 699  VAL A C   1 
ATOM   5556 O O   . VAL A 1 699 ? -34.977 -4.106  35.021 1.00 18.06 ? 699  VAL A O   1 
ATOM   5557 C CB  . VAL A 1 699 ? -37.647 -3.236  36.004 1.00 18.57 ? 699  VAL A CB  1 
ATOM   5558 C CG1 . VAL A 1 699 ? -38.140 -2.812  34.626 1.00 19.81 ? 699  VAL A CG1 1 
ATOM   5559 C CG2 . VAL A 1 699 ? -38.731 -3.144  37.047 1.00 20.01 ? 699  VAL A CG2 1 
ATOM   5560 N N   . TRP A 1 700 ? -36.258 -5.464  33.775 1.00 16.70 ? 700  TRP A N   1 
ATOM   5561 C CA  . TRP A 1 700 ? -35.358 -5.518  32.616 1.00 15.93 ? 700  TRP A CA  1 
ATOM   5562 C C   . TRP A 1 700 ? -36.081 -5.043  31.356 1.00 16.40 ? 700  TRP A C   1 
ATOM   5563 O O   . TRP A 1 700 ? -37.302 -5.281  31.195 1.00 15.48 ? 700  TRP A O   1 
ATOM   5564 C CB  . TRP A 1 700 ? -34.813 -6.931  32.410 1.00 15.42 ? 700  TRP A CB  1 
ATOM   5565 C CG  . TRP A 1 700 ? -33.969 -7.423  33.582 1.00 15.92 ? 700  TRP A CG  1 
ATOM   5566 C CD1 . TRP A 1 700 ? -34.372 -8.243  34.598 1.00 16.26 ? 700  TRP A CD1 1 
ATOM   5567 C CD2 . TRP A 1 700 ? -32.608 -7.088  33.855 1.00 15.78 ? 700  TRP A CD2 1 
ATOM   5568 N NE1 . TRP A 1 700 ? -33.337 -8.454  35.472 1.00 16.87 ? 700  TRP A NE1 1 
ATOM   5569 C CE2 . TRP A 1 700 ? -32.242 -7.753  35.039 1.00 16.01 ? 700  TRP A CE2 1 
ATOM   5570 C CE3 . TRP A 1 700 ? -31.646 -6.315  33.189 1.00 14.61 ? 700  TRP A CE3 1 
ATOM   5571 C CZ2 . TRP A 1 700 ? -30.956 -7.657  35.590 1.00 17.88 ? 700  TRP A CZ2 1 
ATOM   5572 C CZ3 . TRP A 1 700 ? -30.376 -6.217  33.729 1.00 15.60 ? 700  TRP A CZ3 1 
ATOM   5573 C CH2 . TRP A 1 700 ? -30.034 -6.887  34.919 1.00 17.06 ? 700  TRP A CH2 1 
ATOM   5574 N N   . TYR A 1 701 ? -35.342 -4.322  30.512 1.00 15.51 ? 701  TYR A N   1 
ATOM   5575 C CA  . TYR A 1 701 ? -35.798 -3.853  29.205 1.00 15.16 ? 701  TYR A CA  1 
ATOM   5576 C C   . TYR A 1 701 ? -34.906 -4.367  28.110 1.00 16.77 ? 701  TYR A C   1 
ATOM   5577 O O   . TYR A 1 701 ? -33.666 -4.288  28.197 1.00 16.31 ? 701  TYR A O   1 
ATOM   5578 C CB  . TYR A 1 701 ? -35.784 -2.332  29.129 1.00 13.94 ? 701  TYR A CB  1 
ATOM   5579 C CG  . TYR A 1 701 ? -36.573 -1.618  30.190 1.00 14.20 ? 701  TYR A CG  1 
ATOM   5580 C CD1 . TYR A 1 701 ? -37.951 -1.397  30.022 1.00 14.90 ? 701  TYR A CD1 1 
ATOM   5581 C CD2 . TYR A 1 701 ? -35.976 -1.190  31.369 1.00 14.62 ? 701  TYR A CD2 1 
ATOM   5582 C CE1 . TYR A 1 701 ? -38.690 -0.717  30.990 1.00 13.46 ? 701  TYR A CE1 1 
ATOM   5583 C CE2 . TYR A 1 701 ? -36.705 -0.541  32.343 1.00 14.02 ? 701  TYR A CE2 1 
ATOM   5584 C CZ  . TYR A 1 701 ? -38.089 -0.325  32.138 1.00 13.99 ? 701  TYR A CZ  1 
ATOM   5585 O OH  . TYR A 1 701 ? -38.843 0.337   33.072 1.00 12.36 ? 701  TYR A OH  1 
ATOM   5586 N N   . ASP A 1 702 ? -35.526 -4.875  27.057 1.00 17.76 ? 702  ASP A N   1 
ATOM   5587 C CA  . ASP A 1 702 ? -34.794 -5.212  25.854 1.00 19.09 ? 702  ASP A CA  1 
ATOM   5588 C C   . ASP A 1 702 ? -34.061 -3.980  25.319 1.00 19.40 ? 702  ASP A C   1 
ATOM   5589 O O   . ASP A 1 702 ? -34.669 -2.924  25.064 1.00 18.10 ? 702  ASP A O   1 
ATOM   5590 C CB  . ASP A 1 702 ? -35.738 -5.784  24.810 1.00 19.83 ? 702  ASP A CB  1 
ATOM   5591 C CG  . ASP A 1 702 ? -35.019 -6.235  23.557 1.00 23.17 ? 702  ASP A CG  1 
ATOM   5592 O OD1 . ASP A 1 702 ? -34.740 -7.440  23.463 1.00 29.87 ? 702  ASP A OD1 1 
ATOM   5593 O OD2 . ASP A 1 702 ? -34.721 -5.395  22.686 1.00 25.58 ? 702  ASP A OD2 1 
ATOM   5594 N N   . TYR A 1 703 ? -32.753 -4.127  25.118 1.00 18.90 ? 703  TYR A N   1 
ATOM   5595 C CA  . TYR A 1 703 ? -31.928 -2.996  24.727 1.00 19.29 ? 703  TYR A CA  1 
ATOM   5596 C C   . TYR A 1 703 ? -32.384 -2.346  23.419 1.00 20.10 ? 703  TYR A C   1 
ATOM   5597 O O   . TYR A 1 703 ? -32.490 -1.135  23.354 1.00 21.37 ? 703  TYR A O   1 
ATOM   5598 C CB  . TYR A 1 703 ? -30.429 -3.353  24.669 1.00 18.98 ? 703  TYR A CB  1 
ATOM   5599 C CG  . TYR A 1 703 ? -29.618 -2.221  24.108 1.00 19.51 ? 703  TYR A CG  1 
ATOM   5600 C CD1 . TYR A 1 703 ? -29.108 -1.227  24.931 1.00 17.56 ? 703  TYR A CD1 1 
ATOM   5601 C CD2 . TYR A 1 703 ? -29.405 -2.115  22.724 1.00 19.11 ? 703  TYR A CD2 1 
ATOM   5602 C CE1 . TYR A 1 703 ? -28.372 -0.174  24.409 1.00 19.03 ? 703  TYR A CE1 1 
ATOM   5603 C CE2 . TYR A 1 703 ? -28.697 -1.058  22.194 1.00 18.98 ? 703  TYR A CE2 1 
ATOM   5604 C CZ  . TYR A 1 703 ? -28.192 -0.091  23.040 1.00 19.03 ? 703  TYR A CZ  1 
ATOM   5605 O OH  . TYR A 1 703 ? -27.485 0.959   22.522 1.00 21.60 ? 703  TYR A OH  1 
ATOM   5606 N N   . GLU A 1 704 ? -32.653 -3.135  22.388 1.00 21.26 ? 704  GLU A N   1 
ATOM   5607 C CA  . GLU A 1 704 ? -32.988 -2.585  21.063 1.00 22.89 ? 704  GLU A CA  1 
ATOM   5608 C C   . GLU A 1 704 ? -34.407 -2.029  20.929 1.00 22.87 ? 704  GLU A C   1 
ATOM   5609 O O   . GLU A 1 704 ? -34.597 -0.949  20.396 1.00 23.23 ? 704  GLU A O   1 
ATOM   5610 C CB  . GLU A 1 704 ? -32.735 -3.628  19.984 1.00 23.54 ? 704  GLU A CB  1 
ATOM   5611 C CG  . GLU A 1 704 ? -31.255 -4.011  19.919 1.00 27.15 ? 704  GLU A CG  1 
ATOM   5612 C CD  . GLU A 1 704 ? -30.825 -4.317  18.519 1.00 30.16 ? 704  GLU A CD  1 
ATOM   5613 O OE1 . GLU A 1 704 ? -30.945 -3.418  17.633 1.00 30.40 ? 704  GLU A OE1 1 
ATOM   5614 O OE2 . GLU A 1 704 ? -30.370 -5.461  18.322 1.00 29.76 ? 704  GLU A OE2 1 
ATOM   5615 N N   . THR A 1 705 ? -35.396 -2.756  21.429 1.00 23.57 ? 705  THR A N   1 
ATOM   5616 C CA  . THR A 1 705 ? -36.783 -2.279  21.349 1.00 23.58 ? 705  THR A CA  1 
ATOM   5617 C C   . THR A 1 705 ? -37.133 -1.335  22.497 1.00 23.20 ? 705  THR A C   1 
ATOM   5618 O O   . THR A 1 705 ? -37.915 -0.408  22.321 1.00 24.05 ? 705  THR A O   1 
ATOM   5619 C CB  . THR A 1 705 ? -37.766 -3.449  21.284 1.00 23.62 ? 705  THR A CB  1 
ATOM   5620 O OG1 . THR A 1 705 ? -37.697 -4.196  22.501 1.00 24.44 ? 705  THR A OG1 1 
ATOM   5621 C CG2 . THR A 1 705 ? -37.415 -4.370  20.119 1.00 24.99 ? 705  THR A CG2 1 
ATOM   5622 N N   . GLY A 1 706 ? -36.537 -1.556  23.668 1.00 22.53 ? 706  GLY A N   1 
ATOM   5623 C CA  . GLY A 1 706 ? -36.851 -0.772  24.843 1.00 22.10 ? 706  GLY A CA  1 
ATOM   5624 C C   . GLY A 1 706 ? -38.017 -1.358  25.634 1.00 22.50 ? 706  GLY A C   1 
ATOM   5625 O O   . GLY A 1 706 ? -38.383 -0.820  26.665 1.00 22.05 ? 706  GLY A O   1 
ATOM   5626 N N   . SER A 1 707 ? -38.597 -2.457  25.150 1.00 22.76 ? 707  SER A N   1 
ATOM   5627 C CA  . SER A 1 707 ? -39.734 -3.089  25.825 1.00 23.17 ? 707  SER A CA  1 
ATOM   5628 C C   . SER A 1 707 ? -39.367 -3.832  27.095 1.00 23.42 ? 707  SER A C   1 
ATOM   5629 O O   . SER A 1 707 ? -38.332 -4.526  27.167 1.00 22.31 ? 707  SER A O   1 
ATOM   5630 C CB  . SER A 1 707 ? -40.463 -4.036  24.895 1.00 23.48 ? 707  SER A CB  1 
ATOM   5631 O OG  . SER A 1 707 ? -39.698 -5.186  24.673 1.00 27.79 ? 707  SER A OG  1 
ATOM   5632 N N   . GLN A 1 708 ? -40.230 -3.690  28.094 1.00 23.65 ? 708  GLN A N   1 
ATOM   5633 C CA  . GLN A 1 708 ? -40.038 -4.343  29.392 1.00 25.07 ? 708  GLN A CA  1 
ATOM   5634 C C   . GLN A 1 708 ? -40.370 -5.826  29.305 1.00 25.73 ? 708  GLN A C   1 
ATOM   5635 O O   . GLN A 1 708 ? -41.507 -6.214  28.986 1.00 26.08 ? 708  GLN A O   1 
ATOM   5636 C CB  . GLN A 1 708 ? -40.881 -3.655  30.467 1.00 25.57 ? 708  GLN A CB  1 
ATOM   5637 C CG  . GLN A 1 708 ? -40.553 -4.051  31.903 1.00 24.73 ? 708  GLN A CG  1 
ATOM   5638 C CD  . GLN A 1 708 ? -41.616 -3.547  32.896 1.00 26.04 ? 708  GLN A CD  1 
ATOM   5639 O OE1 . GLN A 1 708 ? -42.176 -2.465  32.731 1.00 25.03 ? 708  GLN A OE1 1 
ATOM   5640 N NE2 . GLN A 1 708 ? -41.866 -4.330  33.946 1.00 26.97 ? 708  GLN A NE2 1 
ATOM   5641 N N   . VAL A 1 709 ? -39.375 -6.660  29.585 1.00 25.42 ? 709  VAL A N   1 
ATOM   5642 C CA  . VAL A 1 709 ? -39.587 -8.097  29.627 1.00 26.25 ? 709  VAL A CA  1 
ATOM   5643 C C   . VAL A 1 709 ? -40.566 -8.424  30.753 1.00 26.83 ? 709  VAL A C   1 
ATOM   5644 O O   . VAL A 1 709 ? -40.671 -7.678  31.727 1.00 25.73 ? 709  VAL A O   1 
ATOM   5645 C CB  . VAL A 1 709 ? -38.269 -8.894  29.774 1.00 26.23 ? 709  VAL A CB  1 
ATOM   5646 C CG1 . VAL A 1 709 ? -37.283 -8.439  28.721 1.00 25.61 ? 709  VAL A CG1 1 
ATOM   5647 C CG2 . VAL A 1 709 ? -37.661 -8.753  31.188 1.00 24.60 ? 709  VAL A CG2 1 
ATOM   5648 N N   . ARG A 1 710 ? -41.304 -9.519  30.613 1.00 28.18 ? 710  ARG A N   1 
ATOM   5649 C CA  . ARG A 1 710 ? -42.199 -9.912  31.703 1.00 30.03 ? 710  ARG A CA  1 
ATOM   5650 C C   . ARG A 1 710 ? -41.465 -10.785 32.733 1.00 29.55 ? 710  ARG A C   1 
ATOM   5651 O O   . ARG A 1 710 ? -41.897 -10.923 33.887 1.00 30.89 ? 710  ARG A O   1 
ATOM   5652 C CB  . ARG A 1 710 ? -43.498 -10.534 31.178 1.00 31.82 ? 710  ARG A CB  1 
ATOM   5653 C CG  . ARG A 1 710 ? -44.531 -9.506  30.624 1.00 34.42 ? 710  ARG A CG  1 
ATOM   5654 C CD  . ARG A 1 710 ? -44.744 -8.288  31.563 1.00 40.40 ? 710  ARG A CD  1 
ATOM   5655 N NE  . ARG A 1 710 ? -45.714 -7.303  31.048 1.00 42.70 ? 710  ARG A NE  1 
ATOM   5656 C CZ  . ARG A 1 710 ? -45.697 -5.992  31.322 1.00 46.42 ? 710  ARG A CZ  1 
ATOM   5657 N NH1 . ARG A 1 710 ? -44.742 -5.470  32.092 1.00 47.71 ? 710  ARG A NH1 1 
ATOM   5658 N NH2 . ARG A 1 710 ? -46.637 -5.192  30.815 1.00 46.48 ? 710  ARG A NH2 1 
ATOM   5659 N N   . TRP A 1 711 ? -40.319 -11.320 32.343 1.00 28.17 ? 711  TRP A N   1 
ATOM   5660 C CA  . TRP A 1 711 ? -39.513 -12.107 33.278 1.00 26.91 ? 711  TRP A CA  1 
ATOM   5661 C C   . TRP A 1 711 ? -38.937 -11.263 34.407 1.00 25.78 ? 711  TRP A C   1 
ATOM   5662 O O   . TRP A 1 711 ? -38.490 -10.147 34.185 1.00 25.83 ? 711  TRP A O   1 
ATOM   5663 C CB  . TRP A 1 711 ? -38.384 -12.836 32.564 1.00 26.82 ? 711  TRP A CB  1 
ATOM   5664 C CG  . TRP A 1 711 ? -38.717 -13.417 31.223 1.00 27.61 ? 711  TRP A CG  1 
ATOM   5665 C CD1 . TRP A 1 711 ? -39.745 -14.275 30.913 1.00 27.77 ? 711  TRP A CD1 1 
ATOM   5666 C CD2 . TRP A 1 711 ? -37.972 -13.231 30.012 1.00 27.85 ? 711  TRP A CD2 1 
ATOM   5667 N NE1 . TRP A 1 711 ? -39.692 -14.599 29.583 1.00 28.33 ? 711  TRP A NE1 1 
ATOM   5668 C CE2 . TRP A 1 711 ? -38.611 -13.979 29.011 1.00 28.73 ? 711  TRP A CE2 1 
ATOM   5669 C CE3 . TRP A 1 711 ? -36.832 -12.483 29.677 1.00 27.84 ? 711  TRP A CE3 1 
ATOM   5670 C CZ2 . TRP A 1 711 ? -38.148 -14.008 27.688 1.00 29.24 ? 711  TRP A CZ2 1 
ATOM   5671 C CZ3 . TRP A 1 711 ? -36.374 -12.516 28.375 1.00 28.33 ? 711  TRP A CZ3 1 
ATOM   5672 C CH2 . TRP A 1 711 ? -37.036 -13.263 27.391 1.00 27.87 ? 711  TRP A CH2 1 
ATOM   5673 N N   . ARG A 1 712 ? -38.949 -11.826 35.616 1.00 25.05 ? 712  ARG A N   1 
ATOM   5674 C CA  . ARG A 1 712 ? -38.275 -11.276 36.790 1.00 24.48 ? 712  ARG A CA  1 
ATOM   5675 C C   . ARG A 1 712 ? -37.964 -12.406 37.789 1.00 23.82 ? 712  ARG A C   1 
ATOM   5676 O O   . ARG A 1 712 ? -38.863 -13.156 38.211 1.00 22.66 ? 712  ARG A O   1 
ATOM   5677 C CB  . ARG A 1 712 ? -39.139 -10.196 37.468 1.00 25.77 ? 712  ARG A CB  1 
ATOM   5678 C CG  . ARG A 1 712 ? -38.465 -9.580  38.677 1.00 24.91 ? 712  ARG A CG  1 
ATOM   5679 C CD  . ARG A 1 712 ? -39.076 -8.278  39.053 1.00 29.09 ? 712  ARG A CD  1 
ATOM   5680 N NE  . ARG A 1 712 ? -38.305 -7.665  40.125 1.00 29.02 ? 712  ARG A NE  1 
ATOM   5681 C CZ  . ARG A 1 712 ? -38.354 -6.381  40.447 1.00 30.53 ? 712  ARG A CZ  1 
ATOM   5682 N NH1 . ARG A 1 712 ? -39.133 -5.558  39.766 1.00 32.33 ? 712  ARG A NH1 1 
ATOM   5683 N NH2 . ARG A 1 712 ? -37.604 -5.916  41.440 1.00 30.68 ? 712  ARG A NH2 1 
ATOM   5684 N N   . LYS A 1 713 ? -36.686 -12.535 38.152 1.00 22.34 ? 713  LYS A N   1 
ATOM   5685 C CA  . LYS A 1 713 ? -36.219 -13.532 39.138 1.00 21.87 ? 713  LYS A CA  1 
ATOM   5686 C C   . LYS A 1 713 ? -36.592 -14.973 38.767 1.00 22.17 ? 713  LYS A C   1 
ATOM   5687 O O   . LYS A 1 713 ? -37.259 -15.684 39.519 1.00 22.16 ? 713  LYS A O   1 
ATOM   5688 C CB  . LYS A 1 713 ? -36.656 -13.163 40.573 1.00 21.07 ? 713  LYS A CB  1 
ATOM   5689 C CG  . LYS A 1 713 ? -35.760 -13.738 41.703 1.00 22.18 ? 713  LYS A CG  1 
ATOM   5690 C CD  . LYS A 1 713 ? -36.308 -13.430 43.122 1.00 20.73 ? 713  LYS A CD  1 
ATOM   5691 C CE  . LYS A 1 713 ? -35.411 -14.051 44.197 1.00 21.79 ? 713  LYS A CE  1 
ATOM   5692 N NZ  . LYS A 1 713 ? -35.722 -13.679 45.610 1.00 21.52 ? 713  LYS A NZ  1 
ATOM   5693 N N   . GLN A 1 714 ? -36.121 -15.420 37.613 1.00 22.20 ? 714  GLN A N   1 
ATOM   5694 C CA  . GLN A 1 714 ? -36.495 -16.740 37.118 1.00 22.49 ? 714  GLN A CA  1 
ATOM   5695 C C   . GLN A 1 714 ? -35.603 -17.161 35.972 1.00 22.97 ? 714  GLN A C   1 
ATOM   5696 O O   . GLN A 1 714 ? -35.059 -16.300 35.281 1.00 22.47 ? 714  GLN A O   1 
ATOM   5697 C CB  . GLN A 1 714 ? -37.952 -16.703 36.617 1.00 22.04 ? 714  GLN A CB  1 
ATOM   5698 C CG  . GLN A 1 714 ? -38.218 -15.680 35.511 1.00 20.37 ? 714  GLN A CG  1 
ATOM   5699 C CD  . GLN A 1 714 ? -39.709 -15.625 35.166 1.00 22.49 ? 714  GLN A CD  1 
ATOM   5700 O OE1 . GLN A 1 714 ? -40.257 -16.587 34.647 1.00 25.37 ? 714  GLN A OE1 1 
ATOM   5701 N NE2 . GLN A 1 714 ? -40.363 -14.525 35.499 1.00 20.95 ? 714  GLN A NE2 1 
ATOM   5702 N N   . LYS A 1 715 ? -35.481 -18.472 35.767 1.00 23.87 ? 715  LYS A N   1 
ATOM   5703 C CA  . LYS A 1 715 ? -34.850 -19.036 34.571 1.00 26.35 ? 715  LYS A CA  1 
ATOM   5704 C C   . LYS A 1 715 ? -35.802 -18.937 33.399 1.00 26.86 ? 715  LYS A C   1 
ATOM   5705 O O   . LYS A 1 715 ? -37.007 -19.140 33.559 1.00 27.65 ? 715  LYS A O   1 
ATOM   5706 C CB  . LYS A 1 715 ? -34.471 -20.502 34.779 1.00 26.58 ? 715  LYS A CB  1 
ATOM   5707 C CG  . LYS A 1 715 ? -33.466 -20.712 35.872 1.00 29.90 ? 715  LYS A CG  1 
ATOM   5708 C CD  . LYS A 1 715 ? -33.643 -22.074 36.546 1.00 33.51 ? 715  LYS A CD  1 
ATOM   5709 C CE  . LYS A 1 715 ? -32.592 -22.247 37.637 1.00 34.59 ? 715  LYS A CE  1 
ATOM   5710 N NZ  . LYS A 1 715 ? -32.369 -20.968 38.398 1.00 32.38 ? 715  LYS A NZ  1 
ATOM   5711 N N   . VAL A 1 716 ? -35.268 -18.603 32.231 1.00 27.52 ? 716  VAL A N   1 
ATOM   5712 C CA  . VAL A 1 716 ? -36.070 -18.468 31.024 1.00 28.15 ? 716  VAL A CA  1 
ATOM   5713 C C   . VAL A 1 716 ? -35.383 -19.117 29.834 1.00 28.55 ? 716  VAL A C   1 
ATOM   5714 O O   . VAL A 1 716 ? -34.159 -19.311 29.829 1.00 29.40 ? 716  VAL A O   1 
ATOM   5715 C CB  . VAL A 1 716 ? -36.400 -16.967 30.689 1.00 28.50 ? 716  VAL A CB  1 
ATOM   5716 C CG1 . VAL A 1 716 ? -37.045 -16.269 31.869 1.00 28.88 ? 716  VAL A CG1 1 
ATOM   5717 C CG2 . VAL A 1 716 ? -35.173 -16.203 30.260 1.00 27.70 ? 716  VAL A CG2 1 
ATOM   5718 N N   . GLU A 1 717 ? -36.172 -19.444 28.821 1.00 29.01 ? 717  GLU A N   1 
ATOM   5719 C CA  . GLU A 1 717 ? -35.649 -19.812 27.515 1.00 30.51 ? 717  GLU A CA  1 
ATOM   5720 C C   . GLU A 1 717 ? -35.698 -18.544 26.668 1.00 29.06 ? 717  GLU A C   1 
ATOM   5721 O O   . GLU A 1 717 ? -36.767 -18.158 26.192 1.00 28.86 ? 717  GLU A O   1 
ATOM   5722 C CB  . GLU A 1 717 ? -36.500 -20.922 26.898 1.00 30.34 ? 717  GLU A CB  1 
ATOM   5723 C CG  . GLU A 1 717 ? -35.812 -21.742 25.829 1.00 33.68 ? 717  GLU A CG  1 
ATOM   5724 C CD  . GLU A 1 717 ? -36.650 -22.933 25.372 1.00 34.81 ? 717  GLU A CD  1 
ATOM   5725 O OE1 . GLU A 1 717 ? -37.858 -22.746 25.050 1.00 41.72 ? 717  GLU A OE1 1 
ATOM   5726 O OE2 . GLU A 1 717 ? -36.099 -24.059 25.316 1.00 40.39 ? 717  GLU A OE2 1 
ATOM   5727 N N   . MET A 1 718 ? -34.553 -17.865 26.534 1.00 27.30 ? 718  MET A N   1 
ATOM   5728 C CA  . MET A 1 718 ? -34.488 -16.622 25.764 1.00 26.86 ? 718  MET A CA  1 
ATOM   5729 C C   . MET A 1 718 ? -34.348 -16.985 24.291 1.00 26.27 ? 718  MET A C   1 
ATOM   5730 O O   . MET A 1 718 ? -33.456 -17.758 23.937 1.00 26.05 ? 718  MET A O   1 
ATOM   5731 C CB  . MET A 1 718 ? -33.293 -15.776 26.216 1.00 26.60 ? 718  MET A CB  1 
ATOM   5732 C CG  . MET A 1 718 ? -33.398 -14.306 25.907 1.00 27.10 ? 718  MET A CG  1 
ATOM   5733 S SD  . MET A 1 718 ? -32.087 -13.360 26.714 1.00 27.63 ? 718  MET A SD  1 
ATOM   5734 C CE  . MET A 1 718 ? -32.725 -13.127 28.381 1.00 24.71 ? 718  MET A CE  1 
ATOM   5735 N N   . GLU A 1 719 ? -35.222 -16.444 23.441 1.00 25.51 ? 719  GLU A N   1 
ATOM   5736 C CA  . GLU A 1 719 ? -35.186 -16.762 22.004 1.00 25.81 ? 719  GLU A CA  1 
ATOM   5737 C C   . GLU A 1 719 ? -34.123 -15.885 21.377 1.00 23.99 ? 719  GLU A C   1 
ATOM   5738 O O   . GLU A 1 719 ? -34.244 -14.670 21.369 1.00 24.14 ? 719  GLU A O   1 
ATOM   5739 C CB  . GLU A 1 719 ? -36.515 -16.461 21.309 1.00 26.38 ? 719  GLU A CB  1 
ATOM   5740 C CG  . GLU A 1 719 ? -37.742 -16.948 22.046 1.00 31.70 ? 719  GLU A CG  1 
ATOM   5741 C CD  . GLU A 1 719 ? -38.218 -18.290 21.572 1.00 39.69 ? 719  GLU A CD  1 
ATOM   5742 O OE1 . GLU A 1 719 ? -37.395 -19.235 21.530 1.00 42.27 ? 719  GLU A OE1 1 
ATOM   5743 O OE2 . GLU A 1 719 ? -39.434 -18.398 21.251 1.00 43.82 ? 719  GLU A OE2 1 
ATOM   5744 N N   . LEU A 1 720 ? -33.077 -16.504 20.869 1.00 23.61 ? 720  LEU A N   1 
ATOM   5745 C CA  . LEU A 1 720 ? -31.973 -15.744 20.289 1.00 22.91 ? 720  LEU A CA  1 
ATOM   5746 C C   . LEU A 1 720 ? -31.560 -16.340 18.955 1.00 22.02 ? 720  LEU A C   1 
ATOM   5747 O O   . LEU A 1 720 ? -30.679 -17.202 18.900 1.00 21.72 ? 720  LEU A O   1 
ATOM   5748 C CB  . LEU A 1 720 ? -30.796 -15.636 21.254 1.00 23.09 ? 720  LEU A CB  1 
ATOM   5749 C CG  . LEU A 1 720 ? -31.077 -14.908 22.565 1.00 24.21 ? 720  LEU A CG  1 
ATOM   5750 C CD1 . LEU A 1 720 ? -29.921 -15.128 23.545 1.00 22.81 ? 720  LEU A CD1 1 
ATOM   5751 C CD2 . LEU A 1 720 ? -31.352 -13.427 22.331 1.00 23.25 ? 720  LEU A CD2 1 
ATOM   5752 N N   . PRO A 1 721 ? -32.202 -15.866 17.871 1.00 21.56 ? 721  PRO A N   1 
ATOM   5753 C CA  . PRO A 1 721 ? -31.935 -16.333 16.518 1.00 21.28 ? 721  PRO A CA  1 
ATOM   5754 C C   . PRO A 1 721 ? -30.465 -16.062 16.174 1.00 20.58 ? 721  PRO A C   1 
ATOM   5755 O O   . PRO A 1 721 ? -29.778 -15.420 16.962 1.00 19.18 ? 721  PRO A O   1 
ATOM   5756 C CB  . PRO A 1 721 ? -32.862 -15.468 15.661 1.00 21.95 ? 721  PRO A CB  1 
ATOM   5757 C CG  . PRO A 1 721 ? -33.941 -15.005 16.573 1.00 22.03 ? 721  PRO A CG  1 
ATOM   5758 C CD  . PRO A 1 721 ? -33.267 -14.843 17.905 1.00 22.54 ? 721  PRO A CD  1 
ATOM   5759 N N   . GLY A 1 722 ? -30.003 -16.539 15.017 1.00 20.08 ? 722  GLY A N   1 
ATOM   5760 C CA  . GLY A 1 722 ? -28.588 -16.450 14.654 1.00 20.95 ? 722  GLY A CA  1 
ATOM   5761 C C   . GLY A 1 722 ? -28.014 -15.057 14.624 1.00 20.62 ? 722  GLY A C   1 
ATOM   5762 O O   . GLY A 1 722 ? -26.800 -14.897 14.728 1.00 22.05 ? 722  GLY A O   1 
ATOM   5763 N N   . ASP A 1 723 ? -28.881 -14.044 14.480 1.00 20.78 ? 723  ASP A N   1 
ATOM   5764 C CA  . ASP A 1 723 ? -28.449 -12.646 14.426 1.00 20.28 ? 723  ASP A CA  1 
ATOM   5765 C C   . ASP A 1 723 ? -28.536 -11.920 15.774 1.00 19.29 ? 723  ASP A C   1 
ATOM   5766 O O   . ASP A 1 723 ? -28.373 -10.708 15.831 1.00 19.32 ? 723  ASP A O   1 
ATOM   5767 C CB  . ASP A 1 723 ? -29.193 -11.854 13.323 1.00 20.86 ? 723  ASP A CB  1 
ATOM   5768 C CG  . ASP A 1 723 ? -30.724 -11.769 13.559 1.00 23.55 ? 723  ASP A CG  1 
ATOM   5769 O OD1 . ASP A 1 723 ? -31.284 -12.575 14.341 1.00 22.40 ? 723  ASP A OD1 1 
ATOM   5770 O OD2 . ASP A 1 723 ? -31.356 -10.871 12.963 1.00 26.57 ? 723  ASP A OD2 1 
ATOM   5771 N N   . LYS A 1 724 ? -28.783 -12.640 16.869 1.00 18.77 ? 724  LYS A N   1 
ATOM   5772 C CA  . LYS A 1 724 ? -29.006 -11.953 18.144 1.00 17.74 ? 724  LYS A CA  1 
ATOM   5773 C C   . LYS A 1 724 ? -28.185 -12.485 19.323 1.00 17.24 ? 724  LYS A C   1 
ATOM   5774 O O   . LYS A 1 724 ? -27.837 -13.662 19.375 1.00 16.07 ? 724  LYS A O   1 
ATOM   5775 C CB  . LYS A 1 724 ? -30.504 -11.981 18.538 1.00 19.33 ? 724  LYS A CB  1 
ATOM   5776 C CG  . LYS A 1 724 ? -31.442 -11.361 17.519 1.00 18.83 ? 724  LYS A CG  1 
ATOM   5777 C CD  . LYS A 1 724 ? -31.393 -9.846  17.528 1.00 20.46 ? 724  LYS A CD  1 
ATOM   5778 C CE  . LYS A 1 724 ? -32.426 -9.292  16.528 1.00 24.93 ? 724  LYS A CE  1 
ATOM   5779 N NZ  . LYS A 1 724 ? -32.025 -7.952  15.971 1.00 28.24 ? 724  LYS A NZ  1 
ATOM   5780 N N   . ILE A 1 725 ? -27.898 -11.572 20.246 1.00 16.40 ? 725  ILE A N   1 
ATOM   5781 C CA  . ILE A 1 725 ? -27.434 -11.883 21.571 1.00 16.94 ? 725  ILE A CA  1 
ATOM   5782 C C   . ILE A 1 725 ? -28.379 -11.147 22.505 1.00 16.65 ? 725  ILE A C   1 
ATOM   5783 O O   . ILE A 1 725 ? -28.926 -10.110 22.138 1.00 17.61 ? 725  ILE A O   1 
ATOM   5784 C CB  . ILE A 1 725 ? -25.914 -11.492 21.786 1.00 16.44 ? 725  ILE A CB  1 
ATOM   5785 C CG1 . ILE A 1 725 ? -25.485 -11.701 23.229 1.00 16.05 ? 725  ILE A CG1 1 
ATOM   5786 C CG2 . ILE A 1 725 ? -25.618 -10.070 21.392 1.00 15.99 ? 725  ILE A CG2 1 
ATOM   5787 C CD1 . ILE A 1 725 ? -23.962 -11.739 23.415 1.00 17.36 ? 725  ILE A CD1 1 
ATOM   5788 N N   . GLY A 1 726 ? -28.604 -11.699 23.690 1.00 16.38 ? 726  GLY A N   1 
ATOM   5789 C CA  . GLY A 1 726 ? -29.456 -11.037 24.682 1.00 16.26 ? 726  GLY A CA  1 
ATOM   5790 C C   . GLY A 1 726 ? -28.756 -9.845  25.296 1.00 15.73 ? 726  GLY A C   1 
ATOM   5791 O O   . GLY A 1 726 ? -27.656 -9.977  25.821 1.00 16.58 ? 726  GLY A O   1 
ATOM   5792 N N   . LEU A 1 727 ? -29.381 -8.676  25.214 1.00 15.96 ? 727  LEU A N   1 
ATOM   5793 C CA  . LEU A 1 727 ? -28.905 -7.490  25.892 1.00 16.38 ? 727  LEU A CA  1 
ATOM   5794 C C   . LEU A 1 727 ? -30.086 -6.856  26.602 1.00 16.51 ? 727  LEU A C   1 
ATOM   5795 O O   . LEU A 1 727 ? -31.029 -6.418  25.920 1.00 16.58 ? 727  LEU A O   1 
ATOM   5796 C CB  . LEU A 1 727 ? -28.304 -6.497  24.889 1.00 15.48 ? 727  LEU A CB  1 
ATOM   5797 C CG  . LEU A 1 727 ? -27.040 -6.931  24.138 1.00 17.68 ? 727  LEU A CG  1 
ATOM   5798 C CD1 . LEU A 1 727 ? -26.733 -5.862  23.111 1.00 16.10 ? 727  LEU A CD1 1 
ATOM   5799 C CD2 . LEU A 1 727 ? -25.873 -7.104  25.130 1.00 15.13 ? 727  LEU A CD2 1 
ATOM   5800 N N   . HIS A 1 728 ? -30.049 -6.790  27.944 1.00 16.09 ? 728  HIS A N   1 
ATOM   5801 C CA  . HIS A 1 728 ? -31.113 -6.074  28.704 1.00 15.23 ? 728  HIS A CA  1 
ATOM   5802 C C   . HIS A 1 728 ? -30.591 -5.011  29.650 1.00 15.32 ? 728  HIS A C   1 
ATOM   5803 O O   . HIS A 1 728 ? -29.555 -5.183  30.281 1.00 16.35 ? 728  HIS A O   1 
ATOM   5804 C CB  . HIS A 1 728 ? -32.035 -7.060  29.462 1.00 15.55 ? 728  HIS A CB  1 
ATOM   5805 C CG  . HIS A 1 728 ? -32.715 -8.029  28.557 1.00 15.65 ? 728  HIS A CG  1 
ATOM   5806 N ND1 . HIS A 1 728 ? -32.082 -9.142  28.053 1.00 17.10 ? 728  HIS A ND1 1 
ATOM   5807 C CD2 . HIS A 1 728 ? -33.959 -8.016  28.009 1.00 18.89 ? 728  HIS A CD2 1 
ATOM   5808 C CE1 . HIS A 1 728 ? -32.905 -9.785  27.247 1.00 19.23 ? 728  HIS A CE1 1 
ATOM   5809 N NE2 . HIS A 1 728 ? -34.050 -9.120  27.199 1.00 20.05 ? 728  HIS A NE2 1 
ATOM   5810 N N   . LEU A 1 729 ? -31.335 -3.915  29.741 1.00 14.67 ? 729  LEU A N   1 
ATOM   5811 C CA  . LEU A 1 729 ? -31.046 -2.787  30.608 1.00 14.81 ? 729  LEU A CA  1 
ATOM   5812 C C   . LEU A 1 729 ? -31.838 -2.892  31.887 1.00 15.36 ? 729  LEU A C   1 
ATOM   5813 O O   . LEU A 1 729 ? -33.089 -3.100  31.856 1.00 15.89 ? 729  LEU A O   1 
ATOM   5814 C CB  . LEU A 1 729 ? -31.406 -1.466  29.907 1.00 13.83 ? 729  LEU A CB  1 
ATOM   5815 C CG  . LEU A 1 729 ? -30.657 -1.227  28.596 1.00 15.55 ? 729  LEU A CG  1 
ATOM   5816 C CD1 . LEU A 1 729 ? -31.101 0.065   27.954 1.00 17.72 ? 729  LEU A CD1 1 
ATOM   5817 C CD2 . LEU A 1 729 ? -29.154 -1.187  28.873 1.00 11.49 ? 729  LEU A CD2 1 
ATOM   5818 N N   . ARG A 1 730 ? -31.125 -2.713  32.994 1.00 14.48 ? 730  ARG A N   1 
ATOM   5819 C CA  . ARG A 1 730 ? -31.675 -2.756  34.356 1.00 15.00 ? 730  ARG A CA  1 
ATOM   5820 C C   . ARG A 1 730 ? -32.484 -1.503  34.720 1.00 15.13 ? 730  ARG A C   1 
ATOM   5821 O O   . ARG A 1 730 ? -31.973 -0.391  34.646 1.00 15.08 ? 730  ARG A O   1 
ATOM   5822 C CB  . ARG A 1 730 ? -30.529 -3.010  35.363 1.00 14.67 ? 730  ARG A CB  1 
ATOM   5823 C CG  . ARG A 1 730 ? -30.969 -3.317  36.787 1.00 14.50 ? 730  ARG A CG  1 
ATOM   5824 C CD  . ARG A 1 730 ? -29.827 -3.734  37.629 1.00 14.14 ? 730  ARG A CD  1 
ATOM   5825 N NE  . ARG A 1 730 ? -30.143 -3.769  39.060 1.00 16.73 ? 730  ARG A NE  1 
ATOM   5826 C CZ  . ARG A 1 730 ? -29.212 -3.905  40.001 1.00 19.20 ? 730  ARG A CZ  1 
ATOM   5827 N NH1 . ARG A 1 730 ? -27.928 -3.999  39.641 1.00 17.02 ? 730  ARG A NH1 1 
ATOM   5828 N NH2 . ARG A 1 730 ? -29.552 -3.934  41.293 1.00 17.74 ? 730  ARG A NH2 1 
ATOM   5829 N N   . GLY A 1 731 ? -33.760 -1.671  35.083 1.00 15.05 ? 731  GLY A N   1 
ATOM   5830 C CA  . GLY A 1 731 ? -34.570 -0.547  35.539 1.00 15.01 ? 731  GLY A CA  1 
ATOM   5831 C C   . GLY A 1 731 ? -33.948 0.073   36.776 1.00 16.34 ? 731  GLY A C   1 
ATOM   5832 O O   . GLY A 1 731 ? -33.442 -0.643  37.636 1.00 16.73 ? 731  GLY A O   1 
ATOM   5833 N N   . GLY A 1 732 ? -33.963 1.401   36.883 1.00 15.44 ? 732  GLY A N   1 
ATOM   5834 C CA  . GLY A 1 732 ? -33.223 2.021   37.978 1.00 16.58 ? 732  GLY A CA  1 
ATOM   5835 C C   . GLY A 1 732 ? -31.893 2.621   37.558 1.00 16.09 ? 732  GLY A C   1 
ATOM   5836 O O   . GLY A 1 732 ? -31.223 3.233   38.356 1.00 16.20 ? 732  GLY A O   1 
ATOM   5837 N N   . TYR A 1 733 ? -31.547 2.511   36.279 1.00 16.40 ? 733  TYR A N   1 
ATOM   5838 C CA  . TYR A 1 733 ? -30.220 2.950   35.830 1.00 16.53 ? 733  TYR A CA  1 
ATOM   5839 C C   . TYR A 1 733 ? -30.295 3.835   34.586 1.00 15.97 ? 733  TYR A C   1 
ATOM   5840 O O   . TYR A 1 733 ? -31.145 3.642   33.734 1.00 15.91 ? 733  TYR A O   1 
ATOM   5841 C CB  . TYR A 1 733 ? -29.299 1.729   35.634 1.00 17.28 ? 733  TYR A CB  1 
ATOM   5842 C CG  . TYR A 1 733 ? -28.973 1.053   36.966 1.00 18.37 ? 733  TYR A CG  1 
ATOM   5843 C CD1 . TYR A 1 733 ? -27.806 1.385   37.656 1.00 16.14 ? 733  TYR A CD1 1 
ATOM   5844 C CD2 . TYR A 1 733 ? -29.845 0.128   37.543 1.00 17.37 ? 733  TYR A CD2 1 
ATOM   5845 C CE1 . TYR A 1 733 ? -27.506 0.808   38.856 1.00 19.58 ? 733  TYR A CE1 1 
ATOM   5846 C CE2 . TYR A 1 733 ? -29.551 -0.465  38.785 1.00 18.48 ? 733  TYR A CE2 1 
ATOM   5847 C CZ  . TYR A 1 733 ? -28.355 -0.122  39.416 1.00 19.67 ? 733  TYR A CZ  1 
ATOM   5848 O OH  . TYR A 1 733 ? -28.004 -0.647  40.652 1.00 22.88 ? 733  TYR A OH  1 
ATOM   5849 N N   . ILE A 1 734 ? -29.417 4.832   34.535 1.00 15.95 ? 734  ILE A N   1 
ATOM   5850 C CA  . ILE A 1 734 ? -29.306 5.763   33.403 1.00 15.41 ? 734  ILE A CA  1 
ATOM   5851 C C   . ILE A 1 734 ? -27.961 5.539   32.721 1.00 16.26 ? 734  ILE A C   1 
ATOM   5852 O O   . ILE A 1 734 ? -26.914 5.573   33.383 1.00 16.61 ? 734  ILE A O   1 
ATOM   5853 C CB  . ILE A 1 734 ? -29.470 7.236   33.851 1.00 15.40 ? 734  ILE A CB  1 
ATOM   5854 C CG1 . ILE A 1 734 ? -30.845 7.414   34.529 1.00 15.17 ? 734  ILE A CG1 1 
ATOM   5855 C CG2 . ILE A 1 734 ? -29.299 8.231   32.653 1.00 14.99 ? 734  ILE A CG2 1 
ATOM   5856 C CD1 . ILE A 1 734 ? -31.095 8.763   35.153 1.00 13.76 ? 734  ILE A CD1 1 
ATOM   5857 N N   . PHE A 1 735 ? -28.031 5.276   31.414 1.00 16.62 ? 735  PHE A N   1 
ATOM   5858 C CA  . PHE A 1 735 ? -26.894 4.881   30.567 1.00 16.79 ? 735  PHE A CA  1 
ATOM   5859 C C   . PHE A 1 735 ? -26.569 6.005   29.600 1.00 16.61 ? 735  PHE A C   1 
ATOM   5860 O O   . PHE A 1 735 ? -27.419 6.374   28.759 1.00 17.30 ? 735  PHE A O   1 
ATOM   5861 C CB  . PHE A 1 735 ? -27.228 3.602   29.776 1.00 16.44 ? 735  PHE A CB  1 
ATOM   5862 C CG  . PHE A 1 735 ? -27.679 2.471   30.641 1.00 14.29 ? 735  PHE A CG  1 
ATOM   5863 C CD1 . PHE A 1 735 ? -26.761 1.545   31.114 1.00 15.01 ? 735  PHE A CD1 1 
ATOM   5864 C CD2 . PHE A 1 735 ? -29.021 2.347   31.002 1.00 13.77 ? 735  PHE A CD2 1 
ATOM   5865 C CE1 . PHE A 1 735 ? -27.166 0.491   31.952 1.00 17.59 ? 735  PHE A CE1 1 
ATOM   5866 C CE2 . PHE A 1 735 ? -29.442 1.319   31.846 1.00 12.02 ? 735  PHE A CE2 1 
ATOM   5867 C CZ  . PHE A 1 735 ? -28.500 0.372   32.302 1.00 15.77 ? 735  PHE A CZ  1 
ATOM   5868 N N   . PRO A 1 736 ? -25.370 6.580   29.741 1.00 16.26 ? 736  PRO A N   1 
ATOM   5869 C CA  . PRO A 1 736 ? -24.860 7.546   28.759 1.00 16.14 ? 736  PRO A CA  1 
ATOM   5870 C C   . PRO A 1 736 ? -24.406 6.856   27.497 1.00 15.96 ? 736  PRO A C   1 
ATOM   5871 O O   . PRO A 1 736 ? -23.717 5.819   27.563 1.00 15.67 ? 736  PRO A O   1 
ATOM   5872 C CB  . PRO A 1 736 ? -23.655 8.175   29.464 1.00 15.85 ? 736  PRO A CB  1 
ATOM   5873 C CG  . PRO A 1 736 ? -23.198 7.150   30.425 1.00 15.56 ? 736  PRO A CG  1 
ATOM   5874 C CD  . PRO A 1 736 ? -24.398 6.329   30.830 1.00 15.93 ? 736  PRO A CD  1 
ATOM   5875 N N   . THR A 1 737 ? -24.813 7.415   26.356 1.00 16.01 ? 737  THR A N   1 
ATOM   5876 C CA  . THR A 1 737 ? -24.437 6.909   25.034 1.00 16.27 ? 737  THR A CA  1 
ATOM   5877 C C   . THR A 1 737 ? -23.866 7.987   24.126 1.00 15.10 ? 737  THR A C   1 
ATOM   5878 O O   . THR A 1 737 ? -23.887 9.167   24.440 1.00 15.60 ? 737  THR A O   1 
ATOM   5879 C CB  . THR A 1 737 ? -25.621 6.192   24.297 1.00 17.45 ? 737  THR A CB  1 
ATOM   5880 O OG1 . THR A 1 737 ? -26.608 7.154   23.899 1.00 20.87 ? 737  THR A OG1 1 
ATOM   5881 C CG2 . THR A 1 737 ? -26.269 5.137   25.164 1.00 18.57 ? 737  THR A CG2 1 
ATOM   5882 N N   . GLN A 1 738 ? -23.338 7.567   22.992 1.00 14.57 ? 738  GLN A N   1 
ATOM   5883 C CA  . GLN A 1 738 ? -22.757 8.480   22.030 1.00 14.39 ? 738  GLN A CA  1 
ATOM   5884 C C   . GLN A 1 738 ? -22.878 7.832   20.684 1.00 14.10 ? 738  GLN A C   1 
ATOM   5885 O O   . GLN A 1 738 ? -22.554 6.664   20.526 1.00 13.20 ? 738  GLN A O   1 
ATOM   5886 C CB  . GLN A 1 738 ? -21.285 8.768   22.372 1.00 14.52 ? 738  GLN A CB  1 
ATOM   5887 C CG  . GLN A 1 738 ? -20.684 9.860   21.481 1.00 14.65 ? 738  GLN A CG  1 
ATOM   5888 C CD  . GLN A 1 738 ? -19.469 10.475  22.098 1.00 11.85 ? 738  GLN A CD  1 
ATOM   5889 O OE1 . GLN A 1 738 ? -18.649 9.765   22.653 1.00 15.66 ? 738  GLN A OE1 1 
ATOM   5890 N NE2 . GLN A 1 738 ? -19.314 11.790  21.968 1.00 9.63  ? 738  GLN A NE2 1 
ATOM   5891 N N   . GLN A 1 739 ? -23.368 8.581   19.706 1.00 15.76 ? 739  GLN A N   1 
ATOM   5892 C CA  . GLN A 1 739 ? -23.630 8.019   18.409 1.00 16.28 ? 739  GLN A CA  1 
ATOM   5893 C C   . GLN A 1 739 ? -22.317 7.386   17.946 1.00 17.00 ? 739  GLN A C   1 
ATOM   5894 O O   . GLN A 1 739 ? -21.258 8.002   18.066 1.00 18.25 ? 739  GLN A O   1 
ATOM   5895 C CB  . GLN A 1 739 ? -24.135 9.088   17.444 1.00 15.95 ? 739  GLN A CB  1 
ATOM   5896 C CG  . GLN A 1 739 ? -24.221 8.596   16.019 1.00 18.35 ? 739  GLN A CG  1 
ATOM   5897 C CD  . GLN A 1 739 ? -24.581 9.682   15.025 1.00 21.41 ? 739  GLN A CD  1 
ATOM   5898 O OE1 . GLN A 1 739 ? -24.682 9.421   13.825 1.00 23.86 ? 739  GLN A OE1 1 
ATOM   5899 N NE2 . GLN A 1 739 ? -24.775 10.894  15.510 1.00 23.20 ? 739  GLN A NE2 1 
ATOM   5900 N N   . PRO A 1 740 ? -22.376 6.132   17.476 1.00 17.73 ? 740  PRO A N   1 
ATOM   5901 C CA  . PRO A 1 740 ? -21.119 5.470   17.139 1.00 18.27 ? 740  PRO A CA  1 
ATOM   5902 C C   . PRO A 1 740 ? -20.545 5.840   15.767 1.00 19.54 ? 740  PRO A C   1 
ATOM   5903 O O   . PRO A 1 740 ? -21.252 6.302   14.881 1.00 19.05 ? 740  PRO A O   1 
ATOM   5904 C CB  . PRO A 1 740 ? -21.496 4.004   17.149 1.00 17.55 ? 740  PRO A CB  1 
ATOM   5905 C CG  . PRO A 1 740 ? -22.942 4.005   16.676 1.00 17.81 ? 740  PRO A CG  1 
ATOM   5906 C CD  . PRO A 1 740 ? -23.547 5.247   17.301 1.00 16.56 ? 740  PRO A CD  1 
ATOM   5907 N N   . ASN A 1 741 ? -19.246 5.628   15.619 1.00 19.99 ? 741  ASN A N   1 
ATOM   5908 C CA  . ASN A 1 741 ? -18.598 5.736   14.335 1.00 21.22 ? 741  ASN A CA  1 
ATOM   5909 C C   . ASN A 1 741 ? -17.617 4.561   14.306 1.00 21.44 ? 741  ASN A C   1 
ATOM   5910 O O   . ASN A 1 741 ? -17.477 3.831   15.299 1.00 21.74 ? 741  ASN A O   1 
ATOM   5911 C CB  . ASN A 1 741 ? -17.872 7.097   14.229 1.00 21.30 ? 741  ASN A CB  1 
ATOM   5912 C CG  . ASN A 1 741 ? -17.740 7.624   12.772 1.00 24.15 ? 741  ASN A CG  1 
ATOM   5913 O OD1 . ASN A 1 741 ? -17.895 6.894   11.794 1.00 23.75 ? 741  ASN A OD1 1 
ATOM   5914 N ND2 . ASN A 1 741 ? -17.429 8.910   12.652 1.00 30.84 ? 741  ASN A ND2 1 
ATOM   5915 N N   . THR A 1 742 ? -16.934 4.377   13.188 1.00 20.98 ? 742  THR A N   1 
ATOM   5916 C CA  . THR A 1 742 ? -16.022 3.233   13.015 1.00 20.15 ? 742  THR A CA  1 
ATOM   5917 C C   . THR A 1 742 ? -14.729 3.336   13.839 1.00 19.44 ? 742  THR A C   1 
ATOM   5918 O O   . THR A 1 742 ? -13.999 2.353   13.968 1.00 20.28 ? 742  THR A O   1 
ATOM   5919 C CB  . THR A 1 742 ? -15.679 3.034   11.522 1.00 20.25 ? 742  THR A CB  1 
ATOM   5920 O OG1 . THR A 1 742 ? -15.083 4.232   11.011 1.00 20.42 ? 742  THR A OG1 1 
ATOM   5921 C CG2 . THR A 1 742 ? -16.922 2.751   10.743 1.00 19.42 ? 742  THR A CG2 1 
ATOM   5922 N N   . THR A 1 743 ? -14.449 4.515   14.382 1.00 18.42 ? 743  THR A N   1 
ATOM   5923 C CA  . THR A 1 743 ? -13.345 4.719   15.307 1.00 19.51 ? 743  THR A CA  1 
ATOM   5924 C C   . THR A 1 743 ? -13.814 5.560   16.496 1.00 19.40 ? 743  THR A C   1 
ATOM   5925 O O   . THR A 1 743 ? -14.729 6.354   16.350 1.00 19.14 ? 743  THR A O   1 
ATOM   5926 C CB  . THR A 1 743 ? -12.150 5.433   14.624 1.00 19.52 ? 743  THR A CB  1 
ATOM   5927 O OG1 . THR A 1 743 ? -12.542 6.761   14.287 1.00 21.06 ? 743  THR A OG1 1 
ATOM   5928 C CG2 . THR A 1 743 ? -11.749 4.715   13.328 1.00 18.63 ? 743  THR A CG2 1 
ATOM   5929 N N   . THR A 1 744 ? -13.188 5.391   17.659 1.00 20.19 ? 744  THR A N   1 
ATOM   5930 C CA  . THR A 1 744 ? -13.461 6.258   18.819 1.00 21.19 ? 744  THR A CA  1 
ATOM   5931 C C   . THR A 1 744 ? -12.909 7.664   18.645 1.00 21.88 ? 744  THR A C   1 
ATOM   5932 O O   . THR A 1 744 ? -13.368 8.593   19.314 1.00 21.94 ? 744  THR A O   1 
ATOM   5933 C CB  . THR A 1 744 ? -12.916 5.697   20.138 1.00 21.27 ? 744  THR A CB  1 
ATOM   5934 O OG1 . THR A 1 744 ? -11.476 5.620   20.062 1.00 21.71 ? 744  THR A OG1 1 
ATOM   5935 C CG2 . THR A 1 744 ? -13.522 4.315   20.446 1.00 20.65 ? 744  THR A CG2 1 
ATOM   5936 N N   . LEU A 1 745 ? -11.918 7.831   17.763 1.00 21.98 ? 745  LEU A N   1 
ATOM   5937 C CA  . LEU A 1 745 ? -11.423 9.171   17.442 1.00 22.00 ? 745  LEU A CA  1 
ATOM   5938 C C   . LEU A 1 745 ? -12.585 10.012  16.920 1.00 22.03 ? 745  LEU A C   1 
ATOM   5939 O O   . LEU A 1 745 ? -12.834 11.119  17.399 1.00 23.05 ? 745  LEU A O   1 
ATOM   5940 C CB  . LEU A 1 745 ? -10.293 9.135   16.390 1.00 21.79 ? 745  LEU A CB  1 
ATOM   5941 C CG  . LEU A 1 745 ? -9.795  10.527  15.994 1.00 23.32 ? 745  LEU A CG  1 
ATOM   5942 C CD1 . LEU A 1 745 ? -8.820  11.008  17.020 1.00 25.38 ? 745  LEU A CD1 1 
ATOM   5943 C CD2 . LEU A 1 745 ? -9.171  10.534  14.627 1.00 24.93 ? 745  LEU A CD2 1 
ATOM   5944 N N   . ALA A 1 746 ? -13.276 9.474   15.932 1.00 22.02 ? 746  ALA A N   1 
ATOM   5945 C CA  . ALA A 1 746 ? -14.482 10.102  15.379 1.00 22.33 ? 746  ALA A CA  1 
ATOM   5946 C C   . ALA A 1 746 ? -15.641 10.064  16.360 1.00 21.94 ? 746  ALA A C   1 
ATOM   5947 O O   . ALA A 1 746 ? -16.257 11.078  16.601 1.00 21.99 ? 746  ALA A O   1 
ATOM   5948 C CB  . ALA A 1 746 ? -14.883 9.426   14.097 1.00 21.31 ? 746  ALA A CB  1 
ATOM   5949 N N   . SER A 1 747 ? -15.928 8.889   16.917 1.00 21.96 ? 747  SER A N   1 
ATOM   5950 C CA  . SER A 1 747 ? -17.112 8.689   17.778 1.00 21.34 ? 747  SER A CA  1 
ATOM   5951 C C   . SER A 1 747 ? -17.187 9.696   18.920 1.00 20.51 ? 747  SER A C   1 
ATOM   5952 O O   . SER A 1 747 ? -18.253 10.204  19.226 1.00 19.76 ? 747  SER A O   1 
ATOM   5953 C CB  . SER A 1 747 ? -17.208 7.234   18.288 1.00 21.13 ? 747  SER A CB  1 
ATOM   5954 O OG  . SER A 1 747 ? -16.428 7.012   19.459 1.00 24.50 ? 747  SER A OG  1 
ATOM   5955 N N   . ARG A 1 748 ? -16.048 10.038  19.519 1.00 20.14 ? 748  ARG A N   1 
ATOM   5956 C CA  . ARG A 1 748 ? -16.052 10.960  20.656 1.00 19.65 ? 748  ARG A CA  1 
ATOM   5957 C C   . ARG A 1 748 ? -16.536 12.391  20.365 1.00 19.50 ? 748  ARG A C   1 
ATOM   5958 O O   . ARG A 1 748 ? -16.820 13.149  21.306 1.00 19.17 ? 748  ARG A O   1 
ATOM   5959 C CB  . ARG A 1 748 ? -14.680 11.011  21.287 1.00 19.68 ? 748  ARG A CB  1 
ATOM   5960 C CG  . ARG A 1 748 ? -14.275 9.714   21.976 1.00 19.62 ? 748  ARG A CG  1 
ATOM   5961 C CD  . ARG A 1 748 ? -12.813 9.799   22.349 1.00 18.89 ? 748  ARG A CD  1 
ATOM   5962 N NE  . ARG A 1 748 ? -12.555 11.051  23.055 1.00 19.11 ? 748  ARG A NE  1 
ATOM   5963 C CZ  . ARG A 1 748 ? -12.712 11.219  24.366 1.00 19.63 ? 748  ARG A CZ  1 
ATOM   5964 N NH1 . ARG A 1 748 ? -13.088 10.205  25.131 1.00 22.39 ? 748  ARG A NH1 1 
ATOM   5965 N NH2 . ARG A 1 748 ? -12.467 12.395  24.923 1.00 19.94 ? 748  ARG A NH2 1 
ATOM   5966 N N   . LYS A 1 749 ? -16.629 12.746  19.081 1.00 18.84 ? 749  LYS A N   1 
ATOM   5967 C CA  . LYS A 1 749 ? -17.154 14.041  18.622 1.00 18.75 ? 749  LYS A CA  1 
ATOM   5968 C C   . LYS A 1 749 ? -18.667 14.032  18.337 1.00 18.09 ? 749  LYS A C   1 
ATOM   5969 O O   . LYS A 1 749 ? -19.250 15.042  17.929 1.00 17.86 ? 749  LYS A O   1 
ATOM   5970 C CB  . LYS A 1 749 ? -16.421 14.462  17.348 1.00 19.56 ? 749  LYS A CB  1 
ATOM   5971 C CG  . LYS A 1 749 ? -14.870 14.540  17.528 1.00 19.45 ? 749  LYS A CG  1 
ATOM   5972 C CD  . LYS A 1 749 ? -14.164 14.814  16.207 1.00 20.17 ? 749  LYS A CD  1 
ATOM   5973 C CE  . LYS A 1 749 ? -12.646 14.977  16.427 1.00 22.82 ? 749  LYS A CE  1 
ATOM   5974 N NZ  . LYS A 1 749 ? -11.820 14.865  15.160 1.00 28.91 ? 749  LYS A NZ  1 
ATOM   5975 N N   . ASN A 1 750 ? -19.300 12.897  18.542 1.00 17.80 ? 750  ASN A N   1 
ATOM   5976 C CA  . ASN A 1 750 ? -20.709 12.744  18.170 1.00 17.57 ? 750  ASN A CA  1 
ATOM   5977 C C   . ASN A 1 750 ? -21.698 13.178  19.278 1.00 17.55 ? 750  ASN A C   1 
ATOM   5978 O O   . ASN A 1 750 ? -21.323 13.260  20.440 1.00 17.18 ? 750  ASN A O   1 
ATOM   5979 C CB  . ASN A 1 750 ? -20.960 11.312  17.686 1.00 16.71 ? 750  ASN A CB  1 
ATOM   5980 C CG  . ASN A 1 750 ? -20.578 11.100  16.216 1.00 16.66 ? 750  ASN A CG  1 
ATOM   5981 O OD1 . ASN A 1 750 ? -20.422 12.046  15.471 1.00 20.04 ? 750  ASN A OD1 1 
ATOM   5982 N ND2 . ASN A 1 750 ? -20.436 9.853   15.805 1.00 13.05 ? 750  ASN A ND2 1 
ATOM   5983 N N   . PRO A 1 751 ? -22.974 13.466  18.916 1.00 18.24 ? 751  PRO A N   1 
ATOM   5984 C CA  . PRO A 1 751 ? -24.006 13.699  19.922 1.00 18.45 ? 751  PRO A CA  1 
ATOM   5985 C C   . PRO A 1 751 ? -24.117 12.564  20.937 1.00 16.92 ? 751  PRO A C   1 
ATOM   5986 O O   . PRO A 1 751 ? -24.003 11.404  20.599 1.00 17.68 ? 751  PRO A O   1 
ATOM   5987 C CB  . PRO A 1 751 ? -25.296 13.757  19.076 1.00 18.62 ? 751  PRO A CB  1 
ATOM   5988 C CG  . PRO A 1 751 ? -24.818 14.363  17.819 1.00 20.09 ? 751  PRO A CG  1 
ATOM   5989 C CD  . PRO A 1 751 ? -23.529 13.629  17.564 1.00 19.43 ? 751  PRO A CD  1 
ATOM   5990 N N   . LEU A 1 752 ? -24.352 12.922  22.175 1.00 17.00 ? 752  LEU A N   1 
ATOM   5991 C CA  . LEU A 1 752 ? -24.590 11.958  23.209 1.00 17.91 ? 752  LEU A CA  1 
ATOM   5992 C C   . LEU A 1 752 ? -26.081 11.754  23.405 1.00 18.19 ? 752  LEU A C   1 
ATOM   5993 O O   . LEU A 1 752 ? -26.911 12.485  22.864 1.00 18.30 ? 752  LEU A O   1 
ATOM   5994 C CB  . LEU A 1 752 ? -23.982 12.449  24.518 1.00 18.79 ? 752  LEU A CB  1 
ATOM   5995 C CG  . LEU A 1 752 ? -22.582 13.006  24.402 1.00 19.46 ? 752  LEU A CG  1 
ATOM   5996 C CD1 . LEU A 1 752 ? -22.445 14.106  25.467 1.00 23.10 ? 752  LEU A CD1 1 
ATOM   5997 C CD2 . LEU A 1 752 ? -21.604 11.896  24.623 1.00 22.94 ? 752  LEU A CD2 1 
ATOM   5998 N N   . GLY A 1 753 ? -26.399 10.748  24.200 1.00 18.20 ? 753  GLY A N   1 
ATOM   5999 C CA  . GLY A 1 753 ? -27.771 10.374  24.487 1.00 17.99 ? 753  GLY A CA  1 
ATOM   6000 C C   . GLY A 1 753 ? -27.774 9.834   25.899 1.00 18.41 ? 753  GLY A C   1 
ATOM   6001 O O   . GLY A 1 753 ? -26.704 9.546   26.492 1.00 17.64 ? 753  GLY A O   1 
ATOM   6002 N N   . LEU A 1 754 ? -28.969 9.752   26.457 1.00 17.83 ? 754  LEU A N   1 
ATOM   6003 C CA  . LEU A 1 754 ? -29.195 9.100   27.718 1.00 18.81 ? 754  LEU A CA  1 
ATOM   6004 C C   . LEU A 1 754 ? -30.248 8.015   27.516 1.00 19.21 ? 754  LEU A C   1 
ATOM   6005 O O   . LEU A 1 754 ? -31.271 8.258   26.866 1.00 20.39 ? 754  LEU A O   1 
ATOM   6006 C CB  . LEU A 1 754 ? -29.661 10.100  28.785 1.00 17.87 ? 754  LEU A CB  1 
ATOM   6007 C CG  . LEU A 1 754 ? -28.712 11.185  29.277 1.00 18.65 ? 754  LEU A CG  1 
ATOM   6008 C CD1 . LEU A 1 754 ? -29.393 12.080  30.291 1.00 17.97 ? 754  LEU A CD1 1 
ATOM   6009 C CD2 . LEU A 1 754 ? -27.471 10.549  29.884 1.00 14.39 ? 754  LEU A CD2 1 
ATOM   6010 N N   . ILE A 1 755 ? -30.001 6.834   28.068 1.00 19.11 ? 755  ILE A N   1 
ATOM   6011 C CA  . ILE A 1 755 ? -31.058 5.821   28.234 1.00 19.69 ? 755  ILE A CA  1 
ATOM   6012 C C   . ILE A 1 755 ? -31.414 5.743   29.716 1.00 19.68 ? 755  ILE A C   1 
ATOM   6013 O O   . ILE A 1 755 ? -30.573 5.403   30.535 1.00 20.23 ? 755  ILE A O   1 
ATOM   6014 C CB  . ILE A 1 755 ? -30.715 4.414   27.684 1.00 18.79 ? 755  ILE A CB  1 
ATOM   6015 C CG1 . ILE A 1 755 ? -30.225 4.494   26.230 1.00 19.75 ? 755  ILE A CG1 1 
ATOM   6016 C CG2 . ILE A 1 755 ? -31.962 3.503   27.767 1.00 18.05 ? 755  ILE A CG2 1 
ATOM   6017 C CD1 . ILE A 1 755 ? -29.449 3.246   25.776 1.00 20.27 ? 755  ILE A CD1 1 
ATOM   6018 N N   . ILE A 1 756 ? -32.653 6.135   30.031 1.00 20.02 ? 756  ILE A N   1 
ATOM   6019 C CA  . ILE A 1 756 ? -33.225 6.101   31.372 1.00 19.03 ? 756  ILE A CA  1 
ATOM   6020 C C   . ILE A 1 756 ? -34.143 4.852   31.412 1.00 19.99 ? 756  ILE A C   1 
ATOM   6021 O O   . ILE A 1 756 ? -35.209 4.840   30.803 1.00 19.48 ? 756  ILE A O   1 
ATOM   6022 C CB  . ILE A 1 756 ? -34.059 7.399   31.644 1.00 19.38 ? 756  ILE A CB  1 
ATOM   6023 C CG1 . ILE A 1 756 ? -33.164 8.658   31.592 1.00 17.74 ? 756  ILE A CG1 1 
ATOM   6024 C CG2 . ILE A 1 756 ? -34.811 7.312   32.943 1.00 16.95 ? 756  ILE A CG2 1 
ATOM   6025 C CD1 . ILE A 1 756 ? -33.917 9.961   31.421 1.00 18.20 ? 756  ILE A CD1 1 
ATOM   6026 N N   . ALA A 1 757 ? -33.709 3.795   32.098 1.00 19.94 ? 757  ALA A N   1 
ATOM   6027 C CA  . ALA A 1 757 ? -34.546 2.636   32.337 1.00 18.55 ? 757  ALA A CA  1 
ATOM   6028 C C   . ALA A 1 757 ? -35.140 2.805   33.717 1.00 19.14 ? 757  ALA A C   1 
ATOM   6029 O O   . ALA A 1 757 ? -34.465 2.638   34.714 1.00 18.12 ? 757  ALA A O   1 
ATOM   6030 C CB  . ALA A 1 757 ? -33.731 1.376   32.276 1.00 19.58 ? 757  ALA A CB  1 
ATOM   6031 N N   . LEU A 1 758 ? -36.428 3.106   33.776 1.00 18.66 ? 758  LEU A N   1 
ATOM   6032 C CA  . LEU A 1 758 ? -37.063 3.357   35.050 1.00 19.28 ? 758  LEU A CA  1 
ATOM   6033 C C   . LEU A 1 758 ? -37.246 2.073   35.863 1.00 19.37 ? 758  LEU A C   1 
ATOM   6034 O O   . LEU A 1 758 ? -37.517 1.013   35.303 1.00 19.86 ? 758  LEU A O   1 
ATOM   6035 C CB  . LEU A 1 758 ? -38.409 4.089   34.840 1.00 18.28 ? 758  LEU A CB  1 
ATOM   6036 C CG  . LEU A 1 758 ? -38.405 5.461   34.173 1.00 18.45 ? 758  LEU A CG  1 
ATOM   6037 C CD1 . LEU A 1 758 ? -39.845 5.984   33.985 1.00 18.59 ? 758  LEU A CD1 1 
ATOM   6038 C CD2 . LEU A 1 758 ? -37.581 6.479   34.949 1.00 19.47 ? 758  LEU A CD2 1 
ATOM   6039 N N   . ASP A 1 759 ? -37.081 2.170   37.182 1.00 21.10 ? 759  ASP A N   1 
ATOM   6040 C CA  . ASP A 1 759 ? -37.418 1.058   38.068 1.00 23.21 ? 759  ASP A CA  1 
ATOM   6041 C C   . ASP A 1 759 ? -38.921 1.064   38.369 1.00 24.54 ? 759  ASP A C   1 
ATOM   6042 O O   . ASP A 1 759 ? -39.662 1.872   37.793 1.00 25.23 ? 759  ASP A O   1 
ATOM   6043 C CB  . ASP A 1 759 ? -36.544 1.010   39.344 1.00 22.90 ? 759  ASP A CB  1 
ATOM   6044 C CG  . ASP A 1 759 ? -36.785 2.171   40.304 1.00 24.33 ? 759  ASP A CG  1 
ATOM   6045 O OD1 . ASP A 1 759 ? -37.813 2.873   40.216 1.00 24.85 ? 759  ASP A OD1 1 
ATOM   6046 O OD2 . ASP A 1 759 ? -35.907 2.402   41.165 1.00 27.72 ? 759  ASP A OD2 1 
ATOM   6047 N N   . GLU A 1 760 ? -39.347 0.164   39.257 1.00 26.28 ? 760  GLU A N   1 
ATOM   6048 C CA  . GLU A 1 760 ? -40.741 -0.035  39.623 1.00 28.33 ? 760  GLU A CA  1 
ATOM   6049 C C   . GLU A 1 760 ? -41.309 1.245   40.241 1.00 28.28 ? 760  GLU A C   1 
ATOM   6050 O O   . GLU A 1 760 ? -42.501 1.529   40.131 1.00 29.03 ? 760  GLU A O   1 
ATOM   6051 C CB  . GLU A 1 760 ? -40.846 -1.208  40.617 1.00 29.33 ? 760  GLU A CB  1 
ATOM   6052 C CG  . GLU A 1 760 ? -39.885 -2.395  40.321 1.00 33.17 ? 760  GLU A CG  1 
ATOM   6053 C CD  . GLU A 1 760 ? -38.600 -2.442  41.174 1.00 38.13 ? 760  GLU A CD  1 
ATOM   6054 O OE1 . GLU A 1 760 ? -38.615 -3.150  42.214 1.00 39.86 ? 760  GLU A OE1 1 
ATOM   6055 O OE2 . GLU A 1 760 ? -37.574 -1.813  40.810 1.00 37.73 ? 760  GLU A OE2 1 
ATOM   6056 N N   . ASN A 1 761 ? -40.444 2.034   40.874 1.00 27.51 ? 761  ASN A N   1 
ATOM   6057 C CA  . ASN A 1 761 ? -40.867 3.325   41.413 1.00 26.98 ? 761  ASN A CA  1 
ATOM   6058 C C   . ASN A 1 761 ? -40.733 4.514   40.461 1.00 25.41 ? 761  ASN A C   1 
ATOM   6059 O O   . ASN A 1 761 ? -40.857 5.650   40.883 1.00 26.14 ? 761  ASN A O   1 
ATOM   6060 C CB  . ASN A 1 761 ? -40.160 3.588   42.740 1.00 27.29 ? 761  ASN A CB  1 
ATOM   6061 C CG  . ASN A 1 761 ? -40.366 2.447   43.731 1.00 30.66 ? 761  ASN A CG  1 
ATOM   6062 O OD1 . ASN A 1 761 ? -41.473 1.902   43.843 1.00 33.00 ? 761  ASN A OD1 1 
ATOM   6063 N ND2 . ASN A 1 761 ? -39.296 2.057   44.429 1.00 31.39 ? 761  ASN A ND2 1 
ATOM   6064 N N   . LYS A 1 762 ? -40.508 4.241   39.179 1.00 23.74 ? 762  LYS A N   1 
ATOM   6065 C CA  . LYS A 1 762 ? -40.343 5.277   38.128 1.00 22.48 ? 762  LYS A CA  1 
ATOM   6066 C C   . LYS A 1 762 ? -39.172 6.232   38.411 1.00 21.57 ? 762  LYS A C   1 
ATOM   6067 O O   . LYS A 1 762 ? -39.240 7.438   38.139 1.00 20.26 ? 762  LYS A O   1 
ATOM   6068 C CB  . LYS A 1 762 ? -41.675 6.014   37.806 1.00 23.44 ? 762  LYS A CB  1 
ATOM   6069 C CG  . LYS A 1 762 ? -42.828 5.037   37.451 1.00 24.01 ? 762  LYS A CG  1 
ATOM   6070 C CD  . LYS A 1 762 ? -42.318 3.942   36.502 1.00 26.00 ? 762  LYS A CD  1 
ATOM   6071 C CE  . LYS A 1 762 ? -43.194 2.715   36.429 1.00 28.57 ? 762  LYS A CE  1 
ATOM   6072 N NZ  . LYS A 1 762 ? -42.476 1.658   35.654 1.00 29.20 ? 762  LYS A NZ  1 
ATOM   6073 N N   . GLU A 1 763 ? -38.096 5.661   38.956 1.00 20.44 ? 763  GLU A N   1 
ATOM   6074 C CA  . GLU A 1 763 ? -36.881 6.406   39.316 1.00 20.75 ? 763  GLU A CA  1 
ATOM   6075 C C   . GLU A 1 763 ? -35.696 5.704   38.659 1.00 18.57 ? 763  GLU A C   1 
ATOM   6076 O O   . GLU A 1 763 ? -35.803 4.556   38.238 1.00 17.56 ? 763  GLU A O   1 
ATOM   6077 C CB  . GLU A 1 763 ? -36.660 6.480   40.860 1.00 20.85 ? 763  GLU A CB  1 
ATOM   6078 C CG  . GLU A 1 763 ? -37.920 6.817   41.684 1.00 25.26 ? 763  GLU A CG  1 
ATOM   6079 C CD  . GLU A 1 763 ? -37.650 7.368   43.083 1.00 25.97 ? 763  GLU A CD  1 
ATOM   6080 O OE1 . GLU A 1 763 ? -36.612 7.040   43.724 1.00 31.71 ? 763  GLU A OE1 1 
ATOM   6081 O OE2 . GLU A 1 763 ? -38.509 8.153   43.538 1.00 31.71 ? 763  GLU A OE2 1 
ATOM   6082 N N   . ALA A 1 764 ? -34.577 6.413   38.549 1.00 17.10 ? 764  ALA A N   1 
ATOM   6083 C CA  . ALA A 1 764 ? -33.392 5.880   37.903 1.00 16.47 ? 764  ALA A CA  1 
ATOM   6084 C C   . ALA A 1 764 ? -32.253 6.805   38.217 1.00 15.87 ? 764  ALA A C   1 
ATOM   6085 O O   . ALA A 1 764 ? -32.473 7.960   38.530 1.00 16.00 ? 764  ALA A O   1 
ATOM   6086 C CB  . ALA A 1 764 ? -33.588 5.751   36.382 1.00 15.57 ? 764  ALA A CB  1 
ATOM   6087 N N   . LYS A 1 765 ? -31.032 6.285   38.163 1.00 16.41 ? 765  LYS A N   1 
ATOM   6088 C CA  . LYS A 1 765 ? -29.842 7.049   38.508 1.00 17.20 ? 765  LYS A CA  1 
ATOM   6089 C C   . LYS A 1 765 ? -28.722 6.586   37.619 1.00 16.48 ? 765  LYS A C   1 
ATOM   6090 O O   . LYS A 1 765 ? -28.714 5.449   37.169 1.00 15.95 ? 765  LYS A O   1 
ATOM   6091 C CB  . LYS A 1 765 ? -29.461 6.836   39.982 1.00 17.51 ? 765  LYS A CB  1 
ATOM   6092 C CG  . LYS A 1 765 ? -30.219 7.742   40.951 1.00 21.32 ? 765  LYS A CG  1 
ATOM   6093 C CD  . LYS A 1 765 ? -30.025 7.306   42.390 1.00 22.56 ? 765  LYS A CD  1 
ATOM   6094 C CE  . LYS A 1 765 ? -30.328 8.446   43.385 1.00 31.73 ? 765  LYS A CE  1 
ATOM   6095 N NZ  . LYS A 1 765 ? -29.504 9.690   43.117 1.00 31.94 ? 765  LYS A NZ  1 
ATOM   6096 N N   . GLY A 1 766 ? -27.777 7.478   37.342 1.00 16.59 ? 766  GLY A N   1 
ATOM   6097 C CA  . GLY A 1 766 ? -26.636 7.107   36.536 1.00 17.14 ? 766  GLY A CA  1 
ATOM   6098 C C   . GLY A 1 766 ? -25.552 8.140   36.707 1.00 17.14 ? 766  GLY A C   1 
ATOM   6099 O O   . GLY A 1 766 ? -25.727 9.136   37.422 1.00 17.49 ? 766  GLY A O   1 
ATOM   6100 N N   . GLU A 1 767 ? -24.435 7.909   36.053 1.00 17.06 ? 767  GLU A N   1 
ATOM   6101 C CA  . GLU A 1 767 ? -23.381 8.912   36.028 1.00 17.85 ? 767  GLU A CA  1 
ATOM   6102 C C   . GLU A 1 767 ? -22.659 8.896   34.698 1.00 16.92 ? 767  GLU A C   1 
ATOM   6103 O O   . GLU A 1 767 ? -22.866 7.994   33.897 1.00 17.04 ? 767  GLU A O   1 
ATOM   6104 C CB  . GLU A 1 767 ? -22.417 8.708   37.180 1.00 17.92 ? 767  GLU A CB  1 
ATOM   6105 C CG  . GLU A 1 767 ? -21.744 7.347   37.158 1.00 21.54 ? 767  GLU A CG  1 
ATOM   6106 C CD  . GLU A 1 767 ? -20.864 7.121   38.363 1.00 27.23 ? 767  GLU A CD  1 
ATOM   6107 O OE1 . GLU A 1 767 ? -20.866 7.997   39.249 1.00 27.95 ? 767  GLU A OE1 1 
ATOM   6108 O OE2 . GLU A 1 767 ? -20.164 6.079   38.417 1.00 27.94 ? 767  GLU A OE2 1 
ATOM   6109 N N   . LEU A 1 768 ? -21.840 9.918   34.455 1.00 16.60 ? 768  LEU A N   1 
ATOM   6110 C CA  . LEU A 1 768 ? -20.977 9.946   33.295 1.00 16.47 ? 768  LEU A CA  1 
ATOM   6111 C C   . LEU A 1 768 ? -19.661 10.610  33.662 1.00 16.23 ? 768  LEU A C   1 
ATOM   6112 O O   . LEU A 1 768 ? -19.665 11.733  34.153 1.00 15.93 ? 768  LEU A O   1 
ATOM   6113 C CB  . LEU A 1 768 ? -21.611 10.737  32.129 1.00 17.10 ? 768  LEU A CB  1 
ATOM   6114 C CG  . LEU A 1 768 ? -20.638 10.958  30.947 1.00 16.22 ? 768  LEU A CG  1 
ATOM   6115 C CD1 . LEU A 1 768 ? -20.333 9.662   30.171 1.00 11.33 ? 768  LEU A CD1 1 
ATOM   6116 C CD2 . LEU A 1 768 ? -21.151 12.040  30.021 1.00 17.66 ? 768  LEU A CD2 1 
ATOM   6117 N N   . PHE A 1 769 ? -18.554 9.911   33.390 1.00 15.24 ? 769  PHE A N   1 
ATOM   6118 C CA  . PHE A 1 769 ? -17.206 10.451  33.492 1.00 14.54 ? 769  PHE A CA  1 
ATOM   6119 C C   . PHE A 1 769 ? -16.742 10.863  32.088 1.00 14.51 ? 769  PHE A C   1 
ATOM   6120 O O   . PHE A 1 769 ? -16.971 10.120  31.146 1.00 15.19 ? 769  PHE A O   1 
ATOM   6121 C CB  . PHE A 1 769 ? -16.254 9.354   34.011 1.00 14.41 ? 769  PHE A CB  1 
ATOM   6122 C CG  . PHE A 1 769 ? -14.799 9.749   33.987 1.00 14.56 ? 769  PHE A CG  1 
ATOM   6123 C CD1 . PHE A 1 769 ? -14.290 10.589  34.955 1.00 13.97 ? 769  PHE A CD1 1 
ATOM   6124 C CD2 . PHE A 1 769 ? -13.932 9.240   33.019 1.00 14.07 ? 769  PHE A CD2 1 
ATOM   6125 C CE1 . PHE A 1 769 ? -12.920 10.933  34.958 1.00 13.91 ? 769  PHE A CE1 1 
ATOM   6126 C CE2 . PHE A 1 769 ? -12.580 9.599   33.003 1.00 13.70 ? 769  PHE A CE2 1 
ATOM   6127 C CZ  . PHE A 1 769 ? -12.086 10.435  33.960 1.00 16.73 ? 769  PHE A CZ  1 
ATOM   6128 N N   . TRP A 1 770 ? -16.110 12.034  31.948 1.00 14.14 ? 770  TRP A N   1 
ATOM   6129 C CA  . TRP A 1 770 ? -15.580 12.454  30.653 1.00 14.30 ? 770  TRP A CA  1 
ATOM   6130 C C   . TRP A 1 770 ? -14.266 13.198  30.821 1.00 14.40 ? 770  TRP A C   1 
ATOM   6131 O O   . TRP A 1 770 ? -14.184 14.176  31.553 1.00 15.35 ? 770  TRP A O   1 
ATOM   6132 C CB  . TRP A 1 770 ? -16.556 13.346  29.889 1.00 12.58 ? 770  TRP A CB  1 
ATOM   6133 C CG  . TRP A 1 770 ? -16.322 13.401  28.393 1.00 12.21 ? 770  TRP A CG  1 
ATOM   6134 C CD1 . TRP A 1 770 ? -15.863 14.487  27.665 1.00 8.42  ? 770  TRP A CD1 1 
ATOM   6135 C CD2 . TRP A 1 770 ? -16.500 12.335  27.442 1.00 10.65 ? 770  TRP A CD2 1 
ATOM   6136 N NE1 . TRP A 1 770 ? -15.774 14.153  26.345 1.00 7.96  ? 770  TRP A NE1 1 
ATOM   6137 C CE2 . TRP A 1 770 ? -16.153 12.847  26.175 1.00 7.57  ? 770  TRP A CE2 1 
ATOM   6138 C CE3 . TRP A 1 770 ? -16.960 11.006  27.534 1.00 13.11 ? 770  TRP A CE3 1 
ATOM   6139 C CZ2 . TRP A 1 770 ? -16.256 12.096  25.016 1.00 7.33  ? 770  TRP A CZ2 1 
ATOM   6140 C CZ3 . TRP A 1 770 ? -17.023 10.251  26.382 1.00 12.35 ? 770  TRP A CZ3 1 
ATOM   6141 C CH2 . TRP A 1 770 ? -16.688 10.801  25.135 1.00 10.47 ? 770  TRP A CH2 1 
ATOM   6142 N N   . ASP A 1 771 ? -13.254 12.758  30.109 1.00 14.67 ? 771  ASP A N   1 
ATOM   6143 C CA  . ASP A 1 771 ? -11.996 13.514  30.102 1.00 16.04 ? 771  ASP A CA  1 
ATOM   6144 C C   . ASP A 1 771 ? -11.452 13.482  28.675 1.00 16.18 ? 771  ASP A C   1 
ATOM   6145 O O   . ASP A 1 771 ? -12.167 13.098  27.762 1.00 16.96 ? 771  ASP A O   1 
ATOM   6146 C CB  . ASP A 1 771 ? -11.037 12.959  31.162 1.00 15.32 ? 771  ASP A CB  1 
ATOM   6147 C CG  . ASP A 1 771 ? -10.549 11.566  30.854 1.00 15.18 ? 771  ASP A CG  1 
ATOM   6148 O OD1 . ASP A 1 771 ? -11.032 10.954  29.883 1.00 19.28 ? 771  ASP A OD1 1 
ATOM   6149 O OD2 . ASP A 1 771 ? -9.655  11.068  31.585 1.00 14.75 ? 771  ASP A OD2 1 
ATOM   6150 N N   . ASP A 1 772 ? -10.189 13.835  28.470 1.00 16.09 ? 772  ASP A N   1 
ATOM   6151 C CA  . ASP A 1 772 ? -9.673  13.841  27.120 1.00 14.77 ? 772  ASP A CA  1 
ATOM   6152 C C   . ASP A 1 772 ? -9.450  12.441  26.525 1.00 13.86 ? 772  ASP A C   1 
ATOM   6153 O O   . ASP A 1 772 ? -9.258  12.292  25.323 1.00 12.67 ? 772  ASP A O   1 
ATOM   6154 C CB  . ASP A 1 772 ? -8.470  14.793  26.988 1.00 15.40 ? 772  ASP A CB  1 
ATOM   6155 C CG  . ASP A 1 772 ? -7.188  14.213  27.583 1.00 17.56 ? 772  ASP A CG  1 
ATOM   6156 O OD1 . ASP A 1 772 ? -7.187  13.043  28.052 1.00 15.90 ? 772  ASP A OD1 1 
ATOM   6157 O OD2 . ASP A 1 772 ? -6.179  14.952  27.562 1.00 19.76 ? 772  ASP A OD2 1 
ATOM   6158 N N   . GLY A 1 773 ? -9.537  11.405  27.350 1.00 13.82 ? 773  GLY A N   1 
ATOM   6159 C CA  . GLY A 1 773 ? -9.515  10.039  26.834 1.00 14.14 ? 773  GLY A CA  1 
ATOM   6160 C C   . GLY A 1 773 ? -8.134  9.469   26.532 1.00 15.30 ? 773  GLY A C   1 
ATOM   6161 O O   . GLY A 1 773 ? -8.020  8.357   26.015 1.00 15.01 ? 773  GLY A O   1 
ATOM   6162 N N   . GLU A 1 774 ? -7.073  10.204  26.849 1.00 16.31 ? 774  GLU A N   1 
ATOM   6163 C CA  . GLU A 1 774 ? -5.736  9.682   26.539 1.00 18.94 ? 774  GLU A CA  1 
ATOM   6164 C C   . GLU A 1 774 ? -4.627  10.227  27.442 1.00 20.17 ? 774  GLU A C   1 
ATOM   6165 O O   . GLU A 1 774 ? -3.554  9.592   27.561 1.00 21.56 ? 774  GLU A O   1 
ATOM   6166 C CB  . GLU A 1 774 ? -5.410  9.947   25.058 1.00 19.24 ? 774  GLU A CB  1 
ATOM   6167 C CG  . GLU A 1 774 ? -5.214  11.421  24.767 1.00 21.18 ? 774  GLU A CG  1 
ATOM   6168 C CD  . GLU A 1 774 ? -5.050  11.736  23.299 1.00 26.46 ? 774  GLU A CD  1 
ATOM   6169 O OE1 . GLU A 1 774 ? -4.810  10.816  22.489 1.00 28.20 ? 774  GLU A OE1 1 
ATOM   6170 O OE2 . GLU A 1 774 ? -5.170  12.934  22.960 1.00 32.86 ? 774  GLU A OE2 1 
ATOM   6171 N N   . THR A 1 775 ? -4.864  11.367  28.092 1.00 21.68 ? 775  THR A N   1 
ATOM   6172 C CA  . THR A 1 775 ? -3.842  11.963  28.974 1.00 23.26 ? 775  THR A CA  1 
ATOM   6173 C C   . THR A 1 775 ? -3.678  11.185  30.295 1.00 24.03 ? 775  THR A C   1 
ATOM   6174 O O   . THR A 1 775 ? -4.672  10.796  30.931 1.00 22.80 ? 775  THR A O   1 
ATOM   6175 C CB  . THR A 1 775 ? -4.082  13.487  29.213 1.00 24.09 ? 775  THR A CB  1 
ATOM   6176 O OG1 . THR A 1 775 ? -4.222  14.150  27.951 1.00 23.40 ? 775  THR A OG1 1 
ATOM   6177 C CG2 . THR A 1 775 ? -2.924  14.119  29.938 1.00 23.34 ? 775  THR A CG2 1 
ATOM   6178 N N   . LYS A 1 776 ? -2.427  10.922  30.685 1.00 24.50 ? 776  LYS A N   1 
ATOM   6179 C CA  . LYS A 1 776 ? -2.168  10.229  31.949 1.00 26.72 ? 776  LYS A CA  1 
ATOM   6180 C C   . LYS A 1 776 ? -2.393  11.247  33.075 1.00 27.32 ? 776  LYS A C   1 
ATOM   6181 O O   . LYS A 1 776 ? -2.137  12.423  32.895 1.00 28.50 ? 776  LYS A O   1 
ATOM   6182 C CB  . LYS A 1 776 ? -0.736  9.681   31.985 1.00 26.93 ? 776  LYS A CB  1 
ATOM   6183 C CG  . LYS A 1 776 ? -0.620  8.201   32.351 1.00 28.59 ? 776  LYS A CG  1 
ATOM   6184 C CD  . LYS A 1 776 ? 0.843   7.719   32.339 1.00 27.96 ? 776  LYS A CD  1 
ATOM   6185 C CE  . LYS A 1 776 ? 0.902   6.221   32.000 1.00 30.00 ? 776  LYS A CE  1 
ATOM   6186 N NZ  . LYS A 1 776 ? 2.271   5.666   31.757 1.00 31.87 ? 776  LYS A NZ  1 
ATOM   6187 N N   . ASP A 1 777 ? -2.901  10.818  34.221 1.00 28.05 ? 777  ASP A N   1 
ATOM   6188 C CA  . ASP A 1 777 ? -3.012  11.732  35.358 1.00 28.72 ? 777  ASP A CA  1 
ATOM   6189 C C   . ASP A 1 777 ? -4.276  12.606  35.337 1.00 27.62 ? 777  ASP A C   1 
ATOM   6190 O O   . ASP A 1 777 ? -4.369  13.527  36.127 1.00 27.40 ? 777  ASP A O   1 
ATOM   6191 C CB  . ASP A 1 777 ? -1.803  12.698  35.417 1.00 29.90 ? 777  ASP A CB  1 
ATOM   6192 C CG  . ASP A 1 777 ? -0.506  12.041  35.904 1.00 33.76 ? 777  ASP A CG  1 
ATOM   6193 O OD1 . ASP A 1 777 ? -0.549  11.059  36.690 1.00 36.36 ? 777  ASP A OD1 1 
ATOM   6194 O OD2 . ASP A 1 777 ? 0.579   12.554  35.511 1.00 38.06 ? 777  ASP A OD2 1 
ATOM   6195 N N   . THR A 1 778 ? -5.230  12.364  34.440 1.00 26.95 ? 778  THR A N   1 
ATOM   6196 C CA  . THR A 1 778 ? -6.399  13.254  34.397 1.00 26.31 ? 778  THR A CA  1 
ATOM   6197 C C   . THR A 1 778 ? -7.211  13.145  35.675 1.00 26.02 ? 778  THR A C   1 
ATOM   6198 O O   . THR A 1 778 ? -7.830  14.121  36.076 1.00 26.46 ? 778  THR A O   1 
ATOM   6199 C CB  . THR A 1 778 ? -7.345  13.018  33.209 1.00 26.41 ? 778  THR A CB  1 
ATOM   6200 O OG1 . THR A 1 778 ? -7.882  11.692  33.270 1.00 25.07 ? 778  THR A OG1 1 
ATOM   6201 C CG2 . THR A 1 778 ? -6.631  13.231  31.899 1.00 24.78 ? 778  THR A CG2 1 
ATOM   6202 N N   . VAL A 1 779 ? -7.193  11.973  36.312 1.00 25.08 ? 779  VAL A N   1 
ATOM   6203 C CA  . VAL A 1 779 ? -7.964  11.745  37.536 1.00 25.53 ? 779  VAL A CA  1 
ATOM   6204 C C   . VAL A 1 779 ? -7.233  12.342  38.747 1.00 26.34 ? 779  VAL A C   1 
ATOM   6205 O O   . VAL A 1 779 ? -7.796  13.170  39.468 1.00 25.53 ? 779  VAL A O   1 
ATOM   6206 C CB  . VAL A 1 779 ? -8.307  10.258  37.726 1.00 25.19 ? 779  VAL A CB  1 
ATOM   6207 C CG1 . VAL A 1 779 ? -8.935  10.014  39.075 1.00 25.02 ? 779  VAL A CG1 1 
ATOM   6208 C CG2 . VAL A 1 779 ? -9.239  9.794   36.618 1.00 24.72 ? 779  VAL A CG2 1 
ATOM   6209 N N   . ALA A 1 780 ? -5.964  11.965  38.918 1.00 26.72 ? 780  ALA A N   1 
ATOM   6210 C CA  . ALA A 1 780 ? -5.119  12.496  39.982 1.00 28.14 ? 780  ALA A CA  1 
ATOM   6211 C C   . ALA A 1 780 ? -5.076  14.011  39.968 1.00 28.79 ? 780  ALA A C   1 
ATOM   6212 O O   . ALA A 1 780 ? -5.060  14.644  41.023 1.00 29.46 ? 780  ALA A O   1 
ATOM   6213 C CB  . ALA A 1 780 ? -3.688  11.922  39.889 1.00 27.80 ? 780  ALA A CB  1 
ATOM   6214 N N   . ASN A 1 781 ? -5.058  14.590  38.771 1.00 30.19 ? 781  ASN A N   1 
ATOM   6215 C CA  . ASN A 1 781 ? -4.957  16.034  38.603 1.00 30.64 ? 781  ASN A CA  1 
ATOM   6216 C C   . ASN A 1 781 ? -6.300  16.720  38.416 1.00 30.01 ? 781  ASN A C   1 
ATOM   6217 O O   . ASN A 1 781 ? -6.364  17.932  38.221 1.00 30.31 ? 781  ASN A O   1 
ATOM   6218 C CB  . ASN A 1 781 ? -4.025  16.370  37.441 1.00 31.41 ? 781  ASN A CB  1 
ATOM   6219 C CG  . ASN A 1 781 ? -2.579  16.128  37.780 1.00 34.33 ? 781  ASN A CG  1 
ATOM   6220 O OD1 . ASN A 1 781 ? -1.826  15.597  36.973 1.00 37.57 ? 781  ASN A OD1 1 
ATOM   6221 N ND2 . ASN A 1 781 ? -2.185  16.499  38.988 1.00 35.73 ? 781  ASN A ND2 1 
ATOM   6222 N N   . LYS A 1 782 ? -7.370  15.938  38.484 1.00 29.31 ? 782  LYS A N   1 
ATOM   6223 C CA  . LYS A 1 782 ? -8.730  16.470  38.439 1.00 27.91 ? 782  LYS A CA  1 
ATOM   6224 C C   . LYS A 1 782 ? -8.942  17.352  37.220 1.00 26.50 ? 782  LYS A C   1 
ATOM   6225 O O   . LYS A 1 782 ? -9.318  18.515  37.339 1.00 26.44 ? 782  LYS A O   1 
ATOM   6226 C CB  . LYS A 1 782 ? -9.048  17.246  39.728 1.00 28.98 ? 782  LYS A CB  1 
ATOM   6227 C CG  . LYS A 1 782 ? -8.779  16.478  40.999 1.00 30.34 ? 782  LYS A CG  1 
ATOM   6228 C CD  . LYS A 1 782 ? -10.021 15.802  41.490 1.00 36.40 ? 782  LYS A CD  1 
ATOM   6229 C CE  . LYS A 1 782 ? -9.773  15.133  42.841 1.00 38.63 ? 782  LYS A CE  1 
ATOM   6230 N NZ  . LYS A 1 782 ? -10.538 13.853  42.963 1.00 40.86 ? 782  LYS A NZ  1 
ATOM   6231 N N   . VAL A 1 783 ? -8.673  16.791  36.045 1.00 24.74 ? 783  VAL A N   1 
ATOM   6232 C CA  . VAL A 1 783 ? -8.994  17.432  34.789 1.00 22.81 ? 783  VAL A CA  1 
ATOM   6233 C C   . VAL A 1 783 ? -9.991  16.481  34.141 1.00 22.05 ? 783  VAL A C   1 
ATOM   6234 O O   . VAL A 1 783 ? -9.647  15.667  33.265 1.00 21.57 ? 783  VAL A O   1 
ATOM   6235 C CB  . VAL A 1 783 ? -7.756  17.695  33.891 1.00 22.81 ? 783  VAL A CB  1 
ATOM   6236 C CG1 . VAL A 1 783 ? -8.173  18.497  32.667 1.00 22.78 ? 783  VAL A CG1 1 
ATOM   6237 C CG2 . VAL A 1 783 ? -6.662  18.480  34.656 1.00 24.18 ? 783  VAL A CG2 1 
ATOM   6238 N N   . TYR A 1 784 ? -11.228 16.577  34.612 1.00 20.76 ? 784  TYR A N   1 
ATOM   6239 C CA  . TYR A 1 784 ? -12.293 15.754  34.096 1.00 20.63 ? 784  TYR A CA  1 
ATOM   6240 C C   . TYR A 1 784 ? -13.669 16.296  34.425 1.00 20.02 ? 784  TYR A C   1 
ATOM   6241 O O   . TYR A 1 784 ? -13.845 17.127  35.307 1.00 19.95 ? 784  TYR A O   1 
ATOM   6242 C CB  . TYR A 1 784 ? -12.168 14.301  34.576 1.00 20.09 ? 784  TYR A CB  1 
ATOM   6243 C CG  . TYR A 1 784 ? -12.283 14.026  36.083 1.00 20.64 ? 784  TYR A CG  1 
ATOM   6244 C CD1 . TYR A 1 784 ? -13.518 13.743  36.670 1.00 19.75 ? 784  TYR A CD1 1 
ATOM   6245 C CD2 . TYR A 1 784 ? -11.143 13.936  36.887 1.00 20.79 ? 784  TYR A CD2 1 
ATOM   6246 C CE1 . TYR A 1 784 ? -13.628 13.443  38.014 1.00 20.24 ? 784  TYR A CE1 1 
ATOM   6247 C CE2 . TYR A 1 784 ? -11.239 13.650  38.243 1.00 21.93 ? 784  TYR A CE2 1 
ATOM   6248 C CZ  . TYR A 1 784 ? -12.489 13.401  38.800 1.00 19.93 ? 784  TYR A CZ  1 
ATOM   6249 O OH  . TYR A 1 784 ? -12.590 13.088  40.130 1.00 19.73 ? 784  TYR A OH  1 
ATOM   6250 N N   . LEU A 1 785 ? -14.651 15.790  33.709 1.00 19.73 ? 785  LEU A N   1 
ATOM   6251 C CA  . LEU A 1 785 ? -16.025 16.073  34.046 1.00 19.65 ? 785  LEU A CA  1 
ATOM   6252 C C   . LEU A 1 785 ? -16.657 14.858  34.740 1.00 19.92 ? 785  LEU A C   1 
ATOM   6253 O O   . LEU A 1 785 ? -16.555 13.745  34.252 1.00 20.42 ? 785  LEU A O   1 
ATOM   6254 C CB  . LEU A 1 785 ? -16.770 16.395  32.758 1.00 19.86 ? 785  LEU A CB  1 
ATOM   6255 C CG  . LEU A 1 785 ? -18.293 16.373  32.887 1.00 20.77 ? 785  LEU A CG  1 
ATOM   6256 C CD1 . LEU A 1 785 ? -18.727 17.591  33.672 1.00 16.53 ? 785  LEU A CD1 1 
ATOM   6257 C CD2 . LEU A 1 785 ? -18.851 16.365  31.509 1.00 22.20 ? 785  LEU A CD2 1 
ATOM   6258 N N   . LEU A 1 786 ? -17.305 15.048  35.887 1.00 19.80 ? 786  LEU A N   1 
ATOM   6259 C CA  . LEU A 1 786 ? -18.155 13.974  36.400 1.00 19.47 ? 786  LEU A CA  1 
ATOM   6260 C C   . LEU A 1 786 ? -19.545 14.509  36.643 1.00 20.24 ? 786  LEU A C   1 
ATOM   6261 O O   . LEU A 1 786 ? -19.717 15.504  37.339 1.00 20.33 ? 786  LEU A O   1 
ATOM   6262 C CB  . LEU A 1 786 ? -17.578 13.290  37.653 1.00 18.96 ? 786  LEU A CB  1 
ATOM   6263 C CG  . LEU A 1 786 ? -18.278 12.023  38.196 1.00 19.15 ? 786  LEU A CG  1 
ATOM   6264 C CD1 . LEU A 1 786 ? -18.160 10.808  37.261 1.00 17.04 ? 786  LEU A CD1 1 
ATOM   6265 C CD2 . LEU A 1 786 ? -17.764 11.658  39.584 1.00 18.44 ? 786  LEU A CD2 1 
ATOM   6266 N N   . CYS A 1 787 ? -20.537 13.857  36.050 1.00 20.77 ? 787  CYS A N   1 
ATOM   6267 C CA  . CYS A 1 787 ? -21.914 14.270  36.230 1.00 22.29 ? 787  CYS A CA  1 
ATOM   6268 C C   . CYS A 1 787 ? -22.847 13.134  36.619 1.00 21.53 ? 787  CYS A C   1 
ATOM   6269 O O   . CYS A 1 787 ? -22.553 11.971  36.385 1.00 19.46 ? 787  CYS A O   1 
ATOM   6270 C CB  . CYS A 1 787 ? -22.462 15.027  35.016 1.00 22.89 ? 787  CYS A CB  1 
ATOM   6271 S SG  . CYS A 1 787 ? -22.375 14.250  33.448 1.00 29.05 ? 787  CYS A SG  1 
ATOM   6272 N N   . GLU A 1 788 ? -23.956 13.508  37.242 1.00 21.26 ? 788  GLU A N   1 
ATOM   6273 C CA  . GLU A 1 788 ? -24.934 12.551  37.743 1.00 22.16 ? 788  GLU A CA  1 
ATOM   6274 C C   . GLU A 1 788 ? -26.312 12.880  37.262 1.00 22.18 ? 788  GLU A C   1 
ATOM   6275 O O   . GLU A 1 788 ? -26.728 14.051  37.207 1.00 22.85 ? 788  GLU A O   1 
ATOM   6276 C CB  . GLU A 1 788 ? -24.930 12.416  39.277 1.00 22.30 ? 788  GLU A CB  1 
ATOM   6277 C CG  . GLU A 1 788 ? -24.048 13.355  40.029 1.00 27.29 ? 788  GLU A CG  1 
ATOM   6278 C CD  . GLU A 1 788 ? -22.604 12.876  40.114 1.00 32.72 ? 788  GLU A CD  1 
ATOM   6279 O OE1 . GLU A 1 788 ? -21.751 13.755  40.332 1.00 35.36 ? 788  GLU A OE1 1 
ATOM   6280 O OE2 . GLU A 1 788 ? -22.317 11.647  39.977 1.00 35.97 ? 788  GLU A OE2 1 
ATOM   6281 N N   . PHE A 1 789 ? -26.999 11.825  36.871 1.00 22.09 ? 789  PHE A N   1 
ATOM   6282 C CA  . PHE A 1 789 ? -28.329 11.898  36.346 1.00 22.48 ? 789  PHE A CA  1 
ATOM   6283 C C   . PHE A 1 789 ? -29.180 11.239  37.400 1.00 22.83 ? 789  PHE A C   1 
ATOM   6284 O O   . PHE A 1 789 ? -28.823 10.179  37.923 1.00 22.11 ? 789  PHE A O   1 
ATOM   6285 C CB  . PHE A 1 789 ? -28.406 11.141  35.007 1.00 22.61 ? 789  PHE A CB  1 
ATOM   6286 C CG  . PHE A 1 789 ? -27.234 11.420  34.077 1.00 21.15 ? 789  PHE A CG  1 
ATOM   6287 C CD1 . PHE A 1 789 ? -27.138 12.641  33.404 1.00 20.52 ? 789  PHE A CD1 1 
ATOM   6288 C CD2 . PHE A 1 789 ? -26.240 10.456  33.880 1.00 22.28 ? 789  PHE A CD2 1 
ATOM   6289 C CE1 . PHE A 1 789 ? -26.061 12.925  32.557 1.00 22.54 ? 789  PHE A CE1 1 
ATOM   6290 C CE2 . PHE A 1 789 ? -25.139 10.715  33.018 1.00 24.87 ? 789  PHE A CE2 1 
ATOM   6291 C CZ  . PHE A 1 789 ? -25.058 11.951  32.355 1.00 24.33 ? 789  PHE A CZ  1 
ATOM   6292 N N   . SER A 1 790 ? -30.261 11.907  37.770 1.00 24.36 ? 790  SER A N   1 
ATOM   6293 C CA  . SER A 1 790 ? -31.312 11.286  38.564 1.00 25.86 ? 790  SER A CA  1 
ATOM   6294 C C   . SER A 1 790 ? -32.709 11.578  38.016 1.00 26.48 ? 790  SER A C   1 
ATOM   6295 O O   . SER A 1 790 ? -32.990 12.683  37.582 1.00 26.76 ? 790  SER A O   1 
ATOM   6296 C CB  . SER A 1 790 ? -31.200 11.658  40.058 1.00 26.69 ? 790  SER A CB  1 
ATOM   6297 O OG  . SER A 1 790 ? -30.496 12.877  40.286 1.00 29.41 ? 790  SER A OG  1 
ATOM   6298 N N   . VAL A 1 791 ? -33.573 10.567  38.033 1.00 27.32 ? 791  VAL A N   1 
ATOM   6299 C CA  . VAL A 1 791 ? -34.977 10.711  37.647 1.00 28.90 ? 791  VAL A CA  1 
ATOM   6300 C C   . VAL A 1 791 ? -35.829 10.324  38.865 1.00 30.17 ? 791  VAL A C   1 
ATOM   6301 O O   . VAL A 1 791 ? -35.652 9.241   39.412 1.00 29.39 ? 791  VAL A O   1 
ATOM   6302 C CB  . VAL A 1 791 ? -35.347 9.814   36.416 1.00 28.29 ? 791  VAL A CB  1 
ATOM   6303 C CG1 . VAL A 1 791 ? -36.860 9.838   36.148 1.00 29.29 ? 791  VAL A CG1 1 
ATOM   6304 C CG2 . VAL A 1 791 ? -34.609 10.264  35.193 1.00 28.70 ? 791  VAL A CG2 1 
ATOM   6305 N N   . THR A 1 792 ? -36.694 11.235  39.319 1.00 32.41 ? 792  THR A N   1 
ATOM   6306 C CA  . THR A 1 792 ? -37.688 10.940  40.360 1.00 35.19 ? 792  THR A CA  1 
ATOM   6307 C C   . THR A 1 792 ? -38.985 11.564  39.908 1.00 36.43 ? 792  THR A C   1 
ATOM   6308 O O   . THR A 1 792 ? -39.049 12.796  39.769 1.00 37.35 ? 792  THR A O   1 
ATOM   6309 C CB  . THR A 1 792 ? -37.358 11.538  41.747 1.00 35.20 ? 792  THR A CB  1 
ATOM   6310 O OG1 . THR A 1 792 ? -36.001 11.265  42.105 1.00 37.02 ? 792  THR A OG1 1 
ATOM   6311 C CG2 . THR A 1 792 ? -38.253 10.908  42.798 1.00 36.92 ? 792  THR A CG2 1 
ATOM   6312 N N   . GLN A 1 793 ? -40.009 10.719  39.753 1.00 37.22 ? 793  GLN A N   1 
ATOM   6313 C CA  . GLN A 1 793 ? -41.192 10.973  38.901 1.00 38.36 ? 793  GLN A CA  1 
ATOM   6314 C C   . GLN A 1 793 ? -41.348 12.393  38.342 1.00 37.30 ? 793  GLN A C   1 
ATOM   6315 O O   . GLN A 1 793 ? -41.318 13.401  39.078 1.00 37.95 ? 793  GLN A O   1 
ATOM   6316 C CB  . GLN A 1 793 ? -42.518 10.403  39.492 1.00 38.14 ? 793  GLN A CB  1 
ATOM   6317 C CG  . GLN A 1 793 ? -43.278 11.291  40.502 1.00 40.63 ? 793  GLN A CG  1 
ATOM   6318 C CD  . GLN A 1 793 ? -44.820 11.237  40.335 1.00 40.97 ? 793  GLN A CD  1 
ATOM   6319 O OE1 . GLN A 1 793 ? -45.539 12.145  40.781 1.00 46.27 ? 793  GLN A OE1 1 
ATOM   6320 N NE2 . GLN A 1 793 ? -45.319 10.185  39.683 1.00 42.50 ? 793  GLN A NE2 1 
ATOM   6321 N N   . ASN A 1 794 ? -41.497 12.453  37.021 1.00 35.87 ? 794  ASN A N   1 
ATOM   6322 C CA  . ASN A 1 794 ? -41.719 13.713  36.321 1.00 34.80 ? 794  ASN A CA  1 
ATOM   6323 C C   . ASN A 1 794 ? -40.486 14.615  36.162 1.00 33.12 ? 794  ASN A C   1 
ATOM   6324 O O   . ASN A 1 794 ? -40.645 15.753  35.719 1.00 32.12 ? 794  ASN A O   1 
ATOM   6325 C CB  . ASN A 1 794 ? -42.854 14.530  36.982 1.00 35.50 ? 794  ASN A CB  1 
ATOM   6326 C CG  . ASN A 1 794 ? -44.101 13.695  37.285 1.00 37.96 ? 794  ASN A CG  1 
ATOM   6327 O OD1 . ASN A 1 794 ? -44.809 13.957  38.265 1.00 41.68 ? 794  ASN A OD1 1 
ATOM   6328 N ND2 . ASN A 1 794 ? -44.362 12.684  36.464 1.00 38.23 ? 794  ASN A ND2 1 
ATOM   6329 N N   . ARG A 1 795 ? -39.283 14.146  36.526 1.00 31.12 ? 795  ARG A N   1 
ATOM   6330 C CA  . ARG A 1 795 ? -38.121 15.053  36.575 1.00 30.05 ? 795  ARG A CA  1 
ATOM   6331 C C   . ARG A 1 795 ? -36.756 14.366  36.401 1.00 28.97 ? 795  ARG A C   1 
ATOM   6332 O O   . ARG A 1 795 ? -36.383 13.525  37.222 1.00 28.53 ? 795  ARG A O   1 
ATOM   6333 C CB  . ARG A 1 795 ? -38.154 15.831  37.893 1.00 30.56 ? 795  ARG A CB  1 
ATOM   6334 C CG  . ARG A 1 795 ? -37.149 16.947  38.078 1.00 32.08 ? 795  ARG A CG  1 
ATOM   6335 C CD  . ARG A 1 795 ? -37.320 17.509  39.486 1.00 37.80 ? 795  ARG A CD  1 
ATOM   6336 N NE  . ARG A 1 795 ? -36.339 18.525  39.866 1.00 42.96 ? 795  ARG A NE  1 
ATOM   6337 C CZ  . ARG A 1 795 ? -36.634 19.800  40.134 1.00 45.64 ? 795  ARG A CZ  1 
ATOM   6338 N NH1 . ARG A 1 795 ? -37.895 20.237  40.055 1.00 48.08 ? 795  ARG A NH1 1 
ATOM   6339 N NH2 . ARG A 1 795 ? -35.669 20.646  40.480 1.00 45.93 ? 795  ARG A NH2 1 
ATOM   6340 N N   . LEU A 1 796 ? -36.030 14.736  35.341 1.00 27.01 ? 796  LEU A N   1 
ATOM   6341 C CA  . LEU A 1 796 ? -34.612 14.367  35.175 1.00 25.73 ? 796  LEU A CA  1 
ATOM   6342 C C   . LEU A 1 796 ? -33.702 15.516  35.613 1.00 25.49 ? 796  LEU A C   1 
ATOM   6343 O O   . LEU A 1 796 ? -33.831 16.643  35.136 1.00 25.50 ? 796  LEU A O   1 
ATOM   6344 C CB  . LEU A 1 796 ? -34.279 13.953  33.725 1.00 24.47 ? 796  LEU A CB  1 
ATOM   6345 C CG  . LEU A 1 796 ? -32.781 13.958  33.352 1.00 23.92 ? 796  LEU A CG  1 
ATOM   6346 C CD1 . LEU A 1 796 ? -32.025 12.785  33.957 1.00 19.99 ? 796  LEU A CD1 1 
ATOM   6347 C CD2 . LEU A 1 796 ? -32.584 14.006  31.846 1.00 24.90 ? 796  LEU A CD2 1 
ATOM   6348 N N   . GLU A 1 797 ? -32.783 15.233  36.526 1.00 25.58 ? 797  GLU A N   1 
ATOM   6349 C CA  . GLU A 1 797 ? -31.805 16.223  36.953 1.00 26.46 ? 797  GLU A CA  1 
ATOM   6350 C C   . GLU A 1 797 ? -30.411 15.820  36.492 1.00 25.60 ? 797  GLU A C   1 
ATOM   6351 O O   . GLU A 1 797 ? -29.997 14.677  36.671 1.00 24.49 ? 797  GLU A O   1 
ATOM   6352 C CB  . GLU A 1 797 ? -31.811 16.395  38.478 1.00 26.33 ? 797  GLU A CB  1 
ATOM   6353 C CG  . GLU A 1 797 ? -33.166 16.827  39.068 1.00 28.49 ? 797  GLU A CG  1 
ATOM   6354 C CD  . GLU A 1 797 ? -33.062 17.272  40.524 1.00 31.15 ? 797  GLU A CD  1 
ATOM   6355 O OE1 . GLU A 1 797 ? -32.488 16.509  41.353 1.00 38.15 ? 797  GLU A OE1 1 
ATOM   6356 O OE2 . GLU A 1 797 ? -33.551 18.390  40.846 1.00 37.73 ? 797  GLU A OE2 1 
ATOM   6357 N N   . VAL A 1 798 ? -29.695 16.760  35.885 1.00 25.66 ? 798  VAL A N   1 
ATOM   6358 C CA  . VAL A 1 798 ? -28.290 16.539  35.525 1.00 25.36 ? 798  VAL A CA  1 
ATOM   6359 C C   . VAL A 1 798 ? -27.515 17.418  36.488 1.00 24.90 ? 798  VAL A C   1 
ATOM   6360 O O   . VAL A 1 798 ? -27.671 18.622  36.494 1.00 24.87 ? 798  VAL A O   1 
ATOM   6361 C CB  . VAL A 1 798 ? -27.994 16.847  34.019 1.00 25.82 ? 798  VAL A CB  1 
ATOM   6362 C CG1 . VAL A 1 798 ? -26.499 16.690  33.691 1.00 25.16 ? 798  VAL A CG1 1 
ATOM   6363 C CG2 . VAL A 1 798 ? -28.856 15.960  33.093 1.00 26.58 ? 798  VAL A CG2 1 
ATOM   6364 N N   . ASN A 1 799 ? -26.781 16.786  37.385 1.00 25.33 ? 799  ASN A N   1 
ATOM   6365 C CA  . ASN A 1 799 ? -25.951 17.471  38.359 1.00 26.96 ? 799  ASN A CA  1 
ATOM   6366 C C   . ASN A 1 799 ? -24.511 17.327  37.927 1.00 26.33 ? 799  ASN A C   1 
ATOM   6367 O O   . ASN A 1 799 ? -24.143 16.319  37.342 1.00 26.47 ? 799  ASN A O   1 
ATOM   6368 C CB  . ASN A 1 799 ? -26.109 16.824  39.738 1.00 27.60 ? 799  ASN A CB  1 
ATOM   6369 C CG  . ASN A 1 799 ? -25.960 17.820  40.877 1.00 32.40 ? 799  ASN A CG  1 
ATOM   6370 O OD1 . ASN A 1 799 ? -25.529 18.964  40.674 1.00 39.65 ? 799  ASN A OD1 1 
ATOM   6371 N ND2 . ASN A 1 799 ? -26.335 17.399  42.091 1.00 35.97 ? 799  ASN A ND2 1 
ATOM   6372 N N   . ILE A 1 800 ? -23.696 18.320  38.234 1.00 26.14 ? 800  ILE A N   1 
ATOM   6373 C CA  . ILE A 1 800 ? -22.298 18.290  37.870 1.00 25.95 ? 800  ILE A CA  1 
ATOM   6374 C C   . ILE A 1 800 ? -21.500 18.293  39.153 1.00 26.05 ? 800  ILE A C   1 
ATOM   6375 O O   . ILE A 1 800 ? -21.566 19.251  39.901 1.00 26.38 ? 800  ILE A O   1 
ATOM   6376 C CB  . ILE A 1 800 ? -21.903 19.526  37.021 1.00 26.01 ? 800  ILE A CB  1 
ATOM   6377 C CG1 . ILE A 1 800 ? -22.905 19.789  35.878 1.00 25.09 ? 800  ILE A CG1 1 
ATOM   6378 C CG2 . ILE A 1 800 ? -20.471 19.383  36.512 1.00 26.46 ? 800  ILE A CG2 1 
ATOM   6379 C CD1 . ILE A 1 800 ? -23.072 18.674  34.867 1.00 25.25 ? 800  ILE A CD1 1 
ATOM   6380 N N   . SER A 1 801 ? -20.764 17.223  39.432 1.00 26.23 ? 801  SER A N   1 
ATOM   6381 C CA  . SER A 1 801 ? -19.950 17.212  40.644 1.00 26.90 ? 801  SER A CA  1 
ATOM   6382 C C   . SER A 1 801 ? -18.490 17.622  40.444 1.00 26.90 ? 801  SER A C   1 
ATOM   6383 O O   . SER A 1 801 ? -17.888 18.168  41.366 1.00 27.48 ? 801  SER A O   1 
ATOM   6384 C CB  . SER A 1 801 ? -20.063 15.888  41.406 1.00 27.09 ? 801  SER A CB  1 
ATOM   6385 O OG  . SER A 1 801 ? -19.433 14.828  40.716 1.00 27.28 ? 801  SER A OG  1 
ATOM   6386 N N   . GLN A 1 802 ? -17.933 17.388  39.258 1.00 26.56 ? 802  GLN A N   1 
ATOM   6387 C CA  . GLN A 1 802 ? -16.562 17.808  38.948 1.00 27.09 ? 802  GLN A CA  1 
ATOM   6388 C C   . GLN A 1 802 ? -16.622 18.379  37.551 1.00 27.06 ? 802  GLN A C   1 
ATOM   6389 O O   . GLN A 1 802 ? -17.168 17.762  36.639 1.00 27.43 ? 802  GLN A O   1 
ATOM   6390 C CB  . GLN A 1 802 ? -15.580 16.627  39.040 1.00 26.87 ? 802  GLN A CB  1 
ATOM   6391 C CG  . GLN A 1 802 ? -14.120 16.941  38.713 1.00 29.04 ? 802  GLN A CG  1 
ATOM   6392 C CD  . GLN A 1 802 ? -13.414 17.657  39.838 1.00 31.17 ? 802  GLN A CD  1 
ATOM   6393 O OE1 . GLN A 1 802 ? -12.599 18.551  39.609 1.00 36.22 ? 802  GLN A OE1 1 
ATOM   6394 N NE2 . GLN A 1 802 ? -13.727 17.282  41.061 1.00 32.15 ? 802  GLN A NE2 1 
ATOM   6395 N N   . SER A 1 803 ? -16.099 19.578  37.387 1.00 27.16 ? 803  SER A N   1 
ATOM   6396 C CA  . SER A 1 803 ? -16.269 20.291  36.142 1.00 28.21 ? 803  SER A CA  1 
ATOM   6397 C C   . SER A 1 803 ? -14.991 20.988  35.741 1.00 27.79 ? 803  SER A C   1 
ATOM   6398 O O   . SER A 1 803 ? -14.978 22.194  35.526 1.00 28.87 ? 803  SER A O   1 
ATOM   6399 C CB  . SER A 1 803 ? -17.397 21.311  36.270 1.00 27.99 ? 803  SER A CB  1 
ATOM   6400 O OG  . SER A 1 803 ? -17.751 21.754  34.988 1.00 31.42 ? 803  SER A OG  1 
ATOM   6401 N N   . THR A 1 804 ? -13.908 20.234  35.633 1.00 27.54 ? 804  THR A N   1 
ATOM   6402 C CA  . THR A 1 804 ? -12.617 20.845  35.296 1.00 26.92 ? 804  THR A CA  1 
ATOM   6403 C C   . THR A 1 804 ? -12.058 20.440  33.920 1.00 26.04 ? 804  THR A C   1 
ATOM   6404 O O   . THR A 1 804 ? -10.862 20.632  33.630 1.00 26.68 ? 804  THR A O   1 
ATOM   6405 C CB  . THR A 1 804 ? -11.601 20.613  36.407 1.00 27.18 ? 804  THR A CB  1 
ATOM   6406 O OG1 . THR A 1 804 ? -11.564 19.220  36.719 1.00 28.64 ? 804  THR A OG1 1 
ATOM   6407 C CG2 . THR A 1 804 ? -12.006 21.381  37.647 1.00 27.81 ? 804  THR A CG2 1 
ATOM   6408 N N   . TYR A 1 805 ? -12.926 19.876  33.090 1.00 24.09 ? 805  TYR A N   1 
ATOM   6409 C CA  . TYR A 1 805 ? -12.624 19.601  31.703 1.00 24.47 ? 805  TYR A CA  1 
ATOM   6410 C C   . TYR A 1 805 ? -13.830 19.912  30.846 1.00 24.99 ? 805  TYR A C   1 
ATOM   6411 O O   . TYR A 1 805 ? -14.935 19.395  31.098 1.00 25.29 ? 805  TYR A O   1 
ATOM   6412 C CB  . TYR A 1 805 ? -12.203 18.141  31.485 1.00 23.41 ? 805  TYR A CB  1 
ATOM   6413 C CG  . TYR A 1 805 ? -11.883 17.815  30.035 1.00 23.86 ? 805  TYR A CG  1 
ATOM   6414 C CD1 . TYR A 1 805 ? -10.705 18.286  29.428 1.00 22.00 ? 805  TYR A CD1 1 
ATOM   6415 C CD2 . TYR A 1 805 ? -12.757 17.050  29.271 1.00 20.78 ? 805  TYR A CD2 1 
ATOM   6416 C CE1 . TYR A 1 805 ? -10.418 17.987  28.091 1.00 21.22 ? 805  TYR A CE1 1 
ATOM   6417 C CE2 . TYR A 1 805 ? -12.484 16.752  27.964 1.00 20.50 ? 805  TYR A CE2 1 
ATOM   6418 C CZ  . TYR A 1 805 ? -11.316 17.208  27.377 1.00 20.39 ? 805  TYR A CZ  1 
ATOM   6419 O OH  . TYR A 1 805 ? -11.077 16.901  26.070 1.00 21.19 ? 805  TYR A OH  1 
ATOM   6420 N N   . LYS A 1 806 ? -13.622 20.776  29.857 1.00 25.47 ? 806  LYS A N   1 
ATOM   6421 C CA  . LYS A 1 806 ? -14.635 21.030  28.847 1.00 25.93 ? 806  LYS A CA  1 
ATOM   6422 C C   . LYS A 1 806 ? -14.128 20.566  27.493 1.00 25.21 ? 806  LYS A C   1 
ATOM   6423 O O   . LYS A 1 806 ? -13.157 21.097  26.966 1.00 25.56 ? 806  LYS A O   1 
ATOM   6424 C CB  . LYS A 1 806 ? -15.080 22.508  28.812 1.00 27.30 ? 806  LYS A CB  1 
ATOM   6425 C CG  . LYS A 1 806 ? -16.177 22.773  27.768 1.00 27.80 ? 806  LYS A CG  1 
ATOM   6426 C CD  . LYS A 1 806 ? -17.428 23.388  28.408 1.00 30.79 ? 806  LYS A CD  1 
ATOM   6427 C CE  . LYS A 1 806 ? -18.547 23.606  27.387 1.00 31.08 ? 806  LYS A CE  1 
ATOM   6428 N NZ  . LYS A 1 806 ? -19.661 24.472  27.898 1.00 33.80 ? 806  LYS A NZ  1 
ATOM   6429 N N   . ASP A 1 807 ? -14.801 19.555  26.959 1.00 23.66 ? 807  ASP A N   1 
ATOM   6430 C CA  . ASP A 1 807 ? -14.537 19.006  25.655 1.00 23.29 ? 807  ASP A CA  1 
ATOM   6431 C C   . ASP A 1 807 ? -14.721 20.075  24.567 1.00 23.21 ? 807  ASP A C   1 
ATOM   6432 O O   . ASP A 1 807 ? -15.733 20.768  24.538 1.00 22.37 ? 807  ASP A O   1 
ATOM   6433 C CB  . ASP A 1 807 ? -15.451 17.792  25.426 1.00 23.27 ? 807  ASP A CB  1 
ATOM   6434 C CG  . ASP A 1 807 ? -15.097 17.007  24.174 1.00 24.78 ? 807  ASP A CG  1 
ATOM   6435 O OD1 . ASP A 1 807 ? -15.293 17.553  23.075 1.00 26.59 ? 807  ASP A OD1 1 
ATOM   6436 O OD2 . ASP A 1 807 ? -14.655 15.840  24.285 1.00 25.25 ? 807  ASP A OD2 1 
ATOM   6437 N N   . PRO A 1 808 ? -13.723 20.221  23.662 1.00 22.93 ? 808  PRO A N   1 
ATOM   6438 C CA  . PRO A 1 808 ? -13.800 21.303  22.679 1.00 22.40 ? 808  PRO A CA  1 
ATOM   6439 C C   . PRO A 1 808 ? -14.772 21.079  21.517 1.00 21.60 ? 808  PRO A C   1 
ATOM   6440 O O   . PRO A 1 808 ? -14.973 21.992  20.704 1.00 20.75 ? 808  PRO A O   1 
ATOM   6441 C CB  . PRO A 1 808 ? -12.370 21.369  22.153 1.00 22.40 ? 808  PRO A CB  1 
ATOM   6442 C CG  . PRO A 1 808 ? -11.909 19.946  22.236 1.00 23.07 ? 808  PRO A CG  1 
ATOM   6443 C CD  . PRO A 1 808 ? -12.483 19.440  23.521 1.00 22.98 ? 808  PRO A CD  1 
ATOM   6444 N N   . ASN A 1 809 ? -15.376 19.891  21.449 1.00 21.72 ? 809  ASN A N   1 
ATOM   6445 C CA  . ASN A 1 809 ? -16.214 19.503  20.328 1.00 21.24 ? 809  ASN A CA  1 
ATOM   6446 C C   . ASN A 1 809 ? -17.722 19.767  20.496 1.00 21.70 ? 809  ASN A C   1 
ATOM   6447 O O   . ASN A 1 809 ? -18.524 19.149  19.803 1.00 21.60 ? 809  ASN A O   1 
ATOM   6448 C CB  . ASN A 1 809 ? -15.993 18.037  19.987 1.00 21.21 ? 809  ASN A CB  1 
ATOM   6449 C CG  . ASN A 1 809 ? -14.561 17.750  19.524 1.00 22.09 ? 809  ASN A CG  1 
ATOM   6450 O OD1 . ASN A 1 809 ? -13.869 16.928  20.109 1.00 24.71 ? 809  ASN A OD1 1 
ATOM   6451 N ND2 . ASN A 1 809 ? -14.122 18.443  18.497 1.00 22.16 ? 809  ASN A ND2 1 
ATOM   6452 N N   . ASN A 1 810 ? -18.064 20.675  21.393 1.00 21.44 ? 810  ASN A N   1 
ATOM   6453 C CA  . ASN A 1 810 ? -19.462 21.051  21.704 1.00 23.08 ? 810  ASN A CA  1 
ATOM   6454 C C   . ASN A 1 810 ? -20.410 19.872  21.800 1.00 21.88 ? 810  ASN A C   1 
ATOM   6455 O O   . ASN A 1 810 ? -21.326 19.717  20.993 1.00 21.82 ? 810  ASN A O   1 
ATOM   6456 C CB  . ASN A 1 810 ? -20.017 22.087  20.721 1.00 24.28 ? 810  ASN A CB  1 
ATOM   6457 C CG  . ASN A 1 810 ? -21.166 22.906  21.319 1.00 27.50 ? 810  ASN A CG  1 
ATOM   6458 O OD1 . ASN A 1 810 ? -21.044 23.504  22.413 1.00 32.52 ? 810  ASN A OD1 1 
ATOM   6459 N ND2 . ASN A 1 810 ? -22.281 22.947  20.596 1.00 32.20 ? 810  ASN A ND2 1 
ATOM   6460 N N   . LEU A 1 811 ? -20.149 19.031  22.791 1.00 20.89 ? 811  LEU A N   1 
ATOM   6461 C CA  . LEU A 1 811 ? -20.870 17.792  22.938 1.00 19.71 ? 811  LEU A CA  1 
ATOM   6462 C C   . LEU A 1 811 ? -22.088 18.107  23.743 1.00 18.60 ? 811  LEU A C   1 
ATOM   6463 O O   . LEU A 1 811 ? -22.040 18.927  24.661 1.00 17.91 ? 811  LEU A O   1 
ATOM   6464 C CB  . LEU A 1 811 ? -20.040 16.740  23.662 1.00 18.48 ? 811  LEU A CB  1 
ATOM   6465 C CG  . LEU A 1 811 ? -18.692 16.321  23.039 1.00 19.49 ? 811  LEU A CG  1 
ATOM   6466 C CD1 . LEU A 1 811 ? -18.008 15.263  23.909 1.00 17.54 ? 811  LEU A CD1 1 
ATOM   6467 C CD2 . LEU A 1 811 ? -18.939 15.790  21.647 1.00 16.50 ? 811  LEU A CD2 1 
ATOM   6468 N N   . ALA A 1 812 ? -23.160 17.406  23.429 1.00 18.01 ? 812  ALA A N   1 
ATOM   6469 C CA  . ALA A 1 812 ? -24.411 17.641  24.128 1.00 18.78 ? 812  ALA A CA  1 
ATOM   6470 C C   . ALA A 1 812 ? -25.256 16.402  23.976 1.00 18.30 ? 812  ALA A C   1 
ATOM   6471 O O   . ALA A 1 812 ? -25.249 15.760  22.920 1.00 18.43 ? 812  ALA A O   1 
ATOM   6472 C CB  . ALA A 1 812 ? -25.137 18.833  23.521 1.00 18.16 ? 812  ALA A CB  1 
ATOM   6473 N N   . PHE A 1 813 ? -25.957 16.058  25.036 1.00 18.89 ? 813  PHE A N   1 
ATOM   6474 C CA  . PHE A 1 813 ? -27.076 15.111  24.924 1.00 19.75 ? 813  PHE A CA  1 
ATOM   6475 C C   . PHE A 1 813 ? -28.100 15.732  23.991 1.00 20.67 ? 813  PHE A C   1 
ATOM   6476 O O   . PHE A 1 813 ? -28.613 16.822  24.272 1.00 22.27 ? 813  PHE A O   1 
ATOM   6477 C CB  . PHE A 1 813 ? -27.662 14.782  26.306 1.00 19.38 ? 813  PHE A CB  1 
ATOM   6478 C CG  . PHE A 1 813 ? -26.630 14.344  27.305 1.00 19.29 ? 813  PHE A CG  1 
ATOM   6479 C CD1 . PHE A 1 813 ? -26.106 13.055  27.270 1.00 18.00 ? 813  PHE A CD1 1 
ATOM   6480 C CD2 . PHE A 1 813 ? -26.139 15.236  28.250 1.00 21.70 ? 813  PHE A CD2 1 
ATOM   6481 C CE1 . PHE A 1 813 ? -25.110 12.660  28.155 1.00 16.33 ? 813  PHE A CE1 1 
ATOM   6482 C CE2 . PHE A 1 813 ? -25.137 14.842  29.148 1.00 21.46 ? 813  PHE A CE2 1 
ATOM   6483 C CZ  . PHE A 1 813 ? -24.634 13.554  29.106 1.00 18.73 ? 813  PHE A CZ  1 
ATOM   6484 N N   . ASN A 1 814 ? -28.364 15.087  22.857 1.00 21.59 ? 814  ASN A N   1 
ATOM   6485 C CA  . ASN A 1 814 ? -29.446 15.538  21.962 1.00 22.54 ? 814  ASN A CA  1 
ATOM   6486 C C   . ASN A 1 814 ? -30.589 14.551  21.853 1.00 22.75 ? 814  ASN A C   1 
ATOM   6487 O O   . ASN A 1 814 ? -31.469 14.717  21.020 1.00 23.02 ? 814  ASN A O   1 
ATOM   6488 C CB  . ASN A 1 814 ? -28.918 15.868  20.559 1.00 22.98 ? 814  ASN A CB  1 
ATOM   6489 C CG  . ASN A 1 814 ? -28.524 14.640  19.794 1.00 23.70 ? 814  ASN A CG  1 
ATOM   6490 O OD1 . ASN A 1 814 ? -28.327 13.579  20.372 1.00 25.88 ? 814  ASN A OD1 1 
ATOM   6491 N ND2 . ASN A 1 814 ? -28.427 14.763  18.471 1.00 28.39 ? 814  ASN A ND2 1 
ATOM   6492 N N   . GLU A 1 815 ? -30.545 13.491  22.661 1.00 23.38 ? 815  GLU A N   1 
ATOM   6493 C CA  . GLU A 1 815 ? -31.632 12.496  22.701 1.00 23.79 ? 815  GLU A CA  1 
ATOM   6494 C C   . GLU A 1 815 ? -31.724 11.908  24.109 1.00 23.41 ? 815  GLU A C   1 
ATOM   6495 O O   . GLU A 1 815 ? -30.683 11.584  24.731 1.00 22.94 ? 815  GLU A O   1 
ATOM   6496 C CB  . GLU A 1 815 ? -31.476 11.378  21.632 1.00 23.77 ? 815  GLU A CB  1 
ATOM   6497 C CG  . GLU A 1 815 ? -32.712 10.465  21.530 1.00 24.69 ? 815  GLU A CG  1 
ATOM   6498 C CD  . GLU A 1 815 ? -32.653 9.307   20.513 1.00 26.53 ? 815  GLU A CD  1 
ATOM   6499 O OE1 . GLU A 1 815 ? -32.548 9.545   19.291 1.00 31.42 ? 815  GLU A OE1 1 
ATOM   6500 O OE2 . GLU A 1 815 ? -32.800 8.128   20.934 1.00 32.46 ? 815  GLU A OE2 1 
ATOM   6501 N N   . ILE A 1 816 ? -32.959 11.825  24.623 1.00 22.50 ? 816  ILE A N   1 
ATOM   6502 C CA  . ILE A 1 816 ? -33.267 11.087  25.853 1.00 21.15 ? 816  ILE A CA  1 
ATOM   6503 C C   . ILE A 1 816 ? -34.353 10.037  25.576 1.00 21.83 ? 816  ILE A C   1 
ATOM   6504 O O   . ILE A 1 816 ? -35.461 10.360  25.131 1.00 21.49 ? 816  ILE A O   1 
ATOM   6505 C CB  . ILE A 1 816 ? -33.654 12.018  27.033 1.00 21.20 ? 816  ILE A CB  1 
ATOM   6506 C CG1 . ILE A 1 816 ? -32.592 13.114  27.249 1.00 21.15 ? 816  ILE A CG1 1 
ATOM   6507 C CG2 . ILE A 1 816 ? -33.835 11.212  28.313 1.00 20.44 ? 816  ILE A CG2 1 
ATOM   6508 C CD1 . ILE A 1 816 ? -33.003 14.228  28.196 1.00 20.14 ? 816  ILE A CD1 1 
ATOM   6509 N N   . LYS A 1 817 ? -34.015 8.775   25.823 1.00 20.71 ? 817  LYS A N   1 
ATOM   6510 C CA  . LYS A 1 817 ? -34.940 7.691   25.657 1.00 21.08 ? 817  LYS A CA  1 
ATOM   6511 C C   . LYS A 1 817 ? -35.306 7.243   27.068 1.00 20.74 ? 817  LYS A C   1 
ATOM   6512 O O   . LYS A 1 817 ? -34.425 6.927   27.848 1.00 21.12 ? 817  LYS A O   1 
ATOM   6513 C CB  . LYS A 1 817 ? -34.270 6.558   24.877 1.00 20.65 ? 817  LYS A CB  1 
ATOM   6514 C CG  . LYS A 1 817 ? -35.148 5.380   24.585 1.00 22.69 ? 817  LYS A CG  1 
ATOM   6515 C CD  . LYS A 1 817 ? -34.377 4.401   23.745 1.00 24.17 ? 817  LYS A CD  1 
ATOM   6516 C CE  . LYS A 1 817 ? -35.306 3.587   22.889 1.00 27.08 ? 817  LYS A CE  1 
ATOM   6517 N NZ  . LYS A 1 817 ? -34.505 2.587   22.084 1.00 30.33 ? 817  LYS A NZ  1 
ATOM   6518 N N   . ILE A 1 818 ? -36.604 7.247   27.382 1.00 19.47 ? 818  ILE A N   1 
ATOM   6519 C CA  . ILE A 1 818 ? -37.103 6.822   28.699 1.00 19.34 ? 818  ILE A CA  1 
ATOM   6520 C C   . ILE A 1 818 ? -37.833 5.508   28.501 1.00 19.12 ? 818  ILE A C   1 
ATOM   6521 O O   . ILE A 1 818 ? -38.710 5.414   27.643 1.00 17.76 ? 818  ILE A O   1 
ATOM   6522 C CB  . ILE A 1 818 ? -38.055 7.902   29.376 1.00 19.42 ? 818  ILE A CB  1 
ATOM   6523 C CG1 . ILE A 1 818 ? -37.380 9.283   29.379 1.00 18.57 ? 818  ILE A CG1 1 
ATOM   6524 C CG2 . ILE A 1 818 ? -38.403 7.495   30.790 1.00 18.25 ? 818  ILE A CG2 1 
ATOM   6525 C CD1 . ILE A 1 818 ? -38.312 10.487  29.623 1.00 18.89 ? 818  ILE A CD1 1 
ATOM   6526 N N   . LEU A 1 819 ? -37.427 4.497   29.270 1.00 18.84 ? 819  LEU A N   1 
ATOM   6527 C CA  . LEU A 1 819 ? -38.002 3.155   29.204 1.00 19.98 ? 819  LEU A CA  1 
ATOM   6528 C C   . LEU A 1 819 ? -39.003 2.947   30.349 1.00 19.74 ? 819  LEU A C   1 
ATOM   6529 O O   . LEU A 1 819 ? -38.786 3.432   31.449 1.00 19.71 ? 819  LEU A O   1 
ATOM   6530 C CB  . LEU A 1 819 ? -36.893 2.080   29.266 1.00 18.93 ? 819  LEU A CB  1 
ATOM   6531 C CG  . LEU A 1 819 ? -35.777 2.258   28.215 1.00 19.89 ? 819  LEU A CG  1 
ATOM   6532 C CD1 . LEU A 1 819 ? -34.779 1.114   28.236 1.00 14.29 ? 819  LEU A CD1 1 
ATOM   6533 C CD2 . LEU A 1 819 ? -36.434 2.385   26.825 1.00 17.87 ? 819  LEU A CD2 1 
ATOM   6534 N N   . GLY A 1 820 ? -40.074 2.214   30.080 1.00 20.19 ? 820  GLY A N   1 
ATOM   6535 C CA  . GLY A 1 820 ? -41.116 1.927   31.111 1.00 20.37 ? 820  GLY A CA  1 
ATOM   6536 C C   . GLY A 1 820 ? -41.837 3.159   31.609 1.00 21.74 ? 820  GLY A C   1 
ATOM   6537 O O   . GLY A 1 820 ? -42.119 3.291   32.803 1.00 22.08 ? 820  GLY A O   1 
ATOM   6538 N N   . THR A 1 821 ? -42.168 4.068   30.698 1.00 21.78 ? 821  THR A N   1 
ATOM   6539 C CA  . THR A 1 821 ? -42.843 5.299   31.104 1.00 23.21 ? 821  THR A CA  1 
ATOM   6540 C C   . THR A 1 821 ? -44.258 5.410   30.518 1.00 23.64 ? 821  THR A C   1 
ATOM   6541 O O   . THR A 1 821 ? -44.559 4.858   29.465 1.00 23.17 ? 821  THR A O   1 
ATOM   6542 C CB  . THR A 1 821 ? -42.020 6.546   30.752 1.00 23.35 ? 821  THR A CB  1 
ATOM   6543 O OG1 . THR A 1 821 ? -42.724 7.723   31.176 1.00 24.37 ? 821  THR A OG1 1 
ATOM   6544 C CG2 . THR A 1 821 ? -41.741 6.616   29.241 1.00 22.60 ? 821  THR A CG2 1 
ATOM   6545 N N   . GLU A 1 822 ? -45.133 6.115   31.219 1.00 24.91 ? 822  GLU A N   1 
ATOM   6546 C CA  . GLU A 1 822 ? -46.410 6.510   30.615 1.00 26.42 ? 822  GLU A CA  1 
ATOM   6547 C C   . GLU A 1 822 ? -46.150 7.723   29.721 1.00 26.68 ? 822  GLU A C   1 
ATOM   6548 O O   . GLU A 1 822 ? -45.093 8.338   29.832 1.00 26.39 ? 822  GLU A O   1 
ATOM   6549 C CB  . GLU A 1 822 ? -47.461 6.776   31.706 1.00 27.07 ? 822  GLU A CB  1 
ATOM   6550 C CG  . GLU A 1 822 ? -47.860 5.496   32.465 1.00 28.93 ? 822  GLU A CG  1 
ATOM   6551 C CD  . GLU A 1 822 ? -48.574 4.469   31.574 1.00 34.57 ? 822  GLU A CD  1 
ATOM   6552 O OE1 . GLU A 1 822 ? -49.424 4.866   30.746 1.00 34.84 ? 822  GLU A OE1 1 
ATOM   6553 O OE2 . GLU A 1 822 ? -48.286 3.256   31.704 1.00 36.81 ? 822  GLU A OE2 1 
ATOM   6554 N N   . GLU A 1 823 ? -47.075 8.078   28.825 1.00 27.87 ? 823  GLU A N   1 
ATOM   6555 C CA  . GLU A 1 823 ? -46.799 9.203   27.909 1.00 28.88 ? 823  GLU A CA  1 
ATOM   6556 C C   . GLU A 1 823 ? -46.398 10.507  28.627 1.00 29.89 ? 823  GLU A C   1 
ATOM   6557 O O   . GLU A 1 823 ? -47.193 11.032  29.420 1.00 29.67 ? 823  GLU A O   1 
ATOM   6558 C CB  . GLU A 1 823 ? -47.974 9.444   26.968 1.00 29.68 ? 823  GLU A CB  1 
ATOM   6559 C CG  . GLU A 1 823 ? -47.678 10.471  25.903 1.00 30.74 ? 823  GLU A CG  1 
ATOM   6560 C CD  . GLU A 1 823 ? -48.663 10.454  24.760 1.00 34.72 ? 823  GLU A CD  1 
ATOM   6561 O OE1 . GLU A 1 823 ? -49.772 9.878   24.911 1.00 36.31 ? 823  GLU A OE1 1 
ATOM   6562 O OE2 . GLU A 1 823 ? -48.322 11.033  23.700 1.00 36.03 ? 823  GLU A OE2 1 
ATOM   6563 N N   . PRO A 1 824 ? -45.166 11.026  28.369 1.00 29.71 ? 824  PRO A N   1 
ATOM   6564 C CA  . PRO A 1 824 ? -44.802 12.322  28.928 1.00 30.78 ? 824  PRO A CA  1 
ATOM   6565 C C   . PRO A 1 824 ? -45.481 13.449  28.137 1.00 32.13 ? 824  PRO A C   1 
ATOM   6566 O O   . PRO A 1 824 ? -45.648 13.342  26.913 1.00 33.04 ? 824  PRO A O   1 
ATOM   6567 C CB  . PRO A 1 824 ? -43.265 12.402  28.763 1.00 30.54 ? 824  PRO A CB  1 
ATOM   6568 C CG  . PRO A 1 824 ? -42.842 11.183  28.037 1.00 29.79 ? 824  PRO A CG  1 
ATOM   6569 C CD  . PRO A 1 824 ? -44.083 10.460  27.543 1.00 30.44 ? 824  PRO A CD  1 
ATOM   6570 N N   . SER A 1 825 ? -45.894 14.498  28.843 1.00 32.66 ? 825  SER A N   1 
ATOM   6571 C CA  . SER A 1 825 ? -46.496 15.688  28.230 1.00 33.27 ? 825  SER A CA  1 
ATOM   6572 C C   . SER A 1 825 ? -45.853 16.909  28.871 1.00 33.29 ? 825  SER A C   1 
ATOM   6573 O O   . SER A 1 825 ? -45.247 16.784  29.934 1.00 33.58 ? 825  SER A O   1 
ATOM   6574 C CB  . SER A 1 825 ? -48.018 15.697  28.447 1.00 33.50 ? 825  SER A CB  1 
ATOM   6575 O OG  . SER A 1 825 ? -48.349 16.017  29.788 1.00 33.92 ? 825  SER A OG  1 
ATOM   6576 N N   . ASN A 1 826 ? -45.995 18.071  28.231 1.00 33.24 ? 826  ASN A N   1 
ATOM   6577 C CA  . ASN A 1 826 ? -45.394 19.346  28.672 1.00 33.00 ? 826  ASN A CA  1 
ATOM   6578 C C   . ASN A 1 826 ? -43.908 19.222  29.064 1.00 32.04 ? 826  ASN A C   1 
ATOM   6579 O O   . ASN A 1 826 ? -43.537 19.586  30.177 1.00 31.90 ? 826  ASN A O   1 
ATOM   6580 C CB  . ASN A 1 826 ? -46.157 19.991  29.846 1.00 33.24 ? 826  ASN A CB  1 
ATOM   6581 C CG  . ASN A 1 826 ? -47.682 20.063  29.638 1.00 36.28 ? 826  ASN A CG  1 
ATOM   6582 O OD1 . ASN A 1 826 ? -48.202 20.028  28.508 1.00 39.16 ? 826  ASN A OD1 1 
ATOM   6583 N ND2 . ASN A 1 826 ? -48.402 20.171  30.750 1.00 36.94 ? 826  ASN A ND2 1 
ATOM   6584 N N   . VAL A 1 827 ? -43.072 18.715  28.163 1.00 31.02 ? 827  VAL A N   1 
ATOM   6585 C CA  . VAL A 1 827 ? -41.641 18.579  28.460 1.00 29.66 ? 827  VAL A CA  1 
ATOM   6586 C C   . VAL A 1 827 ? -40.936 19.946  28.489 1.00 29.67 ? 827  VAL A C   1 
ATOM   6587 O O   . VAL A 1 827 ? -40.887 20.682  27.496 1.00 29.04 ? 827  VAL A O   1 
ATOM   6588 C CB  . VAL A 1 827 ? -40.950 17.534  27.545 1.00 29.50 ? 827  VAL A CB  1 
ATOM   6589 C CG1 . VAL A 1 827 ? -39.497 17.321  27.962 1.00 27.58 ? 827  VAL A CG1 1 
ATOM   6590 C CG2 . VAL A 1 827 ? -41.704 16.208  27.614 1.00 28.29 ? 827  VAL A CG2 1 
ATOM   6591 N N   . THR A 1 828 ? -40.431 20.286  29.667 1.00 30.54 ? 828  THR A N   1 
ATOM   6592 C CA  . THR A 1 828 ? -39.723 21.544  29.927 1.00 31.22 ? 828  THR A CA  1 
ATOM   6593 C C   . THR A 1 828 ? -38.262 21.259  30.296 1.00 31.40 ? 828  THR A C   1 
ATOM   6594 O O   . THR A 1 828 ? -37.977 20.318  31.040 1.00 30.57 ? 828  THR A O   1 
ATOM   6595 C CB  . THR A 1 828 ? -40.376 22.314  31.100 1.00 31.59 ? 828  THR A CB  1 
ATOM   6596 O OG1 . THR A 1 828 ? -41.794 22.455  30.864 1.00 34.33 ? 828  THR A OG1 1 
ATOM   6597 C CG2 . THR A 1 828 ? -39.767 23.698  31.226 1.00 32.21 ? 828  THR A CG2 1 
ATOM   6598 N N   . VAL A 1 829 ? -37.355 22.089  29.791 1.00 31.38 ? 829  VAL A N   1 
ATOM   6599 C CA  . VAL A 1 829 ? -35.922 21.928  30.024 1.00 32.39 ? 829  VAL A CA  1 
ATOM   6600 C C   . VAL A 1 829 ? -35.450 23.221  30.655 1.00 33.06 ? 829  VAL A C   1 
ATOM   6601 O O   . VAL A 1 829 ? -35.568 24.282  30.049 1.00 32.94 ? 829  VAL A O   1 
ATOM   6602 C CB  . VAL A 1 829 ? -35.151 21.684  28.698 1.00 31.86 ? 829  VAL A CB  1 
ATOM   6603 C CG1 . VAL A 1 829 ? -33.657 21.557  28.941 1.00 32.61 ? 829  VAL A CG1 1 
ATOM   6604 C CG2 . VAL A 1 829 ? -35.687 20.477  27.978 1.00 30.78 ? 829  VAL A CG2 1 
ATOM   6605 N N   . LYS A 1 830 ? -34.964 23.146  31.885 1.00 33.93 ? 830  LYS A N   1 
ATOM   6606 C CA  . LYS A 1 830 ? -34.462 24.334  32.557 1.00 35.76 ? 830  LYS A CA  1 
ATOM   6607 C C   . LYS A 1 830 ? -32.960 24.232  32.784 1.00 36.58 ? 830  LYS A C   1 
ATOM   6608 O O   . LYS A 1 830 ? -32.452 23.159  33.065 1.00 35.87 ? 830  LYS A O   1 
ATOM   6609 C CB  . LYS A 1 830 ? -35.218 24.575  33.865 1.00 35.62 ? 830  LYS A CB  1 
ATOM   6610 C CG  . LYS A 1 830 ? -36.735 24.716  33.654 1.00 36.68 ? 830  LYS A CG  1 
ATOM   6611 C CD  . LYS A 1 830 ? -37.455 25.330  34.850 1.00 36.71 ? 830  LYS A CD  1 
ATOM   6612 C CE  . LYS A 1 830 ? -38.980 25.312  34.623 1.00 39.82 ? 830  LYS A CE  1 
ATOM   6613 N NZ  . LYS A 1 830 ? -39.756 25.842  35.795 1.00 42.06 ? 830  LYS A NZ  1 
ATOM   6614 N N   . HIS A 1 831 ? -32.273 25.358  32.627 1.00 38.92 ? 831  HIS A N   1 
ATOM   6615 C CA  . HIS A 1 831 ? -30.849 25.497  32.876 1.00 41.05 ? 831  HIS A CA  1 
ATOM   6616 C C   . HIS A 1 831 ? -30.707 26.458  34.052 1.00 42.76 ? 831  HIS A C   1 
ATOM   6617 O O   . HIS A 1 831 ? -30.944 27.655  33.899 1.00 42.96 ? 831  HIS A O   1 
ATOM   6618 C CB  . HIS A 1 831 ? -30.184 26.090  31.635 1.00 41.34 ? 831  HIS A CB  1 
ATOM   6619 C CG  . HIS A 1 831 ? -28.688 26.032  31.643 1.00 42.45 ? 831  HIS A CG  1 
ATOM   6620 N ND1 . HIS A 1 831 ? -27.930 26.347  30.533 1.00 43.83 ? 831  HIS A ND1 1 
ATOM   6621 C CD2 . HIS A 1 831 ? -27.808 25.687  32.614 1.00 43.87 ? 831  HIS A CD2 1 
ATOM   6622 C CE1 . HIS A 1 831 ? -26.647 26.208  30.825 1.00 44.69 ? 831  HIS A CE1 1 
ATOM   6623 N NE2 . HIS A 1 831 ? -26.547 25.807  32.080 1.00 44.83 ? 831  HIS A NE2 1 
ATOM   6624 N N   . ASN A 1 832 ? -30.329 25.931  35.220 1.00 44.99 ? 832  ASN A N   1 
ATOM   6625 C CA  . ASN A 1 832 ? -30.346 26.676  36.494 1.00 46.72 ? 832  ASN A CA  1 
ATOM   6626 C C   . ASN A 1 832 ? -31.688 27.364  36.741 1.00 47.91 ? 832  ASN A C   1 
ATOM   6627 O O   . ASN A 1 832 ? -31.743 28.560  37.038 1.00 48.45 ? 832  ASN A O   1 
ATOM   6628 C CB  . ASN A 1 832 ? -29.192 27.687  36.581 1.00 46.98 ? 832  ASN A CB  1 
ATOM   6629 C CG  . ASN A 1 832 ? -27.827 27.051  36.344 1.00 47.61 ? 832  ASN A CG  1 
ATOM   6630 O OD1 . ASN A 1 832 ? -27.466 26.060  36.981 1.00 48.56 ? 832  ASN A OD1 1 
ATOM   6631 N ND2 . ASN A 1 832 ? -27.059 27.632  35.431 1.00 48.45 ? 832  ASN A ND2 1 
ATOM   6632 N N   . GLY A 1 833 ? -32.771 26.605  36.590 1.00 49.00 ? 833  GLY A N   1 
ATOM   6633 C CA  . GLY A 1 833 ? -34.117 27.114  36.836 1.00 50.29 ? 833  GLY A CA  1 
ATOM   6634 C C   . GLY A 1 833 ? -34.670 28.014  35.748 1.00 51.18 ? 833  GLY A C   1 
ATOM   6635 O O   . GLY A 1 833 ? -35.815 28.452  35.836 1.00 51.35 ? 833  GLY A O   1 
ATOM   6636 N N   . VAL A 1 834 ? -33.864 28.272  34.720 1.00 51.87 ? 834  VAL A N   1 
ATOM   6637 C CA  . VAL A 1 834 ? -34.226 29.190  33.641 1.00 52.67 ? 834  VAL A CA  1 
ATOM   6638 C C   . VAL A 1 834 ? -34.723 28.450  32.389 1.00 53.37 ? 834  VAL A C   1 
ATOM   6639 O O   . VAL A 1 834 ? -33.940 27.776  31.714 1.00 53.03 ? 834  VAL A O   1 
ATOM   6640 C CB  . VAL A 1 834 ? -33.035 30.103  33.260 1.00 52.60 ? 834  VAL A CB  1 
ATOM   6641 C CG1 . VAL A 1 834 ? -33.499 31.263  32.391 1.00 52.73 ? 834  VAL A CG1 1 
ATOM   6642 C CG2 . VAL A 1 834 ? -32.316 30.613  34.515 1.00 52.97 ? 834  VAL A CG2 1 
ATOM   6643 N N   . PRO A 1 835 ? -36.036 28.558  32.089 1.00 54.23 ? 835  PRO A N   1 
ATOM   6644 C CA  . PRO A 1 835 ? -36.588 28.033  30.848 1.00 54.87 ? 835  PRO A CA  1 
ATOM   6645 C C   . PRO A 1 835 ? -36.820 29.129  29.800 1.00 55.93 ? 835  PRO A C   1 
ATOM   6646 O O   . PRO A 1 835 ? -37.506 30.123  30.097 1.00 56.11 ? 835  PRO A O   1 
ATOM   6647 C CB  . PRO A 1 835 ? -37.944 27.484  31.299 1.00 55.24 ? 835  PRO A CB  1 
ATOM   6648 C CG  . PRO A 1 835 ? -38.341 28.376  32.515 1.00 54.45 ? 835  PRO A CG  1 
ATOM   6649 C CD  . PRO A 1 835 ? -37.096 29.131  32.945 1.00 54.25 ? 835  PRO A CD  1 
ATOM   6650 N N   . SER A 1 836 ? -36.266 29.000  28.593 1.00 56.59 ? 836  SER A N   1 
ATOM   6651 C CA  . SER A 1 836 ? -35.271 28.010  28.195 1.00 57.12 ? 836  SER A CA  1 
ATOM   6652 C C   . SER A 1 836 ? -34.706 28.455  26.841 1.00 57.58 ? 836  SER A C   1 
ATOM   6653 O O   . SER A 1 836 ? -35.351 28.308  25.792 1.00 57.53 ? 836  SER A O   1 
ATOM   6654 C CB  . SER A 1 836 ? -35.871 26.610  28.062 1.00 57.27 ? 836  SER A CB  1 
ATOM   6655 O OG  . SER A 1 836 ? -34.947 25.731  27.440 1.00 56.96 ? 836  SER A OG  1 
ATOM   6656 N N   . SER A 1 839 ? -39.357 24.053  23.243 1.00 30.07 ? 839  SER A N   1 
ATOM   6657 C CA  . SER A 1 839 ? -40.026 22.782  23.507 1.00 29.94 ? 839  SER A CA  1 
ATOM   6658 C C   . SER A 1 839 ? -39.361 21.649  22.722 1.00 28.62 ? 839  SER A C   1 
ATOM   6659 O O   . SER A 1 839 ? -39.288 21.704  21.481 1.00 29.54 ? 839  SER A O   1 
ATOM   6660 C CB  . SER A 1 839 ? -41.527 22.868  23.174 1.00 30.69 ? 839  SER A CB  1 
ATOM   6661 O OG  . SER A 1 839 ? -42.168 21.601  23.345 1.00 33.47 ? 839  SER A OG  1 
ATOM   6662 N N   . PRO A 1 840 ? -38.802 20.653  23.437 1.00 26.63 ? 840  PRO A N   1 
ATOM   6663 C CA  . PRO A 1 840 ? -38.268 19.475  22.776 1.00 25.22 ? 840  PRO A CA  1 
ATOM   6664 C C   . PRO A 1 840 ? -39.341 18.718  22.025 1.00 24.38 ? 840  PRO A C   1 
ATOM   6665 O O   . PRO A 1 840 ? -40.516 18.822  22.358 1.00 24.00 ? 840  PRO A O   1 
ATOM   6666 C CB  . PRO A 1 840 ? -37.793 18.610  23.935 1.00 24.59 ? 840  PRO A CB  1 
ATOM   6667 C CG  . PRO A 1 840 ? -38.428 19.164  25.128 1.00 26.34 ? 840  PRO A CG  1 
ATOM   6668 C CD  . PRO A 1 840 ? -38.554 20.607  24.885 1.00 26.50 ? 840  PRO A CD  1 
ATOM   6669 N N   . THR A 1 841 ? -38.917 17.943  21.035 1.00 23.09 ? 841  THR A N   1 
ATOM   6670 C CA  . THR A 1 841 ? -39.793 16.984  20.370 1.00 21.32 ? 841  THR A CA  1 
ATOM   6671 C C   . THR A 1 841 ? -39.889 15.716  21.211 1.00 21.23 ? 841  THR A C   1 
ATOM   6672 O O   . THR A 1 841 ? -38.889 15.242  21.743 1.00 20.25 ? 841  THR A O   1 
ATOM   6673 C CB  . THR A 1 841 ? -39.270 16.682  18.956 1.00 21.00 ? 841  THR A CB  1 
ATOM   6674 O OG1 . THR A 1 841 ? -39.464 17.840  18.149 1.00 19.31 ? 841  THR A OG1 1 
ATOM   6675 C CG2 . THR A 1 841 ? -39.997 15.506  18.305 1.00 20.97 ? 841  THR A CG2 1 
ATOM   6676 N N   . VAL A 1 842 ? -41.105 15.179  21.335 1.00 20.85 ? 842  VAL A N   1 
ATOM   6677 C CA  . VAL A 1 842 ? -41.345 13.958  22.099 1.00 21.19 ? 842  VAL A CA  1 
ATOM   6678 C C   . VAL A 1 842 ? -42.088 12.971  21.202 1.00 21.25 ? 842  VAL A C   1 
ATOM   6679 O O   . VAL A 1 842 ? -43.150 13.306  20.630 1.00 20.32 ? 842  VAL A O   1 
ATOM   6680 C CB  . VAL A 1 842 ? -42.155 14.239  23.422 1.00 22.22 ? 842  VAL A CB  1 
ATOM   6681 C CG1 . VAL A 1 842 ? -42.413 12.959  24.192 1.00 21.59 ? 842  VAL A CG1 1 
ATOM   6682 C CG2 . VAL A 1 842 ? -41.418 15.260  24.309 1.00 21.73 ? 842  VAL A CG2 1 
ATOM   6683 N N   . THR A 1 843 ? -41.485 11.792  21.029 1.00 19.94 ? 843  THR A N   1 
ATOM   6684 C CA  . THR A 1 843 ? -42.072 10.684  20.298 1.00 20.44 ? 843  THR A CA  1 
ATOM   6685 C C   . THR A 1 843 ? -42.448 9.613   21.319 1.00 20.50 ? 843  THR A C   1 
ATOM   6686 O O   . THR A 1 843 ? -41.662 9.305   22.220 1.00 20.63 ? 843  THR A O   1 
ATOM   6687 C CB  . THR A 1 843 ? -41.096 10.132  19.241 1.00 20.48 ? 843  THR A CB  1 
ATOM   6688 O OG1 . THR A 1 843 ? -40.525 11.230  18.510 1.00 22.61 ? 843  THR A OG1 1 
ATOM   6689 C CG2 . THR A 1 843 ? -41.802 9.218   18.269 1.00 21.00 ? 843  THR A CG2 1 
ATOM   6690 N N   . TYR A 1 844 ? -43.654 9.061   21.203 1.00 20.48 ? 844  TYR A N   1 
ATOM   6691 C CA  . TYR A 1 844 ? -44.102 8.091   22.191 1.00 20.41 ? 844  TYR A CA  1 
ATOM   6692 C C   . TYR A 1 844 ? -44.662 6.814   21.559 1.00 21.02 ? 844  TYR A C   1 
ATOM   6693 O O   . TYR A 1 844 ? -45.424 6.841   20.575 1.00 19.71 ? 844  TYR A O   1 
ATOM   6694 C CB  . TYR A 1 844 ? -45.072 8.733   23.236 1.00 20.60 ? 844  TYR A CB  1 
ATOM   6695 C CG  . TYR A 1 844 ? -45.445 7.771   24.351 1.00 19.91 ? 844  TYR A CG  1 
ATOM   6696 C CD1 . TYR A 1 844 ? -44.487 7.341   25.268 1.00 22.28 ? 844  TYR A CD1 1 
ATOM   6697 C CD2 . TYR A 1 844 ? -46.734 7.214   24.432 1.00 21.81 ? 844  TYR A CD2 1 
ATOM   6698 C CE1 . TYR A 1 844 ? -44.807 6.417   26.273 1.00 22.19 ? 844  TYR A CE1 1 
ATOM   6699 C CE2 . TYR A 1 844 ? -47.070 6.290   25.450 1.00 20.22 ? 844  TYR A CE2 1 
ATOM   6700 C CZ  . TYR A 1 844 ? -46.091 5.894   26.356 1.00 21.37 ? 844  TYR A CZ  1 
ATOM   6701 O OH  . TYR A 1 844 ? -46.394 4.991   27.365 1.00 20.36 ? 844  TYR A OH  1 
ATOM   6702 N N   . ASP A 1 845 ? -44.255 5.683   22.136 1.00 21.65 ? 845  ASP A N   1 
ATOM   6703 C CA  . ASP A 1 845 ? -44.715 4.388   21.712 1.00 22.32 ? 845  ASP A CA  1 
ATOM   6704 C C   . ASP A 1 845 ? -45.523 3.812   22.869 1.00 23.34 ? 845  ASP A C   1 
ATOM   6705 O O   . ASP A 1 845 ? -44.976 3.325   23.845 1.00 22.27 ? 845  ASP A O   1 
ATOM   6706 C CB  . ASP A 1 845 ? -43.528 3.490   21.307 1.00 22.88 ? 845  ASP A CB  1 
ATOM   6707 C CG  . ASP A 1 845 ? -43.964 2.145   20.738 1.00 23.91 ? 845  ASP A CG  1 
ATOM   6708 O OD1 . ASP A 1 845 ? -44.898 1.540   21.272 1.00 28.54 ? 845  ASP A OD1 1 
ATOM   6709 O OD2 . ASP A 1 845 ? -43.380 1.672   19.752 1.00 23.75 ? 845  ASP A OD2 1 
ATOM   6710 N N   . SER A 1 846 ? -46.849 3.872   22.736 1.00 24.23 ? 846  SER A N   1 
ATOM   6711 C CA  . SER A 1 846 ? -47.749 3.455   23.802 1.00 25.22 ? 846  SER A CA  1 
ATOM   6712 C C   . SER A 1 846 ? -47.759 1.957   24.038 1.00 25.19 ? 846  SER A C   1 
ATOM   6713 O O   . SER A 1 846 ? -47.992 1.524   25.156 1.00 25.79 ? 846  SER A O   1 
ATOM   6714 C CB  . SER A 1 846 ? -49.166 3.953   23.516 1.00 25.60 ? 846  SER A CB  1 
ATOM   6715 O OG  . SER A 1 846 ? -49.670 3.244   22.411 1.00 25.84 ? 846  SER A OG  1 
ATOM   6716 N N   . ASN A 1 847 ? -47.501 1.163   22.999 1.00 25.14 ? 847  ASN A N   1 
ATOM   6717 C CA  . ASN A 1 847 ? -47.398 -0.288  23.155 1.00 25.58 ? 847  ASN A CA  1 
ATOM   6718 C C   . ASN A 1 847 ? -46.188 -0.673  24.002 1.00 24.84 ? 847  ASN A C   1 
ATOM   6719 O O   . ASN A 1 847 ? -46.292 -1.460  24.950 1.00 25.10 ? 847  ASN A O   1 
ATOM   6720 C CB  . ASN A 1 847 ? -47.291 -0.987  21.793 1.00 26.04 ? 847  ASN A CB  1 
ATOM   6721 C CG  . ASN A 1 847 ? -47.262 -2.509  21.917 1.00 31.13 ? 847  ASN A CG  1 
ATOM   6722 O OD1 . ASN A 1 847 ? -46.211 -3.158  21.725 1.00 33.81 ? 847  ASN A OD1 1 
ATOM   6723 N ND2 . ASN A 1 847 ? -48.412 -3.093  22.285 1.00 34.57 ? 847  ASN A ND2 1 
ATOM   6724 N N   . LEU A 1 848 ? -45.042 -0.107  23.645 1.00 23.38 ? 848  LEU A N   1 
ATOM   6725 C CA  . LEU A 1 848 ? -43.777 -0.461  24.284 1.00 22.08 ? 848  LEU A CA  1 
ATOM   6726 C C   . LEU A 1 848 ? -43.511 0.295   25.575 1.00 21.31 ? 848  LEU A C   1 
ATOM   6727 O O   . LEU A 1 848 ? -42.611 -0.088  26.327 1.00 21.23 ? 848  LEU A O   1 
ATOM   6728 C CB  . LEU A 1 848 ? -42.637 -0.204  23.296 1.00 22.49 ? 848  LEU A CB  1 
ATOM   6729 C CG  . LEU A 1 848 ? -42.178 -1.422  22.495 1.00 23.62 ? 848  LEU A CG  1 
ATOM   6730 C CD1 . LEU A 1 848 ? -43.288 -2.433  22.206 1.00 24.76 ? 848  LEU A CD1 1 
ATOM   6731 C CD2 . LEU A 1 848 ? -41.508 -0.971  21.219 1.00 25.51 ? 848  LEU A CD2 1 
ATOM   6732 N N   . LYS A 1 849 ? -44.261 1.377   25.820 1.00 19.89 ? 849  LYS A N   1 
ATOM   6733 C CA  . LYS A 1 849 ? -44.011 2.293   26.951 1.00 19.50 ? 849  LYS A CA  1 
ATOM   6734 C C   . LYS A 1 849 ? -42.615 2.984   26.869 1.00 19.88 ? 849  LYS A C   1 
ATOM   6735 O O   . LYS A 1 849 ? -41.893 3.103   27.863 1.00 17.58 ? 849  LYS A O   1 
ATOM   6736 C CB  . LYS A 1 849 ? -44.203 1.564   28.291 1.00 19.50 ? 849  LYS A CB  1 
ATOM   6737 C CG  . LYS A 1 849 ? -45.556 0.838   28.425 1.00 20.08 ? 849  LYS A CG  1 
ATOM   6738 C CD  . LYS A 1 849 ? -46.692 1.848   28.437 1.00 18.74 ? 849  LYS A CD  1 
ATOM   6739 C CE  . LYS A 1 849 ? -48.067 1.154   28.478 1.00 24.32 ? 849  LYS A CE  1 
ATOM   6740 N NZ  . LYS A 1 849 ? -49.222 2.149   28.581 1.00 25.49 ? 849  LYS A NZ  1 
ATOM   6741 N N   . VAL A 1 850 ? -42.275 3.457   25.671 1.00 20.04 ? 850  VAL A N   1 
ATOM   6742 C CA  . VAL A 1 850 ? -41.020 4.148   25.409 1.00 19.96 ? 850  VAL A CA  1 
ATOM   6743 C C   . VAL A 1 850 ? -41.286 5.565   24.915 1.00 19.80 ? 850  VAL A C   1 
ATOM   6744 O O   . VAL A 1 850 ? -42.018 5.763   23.939 1.00 20.34 ? 850  VAL A O   1 
ATOM   6745 C CB  . VAL A 1 850 ? -40.202 3.379   24.336 1.00 19.72 ? 850  VAL A CB  1 
ATOM   6746 C CG1 . VAL A 1 850 ? -38.831 4.069   24.032 1.00 20.30 ? 850  VAL A CG1 1 
ATOM   6747 C CG2 . VAL A 1 850 ? -39.976 1.946   24.797 1.00 19.34 ? 850  VAL A CG2 1 
ATOM   6748 N N   . ALA A 1 851 ? -40.674 6.543   25.575 1.00 19.40 ? 851  ALA A N   1 
ATOM   6749 C CA  . ALA A 1 851 ? -40.652 7.920   25.092 1.00 19.09 ? 851  ALA A CA  1 
ATOM   6750 C C   . ALA A 1 851 ? -39.223 8.263   24.629 1.00 19.40 ? 851  ALA A C   1 
ATOM   6751 O O   . ALA A 1 851 ? -38.254 7.872   25.276 1.00 18.78 ? 851  ALA A O   1 
ATOM   6752 C CB  . ALA A 1 851 ? -41.096 8.872   26.201 1.00 18.82 ? 851  ALA A CB  1 
ATOM   6753 N N   . ILE A 1 852 ? -39.100 8.963   23.496 1.00 19.26 ? 852  ILE A N   1 
ATOM   6754 C CA  . ILE A 1 852 ? -37.815 9.531   23.055 1.00 19.04 ? 852  ILE A CA  1 
ATOM   6755 C C   . ILE A 1 852 ? -37.970 11.044  22.974 1.00 19.26 ? 852  ILE A C   1 
ATOM   6756 O O   . ILE A 1 852 ? -38.879 11.550  22.308 1.00 19.33 ? 852  ILE A O   1 
ATOM   6757 C CB  . ILE A 1 852 ? -37.313 8.963   21.692 1.00 18.58 ? 852  ILE A CB  1 
ATOM   6758 C CG1 . ILE A 1 852 ? -37.222 7.448   21.746 1.00 19.44 ? 852  ILE A CG1 1 
ATOM   6759 C CG2 . ILE A 1 852 ? -35.899 9.551   21.335 1.00 18.69 ? 852  ILE A CG2 1 
ATOM   6760 C CD1 . ILE A 1 852 ? -37.158 6.773   20.357 1.00 21.53 ? 852  ILE A CD1 1 
ATOM   6761 N N   . ILE A 1 853 ? -37.095 11.757  23.671 1.00 18.95 ? 853  ILE A N   1 
ATOM   6762 C CA  . ILE A 1 853 ? -37.068 13.193  23.660 1.00 19.12 ? 853  ILE A CA  1 
ATOM   6763 C C   . ILE A 1 853 ? -35.911 13.604  22.769 1.00 20.91 ? 853  ILE A C   1 
ATOM   6764 O O   . ILE A 1 853 ? -34.732 13.303  23.068 1.00 20.51 ? 853  ILE A O   1 
ATOM   6765 C CB  . ILE A 1 853 ? -36.889 13.779  25.104 1.00 19.15 ? 853  ILE A CB  1 
ATOM   6766 C CG1 . ILE A 1 853 ? -37.935 13.191  26.089 1.00 19.60 ? 853  ILE A CG1 1 
ATOM   6767 C CG2 . ILE A 1 853 ? -36.863 15.293  25.073 1.00 18.61 ? 853  ILE A CG2 1 
ATOM   6768 C CD1 . ILE A 1 853 ? -37.793 13.678  27.569 1.00 19.06 ? 853  ILE A CD1 1 
ATOM   6769 N N   . THR A 1 854 ? -36.252 14.295  21.681 1.00 22.05 ? 854  THR A N   1 
ATOM   6770 C CA  . THR A 1 854 ? -35.279 14.855  20.738 1.00 23.61 ? 854  THR A CA  1 
ATOM   6771 C C   . THR A 1 854 ? -35.483 16.363  20.594 1.00 24.57 ? 854  THR A C   1 
ATOM   6772 O O   . THR A 1 854 ? -36.289 16.971  21.321 1.00 24.06 ? 854  THR A O   1 
ATOM   6773 C CB  . THR A 1 854 ? -35.373 14.198  19.334 1.00 23.74 ? 854  THR A CB  1 
ATOM   6774 O OG1 . THR A 1 854 ? -36.726 14.237  18.846 1.00 22.58 ? 854  THR A OG1 1 
ATOM   6775 C CG2 . THR A 1 854 ? -34.907 12.745  19.371 1.00 23.47 ? 854  THR A CG2 1 
ATOM   6776 N N   . ASP A 1 855 ? -34.769 16.958  19.637 1.00 24.78 ? 855  ASP A N   1 
ATOM   6777 C CA  . ASP A 1 855 ? -34.751 18.406  19.449 1.00 25.91 ? 855  ASP A CA  1 
ATOM   6778 C C   . ASP A 1 855 ? -34.432 19.118  20.784 1.00 26.02 ? 855  ASP A C   1 
ATOM   6779 O O   . ASP A 1 855 ? -35.137 20.033  21.245 1.00 25.82 ? 855  ASP A O   1 
ATOM   6780 C CB  . ASP A 1 855 ? -36.063 18.880  18.814 1.00 26.46 ? 855  ASP A CB  1 
ATOM   6781 C CG  . ASP A 1 855 ? -36.019 20.329  18.422 1.00 29.64 ? 855  ASP A CG  1 
ATOM   6782 O OD1 . ASP A 1 855 ? -34.885 20.855  18.210 1.00 31.14 ? 855  ASP A OD1 1 
ATOM   6783 O OD2 . ASP A 1 855 ? -37.126 20.937  18.357 1.00 29.81 ? 855  ASP A OD2 1 
ATOM   6784 N N   . ILE A 1 856 ? -33.355 18.652  21.397 1.00 25.06 ? 856  ILE A N   1 
ATOM   6785 C CA  . ILE A 1 856 ? -32.958 19.064  22.723 1.00 25.32 ? 856  ILE A CA  1 
ATOM   6786 C C   . ILE A 1 856 ? -31.437 19.165  22.663 1.00 24.57 ? 856  ILE A C   1 
ATOM   6787 O O   . ILE A 1 856 ? -30.809 18.556  21.800 1.00 24.04 ? 856  ILE A O   1 
ATOM   6788 C CB  . ILE A 1 856 ? -33.479 18.065  23.813 1.00 25.06 ? 856  ILE A CB  1 
ATOM   6789 C CG1 . ILE A 1 856 ? -33.755 18.793  25.131 1.00 25.35 ? 856  ILE A CG1 1 
ATOM   6790 C CG2 . ILE A 1 856 ? -32.551 16.847  23.999 1.00 26.82 ? 856  ILE A CG2 1 
ATOM   6791 C CD1 . ILE A 1 856 ? -34.085 17.840  26.312 1.00 26.83 ? 856  ILE A CD1 1 
ATOM   6792 N N   . ASP A 1 857 ? -30.858 19.969  23.536 1.00 24.40 ? 857  ASP A N   1 
ATOM   6793 C CA  . ASP A 1 857 ? -29.430 20.242  23.467 1.00 24.07 ? 857  ASP A CA  1 
ATOM   6794 C C   . ASP A 1 857 ? -28.935 20.478  24.883 1.00 22.64 ? 857  ASP A C   1 
ATOM   6795 O O   . ASP A 1 857 ? -28.864 21.613  25.333 1.00 23.10 ? 857  ASP A O   1 
ATOM   6796 C CB  . ASP A 1 857 ? -29.199 21.476  22.572 1.00 25.26 ? 857  ASP A CB  1 
ATOM   6797 C CG  . ASP A 1 857 ? -27.732 21.741  22.274 1.00 29.01 ? 857  ASP A CG  1 
ATOM   6798 O OD1 . ASP A 1 857 ? -27.010 20.810  21.860 1.00 31.68 ? 857  ASP A OD1 1 
ATOM   6799 O OD2 . ASP A 1 857 ? -27.320 22.912  22.412 1.00 34.32 ? 857  ASP A OD2 1 
ATOM   6800 N N   . LEU A 1 858 ? -28.610 19.401  25.601 1.00 21.03 ? 858  LEU A N   1 
ATOM   6801 C CA  . LEU A 1 858 ? -28.090 19.529  26.958 1.00 19.51 ? 858  LEU A CA  1 
ATOM   6802 C C   . LEU A 1 858 ? -26.561 19.489  26.931 1.00 20.61 ? 858  LEU A C   1 
ATOM   6803 O O   . LEU A 1 858 ? -25.962 18.427  26.889 1.00 20.26 ? 858  LEU A O   1 
ATOM   6804 C CB  . LEU A 1 858 ? -28.628 18.427  27.867 1.00 19.34 ? 858  LEU A CB  1 
ATOM   6805 C CG  . LEU A 1 858 ? -30.138 18.077  27.840 1.00 19.15 ? 858  LEU A CG  1 
ATOM   6806 C CD1 . LEU A 1 858 ? -30.525 17.325  29.096 1.00 21.90 ? 858  LEU A CD1 1 
ATOM   6807 C CD2 . LEU A 1 858 ? -30.964 19.319  27.719 1.00 18.51 ? 858  LEU A CD2 1 
ATOM   6808 N N   . LEU A 1 859 ? -25.939 20.651  26.968 1.00 20.64 ? 859  LEU A N   1 
ATOM   6809 C CA  . LEU A 1 859 ? -24.490 20.733  26.898 1.00 21.17 ? 859  LEU A CA  1 
ATOM   6810 C C   . LEU A 1 859 ? -23.801 19.897  27.980 1.00 21.10 ? 859  LEU A C   1 
ATOM   6811 O O   . LEU A 1 859 ? -24.027 20.058  29.195 1.00 20.37 ? 859  LEU A O   1 
ATOM   6812 C CB  . LEU A 1 859 ? -24.018 22.196  26.929 1.00 20.41 ? 859  LEU A CB  1 
ATOM   6813 C CG  . LEU A 1 859 ? -24.553 23.148  25.851 1.00 21.82 ? 859  LEU A CG  1 
ATOM   6814 C CD1 . LEU A 1 859 ? -23.990 24.563  26.058 1.00 21.09 ? 859  LEU A CD1 1 
ATOM   6815 C CD2 . LEU A 1 859 ? -24.257 22.645  24.433 1.00 20.99 ? 859  LEU A CD2 1 
ATOM   6816 N N   . LEU A 1 860 ? -22.972 18.975  27.513 1.00 21.93 ? 860  LEU A N   1 
ATOM   6817 C CA  . LEU A 1 860 ? -22.065 18.247  28.406 1.00 22.82 ? 860  LEU A CA  1 
ATOM   6818 C C   . LEU A 1 860 ? -21.377 19.270  29.304 1.00 22.84 ? 860  LEU A C   1 
ATOM   6819 O O   . LEU A 1 860 ? -20.901 20.314  28.818 1.00 23.77 ? 860  LEU A O   1 
ATOM   6820 C CB  . LEU A 1 860 ? -21.063 17.437  27.579 1.00 22.20 ? 860  LEU A CB  1 
ATOM   6821 C CG  . LEU A 1 860 ? -20.144 16.455  28.296 1.00 23.41 ? 860  LEU A CG  1 
ATOM   6822 C CD1 . LEU A 1 860 ? -20.922 15.276  28.794 1.00 24.34 ? 860  LEU A CD1 1 
ATOM   6823 C CD2 . LEU A 1 860 ? -19.014 16.008  27.381 1.00 22.31 ? 860  LEU A CD2 1 
ATOM   6824 N N   . GLY A 1 861 ? -21.395 19.015  30.606 1.00 22.99 ? 861  GLY A N   1 
ATOM   6825 C CA  . GLY A 1 861 ? -20.783 19.928  31.573 1.00 24.18 ? 861  GLY A CA  1 
ATOM   6826 C C   . GLY A 1 861 ? -21.730 20.944  32.198 1.00 24.41 ? 861  GLY A C   1 
ATOM   6827 O O   . GLY A 1 861 ? -21.326 21.690  33.071 1.00 24.73 ? 861  GLY A O   1 
ATOM   6828 N N   . GLU A 1 862 ? -22.987 20.988  31.761 1.00 24.45 ? 862  GLU A N   1 
ATOM   6829 C CA  . GLU A 1 862 ? -23.953 21.935  32.354 1.00 24.32 ? 862  GLU A CA  1 
ATOM   6830 C C   . GLU A 1 862 ? -25.051 21.224  33.130 1.00 23.33 ? 862  GLU A C   1 
ATOM   6831 O O   . GLU A 1 862 ? -25.495 20.159  32.744 1.00 23.10 ? 862  GLU A O   1 
ATOM   6832 C CB  . GLU A 1 862 ? -24.604 22.832  31.277 1.00 24.80 ? 862  GLU A CB  1 
ATOM   6833 C CG  . GLU A 1 862 ? -23.674 23.790  30.535 1.00 27.08 ? 862  GLU A CG  1 
ATOM   6834 C CD  . GLU A 1 862 ? -23.017 24.801  31.458 1.00 33.01 ? 862  GLU A CD  1 
ATOM   6835 O OE1 . GLU A 1 862 ? -23.738 25.423  32.280 1.00 33.68 ? 862  GLU A OE1 1 
ATOM   6836 O OE2 . GLU A 1 862 ? -21.773 24.966  31.368 1.00 35.55 ? 862  GLU A OE2 1 
ATOM   6837 N N   . ALA A 1 863 ? -25.500 21.843  34.210 1.00 22.71 ? 863  ALA A N   1 
ATOM   6838 C CA  . ALA A 1 863 ? -26.613 21.338  34.988 1.00 22.85 ? 863  ALA A CA  1 
ATOM   6839 C C   . ALA A 1 863 ? -27.948 21.694  34.326 1.00 23.15 ? 863  ALA A C   1 
ATOM   6840 O O   . ALA A 1 863 ? -28.112 22.814  33.834 1.00 23.11 ? 863  ALA A O   1 
ATOM   6841 C CB  . ALA A 1 863 ? -26.560 21.921  36.364 1.00 23.35 ? 863  ALA A CB  1 
ATOM   6842 N N   . TYR A 1 864 ? -28.877 20.734  34.313 1.00 22.77 ? 864  TYR A N   1 
ATOM   6843 C CA  . TYR A 1 864 ? -30.207 20.892  33.706 1.00 22.49 ? 864  TYR A CA  1 
ATOM   6844 C C   . TYR A 1 864 ? -31.249 20.155  34.539 1.00 22.80 ? 864  TYR A C   1 
ATOM   6845 O O   . TYR A 1 864 ? -30.929 19.206  35.245 1.00 22.40 ? 864  TYR A O   1 
ATOM   6846 C CB  . TYR A 1 864 ? -30.274 20.306  32.286 1.00 21.72 ? 864  TYR A CB  1 
ATOM   6847 C CG  . TYR A 1 864 ? -29.456 21.046  31.263 1.00 22.83 ? 864  TYR A CG  1 
ATOM   6848 C CD1 . TYR A 1 864 ? -29.992 22.126  30.552 1.00 21.45 ? 864  TYR A CD1 1 
ATOM   6849 C CD2 . TYR A 1 864 ? -28.147 20.662  30.999 1.00 21.94 ? 864  TYR A CD2 1 
ATOM   6850 C CE1 . TYR A 1 864 ? -29.221 22.807  29.594 1.00 23.55 ? 864  TYR A CE1 1 
ATOM   6851 C CE2 . TYR A 1 864 ? -27.368 21.343  30.076 1.00 22.75 ? 864  TYR A CE2 1 
ATOM   6852 C CZ  . TYR A 1 864 ? -27.889 22.410  29.378 1.00 22.44 ? 864  TYR A CZ  1 
ATOM   6853 O OH  . TYR A 1 864 ? -27.089 23.060  28.434 1.00 19.89 ? 864  TYR A OH  1 
ATOM   6854 N N   . THR A 1 865 ? -32.491 20.609  34.430 1.00 23.51 ? 865  THR A N   1 
ATOM   6855 C CA  . THR A 1 865 ? -33.649 19.876  34.909 1.00 24.76 ? 865  THR A CA  1 
ATOM   6856 C C   . THR A 1 865 ? -34.575 19.712  33.705 1.00 25.42 ? 865  THR A C   1 
ATOM   6857 O O   . THR A 1 865 ? -34.912 20.684  33.041 1.00 26.10 ? 865  THR A O   1 
ATOM   6858 C CB  . THR A 1 865 ? -34.325 20.612  36.083 1.00 24.62 ? 865  THR A CB  1 
ATOM   6859 O OG1 . THR A 1 865 ? -33.388 20.731  37.178 1.00 24.54 ? 865  THR A OG1 1 
ATOM   6860 C CG2 . THR A 1 865 ? -35.531 19.836  36.574 1.00 25.55 ? 865  THR A CG2 1 
ATOM   6861 N N   . VAL A 1 866 ? -34.939 18.479  33.391 1.00 25.85 ? 866  VAL A N   1 
ATOM   6862 C CA  . VAL A 1 866 ? -35.917 18.219  32.353 1.00 25.94 ? 866  VAL A CA  1 
ATOM   6863 C C   . VAL A 1 866 ? -37.134 17.757  33.121 1.00 26.90 ? 866  VAL A C   1 
ATOM   6864 O O   . VAL A 1 866 ? -37.020 16.876  33.964 1.00 27.20 ? 866  VAL A O   1 
ATOM   6865 C CB  . VAL A 1 866 ? -35.418 17.139  31.361 1.00 25.69 ? 866  VAL A CB  1 
ATOM   6866 C CG1 . VAL A 1 866 ? -36.449 16.843  30.274 1.00 24.32 ? 866  VAL A CG1 1 
ATOM   6867 C CG2 . VAL A 1 866 ? -34.087 17.569  30.736 1.00 24.19 ? 866  VAL A CG2 1 
ATOM   6868 N N   . GLU A 1 867 ? -38.281 18.380  32.862 1.00 27.91 ? 867  GLU A N   1 
ATOM   6869 C CA  . GLU A 1 867 ? -39.487 18.123  33.635 1.00 29.11 ? 867  GLU A CA  1 
ATOM   6870 C C   . GLU A 1 867 ? -40.633 17.766  32.712 1.00 29.14 ? 867  GLU A C   1 
ATOM   6871 O O   . GLU A 1 867 ? -40.765 18.328  31.629 1.00 27.90 ? 867  GLU A O   1 
ATOM   6872 C CB  . GLU A 1 867 ? -39.863 19.347  34.474 1.00 29.59 ? 867  GLU A CB  1 
ATOM   6873 C CG  . GLU A 1 867 ? -39.080 19.464  35.786 1.00 34.01 ? 867  GLU A CG  1 
ATOM   6874 C CD  . GLU A 1 867 ? -39.778 20.321  36.831 1.00 38.61 ? 867  GLU A CD  1 
ATOM   6875 O OE1 . GLU A 1 867 ? -39.735 21.563  36.703 1.00 40.39 ? 867  GLU A OE1 1 
ATOM   6876 O OE2 . GLU A 1 867 ? -40.348 19.744  37.792 1.00 39.91 ? 867  GLU A OE2 1 
ATOM   6877 N N   . TRP A 1 868 ? -41.481 16.848  33.153 1.00 30.19 ? 868  TRP A N   1 
ATOM   6878 C CA  . TRP A 1 868 ? -42.653 16.499  32.376 1.00 31.10 ? 868  TRP A CA  1 
ATOM   6879 C C   . TRP A 1 868 ? -43.840 16.141  33.274 1.00 32.13 ? 868  TRP A C   1 
ATOM   6880 O O   . TRP A 1 868 ? -43.686 15.942  34.476 1.00 31.62 ? 868  TRP A O   1 
ATOM   6881 C CB  . TRP A 1 868 ? -42.327 15.368  31.383 1.00 31.05 ? 868  TRP A CB  1 
ATOM   6882 C CG  . TRP A 1 868 ? -41.957 14.054  32.026 1.00 30.72 ? 868  TRP A CG  1 
ATOM   6883 C CD1 . TRP A 1 868 ? -42.813 13.056  32.408 1.00 30.99 ? 868  TRP A CD1 1 
ATOM   6884 C CD2 . TRP A 1 868 ? -40.643 13.605  32.370 1.00 30.79 ? 868  TRP A CD2 1 
ATOM   6885 N NE1 . TRP A 1 868 ? -42.114 12.019  32.962 1.00 30.64 ? 868  TRP A NE1 1 
ATOM   6886 C CE2 . TRP A 1 868 ? -40.778 12.331  32.953 1.00 31.40 ? 868  TRP A CE2 1 
ATOM   6887 C CE3 . TRP A 1 868 ? -39.360 14.150  32.226 1.00 29.91 ? 868  TRP A CE3 1 
ATOM   6888 C CZ2 . TRP A 1 868 ? -39.674 11.582  33.382 1.00 32.01 ? 868  TRP A CZ2 1 
ATOM   6889 C CZ3 . TRP A 1 868 ? -38.265 13.406  32.666 1.00 30.84 ? 868  TRP A CZ3 1 
ATOM   6890 C CH2 . TRP A 1 868 ? -38.433 12.145  33.235 1.00 30.81 ? 868  TRP A CH2 1 
ATOM   6891 N N   . ALA A 1 869 ? -45.018 16.055  32.668 1.00 33.20 ? 869  ALA A N   1 
ATOM   6892 C CA  . ALA A 1 869 ? -46.218 15.626  33.364 1.00 34.81 ? 869  ALA A CA  1 
ATOM   6893 C C   . ALA A 1 869 ? -46.740 14.351  32.711 1.00 36.17 ? 869  ALA A C   1 
ATOM   6894 O O   . ALA A 1 869 ? -46.203 13.900  31.685 1.00 35.77 ? 869  ALA A O   1 
ATOM   6895 C CB  . ALA A 1 869 ? -47.262 16.720  33.309 1.00 34.99 ? 869  ALA A CB  1 
ATOM   6896 N N   . HIS A 1 870 ? -47.765 13.757  33.329 1.00 37.90 ? 870  HIS A N   1 
ATOM   6897 C CA  . HIS A 1 870 ? -48.485 12.625  32.764 1.00 39.00 ? 870  HIS A CA  1 
ATOM   6898 C C   . HIS A 1 870 ? -49.985 12.928  32.842 1.00 39.78 ? 870  HIS A C   1 
ATOM   6899 O O   . HIS A 1 870 ? -50.754 12.555  31.952 1.00 40.23 ? 870  HIS A O   1 
ATOM   6900 C CB  . HIS A 1 870 ? -48.191 11.340  33.537 1.00 39.83 ? 870  HIS A CB  1 
ATOM   6901 C CG  . HIS A 1 870 ? -46.737 10.976  33.605 1.00 41.43 ? 870  HIS A CG  1 
ATOM   6902 N ND1 . HIS A 1 870 ? -46.113 10.213  32.643 1.00 42.48 ? 870  HIS A ND1 1 
ATOM   6903 C CD2 . HIS A 1 870 ? -45.794 11.248  34.535 1.00 43.11 ? 870  HIS A CD2 1 
ATOM   6904 C CE1 . HIS A 1 870 ? -44.845 10.038  32.971 1.00 43.53 ? 870  HIS A CE1 1 
ATOM   6905 N NE2 . HIS A 1 870 ? -44.627 10.652  34.120 1.00 44.63 ? 870  HIS A NE2 1 
HETATM 6906 C C1  . NAG B 2 .   ? -17.242 9.318   11.268 1.00 35.70 ? 2001 NAG A C1  1 
HETATM 6907 C C2  . NAG B 2 .   ? -17.779 10.757  11.198 1.00 37.64 ? 2001 NAG A C2  1 
HETATM 6908 C C3  . NAG B 2 .   ? -17.468 11.367  9.813  1.00 39.41 ? 2001 NAG A C3  1 
HETATM 6909 C C4  . NAG B 2 .   ? -15.961 11.333  9.581  1.00 37.81 ? 2001 NAG A C4  1 
HETATM 6910 C C5  . NAG B 2 .   ? -15.503 9.884   9.685  1.00 39.24 ? 2001 NAG A C5  1 
HETATM 6911 C C6  . NAG B 2 .   ? -13.999 9.732   9.483  1.00 40.82 ? 2001 NAG A C6  1 
HETATM 6912 C C7  . NAG B 2 .   ? -19.752 11.890  12.142 1.00 40.14 ? 2001 NAG A C7  1 
HETATM 6913 C C8  . NAG B 2 .   ? -21.188 11.723  12.538 1.00 39.39 ? 2001 NAG A C8  1 
HETATM 6914 N N2  . NAG B 2 .   ? -19.192 10.828  11.539 1.00 37.74 ? 2001 NAG A N2  1 
HETATM 6915 O O3  . NAG B 2 .   ? -17.925 12.704  9.681  1.00 39.24 ? 2001 NAG A O3  1 
HETATM 6916 O O4  . NAG B 2 .   ? -15.650 11.864  8.316  1.00 41.23 ? 2001 NAG A O4  1 
HETATM 6917 O O5  . NAG B 2 .   ? -15.861 9.347   10.954 1.00 37.93 ? 2001 NAG A O5  1 
HETATM 6918 O O6  . NAG B 2 .   ? -13.730 8.380   9.158  1.00 43.97 ? 2001 NAG A O6  1 
HETATM 6919 O O7  . NAG B 2 .   ? -19.181 12.974  12.371 1.00 39.85 ? 2001 NAG A O7  1 
HETATM 6920 C C1  . NAG C 2 .   ? 24.943  -10.193 35.474 1.00 27.08 ? 2002 NAG A C1  1 
HETATM 6921 C C2  . NAG C 2 .   ? 24.747  -9.317  36.722 1.00 29.79 ? 2002 NAG A C2  1 
HETATM 6922 C C3  . NAG C 2 .   ? 25.349  -7.905  36.540 1.00 28.45 ? 2002 NAG A C3  1 
HETATM 6923 C C4  . NAG C 2 .   ? 26.802  -7.960  36.072 1.00 28.18 ? 2002 NAG A C4  1 
HETATM 6924 C C5  . NAG C 2 .   ? 26.930  -8.911  34.894 1.00 27.87 ? 2002 NAG A C5  1 
HETATM 6925 C C6  . NAG C 2 .   ? 28.410  -9.138  34.557 1.00 28.32 ? 2002 NAG A C6  1 
HETATM 6926 C C7  . NAG C 2 .   ? 22.915  -9.908  38.181 1.00 33.05 ? 2002 NAG A C7  1 
HETATM 6927 C C8  . NAG C 2 .   ? 21.438  -9.844  38.459 1.00 33.78 ? 2002 NAG A C8  1 
HETATM 6928 N N2  . NAG C 2 .   ? 23.340  -9.274  37.100 1.00 30.21 ? 2002 NAG A N2  1 
HETATM 6929 O O3  . NAG C 2 .   ? 25.288  -7.186  37.744 1.00 26.84 ? 2002 NAG A O3  1 
HETATM 6930 O O4  . NAG C 2 .   ? 27.302  -6.667  35.731 1.00 30.96 ? 2002 NAG A O4  1 
HETATM 6931 O O5  . NAG C 2 .   ? 26.341  -10.166 35.196 1.00 28.59 ? 2002 NAG A O5  1 
HETATM 6932 O O6  . NAG C 2 .   ? 28.466  -9.903  33.377 1.00 26.98 ? 2002 NAG A O6  1 
HETATM 6933 O O7  . NAG C 2 .   ? 23.667  -10.515 38.947 1.00 36.59 ? 2002 NAG A O7  1 
HETATM 6934 S S   . SO4 D 3 .   ? -26.184 -1.448  12.240 1.00 36.07 ? 4001 SO4 A S   1 
HETATM 6935 O O1  . SO4 D 3 .   ? -24.954 -2.114  11.838 1.00 37.33 ? 4001 SO4 A O1  1 
HETATM 6936 O O2  . SO4 D 3 .   ? -26.544 -0.556  11.154 1.00 37.43 ? 4001 SO4 A O2  1 
HETATM 6937 O O3  . SO4 D 3 .   ? -27.256 -2.422  12.435 1.00 39.05 ? 4001 SO4 A O3  1 
HETATM 6938 O O4  . SO4 D 3 .   ? -26.032 -0.664  13.452 1.00 36.46 ? 4001 SO4 A O4  1 
HETATM 6939 O O7  . 3CU E 4 .   ? 1.203   -15.881 23.461 1.00 16.35 ? 1001 3CU A O7  1 
HETATM 6940 C C7  . 3CU E 4 .   ? 0.837   -16.391 22.191 1.00 17.72 ? 1001 3CU A C7  1 
HETATM 6941 C C7A . 3CU E 4 .   ? 0.985   -15.255 21.171 1.00 18.01 ? 1001 3CU A C7A 1 
HETATM 6942 C C1  . 3CU E 4 .   ? -0.113  -15.292 20.086 1.00 19.02 ? 1001 3CU A C1  1 
HETATM 6943 O O1  . 3CU E 4 .   ? -1.248  -14.457 20.375 1.00 16.00 ? 1001 3CU A O1  1 
HETATM 6944 C C2  . 3CU E 4 .   ? 0.705   -14.742 18.914 1.00 18.00 ? 1001 3CU A C2  1 
HETATM 6945 O O2  . 3CU E 4 .   ? 0.042   -14.937 17.680 1.00 18.32 ? 1001 3CU A O2  1 
HETATM 6946 C C3  . 3CU E 4 .   ? 1.867   -15.700 18.998 1.00 16.43 ? 1001 3CU A C3  1 
HETATM 6947 C C8  . 3CU E 4 .   ? 3.053   -15.275 18.113 1.00 15.10 ? 1001 3CU A C8  1 
HETATM 6948 O O8  . 3CU E 4 .   ? 3.387   -13.911 18.365 1.00 17.54 ? 1001 3CU A O8  1 
HETATM 6949 N N4  . 3CU E 4 .   ? 2.248   -15.556 20.421 1.00 19.73 ? 1001 3CU A N4  1 
HETATM 6950 C C5  . 3CU E 4 .   ? 2.858   -16.806 20.959 1.00 17.70 ? 1001 3CU A C5  1 
HETATM 6951 C C6  . 3CU E 4 .   ? 1.795   -17.516 21.744 1.00 19.38 ? 1001 3CU A C6  1 
HETATM 6952 O OXT . 3CU E 4 .   ? 1.083   -18.391 20.865 1.00 19.77 ? 1001 3CU A OXT 1 
HETATM 6953 C C1  . GOL F 5 .   ? 2.694   -21.038 22.517 1.00 24.98 ? 3001 GOL A C1  1 
HETATM 6954 O O1  . GOL F 5 .   ? 2.547   -20.288 23.709 1.00 27.24 ? 3001 GOL A O1  1 
HETATM 6955 C C2  . GOL F 5 .   ? 4.118   -20.803 21.995 1.00 28.23 ? 3001 GOL A C2  1 
HETATM 6956 O O2  . GOL F 5 .   ? 5.022   -20.908 23.062 1.00 28.33 ? 3001 GOL A O2  1 
HETATM 6957 C C3  . GOL F 5 .   ? 4.463   -21.896 20.990 1.00 29.01 ? 3001 GOL A C3  1 
HETATM 6958 O O3  . GOL F 5 .   ? 3.749   -21.585 19.820 1.00 30.53 ? 3001 GOL A O3  1 
HETATM 6959 C C1  . GOL G 5 .   ? -4.787  -1.157  31.071 1.00 32.30 ? 3002 GOL A C1  1 
HETATM 6960 O O1  . GOL G 5 .   ? -6.170  -1.005  31.349 1.00 36.49 ? 3002 GOL A O1  1 
HETATM 6961 C C2  . GOL G 5 .   ? -4.499  -0.879  29.598 1.00 31.51 ? 3002 GOL A C2  1 
HETATM 6962 O O2  . GOL G 5 .   ? -4.877  0.432   29.282 1.00 31.99 ? 3002 GOL A O2  1 
HETATM 6963 C C3  . GOL G 5 .   ? -2.991  -0.967  29.371 1.00 31.02 ? 3002 GOL A C3  1 
HETATM 6964 O O3  . GOL G 5 .   ? -2.372  0.296   29.378 1.00 26.94 ? 3002 GOL A O3  1 
HETATM 6965 C C1  . GOL H 5 .   ? -6.385  -11.934 2.423  1.00 32.43 ? 3003 GOL A C1  1 
HETATM 6966 O O1  . GOL H 5 .   ? -7.615  -12.614 2.227  1.00 34.48 ? 3003 GOL A O1  1 
HETATM 6967 C C2  . GOL H 5 .   ? -5.756  -12.493 3.679  1.00 31.30 ? 3003 GOL A C2  1 
HETATM 6968 O O2  . GOL H 5 .   ? -5.958  -13.883 3.665  1.00 32.11 ? 3003 GOL A O2  1 
HETATM 6969 C C3  . GOL H 5 .   ? -4.257  -12.226 3.702  1.00 31.08 ? 3003 GOL A C3  1 
HETATM 6970 O O3  . GOL H 5 .   ? -3.782  -12.502 5.006  1.00 32.99 ? 3003 GOL A O3  1 
HETATM 6971 C C1  . GOL I 5 .   ? -4.310  -11.382 70.224 1.00 36.68 ? 3004 GOL A C1  1 
HETATM 6972 O O1  . GOL I 5 .   ? -4.160  -10.152 70.870 1.00 33.52 ? 3004 GOL A O1  1 
HETATM 6973 C C2  . GOL I 5 .   ? -5.649  -11.930 70.677 1.00 38.69 ? 3004 GOL A C2  1 
HETATM 6974 O O2  . GOL I 5 .   ? -6.661  -11.114 70.120 1.00 40.22 ? 3004 GOL A O2  1 
HETATM 6975 C C3  . GOL I 5 .   ? -5.759  -13.355 70.186 1.00 36.50 ? 3004 GOL A C3  1 
HETATM 6976 O O3  . GOL I 5 .   ? -6.548  -14.164 71.034 1.00 36.95 ? 3004 GOL A O3  1 
HETATM 6977 C C1  . GOL J 5 .   ? -15.163 -22.348 60.388 1.00 36.67 ? 3005 GOL A C1  1 
HETATM 6978 O O1  . GOL J 5 .   ? -16.021 -21.924 59.348 1.00 27.63 ? 3005 GOL A O1  1 
HETATM 6979 C C2  . GOL J 5 .   ? -15.818 -22.282 61.757 1.00 38.21 ? 3005 GOL A C2  1 
HETATM 6980 O O2  . GOL J 5 .   ? -17.005 -23.040 61.726 1.00 42.09 ? 3005 GOL A O2  1 
HETATM 6981 C C3  . GOL J 5 .   ? -14.897 -22.846 62.838 1.00 40.68 ? 3005 GOL A C3  1 
HETATM 6982 O O3  . GOL J 5 .   ? -13.901 -21.907 63.195 1.00 42.92 ? 3005 GOL A O3  1 
HETATM 6983 C C1  . GOL K 5 .   ? -5.150  3.758   1.871  1.00 67.72 ? 3006 GOL A C1  1 
HETATM 6984 O O1  . GOL K 5 .   ? -4.829  5.067   2.306  1.00 66.46 ? 3006 GOL A O1  1 
HETATM 6985 C C2  . GOL K 5 .   ? -4.427  2.772   2.787  1.00 68.05 ? 3006 GOL A C2  1 
HETATM 6986 O O2  . GOL K 5 .   ? -4.806  3.016   4.128  1.00 68.93 ? 3006 GOL A O2  1 
HETATM 6987 C C3  . GOL K 5 .   ? -4.684  1.312   2.417  1.00 67.88 ? 3006 GOL A C3  1 
HETATM 6988 O O3  . GOL K 5 .   ? -4.464  0.493   3.549  1.00 66.87 ? 3006 GOL A O3  1 
HETATM 6989 C C1  . GOL L 5 .   ? -4.398  16.004  32.352 1.00 44.09 ? 3007 GOL A C1  1 
HETATM 6990 O O1  . GOL L 5 .   ? -4.165  16.415  33.677 1.00 41.26 ? 3007 GOL A O1  1 
HETATM 6991 C C2  . GOL L 5 .   ? -5.129  17.096  31.573 1.00 44.54 ? 3007 GOL A C2  1 
HETATM 6992 O O2  . GOL L 5 .   ? -4.203  18.114  31.292 1.00 46.95 ? 3007 GOL A O2  1 
HETATM 6993 C C3  . GOL L 5 .   ? -5.704  16.528  30.274 1.00 44.68 ? 3007 GOL A C3  1 
HETATM 6994 O O3  . GOL L 5 .   ? -6.964  17.054  29.904 1.00 42.35 ? 3007 GOL A O3  1 
HETATM 6995 C C1  . GOL M 5 .   ? -25.016 5.327   14.322 1.00 43.17 ? 3008 GOL A C1  1 
HETATM 6996 O O1  . GOL M 5 .   ? -26.222 6.035   14.573 1.00 40.44 ? 3008 GOL A O1  1 
HETATM 6997 C C2  . GOL M 5 .   ? -24.104 5.985   13.283 1.00 42.02 ? 3008 GOL A C2  1 
HETATM 6998 O O2  . GOL M 5 .   ? -23.478 7.119   13.810 1.00 39.93 ? 3008 GOL A O2  1 
HETATM 6999 C C3  . GOL M 5 .   ? -22.990 5.041   12.855 1.00 43.35 ? 3008 GOL A C3  1 
HETATM 7000 O O3  . GOL M 5 .   ? -22.515 5.425   11.581 1.00 42.53 ? 3008 GOL A O3  1 
HETATM 7001 C C1  . GOL N 5 .   ? -11.105 -15.470 71.920 1.00 42.77 ? 3009 GOL A C1  1 
HETATM 7002 O O1  . GOL N 5 .   ? -10.863 -15.595 73.317 1.00 40.69 ? 3009 GOL A O1  1 
HETATM 7003 C C2  . GOL N 5 .   ? -10.982 -14.041 71.363 1.00 42.19 ? 3009 GOL A C2  1 
HETATM 7004 O O2  . GOL N 5 .   ? -11.593 -13.048 72.154 1.00 43.90 ? 3009 GOL A O2  1 
HETATM 7005 C C3  . GOL N 5 .   ? -9.542  -13.655 71.037 1.00 42.21 ? 3009 GOL A C3  1 
HETATM 7006 O O3  . GOL N 5 .   ? -9.490  -12.359 70.461 1.00 42.53 ? 3009 GOL A O3  1 
HETATM 7007 O O   . HOH O 6 .   ? 2.745   -42.833 50.533 1.00 18.13 ? 4002 HOH A O   1 
HETATM 7008 O O   . HOH O 6 .   ? 10.625  -15.911 34.618 1.00 18.60 ? 4003 HOH A O   1 
HETATM 7009 O O   . HOH O 6 .   ? -1.546  -13.864 33.217 1.00 21.00 ? 4004 HOH A O   1 
HETATM 7010 O O   . HOH O 6 .   ? -7.970  -14.161 10.746 1.00 18.76 ? 4005 HOH A O   1 
HETATM 7011 O O   . HOH O 6 .   ? 11.541  -28.784 39.301 1.00 17.61 ? 4006 HOH A O   1 
HETATM 7012 O O   . HOH O 6 .   ? -8.004  -2.813  51.817 1.00 18.96 ? 4007 HOH A O   1 
HETATM 7013 O O   . HOH O 6 .   ? -3.725  -6.205  39.070 1.00 10.35 ? 4008 HOH A O   1 
HETATM 7014 O O   . HOH O 6 .   ? 9.345   -21.507 43.448 1.00 17.93 ? 4009 HOH A O   1 
HETATM 7015 O O   . HOH O 6 .   ? -9.054  15.432  30.628 1.00 18.39 ? 4010 HOH A O   1 
HETATM 7016 O O   . HOH O 6 .   ? -31.824 -11.757 41.317 1.00 20.23 ? 4011 HOH A O   1 
HETATM 7017 O O   . HOH O 6 .   ? -19.995 -6.711  59.285 1.00 23.19 ? 4012 HOH A O   1 
HETATM 7018 O O   . HOH O 6 .   ? -4.011  -32.478 49.098 1.00 23.43 ? 4013 HOH A O   1 
HETATM 7019 O O   . HOH O 6 .   ? -4.423  -9.086  41.117 1.00 11.15 ? 4014 HOH A O   1 
HETATM 7020 O O   . HOH O 6 .   ? -17.693 7.300   21.710 1.00 17.43 ? 4015 HOH A O   1 
HETATM 7021 O O   . HOH O 6 .   ? -22.216 -13.954 35.987 1.00 14.54 ? 4016 HOH A O   1 
HETATM 7022 O O   . HOH O 6 .   ? -8.147  -12.592 13.027 1.00 13.66 ? 4017 HOH A O   1 
HETATM 7023 O O   . HOH O 6 .   ? 6.127   -14.158 34.967 1.00 13.67 ? 4018 HOH A O   1 
HETATM 7024 O O   . HOH O 6 .   ? -18.198 -6.519  61.363 1.00 17.11 ? 4019 HOH A O   1 
HETATM 7025 O O   . HOH O 6 .   ? -4.743  9.176   37.585 1.00 26.20 ? 4020 HOH A O   1 
HETATM 7026 O O   . HOH O 6 .   ? -7.863  -17.741 36.466 1.00 15.13 ? 4021 HOH A O   1 
HETATM 7027 O O   . HOH O 6 .   ? -21.310 -6.246  45.071 1.00 16.39 ? 4022 HOH A O   1 
HETATM 7028 O O   . HOH O 6 .   ? -20.286 -20.956 38.290 1.00 15.44 ? 4023 HOH A O   1 
HETATM 7029 O O   . HOH O 6 .   ? 2.385   -8.262  34.107 1.00 20.16 ? 4024 HOH A O   1 
HETATM 7030 O O   . HOH O 6 .   ? -3.333  4.054   31.466 1.00 16.84 ? 4025 HOH A O   1 
HETATM 7031 O O   . HOH O 6 .   ? -6.789  -32.819 49.297 1.00 25.67 ? 4026 HOH A O   1 
HETATM 7032 O O   . HOH O 6 .   ? -3.254  7.279   25.132 1.00 20.70 ? 4027 HOH A O   1 
HETATM 7033 O O   . HOH O 6 .   ? -13.434 -18.541 40.108 1.00 16.99 ? 4028 HOH A O   1 
HETATM 7034 O O   . HOH O 6 .   ? -2.388  -27.138 56.668 1.00 16.75 ? 4029 HOH A O   1 
HETATM 7035 O O   . HOH O 6 .   ? 6.132   -12.062 50.345 1.00 16.75 ? 4030 HOH A O   1 
HETATM 7036 O O   . HOH O 6 .   ? -19.928 6.047   20.512 1.00 13.34 ? 4031 HOH A O   1 
HETATM 7037 O O   . HOH O 6 .   ? -20.489 -16.300 5.704  1.00 22.66 ? 4032 HOH A O   1 
HETATM 7038 O O   . HOH O 6 .   ? -18.899 -19.192 61.845 1.00 22.51 ? 4033 HOH A O   1 
HETATM 7039 O O   . HOH O 6 .   ? -7.420  -12.316 8.617  1.00 13.64 ? 4034 HOH A O   1 
HETATM 7040 O O   . HOH O 6 .   ? -7.903  -16.434 24.458 1.00 15.77 ? 4035 HOH A O   1 
HETATM 7041 O O   . HOH O 6 .   ? -22.257 -26.689 21.952 1.00 22.72 ? 4036 HOH A O   1 
HETATM 7042 O O   . HOH O 6 .   ? -2.431  -30.710 52.848 1.00 15.99 ? 4037 HOH A O   1 
HETATM 7043 O O   . HOH O 6 .   ? -6.189  -33.383 59.227 1.00 11.73 ? 4038 HOH A O   1 
HETATM 7044 O O   . HOH O 6 .   ? 6.676   -21.031 30.475 1.00 13.51 ? 4039 HOH A O   1 
HETATM 7045 O O   . HOH O 6 .   ? -31.651 -9.980  43.918 1.00 22.74 ? 4040 HOH A O   1 
HETATM 7046 O O   . HOH O 6 .   ? 0.770   5.448   1.857  1.00 25.01 ? 4041 HOH A O   1 
HETATM 7047 O O   . HOH O 6 .   ? -21.632 -13.631 57.078 1.00 24.31 ? 4042 HOH A O   1 
HETATM 7048 O O   . HOH O 6 .   ? 12.278  -18.762 49.206 1.00 19.88 ? 4043 HOH A O   1 
HETATM 7049 O O   . HOH O 6 .   ? -42.626 -2.331  27.566 1.00 23.33 ? 4044 HOH A O   1 
HETATM 7050 O O   . HOH O 6 .   ? -6.896  -10.381 10.946 1.00 15.80 ? 4045 HOH A O   1 
HETATM 7051 O O   . HOH O 6 .   ? -24.525 5.220   34.579 1.00 16.41 ? 4046 HOH A O   1 
HETATM 7052 O O   . HOH O 6 .   ? -0.708  -13.262 43.056 1.00 19.34 ? 4047 HOH A O   1 
HETATM 7053 O O   . HOH O 6 .   ? -29.517 -10.241 28.481 1.00 19.53 ? 4048 HOH A O   1 
HETATM 7054 O O   . HOH O 6 .   ? -12.254 -25.801 41.945 1.00 16.95 ? 4049 HOH A O   1 
HETATM 7055 O O   . HOH O 6 .   ? -13.618 0.549   9.878  1.00 15.81 ? 4050 HOH A O   1 
HETATM 7056 O O   . HOH O 6 .   ? -7.389  -11.449 22.247 1.00 15.61 ? 4051 HOH A O   1 
HETATM 7057 O O   . HOH O 6 .   ? -2.899  -6.020  75.937 1.00 20.19 ? 4052 HOH A O   1 
HETATM 7058 O O   . HOH O 6 .   ? -6.640  -31.797 52.119 1.00 13.58 ? 4053 HOH A O   1 
HETATM 7059 O O   . HOH O 6 .   ? -10.961 -18.711 30.112 1.00 21.51 ? 4054 HOH A O   1 
HETATM 7060 O O   . HOH O 6 .   ? -4.737  -3.891  39.345 1.00 20.41 ? 4055 HOH A O   1 
HETATM 7061 O O   . HOH O 6 .   ? -5.561  -13.267 6.968  1.00 21.25 ? 4056 HOH A O   1 
HETATM 7062 O O   . HOH O 6 .   ? 15.831  -10.554 19.038 1.00 18.97 ? 4057 HOH A O   1 
HETATM 7063 O O   . HOH O 6 .   ? -14.563 14.515  22.022 1.00 11.91 ? 4058 HOH A O   1 
HETATM 7064 O O   . HOH O 6 .   ? -9.559  -26.494 32.647 1.00 17.03 ? 4059 HOH A O   1 
HETATM 7065 O O   . HOH O 6 .   ? -23.255 -15.400 21.295 1.00 14.44 ? 4060 HOH A O   1 
HETATM 7066 O O   . HOH O 6 .   ? 2.661   -5.950  64.553 1.00 16.94 ? 4061 HOH A O   1 
HETATM 7067 O O   . HOH O 6 .   ? -3.579  -24.598 58.784 1.00 17.29 ? 4062 HOH A O   1 
HETATM 7068 O O   . HOH O 6 .   ? -0.018  -2.696  41.331 1.00 21.26 ? 4063 HOH A O   1 
HETATM 7069 O O   . HOH O 6 .   ? -25.279 18.265  31.010 1.00 18.20 ? 4064 HOH A O   1 
HETATM 7070 O O   . HOH O 6 .   ? -40.647 0.158   27.975 1.00 21.18 ? 4065 HOH A O   1 
HETATM 7071 O O   . HOH O 6 .   ? -24.584 -19.753 33.998 1.00 20.22 ? 4066 HOH A O   1 
HETATM 7072 O O   . HOH O 6 .   ? 6.324   -12.126 60.981 1.00 13.67 ? 4067 HOH A O   1 
HETATM 7073 O O   . HOH O 6 .   ? -29.955 -7.655  20.650 1.00 30.21 ? 4068 HOH A O   1 
HETATM 7074 O O   . HOH O 6 .   ? -25.015 -4.280  10.179 1.00 26.37 ? 4069 HOH A O   1 
HETATM 7075 O O   . HOH O 6 .   ? -9.958  0.412   45.729 1.00 23.74 ? 4070 HOH A O   1 
HETATM 7076 O O   . HOH O 6 .   ? -25.673 -17.603 28.002 1.00 19.49 ? 4071 HOH A O   1 
HETATM 7077 O O   . HOH O 6 .   ? -4.139  -12.385 43.051 1.00 13.15 ? 4072 HOH A O   1 
HETATM 7078 O O   . HOH O 6 .   ? -7.889  -18.370 26.508 1.00 21.72 ? 4073 HOH A O   1 
HETATM 7079 O O   . HOH O 6 .   ? -6.165  -24.176 33.358 1.00 21.32 ? 4074 HOH A O   1 
HETATM 7080 O O   . HOH O 6 .   ? 14.600  -19.746 56.911 1.00 23.95 ? 4075 HOH A O   1 
HETATM 7081 O O   . HOH O 6 .   ? 19.368  -15.579 17.800 1.00 24.51 ? 4076 HOH A O   1 
HETATM 7082 O O   . HOH O 6 .   ? -23.857 -8.931  60.339 1.00 29.55 ? 4077 HOH A O   1 
HETATM 7083 O O   . HOH O 6 .   ? 13.346  -10.571 19.785 1.00 20.75 ? 4078 HOH A O   1 
HETATM 7084 O O   . HOH O 6 .   ? -32.503 -3.424  40.683 1.00 25.92 ? 4079 HOH A O   1 
HETATM 7085 O O   . HOH O 6 .   ? -0.576  6.241   22.295 1.00 22.55 ? 4080 HOH A O   1 
HETATM 7086 O O   . HOH O 6 .   ? -11.157 3.716   9.812  1.00 18.24 ? 4081 HOH A O   1 
HETATM 7087 O O   . HOH O 6 .   ? 0.187   -20.121 36.818 1.00 18.43 ? 4082 HOH A O   1 
HETATM 7088 O O   . HOH O 6 .   ? 4.649   -32.274 40.175 1.00 25.15 ? 4083 HOH A O   1 
HETATM 7089 O O   . HOH O 6 .   ? -17.189 -16.988 66.227 1.00 31.97 ? 4084 HOH A O   1 
HETATM 7090 O O   . HOH O 6 .   ? 10.084  -28.003 47.652 1.00 20.07 ? 4085 HOH A O   1 
HETATM 7091 O O   . HOH O 6 .   ? -24.270 3.503   36.576 1.00 35.50 ? 4086 HOH A O   1 
HETATM 7092 O O   . HOH O 6 .   ? -7.384  -35.291 48.959 1.00 26.68 ? 4087 HOH A O   1 
HETATM 7093 O O   . HOH O 6 .   ? -11.472 -3.406  23.530 1.00 19.52 ? 4088 HOH A O   1 
HETATM 7094 O O   . HOH O 6 .   ? -17.186 -13.052 42.486 1.00 23.05 ? 4089 HOH A O   1 
HETATM 7095 O O   . HOH O 6 .   ? -11.759 -18.837 25.066 1.00 13.67 ? 4090 HOH A O   1 
HETATM 7096 O O   . HOH O 6 .   ? 6.834   -12.778 6.145  1.00 27.53 ? 4091 HOH A O   1 
HETATM 7097 O O   . HOH O 6 .   ? -39.307 20.665  19.086 1.00 27.97 ? 4092 HOH A O   1 
HETATM 7098 O O   . HOH O 6 .   ? 0.489   -31.428 53.160 1.00 18.45 ? 4093 HOH A O   1 
HETATM 7099 O O   . HOH O 6 .   ? 12.662  -27.467 52.554 1.00 18.67 ? 4094 HOH A O   1 
HETATM 7100 O O   . HOH O 6 .   ? 6.169   -10.394 51.865 1.00 20.71 ? 4095 HOH A O   1 
HETATM 7101 O O   . HOH O 6 .   ? -11.001 -19.585 34.463 1.00 19.35 ? 4096 HOH A O   1 
HETATM 7102 O O   . HOH O 6 .   ? -14.914 -25.411 57.249 1.00 25.44 ? 4097 HOH A O   1 
HETATM 7103 O O   . HOH O 6 .   ? -6.350  -17.959 30.376 1.00 23.22 ? 4098 HOH A O   1 
HETATM 7104 O O   . HOH O 6 .   ? 16.344  -14.478 13.699 1.00 25.44 ? 4099 HOH A O   1 
HETATM 7105 O O   . HOH O 6 .   ? -21.845 -5.012  58.503 1.00 31.25 ? 4100 HOH A O   1 
HETATM 7106 O O   . HOH O 6 .   ? -14.853 6.938   12.021 1.00 32.73 ? 4101 HOH A O   1 
HETATM 7107 O O   . HOH O 6 .   ? -3.975  -39.318 51.802 1.00 20.31 ? 4102 HOH A O   1 
HETATM 7108 O O   . HOH O 6 .   ? -14.800 2.083   7.921  1.00 24.16 ? 4103 HOH A O   1 
HETATM 7109 O O   . HOH O 6 .   ? -23.238 17.023  31.584 1.00 27.16 ? 4104 HOH A O   1 
HETATM 7110 O O   . HOH O 6 .   ? -3.083  -31.786 46.439 1.00 25.76 ? 4105 HOH A O   1 
HETATM 7111 O O   . HOH O 6 .   ? -26.342 -21.273 25.005 1.00 28.03 ? 4106 HOH A O   1 
HETATM 7112 O O   . HOH O 6 .   ? 7.713   -14.562 50.085 1.00 17.11 ? 4107 HOH A O   1 
HETATM 7113 O O   . HOH O 6 .   ? -2.730  7.414   22.516 1.00 34.34 ? 4108 HOH A O   1 
HETATM 7114 O O   . HOH O 6 .   ? -12.571 -6.339  67.218 1.00 35.77 ? 4109 HOH A O   1 
HETATM 7115 O O   . HOH O 6 .   ? -20.659 1.022   11.012 1.00 24.66 ? 4110 HOH A O   1 
HETATM 7116 O O   . HOH O 6 .   ? -35.198 -2.696  38.449 1.00 20.06 ? 4111 HOH A O   1 
HETATM 7117 O O   . HOH O 6 .   ? -9.905  7.719   20.826 1.00 29.56 ? 4112 HOH A O   1 
HETATM 7118 O O   . HOH O 6 .   ? -18.118 19.668  25.114 1.00 27.04 ? 4113 HOH A O   1 
HETATM 7119 O O   . HOH O 6 .   ? -44.617 6.578   33.936 1.00 28.58 ? 4114 HOH A O   1 
HETATM 7120 O O   . HOH O 6 .   ? 3.229   7.918   29.207 1.00 22.70 ? 4115 HOH A O   1 
HETATM 7121 O O   . HOH O 6 .   ? -14.023 10.795  27.606 1.00 21.33 ? 4116 HOH A O   1 
HETATM 7122 O O   . HOH O 6 .   ? -4.998  1.731   27.400 1.00 15.38 ? 4117 HOH A O   1 
HETATM 7123 O O   . HOH O 6 .   ? -23.202 -14.757 38.936 1.00 23.84 ? 4118 HOH A O   1 
HETATM 7124 O O   . HOH O 6 .   ? 19.847  -13.918 29.751 1.00 20.41 ? 4119 HOH A O   1 
HETATM 7125 O O   . HOH O 6 .   ? 7.423   -21.492 33.256 1.00 24.91 ? 4120 HOH A O   1 
HETATM 7126 O O   . HOH O 6 .   ? -38.508 12.332  19.499 1.00 21.32 ? 4121 HOH A O   1 
HETATM 7127 O O   . HOH O 6 .   ? 2.926   -32.166 37.949 1.00 33.50 ? 4122 HOH A O   1 
HETATM 7128 O O   . HOH O 6 .   ? 26.144  -15.818 27.379 1.00 38.79 ? 4123 HOH A O   1 
HETATM 7129 O O   . HOH O 6 .   ? -4.415  5.447   34.919 1.00 30.87 ? 4124 HOH A O   1 
HETATM 7130 O O   . HOH O 6 .   ? -11.203 22.083  29.455 1.00 28.84 ? 4125 HOH A O   1 
HETATM 7131 O O   . HOH O 6 .   ? -11.500 12.388  19.379 1.00 20.13 ? 4126 HOH A O   1 
HETATM 7132 O O   . HOH O 6 .   ? -16.035 -8.314  2.744  1.00 31.15 ? 4127 HOH A O   1 
HETATM 7133 O O   . HOH O 6 .   ? 4.792   -25.913 34.457 1.00 22.16 ? 4128 HOH A O   1 
HETATM 7134 O O   . HOH O 6 .   ? -33.802 -10.787 45.092 1.00 26.18 ? 4129 HOH A O   1 
HETATM 7135 O O   . HOH O 6 .   ? 16.007  -14.903 45.736 1.00 29.43 ? 4130 HOH A O   1 
HETATM 7136 O O   . HOH O 6 .   ? -12.359 1.942   11.427 1.00 26.33 ? 4131 HOH A O   1 
HETATM 7137 O O   . HOH O 6 .   ? 10.584  -13.834 23.866 1.00 20.54 ? 4132 HOH A O   1 
HETATM 7138 O O   . HOH O 6 .   ? -5.106  -29.836 52.092 1.00 22.88 ? 4133 HOH A O   1 
HETATM 7139 O O   . HOH O 6 .   ? -12.283 13.437  21.607 1.00 20.43 ? 4134 HOH A O   1 
HETATM 7140 O O   . HOH O 6 .   ? -4.448  -23.328 21.298 1.00 30.09 ? 4135 HOH A O   1 
HETATM 7141 O O   . HOH O 6 .   ? -4.349  2.233   43.363 1.00 26.19 ? 4136 HOH A O   1 
HETATM 7142 O O   . HOH O 6 .   ? 11.760  -11.911 8.248  1.00 25.44 ? 4137 HOH A O   1 
HETATM 7143 O O   . HOH O 6 .   ? -8.768  -18.373 31.631 1.00 24.41 ? 4138 HOH A O   1 
HETATM 7144 O O   . HOH O 6 .   ? -9.933  -21.913 26.491 1.00 28.10 ? 4139 HOH A O   1 
HETATM 7145 O O   . HOH O 6 .   ? -32.984 13.690  41.646 1.00 33.37 ? 4140 HOH A O   1 
HETATM 7146 O O   . HOH O 6 .   ? 5.775   5.098   11.281 1.00 37.30 ? 4141 HOH A O   1 
HETATM 7147 O O   . HOH O 6 .   ? 1.403   -4.361  54.113 1.00 24.61 ? 4142 HOH A O   1 
HETATM 7148 O O   . HOH O 6 .   ? -10.422 -38.393 64.385 1.00 35.72 ? 4143 HOH A O   1 
HETATM 7149 O O   . HOH O 6 .   ? 7.357   -15.656 47.735 1.00 20.85 ? 4144 HOH A O   1 
HETATM 7150 O O   . HOH O 6 .   ? -2.237  5.201   0.892  1.00 22.80 ? 4145 HOH A O   1 
HETATM 7151 O O   . HOH O 6 .   ? 8.366   -22.288 25.800 1.00 30.44 ? 4146 HOH A O   1 
HETATM 7152 O O   . HOH O 6 .   ? -7.854  -27.648 51.937 1.00 14.14 ? 4147 HOH A O   1 
HETATM 7153 O O   . HOH O 6 .   ? -22.885 -21.874 9.656  1.00 28.02 ? 4148 HOH A O   1 
HETATM 7154 O O   . HOH O 6 .   ? -16.921 -0.136  37.195 1.00 13.28 ? 4149 HOH A O   1 
HETATM 7155 O O   . HOH O 6 .   ? 4.046   -4.557  62.784 1.00 33.52 ? 4150 HOH A O   1 
HETATM 7156 O O   . HOH O 6 .   ? 9.541   -11.877 11.414 1.00 22.16 ? 4151 HOH A O   1 
HETATM 7157 O O   . HOH O 6 .   ? 14.648  -2.799  10.738 1.00 27.28 ? 4152 HOH A O   1 
HETATM 7158 O O   . HOH O 6 .   ? -11.600 -10.259 23.008 1.00 13.46 ? 4153 HOH A O   1 
HETATM 7159 O O   . HOH O 6 .   ? 16.293  -32.313 36.463 1.00 22.31 ? 4154 HOH A O   1 
HETATM 7160 O O   . HOH O 6 .   ? -41.404 -5.645  21.714 1.00 36.28 ? 4155 HOH A O   1 
HETATM 7161 O O   . HOH O 6 .   ? -13.682 -17.041 6.262  1.00 28.37 ? 4156 HOH A O   1 
HETATM 7162 O O   . HOH O 6 .   ? 11.287  -12.233 19.113 1.00 24.41 ? 4157 HOH A O   1 
HETATM 7163 O O   . HOH O 6 .   ? -18.849 0.572   38.652 1.00 20.64 ? 4158 HOH A O   1 
HETATM 7164 O O   . HOH O 6 .   ? -6.906  -32.472 45.089 1.00 17.94 ? 4159 HOH A O   1 
HETATM 7165 O O   . HOH O 6 .   ? -25.603 -14.771 21.222 1.00 19.86 ? 4160 HOH A O   1 
HETATM 7166 O O   . HOH O 6 .   ? -19.784 -19.716 30.179 1.00 22.29 ? 4161 HOH A O   1 
HETATM 7167 O O   . HOH O 6 .   ? 25.192  -18.615 30.453 1.00 22.78 ? 4162 HOH A O   1 
HETATM 7168 O O   . HOH O 6 .   ? 4.166   7.745   35.676 1.00 39.16 ? 4163 HOH A O   1 
HETATM 7169 O O   . HOH O 6 .   ? -12.687 21.342  41.327 1.00 34.23 ? 4164 HOH A O   1 
HETATM 7170 O O   . HOH O 6 .   ? 10.211  0.718   4.283  1.00 33.89 ? 4165 HOH A O   1 
HETATM 7171 O O   . HOH O 6 .   ? -17.691 -5.559  56.170 1.00 23.10 ? 4166 HOH A O   1 
HETATM 7172 O O   . HOH O 6 .   ? -36.025 -9.589  25.214 1.00 27.46 ? 4167 HOH A O   1 
HETATM 7173 O O   . HOH O 6 .   ? -22.364 5.462   33.327 1.00 21.82 ? 4168 HOH A O   1 
HETATM 7174 O O   . HOH O 6 .   ? -18.082 -21.190 63.150 1.00 42.15 ? 4169 HOH A O   1 
HETATM 7175 O O   . HOH O 6 .   ? -24.631 -15.458 5.515  1.00 27.85 ? 4170 HOH A O   1 
HETATM 7176 O O   . HOH O 6 .   ? -12.068 0.322   49.819 1.00 30.49 ? 4171 HOH A O   1 
HETATM 7177 O O   . HOH O 6 .   ? 11.902  -14.716 57.633 1.00 28.72 ? 4172 HOH A O   1 
HETATM 7178 O O   . HOH O 6 .   ? 7.349   -24.629 34.280 1.00 30.14 ? 4173 HOH A O   1 
HETATM 7179 O O   . HOH O 6 .   ? -31.429 2.401   22.363 1.00 44.07 ? 4174 HOH A O   1 
HETATM 7180 O O   . HOH O 6 .   ? -28.091 -17.269 52.409 1.00 29.27 ? 4175 HOH A O   1 
HETATM 7181 O O   . HOH O 6 .   ? -8.385  -31.423 47.540 1.00 28.05 ? 4176 HOH A O   1 
HETATM 7182 O O   . HOH O 6 .   ? -39.179 3.917   20.547 1.00 33.97 ? 4177 HOH A O   1 
HETATM 7183 O O   . HOH O 6 .   ? -5.648  -25.612 31.060 1.00 19.60 ? 4178 HOH A O   1 
HETATM 7184 O O   . HOH O 6 .   ? -7.371  11.038  11.681 1.00 38.49 ? 4179 HOH A O   1 
HETATM 7185 O O   . HOH O 6 .   ? 12.388  -9.451  34.876 1.00 20.47 ? 4180 HOH A O   1 
HETATM 7186 O O   . HOH O 6 .   ? -21.774 -0.174  40.669 1.00 27.46 ? 4181 HOH A O   1 
HETATM 7187 O O   . HOH O 6 .   ? -12.803 -20.736 32.694 1.00 22.46 ? 4182 HOH A O   1 
HETATM 7188 O O   . HOH O 6 .   ? 0.426   1.495   31.653 1.00 22.48 ? 4183 HOH A O   1 
HETATM 7189 O O   . HOH O 6 .   ? 22.188  -8.149  34.696 1.00 21.31 ? 4184 HOH A O   1 
HETATM 7190 O O   . HOH O 6 .   ? -22.333 -22.575 51.131 1.00 39.53 ? 4185 HOH A O   1 
HETATM 7191 O O   . HOH O 6 .   ? 9.848   -4.780  18.261 1.00 23.40 ? 4186 HOH A O   1 
HETATM 7192 O O   . HOH O 6 .   ? -18.106 -26.924 45.858 1.00 21.60 ? 4187 HOH A O   1 
HETATM 7193 O O   . HOH O 6 .   ? -21.063 2.051   38.557 1.00 28.51 ? 4188 HOH A O   1 
HETATM 7194 O O   . HOH O 6 .   ? -0.745  -20.698 15.654 1.00 21.31 ? 4189 HOH A O   1 
HETATM 7195 O O   . HOH O 6 .   ? -33.300 9.070   41.895 1.00 39.80 ? 4190 HOH A O   1 
HETATM 7196 O O   . HOH O 6 .   ? 3.912   -48.675 59.331 1.00 30.27 ? 4191 HOH A O   1 
HETATM 7197 O O   . HOH O 6 .   ? -11.407 -4.135  0.395  1.00 33.11 ? 4192 HOH A O   1 
HETATM 7198 O O   . HOH O 6 .   ? -8.971  -31.294 60.265 1.00 25.70 ? 4193 HOH A O   1 
HETATM 7199 O O   . HOH O 6 .   ? -12.937 -28.829 24.018 1.00 33.19 ? 4194 HOH A O   1 
HETATM 7200 O O   . HOH O 6 .   ? 1.491   -10.572 -0.165 1.00 33.25 ? 4195 HOH A O   1 
HETATM 7201 O O   . HOH O 6 .   ? -8.753  -8.552  67.379 1.00 25.06 ? 4196 HOH A O   1 
HETATM 7202 O O   . HOH O 6 .   ? -6.000  -28.516 38.225 1.00 31.77 ? 4197 HOH A O   1 
HETATM 7203 O O   . HOH O 6 .   ? -20.925 -23.246 10.853 1.00 25.02 ? 4198 HOH A O   1 
HETATM 7204 O O   . HOH O 6 .   ? 6.105   -7.586  54.735 1.00 35.08 ? 4199 HOH A O   1 
HETATM 7205 O O   . HOH O 6 .   ? -18.589 -28.635 41.962 1.00 42.83 ? 4200 HOH A O   1 
HETATM 7206 O O   . HOH O 6 .   ? -12.073 15.262  24.256 1.00 21.95 ? 4201 HOH A O   1 
HETATM 7207 O O   . HOH O 6 .   ? -43.021 -0.814  30.470 1.00 23.74 ? 4202 HOH A O   1 
HETATM 7208 O O   . HOH O 6 .   ? -3.022  -43.954 62.374 1.00 29.19 ? 4203 HOH A O   1 
HETATM 7209 O O   . HOH O 6 .   ? 6.272   -4.646  49.233 1.00 31.76 ? 4204 HOH A O   1 
HETATM 7210 O O   . HOH O 6 .   ? 2.642   -7.767  51.773 1.00 21.97 ? 4205 HOH A O   1 
HETATM 7211 O O   . HOH O 6 .   ? 4.938   -15.312 71.863 1.00 22.39 ? 4206 HOH A O   1 
HETATM 7212 O O   . HOH O 6 .   ? 4.512   9.764   21.286 1.00 30.64 ? 4207 HOH A O   1 
HETATM 7213 O O   . HOH O 6 .   ? 4.788   -6.356  50.565 1.00 25.87 ? 4208 HOH A O   1 
HETATM 7214 O O   . HOH O 6 .   ? 20.306  -7.181  36.240 1.00 26.47 ? 4209 HOH A O   1 
HETATM 7215 O O   . HOH O 6 .   ? -49.809 6.934   28.599 1.00 27.74 ? 4210 HOH A O   1 
HETATM 7216 O O   . HOH O 6 .   ? 18.697  0.629   24.392 1.00 24.28 ? 4211 HOH A O   1 
HETATM 7217 O O   . HOH O 6 .   ? -15.731 -5.684  2.859  1.00 27.33 ? 4212 HOH A O   1 
HETATM 7218 O O   . HOH O 6 .   ? -20.570 4.060   37.015 1.00 41.26 ? 4213 HOH A O   1 
HETATM 7219 O O   . HOH O 6 .   ? -29.333 -8.728  45.545 1.00 27.29 ? 4214 HOH A O   1 
HETATM 7220 O O   . HOH O 6 .   ? -1.988  -22.514 16.918 1.00 28.40 ? 4215 HOH A O   1 
HETATM 7221 O O   . HOH O 6 .   ? -25.923 -1.198  41.789 1.00 35.95 ? 4216 HOH A O   1 
HETATM 7222 O O   . HOH O 6 .   ? -4.591  -16.619 5.372  1.00 38.36 ? 4217 HOH A O   1 
HETATM 7223 O O   . HOH O 6 .   ? 4.884   -8.289  -0.465 1.00 38.24 ? 4218 HOH A O   1 
HETATM 7224 O O   . HOH O 6 .   ? -9.308  2.438   58.448 1.00 28.38 ? 4219 HOH A O   1 
HETATM 7225 O O   . HOH O 6 .   ? -19.398 -1.623  42.205 1.00 26.80 ? 4220 HOH A O   1 
HETATM 7226 O O   . HOH O 6 .   ? -22.616 -8.443  67.379 1.00 39.98 ? 4221 HOH A O   1 
HETATM 7227 O O   . HOH O 6 .   ? -15.891 -36.095 49.361 1.00 26.13 ? 4222 HOH A O   1 
HETATM 7228 O O   . HOH O 6 .   ? -24.102 20.643  20.791 1.00 34.11 ? 4223 HOH A O   1 
HETATM 7229 O O   . HOH O 6 .   ? 6.833   -8.021  50.616 1.00 23.66 ? 4224 HOH A O   1 
HETATM 7230 O O   . HOH O 6 .   ? 15.556  -0.354  19.217 1.00 25.53 ? 4225 HOH A O   1 
HETATM 7231 O O   . HOH O 6 .   ? -24.772 20.910  39.204 1.00 30.51 ? 4226 HOH A O   1 
HETATM 7232 O O   . HOH O 6 .   ? -15.759 -37.571 47.626 1.00 23.32 ? 4227 HOH A O   1 
HETATM 7233 O O   . HOH O 6 .   ? -9.912  -0.649  53.950 1.00 37.85 ? 4228 HOH A O   1 
HETATM 7234 O O   . HOH O 6 .   ? -25.024 -26.422 14.280 1.00 34.49 ? 4229 HOH A O   1 
HETATM 7235 O O   . HOH O 6 .   ? 0.354   -0.894  51.425 1.00 33.69 ? 4230 HOH A O   1 
HETATM 7236 O O   . HOH O 6 .   ? -26.531 8.281   21.337 1.00 33.74 ? 4231 HOH A O   1 
HETATM 7237 O O   . HOH O 6 .   ? 5.176   -47.089 51.229 1.00 40.51 ? 4232 HOH A O   1 
HETATM 7238 O O   . HOH O 6 .   ? -11.174 -4.576  37.940 1.00 27.75 ? 4233 HOH A O   1 
HETATM 7239 O O   . HOH O 6 .   ? 4.229   -21.170 76.440 1.00 30.24 ? 4234 HOH A O   1 
HETATM 7240 O O   . HOH O 6 .   ? -8.573  -26.462 11.795 1.00 24.48 ? 4235 HOH A O   1 
HETATM 7241 O O   . HOH O 6 .   ? 20.428  -11.085 15.641 1.00 25.61 ? 4236 HOH A O   1 
HETATM 7242 O O   . HOH O 6 .   ? -2.582  -14.939 5.083  1.00 32.89 ? 4237 HOH A O   1 
HETATM 7243 O O   . HOH O 6 .   ? -19.662 -25.356 15.086 1.00 34.50 ? 4238 HOH A O   1 
HETATM 7244 O O   . HOH O 6 .   ? -27.547 10.339  20.198 1.00 30.29 ? 4239 HOH A O   1 
HETATM 7245 O O   . HOH O 6 .   ? 4.049   -6.475  1.269  1.00 26.39 ? 4240 HOH A O   1 
HETATM 7246 O O   . HOH O 6 .   ? -20.024 2.836   12.872 1.00 31.19 ? 4241 HOH A O   1 
HETATM 7247 O O   . HOH O 6 .   ? -20.212 18.921  17.720 1.00 34.26 ? 4242 HOH A O   1 
HETATM 7248 O O   . HOH O 6 .   ? 25.270  -14.150 25.048 1.00 42.91 ? 4243 HOH A O   1 
HETATM 7249 O O   . HOH O 6 .   ? -44.741 -3.393  27.460 1.00 36.10 ? 4244 HOH A O   1 
HETATM 7250 O O   . HOH O 6 .   ? -21.825 -23.288 39.252 1.00 37.01 ? 4245 HOH A O   1 
HETATM 7251 O O   . HOH O 6 .   ? -45.576 -0.044  17.887 1.00 44.24 ? 4246 HOH A O   1 
HETATM 7252 O O   . HOH O 6 .   ? -4.127  2.854   38.687 1.00 21.57 ? 4247 HOH A O   1 
HETATM 7253 O O   . HOH O 6 .   ? -29.778 -20.313 38.054 1.00 47.45 ? 4248 HOH A O   1 
HETATM 7254 O O   . HOH O 6 .   ? -32.421 27.382  25.826 1.00 36.84 ? 4249 HOH A O   1 
HETATM 7255 O O   . HOH O 6 .   ? -27.578 -18.535 29.767 1.00 31.42 ? 4250 HOH A O   1 
HETATM 7256 O O   . HOH O 6 .   ? 13.857  -17.511 51.094 1.00 22.08 ? 4251 HOH A O   1 
HETATM 7257 O O   . HOH O 6 .   ? 0.537   2.625   34.136 1.00 32.80 ? 4252 HOH A O   1 
HETATM 7258 O O   . HOH O 6 .   ? 18.393  -1.448  16.179 1.00 27.00 ? 4253 HOH A O   1 
HETATM 7259 O O   . HOH O 6 .   ? -48.180 15.173  36.168 1.00 44.11 ? 4254 HOH A O   1 
HETATM 7260 O O   . HOH O 6 .   ? 11.641  -12.389 56.107 1.00 24.65 ? 4255 HOH A O   1 
HETATM 7261 O O   . HOH O 6 .   ? -8.854  -33.465 43.064 1.00 40.76 ? 4256 HOH A O   1 
HETATM 7262 O O   . HOH O 6 .   ? -20.895 -2.220  46.914 1.00 20.61 ? 4257 HOH A O   1 
HETATM 7263 O O   . HOH O 6 .   ? -25.771 16.706  20.383 1.00 46.63 ? 4258 HOH A O   1 
HETATM 7264 O O   . HOH O 6 .   ? 6.808   -11.777 69.920 1.00 31.03 ? 4259 HOH A O   1 
HETATM 7265 O O   . HOH O 6 .   ? -24.258 24.143  35.479 1.00 28.10 ? 4260 HOH A O   1 
HETATM 7266 O O   . HOH O 6 .   ? -42.253 8.339   34.230 1.00 42.00 ? 4261 HOH A O   1 
HETATM 7267 O O   . HOH O 6 .   ? -34.414 -11.399 23.905 1.00 41.07 ? 4262 HOH A O   1 
HETATM 7268 O O   . HOH O 6 .   ? -0.969  -29.112 35.890 1.00 22.80 ? 4263 HOH A O   1 
HETATM 7269 O O   . HOH O 6 .   ? -16.765 -3.275  71.099 1.00 73.80 ? 4264 HOH A O   1 
HETATM 7270 O O   . HOH O 6 .   ? -0.158  -20.888 24.822 1.00 25.49 ? 4265 HOH A O   1 
HETATM 7271 O O   . HOH O 6 .   ? -40.093 8.939   35.396 1.00 35.46 ? 4266 HOH A O   1 
HETATM 7272 O O   . HOH O 6 .   ? -27.292 -8.838  11.535 1.00 31.75 ? 4267 HOH A O   1 
HETATM 7273 O O   . HOH O 6 .   ? 12.176  -13.709 21.399 1.00 28.81 ? 4268 HOH A O   1 
HETATM 7274 O O   . HOH O 6 .   ? -28.638 17.625  40.462 1.00 46.89 ? 4269 HOH A O   1 
HETATM 7275 O O   . HOH O 6 .   ? 13.090  -21.516 49.575 1.00 23.25 ? 4270 HOH A O   1 
HETATM 7276 O O   . HOH O 6 .   ? 10.143  -15.345 25.768 1.00 24.98 ? 4271 HOH A O   1 
HETATM 7277 O O   . HOH O 6 .   ? 11.349  7.063   23.764 1.00 60.80 ? 4272 HOH A O   1 
HETATM 7278 O O   . HOH O 6 .   ? 30.227  -6.752  35.949 1.00 41.16 ? 4273 HOH A O   1 
HETATM 7279 O O   . HOH O 6 .   ? -17.099 -37.794 52.290 1.00 40.36 ? 4274 HOH A O   1 
HETATM 7280 O O   . HOH O 6 .   ? -18.714 -3.011  66.881 1.00 52.66 ? 4275 HOH A O   1 
HETATM 7281 O O   . HOH O 6 .   ? 4.310   -11.883 36.231 1.00 24.57 ? 4276 HOH A O   1 
HETATM 7282 O O   . HOH O 6 .   ? -8.015  1.663   53.144 1.00 25.81 ? 4277 HOH A O   1 
HETATM 7283 O O   . HOH O 6 .   ? 7.968   -15.617 73.959 1.00 31.99 ? 4278 HOH A O   1 
HETATM 7284 O O   . HOH O 6 .   ? -5.958  -3.631  33.207 1.00 35.86 ? 4279 HOH A O   1 
HETATM 7285 O O   . HOH O 6 .   ? -13.930 -35.796 43.969 1.00 37.16 ? 4280 HOH A O   1 
HETATM 7286 O O   . HOH O 6 .   ? -21.100 4.010   34.662 1.00 35.30 ? 4281 HOH A O   1 
HETATM 7287 O O   . HOH O 6 .   ? -14.025 11.813  5.945  1.00 36.89 ? 4282 HOH A O   1 
HETATM 7288 O O   . HOH O 6 .   ? -22.125 -15.694 7.777  1.00 25.27 ? 4283 HOH A O   1 
HETATM 7289 O O   . HOH O 6 .   ? -0.079  -32.623 44.868 1.00 32.99 ? 4284 HOH A O   1 
HETATM 7290 O O   . HOH O 6 .   ? -9.410  10.526  20.748 1.00 27.25 ? 4285 HOH A O   1 
HETATM 7291 O O   . HOH O 6 .   ? -14.816 -2.414  52.317 1.00 36.36 ? 4286 HOH A O   1 
HETATM 7292 O O   . HOH O 6 .   ? -21.682 -25.040 13.436 1.00 33.11 ? 4287 HOH A O   1 
HETATM 7293 O O   . HOH O 6 .   ? 12.423  -37.769 57.625 1.00 49.52 ? 4288 HOH A O   1 
HETATM 7294 O O   . HOH O 6 .   ? -8.296  4.315   62.418 1.00 28.83 ? 4289 HOH A O   1 
HETATM 7295 O O   . HOH O 6 .   ? -10.363 -19.494 11.276 1.00 26.03 ? 4290 HOH A O   1 
HETATM 7296 O O   . HOH O 6 .   ? 7.329   -7.583  68.809 1.00 29.52 ? 4291 HOH A O   1 
HETATM 7297 O O   . HOH O 6 .   ? -40.835 2.266   19.776 1.00 33.22 ? 4292 HOH A O   1 
HETATM 7298 O O   . HOH O 6 .   ? -33.239 6.169   42.401 1.00 35.23 ? 4293 HOH A O   1 
HETATM 7299 O O   . HOH O 6 .   ? -33.247 -23.868 25.927 1.00 41.25 ? 4294 HOH A O   1 
HETATM 7300 O O   . HOH O 6 .   ? 10.030  -38.768 57.561 1.00 51.82 ? 4295 HOH A O   1 
HETATM 7301 O O   . HOH O 6 .   ? 8.693   -14.282 9.866  1.00 31.52 ? 4296 HOH A O   1 
HETATM 7302 O O   . HOH O 6 .   ? -18.104 -4.492  2.536  1.00 31.52 ? 4297 HOH A O   1 
HETATM 7303 O O   . HOH O 6 .   ? -4.243  2.103   60.479 1.00 26.43 ? 4298 HOH A O   1 
HETATM 7304 O O   . HOH O 6 .   ? 10.633  -31.202 40.170 1.00 28.17 ? 4299 HOH A O   1 
HETATM 7305 O O   . HOH O 6 .   ? -16.604 -27.384 19.383 1.00 27.77 ? 4300 HOH A O   1 
HETATM 7306 O O   . HOH O 6 .   ? -41.477 -5.957  37.765 1.00 35.14 ? 4301 HOH A O   1 
HETATM 7307 O O   . HOH O 6 .   ? -31.563 -16.256 47.884 1.00 37.29 ? 4302 HOH A O   1 
HETATM 7308 O O   . HOH O 6 .   ? 27.366  -6.994  21.317 1.00 35.82 ? 4303 HOH A O   1 
HETATM 7309 O O   . HOH O 6 .   ? -48.161 6.203   20.812 1.00 34.17 ? 4304 HOH A O   1 
HETATM 7310 O O   . HOH O 6 .   ? -8.385  -24.569 24.268 1.00 30.65 ? 4305 HOH A O   1 
HETATM 7311 O O   . HOH O 6 .   ? 0.740   -13.671 45.197 1.00 27.52 ? 4306 HOH A O   1 
HETATM 7312 O O   . HOH O 6 .   ? -1.071  -17.569 8.262  1.00 26.86 ? 4307 HOH A O   1 
HETATM 7313 O O   . HOH O 6 .   ? -16.748 14.348  42.008 1.00 35.04 ? 4308 HOH A O   1 
HETATM 7314 O O   . HOH O 6 .   ? -3.315  -5.008  -0.426 1.00 39.45 ? 4309 HOH A O   1 
HETATM 7315 O O   . HOH O 6 .   ? 21.803  -21.363 35.490 1.00 28.25 ? 4310 HOH A O   1 
HETATM 7316 O O   . HOH O 6 .   ? -6.173  -40.431 49.296 1.00 22.31 ? 4311 HOH A O   1 
HETATM 7317 O O   . HOH O 6 .   ? -37.195 -14.475 24.105 1.00 41.65 ? 4312 HOH A O   1 
HETATM 7318 O O   . HOH O 6 .   ? -14.414 -20.007 58.039 1.00 23.01 ? 4313 HOH A O   1 
HETATM 7319 O O   . HOH O 6 .   ? -9.230  -5.661  0.776  1.00 38.67 ? 4314 HOH A O   1 
HETATM 7320 O O   . HOH O 6 .   ? -9.181  5.755   17.211 1.00 34.10 ? 4315 HOH A O   1 
HETATM 7321 O O   . HOH O 6 .   ? 13.478  4.876   33.222 1.00 37.29 ? 4316 HOH A O   1 
HETATM 7322 O O   . HOH O 6 .   ? -5.629  8.804   41.068 1.00 39.63 ? 4317 HOH A O   1 
HETATM 7323 O O   . HOH O 6 .   ? -15.084 12.431  41.296 1.00 45.10 ? 4318 HOH A O   1 
HETATM 7324 O O   . HOH O 6 .   ? 11.959  2.794   8.106  1.00 26.48 ? 4319 HOH A O   1 
HETATM 7325 O O   . HOH O 6 .   ? -10.446 -14.731 3.227  1.00 34.30 ? 4320 HOH A O   1 
HETATM 7326 O O   . HOH O 6 .   ? -3.673  -29.377 37.278 1.00 41.69 ? 4321 HOH A O   1 
HETATM 7327 O O   . HOH O 6 .   ? 18.171  -33.681 37.856 1.00 32.29 ? 4322 HOH A O   1 
HETATM 7328 O O   . HOH O 6 .   ? 14.168  2.793   35.559 1.00 32.07 ? 4323 HOH A O   1 
HETATM 7329 O O   . HOH O 6 .   ? -47.921 10.158  21.226 1.00 33.53 ? 4324 HOH A O   1 
HETATM 7330 O O   . HOH O 6 .   ? -15.144 20.963  39.862 1.00 26.12 ? 4325 HOH A O   1 
HETATM 7331 O O   . HOH O 6 .   ? 1.594   8.723   11.816 1.00 32.52 ? 4326 HOH A O   1 
HETATM 7332 O O   . HOH O 6 .   ? 2.051   10.386  22.178 1.00 30.36 ? 4327 HOH A O   1 
HETATM 7333 O O   . HOH O 6 .   ? 7.460   -8.020  62.917 1.00 30.81 ? 4328 HOH A O   1 
HETATM 7334 O O   . HOH O 6 .   ? -17.542 -20.603 65.551 1.00 44.50 ? 4329 HOH A O   1 
HETATM 7335 O O   . HOH O 6 .   ? -0.102  -23.401 24.023 1.00 26.90 ? 4330 HOH A O   1 
HETATM 7336 O O   . HOH O 6 .   ? 7.892   -11.287 7.657  1.00 32.75 ? 4331 HOH A O   1 
HETATM 7337 O O   . HOH O 6 .   ? -8.835  -17.747 4.389  1.00 29.70 ? 4332 HOH A O   1 
HETATM 7338 O O   . HOH O 6 .   ? 20.091  -20.103 17.080 1.00 32.67 ? 4333 HOH A O   1 
HETATM 7339 O O   . HOH O 6 .   ? 6.887   -14.051 7.940  1.00 29.23 ? 4334 HOH A O   1 
HETATM 7340 O O   . HOH O 6 .   ? -32.873 -6.554  18.274 1.00 54.31 ? 4335 HOH A O   1 
HETATM 7341 O O   . HOH O 6 .   ? -27.254 -4.463  43.364 1.00 29.04 ? 4336 HOH A O   1 
HETATM 7342 O O   . HOH O 6 .   ? 0.393   -9.934  12.209 1.00 27.42 ? 4337 HOH A O   1 
HETATM 7343 O O   . HOH O 6 .   ? -7.405  -4.726  -0.867 1.00 45.88 ? 4338 HOH A O   1 
HETATM 7344 O O   . HOH O 6 .   ? -18.743 26.658  29.185 1.00 41.01 ? 4339 HOH A O   1 
HETATM 7345 O O   . HOH O 6 .   ? -26.042 -20.713 17.388 1.00 31.62 ? 4340 HOH A O   1 
HETATM 7346 O O   . HOH O 6 .   ? 10.834  6.605   30.897 1.00 30.15 ? 4341 HOH A O   1 
HETATM 7347 O O   . HOH O 6 .   ? 5.535   11.629  19.899 1.00 46.03 ? 4342 HOH A O   1 
HETATM 7348 O O   . HOH O 6 .   ? -16.672 -13.706 69.621 1.00 48.12 ? 4343 HOH A O   1 
HETATM 7349 O O   . HOH O 6 .   ? -33.060 4.207   41.228 1.00 34.83 ? 4344 HOH A O   1 
HETATM 7350 O O   . HOH O 6 .   ? -27.084 -19.949 14.679 1.00 37.16 ? 4345 HOH A O   1 
HETATM 7351 O O   . HOH O 6 .   ? 9.314   4.221   4.523  1.00 40.17 ? 4346 HOH A O   1 
HETATM 7352 O O   . HOH O 6 .   ? 12.912  -32.615 40.233 1.00 29.15 ? 4347 HOH A O   1 
HETATM 7353 O O   . HOH O 6 .   ? 16.175  -19.136 46.503 1.00 39.54 ? 4348 HOH A O   1 
HETATM 7354 O O   . HOH O 6 .   ? -0.123  -0.738  53.894 1.00 41.14 ? 4349 HOH A O   1 
HETATM 7355 O O   . HOH O 6 .   ? -14.979 -26.988 58.730 1.00 25.87 ? 4350 HOH A O   1 
HETATM 7356 O O   . HOH O 6 .   ? -28.150 -21.804 13.643 1.00 43.95 ? 4351 HOH A O   1 
HETATM 7357 O O   . HOH O 6 .   ? 5.796   -13.688 20.417 1.00 20.64 ? 4352 HOH A O   1 
HETATM 7358 O O   . HOH O 6 .   ? -3.183  -15.840 21.346 1.00 17.63 ? 4353 HOH A 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   SER 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   CYS 4   4   ?   ?   ?   A . n 
A 1 5   PRO 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   ?   ?   ?   A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  CYS 15  15  15  CYS CYS A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  CYS 26  26  26  CYS CYS A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  CYS 31  31  31  CYS CYS A . n 
A 1 32  CYS 32  32  32  CYS CYS A . n 
A 1 33  TRP 33  33  33  TRP TRP A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  ASN 60  60  60  ASN ASN A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ALA 67  67  67  ALA ALA 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  LYS 70  70  70  LYS LYS A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 HIS 115 115 115 HIS HIS A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 TYR 129 129 129 TYR TYR A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 HIS 183 183 183 HIS HIS A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 HIS 185 185 185 HIS HIS A . n 
A 1 186 GLN 186 186 186 GLN GLN A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 HIS 190 190 190 HIS HIS A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 TRP 197 197 197 TRP TRP A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 CYS 222 222 222 CYS CYS A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 THR 252 252 252 THR THR A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 GLN 275 275 275 GLN GLN A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 TYR 277 277 277 TYR TYR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 TYR 289 289 289 TYR TYR A . n 
A 1 290 TRP 290 290 290 TRP TRP A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 HIS 295 295 295 HIS HIS A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 ASN 306 306 306 ASN ASN A . n 
A 1 307 MET 307 307 307 MET MET A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 ARG 313 313 313 ARG ARG A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 ARG 315 315 315 ARG ARG A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 GLN 318 318 318 GLN GLN A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 TYR 321 321 321 TYR TYR A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 GLN 324 324 324 GLN GLN A . n 
A 1 325 HIS 325 325 325 HIS HIS A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 ASP 327 327 327 ASP ASP A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 MET 331 331 331 MET MET A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 ARG 334 334 334 ARG ARG A . n 
A 1 335 ARG 335 335 335 ARG ARG A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 THR 338 338 338 THR THR A . n 
A 1 339 TYR 339 339 339 TYR TYR A . n 
A 1 340 ASP 340 340 340 ASP ASP A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 PHE 344 344 344 PHE PHE A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 GLU 349 349 349 GLU GLU A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 HIS 355 355 355 HIS HIS A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ASN 357 357 357 ASN ASN A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 ASP 366 366 366 ASP ASP A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 ASN 372 372 372 ASN ASN A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 TYR 379 379 379 TYR TYR A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 PRO 381 381 381 PRO PRO A . n 
A 1 382 TYR 382 382 382 TYR TYR A . n 
A 1 383 ASP 383 383 383 ASP ASP A . n 
A 1 384 ARG 384 384 384 ARG ARG A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 ASP 387 387 387 ASP ASP A . n 
A 1 388 MET 388 388 388 MET MET A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 VAL 392 392 392 VAL VAL A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 PRO 400 400 400 PRO PRO 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 GLY 403 403 403 GLY GLY A . n 
A 1 404 GLU 404 404 404 GLU GLU A . n 
A 1 405 VAL 405 405 405 VAL VAL A . n 
A 1 406 TRP 406 406 406 TRP TRP A . n 
A 1 407 PRO 407 407 407 PRO PRO A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 GLN 409 409 409 GLN GLN A . n 
A 1 410 THR 410 410 410 THR THR A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 PRO 413 413 413 PRO PRO A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 THR 416 416 416 THR THR A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 CYS 420 420 420 CYS CYS A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 VAL 422 422 422 VAL VAL A . n 
A 1 423 TRP 423 423 423 TRP TRP A . n 
A 1 424 TRP 424 424 424 TRP TRP A . n 
A 1 425 THR 425 425 425 THR THR A . n 
A 1 426 LYS 426 426 426 LYS LYS A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 PHE 428 428 428 PHE PHE A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 PHE 431 431 431 PHE PHE A . n 
A 1 432 HIS 432 432 432 HIS HIS A . n 
A 1 433 ASN 433 433 433 ASN ASN A . n 
A 1 434 GLN 434 434 434 GLN GLN A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 GLU 436 436 436 GLU GLU A . n 
A 1 437 PHE 437 437 437 PHE PHE A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 ILE 440 440 440 ILE ILE A . n 
A 1 441 TRP 441 441 441 TRP TRP A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 MET 444 444 444 MET MET A . n 
A 1 445 ASN 445 445 445 ASN ASN A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 VAL 447 447 447 VAL VAL A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 ASN 449 449 449 ASN ASN A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 ASP 452 452 452 ASP ASP A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 SER 456 456 456 SER SER A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 CYS 458 458 458 CYS CYS A . n 
A 1 459 SER 459 459 459 SER SER A . n 
A 1 460 THR 460 460 460 THR THR A . n 
A 1 461 ASN 461 461 461 ASN ASN A . n 
A 1 462 ASN 462 462 462 ASN ASN A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 ASN 464 464 464 ASN ASN A . n 
A 1 465 ASN 465 465 465 ASN ASN A . n 
A 1 466 PRO 466 466 466 PRO PRO A . n 
A 1 467 PRO 467 467 467 PRO PRO A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 THR 469 469 469 THR THR A . n 
A 1 470 PRO 470 470 470 PRO PRO A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 LEU 473 473 473 LEU LEU A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 GLY 475 475 475 GLY GLY A . n 
A 1 476 TYR 476 476 476 TYR TYR A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 PHE 478 478 478 PHE PHE A . n 
A 1 479 CYS 479 479 479 CYS CYS A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 CYS 483 483 483 CYS CYS A . n 
A 1 484 MET 484 484 484 MET MET A . n 
A 1 485 ASP 485 485 485 ASP ASP A . n 
A 1 486 ALA 486 486 486 ALA ALA A . n 
A 1 487 VAL 487 487 487 VAL VAL A . n 
A 1 488 GLN 488 488 488 GLN GLN A . n 
A 1 489 HIS 489 489 489 HIS HIS A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 LYS 492 492 492 LYS LYS A . n 
A 1 493 GLN 493 493 493 GLN GLN A . n 
A 1 494 TYR 494 494 494 TYR TYR A . n 
A 1 495 ASP 495 495 495 ASP ASP A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 HIS 497 497 497 HIS HIS A . n 
A 1 498 ASN 498 498 498 ASN ASN A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 TYR 500 500 500 TYR TYR A . n 
A 1 501 GLY 501 501 501 GLY GLY A . n 
A 1 502 TYR 502 502 502 TYR TYR A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 MET 504 504 504 MET MET A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 VAL 506 506 506 VAL VAL A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 THR 508 508 508 THR THR A . n 
A 1 509 ALA 509 509 509 ALA ALA A . n 
A 1 510 GLU 510 510 510 GLU GLU A . n 
A 1 511 ALA 511 511 511 ALA ALA A . n 
A 1 512 ALA 512 512 512 ALA ALA A . n 
A 1 513 LYS 513 513 513 LYS LYS A . n 
A 1 514 THR 514 514 514 THR THR A . n 
A 1 515 VAL 515 515 515 VAL VAL A . n 
A 1 516 PHE 516 516 516 PHE PHE A . n 
A 1 517 PRO 517 517 517 PRO PRO A . n 
A 1 518 ASN 518 518 518 ASN ASN A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 ARG 520 520 520 ARG ARG A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 PHE 522 522 522 PHE PHE A . n 
A 1 523 ILE 523 523 523 ILE ILE A . n 
A 1 524 LEU 524 524 524 LEU LEU A . n 
A 1 525 THR 525 525 525 THR THR A . n 
A 1 526 ARG 526 526 526 ARG ARG A . n 
A 1 527 SER 527 527 527 SER SER A . n 
A 1 528 THR 528 528 528 THR THR A . n 
A 1 529 PHE 529 529 529 PHE PHE A . n 
A 1 530 ALA 530 530 530 ALA ALA A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 SER 532 532 532 SER SER A . n 
A 1 533 GLY 533 533 533 GLY GLY A . n 
A 1 534 LYS 534 534 534 LYS LYS A . n 
A 1 535 PHE 535 535 535 PHE PHE A . n 
A 1 536 ALA 536 536 536 ALA ALA A . n 
A 1 537 ALA 537 537 537 ALA ALA A . n 
A 1 538 HIS 538 538 538 HIS HIS A . n 
A 1 539 TRP 539 539 539 TRP TRP A . n 
A 1 540 LEU 540 540 540 LEU LEU A . n 
A 1 541 GLY 541 541 541 GLY GLY A . n 
A 1 542 ASP 542 542 542 ASP ASP A . n 
A 1 543 ASN 543 543 543 ASN ASN A . n 
A 1 544 THR 544 544 544 THR THR A . n 
A 1 545 ALA 545 545 545 ALA ALA A . n 
A 1 546 THR 546 546 546 THR THR A . n 
A 1 547 TRP 547 547 547 TRP TRP A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 ASP 549 549 549 ASP ASP A . n 
A 1 550 LEU 550 550 550 LEU LEU A . n 
A 1 551 ARG 551 551 551 ARG ARG A . n 
A 1 552 TRP 552 552 552 TRP TRP A . n 
A 1 553 SER 553 553 553 SER SER A . n 
A 1 554 ILE 554 554 554 ILE ILE A . n 
A 1 555 PRO 555 555 555 PRO PRO A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 VAL 557 557 557 VAL VAL A . n 
A 1 558 LEU 558 558 558 LEU LEU A . n 
A 1 559 GLU 559 559 559 GLU GLU A . n 
A 1 560 PHE 560 560 560 PHE PHE A . n 
A 1 561 ASN 561 561 561 ASN ASN A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 PHE 563 563 563 PHE PHE A . n 
A 1 564 GLY 564 564 564 GLY GLY A . n 
A 1 565 ILE 565 565 565 ILE ILE A . n 
A 1 566 PRO 566 566 566 PRO PRO A . n 
A 1 567 MET 567 567 567 MET MET A . n 
A 1 568 VAL 568 568 568 VAL VAL A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 PRO 570 570 570 PRO PRO A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 ILE 572 572 572 ILE ILE A . n 
A 1 573 CYS 573 573 573 CYS CYS A . n 
A 1 574 GLY 574 574 574 GLY GLY A . n 
A 1 575 PHE 575 575 575 PHE PHE A . n 
A 1 576 ALA 576 576 576 ALA ALA A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 ASP 578 578 578 ASP ASP A . n 
A 1 579 THR 579 579 579 THR THR A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 GLU 581 581 581 GLU GLU A . n 
A 1 582 GLU 582 582 582 GLU GLU A . n 
A 1 583 LEU 583 583 583 LEU LEU A . n 
A 1 584 CYS 584 584 584 CYS CYS A . n 
A 1 585 ARG 585 585 585 ARG ARG A . n 
A 1 586 ARG 586 586 586 ARG ARG A . n 
A 1 587 TRP 587 587 587 TRP TRP A . n 
A 1 588 MET 588 588 588 MET MET A . n 
A 1 589 GLN 589 589 589 GLN GLN A . n 
A 1 590 LEU 590 590 590 LEU LEU A . n 
A 1 591 GLY 591 591 591 GLY GLY A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 PHE 593 593 593 PHE PHE A . n 
A 1 594 TYR 594 594 594 TYR TYR A . n 
A 1 595 PRO 595 595 595 PRO PRO A . n 
A 1 596 PHE 596 596 596 PHE PHE A . n 
A 1 597 SER 597 597 597 SER SER A . n 
A 1 598 ARG 598 598 598 ARG ARG A . n 
A 1 599 ASN 599 599 599 ASN ASN A . n 
A 1 600 HIS 600 600 600 HIS HIS A . n 
A 1 601 ASN 601 601 601 ASN ASN A . n 
A 1 602 GLY 602 602 602 GLY GLY A . n 
A 1 603 GLN 603 603 603 GLN GLN A . n 
A 1 604 GLY 604 604 604 GLY GLY A . n 
A 1 605 TYR 605 605 605 TYR TYR A . n 
A 1 606 LYS 606 606 606 LYS LYS A . n 
A 1 607 ASP 607 607 607 ASP ASP A . n 
A 1 608 GLN 608 608 608 GLN GLN A . n 
A 1 609 ASP 609 609 609 ASP ASP A . n 
A 1 610 PRO 610 610 610 PRO PRO A . n 
A 1 611 ALA 611 611 611 ALA ALA A . n 
A 1 612 SER 612 612 612 SER SER A . n 
A 1 613 PHE 613 613 613 PHE PHE A . n 
A 1 614 GLY 614 614 614 GLY GLY A . n 
A 1 615 ALA 615 615 615 ALA ALA A . n 
A 1 616 ASP 616 616 616 ASP ASP A . n 
A 1 617 SER 617 617 617 SER SER A . n 
A 1 618 LEU 618 618 618 LEU LEU A . n 
A 1 619 LEU 619 619 619 LEU LEU A . n 
A 1 620 LEU 620 620 620 LEU LEU A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 SER 622 622 622 SER SER A . n 
A 1 623 SER 623 623 623 SER SER A . n 
A 1 624 ARG 624 624 624 ARG ARG A . n 
A 1 625 HIS 625 625 625 HIS HIS A . n 
A 1 626 TYR 626 626 626 TYR TYR A . n 
A 1 627 LEU 627 627 627 LEU LEU A . n 
A 1 628 ASN 628 628 628 ASN ASN A . n 
A 1 629 ILE 629 629 629 ILE ILE A . n 
A 1 630 ARG 630 630 630 ARG ARG A . n 
A 1 631 TYR 631 631 631 TYR TYR A . n 
A 1 632 THR 632 632 632 THR THR A . n 
A 1 633 LEU 633 633 633 LEU LEU A . n 
A 1 634 LEU 634 634 634 LEU LEU A . n 
A 1 635 PRO 635 635 635 PRO PRO A . n 
A 1 636 TYR 636 636 636 TYR TYR A . n 
A 1 637 LEU 637 637 637 LEU LEU A . n 
A 1 638 TYR 638 638 638 TYR TYR A . n 
A 1 639 THR 639 639 639 THR THR A . n 
A 1 640 LEU 640 640 640 LEU LEU A . n 
A 1 641 PHE 641 641 641 PHE PHE A . n 
A 1 642 PHE 642 642 642 PHE PHE A . n 
A 1 643 ARG 643 643 643 ARG ARG A . n 
A 1 644 ALA 644 644 644 ALA ALA A . n 
A 1 645 HIS 645 645 645 HIS HIS A . n 
A 1 646 SER 646 646 646 SER SER A . n 
A 1 647 ARG 647 647 647 ARG ARG A . n 
A 1 648 GLY 648 648 648 GLY GLY A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 THR 650 650 650 THR THR A . n 
A 1 651 VAL 651 651 651 VAL VAL A . n 
A 1 652 ALA 652 652 652 ALA ALA A . n 
A 1 653 ARG 653 653 653 ARG ARG A . n 
A 1 654 PRO 654 654 654 PRO PRO A . n 
A 1 655 LEU 655 655 655 LEU LEU A . n 
A 1 656 LEU 656 656 656 LEU LEU A . n 
A 1 657 HIS 657 657 657 HIS HIS A . n 
A 1 658 GLU 658 658 658 GLU GLU A . n 
A 1 659 PHE 659 659 659 PHE PHE A . n 
A 1 660 TYR 660 660 660 TYR TYR A . n 
A 1 661 GLU 661 661 661 GLU GLU A . n 
A 1 662 ASP 662 662 662 ASP ASP A . n 
A 1 663 ASN 663 663 663 ASN ASN A . n 
A 1 664 SER 664 664 664 SER SER A . n 
A 1 665 THR 665 665 665 THR THR A . n 
A 1 666 TRP 666 666 666 TRP TRP A . n 
A 1 667 ASP 667 667 667 ASP ASP A . n 
A 1 668 VAL 668 668 668 VAL VAL A . n 
A 1 669 HIS 669 669 669 HIS HIS A . n 
A 1 670 GLN 670 670 670 GLN GLN A . n 
A 1 671 GLN 671 671 671 GLN GLN A . n 
A 1 672 PHE 672 672 672 PHE PHE A . n 
A 1 673 LEU 673 673 673 LEU LEU A . n 
A 1 674 TRP 674 674 674 TRP TRP A . n 
A 1 675 GLY 675 675 675 GLY GLY A . n 
A 1 676 PRO 676 676 676 PRO PRO A . n 
A 1 677 GLY 677 677 677 GLY GLY A . n 
A 1 678 LEU 678 678 678 LEU LEU A . n 
A 1 679 LEU 679 679 679 LEU LEU A . n 
A 1 680 ILE 680 680 680 ILE ILE A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 PRO 682 682 682 PRO PRO A . n 
A 1 683 VAL 683 683 683 VAL VAL A . n 
A 1 684 LEU 684 684 684 LEU LEU A . n 
A 1 685 ASP 685 685 685 ASP ASP A . n 
A 1 686 GLU 686 686 686 GLU GLU A . n 
A 1 687 GLY 687 687 687 GLY GLY A . n 
A 1 688 ALA 688 688 688 ALA ALA A . n 
A 1 689 GLU 689 689 689 GLU GLU A . n 
A 1 690 LYS 690 690 690 LYS LYS A . n 
A 1 691 VAL 691 691 691 VAL VAL A . n 
A 1 692 MET 692 692 692 MET MET A . n 
A 1 693 ALA 693 693 693 ALA ALA A . n 
A 1 694 TYR 694 694 694 TYR TYR A . n 
A 1 695 VAL 695 695 695 VAL VAL A . n 
A 1 696 PRO 696 696 696 PRO PRO A . n 
A 1 697 ASP 697 697 697 ASP ASP A . n 
A 1 698 ALA 698 698 698 ALA ALA A . n 
A 1 699 VAL 699 699 699 VAL VAL A . n 
A 1 700 TRP 700 700 700 TRP TRP A . n 
A 1 701 TYR 701 701 701 TYR TYR A . n 
A 1 702 ASP 702 702 702 ASP ASP A . n 
A 1 703 TYR 703 703 703 TYR TYR A . n 
A 1 704 GLU 704 704 704 GLU GLU A . n 
A 1 705 THR 705 705 705 THR THR A . n 
A 1 706 GLY 706 706 706 GLY GLY A . n 
A 1 707 SER 707 707 707 SER SER A . n 
A 1 708 GLN 708 708 708 GLN GLN A . n 
A 1 709 VAL 709 709 709 VAL VAL A . n 
A 1 710 ARG 710 710 710 ARG ARG A . n 
A 1 711 TRP 711 711 711 TRP TRP A . n 
A 1 712 ARG 712 712 712 ARG ARG A . n 
A 1 713 LYS 713 713 713 LYS LYS A . n 
A 1 714 GLN 714 714 714 GLN GLN A . n 
A 1 715 LYS 715 715 715 LYS LYS A . n 
A 1 716 VAL 716 716 716 VAL VAL A . n 
A 1 717 GLU 717 717 717 GLU GLU A . n 
A 1 718 MET 718 718 718 MET MET A . n 
A 1 719 GLU 719 719 719 GLU GLU A . n 
A 1 720 LEU 720 720 720 LEU LEU A . n 
A 1 721 PRO 721 721 721 PRO PRO A . n 
A 1 722 GLY 722 722 722 GLY GLY A . n 
A 1 723 ASP 723 723 723 ASP ASP A . n 
A 1 724 LYS 724 724 724 LYS LYS A . n 
A 1 725 ILE 725 725 725 ILE ILE A . n 
A 1 726 GLY 726 726 726 GLY GLY A . n 
A 1 727 LEU 727 727 727 LEU LEU A . n 
A 1 728 HIS 728 728 728 HIS HIS A . n 
A 1 729 LEU 729 729 729 LEU LEU A . n 
A 1 730 ARG 730 730 730 ARG ARG A . n 
A 1 731 GLY 731 731 731 GLY GLY A . n 
A 1 732 GLY 732 732 732 GLY GLY A . n 
A 1 733 TYR 733 733 733 TYR TYR A . n 
A 1 734 ILE 734 734 734 ILE ILE A . n 
A 1 735 PHE 735 735 735 PHE PHE A . n 
A 1 736 PRO 736 736 736 PRO PRO A . n 
A 1 737 THR 737 737 737 THR THR A . n 
A 1 738 GLN 738 738 738 GLN GLN A . n 
A 1 739 GLN 739 739 739 GLN GLN A . n 
A 1 740 PRO 740 740 740 PRO PRO A . n 
A 1 741 ASN 741 741 741 ASN ASN A . n 
A 1 742 THR 742 742 742 THR THR A . n 
A 1 743 THR 743 743 743 THR THR A . n 
A 1 744 THR 744 744 744 THR THR A . n 
A 1 745 LEU 745 745 745 LEU LEU A . n 
A 1 746 ALA 746 746 746 ALA ALA A . n 
A 1 747 SER 747 747 747 SER SER A . n 
A 1 748 ARG 748 748 748 ARG ARG A . n 
A 1 749 LYS 749 749 749 LYS LYS A . n 
A 1 750 ASN 750 750 750 ASN ASN A . n 
A 1 751 PRO 751 751 751 PRO PRO A . n 
A 1 752 LEU 752 752 752 LEU LEU A . n 
A 1 753 GLY 753 753 753 GLY GLY A . n 
A 1 754 LEU 754 754 754 LEU LEU A . n 
A 1 755 ILE 755 755 755 ILE ILE A . n 
A 1 756 ILE 756 756 756 ILE ILE A . n 
A 1 757 ALA 757 757 757 ALA ALA A . n 
A 1 758 LEU 758 758 758 LEU LEU A . n 
A 1 759 ASP 759 759 759 ASP ASP A . n 
A 1 760 GLU 760 760 760 GLU GLU A . n 
A 1 761 ASN 761 761 761 ASN ASN A . n 
A 1 762 LYS 762 762 762 LYS LYS A . n 
A 1 763 GLU 763 763 763 GLU GLU A . n 
A 1 764 ALA 764 764 764 ALA ALA A . n 
A 1 765 LYS 765 765 765 LYS LYS A . n 
A 1 766 GLY 766 766 766 GLY GLY A . n 
A 1 767 GLU 767 767 767 GLU GLU A . n 
A 1 768 LEU 768 768 768 LEU LEU A . n 
A 1 769 PHE 769 769 769 PHE PHE A . n 
A 1 770 TRP 770 770 770 TRP TRP A . n 
A 1 771 ASP 771 771 771 ASP ASP A . n 
A 1 772 ASP 772 772 772 ASP ASP A . n 
A 1 773 GLY 773 773 773 GLY GLY A . n 
A 1 774 GLU 774 774 774 GLU GLU A . n 
A 1 775 THR 775 775 775 THR THR A . n 
A 1 776 LYS 776 776 776 LYS LYS A . n 
A 1 777 ASP 777 777 777 ASP ASP A . n 
A 1 778 THR 778 778 778 THR THR A . n 
A 1 779 VAL 779 779 779 VAL VAL A . n 
A 1 780 ALA 780 780 780 ALA ALA A . n 
A 1 781 ASN 781 781 781 ASN ASN A . n 
A 1 782 LYS 782 782 782 LYS LYS A . n 
A 1 783 VAL 783 783 783 VAL VAL A . n 
A 1 784 TYR 784 784 784 TYR TYR A . n 
A 1 785 LEU 785 785 785 LEU LEU A . n 
A 1 786 LEU 786 786 786 LEU LEU A . n 
A 1 787 CYS 787 787 787 CYS CYS A . n 
A 1 788 GLU 788 788 788 GLU GLU A . n 
A 1 789 PHE 789 789 789 PHE PHE A . n 
A 1 790 SER 790 790 790 SER SER A . n 
A 1 791 VAL 791 791 791 VAL VAL A . n 
A 1 792 THR 792 792 792 THR THR A . n 
A 1 793 GLN 793 793 793 GLN GLN A . n 
A 1 794 ASN 794 794 794 ASN ASN A . n 
A 1 795 ARG 795 795 795 ARG ARG A . n 
A 1 796 LEU 796 796 796 LEU LEU A . n 
A 1 797 GLU 797 797 797 GLU GLU A . n 
A 1 798 VAL 798 798 798 VAL VAL A . n 
A 1 799 ASN 799 799 799 ASN ASN A . n 
A 1 800 ILE 800 800 800 ILE ILE A . n 
A 1 801 SER 801 801 801 SER SER A . n 
A 1 802 GLN 802 802 802 GLN GLN A . n 
A 1 803 SER 803 803 803 SER SER A . n 
A 1 804 THR 804 804 804 THR THR A . n 
A 1 805 TYR 805 805 805 TYR TYR A . n 
A 1 806 LYS 806 806 806 LYS LYS A . n 
A 1 807 ASP 807 807 807 ASP ASP A . n 
A 1 808 PRO 808 808 808 PRO PRO A . n 
A 1 809 ASN 809 809 809 ASN ASN A . n 
A 1 810 ASN 810 810 810 ASN ASN A . n 
A 1 811 LEU 811 811 811 LEU LEU A . n 
A 1 812 ALA 812 812 812 ALA ALA A . n 
A 1 813 PHE 813 813 813 PHE PHE A . n 
A 1 814 ASN 814 814 814 ASN ASN A . n 
A 1 815 GLU 815 815 815 GLU GLU A . n 
A 1 816 ILE 816 816 816 ILE ILE A . n 
A 1 817 LYS 817 817 817 LYS LYS A . n 
A 1 818 ILE 818 818 818 ILE ILE A . n 
A 1 819 LEU 819 819 819 LEU LEU A . n 
A 1 820 GLY 820 820 820 GLY GLY A . n 
A 1 821 THR 821 821 821 THR THR A . n 
A 1 822 GLU 822 822 822 GLU GLU A . n 
A 1 823 GLU 823 823 823 GLU GLU A . n 
A 1 824 PRO 824 824 824 PRO PRO A . n 
A 1 825 SER 825 825 825 SER SER A . n 
A 1 826 ASN 826 826 826 ASN ASN A . n 
A 1 827 VAL 827 827 827 VAL VAL A . n 
A 1 828 THR 828 828 828 THR THR A . n 
A 1 829 VAL 829 829 829 VAL VAL A . n 
A 1 830 LYS 830 830 830 LYS LYS A . n 
A 1 831 HIS 831 831 831 HIS HIS A . n 
A 1 832 ASN 832 832 832 ASN ASN A . n 
A 1 833 GLY 833 833 833 GLY GLY A . n 
A 1 834 VAL 834 834 834 VAL VAL A . n 
A 1 835 PRO 835 835 835 PRO PRO A . n 
A 1 836 SER 836 836 836 SER SER A . n 
A 1 837 GLN 837 837 ?   ?   ?   A . n 
A 1 838 THR 838 838 ?   ?   ?   A . n 
A 1 839 SER 839 839 839 SER SER A . n 
A 1 840 PRO 840 840 840 PRO PRO A . n 
A 1 841 THR 841 841 841 THR THR A . n 
A 1 842 VAL 842 842 842 VAL VAL A . n 
A 1 843 THR 843 843 843 THR THR A . n 
A 1 844 TYR 844 844 844 TYR TYR A . n 
A 1 845 ASP 845 845 845 ASP ASP A . n 
A 1 846 SER 846 846 846 SER SER A . n 
A 1 847 ASN 847 847 847 ASN ASN A . n 
A 1 848 LEU 848 848 848 LEU LEU A . n 
A 1 849 LYS 849 849 849 LYS LYS A . n 
A 1 850 VAL 850 850 850 VAL VAL A . n 
A 1 851 ALA 851 851 851 ALA ALA A . n 
A 1 852 ILE 852 852 852 ILE ILE A . n 
A 1 853 ILE 853 853 853 ILE ILE A . n 
A 1 854 THR 854 854 854 THR THR A . n 
A 1 855 ASP 855 855 855 ASP ASP A . n 
A 1 856 ILE 856 856 856 ILE ILE A . n 
A 1 857 ASP 857 857 857 ASP ASP 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 LEU 860 860 860 LEU LEU A . n 
A 1 861 GLY 861 861 861 GLY GLY A . n 
A 1 862 GLU 862 862 862 GLU GLU A . n 
A 1 863 ALA 863 863 863 ALA ALA A . n 
A 1 864 TYR 864 864 864 TYR TYR A . n 
A 1 865 THR 865 865 865 THR THR A . n 
A 1 866 VAL 866 866 866 VAL VAL A . n 
A 1 867 GLU 867 867 867 GLU GLU A . n 
A 1 868 TRP 868 868 868 TRP TRP A . n 
A 1 869 ALA 869 869 869 ALA ALA A . n 
A 1 870 HIS 870 870 870 HIS HIS A . 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 
B 2 NAG 1   2001 2001 NAG NAG A . 
C 2 NAG 1   2002 2002 NAG NAG A . 
D 3 SO4 1   4001 4001 SO4 SO4 A . 
E 4 3CU 1   1001 1001 3CU 3CU A . 
F 5 GOL 1   3001 3001 GOL GOL A . 
G 5 GOL 1   3002 3002 GOL GOL A . 
H 5 GOL 1   3003 3003 GOL GOL A . 
I 5 GOL 1   3004 3004 GOL GOL A . 
J 5 GOL 1   3005 3005 GOL GOL A . 
K 5 GOL 1   3006 3006 GOL GOL A . 
L 5 GOL 1   3007 3007 GOL GOL A . 
M 5 GOL 1   3008 3008 GOL GOL A . 
N 5 GOL 1   3009 3009 GOL GOL A . 
O 6 HOH 1   4002 1    HOH HOH A . 
O 6 HOH 2   4003 2    HOH HOH A . 
O 6 HOH 3   4004 3    HOH HOH A . 
O 6 HOH 4   4005 4    HOH HOH A . 
O 6 HOH 5   4006 5    HOH HOH A . 
O 6 HOH 6   4007 6    HOH HOH A . 
O 6 HOH 7   4008 7    HOH HOH A . 
O 6 HOH 8   4009 8    HOH HOH A . 
O 6 HOH 9   4010 9    HOH HOH A . 
O 6 HOH 10  4011 10   HOH HOH A . 
O 6 HOH 11  4012 11   HOH HOH A . 
O 6 HOH 12  4013 12   HOH HOH A . 
O 6 HOH 13  4014 13   HOH HOH A . 
O 6 HOH 14  4015 14   HOH HOH A . 
O 6 HOH 15  4016 15   HOH HOH A . 
O 6 HOH 16  4017 16   HOH HOH A . 
O 6 HOH 17  4018 17   HOH HOH A . 
O 6 HOH 18  4019 18   HOH HOH A . 
O 6 HOH 19  4020 19   HOH HOH A . 
O 6 HOH 20  4021 20   HOH HOH A . 
O 6 HOH 21  4022 21   HOH HOH A . 
O 6 HOH 22  4023 22   HOH HOH A . 
O 6 HOH 23  4024 23   HOH HOH A . 
O 6 HOH 24  4025 24   HOH HOH A . 
O 6 HOH 25  4026 25   HOH HOH A . 
O 6 HOH 26  4027 26   HOH HOH A . 
O 6 HOH 27  4028 27   HOH HOH A . 
O 6 HOH 28  4029 28   HOH HOH A . 
O 6 HOH 29  4030 29   HOH HOH A . 
O 6 HOH 30  4031 30   HOH HOH A . 
O 6 HOH 31  4032 31   HOH HOH A . 
O 6 HOH 32  4033 32   HOH HOH A . 
O 6 HOH 33  4034 33   HOH HOH A . 
O 6 HOH 34  4035 34   HOH HOH A . 
O 6 HOH 35  4036 35   HOH HOH A . 
O 6 HOH 36  4037 36   HOH HOH A . 
O 6 HOH 37  4038 37   HOH HOH A . 
O 6 HOH 38  4039 38   HOH HOH A . 
O 6 HOH 39  4040 39   HOH HOH A . 
O 6 HOH 40  4041 40   HOH HOH A . 
O 6 HOH 41  4042 41   HOH HOH A . 
O 6 HOH 42  4043 42   HOH HOH A . 
O 6 HOH 43  4044 43   HOH HOH A . 
O 6 HOH 44  4045 44   HOH HOH A . 
O 6 HOH 45  4046 45   HOH HOH A . 
O 6 HOH 46  4047 46   HOH HOH A . 
O 6 HOH 47  4048 47   HOH HOH A . 
O 6 HOH 48  4049 48   HOH HOH A . 
O 6 HOH 49  4050 49   HOH HOH A . 
O 6 HOH 50  4051 50   HOH HOH A . 
O 6 HOH 51  4052 51   HOH HOH A . 
O 6 HOH 52  4053 52   HOH HOH A . 
O 6 HOH 53  4054 53   HOH HOH A . 
O 6 HOH 54  4055 54   HOH HOH A . 
O 6 HOH 55  4056 55   HOH HOH A . 
O 6 HOH 56  4057 56   HOH HOH A . 
O 6 HOH 57  4058 57   HOH HOH A . 
O 6 HOH 58  4059 58   HOH HOH A . 
O 6 HOH 59  4060 59   HOH HOH A . 
O 6 HOH 60  4061 60   HOH HOH A . 
O 6 HOH 61  4062 61   HOH HOH A . 
O 6 HOH 62  4063 62   HOH HOH A . 
O 6 HOH 63  4064 63   HOH HOH A . 
O 6 HOH 64  4065 64   HOH HOH A . 
O 6 HOH 65  4066 65   HOH HOH A . 
O 6 HOH 66  4067 66   HOH HOH A . 
O 6 HOH 67  4068 67   HOH HOH A . 
O 6 HOH 68  4069 68   HOH HOH A . 
O 6 HOH 69  4070 69   HOH HOH A . 
O 6 HOH 70  4071 70   HOH HOH A . 
O 6 HOH 71  4072 71   HOH HOH A . 
O 6 HOH 72  4073 72   HOH HOH A . 
O 6 HOH 73  4074 73   HOH HOH A . 
O 6 HOH 74  4075 74   HOH HOH A . 
O 6 HOH 75  4076 75   HOH HOH A . 
O 6 HOH 76  4077 76   HOH HOH A . 
O 6 HOH 77  4078 77   HOH HOH A . 
O 6 HOH 78  4079 78   HOH HOH A . 
O 6 HOH 79  4080 79   HOH HOH A . 
O 6 HOH 80  4081 80   HOH HOH A . 
O 6 HOH 81  4082 81   HOH HOH A . 
O 6 HOH 82  4083 82   HOH HOH A . 
O 6 HOH 83  4084 83   HOH HOH A . 
O 6 HOH 84  4085 84   HOH HOH A . 
O 6 HOH 85  4086 85   HOH HOH A . 
O 6 HOH 86  4087 86   HOH HOH A . 
O 6 HOH 87  4088 87   HOH HOH A . 
O 6 HOH 88  4089 88   HOH HOH A . 
O 6 HOH 89  4090 89   HOH HOH A . 
O 6 HOH 90  4091 90   HOH HOH A . 
O 6 HOH 91  4092 91   HOH HOH A . 
O 6 HOH 92  4093 92   HOH HOH A . 
O 6 HOH 93  4094 93   HOH HOH A . 
O 6 HOH 94  4095 94   HOH HOH A . 
O 6 HOH 95  4096 95   HOH HOH A . 
O 6 HOH 96  4097 96   HOH HOH A . 
O 6 HOH 97  4098 97   HOH HOH A . 
O 6 HOH 98  4099 98   HOH HOH A . 
O 6 HOH 99  4100 99   HOH HOH A . 
O 6 HOH 100 4101 100  HOH HOH A . 
O 6 HOH 101 4102 101  HOH HOH A . 
O 6 HOH 102 4103 102  HOH HOH A . 
O 6 HOH 103 4104 103  HOH HOH A . 
O 6 HOH 104 4105 104  HOH HOH A . 
O 6 HOH 105 4106 105  HOH HOH A . 
O 6 HOH 106 4107 106  HOH HOH A . 
O 6 HOH 107 4108 107  HOH HOH A . 
O 6 HOH 108 4109 108  HOH HOH A . 
O 6 HOH 109 4110 109  HOH HOH A . 
O 6 HOH 110 4111 110  HOH HOH A . 
O 6 HOH 111 4112 111  HOH HOH A . 
O 6 HOH 112 4113 112  HOH HOH A . 
O 6 HOH 113 4114 113  HOH HOH A . 
O 6 HOH 114 4115 114  HOH HOH A . 
O 6 HOH 115 4116 115  HOH HOH A . 
O 6 HOH 116 4117 116  HOH HOH A . 
O 6 HOH 117 4118 117  HOH HOH A . 
O 6 HOH 118 4119 118  HOH HOH A . 
O 6 HOH 119 4120 119  HOH HOH A . 
O 6 HOH 120 4121 120  HOH HOH A . 
O 6 HOH 121 4122 121  HOH HOH A . 
O 6 HOH 122 4123 122  HOH HOH A . 
O 6 HOH 123 4124 123  HOH HOH A . 
O 6 HOH 124 4125 124  HOH HOH A . 
O 6 HOH 125 4126 125  HOH HOH A . 
O 6 HOH 126 4127 126  HOH HOH A . 
O 6 HOH 127 4128 127  HOH HOH A . 
O 6 HOH 128 4129 128  HOH HOH A . 
O 6 HOH 129 4130 129  HOH HOH A . 
O 6 HOH 130 4131 130  HOH HOH A . 
O 6 HOH 131 4132 131  HOH HOH A . 
O 6 HOH 132 4133 132  HOH HOH A . 
O 6 HOH 133 4134 133  HOH HOH A . 
O 6 HOH 134 4135 134  HOH HOH A . 
O 6 HOH 135 4136 135  HOH HOH A . 
O 6 HOH 136 4137 136  HOH HOH A . 
O 6 HOH 137 4138 137  HOH HOH A . 
O 6 HOH 138 4139 138  HOH HOH A . 
O 6 HOH 139 4140 139  HOH HOH A . 
O 6 HOH 140 4141 140  HOH HOH A . 
O 6 HOH 141 4142 141  HOH HOH A . 
O 6 HOH 142 4143 142  HOH HOH A . 
O 6 HOH 143 4144 143  HOH HOH A . 
O 6 HOH 144 4145 144  HOH HOH A . 
O 6 HOH 145 4146 145  HOH HOH A . 
O 6 HOH 146 4147 146  HOH HOH A . 
O 6 HOH 147 4148 147  HOH HOH A . 
O 6 HOH 148 4149 148  HOH HOH A . 
O 6 HOH 149 4150 149  HOH HOH A . 
O 6 HOH 150 4151 150  HOH HOH A . 
O 6 HOH 151 4152 151  HOH HOH A . 
O 6 HOH 152 4153 152  HOH HOH A . 
O 6 HOH 153 4154 153  HOH HOH A . 
O 6 HOH 154 4155 154  HOH HOH A . 
O 6 HOH 155 4156 155  HOH HOH A . 
O 6 HOH 156 4157 156  HOH HOH A . 
O 6 HOH 157 4158 157  HOH HOH A . 
O 6 HOH 158 4159 158  HOH HOH A . 
O 6 HOH 159 4160 159  HOH HOH A . 
O 6 HOH 160 4161 160  HOH HOH A . 
O 6 HOH 161 4162 161  HOH HOH A . 
O 6 HOH 162 4163 162  HOH HOH A . 
O 6 HOH 163 4164 163  HOH HOH A . 
O 6 HOH 164 4165 164  HOH HOH A . 
O 6 HOH 165 4166 165  HOH HOH A . 
O 6 HOH 166 4167 166  HOH HOH A . 
O 6 HOH 167 4168 167  HOH HOH A . 
O 6 HOH 168 4169 168  HOH HOH A . 
O 6 HOH 169 4170 169  HOH HOH A . 
O 6 HOH 170 4171 170  HOH HOH A . 
O 6 HOH 171 4172 171  HOH HOH A . 
O 6 HOH 172 4173 172  HOH HOH A . 
O 6 HOH 173 4174 173  HOH HOH A . 
O 6 HOH 174 4175 174  HOH HOH A . 
O 6 HOH 175 4176 175  HOH HOH A . 
O 6 HOH 176 4177 176  HOH HOH A . 
O 6 HOH 177 4178 177  HOH HOH A . 
O 6 HOH 178 4179 178  HOH HOH A . 
O 6 HOH 179 4180 179  HOH HOH A . 
O 6 HOH 180 4181 180  HOH HOH A . 
O 6 HOH 181 4182 181  HOH HOH A . 
O 6 HOH 182 4183 182  HOH HOH A . 
O 6 HOH 183 4184 183  HOH HOH A . 
O 6 HOH 184 4185 184  HOH HOH A . 
O 6 HOH 185 4186 185  HOH HOH A . 
O 6 HOH 186 4187 186  HOH HOH A . 
O 6 HOH 187 4188 187  HOH HOH A . 
O 6 HOH 188 4189 188  HOH HOH A . 
O 6 HOH 189 4190 189  HOH HOH A . 
O 6 HOH 190 4191 190  HOH HOH A . 
O 6 HOH 191 4192 191  HOH HOH A . 
O 6 HOH 192 4193 192  HOH HOH A . 
O 6 HOH 193 4194 193  HOH HOH A . 
O 6 HOH 194 4195 194  HOH HOH A . 
O 6 HOH 195 4196 195  HOH HOH A . 
O 6 HOH 196 4197 196  HOH HOH A . 
O 6 HOH 197 4198 197  HOH HOH A . 
O 6 HOH 198 4199 198  HOH HOH A . 
O 6 HOH 199 4200 199  HOH HOH A . 
O 6 HOH 200 4201 200  HOH HOH A . 
O 6 HOH 201 4202 201  HOH HOH A . 
O 6 HOH 202 4203 202  HOH HOH A . 
O 6 HOH 203 4204 203  HOH HOH A . 
O 6 HOH 204 4205 204  HOH HOH A . 
O 6 HOH 205 4206 205  HOH HOH A . 
O 6 HOH 206 4207 206  HOH HOH A . 
O 6 HOH 207 4208 207  HOH HOH A . 
O 6 HOH 208 4209 208  HOH HOH A . 
O 6 HOH 209 4210 209  HOH HOH A . 
O 6 HOH 210 4211 210  HOH HOH A . 
O 6 HOH 211 4212 211  HOH HOH A . 
O 6 HOH 212 4213 212  HOH HOH A . 
O 6 HOH 213 4214 213  HOH HOH A . 
O 6 HOH 214 4215 214  HOH HOH A . 
O 6 HOH 215 4216 215  HOH HOH A . 
O 6 HOH 216 4217 216  HOH HOH A . 
O 6 HOH 217 4218 217  HOH HOH A . 
O 6 HOH 218 4219 218  HOH HOH A . 
O 6 HOH 219 4220 219  HOH HOH A . 
O 6 HOH 220 4221 220  HOH HOH A . 
O 6 HOH 221 4222 221  HOH HOH A . 
O 6 HOH 222 4223 222  HOH HOH A . 
O 6 HOH 223 4224 223  HOH HOH A . 
O 6 HOH 224 4225 224  HOH HOH A . 
O 6 HOH 225 4226 225  HOH HOH A . 
O 6 HOH 226 4227 226  HOH HOH A . 
O 6 HOH 227 4228 227  HOH HOH A . 
O 6 HOH 228 4229 228  HOH HOH A . 
O 6 HOH 229 4230 229  HOH HOH A . 
O 6 HOH 230 4231 230  HOH HOH A . 
O 6 HOH 231 4232 231  HOH HOH A . 
O 6 HOH 232 4233 232  HOH HOH A . 
O 6 HOH 233 4234 233  HOH HOH A . 
O 6 HOH 234 4235 234  HOH HOH A . 
O 6 HOH 235 4236 235  HOH HOH A . 
O 6 HOH 236 4237 236  HOH HOH A . 
O 6 HOH 237 4238 237  HOH HOH A . 
O 6 HOH 238 4239 238  HOH HOH A . 
O 6 HOH 239 4240 239  HOH HOH A . 
O 6 HOH 240 4241 240  HOH HOH A . 
O 6 HOH 241 4242 241  HOH HOH A . 
O 6 HOH 242 4243 242  HOH HOH A . 
O 6 HOH 243 4244 243  HOH HOH A . 
O 6 HOH 244 4245 244  HOH HOH A . 
O 6 HOH 245 4246 245  HOH HOH A . 
O 6 HOH 246 4247 246  HOH HOH A . 
O 6 HOH 247 4248 247  HOH HOH A . 
O 6 HOH 248 4249 248  HOH HOH A . 
O 6 HOH 249 4250 249  HOH HOH A . 
O 6 HOH 250 4251 250  HOH HOH A . 
O 6 HOH 251 4252 251  HOH HOH A . 
O 6 HOH 252 4253 252  HOH HOH A . 
O 6 HOH 253 4254 253  HOH HOH A . 
O 6 HOH 254 4255 254  HOH HOH A . 
O 6 HOH 255 4256 255  HOH HOH A . 
O 6 HOH 256 4257 256  HOH HOH A . 
O 6 HOH 257 4258 257  HOH HOH A . 
O 6 HOH 258 4259 258  HOH HOH A . 
O 6 HOH 259 4260 259  HOH HOH A . 
O 6 HOH 260 4261 260  HOH HOH A . 
O 6 HOH 261 4262 261  HOH HOH A . 
O 6 HOH 262 4263 262  HOH HOH A . 
O 6 HOH 263 4264 263  HOH HOH A . 
O 6 HOH 264 4265 264  HOH HOH A . 
O 6 HOH 265 4266 265  HOH HOH A . 
O 6 HOH 266 4267 266  HOH HOH A . 
O 6 HOH 267 4268 267  HOH HOH A . 
O 6 HOH 268 4269 268  HOH HOH A . 
O 6 HOH 269 4270 269  HOH HOH A . 
O 6 HOH 270 4271 270  HOH HOH A . 
O 6 HOH 271 4272 271  HOH HOH A . 
O 6 HOH 272 4273 272  HOH HOH A . 
O 6 HOH 273 4274 273  HOH HOH A . 
O 6 HOH 274 4275 274  HOH HOH A . 
O 6 HOH 275 4276 275  HOH HOH A . 
O 6 HOH 276 4277 276  HOH HOH A . 
O 6 HOH 277 4278 277  HOH HOH A . 
O 6 HOH 278 4279 278  HOH HOH A . 
O 6 HOH 279 4280 279  HOH HOH A . 
O 6 HOH 280 4281 280  HOH HOH A . 
O 6 HOH 281 4282 281  HOH HOH A . 
O 6 HOH 282 4283 282  HOH HOH A . 
O 6 HOH 283 4284 283  HOH HOH A . 
O 6 HOH 284 4285 284  HOH HOH A . 
O 6 HOH 285 4286 285  HOH HOH A . 
O 6 HOH 286 4287 286  HOH HOH A . 
O 6 HOH 287 4288 287  HOH HOH A . 
O 6 HOH 288 4289 288  HOH HOH A . 
O 6 HOH 289 4290 289  HOH HOH A . 
O 6 HOH 290 4291 290  HOH HOH A . 
O 6 HOH 291 4292 291  HOH HOH A . 
O 6 HOH 292 4293 292  HOH HOH A . 
O 6 HOH 293 4294 293  HOH HOH A . 
O 6 HOH 294 4295 294  HOH HOH A . 
O 6 HOH 295 4296 295  HOH HOH A . 
O 6 HOH 296 4297 296  HOH HOH A . 
O 6 HOH 297 4298 297  HOH HOH A . 
O 6 HOH 298 4299 298  HOH HOH A . 
O 6 HOH 299 4300 299  HOH HOH A . 
O 6 HOH 300 4301 300  HOH HOH A . 
O 6 HOH 301 4302 301  HOH HOH A . 
O 6 HOH 302 4303 302  HOH HOH A . 
O 6 HOH 303 4304 303  HOH HOH A . 
O 6 HOH 304 4305 304  HOH HOH A . 
O 6 HOH 305 4306 305  HOH HOH A . 
O 6 HOH 306 4307 306  HOH HOH A . 
O 6 HOH 307 4308 307  HOH HOH A . 
O 6 HOH 308 4309 308  HOH HOH A . 
O 6 HOH 309 4310 309  HOH HOH A . 
O 6 HOH 310 4311 310  HOH HOH A . 
O 6 HOH 311 4312 311  HOH HOH A . 
O 6 HOH 312 4313 312  HOH HOH A . 
O 6 HOH 313 4314 313  HOH HOH A . 
O 6 HOH 314 4315 314  HOH HOH A . 
O 6 HOH 315 4316 315  HOH HOH A . 
O 6 HOH 316 4317 316  HOH HOH A . 
O 6 HOH 317 4318 317  HOH HOH A . 
O 6 HOH 318 4319 318  HOH HOH A . 
O 6 HOH 319 4320 319  HOH HOH A . 
O 6 HOH 320 4321 320  HOH HOH A . 
O 6 HOH 321 4322 321  HOH HOH A . 
O 6 HOH 322 4323 322  HOH HOH A . 
O 6 HOH 323 4324 323  HOH HOH A . 
O 6 HOH 324 4325 324  HOH HOH A . 
O 6 HOH 325 4326 325  HOH HOH A . 
O 6 HOH 326 4327 326  HOH HOH A . 
O 6 HOH 327 4328 327  HOH HOH A . 
O 6 HOH 328 4329 328  HOH HOH A . 
O 6 HOH 329 4330 329  HOH HOH A . 
O 6 HOH 330 4331 330  HOH HOH A . 
O 6 HOH 331 4332 331  HOH HOH A . 
O 6 HOH 332 4333 332  HOH HOH A . 
O 6 HOH 333 4334 333  HOH HOH A . 
O 6 HOH 334 4335 334  HOH HOH A . 
O 6 HOH 335 4336 335  HOH HOH A . 
O 6 HOH 336 4337 336  HOH HOH A . 
O 6 HOH 337 4338 337  HOH HOH A . 
O 6 HOH 338 4339 338  HOH HOH A . 
O 6 HOH 339 4340 339  HOH HOH A . 
O 6 HOH 340 4341 340  HOH HOH A . 
O 6 HOH 341 4342 341  HOH HOH A . 
O 6 HOH 342 4343 342  HOH HOH A . 
O 6 HOH 343 4344 343  HOH HOH A . 
O 6 HOH 344 4345 344  HOH HOH A . 
O 6 HOH 345 4346 345  HOH HOH A . 
O 6 HOH 346 4347 346  HOH HOH A . 
O 6 HOH 347 4348 347  HOH HOH A . 
O 6 HOH 348 4349 348  HOH HOH A . 
O 6 HOH 349 4350 349  HOH HOH A . 
O 6 HOH 350 4351 350  HOH HOH A . 
O 6 HOH 351 4352 351  HOH HOH A . 
O 6 HOH 352 4353 352  HOH HOH A . 
# 
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 393 A ASN 393 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 741 A ASN 741 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_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_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 2009-02-24 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-10-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
_pdbx_phasing_MR.entry_id                     3CTT 
_pdbx_phasing_MR.method_rotation              ? 
_pdbx_phasing_MR.method_translation           ? 
_pdbx_phasing_MR.model_details                'Phaser MODE: MR_AUTO' 
_pdbx_phasing_MR.R_factor                     ? 
_pdbx_phasing_MR.R_rigid_body                 ? 
_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc   ? 
_pdbx_phasing_MR.correlation_coeff_Io_to_Ic   ? 
_pdbx_phasing_MR.d_res_high_rotation          2.500 
_pdbx_phasing_MR.d_res_low_rotation           15.660 
_pdbx_phasing_MR.d_res_high_translation       2.500 
_pdbx_phasing_MR.d_res_low_translation        15.660 
_pdbx_phasing_MR.packing                      ? 
_pdbx_phasing_MR.reflns_percent_rotation      ? 
_pdbx_phasing_MR.reflns_percent_translation   ? 
_pdbx_phasing_MR.sigma_F_rotation             ? 
_pdbx_phasing_MR.sigma_F_translation          ? 
_pdbx_phasing_MR.sigma_I_rotation             ? 
_pdbx_phasing_MR.sigma_I_translation          ? 
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
DENZO       .     ?                    package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu       'data reduction'  
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 1 
SCALEPACK   .     ?                    package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu       'data scaling'    
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 2 
PHASER      .     ?                    other   'R. J. Read'         cimr-phaser@lists.cam.ac.uk phasing           
http://www-structmed.cimr.cam.ac.uk/phaser/      ?          ? 3 
REFMAC      .     ?                    program 'Murshudov, G.N.'    ccp4@dl.ac.uk               refinement        
http://www.ccp4.ac.uk/main.html                  Fortran_77 ? 4 
PDB_EXTRACT 3.005 'September 10, 2007' package PDB                  sw-help@rcsb.rutgers.edu    'data extraction' 
http://pdb.rutgers.edu/software/                 C++        ? 5 
HKL-2000    .     ?                    ?       ?                    ?                           'data collection' ? ?          ? 6 
# 
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 OD2 A ASP 772  ? ? OG1 A THR 775  ? ? 2.15 
2 1 O   A HOH 4097 ? ? O   A HOH 4350 ? ? 2.16 
# 
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 34  ? ? -157.73 89.27   
2  1 SER A 40  ? ? 78.46   -14.36  
3  1 HIS A 50  ? ? 155.95  158.06  
4  1 SER A 51  ? ? 91.18   -136.42 
5  1 SER A 80  ? ? -56.52  99.75   
6  1 LEU A 151 ? ? -97.81  -61.02  
7  1 PHE A 161 ? ? -151.00 80.89   
8  1 LEU A 180 ? ? 65.30   146.58  
9  1 GLN A 186 ? ? 75.15   -46.57  
10 1 ASP A 191 ? ? -43.29  92.32   
11 1 TRP A 194 ? ? -55.11  107.42  
12 1 PRO A 206 ? ? -65.83  96.08   
13 1 LEU A 213 ? ? -118.68 -148.59 
14 1 GLU A 300 ? ? 71.81   69.58   
15 1 TYR A 321 ? ? -170.40 100.17  
16 1 VAL A 342 ? ? -106.01 -61.66  
17 1 LYS A 377 ? ? -154.95 68.34   
18 1 VAL A 405 ? ? -130.41 -148.15 
19 1 ASP A 474 ? ? 77.18   -23.61  
20 1 THR A 481 ? ? -150.88 -158.02 
21 1 ASN A 518 ? ? 57.51   13.14   
22 1 SER A 521 ? ? 58.70   -142.62 
23 1 ASN A 543 ? ? -74.59  -169.13 
24 1 ILE A 565 ? ? -118.30 71.75   
25 1 CYS A 573 ? ? 80.78   -11.20  
26 1 LEU A 577 ? ? 88.61   157.36  
27 1 VAL A 651 ? ? -107.17 -67.39  
28 1 GLU A 774 ? ? -154.05 -20.44  
29 1 ASP A 777 ? ? 83.93   8.85    
30 1 VAL A 783 ? ? -117.57 79.05   
31 1 GLN A 793 ? ? -10.17  126.39  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1   ? A SER 1   
2 1 Y 1 A ALA 2   ? A ALA 2   
3 1 Y 1 A GLU 3   ? A GLU 3   
4 1 Y 1 A CYS 4   ? A CYS 4   
5 1 Y 1 A PRO 5   ? A PRO 5   
6 1 Y 1 A VAL 6   ? A VAL 6   
7 1 Y 1 A GLN 837 ? A GLN 837 
8 1 Y 1 A THR 838 ? A THR 838 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'SULFATE ION'          SO4 
4 CASUARINE              3CU 
5 GLYCEROL               GOL 
6 water                  HOH 
# 
