data_3L4X
# 
_entry.id   3L4X 
# 
_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   3L4X         
RCSB  RCSB056837   
WWPDB D_1000056837 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3L4T . unspecified 
PDB 3L4U . unspecified 
PDB 3L4V . unspecified 
PDB 3L4W . unspecified 
PDB 3L4Y . unspecified 
PDB 3L4Z . unspecified 
# 
_pdbx_database_status.entry_id                        3L4X 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2009-12-21 
_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                     
;New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltase-glucoamylase with compounds from Salacia reticulata.
;
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            49 
_citation.page_first                443 
_citation.page_last                 451 
_citation.year                      2010 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20039683 
_citation.pdbx_database_id_DOI      10.1021/bi9016457 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Sim, L.'         1 
primary 'Jayakanthan, K.' 2 
primary 'Mohan, S.'       3 
primary 'Nasi, R.'        4 
primary 'Johnston, B.D.'  5 
primary 'Pinto, B.M.'     6 
primary 'Rose, D.R.'      7 
# 
_cell.length_a           87.173 
_cell.length_b           109.437 
_cell.length_c           109.327 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           3L4X 
_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                         3L4X 
_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, intestinal' 99276.742 1   '3.2.1.20, 3.2.1.3' ? 'UNP residues 87-954' ? 
2 non-polymer syn 
;(1S,2R,3S,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium-1-yl]-1-hydroxyethyl}-2,3,4,5-tetrahydroxypentyl sulfate
;
424.442   1   ?                   ? ?                     ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   3   ?                   ? ?                     ? 
4 non-polymer syn GLYCEROL 92.094    4   ?                   ? ?                     ? 
5 water       nat water 18.015    613 ?                   ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Maltase, Alpha-glucosidase, Glucoamylase, Glucan 1,4-alpha-glucosidase' 
# 
_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
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAHHHHHH
;
_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 
1 871 HIS n 
1 872 HIS n 
1 873 HIS n 
1 874 HIS n 
1 875 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                 'MGA, MGAM, 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     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_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
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNI
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              3L4X 
_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 3L4X ASP A 772 ? UNP O43451 ASN 858 VARIANT          772 1 
1 3L4X ALA A 869 ? UNP O43451 ?   ?   'EXPRESSION TAG' 869 2 
1 3L4X HIS A 870 ? UNP O43451 ?   ?   'EXPRESSION TAG' 870 3 
1 3L4X HIS A 871 ? UNP O43451 ?   ?   'EXPRESSION TAG' 871 4 
1 3L4X HIS A 872 ? UNP O43451 ?   ?   'EXPRESSION TAG' 872 5 
1 3L4X HIS A 873 ? UNP O43451 ?   ?   'EXPRESSION TAG' 873 6 
1 3L4X HIS A 874 ? UNP O43451 ?   ?   'EXPRESSION TAG' 874 7 
1 3L4X HIS A 875 ? UNP O43451 ?   ?   'EXPRESSION TAG' 875 8 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'     75.067  
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 
NR3 non-polymer         . 
;(1S,2R,3S,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium-1-yl]-1-hydroxyethyl}-2,3,4,5-tetrahydroxypentyl sulfate
;
?                               'C12 H24 O12 S2' 424.442 
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ?                               'C5 H11 N O2'    117.146 
# 
_exptl.crystals_number   1 
_exptl.entry_id          3L4X 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.63 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   53.17 
_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.pdbx_details    '20% PEG 3350, 0.2M sodium sulfate, pH 6.5, vapor diffusion, hanging drop, temperature 293K' 
_exptl_crystal_grow.temp_details    ? 
_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   2007-04-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_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_list        0.9175 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
# 
_reflns.entry_id                     3L4X 
_reflns.d_resolution_high            1.900 
_reflns.d_resolution_low             30.000 
_reflns.number_obs                   82586 
_reflns.pdbx_Rmerge_I_obs            0.112 
_reflns.pdbx_netI_over_sigmaI        15.800 
_reflns.pdbx_chi_squared             1.409 
_reflns.pdbx_redundancy              7.900 
_reflns.percent_possible_obs         99.600 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
1.90 1.97  ? ? ? 0.354 ? ? 2.181 8.10 ? 8206 100.00 ? 1  
1.97 2.05  ? ? ? 0.268 ? ? 1.889 8.10 ? 8183 100.00 ? 2  
2.05 2.14  ? ? ? 0.220 ? ? 1.610 8.10 ? 8226 100.00 ? 3  
2.14 2.25  ? ? ? 0.182 ? ? 1.503 8.10 ? 8195 100.00 ? 4  
2.25 2.39  ? ? ? 0.157 ? ? 1.270 8.10 ? 8240 100.00 ? 5  
2.39 2.58  ? ? ? 0.137 ? ? 1.220 8.10 ? 8251 100.00 ? 6  
2.58 2.84  ? ? ? 0.120 ? ? 1.187 8.10 ? 8264 100.00 ? 7  
2.84 3.25  ? ? ? 0.103 ? ? 1.186 8.00 ? 8307 99.90  ? 8  
3.25 4.09  ? ? ? 0.089 ? ? 0.978 7.80 ? 8296 99.00  ? 9  
4.09 30.00 ? ? ? 0.090 ? ? 0.988 6.80 ? 8418 96.70  ? 10 
# 
_refine.entry_id                                 3L4X 
_refine.ls_d_res_high                            1.900 
_refine.ls_d_res_low                             18.880 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.240 
_refine.ls_number_reflns_obs                     80580 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.207 
_refine.ls_R_factor_R_work                       0.205 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.244 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  4032 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               21.815 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.010 
_refine.aniso_B[2][2]                            0.000 
_refine.aniso_B[3][3]                            0.000 
_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               0.919 
_refine.correlation_coeff_Fo_to_Fc_free          0.892 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       0.163 
_refine.pdbx_overall_ESU_R_Free                  0.151 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                63.06 
_refine.B_iso_min                                6.65 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_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        6936 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         92 
_refine_hist.number_atoms_solvent             613 
_refine_hist.number_atoms_total               7641 
_refine_hist.d_res_high                       1.900 
_refine_hist.d_res_low                        18.880 
# 
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         7232 0.016  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      9869 1.633  1.946  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   869  6.709  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   365  35.528 24.247 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   1101 12.833 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   40   17.337 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           1063 0.120  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     5641 0.007  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            3516 0.208  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          4916 0.315  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    658  0.149  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   69   0.179  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 11   0.129  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              4316 0.969  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             7001 1.669  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              2916 2.592  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             2864 3.870  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.900 
_refine_ls_shell.d_res_low                        1.949 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               94.960 
_refine_ls_shell.number_reflns_R_work             5406 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.238 
_refine_ls_shell.R_factor_R_free                  0.345 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             304 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                5710 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3L4X 
_struct.title                     'Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8' 
_struct.pdbx_descriptor           'Maltase-glucoamylase, intestinal (E.C.3.2.1.20, 3.2.1.3)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3L4X 
_struct_keywords.text            
;Glycoside Hydrolase Family 31, Cell membrane, Disulfide bond, Glycoprotein, Glycosidase, Hydrolase, Membrane, Multifunctional enzyme, Polymorphism, Signal-anchor, Sulfation, Transmembrane
;
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  ? GLY A 30  ? THR A 22  GLY A 30  1 ? 9  
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 PRO A 654 ? TYR A 660 ? PRO A 654 TYR A 660 1 ? 7  
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 ? ? ? ? ? ? ? 2.031 ? 
disulf2 disulf ? ? A CYS 26  SG  ? ? ? 1_555 A CYS 44  SG ? ? A CYS 26   A CYS 44   1_555 ? ? ? ? ? ? ? 2.952 ? 
disulf3 disulf ? ? A CYS 573 SG  ? ? ? 1_555 A CYS 584 SG ? ? A CYS 573  A CYS 584  1_555 ? ? ? ? ? ? ? 2.078 ? 
covale1 covale ? ? A ASN 393 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 393  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale2 covale ? ? C NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? A NAG 2001 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale3 covale ? ? A ASN 741 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 741  A NAG 2003 1_555 ? ? ? ? ? ? ? 1.477 ? 
# 
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 4.84  
2 GLY 181 A . ? GLY 181 A GLU 182 A ? GLU 182 A 1 -2.58 
3 ALA 248 A . ? ALA 248 A PRO 249 A ? PRO 249 A 1 -1.15 
4 GLU 446 A . ? GLU 446 A VAL 447 A ? VAL 447 A 1 4.55  
5 PRO 835 A . ? PRO 835 A SER 836 A ? SER 836 A 1 17.68 
# 
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 ? 11 ? 
K ? 10 ? 
# 
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  ? anti-parallel 
J 6  7  ? parallel      
J 7  8  ? anti-parallel 
J 8  9  ? parallel      
J 9  10 ? anti-parallel 
J 10 11 ? 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  ? anti-parallel 
K 6  7  ? parallel      
K 7  8  ? anti-parallel 
K 8  9  ? parallel      
K 9  10 ? 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  VAL A 834 ? PRO A 835 ? VAL A 834 PRO A 835 
J 2  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
J 3  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
J 4  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
J 5  LEU A 785 ? VAL A 791 ? LEU A 785 VAL A 791 
J 6  ALA A 764 ? TRP A 770 ? ALA A 764 TRP A 770 
J 7  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
J 8  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
J 9  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
J 10 VAL A 850 ? THR A 854 ? VAL A 850 THR A 854 
J 11 THR A 841 ? ASP A 845 ? THR A 841 ASP A 845 
K 1  VAL A 834 ? PRO A 835 ? VAL A 834 PRO A 835 
K 2  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
K 3  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
K 4  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
K 5  LEU A 785 ? VAL A 791 ? LEU A 785 VAL A 791 
K 6  ALA A 764 ? TRP A 770 ? ALA A 764 TRP A 770 
K 7  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
K 8  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
K 9  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
K 10 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 HIS A 53  ? N HIS A 53  O LYS A 70  ? O LYS A 70  
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 TYR A 263 ? O TYR A 263 N PHE A 234 ? N PHE A 234 
B 6  7  O PHE A 231 ? O PHE A 231 N CYS A 222 ? N CYS A 222 
B 7  8  O LEU A 221 ? O LEU A 221 N TYR A 178 ? N TYR A 178 
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 ILE A 523 ? N ILE A 523 
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 LYS A 360 ? O LYS A 360 N GLN A 324 ? N GLN A 324 
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  O VAL A 834 ? O VAL A 834 N HIS A 831 ? N HIS A 831 
J 2  3  N SER A 825 ? N SER A 825 O ALA A 869 ? O ALA A 869 
J 3  4  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
J 4  5  O ASN A 799 ? O ASN A 799 N GLU A 788 ? N GLU A 788 
J 5  6  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
J 6  7  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
J 7  8  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
J 8  9  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
J 9  10 N ILE A 816 ? N ILE A 816 O ILE A 853 ? O ILE A 853 
J 10 11 O THR A 854 ? O THR A 854 N THR A 841 ? N THR A 841 
K 1  2  O VAL A 834 ? O VAL A 834 N HIS A 831 ? N HIS A 831 
K 2  3  N SER A 825 ? N SER A 825 O ALA A 869 ? O ALA A 869 
K 3  4  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
K 4  5  O ASN A 799 ? O ASN A 799 N GLU A 788 ? N GLU A 788 
K 5  6  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
K 6  7  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
K 7  8  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
K 8  9  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
K 9  10 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 ? ? ? ? 15 'BINDING SITE FOR RESIDUE NR3 A 1001' 
AC2 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG A 2001' 
AC3 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 2002' 
AC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 2003' 
AC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL A 3001' 
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3002' 
AC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3003' 
AC8 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL A 3004' 
# 
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 15 ASP A 203 ? ASP A 203  . ? 1_555 ? 
2  AC1 15 TYR A 299 ? TYR A 299  . ? 1_555 ? 
3  AC1 15 ASP A 327 ? ASP A 327  . ? 1_555 ? 
4  AC1 15 ILE A 364 ? ILE A 364  . ? 1_555 ? 
5  AC1 15 TRP A 441 ? TRP A 441  . ? 1_555 ? 
6  AC1 15 ASP A 443 ? ASP A 443  . ? 1_555 ? 
7  AC1 15 ARG A 526 ? ARG A 526  . ? 1_555 ? 
8  AC1 15 TRP A 539 ? TRP A 539  . ? 1_555 ? 
9  AC1 15 ASP A 542 ? ASP A 542  . ? 1_555 ? 
10 AC1 15 PHE A 575 ? PHE A 575  . ? 1_555 ? 
11 AC1 15 HIS A 600 ? HIS A 600  . ? 1_555 ? 
12 AC1 15 HOH J .   ? HOH A 4079 . ? 1_555 ? 
13 AC1 15 HOH J .   ? HOH A 4104 . ? 1_555 ? 
14 AC1 15 HOH J .   ? HOH A 4147 . ? 1_555 ? 
15 AC1 15 HOH J .   ? HOH A 4158 . ? 1_555 ? 
16 AC2 11 LYS A 389 ? LYS A 389  . ? 1_555 ? 
17 AC2 11 ASN A 393 ? ASN A 393  . ? 1_555 ? 
18 AC2 11 GLY A 397 ? GLY A 397  . ? 1_555 ? 
19 AC2 11 VAL A 398 ? VAL A 398  . ? 1_555 ? 
20 AC2 11 VAL A 487 ? VAL A 487  . ? 1_555 ? 
21 AC2 11 GLN A 488 ? GLN A 488  . ? 1_555 ? 
22 AC2 11 HIS A 489 ? HIS A 489  . ? 1_555 ? 
23 AC2 11 NAG D .   ? NAG A 2002 . ? 1_555 ? 
24 AC2 11 HOH J .   ? HOH A 4182 . ? 1_555 ? 
25 AC2 11 HOH J .   ? HOH A 4263 . ? 1_555 ? 
26 AC2 11 HOH J .   ? HOH A 4594 . ? 1_555 ? 
27 AC3 2  LYS A 389 ? LYS A 389  . ? 1_555 ? 
28 AC3 2  NAG C .   ? NAG A 2001 . ? 1_555 ? 
29 AC4 10 SER A 146 ? SER A 146  . ? 2_454 ? 
30 AC4 10 ASN A 147 ? ASN A 147  . ? 2_454 ? 
31 AC4 10 ASN A 741 ? ASN A 741  . ? 1_555 ? 
32 AC4 10 ALA A 746 ? ALA A 746  . ? 1_555 ? 
33 AC4 10 ASN A 750 ? ASN A 750  . ? 1_555 ? 
34 AC4 10 HOH J .   ? HOH A 4160 . ? 1_555 ? 
35 AC4 10 HOH J .   ? HOH A 4455 . ? 2_454 ? 
36 AC4 10 HOH J .   ? HOH A 4503 . ? 1_555 ? 
37 AC4 10 HOH J .   ? HOH A 4558 . ? 1_555 ? 
38 AC4 10 HOH J .   ? HOH A 4639 . ? 1_555 ? 
39 AC5 7  ALA A 285 ? ALA A 285  . ? 1_555 ? 
40 AC5 7  ALA A 536 ? ALA A 536  . ? 1_555 ? 
41 AC5 7  ALA A 537 ? ALA A 537  . ? 1_555 ? 
42 AC5 7  MET A 567 ? MET A 567  . ? 1_555 ? 
43 AC5 7  HOH J .   ? HOH A 4109 . ? 1_555 ? 
44 AC5 7  HOH J .   ? HOH A 4154 . ? 1_555 ? 
45 AC5 7  HOH J .   ? HOH A 4290 . ? 1_555 ? 
46 AC6 5  GLU A 582 ? GLU A 582  . ? 1_555 ? 
47 AC6 5  ARG A 585 ? ARG A 585  . ? 1_555 ? 
48 AC6 5  GLU A 689 ? GLU A 689  . ? 1_555 ? 
49 AC6 5  GLY A 722 ? GLY A 722  . ? 1_555 ? 
50 AC6 5  HOH J .   ? HOH A 4152 . ? 1_555 ? 
51 AC7 5  ASN A 306 ? ASN A 306  . ? 1_555 ? 
52 AC7 5  GLU A 309 ? GLU A 309  . ? 1_555 ? 
53 AC7 5  ARG A 313 ? ARG A 313  . ? 1_555 ? 
54 AC7 5  ASP A 607 ? ASP A 607  . ? 1_555 ? 
55 AC7 5  HOH J .   ? HOH A 4033 . ? 1_555 ? 
56 AC8 7  PHE A 65  ? PHE A 65   . ? 2_454 ? 
57 AC8 7  VAL A 131 ? VAL A 131  . ? 2_454 ? 
58 AC8 7  GLU A 132 ? GLU A 132  . ? 2_454 ? 
59 AC8 7  ILE A 133 ? ILE A 133  . ? 2_454 ? 
60 AC8 7  THR A 843 ? THR A 843  . ? 1_555 ? 
61 AC8 7  THR A 854 ? THR A 854  . ? 1_555 ? 
62 AC8 7  HOH J .   ? HOH A 4582 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3L4X 
_atom_sites.fract_transf_matrix[1][1]   0.011471 
_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]   0.009138 
_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]   0.009147 
_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   ? -13.053 -37.131 63.348 1.00 40.46 ? 7    VAL A N   1 
ATOM   2    C CA  . VAL A 1 7   ? -12.633 -36.218 62.247 1.00 40.16 ? 7    VAL A CA  1 
ATOM   3    C C   . VAL A 1 7   ? -13.456 -36.524 60.985 1.00 38.82 ? 7    VAL A C   1 
ATOM   4    O O   . VAL A 1 7   ? -13.037 -37.350 60.162 1.00 40.08 ? 7    VAL A O   1 
ATOM   5    C CB  . VAL A 1 7   ? -11.088 -36.335 61.937 1.00 40.48 ? 7    VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 7   ? -10.624 -35.232 60.990 1.00 40.62 ? 7    VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 7   ? -10.265 -36.297 63.221 1.00 42.31 ? 7    VAL A CG2 1 
ATOM   8    N N   . ASN A 1 8   ? -14.633 -35.887 60.885 1.00 36.86 ? 8    ASN A N   1 
ATOM   9    C CA  . ASN A 1 8   ? -15.442 -35.739 59.659 1.00 33.71 ? 8    ASN A CA  1 
ATOM   10   C C   . ASN A 1 8   ? -14.529 -35.839 58.460 1.00 31.59 ? 8    ASN A C   1 
ATOM   11   O O   . ASN A 1 8   ? -13.522 -35.135 58.392 1.00 30.18 ? 8    ASN A O   1 
ATOM   12   C CB  . ASN A 1 8   ? -16.108 -34.360 59.674 1.00 33.97 ? 8    ASN A CB  1 
ATOM   13   C CG  . ASN A 1 8   ? -17.100 -34.119 58.493 1.00 35.69 ? 8    ASN A CG  1 
ATOM   14   O OD1 . ASN A 1 8   ? -16.948 -34.616 57.367 1.00 33.79 ? 8    ASN A OD1 1 
ATOM   15   N ND2 . ASN A 1 8   ? -18.111 -33.303 58.770 1.00 40.61 ? 8    ASN A ND2 1 
ATOM   16   N N   . GLU A 1 9   ? -14.854 -36.713 57.517 1.00 29.69 ? 9    GLU A N   1 
ATOM   17   C CA  . GLU A 1 9   ? -13.905 -36.949 56.439 1.00 29.08 ? 9    GLU A CA  1 
ATOM   18   C C   . GLU A 1 9   ? -13.701 -35.739 55.512 1.00 26.32 ? 9    GLU A C   1 
ATOM   19   O O   . GLU A 1 9   ? -12.643 -35.597 54.922 1.00 24.61 ? 9    GLU A O   1 
ATOM   20   C CB  . GLU A 1 9   ? -14.172 -38.261 55.695 1.00 30.40 ? 9    GLU A CB  1 
ATOM   21   C CG  . GLU A 1 9   ? -15.485 -38.411 54.978 1.00 31.92 ? 9    GLU A CG  1 
ATOM   22   C CD  . GLU A 1 9   ? -15.610 -39.812 54.387 1.00 33.47 ? 9    GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 9   ? -15.472 -40.820 55.134 1.00 39.59 ? 9    GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 9   ? -15.832 -39.917 53.159 1.00 40.17 ? 9    GLU A OE2 1 
ATOM   25   N N   . LEU A 1 10  ? -14.689 -34.841 55.427 1.00 23.03 ? 10   LEU A N   1 
ATOM   26   C CA  . LEU A 1 10  ? -14.532 -33.661 54.580 1.00 22.09 ? 10   LEU A CA  1 
ATOM   27   C C   . LEU A 1 10  ? -13.541 -32.657 55.129 1.00 20.02 ? 10   LEU A C   1 
ATOM   28   O O   . LEU A 1 10  ? -13.097 -31.796 54.395 1.00 19.94 ? 10   LEU A O   1 
ATOM   29   C CB  . LEU A 1 10  ? -15.872 -32.967 54.342 1.00 21.81 ? 10   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 10  ? -17.014 -33.815 53.786 1.00 23.28 ? 10   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 10  ? -18.155 -32.872 53.500 1.00 24.30 ? 10   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 10  ? -16.608 -34.537 52.522 1.00 23.67 ? 10   LEU A CD2 1 
ATOM   33   N N   . GLU A 1 11  ? -13.189 -32.783 56.408 1.00 18.84 ? 11   GLU A N   1 
ATOM   34   C CA  . GLU A 1 11  ? -12.271 -31.856 57.075 1.00 19.70 ? 11   GLU A CA  1 
ATOM   35   C C   . GLU A 1 11  ? -10.836 -32.396 57.163 1.00 18.47 ? 11   GLU A C   1 
ATOM   36   O O   . GLU A 1 11  ? -9.953  -31.711 57.672 1.00 17.19 ? 11   GLU A O   1 
ATOM   37   C CB  . GLU A 1 11  ? -12.781 -31.523 58.472 1.00 19.67 ? 11   GLU A CB  1 
ATOM   38   C CG  . GLU A 1 11  ? -14.091 -30.722 58.408 1.00 22.53 ? 11   GLU A CG  1 
ATOM   39   C CD  . GLU A 1 11  ? -14.756 -30.472 59.751 1.00 25.75 ? 11   GLU A CD  1 
ATOM   40   O OE1 . GLU A 1 11  ? -14.111 -30.634 60.810 1.00 33.28 ? 11   GLU A OE1 1 
ATOM   41   O OE2 . GLU A 1 11  ? -15.960 -30.080 59.729 1.00 33.47 ? 11   GLU A OE2 1 
ATOM   42   N N   . ARG A 1 12  ? -10.607 -33.600 56.655 1.00 18.40 ? 12   ARG A N   1 
ATOM   43   C CA  . ARG A 1 12  ? -9.228  -34.137 56.700 1.00 19.18 ? 12   ARG A CA  1 
ATOM   44   C C   . ARG A 1 12  ? -8.305  -33.373 55.764 1.00 18.10 ? 12   ARG A C   1 
ATOM   45   O O   . ARG A 1 12  ? -8.651  -33.141 54.606 1.00 19.16 ? 12   ARG A O   1 
ATOM   46   C CB  . ARG A 1 12  ? -9.203  -35.601 56.297 1.00 19.39 ? 12   ARG A CB  1 
ATOM   47   C CG  . ARG A 1 12  ? -10.083 -36.502 57.147 1.00 22.41 ? 12   ARG A CG  1 
ATOM   48   C CD  . ARG A 1 12  ? -10.170 -37.783 56.369 1.00 25.39 ? 12   ARG A CD  1 
ATOM   49   N NE  . ARG A 1 12  ? -10.860 -38.851 57.052 1.00 31.73 ? 12   ARG A NE  1 
ATOM   50   C CZ  . ARG A 1 12  ? -10.736 -40.143 56.727 1.00 32.68 ? 12   ARG A CZ  1 
ATOM   51   N NH1 . ARG A 1 12  ? -9.887  -40.579 55.756 1.00 29.36 ? 12   ARG A NH1 1 
ATOM   52   N NH2 . ARG A 1 12  ? -11.449 -41.006 57.411 1.00 31.58 ? 12   ARG A NH2 1 
ATOM   53   N N   . ILE A 1 13  ? -7.122  -33.042 56.257 1.00 17.38 ? 13   ILE A N   1 
ATOM   54   C CA  . ILE A 1 13  ? -6.122  -32.290 55.517 1.00 16.11 ? 13   ILE A CA  1 
ATOM   55   C C   . ILE A 1 13  ? -5.023  -33.287 55.102 1.00 16.38 ? 13   ILE A C   1 
ATOM   56   O O   . ILE A 1 13  ? -4.404  -33.919 55.943 1.00 14.25 ? 13   ILE A O   1 
ATOM   57   C CB  . ILE A 1 13  ? -5.556  -31.122 56.340 1.00 16.06 ? 13   ILE A CB  1 
ATOM   58   C CG1 . ILE A 1 13  ? -6.667  -30.113 56.711 1.00 15.75 ? 13   ILE A CG1 1 
ATOM   59   C CG2 . ILE A 1 13  ? -4.471  -30.365 55.584 1.00 15.74 ? 13   ILE A CG2 1 
ATOM   60   C CD1 . ILE A 1 13  ? -7.349  -29.445 55.522 1.00 17.24 ? 13   ILE A CD1 1 
ATOM   61   N N   . ASN A 1 14  ? -4.867  -33.435 53.796 1.00 16.12 ? 14   ASN A N   1 
ATOM   62   C CA  . ASN A 1 14  ? -3.999  -34.449 53.195 1.00 16.91 ? 14   ASN A CA  1 
ATOM   63   C C   . ASN A 1 14  ? -2.523  -34.316 53.633 1.00 16.30 ? 14   ASN A C   1 
ATOM   64   O O   . ASN A 1 14  ? -1.884  -33.279 53.405 1.00 16.56 ? 14   ASN A O   1 
ATOM   65   C CB  . ASN A 1 14  ? -4.135  -34.363 51.671 1.00 16.42 ? 14   ASN A CB  1 
ATOM   66   C CG  . ASN A 1 14  ? -3.379  -35.483 50.941 1.00 19.19 ? 14   ASN A CG  1 
ATOM   67   O OD1 . ASN A 1 14  ? -2.937  -36.439 51.556 1.00 16.46 ? 14   ASN A OD1 1 
ATOM   68   N ND2 . ASN A 1 14  ? -3.260  -35.361 49.617 1.00 19.02 ? 14   ASN A ND2 1 
ATOM   69   N N   . CYS A 1 15  ? -1.979  -35.395 54.221 1.00 17.56 ? 15   CYS A N   1 
ATOM   70   C CA  . CYS A 1 15  ? -0.600  -35.439 54.750 1.00 18.26 ? 15   CYS A CA  1 
ATOM   71   C C   . CYS A 1 15  ? 0.363   -36.076 53.731 1.00 18.14 ? 15   CYS A C   1 
ATOM   72   O O   . CYS A 1 15  ? 1.589   -36.102 53.947 1.00 17.81 ? 15   CYS A O   1 
ATOM   73   C CB  . CYS A 1 15  ? -0.597  -36.238 56.081 1.00 19.04 ? 15   CYS A CB  1 
ATOM   74   S SG  . CYS A 1 15  ? 1.031   -36.624 56.748 1.00 23.07 ? 15   CYS A SG  1 
ATOM   75   N N   . ILE A 1 16  ? -0.202  -36.613 52.640 1.00 17.21 ? 16   ILE A N   1 
ATOM   76   C CA  . ILE A 1 16  ? 0.611   -37.204 51.571 1.00 17.06 ? 16   ILE A CA  1 
ATOM   77   C C   . ILE A 1 16  ? 0.202   -36.595 50.231 1.00 17.57 ? 16   ILE A C   1 
ATOM   78   O O   . ILE A 1 16  ? -0.448  -37.264 49.423 1.00 18.64 ? 16   ILE A O   1 
ATOM   79   C CB  . ILE A 1 16  ? 0.518   -38.761 51.516 1.00 16.28 ? 16   ILE A CB  1 
ATOM   80   C CG1 . ILE A 1 16  ? 0.809   -39.369 52.878 1.00 16.16 ? 16   ILE A CG1 1 
ATOM   81   C CG2 . ILE A 1 16  ? 1.468   -39.286 50.475 1.00 18.60 ? 16   ILE A CG2 1 
ATOM   82   C CD1 . ILE A 1 16  ? 0.724   -40.917 52.935 1.00 14.93 ? 16   ILE A CD1 1 
ATOM   83   N N   . PRO A 1 17  ? 0.588   -35.330 49.987 1.00 18.49 ? 17   PRO A N   1 
ATOM   84   C CA  . PRO A 1 17  ? 0.244   -34.678 48.723 1.00 20.56 ? 17   PRO A CA  1 
ATOM   85   C C   . PRO A 1 17  ? 1.130   -35.108 47.548 1.00 22.63 ? 17   PRO A C   1 
ATOM   86   O O   . PRO A 1 17  ? 0.818   -34.791 46.384 1.00 23.14 ? 17   PRO A O   1 
ATOM   87   C CB  . PRO A 1 17  ? 0.478   -33.199 49.047 1.00 20.28 ? 17   PRO A CB  1 
ATOM   88   C CG  . PRO A 1 17  ? 1.596   -33.197 50.004 1.00 20.23 ? 17   PRO A CG  1 
ATOM   89   C CD  . PRO A 1 17  ? 1.336   -34.416 50.873 1.00 19.16 ? 17   PRO A CD  1 
ATOM   90   N N   . ASP A 1 18  ? 2.204   -35.844 47.853 1.00 22.38 ? 18   ASP A N   1 
ATOM   91   C CA  . ASP A 1 18  ? 3.355   -35.976 46.965 1.00 24.48 ? 18   ASP A CA  1 
ATOM   92   C C   . ASP A 1 18  ? 3.474   -37.351 46.336 1.00 26.11 ? 18   ASP A C   1 
ATOM   93   O O   . ASP A 1 18  ? 4.323   -37.555 45.457 1.00 26.77 ? 18   ASP A O   1 
ATOM   94   C CB  . ASP A 1 18  ? 4.640   -35.708 47.747 1.00 23.77 ? 18   ASP A CB  1 
ATOM   95   C CG  . ASP A 1 18  ? 4.705   -36.488 49.085 1.00 25.55 ? 18   ASP A CG  1 
ATOM   96   O OD1 . ASP A 1 18  ? 3.690   -36.557 49.830 1.00 25.01 ? 18   ASP A OD1 1 
ATOM   97   O OD2 . ASP A 1 18  ? 5.799   -37.019 49.413 1.00 28.26 ? 18   ASP A OD2 1 
ATOM   98   N N   . GLN A 1 19  ? 2.670   -38.299 46.807 1.00 25.72 ? 19   GLN A N   1 
ATOM   99   C CA  . GLN A 1 19  ? 2.764   -39.667 46.310 1.00 27.53 ? 19   GLN A CA  1 
ATOM   100  C C   . GLN A 1 19  ? 1.490   -40.442 46.589 1.00 27.88 ? 19   GLN A C   1 
ATOM   101  O O   . GLN A 1 19  ? 0.632   -39.943 47.307 1.00 27.74 ? 19   GLN A O   1 
ATOM   102  C CB  . GLN A 1 19  ? 3.953   -40.360 46.953 1.00 27.81 ? 19   GLN A CB  1 
ATOM   103  C CG  . GLN A 1 19  ? 3.823   -40.620 48.409 1.00 28.35 ? 19   GLN A CG  1 
ATOM   104  C CD  . GLN A 1 19  ? 5.168   -40.885 49.048 1.00 32.90 ? 19   GLN A CD  1 
ATOM   105  O OE1 . GLN A 1 19  ? 6.185   -40.386 48.590 1.00 36.84 ? 19   GLN A OE1 1 
ATOM   106  N NE2 . GLN A 1 19  ? 5.179   -41.670 50.098 1.00 31.54 ? 19   GLN A NE2 1 
ATOM   107  N N   . PRO A 1 20  ? 1.348   -41.657 45.999 1.00 28.19 ? 20   PRO A N   1 
ATOM   108  C CA  . PRO A 1 20  ? 0.228   -42.541 46.345 1.00 27.81 ? 20   PRO A CA  1 
ATOM   109  C C   . PRO A 1 20  ? 0.260   -42.870 47.849 1.00 26.43 ? 20   PRO A C   1 
ATOM   110  O O   . PRO A 1 20  ? 1.296   -43.255 48.346 1.00 26.55 ? 20   PRO A O   1 
ATOM   111  C CB  . PRO A 1 20  ? 0.513   -43.806 45.528 1.00 27.55 ? 20   PRO A CB  1 
ATOM   112  C CG  . PRO A 1 20  ? 1.368   -43.327 44.386 1.00 28.51 ? 20   PRO A CG  1 
ATOM   113  C CD  . PRO A 1 20  ? 2.218   -42.256 44.964 1.00 28.91 ? 20   PRO A CD  1 
ATOM   114  N N   . PRO A 1 21  ? -0.866  -42.718 48.555 1.00 25.65 ? 21   PRO A N   1 
ATOM   115  C CA  . PRO A 1 21  ? -0.885  -42.871 50.025 1.00 25.06 ? 21   PRO A CA  1 
ATOM   116  C C   . PRO A 1 21  ? -0.631  -44.301 50.512 1.00 23.98 ? 21   PRO A C   1 
ATOM   117  O O   . PRO A 1 21  ? -1.279  -45.245 50.035 1.00 23.22 ? 21   PRO A O   1 
ATOM   118  C CB  . PRO A 1 21  ? -2.304  -42.442 50.415 1.00 24.76 ? 21   PRO A CB  1 
ATOM   119  C CG  . PRO A 1 21  ? -3.131  -42.674 49.172 1.00 27.08 ? 21   PRO A CG  1 
ATOM   120  C CD  . PRO A 1 21  ? -2.197  -42.394 48.006 1.00 26.64 ? 21   PRO A CD  1 
ATOM   121  N N   . THR A 1 22  ? 0.287   -44.442 51.470 1.00 22.47 ? 22   THR A N   1 
ATOM   122  C CA  . THR A 1 22  ? 0.593   -45.723 52.083 1.00 21.94 ? 22   THR A CA  1 
ATOM   123  C C   . THR A 1 22  ? 0.638   -45.574 53.603 1.00 22.29 ? 22   THR A C   1 
ATOM   124  O O   . THR A 1 22  ? 0.982   -44.505 54.103 1.00 21.47 ? 22   THR A O   1 
ATOM   125  C CB  . THR A 1 22  ? 1.949   -46.306 51.580 1.00 21.93 ? 22   THR A CB  1 
ATOM   126  O OG1 . THR A 1 22  ? 3.034   -45.473 51.978 1.00 21.92 ? 22   THR A OG1 1 
ATOM   127  C CG2 . THR A 1 22  ? 1.966   -46.430 50.042 1.00 20.77 ? 22   THR A CG2 1 
ATOM   128  N N   . LYS A 1 23  ? 0.296   -46.637 54.321 1.00 22.66 ? 23   LYS A N   1 
ATOM   129  C CA  . LYS A 1 23  ? 0.350   -46.610 55.795 1.00 23.49 ? 23   LYS A CA  1 
ATOM   130  C C   . LYS A 1 23  ? 1.784   -46.409 56.248 1.00 22.95 ? 23   LYS A C   1 
ATOM   131  O O   . LYS A 1 23  ? 2.031   -45.772 57.246 1.00 21.96 ? 23   LYS A O   1 
ATOM   132  C CB  . LYS A 1 23  ? -0.206  -47.894 56.408 1.00 24.40 ? 23   LYS A CB  1 
ATOM   133  C CG  . LYS A 1 23  ? -0.443  -47.795 57.950 1.00 25.38 ? 23   LYS A CG  1 
ATOM   134  C CD  . LYS A 1 23  ? -1.035  -49.102 58.483 1.00 26.97 ? 23   LYS A CD  1 
ATOM   135  C CE  . LYS A 1 23  ? -1.351  -49.050 59.996 1.00 30.14 ? 23   LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 23  ? -0.405  -48.294 60.860 1.00 33.60 ? 23   LYS A NZ  1 
ATOM   137  N N   . ALA A 1 24  ? 2.740   -46.968 55.517 1.00 22.43 ? 24   ALA A N   1 
ATOM   138  C CA  . ALA A 1 24  ? 4.128   -46.840 55.904 1.00 22.75 ? 24   ALA A CA  1 
ATOM   139  C C   . ALA A 1 24  ? 4.552   -45.359 55.936 1.00 22.48 ? 24   ALA A C   1 
ATOM   140  O O   . ALA A 1 24  ? 5.131   -44.878 56.920 1.00 23.01 ? 24   ALA A O   1 
ATOM   141  C CB  . ALA A 1 24  ? 5.031   -47.675 54.935 1.00 23.93 ? 24   ALA A CB  1 
ATOM   142  N N   . THR A 1 25  ? 4.227   -44.622 54.878 1.00 21.53 ? 25   THR A N   1 
ATOM   143  C CA  . THR A 1 25  ? 4.590   -43.212 54.801 1.00 22.31 ? 25   THR A CA  1 
ATOM   144  C C   . THR A 1 25  ? 3.774   -42.448 55.842 1.00 21.73 ? 25   THR A C   1 
ATOM   145  O O   . THR A 1 25  ? 4.304   -41.576 56.516 1.00 20.87 ? 25   THR A O   1 
ATOM   146  C CB  . THR A 1 25  ? 4.356   -42.630 53.384 1.00 21.96 ? 25   THR A CB  1 
ATOM   147  O OG1 . THR A 1 25  ? 5.360   -43.134 52.496 1.00 24.89 ? 25   THR A OG1 1 
ATOM   148  C CG2 . THR A 1 25  ? 4.482   -41.078 53.373 1.00 21.14 ? 25   THR A CG2 1 
ATOM   149  N N   . CYS A 1 26  ? 2.500   -42.821 55.968 1.00 23.16 ? 26   CYS A N   1 
ATOM   150  C CA  . CYS A 1 26  ? 1.615   -42.196 56.945 1.00 23.82 ? 26   CYS A CA  1 
ATOM   151  C C   . CYS A 1 26  ? 2.197   -42.294 58.346 1.00 23.54 ? 26   CYS A C   1 
ATOM   152  O O   . CYS A 1 26  ? 2.290   -41.287 59.057 1.00 22.31 ? 26   CYS A O   1 
ATOM   153  C CB  . CYS A 1 26  ? 0.254   -42.861 56.920 1.00 24.32 ? 26   CYS A CB  1 
ATOM   154  S SG  . CYS A 1 26  ? -0.859  -41.997 58.050 1.00 28.90 ? 26   CYS A SG  1 
ATOM   155  N N   . ASP A 1 27  ? 2.609   -43.508 58.724 1.00 24.34 ? 27   ASP A N   1 
ATOM   156  C CA  . ASP A 1 27  ? 3.223   -43.761 60.045 1.00 25.14 ? 27   ASP A CA  1 
ATOM   157  C C   . ASP A 1 27  ? 4.509   -42.993 60.253 1.00 24.99 ? 27   ASP A C   1 
ATOM   158  O O   . ASP A 1 27  ? 4.723   -42.434 61.323 1.00 25.33 ? 27   ASP A O   1 
ATOM   159  C CB  . ASP A 1 27  ? 3.459   -45.263 60.255 1.00 24.99 ? 27   ASP A CB  1 
ATOM   160  C CG  . ASP A 1 27  ? 2.169   -46.022 60.477 1.00 28.70 ? 27   ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 27  ? 1.125   -45.387 60.708 1.00 29.98 ? 27   ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 27  ? 2.171   -47.259 60.414 1.00 34.13 ? 27   ASP A OD2 1 
ATOM   163  N N   . GLN A 1 28  ? 5.378   -42.968 59.240 1.00 24.89 ? 28   GLN A N   1 
ATOM   164  C CA  . GLN A 1 28  ? 6.638   -42.212 59.306 1.00 25.46 ? 28   GLN A CA  1 
ATOM   165  C C   . GLN A 1 28  ? 6.433   -40.703 59.528 1.00 24.25 ? 28   GLN A C   1 
ATOM   166  O O   . GLN A 1 28  ? 7.258   -40.004 60.166 1.00 23.44 ? 28   GLN A O   1 
ATOM   167  C CB  . GLN A 1 28  ? 7.415   -42.448 58.004 1.00 25.47 ? 28   GLN A CB  1 
ATOM   168  C CG  . GLN A 1 28  ? 8.708   -41.683 57.881 1.00 28.11 ? 28   GLN A CG  1 
ATOM   169  C CD  . GLN A 1 28  ? 9.265   -41.672 56.462 1.00 30.63 ? 28   GLN A CD  1 
ATOM   170  O OE1 . GLN A 1 28  ? 8.838   -42.472 55.588 1.00 39.31 ? 28   GLN A OE1 1 
ATOM   171  N NE2 . GLN A 1 28  ? 10.197  -40.735 56.202 1.00 34.71 ? 28   GLN A NE2 1 
ATOM   172  N N   . ARG A 1 29  ? 5.335   -40.191 58.987 1.00 22.65 ? 29   ARG A N   1 
ATOM   173  C CA  . ARG A 1 29  ? 5.089   -38.745 59.011 1.00 22.00 ? 29   ARG A CA  1 
ATOM   174  C C   . ARG A 1 29  ? 4.298   -38.361 60.253 1.00 22.18 ? 29   ARG A C   1 
ATOM   175  O O   . ARG A 1 29  ? 4.085   -37.169 60.520 1.00 22.29 ? 29   ARG A O   1 
ATOM   176  C CB  . ARG A 1 29  ? 4.363   -38.322 57.730 1.00 21.51 ? 29   ARG A CB  1 
ATOM   177  C CG  . ARG A 1 29  ? 5.194   -38.502 56.494 1.00 22.13 ? 29   ARG A CG  1 
ATOM   178  C CD  . ARG A 1 29  ? 4.541   -37.894 55.271 1.00 24.27 ? 29   ARG A CD  1 
ATOM   179  N NE  . ARG A 1 29  ? 5.436   -38.107 54.136 1.00 22.75 ? 29   ARG A NE  1 
ATOM   180  C CZ  . ARG A 1 29  ? 5.182   -37.747 52.898 1.00 23.09 ? 29   ARG A CZ  1 
ATOM   181  N NH1 . ARG A 1 29  ? 4.058   -37.098 52.598 1.00 16.61 ? 29   ARG A NH1 1 
ATOM   182  N NH2 . ARG A 1 29  ? 6.079   -38.016 51.962 1.00 22.24 ? 29   ARG A NH2 1 
ATOM   183  N N   . GLY A 1 30  ? 3.875   -39.381 61.014 1.00 21.86 ? 30   GLY A N   1 
ATOM   184  C CA  . GLY A 1 30  ? 3.084   -39.218 62.227 1.00 20.99 ? 30   GLY A CA  1 
ATOM   185  C C   . GLY A 1 30  ? 1.663   -38.711 61.960 1.00 21.83 ? 30   GLY A C   1 
ATOM   186  O O   . GLY A 1 30  ? 1.109   -37.980 62.776 1.00 21.75 ? 30   GLY A O   1 
ATOM   187  N N   . CYS A 1 31  ? 1.073   -39.121 60.842 1.00 20.48 ? 31   CYS A N   1 
ATOM   188  C CA  . CYS A 1 31  ? -0.290  -38.699 60.457 1.00 21.41 ? 31   CYS A CA  1 
ATOM   189  C C   . CYS A 1 31  ? -1.307  -39.791 60.732 1.00 21.41 ? 31   CYS A C   1 
ATOM   190  O O   . CYS A 1 31  ? -0.948  -40.850 61.272 1.00 22.27 ? 31   CYS A O   1 
ATOM   191  C CB  . CYS A 1 31  ? -0.290  -38.241 58.985 1.00 20.55 ? 31   CYS A CB  1 
ATOM   192  S SG  . CYS A 1 31  ? 0.681   -36.739 58.745 1.00 22.00 ? 31   CYS A SG  1 
ATOM   193  N N   . CYS A 1 32  ? -2.584  -39.551 60.425 1.00 21.40 ? 32   CYS A N   1 
ATOM   194  C CA  . CYS A 1 32  ? -3.630  -40.529 60.702 1.00 23.32 ? 32   CYS A CA  1 
ATOM   195  C C   . CYS A 1 32  ? -3.979  -41.318 59.434 1.00 23.08 ? 32   CYS A C   1 
ATOM   196  O O   . CYS A 1 32  ? -4.048  -40.743 58.346 1.00 21.77 ? 32   CYS A O   1 
ATOM   197  C CB  . CYS A 1 32  ? -4.891  -39.836 61.206 1.00 23.59 ? 32   CYS A CB  1 
ATOM   198  S SG  . CYS A 1 32  ? -4.562  -38.654 62.488 1.00 27.13 ? 32   CYS A SG  1 
ATOM   199  N N   . TRP A 1 33  ? -4.206  -42.626 59.585 1.00 23.57 ? 33   TRP A N   1 
ATOM   200  C CA  . TRP A 1 33  ? -4.496  -43.518 58.463 1.00 24.93 ? 33   TRP A CA  1 
ATOM   201  C C   . TRP A 1 33  ? -5.933  -44.055 58.505 1.00 26.97 ? 33   TRP A C   1 
ATOM   202  O O   . TRP A 1 33  ? -6.355  -44.651 59.498 1.00 27.05 ? 33   TRP A O   1 
ATOM   203  C CB  . TRP A 1 33  ? -3.497  -44.688 58.472 1.00 24.96 ? 33   TRP A CB  1 
ATOM   204  C CG  . TRP A 1 33  ? -3.668  -45.649 57.360 1.00 23.73 ? 33   TRP A CG  1 
ATOM   205  C CD1 . TRP A 1 33  ? -4.150  -46.932 57.452 1.00 25.20 ? 33   TRP A CD1 1 
ATOM   206  C CD2 . TRP A 1 33  ? -3.340  -45.442 55.977 1.00 24.76 ? 33   TRP A CD2 1 
ATOM   207  N NE1 . TRP A 1 33  ? -4.163  -47.521 56.204 1.00 23.54 ? 33   TRP A NE1 1 
ATOM   208  C CE2 . TRP A 1 33  ? -3.665  -46.639 55.284 1.00 24.84 ? 33   TRP A CE2 1 
ATOM   209  C CE3 . TRP A 1 33  ? -2.818  -44.363 55.251 1.00 23.53 ? 33   TRP A CE3 1 
ATOM   210  C CZ2 . TRP A 1 33  ? -3.470  -46.788 53.907 1.00 24.16 ? 33   TRP A CZ2 1 
ATOM   211  C CZ3 . TRP A 1 33  ? -2.621  -44.516 53.875 1.00 23.81 ? 33   TRP A CZ3 1 
ATOM   212  C CH2 . TRP A 1 33  ? -2.960  -45.718 53.222 1.00 24.68 ? 33   TRP A CH2 1 
ATOM   213  N N   . ASN A 1 34  ? -6.685  -43.846 57.428 1.00 28.44 ? 34   ASN A N   1 
ATOM   214  C CA  . ASN A 1 34  ? -8.058  -44.339 57.336 1.00 31.36 ? 34   ASN A CA  1 
ATOM   215  C C   . ASN A 1 34  ? -8.444  -44.388 55.864 1.00 32.82 ? 34   ASN A C   1 
ATOM   216  O O   . ASN A 1 34  ? -8.931  -43.390 55.304 1.00 31.92 ? 34   ASN A O   1 
ATOM   217  C CB  . ASN A 1 34  ? -9.017  -43.454 58.151 1.00 31.89 ? 34   ASN A CB  1 
ATOM   218  C CG  . ASN A 1 34  ? -10.470 -43.978 58.169 1.00 34.87 ? 34   ASN A CG  1 
ATOM   219  O OD1 . ASN A 1 34  ? -10.884 -44.768 57.325 1.00 38.59 ? 34   ASN A OD1 1 
ATOM   220  N ND2 . ASN A 1 34  ? -11.245 -43.507 59.130 1.00 36.87 ? 34   ASN A ND2 1 
ATOM   221  N N   . PRO A 1 35  ? -8.204  -45.546 55.214 1.00 34.80 ? 35   PRO A N   1 
ATOM   222  C CA  . PRO A 1 35  ? -8.481  -45.654 53.795 1.00 36.48 ? 35   PRO A CA  1 
ATOM   223  C C   . PRO A 1 35  ? -9.962  -45.796 53.465 1.00 38.38 ? 35   PRO A C   1 
ATOM   224  O O   . PRO A 1 35  ? -10.290 -45.912 52.292 1.00 39.55 ? 35   PRO A O   1 
ATOM   225  C CB  . PRO A 1 35  ? -7.733  -46.929 53.369 1.00 36.13 ? 35   PRO A CB  1 
ATOM   226  C CG  . PRO A 1 35  ? -6.995  -47.400 54.581 1.00 36.05 ? 35   PRO A CG  1 
ATOM   227  C CD  . PRO A 1 35  ? -7.652  -46.798 55.758 1.00 34.71 ? 35   PRO A CD  1 
ATOM   228  N N   . GLN A 1 36  ? -10.843 -45.771 54.461 1.00 40.11 ? 36   GLN A N   1 
ATOM   229  C CA  . GLN A 1 36  ? -12.272 -46.093 54.230 1.00 42.49 ? 36   GLN A CA  1 
ATOM   230  C C   . GLN A 1 36  ? -13.208 -44.938 53.772 1.00 42.94 ? 36   GLN A C   1 
ATOM   231  O O   . GLN A 1 36  ? -14.431 -45.122 53.735 1.00 43.69 ? 36   GLN A O   1 
ATOM   232  C CB  . GLN A 1 36  ? -12.900 -46.825 55.443 1.00 42.94 ? 36   GLN A CB  1 
ATOM   233  C CG  . GLN A 1 36  ? -12.127 -48.034 56.021 1.00 45.83 ? 36   GLN A CG  1 
ATOM   234  C CD  . GLN A 1 36  ? -11.743 -49.090 54.985 1.00 49.16 ? 36   GLN A CD  1 
ATOM   235  O OE1 . GLN A 1 36  ? -12.498 -49.378 54.039 1.00 49.52 ? 36   GLN A OE1 1 
ATOM   236  N NE2 . GLN A 1 36  ? -10.562 -49.682 55.169 1.00 49.80 ? 36   GLN A NE2 1 
ATOM   237  N N   . GLY A 1 37  ? -12.660 -43.774 53.414 1.00 43.28 ? 37   GLY A N   1 
ATOM   238  C CA  . GLY A 1 37  ? -13.494 -42.641 52.950 1.00 42.80 ? 37   GLY A CA  1 
ATOM   239  C C   . GLY A 1 37  ? -13.987 -42.757 51.506 1.00 42.66 ? 37   GLY A C   1 
ATOM   240  O O   . GLY A 1 37  ? -13.650 -43.727 50.797 1.00 43.81 ? 37   GLY A O   1 
ATOM   241  N N   . ALA A 1 38  ? -14.774 -41.770 51.055 1.00 41.24 ? 38   ALA A N   1 
ATOM   242  C CA  . ALA A 1 38  ? -15.236 -41.715 49.658 1.00 39.52 ? 38   ALA A CA  1 
ATOM   243  C C   . ALA A 1 38  ? -14.105 -41.300 48.713 1.00 38.29 ? 38   ALA A C   1 
ATOM   244  O O   . ALA A 1 38  ? -13.018 -40.954 49.174 1.00 37.47 ? 38   ALA A O   1 
ATOM   245  C CB  . ALA A 1 38  ? -16.407 -40.763 49.533 1.00 39.99 ? 38   ALA A CB  1 
ATOM   246  N N   . VAL A 1 39  ? -14.355 -41.330 47.402 1.00 36.02 ? 39   VAL A N   1 
ATOM   247  C CA  . VAL A 1 39  ? -13.350 -40.889 46.424 1.00 34.04 ? 39   VAL A CA  1 
ATOM   248  C C   . VAL A 1 39  ? -12.729 -39.528 46.808 1.00 32.22 ? 39   VAL A C   1 
ATOM   249  O O   . VAL A 1 39  ? -13.426 -38.612 47.258 1.00 31.94 ? 39   VAL A O   1 
ATOM   250  C CB  . VAL A 1 39  ? -13.881 -40.891 44.950 1.00 33.99 ? 39   VAL A CB  1 
ATOM   251  C CG1 . VAL A 1 39  ? -14.988 -39.862 44.744 1.00 34.99 ? 39   VAL A CG1 1 
ATOM   252  C CG2 . VAL A 1 39  ? -12.737 -40.668 43.963 1.00 34.28 ? 39   VAL A CG2 1 
ATOM   253  N N   . SER A 1 40  ? -11.408 -39.447 46.684 1.00 29.86 ? 40   SER A N   1 
ATOM   254  C CA  . SER A 1 40  ? -10.638 -38.199 46.872 1.00 28.59 ? 40   SER A CA  1 
ATOM   255  C C   . SER A 1 40  ? -10.459 -37.803 48.331 1.00 26.18 ? 40   SER A C   1 
ATOM   256  O O   . SER A 1 40  ? -9.617  -36.970 48.635 1.00 26.05 ? 40   SER A O   1 
ATOM   257  C CB  . SER A 1 40  ? -11.211 -37.020 46.059 1.00 28.83 ? 40   SER A CB  1 
ATOM   258  O OG  . SER A 1 40  ? -11.376 -37.375 44.690 1.00 32.86 ? 40   SER A OG  1 
ATOM   259  N N   . VAL A 1 41  ? -11.211 -38.420 49.234 1.00 23.59 ? 41   VAL A N   1 
ATOM   260  C CA  . VAL A 1 41  ? -10.990 -38.196 50.668 1.00 22.72 ? 41   VAL A CA  1 
ATOM   261  C C   . VAL A 1 41  ? -9.602  -38.727 51.025 1.00 21.25 ? 41   VAL A C   1 
ATOM   262  O O   . VAL A 1 41  ? -9.299  -39.877 50.719 1.00 21.13 ? 41   VAL A O   1 
ATOM   263  C CB  . VAL A 1 41  ? -12.067 -38.860 51.522 1.00 22.79 ? 41   VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 41  ? -11.741 -38.769 53.031 1.00 23.20 ? 41   VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 41  ? -13.399 -38.217 51.211 1.00 22.55 ? 41   VAL A CG2 1 
ATOM   266  N N   . PRO A 1 42  ? -8.762  -37.889 51.655 1.00 20.57 ? 42   PRO A N   1 
ATOM   267  C CA  . PRO A 1 42  ? -7.385  -38.330 51.915 1.00 20.27 ? 42   PRO A CA  1 
ATOM   268  C C   . PRO A 1 42  ? -7.344  -39.542 52.835 1.00 20.37 ? 42   PRO A C   1 
ATOM   269  O O   . PRO A 1 42  ? -7.917  -39.526 53.917 1.00 21.64 ? 42   PRO A O   1 
ATOM   270  C CB  . PRO A 1 42  ? -6.750  -37.123 52.646 1.00 20.16 ? 42   PRO A CB  1 
ATOM   271  C CG  . PRO A 1 42  ? -7.596  -35.975 52.350 1.00 21.90 ? 42   PRO A CG  1 
ATOM   272  C CD  . PRO A 1 42  ? -9.003  -36.529 52.167 1.00 19.82 ? 42   PRO A CD  1 
ATOM   273  N N   . TRP A 1 43  ? -6.635  -40.582 52.423 1.00 21.44 ? 43   TRP A N   1 
ATOM   274  C CA  . TRP A 1 43  ? -6.440  -41.754 53.279 1.00 21.53 ? 43   TRP A CA  1 
ATOM   275  C C   . TRP A 1 43  ? -5.496  -41.434 54.445 1.00 20.27 ? 43   TRP A C   1 
ATOM   276  O O   . TRP A 1 43  ? -5.625  -41.962 55.546 1.00 21.06 ? 43   TRP A O   1 
ATOM   277  C CB  . TRP A 1 43  ? -5.857  -42.874 52.414 1.00 22.95 ? 43   TRP A CB  1 
ATOM   278  C CG  . TRP A 1 43  ? -6.843  -43.509 51.490 1.00 25.00 ? 43   TRP A CG  1 
ATOM   279  C CD1 . TRP A 1 43  ? -8.139  -43.104 51.243 1.00 26.30 ? 43   TRP A CD1 1 
ATOM   280  C CD2 . TRP A 1 43  ? -6.618  -44.655 50.657 1.00 26.89 ? 43   TRP A CD2 1 
ATOM   281  N NE1 . TRP A 1 43  ? -8.731  -43.948 50.342 1.00 26.51 ? 43   TRP A NE1 1 
ATOM   282  C CE2 . TRP A 1 43  ? -7.828  -44.907 49.963 1.00 26.67 ? 43   TRP A CE2 1 
ATOM   283  C CE3 . TRP A 1 43  ? -5.525  -45.515 50.458 1.00 27.01 ? 43   TRP A CE3 1 
ATOM   284  C CZ2 . TRP A 1 43  ? -7.969  -45.958 49.053 1.00 26.44 ? 43   TRP A CZ2 1 
ATOM   285  C CZ3 . TRP A 1 43  ? -5.660  -46.568 49.550 1.00 27.22 ? 43   TRP A CZ3 1 
ATOM   286  C CH2 . TRP A 1 43  ? -6.895  -46.787 48.867 1.00 26.90 ? 43   TRP A CH2 1 
ATOM   287  N N   . CYS A 1 44  ? -4.538  -40.566 54.189 1.00 19.65 ? 44   CYS A N   1 
ATOM   288  C CA  . CYS A 1 44  ? -3.589  -40.144 55.211 1.00 18.55 ? 44   CYS A CA  1 
ATOM   289  C C   . CYS A 1 44  ? -3.729  -38.626 55.432 1.00 17.98 ? 44   CYS A C   1 
ATOM   290  O O   . CYS A 1 44  ? -3.629  -37.827 54.485 1.00 17.07 ? 44   CYS A O   1 
ATOM   291  C CB  . CYS A 1 44  ? -2.179  -40.534 54.814 1.00 19.17 ? 44   CYS A CB  1 
ATOM   292  S SG  . CYS A 1 44  ? -0.976  -39.912 55.963 1.00 21.42 ? 44   CYS A SG  1 
ATOM   293  N N   . TYR A 1 45  ? -3.974  -38.248 56.675 1.00 17.53 ? 45   TYR A N   1 
ATOM   294  C CA  . TYR A 1 45  ? -4.298  -36.859 57.012 1.00 19.04 ? 45   TYR A CA  1 
ATOM   295  C C   . TYR A 1 45  ? -3.703  -36.450 58.347 1.00 19.32 ? 45   TYR A C   1 
ATOM   296  O O   . TYR A 1 45  ? -3.386  -37.304 59.170 1.00 19.99 ? 45   TYR A O   1 
ATOM   297  C CB  . TYR A 1 45  ? -5.829  -36.670 57.012 1.00 18.88 ? 45   TYR A CB  1 
ATOM   298  C CG  . TYR A 1 45  ? -6.575  -37.539 57.997 1.00 20.65 ? 45   TYR A CG  1 
ATOM   299  C CD1 . TYR A 1 45  ? -6.947  -37.046 59.249 1.00 21.59 ? 45   TYR A CD1 1 
ATOM   300  C CD2 . TYR A 1 45  ? -6.918  -38.862 57.677 1.00 22.76 ? 45   TYR A CD2 1 
ATOM   301  C CE1 . TYR A 1 45  ? -7.636  -37.838 60.148 1.00 23.53 ? 45   TYR A CE1 1 
ATOM   302  C CE2 . TYR A 1 45  ? -7.591  -39.648 58.566 1.00 23.16 ? 45   TYR A CE2 1 
ATOM   303  C CZ  . TYR A 1 45  ? -7.955  -39.129 59.800 1.00 23.93 ? 45   TYR A CZ  1 
ATOM   304  O OH  . TYR A 1 45  ? -8.633  -39.940 60.687 1.00 26.67 ? 45   TYR A OH  1 
ATOM   305  N N   . TYR A 1 46  ? -3.484  -35.149 58.528 1.00 19.87 ? 46   TYR A N   1 
ATOM   306  C CA  . TYR A 1 46  ? -2.765  -34.649 59.678 1.00 21.85 ? 46   TYR A CA  1 
ATOM   307  C C   . TYR A 1 46  ? -3.526  -34.863 60.969 1.00 23.85 ? 46   TYR A C   1 
ATOM   308  O O   . TYR A 1 46  ? -4.769  -34.782 61.008 1.00 23.42 ? 46   TYR A O   1 
ATOM   309  C CB  . TYR A 1 46  ? -2.392  -33.177 59.527 1.00 21.52 ? 46   TYR A CB  1 
ATOM   310  C CG  . TYR A 1 46  ? -1.389  -32.913 58.458 1.00 22.26 ? 46   TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 46  ? -0.012  -33.168 58.669 1.00 21.82 ? 46   TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 46  ? -1.775  -32.380 57.245 1.00 19.80 ? 46   TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 46  ? 0.925   -32.907 57.676 1.00 21.92 ? 46   TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 46  ? -0.834  -32.135 56.240 1.00 20.85 ? 46   TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 46  ? 0.501   -32.400 56.470 1.00 22.18 ? 46   TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 46  ? 1.419   -32.163 55.473 1.00 22.23 ? 46   TYR A OH  1 
ATOM   317  N N   . SER A 1 47  ? -2.772  -35.188 62.019 1.00 26.27 ? 47   SER A N   1 
ATOM   318  C CA  . SER A 1 47  ? -3.359  -35.331 63.345 1.00 30.10 ? 47   SER A CA  1 
ATOM   319  C C   . SER A 1 47  ? -3.618  -33.978 63.991 1.00 32.79 ? 47   SER A C   1 
ATOM   320  O O   . SER A 1 47  ? -3.219  -32.929 63.464 1.00 32.42 ? 47   SER A O   1 
ATOM   321  C CB  . SER A 1 47  ? -2.472  -36.187 64.249 1.00 29.55 ? 47   SER A CB  1 
ATOM   322  O OG  . SER A 1 47  ? -1.196  -35.570 64.401 1.00 30.13 ? 47   SER A OG  1 
ATOM   323  N N   . LYS A 1 48  ? -4.253  -34.041 65.163 1.00 36.55 ? 48   LYS A N   1 
ATOM   324  C CA  . LYS A 1 48  ? -4.766  -32.892 65.920 1.00 40.05 ? 48   LYS A CA  1 
ATOM   325  C C   . LYS A 1 48  ? -3.700  -31.959 66.477 1.00 41.50 ? 48   LYS A C   1 
ATOM   326  O O   . LYS A 1 48  ? -4.018  -30.834 66.881 1.00 42.45 ? 48   LYS A O   1 
ATOM   327  C CB  . LYS A 1 48  ? -5.628  -33.391 67.085 1.00 40.27 ? 48   LYS A CB  1 
ATOM   328  C CG  . LYS A 1 48  ? -7.120  -33.486 66.797 1.00 42.50 ? 48   LYS A CG  1 
ATOM   329  C CD  . LYS A 1 48  ? -7.783  -34.596 67.631 1.00 45.51 ? 48   LYS A CD  1 
ATOM   330  C CE  . LYS A 1 48  ? -7.622  -34.398 69.149 1.00 47.27 ? 48   LYS A CE  1 
ATOM   331  N NZ  . LYS A 1 48  ? -8.699  -33.529 69.750 1.00 48.90 ? 48   LYS A NZ  1 
ATOM   332  N N   . ASN A 1 49  ? -2.453  -32.429 66.506 1.00 43.07 ? 49   ASN A N   1 
ATOM   333  C CA  . ASN A 1 49  ? -1.343  -31.658 67.027 1.00 44.82 ? 49   ASN A CA  1 
ATOM   334  C C   . ASN A 1 49  ? -0.089  -32.047 66.246 1.00 45.19 ? 49   ASN A C   1 
ATOM   335  O O   . ASN A 1 49  ? 0.645   -32.946 66.645 1.00 46.42 ? 49   ASN A O   1 
ATOM   336  C CB  . ASN A 1 49  ? -1.171  -31.966 68.526 1.00 45.37 ? 49   ASN A CB  1 
ATOM   337  C CG  . ASN A 1 49  ? -1.300  -30.729 69.408 1.00 47.02 ? 49   ASN A CG  1 
ATOM   338  O OD1 . ASN A 1 49  ? -0.384  -29.904 69.497 1.00 48.16 ? 49   ASN A OD1 1 
ATOM   339  N ND2 . ASN A 1 49  ? -2.442  -30.610 70.087 1.00 48.65 ? 49   ASN A ND2 1 
ATOM   340  N N   . HIS A 1 50  ? 0.133   -31.406 65.104 1.00 45.38 ? 50   HIS A N   1 
ATOM   341  C CA  . HIS A 1 50  ? 1.283   -31.734 64.254 1.00 44.91 ? 50   HIS A CA  1 
ATOM   342  C C   . HIS A 1 50  ? 2.352   -30.633 64.289 1.00 43.57 ? 50   HIS A C   1 
ATOM   343  O O   . HIS A 1 50  ? 3.548   -30.898 64.070 1.00 44.23 ? 50   HIS A O   1 
ATOM   344  C CB  . HIS A 1 50  ? 0.839   -31.988 62.792 1.00 45.97 ? 50   HIS A CB  1 
ATOM   345  C CG  . HIS A 1 50  ? 1.955   -32.411 61.875 1.00 47.83 ? 50   HIS A CG  1 
ATOM   346  N ND1 . HIS A 1 50  ? 2.334   -33.730 61.713 1.00 49.88 ? 50   HIS A ND1 1 
ATOM   347  C CD2 . HIS A 1 50  ? 2.773   -31.687 61.072 1.00 48.95 ? 50   HIS A CD2 1 
ATOM   348  C CE1 . HIS A 1 50  ? 3.341   -33.797 60.859 1.00 49.99 ? 50   HIS A CE1 1 
ATOM   349  N NE2 . HIS A 1 50  ? 3.622   -32.572 60.448 1.00 49.49 ? 50   HIS A NE2 1 
ATOM   350  N N   . SER A 1 51  ? 1.927   -29.404 64.586 1.00 40.51 ? 51   SER A N   1 
ATOM   351  C CA  . SER A 1 51  ? 2.621   -28.264 64.008 1.00 37.42 ? 51   SER A CA  1 
ATOM   352  C C   . SER A 1 51  ? 3.425   -27.355 64.949 1.00 34.87 ? 51   SER A C   1 
ATOM   353  O O   . SER A 1 51  ? 4.560   -27.679 65.310 1.00 35.89 ? 51   SER A O   1 
ATOM   354  C CB  . SER A 1 51  ? 1.670   -27.457 63.095 1.00 37.92 ? 51   SER A CB  1 
ATOM   355  O OG  . SER A 1 51  ? 0.684   -26.746 63.818 1.00 36.64 ? 51   SER A OG  1 
ATOM   356  N N   . TYR A 1 52  ? 2.858   -26.200 65.279 1.00 30.00 ? 52   TYR A N   1 
ATOM   357  C CA  . TYR A 1 52  ? 3.542   -25.164 66.045 1.00 26.09 ? 52   TYR A CA  1 
ATOM   358  C C   . TYR A 1 52  ? 2.722   -24.832 67.258 1.00 24.65 ? 52   TYR A C   1 
ATOM   359  O O   . TYR A 1 52  ? 1.509   -25.041 67.266 1.00 23.87 ? 52   TYR A O   1 
ATOM   360  C CB  . TYR A 1 52  ? 3.699   -23.902 65.191 1.00 24.78 ? 52   TYR A CB  1 
ATOM   361  C CG  . TYR A 1 52  ? 4.816   -24.013 64.202 1.00 22.03 ? 52   TYR A CG  1 
ATOM   362  C CD1 . TYR A 1 52  ? 4.642   -24.665 62.982 1.00 20.75 ? 52   TYR A CD1 1 
ATOM   363  C CD2 . TYR A 1 52  ? 6.068   -23.467 64.481 1.00 21.21 ? 52   TYR A CD2 1 
ATOM   364  C CE1 . TYR A 1 52  ? 5.696   -24.764 62.052 1.00 21.65 ? 52   TYR A CE1 1 
ATOM   365  C CE2 . TYR A 1 52  ? 7.137   -23.586 63.562 1.00 22.79 ? 52   TYR A CE2 1 
ATOM   366  C CZ  . TYR A 1 52  ? 6.939   -24.230 62.367 1.00 23.56 ? 52   TYR A CZ  1 
ATOM   367  O OH  . TYR A 1 52  ? 7.987   -24.337 61.472 1.00 23.79 ? 52   TYR A OH  1 
ATOM   368  N N   . HIS A 1 53  ? 3.382   -24.339 68.293 1.00 23.66 ? 53   HIS A N   1 
ATOM   369  C CA  . HIS A 1 53  ? 2.683   -23.777 69.433 1.00 23.34 ? 53   HIS A CA  1 
ATOM   370  C C   . HIS A 1 53  ? 3.206   -22.392 69.689 1.00 22.32 ? 53   HIS A C   1 
ATOM   371  O O   . HIS A 1 53  ? 4.338   -22.061 69.347 1.00 20.43 ? 53   HIS A O   1 
ATOM   372  C CB  . HIS A 1 53  ? 2.790   -24.649 70.690 1.00 24.23 ? 53   HIS A CB  1 
ATOM   373  C CG  . HIS A 1 53  ? 4.194   -24.912 71.131 1.00 26.78 ? 53   HIS A CG  1 
ATOM   374  N ND1 . HIS A 1 53  ? 4.810   -24.190 72.132 1.00 32.46 ? 53   HIS A ND1 1 
ATOM   375  C CD2 . HIS A 1 53  ? 5.106   -25.810 70.701 1.00 29.44 ? 53   HIS A CD2 1 
ATOM   376  C CE1 . HIS A 1 53  ? 6.045   -24.631 72.296 1.00 30.35 ? 53   HIS A CE1 1 
ATOM   377  N NE2 . HIS A 1 53  ? 6.254   -25.607 71.433 1.00 30.52 ? 53   HIS A NE2 1 
ATOM   378  N N   . VAL A 1 54  ? 2.365   -21.555 70.276 1.00 20.84 ? 54   VAL A N   1 
ATOM   379  C CA  . VAL A 1 54  ? 2.813   -20.240 70.684 1.00 20.58 ? 54   VAL A CA  1 
ATOM   380  C C   . VAL A 1 54  ? 3.689   -20.420 71.915 1.00 21.06 ? 54   VAL A C   1 
ATOM   381  O O   . VAL A 1 54  ? 3.300   -21.102 72.863 1.00 21.11 ? 54   VAL A O   1 
ATOM   382  C CB  . VAL A 1 54  ? 1.608   -19.322 70.987 1.00 20.16 ? 54   VAL A CB  1 
ATOM   383  C CG1 . VAL A 1 54  ? 2.046   -18.034 71.664 1.00 20.32 ? 54   VAL A CG1 1 
ATOM   384  C CG2 . VAL A 1 54  ? 0.878   -19.012 69.664 1.00 20.54 ? 54   VAL A CG2 1 
ATOM   385  N N   . GLU A 1 55  ? 4.873   -19.818 71.873 1.00 21.92 ? 55   GLU A N   1 
ATOM   386  C CA  . GLU A 1 55  ? 5.775   -19.766 73.002 1.00 24.54 ? 55   GLU A CA  1 
ATOM   387  C C   . GLU A 1 55  ? 5.639   -18.418 73.729 1.00 23.98 ? 55   GLU A C   1 
ATOM   388  O O   . GLU A 1 55  ? 5.926   -17.345 73.162 1.00 24.79 ? 55   GLU A O   1 
ATOM   389  C CB  . GLU A 1 55  ? 7.214   -19.976 72.516 1.00 25.41 ? 55   GLU A CB  1 
ATOM   390  C CG  . GLU A 1 55  ? 8.270   -20.086 73.623 1.00 32.14 ? 55   GLU A CG  1 
ATOM   391  C CD  . GLU A 1 55  ? 8.167   -21.378 74.440 1.00 38.89 ? 55   GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 55  ? 7.911   -22.465 73.866 1.00 42.94 ? 55   GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 55  ? 8.363   -21.309 75.671 1.00 43.85 ? 55   GLU A OE2 1 
ATOM   394  N N   . GLY A 1 56  ? 5.185   -18.474 74.977 1.00 23.13 ? 56   GLY A N   1 
ATOM   395  C CA  . GLY A 1 56  ? 5.135   -17.287 75.797 1.00 22.97 ? 56   GLY A CA  1 
ATOM   396  C C   . GLY A 1 56  ? 3.960   -16.402 75.421 1.00 22.17 ? 56   GLY A C   1 
ATOM   397  O O   . GLY A 1 56  ? 2.950   -16.895 74.907 1.00 22.43 ? 56   GLY A O   1 
ATOM   398  N N   . ASN A 1 57  ? 4.078   -15.113 75.689 1.00 21.00 ? 57   ASN A N   1 
ATOM   399  C CA  . ASN A 1 57  ? 2.942   -14.196 75.474 1.00 21.22 ? 57   ASN A CA  1 
ATOM   400  C C   . ASN A 1 57  ? 3.026   -13.526 74.130 1.00 20.22 ? 57   ASN A C   1 
ATOM   401  O O   . ASN A 1 57  ? 4.119   -13.313 73.571 1.00 19.29 ? 57   ASN A O   1 
ATOM   402  C CB  . ASN A 1 57  ? 2.845   -13.129 76.570 1.00 21.19 ? 57   ASN A CB  1 
ATOM   403  C CG  . ASN A 1 57  ? 2.608   -13.718 77.942 1.00 21.63 ? 57   ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 57  ? 2.051   -14.788 78.075 1.00 20.77 ? 57   ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 57  ? 3.035   -13.006 78.969 1.00 24.71 ? 57   ASN A ND2 1 
ATOM   406  N N   . LEU A 1 58  ? 1.862   -13.186 73.601 1.00 18.02 ? 58   LEU A N   1 
ATOM   407  C CA  . LEU A 1 58  ? 1.781   -12.252 72.506 1.00 17.88 ? 58   LEU A CA  1 
ATOM   408  C C   . LEU A 1 58  ? 2.203   -10.892 73.001 1.00 17.21 ? 58   LEU A C   1 
ATOM   409  O O   . LEU A 1 58  ? 2.002   -10.550 74.169 1.00 18.02 ? 58   LEU A O   1 
ATOM   410  C CB  . LEU A 1 58  ? 0.329   -12.170 71.920 1.00 17.64 ? 58   LEU A CB  1 
ATOM   411  C CG  . LEU A 1 58  ? -0.045  -13.218 70.860 1.00 18.38 ? 58   LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 58  ? 0.290   -14.615 71.328 1.00 17.05 ? 58   LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 58  ? -1.555  -13.172 70.489 1.00 18.37 ? 58   LEU A CD2 1 
ATOM   414  N N   . VAL A 1 59  ? 2.776   -10.109 72.105 1.00 17.89 ? 59   VAL A N   1 
ATOM   415  C CA  . VAL A 1 59  ? 3.210   -8.761  72.413 1.00 19.06 ? 59   VAL A CA  1 
ATOM   416  C C   . VAL A 1 59  ? 2.440   -7.747  71.590 1.00 18.50 ? 59   VAL A C   1 
ATOM   417  O O   . VAL A 1 59  ? 2.475   -7.785  70.369 1.00 18.35 ? 59   VAL A O   1 
ATOM   418  C CB  . VAL A 1 59  ? 4.704   -8.595  72.048 1.00 19.10 ? 59   VAL A CB  1 
ATOM   419  C CG1 . VAL A 1 59  ? 5.206   -7.235  72.491 1.00 21.58 ? 59   VAL A CG1 1 
ATOM   420  C CG2 . VAL A 1 59  ? 5.498   -9.712  72.691 1.00 22.34 ? 59   VAL A CG2 1 
ATOM   421  N N   . ASN A 1 60  ? 1.777   -6.808  72.254 1.00 19.43 ? 60   ASN A N   1 
ATOM   422  C CA  . ASN A 1 60  ? 1.241   -5.639  71.555 1.00 19.36 ? 60   ASN A CA  1 
ATOM   423  C C   . ASN A 1 60  ? 2.274   -4.749  70.898 1.00 20.09 ? 60   ASN A C   1 
ATOM   424  O O   . ASN A 1 60  ? 3.285   -4.386  71.502 1.00 20.50 ? 60   ASN A O   1 
ATOM   425  C CB  . ASN A 1 60  ? 0.410   -4.772  72.492 1.00 20.41 ? 60   ASN A CB  1 
ATOM   426  C CG  . ASN A 1 60  ? -0.833  -5.479  72.953 1.00 19.85 ? 60   ASN A CG  1 
ATOM   427  O OD1 . ASN A 1 60  ? -1.860  -5.510  72.253 1.00 26.04 ? 60   ASN A OD1 1 
ATOM   428  N ND2 . ASN A 1 60  ? -0.756  -6.060  74.111 1.00 21.67 ? 60   ASN A ND2 1 
ATOM   429  N N   . THR A 1 61  ? 1.998   -4.388  69.654 1.00 18.54 ? 61   THR A N   1 
ATOM   430  C CA  . THR A 1 61  ? 2.818   -3.459  68.913 1.00 18.86 ? 61   THR A CA  1 
ATOM   431  C C   . THR A 1 61  ? 1.897   -2.290  68.551 1.00 19.30 ? 61   THR A C   1 
ATOM   432  O O   . THR A 1 61  ? 0.688   -2.398  68.745 1.00 19.22 ? 61   THR A O   1 
ATOM   433  C CB  . THR A 1 61  ? 3.329   -4.091  67.645 1.00 18.92 ? 61   THR A CB  1 
ATOM   434  O OG1 . THR A 1 61  ? 2.218   -4.418  66.785 1.00 20.70 ? 61   THR A OG1 1 
ATOM   435  C CG2 . THR A 1 61  ? 4.184   -5.372  67.921 1.00 19.00 ? 61   THR A CG2 1 
ATOM   436  N N   . ASN A 1 62  ? 2.439   -1.204  68.012 1.00 19.85 ? 62   ASN A N   1 
ATOM   437  C CA  . ASN A 1 62  ? 1.573   -0.103  67.553 1.00 21.49 ? 62   ASN A CA  1 
ATOM   438  C C   . ASN A 1 62  ? 0.548   -0.526  66.492 1.00 20.35 ? 62   ASN A C   1 
ATOM   439  O O   . ASN A 1 62  ? -0.563  -0.022  66.482 1.00 20.20 ? 62   ASN A O   1 
ATOM   440  C CB  . ASN A 1 62  ? 2.389   1.071   67.036 1.00 22.27 ? 62   ASN A CB  1 
ATOM   441  C CG  . ASN A 1 62  ? 3.130   1.802   68.154 1.00 26.71 ? 62   ASN A CG  1 
ATOM   442  O OD1 . ASN A 1 62  ? 4.246   2.275   67.951 1.00 31.20 ? 62   ASN A OD1 1 
ATOM   443  N ND2 . ASN A 1 62  ? 2.515   1.894   69.324 1.00 26.05 ? 62   ASN A ND2 1 
ATOM   444  N N   . ALA A 1 63  ? 0.947   -1.442  65.608 1.00 19.17 ? 63   ALA A N   1 
ATOM   445  C CA  . ALA A 1 63  ? 0.102   -1.929  64.489 1.00 19.04 ? 63   ALA A CA  1 
ATOM   446  C C   . ALA A 1 63  ? -0.851  -3.082  64.826 1.00 18.37 ? 63   ALA A C   1 
ATOM   447  O O   . ALA A 1 63  ? -1.855  -3.279  64.149 1.00 19.32 ? 63   ALA A O   1 
ATOM   448  C CB  . ALA A 1 63  ? 1.000   -2.306  63.295 1.00 19.52 ? 63   ALA A CB  1 
ATOM   449  N N   . GLY A 1 64  ? -0.534  -3.853  65.854 1.00 17.57 ? 64   GLY A N   1 
ATOM   450  C CA  . GLY A 1 64  ? -1.265  -5.075  66.183 1.00 17.63 ? 64   GLY A CA  1 
ATOM   451  C C   . GLY A 1 64  ? -0.555  -5.880  67.268 1.00 17.22 ? 64   GLY A C   1 
ATOM   452  O O   . GLY A 1 64  ? -0.537  -5.490  68.431 1.00 16.11 ? 64   GLY A O   1 
ATOM   453  N N   . PHE A 1 65  ? 0.038   -7.007  66.889 1.00 16.90 ? 65   PHE A N   1 
ATOM   454  C CA  . PHE A 1 65  ? 0.736   -7.858  67.862 1.00 17.39 ? 65   PHE A CA  1 
ATOM   455  C C   . PHE A 1 65  ? 1.714   -8.785  67.152 1.00 17.59 ? 65   PHE A C   1 
ATOM   456  O O   . PHE A 1 65  ? 1.624   -8.986  65.937 1.00 16.63 ? 65   PHE A O   1 
ATOM   457  C CB  . PHE A 1 65  ? -0.250  -8.686  68.719 1.00 17.92 ? 65   PHE A CB  1 
ATOM   458  C CG  . PHE A 1 65  ? -1.056  -9.682  67.926 1.00 20.12 ? 65   PHE A CG  1 
ATOM   459  C CD1 . PHE A 1 65  ? -0.540  -10.961 67.648 1.00 18.87 ? 65   PHE A CD1 1 
ATOM   460  C CD2 . PHE A 1 65  ? -2.351  -9.340  67.461 1.00 22.34 ? 65   PHE A CD2 1 
ATOM   461  C CE1 . PHE A 1 65  ? -1.265  -11.879 66.912 1.00 20.51 ? 65   PHE A CE1 1 
ATOM   462  C CE2 . PHE A 1 65  ? -3.100  -10.253 66.739 1.00 20.64 ? 65   PHE A CE2 1 
ATOM   463  C CZ  . PHE A 1 65  ? -2.552  -11.525 66.450 1.00 18.37 ? 65   PHE A CZ  1 
ATOM   464  N N   . THR A 1 66  ? 2.669   -9.316  67.914 1.00 17.53 ? 66   THR A N   1 
ATOM   465  C CA  . THR A 1 66  ? 3.547   -10.391 67.422 1.00 17.83 ? 66   THR A CA  1 
ATOM   466  C C   . THR A 1 66  ? 3.452   -11.581 68.381 1.00 17.25 ? 66   THR A C   1 
ATOM   467  O O   . THR A 1 66  ? 3.082   -11.426 69.553 1.00 17.85 ? 66   THR A O   1 
ATOM   468  C CB  . THR A 1 66  ? 5.023   -9.912  67.253 1.00 18.65 ? 66   THR A CB  1 
ATOM   469  O OG1 . THR A 1 66  ? 5.482   -9.323  68.467 1.00 19.33 ? 66   THR A OG1 1 
ATOM   470  C CG2 . THR A 1 66  ? 5.175   -8.888  66.129 1.00 18.44 ? 66   THR A CG2 1 
ATOM   471  N N   . ALA A 1 67  ? 3.781   -12.773 67.876 1.00 16.68 ? 67   ALA A N   1 
ATOM   472  C CA  . ALA A 1 67  ? 3.811   -13.992 68.634 1.00 17.33 ? 67   ALA A CA  1 
ATOM   473  C C   . ALA A 1 67  ? 4.996   -14.791 68.117 1.00 18.27 ? 67   ALA A C   1 
ATOM   474  O O   . ALA A 1 67  ? 5.313   -14.773 66.913 1.00 18.76 ? 67   ALA A O   1 
ATOM   475  C CB  . ALA A 1 67  ? 2.558   -14.801 68.386 1.00 17.16 ? 67   ALA A CB  1 
ATOM   476  N N   . ARG A 1 68  ? 5.658   -15.459 69.032 1.00 18.27 ? 68   ARG A N   1 
ATOM   477  C CA  . ARG A 1 68  ? 6.685   -16.433 68.638 1.00 19.80 ? 68   ARG A CA  1 
ATOM   478  C C   . ARG A 1 68  ? 6.062   -17.785 68.614 1.00 19.65 ? 68   ARG A C   1 
ATOM   479  O O   . ARG A 1 68  ? 5.397   -18.163 69.581 1.00 19.91 ? 68   ARG A O   1 
ATOM   480  C CB  . ARG A 1 68  ? 7.808   -16.421 69.654 1.00 20.05 ? 68   ARG A CB  1 
ATOM   481  C CG  . ARG A 1 68  ? 8.565   -15.149 69.663 1.00 25.05 ? 68   ARG A CG  1 
ATOM   482  C CD  . ARG A 1 68  ? 9.717   -15.315 70.674 1.00 33.67 ? 68   ARG A CD  1 
ATOM   483  N NE  . ARG A 1 68  ? 10.520  -14.112 70.852 1.00 41.87 ? 68   ARG A NE  1 
ATOM   484  C CZ  . ARG A 1 68  ? 11.353  -13.920 71.878 1.00 46.51 ? 68   ARG A CZ  1 
ATOM   485  N NH1 . ARG A 1 68  ? 11.472  -14.844 72.832 1.00 47.33 ? 68   ARG A NH1 1 
ATOM   486  N NH2 . ARG A 1 68  ? 12.063  -12.799 71.960 1.00 47.92 ? 68   ARG A NH2 1 
ATOM   487  N N   . LEU A 1 69  ? 6.259   -18.506 67.508 1.00 18.83 ? 69   LEU A N   1 
ATOM   488  C CA  . LEU A 1 69  ? 5.769   -19.832 67.358 1.00 20.28 ? 69   LEU A CA  1 
ATOM   489  C C   . LEU A 1 69  ? 6.963   -20.780 67.400 1.00 22.62 ? 69   LEU A C   1 
ATOM   490  O O   . LEU A 1 69  ? 8.006   -20.512 66.786 1.00 22.00 ? 69   LEU A O   1 
ATOM   491  C CB  . LEU A 1 69  ? 5.026   -19.991 66.024 1.00 19.88 ? 69   LEU A CB  1 
ATOM   492  C CG  . LEU A 1 69  ? 3.931   -18.992 65.668 1.00 20.73 ? 69   LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 69  ? 3.177   -19.505 64.441 1.00 18.51 ? 69   LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 69  ? 3.025   -18.762 66.850 1.00 23.85 ? 69   LEU A CD2 1 
ATOM   495  N N   . LYS A 1 70  ? 6.806   -21.866 68.133 1.00 24.50 ? 70   LYS A N   1 
ATOM   496  C CA  . LYS A 1 70  ? 7.892   -22.829 68.261 1.00 27.87 ? 70   LYS A CA  1 
ATOM   497  C C   . LYS A 1 70  ? 7.451   -24.138 67.654 1.00 28.87 ? 70   LYS A C   1 
ATOM   498  O O   . LYS A 1 70  ? 6.348   -24.625 67.907 1.00 27.77 ? 70   LYS A O   1 
ATOM   499  C CB  . LYS A 1 70  ? 8.269   -22.964 69.744 1.00 27.92 ? 70   LYS A CB  1 
ATOM   500  C CG  . LYS A 1 70  ? 9.523   -23.733 70.083 1.00 32.78 ? 70   LYS A CG  1 
ATOM   501  C CD  . LYS A 1 70  ? 9.910   -23.353 71.529 1.00 36.19 ? 70   LYS A CD  1 
ATOM   502  C CE  . LYS A 1 70  ? 11.125  -24.111 72.062 1.00 40.69 ? 70   LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 70  ? 11.428  -23.632 73.443 1.00 39.68 ? 70   LYS A NZ  1 
ATOM   504  N N   . ASN A 1 71  ? 8.327   -24.702 66.834 1.00 31.65 ? 71   ASN A N   1 
ATOM   505  C CA  . ASN A 1 71  ? 8.076   -25.982 66.205 1.00 35.24 ? 71   ASN A CA  1 
ATOM   506  C C   . ASN A 1 71  ? 8.005   -27.106 67.246 1.00 37.49 ? 71   ASN A C   1 
ATOM   507  O O   . ASN A 1 71  ? 8.911   -27.256 68.062 1.00 38.20 ? 71   ASN A O   1 
ATOM   508  C CB  . ASN A 1 71  ? 9.175   -26.250 65.162 1.00 34.87 ? 71   ASN A CB  1 
ATOM   509  C CG  . ASN A 1 71  ? 8.923   -27.481 64.354 1.00 36.65 ? 71   ASN A CG  1 
ATOM   510  O OD1 . ASN A 1 71  ? 7.828   -27.683 63.810 1.00 36.18 ? 71   ASN A OD1 1 
ATOM   511  N ND2 . ASN A 1 71  ? 9.949   -28.336 64.262 1.00 38.77 ? 71   ASN A ND2 1 
ATOM   512  N N   . LEU A 1 72  ? 6.901   -27.849 67.235 1.00 40.71 ? 72   LEU A N   1 
ATOM   513  C CA  . LEU A 1 72  ? 6.805   -29.129 67.944 1.00 43.43 ? 72   LEU A CA  1 
ATOM   514  C C   . LEU A 1 72  ? 7.576   -30.200 67.148 1.00 45.14 ? 72   LEU A C   1 
ATOM   515  O O   . LEU A 1 72  ? 7.487   -30.233 65.923 1.00 45.58 ? 72   LEU A O   1 
ATOM   516  C CB  . LEU A 1 72  ? 5.340   -29.578 68.066 1.00 43.58 ? 72   LEU A CB  1 
ATOM   517  C CG  . LEU A 1 72  ? 4.317   -29.170 69.139 1.00 43.53 ? 72   LEU A CG  1 
ATOM   518  C CD1 . LEU A 1 72  ? 4.895   -29.062 70.566 1.00 44.18 ? 72   LEU A CD1 1 
ATOM   519  C CD2 . LEU A 1 72  ? 3.597   -27.915 68.738 1.00 43.92 ? 72   LEU A CD2 1 
ATOM   520  N N   . PRO A 1 73  ? 8.287   -31.110 67.834 1.00 46.80 ? 73   PRO A N   1 
ATOM   521  C CA  . PRO A 1 73  ? 9.102   -32.124 67.132 1.00 48.03 ? 73   PRO A CA  1 
ATOM   522  C C   . PRO A 1 73  ? 8.352   -32.868 66.001 1.00 48.78 ? 73   PRO A C   1 
ATOM   523  O O   . PRO A 1 73  ? 7.252   -33.387 66.228 1.00 48.72 ? 73   PRO A O   1 
ATOM   524  C CB  . PRO A 1 73  ? 9.503   -33.101 68.262 1.00 47.95 ? 73   PRO A CB  1 
ATOM   525  C CG  . PRO A 1 73  ? 8.551   -32.771 69.438 1.00 48.41 ? 73   PRO A CG  1 
ATOM   526  C CD  . PRO A 1 73  ? 8.339   -31.283 69.298 1.00 47.23 ? 73   PRO A CD  1 
ATOM   527  N N   . SER A 1 74  ? 8.933   -32.880 64.796 1.00 49.60 ? 74   SER A N   1 
ATOM   528  C CA  . SER A 1 74  ? 8.356   -33.578 63.624 1.00 50.63 ? 74   SER A CA  1 
ATOM   529  C C   . SER A 1 74  ? 9.398   -33.981 62.573 1.00 50.79 ? 74   SER A C   1 
ATOM   530  O O   . SER A 1 74  ? 10.321  -33.218 62.298 1.00 51.00 ? 74   SER A O   1 
ATOM   531  C CB  . SER A 1 74  ? 7.266   -32.735 62.959 1.00 50.79 ? 74   SER A CB  1 
ATOM   532  O OG  . SER A 1 74  ? 5.987   -33.295 63.206 1.00 52.37 ? 74   SER A OG  1 
ATOM   533  N N   . SER A 1 75  ? 9.229   -35.164 61.970 1.00 51.14 ? 75   SER A N   1 
ATOM   534  C CA  . SER A 1 75  ? 10.217  -35.691 61.005 1.00 51.13 ? 75   SER A CA  1 
ATOM   535  C C   . SER A 1 75  ? 10.244  -34.849 59.717 1.00 50.72 ? 75   SER A C   1 
ATOM   536  O O   . SER A 1 75  ? 9.197   -34.377 59.276 1.00 50.98 ? 75   SER A O   1 
ATOM   537  C CB  . SER A 1 75  ? 10.033  -37.205 60.747 1.00 51.21 ? 75   SER A CB  1 
ATOM   538  O OG  . SER A 1 75  ? 10.994  -37.983 61.488 1.00 51.84 ? 75   SER A OG  1 
ATOM   539  N N   . PRO A 1 76  ? 11.446  -34.625 59.137 1.00 50.11 ? 76   PRO A N   1 
ATOM   540  C CA  . PRO A 1 76  ? 11.504  -33.676 58.036 1.00 49.58 ? 76   PRO A CA  1 
ATOM   541  C C   . PRO A 1 76  ? 11.094  -34.335 56.714 1.00 48.73 ? 76   PRO A C   1 
ATOM   542  O O   . PRO A 1 76  ? 11.841  -35.162 56.172 1.00 49.47 ? 76   PRO A O   1 
ATOM   543  C CB  . PRO A 1 76  ? 12.976  -33.237 58.024 1.00 49.84 ? 76   PRO A CB  1 
ATOM   544  C CG  . PRO A 1 76  ? 13.737  -34.362 58.632 1.00 49.73 ? 76   PRO A CG  1 
ATOM   545  C CD  . PRO A 1 76  ? 12.767  -35.225 59.417 1.00 50.25 ? 76   PRO A CD  1 
ATOM   546  N N   . VAL A 1 77  ? 9.905   -33.986 56.218 1.00 47.19 ? 77   VAL A N   1 
ATOM   547  C CA  . VAL A 1 77  ? 9.382   -34.579 54.985 1.00 45.63 ? 77   VAL A CA  1 
ATOM   548  C C   . VAL A 1 77  ? 9.931   -33.880 53.736 1.00 44.51 ? 77   VAL A C   1 
ATOM   549  O O   . VAL A 1 77  ? 10.498  -34.529 52.840 1.00 44.27 ? 77   VAL A O   1 
ATOM   550  C CB  . VAL A 1 77  ? 7.834   -34.580 54.949 1.00 45.87 ? 77   VAL A CB  1 
ATOM   551  C CG1 . VAL A 1 77  ? 7.344   -35.212 53.666 1.00 45.88 ? 77   VAL A CG1 1 
ATOM   552  C CG2 . VAL A 1 77  ? 7.261   -35.312 56.161 1.00 46.19 ? 77   VAL A CG2 1 
ATOM   553  N N   . PHE A 1 78  ? 9.745   -32.562 53.667 1.00 42.41 ? 78   PHE A N   1 
ATOM   554  C CA  . PHE A 1 78  ? 10.203  -31.793 52.514 1.00 41.22 ? 78   PHE A CA  1 
ATOM   555  C C   . PHE A 1 78  ? 11.365  -30.900 52.910 1.00 41.33 ? 78   PHE A C   1 
ATOM   556  O O   . PHE A 1 78  ? 11.511  -29.768 52.435 1.00 40.89 ? 78   PHE A O   1 
ATOM   557  C CB  . PHE A 1 78  ? 9.048   -31.028 51.882 1.00 39.84 ? 78   PHE A CB  1 
ATOM   558  C CG  . PHE A 1 78  ? 7.917   -31.914 51.472 1.00 38.21 ? 78   PHE A CG  1 
ATOM   559  C CD1 . PHE A 1 78  ? 6.682   -31.816 52.088 1.00 37.11 ? 78   PHE A CD1 1 
ATOM   560  C CD2 . PHE A 1 78  ? 8.104   -32.885 50.501 1.00 36.09 ? 78   PHE A CD2 1 
ATOM   561  C CE1 . PHE A 1 78  ? 5.629   -32.645 51.718 1.00 37.49 ? 78   PHE A CE1 1 
ATOM   562  C CE2 . PHE A 1 78  ? 7.059   -33.731 50.131 1.00 37.48 ? 78   PHE A CE2 1 
ATOM   563  C CZ  . PHE A 1 78  ? 5.822   -33.606 50.738 1.00 37.22 ? 78   PHE A CZ  1 
ATOM   564  N N   . GLY A 1 79  ? 12.188  -31.445 53.802 1.00 41.85 ? 79   GLY A N   1 
ATOM   565  C CA  . GLY A 1 79  ? 13.454  -30.846 54.167 1.00 42.28 ? 79   GLY A CA  1 
ATOM   566  C C   . GLY A 1 79  ? 13.428  -29.881 55.329 1.00 42.44 ? 79   GLY A C   1 
ATOM   567  O O   . GLY A 1 79  ? 12.690  -30.071 56.304 1.00 42.81 ? 79   GLY A O   1 
ATOM   568  N N   . SER A 1 80  ? 14.242  -28.834 55.180 1.00 42.73 ? 80   SER A N   1 
ATOM   569  C CA  . SER A 1 80  ? 14.712  -27.982 56.270 1.00 42.06 ? 80   SER A CA  1 
ATOM   570  C C   . SER A 1 80  ? 13.625  -27.131 56.939 1.00 41.14 ? 80   SER A C   1 
ATOM   571  O O   . SER A 1 80  ? 13.320  -26.021 56.498 1.00 40.46 ? 80   SER A O   1 
ATOM   572  C CB  . SER A 1 80  ? 15.879  -27.119 55.781 1.00 42.73 ? 80   SER A CB  1 
ATOM   573  O OG  . SER A 1 80  ? 16.887  -27.939 55.198 1.00 44.60 ? 80   SER A OG  1 
ATOM   574  N N   . ASN A 1 81  ? 13.089  -27.689 58.023 1.00 39.52 ? 81   ASN A N   1 
ATOM   575  C CA  . ASN A 1 81  ? 12.019  -27.127 58.827 1.00 38.30 ? 81   ASN A CA  1 
ATOM   576  C C   . ASN A 1 81  ? 12.407  -25.852 59.605 1.00 37.38 ? 81   ASN A C   1 
ATOM   577  O O   . ASN A 1 81  ? 13.573  -25.668 59.952 1.00 37.25 ? 81   ASN A O   1 
ATOM   578  C CB  . ASN A 1 81  ? 11.557  -28.204 59.787 1.00 38.85 ? 81   ASN A CB  1 
ATOM   579  C CG  . ASN A 1 81  ? 10.147  -28.003 60.243 1.00 40.29 ? 81   ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 81  ? 9.819   -26.987 60.842 1.00 42.46 ? 81   ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 81  ? 9.292   -28.988 59.976 1.00 44.35 ? 81   ASN A ND2 1 
ATOM   582  N N   . VAL A 1 82  ? 11.445  -24.963 59.869 1.00 35.11 ? 82   VAL A N   1 
ATOM   583  C CA  . VAL A 1 82  ? 11.774  -23.693 60.536 1.00 33.02 ? 82   VAL A CA  1 
ATOM   584  C C   . VAL A 1 82  ? 11.378  -23.760 62.003 1.00 32.78 ? 82   VAL A C   1 
ATOM   585  O O   . VAL A 1 82  ? 10.188  -23.844 62.327 1.00 32.91 ? 82   VAL A O   1 
ATOM   586  C CB  . VAL A 1 82  ? 11.180  -22.465 59.777 1.00 33.34 ? 82   VAL A CB  1 
ATOM   587  C CG1 . VAL A 1 82  ? 11.285  -21.201 60.588 1.00 32.53 ? 82   VAL A CG1 1 
ATOM   588  C CG2 . VAL A 1 82  ? 11.872  -22.301 58.431 1.00 31.69 ? 82   VAL A CG2 1 
ATOM   589  N N   . ASP A 1 83  ? 12.382  -23.756 62.883 1.00 31.57 ? 83   ASP A N   1 
ATOM   590  C CA  . ASP A 1 83  ? 12.178  -24.015 64.320 1.00 32.13 ? 83   ASP A CA  1 
ATOM   591  C C   . ASP A 1 83  ? 11.433  -22.903 65.060 1.00 29.72 ? 83   ASP A C   1 
ATOM   592  O O   . ASP A 1 83  ? 10.585  -23.178 65.894 1.00 30.84 ? 83   ASP A O   1 
ATOM   593  C CB  . ASP A 1 83  ? 13.513  -24.207 65.033 1.00 32.68 ? 83   ASP A CB  1 
ATOM   594  C CG  . ASP A 1 83  ? 14.028  -25.623 64.955 1.00 37.36 ? 83   ASP A CG  1 
ATOM   595  O OD1 . ASP A 1 83  ? 13.345  -26.526 64.374 1.00 41.06 ? 83   ASP A OD1 1 
ATOM   596  O OD2 . ASP A 1 83  ? 15.143  -25.821 65.501 1.00 40.77 ? 83   ASP A OD2 1 
ATOM   597  N N   . ASN A 1 84  ? 11.790  -21.660 64.779 1.00 27.63 ? 84   ASN A N   1 
ATOM   598  C CA  . ASN A 1 84  ? 11.137  -20.518 65.398 1.00 26.03 ? 84   ASN A CA  1 
ATOM   599  C C   . ASN A 1 84  ? 10.520  -19.647 64.348 1.00 23.59 ? 84   ASN A C   1 
ATOM   600  O O   . ASN A 1 84  ? 11.214  -19.091 63.504 1.00 23.11 ? 84   ASN A O   1 
ATOM   601  C CB  . ASN A 1 84  ? 12.132  -19.701 66.192 1.00 26.08 ? 84   ASN A CB  1 
ATOM   602  C CG  . ASN A 1 84  ? 12.779  -20.505 67.288 1.00 29.49 ? 84   ASN A CG  1 
ATOM   603  O OD1 . ASN A 1 84  ? 13.863  -21.067 67.097 1.00 33.09 ? 84   ASN A OD1 1 
ATOM   604  N ND2 . ASN A 1 84  ? 12.110  -20.605 68.424 1.00 29.29 ? 84   ASN A ND2 1 
ATOM   605  N N   . VAL A 1 85  ? 9.202   -19.547 64.410 1.00 22.38 ? 85   VAL A N   1 
ATOM   606  C CA  . VAL A 1 85  ? 8.449   -18.783 63.440 1.00 19.43 ? 85   VAL A CA  1 
ATOM   607  C C   . VAL A 1 85  ? 7.963   -17.516 64.154 1.00 19.04 ? 85   VAL A C   1 
ATOM   608  O O   . VAL A 1 85  ? 7.636   -17.569 65.348 1.00 18.90 ? 85   VAL A O   1 
ATOM   609  C CB  . VAL A 1 85  ? 7.289   -19.659 62.834 1.00 19.77 ? 85   VAL A CB  1 
ATOM   610  C CG1 . VAL A 1 85  ? 6.247   -18.785 62.131 1.00 17.74 ? 85   VAL A CG1 1 
ATOM   611  C CG2 . VAL A 1 85  ? 7.852   -20.609 61.800 1.00 19.50 ? 85   VAL A CG2 1 
ATOM   612  N N   . LEU A 1 86  ? 7.966   -16.381 63.457 1.00 17.43 ? 86   LEU A N   1 
ATOM   613  C CA  . LEU A 1 86  ? 7.438   -15.149 64.015 1.00 17.89 ? 86   LEU A CA  1 
ATOM   614  C C   . LEU A 1 86  ? 6.100   -14.888 63.324 1.00 17.54 ? 86   LEU A C   1 
ATOM   615  O O   . LEU A 1 86  ? 5.990   -14.968 62.112 1.00 17.32 ? 86   LEU A O   1 
ATOM   616  C CB  . LEU A 1 86  ? 8.386   -13.960 63.790 1.00 18.44 ? 86   LEU A CB  1 
ATOM   617  C CG  . LEU A 1 86  ? 7.891   -12.602 64.313 1.00 19.11 ? 86   LEU A CG  1 
ATOM   618  C CD1 . LEU A 1 86  ? 7.990   -12.469 65.843 1.00 20.22 ? 86   LEU A CD1 1 
ATOM   619  C CD2 . LEU A 1 86  ? 8.541   -11.451 63.614 1.00 22.32 ? 86   LEU A CD2 1 
ATOM   620  N N   . LEU A 1 87  ? 5.088   -14.579 64.118 1.00 18.24 ? 87   LEU A N   1 
ATOM   621  C CA  . LEU A 1 87  ? 3.835   -14.079 63.582 1.00 17.52 ? 87   LEU A CA  1 
ATOM   622  C C   . LEU A 1 87  ? 3.772   -12.575 63.852 1.00 16.69 ? 87   LEU A C   1 
ATOM   623  O O   . LEU A 1 87  ? 3.946   -12.135 64.992 1.00 15.68 ? 87   LEU A O   1 
ATOM   624  C CB  . LEU A 1 87  ? 2.658   -14.818 64.268 1.00 17.24 ? 87   LEU A CB  1 
ATOM   625  C CG  . LEU A 1 87  ? 1.270   -14.214 63.997 1.00 19.37 ? 87   LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 87  ? 0.930   -14.300 62.530 1.00 17.18 ? 87   LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 87  ? 0.213   -14.955 64.800 1.00 17.68 ? 87   LEU A CD2 1 
ATOM   628  N N   . THR A 1 88  ? 3.533   -11.787 62.805 1.00 17.71 ? 88   THR A N   1 
ATOM   629  C CA  . THR A 1 88  ? 3.380   -10.351 62.905 1.00 17.66 ? 88   THR A CA  1 
ATOM   630  C C   . THR A 1 88  ? 2.003   -10.063 62.337 1.00 17.67 ? 88   THR A C   1 
ATOM   631  O O   . THR A 1 88  ? 1.730   -10.410 61.198 1.00 16.44 ? 88   THR A O   1 
ATOM   632  C CB  . THR A 1 88  ? 4.397   -9.601  62.074 1.00 19.04 ? 88   THR A CB  1 
ATOM   633  O OG1 . THR A 1 88  ? 5.729   -9.952  62.495 1.00 21.31 ? 88   THR A OG1 1 
ATOM   634  C CG2 . THR A 1 88  ? 4.219   -8.094  62.221 1.00 19.08 ? 88   THR A CG2 1 
ATOM   635  N N   . ALA A 1 89  ? 1.168   -9.403  63.126 1.00 17.22 ? 89   ALA A N   1 
ATOM   636  C CA  . ALA A 1 89  ? -0.214  -9.132  62.740 1.00 16.74 ? 89   ALA A CA  1 
ATOM   637  C C   . ALA A 1 89  ? -0.402  -7.629  62.783 1.00 16.63 ? 89   ALA A C   1 
ATOM   638  O O   . ALA A 1 89  ? 0.145   -6.958  63.692 1.00 15.50 ? 89   ALA A O   1 
ATOM   639  C CB  . ALA A 1 89  ? -1.167  -9.828  63.729 1.00 17.44 ? 89   ALA A CB  1 
ATOM   640  N N   . GLU A 1 90  ? -1.120  -7.071  61.789 1.00 17.00 ? 90   GLU A N   1 
ATOM   641  C CA  . GLU A 1 90  ? -1.315  -5.621  61.708 1.00 17.22 ? 90   GLU A CA  1 
ATOM   642  C C   . GLU A 1 90  ? -2.772  -5.337  61.391 1.00 17.56 ? 90   GLU A C   1 
ATOM   643  O O   . GLU A 1 90  ? -3.271  -5.825  60.388 1.00 16.13 ? 90   GLU A O   1 
ATOM   644  C CB  . GLU A 1 90  ? -0.456  -4.997  60.614 1.00 18.51 ? 90   GLU A CB  1 
ATOM   645  C CG  . GLU A 1 90  ? 1.038   -5.344  60.788 1.00 19.76 ? 90   GLU A CG  1 
ATOM   646  C CD  . GLU A 1 90  ? 1.915   -4.908  59.638 1.00 21.25 ? 90   GLU A CD  1 
ATOM   647  O OE1 . GLU A 1 90  ? 1.446   -4.782  58.484 1.00 22.34 ? 90   GLU A OE1 1 
ATOM   648  O OE2 . GLU A 1 90  ? 3.116   -4.664  59.905 1.00 27.06 ? 90   GLU A OE2 1 
ATOM   649  N N   . TYR A 1 91  ? -3.410  -4.531  62.228 1.00 16.90 ? 91   TYR A N   1 
ATOM   650  C CA  . TYR A 1 91  ? -4.828  -4.157  62.014 1.00 17.58 ? 91   TYR A CA  1 
ATOM   651  C C   . TYR A 1 91  ? -4.784  -2.965  61.094 1.00 16.12 ? 91   TYR A C   1 
ATOM   652  O O   . TYR A 1 91  ? -4.860  -1.818  61.534 1.00 16.84 ? 91   TYR A O   1 
ATOM   653  C CB  . TYR A 1 91  ? -5.479  -3.842  63.345 1.00 19.62 ? 91   TYR A CB  1 
ATOM   654  C CG  . TYR A 1 91  ? -5.566  -5.021  64.298 1.00 21.52 ? 91   TYR A CG  1 
ATOM   655  C CD1 . TYR A 1 91  ? -6.340  -6.123  63.994 1.00 25.72 ? 91   TYR A CD1 1 
ATOM   656  C CD2 . TYR A 1 91  ? -4.913  -5.007  65.532 1.00 25.72 ? 91   TYR A CD2 1 
ATOM   657  C CE1 . TYR A 1 91  ? -6.439  -7.210  64.875 1.00 24.78 ? 91   TYR A CE1 1 
ATOM   658  C CE2 . TYR A 1 91  ? -5.006  -6.104  66.442 1.00 27.48 ? 91   TYR A CE2 1 
ATOM   659  C CZ  . TYR A 1 91  ? -5.768  -7.199  66.095 1.00 25.84 ? 91   TYR A CZ  1 
ATOM   660  O OH  . TYR A 1 91  ? -5.903  -8.288  66.934 1.00 23.06 ? 91   TYR A OH  1 
ATOM   661  N N   . GLN A 1 92  ? -4.588  -3.220  59.806 1.00 15.37 ? 92   GLN A N   1 
ATOM   662  C CA  . GLN A 1 92  ? -4.206  -2.122  58.910 1.00 15.30 ? 92   GLN A CA  1 
ATOM   663  C C   . GLN A 1 92  ? -5.325  -1.138  58.660 1.00 14.87 ? 92   GLN A C   1 
ATOM   664  O O   . GLN A 1 92  ? -5.089  0.052   58.614 1.00 15.03 ? 92   GLN A O   1 
ATOM   665  C CB  . GLN A 1 92  ? -3.702  -2.625  57.587 1.00 15.18 ? 92   GLN A CB  1 
ATOM   666  C CG  . GLN A 1 92  ? -2.355  -3.396  57.731 1.00 15.76 ? 92   GLN A CG  1 
ATOM   667  C CD  . GLN A 1 92  ? -1.692  -3.647  56.394 1.00 18.67 ? 92   GLN A CD  1 
ATOM   668  O OE1 . GLN A 1 92  ? -2.318  -3.591  55.334 1.00 16.81 ? 92   GLN A OE1 1 
ATOM   669  N NE2 . GLN A 1 92  ? -0.406  -3.969  56.446 1.00 14.97 ? 92   GLN A NE2 1 
ATOM   670  N N   . THR A 1 93  ? -6.526  -1.649  58.474 1.00 14.69 ? 93   THR A N   1 
ATOM   671  C CA  . THR A 1 93  ? -7.682  -0.749  58.292 1.00 15.00 ? 93   THR A CA  1 
ATOM   672  C C   . THR A 1 93  ? -8.873  -1.425  58.941 1.00 15.25 ? 93   THR A C   1 
ATOM   673  O O   . THR A 1 93  ? -8.787  -2.573  59.371 1.00 13.18 ? 93   THR A O   1 
ATOM   674  C CB  . THR A 1 93  ? -8.027  -0.481  56.784 1.00 15.67 ? 93   THR A CB  1 
ATOM   675  O OG1 . THR A 1 93  ? -8.736  -1.615  56.281 1.00 17.65 ? 93   THR A OG1 1 
ATOM   676  C CG2 . THR A 1 93  ? -6.831  -0.161  55.884 1.00 17.29 ? 93   THR A CG2 1 
ATOM   677  N N   . SER A 1 94  ? -10.009 -0.734  59.018 1.00 15.49 ? 94   SER A N   1 
ATOM   678  C CA  . SER A 1 94  ? -11.216 -1.350  59.571 1.00 16.62 ? 94   SER A CA  1 
ATOM   679  C C   . SER A 1 94  ? -11.653 -2.593  58.790 1.00 16.27 ? 94   SER A C   1 
ATOM   680  O O   . SER A 1 94  ? -12.385 -3.442  59.332 1.00 16.44 ? 94   SER A O   1 
ATOM   681  C CB  . SER A 1 94  ? -12.400 -0.340  59.559 1.00 17.66 ? 94   SER A CB  1 
ATOM   682  O OG  . SER A 1 94  ? -12.035 0.883   60.147 1.00 23.58 ? 94   SER A OG  1 
ATOM   683  N N   . ASN A 1 95  ? -11.232 -2.694  57.521 1.00 14.48 ? 95   ASN A N   1 
ATOM   684  C CA  . ASN A 1 95  ? -11.656 -3.794  56.689 1.00 14.95 ? 95   ASN A CA  1 
ATOM   685  C C   . ASN A 1 95  ? -10.542 -4.663  56.145 1.00 14.72 ? 95   ASN A C   1 
ATOM   686  O O   . ASN A 1 95  ? -10.797 -5.492  55.309 1.00 15.47 ? 95   ASN A O   1 
ATOM   687  C CB  . ASN A 1 95  ? -12.435 -3.285  55.508 1.00 14.97 ? 95   ASN A CB  1 
ATOM   688  C CG  . ASN A 1 95  ? -13.764 -2.674  55.930 1.00 18.96 ? 95   ASN A CG  1 
ATOM   689  O OD1 . ASN A 1 95  ? -14.794 -3.332  55.896 1.00 27.35 ? 95   ASN A OD1 1 
ATOM   690  N ND2 . ASN A 1 95  ? -13.723 -1.442  56.365 1.00 19.09 ? 95   ASN A ND2 1 
ATOM   691  N N   . ARG A 1 96  ? -9.322  -4.457  56.606 1.00 13.73 ? 96   ARG A N   1 
ATOM   692  C CA  . ARG A 1 96  ? -8.217  -5.249  56.064 1.00 12.56 ? 96   ARG A CA  1 
ATOM   693  C C   . ARG A 1 96  ? -7.290  -5.621  57.211 1.00 13.58 ? 96   ARG A C   1 
ATOM   694  O O   . ARG A 1 96  ? -6.812  -4.744  57.964 1.00 14.27 ? 96   ARG A O   1 
ATOM   695  C CB  . ARG A 1 96  ? -7.477  -4.457  54.978 1.00 12.59 ? 96   ARG A CB  1 
ATOM   696  C CG  . ARG A 1 96  ? -6.216  -5.197  54.426 1.00 12.19 ? 96   ARG A CG  1 
ATOM   697  C CD  . ARG A 1 96  ? -5.564  -4.403  53.326 1.00 14.01 ? 96   ARG A CD  1 
ATOM   698  N NE  . ARG A 1 96  ? -4.662  -3.353  53.801 1.00 16.07 ? 96   ARG A NE  1 
ATOM   699  C CZ  . ARG A 1 96  ? -4.731  -2.071  53.466 1.00 18.48 ? 96   ARG A CZ  1 
ATOM   700  N NH1 . ARG A 1 96  ? -5.702  -1.604  52.665 1.00 19.60 ? 96   ARG A NH1 1 
ATOM   701  N NH2 . ARG A 1 96  ? -3.813  -1.231  53.927 1.00 19.27 ? 96   ARG A NH2 1 
ATOM   702  N N   . PHE A 1 97  ? -7.066  -6.928  57.336 1.00 13.09 ? 97   PHE A N   1 
ATOM   703  C CA  . PHE A 1 97  ? -6.182  -7.497  58.311 1.00 13.31 ? 97   PHE A CA  1 
ATOM   704  C C   . PHE A 1 97  ? -4.967  -8.046  57.537 1.00 13.47 ? 97   PHE A C   1 
ATOM   705  O O   . PHE A 1 97  ? -5.115  -8.625  56.455 1.00 12.73 ? 97   PHE A O   1 
ATOM   706  C CB  . PHE A 1 97  ? -6.897  -8.619  59.080 1.00 12.06 ? 97   PHE A CB  1 
ATOM   707  C CG  . PHE A 1 97  ? -6.042  -9.293  60.115 1.00 13.88 ? 97   PHE A CG  1 
ATOM   708  C CD1 . PHE A 1 97  ? -5.467  -8.548  61.171 1.00 13.60 ? 97   PHE A CD1 1 
ATOM   709  C CD2 . PHE A 1 97  ? -5.731  -10.637 60.001 1.00 13.49 ? 97   PHE A CD2 1 
ATOM   710  C CE1 . PHE A 1 97  ? -4.631  -9.141  62.092 1.00 13.05 ? 97   PHE A CE1 1 
ATOM   711  C CE2 . PHE A 1 97  ? -4.877  -11.265 60.963 1.00 14.48 ? 97   PHE A CE2 1 
ATOM   712  C CZ  . PHE A 1 97  ? -4.339  -10.533 61.982 1.00 11.89 ? 97   PHE A CZ  1 
ATOM   713  N N   . HIS A 1 98  ? -3.783  -7.910  58.118 1.00 15.26 ? 98   HIS A N   1 
ATOM   714  C CA  . HIS A 1 98  ? -2.576  -8.392  57.457 1.00 15.27 ? 98   HIS A CA  1 
ATOM   715  C C   . HIS A 1 98  ? -1.866  -9.241  58.505 1.00 15.36 ? 98   HIS A C   1 
ATOM   716  O O   . HIS A 1 98  ? -1.730  -8.797  59.637 1.00 14.38 ? 98   HIS A O   1 
ATOM   717  C CB  . HIS A 1 98  ? -1.732  -7.176  57.021 1.00 16.26 ? 98   HIS A CB  1 
ATOM   718  C CG  . HIS A 1 98  ? -0.347  -7.515  56.532 1.00 18.18 ? 98   HIS A CG  1 
ATOM   719  N ND1 . HIS A 1 98  ? -0.093  -8.546  55.650 1.00 19.76 ? 98   HIS A ND1 1 
ATOM   720  C CD2 . HIS A 1 98  ? 0.856   -6.929  56.776 1.00 19.61 ? 98   HIS A CD2 1 
ATOM   721  C CE1 . HIS A 1 98  ? 1.209   -8.601  55.392 1.00 17.26 ? 98   HIS A CE1 1 
ATOM   722  N NE2 . HIS A 1 98  ? 1.804   -7.621  56.049 1.00 20.46 ? 98   HIS A NE2 1 
ATOM   723  N N   . PHE A 1 99  ? -1.473  -10.476 58.168 1.00 15.69 ? 99   PHE A N   1 
ATOM   724  C CA  . PHE A 1 99  ? -0.587  -11.250 59.065 1.00 16.65 ? 99   PHE A CA  1 
ATOM   725  C C   . PHE A 1 99  ? 0.482   -11.961 58.235 1.00 17.61 ? 99   PHE A C   1 
ATOM   726  O O   . PHE A 1 99  ? 0.225   -12.372 57.099 1.00 16.72 ? 99   PHE A O   1 
ATOM   727  C CB  . PHE A 1 99  ? -1.334  -12.213 60.005 1.00 16.66 ? 99   PHE A CB  1 
ATOM   728  C CG  . PHE A 1 99  ? -1.952  -13.432 59.328 1.00 17.72 ? 99   PHE A CG  1 
ATOM   729  C CD1 . PHE A 1 99  ? -1.283  -14.654 59.318 1.00 18.71 ? 99   PHE A CD1 1 
ATOM   730  C CD2 . PHE A 1 99  ? -3.226  -13.370 58.764 1.00 18.39 ? 99   PHE A CD2 1 
ATOM   731  C CE1 . PHE A 1 99  ? -1.851  -15.767 58.723 1.00 19.64 ? 99   PHE A CE1 1 
ATOM   732  C CE2 . PHE A 1 99  ? -3.823  -14.520 58.168 1.00 18.74 ? 99   PHE A CE2 1 
ATOM   733  C CZ  . PHE A 1 99  ? -3.132  -15.709 58.163 1.00 17.16 ? 99   PHE A CZ  1 
ATOM   734  N N   . LYS A 1 100 ? 1.683   -12.047 58.794 1.00 17.81 ? 100  LYS A N   1 
ATOM   735  C CA  . LYS A 1 100 ? 2.768   -12.744 58.119 1.00 19.67 ? 100  LYS A CA  1 
ATOM   736  C C   . LYS A 1 100 ? 3.490   -13.674 59.067 1.00 19.01 ? 100  LYS A C   1 
ATOM   737  O O   . LYS A 1 100 ? 3.593   -13.425 60.269 1.00 19.66 ? 100  LYS A O   1 
ATOM   738  C CB  . LYS A 1 100 ? 3.726   -11.801 57.351 1.00 20.66 ? 100  LYS A CB  1 
ATOM   739  C CG  . LYS A 1 100 ? 4.406   -10.739 58.114 1.00 23.50 ? 100  LYS A CG  1 
ATOM   740  C CD  . LYS A 1 100 ? 5.286   -9.891  57.179 1.00 22.63 ? 100  LYS A CD  1 
ATOM   741  C CE  . LYS A 1 100 ? 6.169   -8.993  58.048 1.00 29.93 ? 100  LYS A CE  1 
ATOM   742  N NZ  . LYS A 1 100 ? 7.156   -8.251  57.210 1.00 32.64 ? 100  LYS A NZ  1 
ATOM   743  N N   . LEU A 1 101 ? 3.924   -14.799 58.510 1.00 19.16 ? 101  LEU A N   1 
ATOM   744  C CA  . LEU A 1 101 ? 4.661   -15.808 59.260 1.00 18.95 ? 101  LEU A CA  1 
ATOM   745  C C   . LEU A 1 101 ? 6.032   -15.818 58.621 1.00 18.83 ? 101  LEU A C   1 
ATOM   746  O O   . LEU A 1 101 ? 6.148   -16.027 57.406 1.00 18.24 ? 101  LEU A O   1 
ATOM   747  C CB  . LEU A 1 101 ? 3.989   -17.174 59.143 1.00 19.18 ? 101  LEU A CB  1 
ATOM   748  C CG  . LEU A 1 101 ? 2.597   -17.220 59.811 1.00 19.90 ? 101  LEU A CG  1 
ATOM   749  C CD1 . LEU A 1 101 ? 1.699   -18.288 59.219 1.00 21.89 ? 101  LEU A CD1 1 
ATOM   750  C CD2 . LEU A 1 101 ? 2.698   -17.374 61.340 1.00 22.27 ? 101  LEU A CD2 1 
ATOM   751  N N   . THR A 1 102 ? 7.047   -15.511 59.419 1.00 18.77 ? 102  THR A N   1 
ATOM   752  C CA  . THR A 1 102 ? 8.406   -15.392 58.904 1.00 20.18 ? 102  THR A CA  1 
ATOM   753  C C   . THR A 1 102 ? 9.307   -16.304 59.751 1.00 19.80 ? 102  THR A C   1 
ATOM   754  O O   . THR A 1 102 ? 8.885   -16.789 60.783 1.00 18.52 ? 102  THR A O   1 
ATOM   755  C CB  . THR A 1 102 ? 8.872   -13.896 58.918 1.00 21.03 ? 102  THR A CB  1 
ATOM   756  O OG1 . THR A 1 102 ? 8.750   -13.341 60.235 1.00 20.67 ? 102  THR A OG1 1 
ATOM   757  C CG2 . THR A 1 102 ? 8.009   -13.029 57.960 1.00 20.62 ? 102  THR A CG2 1 
ATOM   758  N N   . ASP A 1 103 ? 10.532  -16.559 59.311 1.00 20.88 ? 103  ASP A N   1 
ATOM   759  C CA  . ASP A 1 103 ? 11.507  -17.266 60.140 1.00 21.93 ? 103  ASP A CA  1 
ATOM   760  C C   . ASP A 1 103 ? 12.065  -16.240 61.137 1.00 23.05 ? 103  ASP A C   1 
ATOM   761  O O   . ASP A 1 103 ? 12.603  -15.220 60.744 1.00 22.99 ? 103  ASP A O   1 
ATOM   762  C CB  . ASP A 1 103 ? 12.623  -17.840 59.232 1.00 20.85 ? 103  ASP A CB  1 
ATOM   763  C CG  . ASP A 1 103 ? 13.676  -18.643 60.005 1.00 24.68 ? 103  ASP A CG  1 
ATOM   764  O OD1 . ASP A 1 103 ? 13.763  -18.513 61.249 1.00 24.07 ? 103  ASP A OD1 1 
ATOM   765  O OD2 . ASP A 1 103 ? 14.431  -19.404 59.340 1.00 25.69 ? 103  ASP A OD2 1 
ATOM   766  N N   . GLN A 1 104 ? 11.931  -16.510 62.427 1.00 25.54 ? 104  GLN A N   1 
ATOM   767  C CA  . GLN A 1 104 ? 12.315  -15.541 63.442 1.00 28.46 ? 104  GLN A CA  1 
ATOM   768  C C   . GLN A 1 104 ? 13.795  -15.169 63.363 1.00 29.90 ? 104  GLN A C   1 
ATOM   769  O O   . GLN A 1 104 ? 14.173  -14.032 63.654 1.00 30.67 ? 104  GLN A O   1 
ATOM   770  C CB  . GLN A 1 104 ? 11.965  -16.097 64.820 1.00 29.11 ? 104  GLN A CB  1 
ATOM   771  C CG  . GLN A 1 104 ? 11.456  -15.058 65.777 1.00 32.02 ? 104  GLN A CG  1 
ATOM   772  C CD  . GLN A 1 104 ? 11.530  -15.504 67.210 1.00 36.37 ? 104  GLN A CD  1 
ATOM   773  O OE1 . GLN A 1 104 ? 11.395  -16.692 67.527 1.00 35.95 ? 104  GLN A OE1 1 
ATOM   774  N NE2 . GLN A 1 104 ? 11.753  -14.544 68.099 1.00 40.55 ? 104  GLN A NE2 1 
ATOM   775  N N   . THR A 1 105 ? 14.633  -16.110 62.937 1.00 31.78 ? 105  THR A N   1 
ATOM   776  C CA  . THR A 1 105 ? 16.093  -15.861 62.929 1.00 33.77 ? 105  THR A CA  1 
ATOM   777  C C   . THR A 1 105 ? 16.779  -15.747 61.560 1.00 34.04 ? 105  THR A C   1 
ATOM   778  O O   . THR A 1 105 ? 18.007  -15.622 61.492 1.00 34.81 ? 105  THR A O   1 
ATOM   779  C CB  . THR A 1 105 ? 16.851  -16.875 63.818 1.00 34.11 ? 105  THR A CB  1 
ATOM   780  O OG1 . THR A 1 105 ? 16.668  -18.199 63.309 1.00 36.46 ? 105  THR A OG1 1 
ATOM   781  C CG2 . THR A 1 105 ? 16.344  -16.818 65.253 1.00 36.37 ? 105  THR A CG2 1 
ATOM   782  N N   . ASN A 1 106 ? 16.011  -15.768 60.469 1.00 33.10 ? 106  ASN A N   1 
ATOM   783  C CA  . ASN A 1 106 ? 16.586  -15.593 59.136 1.00 32.35 ? 106  ASN A CA  1 
ATOM   784  C C   . ASN A 1 106 ? 15.668  -14.795 58.221 1.00 31.01 ? 106  ASN A C   1 
ATOM   785  O O   . ASN A 1 106 ? 14.453  -15.015 58.212 1.00 29.27 ? 106  ASN A O   1 
ATOM   786  C CB  . ASN A 1 106 ? 16.884  -16.953 58.483 1.00 33.38 ? 106  ASN A CB  1 
ATOM   787  C CG  . ASN A 1 106 ? 17.837  -17.820 59.313 1.00 36.81 ? 106  ASN A CG  1 
ATOM   788  O OD1 . ASN A 1 106 ? 17.457  -18.896 59.803 1.00 40.26 ? 106  ASN A OD1 1 
ATOM   789  N ND2 . ASN A 1 106 ? 19.073  -17.357 59.475 1.00 37.69 ? 106  ASN A ND2 1 
ATOM   790  N N   . ASN A 1 107 ? 16.255  -13.868 57.471 1.00 29.42 ? 107  ASN A N   1 
ATOM   791  C CA  . ASN A 1 107 ? 15.549  -13.167 56.424 1.00 29.09 ? 107  ASN A CA  1 
ATOM   792  C C   . ASN A 1 107 ? 15.231  -14.171 55.314 1.00 27.35 ? 107  ASN A C   1 
ATOM   793  O O   . ASN A 1 107 ? 16.062  -15.016 54.978 1.00 27.00 ? 107  ASN A O   1 
ATOM   794  C CB  . ASN A 1 107 ? 16.383  -12.005 55.874 1.00 29.87 ? 107  ASN A CB  1 
ATOM   795  C CG  . ASN A 1 107 ? 16.548  -10.844 56.873 1.00 32.82 ? 107  ASN A CG  1 
ATOM   796  O OD1 . ASN A 1 107 ? 17.605  -10.199 56.899 1.00 38.33 ? 107  ASN A OD1 1 
ATOM   797  N ND2 . ASN A 1 107 ? 15.517  -10.558 57.674 1.00 34.69 ? 107  ASN A ND2 1 
ATOM   798  N N   . ARG A 1 108 ? 14.011  -14.113 54.789 1.00 23.69 ? 108  ARG A N   1 
ATOM   799  C CA  . ARG A 1 108 ? 13.593  -14.972 53.661 1.00 20.16 ? 108  ARG A CA  1 
ATOM   800  C C   . ARG A 1 108 ? 13.071  -14.091 52.537 1.00 19.09 ? 108  ARG A C   1 
ATOM   801  O O   . ARG A 1 108 ? 12.757  -12.922 52.759 1.00 18.08 ? 108  ARG A O   1 
ATOM   802  C CB  . ARG A 1 108 ? 12.497  -15.961 54.089 1.00 21.13 ? 108  ARG A CB  1 
ATOM   803  C CG  . ARG A 1 108 ? 12.934  -17.004 55.101 1.00 20.26 ? 108  ARG A CG  1 
ATOM   804  C CD  . ARG A 1 108 ? 11.767  -17.889 55.539 1.00 17.21 ? 108  ARG A CD  1 
ATOM   805  N NE  . ARG A 1 108 ? 11.198  -18.585 54.384 1.00 15.01 ? 108  ARG A NE  1 
ATOM   806  C CZ  . ARG A 1 108 ? 11.689  -19.688 53.853 1.00 18.99 ? 108  ARG A CZ  1 
ATOM   807  N NH1 . ARG A 1 108 ? 12.756  -20.294 54.399 1.00 16.11 ? 108  ARG A NH1 1 
ATOM   808  N NH2 . ARG A 1 108 ? 11.100  -20.215 52.789 1.00 15.46 ? 108  ARG A NH2 1 
ATOM   809  N N   . PHE A 1 109 ? 12.954  -14.664 51.340 1.00 17.37 ? 109  PHE A N   1 
ATOM   810  C CA  . PHE A 1 109 ? 12.525  -13.906 50.200 1.00 16.04 ? 109  PHE A CA  1 
ATOM   811  C C   . PHE A 1 109 ? 11.103  -13.382 50.452 1.00 16.54 ? 109  PHE A C   1 
ATOM   812  O O   . PHE A 1 109 ? 10.232  -14.158 50.809 1.00 14.84 ? 109  PHE A O   1 
ATOM   813  C CB  . PHE A 1 109 ? 12.496  -14.759 48.944 1.00 16.55 ? 109  PHE A CB  1 
ATOM   814  C CG  . PHE A 1 109 ? 11.912  -14.020 47.766 1.00 15.88 ? 109  PHE A CG  1 
ATOM   815  C CD1 . PHE A 1 109 ? 12.670  -13.080 47.079 1.00 17.56 ? 109  PHE A CD1 1 
ATOM   816  C CD2 . PHE A 1 109 ? 10.545  -14.177 47.431 1.00 17.37 ? 109  PHE A CD2 1 
ATOM   817  C CE1 . PHE A 1 109 ? 12.106  -12.342 46.035 1.00 19.10 ? 109  PHE A CE1 1 
ATOM   818  C CE2 . PHE A 1 109 ? 9.993   -13.453 46.392 1.00 15.48 ? 109  PHE A CE2 1 
ATOM   819  C CZ  . PHE A 1 109 ? 10.772  -12.533 45.698 1.00 15.33 ? 109  PHE A CZ  1 
ATOM   820  N N   . GLU A 1 110 ? 10.926  -12.085 50.268 1.00 16.44 ? 110  GLU A N   1 
ATOM   821  C CA  . GLU A 1 110 ? 9.602   -11.456 50.302 1.00 17.42 ? 110  GLU A CA  1 
ATOM   822  C C   . GLU A 1 110 ? 9.387   -10.738 48.990 1.00 17.43 ? 110  GLU A C   1 
ATOM   823  O O   . GLU A 1 110 ? 10.301  -10.082 48.468 1.00 17.59 ? 110  GLU A O   1 
ATOM   824  C CB  . GLU A 1 110 ? 9.525   -10.481 51.472 1.00 18.21 ? 110  GLU A CB  1 
ATOM   825  C CG  . GLU A 1 110 ? 9.838   -11.124 52.793 1.00 21.40 ? 110  GLU A CG  1 
ATOM   826  C CD  . GLU A 1 110 ? 9.395   -10.318 53.966 1.00 29.84 ? 110  GLU A CD  1 
ATOM   827  O OE1 . GLU A 1 110 ? 8.308   -9.655  53.895 1.00 33.47 ? 110  GLU A OE1 1 
ATOM   828  O OE2 . GLU A 1 110 ? 10.110  -10.402 54.987 1.00 28.45 ? 110  GLU A OE2 1 
ATOM   829  N N   . VAL A 1 111 ? 8.162   -10.809 48.454 1.00 16.95 ? 111  VAL A N   1 
ATOM   830  C CA  . VAL A 1 111 ? 7.874   -10.194 47.148 1.00 15.72 ? 111  VAL A CA  1 
ATOM   831  C C   . VAL A 1 111 ? 8.126   -8.703  47.155 1.00 15.99 ? 111  VAL A C   1 
ATOM   832  O O   . VAL A 1 111 ? 7.559   -7.978  47.979 1.00 16.43 ? 111  VAL A O   1 
ATOM   833  C CB  . VAL A 1 111 ? 6.409   -10.468 46.707 1.00 16.06 ? 111  VAL A CB  1 
ATOM   834  C CG1 . VAL A 1 111 ? 6.077   -9.783  45.356 1.00 14.90 ? 111  VAL A CG1 1 
ATOM   835  C CG2 . VAL A 1 111 ? 6.166   -11.983 46.674 1.00 15.93 ? 111  VAL A CG2 1 
ATOM   836  N N   . PRO A 1 112 ? 8.986   -8.214  46.244 1.00 15.92 ? 112  PRO A N   1 
ATOM   837  C CA  . PRO A 1 112 ? 9.274   -6.783  46.197 1.00 17.22 ? 112  PRO A CA  1 
ATOM   838  C C   . PRO A 1 112 ? 8.217   -6.007  45.396 1.00 17.06 ? 112  PRO A C   1 
ATOM   839  O O   . PRO A 1 112 ? 8.514   -5.408  44.363 1.00 18.03 ? 112  PRO A O   1 
ATOM   840  C CB  . PRO A 1 112 ? 10.616  -6.715  45.455 1.00 17.28 ? 112  PRO A CB  1 
ATOM   841  C CG  . PRO A 1 112 ? 10.694  -7.898  44.685 1.00 17.29 ? 112  PRO A CG  1 
ATOM   842  C CD  . PRO A 1 112 ? 9.802   -8.972  45.270 1.00 17.25 ? 112  PRO A CD  1 
ATOM   843  N N   . HIS A 1 113 ? 6.987   -6.027  45.871 1.00 17.28 ? 113  HIS A N   1 
ATOM   844  C CA  . HIS A 1 113 ? 5.884   -5.425  45.110 1.00 17.14 ? 113  HIS A CA  1 
ATOM   845  C C   . HIS A 1 113 ? 6.039   -3.912  44.872 1.00 17.77 ? 113  HIS A C   1 
ATOM   846  O O   . HIS A 1 113 ? 6.490   -3.179  45.751 1.00 18.34 ? 113  HIS A O   1 
ATOM   847  C CB  . HIS A 1 113 ? 4.574   -5.727  45.831 1.00 17.23 ? 113  HIS A CB  1 
ATOM   848  C CG  . HIS A 1 113 ? 3.393   -5.732  44.923 1.00 17.45 ? 113  HIS A CG  1 
ATOM   849  N ND1 . HIS A 1 113 ? 2.540   -4.648  44.811 1.00 16.84 ? 113  HIS A ND1 1 
ATOM   850  C CD2 . HIS A 1 113 ? 2.922   -6.676  44.075 1.00 18.08 ? 113  HIS A CD2 1 
ATOM   851  C CE1 . HIS A 1 113 ? 1.607   -4.921  43.915 1.00 15.37 ? 113  HIS A CE1 1 
ATOM   852  N NE2 . HIS A 1 113 ? 1.802   -6.150  43.466 1.00 13.93 ? 113  HIS A NE2 1 
ATOM   853  N N   . GLU A 1 114 ? 5.649   -3.446  43.688 1.00 18.45 ? 114  GLU A N   1 
ATOM   854  C CA  . GLU A 1 114 ? 5.832   -2.047  43.300 1.00 19.53 ? 114  GLU A CA  1 
ATOM   855  C C   . GLU A 1 114 ? 4.784   -1.156  43.977 1.00 19.76 ? 114  GLU A C   1 
ATOM   856  O O   . GLU A 1 114 ? 5.042   0.024   44.238 1.00 19.85 ? 114  GLU A O   1 
ATOM   857  C CB  . GLU A 1 114 ? 5.761   -1.923  41.765 1.00 21.25 ? 114  GLU A CB  1 
ATOM   858  C CG  . GLU A 1 114 ? 5.989   -0.531  41.145 1.00 22.40 ? 114  GLU A CG  1 
ATOM   859  C CD  . GLU A 1 114 ? 4.770   0.375   41.231 1.00 25.99 ? 114  GLU A CD  1 
ATOM   860  O OE1 . GLU A 1 114 ? 3.595   -0.096  41.390 1.00 22.23 ? 114  GLU A OE1 1 
ATOM   861  O OE2 . GLU A 1 114 ? 4.984   1.580   41.138 1.00 29.76 ? 114  GLU A OE2 1 
ATOM   862  N N   . HIS A 1 115 ? 3.611   -1.706  44.282 1.00 17.30 ? 115  HIS A N   1 
ATOM   863  C CA  . HIS A 1 115 ? 2.558   -0.844  44.819 1.00 17.39 ? 115  HIS A CA  1 
ATOM   864  C C   . HIS A 1 115 ? 2.440   -0.968  46.347 1.00 17.02 ? 115  HIS A C   1 
ATOM   865  O O   . HIS A 1 115 ? 2.407   0.048   47.051 1.00 17.02 ? 115  HIS A O   1 
ATOM   866  C CB  . HIS A 1 115 ? 1.219   -1.137  44.133 1.00 16.79 ? 115  HIS A CB  1 
ATOM   867  C CG  . HIS A 1 115 ? 0.139   -0.178  44.505 1.00 17.68 ? 115  HIS A CG  1 
ATOM   868  N ND1 . HIS A 1 115 ? 0.011   1.055   43.913 1.00 20.25 ? 115  HIS A ND1 1 
ATOM   869  C CD2 . HIS A 1 115 ? -0.855  -0.265  45.418 1.00 17.58 ? 115  HIS A CD2 1 
ATOM   870  C CE1 . HIS A 1 115 ? -1.032  1.687   44.429 1.00 21.48 ? 115  HIS A CE1 1 
ATOM   871  N NE2 . HIS A 1 115 ? -1.562  0.915   45.363 1.00 18.59 ? 115  HIS A NE2 1 
ATOM   872  N N   . VAL A 1 116 ? 2.350   -2.197  46.852 1.00 15.62 ? 116  VAL A N   1 
ATOM   873  C CA  . VAL A 1 116 ? 2.173   -2.465  48.264 1.00 17.91 ? 116  VAL A CA  1 
ATOM   874  C C   . VAL A 1 116 ? 3.384   -1.915  49.040 1.00 19.87 ? 116  VAL A C   1 
ATOM   875  O O   . VAL A 1 116 ? 4.519   -2.159  48.647 1.00 19.84 ? 116  VAL A O   1 
ATOM   876  C CB  . VAL A 1 116 ? 1.961   -3.971  48.523 1.00 17.85 ? 116  VAL A CB  1 
ATOM   877  C CG1 . VAL A 1 116 ? 1.980   -4.326  50.001 1.00 17.06 ? 116  VAL A CG1 1 
ATOM   878  C CG2 . VAL A 1 116 ? 0.601   -4.437  47.921 1.00 16.98 ? 116  VAL A CG2 1 
ATOM   879  N N   . GLN A 1 117 ? 3.141   -1.154  50.104 1.00 20.89 ? 117  GLN A N   1 
ATOM   880  C CA  . GLN A 1 117 ? 4.244   -0.687  50.959 1.00 24.60 ? 117  GLN A CA  1 
ATOM   881  C C   . GLN A 1 117 ? 4.190   -1.327  52.324 1.00 24.64 ? 117  GLN A C   1 
ATOM   882  O O   . GLN A 1 117 ? 3.157   -1.827  52.726 1.00 23.79 ? 117  GLN A O   1 
ATOM   883  C CB  . GLN A 1 117 ? 4.182   0.816   51.181 1.00 25.15 ? 117  GLN A CB  1 
ATOM   884  C CG  . GLN A 1 117 ? 4.210   1.668   49.974 1.00 30.26 ? 117  GLN A CG  1 
ATOM   885  C CD  . GLN A 1 117 ? 3.917   3.095   50.363 1.00 36.67 ? 117  GLN A CD  1 
ATOM   886  O OE1 . GLN A 1 117 ? 2.777   3.438   50.709 1.00 41.42 ? 117  GLN A OE1 1 
ATOM   887  N NE2 . GLN A 1 117 ? 4.944   3.930   50.364 1.00 37.75 ? 117  GLN A NE2 1 
ATOM   888  N N   . SER A 1 118 ? 5.302   -1.263  53.061 1.00 25.62 ? 118  SER A N   1 
ATOM   889  C CA  . SER A 1 118 ? 5.295   -1.706  54.453 1.00 26.97 ? 118  SER A CA  1 
ATOM   890  C C   . SER A 1 118 ? 4.403   -0.761  55.265 1.00 27.26 ? 118  SER A C   1 
ATOM   891  O O   . SER A 1 118 ? 4.295   0.437   54.972 1.00 26.98 ? 118  SER A O   1 
ATOM   892  C CB  . SER A 1 118 ? 6.720   -1.742  55.027 1.00 26.99 ? 118  SER A CB  1 
ATOM   893  O OG  . SER A 1 118 ? 7.250   -0.435  54.965 1.00 31.22 ? 118  SER A OG  1 
ATOM   894  N N   . PHE A 1 119 ? 3.721   -1.332  56.247 1.00 27.72 ? 119  PHE A N   1 
ATOM   895  C CA  . PHE A 1 119 ? 2.829   -0.589  57.120 1.00 28.89 ? 119  PHE A CA  1 
ATOM   896  C C   . PHE A 1 119 ? 3.654   0.046   58.211 1.00 30.20 ? 119  PHE A C   1 
ATOM   897  O O   . PHE A 1 119 ? 4.451   -0.613  58.864 1.00 29.29 ? 119  PHE A O   1 
ATOM   898  C CB  . PHE A 1 119 ? 1.825   -1.552  57.744 1.00 28.32 ? 119  PHE A CB  1 
ATOM   899  C CG  . PHE A 1 119 ? 0.750   -0.889  58.532 1.00 27.38 ? 119  PHE A CG  1 
ATOM   900  C CD1 . PHE A 1 119 ? -0.193  -0.077  57.907 1.00 27.18 ? 119  PHE A CD1 1 
ATOM   901  C CD2 . PHE A 1 119 ? 0.658   -1.085  59.891 1.00 26.13 ? 119  PHE A CD2 1 
ATOM   902  C CE1 . PHE A 1 119 ? -1.213  0.534   58.643 1.00 23.55 ? 119  PHE A CE1 1 
ATOM   903  C CE2 . PHE A 1 119 ? -0.363  -0.460  60.648 1.00 27.03 ? 119  PHE A CE2 1 
ATOM   904  C CZ  . PHE A 1 119 ? -1.292  0.353   60.010 1.00 26.54 ? 119  PHE A CZ  1 
ATOM   905  N N   . SER A 1 120 ? 3.475   1.347   58.368 1.00 32.02 ? 120  SER A N   1 
ATOM   906  C CA  . SER A 1 120 ? 3.918   2.066   59.552 1.00 33.97 ? 120  SER A CA  1 
ATOM   907  C C   . SER A 1 120 ? 2.622   2.708   59.958 1.00 34.23 ? 120  SER A C   1 
ATOM   908  O O   . SER A 1 120 ? 1.752   2.943   59.121 1.00 36.11 ? 120  SER A O   1 
ATOM   909  C CB  . SER A 1 120 ? 4.950   3.125   59.186 1.00 33.83 ? 120  SER A CB  1 
ATOM   910  O OG  . SER A 1 120 ? 4.398   4.013   58.230 1.00 37.40 ? 120  SER A OG  1 
ATOM   911  N N   . GLY A 1 121 ? 2.444   2.984   61.224 1.00 34.42 ? 121  GLY A N   1 
ATOM   912  C CA  . GLY A 1 121 ? 1.118   3.430   61.629 1.00 32.29 ? 121  GLY A CA  1 
ATOM   913  C C   . GLY A 1 121 ? 0.559   2.560   62.723 1.00 31.34 ? 121  GLY A C   1 
ATOM   914  O O   . GLY A 1 121 ? 1.201   1.598   63.180 1.00 29.76 ? 121  GLY A O   1 
ATOM   915  N N   . ASN A 1 122 ? -0.648  2.913   63.151 1.00 28.97 ? 122  ASN A N   1 
ATOM   916  C CA  . ASN A 1 122 ? -1.209  2.352   64.345 1.00 28.46 ? 122  ASN A CA  1 
ATOM   917  C C   . ASN A 1 122 ? -2.403  1.509   63.966 1.00 26.59 ? 122  ASN A C   1 
ATOM   918  O O   . ASN A 1 122 ? -3.011  1.780   62.943 1.00 26.34 ? 122  ASN A O   1 
ATOM   919  C CB  . ASN A 1 122 ? -1.633  3.489   65.282 1.00 29.33 ? 122  ASN A CB  1 
ATOM   920  C CG  . ASN A 1 122 ? -0.437  4.290   65.793 1.00 32.01 ? 122  ASN A CG  1 
ATOM   921  O OD1 . ASN A 1 122 ? 0.601   3.724   66.121 1.00 32.55 ? 122  ASN A OD1 1 
ATOM   922  N ND2 . ASN A 1 122 ? -0.578  5.599   65.839 1.00 32.60 ? 122  ASN A ND2 1 
ATOM   923  N N   . ALA A 1 123 ? -2.725  0.521   64.797 1.00 25.28 ? 123  ALA A N   1 
ATOM   924  C CA  . ALA A 1 123 ? -3.876  -0.354  64.584 1.00 24.11 ? 123  ALA A CA  1 
ATOM   925  C C   . ALA A 1 123 ? -5.097  0.526   64.278 1.00 24.37 ? 123  ALA A C   1 
ATOM   926  O O   . ALA A 1 123 ? -5.295  1.569   64.918 1.00 22.94 ? 123  ALA A O   1 
ATOM   927  C CB  . ALA A 1 123 ? -4.129  -1.193  65.821 1.00 24.64 ? 123  ALA A CB  1 
ATOM   928  N N   . ALA A 1 124 ? -5.904  0.124   63.310 1.00 23.68 ? 124  ALA A N   1 
ATOM   929  C CA  . ALA A 1 124 ? -7.075  0.907   62.950 1.00 23.12 ? 124  ALA A CA  1 
ATOM   930  C C   . ALA A 1 124 ? -8.108  0.859   64.068 1.00 23.83 ? 124  ALA A C   1 
ATOM   931  O O   . ALA A 1 124 ? -8.141  -0.098  64.833 1.00 24.13 ? 124  ALA A O   1 
ATOM   932  C CB  . ALA A 1 124 ? -7.686  0.406   61.658 1.00 22.82 ? 124  ALA A CB  1 
ATOM   933  N N   . ALA A 1 125 ? -8.922  1.911   64.138 1.00 24.13 ? 125  ALA A N   1 
ATOM   934  C CA  . ALA A 1 125 ? -10.110 1.990   65.005 1.00 25.31 ? 125  ALA A CA  1 
ATOM   935  C C   . ALA A 1 125 ? -11.297 1.337   64.300 1.00 25.59 ? 125  ALA A C   1 
ATOM   936  O O   . ALA A 1 125 ? -11.279 1.162   63.073 1.00 26.74 ? 125  ALA A O   1 
ATOM   937  C CB  . ALA A 1 125 ? -10.431 3.477   65.307 1.00 25.94 ? 125  ALA A CB  1 
ATOM   938  N N   . SER A 1 126 ? -12.332 0.985   65.060 1.00 26.10 ? 126  SER A N   1 
ATOM   939  C CA  . SER A 1 126 ? -13.622 0.519   64.504 1.00 25.89 ? 126  SER A CA  1 
ATOM   940  C C   . SER A 1 126 ? -13.501 -0.673  63.561 1.00 24.88 ? 126  SER A C   1 
ATOM   941  O O   . SER A 1 126 ? -14.083 -0.670  62.447 1.00 24.78 ? 126  SER A O   1 
ATOM   942  C CB  . SER A 1 126 ? -14.362 1.645   63.780 1.00 26.51 ? 126  SER A CB  1 
ATOM   943  O OG  . SER A 1 126 ? -14.570 2.762   64.627 1.00 30.06 ? 126  SER A OG  1 
ATOM   944  N N   . LEU A 1 127 ? -12.766 -1.698  63.992 1.00 22.84 ? 127  LEU A N   1 
ATOM   945  C CA  . LEU A 1 127 ? -12.558 -2.870  63.134 1.00 21.20 ? 127  LEU A CA  1 
ATOM   946  C C   . LEU A 1 127 ? -13.860 -3.568  62.833 1.00 21.14 ? 127  LEU A C   1 
ATOM   947  O O   . LEU A 1 127 ? -14.719 -3.678  63.715 1.00 21.00 ? 127  LEU A O   1 
ATOM   948  C CB  . LEU A 1 127 ? -11.632 -3.865  63.812 1.00 21.12 ? 127  LEU A CB  1 
ATOM   949  C CG  . LEU A 1 127 ? -10.266 -3.306  64.203 1.00 19.29 ? 127  LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 127 ? -9.483  -4.389  64.921 1.00 24.00 ? 127  LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 127 ? -9.533  -2.837  62.977 1.00 18.13 ? 127  LEU A CD2 1 
ATOM   952  N N   . THR A 1 128 ? -14.011 -4.043  61.600 1.00 19.40 ? 128  THR A N   1 
ATOM   953  C CA  . THR A 1 128 ? -15.178 -4.859  61.252 1.00 19.90 ? 128  THR A CA  1 
ATOM   954  C C   . THR A 1 128 ? -14.923 -6.336  61.579 1.00 19.05 ? 128  THR A C   1 
ATOM   955  O O   . THR A 1 128 ? -15.814 -7.190  61.457 1.00 17.02 ? 128  THR A O   1 
ATOM   956  C CB  . THR A 1 128 ? -15.532 -4.726  59.764 1.00 20.84 ? 128  THR A CB  1 
ATOM   957  O OG1 . THR A 1 128 ? -14.477 -5.281  58.989 1.00 22.06 ? 128  THR A OG1 1 
ATOM   958  C CG2 . THR A 1 128 ? -15.690 -3.278  59.386 1.00 22.33 ? 128  THR A CG2 1 
ATOM   959  N N   . TYR A 1 129 ? -13.688 -6.628  61.992 1.00 17.00 ? 129  TYR A N   1 
ATOM   960  C CA  . TYR A 1 129 ? -13.283 -7.996  62.268 1.00 18.24 ? 129  TYR A CA  1 
ATOM   961  C C   . TYR A 1 129 ? -12.616 -8.146  63.667 1.00 18.18 ? 129  TYR A C   1 
ATOM   962  O O   . TYR A 1 129 ? -12.179 -7.151  64.270 1.00 17.58 ? 129  TYR A O   1 
ATOM   963  C CB  . TYR A 1 129 ? -12.342 -8.490  61.155 1.00 17.08 ? 129  TYR A CB  1 
ATOM   964  C CG  . TYR A 1 129 ? -11.081 -7.658  61.041 1.00 17.23 ? 129  TYR A CG  1 
ATOM   965  C CD1 . TYR A 1 129 ? -9.953  -7.953  61.817 1.00 18.49 ? 129  TYR A CD1 1 
ATOM   966  C CD2 . TYR A 1 129 ? -11.027 -6.569  60.178 1.00 16.69 ? 129  TYR A CD2 1 
ATOM   967  C CE1 . TYR A 1 129 ? -8.808  -7.147  61.733 1.00 16.75 ? 129  TYR A CE1 1 
ATOM   968  C CE2 . TYR A 1 129 ? -9.874  -5.771  60.072 1.00 13.88 ? 129  TYR A CE2 1 
ATOM   969  C CZ  . TYR A 1 129 ? -8.780  -6.086  60.849 1.00 15.76 ? 129  TYR A CZ  1 
ATOM   970  O OH  . TYR A 1 129 ? -7.674  -5.276  60.720 1.00 19.22 ? 129  TYR A OH  1 
ATOM   971  N N   . GLN A 1 130 ? -12.528 -9.390  64.141 1.00 18.20 ? 130  GLN A N   1 
ATOM   972  C CA  . GLN A 1 130 ? -11.779 -9.730  65.346 1.00 19.50 ? 130  GLN A CA  1 
ATOM   973  C C   . GLN A 1 130 ? -10.830 -10.871 65.008 1.00 18.67 ? 130  GLN A C   1 
ATOM   974  O O   . GLN A 1 130 ? -11.166 -11.748 64.233 1.00 19.36 ? 130  GLN A O   1 
ATOM   975  C CB  . GLN A 1 130 ? -12.703 -10.167 66.467 1.00 20.31 ? 130  GLN A CB  1 
ATOM   976  C CG  . GLN A 1 130 ? -12.070 -10.219 67.847 1.00 26.12 ? 130  GLN A CG  1 
ATOM   977  C CD  . GLN A 1 130 ? -13.098 -10.429 68.934 1.00 33.14 ? 130  GLN A CD  1 
ATOM   978  O OE1 . GLN A 1 130 ? -14.308 -10.528 68.668 1.00 35.30 ? 130  GLN A OE1 1 
ATOM   979  N NE2 . GLN A 1 130 ? -12.629 -10.500 70.173 1.00 34.83 ? 130  GLN A NE2 1 
ATOM   980  N N   . VAL A 1 131 ? -9.668  -10.847 65.622 1.00 17.99 ? 131  VAL A N   1 
ATOM   981  C CA  . VAL A 1 131 ? -8.644  -11.885 65.418 1.00 17.09 ? 131  VAL A CA  1 
ATOM   982  C C   . VAL A 1 131 ? -8.496  -12.643 66.723 1.00 17.65 ? 131  VAL A C   1 
ATOM   983  O O   . VAL A 1 131 ? -8.479  -12.037 67.810 1.00 16.94 ? 131  VAL A O   1 
ATOM   984  C CB  . VAL A 1 131 ? -7.325  -11.256 64.992 1.00 16.47 ? 131  VAL A CB  1 
ATOM   985  C CG1 . VAL A 1 131 ? -6.216  -12.363 64.806 1.00 15.55 ? 131  VAL A CG1 1 
ATOM   986  C CG2 . VAL A 1 131 ? -7.548  -10.440 63.696 1.00 18.19 ? 131  VAL A CG2 1 
ATOM   987  N N   . GLU A 1 132 ? -8.444  -13.969 66.631 1.00 17.87 ? 132  GLU A N   1 
ATOM   988  C CA  . GLU A 1 132 ? -8.281  -14.820 67.811 1.00 20.48 ? 132  GLU A CA  1 
ATOM   989  C C   . GLU A 1 132 ? -7.127  -15.782 67.553 1.00 19.93 ? 132  GLU A C   1 
ATOM   990  O O   . GLU A 1 132 ? -7.044  -16.368 66.485 1.00 19.77 ? 132  GLU A O   1 
ATOM   991  C CB  . GLU A 1 132 ? -9.590  -15.553 68.144 1.00 21.86 ? 132  GLU A CB  1 
ATOM   992  C CG  . GLU A 1 132 ? -9.448  -16.926 68.763 1.00 29.71 ? 132  GLU A CG  1 
ATOM   993  C CD  . GLU A 1 132 ? -9.294  -16.907 70.273 1.00 36.57 ? 132  GLU A CD  1 
ATOM   994  O OE1 . GLU A 1 132 ? -9.017  -15.819 70.835 1.00 42.60 ? 132  GLU A OE1 1 
ATOM   995  O OE2 . GLU A 1 132 ? -9.459  -17.990 70.896 1.00 39.30 ? 132  GLU A OE2 1 
ATOM   996  N N   . ILE A 1 133 ? -6.208  -15.879 68.505 1.00 18.83 ? 133  ILE A N   1 
ATOM   997  C CA  . ILE A 1 133 ? -5.015  -16.759 68.364 1.00 17.83 ? 133  ILE A CA  1 
ATOM   998  C C   . ILE A 1 133 ? -5.129  -17.855 69.401 1.00 18.21 ? 133  ILE A C   1 
ATOM   999  O O   . ILE A 1 133 ? -5.339  -17.559 70.585 1.00 18.00 ? 133  ILE A O   1 
ATOM   1000 C CB  . ILE A 1 133 ? -3.695  -15.956 68.613 1.00 19.16 ? 133  ILE A CB  1 
ATOM   1001 C CG1 . ILE A 1 133 ? -3.576  -14.773 67.659 1.00 17.94 ? 133  ILE A CG1 1 
ATOM   1002 C CG2 . ILE A 1 133 ? -2.427  -16.884 68.527 1.00 18.15 ? 133  ILE A CG2 1 
ATOM   1003 C CD1 . ILE A 1 133 ? -3.528  -15.172 66.168 1.00 19.17 ? 133  ILE A CD1 1 
ATOM   1004 N N   . SER A 1 134 ? -5.039  -19.118 68.980 1.00 19.21 ? 134  SER A N   1 
ATOM   1005 C CA  . SER A 1 134 ? -4.924  -20.224 69.902 1.00 21.09 ? 134  SER A CA  1 
ATOM   1006 C C   . SER A 1 134 ? -3.467  -20.647 69.938 1.00 22.75 ? 134  SER A C   1 
ATOM   1007 O O   . SER A 1 134 ? -2.763  -20.549 68.936 1.00 21.99 ? 134  SER A O   1 
ATOM   1008 C CB  . SER A 1 134 ? -5.838  -21.381 69.483 1.00 21.75 ? 134  SER A CB  1 
ATOM   1009 O OG  . SER A 1 134 ? -7.192  -20.919 69.489 1.00 26.30 ? 134  SER A OG  1 
ATOM   1010 N N   . ARG A 1 135 ? -2.999  -21.086 71.095 1.00 24.12 ? 135  ARG A N   1 
ATOM   1011 C CA  . ARG A 1 135 ? -1.568  -21.291 71.227 1.00 26.32 ? 135  ARG A CA  1 
ATOM   1012 C C   . ARG A 1 135 ? -1.137  -22.752 71.199 1.00 26.18 ? 135  ARG A C   1 
ATOM   1013 O O   . ARG A 1 135 ? -0.009  -23.046 70.818 1.00 27.09 ? 135  ARG A O   1 
ATOM   1014 C CB  . ARG A 1 135 ? -1.049  -20.669 72.507 1.00 28.36 ? 135  ARG A CB  1 
ATOM   1015 C CG  . ARG A 1 135 ? -1.538  -19.266 72.883 1.00 32.33 ? 135  ARG A CG  1 
ATOM   1016 C CD  . ARG A 1 135 ? -1.615  -19.339 74.363 1.00 39.91 ? 135  ARG A CD  1 
ATOM   1017 N NE  . ARG A 1 135 ? -0.304  -19.687 74.875 1.00 43.37 ? 135  ARG A NE  1 
ATOM   1018 C CZ  . ARG A 1 135 ? 0.634   -18.780 75.127 1.00 44.96 ? 135  ARG A CZ  1 
ATOM   1019 N NH1 . ARG A 1 135 ? 0.376   -17.466 74.937 1.00 42.97 ? 135  ARG A NH1 1 
ATOM   1020 N NH2 . ARG A 1 135 ? 1.819   -19.190 75.567 1.00 45.17 ? 135  ARG A NH2 1 
ATOM   1021 N N   . GLN A 1 136 ? -2.000  -23.667 71.638 1.00 26.60 ? 136  GLN A N   1 
ATOM   1022 C CA  . GLN A 1 136 ? -1.568  -25.080 71.801 1.00 27.90 ? 136  GLN A CA  1 
ATOM   1023 C C   . GLN A 1 136 ? -2.556  -26.062 71.158 1.00 26.87 ? 136  GLN A C   1 
ATOM   1024 O O   . GLN A 1 136 ? -3.419  -26.589 71.838 1.00 29.18 ? 136  GLN A O   1 
ATOM   1025 C CB  . GLN A 1 136 ? -1.342  -25.440 73.284 1.00 27.92 ? 136  GLN A CB  1 
ATOM   1026 C CG  . GLN A 1 136 ? -0.789  -24.327 74.208 1.00 32.05 ? 136  GLN A CG  1 
ATOM   1027 C CD  . GLN A 1 136 ? 0.669   -23.955 73.950 1.00 38.30 ? 136  GLN A CD  1 
ATOM   1028 O OE1 . GLN A 1 136 ? 1.510   -24.817 73.658 1.00 39.14 ? 136  GLN A OE1 1 
ATOM   1029 N NE2 . GLN A 1 136 ? 0.979   -22.658 74.077 1.00 38.65 ? 136  GLN A NE2 1 
ATOM   1030 N N   . PRO A 1 137 ? -2.453  -26.305 69.842 1.00 25.98 ? 137  PRO A N   1 
ATOM   1031 C CA  . PRO A 1 137 ? -1.467  -25.851 68.873 1.00 24.58 ? 137  PRO A CA  1 
ATOM   1032 C C   . PRO A 1 137 ? -1.856  -24.495 68.283 1.00 23.75 ? 137  PRO A C   1 
ATOM   1033 O O   . PRO A 1 137 ? -2.978  -24.007 68.493 1.00 21.27 ? 137  PRO A O   1 
ATOM   1034 C CB  . PRO A 1 137 ? -1.522  -26.945 67.801 1.00 25.08 ? 137  PRO A CB  1 
ATOM   1035 C CG  . PRO A 1 137 ? -2.946  -27.434 67.851 1.00 25.48 ? 137  PRO A CG  1 
ATOM   1036 C CD  . PRO A 1 137 ? -3.498  -27.124 69.207 1.00 25.66 ? 137  PRO A CD  1 
ATOM   1037 N N   . PHE A 1 138 ? -0.922  -23.883 67.568 1.00 21.68 ? 138  PHE A N   1 
ATOM   1038 C CA  . PHE A 1 138 ? -1.183  -22.581 66.968 1.00 20.79 ? 138  PHE A CA  1 
ATOM   1039 C C   . PHE A 1 138 ? -2.331  -22.632 65.967 1.00 20.46 ? 138  PHE A C   1 
ATOM   1040 O O   . PHE A 1 138 ? -2.371  -23.491 65.078 1.00 19.85 ? 138  PHE A O   1 
ATOM   1041 C CB  . PHE A 1 138 ? 0.066   -22.053 66.251 1.00 20.43 ? 138  PHE A CB  1 
ATOM   1042 C CG  . PHE A 1 138 ? -0.207  -20.869 65.371 1.00 19.92 ? 138  PHE A CG  1 
ATOM   1043 C CD1 . PHE A 1 138 ? -0.239  -21.003 63.982 1.00 19.14 ? 138  PHE A CD1 1 
ATOM   1044 C CD2 . PHE A 1 138 ? -0.488  -19.634 65.928 1.00 21.09 ? 138  PHE A CD2 1 
ATOM   1045 C CE1 . PHE A 1 138 ? -0.519  -19.920 63.175 1.00 19.08 ? 138  PHE A CE1 1 
ATOM   1046 C CE2 . PHE A 1 138 ? -0.783  -18.545 65.106 1.00 20.92 ? 138  PHE A CE2 1 
ATOM   1047 C CZ  . PHE A 1 138 ? -0.769  -18.693 63.735 1.00 19.30 ? 138  PHE A CZ  1 
ATOM   1048 N N   . SER A 1 139 ? -3.261  -21.691 66.100 1.00 19.65 ? 139  SER A N   1 
ATOM   1049 C CA  . SER A 1 139 ? -4.131  -21.386 64.974 1.00 18.47 ? 139  SER A CA  1 
ATOM   1050 C C   . SER A 1 139 ? -4.502  -19.900 65.024 1.00 17.66 ? 139  SER A C   1 
ATOM   1051 O O   . SER A 1 139 ? -4.343  -19.236 66.064 1.00 17.96 ? 139  SER A O   1 
ATOM   1052 C CB  . SER A 1 139 ? -5.359  -22.291 64.948 1.00 19.19 ? 139  SER A CB  1 
ATOM   1053 O OG  . SER A 1 139 ? -6.185  -22.086 66.082 1.00 21.05 ? 139  SER A OG  1 
ATOM   1054 N N   . ILE A 1 140 ? -4.931  -19.373 63.885 1.00 15.68 ? 140  ILE A N   1 
ATOM   1055 C CA  . ILE A 1 140 ? -5.366  -17.983 63.785 1.00 16.31 ? 140  ILE A CA  1 
ATOM   1056 C C   . ILE A 1 140 ? -6.741  -17.964 63.158 1.00 16.02 ? 140  ILE A C   1 
ATOM   1057 O O   . ILE A 1 140 ? -6.986  -18.644 62.159 1.00 16.04 ? 140  ILE A O   1 
ATOM   1058 C CB  . ILE A 1 140 ? -4.389  -17.083 62.991 1.00 15.17 ? 140  ILE A CB  1 
ATOM   1059 C CG1 . ILE A 1 140 ? -4.884  -15.610 62.952 1.00 15.92 ? 140  ILE A CG1 1 
ATOM   1060 C CG2 . ILE A 1 140 ? -4.078  -17.656 61.568 1.00 15.84 ? 140  ILE A CG2 1 
ATOM   1061 C CD1 . ILE A 1 140 ? -3.814  -14.540 62.441 1.00 17.04 ? 140  ILE A CD1 1 
ATOM   1062 N N   . LYS A 1 141 ? -7.614  -17.142 63.728 1.00 16.91 ? 141  LYS A N   1 
ATOM   1063 C CA  . LYS A 1 141 ? -9.005  -17.068 63.291 1.00 17.85 ? 141  LYS A CA  1 
ATOM   1064 C C   . LYS A 1 141 ? -9.342  -15.596 63.078 1.00 16.52 ? 141  LYS A C   1 
ATOM   1065 O O   . LYS A 1 141 ? -8.869  -14.724 63.808 1.00 17.02 ? 141  LYS A O   1 
ATOM   1066 C CB  . LYS A 1 141 ? -9.943  -17.652 64.382 1.00 18.17 ? 141  LYS A CB  1 
ATOM   1067 C CG  . LYS A 1 141 ? -11.318 -17.984 63.858 1.00 23.48 ? 141  LYS A CG  1 
ATOM   1068 C CD  . LYS A 1 141 ? -12.344 -18.332 64.956 1.00 23.36 ? 141  LYS A CD  1 
ATOM   1069 C CE  . LYS A 1 141 ? -12.017 -19.600 65.715 1.00 31.22 ? 141  LYS A CE  1 
ATOM   1070 N NZ  . LYS A 1 141 ? -12.910 -19.668 66.952 1.00 35.92 ? 141  LYS A NZ  1 
ATOM   1071 N N   . VAL A 1 142 ? -10.122 -15.307 62.046 1.00 15.54 ? 142  VAL A N   1 
ATOM   1072 C CA  . VAL A 1 142 ? -10.566 -13.952 61.832 1.00 15.13 ? 142  VAL A CA  1 
ATOM   1073 C C   . VAL A 1 142 ? -12.067 -14.104 61.706 1.00 15.04 ? 142  VAL A C   1 
ATOM   1074 O O   . VAL A 1 142 ? -12.547 -14.896 60.904 1.00 14.59 ? 142  VAL A O   1 
ATOM   1075 C CB  . VAL A 1 142 ? -9.989  -13.313 60.566 1.00 15.68 ? 142  VAL A CB  1 
ATOM   1076 C CG1 . VAL A 1 142 ? -10.535 -11.884 60.382 1.00 15.12 ? 142  VAL A CG1 1 
ATOM   1077 C CG2 . VAL A 1 142 ? -8.431  -13.248 60.629 1.00 15.83 ? 142  VAL A CG2 1 
ATOM   1078 N N   . THR A 1 143 ? -12.783 -13.362 62.534 1.00 16.20 ? 143  THR A N   1 
ATOM   1079 C CA  . THR A 1 143 ? -14.244 -13.426 62.548 1.00 16.94 ? 143  THR A CA  1 
ATOM   1080 C C   . THR A 1 143 ? -14.809 -12.057 62.230 1.00 16.95 ? 143  THR A C   1 
ATOM   1081 O O   . THR A 1 143 ? -14.174 -11.034 62.514 1.00 18.14 ? 143  THR A O   1 
ATOM   1082 C CB  . THR A 1 143 ? -14.761 -13.872 63.925 1.00 17.66 ? 143  THR A CB  1 
ATOM   1083 O OG1 . THR A 1 143 ? -14.399 -12.877 64.906 1.00 23.80 ? 143  THR A OG1 1 
ATOM   1084 C CG2 . THR A 1 143 ? -14.104 -15.179 64.318 1.00 15.26 ? 143  THR A CG2 1 
ATOM   1085 N N   . ARG A 1 144 ? -16.001 -12.058 61.648 1.00 16.48 ? 144  ARG A N   1 
ATOM   1086 C CA  . ARG A 1 144 ? -16.762 -10.835 61.361 1.00 17.13 ? 144  ARG A CA  1 
ATOM   1087 C C   . ARG A 1 144 ? -17.417 -10.423 62.686 1.00 17.08 ? 144  ARG A C   1 
ATOM   1088 O O   . ARG A 1 144 ? -18.093 -11.241 63.320 1.00 17.20 ? 144  ARG A O   1 
ATOM   1089 C CB  . ARG A 1 144 ? -17.863 -11.127 60.347 1.00 16.47 ? 144  ARG A CB  1 
ATOM   1090 C CG  . ARG A 1 144 ? -18.648 -9.887  59.972 1.00 14.77 ? 144  ARG A CG  1 
ATOM   1091 C CD  . ARG A 1 144 ? -19.611 -10.172 58.840 1.00 15.34 ? 144  ARG A CD  1 
ATOM   1092 N NE  . ARG A 1 144 ? -18.956 -10.329 57.539 1.00 16.61 ? 144  ARG A NE  1 
ATOM   1093 C CZ  . ARG A 1 144 ? -18.494 -9.326  56.785 1.00 14.62 ? 144  ARG A CZ  1 
ATOM   1094 N NH1 . ARG A 1 144 ? -18.564 -8.069  57.182 1.00 17.93 ? 144  ARG A NH1 1 
ATOM   1095 N NH2 . ARG A 1 144 ? -17.923 -9.590  55.625 1.00 17.57 ? 144  ARG A NH2 1 
ATOM   1096 N N   . ARG A 1 145 ? -17.202 -9.176  63.098 1.00 18.55 ? 145  ARG A N   1 
ATOM   1097 C CA  A ARG A 1 145 ? -17.651 -8.702  64.414 0.50 19.47 ? 145  ARG A CA  1 
ATOM   1098 C CA  B ARG A 1 145 ? -17.638 -8.716  64.422 0.50 19.59 ? 145  ARG A CA  1 
ATOM   1099 C C   . ARG A 1 145 ? -19.167 -8.706  64.528 1.00 20.13 ? 145  ARG A C   1 
ATOM   1100 O O   . ARG A 1 145 ? -19.732 -9.181  65.532 1.00 19.74 ? 145  ARG A O   1 
ATOM   1101 C CB  A ARG A 1 145 ? -17.127 -7.298  64.692 0.50 19.67 ? 145  ARG A CB  1 
ATOM   1102 C CB  B ARG A 1 145 ? -17.034 -7.341  64.751 0.50 19.52 ? 145  ARG A CB  1 
ATOM   1103 C CG  A ARG A 1 145 ? -15.807 -7.247  65.448 0.50 21.31 ? 145  ARG A CG  1 
ATOM   1104 C CG  B ARG A 1 145 ? -16.753 -7.112  66.249 0.50 20.52 ? 145  ARG A CG  1 
ATOM   1105 C CD  A ARG A 1 145 ? -15.392 -5.811  65.725 0.50 24.77 ? 145  ARG A CD  1 
ATOM   1106 C CD  B ARG A 1 145 ? -15.771 -5.954  66.553 0.50 20.82 ? 145  ARG A CD  1 
ATOM   1107 N NE  A ARG A 1 145 ? -16.314 -5.058  66.590 0.50 25.77 ? 145  ARG A NE  1 
ATOM   1108 N NE  B ARG A 1 145 ? -14.347 -6.220  66.299 0.50 21.29 ? 145  ARG A NE  1 
ATOM   1109 C CZ  A ARG A 1 145 ? -16.194 -3.762  66.862 0.50 26.11 ? 145  ARG A CZ  1 
ATOM   1110 C CZ  B ARG A 1 145 ? -13.426 -6.420  67.244 0.50 23.27 ? 145  ARG A CZ  1 
ATOM   1111 N NH1 A ARG A 1 145 ? -15.201 -3.050  66.337 0.50 28.26 ? 145  ARG A NH1 1 
ATOM   1112 N NH1 B ARG A 1 145 ? -13.772 -6.405  68.529 0.50 25.49 ? 145  ARG A NH1 1 
ATOM   1113 N NH2 A ARG A 1 145 ? -17.066 -3.164  67.654 0.50 27.97 ? 145  ARG A NH2 1 
ATOM   1114 N NH2 B ARG A 1 145 ? -12.159 -6.644  66.911 0.50 19.38 ? 145  ARG A NH2 1 
ATOM   1115 N N   . SER A 1 146 ? -19.821 -8.198  63.487 1.00 20.30 ? 146  SER A N   1 
ATOM   1116 C CA  . SER A 1 146 ? -21.290 -8.039  63.509 1.00 20.32 ? 146  SER A CA  1 
ATOM   1117 C C   . SER A 1 146 ? -22.084 -9.319  63.835 1.00 20.94 ? 146  SER A C   1 
ATOM   1118 O O   . SER A 1 146 ? -22.990 -9.309  64.694 1.00 21.59 ? 146  SER A O   1 
ATOM   1119 C CB  . SER A 1 146 ? -21.737 -7.400  62.194 1.00 20.21 ? 146  SER A CB  1 
ATOM   1120 O OG  . SER A 1 146 ? -21.711 -8.337  61.144 1.00 17.93 ? 146  SER A OG  1 
ATOM   1121 N N   . ASN A 1 147 ? -21.738 -10.434 63.193 1.00 20.52 ? 147  ASN A N   1 
ATOM   1122 C CA  . ASN A 1 147 ? -22.464 -11.694 63.363 1.00 20.34 ? 147  ASN A CA  1 
ATOM   1123 C C   . ASN A 1 147 ? -21.615 -12.855 63.899 1.00 20.54 ? 147  ASN A C   1 
ATOM   1124 O O   . ASN A 1 147 ? -22.107 -13.974 64.020 1.00 20.27 ? 147  ASN A O   1 
ATOM   1125 C CB  . ASN A 1 147 ? -23.185 -12.092 62.070 1.00 20.78 ? 147  ASN A CB  1 
ATOM   1126 C CG  . ASN A 1 147 ? -22.220 -12.334 60.907 1.00 22.15 ? 147  ASN A CG  1 
ATOM   1127 O OD1 . ASN A 1 147 ? -20.981 -12.254 61.069 1.00 16.74 ? 147  ASN A OD1 1 
ATOM   1128 N ND2 . ASN A 1 147 ? -22.778 -12.645 59.744 1.00 21.86 ? 147  ASN A ND2 1 
ATOM   1129 N N   . ASN A 1 148 ? -20.367 -12.557 64.275 1.00 19.43 ? 148  ASN A N   1 
ATOM   1130 C CA  . ASN A 1 148 ? -19.372 -13.554 64.719 1.00 20.64 ? 148  ASN A CA  1 
ATOM   1131 C C   . ASN A 1 148 ? -19.144 -14.702 63.726 1.00 19.69 ? 148  ASN A C   1 
ATOM   1132 O O   . ASN A 1 148 ? -18.752 -15.801 64.128 1.00 19.75 ? 148  ASN A O   1 
ATOM   1133 C CB  . ASN A 1 148 ? -19.627 -14.056 66.171 1.00 21.88 ? 148  ASN A CB  1 
ATOM   1134 C CG  . ASN A 1 148 ? -19.205 -13.033 67.254 1.00 22.59 ? 148  ASN A CG  1 
ATOM   1135 O OD1 . ASN A 1 148 ? -19.612 -13.148 68.411 1.00 27.52 ? 148  ASN A OD1 1 
ATOM   1136 N ND2 . ASN A 1 148 ? -18.395 -12.057 66.889 1.00 21.10 ? 148  ASN A ND2 1 
ATOM   1137 N N   . ARG A 1 149 ? -19.336 -14.435 62.432 1.00 17.91 ? 149  ARG A N   1 
ATOM   1138 C CA  . ARG A 1 149 ? -19.128 -15.485 61.407 1.00 17.79 ? 149  ARG A CA  1 
ATOM   1139 C C   . ARG A 1 149 ? -17.625 -15.720 61.324 1.00 17.06 ? 149  ARG A C   1 
ATOM   1140 O O   . ARG A 1 149 ? -16.871 -14.762 61.169 1.00 16.94 ? 149  ARG A O   1 
ATOM   1141 C CB  . ARG A 1 149 ? -19.640 -15.044 60.044 1.00 18.17 ? 149  ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 149 ? -19.291 -15.975 58.885 1.00 21.91 ? 149  ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 149 ? -20.426 -16.916 58.568 1.00 29.40 ? 149  ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 149 ? -21.643 -16.172 58.226 1.00 32.25 ? 149  ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 149 ? -22.845 -16.726 58.124 1.00 37.26 ? 149  ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 149 ? -23.006 -18.039 58.335 1.00 37.80 ? 149  ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 149 ? -23.892 -15.967 57.819 1.00 37.44 ? 149  ARG A NH2 1 
ATOM   1148 N N   . VAL A 1 150 ? -17.207 -16.972 61.474 1.00 17.11 ? 150  VAL A N   1 
ATOM   1149 C CA  . VAL A 1 150 ? -15.777 -17.305 61.300 1.00 17.07 ? 150  VAL A CA  1 
ATOM   1150 C C   . VAL A 1 150 ? -15.461 -17.274 59.807 1.00 16.13 ? 150  VAL A C   1 
ATOM   1151 O O   . VAL A 1 150 ? -16.063 -18.013 59.003 1.00 16.11 ? 150  VAL A O   1 
ATOM   1152 C CB  . VAL A 1 150 ? -15.416 -18.677 61.910 1.00 18.13 ? 150  VAL A CB  1 
ATOM   1153 C CG1 . VAL A 1 150 ? -13.953 -19.003 61.616 1.00 18.04 ? 150  VAL A CG1 1 
ATOM   1154 C CG2 . VAL A 1 150 ? -15.661 -18.667 63.427 1.00 19.19 ? 150  VAL A CG2 1 
ATOM   1155 N N   . LEU A 1 151 ? -14.511 -16.415 59.432 1.00 14.42 ? 151  LEU A N   1 
ATOM   1156 C CA  . LEU A 1 151 ? -14.154 -16.218 58.035 1.00 14.33 ? 151  LEU A CA  1 
ATOM   1157 C C   . LEU A 1 151 ? -12.866 -16.988 57.682 1.00 16.24 ? 151  LEU A C   1 
ATOM   1158 O O   . LEU A 1 151 ? -12.835 -17.806 56.771 1.00 18.04 ? 151  LEU A O   1 
ATOM   1159 C CB  . LEU A 1 151 ? -13.931 -14.721 57.764 1.00 14.09 ? 151  LEU A CB  1 
ATOM   1160 C CG  . LEU A 1 151 ? -15.194 -13.851 58.065 1.00 13.93 ? 151  LEU A CG  1 
ATOM   1161 C CD1 . LEU A 1 151 ? -14.909 -12.422 57.610 1.00 14.17 ? 151  LEU A CD1 1 
ATOM   1162 C CD2 . LEU A 1 151 ? -16.347 -14.394 57.339 1.00 18.31 ? 151  LEU A CD2 1 
ATOM   1163 N N   . PHE A 1 152 ? -11.822 -16.694 58.432 1.00 16.37 ? 152  PHE A N   1 
ATOM   1164 C CA  . PHE A 1 152 ? -10.523 -17.391 58.288 1.00 17.62 ? 152  PHE A CA  1 
ATOM   1165 C C   . PHE A 1 152 ? -10.353 -18.201 59.569 1.00 17.19 ? 152  PHE A C   1 
ATOM   1166 O O   . PHE A 1 152 ? -10.606 -17.697 60.661 1.00 18.56 ? 152  PHE A O   1 
ATOM   1167 C CB  . PHE A 1 152 ? -9.444  -16.350 58.153 1.00 16.32 ? 152  PHE A CB  1 
ATOM   1168 C CG  . PHE A 1 152 ? -8.118  -16.895 57.649 1.00 19.00 ? 152  PHE A CG  1 
ATOM   1169 C CD1 . PHE A 1 152 ? -7.757  -16.773 56.304 1.00 17.50 ? 152  PHE A CD1 1 
ATOM   1170 C CD2 . PHE A 1 152 ? -7.255  -17.527 58.515 1.00 18.21 ? 152  PHE A CD2 1 
ATOM   1171 C CE1 . PHE A 1 152 ? -6.503  -17.250 55.820 1.00 20.05 ? 152  PHE A CE1 1 
ATOM   1172 C CE2 . PHE A 1 152 ? -6.004  -18.035 58.047 1.00 18.39 ? 152  PHE A CE2 1 
ATOM   1173 C CZ  . PHE A 1 152 ? -5.641  -17.899 56.710 1.00 18.79 ? 152  PHE A CZ  1 
ATOM   1174 N N   . ASP A 1 153 ? -10.015 -19.475 59.450 1.00 18.30 ? 153  ASP A N   1 
ATOM   1175 C CA  . ASP A 1 153 ? -9.752  -20.290 60.629 1.00 18.90 ? 153  ASP A CA  1 
ATOM   1176 C C   . ASP A 1 153 ? -8.754  -21.369 60.222 1.00 17.38 ? 153  ASP A C   1 
ATOM   1177 O O   . ASP A 1 153 ? -9.121  -22.328 59.543 1.00 17.02 ? 153  ASP A O   1 
ATOM   1178 C CB  . ASP A 1 153 ? -11.065 -20.947 61.112 1.00 19.14 ? 153  ASP A CB  1 
ATOM   1179 C CG  . ASP A 1 153 ? -10.868 -21.868 62.305 1.00 22.80 ? 153  ASP A CG  1 
ATOM   1180 O OD1 . ASP A 1 153 ? -9.745  -21.969 62.873 1.00 22.79 ? 153  ASP A OD1 1 
ATOM   1181 O OD2 . ASP A 1 153 ? -11.869 -22.515 62.688 1.00 27.16 ? 153  ASP A OD2 1 
ATOM   1182 N N   . SER A 1 154 ? -7.503  -21.199 60.627 1.00 18.27 ? 154  SER A N   1 
ATOM   1183 C CA  . SER A 1 154 ? -6.426  -22.140 60.272 1.00 17.80 ? 154  SER A CA  1 
ATOM   1184 C C   . SER A 1 154 ? -6.461  -23.448 61.099 1.00 18.87 ? 154  SER A C   1 
ATOM   1185 O O   . SER A 1 154 ? -5.697  -24.399 60.819 1.00 17.65 ? 154  SER A O   1 
ATOM   1186 C CB  . SER A 1 154 ? -5.062  -21.448 60.434 1.00 17.82 ? 154  SER A CB  1 
ATOM   1187 O OG  . SER A 1 154 ? -4.681  -21.409 61.818 1.00 18.64 ? 154  SER A OG  1 
ATOM   1188 N N   . SER A 1 155 ? -7.331  -23.519 62.124 1.00 18.99 ? 155  SER A N   1 
ATOM   1189 C CA  . SER A 1 155 ? -7.304  -24.661 63.044 1.00 19.48 ? 155  SER A CA  1 
ATOM   1190 C C   . SER A 1 155 ? -7.678  -26.013 62.406 1.00 18.89 ? 155  SER A C   1 
ATOM   1191 O O   . SER A 1 155 ? -7.491  -27.062 63.026 1.00 18.87 ? 155  SER A O   1 
ATOM   1192 C CB  . SER A 1 155 ? -8.194  -24.394 64.277 1.00 20.61 ? 155  SER A CB  1 
ATOM   1193 O OG  . SER A 1 155 ? -9.574  -24.408 63.894 1.00 21.83 ? 155  SER A OG  1 
ATOM   1194 N N   . ILE A 1 156 ? -8.189  -25.989 61.175 1.00 17.71 ? 156  ILE A N   1 
ATOM   1195 C CA  . ILE A 1 156 ? -8.519  -27.226 60.446 1.00 17.25 ? 156  ILE A CA  1 
ATOM   1196 C C   . ILE A 1 156 ? -7.264  -28.058 60.129 1.00 16.91 ? 156  ILE A C   1 
ATOM   1197 O O   . ILE A 1 156 ? -7.334  -29.264 59.998 1.00 17.15 ? 156  ILE A O   1 
ATOM   1198 C CB  . ILE A 1 156 ? -9.370  -26.934 59.167 1.00 17.15 ? 156  ILE A CB  1 
ATOM   1199 C CG1 . ILE A 1 156 ? -10.003 -28.229 58.650 1.00 16.87 ? 156  ILE A CG1 1 
ATOM   1200 C CG2 . ILE A 1 156 ? -8.620  -26.095 58.091 1.00 18.16 ? 156  ILE A CG2 1 
ATOM   1201 C CD1 . ILE A 1 156 ? -10.925 -28.041 57.452 1.00 15.10 ? 156  ILE A CD1 1 
ATOM   1202 N N   . GLY A 1 157 ? -6.123  -27.395 60.032 1.00 16.71 ? 157  GLY A N   1 
ATOM   1203 C CA  . GLY A 1 157 ? -4.908  -28.073 59.640 1.00 17.16 ? 157  GLY A CA  1 
ATOM   1204 C C   . GLY A 1 157 ? -3.716  -27.465 60.348 1.00 16.97 ? 157  GLY A C   1 
ATOM   1205 O O   . GLY A 1 157 ? -3.831  -26.511 61.118 1.00 16.36 ? 157  GLY A O   1 
ATOM   1206 N N   . PRO A 1 158 ? -2.560  -28.053 60.119 1.00 17.02 ? 158  PRO A N   1 
ATOM   1207 C CA  . PRO A 1 158 ? -1.307  -27.575 60.676 1.00 17.45 ? 158  PRO A CA  1 
ATOM   1208 C C   . PRO A 1 158 ? -0.807  -26.325 59.985 1.00 16.99 ? 158  PRO A C   1 
ATOM   1209 O O   . PRO A 1 158 ? -1.217  -26.010 58.864 1.00 17.87 ? 158  PRO A O   1 
ATOM   1210 C CB  . PRO A 1 158 ? -0.355  -28.754 60.384 1.00 16.85 ? 158  PRO A CB  1 
ATOM   1211 C CG  . PRO A 1 158 ? -0.841  -29.289 59.098 1.00 17.02 ? 158  PRO A CG  1 
ATOM   1212 C CD  . PRO A 1 158 ? -2.373  -29.257 59.292 1.00 17.32 ? 158  PRO A CD  1 
ATOM   1213 N N   . LEU A 1 159 ? 0.064   -25.592 60.660 1.00 17.33 ? 159  LEU A N   1 
ATOM   1214 C CA  . LEU A 1 159 ? 0.982   -24.732 59.960 1.00 15.95 ? 159  LEU A CA  1 
ATOM   1215 C C   . LEU A 1 159 ? 2.213   -25.562 59.640 1.00 17.15 ? 159  LEU A C   1 
ATOM   1216 O O   . LEU A 1 159 ? 2.782   -26.171 60.557 1.00 16.07 ? 159  LEU A O   1 
ATOM   1217 C CB  . LEU A 1 159 ? 1.404   -23.552 60.841 1.00 16.53 ? 159  LEU A CB  1 
ATOM   1218 C CG  . LEU A 1 159 ? 2.654   -22.756 60.402 1.00 15.23 ? 159  LEU A CG  1 
ATOM   1219 C CD1 . LEU A 1 159 ? 2.472   -22.091 59.006 1.00 15.23 ? 159  LEU A CD1 1 
ATOM   1220 C CD2 . LEU A 1 159 ? 3.032   -21.701 61.468 1.00 15.83 ? 159  LEU A CD2 1 
ATOM   1221 N N   . LEU A 1 160 ? 2.648   -25.551 58.368 1.00 16.69 ? 160  LEU A N   1 
ATOM   1222 C CA  . LEU A 1 160 ? 3.898   -26.247 57.970 1.00 17.34 ? 160  LEU A CA  1 
ATOM   1223 C C   . LEU A 1 160 ? 4.828   -25.181 57.447 1.00 18.16 ? 160  LEU A C   1 
ATOM   1224 O O   . LEU A 1 160 ? 4.401   -24.318 56.685 1.00 17.31 ? 160  LEU A O   1 
ATOM   1225 C CB  . LEU A 1 160 ? 3.626   -27.343 56.927 1.00 16.92 ? 160  LEU A CB  1 
ATOM   1226 C CG  . LEU A 1 160 ? 2.578   -28.359 57.444 1.00 18.92 ? 160  LEU A CG  1 
ATOM   1227 C CD1 . LEU A 1 160 ? 2.129   -29.288 56.348 1.00 23.31 ? 160  LEU A CD1 1 
ATOM   1228 C CD2 . LEU A 1 160 ? 3.102   -29.156 58.623 1.00 22.09 ? 160  LEU A CD2 1 
ATOM   1229 N N   . PHE A 1 161 ? 6.089   -25.186 57.906 1.00 18.76 ? 161  PHE A N   1 
ATOM   1230 C CA  . PHE A 1 161 ? 7.008   -24.149 57.495 1.00 19.50 ? 161  PHE A CA  1 
ATOM   1231 C C   . PHE A 1 161 ? 8.432   -24.704 57.399 1.00 20.23 ? 161  PHE A C   1 
ATOM   1232 O O   . PHE A 1 161 ? 9.203   -24.589 58.355 1.00 21.19 ? 161  PHE A O   1 
ATOM   1233 C CB  . PHE A 1 161 ? 6.954   -22.993 58.506 1.00 20.13 ? 161  PHE A CB  1 
ATOM   1234 C CG  . PHE A 1 161 ? 7.445   -21.665 57.980 1.00 22.16 ? 161  PHE A CG  1 
ATOM   1235 C CD1 . PHE A 1 161 ? 6.709   -20.504 58.227 1.00 26.98 ? 161  PHE A CD1 1 
ATOM   1236 C CD2 . PHE A 1 161 ? 8.608   -21.567 57.227 1.00 25.55 ? 161  PHE A CD2 1 
ATOM   1237 C CE1 . PHE A 1 161 ? 7.147   -19.271 57.742 1.00 27.46 ? 161  PHE A CE1 1 
ATOM   1238 C CE2 . PHE A 1 161 ? 9.080   -20.343 56.757 1.00 26.00 ? 161  PHE A CE2 1 
ATOM   1239 C CZ  . PHE A 1 161 ? 8.360   -19.188 57.016 1.00 25.13 ? 161  PHE A CZ  1 
ATOM   1240 N N   . ALA A 1 162 ? 8.754   -25.309 56.263 1.00 20.49 ? 162  ALA A N   1 
ATOM   1241 C CA  . ALA A 1 162 ? 10.146  -25.662 55.934 1.00 20.55 ? 162  ALA A CA  1 
ATOM   1242 C C   . ALA A 1 162 ? 10.673  -24.710 54.872 1.00 20.66 ? 162  ALA A C   1 
ATOM   1243 O O   . ALA A 1 162 ? 9.910   -23.962 54.267 1.00 20.98 ? 162  ALA A O   1 
ATOM   1244 C CB  . ALA A 1 162 ? 10.208  -27.078 55.465 1.00 20.32 ? 162  ALA A CB  1 
ATOM   1245 N N   . ASP A 1 163 ? 11.980  -24.725 54.616 1.00 19.93 ? 163  ASP A N   1 
ATOM   1246 C CA  . ASP A 1 163 ? 12.548  -23.785 53.686 1.00 19.91 ? 163  ASP A CA  1 
ATOM   1247 C C   . ASP A 1 163 ? 11.849  -23.852 52.323 1.00 18.70 ? 163  ASP A C   1 
ATOM   1248 O O   . ASP A 1 163 ? 11.616  -22.817 51.689 1.00 18.83 ? 163  ASP A O   1 
ATOM   1249 C CB  . ASP A 1 163 ? 14.042  -24.098 53.536 1.00 21.45 ? 163  ASP A CB  1 
ATOM   1250 C CG  . ASP A 1 163 ? 14.806  -23.049 52.747 1.00 24.82 ? 163  ASP A CG  1 
ATOM   1251 O OD1 . ASP A 1 163 ? 14.584  -21.818 52.884 1.00 27.99 ? 163  ASP A OD1 1 
ATOM   1252 O OD2 . ASP A 1 163 ? 15.708  -23.474 52.001 1.00 28.59 ? 163  ASP A OD2 1 
ATOM   1253 N N   . GLN A 1 164 ? 11.506  -25.066 51.874 1.00 17.13 ? 164  GLN A N   1 
ATOM   1254 C CA  . GLN A 1 164 ? 10.885  -25.202 50.550 1.00 17.20 ? 164  GLN A CA  1 
ATOM   1255 C C   . GLN A 1 164 ? 9.540   -25.862 50.600 1.00 16.15 ? 164  GLN A C   1 
ATOM   1256 O O   . GLN A 1 164 ? 9.123   -26.506 49.638 1.00 16.81 ? 164  GLN A O   1 
ATOM   1257 C CB  . GLN A 1 164 ? 11.809  -25.956 49.589 1.00 17.81 ? 164  GLN A CB  1 
ATOM   1258 C CG  . GLN A 1 164 ? 13.114  -25.240 49.397 1.00 17.67 ? 164  GLN A CG  1 
ATOM   1259 C CD  . GLN A 1 164 ? 13.969  -25.920 48.350 1.00 17.56 ? 164  GLN A CD  1 
ATOM   1260 O OE1 . GLN A 1 164 ? 13.720  -25.820 47.131 1.00 19.68 ? 164  GLN A OE1 1 
ATOM   1261 N NE2 . GLN A 1 164 ? 14.916  -26.694 48.816 1.00 18.39 ? 164  GLN A NE2 1 
ATOM   1262 N N   . PHE A 1 165 ? 8.842   -25.713 51.727 1.00 16.49 ? 165  PHE A N   1 
ATOM   1263 C CA  . PHE A 1 165 ? 7.461   -26.230 51.837 1.00 16.38 ? 165  PHE A CA  1 
ATOM   1264 C C   . PHE A 1 165 ? 6.745   -25.473 52.954 1.00 16.30 ? 165  PHE A C   1 
ATOM   1265 O O   . PHE A 1 165 ? 7.048   -25.650 54.144 1.00 16.73 ? 165  PHE A O   1 
ATOM   1266 C CB  . PHE A 1 165 ? 7.403   -27.752 52.074 1.00 16.71 ? 165  PHE A CB  1 
ATOM   1267 C CG  . PHE A 1 165 ? 6.006   -28.349 51.936 1.00 18.21 ? 165  PHE A CG  1 
ATOM   1268 C CD1 . PHE A 1 165 ? 5.538   -28.795 50.705 1.00 18.30 ? 165  PHE A CD1 1 
ATOM   1269 C CD2 . PHE A 1 165 ? 5.187   -28.468 53.042 1.00 20.46 ? 165  PHE A CD2 1 
ATOM   1270 C CE1 . PHE A 1 165 ? 4.245   -29.373 50.595 1.00 22.15 ? 165  PHE A CE1 1 
ATOM   1271 C CE2 . PHE A 1 165 ? 3.894   -29.026 52.939 1.00 20.54 ? 165  PHE A CE2 1 
ATOM   1272 C CZ  . PHE A 1 165 ? 3.438   -29.479 51.732 1.00 18.87 ? 165  PHE A CZ  1 
ATOM   1273 N N   . LEU A 1 166 ? 5.785   -24.623 52.566 1.00 15.52 ? 166  LEU A N   1 
ATOM   1274 C CA  . LEU A 1 166 ? 5.032   -23.817 53.540 1.00 15.14 ? 166  LEU A CA  1 
ATOM   1275 C C   . LEU A 1 166 ? 3.560   -24.084 53.260 1.00 14.67 ? 166  LEU A C   1 
ATOM   1276 O O   . LEU A 1 166 ? 3.177   -24.120 52.108 1.00 14.51 ? 166  LEU A O   1 
ATOM   1277 C CB  . LEU A 1 166 ? 5.351   -22.333 53.386 1.00 14.20 ? 166  LEU A CB  1 
ATOM   1278 C CG  . LEU A 1 166 ? 6.778   -21.832 53.648 1.00 17.28 ? 166  LEU A CG  1 
ATOM   1279 C CD1 . LEU A 1 166 ? 7.594   -22.013 52.406 1.00 16.93 ? 166  LEU A CD1 1 
ATOM   1280 C CD2 . LEU A 1 166 ? 6.722   -20.362 54.019 1.00 14.90 ? 166  LEU A CD2 1 
ATOM   1281 N N   . GLN A 1 167 ? 2.772   -24.372 54.290 1.00 15.02 ? 167  GLN A N   1 
ATOM   1282 C CA  . GLN A 1 167 ? 1.357   -24.661 54.075 1.00 14.08 ? 167  GLN A CA  1 
ATOM   1283 C C   . GLN A 1 167 ? 0.530   -24.088 55.216 1.00 14.15 ? 167  GLN A C   1 
ATOM   1284 O O   . GLN A 1 167 ? 0.885   -24.222 56.397 1.00 13.27 ? 167  GLN A O   1 
ATOM   1285 C CB  . GLN A 1 167 ? 1.098   -26.183 53.985 1.00 15.15 ? 167  GLN A CB  1 
ATOM   1286 C CG  . GLN A 1 167 ? -0.394  -26.587 53.845 1.00 15.17 ? 167  GLN A CG  1 
ATOM   1287 C CD  . GLN A 1 167 ? -0.563  -28.086 53.694 1.00 14.86 ? 167  GLN A CD  1 
ATOM   1288 O OE1 . GLN A 1 167 ? -1.293  -28.735 54.476 1.00 18.86 ? 167  GLN A OE1 1 
ATOM   1289 N NE2 . GLN A 1 167 ? 0.120   -28.651 52.733 1.00 13.96 ? 167  GLN A NE2 1 
ATOM   1290 N N   . LEU A 1 168 ? -0.593  -23.464 54.864 1.00 14.03 ? 168  LEU A N   1 
ATOM   1291 C CA  . LEU A 1 168 ? -1.606  -23.110 55.871 1.00 15.23 ? 168  LEU A CA  1 
ATOM   1292 C C   . LEU A 1 168 ? -2.968  -23.318 55.227 1.00 15.37 ? 168  LEU A C   1 
ATOM   1293 O O   . LEU A 1 168 ? -3.104  -23.083 54.030 1.00 14.80 ? 168  LEU A O   1 
ATOM   1294 C CB  . LEU A 1 168 ? -1.463  -21.625 56.281 1.00 15.92 ? 168  LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 168 ? -2.184  -21.148 57.576 1.00 14.86 ? 168  LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 168 ? -1.724  -21.851 58.871 1.00 18.25 ? 168  LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 168 ? -2.055  -19.621 57.696 1.00 16.36 ? 168  LEU A CD2 1 
ATOM   1298 N N   . SER A 1 169 ? -3.953  -23.750 56.017 1.00 16.08 ? 169  SER A N   1 
ATOM   1299 C CA  . SER A 1 169 ? -5.295  -23.991 55.531 1.00 17.10 ? 169  SER A CA  1 
ATOM   1300 C C   . SER A 1 169 ? -6.246  -23.018 56.193 1.00 17.20 ? 169  SER A C   1 
ATOM   1301 O O   . SER A 1 169 ? -5.928  -22.450 57.199 1.00 18.24 ? 169  SER A O   1 
ATOM   1302 C CB  . SER A 1 169 ? -5.773  -25.386 55.924 1.00 16.50 ? 169  SER A CB  1 
ATOM   1303 O OG  . SER A 1 169 ? -4.892  -26.383 55.487 1.00 19.18 ? 169  SER A OG  1 
ATOM   1304 N N   . THR A 1 170 ? -7.427  -22.856 55.618 1.00 17.67 ? 170  THR A N   1 
ATOM   1305 C CA  . THR A 1 170 ? -8.489  -22.132 56.312 1.00 17.40 ? 170  THR A CA  1 
ATOM   1306 C C   . THR A 1 170 ? -9.850  -22.775 56.038 1.00 17.30 ? 170  THR A C   1 
ATOM   1307 O O   . THR A 1 170 ? -10.169 -23.112 54.887 1.00 16.51 ? 170  THR A O   1 
ATOM   1308 C CB  . THR A 1 170 ? -8.514  -20.651 55.941 1.00 18.03 ? 170  THR A CB  1 
ATOM   1309 O OG1 . THR A 1 170 ? -9.609  -20.006 56.633 1.00 18.77 ? 170  THR A OG1 1 
ATOM   1310 C CG2 . THR A 1 170 ? -8.654  -20.440 54.413 1.00 18.02 ? 170  THR A CG2 1 
ATOM   1311 N N   . ARG A 1 171 ? -10.641 -22.950 57.083 1.00 16.72 ? 171  ARG A N   1 
ATOM   1312 C CA  . ARG A 1 171 ? -12.069 -23.216 56.872 1.00 17.25 ? 171  ARG A CA  1 
ATOM   1313 C C   . ARG A 1 171 ? -12.662 -22.030 56.128 1.00 16.54 ? 171  ARG A C   1 
ATOM   1314 O O   . ARG A 1 171 ? -12.130 -20.900 56.186 1.00 17.78 ? 171  ARG A O   1 
ATOM   1315 C CB  . ARG A 1 171 ? -12.810 -23.380 58.200 1.00 16.57 ? 171  ARG A CB  1 
ATOM   1316 C CG  . ARG A 1 171 ? -12.325 -24.485 59.079 1.00 19.23 ? 171  ARG A CG  1 
ATOM   1317 C CD  . ARG A 1 171 ? -13.128 -24.546 60.363 1.00 24.06 ? 171  ARG A CD  1 
ATOM   1318 N NE  . ARG A 1 171 ? -12.241 -24.943 61.467 1.00 27.63 ? 171  ARG A NE  1 
ATOM   1319 C CZ  . ARG A 1 171 ? -12.042 -26.195 61.826 1.00 27.70 ? 171  ARG A CZ  1 
ATOM   1320 N NH1 . ARG A 1 171 ? -12.679 -27.171 61.202 1.00 30.62 ? 171  ARG A NH1 1 
ATOM   1321 N NH2 . ARG A 1 171 ? -11.220 -26.467 62.824 1.00 31.91 ? 171  ARG A NH2 1 
ATOM   1322 N N   . LEU A 1 172 ? -13.791 -22.272 55.483 1.00 16.28 ? 172  LEU A N   1 
ATOM   1323 C CA  . LEU A 1 172 ? -14.524 -21.219 54.803 1.00 15.58 ? 172  LEU A CA  1 
ATOM   1324 C C   . LEU A 1 172 ? -15.957 -21.264 55.253 1.00 15.83 ? 172  LEU A C   1 
ATOM   1325 O O   . LEU A 1 172 ? -16.443 -22.317 55.630 1.00 14.64 ? 172  LEU A O   1 
ATOM   1326 C CB  . LEU A 1 172 ? -14.420 -21.371 53.278 1.00 16.09 ? 172  LEU A CB  1 
ATOM   1327 C CG  . LEU A 1 172 ? -12.995 -21.217 52.689 1.00 17.37 ? 172  LEU A CG  1 
ATOM   1328 C CD1 . LEU A 1 172 ? -13.014 -21.649 51.230 1.00 21.29 ? 172  LEU A CD1 1 
ATOM   1329 C CD2 . LEU A 1 172 ? -12.476 -19.800 52.835 1.00 16.06 ? 172  LEU A CD2 1 
ATOM   1330 N N   . PRO A 1 173 ? -16.622 -20.102 55.277 1.00 17.17 ? 173  PRO A N   1 
ATOM   1331 C CA  . PRO A 1 173 ? -18.003 -20.067 55.748 1.00 18.17 ? 173  PRO A CA  1 
ATOM   1332 C C   . PRO A 1 173 ? -19.056 -20.510 54.743 1.00 19.68 ? 173  PRO A C   1 
ATOM   1333 O O   . PRO A 1 173 ? -20.230 -20.682 55.141 1.00 19.71 ? 173  PRO A O   1 
ATOM   1334 C CB  . PRO A 1 173 ? -18.194 -18.589 56.144 1.00 18.33 ? 173  PRO A CB  1 
ATOM   1335 C CG  . PRO A 1 173 ? -17.326 -17.824 55.202 1.00 17.08 ? 173  PRO A CG  1 
ATOM   1336 C CD  . PRO A 1 173 ? -16.099 -18.754 54.965 1.00 17.21 ? 173  PRO A CD  1 
ATOM   1337 N N   . SER A 1 174 ? -18.676 -20.666 53.467 1.00 18.56 ? 174  SER A N   1 
ATOM   1338 C CA  . SER A 1 174 ? -19.575 -21.118 52.440 1.00 20.48 ? 174  SER A CA  1 
ATOM   1339 C C   . SER A 1 174 ? -18.788 -21.708 51.275 1.00 20.47 ? 174  SER A C   1 
ATOM   1340 O O   . SER A 1 174 ? -17.544 -21.660 51.240 1.00 21.46 ? 174  SER A O   1 
ATOM   1341 C CB  . SER A 1 174 ? -20.467 -19.954 51.928 1.00 19.77 ? 174  SER A CB  1 
ATOM   1342 O OG  . SER A 1 174 ? -19.724 -19.155 51.028 1.00 19.46 ? 174  SER A OG  1 
ATOM   1343 N N   . THR A 1 175 ? -19.531 -22.268 50.336 1.00 19.28 ? 175  THR A N   1 
ATOM   1344 C CA  . THR A 1 175 ? -18.967 -22.781 49.113 1.00 20.20 ? 175  THR A CA  1 
ATOM   1345 C C   . THR A 1 175 ? -19.028 -21.780 47.954 1.00 19.35 ? 175  THR A C   1 
ATOM   1346 O O   . THR A 1 175 ? -18.662 -22.130 46.824 1.00 20.27 ? 175  THR A O   1 
ATOM   1347 C CB  . THR A 1 175 ? -19.665 -24.123 48.706 1.00 21.36 ? 175  THR A CB  1 
ATOM   1348 O OG1 . THR A 1 175 ? -21.070 -23.891 48.590 1.00 22.70 ? 175  THR A OG1 1 
ATOM   1349 C CG2 . THR A 1 175 ? -19.434 -25.187 49.781 1.00 22.38 ? 175  THR A CG2 1 
ATOM   1350 N N   . ASN A 1 176 ? -19.462 -20.539 48.213 1.00 16.98 ? 176  ASN A N   1 
ATOM   1351 C CA  . ASN A 1 176 ? -19.501 -19.537 47.149 1.00 15.59 ? 176  ASN A CA  1 
ATOM   1352 C C   . ASN A 1 176 ? -18.125 -18.914 47.080 1.00 14.90 ? 176  ASN A C   1 
ATOM   1353 O O   . ASN A 1 176 ? -17.886 -17.910 47.708 1.00 13.69 ? 176  ASN A O   1 
ATOM   1354 C CB  . ASN A 1 176 ? -20.512 -18.448 47.476 1.00 14.92 ? 176  ASN A CB  1 
ATOM   1355 C CG  . ASN A 1 176 ? -21.868 -19.014 47.760 1.00 18.66 ? 176  ASN A CG  1 
ATOM   1356 O OD1 . ASN A 1 176 ? -22.302 -19.942 47.076 1.00 19.09 ? 176  ASN A OD1 1 
ATOM   1357 N ND2 . ASN A 1 176 ? -22.536 -18.493 48.787 1.00 19.37 ? 176  ASN A ND2 1 
ATOM   1358 N N   . VAL A 1 177 ? -17.233 -19.540 46.332 1.00 14.88 ? 177  VAL A N   1 
ATOM   1359 C CA  . VAL A 1 177 ? -15.801 -19.187 46.332 1.00 13.99 ? 177  VAL A CA  1 
ATOM   1360 C C   . VAL A 1 177 ? -15.395 -18.883 44.879 1.00 13.80 ? 177  VAL A C   1 
ATOM   1361 O O   . VAL A 1 177 ? -15.721 -19.662 43.983 1.00 13.56 ? 177  VAL A O   1 
ATOM   1362 C CB  . VAL A 1 177 ? -14.995 -20.350 46.875 1.00 15.23 ? 177  VAL A CB  1 
ATOM   1363 C CG1 . VAL A 1 177 ? -13.485 -20.081 46.638 1.00 14.40 ? 177  VAL A CG1 1 
ATOM   1364 C CG2 . VAL A 1 177 ? -15.312 -20.544 48.384 1.00 18.02 ? 177  VAL A CG2 1 
ATOM   1365 N N   . TYR A 1 178 ? -14.738 -17.735 44.631 1.00 12.77 ? 178  TYR A N   1 
ATOM   1366 C CA  . TYR A 1 178 ? -14.512 -17.273 43.250 1.00 12.27 ? 178  TYR A CA  1 
ATOM   1367 C C   . TYR A 1 178 ? -13.097 -16.727 43.188 1.00 12.49 ? 178  TYR A C   1 
ATOM   1368 O O   . TYR A 1 178 ? -12.697 -16.016 44.085 1.00 13.32 ? 178  TYR A O   1 
ATOM   1369 C CB  . TYR A 1 178 ? -15.457 -16.091 42.885 1.00 11.81 ? 178  TYR A CB  1 
ATOM   1370 C CG  . TYR A 1 178 ? -16.884 -16.424 43.196 1.00 11.09 ? 178  TYR A CG  1 
ATOM   1371 C CD1 . TYR A 1 178 ? -17.668 -17.096 42.283 1.00 11.41 ? 178  TYR A CD1 1 
ATOM   1372 C CD2 . TYR A 1 178 ? -17.431 -16.075 44.427 1.00 11.57 ? 178  TYR A CD2 1 
ATOM   1373 C CE1 . TYR A 1 178 ? -18.997 -17.453 42.602 1.00 10.19 ? 178  TYR A CE1 1 
ATOM   1374 C CE2 . TYR A 1 178 ? -18.771 -16.411 44.755 1.00 11.95 ? 178  TYR A CE2 1 
ATOM   1375 C CZ  . TYR A 1 178 ? -19.509 -17.108 43.843 1.00 10.64 ? 178  TYR A CZ  1 
ATOM   1376 O OH  . TYR A 1 178 ? -20.843 -17.417 44.131 1.00 14.04 ? 178  TYR A OH  1 
ATOM   1377 N N   . GLY A 1 179 ? -12.363 -17.019 42.121 1.00 13.58 ? 179  GLY A N   1 
ATOM   1378 C CA  . GLY A 1 179 ? -11.002 -16.438 42.011 1.00 12.04 ? 179  GLY A CA  1 
ATOM   1379 C C   . GLY A 1 179 ? -9.949  -17.503 41.786 1.00 13.17 ? 179  GLY A C   1 
ATOM   1380 O O   . GLY A 1 179 ? -10.270 -18.605 41.361 1.00 13.48 ? 179  GLY A O   1 
ATOM   1381 N N   . LEU A 1 180 ? -8.705  -17.162 42.112 1.00 12.76 ? 180  LEU A N   1 
ATOM   1382 C CA  . LEU A 1 180 ? -7.515  -17.986 41.865 1.00 14.34 ? 180  LEU A CA  1 
ATOM   1383 C C   . LEU A 1 180 ? -7.209  -17.974 40.389 1.00 14.34 ? 180  LEU A C   1 
ATOM   1384 O O   . LEU A 1 180 ? -8.112  -17.897 39.548 1.00 15.10 ? 180  LEU A O   1 
ATOM   1385 C CB  . LEU A 1 180 ? -7.653  -19.427 42.371 1.00 14.09 ? 180  LEU A CB  1 
ATOM   1386 C CG  . LEU A 1 180 ? -8.077  -19.607 43.839 1.00 15.32 ? 180  LEU A CG  1 
ATOM   1387 C CD1 . LEU A 1 180 ? -8.397  -21.080 44.076 1.00 19.10 ? 180  LEU A CD1 1 
ATOM   1388 C CD2 . LEU A 1 180 ? -7.043  -19.071 44.850 1.00 16.90 ? 180  LEU A CD2 1 
ATOM   1389 N N   . GLY A 1 181 ? -5.930  -18.049 40.045 1.00 13.44 ? 181  GLY A N   1 
ATOM   1390 C CA  . GLY A 1 181 ? -5.570  -17.972 38.644 1.00 13.71 ? 181  GLY A CA  1 
ATOM   1391 C C   . GLY A 1 181 ? -4.066  -18.116 38.463 1.00 13.99 ? 181  GLY A C   1 
ATOM   1392 O O   . GLY A 1 181 ? -3.354  -18.123 39.443 1.00 14.74 ? 181  GLY A O   1 
ATOM   1393 N N   . GLU A 1 182 ? -3.595  -18.181 37.219 1.00 14.47 ? 182  GLU A N   1 
ATOM   1394 C CA  . GLU A 1 182 ? -4.471  -18.175 36.030 1.00 14.78 ? 182  GLU A CA  1 
ATOM   1395 C C   . GLU A 1 182 ? -4.810  -19.591 35.581 1.00 15.08 ? 182  GLU A C   1 
ATOM   1396 O O   . GLU A 1 182 ? -3.914  -20.407 35.442 1.00 14.61 ? 182  GLU A O   1 
ATOM   1397 C CB  . GLU A 1 182 ? -3.816  -17.449 34.876 1.00 15.82 ? 182  GLU A CB  1 
ATOM   1398 C CG  . GLU A 1 182 ? -4.768  -17.273 33.705 1.00 14.60 ? 182  GLU A CG  1 
ATOM   1399 C CD  . GLU A 1 182 ? -4.216  -16.337 32.645 1.00 21.16 ? 182  GLU A CD  1 
ATOM   1400 O OE1 . GLU A 1 182 ? -3.021  -15.947 32.736 1.00 20.52 ? 182  GLU A OE1 1 
ATOM   1401 O OE2 . GLU A 1 182 ? -4.976  -16.008 31.717 1.00 20.58 ? 182  GLU A OE2 1 
ATOM   1402 N N   . HIS A 1 183 ? -6.099  -19.897 35.405 1.00 14.38 ? 183  HIS A N   1 
ATOM   1403 C CA  . HIS A 1 183 ? -6.508  -21.262 35.044 1.00 14.87 ? 183  HIS A CA  1 
ATOM   1404 C C   . HIS A 1 183 ? -7.747  -21.163 34.154 1.00 15.57 ? 183  HIS A C   1 
ATOM   1405 O O   . HIS A 1 183 ? -8.396  -20.106 34.081 1.00 15.86 ? 183  HIS A O   1 
ATOM   1406 C CB  . HIS A 1 183 ? -6.920  -22.143 36.274 1.00 15.36 ? 183  HIS A CB  1 
ATOM   1407 C CG  . HIS A 1 183 ? -6.042  -22.014 37.479 1.00 16.06 ? 183  HIS A CG  1 
ATOM   1408 N ND1 . HIS A 1 183 ? -4.768  -22.556 37.552 1.00 17.69 ? 183  HIS A ND1 1 
ATOM   1409 C CD2 . HIS A 1 183 ? -6.293  -21.482 38.688 1.00 10.73 ? 183  HIS A CD2 1 
ATOM   1410 C CE1 . HIS A 1 183 ? -4.246  -22.279 38.730 1.00 12.10 ? 183  HIS A CE1 1 
ATOM   1411 N NE2 . HIS A 1 183 ? -5.143  -21.606 39.431 1.00 16.90 ? 183  HIS A NE2 1 
ATOM   1412 N N   . VAL A 1 184 ? -8.113  -22.277 33.527 1.00 14.86 ? 184  VAL A N   1 
ATOM   1413 C CA  . VAL A 1 184 ? -9.450  -22.406 32.930 1.00 15.39 ? 184  VAL A CA  1 
ATOM   1414 C C   . VAL A 1 184 ? -10.252 -23.244 33.943 1.00 15.87 ? 184  VAL A C   1 
ATOM   1415 O O   . VAL A 1 184 ? -10.074 -24.460 34.051 1.00 16.10 ? 184  VAL A O   1 
ATOM   1416 C CB  . VAL A 1 184 ? -9.402  -23.029 31.496 1.00 14.86 ? 184  VAL A CB  1 
ATOM   1417 C CG1 . VAL A 1 184 ? -10.814 -23.472 30.992 1.00 14.77 ? 184  VAL A CG1 1 
ATOM   1418 C CG2 . VAL A 1 184 ? -8.729  -22.063 30.508 1.00 13.68 ? 184  VAL A CG2 1 
ATOM   1419 N N   . HIS A 1 185 ? -11.079 -22.590 34.752 1.00 16.17 ? 185  HIS A N   1 
ATOM   1420 C CA  . HIS A 1 185 ? -11.842 -23.327 35.778 1.00 16.12 ? 185  HIS A CA  1 
ATOM   1421 C C   . HIS A 1 185 ? -13.086 -23.967 35.191 1.00 16.95 ? 185  HIS A C   1 
ATOM   1422 O O   . HIS A 1 185 ? -13.687 -24.847 35.823 1.00 18.19 ? 185  HIS A O   1 
ATOM   1423 C CB  . HIS A 1 185 ? -12.250 -22.436 36.966 1.00 15.86 ? 185  HIS A CB  1 
ATOM   1424 C CG  . HIS A 1 185 ? -11.089 -21.812 37.683 1.00 15.93 ? 185  HIS A CG  1 
ATOM   1425 N ND1 . HIS A 1 185 ? -11.046 -20.468 37.992 1.00 15.07 ? 185  HIS A ND1 1 
ATOM   1426 C CD2 . HIS A 1 185 ? -9.916  -22.338 38.127 1.00 16.58 ? 185  HIS A CD2 1 
ATOM   1427 C CE1 . HIS A 1 185 ? -9.897  -20.192 38.590 1.00 17.37 ? 185  HIS A CE1 1 
ATOM   1428 N NE2 . HIS A 1 185 ? -9.193  -21.309 38.687 1.00 14.94 ? 185  HIS A NE2 1 
ATOM   1429 N N   . GLN A 1 186 ? -13.499 -23.470 34.030 1.00 18.43 ? 186  GLN A N   1 
ATOM   1430 C CA  . GLN A 1 186 ? -14.675 -23.932 33.281 1.00 20.02 ? 186  GLN A CA  1 
ATOM   1431 C C   . GLN A 1 186 ? -15.961 -23.386 33.903 1.00 20.37 ? 186  GLN A C   1 
ATOM   1432 O O   . GLN A 1 186 ? -16.853 -22.926 33.206 1.00 22.88 ? 186  GLN A O   1 
ATOM   1433 C CB  . GLN A 1 186 ? -14.691 -25.450 33.097 1.00 19.93 ? 186  GLN A CB  1 
ATOM   1434 C CG  . GLN A 1 186 ? -13.343 -25.988 32.557 1.00 19.98 ? 186  GLN A CG  1 
ATOM   1435 C CD  . GLN A 1 186 ? -13.430 -27.423 32.162 1.00 23.24 ? 186  GLN A CD  1 
ATOM   1436 O OE1 . GLN A 1 186 ? -14.522 -27.952 31.935 1.00 22.35 ? 186  GLN A OE1 1 
ATOM   1437 N NE2 . GLN A 1 186 ? -12.297 -28.069 32.071 1.00 22.88 ? 186  GLN A NE2 1 
ATOM   1438 N N   . GLN A 1 187 ? -16.034 -23.358 35.220 1.00 20.85 ? 187  GLN A N   1 
ATOM   1439 C CA  . GLN A 1 187 ? -17.159 -22.702 35.889 1.00 20.26 ? 187  GLN A CA  1 
ATOM   1440 C C   . GLN A 1 187 ? -16.606 -21.510 36.670 1.00 19.26 ? 187  GLN A C   1 
ATOM   1441 O O   . GLN A 1 187 ? -15.409 -21.393 36.815 1.00 18.25 ? 187  GLN A O   1 
ATOM   1442 C CB  . GLN A 1 187 ? -17.829 -23.699 36.803 1.00 21.60 ? 187  GLN A CB  1 
ATOM   1443 C CG  . GLN A 1 187 ? -16.831 -24.384 37.739 1.00 25.31 ? 187  GLN A CG  1 
ATOM   1444 C CD  . GLN A 1 187 ? -17.397 -25.630 38.363 1.00 31.65 ? 187  GLN A CD  1 
ATOM   1445 O OE1 . GLN A 1 187 ? -17.695 -25.653 39.554 1.00 36.26 ? 187  GLN A OE1 1 
ATOM   1446 N NE2 . GLN A 1 187 ? -17.556 -26.672 37.563 1.00 34.46 ? 187  GLN A NE2 1 
ATOM   1447 N N   . TYR A 1 188 ? -17.471 -20.624 37.158 1.00 17.20 ? 188  TYR A N   1 
ATOM   1448 C CA  . TYR A 1 188 ? -17.031 -19.474 37.901 1.00 16.98 ? 188  TYR A CA  1 
ATOM   1449 C C   . TYR A 1 188 ? -17.050 -19.751 39.420 1.00 16.92 ? 188  TYR A C   1 
ATOM   1450 O O   . TYR A 1 188 ? -16.070 -19.468 40.121 1.00 15.90 ? 188  TYR A O   1 
ATOM   1451 C CB  . TYR A 1 188 ? -17.883 -18.232 37.552 1.00 16.31 ? 188  TYR A CB  1 
ATOM   1452 C CG  . TYR A 1 188 ? -17.444 -16.980 38.258 1.00 15.10 ? 188  TYR A CG  1 
ATOM   1453 C CD1 . TYR A 1 188 ? -16.117 -16.523 38.162 1.00 14.65 ? 188  TYR A CD1 1 
ATOM   1454 C CD2 . TYR A 1 188 ? -18.337 -16.263 39.054 1.00 12.21 ? 188  TYR A CD2 1 
ATOM   1455 C CE1 . TYR A 1 188 ? -15.703 -15.366 38.819 1.00 15.33 ? 188  TYR A CE1 1 
ATOM   1456 C CE2 . TYR A 1 188 ? -17.938 -15.091 39.710 1.00 13.95 ? 188  TYR A CE2 1 
ATOM   1457 C CZ  . TYR A 1 188 ? -16.594 -14.670 39.592 1.00 13.05 ? 188  TYR A CZ  1 
ATOM   1458 O OH  . TYR A 1 188 ? -16.175 -13.548 40.221 1.00 13.63 ? 188  TYR A OH  1 
ATOM   1459 N N   . ARG A 1 189 ? -18.138 -20.319 39.945 1.00 15.07 ? 189  ARG A N   1 
ATOM   1460 C CA  . ARG A 1 189 ? -18.111 -20.698 41.368 1.00 15.07 ? 189  ARG A CA  1 
ATOM   1461 C C   . ARG A 1 189 ? -17.296 -21.976 41.500 1.00 15.94 ? 189  ARG A C   1 
ATOM   1462 O O   . ARG A 1 189 ? -17.463 -22.936 40.746 1.00 16.95 ? 189  ARG A O   1 
ATOM   1463 C CB  . ARG A 1 189 ? -19.488 -20.927 41.963 1.00 15.98 ? 189  ARG A CB  1 
ATOM   1464 C CG  . ARG A 1 189 ? -19.412 -21.148 43.468 1.00 17.05 ? 189  ARG A CG  1 
ATOM   1465 C CD  . ARG A 1 189 ? -20.790 -21.261 44.071 1.00 17.49 ? 189  ARG A CD  1 
ATOM   1466 N NE  . ARG A 1 189 ? -21.470 -22.459 43.594 1.00 19.65 ? 189  ARG A NE  1 
ATOM   1467 C CZ  . ARG A 1 189 ? -22.752 -22.721 43.892 1.00 27.63 ? 189  ARG A CZ  1 
ATOM   1468 N NH1 . ARG A 1 189 ? -23.426 -21.904 44.689 1.00 25.55 ? 189  ARG A NH1 1 
ATOM   1469 N NH2 . ARG A 1 189 ? -23.353 -23.813 43.429 1.00 28.24 ? 189  ARG A NH2 1 
ATOM   1470 N N   . HIS A 1 190 ? -16.411 -21.990 42.459 1.00 16.86 ? 190  HIS A N   1 
ATOM   1471 C CA  . HIS A 1 190 ? -15.474 -23.124 42.538 1.00 19.43 ? 190  HIS A CA  1 
ATOM   1472 C C   . HIS A 1 190 ? -16.091 -24.437 42.864 1.00 22.37 ? 190  HIS A C   1 
ATOM   1473 O O   . HIS A 1 190 ? -16.940 -24.507 43.740 1.00 21.66 ? 190  HIS A O   1 
ATOM   1474 C CB  . HIS A 1 190 ? -14.360 -22.808 43.504 1.00 18.58 ? 190  HIS A CB  1 
ATOM   1475 C CG  . HIS A 1 190 ? -13.162 -22.286 42.794 1.00 18.72 ? 190  HIS A CG  1 
ATOM   1476 N ND1 . HIS A 1 190 ? -12.929 -20.941 42.607 1.00 20.27 ? 190  HIS A ND1 1 
ATOM   1477 C CD2 . HIS A 1 190 ? -12.197 -22.936 42.115 1.00 19.30 ? 190  HIS A CD2 1 
ATOM   1478 C CE1 . HIS A 1 190 ? -11.835 -20.783 41.883 1.00 16.85 ? 190  HIS A CE1 1 
ATOM   1479 N NE2 . HIS A 1 190 ? -11.361 -21.982 41.588 1.00 21.28 ? 190  HIS A NE2 1 
ATOM   1480 N N   . ASP A 1 191 ? -15.660 -25.470 42.122 1.00 24.80 ? 191  ASP A N   1 
ATOM   1481 C CA  . ASP A 1 191 ? -15.853 -26.845 42.550 1.00 26.17 ? 191  ASP A CA  1 
ATOM   1482 C C   . ASP A 1 191 ? -15.059 -27.052 43.834 1.00 26.05 ? 191  ASP A C   1 
ATOM   1483 O O   . ASP A 1 191 ? -13.806 -27.124 43.802 1.00 24.03 ? 191  ASP A O   1 
ATOM   1484 C CB  . ASP A 1 191 ? -15.383 -27.822 41.465 1.00 27.62 ? 191  ASP A CB  1 
ATOM   1485 C CG  . ASP A 1 191 ? -15.847 -29.235 41.734 1.00 31.23 ? 191  ASP A CG  1 
ATOM   1486 O OD1 . ASP A 1 191 ? -16.361 -29.469 42.852 1.00 33.42 ? 191  ASP A OD1 1 
ATOM   1487 O OD2 . ASP A 1 191 ? -15.707 -30.098 40.841 1.00 37.56 ? 191  ASP A OD2 1 
ATOM   1488 N N   . MET A 1 192 ? -15.770 -27.134 44.970 1.00 25.21 ? 192  MET A N   1 
ATOM   1489 C CA  . MET A 1 192 ? -15.091 -27.407 46.250 1.00 25.14 ? 192  MET A CA  1 
ATOM   1490 C C   . MET A 1 192 ? -14.824 -28.898 46.512 1.00 25.95 ? 192  MET A C   1 
ATOM   1491 O O   . MET A 1 192 ? -14.338 -29.246 47.575 1.00 24.23 ? 192  MET A O   1 
ATOM   1492 C CB  . MET A 1 192 ? -15.811 -26.764 47.451 1.00 23.73 ? 192  MET A CB  1 
ATOM   1493 C CG  . MET A 1 192 ? -15.897 -25.201 47.475 1.00 23.68 ? 192  MET A CG  1 
ATOM   1494 S SD  . MET A 1 192 ? -14.330 -24.292 47.345 1.00 25.15 ? 192  MET A SD  1 
ATOM   1495 C CE  . MET A 1 192 ? -13.608 -24.592 48.978 1.00 19.54 ? 192  MET A CE  1 
ATOM   1496 N N   . ASN A 1 193 ? -15.119 -29.769 45.544 1.00 26.72 ? 193  ASN A N   1 
ATOM   1497 C CA  . ASN A 1 193 ? -14.972 -31.210 45.725 1.00 26.89 ? 193  ASN A CA  1 
ATOM   1498 C C   . ASN A 1 193 ? -13.569 -31.811 45.462 1.00 25.83 ? 193  ASN A C   1 
ATOM   1499 O O   . ASN A 1 193 ? -13.365 -32.521 44.461 1.00 27.47 ? 193  ASN A O   1 
ATOM   1500 C CB  . ASN A 1 193 ? -16.028 -31.966 44.907 1.00 28.48 ? 193  ASN A CB  1 
ATOM   1501 C CG  . ASN A 1 193 ? -17.447 -31.622 45.336 1.00 32.21 ? 193  ASN A CG  1 
ATOM   1502 O OD1 . ASN A 1 193 ? -18.242 -31.141 44.527 1.00 38.83 ? 193  ASN A OD1 1 
ATOM   1503 N ND2 . ASN A 1 193 ? -17.765 -31.845 46.612 1.00 35.92 ? 193  ASN A ND2 1 
ATOM   1504 N N   . TRP A 1 194 ? -12.640 -31.537 46.369 1.00 22.30 ? 194  TRP A N   1 
ATOM   1505 C CA  . TRP A 1 194 ? -11.281 -32.059 46.324 1.00 20.51 ? 194  TRP A CA  1 
ATOM   1506 C C   . TRP A 1 194 ? -10.724 -31.677 44.981 1.00 19.96 ? 194  TRP A C   1 
ATOM   1507 O O   . TRP A 1 194 ? -10.874 -32.426 44.020 1.00 22.87 ? 194  TRP A O   1 
ATOM   1508 C CB  . TRP A 1 194 ? -11.307 -33.584 46.531 1.00 19.05 ? 194  TRP A CB  1 
ATOM   1509 C CG  . TRP A 1 194 ? -12.053 -34.004 47.803 1.00 16.19 ? 194  TRP A CG  1 
ATOM   1510 C CD1 . TRP A 1 194 ? -13.327 -34.549 47.891 1.00 18.62 ? 194  TRP A CD1 1 
ATOM   1511 C CD2 . TRP A 1 194 ? -11.559 -33.926 49.141 1.00 16.53 ? 194  TRP A CD2 1 
ATOM   1512 N NE1 . TRP A 1 194 ? -13.635 -34.796 49.209 1.00 16.50 ? 194  TRP A NE1 1 
ATOM   1513 C CE2 . TRP A 1 194 ? -12.571 -34.418 49.994 1.00 15.47 ? 194  TRP A CE2 1 
ATOM   1514 C CE3 . TRP A 1 194 ? -10.334 -33.480 49.708 1.00 14.91 ? 194  TRP A CE3 1 
ATOM   1515 C CZ2 . TRP A 1 194 ? -12.406 -34.500 51.385 1.00 14.94 ? 194  TRP A CZ2 1 
ATOM   1516 C CZ3 . TRP A 1 194 ? -10.180 -33.536 51.075 1.00 15.79 ? 194  TRP A CZ3 1 
ATOM   1517 C CH2 . TRP A 1 194 ? -11.215 -34.038 51.907 1.00 17.33 ? 194  TRP A CH2 1 
ATOM   1518 N N   . LYS A 1 195 ? -10.219 -30.458 44.872 1.00 18.21 ? 195  LYS A N   1 
ATOM   1519 C CA  . LYS A 1 195 ? -9.625  -29.966 43.630 1.00 17.77 ? 195  LYS A CA  1 
ATOM   1520 C C   . LYS A 1 195 ? -8.324  -29.283 43.990 1.00 16.67 ? 195  LYS A C   1 
ATOM   1521 O O   . LYS A 1 195 ? -8.259  -28.560 44.982 1.00 16.28 ? 195  LYS A O   1 
ATOM   1522 C CB  . LYS A 1 195 ? -10.545 -28.932 42.966 1.00 19.27 ? 195  LYS A CB  1 
ATOM   1523 C CG  . LYS A 1 195 ? -11.693 -29.517 42.107 1.00 23.33 ? 195  LYS A CG  1 
ATOM   1524 C CD  . LYS A 1 195 ? -11.130 -30.167 40.783 1.00 27.86 ? 195  LYS A CD  1 
ATOM   1525 C CE  . LYS A 1 195 ? -10.007 -29.294 40.133 1.00 30.44 ? 195  LYS A CE  1 
ATOM   1526 N NZ  . LYS A 1 195 ? -9.435  -29.702 38.779 1.00 31.95 ? 195  LYS A NZ  1 
ATOM   1527 N N   . THR A 1 196 ? -7.285  -29.536 43.211 1.00 15.19 ? 196  THR A N   1 
ATOM   1528 C CA  . THR A 1 196 ? -6.000  -28.849 43.437 1.00 14.40 ? 196  THR A CA  1 
ATOM   1529 C C   . THR A 1 196 ? -5.670  -28.012 42.205 1.00 13.95 ? 196  THR A C   1 
ATOM   1530 O O   . THR A 1 196 ? -5.724  -28.550 41.089 1.00 14.63 ? 196  THR A O   1 
ATOM   1531 C CB  . THR A 1 196 ? -4.845  -29.896 43.726 1.00 15.27 ? 196  THR A CB  1 
ATOM   1532 O OG1 . THR A 1 196 ? -5.108  -30.610 44.953 1.00 16.00 ? 196  THR A OG1 1 
ATOM   1533 C CG2 . THR A 1 196 ? -3.550  -29.176 43.900 1.00 15.95 ? 196  THR A CG2 1 
ATOM   1534 N N   . TRP A 1 197 ? -5.352  -26.710 42.396 1.00 14.77 ? 197  TRP A N   1 
ATOM   1535 C CA  . TRP A 1 197 ? -5.003  -25.762 41.325 1.00 14.24 ? 197  TRP A CA  1 
ATOM   1536 C C   . TRP A 1 197 ? -3.582  -25.276 41.474 1.00 14.16 ? 197  TRP A C   1 
ATOM   1537 O O   . TRP A 1 197 ? -3.274  -24.593 42.449 1.00 14.56 ? 197  TRP A O   1 
ATOM   1538 C CB  . TRP A 1 197 ? -5.934  -24.543 41.325 1.00 15.21 ? 197  TRP A CB  1 
ATOM   1539 C CG  . TRP A 1 197 ? -7.349  -24.947 41.007 1.00 13.62 ? 197  TRP A CG  1 
ATOM   1540 C CD1 . TRP A 1 197 ? -8.350  -25.174 41.902 1.00 18.60 ? 197  TRP A CD1 1 
ATOM   1541 C CD2 . TRP A 1 197 ? -7.891  -25.213 39.712 1.00 14.88 ? 197  TRP A CD2 1 
ATOM   1542 N NE1 . TRP A 1 197 ? -9.496  -25.563 41.244 1.00 17.75 ? 197  TRP A NE1 1 
ATOM   1543 C CE2 . TRP A 1 197 ? -9.242  -25.595 39.899 1.00 15.52 ? 197  TRP A CE2 1 
ATOM   1544 C CE3 . TRP A 1 197 ? -7.366  -25.197 38.399 1.00 12.79 ? 197  TRP A CE3 1 
ATOM   1545 C CZ2 . TRP A 1 197 ? -10.079 -25.928 38.836 1.00 15.24 ? 197  TRP A CZ2 1 
ATOM   1546 C CZ3 . TRP A 1 197 ? -8.228  -25.509 37.331 1.00 16.39 ? 197  TRP A CZ3 1 
ATOM   1547 C CH2 . TRP A 1 197 ? -9.570  -25.875 37.573 1.00 15.12 ? 197  TRP A CH2 1 
ATOM   1548 N N   . PRO A 1 198 ? -2.702  -25.685 40.547 1.00 14.74 ? 198  PRO A N   1 
ATOM   1549 C CA  . PRO A 1 198 ? -1.316  -25.232 40.606 1.00 14.82 ? 198  PRO A CA  1 
ATOM   1550 C C   . PRO A 1 198 ? -1.170  -23.815 40.034 1.00 14.01 ? 198  PRO A C   1 
ATOM   1551 O O   . PRO A 1 198 ? -1.840  -23.463 39.062 1.00 13.61 ? 198  PRO A O   1 
ATOM   1552 C CB  . PRO A 1 198 ? -0.616  -26.257 39.713 1.00 15.06 ? 198  PRO A CB  1 
ATOM   1553 C CG  . PRO A 1 198 ? -1.634  -26.570 38.641 1.00 16.16 ? 198  PRO A CG  1 
ATOM   1554 C CD  . PRO A 1 198 ? -2.931  -26.633 39.429 1.00 13.84 ? 198  PRO A CD  1 
ATOM   1555 N N   . ILE A 1 199 ? -0.278  -23.013 40.608 1.00 14.05 ? 199  ILE A N   1 
ATOM   1556 C CA  . ILE A 1 199 ? -0.070  -21.663 40.162 1.00 13.95 ? 199  ILE A CA  1 
ATOM   1557 C C   . ILE A 1 199 ? 1.437   -21.496 39.925 1.00 13.90 ? 199  ILE A C   1 
ATOM   1558 O O   . ILE A 1 199 ? 2.220   -21.556 40.862 1.00 13.51 ? 199  ILE A O   1 
ATOM   1559 C CB  . ILE A 1 199 ? -0.589  -20.655 41.212 1.00 14.84 ? 199  ILE A CB  1 
ATOM   1560 C CG1 . ILE A 1 199 ? -2.122  -20.835 41.424 1.00 15.05 ? 199  ILE A CG1 1 
ATOM   1561 C CG2 . ILE A 1 199 ? -0.223  -19.242 40.802 1.00 16.09 ? 199  ILE A CG2 1 
ATOM   1562 C CD1 . ILE A 1 199 ? -2.719  -19.993 42.588 1.00 14.59 ? 199  ILE A CD1 1 
ATOM   1563 N N   . PHE A 1 200 ? 1.805   -21.331 38.667 1.00 13.16 ? 200  PHE A N   1 
ATOM   1564 C CA  . PHE A 1 200 ? 3.217   -21.128 38.273 1.00 14.22 ? 200  PHE A CA  1 
ATOM   1565 C C   . PHE A 1 200 ? 3.188   -20.724 36.826 1.00 12.97 ? 200  PHE A C   1 
ATOM   1566 O O   . PHE A 1 200 ? 2.742   -21.483 35.958 1.00 15.01 ? 200  PHE A O   1 
ATOM   1567 C CB  . PHE A 1 200 ? 4.000   -22.432 38.434 1.00 13.83 ? 200  PHE A CB  1 
ATOM   1568 C CG  . PHE A 1 200 ? 5.487   -22.249 38.316 1.00 16.55 ? 200  PHE A CG  1 
ATOM   1569 C CD1 . PHE A 1 200 ? 6.165   -21.490 39.252 1.00 15.69 ? 200  PHE A CD1 1 
ATOM   1570 C CD2 . PHE A 1 200 ? 6.157   -22.775 37.241 1.00 17.76 ? 200  PHE A CD2 1 
ATOM   1571 C CE1 . PHE A 1 200 ? 7.605   -21.316 39.163 1.00 17.52 ? 200  PHE A CE1 1 
ATOM   1572 C CE2 . PHE A 1 200 ? 7.547   -22.583 37.114 1.00 20.93 ? 200  PHE A CE2 1 
ATOM   1573 C CZ  . PHE A 1 200 ? 8.242   -21.871 38.066 1.00 17.34 ? 200  PHE A CZ  1 
ATOM   1574 N N   . ASN A 1 201 ? 3.640   -19.500 36.565 1.00 14.26 ? 201  ASN A N   1 
ATOM   1575 C CA  . ASN A 1 201 ? 3.535   -18.882 35.260 1.00 13.98 ? 201  ASN A CA  1 
ATOM   1576 C C   . ASN A 1 201 ? 4.102   -19.729 34.161 1.00 14.83 ? 201  ASN A C   1 
ATOM   1577 O O   . ASN A 1 201 ? 5.272   -20.131 34.183 1.00 13.53 ? 201  ASN A O   1 
ATOM   1578 C CB  . ASN A 1 201 ? 4.117   -17.475 35.297 1.00 14.38 ? 201  ASN A CB  1 
ATOM   1579 C CG  . ASN A 1 201 ? 3.296   -16.544 36.201 1.00 14.70 ? 201  ASN A CG  1 
ATOM   1580 O OD1 . ASN A 1 201 ? 2.277   -16.966 36.771 1.00 18.70 ? 201  ASN A OD1 1 
ATOM   1581 N ND2 . ASN A 1 201 ? 3.678   -15.281 36.270 1.00 14.37 ? 201  ASN A ND2 1 
ATOM   1582 N N   . ARG A 1 202 ? 3.235   -20.062 33.221 1.00 14.55 ? 202  ARG A N   1 
ATOM   1583 C CA  . ARG A 1 202 ? 3.584   -21.075 32.224 1.00 15.25 ? 202  ARG A CA  1 
ATOM   1584 C C   . ARG A 1 202 ? 2.876   -20.808 30.899 1.00 15.62 ? 202  ARG A C   1 
ATOM   1585 O O   . ARG A 1 202 ? 1.665   -20.580 30.865 1.00 14.54 ? 202  ARG A O   1 
ATOM   1586 C CB  . ARG A 1 202 ? 3.269   -22.494 32.761 1.00 14.52 ? 202  ARG A CB  1 
ATOM   1587 C CG  . ARG A 1 202 ? 3.306   -23.605 31.702 1.00 16.25 ? 202  ARG A CG  1 
ATOM   1588 C CD  . ARG A 1 202 ? 4.753   -23.872 31.180 1.00 17.62 ? 202  ARG A CD  1 
ATOM   1589 N NE  . ARG A 1 202 ? 4.725   -24.756 30.015 1.00 18.98 ? 202  ARG A NE  1 
ATOM   1590 C CZ  . ARG A 1 202 ? 4.884   -26.079 30.059 1.00 18.96 ? 202  ARG A CZ  1 
ATOM   1591 N NH1 . ARG A 1 202 ? 5.131   -26.699 31.210 1.00 17.70 ? 202  ARG A NH1 1 
ATOM   1592 N NH2 . ARG A 1 202 ? 4.800   -26.785 28.935 1.00 18.05 ? 202  ARG A NH2 1 
ATOM   1593 N N   . ASP A 1 203 ? 3.653   -20.842 29.815 1.00 16.39 ? 203  ASP A N   1 
ATOM   1594 C CA  . ASP A 1 203 ? 3.134   -20.883 28.462 1.00 17.66 ? 203  ASP A CA  1 
ATOM   1595 C C   . ASP A 1 203 ? 2.512   -22.251 28.186 1.00 18.31 ? 203  ASP A C   1 
ATOM   1596 O O   . ASP A 1 203 ? 3.213   -23.237 27.912 1.00 17.65 ? 203  ASP A O   1 
ATOM   1597 C CB  . ASP A 1 203 ? 4.266   -20.562 27.478 1.00 18.16 ? 203  ASP A CB  1 
ATOM   1598 C CG  . ASP A 1 203 ? 3.820   -20.541 26.040 1.00 20.99 ? 203  ASP A CG  1 
ATOM   1599 O OD1 . ASP A 1 203 ? 2.643   -20.885 25.734 1.00 21.57 ? 203  ASP A OD1 1 
ATOM   1600 O OD2 . ASP A 1 203 ? 4.668   -20.154 25.205 1.00 21.99 ? 203  ASP A OD2 1 
ATOM   1601 N N   . THR A 1 204 ? 1.192   -22.332 28.317 1.00 18.61 ? 204  THR A N   1 
ATOM   1602 C CA  . THR A 1 204 ? 0.493   -23.577 28.044 1.00 21.35 ? 204  THR A CA  1 
ATOM   1603 C C   . THR A 1 204 ? -0.881  -23.258 27.521 1.00 20.62 ? 204  THR A C   1 
ATOM   1604 O O   . THR A 1 204 ? -1.386  -22.156 27.744 1.00 20.32 ? 204  THR A O   1 
ATOM   1605 C CB  . THR A 1 204 ? 0.341   -24.476 29.264 1.00 21.88 ? 204  THR A CB  1 
ATOM   1606 O OG1 . THR A 1 204 ? 0.075   -23.702 30.422 1.00 30.28 ? 204  THR A OG1 1 
ATOM   1607 C CG2 . THR A 1 204 ? 1.597   -25.267 29.522 1.00 27.88 ? 204  THR A CG2 1 
ATOM   1608 N N   . THR A 1 205 ? -1.494  -24.220 26.840 1.00 19.76 ? 205  THR A N   1 
ATOM   1609 C CA  . THR A 1 205 ? -2.789  -23.971 26.225 1.00 20.08 ? 205  THR A CA  1 
ATOM   1610 C C   . THR A 1 205 ? -3.879  -23.885 27.299 1.00 19.27 ? 205  THR A C   1 
ATOM   1611 O O   . THR A 1 205 ? -4.020  -24.792 28.122 1.00 18.04 ? 205  THR A O   1 
ATOM   1612 C CB  . THR A 1 205 ? -3.141  -25.087 25.227 1.00 21.13 ? 205  THR A CB  1 
ATOM   1613 O OG1 . THR A 1 205 ? -2.032  -25.287 24.338 1.00 24.89 ? 205  THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 205 ? -4.369  -24.703 24.429 1.00 20.97 ? 205  THR A CG2 1 
ATOM   1615 N N   . PRO A 1 206 ? -4.649  -22.788 27.294 1.00 18.60 ? 206  PRO A N   1 
ATOM   1616 C CA  . PRO A 1 206 ? -5.797  -22.754 28.188 1.00 19.02 ? 206  PRO A CA  1 
ATOM   1617 C C   . PRO A 1 206 ? -6.840  -23.745 27.699 1.00 19.62 ? 206  PRO A C   1 
ATOM   1618 O O   . PRO A 1 206 ? -7.671  -23.404 26.876 1.00 21.39 ? 206  PRO A O   1 
ATOM   1619 C CB  . PRO A 1 206 ? -6.321  -21.312 28.082 1.00 17.63 ? 206  PRO A CB  1 
ATOM   1620 C CG  . PRO A 1 206 ? -5.730  -20.736 26.821 1.00 19.03 ? 206  PRO A CG  1 
ATOM   1621 C CD  . PRO A 1 206 ? -4.479  -21.554 26.492 1.00 19.64 ? 206  PRO A CD  1 
ATOM   1622 N N   . ASN A 1 207 ? -6.801  -24.962 28.204 1.00 20.76 ? 207  ASN A N   1 
ATOM   1623 C CA  . ASN A 1 207 ? -7.747  -25.985 27.726 1.00 20.59 ? 207  ASN A CA  1 
ATOM   1624 C C   . ASN A 1 207 ? -8.462  -26.628 28.904 1.00 20.73 ? 207  ASN A C   1 
ATOM   1625 O O   . ASN A 1 207 ? -8.419  -26.107 30.020 1.00 19.37 ? 207  ASN A O   1 
ATOM   1626 C CB  . ASN A 1 207 ? -6.997  -27.004 26.868 1.00 21.47 ? 207  ASN A CB  1 
ATOM   1627 C CG  . ASN A 1 207 ? -5.870  -27.661 27.614 1.00 21.22 ? 207  ASN A CG  1 
ATOM   1628 O OD1 . ASN A 1 207 ? -5.897  -27.734 28.834 1.00 24.25 ? 207  ASN A OD1 1 
ATOM   1629 N ND2 . ASN A 1 207 ? -4.868  -28.134 26.895 1.00 22.90 ? 207  ASN A ND2 1 
ATOM   1630 N N   . GLY A 1 208 ? -9.122  -27.758 28.661 1.00 20.45 ? 208  GLY A N   1 
ATOM   1631 C CA  . GLY A 1 208 ? -9.883  -28.431 29.693 1.00 21.80 ? 208  GLY A CA  1 
ATOM   1632 C C   . GLY A 1 208 ? -9.102  -29.203 30.734 1.00 22.11 ? 208  GLY A C   1 
ATOM   1633 O O   . GLY A 1 208 ? -9.707  -29.834 31.579 1.00 21.22 ? 208  GLY A O   1 
ATOM   1634 N N   . ASN A 1 209 ? -7.765  -29.142 30.687 1.00 22.27 ? 209  ASN A N   1 
ATOM   1635 C CA  . ASN A 1 209 ? -6.932  -29.904 31.605 1.00 22.12 ? 209  ASN A CA  1 
ATOM   1636 C C   . ASN A 1 209 ? -6.622  -29.260 32.967 1.00 21.90 ? 209  ASN A C   1 
ATOM   1637 O O   . ASN A 1 209 ? -5.956  -29.876 33.797 1.00 21.64 ? 209  ASN A O   1 
ATOM   1638 C CB  . ASN A 1 209 ? -5.612  -30.294 30.922 1.00 22.99 ? 209  ASN A CB  1 
ATOM   1639 C CG  . ASN A 1 209 ? -5.814  -31.333 29.839 1.00 27.61 ? 209  ASN A CG  1 
ATOM   1640 O OD1 . ASN A 1 209 ? -6.689  -32.204 29.956 1.00 32.65 ? 209  ASN A OD1 1 
ATOM   1641 N ND2 . ASN A 1 209 ? -5.028  -31.245 28.774 1.00 32.90 ? 209  ASN A ND2 1 
ATOM   1642 N N   . GLY A 1 210 ? -7.078  -28.038 33.189 1.00 19.92 ? 210  GLY A N   1 
ATOM   1643 C CA  . GLY A 1 210 ? -6.902  -27.402 34.500 1.00 18.76 ? 210  GLY A CA  1 
ATOM   1644 C C   . GLY A 1 210 ? -5.465  -27.211 34.960 1.00 18.27 ? 210  GLY A C   1 
ATOM   1645 O O   . GLY A 1 210 ? -5.178  -27.323 36.155 1.00 19.14 ? 210  GLY A O   1 
ATOM   1646 N N   . THR A 1 211 ? -4.568  -26.893 34.032 1.00 15.45 ? 211  THR A N   1 
ATOM   1647 C CA  . THR A 1 211 ? -3.167  -26.633 34.385 1.00 15.55 ? 211  THR A CA  1 
ATOM   1648 C C   . THR A 1 211 ? -2.921  -25.206 34.857 1.00 14.54 ? 211  THR A C   1 
ATOM   1649 O O   . THR A 1 211 ? -3.752  -24.307 34.643 1.00 13.65 ? 211  THR A O   1 
ATOM   1650 C CB  . THR A 1 211 ? -2.187  -26.910 33.182 1.00 14.48 ? 211  THR A CB  1 
ATOM   1651 O OG1 . THR A 1 211 ? -2.332  -25.881 32.188 1.00 15.91 ? 211  THR A OG1 1 
ATOM   1652 C CG2 . THR A 1 211 ? -2.436  -28.269 32.544 1.00 17.28 ? 211  THR A CG2 1 
ATOM   1653 N N   . ASN A 1 212 ? -1.760  -24.989 35.478 1.00 12.52 ? 212  ASN A N   1 
ATOM   1654 C CA  . ASN A 1 212 ? -1.247  -23.639 35.588 1.00 13.95 ? 212  ASN A CA  1 
ATOM   1655 C C   . ASN A 1 212 ? -1.098  -23.004 34.197 1.00 13.98 ? 212  ASN A C   1 
ATOM   1656 O O   . ASN A 1 212 ? -0.715  -23.686 33.247 1.00 14.80 ? 212  ASN A O   1 
ATOM   1657 C CB  . ASN A 1 212 ? 0.122   -23.638 36.288 1.00 13.76 ? 212  ASN A CB  1 
ATOM   1658 C CG  . ASN A 1 212 ? 1.083   -24.675 35.709 1.00 15.10 ? 212  ASN A CG  1 
ATOM   1659 O OD1 . ASN A 1 212 ? 0.729   -25.853 35.550 1.00 16.14 ? 212  ASN A OD1 1 
ATOM   1660 N ND2 . ASN A 1 212 ? 2.313   -24.248 35.444 1.00 13.86 ? 212  ASN A ND2 1 
ATOM   1661 N N   . LEU A 1 213 ? -1.451  -21.714 34.082 1.00 12.47 ? 213  LEU A N   1 
ATOM   1662 C CA  . LEU A 1 213 ? -1.365  -20.988 32.831 1.00 12.61 ? 213  LEU A CA  1 
ATOM   1663 C C   . LEU A 1 213 ? -0.451  -19.778 33.015 1.00 13.15 ? 213  LEU A C   1 
ATOM   1664 O O   . LEU A 1 213 ? 0.487   -19.819 33.815 1.00 12.80 ? 213  LEU A O   1 
ATOM   1665 C CB  . LEU A 1 213 ? -2.765  -20.592 32.284 1.00 12.08 ? 213  LEU A CB  1 
ATOM   1666 C CG  . LEU A 1 213 ? -3.702  -21.787 32.050 1.00 11.38 ? 213  LEU A CG  1 
ATOM   1667 C CD1 . LEU A 1 213 ? -5.105  -21.199 31.751 1.00 12.99 ? 213  LEU A CD1 1 
ATOM   1668 C CD2 . LEU A 1 213 ? -3.180  -22.654 30.917 1.00 14.45 ? 213  LEU A CD2 1 
ATOM   1669 N N   . TYR A 1 214 ? -0.730  -18.687 32.310 1.00 14.29 ? 214  TYR A N   1 
ATOM   1670 C CA  . TYR A 1 214 ? 0.266   -17.608 32.126 1.00 14.58 ? 214  TYR A CA  1 
ATOM   1671 C C   . TYR A 1 214 ? 0.627   -16.744 33.344 1.00 15.84 ? 214  TYR A C   1 
ATOM   1672 O O   . TYR A 1 214 ? 1.763   -16.227 33.419 1.00 14.75 ? 214  TYR A O   1 
ATOM   1673 C CB  . TYR A 1 214 ? -0.205  -16.685 30.987 1.00 15.04 ? 214  TYR A CB  1 
ATOM   1674 C CG  . TYR A 1 214 ? -0.660  -17.444 29.789 1.00 15.45 ? 214  TYR A CG  1 
ATOM   1675 C CD1 . TYR A 1 214 ? 0.264   -18.042 28.948 1.00 13.90 ? 214  TYR A CD1 1 
ATOM   1676 C CD2 . TYR A 1 214 ? -2.012  -17.599 29.503 1.00 11.47 ? 214  TYR A CD2 1 
ATOM   1677 C CE1 . TYR A 1 214 ? -0.135  -18.767 27.845 1.00 16.12 ? 214  TYR A CE1 1 
ATOM   1678 C CE2 . TYR A 1 214 ? -2.426  -18.343 28.409 1.00 16.66 ? 214  TYR A CE2 1 
ATOM   1679 C CZ  . TYR A 1 214 ? -1.475  -18.917 27.578 1.00 16.66 ? 214  TYR A CZ  1 
ATOM   1680 O OH  . TYR A 1 214 ? -1.845  -19.583 26.442 1.00 16.69 ? 214  TYR A OH  1 
ATOM   1681 N N   . GLY A 1 215 ? -0.310  -16.655 34.299 1.00 14.58 ? 215  GLY A N   1 
ATOM   1682 C CA  . GLY A 1 215 ? -0.272  -15.675 35.387 1.00 14.48 ? 215  GLY A CA  1 
ATOM   1683 C C   . GLY A 1 215 ? -0.481  -16.301 36.741 1.00 13.28 ? 215  GLY A C   1 
ATOM   1684 O O   . GLY A 1 215 ? -0.877  -17.441 36.841 1.00 13.67 ? 215  GLY A O   1 
ATOM   1685 N N   . ALA A 1 216 ? -0.247  -15.537 37.796 1.00 12.89 ? 216  ALA A N   1 
ATOM   1686 C CA  . ALA A 1 216 ? -0.287  -16.061 39.137 1.00 12.88 ? 216  ALA A CA  1 
ATOM   1687 C C   . ALA A 1 216 ? -1.114  -15.112 39.974 1.00 13.05 ? 216  ALA A C   1 
ATOM   1688 O O   . ALA A 1 216 ? -0.717  -13.955 40.189 1.00 15.05 ? 216  ALA A O   1 
ATOM   1689 C CB  . ALA A 1 216 ? 1.164   -16.124 39.711 1.00 12.68 ? 216  ALA A CB  1 
ATOM   1690 N N   . GLN A 1 217 ? -2.259  -15.599 40.410 1.00 13.39 ? 217  GLN A N   1 
ATOM   1691 C CA  . GLN A 1 217 ? -3.262  -14.795 41.101 1.00 13.64 ? 217  GLN A CA  1 
ATOM   1692 C C   . GLN A 1 217 ? -3.836  -15.598 42.277 1.00 14.21 ? 217  GLN A C   1 
ATOM   1693 O O   . GLN A 1 217 ? -4.620  -16.539 42.081 1.00 14.31 ? 217  GLN A O   1 
ATOM   1694 C CB  . GLN A 1 217 ? -4.383  -14.413 40.120 1.00 13.53 ? 217  GLN A CB  1 
ATOM   1695 C CG  . GLN A 1 217 ? -3.961  -13.585 38.849 1.00 13.12 ? 217  GLN A CG  1 
ATOM   1696 C CD  . GLN A 1 217 ? -3.507  -12.169 39.214 1.00 14.88 ? 217  GLN A CD  1 
ATOM   1697 O OE1 . GLN A 1 217 ? -3.801  -11.655 40.308 1.00 13.40 ? 217  GLN A OE1 1 
ATOM   1698 N NE2 . GLN A 1 217 ? -2.776  -11.541 38.306 1.00 15.09 ? 217  GLN A NE2 1 
ATOM   1699 N N   . THR A 1 218 ? -3.420  -15.254 43.496 1.00 13.67 ? 218  THR A N   1 
ATOM   1700 C CA  . THR A 1 218 ? -3.781  -16.035 44.651 1.00 14.68 ? 218  THR A CA  1 
ATOM   1701 C C   . THR A 1 218 ? -5.044  -15.527 45.343 1.00 14.13 ? 218  THR A C   1 
ATOM   1702 O O   . THR A 1 218 ? -5.486  -16.124 46.318 1.00 17.32 ? 218  THR A O   1 
ATOM   1703 C CB  . THR A 1 218 ? -2.674  -16.024 45.704 1.00 15.20 ? 218  THR A CB  1 
ATOM   1704 O OG1 . THR A 1 218 ? -2.459  -14.682 46.128 1.00 17.75 ? 218  THR A OG1 1 
ATOM   1705 C CG2 . THR A 1 218 ? -1.341  -16.541 45.102 1.00 13.82 ? 218  THR A CG2 1 
ATOM   1706 N N   . PHE A 1 219 ? -5.602  -14.423 44.864 1.00 14.17 ? 219  PHE A N   1 
ATOM   1707 C CA  . PHE A 1 219 ? -6.788  -13.858 45.491 1.00 12.11 ? 219  PHE A CA  1 
ATOM   1708 C C   . PHE A 1 219 ? -8.053  -14.719 45.246 1.00 13.74 ? 219  PHE A C   1 
ATOM   1709 O O   . PHE A 1 219 ? -8.270  -15.229 44.139 1.00 13.85 ? 219  PHE A O   1 
ATOM   1710 C CB  . PHE A 1 219 ? -7.024  -12.461 44.941 1.00 12.78 ? 219  PHE A CB  1 
ATOM   1711 C CG  . PHE A 1 219 ? -8.323  -11.808 45.455 1.00 12.94 ? 219  PHE A CG  1 
ATOM   1712 C CD1 . PHE A 1 219 ? -8.389  -11.325 46.752 1.00 13.02 ? 219  PHE A CD1 1 
ATOM   1713 C CD2 . PHE A 1 219 ? -9.445  -11.714 44.633 1.00 14.20 ? 219  PHE A CD2 1 
ATOM   1714 C CE1 . PHE A 1 219 ? -9.606  -10.748 47.254 1.00 13.31 ? 219  PHE A CE1 1 
ATOM   1715 C CE2 . PHE A 1 219 ? -10.624 -11.123 45.099 1.00 13.84 ? 219  PHE A CE2 1 
ATOM   1716 C CZ  . PHE A 1 219 ? -10.699 -10.628 46.398 1.00 12.74 ? 219  PHE A CZ  1 
ATOM   1717 N N   . PHE A 1 220 ? -8.896  -14.824 46.277 1.00 13.83 ? 220  PHE A N   1 
ATOM   1718 C CA  . PHE A 1 220 ? -10.244 -15.352 46.125 1.00 14.26 ? 220  PHE A CA  1 
ATOM   1719 C C   . PHE A 1 220 ? -11.207 -14.541 46.977 1.00 13.18 ? 220  PHE A C   1 
ATOM   1720 O O   . PHE A 1 220 ? -10.816 -13.951 47.958 1.00 12.82 ? 220  PHE A O   1 
ATOM   1721 C CB  . PHE A 1 220 ? -10.359 -16.855 46.438 1.00 15.77 ? 220  PHE A CB  1 
ATOM   1722 C CG  . PHE A 1 220 ? -10.275 -17.201 47.911 1.00 16.66 ? 220  PHE A CG  1 
ATOM   1723 C CD1 . PHE A 1 220 ? -11.406 -17.183 48.718 1.00 14.82 ? 220  PHE A CD1 1 
ATOM   1724 C CD2 . PHE A 1 220 ? -9.044  -17.551 48.484 1.00 16.22 ? 220  PHE A CD2 1 
ATOM   1725 C CE1 . PHE A 1 220 ? -11.335 -17.484 50.072 1.00 18.84 ? 220  PHE A CE1 1 
ATOM   1726 C CE2 . PHE A 1 220 ? -8.967  -17.852 49.860 1.00 16.75 ? 220  PHE A CE2 1 
ATOM   1727 C CZ  . PHE A 1 220 ? -10.115 -17.828 50.641 1.00 18.66 ? 220  PHE A CZ  1 
ATOM   1728 N N   . LEU A 1 221 ? -12.475 -14.579 46.586 1.00 13.43 ? 221  LEU A N   1 
ATOM   1729 C CA  . LEU A 1 221 ? -13.531 -13.859 47.244 1.00 13.70 ? 221  LEU A CA  1 
ATOM   1730 C C   . LEU A 1 221 ? -14.527 -14.945 47.628 1.00 13.59 ? 221  LEU A C   1 
ATOM   1731 O O   . LEU A 1 221 ? -14.777 -15.860 46.851 1.00 13.43 ? 221  LEU A O   1 
ATOM   1732 C CB  . LEU A 1 221 ? -14.201 -12.911 46.236 1.00 12.90 ? 221  LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 221 ? -15.315 -11.980 46.670 1.00 15.06 ? 221  LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 221 ? -15.188 -10.762 45.816 1.00 15.08 ? 221  LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 221 ? -16.671 -12.671 46.418 1.00 17.47 ? 221  LEU A CD2 1 
ATOM   1736 N N   . CYS A 1 222 ? -15.119 -14.792 48.808 1.00 14.80 ? 222  CYS A N   1 
ATOM   1737 C CA  . CYS A 1 222 ? -16.164 -15.682 49.303 1.00 15.44 ? 222  CYS A CA  1 
ATOM   1738 C C   . CYS A 1 222 ? -17.405 -14.867 49.661 1.00 14.93 ? 222  CYS A C   1 
ATOM   1739 O O   . CYS A 1 222 ? -17.325 -13.960 50.482 1.00 14.03 ? 222  CYS A O   1 
ATOM   1740 C CB  . CYS A 1 222 ? -15.643 -16.382 50.542 1.00 16.65 ? 222  CYS A CB  1 
ATOM   1741 S SG  . CYS A 1 222 ? -16.863 -17.492 51.286 1.00 18.64 ? 222  CYS A SG  1 
ATOM   1742 N N   . LEU A 1 223 ? -18.536 -15.202 49.050 1.00 15.23 ? 223  LEU A N   1 
ATOM   1743 C CA  . LEU A 1 223 ? -19.832 -14.616 49.414 1.00 15.44 ? 223  LEU A CA  1 
ATOM   1744 C C   . LEU A 1 223 ? -20.395 -15.484 50.556 1.00 15.68 ? 223  LEU A C   1 
ATOM   1745 O O   . LEU A 1 223 ? -20.722 -16.664 50.362 1.00 16.27 ? 223  LEU A O   1 
ATOM   1746 C CB  . LEU A 1 223 ? -20.796 -14.622 48.205 1.00 14.92 ? 223  LEU A CB  1 
ATOM   1747 C CG  . LEU A 1 223 ? -22.270 -14.268 48.521 1.00 15.45 ? 223  LEU A CG  1 
ATOM   1748 C CD1 . LEU A 1 223 ? -22.426 -12.806 48.976 1.00 15.36 ? 223  LEU A CD1 1 
ATOM   1749 C CD2 . LEU A 1 223 ? -23.147 -14.531 47.328 1.00 15.63 ? 223  LEU A CD2 1 
ATOM   1750 N N   . GLU A 1 224 ? -20.497 -14.891 51.736 1.00 15.95 ? 224  GLU A N   1 
ATOM   1751 C CA  . GLU A 1 224 ? -20.825 -15.640 52.964 1.00 16.90 ? 224  GLU A CA  1 
ATOM   1752 C C   . GLU A 1 224 ? -22.275 -16.096 52.964 1.00 17.72 ? 224  GLU A C   1 
ATOM   1753 O O   . GLU A 1 224 ? -22.571 -17.220 53.330 1.00 17.76 ? 224  GLU A O   1 
ATOM   1754 C CB  . GLU A 1 224 ? -20.537 -14.789 54.201 1.00 17.05 ? 224  GLU A CB  1 
ATOM   1755 C CG  . GLU A 1 224 ? -19.054 -14.374 54.326 1.00 19.41 ? 224  GLU A CG  1 
ATOM   1756 C CD  . GLU A 1 224 ? -18.860 -13.156 55.223 1.00 21.13 ? 224  GLU A CD  1 
ATOM   1757 O OE1 . GLU A 1 224 ? -19.515 -13.033 56.301 1.00 21.96 ? 224  GLU A OE1 1 
ATOM   1758 O OE2 . GLU A 1 224 ? -17.997 -12.348 54.870 1.00 23.62 ? 224  GLU A OE2 1 
ATOM   1759 N N   . ASP A 1 225 ? -23.176 -15.230 52.531 1.00 19.35 ? 225  ASP A N   1 
ATOM   1760 C CA  . ASP A 1 225 ? -24.608 -15.575 52.535 1.00 19.91 ? 225  ASP A CA  1 
ATOM   1761 C C   . ASP A 1 225 ? -25.405 -14.577 51.698 1.00 19.97 ? 225  ASP A C   1 
ATOM   1762 O O   . ASP A 1 225 ? -24.848 -13.598 51.153 1.00 18.67 ? 225  ASP A O   1 
ATOM   1763 C CB  . ASP A 1 225 ? -25.147 -15.633 53.996 1.00 21.42 ? 225  ASP A CB  1 
ATOM   1764 C CG  . ASP A 1 225 ? -24.960 -14.338 54.770 1.00 24.07 ? 225  ASP A CG  1 
ATOM   1765 O OD1 . ASP A 1 225 ? -25.433 -13.257 54.317 1.00 28.20 ? 225  ASP A OD1 1 
ATOM   1766 O OD2 . ASP A 1 225 ? -24.390 -14.367 55.893 1.00 31.29 ? 225  ASP A OD2 1 
ATOM   1767 N N   . ALA A 1 226 ? -26.718 -14.803 51.615 1.00 18.74 ? 226  ALA A N   1 
ATOM   1768 C CA  . ALA A 1 226 ? -27.572 -13.948 50.781 1.00 18.40 ? 226  ALA A CA  1 
ATOM   1769 C C   . ALA A 1 226 ? -27.668 -12.480 51.241 1.00 18.59 ? 226  ALA A C   1 
ATOM   1770 O O   . ALA A 1 226 ? -28.215 -11.658 50.529 1.00 19.64 ? 226  ALA A O   1 
ATOM   1771 C CB  . ALA A 1 226 ? -28.986 -14.589 50.646 1.00 18.82 ? 226  ALA A CB  1 
ATOM   1772 N N   . SER A 1 227 ? -27.121 -12.114 52.402 1.00 17.18 ? 227  SER A N   1 
ATOM   1773 C CA  . SER A 1 227 ? -27.116 -10.714 52.803 1.00 18.64 ? 227  SER A CA  1 
ATOM   1774 C C   . SER A 1 227 ? -26.151 -9.910  51.963 1.00 18.51 ? 227  SER A C   1 
ATOM   1775 O O   . SER A 1 227 ? -26.272 -8.691  51.895 1.00 17.15 ? 227  SER A O   1 
ATOM   1776 C CB  . SER A 1 227 ? -26.743 -10.515 54.280 1.00 18.50 ? 227  SER A CB  1 
ATOM   1777 O OG  . SER A 1 227 ? -25.428 -11.005 54.509 1.00 24.10 ? 227  SER A OG  1 
ATOM   1778 N N   . GLY A 1 228 ? -25.197 -10.606 51.334 1.00 16.63 ? 228  GLY A N   1 
ATOM   1779 C CA  . GLY A 1 228 ? -24.157 -9.924  50.553 1.00 15.22 ? 228  GLY A CA  1 
ATOM   1780 C C   . GLY A 1 228 ? -22.822 -9.918  51.260 1.00 14.69 ? 228  GLY A C   1 
ATOM   1781 O O   . GLY A 1 228 ? -21.802 -9.702  50.611 1.00 12.17 ? 228  GLY A O   1 
ATOM   1782 N N   . LEU A 1 229 ? -22.818 -10.160 52.580 1.00 13.83 ? 229  LEU A N   1 
ATOM   1783 C CA  . LEU A 1 229 ? -21.583 -10.064 53.370 1.00 13.77 ? 229  LEU A CA  1 
ATOM   1784 C C   . LEU A 1 229 ? -20.532 -10.979 52.714 1.00 12.99 ? 229  LEU A C   1 
ATOM   1785 O O   . LEU A 1 229 ? -20.840 -12.111 52.385 1.00 12.81 ? 229  LEU A O   1 
ATOM   1786 C CB  . LEU A 1 229 ? -21.822 -10.502 54.812 1.00 14.63 ? 229  LEU A CB  1 
ATOM   1787 C CG  . LEU A 1 229 ? -22.720 -9.558  55.637 1.00 15.05 ? 229  LEU A CG  1 
ATOM   1788 C CD1 . LEU A 1 229 ? -22.964 -10.054 57.037 1.00 19.59 ? 229  LEU A CD1 1 
ATOM   1789 C CD2 . LEU A 1 229 ? -22.216 -8.142  55.613 1.00 15.47 ? 229  LEU A CD2 1 
ATOM   1790 N N   . SER A 1 230 ? -19.323 -10.472 52.492 1.00 14.28 ? 230  SER A N   1 
ATOM   1791 C CA  . SER A 1 230 ? -18.343 -11.236 51.696 1.00 13.29 ? 230  SER A CA  1 
ATOM   1792 C C   . SER A 1 230 ? -16.977 -10.929 52.275 1.00 12.86 ? 230  SER A C   1 
ATOM   1793 O O   . SER A 1 230 ? -16.813 -9.944  52.959 1.00 10.58 ? 230  SER A O   1 
ATOM   1794 C CB  . SER A 1 230 ? -18.348 -10.783 50.225 1.00 13.61 ? 230  SER A CB  1 
ATOM   1795 O OG  . SER A 1 230 ? -19.612 -10.994 49.582 1.00 14.57 ? 230  SER A OG  1 
ATOM   1796 N N   . PHE A 1 231 ? -15.983 -11.771 51.968 1.00 12.57 ? 231  PHE A N   1 
ATOM   1797 C CA  . PHE A 1 231 ? -14.605 -11.431 52.407 1.00 12.33 ? 231  PHE A CA  1 
ATOM   1798 C C   . PHE A 1 231 ? -13.665 -11.994 51.353 1.00 12.65 ? 231  PHE A C   1 
ATOM   1799 O O   . PHE A 1 231 ? -14.109 -12.717 50.463 1.00 12.78 ? 231  PHE A O   1 
ATOM   1800 C CB  . PHE A 1 231 ? -14.309 -11.985 53.806 1.00 14.41 ? 231  PHE A CB  1 
ATOM   1801 C CG  . PHE A 1 231 ? -14.045 -13.461 53.847 1.00 15.14 ? 231  PHE A CG  1 
ATOM   1802 C CD1 . PHE A 1 231 ? -12.729 -13.931 53.925 1.00 17.50 ? 231  PHE A CD1 1 
ATOM   1803 C CD2 . PHE A 1 231 ? -15.103 -14.393 53.815 1.00 15.68 ? 231  PHE A CD2 1 
ATOM   1804 C CE1 . PHE A 1 231 ? -12.460 -15.299 53.966 1.00 18.00 ? 231  PHE A CE1 1 
ATOM   1805 C CE2 . PHE A 1 231 ? -14.836 -15.762 53.882 1.00 17.20 ? 231  PHE A CE2 1 
ATOM   1806 C CZ  . PHE A 1 231 ? -13.511 -16.225 53.939 1.00 16.31 ? 231  PHE A CZ  1 
ATOM   1807 N N   . GLY A 1 232 ? -12.380 -11.640 51.435 1.00 12.72 ? 232  GLY A N   1 
ATOM   1808 C CA  . GLY A 1 232 ? -11.446 -12.068 50.420 1.00 11.36 ? 232  GLY A CA  1 
ATOM   1809 C C   . GLY A 1 232 ? -10.124 -12.360 51.110 1.00 10.44 ? 232  GLY A C   1 
ATOM   1810 O O   . GLY A 1 232 ? -9.931  -11.980 52.253 1.00 11.72 ? 232  GLY A O   1 
ATOM   1811 N N   . VAL A 1 233 ? -9.281  -13.113 50.446 1.00 10.60 ? 233  VAL A N   1 
ATOM   1812 C CA  . VAL A 1 233 ? -7.959  -13.503 51.030 1.00 10.91 ? 233  VAL A CA  1 
ATOM   1813 C C   . VAL A 1 233 ? -6.953  -13.372 49.905 1.00 11.36 ? 233  VAL A C   1 
ATOM   1814 O O   . VAL A 1 233 ? -7.228  -13.783 48.779 1.00 10.86 ? 233  VAL A O   1 
ATOM   1815 C CB  . VAL A 1 233 ? -7.955  -14.964 51.611 1.00 11.88 ? 233  VAL A CB  1 
ATOM   1816 C CG1 . VAL A 1 233 ? -6.507  -15.412 52.004 1.00 12.65 ? 233  VAL A CG1 1 
ATOM   1817 C CG2 . VAL A 1 233 ? -8.921  -15.128 52.849 1.00 13.86 ? 233  VAL A CG2 1 
ATOM   1818 N N   . PHE A 1 234 ? -5.794  -12.767 50.198 1.00 11.07 ? 234  PHE A N   1 
ATOM   1819 C CA  . PHE A 1 234 ? -4.761  -12.689 49.207 1.00 12.18 ? 234  PHE A CA  1 
ATOM   1820 C C   . PHE A 1 234 ? -3.491  -13.195 49.922 1.00 12.67 ? 234  PHE A C   1 
ATOM   1821 O O   . PHE A 1 234 ? -3.279  -12.890 51.096 1.00 11.73 ? 234  PHE A O   1 
ATOM   1822 C CB  . PHE A 1 234 ? -4.595  -11.240 48.758 1.00 13.67 ? 234  PHE A CB  1 
ATOM   1823 C CG  . PHE A 1 234 ? -3.353  -11.001 47.979 1.00 10.16 ? 234  PHE A CG  1 
ATOM   1824 C CD1 . PHE A 1 234 ? -3.160  -11.640 46.731 1.00 11.11 ? 234  PHE A CD1 1 
ATOM   1825 C CD2 . PHE A 1 234 ? -2.411  -10.107 48.441 1.00 13.57 ? 234  PHE A CD2 1 
ATOM   1826 C CE1 . PHE A 1 234 ? -1.989  -11.442 45.990 1.00 16.15 ? 234  PHE A CE1 1 
ATOM   1827 C CE2 . PHE A 1 234 ? -1.231  -9.868  47.681 1.00 15.57 ? 234  PHE A CE2 1 
ATOM   1828 C CZ  . PHE A 1 234 ? -1.024  -10.552 46.487 1.00 14.00 ? 234  PHE A CZ  1 
ATOM   1829 N N   . LEU A 1 235 ? -2.716  -14.013 49.209 1.00 13.13 ? 235  LEU A N   1 
ATOM   1830 C CA  . LEU A 1 235 ? -1.416  -14.466 49.673 1.00 13.17 ? 235  LEU A CA  1 
ATOM   1831 C C   . LEU A 1 235 ? -0.308  -13.762 48.844 1.00 11.99 ? 235  LEU A C   1 
ATOM   1832 O O   . LEU A 1 235 ? -0.226  -13.913 47.627 1.00 12.40 ? 235  LEU A O   1 
ATOM   1833 C CB  . LEU A 1 235 ? -1.340  -15.994 49.552 1.00 13.13 ? 235  LEU A CB  1 
ATOM   1834 C CG  . LEU A 1 235 ? 0.063   -16.620 49.746 1.00 14.84 ? 235  LEU A CG  1 
ATOM   1835 C CD1 . LEU A 1 235 ? 0.632   -16.225 51.109 1.00 13.34 ? 235  LEU A CD1 1 
ATOM   1836 C CD2 . LEU A 1 235 ? -0.107  -18.153 49.612 1.00 15.66 ? 235  LEU A CD2 1 
ATOM   1837 N N   . MET A 1 236 ? 0.503   -12.941 49.488 1.00 12.23 ? 236  MET A N   1 
ATOM   1838 C CA  . MET A 1 236 ? 1.577   -12.246 48.788 1.00 13.12 ? 236  MET A CA  1 
ATOM   1839 C C   . MET A 1 236 ? 2.769   -13.201 48.784 1.00 14.40 ? 236  MET A C   1 
ATOM   1840 O O   . MET A 1 236 ? 3.609   -13.152 49.702 1.00 13.93 ? 236  MET A O   1 
ATOM   1841 C CB  . MET A 1 236 ? 2.006   -10.985 49.565 1.00 12.99 ? 236  MET A CB  1 
ATOM   1842 C CG  . MET A 1 236 ? 3.089   -10.122 48.818 1.00 15.80 ? 236  MET A CG  1 
ATOM   1843 S SD  . MET A 1 236 ? 2.677   -9.411  47.211 1.00 21.12 ? 236  MET A SD  1 
ATOM   1844 C CE  . MET A 1 236 ? 2.059   -7.794  47.725 1.00 19.41 ? 236  MET A CE  1 
ATOM   1845 N N   . ASN A 1 237 ? 2.839   -14.047 47.760 1.00 15.06 ? 237  ASN A N   1 
ATOM   1846 C CA  . ASN A 1 237 ? 3.945   -15.047 47.619 1.00 14.26 ? 237  ASN A CA  1 
ATOM   1847 C C   . ASN A 1 237 ? 4.048   -15.343 46.115 1.00 14.74 ? 237  ASN A C   1 
ATOM   1848 O O   . ASN A 1 237 ? 3.030   -15.557 45.434 1.00 13.59 ? 237  ASN A O   1 
ATOM   1849 C CB  . ASN A 1 237 ? 3.633   -16.285 48.513 1.00 13.09 ? 237  ASN A CB  1 
ATOM   1850 C CG  . ASN A 1 237 ? 4.697   -17.400 48.429 1.00 15.11 ? 237  ASN A CG  1 
ATOM   1851 O OD1 . ASN A 1 237 ? 4.807   -18.069 47.414 1.00 14.53 ? 237  ASN A OD1 1 
ATOM   1852 N ND2 . ASN A 1 237 ? 5.370   -17.671 49.550 1.00 14.79 ? 237  ASN A ND2 1 
ATOM   1853 N N   . SER A 1 238 ? 5.276   -15.282 45.576 1.00 13.87 ? 238  SER A N   1 
ATOM   1854 C CA  . SER A 1 238 ? 5.512   -15.566 44.168 1.00 15.37 ? 238  SER A CA  1 
ATOM   1855 C C   . SER A 1 238 ? 6.229   -16.914 43.812 1.00 15.70 ? 238  SER A C   1 
ATOM   1856 O O   . SER A 1 238 ? 6.682   -17.079 42.679 1.00 15.86 ? 238  SER A O   1 
ATOM   1857 C CB  . SER A 1 238 ? 6.350   -14.411 43.585 1.00 15.72 ? 238  SER A CB  1 
ATOM   1858 O OG  . SER A 1 238 ? 7.524   -14.251 44.344 1.00 15.63 ? 238  SER A OG  1 
ATOM   1859 N N   . ASN A 1 239 ? 6.375   -17.815 44.778 1.00 16.22 ? 239  ASN A N   1 
ATOM   1860 C CA  . ASN A 1 239 ? 6.936   -19.153 44.533 1.00 16.77 ? 239  ASN A CA  1 
ATOM   1861 C C   . ASN A 1 239 ? 5.897   -20.046 43.894 1.00 16.61 ? 239  ASN A C   1 
ATOM   1862 O O   . ASN A 1 239 ? 4.675   -19.709 43.918 1.00 15.55 ? 239  ASN A O   1 
ATOM   1863 C CB  . ASN A 1 239 ? 7.494   -19.762 45.829 1.00 16.89 ? 239  ASN A CB  1 
ATOM   1864 C CG  . ASN A 1 239 ? 8.720   -19.015 46.329 1.00 17.18 ? 239  ASN A CG  1 
ATOM   1865 O OD1 . ASN A 1 239 ? 9.888   -19.387 46.030 1.00 21.54 ? 239  ASN A OD1 1 
ATOM   1866 N ND2 . ASN A 1 239 ? 8.486   -17.952 47.067 1.00 16.26 ? 239  ASN A ND2 1 
ATOM   1867 N N   . ALA A 1 240 ? 6.348   -21.127 43.252 1.00 14.29 ? 240  ALA A N   1 
ATOM   1868 C CA  . ALA A 1 240 ? 5.402   -22.165 42.780 1.00 15.18 ? 240  ALA A CA  1 
ATOM   1869 C C   . ALA A 1 240 ? 4.515   -22.602 43.914 1.00 14.90 ? 240  ALA A C   1 
ATOM   1870 O O   . ALA A 1 240 ? 4.976   -22.794 45.016 1.00 14.26 ? 240  ALA A O   1 
ATOM   1871 C CB  . ALA A 1 240 ? 6.156   -23.389 42.193 1.00 15.88 ? 240  ALA A CB  1 
ATOM   1872 N N   . MET A 1 241 ? 3.209   -22.726 43.669 1.00 14.60 ? 241  MET A N   1 
ATOM   1873 C CA  . MET A 1 241 ? 2.352   -23.133 44.755 1.00 15.17 ? 241  MET A CA  1 
ATOM   1874 C C   . MET A 1 241 ? 1.164   -23.888 44.167 1.00 14.57 ? 241  MET A C   1 
ATOM   1875 O O   . MET A 1 241 ? 0.994   -23.963 42.940 1.00 13.70 ? 241  MET A O   1 
ATOM   1876 C CB  . MET A 1 241 ? 1.867   -21.900 45.547 1.00 16.18 ? 241  MET A CB  1 
ATOM   1877 C CG  . MET A 1 241 ? 0.875   -21.079 44.781 1.00 15.66 ? 241  MET A CG  1 
ATOM   1878 S SD  . MET A 1 241 ? 0.149   -19.846 45.883 1.00 19.96 ? 241  MET A SD  1 
ATOM   1879 C CE  . MET A 1 241 ? 1.519   -18.707 45.960 1.00 15.64 ? 241  MET A CE  1 
ATOM   1880 N N   . GLU A 1 242 ? 0.373   -24.482 45.034 1.00 14.97 ? 242  GLU A N   1 
ATOM   1881 C CA  . GLU A 1 242 ? -0.933  -24.983 44.601 1.00 16.47 ? 242  GLU A CA  1 
ATOM   1882 C C   . GLU A 1 242 ? -1.958  -24.704 45.674 1.00 16.15 ? 242  GLU A C   1 
ATOM   1883 O O   . GLU A 1 242 ? -1.628  -24.564 46.857 1.00 15.94 ? 242  GLU A O   1 
ATOM   1884 C CB  . GLU A 1 242 ? -0.896  -26.470 44.240 1.00 17.16 ? 242  GLU A CB  1 
ATOM   1885 C CG  . GLU A 1 242 ? -0.416  -27.392 45.347 1.00 18.90 ? 242  GLU A CG  1 
ATOM   1886 C CD  . GLU A 1 242 ? -0.037  -28.769 44.820 1.00 22.09 ? 242  GLU A CD  1 
ATOM   1887 O OE1 . GLU A 1 242 ? 0.185   -28.933 43.593 1.00 22.28 ? 242  GLU A OE1 1 
ATOM   1888 O OE2 . GLU A 1 242 ? 0.051   -29.694 45.633 1.00 24.05 ? 242  GLU A OE2 1 
ATOM   1889 N N   . VAL A 1 243 ? -3.225  -24.648 45.276 1.00 16.23 ? 243  VAL A N   1 
ATOM   1890 C CA  . VAL A 1 243 ? -4.240  -24.308 46.229 1.00 14.90 ? 243  VAL A CA  1 
ATOM   1891 C C   . VAL A 1 243 ? -5.197  -25.512 46.210 1.00 15.36 ? 243  VAL A C   1 
ATOM   1892 O O   . VAL A 1 243 ? -5.524  -26.000 45.140 1.00 14.12 ? 243  VAL A O   1 
ATOM   1893 C CB  . VAL A 1 243 ? -4.938  -23.002 45.792 1.00 15.86 ? 243  VAL A CB  1 
ATOM   1894 C CG1 . VAL A 1 243 ? -6.067  -22.693 46.690 1.00 15.00 ? 243  VAL A CG1 1 
ATOM   1895 C CG2 . VAL A 1 243 ? -3.911  -21.819 45.724 1.00 16.96 ? 243  VAL A CG2 1 
ATOM   1896 N N   . VAL A 1 244 ? -5.583  -26.000 47.388 1.00 14.36 ? 244  VAL A N   1 
ATOM   1897 C CA  . VAL A 1 244 ? -6.307  -27.255 47.511 1.00 15.52 ? 244  VAL A CA  1 
ATOM   1898 C C   . VAL A 1 244 ? -7.671  -26.907 48.074 1.00 15.11 ? 244  VAL A C   1 
ATOM   1899 O O   . VAL A 1 244 ? -7.769  -26.354 49.154 1.00 14.78 ? 244  VAL A O   1 
ATOM   1900 C CB  . VAL A 1 244 ? -5.569  -28.255 48.419 1.00 15.80 ? 244  VAL A CB  1 
ATOM   1901 C CG1 . VAL A 1 244 ? -6.336  -29.594 48.571 1.00 16.49 ? 244  VAL A CG1 1 
ATOM   1902 C CG2 . VAL A 1 244 ? -4.187  -28.525 47.840 1.00 17.47 ? 244  VAL A CG2 1 
ATOM   1903 N N   . LEU A 1 245 ? -8.713  -27.254 47.341 1.00 16.33 ? 245  LEU A N   1 
ATOM   1904 C CA  . LEU A 1 245 ? -10.068 -26.920 47.750 1.00 16.56 ? 245  LEU A CA  1 
ATOM   1905 C C   . LEU A 1 245 ? -10.750 -28.196 48.169 1.00 16.63 ? 245  LEU A C   1 
ATOM   1906 O O   . LEU A 1 245 ? -10.570 -29.234 47.521 1.00 18.02 ? 245  LEU A O   1 
ATOM   1907 C CB  . LEU A 1 245 ? -10.840 -26.246 46.591 1.00 17.07 ? 245  LEU A CB  1 
ATOM   1908 C CG  . LEU A 1 245 ? -10.167 -25.121 45.776 1.00 20.77 ? 245  LEU A CG  1 
ATOM   1909 C CD1 . LEU A 1 245 ? -11.185 -24.651 44.782 1.00 22.65 ? 245  LEU A CD1 1 
ATOM   1910 C CD2 . LEU A 1 245 ? -9.850  -24.005 46.656 1.00 22.37 ? 245  LEU A CD2 1 
ATOM   1911 N N   . GLN A 1 246 ? -11.476 -28.163 49.283 1.00 15.87 ? 246  GLN A N   1 
ATOM   1912 C CA  . GLN A 1 246 ? -12.168 -29.381 49.731 1.00 15.86 ? 246  GLN A CA  1 
ATOM   1913 C C   . GLN A 1 246 ? -13.513 -29.043 50.332 1.00 16.83 ? 246  GLN A C   1 
ATOM   1914 O O   . GLN A 1 246 ? -13.740 -27.885 50.690 1.00 15.69 ? 246  GLN A O   1 
ATOM   1915 C CB  . GLN A 1 246 ? -11.341 -30.173 50.714 1.00 16.78 ? 246  GLN A CB  1 
ATOM   1916 C CG  . GLN A 1 246 ? -11.115 -29.540 52.072 1.00 15.30 ? 246  GLN A CG  1 
ATOM   1917 C CD  . GLN A 1 246 ? -10.047 -30.315 52.813 1.00 18.95 ? 246  GLN A CD  1 
ATOM   1918 O OE1 . GLN A 1 246 ? -8.863  -30.178 52.508 1.00 16.30 ? 246  GLN A OE1 1 
ATOM   1919 N NE2 . GLN A 1 246 ? -10.453 -31.127 53.780 1.00 18.04 ? 246  GLN A NE2 1 
ATOM   1920 N N   . PRO A 1 247 ? -14.414 -30.045 50.405 1.00 17.45 ? 247  PRO A N   1 
ATOM   1921 C CA  . PRO A 1 247 ? -15.826 -29.767 50.716 1.00 18.50 ? 247  PRO A CA  1 
ATOM   1922 C C   . PRO A 1 247 ? -16.147 -29.470 52.165 1.00 19.13 ? 247  PRO A C   1 
ATOM   1923 O O   . PRO A 1 247 ? -17.314 -29.281 52.472 1.00 20.48 ? 247  PRO A O   1 
ATOM   1924 C CB  . PRO A 1 247 ? -16.551 -31.068 50.324 1.00 18.75 ? 247  PRO A CB  1 
ATOM   1925 C CG  . PRO A 1 247 ? -15.554 -31.934 49.689 1.00 19.59 ? 247  PRO A CG  1 
ATOM   1926 C CD  . PRO A 1 247 ? -14.193 -31.456 50.103 1.00 18.76 ? 247  PRO A CD  1 
ATOM   1927 N N   . ALA A 1 248 ? -15.161 -29.437 53.058 1.00 19.66 ? 248  ALA A N   1 
ATOM   1928 C CA  . ALA A 1 248 ? -15.381 -28.991 54.452 1.00 19.22 ? 248  ALA A CA  1 
ATOM   1929 C C   . ALA A 1 248 ? -16.448 -27.877 54.664 1.00 20.96 ? 248  ALA A C   1 
ATOM   1930 O O   . ALA A 1 248 ? -17.299 -28.019 55.586 1.00 18.77 ? 248  ALA A O   1 
ATOM   1931 C CB  . ALA A 1 248 ? -14.067 -28.581 55.078 1.00 20.44 ? 248  ALA A CB  1 
ATOM   1932 N N   . PRO A 1 249 ? -16.363 -26.701 53.895 1.00 18.41 ? 249  PRO A N   1 
ATOM   1933 C CA  . PRO A 1 249 ? -15.390 -26.292 52.886 1.00 17.77 ? 249  PRO A CA  1 
ATOM   1934 C C   . PRO A 1 249 ? -14.132 -25.665 53.477 1.00 17.15 ? 249  PRO A C   1 
ATOM   1935 O O   . PRO A 1 249 ? -14.157 -25.074 54.566 1.00 16.53 ? 249  PRO A O   1 
ATOM   1936 C CB  . PRO A 1 249 ? -16.156 -25.240 52.080 1.00 18.45 ? 249  PRO A CB  1 
ATOM   1937 C CG  . PRO A 1 249 ? -16.995 -24.604 53.052 1.00 17.28 ? 249  PRO A CG  1 
ATOM   1938 C CD  . PRO A 1 249 ? -17.412 -25.675 54.037 1.00 19.32 ? 249  PRO A CD  1 
ATOM   1939 N N   . ALA A 1 250 ? -13.033 -25.795 52.742 1.00 16.29 ? 250  ALA A N   1 
ATOM   1940 C CA  . ALA A 1 250 ? -11.754 -25.293 53.231 1.00 15.73 ? 250  ALA A CA  1 
ATOM   1941 C C   . ALA A 1 250 ? -10.827 -25.135 52.054 1.00 14.43 ? 250  ALA A C   1 
ATOM   1942 O O   . ALA A 1 250 ? -11.034 -25.754 50.999 1.00 13.17 ? 250  ALA A O   1 
ATOM   1943 C CB  . ALA A 1 250 ? -11.184 -26.285 54.215 1.00 16.18 ? 250  ALA A CB  1 
ATOM   1944 N N   . ILE A 1 251 ? -9.808  -24.299 52.238 1.00 14.22 ? 251  ILE A N   1 
ATOM   1945 C CA  A ILE A 1 251 ? -8.799  -24.073 51.218 0.50 13.88 ? 251  ILE A CA  1 
ATOM   1946 C CA  B ILE A 1 251 ? -8.780  -24.047 51.221 0.50 14.64 ? 251  ILE A CA  1 
ATOM   1947 C C   . ILE A 1 251 ? -7.432  -24.174 51.887 1.00 14.83 ? 251  ILE A C   1 
ATOM   1948 O O   . ILE A 1 251 ? -7.257  -23.753 53.028 1.00 15.10 ? 251  ILE A O   1 
ATOM   1949 C CB  A ILE A 1 251 ? -9.025  -22.705 50.473 0.50 13.99 ? 251  ILE A CB  1 
ATOM   1950 C CB  B ILE A 1 251 ? -8.864  -22.619 50.594 0.50 14.64 ? 251  ILE A CB  1 
ATOM   1951 C CG1 A ILE A 1 251 ? -8.035  -22.493 49.323 0.50 14.34 ? 251  ILE A CG1 1 
ATOM   1952 C CG1 B ILE A 1 251 ? -9.974  -22.546 49.546 0.50 16.08 ? 251  ILE A CG1 1 
ATOM   1953 C CG2 A ILE A 1 251 ? -9.026  -21.534 51.434 0.50 13.35 ? 251  ILE A CG2 1 
ATOM   1954 C CG2 B ILE A 1 251 ? -7.520  -22.210 49.935 0.50 16.24 ? 251  ILE A CG2 1 
ATOM   1955 C CD1 A ILE A 1 251 ? -8.318  -21.258 48.488 0.50 13.42 ? 251  ILE A CD1 1 
ATOM   1956 C CD1 B ILE A 1 251 ? -10.110 -21.184 48.901 0.50 15.22 ? 251  ILE A CD1 1 
ATOM   1957 N N   . THR A 1 252 ? -6.492  -24.768 51.177 1.00 14.03 ? 252  THR A N   1 
ATOM   1958 C CA  . THR A 1 252 ? -5.140  -24.904 51.689 1.00 15.27 ? 252  THR A CA  1 
ATOM   1959 C C   . THR A 1 252 ? -4.227  -24.263 50.651 1.00 14.98 ? 252  THR A C   1 
ATOM   1960 O O   . THR A 1 252 ? -4.388  -24.508 49.451 1.00 14.47 ? 252  THR A O   1 
ATOM   1961 C CB  . THR A 1 252 ? -4.826  -26.404 51.881 1.00 15.80 ? 252  THR A CB  1 
ATOM   1962 O OG1 . THR A 1 252 ? -5.690  -26.946 52.905 1.00 16.57 ? 252  THR A OG1 1 
ATOM   1963 C CG2 . THR A 1 252 ? -3.367  -26.633 52.291 1.00 16.91 ? 252  THR A CG2 1 
ATOM   1964 N N   . TYR A 1 253 ? -3.262  -23.452 51.106 1.00 14.14 ? 253  TYR A N   1 
ATOM   1965 C CA  . TYR A 1 253 ? -2.258  -22.896 50.234 1.00 14.27 ? 253  TYR A CA  1 
ATOM   1966 C C   . TYR A 1 253 ? -0.983  -23.686 50.545 1.00 14.42 ? 253  TYR A C   1 
ATOM   1967 O O   . TYR A 1 253 ? -0.643  -23.881 51.715 1.00 14.19 ? 253  TYR A O   1 
ATOM   1968 C CB  . TYR A 1 253 ? -1.999  -21.442 50.603 1.00 16.24 ? 253  TYR A CB  1 
ATOM   1969 C CG  . TYR A 1 253 ? -3.047  -20.437 50.108 1.00 16.94 ? 253  TYR A CG  1 
ATOM   1970 C CD1 . TYR A 1 253 ? -2.968  -19.929 48.827 1.00 18.28 ? 253  TYR A CD1 1 
ATOM   1971 C CD2 . TYR A 1 253 ? -4.103  -20.018 50.927 1.00 22.25 ? 253  TYR A CD2 1 
ATOM   1972 C CE1 . TYR A 1 253 ? -3.893  -18.977 48.337 1.00 21.30 ? 253  TYR A CE1 1 
ATOM   1973 C CE2 . TYR A 1 253 ? -5.051  -19.073 50.442 1.00 19.14 ? 253  TYR A CE2 1 
ATOM   1974 C CZ  . TYR A 1 253 ? -4.930  -18.576 49.159 1.00 21.25 ? 253  TYR A CZ  1 
ATOM   1975 O OH  . TYR A 1 253 ? -5.844  -17.640 48.679 1.00 22.48 ? 253  TYR A OH  1 
ATOM   1976 N N   . ARG A 1 254 ? -0.293  -24.090 49.503 1.00 14.52 ? 254  ARG A N   1 
ATOM   1977 C CA  A ARG A 1 254 ? 0.906   -24.919 49.625 0.50 16.03 ? 254  ARG A CA  1 
ATOM   1978 C CA  B ARG A 1 254 ? 0.912   -24.908 49.649 0.50 15.14 ? 254  ARG A CA  1 
ATOM   1979 C C   . ARG A 1 254 ? 1.952   -24.297 48.728 1.00 15.58 ? 254  ARG A C   1 
ATOM   1980 O O   . ARG A 1 254 ? 1.837   -24.403 47.528 1.00 17.73 ? 254  ARG A O   1 
ATOM   1981 C CB  A ARG A 1 254 ? 0.549   -26.309 49.098 0.50 16.86 ? 254  ARG A CB  1 
ATOM   1982 C CB  B ARG A 1 254 ? 0.536   -26.326 49.219 0.50 15.53 ? 254  ARG A CB  1 
ATOM   1983 C CG  A ARG A 1 254 ? 1.053   -27.440 49.945 0.50 19.43 ? 254  ARG A CG  1 
ATOM   1984 C CG  B ARG A 1 254 ? 1.495   -27.435 49.586 0.50 13.70 ? 254  ARG A CG  1 
ATOM   1985 C CD  A ARG A 1 254 ? 1.228   -28.727 49.162 0.50 22.36 ? 254  ARG A CD  1 
ATOM   1986 C CD  B ARG A 1 254 ? 0.911   -28.735 49.045 0.50 12.31 ? 254  ARG A CD  1 
ATOM   1987 N NE  A ARG A 1 254 ? 0.032   -29.223 48.483 0.50 23.71 ? 254  ARG A NE  1 
ATOM   1988 N NE  B ARG A 1 254 ? -0.185  -29.355 49.799 0.50 6.95  ? 254  ARG A NE  1 
ATOM   1989 C CZ  A ARG A 1 254 ? -1.010  -29.787 49.086 0.50 23.29 ? 254  ARG A CZ  1 
ATOM   1990 C CZ  B ARG A 1 254 ? -1.066  -30.198 49.245 0.50 7.88  ? 254  ARG A CZ  1 
ATOM   1991 N NH1 A ARG A 1 254 ? -1.048  -29.910 50.400 0.50 21.87 ? 254  ARG A NH1 1 
ATOM   1992 N NH1 B ARG A 1 254 ? -0.995  -30.450 47.932 0.50 8.92  ? 254  ARG A NH1 1 
ATOM   1993 N NH2 A ARG A 1 254 ? -2.020  -30.229 48.358 0.50 23.74 ? 254  ARG A NH2 1 
ATOM   1994 N NH2 B ARG A 1 254 ? -2.013  -30.792 49.965 0.50 6.65  ? 254  ARG A NH2 1 
ATOM   1995 N N   . THR A 1 255 ? 2.961   -23.626 49.278 1.00 15.85 ? 255  THR A N   1 
ATOM   1996 C CA  . THR A 1 255 ? 3.952   -22.977 48.426 1.00 15.43 ? 255  THR A CA  1 
ATOM   1997 C C   . THR A 1 255 ? 5.365   -23.533 48.722 1.00 15.68 ? 255  THR A C   1 
ATOM   1998 O O   . THR A 1 255 ? 5.617   -24.068 49.803 1.00 15.37 ? 255  THR A O   1 
ATOM   1999 C CB  . THR A 1 255 ? 3.923   -21.444 48.565 1.00 15.94 ? 255  THR A CB  1 
ATOM   2000 O OG1 . THR A 1 255 ? 4.958   -20.850 47.749 1.00 19.45 ? 255  THR A OG1 1 
ATOM   2001 C CG2 . THR A 1 255 ? 4.096   -21.018 50.021 1.00 17.06 ? 255  THR A CG2 1 
ATOM   2002 N N   . ILE A 1 256 ? 6.282   -23.359 47.779 1.00 15.15 ? 256  ILE A N   1 
ATOM   2003 C CA  . ILE A 1 256 ? 7.594   -24.000 47.964 1.00 14.96 ? 256  ILE A CA  1 
ATOM   2004 C C   . ILE A 1 256 ? 8.707   -22.969 48.241 1.00 16.45 ? 256  ILE A C   1 
ATOM   2005 O O   . ILE A 1 256 ? 9.913   -23.254 48.076 1.00 15.86 ? 256  ILE A O   1 
ATOM   2006 C CB  . ILE A 1 256 ? 7.950   -24.961 46.807 1.00 15.51 ? 256  ILE A CB  1 
ATOM   2007 C CG1 . ILE A 1 256 ? 8.206   -24.201 45.494 1.00 15.01 ? 256  ILE A CG1 1 
ATOM   2008 C CG2 . ILE A 1 256 ? 6.898   -26.069 46.668 1.00 16.08 ? 256  ILE A CG2 1 
ATOM   2009 C CD1 . ILE A 1 256 ? 8.772   -25.074 44.424 1.00 13.24 ? 256  ILE A CD1 1 
ATOM   2010 N N   . GLY A 1 257 ? 8.317   -21.774 48.692 1.00 14.98 ? 257  GLY A N   1 
ATOM   2011 C CA  . GLY A 1 257 ? 9.342   -20.875 49.209 1.00 14.65 ? 257  GLY A CA  1 
ATOM   2012 C C   . GLY A 1 257 ? 8.747   -19.626 49.759 1.00 15.42 ? 257  GLY A C   1 
ATOM   2013 O O   . GLY A 1 257 ? 7.524   -19.534 49.913 1.00 15.29 ? 257  GLY A O   1 
ATOM   2014 N N   . GLY A 1 258 ? 9.617   -18.659 49.992 1.00 13.20 ? 258  GLY A N   1 
ATOM   2015 C CA  . GLY A 1 258 ? 9.253   -17.370 50.554 1.00 13.83 ? 258  GLY A CA  1 
ATOM   2016 C C   . GLY A 1 258 ? 8.628   -17.464 51.928 1.00 13.09 ? 258  GLY A C   1 
ATOM   2017 O O   . GLY A 1 258 ? 9.008   -18.280 52.784 1.00 12.36 ? 258  GLY A O   1 
ATOM   2018 N N   . ILE A 1 259 ? 7.587   -16.654 52.123 1.00 13.32 ? 259  ILE A N   1 
ATOM   2019 C CA  . ILE A 1 259 ? 6.976   -16.534 53.439 1.00 15.29 ? 259  ILE A CA  1 
ATOM   2020 C C   . ILE A 1 259 ? 5.447   -16.584 53.262 1.00 15.34 ? 259  ILE A C   1 
ATOM   2021 O O   . ILE A 1 259 ? 4.937   -16.373 52.150 1.00 15.35 ? 259  ILE A O   1 
ATOM   2022 C CB  . ILE A 1 259 ? 7.397   -15.221 54.230 1.00 15.36 ? 259  ILE A CB  1 
ATOM   2023 C CG1 . ILE A 1 259 ? 6.923   -13.921 53.524 1.00 14.44 ? 259  ILE A CG1 1 
ATOM   2024 C CG2 . ILE A 1 259 ? 8.919   -15.186 54.505 1.00 16.19 ? 259  ILE A CG2 1 
ATOM   2025 C CD1 . ILE A 1 259 ? 6.751   -12.698 54.450 1.00 15.91 ? 259  ILE A CD1 1 
ATOM   2026 N N   . LEU A 1 260 ? 4.733   -16.806 54.362 1.00 15.30 ? 260  LEU A N   1 
ATOM   2027 C CA  . LEU A 1 260 ? 3.270   -16.774 54.275 1.00 15.94 ? 260  LEU A CA  1 
ATOM   2028 C C   . LEU A 1 260 ? 2.812   -15.366 54.661 1.00 16.93 ? 260  LEU A C   1 
ATOM   2029 O O   . LEU A 1 260 ? 2.836   -15.011 55.817 1.00 19.05 ? 260  LEU A O   1 
ATOM   2030 C CB  . LEU A 1 260 ? 2.652   -17.839 55.156 1.00 15.40 ? 260  LEU A CB  1 
ATOM   2031 C CG  . LEU A 1 260 ? 2.920   -19.271 54.712 1.00 13.57 ? 260  LEU A CG  1 
ATOM   2032 C CD1 . LEU A 1 260 ? 2.419   -20.212 55.755 1.00 17.23 ? 260  LEU A CD1 1 
ATOM   2033 C CD2 . LEU A 1 260 ? 2.362   -19.630 53.291 1.00 14.29 ? 260  LEU A CD2 1 
ATOM   2034 N N   . ASP A 1 261 ? 2.473   -14.551 53.675 1.00 17.56 ? 261  ASP A N   1 
ATOM   2035 C CA  . ASP A 1 261 ? 2.152   -13.154 53.936 1.00 16.53 ? 261  ASP A CA  1 
ATOM   2036 C C   . ASP A 1 261 ? 0.703   -12.975 53.472 1.00 16.26 ? 261  ASP A C   1 
ATOM   2037 O O   . ASP A 1 261 ? 0.467   -12.918 52.270 1.00 14.67 ? 261  ASP A O   1 
ATOM   2038 C CB  . ASP A 1 261 ? 3.048   -12.284 53.078 1.00 17.94 ? 261  ASP A CB  1 
ATOM   2039 C CG  . ASP A 1 261 ? 2.863   -10.799 53.340 1.00 20.60 ? 261  ASP A CG  1 
ATOM   2040 O OD1 . ASP A 1 261 ? 1.944   -10.449 54.097 1.00 24.73 ? 261  ASP A OD1 1 
ATOM   2041 O OD2 . ASP A 1 261 ? 3.622   -9.960  52.804 1.00 19.16 ? 261  ASP A OD2 1 
ATOM   2042 N N   . PHE A 1 262 ? -0.234  -12.867 54.421 1.00 15.52 ? 262  PHE A N   1 
ATOM   2043 C CA  . PHE A 1 262 ? -1.655  -13.020 54.091 1.00 13.90 ? 262  PHE A CA  1 
ATOM   2044 C C   . PHE A 1 262 ? -2.383  -11.712 54.395 1.00 13.45 ? 262  PHE A C   1 
ATOM   2045 O O   . PHE A 1 262 ? -2.083  -11.051 55.420 1.00 13.23 ? 262  PHE A O   1 
ATOM   2046 C CB  . PHE A 1 262 ? -2.321  -14.121 54.940 1.00 14.52 ? 262  PHE A CB  1 
ATOM   2047 C CG  . PHE A 1 262 ? -2.197  -15.528 54.386 1.00 15.87 ? 262  PHE A CG  1 
ATOM   2048 C CD1 . PHE A 1 262 ? -2.931  -15.943 53.262 1.00 17.94 ? 262  PHE A CD1 1 
ATOM   2049 C CD2 . PHE A 1 262 ? -1.342  -16.449 55.002 1.00 16.52 ? 262  PHE A CD2 1 
ATOM   2050 C CE1 . PHE A 1 262 ? -2.811  -17.255 52.774 1.00 19.16 ? 262  PHE A CE1 1 
ATOM   2051 C CE2 . PHE A 1 262 ? -1.241  -17.741 54.525 1.00 14.66 ? 262  PHE A CE2 1 
ATOM   2052 C CZ  . PHE A 1 262 ? -1.959  -18.143 53.404 1.00 18.51 ? 262  PHE A CZ  1 
ATOM   2053 N N   . TYR A 1 263 ? -3.372  -11.393 53.567 1.00 13.41 ? 263  TYR A N   1 
ATOM   2054 C CA  . TYR A 1 263 ? -4.286  -10.263 53.835 1.00 13.33 ? 263  TYR A CA  1 
ATOM   2055 C C   . TYR A 1 263 ? -5.681  -10.827 53.808 1.00 13.77 ? 263  TYR A C   1 
ATOM   2056 O O   . TYR A 1 263 ? -5.953  -11.743 53.012 1.00 13.06 ? 263  TYR A O   1 
ATOM   2057 C CB  . TYR A 1 263 ? -4.181  -9.211  52.725 1.00 14.67 ? 263  TYR A CB  1 
ATOM   2058 C CG  . TYR A 1 263 ? -2.836  -8.481  52.711 1.00 14.14 ? 263  TYR A CG  1 
ATOM   2059 C CD1 . TYR A 1 263 ? -2.701  -7.241  53.306 1.00 16.84 ? 263  TYR A CD1 1 
ATOM   2060 C CD2 . TYR A 1 263 ? -1.718  -9.055  52.096 1.00 17.71 ? 263  TYR A CD2 1 
ATOM   2061 C CE1 . TYR A 1 263 ? -1.510  -6.540  53.271 1.00 16.47 ? 263  TYR A CE1 1 
ATOM   2062 C CE2 . TYR A 1 263 ? -0.502  -8.372  52.074 1.00 17.44 ? 263  TYR A CE2 1 
ATOM   2063 C CZ  . TYR A 1 263 ? -0.408  -7.139  52.670 1.00 16.78 ? 263  TYR A CZ  1 
ATOM   2064 O OH  . TYR A 1 263 ? 0.749   -6.429  52.674 1.00 14.61 ? 263  TYR A OH  1 
ATOM   2065 N N   . VAL A 1 264 ? -6.561  -10.292 54.662 1.00 12.63 ? 264  VAL A N   1 
ATOM   2066 C CA  . VAL A 1 264 ? -7.942  -10.755 54.710 1.00 13.36 ? 264  VAL A CA  1 
ATOM   2067 C C   . VAL A 1 264 ? -8.778  -9.462  54.634 1.00 12.56 ? 264  VAL A C   1 
ATOM   2068 O O   . VAL A 1 264 ? -8.446  -8.500  55.303 1.00 13.03 ? 264  VAL A O   1 
ATOM   2069 C CB  . VAL A 1 264 ? -8.241  -11.558 56.004 1.00 13.80 ? 264  VAL A CB  1 
ATOM   2070 C CG1 . VAL A 1 264 ? -9.740  -11.970 56.110 1.00 13.81 ? 264  VAL A CG1 1 
ATOM   2071 C CG2 . VAL A 1 264 ? -7.354  -12.846 56.138 1.00 13.50 ? 264  VAL A CG2 1 
ATOM   2072 N N   . PHE A 1 265 ? -9.831  -9.457  53.800 1.00 12.19 ? 265  PHE A N   1 
ATOM   2073 C CA  . PHE A 1 265 ? -10.552 -8.222  53.463 1.00 12.97 ? 265  PHE A CA  1 
ATOM   2074 C C   . PHE A 1 265 ? -11.987 -8.518  53.759 1.00 12.58 ? 265  PHE A C   1 
ATOM   2075 O O   . PHE A 1 265 ? -12.442 -9.588  53.389 1.00 13.34 ? 265  PHE A O   1 
ATOM   2076 C CB  . PHE A 1 265 ? -10.449 -7.923  51.950 1.00 12.60 ? 265  PHE A CB  1 
ATOM   2077 C CG  . PHE A 1 265 ? -9.021  -7.870  51.411 1.00 14.47 ? 265  PHE A CG  1 
ATOM   2078 C CD1 . PHE A 1 265 ? -8.258  -6.726  51.547 1.00 12.54 ? 265  PHE A CD1 1 
ATOM   2079 C CD2 . PHE A 1 265 ? -8.478  -8.962  50.741 1.00 16.65 ? 265  PHE A CD2 1 
ATOM   2080 C CE1 . PHE A 1 265 ? -6.915  -6.675  51.061 1.00 15.29 ? 265  PHE A CE1 1 
ATOM   2081 C CE2 . PHE A 1 265 ? -7.159  -8.922  50.238 1.00 17.48 ? 265  PHE A CE2 1 
ATOM   2082 C CZ  . PHE A 1 265 ? -6.389  -7.768  50.391 1.00 15.58 ? 265  PHE A CZ  1 
ATOM   2083 N N   . LEU A 1 266 ? -12.698 -7.577  54.371 1.00 13.58 ? 266  LEU A N   1 
ATOM   2084 C CA  . LEU A 1 266 ? -14.126 -7.791  54.627 1.00 13.16 ? 266  LEU A CA  1 
ATOM   2085 C C   . LEU A 1 266 ? -14.901 -6.731  53.903 1.00 13.23 ? 266  LEU A C   1 
ATOM   2086 O O   . LEU A 1 266 ? -14.458 -5.624  53.789 1.00 13.75 ? 266  LEU A O   1 
ATOM   2087 C CB  . LEU A 1 266 ? -14.430 -7.692  56.126 1.00 12.79 ? 266  LEU A CB  1 
ATOM   2088 C CG  . LEU A 1 266 ? -14.210 -8.968  56.951 1.00 13.97 ? 266  LEU A CG  1 
ATOM   2089 C CD1 . LEU A 1 266 ? -12.712 -9.201  57.210 1.00 18.39 ? 266  LEU A CD1 1 
ATOM   2090 C CD2 . LEU A 1 266 ? -14.906 -8.777  58.276 1.00 17.02 ? 266  LEU A CD2 1 
ATOM   2091 N N   . GLY A 1 267 ? -16.098 -7.060  53.443 1.00 13.69 ? 267  GLY A N   1 
ATOM   2092 C CA  . GLY A 1 267 ? -16.912 -6.060  52.768 1.00 13.09 ? 267  GLY A CA  1 
ATOM   2093 C C   . GLY A 1 267 ? -18.356 -6.406  53.032 1.00 13.26 ? 267  GLY A C   1 
ATOM   2094 O O   . GLY A 1 267 ? -18.678 -7.518  53.471 1.00 13.67 ? 267  GLY A O   1 
ATOM   2095 N N   . ASN A 1 268 ? -19.236 -5.445  52.762 1.00 13.93 ? 268  ASN A N   1 
ATOM   2096 C CA  . ASN A 1 268 ? -20.658 -5.696  52.927 1.00 15.34 ? 268  ASN A CA  1 
ATOM   2097 C C   . ASN A 1 268 ? -21.308 -6.309  51.707 1.00 15.20 ? 268  ASN A C   1 
ATOM   2098 O O   . ASN A 1 268 ? -22.471 -6.763  51.770 1.00 14.32 ? 268  ASN A O   1 
ATOM   2099 C CB  . ASN A 1 268 ? -21.386 -4.391  53.297 1.00 16.50 ? 268  ASN A CB  1 
ATOM   2100 C CG  . ASN A 1 268 ? -21.080 -3.955  54.712 1.00 20.38 ? 268  ASN A CG  1 
ATOM   2101 O OD1 . ASN A 1 268 ? -20.718 -4.779  55.560 1.00 23.44 ? 268  ASN A OD1 1 
ATOM   2102 N ND2 . ASN A 1 268 ? -21.193 -2.647  54.973 1.00 21.34 ? 268  ASN A ND2 1 
ATOM   2103 N N   . THR A 1 269 ? -20.573 -6.310  50.597 1.00 14.39 ? 269  THR A N   1 
ATOM   2104 C CA  . THR A 1 269 ? -20.991 -6.864  49.314 1.00 15.06 ? 269  THR A CA  1 
ATOM   2105 C C   . THR A 1 269 ? -19.752 -7.415  48.607 1.00 14.31 ? 269  THR A C   1 
ATOM   2106 O O   . THR A 1 269 ? -18.625 -7.026  48.982 1.00 13.66 ? 269  THR A O   1 
ATOM   2107 C CB  . THR A 1 269 ? -21.539 -5.763  48.376 1.00 14.36 ? 269  THR A CB  1 
ATOM   2108 O OG1 . THR A 1 269 ? -20.508 -4.807  48.138 1.00 17.21 ? 269  THR A OG1 1 
ATOM   2109 C CG2 . THR A 1 269 ? -22.769 -5.038  48.971 1.00 15.99 ? 269  THR A CG2 1 
ATOM   2110 N N   . PRO A 1 270 ? -19.939 -8.291  47.591 1.00 14.57 ? 270  PRO A N   1 
ATOM   2111 C CA  . PRO A 1 270 ? -18.779 -8.757  46.786 1.00 14.27 ? 270  PRO A CA  1 
ATOM   2112 C C   . PRO A 1 270 ? -17.980 -7.606  46.167 1.00 14.69 ? 270  PRO A C   1 
ATOM   2113 O O   . PRO A 1 270 ? -16.733 -7.622  46.253 1.00 13.59 ? 270  PRO A O   1 
ATOM   2114 C CB  . PRO A 1 270 ? -19.425 -9.651  45.718 1.00 14.63 ? 270  PRO A CB  1 
ATOM   2115 C CG  . PRO A 1 270 ? -20.702 -10.197 46.440 1.00 14.32 ? 270  PRO A CG  1 
ATOM   2116 C CD  . PRO A 1 270 ? -21.198 -8.960  47.167 1.00 13.17 ? 270  PRO A CD  1 
ATOM   2117 N N   . GLU A 1 271 ? -18.662 -6.576  45.640 1.00 13.79 ? 271  GLU A N   1 
ATOM   2118 C CA  . GLU A 1 271 ? -17.962 -5.406  45.091 1.00 14.90 ? 271  GLU A CA  1 
ATOM   2119 C C   . GLU A 1 271 ? -17.033 -4.705  46.097 1.00 14.60 ? 271  GLU A C   1 
ATOM   2120 O O   . GLU A 1 271 ? -15.893 -4.309  45.750 1.00 15.55 ? 271  GLU A O   1 
ATOM   2121 C CB  . GLU A 1 271 ? -18.955 -4.385  44.458 1.00 14.62 ? 271  GLU A CB  1 
ATOM   2122 C CG  . GLU A 1 271 ? -19.515 -4.834  43.097 1.00 17.21 ? 271  GLU A CG  1 
ATOM   2123 C CD  . GLU A 1 271 ? -18.446 -4.861  42.006 1.00 18.84 ? 271  GLU A CD  1 
ATOM   2124 O OE1 . GLU A 1 271 ? -17.894 -3.770  41.633 1.00 18.10 ? 271  GLU A OE1 1 
ATOM   2125 O OE2 . GLU A 1 271 ? -18.154 -5.989  41.549 1.00 18.96 ? 271  GLU A OE2 1 
ATOM   2126 N N   . GLN A 1 272 ? -17.496 -4.566  47.336 1.00 14.20 ? 272  GLN A N   1 
ATOM   2127 C CA  . GLN A 1 272 ? -16.682 -3.917  48.368 1.00 14.05 ? 272  GLN A CA  1 
ATOM   2128 C C   . GLN A 1 272 ? -15.418 -4.730  48.687 1.00 14.25 ? 272  GLN A C   1 
ATOM   2129 O O   . GLN A 1 272 ? -14.389 -4.139  49.000 1.00 13.72 ? 272  GLN A O   1 
ATOM   2130 C CB  . GLN A 1 272 ? -17.480 -3.733  49.628 1.00 13.77 ? 272  GLN A CB  1 
ATOM   2131 C CG  . GLN A 1 272 ? -18.495 -2.595  49.463 1.00 15.49 ? 272  GLN A CG  1 
ATOM   2132 C CD  . GLN A 1 272 ? -19.215 -2.297  50.720 1.00 24.23 ? 272  GLN A CD  1 
ATOM   2133 O OE1 . GLN A 1 272 ? -18.871 -2.810  51.800 1.00 26.91 ? 272  GLN A OE1 1 
ATOM   2134 N NE2 . GLN A 1 272 ? -20.236 -1.456  50.609 1.00 26.21 ? 272  GLN A NE2 1 
ATOM   2135 N N   . VAL A 1 273 ? -15.519 -6.049  48.617 1.00 13.42 ? 273  VAL A N   1 
ATOM   2136 C CA  . VAL A 1 273 ? -14.317 -6.938  48.830 1.00 12.90 ? 273  VAL A CA  1 
ATOM   2137 C C   . VAL A 1 273 ? -13.312 -6.681  47.716 1.00 14.38 ? 273  VAL A C   1 
ATOM   2138 O O   . VAL A 1 273 ? -12.114 -6.528  47.978 1.00 14.01 ? 273  VAL A O   1 
ATOM   2139 C CB  . VAL A 1 273 ? -14.666 -8.445  48.876 1.00 14.39 ? 273  VAL A CB  1 
ATOM   2140 C CG1 . VAL A 1 273 ? -13.380 -9.312  48.881 1.00 13.14 ? 273  VAL A CG1 1 
ATOM   2141 C CG2 . VAL A 1 273 ? -15.447 -8.749  50.134 1.00 13.77 ? 273  VAL A CG2 1 
ATOM   2142 N N   . VAL A 1 274 ? -13.791 -6.655  46.473 1.00 12.91 ? 274  VAL A N   1 
ATOM   2143 C CA  . VAL A 1 274 ? -12.912 -6.339  45.353 1.00 12.74 ? 274  VAL A CA  1 
ATOM   2144 C C   . VAL A 1 274 ? -12.278 -4.962  45.549 1.00 13.00 ? 274  VAL A C   1 
ATOM   2145 O O   . VAL A 1 274 ? -11.051 -4.792  45.356 1.00 10.89 ? 274  VAL A O   1 
ATOM   2146 C CB  . VAL A 1 274 ? -13.619 -6.436  43.981 1.00 13.37 ? 274  VAL A CB  1 
ATOM   2147 C CG1 . VAL A 1 274 ? -12.662 -6.034  42.864 1.00 11.47 ? 274  VAL A CG1 1 
ATOM   2148 C CG2 . VAL A 1 274 ? -14.144 -7.873  43.740 1.00 12.21 ? 274  VAL A CG2 1 
ATOM   2149 N N   . GLN A 1 275 ? -13.086 -3.963  45.943 1.00 10.49 ? 275  GLN A N   1 
ATOM   2150 C CA  . GLN A 1 275 ? -12.539 -2.626  46.209 1.00 11.70 ? 275  GLN A CA  1 
ATOM   2151 C C   . GLN A 1 275 ? -11.453 -2.686  47.299 1.00 12.76 ? 275  GLN A C   1 
ATOM   2152 O O   . GLN A 1 275 ? -10.402 -2.024  47.173 1.00 11.19 ? 275  GLN A O   1 
ATOM   2153 C CB  . GLN A 1 275 ? -13.648 -1.629  46.603 1.00 12.45 ? 275  GLN A CB  1 
ATOM   2154 C CG  . GLN A 1 275 ? -14.644 -1.374  45.487 1.00 11.79 ? 275  GLN A CG  1 
ATOM   2155 C CD  . GLN A 1 275 ? -15.943 -0.699  45.998 1.00 15.67 ? 275  GLN A CD  1 
ATOM   2156 O OE1 . GLN A 1 275 ? -16.236 -0.730  47.184 1.00 16.20 ? 275  GLN A OE1 1 
ATOM   2157 N NE2 . GLN A 1 275 ? -16.718 -0.130  45.082 1.00 16.73 ? 275  GLN A NE2 1 
ATOM   2158 N N   . GLU A 1 276 ? -11.676 -3.475  48.348 1.00 10.93 ? 276  GLU A N   1 
ATOM   2159 C CA  . GLU A 1 276 ? -10.668 -3.567  49.427 1.00 12.05 ? 276  GLU A CA  1 
ATOM   2160 C C   . GLU A 1 276 ? -9.383  -4.214  48.935 1.00 12.01 ? 276  GLU A C   1 
ATOM   2161 O O   . GLU A 1 276 ? -8.291  -3.733  49.277 1.00 12.19 ? 276  GLU A O   1 
ATOM   2162 C CB  . GLU A 1 276 ? -11.184 -4.381  50.625 1.00 13.29 ? 276  GLU A CB  1 
ATOM   2163 C CG  . GLU A 1 276 ? -12.337 -3.703  51.388 1.00 14.56 ? 276  GLU A CG  1 
ATOM   2164 C CD  . GLU A 1 276 ? -11.911 -2.414  52.085 1.00 21.86 ? 276  GLU A CD  1 
ATOM   2165 O OE1 . GLU A 1 276 ? -10.681 -2.182  52.267 1.00 25.03 ? 276  GLU A OE1 1 
ATOM   2166 O OE2 . GLU A 1 276 ? -12.805 -1.622  52.482 1.00 24.23 ? 276  GLU A OE2 1 
ATOM   2167 N N   . TYR A 1 277 ? -9.530  -5.283  48.155 1.00 11.70 ? 277  TYR A N   1 
ATOM   2168 C CA  . TYR A 1 277 ? -8.350  -5.966  47.539 1.00 13.75 ? 277  TYR A CA  1 
ATOM   2169 C C   . TYR A 1 277 ? -7.542  -5.002  46.640 1.00 13.48 ? 277  TYR A C   1 
ATOM   2170 O O   . TYR A 1 277 ? -6.321  -4.872  46.773 1.00 12.63 ? 277  TYR A O   1 
ATOM   2171 C CB  . TYR A 1 277 ? -8.815  -7.219  46.759 1.00 15.27 ? 277  TYR A CB  1 
ATOM   2172 C CG  . TYR A 1 277 ? -7.706  -7.855  45.967 1.00 13.08 ? 277  TYR A CG  1 
ATOM   2173 C CD1 . TYR A 1 277 ? -6.507  -8.226  46.595 1.00 13.25 ? 277  TYR A CD1 1 
ATOM   2174 C CD2 . TYR A 1 277 ? -7.848  -8.066  44.607 1.00 13.14 ? 277  TYR A CD2 1 
ATOM   2175 C CE1 . TYR A 1 277 ? -5.463  -8.813  45.866 1.00 15.45 ? 277  TYR A CE1 1 
ATOM   2176 C CE2 . TYR A 1 277 ? -6.827  -8.655  43.860 1.00 15.71 ? 277  TYR A CE2 1 
ATOM   2177 C CZ  . TYR A 1 277 ? -5.637  -9.003  44.503 1.00 15.45 ? 277  TYR A CZ  1 
ATOM   2178 O OH  . TYR A 1 277 ? -4.638  -9.567  43.757 1.00 15.72 ? 277  TYR A OH  1 
ATOM   2179 N N   . LEU A 1 278 ? -8.231  -4.255  45.788 1.00 12.60 ? 278  LEU A N   1 
ATOM   2180 C CA  . LEU A 1 278 ? -7.581  -3.338  44.855 1.00 13.66 ? 278  LEU A CA  1 
ATOM   2181 C C   . LEU A 1 278 ? -6.972  -2.110  45.516 1.00 14.59 ? 278  LEU A C   1 
ATOM   2182 O O   . LEU A 1 278 ? -5.956  -1.547  45.018 1.00 13.43 ? 278  LEU A O   1 
ATOM   2183 C CB  . LEU A 1 278 ? -8.525  -2.953  43.692 1.00 15.04 ? 278  LEU A CB  1 
ATOM   2184 C CG  . LEU A 1 278 ? -8.950  -4.208  42.881 1.00 12.63 ? 278  LEU A CG  1 
ATOM   2185 C CD1 . LEU A 1 278 ? -9.790  -3.780  41.723 1.00 12.56 ? 278  LEU A CD1 1 
ATOM   2186 C CD2 . LEU A 1 278 ? -7.709  -5.064  42.364 1.00 13.22 ? 278  LEU A CD2 1 
ATOM   2187 N N   . GLU A 1 279 ? -7.591  -1.662  46.607 1.00 13.53 ? 279  GLU A N   1 
ATOM   2188 C CA  . GLU A 1 279 ? -7.003  -0.589  47.432 1.00 15.12 ? 279  GLU A CA  1 
ATOM   2189 C C   . GLU A 1 279 ? -5.632  -1.023  47.933 1.00 15.47 ? 279  GLU A C   1 
ATOM   2190 O O   . GLU A 1 279 ? -4.704  -0.216  48.007 1.00 17.13 ? 279  GLU A O   1 
ATOM   2191 C CB  . GLU A 1 279 ? -7.903  -0.254  48.619 1.00 15.83 ? 279  GLU A CB  1 
ATOM   2192 C CG  . GLU A 1 279 ? -7.214  0.576   49.742 1.00 19.19 ? 279  GLU A CG  1 
ATOM   2193 C CD  . GLU A 1 279 ? -6.778  1.973   49.304 1.00 25.65 ? 279  GLU A CD  1 
ATOM   2194 O OE1 . GLU A 1 279 ? -7.326  2.521   48.302 1.00 24.86 ? 279  GLU A OE1 1 
ATOM   2195 O OE2 . GLU A 1 279 ? -5.867  2.539   49.963 1.00 24.35 ? 279  GLU A OE2 1 
ATOM   2196 N N   . LEU A 1 280 ? -5.514  -2.290  48.279 1.00 15.23 ? 280  LEU A N   1 
ATOM   2197 C CA  . LEU A 1 280 ? -4.203  -2.849  48.686 1.00 14.85 ? 280  LEU A CA  1 
ATOM   2198 C C   . LEU A 1 280 ? -3.225  -2.973  47.503 1.00 15.51 ? 280  LEU A C   1 
ATOM   2199 O O   . LEU A 1 280 ? -2.147  -2.340  47.475 1.00 14.34 ? 280  LEU A O   1 
ATOM   2200 C CB  . LEU A 1 280 ? -4.376  -4.187  49.413 1.00 14.15 ? 280  LEU A CB  1 
ATOM   2201 C CG  . LEU A 1 280 ? -2.964  -4.769  49.685 1.00 16.70 ? 280  LEU A CG  1 
ATOM   2202 C CD1 . LEU A 1 280 ? -2.262  -3.940  50.774 1.00 12.79 ? 280  LEU A CD1 1 
ATOM   2203 C CD2 . LEU A 1 280 ? -3.033  -6.209  49.994 1.00 14.32 ? 280  LEU A CD2 1 
ATOM   2204 N N   . ILE A 1 281 ? -3.630  -3.739  46.506 1.00 14.54 ? 281  ILE A N   1 
ATOM   2205 C CA  . ILE A 1 281 ? -2.695  -4.233  45.484 1.00 16.29 ? 281  ILE A CA  1 
ATOM   2206 C C   . ILE A 1 281 ? -2.485  -3.258  44.332 1.00 16.01 ? 281  ILE A C   1 
ATOM   2207 O O   . ILE A 1 281 ? -1.508  -3.371  43.613 1.00 15.61 ? 281  ILE A O   1 
ATOM   2208 C CB  . ILE A 1 281 ? -3.179  -5.624  44.984 1.00 17.26 ? 281  ILE A CB  1 
ATOM   2209 C CG1 . ILE A 1 281 ? -2.011  -6.481  44.514 1.00 19.86 ? 281  ILE A CG1 1 
ATOM   2210 C CG2 . ILE A 1 281 ? -4.297  -5.485  43.919 1.00 15.18 ? 281  ILE A CG2 1 
ATOM   2211 C CD1 . ILE A 1 281 ? -1.214  -7.020  45.678 1.00 21.61 ? 281  ILE A CD1 1 
ATOM   2212 N N   . GLY A 1 282 ? -3.363  -2.253  44.194 1.00 13.07 ? 282  GLY A N   1 
ATOM   2213 C CA  . GLY A 1 282 ? -3.244  -1.313  43.092 1.00 14.82 ? 282  GLY A CA  1 
ATOM   2214 C C   . GLY A 1 282 ? -4.474  -1.416  42.203 1.00 14.39 ? 282  GLY A C   1 
ATOM   2215 O O   . GLY A 1 282 ? -4.743  -2.487  41.651 1.00 14.09 ? 282  GLY A O   1 
ATOM   2216 N N   . ARG A 1 283 ? -5.199  -0.301  42.058 1.00 13.80 ? 283  ARG A N   1 
ATOM   2217 C CA  . ARG A 1 283 ? -6.359  -0.276  41.157 1.00 13.75 ? 283  ARG A CA  1 
ATOM   2218 C C   . ARG A 1 283 ? -5.914  -0.250  39.718 1.00 14.92 ? 283  ARG A C   1 
ATOM   2219 O O   . ARG A 1 283 ? -4.783  0.230   39.405 1.00 15.42 ? 283  ARG A O   1 
ATOM   2220 C CB  . ARG A 1 283 ? -7.288  0.929   41.470 1.00 13.02 ? 283  ARG A CB  1 
ATOM   2221 C CG  . ARG A 1 283 ? -8.099  0.690   42.676 1.00 12.09 ? 283  ARG A CG  1 
ATOM   2222 C CD  . ARG A 1 283 ? -9.038  1.903   42.971 1.00 15.84 ? 283  ARG A CD  1 
ATOM   2223 N NE  . ARG A 1 283 ? -8.251  3.061   43.422 1.00 16.26 ? 283  ARG A NE  1 
ATOM   2224 C CZ  . ARG A 1 283 ? -7.898  3.279   44.684 1.00 18.24 ? 283  ARG A CZ  1 
ATOM   2225 N NH1 . ARG A 1 283 ? -8.258  2.455   45.672 1.00 19.66 ? 283  ARG A NH1 1 
ATOM   2226 N NH2 . ARG A 1 283 ? -7.195  4.347   44.966 1.00 23.19 ? 283  ARG A NH2 1 
ATOM   2227 N N   . PRO A 1 284 ? -6.769  -0.749  38.811 1.00 14.24 ? 284  PRO A N   1 
ATOM   2228 C CA  . PRO A 1 284 ? -6.337  -0.762  37.402 1.00 15.09 ? 284  PRO A CA  1 
ATOM   2229 C C   . PRO A 1 284 ? -6.158  0.613   36.785 1.00 14.89 ? 284  PRO A C   1 
ATOM   2230 O O   . PRO A 1 284 ? -6.802  1.589   37.203 1.00 16.52 ? 284  PRO A O   1 
ATOM   2231 C CB  . PRO A 1 284 ? -7.487  -1.459  36.672 1.00 15.29 ? 284  PRO A CB  1 
ATOM   2232 C CG  . PRO A 1 284 ? -8.686  -1.274  37.605 1.00 14.70 ? 284  PRO A CG  1 
ATOM   2233 C CD  . PRO A 1 284 ? -8.141  -1.301  38.991 1.00 14.35 ? 284  PRO A CD  1 
ATOM   2234 N N   . ALA A 1 285 ? -5.273  0.688   35.804 1.00 15.26 ? 285  ALA A N   1 
ATOM   2235 C CA  . ALA A 1 285 ? -5.088  1.884   35.010 1.00 15.60 ? 285  ALA A CA  1 
ATOM   2236 C C   . ALA A 1 285 ? -6.387  2.241   34.292 1.00 15.86 ? 285  ALA A C   1 
ATOM   2237 O O   . ALA A 1 285 ? -7.139  1.353   33.891 1.00 16.04 ? 285  ALA A O   1 
ATOM   2238 C CB  . ALA A 1 285 ? -3.969  1.660   33.989 1.00 15.69 ? 285  ALA A CB  1 
ATOM   2239 N N   . LEU A 1 286 ? -6.639  3.530   34.125 1.00 15.81 ? 286  LEU A N   1 
ATOM   2240 C CA  . LEU A 1 286 ? -7.710  3.963   33.232 1.00 16.71 ? 286  LEU A CA  1 
ATOM   2241 C C   . LEU A 1 286 ? -7.171  3.798   31.829 1.00 15.72 ? 286  LEU A C   1 
ATOM   2242 O O   . LEU A 1 286 ? -6.091  4.362   31.495 1.00 17.06 ? 286  LEU A O   1 
ATOM   2243 C CB  . LEU A 1 286 ? -8.103  5.426   33.508 1.00 16.30 ? 286  LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 286 ? -9.276  6.059   32.742 1.00 17.30 ? 286  LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 286 ? -10.615 5.397   33.070 1.00 17.87 ? 286  LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 286 ? -9.330  7.547   33.101 1.00 17.47 ? 286  LEU A CD2 1 
ATOM   2247 N N   . PRO A 1 287 ? -7.887  3.028   30.991 1.00 16.31 ? 287  PRO A N   1 
ATOM   2248 C CA  . PRO A 1 287 ? -7.373  2.830   29.640 1.00 16.25 ? 287  PRO A CA  1 
ATOM   2249 C C   . PRO A 1 287 ? -7.525  4.090   28.790 1.00 15.85 ? 287  PRO A C   1 
ATOM   2250 O O   . PRO A 1 287 ? -8.343  4.986   29.122 1.00 15.65 ? 287  PRO A O   1 
ATOM   2251 C CB  . PRO A 1 287 ? -8.277  1.741   29.068 1.00 16.35 ? 287  PRO A CB  1 
ATOM   2252 C CG  . PRO A 1 287 ? -9.564  1.920   29.804 1.00 18.37 ? 287  PRO A CG  1 
ATOM   2253 C CD  . PRO A 1 287 ? -9.182  2.344   31.198 1.00 16.19 ? 287  PRO A CD  1 
ATOM   2254 N N   . SER A 1 288 ? -6.764  4.147   27.700 1.00 15.09 ? 288  SER A N   1 
ATOM   2255 C CA  . SER A 1 288 ? -7.040  5.124   26.640 1.00 13.82 ? 288  SER A CA  1 
ATOM   2256 C C   . SER A 1 288 ? -8.406  4.773   26.125 1.00 14.34 ? 288  SER A C   1 
ATOM   2257 O O   . SER A 1 288 ? -8.761  3.588   26.017 1.00 11.87 ? 288  SER A O   1 
ATOM   2258 C CB  . SER A 1 288 ? -6.040  5.005   25.504 1.00 14.60 ? 288  SER A CB  1 
ATOM   2259 O OG  . SER A 1 288 ? -4.741  5.351   26.003 1.00 12.59 ? 288  SER A OG  1 
ATOM   2260 N N   . TYR A 1 289 ? -9.189  5.793   25.821 1.00 13.81 ? 289  TYR A N   1 
ATOM   2261 C CA  . TYR A 1 289 ? -10.564 5.509   25.365 1.00 13.97 ? 289  TYR A CA  1 
ATOM   2262 C C   . TYR A 1 289 ? -10.547 4.682   24.066 1.00 14.65 ? 289  TYR A C   1 
ATOM   2263 O O   . TYR A 1 289 ? -11.408 3.821   23.854 1.00 14.53 ? 289  TYR A O   1 
ATOM   2264 C CB  . TYR A 1 289 ? -11.253 6.851   25.183 1.00 14.95 ? 289  TYR A CB  1 
ATOM   2265 C CG  . TYR A 1 289 ? -12.752 6.818   24.993 1.00 15.33 ? 289  TYR A CG  1 
ATOM   2266 C CD1 . TYR A 1 289 ? -13.605 7.101   26.049 1.00 17.42 ? 289  TYR A CD1 1 
ATOM   2267 C CD2 . TYR A 1 289 ? -13.297 6.616   23.736 1.00 15.47 ? 289  TYR A CD2 1 
ATOM   2268 C CE1 . TYR A 1 289 ? -15.023 7.141   25.845 1.00 16.19 ? 289  TYR A CE1 1 
ATOM   2269 C CE2 . TYR A 1 289 ? -14.710 6.644   23.527 1.00 18.13 ? 289  TYR A CE2 1 
ATOM   2270 C CZ  . TYR A 1 289 ? -15.535 6.927   24.600 1.00 15.53 ? 289  TYR A CZ  1 
ATOM   2271 O OH  . TYR A 1 289 ? -16.911 6.988   24.419 1.00 16.15 ? 289  TYR A OH  1 
ATOM   2272 N N   . TRP A 1 290 ? -9.513  4.864   23.226 1.00 14.14 ? 290  TRP A N   1 
ATOM   2273 C CA  . TRP A 1 290 ? -9.453  4.089   21.984 1.00 14.63 ? 290  TRP A CA  1 
ATOM   2274 C C   . TRP A 1 290 ? -9.256  2.575   22.173 1.00 14.25 ? 290  TRP A C   1 
ATOM   2275 O O   . TRP A 1 290 ? -9.649  1.777   21.309 1.00 13.42 ? 290  TRP A O   1 
ATOM   2276 C CB  . TRP A 1 290 ? -8.392  4.636   21.040 1.00 16.14 ? 290  TRP A CB  1 
ATOM   2277 C CG  . TRP A 1 290 ? -6.950  4.701   21.556 1.00 14.56 ? 290  TRP A CG  1 
ATOM   2278 C CD1 . TRP A 1 290 ? -6.304  5.791   22.011 1.00 15.63 ? 290  TRP A CD1 1 
ATOM   2279 C CD2 . TRP A 1 290 ? -5.976  3.631   21.534 1.00 15.96 ? 290  TRP A CD2 1 
ATOM   2280 N NE1 . TRP A 1 290 ? -4.983  5.480   22.290 1.00 14.54 ? 290  TRP A NE1 1 
ATOM   2281 C CE2 . TRP A 1 290 ? -4.772  4.153   22.032 1.00 15.58 ? 290  TRP A CE2 1 
ATOM   2282 C CE3 . TRP A 1 290 ? -6.038  2.274   21.202 1.00 15.23 ? 290  TRP A CE3 1 
ATOM   2283 C CZ2 . TRP A 1 290 ? -3.591  3.364   22.145 1.00 16.30 ? 290  TRP A CZ2 1 
ATOM   2284 C CZ3 . TRP A 1 290 ? -4.887  1.498   21.303 1.00 17.59 ? 290  TRP A CZ3 1 
ATOM   2285 C CH2 . TRP A 1 290 ? -3.684  2.051   21.773 1.00 15.80 ? 290  TRP A CH2 1 
ATOM   2286 N N   . ALA A 1 291 ? -8.645  2.206   23.300 1.00 13.62 ? 291  ALA A N   1 
ATOM   2287 C CA  . ALA A 1 291 ? -8.405  0.793   23.638 1.00 14.87 ? 291  ALA A CA  1 
ATOM   2288 C C   . ALA A 1 291 ? -9.699  0.054   23.923 1.00 14.90 ? 291  ALA A C   1 
ATOM   2289 O O   . ALA A 1 291 ? -9.731  -1.156  23.918 1.00 13.58 ? 291  ALA A O   1 
ATOM   2290 C CB  . ALA A 1 291 ? -7.493  0.694   24.824 1.00 14.54 ? 291  ALA A CB  1 
ATOM   2291 N N   . LEU A 1 292 ? -10.779 0.804   24.183 1.00 14.82 ? 292  LEU A N   1 
ATOM   2292 C CA  . LEU A 1 292 ? -12.102 0.203   24.408 1.00 15.25 ? 292  LEU A CA  1 
ATOM   2293 C C   . LEU A 1 292 ? -12.756 -0.195  23.086 1.00 15.25 ? 292  LEU A C   1 
ATOM   2294 O O   . LEU A 1 292 ? -13.780 -0.882  23.046 1.00 15.86 ? 292  LEU A O   1 
ATOM   2295 C CB  . LEU A 1 292 ? -13.026 1.200   25.152 1.00 15.72 ? 292  LEU A CB  1 
ATOM   2296 C CG  . LEU A 1 292 ? -12.650 1.688   26.568 1.00 18.99 ? 292  LEU A CG  1 
ATOM   2297 C CD1 . LEU A 1 292 ? -13.791 2.583   27.077 1.00 21.75 ? 292  LEU A CD1 1 
ATOM   2298 C CD2 . LEU A 1 292 ? -12.457 0.527   27.474 1.00 23.21 ? 292  LEU A CD2 1 
ATOM   2299 N N   . GLY A 1 293 ? -12.186 0.232   21.980 1.00 15.31 ? 293  GLY A N   1 
ATOM   2300 C CA  . GLY A 1 293 ? -12.760 -0.129  20.690 1.00 14.96 ? 293  GLY A CA  1 
ATOM   2301 C C   . GLY A 1 293 ? -12.441 -1.559  20.319 1.00 14.64 ? 293  GLY A C   1 
ATOM   2302 O O   . GLY A 1 293 ? -11.891 -2.330  21.127 1.00 16.22 ? 293  GLY A O   1 
ATOM   2303 N N   . PHE A 1 294 ? -12.738 -1.914  19.084 1.00 14.08 ? 294  PHE A N   1 
ATOM   2304 C CA  . PHE A 1 294 ? -12.503 -3.261  18.611 1.00 14.02 ? 294  PHE A CA  1 
ATOM   2305 C C   . PHE A 1 294 ? -11.060 -3.339  18.083 1.00 14.16 ? 294  PHE A C   1 
ATOM   2306 O O   . PHE A 1 294 ? -10.608 -2.408  17.400 1.00 14.69 ? 294  PHE A O   1 
ATOM   2307 C CB  . PHE A 1 294 ? -13.463 -3.588  17.491 1.00 13.62 ? 294  PHE A CB  1 
ATOM   2308 C CG  . PHE A 1 294 ? -13.267 -4.967  16.898 1.00 15.57 ? 294  PHE A CG  1 
ATOM   2309 C CD1 . PHE A 1 294 ? -13.476 -6.123  17.682 1.00 14.37 ? 294  PHE A CD1 1 
ATOM   2310 C CD2 . PHE A 1 294 ? -12.925 -5.108  15.560 1.00 16.48 ? 294  PHE A CD2 1 
ATOM   2311 C CE1 . PHE A 1 294 ? -13.325 -7.416  17.129 1.00 15.77 ? 294  PHE A CE1 1 
ATOM   2312 C CE2 . PHE A 1 294 ? -12.751 -6.395  14.990 1.00 17.11 ? 294  PHE A CE2 1 
ATOM   2313 C CZ  . PHE A 1 294 ? -12.928 -7.549  15.782 1.00 16.67 ? 294  PHE A CZ  1 
ATOM   2314 N N   . HIS A 1 295 ? -10.374 -4.441  18.383 1.00 14.36 ? 295  HIS A N   1 
ATOM   2315 C CA  . HIS A 1 295 ? -8.982  -4.677  17.974 1.00 15.05 ? 295  HIS A CA  1 
ATOM   2316 C C   . HIS A 1 295 ? -8.951  -5.866  16.994 1.00 15.20 ? 295  HIS A C   1 
ATOM   2317 O O   . HIS A 1 295 ? -9.694  -6.861  17.170 1.00 14.69 ? 295  HIS A O   1 
ATOM   2318 C CB  . HIS A 1 295 ? -8.114  -5.092  19.170 1.00 15.17 ? 295  HIS A CB  1 
ATOM   2319 C CG  . HIS A 1 295 ? -7.938  -4.058  20.250 1.00 16.30 ? 295  HIS A CG  1 
ATOM   2320 N ND1 . HIS A 1 295 ? -8.978  -3.560  21.023 1.00 18.74 ? 295  HIS A ND1 1 
ATOM   2321 C CD2 . HIS A 1 295 ? -6.810  -3.495  20.737 1.00 11.15 ? 295  HIS A CD2 1 
ATOM   2322 C CE1 . HIS A 1 295 ? -8.488  -2.708  21.916 1.00 11.28 ? 295  HIS A CE1 1 
ATOM   2323 N NE2 . HIS A 1 295 ? -7.177  -2.649  21.750 1.00 19.33 ? 295  HIS A NE2 1 
ATOM   2324 N N   . LEU A 1 296 ? -8.090  -5.803  15.975 1.00 14.96 ? 296  LEU A N   1 
ATOM   2325 C CA  . LEU A 1 296 ? -8.007  -6.901  14.999 1.00 15.32 ? 296  LEU A CA  1 
ATOM   2326 C C   . LEU A 1 296 ? -6.533  -7.316  14.859 1.00 15.41 ? 296  LEU A C   1 
ATOM   2327 O O   . LEU A 1 296 ? -5.644  -6.470  14.908 1.00 15.50 ? 296  LEU A O   1 
ATOM   2328 C CB  . LEU A 1 296 ? -8.584  -6.451  13.655 1.00 16.04 ? 296  LEU A CB  1 
ATOM   2329 C CG  . LEU A 1 296 ? -8.724  -7.504  12.555 1.00 17.69 ? 296  LEU A CG  1 
ATOM   2330 C CD1 . LEU A 1 296 ? -9.656  -8.681  12.980 1.00 18.79 ? 296  LEU A CD1 1 
ATOM   2331 C CD2 . LEU A 1 296 ? -9.158  -6.872  11.246 1.00 15.73 ? 296  LEU A CD2 1 
ATOM   2332 N N   . SER A 1 297 ? -6.286  -8.604  14.693 1.00 16.46 ? 297  SER A N   1 
ATOM   2333 C CA  . SER A 1 297 ? -4.918  -9.127  14.805 1.00 17.44 ? 297  SER A CA  1 
ATOM   2334 C C   . SER A 1 297 ? -4.839  -10.486 14.131 1.00 17.43 ? 297  SER A C   1 
ATOM   2335 O O   . SER A 1 297 ? -5.842  -11.198 14.000 1.00 17.96 ? 297  SER A O   1 
ATOM   2336 C CB  . SER A 1 297 ? -4.575  -9.274  16.302 1.00 17.36 ? 297  SER A CB  1 
ATOM   2337 O OG  . SER A 1 297 ? -3.253  -9.772  16.494 1.00 20.15 ? 297  SER A OG  1 
ATOM   2338 N N   . ARG A 1 298 ? -3.648  -10.878 13.675 1.00 17.35 ? 298  ARG A N   1 
ATOM   2339 C CA  . ARG A 1 298 ? -3.415  -12.307 13.493 1.00 16.84 ? 298  ARG A CA  1 
ATOM   2340 C C   . ARG A 1 298 ? -1.956  -12.561 13.541 1.00 17.41 ? 298  ARG A C   1 
ATOM   2341 O O   . ARG A 1 298 ? -1.143  -11.658 13.328 1.00 16.54 ? 298  ARG A O   1 
ATOM   2342 C CB  . ARG A 1 298 ? -4.002  -12.915 12.210 1.00 16.85 ? 298  ARG A CB  1 
ATOM   2343 C CG  . ARG A 1 298 ? -3.208  -12.702 10.931 1.00 18.05 ? 298  ARG A CG  1 
ATOM   2344 C CD  . ARG A 1 298 ? -3.617  -13.669 9.783  1.00 19.18 ? 298  ARG A CD  1 
ATOM   2345 N NE  . ARG A 1 298 ? -3.378  -15.088 10.114 1.00 21.42 ? 298  ARG A NE  1 
ATOM   2346 C CZ  . ARG A 1 298 ? -4.065  -16.112 9.600  1.00 22.14 ? 298  ARG A CZ  1 
ATOM   2347 N NH1 . ARG A 1 298 ? -5.061  -15.900 8.737  1.00 21.31 ? 298  ARG A NH1 1 
ATOM   2348 N NH2 . ARG A 1 298 ? -3.772  -17.367 9.966  1.00 20.62 ? 298  ARG A NH2 1 
ATOM   2349 N N   . TYR A 1 299 ? -1.640  -13.811 13.824 1.00 17.70 ? 299  TYR A N   1 
ATOM   2350 C CA  . TYR A 1 299 ? -0.275  -14.269 13.772 1.00 18.62 ? 299  TYR A CA  1 
ATOM   2351 C C   . TYR A 1 299 ? -0.056  -14.632 12.293 1.00 18.72 ? 299  TYR A C   1 
ATOM   2352 O O   . TYR A 1 299 ? -0.802  -15.430 11.716 1.00 19.37 ? 299  TYR A O   1 
ATOM   2353 C CB  . TYR A 1 299 ? -0.132  -15.446 14.738 1.00 18.34 ? 299  TYR A CB  1 
ATOM   2354 C CG  . TYR A 1 299 ? 1.224   -16.130 14.790 1.00 19.70 ? 299  TYR A CG  1 
ATOM   2355 C CD1 . TYR A 1 299 ? 1.351   -17.379 15.411 1.00 20.31 ? 299  TYR A CD1 1 
ATOM   2356 C CD2 . TYR A 1 299 ? 2.354   -15.550 14.236 1.00 19.59 ? 299  TYR A CD2 1 
ATOM   2357 C CE1 . TYR A 1 299 ? 2.586   -18.041 15.479 1.00 21.46 ? 299  TYR A CE1 1 
ATOM   2358 C CE2 . TYR A 1 299 ? 3.615   -16.211 14.298 1.00 21.96 ? 299  TYR A CE2 1 
ATOM   2359 C CZ  . TYR A 1 299 ? 3.701   -17.459 14.915 1.00 21.24 ? 299  TYR A CZ  1 
ATOM   2360 O OH  . TYR A 1 299 ? 4.907   -18.145 14.999 1.00 21.66 ? 299  TYR A OH  1 
ATOM   2361 N N   . GLU A 1 300 ? 0.910   -13.972 11.671 1.00 19.74 ? 300  GLU A N   1 
ATOM   2362 C CA  . GLU A 1 300 ? 1.330   -14.265 10.304 1.00 21.30 ? 300  GLU A CA  1 
ATOM   2363 C C   . GLU A 1 300 ? 0.291   -13.846 9.255  1.00 21.42 ? 300  GLU A C   1 
ATOM   2364 O O   . GLU A 1 300 ? -0.299  -14.686 8.571  1.00 21.98 ? 300  GLU A O   1 
ATOM   2365 C CB  . GLU A 1 300 ? 1.805   -15.723 10.118 1.00 21.92 ? 300  GLU A CB  1 
ATOM   2366 C CG  . GLU A 1 300 ? 3.169   -16.036 10.746 1.00 27.30 ? 300  GLU A CG  1 
ATOM   2367 C CD  . GLU A 1 300 ? 4.361   -15.561 9.952  1.00 31.07 ? 300  GLU A CD  1 
ATOM   2368 O OE1 . GLU A 1 300 ? 4.213   -15.256 8.743  1.00 31.48 ? 300  GLU A OE1 1 
ATOM   2369 O OE2 . GLU A 1 300 ? 5.463   -15.493 10.555 1.00 36.47 ? 300  GLU A OE2 1 
ATOM   2370 N N   . TYR A 1 301 ? 0.089   -12.536 9.128  1.00 20.90 ? 301  TYR A N   1 
ATOM   2371 C CA  . TYR A 1 301 ? -0.352  -11.982 7.843  1.00 20.55 ? 301  TYR A CA  1 
ATOM   2372 C C   . TYR A 1 301 ? 0.710   -12.303 6.792  1.00 20.94 ? 301  TYR A C   1 
ATOM   2373 O O   . TYR A 1 301 ? 0.373   -12.536 5.643  1.00 20.33 ? 301  TYR A O   1 
ATOM   2374 C CB  . TYR A 1 301 ? -0.566  -10.480 7.891  1.00 20.04 ? 301  TYR A CB  1 
ATOM   2375 C CG  . TYR A 1 301 ? -1.724  -10.076 8.763  1.00 19.39 ? 301  TYR A CG  1 
ATOM   2376 C CD1 . TYR A 1 301 ? -3.044  -10.237 8.318  1.00 17.70 ? 301  TYR A CD1 1 
ATOM   2377 C CD2 . TYR A 1 301 ? -1.491  -9.547  10.035 1.00 20.49 ? 301  TYR A CD2 1 
ATOM   2378 C CE1 . TYR A 1 301 ? -4.133  -9.863  9.143  1.00 19.27 ? 301  TYR A CE1 1 
ATOM   2379 C CE2 . TYR A 1 301 ? -2.549  -9.151  10.852 1.00 18.66 ? 301  TYR A CE2 1 
ATOM   2380 C CZ  . TYR A 1 301 ? -3.863  -9.317  10.398 1.00 18.77 ? 301  TYR A CZ  1 
ATOM   2381 O OH  . TYR A 1 301 ? -4.906  -8.956  11.227 1.00 18.83 ? 301  TYR A OH  1 
ATOM   2382 N N   . GLY A 1 302 ? 1.977   -12.324 7.201  1.00 21.30 ? 302  GLY A N   1 
ATOM   2383 C CA  . GLY A 1 302 ? 3.072   -12.745 6.305  1.00 21.50 ? 302  GLY A CA  1 
ATOM   2384 C C   . GLY A 1 302 ? 3.721   -11.557 5.634  1.00 21.05 ? 302  GLY A C   1 
ATOM   2385 O O   . GLY A 1 302 ? 4.957   -11.437 5.611  1.00 20.80 ? 302  GLY A O   1 
ATOM   2386 N N   . THR A 1 303 ? 2.885   -10.680 5.083  1.00 20.41 ? 303  THR A N   1 
ATOM   2387 C CA  . THR A 1 303 ? 3.305   -9.459  4.429  1.00 21.12 ? 303  THR A CA  1 
ATOM   2388 C C   . THR A 1 303 ? 2.420   -8.292  4.808  1.00 21.19 ? 303  THR A C   1 
ATOM   2389 O O   . THR A 1 303 ? 1.266   -8.477  5.190  1.00 20.41 ? 303  THR A O   1 
ATOM   2390 C CB  . THR A 1 303 ? 3.268   -9.539  2.855  1.00 20.51 ? 303  THR A CB  1 
ATOM   2391 O OG1 . THR A 1 303 ? 1.916   -9.666  2.374  1.00 22.10 ? 303  THR A OG1 1 
ATOM   2392 C CG2 . THR A 1 303 ? 4.078   -10.716 2.353  1.00 22.62 ? 303  THR A CG2 1 
ATOM   2393 N N   . LEU A 1 304 ? 2.971   -7.094  4.646  1.00 21.37 ? 304  LEU A N   1 
ATOM   2394 C CA  . LEU A 1 304 ? 2.215   -5.879  4.874  1.00 21.15 ? 304  LEU A CA  1 
ATOM   2395 C C   . LEU A 1 304 ? 1.062   -5.756  3.879  1.00 22.46 ? 304  LEU A C   1 
ATOM   2396 O O   . LEU A 1 304 ? -0.002  -5.234  4.231  1.00 22.85 ? 304  LEU A O   1 
ATOM   2397 C CB  . LEU A 1 304 ? 3.142   -4.680  4.786  1.00 20.95 ? 304  LEU A CB  1 
ATOM   2398 C CG  . LEU A 1 304 ? 2.520   -3.309  5.010  1.00 20.27 ? 304  LEU A CG  1 
ATOM   2399 C CD1 . LEU A 1 304 ? 1.886   -3.276  6.399  1.00 18.45 ? 304  LEU A CD1 1 
ATOM   2400 C CD2 . LEU A 1 304 ? 3.580   -2.218  4.863  1.00 19.18 ? 304  LEU A CD2 1 
ATOM   2401 N N   . ASP A 1 305 ? 1.277   -6.201  2.639  1.00 23.34 ? 305  ASP A N   1 
ATOM   2402 C CA  . ASP A 1 305 ? 0.210   -6.246  1.625  1.00 24.50 ? 305  ASP A CA  1 
ATOM   2403 C C   . ASP A 1 305 ? -0.994  -7.070  2.093  1.00 23.74 ? 305  ASP A C   1 
ATOM   2404 O O   . ASP A 1 305 ? -2.153  -6.667  1.909  1.00 22.18 ? 305  ASP A O   1 
ATOM   2405 C CB  . ASP A 1 305 ? 0.715   -6.840  0.307  1.00 26.17 ? 305  ASP A CB  1 
ATOM   2406 C CG  . ASP A 1 305 ? 1.588   -5.880  -0.511 1.00 29.79 ? 305  ASP A CG  1 
ATOM   2407 O OD1 . ASP A 1 305 ? 1.770   -4.690  -0.159 1.00 34.21 ? 305  ASP A OD1 1 
ATOM   2408 O OD2 . ASP A 1 305 ? 2.090   -6.349  -1.559 1.00 35.24 ? 305  ASP A OD2 1 
ATOM   2409 N N   . ASN A 1 306 ? -0.708  -8.234  2.671  1.00 22.68 ? 306  ASN A N   1 
ATOM   2410 C CA  . ASN A 1 306 ? -1.737  -9.090  3.257  1.00 23.49 ? 306  ASN A CA  1 
ATOM   2411 C C   . ASN A 1 306 ? -2.414  -8.441  4.455  1.00 22.69 ? 306  ASN A C   1 
ATOM   2412 O O   . ASN A 1 306 ? -3.631  -8.512  4.570  1.00 23.95 ? 306  ASN A O   1 
ATOM   2413 C CB  . ASN A 1 306 ? -1.155  -10.453 3.656  1.00 23.71 ? 306  ASN A CB  1 
ATOM   2414 C CG  . ASN A 1 306 ? -0.840  -11.326 2.451  1.00 26.03 ? 306  ASN A CG  1 
ATOM   2415 O OD1 . ASN A 1 306 ? -1.363  -11.113 1.355  1.00 27.98 ? 306  ASN A OD1 1 
ATOM   2416 N ND2 . ASN A 1 306 ? 0.014   -12.314 2.652  1.00 27.28 ? 306  ASN A ND2 1 
ATOM   2417 N N   . MET A 1 307 ? -1.635  -7.811  5.338  1.00 22.46 ? 307  MET A N   1 
ATOM   2418 C CA  . MET A 1 307 ? -2.216  -7.068  6.477  1.00 22.51 ? 307  MET A CA  1 
ATOM   2419 C C   . MET A 1 307 ? -3.105  -5.933  5.962  1.00 22.59 ? 307  MET A C   1 
ATOM   2420 O O   . MET A 1 307 ? -4.245  -5.769  6.398  1.00 21.90 ? 307  MET A O   1 
ATOM   2421 C CB  . MET A 1 307 ? -1.109  -6.535  7.408  1.00 22.43 ? 307  MET A CB  1 
ATOM   2422 C CG  . MET A 1 307 ? -1.630  -5.785  8.659  1.00 22.15 ? 307  MET A CG  1 
ATOM   2423 S SD  . MET A 1 307 ? -0.259  -5.125  9.594  1.00 24.65 ? 307  MET A SD  1 
ATOM   2424 C CE  . MET A 1 307 ? 0.335   -6.612  10.370 1.00 22.36 ? 307  MET A CE  1 
ATOM   2425 N N   . ARG A 1 308 ? -2.573  -5.169  5.002  1.00 22.81 ? 308  ARG A N   1 
ATOM   2426 C CA  . ARG A 1 308 ? -3.231  -4.013  4.395  1.00 24.71 ? 308  ARG A CA  1 
ATOM   2427 C C   . ARG A 1 308 ? -4.548  -4.446  3.705  1.00 23.96 ? 308  ARG A C   1 
ATOM   2428 O O   . ARG A 1 308 ? -5.558  -3.732  3.801  1.00 22.70 ? 308  ARG A O   1 
ATOM   2429 C CB  . ARG A 1 308 ? -2.168  -3.326  3.479  1.00 24.59 ? 308  ARG A CB  1 
ATOM   2430 C CG  . ARG A 1 308 ? -2.490  -2.191  2.563  1.00 29.83 ? 308  ARG A CG  1 
ATOM   2431 C CD  . ARG A 1 308 ? -1.142  -1.745  1.887  1.00 29.27 ? 308  ARG A CD  1 
ATOM   2432 N NE  . ARG A 1 308 ? -0.541  -0.566  2.523  1.00 37.04 ? 308  ARG A NE  1 
ATOM   2433 C CZ  . ARG A 1 308 ? 0.755   -0.237  2.469  1.00 39.08 ? 308  ARG A CZ  1 
ATOM   2434 N NH1 . ARG A 1 308 ? 1.646   -1.013  1.860  1.00 38.82 ? 308  ARG A NH1 1 
ATOM   2435 N NH2 . ARG A 1 308 ? 1.175   0.873   3.049  1.00 40.44 ? 308  ARG A NH2 1 
ATOM   2436 N N   . GLU A 1 309 ? -4.563  -5.626  3.073  1.00 23.13 ? 309  GLU A N   1 
ATOM   2437 C CA  . GLU A 1 309 ? -5.778  -6.193  2.455  1.00 24.18 ? 309  GLU A CA  1 
ATOM   2438 C C   . GLU A 1 309 ? -6.864  -6.511  3.493  1.00 22.33 ? 309  GLU A C   1 
ATOM   2439 O O   . GLU A 1 309 ? -8.048  -6.260  3.269  1.00 21.76 ? 309  GLU A O   1 
ATOM   2440 C CB  . GLU A 1 309 ? -5.472  -7.471  1.650  1.00 24.25 ? 309  GLU A CB  1 
ATOM   2441 C CG  . GLU A 1 309 ? -6.719  -8.070  0.916  1.00 25.67 ? 309  GLU A CG  1 
ATOM   2442 C CD  . GLU A 1 309 ? -6.410  -9.361  0.154  1.00 29.41 ? 309  GLU A CD  1 
ATOM   2443 O OE1 . GLU A 1 309 ? -5.193  -9.686  -0.014 1.00 35.57 ? 309  GLU A OE1 1 
ATOM   2444 O OE2 . GLU A 1 309 ? -7.385  -10.069 -0.226 1.00 33.88 ? 309  GLU A OE2 1 
ATOM   2445 N N   . VAL A 1 310 ? -6.451  -7.097  4.609  1.00 20.80 ? 310  VAL A N   1 
ATOM   2446 C CA  . VAL A 1 310 ? -7.363  -7.359  5.719  1.00 19.86 ? 310  VAL A CA  1 
ATOM   2447 C C   . VAL A 1 310 ? -7.917  -6.064  6.304  1.00 19.20 ? 310  VAL A C   1 
ATOM   2448 O O   . VAL A 1 310 ? -9.134  -5.955  6.491  1.00 19.16 ? 310  VAL A O   1 
ATOM   2449 C CB  . VAL A 1 310 ? -6.690  -8.240  6.814  1.00 19.57 ? 310  VAL A CB  1 
ATOM   2450 C CG1 . VAL A 1 310 ? -7.555  -8.313  8.080  1.00 19.89 ? 310  VAL A CG1 1 
ATOM   2451 C CG2 . VAL A 1 310 ? -6.440  -9.634  6.258  1.00 19.12 ? 310  VAL A CG2 1 
ATOM   2452 N N   . VAL A 1 311 ? -7.034  -5.098  6.607  1.00 18.89 ? 311  VAL A N   1 
ATOM   2453 C CA  . VAL A 1 311 ? -7.439  -3.788  7.132  1.00 19.53 ? 311  VAL A CA  1 
ATOM   2454 C C   . VAL A 1 311 ? -8.486  -3.187  6.194  1.00 20.17 ? 311  VAL A C   1 
ATOM   2455 O O   . VAL A 1 311 ? -9.546  -2.752  6.640  1.00 19.49 ? 311  VAL A O   1 
ATOM   2456 C CB  . VAL A 1 311 ? -6.248  -2.777  7.274  1.00 19.48 ? 311  VAL A CB  1 
ATOM   2457 C CG1 . VAL A 1 311 ? -6.754  -1.370  7.658  1.00 21.07 ? 311  VAL A CG1 1 
ATOM   2458 C CG2 . VAL A 1 311 ? -5.236  -3.229  8.319  1.00 18.56 ? 311  VAL A CG2 1 
ATOM   2459 N N   . GLU A 1 312 ? -8.195  -3.177  4.896  1.00 20.11 ? 312  GLU A N   1 
ATOM   2460 C CA  . GLU A 1 312 ? -9.081  -2.505  3.965  1.00 22.38 ? 312  GLU A CA  1 
ATOM   2461 C C   . GLU A 1 312 ? -10.466 -3.133  3.794  1.00 21.17 ? 312  GLU A C   1 
ATOM   2462 O O   . GLU A 1 312 ? -11.461 -2.397  3.720  1.00 21.21 ? 312  GLU A O   1 
ATOM   2463 C CB  . GLU A 1 312 ? -8.356  -2.230  2.647  1.00 23.89 ? 312  GLU A CB  1 
ATOM   2464 C CG  . GLU A 1 312 ? -7.326  -1.100  2.870  1.00 29.28 ? 312  GLU A CG  1 
ATOM   2465 C CD  . GLU A 1 312 ? -7.976  0.226   3.339  1.00 38.02 ? 312  GLU A CD  1 
ATOM   2466 O OE1 . GLU A 1 312 ? -8.760  0.827   2.543  1.00 40.80 ? 312  GLU A OE1 1 
ATOM   2467 O OE2 . GLU A 1 312 ? -7.695  0.663   4.494  1.00 38.89 ? 312  GLU A OE2 1 
ATOM   2468 N N   . ARG A 1 313 ? -10.558 -4.462  3.778  1.00 20.15 ? 313  ARG A N   1 
ATOM   2469 C CA  . ARG A 1 313 ? -11.895 -5.094  3.629  1.00 20.44 ? 313  ARG A CA  1 
ATOM   2470 C C   . ARG A 1 313 ? -12.790 -4.893  4.869  1.00 19.65 ? 313  ARG A C   1 
ATOM   2471 O O   . ARG A 1 313 ? -14.027 -4.728  4.756  1.00 19.98 ? 313  ARG A O   1 
ATOM   2472 C CB  . ARG A 1 313 ? -11.813 -6.573  3.214  1.00 20.61 ? 313  ARG A CB  1 
ATOM   2473 C CG  . ARG A 1 313 ? -11.170 -7.510  4.238  1.00 21.44 ? 313  ARG A CG  1 
ATOM   2474 C CD  . ARG A 1 313 ? -11.430 -8.939  3.834  1.00 22.37 ? 313  ARG A CD  1 
ATOM   2475 N NE  . ARG A 1 313 ? -10.719 -9.862  4.705  1.00 21.93 ? 313  ARG A NE  1 
ATOM   2476 C CZ  . ARG A 1 313 ? -9.806  -10.738 4.284  1.00 24.06 ? 313  ARG A CZ  1 
ATOM   2477 N NH1 . ARG A 1 313 ? -9.508  -10.840 2.990  1.00 27.12 ? 313  ARG A NH1 1 
ATOM   2478 N NH2 . ARG A 1 313 ? -9.218  -11.542 5.157  1.00 22.59 ? 313  ARG A NH2 1 
ATOM   2479 N N   . ASN A 1 314 ? -12.182 -4.877  6.050  1.00 19.12 ? 314  ASN A N   1 
ATOM   2480 C CA  . ASN A 1 314 ? -12.947 -4.500  7.271  1.00 19.61 ? 314  ASN A CA  1 
ATOM   2481 C C   . ASN A 1 314 ? -13.352 -3.037  7.357  1.00 20.20 ? 314  ASN A C   1 
ATOM   2482 O O   . ASN A 1 314 ? -14.461 -2.727  7.791  1.00 20.00 ? 314  ASN A O   1 
ATOM   2483 C CB  . ASN A 1 314 ? -12.262 -5.010  8.536  1.00 19.59 ? 314  ASN A CB  1 
ATOM   2484 C CG  . ASN A 1 314 ? -12.274 -6.517  8.604  1.00 19.16 ? 314  ASN A CG  1 
ATOM   2485 O OD1 . ASN A 1 314 ? -13.245 -7.112  9.071  1.00 17.42 ? 314  ASN A OD1 1 
ATOM   2486 N ND2 . ASN A 1 314 ? -11.216 -7.156  8.086  1.00 15.35 ? 314  ASN A ND2 1 
ATOM   2487 N N   . ARG A 1 315 ? -12.470 -2.134  6.931  1.00 20.44 ? 315  ARG A N   1 
ATOM   2488 C CA  . ARG A 1 315 ? -12.816 -0.712  6.775  1.00 20.28 ? 315  ARG A CA  1 
ATOM   2489 C C   . ARG A 1 315 ? -13.896 -0.502  5.698  1.00 21.28 ? 315  ARG A C   1 
ATOM   2490 O O   . ARG A 1 315 ? -14.819 0.288   5.910  1.00 21.71 ? 315  ARG A O   1 
ATOM   2491 C CB  . ARG A 1 315 ? -11.559 0.130   6.460  1.00 20.27 ? 315  ARG A CB  1 
ATOM   2492 C CG  . ARG A 1 315 ? -10.619 0.301   7.669  1.00 19.89 ? 315  ARG A CG  1 
ATOM   2493 C CD  . ARG A 1 315 ? -9.576  1.374   7.454  1.00 21.20 ? 315  ARG A CD  1 
ATOM   2494 N NE  . ARG A 1 315 ? -10.183 2.686   7.464  1.00 26.30 ? 315  ARG A NE  1 
ATOM   2495 C CZ  . ARG A 1 315 ? -10.388 3.436   6.390  1.00 31.46 ? 315  ARG A CZ  1 
ATOM   2496 N NH1 . ARG A 1 315 ? -10.005 3.015   5.187  1.00 32.96 ? 315  ARG A NH1 1 
ATOM   2497 N NH2 . ARG A 1 315 ? -10.986 4.616   6.527  1.00 35.08 ? 315  ARG A NH2 1 
ATOM   2498 N N   . ALA A 1 316 ? -13.794 -1.216  4.572  1.00 21.19 ? 316  ALA A N   1 
ATOM   2499 C CA  . ALA A 1 316 ? -14.825 -1.171  3.490  1.00 22.05 ? 316  ALA A CA  1 
ATOM   2500 C C   . ALA A 1 316 ? -16.204 -1.607  3.999  1.00 22.45 ? 316  ALA A C   1 
ATOM   2501 O O   . ALA A 1 316 ? -17.262 -1.083  3.575  1.00 22.48 ? 316  ALA A O   1 
ATOM   2502 C CB  . ALA A 1 316 ? -14.384 -2.042  2.275  1.00 21.77 ? 316  ALA A CB  1 
ATOM   2503 N N   . ALA A 1 317 ? -16.204 -2.545  4.939  1.00 21.52 ? 317  ALA A N   1 
ATOM   2504 C CA  . ALA A 1 317 ? -17.438 -3.026  5.550  1.00 21.14 ? 317  ALA A CA  1 
ATOM   2505 C C   . ALA A 1 317 ? -18.019 -2.086  6.629  1.00 20.32 ? 317  ALA A C   1 
ATOM   2506 O O   . ALA A 1 317 ? -19.055 -2.403  7.199  1.00 20.81 ? 317  ALA A O   1 
ATOM   2507 C CB  . ALA A 1 317 ? -17.186 -4.383  6.159  1.00 21.27 ? 317  ALA A CB  1 
ATOM   2508 N N   . GLN A 1 318 ? -17.342 -0.980  6.933  1.00 19.16 ? 318  GLN A N   1 
ATOM   2509 C CA  . GLN A 1 318 ? -17.724 -0.024  7.996  1.00 20.85 ? 318  GLN A CA  1 
ATOM   2510 C C   . GLN A 1 318 ? -17.773 -0.695  9.376  1.00 20.80 ? 318  GLN A C   1 
ATOM   2511 O O   . GLN A 1 318 ? -18.639 -0.416  10.208 1.00 23.01 ? 318  GLN A O   1 
ATOM   2512 C CB  . GLN A 1 318 ? -19.032 0.750   7.666  1.00 22.20 ? 318  GLN A CB  1 
ATOM   2513 C CG  . GLN A 1 318 ? -19.014 1.489   6.279  1.00 24.95 ? 318  GLN A CG  1 
ATOM   2514 C CD  . GLN A 1 318 ? -17.875 2.472   6.135  1.00 29.78 ? 318  GLN A CD  1 
ATOM   2515 O OE1 . GLN A 1 318 ? -17.637 3.321   7.003  1.00 30.31 ? 318  GLN A OE1 1 
ATOM   2516 N NE2 . GLN A 1 318 ? -17.120 2.333   5.045  1.00 31.14 ? 318  GLN A NE2 1 
ATOM   2517 N N   . LEU A 1 319 ? -16.826 -1.599  9.602  1.00 20.59 ? 319  LEU A N   1 
ATOM   2518 C CA  . LEU A 1 319 ? -16.709 -2.265  10.898 1.00 20.65 ? 319  LEU A CA  1 
ATOM   2519 C C   . LEU A 1 319 ? -16.195 -1.268  11.930 1.00 19.64 ? 319  LEU A C   1 
ATOM   2520 O O   . LEU A 1 319 ? -15.220 -0.556  11.685 1.00 19.75 ? 319  LEU A O   1 
ATOM   2521 C CB  . LEU A 1 319 ? -15.792 -3.490  10.789 1.00 20.27 ? 319  LEU A CB  1 
ATOM   2522 C CG  . LEU A 1 319 ? -15.875 -4.507  11.941 1.00 21.22 ? 319  LEU A CG  1 
ATOM   2523 C CD1 . LEU A 1 319 ? -17.192 -5.310  11.923 1.00 21.33 ? 319  LEU A CD1 1 
ATOM   2524 C CD2 . LEU A 1 319 ? -14.646 -5.424  11.949 1.00 19.54 ? 319  LEU A CD2 1 
ATOM   2525 N N   . PRO A 1 320 ? -16.862 -1.189  13.102 1.00 19.03 ? 320  PRO A N   1 
ATOM   2526 C CA  . PRO A 1 320 ? -16.235 -0.401  14.149 1.00 17.51 ? 320  PRO A CA  1 
ATOM   2527 C C   . PRO A 1 320 ? -14.882 -1.065  14.442 1.00 16.66 ? 320  PRO A C   1 
ATOM   2528 O O   . PRO A 1 320 ? -14.814 -2.282  14.627 1.00 16.43 ? 320  PRO A O   1 
ATOM   2529 C CB  . PRO A 1 320 ? -17.221 -0.520  15.302 1.00 17.96 ? 320  PRO A CB  1 
ATOM   2530 C CG  . PRO A 1 320 ? -18.555 -0.799  14.575 1.00 17.74 ? 320  PRO A CG  1 
ATOM   2531 C CD  . PRO A 1 320 ? -18.157 -1.750  13.526 1.00 18.05 ? 320  PRO A CD  1 
ATOM   2532 N N   . TYR A 1 321 ? -13.804 -0.296  14.413 1.00 15.94 ? 321  TYR A N   1 
ATOM   2533 C CA  . TYR A 1 321 ? -12.477 -0.937  14.278 1.00 15.57 ? 321  TYR A CA  1 
ATOM   2534 C C   . TYR A 1 321 ? -11.393 0.073   14.591 1.00 16.23 ? 321  TYR A C   1 
ATOM   2535 O O   . TYR A 1 321 ? -11.026 0.905   13.752 1.00 17.06 ? 321  TYR A O   1 
ATOM   2536 C CB  . TYR A 1 321 ? -12.390 -1.552  12.860 1.00 15.59 ? 321  TYR A CB  1 
ATOM   2537 C CG  . TYR A 1 321 ? -11.060 -2.090  12.292 1.00 16.49 ? 321  TYR A CG  1 
ATOM   2538 C CD1 . TYR A 1 321 ? -10.027 -2.542  13.106 1.00 16.32 ? 321  TYR A CD1 1 
ATOM   2539 C CD2 . TYR A 1 321 ? -10.918 -2.210  10.904 1.00 17.79 ? 321  TYR A CD2 1 
ATOM   2540 C CE1 . TYR A 1 321 ? -8.801  -3.056  12.528 1.00 13.23 ? 321  TYR A CE1 1 
ATOM   2541 C CE2 . TYR A 1 321 ? -9.759  -2.713  10.326 1.00 19.18 ? 321  TYR A CE2 1 
ATOM   2542 C CZ  . TYR A 1 321 ? -8.712  -3.127  11.142 1.00 15.63 ? 321  TYR A CZ  1 
ATOM   2543 O OH  . TYR A 1 321 ? -7.615  -3.627  10.550 1.00 19.29 ? 321  TYR A OH  1 
ATOM   2544 N N   . ASP A 1 322 ? -10.904 0.031   15.830 1.00 14.89 ? 322  ASP A N   1 
ATOM   2545 C CA  . ASP A 1 322 ? -10.008 1.076   16.301 1.00 15.22 ? 322  ASP A CA  1 
ATOM   2546 C C   . ASP A 1 322 ? -8.537  0.720   16.193 1.00 15.17 ? 322  ASP A C   1 
ATOM   2547 O O   . ASP A 1 322 ? -7.672  1.623   15.997 1.00 14.56 ? 322  ASP A O   1 
ATOM   2548 C CB  . ASP A 1 322 ? -10.331 1.447   17.754 1.00 14.97 ? 322  ASP A CB  1 
ATOM   2549 C CG  . ASP A 1 322 ? -11.282 2.611   17.834 1.00 18.26 ? 322  ASP A CG  1 
ATOM   2550 O OD1 . ASP A 1 322 ? -10.813 3.748   18.111 1.00 18.27 ? 322  ASP A OD1 1 
ATOM   2551 O OD2 . ASP A 1 322 ? -12.481 2.370   17.530 1.00 17.90 ? 322  ASP A OD2 1 
ATOM   2552 N N   . VAL A 1 323 ? -8.244  -0.572  16.361 1.00 14.30 ? 323  VAL A N   1 
ATOM   2553 C CA  . VAL A 1 323 ? -6.863  -0.956  16.594 1.00 13.55 ? 323  VAL A CA  1 
ATOM   2554 C C   . VAL A 1 323 ? -6.446  -2.108  15.708 1.00 13.78 ? 323  VAL A C   1 
ATOM   2555 O O   . VAL A 1 323 ? -7.155  -3.094  15.581 1.00 12.92 ? 323  VAL A O   1 
ATOM   2556 C CB  . VAL A 1 323 ? -6.620  -1.336  18.103 1.00 13.17 ? 323  VAL A CB  1 
ATOM   2557 C CG1 . VAL A 1 323 ? -5.112  -1.387  18.418 1.00 14.27 ? 323  VAL A CG1 1 
ATOM   2558 C CG2 . VAL A 1 323 ? -7.273  -0.335  19.025 1.00 9.98  ? 323  VAL A CG2 1 
ATOM   2559 N N   . GLN A 1 324 ? -5.263  -1.984  15.100 1.00 13.69 ? 324  GLN A N   1 
ATOM   2560 C CA  . GLN A 1 324 ? -4.705  -3.086  14.339 1.00 14.18 ? 324  GLN A CA  1 
ATOM   2561 C C   . GLN A 1 324 ? -3.467  -3.557  15.098 1.00 14.32 ? 324  GLN A C   1 
ATOM   2562 O O   . GLN A 1 324 ? -2.666  -2.723  15.501 1.00 13.65 ? 324  GLN A O   1 
ATOM   2563 C CB  . GLN A 1 324 ? -4.330  -2.607  12.921 1.00 14.48 ? 324  GLN A CB  1 
ATOM   2564 C CG  . GLN A 1 324 ? -3.731  -3.706  12.020 1.00 14.43 ? 324  GLN A CG  1 
ATOM   2565 C CD  . GLN A 1 324 ? -4.576  -4.996  11.892 1.00 16.66 ? 324  GLN A CD  1 
ATOM   2566 O OE1 . GLN A 1 324 ? -5.765  -4.952  11.611 1.00 18.24 ? 324  GLN A OE1 1 
ATOM   2567 N NE2 . GLN A 1 324 ? -3.923  -6.147  12.039 1.00 15.28 ? 324  GLN A NE2 1 
ATOM   2568 N N   . HIS A 1 325 ? -3.325  -4.875  15.307 1.00 15.36 ? 325  HIS A N   1 
ATOM   2569 C CA  . HIS A 1 325 ? -2.118  -5.418  15.985 1.00 16.43 ? 325  HIS A CA  1 
ATOM   2570 C C   . HIS A 1 325 ? -1.191  -6.023  14.919 1.00 15.94 ? 325  HIS A C   1 
ATOM   2571 O O   . HIS A 1 325 ? -1.630  -6.517  13.881 1.00 16.52 ? 325  HIS A O   1 
ATOM   2572 C CB  . HIS A 1 325 ? -2.461  -6.473  17.066 1.00 17.47 ? 325  HIS A CB  1 
ATOM   2573 C CG  . HIS A 1 325 ? -3.239  -5.948  18.248 1.00 16.76 ? 325  HIS A CG  1 
ATOM   2574 N ND1 . HIS A 1 325 ? -3.029  -6.400  19.530 1.00 18.26 ? 325  HIS A ND1 1 
ATOM   2575 C CD2 . HIS A 1 325 ? -4.197  -4.995  18.345 1.00 15.15 ? 325  HIS A CD2 1 
ATOM   2576 C CE1 . HIS A 1 325 ? -3.824  -5.757  20.365 1.00 18.96 ? 325  HIS A CE1 1 
ATOM   2577 N NE2 . HIS A 1 325 ? -4.547  -4.901  19.669 1.00 15.15 ? 325  HIS A NE2 1 
ATOM   2578 N N   . ALA A 1 326 ? 0.106   -5.896  15.139 1.00 16.27 ? 326  ALA A N   1 
ATOM   2579 C CA  . ALA A 1 326 ? 1.076   -6.443  14.214 1.00 16.34 ? 326  ALA A CA  1 
ATOM   2580 C C   . ALA A 1 326 ? 1.839   -7.436  15.076 1.00 15.98 ? 326  ALA A C   1 
ATOM   2581 O O   . ALA A 1 326 ? 2.408   -7.042  16.085 1.00 15.93 ? 326  ALA A O   1 
ATOM   2582 C CB  . ALA A 1 326 ? 2.035   -5.309  13.689 1.00 15.99 ? 326  ALA A CB  1 
ATOM   2583 N N   . ASP A 1 327 ? 1.795   -8.702  14.690 1.00 16.14 ? 327  ASP A N   1 
ATOM   2584 C CA  . ASP A 1 327 ? 2.420   -9.822  15.423 1.00 17.49 ? 327  ASP A CA  1 
ATOM   2585 C C   . ASP A 1 327 ? 3.847   -9.997  14.880 1.00 18.26 ? 327  ASP A C   1 
ATOM   2586 O O   . ASP A 1 327 ? 4.336   -9.138  14.139 1.00 18.37 ? 327  ASP A O   1 
ATOM   2587 C CB  . ASP A 1 327 ? 1.589   -11.089 15.173 1.00 17.86 ? 327  ASP A CB  1 
ATOM   2588 C CG  . ASP A 1 327 ? 1.730   -12.132 16.259 1.00 19.57 ? 327  ASP A CG  1 
ATOM   2589 O OD1 . ASP A 1 327 ? 2.799   -12.256 16.907 1.00 22.51 ? 327  ASP A OD1 1 
ATOM   2590 O OD2 . ASP A 1 327 ? 0.748   -12.872 16.435 1.00 20.36 ? 327  ASP A OD2 1 
ATOM   2591 N N   . ILE A 1 328 ? 4.529   -11.083 15.237 1.00 18.50 ? 328  ILE A N   1 
ATOM   2592 C CA  . ILE A 1 328 ? 5.976   -11.151 14.973 1.00 19.18 ? 328  ILE A CA  1 
ATOM   2593 C C   . ILE A 1 328 ? 6.358   -11.189 13.511 1.00 19.77 ? 328  ILE A C   1 
ATOM   2594 O O   . ILE A 1 328 ? 7.541   -10.975 13.187 1.00 20.76 ? 328  ILE A O   1 
ATOM   2595 C CB  . ILE A 1 328 ? 6.666   -12.330 15.724 1.00 18.53 ? 328  ILE A CB  1 
ATOM   2596 C CG1 . ILE A 1 328 ? 5.999   -13.678 15.357 1.00 17.17 ? 328  ILE A CG1 1 
ATOM   2597 C CG2 . ILE A 1 328 ? 6.653   -12.041 17.207 1.00 18.97 ? 328  ILE A CG2 1 
ATOM   2598 C CD1 . ILE A 1 328 ? 6.663   -14.910 16.059 1.00 17.73 ? 328  ILE A CD1 1 
ATOM   2599 N N   . ASP A 1 329 ? 5.379   -11.412 12.626 1.00 19.53 ? 329  ASP A N   1 
ATOM   2600 C CA  . ASP A 1 329 ? 5.660   -11.338 11.183 1.00 19.96 ? 329  ASP A CA  1 
ATOM   2601 C C   . ASP A 1 329 ? 6.153   -9.951  10.704 1.00 19.06 ? 329  ASP A C   1 
ATOM   2602 O O   . ASP A 1 329 ? 6.822   -9.878  9.673  1.00 18.81 ? 329  ASP A O   1 
ATOM   2603 C CB  . ASP A 1 329 ? 4.539   -11.946 10.304 1.00 20.87 ? 329  ASP A CB  1 
ATOM   2604 C CG  . ASP A 1 329 ? 3.136   -11.500 10.719 1.00 24.02 ? 329  ASP A CG  1 
ATOM   2605 O OD1 . ASP A 1 329 ? 2.830   -11.508 11.929 1.00 25.78 ? 329  ASP A OD1 1 
ATOM   2606 O OD2 . ASP A 1 329 ? 2.320   -11.169 9.828  1.00 27.13 ? 329  ASP A OD2 1 
ATOM   2607 N N   . TYR A 1 330 ? 5.898   -8.865  11.455 1.00 17.76 ? 330  TYR A N   1 
ATOM   2608 C CA  . TYR A 1 330 ? 6.376   -7.537  11.006 1.00 17.83 ? 330  TYR A CA  1 
ATOM   2609 C C   . TYR A 1 330 ? 7.882   -7.432  11.131 1.00 17.57 ? 330  TYR A C   1 
ATOM   2610 O O   . TYR A 1 330 ? 8.509   -6.624  10.441 1.00 17.96 ? 330  TYR A O   1 
ATOM   2611 C CB  . TYR A 1 330 ? 5.690   -6.351  11.717 1.00 18.03 ? 330  TYR A CB  1 
ATOM   2612 C CG  . TYR A 1 330 ? 6.164   -6.056  13.119 1.00 17.30 ? 330  TYR A CG  1 
ATOM   2613 C CD1 . TYR A 1 330 ? 7.343   -5.352  13.363 1.00 17.95 ? 330  TYR A CD1 1 
ATOM   2614 C CD2 . TYR A 1 330 ? 5.407   -6.445  14.207 1.00 18.96 ? 330  TYR A CD2 1 
ATOM   2615 C CE1 . TYR A 1 330 ? 7.767   -5.090  14.646 1.00 17.49 ? 330  TYR A CE1 1 
ATOM   2616 C CE2 . TYR A 1 330 ? 5.828   -6.210  15.491 1.00 17.56 ? 330  TYR A CE2 1 
ATOM   2617 C CZ  . TYR A 1 330 ? 6.988   -5.518  15.713 1.00 16.51 ? 330  TYR A CZ  1 
ATOM   2618 O OH  . TYR A 1 330 ? 7.386   -5.260  16.997 1.00 16.61 ? 330  TYR A OH  1 
ATOM   2619 N N   . MET A 1 331 ? 8.445   -8.240  12.020 1.00 17.30 ? 331  MET A N   1 
ATOM   2620 C CA  . MET A 1 331 ? 9.853   -8.130  12.407 1.00 18.04 ? 331  MET A CA  1 
ATOM   2621 C C   . MET A 1 331 ? 10.780  -8.675  11.314 1.00 18.34 ? 331  MET A C   1 
ATOM   2622 O O   . MET A 1 331 ? 10.367  -9.453  10.469 1.00 19.25 ? 331  MET A O   1 
ATOM   2623 C CB  . MET A 1 331 ? 10.120  -8.867  13.717 1.00 17.00 ? 331  MET A CB  1 
ATOM   2624 C CG  . MET A 1 331 ? 9.282   -8.386  14.956 1.00 16.94 ? 331  MET A CG  1 
ATOM   2625 S SD  . MET A 1 331 ? 9.512   -9.425  16.369 1.00 19.48 ? 331  MET A SD  1 
ATOM   2626 C CE  . MET A 1 331 ? 8.500   -8.543  17.613 1.00 14.36 ? 331  MET A CE  1 
ATOM   2627 N N   . ASP A 1 332 ? 12.049  -8.276  11.370 1.00 19.63 ? 332  ASP A N   1 
ATOM   2628 C CA  . ASP A 1 332 ? 13.097  -8.871  10.519 1.00 20.87 ? 332  ASP A CA  1 
ATOM   2629 C C   . ASP A 1 332 ? 13.564  -10.146 11.204 1.00 19.56 ? 332  ASP A C   1 
ATOM   2630 O O   . ASP A 1 332 ? 14.269  -10.111 12.231 1.00 18.95 ? 332  ASP A O   1 
ATOM   2631 C CB  . ASP A 1 332 ? 14.257  -7.887  10.344 1.00 20.87 ? 332  ASP A CB  1 
ATOM   2632 C CG  . ASP A 1 332 ? 15.301  -8.373  9.328  1.00 26.58 ? 332  ASP A CG  1 
ATOM   2633 O OD1 . ASP A 1 332 ? 15.299  -9.559  8.951  1.00 29.89 ? 332  ASP A OD1 1 
ATOM   2634 O OD2 . ASP A 1 332 ? 16.144  -7.545  8.949  1.00 31.90 ? 332  ASP A OD2 1 
ATOM   2635 N N   . GLU A 1 333 ? 13.122  -11.276 10.665 1.00 20.09 ? 333  GLU A N   1 
ATOM   2636 C CA  . GLU A 1 333 ? 13.418  -12.605 11.223 1.00 21.14 ? 333  GLU A CA  1 
ATOM   2637 C C   . GLU A 1 333 ? 13.027  -12.737 12.711 1.00 20.47 ? 333  GLU A C   1 
ATOM   2638 O O   . GLU A 1 333 ? 13.786  -13.252 13.536 1.00 19.45 ? 333  GLU A O   1 
ATOM   2639 C CB  . GLU A 1 333 ? 14.892  -13.014 10.950 1.00 22.52 ? 333  GLU A CB  1 
ATOM   2640 C CG  . GLU A 1 333 ? 15.280  -12.855 9.458  1.00 27.84 ? 333  GLU A CG  1 
ATOM   2641 C CD  . GLU A 1 333 ? 14.892  -14.022 8.554  1.00 36.83 ? 333  GLU A CD  1 
ATOM   2642 O OE1 . GLU A 1 333 ? 14.176  -14.957 8.993  1.00 38.81 ? 333  GLU A OE1 1 
ATOM   2643 O OE2 . GLU A 1 333 ? 15.327  -14.010 7.366  1.00 41.41 ? 333  GLU A OE2 1 
ATOM   2644 N N   . ARG A 1 334 ? 11.823  -12.242 13.038 1.00 19.58 ? 334  ARG A N   1 
ATOM   2645 C CA  . ARG A 1 334 ? 11.255  -12.410 14.381 1.00 19.29 ? 334  ARG A CA  1 
ATOM   2646 C C   . ARG A 1 334 ? 12.058  -11.766 15.538 1.00 18.98 ? 334  ARG A C   1 
ATOM   2647 O O   . ARG A 1 334 ? 11.956  -12.176 16.697 1.00 19.20 ? 334  ARG A O   1 
ATOM   2648 C CB  . ARG A 1 334 ? 10.895  -13.887 14.614 1.00 18.87 ? 334  ARG A CB  1 
ATOM   2649 C CG  . ARG A 1 334 ? 9.895   -14.386 13.570 1.00 20.86 ? 334  ARG A CG  1 
ATOM   2650 C CD  . ARG A 1 334 ? 9.545   -15.878 13.702 1.00 22.38 ? 334  ARG A CD  1 
ATOM   2651 N NE  . ARG A 1 334 ? 8.309   -16.191 12.984 1.00 26.12 ? 334  ARG A NE  1 
ATOM   2652 C CZ  . ARG A 1 334 ? 7.631   -17.327 13.122 1.00 28.55 ? 334  ARG A CZ  1 
ATOM   2653 N NH1 . ARG A 1 334 ? 8.076   -18.272 13.942 1.00 30.73 ? 334  ARG A NH1 1 
ATOM   2654 N NH2 . ARG A 1 334 ? 6.524   -17.520 12.439 1.00 29.62 ? 334  ARG A NH2 1 
ATOM   2655 N N   . ARG A 1 335 ? 12.843  -10.735 15.212 1.00 19.16 ? 335  ARG A N   1 
ATOM   2656 C CA  . ARG A 1 335 ? 13.615  -9.984  16.210 1.00 19.11 ? 335  ARG A CA  1 
ATOM   2657 C C   . ARG A 1 335 ? 12.988  -8.653  16.570 1.00 19.02 ? 335  ARG A C   1 
ATOM   2658 O O   . ARG A 1 335 ? 12.610  -7.878  15.670 1.00 20.28 ? 335  ARG A O   1 
ATOM   2659 C CB  . ARG A 1 335 ? 15.032  -9.716  15.682 1.00 20.43 ? 335  ARG A CB  1 
ATOM   2660 C CG  . ARG A 1 335 ? 15.819  -10.979 15.517 1.00 20.12 ? 335  ARG A CG  1 
ATOM   2661 C CD  . ARG A 1 335 ? 17.219  -10.674 15.041 1.00 25.06 ? 335  ARG A CD  1 
ATOM   2662 N NE  . ARG A 1 335 ? 17.180  -10.121 13.695 1.00 26.60 ? 335  ARG A NE  1 
ATOM   2663 C CZ  . ARG A 1 335 ? 18.229  -9.597  13.077 1.00 31.84 ? 335  ARG A CZ  1 
ATOM   2664 N NH1 . ARG A 1 335 ? 19.413  -9.576  13.681 1.00 29.93 ? 335  ARG A NH1 1 
ATOM   2665 N NH2 . ARG A 1 335 ? 18.094  -9.117  11.840 1.00 31.12 ? 335  ARG A NH2 1 
ATOM   2666 N N   . ASP A 1 336 ? 12.886  -8.379  17.875 1.00 20.04 ? 336  ASP A N   1 
ATOM   2667 C CA  . ASP A 1 336 ? 12.305  -7.113  18.392 1.00 19.54 ? 336  ASP A CA  1 
ATOM   2668 C C   . ASP A 1 336 ? 13.022  -5.923  17.776 1.00 20.28 ? 336  ASP A C   1 
ATOM   2669 O O   . ASP A 1 336 ? 14.236  -5.988  17.524 1.00 20.02 ? 336  ASP A O   1 
ATOM   2670 C CB  . ASP A 1 336 ? 12.578  -6.943  19.878 1.00 18.71 ? 336  ASP A CB  1 
ATOM   2671 C CG  . ASP A 1 336 ? 11.697  -7.781  20.771 1.00 19.81 ? 336  ASP A CG  1 
ATOM   2672 O OD1 . ASP A 1 336 ? 10.649  -8.307  20.317 1.00 21.18 ? 336  ASP A OD1 1 
ATOM   2673 O OD2 . ASP A 1 336 ? 12.062  -7.835  21.978 1.00 20.30 ? 336  ASP A OD2 1 
ATOM   2674 N N   . PHE A 1 337 ? 12.285  -4.826  17.614 1.00 18.86 ? 337  PHE A N   1 
ATOM   2675 C CA  . PHE A 1 337 ? 12.824  -3.497  17.250 1.00 19.15 ? 337  PHE A CA  1 
ATOM   2676 C C   . PHE A 1 337 ? 13.449  -3.423  15.847 1.00 19.63 ? 337  PHE A C   1 
ATOM   2677 O O   . PHE A 1 337 ? 14.386  -2.647  15.614 1.00 20.11 ? 337  PHE A O   1 
ATOM   2678 C CB  . PHE A 1 337 ? 13.810  -2.960  18.303 1.00 18.45 ? 337  PHE A CB  1 
ATOM   2679 C CG  . PHE A 1 337 ? 13.328  -3.094  19.719 1.00 19.57 ? 337  PHE A CG  1 
ATOM   2680 C CD1 . PHE A 1 337 ? 12.154  -2.451  20.136 1.00 19.75 ? 337  PHE A CD1 1 
ATOM   2681 C CD2 . PHE A 1 337 ? 14.019  -3.900  20.635 1.00 16.01 ? 337  PHE A CD2 1 
ATOM   2682 C CE1 . PHE A 1 337 ? 11.713  -2.582  21.467 1.00 16.53 ? 337  PHE A CE1 1 
ATOM   2683 C CE2 . PHE A 1 337 ? 13.562  -4.053  21.961 1.00 18.84 ? 337  PHE A CE2 1 
ATOM   2684 C CZ  . PHE A 1 337 ? 12.391  -3.382  22.360 1.00 18.12 ? 337  PHE A CZ  1 
ATOM   2685 N N   . THR A 1 338 ? 12.920  -4.239  14.951 1.00 19.98 ? 338  THR A N   1 
ATOM   2686 C CA  . THR A 1 338 ? 13.230  -4.242  13.541 1.00 20.57 ? 338  THR A CA  1 
ATOM   2687 C C   . THR A 1 338 ? 11.911  -4.451  12.818 1.00 21.00 ? 338  THR A C   1 
ATOM   2688 O O   . THR A 1 338 ? 10.910  -4.882  13.411 1.00 20.39 ? 338  THR A O   1 
ATOM   2689 C CB  . THR A 1 338 ? 14.144  -5.436  13.189 1.00 20.51 ? 338  THR A CB  1 
ATOM   2690 O OG1 . THR A 1 338 ? 13.434  -6.678  13.351 1.00 21.95 ? 338  THR A OG1 1 
ATOM   2691 C CG2 . THR A 1 338 ? 15.400  -5.449  14.087 1.00 20.18 ? 338  THR A CG2 1 
ATOM   2692 N N   . TYR A 1 339 ? 11.894  -4.153  11.535 1.00 20.63 ? 339  TYR A N   1 
ATOM   2693 C CA  . TYR A 1 339 ? 10.847  -4.671  10.697 1.00 21.88 ? 339  TYR A CA  1 
ATOM   2694 C C   . TYR A 1 339 ? 11.445  -5.239  9.418  1.00 22.89 ? 339  TYR A C   1 
ATOM   2695 O O   . TYR A 1 339 ? 12.574  -4.860  9.031  1.00 22.58 ? 339  TYR A O   1 
ATOM   2696 C CB  . TYR A 1 339 ? 9.759   -3.630  10.450 1.00 23.04 ? 339  TYR A CB  1 
ATOM   2697 C CG  . TYR A 1 339 ? 10.094  -2.435  9.584  1.00 24.29 ? 339  TYR A CG  1 
ATOM   2698 C CD1 . TYR A 1 339 ? 10.007  -2.514  8.192  1.00 24.90 ? 339  TYR A CD1 1 
ATOM   2699 C CD2 . TYR A 1 339 ? 10.438  -1.222  10.147 1.00 24.33 ? 339  TYR A CD2 1 
ATOM   2700 C CE1 . TYR A 1 339 ? 10.275  -1.408  7.390  1.00 23.89 ? 339  TYR A CE1 1 
ATOM   2701 C CE2 . TYR A 1 339 ? 10.710  -0.107  9.352  1.00 25.59 ? 339  TYR A CE2 1 
ATOM   2702 C CZ  . TYR A 1 339 ? 10.614  -0.225  7.979  1.00 23.11 ? 339  TYR A CZ  1 
ATOM   2703 O OH  . TYR A 1 339 ? 10.863  0.856   7.195  1.00 27.60 ? 339  TYR A OH  1 
ATOM   2704 N N   . ASP A 1 340 ? 10.709  -6.155  8.796  1.00 22.64 ? 340  ASP A N   1 
ATOM   2705 C CA  . ASP A 1 340 ? 11.148  -6.847  7.589  1.00 24.72 ? 340  ASP A CA  1 
ATOM   2706 C C   . ASP A 1 340 ? 11.112  -5.860  6.415  1.00 24.84 ? 340  ASP A C   1 
ATOM   2707 O O   . ASP A 1 340 ? 10.056  -5.503  5.920  1.00 24.54 ? 340  ASP A O   1 
ATOM   2708 C CB  . ASP A 1 340 ? 10.239  -8.050  7.331  1.00 24.08 ? 340  ASP A CB  1 
ATOM   2709 C CG  . ASP A 1 340 ? 10.737  -8.951  6.210  1.00 26.59 ? 340  ASP A CG  1 
ATOM   2710 O OD1 . ASP A 1 340 ? 11.409  -8.463  5.289  1.00 27.12 ? 340  ASP A OD1 1 
ATOM   2711 O OD2 . ASP A 1 340 ? 10.419  -10.153 6.236  1.00 27.90 ? 340  ASP A OD2 1 
ATOM   2712 N N   . SER A 1 341 ? 12.289  -5.441  5.964  1.00 26.08 ? 341  SER A N   1 
ATOM   2713 C CA  . SER A 1 341 ? 12.414  -4.407  4.928  1.00 26.84 ? 341  SER A CA  1 
ATOM   2714 C C   . SER A 1 341 ? 11.920  -4.859  3.565  1.00 26.61 ? 341  SER A C   1 
ATOM   2715 O O   . SER A 1 341 ? 11.751  -4.036  2.679  1.00 27.40 ? 341  SER A O   1 
ATOM   2716 C CB  . SER A 1 341 ? 13.883  -4.014  4.794  1.00 27.14 ? 341  SER A CB  1 
ATOM   2717 O OG  . SER A 1 341 ? 14.585  -5.160  4.308  1.00 29.75 ? 341  SER A OG  1 
ATOM   2718 N N   . VAL A 1 342 ? 11.704  -6.161  3.380  1.00 26.60 ? 342  VAL A N   1 
ATOM   2719 C CA  . VAL A 1 342 ? 11.119  -6.689  2.139  1.00 26.40 ? 342  VAL A CA  1 
ATOM   2720 C C   . VAL A 1 342 ? 9.618   -6.957  2.301  1.00 25.91 ? 342  VAL A C   1 
ATOM   2721 O O   . VAL A 1 342 ? 8.787   -6.332  1.633  1.00 25.80 ? 342  VAL A O   1 
ATOM   2722 C CB  . VAL A 1 342 ? 11.911  -7.949  1.620  1.00 26.93 ? 342  VAL A CB  1 
ATOM   2723 C CG1 . VAL A 1 342 ? 11.222  -8.640  0.456  1.00 27.26 ? 342  VAL A CG1 1 
ATOM   2724 C CG2 . VAL A 1 342 ? 13.336  -7.533  1.218  1.00 27.79 ? 342  VAL A CG2 1 
ATOM   2725 N N   . ASP A 1 343 ? 9.250   -7.872  3.193  1.00 24.98 ? 343  ASP A N   1 
ATOM   2726 C CA  . ASP A 1 343 ? 7.815   -8.208  3.329  1.00 23.97 ? 343  ASP A CA  1 
ATOM   2727 C C   . ASP A 1 343 ? 6.987   -7.096  3.984  1.00 22.67 ? 343  ASP A C   1 
ATOM   2728 O O   . ASP A 1 343 ? 5.772   -7.018  3.755  1.00 22.07 ? 343  ASP A O   1 
ATOM   2729 C CB  . ASP A 1 343 ? 7.624   -9.509  4.099  1.00 24.66 ? 343  ASP A CB  1 
ATOM   2730 C CG  . ASP A 1 343 ? 7.988   -10.750 3.288  1.00 27.49 ? 343  ASP A CG  1 
ATOM   2731 O OD1 . ASP A 1 343 ? 8.281   -10.653 2.075  1.00 31.53 ? 343  ASP A OD1 1 
ATOM   2732 O OD2 . ASP A 1 343 ? 7.925   -11.845 3.880  1.00 31.45 ? 343  ASP A OD2 1 
ATOM   2733 N N   . PHE A 1 344 ? 7.633   -6.271  4.804  1.00 22.37 ? 344  PHE A N   1 
ATOM   2734 C CA  . PHE A 1 344 ? 6.981   -5.116  5.435  1.00 22.53 ? 344  PHE A CA  1 
ATOM   2735 C C   . PHE A 1 344 ? 7.606   -3.799  4.969  1.00 21.91 ? 344  PHE A C   1 
ATOM   2736 O O   . PHE A 1 344 ? 7.691   -2.830  5.710  1.00 21.47 ? 344  PHE A O   1 
ATOM   2737 C CB  . PHE A 1 344 ? 6.928   -5.261  6.961  1.00 21.90 ? 344  PHE A CB  1 
ATOM   2738 C CG  . PHE A 1 344 ? 5.827   -6.189  7.433  1.00 22.45 ? 344  PHE A CG  1 
ATOM   2739 C CD1 . PHE A 1 344 ? 5.943   -7.575  7.279  1.00 22.41 ? 344  PHE A CD1 1 
ATOM   2740 C CD2 . PHE A 1 344 ? 4.635   -5.668  7.972  1.00 22.59 ? 344  PHE A CD2 1 
ATOM   2741 C CE1 . PHE A 1 344 ? 4.891   -8.441  7.680  1.00 20.70 ? 344  PHE A CE1 1 
ATOM   2742 C CE2 . PHE A 1 344 ? 3.593   -6.518  8.376  1.00 20.85 ? 344  PHE A CE2 1 
ATOM   2743 C CZ  . PHE A 1 344 ? 3.713   -7.891  8.231  1.00 23.45 ? 344  PHE A CZ  1 
ATOM   2744 N N   . LYS A 1 345 ? 8.030   -3.774  3.708  1.00 23.34 ? 345  LYS A N   1 
ATOM   2745 C CA  . LYS A 1 345 ? 8.556   -2.540  3.098  1.00 24.20 ? 345  LYS A CA  1 
ATOM   2746 C C   . LYS A 1 345 ? 7.406   -1.536  3.054  1.00 23.59 ? 345  LYS A C   1 
ATOM   2747 O O   . LYS A 1 345 ? 6.289   -1.862  2.636  1.00 24.08 ? 345  LYS A O   1 
ATOM   2748 C CB  . LYS A 1 345 ? 9.069   -2.825  1.682  1.00 23.89 ? 345  LYS A CB  1 
ATOM   2749 C CG  . LYS A 1 345 ? 9.672   -1.595  0.955  1.00 27.57 ? 345  LYS A CG  1 
ATOM   2750 C CD  . LYS A 1 345 ? 9.903   -1.900  -0.548 1.00 26.50 ? 345  LYS A CD  1 
ATOM   2751 C CE  . LYS A 1 345 ? 10.156  -0.615  -1.336 1.00 33.74 ? 345  LYS A CE  1 
ATOM   2752 N NZ  . LYS A 1 345 ? 10.465  -0.887  -2.779 1.00 35.99 ? 345  LYS A NZ  1 
ATOM   2753 N N   . GLY A 1 346 ? 7.666   -0.323  3.494  1.00 24.00 ? 346  GLY A N   1 
ATOM   2754 C CA  . GLY A 1 346 ? 6.604   0.684   3.560  1.00 24.76 ? 346  GLY A CA  1 
ATOM   2755 C C   . GLY A 1 346 ? 5.761   0.624   4.824  1.00 25.25 ? 346  GLY A C   1 
ATOM   2756 O O   . GLY A 1 346 ? 4.662   1.222   4.889  1.00 25.17 ? 346  GLY A O   1 
ATOM   2757 N N   . PHE A 1 347 ? 6.264   -0.088  5.834  1.00 24.34 ? 347  PHE A N   1 
ATOM   2758 C CA  . PHE A 1 347 ? 5.624   -0.125  7.169  1.00 24.33 ? 347  PHE A CA  1 
ATOM   2759 C C   . PHE A 1 347 ? 5.327   1.296   7.708  1.00 23.81 ? 347  PHE A C   1 
ATOM   2760 O O   . PHE A 1 347 ? 4.189   1.541   8.134  1.00 23.01 ? 347  PHE A O   1 
ATOM   2761 C CB  . PHE A 1 347 ? 6.421   -1.010  8.157  1.00 24.60 ? 347  PHE A CB  1 
ATOM   2762 C CG  . PHE A 1 347 ? 5.617   -1.573  9.315  1.00 25.58 ? 347  PHE A CG  1 
ATOM   2763 C CD1 . PHE A 1 347 ? 4.229   -1.757  9.235  1.00 25.46 ? 347  PHE A CD1 1 
ATOM   2764 C CD2 . PHE A 1 347 ? 6.271   -1.978  10.470 1.00 25.31 ? 347  PHE A CD2 1 
ATOM   2765 C CE1 . PHE A 1 347 ? 3.519   -2.305  10.318 1.00 25.26 ? 347  PHE A CE1 1 
ATOM   2766 C CE2 . PHE A 1 347 ? 5.575   -2.508  11.559 1.00 26.56 ? 347  PHE A CE2 1 
ATOM   2767 C CZ  . PHE A 1 347 ? 4.194   -2.665  11.484 1.00 23.92 ? 347  PHE A CZ  1 
ATOM   2768 N N   . PRO A 1 348 ? 6.317   2.242   7.674  1.00 23.28 ? 348  PRO A N   1 
ATOM   2769 C CA  . PRO A 1 348 ? 6.000   3.590   8.144  1.00 22.85 ? 348  PRO A CA  1 
ATOM   2770 C C   . PRO A 1 348 ? 4.871   4.276   7.383  1.00 21.92 ? 348  PRO A C   1 
ATOM   2771 O O   . PRO A 1 348 ? 4.105   5.011   8.004  1.00 21.69 ? 348  PRO A O   1 
ATOM   2772 C CB  . PRO A 1 348 ? 7.326   4.344   7.975  1.00 23.28 ? 348  PRO A CB  1 
ATOM   2773 C CG  . PRO A 1 348 ? 8.367   3.228   8.087  1.00 23.63 ? 348  PRO A CG  1 
ATOM   2774 C CD  . PRO A 1 348 ? 7.748   2.140   7.304  1.00 23.33 ? 348  PRO A CD  1 
ATOM   2775 N N   . GLU A 1 349 ? 4.748   4.026   6.081  1.00 20.89 ? 349  GLU A N   1 
ATOM   2776 C CA  . GLU A 1 349 ? 3.652   4.621   5.300  1.00 22.90 ? 349  GLU A CA  1 
ATOM   2777 C C   . GLU A 1 349 ? 2.295   4.038   5.739  1.00 22.39 ? 349  GLU A C   1 
ATOM   2778 O O   . GLU A 1 349 ? 1.269   4.724   5.748  1.00 20.60 ? 349  GLU A O   1 
ATOM   2779 C CB  . GLU A 1 349 ? 3.861   4.411   3.800  1.00 22.89 ? 349  GLU A CB  1 
ATOM   2780 C CG  . GLU A 1 349 ? 5.201   5.016   3.264  1.00 26.00 ? 349  GLU A CG  1 
ATOM   2781 C CD  . GLU A 1 349 ? 5.762   4.319   2.014  1.00 27.12 ? 349  GLU A CD  1 
ATOM   2782 O OE1 . GLU A 1 349 ? 4.980   3.974   1.109  1.00 33.60 ? 349  GLU A OE1 1 
ATOM   2783 O OE2 . GLU A 1 349 ? 7.004   4.156   1.918  1.00 30.98 ? 349  GLU A OE2 1 
ATOM   2784 N N   . PHE A 1 350 ? 2.306   2.759   6.076  1.00 22.12 ? 350  PHE A N   1 
ATOM   2785 C CA  . PHE A 1 350 ? 1.072   2.052   6.503  1.00 21.05 ? 350  PHE A CA  1 
ATOM   2786 C C   . PHE A 1 350 ? 0.587   2.573   7.847  1.00 20.83 ? 350  PHE A C   1 
ATOM   2787 O O   . PHE A 1 350 ? -0.640  2.691   8.075  1.00 21.05 ? 350  PHE A O   1 
ATOM   2788 C CB  . PHE A 1 350 ? 1.335   0.551   6.609  1.00 21.65 ? 350  PHE A CB  1 
ATOM   2789 C CG  . PHE A 1 350 ? 0.240   -0.221  7.350  1.00 20.96 ? 350  PHE A CG  1 
ATOM   2790 C CD1 . PHE A 1 350 ? -0.961  -0.509  6.731  1.00 24.97 ? 350  PHE A CD1 1 
ATOM   2791 C CD2 . PHE A 1 350 ? 0.461   -0.680  8.652  1.00 22.10 ? 350  PHE A CD2 1 
ATOM   2792 C CE1 . PHE A 1 350 ? -1.959  -1.229  7.397  1.00 23.15 ? 350  PHE A CE1 1 
ATOM   2793 C CE2 . PHE A 1 350 ? -0.516  -1.430  9.328  1.00 21.19 ? 350  PHE A CE2 1 
ATOM   2794 C CZ  . PHE A 1 350 ? -1.736  -1.680  8.697  1.00 21.95 ? 350  PHE A CZ  1 
ATOM   2795 N N   . VAL A 1 351 ? 1.535   2.858   8.732  1.00 20.03 ? 351  VAL A N   1 
ATOM   2796 C CA  . VAL A 1 351 ? 1.247   3.472   10.035 1.00 20.47 ? 351  VAL A CA  1 
ATOM   2797 C C   . VAL A 1 351 ? 0.564   4.842   9.840  1.00 19.95 ? 351  VAL A C   1 
ATOM   2798 O O   . VAL A 1 351 ? -0.444  5.130   10.504 1.00 17.42 ? 351  VAL A O   1 
ATOM   2799 C CB  . VAL A 1 351 ? 2.507   3.523   10.943 1.00 21.29 ? 351  VAL A CB  1 
ATOM   2800 C CG1 . VAL A 1 351 ? 2.225   4.232   12.267 1.00 22.97 ? 351  VAL A CG1 1 
ATOM   2801 C CG2 . VAL A 1 351 ? 3.009   2.094   11.213 1.00 22.35 ? 351  VAL A CG2 1 
ATOM   2802 N N   . ASN A 1 352 ? 1.078   5.667   8.916  1.00 19.23 ? 352  ASN A N   1 
ATOM   2803 C CA  . ASN A 1 352 ? 0.388   6.933   8.563  1.00 19.05 ? 352  ASN A CA  1 
ATOM   2804 C C   . ASN A 1 352 ? -1.042  6.710   8.071  1.00 18.38 ? 352  ASN A C   1 
ATOM   2805 O O   . ASN A 1 352 ? -1.944  7.507   8.409  1.00 17.22 ? 352  ASN A O   1 
ATOM   2806 C CB  . ASN A 1 352 ? 1.132   7.694   7.466  1.00 18.65 ? 352  ASN A CB  1 
ATOM   2807 C CG  . ASN A 1 352 ? 2.380   8.354   7.971  1.00 21.93 ? 352  ASN A CG  1 
ATOM   2808 O OD1 . ASN A 1 352 ? 2.684   8.314   9.168  1.00 22.01 ? 352  ASN A OD1 1 
ATOM   2809 N ND2 . ASN A 1 352 ? 3.114   8.992   7.063  1.00 23.63 ? 352  ASN A ND2 1 
ATOM   2810 N N   . GLU A 1 353 ? -1.225  5.698   7.229  1.00 18.81 ? 353  GLU A N   1 
ATOM   2811 C CA  . GLU A 1 353 ? -2.592  5.326   6.737  1.00 20.81 ? 353  GLU A CA  1 
ATOM   2812 C C   . GLU A 1 353 ? -3.536  4.987   7.883  1.00 20.21 ? 353  GLU A C   1 
ATOM   2813 O O   . GLU A 1 353 ? -4.693  5.411   7.875  1.00 19.66 ? 353  GLU A O   1 
ATOM   2814 C CB  . GLU A 1 353 ? -2.558  4.146   5.750  1.00 21.03 ? 353  GLU A CB  1 
ATOM   2815 C CG  . GLU A 1 353 ? -1.925  4.501   4.410  1.00 23.96 ? 353  GLU A CG  1 
ATOM   2816 C CD  . GLU A 1 353 ? -1.535  3.311   3.557  1.00 26.00 ? 353  GLU A CD  1 
ATOM   2817 O OE1 . GLU A 1 353 ? -1.544  2.145   4.041  1.00 30.02 ? 353  GLU A OE1 1 
ATOM   2818 O OE2 . GLU A 1 353 ? -1.151  3.580   2.389  1.00 31.89 ? 353  GLU A OE2 1 
ATOM   2819 N N   . LEU A 1 354 ? -3.067  4.174   8.832  1.00 19.42 ? 354  LEU A N   1 
ATOM   2820 C CA  . LEU A 1 354 ? -3.899  3.813   9.998  1.00 18.64 ? 354  LEU A CA  1 
ATOM   2821 C C   . LEU A 1 354 ? -4.250  5.100   10.718 1.00 18.64 ? 354  LEU A C   1 
ATOM   2822 O O   . LEU A 1 354 ? -5.412  5.342   11.023 1.00 16.77 ? 354  LEU A O   1 
ATOM   2823 C CB  . LEU A 1 354 ? -3.148  2.874   10.980 1.00 18.61 ? 354  LEU A CB  1 
ATOM   2824 C CG  . LEU A 1 354 ? -2.981  1.401   10.607 1.00 17.95 ? 354  LEU A CG  1 
ATOM   2825 C CD1 . LEU A 1 354 ? -2.103  0.742   11.700 1.00 17.68 ? 354  LEU A CD1 1 
ATOM   2826 C CD2 . LEU A 1 354 ? -4.295  0.646   10.443 1.00 19.83 ? 354  LEU A CD2 1 
ATOM   2827 N N   . HIS A 1 355 ? -3.236  5.942   10.962 1.00 17.97 ? 355  HIS A N   1 
ATOM   2828 C CA  . HIS A 1 355 ? -3.440  7.152   11.746 1.00 18.86 ? 355  HIS A CA  1 
ATOM   2829 C C   . HIS A 1 355 ? -4.406  8.109   11.056 1.00 19.29 ? 355  HIS A C   1 
ATOM   2830 O O   . HIS A 1 355 ? -5.317  8.671   11.711 1.00 17.31 ? 355  HIS A O   1 
ATOM   2831 C CB  . HIS A 1 355 ? -2.098  7.816   12.072 1.00 19.56 ? 355  HIS A CB  1 
ATOM   2832 C CG  . HIS A 1 355 ? -1.322  7.070   13.112 1.00 20.74 ? 355  HIS A CG  1 
ATOM   2833 N ND1 . HIS A 1 355 ? -0.002  7.324   13.393 1.00 19.50 ? 355  HIS A ND1 1 
ATOM   2834 C CD2 . HIS A 1 355 ? -1.698  6.057   13.934 1.00 20.39 ? 355  HIS A CD2 1 
ATOM   2835 C CE1 . HIS A 1 355 ? 0.404   6.512   14.358 1.00 19.47 ? 355  HIS A CE1 1 
ATOM   2836 N NE2 . HIS A 1 355 ? -0.599  5.714   14.683 1.00 20.95 ? 355  HIS A NE2 1 
ATOM   2837 N N   . ASN A 1 356 ? -4.225  8.264   9.741  1.00 18.56 ? 356  ASN A N   1 
ATOM   2838 C CA  . ASN A 1 356 ? -5.149  9.088   8.944  1.00 20.10 ? 356  ASN A CA  1 
ATOM   2839 C C   . ASN A 1 356 ? -6.583  8.576   8.968  1.00 20.97 ? 356  ASN A C   1 
ATOM   2840 O O   . ASN A 1 356 ? -7.520  9.351   8.742  1.00 21.19 ? 356  ASN A O   1 
ATOM   2841 C CB  . ASN A 1 356 ? -4.703  9.147   7.479  1.00 20.99 ? 356  ASN A CB  1 
ATOM   2842 C CG  . ASN A 1 356 ? -5.414  10.233  6.707  1.00 21.54 ? 356  ASN A CG  1 
ATOM   2843 O OD1 . ASN A 1 356 ? -5.587  11.324  7.214  1.00 24.85 ? 356  ASN A OD1 1 
ATOM   2844 N ND2 . ASN A 1 356 ? -5.806  9.943   5.467  1.00 23.90 ? 356  ASN A ND2 1 
ATOM   2845 N N   . ASN A 1 357 ? -6.750  7.272   9.172  1.00 20.06 ? 357  ASN A N   1 
ATOM   2846 C CA  . ASN A 1 357 ? -8.089  6.655   9.231  1.00 21.47 ? 357  ASN A CA  1 
ATOM   2847 C C   . ASN A 1 357 ? -8.674  6.640   10.650 1.00 20.90 ? 357  ASN A C   1 
ATOM   2848 O O   . ASN A 1 357 ? -9.779  6.082   10.907 1.00 20.48 ? 357  ASN A O   1 
ATOM   2849 C CB  . ASN A 1 357 ? -8.042  5.246   8.619  1.00 22.52 ? 357  ASN A CB  1 
ATOM   2850 C CG  . ASN A 1 357 ? -7.742  5.261   7.099  1.00 26.11 ? 357  ASN A CG  1 
ATOM   2851 O OD1 . ASN A 1 357 ? -7.094  4.370   6.598  1.00 30.47 ? 357  ASN A OD1 1 
ATOM   2852 N ND2 . ASN A 1 357 ? -8.261  6.247   6.378  1.00 32.44 ? 357  ASN A ND2 1 
ATOM   2853 N N   . GLY A 1 358 ? -7.937  7.269   11.559 1.00 18.86 ? 358  GLY A N   1 
ATOM   2854 C CA  . GLY A 1 358 ? -8.300  7.375   12.970 1.00 19.18 ? 358  GLY A CA  1 
ATOM   2855 C C   . GLY A 1 358 ? -8.114  6.077   13.740 1.00 18.66 ? 358  GLY A C   1 
ATOM   2856 O O   . GLY A 1 358 ? -8.753  5.869   14.772 1.00 19.32 ? 358  GLY A O   1 
ATOM   2857 N N   . GLN A 1 359 ? -7.217  5.217   13.248 1.00 17.76 ? 359  GLN A N   1 
ATOM   2858 C CA  . GLN A 1 359 ? -6.895  3.963   13.916 1.00 16.19 ? 359  GLN A CA  1 
ATOM   2859 C C   . GLN A 1 359 ? -5.521  3.976   14.601 1.00 16.78 ? 359  GLN A C   1 
ATOM   2860 O O   . GLN A 1 359 ? -4.741  4.949   14.491 1.00 16.19 ? 359  GLN A O   1 
ATOM   2861 C CB  . GLN A 1 359 ? -6.974  2.818   12.922 1.00 16.95 ? 359  GLN A CB  1 
ATOM   2862 C CG  . GLN A 1 359 ? -8.355  2.625   12.315 1.00 18.15 ? 359  GLN A CG  1 
ATOM   2863 C CD  . GLN A 1 359 ? -8.291  1.653   11.207 1.00 20.01 ? 359  GLN A CD  1 
ATOM   2864 O OE1 . GLN A 1 359 ? -7.613  1.887   10.190 1.00 21.95 ? 359  GLN A OE1 1 
ATOM   2865 N NE2 . GLN A 1 359 ? -8.940  0.505   11.396 1.00 18.66 ? 359  GLN A NE2 1 
ATOM   2866 N N   . LYS A 1 360 ? -5.249  2.905   15.345 1.00 15.71 ? 360  LYS A N   1 
ATOM   2867 C CA  . LYS A 1 360 ? -4.065  2.817   16.175 1.00 15.48 ? 360  LYS A CA  1 
ATOM   2868 C C   . LYS A 1 360 ? -3.311  1.550   15.819 1.00 15.30 ? 360  LYS A C   1 
ATOM   2869 O O   . LYS A 1 360 ? -3.906  0.562   15.412 1.00 15.26 ? 360  LYS A O   1 
ATOM   2870 C CB  . LYS A 1 360 ? -4.438  2.811   17.664 1.00 16.54 ? 360  LYS A CB  1 
ATOM   2871 C CG  . LYS A 1 360 ? -5.312  4.051   18.095 1.00 18.54 ? 360  LYS A CG  1 
ATOM   2872 C CD  . LYS A 1 360 ? -4.456  5.338   18.109 1.00 19.70 ? 360  LYS A CD  1 
ATOM   2873 C CE  . LYS A 1 360 ? -5.273  6.557   18.521 1.00 22.12 ? 360  LYS A CE  1 
ATOM   2874 N NZ  . LYS A 1 360 ? -4.448  7.800   18.767 1.00 26.17 ? 360  LYS A NZ  1 
ATOM   2875 N N   . LEU A 1 361 ? -1.998  1.580   16.011 1.00 15.74 ? 361  LEU A N   1 
ATOM   2876 C CA  . LEU A 1 361 ? -1.183  0.393   15.770 1.00 16.00 ? 361  LEU A CA  1 
ATOM   2877 C C   . LEU A 1 361 ? -0.670  -0.087  17.107 1.00 15.07 ? 361  LEU A C   1 
ATOM   2878 O O   . LEU A 1 361 ? -0.101  0.681   17.855 1.00 16.11 ? 361  LEU A O   1 
ATOM   2879 C CB  . LEU A 1 361 ? 0.020   0.714   14.844 1.00 16.47 ? 361  LEU A CB  1 
ATOM   2880 C CG  . LEU A 1 361 ? 1.035   -0.443  14.726 1.00 16.67 ? 361  LEU A CG  1 
ATOM   2881 C CD1 . LEU A 1 361 ? 0.417   -1.602  13.965 1.00 18.16 ? 361  LEU A CD1 1 
ATOM   2882 C CD2 . LEU A 1 361 ? 2.333   0.057   14.047 1.00 17.20 ? 361  LEU A CD2 1 
ATOM   2883 N N   . VAL A 1 362 ? -0.821  -1.376  17.378 1.00 15.47 ? 362  VAL A N   1 
ATOM   2884 C CA  . VAL A 1 362 ? -0.252  -1.975  18.562 1.00 14.85 ? 362  VAL A CA  1 
ATOM   2885 C C   . VAL A 1 362 ? 0.731   -3.022  18.035 1.00 14.20 ? 362  VAL A C   1 
ATOM   2886 O O   . VAL A 1 362 ? 0.354   -3.858  17.231 1.00 14.49 ? 362  VAL A O   1 
ATOM   2887 C CB  . VAL A 1 362 ? -1.318  -2.639  19.468 1.00 15.72 ? 362  VAL A CB  1 
ATOM   2888 C CG1 . VAL A 1 362 ? -0.614  -3.581  20.499 1.00 15.72 ? 362  VAL A CG1 1 
ATOM   2889 C CG2 . VAL A 1 362 ? -2.105  -1.558  20.206 1.00 13.54 ? 362  VAL A CG2 1 
ATOM   2890 N N   . ILE A 1 363 ? 1.970   -2.952  18.485 1.00 14.61 ? 363  ILE A N   1 
ATOM   2891 C CA  . ILE A 1 363 ? 3.001   -3.926  18.082 1.00 16.39 ? 363  ILE A CA  1 
ATOM   2892 C C   . ILE A 1 363 ? 3.328   -4.917  19.187 1.00 15.14 ? 363  ILE A C   1 
ATOM   2893 O O   . ILE A 1 363 ? 3.384   -4.551  20.339 1.00 16.28 ? 363  ILE A O   1 
ATOM   2894 C CB  . ILE A 1 363 ? 4.343   -3.202  17.630 1.00 16.65 ? 363  ILE A CB  1 
ATOM   2895 C CG1 . ILE A 1 363 ? 4.900   -2.270  18.717 1.00 18.26 ? 363  ILE A CG1 1 
ATOM   2896 C CG2 . ILE A 1 363 ? 4.122   -2.522  16.273 1.00 18.32 ? 363  ILE A CG2 1 
ATOM   2897 C CD1 . ILE A 1 363 ? 6.476   -1.958  18.569 1.00 18.71 ? 363  ILE A CD1 1 
ATOM   2898 N N   . ILE A 1 364 ? 3.582   -6.173  18.815 1.00 15.80 ? 364  ILE A N   1 
ATOM   2899 C CA  . ILE A 1 364 ? 4.034   -7.174  19.756 1.00 15.24 ? 364  ILE A CA  1 
ATOM   2900 C C   . ILE A 1 364 ? 5.517   -6.918  19.951 1.00 16.89 ? 364  ILE A C   1 
ATOM   2901 O O   . ILE A 1 364 ? 6.195   -6.583  18.976 1.00 15.67 ? 364  ILE A O   1 
ATOM   2902 C CB  . ILE A 1 364 ? 3.771   -8.622  19.247 1.00 15.39 ? 364  ILE A CB  1 
ATOM   2903 C CG1 . ILE A 1 364 ? 3.893   -9.638  20.402 1.00 15.87 ? 364  ILE A CG1 1 
ATOM   2904 C CG2 . ILE A 1 364 ? 4.730   -9.041  18.082 1.00 15.85 ? 364  ILE A CG2 1 
ATOM   2905 C CD1 . ILE A 1 364 ? 3.234   -10.992 20.088 1.00 16.13 ? 364  ILE A CD1 1 
ATOM   2906 N N   . VAL A 1 365 ? 5.968   -7.070  21.199 1.00 16.50 ? 365  VAL A N   1 
ATOM   2907 C CA  . VAL A 1 365 ? 7.367   -7.031  21.581 1.00 18.69 ? 365  VAL A CA  1 
ATOM   2908 C C   . VAL A 1 365 ? 7.531   -8.257  22.524 1.00 19.45 ? 365  VAL A C   1 
ATOM   2909 O O   . VAL A 1 365 ? 6.680   -8.532  23.388 1.00 19.91 ? 365  VAL A O   1 
ATOM   2910 C CB  . VAL A 1 365 ? 7.772   -5.667  22.256 1.00 18.54 ? 365  VAL A CB  1 
ATOM   2911 C CG1 . VAL A 1 365 ? 9.303   -5.554  22.411 1.00 20.76 ? 365  VAL A CG1 1 
ATOM   2912 C CG2 . VAL A 1 365 ? 7.283   -4.461  21.453 1.00 19.07 ? 365  VAL A CG2 1 
ATOM   2913 N N   . ASP A 1 366 ? 8.583   -9.036  22.292 1.00 19.30 ? 366  ASP A N   1 
ATOM   2914 C CA  . ASP A 1 366 ? 8.867   -10.226 23.092 1.00 19.63 ? 366  ASP A CA  1 
ATOM   2915 C C   . ASP A 1 366 ? 9.991   -9.839  24.041 1.00 19.23 ? 366  ASP A C   1 
ATOM   2916 O O   . ASP A 1 366 ? 10.718  -8.896  23.750 1.00 18.44 ? 366  ASP A O   1 
ATOM   2917 C CB  . ASP A 1 366 ? 9.304   -11.391 22.179 1.00 19.61 ? 366  ASP A CB  1 
ATOM   2918 C CG  . ASP A 1 366 ? 8.178   -11.894 21.292 1.00 23.82 ? 366  ASP A CG  1 
ATOM   2919 O OD1 . ASP A 1 366 ? 7.085   -12.208 21.832 1.00 21.52 ? 366  ASP A OD1 1 
ATOM   2920 O OD2 . ASP A 1 366 ? 8.398   -11.992 20.059 1.00 23.02 ? 366  ASP A OD2 1 
ATOM   2921 N N   . PRO A 1 367 ? 10.089  -10.487 25.210 1.00 18.67 ? 367  PRO A N   1 
ATOM   2922 C CA  . PRO A 1 367 ? 11.209  -10.092 26.039 1.00 19.01 ? 367  PRO A CA  1 
ATOM   2923 C C   . PRO A 1 367 ? 12.547  -10.600 25.474 1.00 19.14 ? 367  PRO A C   1 
ATOM   2924 O O   . PRO A 1 367 ? 13.530  -9.883  25.535 1.00 20.12 ? 367  PRO A O   1 
ATOM   2925 C CB  . PRO A 1 367 ? 10.926  -10.784 27.377 1.00 18.54 ? 367  PRO A CB  1 
ATOM   2926 C CG  . PRO A 1 367 ? 10.052  -11.926 27.032 1.00 19.56 ? 367  PRO A CG  1 
ATOM   2927 C CD  . PRO A 1 367 ? 9.217   -11.468 25.884 1.00 19.06 ? 367  PRO A CD  1 
ATOM   2928 N N   . ALA A 1 368 ? 12.554  -11.789 24.887 1.00 18.89 ? 368  ALA A N   1 
ATOM   2929 C CA  . ALA A 1 368 ? 13.849  -12.432 24.600 1.00 19.44 ? 368  ALA A CA  1 
ATOM   2930 C C   . ALA A 1 368 ? 14.514  -11.732 23.435 1.00 18.78 ? 368  ALA A C   1 
ATOM   2931 O O   . ALA A 1 368 ? 13.846  -11.378 22.467 1.00 19.88 ? 368  ALA A O   1 
ATOM   2932 C CB  . ALA A 1 368 ? 13.670  -13.889 24.334 1.00 19.31 ? 368  ALA A CB  1 
ATOM   2933 N N   . ILE A 1 369 ? 15.838  -11.558 23.517 1.00 18.48 ? 369  ILE A N   1 
ATOM   2934 C CA  . ILE A 1 369 ? 16.579  -10.766 22.556 1.00 17.37 ? 369  ILE A CA  1 
ATOM   2935 C C   . ILE A 1 369 ? 17.628  -11.676 21.888 1.00 18.18 ? 369  ILE A C   1 
ATOM   2936 O O   . ILE A 1 369 ? 18.376  -12.348 22.593 1.00 17.28 ? 369  ILE A O   1 
ATOM   2937 C CB  . ILE A 1 369 ? 17.311  -9.563  23.237 1.00 17.75 ? 369  ILE A CB  1 
ATOM   2938 C CG1 . ILE A 1 369 ? 16.323  -8.596  23.917 1.00 17.08 ? 369  ILE A CG1 1 
ATOM   2939 C CG2 . ILE A 1 369 ? 18.205  -8.798  22.215 1.00 19.16 ? 369  ILE A CG2 1 
ATOM   2940 C CD1 . ILE A 1 369 ? 15.301  -7.988  22.945 1.00 18.05 ? 369  ILE A CD1 1 
ATOM   2941 N N   . SER A 1 370 ? 17.655  -11.663 20.553 1.00 18.94 ? 370  SER A N   1 
ATOM   2942 C CA  . SER A 1 370 ? 18.575  -12.483 19.763 1.00 20.66 ? 370  SER A CA  1 
ATOM   2943 C C   . SER A 1 370 ? 19.985  -12.161 20.209 1.00 20.58 ? 370  SER A C   1 
ATOM   2944 O O   . SER A 1 370 ? 20.298  -11.006 20.371 1.00 20.40 ? 370  SER A O   1 
ATOM   2945 C CB  . SER A 1 370 ? 18.454  -12.140 18.279 1.00 20.52 ? 370  SER A CB  1 
ATOM   2946 O OG  . SER A 1 370 ? 19.348  -12.950 17.517 1.00 21.49 ? 370  SER A OG  1 
ATOM   2947 N N   . ASN A 1 371 ? 20.821  -13.171 20.431 1.00 21.72 ? 371  ASN A N   1 
ATOM   2948 C CA  . ASN A 1 371 ? 22.226  -12.870 20.799 1.00 23.19 ? 371  ASN A CA  1 
ATOM   2949 C C   . ASN A 1 371 ? 23.143  -12.954 19.587 1.00 24.95 ? 371  ASN A C   1 
ATOM   2950 O O   . ASN A 1 371 ? 24.370  -12.992 19.735 1.00 25.28 ? 371  ASN A O   1 
ATOM   2951 C CB  . ASN A 1 371 ? 22.736  -13.791 21.929 1.00 22.70 ? 371  ASN A CB  1 
ATOM   2952 C CG  . ASN A 1 371 ? 22.782  -15.266 21.533 1.00 24.02 ? 371  ASN A CG  1 
ATOM   2953 O OD1 . ASN A 1 371 ? 22.294  -15.660 20.491 1.00 24.49 ? 371  ASN A OD1 1 
ATOM   2954 N ND2 . ASN A 1 371 ? 23.360  -16.089 22.404 1.00 24.40 ? 371  ASN A ND2 1 
ATOM   2955 N N   . ASN A 1 372 ? 22.545  -12.974 18.408 1.00 25.30 ? 372  ASN A N   1 
ATOM   2956 C CA  . ASN A 1 372 ? 23.312  -13.109 17.172 1.00 27.31 ? 372  ASN A CA  1 
ATOM   2957 C C   . ASN A 1 372 ? 23.690  -11.725 16.673 1.00 27.34 ? 372  ASN A C   1 
ATOM   2958 O O   . ASN A 1 372 ? 22.905  -11.050 16.022 1.00 26.79 ? 372  ASN A O   1 
ATOM   2959 C CB  . ASN A 1 372 ? 22.513  -13.879 16.134 1.00 27.81 ? 372  ASN A CB  1 
ATOM   2960 C CG  . ASN A 1 372 ? 23.380  -14.386 14.976 1.00 30.09 ? 372  ASN A CG  1 
ATOM   2961 O OD1 . ASN A 1 372 ? 24.326  -13.727 14.560 1.00 30.92 ? 372  ASN A OD1 1 
ATOM   2962 N ND2 . ASN A 1 372 ? 23.030  -15.543 14.442 1.00 32.79 ? 372  ASN A ND2 1 
ATOM   2963 N N   . SER A 1 373 ? 24.917  -11.316 16.982 1.00 28.69 ? 373  SER A N   1 
ATOM   2964 C CA  . SER A 1 373 ? 25.418  -10.028 16.580 1.00 29.73 ? 373  SER A CA  1 
ATOM   2965 C C   . SER A 1 373 ? 26.926  -10.119 16.355 1.00 31.71 ? 373  SER A C   1 
ATOM   2966 O O   . SER A 1 373 ? 27.622  -10.788 17.101 1.00 32.32 ? 373  SER A O   1 
ATOM   2967 C CB  . SER A 1 373 ? 25.161  -9.003  17.666 1.00 29.55 ? 373  SER A CB  1 
ATOM   2968 O OG  . SER A 1 373 ? 25.469  -7.703  17.196 1.00 26.81 ? 373  SER A OG  1 
ATOM   2969 N N   . SER A 1 374 ? 27.400  -9.437  15.324 1.00 34.37 ? 374  SER A N   1 
ATOM   2970 C CA  . SER A 1 374 ? 28.836  -9.372  14.993 1.00 36.93 ? 374  SER A CA  1 
ATOM   2971 C C   . SER A 1 374 ? 29.140  -7.976  14.435 1.00 38.41 ? 374  SER A C   1 
ATOM   2972 O O   . SER A 1 374 ? 28.216  -7.209  14.177 1.00 38.36 ? 374  SER A O   1 
ATOM   2973 C CB  . SER A 1 374 ? 29.183  -10.466 13.968 1.00 36.75 ? 374  SER A CB  1 
ATOM   2974 O OG  . SER A 1 374 ? 28.430  -10.322 12.764 1.00 37.40 ? 374  SER A OG  1 
ATOM   2975 N N   . SER A 1 375 ? 30.419  -7.627  14.270 1.00 40.01 ? 375  SER A N   1 
ATOM   2976 C CA  . SER A 1 375 ? 30.782  -6.375  13.578 1.00 41.25 ? 375  SER A CA  1 
ATOM   2977 C C   . SER A 1 375 ? 30.221  -6.332  12.153 1.00 41.66 ? 375  SER A C   1 
ATOM   2978 O O   . SER A 1 375 ? 29.803  -5.280  11.664 1.00 42.62 ? 375  SER A O   1 
ATOM   2979 C CB  . SER A 1 375 ? 32.305  -6.198  13.532 1.00 41.85 ? 375  SER A CB  1 
ATOM   2980 O OG  . SER A 1 375 ? 32.874  -6.232  14.838 1.00 43.50 ? 375  SER A OG  1 
ATOM   2981 N N   . SER A 1 376 ? 30.213  -7.484  11.494 1.00 41.81 ? 376  SER A N   1 
ATOM   2982 C CA  . SER A 1 376 ? 29.660  -7.624  10.154 1.00 41.83 ? 376  SER A CA  1 
ATOM   2983 C C   . SER A 1 376 ? 28.179  -7.200  10.119 1.00 41.25 ? 376  SER A C   1 
ATOM   2984 O O   . SER A 1 376 ? 27.799  -6.288  9.381  1.00 41.36 ? 376  SER A O   1 
ATOM   2985 C CB  . SER A 1 376 ? 29.833  -9.079  9.690  1.00 42.14 ? 376  SER A CB  1 
ATOM   2986 O OG  . SER A 1 376 ? 29.528  -9.240  8.317  1.00 44.36 ? 376  SER A OG  1 
ATOM   2987 N N   . LYS A 1 377 ? 27.351  -7.861  10.929 1.00 39.85 ? 377  LYS A N   1 
ATOM   2988 C CA  . LYS A 1 377 ? 25.931  -7.534  11.016 1.00 38.25 ? 377  LYS A CA  1 
ATOM   2989 C C   . LYS A 1 377 ? 25.565  -7.262  12.487 1.00 35.85 ? 377  LYS A C   1 
ATOM   2990 O O   . LYS A 1 377 ? 25.205  -8.197  13.209 1.00 35.40 ? 377  LYS A O   1 
ATOM   2991 C CB  . LYS A 1 377 ? 25.106  -8.710  10.493 1.00 39.30 ? 377  LYS A CB  1 
ATOM   2992 C CG  . LYS A 1 377 ? 24.057  -8.326  9.458  1.00 42.42 ? 377  LYS A CG  1 
ATOM   2993 C CD  . LYS A 1 377 ? 24.622  -8.388  8.036  1.00 45.82 ? 377  LYS A CD  1 
ATOM   2994 C CE  . LYS A 1 377 ? 23.615  -7.820  7.024  1.00 46.84 ? 377  LYS A CE  1 
ATOM   2995 N NZ  . LYS A 1 377 ? 24.081  -8.023  5.628  1.00 47.26 ? 377  LYS A NZ  1 
ATOM   2996 N N   . PRO A 1 378 ? 25.697  -6.004  12.946 1.00 33.74 ? 378  PRO A N   1 
ATOM   2997 C CA  . PRO A 1 378 ? 25.363  -5.753  14.351 1.00 31.78 ? 378  PRO A CA  1 
ATOM   2998 C C   . PRO A 1 378 ? 23.862  -5.910  14.602 1.00 29.23 ? 378  PRO A C   1 
ATOM   2999 O O   . PRO A 1 378 ? 23.060  -5.579  13.725 1.00 30.15 ? 378  PRO A O   1 
ATOM   3000 C CB  . PRO A 1 378 ? 25.759  -4.293  14.567 1.00 31.88 ? 378  PRO A CB  1 
ATOM   3001 C CG  . PRO A 1 378 ? 25.841  -3.693  13.214 1.00 33.14 ? 378  PRO A CG  1 
ATOM   3002 C CD  . PRO A 1 378 ? 26.160  -4.785  12.255 1.00 33.31 ? 378  PRO A CD  1 
ATOM   3003 N N   . TYR A 1 379 ? 23.498  -6.401  15.783 1.00 26.18 ? 379  TYR A N   1 
ATOM   3004 C CA  . TYR A 1 379 ? 22.076  -6.352  16.201 1.00 23.46 ? 379  TYR A CA  1 
ATOM   3005 C C   . TYR A 1 379 ? 21.990  -5.434  17.401 1.00 21.56 ? 379  TYR A C   1 
ATOM   3006 O O   . TYR A 1 379 ? 22.312  -5.831  18.516 1.00 21.78 ? 379  TYR A O   1 
ATOM   3007 C CB  . TYR A 1 379 ? 21.503  -7.751  16.499 1.00 21.71 ? 379  TYR A CB  1 
ATOM   3008 C CG  . TYR A 1 379 ? 20.039  -7.689  16.967 1.00 20.66 ? 379  TYR A CG  1 
ATOM   3009 C CD1 . TYR A 1 379 ? 19.065  -7.056  16.199 1.00 18.84 ? 379  TYR A CD1 1 
ATOM   3010 C CD2 . TYR A 1 379 ? 19.663  -8.240  18.182 1.00 21.73 ? 379  TYR A CD2 1 
ATOM   3011 C CE1 . TYR A 1 379 ? 17.678  -7.003  16.657 1.00 20.04 ? 379  TYR A CE1 1 
ATOM   3012 C CE2 . TYR A 1 379 ? 18.330  -8.186  18.639 1.00 18.90 ? 379  TYR A CE2 1 
ATOM   3013 C CZ  . TYR A 1 379 ? 17.353  -7.577  17.883 1.00 20.82 ? 379  TYR A CZ  1 
ATOM   3014 O OH  . TYR A 1 379 ? 16.042  -7.570  18.411 1.00 19.72 ? 379  TYR A OH  1 
ATOM   3015 N N   . GLY A 1 380 ? 21.577  -4.191  17.145 1.00 21.06 ? 380  GLY A N   1 
ATOM   3016 C CA  . GLY A 1 380 ? 21.572  -3.103  18.122 1.00 20.89 ? 380  GLY A CA  1 
ATOM   3017 C C   . GLY A 1 380 ? 21.058  -3.374  19.532 1.00 20.53 ? 380  GLY A C   1 
ATOM   3018 O O   . GLY A 1 380 ? 21.747  -3.084  20.497 1.00 19.06 ? 380  GLY A O   1 
ATOM   3019 N N   . PRO A 1 381 ? 19.817  -3.913  19.667 1.00 20.37 ? 381  PRO A N   1 
ATOM   3020 C CA  . PRO A 1 381 ? 19.234  -4.178  21.006 1.00 19.52 ? 381  PRO A CA  1 
ATOM   3021 C C   . PRO A 1 381 ? 20.091  -5.108  21.879 1.00 19.29 ? 381  PRO A C   1 
ATOM   3022 O O   . PRO A 1 381 ? 20.202  -4.900  23.081 1.00 19.69 ? 381  PRO A O   1 
ATOM   3023 C CB  . PRO A 1 381 ? 17.872  -4.830  20.666 1.00 19.27 ? 381  PRO A CB  1 
ATOM   3024 C CG  . PRO A 1 381 ? 17.512  -4.204  19.349 1.00 18.79 ? 381  PRO A CG  1 
ATOM   3025 C CD  . PRO A 1 381 ? 18.864  -4.244  18.595 1.00 19.87 ? 381  PRO A CD  1 
ATOM   3026 N N   . TYR A 1 382 ? 20.704  -6.108  21.264 1.00 20.41 ? 382  TYR A N   1 
ATOM   3027 C CA  . TYR A 1 382 ? 21.601  -7.020  21.973 1.00 20.71 ? 382  TYR A CA  1 
ATOM   3028 C C   . TYR A 1 382 ? 22.914  -6.331  22.363 1.00 21.00 ? 382  TYR A C   1 
ATOM   3029 O O   . TYR A 1 382 ? 23.365  -6.477  23.503 1.00 20.73 ? 382  TYR A O   1 
ATOM   3030 C CB  . TYR A 1 382 ? 21.867  -8.280  21.143 1.00 21.79 ? 382  TYR A CB  1 
ATOM   3031 C CG  . TYR A 1 382 ? 22.862  -9.185  21.795 1.00 22.89 ? 382  TYR A CG  1 
ATOM   3032 C CD1 . TYR A 1 382 ? 22.526  -9.898  22.937 1.00 21.71 ? 382  TYR A CD1 1 
ATOM   3033 C CD2 . TYR A 1 382 ? 24.179  -9.288  21.304 1.00 24.35 ? 382  TYR A CD2 1 
ATOM   3034 C CE1 . TYR A 1 382 ? 23.465  -10.730 23.586 1.00 25.61 ? 382  TYR A CE1 1 
ATOM   3035 C CE2 . TYR A 1 382 ? 25.123  -10.119 21.945 1.00 25.47 ? 382  TYR A CE2 1 
ATOM   3036 C CZ  . TYR A 1 382 ? 24.753  -10.840 23.079 1.00 25.03 ? 382  TYR A CZ  1 
ATOM   3037 O OH  . TYR A 1 382 ? 25.656  -11.669 23.751 1.00 25.66 ? 382  TYR A OH  1 
ATOM   3038 N N   . ASP A 1 383 ? 23.556  -5.634  21.417 1.00 21.41 ? 383  ASP A N   1 
ATOM   3039 C CA  . ASP A 1 383 ? 24.795  -4.880  21.758 1.00 22.63 ? 383  ASP A CA  1 
ATOM   3040 C C   . ASP A 1 383 ? 24.580  -3.887  22.888 1.00 22.68 ? 383  ASP A C   1 
ATOM   3041 O O   . ASP A 1 383 ? 25.354  -3.867  23.848 1.00 22.32 ? 383  ASP A O   1 
ATOM   3042 C CB  . ASP A 1 383 ? 25.363  -4.131  20.540 1.00 22.87 ? 383  ASP A CB  1 
ATOM   3043 C CG  . ASP A 1 383 ? 25.751  -5.050  19.412 1.00 25.55 ? 383  ASP A CG  1 
ATOM   3044 O OD1 . ASP A 1 383 ? 25.822  -6.290  19.610 1.00 25.56 ? 383  ASP A OD1 1 
ATOM   3045 O OD2 . ASP A 1 383 ? 25.983  -4.509  18.300 1.00 31.20 ? 383  ASP A OD2 1 
ATOM   3046 N N   . ARG A 1 384 ? 23.522  -3.066  22.770 1.00 21.73 ? 384  ARG A N   1 
ATOM   3047 C CA  . ARG A 1 384 ? 23.204  -2.079  23.789 1.00 21.98 ? 384  ARG A CA  1 
ATOM   3048 C C   . ARG A 1 384 ? 22.875  -2.711  25.129 1.00 21.75 ? 384  ARG A C   1 
ATOM   3049 O O   . ARG A 1 384 ? 23.309  -2.204  26.162 1.00 21.45 ? 384  ARG A O   1 
ATOM   3050 C CB  . ARG A 1 384 ? 22.090  -1.126  23.322 1.00 22.23 ? 384  ARG A CB  1 
ATOM   3051 C CG  . ARG A 1 384 ? 22.534  -0.125  22.272 1.00 22.51 ? 384  ARG A CG  1 
ATOM   3052 C CD  . ARG A 1 384 ? 21.394  0.860   21.880 1.00 23.00 ? 384  ARG A CD  1 
ATOM   3053 N NE  . ARG A 1 384 ? 20.335  0.216   21.100 1.00 25.03 ? 384  ARG A NE  1 
ATOM   3054 C CZ  . ARG A 1 384 ? 20.339  0.093   19.775 1.00 25.57 ? 384  ARG A CZ  1 
ATOM   3055 N NH1 . ARG A 1 384 ? 21.344  0.587   19.054 1.00 26.39 ? 384  ARG A NH1 1 
ATOM   3056 N NH2 . ARG A 1 384 ? 19.339  -0.517  19.164 1.00 24.81 ? 384  ARG A NH2 1 
ATOM   3057 N N   . GLY A 1 385 ? 22.107  -3.815  25.125 1.00 22.02 ? 385  GLY A N   1 
ATOM   3058 C CA  . GLY A 1 385 ? 21.809  -4.548  26.367 1.00 21.42 ? 385  GLY A CA  1 
ATOM   3059 C C   . GLY A 1 385 ? 23.020  -5.203  27.030 1.00 22.71 ? 385  GLY A C   1 
ATOM   3060 O O   . GLY A 1 385 ? 23.154  -5.199  28.258 1.00 21.02 ? 385  GLY A O   1 
ATOM   3061 N N   . SER A 1 386 ? 23.904  -5.768  26.210 1.00 22.97 ? 386  SER A N   1 
ATOM   3062 C CA  . SER A 1 386 ? 25.146  -6.354  26.726 1.00 25.28 ? 386  SER A CA  1 
ATOM   3063 C C   . SER A 1 386 ? 26.048  -5.266  27.287 1.00 25.39 ? 386  SER A C   1 
ATOM   3064 O O   . SER A 1 386 ? 26.665  -5.472  28.305 1.00 26.47 ? 386  SER A O   1 
ATOM   3065 C CB  . SER A 1 386 ? 25.871  -7.105  25.624 1.00 25.00 ? 386  SER A CB  1 
ATOM   3066 O OG  . SER A 1 386 ? 25.006  -8.070  25.092 1.00 26.16 ? 386  SER A OG  1 
ATOM   3067 N N   . ASP A 1 387 ? 26.088  -4.107  26.627 1.00 27.42 ? 387  ASP A N   1 
ATOM   3068 C CA  . ASP A 1 387 ? 26.862  -2.945  27.124 1.00 28.31 ? 387  ASP A CA  1 
ATOM   3069 C C   . ASP A 1 387 ? 26.437  -2.554  28.546 1.00 28.55 ? 387  ASP A C   1 
ATOM   3070 O O   . ASP A 1 387 ? 27.274  -2.229  29.411 1.00 27.35 ? 387  ASP A O   1 
ATOM   3071 C CB  . ASP A 1 387 ? 26.679  -1.738  26.197 1.00 29.12 ? 387  ASP A CB  1 
ATOM   3072 C CG  . ASP A 1 387 ? 27.493  -1.835  24.914 1.00 32.78 ? 387  ASP A CG  1 
ATOM   3073 O OD1 . ASP A 1 387 ? 28.345  -2.758  24.775 1.00 35.90 ? 387  ASP A OD1 1 
ATOM   3074 O OD2 . ASP A 1 387 ? 27.263  -0.969  24.036 1.00 34.60 ? 387  ASP A OD2 1 
ATOM   3075 N N   . MET A 1 388 ? 25.121  -2.597  28.780 1.00 27.70 ? 388  MET A N   1 
ATOM   3076 C CA  . MET A 1 388 ? 24.532  -2.199  30.042 1.00 28.19 ? 388  MET A CA  1 
ATOM   3077 C C   . MET A 1 388 ? 24.424  -3.339  31.043 1.00 25.70 ? 388  MET A C   1 
ATOM   3078 O O   . MET A 1 388 ? 24.093  -3.122  32.205 1.00 25.24 ? 388  MET A O   1 
ATOM   3079 C CB  . MET A 1 388 ? 23.151  -1.587  29.786 1.00 27.28 ? 388  MET A CB  1 
ATOM   3080 C CG  . MET A 1 388 ? 23.222  -0.287  28.966 1.00 30.67 ? 388  MET A CG  1 
ATOM   3081 S SD  . MET A 1 388 ? 21.607  0.471   28.674 1.00 33.46 ? 388  MET A SD  1 
ATOM   3082 C CE  . MET A 1 388 ? 21.208  0.913   30.359 1.00 30.25 ? 388  MET A CE  1 
ATOM   3083 N N   . LYS A 1 389 ? 24.687  -4.552  30.575 1.00 24.94 ? 389  LYS A N   1 
ATOM   3084 C CA  . LYS A 1 389 ? 24.777  -5.724  31.443 1.00 24.78 ? 389  LYS A CA  1 
ATOM   3085 C C   . LYS A 1 389 ? 23.449  -5.999  32.173 1.00 23.43 ? 389  LYS A C   1 
ATOM   3086 O O   . LYS A 1 389 ? 23.431  -6.269  33.375 1.00 22.69 ? 389  LYS A O   1 
ATOM   3087 C CB  . LYS A 1 389 ? 25.955  -5.579  32.437 1.00 24.80 ? 389  LYS A CB  1 
ATOM   3088 C CG  . LYS A 1 389 ? 27.324  -5.564  31.715 1.00 26.59 ? 389  LYS A CG  1 
ATOM   3089 C CD  . LYS A 1 389 ? 28.454  -5.184  32.647 1.00 27.85 ? 389  LYS A CD  1 
ATOM   3090 C CE  . LYS A 1 389 ? 29.764  -5.148  31.848 1.00 32.53 ? 389  LYS A CE  1 
ATOM   3091 N NZ  . LYS A 1 389 ? 30.127  -6.535  31.357 1.00 35.98 ? 389  LYS A NZ  1 
ATOM   3092 N N   . ILE A 1 390 ? 22.365  -5.976  31.407 1.00 22.53 ? 390  ILE A N   1 
ATOM   3093 C CA  . ILE A 1 390 ? 21.014  -6.055  31.978 1.00 21.53 ? 390  ILE A CA  1 
ATOM   3094 C C   . ILE A 1 390 ? 20.308  -7.386  31.669 1.00 21.24 ? 390  ILE A C   1 
ATOM   3095 O O   . ILE A 1 390 ? 19.093  -7.467  31.760 1.00 20.51 ? 390  ILE A O   1 
ATOM   3096 C CB  . ILE A 1 390 ? 20.136  -4.829  31.576 1.00 21.73 ? 390  ILE A CB  1 
ATOM   3097 C CG1 . ILE A 1 390 ? 20.140  -4.508  30.076 1.00 21.86 ? 390  ILE A CG1 1 
ATOM   3098 C CG2 . ILE A 1 390 ? 20.587  -3.585  32.349 1.00 23.23 ? 390  ILE A CG2 1 
ATOM   3099 C CD1 . ILE A 1 390 ? 19.546  -5.551  29.093 1.00 21.81 ? 390  ILE A CD1 1 
ATOM   3100 N N   . TRP A 1 391 ? 21.078  -8.425  31.315 1.00 20.54 ? 391  TRP A N   1 
ATOM   3101 C CA  . TRP A 1 391 ? 20.484  -9.776  31.101 1.00 19.90 ? 391  TRP A CA  1 
ATOM   3102 C C   . TRP A 1 391 ? 20.306  -10.596 32.359 1.00 18.80 ? 391  TRP A C   1 
ATOM   3103 O O   . TRP A 1 391 ? 20.990  -10.367 33.351 1.00 18.11 ? 391  TRP A O   1 
ATOM   3104 C CB  . TRP A 1 391 ? 21.293  -10.586 30.096 1.00 19.87 ? 391  TRP A CB  1 
ATOM   3105 C CG  . TRP A 1 391 ? 21.707  -9.849  28.858 1.00 20.00 ? 391  TRP A CG  1 
ATOM   3106 C CD1 . TRP A 1 391 ? 23.004  -9.695  28.385 1.00 21.50 ? 391  TRP A CD1 1 
ATOM   3107 C CD2 . TRP A 1 391 ? 20.860  -9.197  27.909 1.00 20.60 ? 391  TRP A CD2 1 
ATOM   3108 N NE1 . TRP A 1 391 ? 22.991  -8.992  27.206 1.00 21.41 ? 391  TRP A NE1 1 
ATOM   3109 C CE2 . TRP A 1 391 ? 21.690  -8.676  26.895 1.00 19.63 ? 391  TRP A CE2 1 
ATOM   3110 C CE3 . TRP A 1 391 ? 19.468  -9.025  27.796 1.00 19.15 ? 391  TRP A CE3 1 
ATOM   3111 C CZ2 . TRP A 1 391 ? 21.181  -7.981  25.809 1.00 21.69 ? 391  TRP A CZ2 1 
ATOM   3112 C CZ3 . TRP A 1 391 ? 18.973  -8.316  26.728 1.00 21.43 ? 391  TRP A CZ3 1 
ATOM   3113 C CH2 . TRP A 1 391 ? 19.817  -7.809  25.738 1.00 20.48 ? 391  TRP A CH2 1 
ATOM   3114 N N   . VAL A 1 392 ? 19.360  -11.552 32.327 1.00 17.73 ? 392  VAL A N   1 
ATOM   3115 C CA  . VAL A 1 392 ? 19.259  -12.556 33.362 1.00 16.69 ? 392  VAL A CA  1 
ATOM   3116 C C   . VAL A 1 392 ? 20.537  -13.415 33.252 1.00 17.57 ? 392  VAL A C   1 
ATOM   3117 O O   . VAL A 1 392 ? 20.930  -13.780 32.142 1.00 17.85 ? 392  VAL A O   1 
ATOM   3118 C CB  . VAL A 1 392 ? 18.048  -13.470 33.135 1.00 16.17 ? 392  VAL A CB  1 
ATOM   3119 C CG1 . VAL A 1 392 ? 18.034  -14.616 34.149 1.00 17.24 ? 392  VAL A CG1 1 
ATOM   3120 C CG2 . VAL A 1 392 ? 16.712  -12.635 33.188 1.00 13.02 ? 392  VAL A CG2 1 
ATOM   3121 N N   . ASN A 1 393 ? 21.179  -13.692 34.373 1.00 18.49 ? 393  ASN A N   1 
ATOM   3122 C CA  . ASN A 1 393 ? 22.435  -14.467 34.353 1.00 20.60 ? 393  ASN A CA  1 
ATOM   3123 C C   . ASN A 1 393 ? 22.163  -15.885 34.751 1.00 21.52 ? 393  ASN A C   1 
ATOM   3124 O O   . ASN A 1 393 ? 21.203  -16.150 35.454 1.00 19.58 ? 393  ASN A O   1 
ATOM   3125 C CB  . ASN A 1 393 ? 23.441  -13.865 35.326 1.00 20.33 ? 393  ASN A CB  1 
ATOM   3126 C CG  . ASN A 1 393 ? 23.934  -12.517 34.866 1.00 20.26 ? 393  ASN A CG  1 
ATOM   3127 O OD1 . ASN A 1 393 ? 23.824  -12.180 33.685 1.00 20.96 ? 393  ASN A OD1 1 
ATOM   3128 N ND2 . ASN A 1 393 ? 24.474  -11.741 35.798 1.00 20.76 ? 393  ASN A ND2 1 
ATOM   3129 N N   . SER A 1 394 ? 23.026  -16.794 34.293 1.00 21.94 ? 394  SER A N   1 
ATOM   3130 C CA  . SER A 1 394 ? 23.093  -18.152 34.820 1.00 24.21 ? 394  SER A CA  1 
ATOM   3131 C C   . SER A 1 394 ? 23.498  -18.150 36.290 1.00 24.32 ? 394  SER A C   1 
ATOM   3132 O O   . SER A 1 394 ? 23.789  -17.109 36.869 1.00 24.60 ? 394  SER A O   1 
ATOM   3133 C CB  . SER A 1 394 ? 24.127  -18.965 34.018 1.00 25.29 ? 394  SER A CB  1 
ATOM   3134 O OG  . SER A 1 394 ? 23.651  -19.121 32.700 1.00 30.99 ? 394  SER A OG  1 
ATOM   3135 N N   . SER A 1 395 ? 23.536  -19.330 36.890 1.00 25.15 ? 395  SER A N   1 
ATOM   3136 C CA  . SER A 1 395 ? 23.756  -19.438 38.312 1.00 27.31 ? 395  SER A CA  1 
ATOM   3137 C C   . SER A 1 395 ? 25.163  -18.978 38.774 1.00 28.01 ? 395  SER A C   1 
ATOM   3138 O O   . SER A 1 395 ? 25.325  -18.608 39.932 1.00 28.61 ? 395  SER A O   1 
ATOM   3139 C CB  . SER A 1 395 ? 23.411  -20.840 38.816 1.00 27.02 ? 395  SER A CB  1 
ATOM   3140 O OG  . SER A 1 395 ? 24.487  -21.734 38.552 1.00 28.33 ? 395  SER A OG  1 
ATOM   3141 N N   . ASP A 1 396 ? 26.141  -18.924 37.871 1.00 29.28 ? 396  ASP A N   1 
ATOM   3142 C CA  . ASP A 1 396 ? 27.456  -18.326 38.217 1.00 29.84 ? 396  ASP A CA  1 
ATOM   3143 C C   . ASP A 1 396 ? 27.369  -16.832 38.557 1.00 29.74 ? 396  ASP A C   1 
ATOM   3144 O O   . ASP A 1 396 ? 28.319  -16.223 39.047 1.00 29.71 ? 396  ASP A O   1 
ATOM   3145 C CB  . ASP A 1 396 ? 28.545  -18.624 37.166 1.00 30.13 ? 396  ASP A CB  1 
ATOM   3146 C CG  . ASP A 1 396 ? 28.345  -17.897 35.826 1.00 31.81 ? 396  ASP A CG  1 
ATOM   3147 O OD1 . ASP A 1 396 ? 27.430  -17.042 35.672 1.00 28.81 ? 396  ASP A OD1 1 
ATOM   3148 O OD2 . ASP A 1 396 ? 29.159  -18.174 34.906 1.00 30.45 ? 396  ASP A OD2 1 
ATOM   3149 N N   . GLY A 1 397 ? 26.208  -16.244 38.283 1.00 29.13 ? 397  GLY A N   1 
ATOM   3150 C CA  . GLY A 1 397 ? 25.963  -14.855 38.597 1.00 28.25 ? 397  GLY A CA  1 
ATOM   3151 C C   . GLY A 1 397 ? 26.607  -13.864 37.646 1.00 28.39 ? 397  GLY A C   1 
ATOM   3152 O O   . GLY A 1 397 ? 26.523  -12.664 37.879 1.00 28.80 ? 397  GLY A O   1 
ATOM   3153 N N   . VAL A 1 398 ? 27.254  -14.333 36.575 1.00 27.88 ? 398  VAL A N   1 
ATOM   3154 C CA  . VAL A 1 398 ? 27.959  -13.400 35.667 1.00 27.41 ? 398  VAL A CA  1 
ATOM   3155 C C   . VAL A 1 398 ? 27.781  -13.620 34.169 1.00 26.13 ? 398  VAL A C   1 
ATOM   3156 O O   . VAL A 1 398 ? 28.036  -12.729 33.370 1.00 27.14 ? 398  VAL A O   1 
ATOM   3157 C CB  . VAL A 1 398 ? 29.476  -13.317 35.971 1.00 28.36 ? 398  VAL A CB  1 
ATOM   3158 C CG1 . VAL A 1 398 ? 29.691  -12.680 37.331 1.00 29.44 ? 398  VAL A CG1 1 
ATOM   3159 C CG2 . VAL A 1 398 ? 30.121  -14.721 35.897 1.00 28.28 ? 398  VAL A CG2 1 
ATOM   3160 N N   . THR A 1 399 ? 27.356  -14.812 33.796 1.00 24.97 ? 399  THR A N   1 
ATOM   3161 C CA  . THR A 1 399 ? 27.196  -15.153 32.409 1.00 25.52 ? 399  THR A CA  1 
ATOM   3162 C C   . THR A 1 399 ? 25.716  -15.066 32.041 1.00 24.62 ? 399  THR A C   1 
ATOM   3163 O O   . THR A 1 399 ? 24.920  -15.752 32.661 1.00 23.07 ? 399  THR A O   1 
ATOM   3164 C CB  . THR A 1 399 ? 27.709  -16.589 32.177 1.00 25.95 ? 399  THR A CB  1 
ATOM   3165 O OG1 . THR A 1 399 ? 29.068  -16.669 32.657 1.00 27.81 ? 399  THR A OG1 1 
ATOM   3166 C CG2 . THR A 1 399 ? 27.665  -16.952 30.713 1.00 27.23 ? 399  THR A CG2 1 
ATOM   3167 N N   . PRO A 1 400 ? 25.366  -14.229 31.043 1.00 24.54 ? 400  PRO A N   1 
ATOM   3168 C CA  . PRO A 1 400 ? 23.969  -14.207 30.565 1.00 23.60 ? 400  PRO A CA  1 
ATOM   3169 C C   . PRO A 1 400 ? 23.444  -15.598 30.208 1.00 23.88 ? 400  PRO A C   1 
ATOM   3170 O O   . PRO A 1 400 ? 24.095  -16.360 29.471 1.00 22.65 ? 400  PRO A O   1 
ATOM   3171 C CB  . PRO A 1 400 ? 24.036  -13.319 29.315 1.00 24.28 ? 400  PRO A CB  1 
ATOM   3172 C CG  . PRO A 1 400 ? 25.166  -12.404 29.562 1.00 24.30 ? 400  PRO A CG  1 
ATOM   3173 C CD  . PRO A 1 400 ? 26.188  -13.212 30.362 1.00 23.50 ? 400  PRO A CD  1 
ATOM   3174 N N   . LEU A 1 401 ? 22.261  -15.924 30.722 1.00 21.62 ? 401  LEU A N   1 
ATOM   3175 C CA  . LEU A 1 401 ? 21.640  -17.198 30.408 1.00 22.04 ? 401  LEU A CA  1 
ATOM   3176 C C   . LEU A 1 401 ? 21.177  -17.197 28.957 1.00 21.97 ? 401  LEU A C   1 
ATOM   3177 O O   . LEU A 1 401 ? 20.574  -16.229 28.490 1.00 21.33 ? 401  LEU A O   1 
ATOM   3178 C CB  . LEU A 1 401 ? 20.479  -17.478 31.385 1.00 20.86 ? 401  LEU A CB  1 
ATOM   3179 C CG  . LEU A 1 401 ? 19.680  -18.782 31.185 1.00 22.76 ? 401  LEU A CG  1 
ATOM   3180 C CD1 . LEU A 1 401 ? 19.100  -19.263 32.477 1.00 22.94 ? 401  LEU A CD1 1 
ATOM   3181 C CD2 . LEU A 1 401 ? 18.583  -18.629 30.137 1.00 23.43 ? 401  LEU A CD2 1 
ATOM   3182 N N   . ILE A 1 402 ? 21.453  -18.285 28.240 1.00 21.94 ? 402  ILE A N   1 
ATOM   3183 C CA  . ILE A 1 402 ? 21.018  -18.407 26.865 1.00 21.51 ? 402  ILE A CA  1 
ATOM   3184 C C   . ILE A 1 402 ? 19.901  -19.421 26.730 1.00 20.46 ? 402  ILE A C   1 
ATOM   3185 O O   . ILE A 1 402 ? 20.005  -20.557 27.189 1.00 20.24 ? 402  ILE A O   1 
ATOM   3186 C CB  . ILE A 1 402 ? 22.197  -18.779 25.913 1.00 21.68 ? 402  ILE A CB  1 
ATOM   3187 C CG1 . ILE A 1 402 ? 23.240  -17.651 25.925 1.00 24.31 ? 402  ILE A CG1 1 
ATOM   3188 C CG2 . ILE A 1 402 ? 21.691  -19.029 24.471 1.00 21.99 ? 402  ILE A CG2 1 
ATOM   3189 C CD1 . ILE A 1 402 ? 24.586  -18.059 25.356 1.00 26.68 ? 402  ILE A CD1 1 
ATOM   3190 N N   . GLY A 1 403 ? 18.802  -18.992 26.129 1.00 20.10 ? 403  GLY A N   1 
ATOM   3191 C CA  . GLY A 1 403 ? 17.719  -19.922 25.837 1.00 18.79 ? 403  GLY A CA  1 
ATOM   3192 C C   . GLY A 1 403 ? 17.397  -19.793 24.367 1.00 19.24 ? 403  GLY A C   1 
ATOM   3193 O O   . GLY A 1 403 ? 18.244  -19.404 23.574 1.00 18.98 ? 403  GLY A O   1 
ATOM   3194 N N   . GLU A 1 404 ? 16.156  -20.104 23.983 1.00 17.94 ? 404  GLU A N   1 
ATOM   3195 C CA  . GLU A 1 404 ? 15.768  -20.039 22.600 1.00 18.44 ? 404  GLU A CA  1 
ATOM   3196 C C   . GLU A 1 404 ? 14.321  -19.569 22.505 1.00 18.22 ? 404  GLU A C   1 
ATOM   3197 O O   . GLU A 1 404 ? 13.458  -20.162 23.153 1.00 18.86 ? 404  GLU A O   1 
ATOM   3198 C CB  . GLU A 1 404 ? 15.834  -21.456 22.015 1.00 18.98 ? 404  GLU A CB  1 
ATOM   3199 C CG  . GLU A 1 404 ? 15.734  -21.540 20.510 1.00 23.71 ? 404  GLU A CG  1 
ATOM   3200 C CD  . GLU A 1 404 ? 15.431  -22.949 20.042 1.00 31.25 ? 404  GLU A CD  1 
ATOM   3201 O OE1 . GLU A 1 404 ? 16.051  -23.896 20.594 1.00 34.09 ? 404  GLU A OE1 1 
ATOM   3202 O OE2 . GLU A 1 404 ? 14.567  -23.114 19.139 1.00 32.18 ? 404  GLU A OE2 1 
ATOM   3203 N N   . VAL A 1 405 ? 14.051  -18.553 21.706 1.00 17.33 ? 405  VAL A N   1 
ATOM   3204 C CA  . VAL A 1 405 ? 12.616  -18.199 21.438 1.00 17.82 ? 405  VAL A CA  1 
ATOM   3205 C C   . VAL A 1 405 ? 12.489  -17.971 19.941 1.00 17.96 ? 405  VAL A C   1 
ATOM   3206 O O   . VAL A 1 405 ? 13.165  -18.645 19.173 1.00 18.38 ? 405  VAL A O   1 
ATOM   3207 C CB  . VAL A 1 405 ? 12.084  -17.050 22.357 1.00 16.99 ? 405  VAL A CB  1 
ATOM   3208 C CG1 . VAL A 1 405 ? 10.493  -17.089 22.419 1.00 15.97 ? 405  VAL A CG1 1 
ATOM   3209 C CG2 . VAL A 1 405 ? 12.598  -17.253 23.754 1.00 15.94 ? 405  VAL A CG2 1 
ATOM   3210 N N   . TRP A 1 406 ? 11.654  -17.043 19.506 1.00 18.24 ? 406  TRP A N   1 
ATOM   3211 C CA  . TRP A 1 406 ? 11.332  -16.892 18.097 1.00 18.63 ? 406  TRP A CA  1 
ATOM   3212 C C   . TRP A 1 406 ? 12.542  -16.627 17.168 1.00 18.96 ? 406  TRP A C   1 
ATOM   3213 O O   . TRP A 1 406 ? 12.618  -17.230 16.114 1.00 19.64 ? 406  TRP A O   1 
ATOM   3214 C CB  . TRP A 1 406 ? 10.342  -15.756 17.924 1.00 18.77 ? 406  TRP A CB  1 
ATOM   3215 C CG  . TRP A 1 406 ? 9.011   -16.008 18.609 1.00 17.40 ? 406  TRP A CG  1 
ATOM   3216 C CD1 . TRP A 1 406 ? 8.418   -15.219 19.559 1.00 20.40 ? 406  TRP A CD1 1 
ATOM   3217 C CD2 . TRP A 1 406 ? 8.127   -17.108 18.393 1.00 19.29 ? 406  TRP A CD2 1 
ATOM   3218 N NE1 . TRP A 1 406 ? 7.194   -15.756 19.939 1.00 17.68 ? 406  TRP A NE1 1 
ATOM   3219 C CE2 . TRP A 1 406 ? 6.983   -16.903 19.227 1.00 17.15 ? 406  TRP A CE2 1 
ATOM   3220 C CE3 . TRP A 1 406 ? 8.161   -18.234 17.555 1.00 17.23 ? 406  TRP A CE3 1 
ATOM   3221 C CZ2 . TRP A 1 406 ? 5.929   -17.804 19.282 1.00 20.49 ? 406  TRP A CZ2 1 
ATOM   3222 C CZ3 . TRP A 1 406 ? 7.076   -19.134 17.592 1.00 19.37 ? 406  TRP A CZ3 1 
ATOM   3223 C CH2 . TRP A 1 406 ? 5.978   -18.901 18.455 1.00 19.67 ? 406  TRP A CH2 1 
ATOM   3224 N N   . PRO A 1 407 ? 13.451  -15.715 17.543 1.00 19.15 ? 407  PRO A N   1 
ATOM   3225 C CA  . PRO A 1 407 ? 14.554  -15.473 16.595 1.00 20.94 ? 407  PRO A CA  1 
ATOM   3226 C C   . PRO A 1 407 ? 15.642  -16.566 16.551 1.00 22.92 ? 407  PRO A C   1 
ATOM   3227 O O   . PRO A 1 407 ? 16.565  -16.480 15.705 1.00 24.09 ? 407  PRO A O   1 
ATOM   3228 C CB  . PRO A 1 407 ? 15.149  -14.158 17.087 1.00 20.86 ? 407  PRO A CB  1 
ATOM   3229 C CG  . PRO A 1 407 ? 14.926  -14.163 18.559 1.00 19.16 ? 407  PRO A CG  1 
ATOM   3230 C CD  . PRO A 1 407 ? 13.552  -14.866 18.741 1.00 19.58 ? 407  PRO A CD  1 
ATOM   3231 N N   . GLY A 1 408 ? 15.533  -17.577 17.403 1.00 22.26 ? 408  GLY A N   1 
ATOM   3232 C CA  . GLY A 1 408 ? 16.673  -18.511 17.645 1.00 23.27 ? 408  GLY A CA  1 
ATOM   3233 C C   . GLY A 1 408 ? 17.225  -18.304 19.045 1.00 22.90 ? 408  GLY A C   1 
ATOM   3234 O O   . GLY A 1 408 ? 16.462  -17.938 19.954 1.00 22.24 ? 408  GLY A O   1 
ATOM   3235 N N   . GLN A 1 409 ? 18.539  -18.521 19.249 1.00 21.96 ? 409  GLN A N   1 
ATOM   3236 C CA  . GLN A 1 409 ? 19.175  -18.316 20.562 1.00 22.57 ? 409  GLN A CA  1 
ATOM   3237 C C   . GLN A 1 409 ? 18.972  -16.897 21.046 1.00 20.82 ? 409  GLN A C   1 
ATOM   3238 O O   . GLN A 1 409 ? 19.063  -15.929 20.268 1.00 20.36 ? 409  GLN A O   1 
ATOM   3239 C CB  . GLN A 1 409 ? 20.707  -18.578 20.543 1.00 22.80 ? 409  GLN A CB  1 
ATOM   3240 C CG  . GLN A 1 409 ? 21.144  -20.006 20.735 1.00 28.22 ? 409  GLN A CG  1 
ATOM   3241 C CD  . GLN A 1 409 ? 22.628  -20.133 21.127 1.00 26.87 ? 409  GLN A CD  1 
ATOM   3242 O OE1 . GLN A 1 409 ? 23.394  -19.145 21.169 1.00 32.63 ? 409  GLN A OE1 1 
ATOM   3243 N NE2 . GLN A 1 409 ? 23.028  -21.346 21.443 1.00 34.76 ? 409  GLN A NE2 1 
ATOM   3244 N N   . THR A 1 410 ? 18.716  -16.767 22.348 1.00 20.17 ? 410  THR A N   1 
ATOM   3245 C CA  . THR A 1 410 ? 18.395  -15.471 22.917 1.00 19.76 ? 410  THR A CA  1 
ATOM   3246 C C   . THR A 1 410 ? 18.895  -15.357 24.331 1.00 17.60 ? 410  THR A C   1 
ATOM   3247 O O   . THR A 1 410 ? 19.072  -16.336 25.024 1.00 18.97 ? 410  THR A O   1 
ATOM   3248 C CB  . THR A 1 410 ? 16.862  -15.260 23.036 1.00 18.44 ? 410  THR A CB  1 
ATOM   3249 O OG1 . THR A 1 410 ? 16.297  -16.387 23.726 1.00 20.27 ? 410  THR A OG1 1 
ATOM   3250 C CG2 . THR A 1 410 ? 16.229  -15.143 21.675 1.00 20.47 ? 410  THR A CG2 1 
ATOM   3251 N N   . VAL A 1 411 ? 19.080  -14.119 24.747 1.00 17.65 ? 411  VAL A N   1 
ATOM   3252 C CA  . VAL A 1 411 ? 19.232  -13.751 26.148 1.00 16.97 ? 411  VAL A CA  1 
ATOM   3253 C C   . VAL A 1 411 ? 17.904  -13.087 26.616 1.00 17.62 ? 411  VAL A C   1 
ATOM   3254 O O   . VAL A 1 411 ? 17.046  -12.765 25.805 1.00 17.22 ? 411  VAL A O   1 
ATOM   3255 C CB  . VAL A 1 411 ? 20.440  -12.820 26.345 1.00 17.54 ? 411  VAL A CB  1 
ATOM   3256 C CG1 . VAL A 1 411 ? 21.771  -13.651 26.221 1.00 16.19 ? 411  VAL A CG1 1 
ATOM   3257 C CG2 . VAL A 1 411 ? 20.395  -11.660 25.365 1.00 16.89 ? 411  VAL A CG2 1 
ATOM   3258 N N   . PHE A 1 412 ? 17.764  -12.902 27.912 1.00 17.68 ? 412  PHE A N   1 
ATOM   3259 C CA  . PHE A 1 412 ? 16.489  -12.446 28.505 1.00 18.14 ? 412  PHE A CA  1 
ATOM   3260 C C   . PHE A 1 412 ? 16.771  -11.219 29.360 1.00 17.46 ? 412  PHE A C   1 
ATOM   3261 O O   . PHE A 1 412 ? 17.615  -11.260 30.257 1.00 17.95 ? 412  PHE A O   1 
ATOM   3262 C CB  . PHE A 1 412 ? 15.866  -13.592 29.349 1.00 17.23 ? 412  PHE A CB  1 
ATOM   3263 C CG  . PHE A 1 412 ? 15.562  -14.831 28.556 1.00 16.76 ? 412  PHE A CG  1 
ATOM   3264 C CD1 . PHE A 1 412 ? 14.325  -14.979 27.947 1.00 18.46 ? 412  PHE A CD1 1 
ATOM   3265 C CD2 . PHE A 1 412 ? 16.541  -15.832 28.348 1.00 19.15 ? 412  PHE A CD2 1 
ATOM   3266 C CE1 . PHE A 1 412 ? 14.035  -16.118 27.201 1.00 18.43 ? 412  PHE A CE1 1 
ATOM   3267 C CE2 . PHE A 1 412 ? 16.253  -16.959 27.593 1.00 17.88 ? 412  PHE A CE2 1 
ATOM   3268 C CZ  . PHE A 1 412 ? 14.982  -17.109 27.029 1.00 18.18 ? 412  PHE A CZ  1 
ATOM   3269 N N   . PRO A 1 413 ? 16.032  -10.123 29.133 1.00 17.18 ? 413  PRO A N   1 
ATOM   3270 C CA  . PRO A 1 413 ? 16.254  -8.950  29.963 1.00 16.97 ? 413  PRO A CA  1 
ATOM   3271 C C   . PRO A 1 413 ? 15.862  -9.186  31.404 1.00 17.56 ? 413  PRO A C   1 
ATOM   3272 O O   . PRO A 1 413 ? 14.895  -9.923  31.692 1.00 18.76 ? 413  PRO A O   1 
ATOM   3273 C CB  . PRO A 1 413 ? 15.342  -7.879  29.343 1.00 16.57 ? 413  PRO A CB  1 
ATOM   3274 C CG  . PRO A 1 413 ? 14.983  -8.401  27.994 1.00 16.48 ? 413  PRO A CG  1 
ATOM   3275 C CD  . PRO A 1 413 ? 14.981  -9.906  28.126 1.00 16.38 ? 413  PRO A CD  1 
ATOM   3276 N N   . ASP A 1 414 ? 16.591  -8.555  32.312 1.00 15.73 ? 414  ASP A N   1 
ATOM   3277 C CA  . ASP A 1 414 ? 16.265  -8.678  33.723 1.00 17.45 ? 414  ASP A CA  1 
ATOM   3278 C C   . ASP A 1 414 ? 15.530  -7.396  34.070 1.00 17.12 ? 414  ASP A C   1 
ATOM   3279 O O   . ASP A 1 414 ? 16.126  -6.351  34.380 1.00 18.04 ? 414  ASP A O   1 
ATOM   3280 C CB  . ASP A 1 414 ? 17.518  -8.898  34.607 1.00 17.19 ? 414  ASP A CB  1 
ATOM   3281 C CG  . ASP A 1 414 ? 17.262  -8.628  36.089 1.00 19.78 ? 414  ASP A CG  1 
ATOM   3282 O OD1 . ASP A 1 414 ? 16.083  -8.631  36.548 1.00 21.18 ? 414  ASP A OD1 1 
ATOM   3283 O OD2 . ASP A 1 414 ? 18.238  -8.400  36.826 1.00 20.60 ? 414  ASP A OD2 1 
ATOM   3284 N N   . TYR A 1 415 ? 14.211  -7.443  33.944 1.00 18.55 ? 415  TYR A N   1 
ATOM   3285 C CA  . TYR A 1 415 ? 13.435  -6.205  34.131 1.00 17.83 ? 415  TYR A CA  1 
ATOM   3286 C C   . TYR A 1 415 ? 13.344  -5.774  35.588 1.00 19.36 ? 415  TYR A C   1 
ATOM   3287 O O   . TYR A 1 415 ? 12.840  -4.667  35.881 1.00 20.71 ? 415  TYR A O   1 
ATOM   3288 C CB  . TYR A 1 415 ? 12.035  -6.349  33.511 1.00 17.38 ? 415  TYR A CB  1 
ATOM   3289 C CG  . TYR A 1 415 ? 11.993  -6.551  32.019 1.00 15.61 ? 415  TYR A CG  1 
ATOM   3290 C CD1 . TYR A 1 415 ? 12.091  -5.481  31.155 1.00 15.70 ? 415  TYR A CD1 1 
ATOM   3291 C CD2 . TYR A 1 415 ? 11.792  -7.811  31.477 1.00 13.70 ? 415  TYR A CD2 1 
ATOM   3292 C CE1 . TYR A 1 415 ? 12.032  -5.646  29.774 1.00 14.51 ? 415  TYR A CE1 1 
ATOM   3293 C CE2 . TYR A 1 415 ? 11.729  -7.990  30.089 1.00 16.38 ? 415  TYR A CE2 1 
ATOM   3294 C CZ  . TYR A 1 415 ? 11.887  -6.900  29.257 1.00 16.12 ? 415  TYR A CZ  1 
ATOM   3295 O OH  . TYR A 1 415 ? 11.802  -7.085  27.902 1.00 17.94 ? 415  TYR A OH  1 
ATOM   3296 N N   . THR A 1 416 ? 13.831  -6.612  36.507 1.00 18.41 ? 416  THR A N   1 
ATOM   3297 C CA  . THR A 1 416 ? 13.883  -6.242  37.931 1.00 19.04 ? 416  THR A CA  1 
ATOM   3298 C C   . THR A 1 416 ? 15.019  -5.267  38.243 1.00 20.60 ? 416  THR A C   1 
ATOM   3299 O O   . THR A 1 416 ? 15.038  -4.637  39.300 1.00 20.05 ? 416  THR A O   1 
ATOM   3300 C CB  . THR A 1 416 ? 13.913  -7.468  38.888 1.00 18.85 ? 416  THR A CB  1 
ATOM   3301 O OG1 . THR A 1 416 ? 15.212  -8.107  38.879 1.00 18.92 ? 416  THR A OG1 1 
ATOM   3302 C CG2 . THR A 1 416 ? 12.842  -8.474  38.508 1.00 18.17 ? 416  THR A CG2 1 
ATOM   3303 N N   . ASN A 1 417 ? 15.970  -5.174  37.321 1.00 21.20 ? 417  ASN A N   1 
ATOM   3304 C CA  . ASN A 1 417 ? 17.043  -4.186  37.371 1.00 23.42 ? 417  ASN A CA  1 
ATOM   3305 C C   . ASN A 1 417 ? 16.549  -2.828  36.829 1.00 24.29 ? 417  ASN A C   1 
ATOM   3306 O O   . ASN A 1 417 ? 16.142  -2.750  35.672 1.00 24.04 ? 417  ASN A O   1 
ATOM   3307 C CB  . ASN A 1 417 ? 18.191  -4.731  36.508 1.00 22.11 ? 417  ASN A CB  1 
ATOM   3308 C CG  . ASN A 1 417 ? 19.436  -3.856  36.539 1.00 25.03 ? 417  ASN A CG  1 
ATOM   3309 O OD1 . ASN A 1 417 ? 19.375  -2.711  36.936 1.00 24.45 ? 417  ASN A OD1 1 
ATOM   3310 N ND2 . ASN A 1 417 ? 20.568  -4.409  36.116 1.00 24.81 ? 417  ASN A ND2 1 
ATOM   3311 N N   . PRO A 1 418 ? 16.573  -1.740  37.660 1.00 26.23 ? 418  PRO A N   1 
ATOM   3312 C CA  . PRO A 1 418 ? 16.152  -0.389  37.201 1.00 26.43 ? 418  PRO A CA  1 
ATOM   3313 C C   . PRO A 1 418 ? 16.845  0.060   35.906 1.00 26.65 ? 418  PRO A C   1 
ATOM   3314 O O   . PRO A 1 418 ? 16.231  0.716   35.053 1.00 25.41 ? 418  PRO A O   1 
ATOM   3315 C CB  . PRO A 1 418 ? 16.587  0.528   38.361 1.00 27.23 ? 418  PRO A CB  1 
ATOM   3316 C CG  . PRO A 1 418 ? 16.527  -0.342  39.565 1.00 28.21 ? 418  PRO A CG  1 
ATOM   3317 C CD  . PRO A 1 418 ? 16.972  -1.724  39.079 1.00 26.83 ? 418  PRO A CD  1 
ATOM   3318 N N   . ASN A 1 419 ? 18.112  -0.331  35.752 1.00 26.24 ? 419  ASN A N   1 
ATOM   3319 C CA  . ASN A 1 419 ? 18.864  -0.024  34.550 1.00 26.55 ? 419  ASN A CA  1 
ATOM   3320 C C   . ASN A 1 419 ? 18.307  -0.706  33.304 1.00 24.87 ? 419  ASN A C   1 
ATOM   3321 O O   . ASN A 1 419 ? 18.517  -0.226  32.188 1.00 23.62 ? 419  ASN A O   1 
ATOM   3322 C CB  . ASN A 1 419 ? 20.345  -0.405  34.752 1.00 27.73 ? 419  ASN A CB  1 
ATOM   3323 C CG  . ASN A 1 419 ? 21.140  0.680   35.471 1.00 32.97 ? 419  ASN A CG  1 
ATOM   3324 O OD1 . ASN A 1 419 ? 20.719  1.849   35.534 1.00 39.36 ? 419  ASN A OD1 1 
ATOM   3325 N ND2 . ASN A 1 419 ? 22.306  0.304   36.014 1.00 37.62 ? 419  ASN A ND2 1 
ATOM   3326 N N   . CYS A 1 420 ? 17.643  -1.857  33.489 1.00 23.46 ? 420  CYS A N   1 
ATOM   3327 C CA  . CYS A 1 420 ? 17.026  -2.570  32.379 1.00 22.67 ? 420  CYS A CA  1 
ATOM   3328 C C   . CYS A 1 420 ? 15.884  -1.760  31.774 1.00 22.57 ? 420  CYS A C   1 
ATOM   3329 O O   . CYS A 1 420 ? 15.721  -1.718  30.570 1.00 21.45 ? 420  CYS A O   1 
ATOM   3330 C CB  . CYS A 1 420 ? 16.523  -3.945  32.804 1.00 22.42 ? 420  CYS A CB  1 
ATOM   3331 S SG  . CYS A 1 420 ? 15.895  -4.958  31.423 1.00 22.71 ? 420  CYS A SG  1 
ATOM   3332 N N   . ALA A 1 421 ? 15.115  -1.093  32.614 1.00 23.16 ? 421  ALA A N   1 
ATOM   3333 C CA  . ALA A 1 421 ? 14.076  -0.199  32.118 1.00 23.15 ? 421  ALA A CA  1 
ATOM   3334 C C   . ALA A 1 421 ? 14.670  0.977   31.337 1.00 23.38 ? 421  ALA A C   1 
ATOM   3335 O O   . ALA A 1 421 ? 14.053  1.467   30.406 1.00 24.22 ? 421  ALA A O   1 
ATOM   3336 C CB  . ALA A 1 421 ? 13.260  0.295   33.258 1.00 23.59 ? 421  ALA A CB  1 
ATOM   3337 N N   . VAL A 1 422 ? 15.861  1.450   31.711 1.00 23.08 ? 422  VAL A N   1 
ATOM   3338 C CA  . VAL A 1 422 ? 16.501  2.503   30.922 1.00 22.71 ? 422  VAL A CA  1 
ATOM   3339 C C   . VAL A 1 422 ? 16.827  1.963   29.536 1.00 21.21 ? 422  VAL A C   1 
ATOM   3340 O O   . VAL A 1 422 ? 16.569  2.626   28.554 1.00 22.36 ? 422  VAL A O   1 
ATOM   3341 C CB  . VAL A 1 422 ? 17.825  3.031   31.572 1.00 23.50 ? 422  VAL A CB  1 
ATOM   3342 C CG1 . VAL A 1 422 ? 18.581  3.912   30.609 1.00 23.10 ? 422  VAL A CG1 1 
ATOM   3343 C CG2 . VAL A 1 422 ? 17.538  3.748   32.884 1.00 25.24 ? 422  VAL A CG2 1 
ATOM   3344 N N   . TRP A 1 423 ? 17.374  0.749   29.466 1.00 20.34 ? 423  TRP A N   1 
ATOM   3345 C CA  . TRP A 1 423 ? 17.726  0.109   28.195 1.00 19.59 ? 423  TRP A CA  1 
ATOM   3346 C C   . TRP A 1 423 ? 16.473  -0.101  27.352 1.00 19.10 ? 423  TRP A C   1 
ATOM   3347 O O   . TRP A 1 423 ? 16.466  0.185   26.176 1.00 17.87 ? 423  TRP A O   1 
ATOM   3348 C CB  . TRP A 1 423 ? 18.436  -1.231  28.441 1.00 20.05 ? 423  TRP A CB  1 
ATOM   3349 C CG  . TRP A 1 423 ? 18.419  -2.182  27.247 1.00 20.92 ? 423  TRP A CG  1 
ATOM   3350 C CD1 . TRP A 1 423 ? 19.219  -2.138  26.135 1.00 20.31 ? 423  TRP A CD1 1 
ATOM   3351 C CD2 . TRP A 1 423 ? 17.546  -3.303  27.071 1.00 19.38 ? 423  TRP A CD2 1 
ATOM   3352 N NE1 . TRP A 1 423 ? 18.891  -3.169  25.271 1.00 20.29 ? 423  TRP A NE1 1 
ATOM   3353 C CE2 . TRP A 1 423 ? 17.858  -3.889  25.825 1.00 20.15 ? 423  TRP A CE2 1 
ATOM   3354 C CE3 . TRP A 1 423 ? 16.515  -3.862  27.850 1.00 17.46 ? 423  TRP A CE3 1 
ATOM   3355 C CZ2 . TRP A 1 423 ? 17.190  -5.009  25.337 1.00 18.97 ? 423  TRP A CZ2 1 
ATOM   3356 C CZ3 . TRP A 1 423 ? 15.852  -4.979  27.357 1.00 18.60 ? 423  TRP A CZ3 1 
ATOM   3357 C CH2 . TRP A 1 423 ? 16.185  -5.530  26.107 1.00 19.59 ? 423  TRP A CH2 1 
ATOM   3358 N N   . TRP A 1 424 ? 15.422  -0.606  27.994 1.00 17.89 ? 424  TRP A N   1 
ATOM   3359 C CA  . TRP A 1 424 ? 14.176  -0.944  27.309 1.00 18.00 ? 424  TRP A CA  1 
ATOM   3360 C C   . TRP A 1 424 ? 13.587  0.334   26.736 1.00 16.49 ? 424  TRP A C   1 
ATOM   3361 O O   . TRP A 1 424 ? 13.142  0.356   25.602 1.00 17.60 ? 424  TRP A O   1 
ATOM   3362 C CB  . TRP A 1 424 ? 13.275  -1.575  28.370 1.00 18.18 ? 424  TRP A CB  1 
ATOM   3363 C CG  . TRP A 1 424 ? 12.009  -2.285  27.955 1.00 19.32 ? 424  TRP A CG  1 
ATOM   3364 C CD1 . TRP A 1 424 ? 10.755  -2.069  28.504 1.00 18.67 ? 424  TRP A CD1 1 
ATOM   3365 C CD2 . TRP A 1 424 ? 11.862  -3.391  27.050 1.00 19.32 ? 424  TRP A CD2 1 
ATOM   3366 N NE1 . TRP A 1 424 ? 9.839   -2.920  27.926 1.00 17.83 ? 424  TRP A NE1 1 
ATOM   3367 C CE2 . TRP A 1 424 ? 10.482  -3.744  27.045 1.00 19.16 ? 424  TRP A CE2 1 
ATOM   3368 C CE3 . TRP A 1 424 ? 12.738  -4.076  26.186 1.00 18.00 ? 424  TRP A CE3 1 
ATOM   3369 C CZ2 . TRP A 1 424 ? 9.977   -4.772  26.245 1.00 19.62 ? 424  TRP A CZ2 1 
ATOM   3370 C CZ3 . TRP A 1 424 ? 12.246  -5.090  25.409 1.00 19.80 ? 424  TRP A CZ3 1 
ATOM   3371 C CH2 . TRP A 1 424 ? 10.874  -5.440  25.443 1.00 20.01 ? 424  TRP A CH2 1 
ATOM   3372 N N   . THR A 1 425 ? 13.556  1.383   27.538 1.00 17.67 ? 425  THR A N   1 
ATOM   3373 C CA  . THR A 1 425 ? 13.001  2.673   27.108 1.00 18.97 ? 425  THR A CA  1 
ATOM   3374 C C   . THR A 1 425 ? 13.720  3.171   25.836 1.00 19.30 ? 425  THR A C   1 
ATOM   3375 O O   . THR A 1 425 ? 13.091  3.565   24.866 1.00 18.00 ? 425  THR A O   1 
ATOM   3376 C CB  . THR A 1 425 ? 13.126  3.720   28.232 1.00 19.33 ? 425  THR A CB  1 
ATOM   3377 O OG1 . THR A 1 425 ? 12.399  3.284   29.398 1.00 21.93 ? 425  THR A OG1 1 
ATOM   3378 C CG2 . THR A 1 425 ? 12.649  5.089   27.773 1.00 20.01 ? 425  THR A CG2 1 
ATOM   3379 N N   . LYS A 1 426 ? 15.055  3.117   25.843 1.00 19.42 ? 426  LYS A N   1 
ATOM   3380 C CA  . LYS A 1 426 ? 15.816  3.562   24.683 1.00 20.39 ? 426  LYS A CA  1 
ATOM   3381 C C   . LYS A 1 426 ? 15.554  2.727   23.446 1.00 18.71 ? 426  LYS A C   1 
ATOM   3382 O O   . LYS A 1 426 ? 15.472  3.268   22.347 1.00 20.38 ? 426  LYS A O   1 
ATOM   3383 C CB  . LYS A 1 426 ? 17.320  3.663   25.005 1.00 20.18 ? 426  LYS A CB  1 
ATOM   3384 C CG  . LYS A 1 426 ? 18.206  4.009   23.799 1.00 26.59 ? 426  LYS A CG  1 
ATOM   3385 C CD  . LYS A 1 426 ? 17.904  5.394   23.192 1.00 30.98 ? 426  LYS A CD  1 
ATOM   3386 C CE  . LYS A 1 426 ? 18.818  6.493   23.751 1.00 33.49 ? 426  LYS A CE  1 
ATOM   3387 N NZ  . LYS A 1 426 ? 18.368  7.882   23.318 1.00 33.67 ? 426  LYS A NZ  1 
ATOM   3388 N N   . GLU A 1 427 ? 15.354  1.415   23.603 1.00 19.10 ? 427  GLU A N   1 
ATOM   3389 C CA  . GLU A 1 427 ? 15.049  0.577   22.448 1.00 18.21 ? 427  GLU A CA  1 
ATOM   3390 C C   . GLU A 1 427 ? 13.703  0.975   21.821 1.00 18.46 ? 427  GLU A C   1 
ATOM   3391 O O   . GLU A 1 427 ? 13.555  1.067   20.608 1.00 17.95 ? 427  GLU A O   1 
ATOM   3392 C CB  . GLU A 1 427 ? 15.067  -0.915  22.796 1.00 17.81 ? 427  GLU A CB  1 
ATOM   3393 C CG  . GLU A 1 427 ? 16.431  -1.486  23.234 1.00 20.36 ? 427  GLU A CG  1 
ATOM   3394 C CD  . GLU A 1 427 ? 17.566  -1.303  22.219 1.00 22.25 ? 427  GLU A CD  1 
ATOM   3395 O OE1 . GLU A 1 427 ? 17.321  -1.204  20.994 1.00 22.06 ? 427  GLU A OE1 1 
ATOM   3396 O OE2 . GLU A 1 427 ? 18.730  -1.259  22.682 1.00 25.42 ? 427  GLU A OE2 1 
ATOM   3397 N N   . PHE A 1 428 ? 12.717  1.222   22.663 1.00 19.02 ? 428  PHE A N   1 
ATOM   3398 C CA  . PHE A 1 428 ? 11.438  1.711   22.153 1.00 19.21 ? 428  PHE A CA  1 
ATOM   3399 C C   . PHE A 1 428 ? 11.503  3.095   21.516 1.00 19.95 ? 428  PHE A C   1 
ATOM   3400 O O   . PHE A 1 428 ? 10.819  3.334   20.546 1.00 20.34 ? 428  PHE A O   1 
ATOM   3401 C CB  . PHE A 1 428 ? 10.427  1.742   23.271 1.00 20.08 ? 428  PHE A CB  1 
ATOM   3402 C CG  . PHE A 1 428 ? 9.803   0.424   23.510 1.00 19.30 ? 428  PHE A CG  1 
ATOM   3403 C CD1 . PHE A 1 428 ? 8.832   -0.056  22.647 1.00 21.64 ? 428  PHE A CD1 1 
ATOM   3404 C CD2 . PHE A 1 428 ? 10.196  -0.351  24.582 1.00 22.82 ? 428  PHE A CD2 1 
ATOM   3405 C CE1 . PHE A 1 428 ? 8.265   -1.298  22.878 1.00 22.16 ? 428  PHE A CE1 1 
ATOM   3406 C CE2 . PHE A 1 428 ? 9.618   -1.596  24.806 1.00 22.68 ? 428  PHE A CE2 1 
ATOM   3407 C CZ  . PHE A 1 428 ? 8.645   -2.041  23.959 1.00 21.83 ? 428  PHE A CZ  1 
ATOM   3408 N N   . GLU A 1 429 ? 12.311  4.000   22.076 1.00 20.86 ? 429  GLU A N   1 
ATOM   3409 C CA  . GLU A 1 429 ? 12.450  5.354   21.506 1.00 22.29 ? 429  GLU A CA  1 
ATOM   3410 C C   . GLU A 1 429 ? 13.024  5.236   20.117 1.00 21.26 ? 429  GLU A C   1 
ATOM   3411 O O   . GLU A 1 429 ? 12.578  5.879   19.186 1.00 20.93 ? 429  GLU A O   1 
ATOM   3412 C CB  . GLU A 1 429 ? 13.449  6.175   22.303 1.00 23.79 ? 429  GLU A CB  1 
ATOM   3413 C CG  . GLU A 1 429 ? 12.976  6.773   23.594 1.00 29.37 ? 429  GLU A CG  1 
ATOM   3414 C CD  . GLU A 1 429 ? 14.113  7.628   24.179 1.00 36.37 ? 429  GLU A CD  1 
ATOM   3415 O OE1 . GLU A 1 429 ? 14.497  8.635   23.530 1.00 40.67 ? 429  GLU A OE1 1 
ATOM   3416 O OE2 . GLU A 1 429 ? 14.650  7.268   25.255 1.00 37.85 ? 429  GLU A OE2 1 
ATOM   3417 N N   . LEU A 1 430 ? 14.092  4.453   19.992 1.00 21.38 ? 430  LEU A N   1 
ATOM   3418 C CA  . LEU A 1 430 ? 14.710  4.235   18.698 1.00 20.49 ? 430  LEU A CA  1 
ATOM   3419 C C   . LEU A 1 430 ? 13.761  3.624   17.679 1.00 21.52 ? 430  LEU A C   1 
ATOM   3420 O O   . LEU A 1 430 ? 13.707  4.066   16.522 1.00 21.21 ? 430  LEU A O   1 
ATOM   3421 C CB  . LEU A 1 430 ? 15.962  3.368   18.850 1.00 21.94 ? 430  LEU A CB  1 
ATOM   3422 C CG  . LEU A 1 430 ? 17.103  4.101   19.551 1.00 21.66 ? 430  LEU A CG  1 
ATOM   3423 C CD1 . LEU A 1 430 ? 18.205  3.116   19.911 1.00 24.33 ? 430  LEU A CD1 1 
ATOM   3424 C CD2 . LEU A 1 430 ? 17.625  5.214   18.635 1.00 26.30 ? 430  LEU A CD2 1 
ATOM   3425 N N   . PHE A 1 431 ? 13.026  2.588   18.084 1.00 20.34 ? 431  PHE A N   1 
ATOM   3426 C CA  . PHE A 1 431 ? 12.099  1.952   17.166 1.00 20.48 ? 431  PHE A CA  1 
ATOM   3427 C C   . PHE A 1 431 ? 10.910  2.851   16.829 1.00 19.98 ? 431  PHE A C   1 
ATOM   3428 O O   . PHE A 1 431 ? 10.387  2.796   15.710 1.00 19.67 ? 431  PHE A O   1 
ATOM   3429 C CB  . PHE A 1 431 ? 11.587  0.609   17.705 1.00 20.35 ? 431  PHE A CB  1 
ATOM   3430 C CG  . PHE A 1 431 ? 10.957  -0.257  16.636 1.00 20.48 ? 431  PHE A CG  1 
ATOM   3431 C CD1 . PHE A 1 431 ? 11.628  -0.489  15.422 1.00 20.82 ? 431  PHE A CD1 1 
ATOM   3432 C CD2 . PHE A 1 431 ? 9.726   -0.864  16.850 1.00 21.63 ? 431  PHE A CD2 1 
ATOM   3433 C CE1 . PHE A 1 431 ? 11.073  -1.283  14.445 1.00 23.14 ? 431  PHE A CE1 1 
ATOM   3434 C CE2 . PHE A 1 431 ? 9.154   -1.672  15.869 1.00 21.56 ? 431  PHE A CE2 1 
ATOM   3435 C CZ  . PHE A 1 431 ? 9.817   -1.877  14.667 1.00 22.58 ? 431  PHE A CZ  1 
ATOM   3436 N N   . HIS A 1 432 ? 10.466  3.643   17.804 1.00 21.67 ? 432  HIS A N   1 
ATOM   3437 C CA  . HIS A 1 432 ? 9.309   4.552   17.581 1.00 22.89 ? 432  HIS A CA  1 
ATOM   3438 C C   . HIS A 1 432 ? 9.668   5.666   16.584 1.00 24.25 ? 432  HIS A C   1 
ATOM   3439 O O   . HIS A 1 432 ? 8.812   6.192   15.881 1.00 23.53 ? 432  HIS A O   1 
ATOM   3440 C CB  . HIS A 1 432 ? 8.808   5.152   18.893 1.00 22.60 ? 432  HIS A CB  1 
ATOM   3441 C CG  . HIS A 1 432 ? 7.478   5.831   18.776 1.00 23.83 ? 432  HIS A CG  1 
ATOM   3442 N ND1 . HIS A 1 432 ? 7.346   7.195   18.614 1.00 25.99 ? 432  HIS A ND1 1 
ATOM   3443 C CD2 . HIS A 1 432 ? 6.217   5.331   18.784 1.00 23.42 ? 432  HIS A CD2 1 
ATOM   3444 C CE1 . HIS A 1 432 ? 6.061   7.509   18.535 1.00 25.47 ? 432  HIS A CE1 1 
ATOM   3445 N NE2 . HIS A 1 432 ? 5.355   6.400   18.641 1.00 23.50 ? 432  HIS A NE2 1 
ATOM   3446 N N   . ASN A 1 433 ? 10.957  5.988   16.506 1.00 25.95 ? 433  ASN A N   1 
ATOM   3447 C CA  . ASN A 1 433 ? 11.433  6.917   15.489 1.00 27.63 ? 433  ASN A CA  1 
ATOM   3448 C C   . ASN A 1 433 ? 11.266  6.392   14.064 1.00 27.54 ? 433  ASN A C   1 
ATOM   3449 O O   . ASN A 1 433 ? 11.203  7.179   13.128 1.00 28.24 ? 433  ASN A O   1 
ATOM   3450 C CB  . ASN A 1 433 ? 12.894  7.315   15.773 1.00 28.09 ? 433  ASN A CB  1 
ATOM   3451 C CG  . ASN A 1 433 ? 13.030  8.157   17.018 1.00 30.83 ? 433  ASN A CG  1 
ATOM   3452 O OD1 . ASN A 1 433 ? 12.090  8.847   17.419 1.00 36.35 ? 433  ASN A OD1 1 
ATOM   3453 N ND2 . ASN A 1 433 ? 14.203  8.113   17.642 1.00 33.38 ? 433  ASN A ND2 1 
ATOM   3454 N N   . GLN A 1 434 ? 11.193  5.065   13.909 1.00 26.91 ? 434  GLN A N   1 
ATOM   3455 C CA  . GLN A 1 434 ? 10.972  4.391   12.618 1.00 27.42 ? 434  GLN A CA  1 
ATOM   3456 C C   . GLN A 1 434 ? 9.497   4.025   12.383 1.00 25.93 ? 434  GLN A C   1 
ATOM   3457 O O   . GLN A 1 434 ? 8.939   4.267   11.312 1.00 25.09 ? 434  GLN A O   1 
ATOM   3458 C CB  . GLN A 1 434 ? 11.827  3.115   12.532 1.00 26.80 ? 434  GLN A CB  1 
ATOM   3459 C CG  . GLN A 1 434 ? 13.337  3.315   12.766 1.00 30.67 ? 434  GLN A CG  1 
ATOM   3460 C CD  . GLN A 1 434 ? 14.086  2.008   13.021 1.00 30.94 ? 434  GLN A CD  1 
ATOM   3461 O OE1 . GLN A 1 434 ? 14.750  1.852   14.056 1.00 37.21 ? 434  GLN A OE1 1 
ATOM   3462 N NE2 . GLN A 1 434 ? 13.976  1.059   12.088 1.00 35.99 ? 434  GLN A NE2 1 
ATOM   3463 N N   . VAL A 1 435 ? 8.864   3.416   13.381 1.00 24.86 ? 435  VAL A N   1 
ATOM   3464 C CA  . VAL A 1 435 ? 7.483   2.933   13.239 1.00 23.38 ? 435  VAL A CA  1 
ATOM   3465 C C   . VAL A 1 435 ? 6.697   3.592   14.377 1.00 23.58 ? 435  VAL A C   1 
ATOM   3466 O O   . VAL A 1 435 ? 6.990   3.343   15.538 1.00 22.21 ? 435  VAL A O   1 
ATOM   3467 C CB  . VAL A 1 435 ? 7.409   1.379   13.349 1.00 23.36 ? 435  VAL A CB  1 
ATOM   3468 C CG1 . VAL A 1 435 ? 5.958   0.843   13.161 1.00 24.07 ? 435  VAL A CG1 1 
ATOM   3469 C CG2 . VAL A 1 435 ? 8.375   0.707   12.352 1.00 24.59 ? 435  VAL A CG2 1 
ATOM   3470 N N   . GLU A 1 436 ? 5.712   4.437   14.057 1.00 22.47 ? 436  GLU A N   1 
ATOM   3471 C CA  . GLU A 1 436 ? 5.105   5.257   15.106 1.00 22.67 ? 436  GLU A CA  1 
ATOM   3472 C C   . GLU A 1 436 ? 3.889   4.536   15.690 1.00 22.19 ? 436  GLU A C   1 
ATOM   3473 O O   . GLU A 1 436 ? 2.754   4.966   15.494 1.00 21.80 ? 436  GLU A O   1 
ATOM   3474 C CB  . GLU A 1 436 ? 4.702   6.620   14.567 1.00 23.62 ? 436  GLU A CB  1 
ATOM   3475 C CG  . GLU A 1 436 ? 5.885   7.530   14.287 1.00 29.11 ? 436  GLU A CG  1 
ATOM   3476 C CD  . GLU A 1 436 ? 5.462   8.976   14.007 1.00 37.41 ? 436  GLU A CD  1 
ATOM   3477 O OE1 . GLU A 1 436 ? 4.269   9.222   13.680 1.00 39.11 ? 436  GLU A OE1 1 
ATOM   3478 O OE2 . GLU A 1 436 ? 6.341   9.866   14.118 1.00 40.00 ? 436  GLU A OE2 1 
ATOM   3479 N N   . PHE A 1 437 ? 4.166   3.442   16.379 1.00 20.70 ? 437  PHE A N   1 
ATOM   3480 C CA  . PHE A 1 437 ? 3.147   2.580   17.017 1.00 19.90 ? 437  PHE A CA  1 
ATOM   3481 C C   . PHE A 1 437 ? 2.548   3.334   18.212 1.00 19.38 ? 437  PHE A C   1 
ATOM   3482 O O   . PHE A 1 437 ? 3.170   4.266   18.748 1.00 18.37 ? 437  PHE A O   1 
ATOM   3483 C CB  . PHE A 1 437 ? 3.784   1.239   17.445 1.00 19.91 ? 437  PHE A CB  1 
ATOM   3484 C CG  . PHE A 1 437 ? 4.958   1.405   18.376 1.00 17.56 ? 437  PHE A CG  1 
ATOM   3485 C CD1 . PHE A 1 437 ? 4.757   1.575   19.738 1.00 16.44 ? 437  PHE A CD1 1 
ATOM   3486 C CD2 . PHE A 1 437 ? 6.254   1.460   17.882 1.00 19.20 ? 437  PHE A CD2 1 
ATOM   3487 C CE1 . PHE A 1 437 ? 5.799   1.765   20.625 1.00 19.92 ? 437  PHE A CE1 1 
ATOM   3488 C CE2 . PHE A 1 437 ? 7.303   1.678   18.763 1.00 13.96 ? 437  PHE A CE2 1 
ATOM   3489 C CZ  . PHE A 1 437 ? 7.084   1.823   20.125 1.00 18.06 ? 437  PHE A CZ  1 
ATOM   3490 N N   . ASP A 1 438 ? 1.341   2.917   18.622 1.00 18.38 ? 438  ASP A N   1 
ATOM   3491 C CA  . ASP A 1 438 ? 0.543   3.623   19.626 1.00 17.63 ? 438  ASP A CA  1 
ATOM   3492 C C   . ASP A 1 438 ? 0.467   2.885   20.970 1.00 16.98 ? 438  ASP A C   1 
ATOM   3493 O O   . ASP A 1 438 ? 0.089   3.458   21.991 1.00 16.78 ? 438  ASP A O   1 
ATOM   3494 C CB  . ASP A 1 438 ? -0.878  3.781   19.089 1.00 17.20 ? 438  ASP A CB  1 
ATOM   3495 C CG  . ASP A 1 438 ? -0.923  4.635   17.857 1.00 17.01 ? 438  ASP A CG  1 
ATOM   3496 O OD1 . ASP A 1 438 ? -0.720  5.857   17.983 1.00 18.78 ? 438  ASP A OD1 1 
ATOM   3497 O OD2 . ASP A 1 438 ? -1.103  4.091   16.767 1.00 19.60 ? 438  ASP A OD2 1 
ATOM   3498 N N   . GLY A 1 439 ? 0.808   1.607   20.960 1.00 16.04 ? 439  GLY A N   1 
ATOM   3499 C CA  . GLY A 1 439 ? 0.708   0.789   22.171 1.00 15.82 ? 439  GLY A CA  1 
ATOM   3500 C C   . GLY A 1 439 ? 1.528   -0.471  21.953 1.00 15.68 ? 439  GLY A C   1 
ATOM   3501 O O   . GLY A 1 439 ? 1.976   -0.719  20.832 1.00 15.78 ? 439  GLY A O   1 
ATOM   3502 N N   . ILE A 1 440 ? 1.686   -1.254  23.016 1.00 15.79 ? 440  ILE A N   1 
ATOM   3503 C CA  . ILE A 1 440 ? 2.648   -2.356  23.044 1.00 15.59 ? 440  ILE A CA  1 
ATOM   3504 C C   . ILE A 1 440 ? 1.967   -3.598  23.586 1.00 16.03 ? 440  ILE A C   1 
ATOM   3505 O O   . ILE A 1 440 ? 1.260   -3.546  24.588 1.00 15.09 ? 440  ILE A O   1 
ATOM   3506 C CB  . ILE A 1 440 ? 3.847   -1.977  23.932 1.00 15.89 ? 440  ILE A CB  1 
ATOM   3507 C CG1 . ILE A 1 440 ? 4.480   -0.667  23.409 1.00 15.95 ? 440  ILE A CG1 1 
ATOM   3508 C CG2 . ILE A 1 440 ? 4.870   -3.134  23.974 1.00 18.90 ? 440  ILE A CG2 1 
ATOM   3509 C CD1 . ILE A 1 440 ? 5.397   0.031   24.452 1.00 17.23 ? 440  ILE A CD1 1 
ATOM   3510 N N   . TRP A 1 441 ? 2.207   -4.722  22.927 1.00 15.38 ? 441  TRP A N   1 
ATOM   3511 C CA  . TRP A 1 441 ? 1.660   -5.986  23.346 1.00 14.28 ? 441  TRP A CA  1 
ATOM   3512 C C   . TRP A 1 441 ? 2.858   -6.864  23.762 1.00 15.12 ? 441  TRP A C   1 
ATOM   3513 O O   . TRP A 1 441 ? 3.653   -7.228  22.922 1.00 14.05 ? 441  TRP A O   1 
ATOM   3514 C CB  . TRP A 1 441 ? 0.820   -6.526  22.184 1.00 15.12 ? 441  TRP A CB  1 
ATOM   3515 C CG  . TRP A 1 441 ? 0.542   -7.994  22.152 1.00 14.49 ? 441  TRP A CG  1 
ATOM   3516 C CD1 . TRP A 1 441 ? 0.525   -8.857  23.210 1.00 16.49 ? 441  TRP A CD1 1 
ATOM   3517 C CD2 . TRP A 1 441 ? 0.222   -8.759  20.997 1.00 17.49 ? 441  TRP A CD2 1 
ATOM   3518 N NE1 . TRP A 1 441 ? 0.212   -10.132 22.778 1.00 17.62 ? 441  TRP A NE1 1 
ATOM   3519 C CE2 . TRP A 1 441 ? 0.026   -10.096 21.420 1.00 17.24 ? 441  TRP A CE2 1 
ATOM   3520 C CE3 . TRP A 1 441 ? 0.056   -8.443  19.629 1.00 15.72 ? 441  TRP A CE3 1 
ATOM   3521 C CZ2 . TRP A 1 441 ? -0.331  -11.106 20.536 1.00 18.92 ? 441  TRP A CZ2 1 
ATOM   3522 C CZ3 . TRP A 1 441 ? -0.263  -9.452  18.757 1.00 16.78 ? 441  TRP A CZ3 1 
ATOM   3523 C CH2 . TRP A 1 441 ? -0.440  -10.773 19.210 1.00 17.15 ? 441  TRP A CH2 1 
ATOM   3524 N N   . ILE A 1 442 ? 3.004   -7.111  25.067 1.00 14.25 ? 442  ILE A N   1 
ATOM   3525 C CA  . ILE A 1 442 ? 4.168   -7.881  25.600 1.00 16.55 ? 442  ILE A CA  1 
ATOM   3526 C C   . ILE A 1 442 ? 3.722   -9.313  25.824 1.00 16.54 ? 442  ILE A C   1 
ATOM   3527 O O   . ILE A 1 442 ? 2.730   -9.586  26.532 1.00 17.16 ? 442  ILE A O   1 
ATOM   3528 C CB  . ILE A 1 442 ? 4.811   -7.230  26.852 1.00 15.57 ? 442  ILE A CB  1 
ATOM   3529 C CG1 . ILE A 1 442 ? 3.738   -6.958  27.937 1.00 15.92 ? 442  ILE A CG1 1 
ATOM   3530 C CG2 . ILE A 1 442 ? 5.459   -5.885  26.484 1.00 15.01 ? 442  ILE A CG2 1 
ATOM   3531 C CD1 . ILE A 1 442 ? 4.250   -6.446  29.254 1.00 16.46 ? 442  ILE A CD1 1 
ATOM   3532 N N   . ASP A 1 443 ? 4.420   -10.226 25.159 1.00 16.19 ? 443  ASP A N   1 
ATOM   3533 C CA  . ASP A 1 443 ? 4.001   -11.608 25.074 1.00 16.35 ? 443  ASP A CA  1 
ATOM   3534 C C   . ASP A 1 443 ? 5.176   -12.511 25.478 1.00 17.21 ? 443  ASP A C   1 
ATOM   3535 O O   . ASP A 1 443 ? 6.276   -12.018 25.672 1.00 16.51 ? 443  ASP A O   1 
ATOM   3536 C CB  . ASP A 1 443 ? 3.590   -11.863 23.626 1.00 15.96 ? 443  ASP A CB  1 
ATOM   3537 C CG  . ASP A 1 443 ? 2.993   -13.205 23.403 1.00 17.18 ? 443  ASP A CG  1 
ATOM   3538 O OD1 . ASP A 1 443 ? 2.342   -13.737 24.309 1.00 17.97 ? 443  ASP A OD1 1 
ATOM   3539 O OD2 . ASP A 1 443 ? 3.196   -13.736 22.292 1.00 19.80 ? 443  ASP A OD2 1 
ATOM   3540 N N   . MET A 1 444 ? 4.900   -13.803 25.647 1.00 16.92 ? 444  MET A N   1 
ATOM   3541 C CA  . MET A 1 444 ? 5.944   -14.815 25.913 1.00 17.65 ? 444  MET A CA  1 
ATOM   3542 C C   . MET A 1 444 ? 6.697   -14.475 27.189 1.00 17.21 ? 444  MET A C   1 
ATOM   3543 O O   . MET A 1 444 ? 7.882   -14.828 27.348 1.00 17.73 ? 444  MET A O   1 
ATOM   3544 C CB  . MET A 1 444 ? 6.941   -14.829 24.739 1.00 17.73 ? 444  MET A CB  1 
ATOM   3545 C CG  . MET A 1 444 ? 6.331   -15.127 23.395 1.00 18.88 ? 444  MET A CG  1 
ATOM   3546 S SD  . MET A 1 444 ? 5.511   -16.702 23.292 1.00 24.48 ? 444  MET A SD  1 
ATOM   3547 C CE  . MET A 1 444 ? 6.936   -17.799 23.152 1.00 22.79 ? 444  MET A CE  1 
ATOM   3548 N N   . ASN A 1 445 ? 6.036   -13.753 28.097 1.00 15.53 ? 445  ASN A N   1 
ATOM   3549 C CA  . ASN A 1 445 ? 6.728   -13.199 29.254 1.00 13.94 ? 445  ASN A CA  1 
ATOM   3550 C C   . ASN A 1 445 ? 6.503   -13.913 30.594 1.00 14.15 ? 445  ASN A C   1 
ATOM   3551 O O   . ASN A 1 445 ? 6.609   -13.316 31.666 1.00 13.22 ? 445  ASN A O   1 
ATOM   3552 C CB  . ASN A 1 445 ? 6.526   -11.681 29.339 1.00 14.70 ? 445  ASN A CB  1 
ATOM   3553 C CG  . ASN A 1 445 ? 5.038   -11.290 29.471 1.00 14.96 ? 445  ASN A CG  1 
ATOM   3554 O OD1 . ASN A 1 445 ? 4.147   -12.124 29.356 1.00 15.61 ? 445  ASN A OD1 1 
ATOM   3555 N ND2 . ASN A 1 445 ? 4.795   -10.034 29.744 1.00 14.87 ? 445  ASN A ND2 1 
ATOM   3556 N N   . GLU A 1 446 ? 6.261   -15.223 30.512 1.00 14.23 ? 446  GLU A N   1 
ATOM   3557 C CA  . GLU A 1 446 ? 6.195   -16.076 31.704 1.00 15.46 ? 446  GLU A CA  1 
ATOM   3558 C C   . GLU A 1 446 ? 7.479   -16.233 32.536 1.00 17.08 ? 446  GLU A C   1 
ATOM   3559 O O   . GLU A 1 446 ? 7.373   -16.304 33.736 1.00 18.18 ? 446  GLU A O   1 
ATOM   3560 C CB  . GLU A 1 446 ? 5.627   -17.453 31.368 1.00 14.02 ? 446  GLU A CB  1 
ATOM   3561 C CG  . GLU A 1 446 ? 4.122   -17.412 30.934 1.00 17.55 ? 446  GLU A CG  1 
ATOM   3562 C CD  . GLU A 1 446 ? 3.931   -16.805 29.567 1.00 22.94 ? 446  GLU A CD  1 
ATOM   3563 O OE1 . GLU A 1 446 ? 4.797   -17.009 28.655 1.00 20.87 ? 446  GLU A OE1 1 
ATOM   3564 O OE2 . GLU A 1 446 ? 2.925   -16.071 29.400 1.00 23.17 ? 446  GLU A OE2 1 
ATOM   3565 N N   . VAL A 1 447 ? 8.690   -16.304 31.981 1.00 19.30 ? 447  VAL A N   1 
ATOM   3566 C CA  . VAL A 1 447 ? 9.065   -16.166 30.588 1.00 20.78 ? 447  VAL A CA  1 
ATOM   3567 C C   . VAL A 1 447 ? 9.025   -17.526 29.847 1.00 21.51 ? 447  VAL A C   1 
ATOM   3568 O O   . VAL A 1 447 ? 9.270   -18.589 30.448 1.00 22.05 ? 447  VAL A O   1 
ATOM   3569 C CB  . VAL A 1 447 ? 10.448  -15.398 30.533 1.00 22.18 ? 447  VAL A CB  1 
ATOM   3570 C CG1 . VAL A 1 447 ? 11.593  -16.274 30.972 1.00 24.80 ? 447  VAL A CG1 1 
ATOM   3571 C CG2 . VAL A 1 447 ? 10.715  -14.801 29.166 1.00 23.89 ? 447  VAL A CG2 1 
ATOM   3572 N N   . SER A 1 448 ? 8.618   -17.496 28.576 1.00 20.12 ? 448  SER A N   1 
ATOM   3573 C CA  . SER A 1 448 ? 8.547   -18.669 27.716 1.00 20.73 ? 448  SER A CA  1 
ATOM   3574 C C   . SER A 1 448 ? 9.920   -18.924 27.052 1.00 20.59 ? 448  SER A C   1 
ATOM   3575 O O   . SER A 1 448 ? 10.563  -18.004 26.509 1.00 20.67 ? 448  SER A O   1 
ATOM   3576 C CB  . SER A 1 448 ? 7.436   -18.504 26.678 1.00 21.38 ? 448  SER A CB  1 
ATOM   3577 O OG  . SER A 1 448 ? 7.259   -19.684 25.892 1.00 23.05 ? 448  SER A OG  1 
ATOM   3578 N N   . ASN A 1 449 ? 10.370  -20.163 27.177 1.00 18.32 ? 449  ASN A N   1 
ATOM   3579 C CA  . ASN A 1 449 ? 11.636  -20.634 26.608 1.00 18.01 ? 449  ASN A CA  1 
ATOM   3580 C C   . ASN A 1 449 ? 11.314  -21.909 25.794 1.00 18.41 ? 449  ASN A C   1 
ATOM   3581 O O   . ASN A 1 449 ? 10.504  -22.762 26.240 1.00 17.75 ? 449  ASN A O   1 
ATOM   3582 C CB  . ASN A 1 449 ? 12.587  -20.915 27.772 1.00 17.86 ? 449  ASN A CB  1 
ATOM   3583 C CG  . ASN A 1 449 ? 14.057  -20.982 27.362 1.00 18.68 ? 449  ASN A CG  1 
ATOM   3584 O OD1 . ASN A 1 449 ? 14.399  -20.862 26.199 1.00 20.41 ? 449  ASN A OD1 1 
ATOM   3585 N ND2 . ASN A 1 449 ? 14.921  -21.185 28.344 1.00 18.75 ? 449  ASN A ND2 1 
ATOM   3586 N N   . PHE A 1 450 ? 11.878  -22.011 24.582 1.00 17.70 ? 450  PHE A N   1 
ATOM   3587 C CA  . PHE A 1 450 ? 11.625  -23.144 23.692 1.00 20.06 ? 450  PHE A CA  1 
ATOM   3588 C C   . PHE A 1 450 ? 12.512  -24.328 24.049 1.00 21.43 ? 450  PHE A C   1 
ATOM   3589 O O   . PHE A 1 450 ? 12.285  -25.439 23.580 1.00 23.30 ? 450  PHE A O   1 
ATOM   3590 C CB  . PHE A 1 450 ? 11.793  -22.776 22.201 1.00 19.57 ? 450  PHE A CB  1 
ATOM   3591 C CG  . PHE A 1 450 ? 10.736  -21.817 21.675 1.00 19.51 ? 450  PHE A CG  1 
ATOM   3592 C CD1 . PHE A 1 450 ? 9.587   -21.545 22.417 1.00 21.00 ? 450  PHE A CD1 1 
ATOM   3593 C CD2 . PHE A 1 450 ? 10.874  -21.230 20.421 1.00 22.28 ? 450  PHE A CD2 1 
ATOM   3594 C CE1 . PHE A 1 450 ? 8.605   -20.685 21.947 1.00 20.00 ? 450  PHE A CE1 1 
ATOM   3595 C CE2 . PHE A 1 450 ? 9.886   -20.353 19.939 1.00 22.55 ? 450  PHE A CE2 1 
ATOM   3596 C CZ  . PHE A 1 450 ? 8.751   -20.092 20.712 1.00 22.74 ? 450  PHE A CZ  1 
ATOM   3597 N N   . VAL A 1 451 ? 13.517  -24.073 24.878 1.00 21.53 ? 451  VAL A N   1 
ATOM   3598 C CA  . VAL A 1 451 ? 14.302  -25.122 25.514 1.00 22.05 ? 451  VAL A CA  1 
ATOM   3599 C C   . VAL A 1 451 ? 13.955  -25.128 27.009 1.00 22.34 ? 451  VAL A C   1 
ATOM   3600 O O   . VAL A 1 451 ? 13.425  -24.148 27.539 1.00 22.69 ? 451  VAL A O   1 
ATOM   3601 C CB  . VAL A 1 451 ? 15.833  -24.923 25.276 1.00 21.37 ? 451  VAL A CB  1 
ATOM   3602 C CG1 . VAL A 1 451 ? 16.155  -25.062 23.819 1.00 23.13 ? 451  VAL A CG1 1 
ATOM   3603 C CG2 . VAL A 1 451 ? 16.305  -23.568 25.772 1.00 21.38 ? 451  VAL A CG2 1 
ATOM   3604 N N   . ASP A 1 452 ? 14.214  -26.235 27.688 1.00 22.21 ? 452  ASP A N   1 
ATOM   3605 C CA  . ASP A 1 452 ? 13.887  -26.324 29.106 1.00 22.58 ? 452  ASP A CA  1 
ATOM   3606 C C   . ASP A 1 452 ? 15.056  -25.787 29.896 1.00 22.25 ? 452  ASP A C   1 
ATOM   3607 O O   . ASP A 1 452 ? 16.130  -26.411 29.925 1.00 22.75 ? 452  ASP A O   1 
ATOM   3608 C CB  . ASP A 1 452 ? 13.567  -27.767 29.496 1.00 22.53 ? 452  ASP A CB  1 
ATOM   3609 C CG  . ASP A 1 452 ? 12.266  -28.272 28.878 1.00 25.92 ? 452  ASP A CG  1 
ATOM   3610 O OD1 . ASP A 1 452 ? 11.365  -27.458 28.534 1.00 23.80 ? 452  ASP A OD1 1 
ATOM   3611 O OD2 . ASP A 1 452 ? 12.130  -29.507 28.763 1.00 29.25 ? 452  ASP A OD2 1 
ATOM   3612 N N   . GLY A 1 453 ? 14.893  -24.603 30.478 1.00 20.21 ? 453  GLY A N   1 
ATOM   3613 C CA  . GLY A 1 453 ? 15.932  -24.031 31.342 1.00 20.10 ? 453  GLY A CA  1 
ATOM   3614 C C   . GLY A 1 453 ? 16.885  -23.106 30.615 1.00 19.83 ? 453  GLY A C   1 
ATOM   3615 O O   . GLY A 1 453 ? 16.852  -21.909 30.776 1.00 18.31 ? 453  GLY A O   1 
ATOM   3616 N N   . SER A 1 454 ? 17.770  -23.693 29.815 1.00 20.66 ? 454  SER A N   1 
ATOM   3617 C CA  . SER A 1 454 ? 18.709  -22.941 29.013 1.00 20.79 ? 454  SER A CA  1 
ATOM   3618 C C   . SER A 1 454 ? 19.196  -23.922 27.922 1.00 21.11 ? 454  SER A C   1 
ATOM   3619 O O   . SER A 1 454 ? 18.846  -25.119 27.938 1.00 19.74 ? 454  SER A O   1 
ATOM   3620 C CB  . SER A 1 454 ? 19.873  -22.473 29.877 1.00 21.94 ? 454  SER A CB  1 
ATOM   3621 O OG  . SER A 1 454 ? 20.797  -23.560 30.055 1.00 23.77 ? 454  SER A OG  1 
ATOM   3622 N N   . VAL A 1 455 ? 19.959  -23.421 26.956 1.00 22.10 ? 455  VAL A N   1 
ATOM   3623 C CA  . VAL A 1 455 ? 20.418  -24.264 25.872 1.00 23.33 ? 455  VAL A CA  1 
ATOM   3624 C C   . VAL A 1 455 ? 21.326  -25.411 26.414 1.00 24.53 ? 455  VAL A C   1 
ATOM   3625 O O   . VAL A 1 455 ? 21.624  -26.383 25.704 1.00 25.33 ? 455  VAL A O   1 
ATOM   3626 C CB  . VAL A 1 455 ? 21.077  -23.417 24.722 1.00 23.97 ? 455  VAL A CB  1 
ATOM   3627 C CG1 . VAL A 1 455 ? 20.066  -22.483 24.088 1.00 23.10 ? 455  VAL A CG1 1 
ATOM   3628 C CG2 . VAL A 1 455 ? 22.322  -22.645 25.196 1.00 24.10 ? 455  VAL A CG2 1 
ATOM   3629 N N   . SER A 1 456 ? 21.739  -25.320 27.672 1.00 24.24 ? 456  SER A N   1 
ATOM   3630 C CA  . SER A 1 456 ? 22.529  -26.409 28.282 1.00 27.16 ? 456  SER A CA  1 
ATOM   3631 C C   . SER A 1 456 ? 21.797  -27.123 29.441 1.00 26.99 ? 456  SER A C   1 
ATOM   3632 O O   . SER A 1 456 ? 22.389  -27.836 30.259 1.00 28.04 ? 456  SER A O   1 
ATOM   3633 C CB  . SER A 1 456 ? 23.940  -25.901 28.635 1.00 26.50 ? 456  SER A CB  1 
ATOM   3634 O OG  . SER A 1 456 ? 23.851  -24.750 29.441 1.00 31.77 ? 456  SER A OG  1 
ATOM   3635 N N   . GLY A 1 457 ? 20.473  -26.973 29.466 1.00 26.10 ? 457  GLY A N   1 
ATOM   3636 C CA  . GLY A 1 457 ? 19.652  -27.571 30.514 1.00 26.16 ? 457  GLY A CA  1 
ATOM   3637 C C   . GLY A 1 457 ? 19.816  -26.850 31.836 1.00 26.09 ? 457  GLY A C   1 
ATOM   3638 O O   . GLY A 1 457 ? 20.137  -25.658 31.864 1.00 25.76 ? 457  GLY A O   1 
ATOM   3639 N N   . CYS A 1 458 ? 19.585  -27.578 32.928 1.00 26.01 ? 458  CYS A N   1 
ATOM   3640 C CA  . CYS A 1 458 ? 19.627  -27.051 34.294 1.00 26.09 ? 458  CYS A CA  1 
ATOM   3641 C C   . CYS A 1 458 ? 20.408  -28.001 35.162 1.00 25.50 ? 458  CYS A C   1 
ATOM   3642 O O   . CYS A 1 458 ? 20.163  -29.193 35.098 1.00 26.73 ? 458  CYS A O   1 
ATOM   3643 C CB  . CYS A 1 458 ? 18.224  -27.047 34.901 1.00 26.33 ? 458  CYS A CB  1 
ATOM   3644 S SG  . CYS A 1 458 ? 17.084  -26.061 34.002 1.00 30.43 ? 458  CYS A SG  1 
ATOM   3645 N N   . SER A 1 459 ? 21.276  -27.478 36.018 1.00 25.31 ? 459  SER A N   1 
ATOM   3646 C CA  . SER A 1 459 ? 21.962  -28.332 37.005 1.00 26.30 ? 459  SER A CA  1 
ATOM   3647 C C   . SER A 1 459 ? 20.985  -28.984 37.980 1.00 25.80 ? 459  SER A C   1 
ATOM   3648 O O   . SER A 1 459 ? 19.975  -28.380 38.355 1.00 25.13 ? 459  SER A O   1 
ATOM   3649 C CB  . SER A 1 459 ? 22.965  -27.513 37.815 1.00 26.47 ? 459  SER A CB  1 
ATOM   3650 O OG  . SER A 1 459 ? 23.848  -26.831 36.945 1.00 29.96 ? 459  SER A OG  1 
ATOM   3651 N N   . THR A 1 460 ? 21.303  -30.204 38.411 1.00 24.71 ? 460  THR A N   1 
ATOM   3652 C CA  . THR A 1 460 ? 20.544  -30.881 39.463 1.00 24.40 ? 460  THR A CA  1 
ATOM   3653 C C   . THR A 1 460 ? 20.905  -30.204 40.784 1.00 23.61 ? 460  THR A C   1 
ATOM   3654 O O   . THR A 1 460 ? 22.076  -30.175 41.184 1.00 24.29 ? 460  THR A O   1 
ATOM   3655 C CB  . THR A 1 460 ? 20.822  -32.431 39.470 1.00 24.62 ? 460  THR A CB  1 
ATOM   3656 O OG1 . THR A 1 460 ? 20.458  -32.993 38.192 1.00 24.03 ? 460  THR A OG1 1 
ATOM   3657 C CG2 . THR A 1 460 ? 20.023  -33.136 40.569 1.00 25.40 ? 460  THR A CG2 1 
ATOM   3658 N N   . ASN A 1 461 ? 19.907  -29.586 41.439 1.00 21.48 ? 461  ASN A N   1 
ATOM   3659 C CA  . ASN A 1 461 ? 20.109  -28.950 42.734 1.00 19.23 ? 461  ASN A CA  1 
ATOM   3660 C C   . ASN A 1 461 ? 18.705  -28.713 43.344 1.00 19.64 ? 461  ASN A C   1 
ATOM   3661 O O   . ASN A 1 461 ? 17.700  -29.029 42.682 1.00 17.45 ? 461  ASN A O   1 
ATOM   3662 C CB  . ASN A 1 461 ? 20.931  -27.651 42.612 1.00 19.39 ? 461  ASN A CB  1 
ATOM   3663 C CG  . ASN A 1 461 ? 20.285  -26.607 41.679 1.00 20.83 ? 461  ASN A CG  1 
ATOM   3664 O OD1 . ASN A 1 461 ? 19.076  -26.337 41.771 1.00 19.57 ? 461  ASN A OD1 1 
ATOM   3665 N ND2 . ASN A 1 461 ? 21.080  -26.016 40.799 1.00 19.37 ? 461  ASN A ND2 1 
ATOM   3666 N N   . ASN A 1 462 ? 18.647  -28.192 44.568 1.00 18.10 ? 462  ASN A N   1 
ATOM   3667 C CA  . ASN A 1 462 ? 17.365  -28.042 45.288 1.00 20.46 ? 462  ASN A CA  1 
ATOM   3668 C C   . ASN A 1 462 ? 16.407  -26.995 44.663 1.00 19.56 ? 462  ASN A C   1 
ATOM   3669 O O   . ASN A 1 462 ? 15.205  -26.959 45.015 1.00 20.28 ? 462  ASN A O   1 
ATOM   3670 C CB  . ASN A 1 462 ? 17.619  -27.717 46.766 1.00 21.01 ? 462  ASN A CB  1 
ATOM   3671 C CG  . ASN A 1 462 ? 18.296  -26.366 46.971 1.00 27.00 ? 462  ASN A CG  1 
ATOM   3672 O OD1 . ASN A 1 462 ? 19.413  -26.122 46.474 1.00 32.56 ? 462  ASN A OD1 1 
ATOM   3673 N ND2 . ASN A 1 462 ? 17.638  -25.478 47.733 1.00 31.42 ? 462  ASN A ND2 1 
ATOM   3674 N N   . LEU A 1 463 ? 16.938  -26.125 43.814 1.00 19.43 ? 463  LEU A N   1 
ATOM   3675 C CA  . LEU A 1 463 ? 16.131  -25.084 43.111 1.00 19.79 ? 463  LEU A CA  1 
ATOM   3676 C C   . LEU A 1 463 ? 15.505  -25.674 41.869 1.00 20.04 ? 463  LEU A C   1 
ATOM   3677 O O   . LEU A 1 463 ? 14.293  -25.577 41.675 1.00 19.07 ? 463  LEU A O   1 
ATOM   3678 C CB  . LEU A 1 463 ? 16.966  -23.841 42.754 1.00 18.87 ? 463  LEU A CB  1 
ATOM   3679 C CG  . LEU A 1 463 ? 17.545  -23.075 43.952 1.00 21.04 ? 463  LEU A CG  1 
ATOM   3680 C CD1 . LEU A 1 463 ? 17.976  -21.697 43.508 1.00 20.19 ? 463  LEU A CD1 1 
ATOM   3681 C CD2 . LEU A 1 463 ? 16.549  -22.926 45.099 1.00 23.45 ? 463  LEU A CD2 1 
ATOM   3682 N N   . ASN A 1 464 ? 16.316  -26.338 41.040 1.00 18.66 ? 464  ASN A N   1 
ATOM   3683 C CA  . ASN A 1 464 ? 15.748  -26.958 39.821 1.00 20.20 ? 464  ASN A CA  1 
ATOM   3684 C C   . ASN A 1 464 ? 14.951  -28.216 40.084 1.00 19.44 ? 464  ASN A C   1 
ATOM   3685 O O   . ASN A 1 464 ? 14.083  -28.583 39.317 1.00 19.89 ? 464  ASN A O   1 
ATOM   3686 C CB  . ASN A 1 464 ? 16.841  -27.240 38.794 1.00 19.34 ? 464  ASN A CB  1 
ATOM   3687 C CG  . ASN A 1 464 ? 17.443  -26.008 38.265 1.00 21.87 ? 464  ASN A CG  1 
ATOM   3688 O OD1 . ASN A 1 464 ? 18.677  -25.899 38.160 1.00 25.41 ? 464  ASN A OD1 1 
ATOM   3689 N ND2 . ASN A 1 464 ? 16.597  -25.041 37.914 1.00 19.73 ? 464  ASN A ND2 1 
ATOM   3690 N N   . ASN A 1 465 ? 15.263  -28.852 41.202 1.00 19.93 ? 465  ASN A N   1 
ATOM   3691 C CA  . ASN A 1 465 ? 14.703  -30.144 41.594 1.00 20.13 ? 465  ASN A CA  1 
ATOM   3692 C C   . ASN A 1 465 ? 14.367  -30.097 43.075 1.00 19.88 ? 465  ASN A C   1 
ATOM   3693 O O   . ASN A 1 465 ? 15.045  -30.688 43.914 1.00 18.56 ? 465  ASN A O   1 
ATOM   3694 C CB  . ASN A 1 465 ? 15.708  -31.274 41.259 1.00 21.86 ? 465  ASN A CB  1 
ATOM   3695 C CG  . ASN A 1 465 ? 16.020  -31.316 39.784 1.00 21.69 ? 465  ASN A CG  1 
ATOM   3696 O OD1 . ASN A 1 465 ? 15.271  -31.904 39.006 1.00 26.09 ? 465  ASN A OD1 1 
ATOM   3697 N ND2 . ASN A 1 465 ? 17.076  -30.630 39.380 1.00 22.66 ? 465  ASN A ND2 1 
ATOM   3698 N N   . PRO A 1 466 ? 13.282  -29.381 43.422 1.00 18.76 ? 466  PRO A N   1 
ATOM   3699 C CA  . PRO A 1 466 ? 13.020  -29.208 44.850 1.00 18.58 ? 466  PRO A CA  1 
ATOM   3700 C C   . PRO A 1 466 ? 12.416  -30.452 45.525 1.00 18.08 ? 466  PRO A C   1 
ATOM   3701 O O   . PRO A 1 466 ? 12.003  -31.382 44.832 1.00 18.60 ? 466  PRO A O   1 
ATOM   3702 C CB  . PRO A 1 466 ? 12.064  -27.976 44.865 1.00 16.73 ? 466  PRO A CB  1 
ATOM   3703 C CG  . PRO A 1 466 ? 11.262  -28.173 43.578 1.00 18.86 ? 466  PRO A CG  1 
ATOM   3704 C CD  . PRO A 1 466 ? 12.299  -28.680 42.569 1.00 18.79 ? 466  PRO A CD  1 
ATOM   3705 N N   . PRO A 1 467 ? 12.388  -30.488 46.877 1.00 19.11 ? 467  PRO A N   1 
ATOM   3706 C CA  . PRO A 1 467 ? 11.843  -31.637 47.614 1.00 19.02 ? 467  PRO A CA  1 
ATOM   3707 C C   . PRO A 1 467 ? 10.363  -31.919 47.300 1.00 19.56 ? 467  PRO A C   1 
ATOM   3708 O O   . PRO A 1 467 ? 9.950   -33.081 47.207 1.00 19.59 ? 467  PRO A O   1 
ATOM   3709 C CB  . PRO A 1 467 ? 12.056  -31.259 49.080 1.00 19.26 ? 467  PRO A CB  1 
ATOM   3710 C CG  . PRO A 1 467 ? 12.395  -29.822 49.092 1.00 19.68 ? 467  PRO A CG  1 
ATOM   3711 C CD  . PRO A 1 467 ? 12.936  -29.450 47.772 1.00 18.69 ? 467  PRO A CD  1 
ATOM   3712 N N   . PHE A 1 468 ? 9.575   -30.854 47.128 1.00 19.65 ? 468  PHE A N   1 
ATOM   3713 C CA  . PHE A 1 468 ? 8.188   -30.986 46.696 1.00 18.76 ? 468  PHE A CA  1 
ATOM   3714 C C   . PHE A 1 468 ? 7.933   -30.119 45.450 1.00 18.14 ? 468  PHE A C   1 
ATOM   3715 O O   . PHE A 1 468 ? 8.366   -28.960 45.380 1.00 18.70 ? 468  PHE A O   1 
ATOM   3716 C CB  . PHE A 1 468 ? 7.242   -30.518 47.807 1.00 18.64 ? 468  PHE A CB  1 
ATOM   3717 C CG  . PHE A 1 468 ? 5.790   -30.557 47.400 1.00 18.72 ? 468  PHE A CG  1 
ATOM   3718 C CD1 . PHE A 1 468 ? 5.107   -31.764 47.379 1.00 20.25 ? 468  PHE A CD1 1 
ATOM   3719 C CD2 . PHE A 1 468 ? 5.125   -29.395 46.996 1.00 18.28 ? 468  PHE A CD2 1 
ATOM   3720 C CE1 . PHE A 1 468 ? 3.753   -31.824 46.997 1.00 19.69 ? 468  PHE A CE1 1 
ATOM   3721 C CE2 . PHE A 1 468 ? 3.780   -29.441 46.591 1.00 16.93 ? 468  PHE A CE2 1 
ATOM   3722 C CZ  . PHE A 1 468 ? 3.095   -30.647 46.608 1.00 19.33 ? 468  PHE A CZ  1 
ATOM   3723 N N   . THR A 1 469 ? 7.267   -30.694 44.455 1.00 18.00 ? 469  THR A N   1 
ATOM   3724 C CA  . THR A 1 469 ? 6.895   -29.963 43.256 1.00 17.71 ? 469  THR A CA  1 
ATOM   3725 C C   . THR A 1 469 ? 5.367   -29.963 43.187 1.00 17.70 ? 469  THR A C   1 
ATOM   3726 O O   . THR A 1 469 ? 4.763   -31.028 43.154 1.00 17.09 ? 469  THR A O   1 
ATOM   3727 C CB  . THR A 1 469 ? 7.503   -30.613 41.977 1.00 19.83 ? 469  THR A CB  1 
ATOM   3728 O OG1 . THR A 1 469 ? 8.935   -30.720 42.136 1.00 19.97 ? 469  THR A OG1 1 
ATOM   3729 C CG2 . THR A 1 469 ? 7.190   -29.726 40.736 1.00 18.44 ? 469  THR A CG2 1 
ATOM   3730 N N   . PRO A 1 470 ? 4.742   -28.759 43.184 1.00 17.84 ? 470  PRO A N   1 
ATOM   3731 C CA  . PRO A 1 470 ? 3.286   -28.670 42.994 1.00 19.15 ? 470  PRO A CA  1 
ATOM   3732 C C   . PRO A 1 470 ? 2.946   -29.323 41.655 1.00 18.57 ? 470  PRO A C   1 
ATOM   3733 O O   . PRO A 1 470 ? 3.842   -29.507 40.831 1.00 20.03 ? 470  PRO A O   1 
ATOM   3734 C CB  . PRO A 1 470 ? 3.014   -27.151 42.948 1.00 18.57 ? 470  PRO A CB  1 
ATOM   3735 C CG  . PRO A 1 470 ? 4.211   -26.514 43.593 1.00 20.30 ? 470  PRO A CG  1 
ATOM   3736 C CD  . PRO A 1 470 ? 5.387   -27.435 43.309 1.00 17.91 ? 470  PRO A CD  1 
ATOM   3737 N N   . ARG A 1 471 ? 1.681   -29.676 41.428 1.00 19.51 ? 471  ARG A N   1 
ATOM   3738 C CA  . ARG A 1 471 ? 1.300   -30.376 40.195 1.00 19.36 ? 471  ARG A CA  1 
ATOM   3739 C C   . ARG A 1 471 ? 1.242   -29.477 38.944 1.00 18.77 ? 471  ARG A C   1 
ATOM   3740 O O   . ARG A 1 471 ? 0.260   -29.466 38.213 1.00 18.05 ? 471  ARG A O   1 
ATOM   3741 C CB  . ARG A 1 471 ? -0.028  -31.126 40.393 1.00 19.81 ? 471  ARG A CB  1 
ATOM   3742 C CG  . ARG A 1 471 ? -1.213  -30.229 40.739 1.00 23.12 ? 471  ARG A CG  1 
ATOM   3743 C CD  . ARG A 1 471 ? -2.481  -31.039 40.766 1.00 28.21 ? 471  ARG A CD  1 
ATOM   3744 N NE  . ARG A 1 471 ? -2.422  -32.060 41.807 1.00 29.66 ? 471  ARG A NE  1 
ATOM   3745 C CZ  . ARG A 1 471 ? -3.389  -32.941 42.049 1.00 32.62 ? 471  ARG A CZ  1 
ATOM   3746 N NH1 . ARG A 1 471 ? -4.504  -32.935 41.307 1.00 32.20 ? 471  ARG A NH1 1 
ATOM   3747 N NH2 . ARG A 1 471 ? -3.234  -33.832 43.031 1.00 32.76 ? 471  ARG A NH2 1 
ATOM   3748 N N   . ILE A 1 472 ? 2.322   -28.751 38.689 1.00 17.76 ? 472  ILE A N   1 
ATOM   3749 C CA  . ILE A 1 472 ? 2.449   -27.954 37.492 1.00 17.50 ? 472  ILE A CA  1 
ATOM   3750 C C   . ILE A 1 472 ? 2.590   -28.814 36.240 1.00 18.21 ? 472  ILE A C   1 
ATOM   3751 O O   . ILE A 1 472 ? 3.040   -29.979 36.302 1.00 17.13 ? 472  ILE A O   1 
ATOM   3752 C CB  . ILE A 1 472 ? 3.658   -26.989 37.575 1.00 16.59 ? 472  ILE A CB  1 
ATOM   3753 C CG1 . ILE A 1 472 ? 4.967   -27.773 37.719 1.00 19.26 ? 472  ILE A CG1 1 
ATOM   3754 C CG2 . ILE A 1 472 ? 3.500   -25.991 38.739 1.00 16.27 ? 472  ILE A CG2 1 
ATOM   3755 C CD1 . ILE A 1 472 ? 6.112   -26.923 37.516 1.00 19.81 ? 472  ILE A CD1 1 
ATOM   3756 N N   . LEU A 1 473 ? 2.168   -28.251 35.111 1.00 18.01 ? 473  LEU A N   1 
ATOM   3757 C CA  . LEU A 1 473 ? 2.251   -28.956 33.848 1.00 18.28 ? 473  LEU A CA  1 
ATOM   3758 C C   . LEU A 1 473 ? 3.680   -29.466 33.614 1.00 17.60 ? 473  LEU A C   1 
ATOM   3759 O O   . LEU A 1 473 ? 4.627   -28.701 33.742 1.00 17.89 ? 473  LEU A O   1 
ATOM   3760 C CB  . LEU A 1 473 ? 1.812   -28.026 32.732 1.00 18.19 ? 473  LEU A CB  1 
ATOM   3761 C CG  . LEU A 1 473 ? 1.815   -28.634 31.328 1.00 19.72 ? 473  LEU A CG  1 
ATOM   3762 C CD1 . LEU A 1 473 ? 0.999   -29.899 31.180 1.00 21.62 ? 473  LEU A CD1 1 
ATOM   3763 C CD2 . LEU A 1 473 ? 1.355   -27.581 30.346 1.00 18.49 ? 473  LEU A CD2 1 
ATOM   3764 N N   . ASP A 1 474 ? 3.802   -30.764 33.331 1.00 18.29 ? 474  ASP A N   1 
ATOM   3765 C CA  . ASP A 1 474 ? 5.085   -31.464 33.065 1.00 20.51 ? 474  ASP A CA  1 
ATOM   3766 C C   . ASP A 1 474 ? 5.917   -31.819 34.277 1.00 20.28 ? 474  ASP A C   1 
ATOM   3767 O O   . ASP A 1 474 ? 6.928   -32.562 34.147 1.00 21.50 ? 474  ASP A O   1 
ATOM   3768 C CB  . ASP A 1 474 ? 5.957   -30.721 32.037 1.00 20.41 ? 474  ASP A CB  1 
ATOM   3769 C CG  . ASP A 1 474 ? 5.273   -30.583 30.692 1.00 25.37 ? 474  ASP A CG  1 
ATOM   3770 O OD1 . ASP A 1 474 ? 4.650   -31.571 30.226 1.00 28.11 ? 474  ASP A OD1 1 
ATOM   3771 O OD2 . ASP A 1 474 ? 5.343   -29.483 30.100 1.00 28.06 ? 474  ASP A OD2 1 
ATOM   3772 N N   . GLY A 1 475 ? 5.534   -31.295 35.437 1.00 19.55 ? 475  GLY A N   1 
ATOM   3773 C CA  . GLY A 1 475 ? 6.158   -31.687 36.702 1.00 19.39 ? 475  GLY A CA  1 
ATOM   3774 C C   . GLY A 1 475 ? 7.576   -31.223 36.993 1.00 18.98 ? 475  GLY A C   1 
ATOM   3775 O O   . GLY A 1 475 ? 8.186   -31.694 37.948 1.00 19.02 ? 475  GLY A O   1 
ATOM   3776 N N   . TYR A 1 476 ? 8.108   -30.306 36.194 1.00 17.79 ? 476  TYR A N   1 
ATOM   3777 C CA  . TYR A 1 476 ? 9.396   -29.699 36.496 1.00 18.29 ? 476  TYR A CA  1 
ATOM   3778 C C   . TYR A 1 476 ? 9.255   -28.215 36.360 1.00 18.00 ? 476  TYR A C   1 
ATOM   3779 O O   . TYR A 1 476 ? 8.654   -27.741 35.395 1.00 17.29 ? 476  TYR A O   1 
ATOM   3780 C CB  . TYR A 1 476 ? 10.487  -30.164 35.519 1.00 20.39 ? 476  TYR A CB  1 
ATOM   3781 C CG  . TYR A 1 476 ? 10.800  -31.641 35.643 1.00 21.10 ? 476  TYR A CG  1 
ATOM   3782 C CD1 . TYR A 1 476 ? 11.948  -32.073 36.309 1.00 22.77 ? 476  TYR A CD1 1 
ATOM   3783 C CD2 . TYR A 1 476 ? 9.942   -32.602 35.099 1.00 23.38 ? 476  TYR A CD2 1 
ATOM   3784 C CE1 . TYR A 1 476 ? 12.228  -33.425 36.436 1.00 23.89 ? 476  TYR A CE1 1 
ATOM   3785 C CE2 . TYR A 1 476 ? 10.221  -33.973 35.223 1.00 24.61 ? 476  TYR A CE2 1 
ATOM   3786 C CZ  . TYR A 1 476 ? 11.357  -34.361 35.882 1.00 24.36 ? 476  TYR A CZ  1 
ATOM   3787 O OH  . TYR A 1 476 ? 11.632  -35.706 36.001 1.00 25.21 ? 476  TYR A OH  1 
ATOM   3788 N N   . LEU A 1 477 ? 9.798   -27.480 37.322 1.00 18.48 ? 477  LEU A N   1 
ATOM   3789 C CA  . LEU A 1 477 ? 9.691   -25.992 37.331 1.00 18.05 ? 477  LEU A CA  1 
ATOM   3790 C C   . LEU A 1 477 ? 10.290  -25.344 36.093 1.00 18.53 ? 477  LEU A C   1 
ATOM   3791 O O   . LEU A 1 477 ? 9.749   -24.375 35.553 1.00 17.08 ? 477  LEU A O   1 
ATOM   3792 C CB  . LEU A 1 477 ? 10.366  -25.424 38.575 1.00 17.60 ? 477  LEU A CB  1 
ATOM   3793 C CG  . LEU A 1 477 ? 9.776   -25.804 39.926 1.00 19.36 ? 477  LEU A CG  1 
ATOM   3794 C CD1 . LEU A 1 477 ? 10.650  -25.191 41.009 1.00 18.19 ? 477  LEU A CD1 1 
ATOM   3795 C CD2 . LEU A 1 477 ? 8.320   -25.275 40.045 1.00 17.15 ? 477  LEU A CD2 1 
ATOM   3796 N N   . PHE A 1 478 ? 11.407  -25.897 35.605 1.00 18.07 ? 478  PHE A N   1 
ATOM   3797 C CA  . PHE A 1 478 ? 12.100  -25.234 34.511 1.00 17.36 ? 478  PHE A CA  1 
ATOM   3798 C C   . PHE A 1 478 ? 11.566  -25.582 33.144 1.00 17.83 ? 478  PHE A C   1 
ATOM   3799 O O   . PHE A 1 478 ? 12.087  -25.107 32.168 1.00 18.03 ? 478  PHE A O   1 
ATOM   3800 C CB  . PHE A 1 478 ? 13.575  -25.563 34.589 1.00 18.63 ? 478  PHE A CB  1 
ATOM   3801 C CG  . PHE A 1 478 ? 13.822  -27.020 34.685 1.00 17.43 ? 478  PHE A CG  1 
ATOM   3802 C CD1 . PHE A 1 478 ? 13.728  -27.820 33.553 1.00 21.20 ? 478  PHE A CD1 1 
ATOM   3803 C CD2 . PHE A 1 478 ? 14.095  -27.615 35.918 1.00 20.06 ? 478  PHE A CD2 1 
ATOM   3804 C CE1 . PHE A 1 478 ? 13.926  -29.200 33.636 1.00 18.19 ? 478  PHE A CE1 1 
ATOM   3805 C CE2 . PHE A 1 478 ? 14.306  -28.998 36.004 1.00 18.65 ? 478  PHE A CE2 1 
ATOM   3806 C CZ  . PHE A 1 478 ? 14.228  -29.774 34.858 1.00 19.56 ? 478  PHE A CZ  1 
ATOM   3807 N N   . CYS A 1 479 ? 10.542  -26.427 33.049 1.00 19.60 ? 479  CYS A N   1 
ATOM   3808 C CA  A CYS A 1 479 ? 9.942   -26.775 31.765 0.50 19.72 ? 479  CYS A CA  1 
ATOM   3809 C CA  B CYS A 1 479 ? 9.955   -26.760 31.740 0.50 19.27 ? 479  CYS A CA  1 
ATOM   3810 C C   . CYS A 1 479 ? 9.451   -25.534 31.007 1.00 19.28 ? 479  CYS A C   1 
ATOM   3811 O O   . CYS A 1 479 ? 8.686   -24.745 31.556 1.00 19.00 ? 479  CYS A O   1 
ATOM   3812 C CB  A CYS A 1 479 ? 8.779   -27.745 31.999 0.50 20.01 ? 479  CYS A CB  1 
ATOM   3813 C CB  B CYS A 1 479 ? 8.814   -27.769 31.875 0.50 19.42 ? 479  CYS A CB  1 
ATOM   3814 S SG  A CYS A 1 479 ? 8.088   -28.373 30.515 0.50 23.96 ? 479  CYS A SG  1 
ATOM   3815 S SG  B CYS A 1 479 ? 9.427   -29.386 32.221 0.50 20.91 ? 479  CYS A SG  1 
ATOM   3816 N N   . LYS A 1 480 ? 9.903   -25.382 29.757 1.00 19.21 ? 480  LYS A N   1 
ATOM   3817 C CA  . LYS A 1 480 ? 9.546   -24.239 28.901 1.00 19.38 ? 480  LYS A CA  1 
ATOM   3818 C C   . LYS A 1 480 ? 9.760   -22.869 29.547 1.00 18.87 ? 480  LYS A C   1 
ATOM   3819 O O   . LYS A 1 480 ? 9.031   -21.905 29.263 1.00 17.11 ? 480  LYS A O   1 
ATOM   3820 C CB  . LYS A 1 480 ? 8.099   -24.390 28.366 1.00 20.80 ? 480  LYS A CB  1 
ATOM   3821 C CG  . LYS A 1 480 ? 7.860   -25.658 27.529 1.00 23.95 ? 480  LYS A CG  1 
ATOM   3822 C CD  . LYS A 1 480 ? 8.919   -25.899 26.441 1.00 28.52 ? 480  LYS A CD  1 
ATOM   3823 C CE  . LYS A 1 480 ? 8.772   -27.309 25.846 1.00 29.66 ? 480  LYS A CE  1 
ATOM   3824 N NZ  . LYS A 1 480 ? 10.103  -27.882 25.430 1.00 35.91 ? 480  LYS A NZ  1 
ATOM   3825 N N   . THR A 1 481 ? 10.753  -22.779 30.428 1.00 16.71 ? 481  THR A N   1 
ATOM   3826 C CA  . THR A 1 481 ? 11.086  -21.490 31.038 1.00 16.67 ? 481  THR A CA  1 
ATOM   3827 C C   . THR A 1 481 ? 12.573  -21.456 31.367 1.00 17.45 ? 481  THR A C   1 
ATOM   3828 O O   . THR A 1 481 ? 13.333  -22.237 30.783 1.00 17.50 ? 481  THR A O   1 
ATOM   3829 C CB  . THR A 1 481 ? 10.134  -21.054 32.235 1.00 16.04 ? 481  THR A CB  1 
ATOM   3830 O OG1 . THR A 1 481 ? 10.397  -19.692 32.551 1.00 16.51 ? 481  THR A OG1 1 
ATOM   3831 C CG2 . THR A 1 481 ? 10.334  -21.897 33.465 1.00 14.41 ? 481  THR A CG2 1 
ATOM   3832 N N   . LEU A 1 482 ? 12.990  -20.537 32.243 1.00 18.33 ? 482  LEU A N   1 
ATOM   3833 C CA  . LEU A 1 482 ? 14.394  -20.404 32.653 1.00 18.61 ? 482  LEU A CA  1 
ATOM   3834 C C   . LEU A 1 482 ? 14.782  -21.338 33.811 1.00 19.36 ? 482  LEU A C   1 
ATOM   3835 O O   . LEU A 1 482 ? 13.926  -21.757 34.593 1.00 18.66 ? 482  LEU A O   1 
ATOM   3836 C CB  . LEU A 1 482 ? 14.707  -18.949 33.029 1.00 18.11 ? 482  LEU A CB  1 
ATOM   3837 C CG  . LEU A 1 482 ? 14.321  -17.849 32.058 1.00 21.00 ? 482  LEU A CG  1 
ATOM   3838 C CD1 . LEU A 1 482 ? 14.849  -16.468 32.496 1.00 19.46 ? 482  LEU A CD1 1 
ATOM   3839 C CD2 . LEU A 1 482 ? 14.827  -18.193 30.652 1.00 20.32 ? 482  LEU A CD2 1 
ATOM   3840 N N   . CYS A 1 483 ? 16.080  -21.687 33.902 1.00 18.86 ? 483  CYS A N   1 
ATOM   3841 C CA  . CYS A 1 483 ? 16.607  -22.385 35.063 1.00 19.31 ? 483  CYS A CA  1 
ATOM   3842 C C   . CYS A 1 483 ? 16.182  -21.679 36.352 1.00 18.86 ? 483  CYS A C   1 
ATOM   3843 O O   . CYS A 1 483 ? 16.188  -20.442 36.422 1.00 18.46 ? 483  CYS A O   1 
ATOM   3844 C CB  . CYS A 1 483 ? 18.142  -22.360 35.029 1.00 20.98 ? 483  CYS A CB  1 
ATOM   3845 S SG  . CYS A 1 483 ? 18.787  -23.262 33.612 1.00 28.76 ? 483  CYS A SG  1 
ATOM   3846 N N   . MET A 1 484 ? 15.823  -22.462 37.369 1.00 17.91 ? 484  MET A N   1 
ATOM   3847 C CA  . MET A 1 484 ? 15.388  -21.863 38.658 1.00 17.75 ? 484  MET A CA  1 
ATOM   3848 C C   . MET A 1 484 ? 16.546  -21.250 39.436 1.00 17.56 ? 484  MET A C   1 
ATOM   3849 O O   . MET A 1 484 ? 16.327  -20.472 40.369 1.00 16.74 ? 484  MET A O   1 
ATOM   3850 C CB  . MET A 1 484 ? 14.693  -22.876 39.552 1.00 16.94 ? 484  MET A CB  1 
ATOM   3851 C CG  . MET A 1 484 ? 13.343  -23.383 39.030 1.00 15.76 ? 484  MET A CG  1 
ATOM   3852 S SD  . MET A 1 484 ? 12.140  -21.970 38.938 1.00 18.40 ? 484  MET A SD  1 
ATOM   3853 C CE  . MET A 1 484 ? 11.966  -21.824 37.193 1.00 14.06 ? 484  MET A CE  1 
ATOM   3854 N N   . ASP A 1 485 ? 17.783  -21.622 39.091 1.00 18.49 ? 485  ASP A N   1 
ATOM   3855 C CA  . ASP A 1 485 ? 18.905  -20.977 39.748 1.00 18.67 ? 485  ASP A CA  1 
ATOM   3856 C C   . ASP A 1 485 ? 19.488  -19.806 38.949 1.00 19.60 ? 485  ASP A C   1 
ATOM   3857 O O   . ASP A 1 485 ? 20.555  -19.276 39.320 1.00 18.79 ? 485  ASP A O   1 
ATOM   3858 C CB  . ASP A 1 485 ? 20.004  -21.997 40.123 1.00 19.76 ? 485  ASP A CB  1 
ATOM   3859 C CG  . ASP A 1 485 ? 20.445  -22.888 38.954 1.00 20.05 ? 485  ASP A CG  1 
ATOM   3860 O OD1 . ASP A 1 485 ? 20.045  -22.682 37.782 1.00 20.10 ? 485  ASP A OD1 1 
ATOM   3861 O OD2 . ASP A 1 485 ? 21.212  -23.853 39.220 1.00 25.29 ? 485  ASP A OD2 1 
ATOM   3862 N N   . ALA A 1 486 ? 18.805  -19.387 37.883 1.00 18.56 ? 486  ALA A N   1 
ATOM   3863 C CA  . ALA A 1 486 ? 19.180  -18.168 37.174 1.00 19.22 ? 486  ALA A CA  1 
ATOM   3864 C C   . ALA A 1 486 ? 19.020  -16.990 38.136 1.00 20.25 ? 486  ALA A C   1 
ATOM   3865 O O   . ALA A 1 486 ? 18.269  -17.071 39.136 1.00 20.08 ? 486  ALA A O   1 
ATOM   3866 C CB  . ALA A 1 486 ? 18.349  -17.977 35.867 1.00 20.08 ? 486  ALA A CB  1 
ATOM   3867 N N   . VAL A 1 487 ? 19.743  -15.914 37.860 1.00 19.64 ? 487  VAL A N   1 
ATOM   3868 C CA  . VAL A 1 487 ? 19.975  -14.846 38.830 1.00 21.13 ? 487  VAL A CA  1 
ATOM   3869 C C   . VAL A 1 487 ? 19.550  -13.509 38.237 1.00 20.08 ? 487  VAL A C   1 
ATOM   3870 O O   . VAL A 1 487 ? 19.945  -13.165 37.124 1.00 18.82 ? 487  VAL A O   1 
ATOM   3871 C CB  . VAL A 1 487 ? 21.509  -14.847 39.219 1.00 22.21 ? 487  VAL A CB  1 
ATOM   3872 C CG1 . VAL A 1 487 ? 21.994  -13.508 39.685 1.00 25.02 ? 487  VAL A CG1 1 
ATOM   3873 C CG2 . VAL A 1 487 ? 21.752  -15.906 40.273 1.00 24.45 ? 487  VAL A CG2 1 
ATOM   3874 N N   . GLN A 1 488 ? 18.678  -12.805 38.962 1.00 19.95 ? 488  GLN A N   1 
ATOM   3875 C CA  . GLN A 1 488 ? 18.212  -11.469 38.599 1.00 20.01 ? 488  GLN A CA  1 
ATOM   3876 C C   . GLN A 1 488 ? 18.410  -10.477 39.768 1.00 20.50 ? 488  GLN A C   1 
ATOM   3877 O O   . GLN A 1 488 ? 18.798  -10.861 40.879 1.00 21.04 ? 488  GLN A O   1 
ATOM   3878 C CB  . GLN A 1 488 ? 16.722  -11.531 38.229 1.00 20.25 ? 488  GLN A CB  1 
ATOM   3879 C CG  . GLN A 1 488 ? 16.490  -12.130 36.871 1.00 20.15 ? 488  GLN A CG  1 
ATOM   3880 C CD  . GLN A 1 488 ? 15.018  -12.188 36.511 1.00 22.77 ? 488  GLN A CD  1 
ATOM   3881 O OE1 . GLN A 1 488 ? 14.444  -11.203 36.051 1.00 27.13 ? 488  GLN A OE1 1 
ATOM   3882 N NE2 . GLN A 1 488 ? 14.410  -13.326 36.720 1.00 23.54 ? 488  GLN A NE2 1 
ATOM   3883 N N   . HIS A 1 489 ? 18.156  -9.196  39.517 1.00 21.14 ? 489  HIS A N   1 
ATOM   3884 C CA  . HIS A 1 489 ? 18.311  -8.180  40.566 1.00 21.21 ? 489  HIS A CA  1 
ATOM   3885 C C   . HIS A 1 489 ? 17.492  -8.495  41.836 1.00 21.18 ? 489  HIS A C   1 
ATOM   3886 O O   . HIS A 1 489 ? 18.023  -8.454  42.950 1.00 21.10 ? 489  HIS A O   1 
ATOM   3887 C CB  . HIS A 1 489 ? 18.015  -6.778  40.015 1.00 22.21 ? 489  HIS A CB  1 
ATOM   3888 C CG  . HIS A 1 489 ? 18.278  -5.694  40.997 1.00 23.82 ? 489  HIS A CG  1 
ATOM   3889 N ND1 . HIS A 1 489 ? 17.303  -4.819  41.423 1.00 27.23 ? 489  HIS A ND1 1 
ATOM   3890 C CD2 . HIS A 1 489 ? 19.407  -5.357  41.663 1.00 27.46 ? 489  HIS A CD2 1 
ATOM   3891 C CE1 . HIS A 1 489 ? 17.818  -3.984  42.310 1.00 26.51 ? 489  HIS A CE1 1 
ATOM   3892 N NE2 . HIS A 1 489 ? 19.090  -4.295  42.480 1.00 31.65 ? 489  HIS A NE2 1 
ATOM   3893 N N   . TRP A 1 490 ? 16.227  -8.894  41.671 1.00 20.62 ? 490  TRP A N   1 
ATOM   3894 C CA  . TRP A 1 490 ? 15.395  -9.223  42.823 1.00 21.20 ? 490  TRP A CA  1 
ATOM   3895 C C   . TRP A 1 490 ? 15.690  -10.546 43.490 1.00 21.58 ? 490  TRP A C   1 
ATOM   3896 O O   . TRP A 1 490 ? 15.184  -10.798 44.571 1.00 22.34 ? 490  TRP A O   1 
ATOM   3897 C CB  . TRP A 1 490 ? 13.903  -9.188  42.461 1.00 20.00 ? 490  TRP A CB  1 
ATOM   3898 C CG  . TRP A 1 490 ? 13.375  -7.853  42.242 1.00 19.77 ? 490  TRP A CG  1 
ATOM   3899 C CD1 . TRP A 1 490 ? 13.994  -6.636  42.503 1.00 20.09 ? 490  TRP A CD1 1 
ATOM   3900 C CD2 . TRP A 1 490 ? 12.076  -7.544  41.746 1.00 18.79 ? 490  TRP A CD2 1 
ATOM   3901 N NE1 . TRP A 1 490 ? 13.161  -5.611  42.145 1.00 20.68 ? 490  TRP A NE1 1 
ATOM   3902 C CE2 . TRP A 1 490 ? 11.980  -6.138  41.670 1.00 21.55 ? 490  TRP A CE2 1 
ATOM   3903 C CE3 . TRP A 1 490 ? 10.998  -8.331  41.300 1.00 22.04 ? 490  TRP A CE3 1 
ATOM   3904 C CZ2 . TRP A 1 490 ? 10.827  -5.493  41.205 1.00 20.55 ? 490  TRP A CZ2 1 
ATOM   3905 C CZ3 . TRP A 1 490 ? 9.849   -7.691  40.843 1.00 21.00 ? 490  TRP A CZ3 1 
ATOM   3906 C CH2 . TRP A 1 490 ? 9.776   -6.292  40.797 1.00 20.13 ? 490  TRP A CH2 1 
ATOM   3907 N N   . GLY A 1 491 ? 16.451  -11.417 42.827 1.00 21.51 ? 491  GLY A N   1 
ATOM   3908 C CA  . GLY A 1 491 ? 16.828  -12.708 43.393 1.00 21.86 ? 491  GLY A CA  1 
ATOM   3909 C C   . GLY A 1 491 ? 16.850  -13.825 42.363 1.00 20.87 ? 491  GLY A C   1 
ATOM   3910 O O   . GLY A 1 491 ? 16.896  -13.571 41.164 1.00 22.07 ? 491  GLY A O   1 
ATOM   3911 N N   . LYS A 1 492 ? 16.803  -15.067 42.830 1.00 21.33 ? 492  LYS A N   1 
ATOM   3912 C CA  . LYS A 1 492 ? 16.888  -16.214 41.947 1.00 20.48 ? 492  LYS A CA  1 
ATOM   3913 C C   . LYS A 1 492 ? 15.548  -16.464 41.271 1.00 20.59 ? 492  LYS A C   1 
ATOM   3914 O O   . LYS A 1 492 ? 14.489  -16.142 41.819 1.00 18.48 ? 492  LYS A O   1 
ATOM   3915 C CB  . LYS A 1 492 ? 17.412  -17.438 42.699 1.00 22.15 ? 492  LYS A CB  1 
ATOM   3916 C CG  . LYS A 1 492 ? 18.932  -17.273 42.974 1.00 24.68 ? 492  LYS A CG  1 
ATOM   3917 C CD  . LYS A 1 492 ? 19.680  -18.545 43.276 1.00 30.24 ? 492  LYS A CD  1 
ATOM   3918 C CE  . LYS A 1 492 ? 21.217  -18.301 43.248 1.00 29.86 ? 492  LYS A CE  1 
ATOM   3919 N NZ  . LYS A 1 492 ? 21.858  -19.126 42.143 1.00 31.93 ? 492  LYS A NZ  1 
ATOM   3920 N N   . GLN A 1 493 ? 15.607  -17.011 40.069 1.00 19.25 ? 493  GLN A N   1 
ATOM   3921 C CA  . GLN A 1 493 ? 14.383  -17.353 39.339 1.00 20.08 ? 493  GLN A CA  1 
ATOM   3922 C C   . GLN A 1 493 ? 13.381  -18.204 40.169 1.00 19.37 ? 493  GLN A C   1 
ATOM   3923 O O   . GLN A 1 493 ? 12.170  -18.040 40.027 1.00 19.33 ? 493  GLN A O   1 
ATOM   3924 C CB  . GLN A 1 493 ? 14.782  -17.991 37.996 1.00 20.65 ? 493  GLN A CB  1 
ATOM   3925 C CG  . GLN A 1 493 ? 13.633  -18.490 37.129 1.00 23.37 ? 493  GLN A CG  1 
ATOM   3926 C CD  . GLN A 1 493 ? 12.924  -17.383 36.338 1.00 23.60 ? 493  GLN A CD  1 
ATOM   3927 O OE1 . GLN A 1 493 ? 13.267  -16.207 36.397 1.00 26.99 ? 493  GLN A OE1 1 
ATOM   3928 N NE2 . GLN A 1 493 ? 11.967  -17.789 35.565 1.00 24.28 ? 493  GLN A NE2 1 
ATOM   3929 N N   . TYR A 1 494 ? 13.877  -19.098 41.029 1.00 17.61 ? 494  TYR A N   1 
ATOM   3930 C CA  . TYR A 1 494 ? 13.019  -19.895 41.920 1.00 17.72 ? 494  TYR A CA  1 
ATOM   3931 C C   . TYR A 1 494 ? 11.996  -19.013 42.651 1.00 18.65 ? 494  TYR A C   1 
ATOM   3932 O O   . TYR A 1 494 ? 10.843  -19.413 42.837 1.00 17.61 ? 494  TYR A O   1 
ATOM   3933 C CB  . TYR A 1 494 ? 13.890  -20.615 42.940 1.00 16.54 ? 494  TYR A CB  1 
ATOM   3934 C CG  . TYR A 1 494 ? 13.208  -21.590 43.827 1.00 15.73 ? 494  TYR A CG  1 
ATOM   3935 C CD1 . TYR A 1 494 ? 13.006  -22.911 43.411 1.00 14.13 ? 494  TYR A CD1 1 
ATOM   3936 C CD2 . TYR A 1 494 ? 12.758  -21.214 45.089 1.00 16.92 ? 494  TYR A CD2 1 
ATOM   3937 C CE1 . TYR A 1 494 ? 12.404  -23.841 44.246 1.00 13.81 ? 494  TYR A CE1 1 
ATOM   3938 C CE2 . TYR A 1 494 ? 12.146  -22.127 45.915 1.00 15.94 ? 494  TYR A CE2 1 
ATOM   3939 C CZ  . TYR A 1 494 ? 11.963  -23.437 45.482 1.00 15.31 ? 494  TYR A CZ  1 
ATOM   3940 O OH  . TYR A 1 494 ? 11.386  -24.354 46.311 1.00 14.83 ? 494  TYR A OH  1 
ATOM   3941 N N   . ASP A 1 495 ? 12.446  -17.846 43.100 1.00 17.29 ? 495  ASP A N   1 
ATOM   3942 C CA  . ASP A 1 495 ? 11.596  -16.943 43.880 1.00 19.41 ? 495  ASP A CA  1 
ATOM   3943 C C   . ASP A 1 495 ? 10.843  -15.919 43.034 1.00 18.78 ? 495  ASP A C   1 
ATOM   3944 O O   . ASP A 1 495 ? 9.753   -15.474 43.417 1.00 20.45 ? 495  ASP A O   1 
ATOM   3945 C CB  . ASP A 1 495 ? 12.431  -16.180 44.917 1.00 18.85 ? 495  ASP A CB  1 
ATOM   3946 C CG  . ASP A 1 495 ? 12.991  -17.068 46.005 1.00 22.38 ? 495  ASP A CG  1 
ATOM   3947 O OD1 . ASP A 1 495 ? 12.296  -17.988 46.490 1.00 23.15 ? 495  ASP A OD1 1 
ATOM   3948 O OD2 . ASP A 1 495 ? 14.150  -16.795 46.412 1.00 19.88 ? 495  ASP A OD2 1 
ATOM   3949 N N   . ILE A 1 496 ? 11.423  -15.510 41.903 1.00 17.92 ? 496  ILE A N   1 
ATOM   3950 C CA  . ILE A 1 496 ? 10.847  -14.364 41.182 1.00 19.16 ? 496  ILE A CA  1 
ATOM   3951 C C   . ILE A 1 496 ? 10.262  -14.708 39.829 1.00 15.66 ? 496  ILE A C   1 
ATOM   3952 O O   . ILE A 1 496 ? 9.819   -13.818 39.123 1.00 17.38 ? 496  ILE A O   1 
ATOM   3953 C CB  . ILE A 1 496 ? 11.825  -13.158 41.067 1.00 19.51 ? 496  ILE A CB  1 
ATOM   3954 C CG1 . ILE A 1 496 ? 12.940  -13.463 40.087 1.00 21.29 ? 496  ILE A CG1 1 
ATOM   3955 C CG2 . ILE A 1 496 ? 12.341  -12.707 42.468 1.00 20.48 ? 496  ILE A CG2 1 
ATOM   3956 C CD1 . ILE A 1 496 ? 13.964  -12.315 39.997 1.00 22.41 ? 496  ILE A CD1 1 
ATOM   3957 N N   . HIS A 1 497 ? 10.235  -15.999 39.483 1.00 15.63 ? 497  HIS A N   1 
ATOM   3958 C CA  . HIS A 1 497 ? 9.730   -16.468 38.180 1.00 14.30 ? 497  HIS A CA  1 
ATOM   3959 C C   . HIS A 1 497 ? 8.321   -15.892 37.924 1.00 13.88 ? 497  HIS A C   1 
ATOM   3960 O O   . HIS A 1 497 ? 8.016   -15.424 36.826 1.00 13.76 ? 497  HIS A O   1 
ATOM   3961 C CB  . HIS A 1 497 ? 9.622   -17.998 38.188 1.00 14.08 ? 497  HIS A CB  1 
ATOM   3962 C CG  . HIS A 1 497 ? 8.983   -18.566 36.961 1.00 15.16 ? 497  HIS A CG  1 
ATOM   3963 N ND1 . HIS A 1 497 ? 7.628   -18.830 36.880 1.00 16.96 ? 497  HIS A ND1 1 
ATOM   3964 C CD2 . HIS A 1 497 ? 9.508   -18.920 35.766 1.00 14.37 ? 497  HIS A CD2 1 
ATOM   3965 C CE1 . HIS A 1 497 ? 7.349   -19.318 35.691 1.00 13.89 ? 497  HIS A CE1 1 
ATOM   3966 N NE2 . HIS A 1 497 ? 8.467   -19.374 34.990 1.00 21.83 ? 497  HIS A NE2 1 
ATOM   3967 N N   . ASN A 1 498 ? 7.478   -15.974 38.940 1.00 15.27 ? 498  ASN A N   1 
ATOM   3968 C CA  . ASN A 1 498 ? 6.069   -15.531 38.793 1.00 15.18 ? 498  ASN A CA  1 
ATOM   3969 C C   . ASN A 1 498 ? 5.978   -14.008 38.666 1.00 15.96 ? 498  ASN A C   1 
ATOM   3970 O O   . ASN A 1 498 ? 4.890   -13.452 38.458 1.00 16.50 ? 498  ASN A O   1 
ATOM   3971 C CB  . ASN A 1 498 ? 5.251   -16.002 39.994 1.00 14.91 ? 498  ASN A CB  1 
ATOM   3972 C CG  . ASN A 1 498 ? 4.731   -17.430 39.851 1.00 16.73 ? 498  ASN A CG  1 
ATOM   3973 O OD1 . ASN A 1 498 ? 4.078   -17.989 40.753 1.00 21.10 ? 498  ASN A OD1 1 
ATOM   3974 N ND2 . ASN A 1 498 ? 4.987   -18.011 38.739 1.00 13.87 ? 498  ASN A ND2 1 
ATOM   3975 N N   . LEU A 1 499 ? 7.113   -13.333 38.860 1.00 15.47 ? 499  LEU A N   1 
ATOM   3976 C CA  . LEU A 1 499 ? 7.200   -11.890 38.756 1.00 15.75 ? 499  LEU A CA  1 
ATOM   3977 C C   . LEU A 1 499 ? 7.759   -11.358 37.475 1.00 15.52 ? 499  LEU A C   1 
ATOM   3978 O O   . LEU A 1 499 ? 7.920   -10.151 37.327 1.00 15.49 ? 499  LEU A O   1 
ATOM   3979 C CB  . LEU A 1 499 ? 8.021   -11.307 39.913 1.00 15.64 ? 499  LEU A CB  1 
ATOM   3980 C CG  . LEU A 1 499 ? 7.578   -11.683 41.334 1.00 16.34 ? 499  LEU A CG  1 
ATOM   3981 C CD1 . LEU A 1 499 ? 8.484   -11.070 42.404 1.00 14.00 ? 499  LEU A CD1 1 
ATOM   3982 C CD2 . LEU A 1 499 ? 6.105   -11.264 41.587 1.00 17.08 ? 499  LEU A CD2 1 
ATOM   3983 N N   . TYR A 1 500 ? 8.128   -12.234 36.558 1.00 15.64 ? 500  TYR A N   1 
ATOM   3984 C CA  . TYR A 1 500 ? 8.762   -11.756 35.329 1.00 15.39 ? 500  TYR A CA  1 
ATOM   3985 C C   . TYR A 1 500 ? 7.888   -10.837 34.476 1.00 15.41 ? 500  TYR A C   1 
ATOM   3986 O O   . TYR A 1 500 ? 8.299   -9.732  34.082 1.00 14.89 ? 500  TYR A O   1 
ATOM   3987 C CB  . TYR A 1 500 ? 9.266   -12.914 34.487 1.00 15.06 ? 500  TYR A CB  1 
ATOM   3988 C CG  . TYR A 1 500 ? 10.218  -12.443 33.430 1.00 16.67 ? 500  TYR A CG  1 
ATOM   3989 C CD1 . TYR A 1 500 ? 11.581  -12.452 33.654 1.00 16.49 ? 500  TYR A CD1 1 
ATOM   3990 C CD2 . TYR A 1 500 ? 9.748   -11.981 32.205 1.00 15.71 ? 500  TYR A CD2 1 
ATOM   3991 C CE1 . TYR A 1 500 ? 12.463  -12.019 32.667 1.00 16.30 ? 500  TYR A CE1 1 
ATOM   3992 C CE2 . TYR A 1 500 ? 10.599  -11.525 31.234 1.00 15.45 ? 500  TYR A CE2 1 
ATOM   3993 C CZ  . TYR A 1 500 ? 11.972  -11.561 31.483 1.00 17.73 ? 500  TYR A CZ  1 
ATOM   3994 O OH  . TYR A 1 500 ? 12.812  -11.131 30.518 1.00 18.68 ? 500  TYR A OH  1 
ATOM   3995 N N   . GLY A 1 501 ? 6.669   -11.287 34.197 1.00 15.87 ? 501  GLY A N   1 
ATOM   3996 C CA  . GLY A 1 501 ? 5.789   -10.507 33.369 1.00 15.83 ? 501  GLY A CA  1 
ATOM   3997 C C   . GLY A 1 501 ? 5.297   -9.268  34.086 1.00 15.14 ? 501  GLY A C   1 
ATOM   3998 O O   . GLY A 1 501 ? 5.077   -8.256  33.456 1.00 16.13 ? 501  GLY A O   1 
ATOM   3999 N N   . TYR A 1 502 ? 5.133   -9.358  35.397 1.00 15.36 ? 502  TYR A N   1 
ATOM   4000 C CA  . TYR A 1 502 ? 4.835   -8.180  36.230 1.00 15.36 ? 502  TYR A CA  1 
ATOM   4001 C C   . TYR A 1 502 ? 5.957   -7.146  36.084 1.00 15.04 ? 502  TYR A C   1 
ATOM   4002 O O   . TYR A 1 502 ? 5.722   -5.977  35.821 1.00 14.51 ? 502  TYR A O   1 
ATOM   4003 C CB  . TYR A 1 502 ? 4.698   -8.651  37.672 1.00 16.26 ? 502  TYR A CB  1 
ATOM   4004 C CG  . TYR A 1 502 ? 4.550   -7.568  38.719 1.00 18.56 ? 502  TYR A CG  1 
ATOM   4005 C CD1 . TYR A 1 502 ? 3.346   -6.901  38.884 1.00 16.22 ? 502  TYR A CD1 1 
ATOM   4006 C CD2 . TYR A 1 502 ? 5.617   -7.244  39.579 1.00 16.91 ? 502  TYR A CD2 1 
ATOM   4007 C CE1 . TYR A 1 502 ? 3.208   -5.919  39.856 1.00 18.02 ? 502  TYR A CE1 1 
ATOM   4008 C CE2 . TYR A 1 502 ? 5.477   -6.276  40.589 1.00 17.13 ? 502  TYR A CE2 1 
ATOM   4009 C CZ  . TYR A 1 502 ? 4.266   -5.612  40.698 1.00 19.77 ? 502  TYR A CZ  1 
ATOM   4010 O OH  . TYR A 1 502 ? 4.104   -4.668  41.669 1.00 20.11 ? 502  TYR A OH  1 
ATOM   4011 N N   . SER A 1 503 ? 7.203   -7.577  36.247 1.00 14.79 ? 503  SER A N   1 
ATOM   4012 C CA  . SER A 1 503 ? 8.320   -6.612  36.161 1.00 15.14 ? 503  SER A CA  1 
ATOM   4013 C C   . SER A 1 503 ? 8.429   -6.039  34.745 1.00 14.87 ? 503  SER A C   1 
ATOM   4014 O O   . SER A 1 503 ? 8.740   -4.858  34.554 1.00 15.54 ? 503  SER A O   1 
ATOM   4015 C CB  . SER A 1 503 ? 9.605   -7.274  36.647 1.00 15.77 ? 503  SER A CB  1 
ATOM   4016 O OG  . SER A 1 503 ? 9.907   -8.359  35.796 1.00 17.94 ? 503  SER A OG  1 
ATOM   4017 N N   . MET A 1 504 ? 8.146   -6.864  33.742 1.00 14.16 ? 504  MET A N   1 
ATOM   4018 C CA  . MET A 1 504 ? 8.150   -6.419  32.370 1.00 15.04 ? 504  MET A CA  1 
ATOM   4019 C C   . MET A 1 504 ? 7.083   -5.343  32.131 1.00 14.66 ? 504  MET A C   1 
ATOM   4020 O O   . MET A 1 504 ? 7.354   -4.324  31.506 1.00 13.88 ? 504  MET A O   1 
ATOM   4021 C CB  . MET A 1 504 ? 7.929   -7.576  31.410 1.00 14.43 ? 504  MET A CB  1 
ATOM   4022 C CG  . MET A 1 504 ? 8.103   -7.181  29.950 1.00 15.95 ? 504  MET A CG  1 
ATOM   4023 S SD  . MET A 1 504 ? 8.021   -8.600  28.882 1.00 16.21 ? 504  MET A SD  1 
ATOM   4024 C CE  . MET A 1 504 ? 8.416   -7.822  27.329 1.00 17.64 ? 504  MET A CE  1 
ATOM   4025 N N   . ALA A 1 505 ? 5.877   -5.590  32.628 1.00 13.79 ? 505  ALA A N   1 
ATOM   4026 C CA  . ALA A 1 505 ? 4.806   -4.570  32.472 1.00 13.76 ? 505  ALA A CA  1 
ATOM   4027 C C   . ALA A 1 505 ? 5.203   -3.251  33.182 1.00 14.48 ? 505  ALA A C   1 
ATOM   4028 O O   . ALA A 1 505 ? 4.958   -2.175  32.622 1.00 15.74 ? 505  ALA A O   1 
ATOM   4029 C CB  . ALA A 1 505 ? 3.450   -5.115  33.018 1.00 13.55 ? 505  ALA A CB  1 
ATOM   4030 N N   . VAL A 1 506 ? 5.826   -3.327  34.370 1.00 14.79 ? 506  VAL A N   1 
ATOM   4031 C CA  . VAL A 1 506 ? 6.259   -2.122  35.114 1.00 15.40 ? 506  VAL A CA  1 
ATOM   4032 C C   . VAL A 1 506 ? 7.297   -1.342  34.264 1.00 16.66 ? 506  VAL A C   1 
ATOM   4033 O O   . VAL A 1 506 ? 7.220   -0.118  34.076 1.00 15.21 ? 506  VAL A O   1 
ATOM   4034 C CB  . VAL A 1 506 ? 6.845   -2.487  36.557 1.00 15.86 ? 506  VAL A CB  1 
ATOM   4035 C CG1 . VAL A 1 506 ? 7.539   -1.290  37.211 1.00 16.22 ? 506  VAL A CG1 1 
ATOM   4036 C CG2 . VAL A 1 506 ? 5.747   -3.068  37.487 1.00 17.42 ? 506  VAL A CG2 1 
ATOM   4037 N N   . ALA A 1 507 ? 8.251   -2.085  33.700 1.00 17.01 ? 507  ALA A N   1 
ATOM   4038 C CA  . ALA A 1 507 ? 9.307   -1.506  32.836 1.00 17.11 ? 507  ALA A CA  1 
ATOM   4039 C C   . ALA A 1 507 ? 8.773   -0.916  31.544 1.00 17.16 ? 507  ALA A C   1 
ATOM   4040 O O   . ALA A 1 507 ? 9.296   0.085   31.055 1.00 16.40 ? 507  ALA A O   1 
ATOM   4041 C CB  . ALA A 1 507 ? 10.357  -2.593  32.518 1.00 17.59 ? 507  ALA A CB  1 
ATOM   4042 N N   . THR A 1 508 ? 7.730   -1.539  30.982 1.00 17.05 ? 508  THR A N   1 
ATOM   4043 C CA  . THR A 1 508 ? 7.072   -1.085  29.758 1.00 17.02 ? 508  THR A CA  1 
ATOM   4044 C C   . THR A 1 508 ? 6.252   0.192   30.002 1.00 17.27 ? 508  THR A C   1 
ATOM   4045 O O   . THR A 1 508 ? 6.287   1.119   29.182 1.00 16.45 ? 508  THR A O   1 
ATOM   4046 C CB  . THR A 1 508 ? 6.230   -2.245  29.107 1.00 17.14 ? 508  THR A CB  1 
ATOM   4047 O OG1 . THR A 1 508 ? 7.120   -3.350  28.844 1.00 19.37 ? 508  THR A OG1 1 
ATOM   4048 C CG2 . THR A 1 508 ? 5.619   -1.849  27.793 1.00 16.44 ? 508  THR A CG2 1 
ATOM   4049 N N   . ALA A 1 509 ? 5.551   0.250   31.133 1.00 17.66 ? 509  ALA A N   1 
ATOM   4050 C CA  . ALA A 1 509 ? 4.907   1.521   31.573 1.00 19.09 ? 509  ALA A CA  1 
ATOM   4051 C C   . ALA A 1 509 ? 5.961   2.610   31.787 1.00 19.95 ? 509  ALA A C   1 
ATOM   4052 O O   . ALA A 1 509 ? 5.765   3.761   31.402 1.00 20.59 ? 509  ALA A O   1 
ATOM   4053 C CB  . ALA A 1 509 ? 4.058   1.322   32.833 1.00 19.71 ? 509  ALA A CB  1 
ATOM   4054 N N   . GLU A 1 510 ? 7.114   2.251   32.341 1.00 21.27 ? 510  GLU A N   1 
ATOM   4055 C CA  . GLU A 1 510 ? 8.183   3.242   32.460 1.00 21.16 ? 510  GLU A CA  1 
ATOM   4056 C C   . GLU A 1 510 ? 8.632   3.764   31.101 1.00 19.87 ? 510  GLU A C   1 
ATOM   4057 O O   . GLU A 1 510 ? 8.773   4.976   30.941 1.00 19.20 ? 510  GLU A O   1 
ATOM   4058 C CB  . GLU A 1 510 ? 9.358   2.703   33.308 1.00 21.92 ? 510  GLU A CB  1 
ATOM   4059 C CG  . GLU A 1 510 ? 10.493  3.689   33.502 1.00 28.80 ? 510  GLU A CG  1 
ATOM   4060 C CD  . GLU A 1 510 ? 10.236  4.750   34.583 1.00 36.14 ? 510  GLU A CD  1 
ATOM   4061 O OE1 . GLU A 1 510 ? 9.177   4.721   35.261 1.00 38.49 ? 510  GLU A OE1 1 
ATOM   4062 O OE2 . GLU A 1 510 ? 11.127  5.618   34.761 1.00 38.73 ? 510  GLU A OE2 1 
ATOM   4063 N N   . ALA A 1 511 ? 8.858   2.861   30.134 1.00 19.23 ? 511  ALA A N   1 
ATOM   4064 C CA  . ALA A 1 511 ? 9.217   3.209   28.764 1.00 19.19 ? 511  ALA A CA  1 
ATOM   4065 C C   . ALA A 1 511 ? 8.171   4.131   28.134 1.00 20.17 ? 511  ALA A C   1 
ATOM   4066 O O   . ALA A 1 511 ? 8.508   5.081   27.411 1.00 18.84 ? 511  ALA A O   1 
ATOM   4067 C CB  . ALA A 1 511 ? 9.404   1.940   27.893 1.00 18.83 ? 511  ALA A CB  1 
ATOM   4068 N N   . ALA A 1 512 ? 6.902   3.877   28.432 1.00 19.76 ? 512  ALA A N   1 
ATOM   4069 C CA  . ALA A 1 512 ? 5.826   4.695   27.873 1.00 20.75 ? 512  ALA A CA  1 
ATOM   4070 C C   . ALA A 1 512 ? 5.897   6.160   28.346 1.00 21.20 ? 512  ALA A C   1 
ATOM   4071 O O   . ALA A 1 512 ? 5.455   7.050   27.632 1.00 21.70 ? 512  ALA A O   1 
ATOM   4072 C CB  . ALA A 1 512 ? 4.463   4.069   28.207 1.00 21.12 ? 512  ALA A CB  1 
ATOM   4073 N N   . LYS A 1 513 ? 6.483   6.411   29.523 1.00 22.06 ? 513  LYS A N   1 
ATOM   4074 C CA  . LYS A 1 513 ? 6.646   7.780   30.043 1.00 23.85 ? 513  LYS A CA  1 
ATOM   4075 C C   . LYS A 1 513 ? 7.441   8.660   29.080 1.00 24.33 ? 513  LYS A C   1 
ATOM   4076 O O   . LYS A 1 513 ? 7.202   9.863   28.975 1.00 24.17 ? 513  LYS A O   1 
ATOM   4077 C CB  . LYS A 1 513 ? 7.338   7.791   31.410 1.00 24.23 ? 513  LYS A CB  1 
ATOM   4078 C CG  . LYS A 1 513 ? 6.557   7.136   32.511 1.00 26.91 ? 513  LYS A CG  1 
ATOM   4079 C CD  . LYS A 1 513 ? 7.135   7.472   33.851 1.00 30.07 ? 513  LYS A CD  1 
ATOM   4080 C CE  . LYS A 1 513 ? 6.465   6.647   34.933 1.00 33.72 ? 513  LYS A CE  1 
ATOM   4081 N NZ  . LYS A 1 513 ? 7.284   6.650   36.167 1.00 37.19 ? 513  LYS A NZ  1 
ATOM   4082 N N   . THR A 1 514 ? 8.401   8.043   28.399 1.00 23.73 ? 514  THR A N   1 
ATOM   4083 C CA  . THR A 1 514 ? 9.286   8.726   27.450 1.00 22.97 ? 514  THR A CA  1 
ATOM   4084 C C   . THR A 1 514 ? 8.772   8.665   26.033 1.00 22.21 ? 514  THR A C   1 
ATOM   4085 O O   . THR A 1 514 ? 8.769   9.672   25.324 1.00 21.63 ? 514  THR A O   1 
ATOM   4086 C CB  . THR A 1 514 ? 10.682  8.062   27.513 1.00 23.22 ? 514  THR A CB  1 
ATOM   4087 O OG1 . THR A 1 514 ? 11.201  8.275   28.822 1.00 24.24 ? 514  THR A OG1 1 
ATOM   4088 C CG2 . THR A 1 514 ? 11.642  8.653   26.474 1.00 25.38 ? 514  THR A CG2 1 
ATOM   4089 N N   . VAL A 1 515 ? 8.313   7.481   25.610 1.00 20.55 ? 515  VAL A N   1 
ATOM   4090 C CA  . VAL A 1 515 ? 7.922   7.274   24.216 1.00 21.01 ? 515  VAL A CA  1 
ATOM   4091 C C   . VAL A 1 515 ? 6.576   7.972   23.916 1.00 20.77 ? 515  VAL A C   1 
ATOM   4092 O O   . VAL A 1 515 ? 6.370   8.490   22.822 1.00 20.52 ? 515  VAL A O   1 
ATOM   4093 C CB  . VAL A 1 515 ? 7.826   5.770   23.883 1.00 21.06 ? 515  VAL A CB  1 
ATOM   4094 C CG1 . VAL A 1 515 ? 7.171   5.554   22.516 1.00 22.76 ? 515  VAL A CG1 1 
ATOM   4095 C CG2 . VAL A 1 515 ? 9.219   5.120   23.918 1.00 23.57 ? 515  VAL A CG2 1 
ATOM   4096 N N   . PHE A 1 516 ? 5.704   8.011   24.921 1.00 20.24 ? 516  PHE A N   1 
ATOM   4097 C CA  . PHE A 1 516 ? 4.378   8.650   24.817 1.00 20.59 ? 516  PHE A CA  1 
ATOM   4098 C C   . PHE A 1 516 ? 4.163   9.676   25.930 1.00 21.62 ? 516  PHE A C   1 
ATOM   4099 O O   . PHE A 1 516 ? 3.379   9.427   26.870 1.00 21.60 ? 516  PHE A O   1 
ATOM   4100 C CB  . PHE A 1 516 ? 3.299   7.557   24.938 1.00 20.89 ? 516  PHE A CB  1 
ATOM   4101 C CG  . PHE A 1 516 ? 3.452   6.456   23.949 1.00 19.89 ? 516  PHE A CG  1 
ATOM   4102 C CD1 . PHE A 1 516 ? 3.283   6.704   22.587 1.00 21.87 ? 516  PHE A CD1 1 
ATOM   4103 C CD2 . PHE A 1 516 ? 3.756   5.165   24.374 1.00 21.72 ? 516  PHE A CD2 1 
ATOM   4104 C CE1 . PHE A 1 516 ? 3.415   5.673   21.668 1.00 24.76 ? 516  PHE A CE1 1 
ATOM   4105 C CE2 . PHE A 1 516 ? 3.874   4.128   23.462 1.00 23.52 ? 516  PHE A CE2 1 
ATOM   4106 C CZ  . PHE A 1 516 ? 3.703   4.383   22.109 1.00 20.31 ? 516  PHE A CZ  1 
ATOM   4107 N N   . PRO A 1 517 ? 4.874   10.827  25.876 1.00 22.48 ? 517  PRO A N   1 
ATOM   4108 C CA  . PRO A 1 517 ? 4.846   11.715  27.032 1.00 23.22 ? 517  PRO A CA  1 
ATOM   4109 C C   . PRO A 1 517 ? 3.432   12.183  27.407 1.00 22.46 ? 517  PRO A C   1 
ATOM   4110 O O   . PRO A 1 517 ? 2.704   12.676  26.555 1.00 23.46 ? 517  PRO A O   1 
ATOM   4111 C CB  . PRO A 1 517 ? 5.693   12.913  26.563 1.00 23.43 ? 517  PRO A CB  1 
ATOM   4112 C CG  . PRO A 1 517 ? 6.650   12.320  25.600 1.00 23.32 ? 517  PRO A CG  1 
ATOM   4113 C CD  . PRO A 1 517 ? 5.755   11.368  24.820 1.00 23.02 ? 517  PRO A CD  1 
ATOM   4114 N N   . ASN A 1 518 ? 3.106   12.015  28.681 1.00 23.05 ? 518  ASN A N   1 
ATOM   4115 C CA  . ASN A 1 518 ? 1.811   12.369  29.296 1.00 24.19 ? 518  ASN A CA  1 
ATOM   4116 C C   . ASN A 1 518 ? 0.592   11.665  28.711 1.00 22.78 ? 518  ASN A C   1 
ATOM   4117 O O   . ASN A 1 518 ? -0.540  12.108  28.949 1.00 23.62 ? 518  ASN A O   1 
ATOM   4118 C CB  . ASN A 1 518 ? 1.590   13.891  29.289 1.00 25.69 ? 518  ASN A CB  1 
ATOM   4119 C CG  . ASN A 1 518 ? 2.730   14.645  29.965 1.00 30.18 ? 518  ASN A CG  1 
ATOM   4120 O OD1 . ASN A 1 518 ? 3.109   14.341  31.109 1.00 37.35 ? 518  ASN A OD1 1 
ATOM   4121 N ND2 . ASN A 1 518 ? 3.281   15.633  29.259 1.00 33.36 ? 518  ASN A ND2 1 
ATOM   4122 N N   . LYS A 1 519 ? 0.811   10.597  27.951 1.00 21.14 ? 519  LYS A N   1 
ATOM   4123 C CA  . LYS A 1 519 ? -0.306  9.755   27.466 1.00 20.49 ? 519  LYS A CA  1 
ATOM   4124 C C   . LYS A 1 519 ? -0.340  8.396   28.156 1.00 19.74 ? 519  LYS A C   1 
ATOM   4125 O O   . LYS A 1 519 ? 0.683   7.885   28.671 1.00 18.67 ? 519  LYS A O   1 
ATOM   4126 C CB  . LYS A 1 519 ? -0.269  9.533   25.939 1.00 21.23 ? 519  LYS A CB  1 
ATOM   4127 C CG  . LYS A 1 519 ? -0.153  10.787  25.064 1.00 24.59 ? 519  LYS A CG  1 
ATOM   4128 C CD  . LYS A 1 519 ? -1.348  11.724  25.196 1.00 25.63 ? 519  LYS A CD  1 
ATOM   4129 C CE  . LYS A 1 519 ? -1.062  13.072  24.523 1.00 26.61 ? 519  LYS A CE  1 
ATOM   4130 N NZ  . LYS A 1 519 ? -2.076  14.101  24.882 1.00 32.53 ? 519  LYS A NZ  1 
ATOM   4131 N N   . ARG A 1 520 ? -1.523  7.783   28.118 1.00 16.54 ? 520  ARG A N   1 
ATOM   4132 C CA  . ARG A 1 520 ? -1.718  6.438   28.641 1.00 15.94 ? 520  ARG A CA  1 
ATOM   4133 C C   . ARG A 1 520 ? -1.151  5.364   27.771 1.00 15.49 ? 520  ARG A C   1 
ATOM   4134 O O   . ARG A 1 520 ? -0.652  4.366   28.305 1.00 16.83 ? 520  ARG A O   1 
ATOM   4135 C CB  . ARG A 1 520 ? -3.224  6.162   28.790 1.00 15.46 ? 520  ARG A CB  1 
ATOM   4136 C CG  . ARG A 1 520 ? -3.818  7.099   29.794 1.00 15.20 ? 520  ARG A CG  1 
ATOM   4137 C CD  . ARG A 1 520 ? -5.362  7.057   29.668 1.00 13.48 ? 520  ARG A CD  1 
ATOM   4138 N NE  . ARG A 1 520 ? -5.889  8.295   30.210 1.00 14.52 ? 520  ARG A NE  1 
ATOM   4139 C CZ  . ARG A 1 520 ? -7.180  8.624   30.247 1.00 16.74 ? 520  ARG A CZ  1 
ATOM   4140 N NH1 . ARG A 1 520 ? -8.106  7.772   29.823 1.00 11.88 ? 520  ARG A NH1 1 
ATOM   4141 N NH2 . ARG A 1 520 ? -7.528  9.800   30.713 1.00 15.34 ? 520  ARG A NH2 1 
ATOM   4142 N N   . SER A 1 521 ? -1.308  5.526   26.456 1.00 15.77 ? 521  SER A N   1 
ATOM   4143 C CA  . SER A 1 521 ? -0.956  4.498   25.467 1.00 15.72 ? 521  SER A CA  1 
ATOM   4144 C C   . SER A 1 521 ? -1.774  3.260   25.833 1.00 16.08 ? 521  SER A C   1 
ATOM   4145 O O   . SER A 1 521 ? -2.887  3.378   26.404 1.00 15.44 ? 521  SER A O   1 
ATOM   4146 C CB  . SER A 1 521 ? 0.564   4.231   25.536 1.00 16.03 ? 521  SER A CB  1 
ATOM   4147 O OG  . SER A 1 521 ? 0.961   3.264   24.579 1.00 14.46 ? 521  SER A OG  1 
ATOM   4148 N N   . PHE A 1 522 ? -1.210  2.080   25.628 1.00 15.48 ? 522  PHE A N   1 
ATOM   4149 C CA  . PHE A 1 522 ? -1.932  0.818   25.911 1.00 14.93 ? 522  PHE A CA  1 
ATOM   4150 C C   . PHE A 1 522 ? -0.856  -0.256  26.037 1.00 15.15 ? 522  PHE A C   1 
ATOM   4151 O O   . PHE A 1 522 ? -0.002  -0.343  25.159 1.00 15.11 ? 522  PHE A O   1 
ATOM   4152 C CB  . PHE A 1 522 ? -2.797  0.500   24.691 1.00 14.51 ? 522  PHE A CB  1 
ATOM   4153 C CG  . PHE A 1 522 ? -3.405  -0.888  24.670 1.00 16.64 ? 522  PHE A CG  1 
ATOM   4154 C CD1 . PHE A 1 522 ? -4.499  -1.193  25.474 1.00 17.06 ? 522  PHE A CD1 1 
ATOM   4155 C CD2 . PHE A 1 522 ? -2.914  -1.867  23.791 1.00 16.34 ? 522  PHE A CD2 1 
ATOM   4156 C CE1 . PHE A 1 522 ? -5.083  -2.503  25.428 1.00 17.23 ? 522  PHE A CE1 1 
ATOM   4157 C CE2 . PHE A 1 522 ? -3.505  -3.141  23.711 1.00 16.43 ? 522  PHE A CE2 1 
ATOM   4158 C CZ  . PHE A 1 522 ? -4.580  -3.456  24.546 1.00 15.16 ? 522  PHE A CZ  1 
ATOM   4159 N N   . ILE A 1 523 ? -0.886  -1.040  27.111 1.00 14.11 ? 523  ILE A N   1 
ATOM   4160 C CA  . ILE A 1 523 ? -0.032  -2.222  27.235 1.00 14.22 ? 523  ILE A CA  1 
ATOM   4161 C C   . ILE A 1 523 ? -0.891  -3.428  27.445 1.00 14.53 ? 523  ILE A C   1 
ATOM   4162 O O   . ILE A 1 523 ? -1.775  -3.423  28.310 1.00 14.46 ? 523  ILE A O   1 
ATOM   4163 C CB  . ILE A 1 523 ? 0.939   -2.108  28.409 1.00 14.05 ? 523  ILE A CB  1 
ATOM   4164 C CG1 . ILE A 1 523 ? 1.832   -0.852  28.217 1.00 13.54 ? 523  ILE A CG1 1 
ATOM   4165 C CG2 . ILE A 1 523 ? 1.760   -3.407  28.552 1.00 14.12 ? 523  ILE A CG2 1 
ATOM   4166 C CD1 . ILE A 1 523 ? 2.442   -0.407  29.499 1.00 19.16 ? 523  ILE A CD1 1 
ATOM   4167 N N   . LEU A 1 524 ? -0.648  -4.458  26.645 1.00 14.34 ? 524  LEU A N   1 
ATOM   4168 C CA  . LEU A 1 524 ? -1.384  -5.751  26.755 1.00 13.53 ? 524  LEU A CA  1 
ATOM   4169 C C   . LEU A 1 524 ? -0.361  -6.806  27.155 1.00 14.37 ? 524  LEU A C   1 
ATOM   4170 O O   . LEU A 1 524 ? 0.635   -6.973  26.449 1.00 15.25 ? 524  LEU A O   1 
ATOM   4171 C CB  . LEU A 1 524 ? -1.991  -6.126  25.411 1.00 12.83 ? 524  LEU A CB  1 
ATOM   4172 C CG  . LEU A 1 524 ? -2.806  -7.430  25.277 1.00 14.37 ? 524  LEU A CG  1 
ATOM   4173 C CD1 . LEU A 1 524 ? -4.089  -7.379  26.174 1.00 14.48 ? 524  LEU A CD1 1 
ATOM   4174 C CD2 . LEU A 1 524 ? -3.159  -7.729  23.839 1.00 13.26 ? 524  LEU A CD2 1 
ATOM   4175 N N   . THR A 1 525 ? -0.593  -7.528  28.245 1.00 13.78 ? 525  THR A N   1 
ATOM   4176 C CA  . THR A 1 525 ? 0.413   -8.518  28.737 1.00 14.43 ? 525  THR A CA  1 
ATOM   4177 C C   . THR A 1 525 ? -0.161  -9.913  28.832 1.00 15.84 ? 525  THR A C   1 
ATOM   4178 O O   . THR A 1 525 ? -1.359  -10.084 29.121 1.00 15.07 ? 525  THR A O   1 
ATOM   4179 C CB  . THR A 1 525 ? 1.047   -8.102  30.102 1.00 14.62 ? 525  THR A CB  1 
ATOM   4180 O OG1 . THR A 1 525 ? 2.156   -8.975  30.420 1.00 15.79 ? 525  THR A OG1 1 
ATOM   4181 C CG2 . THR A 1 525 ? 0.004   -8.133  31.253 1.00 12.79 ? 525  THR A CG2 1 
ATOM   4182 N N   . ARG A 1 526 ? 0.690   -10.907 28.585 1.00 15.81 ? 526  ARG A N   1 
ATOM   4183 C CA  . ARG A 1 526 ? 0.294   -12.305 28.789 1.00 16.90 ? 526  ARG A CA  1 
ATOM   4184 C C   . ARG A 1 526 ? 0.432   -12.690 30.255 1.00 16.58 ? 526  ARG A C   1 
ATOM   4185 O O   . ARG A 1 526 ? -0.573  -12.963 30.922 1.00 16.42 ? 526  ARG A O   1 
ATOM   4186 C CB  . ARG A 1 526 ? 1.077   -13.281 27.884 1.00 16.61 ? 526  ARG A CB  1 
ATOM   4187 C CG  . ARG A 1 526 ? 0.281   -14.612 27.720 1.00 17.44 ? 526  ARG A CG  1 
ATOM   4188 C CD  . ARG A 1 526 ? 0.714   -15.348 26.516 1.00 18.61 ? 526  ARG A CD  1 
ATOM   4189 N NE  . ARG A 1 526 ? 1.930   -16.089 26.786 1.00 21.24 ? 526  ARG A NE  1 
ATOM   4190 C CZ  . ARG A 1 526 ? 2.635   -16.744 25.872 1.00 22.51 ? 526  ARG A CZ  1 
ATOM   4191 N NH1 . ARG A 1 526 ? 2.298   -16.684 24.587 1.00 21.88 ? 526  ARG A NH1 1 
ATOM   4192 N NH2 . ARG A 1 526 ? 3.718   -17.413 26.247 1.00 21.00 ? 526  ARG A NH2 1 
ATOM   4193 N N   . SER A 1 527 ? 1.673   -12.735 30.756 1.00 15.77 ? 527  SER A N   1 
ATOM   4194 C CA  . SER A 1 527 ? 1.903   -13.084 32.149 1.00 16.00 ? 527  SER A CA  1 
ATOM   4195 C C   . SER A 1 527 ? 1.561   -11.926 33.091 1.00 15.29 ? 527  SER A C   1 
ATOM   4196 O O   . SER A 1 527 ? 1.820   -10.765 32.770 1.00 16.37 ? 527  SER A O   1 
ATOM   4197 C CB  . SER A 1 527 ? 3.364   -13.491 32.387 1.00 16.53 ? 527  SER A CB  1 
ATOM   4198 O OG  . SER A 1 527 ? 3.399   -14.260 33.555 1.00 20.30 ? 527  SER A OG  1 
ATOM   4199 N N   . THR A 1 528 ? 0.967   -12.252 34.225 1.00 14.38 ? 528  THR A N   1 
ATOM   4200 C CA  . THR A 1 528 ? 0.592   -11.250 35.239 1.00 15.11 ? 528  THR A CA  1 
ATOM   4201 C C   . THR A 1 528 ? 0.936   -11.761 36.621 1.00 15.06 ? 528  THR A C   1 
ATOM   4202 O O   . THR A 1 528 ? 1.089   -12.959 36.816 1.00 15.81 ? 528  THR A O   1 
ATOM   4203 C CB  . THR A 1 528 ? -0.957  -10.951 35.235 1.00 14.41 ? 528  THR A CB  1 
ATOM   4204 O OG1 . THR A 1 528 ? -1.669  -12.127 35.583 1.00 15.47 ? 528  THR A OG1 1 
ATOM   4205 C CG2 . THR A 1 528 ? -1.425  -10.452 33.866 1.00 16.32 ? 528  THR A CG2 1 
ATOM   4206 N N   . PHE A 1 529 ? 0.984   -10.857 37.601 1.00 13.08 ? 529  PHE A N   1 
ATOM   4207 C CA  . PHE A 1 529 ? 1.007   -11.206 38.989 1.00 13.44 ? 529  PHE A CA  1 
ATOM   4208 C C   . PHE A 1 529 ? -0.062  -10.280 39.597 1.00 13.77 ? 529  PHE A C   1 
ATOM   4209 O O   . PHE A 1 529 ? -0.591  -9.424  38.916 1.00 14.05 ? 529  PHE A O   1 
ATOM   4210 C CB  . PHE A 1 529 ? 2.389   -10.904 39.617 1.00 13.03 ? 529  PHE A CB  1 
ATOM   4211 C CG  . PHE A 1 529 ? 2.550   -11.384 41.033 1.00 12.95 ? 529  PHE A CG  1 
ATOM   4212 C CD1 . PHE A 1 529 ? 2.685   -12.728 41.316 1.00 14.59 ? 529  PHE A CD1 1 
ATOM   4213 C CD2 . PHE A 1 529 ? 2.567   -10.478 42.086 1.00 14.79 ? 529  PHE A CD2 1 
ATOM   4214 C CE1 . PHE A 1 529 ? 2.834   -13.177 42.633 1.00 15.98 ? 529  PHE A CE1 1 
ATOM   4215 C CE2 . PHE A 1 529 ? 2.725   -10.895 43.399 1.00 14.99 ? 529  PHE A CE2 1 
ATOM   4216 C CZ  . PHE A 1 529 ? 2.839   -12.267 43.685 1.00 16.71 ? 529  PHE A CZ  1 
ATOM   4217 N N   . ALA A 1 530 ? -0.314  -10.428 40.874 1.00 13.54 ? 530  ALA A N   1 
ATOM   4218 C CA  . ALA A 1 530 ? -1.270  -9.550  41.572 1.00 15.14 ? 530  ALA A CA  1 
ATOM   4219 C C   . ALA A 1 530 ? -0.811  -8.098  41.417 1.00 15.11 ? 530  ALA A C   1 
ATOM   4220 O O   . ALA A 1 530 ? 0.337   -7.783  41.712 1.00 16.44 ? 530  ALA A O   1 
ATOM   4221 C CB  . ALA A 1 530 ? -1.278  -9.925  43.025 1.00 14.38 ? 530  ALA A CB  1 
ATOM   4222 N N   . GLY A 1 531 ? -1.684  -7.214  40.946 1.00 15.05 ? 531  GLY A N   1 
ATOM   4223 C CA  . GLY A 1 531 ? -1.270  -5.806  40.706 1.00 14.00 ? 531  GLY A CA  1 
ATOM   4224 C C   . GLY A 1 531 ? -0.914  -5.441  39.272 1.00 13.41 ? 531  GLY A C   1 
ATOM   4225 O O   . GLY A 1 531 ? -0.737  -4.279  38.980 1.00 12.89 ? 531  GLY A O   1 
ATOM   4226 N N   . SER A 1 532 ? -0.838  -6.418  38.361 1.00 13.38 ? 532  SER A N   1 
ATOM   4227 C CA  . SER A 1 532 ? -0.498  -6.134  36.957 1.00 12.89 ? 532  SER A CA  1 
ATOM   4228 C C   . SER A 1 532 ? -1.465  -5.191  36.257 1.00 13.17 ? 532  SER A C   1 
ATOM   4229 O O   . SER A 1 532 ? -1.068  -4.495  35.326 1.00 12.09 ? 532  SER A O   1 
ATOM   4230 C CB  . SER A 1 532 ? -0.330  -7.388  36.094 1.00 13.42 ? 532  SER A CB  1 
ATOM   4231 O OG  . SER A 1 532 ? 0.895   -8.076  36.395 1.00 13.48 ? 532  SER A OG  1 
ATOM   4232 N N   . GLY A 1 533 ? -2.731  -5.222  36.660 1.00 13.58 ? 533  GLY A N   1 
ATOM   4233 C CA  . GLY A 1 533 ? -3.731  -4.313  36.063 1.00 13.37 ? 533  GLY A CA  1 
ATOM   4234 C C   . GLY A 1 533 ? -3.452  -2.808  36.198 1.00 13.62 ? 533  GLY A C   1 
ATOM   4235 O O   . GLY A 1 533 ? -4.033  -1.980  35.454 1.00 13.22 ? 533  GLY A O   1 
ATOM   4236 N N   . LYS A 1 534 ? -2.628  -2.431  37.175 1.00 13.18 ? 534  LYS A N   1 
ATOM   4237 C CA  . LYS A 1 534 ? -2.188  -1.036  37.328 1.00 14.42 ? 534  LYS A CA  1 
ATOM   4238 C C   . LYS A 1 534 ? -1.456  -0.543  36.086 1.00 15.40 ? 534  LYS A C   1 
ATOM   4239 O O   . LYS A 1 534 ? -1.395  0.650   35.815 1.00 16.72 ? 534  LYS A O   1 
ATOM   4240 C CB  . LYS A 1 534 ? -1.320  -0.908  38.585 1.00 14.24 ? 534  LYS A CB  1 
ATOM   4241 C CG  . LYS A 1 534 ? -0.682  0.452   38.845 1.00 16.46 ? 534  LYS A CG  1 
ATOM   4242 C CD  . LYS A 1 534 ? -0.058  0.534   40.237 1.00 16.26 ? 534  LYS A CD  1 
ATOM   4243 C CE  . LYS A 1 534 ? 0.805   1.816   40.364 1.00 22.35 ? 534  LYS A CE  1 
ATOM   4244 N NZ  . LYS A 1 534 ? 1.553   1.825   41.655 1.00 23.67 ? 534  LYS A NZ  1 
ATOM   4245 N N   . PHE A 1 535 ? -0.875  -1.489  35.354 1.00 15.00 ? 535  PHE A N   1 
ATOM   4246 C CA  . PHE A 1 535 ? -0.052  -1.236  34.175 1.00 14.47 ? 535  PHE A CA  1 
ATOM   4247 C C   . PHE A 1 535 ? -0.644  -1.705  32.868 1.00 14.93 ? 535  PHE A C   1 
ATOM   4248 O O   . PHE A 1 535 ? -0.394  -1.097  31.826 1.00 15.28 ? 535  PHE A O   1 
ATOM   4249 C CB  . PHE A 1 535 ? 1.319   -1.910  34.389 1.00 15.42 ? 535  PHE A CB  1 
ATOM   4250 C CG  . PHE A 1 535 ? 1.963   -1.493  35.676 1.00 17.43 ? 535  PHE A CG  1 
ATOM   4251 C CD1 . PHE A 1 535 ? 2.578   -0.266  35.778 1.00 18.27 ? 535  PHE A CD1 1 
ATOM   4252 C CD2 . PHE A 1 535 ? 1.897   -2.300  36.808 1.00 20.96 ? 535  PHE A CD2 1 
ATOM   4253 C CE1 . PHE A 1 535 ? 3.126   0.164   36.998 1.00 20.94 ? 535  PHE A CE1 1 
ATOM   4254 C CE2 . PHE A 1 535 ? 2.440   -1.866  38.016 1.00 22.09 ? 535  PHE A CE2 1 
ATOM   4255 C CZ  . PHE A 1 535 ? 3.060   -0.630  38.094 1.00 18.69 ? 535  PHE A CZ  1 
ATOM   4256 N N   . ALA A 1 536 ? -1.434  -2.781  32.884 1.00 14.49 ? 536  ALA A N   1 
ATOM   4257 C CA  . ALA A 1 536 ? -1.693  -3.442  31.633 1.00 13.79 ? 536  ALA A CA  1 
ATOM   4258 C C   . ALA A 1 536 ? -3.061  -4.119  31.572 1.00 13.67 ? 536  ALA A C   1 
ATOM   4259 O O   . ALA A 1 536 ? -3.614  -4.461  32.598 1.00 13.67 ? 536  ALA A O   1 
ATOM   4260 C CB  . ALA A 1 536 ? -0.571  -4.493  31.371 1.00 15.04 ? 536  ALA A CB  1 
ATOM   4261 N N   . ALA A 1 537 ? -3.579  -4.254  30.359 1.00 12.73 ? 537  ALA A N   1 
ATOM   4262 C CA  . ALA A 1 537 ? -4.658  -5.187  30.018 1.00 13.37 ? 537  ALA A CA  1 
ATOM   4263 C C   . ALA A 1 537 ? -4.095  -6.629  29.911 1.00 13.97 ? 537  ALA A C   1 
ATOM   4264 O O   . ALA A 1 537 ? -2.882  -6.850  29.865 1.00 14.01 ? 537  ALA A O   1 
ATOM   4265 C CB  . ALA A 1 537 ? -5.258  -4.788  28.675 1.00 12.48 ? 537  ALA A CB  1 
ATOM   4266 N N   . HIS A 1 538 ? -4.993  -7.593  29.784 1.00 13.89 ? 538  HIS A N   1 
ATOM   4267 C CA  . HIS A 1 538 ? -4.597  -8.988  29.664 1.00 14.39 ? 538  HIS A CA  1 
ATOM   4268 C C   . HIS A 1 538 ? -5.479  -9.665  28.626 1.00 14.74 ? 538  HIS A C   1 
ATOM   4269 O O   . HIS A 1 538 ? -6.636  -9.276  28.437 1.00 14.47 ? 538  HIS A O   1 
ATOM   4270 C CB  . HIS A 1 538 ? -4.709  -9.681  31.042 1.00 13.48 ? 538  HIS A CB  1 
ATOM   4271 C CG  . HIS A 1 538 ? -4.500  -11.169 31.013 1.00 13.20 ? 538  HIS A CG  1 
ATOM   4272 N ND1 . HIS A 1 538 ? -3.313  -11.748 30.608 1.00 12.71 ? 538  HIS A ND1 1 
ATOM   4273 C CD2 . HIS A 1 538 ? -5.331  -12.198 31.334 1.00 12.15 ? 538  HIS A CD2 1 
ATOM   4274 C CE1 . HIS A 1 538 ? -3.412  -13.068 30.714 1.00 14.23 ? 538  HIS A CE1 1 
ATOM   4275 N NE2 . HIS A 1 538 ? -4.629  -13.368 31.150 1.00 14.70 ? 538  HIS A NE2 1 
ATOM   4276 N N   . TRP A 1 539 ? -4.932  -10.644 27.902 1.00 14.16 ? 539  TRP A N   1 
ATOM   4277 C CA  . TRP A 1 539 ? -5.787  -11.545 27.139 1.00 15.03 ? 539  TRP A CA  1 
ATOM   4278 C C   . TRP A 1 539 ? -5.586  -12.984 27.589 1.00 15.56 ? 539  TRP A C   1 
ATOM   4279 O O   . TRP A 1 539 ? -4.524  -13.354 28.112 1.00 15.60 ? 539  TRP A O   1 
ATOM   4280 C CB  . TRP A 1 539 ? -5.669  -11.372 25.594 1.00 15.54 ? 539  TRP A CB  1 
ATOM   4281 C CG  . TRP A 1 539 ? -4.587  -12.217 24.934 1.00 15.21 ? 539  TRP A CG  1 
ATOM   4282 C CD1 . TRP A 1 539 ? -4.771  -13.284 24.091 1.00 16.04 ? 539  TRP A CD1 1 
ATOM   4283 C CD2 . TRP A 1 539 ? -3.176  -12.033 25.047 1.00 15.83 ? 539  TRP A CD2 1 
ATOM   4284 N NE1 . TRP A 1 539 ? -3.555  -13.773 23.673 1.00 18.46 ? 539  TRP A NE1 1 
ATOM   4285 C CE2 . TRP A 1 539 ? -2.557  -13.028 24.245 1.00 17.13 ? 539  TRP A CE2 1 
ATOM   4286 C CE3 . TRP A 1 539 ? -2.377  -11.103 25.720 1.00 16.59 ? 539  TRP A CE3 1 
ATOM   4287 C CZ2 . TRP A 1 539 ? -1.169  -13.141 24.120 1.00 17.23 ? 539  TRP A CZ2 1 
ATOM   4288 C CZ3 . TRP A 1 539 ? -0.979  -11.230 25.616 1.00 16.80 ? 539  TRP A CZ3 1 
ATOM   4289 C CH2 . TRP A 1 539 ? -0.403  -12.249 24.822 1.00 16.30 ? 539  TRP A CH2 1 
ATOM   4290 N N   . LEU A 1 540 ? -6.598  -13.809 27.375 1.00 15.92 ? 540  LEU A N   1 
ATOM   4291 C CA  . LEU A 1 540 ? -6.633  -15.112 28.025 1.00 16.45 ? 540  LEU A CA  1 
ATOM   4292 C C   . LEU A 1 540 ? -5.774  -16.158 27.301 1.00 16.98 ? 540  LEU A C   1 
ATOM   4293 O O   . LEU A 1 540 ? -5.784  -17.320 27.666 1.00 18.31 ? 540  LEU A O   1 
ATOM   4294 C CB  . LEU A 1 540 ? -8.081  -15.576 28.210 1.00 16.59 ? 540  LEU A CB  1 
ATOM   4295 C CG  . LEU A 1 540 ? -8.861  -14.653 29.155 1.00 18.36 ? 540  LEU A CG  1 
ATOM   4296 C CD1 . LEU A 1 540 ? -10.336 -14.989 29.041 1.00 19.67 ? 540  LEU A CD1 1 
ATOM   4297 C CD2 . LEU A 1 540 ? -8.385  -14.732 30.608 1.00 17.61 ? 540  LEU A CD2 1 
ATOM   4298 N N   . GLY A 1 541 ? -5.002  -15.720 26.308 1.00 16.93 ? 541  GLY A N   1 
ATOM   4299 C CA  . GLY A 1 541 ? -3.931  -16.552 25.722 1.00 16.60 ? 541  GLY A CA  1 
ATOM   4300 C C   . GLY A 1 541 ? -4.360  -17.326 24.503 1.00 16.87 ? 541  GLY A C   1 
ATOM   4301 O O   . GLY A 1 541 ? -5.333  -16.944 23.837 1.00 15.90 ? 541  GLY A O   1 
ATOM   4302 N N   . ASP A 1 542 ? -3.655  -18.434 24.238 1.00 16.23 ? 542  ASP A N   1 
ATOM   4303 C CA  . ASP A 1 542 ? -3.767  -19.202 22.991 1.00 16.97 ? 542  ASP A CA  1 
ATOM   4304 C C   . ASP A 1 542 ? -4.909  -20.209 23.051 1.00 17.23 ? 542  ASP A C   1 
ATOM   4305 O O   . ASP A 1 542 ? -4.682  -21.413 23.158 1.00 17.57 ? 542  ASP A O   1 
ATOM   4306 C CB  . ASP A 1 542 ? -2.451  -19.952 22.692 1.00 17.19 ? 542  ASP A CB  1 
ATOM   4307 C CG  . ASP A 1 542 ? -1.270  -19.018 22.548 1.00 20.31 ? 542  ASP A CG  1 
ATOM   4308 O OD1 . ASP A 1 542 ? -1.480  -17.806 22.270 1.00 22.67 ? 542  ASP A OD1 1 
ATOM   4309 O OD2 . ASP A 1 542 ? -0.116  -19.521 22.672 1.00 24.54 ? 542  ASP A OD2 1 
ATOM   4310 N N   . ASN A 1 543 ? -6.136  -19.704 22.988 1.00 15.44 ? 543  ASN A N   1 
ATOM   4311 C CA  . ASN A 1 543 ? -7.303  -20.562 23.029 1.00 16.19 ? 543  ASN A CA  1 
ATOM   4312 C C   . ASN A 1 543 ? -7.501  -21.278 21.671 1.00 16.57 ? 543  ASN A C   1 
ATOM   4313 O O   . ASN A 1 543 ? -6.644  -21.233 20.779 1.00 17.60 ? 543  ASN A O   1 
ATOM   4314 C CB  . ASN A 1 543 ? -8.545  -19.742 23.472 1.00 13.95 ? 543  ASN A CB  1 
ATOM   4315 C CG  . ASN A 1 543 ? -8.972  -18.730 22.424 1.00 15.00 ? 543  ASN A CG  1 
ATOM   4316 O OD1 . ASN A 1 543 ? -8.273  -18.542 21.433 1.00 13.53 ? 543  ASN A OD1 1 
ATOM   4317 N ND2 . ASN A 1 543 ? -10.144 -18.095 22.605 1.00 14.42 ? 543  ASN A ND2 1 
ATOM   4318 N N   . THR A 1 544 ? -8.625  -21.974 21.529 1.00 17.81 ? 544  THR A N   1 
ATOM   4319 C CA  . THR A 1 544 ? -8.868  -22.820 20.367 1.00 18.26 ? 544  THR A CA  1 
ATOM   4320 C C   . THR A 1 544 ? -10.263 -22.502 19.866 1.00 18.51 ? 544  THR A C   1 
ATOM   4321 O O   . THR A 1 544 ? -11.108 -22.068 20.642 1.00 18.27 ? 544  THR A O   1 
ATOM   4322 C CB  . THR A 1 544 ? -8.716  -24.306 20.772 1.00 19.51 ? 544  THR A CB  1 
ATOM   4323 O OG1 . THR A 1 544 ? -7.459  -24.441 21.449 1.00 19.80 ? 544  THR A OG1 1 
ATOM   4324 C CG2 . THR A 1 544 ? -8.681  -25.247 19.570 1.00 19.97 ? 544  THR A CG2 1 
ATOM   4325 N N   . ALA A 1 545 ? -10.475 -22.668 18.563 1.00 17.57 ? 545  ALA A N   1 
ATOM   4326 C CA  . ALA A 1 545 ? -11.759 -22.433 17.929 1.00 17.71 ? 545  ALA A CA  1 
ATOM   4327 C C   . ALA A 1 545 ? -12.765 -23.559 18.216 1.00 18.56 ? 545  ALA A C   1 
ATOM   4328 O O   . ALA A 1 545 ? -13.101 -24.365 17.332 1.00 18.45 ? 545  ALA A O   1 
ATOM   4329 C CB  . ALA A 1 545 ? -11.546 -22.234 16.431 1.00 18.88 ? 545  ALA A CB  1 
ATOM   4330 N N   . THR A 1 546 ? -13.227 -23.621 19.465 1.00 17.11 ? 546  THR A N   1 
ATOM   4331 C CA  . THR A 1 546 ? -14.215 -24.645 19.861 1.00 17.51 ? 546  THR A CA  1 
ATOM   4332 C C   . THR A 1 546 ? -15.327 -24.015 20.696 1.00 16.16 ? 546  THR A C   1 
ATOM   4333 O O   . THR A 1 546 ? -15.157 -22.960 21.281 1.00 13.53 ? 546  THR A O   1 
ATOM   4334 C CB  . THR A 1 546 ? -13.649 -25.835 20.692 1.00 17.48 ? 546  THR A CB  1 
ATOM   4335 O OG1 . THR A 1 546 ? -13.456 -25.472 22.080 1.00 20.80 ? 546  THR A OG1 1 
ATOM   4336 C CG2 . THR A 1 546 ? -12.353 -26.421 20.109 1.00 18.70 ? 546  THR A CG2 1 
ATOM   4337 N N   . TRP A 1 547 ? -16.465 -24.690 20.764 1.00 16.40 ? 547  TRP A N   1 
ATOM   4338 C CA  . TRP A 1 547 ? -17.537 -24.191 21.599 1.00 16.88 ? 547  TRP A CA  1 
ATOM   4339 C C   . TRP A 1 547 ? -17.173 -24.214 23.094 1.00 16.94 ? 547  TRP A C   1 
ATOM   4340 O O   . TRP A 1 547 ? -17.633 -23.370 23.840 1.00 16.19 ? 547  TRP A O   1 
ATOM   4341 C CB  . TRP A 1 547 ? -18.822 -24.973 21.329 1.00 17.11 ? 547  TRP A CB  1 
ATOM   4342 C CG  . TRP A 1 547 ? -19.335 -24.650 19.952 1.00 17.54 ? 547  TRP A CG  1 
ATOM   4343 C CD1 . TRP A 1 547 ? -18.970 -25.247 18.766 1.00 19.93 ? 547  TRP A CD1 1 
ATOM   4344 C CD2 . TRP A 1 547 ? -20.241 -23.601 19.616 1.00 18.37 ? 547  TRP A CD2 1 
ATOM   4345 N NE1 . TRP A 1 547 ? -19.657 -24.670 17.717 1.00 20.09 ? 547  TRP A NE1 1 
ATOM   4346 C CE2 . TRP A 1 547 ? -20.433 -23.645 18.211 1.00 19.54 ? 547  TRP A CE2 1 
ATOM   4347 C CE3 . TRP A 1 547 ? -20.933 -22.634 20.371 1.00 17.38 ? 547  TRP A CE3 1 
ATOM   4348 C CZ2 . TRP A 1 547 ? -21.284 -22.742 17.534 1.00 19.90 ? 547  TRP A CZ2 1 
ATOM   4349 C CZ3 . TRP A 1 547 ? -21.785 -21.743 19.707 1.00 17.79 ? 547  TRP A CZ3 1 
ATOM   4350 C CH2 . TRP A 1 547 ? -21.953 -21.804 18.295 1.00 18.05 ? 547  TRP A CH2 1 
ATOM   4351 N N   . ASP A 1 548 ? -16.356 -25.176 23.525 1.00 16.17 ? 548  ASP A N   1 
ATOM   4352 C CA  . ASP A 1 548 ? -15.908 -25.222 24.917 1.00 16.89 ? 548  ASP A CA  1 
ATOM   4353 C C   . ASP A 1 548 ? -15.161 -23.944 25.270 1.00 16.76 ? 548  ASP A C   1 
ATOM   4354 O O   . ASP A 1 548 ? -15.468 -23.342 26.280 1.00 15.80 ? 548  ASP A O   1 
ATOM   4355 C CB  . ASP A 1 548 ? -14.966 -26.389 25.177 1.00 17.56 ? 548  ASP A CB  1 
ATOM   4356 C CG  . ASP A 1 548 ? -15.693 -27.684 25.466 1.00 22.25 ? 548  ASP A CG  1 
ATOM   4357 O OD1 . ASP A 1 548 ? -16.860 -27.666 25.937 1.00 23.65 ? 548  ASP A OD1 1 
ATOM   4358 O OD2 . ASP A 1 548 ? -15.042 -28.722 25.253 1.00 26.13 ? 548  ASP A OD2 1 
ATOM   4359 N N   . ASP A 1 549 ? -14.198 -23.551 24.423 1.00 15.51 ? 549  ASP A N   1 
ATOM   4360 C CA  . ASP A 1 549 ? -13.399 -22.329 24.648 1.00 15.57 ? 549  ASP A CA  1 
ATOM   4361 C C   . ASP A 1 549 ? -14.279 -21.076 24.694 1.00 14.97 ? 549  ASP A C   1 
ATOM   4362 O O   . ASP A 1 549 ? -14.059 -20.189 25.511 1.00 13.92 ? 549  ASP A O   1 
ATOM   4363 C CB  . ASP A 1 549 ? -12.322 -22.144 23.565 1.00 15.37 ? 549  ASP A CB  1 
ATOM   4364 C CG  . ASP A 1 549 ? -11.179 -23.189 23.645 1.00 18.74 ? 549  ASP A CG  1 
ATOM   4365 O OD1 . ASP A 1 549 ? -10.030 -22.839 24.035 1.00 20.75 ? 549  ASP A OD1 1 
ATOM   4366 O OD2 . ASP A 1 549 ? -11.424 -24.368 23.271 1.00 24.17 ? 549  ASP A OD2 1 
ATOM   4367 N N   . LEU A 1 550 ? -15.296 -21.010 23.836 1.00 14.28 ? 550  LEU A N   1 
ATOM   4368 C CA  . LEU A 1 550 ? -16.248 -19.900 23.916 1.00 15.26 ? 550  LEU A CA  1 
ATOM   4369 C C   . LEU A 1 550 ? -16.909 -19.831 25.322 1.00 15.75 ? 550  LEU A C   1 
ATOM   4370 O O   . LEU A 1 550 ? -16.939 -18.782 25.964 1.00 16.10 ? 550  LEU A O   1 
ATOM   4371 C CB  . LEU A 1 550 ? -17.298 -20.062 22.806 1.00 15.36 ? 550  LEU A CB  1 
ATOM   4372 C CG  . LEU A 1 550 ? -18.508 -19.144 22.888 1.00 17.26 ? 550  LEU A CG  1 
ATOM   4373 C CD1 . LEU A 1 550 ? -18.083 -17.741 22.625 1.00 18.75 ? 550  LEU A CD1 1 
ATOM   4374 C CD2 . LEU A 1 550 ? -19.616 -19.585 21.941 1.00 18.26 ? 550  LEU A CD2 1 
ATOM   4375 N N   . ARG A 1 551 ? -17.455 -20.958 25.797 1.00 16.23 ? 551  ARG A N   1 
ATOM   4376 C CA  . ARG A 1 551 ? -18.078 -21.008 27.118 1.00 16.17 ? 551  ARG A CA  1 
ATOM   4377 C C   . ARG A 1 551 ? -17.060 -20.693 28.241 1.00 15.79 ? 551  ARG A C   1 
ATOM   4378 O O   . ARG A 1 551 ? -17.371 -19.978 29.190 1.00 17.16 ? 551  ARG A O   1 
ATOM   4379 C CB  . ARG A 1 551 ? -18.701 -22.388 27.339 1.00 16.67 ? 551  ARG A CB  1 
ATOM   4380 C CG  . ARG A 1 551 ? -19.987 -22.613 26.508 1.00 15.22 ? 551  ARG A CG  1 
ATOM   4381 C CD  . ARG A 1 551 ? -20.615 -23.989 26.796 1.00 18.92 ? 551  ARG A CD  1 
ATOM   4382 N NE  . ARG A 1 551 ? -19.843 -25.124 26.291 1.00 19.84 ? 551  ARG A NE  1 
ATOM   4383 C CZ  . ARG A 1 551 ? -19.994 -25.710 25.096 1.00 22.17 ? 551  ARG A CZ  1 
ATOM   4384 N NH1 . ARG A 1 551 ? -20.874 -25.276 24.192 1.00 19.45 ? 551  ARG A NH1 1 
ATOM   4385 N NH2 . ARG A 1 551 ? -19.252 -26.757 24.790 1.00 21.46 ? 551  ARG A NH2 1 
ATOM   4386 N N   . TRP A 1 552 ? -15.855 -21.218 28.119 1.00 15.14 ? 552  TRP A N   1 
ATOM   4387 C CA  . TRP A 1 552 ? -14.844 -21.080 29.192 1.00 15.29 ? 552  TRP A CA  1 
ATOM   4388 C C   . TRP A 1 552 ? -14.314 -19.657 29.313 1.00 15.98 ? 552  TRP A C   1 
ATOM   4389 O O   . TRP A 1 552 ? -13.686 -19.291 30.336 1.00 16.13 ? 552  TRP A O   1 
ATOM   4390 C CB  . TRP A 1 552 ? -13.670 -22.009 28.900 1.00 15.80 ? 552  TRP A CB  1 
ATOM   4391 C CG  . TRP A 1 552 ? -14.037 -23.450 28.997 1.00 17.75 ? 552  TRP A CG  1 
ATOM   4392 C CD1 . TRP A 1 552 ? -15.103 -23.975 29.648 1.00 17.57 ? 552  TRP A CD1 1 
ATOM   4393 C CD2 . TRP A 1 552 ? -13.290 -24.556 28.467 1.00 18.81 ? 552  TRP A CD2 1 
ATOM   4394 N NE1 . TRP A 1 552 ? -15.088 -25.354 29.534 1.00 16.81 ? 552  TRP A NE1 1 
ATOM   4395 C CE2 . TRP A 1 552 ? -13.988 -25.722 28.799 1.00 19.83 ? 552  TRP A CE2 1 
ATOM   4396 C CE3 . TRP A 1 552 ? -12.127 -24.658 27.693 1.00 18.01 ? 552  TRP A CE3 1 
ATOM   4397 C CZ2 . TRP A 1 552 ? -13.534 -27.003 28.431 1.00 19.32 ? 552  TRP A CZ2 1 
ATOM   4398 C CZ3 . TRP A 1 552 ? -11.684 -25.944 27.307 1.00 18.52 ? 552  TRP A CZ3 1 
ATOM   4399 C CH2 . TRP A 1 552 ? -12.399 -27.081 27.684 1.00 18.97 ? 552  TRP A CH2 1 
ATOM   4400 N N   . SER A 1 553 ? -14.526 -18.868 28.269 1.00 15.72 ? 553  SER A N   1 
ATOM   4401 C CA  . SER A 1 553 ? -14.052 -17.459 28.278 1.00 16.68 ? 553  SER A CA  1 
ATOM   4402 C C   . SER A 1 553 ? -14.707 -16.590 29.342 1.00 15.83 ? 553  SER A C   1 
ATOM   4403 O O   . SER A 1 553 ? -14.060 -15.682 29.859 1.00 14.34 ? 553  SER A O   1 
ATOM   4404 C CB  . SER A 1 553 ? -14.208 -16.791 26.912 1.00 16.85 ? 553  SER A CB  1 
ATOM   4405 O OG  . SER A 1 553 ? -15.591 -16.506 26.632 1.00 15.60 ? 553  SER A OG  1 
ATOM   4406 N N   . ILE A 1 554 ? -15.978 -16.851 29.665 1.00 15.54 ? 554  ILE A N   1 
ATOM   4407 C CA  . ILE A 1 554 ? -16.694 -15.951 30.547 1.00 14.89 ? 554  ILE A CA  1 
ATOM   4408 C C   . ILE A 1 554 ? -16.162 -16.040 31.970 1.00 15.08 ? 554  ILE A C   1 
ATOM   4409 O O   . ILE A 1 554 ? -15.857 -15.016 32.545 1.00 14.98 ? 554  ILE A O   1 
ATOM   4410 C CB  . ILE A 1 554 ? -18.251 -16.126 30.492 1.00 15.73 ? 554  ILE A CB  1 
ATOM   4411 C CG1 . ILE A 1 554 ? -18.745 -15.665 29.119 1.00 17.66 ? 554  ILE A CG1 1 
ATOM   4412 C CG2 . ILE A 1 554 ? -18.879 -15.239 31.546 1.00 15.41 ? 554  ILE A CG2 1 
ATOM   4413 C CD1 . ILE A 1 554 ? -20.175 -16.177 28.748 1.00 15.65 ? 554  ILE A CD1 1 
ATOM   4414 N N   . PRO A 1 555 ? -16.024 -17.253 32.536 1.00 14.73 ? 555  PRO A N   1 
ATOM   4415 C CA  . PRO A 1 555 ? -15.367 -17.202 33.852 1.00 16.08 ? 555  PRO A CA  1 
ATOM   4416 C C   . PRO A 1 555 ? -13.999 -16.564 33.904 1.00 15.83 ? 555  PRO A C   1 
ATOM   4417 O O   . PRO A 1 555 ? -13.687 -15.928 34.922 1.00 15.18 ? 555  PRO A O   1 
ATOM   4418 C CB  . PRO A 1 555 ? -15.261 -18.675 34.261 1.00 16.07 ? 555  PRO A CB  1 
ATOM   4419 C CG  . PRO A 1 555 ? -16.431 -19.338 33.605 1.00 14.65 ? 555  PRO A CG  1 
ATOM   4420 C CD  . PRO A 1 555 ? -16.478 -18.626 32.225 1.00 15.18 ? 555  PRO A CD  1 
ATOM   4421 N N   . GLY A 1 556 ? -13.189 -16.752 32.857 1.00 16.00 ? 556  GLY A N   1 
ATOM   4422 C CA  . GLY A 1 556 ? -11.835 -16.153 32.787 1.00 14.40 ? 556  GLY A CA  1 
ATOM   4423 C C   . GLY A 1 556 ? -11.917 -14.636 32.821 1.00 15.00 ? 556  GLY A C   1 
ATOM   4424 O O   . GLY A 1 556 ? -11.147 -14.007 33.512 1.00 13.90 ? 556  GLY A O   1 
ATOM   4425 N N   . VAL A 1 557 ? -12.880 -14.053 32.085 1.00 13.43 ? 557  VAL A N   1 
ATOM   4426 C CA  . VAL A 1 557 ? -13.067 -12.607 32.069 1.00 13.19 ? 557  VAL A CA  1 
ATOM   4427 C C   . VAL A 1 557 ? -13.515 -12.101 33.452 1.00 13.07 ? 557  VAL A C   1 
ATOM   4428 O O   . VAL A 1 557 ? -13.029 -11.069 33.945 1.00 11.84 ? 557  VAL A O   1 
ATOM   4429 C CB  . VAL A 1 557 ? -14.111 -12.187 30.961 1.00 13.33 ? 557  VAL A CB  1 
ATOM   4430 C CG1 . VAL A 1 557 ? -14.607 -10.782 31.166 1.00 15.52 ? 557  VAL A CG1 1 
ATOM   4431 C CG2 . VAL A 1 557 ? -13.501 -12.301 29.590 1.00 13.49 ? 557  VAL A CG2 1 
ATOM   4432 N N   . LEU A 1 558 ? -14.479 -12.793 34.081 1.00 11.94 ? 558  LEU A N   1 
ATOM   4433 C CA  . LEU A 1 558 ? -14.935 -12.379 35.422 1.00 11.63 ? 558  LEU A CA  1 
ATOM   4434 C C   . LEU A 1 558 ? -13.835 -12.442 36.487 1.00 12.28 ? 558  LEU A C   1 
ATOM   4435 O O   . LEU A 1 558 ? -13.706 -11.554 37.345 1.00 11.39 ? 558  LEU A O   1 
ATOM   4436 C CB  . LEU A 1 558 ? -16.097 -13.291 35.852 1.00 12.47 ? 558  LEU A CB  1 
ATOM   4437 C CG  . LEU A 1 558 ? -17.328 -13.119 34.975 1.00 13.02 ? 558  LEU A CG  1 
ATOM   4438 C CD1 . LEU A 1 558 ? -18.379 -14.155 35.346 1.00 11.98 ? 558  LEU A CD1 1 
ATOM   4439 C CD2 . LEU A 1 558 ? -17.882 -11.703 35.047 1.00 17.26 ? 558  LEU A CD2 1 
ATOM   4440 N N   . GLU A 1 559 ? -13.035 -13.510 36.436 1.00 10.94 ? 559  GLU A N   1 
ATOM   4441 C CA  . GLU A 1 559 ? -11.986 -13.674 37.430 1.00 11.69 ? 559  GLU A CA  1 
ATOM   4442 C C   . GLU A 1 559 ? -10.953 -12.558 37.272 1.00 11.49 ? 559  GLU A C   1 
ATOM   4443 O O   . GLU A 1 559 ? -10.478 -12.045 38.273 1.00 12.11 ? 559  GLU A O   1 
ATOM   4444 C CB  . GLU A 1 559 ? -11.326 -15.053 37.260 1.00 11.81 ? 559  GLU A CB  1 
ATOM   4445 C CG  . GLU A 1 559 ? -12.216 -16.218 37.753 1.00 14.64 ? 559  GLU A CG  1 
ATOM   4446 C CD  . GLU A 1 559 ? -11.866 -17.559 37.113 1.00 20.98 ? 559  GLU A CD  1 
ATOM   4447 O OE1 . GLU A 1 559 ? -10.924 -17.597 36.268 1.00 19.72 ? 559  GLU A OE1 1 
ATOM   4448 O OE2 . GLU A 1 559 ? -12.588 -18.568 37.413 1.00 20.70 ? 559  GLU A OE2 1 
ATOM   4449 N N   . PHE A 1 560 ? -10.560 -12.208 36.044 1.00 10.44 ? 560  PHE A N   1 
ATOM   4450 C CA  . PHE A 1 560 ? -9.571  -11.085 35.905 1.00 11.19 ? 560  PHE A CA  1 
ATOM   4451 C C   . PHE A 1 560 ? -10.114 -9.757  36.346 1.00 12.29 ? 560  PHE A C   1 
ATOM   4452 O O   . PHE A 1 560 ? -9.372  -8.877  36.761 1.00 11.52 ? 560  PHE A O   1 
ATOM   4453 C CB  . PHE A 1 560 ? -8.951  -11.048 34.515 1.00 10.10 ? 560  PHE A CB  1 
ATOM   4454 C CG  . PHE A 1 560 ? -7.794  -11.988 34.435 1.00 13.68 ? 560  PHE A CG  1 
ATOM   4455 C CD1 . PHE A 1 560 ? -7.987  -13.306 34.105 1.00 14.36 ? 560  PHE A CD1 1 
ATOM   4456 C CD2 . PHE A 1 560 ? -6.533  -11.556 34.850 1.00 13.94 ? 560  PHE A CD2 1 
ATOM   4457 C CE1 . PHE A 1 560 ? -6.923  -14.220 34.138 1.00 16.69 ? 560  PHE A CE1 1 
ATOM   4458 C CE2 . PHE A 1 560 ? -5.431  -12.463 34.861 1.00 14.14 ? 560  PHE A CE2 1 
ATOM   4459 C CZ  . PHE A 1 560 ? -5.649  -13.775 34.501 1.00 13.18 ? 560  PHE A CZ  1 
ATOM   4460 N N   . ASN A 1 561 ? -11.431 -9.598  36.259 1.00 11.41 ? 561  ASN A N   1 
ATOM   4461 C CA  . ASN A 1 561 ? -12.045 -8.412  36.870 1.00 12.60 ? 561  ASN A CA  1 
ATOM   4462 C C   . ASN A 1 561 ? -11.891 -8.399  38.405 1.00 12.48 ? 561  ASN A C   1 
ATOM   4463 O O   . ASN A 1 561 ? -11.607 -7.348  39.007 1.00 13.89 ? 561  ASN A O   1 
ATOM   4464 C CB  . ASN A 1 561 ? -13.511 -8.272  36.417 1.00 11.79 ? 561  ASN A CB  1 
ATOM   4465 C CG  . ASN A 1 561 ? -13.605 -7.508  35.114 1.00 14.00 ? 561  ASN A CG  1 
ATOM   4466 O OD1 . ASN A 1 561 ? -13.972 -6.323  35.109 1.00 14.73 ? 561  ASN A OD1 1 
ATOM   4467 N ND2 . ASN A 1 561 ? -13.150 -8.138  34.013 1.00 15.59 ? 561  ASN A ND2 1 
ATOM   4468 N N   . LEU A 1 562 ? -12.038 -9.562  39.038 1.00 12.92 ? 562  LEU A N   1 
ATOM   4469 C CA  . LEU A 1 562 ? -11.785 -9.669  40.470 1.00 12.73 ? 562  LEU A CA  1 
ATOM   4470 C C   . LEU A 1 562 ? -10.345 -9.303  40.731 1.00 12.67 ? 562  LEU A C   1 
ATOM   4471 O O   . LEU A 1 562 ? -10.028 -8.739  41.760 1.00 12.37 ? 562  LEU A O   1 
ATOM   4472 C CB  . LEU A 1 562 ? -11.955 -11.096 40.962 1.00 13.80 ? 562  LEU A CB  1 
ATOM   4473 C CG  . LEU A 1 562 ? -13.279 -11.802 40.899 1.00 15.54 ? 562  LEU A CG  1 
ATOM   4474 C CD1 . LEU A 1 562 ? -13.056 -13.114 41.674 1.00 17.37 ? 562  LEU A CD1 1 
ATOM   4475 C CD2 . LEU A 1 562 ? -14.413 -10.911 41.492 1.00 14.38 ? 562  LEU A CD2 1 
ATOM   4476 N N   . PHE A 1 563 ? -9.465  -9.701  39.820 1.00 12.75 ? 563  PHE A N   1 
ATOM   4477 C CA  . PHE A 1 563 ? -8.010  -9.446  39.997 1.00 13.06 ? 563  PHE A CA  1 
ATOM   4478 C C   . PHE A 1 563 ? -7.578  -7.999  39.675 1.00 14.16 ? 563  PHE A C   1 
ATOM   4479 O O   . PHE A 1 563 ? -6.370  -7.643  39.725 1.00 13.34 ? 563  PHE A O   1 
ATOM   4480 C CB  . PHE A 1 563 ? -7.217  -10.457 39.109 1.00 12.20 ? 563  PHE A CB  1 
ATOM   4481 C CG  . PHE A 1 563 ? -7.558  -11.914 39.363 1.00 11.34 ? 563  PHE A CG  1 
ATOM   4482 C CD1 . PHE A 1 563 ? -7.919  -12.370 40.646 1.00 13.53 ? 563  PHE A CD1 1 
ATOM   4483 C CD2 . PHE A 1 563 ? -7.432  -12.844 38.321 1.00 13.09 ? 563  PHE A CD2 1 
ATOM   4484 C CE1 . PHE A 1 563 ? -8.195  -13.701 40.862 1.00 14.22 ? 563  PHE A CE1 1 
ATOM   4485 C CE2 . PHE A 1 563 ? -7.737  -14.200 38.530 1.00 16.78 ? 563  PHE A CE2 1 
ATOM   4486 C CZ  . PHE A 1 563 ? -8.100  -14.612 39.797 1.00 13.19 ? 563  PHE A CZ  1 
ATOM   4487 N N   . GLY A 1 564 ? -8.524  -7.121  39.364 1.00 12.41 ? 564  GLY A N   1 
ATOM   4488 C CA  . GLY A 1 564 ? -8.145  -5.759  39.005 1.00 13.14 ? 564  GLY A CA  1 
ATOM   4489 C C   . GLY A 1 564 ? -7.492  -5.594  37.646 1.00 13.15 ? 564  GLY A C   1 
ATOM   4490 O O   . GLY A 1 564 ? -6.732  -4.656  37.441 1.00 14.08 ? 564  GLY A O   1 
ATOM   4491 N N   . ILE A 1 565 ? -7.748  -6.527  36.734 1.00 11.41 ? 565  ILE A N   1 
ATOM   4492 C CA  . ILE A 1 565 ? -7.355  -6.394  35.331 1.00 12.63 ? 565  ILE A CA  1 
ATOM   4493 C C   . ILE A 1 565 ? -8.644  -6.425  34.502 1.00 12.61 ? 565  ILE A C   1 
ATOM   4494 O O   . ILE A 1 565 ? -8.944  -7.397  33.813 1.00 12.85 ? 565  ILE A O   1 
ATOM   4495 C CB  . ILE A 1 565 ? -6.399  -7.538  34.932 1.00 13.59 ? 565  ILE A CB  1 
ATOM   4496 C CG1 . ILE A 1 565 ? -5.279  -7.615  35.981 1.00 13.30 ? 565  ILE A CG1 1 
ATOM   4497 C CG2 . ILE A 1 565 ? -5.923  -7.348  33.487 1.00 14.89 ? 565  ILE A CG2 1 
ATOM   4498 C CD1 . ILE A 1 565 ? -4.179  -8.767  35.771 1.00 15.59 ? 565  ILE A CD1 1 
ATOM   4499 N N   . PRO A 1 566 ? -9.433  -5.337  34.593 1.00 12.99 ? 566  PRO A N   1 
ATOM   4500 C CA  . PRO A 1 566 ? -10.742 -5.395  33.962 1.00 13.11 ? 566  PRO A CA  1 
ATOM   4501 C C   . PRO A 1 566 ? -10.751 -5.431  32.438 1.00 12.66 ? 566  PRO A C   1 
ATOM   4502 O O   . PRO A 1 566 ? -11.679 -5.961  31.873 1.00 11.82 ? 566  PRO A O   1 
ATOM   4503 C CB  . PRO A 1 566 ? -11.458 -4.151  34.491 1.00 12.24 ? 566  PRO A CB  1 
ATOM   4504 C CG  . PRO A 1 566 ? -10.342 -3.169  34.828 1.00 12.78 ? 566  PRO A CG  1 
ATOM   4505 C CD  . PRO A 1 566 ? -9.182  -4.064  35.288 1.00 13.10 ? 566  PRO A CD  1 
ATOM   4506 N N   . MET A 1 567 ? -9.763  -4.832  31.789 1.00 12.19 ? 567  MET A N   1 
ATOM   4507 C CA  . MET A 1 567 ? -9.627  -4.933  30.355 1.00 13.88 ? 567  MET A CA  1 
ATOM   4508 C C   . MET A 1 567 ? -9.028  -6.301  30.029 1.00 12.96 ? 567  MET A C   1 
ATOM   4509 O O   . MET A 1 567 ? -7.794  -6.465  30.021 1.00 14.35 ? 567  MET A O   1 
ATOM   4510 C CB  . MET A 1 567 ? -8.750  -3.785  29.814 1.00 12.81 ? 567  MET A CB  1 
ATOM   4511 C CG  . MET A 1 567 ? -8.839  -3.737  28.284 1.00 16.71 ? 567  MET A CG  1 
ATOM   4512 S SD  . MET A 1 567 ? -8.249  -2.207  27.600 1.00 20.26 ? 567  MET A SD  1 
ATOM   4513 C CE  . MET A 1 567 ? -9.825  -1.353  27.520 1.00 19.00 ? 567  MET A CE  1 
ATOM   4514 N N   . VAL A 1 568 ? -9.909  -7.288  29.823 1.00 10.79 ? 568  VAL A N   1 
ATOM   4515 C CA  . VAL A 1 568 ? -9.536  -8.676  29.630 1.00 12.08 ? 568  VAL A CA  1 
ATOM   4516 C C   . VAL A 1 568 ? -10.514 -9.260  28.614 1.00 13.16 ? 568  VAL A C   1 
ATOM   4517 O O   . VAL A 1 568 ? -11.680 -8.849  28.540 1.00 12.24 ? 568  VAL A O   1 
ATOM   4518 C CB  . VAL A 1 568 ? -9.495  -9.495  30.981 1.00 10.78 ? 568  VAL A CB  1 
ATOM   4519 C CG1 . VAL A 1 568 ? -10.880 -9.444  31.706 1.00 9.91  ? 568  VAL A CG1 1 
ATOM   4520 C CG2 . VAL A 1 568 ? -8.984  -10.970 30.779 1.00 11.58 ? 568  VAL A CG2 1 
ATOM   4521 N N   . GLY A 1 569 ? -10.028 -10.219 27.842 1.00 13.61 ? 569  GLY A N   1 
ATOM   4522 C CA  . GLY A 1 569 ? -10.810 -10.837 26.790 1.00 14.94 ? 569  GLY A CA  1 
ATOM   4523 C C   . GLY A 1 569 ? -10.011 -12.005 26.243 1.00 15.04 ? 569  GLY A C   1 
ATOM   4524 O O   . GLY A 1 569 ? -8.783  -12.045 26.438 1.00 16.46 ? 569  GLY A O   1 
ATOM   4525 N N   . PRO A 1 570 ? -10.678 -12.956 25.586 1.00 15.49 ? 570  PRO A N   1 
ATOM   4526 C CA  . PRO A 1 570 ? -9.941  -14.001 24.888 1.00 15.66 ? 570  PRO A CA  1 
ATOM   4527 C C   . PRO A 1 570 ? -9.622  -13.555 23.435 1.00 16.42 ? 570  PRO A C   1 
ATOM   4528 O O   . PRO A 1 570 ? -10.021 -12.446 22.989 1.00 16.61 ? 570  PRO A O   1 
ATOM   4529 C CB  . PRO A 1 570 ? -10.950 -15.152 24.860 1.00 15.76 ? 570  PRO A CB  1 
ATOM   4530 C CG  . PRO A 1 570 ? -12.306 -14.415 24.644 1.00 15.79 ? 570  PRO A CG  1 
ATOM   4531 C CD  . PRO A 1 570 ? -12.148 -13.117 25.438 1.00 15.72 ? 570  PRO A CD  1 
ATOM   4532 N N   . ASP A 1 571 ? -9.002  -14.449 22.671 1.00 16.29 ? 571  ASP A N   1 
ATOM   4533 C CA  . ASP A 1 571 ? -8.920  -14.248 21.211 1.00 15.67 ? 571  ASP A CA  1 
ATOM   4534 C C   . ASP A 1 571 ? -10.287 -14.619 20.616 1.00 16.22 ? 571  ASP A C   1 
ATOM   4535 O O   . ASP A 1 571 ? -10.633 -15.787 20.555 1.00 16.51 ? 571  ASP A O   1 
ATOM   4536 C CB  . ASP A 1 571 ? -7.873  -15.151 20.621 1.00 14.90 ? 571  ASP A CB  1 
ATOM   4537 C CG  . ASP A 1 571 ? -6.455  -14.719 20.978 1.00 15.68 ? 571  ASP A CG  1 
ATOM   4538 O OD1 . ASP A 1 571 ? -6.255  -13.543 21.348 1.00 18.71 ? 571  ASP A OD1 1 
ATOM   4539 O OD2 . ASP A 1 571 ? -5.539  -15.558 20.850 1.00 19.16 ? 571  ASP A OD2 1 
ATOM   4540 N N   . ILE A 1 572 ? -11.053 -13.627 20.184 1.00 16.74 ? 572  ILE A N   1 
ATOM   4541 C CA  . ILE A 1 572 ? -12.403 -13.897 19.701 1.00 16.05 ? 572  ILE A CA  1 
ATOM   4542 C C   . ILE A 1 572 ? -12.286 -14.782 18.439 1.00 16.76 ? 572  ILE A C   1 
ATOM   4543 O O   . ILE A 1 572 ? -11.432 -14.526 17.581 1.00 17.72 ? 572  ILE A O   1 
ATOM   4544 C CB  . ILE A 1 572 ? -13.166 -12.602 19.361 1.00 16.22 ? 572  ILE A CB  1 
ATOM   4545 C CG1 . ILE A 1 572 ? -13.435 -11.786 20.644 1.00 15.86 ? 572  ILE A CG1 1 
ATOM   4546 C CG2 . ILE A 1 572 ? -14.474 -12.929 18.559 1.00 16.06 ? 572  ILE A CG2 1 
ATOM   4547 C CD1 . ILE A 1 572 ? -13.923 -10.358 20.383 1.00 16.35 ? 572  ILE A CD1 1 
ATOM   4548 N N   . CYS A 1 573 ? -13.148 -15.802 18.355 1.00 16.67 ? 573  CYS A N   1 
ATOM   4549 C CA  . CYS A 1 573 ? -13.212 -16.798 17.260 1.00 16.80 ? 573  CYS A CA  1 
ATOM   4550 C C   . CYS A 1 573 ? -12.210 -17.925 17.408 1.00 17.51 ? 573  CYS A C   1 
ATOM   4551 O O   . CYS A 1 573 ? -12.373 -18.984 16.798 1.00 18.70 ? 573  CYS A O   1 
ATOM   4552 C CB  . CYS A 1 573 ? -13.186 -16.178 15.851 1.00 17.55 ? 573  CYS A CB  1 
ATOM   4553 S SG  . CYS A 1 573 ? -14.692 -15.168 15.629 1.00 19.05 ? 573  CYS A SG  1 
ATOM   4554 N N   . GLY A 1 574 ? -11.214 -17.715 18.251 1.00 16.46 ? 574  GLY A N   1 
ATOM   4555 C CA  . GLY A 1 574 ? -10.311 -18.787 18.652 1.00 17.37 ? 574  GLY A CA  1 
ATOM   4556 C C   . GLY A 1 574 ? -8.982  -18.652 17.936 1.00 17.76 ? 574  GLY A C   1 
ATOM   4557 O O   . GLY A 1 574 ? -8.966  -18.566 16.728 1.00 18.54 ? 574  GLY A O   1 
ATOM   4558 N N   . PHE A 1 575 ? -7.890  -18.700 18.695 1.00 17.08 ? 575  PHE A N   1 
ATOM   4559 C CA  . PHE A 1 575 ? -6.530  -18.567 18.148 1.00 17.86 ? 575  PHE A CA  1 
ATOM   4560 C C   . PHE A 1 575 ? -6.206  -19.812 17.304 1.00 17.77 ? 575  PHE A C   1 
ATOM   4561 O O   . PHE A 1 575 ? -6.131  -19.702 16.081 1.00 18.21 ? 575  PHE A O   1 
ATOM   4562 C CB  . PHE A 1 575 ? -5.547  -18.360 19.293 1.00 15.93 ? 575  PHE A CB  1 
ATOM   4563 C CG  . PHE A 1 575 ? -4.088  -18.347 18.891 1.00 17.54 ? 575  PHE A CG  1 
ATOM   4564 C CD1 . PHE A 1 575 ? -3.500  -17.197 18.329 1.00 14.52 ? 575  PHE A CD1 1 
ATOM   4565 C CD2 . PHE A 1 575 ? -3.299  -19.457 19.135 1.00 17.87 ? 575  PHE A CD2 1 
ATOM   4566 C CE1 . PHE A 1 575 ? -2.122  -17.178 18.001 1.00 19.24 ? 575  PHE A CE1 1 
ATOM   4567 C CE2 . PHE A 1 575 ? -1.916  -19.458 18.786 1.00 17.75 ? 575  PHE A CE2 1 
ATOM   4568 C CZ  . PHE A 1 575 ? -1.332  -18.307 18.251 1.00 16.83 ? 575  PHE A CZ  1 
ATOM   4569 N N   . ALA A 1 576 ? -6.059  -20.986 17.933 1.00 17.64 ? 576  ALA A N   1 
ATOM   4570 C CA  . ALA A 1 576 ? -5.751  -22.236 17.201 1.00 18.71 ? 576  ALA A CA  1 
ATOM   4571 C C   . ALA A 1 576 ? -6.969  -22.788 16.413 1.00 18.71 ? 576  ALA A C   1 
ATOM   4572 O O   . ALA A 1 576 ? -8.074  -22.749 16.904 1.00 20.18 ? 576  ALA A O   1 
ATOM   4573 C CB  . ALA A 1 576 ? -5.231  -23.316 18.176 1.00 17.68 ? 576  ALA A CB  1 
ATOM   4574 N N   . LEU A 1 577 ? -6.727  -23.284 15.190 1.00 18.92 ? 577  LEU A N   1 
ATOM   4575 C CA  . LEU A 1 577 ? -7.706  -23.955 14.330 1.00 19.83 ? 577  LEU A CA  1 
ATOM   4576 C C   . LEU A 1 577 ? -8.504  -22.985 13.455 1.00 20.01 ? 577  LEU A C   1 
ATOM   4577 O O   . LEU A 1 577 ? -8.655  -21.804 13.790 1.00 18.46 ? 577  LEU A O   1 
ATOM   4578 C CB  . LEU A 1 577 ? -8.665  -24.875 15.135 1.00 19.47 ? 577  LEU A CB  1 
ATOM   4579 C CG  . LEU A 1 577 ? -8.230  -26.283 15.545 1.00 22.90 ? 577  LEU A CG  1 
ATOM   4580 C CD1 . LEU A 1 577 ? -6.730  -26.456 15.765 1.00 24.96 ? 577  LEU A CD1 1 
ATOM   4581 C CD2 . LEU A 1 577 ? -9.063  -26.794 16.691 1.00 20.89 ? 577  LEU A CD2 1 
ATOM   4582 N N   . ASP A 1 578 ? -9.002  -23.516 12.334 1.00 20.17 ? 578  ASP A N   1 
ATOM   4583 C CA  . ASP A 1 578 ? -9.988  -22.840 11.489 1.00 21.27 ? 578  ASP A CA  1 
ATOM   4584 C C   . ASP A 1 578 ? -11.300 -22.727 12.275 1.00 21.26 ? 578  ASP A C   1 
ATOM   4585 O O   . ASP A 1 578 ? -11.757 -23.699 12.876 1.00 22.11 ? 578  ASP A O   1 
ATOM   4586 C CB  . ASP A 1 578 ? -10.267 -23.670 10.233 1.00 22.34 ? 578  ASP A CB  1 
ATOM   4587 C CG  . ASP A 1 578 ? -9.060  -23.780 9.284  1.00 23.79 ? 578  ASP A CG  1 
ATOM   4588 O OD1 . ASP A 1 578 ? -7.976  -23.180 9.506  1.00 24.37 ? 578  ASP A OD1 1 
ATOM   4589 O OD2 . ASP A 1 578 ? -9.209  -24.517 8.299  1.00 26.43 ? 578  ASP A OD2 1 
ATOM   4590 N N   . THR A 1 579 ? -11.903 -21.544 12.266 1.00 21.03 ? 579  THR A N   1 
ATOM   4591 C CA  . THR A 1 579 ? -13.103 -21.323 13.034 1.00 21.18 ? 579  THR A CA  1 
ATOM   4592 C C   . THR A 1 579 ? -14.324 -21.606 12.154 1.00 21.75 ? 579  THR A C   1 
ATOM   4593 O O   . THR A 1 579 ? -14.372 -21.131 11.022 1.00 21.31 ? 579  THR A O   1 
ATOM   4594 C CB  . THR A 1 579 ? -13.127 -19.907 13.665 1.00 20.98 ? 579  THR A CB  1 
ATOM   4595 O OG1 . THR A 1 579 ? -14.121 -19.844 14.683 1.00 21.76 ? 579  THR A OG1 1 
ATOM   4596 C CG2 . THR A 1 579 ? -13.380 -18.782 12.629 1.00 20.40 ? 579  THR A CG2 1 
ATOM   4597 N N   . PRO A 1 580 ? -15.281 -22.400 12.667 1.00 21.85 ? 580  PRO A N   1 
ATOM   4598 C CA  . PRO A 1 580 ? -16.572 -22.578 11.979 1.00 22.04 ? 580  PRO A CA  1 
ATOM   4599 C C   . PRO A 1 580 ? -17.322 -21.237 11.913 1.00 21.58 ? 580  PRO A C   1 
ATOM   4600 O O   . PRO A 1 580 ? -17.253 -20.449 12.863 1.00 20.85 ? 580  PRO A O   1 
ATOM   4601 C CB  . PRO A 1 580 ? -17.343 -23.537 12.896 1.00 22.06 ? 580  PRO A CB  1 
ATOM   4602 C CG  . PRO A 1 580 ? -16.362 -24.096 13.847 1.00 23.88 ? 580  PRO A CG  1 
ATOM   4603 C CD  . PRO A 1 580 ? -15.215 -23.136 13.946 1.00 21.99 ? 580  PRO A CD  1 
ATOM   4604 N N   . GLU A 1 581 ? -18.027 -20.964 10.814 1.00 20.60 ? 581  GLU A N   1 
ATOM   4605 C CA  . GLU A 1 581 ? -18.841 -19.741 10.730 1.00 20.69 ? 581  GLU A CA  1 
ATOM   4606 C C   . GLU A 1 581 ? -19.778 -19.515 11.926 1.00 19.22 ? 581  GLU A C   1 
ATOM   4607 O O   . GLU A 1 581 ? -19.954 -18.388 12.378 1.00 18.60 ? 581  GLU A O   1 
ATOM   4608 C CB  . GLU A 1 581 ? -19.659 -19.724 9.436  1.00 20.59 ? 581  GLU A CB  1 
ATOM   4609 C CG  . GLU A 1 581 ? -20.376 -18.415 9.158  1.00 23.10 ? 581  GLU A CG  1 
ATOM   4610 C CD  . GLU A 1 581 ? -21.730 -18.290 9.840  1.00 24.64 ? 581  GLU A CD  1 
ATOM   4611 O OE1 . GLU A 1 581 ? -22.287 -19.287 10.377 1.00 24.20 ? 581  GLU A OE1 1 
ATOM   4612 O OE2 . GLU A 1 581 ? -22.264 -17.167 9.812  1.00 29.27 ? 581  GLU A OE2 1 
ATOM   4613 N N   . GLU A 1 582 ? -20.439 -20.566 12.381 1.00 18.89 ? 582  GLU A N   1 
ATOM   4614 C CA  . GLU A 1 582 ? -21.453 -20.401 13.403 1.00 19.86 ? 582  GLU A CA  1 
ATOM   4615 C C   . GLU A 1 582 ? -20.798 -20.026 14.749 1.00 18.51 ? 582  GLU A C   1 
ATOM   4616 O O   . GLU A 1 582 ? -21.298 -19.166 15.486 1.00 17.75 ? 582  GLU A O   1 
ATOM   4617 C CB  . GLU A 1 582 ? -22.306 -21.661 13.543 1.00 19.40 ? 582  GLU A CB  1 
ATOM   4618 C CG  . GLU A 1 582 ? -23.420 -21.490 14.565 1.00 21.98 ? 582  GLU A CG  1 
ATOM   4619 C CD  . GLU A 1 582 ? -24.016 -22.792 15.032 1.00 25.88 ? 582  GLU A CD  1 
ATOM   4620 O OE1 . GLU A 1 582 ? -23.727 -23.867 14.433 1.00 29.89 ? 582  GLU A OE1 1 
ATOM   4621 O OE2 . GLU A 1 582 ? -24.796 -22.746 16.009 1.00 28.43 ? 582  GLU A OE2 1 
ATOM   4622 N N   . LEU A 1 583 ? -19.676 -20.674 15.040 1.00 17.36 ? 583  LEU A N   1 
ATOM   4623 C CA  . LEU A 1 583 ? -18.937 -20.407 16.266 1.00 16.97 ? 583  LEU A CA  1 
ATOM   4624 C C   . LEU A 1 583 ? -18.392 -18.971 16.217 1.00 16.95 ? 583  LEU A C   1 
ATOM   4625 O O   . LEU A 1 583 ? -18.597 -18.227 17.146 1.00 17.05 ? 583  LEU A O   1 
ATOM   4626 C CB  . LEU A 1 583 ? -17.796 -21.425 16.472 1.00 16.12 ? 583  LEU A CB  1 
ATOM   4627 C CG  . LEU A 1 583 ? -16.801 -21.045 17.589 1.00 16.79 ? 583  LEU A CG  1 
ATOM   4628 C CD1 . LEU A 1 583 ? -17.462 -21.091 18.964 1.00 16.51 ? 583  LEU A CD1 1 
ATOM   4629 C CD2 . LEU A 1 583 ? -15.588 -21.967 17.545 1.00 15.92 ? 583  LEU A CD2 1 
ATOM   4630 N N   . CYS A 1 584 ? -17.767 -18.573 15.110 1.00 18.23 ? 584  CYS A N   1 
ATOM   4631 C CA  . CYS A 1 584 ? -17.251 -17.206 14.982 1.00 17.95 ? 584  CYS A CA  1 
ATOM   4632 C C   . CYS A 1 584 ? -18.341 -16.133 15.070 1.00 17.95 ? 584  CYS A C   1 
ATOM   4633 O O   . CYS A 1 584 ? -18.139 -15.114 15.712 1.00 17.98 ? 584  CYS A O   1 
ATOM   4634 C CB  . CYS A 1 584 ? -16.417 -17.052 13.724 1.00 18.88 ? 584  CYS A CB  1 
ATOM   4635 S SG  . CYS A 1 584 ? -15.318 -15.572 13.689 1.00 20.02 ? 584  CYS A SG  1 
ATOM   4636 N N   . ARG A 1 585 ? -19.506 -16.388 14.465 1.00 16.60 ? 585  ARG A N   1 
ATOM   4637 C CA  . ARG A 1 585 ? -20.638 -15.482 14.567 1.00 16.07 ? 585  ARG A CA  1 
ATOM   4638 C C   . ARG A 1 585 ? -21.108 -15.320 16.014 1.00 15.77 ? 585  ARG A C   1 
ATOM   4639 O O   . ARG A 1 585 ? -21.269 -14.188 16.478 1.00 15.17 ? 585  ARG A O   1 
ATOM   4640 C CB  . ARG A 1 585 ? -21.798 -15.982 13.684 1.00 15.60 ? 585  ARG A CB  1 
ATOM   4641 C CG  . ARG A 1 585 ? -23.130 -15.186 13.837 1.00 16.55 ? 585  ARG A CG  1 
ATOM   4642 C CD  . ARG A 1 585 ? -24.022 -15.403 12.557 1.00 16.25 ? 585  ARG A CD  1 
ATOM   4643 N NE  . ARG A 1 585 ? -24.026 -16.780 12.076 1.00 17.66 ? 585  ARG A NE  1 
ATOM   4644 C CZ  . ARG A 1 585 ? -24.726 -17.783 12.624 1.00 19.39 ? 585  ARG A CZ  1 
ATOM   4645 N NH1 . ARG A 1 585 ? -25.489 -17.588 13.686 1.00 25.74 ? 585  ARG A NH1 1 
ATOM   4646 N NH2 . ARG A 1 585 ? -24.642 -19.002 12.134 1.00 17.50 ? 585  ARG A NH2 1 
ATOM   4647 N N   . ARG A 1 586 ? -21.311 -16.430 16.731 1.00 15.30 ? 586  ARG A N   1 
ATOM   4648 C CA  . ARG A 1 586 ? -21.688 -16.343 18.152 1.00 15.18 ? 586  ARG A CA  1 
ATOM   4649 C C   . ARG A 1 586 ? -20.581 -15.694 19.000 1.00 14.82 ? 586  ARG A C   1 
ATOM   4650 O O   . ARG A 1 586 ? -20.859 -14.967 19.960 1.00 15.39 ? 586  ARG A O   1 
ATOM   4651 C CB  . ARG A 1 586 ? -22.064 -17.713 18.746 1.00 14.35 ? 586  ARG A CB  1 
ATOM   4652 C CG  . ARG A 1 586 ? -23.288 -18.364 18.114 1.00 16.35 ? 586  ARG A CG  1 
ATOM   4653 C CD  . ARG A 1 586 ? -24.401 -17.377 18.011 1.00 15.73 ? 586  ARG A CD  1 
ATOM   4654 N NE  . ARG A 1 586 ? -25.691 -18.050 17.883 1.00 17.65 ? 586  ARG A NE  1 
ATOM   4655 C CZ  . ARG A 1 586 ? -26.864 -17.424 17.941 1.00 17.33 ? 586  ARG A CZ  1 
ATOM   4656 N NH1 . ARG A 1 586 ? -26.907 -16.121 18.088 1.00 15.14 ? 586  ARG A NH1 1 
ATOM   4657 N NH2 . ARG A 1 586 ? -28.005 -18.121 17.830 1.00 16.61 ? 586  ARG A NH2 1 
ATOM   4658 N N   . TRP A 1 587 ? -19.326 -15.976 18.664 1.00 15.04 ? 587  TRP A N   1 
ATOM   4659 C CA  . TRP A 1 587 ? -18.227 -15.456 19.464 1.00 14.71 ? 587  TRP A CA  1 
ATOM   4660 C C   . TRP A 1 587 ? -18.067 -13.950 19.220 1.00 14.71 ? 587  TRP A C   1 
ATOM   4661 O O   . TRP A 1 587 ? -17.752 -13.212 20.139 1.00 15.05 ? 587  TRP A O   1 
ATOM   4662 C CB  . TRP A 1 587 ? -16.906 -16.167 19.114 1.00 14.30 ? 587  TRP A CB  1 
ATOM   4663 C CG  . TRP A 1 587 ? -15.984 -16.294 20.271 1.00 14.71 ? 587  TRP A CG  1 
ATOM   4664 C CD1 . TRP A 1 587 ? -15.824 -15.411 21.309 1.00 14.24 ? 587  TRP A CD1 1 
ATOM   4665 C CD2 . TRP A 1 587 ? -15.066 -17.372 20.511 1.00 14.78 ? 587  TRP A CD2 1 
ATOM   4666 N NE1 . TRP A 1 587 ? -14.874 -15.877 22.192 1.00 13.36 ? 587  TRP A NE1 1 
ATOM   4667 C CE2 . TRP A 1 587 ? -14.389 -17.080 21.718 1.00 14.25 ? 587  TRP A CE2 1 
ATOM   4668 C CE3 . TRP A 1 587 ? -14.774 -18.573 19.831 1.00 14.48 ? 587  TRP A CE3 1 
ATOM   4669 C CZ2 . TRP A 1 587 ? -13.409 -17.945 22.262 1.00 13.88 ? 587  TRP A CZ2 1 
ATOM   4670 C CZ3 . TRP A 1 587 ? -13.806 -19.435 20.377 1.00 15.36 ? 587  TRP A CZ3 1 
ATOM   4671 C CH2 . TRP A 1 587 ? -13.136 -19.108 21.574 1.00 13.34 ? 587  TRP A CH2 1 
ATOM   4672 N N   . MET A 1 588 ? -18.290 -13.492 17.989 1.00 14.62 ? 588  MET A N   1 
ATOM   4673 C CA  . MET A 1 588 ? -18.277 -12.046 17.703 1.00 14.67 ? 588  MET A CA  1 
ATOM   4674 C C   . MET A 1 588 ? -19.414 -11.302 18.386 1.00 14.78 ? 588  MET A C   1 
ATOM   4675 O O   . MET A 1 588 ? -19.245 -10.179 18.823 1.00 14.29 ? 588  MET A O   1 
ATOM   4676 C CB  . MET A 1 588 ? -18.302 -11.756 16.204 1.00 15.84 ? 588  MET A CB  1 
ATOM   4677 C CG  . MET A 1 588 ? -16.967 -11.942 15.497 1.00 15.99 ? 588  MET A CG  1 
ATOM   4678 S SD  . MET A 1 588 ? -15.650 -10.800 16.021 1.00 18.24 ? 588  MET A SD  1 
ATOM   4679 C CE  . MET A 1 588 ? -16.315 -9.183  15.611 1.00 19.93 ? 588  MET A CE  1 
ATOM   4680 N N   . GLN A 1 589 ? -20.575 -11.942 18.498 1.00 13.87 ? 589  GLN A N   1 
ATOM   4681 C CA  . GLN A 1 589 ? -21.694 -11.332 19.212 1.00 14.61 ? 589  GLN A CA  1 
ATOM   4682 C C   . GLN A 1 589 ? -21.357 -11.141 20.669 1.00 14.36 ? 589  GLN A C   1 
ATOM   4683 O O   . GLN A 1 589 ? -21.562 -10.050 21.203 1.00 15.99 ? 589  GLN A O   1 
ATOM   4684 C CB  . GLN A 1 589 ? -22.941 -12.227 19.106 1.00 14.37 ? 589  GLN A CB  1 
ATOM   4685 C CG  . GLN A 1 589 ? -23.491 -12.184 17.676 1.00 17.07 ? 589  GLN A CG  1 
ATOM   4686 C CD  . GLN A 1 589 ? -24.504 -13.278 17.347 1.00 17.94 ? 589  GLN A CD  1 
ATOM   4687 O OE1 . GLN A 1 589 ? -24.752 -14.200 18.130 1.00 17.69 ? 589  GLN A OE1 1 
ATOM   4688 N NE2 . GLN A 1 589 ? -25.083 -13.172 16.164 1.00 21.19 ? 589  GLN A NE2 1 
ATOM   4689 N N   . LEU A 1 590 ? -20.821 -12.194 21.306 1.00 12.94 ? 590  LEU A N   1 
ATOM   4690 C CA  . LEU A 1 590 ? -20.438 -12.104 22.707 1.00 13.15 ? 590  LEU A CA  1 
ATOM   4691 C C   . LEU A 1 590 ? -19.219 -11.189 22.824 1.00 13.49 ? 590  LEU A C   1 
ATOM   4692 O O   . LEU A 1 590 ? -19.140 -10.390 23.761 1.00 13.10 ? 590  LEU A O   1 
ATOM   4693 C CB  . LEU A 1 590 ? -20.092 -13.478 23.286 1.00 12.95 ? 590  LEU A CB  1 
ATOM   4694 C CG  . LEU A 1 590 ? -19.431 -13.448 24.697 1.00 12.40 ? 590  LEU A CG  1 
ATOM   4695 C CD1 . LEU A 1 590 ? -20.353 -12.793 25.704 1.00 14.08 ? 590  LEU A CD1 1 
ATOM   4696 C CD2 . LEU A 1 590 ? -19.150 -14.883 25.090 1.00 17.08 ? 590  LEU A CD2 1 
ATOM   4697 N N   . GLY A 1 591 ? -18.267 -11.369 21.899 1.00 14.55 ? 591  GLY A N   1 
ATOM   4698 C CA  . GLY A 1 591 ? -16.993 -10.627 21.895 1.00 14.87 ? 591  GLY A CA  1 
ATOM   4699 C C   . GLY A 1 591 ? -17.148 -9.109  21.783 1.00 14.28 ? 591  GLY A C   1 
ATOM   4700 O O   . GLY A 1 591 ? -16.300 -8.336  22.254 1.00 13.68 ? 591  GLY A O   1 
ATOM   4701 N N   . ALA A 1 592 ? -18.222 -8.647  21.141 1.00 12.98 ? 592  ALA A N   1 
ATOM   4702 C CA  . ALA A 1 592 ? -18.570 -7.235  21.211 1.00 13.51 ? 592  ALA A CA  1 
ATOM   4703 C C   . ALA A 1 592 ? -18.728 -6.683  22.638 1.00 13.31 ? 592  ALA A C   1 
ATOM   4704 O O   . ALA A 1 592 ? -18.713 -5.450  22.847 1.00 13.89 ? 592  ALA A O   1 
ATOM   4705 C CB  . ALA A 1 592 ? -19.833 -6.926  20.355 1.00 13.24 ? 592  ALA A CB  1 
ATOM   4706 N N   . PHE A 1 593 ? -18.919 -7.571  23.608 1.00 13.00 ? 593  PHE A N   1 
ATOM   4707 C CA  . PHE A 1 593 ? -19.121 -7.156  25.012 1.00 13.79 ? 593  PHE A CA  1 
ATOM   4708 C C   . PHE A 1 593 ? -18.033 -7.597  25.970 1.00 14.08 ? 593  PHE A C   1 
ATOM   4709 O O   . PHE A 1 593 ? -18.203 -7.483  27.186 1.00 14.63 ? 593  PHE A O   1 
ATOM   4710 C CB  . PHE A 1 593 ? -20.542 -7.581  25.464 1.00 13.80 ? 593  PHE A CB  1 
ATOM   4711 C CG  . PHE A 1 593 ? -21.570 -6.982  24.569 1.00 14.86 ? 593  PHE A CG  1 
ATOM   4712 C CD1 . PHE A 1 593 ? -21.955 -5.647  24.776 1.00 14.52 ? 593  PHE A CD1 1 
ATOM   4713 C CD2 . PHE A 1 593 ? -22.004 -7.657  23.422 1.00 16.44 ? 593  PHE A CD2 1 
ATOM   4714 C CE1 . PHE A 1 593 ? -22.791 -5.003  23.898 1.00 14.24 ? 593  PHE A CE1 1 
ATOM   4715 C CE2 . PHE A 1 593 ? -22.940 -7.019  22.534 1.00 14.50 ? 593  PHE A CE2 1 
ATOM   4716 C CZ  . PHE A 1 593 ? -23.299 -5.702  22.781 1.00 13.76 ? 593  PHE A CZ  1 
ATOM   4717 N N   . TYR A 1 594 ? -16.904 -8.082  25.442 1.00 13.08 ? 594  TYR A N   1 
ATOM   4718 C CA  . TYR A 1 594 ? -15.787 -8.377  26.346 1.00 13.12 ? 594  TYR A CA  1 
ATOM   4719 C C   . TYR A 1 594 ? -15.131 -7.028  26.621 1.00 14.30 ? 594  TYR A C   1 
ATOM   4720 O O   . TYR A 1 594 ? -15.082 -6.211  25.715 1.00 15.03 ? 594  TYR A O   1 
ATOM   4721 C CB  . TYR A 1 594 ? -14.743 -9.250  25.670 1.00 13.12 ? 594  TYR A CB  1 
ATOM   4722 C CG  . TYR A 1 594 ? -15.079 -10.700 25.480 1.00 13.20 ? 594  TYR A CG  1 
ATOM   4723 C CD1 . TYR A 1 594 ? -15.612 -11.482 26.505 1.00 16.21 ? 594  TYR A CD1 1 
ATOM   4724 C CD2 . TYR A 1 594 ? -14.754 -11.310 24.278 1.00 13.98 ? 594  TYR A CD2 1 
ATOM   4725 C CE1 . TYR A 1 594 ? -15.869 -12.865 26.291 1.00 13.82 ? 594  TYR A CE1 1 
ATOM   4726 C CE2 . TYR A 1 594 ? -14.986 -12.629 24.058 1.00 13.55 ? 594  TYR A CE2 1 
ATOM   4727 C CZ  . TYR A 1 594 ? -15.533 -13.404 25.056 1.00 13.34 ? 594  TYR A CZ  1 
ATOM   4728 O OH  . TYR A 1 594 ? -15.728 -14.719 24.761 1.00 15.39 ? 594  TYR A OH  1 
ATOM   4729 N N   . PRO A 1 595 ? -14.686 -6.772  27.865 1.00 14.79 ? 595  PRO A N   1 
ATOM   4730 C CA  . PRO A 1 595 ? -14.107 -5.472  28.127 1.00 15.11 ? 595  PRO A CA  1 
ATOM   4731 C C   . PRO A 1 595 ? -12.857 -5.185  27.241 1.00 15.96 ? 595  PRO A C   1 
ATOM   4732 O O   . PRO A 1 595 ? -12.675 -4.058  26.816 1.00 17.53 ? 595  PRO A O   1 
ATOM   4733 C CB  . PRO A 1 595 ? -13.779 -5.497  29.637 1.00 15.27 ? 595  PRO A CB  1 
ATOM   4734 C CG  . PRO A 1 595 ? -14.235 -6.804  30.174 1.00 15.65 ? 595  PRO A CG  1 
ATOM   4735 C CD  . PRO A 1 595 ? -14.722 -7.667  29.040 1.00 14.52 ? 595  PRO A CD  1 
ATOM   4736 N N   . PHE A 1 596 ? -12.032 -6.196  26.973 1.00 15.79 ? 596  PHE A N   1 
ATOM   4737 C CA  . PHE A 1 596 ? -11.018 -6.154  25.883 1.00 15.44 ? 596  PHE A CA  1 
ATOM   4738 C C   . PHE A 1 596 ? -11.559 -7.019  24.739 1.00 15.72 ? 596  PHE A C   1 
ATOM   4739 O O   . PHE A 1 596 ? -11.689 -8.233  24.889 1.00 15.52 ? 596  PHE A O   1 
ATOM   4740 C CB  . PHE A 1 596 ? -9.664  -6.749  26.342 1.00 14.58 ? 596  PHE A CB  1 
ATOM   4741 C CG  . PHE A 1 596 ? -8.630  -6.857  25.229 1.00 14.50 ? 596  PHE A CG  1 
ATOM   4742 C CD1 . PHE A 1 596 ? -8.209  -5.708  24.552 1.00 17.10 ? 596  PHE A CD1 1 
ATOM   4743 C CD2 . PHE A 1 596 ? -8.058  -8.086  24.881 1.00 15.78 ? 596  PHE A CD2 1 
ATOM   4744 C CE1 . PHE A 1 596 ? -7.279  -5.782  23.539 1.00 14.03 ? 596  PHE A CE1 1 
ATOM   4745 C CE2 . PHE A 1 596 ? -7.097  -8.171  23.843 1.00 14.84 ? 596  PHE A CE2 1 
ATOM   4746 C CZ  . PHE A 1 596 ? -6.700  -7.005  23.197 1.00 13.88 ? 596  PHE A CZ  1 
ATOM   4747 N N   . SER A 1 597 ? -11.877 -6.379  23.607 1.00 15.48 ? 597  SER A N   1 
ATOM   4748 C CA  . SER A 1 597 ? -12.496 -7.010  22.436 1.00 15.35 ? 597  SER A CA  1 
ATOM   4749 C C   . SER A 1 597 ? -11.519 -7.115  21.252 1.00 15.29 ? 597  SER A C   1 
ATOM   4750 O O   . SER A 1 597 ? -11.262 -6.109  20.562 1.00 15.90 ? 597  SER A O   1 
ATOM   4751 C CB  . SER A 1 597 ? -13.723 -6.173  21.999 1.00 14.87 ? 597  SER A CB  1 
ATOM   4752 O OG  . SER A 1 597 ? -14.390 -6.807  20.926 1.00 16.33 ? 597  SER A OG  1 
ATOM   4753 N N   . ARG A 1 598 ? -10.943 -8.302  21.049 1.00 15.42 ? 598  ARG A N   1 
ATOM   4754 C CA  . ARG A 1 598 ? -9.954  -8.527  19.995 1.00 14.63 ? 598  ARG A CA  1 
ATOM   4755 C C   . ARG A 1 598 ? -10.193 -9.871  19.312 1.00 14.24 ? 598  ARG A C   1 
ATOM   4756 O O   . ARG A 1 598 ? -10.300 -10.911 19.973 1.00 14.47 ? 598  ARG A O   1 
ATOM   4757 C CB  . ARG A 1 598 ? -8.492  -8.477  20.530 1.00 15.38 ? 598  ARG A CB  1 
ATOM   4758 C CG  . ARG A 1 598 ? -7.452  -8.721  19.451 1.00 14.88 ? 598  ARG A CG  1 
ATOM   4759 C CD  . ARG A 1 598 ? -6.018  -8.573  20.004 1.00 15.33 ? 598  ARG A CD  1 
ATOM   4760 N NE  . ARG A 1 598 ? -5.628  -9.775  20.714 1.00 17.45 ? 598  ARG A NE  1 
ATOM   4761 C CZ  . ARG A 1 598 ? -4.371  -10.151 20.863 1.00 18.04 ? 598  ARG A CZ  1 
ATOM   4762 N NH1 . ARG A 1 598 ? -3.403  -9.381  20.378 1.00 17.89 ? 598  ARG A NH1 1 
ATOM   4763 N NH2 . ARG A 1 598 ? -4.098  -11.297 21.465 1.00 17.96 ? 598  ARG A NH2 1 
ATOM   4764 N N   . ASN A 1 599 ? -10.306 -9.837  17.986 1.00 14.06 ? 599  ASN A N   1 
ATOM   4765 C CA  . ASN A 1 599 ? -10.326 -11.041 17.156 1.00 15.48 ? 599  ASN A CA  1 
ATOM   4766 C C   . ASN A 1 599 ? -8.858  -11.266 16.750 1.00 15.62 ? 599  ASN A C   1 
ATOM   4767 O O   . ASN A 1 599 ? -8.247  -10.395 16.110 1.00 17.63 ? 599  ASN A O   1 
ATOM   4768 C CB  . ASN A 1 599 ? -11.220 -10.749 15.924 1.00 15.17 ? 599  ASN A CB  1 
ATOM   4769 C CG  . ASN A 1 599 ? -11.352 -11.938 14.938 1.00 17.33 ? 599  ASN A CG  1 
ATOM   4770 O OD1 . ASN A 1 599 ? -10.385 -12.646 14.634 1.00 18.51 ? 599  ASN A OD1 1 
ATOM   4771 N ND2 . ASN A 1 599 ? -12.568 -12.115 14.393 1.00 17.94 ? 599  ASN A ND2 1 
ATOM   4772 N N   . HIS A 1 600 ? -8.304  -12.413 17.133 1.00 15.97 ? 600  HIS A N   1 
ATOM   4773 C CA  . HIS A 1 600 ? -6.905  -12.777 16.849 1.00 15.94 ? 600  HIS A CA  1 
ATOM   4774 C C   . HIS A 1 600 ? -6.863  -14.251 16.411 1.00 16.71 ? 600  HIS A C   1 
ATOM   4775 O O   . HIS A 1 600 ? -7.714  -15.054 16.816 1.00 17.65 ? 600  HIS A O   1 
ATOM   4776 C CB  . HIS A 1 600 ? -6.061  -12.510 18.083 1.00 15.78 ? 600  HIS A CB  1 
ATOM   4777 C CG  . HIS A 1 600 ? -4.618  -12.896 17.946 1.00 14.22 ? 600  HIS A CG  1 
ATOM   4778 N ND1 . HIS A 1 600 ? -3.819  -12.437 16.922 1.00 15.29 ? 600  HIS A ND1 1 
ATOM   4779 C CD2 . HIS A 1 600 ? -3.818  -13.639 18.745 1.00 15.71 ? 600  HIS A CD2 1 
ATOM   4780 C CE1 . HIS A 1 600 ? -2.588  -12.902 17.078 1.00 16.87 ? 600  HIS A CE1 1 
ATOM   4781 N NE2 . HIS A 1 600 ? -2.559  -13.634 18.178 1.00 16.55 ? 600  HIS A NE2 1 
ATOM   4782 N N   . ASN A 1 601 ? -5.893  -14.628 15.577 1.00 16.20 ? 601  ASN A N   1 
ATOM   4783 C CA  . ASN A 1 601 ? -5.940  -15.945 14.946 1.00 16.43 ? 601  ASN A CA  1 
ATOM   4784 C C   . ASN A 1 601 ? -4.508  -16.434 14.864 1.00 16.15 ? 601  ASN A C   1 
ATOM   4785 O O   . ASN A 1 601 ? -3.596  -15.617 14.706 1.00 16.80 ? 601  ASN A O   1 
ATOM   4786 C CB  . ASN A 1 601 ? -6.510  -15.771 13.543 1.00 14.60 ? 601  ASN A CB  1 
ATOM   4787 C CG  . ASN A 1 601 ? -6.816  -17.085 12.817 1.00 15.81 ? 601  ASN A CG  1 
ATOM   4788 O OD1 . ASN A 1 601 ? -6.887  -18.163 13.395 1.00 16.88 ? 601  ASN A OD1 1 
ATOM   4789 N ND2 . ASN A 1 601 ? -6.997  -16.976 11.512 1.00 19.09 ? 601  ASN A ND2 1 
ATOM   4790 N N   . GLY A 1 602 ? -4.309  -17.741 14.999 1.00 16.86 ? 602  GLY A N   1 
ATOM   4791 C CA  . GLY A 1 602 ? -2.960  -18.324 14.916 1.00 16.13 ? 602  GLY A CA  1 
ATOM   4792 C C   . GLY A 1 602 ? -2.434  -18.445 13.498 1.00 17.78 ? 602  GLY A C   1 
ATOM   4793 O O   . GLY A 1 602 ? -3.097  -18.084 12.536 1.00 17.50 ? 602  GLY A O   1 
ATOM   4794 N N   . GLN A 1 603 ? -1.213  -18.952 13.381 1.00 18.82 ? 603  GLN A N   1 
ATOM   4795 C CA  . GLN A 1 603 ? -0.498  -19.024 12.122 1.00 21.67 ? 603  GLN A CA  1 
ATOM   4796 C C   . GLN A 1 603 ? -1.105  -20.094 11.241 1.00 22.23 ? 603  GLN A C   1 
ATOM   4797 O O   . GLN A 1 603 ? -1.361  -21.203 11.707 1.00 22.71 ? 603  GLN A O   1 
ATOM   4798 C CB  . GLN A 1 603 ? 0.961   -19.384 12.425 1.00 21.54 ? 603  GLN A CB  1 
ATOM   4799 C CG  . GLN A 1 603 ? 1.902   -19.368 11.232 1.00 25.18 ? 603  GLN A CG  1 
ATOM   4800 C CD  . GLN A 1 603 ? 3.321   -19.818 11.623 1.00 25.75 ? 603  GLN A CD  1 
ATOM   4801 O OE1 . GLN A 1 603 ? 3.509   -20.697 12.474 1.00 32.53 ? 603  GLN A OE1 1 
ATOM   4802 N NE2 . GLN A 1 603 ? 4.317   -19.224 10.988 1.00 33.12 ? 603  GLN A NE2 1 
ATOM   4803 N N   . GLY A 1 604 ? -1.358  -19.740 9.979  1.00 22.39 ? 604  GLY A N   1 
ATOM   4804 C CA  . GLY A 1 604 ? -1.711  -20.724 8.964  1.00 23.11 ? 604  GLY A CA  1 
ATOM   4805 C C   . GLY A 1 604 ? -3.186  -21.005 8.838  1.00 22.67 ? 604  GLY A C   1 
ATOM   4806 O O   . GLY A 1 604 ? -3.622  -21.493 7.795  1.00 22.77 ? 604  GLY A O   1 
ATOM   4807 N N   . TYR A 1 605 ? -3.977  -20.679 9.862  1.00 21.72 ? 605  TYR A N   1 
ATOM   4808 C CA  . TYR A 1 605 ? -5.417  -20.967 9.815  1.00 21.63 ? 605  TYR A CA  1 
ATOM   4809 C C   . TYR A 1 605 ? -6.173  -20.031 8.858  1.00 22.04 ? 605  TYR A C   1 
ATOM   4810 O O   . TYR A 1 605 ? -5.713  -18.945 8.551  1.00 22.85 ? 605  TYR A O   1 
ATOM   4811 C CB  . TYR A 1 605 ? -6.056  -20.974 11.236 1.00 22.14 ? 605  TYR A CB  1 
ATOM   4812 C CG  . TYR A 1 605 ? -5.238  -21.803 12.181 1.00 21.35 ? 605  TYR A CG  1 
ATOM   4813 C CD1 . TYR A 1 605 ? -5.156  -23.192 12.022 1.00 22.80 ? 605  TYR A CD1 1 
ATOM   4814 C CD2 . TYR A 1 605 ? -4.497  -21.205 13.195 1.00 21.91 ? 605  TYR A CD2 1 
ATOM   4815 C CE1 . TYR A 1 605 ? -4.344  -23.960 12.864 1.00 25.29 ? 605  TYR A CE1 1 
ATOM   4816 C CE2 . TYR A 1 605 ? -3.692  -21.945 14.025 1.00 22.97 ? 605  TYR A CE2 1 
ATOM   4817 C CZ  . TYR A 1 605 ? -3.618  -23.316 13.862 1.00 23.50 ? 605  TYR A CZ  1 
ATOM   4818 O OH  . TYR A 1 605 ? -2.829  -24.031 14.721 1.00 24.96 ? 605  TYR A OH  1 
ATOM   4819 N N   . LYS A 1 606 ? -7.315  -20.509 8.377  1.00 22.24 ? 606  LYS A N   1 
ATOM   4820 C CA  . LYS A 1 606 ? -8.274  -19.752 7.562  1.00 24.33 ? 606  LYS A CA  1 
ATOM   4821 C C   . LYS A 1 606 ? -8.521  -18.388 8.216  1.00 23.57 ? 606  LYS A C   1 
ATOM   4822 O O   . LYS A 1 606 ? -8.503  -18.287 9.442  1.00 23.70 ? 606  LYS A O   1 
ATOM   4823 C CB  . LYS A 1 606 ? -9.561  -20.596 7.459  1.00 23.50 ? 606  LYS A CB  1 
ATOM   4824 C CG  . LYS A 1 606 ? -10.832 -19.870 7.130  1.00 27.61 ? 606  LYS A CG  1 
ATOM   4825 C CD  . LYS A 1 606 ? -12.035 -20.855 7.154  1.00 27.89 ? 606  LYS A CD  1 
ATOM   4826 C CE  . LYS A 1 606 ? -13.374 -20.089 7.261  1.00 35.12 ? 606  LYS A CE  1 
ATOM   4827 N NZ  . LYS A 1 606 ? -14.495 -20.948 7.812  1.00 36.52 ? 606  LYS A NZ  1 
ATOM   4828 N N   . ASP A 1 607 ? -8.677  -17.346 7.398  1.00 23.15 ? 607  ASP A N   1 
ATOM   4829 C CA  . ASP A 1 607 ? -8.936  -15.987 7.878  1.00 22.08 ? 607  ASP A CA  1 
ATOM   4830 C C   . ASP A 1 607 ? -10.203 -16.002 8.724  1.00 21.32 ? 607  ASP A C   1 
ATOM   4831 O O   . ASP A 1 607 ? -11.193 -16.679 8.400  1.00 20.78 ? 607  ASP A O   1 
ATOM   4832 C CB  . ASP A 1 607 ? -9.134  -15.036 6.690  1.00 22.44 ? 607  ASP A CB  1 
ATOM   4833 C CG  . ASP A 1 607 ? -7.867  -14.782 5.916  1.00 25.34 ? 607  ASP A CG  1 
ATOM   4834 O OD1 . ASP A 1 607 ? -6.770  -15.141 6.402  1.00 28.82 ? 607  ASP A OD1 1 
ATOM   4835 O OD2 . ASP A 1 607 ? -7.955  -14.206 4.810  1.00 26.90 ? 607  ASP A OD2 1 
ATOM   4836 N N   . GLN A 1 608 ? -10.197 -15.227 9.796  1.00 19.78 ? 608  GLN A N   1 
ATOM   4837 C CA  . GLN A 1 608 ? -11.409 -15.132 10.596 1.00 18.53 ? 608  GLN A CA  1 
ATOM   4838 C C   . GLN A 1 608 ? -11.766 -13.698 10.982 1.00 17.70 ? 608  GLN A C   1 
ATOM   4839 O O   . GLN A 1 608 ? -12.567 -13.491 11.882 1.00 17.60 ? 608  GLN A O   1 
ATOM   4840 C CB  . GLN A 1 608 ? -11.288 -16.046 11.825 1.00 17.99 ? 608  GLN A CB  1 
ATOM   4841 C CG  . GLN A 1 608 ? -10.234 -15.639 12.794 1.00 18.64 ? 608  GLN A CG  1 
ATOM   4842 C CD  . GLN A 1 608 ? -9.988  -16.678 13.876 1.00 18.83 ? 608  GLN A CD  1 
ATOM   4843 O OE1 . GLN A 1 608 ? -9.958  -17.884 13.619 1.00 20.16 ? 608  GLN A OE1 1 
ATOM   4844 N NE2 . GLN A 1 608 ? -9.804  -16.204 15.106 1.00 17.92 ? 608  GLN A NE2 1 
ATOM   4845 N N   . ASP A 1 609 ? -11.163 -12.711 10.305 1.00 17.29 ? 609  ASP A N   1 
ATOM   4846 C CA  . ASP A 1 609 ? -11.537 -11.334 10.477 1.00 16.81 ? 609  ASP A CA  1 
ATOM   4847 C C   . ASP A 1 609 ? -12.980 -11.239 9.980  1.00 18.04 ? 609  ASP A C   1 
ATOM   4848 O O   . ASP A 1 609 ? -13.382 -12.006 9.091  1.00 18.35 ? 609  ASP A O   1 
ATOM   4849 C CB  . ASP A 1 609 ? -10.616 -10.388 9.690  1.00 17.87 ? 609  ASP A CB  1 
ATOM   4850 C CG  . ASP A 1 609 ? -10.557 -10.725 8.238  1.00 17.25 ? 609  ASP A CG  1 
ATOM   4851 O OD1 . ASP A 1 609 ? -9.822  -11.659 7.869  1.00 18.74 ? 609  ASP A OD1 1 
ATOM   4852 O OD2 . ASP A 1 609 ? -11.236 -10.049 7.456  1.00 18.49 ? 609  ASP A OD2 1 
ATOM   4853 N N   . PRO A 1 610 ? -13.781 -10.365 10.596 1.00 17.88 ? 610  PRO A N   1 
ATOM   4854 C CA  . PRO A 1 610 ? -15.215 -10.308 10.262 1.00 18.67 ? 610  PRO A CA  1 
ATOM   4855 C C   . PRO A 1 610 ? -15.550 -10.193 8.759  1.00 18.98 ? 610  PRO A C   1 
ATOM   4856 O O   . PRO A 1 610 ? -16.392 -10.937 8.276  1.00 19.31 ? 610  PRO A O   1 
ATOM   4857 C CB  . PRO A 1 610 ? -15.695 -9.093  11.059 1.00 17.30 ? 610  PRO A CB  1 
ATOM   4858 C CG  . PRO A 1 610 ? -14.782 -9.092  12.280 1.00 18.14 ? 610  PRO A CG  1 
ATOM   4859 C CD  . PRO A 1 610 ? -13.436 -9.408  11.667 1.00 19.26 ? 610  PRO A CD  1 
ATOM   4860 N N   . ALA A 1 611 ? -14.877 -9.305  8.021  1.00 19.47 ? 611  ALA A N   1 
ATOM   4861 C CA  . ALA A 1 611 ? -15.199 -9.106  6.599  1.00 19.89 ? 611  ALA A CA  1 
ATOM   4862 C C   . ALA A 1 611 ? -14.773 -10.271 5.701  1.00 20.57 ? 611  ALA A C   1 
ATOM   4863 O O   . ALA A 1 611 ? -15.233 -10.380 4.563  1.00 20.04 ? 611  ALA A O   1 
ATOM   4864 C CB  . ALA A 1 611 ? -14.631 -7.796  6.084  1.00 18.85 ? 611  ALA A CB  1 
ATOM   4865 N N   . SER A 1 612 ? -13.934 -11.171 6.222  1.00 21.31 ? 612  SER A N   1 
ATOM   4866 C CA  . SER A 1 612 ? -13.486 -12.334 5.443  1.00 22.45 ? 612  SER A CA  1 
ATOM   4867 C C   . SER A 1 612 ? -14.607 -13.350 5.231  1.00 23.11 ? 612  SER A C   1 
ATOM   4868 O O   . SER A 1 612 ? -14.517 -14.207 4.343  1.00 23.49 ? 612  SER A O   1 
ATOM   4869 C CB  . SER A 1 612 ? -12.263 -13.017 6.079  1.00 21.91 ? 612  SER A CB  1 
ATOM   4870 O OG  . SER A 1 612 ? -12.668 -13.851 7.153  1.00 22.79 ? 612  SER A OG  1 
ATOM   4871 N N   . PHE A 1 613 ? -15.691 -13.210 5.993  1.00 23.36 ? 613  PHE A N   1 
ATOM   4872 C CA  . PHE A 1 613 ? -16.832 -14.112 5.859  1.00 23.67 ? 613  PHE A CA  1 
ATOM   4873 C C   . PHE A 1 613 ? -17.806 -13.709 4.748  1.00 24.47 ? 613  PHE A C   1 
ATOM   4874 O O   . PHE A 1 613 ? -18.726 -14.460 4.431  1.00 24.11 ? 613  PHE A O   1 
ATOM   4875 C CB  . PHE A 1 613 ? -17.554 -14.263 7.205  1.00 23.41 ? 613  PHE A CB  1 
ATOM   4876 C CG  . PHE A 1 613 ? -16.751 -15.010 8.212  1.00 23.48 ? 613  PHE A CG  1 
ATOM   4877 C CD1 . PHE A 1 613 ? -16.942 -16.371 8.387  1.00 22.98 ? 613  PHE A CD1 1 
ATOM   4878 C CD2 . PHE A 1 613 ? -15.787 -14.352 8.981  1.00 20.37 ? 613  PHE A CD2 1 
ATOM   4879 C CE1 . PHE A 1 613 ? -16.173 -17.074 9.319  1.00 22.86 ? 613  PHE A CE1 1 
ATOM   4880 C CE2 . PHE A 1 613 ? -15.032 -15.053 9.915  1.00 19.62 ? 613  PHE A CE2 1 
ATOM   4881 C CZ  . PHE A 1 613 ? -15.227 -16.415 10.067 1.00 22.33 ? 613  PHE A CZ  1 
ATOM   4882 N N   . GLY A 1 614 ? -17.577 -12.539 4.156  1.00 25.88 ? 614  GLY A N   1 
ATOM   4883 C CA  . GLY A 1 614 ? -18.404 -12.035 3.064  1.00 26.23 ? 614  GLY A CA  1 
ATOM   4884 C C   . GLY A 1 614 ? -18.985 -10.676 3.340  1.00 27.44 ? 614  GLY A C   1 
ATOM   4885 O O   . GLY A 1 614 ? -19.523 -10.427 4.437  1.00 26.97 ? 614  GLY A O   1 
ATOM   4886 N N   . ALA A 1 615 ? -18.916 -9.804  2.332  1.00 27.76 ? 615  ALA A N   1 
ATOM   4887 C CA  . ALA A 1 615 ? -19.328 -8.413  2.490  1.00 29.15 ? 615  ALA A CA  1 
ATOM   4888 C C   . ALA A 1 615 ? -20.786 -8.321  2.841  1.00 29.21 ? 615  ALA A C   1 
ATOM   4889 O O   . ALA A 1 615 ? -21.219 -7.314  3.395  1.00 31.00 ? 615  ALA A O   1 
ATOM   4890 C CB  . ALA A 1 615 ? -19.018 -7.584  1.220  1.00 29.83 ? 615  ALA A CB  1 
ATOM   4891 N N   . ASP A 1 616 ? -21.544 -9.373  2.548  1.00 29.88 ? 616  ASP A N   1 
ATOM   4892 C CA  . ASP A 1 616 ? -22.974 -9.388  2.836  1.00 29.93 ? 616  ASP A CA  1 
ATOM   4893 C C   . ASP A 1 616 ? -23.403 -10.572 3.724  1.00 27.85 ? 616  ASP A C   1 
ATOM   4894 O O   . ASP A 1 616 ? -24.577 -10.953 3.762  1.00 27.07 ? 616  ASP A O   1 
ATOM   4895 C CB  . ASP A 1 616 ? -23.796 -9.300  1.521  1.00 31.83 ? 616  ASP A CB  1 
ATOM   4896 C CG  . ASP A 1 616 ? -23.691 -7.914  0.842  1.00 36.65 ? 616  ASP A CG  1 
ATOM   4897 O OD1 . ASP A 1 616 ? -23.511 -7.851  -0.403 1.00 42.66 ? 616  ASP A OD1 1 
ATOM   4898 O OD2 . ASP A 1 616 ? -23.779 -6.870  1.542  1.00 40.76 ? 616  ASP A OD2 1 
ATOM   4899 N N   . SER A 1 617 ? -22.448 -11.131 4.473  1.00 25.15 ? 617  SER A N   1 
ATOM   4900 C CA  . SER A 1 617 ? -22.671 -12.345 5.262  1.00 23.12 ? 617  SER A CA  1 
ATOM   4901 C C   . SER A 1 617 ? -23.418 -12.029 6.552  1.00 22.50 ? 617  SER A C   1 
ATOM   4902 O O   . SER A 1 617 ? -23.338 -10.909 7.041  1.00 21.97 ? 617  SER A O   1 
ATOM   4903 C CB  . SER A 1 617 ? -21.342 -13.006 5.616  1.00 23.64 ? 617  SER A CB  1 
ATOM   4904 O OG  . SER A 1 617 ? -20.554 -12.150 6.433  1.00 22.09 ? 617  SER A OG  1 
ATOM   4905 N N   . LEU A 1 618 ? -24.129 -13.015 7.100  1.00 22.23 ? 618  LEU A N   1 
ATOM   4906 C CA  . LEU A 1 618 ? -24.772 -12.867 8.414  1.00 21.86 ? 618  LEU A CA  1 
ATOM   4907 C C   . LEU A 1 618 ? -23.740 -12.506 9.492  1.00 21.08 ? 618  LEU A C   1 
ATOM   4908 O O   . LEU A 1 618 ? -23.985 -11.657 10.350 1.00 20.00 ? 618  LEU A O   1 
ATOM   4909 C CB  . LEU A 1 618 ? -25.523 -14.134 8.809  1.00 22.35 ? 618  LEU A CB  1 
ATOM   4910 C CG  . LEU A 1 618 ? -26.293 -14.093 10.142 1.00 21.96 ? 618  LEU A CG  1 
ATOM   4911 C CD1 . LEU A 1 618 ? -27.318 -12.981 10.159 1.00 25.97 ? 618  LEU A CD1 1 
ATOM   4912 C CD2 . LEU A 1 618 ? -26.925 -15.461 10.396 1.00 23.00 ? 618  LEU A CD2 1 
ATOM   4913 N N   . LEU A 1 619 ? -22.568 -13.132 9.438  1.00 19.38 ? 619  LEU A N   1 
ATOM   4914 C CA  . LEU A 1 619 ? -21.570 -12.878 10.471 1.00 18.46 ? 619  LEU A CA  1 
ATOM   4915 C C   . LEU A 1 619 ? -21.127 -11.415 10.419 1.00 18.45 ? 619  LEU A C   1 
ATOM   4916 O O   . LEU A 1 619 ? -21.028 -10.766 11.458 1.00 18.19 ? 619  LEU A O   1 
ATOM   4917 C CB  . LEU A 1 619 ? -20.358 -13.821 10.305 1.00 18.49 ? 619  LEU A CB  1 
ATOM   4918 C CG  . LEU A 1 619 ? -19.262 -13.709 11.368 1.00 17.57 ? 619  LEU A CG  1 
ATOM   4919 C CD1 . LEU A 1 619 ? -18.585 -15.046 11.530 1.00 17.42 ? 619  LEU A CD1 1 
ATOM   4920 C CD2 . LEU A 1 619 ? -18.188 -12.609 11.055 1.00 16.81 ? 619  LEU A CD2 1 
ATOM   4921 N N   . LEU A 1 620 ? -20.843 -10.879 9.221  1.00 18.97 ? 620  LEU A N   1 
ATOM   4922 C CA  . LEU A 1 620 ? -20.307 -9.513  9.150  1.00 18.83 ? 620  LEU A CA  1 
ATOM   4923 C C   . LEU A 1 620 ? -21.380 -8.531  9.592  1.00 19.04 ? 620  LEU A C   1 
ATOM   4924 O O   . LEU A 1 620 ? -21.120 -7.616  10.377 1.00 17.88 ? 620  LEU A O   1 
ATOM   4925 C CB  . LEU A 1 620 ? -19.806 -9.159  7.741  1.00 19.94 ? 620  LEU A CB  1 
ATOM   4926 C CG  . LEU A 1 620 ? -19.384 -7.690  7.617  1.00 20.34 ? 620  LEU A CG  1 
ATOM   4927 C CD1 . LEU A 1 620 ? -18.100 -7.466  8.448  1.00 19.26 ? 620  LEU A CD1 1 
ATOM   4928 C CD2 . LEU A 1 620 ? -19.141 -7.324  6.152  1.00 24.51 ? 620  LEU A CD2 1 
ATOM   4929 N N   . ASN A 1 621 ? -22.587 -8.727  9.077  1.00 19.47 ? 621  ASN A N   1 
ATOM   4930 C CA  . ASN A 1 621 ? -23.737 -7.894  9.456  1.00 20.24 ? 621  ASN A CA  1 
ATOM   4931 C C   . ASN A 1 621 ? -23.971 -7.885  10.948 1.00 19.49 ? 621  ASN A C   1 
ATOM   4932 O O   . ASN A 1 621 ? -24.113 -6.817  11.550 1.00 18.67 ? 621  ASN A O   1 
ATOM   4933 C CB  . ASN A 1 621 ? -25.012 -8.354  8.744  1.00 21.77 ? 621  ASN A CB  1 
ATOM   4934 C CG  . ASN A 1 621 ? -24.986 -8.008  7.268  1.00 26.07 ? 621  ASN A CG  1 
ATOM   4935 O OD1 . ASN A 1 621 ? -24.245 -7.112  6.840  1.00 29.73 ? 621  ASN A OD1 1 
ATOM   4936 N ND2 . ASN A 1 621 ? -25.809 -8.694  6.482  1.00 32.36 ? 621  ASN A ND2 1 
ATOM   4937 N N   . SER A 1 622 ? -23.997 -9.066  11.546 1.00 19.73 ? 622  SER A N   1 
ATOM   4938 C CA  . SER A 1 622 ? -24.223 -9.135  12.988 1.00 19.73 ? 622  SER A CA  1 
ATOM   4939 C C   . SER A 1 622 ? -23.045 -8.558  13.804 1.00 18.24 ? 622  SER A C   1 
ATOM   4940 O O   . SER A 1 622 ? -23.240 -7.827  14.807 1.00 16.96 ? 622  SER A O   1 
ATOM   4941 C CB  . SER A 1 622 ? -24.529 -10.555 13.417 1.00 20.13 ? 622  SER A CB  1 
ATOM   4942 O OG  . SER A 1 622 ? -24.834 -10.503 14.781 1.00 24.96 ? 622  SER A OG  1 
ATOM   4943 N N   . SER A 1 623 ? -21.822 -8.892  13.393 1.00 17.38 ? 623  SER A N   1 
ATOM   4944 C CA  . SER A 1 623 ? -20.668 -8.291  14.015 1.00 17.70 ? 623  SER A CA  1 
ATOM   4945 C C   . SER A 1 623 ? -20.753 -6.788  14.011 1.00 17.59 ? 623  SER A C   1 
ATOM   4946 O O   . SER A 1 623 ? -20.557 -6.165  15.047 1.00 19.16 ? 623  SER A O   1 
ATOM   4947 C CB  . SER A 1 623 ? -19.367 -8.761  13.345 1.00 17.75 ? 623  SER A CB  1 
ATOM   4948 O OG  . SER A 1 623 ? -19.277 -10.152 13.462 1.00 17.59 ? 623  SER A OG  1 
ATOM   4949 N N   . ARG A 1 624 ? -21.035 -6.197  12.849 1.00 17.71 ? 624  ARG A N   1 
ATOM   4950 C CA  . ARG A 1 624 ? -21.109 -4.740  12.731 1.00 17.90 ? 624  ARG A CA  1 
ATOM   4951 C C   . ARG A 1 624 ? -22.216 -4.226  13.642 1.00 16.65 ? 624  ARG A C   1 
ATOM   4952 O O   . ARG A 1 624 ? -22.044 -3.234  14.313 1.00 15.11 ? 624  ARG A O   1 
ATOM   4953 C CB  . ARG A 1 624 ? -21.350 -4.303  11.253 1.00 17.98 ? 624  ARG A CB  1 
ATOM   4954 C CG  . ARG A 1 624 ? -21.434 -2.791  11.001 1.00 18.05 ? 624  ARG A CG  1 
ATOM   4955 C CD  . ARG A 1 624 ? -21.523 -2.527  9.456  1.00 20.30 ? 624  ARG A CD  1 
ATOM   4956 N NE  . ARG A 1 624 ? -22.518 -3.424  8.864  1.00 27.47 ? 624  ARG A NE  1 
ATOM   4957 C CZ  . ARG A 1 624 ? -22.372 -4.104  7.738  1.00 27.13 ? 624  ARG A CZ  1 
ATOM   4958 N NH1 . ARG A 1 624 ? -21.253 -4.018  6.992  1.00 23.93 ? 624  ARG A NH1 1 
ATOM   4959 N NH2 . ARG A 1 624 ? -23.366 -4.903  7.365  1.00 29.18 ? 624  ARG A NH2 1 
ATOM   4960 N N   . HIS A 1 625 ? -23.352 -4.926  13.653 1.00 16.57 ? 625  HIS A N   1 
ATOM   4961 C CA  . HIS A 1 625 ? -24.500 -4.496  14.431 1.00 16.42 ? 625  HIS A CA  1 
ATOM   4962 C C   . HIS A 1 625 ? -24.150 -4.386  15.923 1.00 15.62 ? 625  HIS A C   1 
ATOM   4963 O O   . HIS A 1 625 ? -24.391 -3.344  16.568 1.00 15.04 ? 625  HIS A O   1 
ATOM   4964 C CB  . HIS A 1 625 ? -25.671 -5.470  14.219 1.00 17.41 ? 625  HIS A CB  1 
ATOM   4965 C CG  . HIS A 1 625 ? -26.920 -5.052  14.924 1.00 19.40 ? 625  HIS A CG  1 
ATOM   4966 N ND1 . HIS A 1 625 ? -27.401 -5.710  16.035 1.00 22.16 ? 625  HIS A ND1 1 
ATOM   4967 C CD2 . HIS A 1 625 ? -27.764 -4.017  14.702 1.00 22.64 ? 625  HIS A CD2 1 
ATOM   4968 C CE1 . HIS A 1 625 ? -28.503 -5.115  16.455 1.00 22.37 ? 625  HIS A CE1 1 
ATOM   4969 N NE2 . HIS A 1 625 ? -28.741 -4.081  15.670 1.00 26.51 ? 625  HIS A NE2 1 
ATOM   4970 N N   . TYR A 1 626 ? -23.577 -5.450  16.469 1.00 14.54 ? 626  TYR A N   1 
ATOM   4971 C CA  . TYR A 1 626 ? -23.289 -5.482  17.903 1.00 15.17 ? 626  TYR A CA  1 
ATOM   4972 C C   . TYR A 1 626 ? -22.067 -4.688  18.292 1.00 14.28 ? 626  TYR A C   1 
ATOM   4973 O O   . TYR A 1 626 ? -22.011 -4.144  19.397 1.00 14.54 ? 626  TYR A O   1 
ATOM   4974 C CB  . TYR A 1 626 ? -23.233 -6.931  18.430 1.00 14.79 ? 626  TYR A CB  1 
ATOM   4975 C CG  . TYR A 1 626 ? -24.634 -7.474  18.540 1.00 17.88 ? 626  TYR A CG  1 
ATOM   4976 C CD1 . TYR A 1 626 ? -25.090 -8.489  17.693 1.00 16.82 ? 626  TYR A CD1 1 
ATOM   4977 C CD2 . TYR A 1 626 ? -25.514 -6.941  19.484 1.00 13.25 ? 626  TYR A CD2 1 
ATOM   4978 C CE1 . TYR A 1 626 ? -26.408 -8.958  17.793 1.00 16.48 ? 626  TYR A CE1 1 
ATOM   4979 C CE2 . TYR A 1 626 ? -26.832 -7.386  19.575 1.00 18.23 ? 626  TYR A CE2 1 
ATOM   4980 C CZ  . TYR A 1 626 ? -27.251 -8.405  18.732 1.00 17.25 ? 626  TYR A CZ  1 
ATOM   4981 O OH  . TYR A 1 626 ? -28.532 -8.869  18.848 1.00 17.39 ? 626  TYR A OH  1 
ATOM   4982 N N   . LEU A 1 627 ? -21.086 -4.608  17.411 1.00 13.91 ? 627  LEU A N   1 
ATOM   4983 C CA  . LEU A 1 627 ? -19.997 -3.647  17.665 1.00 13.36 ? 627  LEU A CA  1 
ATOM   4984 C C   . LEU A 1 627 ? -20.534 -2.218  17.639 1.00 13.95 ? 627  LEU A C   1 
ATOM   4985 O O   . LEU A 1 627 ? -20.028 -1.351  18.321 1.00 14.05 ? 627  LEU A O   1 
ATOM   4986 C CB  . LEU A 1 627 ? -18.859 -3.810  16.666 1.00 11.78 ? 627  LEU A CB  1 
ATOM   4987 C CG  . LEU A 1 627 ? -17.959 -5.020  16.975 1.00 13.37 ? 627  LEU A CG  1 
ATOM   4988 C CD1 . LEU A 1 627 ? -17.051 -5.165  15.781 1.00 13.76 ? 627  LEU A CD1 1 
ATOM   4989 C CD2 . LEU A 1 627 ? -17.209 -4.805  18.291 1.00 14.31 ? 627  LEU A CD2 1 
ATOM   4990 N N   . ASN A 1 628 ? -21.575 -1.952  16.847 1.00 14.56 ? 628  ASN A N   1 
ATOM   4991 C CA  . ASN A 1 628 ? -22.089 -0.602  16.845 1.00 14.84 ? 628  ASN A CA  1 
ATOM   4992 C C   . ASN A 1 628 ? -22.792 -0.301  18.164 1.00 14.23 ? 628  ASN A C   1 
ATOM   4993 O O   . ASN A 1 628 ? -22.741 0.821   18.664 1.00 14.98 ? 628  ASN A O   1 
ATOM   4994 C CB  . ASN A 1 628 ? -23.000 -0.345  15.641 1.00 15.68 ? 628  ASN A CB  1 
ATOM   4995 C CG  . ASN A 1 628 ? -22.235 0.194   14.441 1.00 19.10 ? 628  ASN A CG  1 
ATOM   4996 O OD1 . ASN A 1 628 ? -22.558 -0.112  13.277 1.00 24.38 ? 628  ASN A OD1 1 
ATOM   4997 N ND2 . ASN A 1 628 ? -21.258 1.013   14.709 1.00 16.32 ? 628  ASN A ND2 1 
ATOM   4998 N N   . ILE A 1 629 ? -23.440 -1.319  18.726 1.00 14.19 ? 629  ILE A N   1 
ATOM   4999 C CA  . ILE A 1 629 ? -24.023 -1.223  20.072 1.00 12.73 ? 629  ILE A CA  1 
ATOM   5000 C C   . ILE A 1 629 ? -22.933 -1.036  21.105 1.00 12.40 ? 629  ILE A C   1 
ATOM   5001 O O   . ILE A 1 629 ? -23.035 -0.191  21.968 1.00 12.70 ? 629  ILE A O   1 
ATOM   5002 C CB  . ILE A 1 629 ? -24.912 -2.460  20.402 1.00 12.51 ? 629  ILE A CB  1 
ATOM   5003 C CG1 . ILE A 1 629 ? -26.206 -2.348  19.554 1.00 12.32 ? 629  ILE A CG1 1 
ATOM   5004 C CG2 . ILE A 1 629 ? -25.243 -2.455  21.942 1.00 12.14 ? 629  ILE A CG2 1 
ATOM   5005 C CD1 . ILE A 1 629 ? -27.066 -3.627  19.536 1.00 13.20 ? 629  ILE A CD1 1 
ATOM   5006 N N   . ARG A 1 630 ? -21.874 -1.834  21.046 1.00 12.15 ? 630  ARG A N   1 
ATOM   5007 C CA  . ARG A 1 630 ? -20.743 -1.571  21.969 1.00 12.26 ? 630  ARG A CA  1 
ATOM   5008 C C   . ARG A 1 630 ? -20.279 -0.118  21.935 1.00 11.88 ? 630  ARG A C   1 
ATOM   5009 O O   . ARG A 1 630 ? -20.108 0.516   23.005 1.00 11.86 ? 630  ARG A O   1 
ATOM   5010 C CB  . ARG A 1 630 ? -19.544 -2.478  21.644 1.00 11.05 ? 630  ARG A CB  1 
ATOM   5011 C CG  . ARG A 1 630 ? -18.311 -2.161  22.523 1.00 11.28 ? 630  ARG A CG  1 
ATOM   5012 C CD  . ARG A 1 630 ? -17.021 -2.747  21.865 1.00 11.63 ? 630  ARG A CD  1 
ATOM   5013 N NE  . ARG A 1 630 ? -15.877 -2.626  22.782 1.00 12.63 ? 630  ARG A NE  1 
ATOM   5014 C CZ  . ARG A 1 630 ? -15.593 -3.464  23.787 1.00 14.52 ? 630  ARG A CZ  1 
ATOM   5015 N NH1 . ARG A 1 630 ? -16.370 -4.513  24.037 1.00 16.24 ? 630  ARG A NH1 1 
ATOM   5016 N NH2 . ARG A 1 630 ? -14.495 -3.270  24.536 1.00 16.38 ? 630  ARG A NH2 1 
ATOM   5017 N N   . TYR A 1 631 ? -20.033 0.397   20.725 1.00 12.15 ? 631  TYR A N   1 
ATOM   5018 C CA  . TYR A 1 631 ? -19.501 1.759   20.558 1.00 13.47 ? 631  TYR A CA  1 
ATOM   5019 C C   . TYR A 1 631 ? -20.522 2.784   21.075 1.00 12.80 ? 631  TYR A C   1 
ATOM   5020 O O   . TYR A 1 631 ? -20.171 3.728   21.771 1.00 14.07 ? 631  TYR A O   1 
ATOM   5021 C CB  . TYR A 1 631 ? -19.136 2.027   19.085 1.00 13.71 ? 631  TYR A CB  1 
ATOM   5022 C CG  . TYR A 1 631 ? -17.721 1.556   18.719 1.00 14.62 ? 631  TYR A CG  1 
ATOM   5023 C CD1 . TYR A 1 631 ? -17.319 0.230   18.933 1.00 15.81 ? 631  TYR A CD1 1 
ATOM   5024 C CD2 . TYR A 1 631 ? -16.795 2.443   18.181 1.00 15.80 ? 631  TYR A CD2 1 
ATOM   5025 C CE1 . TYR A 1 631 ? -16.032 -0.211  18.598 1.00 14.56 ? 631  TYR A CE1 1 
ATOM   5026 C CE2 . TYR A 1 631 ? -15.475 2.004   17.841 1.00 16.97 ? 631  TYR A CE2 1 
ATOM   5027 C CZ  . TYR A 1 631 ? -15.109 0.712   18.073 1.00 16.77 ? 631  TYR A CZ  1 
ATOM   5028 O OH  . TYR A 1 631 ? -13.832 0.308   17.721 1.00 14.95 ? 631  TYR A OH  1 
ATOM   5029 N N   . THR A 1 632 ? -21.803 2.523   20.834 1.00 13.80 ? 632  THR A N   1 
ATOM   5030 C CA  . THR A 1 632 ? -22.879 3.394   21.366 1.00 12.47 ? 632  THR A CA  1 
ATOM   5031 C C   . THR A 1 632 ? -22.808 3.517   22.892 1.00 13.56 ? 632  THR A C   1 
ATOM   5032 O O   . THR A 1 632 ? -22.996 4.591   23.448 1.00 13.78 ? 632  THR A O   1 
ATOM   5033 C CB  . THR A 1 632 ? -24.290 2.841   20.980 1.00 12.52 ? 632  THR A CB  1 
ATOM   5034 O OG1 . THR A 1 632 ? -24.414 2.784   19.558 1.00 13.28 ? 632  THR A OG1 1 
ATOM   5035 C CG2 . THR A 1 632 ? -25.389 3.755   21.541 1.00 14.78 ? 632  THR A CG2 1 
ATOM   5036 N N   . LEU A 1 633 ? -22.475 2.414   23.555 1.00 12.91 ? 633  LEU A N   1 
ATOM   5037 C CA  . LEU A 1 633 ? -22.369 2.370   25.016 1.00 14.01 ? 633  LEU A CA  1 
ATOM   5038 C C   . LEU A 1 633 ? -20.967 2.661   25.549 1.00 14.05 ? 633  LEU A C   1 
ATOM   5039 O O   . LEU A 1 633 ? -20.743 2.509   26.728 1.00 13.86 ? 633  LEU A O   1 
ATOM   5040 C CB  . LEU A 1 633 ? -22.841 1.013   25.558 1.00 13.98 ? 633  LEU A CB  1 
ATOM   5041 C CG  . LEU A 1 633 ? -24.339 0.766   25.294 1.00 15.75 ? 633  LEU A CG  1 
ATOM   5042 C CD1 . LEU A 1 633 ? -24.631 -0.738  25.501 1.00 16.79 ? 633  LEU A CD1 1 
ATOM   5043 C CD2 . LEU A 1 633 ? -25.168 1.613   26.234 1.00 16.71 ? 633  LEU A CD2 1 
ATOM   5044 N N   . LEU A 1 634 ? -20.050 3.118   24.706 1.00 14.12 ? 634  LEU A N   1 
ATOM   5045 C CA  . LEU A 1 634 ? -18.723 3.436   25.234 1.00 14.78 ? 634  LEU A CA  1 
ATOM   5046 C C   . LEU A 1 634 ? -18.653 4.457   26.379 1.00 13.97 ? 634  LEU A C   1 
ATOM   5047 O O   . LEU A 1 634 ? -17.830 4.286   27.259 1.00 14.66 ? 634  LEU A O   1 
ATOM   5048 C CB  . LEU A 1 634 ? -17.703 3.742   24.118 1.00 14.21 ? 634  LEU A CB  1 
ATOM   5049 C CG  . LEU A 1 634 ? -17.201 2.537   23.292 1.00 19.28 ? 634  LEU A CG  1 
ATOM   5050 C CD1 . LEU A 1 634 ? -16.260 3.027   22.190 1.00 18.95 ? 634  LEU A CD1 1 
ATOM   5051 C CD2 . LEU A 1 634 ? -16.510 1.490   24.138 1.00 20.49 ? 634  LEU A CD2 1 
ATOM   5052 N N   . PRO A 1 635 ? -19.474 5.545   26.370 1.00 13.76 ? 635  PRO A N   1 
ATOM   5053 C CA  . PRO A 1 635 ? -19.447 6.415   27.529 1.00 14.19 ? 635  PRO A CA  1 
ATOM   5054 C C   . PRO A 1 635 ? -19.825 5.681   28.828 1.00 13.58 ? 635  PRO A C   1 
ATOM   5055 O O   . PRO A 1 635 ? -19.298 5.984   29.852 1.00 14.02 ? 635  PRO A O   1 
ATOM   5056 C CB  . PRO A 1 635 ? -20.513 7.498   27.181 1.00 14.64 ? 635  PRO A CB  1 
ATOM   5057 C CG  . PRO A 1 635 ? -20.440 7.568   25.688 1.00 13.21 ? 635  PRO A CG  1 
ATOM   5058 C CD  . PRO A 1 635 ? -20.374 6.094   25.329 1.00 14.42 ? 635  PRO A CD  1 
ATOM   5059 N N   . TYR A 1 636 ? -20.763 4.745   28.766 1.00 12.84 ? 636  TYR A N   1 
ATOM   5060 C CA  . TYR A 1 636 ? -21.102 3.918   29.922 1.00 13.01 ? 636  TYR A CA  1 
ATOM   5061 C C   . TYR A 1 636 ? -19.879 3.017   30.296 1.00 12.10 ? 636  TYR A C   1 
ATOM   5062 O O   . TYR A 1 636 ? -19.434 2.983   31.447 1.00 12.47 ? 636  TYR A O   1 
ATOM   5063 C CB  . TYR A 1 636 ? -22.344 3.092   29.575 1.00 13.57 ? 636  TYR A CB  1 
ATOM   5064 C CG  . TYR A 1 636 ? -22.782 2.119   30.650 1.00 13.53 ? 636  TYR A CG  1 
ATOM   5065 C CD1 . TYR A 1 636 ? -23.135 2.543   31.938 1.00 15.73 ? 636  TYR A CD1 1 
ATOM   5066 C CD2 . TYR A 1 636 ? -22.830 0.763   30.359 1.00 13.17 ? 636  TYR A CD2 1 
ATOM   5067 C CE1 . TYR A 1 636 ? -23.522 1.608   32.944 1.00 16.33 ? 636  TYR A CE1 1 
ATOM   5068 C CE2 . TYR A 1 636 ? -23.206 -0.169  31.329 1.00 14.86 ? 636  TYR A CE2 1 
ATOM   5069 C CZ  . TYR A 1 636 ? -23.565 0.258   32.605 1.00 14.26 ? 636  TYR A CZ  1 
ATOM   5070 O OH  . TYR A 1 636 ? -23.892 -0.713  33.524 1.00 15.27 ? 636  TYR A OH  1 
ATOM   5071 N N   . LEU A 1 637 ? -19.350 2.299   29.327 1.00 11.92 ? 637  LEU A N   1 
ATOM   5072 C CA  . LEU A 1 637 ? -18.207 1.383   29.604 1.00 11.88 ? 637  LEU A CA  1 
ATOM   5073 C C   . LEU A 1 637 ? -17.013 2.178   30.157 1.00 12.03 ? 637  LEU A C   1 
ATOM   5074 O O   . LEU A 1 637 ? -16.320 1.725   31.082 1.00 11.66 ? 637  LEU A O   1 
ATOM   5075 C CB  . LEU A 1 637 ? -17.806 0.615   28.340 1.00 12.30 ? 637  LEU A CB  1 
ATOM   5076 C CG  . LEU A 1 637 ? -16.593 -0.344  28.514 1.00 12.88 ? 637  LEU A CG  1 
ATOM   5077 C CD1 . LEU A 1 637 ? -16.925 -1.473  29.502 1.00 15.52 ? 637  LEU A CD1 1 
ATOM   5078 C CD2 . LEU A 1 637 ? -16.259 -0.900  27.160 1.00 14.38 ? 637  LEU A CD2 1 
ATOM   5079 N N   . TYR A 1 638 ? -16.761 3.352   29.588 1.00 12.47 ? 638  TYR A N   1 
ATOM   5080 C CA  . TYR A 1 638 ? -15.591 4.180   30.039 1.00 11.47 ? 638  TYR A CA  1 
ATOM   5081 C C   . TYR A 1 638 ? -15.809 4.678   31.456 1.00 11.90 ? 638  TYR A C   1 
ATOM   5082 O O   . TYR A 1 638 ? -14.910 4.767   32.280 1.00 11.08 ? 638  TYR A O   1 
ATOM   5083 C CB  . TYR A 1 638 ? -15.449 5.374   29.105 1.00 12.00 ? 638  TYR A CB  1 
ATOM   5084 C CG  . TYR A 1 638 ? -14.182 6.187   29.283 1.00 13.56 ? 638  TYR A CG  1 
ATOM   5085 C CD1 . TYR A 1 638 ? -12.935 5.566   29.228 1.00 12.50 ? 638  TYR A CD1 1 
ATOM   5086 C CD2 . TYR A 1 638 ? -14.240 7.546   29.475 1.00 10.95 ? 638  TYR A CD2 1 
ATOM   5087 C CE1 . TYR A 1 638 ? -11.749 6.315   29.353 1.00 12.03 ? 638  TYR A CE1 1 
ATOM   5088 C CE2 . TYR A 1 638 ? -13.083 8.311   29.598 1.00 13.86 ? 638  TYR A CE2 1 
ATOM   5089 C CZ  . TYR A 1 638 ? -11.844 7.691   29.539 1.00 14.47 ? 638  TYR A CZ  1 
ATOM   5090 O OH  . TYR A 1 638 ? -10.697 8.488   29.647 1.00 13.65 ? 638  TYR A OH  1 
ATOM   5091 N N   . THR A 1 639 ? -17.056 5.031   31.781 1.00 10.47 ? 639  THR A N   1 
ATOM   5092 C CA  . THR A 1 639 ? -17.320 5.439   33.141 1.00 9.56  ? 639  THR A CA  1 
ATOM   5093 C C   . THR A 1 639 ? -17.142 4.264   34.116 1.00 9.55  ? 639  THR A C   1 
ATOM   5094 O O   . THR A 1 639 ? -16.727 4.476   35.258 1.00 11.09 ? 639  THR A O   1 
ATOM   5095 C CB  . THR A 1 639 ? -18.775 6.005   33.270 1.00 8.83  ? 639  THR A CB  1 
ATOM   5096 O OG1 . THR A 1 639 ? -18.879 7.113   32.396 1.00 11.28 ? 639  THR A OG1 1 
ATOM   5097 C CG2 . THR A 1 639 ? -19.051 6.494   34.676 1.00 12.48 ? 639  THR A CG2 1 
ATOM   5098 N N   . LEU A 1 640 ? -17.503 3.057   33.691 1.00 9.94  ? 640  LEU A N   1 
ATOM   5099 C CA  . LEU A 1 640 ? -17.230 1.851   34.481 1.00 10.56 ? 640  LEU A CA  1 
ATOM   5100 C C   . LEU A 1 640 ? -15.733 1.673   34.702 1.00 11.12 ? 640  LEU A C   1 
ATOM   5101 O O   . LEU A 1 640 ? -15.315 1.335   35.806 1.00 10.65 ? 640  LEU A O   1 
ATOM   5102 C CB  . LEU A 1 640 ? -17.782 0.608   33.814 1.00 10.47 ? 640  LEU A CB  1 
ATOM   5103 C CG  . LEU A 1 640 ? -19.302 0.562   33.714 1.00 10.12 ? 640  LEU A CG  1 
ATOM   5104 C CD1 . LEU A 1 640 ? -19.667 -0.724  33.070 1.00 10.44 ? 640  LEU A CD1 1 
ATOM   5105 C CD2 . LEU A 1 640 ? -19.907 0.699   35.130 1.00 12.36 ? 640  LEU A CD2 1 
ATOM   5106 N N   . PHE A 1 641 ? -14.944 1.910   33.666 1.00 12.10 ? 641  PHE A N   1 
ATOM   5107 C CA  . PHE A 1 641 ? -13.477 1.888   33.858 1.00 13.65 ? 641  PHE A CA  1 
ATOM   5108 C C   . PHE A 1 641 ? -12.962 2.972   34.791 1.00 12.74 ? 641  PHE A C   1 
ATOM   5109 O O   . PHE A 1 641 ? -11.986 2.752   35.541 1.00 12.25 ? 641  PHE A O   1 
ATOM   5110 C CB  . PHE A 1 641 ? -12.727 1.930   32.528 1.00 14.16 ? 641  PHE A CB  1 
ATOM   5111 C CG  . PHE A 1 641 ? -12.572 0.590   31.868 1.00 14.51 ? 641  PHE A CG  1 
ATOM   5112 C CD1 . PHE A 1 641 ? -11.542 -0.277  32.261 1.00 15.18 ? 641  PHE A CD1 1 
ATOM   5113 C CD2 . PHE A 1 641 ? -13.454 0.199   30.873 1.00 13.57 ? 641  PHE A CD2 1 
ATOM   5114 C CE1 . PHE A 1 641 ? -11.401 -1.508  31.656 1.00 13.82 ? 641  PHE A CE1 1 
ATOM   5115 C CE2 . PHE A 1 641 ? -13.336 -1.026  30.245 1.00 16.15 ? 641  PHE A CE2 1 
ATOM   5116 C CZ  . PHE A 1 641 ? -12.288 -1.898  30.641 1.00 15.23 ? 641  PHE A CZ  1 
ATOM   5117 N N   . PHE A 1 642 ? -13.557 4.170   34.722 1.00 13.20 ? 642  PHE A N   1 
ATOM   5118 C CA  . PHE A 1 642 ? -13.264 5.216   35.674 1.00 12.09 ? 642  PHE A CA  1 
ATOM   5119 C C   . PHE A 1 642 ? -13.532 4.744   37.106 1.00 12.34 ? 642  PHE A C   1 
ATOM   5120 O O   . PHE A 1 642 ? -12.726 4.999   38.015 1.00 10.82 ? 642  PHE A O   1 
ATOM   5121 C CB  . PHE A 1 642 ? -14.061 6.550   35.389 1.00 13.05 ? 642  PHE A CB  1 
ATOM   5122 C CG  . PHE A 1 642 ? -14.093 7.484   36.546 1.00 13.53 ? 642  PHE A CG  1 
ATOM   5123 C CD1 . PHE A 1 642 ? -12.924 8.153   36.984 1.00 15.22 ? 642  PHE A CD1 1 
ATOM   5124 C CD2 . PHE A 1 642 ? -15.293 7.722   37.228 1.00 17.29 ? 642  PHE A CD2 1 
ATOM   5125 C CE1 . PHE A 1 642 ? -12.956 9.026   38.096 1.00 17.31 ? 642  PHE A CE1 1 
ATOM   5126 C CE2 . PHE A 1 642 ? -15.327 8.600   38.321 1.00 14.00 ? 642  PHE A CE2 1 
ATOM   5127 C CZ  . PHE A 1 642 ? -14.171 9.248   38.762 1.00 16.34 ? 642  PHE A CZ  1 
ATOM   5128 N N   . ARG A 1 643 ? -14.671 4.088   37.339 1.00 11.16 ? 643  ARG A N   1 
ATOM   5129 C CA  . ARG A 1 643 ? -14.922 3.584   38.679 1.00 11.33 ? 643  ARG A CA  1 
ATOM   5130 C C   . ARG A 1 643 ? -13.966 2.458   39.080 1.00 12.43 ? 643  ARG A C   1 
ATOM   5131 O O   . ARG A 1 643 ? -13.561 2.426   40.225 1.00 13.55 ? 643  ARG A O   1 
ATOM   5132 C CB  . ARG A 1 643 ? -16.400 3.178   38.920 1.00 12.28 ? 643  ARG A CB  1 
ATOM   5133 C CG  . ARG A 1 643 ? -17.328 4.384   38.857 1.00 11.48 ? 643  ARG A CG  1 
ATOM   5134 C CD  . ARG A 1 643 ? -17.047 5.378   39.970 1.00 15.48 ? 643  ARG A CD  1 
ATOM   5135 N NE  . ARG A 1 643 ? -18.139 6.359   40.094 1.00 20.32 ? 643  ARG A NE  1 
ATOM   5136 C CZ  . ARG A 1 643 ? -18.108 7.452   40.855 1.00 23.03 ? 643  ARG A CZ  1 
ATOM   5137 N NH1 . ARG A 1 643 ? -17.049 7.743   41.605 1.00 24.79 ? 643  ARG A NH1 1 
ATOM   5138 N NH2 . ARG A 1 643 ? -19.168 8.250   40.890 1.00 25.32 ? 643  ARG A NH2 1 
ATOM   5139 N N   . ALA A 1 644 ? -13.563 1.598   38.148 1.00 12.40 ? 644  ALA A N   1 
ATOM   5140 C CA  . ALA A 1 644 ? -12.561 0.554   38.491 1.00 12.52 ? 644  ALA A CA  1 
ATOM   5141 C C   . ALA A 1 644 ? -11.238 1.210   38.931 1.00 13.80 ? 644  ALA A C   1 
ATOM   5142 O O   . ALA A 1 644 ? -10.628 0.821   39.954 1.00 14.18 ? 644  ALA A O   1 
ATOM   5143 C CB  . ALA A 1 644 ? -12.329 -0.371  37.257 1.00 13.09 ? 644  ALA A CB  1 
ATOM   5144 N N   . HIS A 1 645 ? -10.801 2.198   38.152 1.00 13.97 ? 645  HIS A N   1 
ATOM   5145 C CA  . HIS A 1 645 ? -9.545  2.930   38.425 1.00 14.74 ? 645  HIS A CA  1 
ATOM   5146 C C   . HIS A 1 645 ? -9.592  3.729   39.734 1.00 14.97 ? 645  HIS A C   1 
ATOM   5147 O O   . HIS A 1 645 ? -8.602  3.784   40.459 1.00 14.05 ? 645  HIS A O   1 
ATOM   5148 C CB  . HIS A 1 645 ? -9.212  3.858   37.255 1.00 14.84 ? 645  HIS A CB  1 
ATOM   5149 C CG  . HIS A 1 645 ? -8.056  4.777   37.513 1.00 17.67 ? 645  HIS A CG  1 
ATOM   5150 N ND1 . HIS A 1 645 ? -6.753  4.324   37.575 1.00 19.38 ? 645  HIS A ND1 1 
ATOM   5151 C CD2 . HIS A 1 645 ? -7.998  6.123   37.686 1.00 21.15 ? 645  HIS A CD2 1 
ATOM   5152 C CE1 . HIS A 1 645 ? -5.941  5.348   37.802 1.00 21.65 ? 645  HIS A CE1 1 
ATOM   5153 N NE2 . HIS A 1 645 ? -6.668  6.452   37.865 1.00 24.27 ? 645  HIS A NE2 1 
ATOM   5154 N N   . SER A 1 646 ? -10.712 4.390   40.022 1.00 14.44 ? 646  SER A N   1 
ATOM   5155 C CA  . SER A 1 646 ? -10.731 5.341   41.129 1.00 15.51 ? 646  SER A CA  1 
ATOM   5156 C C   . SER A 1 646 ? -11.247 4.747   42.425 1.00 16.99 ? 646  SER A C   1 
ATOM   5157 O O   . SER A 1 646 ? -10.901 5.206   43.533 1.00 16.69 ? 646  SER A O   1 
ATOM   5158 C CB  . SER A 1 646 ? -11.549 6.581   40.740 1.00 17.37 ? 646  SER A CB  1 
ATOM   5159 O OG  . SER A 1 646 ? -12.879 6.208   40.411 1.00 16.71 ? 646  SER A OG  1 
ATOM   5160 N N   . ARG A 1 647 ? -12.094 3.729   42.289 1.00 15.48 ? 647  ARG A N   1 
ATOM   5161 C CA  . ARG A 1 647 ? -12.814 3.183   43.425 1.00 17.30 ? 647  ARG A CA  1 
ATOM   5162 C C   . ARG A 1 647 ? -12.561 1.680   43.606 1.00 16.26 ? 647  ARG A C   1 
ATOM   5163 O O   . ARG A 1 647 ? -12.644 1.156   44.715 1.00 17.43 ? 647  ARG A O   1 
ATOM   5164 C CB  . ARG A 1 647 ? -14.322 3.436   43.246 1.00 17.09 ? 647  ARG A CB  1 
ATOM   5165 C CG  . ARG A 1 647 ? -15.116 3.119   44.502 1.00 20.67 ? 647  ARG A CG  1 
ATOM   5166 C CD  . ARG A 1 647 ? -16.495 3.790   44.478 1.00 22.28 ? 647  ARG A CD  1 
ATOM   5167 N NE  . ARG A 1 647 ? -17.358 3.224   43.447 1.00 21.16 ? 647  ARG A NE  1 
ATOM   5168 C CZ  . ARG A 1 647 ? -18.440 3.838   42.990 1.00 22.29 ? 647  ARG A CZ  1 
ATOM   5169 N NH1 . ARG A 1 647 ? -18.768 5.053   43.460 1.00 20.99 ? 647  ARG A NH1 1 
ATOM   5170 N NH2 . ARG A 1 647 ? -19.173 3.266   42.044 1.00 22.50 ? 647  ARG A NH2 1 
ATOM   5171 N N   . GLY A 1 648 ? -12.249 1.008   42.506 1.00 14.86 ? 648  GLY A N   1 
ATOM   5172 C CA  . GLY A 1 648 ? -11.961 -0.430  42.502 1.00 15.34 ? 648  GLY A CA  1 
ATOM   5173 C C   . GLY A 1 648 ? -13.127 -1.331  42.114 1.00 16.01 ? 648  GLY A C   1 
ATOM   5174 O O   . GLY A 1 648 ? -13.059 -2.539  42.328 1.00 16.16 ? 648  GLY A O   1 
ATOM   5175 N N   . ASP A 1 649 ? -14.204 -0.766  41.558 1.00 16.56 ? 649  ASP A N   1 
ATOM   5176 C CA  . ASP A 1 649 ? -15.333 -1.592  41.047 1.00 18.00 ? 649  ASP A CA  1 
ATOM   5177 C C   . ASP A 1 649 ? -14.918 -2.543  39.906 1.00 17.95 ? 649  ASP A C   1 
ATOM   5178 O O   . ASP A 1 649 ? -13.968 -2.258  39.160 1.00 19.96 ? 649  ASP A O   1 
ATOM   5179 C CB  . ASP A 1 649 ? -16.455 -0.700  40.461 1.00 18.26 ? 649  ASP A CB  1 
ATOM   5180 C CG  . ASP A 1 649 ? -17.006 0.321   41.425 1.00 21.99 ? 649  ASP A CG  1 
ATOM   5181 O OD1 . ASP A 1 649 ? -16.323 0.734   42.380 1.00 22.91 ? 649  ASP A OD1 1 
ATOM   5182 O OD2 . ASP A 1 649 ? -18.181 0.749   41.195 1.00 26.13 ? 649  ASP A OD2 1 
ATOM   5183 N N   . THR A 1 650 ? -15.634 -3.655  39.722 1.00 15.97 ? 650  THR A N   1 
ATOM   5184 C CA  . THR A 1 650 ? -15.429 -4.476  38.531 1.00 15.14 ? 650  THR A CA  1 
ATOM   5185 C C   . THR A 1 650 ? -16.101 -3.795  37.333 1.00 14.45 ? 650  THR A C   1 
ATOM   5186 O O   . THR A 1 650 ? -17.006 -2.941  37.512 1.00 14.43 ? 650  THR A O   1 
ATOM   5187 C CB  . THR A 1 650 ? -16.020 -5.911  38.697 1.00 16.08 ? 650  THR A CB  1 
ATOM   5188 O OG1 . THR A 1 650 ? -17.412 -5.795  39.036 1.00 15.57 ? 650  THR A OG1 1 
ATOM   5189 C CG2 . THR A 1 650 ? -15.296 -6.668  39.802 1.00 16.34 ? 650  THR A CG2 1 
ATOM   5190 N N   . VAL A 1 651 ? -15.709 -4.216  36.144 1.00 11.39 ? 651  VAL A N   1 
ATOM   5191 C CA  . VAL A 1 651 ? -16.289 -3.722  34.896 1.00 11.73 ? 651  VAL A CA  1 
ATOM   5192 C C   . VAL A 1 651 ? -17.186 -4.791  34.279 1.00 12.10 ? 651  VAL A C   1 
ATOM   5193 O O   . VAL A 1 651 ? -18.394 -4.595  34.244 1.00 12.86 ? 651  VAL A O   1 
ATOM   5194 C CB  . VAL A 1 651 ? -15.202 -3.244  33.902 1.00 10.35 ? 651  VAL A CB  1 
ATOM   5195 C CG1 . VAL A 1 651 ? -15.825 -2.903  32.560 1.00 10.72 ? 651  VAL A CG1 1 
ATOM   5196 C CG2 . VAL A 1 651 ? -14.506 -2.051  34.462 1.00 11.41 ? 651  VAL A CG2 1 
ATOM   5197 N N   . ALA A 1 652 ? -16.611 -5.910  33.807 1.00 13.35 ? 652  ALA A N   1 
ATOM   5198 C CA  . ALA A 1 652 ? -17.378 -7.157  33.580 1.00 12.87 ? 652  ALA A CA  1 
ATOM   5199 C C   . ALA A 1 652 ? -17.640 -7.794  34.937 1.00 13.89 ? 652  ALA A C   1 
ATOM   5200 O O   . ALA A 1 652 ? -16.713 -8.117  35.701 1.00 14.56 ? 652  ALA A O   1 
ATOM   5201 C CB  . ALA A 1 652 ? -16.610 -8.130  32.656 1.00 12.86 ? 652  ALA A CB  1 
ATOM   5202 N N   . ARG A 1 653 ? -18.908 -7.988  35.250 1.00 13.92 ? 653  ARG A N   1 
ATOM   5203 C CA  . ARG A 1 653 ? -19.323 -8.181  36.636 1.00 14.16 ? 653  ARG A CA  1 
ATOM   5204 C C   . ARG A 1 653 ? -20.214 -9.396  36.691 1.00 12.88 ? 653  ARG A C   1 
ATOM   5205 O O   . ARG A 1 653 ? -21.060 -9.573  35.791 1.00 12.68 ? 653  ARG A O   1 
ATOM   5206 C CB  . ARG A 1 653 ? -20.075 -6.936  37.121 1.00 13.90 ? 653  ARG A CB  1 
ATOM   5207 C CG  . ARG A 1 653 ? -20.411 -6.993  38.605 1.00 14.97 ? 653  ARG A CG  1 
ATOM   5208 C CD  . ARG A 1 653 ? -21.002 -5.679  39.087 1.00 14.38 ? 653  ARG A CD  1 
ATOM   5209 N NE  . ARG A 1 653 ? -20.045 -4.562  38.874 1.00 13.28 ? 653  ARG A NE  1 
ATOM   5210 C CZ  . ARG A 1 653 ? -20.352 -3.298  39.101 1.00 16.74 ? 653  ARG A CZ  1 
ATOM   5211 N NH1 . ARG A 1 653 ? -21.551 -2.994  39.587 1.00 11.56 ? 653  ARG A NH1 1 
ATOM   5212 N NH2 . ARG A 1 653 ? -19.470 -2.327  38.855 1.00 16.41 ? 653  ARG A NH2 1 
ATOM   5213 N N   . PRO A 1 654 ? -19.993 -10.291 37.686 1.00 14.25 ? 654  PRO A N   1 
ATOM   5214 C CA  . PRO A 1 654 ? -20.888 -11.460 37.814 1.00 13.21 ? 654  PRO A CA  1 
ATOM   5215 C C   . PRO A 1 654 ? -22.290 -11.034 38.212 1.00 12.69 ? 654  PRO A C   1 
ATOM   5216 O O   . PRO A 1 654 ? -22.455 -10.066 38.916 1.00 13.14 ? 654  PRO A O   1 
ATOM   5217 C CB  . PRO A 1 654 ? -20.244 -12.277 38.934 1.00 14.17 ? 654  PRO A CB  1 
ATOM   5218 C CG  . PRO A 1 654 ? -18.701 -11.767 38.961 1.00 13.77 ? 654  PRO A CG  1 
ATOM   5219 C CD  . PRO A 1 654 ? -18.878 -10.307 38.677 1.00 12.80 ? 654  PRO A CD  1 
ATOM   5220 N N   . LEU A 1 655 ? -23.307 -11.758 37.778 1.00 12.35 ? 655  LEU A N   1 
ATOM   5221 C CA  . LEU A 1 655 ? -24.663 -11.439 38.244 1.00 12.73 ? 655  LEU A CA  1 
ATOM   5222 C C   . LEU A 1 655 ? -24.779 -11.367 39.745 1.00 12.34 ? 655  LEU A C   1 
ATOM   5223 O O   . LEU A 1 655 ? -25.472 -10.523 40.263 1.00 13.70 ? 655  LEU A O   1 
ATOM   5224 C CB  . LEU A 1 655 ? -25.659 -12.486 37.720 1.00 13.52 ? 655  LEU A CB  1 
ATOM   5225 C CG  . LEU A 1 655 ? -26.300 -12.133 36.375 1.00 14.63 ? 655  LEU A CG  1 
ATOM   5226 C CD1 . LEU A 1 655 ? -25.239 -11.990 35.260 1.00 15.55 ? 655  LEU A CD1 1 
ATOM   5227 C CD2 . LEU A 1 655 ? -27.363 -13.241 36.048 1.00 14.52 ? 655  LEU A CD2 1 
ATOM   5228 N N   . LEU A 1 656 ? -24.099 -12.270 40.452 1.00 12.66 ? 656  LEU A N   1 
ATOM   5229 C CA  . LEU A 1 656 ? -24.156 -12.349 41.910 1.00 13.00 ? 656  LEU A CA  1 
ATOM   5230 C C   . LEU A 1 656 ? -23.605 -11.112 42.631 1.00 13.11 ? 656  LEU A C   1 
ATOM   5231 O O   . LEU A 1 656 ? -23.936 -10.897 43.779 1.00 13.01 ? 656  LEU A O   1 
ATOM   5232 C CB  . LEU A 1 656 ? -23.461 -13.645 42.397 1.00 13.65 ? 656  LEU A CB  1 
ATOM   5233 C CG  . LEU A 1 656 ? -21.931 -13.584 42.337 1.00 14.46 ? 656  LEU A CG  1 
ATOM   5234 C CD1 . LEU A 1 656 ? -21.340 -13.313 43.752 1.00 16.11 ? 656  LEU A CD1 1 
ATOM   5235 C CD2 . LEU A 1 656 ? -21.381 -14.901 41.778 1.00 16.35 ? 656  LEU A CD2 1 
ATOM   5236 N N   . HIS A 1 657 ? -22.774 -10.290 41.979 1.00 13.05 ? 657  HIS A N   1 
ATOM   5237 C CA  . HIS A 1 657 ? -22.304 -9.076  42.640 1.00 13.17 ? 657  HIS A CA  1 
ATOM   5238 C C   . HIS A 1 657 ? -23.418 -8.034  42.763 1.00 14.11 ? 657  HIS A C   1 
ATOM   5239 O O   . HIS A 1 657 ? -23.373 -7.188  43.633 1.00 15.01 ? 657  HIS A O   1 
ATOM   5240 C CB  . HIS A 1 657 ? -21.128 -8.447  41.887 1.00 13.41 ? 657  HIS A CB  1 
ATOM   5241 C CG  . HIS A 1 657 ? -19.840 -9.204  42.076 1.00 12.18 ? 657  HIS A CG  1 
ATOM   5242 N ND1 . HIS A 1 657 ? -18.614 -8.573  42.129 1.00 12.50 ? 657  HIS A ND1 1 
ATOM   5243 C CD2 . HIS A 1 657 ? -19.603 -10.508 42.323 1.00 14.81 ? 657  HIS A CD2 1 
ATOM   5244 C CE1 . HIS A 1 657 ? -17.661 -9.476  42.338 1.00 14.63 ? 657  HIS A CE1 1 
ATOM   5245 N NE2 . HIS A 1 657 ? -18.232 -10.657 42.463 1.00 13.02 ? 657  HIS A NE2 1 
ATOM   5246 N N   . GLU A 1 658 ? -24.384 -8.106  41.873 1.00 13.63 ? 658  GLU A N   1 
ATOM   5247 C CA  . GLU A 1 658 ? -25.556 -7.237  41.989 1.00 14.61 ? 658  GLU A CA  1 
ATOM   5248 C C   . GLU A 1 658 ? -26.733 -7.938  42.605 1.00 15.05 ? 658  GLU A C   1 
ATOM   5249 O O   . GLU A 1 658 ? -27.643 -7.277  43.138 1.00 15.78 ? 658  GLU A O   1 
ATOM   5250 C CB  . GLU A 1 658 ? -25.967 -6.749  40.618 1.00 14.65 ? 658  GLU A CB  1 
ATOM   5251 C CG  . GLU A 1 658 ? -24.973 -5.741  39.996 1.00 14.64 ? 658  GLU A CG  1 
ATOM   5252 C CD  . GLU A 1 658 ? -24.789 -4.477  40.793 1.00 19.47 ? 658  GLU A CD  1 
ATOM   5253 O OE1 . GLU A 1 658 ? -25.800 -3.850  41.219 1.00 18.37 ? 658  GLU A OE1 1 
ATOM   5254 O OE2 . GLU A 1 658 ? -23.608 -4.077  40.962 1.00 16.68 ? 658  GLU A OE2 1 
ATOM   5255 N N   . PHE A 1 659 ? -26.775 -9.255  42.462 1.00 14.40 ? 659  PHE A N   1 
ATOM   5256 C CA  . PHE A 1 659 ? -27.998 -10.008 42.833 1.00 15.14 ? 659  PHE A CA  1 
ATOM   5257 C C   . PHE A 1 659 ? -27.719 -11.119 43.858 1.00 15.74 ? 659  PHE A C   1 
ATOM   5258 O O   . PHE A 1 659 ? -28.361 -12.194 43.837 1.00 15.08 ? 659  PHE A O   1 
ATOM   5259 C CB  . PHE A 1 659 ? -28.703 -10.513 41.560 1.00 14.47 ? 659  PHE A CB  1 
ATOM   5260 C CG  . PHE A 1 659 ? -29.100 -9.411  40.641 1.00 14.14 ? 659  PHE A CG  1 
ATOM   5261 C CD1 . PHE A 1 659 ? -30.189 -8.580  40.975 1.00 14.05 ? 659  PHE A CD1 1 
ATOM   5262 C CD2 . PHE A 1 659 ? -28.416 -9.190  39.449 1.00 13.40 ? 659  PHE A CD2 1 
ATOM   5263 C CE1 . PHE A 1 659 ? -30.573 -7.521  40.112 1.00 13.23 ? 659  PHE A CE1 1 
ATOM   5264 C CE2 . PHE A 1 659 ? -28.783 -8.140  38.586 1.00 14.24 ? 659  PHE A CE2 1 
ATOM   5265 C CZ  . PHE A 1 659 ? -29.910 -7.313  38.932 1.00 13.97 ? 659  PHE A CZ  1 
ATOM   5266 N N   . TYR A 1 660 ? -26.808 -10.810 44.797 1.00 15.71 ? 660  TYR A N   1 
ATOM   5267 C CA  . TYR A 1 660 ? -26.319 -11.778 45.847 1.00 16.61 ? 660  TYR A CA  1 
ATOM   5268 C C   . TYR A 1 660 ? -27.456 -12.279 46.737 1.00 16.64 ? 660  TYR A C   1 
ATOM   5269 O O   . TYR A 1 660 ? -27.371 -13.360 47.291 1.00 16.76 ? 660  TYR A O   1 
ATOM   5270 C CB  . TYR A 1 660 ? -25.242 -11.162 46.755 1.00 16.38 ? 660  TYR A CB  1 
ATOM   5271 C CG  . TYR A 1 660 ? -25.472 -9.730  47.098 1.00 17.47 ? 660  TYR A CG  1 
ATOM   5272 C CD1 . TYR A 1 660 ? -26.285 -9.357  48.151 1.00 15.33 ? 660  TYR A CD1 1 
ATOM   5273 C CD2 . TYR A 1 660 ? -24.811 -8.704  46.379 1.00 18.19 ? 660  TYR A CD2 1 
ATOM   5274 C CE1 . TYR A 1 660 ? -26.498 -8.012  48.449 1.00 17.32 ? 660  TYR A CE1 1 
ATOM   5275 C CE2 . TYR A 1 660 ? -25.023 -7.395  46.666 1.00 20.44 ? 660  TYR A CE2 1 
ATOM   5276 C CZ  . TYR A 1 660 ? -25.873 -7.045  47.694 1.00 19.83 ? 660  TYR A CZ  1 
ATOM   5277 O OH  . TYR A 1 660 ? -26.055 -5.719  47.951 1.00 21.56 ? 660  TYR A OH  1 
ATOM   5278 N N   . GLU A 1 661 ? -28.518 -11.486 46.882 1.00 17.50 ? 661  GLU A N   1 
ATOM   5279 C CA  . GLU A 1 661 ? -29.684 -11.913 47.686 1.00 19.33 ? 661  GLU A CA  1 
ATOM   5280 C C   . GLU A 1 661 ? -30.395 -13.112 47.081 1.00 17.83 ? 661  GLU A C   1 
ATOM   5281 O O   . GLU A 1 661 ? -31.131 -13.831 47.774 1.00 18.10 ? 661  GLU A O   1 
ATOM   5282 C CB  . GLU A 1 661 ? -30.689 -10.737 47.906 1.00 19.32 ? 661  GLU A CB  1 
ATOM   5283 C CG  . GLU A 1 661 ? -30.104 -9.596  48.772 1.00 23.08 ? 661  GLU A CG  1 
ATOM   5284 C CD  . GLU A 1 661 ? -31.115 -8.503  49.155 1.00 26.56 ? 661  GLU A CD  1 
ATOM   5285 O OE1 . GLU A 1 661 ? -32.324 -8.628  48.795 1.00 35.90 ? 661  GLU A OE1 1 
ATOM   5286 O OE2 . GLU A 1 661 ? -30.705 -7.518  49.830 1.00 34.41 ? 661  GLU A OE2 1 
ATOM   5287 N N   . ASP A 1 662 ? -30.161 -13.337 45.793 1.00 16.79 ? 662  ASP A N   1 
ATOM   5288 C CA  . ASP A 1 662 ? -30.788 -14.392 45.037 1.00 16.95 ? 662  ASP A CA  1 
ATOM   5289 C C   . ASP A 1 662 ? -29.850 -15.555 44.769 1.00 17.55 ? 662  ASP A C   1 
ATOM   5290 O O   . ASP A 1 662 ? -29.050 -15.481 43.839 1.00 16.65 ? 662  ASP A O   1 
ATOM   5291 C CB  . ASP A 1 662 ? -31.295 -13.781 43.718 1.00 16.62 ? 662  ASP A CB  1 
ATOM   5292 C CG  . ASP A 1 662 ? -32.065 -14.764 42.842 1.00 17.75 ? 662  ASP A CG  1 
ATOM   5293 O OD1 . ASP A 1 662 ? -32.195 -15.971 43.165 1.00 17.60 ? 662  ASP A OD1 1 
ATOM   5294 O OD2 . ASP A 1 662 ? -32.545 -14.292 41.794 1.00 18.42 ? 662  ASP A OD2 1 
ATOM   5295 N N   . ASN A 1 663 ? -29.966 -16.650 45.549 1.00 16.28 ? 663  ASN A N   1 
ATOM   5296 C CA  . ASN A 1 663 ? -29.075 -17.801 45.362 1.00 17.75 ? 663  ASN A CA  1 
ATOM   5297 C C   . ASN A 1 663 ? -29.051 -18.426 43.952 1.00 16.46 ? 663  ASN A C   1 
ATOM   5298 O O   . ASN A 1 663 ? -28.066 -19.103 43.611 1.00 16.18 ? 663  ASN A O   1 
ATOM   5299 C CB  . ASN A 1 663 ? -29.280 -18.886 46.451 1.00 17.51 ? 663  ASN A CB  1 
ATOM   5300 C CG  . ASN A 1 663 ? -30.543 -19.669 46.228 1.00 21.99 ? 663  ASN A CG  1 
ATOM   5301 O OD1 . ASN A 1 663 ? -31.529 -19.120 45.766 1.00 27.45 ? 663  ASN A OD1 1 
ATOM   5302 N ND2 . ASN A 1 663 ? -30.526 -20.958 46.555 1.00 26.98 ? 663  ASN A ND2 1 
ATOM   5303 N N   . SER A 1 664 ? -30.078 -18.207 43.109 1.00 16.62 ? 664  SER A N   1 
ATOM   5304 C CA  . SER A 1 664 ? -29.998 -18.681 41.717 1.00 17.58 ? 664  SER A CA  1 
ATOM   5305 C C   . SER A 1 664 ? -28.901 -17.997 40.875 1.00 17.26 ? 664  SER A C   1 
ATOM   5306 O O   . SER A 1 664 ? -28.592 -18.471 39.786 1.00 19.49 ? 664  SER A O   1 
ATOM   5307 C CB  . SER A 1 664 ? -31.338 -18.558 40.959 1.00 18.56 ? 664  SER A CB  1 
ATOM   5308 O OG  . SER A 1 664 ? -32.332 -19.199 41.692 1.00 20.26 ? 664  SER A OG  1 
ATOM   5309 N N   . THR A 1 665 ? -28.343 -16.897 41.364 1.00 16.54 ? 665  THR A N   1 
ATOM   5310 C CA  . THR A 1 665 ? -27.272 -16.206 40.627 1.00 15.33 ? 665  THR A CA  1 
ATOM   5311 C C   . THR A 1 665 ? -25.875 -16.684 41.035 1.00 16.52 ? 665  THR A C   1 
ATOM   5312 O O   . THR A 1 665 ? -24.904 -16.322 40.359 1.00 16.15 ? 665  THR A O   1 
ATOM   5313 C CB  . THR A 1 665 ? -27.316 -14.680 40.787 1.00 16.42 ? 665  THR A CB  1 
ATOM   5314 O OG1 . THR A 1 665 ? -27.033 -14.287 42.133 1.00 16.01 ? 665  THR A OG1 1 
ATOM   5315 C CG2 . THR A 1 665 ? -28.657 -14.120 40.366 1.00 14.47 ? 665  THR A CG2 1 
ATOM   5316 N N   . TRP A 1 666 ? -25.773 -17.465 42.121 1.00 15.39 ? 666  TRP A N   1 
ATOM   5317 C CA  . TRP A 1 666 ? -24.452 -17.753 42.723 1.00 16.15 ? 666  TRP A CA  1 
ATOM   5318 C C   . TRP A 1 666 ? -23.558 -18.622 41.862 1.00 16.73 ? 666  TRP A C   1 
ATOM   5319 O O   . TRP A 1 666 ? -22.337 -18.633 42.044 1.00 16.27 ? 666  TRP A O   1 
ATOM   5320 C CB  . TRP A 1 666 ? -24.568 -18.370 44.126 1.00 16.21 ? 666  TRP A CB  1 
ATOM   5321 C CG  . TRP A 1 666 ? -25.265 -17.474 45.177 1.00 17.83 ? 666  TRP A CG  1 
ATOM   5322 C CD1 . TRP A 1 666 ? -25.596 -16.161 45.058 1.00 15.92 ? 666  TRP A CD1 1 
ATOM   5323 C CD2 . TRP A 1 666 ? -25.605 -17.858 46.502 1.00 18.08 ? 666  TRP A CD2 1 
ATOM   5324 N NE1 . TRP A 1 666 ? -26.193 -15.702 46.232 1.00 18.97 ? 666  TRP A NE1 1 
ATOM   5325 C CE2 . TRP A 1 666 ? -26.206 -16.734 47.133 1.00 18.32 ? 666  TRP A CE2 1 
ATOM   5326 C CE3 . TRP A 1 666 ? -25.510 -19.068 47.212 1.00 22.43 ? 666  TRP A CE3 1 
ATOM   5327 C CZ2 . TRP A 1 666 ? -26.676 -16.772 48.446 1.00 17.74 ? 666  TRP A CZ2 1 
ATOM   5328 C CZ3 . TRP A 1 666 ? -25.978 -19.098 48.555 1.00 19.35 ? 666  TRP A CZ3 1 
ATOM   5329 C CH2 . TRP A 1 666 ? -26.564 -17.954 49.134 1.00 19.56 ? 666  TRP A CH2 1 
ATOM   5330 N N   . ASP A 1 667 ? -24.128 -19.372 40.934 1.00 17.41 ? 667  ASP A N   1 
ATOM   5331 C CA  . ASP A 1 667 ? -23.226 -20.078 40.036 1.00 20.08 ? 667  ASP A CA  1 
ATOM   5332 C C   . ASP A 1 667 ? -23.378 -19.694 38.575 1.00 19.54 ? 667  ASP A C   1 
ATOM   5333 O O   . ASP A 1 667 ? -22.822 -20.360 37.695 1.00 21.33 ? 667  ASP A O   1 
ATOM   5334 C CB  . ASP A 1 667 ? -23.218 -21.580 40.281 1.00 21.92 ? 667  ASP A CB  1 
ATOM   5335 C CG  . ASP A 1 667 ? -24.496 -22.229 39.931 1.00 27.81 ? 667  ASP A CG  1 
ATOM   5336 O OD1 . ASP A 1 667 ? -25.506 -21.507 39.739 1.00 34.37 ? 667  ASP A OD1 1 
ATOM   5337 O OD2 . ASP A 1 667 ? -24.466 -23.474 39.832 1.00 35.14 ? 667  ASP A OD2 1 
ATOM   5338 N N   . VAL A 1 668 ? -24.065 -18.589 38.314 1.00 17.21 ? 668  VAL A N   1 
ATOM   5339 C CA  . VAL A 1 668 ? -24.278 -18.161 36.928 1.00 16.90 ? 668  VAL A CA  1 
ATOM   5340 C C   . VAL A 1 668 ? -22.962 -17.732 36.316 1.00 17.47 ? 668  VAL A C   1 
ATOM   5341 O O   . VAL A 1 668 ? -22.324 -16.827 36.827 1.00 17.54 ? 668  VAL A O   1 
ATOM   5342 C CB  . VAL A 1 668 ? -25.334 -17.039 36.810 1.00 16.87 ? 668  VAL A CB  1 
ATOM   5343 C CG1 . VAL A 1 668 ? -25.367 -16.482 35.417 1.00 16.98 ? 668  VAL A CG1 1 
ATOM   5344 C CG2 . VAL A 1 668 ? -26.688 -17.604 37.165 1.00 17.25 ? 668  VAL A CG2 1 
ATOM   5345 N N   . HIS A 1 669 ? -22.573 -18.398 35.232 1.00 17.76 ? 669  HIS A N   1 
ATOM   5346 C CA  . HIS A 1 669 ? -21.305 -18.118 34.555 1.00 19.70 ? 669  HIS A CA  1 
ATOM   5347 C C   . HIS A 1 669 ? -21.500 -18.090 33.024 1.00 19.85 ? 669  HIS A C   1 
ATOM   5348 O O   . HIS A 1 669 ? -20.523 -18.012 32.292 1.00 20.01 ? 669  HIS A O   1 
ATOM   5349 C CB  . HIS A 1 669 ? -20.245 -19.185 34.954 1.00 19.57 ? 669  HIS A CB  1 
ATOM   5350 C CG  . HIS A 1 669 ? -20.645 -20.590 34.639 1.00 24.29 ? 669  HIS A CG  1 
ATOM   5351 N ND1 . HIS A 1 669 ? -20.112 -21.289 33.582 1.00 26.86 ? 669  HIS A ND1 1 
ATOM   5352 C CD2 . HIS A 1 669 ? -21.588 -21.397 35.182 1.00 28.90 ? 669  HIS A CD2 1 
ATOM   5353 C CE1 . HIS A 1 669 ? -20.672 -22.481 33.513 1.00 29.91 ? 669  HIS A CE1 1 
ATOM   5354 N NE2 . HIS A 1 669 ? -21.570 -22.576 34.474 1.00 32.64 ? 669  HIS A NE2 1 
ATOM   5355 N N   . GLN A 1 670 ? -22.746 -18.181 32.548 1.00 17.88 ? 670  GLN A N   1 
ATOM   5356 C CA  . GLN A 1 670 ? -23.034 -18.180 31.105 1.00 19.68 ? 670  GLN A CA  1 
ATOM   5357 C C   . GLN A 1 670 ? -23.649 -16.837 30.678 1.00 18.16 ? 670  GLN A C   1 
ATOM   5358 O O   . GLN A 1 670 ? -24.049 -16.650 29.518 1.00 17.33 ? 670  GLN A O   1 
ATOM   5359 C CB  . GLN A 1 670 ? -24.011 -19.324 30.745 1.00 19.99 ? 670  GLN A CB  1 
ATOM   5360 C CG  . GLN A 1 670 ? -23.358 -20.716 30.545 1.00 24.39 ? 670  GLN A CG  1 
ATOM   5361 C CD  . GLN A 1 670 ? -24.110 -21.613 29.478 1.00 26.50 ? 670  GLN A CD  1 
ATOM   5362 O OE1 . GLN A 1 670 ? -23.536 -22.584 28.931 1.00 31.11 ? 670  GLN A OE1 1 
ATOM   5363 N NE2 . GLN A 1 670 ? -25.373 -21.254 29.163 1.00 31.95 ? 670  GLN A NE2 1 
ATOM   5364 N N   . GLN A 1 671 ? -23.761 -15.939 31.663 1.00 16.12 ? 671  GLN A N   1 
ATOM   5365 C CA  . GLN A 1 671 ? -24.228 -14.578 31.503 1.00 15.16 ? 671  GLN A CA  1 
ATOM   5366 C C   . GLN A 1 671 ? -23.312 -13.685 32.338 1.00 14.56 ? 671  GLN A C   1 
ATOM   5367 O O   . GLN A 1 671 ? -22.674 -14.172 33.269 1.00 15.10 ? 671  GLN A O   1 
ATOM   5368 C CB  . GLN A 1 671 ? -25.638 -14.458 32.075 1.00 15.74 ? 671  GLN A CB  1 
ATOM   5369 C CG  . GLN A 1 671 ? -26.744 -15.022 31.174 1.00 17.04 ? 671  GLN A CG  1 
ATOM   5370 C CD  . GLN A 1 671 ? -28.049 -15.082 31.924 1.00 19.40 ? 671  GLN A CD  1 
ATOM   5371 O OE1 . GLN A 1 671 ? -28.230 -15.948 32.769 1.00 19.93 ? 671  GLN A OE1 1 
ATOM   5372 N NE2 . GLN A 1 671 ? -28.936 -14.104 31.679 1.00 20.75 ? 671  GLN A NE2 1 
ATOM   5373 N N   . PHE A 1 672 ? -23.244 -12.403 32.005 1.00 13.79 ? 672  PHE A N   1 
ATOM   5374 C CA  . PHE A 1 672 ? -22.574 -11.442 32.875 1.00 13.89 ? 672  PHE A CA  1 
ATOM   5375 C C   . PHE A 1 672 ? -23.144 -10.052 32.677 1.00 14.04 ? 672  PHE A C   1 
ATOM   5376 O O   . PHE A 1 672 ? -24.025 -9.832  31.804 1.00 13.03 ? 672  PHE A O   1 
ATOM   5377 C CB  . PHE A 1 672 ? -21.037 -11.501 32.666 1.00 14.22 ? 672  PHE A CB  1 
ATOM   5378 C CG  . PHE A 1 672 ? -20.585 -11.041 31.316 1.00 15.61 ? 672  PHE A CG  1 
ATOM   5379 C CD1 . PHE A 1 672 ? -20.020 -9.777  31.156 1.00 16.97 ? 672  PHE A CD1 1 
ATOM   5380 C CD2 . PHE A 1 672 ? -20.663 -11.882 30.213 1.00 16.67 ? 672  PHE A CD2 1 
ATOM   5381 C CE1 . PHE A 1 672 ? -19.600 -9.328  29.902 1.00 16.47 ? 672  PHE A CE1 1 
ATOM   5382 C CE2 . PHE A 1 672 ? -20.244 -11.448 28.955 1.00 19.43 ? 672  PHE A CE2 1 
ATOM   5383 C CZ  . PHE A 1 672 ? -19.710 -10.166 28.792 1.00 16.52 ? 672  PHE A CZ  1 
ATOM   5384 N N   . LEU A 1 673 ? -22.690 -9.112  33.502 1.00 12.98 ? 673  LEU A N   1 
ATOM   5385 C CA  . LEU A 1 673 ? -23.134 -7.740  33.388 1.00 13.87 ? 673  LEU A CA  1 
ATOM   5386 C C   . LEU A 1 673 ? -21.987 -6.844  32.944 1.00 14.98 ? 673  LEU A C   1 
ATOM   5387 O O   . LEU A 1 673 ? -20.822 -7.121  33.265 1.00 14.99 ? 673  LEU A O   1 
ATOM   5388 C CB  . LEU A 1 673 ? -23.599 -7.245  34.741 1.00 13.07 ? 673  LEU A CB  1 
ATOM   5389 C CG  . LEU A 1 673 ? -24.528 -8.156  35.531 1.00 14.11 ? 673  LEU A CG  1 
ATOM   5390 C CD1 . LEU A 1 673 ? -24.622 -7.633  36.959 1.00 14.82 ? 673  LEU A CD1 1 
ATOM   5391 C CD2 . LEU A 1 673 ? -25.899 -8.162  34.884 1.00 16.98 ? 673  LEU A CD2 1 
ATOM   5392 N N   . TRP A 1 674 ? -22.327 -5.768  32.245 1.00 14.80 ? 674  TRP A N   1 
ATOM   5393 C CA  . TRP A 1 674 ? -21.458 -4.589  32.272 1.00 15.13 ? 674  TRP A CA  1 
ATOM   5394 C C   . TRP A 1 674 ? -21.905 -3.722  33.430 1.00 15.55 ? 674  TRP A C   1 
ATOM   5395 O O   . TRP A 1 674 ? -23.017 -3.136  33.365 1.00 15.33 ? 674  TRP A O   1 
ATOM   5396 C CB  . TRP A 1 674 ? -21.640 -3.786  30.990 1.00 14.75 ? 674  TRP A CB  1 
ATOM   5397 C CG  . TRP A 1 674 ? -20.816 -4.178  29.808 1.00 15.06 ? 674  TRP A CG  1 
ATOM   5398 C CD1 . TRP A 1 674 ? -20.130 -5.340  29.600 1.00 16.69 ? 674  TRP A CD1 1 
ATOM   5399 C CD2 . TRP A 1 674 ? -20.587 -3.355  28.664 1.00 14.72 ? 674  TRP A CD2 1 
ATOM   5400 N NE1 . TRP A 1 674 ? -19.481 -5.287  28.373 1.00 18.01 ? 674  TRP A NE1 1 
ATOM   5401 C CE2 . TRP A 1 674 ? -19.750 -4.074  27.787 1.00 17.18 ? 674  TRP A CE2 1 
ATOM   5402 C CE3 . TRP A 1 674 ? -21.000 -2.057  28.306 1.00 15.64 ? 674  TRP A CE3 1 
ATOM   5403 C CZ2 . TRP A 1 674 ? -19.340 -3.555  26.560 1.00 16.87 ? 674  TRP A CZ2 1 
ATOM   5404 C CZ3 . TRP A 1 674 ? -20.576 -1.536  27.082 1.00 15.58 ? 674  TRP A CZ3 1 
ATOM   5405 C CH2 . TRP A 1 674 ? -19.746 -2.291  26.233 1.00 16.65 ? 674  TRP A CH2 1 
ATOM   5406 N N   . GLY A 1 675 ? -21.042 -3.560  34.443 1.00 14.35 ? 675  GLY A N   1 
ATOM   5407 C CA  . GLY A 1 675 ? -21.402 -2.736  35.599 1.00 13.88 ? 675  GLY A CA  1 
ATOM   5408 C C   . GLY A 1 675 ? -22.703 -3.225  36.258 1.00 13.82 ? 675  GLY A C   1 
ATOM   5409 O O   . GLY A 1 675 ? -22.939 -4.426  36.317 1.00 12.61 ? 675  GLY A O   1 
ATOM   5410 N N   . PRO A 1 676 ? -23.505 -2.305  36.786 1.00 14.32 ? 676  PRO A N   1 
ATOM   5411 C CA  . PRO A 1 676 ? -24.734 -2.755  37.443 1.00 15.92 ? 676  PRO A CA  1 
ATOM   5412 C C   . PRO A 1 676 ? -25.911 -2.996  36.501 1.00 16.67 ? 676  PRO A C   1 
ATOM   5413 O O   . PRO A 1 676 ? -26.872 -3.684  36.894 1.00 17.56 ? 676  PRO A O   1 
ATOM   5414 C CB  . PRO A 1 676 ? -25.044 -1.604  38.394 1.00 15.66 ? 676  PRO A CB  1 
ATOM   5415 C CG  . PRO A 1 676 ? -24.530 -0.369  37.614 1.00 17.13 ? 676  PRO A CG  1 
ATOM   5416 C CD  . PRO A 1 676 ? -23.268 -0.852  36.959 1.00 14.03 ? 676  PRO A CD  1 
ATOM   5417 N N   . GLY A 1 677 ? -25.824 -2.513  35.267 1.00 16.02 ? 677  GLY A N   1 
ATOM   5418 C CA  . GLY A 1 677 ? -27.055 -2.234  34.512 1.00 16.62 ? 677  GLY A CA  1 
ATOM   5419 C C   . GLY A 1 677 ? -27.314 -2.980  33.218 1.00 16.48 ? 677  GLY A C   1 
ATOM   5420 O O   . GLY A 1 677 ? -28.450 -2.992  32.741 1.00 16.44 ? 677  GLY A O   1 
ATOM   5421 N N   . LEU A 1 678 ? -26.269 -3.538  32.597 1.00 15.51 ? 678  LEU A N   1 
ATOM   5422 C CA  . LEU A 1 678 ? -26.457 -4.219  31.300 1.00 15.23 ? 678  LEU A CA  1 
ATOM   5423 C C   . LEU A 1 678 ? -26.242 -5.718  31.444 1.00 15.76 ? 678  LEU A C   1 
ATOM   5424 O O   . LEU A 1 678 ? -25.162 -6.172  31.812 1.00 15.83 ? 678  LEU A O   1 
ATOM   5425 C CB  . LEU A 1 678 ? -25.526 -3.631  30.212 1.00 15.64 ? 678  LEU A CB  1 
ATOM   5426 C CG  . LEU A 1 678 ? -25.446 -4.345  28.847 1.00 14.11 ? 678  LEU A CG  1 
ATOM   5427 C CD1 . LEU A 1 678 ? -26.776 -4.081  28.125 1.00 17.74 ? 678  LEU A CD1 1 
ATOM   5428 C CD2 . LEU A 1 678 ? -24.330 -3.701  28.043 1.00 15.73 ? 678  LEU A CD2 1 
ATOM   5429 N N   . LEU A 1 679 ? -27.270 -6.493  31.133 1.00 14.32 ? 679  LEU A N   1 
ATOM   5430 C CA  . LEU A 1 679 ? -27.215 -7.938  31.220 1.00 14.47 ? 679  LEU A CA  1 
ATOM   5431 C C   . LEU A 1 679 ? -26.966 -8.529  29.836 1.00 14.38 ? 679  LEU A C   1 
ATOM   5432 O O   . LEU A 1 679 ? -27.711 -8.274  28.875 1.00 14.15 ? 679  LEU A O   1 
ATOM   5433 C CB  . LEU A 1 679 ? -28.574 -8.440  31.770 1.00 13.60 ? 679  LEU A CB  1 
ATOM   5434 C CG  . LEU A 1 679 ? -28.752 -9.942  31.840 1.00 13.57 ? 679  LEU A CG  1 
ATOM   5435 C CD1 . LEU A 1 679 ? -27.748 -10.680 32.816 1.00 17.60 ? 679  LEU A CD1 1 
ATOM   5436 C CD2 . LEU A 1 679 ? -30.219 -10.284 32.113 1.00 15.63 ? 679  LEU A CD2 1 
ATOM   5437 N N   . ILE A 1 680 ? -25.897 -9.306  29.725 1.00 13.96 ? 680  ILE A N   1 
ATOM   5438 C CA  . ILE A 1 680 ? -25.516 -9.916  28.458 1.00 14.36 ? 680  ILE A CA  1 
ATOM   5439 C C   . ILE A 1 680 ? -25.758 -11.433 28.506 1.00 15.01 ? 680  ILE A C   1 
ATOM   5440 O O   . ILE A 1 680 ? -25.198 -12.137 29.354 1.00 14.42 ? 680  ILE A O   1 
ATOM   5441 C CB  . ILE A 1 680 ? -24.014 -9.625  28.128 1.00 14.00 ? 680  ILE A CB  1 
ATOM   5442 C CG1 . ILE A 1 680 ? -23.812 -8.113  27.996 1.00 15.36 ? 680  ILE A CG1 1 
ATOM   5443 C CG2 . ILE A 1 680 ? -23.607 -10.307 26.797 1.00 15.46 ? 680  ILE A CG2 1 
ATOM   5444 C CD1 . ILE A 1 680 ? -22.705 -7.519  28.928 1.00 22.19 ? 680  ILE A CD1 1 
ATOM   5445 N N   . THR A 1 681 ? -26.541 -11.921 27.545 1.00 14.66 ? 681  THR A N   1 
ATOM   5446 C CA  . THR A 1 681 ? -26.988 -13.329 27.488 1.00 15.42 ? 681  THR A CA  1 
ATOM   5447 C C   . THR A 1 681 ? -26.673 -13.921 26.118 1.00 14.81 ? 681  THR A C   1 
ATOM   5448 O O   . THR A 1 681 ? -27.502 -13.912 25.199 1.00 15.57 ? 681  THR A O   1 
ATOM   5449 C CB  . THR A 1 681 ? -28.498 -13.462 27.815 1.00 15.99 ? 681  THR A CB  1 
ATOM   5450 O OG1 . THR A 1 681 ? -28.768 -12.839 29.066 1.00 18.43 ? 681  THR A OG1 1 
ATOM   5451 C CG2 . THR A 1 681 ? -28.936 -14.946 27.921 1.00 17.20 ? 681  THR A CG2 1 
ATOM   5452 N N   . PRO A 1 682 ? -25.465 -14.493 25.973 1.00 13.18 ? 682  PRO A N   1 
ATOM   5453 C CA  . PRO A 1 682 ? -25.087 -15.114 24.737 1.00 13.51 ? 682  PRO A CA  1 
ATOM   5454 C C   . PRO A 1 682 ? -25.610 -16.526 24.491 1.00 14.07 ? 682  PRO A C   1 
ATOM   5455 O O   . PRO A 1 682 ? -25.843 -17.299 25.424 1.00 14.71 ? 682  PRO A O   1 
ATOM   5456 C CB  . PRO A 1 682 ? -23.550 -15.228 24.863 1.00 13.30 ? 682  PRO A CB  1 
ATOM   5457 C CG  . PRO A 1 682 ? -23.342 -15.460 26.344 1.00 12.25 ? 682  PRO A CG  1 
ATOM   5458 C CD  . PRO A 1 682 ? -24.389 -14.537 26.988 1.00 13.37 ? 682  PRO A CD  1 
ATOM   5459 N N   . VAL A 1 683 ? -25.731 -16.871 23.211 1.00 15.84 ? 683  VAL A N   1 
ATOM   5460 C CA  . VAL A 1 683 ? -25.924 -18.264 22.818 1.00 16.78 ? 683  VAL A CA  1 
ATOM   5461 C C   . VAL A 1 683 ? -24.520 -18.879 22.835 1.00 18.01 ? 683  VAL A C   1 
ATOM   5462 O O   . VAL A 1 683 ? -23.586 -18.319 22.234 1.00 19.00 ? 683  VAL A O   1 
ATOM   5463 C CB  . VAL A 1 683 ? -26.590 -18.366 21.414 1.00 16.29 ? 683  VAL A CB  1 
ATOM   5464 C CG1 . VAL A 1 683 ? -26.537 -19.831 20.863 1.00 17.37 ? 683  VAL A CG1 1 
ATOM   5465 C CG2 . VAL A 1 683 ? -28.038 -17.866 21.492 1.00 16.81 ? 683  VAL A CG2 1 
ATOM   5466 N N   . LEU A 1 684 ? -24.371 -19.985 23.556 1.00 17.60 ? 684  LEU A N   1 
ATOM   5467 C CA  . LEU A 1 684 ? -23.049 -20.597 23.772 1.00 20.14 ? 684  LEU A CA  1 
ATOM   5468 C C   . LEU A 1 684 ? -22.992 -22.064 23.332 1.00 20.91 ? 684  LEU A C   1 
ATOM   5469 O O   . LEU A 1 684 ? -22.025 -22.770 23.642 1.00 20.90 ? 684  LEU A O   1 
ATOM   5470 C CB  . LEU A 1 684 ? -22.685 -20.506 25.265 1.00 19.56 ? 684  LEU A CB  1 
ATOM   5471 C CG  . LEU A 1 684 ? -22.647 -19.090 25.815 1.00 20.01 ? 684  LEU A CG  1 
ATOM   5472 C CD1 . LEU A 1 684 ? -22.522 -19.118 27.342 1.00 19.79 ? 684  LEU A CD1 1 
ATOM   5473 C CD2 . LEU A 1 684 ? -21.451 -18.393 25.190 1.00 19.16 ? 684  LEU A CD2 1 
ATOM   5474 N N   . ASP A 1 685 ? -24.033 -22.518 22.633 1.00 22.03 ? 685  ASP A N   1 
ATOM   5475 C CA  . ASP A 1 685 ? -24.166 -23.931 22.243 1.00 22.82 ? 685  ASP A CA  1 
ATOM   5476 C C   . ASP A 1 685 ? -24.398 -24.067 20.744 1.00 22.84 ? 685  ASP A C   1 
ATOM   5477 O O   . ASP A 1 685 ? -25.226 -23.363 20.148 1.00 21.08 ? 685  ASP A O   1 
ATOM   5478 C CB  . ASP A 1 685 ? -25.294 -24.632 23.014 1.00 24.66 ? 685  ASP A CB  1 
ATOM   5479 C CG  . ASP A 1 685 ? -24.988 -24.790 24.491 1.00 28.31 ? 685  ASP A CG  1 
ATOM   5480 O OD1 . ASP A 1 685 ? -24.114 -25.603 24.857 1.00 35.15 ? 685  ASP A OD1 1 
ATOM   5481 O OD2 . ASP A 1 685 ? -25.631 -24.099 25.295 1.00 35.71 ? 685  ASP A OD2 1 
ATOM   5482 N N   . GLU A 1 686 ? -23.628 -24.971 20.152 1.00 23.01 ? 686  GLU A N   1 
ATOM   5483 C CA  . GLU A 1 686 ? -23.658 -25.252 18.732 1.00 24.46 ? 686  GLU A CA  1 
ATOM   5484 C C   . GLU A 1 686 ? -25.060 -25.652 18.302 1.00 24.80 ? 686  GLU A C   1 
ATOM   5485 O O   . GLU A 1 686 ? -25.680 -26.525 18.932 1.00 24.51 ? 686  GLU A O   1 
ATOM   5486 C CB  . GLU A 1 686 ? -22.678 -26.375 18.397 1.00 23.61 ? 686  GLU A CB  1 
ATOM   5487 C CG  . GLU A 1 686 ? -22.436 -26.522 16.904 1.00 25.73 ? 686  GLU A CG  1 
ATOM   5488 C CD  . GLU A 1 686 ? -21.480 -27.659 16.561 1.00 26.35 ? 686  GLU A CD  1 
ATOM   5489 O OE1 . GLU A 1 686 ? -20.781 -28.140 17.462 1.00 29.12 ? 686  GLU A OE1 1 
ATOM   5490 O OE2 . GLU A 1 686 ? -21.460 -28.092 15.384 1.00 31.71 ? 686  GLU A OE2 1 
ATOM   5491 N N   . GLY A 1 687 ? -25.538 -24.999 17.240 1.00 24.46 ? 687  GLY A N   1 
ATOM   5492 C CA  . GLY A 1 687 ? -26.858 -25.267 16.661 1.00 25.37 ? 687  GLY A CA  1 
ATOM   5493 C C   . GLY A 1 687 ? -27.987 -24.505 17.314 1.00 25.31 ? 687  GLY A C   1 
ATOM   5494 O O   . GLY A 1 687 ? -29.100 -24.467 16.783 1.00 25.86 ? 687  GLY A O   1 
ATOM   5495 N N   . ALA A 1 688 ? -27.712 -23.881 18.462 1.00 24.19 ? 688  ALA A N   1 
ATOM   5496 C CA  . ALA A 1 688 ? -28.782 -23.265 19.264 1.00 23.62 ? 688  ALA A CA  1 
ATOM   5497 C C   . ALA A 1 688 ? -29.281 -21.914 18.752 1.00 23.66 ? 688  ALA A C   1 
ATOM   5498 O O   . ALA A 1 688 ? -28.495 -21.089 18.279 1.00 22.13 ? 688  ALA A O   1 
ATOM   5499 C CB  . ALA A 1 688 ? -28.377 -23.178 20.754 1.00 23.32 ? 688  ALA A CB  1 
ATOM   5500 N N   . GLU A 1 689 ? -30.603 -21.722 18.817 1.00 24.35 ? 689  GLU A N   1 
ATOM   5501 C CA  . GLU A 1 689 ? -31.241 -20.433 18.520 1.00 26.60 ? 689  GLU A CA  1 
ATOM   5502 C C   . GLU A 1 689 ? -32.070 -19.993 19.741 1.00 25.88 ? 689  GLU A C   1 
ATOM   5503 O O   . GLU A 1 689 ? -33.022 -19.197 19.662 1.00 24.59 ? 689  GLU A O   1 
ATOM   5504 C CB  . GLU A 1 689 ? -32.054 -20.475 17.205 1.00 26.71 ? 689  GLU A CB  1 
ATOM   5505 C CG  . GLU A 1 689 ? -31.185 -20.368 15.926 1.00 29.84 ? 689  GLU A CG  1 
ATOM   5506 C CD  . GLU A 1 689 ? -31.954 -19.941 14.665 1.00 31.65 ? 689  GLU A CD  1 
ATOM   5507 O OE1 . GLU A 1 689 ? -33.008 -20.567 14.400 1.00 36.36 ? 689  GLU A OE1 1 
ATOM   5508 O OE2 . GLU A 1 689 ? -31.501 -18.994 13.935 1.00 37.24 ? 689  GLU A OE2 1 
ATOM   5509 N N   . LYS A 1 690 ? -31.617 -20.480 20.884 1.00 26.45 ? 690  LYS A N   1 
ATOM   5510 C CA  . LYS A 1 690 ? -32.230 -20.254 22.174 1.00 28.56 ? 690  LYS A CA  1 
ATOM   5511 C C   . LYS A 1 690 ? -31.126 -20.329 23.197 1.00 28.37 ? 690  LYS A C   1 
ATOM   5512 O O   . LYS A 1 690 ? -30.067 -20.898 22.935 1.00 29.24 ? 690  LYS A O   1 
ATOM   5513 C CB  . LYS A 1 690 ? -33.243 -21.357 22.503 1.00 28.92 ? 690  LYS A CB  1 
ATOM   5514 C CG  . LYS A 1 690 ? -34.583 -21.201 21.818 1.00 33.19 ? 690  LYS A CG  1 
ATOM   5515 C CD  . LYS A 1 690 ? -35.366 -22.494 21.880 1.00 35.94 ? 690  LYS A CD  1 
ATOM   5516 C CE  . LYS A 1 690 ? -36.645 -22.412 21.074 1.00 40.98 ? 690  LYS A CE  1 
ATOM   5517 N NZ  . LYS A 1 690 ? -37.484 -23.638 21.323 1.00 43.23 ? 690  LYS A NZ  1 
ATOM   5518 N N   . VAL A 1 691 ? -31.360 -19.745 24.362 1.00 28.47 ? 691  VAL A N   1 
ATOM   5519 C CA  . VAL A 1 691 ? -30.470 -19.973 25.489 1.00 29.28 ? 691  VAL A CA  1 
ATOM   5520 C C   . VAL A 1 691 ? -31.306 -20.039 26.764 1.00 28.12 ? 691  VAL A C   1 
ATOM   5521 O O   . VAL A 1 691 ? -32.190 -19.213 26.986 1.00 26.97 ? 691  VAL A O   1 
ATOM   5522 C CB  . VAL A 1 691 ? -29.354 -18.908 25.576 1.00 28.84 ? 691  VAL A CB  1 
ATOM   5523 C CG1 . VAL A 1 691 ? -29.877 -17.626 26.156 1.00 30.81 ? 691  VAL A CG1 1 
ATOM   5524 C CG2 . VAL A 1 691 ? -28.200 -19.405 26.444 1.00 33.77 ? 691  VAL A CG2 1 
ATOM   5525 N N   . MET A 1 692 ? -31.047 -21.069 27.555 1.00 28.18 ? 692  MET A N   1 
ATOM   5526 C CA  . MET A 1 692 ? -31.589 -21.163 28.899 1.00 28.53 ? 692  MET A CA  1 
ATOM   5527 C C   . MET A 1 692 ? -30.799 -20.102 29.697 1.00 27.35 ? 692  MET A C   1 
ATOM   5528 O O   . MET A 1 692 ? -29.584 -20.151 29.770 1.00 27.08 ? 692  MET A O   1 
ATOM   5529 C CB  . MET A 1 692 ? -31.401 -22.579 29.464 1.00 30.01 ? 692  MET A CB  1 
ATOM   5530 C CG  . MET A 1 692 ? -32.392 -23.621 28.899 1.00 34.13 ? 692  MET A CG  1 
ATOM   5531 S SD  . MET A 1 692 ? -34.140 -23.126 29.103 1.00 43.02 ? 692  MET A SD  1 
ATOM   5532 C CE  . MET A 1 692 ? -35.019 -24.678 28.794 1.00 37.86 ? 692  MET A CE  1 
ATOM   5533 N N   . ALA A 1 693 ? -31.500 -19.133 30.248 1.00 25.71 ? 693  ALA A N   1 
ATOM   5534 C CA  . ALA A 1 693 ? -30.850 -17.996 30.903 1.00 24.78 ? 693  ALA A CA  1 
ATOM   5535 C C   . ALA A 1 693 ? -31.505 -17.717 32.231 1.00 23.46 ? 693  ALA A C   1 
ATOM   5536 O O   . ALA A 1 693 ? -32.649 -18.099 32.447 1.00 24.50 ? 693  ALA A O   1 
ATOM   5537 C CB  . ALA A 1 693 ? -30.961 -16.774 30.033 1.00 24.14 ? 693  ALA A CB  1 
ATOM   5538 N N   . TYR A 1 694 ? -30.795 -17.016 33.107 1.00 21.98 ? 694  TYR A N   1 
ATOM   5539 C CA  . TYR A 1 694 ? -31.415 -16.499 34.314 1.00 20.11 ? 694  TYR A CA  1 
ATOM   5540 C C   . TYR A 1 694 ? -31.730 -15.003 34.191 1.00 19.73 ? 694  TYR A C   1 
ATOM   5541 O O   . TYR A 1 694 ? -30.893 -14.165 33.765 1.00 18.84 ? 694  TYR A O   1 
ATOM   5542 C CB  . TYR A 1 694 ? -30.600 -16.860 35.585 1.00 21.14 ? 694  TYR A CB  1 
ATOM   5543 C CG  . TYR A 1 694 ? -31.399 -16.622 36.841 1.00 20.17 ? 694  TYR A CG  1 
ATOM   5544 C CD1 . TYR A 1 694 ? -32.488 -17.452 37.163 1.00 21.59 ? 694  TYR A CD1 1 
ATOM   5545 C CD2 . TYR A 1 694 ? -31.109 -15.555 37.685 1.00 20.01 ? 694  TYR A CD2 1 
ATOM   5546 C CE1 . TYR A 1 694 ? -33.247 -17.219 38.296 1.00 20.36 ? 694  TYR A CE1 1 
ATOM   5547 C CE2 . TYR A 1 694 ? -31.850 -15.319 38.831 1.00 19.19 ? 694  TYR A CE2 1 
ATOM   5548 C CZ  . TYR A 1 694 ? -32.921 -16.172 39.125 1.00 21.56 ? 694  TYR A CZ  1 
ATOM   5549 O OH  . TYR A 1 694 ? -33.679 -15.945 40.229 1.00 20.21 ? 694  TYR A OH  1 
ATOM   5550 N N   . VAL A 1 695 ? -32.974 -14.670 34.500 1.00 16.89 ? 695  VAL A N   1 
ATOM   5551 C CA  . VAL A 1 695 ? -33.386 -13.268 34.595 1.00 17.06 ? 695  VAL A CA  1 
ATOM   5552 C C   . VAL A 1 695 ? -33.501 -12.863 36.077 1.00 16.97 ? 695  VAL A C   1 
ATOM   5553 O O   . VAL A 1 695 ? -34.432 -13.283 36.797 1.00 16.28 ? 695  VAL A O   1 
ATOM   5554 C CB  . VAL A 1 695 ? -34.738 -13.042 33.870 1.00 17.05 ? 695  VAL A CB  1 
ATOM   5555 C CG1 . VAL A 1 695 ? -35.168 -11.563 33.994 1.00 14.47 ? 695  VAL A CG1 1 
ATOM   5556 C CG2 . VAL A 1 695 ? -34.644 -13.494 32.396 1.00 18.86 ? 695  VAL A CG2 1 
ATOM   5557 N N   . PRO A 1 696 ? -32.558 -12.032 36.557 1.00 16.06 ? 696  PRO A N   1 
ATOM   5558 C CA  . PRO A 1 696 ? -32.535 -11.577 37.947 1.00 15.84 ? 696  PRO A CA  1 
ATOM   5559 C C   . PRO A 1 696 ? -33.759 -10.757 38.413 1.00 16.39 ? 696  PRO A C   1 
ATOM   5560 O O   . PRO A 1 696 ? -34.608 -10.349 37.594 1.00 17.45 ? 696  PRO A O   1 
ATOM   5561 C CB  . PRO A 1 696 ? -31.269 -10.710 37.992 1.00 14.93 ? 696  PRO A CB  1 
ATOM   5562 C CG  . PRO A 1 696 ? -30.394 -11.303 36.873 1.00 15.60 ? 696  PRO A CG  1 
ATOM   5563 C CD  . PRO A 1 696 ? -31.391 -11.517 35.795 1.00 15.48 ? 696  PRO A CD  1 
ATOM   5564 N N   . ASP A 1 697 ? -33.820 -10.527 39.726 1.00 16.27 ? 697  ASP A N   1 
ATOM   5565 C CA  . ASP A 1 697 ? -34.915 -9.798  40.400 1.00 16.68 ? 697  ASP A CA  1 
ATOM   5566 C C   . ASP A 1 697 ? -34.809 -8.293  40.153 1.00 16.53 ? 697  ASP A C   1 
ATOM   5567 O O   . ASP A 1 697 ? -34.516 -7.508  41.052 1.00 17.12 ? 697  ASP A O   1 
ATOM   5568 C CB  . ASP A 1 697 ? -34.903 -10.140 41.892 1.00 16.97 ? 697  ASP A CB  1 
ATOM   5569 C CG  . ASP A 1 697 ? -36.115 -9.626  42.649 1.00 20.24 ? 697  ASP A CG  1 
ATOM   5570 O OD1 . ASP A 1 697 ? -37.091 -9.116  42.033 1.00 20.74 ? 697  ASP A OD1 1 
ATOM   5571 O OD2 . ASP A 1 697 ? -36.068 -9.735  43.897 1.00 21.21 ? 697  ASP A OD2 1 
ATOM   5572 N N   . ALA A 1 698 ? -35.092 -7.890  38.916 1.00 16.53 ? 698  ALA A N   1 
ATOM   5573 C CA  . ALA A 1 698 ? -35.175 -6.470  38.570 1.00 16.33 ? 698  ALA A CA  1 
ATOM   5574 C C   . ALA A 1 698 ? -36.196 -6.324  37.474 1.00 15.97 ? 698  ALA A C   1 
ATOM   5575 O O   . ALA A 1 698 ? -36.587 -7.336  36.861 1.00 15.92 ? 698  ALA A O   1 
ATOM   5576 C CB  . ALA A 1 698 ? -33.795 -5.965  38.059 1.00 15.53 ? 698  ALA A CB  1 
ATOM   5577 N N   . VAL A 1 699 ? -36.584 -5.079  37.191 1.00 15.56 ? 699  VAL A N   1 
ATOM   5578 C CA  . VAL A 1 699 ? -37.282 -4.768  35.928 1.00 16.56 ? 699  VAL A CA  1 
ATOM   5579 C C   . VAL A 1 699 ? -36.241 -4.842  34.811 1.00 17.14 ? 699  VAL A C   1 
ATOM   5580 O O   . VAL A 1 699 ? -35.113 -4.336  35.007 1.00 16.83 ? 699  VAL A O   1 
ATOM   5581 C CB  . VAL A 1 699 ? -37.872 -3.346  35.941 1.00 16.78 ? 699  VAL A CB  1 
ATOM   5582 C CG1 . VAL A 1 699 ? -38.475 -3.012  34.566 1.00 18.73 ? 699  VAL A CG1 1 
ATOM   5583 C CG2 . VAL A 1 699 ? -38.916 -3.200  37.050 1.00 19.18 ? 699  VAL A CG2 1 
ATOM   5584 N N   . TRP A 1 700 ? -36.550 -5.514  33.698 1.00 15.96 ? 700  TRP A N   1 
ATOM   5585 C CA  . TRP A 1 700 ? -35.569 -5.541  32.575 1.00 17.23 ? 700  TRP A CA  1 
ATOM   5586 C C   . TRP A 1 700 ? -36.207 -5.089  31.269 1.00 17.38 ? 700  TRP A C   1 
ATOM   5587 O O   . TRP A 1 700 ? -37.384 -5.432  30.985 1.00 17.72 ? 700  TRP A O   1 
ATOM   5588 C CB  . TRP A 1 700 ? -34.954 -6.932  32.361 1.00 16.28 ? 700  TRP A CB  1 
ATOM   5589 C CG  . TRP A 1 700 ? -34.179 -7.460  33.515 1.00 17.34 ? 700  TRP A CG  1 
ATOM   5590 C CD1 . TRP A 1 700 ? -34.627 -8.267  34.518 1.00 16.30 ? 700  TRP A CD1 1 
ATOM   5591 C CD2 . TRP A 1 700 ? -32.792 -7.183  33.801 1.00 15.04 ? 700  TRP A CD2 1 
ATOM   5592 N NE1 . TRP A 1 700 ? -33.599 -8.504  35.426 1.00 16.65 ? 700  TRP A NE1 1 
ATOM   5593 C CE2 . TRP A 1 700 ? -32.475 -7.837  35.012 1.00 17.60 ? 700  TRP A CE2 1 
ATOM   5594 C CE3 . TRP A 1 700 ? -31.815 -6.402  33.167 1.00 15.10 ? 700  TRP A CE3 1 
ATOM   5595 C CZ2 . TRP A 1 700 ? -31.186 -7.783  35.590 1.00 16.50 ? 700  TRP A CZ2 1 
ATOM   5596 C CZ3 . TRP A 1 700 ? -30.529 -6.326  33.743 1.00 15.60 ? 700  TRP A CZ3 1 
ATOM   5597 C CH2 . TRP A 1 700 ? -30.241 -7.003  34.954 1.00 16.99 ? 700  TRP A CH2 1 
ATOM   5598 N N   . TYR A 1 701 ? -35.427 -4.373  30.450 1.00 15.77 ? 701  TYR A N   1 
ATOM   5599 C CA  . TYR A 1 701 ? -35.876 -3.920  29.131 1.00 15.26 ? 701  TYR A CA  1 
ATOM   5600 C C   . TYR A 1 701 ? -35.008 -4.437  28.002 1.00 16.91 ? 701  TYR A C   1 
ATOM   5601 O O   . TYR A 1 701 ? -33.741 -4.361  28.047 1.00 14.50 ? 701  TYR A O   1 
ATOM   5602 C CB  . TYR A 1 701 ? -35.883 -2.383  29.090 1.00 15.44 ? 701  TYR A CB  1 
ATOM   5603 C CG  . TYR A 1 701 ? -36.698 -1.694  30.164 1.00 15.19 ? 701  TYR A CG  1 
ATOM   5604 C CD1 . TYR A 1 701 ? -38.060 -1.429  29.960 1.00 17.04 ? 701  TYR A CD1 1 
ATOM   5605 C CD2 . TYR A 1 701 ? -36.112 -1.245  31.351 1.00 14.84 ? 701  TYR A CD2 1 
ATOM   5606 C CE1 . TYR A 1 701 ? -38.823 -0.781  30.931 1.00 16.32 ? 701  TYR A CE1 1 
ATOM   5607 C CE2 . TYR A 1 701 ? -36.892 -0.587  32.350 1.00 15.77 ? 701  TYR A CE2 1 
ATOM   5608 C CZ  . TYR A 1 701 ? -38.260 -0.365  32.089 1.00 16.13 ? 701  TYR A CZ  1 
ATOM   5609 O OH  . TYR A 1 701 ? -39.042 0.271   33.018 1.00 15.67 ? 701  TYR A OH  1 
ATOM   5610 N N   . ASP A 1 702 ? -35.643 -4.968  26.974 1.00 16.49 ? 702  ASP A N   1 
ATOM   5611 C CA  . ASP A 1 702 ? -34.906 -5.281  25.742 1.00 17.37 ? 702  ASP A CA  1 
ATOM   5612 C C   . ASP A 1 702 ? -34.131 -4.047  25.208 1.00 17.61 ? 702  ASP A C   1 
ATOM   5613 O O   . ASP A 1 702 ? -34.679 -2.956  24.997 1.00 16.40 ? 702  ASP A O   1 
ATOM   5614 C CB  . ASP A 1 702 ? -35.852 -5.873  24.709 1.00 18.78 ? 702  ASP A CB  1 
ATOM   5615 C CG  . ASP A 1 702 ? -35.162 -6.290  23.465 1.00 21.55 ? 702  ASP A CG  1 
ATOM   5616 O OD1 . ASP A 1 702 ? -34.875 -7.488  23.358 1.00 29.54 ? 702  ASP A OD1 1 
ATOM   5617 O OD2 . ASP A 1 702 ? -34.887 -5.428  22.605 1.00 24.47 ? 702  ASP A OD2 1 
ATOM   5618 N N   . TYR A 1 703 ? -32.818 -4.209  25.030 1.00 17.75 ? 703  TYR A N   1 
ATOM   5619 C CA  . TYR A 1 703 ? -31.994 -3.073  24.660 1.00 19.00 ? 703  TYR A CA  1 
ATOM   5620 C C   . TYR A 1 703 ? -32.469 -2.435  23.350 1.00 19.44 ? 703  TYR A C   1 
ATOM   5621 O O   . TYR A 1 703 ? -32.530 -1.209  23.258 1.00 21.60 ? 703  TYR A O   1 
ATOM   5622 C CB  . TYR A 1 703 ? -30.493 -3.472  24.544 1.00 18.67 ? 703  TYR A CB  1 
ATOM   5623 C CG  . TYR A 1 703 ? -29.651 -2.313  24.027 1.00 21.31 ? 703  TYR A CG  1 
ATOM   5624 C CD1 . TYR A 1 703 ? -29.166 -1.347  24.892 1.00 20.07 ? 703  TYR A CD1 1 
ATOM   5625 C CD2 . TYR A 1 703 ? -29.394 -2.164  22.658 1.00 21.65 ? 703  TYR A CD2 1 
ATOM   5626 C CE1 . TYR A 1 703 ? -28.426 -0.253  24.417 1.00 20.33 ? 703  TYR A CE1 1 
ATOM   5627 C CE2 . TYR A 1 703 ? -28.672 -1.077  22.164 1.00 21.58 ? 703  TYR A CE2 1 
ATOM   5628 C CZ  . TYR A 1 703 ? -28.191 -0.128  23.059 1.00 21.39 ? 703  TYR A CZ  1 
ATOM   5629 O OH  . TYR A 1 703 ? -27.481 0.957   22.597 1.00 23.66 ? 703  TYR A OH  1 
ATOM   5630 N N   . GLU A 1 704 ? -32.766 -3.248  22.342 1.00 19.97 ? 704  GLU A N   1 
ATOM   5631 C CA  . GLU A 1 704 ? -33.005 -2.709  21.010 1.00 21.13 ? 704  GLU A CA  1 
ATOM   5632 C C   . GLU A 1 704 ? -34.394 -2.115  20.861 1.00 20.80 ? 704  GLU A C   1 
ATOM   5633 O O   . GLU A 1 704 ? -34.539 -1.024  20.337 1.00 21.73 ? 704  GLU A O   1 
ATOM   5634 C CB  . GLU A 1 704 ? -32.747 -3.750  19.944 1.00 21.92 ? 704  GLU A CB  1 
ATOM   5635 C CG  . GLU A 1 704 ? -31.209 -3.949  19.761 1.00 26.46 ? 704  GLU A CG  1 
ATOM   5636 C CD  . GLU A 1 704 ? -30.851 -4.471  18.419 1.00 29.68 ? 704  GLU A CD  1 
ATOM   5637 O OE1 . GLU A 1 704 ? -31.037 -3.729  17.409 1.00 32.82 ? 704  GLU A OE1 1 
ATOM   5638 O OE2 . GLU A 1 704 ? -30.383 -5.624  18.373 1.00 33.91 ? 704  GLU A OE2 1 
ATOM   5639 N N   . THR A 1 705 ? -35.391 -2.811  21.392 1.00 21.05 ? 705  THR A N   1 
ATOM   5640 C CA  . THR A 1 705 ? -36.792 -2.312  21.316 1.00 20.60 ? 705  THR A CA  1 
ATOM   5641 C C   . THR A 1 705 ? -37.178 -1.393  22.477 1.00 20.67 ? 705  THR A C   1 
ATOM   5642 O O   . THR A 1 705 ? -38.092 -0.544  22.349 1.00 19.37 ? 705  THR A O   1 
ATOM   5643 C CB  . THR A 1 705 ? -37.789 -3.496  21.246 1.00 21.02 ? 705  THR A CB  1 
ATOM   5644 O OG1 . THR A 1 705 ? -37.782 -4.193  22.479 1.00 21.43 ? 705  THR A OG1 1 
ATOM   5645 C CG2 . THR A 1 705 ? -37.410 -4.499  20.188 1.00 23.55 ? 705  THR A CG2 1 
ATOM   5646 N N   . GLY A 1 706 ? -36.522 -1.578  23.632 1.00 17.88 ? 706  GLY A N   1 
ATOM   5647 C CA  . GLY A 1 706 ? -36.913 -0.910  24.841 1.00 18.16 ? 706  GLY A CA  1 
ATOM   5648 C C   . GLY A 1 706 ? -38.147 -1.485  25.553 1.00 17.43 ? 706  GLY A C   1 
ATOM   5649 O O   . GLY A 1 706 ? -38.548 -0.949  26.582 1.00 16.64 ? 706  GLY A O   1 
ATOM   5650 N N   . SER A 1 707 ? -38.682 -2.603  25.065 1.00 18.64 ? 707  SER A N   1 
ATOM   5651 C CA  . SER A 1 707 ? -39.856 -3.211  25.711 1.00 20.29 ? 707  SER A CA  1 
ATOM   5652 C C   . SER A 1 707 ? -39.507 -3.888  27.017 1.00 20.16 ? 707  SER A C   1 
ATOM   5653 O O   . SER A 1 707 ? -38.472 -4.557  27.135 1.00 18.35 ? 707  SER A O   1 
ATOM   5654 C CB  . SER A 1 707 ? -40.613 -4.162  24.782 1.00 20.96 ? 707  SER A CB  1 
ATOM   5655 O OG  . SER A 1 707 ? -39.770 -5.229  24.386 1.00 28.76 ? 707  SER A OG  1 
ATOM   5656 N N   . GLN A 1 708 ? -40.363 -3.688  28.016 1.00 20.05 ? 708  GLN A N   1 
ATOM   5657 C CA  . GLN A 1 708 ? -40.155 -4.339  29.308 1.00 21.46 ? 708  GLN A CA  1 
ATOM   5658 C C   . GLN A 1 708 ? -40.437 -5.843  29.178 1.00 22.45 ? 708  GLN A C   1 
ATOM   5659 O O   . GLN A 1 708 ? -41.532 -6.246  28.722 1.00 23.36 ? 708  GLN A O   1 
ATOM   5660 C CB  . GLN A 1 708 ? -41.067 -3.720  30.365 1.00 21.40 ? 708  GLN A CB  1 
ATOM   5661 C CG  . GLN A 1 708 ? -40.742 -4.207  31.792 1.00 20.28 ? 708  GLN A CG  1 
ATOM   5662 C CD  . GLN A 1 708 ? -41.662 -3.624  32.850 1.00 23.16 ? 708  GLN A CD  1 
ATOM   5663 O OE1 . GLN A 1 708 ? -42.250 -2.568  32.666 1.00 23.96 ? 708  GLN A OE1 1 
ATOM   5664 N NE2 . GLN A 1 708 ? -41.746 -4.306  33.999 1.00 25.78 ? 708  GLN A NE2 1 
ATOM   5665 N N   . VAL A 1 709 ? -39.497 -6.688  29.582 1.00 20.50 ? 709  VAL A N   1 
ATOM   5666 C CA  . VAL A 1 709 ? -39.752 -8.123  29.545 1.00 21.73 ? 709  VAL A CA  1 
ATOM   5667 C C   . VAL A 1 709 ? -40.724 -8.517  30.677 1.00 21.69 ? 709  VAL A C   1 
ATOM   5668 O O   . VAL A 1 709 ? -40.857 -7.814  31.689 1.00 20.29 ? 709  VAL A O   1 
ATOM   5669 C CB  . VAL A 1 709 ? -38.470 -8.990  29.549 1.00 22.03 ? 709  VAL A CB  1 
ATOM   5670 C CG1 . VAL A 1 709 ? -37.540 -8.510  28.468 1.00 22.78 ? 709  VAL A CG1 1 
ATOM   5671 C CG2 . VAL A 1 709 ? -37.766 -8.961  30.913 1.00 22.51 ? 709  VAL A CG2 1 
ATOM   5672 N N   . ARG A 1 710 ? -41.436 -9.617  30.488 1.00 23.38 ? 710  ARG A N   1 
ATOM   5673 C CA  . ARG A 1 710 ? -42.333 -10.039 31.563 1.00 26.35 ? 710  ARG A CA  1 
ATOM   5674 C C   . ARG A 1 710 ? -41.560 -10.890 32.589 1.00 26.71 ? 710  ARG A C   1 
ATOM   5675 O O   . ARG A 1 710 ? -41.964 -11.006 33.746 1.00 28.90 ? 710  ARG A O   1 
ATOM   5676 C CB  . ARG A 1 710 ? -43.613 -10.684 31.008 1.00 28.53 ? 710  ARG A CB  1 
ATOM   5677 C CG  . ARG A 1 710 ? -44.547 -9.632  30.331 1.00 32.77 ? 710  ARG A CG  1 
ATOM   5678 C CD  . ARG A 1 710 ? -44.731 -8.370  31.225 1.00 39.33 ? 710  ARG A CD  1 
ATOM   5679 N NE  . ARG A 1 710 ? -45.596 -7.325  30.656 1.00 41.04 ? 710  ARG A NE  1 
ATOM   5680 C CZ  . ARG A 1 710 ? -45.691 -6.085  31.143 1.00 46.12 ? 710  ARG A CZ  1 
ATOM   5681 N NH1 . ARG A 1 710 ? -44.979 -5.718  32.212 1.00 46.56 ? 710  ARG A NH1 1 
ATOM   5682 N NH2 . ARG A 1 710 ? -46.504 -5.205  30.566 1.00 46.70 ? 710  ARG A NH2 1 
ATOM   5683 N N   . TRP A 1 711 ? -40.400 -11.396 32.193 1.00 25.48 ? 711  TRP A N   1 
ATOM   5684 C CA  . TRP A 1 711 ? -39.584 -12.195 33.110 1.00 25.18 ? 711  TRP A CA  1 
ATOM   5685 C C   . TRP A 1 711 ? -39.037 -11.403 34.292 1.00 23.64 ? 711  TRP A C   1 
ATOM   5686 O O   . TRP A 1 711 ? -38.521 -10.282 34.124 1.00 23.61 ? 711  TRP A O   1 
ATOM   5687 C CB  . TRP A 1 711 ? -38.419 -12.848 32.385 1.00 25.95 ? 711  TRP A CB  1 
ATOM   5688 C CG  . TRP A 1 711 ? -38.708 -13.458 31.043 1.00 27.89 ? 711  TRP A CG  1 
ATOM   5689 C CD1 . TRP A 1 711 ? -39.694 -14.360 30.724 1.00 29.12 ? 711  TRP A CD1 1 
ATOM   5690 C CD2 . TRP A 1 711 ? -37.949 -13.248 29.850 1.00 27.87 ? 711  TRP A CD2 1 
ATOM   5691 N NE1 . TRP A 1 711 ? -39.598 -14.704 29.392 1.00 29.75 ? 711  TRP A NE1 1 
ATOM   5692 C CE2 . TRP A 1 711 ? -38.541 -14.030 28.834 1.00 29.21 ? 711  TRP A CE2 1 
ATOM   5693 C CE3 . TRP A 1 711 ? -36.845 -12.446 29.533 1.00 27.99 ? 711  TRP A CE3 1 
ATOM   5694 C CZ2 . TRP A 1 711 ? -38.053 -14.043 27.523 1.00 29.26 ? 711  TRP A CZ2 1 
ATOM   5695 C CZ3 . TRP A 1 711 ? -36.356 -12.465 28.230 1.00 29.69 ? 711  TRP A CZ3 1 
ATOM   5696 C CH2 . TRP A 1 711 ? -36.962 -13.255 27.241 1.00 29.17 ? 711  TRP A CH2 1 
ATOM   5697 N N   . ARG A 1 712 ? -39.110 -12.000 35.481 1.00 22.69 ? 712  ARG A N   1 
ATOM   5698 C CA  . ARG A 1 712 ? -38.423 -11.457 36.657 1.00 21.59 ? 712  ARG A CA  1 
ATOM   5699 C C   . ARG A 1 712 ? -38.074 -12.540 37.693 1.00 21.46 ? 712  ARG A C   1 
ATOM   5700 O O   . ARG A 1 712 ? -38.927 -13.353 38.106 1.00 19.17 ? 712  ARG A O   1 
ATOM   5701 C CB  . ARG A 1 712 ? -39.209 -10.333 37.303 1.00 22.33 ? 712  ARG A CB  1 
ATOM   5702 C CG  . ARG A 1 712 ? -38.486 -9.691  38.467 1.00 20.98 ? 712  ARG A CG  1 
ATOM   5703 C CD  . ARG A 1 712 ? -39.189 -8.432  38.913 1.00 23.87 ? 712  ARG A CD  1 
ATOM   5704 N NE  . ARG A 1 712 ? -38.448 -7.811  40.001 1.00 26.16 ? 712  ARG A NE  1 
ATOM   5705 C CZ  . ARG A 1 712 ? -38.559 -6.549  40.372 1.00 27.02 ? 712  ARG A CZ  1 
ATOM   5706 N NH1 . ARG A 1 712 ? -39.406 -5.739  39.756 1.00 28.93 ? 712  ARG A NH1 1 
ATOM   5707 N NH2 . ARG A 1 712 ? -37.824 -6.108  41.383 1.00 28.78 ? 712  ARG A NH2 1 
ATOM   5708 N N   . LYS A 1 713 ? -36.802 -12.556 38.098 1.00 19.85 ? 713  LYS A N   1 
ATOM   5709 C CA  . LYS A 1 713 ? -36.327 -13.544 39.066 1.00 19.72 ? 713  LYS A CA  1 
ATOM   5710 C C   . LYS A 1 713 ? -36.677 -14.995 38.666 1.00 20.43 ? 713  LYS A C   1 
ATOM   5711 O O   . LYS A 1 713 ? -37.352 -15.730 39.419 1.00 19.89 ? 713  LYS A O   1 
ATOM   5712 C CB  . LYS A 1 713 ? -36.846 -13.206 40.477 1.00 19.48 ? 713  LYS A CB  1 
ATOM   5713 C CG  . LYS A 1 713 ? -35.991 -13.803 41.604 1.00 19.84 ? 713  LYS A CG  1 
ATOM   5714 C CD  . LYS A 1 713 ? -36.521 -13.415 42.987 1.00 17.40 ? 713  LYS A CD  1 
ATOM   5715 C CE  . LYS A 1 713 ? -35.600 -13.973 44.085 1.00 20.94 ? 713  LYS A CE  1 
ATOM   5716 N NZ  . LYS A 1 713 ? -36.038 -13.595 45.472 1.00 23.71 ? 713  LYS A NZ  1 
ATOM   5717 N N   . GLN A 1 714 ? -36.194 -15.430 37.506 1.00 20.55 ? 714  GLN A N   1 
ATOM   5718 C CA  . GLN A 1 714 ? -36.580 -16.737 36.988 1.00 21.98 ? 714  GLN A CA  1 
ATOM   5719 C C   . GLN A 1 714 ? -35.719 -17.212 35.841 1.00 22.21 ? 714  GLN A C   1 
ATOM   5720 O O   . GLN A 1 714 ? -35.118 -16.391 35.122 1.00 22.19 ? 714  GLN A O   1 
ATOM   5721 C CB  . GLN A 1 714 ? -38.057 -16.711 36.540 1.00 21.51 ? 714  GLN A CB  1 
ATOM   5722 C CG  . GLN A 1 714 ? -38.328 -15.839 35.321 1.00 22.20 ? 714  GLN A CG  1 
ATOM   5723 C CD  . GLN A 1 714 ? -39.807 -15.821 34.972 1.00 23.78 ? 714  GLN A CD  1 
ATOM   5724 O OE1 . GLN A 1 714 ? -40.347 -16.836 34.539 1.00 30.11 ? 714  GLN A OE1 1 
ATOM   5725 N NE2 . GLN A 1 714 ? -40.465 -14.684 35.177 1.00 22.80 ? 714  GLN A NE2 1 
ATOM   5726 N N   . LYS A 1 715 ? -35.645 -18.533 35.681 1.00 22.52 ? 715  LYS A N   1 
ATOM   5727 C CA  . LYS A 1 715 ? -34.938 -19.146 34.556 1.00 25.29 ? 715  LYS A CA  1 
ATOM   5728 C C   . LYS A 1 715 ? -35.863 -19.042 33.353 1.00 24.95 ? 715  LYS A C   1 
ATOM   5729 O O   . LYS A 1 715 ? -37.069 -19.235 33.478 1.00 24.97 ? 715  LYS A O   1 
ATOM   5730 C CB  . LYS A 1 715 ? -34.585 -20.608 34.838 1.00 25.24 ? 715  LYS A CB  1 
ATOM   5731 C CG  . LYS A 1 715 ? -33.378 -20.805 35.802 1.00 29.51 ? 715  LYS A CG  1 
ATOM   5732 C CD  . LYS A 1 715 ? -33.376 -22.209 36.463 1.00 28.24 ? 715  LYS A CD  1 
ATOM   5733 C CE  . LYS A 1 715 ? -32.281 -22.356 37.542 1.00 30.97 ? 715  LYS A CE  1 
ATOM   5734 N NZ  . LYS A 1 715 ? -32.083 -21.061 38.295 1.00 30.48 ? 715  LYS A NZ  1 
ATOM   5735 N N   . VAL A 1 716 ? -35.316 -18.684 32.198 1.00 24.56 ? 716  VAL A N   1 
ATOM   5736 C CA  . VAL A 1 716 ? -36.140 -18.544 30.998 1.00 25.22 ? 716  VAL A CA  1 
ATOM   5737 C C   . VAL A 1 716 ? -35.466 -19.207 29.818 1.00 25.76 ? 716  VAL A C   1 
ATOM   5738 O O   . VAL A 1 716 ? -34.244 -19.435 29.819 1.00 26.42 ? 716  VAL A O   1 
ATOM   5739 C CB  . VAL A 1 716 ? -36.449 -17.053 30.671 1.00 25.19 ? 716  VAL A CB  1 
ATOM   5740 C CG1 . VAL A 1 716 ? -37.036 -16.342 31.877 1.00 26.54 ? 716  VAL A CG1 1 
ATOM   5741 C CG2 . VAL A 1 716 ? -35.216 -16.319 30.191 1.00 25.75 ? 716  VAL A CG2 1 
ATOM   5742 N N   . GLU A 1 717 ? -36.249 -19.519 28.797 1.00 25.68 ? 717  GLU A N   1 
ATOM   5743 C CA  . GLU A 1 717 ? -35.679 -19.893 27.518 1.00 26.58 ? 717  GLU A CA  1 
ATOM   5744 C C   . GLU A 1 717 ? -35.748 -18.650 26.631 1.00 26.29 ? 717  GLU A C   1 
ATOM   5745 O O   . GLU A 1 717 ? -36.835 -18.248 26.168 1.00 26.41 ? 717  GLU A O   1 
ATOM   5746 C CB  . GLU A 1 717 ? -36.454 -21.068 26.916 1.00 27.34 ? 717  GLU A CB  1 
ATOM   5747 C CG  . GLU A 1 717 ? -35.772 -21.740 25.772 1.00 30.99 ? 717  GLU A CG  1 
ATOM   5748 C CD  . GLU A 1 717 ? -36.635 -22.824 25.163 1.00 37.56 ? 717  GLU A CD  1 
ATOM   5749 O OE1 . GLU A 1 717 ? -36.107 -23.943 24.965 1.00 40.56 ? 717  GLU A OE1 1 
ATOM   5750 O OE2 . GLU A 1 717 ? -37.835 -22.548 24.881 1.00 38.27 ? 717  GLU A OE2 1 
ATOM   5751 N N   . MET A 1 718 ? -34.603 -17.999 26.449 1.00 25.26 ? 718  MET A N   1 
ATOM   5752 C CA  . MET A 1 718 ? -34.567 -16.763 25.709 1.00 25.60 ? 718  MET A CA  1 
ATOM   5753 C C   . MET A 1 718 ? -34.409 -17.083 24.225 1.00 25.10 ? 718  MET A C   1 
ATOM   5754 O O   . MET A 1 718 ? -33.541 -17.859 23.853 1.00 24.21 ? 718  MET A O   1 
ATOM   5755 C CB  . MET A 1 718 ? -33.399 -15.908 26.205 1.00 25.45 ? 718  MET A CB  1 
ATOM   5756 C CG  . MET A 1 718 ? -33.627 -14.451 26.059 1.00 28.18 ? 718  MET A CG  1 
ATOM   5757 S SD  . MET A 1 718 ? -32.187 -13.542 26.681 1.00 26.76 ? 718  MET A SD  1 
ATOM   5758 C CE  . MET A 1 718 ? -32.475 -13.437 28.426 1.00 22.93 ? 718  MET A CE  1 
ATOM   5759 N N   . GLU A 1 719 ? -35.273 -16.526 23.385 1.00 24.71 ? 719  GLU A N   1 
ATOM   5760 C CA  . GLU A 1 719 ? -35.206 -16.841 21.943 1.00 25.09 ? 719  GLU A CA  1 
ATOM   5761 C C   . GLU A 1 719 ? -34.135 -15.964 21.293 1.00 23.53 ? 719  GLU A C   1 
ATOM   5762 O O   . GLU A 1 719 ? -34.265 -14.746 21.248 1.00 22.99 ? 719  GLU A O   1 
ATOM   5763 C CB  . GLU A 1 719 ? -36.548 -16.578 21.263 1.00 25.66 ? 719  GLU A CB  1 
ATOM   5764 C CG  . GLU A 1 719 ? -37.735 -17.250 21.960 1.00 32.48 ? 719  GLU A CG  1 
ATOM   5765 C CD  . GLU A 1 719 ? -37.952 -18.688 21.542 1.00 39.56 ? 719  GLU A CD  1 
ATOM   5766 O OE1 . GLU A 1 719 ? -37.179 -19.189 20.699 1.00 43.23 ? 719  GLU A OE1 1 
ATOM   5767 O OE2 . GLU A 1 719 ? -38.919 -19.318 22.050 1.00 43.42 ? 719  GLU A OE2 1 
ATOM   5768 N N   . LEU A 1 720 ? -33.072 -16.590 20.816 1.00 23.03 ? 720  LEU A N   1 
ATOM   5769 C CA  . LEU A 1 720 ? -31.976 -15.847 20.225 1.00 22.61 ? 720  LEU A CA  1 
ATOM   5770 C C   . LEU A 1 720 ? -31.523 -16.468 18.904 1.00 21.62 ? 720  LEU A C   1 
ATOM   5771 O O   . LEU A 1 720 ? -30.599 -17.283 18.877 1.00 20.86 ? 720  LEU A O   1 
ATOM   5772 C CB  . LEU A 1 720 ? -30.814 -15.709 21.214 1.00 22.22 ? 720  LEU A CB  1 
ATOM   5773 C CG  . LEU A 1 720 ? -31.115 -15.048 22.547 1.00 24.12 ? 720  LEU A CG  1 
ATOM   5774 C CD1 . LEU A 1 720 ? -29.953 -15.319 23.510 1.00 24.37 ? 720  LEU A CD1 1 
ATOM   5775 C CD2 . LEU A 1 720 ? -31.419 -13.552 22.392 1.00 25.72 ? 720  LEU A CD2 1 
ATOM   5776 N N   . PRO A 1 721 ? -32.159 -16.054 17.794 1.00 21.52 ? 721  PRO A N   1 
ATOM   5777 C CA  . PRO A 1 721 ? -31.840 -16.559 16.454 1.00 22.16 ? 721  PRO A CA  1 
ATOM   5778 C C   . PRO A 1 721 ? -30.380 -16.226 16.089 1.00 21.74 ? 721  PRO A C   1 
ATOM   5779 O O   . PRO A 1 721 ? -29.707 -15.509 16.840 1.00 22.13 ? 721  PRO A O   1 
ATOM   5780 C CB  . PRO A 1 721 ? -32.826 -15.824 15.540 1.00 22.66 ? 721  PRO A CB  1 
ATOM   5781 C CG  . PRO A 1 721 ? -33.858 -15.236 16.431 1.00 22.61 ? 721  PRO A CG  1 
ATOM   5782 C CD  . PRO A 1 721 ? -33.230 -15.047 17.778 1.00 22.13 ? 721  PRO A CD  1 
ATOM   5783 N N   . GLY A 1 722 ? -29.888 -16.754 14.975 1.00 20.90 ? 722  GLY A N   1 
ATOM   5784 C CA  . GLY A 1 722 ? -28.464 -16.597 14.597 1.00 20.90 ? 722  GLY A CA  1 
ATOM   5785 C C   . GLY A 1 722 ? -27.916 -15.183 14.566 1.00 20.30 ? 722  GLY A C   1 
ATOM   5786 O O   . GLY A 1 722 ? -26.698 -15.000 14.632 1.00 19.89 ? 722  GLY A O   1 
ATOM   5787 N N   . ASP A 1 723 ? -28.805 -14.186 14.438 1.00 20.20 ? 723  ASP A N   1 
ATOM   5788 C CA  . ASP A 1 723 ? -28.424 -12.762 14.405 1.00 20.78 ? 723  ASP A CA  1 
ATOM   5789 C C   . ASP A 1 723 ? -28.555 -12.011 15.745 1.00 19.45 ? 723  ASP A C   1 
ATOM   5790 O O   . ASP A 1 723 ? -28.397 -10.796 15.777 1.00 20.52 ? 723  ASP A O   1 
ATOM   5791 C CB  . ASP A 1 723 ? -29.196 -11.990 13.310 1.00 21.72 ? 723  ASP A CB  1 
ATOM   5792 C CG  . ASP A 1 723 ? -30.704 -11.991 13.540 1.00 25.48 ? 723  ASP A CG  1 
ATOM   5793 O OD1 . ASP A 1 723 ? -31.193 -12.892 14.254 1.00 25.51 ? 723  ASP A OD1 1 
ATOM   5794 O OD2 . ASP A 1 723 ? -31.397 -11.087 12.991 1.00 31.14 ? 723  ASP A OD2 1 
ATOM   5795 N N   . LYS A 1 724 ? -28.843 -12.720 16.836 1.00 19.83 ? 724  LYS A N   1 
ATOM   5796 C CA  . LYS A 1 724 ? -29.096 -12.071 18.135 1.00 18.74 ? 724  LYS A CA  1 
ATOM   5797 C C   . LYS A 1 724 ? -28.224 -12.570 19.285 1.00 17.88 ? 724  LYS A C   1 
ATOM   5798 O O   . LYS A 1 724 ? -27.873 -13.731 19.327 1.00 18.53 ? 724  LYS A O   1 
ATOM   5799 C CB  . LYS A 1 724 ? -30.566 -12.243 18.554 1.00 19.66 ? 724  LYS A CB  1 
ATOM   5800 C CG  . LYS A 1 724 ? -31.564 -11.615 17.597 1.00 19.50 ? 724  LYS A CG  1 
ATOM   5801 C CD  . LYS A 1 724 ? -31.450 -10.118 17.508 1.00 25.23 ? 724  LYS A CD  1 
ATOM   5802 C CE  . LYS A 1 724 ? -32.431 -9.564  16.442 1.00 28.25 ? 724  LYS A CE  1 
ATOM   5803 N NZ  . LYS A 1 724 ? -32.523 -8.073  16.519 1.00 31.17 ? 724  LYS A NZ  1 
ATOM   5804 N N   . ILE A 1 725 ? -27.899 -11.643 20.194 1.00 16.61 ? 725  ILE A N   1 
ATOM   5805 C CA  . ILE A 1 725 ? -27.414 -11.935 21.536 1.00 16.68 ? 725  ILE A CA  1 
ATOM   5806 C C   . ILE A 1 725 ? -28.356 -11.206 22.468 1.00 16.59 ? 725  ILE A C   1 
ATOM   5807 O O   . ILE A 1 725 ? -28.901 -10.167 22.106 1.00 17.40 ? 725  ILE A O   1 
ATOM   5808 C CB  . ILE A 1 725 ? -25.920 -11.503 21.741 1.00 15.82 ? 725  ILE A CB  1 
ATOM   5809 C CG1 . ILE A 1 725 ? -25.483 -11.688 23.199 1.00 15.82 ? 725  ILE A CG1 1 
ATOM   5810 C CG2 . ILE A 1 725 ? -25.696 -10.067 21.311 1.00 16.02 ? 725  ILE A CG2 1 
ATOM   5811 C CD1 . ILE A 1 725 ? -23.946 -11.906 23.359 1.00 16.50 ? 725  ILE A CD1 1 
ATOM   5812 N N   . GLY A 1 726 ? -28.605 -11.764 23.644 1.00 16.58 ? 726  GLY A N   1 
ATOM   5813 C CA  . GLY A 1 726 ? -29.500 -11.088 24.594 1.00 15.99 ? 726  GLY A CA  1 
ATOM   5814 C C   . GLY A 1 726 ? -28.840 -9.888  25.228 1.00 15.49 ? 726  GLY A C   1 
ATOM   5815 O O   . GLY A 1 726 ? -27.745 -9.999  25.793 1.00 14.35 ? 726  GLY A O   1 
ATOM   5816 N N   . LEU A 1 727 ? -29.503 -8.734  25.175 1.00 15.16 ? 727  LEU A N   1 
ATOM   5817 C CA  . LEU A 1 727 ? -28.972 -7.550  25.841 1.00 15.37 ? 727  LEU A CA  1 
ATOM   5818 C C   . LEU A 1 727 ? -30.147 -6.918  26.521 1.00 15.67 ? 727  LEU A C   1 
ATOM   5819 O O   . LEU A 1 727 ? -31.114 -6.544  25.817 1.00 15.10 ? 727  LEU A O   1 
ATOM   5820 C CB  . LEU A 1 727 ? -28.412 -6.556  24.832 1.00 15.45 ? 727  LEU A CB  1 
ATOM   5821 C CG  . LEU A 1 727 ? -27.140 -6.969  24.076 1.00 17.49 ? 727  LEU A CG  1 
ATOM   5822 C CD1 . LEU A 1 727 ? -26.879 -5.886  23.005 1.00 15.89 ? 727  LEU A CD1 1 
ATOM   5823 C CD2 . LEU A 1 727 ? -25.986 -7.108  25.025 1.00 17.30 ? 727  LEU A CD2 1 
ATOM   5824 N N   . HIS A 1 728 ? -30.087 -6.802  27.854 1.00 14.95 ? 728  HIS A N   1 
ATOM   5825 C CA  . HIS A 1 728 ? -31.162 -6.160  28.616 1.00 14.80 ? 728  HIS A CA  1 
ATOM   5826 C C   . HIS A 1 728 ? -30.670 -5.090  29.572 1.00 15.25 ? 728  HIS A C   1 
ATOM   5827 O O   . HIS A 1 728 ? -29.633 -5.251  30.246 1.00 14.43 ? 728  HIS A O   1 
ATOM   5828 C CB  . HIS A 1 728 ? -31.925 -7.222  29.393 1.00 15.29 ? 728  HIS A CB  1 
ATOM   5829 C CG  . HIS A 1 728 ? -32.650 -8.163  28.491 1.00 15.85 ? 728  HIS A CG  1 
ATOM   5830 N ND1 . HIS A 1 728 ? -32.048 -9.275  27.950 1.00 15.62 ? 728  HIS A ND1 1 
ATOM   5831 C CD2 . HIS A 1 728 ? -33.889 -8.095  27.941 1.00 14.69 ? 728  HIS A CD2 1 
ATOM   5832 C CE1 . HIS A 1 728 ? -32.900 -9.891  27.147 1.00 18.34 ? 728  HIS A CE1 1 
ATOM   5833 N NE2 . HIS A 1 728 ? -34.024 -9.191  27.123 1.00 18.20 ? 728  HIS A NE2 1 
ATOM   5834 N N   . LEU A 1 729 ? -31.462 -4.030  29.679 1.00 14.47 ? 729  LEU A N   1 
ATOM   5835 C CA  . LEU A 1 729 ? -31.176 -2.909  30.541 1.00 14.83 ? 729  LEU A CA  1 
ATOM   5836 C C   . LEU A 1 729 ? -31.970 -2.980  31.841 1.00 15.43 ? 729  LEU A C   1 
ATOM   5837 O O   . LEU A 1 729 ? -33.195 -3.187  31.833 1.00 15.61 ? 729  LEU A O   1 
ATOM   5838 C CB  . LEU A 1 729 ? -31.464 -1.583  29.803 1.00 13.61 ? 729  LEU A CB  1 
ATOM   5839 C CG  . LEU A 1 729 ? -30.602 -1.301  28.552 1.00 14.14 ? 729  LEU A CG  1 
ATOM   5840 C CD1 . LEU A 1 729 ? -31.120 0.019   27.983 1.00 15.22 ? 729  LEU A CD1 1 
ATOM   5841 C CD2 . LEU A 1 729 ? -29.150 -1.086  28.965 1.00 15.45 ? 729  LEU A CD2 1 
ATOM   5842 N N   . ARG A 1 730 ? -31.258 -2.770  32.947 1.00 14.91 ? 730  ARG A N   1 
ATOM   5843 C CA  . ARG A 1 730 ? -31.838 -2.834  34.283 1.00 14.75 ? 730  ARG A CA  1 
ATOM   5844 C C   . ARG A 1 730 ? -32.631 -1.602  34.681 1.00 14.76 ? 730  ARG A C   1 
ATOM   5845 O O   . ARG A 1 730 ? -32.125 -0.483  34.669 1.00 14.56 ? 730  ARG A O   1 
ATOM   5846 C CB  . ARG A 1 730 ? -30.738 -3.116  35.300 1.00 14.32 ? 730  ARG A CB  1 
ATOM   5847 C CG  . ARG A 1 730 ? -31.233 -3.347  36.738 1.00 13.90 ? 730  ARG A CG  1 
ATOM   5848 C CD  . ARG A 1 730 ? -30.048 -3.775  37.560 1.00 15.27 ? 730  ARG A CD  1 
ATOM   5849 N NE  . ARG A 1 730 ? -30.366 -3.855  38.988 1.00 11.72 ? 730  ARG A NE  1 
ATOM   5850 C CZ  . ARG A 1 730 ? -29.432 -3.958  39.911 1.00 17.26 ? 730  ARG A CZ  1 
ATOM   5851 N NH1 . ARG A 1 730 ? -28.149 -3.987  39.529 1.00 15.17 ? 730  ARG A NH1 1 
ATOM   5852 N NH2 . ARG A 1 730 ? -29.751 -4.028  41.191 1.00 15.61 ? 730  ARG A NH2 1 
ATOM   5853 N N   . GLY A 1 731 ? -33.888 -1.811  35.076 1.00 15.15 ? 731  GLY A N   1 
ATOM   5854 C CA  . GLY A 1 731 ? -34.675 -0.711  35.596 1.00 14.96 ? 731  GLY A CA  1 
ATOM   5855 C C   . GLY A 1 731 ? -33.994 -0.104  36.818 1.00 15.49 ? 731  GLY A C   1 
ATOM   5856 O O   . GLY A 1 731 ? -33.527 -0.824  37.713 1.00 15.93 ? 731  GLY A O   1 
ATOM   5857 N N   . GLY A 1 732 ? -33.935 1.228   36.856 1.00 14.45 ? 732  GLY A N   1 
ATOM   5858 C CA  . GLY A 1 732 ? -33.308 1.964   37.970 1.00 14.45 ? 732  GLY A CA  1 
ATOM   5859 C C   . GLY A 1 732 ? -31.991 2.608   37.568 1.00 14.31 ? 732  GLY A C   1 
ATOM   5860 O O   . GLY A 1 732 ? -31.363 3.300   38.371 1.00 14.13 ? 732  GLY A O   1 
ATOM   5861 N N   . TYR A 1 733 ? -31.608 2.381   36.318 1.00 14.31 ? 733  TYR A N   1 
ATOM   5862 C CA  . TYR A 1 733 ? -30.331 2.876   35.790 1.00 14.58 ? 733  TYR A CA  1 
ATOM   5863 C C   . TYR A 1 733 ? -30.454 3.763   34.550 1.00 14.67 ? 733  TYR A C   1 
ATOM   5864 O O   . TYR A 1 733 ? -31.380 3.616   33.720 1.00 14.82 ? 733  TYR A O   1 
ATOM   5865 C CB  . TYR A 1 733 ? -29.348 1.683   35.584 1.00 13.65 ? 733  TYR A CB  1 
ATOM   5866 C CG  . TYR A 1 733 ? -29.067 1.010   36.891 1.00 17.75 ? 733  TYR A CG  1 
ATOM   5867 C CD1 . TYR A 1 733 ? -27.990 1.419   37.684 1.00 18.32 ? 733  TYR A CD1 1 
ATOM   5868 C CD2 . TYR A 1 733 ? -29.933 0.020   37.396 1.00 14.85 ? 733  TYR A CD2 1 
ATOM   5869 C CE1 . TYR A 1 733 ? -27.756 0.829   38.918 1.00 18.34 ? 733  TYR A CE1 1 
ATOM   5870 C CE2 . TYR A 1 733 ? -29.729 -0.540  38.657 1.00 20.68 ? 733  TYR A CE2 1 
ATOM   5871 C CZ  . TYR A 1 733 ? -28.628 -0.137  39.398 1.00 21.66 ? 733  TYR A CZ  1 
ATOM   5872 O OH  . TYR A 1 733 ? -28.409 -0.693  40.642 1.00 21.57 ? 733  TYR A OH  1 
ATOM   5873 N N   . ILE A 1 734 ? -29.530 4.726   34.457 1.00 14.00 ? 734  ILE A N   1 
ATOM   5874 C CA  . ILE A 1 734 ? -29.504 5.684   33.365 1.00 14.70 ? 734  ILE A CA  1 
ATOM   5875 C C   . ILE A 1 734 ? -28.166 5.508   32.697 1.00 15.23 ? 734  ILE A C   1 
ATOM   5876 O O   . ILE A 1 734 ? -27.127 5.494   33.396 1.00 15.86 ? 734  ILE A O   1 
ATOM   5877 C CB  . ILE A 1 734 ? -29.704 7.141   33.837 1.00 14.31 ? 734  ILE A CB  1 
ATOM   5878 C CG1 . ILE A 1 734 ? -31.055 7.259   34.591 1.00 15.25 ? 734  ILE A CG1 1 
ATOM   5879 C CG2 . ILE A 1 734 ? -29.631 8.142   32.631 1.00 14.40 ? 734  ILE A CG2 1 
ATOM   5880 C CD1 . ILE A 1 734 ? -31.295 8.596   35.262 1.00 14.36 ? 734  ILE A CD1 1 
ATOM   5881 N N   . PHE A 1 735 ? -28.216 5.281   31.384 1.00 15.34 ? 735  PHE A N   1 
ATOM   5882 C CA  . PHE A 1 735 ? -27.023 4.878   30.623 1.00 14.18 ? 735  PHE A CA  1 
ATOM   5883 C C   . PHE A 1 735 ? -26.654 5.976   29.634 1.00 14.21 ? 735  PHE A C   1 
ATOM   5884 O O   . PHE A 1 735 ? -27.460 6.326   28.773 1.00 14.81 ? 735  PHE A O   1 
ATOM   5885 C CB  . PHE A 1 735 ? -27.273 3.589   29.849 1.00 14.09 ? 735  PHE A CB  1 
ATOM   5886 C CG  . PHE A 1 735 ? -27.733 2.439   30.688 1.00 14.45 ? 735  PHE A CG  1 
ATOM   5887 C CD1 . PHE A 1 735 ? -26.842 1.443   31.072 1.00 17.18 ? 735  PHE A CD1 1 
ATOM   5888 C CD2 . PHE A 1 735 ? -29.083 2.349   31.083 1.00 13.77 ? 735  PHE A CD2 1 
ATOM   5889 C CE1 . PHE A 1 735 ? -27.255 0.364   31.861 1.00 17.42 ? 735  PHE A CE1 1 
ATOM   5890 C CE2 . PHE A 1 735 ? -29.522 1.290   31.880 1.00 12.91 ? 735  PHE A CE2 1 
ATOM   5891 C CZ  . PHE A 1 735 ? -28.636 0.282   32.252 1.00 12.75 ? 735  PHE A CZ  1 
ATOM   5892 N N   . PRO A 1 736 ? -25.432 6.533   29.768 1.00 13.72 ? 736  PRO A N   1 
ATOM   5893 C CA  . PRO A 1 736 ? -24.983 7.500   28.792 1.00 13.52 ? 736  PRO A CA  1 
ATOM   5894 C C   . PRO A 1 736 ? -24.520 6.824   27.514 1.00 14.12 ? 736  PRO A C   1 
ATOM   5895 O O   . PRO A 1 736 ? -23.847 5.757   27.535 1.00 14.72 ? 736  PRO A O   1 
ATOM   5896 C CB  . PRO A 1 736 ? -23.819 8.247   29.513 1.00 12.53 ? 736  PRO A CB  1 
ATOM   5897 C CG  . PRO A 1 736 ? -23.220 7.229   30.406 1.00 12.07 ? 736  PRO A CG  1 
ATOM   5898 C CD  . PRO A 1 736 ? -24.450 6.329   30.856 1.00 10.99 ? 736  PRO A CD  1 
ATOM   5899 N N   . THR A 1 737 ? -24.863 7.454   26.389 1.00 14.53 ? 737  THR A N   1 
ATOM   5900 C CA  . THR A 1 737 ? -24.549 6.905   25.064 1.00 14.04 ? 737  THR A CA  1 
ATOM   5901 C C   . THR A 1 737 ? -24.001 7.979   24.133 1.00 12.45 ? 737  THR A C   1 
ATOM   5902 O O   . THR A 1 737 ? -24.068 9.159   24.411 1.00 14.09 ? 737  THR A O   1 
ATOM   5903 C CB  . THR A 1 737 ? -25.789 6.246   24.352 1.00 15.53 ? 737  THR A CB  1 
ATOM   5904 O OG1 . THR A 1 737 ? -26.710 7.268   23.987 1.00 16.27 ? 737  THR A OG1 1 
ATOM   5905 C CG2 . THR A 1 737 ? -26.499 5.229   25.243 1.00 16.73 ? 737  THR A CG2 1 
ATOM   5906 N N   . GLN A 1 738 ? -23.392 7.552   23.046 1.00 13.43 ? 738  GLN A N   1 
ATOM   5907 C CA  . GLN A 1 738 ? -22.854 8.501   22.072 1.00 13.50 ? 738  GLN A CA  1 
ATOM   5908 C C   . GLN A 1 738 ? -22.985 7.825   20.726 1.00 14.64 ? 738  GLN A C   1 
ATOM   5909 O O   . GLN A 1 738 ? -22.613 6.671   20.585 1.00 14.47 ? 738  GLN A O   1 
ATOM   5910 C CB  . GLN A 1 738 ? -21.382 8.818   22.408 1.00 13.78 ? 738  GLN A CB  1 
ATOM   5911 C CG  . GLN A 1 738 ? -20.759 9.861   21.462 1.00 13.54 ? 738  GLN A CG  1 
ATOM   5912 C CD  . GLN A 1 738 ? -19.517 10.506  22.077 1.00 16.75 ? 738  GLN A CD  1 
ATOM   5913 O OE1 . GLN A 1 738 ? -18.689 9.810   22.629 1.00 15.92 ? 738  GLN A OE1 1 
ATOM   5914 N NE2 . GLN A 1 738 ? -19.382 11.826  21.963 1.00 16.27 ? 738  GLN A NE2 1 
ATOM   5915 N N   . GLN A 1 739 ? -23.542 8.526   19.730 1.00 13.67 ? 739  GLN A N   1 
ATOM   5916 C CA  . GLN A 1 739 ? -23.694 7.993   18.398 1.00 16.30 ? 739  GLN A CA  1 
ATOM   5917 C C   . GLN A 1 739 ? -22.371 7.357   17.957 1.00 16.32 ? 739  GLN A C   1 
ATOM   5918 O O   . GLN A 1 739 ? -21.317 8.009   18.040 1.00 16.63 ? 739  GLN A O   1 
ATOM   5919 C CB  . GLN A 1 739 ? -24.059 9.113   17.422 1.00 16.38 ? 739  GLN A CB  1 
ATOM   5920 C CG  . GLN A 1 739 ? -24.284 8.642   15.983 1.00 18.42 ? 739  GLN A CG  1 
ATOM   5921 C CD  . GLN A 1 739 ? -24.570 9.783   15.022 1.00 20.13 ? 739  GLN A CD  1 
ATOM   5922 O OE1 . GLN A 1 739 ? -24.782 10.924  15.447 1.00 22.53 ? 739  GLN A OE1 1 
ATOM   5923 N NE2 . GLN A 1 739 ? -24.576 9.476   13.699 1.00 21.10 ? 739  GLN A NE2 1 
ATOM   5924 N N   . PRO A 1 740 ? -22.437 6.106   17.501 1.00 16.29 ? 740  PRO A N   1 
ATOM   5925 C CA  . PRO A 1 740 ? -21.218 5.364   17.162 1.00 16.42 ? 740  PRO A CA  1 
ATOM   5926 C C   . PRO A 1 740 ? -20.622 5.828   15.817 1.00 17.60 ? 740  PRO A C   1 
ATOM   5927 O O   . PRO A 1 740 ? -21.297 6.430   14.963 1.00 15.57 ? 740  PRO A O   1 
ATOM   5928 C CB  . PRO A 1 740 ? -21.704 3.918   17.070 1.00 15.56 ? 740  PRO A CB  1 
ATOM   5929 C CG  . PRO A 1 740 ? -23.122 4.045   16.629 1.00 16.49 ? 740  PRO A CG  1 
ATOM   5930 C CD  . PRO A 1 740 ? -23.650 5.277   17.323 1.00 14.24 ? 740  PRO A CD  1 
ATOM   5931 N N   . ASN A 1 741 ? -19.335 5.562   15.650 1.00 17.48 ? 741  ASN A N   1 
ATOM   5932 C CA  . ASN A 1 741 ? -18.678 5.770   14.374 1.00 18.34 ? 741  ASN A CA  1 
ATOM   5933 C C   . ASN A 1 741 ? -17.662 4.629   14.330 1.00 18.22 ? 741  ASN A C   1 
ATOM   5934 O O   . ASN A 1 741 ? -17.517 3.864   15.303 1.00 18.55 ? 741  ASN A O   1 
ATOM   5935 C CB  . ASN A 1 741 ? -17.990 7.145   14.323 1.00 18.49 ? 741  ASN A CB  1 
ATOM   5936 C CG  . ASN A 1 741 ? -17.758 7.676   12.858 1.00 21.16 ? 741  ASN A CG  1 
ATOM   5937 O OD1 . ASN A 1 741 ? -17.811 6.926   11.881 1.00 22.58 ? 741  ASN A OD1 1 
ATOM   5938 N ND2 . ASN A 1 741 ? -17.506 8.978   12.741 1.00 28.27 ? 741  ASN A ND2 1 
ATOM   5939 N N   . THR A 1 742 ? -16.976 4.496   13.208 1.00 17.60 ? 742  THR A N   1 
ATOM   5940 C CA  . THR A 1 742 ? -16.102 3.344   12.999 1.00 17.66 ? 742  THR A CA  1 
ATOM   5941 C C   . THR A 1 742 ? -14.825 3.415   13.836 1.00 16.50 ? 742  THR A C   1 
ATOM   5942 O O   . THR A 1 742 ? -14.114 2.401   13.952 1.00 17.01 ? 742  THR A O   1 
ATOM   5943 C CB  . THR A 1 742 ? -15.712 3.191   11.522 1.00 17.25 ? 742  THR A CB  1 
ATOM   5944 O OG1 . THR A 1 742 ? -15.039 4.379   11.097 1.00 19.59 ? 742  THR A OG1 1 
ATOM   5945 C CG2 . THR A 1 742 ? -16.927 2.908   10.667 1.00 20.10 ? 742  THR A CG2 1 
ATOM   5946 N N   . THR A 1 743 ? -14.527 4.585   14.387 1.00 16.91 ? 743  THR A N   1 
ATOM   5947 C CA  . THR A 1 743 ? -13.384 4.764   15.304 1.00 16.96 ? 743  THR A CA  1 
ATOM   5948 C C   . THR A 1 743 ? -13.812 5.603   16.501 1.00 17.14 ? 743  THR A C   1 
ATOM   5949 O O   . THR A 1 743 ? -14.771 6.419   16.404 1.00 17.31 ? 743  THR A O   1 
ATOM   5950 C CB  . THR A 1 743 ? -12.190 5.473   14.598 1.00 17.92 ? 743  THR A CB  1 
ATOM   5951 O OG1 . THR A 1 743 ? -12.541 6.824   14.333 1.00 17.53 ? 743  THR A OG1 1 
ATOM   5952 C CG2 . THR A 1 743 ? -11.868 4.793   13.261 1.00 17.90 ? 743  THR A CG2 1 
ATOM   5953 N N   . THR A 1 744 ? -13.132 5.449   17.634 1.00 16.57 ? 744  THR A N   1 
ATOM   5954 C CA  . THR A 1 744 ? -13.477 6.279   18.792 1.00 17.67 ? 744  THR A CA  1 
ATOM   5955 C C   . THR A 1 744 ? -12.932 7.707   18.607 1.00 18.48 ? 744  THR A C   1 
ATOM   5956 O O   . THR A 1 744 ? -13.468 8.653   19.176 1.00 18.92 ? 744  THR A O   1 
ATOM   5957 C CB  . THR A 1 744 ? -12.939 5.704   20.107 1.00 18.77 ? 744  THR A CB  1 
ATOM   5958 O OG1 . THR A 1 744 ? -11.503 5.584   20.016 1.00 16.49 ? 744  THR A OG1 1 
ATOM   5959 C CG2 . THR A 1 744 ? -13.547 4.345   20.415 1.00 17.39 ? 744  THR A CG2 1 
ATOM   5960 N N   . LEU A 1 745 ? -11.885 7.885   17.793 1.00 18.35 ? 745  LEU A N   1 
ATOM   5961 C CA  . LEU A 1 745 ? -11.413 9.256   17.471 1.00 18.92 ? 745  LEU A CA  1 
ATOM   5962 C C   . LEU A 1 745 ? -12.617 10.089  16.991 1.00 19.01 ? 745  LEU A C   1 
ATOM   5963 O O   . LEU A 1 745 ? -12.861 11.210  17.467 1.00 19.57 ? 745  LEU A O   1 
ATOM   5964 C CB  . LEU A 1 745 ? -10.354 9.225   16.358 1.00 19.90 ? 745  LEU A CB  1 
ATOM   5965 C CG  . LEU A 1 745 ? -9.751  10.614  16.073 1.00 21.98 ? 745  LEU A CG  1 
ATOM   5966 C CD1 . LEU A 1 745 ? -8.922  11.070  17.237 1.00 24.38 ? 745  LEU A CD1 1 
ATOM   5967 C CD2 . LEU A 1 745 ? -8.899  10.594  14.825 1.00 26.90 ? 745  LEU A CD2 1 
ATOM   5968 N N   . ALA A 1 746 ? -13.368 9.508   16.073 1.00 17.85 ? 746  ALA A N   1 
ATOM   5969 C CA  . ALA A 1 746 ? -14.548 10.147  15.502 1.00 18.91 ? 746  ALA A CA  1 
ATOM   5970 C C   . ALA A 1 746 ? -15.767 10.093  16.407 1.00 18.59 ? 746  ALA A C   1 
ATOM   5971 O O   . ALA A 1 746 ? -16.487 11.096  16.500 1.00 19.23 ? 746  ALA A O   1 
ATOM   5972 C CB  . ALA A 1 746 ? -14.886 9.554   14.159 1.00 18.61 ? 746  ALA A CB  1 
ATOM   5973 N N   . SER A 1 747 ? -16.019 8.956   17.053 1.00 17.70 ? 747  SER A N   1 
ATOM   5974 C CA  . SER A 1 747 ? -17.276 8.789   17.831 1.00 17.85 ? 747  SER A CA  1 
ATOM   5975 C C   . SER A 1 747 ? -17.346 9.761   19.006 1.00 17.16 ? 747  SER A C   1 
ATOM   5976 O O   . SER A 1 747 ? -18.410 10.262  19.324 1.00 17.90 ? 747  SER A O   1 
ATOM   5977 C CB  . SER A 1 747 ? -17.464 7.328   18.291 1.00 17.49 ? 747  SER A CB  1 
ATOM   5978 O OG  . SER A 1 747 ? -16.559 6.995   19.326 1.00 17.15 ? 747  SER A OG  1 
ATOM   5979 N N   . ARG A 1 748 ? -16.196 10.079  19.605 1.00 16.00 ? 748  ARG A N   1 
ATOM   5980 C CA  . ARG A 1 748 ? -16.145 10.989  20.737 1.00 16.18 ? 748  ARG A CA  1 
ATOM   5981 C C   . ARG A 1 748 ? -16.587 12.411  20.379 1.00 15.12 ? 748  ARG A C   1 
ATOM   5982 O O   . ARG A 1 748 ? -16.839 13.208  21.270 1.00 15.89 ? 748  ARG A O   1 
ATOM   5983 C CB  . ARG A 1 748 ? -14.725 11.033  21.339 1.00 16.29 ? 748  ARG A CB  1 
ATOM   5984 C CG  . ARG A 1 748 ? -14.323 9.786   22.120 1.00 16.64 ? 748  ARG A CG  1 
ATOM   5985 C CD  . ARG A 1 748 ? -12.818 9.858   22.512 1.00 16.38 ? 748  ARG A CD  1 
ATOM   5986 N NE  . ARG A 1 748 ? -12.524 11.104  23.190 1.00 15.45 ? 748  ARG A NE  1 
ATOM   5987 C CZ  . ARG A 1 748 ? -12.697 11.307  24.498 1.00 18.81 ? 748  ARG A CZ  1 
ATOM   5988 N NH1 . ARG A 1 748 ? -13.152 10.330  25.276 1.00 20.43 ? 748  ARG A NH1 1 
ATOM   5989 N NH2 . ARG A 1 748 ? -12.411 12.487  25.033 1.00 17.28 ? 748  ARG A NH2 1 
ATOM   5990 N N   . LYS A 1 749 ? -16.647 12.737  19.101 1.00 16.48 ? 749  LYS A N   1 
ATOM   5991 C CA  . LYS A 1 749 ? -17.135 14.064  18.642 1.00 17.81 ? 749  LYS A CA  1 
ATOM   5992 C C   . LYS A 1 749 ? -18.643 14.041  18.390 1.00 17.78 ? 749  LYS A C   1 
ATOM   5993 O O   . LYS A 1 749 ? -19.233 15.068  18.031 1.00 19.81 ? 749  LYS A O   1 
ATOM   5994 C CB  . LYS A 1 749 ? -16.446 14.484  17.337 1.00 18.22 ? 749  LYS A CB  1 
ATOM   5995 C CG  . LYS A 1 749 ? -14.888 14.554  17.496 1.00 20.69 ? 749  LYS A CG  1 
ATOM   5996 C CD  . LYS A 1 749 ? -14.220 14.792  16.162 1.00 25.03 ? 749  LYS A CD  1 
ATOM   5997 C CE  . LYS A 1 749 ? -12.704 14.655  16.340 1.00 27.09 ? 749  LYS A CE  1 
ATOM   5998 N NZ  . LYS A 1 749 ? -11.942 14.902  15.074 1.00 31.33 ? 749  LYS A NZ  1 
ATOM   5999 N N   . ASN A 1 750 ? -19.280 12.895  18.562 1.00 17.85 ? 750  ASN A N   1 
ATOM   6000 C CA  . ASN A 1 750 ? -20.712 12.770  18.190 1.00 17.68 ? 750  ASN A CA  1 
ATOM   6001 C C   . ASN A 1 750 ? -21.706 13.188  19.317 1.00 17.28 ? 750  ASN A C   1 
ATOM   6002 O O   . ASN A 1 750 ? -21.344 13.256  20.486 1.00 16.60 ? 750  ASN A O   1 
ATOM   6003 C CB  . ASN A 1 750 ? -21.049 11.360  17.716 1.00 17.19 ? 750  ASN A CB  1 
ATOM   6004 C CG  . ASN A 1 750 ? -20.641 11.091  16.276 1.00 20.21 ? 750  ASN A CG  1 
ATOM   6005 O OD1 . ASN A 1 750 ? -20.368 12.015  15.495 1.00 20.14 ? 750  ASN A OD1 1 
ATOM   6006 N ND2 . ASN A 1 750 ? -20.573 9.817   15.924 1.00 18.43 ? 750  ASN A ND2 1 
ATOM   6007 N N   . PRO A 1 751 ? -22.961 13.474  18.946 1.00 18.41 ? 751  PRO A N   1 
ATOM   6008 C CA  . PRO A 1 751 ? -24.014 13.771  19.929 1.00 18.96 ? 751  PRO A CA  1 
ATOM   6009 C C   . PRO A 1 751 ? -24.164 12.629  20.945 1.00 18.25 ? 751  PRO A C   1 
ATOM   6010 O O   . PRO A 1 751 ? -23.999 11.458  20.588 1.00 19.32 ? 751  PRO A O   1 
ATOM   6011 C CB  . PRO A 1 751 ? -25.266 13.829  19.072 1.00 20.08 ? 751  PRO A CB  1 
ATOM   6012 C CG  . PRO A 1 751 ? -24.777 14.226  17.709 1.00 20.07 ? 751  PRO A CG  1 
ATOM   6013 C CD  . PRO A 1 751 ? -23.465 13.572  17.556 1.00 18.59 ? 751  PRO A CD  1 
ATOM   6014 N N   . LEU A 1 752 ? -24.470 12.999  22.181 1.00 17.87 ? 752  LEU A N   1 
ATOM   6015 C CA  . LEU A 1 752 ? -24.685 12.073  23.276 1.00 17.32 ? 752  LEU A CA  1 
ATOM   6016 C C   . LEU A 1 752 ? -26.180 11.801  23.453 1.00 17.89 ? 752  LEU A C   1 
ATOM   6017 O O   . LEU A 1 752 ? -27.012 12.531  22.935 1.00 16.39 ? 752  LEU A O   1 
ATOM   6018 C CB  . LEU A 1 752 ? -24.114 12.648  24.573 1.00 18.28 ? 752  LEU A CB  1 
ATOM   6019 C CG  . LEU A 1 752 ? -22.639 13.104  24.435 1.00 20.01 ? 752  LEU A CG  1 
ATOM   6020 C CD1 . LEU A 1 752 ? -22.217 13.964  25.606 1.00 22.24 ? 752  LEU A CD1 1 
ATOM   6021 C CD2 . LEU A 1 752 ? -21.847 11.878  24.410 1.00 20.85 ? 752  LEU A CD2 1 
ATOM   6022 N N   . GLY A 1 753 ? -26.479 10.749  24.203 1.00 17.37 ? 753  GLY A N   1 
ATOM   6023 C CA  . GLY A 1 753 ? -27.880 10.366  24.492 1.00 16.78 ? 753  GLY A CA  1 
ATOM   6024 C C   . GLY A 1 753 ? -27.914 9.857   25.919 1.00 17.79 ? 753  GLY A C   1 
ATOM   6025 O O   . GLY A 1 753 ? -26.870 9.584   26.521 1.00 15.48 ? 753  GLY A O   1 
ATOM   6026 N N   . LEU A 1 754 ? -29.122 9.748   26.468 1.00 17.00 ? 754  LEU A N   1 
ATOM   6027 C CA  . LEU A 1 754 ? -29.311 9.117   27.737 1.00 17.42 ? 754  LEU A CA  1 
ATOM   6028 C C   . LEU A 1 754 ? -30.350 8.027   27.522 1.00 17.16 ? 754  LEU A C   1 
ATOM   6029 O O   . LEU A 1 754 ? -31.338 8.265   26.824 1.00 18.31 ? 754  LEU A O   1 
ATOM   6030 C CB  . LEU A 1 754 ? -29.806 10.136  28.779 1.00 16.17 ? 754  LEU A CB  1 
ATOM   6031 C CG  . LEU A 1 754 ? -28.829 11.147  29.363 1.00 19.43 ? 754  LEU A CG  1 
ATOM   6032 C CD1 . LEU A 1 754 ? -29.546 12.037  30.374 1.00 20.68 ? 754  LEU A CD1 1 
ATOM   6033 C CD2 . LEU A 1 754 ? -27.580 10.406  29.994 1.00 16.95 ? 754  LEU A CD2 1 
ATOM   6034 N N   . ILE A 1 755 ? -30.135 6.841   28.088 1.00 16.86 ? 755  ILE A N   1 
ATOM   6035 C CA  . ILE A 1 755 ? -31.235 5.836   28.149 1.00 16.66 ? 755  ILE A CA  1 
ATOM   6036 C C   . ILE A 1 755 ? -31.650 5.751   29.625 1.00 17.40 ? 755  ILE A C   1 
ATOM   6037 O O   . ILE A 1 755 ? -30.844 5.384   30.480 1.00 17.17 ? 755  ILE A O   1 
ATOM   6038 C CB  . ILE A 1 755 ? -30.855 4.425   27.565 1.00 15.87 ? 755  ILE A CB  1 
ATOM   6039 C CG1 . ILE A 1 755 ? -30.401 4.500   26.099 1.00 17.37 ? 755  ILE A CG1 1 
ATOM   6040 C CG2 . ILE A 1 755 ? -32.018 3.409   27.697 1.00 16.32 ? 755  ILE A CG2 1 
ATOM   6041 C CD1 . ILE A 1 755 ? -29.601 3.189   25.637 1.00 18.12 ? 755  ILE A CD1 1 
ATOM   6042 N N   . ILE A 1 756 ? -32.909 6.102   29.920 1.00 16.38 ? 756  ILE A N   1 
ATOM   6043 C CA  . ILE A 1 756 ? -33.437 6.070   31.291 1.00 16.23 ? 756  ILE A CA  1 
ATOM   6044 C C   . ILE A 1 756 ? -34.329 4.806   31.383 1.00 16.95 ? 756  ILE A C   1 
ATOM   6045 O O   . ILE A 1 756 ? -35.412 4.768   30.789 1.00 17.47 ? 756  ILE A O   1 
ATOM   6046 C CB  . ILE A 1 756 ? -34.233 7.397   31.615 1.00 15.32 ? 756  ILE A CB  1 
ATOM   6047 C CG1 . ILE A 1 756 ? -33.282 8.609   31.552 1.00 15.82 ? 756  ILE A CG1 1 
ATOM   6048 C CG2 . ILE A 1 756 ? -34.901 7.344   32.983 1.00 15.00 ? 756  ILE A CG2 1 
ATOM   6049 C CD1 . ILE A 1 756 ? -33.972 9.949   31.471 1.00 16.28 ? 756  ILE A CD1 1 
ATOM   6050 N N   . ALA A 1 757 ? -33.856 3.778   32.079 1.00 17.67 ? 757  ALA A N   1 
ATOM   6051 C CA  . ALA A 1 757 ? -34.599 2.525   32.261 1.00 17.10 ? 757  ALA A CA  1 
ATOM   6052 C C   . ALA A 1 757 ? -35.275 2.687   33.623 1.00 17.38 ? 757  ALA A C   1 
ATOM   6053 O O   . ALA A 1 757 ? -34.652 2.624   34.653 1.00 17.58 ? 757  ALA A O   1 
ATOM   6054 C CB  . ALA A 1 757 ? -33.662 1.330   32.247 1.00 18.73 ? 757  ALA A CB  1 
ATOM   6055 N N   . LEU A 1 758 ? -36.569 2.969   33.623 1.00 16.25 ? 758  LEU A N   1 
ATOM   6056 C CA  . LEU A 1 758 ? -37.268 3.217   34.890 1.00 16.37 ? 758  LEU A CA  1 
ATOM   6057 C C   . LEU A 1 758 ? -37.472 1.942   35.760 1.00 17.40 ? 758  LEU A C   1 
ATOM   6058 O O   . LEU A 1 758 ? -37.782 0.861   35.253 1.00 17.02 ? 758  LEU A O   1 
ATOM   6059 C CB  . LEU A 1 758 ? -38.607 3.923   34.603 1.00 16.07 ? 758  LEU A CB  1 
ATOM   6060 C CG  . LEU A 1 758 ? -38.599 5.354   34.076 1.00 14.90 ? 758  LEU A CG  1 
ATOM   6061 C CD1 . LEU A 1 758 ? -40.088 5.851   33.846 1.00 17.44 ? 758  LEU A CD1 1 
ATOM   6062 C CD2 . LEU A 1 758 ? -37.866 6.274   35.012 1.00 18.17 ? 758  LEU A CD2 1 
ATOM   6063 N N   . ASP A 1 759 ? -37.282 2.075   37.075 1.00 18.71 ? 759  ASP A N   1 
ATOM   6064 C CA  . ASP A 1 759 ? -37.621 0.982   37.990 1.00 20.60 ? 759  ASP A CA  1 
ATOM   6065 C C   . ASP A 1 759 ? -39.137 0.977   38.321 1.00 22.52 ? 759  ASP A C   1 
ATOM   6066 O O   . ASP A 1 759 ? -39.885 1.780   37.750 1.00 21.73 ? 759  ASP A O   1 
ATOM   6067 C CB  . ASP A 1 759 ? -36.734 1.014   39.245 1.00 20.82 ? 759  ASP A CB  1 
ATOM   6068 C CG  . ASP A 1 759 ? -37.056 2.146   40.198 1.00 22.79 ? 759  ASP A CG  1 
ATOM   6069 O OD1 . ASP A 1 759 ? -38.132 2.796   40.097 1.00 22.45 ? 759  ASP A OD1 1 
ATOM   6070 O OD2 . ASP A 1 759 ? -36.203 2.403   41.081 1.00 24.35 ? 759  ASP A OD2 1 
ATOM   6071 N N   . GLU A 1 760 ? -39.561 0.069   39.218 1.00 24.17 ? 760  GLU A N   1 
ATOM   6072 C CA  . GLU A 1 760 ? -40.988 -0.102  39.583 1.00 26.79 ? 760  GLU A CA  1 
ATOM   6073 C C   . GLU A 1 760 ? -41.525 1.175   40.206 1.00 26.73 ? 760  GLU A C   1 
ATOM   6074 O O   . GLU A 1 760 ? -42.737 1.437   40.184 1.00 27.96 ? 760  GLU A O   1 
ATOM   6075 C CB  . GLU A 1 760 ? -41.180 -1.259  40.593 1.00 27.99 ? 760  GLU A CB  1 
ATOM   6076 C CG  . GLU A 1 760 ? -40.396 -2.550  40.322 1.00 32.66 ? 760  GLU A CG  1 
ATOM   6077 C CD  . GLU A 1 760 ? -38.997 -2.552  40.946 1.00 37.67 ? 760  GLU A CD  1 
ATOM   6078 O OE1 . GLU A 1 760 ? -38.808 -3.246  41.968 1.00 42.11 ? 760  GLU A OE1 1 
ATOM   6079 O OE2 . GLU A 1 760 ? -38.093 -1.860  40.430 1.00 39.91 ? 760  GLU A OE2 1 
ATOM   6080 N N   . ASN A 1 761 ? -40.636 1.975   40.795 1.00 25.20 ? 761  ASN A N   1 
ATOM   6081 C CA  . ASN A 1 761 ? -41.036 3.284   41.328 1.00 24.98 ? 761  ASN A CA  1 
ATOM   6082 C C   . ASN A 1 761 ? -40.897 4.482   40.358 1.00 23.38 ? 761  ASN A C   1 
ATOM   6083 O O   . ASN A 1 761 ? -41.128 5.628   40.733 1.00 23.07 ? 761  ASN A O   1 
ATOM   6084 C CB  . ASN A 1 761 ? -40.344 3.514   42.675 1.00 25.82 ? 761  ASN A CB  1 
ATOM   6085 C CG  . ASN A 1 761 ? -40.549 2.337   43.642 1.00 29.81 ? 761  ASN A CG  1 
ATOM   6086 O OD1 . ASN A 1 761 ? -41.686 1.862   43.852 1.00 32.38 ? 761  ASN A OD1 1 
ATOM   6087 N ND2 . ASN A 1 761 ? -39.460 1.844   44.204 1.00 28.56 ? 761  ASN A ND2 1 
ATOM   6088 N N   . LYS A 1 762 ? -40.561 4.186   39.097 1.00 21.13 ? 762  LYS A N   1 
ATOM   6089 C CA  . LYS A 1 762 ? -40.420 5.184   38.021 1.00 21.46 ? 762  LYS A CA  1 
ATOM   6090 C C   . LYS A 1 762 ? -39.275 6.130   38.348 1.00 19.25 ? 762  LYS A C   1 
ATOM   6091 O O   . LYS A 1 762 ? -39.335 7.333   38.130 1.00 20.12 ? 762  LYS A O   1 
ATOM   6092 C CB  . LYS A 1 762 ? -41.747 5.908   37.681 1.00 22.67 ? 762  LYS A CB  1 
ATOM   6093 C CG  . LYS A 1 762 ? -42.886 4.908   37.266 1.00 25.32 ? 762  LYS A CG  1 
ATOM   6094 C CD  . LYS A 1 762 ? -42.303 3.672   36.571 1.00 26.54 ? 762  LYS A CD  1 
ATOM   6095 C CE  . LYS A 1 762 ? -43.282 2.783   35.806 1.00 30.28 ? 762  LYS A CE  1 
ATOM   6096 N NZ  . LYS A 1 762 ? -44.576 2.539   36.496 1.00 31.55 ? 762  LYS A NZ  1 
ATOM   6097 N N   . GLU A 1 763 ? -38.231 5.549   38.909 1.00 18.46 ? 763  GLU A N   1 
ATOM   6098 C CA  . GLU A 1 763 ? -37.021 6.300   39.295 1.00 17.24 ? 763  GLU A CA  1 
ATOM   6099 C C   . GLU A 1 763 ? -35.820 5.650   38.642 1.00 15.98 ? 763  GLU A C   1 
ATOM   6100 O O   . GLU A 1 763 ? -35.872 4.503   38.266 1.00 15.21 ? 763  GLU A O   1 
ATOM   6101 C CB  . GLU A 1 763 ? -36.822 6.273   40.803 1.00 18.47 ? 763  GLU A CB  1 
ATOM   6102 C CG  . GLU A 1 763 ? -37.989 6.885   41.601 1.00 23.04 ? 763  GLU A CG  1 
ATOM   6103 C CD  . GLU A 1 763 ? -37.682 6.980   43.069 1.00 29.08 ? 763  GLU A CD  1 
ATOM   6104 O OE1 . GLU A 1 763 ? -37.166 5.992   43.647 1.00 32.05 ? 763  GLU A OE1 1 
ATOM   6105 O OE2 . GLU A 1 763 ? -37.982 8.045   43.647 1.00 33.24 ? 763  GLU A OE2 1 
ATOM   6106 N N   . ALA A 1 764 ? -34.721 6.393   38.497 1.00 15.37 ? 764  ALA A N   1 
ATOM   6107 C CA  . ALA A 1 764 ? -33.505 5.774   37.928 1.00 14.62 ? 764  ALA A CA  1 
ATOM   6108 C C   . ALA A 1 764 ? -32.361 6.682   38.237 1.00 13.45 ? 764  ALA A C   1 
ATOM   6109 O O   . ALA A 1 764 ? -32.572 7.836   38.525 1.00 13.79 ? 764  ALA A O   1 
ATOM   6110 C CB  . ALA A 1 764 ? -33.619 5.644   36.409 1.00 15.12 ? 764  ALA A CB  1 
ATOM   6111 N N   . LYS A 1 765 ? -31.128 6.175   38.188 1.00 13.95 ? 765  LYS A N   1 
ATOM   6112 C CA  . LYS A 1 765 ? -29.991 7.030   38.549 1.00 13.78 ? 765  LYS A CA  1 
ATOM   6113 C C   . LYS A 1 765 ? -28.855 6.603   37.630 1.00 13.42 ? 765  LYS A C   1 
ATOM   6114 O O   . LYS A 1 765 ? -28.818 5.487   37.199 1.00 13.34 ? 765  LYS A O   1 
ATOM   6115 C CB  . LYS A 1 765 ? -29.539 6.811   40.002 1.00 17.08 ? 765  LYS A CB  1 
ATOM   6116 C CG  . LYS A 1 765 ? -30.529 7.299   41.067 1.00 23.59 ? 765  LYS A CG  1 
ATOM   6117 C CD  . LYS A 1 765 ? -30.088 6.817   42.441 1.00 30.61 ? 765  LYS A CD  1 
ATOM   6118 C CE  . LYS A 1 765 ? -30.736 7.649   43.554 1.00 34.91 ? 765  LYS A CE  1 
ATOM   6119 N NZ  . LYS A 1 765 ? -30.303 9.077   43.441 1.00 38.92 ? 765  LYS A NZ  1 
ATOM   6120 N N   . GLY A 1 766 ? -27.952 7.518   37.307 1.00 13.69 ? 766  GLY A N   1 
ATOM   6121 C CA  . GLY A 1 766 ? -26.803 7.116   36.476 1.00 13.63 ? 766  GLY A CA  1 
ATOM   6122 C C   . GLY A 1 766 ? -25.706 8.162   36.645 1.00 14.11 ? 766  GLY A C   1 
ATOM   6123 O O   . GLY A 1 766 ? -25.859 9.123   37.373 1.00 14.71 ? 766  GLY A O   1 
ATOM   6124 N N   . GLU A 1 767 ? -24.589 7.978   35.958 1.00 14.59 ? 767  GLU A N   1 
ATOM   6125 C CA  . GLU A 1 767 ? -23.509 8.960   36.012 1.00 14.67 ? 767  GLU A CA  1 
ATOM   6126 C C   . GLU A 1 767 ? -22.716 8.894   34.695 1.00 14.04 ? 767  GLU A C   1 
ATOM   6127 O O   . GLU A 1 767 ? -22.859 7.956   33.915 1.00 13.53 ? 767  GLU A O   1 
ATOM   6128 C CB  . GLU A 1 767 ? -22.626 8.708   37.230 1.00 16.01 ? 767  GLU A CB  1 
ATOM   6129 C CG  . GLU A 1 767 ? -21.821 7.405   37.122 1.00 19.06 ? 767  GLU A CG  1 
ATOM   6130 C CD  . GLU A 1 767 ? -21.130 7.026   38.399 1.00 25.85 ? 767  GLU A CD  1 
ATOM   6131 O OE1 . GLU A 1 767 ? -21.190 7.824   39.371 1.00 30.61 ? 767  GLU A OE1 1 
ATOM   6132 O OE2 . GLU A 1 767 ? -20.509 5.942   38.426 1.00 29.30 ? 767  GLU A OE2 1 
ATOM   6133 N N   . LEU A 1 768 ? -21.921 9.927   34.434 1.00 14.67 ? 768  LEU A N   1 
ATOM   6134 C CA  . LEU A 1 768 ? -21.055 9.959   33.260 1.00 14.53 ? 768  LEU A CA  1 
ATOM   6135 C C   . LEU A 1 768 ? -19.758 10.646  33.657 1.00 14.81 ? 768  LEU A C   1 
ATOM   6136 O O   . LEU A 1 768 ? -19.775 11.715  34.226 1.00 14.98 ? 768  LEU A O   1 
ATOM   6137 C CB  . LEU A 1 768 ? -21.692 10.703  32.064 1.00 15.28 ? 768  LEU A CB  1 
ATOM   6138 C CG  . LEU A 1 768 ? -20.775 11.053  30.868 1.00 15.05 ? 768  LEU A CG  1 
ATOM   6139 C CD1 . LEU A 1 768 ? -20.238 9.748   30.188 1.00 16.38 ? 768  LEU A CD1 1 
ATOM   6140 C CD2 . LEU A 1 768 ? -21.528 11.870  29.850 1.00 16.04 ? 768  LEU A CD2 1 
ATOM   6141 N N   . PHE A 1 769 ? -18.659 9.943   33.431 1.00 13.08 ? 769  PHE A N   1 
ATOM   6142 C CA  . PHE A 1 769 ? -17.299 10.488  33.548 1.00 12.83 ? 769  PHE A CA  1 
ATOM   6143 C C   . PHE A 1 769 ? -16.863 10.899  32.156 1.00 12.06 ? 769  PHE A C   1 
ATOM   6144 O O   . PHE A 1 769 ? -17.094 10.178  31.162 1.00 12.27 ? 769  PHE A O   1 
ATOM   6145 C CB  . PHE A 1 769 ? -16.377 9.374   34.069 1.00 12.86 ? 769  PHE A CB  1 
ATOM   6146 C CG  . PHE A 1 769 ? -14.935 9.722   34.022 1.00 11.68 ? 769  PHE A CG  1 
ATOM   6147 C CD1 . PHE A 1 769 ? -14.378 10.506  35.021 1.00 12.99 ? 769  PHE A CD1 1 
ATOM   6148 C CD2 . PHE A 1 769 ? -14.122 9.230   32.986 1.00 13.22 ? 769  PHE A CD2 1 
ATOM   6149 C CE1 . PHE A 1 769 ? -12.984 10.802  34.990 1.00 12.38 ? 769  PHE A CE1 1 
ATOM   6150 C CE2 . PHE A 1 769 ? -12.743 9.529   32.957 1.00 13.00 ? 769  PHE A CE2 1 
ATOM   6151 C CZ  . PHE A 1 769 ? -12.203 10.319  33.960 1.00 14.97 ? 769  PHE A CZ  1 
ATOM   6152 N N   . TRP A 1 770 ? -16.203 12.057  32.036 1.00 14.39 ? 770  TRP A N   1 
ATOM   6153 C CA  . TRP A 1 770 ? -15.729 12.465  30.718 1.00 14.50 ? 770  TRP A CA  1 
ATOM   6154 C C   . TRP A 1 770 ? -14.439 13.269  30.902 1.00 15.09 ? 770  TRP A C   1 
ATOM   6155 O O   . TRP A 1 770 ? -14.388 14.214  31.675 1.00 15.69 ? 770  TRP A O   1 
ATOM   6156 C CB  . TRP A 1 770 ? -16.743 13.320  29.960 1.00 16.08 ? 770  TRP A CB  1 
ATOM   6157 C CG  . TRP A 1 770 ? -16.473 13.374  28.466 1.00 14.95 ? 770  TRP A CG  1 
ATOM   6158 C CD1 . TRP A 1 770 ? -15.909 14.427  27.758 1.00 16.76 ? 770  TRP A CD1 1 
ATOM   6159 C CD2 . TRP A 1 770 ? -16.744 12.347  27.500 1.00 19.15 ? 770  TRP A CD2 1 
ATOM   6160 N NE1 . TRP A 1 770 ? -15.823 14.099  26.429 1.00 15.95 ? 770  TRP A NE1 1 
ATOM   6161 C CE2 . TRP A 1 770 ? -16.333 12.839  26.238 1.00 17.63 ? 770  TRP A CE2 1 
ATOM   6162 C CE3 . TRP A 1 770 ? -17.275 11.045  27.580 1.00 19.52 ? 770  TRP A CE3 1 
ATOM   6163 C CZ2 . TRP A 1 770 ? -16.467 12.086  25.051 1.00 19.02 ? 770  TRP A CZ2 1 
ATOM   6164 C CZ3 . TRP A 1 770 ? -17.392 10.288  26.390 1.00 20.01 ? 770  TRP A CZ3 1 
ATOM   6165 C CH2 . TRP A 1 770 ? -16.997 10.820  25.150 1.00 17.96 ? 770  TRP A CH2 1 
ATOM   6166 N N   . ASP A 1 771 ? -13.401 12.812  30.240 1.00 14.83 ? 771  ASP A N   1 
ATOM   6167 C CA  . ASP A 1 771 ? -12.120 13.548  30.222 1.00 14.00 ? 771  ASP A CA  1 
ATOM   6168 C C   . ASP A 1 771 ? -11.628 13.506  28.791 1.00 14.38 ? 771  ASP A C   1 
ATOM   6169 O O   . ASP A 1 771 ? -12.388 13.154  27.886 1.00 14.58 ? 771  ASP A O   1 
ATOM   6170 C CB  . ASP A 1 771 ? -11.146 12.962  31.256 1.00 13.49 ? 771  ASP A CB  1 
ATOM   6171 C CG  . ASP A 1 771 ? -10.653 11.555  30.911 1.00 12.35 ? 771  ASP A CG  1 
ATOM   6172 O OD1 . ASP A 1 771 ? -11.081 10.943  29.918 1.00 14.23 ? 771  ASP A OD1 1 
ATOM   6173 O OD2 . ASP A 1 771 ? -9.752  11.095  31.647 1.00 14.71 ? 771  ASP A OD2 1 
ATOM   6174 N N   . ASP A 1 772 ? -10.351 13.833  28.552 1.00 14.77 ? 772  ASP A N   1 
ATOM   6175 C CA  . ASP A 1 772 ? -9.863  13.826  27.204 1.00 14.93 ? 772  ASP A CA  1 
ATOM   6176 C C   . ASP A 1 772 ? -9.529  12.439  26.613 1.00 14.34 ? 772  ASP A C   1 
ATOM   6177 O O   . ASP A 1 772 ? -9.151  12.358  25.471 1.00 15.10 ? 772  ASP A O   1 
ATOM   6178 C CB  . ASP A 1 772 ? -8.692  14.853  27.036 1.00 14.86 ? 772  ASP A CB  1 
ATOM   6179 C CG  . ASP A 1 772 ? -7.352  14.316  27.571 1.00 19.82 ? 772  ASP A CG  1 
ATOM   6180 O OD1 . ASP A 1 772 ? -7.301  13.126  27.968 1.00 17.41 ? 772  ASP A OD1 1 
ATOM   6181 O OD2 . ASP A 1 772 ? -6.371  15.102  27.646 1.00 18.81 ? 772  ASP A OD2 1 
ATOM   6182 N N   . GLY A 1 773 ? -9.709  11.360  27.366 1.00 14.31 ? 773  GLY A N   1 
ATOM   6183 C CA  . GLY A 1 773 ? -9.625  9.988   26.800 1.00 14.32 ? 773  GLY A CA  1 
ATOM   6184 C C   . GLY A 1 773 ? -8.197  9.481   26.640 1.00 15.79 ? 773  GLY A C   1 
ATOM   6185 O O   . GLY A 1 773 ? -7.997  8.365   26.203 1.00 14.89 ? 773  GLY A O   1 
ATOM   6186 N N   . GLU A 1 774 ? -7.203  10.296  26.988 1.00 15.33 ? 774  GLU A N   1 
ATOM   6187 C CA  . GLU A 1 774 ? -5.819  9.839   26.732 1.00 18.16 ? 774  GLU A CA  1 
ATOM   6188 C C   . GLU A 1 774 ? -4.706  10.343  27.628 1.00 18.10 ? 774  GLU A C   1 
ATOM   6189 O O   . GLU A 1 774 ? -3.647  9.687   27.703 1.00 17.57 ? 774  GLU A O   1 
ATOM   6190 C CB  . GLU A 1 774 ? -5.441  10.085  25.278 1.00 17.86 ? 774  GLU A CB  1 
ATOM   6191 C CG  . GLU A 1 774 ? -5.510  11.516  24.829 1.00 23.23 ? 774  GLU A CG  1 
ATOM   6192 C CD  . GLU A 1 774 ? -5.278  11.607  23.340 1.00 30.78 ? 774  GLU A CD  1 
ATOM   6193 O OE1 . GLU A 1 774 ? -6.209  11.262  22.589 1.00 34.36 ? 774  GLU A OE1 1 
ATOM   6194 O OE2 . GLU A 1 774 ? -4.160  11.990  22.928 1.00 31.77 ? 774  GLU A OE2 1 
ATOM   6195 N N   . THR A 1 775 ? -4.903  11.487  28.277 1.00 18.74 ? 775  THR A N   1 
ATOM   6196 C CA  . THR A 1 775 ? -3.821  12.049  29.130 1.00 20.97 ? 775  THR A CA  1 
ATOM   6197 C C   . THR A 1 775 ? -3.678  11.247  30.413 1.00 21.44 ? 775  THR A C   1 
ATOM   6198 O O   . THR A 1 775 ? -4.691  10.830  31.011 1.00 19.64 ? 775  THR A O   1 
ATOM   6199 C CB  . THR A 1 775 ? -4.044  13.551  29.432 1.00 21.18 ? 775  THR A CB  1 
ATOM   6200 O OG1 . THR A 1 775 ? -4.089  14.255  28.190 1.00 21.76 ? 775  THR A OG1 1 
ATOM   6201 C CG2 . THR A 1 775 ? -2.914  14.106  30.302 1.00 22.29 ? 775  THR A CG2 1 
ATOM   6202 N N   . LYS A 1 776 ? -2.431  10.961  30.800 1.00 22.08 ? 776  LYS A N   1 
ATOM   6203 C CA  . LYS A 1 776 ? -2.163  10.202  32.011 1.00 24.69 ? 776  LYS A CA  1 
ATOM   6204 C C   . LYS A 1 776 ? -2.431  11.096  33.235 1.00 25.62 ? 776  LYS A C   1 
ATOM   6205 O O   . LYS A 1 776 ? -2.182  12.291  33.192 1.00 25.93 ? 776  LYS A O   1 
ATOM   6206 C CB  . LYS A 1 776 ? -0.726  9.612   31.995 1.00 26.21 ? 776  LYS A CB  1 
ATOM   6207 C CG  . LYS A 1 776 ? -0.490  8.447   32.979 1.00 27.56 ? 776  LYS A CG  1 
ATOM   6208 C CD  . LYS A 1 776 ? 0.884   7.782   32.765 1.00 26.91 ? 776  LYS A CD  1 
ATOM   6209 C CE  . LYS A 1 776 ? 0.775   6.539   31.887 1.00 29.61 ? 776  LYS A CE  1 
ATOM   6210 N NZ  . LYS A 1 776 ? 1.951   5.592   31.959 1.00 32.96 ? 776  LYS A NZ  1 
ATOM   6211 N N   . ASP A 1 777 ? -3.006  10.525  34.292 1.00 26.56 ? 777  ASP A N   1 
ATOM   6212 C CA  . ASP A 1 777 ? -3.210  11.243  35.571 1.00 27.50 ? 777  ASP A CA  1 
ATOM   6213 C C   . ASP A 1 777 ? -4.343  12.308  35.556 1.00 26.24 ? 777  ASP A C   1 
ATOM   6214 O O   . ASP A 1 777 ? -4.384  13.173  36.422 1.00 26.81 ? 777  ASP A O   1 
ATOM   6215 C CB  . ASP A 1 777 ? -1.900  11.891  36.060 1.00 28.84 ? 777  ASP A CB  1 
ATOM   6216 C CG  . ASP A 1 777 ? -0.851  10.875  36.509 1.00 33.55 ? 777  ASP A CG  1 
ATOM   6217 O OD1 . ASP A 1 777 ? -1.201  9.700   36.788 1.00 37.47 ? 777  ASP A OD1 1 
ATOM   6218 O OD2 . ASP A 1 777 ? 0.339   11.270  36.602 1.00 37.39 ? 777  ASP A OD2 1 
ATOM   6219 N N   . THR A 1 778 ? -5.252  12.252  34.585 1.00 24.70 ? 778  THR A N   1 
ATOM   6220 C CA  . THR A 1 778 ? -6.360  13.218  34.556 1.00 23.18 ? 778  THR A CA  1 
ATOM   6221 C C   . THR A 1 778 ? -7.245  13.073  35.788 1.00 22.10 ? 778  THR A C   1 
ATOM   6222 O O   . THR A 1 778 ? -7.888  14.051  36.209 1.00 22.06 ? 778  THR A O   1 
ATOM   6223 C CB  . THR A 1 778 ? -7.273  13.070  33.320 1.00 23.18 ? 778  THR A CB  1 
ATOM   6224 O OG1 . THR A 1 778 ? -7.786  11.746  33.292 1.00 24.68 ? 778  THR A OG1 1 
ATOM   6225 C CG2 . THR A 1 778 ? -6.535  13.356  32.021 1.00 22.19 ? 778  THR A CG2 1 
ATOM   6226 N N   . VAL A 1 779 ? -7.293  11.866  36.349 1.00 20.62 ? 779  VAL A N   1 
ATOM   6227 C CA  . VAL A 1 779 ? -8.100  11.606  37.534 1.00 21.72 ? 779  VAL A CA  1 
ATOM   6228 C C   . VAL A 1 779 ? -7.360  12.109  38.781 1.00 22.39 ? 779  VAL A C   1 
ATOM   6229 O O   . VAL A 1 779 ? -7.882  12.908  39.563 1.00 21.56 ? 779  VAL A O   1 
ATOM   6230 C CB  . VAL A 1 779 ? -8.517  10.116  37.630 1.00 21.08 ? 779  VAL A CB  1 
ATOM   6231 C CG1 . VAL A 1 779 ? -9.182  9.823   38.942 1.00 22.54 ? 779  VAL A CG1 1 
ATOM   6232 C CG2 . VAL A 1 779 ? -9.416  9.731   36.469 1.00 21.75 ? 779  VAL A CG2 1 
ATOM   6233 N N   . ALA A 1 780 ? -6.113  11.679  38.936 1.00 23.87 ? 780  ALA A N   1 
ATOM   6234 C CA  . ALA A 1 780 ? -5.287  12.170  40.029 1.00 25.42 ? 780  ALA A CA  1 
ATOM   6235 C C   . ALA A 1 780 ? -5.141  13.704  40.023 1.00 26.04 ? 780  ALA A C   1 
ATOM   6236 O O   . ALA A 1 780 ? -5.190  14.335  41.077 1.00 27.04 ? 780  ALA A O   1 
ATOM   6237 C CB  . ALA A 1 780 ? -3.903  11.460  40.017 1.00 26.10 ? 780  ALA A CB  1 
ATOM   6238 N N   . ASN A 1 781 ? -5.015  14.316  38.849 1.00 26.88 ? 781  ASN A N   1 
ATOM   6239 C CA  . ASN A 1 781 ? -4.874  15.774  38.752 1.00 27.86 ? 781  ASN A CA  1 
ATOM   6240 C C   . ASN A 1 781 ? -6.203  16.524  38.638 1.00 27.29 ? 781  ASN A C   1 
ATOM   6241 O O   . ASN A 1 781 ? -6.231  17.738  38.483 1.00 28.03 ? 781  ASN A O   1 
ATOM   6242 C CB  . ASN A 1 781 ? -3.930  16.141  37.614 1.00 28.61 ? 781  ASN A CB  1 
ATOM   6243 C CG  . ASN A 1 781 ? -2.543  15.616  37.854 1.00 31.81 ? 781  ASN A CG  1 
ATOM   6244 O OD1 . ASN A 1 781 ? -1.864  15.139  36.939 1.00 34.49 ? 781  ASN A OD1 1 
ATOM   6245 N ND2 . ASN A 1 781 ? -2.129  15.649  39.109 1.00 30.83 ? 781  ASN A ND2 1 
ATOM   6246 N N   . LYS A 1 782 ? -7.297  15.778  38.716 1.00 26.33 ? 782  LYS A N   1 
ATOM   6247 C CA  . LYS A 1 782 ? -8.667  16.350  38.695 1.00 25.76 ? 782  LYS A CA  1 
ATOM   6248 C C   . LYS A 1 782 ? -9.016  17.246  37.506 1.00 24.64 ? 782  LYS A C   1 
ATOM   6249 O O   . LYS A 1 782 ? -9.539  18.361  37.682 1.00 24.62 ? 782  LYS A O   1 
ATOM   6250 C CB  . LYS A 1 782 ? -8.968  17.089  40.004 1.00 26.56 ? 782  LYS A CB  1 
ATOM   6251 C CG  . LYS A 1 782 ? -8.849  16.258  41.234 1.00 27.67 ? 782  LYS A CG  1 
ATOM   6252 C CD  . LYS A 1 782 ? -10.176 15.567  41.494 1.00 35.46 ? 782  LYS A CD  1 
ATOM   6253 C CE  . LYS A 1 782 ? -10.278 15.095  42.946 1.00 38.31 ? 782  LYS A CE  1 
ATOM   6254 N NZ  . LYS A 1 782 ? -11.184 13.904  43.035 1.00 40.94 ? 782  LYS A NZ  1 
ATOM   6255 N N   . VAL A 1 783 ? -8.753  16.739  36.307 1.00 22.08 ? 783  VAL A N   1 
ATOM   6256 C CA  . VAL A 1 783 ? -9.115  17.383  35.055 1.00 21.04 ? 783  VAL A CA  1 
ATOM   6257 C C   . VAL A 1 783 ? -10.142 16.452  34.416 1.00 19.54 ? 783  VAL A C   1 
ATOM   6258 O O   . VAL A 1 783 ? -9.845  15.631  33.548 1.00 18.94 ? 783  VAL A O   1 
ATOM   6259 C CB  . VAL A 1 783 ? -7.863  17.646  34.134 1.00 20.60 ? 783  VAL A CB  1 
ATOM   6260 C CG1 . VAL A 1 783 ? -8.242  18.412  32.897 1.00 21.60 ? 783  VAL A CG1 1 
ATOM   6261 C CG2 . VAL A 1 783 ? -6.779  18.433  34.909 1.00 23.21 ? 783  VAL A CG2 1 
ATOM   6262 N N   . TYR A 1 784 ? -11.388 16.566  34.871 1.00 17.73 ? 784  TYR A N   1 
ATOM   6263 C CA  . TYR A 1 784 ? -12.407 15.740  34.274 1.00 16.87 ? 784  TYR A CA  1 
ATOM   6264 C C   . TYR A 1 784 ? -13.771 16.273  34.634 1.00 15.62 ? 784  TYR A C   1 
ATOM   6265 O O   . TYR A 1 784 ? -13.888 17.108  35.522 1.00 16.60 ? 784  TYR A O   1 
ATOM   6266 C CB  . TYR A 1 784 ? -12.305 14.291  34.740 1.00 16.51 ? 784  TYR A CB  1 
ATOM   6267 C CG  . TYR A 1 784 ? -12.465 13.973  36.240 1.00 17.99 ? 784  TYR A CG  1 
ATOM   6268 C CD1 . TYR A 1 784 ? -13.707 13.619  36.805 1.00 17.32 ? 784  TYR A CD1 1 
ATOM   6269 C CD2 . TYR A 1 784 ? -11.352 13.921  37.065 1.00 17.99 ? 784  TYR A CD2 1 
ATOM   6270 C CE1 . TYR A 1 784 ? -13.807 13.274  38.170 1.00 20.03 ? 784  TYR A CE1 1 
ATOM   6271 C CE2 . TYR A 1 784 ? -11.442 13.580  38.402 1.00 18.48 ? 784  TYR A CE2 1 
ATOM   6272 C CZ  . TYR A 1 784 ? -12.674 13.257  38.947 1.00 21.16 ? 784  TYR A CZ  1 
ATOM   6273 O OH  . TYR A 1 784 ? -12.702 12.916  40.266 1.00 20.52 ? 784  TYR A OH  1 
ATOM   6274 N N   . LEU A 1 785 ? -14.764 15.753  33.940 1.00 16.12 ? 785  LEU A N   1 
ATOM   6275 C CA  . LEU A 1 785 ? -16.175 16.091  34.200 1.00 16.43 ? 785  LEU A CA  1 
ATOM   6276 C C   . LEU A 1 785 ? -16.768 14.835  34.808 1.00 16.57 ? 785  LEU A C   1 
ATOM   6277 O O   . LEU A 1 785 ? -16.478 13.725  34.338 1.00 16.11 ? 785  LEU A O   1 
ATOM   6278 C CB  . LEU A 1 785 ? -16.882 16.399  32.884 1.00 17.30 ? 785  LEU A CB  1 
ATOM   6279 C CG  . LEU A 1 785 ? -18.436 16.453  32.853 1.00 19.37 ? 785  LEU A CG  1 
ATOM   6280 C CD1 . LEU A 1 785 ? -19.020 17.497  33.772 1.00 22.47 ? 785  LEU A CD1 1 
ATOM   6281 C CD2 . LEU A 1 785 ? -18.874 16.686  31.455 1.00 24.34 ? 785  LEU A CD2 1 
ATOM   6282 N N   . LEU A 1 786 ? -17.572 14.984  35.862 1.00 16.18 ? 786  LEU A N   1 
ATOM   6283 C CA  . LEU A 1 786 ? -18.348 13.868  36.361 1.00 16.43 ? 786  LEU A CA  1 
ATOM   6284 C C   . LEU A 1 786 ? -19.740 14.436  36.600 1.00 17.16 ? 786  LEU A C   1 
ATOM   6285 O O   . LEU A 1 786 ? -19.892 15.406  37.338 1.00 18.38 ? 786  LEU A O   1 
ATOM   6286 C CB  . LEU A 1 786 ? -17.765 13.309  37.655 1.00 16.26 ? 786  LEU A CB  1 
ATOM   6287 C CG  . LEU A 1 786 ? -18.468 12.106  38.297 1.00 15.87 ? 786  LEU A CG  1 
ATOM   6288 C CD1 . LEU A 1 786 ? -18.488 10.887  37.353 1.00 18.57 ? 786  LEU A CD1 1 
ATOM   6289 C CD2 . LEU A 1 786 ? -17.892 11.806  39.663 1.00 17.32 ? 786  LEU A CD2 1 
ATOM   6290 N N   . CYS A 1 787 ? -20.743 13.869  35.959 1.00 18.24 ? 787  CYS A N   1 
ATOM   6291 C CA  . CYS A 1 787 ? -22.102 14.349  36.249 1.00 19.22 ? 787  CYS A CA  1 
ATOM   6292 C C   . CYS A 1 787 ? -22.985 13.207  36.689 1.00 18.89 ? 787  CYS A C   1 
ATOM   6293 O O   . CYS A 1 787 ? -22.663 12.060  36.471 1.00 16.19 ? 787  CYS A O   1 
ATOM   6294 C CB  . CYS A 1 787 ? -22.727 15.027  35.070 1.00 21.03 ? 787  CYS A CB  1 
ATOM   6295 S SG  . CYS A 1 787 ? -22.523 14.303  33.515 1.00 30.58 ? 787  CYS A SG  1 
ATOM   6296 N N   . GLU A 1 788 ? -24.119 13.551  37.290 1.00 17.97 ? 788  GLU A N   1 
ATOM   6297 C CA  . GLU A 1 788 ? -24.983 12.559  37.889 1.00 18.42 ? 788  GLU A CA  1 
ATOM   6298 C C   . GLU A 1 788 ? -26.323 12.825  37.291 1.00 17.70 ? 788  GLU A C   1 
ATOM   6299 O O   . GLU A 1 788 ? -26.689 13.996  37.087 1.00 19.47 ? 788  GLU A O   1 
ATOM   6300 C CB  . GLU A 1 788 ? -25.062 12.738  39.411 1.00 19.61 ? 788  GLU A CB  1 
ATOM   6301 C CG  . GLU A 1 788 ? -23.785 12.381  40.111 1.00 26.01 ? 788  GLU A CG  1 
ATOM   6302 C CD  . GLU A 1 788 ? -22.886 13.576  40.261 1.00 33.43 ? 788  GLU A CD  1 
ATOM   6303 O OE1 . GLU A 1 788 ? -21.671 13.428  39.971 1.00 33.75 ? 788  GLU A OE1 1 
ATOM   6304 O OE2 . GLU A 1 788 ? -23.394 14.672  40.670 1.00 35.32 ? 788  GLU A OE2 1 
ATOM   6305 N N   . PHE A 1 789 ? -27.035 11.753  36.993 1.00 16.94 ? 789  PHE A N   1 
ATOM   6306 C CA  . PHE A 1 789 ? -28.397 11.828  36.427 1.00 16.05 ? 789  PHE A CA  1 
ATOM   6307 C C   . PHE A 1 789 ? -29.325 11.198  37.430 1.00 17.09 ? 789  PHE A C   1 
ATOM   6308 O O   . PHE A 1 789 ? -29.008 10.154  38.005 1.00 16.80 ? 789  PHE A O   1 
ATOM   6309 C CB  . PHE A 1 789 ? -28.477 11.000  35.140 1.00 15.94 ? 789  PHE A CB  1 
ATOM   6310 C CG  . PHE A 1 789 ? -27.372 11.304  34.140 1.00 18.73 ? 789  PHE A CG  1 
ATOM   6311 C CD1 . PHE A 1 789 ? -27.242 12.583  33.575 1.00 18.64 ? 789  PHE A CD1 1 
ATOM   6312 C CD2 . PHE A 1 789 ? -26.469 10.298  33.765 1.00 18.98 ? 789  PHE A CD2 1 
ATOM   6313 C CE1 . PHE A 1 789 ? -26.211 12.872  32.643 1.00 20.91 ? 789  PHE A CE1 1 
ATOM   6314 C CE2 . PHE A 1 789 ? -25.434 10.572  32.824 1.00 20.23 ? 789  PHE A CE2 1 
ATOM   6315 C CZ  . PHE A 1 789 ? -25.310 11.852  32.276 1.00 20.16 ? 789  PHE A CZ  1 
ATOM   6316 N N   . SER A 1 790 ? -30.493 11.807  37.649 1.00 17.33 ? 790  SER A N   1 
ATOM   6317 C CA  . SER A 1 790 ? -31.481 11.147  38.493 1.00 19.23 ? 790  SER A CA  1 
ATOM   6318 C C   . SER A 1 790 ? -32.855 11.506  38.010 1.00 18.91 ? 790  SER A C   1 
ATOM   6319 O O   . SER A 1 790 ? -33.092 12.635  37.617 1.00 18.86 ? 790  SER A O   1 
ATOM   6320 C CB  . SER A 1 790 ? -31.338 11.475  39.983 1.00 20.16 ? 790  SER A CB  1 
ATOM   6321 O OG  . SER A 1 790 ? -31.325 12.867  40.223 1.00 25.53 ? 790  SER A OG  1 
ATOM   6322 N N   . VAL A 1 791 ? -33.748 10.538  38.102 1.00 20.97 ? 791  VAL A N   1 
ATOM   6323 C CA  . VAL A 1 791 ? -35.125 10.680  37.682 1.00 22.34 ? 791  VAL A CA  1 
ATOM   6324 C C   . VAL A 1 791 ? -35.974 10.237  38.881 1.00 24.44 ? 791  VAL A C   1 
ATOM   6325 O O   . VAL A 1 791 ? -35.798 9.149   39.398 1.00 22.05 ? 791  VAL A O   1 
ATOM   6326 C CB  . VAL A 1 791 ? -35.400 9.812   36.428 1.00 22.35 ? 791  VAL A CB  1 
ATOM   6327 C CG1 . VAL A 1 791 ? -36.926 9.722   36.123 1.00 24.47 ? 791  VAL A CG1 1 
ATOM   6328 C CG2 . VAL A 1 791 ? -34.614 10.337  35.230 1.00 22.53 ? 791  VAL A CG2 1 
ATOM   6329 N N   . THR A 1 792 ? -36.830 11.132  39.364 1.00 26.84 ? 792  THR A N   1 
ATOM   6330 C CA  . THR A 1 792 ? -37.743 10.824  40.472 1.00 30.61 ? 792  THR A CA  1 
ATOM   6331 C C   . THR A 1 792 ? -38.917 11.636  40.120 1.00 31.79 ? 792  THR A C   1 
ATOM   6332 O O   . THR A 1 792 ? -38.766 12.860  39.912 1.00 31.43 ? 792  THR A O   1 
ATOM   6333 C CB  . THR A 1 792 ? -37.329 11.370  41.830 1.00 30.07 ? 792  THR A CB  1 
ATOM   6334 O OG1 . THR A 1 792 ? -35.908 11.457  41.944 1.00 37.00 ? 792  THR A OG1 1 
ATOM   6335 C CG2 . THR A 1 792 ? -37.887 10.479  42.920 1.00 32.84 ? 792  THR A CG2 1 
ATOM   6336 N N   . GLN A 1 793 ? -40.064 10.953  40.154 1.00 33.37 ? 793  GLN A N   1 
ATOM   6337 C CA  . GLN A 1 793 ? -41.223 11.151  39.272 1.00 35.33 ? 793  GLN A CA  1 
ATOM   6338 C C   . GLN A 1 793 ? -41.388 12.514  38.593 1.00 33.51 ? 793  GLN A C   1 
ATOM   6339 O O   . GLN A 1 793 ? -41.276 13.575  39.222 1.00 34.48 ? 793  GLN A O   1 
ATOM   6340 C CB  . GLN A 1 793 ? -42.522 10.587  39.905 1.00 35.43 ? 793  GLN A CB  1 
ATOM   6341 C CG  . GLN A 1 793 ? -42.300 9.140   40.454 1.00 38.95 ? 793  GLN A CG  1 
ATOM   6342 C CD  . GLN A 1 793 ? -43.573 8.320   40.645 1.00 39.61 ? 793  GLN A CD  1 
ATOM   6343 O OE1 . GLN A 1 793 ? -44.167 7.814   39.673 1.00 45.66 ? 793  GLN A OE1 1 
ATOM   6344 N NE2 . GLN A 1 793 ? -43.966 8.131   41.903 1.00 42.58 ? 793  GLN A NE2 1 
ATOM   6345 N N   . ASN A 1 794 ? -41.591 12.452  37.277 1.00 31.66 ? 794  ASN A N   1 
ATOM   6346 C CA  . ASN A 1 794 ? -41.870 13.634  36.460 1.00 30.81 ? 794  ASN A CA  1 
ATOM   6347 C C   . ASN A 1 794 ? -40.610 14.469  36.186 1.00 27.94 ? 794  ASN A C   1 
ATOM   6348 O O   . ASN A 1 794 ? -40.742 15.550  35.644 1.00 26.69 ? 794  ASN A O   1 
ATOM   6349 C CB  . ASN A 1 794 ? -42.894 14.599  37.132 1.00 31.72 ? 794  ASN A CB  1 
ATOM   6350 C CG  . ASN A 1 794 ? -44.252 13.947  37.439 1.00 36.15 ? 794  ASN A CG  1 
ATOM   6351 O OD1 . ASN A 1 794 ? -44.571 13.675  38.607 1.00 40.34 ? 794  ASN A OD1 1 
ATOM   6352 N ND2 . ASN A 1 794 ? -45.068 13.735  36.400 1.00 36.10 ? 794  ASN A ND2 1 
ATOM   6353 N N   . ARG A 1 795 ? -39.418 14.031  36.618 1.00 25.66 ? 795  ARG A N   1 
ATOM   6354 C CA  . ARG A 1 795 ? -38.277 14.967  36.604 1.00 24.33 ? 795  ARG A CA  1 
ATOM   6355 C C   . ARG A 1 795 ? -36.917 14.282  36.421 1.00 23.05 ? 795  ARG A C   1 
ATOM   6356 O O   . ARG A 1 795 ? -36.585 13.438  37.223 1.00 22.78 ? 795  ARG A O   1 
ATOM   6357 C CB  . ARG A 1 795 ? -38.269 15.748  37.913 1.00 24.20 ? 795  ARG A CB  1 
ATOM   6358 C CG  . ARG A 1 795 ? -37.239 16.852  38.079 1.00 26.41 ? 795  ARG A CG  1 
ATOM   6359 C CD  . ARG A 1 795 ? -37.469 17.565  39.405 1.00 27.22 ? 795  ARG A CD  1 
ATOM   6360 N NE  . ARG A 1 795 ? -36.532 18.667  39.634 1.00 36.54 ? 795  ARG A NE  1 
ATOM   6361 C CZ  . ARG A 1 795 ? -36.879 19.901  40.010 1.00 39.39 ? 795  ARG A CZ  1 
ATOM   6362 N NH1 . ARG A 1 795 ? -38.164 20.209  40.204 1.00 42.78 ? 795  ARG A NH1 1 
ATOM   6363 N NH2 . ARG A 1 795 ? -35.940 20.837  40.202 1.00 40.39 ? 795  ARG A NH2 1 
ATOM   6364 N N   . LEU A 1 796 ? -36.146 14.699  35.416 1.00 20.47 ? 796  LEU A N   1 
ATOM   6365 C CA  . LEU A 1 796 ? -34.739 14.272  35.286 1.00 20.01 ? 796  LEU A CA  1 
ATOM   6366 C C   . LEU A 1 796 ? -33.901 15.443  35.735 1.00 19.65 ? 796  LEU A C   1 
ATOM   6367 O O   . LEU A 1 796 ? -34.141 16.582  35.312 1.00 19.78 ? 796  LEU A O   1 
ATOM   6368 C CB  . LEU A 1 796 ? -34.410 13.900  33.827 1.00 19.89 ? 796  LEU A CB  1 
ATOM   6369 C CG  . LEU A 1 796 ? -32.953 13.989  33.377 1.00 19.80 ? 796  LEU A CG  1 
ATOM   6370 C CD1 . LEU A 1 796 ? -32.157 12.830  34.018 1.00 15.91 ? 796  LEU A CD1 1 
ATOM   6371 C CD2 . LEU A 1 796 ? -32.836 13.955  31.850 1.00 19.30 ? 796  LEU A CD2 1 
ATOM   6372 N N   . GLU A 1 797 ? -32.935 15.199  36.609 1.00 20.54 ? 797  GLU A N   1 
ATOM   6373 C CA  . GLU A 1 797 ? -31.958 16.218  36.957 1.00 22.08 ? 797  GLU A CA  1 
ATOM   6374 C C   . GLU A 1 797 ? -30.612 15.784  36.413 1.00 21.36 ? 797  GLU A C   1 
ATOM   6375 O O   . GLU A 1 797 ? -30.262 14.598  36.509 1.00 20.17 ? 797  GLU A O   1 
ATOM   6376 C CB  . GLU A 1 797 ? -31.880 16.418  38.484 1.00 22.26 ? 797  GLU A CB  1 
ATOM   6377 C CG  . GLU A 1 797 ? -33.164 16.981  39.096 1.00 27.35 ? 797  GLU A CG  1 
ATOM   6378 C CD  . GLU A 1 797 ? -33.272 16.773  40.599 1.00 29.05 ? 797  GLU A CD  1 
ATOM   6379 O OE1 . GLU A 1 797 ? -32.215 16.717  41.303 1.00 38.54 ? 797  GLU A OE1 1 
ATOM   6380 O OE2 . GLU A 1 797 ? -34.432 16.680  41.083 1.00 39.18 ? 797  GLU A OE2 1 
ATOM   6381 N N   . VAL A 1 798 ? -29.890 16.731  35.804 1.00 21.60 ? 798  VAL A N   1 
ATOM   6382 C CA  . VAL A 1 798 ? -28.473 16.525  35.432 1.00 22.14 ? 798  VAL A CA  1 
ATOM   6383 C C   . VAL A 1 798 ? -27.680 17.441  36.354 1.00 22.27 ? 798  VAL A C   1 
ATOM   6384 O O   . VAL A 1 798 ? -27.873 18.650  36.345 1.00 21.68 ? 798  VAL A O   1 
ATOM   6385 C CB  . VAL A 1 798 ? -28.212 16.841  33.917 1.00 22.11 ? 798  VAL A CB  1 
ATOM   6386 C CG1 . VAL A 1 798 ? -26.778 16.513  33.529 1.00 22.00 ? 798  VAL A CG1 1 
ATOM   6387 C CG2 . VAL A 1 798 ? -29.158 16.078  33.043 1.00 22.88 ? 798  VAL A CG2 1 
ATOM   6388 N N   . ASN A 1 799 ? -26.828 16.849  37.185 1.00 23.16 ? 799  ASN A N   1 
ATOM   6389 C CA  . ASN A 1 799 ? -26.158 17.503  38.279 1.00 24.58 ? 799  ASN A CA  1 
ATOM   6390 C C   . ASN A 1 799 ? -24.651 17.329  38.070 1.00 24.95 ? 799  ASN A C   1 
ATOM   6391 O O   . ASN A 1 799 ? -24.187 16.229  37.748 1.00 25.09 ? 799  ASN A O   1 
ATOM   6392 C CB  . ASN A 1 799 ? -26.596 16.787  39.564 1.00 26.20 ? 799  ASN A CB  1 
ATOM   6393 C CG  . ASN A 1 799 ? -26.353 17.600  40.813 1.00 30.94 ? 799  ASN A CG  1 
ATOM   6394 O OD1 . ASN A 1 799 ? -25.281 18.199  40.997 1.00 38.91 ? 799  ASN A OD1 1 
ATOM   6395 N ND2 . ASN A 1 799 ? -27.335 17.603  41.710 1.00 35.25 ? 799  ASN A ND2 1 
ATOM   6396 N N   . ILE A 1 800 ? -23.887 18.398  38.222 1.00 24.10 ? 800  ILE A N   1 
ATOM   6397 C CA  . ILE A 1 800 ? -22.459 18.327  37.943 1.00 24.05 ? 800  ILE A CA  1 
ATOM   6398 C C   . ILE A 1 800 ? -21.683 18.250  39.250 1.00 23.82 ? 800  ILE A C   1 
ATOM   6399 O O   . ILE A 1 800 ? -21.780 19.140  40.086 1.00 23.27 ? 800  ILE A O   1 
ATOM   6400 C CB  . ILE A 1 800 ? -21.986 19.562  37.136 1.00 24.44 ? 800  ILE A CB  1 
ATOM   6401 C CG1 . ILE A 1 800 ? -22.952 19.889  35.985 1.00 23.99 ? 800  ILE A CG1 1 
ATOM   6402 C CG2 . ILE A 1 800 ? -20.585 19.367  36.632 1.00 23.51 ? 800  ILE A CG2 1 
ATOM   6403 C CD1 . ILE A 1 800 ? -23.202 18.755  34.959 1.00 27.22 ? 800  ILE A CD1 1 
ATOM   6404 N N   . SER A 1 801 ? -20.907 17.190  39.436 1.00 23.46 ? 801  SER A N   1 
ATOM   6405 C CA  . SER A 1 801 ? -20.142 17.073  40.653 1.00 24.91 ? 801  SER A CA  1 
ATOM   6406 C C   . SER A 1 801 ? -18.668 17.502  40.483 1.00 25.02 ? 801  SER A C   1 
ATOM   6407 O O   . SER A 1 801 ? -18.095 18.024  41.409 1.00 26.80 ? 801  SER A O   1 
ATOM   6408 C CB  . SER A 1 801 ? -20.267 15.670  41.250 1.00 25.83 ? 801  SER A CB  1 
ATOM   6409 O OG  . SER A 1 801 ? -19.374 14.742  40.655 1.00 28.53 ? 801  SER A OG  1 
ATOM   6410 N N   . GLN A 1 802 ? -18.082 17.302  39.305 1.00 24.28 ? 802  GLN A N   1 
ATOM   6411 C CA  . GLN A 1 802 ? -16.696 17.763  39.021 1.00 23.73 ? 802  GLN A CA  1 
ATOM   6412 C C   . GLN A 1 802 ? -16.780 18.345  37.648 1.00 23.66 ? 802  GLN A C   1 
ATOM   6413 O O   . GLN A 1 802 ? -17.415 17.775  36.757 1.00 22.36 ? 802  GLN A O   1 
ATOM   6414 C CB  . GLN A 1 802 ? -15.692 16.605  39.060 1.00 24.11 ? 802  GLN A CB  1 
ATOM   6415 C CG  . GLN A 1 802 ? -14.193 16.978  38.751 1.00 24.81 ? 802  GLN A CG  1 
ATOM   6416 C CD  . GLN A 1 802 ? -13.518 17.734  39.872 1.00 28.87 ? 802  GLN A CD  1 
ATOM   6417 O OE1 . GLN A 1 802 ? -12.647 18.593  39.641 1.00 31.52 ? 802  GLN A OE1 1 
ATOM   6418 N NE2 . GLN A 1 802 ? -13.913 17.440  41.088 1.00 27.43 ? 802  GLN A NE2 1 
ATOM   6419 N N   . SER A 1 803 ? -16.175 19.509  37.468 1.00 23.65 ? 803  SER A N   1 
ATOM   6420 C CA  . SER A 1 803 ? -16.341 20.233  36.241 1.00 25.08 ? 803  SER A CA  1 
ATOM   6421 C C   . SER A 1 803 ? -15.027 20.920  35.902 1.00 25.36 ? 803  SER A C   1 
ATOM   6422 O O   . SER A 1 803 ? -14.943 22.144  35.835 1.00 26.22 ? 803  SER A O   1 
ATOM   6423 C CB  . SER A 1 803 ? -17.479 21.251  36.418 1.00 26.08 ? 803  SER A CB  1 
ATOM   6424 O OG  . SER A 1 803 ? -17.355 22.262  35.461 1.00 29.41 ? 803  SER A OG  1 
ATOM   6425 N N   . THR A 1 804 ? -13.978 20.126  35.730 1.00 24.16 ? 804  THR A N   1 
ATOM   6426 C CA  . THR A 1 804 ? -12.678 20.710  35.432 1.00 23.92 ? 804  THR A CA  1 
ATOM   6427 C C   . THR A 1 804 ? -12.138 20.319  34.062 1.00 23.43 ? 804  THR A C   1 
ATOM   6428 O O   . THR A 1 804 ? -10.978 20.590  33.745 1.00 24.45 ? 804  THR A O   1 
ATOM   6429 C CB  . THR A 1 804 ? -11.661 20.403  36.530 1.00 23.10 ? 804  THR A CB  1 
ATOM   6430 O OG1 . THR A 1 804 ? -11.722 19.012  36.856 1.00 21.90 ? 804  THR A OG1 1 
ATOM   6431 C CG2 . THR A 1 804 ? -11.951 21.234  37.774 1.00 23.32 ? 804  THR A CG2 1 
ATOM   6432 N N   . TYR A 1 805 ? -12.988 19.712  33.239 1.00 22.56 ? 805  TYR A N   1 
ATOM   6433 C CA  . TYR A 1 805 ? -12.656 19.466  31.867 1.00 22.58 ? 805  TYR A CA  1 
ATOM   6434 C C   . TYR A 1 805 ? -13.820 19.839  30.967 1.00 22.78 ? 805  TYR A C   1 
ATOM   6435 O O   . TYR A 1 805 ? -14.939 19.343  31.151 1.00 22.96 ? 805  TYR A O   1 
ATOM   6436 C CB  . TYR A 1 805 ? -12.295 17.987  31.611 1.00 21.38 ? 805  TYR A CB  1 
ATOM   6437 C CG  . TYR A 1 805 ? -11.955 17.748  30.163 1.00 20.94 ? 805  TYR A CG  1 
ATOM   6438 C CD1 . TYR A 1 805 ? -10.761 18.275  29.604 1.00 19.50 ? 805  TYR A CD1 1 
ATOM   6439 C CD2 . TYR A 1 805 ? -12.817 17.041  29.336 1.00 19.30 ? 805  TYR A CD2 1 
ATOM   6440 C CE1 . TYR A 1 805 ? -10.463 18.074  28.279 1.00 20.01 ? 805  TYR A CE1 1 
ATOM   6441 C CE2 . TYR A 1 805 ? -12.539 16.857  28.002 1.00 20.65 ? 805  TYR A CE2 1 
ATOM   6442 C CZ  . TYR A 1 805 ? -11.354 17.347  27.488 1.00 21.11 ? 805  TYR A CZ  1 
ATOM   6443 O OH  . TYR A 1 805 ? -11.102 17.147  26.177 1.00 19.36 ? 805  TYR A OH  1 
ATOM   6444 N N   . LYS A 1 806 ? -13.566 20.664  29.967 1.00 22.14 ? 806  LYS A N   1 
ATOM   6445 C CA  . LYS A 1 806 ? -14.640 20.924  29.020 1.00 23.10 ? 806  LYS A CA  1 
ATOM   6446 C C   . LYS A 1 806 ? -14.200 20.538  27.634 1.00 22.00 ? 806  LYS A C   1 
ATOM   6447 O O   . LYS A 1 806 ? -13.279 21.126  27.057 1.00 21.58 ? 806  LYS A O   1 
ATOM   6448 C CB  . LYS A 1 806 ? -15.169 22.367  29.091 1.00 24.21 ? 806  LYS A CB  1 
ATOM   6449 C CG  . LYS A 1 806 ? -16.359 22.582  28.139 1.00 26.31 ? 806  LYS A CG  1 
ATOM   6450 C CD  . LYS A 1 806 ? -17.383 23.541  28.707 1.00 30.98 ? 806  LYS A CD  1 
ATOM   6451 C CE  . LYS A 1 806 ? -18.596 23.628  27.783 1.00 31.57 ? 806  LYS A CE  1 
ATOM   6452 N NZ  . LYS A 1 806 ? -19.496 24.728  28.203 1.00 36.14 ? 806  LYS A NZ  1 
ATOM   6453 N N   . ASP A 1 807 ? -14.876 19.530  27.100 1.00 20.10 ? 807  ASP A N   1 
ATOM   6454 C CA  . ASP A 1 807 ? -14.582 19.003  25.778 1.00 19.49 ? 807  ASP A CA  1 
ATOM   6455 C C   . ASP A 1 807 ? -14.777 20.053  24.687 1.00 19.77 ? 807  ASP A C   1 
ATOM   6456 O O   . ASP A 1 807 ? -15.834 20.684  24.608 1.00 17.00 ? 807  ASP A O   1 
ATOM   6457 C CB  . ASP A 1 807 ? -15.501 17.803  25.512 1.00 20.53 ? 807  ASP A CB  1 
ATOM   6458 C CG  . ASP A 1 807 ? -15.064 16.993  24.308 1.00 22.99 ? 807  ASP A CG  1 
ATOM   6459 O OD1 . ASP A 1 807 ? -15.126 17.533  23.193 1.00 25.87 ? 807  ASP A OD1 1 
ATOM   6460 O OD2 . ASP A 1 807 ? -14.667 15.825  24.480 1.00 23.40 ? 807  ASP A OD2 1 
ATOM   6461 N N   . PRO A 1 808 ? -13.746 20.266  23.836 1.00 20.16 ? 808  PRO A N   1 
ATOM   6462 C CA  . PRO A 1 808 ? -13.879 21.337  22.837 1.00 20.30 ? 808  PRO A CA  1 
ATOM   6463 C C   . PRO A 1 808 ? -14.858 21.085  21.664 1.00 20.97 ? 808  PRO A C   1 
ATOM   6464 O O   . PRO A 1 808 ? -15.079 21.975  20.832 1.00 21.11 ? 808  PRO A O   1 
ATOM   6465 C CB  . PRO A 1 808 ? -12.431 21.517  22.339 1.00 20.94 ? 808  PRO A CB  1 
ATOM   6466 C CG  . PRO A 1 808 ? -11.807 20.125  22.474 1.00 20.44 ? 808  PRO A CG  1 
ATOM   6467 C CD  . PRO A 1 808 ? -12.425 19.593  23.783 1.00 20.65 ? 808  PRO A CD  1 
ATOM   6468 N N   . ASN A 1 809 ? -15.427 19.885  21.584 1.00 19.60 ? 809  ASN A N   1 
ATOM   6469 C CA  . ASN A 1 809 ? -16.247 19.513  20.453 1.00 20.24 ? 809  ASN A CA  1 
ATOM   6470 C C   . ASN A 1 809 ? -17.726 19.824  20.626 1.00 20.63 ? 809  ASN A C   1 
ATOM   6471 O O   . ASN A 1 809 ? -18.545 19.230  19.929 1.00 21.57 ? 809  ASN A O   1 
ATOM   6472 C CB  . ASN A 1 809 ? -16.089 18.024  20.143 1.00 20.31 ? 809  ASN A CB  1 
ATOM   6473 C CG  . ASN A 1 809 ? -14.725 17.710  19.590 1.00 21.57 ? 809  ASN A CG  1 
ATOM   6474 O OD1 . ASN A 1 809 ? -14.017 16.855  20.096 1.00 24.37 ? 809  ASN A OD1 1 
ATOM   6475 N ND2 . ASN A 1 809 ? -14.343 18.436  18.582 1.00 17.35 ? 809  ASN A ND2 1 
ATOM   6476 N N   . ASN A 1 810 ? -18.063 20.726  21.529 1.00 20.79 ? 810  ASN A N   1 
ATOM   6477 C CA  . ASN A 1 810 ? -19.497 21.183  21.654 1.00 21.19 ? 810  ASN A CA  1 
ATOM   6478 C C   . ASN A 1 810 ? -20.468 20.001  21.874 1.00 20.52 ? 810  ASN A C   1 
ATOM   6479 O O   . ASN A 1 810 ? -21.511 19.870  21.174 1.00 20.36 ? 810  ASN A O   1 
ATOM   6480 C CB  . ASN A 1 810 ? -19.896 21.989  20.396 1.00 22.44 ? 810  ASN A CB  1 
ATOM   6481 C CG  . ASN A 1 810 ? -21.304 22.673  20.495 1.00 22.54 ? 810  ASN A CG  1 
ATOM   6482 O OD1 . ASN A 1 810 ? -21.688 23.208  21.538 1.00 30.28 ? 810  ASN A OD1 1 
ATOM   6483 N ND2 . ASN A 1 810 ? -22.013 22.714  19.364 1.00 27.65 ? 810  ASN A ND2 1 
ATOM   6484 N N   . LEU A 1 811 ? -20.129 19.134  22.824 1.00 18.20 ? 811  LEU A N   1 
ATOM   6485 C CA  . LEU A 1 811 ? -20.887 17.890  22.997 1.00 16.88 ? 811  LEU A CA  1 
ATOM   6486 C C   . LEU A 1 811 ? -22.134 18.196  23.775 1.00 15.86 ? 811  LEU A C   1 
ATOM   6487 O O   . LEU A 1 811 ? -22.125 18.988  24.721 1.00 15.00 ? 811  LEU A O   1 
ATOM   6488 C CB  . LEU A 1 811 ? -20.077 16.819  23.743 1.00 16.55 ? 811  LEU A CB  1 
ATOM   6489 C CG  . LEU A 1 811 ? -18.767 16.384  23.061 1.00 17.04 ? 811  LEU A CG  1 
ATOM   6490 C CD1 . LEU A 1 811 ? -18.041 15.310  23.931 1.00 18.47 ? 811  LEU A CD1 1 
ATOM   6491 C CD2 . LEU A 1 811 ? -19.022 15.867  21.622 1.00 14.67 ? 811  LEU A CD2 1 
ATOM   6492 N N   . ALA A 1 812 ? -23.211 17.528  23.390 1.00 16.70 ? 812  ALA A N   1 
ATOM   6493 C CA  . ALA A 1 812 ? -24.452 17.716  24.134 1.00 16.10 ? 812  ALA A CA  1 
ATOM   6494 C C   . ALA A 1 812 ? -25.293 16.461  23.997 1.00 16.26 ? 812  ALA A C   1 
ATOM   6495 O O   . ALA A 1 812 ? -25.174 15.727  23.022 1.00 16.37 ? 812  ALA A O   1 
ATOM   6496 C CB  . ALA A 1 812 ? -25.228 18.911  23.575 1.00 16.63 ? 812  ALA A CB  1 
ATOM   6497 N N   . PHE A 1 813 ? -26.158 16.257  24.981 1.00 16.74 ? 813  PHE A N   1 
ATOM   6498 C CA  . PHE A 1 813 ? -27.178 15.216  24.926 1.00 17.30 ? 813  PHE A CA  1 
ATOM   6499 C C   . PHE A 1 813 ? -28.268 15.717  24.010 1.00 18.69 ? 813  PHE A C   1 
ATOM   6500 O O   . PHE A 1 813 ? -28.886 16.750  24.305 1.00 19.67 ? 813  PHE A O   1 
ATOM   6501 C CB  . PHE A 1 813 ? -27.740 14.969  26.331 1.00 18.22 ? 813  PHE A CB  1 
ATOM   6502 C CG  . PHE A 1 813 ? -26.726 14.454  27.309 1.00 19.26 ? 813  PHE A CG  1 
ATOM   6503 C CD1 . PHE A 1 813 ? -26.311 13.115  27.260 1.00 19.54 ? 813  PHE A CD1 1 
ATOM   6504 C CD2 . PHE A 1 813 ? -26.160 15.292  28.260 1.00 20.44 ? 813  PHE A CD2 1 
ATOM   6505 C CE1 . PHE A 1 813 ? -25.354 12.646  28.153 1.00 17.17 ? 813  PHE A CE1 1 
ATOM   6506 C CE2 . PHE A 1 813 ? -25.183 14.807  29.166 1.00 22.23 ? 813  PHE A CE2 1 
ATOM   6507 C CZ  . PHE A 1 813 ? -24.787 13.481  29.099 1.00 18.41 ? 813  PHE A CZ  1 
ATOM   6508 N N   . ASN A 1 814 ? -28.505 15.027  22.898 1.00 18.13 ? 814  ASN A N   1 
ATOM   6509 C CA  . ASN A 1 814 ? -29.504 15.502  21.965 1.00 20.24 ? 814  ASN A CA  1 
ATOM   6510 C C   . ASN A 1 814 ? -30.681 14.545  21.866 1.00 19.89 ? 814  ASN A C   1 
ATOM   6511 O O   . ASN A 1 814 ? -31.528 14.707  21.009 1.00 20.24 ? 814  ASN A O   1 
ATOM   6512 C CB  . ASN A 1 814 ? -28.897 15.764  20.602 1.00 21.20 ? 814  ASN A CB  1 
ATOM   6513 C CG  . ASN A 1 814 ? -28.739 14.540  19.788 1.00 23.52 ? 814  ASN A CG  1 
ATOM   6514 O OD1 . ASN A 1 814 ? -28.674 13.415  20.306 1.00 27.43 ? 814  ASN A OD1 1 
ATOM   6515 N ND2 . ASN A 1 814 ? -28.644 14.734  18.468 1.00 30.30 ? 814  ASN A ND2 1 
ATOM   6516 N N   . GLU A 1 815 ? -30.665 13.509  22.698 1.00 20.18 ? 815  GLU A N   1 
ATOM   6517 C CA  . GLU A 1 815 ? -31.772 12.509  22.715 1.00 21.69 ? 815  GLU A CA  1 
ATOM   6518 C C   . GLU A 1 815 ? -31.856 11.910  24.106 1.00 20.76 ? 815  GLU A C   1 
ATOM   6519 O O   . GLU A 1 815 ? -30.826 11.562  24.722 1.00 18.87 ? 815  GLU A O   1 
ATOM   6520 C CB  . GLU A 1 815 ? -31.585 11.411  21.657 1.00 20.84 ? 815  GLU A CB  1 
ATOM   6521 C CG  . GLU A 1 815 ? -32.754 10.369  21.585 1.00 23.17 ? 815  GLU A CG  1 
ATOM   6522 C CD  . GLU A 1 815 ? -32.688 9.396   20.398 1.00 27.46 ? 815  GLU A CD  1 
ATOM   6523 O OE1 . GLU A 1 815 ? -32.443 9.813   19.240 1.00 33.49 ? 815  GLU A OE1 1 
ATOM   6524 O OE2 . GLU A 1 815 ? -32.937 8.183   20.621 1.00 38.33 ? 815  GLU A OE2 1 
ATOM   6525 N N   . ILE A 1 816 ? -33.091 11.789  24.608 1.00 19.40 ? 816  ILE A N   1 
ATOM   6526 C CA  . ILE A 1 816 ? -33.323 11.095  25.877 1.00 18.14 ? 816  ILE A CA  1 
ATOM   6527 C C   . ILE A 1 816 ? -34.386 10.008  25.586 1.00 17.52 ? 816  ILE A C   1 
ATOM   6528 O O   . ILE A 1 816 ? -35.449 10.313  25.067 1.00 16.98 ? 816  ILE A O   1 
ATOM   6529 C CB  . ILE A 1 816 ? -33.765 12.044  26.988 1.00 18.04 ? 816  ILE A CB  1 
ATOM   6530 C CG1 . ILE A 1 816 ? -32.655 13.082  27.327 1.00 18.20 ? 816  ILE A CG1 1 
ATOM   6531 C CG2 . ILE A 1 816 ? -34.135 11.278  28.261 1.00 18.55 ? 816  ILE A CG2 1 
ATOM   6532 C CD1 . ILE A 1 816 ? -33.129 14.210  28.234 1.00 18.80 ? 816  ILE A CD1 1 
ATOM   6533 N N   . LYS A 1 817 ? -34.057 8.749   25.851 1.00 16.47 ? 817  LYS A N   1 
ATOM   6534 C CA  . LYS A 1 817 ? -35.009 7.655   25.650 1.00 17.67 ? 817  LYS A CA  1 
ATOM   6535 C C   . LYS A 1 817 ? -35.440 7.187   27.049 1.00 18.32 ? 817  LYS A C   1 
ATOM   6536 O O   . LYS A 1 817 ? -34.603 6.864   27.888 1.00 17.05 ? 817  LYS A O   1 
ATOM   6537 C CB  . LYS A 1 817 ? -34.424 6.530   24.780 1.00 18.04 ? 817  LYS A CB  1 
ATOM   6538 C CG  . LYS A 1 817 ? -35.297 5.296   24.594 1.00 20.59 ? 817  LYS A CG  1 
ATOM   6539 C CD  . LYS A 1 817 ? -34.679 4.378   23.567 1.00 23.99 ? 817  LYS A CD  1 
ATOM   6540 C CE  . LYS A 1 817 ? -35.681 3.507   22.865 1.00 29.12 ? 817  LYS A CE  1 
ATOM   6541 N NZ  . LYS A 1 817 ? -35.044 2.841   21.626 1.00 30.70 ? 817  LYS A NZ  1 
ATOM   6542 N N   . ILE A 1 818 ? -36.760 7.176   27.303 1.00 17.08 ? 818  ILE A N   1 
ATOM   6543 C CA  . ILE A 1 818 ? -37.280 6.783   28.618 1.00 17.85 ? 818  ILE A CA  1 
ATOM   6544 C C   . ILE A 1 818 ? -38.046 5.477   28.437 1.00 17.94 ? 818  ILE A C   1 
ATOM   6545 O O   . ILE A 1 818 ? -38.927 5.402   27.571 1.00 16.94 ? 818  ILE A O   1 
ATOM   6546 C CB  . ILE A 1 818 ? -38.232 7.860   29.232 1.00 17.26 ? 818  ILE A CB  1 
ATOM   6547 C CG1 . ILE A 1 818 ? -37.550 9.246   29.281 1.00 18.97 ? 818  ILE A CG1 1 
ATOM   6548 C CG2 . ILE A 1 818 ? -38.676 7.410   30.615 1.00 18.00 ? 818  ILE A CG2 1 
ATOM   6549 C CD1 . ILE A 1 818 ? -38.569 10.440  29.566 1.00 20.86 ? 818  ILE A CD1 1 
ATOM   6550 N N   . LEU A 1 819 ? -37.650 4.443   29.184 1.00 16.75 ? 819  LEU A N   1 
ATOM   6551 C CA  . LEU A 1 819 ? -38.236 3.108   29.070 1.00 17.58 ? 819  LEU A CA  1 
ATOM   6552 C C   . LEU A 1 819 ? -39.150 2.909   30.276 1.00 17.20 ? 819  LEU A C   1 
ATOM   6553 O O   . LEU A 1 819 ? -38.818 3.301   31.376 1.00 17.29 ? 819  LEU A O   1 
ATOM   6554 C CB  . LEU A 1 819 ? -37.144 1.998   29.051 1.00 16.58 ? 819  LEU A CB  1 
ATOM   6555 C CG  . LEU A 1 819 ? -35.965 2.177   28.063 1.00 17.82 ? 819  LEU A CG  1 
ATOM   6556 C CD1 . LEU A 1 819 ? -34.918 1.037   28.142 1.00 16.87 ? 819  LEU A CD1 1 
ATOM   6557 C CD2 . LEU A 1 819 ? -36.531 2.286   26.630 1.00 11.82 ? 819  LEU A CD2 1 
ATOM   6558 N N   . GLY A 1 820 ? -40.284 2.273   30.062 1.00 17.75 ? 820  GLY A N   1 
ATOM   6559 C CA  . GLY A 1 820 ? -41.190 1.914   31.154 1.00 18.41 ? 820  GLY A CA  1 
ATOM   6560 C C   . GLY A 1 820 ? -42.057 3.075   31.606 1.00 19.77 ? 820  GLY A C   1 
ATOM   6561 O O   . GLY A 1 820 ? -42.475 3.153   32.772 1.00 19.77 ? 820  GLY A O   1 
ATOM   6562 N N   . THR A 1 821 ? -42.349 3.979   30.682 1.00 19.17 ? 821  THR A N   1 
ATOM   6563 C CA  . THR A 1 821 ? -43.076 5.193   31.031 1.00 20.31 ? 821  THR A CA  1 
ATOM   6564 C C   . THR A 1 821 ? -44.478 5.297   30.379 1.00 20.02 ? 821  THR A C   1 
ATOM   6565 O O   . THR A 1 821 ? -44.727 4.790   29.277 1.00 18.15 ? 821  THR A O   1 
ATOM   6566 C CB  . THR A 1 821 ? -42.238 6.441   30.721 1.00 20.31 ? 821  THR A CB  1 
ATOM   6567 O OG1 . THR A 1 821 ? -42.931 7.612   31.152 1.00 23.11 ? 821  THR A OG1 1 
ATOM   6568 C CG2 . THR A 1 821 ? -41.933 6.560   29.211 1.00 18.60 ? 821  THR A CG2 1 
ATOM   6569 N N   . GLU A 1 822 ? -45.402 5.943   31.092 1.00 21.58 ? 822  GLU A N   1 
ATOM   6570 C CA  . GLU A 1 822 ? -46.650 6.383   30.491 1.00 23.18 ? 822  GLU A CA  1 
ATOM   6571 C C   . GLU A 1 822 ? -46.333 7.616   29.647 1.00 23.82 ? 822  GLU A C   1 
ATOM   6572 O O   . GLU A 1 822 ? -45.306 8.258   29.855 1.00 24.11 ? 822  GLU A O   1 
ATOM   6573 C CB  . GLU A 1 822 ? -47.698 6.723   31.582 1.00 23.98 ? 822  GLU A CB  1 
ATOM   6574 C CG  . GLU A 1 822 ? -48.202 5.473   32.338 1.00 24.36 ? 822  GLU A CG  1 
ATOM   6575 C CD  . GLU A 1 822 ? -48.759 4.402   31.418 1.00 30.04 ? 822  GLU A CD  1 
ATOM   6576 O OE1 . GLU A 1 822 ? -49.617 4.714   30.549 1.00 33.77 ? 822  GLU A OE1 1 
ATOM   6577 O OE2 . GLU A 1 822 ? -48.349 3.234   31.562 1.00 32.87 ? 822  GLU A OE2 1 
ATOM   6578 N N   . GLU A 1 823 ? -47.218 7.984   28.730 1.00 24.98 ? 823  GLU A N   1 
ATOM   6579 C CA  . GLU A 1 823 ? -46.931 9.127   27.849 1.00 26.55 ? 823  GLU A CA  1 
ATOM   6580 C C   . GLU A 1 823 ? -46.525 10.416  28.593 1.00 26.98 ? 823  GLU A C   1 
ATOM   6581 O O   . GLU A 1 823 ? -47.305 10.918  29.419 1.00 27.29 ? 823  GLU A O   1 
ATOM   6582 C CB  . GLU A 1 823 ? -48.131 9.396   26.946 1.00 27.06 ? 823  GLU A CB  1 
ATOM   6583 C CG  . GLU A 1 823 ? -47.797 10.360  25.828 1.00 29.75 ? 823  GLU A CG  1 
ATOM   6584 C CD  . GLU A 1 823 ? -48.799 10.356  24.704 1.00 34.67 ? 823  GLU A CD  1 
ATOM   6585 O OE1 . GLU A 1 823 ? -49.865 9.709   24.832 1.00 35.42 ? 823  GLU A OE1 1 
ATOM   6586 O OE2 . GLU A 1 823 ? -48.500 11.011  23.685 1.00 36.25 ? 823  GLU A OE2 1 
ATOM   6587 N N   . PRO A 1 824 ? -45.304 10.943  28.345 1.00 27.56 ? 824  PRO A N   1 
ATOM   6588 C CA  . PRO A 1 824 ? -44.984 12.264  28.871 1.00 28.57 ? 824  PRO A CA  1 
ATOM   6589 C C   . PRO A 1 824 ? -45.736 13.374  28.115 1.00 30.10 ? 824  PRO A C   1 
ATOM   6590 O O   . PRO A 1 824 ? -45.888 13.301  26.881 1.00 31.92 ? 824  PRO A O   1 
ATOM   6591 C CB  . PRO A 1 824 ? -43.462 12.403  28.639 1.00 28.59 ? 824  PRO A CB  1 
ATOM   6592 C CG  . PRO A 1 824 ? -42.990 11.082  28.189 1.00 27.76 ? 824  PRO A CG  1 
ATOM   6593 C CD  . PRO A 1 824 ? -44.157 10.352  27.623 1.00 27.59 ? 824  PRO A CD  1 
ATOM   6594 N N   . SER A 1 825 ? -46.211 14.374  28.851 1.00 29.61 ? 825  SER A N   1 
ATOM   6595 C CA  . SER A 1 825 ? -46.732 15.594  28.240 1.00 30.78 ? 825  SER A CA  1 
ATOM   6596 C C   . SER A 1 825 ? -46.083 16.818  28.866 1.00 30.57 ? 825  SER A C   1 
ATOM   6597 O O   . SER A 1 825 ? -45.491 16.720  29.945 1.00 30.36 ? 825  SER A O   1 
ATOM   6598 C CB  . SER A 1 825 ? -48.250 15.662  28.403 1.00 30.22 ? 825  SER A CB  1 
ATOM   6599 O OG  . SER A 1 825 ? -48.600 15.754  29.772 1.00 31.99 ? 825  SER A OG  1 
ATOM   6600 N N   . ASN A 1 826 ? -46.193 17.961  28.182 1.00 30.83 ? 826  ASN A N   1 
ATOM   6601 C CA  . ASN A 1 826 ? -45.648 19.245  28.656 1.00 31.59 ? 826  ASN A CA  1 
ATOM   6602 C C   . ASN A 1 826 ? -44.183 19.152  29.066 1.00 30.57 ? 826  ASN A C   1 
ATOM   6603 O O   . ASN A 1 826 ? -43.829 19.597  30.159 1.00 30.01 ? 826  ASN A O   1 
ATOM   6604 C CB  . ASN A 1 826 ? -46.434 19.775  29.863 1.00 31.77 ? 826  ASN A CB  1 
ATOM   6605 C CG  . ASN A 1 826 ? -47.924 19.874  29.612 1.00 35.99 ? 826  ASN A CG  1 
ATOM   6606 O OD1 . ASN A 1 826 ? -48.382 19.839  28.463 1.00 39.43 ? 826  ASN A OD1 1 
ATOM   6607 N ND2 . ASN A 1 826 ? -48.694 20.000  30.698 1.00 38.42 ? 826  ASN A ND2 1 
ATOM   6608 N N   . VAL A 1 827 ? -43.348 18.574  28.206 1.00 30.01 ? 827  VAL A N   1 
ATOM   6609 C CA  . VAL A 1 827 ? -41.929 18.423  28.516 1.00 29.17 ? 827  VAL A CA  1 
ATOM   6610 C C   . VAL A 1 827 ? -41.238 19.784  28.510 1.00 28.96 ? 827  VAL A C   1 
ATOM   6611 O O   . VAL A 1 827 ? -41.337 20.540  27.551 1.00 29.33 ? 827  VAL A O   1 
ATOM   6612 C CB  . VAL A 1 827 ? -41.232 17.412  27.578 1.00 29.44 ? 827  VAL A CB  1 
ATOM   6613 C CG1 . VAL A 1 827 ? -39.742 17.319  27.898 1.00 29.28 ? 827  VAL A CG1 1 
ATOM   6614 C CG2 . VAL A 1 827 ? -41.894 16.059  27.683 1.00 28.38 ? 827  VAL A CG2 1 
ATOM   6615 N N   . THR A 1 828 ? -40.560 20.083  29.610 1.00 28.67 ? 828  THR A N   1 
ATOM   6616 C CA  . THR A 1 828 ? -39.978 21.381  29.880 1.00 28.95 ? 828  THR A CA  1 
ATOM   6617 C C   . THR A 1 828 ? -38.522 21.192  30.283 1.00 27.79 ? 828  THR A C   1 
ATOM   6618 O O   . THR A 1 828 ? -38.199 20.271  31.017 1.00 27.08 ? 828  THR A O   1 
ATOM   6619 C CB  . THR A 1 828 ? -40.766 22.089  31.007 1.00 29.30 ? 828  THR A CB  1 
ATOM   6620 O OG1 . THR A 1 828 ? -42.042 22.511  30.487 1.00 32.24 ? 828  THR A OG1 1 
ATOM   6621 C CG2 . THR A 1 828 ? -40.053 23.323  31.515 1.00 32.33 ? 828  THR A CG2 1 
ATOM   6622 N N   . VAL A 1 829 ? -37.665 22.089  29.821 1.00 26.97 ? 829  VAL A N   1 
ATOM   6623 C CA  . VAL A 1 829 ? -36.232 21.990  30.094 1.00 26.68 ? 829  VAL A CA  1 
ATOM   6624 C C   . VAL A 1 829 ? -35.815 23.288  30.761 1.00 26.94 ? 829  VAL A C   1 
ATOM   6625 O O   . VAL A 1 829 ? -36.124 24.376  30.251 1.00 27.79 ? 829  VAL A O   1 
ATOM   6626 C CB  . VAL A 1 829 ? -35.434 21.792  28.795 1.00 27.04 ? 829  VAL A CB  1 
ATOM   6627 C CG1 . VAL A 1 829 ? -33.937 21.774  29.081 1.00 26.58 ? 829  VAL A CG1 1 
ATOM   6628 C CG2 . VAL A 1 829 ? -35.899 20.567  28.058 1.00 25.08 ? 829  VAL A CG2 1 
ATOM   6629 N N   . LYS A 1 830 ? -35.181 23.185  31.924 1.00 25.92 ? 830  LYS A N   1 
ATOM   6630 C CA  . LYS A 1 830 ? -34.636 24.334  32.610 1.00 27.22 ? 830  LYS A CA  1 
ATOM   6631 C C   . LYS A 1 830 ? -33.123 24.191  32.637 1.00 27.76 ? 830  LYS A C   1 
ATOM   6632 O O   . LYS A 1 830 ? -32.617 23.084  32.721 1.00 25.88 ? 830  LYS A O   1 
ATOM   6633 C CB  . LYS A 1 830 ? -35.125 24.419  34.048 1.00 27.59 ? 830  LYS A CB  1 
ATOM   6634 C CG  . LYS A 1 830 ? -36.636 24.645  34.192 1.00 30.02 ? 830  LYS A CG  1 
ATOM   6635 C CD  . LYS A 1 830 ? -36.972 24.860  35.654 1.00 36.12 ? 830  LYS A CD  1 
ATOM   6636 C CE  . LYS A 1 830 ? -38.473 25.030  35.866 1.00 40.76 ? 830  LYS A CE  1 
ATOM   6637 N NZ  . LYS A 1 830 ? -38.822 24.998  37.329 1.00 42.29 ? 830  LYS A NZ  1 
ATOM   6638 N N   . HIS A 1 831 ? -32.430 25.321  32.618 1.00 29.24 ? 831  HIS A N   1 
ATOM   6639 C CA  . HIS A 1 831 ? -30.972 25.345  32.657 1.00 31.70 ? 831  HIS A CA  1 
ATOM   6640 C C   . HIS A 1 831 ? -30.567 26.215  33.844 1.00 33.37 ? 831  HIS A C   1 
ATOM   6641 O O   . HIS A 1 831 ? -30.862 27.411  33.875 1.00 33.60 ? 831  HIS A O   1 
ATOM   6642 C CB  . HIS A 1 831 ? -30.434 25.838  31.310 1.00 31.93 ? 831  HIS A CB  1 
ATOM   6643 C CG  . HIS A 1 831 ? -28.943 25.993  31.246 1.00 32.44 ? 831  HIS A CG  1 
ATOM   6644 N ND1 . HIS A 1 831 ? -28.332 26.871  30.376 1.00 35.16 ? 831  HIS A ND1 1 
ATOM   6645 C CD2 . HIS A 1 831 ? -27.942 25.402  31.945 1.00 34.26 ? 831  HIS A CD2 1 
ATOM   6646 C CE1 . HIS A 1 831 ? -27.021 26.807  30.533 1.00 35.19 ? 831  HIS A CE1 1 
ATOM   6647 N NE2 . HIS A 1 831 ? -26.758 25.924  31.480 1.00 34.83 ? 831  HIS A NE2 1 
ATOM   6648 N N   . ASN A 1 832 ? -29.926 25.589  34.833 1.00 35.69 ? 832  ASN A N   1 
ATOM   6649 C CA  . ASN A 1 832 ? -29.584 26.228  36.111 1.00 38.18 ? 832  ASN A CA  1 
ATOM   6650 C C   . ASN A 1 832 ? -30.840 26.751  36.830 1.00 39.22 ? 832  ASN A C   1 
ATOM   6651 O O   . ASN A 1 832 ? -30.775 27.734  37.570 1.00 39.27 ? 832  ASN A O   1 
ATOM   6652 C CB  . ASN A 1 832 ? -28.556 27.370  35.925 1.00 38.48 ? 832  ASN A CB  1 
ATOM   6653 C CG  . ASN A 1 832 ? -27.187 26.888  35.426 1.00 40.84 ? 832  ASN A CG  1 
ATOM   6654 O OD1 . ASN A 1 832 ? -26.679 25.848  35.842 1.00 41.76 ? 832  ASN A OD1 1 
ATOM   6655 N ND2 . ASN A 1 832 ? -26.578 27.672  34.531 1.00 42.14 ? 832  ASN A ND2 1 
ATOM   6656 N N   . GLY A 1 833 ? -31.978 26.099  36.592 1.00 40.10 ? 833  GLY A N   1 
ATOM   6657 C CA  . GLY A 1 833 ? -33.250 26.498  37.213 1.00 41.60 ? 833  GLY A CA  1 
ATOM   6658 C C   . GLY A 1 833 ? -34.098 27.453  36.392 1.00 42.68 ? 833  GLY A C   1 
ATOM   6659 O O   . GLY A 1 833 ? -35.232 27.780  36.779 1.00 42.94 ? 833  GLY A O   1 
ATOM   6660 N N   . VAL A 1 834 ? -33.565 27.873  35.244 1.00 43.33 ? 834  VAL A N   1 
ATOM   6661 C CA  . VAL A 1 834 ? -34.184 28.899  34.407 1.00 44.26 ? 834  VAL A CA  1 
ATOM   6662 C C   . VAL A 1 834 ? -34.798 28.297  33.147 1.00 45.04 ? 834  VAL A C   1 
ATOM   6663 O O   . VAL A 1 834 ? -34.096 27.659  32.347 1.00 44.47 ? 834  VAL A O   1 
ATOM   6664 C CB  . VAL A 1 834 ? -33.173 30.014  34.021 1.00 44.29 ? 834  VAL A CB  1 
ATOM   6665 C CG1 . VAL A 1 834 ? -33.791 31.001  33.015 1.00 44.44 ? 834  VAL A CG1 1 
ATOM   6666 C CG2 . VAL A 1 834 ? -32.687 30.740  35.262 1.00 44.70 ? 834  VAL A CG2 1 
ATOM   6667 N N   . PRO A 1 835 ? -36.125 28.476  32.974 1.00 45.99 ? 835  PRO A N   1 
ATOM   6668 C CA  . PRO A 1 835 ? -36.843 28.031  31.785 1.00 46.85 ? 835  PRO A CA  1 
ATOM   6669 C C   . PRO A 1 835 ? -36.070 28.419  30.518 1.00 47.83 ? 835  PRO A C   1 
ATOM   6670 O O   . PRO A 1 835 ? -35.308 29.381  30.570 1.00 48.52 ? 835  PRO A O   1 
ATOM   6671 C CB  . PRO A 1 835 ? -38.160 28.805  31.896 1.00 47.14 ? 835  PRO A CB  1 
ATOM   6672 C CG  . PRO A 1 835 ? -38.396 28.866  33.360 1.00 46.47 ? 835  PRO A CG  1 
ATOM   6673 C CD  . PRO A 1 835 ? -37.035 29.120  33.945 1.00 46.28 ? 835  PRO A CD  1 
ATOM   6674 N N   . SER A 1 836 ? -36.248 27.758  29.374 1.00 48.61 ? 836  SER A N   1 
ATOM   6675 C CA  . SER A 1 836 ? -37.356 26.873  28.984 1.00 49.72 ? 836  SER A CA  1 
ATOM   6676 C C   . SER A 1 836 ? -37.837 27.374  27.625 1.00 49.91 ? 836  SER A C   1 
ATOM   6677 O O   . SER A 1 836 ? -37.084 28.052  26.913 1.00 50.30 ? 836  SER A O   1 
ATOM   6678 C CB  . SER A 1 836 ? -38.522 26.851  29.977 1.00 50.05 ? 836  SER A CB  1 
ATOM   6679 O OG  . SER A 1 836 ? -39.245 25.640  29.880 1.00 50.85 ? 836  SER A OG  1 
ATOM   6680 N N   . THR A 1 838 ? -38.441 27.189  24.275 1.00 43.64 ? 838  THR A N   1 
ATOM   6681 C CA  . THR A 1 838 ? -38.298 25.994  23.434 1.00 43.34 ? 838  THR A CA  1 
ATOM   6682 C C   . THR A 1 838 ? -38.937 24.737  24.055 1.00 41.65 ? 838  THR A C   1 
ATOM   6683 O O   . THR A 1 838 ? -38.758 24.454  25.233 1.00 42.67 ? 838  THR A O   1 
ATOM   6684 C CB  . THR A 1 838 ? -36.815 25.701  23.100 1.00 43.53 ? 838  THR A CB  1 
ATOM   6685 O OG1 . THR A 1 838 ? -36.092 25.443  24.310 1.00 45.54 ? 838  THR A OG1 1 
ATOM   6686 C CG2 . THR A 1 838 ? -36.169 26.885  22.348 1.00 44.94 ? 838  THR A CG2 1 
ATOM   6687 N N   . SER A 1 839 ? -39.705 24.019  23.245 1.00 39.43 ? 839  SER A N   1 
ATOM   6688 C CA  . SER A 1 839 ? -40.379 22.783  23.633 1.00 36.78 ? 839  SER A CA  1 
ATOM   6689 C C   . SER A 1 839 ? -39.643 21.667  22.885 1.00 33.73 ? 839  SER A C   1 
ATOM   6690 O O   . SER A 1 839 ? -39.474 21.770  21.665 1.00 34.20 ? 839  SER A O   1 
ATOM   6691 C CB  . SER A 1 839 ? -41.839 22.854  23.176 1.00 37.40 ? 839  SER A CB  1 
ATOM   6692 O OG  . SER A 1 839 ? -42.640 21.816  23.727 1.00 39.72 ? 839  SER A OG  1 
ATOM   6693 N N   . PRO A 1 840 ? -39.147 20.626  23.600 1.00 30.73 ? 840  PRO A N   1 
ATOM   6694 C CA  . PRO A 1 840 ? -38.492 19.563  22.837 1.00 27.81 ? 840  PRO A CA  1 
ATOM   6695 C C   . PRO A 1 840 ? -39.515 18.712  22.103 1.00 25.99 ? 840  PRO A C   1 
ATOM   6696 O O   . PRO A 1 840 ? -40.701 18.789  22.404 1.00 25.36 ? 840  PRO A O   1 
ATOM   6697 C CB  . PRO A 1 840 ? -37.790 18.731  23.904 1.00 27.98 ? 840  PRO A CB  1 
ATOM   6698 C CG  . PRO A 1 840 ? -38.544 18.989  25.151 1.00 30.50 ? 840  PRO A CG  1 
ATOM   6699 C CD  . PRO A 1 840 ? -39.107 20.372  25.053 1.00 29.96 ? 840  PRO A CD  1 
ATOM   6700 N N   . THR A 1 841 ? -39.051 17.915  21.146 1.00 23.05 ? 841  THR A N   1 
ATOM   6701 C CA  . THR A 1 841 ? -39.902 16.939  20.431 1.00 21.46 ? 841  THR A CA  1 
ATOM   6702 C C   . THR A 1 841 ? -40.027 15.643  21.216 1.00 20.93 ? 841  THR A C   1 
ATOM   6703 O O   . THR A 1 841 ? -39.029 15.113  21.688 1.00 20.18 ? 841  THR A O   1 
ATOM   6704 C CB  . THR A 1 841 ? -39.303 16.666  19.010 1.00 21.08 ? 841  THR A CB  1 
ATOM   6705 O OG1 . THR A 1 841 ? -39.340 17.869  18.251 1.00 20.04 ? 841  THR A OG1 1 
ATOM   6706 C CG2 . THR A 1 841 ? -40.011 15.534  18.257 1.00 20.23 ? 841  THR A CG2 1 
ATOM   6707 N N   . VAL A 1 842 ? -41.255 15.128  21.374 1.00 20.07 ? 842  VAL A N   1 
ATOM   6708 C CA  . VAL A 1 842 ? -41.450 13.886  22.093 1.00 20.40 ? 842  VAL A CA  1 
ATOM   6709 C C   . VAL A 1 842 ? -42.212 12.924  21.211 1.00 20.30 ? 842  VAL A C   1 
ATOM   6710 O O   . VAL A 1 842 ? -43.271 13.293  20.632 1.00 18.81 ? 842  VAL A O   1 
ATOM   6711 C CB  . VAL A 1 842 ? -42.232 14.077  23.442 1.00 21.93 ? 842  VAL A CB  1 
ATOM   6712 C CG1 . VAL A 1 842 ? -42.493 12.706  24.110 1.00 23.19 ? 842  VAL A CG1 1 
ATOM   6713 C CG2 . VAL A 1 842 ? -41.491 15.027  24.362 1.00 23.56 ? 842  VAL A CG2 1 
ATOM   6714 N N   . THR A 1 843 ? -41.632 11.736  21.046 1.00 18.65 ? 843  THR A N   1 
ATOM   6715 C CA  . THR A 1 843 ? -42.265 10.616  20.348 1.00 19.20 ? 843  THR A CA  1 
ATOM   6716 C C   . THR A 1 843 ? -42.610 9.526   21.349 1.00 18.98 ? 843  THR A C   1 
ATOM   6717 O O   . THR A 1 843 ? -41.803 9.174   22.212 1.00 18.40 ? 843  THR A O   1 
ATOM   6718 C CB  . THR A 1 843 ? -41.348 10.099  19.253 1.00 19.78 ? 843  THR A CB  1 
ATOM   6719 O OG1 . THR A 1 843 ? -40.896 11.213  18.464 1.00 19.40 ? 843  THR A OG1 1 
ATOM   6720 C CG2 . THR A 1 843 ? -42.040 9.100   18.365 1.00 18.50 ? 843  THR A CG2 1 
ATOM   6721 N N   . TYR A 1 844 ? -43.829 8.993   21.253 1.00 18.82 ? 844  TYR A N   1 
ATOM   6722 C CA  . TYR A 1 844 ? -44.243 8.015   22.224 1.00 18.06 ? 844  TYR A CA  1 
ATOM   6723 C C   . TYR A 1 844 ? -44.804 6.761   21.562 1.00 18.62 ? 844  TYR A C   1 
ATOM   6724 O O   . TYR A 1 844 ? -45.601 6.826   20.608 1.00 17.75 ? 844  TYR A O   1 
ATOM   6725 C CB  . TYR A 1 844 ? -45.253 8.633   23.228 1.00 19.10 ? 844  TYR A CB  1 
ATOM   6726 C CG  . TYR A 1 844 ? -45.612 7.681   24.351 1.00 18.50 ? 844  TYR A CG  1 
ATOM   6727 C CD1 . TYR A 1 844 ? -44.656 7.289   25.291 1.00 18.41 ? 844  TYR A CD1 1 
ATOM   6728 C CD2 . TYR A 1 844 ? -46.914 7.154   24.463 1.00 19.86 ? 844  TYR A CD2 1 
ATOM   6729 C CE1 . TYR A 1 844 ? -44.967 6.387   26.311 1.00 15.88 ? 844  TYR A CE1 1 
ATOM   6730 C CE2 . TYR A 1 844 ? -47.237 6.279   25.465 1.00 16.89 ? 844  TYR A CE2 1 
ATOM   6731 C CZ  . TYR A 1 844 ? -46.271 5.895   26.393 1.00 18.71 ? 844  TYR A CZ  1 
ATOM   6732 O OH  . TYR A 1 844 ? -46.616 5.025   27.393 1.00 20.53 ? 844  TYR A OH  1 
ATOM   6733 N N   . ASP A 1 845 ? -44.348 5.612   22.062 1.00 18.63 ? 845  ASP A N   1 
ATOM   6734 C CA  . ASP A 1 845 ? -44.831 4.320   21.648 1.00 19.83 ? 845  ASP A CA  1 
ATOM   6735 C C   . ASP A 1 845 ? -45.699 3.777   22.791 1.00 20.83 ? 845  ASP A C   1 
ATOM   6736 O O   . ASP A 1 845 ? -45.198 3.313   23.810 1.00 19.54 ? 845  ASP A O   1 
ATOM   6737 C CB  . ASP A 1 845 ? -43.653 3.379   21.366 1.00 20.23 ? 845  ASP A CB  1 
ATOM   6738 C CG  . ASP A 1 845 ? -44.081 2.074   20.718 1.00 22.60 ? 845  ASP A CG  1 
ATOM   6739 O OD1 . ASP A 1 845 ? -45.175 1.527   21.047 1.00 24.55 ? 845  ASP A OD1 1 
ATOM   6740 O OD2 . ASP A 1 845 ? -43.317 1.566   19.881 1.00 26.44 ? 845  ASP A OD2 1 
ATOM   6741 N N   . SER A 1 846 ? -47.012 3.814   22.622 1.00 22.50 ? 846  SER A N   1 
ATOM   6742 C CA  . SER A 1 846 ? -47.887 3.357   23.696 1.00 24.47 ? 846  SER A CA  1 
ATOM   6743 C C   . SER A 1 846 ? -47.946 1.835   23.918 1.00 24.41 ? 846  SER A C   1 
ATOM   6744 O O   . SER A 1 846 ? -48.297 1.407   25.034 1.00 25.74 ? 846  SER A O   1 
ATOM   6745 C CB  . SER A 1 846 ? -49.305 3.882   23.459 1.00 24.71 ? 846  SER A CB  1 
ATOM   6746 O OG  . SER A 1 846 ? -49.843 3.099   22.419 1.00 27.55 ? 846  SER A OG  1 
ATOM   6747 N N   . ASN A 1 847 ? -47.651 1.022   22.901 1.00 24.65 ? 847  ASN A N   1 
ATOM   6748 C CA  . ASN A 1 847 ? -47.563 -0.444  23.076 1.00 24.73 ? 847  ASN A CA  1 
ATOM   6749 C C   . ASN A 1 847 ? -46.306 -0.826  23.885 1.00 24.07 ? 847  ASN A C   1 
ATOM   6750 O O   . ASN A 1 847 ? -46.361 -1.703  24.752 1.00 24.43 ? 847  ASN A O   1 
ATOM   6751 C CB  . ASN A 1 847 ? -47.547 -1.219  21.746 1.00 25.72 ? 847  ASN A CB  1 
ATOM   6752 C CG  . ASN A 1 847 ? -47.697 -2.769  21.944 1.00 28.90 ? 847  ASN A CG  1 
ATOM   6753 O OD1 . ASN A 1 847 ? -46.833 -3.563  21.511 1.00 35.93 ? 847  ASN A OD1 1 
ATOM   6754 N ND2 . ASN A 1 847 ? -48.781 -3.188  22.622 1.00 34.81 ? 847  ASN A ND2 1 
ATOM   6755 N N   . LEU A 1 848 ? -45.187 -0.159  23.606 1.00 22.88 ? 848  LEU A N   1 
ATOM   6756 C CA  . LEU A 1 848 ? -43.912 -0.493  24.252 1.00 22.16 ? 848  LEU A CA  1 
ATOM   6757 C C   . LEU A 1 848 ? -43.616 0.302   25.525 1.00 19.93 ? 848  LEU A C   1 
ATOM   6758 O O   . LEU A 1 848 ? -42.677 -0.025  26.266 1.00 18.04 ? 848  LEU A O   1 
ATOM   6759 C CB  . LEU A 1 848 ? -42.767 -0.264  23.241 1.00 23.06 ? 848  LEU A CB  1 
ATOM   6760 C CG  . LEU A 1 848 ? -42.312 -1.468  22.409 1.00 25.60 ? 848  LEU A CG  1 
ATOM   6761 C CD1 . LEU A 1 848 ? -43.427 -2.444  22.031 1.00 28.82 ? 848  LEU A CD1 1 
ATOM   6762 C CD2 . LEU A 1 848 ? -41.534 -1.010  21.204 1.00 25.08 ? 848  LEU A CD2 1 
ATOM   6763 N N   . LYS A 1 849 ? -44.392 1.361   25.760 1.00 16.94 ? 849  LYS A N   1 
ATOM   6764 C CA  . LYS A 1 849 ? -44.189 2.314   26.867 1.00 15.75 ? 849  LYS A CA  1 
ATOM   6765 C C   . LYS A 1 849 ? -42.770 2.951   26.793 1.00 15.50 ? 849  LYS A C   1 
ATOM   6766 O O   . LYS A 1 849 ? -42.081 3.034   27.784 1.00 14.46 ? 849  LYS A O   1 
ATOM   6767 C CB  . LYS A 1 849 ? -44.429 1.677   28.244 1.00 16.23 ? 849  LYS A CB  1 
ATOM   6768 C CG  . LYS A 1 849 ? -45.772 0.909   28.350 1.00 17.87 ? 849  LYS A CG  1 
ATOM   6769 C CD  . LYS A 1 849 ? -46.892 1.892   28.276 1.00 17.12 ? 849  LYS A CD  1 
ATOM   6770 C CE  . LYS A 1 849 ? -48.266 1.249   28.610 1.00 22.44 ? 849  LYS A CE  1 
ATOM   6771 N NZ  . LYS A 1 849 ? -49.359 2.258   28.493 1.00 25.92 ? 849  LYS A NZ  1 
ATOM   6772 N N   . VAL A 1 850 ? -42.403 3.390   25.602 1.00 15.58 ? 850  VAL A N   1 
ATOM   6773 C CA  . VAL A 1 850 ? -41.113 4.102   25.343 1.00 15.99 ? 850  VAL A CA  1 
ATOM   6774 C C   . VAL A 1 850 ? -41.407 5.516   24.836 1.00 16.31 ? 850  VAL A C   1 
ATOM   6775 O O   . VAL A 1 850 ? -42.169 5.683   23.844 1.00 17.27 ? 850  VAL A O   1 
ATOM   6776 C CB  . VAL A 1 850 ? -40.327 3.358   24.295 1.00 15.24 ? 850  VAL A CB  1 
ATOM   6777 C CG1 . VAL A 1 850 ? -38.952 4.072   23.996 1.00 16.72 ? 850  VAL A CG1 1 
ATOM   6778 C CG2 . VAL A 1 850 ? -40.118 1.888   24.744 1.00 15.76 ? 850  VAL A CG2 1 
ATOM   6779 N N   . ALA A 1 851 ? -40.769 6.511   25.472 1.00 15.42 ? 851  ALA A N   1 
ATOM   6780 C CA  . ALA A 1 851 ? -40.795 7.889   25.029 1.00 15.39 ? 851  ALA A CA  1 
ATOM   6781 C C   . ALA A 1 851 ? -39.385 8.229   24.572 1.00 16.70 ? 851  ALA A C   1 
ATOM   6782 O O   . ALA A 1 851 ? -38.430 7.772   25.196 1.00 15.87 ? 851  ALA A O   1 
ATOM   6783 C CB  . ALA A 1 851 ? -41.144 8.770   26.153 1.00 14.77 ? 851  ALA A CB  1 
ATOM   6784 N N   . ILE A 1 852 ? -39.276 8.983   23.486 1.00 16.14 ? 852  ILE A N   1 
ATOM   6785 C CA  . ILE A 1 852 ? -37.979 9.567   23.096 1.00 16.95 ? 852  ILE A CA  1 
ATOM   6786 C C   . ILE A 1 852 ? -38.115 11.063  22.962 1.00 17.18 ? 852  ILE A C   1 
ATOM   6787 O O   . ILE A 1 852 ? -38.995 11.562  22.238 1.00 18.30 ? 852  ILE A O   1 
ATOM   6788 C CB  . ILE A 1 852 ? -37.438 8.973   21.801 1.00 16.45 ? 852  ILE A CB  1 
ATOM   6789 C CG1 . ILE A 1 852 ? -37.464 7.437   21.870 1.00 18.42 ? 852  ILE A CG1 1 
ATOM   6790 C CG2 . ILE A 1 852 ? -35.989 9.559   21.519 1.00 17.24 ? 852  ILE A CG2 1 
ATOM   6791 C CD1 . ILE A 1 852 ? -36.870 6.731   20.628 1.00 19.78 ? 852  ILE A CD1 1 
ATOM   6792 N N   . ILE A 1 853 ? -37.248 11.784  23.661 1.00 17.40 ? 853  ILE A N   1 
ATOM   6793 C CA  . ILE A 1 853 ? -37.238 13.231  23.638 1.00 18.19 ? 853  ILE A CA  1 
ATOM   6794 C C   . ILE A 1 853 ? -36.112 13.618  22.712 1.00 19.62 ? 853  ILE A C   1 
ATOM   6795 O O   . ILE A 1 853 ? -34.955 13.181  22.901 1.00 17.60 ? 853  ILE A O   1 
ATOM   6796 C CB  . ILE A 1 853 ? -37.032 13.822  25.035 1.00 18.44 ? 853  ILE A CB  1 
ATOM   6797 C CG1 . ILE A 1 853 ? -38.183 13.358  25.975 1.00 19.52 ? 853  ILE A CG1 1 
ATOM   6798 C CG2 . ILE A 1 853 ? -36.975 15.355  24.970 1.00 19.49 ? 853  ILE A CG2 1 
ATOM   6799 C CD1 . ILE A 1 853 ? -37.972 13.718  27.404 1.00 21.60 ? 853  ILE A CD1 1 
ATOM   6800 N N   . THR A 1 854 ? -36.457 14.392  21.687 1.00 19.86 ? 854  THR A N   1 
ATOM   6801 C CA  . THR A 1 854 ? -35.449 14.924  20.762 1.00 21.63 ? 854  THR A CA  1 
ATOM   6802 C C   . THR A 1 854 ? -35.592 16.448  20.607 1.00 21.75 ? 854  THR A C   1 
ATOM   6803 O O   . THR A 1 854 ? -36.379 17.082  21.323 1.00 19.66 ? 854  THR A O   1 
ATOM   6804 C CB  . THR A 1 854 ? -35.505 14.238  19.379 1.00 22.04 ? 854  THR A CB  1 
ATOM   6805 O OG1 . THR A 1 854 ? -36.838 14.268  18.849 1.00 20.98 ? 854  THR A OG1 1 
ATOM   6806 C CG2 . THR A 1 854 ? -35.028 12.789  19.457 1.00 23.20 ? 854  THR A CG2 1 
ATOM   6807 N N   . ASP A 1 855 ? -34.843 17.029  19.659 1.00 23.08 ? 855  ASP A N   1 
ATOM   6808 C CA  . ASP A 1 855 ? -34.811 18.490  19.479 1.00 24.56 ? 855  ASP A CA  1 
ATOM   6809 C C   . ASP A 1 855 ? -34.514 19.162  20.825 1.00 24.83 ? 855  ASP A C   1 
ATOM   6810 O O   . ASP A 1 855 ? -35.219 20.074  21.294 1.00 23.92 ? 855  ASP A O   1 
ATOM   6811 C CB  . ASP A 1 855 ? -36.094 19.011  18.811 1.00 25.38 ? 855  ASP A CB  1 
ATOM   6812 C CG  . ASP A 1 855 ? -35.995 20.488  18.409 1.00 29.10 ? 855  ASP A CG  1 
ATOM   6813 O OD1 . ASP A 1 855 ? -34.865 21.007  18.204 1.00 33.47 ? 855  ASP A OD1 1 
ATOM   6814 O OD2 . ASP A 1 855 ? -37.054 21.164  18.348 1.00 32.32 ? 855  ASP A OD2 1 
ATOM   6815 N N   . ILE A 1 856 ? -33.458 18.650  21.448 1.00 24.44 ? 856  ILE A N   1 
ATOM   6816 C CA  . ILE A 1 856 ? -32.979 19.083  22.745 1.00 25.70 ? 856  ILE A CA  1 
ATOM   6817 C C   . ILE A 1 856 ? -31.449 19.171  22.595 1.00 24.71 ? 856  ILE A C   1 
ATOM   6818 O O   . ILE A 1 856 ? -30.885 18.492  21.751 1.00 25.14 ? 856  ILE A O   1 
ATOM   6819 C CB  . ILE A 1 856 ? -33.457 18.069  23.848 1.00 26.17 ? 856  ILE A CB  1 
ATOM   6820 C CG1 . ILE A 1 856 ? -33.568 18.701  25.234 1.00 28.48 ? 856  ILE A CG1 1 
ATOM   6821 C CG2 . ILE A 1 856 ? -32.625 16.784  23.854 1.00 27.70 ? 856  ILE A CG2 1 
ATOM   6822 C CD1 . ILE A 1 856 ? -34.385 17.835  26.249 1.00 28.22 ? 856  ILE A CD1 1 
ATOM   6823 N N   . ASP A 1 857 ? -30.803 20.016  23.385 1.00 23.79 ? 857  ASP A N   1 
ATOM   6824 C CA  . ASP A 1 857 ? -29.344 20.204  23.315 1.00 25.05 ? 857  ASP A CA  1 
ATOM   6825 C C   . ASP A 1 857 ? -28.896 20.483  24.751 1.00 22.72 ? 857  ASP A C   1 
ATOM   6826 O O   . ASP A 1 857 ? -28.786 21.634  25.166 1.00 23.65 ? 857  ASP A O   1 
ATOM   6827 C CB  . ASP A 1 857 ? -29.044 21.380  22.363 1.00 25.72 ? 857  ASP A CB  1 
ATOM   6828 C CG  . ASP A 1 857 ? -27.564 21.684  22.213 1.00 30.25 ? 857  ASP A CG  1 
ATOM   6829 O OD1 . ASP A 1 857 ? -26.787 20.806  21.778 1.00 32.78 ? 857  ASP A OD1 1 
ATOM   6830 O OD2 . ASP A 1 857 ? -27.201 22.843  22.490 1.00 36.14 ? 857  ASP A OD2 1 
ATOM   6831 N N   . LEU A 1 858 ? -28.695 19.438  25.546 1.00 20.50 ? 858  LEU A N   1 
ATOM   6832 C CA  . LEU A 1 858 ? -28.260 19.650  26.920 1.00 19.05 ? 858  LEU A CA  1 
ATOM   6833 C C   . LEU A 1 858 ? -26.754 19.593  26.957 1.00 19.79 ? 858  LEU A C   1 
ATOM   6834 O O   . LEU A 1 858 ? -26.190 18.503  26.842 1.00 19.27 ? 858  LEU A O   1 
ATOM   6835 C CB  . LEU A 1 858 ? -28.833 18.582  27.850 1.00 19.05 ? 858  LEU A CB  1 
ATOM   6836 C CG  . LEU A 1 858 ? -30.357 18.346  27.740 1.00 20.43 ? 858  LEU A CG  1 
ATOM   6837 C CD1 . LEU A 1 858 ? -30.780 17.407  28.807 1.00 20.26 ? 858  LEU A CD1 1 
ATOM   6838 C CD2 . LEU A 1 858 ? -31.091 19.677  27.848 1.00 22.06 ? 858  LEU A CD2 1 
ATOM   6839 N N   . LEU A 1 859 ? -26.094 20.735  27.109 1.00 18.13 ? 859  LEU A N   1 
ATOM   6840 C CA  . LEU A 1 859 ? -24.636 20.737  26.939 1.00 18.42 ? 859  LEU A CA  1 
ATOM   6841 C C   . LEU A 1 859 ? -23.949 19.899  28.019 1.00 18.32 ? 859  LEU A C   1 
ATOM   6842 O O   . LEU A 1 859 ? -24.251 19.983  29.206 1.00 15.49 ? 859  LEU A O   1 
ATOM   6843 C CB  . LEU A 1 859 ? -24.092 22.170  26.966 1.00 18.23 ? 859  LEU A CB  1 
ATOM   6844 C CG  . LEU A 1 859 ? -24.723 23.207  26.029 1.00 19.90 ? 859  LEU A CG  1 
ATOM   6845 C CD1 . LEU A 1 859 ? -24.032 24.574  26.319 1.00 20.05 ? 859  LEU A CD1 1 
ATOM   6846 C CD2 . LEU A 1 859 ? -24.617 22.790  24.556 1.00 21.83 ? 859  LEU A CD2 1 
ATOM   6847 N N   . LEU A 1 860 ? -23.004 19.075  27.578 1.00 20.15 ? 860  LEU A N   1 
ATOM   6848 C CA  . LEU A 1 860 ? -22.187 18.338  28.491 1.00 21.96 ? 860  LEU A CA  1 
ATOM   6849 C C   . LEU A 1 860 ? -21.501 19.298  29.439 1.00 22.98 ? 860  LEU A C   1 
ATOM   6850 O O   . LEU A 1 860 ? -20.872 20.286  29.023 1.00 24.47 ? 860  LEU A O   1 
ATOM   6851 C CB  . LEU A 1 860 ? -21.156 17.515  27.694 1.00 22.37 ? 860  LEU A CB  1 
ATOM   6852 C CG  . LEU A 1 860 ? -20.376 16.492  28.475 1.00 23.00 ? 860  LEU A CG  1 
ATOM   6853 C CD1 . LEU A 1 860 ? -21.259 15.366  28.972 1.00 22.87 ? 860  LEU A CD1 1 
ATOM   6854 C CD2 . LEU A 1 860 ? -19.259 15.996  27.570 1.00 24.09 ? 860  LEU A CD2 1 
ATOM   6855 N N   . GLY A 1 861 ? -21.652 19.036  30.723 1.00 22.05 ? 861  GLY A N   1 
ATOM   6856 C CA  . GLY A 1 861 ? -21.016 19.877  31.711 1.00 22.81 ? 861  GLY A CA  1 
ATOM   6857 C C   . GLY A 1 861 ? -21.896 20.952  32.311 1.00 22.71 ? 861  GLY A C   1 
ATOM   6858 O O   . GLY A 1 861 ? -21.429 21.702  33.145 1.00 23.62 ? 861  GLY A O   1 
ATOM   6859 N N   . GLU A 1 862 ? -23.168 21.019  31.899 1.00 22.21 ? 862  GLU A N   1 
ATOM   6860 C CA  . GLU A 1 862 ? -24.132 22.016  32.409 1.00 21.77 ? 862  GLU A CA  1 
ATOM   6861 C C   . GLU A 1 862 ? -25.261 21.293  33.169 1.00 21.84 ? 862  GLU A C   1 
ATOM   6862 O O   . GLU A 1 862 ? -25.598 20.166  32.855 1.00 20.49 ? 862  GLU A O   1 
ATOM   6863 C CB  . GLU A 1 862 ? -24.780 22.830  31.262 1.00 22.44 ? 862  GLU A CB  1 
ATOM   6864 C CG  . GLU A 1 862 ? -23.907 23.867  30.565 1.00 24.95 ? 862  GLU A CG  1 
ATOM   6865 C CD  . GLU A 1 862 ? -23.304 24.856  31.538 1.00 29.87 ? 862  GLU A CD  1 
ATOM   6866 O OE1 . GLU A 1 862 ? -24.080 25.561  32.231 1.00 33.43 ? 862  GLU A OE1 1 
ATOM   6867 O OE2 . GLU A 1 862 ? -22.056 24.946  31.596 1.00 32.92 ? 862  GLU A OE2 1 
ATOM   6868 N N   . ALA A 1 863 ? -25.841 21.979  34.142 1.00 20.79 ? 863  ALA A N   1 
ATOM   6869 C CA  . ALA A 1 863 ? -26.913 21.442  34.974 1.00 20.96 ? 863  ALA A CA  1 
ATOM   6870 C C   . ALA A 1 863 ? -28.236 21.721  34.303 1.00 20.45 ? 863  ALA A C   1 
ATOM   6871 O O   . ALA A 1 863 ? -28.486 22.841  33.850 1.00 19.47 ? 863  ALA A O   1 
ATOM   6872 C CB  . ALA A 1 863 ? -26.883 22.106  36.325 1.00 21.71 ? 863  ALA A CB  1 
ATOM   6873 N N   . TYR A 1 864 ? -29.097 20.713  34.266 1.00 20.99 ? 864  TYR A N   1 
ATOM   6874 C CA  . TYR A 1 864 ? -30.400 20.870  33.656 1.00 20.78 ? 864  TYR A CA  1 
ATOM   6875 C C   . TYR A 1 864 ? -31.425 20.135  34.495 1.00 21.67 ? 864  TYR A C   1 
ATOM   6876 O O   . TYR A 1 864 ? -31.090 19.230  35.250 1.00 20.00 ? 864  TYR A O   1 
ATOM   6877 C CB  . TYR A 1 864 ? -30.430 20.274  32.254 1.00 20.18 ? 864  TYR A CB  1 
ATOM   6878 C CG  . TYR A 1 864 ? -29.581 21.015  31.252 1.00 19.88 ? 864  TYR A CG  1 
ATOM   6879 C CD1 . TYR A 1 864 ? -30.078 22.134  30.573 1.00 19.88 ? 864  TYR A CD1 1 
ATOM   6880 C CD2 . TYR A 1 864 ? -28.284 20.575  30.962 1.00 19.54 ? 864  TYR A CD2 1 
ATOM   6881 C CE1 . TYR A 1 864 ? -29.285 22.818  29.657 1.00 19.73 ? 864  TYR A CE1 1 
ATOM   6882 C CE2 . TYR A 1 864 ? -27.480 21.270  30.052 1.00 16.71 ? 864  TYR A CE2 1 
ATOM   6883 C CZ  . TYR A 1 864 ? -27.980 22.362  29.409 1.00 19.86 ? 864  TYR A CZ  1 
ATOM   6884 O OH  . TYR A 1 864 ? -27.194 23.021  28.514 1.00 18.36 ? 864  TYR A OH  1 
ATOM   6885 N N   . THR A 1 865 ? -32.670 20.572  34.351 1.00 22.43 ? 865  THR A N   1 
ATOM   6886 C CA  . THR A 1 865 ? -33.816 19.823  34.839 1.00 24.93 ? 865  THR A CA  1 
ATOM   6887 C C   . THR A 1 865 ? -34.767 19.627  33.667 1.00 25.00 ? 865  THR A C   1 
ATOM   6888 O O   . THR A 1 865 ? -35.106 20.595  32.993 1.00 26.32 ? 865  THR A O   1 
ATOM   6889 C CB  . THR A 1 865 ? -34.542 20.609  35.952 1.00 25.28 ? 865  THR A CB  1 
ATOM   6890 O OG1 . THR A 1 865 ? -33.629 20.862  37.031 1.00 28.01 ? 865  THR A OG1 1 
ATOM   6891 C CG2 . THR A 1 865 ? -35.720 19.785  36.494 1.00 26.57 ? 865  THR A CG2 1 
ATOM   6892 N N   . VAL A 1 866 ? -35.181 18.388  33.397 1.00 24.74 ? 866  VAL A N   1 
ATOM   6893 C CA  . VAL A 1 866 ? -36.186 18.146  32.376 1.00 23.98 ? 866  VAL A CA  1 
ATOM   6894 C C   . VAL A 1 866 ? -37.394 17.617  33.147 1.00 24.38 ? 866  VAL A C   1 
ATOM   6895 O O   . VAL A 1 866 ? -37.270 16.663  33.904 1.00 23.47 ? 866  VAL A O   1 
ATOM   6896 C CB  . VAL A 1 866 ? -35.705 17.160  31.295 1.00 23.11 ? 866  VAL A CB  1 
ATOM   6897 C CG1 . VAL A 1 866 ? -36.767 16.951  30.200 1.00 23.35 ? 866  VAL A CG1 1 
ATOM   6898 C CG2 . VAL A 1 866 ? -34.387 17.673  30.654 1.00 22.11 ? 866  VAL A CG2 1 
ATOM   6899 N N   . GLU A 1 867 ? -38.535 18.280  32.990 1.00 24.40 ? 867  GLU A N   1 
ATOM   6900 C CA  . GLU A 1 867 ? -39.705 17.920  33.772 1.00 26.36 ? 867  GLU A CA  1 
ATOM   6901 C C   . GLU A 1 867 ? -40.803 17.597  32.787 1.00 25.08 ? 867  GLU A C   1 
ATOM   6902 O O   . GLU A 1 867 ? -40.827 18.142  31.689 1.00 24.09 ? 867  GLU A O   1 
ATOM   6903 C CB  . GLU A 1 867 ? -40.146 19.074  34.669 1.00 25.96 ? 867  GLU A CB  1 
ATOM   6904 C CG  . GLU A 1 867 ? -39.195 19.396  35.834 1.00 30.52 ? 867  GLU A CG  1 
ATOM   6905 C CD  . GLU A 1 867 ? -39.597 20.676  36.560 1.00 30.90 ? 867  GLU A CD  1 
ATOM   6906 O OE1 . GLU A 1 867 ? -38.797 21.630  36.598 1.00 34.44 ? 867  GLU A OE1 1 
ATOM   6907 O OE2 . GLU A 1 867 ? -40.740 20.721  37.068 1.00 38.05 ? 867  GLU A OE2 1 
ATOM   6908 N N   . TRP A 1 868 ? -41.697 16.704  33.176 1.00 26.47 ? 868  TRP A N   1 
ATOM   6909 C CA  . TRP A 1 868 ? -42.842 16.399  32.345 1.00 28.31 ? 868  TRP A CA  1 
ATOM   6910 C C   . TRP A 1 868 ? -44.039 16.103  33.239 1.00 29.55 ? 868  TRP A C   1 
ATOM   6911 O O   . TRP A 1 868 ? -43.882 15.961  34.443 1.00 28.91 ? 868  TRP A O   1 
ATOM   6912 C CB  . TRP A 1 868 ? -42.536 15.222  31.410 1.00 27.76 ? 868  TRP A CB  1 
ATOM   6913 C CG  . TRP A 1 868 ? -42.118 13.950  32.074 1.00 28.57 ? 868  TRP A CG  1 
ATOM   6914 C CD1 . TRP A 1 868 ? -42.932 12.921  32.464 1.00 28.38 ? 868  TRP A CD1 1 
ATOM   6915 C CD2 . TRP A 1 868 ? -40.777 13.544  32.387 1.00 28.14 ? 868  TRP A CD2 1 
ATOM   6916 N NE1 . TRP A 1 868 ? -42.177 11.909  33.014 1.00 29.14 ? 868  TRP A NE1 1 
ATOM   6917 C CE2 . TRP A 1 868 ? -40.856 12.275  32.990 1.00 28.61 ? 868  TRP A CE2 1 
ATOM   6918 C CE3 . TRP A 1 868 ? -39.517 14.147  32.232 1.00 28.32 ? 868  TRP A CE3 1 
ATOM   6919 C CZ2 . TRP A 1 868 ? -39.717 11.572  33.421 1.00 29.18 ? 868  TRP A CZ2 1 
ATOM   6920 C CZ3 . TRP A 1 868 ? -38.386 13.450  32.663 1.00 27.22 ? 868  TRP A CZ3 1 
ATOM   6921 C CH2 . TRP A 1 868 ? -38.499 12.182  33.255 1.00 28.16 ? 868  TRP A CH2 1 
ATOM   6922 N N   . ALA A 1 869 ? -45.226 16.054  32.639 1.00 31.65 ? 869  ALA A N   1 
ATOM   6923 C CA  . ALA A 1 869 ? -46.437 15.587  33.310 1.00 33.11 ? 869  ALA A CA  1 
ATOM   6924 C C   . ALA A 1 869 ? -46.931 14.296  32.650 1.00 34.58 ? 869  ALA A C   1 
ATOM   6925 O O   . ALA A 1 869 ? -46.368 13.846  31.642 1.00 33.96 ? 869  ALA A O   1 
ATOM   6926 C CB  . ALA A 1 869 ? -47.498 16.652  33.253 1.00 33.64 ? 869  ALA A CB  1 
ATOM   6927 N N   . HIS A 1 870 ? -47.970 13.690  33.231 1.00 35.66 ? 870  HIS A N   1 
ATOM   6928 C CA  . HIS A 1 870 ? -48.567 12.454  32.712 1.00 37.30 ? 870  HIS A CA  1 
ATOM   6929 C C   . HIS A 1 870 ? -50.082 12.634  32.551 1.00 38.17 ? 870  HIS A C   1 
ATOM   6930 O O   . HIS A 1 870 ? -50.581 12.755  31.428 1.00 39.12 ? 870  HIS A O   1 
ATOM   6931 C CB  . HIS A 1 870 ? -48.313 11.263  33.638 1.00 37.73 ? 870  HIS A CB  1 
ATOM   6932 C CG  . HIS A 1 870 ? -46.882 10.811  33.697 1.00 38.86 ? 870  HIS A CG  1 
ATOM   6933 N ND1 . HIS A 1 870 ? -46.277 10.105  32.679 1.00 39.63 ? 870  HIS A ND1 1 
ATOM   6934 C CD2 . HIS A 1 870 ? -45.958 10.915  34.679 1.00 40.73 ? 870  HIS A CD2 1 
ATOM   6935 C CE1 . HIS A 1 870 ? -45.032 9.823   33.018 1.00 40.61 ? 870  HIS A CE1 1 
ATOM   6936 N NE2 . HIS A 1 870 ? -44.812 10.302  34.228 1.00 41.08 ? 870  HIS A NE2 1 
HETATM 6937 O OAA . NR3 B 2 .   ? 3.852   -25.949 20.856 1.00 45.87 ? 1001 NR3 A OAA 1 
HETATM 6938 O OAB . NR3 B 2 .   ? 3.707   -14.018 18.514 1.00 20.36 ? 1001 NR3 A OAB 1 
HETATM 6939 O OAC . NR3 B 2 .   ? 5.325   -22.748 21.424 1.00 44.70 ? 1001 NR3 A OAC 1 
HETATM 6940 O OAD . NR3 B 2 .   ? -0.985  -14.590 20.757 1.00 20.82 ? 1001 NR3 A OAD 1 
HETATM 6941 O OAE . NR3 B 2 .   ? 2.201   -18.747 22.666 1.00 22.97 ? 1001 NR3 A OAE 1 
HETATM 6942 O OAF . NR3 B 2 .   ? 1.734   -23.444 21.979 1.00 41.16 ? 1001 NR3 A OAF 1 
HETATM 6943 O OAG . NR3 B 2 .   ? 0.064   -14.620 18.080 1.00 22.46 ? 1001 NR3 A OAG 1 
HETATM 6944 O OAH . NR3 B 2 .   ? 4.271   -20.927 22.736 1.00 26.11 ? 1001 NR3 A OAH 1 
HETATM 6945 O OAI . NR3 B 2 .   ? 1.537   -20.454 18.166 1.00 26.12 ? 1001 NR3 A OAI 1 
HETATM 6946 O OAJ . NR3 B 2 .   ? 3.383   -21.984 17.725 1.00 28.30 ? 1001 NR3 A OAJ 1 
HETATM 6947 O OAK . NR3 B 2 .   ? 1.571   -22.576 19.185 1.00 28.04 ? 1001 NR3 A OAK 1 
HETATM 6948 C CAL . NR3 B 2 .   ? 4.424   -25.010 21.805 1.00 44.61 ? 1001 NR3 A CAL 1 
HETATM 6949 C CAM . NR3 B 2 .   ? 3.205   -15.275 18.017 1.00 19.03 ? 1001 NR3 A CAM 1 
HETATM 6950 C CAN . NR3 B 2 .   ? 1.156   -15.783 21.464 1.00 20.40 ? 1001 NR3 A CAN 1 
HETATM 6951 C CAO . NR3 B 2 .   ? 2.267   -18.226 20.292 1.00 21.75 ? 1001 NR3 A CAO 1 
HETATM 6952 O OAP . NR3 B 2 .   ? 3.131   -20.984 19.904 1.00 26.11 ? 1001 NR3 A OAP 1 
HETATM 6953 C CAQ . NR3 B 2 .   ? 4.111   -23.546 21.406 1.00 41.36 ? 1001 NR3 A CAQ 1 
HETATM 6954 C CAR . NR3 B 2 .   ? 0.145   -15.445 20.348 1.00 22.35 ? 1001 NR3 A CAR 1 
HETATM 6955 C CAS . NR3 B 2 .   ? 2.779   -19.129 21.414 1.00 23.44 ? 1001 NR3 A CAS 1 
HETATM 6956 C CAT . NR3 B 2 .   ? 3.027   -22.943 22.328 1.00 37.39 ? 1001 NR3 A CAT 1 
HETATM 6957 C CAU . NR3 B 2 .   ? 0.943   -14.778 19.203 1.00 19.80 ? 1001 NR3 A CAU 1 
HETATM 6958 C CAV . NR3 B 2 .   ? 2.974   -21.409 22.384 1.00 29.28 ? 1001 NR3 A CAV 1 
HETATM 6959 C CAW . NR3 B 2 .   ? 2.040   -15.819 18.859 1.00 21.25 ? 1001 NR3 A CAW 1 
HETATM 6960 C CAX . NR3 B 2 .   ? 2.472   -20.620 21.135 1.00 26.15 ? 1001 NR3 A CAX 1 
HETATM 6961 S SAY . NR3 B 2 .   ? 2.567   -16.460 20.486 1.00 23.38 ? 1001 NR3 A SAY 1 
HETATM 6962 S SAZ . NR3 B 2 .   ? 2.401   -21.503 18.760 1.00 26.87 ? 1001 NR3 A SAZ 1 
HETATM 6963 C C1  . NAG C 3 .   ? 24.940  -10.463 35.323 1.00 24.60 ? 2001 NAG A C1  1 
HETATM 6964 C C2  . NAG C 3 .   ? 24.784  -9.627  36.600 1.00 26.08 ? 2001 NAG A C2  1 
HETATM 6965 C C3  . NAG C 3 .   ? 25.409  -8.233  36.447 1.00 27.63 ? 2001 NAG A C3  1 
HETATM 6966 C C4  . NAG C 3 .   ? 26.860  -8.294  35.939 1.00 28.21 ? 2001 NAG A C4  1 
HETATM 6967 C C5  . NAG C 3 .   ? 26.888  -9.216  34.721 1.00 26.38 ? 2001 NAG A C5  1 
HETATM 6968 C C6  . NAG C 3 .   ? 28.302  -9.435  34.174 1.00 24.81 ? 2001 NAG A C6  1 
HETATM 6969 C C7  . NAG C 3 .   ? 22.928  -9.977  38.133 1.00 29.31 ? 2001 NAG A C7  1 
HETATM 6970 C C8  . NAG C 3 .   ? 21.484  -9.766  38.474 1.00 30.59 ? 2001 NAG A C8  1 
HETATM 6971 N N2  . NAG C 3 .   ? 23.378  -9.489  36.982 1.00 27.42 ? 2001 NAG A N2  1 
HETATM 6972 O O3  . NAG C 3 .   ? 25.344  -7.586  37.692 1.00 25.05 ? 2001 NAG A O3  1 
HETATM 6973 O O4  . NAG C 3 .   ? 27.314  -7.022  35.494 1.00 32.64 ? 2001 NAG A O4  1 
HETATM 6974 O O5  . NAG C 3 .   ? 26.322  -10.489 34.996 1.00 27.01 ? 2001 NAG A O5  1 
HETATM 6975 O O6  . NAG C 3 .   ? 28.224  -10.190 32.975 1.00 26.32 ? 2001 NAG A O6  1 
HETATM 6976 O O7  . NAG C 3 .   ? 23.628  -10.590 38.934 1.00 34.20 ? 2001 NAG A O7  1 
HETATM 6977 C C1  . NAG D 3 .   ? 27.760  -6.114  36.522 1.00 38.16 ? 2002 NAG A C1  1 
HETATM 6978 C C2  . NAG D 3 .   ? 29.220  -5.763  36.227 1.00 40.03 ? 2002 NAG A C2  1 
HETATM 6979 C C3  . NAG D 3 .   ? 29.761  -4.670  37.141 1.00 42.82 ? 2002 NAG A C3  1 
HETATM 6980 C C4  . NAG D 3 .   ? 28.836  -3.457  37.150 1.00 43.30 ? 2002 NAG A C4  1 
HETATM 6981 C C5  . NAG D 3 .   ? 27.360  -3.841  37.299 1.00 43.40 ? 2002 NAG A C5  1 
HETATM 6982 C C6  . NAG D 3 .   ? 26.496  -2.676  36.841 1.00 44.07 ? 2002 NAG A C6  1 
HETATM 6983 C C7  . NAG D 3 .   ? 30.851  -7.319  35.299 1.00 40.84 ? 2002 NAG A C7  1 
HETATM 6984 C C8  . NAG D 3 .   ? 31.614  -8.603  35.479 1.00 41.22 ? 2002 NAG A C8  1 
HETATM 6985 N N2  . NAG D 3 .   ? 30.048  -6.956  36.299 1.00 40.31 ? 2002 NAG A N2  1 
HETATM 6986 O O3  . NAG D 3 .   ? 31.045  -4.287  36.677 1.00 45.22 ? 2002 NAG A O3  1 
HETATM 6987 O O4  . NAG D 3 .   ? 29.202  -2.613  38.226 1.00 46.28 ? 2002 NAG A O4  1 
HETATM 6988 O O5  . NAG D 3 .   ? 26.967  -4.946  36.502 1.00 39.46 ? 2002 NAG A O5  1 
HETATM 6989 O O6  . NAG D 3 .   ? 25.258  -2.782  37.498 1.00 48.22 ? 2002 NAG A O6  1 
HETATM 6990 O O7  . NAG D 3 .   ? 30.982  -6.664  34.266 1.00 40.76 ? 2002 NAG A O7  1 
HETATM 6991 C C1  . NAG E 3 .   ? -17.336 9.447   11.351 1.00 32.37 ? 2003 NAG A C1  1 
HETATM 6992 C C2  . NAG E 3 .   ? -17.765 10.908  11.253 1.00 35.30 ? 2003 NAG A C2  1 
HETATM 6993 C C3  . NAG E 3 .   ? -17.428 11.511  9.875  1.00 36.37 ? 2003 NAG A C3  1 
HETATM 6994 C C4  . NAG E 3 .   ? -15.941 11.391  9.614  1.00 35.63 ? 2003 NAG A C4  1 
HETATM 6995 C C5  . NAG E 3 .   ? -15.553 9.913   9.740  1.00 36.57 ? 2003 NAG A C5  1 
HETATM 6996 C C6  . NAG E 3 .   ? -14.043 9.694   9.588  1.00 35.99 ? 2003 NAG A C6  1 
HETATM 6997 C C7  . NAG E 3 .   ? -19.814 11.710  12.350 1.00 41.66 ? 2003 NAG A C7  1 
HETATM 6998 C C8  . NAG E 3 .   ? -19.414 13.152  12.569 1.00 41.59 ? 2003 NAG A C8  1 
HETATM 6999 N N2  . NAG E 3 .   ? -19.193 10.995  11.420 1.00 37.86 ? 2003 NAG A N2  1 
HETATM 7000 O O3  . NAG E 3 .   ? -17.865 12.868  9.804  1.00 38.43 ? 2003 NAG A O3  1 
HETATM 7001 O O4  . NAG E 3 .   ? -15.650 11.879  8.326  1.00 39.95 ? 2003 NAG A O4  1 
HETATM 7002 O O5  . NAG E 3 .   ? -15.960 9.430   11.016 1.00 35.41 ? 2003 NAG A O5  1 
HETATM 7003 O O6  . NAG E 3 .   ? -13.791 8.300   9.539  1.00 38.31 ? 2003 NAG A O6  1 
HETATM 7004 O O7  . NAG E 3 .   ? -20.713 11.190  13.004 1.00 44.58 ? 2003 NAG A O7  1 
HETATM 7005 C C1  . GOL F 4 .   ? -6.825  -0.635  31.590 1.00 29.58 ? 3001 GOL A C1  1 
HETATM 7006 O O1  . GOL F 4 .   ? -7.060  -1.278  32.849 1.00 27.00 ? 3001 GOL A O1  1 
HETATM 7007 C C2  . GOL F 4 .   ? -5.628  -1.383  30.913 1.00 29.38 ? 3001 GOL A C2  1 
HETATM 7008 O O2  . GOL F 4 .   ? -4.421  -1.312  31.714 1.00 31.00 ? 3001 GOL A O2  1 
HETATM 7009 C C3  . GOL F 4 .   ? -5.400  -0.974  29.438 1.00 29.41 ? 3001 GOL A C3  1 
HETATM 7010 O O3  . GOL F 4 .   ? -4.564  0.132   29.476 1.00 27.84 ? 3001 GOL A O3  1 
HETATM 7011 C C1  . GOL G 4 .   ? -28.703 -22.346 13.240 1.00 39.96 ? 3002 GOL A C1  1 
HETATM 7012 O O1  . GOL G 4 .   ? -28.281 -23.391 12.393 1.00 43.50 ? 3002 GOL A O1  1 
HETATM 7013 C C2  . GOL G 4 .   ? -27.439 -21.640 13.698 1.00 36.87 ? 3002 GOL A C2  1 
HETATM 7014 O O2  . GOL G 4 .   ? -26.710 -21.164 12.579 1.00 36.99 ? 3002 GOL A O2  1 
HETATM 7015 C C3  . GOL G 4 .   ? -27.844 -20.455 14.542 1.00 33.55 ? 3002 GOL A C3  1 
HETATM 7016 O O3  . GOL G 4 .   ? -26.681 -19.684 14.692 1.00 30.12 ? 3002 GOL A O3  1 
HETATM 7017 C C1  . GOL H 4 .   ? -6.201  -11.667 2.475  1.00 34.06 ? 3003 GOL A C1  1 
HETATM 7018 O O1  . GOL H 4 .   ? -7.344  -12.424 2.141  1.00 37.17 ? 3003 GOL A O1  1 
HETATM 7019 C C2  . GOL H 4 .   ? -5.610  -12.290 3.722  1.00 33.73 ? 3003 GOL A C2  1 
HETATM 7020 O O2  . GOL H 4 .   ? -5.680  -13.685 3.596  1.00 33.43 ? 3003 GOL A O2  1 
HETATM 7021 C C3  . GOL H 4 .   ? -4.164  -11.868 3.857  1.00 32.78 ? 3003 GOL A C3  1 
HETATM 7022 O O3  . GOL H 4 .   ? -3.673  -12.269 5.121  1.00 32.91 ? 3003 GOL A O3  1 
HETATM 7023 C C1  . GOL I 4 .   ? -38.269 12.975  15.814 1.00 37.40 ? 3004 GOL A C1  1 
HETATM 7024 O O1  . GOL I 4 .   ? -37.210 13.889  16.037 1.00 37.47 ? 3004 GOL A O1  1 
HETATM 7025 C C2  . GOL I 4 .   ? -37.795 11.705  15.114 1.00 38.82 ? 3004 GOL A C2  1 
HETATM 7026 O O2  . GOL I 4 .   ? -36.735 11.081  15.810 1.00 39.95 ? 3004 GOL A O2  1 
HETATM 7027 C C3  . GOL I 4 .   ? -38.955 10.718  15.036 1.00 38.07 ? 3004 GOL A C3  1 
HETATM 7028 O O3  . GOL I 4 .   ? -39.312 10.208  16.301 1.00 36.16 ? 3004 GOL A O3  1 
HETATM 7029 O O   . HOH J 5 .   ? -19.890 6.084   20.433 1.00 15.72 ? 4002 HOH A O   1 
HETATM 7030 O O   . HOH J 5 .   ? -6.738  -31.954 52.029 1.00 17.56 ? 4003 HOH A O   1 
HETATM 7031 O O   . HOH J 5 .   ? -7.954  -12.389 13.129 1.00 18.86 ? 4004 HOH A O   1 
HETATM 7032 O O   . HOH J 5 .   ? 20.343  -11.097 15.504 1.00 24.27 ? 4005 HOH A O   1 
HETATM 7033 O O   . HOH J 5 .   ? -19.190 0.527   38.705 1.00 15.35 ? 4006 HOH A O   1 
HETATM 7034 O O   . HOH J 5 .   ? -3.925  -6.326  39.088 1.00 14.04 ? 4007 HOH A O   1 
HETATM 7035 O O   . HOH J 5 .   ? -2.456  -30.614 52.700 1.00 19.06 ? 4008 HOH A O   1 
HETATM 7036 O O   . HOH J 5 .   ? -8.058  -17.870 36.594 1.00 16.67 ? 4009 HOH A O   1 
HETATM 7037 O O   . HOH J 5 .   ? -11.496 -3.396  23.613 1.00 12.54 ? 4010 HOH A O   1 
HETATM 7038 O O   . HOH J 5 .   ? -20.104 -6.883  59.229 1.00 21.08 ? 4011 HOH A O   1 
HETATM 7039 O O   . HOH J 5 .   ? -32.033 -11.809 41.338 1.00 16.74 ? 4012 HOH A O   1 
HETATM 7040 O O   . HOH J 5 .   ? -4.448  -9.011  41.188 1.00 12.11 ? 4014 HOH A O   1 
HETATM 7041 O O   . HOH J 5 .   ? 11.446  -28.869 39.052 1.00 18.12 ? 4015 HOH A O   1 
HETATM 7042 O O   . HOH J 5 .   ? -7.347  -12.221 8.731  1.00 16.82 ? 4016 HOH A O   1 
HETATM 7043 O O   . HOH J 5 .   ? -22.298 -13.995 35.951 1.00 15.34 ? 4017 HOH A O   1 
HETATM 7044 O O   . HOH J 5 .   ? -8.095  -2.783  51.728 1.00 15.84 ? 4018 HOH A O   1 
HETATM 7045 O O   . HOH J 5 .   ? -24.795 5.286   34.577 1.00 14.08 ? 4019 HOH A O   1 
HETATM 7046 O O   . HOH J 5 .   ? -17.831 7.299   21.789 1.00 18.56 ? 4020 HOH A O   1 
HETATM 7047 O O   . HOH J 5 .   ? -29.603 -10.360 28.323 1.00 14.92 ? 4021 HOH A O   1 
HETATM 7048 O O   . HOH J 5 .   ? 2.198   -8.313  34.038 1.00 16.20 ? 4022 HOH A O   1 
HETATM 7049 O O   . HOH J 5 .   ? 9.236   -21.591 43.528 1.00 18.51 ? 4023 HOH A O   1 
HETATM 7050 O O   . HOH J 5 .   ? -13.609 0.518   9.959  1.00 15.55 ? 4024 HOH A O   1 
HETATM 7051 O O   . HOH J 5 .   ? -14.683 14.695  22.001 1.00 17.68 ? 4025 HOH A O   1 
HETATM 7052 O O   . HOH J 5 .   ? -7.991  -18.336 26.384 1.00 20.16 ? 4026 HOH A O   1 
HETATM 7053 O O   . HOH J 5 .   ? -4.186  -32.710 48.902 1.00 20.13 ? 4027 HOH A O   1 
HETATM 7054 O O   . HOH J 5 .   ? -11.732 -18.733 25.174 1.00 15.07 ? 4028 HOH A O   1 
HETATM 7055 O O   . HOH J 5 .   ? -7.032  -10.383 11.018 1.00 15.17 ? 4029 HOH A O   1 
HETATM 7056 O O   . HOH J 5 .   ? -12.402 13.580  21.735 1.00 19.55 ? 4030 HOH A O   1 
HETATM 7057 O O   . HOH J 5 .   ? 2.642   -42.983 50.477 1.00 23.58 ? 4031 HOH A O   1 
HETATM 7058 O O   . HOH J 5 .   ? -3.235  7.362   25.392 1.00 20.01 ? 4032 HOH A O   1 
HETATM 7059 O O   . HOH J 5 .   ? -5.495  -13.266 6.999  1.00 18.24 ? 4033 HOH A O   1 
HETATM 7060 O O   . HOH J 5 .   ? -11.576 -10.244 23.063 1.00 15.81 ? 4034 HOH A O   1 
HETATM 7061 O O   . HOH J 5 .   ? 6.569   -21.177 30.168 1.00 15.54 ? 4035 HOH A O   1 
HETATM 7062 O O   . HOH J 5 .   ? 6.524   -12.079 60.853 1.00 18.29 ? 4036 HOH A O   1 
HETATM 7063 O O   . HOH J 5 .   ? -17.399 -13.162 42.497 1.00 18.70 ? 4037 HOH A O   1 
HETATM 7064 O O   . HOH J 5 .   ? 4.660   -25.850 34.112 1.00 16.25 ? 4038 HOH A O   1 
HETATM 7065 O O   . HOH J 5 .   ? -11.456 12.375  19.515 1.00 26.68 ? 4039 HOH A O   1 
HETATM 7066 O O   . HOH J 5 .   ? -6.764  -32.955 49.348 1.00 20.10 ? 4040 HOH A O   1 
HETATM 7067 O O   . HOH J 5 .   ? -0.150  -2.675  41.323 1.00 16.96 ? 4041 HOH A O   1 
HETATM 7068 O O   . HOH J 5 .   ? 15.561  -10.496 18.961 1.00 17.94 ? 4042 HOH A O   1 
HETATM 7069 O O   . HOH J 5 .   ? -4.873  -3.762  39.273 1.00 18.71 ? 4043 HOH A O   1 
HETATM 7070 O O   . HOH J 5 .   ? -6.338  -17.971 30.398 1.00 20.05 ? 4044 HOH A O   1 
HETATM 7071 O O   . HOH J 5 .   ? -6.213  -24.288 33.349 1.00 17.84 ? 4045 HOH A O   1 
HETATM 7072 O O   . HOH J 5 .   ? -7.845  -16.338 24.456 1.00 16.71 ? 4046 HOH A O   1 
HETATM 7073 O O   . HOH J 5 .   ? -4.263  -12.274 43.011 1.00 13.57 ? 4047 HOH A O   1 
HETATM 7074 O O   . HOH J 5 .   ? -23.275 -14.772 38.989 1.00 14.45 ? 4048 HOH A O   1 
HETATM 7075 O O   . HOH J 5 .   ? -8.905  15.478  30.685 1.00 16.85 ? 4049 HOH A O   1 
HETATM 7076 O O   . HOH J 5 .   ? 10.289  -15.350 25.956 1.00 19.51 ? 4050 HOH A O   1 
HETATM 7077 O O   . HOH J 5 .   ? -21.594 -6.149  45.195 1.00 17.25 ? 4051 HOH A O   1 
HETATM 7078 O O   . HOH J 5 .   ? 10.263  -16.067 34.507 1.00 17.05 ? 4052 HOH A O   1 
HETATM 7079 O O   . HOH J 5 .   ? -42.756 -2.401  27.543 1.00 20.46 ? 4053 HOH A O   1 
HETATM 7080 O O   . HOH J 5 .   ? -3.863  1.912   46.392 1.00 23.38 ? 4054 HOH A O   1 
HETATM 7081 O O   . HOH J 5 .   ? -1.683  -13.826 33.247 1.00 18.01 ? 4055 HOH A O   1 
HETATM 7082 O O   . HOH J 5 .   ? -23.174 -15.520 21.414 1.00 16.21 ? 4056 HOH A O   1 
HETATM 7083 O O   . HOH J 5 .   ? -0.012  -20.220 36.755 1.00 14.53 ? 4057 HOH A O   1 
HETATM 7084 O O   . HOH J 5 .   ? -16.363 22.407  18.435 1.00 20.13 ? 4058 HOH A O   1 
HETATM 7085 O O   . HOH J 5 .   ? -18.447 -6.611  61.449 1.00 14.31 ? 4059 HOH A O   1 
HETATM 7086 O O   . HOH J 5 .   ? 12.633  -27.565 52.671 1.00 21.49 ? 4060 HOH A O   1 
HETATM 7087 O O   . HOH J 5 .   ? -3.106  -31.722 46.398 1.00 24.78 ? 4061 HOH A O   1 
HETATM 7088 O O   . HOH J 5 .   ? -12.912 -20.821 32.666 1.00 15.70 ? 4062 HOH A O   1 
HETATM 7089 O O   . HOH J 5 .   ? 2.441   -2.794  41.283 1.00 17.80 ? 4063 HOH A O   1 
HETATM 7090 O O   . HOH J 5 .   ? -10.196 0.384   45.620 1.00 17.69 ? 4065 HOH A O   1 
HETATM 7091 O O   . HOH J 5 .   ? -4.476  2.156   43.519 1.00 20.41 ? 4066 HOH A O   1 
HETATM 7092 O O   . HOH J 5 .   ? -15.024 2.127   7.916  1.00 22.91 ? 4067 HOH A O   1 
HETATM 7093 O O   . HOH J 5 .   ? -19.757 -19.852 30.152 1.00 21.77 ? 4068 HOH A O   1 
HETATM 7094 O O   . HOH J 5 .   ? 5.950   -10.311 51.994 1.00 20.14 ? 4069 HOH A O   1 
HETATM 7095 O O   . HOH J 5 .   ? -35.378 -2.766  38.523 1.00 19.44 ? 4070 HOH A O   1 
HETATM 7096 O O   . HOH J 5 .   ? 6.080   -12.294 50.107 1.00 17.52 ? 4072 HOH A O   1 
HETATM 7097 O O   . HOH J 5 .   ? -20.378 -16.467 5.838  1.00 26.24 ? 4073 HOH A O   1 
HETATM 7098 O O   . HOH J 5 .   ? -25.955 -17.729 28.013 1.00 20.10 ? 4074 HOH A O   1 
HETATM 7099 O O   . HOH J 5 .   ? 0.605   5.716   1.940  1.00 26.78 ? 4075 HOH A O   1 
HETATM 7100 O O   . HOH J 5 .   ? -11.178 3.746   9.869  1.00 24.94 ? 4076 HOH A O   1 
HETATM 7101 O O   . HOH J 5 .   ? -10.860 -18.677 30.063 1.00 19.84 ? 4077 HOH A O   1 
HETATM 7102 O O   . HOH J 5 .   ? 0.535   -31.493 53.082 1.00 19.58 ? 4078 HOH A O   1 
HETATM 7103 O O   . HOH J 5 .   ? 5.292   -13.587 20.647 1.00 19.55 ? 4079 HOH A O   1 
HETATM 7104 O O   . HOH J 5 .   ? -21.910 -13.601 57.212 1.00 22.17 ? 4081 HOH A O   1 
HETATM 7105 O O   . HOH J 5 .   ? 15.508  -0.229  19.283 1.00 20.07 ? 4082 HOH A O   1 
HETATM 7106 O O   . HOH J 5 .   ? -21.246 2.105   38.472 1.00 26.22 ? 4083 HOH A O   1 
HETATM 7107 O O   . HOH J 5 .   ? -11.057 -19.587 34.435 1.00 15.34 ? 4084 HOH A O   1 
HETATM 7108 O O   . HOH J 5 .   ? -40.596 0.109   27.985 1.00 18.35 ? 4085 HOH A O   1 
HETATM 7109 O O   . HOH J 5 .   ? -20.304 -21.035 38.355 1.00 19.76 ? 4086 HOH A O   1 
HETATM 7110 O O   . HOH J 5 .   ? -25.860 -14.801 21.163 1.00 20.64 ? 4087 HOH A O   1 
HETATM 7111 O O   . HOH J 5 .   ? -5.007  -29.786 51.949 1.00 23.27 ? 4088 HOH A O   1 
HETATM 7112 O O   . HOH J 5 .   ? 7.365   -24.542 34.015 1.00 24.27 ? 4089 HOH A O   1 
HETATM 7113 O O   . HOH J 5 .   ? -12.239 -25.825 41.810 1.00 24.09 ? 4090 HOH A O   1 
HETATM 7114 O O   . HOH J 5 .   ? 11.882  -14.884 57.491 1.00 19.58 ? 4091 HOH A O   1 
HETATM 7115 O O   . HOH J 5 .   ? -21.830 -26.707 21.844 1.00 23.58 ? 4092 HOH A O   1 
HETATM 7116 O O   . HOH J 5 .   ? 12.207  -18.967 49.098 1.00 21.25 ? 4093 HOH A O   1 
HETATM 7117 O O   . HOH J 5 .   ? 19.762  -14.027 29.721 1.00 17.89 ? 4094 HOH A O   1 
HETATM 7118 O O   . HOH J 5 .   ? -12.364 1.978   11.470 1.00 22.15 ? 4095 HOH A O   1 
HETATM 7119 O O   . HOH J 5 .   ? -21.105 -2.358  46.939 1.00 22.79 ? 4096 HOH A O   1 
HETATM 7120 O O   . HOH J 5 .   ? 14.522  -19.745 56.742 1.00 23.20 ? 4097 HOH A O   1 
HETATM 7121 O O   . HOH J 5 .   ? 13.793  -17.465 51.029 1.00 18.89 ? 4098 HOH A O   1 
HETATM 7122 O O   . HOH J 5 .   ? -17.023 -0.216  37.241 1.00 16.68 ? 4099 HOH A O   1 
HETATM 7123 O O   . HOH J 5 .   ? -7.674  -14.029 10.778 1.00 14.95 ? 4100 HOH A O   1 
HETATM 7124 O O   . HOH J 5 .   ? -5.513  -25.906 31.141 1.00 25.02 ? 4101 HOH A O   1 
HETATM 7125 O O   . HOH J 5 .   ? 6.131   -14.275 34.884 1.00 16.40 ? 4102 HOH A O   1 
HETATM 7126 O O   . HOH J 5 .   ? 9.895   -27.881 47.501 1.00 18.58 ? 4103 HOH A O   1 
HETATM 7127 O O   . HOH J 5 .   ? -2.982  -15.758 21.728 1.00 19.00 ? 4104 HOH A O   1 
HETATM 7128 O O   . HOH J 5 .   ? -22.713 -3.755  45.340 1.00 23.45 ? 4105 HOH A O   1 
HETATM 7129 O O   . HOH J 5 .   ? 2.555   -6.014  64.558 1.00 19.49 ? 4106 HOH A O   1 
HETATM 7130 O O   . HOH J 5 .   ? -5.071  1.912   27.275 1.00 15.88 ? 4109 HOH A O   1 
HETATM 7131 O O   . HOH J 5 .   ? -2.951  -6.097  75.876 1.00 20.74 ? 4110 HOH A O   1 
HETATM 7132 O O   . HOH J 5 .   ? -7.265  -11.312 22.232 1.00 19.40 ? 4111 HOH A O   1 
HETATM 7133 O O   . HOH J 5 .   ? -32.442 -23.722 19.513 1.00 26.90 ? 4112 HOH A O   1 
HETATM 7134 O O   . HOH J 5 .   ? -7.936  -27.709 51.847 1.00 19.22 ? 4113 HOH A O   1 
HETATM 7135 O O   . HOH J 5 .   ? -25.235 -3.854  46.309 1.00 29.88 ? 4114 HOH A O   1 
HETATM 7136 O O   . HOH J 5 .   ? -3.696  -24.665 58.666 1.00 20.32 ? 4115 HOH A O   1 
HETATM 7137 O O   . HOH J 5 .   ? -27.602 -4.548  43.234 1.00 19.68 ? 4116 HOH A O   1 
HETATM 7138 O O   . HOH J 5 .   ? 3.020   -32.231 37.743 1.00 23.68 ? 4117 HOH A O   1 
HETATM 7139 O O   . HOH J 5 .   ? -3.754  -39.358 51.683 1.00 18.56 ? 4118 HOH A O   1 
HETATM 7140 O O   . HOH J 5 .   ? 9.377   -11.783 11.426 1.00 15.21 ? 4119 HOH A O   1 
HETATM 7141 O O   . HOH J 5 .   ? 16.047  -15.364 45.709 1.00 24.67 ? 4120 HOH A O   1 
HETATM 7142 O O   . HOH J 5 .   ? 7.735   -14.534 50.027 1.00 13.90 ? 4121 HOH A O   1 
HETATM 7143 O O   . HOH J 5 .   ? 1.329   -4.187  54.042 1.00 24.44 ? 4123 HOH A O   1 
HETATM 7144 O O   . HOH J 5 .   ? -4.960  8.781   37.733 1.00 33.18 ? 4124 HOH A O   1 
HETATM 7145 O O   . HOH J 5 .   ? 13.141  -10.506 19.911 1.00 20.33 ? 4125 HOH A O   1 
HETATM 7146 O O   . HOH J 5 .   ? 1.763   -32.650 33.530 1.00 22.23 ? 4126 HOH A O   1 
HETATM 7147 O O   . HOH J 5 .   ? -21.968 -15.601 7.760  1.00 20.63 ? 4127 HOH A O   1 
HETATM 7148 O O   . HOH J 5 .   ? 2.681   -7.734  51.647 1.00 20.44 ? 4128 HOH A O   1 
HETATM 7149 O O   . HOH J 5 .   ? 7.058   -21.719 33.165 1.00 24.63 ? 4129 HOH A O   1 
HETATM 7150 O O   . HOH J 5 .   ? -6.460  -33.354 59.090 1.00 18.90 ? 4130 HOH A O   1 
HETATM 7151 O O   . HOH J 5 .   ? 10.542  -13.702 23.866 1.00 21.96 ? 4131 HOH A O   1 
HETATM 7152 O O   . HOH J 5 .   ? 18.874  0.627   24.654 1.00 20.15 ? 4132 HOH A O   1 
HETATM 7153 O O   . HOH J 5 .   ? -9.930  -21.770 26.567 1.00 27.99 ? 4133 HOH A O   1 
HETATM 7154 O O   . HOH J 5 .   ? -25.511 18.279  30.884 1.00 22.28 ? 4134 HOH A O   1 
HETATM 7155 O O   . HOH J 5 .   ? -2.497  -27.048 56.525 1.00 19.56 ? 4135 HOH A O   1 
HETATM 7156 O O   . HOH J 5 .   ? -8.757  -18.440 31.622 1.00 22.85 ? 4136 HOH A O   1 
HETATM 7157 O O   . HOH J 5 .   ? -24.866 20.866  39.200 1.00 24.34 ? 4137 HOH A O   1 
HETATM 7158 O O   . HOH J 5 .   ? 5.964   5.221   11.354 1.00 26.03 ? 4139 HOH A O   1 
HETATM 7159 O O   . HOH J 5 .   ? -23.282 17.081  31.638 1.00 29.96 ? 4141 HOH A O   1 
HETATM 7160 O O   . HOH J 5 .   ? -13.612 -18.534 40.081 1.00 16.40 ? 4143 HOH A O   1 
HETATM 7161 O O   . HOH J 5 .   ? -31.789 -10.147 43.807 1.00 22.44 ? 4144 HOH A O   1 
HETATM 7162 O O   . HOH J 5 .   ? -15.636 -5.631  2.911  1.00 27.26 ? 4145 HOH A O   1 
HETATM 7163 O O   . HOH J 5 .   ? -13.795 -24.810 39.869 1.00 25.60 ? 4146 HOH A O   1 
HETATM 7164 O O   . HOH J 5 .   ? 4.528   -20.715 15.445 1.00 23.36 ? 4147 HOH A O   1 
HETATM 7165 O O   . HOH J 5 .   ? -20.531 3.073   12.973 1.00 25.69 ? 4149 HOH A O   1 
HETATM 7166 O O   . HOH J 5 .   ? -38.601 12.348  19.592 1.00 22.66 ? 4150 HOH A O   1 
HETATM 7167 O O   . HOH J 5 .   ? -24.574 3.625   36.656 1.00 33.51 ? 4151 HOH A O   1 
HETATM 7168 O O   . HOH J 5 .   ? -25.898 -20.913 17.283 1.00 24.04 ? 4152 HOH A O   1 
HETATM 7169 O O   . HOH J 5 .   ? 6.086   -4.521  48.925 1.00 29.65 ? 4153 HOH A O   1 
HETATM 7170 O O   . HOH J 5 .   ? -2.262  0.093   29.517 1.00 26.90 ? 4154 HOH A O   1 
HETATM 7171 O O   . HOH J 5 .   ? -3.564  4.132   31.463 1.00 20.38 ? 4155 HOH A O   1 
HETATM 7172 O O   . HOH J 5 .   ? -30.136 -7.450  20.121 1.00 28.50 ? 4156 HOH A O   1 
HETATM 7173 O O   . HOH J 5 .   ? -14.553 -20.136 57.999 1.00 18.52 ? 4157 HOH A O   1 
HETATM 7174 O O   . HOH J 5 .   ? -0.189  -20.560 15.707 1.00 21.04 ? 4158 HOH A O   1 
HETATM 7175 O O   . HOH J 5 .   ? -15.089 -25.559 57.042 1.00 24.29 ? 4159 HOH A O   1 
HETATM 7176 O O   . HOH J 5 .   ? -14.463 6.986   12.242 1.00 25.54 ? 4160 HOH A O   1 
HETATM 7177 O O   . HOH J 5 .   ? -0.710  -13.242 43.051 1.00 21.44 ? 4161 HOH A O   1 
HETATM 7178 O O   . HOH J 5 .   ? -20.722 0.810   10.925 1.00 22.08 ? 4162 HOH A O   1 
HETATM 7179 O O   . HOH J 5 .   ? -8.398  -31.472 47.413 1.00 26.96 ? 4163 HOH A O   1 
HETATM 7180 O O   . HOH J 5 .   ? 7.370   -15.645 47.459 1.00 20.36 ? 4164 HOH A O   1 
HETATM 7181 O O   . HOH J 5 .   ? -12.147 15.372  24.440 1.00 24.51 ? 4165 HOH A O   1 
HETATM 7182 O O   . HOH J 5 .   ? 10.892  -12.144 19.113 1.00 21.35 ? 4166 HOH A O   1 
HETATM 7183 O O   . HOH J 5 .   ? 6.834   -8.020  50.500 1.00 18.40 ? 4167 HOH A O   1 
HETATM 7184 O O   . HOH J 5 .   ? 11.732  -12.565 55.940 1.00 26.13 ? 4168 HOH A O   1 
HETATM 7185 O O   . HOH J 5 .   ? 22.948  -20.370 29.460 1.00 23.97 ? 4169 HOH A O   1 
HETATM 7186 O O   . HOH J 5 .   ? -6.899  16.863  29.924 1.00 25.63 ? 4171 HOH A O   1 
HETATM 7187 O O   . HOH J 5 .   ? -14.654 7.007   42.161 1.00 25.57 ? 4172 HOH A O   1 
HETATM 7188 O O   . HOH J 5 .   ? -15.000 12.385  41.399 1.00 32.12 ? 4173 HOH A O   1 
HETATM 7189 O O   . HOH J 5 .   ? -11.112 22.061  29.779 1.00 25.97 ? 4174 HOH A O   1 
HETATM 7190 O O   . HOH J 5 .   ? -18.086 -5.620  55.957 1.00 25.21 ? 4175 HOH A O   1 
HETATM 7191 O O   . HOH J 5 .   ? -1.153  -29.109 35.806 1.00 25.48 ? 4176 HOH A O   1 
HETATM 7192 O O   . HOH J 5 .   ? -23.985 -9.176  60.387 1.00 24.98 ? 4177 HOH A O   1 
HETATM 7193 O O   . HOH J 5 .   ? -18.081 -22.936 8.641  1.00 32.10 ? 4178 HOH A O   1 
HETATM 7194 O O   . HOH J 5 .   ? -22.149 -0.173  40.324 1.00 28.94 ? 4179 HOH A O   1 
HETATM 7195 O O   . HOH J 5 .   ? -6.998  -32.358 44.878 1.00 22.19 ? 4180 HOH A O   1 
HETATM 7196 O O   . HOH J 5 .   ? 10.452  -31.312 39.735 1.00 24.67 ? 4181 HOH A O   1 
HETATM 7197 O O   . HOH J 5 .   ? 22.218  -8.360  34.538 1.00 19.71 ? 4182 HOH A O   1 
HETATM 7198 O O   . HOH J 5 .   ? -20.479 -28.478 20.484 1.00 33.12 ? 4183 HOH A O   1 
HETATM 7199 O O   . HOH J 5 .   ? 10.655  -41.095 59.325 1.00 35.06 ? 4184 HOH A O   1 
HETATM 7200 O O   . HOH J 5 .   ? -10.179 -19.419 11.389 1.00 26.13 ? 4185 HOH A O   1 
HETATM 7201 O O   . HOH J 5 .   ? -22.542 5.416   33.313 1.00 20.32 ? 4186 HOH A O   1 
HETATM 7202 O O   . HOH J 5 .   ? -18.251 19.769  25.109 1.00 21.65 ? 4188 HOH A O   1 
HETATM 7203 O O   . HOH J 5 .   ? -16.100 -36.098 49.470 1.00 27.43 ? 4189 HOH A O   1 
HETATM 7204 O O   . HOH J 5 .   ? -15.955 -21.812 59.356 1.00 28.73 ? 4194 HOH A O   1 
HETATM 7205 O O   . HOH J 5 .   ? -5.897  1.593   52.621 1.00 34.95 ? 4195 HOH A O   1 
HETATM 7206 O O   . HOH J 5 .   ? -21.466 -5.040  58.182 1.00 33.76 ? 4196 HOH A O   1 
HETATM 7207 O O   . HOH J 5 .   ? 10.820  6.574   30.890 1.00 24.32 ? 4197 HOH A O   1 
HETATM 7208 O O   . HOH J 5 .   ? 0.049   -20.917 25.223 1.00 22.00 ? 4198 HOH A O   1 
HETATM 7209 O O   . HOH J 5 .   ? -49.784 6.754   28.770 1.00 29.65 ? 4199 HOH A O   1 
HETATM 7210 O O   . HOH J 5 .   ? -2.587  -26.532 29.479 1.00 22.41 ? 4200 HOH A O   1 
HETATM 7211 O O   . HOH J 5 .   ? 21.672  -21.361 35.631 1.00 27.16 ? 4201 HOH A O   1 
HETATM 7212 O O   . HOH J 5 .   ? -19.078 -19.103 61.866 1.00 23.08 ? 4202 HOH A O   1 
HETATM 7213 O O   . HOH J 5 .   ? -24.687 -6.773  53.104 1.00 23.53 ? 4203 HOH A O   1 
HETATM 7214 O O   . HOH J 5 .   ? -2.479  5.436   0.909  1.00 25.88 ? 4204 HOH A O   1 
HETATM 7215 O O   . HOH J 5 .   ? -7.241  -35.502 48.877 1.00 32.80 ? 4205 HOH A O   1 
HETATM 7216 O O   . HOH J 5 .   ? -8.306  -26.291 11.678 1.00 27.23 ? 4206 HOH A O   1 
HETATM 7217 O O   . HOH J 5 .   ? -26.349 -21.404 24.968 1.00 26.96 ? 4207 HOH A O   1 
HETATM 7218 O O   . HOH J 5 .   ? 7.164   -27.094 59.619 1.00 27.13 ? 4208 HOH A O   1 
HETATM 7219 O O   . HOH J 5 .   ? 4.800   -15.458 71.706 1.00 21.33 ? 4209 HOH A O   1 
HETATM 7220 O O   . HOH J 5 .   ? 4.222   -11.915 36.210 1.00 19.03 ? 4210 HOH A O   1 
HETATM 7221 O O   . HOH J 5 .   ? -32.112 16.125  18.985 1.00 25.72 ? 4212 HOH A O   1 
HETATM 7222 O O   . HOH J 5 .   ? -33.941 -10.898 45.073 1.00 25.34 ? 4213 HOH A O   1 
HETATM 7223 O O   . HOH J 5 .   ? 6.902   -12.553 6.058  1.00 19.88 ? 4214 HOH A O   1 
HETATM 7224 O O   . HOH J 5 .   ? -6.040  -40.676 49.425 1.00 26.24 ? 4215 HOH A O   1 
HETATM 7225 O O   . HOH J 5 .   ? -20.588 -23.308 10.884 1.00 26.86 ? 4216 HOH A O   1 
HETATM 7226 O O   . HOH J 5 .   ? -44.749 6.514   33.969 1.00 25.98 ? 4217 HOH A O   1 
HETATM 7227 O O   . HOH J 5 .   ? 12.463  -9.614  34.894 1.00 24.92 ? 4218 HOH A O   1 
HETATM 7228 O O   . HOH J 5 .   ? 4.160   -6.462  1.370  1.00 27.50 ? 4219 HOH A O   1 
HETATM 7229 O O   . HOH J 5 .   ? 0.845   -9.846  12.264 1.00 26.34 ? 4220 HOH A O   1 
HETATM 7230 O O   . HOH J 5 .   ? -9.368  -26.556 32.515 1.00 24.10 ? 4221 HOH A O   1 
HETATM 7231 O O   . HOH J 5 .   ? -9.464  2.068   58.780 1.00 28.86 ? 4222 HOH A O   1 
HETATM 7232 O O   . HOH J 5 .   ? -6.222  -28.614 38.340 1.00 30.72 ? 4223 HOH A O   1 
HETATM 7233 O O   . HOH J 5 .   ? 0.301   -0.871  51.427 1.00 31.23 ? 4224 HOH A O   1 
HETATM 7234 O O   . HOH J 5 .   ? -8.943  -31.201 60.226 1.00 27.31 ? 4225 HOH A O   1 
HETATM 7235 O O   . HOH J 5 .   ? 21.159  1.894   25.388 1.00 27.35 ? 4226 HOH A O   1 
HETATM 7236 O O   . HOH J 5 .   ? -22.731 -21.987 9.646  1.00 31.01 ? 4227 HOH A O   1 
HETATM 7237 O O   . HOH J 5 .   ? -8.601  1.851   53.270 1.00 30.60 ? 4228 HOH A O   1 
HETATM 7238 O O   . HOH J 5 .   ? -1.489  -0.406  49.075 1.00 21.57 ? 4229 HOH A O   1 
HETATM 7239 O O   . HOH J 5 .   ? -0.782  -17.351 8.313  1.00 22.84 ? 4230 HOH A O   1 
HETATM 7240 O O   . HOH J 5 .   ? 4.158   -4.115  73.992 1.00 27.77 ? 4231 HOH A O   1 
HETATM 7241 O O   . HOH J 5 .   ? -28.197 24.925  27.357 1.00 34.92 ? 4232 HOH A O   1 
HETATM 7242 O O   . HOH J 5 .   ? -11.355 -4.629  38.088 1.00 18.49 ? 4233 HOH A O   1 
HETATM 7243 O O   . HOH J 5 .   ? -1.461  2.954   30.757 1.00 35.93 ? 4234 HOH A O   1 
HETATM 7244 O O   . HOH J 5 .   ? -16.394 -27.277 19.302 1.00 27.36 ? 4235 HOH A O   1 
HETATM 7245 O O   . HOH J 5 .   ? -20.573 20.946  25.720 1.00 26.33 ? 4236 HOH A O   1 
HETATM 7246 O O   . HOH J 5 .   ? -37.360 -20.198 37.378 1.00 26.64 ? 4237 HOH A O   1 
HETATM 7247 O O   . HOH J 5 .   ? 0.447   1.447   31.877 1.00 28.06 ? 4238 HOH A O   1 
HETATM 7248 O O   . HOH J 5 .   ? -8.008  -24.281 24.289 1.00 30.18 ? 4240 HOH A O   1 
HETATM 7249 O O   . HOH J 5 .   ? -10.155 -19.302 27.515 1.00 30.79 ? 4241 HOH A O   1 
HETATM 7250 O O   . HOH J 5 .   ? 11.653  -11.715 8.382  1.00 28.29 ? 4242 HOH A O   1 
HETATM 7251 O O   . HOH J 5 .   ? -24.035 -28.017 23.585 1.00 33.06 ? 4243 HOH A O   1 
HETATM 7252 O O   . HOH J 5 .   ? 8.186   -11.162 7.616  1.00 28.31 ? 4244 HOH A O   1 
HETATM 7253 O O   . HOH J 5 .   ? 12.692  -32.737 40.066 1.00 26.99 ? 4245 HOH A O   1 
HETATM 7254 O O   . HOH J 5 .   ? -39.183 20.570  19.013 1.00 30.88 ? 4246 HOH A O   1 
HETATM 7255 O O   . HOH J 5 .   ? -23.758 6.467   13.696 1.00 27.35 ? 4247 HOH A O   1 
HETATM 7256 O O   . HOH J 5 .   ? -36.163 -9.522  25.187 1.00 27.97 ? 4248 HOH A O   1 
HETATM 7257 O O   . HOH J 5 .   ? -8.802  -8.689  67.332 1.00 26.32 ? 4249 HOH A O   1 
HETATM 7258 O O   . HOH J 5 .   ? -26.393 16.729  20.043 1.00 45.09 ? 4250 HOH A O   1 
HETATM 7259 O O   . HOH J 5 .   ? 4.687   -6.421  50.386 1.00 22.06 ? 4251 HOH A O   1 
HETATM 7260 O O   . HOH J 5 .   ? 25.454  1.069   24.259 1.00 39.45 ? 4253 HOH A O   1 
HETATM 7261 O O   . HOH J 5 .   ? -26.351 -1.384  16.064 1.00 21.28 ? 4254 HOH A O   1 
HETATM 7262 O O   . HOH J 5 .   ? -10.026 -0.547  54.035 1.00 25.72 ? 4255 HOH A O   1 
HETATM 7263 O O   . HOH J 5 .   ? -44.891 -3.398  27.327 1.00 40.37 ? 4256 HOH A O   1 
HETATM 7264 O O   . HOH J 5 .   ? -9.317  5.973   17.276 1.00 26.13 ? 4257 HOH A O   1 
HETATM 7265 O O   . HOH J 5 .   ? 23.845  1.787   19.666 1.00 32.88 ? 4258 HOH A O   1 
HETATM 7266 O O   . HOH J 5 .   ? -4.580  5.394   34.830 1.00 26.96 ? 4259 HOH A O   1 
HETATM 7267 O O   . HOH J 5 .   ? -18.228 -27.279 45.883 1.00 27.78 ? 4260 HOH A O   1 
HETATM 7268 O O   . HOH J 5 .   ? -19.600 -1.553  42.252 1.00 26.41 ? 4261 HOH A O   1 
HETATM 7269 O O   . HOH J 5 .   ? 13.070  -21.489 49.503 1.00 24.42 ? 4262 HOH A O   1 
HETATM 7270 O O   . HOH J 5 .   ? 26.225  -9.391  31.306 1.00 33.35 ? 4263 HOH A O   1 
HETATM 7271 O O   . HOH J 5 .   ? -29.769 -20.346 38.100 1.00 37.79 ? 4264 HOH A O   1 
HETATM 7272 O O   . HOH J 5 .   ? -6.158  9.241   34.592 1.00 32.81 ? 4265 HOH A O   1 
HETATM 7273 O O   . HOH J 5 .   ? -2.725  -29.218 28.729 1.00 29.48 ? 4266 HOH A O   1 
HETATM 7274 O O   . HOH J 5 .   ? -36.447 0.697   18.618 1.00 32.74 ? 4267 HOH A O   1 
HETATM 7275 O O   . HOH J 5 .   ? -24.981 -4.426  10.287 1.00 28.02 ? 4268 HOH A O   1 
HETATM 7276 O O   . HOH J 5 .   ? -24.339 -15.570 5.607  1.00 34.76 ? 4269 HOH A O   1 
HETATM 7277 O O   . HOH J 5 .   ? -1.478  -47.765 50.390 1.00 27.45 ? 4270 HOH A O   1 
HETATM 7278 O O   . HOH J 5 .   ? -20.970 -22.341 29.872 1.00 52.68 ? 4271 HOH A O   1 
HETATM 7279 O O   . HOH J 5 .   ? 25.082  -18.966 30.569 1.00 32.61 ? 4272 HOH A O   1 
HETATM 7280 O O   . HOH J 5 .   ? 25.069  -14.480 24.501 1.00 32.25 ? 4273 HOH A O   1 
HETATM 7281 O O   . HOH J 5 .   ? -24.620 -19.909 33.925 1.00 21.93 ? 4274 HOH A O   1 
HETATM 7282 O O   . HOH J 5 .   ? -32.685 -3.496  40.431 1.00 22.91 ? 4275 HOH A O   1 
HETATM 7283 O O   . HOH J 5 .   ? -43.120 -0.964  30.407 1.00 24.88 ? 4276 HOH A O   1 
HETATM 7284 O O   . HOH J 5 .   ? 23.758  -9.312  31.938 1.00 22.23 ? 4277 HOH A O   1 
HETATM 7285 O O   . HOH J 5 .   ? 8.051   -39.078 54.820 1.00 40.56 ? 4278 HOH A O   1 
HETATM 7286 O O   . HOH J 5 .   ? -11.685 -14.502 65.925 1.00 34.37 ? 4279 HOH A O   1 
HETATM 7287 O O   . HOH J 5 .   ? -2.109  -22.424 16.824 1.00 34.11 ? 4280 HOH A O   1 
HETATM 7288 O O   . HOH J 5 .   ? -9.111  18.275  25.099 1.00 26.35 ? 4281 HOH A O   1 
HETATM 7289 O O   . HOH J 5 .   ? -27.248 -9.033  14.314 1.00 26.91 ? 4282 HOH A O   1 
HETATM 7290 O O   . HOH J 5 .   ? -42.363 8.456   33.723 1.00 37.17 ? 4284 HOH A O   1 
HETATM 7291 O O   . HOH J 5 .   ? -27.719 -18.494 29.793 1.00 30.53 ? 4285 HOH A O   1 
HETATM 7292 O O   . HOH J 5 .   ? -27.894 -17.311 52.392 1.00 32.40 ? 4286 HOH A O   1 
HETATM 7293 O O   . HOH J 5 .   ? 13.005  5.127   31.383 1.00 28.64 ? 4287 HOH A O   1 
HETATM 7294 O O   . HOH J 5 .   ? 11.777  -13.588 21.373 1.00 25.17 ? 4288 HOH A O   1 
HETATM 7295 O O   . HOH J 5 .   ? 25.959  -15.843 27.435 1.00 30.59 ? 4289 HOH A O   1 
HETATM 7296 O O   . HOH J 5 .   ? -6.836  -3.772  33.024 1.00 30.38 ? 4290 HOH A O   1 
HETATM 7297 O O   . HOH J 5 .   ? 1.303   -18.673 7.419  1.00 37.20 ? 4291 HOH A O   1 
HETATM 7298 O O   . HOH J 5 .   ? -17.494 -17.141 66.290 1.00 39.60 ? 4292 HOH A O   1 
HETATM 7299 O O   . HOH J 5 .   ? 23.876  -31.169 37.687 1.00 29.35 ? 4293 HOH A O   1 
HETATM 7300 O O   . HOH J 5 .   ? -13.362 -16.641 6.487  1.00 32.80 ? 4294 HOH A O   1 
HETATM 7301 O O   . HOH J 5 .   ? 7.441   -8.136  63.034 1.00 33.65 ? 4295 HOH A O   1 
HETATM 7302 O O   . HOH J 5 .   ? 15.623  -19.507 47.043 1.00 43.86 ? 4296 HOH A O   1 
HETATM 7303 O O   . HOH J 5 .   ? -41.739 0.251   35.021 1.00 39.76 ? 4297 HOH A O   1 
HETATM 7304 O O   . HOH J 5 .   ? 16.411  -14.198 13.807 1.00 28.13 ? 4298 HOH A O   1 
HETATM 7305 O O   . HOH J 5 .   ? -32.468 22.130  24.959 1.00 35.24 ? 4299 HOH A O   1 
HETATM 7306 O O   . HOH J 5 .   ? 8.999   -6.947  51.838 1.00 27.75 ? 4300 HOH A O   1 
HETATM 7307 O O   . HOH J 5 .   ? -9.898  7.925   20.911 1.00 28.85 ? 4301 HOH A O   1 
HETATM 7308 O O   . HOH J 5 .   ? -18.849 -4.349  62.810 1.00 31.22 ? 4302 HOH A O   1 
HETATM 7309 O O   . HOH J 5 .   ? 7.699   -37.248 47.777 1.00 37.94 ? 4303 HOH A O   1 
HETATM 7310 O O   . HOH J 5 .   ? 3.192   7.877   29.441 1.00 27.15 ? 4304 HOH A O   1 
HETATM 7311 O O   . HOH J 5 .   ? -15.818 -8.327  2.767  1.00 30.75 ? 4305 HOH A O   1 
HETATM 7312 O O   . HOH J 5 .   ? 20.375  -7.368  36.221 1.00 25.88 ? 4306 HOH A O   1 
HETATM 7313 O O   . HOH J 5 .   ? -15.655 -37.731 47.428 1.00 36.33 ? 4307 HOH A O   1 
HETATM 7314 O O   . HOH J 5 .   ? 6.708   -33.486 44.269 1.00 27.88 ? 4308 HOH A O   1 
HETATM 7315 O O   . HOH J 5 .   ? -41.466 -5.451  21.777 1.00 41.56 ? 4309 HOH A O   1 
HETATM 7316 O O   . HOH J 5 .   ? 9.848   -4.639  18.335 1.00 22.24 ? 4310 HOH A O   1 
HETATM 7317 O O   . HOH J 5 .   ? 10.218  11.859  25.452 1.00 34.89 ? 4311 HOH A O   1 
HETATM 7318 O O   . HOH J 5 .   ? -14.929 -27.243 58.863 1.00 38.52 ? 4312 HOH A O   1 
HETATM 7319 O O   . HOH J 5 .   ? -20.672 3.947   36.870 1.00 36.69 ? 4313 HOH A O   1 
HETATM 7320 O O   . HOH J 5 .   ? 14.434  -28.595 26.048 1.00 33.44 ? 4314 HOH A O   1 
HETATM 7321 O O   . HOH J 5 .   ? -3.418  -23.660 62.418 1.00 25.88 ? 4315 HOH A O   1 
HETATM 7322 O O   . HOH J 5 .   ? 7.119   -7.440  68.817 1.00 41.17 ? 4316 HOH A O   1 
HETATM 7323 O O   . HOH J 5 .   ? -4.352  7.680   33.625 1.00 35.18 ? 4317 HOH A O   1 
HETATM 7324 O O   . HOH J 5 .   ? -26.062 -1.232  41.659 1.00 30.03 ? 4318 HOH A O   1 
HETATM 7325 O O   . HOH J 5 .   ? 7.286   -9.678  -0.194 1.00 38.02 ? 4319 HOH A O   1 
HETATM 7326 O O   . HOH J 5 .   ? -24.390 24.404  35.337 1.00 33.79 ? 4320 HOH A O   1 
HETATM 7327 O O   . HOH J 5 .   ? 6.489   -13.949 8.023  1.00 31.56 ? 4321 HOH A O   1 
HETATM 7328 O O   . HOH J 5 .   ? 0.985   -41.913 63.226 1.00 35.14 ? 4322 HOH A O   1 
HETATM 7329 O O   . HOH J 5 .   ? -28.655 -22.973 24.219 1.00 29.39 ? 4323 HOH A O   1 
HETATM 7330 O O   . HOH J 5 .   ? -40.395 8.916   35.479 1.00 39.94 ? 4324 HOH A O   1 
HETATM 7331 O O   . HOH J 5 .   ? -22.237 -22.860 51.314 1.00 41.67 ? 4325 HOH A O   1 
HETATM 7332 O O   . HOH J 5 .   ? -18.906 -28.585 22.464 1.00 35.43 ? 4327 HOH A O   1 
HETATM 7333 O O   . HOH J 5 .   ? 19.121  -15.496 17.684 1.00 23.08 ? 4329 HOH A O   1 
HETATM 7334 O O   . HOH J 5 .   ? 6.388   1.914   35.882 1.00 31.75 ? 4330 HOH A O   1 
HETATM 7335 O O   . HOH J 5 .   ? -18.063 -26.324 28.045 1.00 33.30 ? 4331 HOH A O   1 
HETATM 7336 O O   . HOH J 5 .   ? -26.828 -10.029 57.360 1.00 39.67 ? 4332 HOH A O   1 
HETATM 7337 O O   . HOH J 5 .   ? -12.954 2.305   47.255 1.00 34.03 ? 4333 HOH A O   1 
HETATM 7338 O O   . HOH J 5 .   ? 7.051   -11.713 69.664 1.00 33.97 ? 4334 HOH A O   1 
HETATM 7339 O O   . HOH J 5 .   ? 10.232  0.591   4.306  1.00 30.91 ? 4337 HOH A O   1 
HETATM 7340 O O   . HOH J 5 .   ? -4.588  2.140   60.603 1.00 25.40 ? 4338 HOH A O   1 
HETATM 7341 O O   . HOH J 5 .   ? 25.898  -10.282 26.752 1.00 35.52 ? 4339 HOH A O   1 
HETATM 7342 O O   . HOH J 5 .   ? 8.787   -7.870  70.661 1.00 38.24 ? 4340 HOH A O   1 
HETATM 7343 O O   . HOH J 5 .   ? 2.849   -17.457 43.253 1.00 32.04 ? 4341 HOH A O   1 
HETATM 7344 O O   . HOH J 5 .   ? 9.020   -5.486  -0.991 1.00 34.60 ? 4342 HOH A O   1 
HETATM 7345 O O   . HOH J 5 .   ? 11.365  -38.787 58.032 1.00 51.55 ? 4343 HOH A O   1 
HETATM 7346 O O   . HOH J 5 .   ? -40.991 -11.016 27.706 1.00 33.80 ? 4345 HOH A O   1 
HETATM 7347 O O   . HOH J 5 .   ? 1.619   8.520   11.615 1.00 32.30 ? 4346 HOH A O   1 
HETATM 7348 O O   . HOH J 5 .   ? -12.195 -1.723  66.865 1.00 30.86 ? 4347 HOH A O   1 
HETATM 7349 O O   . HOH J 5 .   ? 0.548   2.802   34.507 1.00 36.38 ? 4348 HOH A O   1 
HETATM 7350 O O   . HOH J 5 .   ? 0.237   -27.759 71.265 1.00 42.66 ? 4349 HOH A O   1 
HETATM 7351 O O   . HOH J 5 .   ? 1.636   -10.474 -0.128 1.00 33.70 ? 4350 HOH A O   1 
HETATM 7352 O O   . HOH J 5 .   ? 9.248   -8.459  65.649 1.00 41.28 ? 4352 HOH A O   1 
HETATM 7353 O O   . HOH J 5 .   ? 17.705  -30.207 36.768 1.00 28.62 ? 4353 HOH A O   1 
HETATM 7354 O O   . HOH J 5 .   ? -17.091 -6.023  69.414 1.00 33.86 ? 4354 HOH A O   1 
HETATM 7355 O O   . HOH J 5 .   ? -13.574 4.980   8.898  1.00 39.43 ? 4355 HOH A O   1 
HETATM 7356 O O   . HOH J 5 .   ? 0.007   -35.154 62.143 1.00 31.89 ? 4356 HOH A O   1 
HETATM 7357 O O   . HOH J 5 .   ? 14.914  -27.498 51.373 1.00 33.77 ? 4357 HOH A O   1 
HETATM 7358 O O   . HOH J 5 .   ? -2.598  -4.801  -0.069 1.00 36.03 ? 4358 HOH A O   1 
HETATM 7359 O O   . HOH J 5 .   ? -14.036 10.267  42.772 1.00 44.25 ? 4359 HOH A O   1 
HETATM 7360 O O   . HOH J 5 .   ? -5.205  7.787   3.781  1.00 44.74 ? 4360 HOH A O   1 
HETATM 7361 O O   . HOH J 5 .   ? 3.667   -25.694 26.738 1.00 33.56 ? 4361 HOH A O   1 
HETATM 7362 O O   . HOH J 5 .   ? -11.612 -45.207 50.457 1.00 27.47 ? 4362 HOH A O   1 
HETATM 7363 O O   . HOH J 5 .   ? -4.244  2.834   38.894 1.00 22.34 ? 4363 HOH A O   1 
HETATM 7364 O O   . HOH J 5 .   ? -12.278 0.666   49.450 1.00 42.07 ? 4364 HOH A O   1 
HETATM 7365 O O   . HOH J 5 .   ? -34.374 -10.498 47.659 1.00 36.22 ? 4365 HOH A O   1 
HETATM 7366 O O   . HOH J 5 .   ? -50.884 5.871   26.264 1.00 30.36 ? 4366 HOH A O   1 
HETATM 7367 O O   . HOH J 5 .   ? 12.217  2.893   8.140  1.00 30.69 ? 4367 HOH A O   1 
HETATM 7368 O O   . HOH J 5 .   ? -8.396  4.286   62.317 1.00 31.39 ? 4368 HOH A O   1 
HETATM 7369 O O   . HOH J 5 .   ? -27.902 1.216   19.769 1.00 31.72 ? 4369 HOH A O   1 
HETATM 7370 O O   . HOH J 5 .   ? -33.975 3.773   41.014 1.00 31.95 ? 4371 HOH A O   1 
HETATM 7371 O O   . HOH J 5 .   ? 11.333  -12.514 60.598 1.00 40.78 ? 4372 HOH A O   1 
HETATM 7372 O O   . HOH J 5 .   ? -0.881  -31.478 34.130 1.00 37.55 ? 4373 HOH A O   1 
HETATM 7373 O O   . HOH J 5 .   ? -13.262 12.649  13.209 1.00 44.91 ? 4374 HOH A O   1 
HETATM 7374 O O   . HOH J 5 .   ? 26.525  -20.765 35.197 1.00 36.08 ? 4375 HOH A O   1 
HETATM 7375 O O   . HOH J 5 .   ? 9.205   4.304   4.537  1.00 40.37 ? 4376 HOH A O   1 
HETATM 7376 O O   . HOH J 5 .   ? -9.629  10.631  20.564 1.00 27.20 ? 4377 HOH A O   1 
HETATM 7377 O O   . HOH J 5 .   ? -15.450 -22.313 61.938 1.00 40.48 ? 4378 HOH A O   1 
HETATM 7378 O O   . HOH J 5 .   ? 14.042  -10.445 53.278 1.00 43.37 ? 4379 HOH A O   1 
HETATM 7379 O O   . HOH J 5 .   ? 13.411  -10.487 49.786 1.00 29.04 ? 4380 HOH A O   1 
HETATM 7380 O O   . HOH J 5 .   ? 5.019   -3.932  1.361  1.00 37.16 ? 4381 HOH A O   1 
HETATM 7381 O O   . HOH J 5 .   ? -29.457 -8.926  45.537 1.00 23.89 ? 4382 HOH A O   1 
HETATM 7382 O O   . HOH J 5 .   ? -48.073 9.935   21.227 1.00 30.13 ? 4383 HOH A O   1 
HETATM 7383 O O   . HOH J 5 .   ? -2.344  2.948   37.051 1.00 24.23 ? 4384 HOH A O   1 
HETATM 7384 O O   . HOH J 5 .   ? -15.173 3.095   48.261 1.00 43.10 ? 4385 HOH A O   1 
HETATM 7385 O O   . HOH J 5 .   ? 24.143  -26.717 41.192 1.00 34.16 ? 4386 HOH A O   1 
HETATM 7386 O O   . HOH J 5 .   ? -10.239 -26.683 24.045 1.00 41.56 ? 4387 HOH A O   1 
HETATM 7387 O O   . HOH J 5 .   ? 8.180   -15.638 73.689 1.00 32.80 ? 4388 HOH A O   1 
HETATM 7388 O O   . HOH J 5 .   ? -28.506 -7.392  52.086 1.00 30.84 ? 4390 HOH A O   1 
HETATM 7389 O O   . HOH J 5 .   ? -17.779 24.367  22.147 1.00 39.68 ? 4391 HOH A O   1 
HETATM 7390 O O   . HOH J 5 .   ? 21.371  -24.726 36.107 1.00 32.16 ? 4392 HOH A O   1 
HETATM 7391 O O   . HOH J 5 .   ? 10.519  -18.915 15.035 1.00 31.60 ? 4393 HOH A O   1 
HETATM 7392 O O   . HOH J 5 .   ? -36.885 3.394   43.463 1.00 35.46 ? 4394 HOH A O   1 
HETATM 7393 O O   . HOH J 5 .   ? -4.845  17.428  31.538 1.00 37.99 ? 4395 HOH A O   1 
HETATM 7394 O O   . HOH J 5 .   ? -41.529 -5.876  37.768 1.00 31.08 ? 4396 HOH A O   1 
HETATM 7395 O O   . HOH J 5 .   ? -8.562  7.905   23.157 1.00 23.95 ? 4397 HOH A O   1 
HETATM 7396 O O   . HOH J 5 .   ? -11.455 -4.090  0.589  1.00 34.58 ? 4398 HOH A O   1 
HETATM 7397 O O   . HOH J 5 .   ? -4.298  16.216  33.635 1.00 35.24 ? 4399 HOH A O   1 
HETATM 7398 O O   . HOH J 5 .   ? -21.482 -24.983 13.167 1.00 33.70 ? 4401 HOH A O   1 
HETATM 7399 O O   . HOH J 5 .   ? -26.752 3.589   18.395 1.00 31.08 ? 4402 HOH A O   1 
HETATM 7400 O O   . HOH J 5 .   ? 4.508   -32.504 40.078 1.00 29.09 ? 4404 HOH A O   1 
HETATM 7401 O O   . HOH J 5 .   ? -9.848  -9.163  0.560  1.00 34.77 ? 4405 HOH A O   1 
HETATM 7402 O O   . HOH J 5 .   ? -48.996 14.162  35.860 1.00 47.88 ? 4406 HOH A O   1 
HETATM 7403 O O   . HOH J 5 .   ? 0.172   1.618   48.307 1.00 29.13 ? 4407 HOH A O   1 
HETATM 7404 O O   . HOH J 5 .   ? 4.034   -4.676  62.659 1.00 32.18 ? 4408 HOH A O   1 
HETATM 7405 O O   . HOH J 5 .   ? 8.845   -26.571 71.731 1.00 44.68 ? 4409 HOH A O   1 
HETATM 7406 O O   . HOH J 5 .   ? -23.310 17.293  20.290 1.00 36.95 ? 4410 HOH A O   1 
HETATM 7407 O O   . HOH J 5 .   ? 8.388   -18.206 41.107 1.00 20.48 ? 4411 HOH A O   1 
HETATM 7408 O O   . HOH J 5 .   ? -3.451  1.456   50.131 1.00 32.89 ? 4412 HOH A O   1 
HETATM 7409 O O   . HOH J 5 .   ? -20.478 -31.320 46.440 1.00 57.29 ? 4413 HOH A O   1 
HETATM 7410 O O   . HOH J 5 .   ? -14.035 10.807  27.680 1.00 22.51 ? 4414 HOH A O   1 
HETATM 7411 O O   . HOH J 5 .   ? -16.417 -27.919 22.120 1.00 28.54 ? 4415 HOH A O   1 
HETATM 7412 O O   . HOH J 5 .   ? -19.509 -25.343 14.969 1.00 31.15 ? 4416 HOH A O   1 
HETATM 7413 O O   . HOH J 5 .   ? -5.647  -24.417 67.401 1.00 41.41 ? 4417 HOH A O   1 
HETATM 7414 O O   . HOH J 5 .   ? -21.214 4.342   40.632 1.00 35.46 ? 4418 HOH A O   1 
HETATM 7415 O O   . HOH J 5 .   ? -25.668 -7.076  55.876 1.00 46.77 ? 4419 HOH A O   1 
HETATM 7416 O O   . HOH J 5 .   ? -10.072 -27.554 12.388 1.00 39.46 ? 4420 HOH A O   1 
HETATM 7417 O O   . HOH J 5 .   ? 18.205  -33.835 37.608 1.00 26.50 ? 4421 HOH A O   1 
HETATM 7418 O O   . HOH J 5 .   ? 7.688   -22.335 25.685 1.00 30.53 ? 4422 HOH A O   1 
HETATM 7419 O O   . HOH J 5 .   ? -10.668 -41.963 49.653 1.00 26.79 ? 4423 HOH A O   1 
HETATM 7420 O O   . HOH J 5 .   ? -0.487  -29.313 27.250 1.00 53.63 ? 4424 HOH A O   1 
HETATM 7421 O O   . HOH J 5 .   ? -15.249 21.068  39.677 1.00 34.73 ? 4425 HOH A O   1 
HETATM 7422 O O   . HOH J 5 .   ? 16.611  5.346   28.198 1.00 33.72 ? 4426 HOH A O   1 
HETATM 7423 O O   . HOH J 5 .   ? -13.821 -5.416  0.318  1.00 41.37 ? 4427 HOH A O   1 
HETATM 7424 O O   . HOH J 5 .   ? 7.239   -24.114 23.588 1.00 43.42 ? 4428 HOH A O   1 
HETATM 7425 O O   . HOH J 5 .   ? -13.578 -26.747 37.699 1.00 36.49 ? 4430 HOH A O   1 
HETATM 7426 O O   . HOH J 5 .   ? -8.510  10.670  23.355 1.00 29.63 ? 4431 HOH A O   1 
HETATM 7427 O O   . HOH J 5 .   ? -25.721 -12.426 57.917 1.00 43.64 ? 4432 HOH A O   1 
HETATM 7428 O O   . HOH J 5 .   ? -18.023 -19.755 59.342 1.00 31.21 ? 4433 HOH A O   1 
HETATM 7429 O O   . HOH J 5 .   ? -15.558 -0.120  57.719 1.00 28.47 ? 4434 HOH A O   1 
HETATM 7430 O O   . HOH J 5 .   ? -35.309 -8.107  20.534 1.00 33.93 ? 4435 HOH A O   1 
HETATM 7431 O O   . HOH J 5 .   ? 4.478   -28.068 61.510 1.00 33.75 ? 4436 HOH A O   1 
HETATM 7432 O O   . HOH J 5 .   ? -2.101  -31.573 29.661 1.00 47.64 ? 4437 HOH A O   1 
HETATM 7433 O O   . HOH J 5 .   ? 13.985  -20.687 63.017 1.00 29.60 ? 4438 HOH A O   1 
HETATM 7434 O O   . HOH J 5 .   ? 3.357   -29.978 28.040 1.00 41.76 ? 4439 HOH A O   1 
HETATM 7435 O O   . HOH J 5 .   ? 6.187   2.245   38.408 1.00 42.85 ? 4440 HOH A O   1 
HETATM 7436 O O   . HOH J 5 .   ? -13.956 -22.053 39.529 1.00 22.77 ? 4441 HOH A O   1 
HETATM 7437 O O   . HOH J 5 .   ? 15.322  6.292   30.332 1.00 32.88 ? 4442 HOH A O   1 
HETATM 7438 O O   . HOH J 5 .   ? 15.187  -23.317 62.128 1.00 34.16 ? 4443 HOH A O   1 
HETATM 7439 O O   . HOH J 5 .   ? -44.074 -0.618  18.729 1.00 53.13 ? 4444 HOH A O   1 
HETATM 7440 O O   . HOH J 5 .   ? -38.675 -6.910  22.407 1.00 40.50 ? 4445 HOH A O   1 
HETATM 7441 O O   . HOH J 5 .   ? 16.244  -4.732  9.914  1.00 36.38 ? 4446 HOH A O   1 
HETATM 7442 O O   . HOH J 5 .   ? -15.382 -17.688 5.517  1.00 46.65 ? 4447 HOH A O   1 
HETATM 7443 O O   . HOH J 5 .   ? -33.408 6.086   42.296 1.00 53.12 ? 4448 HOH A O   1 
HETATM 7444 O O   . HOH J 5 .   ? -26.441 -16.702 6.755  1.00 46.73 ? 4449 HOH A O   1 
HETATM 7445 O O   . HOH J 5 .   ? 2.414   4.310   0.343  1.00 38.26 ? 4450 HOH A O   1 
HETATM 7446 O O   . HOH J 5 .   ? -34.895 0.166   41.912 1.00 36.17 ? 4451 HOH A O   1 
HETATM 7447 O O   . HOH J 5 .   ? 27.522  -7.379  21.275 1.00 42.42 ? 4452 HOH A O   1 
HETATM 7448 O O   . HOH J 5 .   ? 3.572   2.966   43.686 1.00 42.49 ? 4453 HOH A O   1 
HETATM 7449 O O   . HOH J 5 .   ? 2.869   7.476   18.584 1.00 32.42 ? 4454 HOH A O   1 
HETATM 7450 O O   . HOH J 5 .   ? -22.718 -8.631  67.405 1.00 39.42 ? 4455 HOH A O   1 
HETATM 7451 O O   . HOH J 5 .   ? 5.398   -0.993  68.051 1.00 31.85 ? 4456 HOH A O   1 
HETATM 7452 O O   . HOH J 5 .   ? -17.879 -4.422  2.500  1.00 40.72 ? 4457 HOH A O   1 
HETATM 7453 O O   . HOH J 5 .   ? 25.856  -0.255  19.827 1.00 41.87 ? 4458 HOH A O   1 
HETATM 7454 O O   . HOH J 5 .   ? 15.456  -18.987 52.315 1.00 45.79 ? 4459 HOH A O   1 
HETATM 7455 O O   . HOH J 5 .   ? -27.145 -18.415 32.751 1.00 27.85 ? 4460 HOH A O   1 
HETATM 7456 O O   . HOH J 5 .   ? -33.637 0.623   44.700 1.00 45.42 ? 4463 HOH A O   1 
HETATM 7457 O O   . HOH J 5 .   ? -45.934 0.463   17.276 1.00 39.98 ? 4464 HOH A O   1 
HETATM 7458 O O   . HOH J 5 .   ? -4.037  1.215   6.849  1.00 35.33 ? 4465 HOH A O   1 
HETATM 7459 O O   . HOH J 5 .   ? -9.190  -5.698  0.915  1.00 31.81 ? 4466 HOH A O   1 
HETATM 7460 O O   . HOH J 5 .   ? 15.555  -22.023 49.363 1.00 37.26 ? 4467 HOH A O   1 
HETATM 7461 O O   . HOH J 5 .   ? -20.826 -23.581 38.918 1.00 47.86 ? 4468 HOH A O   1 
HETATM 7462 O O   . HOH J 5 .   ? -17.812 -34.278 48.299 1.00 48.28 ? 4469 HOH A O   1 
HETATM 7463 O O   . HOH J 5 .   ? -5.243  9.755   14.180 1.00 38.84 ? 4470 HOH A O   1 
HETATM 7464 O O   . HOH J 5 .   ? -32.557 -7.501  43.328 1.00 31.22 ? 4471 HOH A O   1 
HETATM 7465 O O   . HOH J 5 .   ? -33.697 8.791   41.650 1.00 34.29 ? 4472 HOH A O   1 
HETATM 7466 O O   . HOH J 5 .   ? -28.913 14.145  39.601 1.00 29.89 ? 4473 HOH A O   1 
HETATM 7467 O O   . HOH J 5 .   ? 20.670  -11.854 42.518 1.00 40.62 ? 4474 HOH A O   1 
HETATM 7468 O O   . HOH J 5 .   ? -30.400 3.183   22.362 1.00 50.91 ? 4475 HOH A O   1 
HETATM 7469 O O   . HOH J 5 .   ? -5.202  -25.649 20.856 1.00 38.58 ? 4476 HOH A O   1 
HETATM 7470 O O   . HOH J 5 .   ? 2.594   -32.622 43.020 1.00 33.93 ? 4477 HOH A O   1 
HETATM 7471 O O   . HOH J 5 .   ? -31.582 2.936   41.099 1.00 34.01 ? 4478 HOH A O   1 
HETATM 7472 O O   . HOH J 5 .   ? -11.132 20.126  41.607 1.00 39.66 ? 4479 HOH A O   1 
HETATM 7473 O O   . HOH J 5 .   ? 27.028  -9.057  28.823 1.00 48.73 ? 4480 HOH A O   1 
HETATM 7474 O O   . HOH J 5 .   ? 1.570   2.714   56.701 1.00 45.38 ? 4481 HOH A O   1 
HETATM 7475 O O   . HOH J 5 .   ? -28.668 -1.074  17.312 1.00 40.57 ? 4482 HOH A O   1 
HETATM 7476 O O   . HOH J 5 .   ? 21.831  -21.671 43.543 1.00 49.14 ? 4484 HOH A O   1 
HETATM 7477 O O   . HOH J 5 .   ? -31.802 23.951  26.488 1.00 44.41 ? 4485 HOH A O   1 
HETATM 7478 O O   . HOH J 5 .   ? 6.046   -4.280  70.882 1.00 37.32 ? 4486 HOH A O   1 
HETATM 7479 O O   . HOH J 5 .   ? -25.695 3.903   39.138 1.00 41.32 ? 4487 HOH A O   1 
HETATM 7480 O O   . HOH J 5 .   ? 4.985   -8.320  -0.375 1.00 44.39 ? 4488 HOH A O   1 
HETATM 7481 O O   . HOH J 5 .   ? 23.461  0.718   25.747 1.00 36.96 ? 4489 HOH A O   1 
HETATM 7482 O O   . HOH J 5 .   ? -6.370  3.825   60.174 1.00 37.28 ? 4490 HOH A O   1 
HETATM 7483 O O   . HOH J 5 .   ? -17.614 -2.842  56.095 1.00 34.61 ? 4491 HOH A O   1 
HETATM 7484 O O   . HOH J 5 .   ? -5.367  -27.060 18.802 1.00 47.40 ? 4493 HOH A O   1 
HETATM 7485 O O   . HOH J 5 .   ? -28.519 3.459   42.267 1.00 43.96 ? 4494 HOH A O   1 
HETATM 7486 O O   . HOH J 5 .   ? 5.900   14.244  30.254 1.00 45.49 ? 4495 HOH A O   1 
HETATM 7487 O O   . HOH J 5 .   ? 4.224   -34.474 43.897 1.00 38.29 ? 4496 HOH A O   1 
HETATM 7488 O O   . HOH J 5 .   ? 16.201  -12.375 46.823 1.00 39.47 ? 4497 HOH A O   1 
HETATM 7489 O O   . HOH J 5 .   ? 14.389  2.812   35.684 1.00 33.78 ? 4498 HOH A O   1 
HETATM 7490 O O   . HOH J 5 .   ? -4.165  0.597   4.317  1.00 63.06 ? 4499 HOH A O   1 
HETATM 7491 O O   . HOH J 5 .   ? 6.802   -46.417 58.608 1.00 35.91 ? 4500 HOH A O   1 
HETATM 7492 O O   . HOH J 5 .   ? -2.518  16.603  28.028 1.00 42.10 ? 4501 HOH A O   1 
HETATM 7493 O O   . HOH J 5 .   ? -21.124 3.722   34.371 1.00 32.06 ? 4502 HOH A O   1 
HETATM 7494 O O   . HOH J 5 .   ? -17.800 11.340  14.538 1.00 42.44 ? 4503 HOH A O   1 
HETATM 7495 O O   . HOH J 5 .   ? 26.231  -18.875 22.367 1.00 44.02 ? 4504 HOH A O   1 
HETATM 7496 O O   . HOH J 5 .   ? -8.836  -18.030 4.599  1.00 29.80 ? 4505 HOH A O   1 
HETATM 7497 O O   . HOH J 5 .   ? -5.528  7.644   15.259 1.00 36.23 ? 4506 HOH A O   1 
HETATM 7498 O O   . HOH J 5 .   ? 7.421   -34.597 32.398 1.00 36.43 ? 4507 HOH A O   1 
HETATM 7499 O O   . HOH J 5 .   ? -18.849 -28.947 47.982 1.00 36.98 ? 4508 HOH A O   1 
HETATM 7500 O O   . HOH J 5 .   ? -35.154 25.873  27.525 1.00 46.17 ? 4509 HOH A O   1 
HETATM 7501 O O   . HOH J 5 .   ? -12.470 -29.160 24.548 1.00 36.62 ? 4510 HOH A O   1 
HETATM 7502 O O   . HOH J 5 .   ? -9.815  0.880   34.811 1.00 27.65 ? 4511 HOH A O   1 
HETATM 7503 O O   . HOH J 5 .   ? -17.529 -10.574 0.072  1.00 35.29 ? 4512 HOH A O   1 
HETATM 7504 O O   . HOH J 5 .   ? 9.222   -25.693 22.908 1.00 45.59 ? 4513 HOH A O   1 
HETATM 7505 O O   . HOH J 5 .   ? -31.590 -8.956  22.876 1.00 33.21 ? 4514 HOH A O   1 
HETATM 7506 O O   . HOH J 5 .   ? -43.962 7.313   44.893 1.00 49.47 ? 4515 HOH A O   1 
HETATM 7507 O O   . HOH J 5 .   ? -18.379 -18.470 5.820  1.00 44.56 ? 4516 HOH A O   1 
HETATM 7508 O O   . HOH J 5 .   ? 7.960   -34.847 46.610 1.00 36.43 ? 4517 HOH A O   1 
HETATM 7509 O O   . HOH J 5 .   ? -12.081 -26.352 12.904 1.00 32.57 ? 4518 HOH A O   1 
HETATM 7510 O O   . HOH J 5 .   ? -13.934 -29.130 38.535 1.00 53.14 ? 4519 HOH A O   1 
HETATM 7511 O O   . HOH J 5 .   ? -28.697 -15.546 6.877  1.00 45.67 ? 4520 HOH A O   1 
HETATM 7512 O O   . HOH J 5 .   ? -39.034 -19.456 29.231 1.00 35.04 ? 4521 HOH A O   1 
HETATM 7513 O O   . HOH J 5 .   ? -35.122 22.155  24.355 1.00 37.00 ? 4522 HOH A O   1 
HETATM 7514 O O   . HOH J 5 .   ? -8.627  20.821  41.603 1.00 46.05 ? 4523 HOH A O   1 
HETATM 7515 O O   . HOH J 5 .   ? -21.817 -30.266 44.589 1.00 43.04 ? 4524 HOH A O   1 
HETATM 7516 O O   . HOH J 5 .   ? -39.334 10.941  37.240 1.00 31.74 ? 4525 HOH A O   1 
HETATM 7517 O O   . HOH J 5 .   ? -39.905 -2.161  18.321 1.00 43.58 ? 4527 HOH A O   1 
HETATM 7518 O O   . HOH J 5 .   ? -31.854 -6.500  22.093 1.00 42.38 ? 4528 HOH A O   1 
HETATM 7519 O O   . HOH J 5 .   ? 16.387  4.478   36.595 1.00 43.85 ? 4529 HOH A O   1 
HETATM 7520 O O   . HOH J 5 .   ? -51.042 18.230  31.645 1.00 49.67 ? 4530 HOH A O   1 
HETATM 7521 O O   . HOH J 5 .   ? -34.382 -6.715  45.715 1.00 44.34 ? 4531 HOH A O   1 
HETATM 7522 O O   . HOH J 5 .   ? -6.642  5.726   42.106 1.00 36.89 ? 4532 HOH A O   1 
HETATM 7523 O O   . HOH J 5 .   ? 11.710  -13.077 36.921 1.00 37.38 ? 4533 HOH A O   1 
HETATM 7524 O O   . HOH J 5 .   ? -33.730 -12.211 14.552 1.00 38.84 ? 4534 HOH A O   1 
HETATM 7525 O O   . HOH J 5 .   ? 25.239  -1.649  17.740 1.00 35.61 ? 4535 HOH A O   1 
HETATM 7526 O O   . HOH J 5 .   ? -40.732 -4.215  19.002 1.00 40.04 ? 4536 HOH A O   1 
HETATM 7527 O O   . HOH J 5 .   ? 13.499  -9.856  4.646  1.00 38.67 ? 4537 HOH A O   1 
HETATM 7528 O O   . HOH J 5 .   ? -34.883 -18.030 41.226 1.00 42.40 ? 4538 HOH A O   1 
HETATM 7529 O O   . HOH J 5 .   ? -35.085 -11.943 23.916 1.00 47.26 ? 4539 HOH A O   1 
HETATM 7530 O O   . HOH J 5 .   ? 18.461  -24.035 20.938 1.00 37.85 ? 4540 HOH A O   1 
HETATM 7531 O O   . HOH J 5 .   ? -9.360  7.204   43.848 1.00 26.64 ? 4541 HOH A O   1 
HETATM 7532 O O   . HOH J 5 .   ? -45.131 -5.913  22.797 1.00 48.34 ? 4542 HOH A O   1 
HETATM 7533 O O   . HOH J 5 .   ? 15.545  -30.514 51.783 1.00 41.75 ? 4543 HOH A O   1 
HETATM 7534 O O   . HOH J 5 .   ? -21.435 -12.065 1.276  1.00 33.85 ? 4544 HOH A O   1 
HETATM 7535 O O   . HOH J 5 .   ? -15.913 0.289   60.450 1.00 45.38 ? 4545 HOH A O   1 
HETATM 7536 O O   . HOH J 5 .   ? 9.201   -13.792 5.812  1.00 36.87 ? 4546 HOH A O   1 
HETATM 7537 O O   . HOH J 5 .   ? -17.953 19.164  28.101 1.00 35.26 ? 4547 HOH A O   1 
HETATM 7538 O O   . HOH J 5 .   ? -14.531 -44.557 48.063 1.00 47.48 ? 4548 HOH A O   1 
HETATM 7539 O O   . HOH J 5 .   ? -26.912 27.154  26.765 1.00 49.31 ? 4549 HOH A O   1 
HETATM 7540 O O   . HOH J 5 .   ? -22.689 -5.774  4.787  1.00 36.89 ? 4550 HOH A O   1 
HETATM 7541 O O   . HOH J 5 .   ? 6.648   -5.508  62.917 1.00 37.96 ? 4551 HOH A O   1 
HETATM 7542 O O   . HOH J 5 .   ? 4.675   9.653   21.216 1.00 40.74 ? 4552 HOH A O   1 
HETATM 7543 O O   . HOH J 5 .   ? -14.962 -2.830  52.668 1.00 42.84 ? 4553 HOH A O   1 
HETATM 7544 O O   . HOH J 5 .   ? -16.584 24.346  24.998 1.00 35.22 ? 4554 HOH A O   1 
HETATM 7545 O O   . HOH J 5 .   ? 15.319  -22.333 56.393 1.00 41.36 ? 4555 HOH A O   1 
HETATM 7546 O O   . HOH J 5 .   ? 15.749  -12.052 49.480 1.00 43.67 ? 4556 HOH A O   1 
HETATM 7547 O O   . HOH J 5 .   ? 3.693   10.024  31.394 1.00 38.17 ? 4557 HOH A O   1 
HETATM 7548 O O   . HOH J 5 .   ? -16.498 13.495  13.448 1.00 40.94 ? 4558 HOH A O   1 
HETATM 7549 O O   . HOH J 5 .   ? 8.293   -3.594  47.749 1.00 26.27 ? 4559 HOH A O   1 
HETATM 7550 O O   . HOH J 5 .   ? 2.204   10.522  22.453 1.00 37.96 ? 4562 HOH A O   1 
HETATM 7551 O O   . HOH J 5 .   ? -2.447  14.839  33.989 1.00 44.48 ? 4563 HOH A O   1 
HETATM 7552 O O   . HOH J 5 .   ? 2.662   -36.679 65.222 1.00 56.14 ? 4564 HOH A O   1 
HETATM 7553 O O   . HOH J 5 .   ? 11.032  -12.069 4.645  1.00 41.64 ? 4565 HOH A O   1 
HETATM 7554 O O   . HOH J 5 .   ? 5.677   11.342  30.276 1.00 41.41 ? 4567 HOH A O   1 
HETATM 7555 O O   . HOH J 5 .   ? -8.495  -30.189 27.025 1.00 35.74 ? 4568 HOH A O   1 
HETATM 7556 O O   . HOH J 5 .   ? -53.286 19.403  32.822 1.00 44.50 ? 4569 HOH A O   1 
HETATM 7557 O O   . HOH J 5 .   ? -22.234 -30.603 21.072 1.00 48.20 ? 4570 HOH A O   1 
HETATM 7558 O O   . HOH J 5 .   ? 13.694  -31.072 29.311 1.00 33.59 ? 4571 HOH A O   1 
HETATM 7559 O O   . HOH J 5 .   ? 2.683   12.930  23.841 1.00 40.03 ? 4572 HOH A O   1 
HETATM 7560 O O   . HOH J 5 .   ? 22.932  -23.164 41.584 1.00 43.73 ? 4574 HOH A O   1 
HETATM 7561 O O   . HOH J 5 .   ? 6.458   -0.642  47.033 1.00 33.37 ? 4575 HOH A O   1 
HETATM 7562 O O   . HOH J 5 .   ? -25.100 -26.149 13.920 1.00 33.59 ? 4576 HOH A O   1 
HETATM 7563 O O   . HOH J 5 .   ? 7.020   -21.318 14.223 1.00 42.69 ? 4577 HOH A O   1 
HETATM 7564 O O   . HOH J 5 .   ? 15.840  -21.239 60.168 1.00 42.25 ? 4578 HOH A O   1 
HETATM 7565 O O   . HOH J 5 .   ? -20.646 -4.830  4.137  1.00 39.92 ? 4579 HOH A O   1 
HETATM 7566 O O   . HOH J 5 .   ? -18.394 22.655  32.229 1.00 43.79 ? 4581 HOH A O   1 
HETATM 7567 O O   . HOH J 5 .   ? -37.547 9.835   18.252 1.00 42.33 ? 4582 HOH A O   1 
HETATM 7568 O O   . HOH J 5 .   ? 22.906  -2.819  35.431 1.00 41.91 ? 4583 HOH A O   1 
HETATM 7569 O O   . HOH J 5 .   ? 3.511   -42.658 63.732 1.00 40.08 ? 4584 HOH A O   1 
HETATM 7570 O O   . HOH J 5 .   ? 9.536   -2.913  43.412 1.00 36.72 ? 4585 HOH A O   1 
HETATM 7571 O O   . HOH J 5 .   ? 15.411  9.494   21.254 1.00 51.15 ? 4586 HOH A O   1 
HETATM 7572 O O   . HOH J 5 .   ? -7.258  -4.297  -0.665 1.00 39.71 ? 4587 HOH A O   1 
HETATM 7573 O O   . HOH J 5 .   ? 18.998  -0.835  16.118 1.00 41.25 ? 4588 HOH A O   1 
HETATM 7574 O O   . HOH J 5 .   ? 10.318  -3.388  36.081 1.00 40.79 ? 4589 HOH A O   1 
HETATM 7575 O O   . HOH J 5 .   ? -6.603  2.231   7.590  1.00 30.13 ? 4591 HOH A O   1 
HETATM 7576 O O   . HOH J 5 .   ? -13.675 -25.671 10.819 1.00 43.81 ? 4593 HOH A O   1 
HETATM 7577 O O   . HOH J 5 .   ? 23.328  -11.257 41.858 1.00 56.69 ? 4594 HOH A O   1 
HETATM 7578 O O   . HOH J 5 .   ? -8.950  21.944  34.349 1.00 35.60 ? 4595 HOH A O   1 
HETATM 7579 O O   . HOH J 5 .   ? 3.648   -39.190 65.899 1.00 37.99 ? 4596 HOH A O   1 
HETATM 7580 O O   . HOH J 5 .   ? -4.746  19.837  32.236 1.00 40.57 ? 4597 HOH A O   1 
HETATM 7581 O O   . HOH J 5 .   ? -1.358  -25.670 64.564 1.00 36.02 ? 4598 HOH A O   1 
HETATM 7582 O O   . HOH J 5 .   ? 16.714  -26.419 52.683 1.00 48.37 ? 4599 HOH A O   1 
HETATM 7583 O O   . HOH J 5 .   ? -18.038 0.743   48.575 1.00 35.96 ? 4600 HOH A O   1 
HETATM 7584 O O   . HOH J 5 .   ? 7.027   -5.355  74.287 1.00 51.30 ? 4601 HOH A O   1 
HETATM 7585 O O   . HOH J 5 .   ? 15.004  -29.032 23.328 1.00 37.32 ? 4602 HOH A O   1 
HETATM 7586 O O   . HOH J 5 .   ? -17.429 -2.026  53.634 1.00 37.15 ? 4603 HOH A O   1 
HETATM 7587 O O   . HOH J 5 .   ? 12.108  -11.140 58.314 1.00 44.22 ? 4604 HOH A O   1 
HETATM 7588 O O   . HOH J 5 .   ? 4.492   -21.171 76.310 1.00 39.04 ? 4605 HOH A O   1 
HETATM 7589 O O   . HOH J 5 .   ? 21.403  -27.872 46.021 1.00 35.05 ? 4606 HOH A O   1 
HETATM 7590 O O   . HOH J 5 .   ? 9.888   -32.837 43.663 1.00 36.29 ? 4607 HOH A O   1 
HETATM 7591 O O   . HOH J 5 .   ? -35.260 -18.617 18.197 1.00 50.72 ? 4608 HOH A O   1 
HETATM 7592 O O   . HOH J 5 .   ? -37.707 4.528   18.161 1.00 30.71 ? 4609 HOH A O   1 
HETATM 7593 O O   . HOH J 5 .   ? 15.665  5.093   15.129 1.00 38.49 ? 4610 HOH A O   1 
HETATM 7594 O O   . HOH J 5 .   ? 18.992  5.934   27.665 1.00 40.81 ? 4611 HOH A O   1 
HETATM 7595 O O   . HOH J 5 .   ? 12.978  -32.924 42.821 1.00 37.32 ? 4612 HOH A O   1 
HETATM 7596 O O   . HOH J 5 .   ? 11.664  -1.457  36.361 1.00 44.04 ? 4613 HOH A O   1 
HETATM 7597 O O   . HOH J 5 .   ? -19.045 -2.354  58.265 1.00 48.28 ? 4614 HOH A O   1 
HETATM 7598 O O   . HOH J 5 .   ? -38.366 -7.852  34.962 1.00 31.99 ? 4615 HOH A O   1 
HETATM 7599 O O   . HOH J 5 .   ? -5.030  -2.917  -0.006 1.00 51.24 ? 4616 HOH A O   1 
HETATM 7600 O O   . HOH J 5 .   ? -50.405 -0.289  25.998 1.00 48.91 ? 4617 HOH A O   1 
HETATM 7601 O O   . HOH J 5 .   ? -9.091  14.082  22.996 1.00 39.28 ? 4618 HOH A O   1 
HETATM 7602 O O   . HOH J 5 .   ? -8.170  -19.583 14.645 1.00 12.40 ? 4619 HOH A O   1 
HETATM 7603 O O   . HOH J 5 .   ? -43.304 11.301  36.203 1.00 39.34 ? 4622 HOH A O   1 
HETATM 7604 O O   . HOH J 5 .   ? -1.097  -0.234  54.704 1.00 30.98 ? 4624 HOH A O   1 
HETATM 7605 O O   . HOH J 5 .   ? -32.552 1.792   23.619 1.00 60.09 ? 4625 HOH A O   1 
HETATM 7606 O O   . HOH J 5 .   ? -5.763  -0.663  1.124  1.00 43.94 ? 4628 HOH A O   1 
HETATM 7607 O O   . HOH J 5 .   ? 7.072   -0.968  59.135 1.00 51.86 ? 4629 HOH A O   1 
HETATM 7608 O O   . HOH J 5 .   ? -38.730 23.997  27.739 1.00 37.40 ? 4630 HOH A O   1 
HETATM 7609 O O   . HOH J 5 .   ? -19.269 1.825   46.189 1.00 44.39 ? 4631 HOH A O   1 
HETATM 7610 O O   . HOH J 5 .   ? -28.176 24.264  24.885 1.00 41.56 ? 4632 HOH A O   1 
HETATM 7611 O O   . HOH J 5 .   ? 12.838  -35.437 39.668 1.00 43.84 ? 4633 HOH A O   1 
HETATM 7612 O O   . HOH J 5 .   ? 0.929   -38.698 65.244 1.00 43.05 ? 4634 HOH A O   1 
HETATM 7613 O O   . HOH J 5 .   ? -33.999 -11.554 20.260 1.00 46.04 ? 4635 HOH A O   1 
HETATM 7614 O O   . HOH J 5 .   ? 5.218   11.116  7.977  1.00 38.73 ? 4636 HOH A O   1 
HETATM 7615 O O   . HOH J 5 .   ? 2.498   -33.934 40.820 1.00 42.10 ? 4637 HOH A O   1 
HETATM 7616 O O   . HOH J 5 .   ? -3.394  8.451   15.808 1.00 44.79 ? 4638 HOH A O   1 
HETATM 7617 O O   . HOH J 5 .   ? -11.895 6.952   8.122  1.00 47.14 ? 4639 HOH A O   1 
HETATM 7618 O O   . HOH J 5 .   ? 13.529  -2.382  35.159 1.00 40.73 ? 4640 HOH A O   1 
HETATM 7619 O O   . HOH J 5 .   ? -40.869 -6.700  35.186 1.00 38.65 ? 4641 HOH A O   1 
HETATM 7620 O O   . HOH J 5 .   ? -17.368 -30.159 57.153 1.00 36.91 ? 4642 HOH A O   1 
HETATM 7621 O O   . HOH J 5 .   ? -48.254 6.229   20.910 1.00 40.21 ? 4643 HOH A O   1 
HETATM 7622 O O   . HOH J 5 .   ? -11.708 -29.108 37.313 1.00 55.38 ? 4644 HOH A O   1 
HETATM 7623 O O   . HOH J 5 .   ? 16.383  7.339   16.347 1.00 50.45 ? 4645 HOH A O   1 
HETATM 7624 O O   . HOH J 5 .   ? -20.441 23.574  23.927 1.00 41.15 ? 4653 HOH A O   1 
HETATM 7625 O O   . HOH J 5 .   ? -35.426 -12.001 17.895 1.00 40.46 ? 4657 HOH A O   1 
HETATM 7626 O O   . HOH J 5 .   ? -2.836  1.517   53.016 1.00 35.28 ? 4659 HOH A O   1 
HETATM 7627 O O   . HOH J 5 .   ? 13.506  4.715   33.700 1.00 41.40 ? 4662 HOH A O   1 
HETATM 7628 O O   . HOH J 5 .   ? -25.461 -28.237 21.151 1.00 42.92 ? 4663 HOH A O   1 
HETATM 7629 O O   . HOH J 5 .   ? 5.207   7.186   10.351 1.00 44.75 ? 4665 HOH A O   1 
HETATM 7630 O O   . HOH J 5 .   ? -23.657 -22.076 48.335 1.00 35.11 ? 4666 HOH A O   1 
HETATM 7631 O O   . HOH J 5 .   ? -21.474 16.704  18.574 1.00 32.95 ? 4667 HOH A O   1 
HETATM 7632 O O   . HOH J 5 .   ? -14.003 -26.977 16.395 1.00 47.78 ? 4668 HOH A O   1 
HETATM 7633 O O   . HOH J 5 .   ? -50.598 17.128  34.692 1.00 51.17 ? 4669 HOH A O   1 
HETATM 7634 O O   . HOH J 5 .   ? -21.215 1.570   44.867 1.00 45.85 ? 4670 HOH A O   1 
HETATM 7635 O O   . HOH J 5 .   ? -6.858  -34.764 62.661 1.00 45.25 ? 4671 HOH A O   1 
HETATM 7636 O O   . HOH J 5 .   ? -0.069  -32.151 44.823 1.00 41.20 ? 4672 HOH A O   1 
HETATM 7637 O O   . HOH J 5 .   ? -3.080  -43.922 62.099 1.00 33.83 ? 4673 HOH A O   1 
HETATM 7638 O O   . HOH J 5 .   ? 11.427  -25.986 68.309 1.00 61.89 ? 4674 HOH A O   1 
HETATM 7639 O O   . HOH J 5 .   ? -19.686 -0.986  45.321 1.00 46.21 ? 4675 HOH A O   1 
HETATM 7640 O O   . HOH J 5 .   ? 29.369  -12.578 17.290 1.00 48.97 ? 4676 HOH A O   1 
HETATM 7641 O O   . HOH J 5 .   ? -19.680 -28.824 50.961 1.00 34.60 ? 4677 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 838 838 838 THR THR 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 
A 1 871 HIS 871 871 ?   ?   ?   A . n 
A 1 872 HIS 872 872 ?   ?   ?   A . n 
A 1 873 HIS 873 873 ?   ?   ?   A . n 
A 1 874 HIS 874 874 ?   ?   ?   A . n 
A 1 875 HIS 875 875 ?   ?   ?   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 NR3 1   1001 1001 NR3 NR3 A . 
C 3 NAG 1   2001 2001 NAG NAG A . 
D 3 NAG 2   2002 2002 NAG NAG A . 
E 3 NAG 1   2003 2003 NAG NAG A . 
F 4 GOL 1   3001 3001 GOL GOL A . 
G 4 GOL 1   3002 3002 GOL GOL A . 
H 4 GOL 1   3003 3003 GOL GOL A . 
I 4 GOL 1   3004 3004 GOL GOL A . 
J 5 HOH 1   4002 4002 HOH HOH A . 
J 5 HOH 2   4003 4003 HOH HOH A . 
J 5 HOH 3   4004 4004 HOH HOH A . 
J 5 HOH 4   4005 4005 HOH HOH A . 
J 5 HOH 5   4006 4006 HOH HOH A . 
J 5 HOH 6   4007 4007 HOH HOH A . 
J 5 HOH 7   4008 4008 HOH HOH A . 
J 5 HOH 8   4009 4009 HOH HOH A . 
J 5 HOH 9   4010 4010 HOH HOH A . 
J 5 HOH 10  4011 4011 HOH HOH A . 
J 5 HOH 11  4012 4012 HOH HOH A . 
J 5 HOH 12  4014 4014 HOH HOH A . 
J 5 HOH 13  4015 4015 HOH HOH A . 
J 5 HOH 14  4016 4016 HOH HOH A . 
J 5 HOH 15  4017 4017 HOH HOH A . 
J 5 HOH 16  4018 4018 HOH HOH A . 
J 5 HOH 17  4019 4019 HOH HOH A . 
J 5 HOH 18  4020 4020 HOH HOH A . 
J 5 HOH 19  4021 4021 HOH HOH A . 
J 5 HOH 20  4022 4022 HOH HOH A . 
J 5 HOH 21  4023 4023 HOH HOH A . 
J 5 HOH 22  4024 4024 HOH HOH A . 
J 5 HOH 23  4025 4025 HOH HOH A . 
J 5 HOH 24  4026 4026 HOH HOH A . 
J 5 HOH 25  4027 4027 HOH HOH A . 
J 5 HOH 26  4028 4028 HOH HOH A . 
J 5 HOH 27  4029 4029 HOH HOH A . 
J 5 HOH 28  4030 4030 HOH HOH A . 
J 5 HOH 29  4031 4031 HOH HOH A . 
J 5 HOH 30  4032 4032 HOH HOH A . 
J 5 HOH 31  4033 4033 HOH HOH A . 
J 5 HOH 32  4034 4034 HOH HOH A . 
J 5 HOH 33  4035 4035 HOH HOH A . 
J 5 HOH 34  4036 4036 HOH HOH A . 
J 5 HOH 35  4037 4037 HOH HOH A . 
J 5 HOH 36  4038 4038 HOH HOH A . 
J 5 HOH 37  4039 4039 HOH HOH A . 
J 5 HOH 38  4040 4040 HOH HOH A . 
J 5 HOH 39  4041 4041 HOH HOH A . 
J 5 HOH 40  4042 4042 HOH HOH A . 
J 5 HOH 41  4043 4043 HOH HOH A . 
J 5 HOH 42  4044 4044 HOH HOH A . 
J 5 HOH 43  4045 4045 HOH HOH A . 
J 5 HOH 44  4046 4046 HOH HOH A . 
J 5 HOH 45  4047 4047 HOH HOH A . 
J 5 HOH 46  4048 4048 HOH HOH A . 
J 5 HOH 47  4049 4049 HOH HOH A . 
J 5 HOH 48  4050 4050 HOH HOH A . 
J 5 HOH 49  4051 4051 HOH HOH A . 
J 5 HOH 50  4052 4052 HOH HOH A . 
J 5 HOH 51  4053 4053 HOH HOH A . 
J 5 HOH 52  4054 4054 HOH HOH A . 
J 5 HOH 53  4055 4055 HOH HOH A . 
J 5 HOH 54  4056 4056 HOH HOH A . 
J 5 HOH 55  4057 4057 HOH HOH A . 
J 5 HOH 56  4058 4058 HOH HOH A . 
J 5 HOH 57  4059 4059 HOH HOH A . 
J 5 HOH 58  4060 4060 HOH HOH A . 
J 5 HOH 59  4061 4061 HOH HOH A . 
J 5 HOH 60  4062 4062 HOH HOH A . 
J 5 HOH 61  4063 4063 HOH HOH A . 
J 5 HOH 62  4065 4065 HOH HOH A . 
J 5 HOH 63  4066 4066 HOH HOH A . 
J 5 HOH 64  4067 4067 HOH HOH A . 
J 5 HOH 65  4068 4068 HOH HOH A . 
J 5 HOH 66  4069 4069 HOH HOH A . 
J 5 HOH 67  4070 4070 HOH HOH A . 
J 5 HOH 68  4072 4072 HOH HOH A . 
J 5 HOH 69  4073 4073 HOH HOH A . 
J 5 HOH 70  4074 4074 HOH HOH A . 
J 5 HOH 71  4075 4075 HOH HOH A . 
J 5 HOH 72  4076 4076 HOH HOH A . 
J 5 HOH 73  4077 4077 HOH HOH A . 
J 5 HOH 74  4078 4078 HOH HOH A . 
J 5 HOH 75  4079 4079 HOH HOH A . 
J 5 HOH 76  4081 4081 HOH HOH A . 
J 5 HOH 77  4082 4082 HOH HOH A . 
J 5 HOH 78  4083 4083 HOH HOH A . 
J 5 HOH 79  4084 4084 HOH HOH A . 
J 5 HOH 80  4085 4085 HOH HOH A . 
J 5 HOH 81  4086 4086 HOH HOH A . 
J 5 HOH 82  4087 4087 HOH HOH A . 
J 5 HOH 83  4088 4088 HOH HOH A . 
J 5 HOH 84  4089 4089 HOH HOH A . 
J 5 HOH 85  4090 4090 HOH HOH A . 
J 5 HOH 86  4091 4091 HOH HOH A . 
J 5 HOH 87  4092 4092 HOH HOH A . 
J 5 HOH 88  4093 4093 HOH HOH A . 
J 5 HOH 89  4094 4094 HOH HOH A . 
J 5 HOH 90  4095 4095 HOH HOH A . 
J 5 HOH 91  4096 4096 HOH HOH A . 
J 5 HOH 92  4097 4097 HOH HOH A . 
J 5 HOH 93  4098 4098 HOH HOH A . 
J 5 HOH 94  4099 4099 HOH HOH A . 
J 5 HOH 95  4100 4100 HOH HOH A . 
J 5 HOH 96  4101 4101 HOH HOH A . 
J 5 HOH 97  4102 4102 HOH HOH A . 
J 5 HOH 98  4103 4103 HOH HOH A . 
J 5 HOH 99  4104 4104 HOH HOH A . 
J 5 HOH 100 4105 4105 HOH HOH A . 
J 5 HOH 101 4106 4106 HOH HOH A . 
J 5 HOH 102 4109 4109 HOH HOH A . 
J 5 HOH 103 4110 4110 HOH HOH A . 
J 5 HOH 104 4111 4111 HOH HOH A . 
J 5 HOH 105 4112 4112 HOH HOH A . 
J 5 HOH 106 4113 4113 HOH HOH A . 
J 5 HOH 107 4114 4114 HOH HOH A . 
J 5 HOH 108 4115 4115 HOH HOH A . 
J 5 HOH 109 4116 4116 HOH HOH A . 
J 5 HOH 110 4117 4117 HOH HOH A . 
J 5 HOH 111 4118 4118 HOH HOH A . 
J 5 HOH 112 4119 4119 HOH HOH A . 
J 5 HOH 113 4120 4120 HOH HOH A . 
J 5 HOH 114 4121 4121 HOH HOH A . 
J 5 HOH 115 4123 4123 HOH HOH A . 
J 5 HOH 116 4124 4124 HOH HOH A . 
J 5 HOH 117 4125 4125 HOH HOH A . 
J 5 HOH 118 4126 4126 HOH HOH A . 
J 5 HOH 119 4127 4127 HOH HOH A . 
J 5 HOH 120 4128 4128 HOH HOH A . 
J 5 HOH 121 4129 4129 HOH HOH A . 
J 5 HOH 122 4130 4130 HOH HOH A . 
J 5 HOH 123 4131 4131 HOH HOH A . 
J 5 HOH 124 4132 4132 HOH HOH A . 
J 5 HOH 125 4133 4133 HOH HOH A . 
J 5 HOH 126 4134 4134 HOH HOH A . 
J 5 HOH 127 4135 4135 HOH HOH A . 
J 5 HOH 128 4136 4136 HOH HOH A . 
J 5 HOH 129 4137 4137 HOH HOH A . 
J 5 HOH 130 4139 4139 HOH HOH A . 
J 5 HOH 131 4141 4141 HOH HOH A . 
J 5 HOH 132 4143 4143 HOH HOH A . 
J 5 HOH 133 4144 4144 HOH HOH A . 
J 5 HOH 134 4145 4145 HOH HOH A . 
J 5 HOH 135 4146 4146 HOH HOH A . 
J 5 HOH 136 4147 4147 HOH HOH A . 
J 5 HOH 137 4149 4149 HOH HOH A . 
J 5 HOH 138 4150 4150 HOH HOH A . 
J 5 HOH 139 4151 4151 HOH HOH A . 
J 5 HOH 140 4152 4152 HOH HOH A . 
J 5 HOH 141 4153 4153 HOH HOH A . 
J 5 HOH 142 4154 4154 HOH HOH A . 
J 5 HOH 143 4155 4155 HOH HOH A . 
J 5 HOH 144 4156 4156 HOH HOH A . 
J 5 HOH 145 4157 4157 HOH HOH A . 
J 5 HOH 146 4158 4158 HOH HOH A . 
J 5 HOH 147 4159 4159 HOH HOH A . 
J 5 HOH 148 4160 4160 HOH HOH A . 
J 5 HOH 149 4161 4161 HOH HOH A . 
J 5 HOH 150 4162 4162 HOH HOH A . 
J 5 HOH 151 4163 4163 HOH HOH A . 
J 5 HOH 152 4164 4164 HOH HOH A . 
J 5 HOH 153 4165 4165 HOH HOH A . 
J 5 HOH 154 4166 4166 HOH HOH A . 
J 5 HOH 155 4167 4167 HOH HOH A . 
J 5 HOH 156 4168 4168 HOH HOH A . 
J 5 HOH 157 4169 4169 HOH HOH A . 
J 5 HOH 158 4171 4171 HOH HOH A . 
J 5 HOH 159 4172 4172 HOH HOH A . 
J 5 HOH 160 4173 4173 HOH HOH A . 
J 5 HOH 161 4174 4174 HOH HOH A . 
J 5 HOH 162 4175 4175 HOH HOH A . 
J 5 HOH 163 4176 4176 HOH HOH A . 
J 5 HOH 164 4177 4177 HOH HOH A . 
J 5 HOH 165 4178 4178 HOH HOH A . 
J 5 HOH 166 4179 4179 HOH HOH A . 
J 5 HOH 167 4180 4180 HOH HOH A . 
J 5 HOH 168 4181 4181 HOH HOH A . 
J 5 HOH 169 4182 4182 HOH HOH A . 
J 5 HOH 170 4183 4183 HOH HOH A . 
J 5 HOH 171 4184 4184 HOH HOH A . 
J 5 HOH 172 4185 4185 HOH HOH A . 
J 5 HOH 173 4186 4186 HOH HOH A . 
J 5 HOH 174 4188 4188 HOH HOH A . 
J 5 HOH 175 4189 4189 HOH HOH A . 
J 5 HOH 176 4194 4194 HOH HOH A . 
J 5 HOH 177 4195 4195 HOH HOH A . 
J 5 HOH 178 4196 4196 HOH HOH A . 
J 5 HOH 179 4197 4197 HOH HOH A . 
J 5 HOH 180 4198 4198 HOH HOH A . 
J 5 HOH 181 4199 4199 HOH HOH A . 
J 5 HOH 182 4200 4200 HOH HOH A . 
J 5 HOH 183 4201 4201 HOH HOH A . 
J 5 HOH 184 4202 4202 HOH HOH A . 
J 5 HOH 185 4203 4203 HOH HOH A . 
J 5 HOH 186 4204 4204 HOH HOH A . 
J 5 HOH 187 4205 4205 HOH HOH A . 
J 5 HOH 188 4206 4206 HOH HOH A . 
J 5 HOH 189 4207 4207 HOH HOH A . 
J 5 HOH 190 4208 4208 HOH HOH A . 
J 5 HOH 191 4209 4209 HOH HOH A . 
J 5 HOH 192 4210 4210 HOH HOH A . 
J 5 HOH 193 4212 4212 HOH HOH A . 
J 5 HOH 194 4213 4213 HOH HOH A . 
J 5 HOH 195 4214 4214 HOH HOH A . 
J 5 HOH 196 4215 4215 HOH HOH A . 
J 5 HOH 197 4216 4216 HOH HOH A . 
J 5 HOH 198 4217 4217 HOH HOH A . 
J 5 HOH 199 4218 4218 HOH HOH A . 
J 5 HOH 200 4219 4219 HOH HOH A . 
J 5 HOH 201 4220 4220 HOH HOH A . 
J 5 HOH 202 4221 4221 HOH HOH A . 
J 5 HOH 203 4222 4222 HOH HOH A . 
J 5 HOH 204 4223 4223 HOH HOH A . 
J 5 HOH 205 4224 4224 HOH HOH A . 
J 5 HOH 206 4225 4225 HOH HOH A . 
J 5 HOH 207 4226 4226 HOH HOH A . 
J 5 HOH 208 4227 4227 HOH HOH A . 
J 5 HOH 209 4228 4228 HOH HOH A . 
J 5 HOH 210 4229 4229 HOH HOH A . 
J 5 HOH 211 4230 4230 HOH HOH A . 
J 5 HOH 212 4231 4231 HOH HOH A . 
J 5 HOH 213 4232 4232 HOH HOH A . 
J 5 HOH 214 4233 4233 HOH HOH A . 
J 5 HOH 215 4234 4234 HOH HOH A . 
J 5 HOH 216 4235 4235 HOH HOH A . 
J 5 HOH 217 4236 4236 HOH HOH A . 
J 5 HOH 218 4237 4237 HOH HOH A . 
J 5 HOH 219 4238 4238 HOH HOH A . 
J 5 HOH 220 4240 4240 HOH HOH A . 
J 5 HOH 221 4241 4241 HOH HOH A . 
J 5 HOH 222 4242 4242 HOH HOH A . 
J 5 HOH 223 4243 4243 HOH HOH A . 
J 5 HOH 224 4244 4244 HOH HOH A . 
J 5 HOH 225 4245 4245 HOH HOH A . 
J 5 HOH 226 4246 4246 HOH HOH A . 
J 5 HOH 227 4247 4247 HOH HOH A . 
J 5 HOH 228 4248 4248 HOH HOH A . 
J 5 HOH 229 4249 4249 HOH HOH A . 
J 5 HOH 230 4250 4250 HOH HOH A . 
J 5 HOH 231 4251 4251 HOH HOH A . 
J 5 HOH 232 4253 4253 HOH HOH A . 
J 5 HOH 233 4254 4254 HOH HOH A . 
J 5 HOH 234 4255 4255 HOH HOH A . 
J 5 HOH 235 4256 4256 HOH HOH A . 
J 5 HOH 236 4257 4257 HOH HOH A . 
J 5 HOH 237 4258 4258 HOH HOH A . 
J 5 HOH 238 4259 4259 HOH HOH A . 
J 5 HOH 239 4260 4260 HOH HOH A . 
J 5 HOH 240 4261 4261 HOH HOH A . 
J 5 HOH 241 4262 4262 HOH HOH A . 
J 5 HOH 242 4263 4263 HOH HOH A . 
J 5 HOH 243 4264 4264 HOH HOH A . 
J 5 HOH 244 4265 4265 HOH HOH A . 
J 5 HOH 245 4266 4266 HOH HOH A . 
J 5 HOH 246 4267 4267 HOH HOH A . 
J 5 HOH 247 4268 4268 HOH HOH A . 
J 5 HOH 248 4269 4269 HOH HOH A . 
J 5 HOH 249 4270 4270 HOH HOH A . 
J 5 HOH 250 4271 4271 HOH HOH A . 
J 5 HOH 251 4272 4272 HOH HOH A . 
J 5 HOH 252 4273 4273 HOH HOH A . 
J 5 HOH 253 4274 4274 HOH HOH A . 
J 5 HOH 254 4275 4275 HOH HOH A . 
J 5 HOH 255 4276 4276 HOH HOH A . 
J 5 HOH 256 4277 4277 HOH HOH A . 
J 5 HOH 257 4278 4278 HOH HOH A . 
J 5 HOH 258 4279 4279 HOH HOH A . 
J 5 HOH 259 4280 4280 HOH HOH A . 
J 5 HOH 260 4281 4281 HOH HOH A . 
J 5 HOH 261 4282 4282 HOH HOH A . 
J 5 HOH 262 4284 4284 HOH HOH A . 
J 5 HOH 263 4285 4285 HOH HOH A . 
J 5 HOH 264 4286 4286 HOH HOH A . 
J 5 HOH 265 4287 4287 HOH HOH A . 
J 5 HOH 266 4288 4288 HOH HOH A . 
J 5 HOH 267 4289 4289 HOH HOH A . 
J 5 HOH 268 4290 4290 HOH HOH A . 
J 5 HOH 269 4291 4291 HOH HOH A . 
J 5 HOH 270 4292 4292 HOH HOH A . 
J 5 HOH 271 4293 4293 HOH HOH A . 
J 5 HOH 272 4294 4294 HOH HOH A . 
J 5 HOH 273 4295 4295 HOH HOH A . 
J 5 HOH 274 4296 4296 HOH HOH A . 
J 5 HOH 275 4297 4297 HOH HOH A . 
J 5 HOH 276 4298 4298 HOH HOH A . 
J 5 HOH 277 4299 4299 HOH HOH A . 
J 5 HOH 278 4300 4300 HOH HOH A . 
J 5 HOH 279 4301 4301 HOH HOH A . 
J 5 HOH 280 4302 4302 HOH HOH A . 
J 5 HOH 281 4303 4303 HOH HOH A . 
J 5 HOH 282 4304 4304 HOH HOH A . 
J 5 HOH 283 4305 4305 HOH HOH A . 
J 5 HOH 284 4306 4306 HOH HOH A . 
J 5 HOH 285 4307 4307 HOH HOH A . 
J 5 HOH 286 4308 4308 HOH HOH A . 
J 5 HOH 287 4309 4309 HOH HOH A . 
J 5 HOH 288 4310 4310 HOH HOH A . 
J 5 HOH 289 4311 4311 HOH HOH A . 
J 5 HOH 290 4312 4312 HOH HOH A . 
J 5 HOH 291 4313 4313 HOH HOH A . 
J 5 HOH 292 4314 4314 HOH HOH A . 
J 5 HOH 293 4315 4315 HOH HOH A . 
J 5 HOH 294 4316 4316 HOH HOH A . 
J 5 HOH 295 4317 4317 HOH HOH A . 
J 5 HOH 296 4318 4318 HOH HOH A . 
J 5 HOH 297 4319 4319 HOH HOH A . 
J 5 HOH 298 4320 4320 HOH HOH A . 
J 5 HOH 299 4321 4321 HOH HOH A . 
J 5 HOH 300 4322 4322 HOH HOH A . 
J 5 HOH 301 4323 4323 HOH HOH A . 
J 5 HOH 302 4324 4324 HOH HOH A . 
J 5 HOH 303 4325 4325 HOH HOH A . 
J 5 HOH 304 4327 4327 HOH HOH A . 
J 5 HOH 305 4329 4329 HOH HOH A . 
J 5 HOH 306 4330 4330 HOH HOH A . 
J 5 HOH 307 4331 4331 HOH HOH A . 
J 5 HOH 308 4332 4332 HOH HOH A . 
J 5 HOH 309 4333 4333 HOH HOH A . 
J 5 HOH 310 4334 4334 HOH HOH A . 
J 5 HOH 311 4337 4337 HOH HOH A . 
J 5 HOH 312 4338 4338 HOH HOH A . 
J 5 HOH 313 4339 4339 HOH HOH A . 
J 5 HOH 314 4340 4340 HOH HOH A . 
J 5 HOH 315 4341 4341 HOH HOH A . 
J 5 HOH 316 4342 4342 HOH HOH A . 
J 5 HOH 317 4343 4343 HOH HOH A . 
J 5 HOH 318 4345 4345 HOH HOH A . 
J 5 HOH 319 4346 4346 HOH HOH A . 
J 5 HOH 320 4347 4347 HOH HOH A . 
J 5 HOH 321 4348 4348 HOH HOH A . 
J 5 HOH 322 4349 4349 HOH HOH A . 
J 5 HOH 323 4350 4350 HOH HOH A . 
J 5 HOH 324 4352 4352 HOH HOH A . 
J 5 HOH 325 4353 4353 HOH HOH A . 
J 5 HOH 326 4354 4354 HOH HOH A . 
J 5 HOH 327 4355 4355 HOH HOH A . 
J 5 HOH 328 4356 4356 HOH HOH A . 
J 5 HOH 329 4357 4357 HOH HOH A . 
J 5 HOH 330 4358 4358 HOH HOH A . 
J 5 HOH 331 4359 4359 HOH HOH A . 
J 5 HOH 332 4360 4360 HOH HOH A . 
J 5 HOH 333 4361 4361 HOH HOH A . 
J 5 HOH 334 4362 4362 HOH HOH A . 
J 5 HOH 335 4363 4363 HOH HOH A . 
J 5 HOH 336 4364 4364 HOH HOH A . 
J 5 HOH 337 4365 4365 HOH HOH A . 
J 5 HOH 338 4366 4366 HOH HOH A . 
J 5 HOH 339 4367 4367 HOH HOH A . 
J 5 HOH 340 4368 4368 HOH HOH A . 
J 5 HOH 341 4369 4369 HOH HOH A . 
J 5 HOH 342 4371 4371 HOH HOH A . 
J 5 HOH 343 4372 4372 HOH HOH A . 
J 5 HOH 344 4373 4373 HOH HOH A . 
J 5 HOH 345 4374 4374 HOH HOH A . 
J 5 HOH 346 4375 4375 HOH HOH A . 
J 5 HOH 347 4376 4376 HOH HOH A . 
J 5 HOH 348 4377 4377 HOH HOH A . 
J 5 HOH 349 4378 4378 HOH HOH A . 
J 5 HOH 350 4379 4379 HOH HOH A . 
J 5 HOH 351 4380 4380 HOH HOH A . 
J 5 HOH 352 4381 4381 HOH HOH A . 
J 5 HOH 353 4382 4382 HOH HOH A . 
J 5 HOH 354 4383 4383 HOH HOH A . 
J 5 HOH 355 4384 4384 HOH HOH A . 
J 5 HOH 356 4385 4385 HOH HOH A . 
J 5 HOH 357 4386 4386 HOH HOH A . 
J 5 HOH 358 4387 4387 HOH HOH A . 
J 5 HOH 359 4388 4388 HOH HOH A . 
J 5 HOH 360 4390 4390 HOH HOH A . 
J 5 HOH 361 4391 4391 HOH HOH A . 
J 5 HOH 362 4392 4392 HOH HOH A . 
J 5 HOH 363 4393 4393 HOH HOH A . 
J 5 HOH 364 4394 4394 HOH HOH A . 
J 5 HOH 365 4395 4395 HOH HOH A . 
J 5 HOH 366 4396 4396 HOH HOH A . 
J 5 HOH 367 4397 4397 HOH HOH A . 
J 5 HOH 368 4398 4398 HOH HOH A . 
J 5 HOH 369 4399 4399 HOH HOH A . 
J 5 HOH 370 4401 4401 HOH HOH A . 
J 5 HOH 371 4402 4402 HOH HOH A . 
J 5 HOH 372 4404 4404 HOH HOH A . 
J 5 HOH 373 4405 4405 HOH HOH A . 
J 5 HOH 374 4406 4406 HOH HOH A . 
J 5 HOH 375 4407 4407 HOH HOH A . 
J 5 HOH 376 4408 4408 HOH HOH A . 
J 5 HOH 377 4409 4409 HOH HOH A . 
J 5 HOH 378 4410 4410 HOH HOH A . 
J 5 HOH 379 4411 4411 HOH HOH A . 
J 5 HOH 380 4412 4412 HOH HOH A . 
J 5 HOH 381 4413 4413 HOH HOH A . 
J 5 HOH 382 4414 4414 HOH HOH A . 
J 5 HOH 383 4415 4415 HOH HOH A . 
J 5 HOH 384 4416 4416 HOH HOH A . 
J 5 HOH 385 4417 4417 HOH HOH A . 
J 5 HOH 386 4418 4418 HOH HOH A . 
J 5 HOH 387 4419 4419 HOH HOH A . 
J 5 HOH 388 4420 4420 HOH HOH A . 
J 5 HOH 389 4421 4421 HOH HOH A . 
J 5 HOH 390 4422 4422 HOH HOH A . 
J 5 HOH 391 4423 4423 HOH HOH A . 
J 5 HOH 392 4424 4424 HOH HOH A . 
J 5 HOH 393 4425 4425 HOH HOH A . 
J 5 HOH 394 4426 4426 HOH HOH A . 
J 5 HOH 395 4427 4427 HOH HOH A . 
J 5 HOH 396 4428 4428 HOH HOH A . 
J 5 HOH 397 4430 4430 HOH HOH A . 
J 5 HOH 398 4431 4431 HOH HOH A . 
J 5 HOH 399 4432 4432 HOH HOH A . 
J 5 HOH 400 4433 4433 HOH HOH A . 
J 5 HOH 401 4434 4434 HOH HOH A . 
J 5 HOH 402 4435 4435 HOH HOH A . 
J 5 HOH 403 4436 4436 HOH HOH A . 
J 5 HOH 404 4437 4437 HOH HOH A . 
J 5 HOH 405 4438 4438 HOH HOH A . 
J 5 HOH 406 4439 4439 HOH HOH A . 
J 5 HOH 407 4440 4440 HOH HOH A . 
J 5 HOH 408 4441 4441 HOH HOH A . 
J 5 HOH 409 4442 4442 HOH HOH A . 
J 5 HOH 410 4443 4443 HOH HOH A . 
J 5 HOH 411 4444 4444 HOH HOH A . 
J 5 HOH 412 4445 4445 HOH HOH A . 
J 5 HOH 413 4446 4446 HOH HOH A . 
J 5 HOH 414 4447 4447 HOH HOH A . 
J 5 HOH 415 4448 4448 HOH HOH A . 
J 5 HOH 416 4449 4449 HOH HOH A . 
J 5 HOH 417 4450 4450 HOH HOH A . 
J 5 HOH 418 4451 4451 HOH HOH A . 
J 5 HOH 419 4452 4452 HOH HOH A . 
J 5 HOH 420 4453 4453 HOH HOH A . 
J 5 HOH 421 4454 4454 HOH HOH A . 
J 5 HOH 422 4455 4455 HOH HOH A . 
J 5 HOH 423 4456 4456 HOH HOH A . 
J 5 HOH 424 4457 4457 HOH HOH A . 
J 5 HOH 425 4458 4458 HOH HOH A . 
J 5 HOH 426 4459 4459 HOH HOH A . 
J 5 HOH 427 4460 4460 HOH HOH A . 
J 5 HOH 428 4463 4463 HOH HOH A . 
J 5 HOH 429 4464 4464 HOH HOH A . 
J 5 HOH 430 4465 4465 HOH HOH A . 
J 5 HOH 431 4466 4466 HOH HOH A . 
J 5 HOH 432 4467 4467 HOH HOH A . 
J 5 HOH 433 4468 4468 HOH HOH A . 
J 5 HOH 434 4469 4469 HOH HOH A . 
J 5 HOH 435 4470 4470 HOH HOH A . 
J 5 HOH 436 4471 4471 HOH HOH A . 
J 5 HOH 437 4472 4472 HOH HOH A . 
J 5 HOH 438 4473 4473 HOH HOH A . 
J 5 HOH 439 4474 4474 HOH HOH A . 
J 5 HOH 440 4475 4475 HOH HOH A . 
J 5 HOH 441 4476 4476 HOH HOH A . 
J 5 HOH 442 4477 4477 HOH HOH A . 
J 5 HOH 443 4478 4478 HOH HOH A . 
J 5 HOH 444 4479 4479 HOH HOH A . 
J 5 HOH 445 4480 4480 HOH HOH A . 
J 5 HOH 446 4481 4481 HOH HOH A . 
J 5 HOH 447 4482 4482 HOH HOH A . 
J 5 HOH 448 4484 4484 HOH HOH A . 
J 5 HOH 449 4485 4485 HOH HOH A . 
J 5 HOH 450 4486 4486 HOH HOH A . 
J 5 HOH 451 4487 4487 HOH HOH A . 
J 5 HOH 452 4488 4488 HOH HOH A . 
J 5 HOH 453 4489 4489 HOH HOH A . 
J 5 HOH 454 4490 4490 HOH HOH A . 
J 5 HOH 455 4491 4491 HOH HOH A . 
J 5 HOH 456 4493 4493 HOH HOH A . 
J 5 HOH 457 4494 4494 HOH HOH A . 
J 5 HOH 458 4495 4495 HOH HOH A . 
J 5 HOH 459 4496 4496 HOH HOH A . 
J 5 HOH 460 4497 4497 HOH HOH A . 
J 5 HOH 461 4498 4498 HOH HOH A . 
J 5 HOH 462 4499 4499 HOH HOH A . 
J 5 HOH 463 4500 4500 HOH HOH A . 
J 5 HOH 464 4501 4501 HOH HOH A . 
J 5 HOH 465 4502 4502 HOH HOH A . 
J 5 HOH 466 4503 4503 HOH HOH A . 
J 5 HOH 467 4504 4504 HOH HOH A . 
J 5 HOH 468 4505 4505 HOH HOH A . 
J 5 HOH 469 4506 4506 HOH HOH A . 
J 5 HOH 470 4507 4507 HOH HOH A . 
J 5 HOH 471 4508 4508 HOH HOH A . 
J 5 HOH 472 4509 4509 HOH HOH A . 
J 5 HOH 473 4510 4510 HOH HOH A . 
J 5 HOH 474 4511 4511 HOH HOH A . 
J 5 HOH 475 4512 4512 HOH HOH A . 
J 5 HOH 476 4513 4513 HOH HOH A . 
J 5 HOH 477 4514 4514 HOH HOH A . 
J 5 HOH 478 4515 4515 HOH HOH A . 
J 5 HOH 479 4516 4516 HOH HOH A . 
J 5 HOH 480 4517 4517 HOH HOH A . 
J 5 HOH 481 4518 4518 HOH HOH A . 
J 5 HOH 482 4519 4519 HOH HOH A . 
J 5 HOH 483 4520 4520 HOH HOH A . 
J 5 HOH 484 4521 4521 HOH HOH A . 
J 5 HOH 485 4522 4522 HOH HOH A . 
J 5 HOH 486 4523 4523 HOH HOH A . 
J 5 HOH 487 4524 4524 HOH HOH A . 
J 5 HOH 488 4525 4525 HOH HOH A . 
J 5 HOH 489 4527 4527 HOH HOH A . 
J 5 HOH 490 4528 4528 HOH HOH A . 
J 5 HOH 491 4529 4529 HOH HOH A . 
J 5 HOH 492 4530 4530 HOH HOH A . 
J 5 HOH 493 4531 4531 HOH HOH A . 
J 5 HOH 494 4532 4532 HOH HOH A . 
J 5 HOH 495 4533 4533 HOH HOH A . 
J 5 HOH 496 4534 4534 HOH HOH A . 
J 5 HOH 497 4535 4535 HOH HOH A . 
J 5 HOH 498 4536 4536 HOH HOH A . 
J 5 HOH 499 4537 4537 HOH HOH A . 
J 5 HOH 500 4538 4538 HOH HOH A . 
J 5 HOH 501 4539 4539 HOH HOH A . 
J 5 HOH 502 4540 4540 HOH HOH A . 
J 5 HOH 503 4541 4541 HOH HOH A . 
J 5 HOH 504 4542 4542 HOH HOH A . 
J 5 HOH 505 4543 4543 HOH HOH A . 
J 5 HOH 506 4544 4544 HOH HOH A . 
J 5 HOH 507 4545 4545 HOH HOH A . 
J 5 HOH 508 4546 4546 HOH HOH A . 
J 5 HOH 509 4547 4547 HOH HOH A . 
J 5 HOH 510 4548 4548 HOH HOH A . 
J 5 HOH 511 4549 4549 HOH HOH A . 
J 5 HOH 512 4550 4550 HOH HOH A . 
J 5 HOH 513 4551 4551 HOH HOH A . 
J 5 HOH 514 4552 4552 HOH HOH A . 
J 5 HOH 515 4553 4553 HOH HOH A . 
J 5 HOH 516 4554 4554 HOH HOH A . 
J 5 HOH 517 4555 4555 HOH HOH A . 
J 5 HOH 518 4556 4556 HOH HOH A . 
J 5 HOH 519 4557 4557 HOH HOH A . 
J 5 HOH 520 4558 4558 HOH HOH A . 
J 5 HOH 521 4559 4559 HOH HOH A . 
J 5 HOH 522 4562 4562 HOH HOH A . 
J 5 HOH 523 4563 4563 HOH HOH A . 
J 5 HOH 524 4564 4564 HOH HOH A . 
J 5 HOH 525 4565 4565 HOH HOH A . 
J 5 HOH 526 4567 4567 HOH HOH A . 
J 5 HOH 527 4568 4568 HOH HOH A . 
J 5 HOH 528 4569 4569 HOH HOH A . 
J 5 HOH 529 4570 4570 HOH HOH A . 
J 5 HOH 530 4571 4571 HOH HOH A . 
J 5 HOH 531 4572 4572 HOH HOH A . 
J 5 HOH 532 4574 4574 HOH HOH A . 
J 5 HOH 533 4575 4575 HOH HOH A . 
J 5 HOH 534 4576 4576 HOH HOH A . 
J 5 HOH 535 4577 4577 HOH HOH A . 
J 5 HOH 536 4578 4578 HOH HOH A . 
J 5 HOH 537 4579 4579 HOH HOH A . 
J 5 HOH 538 4581 4581 HOH HOH A . 
J 5 HOH 539 4582 4582 HOH HOH A . 
J 5 HOH 540 4583 4583 HOH HOH A . 
J 5 HOH 541 4584 4584 HOH HOH A . 
J 5 HOH 542 4585 4585 HOH HOH A . 
J 5 HOH 543 4586 4586 HOH HOH A . 
J 5 HOH 544 4587 4587 HOH HOH A . 
J 5 HOH 545 4588 4588 HOH HOH A . 
J 5 HOH 546 4589 4589 HOH HOH A . 
J 5 HOH 547 4591 4591 HOH HOH A . 
J 5 HOH 548 4593 4593 HOH HOH A . 
J 5 HOH 549 4594 4594 HOH HOH A . 
J 5 HOH 550 4595 4595 HOH HOH A . 
J 5 HOH 551 4596 4596 HOH HOH A . 
J 5 HOH 552 4597 4597 HOH HOH A . 
J 5 HOH 553 4598 4598 HOH HOH A . 
J 5 HOH 554 4599 4599 HOH HOH A . 
J 5 HOH 555 4600 4600 HOH HOH A . 
J 5 HOH 556 4601 4601 HOH HOH A . 
J 5 HOH 557 4602 4602 HOH HOH A . 
J 5 HOH 558 4603 4603 HOH HOH A . 
J 5 HOH 559 4604 4604 HOH HOH A . 
J 5 HOH 560 4605 4605 HOH HOH A . 
J 5 HOH 561 4606 4606 HOH HOH A . 
J 5 HOH 562 4607 4607 HOH HOH A . 
J 5 HOH 563 4608 4608 HOH HOH A . 
J 5 HOH 564 4609 4609 HOH HOH A . 
J 5 HOH 565 4610 4610 HOH HOH A . 
J 5 HOH 566 4611 4611 HOH HOH A . 
J 5 HOH 567 4612 4612 HOH HOH A . 
J 5 HOH 568 4613 4613 HOH HOH A . 
J 5 HOH 569 4614 4614 HOH HOH A . 
J 5 HOH 570 4615 4615 HOH HOH A . 
J 5 HOH 571 4616 4616 HOH HOH A . 
J 5 HOH 572 4617 4617 HOH HOH A . 
J 5 HOH 573 4618 4618 HOH HOH A . 
J 5 HOH 574 4619 4619 HOH HOH A . 
J 5 HOH 575 4622 4622 HOH HOH A . 
J 5 HOH 576 4624 4624 HOH HOH A . 
J 5 HOH 577 4625 4625 HOH HOH A . 
J 5 HOH 578 4628 4628 HOH HOH A . 
J 5 HOH 579 4629 4629 HOH HOH A . 
J 5 HOH 580 4630 4630 HOH HOH A . 
J 5 HOH 581 4631 4631 HOH HOH A . 
J 5 HOH 582 4632 4632 HOH HOH A . 
J 5 HOH 583 4633 4633 HOH HOH A . 
J 5 HOH 584 4634 4634 HOH HOH A . 
J 5 HOH 585 4635 4635 HOH HOH A . 
J 5 HOH 586 4636 4636 HOH HOH A . 
J 5 HOH 587 4637 4637 HOH HOH A . 
J 5 HOH 588 4638 4638 HOH HOH A . 
J 5 HOH 589 4639 4639 HOH HOH A . 
J 5 HOH 590 4640 4640 HOH HOH A . 
J 5 HOH 591 4641 4641 HOH HOH A . 
J 5 HOH 592 4642 4642 HOH HOH A . 
J 5 HOH 593 4643 4643 HOH HOH A . 
J 5 HOH 594 4644 4644 HOH HOH A . 
J 5 HOH 595 4645 4645 HOH HOH A . 
J 5 HOH 596 4653 4653 HOH HOH A . 
J 5 HOH 597 4657 4657 HOH HOH A . 
J 5 HOH 598 4659 4659 HOH HOH A . 
J 5 HOH 599 4662 4662 HOH HOH A . 
J 5 HOH 600 4663 4663 HOH HOH A . 
J 5 HOH 601 4665 4665 HOH HOH A . 
J 5 HOH 602 4666 4666 HOH HOH A . 
J 5 HOH 603 4667 4667 HOH HOH A . 
J 5 HOH 604 4668 4668 HOH HOH A . 
J 5 HOH 605 4669 4669 HOH HOH A . 
J 5 HOH 606 4670 4670 HOH HOH A . 
J 5 HOH 607 4671 4671 HOH HOH A . 
J 5 HOH 608 4672 4672 HOH HOH A . 
J 5 HOH 609 4673 4673 HOH HOH A . 
J 5 HOH 610 4674 4674 HOH HOH A . 
J 5 HOH 611 4675 4675 HOH HOH A . 
J 5 HOH 612 4676 4676 HOH HOH A . 
J 5 HOH 613 4677 4677 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 
# 
_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 2010-02-09 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-01 
# 
_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' 'Version format compliance' 
2 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 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.classification'       
2 3 'Structure model' '_software.contact_author'       
3 3 'Structure model' '_software.contact_author_email' 
4 3 'Structure model' '_software.date'                 
5 3 'Structure model' '_software.language'             
6 3 'Structure model' '_software.location'             
7 3 'Structure model' '_software.name'                 
8 3 'Structure model' '_software.type'                 
9 3 'Structure model' '_software.version'              
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 DENZO       .        ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com      'data reduction'  
http://www.hkl-xray.com/                     ?          ? 
2 SCALEPACK   .        ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com      'data scaling'    
http://www.hkl-xray.com/                     ?          ? 
3 REFMAC      5.2.0019 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 
4 PDB_EXTRACT 3.005    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              12 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              12 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              12 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.27 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.03 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 8   ? ? -25.15  127.42  
2  1 SER A 40  ? ? 76.22   -13.55  
3  1 SER A 51  ? ? -111.90 -102.45 
4  1 SER A 80  ? ? -67.45  94.28   
5  1 LEU A 180 ? ? 72.43   147.27  
6  1 GLN A 186 ? ? 77.58   -40.23  
7  1 TRP A 194 ? ? 55.02   83.42   
8  1 PHE A 200 ? ? -169.47 116.28  
9  1 PRO A 206 ? ? -69.45  92.72   
10 1 ASN A 207 ? ? -128.05 -165.70 
11 1 LEU A 213 ? ? -121.57 -147.35 
12 1 GLU A 300 ? ? 70.94   67.11   
13 1 TYR A 321 ? ? -166.80 97.64   
14 1 VAL A 342 ? ? -98.85  -62.87  
15 1 VAL A 405 ? ? -134.60 -145.08 
16 1 ASP A 474 ? ? 78.54   -10.16  
17 1 ASN A 518 ? ? 60.00   15.43   
18 1 SER A 521 ? ? 58.09   -145.37 
19 1 ILE A 565 ? ? -118.97 71.22   
20 1 CYS A 573 ? ? 82.31   -16.73  
21 1 LEU A 577 ? ? 87.17   155.23  
22 1 VAL A 651 ? ? -106.74 -67.76  
23 1 GLU A 774 ? ? -151.61 -23.09  
24 1 GLN A 793 ? ? -23.14  129.57  
25 1 PRO A 835 ? ? -45.82  156.59  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 HIS A 50  ? ? SER A 51  ? ? -148.79 
2 1 THR A 792 ? ? GLN A 793 ? ? -145.94 
# 
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 HIS 871 ? A HIS 871 
9  1 Y 1 A HIS 872 ? A HIS 872 
10 1 Y 1 A HIS 873 ? A HIS 873 
11 1 Y 1 A HIS 874 ? A HIS 874 
12 1 Y 1 A HIS 875 ? A HIS 875 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(1S,2R,3S,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium-1-yl]-1-hydroxyethyl}-2,3,4,5-tetrahydroxypentyl sulfate
;
NR3 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 GLYCEROL GOL 
5 water HOH 
# 
