data_3L4V
# 
_entry.id   3L4V 
# 
_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   3L4V         
RCSB  RCSB056835   
WWPDB D_1000056835 
# 
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 3L4W . unspecified 
PDB 3L4X . unspecified 
PDB 3L4Y . unspecified 
PDB 3L4Z . unspecified 
# 
_pdbx_database_status.entry_id                        3L4V 
_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           91.278 
_cell.length_b           109.693 
_cell.length_c           110.075 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           3L4V 
_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                         3L4V 
_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,3R,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   5   ?                   ? ?                     ? 
4 water       nat water 18.015    676 ?                   ? ?                     ? 
# 
_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              3L4V 
_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 3L4V ASP A 772 ? UNP O43451 ASN 858 VARIANT          772 1 
1 3L4V ALA A 869 ? UNP O43451 ?   ?   'EXPRESSION TAG' 869 2 
1 3L4V HIS A 870 ? UNP O43451 ?   ?   'EXPRESSION TAG' 870 3 
1 3L4V HIS A 871 ? UNP O43451 ?   ?   'EXPRESSION TAG' 871 4 
1 3L4V HIS A 872 ? UNP O43451 ?   ?   'EXPRESSION TAG' 872 5 
1 3L4V HIS A 873 ? UNP O43451 ?   ?   'EXPRESSION TAG' 873 6 
1 3L4V HIS A 874 ? UNP O43451 ?   ?   'EXPRESSION TAG' 874 7 
1 3L4V 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  
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 
KTL non-polymer         . 
;(1S,2R,3R,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 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
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.entry_id          3L4V 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.78 
_exptl_crystal.density_percent_sol   55.68 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '20% PEG 3350, 0.2M sodium sulfate, pH 6.5, vapor diffusion, hanging drop, temperature 293K' 
# 
_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   2009-04-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9175 
# 
_reflns.entry_id                     3L4V 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20.000 
_reflns.d_resolution_high            2.100 
_reflns.number_obs                   65399 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.122 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        9.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              7.300 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
2.10 2.14  100.00 0.515 ? ? 7.40 ? 1  
2.14 2.17  100.00 0.448 ? ? 7.40 ? 2  
2.17 2.22  100.00 0.425 ? ? 7.40 ? 3  
2.22 2.26  100.00 0.324 ? ? 7.40 ? 4  
2.26 2.31  100.00 0.381 ? ? 7.40 ? 5  
2.31 2.36  100.00 0.329 ? ? 7.40 ? 6  
2.36 2.42  100.00 0.283 ? ? 7.40 ? 7  
2.42 2.49  100.00 0.249 ? ? 7.40 ? 8  
2.49 2.56  100.00 0.233 ? ? 7.40 ? 9  
2.56 2.64  100.00 0.206 ? ? 7.40 ? 10 
2.64 2.74  100.00 0.179 ? ? 7.40 ? 11 
2.74 2.85  100.00 0.158 ? ? 7.40 ? 12 
2.85 2.98  100.00 0.136 ? ? 7.40 ? 13 
2.98 3.13  100.00 0.119 ? ? 7.40 ? 14 
3.13 3.33  100.00 0.101 ? ? 7.40 ? 15 
3.33 3.59  100.00 0.091 ? ? 7.40 ? 16 
3.59 3.94  100.00 0.081 ? ? 7.30 ? 17 
3.94 4.51  99.80  0.075 ? ? 7.30 ? 18 
4.51 5.66  99.90  0.073 ? ? 7.20 ? 19 
5.66 20.00 98.70  0.091 ? ? 6.60 ? 20 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3L4V 
_refine.ls_number_reflns_obs                     61109 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.81 
_refine.ls_d_res_high                            2.10 
_refine.ls_percent_reflns_obs                    99.00 
_refine.ls_R_factor_obs                          0.18456 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18209 
_refine.ls_R_factor_R_free                       0.23160 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  3266 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            0.50 
_refine.occupancy_max                            1.00 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_refine.B_iso_mean                               26.477 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.198 
_refine.pdbx_overall_ESU_R_Free                  0.177 
_refine.overall_SU_ML                            0.122 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.654 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6986 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         96 
_refine_hist.number_atoms_solvent             676 
_refine_hist.number_atoms_total               7758 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        19.81 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.015  0.022  ? 7300 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.583  1.949  ? 9983 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.774  5.000  ? 885  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.678 24.424 ? 373  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.762 15.000 ? 1115 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       14.552 15.000 ? 39   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.116  0.200  ? 1079 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 5720 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.206  0.200  ? 3349 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.312  0.200  ? 4901 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.161  0.200  ? 688  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.282  0.200  ? 50   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.230  0.200  ? 12   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.915  1.500  ? 4472 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.516  2.000  ? 7058 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.418  3.000  ? 3292 'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.693  4.500  ? 2915 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_R_work             4398 
_refine_ls_shell.R_factor_R_work                  0.231 
_refine_ls_shell.percent_reflns_obs               98.74 
_refine_ls_shell.R_factor_R_free                  0.303 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             240 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  3L4V 
_struct.title                     'Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol' 
_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        3L4V 
_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 3 ? 
G N N 3 ? 
H N N 4 ? 
# 
_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 ? GLY A 293 ? SER A 288 GLY A 293 5 ? 6  
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 GLN A 493 ? HIS A 497 ? GLN A 493 HIS A 497 1 ? 5  
HELX_P HELX_P12 12 LEU A 499 ? PHE A 516 ? LEU A 499 PHE A 516 1 ? 18 
HELX_P HELX_P13 13 GLY A 531 ? PHE A 535 ? GLY A 531 PHE A 535 5 ? 5  
HELX_P HELX_P14 14 THR A 546 ? PHE A 563 ? THR A 546 PHE A 563 1 ? 18 
HELX_P HELX_P15 15 PRO A 580 ? ALA A 592 ? PRO A 580 ALA A 592 1 ? 13 
HELX_P HELX_P16 16 ASP A 609 ? GLY A 614 ? ASP A 609 GLY A 614 5 ? 6  
HELX_P HELX_P17 17 SER A 617 ? LEU A 633 ? SER A 617 LEU A 633 1 ? 17 
HELX_P HELX_P18 18 LEU A 633 ? ARG A 647 ? LEU A 633 ARG A 647 1 ? 15 
HELX_P HELX_P19 19 PRO A 654 ? PHE A 659 ? PRO A 654 PHE A 659 1 ? 6  
HELX_P HELX_P20 20 ASP A 662 ? TRP A 666 ? ASP A 662 TRP A 666 5 ? 5  
HELX_P HELX_P21 21 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 ? ? ? ? ? ? ? 2.033 ? 
disulf2 disulf ? ? A CYS 458 SG  ? ? ? 1_555 A CYS 483 SG ? ? A CYS 458  A CYS 483  1_555 ? ? ? ? ? ? ? 2.874 ? 
disulf3 disulf ? ? A CYS 573 SG  ? ? ? 1_555 A CYS 584 SG ? ? A CYS 573  A CYS 584  1_555 ? ? ? ? ? ? ? 2.052 ? 
covale1 covale ? ? E NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? A NAG 2003 A NAG 2004 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale2 covale ? ? A ASN 393 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 393  A NAG 2003 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale3 covale ? ? C NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? A NAG 2001 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale4 covale ? ? A ASN 209 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 209  A NAG 2005 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale5 covale ? ? A ASN 741 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 741  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.460 ? 
# 
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 1.11  
2 GLY 181 A . ? GLY 181 A GLU 182 A ? GLU 182 A 1 2.07  
3 ALA 248 A . ? ALA 248 A PRO 249 A ? PRO 249 A 1 -5.85 
4 GLU 446 A . ? GLU 446 A VAL 447 A ? VAL 447 A 1 6.26  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 8  ? 
C ? 3  ? 
D ? 5  ? 
E ? 9  ? 
F ? 3  ? 
G ? 2  ? 
H ? 5  ? 
I ? 2  ? 
J ? 10 ? 
K ? 9  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? anti-parallel 
B 1 2  ? anti-parallel 
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? anti-parallel 
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
D 1 2  ? anti-parallel 
D 2 3  ? anti-parallel 
D 3 4  ? anti-parallel 
D 4 5  ? anti-parallel 
E 1 2  ? parallel      
E 2 3  ? parallel      
E 3 4  ? parallel      
E 4 5  ? parallel      
E 5 6  ? parallel      
E 6 7  ? parallel      
E 7 8  ? parallel      
E 8 9  ? parallel      
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
G 1 2  ? anti-parallel 
H 1 2  ? anti-parallel 
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? anti-parallel 
I 1 2  ? anti-parallel 
J 1 2  ? anti-parallel 
J 2 3  ? anti-parallel 
J 3 4  ? anti-parallel 
J 4 5  ? anti-parallel 
J 5 6  ? parallel      
J 6 7  ? anti-parallel 
J 7 8  ? parallel      
J 8 9  ? anti-parallel 
J 9 10 ? anti-parallel 
K 1 2  ? anti-parallel 
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? anti-parallel 
K 5 6  ? parallel      
K 6 7  ? anti-parallel 
K 7 8  ? parallel      
K 8 9  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  CYS A 32  ? TRP A 33  ? CYS A 32  TRP A 33  
A 2  CYS A 44  ? TYR A 45  ? CYS A 44  TYR A 45  
B 1  SER A 51  ? ASN A 60  ? SER A 51  ASN A 60  
B 2  GLY A 64  ? LEU A 72  ? GLY A 64  LEU A 72  
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  HIS A 295 ? LEU A 296 ? HIS A 295 LEU A 296 
E 8  ARG A 598 ? ASN A 599 ? ARG A 598 ASN A 599 
E 9  ASP A 571 ? ILE A 572 ? ASP A 571 ILE A 572 
F 1  ILE A 369 ? SER A 370 ? ILE A 369 SER A 370 
F 2  GLY A 408 ? VAL A 411 ? GLY A 408 VAL A 411 
F 3  GLY A 403 ? VAL A 405 ? GLY A 403 VAL A 405 
G 1  VAL A 487 ? GLN A 488 ? VAL A 487 GLN A 488 
G 2  GLY A 491 ? LYS A 492 ? GLY A 491 LYS A 492 
H 1  ALA A 652 ? ARG A 653 ? ALA A 652 ARG A 653 
H 2  PHE A 672 ? TRP A 674 ? PHE A 672 TRP A 674 
H 3  LEU A 678 ? THR A 681 ? LEU A 678 THR A 681 
H 4  GLY A 726 ? ARG A 730 ? GLY A 726 ARG A 730 
H 5  TRP A 700 ? ASP A 702 ? TRP A 700 ASP A 702 
I 1  LYS A 690 ? VAL A 695 ? LYS A 690 VAL A 695 
I 2  GLN A 714 ? GLU A 719 ? GLN A 714 GLU A 719 
J 1  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
J 2  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
J 3  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
J 4  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
J 5  ALA A 764 ? TRP A 770 ? ALA A 764 TRP A 770 
J 6  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
J 7  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
J 8  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
J 9  VAL A 850 ? THR A 854 ? VAL A 850 THR A 854 
J 10 THR A 841 ? ASP A 845 ? THR A 841 ASP A 845 
K 1  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
K 2  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
K 3  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
K 4  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
K 5  ALA A 764 ? TRP A 770 ? ALA A 764 TRP A 770 
K 6  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
K 7  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
K 8  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
K 9  LEU A 858 ? LEU A 859 ? LEU A 858 LEU A 859 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N CYS A 32  ? N CYS A 32  O TYR A 45  ? O TYR A 45  
B 1 2  N GLU A 55  ? N GLU A 55  O ARG A 68  ? O ARG A 68  
B 2 3  N ALA A 67  ? N ALA A 67  O LEU A 87  ? O LEU A 87  
B 3 4  N GLU A 90  ? N GLU A 90  O HIS A 98  ? O HIS A 98  
B 4 5  N PHE A 99  ? N PHE A 99  O PHE A 262 ? O PHE A 262 
B 5 6  O PHE A 265 ? O PHE A 265 N GLY A 232 ? N GLY A 232 
B 6 7  O PHE A 231 ? O PHE A 231 N CYS A 222 ? N CYS A 222 
B 7 8  O LEU A 221 ? O LEU A 221 N TYR A 178 ? N TYR A 178 
C 1 2  N GLU A 132 ? N GLU A 132 O LYS A 141 ? O LYS A 141 
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 VAL A 323 ? O VAL A 323 N LEU A 296 ? N LEU A 296 
E 7 8  N HIS A 295 ? N HIS A 295 O ASN A 599 ? O ASN A 599 
E 8 9  O ARG A 598 ? O ARG A 598 N ILE A 572 ? N ILE A 572 
F 1 2  N ILE A 369 ? N ILE A 369 O VAL A 411 ? O VAL A 411 
F 2 3  O THR A 410 ? O THR A 410 N GLY A 403 ? N GLY A 403 
G 1 2  N GLN A 488 ? N GLN A 488 O GLY A 491 ? O GLY A 491 
H 1 2  N ARG A 653 ? N ARG A 653 O LEU A 673 ? O LEU A 673 
H 2 3  N PHE A 672 ? N PHE A 672 O ILE A 680 ? O ILE A 680 
H 3 4  N LEU A 679 ? N LEU A 679 O HIS A 728 ? O HIS A 728 
H 4 5  O LEU A 729 ? O LEU A 729 N TYR A 701 ? N TYR A 701 
I 1 2  N VAL A 691 ? N VAL A 691 O MET A 718 ? O MET A 718 
J 1 2  N LYS A 830 ? N LYS A 830 O THR A 865 ? O THR A 865 
J 2 3  O TYR A 864 ? O TYR A 864 N VAL A 798 ? N VAL A 798 
J 3 4  O GLU A 797 ? O GLU A 797 N SER A 790 ? N SER A 790 
J 4 5  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
J 5 6  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
J 6 7  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
J 7 8  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
J 8 9  N ILE A 818 ? N ILE A 818 O ALA A 851 ? O ALA A 851 
J 9 10 O ILE A 852 ? O ILE A 852 N THR A 843 ? N THR A 843 
K 1 2  N LYS A 830 ? N LYS A 830 O THR A 865 ? O THR A 865 
K 2 3  O TYR A 864 ? O TYR A 864 N VAL A 798 ? N VAL A 798 
K 3 4  O GLU A 797 ? O GLU A 797 N SER A 790 ? N SER A 790 
K 4 5  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
K 5 6  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
K 6 7  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
K 7 8  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
K 8 9  N PHE A 813 ? N PHE A 813 O LEU A 858 ? O LEU A 858 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE KTL A 1001' 
AC2 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG A 2001' 
AC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 2002' 
AC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 2003' 
AC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 2004' 
AC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 2005' 
# 
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 21 ASP A 203 ? ASP A 203  . ? 1_555 ? 
2  AC1 21 TYR A 299 ? TYR A 299  . ? 1_555 ? 
3  AC1 21 ASP A 327 ? ASP A 327  . ? 1_555 ? 
4  AC1 21 ILE A 364 ? ILE A 364  . ? 1_555 ? 
5  AC1 21 TRP A 406 ? TRP A 406  . ? 1_555 ? 
6  AC1 21 TRP A 441 ? TRP A 441  . ? 1_555 ? 
7  AC1 21 ASP A 443 ? ASP A 443  . ? 1_555 ? 
8  AC1 21 ARG A 526 ? ARG A 526  . ? 1_555 ? 
9  AC1 21 TRP A 539 ? TRP A 539  . ? 1_555 ? 
10 AC1 21 ASP A 542 ? ASP A 542  . ? 1_555 ? 
11 AC1 21 PHE A 575 ? PHE A 575  . ? 1_555 ? 
12 AC1 21 HIS A 600 ? HIS A 600  . ? 1_555 ? 
13 AC1 21 HOH H .   ? HOH A 927  . ? 1_555 ? 
14 AC1 21 HOH H .   ? HOH A 1040 . ? 1_555 ? 
15 AC1 21 HOH H .   ? HOH A 1041 . ? 1_555 ? 
16 AC1 21 HOH H .   ? HOH A 1085 . ? 1_555 ? 
17 AC1 21 HOH H .   ? HOH A 1282 . ? 1_555 ? 
18 AC1 21 HOH H .   ? HOH A 1295 . ? 1_555 ? 
19 AC1 21 HOH H .   ? HOH A 1298 . ? 1_555 ? 
20 AC1 21 HOH H .   ? HOH A 1356 . ? 1_555 ? 
21 AC1 21 HOH H .   ? HOH A 1518 . ? 1_555 ? 
22 AC2 9  SER A 146 ? SER A 146  . ? 2_675 ? 
23 AC2 9  ASN A 147 ? ASN A 147  . ? 2_675 ? 
24 AC2 9  ASN A 148 ? ASN A 148  . ? 2_675 ? 
25 AC2 9  ASN A 741 ? ASN A 741  . ? 1_555 ? 
26 AC2 9  ASN A 750 ? ASN A 750  . ? 1_555 ? 
27 AC2 9  HOH H .   ? HOH A 945  . ? 1_555 ? 
28 AC2 9  HOH H .   ? HOH A 1089 . ? 1_555 ? 
29 AC2 9  HOH H .   ? HOH A 1247 . ? 1_555 ? 
30 AC2 9  NAG D .   ? NAG A 2002 . ? 1_555 ? 
31 AC3 3  HOH H .   ? HOH A 1173 . ? 2_675 ? 
32 AC3 3  HOH H .   ? HOH A 1350 . ? 2_675 ? 
33 AC3 3  NAG C .   ? NAG A 2001 . ? 1_555 ? 
34 AC4 10 LYS A 389 ? LYS A 389  . ? 1_555 ? 
35 AC4 10 ASN A 393 ? ASN A 393  . ? 1_555 ? 
36 AC4 10 GLY A 397 ? GLY A 397  . ? 1_555 ? 
37 AC4 10 VAL A 398 ? VAL A 398  . ? 1_555 ? 
38 AC4 10 VAL A 487 ? VAL A 487  . ? 1_555 ? 
39 AC4 10 GLN A 488 ? GLN A 488  . ? 1_555 ? 
40 AC4 10 HIS A 489 ? HIS A 489  . ? 1_555 ? 
41 AC4 10 HOH H .   ? HOH A 1193 . ? 1_555 ? 
42 AC4 10 HOH H .   ? HOH A 1449 . ? 1_555 ? 
43 AC4 10 NAG F .   ? NAG A 2004 . ? 1_555 ? 
44 AC5 3  LYS A 389 ? LYS A 389  . ? 1_555 ? 
45 AC5 3  HOH H .   ? HOH A 1458 . ? 1_555 ? 
46 AC5 3  NAG E .   ? NAG A 2003 . ? 1_555 ? 
47 AC6 3  GLY A 208 ? GLY A 208  . ? 1_555 ? 
48 AC6 3  ASN A 209 ? ASN A 209  . ? 1_555 ? 
49 AC6 3  HOH H .   ? HOH A 1482 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3L4V 
_atom_sites.fract_transf_matrix[1][1]   0.010956 
_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]   0.009116 
_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]   0.009085 
_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   ? 57.864 72.502  -8.520  1.00 47.90 ? 7    VAL A N   1 
ATOM   2    C CA  . VAL A 1 7   ? 57.998 73.475  -7.395  1.00 47.33 ? 7    VAL A CA  1 
ATOM   3    C C   . VAL A 1 7   ? 59.129 73.038  -6.448  1.00 46.61 ? 7    VAL A C   1 
ATOM   4    O O   . VAL A 1 7   ? 59.064 71.957  -5.869  1.00 46.74 ? 7    VAL A O   1 
ATOM   5    C CB  . VAL A 1 7   ? 56.643 73.635  -6.598  1.00 47.58 ? 7    VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 7   ? 56.647 74.889  -5.735  1.00 47.02 ? 7    VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 7   ? 55.464 73.703  -7.553  1.00 48.06 ? 7    VAL A CG2 1 
ATOM   8    N N   . ASN A 1 8   ? 60.168 73.877  -6.328  1.00 45.04 ? 8    ASN A N   1 
ATOM   9    C CA  . ASN A 1 8   ? 61.108 73.854  -5.193  1.00 42.89 ? 8    ASN A CA  1 
ATOM   10   C C   . ASN A 1 8   ? 60.268 73.808  -3.908  1.00 41.15 ? 8    ASN A C   1 
ATOM   11   O O   . ASN A 1 8   ? 59.292 74.550  -3.790  1.00 39.87 ? 8    ASN A O   1 
ATOM   12   C CB  . ASN A 1 8   ? 62.015 75.105  -5.320  1.00 43.76 ? 8    ASN A CB  1 
ATOM   13   C CG  . ASN A 1 8   ? 62.703 75.546  -4.010  1.00 45.94 ? 8    ASN A CG  1 
ATOM   14   O OD1 . ASN A 1 8   ? 63.111 76.711  -3.904  1.00 49.60 ? 8    ASN A OD1 1 
ATOM   15   N ND2 . ASN A 1 8   ? 62.861 74.646  -3.043  1.00 47.51 ? 8    ASN A ND2 1 
ATOM   16   N N   . GLU A 1 9   ? 60.604 72.917  -2.970  1.00 38.70 ? 9    GLU A N   1 
ATOM   17   C CA  . GLU A 1 9   ? 59.767 72.738  -1.762  1.00 38.03 ? 9    GLU A CA  1 
ATOM   18   C C   . GLU A 1 9   ? 59.563 73.962  -0.824  1.00 34.70 ? 9    GLU A C   1 
ATOM   19   O O   . GLU A 1 9   ? 58.517 74.086  -0.197  1.00 33.95 ? 9    GLU A O   1 
ATOM   20   C CB  . GLU A 1 9   ? 60.126 71.446  -0.988  1.00 38.32 ? 9    GLU A CB  1 
ATOM   21   C CG  . GLU A 1 9   ? 61.394 71.446  -0.169  1.00 40.33 ? 9    GLU A CG  1 
ATOM   22   C CD  . GLU A 1 9   ? 61.698 70.053  0.431   1.00 42.40 ? 9    GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 9   ? 61.493 69.020  -0.265  1.00 47.52 ? 9    GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 9   ? 62.157 69.980  1.605   1.00 47.49 ? 9    GLU A OE2 1 
ATOM   25   N N   . LEU A 1 10  ? 60.529 74.884  -0.801  1.00 31.88 ? 10   LEU A N   1 
ATOM   26   C CA  . LEU A 1 10  ? 60.451 76.100  0.021   1.00 29.43 ? 10   LEU A CA  1 
ATOM   27   C C   . LEU A 1 10  ? 59.394 77.061  -0.483  1.00 28.01 ? 10   LEU A C   1 
ATOM   28   O O   . LEU A 1 10  ? 58.922 77.916  0.283   1.00 27.46 ? 10   LEU A O   1 
ATOM   29   C CB  . LEU A 1 10  ? 61.823 76.783  0.145   1.00 29.25 ? 10   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 10  ? 62.885 75.809  0.691   1.00 30.21 ? 10   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 10  ? 64.204 76.466  0.961   1.00 31.76 ? 10   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 10  ? 62.410 75.041  1.942   1.00 30.76 ? 10   LEU A CD2 1 
ATOM   33   N N   . GLU A 1 11  ? 58.968 76.863  -1.736  1.00 25.72 ? 11   GLU A N   1 
ATOM   34   C CA  . GLU A 1 11  ? 58.020 77.746  -2.420  1.00 24.88 ? 11   GLU A CA  1 
ATOM   35   C C   . GLU A 1 11  ? 56.618 77.202  -2.546  1.00 24.83 ? 11   GLU A C   1 
ATOM   36   O O   . GLU A 1 11  ? 55.786 77.841  -3.194  1.00 23.82 ? 11   GLU A O   1 
ATOM   37   C CB  . GLU A 1 11  ? 58.524 78.124  -3.810  1.00 25.27 ? 11   GLU A CB  1 
ATOM   38   C CG  . GLU A 1 11  ? 59.886 78.782  -3.744  1.00 29.97 ? 11   GLU A CG  1 
ATOM   39   C CD  . GLU A 1 11  ? 60.558 78.972  -5.081  1.00 35.84 ? 11   GLU A CD  1 
ATOM   40   O OE1 . GLU A 1 11  ? 59.923 78.743  -6.130  1.00 36.60 ? 11   GLU A OE1 1 
ATOM   41   O OE2 . GLU A 1 11  ? 61.746 79.386  -5.057  1.00 40.97 ? 11   GLU A OE2 1 
ATOM   42   N N   . ARG A 1 12  ? 56.338 76.038  -1.947  1.00 23.52 ? 12   ARG A N   1 
ATOM   43   C CA  . ARG A 1 12  ? 54.967 75.510  -2.018  1.00 23.98 ? 12   ARG A CA  1 
ATOM   44   C C   . ARG A 1 12  ? 54.071 76.318  -1.111  1.00 22.92 ? 12   ARG A C   1 
ATOM   45   O O   . ARG A 1 12  ? 54.447 76.620  0.028   1.00 22.45 ? 12   ARG A O   1 
ATOM   46   C CB  . ARG A 1 12  ? 54.904 74.054  -1.612  1.00 24.11 ? 12   ARG A CB  1 
ATOM   47   C CG  . ARG A 1 12  ? 55.779 73.106  -2.417  1.00 26.60 ? 12   ARG A CG  1 
ATOM   48   C CD  . ARG A 1 12  ? 55.712 71.731  -1.779  1.00 30.06 ? 12   ARG A CD  1 
ATOM   49   N NE  . ARG A 1 12  ? 56.604 70.781  -2.434  1.00 36.31 ? 12   ARG A NE  1 
ATOM   50   C CZ  . ARG A 1 12  ? 56.775 69.513  -2.050  1.00 37.59 ? 12   ARG A CZ  1 
ATOM   51   N NH1 . ARG A 1 12  ? 56.106 69.010  -0.999  1.00 36.55 ? 12   ARG A NH1 1 
ATOM   52   N NH2 . ARG A 1 12  ? 57.641 68.754  -2.708  1.00 37.90 ? 12   ARG A NH2 1 
ATOM   53   N N   . ILE A 1 13  ? 52.913 76.708  -1.640  1.00 22.49 ? 13   ILE A N   1 
ATOM   54   C CA  . ILE A 1 13  ? 51.907 77.478  -0.921  1.00 21.39 ? 13   ILE A CA  1 
ATOM   55   C C   . ILE A 1 13  ? 50.780 76.503  -0.490  1.00 22.37 ? 13   ILE A C   1 
ATOM   56   O O   . ILE A 1 13  ? 50.119 75.890  -1.319  1.00 22.54 ? 13   ILE A O   1 
ATOM   57   C CB  . ILE A 1 13  ? 51.353 78.647  -1.780  1.00 21.56 ? 13   ILE A CB  1 
ATOM   58   C CG1 . ILE A 1 13  ? 52.467 79.628  -2.211  1.00 20.14 ? 13   ILE A CG1 1 
ATOM   59   C CG2 . ILE A 1 13  ? 50.227 79.373  -1.067  1.00 20.80 ? 13   ILE A CG2 1 
ATOM   60   C CD1 . ILE A 1 13  ? 53.272 80.335  -1.084  1.00 17.58 ? 13   ILE A CD1 1 
ATOM   61   N N   . ASN A 1 14  ? 50.567 76.385  0.813   1.00 22.19 ? 14   ASN A N   1 
ATOM   62   C CA  . ASN A 1 14  ? 49.752 75.344  1.399   1.00 21.70 ? 14   ASN A CA  1 
ATOM   63   C C   . ASN A 1 14  ? 48.295 75.467  1.000   1.00 21.74 ? 14   ASN A C   1 
ATOM   64   O O   . ASN A 1 14  ? 47.650 76.498  1.232   1.00 20.66 ? 14   ASN A O   1 
ATOM   65   C CB  . ASN A 1 14  ? 49.901 75.425  2.926   1.00 22.15 ? 14   ASN A CB  1 
ATOM   66   C CG  . ASN A 1 14  ? 49.269 74.223  3.655   1.00 22.36 ? 14   ASN A CG  1 
ATOM   67   O OD1 . ASN A 1 14  ? 48.858 73.233  3.032   1.00 18.79 ? 14   ASN A OD1 1 
ATOM   68   N ND2 . ASN A 1 14  ? 49.215 74.314  4.983   1.00 18.93 ? 14   ASN A ND2 1 
ATOM   69   N N   . CYS A 1 15  ? 47.793 74.404  0.379   1.00 23.08 ? 15   CYS A N   1 
ATOM   70   C CA  . CYS A 1 15  ? 46.398 74.302  -0.051  1.00 23.00 ? 15   CYS A CA  1 
ATOM   71   C C   . CYS A 1 15  ? 45.494 73.639  1.024   1.00 22.41 ? 15   CYS A C   1 
ATOM   72   O O   . CYS A 1 15  ? 44.265 73.640  0.916   1.00 22.73 ? 15   CYS A O   1 
ATOM   73   C CB  . CYS A 1 15  ? 46.335 73.560  -1.412  1.00 22.92 ? 15   CYS A CB  1 
ATOM   74   S SG  . CYS A 1 15  ? 44.664 73.236  -2.012  1.00 28.20 ? 15   CYS A SG  1 
ATOM   75   N N   . ILE A 1 16  ? 46.092 73.082  2.068   1.00 22.49 ? 16   ILE A N   1 
ATOM   76   C CA  . ILE A 1 16  ? 45.290 72.519  3.168   1.00 22.48 ? 16   ILE A CA  1 
ATOM   77   C C   . ILE A 1 16  ? 45.764 73.098  4.515   1.00 23.00 ? 16   ILE A C   1 
ATOM   78   O O   . ILE A 1 16  ? 46.382 72.398  5.311   1.00 21.41 ? 16   ILE A O   1 
ATOM   79   C CB  . ILE A 1 16  ? 45.248 70.912  3.173   1.00 23.20 ? 16   ILE A CB  1 
ATOM   80   C CG1 . ILE A 1 16  ? 44.753 70.359  1.820   1.00 19.01 ? 16   ILE A CG1 1 
ATOM   81   C CG2 . ILE A 1 16  ? 44.308 70.406  4.271   1.00 22.23 ? 16   ILE A CG2 1 
ATOM   82   C CD1 . ILE A 1 16  ? 44.957 68.836  1.634   1.00 21.91 ? 16   ILE A CD1 1 
ATOM   83   N N   . PRO A 1 17  ? 45.452 74.383  4.771   1.00 23.78 ? 17   PRO A N   1 
ATOM   84   C CA  . PRO A 1 17  ? 45.847 75.030  6.037   1.00 24.71 ? 17   PRO A CA  1 
ATOM   85   C C   . PRO A 1 17  ? 44.936 74.617  7.208   1.00 25.59 ? 17   PRO A C   1 
ATOM   86   O O   . PRO A 1 17  ? 45.247 74.910  8.366   1.00 26.69 ? 17   PRO A O   1 
ATOM   87   C CB  . PRO A 1 17  ? 45.658 76.507  5.732   1.00 24.59 ? 17   PRO A CB  1 
ATOM   88   C CG  . PRO A 1 17  ? 44.476 76.523  4.792   1.00 24.03 ? 17   PRO A CG  1 
ATOM   89   C CD  . PRO A 1 17  ? 44.683 75.303  3.907   1.00 23.44 ? 17   PRO A CD  1 
ATOM   90   N N   . ASP A 1 18  ? 43.852 73.902  6.899   1.00 26.19 ? 18   ASP A N   1 
ATOM   91   C CA  . ASP A 1 18  ? 42.729 73.694  7.822   1.00 27.20 ? 18   ASP A CA  1 
ATOM   92   C C   . ASP A 1 18  ? 42.654 72.310  8.523   1.00 28.01 ? 18   ASP A C   1 
ATOM   93   O O   . ASP A 1 18  ? 41.898 72.150  9.474   1.00 27.13 ? 18   ASP A O   1 
ATOM   94   C CB  . ASP A 1 18  ? 41.413 73.953  7.073   1.00 27.02 ? 18   ASP A CB  1 
ATOM   95   C CG  . ASP A 1 18  ? 41.289 73.111  5.786   1.00 27.81 ? 18   ASP A CG  1 
ATOM   96   O OD1 . ASP A 1 18  ? 42.217 73.074  4.974   1.00 26.00 ? 18   ASP A OD1 1 
ATOM   97   O OD2 . ASP A 1 18  ? 40.253 72.471  5.573   1.00 32.09 ? 18   ASP A OD2 1 
ATOM   98   N N   . GLN A 1 19  ? 43.406 71.320  8.029   1.00 28.58 ? 19   GLN A N   1 
ATOM   99   C CA  . GLN A 1 19  ? 43.308 69.929  8.506   1.00 29.18 ? 19   GLN A CA  1 
ATOM   100  C C   . GLN A 1 19  ? 44.584 69.175  8.148   1.00 29.55 ? 19   GLN A C   1 
ATOM   101  O O   . GLN A 1 19  ? 45.346 69.659  7.338   1.00 30.08 ? 19   GLN A O   1 
ATOM   102  C CB  . GLN A 1 19  ? 42.064 69.245  7.914   1.00 29.38 ? 19   GLN A CB  1 
ATOM   103  C CG  . GLN A 1 19  ? 42.046 69.064  6.393   1.00 28.19 ? 19   GLN A CG  1 
ATOM   104  C CD  . GLN A 1 19  ? 40.697 68.627  5.872   1.00 30.16 ? 19   GLN A CD  1 
ATOM   105  O OE1 . GLN A 1 19  ? 39.671 69.016  6.413   1.00 36.38 ? 19   GLN A OE1 1 
ATOM   106  N NE2 . GLN A 1 19  ? 40.681 67.846  4.808   1.00 25.64 ? 19   GLN A NE2 1 
ATOM   107  N N   . PRO A 1 20  ? 44.861 68.008  8.784   1.00 30.60 ? 20   PRO A N   1 
ATOM   108  C CA  . PRO A 1 20  ? 46.019 67.209  8.286   1.00 29.87 ? 20   PRO A CA  1 
ATOM   109  C C   . PRO A 1 20  ? 45.856 66.795  6.799   1.00 28.75 ? 20   PRO A C   1 
ATOM   110  O O   . PRO A 1 20  ? 44.735 66.486  6.353   1.00 27.59 ? 20   PRO A O   1 
ATOM   111  C CB  . PRO A 1 20  ? 46.062 65.979  9.209   1.00 29.67 ? 20   PRO A CB  1 
ATOM   112  C CG  . PRO A 1 20  ? 44.907 66.075  10.129  1.00 31.01 ? 20   PRO A CG  1 
ATOM   113  C CD  . PRO A 1 20  ? 44.203 67.397  9.958   1.00 31.14 ? 20   PRO A CD  1 
ATOM   114  N N   . PRO A 1 21  ? 46.963 66.837  6.033   1.00 27.84 ? 21   PRO A N   1 
ATOM   115  C CA  . PRO A 1 21  ? 46.855 66.737  4.567   1.00 26.74 ? 21   PRO A CA  1 
ATOM   116  C C   . PRO A 1 21  ? 46.502 65.332  4.080   1.00 26.53 ? 21   PRO A C   1 
ATOM   117  O O   . PRO A 1 21  ? 47.075 64.357  4.563   1.00 27.27 ? 21   PRO A O   1 
ATOM   118  C CB  . PRO A 1 21  ? 48.233 67.167  4.087   1.00 26.19 ? 21   PRO A CB  1 
ATOM   119  C CG  . PRO A 1 21  ? 49.162 66.875  5.240   1.00 26.36 ? 21   PRO A CG  1 
ATOM   120  C CD  . PRO A 1 21  ? 48.362 66.988  6.495   1.00 27.40 ? 21   PRO A CD  1 
ATOM   121  N N   . THR A 1 22  ? 45.520 65.222  3.184   1.00 26.38 ? 22   THR A N   1 
ATOM   122  C CA  . THR A 1 22  ? 45.174 63.928  2.553   1.00 26.14 ? 22   THR A CA  1 
ATOM   123  C C   . THR A 1 22  ? 45.091 64.091  1.052   1.00 26.85 ? 22   THR A C   1 
ATOM   124  O O   . THR A 1 22  ? 44.695 65.146  0.573   1.00 27.01 ? 22   THR A O   1 
ATOM   125  C CB  . THR A 1 22  ? 43.803 63.346  3.028   1.00 25.12 ? 22   THR A CB  1 
ATOM   126  O OG1 . THR A 1 22  ? 42.741 64.217  2.638   1.00 25.54 ? 22   THR A OG1 1 
ATOM   127  C CG2 . THR A 1 22  ? 43.757 63.178  4.527   1.00 24.41 ? 22   THR A CG2 1 
ATOM   128  N N   . LYS A 1 23  ? 45.423 63.043  0.311   1.00 27.90 ? 23   LYS A N   1 
ATOM   129  C CA  . LYS A 1 23  ? 45.296 63.090  -1.149  1.00 29.54 ? 23   LYS A CA  1 
ATOM   130  C C   . LYS A 1 23  ? 43.867 63.356  -1.601  1.00 29.08 ? 23   LYS A C   1 
ATOM   131  O O   . LYS A 1 23  ? 43.637 64.089  -2.559  1.00 29.01 ? 23   LYS A O   1 
ATOM   132  C CB  . LYS A 1 23  ? 45.898 61.853  -1.842  1.00 29.54 ? 23   LYS A CB  1 
ATOM   133  C CG  . LYS A 1 23  ? 46.160 62.079  -3.352  1.00 31.34 ? 23   LYS A CG  1 
ATOM   134  C CD  . LYS A 1 23  ? 46.449 60.766  -4.118  1.00 31.50 ? 23   LYS A CD  1 
ATOM   135  C CE  . LYS A 1 23  ? 46.859 60.975  -5.599  1.00 34.22 ? 23   LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 23  ? 45.994 61.907  -6.419  1.00 35.38 ? 23   LYS A NZ  1 
ATOM   137  N N   . ALA A 1 24  ? 42.902 62.775  -0.908  1.00 29.71 ? 24   ALA A N   1 
ATOM   138  C CA  . ALA A 1 24  ? 41.510 62.934  -1.292  1.00 30.11 ? 24   ALA A CA  1 
ATOM   139  C C   . ALA A 1 24  ? 41.033 64.397  -1.213  1.00 30.51 ? 24   ALA A C   1 
ATOM   140  O O   . ALA A 1 24  ? 40.354 64.892  -2.131  1.00 30.96 ? 24   ALA A O   1 
ATOM   141  C CB  . ALA A 1 24  ? 40.635 62.031  -0.432  1.00 30.65 ? 24   ALA A CB  1 
ATOM   142  N N   . THR A 1 25  ? 41.374 65.095  -0.127  1.00 30.55 ? 25   THR A N   1 
ATOM   143  C CA  . THR A 1 25  ? 41.044 66.524  0.001   1.00 30.85 ? 25   THR A CA  1 
ATOM   144  C C   . THR A 1 25  ? 41.781 67.372  -1.062  1.00 31.23 ? 25   THR A C   1 
ATOM   145  O O   . THR A 1 25  ? 41.213 68.294  -1.633  1.00 30.27 ? 25   THR A O   1 
ATOM   146  C CB  . THR A 1 25  ? 41.360 67.031  1.418   1.00 31.42 ? 25   THR A CB  1 
ATOM   147  O OG1 . THR A 1 25  ? 40.463 66.400  2.337   1.00 32.07 ? 25   THR A OG1 1 
ATOM   148  C CG2 . THR A 1 25  ? 41.209 68.545  1.527   1.00 28.84 ? 25   THR A CG2 1 
ATOM   149  N N   . CYS A 1 26  ? 43.039 67.030  -1.319  1.00 32.27 ? 26   CYS A N   1 
ATOM   150  C CA  . CYS A 1 26  ? 43.850 67.698  -2.341  1.00 33.55 ? 26   CYS A CA  1 
ATOM   151  C C   . CYS A 1 26  ? 43.220 67.603  -3.738  1.00 33.98 ? 26   CYS A C   1 
ATOM   152  O O   . CYS A 1 26  ? 43.051 68.621  -4.417  1.00 33.30 ? 26   CYS A O   1 
ATOM   153  C CB  . CYS A 1 26  ? 45.239 67.065  -2.371  1.00 32.91 ? 26   CYS A CB  1 
ATOM   154  S SG  . CYS A 1 26  ? 46.428 67.801  -3.561  1.00 36.66 ? 26   CYS A SG  1 
ATOM   155  N N   . ASP A 1 27  ? 42.881 66.380  -4.157  1.00 34.89 ? 27   ASP A N   1 
ATOM   156  C CA  . ASP A 1 27  ? 42.226 66.149  -5.451  1.00 36.10 ? 27   ASP A CA  1 
ATOM   157  C C   . ASP A 1 27  ? 40.915 66.913  -5.520  1.00 36.32 ? 27   ASP A C   1 
ATOM   158  O O   . ASP A 1 27  ? 40.678 67.610  -6.482  1.00 37.06 ? 27   ASP A O   1 
ATOM   159  C CB  . ASP A 1 27  ? 41.964 64.658  -5.704  1.00 36.61 ? 27   ASP A CB  1 
ATOM   160  C CG  . ASP A 1 27  ? 43.230 63.843  -5.815  1.00 38.26 ? 27   ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 27  ? 44.339 64.391  -6.023  1.00 42.17 ? 27   ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 27  ? 43.122 62.612  -5.680  1.00 42.67 ? 27   ASP A OD2 1 
ATOM   163  N N   . GLN A 1 28  ? 40.086 66.809  -4.488  1.00 36.76 ? 28   GLN A N   1 
ATOM   164  C CA  . GLN A 1 28  ? 38.828 67.564  -4.416  1.00 38.27 ? 28   GLN A CA  1 
ATOM   165  C C   . GLN A 1 28  ? 39.012 69.086  -4.565  1.00 36.98 ? 28   GLN A C   1 
ATOM   166  O O   . GLN A 1 28  ? 38.152 69.762  -5.120  1.00 37.14 ? 28   GLN A O   1 
ATOM   167  C CB  . GLN A 1 28  ? 38.052 67.189  -3.135  1.00 38.00 ? 28   GLN A CB  1 
ATOM   168  C CG  . GLN A 1 28  ? 37.123 68.238  -2.549  1.00 40.95 ? 28   GLN A CG  1 
ATOM   169  C CD  . GLN A 1 28  ? 36.935 68.044  -1.017  1.00 43.12 ? 28   GLN A CD  1 
ATOM   170  O OE1 . GLN A 1 28  ? 37.065 69.002  -0.217  1.00 47.31 ? 28   GLN A OE1 1 
ATOM   171  N NE2 . GLN A 1 28  ? 36.659 66.789  -0.606  1.00 47.22 ? 28   GLN A NE2 1 
ATOM   172  N N   . ARG A 1 29  ? 40.141 69.612  -4.088  1.00 36.07 ? 29   ARG A N   1 
ATOM   173  C CA  . ARG A 1 29  ? 40.421 71.046  -4.170  1.00 34.84 ? 29   ARG A CA  1 
ATOM   174  C C   . ARG A 1 29  ? 41.129 71.419  -5.463  1.00 34.65 ? 29   ARG A C   1 
ATOM   175  O O   . ARG A 1 29  ? 41.268 72.591  -5.769  1.00 35.12 ? 29   ARG A O   1 
ATOM   176  C CB  . ARG A 1 29  ? 41.226 71.515  -2.939  1.00 35.29 ? 29   ARG A CB  1 
ATOM   177  C CG  . ARG A 1 29  ? 40.374 71.489  -1.658  1.00 34.43 ? 29   ARG A CG  1 
ATOM   178  C CD  . ARG A 1 29  ? 41.154 71.853  -0.426  1.00 33.56 ? 29   ARG A CD  1 
ATOM   179  N NE  . ARG A 1 29  ? 40.329 71.688  0.774   1.00 29.68 ? 29   ARG A NE  1 
ATOM   180  C CZ  . ARG A 1 29  ? 40.695 72.059  1.996   1.00 30.68 ? 29   ARG A CZ  1 
ATOM   181  N NH1 . ARG A 1 29  ? 41.893 72.634  2.212   1.00 25.53 ? 29   ARG A NH1 1 
ATOM   182  N NH2 . ARG A 1 29  ? 39.870 71.840  3.012   1.00 27.53 ? 29   ARG A NH2 1 
ATOM   183  N N   . GLY A 1 30  ? 41.568 70.418  -6.223  1.00 34.11 ? 30   GLY A N   1 
ATOM   184  C CA  . GLY A 1 30  ? 42.292 70.650  -7.459  1.00 33.10 ? 30   GLY A CA  1 
ATOM   185  C C   . GLY A 1 30  ? 43.706 71.124  -7.233  1.00 32.73 ? 30   GLY A C   1 
ATOM   186  O O   . GLY A 1 30  ? 44.241 71.819  -8.072  1.00 33.17 ? 30   GLY A O   1 
ATOM   187  N N   . CYS A 1 31  ? 44.319 70.756  -6.107  1.00 32.35 ? 31   CYS A N   1 
ATOM   188  C CA  . CYS A 1 31  ? 45.701 71.184  -5.797  1.00 31.77 ? 31   CYS A CA  1 
ATOM   189  C C   . CYS A 1 31  ? 46.687 70.117  -6.167  1.00 31.97 ? 31   CYS A C   1 
ATOM   190  O O   . CYS A 1 31  ? 46.290 69.129  -6.757  1.00 32.92 ? 31   CYS A O   1 
ATOM   191  C CB  . CYS A 1 31  ? 45.852 71.613  -4.329  1.00 31.30 ? 31   CYS A CB  1 
ATOM   192  S SG  . CYS A 1 31  ? 44.870 73.100  -4.030  1.00 30.57 ? 31   CYS A SG  1 
ATOM   193  N N   . CYS A 1 32  ? 47.956 70.312  -5.836  1.00 31.84 ? 32   CYS A N   1 
ATOM   194  C CA  . CYS A 1 32  ? 49.000 69.358  -6.164  1.00 33.41 ? 32   CYS A CA  1 
ATOM   195  C C   . CYS A 1 32  ? 49.395 68.597  -4.936  1.00 33.38 ? 32   CYS A C   1 
ATOM   196  O O   . CYS A 1 32  ? 49.490 69.182  -3.863  1.00 31.95 ? 32   CYS A O   1 
ATOM   197  C CB  . CYS A 1 32  ? 50.270 70.055  -6.642  1.00 33.47 ? 32   CYS A CB  1 
ATOM   198  S SG  . CYS A 1 32  ? 50.027 71.214  -7.956  1.00 38.42 ? 32   CYS A SG  1 
ATOM   199  N N   . TRP A 1 33  ? 49.696 67.312  -5.124  1.00 34.04 ? 33   TRP A N   1 
ATOM   200  C CA  . TRP A 1 33  ? 50.015 66.395  -4.032  1.00 35.44 ? 33   TRP A CA  1 
ATOM   201  C C   . TRP A 1 33  ? 51.452 65.916  -4.161  1.00 36.24 ? 33   TRP A C   1 
ATOM   202  O O   . TRP A 1 33  ? 51.860 65.445  -5.219  1.00 36.32 ? 33   TRP A O   1 
ATOM   203  C CB  . TRP A 1 33  ? 49.055 65.191  -4.054  1.00 34.81 ? 33   TRP A CB  1 
ATOM   204  C CG  . TRP A 1 33  ? 49.276 64.203  -2.944  1.00 35.18 ? 33   TRP A CG  1 
ATOM   205  C CD1 . TRP A 1 33  ? 49.841 62.950  -3.053  1.00 36.04 ? 33   TRP A CD1 1 
ATOM   206  C CD2 . TRP A 1 33  ? 48.943 64.372  -1.558  1.00 34.60 ? 33   TRP A CD2 1 
ATOM   207  N NE1 . TRP A 1 33  ? 49.885 62.345  -1.821  1.00 35.72 ? 33   TRP A NE1 1 
ATOM   208  C CE2 . TRP A 1 33  ? 49.346 63.193  -0.884  1.00 35.25 ? 33   TRP A CE2 1 
ATOM   209  C CE3 . TRP A 1 33  ? 48.353 65.408  -0.817  1.00 34.68 ? 33   TRP A CE3 1 
ATOM   210  C CZ2 . TRP A 1 33  ? 49.167 63.017  0.499   1.00 33.24 ? 33   TRP A CZ2 1 
ATOM   211  C CZ3 . TRP A 1 33  ? 48.185 65.233  0.554   1.00 35.19 ? 33   TRP A CZ3 1 
ATOM   212  C CH2 . TRP A 1 33  ? 48.596 64.043  1.196   1.00 34.12 ? 33   TRP A CH2 1 
ATOM   213  N N   . ASN A 1 34  ? 52.215 66.051  -3.085  1.00 37.93 ? 34   ASN A N   1 
ATOM   214  C CA  . ASN A 1 34  ? 53.555 65.522  -3.019  1.00 39.56 ? 34   ASN A CA  1 
ATOM   215  C C   . ASN A 1 34  ? 53.954 65.282  -1.559  1.00 41.09 ? 34   ASN A C   1 
ATOM   216  O O   . ASN A 1 34  ? 54.618 66.120  -0.939  1.00 40.72 ? 34   ASN A O   1 
ATOM   217  C CB  . ASN A 1 34  ? 54.551 66.453  -3.718  1.00 39.93 ? 34   ASN A CB  1 
ATOM   218  C CG  . ASN A 1 34  ? 55.917 65.805  -3.909  1.00 42.06 ? 34   ASN A CG  1 
ATOM   219  O OD1 . ASN A 1 34  ? 56.426 65.108  -3.024  1.00 43.22 ? 34   ASN A OD1 1 
ATOM   220  N ND2 . ASN A 1 34  ? 56.520 66.038  -5.070  1.00 44.28 ? 34   ASN A ND2 1 
ATOM   221  N N   . PRO A 1 35  ? 53.589 64.107  -1.013  1.00 42.50 ? 35   PRO A N   1 
ATOM   222  C CA  . PRO A 1 35  ? 53.806 63.827  0.397   1.00 43.60 ? 35   PRO A CA  1 
ATOM   223  C C   . PRO A 1 35  ? 55.277 63.701  0.766   1.00 44.60 ? 35   PRO A C   1 
ATOM   224  O O   . PRO A 1 35  ? 55.593 63.351  1.895   1.00 45.38 ? 35   PRO A O   1 
ATOM   225  C CB  . PRO A 1 35  ? 53.078 62.501  0.607   1.00 43.38 ? 35   PRO A CB  1 
ATOM   226  C CG  . PRO A 1 35  ? 53.123 61.861  -0.700  1.00 43.57 ? 35   PRO A CG  1 
ATOM   227  C CD  . PRO A 1 35  ? 52.991 62.958  -1.706  1.00 42.51 ? 35   PRO A CD  1 
ATOM   228  N N   . GLN A 1 36  ? 56.171 64.006  -0.163  1.00 46.26 ? 36   GLN A N   1 
ATOM   229  C CA  . GLN A 1 36  ? 57.596 64.030  0.160   1.00 48.11 ? 36   GLN A CA  1 
ATOM   230  C C   . GLN A 1 36  ? 58.116 65.472  0.409   1.00 48.33 ? 36   GLN A C   1 
ATOM   231  O O   . GLN A 1 36  ? 57.911 66.383  -0.415  1.00 49.05 ? 36   GLN A O   1 
ATOM   232  C CB  . GLN A 1 36  ? 58.429 63.247  -0.886  1.00 48.94 ? 36   GLN A CB  1 
ATOM   233  C CG  . GLN A 1 36  ? 58.701 61.729  -0.512  1.00 52.77 ? 36   GLN A CG  1 
ATOM   234  C CD  . GLN A 1 36  ? 57.688 60.683  -1.090  1.00 57.73 ? 36   GLN A CD  1 
ATOM   235  O OE1 . GLN A 1 36  ? 58.096 59.649  -1.644  1.00 59.88 ? 36   GLN A OE1 1 
ATOM   236  N NE2 . GLN A 1 36  ? 56.386 60.939  -0.936  1.00 59.36 ? 36   GLN A NE2 1 
ATOM   237  N N   . GLY A 1 37  ? 58.762 65.670  1.561   1.00 47.43 ? 37   GLY A N   1 
ATOM   238  C CA  . GLY A 1 37  ? 59.266 66.981  1.956   1.00 46.20 ? 37   GLY A CA  1 
ATOM   239  C C   . GLY A 1 37  ? 59.640 67.013  3.427   1.00 45.63 ? 37   GLY A C   1 
ATOM   240  O O   . GLY A 1 37  ? 59.083 66.255  4.244   1.00 45.46 ? 37   GLY A O   1 
ATOM   241  N N   . ALA A 1 38  ? 60.606 67.875  3.760   1.00 44.61 ? 38   ALA A N   1 
ATOM   242  C CA  . ALA A 1 38  ? 61.023 68.098  5.148   1.00 43.22 ? 38   ALA A CA  1 
ATOM   243  C C   . ALA A 1 38  ? 59.837 68.517  6.052   1.00 41.90 ? 38   ALA A C   1 
ATOM   244  O O   . ALA A 1 38  ? 58.774 68.898  5.566   1.00 42.12 ? 38   ALA A O   1 
ATOM   245  C CB  . ALA A 1 38  ? 62.147 69.157  5.188   1.00 43.60 ? 38   ALA A CB  1 
ATOM   246  N N   . VAL A 1 39  ? 60.023 68.454  7.360   1.00 40.25 ? 39   VAL A N   1 
ATOM   247  C CA  . VAL A 1 39  ? 58.966 68.842  8.291   1.00 39.15 ? 39   VAL A CA  1 
ATOM   248  C C   . VAL A 1 39  ? 58.363 70.232  7.969   1.00 37.37 ? 39   VAL A C   1 
ATOM   249  O O   . VAL A 1 39  ? 59.091 71.181  7.654   1.00 37.74 ? 39   VAL A O   1 
ATOM   250  C CB  . VAL A 1 39  ? 59.444 68.730  9.770   1.00 39.50 ? 39   VAL A CB  1 
ATOM   251  C CG1 . VAL A 1 39  ? 60.384 69.877  10.144  1.00 39.76 ? 39   VAL A CG1 1 
ATOM   252  C CG2 . VAL A 1 39  ? 58.236 68.627  10.734  1.00 40.57 ? 39   VAL A CG2 1 
ATOM   253  N N   . SER A 1 40  ? 57.041 70.331  8.046   1.00 34.70 ? 40   SER A N   1 
ATOM   254  C CA  . SER A 1 40  ? 56.287 71.602  7.798   1.00 32.67 ? 40   SER A CA  1 
ATOM   255  C C   . SER A 1 40  ? 56.063 71.968  6.327   1.00 30.22 ? 40   SER A C   1 
ATOM   256  O O   . SER A 1 40  ? 55.230 72.826  6.018   1.00 29.11 ? 40   SER A O   1 
ATOM   257  C CB  . SER A 1 40  ? 56.899 72.796  8.538   1.00 32.54 ? 40   SER A CB  1 
ATOM   258  O OG  . SER A 1 40  ? 56.823 72.624  9.935   1.00 34.46 ? 40   SER A OG  1 
ATOM   259  N N   . VAL A 1 41  ? 56.787 71.309  5.437   1.00 27.95 ? 41   VAL A N   1 
ATOM   260  C CA  . VAL A 1 41  ? 56.602 71.502  4.013   1.00 27.40 ? 41   VAL A CA  1 
ATOM   261  C C   . VAL A 1 41  ? 55.209 70.938  3.671   1.00 27.45 ? 41   VAL A C   1 
ATOM   262  O O   . VAL A 1 41  ? 54.906 69.789  4.005   1.00 27.38 ? 41   VAL A O   1 
ATOM   263  C CB  . VAL A 1 41  ? 57.750 70.820  3.212   1.00 27.49 ? 41   VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 41  ? 57.550 70.904  1.698   1.00 27.14 ? 41   VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 41  ? 59.096 71.406  3.591   1.00 25.58 ? 41   VAL A CG2 1 
ATOM   266  N N   . PRO A 1 42  ? 54.356 71.754  3.026   1.00 27.40 ? 42   PRO A N   1 
ATOM   267  C CA  . PRO A 1 42  ? 53.009 71.309  2.685   1.00 26.94 ? 42   PRO A CA  1 
ATOM   268  C C   . PRO A 1 42  ? 53.013 70.138  1.692   1.00 27.20 ? 42   PRO A C   1 
ATOM   269  O O   . PRO A 1 42  ? 53.593 70.214  0.601   1.00 27.26 ? 42   PRO A O   1 
ATOM   270  C CB  . PRO A 1 42  ? 52.351 72.540  2.046   1.00 27.05 ? 42   PRO A CB  1 
ATOM   271  C CG  . PRO A 1 42  ? 53.395 73.578  1.886   1.00 26.73 ? 42   PRO A CG  1 
ATOM   272  C CD  . PRO A 1 42  ? 54.654 73.121  2.549   1.00 27.35 ? 42   PRO A CD  1 
ATOM   273  N N   . TRP A 1 43  ? 52.348 69.062  2.080   1.00 27.63 ? 43   TRP A N   1 
ATOM   274  C CA  . TRP A 1 43  ? 52.079 67.930  1.178   1.00 27.87 ? 43   TRP A CA  1 
ATOM   275  C C   . TRP A 1 43  ? 51.162 68.334  0.054   1.00 26.34 ? 43   TRP A C   1 
ATOM   276  O O   . TRP A 1 43  ? 51.226 67.799  -1.040  1.00 25.98 ? 43   TRP A O   1 
ATOM   277  C CB  . TRP A 1 43  ? 51.442 66.792  1.985   1.00 29.21 ? 43   TRP A CB  1 
ATOM   278  C CG  . TRP A 1 43  ? 52.438 66.071  2.823   1.00 31.00 ? 43   TRP A CG  1 
ATOM   279  C CD1 . TRP A 1 43  ? 53.758 66.404  3.003   1.00 31.93 ? 43   TRP A CD1 1 
ATOM   280  C CD2 . TRP A 1 43  ? 52.207 64.886  3.596   1.00 32.96 ? 43   TRP A CD2 1 
ATOM   281  N NE1 . TRP A 1 43  ? 54.362 65.493  3.841   1.00 33.66 ? 43   TRP A NE1 1 
ATOM   282  C CE2 . TRP A 1 43  ? 53.435 64.550  4.216   1.00 33.66 ? 43   TRP A CE2 1 
ATOM   283  C CE3 . TRP A 1 43  ? 51.079 64.072  3.822   1.00 32.88 ? 43   TRP A CE3 1 
ATOM   284  C CZ2 . TRP A 1 43  ? 53.570 63.440  5.060   1.00 33.14 ? 43   TRP A CZ2 1 
ATOM   285  C CZ3 . TRP A 1 43  ? 51.206 62.978  4.660   1.00 32.26 ? 43   TRP A CZ3 1 
ATOM   286  C CH2 . TRP A 1 43  ? 52.452 62.668  5.269   1.00 33.08 ? 43   TRP A CH2 1 
ATOM   287  N N   . CYS A 1 44  ? 50.304 69.299  0.335   1.00 26.78 ? 44   CYS A N   1 
ATOM   288  C CA  . CYS A 1 44  ? 49.312 69.740  -0.630  1.00 26.62 ? 44   CYS A CA  1 
ATOM   289  C C   . CYS A 1 44  ? 49.381 71.257  -0.845  1.00 26.93 ? 44   CYS A C   1 
ATOM   290  O O   . CYS A 1 44  ? 49.276 72.036  0.112   1.00 26.23 ? 44   CYS A O   1 
ATOM   291  C CB  . CYS A 1 44  ? 47.919 69.302  -0.203  1.00 25.28 ? 44   CYS A CB  1 
ATOM   292  S SG  . CYS A 1 44  ? 46.672 69.929  -1.338  1.00 27.06 ? 44   CYS A SG  1 
ATOM   293  N N   . TYR A 1 45  ? 49.543 71.657  -2.108  1.00 28.27 ? 45   TYR A N   1 
ATOM   294  C CA  . TYR A 1 45  ? 49.891 73.044  -2.463  1.00 29.71 ? 45   TYR A CA  1 
ATOM   295  C C   . TYR A 1 45  ? 49.232 73.490  -3.745  1.00 30.33 ? 45   TYR A C   1 
ATOM   296  O O   . TYR A 1 45  ? 48.852 72.657  -4.568  1.00 30.10 ? 45   TYR A O   1 
ATOM   297  C CB  . TYR A 1 45  ? 51.407 73.252  -2.539  1.00 30.31 ? 45   TYR A CB  1 
ATOM   298  C CG  . TYR A 1 45  ? 52.179 72.364  -3.478  1.00 31.64 ? 45   TYR A CG  1 
ATOM   299  C CD1 . TYR A 1 45  ? 52.502 72.790  -4.766  1.00 32.95 ? 45   TYR A CD1 1 
ATOM   300  C CD2 . TYR A 1 45  ? 52.649 71.117  -3.061  1.00 32.35 ? 45   TYR A CD2 1 
ATOM   301  C CE1 . TYR A 1 45  ? 53.232 71.982  -5.626  1.00 31.97 ? 45   TYR A CE1 1 
ATOM   302  C CE2 . TYR A 1 45  ? 53.392 70.301  -3.915  1.00 32.59 ? 45   TYR A CE2 1 
ATOM   303  C CZ  . TYR A 1 45  ? 53.677 70.733  -5.196  1.00 32.39 ? 45   TYR A CZ  1 
ATOM   304  O OH  . TYR A 1 45  ? 54.416 69.911  -6.041  1.00 32.64 ? 45   TYR A OH  1 
ATOM   305  N N   . TYR A 1 46  ? 49.065 74.796  -3.908  1.00 30.74 ? 46   TYR A N   1 
ATOM   306  C CA  . TYR A 1 46  ? 48.383 75.321  -5.075  1.00 33.45 ? 46   TYR A CA  1 
ATOM   307  C C   . TYR A 1 46  ? 49.258 75.116  -6.319  1.00 35.59 ? 46   TYR A C   1 
ATOM   308  O O   . TYR A 1 46  ? 50.488 75.189  -6.230  1.00 35.82 ? 46   TYR A O   1 
ATOM   309  C CB  . TYR A 1 46  ? 48.007 76.787  -4.868  1.00 32.14 ? 46   TYR A CB  1 
ATOM   310  C CG  . TYR A 1 46  ? 47.014 77.010  -3.754  1.00 29.60 ? 46   TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 46  ? 45.652 76.771  -3.942  1.00 28.91 ? 46   TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 46  ? 47.434 77.475  -2.503  1.00 28.82 ? 46   TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 46  ? 44.732 76.980  -2.898  1.00 27.60 ? 46   TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 46  ? 46.523 77.711  -1.465  1.00 26.21 ? 46   TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 46  ? 45.181 77.444  -1.671  1.00 28.43 ? 46   TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 46  ? 44.285 77.673  -0.638  1.00 30.15 ? 46   TYR A OH  1 
ATOM   317  N N   . SER A 1 47  ? 48.631 74.792  -7.447  1.00 39.22 ? 47   SER A N   1 
ATOM   318  C CA  . SER A 1 47  ? 49.363 74.601  -8.726  1.00 43.39 ? 47   SER A CA  1 
ATOM   319  C C   . SER A 1 47  ? 49.945 75.898  -9.274  1.00 45.77 ? 47   SER A C   1 
ATOM   320  O O   . SER A 1 47  ? 49.495 76.988  -8.879  1.00 46.48 ? 47   SER A O   1 
ATOM   321  C CB  . SER A 1 47  ? 48.451 73.990  -9.795  1.00 42.85 ? 47   SER A CB  1 
ATOM   322  O OG  . SER A 1 47  ? 47.134 74.502  -9.689  1.00 44.60 ? 47   SER A OG  1 
ATOM   323  N N   . LYS A 1 48  ? 50.933 75.778  -10.178 1.00 48.67 ? 48   LYS A N   1 
ATOM   324  C CA  . LYS A 1 48  ? 51.450 76.915  -10.991 1.00 50.80 ? 48   LYS A CA  1 
ATOM   325  C C   . LYS A 1 48  ? 50.277 77.757  -11.503 1.00 51.44 ? 48   LYS A C   1 
ATOM   326  O O   . LYS A 1 48  ? 50.186 78.954  -11.209 1.00 52.15 ? 48   LYS A O   1 
ATOM   327  C CB  . LYS A 1 48  ? 52.275 76.422  -12.202 1.00 51.21 ? 48   LYS A CB  1 
ATOM   328  C CG  . LYS A 1 48  ? 53.696 75.850  -11.920 1.00 53.64 ? 48   LYS A CG  1 
ATOM   329  C CD  . LYS A 1 48  ? 54.830 76.772  -12.456 1.00 55.94 ? 48   LYS A CD  1 
ATOM   330  C CE  . LYS A 1 48  ? 54.906 76.791  -14.005 1.00 56.71 ? 48   LYS A CE  1 
ATOM   331  N NZ  . LYS A 1 48  ? 55.706 77.945  -14.563 1.00 55.75 ? 48   LYS A NZ  1 
ATOM   332  N N   . ASN A 1 49  ? 49.373 77.123  -12.248 1.00 51.94 ? 49   ASN A N   1 
ATOM   333  C CA  . ASN A 1 49  ? 48.217 77.814  -12.797 1.00 52.77 ? 49   ASN A CA  1 
ATOM   334  C C   . ASN A 1 49  ? 46.964 77.605  -11.959 1.00 52.65 ? 49   ASN A C   1 
ATOM   335  O O   . ASN A 1 49  ? 47.024 76.948  -10.917 1.00 53.69 ? 49   ASN A O   1 
ATOM   336  C CB  . ASN A 1 49  ? 48.011 77.482  -14.292 1.00 53.39 ? 49   ASN A CB  1 
ATOM   337  C CG  . ASN A 1 49  ? 48.712 78.500  -15.235 1.00 54.23 ? 49   ASN A CG  1 
ATOM   338  O OD1 . ASN A 1 49  ? 48.064 79.400  -15.786 1.00 55.54 ? 49   ASN A OD1 1 
ATOM   339  N ND2 . ASN A 1 49  ? 50.035 78.362  -15.402 1.00 53.93 ? 49   ASN A ND2 1 
ATOM   340  N N   . HIS A 1 50  ? 45.839 78.153  -12.426 1.00 52.28 ? 50   HIS A N   1 
ATOM   341  C CA  . HIS A 1 50  ? 44.612 78.378  -11.631 1.00 51.28 ? 50   HIS A CA  1 
ATOM   342  C C   . HIS A 1 50  ? 44.821 79.618  -10.771 1.00 49.47 ? 50   HIS A C   1 
ATOM   343  O O   . HIS A 1 50  ? 45.974 79.956  -10.468 1.00 50.42 ? 50   HIS A O   1 
ATOM   344  C CB  . HIS A 1 50  ? 44.211 77.192  -10.741 1.00 51.91 ? 50   HIS A CB  1 
ATOM   345  C CG  . HIS A 1 50  ? 43.673 77.607  -9.396  1.00 54.85 ? 50   HIS A CG  1 
ATOM   346  N ND1 . HIS A 1 50  ? 44.356 77.386  -8.213  1.00 57.54 ? 50   HIS A ND1 1 
ATOM   347  C CD2 . HIS A 1 50  ? 42.524 78.245  -9.049  1.00 57.08 ? 50   HIS A CD2 1 
ATOM   348  C CE1 . HIS A 1 50  ? 43.645 77.852  -7.198  1.00 57.39 ? 50   HIS A CE1 1 
ATOM   349  N NE2 . HIS A 1 50  ? 42.537 78.392  -7.678  1.00 58.53 ? 50   HIS A NE2 1 
ATOM   350  N N   . SER A 1 51  ? 43.710 80.256  -10.369 1.00 46.31 ? 51   SER A N   1 
ATOM   351  C CA  . SER A 1 51  ? 43.681 81.500  -9.589  1.00 43.62 ? 51   SER A CA  1 
ATOM   352  C C   . SER A 1 51  ? 42.745 82.467  -10.345 1.00 41.14 ? 51   SER A C   1 
ATOM   353  O O   . SER A 1 51  ? 41.597 82.111  -10.648 1.00 41.78 ? 51   SER A O   1 
ATOM   354  C CB  . SER A 1 51  ? 45.108 82.095  -9.411  1.00 43.83 ? 51   SER A CB  1 
ATOM   355  O OG  . SER A 1 51  ? 45.112 83.392  -8.825  1.00 43.20 ? 51   SER A OG  1 
ATOM   356  N N   . TYR A 1 52  ? 43.247 83.667  -10.641 1.00 37.01 ? 52   TYR A N   1 
ATOM   357  C CA  . TYR A 1 52  ? 42.594 84.653  -11.486 1.00 33.08 ? 52   TYR A CA  1 
ATOM   358  C C   . TYR A 1 52  ? 43.500 84.947  -12.688 1.00 31.58 ? 52   TYR A C   1 
ATOM   359  O O   . TYR A 1 52  ? 44.695 84.719  -12.635 1.00 29.53 ? 52   TYR A O   1 
ATOM   360  C CB  . TYR A 1 52  ? 42.380 85.930  -10.692 1.00 32.32 ? 52   TYR A CB  1 
ATOM   361  C CG  . TYR A 1 52  ? 41.252 85.855  -9.696  1.00 31.17 ? 52   TYR A CG  1 
ATOM   362  C CD1 . TYR A 1 52  ? 41.425 85.237  -8.456  1.00 29.82 ? 52   TYR A CD1 1 
ATOM   363  C CD2 . TYR A 1 52  ? 40.025 86.414  -9.991  1.00 29.31 ? 52   TYR A CD2 1 
ATOM   364  C CE1 . TYR A 1 52  ? 40.381 85.166  -7.537  1.00 30.97 ? 52   TYR A CE1 1 
ATOM   365  C CE2 . TYR A 1 52  ? 38.975 86.361  -9.087  1.00 31.04 ? 52   TYR A CE2 1 
ATOM   366  C CZ  . TYR A 1 52  ? 39.168 85.729  -7.862  1.00 31.24 ? 52   TYR A CZ  1 
ATOM   367  O OH  . TYR A 1 52  ? 38.136 85.682  -6.985  1.00 30.83 ? 52   TYR A OH  1 
ATOM   368  N N   . HIS A 1 53  ? 42.926 85.433  -13.778 1.00 30.51 ? 53   HIS A N   1 
ATOM   369  C CA  . HIS A 1 53  ? 43.731 85.911  -14.903 1.00 30.12 ? 53   HIS A CA  1 
ATOM   370  C C   . HIS A 1 53  ? 43.314 87.338  -15.180 1.00 29.16 ? 53   HIS A C   1 
ATOM   371  O O   . HIS A 1 53  ? 42.201 87.734  -14.839 1.00 28.42 ? 53   HIS A O   1 
ATOM   372  C CB  . HIS A 1 53  ? 43.551 85.028  -16.166 1.00 30.17 ? 53   HIS A CB  1 
ATOM   373  C CG  . HIS A 1 53  ? 42.168 85.062  -16.750 1.00 33.21 ? 53   HIS A CG  1 
ATOM   374  N ND1 . HIS A 1 53  ? 41.747 86.047  -17.620 1.00 35.14 ? 53   HIS A ND1 1 
ATOM   375  C CD2 . HIS A 1 53  ? 41.112 84.222  -16.600 1.00 34.27 ? 53   HIS A CD2 1 
ATOM   376  C CE1 . HIS A 1 53  ? 40.493 85.817  -17.974 1.00 35.62 ? 53   HIS A CE1 1 
ATOM   377  N NE2 . HIS A 1 53  ? 40.084 84.715  -17.370 1.00 34.60 ? 53   HIS A NE2 1 
ATOM   378  N N   . VAL A 1 54  ? 44.184 88.120  -15.818 1.00 28.50 ? 54   VAL A N   1 
ATOM   379  C CA  . VAL A 1 54  ? 43.766 89.458  -16.212 1.00 28.35 ? 54   VAL A CA  1 
ATOM   380  C C   . VAL A 1 54  ? 42.879 89.362  -17.439 1.00 28.42 ? 54   VAL A C   1 
ATOM   381  O O   . VAL A 1 54  ? 43.233 88.688  -18.400 1.00 28.66 ? 54   VAL A O   1 
ATOM   382  C CB  . VAL A 1 54  ? 44.961 90.413  -16.474 1.00 27.94 ? 54   VAL A CB  1 
ATOM   383  C CG1 . VAL A 1 54  ? 44.442 91.818  -16.859 1.00 26.23 ? 54   VAL A CG1 1 
ATOM   384  C CG2 . VAL A 1 54  ? 45.848 90.471  -15.245 1.00 26.66 ? 54   VAL A CG2 1 
ATOM   385  N N   . GLU A 1 55  ? 41.747 90.047  -17.402 1.00 28.98 ? 55   GLU A N   1 
ATOM   386  C CA  . GLU A 1 55  ? 40.854 90.100  -18.548 1.00 30.61 ? 55   GLU A CA  1 
ATOM   387  C C   . GLU A 1 55  ? 41.019 91.412  -19.346 1.00 29.74 ? 55   GLU A C   1 
ATOM   388  O O   . GLU A 1 55  ? 40.788 92.498  -18.825 1.00 29.36 ? 55   GLU A O   1 
ATOM   389  C CB  . GLU A 1 55  ? 39.389 89.889  -18.111 1.00 30.67 ? 55   GLU A CB  1 
ATOM   390  C CG  . GLU A 1 55  ? 38.374 89.936  -19.277 1.00 36.46 ? 55   GLU A CG  1 
ATOM   391  C CD  . GLU A 1 55  ? 38.155 88.586  -20.013 1.00 44.33 ? 55   GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 55  ? 39.076 87.721  -20.089 1.00 45.92 ? 55   GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 55  ? 37.027 88.394  -20.544 1.00 48.66 ? 55   GLU A OE2 1 
ATOM   394  N N   . GLY A 1 56  ? 41.385 91.298  -20.621 1.00 29.97 ? 56   GLY A N   1 
ATOM   395  C CA  . GLY A 1 56  ? 41.601 92.489  -21.465 1.00 29.46 ? 56   GLY A CA  1 
ATOM   396  C C   . GLY A 1 56  ? 42.789 93.311  -20.962 1.00 28.93 ? 56   GLY A C   1 
ATOM   397  O O   . GLY A 1 56  ? 43.701 92.747  -20.357 1.00 28.00 ? 56   GLY A O   1 
ATOM   398  N N   . ASN A 1 57  ? 42.764 94.631  -21.191 1.00 28.34 ? 57   ASN A N   1 
ATOM   399  C CA  . ASN A 1 57  ? 43.920 95.489  -20.903 1.00 28.23 ? 57   ASN A CA  1 
ATOM   400  C C   . ASN A 1 57  ? 43.780 96.232  -19.577 1.00 28.76 ? 57   ASN A C   1 
ATOM   401  O O   . ASN A 1 57  ? 42.656 96.458  -19.075 1.00 29.47 ? 57   ASN A O   1 
ATOM   402  C CB  . ASN A 1 57  ? 44.158 96.536  -22.023 1.00 27.48 ? 57   ASN A CB  1 
ATOM   403  C CG  . ASN A 1 57  ? 44.431 95.919  -23.395 1.00 27.45 ? 57   ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 57  ? 44.906 94.788  -23.523 1.00 25.05 ? 57   ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 57  ? 44.145 96.682  -24.430 1.00 27.33 ? 57   ASN A ND2 1 
ATOM   406  N N   . LEU A 1 58  ? 44.926 96.671  -19.055 1.00 28.27 ? 58   LEU A N   1 
ATOM   407  C CA  . LEU A 1 58  ? 44.967 97.666  -17.982 1.00 27.15 ? 58   LEU A CA  1 
ATOM   408  C C   . LEU A 1 58  ? 44.549 99.025  -18.518 1.00 26.38 ? 58   LEU A C   1 
ATOM   409  O O   . LEU A 1 58  ? 44.752 99.326  -19.699 1.00 25.74 ? 58   LEU A O   1 
ATOM   410  C CB  . LEU A 1 58  ? 46.356 97.741  -17.334 1.00 26.87 ? 58   LEU A CB  1 
ATOM   411  C CG  . LEU A 1 58  ? 46.710 96.628  -16.345 1.00 27.47 ? 58   LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 58  ? 46.608 95.186  -16.921 1.00 27.58 ? 58   LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 58  ? 48.080 96.867  -15.790 1.00 23.87 ? 58   LEU A CD2 1 
ATOM   414  N N   . VAL A 1 59  ? 43.943 99.816  -17.637 1.00 25.68 ? 59   VAL A N   1 
ATOM   415  C CA  . VAL A 1 59  ? 43.395 101.139 -17.938 1.00 25.59 ? 59   VAL A CA  1 
ATOM   416  C C   . VAL A 1 59  ? 44.188 102.139 -17.126 1.00 25.49 ? 59   VAL A C   1 
ATOM   417  O O   . VAL A 1 59  ? 44.171 102.062 -15.911 1.00 24.05 ? 59   VAL A O   1 
ATOM   418  C CB  . VAL A 1 59  ? 41.891 101.226 -17.524 1.00 25.36 ? 59   VAL A CB  1 
ATOM   419  C CG1 . VAL A 1 59  ? 41.300 102.653 -17.705 1.00 25.97 ? 59   VAL A CG1 1 
ATOM   420  C CG2 . VAL A 1 59  ? 41.053 100.170 -18.325 1.00 26.92 ? 59   VAL A CG2 1 
ATOM   421  N N   . ASN A 1 60  ? 44.883 103.066 -17.794 1.00 25.47 ? 60   ASN A N   1 
ATOM   422  C CA  . ASN A 1 60  ? 45.472 104.217 -17.107 1.00 26.77 ? 60   ASN A CA  1 
ATOM   423  C C   . ASN A 1 60  ? 44.435 105.102 -16.474 1.00 27.01 ? 60   ASN A C   1 
ATOM   424  O O   . ASN A 1 60  ? 43.423 105.440 -17.099 1.00 27.62 ? 60   ASN A O   1 
ATOM   425  C CB  . ASN A 1 60  ? 46.269 105.103 -18.062 1.00 27.54 ? 60   ASN A CB  1 
ATOM   426  C CG  . ASN A 1 60  ? 47.597 104.514 -18.411 1.00 30.89 ? 60   ASN A CG  1 
ATOM   427  O OD1 . ASN A 1 60  ? 48.600 104.735 -17.709 1.00 34.91 ? 60   ASN A OD1 1 
ATOM   428  N ND2 . ASN A 1 60  ? 47.632 103.758 -19.506 1.00 30.63 ? 60   ASN A ND2 1 
ATOM   429  N N   . THR A 1 61  ? 44.698 105.491 -15.238 1.00 26.42 ? 61   THR A N   1 
ATOM   430  C CA  . THR A 1 61  ? 43.878 106.441 -14.533 1.00 27.11 ? 61   THR A CA  1 
ATOM   431  C C   . THR A 1 61  ? 44.840 107.565 -14.111 1.00 27.94 ? 61   THR A C   1 
ATOM   432  O O   . THR A 1 61  ? 46.072 107.454 -14.291 1.00 27.21 ? 61   THR A O   1 
ATOM   433  C CB  . THR A 1 61  ? 43.237 105.812 -13.273 1.00 27.39 ? 61   THR A CB  1 
ATOM   434  O OG1 . THR A 1 61  ? 44.279 105.328 -12.447 1.00 26.70 ? 61   THR A OG1 1 
ATOM   435  C CG2 . THR A 1 61  ? 42.309 104.605 -13.613 1.00 26.08 ? 61   THR A CG2 1 
ATOM   436  N N   . ASN A 1 62  ? 44.269 108.644 -13.579 1.00 28.83 ? 62   ASN A N   1 
ATOM   437  C CA  . ASN A 1 62  ? 45.053 109.751 -13.041 1.00 29.25 ? 62   ASN A CA  1 
ATOM   438  C C   . ASN A 1 62  ? 46.008 109.307 -11.940 1.00 28.25 ? 62   ASN A C   1 
ATOM   439  O O   . ASN A 1 62  ? 47.161 109.712 -11.960 1.00 29.07 ? 62   ASN A O   1 
ATOM   440  C CB  . ASN A 1 62  ? 44.141 110.876 -12.552 1.00 29.85 ? 62   ASN A CB  1 
ATOM   441  C CG  . ASN A 1 62  ? 43.436 111.596 -13.690 1.00 32.43 ? 62   ASN A CG  1 
ATOM   442  O OD1 . ASN A 1 62  ? 42.370 112.162 -13.489 1.00 35.03 ? 62   ASN A OD1 1 
ATOM   443  N ND2 . ASN A 1 62  ? 44.034 111.590 -14.890 1.00 34.25 ? 62   ASN A ND2 1 
ATOM   444  N N   . ALA A 1 63  ? 45.544 108.453 -11.023 1.00 26.80 ? 63   ALA A N   1 
ATOM   445  C CA  . ALA A 1 63  ? 46.344 107.957 -9.891  1.00 25.35 ? 63   ALA A CA  1 
ATOM   446  C C   . ALA A 1 63  ? 47.301 106.815 -10.242 1.00 25.35 ? 63   ALA A C   1 
ATOM   447  O O   . ALA A 1 63  ? 48.333 106.641 -9.578  1.00 25.22 ? 63   ALA A O   1 
ATOM   448  C CB  . ALA A 1 63  ? 45.421 107.506 -8.747  1.00 26.40 ? 63   ALA A CB  1 
ATOM   449  N N   . GLY A 1 64  ? 46.973 106.034 -11.269 1.00 24.22 ? 64   GLY A N   1 
ATOM   450  C CA  . GLY A 1 64  ? 47.774 104.853 -11.629 1.00 23.91 ? 64   GLY A CA  1 
ATOM   451  C C   . GLY A 1 64  ? 47.084 104.009 -12.713 1.00 24.17 ? 64   GLY A C   1 
ATOM   452  O O   . GLY A 1 64  ? 47.140 104.356 -13.908 1.00 23.42 ? 64   GLY A O   1 
ATOM   453  N N   . PHE A 1 65  ? 46.465 102.900 -12.316 1.00 22.71 ? 65   PHE A N   1 
ATOM   454  C CA  . PHE A 1 65  ? 45.789 102.021 -13.277 1.00 23.24 ? 65   PHE A CA  1 
ATOM   455  C C   . PHE A 1 65  ? 44.791 101.078 -12.596 1.00 23.37 ? 65   PHE A C   1 
ATOM   456  O O   . PHE A 1 65  ? 44.861 100.847 -11.401 1.00 22.66 ? 65   PHE A O   1 
ATOM   457  C CB  . PHE A 1 65  ? 46.792 101.201 -14.110 1.00 23.50 ? 65   PHE A CB  1 
ATOM   458  C CG  . PHE A 1 65  ? 47.621 100.208 -13.287 1.00 24.73 ? 65   PHE A CG  1 
ATOM   459  C CD1 . PHE A 1 65  ? 47.135 98.939  -13.003 1.00 24.94 ? 65   PHE A CD1 1 
ATOM   460  C CD2 . PHE A 1 65  ? 48.897 100.550 -12.837 1.00 25.34 ? 65   PHE A CD2 1 
ATOM   461  C CE1 . PHE A 1 65  ? 47.884 98.031  -12.272 1.00 25.00 ? 65   PHE A CE1 1 
ATOM   462  C CE2 . PHE A 1 65  ? 49.653 99.661  -12.110 1.00 25.42 ? 65   PHE A CE2 1 
ATOM   463  C CZ  . PHE A 1 65  ? 49.137 98.396  -11.815 1.00 26.30 ? 65   PHE A CZ  1 
ATOM   464  N N   . THR A 1 66  ? 43.848 100.557 -13.378 1.00 24.05 ? 66   THR A N   1 
ATOM   465  C CA  . THR A 1 66  ? 42.910 99.515  -12.920 1.00 24.00 ? 66   THR A CA  1 
ATOM   466  C C   . THR A 1 66  ? 43.064 98.308  -13.841 1.00 24.23 ? 66   THR A C   1 
ATOM   467  O O   . THR A 1 66  ? 43.544 98.448  -14.981 1.00 24.27 ? 66   THR A O   1 
ATOM   468  C CB  . THR A 1 66  ? 41.430 100.021 -12.897 1.00 24.90 ? 66   THR A CB  1 
ATOM   469  O OG1 . THR A 1 66  ? 41.048 100.479 -14.203 1.00 25.38 ? 66   THR A OG1 1 
ATOM   470  C CG2 . THR A 1 66  ? 41.259 101.155 -11.889 1.00 23.94 ? 66   THR A CG2 1 
ATOM   471  N N   . ALA A 1 67  ? 42.718 97.122  -13.345 1.00 23.96 ? 67   ALA A N   1 
ATOM   472  C CA  . ALA A 1 67  ? 42.641 95.907  -14.144 1.00 24.96 ? 67   ALA A CA  1 
ATOM   473  C C   . ALA A 1 67  ? 41.429 95.106  -13.671 1.00 26.37 ? 67   ALA A C   1 
ATOM   474  O O   . ALA A 1 67  ? 41.105 95.124  -12.489 1.00 27.09 ? 67   ALA A O   1 
ATOM   475  C CB  . ALA A 1 67  ? 43.887 95.068  -13.987 1.00 24.36 ? 67   ALA A CB  1 
ATOM   476  N N   . ARG A 1 68  ? 40.777 94.406  -14.591 1.00 27.58 ? 68   ARG A N   1 
ATOM   477  C CA  . ARG A 1 68  ? 39.718 93.455  -14.255 1.00 29.24 ? 68   ARG A CA  1 
ATOM   478  C C   . ARG A 1 68  ? 40.338 92.077  -14.221 1.00 28.78 ? 68   ARG A C   1 
ATOM   479  O O   . ARG A 1 68  ? 41.062 91.682  -15.161 1.00 28.43 ? 68   ARG A O   1 
ATOM   480  C CB  . ARG A 1 68  ? 38.584 93.555  -15.276 1.00 30.65 ? 68   ARG A CB  1 
ATOM   481  C CG  . ARG A 1 68  ? 37.941 94.944  -15.267 1.00 35.56 ? 68   ARG A CG  1 
ATOM   482  C CD  . ARG A 1 68  ? 37.290 95.338  -16.610 1.00 46.18 ? 68   ARG A CD  1 
ATOM   483  N NE  . ARG A 1 68  ? 35.867 94.962  -16.683 1.00 53.62 ? 68   ARG A NE  1 
ATOM   484  C CZ  . ARG A 1 68  ? 34.838 95.785  -16.434 1.00 58.06 ? 68   ARG A CZ  1 
ATOM   485  N NH1 . ARG A 1 68  ? 35.054 97.058  -16.091 1.00 58.58 ? 68   ARG A NH1 1 
ATOM   486  N NH2 . ARG A 1 68  ? 33.577 95.333  -16.519 1.00 59.25 ? 68   ARG A NH2 1 
ATOM   487  N N   . LEU A 1 69  ? 40.140 91.377  -13.107 1.00 27.96 ? 69   LEU A N   1 
ATOM   488  C CA  . LEU A 1 69  ? 40.614 90.000  -12.974 1.00 28.82 ? 69   LEU A CA  1 
ATOM   489  C C   . LEU A 1 69  ? 39.388 89.086  -12.980 1.00 30.61 ? 69   LEU A C   1 
ATOM   490  O O   . LEU A 1 69  ? 38.362 89.428  -12.391 1.00 30.40 ? 69   LEU A O   1 
ATOM   491  C CB  . LEU A 1 69  ? 41.439 89.797  -11.694 1.00 28.07 ? 69   LEU A CB  1 
ATOM   492  C CG  . LEU A 1 69  ? 42.478 90.823  -11.196 1.00 26.96 ? 69   LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 69  ? 43.289 90.186  -10.086 1.00 25.45 ? 69   LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 69  ? 43.379 91.310  -12.283 1.00 19.05 ? 69   LEU A CD2 1 
ATOM   495  N N   . LYS A 1 70  ? 39.486 87.957  -13.675 1.00 32.65 ? 70   LYS A N   1 
ATOM   496  C CA  . LYS A 1 70  ? 38.350 87.059  -13.836 1.00 34.95 ? 70   LYS A CA  1 
ATOM   497  C C   . LYS A 1 70  ? 38.767 85.717  -13.277 1.00 36.16 ? 70   LYS A C   1 
ATOM   498  O O   . LYS A 1 70  ? 39.876 85.252  -13.550 1.00 34.82 ? 70   LYS A O   1 
ATOM   499  C CB  . LYS A 1 70  ? 37.966 86.947  -15.309 1.00 35.17 ? 70   LYS A CB  1 
ATOM   500  C CG  . LYS A 1 70  ? 36.629 86.266  -15.598 1.00 38.93 ? 70   LYS A CG  1 
ATOM   501  C CD  . LYS A 1 70  ? 36.079 86.755  -16.967 1.00 43.46 ? 70   LYS A CD  1 
ATOM   502  C CE  . LYS A 1 70  ? 35.146 85.733  -17.659 1.00 44.20 ? 70   LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 70  ? 34.842 86.111  -19.080 1.00 41.85 ? 70   LYS A NZ  1 
ATOM   504  N N   . ASN A 1 71  ? 37.885 85.108  -12.485 1.00 37.97 ? 71   ASN A N   1 
ATOM   505  C CA  . ASN A 1 71  ? 38.194 83.848  -11.797 1.00 41.27 ? 71   ASN A CA  1 
ATOM   506  C C   . ASN A 1 71  ? 38.338 82.632  -12.725 1.00 43.31 ? 71   ASN A C   1 
ATOM   507  O O   . ASN A 1 71  ? 37.440 82.326  -13.495 1.00 43.46 ? 71   ASN A O   1 
ATOM   508  C CB  . ASN A 1 71  ? 37.132 83.585  -10.713 1.00 41.25 ? 71   ASN A CB  1 
ATOM   509  C CG  . ASN A 1 71  ? 37.437 82.371  -9.848  1.00 42.90 ? 71   ASN A CG  1 
ATOM   510  O OD1 . ASN A 1 71  ? 38.595 82.113  -9.464  1.00 44.45 ? 71   ASN A OD1 1 
ATOM   511  N ND2 . ASN A 1 71  ? 36.380 81.618  -9.509  1.00 44.93 ? 71   ASN A ND2 1 
ATOM   512  N N   . LEU A 1 72  ? 39.473 81.944  -12.643 1.00 46.75 ? 72   LEU A N   1 
ATOM   513  C CA  . LEU A 1 72  ? 39.653 80.648  -13.328 1.00 50.13 ? 72   LEU A CA  1 
ATOM   514  C C   . LEU A 1 72  ? 38.926 79.534  -12.535 1.00 52.32 ? 72   LEU A C   1 
ATOM   515  O O   . LEU A 1 72  ? 39.400 79.132  -11.464 1.00 52.88 ? 72   LEU A O   1 
ATOM   516  C CB  . LEU A 1 72  ? 41.150 80.301  -13.459 1.00 50.09 ? 72   LEU A CB  1 
ATOM   517  C CG  . LEU A 1 72  ? 42.116 80.767  -14.573 1.00 50.60 ? 72   LEU A CG  1 
ATOM   518  C CD1 . LEU A 1 72  ? 41.518 80.712  -15.997 1.00 51.48 ? 72   LEU A CD1 1 
ATOM   519  C CD2 . LEU A 1 72  ? 42.689 82.109  -14.283 1.00 48.59 ? 72   LEU A CD2 1 
ATOM   520  N N   . PRO A 1 73  ? 37.777 79.031  -13.053 1.00 54.35 ? 73   PRO A N   1 
ATOM   521  C CA  . PRO A 1 73  ? 36.855 78.240  -12.210 1.00 55.28 ? 73   PRO A CA  1 
ATOM   522  C C   . PRO A 1 73  ? 37.477 77.015  -11.554 1.00 55.95 ? 73   PRO A C   1 
ATOM   523  O O   . PRO A 1 73  ? 38.385 76.391  -12.109 1.00 56.37 ? 73   PRO A O   1 
ATOM   524  C CB  . PRO A 1 73  ? 35.734 77.840  -13.184 1.00 55.40 ? 73   PRO A CB  1 
ATOM   525  C CG  . PRO A 1 73  ? 35.762 78.928  -14.229 1.00 55.29 ? 73   PRO A CG  1 
ATOM   526  C CD  . PRO A 1 73  ? 37.250 79.170  -14.428 1.00 54.83 ? 73   PRO A CD  1 
ATOM   527  N N   . SER A 1 74  ? 36.995 76.732  -10.349 1.00 56.66 ? 74   SER A N   1 
ATOM   528  C CA  . SER A 1 74  ? 37.411 75.604  -9.522  1.00 57.46 ? 74   SER A CA  1 
ATOM   529  C C   . SER A 1 74  ? 36.280 75.430  -8.526  1.00 57.60 ? 74   SER A C   1 
ATOM   530  O O   . SER A 1 74  ? 35.388 76.289  -8.439  1.00 57.88 ? 74   SER A O   1 
ATOM   531  C CB  . SER A 1 74  ? 38.723 75.882  -8.766  1.00 57.79 ? 74   SER A CB  1 
ATOM   532  O OG  . SER A 1 74  ? 39.875 75.784  -9.595  1.00 58.03 ? 74   SER A OG  1 
ATOM   533  N N   . SER A 1 75  ? 36.296 74.317  -7.792  1.00 57.49 ? 75   SER A N   1 
ATOM   534  C CA  . SER A 1 75  ? 35.239 74.047  -6.809  1.00 56.96 ? 75   SER A CA  1 
ATOM   535  C C   . SER A 1 75  ? 35.580 74.836  -5.539  1.00 56.07 ? 75   SER A C   1 
ATOM   536  O O   . SER A 1 75  ? 36.768 75.045  -5.242  1.00 56.28 ? 75   SER A O   1 
ATOM   537  C CB  . SER A 1 75  ? 35.073 72.530  -6.537  1.00 57.27 ? 75   SER A CB  1 
ATOM   538  O OG  . SER A 1 75  ? 34.543 71.826  -7.671  1.00 57.81 ? 75   SER A OG  1 
ATOM   539  N N   . PRO A 1 76  ? 34.547 75.337  -4.828  1.00 55.17 ? 76   PRO A N   1 
ATOM   540  C CA  . PRO A 1 76  ? 34.754 76.089  -3.592  1.00 54.26 ? 76   PRO A CA  1 
ATOM   541  C C   . PRO A 1 76  ? 35.561 75.313  -2.555  1.00 53.12 ? 76   PRO A C   1 
ATOM   542  O O   . PRO A 1 76  ? 35.290 74.130  -2.317  1.00 53.25 ? 76   PRO A O   1 
ATOM   543  C CB  . PRO A 1 76  ? 33.324 76.323  -3.092  1.00 54.36 ? 76   PRO A CB  1 
ATOM   544  C CG  . PRO A 1 76  ? 32.524 76.368  -4.337  1.00 54.89 ? 76   PRO A CG  1 
ATOM   545  C CD  . PRO A 1 76  ? 33.117 75.274  -5.169  1.00 55.02 ? 76   PRO A CD  1 
ATOM   546  N N   . VAL A 1 77  ? 36.569 75.975  -1.983  1.00 51.49 ? 77   VAL A N   1 
ATOM   547  C CA  . VAL A 1 77  ? 37.287 75.463  -0.820  1.00 49.32 ? 77   VAL A CA  1 
ATOM   548  C C   . VAL A 1 77  ? 36.525 75.974  0.416   1.00 47.53 ? 77   VAL A C   1 
ATOM   549  O O   . VAL A 1 77  ? 35.739 75.233  1.031   1.00 47.29 ? 77   VAL A O   1 
ATOM   550  C CB  . VAL A 1 77  ? 38.756 75.954  -0.809  1.00 49.49 ? 77   VAL A CB  1 
ATOM   551  C CG1 . VAL A 1 77  ? 39.642 74.945  -0.123  1.00 49.95 ? 77   VAL A CG1 1 
ATOM   552  C CG2 . VAL A 1 77  ? 39.265 76.195  -2.217  1.00 49.83 ? 77   VAL A CG2 1 
ATOM   553  N N   . PHE A 1 78  ? 36.735 77.255  0.740   1.00 44.85 ? 78   PHE A N   1 
ATOM   554  C CA  . PHE A 1 78  ? 36.033 77.941  1.831   1.00 42.86 ? 78   PHE A CA  1 
ATOM   555  C C   . PHE A 1 78  ? 35.193 79.035  1.205   1.00 42.36 ? 78   PHE A C   1 
ATOM   556  O O   . PHE A 1 78  ? 35.560 80.208  1.247   1.00 42.40 ? 78   PHE A O   1 
ATOM   557  C CB  . PHE A 1 78  ? 37.030 78.538  2.842   1.00 41.25 ? 78   PHE A CB  1 
ATOM   558  C CG  . PHE A 1 78  ? 38.164 77.618  3.186   1.00 38.09 ? 78   PHE A CG  1 
ATOM   559  C CD1 . PHE A 1 78  ? 39.417 77.798  2.615   1.00 36.05 ? 78   PHE A CD1 1 
ATOM   560  C CD2 . PHE A 1 78  ? 37.969 76.546  4.052   1.00 34.78 ? 78   PHE A CD2 1 
ATOM   561  C CE1 . PHE A 1 78  ? 40.482 76.942  2.927   1.00 34.17 ? 78   PHE A CE1 1 
ATOM   562  C CE2 . PHE A 1 78  ? 39.021 75.692  4.375   1.00 32.85 ? 78   PHE A CE2 1 
ATOM   563  C CZ  . PHE A 1 78  ? 40.280 75.888  3.808   1.00 35.12 ? 78   PHE A CZ  1 
ATOM   564  N N   . GLY A 1 79  ? 34.068 78.637  0.614   1.00 41.73 ? 79   GLY A N   1 
ATOM   565  C CA  . GLY A 1 79  ? 33.243 79.535  -0.199  1.00 40.99 ? 79   GLY A CA  1 
ATOM   566  C C   . GLY A 1 79  ? 33.833 79.586  -1.591  1.00 40.45 ? 79   GLY A C   1 
ATOM   567  O O   . GLY A 1 79  ? 34.967 79.141  -1.814  1.00 39.87 ? 79   GLY A O   1 
ATOM   568  N N   . SER A 1 80  ? 33.076 80.112  -2.546  1.00 40.05 ? 80   SER A N   1 
ATOM   569  C CA  . SER A 1 80  ? 33.600 80.168  -3.920  1.00 39.97 ? 80   SER A CA  1 
ATOM   570  C C   . SER A 1 80  ? 34.171 81.552  -4.234  1.00 39.04 ? 80   SER A C   1 
ATOM   571  O O   . SER A 1 80  ? 33.583 82.568  -3.840  1.00 38.08 ? 80   SER A O   1 
ATOM   572  C CB  . SER A 1 80  ? 32.552 79.729  -4.947  1.00 39.62 ? 80   SER A CB  1 
ATOM   573  O OG  . SER A 1 80  ? 31.359 80.427  -4.716  1.00 41.52 ? 80   SER A OG  1 
ATOM   574  N N   . ASN A 1 81  ? 35.333 81.580  -4.900  1.00 38.46 ? 81   ASN A N   1 
ATOM   575  C CA  . ASN A 1 81  ? 35.935 82.851  -5.279  1.00 38.42 ? 81   ASN A CA  1 
ATOM   576  C C   . ASN A 1 81  ? 34.884 83.739  -5.965  1.00 37.91 ? 81   ASN A C   1 
ATOM   577  O O   . ASN A 1 81  ? 34.070 83.270  -6.774  1.00 37.96 ? 81   ASN A O   1 
ATOM   578  C CB  . ASN A 1 81  ? 37.149 82.664  -6.192  1.00 38.81 ? 81   ASN A CB  1 
ATOM   579  C CG  . ASN A 1 81  ? 38.401 82.172  -5.451  1.00 40.66 ? 81   ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 81  ? 39.114 81.303  -5.953  1.00 45.60 ? 81   ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 81  ? 38.674 82.721  -4.276  1.00 39.41 ? 81   ASN A ND2 1 
ATOM   582  N N   . VAL A 1 82  ? 34.873 85.003  -5.573  1.00 36.15 ? 82   VAL A N   1 
ATOM   583  C CA  . VAL A 1 82  ? 34.203 86.060  -6.281  1.00 34.99 ? 82   VAL A CA  1 
ATOM   584  C C   . VAL A 1 82  ? 34.585 86.002  -7.788  1.00 34.74 ? 82   VAL A C   1 
ATOM   585  O O   . VAL A 1 82  ? 35.761 85.842  -8.136  1.00 33.23 ? 82   VAL A O   1 
ATOM   586  C CB  . VAL A 1 82  ? 34.603 87.371  -5.569  1.00 35.59 ? 82   VAL A CB  1 
ATOM   587  C CG1 . VAL A 1 82  ? 34.561 88.581  -6.464  1.00 34.01 ? 82   VAL A CG1 1 
ATOM   588  C CG2 . VAL A 1 82  ? 33.768 87.550  -4.289  1.00 34.82 ? 82   VAL A CG2 1 
ATOM   589  N N   . ASP A 1 83  ? 33.580 86.099  -8.669  1.00 34.84 ? 83   ASP A N   1 
ATOM   590  C CA  . ASP A 1 83  ? 33.790 85.951  -10.129 1.00 35.19 ? 83   ASP A CA  1 
ATOM   591  C C   . ASP A 1 83  ? 34.691 87.036  -10.734 1.00 34.00 ? 83   ASP A C   1 
ATOM   592  O O   . ASP A 1 83  ? 35.564 86.748  -11.541 1.00 34.43 ? 83   ASP A O   1 
ATOM   593  C CB  . ASP A 1 83  ? 32.463 85.984  -10.889 1.00 35.75 ? 83   ASP A CB  1 
ATOM   594  C CG  . ASP A 1 83  ? 31.519 84.825  -10.522 1.00 41.06 ? 83   ASP A CG  1 
ATOM   595  O OD1 . ASP A 1 83  ? 31.992 83.739  -10.071 1.00 43.31 ? 83   ASP A OD1 1 
ATOM   596  O OD2 . ASP A 1 83  ? 30.289 85.018  -10.720 1.00 45.43 ? 83   ASP A OD2 1 
ATOM   597  N N   . ASN A 1 84  ? 34.425 88.282  -10.382 1.00 32.83 ? 84   ASN A N   1 
ATOM   598  C CA  . ASN A 1 84  ? 35.162 89.389  -10.948 1.00 33.06 ? 84   ASN A CA  1 
ATOM   599  C C   . ASN A 1 84  ? 35.772 90.284  -9.882  1.00 31.23 ? 84   ASN A C   1 
ATOM   600  O O   . ASN A 1 84  ? 35.063 90.879  -9.063  1.00 30.64 ? 84   ASN A O   1 
ATOM   601  C CB  . ASN A 1 84  ? 34.285 90.198  -11.895 1.00 33.89 ? 84   ASN A CB  1 
ATOM   602  C CG  . ASN A 1 84  ? 34.144 89.547  -13.236 1.00 36.98 ? 84   ASN A CG  1 
ATOM   603  O OD1 . ASN A 1 84  ? 33.360 88.618  -13.399 1.00 39.77 ? 84   ASN A OD1 1 
ATOM   604  N ND2 . ASN A 1 84  ? 34.926 90.016  -14.209 1.00 41.78 ? 84   ASN A ND2 1 
ATOM   605  N N   . VAL A 1 85  ? 37.094 90.360  -9.918  1.00 28.66 ? 85   VAL A N   1 
ATOM   606  C CA  . VAL A 1 85  ? 37.853 91.189  -8.983  1.00 26.81 ? 85   VAL A CA  1 
ATOM   607  C C   . VAL A 1 85  ? 38.400 92.461  -9.667  1.00 26.33 ? 85   VAL A C   1 
ATOM   608  O O   . VAL A 1 85  ? 38.846 92.413  -10.808 1.00 25.90 ? 85   VAL A O   1 
ATOM   609  C CB  . VAL A 1 85  ? 38.952 90.346  -8.285  1.00 26.36 ? 85   VAL A CB  1 
ATOM   610  C CG1 . VAL A 1 85  ? 39.853 91.220  -7.411  1.00 21.87 ? 85   VAL A CG1 1 
ATOM   611  C CG2 . VAL A 1 85  ? 38.270 89.266  -7.409  1.00 24.75 ? 85   VAL A CG2 1 
ATOM   612  N N   . LEU A 1 86  ? 38.298 93.602  -9.005  1.00 24.76 ? 86   LEU A N   1 
ATOM   613  C CA  . LEU A 1 86  ? 38.835 94.816  -9.587  1.00 24.76 ? 86   LEU A CA  1 
ATOM   614  C C   . LEU A 1 86  ? 40.149 95.138  -8.884  1.00 24.35 ? 86   LEU A C   1 
ATOM   615  O O   . LEU A 1 86  ? 40.188 95.255  -7.655  1.00 25.34 ? 86   LEU A O   1 
ATOM   616  C CB  . LEU A 1 86  ? 37.856 96.021  -9.498  1.00 23.34 ? 86   LEU A CB  1 
ATOM   617  C CG  . LEU A 1 86  ? 38.460 97.318  -10.077 1.00 24.32 ? 86   LEU A CG  1 
ATOM   618  C CD1 . LEU A 1 86  ? 38.485 97.254  -11.606 1.00 24.97 ? 86   LEU A CD1 1 
ATOM   619  C CD2 . LEU A 1 86  ? 37.795 98.610  -9.605  1.00 25.99 ? 86   LEU A CD2 1 
ATOM   620  N N   . LEU A 1 87  ? 41.214 95.289  -9.658  1.00 24.58 ? 87   LEU A N   1 
ATOM   621  C CA  . LEU A 1 87  ? 42.501 95.802  -9.120  1.00 24.23 ? 87   LEU A CA  1 
ATOM   622  C C   . LEU A 1 87  ? 42.647 97.300  -9.344  1.00 24.07 ? 87   LEU A C   1 
ATOM   623  O O   . LEU A 1 87  ? 42.753 97.717  -10.471 1.00 24.65 ? 87   LEU A O   1 
ATOM   624  C CB  . LEU A 1 87  ? 43.699 95.078  -9.772  1.00 24.60 ? 87   LEU A CB  1 
ATOM   625  C CG  . LEU A 1 87  ? 45.117 95.653  -9.512  1.00 24.23 ? 87   LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 87  ? 45.483 95.620  -8.023  1.00 22.75 ? 87   LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 87  ? 46.140 94.846  -10.293 1.00 24.25 ? 87   LEU A CD2 1 
ATOM   628  N N   . THR A 1 88  ? 42.693 98.089  -8.273  1.00 23.97 ? 88   THR A N   1 
ATOM   629  C CA  . THR A 1 88  ? 42.955 99.521  -8.324  1.00 24.60 ? 88   THR A CA  1 
ATOM   630  C C   . THR A 1 88  ? 44.341 99.868  -7.745  1.00 24.66 ? 88   THR A C   1 
ATOM   631  O O   . THR A 1 88  ? 44.610 99.604  -6.578  1.00 24.84 ? 88   THR A O   1 
ATOM   632  C CB  . THR A 1 88  ? 41.909 100.313 -7.528  1.00 24.78 ? 88   THR A CB  1 
ATOM   633  O OG1 . THR A 1 88  ? 40.605 99.970  -8.003  1.00 26.22 ? 88   THR A OG1 1 
ATOM   634  C CG2 . THR A 1 88  ? 42.121 101.826 -7.703  1.00 26.06 ? 88   THR A CG2 1 
ATOM   635  N N   . ALA A 1 89  ? 45.188 100.470 -8.577  1.00 24.15 ? 89   ALA A N   1 
ATOM   636  C CA  . ALA A 1 89  ? 46.573 100.768 -8.240  1.00 23.79 ? 89   ALA A CA  1 
ATOM   637  C C   . ALA A 1 89  ? 46.810 102.275 -8.291  1.00 24.06 ? 89   ALA A C   1 
ATOM   638  O O   . ALA A 1 89  ? 46.499 102.926 -9.298  1.00 23.99 ? 89   ALA A O   1 
ATOM   639  C CB  . ALA A 1 89  ? 47.501 100.030 -9.186  1.00 22.74 ? 89   ALA A CB  1 
ATOM   640  N N   . GLU A 1 90  ? 47.275 102.848 -7.171  1.00 23.53 ? 90   GLU A N   1 
ATOM   641  C CA  . GLU A 1 90  ? 47.533 104.271 -7.096  1.00 23.11 ? 90   GLU A CA  1 
ATOM   642  C C   . GLU A 1 90  ? 49.005 104.514 -6.736  1.00 23.00 ? 90   GLU A C   1 
ATOM   643  O O   . GLU A 1 90  ? 49.521 103.946 -5.771  1.00 22.77 ? 90   GLU A O   1 
ATOM   644  C CB  . GLU A 1 90  ? 46.609 104.942 -6.071  1.00 22.94 ? 90   GLU A CB  1 
ATOM   645  C CG  . GLU A 1 90  ? 45.191 104.378 -6.054  1.00 24.32 ? 90   GLU A CG  1 
ATOM   646  C CD  . GLU A 1 90  ? 44.383 104.937 -4.914  1.00 26.06 ? 90   GLU A CD  1 
ATOM   647  O OE1 . GLU A 1 90  ? 44.916 105.055 -3.779  1.00 26.00 ? 90   GLU A OE1 1 
ATOM   648  O OE2 . GLU A 1 90  ? 43.212 105.285 -5.162  1.00 29.22 ? 90   GLU A OE2 1 
ATOM   649  N N   . TYR A 1 91  ? 49.673 105.343 -7.530  1.00 22.67 ? 91   TYR A N   1 
ATOM   650  C CA  . TYR A 1 91  ? 51.069 105.717 -7.277  1.00 22.58 ? 91   TYR A CA  1 
ATOM   651  C C   . TYR A 1 91  ? 51.045 106.961 -6.413  1.00 21.17 ? 91   TYR A C   1 
ATOM   652  O O   . TYR A 1 91  ? 51.194 108.076 -6.898  1.00 20.24 ? 91   TYR A O   1 
ATOM   653  C CB  . TYR A 1 91  ? 51.796 106.020 -8.600  1.00 23.60 ? 91   TYR A CB  1 
ATOM   654  C CG  . TYR A 1 91  ? 51.941 104.865 -9.577  1.00 24.41 ? 91   TYR A CG  1 
ATOM   655  C CD1 . TYR A 1 91  ? 52.955 103.943 -9.449  1.00 27.64 ? 91   TYR A CD1 1 
ATOM   656  C CD2 . TYR A 1 91  ? 51.112 104.750 -10.673 1.00 27.94 ? 91   TYR A CD2 1 
ATOM   657  C CE1 . TYR A 1 91  ? 53.144 102.904 -10.377 1.00 26.91 ? 91   TYR A CE1 1 
ATOM   658  C CE2 . TYR A 1 91  ? 51.256 103.685 -11.602 1.00 30.41 ? 91   TYR A CE2 1 
ATOM   659  C CZ  . TYR A 1 91  ? 52.281 102.770 -11.436 1.00 28.81 ? 91   TYR A CZ  1 
ATOM   660  O OH  . TYR A 1 91  ? 52.446 101.741 -12.324 1.00 27.52 ? 91   TYR A OH  1 
ATOM   661  N N   . GLN A 1 92  ? 50.844 106.771 -5.122  1.00 20.28 ? 92   GLN A N   1 
ATOM   662  C CA  . GLN A 1 92  ? 50.520 107.879 -4.227  1.00 20.36 ? 92   GLN A CA  1 
ATOM   663  C C   . GLN A 1 92  ? 51.655 108.870 -3.984  1.00 20.26 ? 92   GLN A C   1 
ATOM   664  O O   . GLN A 1 92  ? 51.421 110.080 -3.968  1.00 21.10 ? 92   GLN A O   1 
ATOM   665  C CB  . GLN A 1 92  ? 49.997 107.344 -2.899  1.00 19.72 ? 92   GLN A CB  1 
ATOM   666  C CG  . GLN A 1 92  ? 48.602 106.685 -3.049  1.00 21.06 ? 92   GLN A CG  1 
ATOM   667  C CD  . GLN A 1 92  ? 48.021 106.201 -1.735  1.00 21.49 ? 92   GLN A CD  1 
ATOM   668  O OE1 . GLN A 1 92  ? 48.696 106.142 -0.707  1.00 22.20 ? 92   GLN A OE1 1 
ATOM   669  N NE2 . GLN A 1 92  ? 46.760 105.882 -1.761  1.00 19.69 ? 92   GLN A NE2 1 
ATOM   670  N N   . THR A 1 93  ? 52.852 108.365 -3.740  1.00 19.56 ? 93   THR A N   1 
ATOM   671  C CA  . THR A 1 93  ? 54.044 109.213 -3.569  1.00 20.56 ? 93   THR A CA  1 
ATOM   672  C C   . THR A 1 93  ? 55.212 108.493 -4.259  1.00 20.05 ? 93   THR A C   1 
ATOM   673  O O   . THR A 1 93  ? 55.049 107.357 -4.717  1.00 18.54 ? 93   THR A O   1 
ATOM   674  C CB  . THR A 1 93  ? 54.366 109.560 -2.061  1.00 20.99 ? 93   THR A CB  1 
ATOM   675  O OG1 . THR A 1 93  ? 55.033 108.474 -1.422  1.00 23.69 ? 93   THR A OG1 1 
ATOM   676  C CG2 . THR A 1 93  ? 53.144 109.929 -1.246  1.00 21.21 ? 93   THR A CG2 1 
ATOM   677  N N   . SER A 1 94  ? 56.382 109.142 -4.345  1.00 20.50 ? 94   SER A N   1 
ATOM   678  C CA  . SER A 1 94  ? 57.606 108.494 -4.845  1.00 21.17 ? 94   SER A CA  1 
ATOM   679  C C   . SER A 1 94  ? 58.008 107.220 -4.121  1.00 20.60 ? 94   SER A C   1 
ATOM   680  O O   . SER A 1 94  ? 58.708 106.367 -4.688  1.00 20.63 ? 94   SER A O   1 
ATOM   681  C CB  . SER A 1 94  ? 58.796 109.493 -4.771  1.00 22.26 ? 94   SER A CB  1 
ATOM   682  O OG  . SER A 1 94  ? 58.393 110.726 -5.384  1.00 26.63 ? 94   SER A OG  1 
ATOM   683  N N   . ASN A 1 95  ? 57.613 107.112 -2.855  1.00 20.31 ? 95   ASN A N   1 
ATOM   684  C CA  . ASN A 1 95  ? 58.043 106.008 -1.986  1.00 20.88 ? 95   ASN A CA  1 
ATOM   685  C C   . ASN A 1 95  ? 56.877 105.149 -1.434  1.00 20.26 ? 95   ASN A C   1 
ATOM   686  O O   . ASN A 1 95  ? 57.086 104.240 -0.636  1.00 20.46 ? 95   ASN A O   1 
ATOM   687  C CB  . ASN A 1 95  ? 58.880 106.553 -0.819  1.00 20.87 ? 95   ASN A CB  1 
ATOM   688  C CG  . ASN A 1 95  ? 60.210 107.192 -1.299  1.00 25.08 ? 95   ASN A CG  1 
ATOM   689  O OD1 . ASN A 1 95  ? 61.244 106.525 -1.394  1.00 31.99 ? 95   ASN A OD1 1 
ATOM   690  N ND2 . ASN A 1 95  ? 60.164 108.455 -1.620  1.00 24.42 ? 95   ASN A ND2 1 
ATOM   691  N N   . ARG A 1 96  ? 55.658 105.451 -1.848  1.00 19.79 ? 96   ARG A N   1 
ATOM   692  C CA  . ARG A 1 96  ? 54.484 104.714 -1.364  1.00 19.38 ? 96   ARG A CA  1 
ATOM   693  C C   . ARG A 1 96  ? 53.584 104.330 -2.509  1.00 19.22 ? 96   ARG A C   1 
ATOM   694  O O   . ARG A 1 96  ? 53.080 105.200 -3.232  1.00 19.48 ? 96   ARG A O   1 
ATOM   695  C CB  . ARG A 1 96  ? 53.695 105.513 -0.335  1.00 19.31 ? 96   ARG A CB  1 
ATOM   696  C CG  . ARG A 1 96  ? 52.468 104.736 0.194   1.00 18.15 ? 96   ARG A CG  1 
ATOM   697  C CD  . ARG A 1 96  ? 51.779 105.484 1.332   1.00 21.26 ? 96   ARG A CD  1 
ATOM   698  N NE  . ARG A 1 96  ? 50.886 106.522 0.858   1.00 22.40 ? 96   ARG A NE  1 
ATOM   699  C CZ  . ARG A 1 96  ? 50.975 107.808 1.179   1.00 26.39 ? 96   ARG A CZ  1 
ATOM   700  N NH1 . ARG A 1 96  ? 51.945 108.264 1.993   1.00 25.21 ? 96   ARG A NH1 1 
ATOM   701  N NH2 . ARG A 1 96  ? 50.069 108.646 0.698   1.00 25.94 ? 96   ARG A NH2 1 
ATOM   702  N N   . PHE A 1 97  ? 53.426 103.016 -2.687  1.00 19.71 ? 97   PHE A N   1 
ATOM   703  C CA  . PHE A 1 97  ? 52.492 102.416 -3.662  1.00 19.26 ? 97   PHE A CA  1 
ATOM   704  C C   . PHE A 1 97  ? 51.286 101.818 -2.911  1.00 19.69 ? 97   PHE A C   1 
ATOM   705  O O   . PHE A 1 97  ? 51.460 101.139 -1.892  1.00 18.37 ? 97   PHE A O   1 
ATOM   706  C CB  . PHE A 1 97  ? 53.208 101.316 -4.472  1.00 18.90 ? 97   PHE A CB  1 
ATOM   707  C CG  . PHE A 1 97  ? 52.326 100.612 -5.503  1.00 19.35 ? 97   PHE A CG  1 
ATOM   708  C CD1 . PHE A 1 97  ? 51.645 101.337 -6.494  1.00 18.30 ? 97   PHE A CD1 1 
ATOM   709  C CD2 . PHE A 1 97  ? 52.207 99.226  -5.486  1.00 17.04 ? 97   PHE A CD2 1 
ATOM   710  C CE1 . PHE A 1 97  ? 50.840 100.681 -7.426  1.00 19.49 ? 97   PHE A CE1 1 
ATOM   711  C CE2 . PHE A 1 97  ? 51.431 98.568  -6.407  1.00 18.94 ? 97   PHE A CE2 1 
ATOM   712  C CZ  . PHE A 1 97  ? 50.731 99.293  -7.386  1.00 19.32 ? 97   PHE A CZ  1 
ATOM   713  N N   . HIS A 1 98  ? 50.091 102.083 -3.428  1.00 19.75 ? 98   HIS A N   1 
ATOM   714  C CA  . HIS A 1 98  ? 48.852 101.528 -2.891  1.00 21.00 ? 98   HIS A CA  1 
ATOM   715  C C   . HIS A 1 98  ? 48.152 100.665 -3.946  1.00 21.37 ? 98   HIS A C   1 
ATOM   716  O O   . HIS A 1 98  ? 47.926 101.117 -5.062  1.00 21.83 ? 98   HIS A O   1 
ATOM   717  C CB  . HIS A 1 98  ? 47.951 102.692 -2.456  1.00 20.46 ? 98   HIS A CB  1 
ATOM   718  C CG  . HIS A 1 98  ? 46.597 102.292 -1.953  1.00 22.37 ? 98   HIS A CG  1 
ATOM   719  N ND1 . HIS A 1 98  ? 46.406 101.352 -0.959  1.00 23.72 ? 98   HIS A ND1 1 
ATOM   720  C CD2 . HIS A 1 98  ? 45.367 102.762 -2.263  1.00 20.21 ? 98   HIS A CD2 1 
ATOM   721  C CE1 . HIS A 1 98  ? 45.117 101.241 -0.700  1.00 19.17 ? 98   HIS A CE1 1 
ATOM   722  N NE2 . HIS A 1 98  ? 44.465 102.083 -1.479  1.00 22.87 ? 98   HIS A NE2 1 
ATOM   723  N N   . PHE A 1 99  ? 47.827 99.418  -3.616  1.00 22.01 ? 99   PHE A N   1 
ATOM   724  C CA  . PHE A 1 99  ? 46.873 98.650  -4.445  1.00 22.02 ? 99   PHE A CA  1 
ATOM   725  C C   . PHE A 1 99  ? 45.758 97.978  -3.613  1.00 22.41 ? 99   PHE A C   1 
ATOM   726  O O   . PHE A 1 99  ? 46.014 97.468  -2.503  1.00 21.53 ? 99   PHE A O   1 
ATOM   727  C CB  . PHE A 1 99  ? 47.606 97.673  -5.393  1.00 21.57 ? 99   PHE A CB  1 
ATOM   728  C CG  . PHE A 1 99  ? 48.252 96.447  -4.706  1.00 22.96 ? 99   PHE A CG  1 
ATOM   729  C CD1 . PHE A 1 99  ? 47.589 95.209  -4.663  1.00 22.46 ? 99   PHE A CD1 1 
ATOM   730  C CD2 . PHE A 1 99  ? 49.541 96.512  -4.196  1.00 23.63 ? 99   PHE A CD2 1 
ATOM   731  C CE1 . PHE A 1 99  ? 48.183 94.085  -4.057  1.00 20.38 ? 99   PHE A CE1 1 
ATOM   732  C CE2 . PHE A 1 99  ? 50.145 95.378  -3.593  1.00 22.81 ? 99   PHE A CE2 1 
ATOM   733  C CZ  . PHE A 1 99  ? 49.461 94.177  -3.532  1.00 21.19 ? 99   PHE A CZ  1 
ATOM   734  N N   . LYS A 1 100 ? 44.530 97.999  -4.140  1.00 23.48 ? 100  LYS A N   1 
ATOM   735  C CA  . LYS A 1 100 ? 43.416 97.276  -3.531  1.00 24.71 ? 100  LYS A CA  1 
ATOM   736  C C   . LYS A 1 100 ? 42.676 96.372  -4.496  1.00 24.62 ? 100  LYS A C   1 
ATOM   737  O O   . LYS A 1 100 ? 42.536 96.688  -5.688  1.00 24.17 ? 100  LYS A O   1 
ATOM   738  C CB  . LYS A 1 100 ? 42.442 98.175  -2.730  1.00 25.13 ? 100  LYS A CB  1 
ATOM   739  C CG  . LYS A 1 100 ? 41.732 99.274  -3.409  1.00 27.52 ? 100  LYS A CG  1 
ATOM   740  C CD  . LYS A 1 100 ? 40.643 99.900  -2.502  1.00 27.29 ? 100  LYS A CD  1 
ATOM   741  C CE  . LYS A 1 100 ? 41.194 100.803 -1.369  1.00 32.29 ? 100  LYS A CE  1 
ATOM   742  N NZ  . LYS A 1 100 ? 40.152 101.587 -0.555  1.00 32.01 ? 100  LYS A NZ  1 
ATOM   743  N N   . LEU A 1 101 ? 42.235 95.232  -3.964  1.00 24.57 ? 101  LEU A N   1 
ATOM   744  C CA  . LEU A 1 101 ? 41.475 94.239  -4.720  1.00 25.20 ? 101  LEU A CA  1 
ATOM   745  C C   . LEU A 1 101 ? 40.078 94.176  -4.142  1.00 25.99 ? 101  LEU A C   1 
ATOM   746  O O   . LEU A 1 101 ? 39.902 93.906  -2.954  1.00 25.54 ? 101  LEU A O   1 
ATOM   747  C CB  . LEU A 1 101 ? 42.160 92.860  -4.671  1.00 24.78 ? 101  LEU A CB  1 
ATOM   748  C CG  . LEU A 1 101 ? 43.550 92.862  -5.329  1.00 25.42 ? 101  LEU A CG  1 
ATOM   749  C CD1 . LEU A 1 101 ? 44.467 91.831  -4.662  1.00 23.74 ? 101  LEU A CD1 1 
ATOM   750  C CD2 . LEU A 1 101 ? 43.451 92.659  -6.851  1.00 19.61 ? 101  LEU A CD2 1 
ATOM   751  N N   . THR A 1 102 ? 39.097 94.488  -4.977  1.00 26.29 ? 102  THR A N   1 
ATOM   752  C CA  . THR A 1 102 ? 37.724 94.566  -4.530  1.00 26.99 ? 102  THR A CA  1 
ATOM   753  C C   . THR A 1 102 ? 36.880 93.568  -5.350  1.00 28.44 ? 102  THR A C   1 
ATOM   754  O O   . THR A 1 102 ? 37.319 93.070  -6.386  1.00 28.14 ? 102  THR A O   1 
ATOM   755  C CB  . THR A 1 102 ? 37.140 95.992  -4.670  1.00 26.49 ? 102  THR A CB  1 
ATOM   756  O OG1 . THR A 1 102 ? 37.431 96.514  -5.969  1.00 24.44 ? 102  THR A OG1 1 
ATOM   757  C CG2 . THR A 1 102 ? 37.703 96.922  -3.620  1.00 27.29 ? 102  THR A CG2 1 
ATOM   758  N N   . ASP A 1 103 ? 35.695 93.254  -4.848  1.00 29.99 ? 103  ASP A N   1 
ATOM   759  C CA  . ASP A 1 103 ? 34.722 92.541  -5.620  1.00 32.19 ? 103  ASP A CA  1 
ATOM   760  C C   . ASP A 1 103 ? 34.172 93.569  -6.604  1.00 33.43 ? 103  ASP A C   1 
ATOM   761  O O   . ASP A 1 103 ? 33.610 94.588  -6.206  1.00 33.38 ? 103  ASP A O   1 
ATOM   762  C CB  . ASP A 1 103 ? 33.613 92.034  -4.696  1.00 32.14 ? 103  ASP A CB  1 
ATOM   763  C CG  . ASP A 1 103 ? 32.544 91.227  -5.428  1.00 34.65 ? 103  ASP A CG  1 
ATOM   764  O OD1 . ASP A 1 103 ? 32.363 91.386  -6.666  1.00 36.39 ? 103  ASP A OD1 1 
ATOM   765  O OD2 . ASP A 1 103 ? 31.870 90.430  -4.742  1.00 38.46 ? 103  ASP A OD2 1 
ATOM   766  N N   . GLN A 1 104 ? 34.336 93.293  -7.889  1.00 35.30 ? 104  GLN A N   1 
ATOM   767  C CA  . GLN A 1 104 ? 33.942 94.227  -8.938  1.00 37.55 ? 104  GLN A CA  1 
ATOM   768  C C   . GLN A 1 104 ? 32.443 94.536  -8.918  1.00 38.28 ? 104  GLN A C   1 
ATOM   769  O O   . GLN A 1 104 ? 32.031 95.631  -9.292  1.00 39.00 ? 104  GLN A O   1 
ATOM   770  C CB  . GLN A 1 104 ? 34.386 93.669  -10.289 1.00 38.02 ? 104  GLN A CB  1 
ATOM   771  C CG  . GLN A 1 104 ? 34.124 94.510  -11.513 1.00 41.28 ? 104  GLN A CG  1 
ATOM   772  C CD  . GLN A 1 104 ? 34.599 93.776  -12.741 1.00 44.77 ? 104  GLN A CD  1 
ATOM   773  O OE1 . GLN A 1 104 ? 35.797 93.714  -12.991 1.00 47.52 ? 104  GLN A OE1 1 
ATOM   774  N NE2 . GLN A 1 104 ? 33.669 93.171  -13.491 1.00 46.80 ? 104  GLN A NE2 1 
ATOM   775  N N   . THR A 1 105 ? 31.640 93.582  -8.454  1.00 39.24 ? 105  THR A N   1 
ATOM   776  C CA  . THR A 1 105 ? 30.184 93.739  -8.393  1.00 40.24 ? 105  THR A CA  1 
ATOM   777  C C   . THR A 1 105 ? 29.600 94.274  -7.065  1.00 40.33 ? 105  THR A C   1 
ATOM   778  O O   . THR A 1 105 ? 28.646 95.074  -7.087  1.00 40.71 ? 105  THR A O   1 
ATOM   779  C CB  . THR A 1 105 ? 29.467 92.415  -8.771  1.00 41.01 ? 105  THR A CB  1 
ATOM   780  O OG1 . THR A 1 105 ? 30.159 91.781  -9.863  1.00 42.43 ? 105  THR A OG1 1 
ATOM   781  C CG2 . THR A 1 105 ? 28.012 92.689  -9.166  1.00 41.07 ? 105  THR A CG2 1 
ATOM   782  N N   . ASN A 1 106 ? 30.146 93.845  -5.923  1.00 39.75 ? 106  ASN A N   1 
ATOM   783  C CA  . ASN A 1 106 ? 29.597 94.255  -4.607  1.00 39.63 ? 106  ASN A CA  1 
ATOM   784  C C   . ASN A 1 106 ? 30.576 95.029  -3.728  1.00 38.57 ? 106  ASN A C   1 
ATOM   785  O O   . ASN A 1 106 ? 31.788 94.776  -3.763  1.00 39.15 ? 106  ASN A O   1 
ATOM   786  C CB  . ASN A 1 106 ? 29.072 93.042  -3.829  1.00 39.58 ? 106  ASN A CB  1 
ATOM   787  C CG  . ASN A 1 106 ? 28.438 92.021  -4.738  1.00 41.82 ? 106  ASN A CG  1 
ATOM   788  O OD1 . ASN A 1 106 ? 29.094 91.053  -5.149  1.00 43.97 ? 106  ASN A OD1 1 
ATOM   789  N ND2 . ASN A 1 106 ? 27.165 92.246  -5.104  1.00 43.33 ? 106  ASN A ND2 1 
ATOM   790  N N   . ASN A 1 107 ? 30.039 95.971  -2.956  1.00 36.83 ? 107  ASN A N   1 
ATOM   791  C CA  . ASN A 1 107 ? 30.803 96.670  -1.938  1.00 35.33 ? 107  ASN A CA  1 
ATOM   792  C C   . ASN A 1 107 ? 31.063 95.653  -0.847  1.00 32.95 ? 107  ASN A C   1 
ATOM   793  O O   . ASN A 1 107 ? 30.224 94.803  -0.573  1.00 33.09 ? 107  ASN A O   1 
ATOM   794  C CB  . ASN A 1 107 ? 30.035 97.870  -1.365  1.00 36.46 ? 107  ASN A CB  1 
ATOM   795  C CG  . ASN A 1 107 ? 29.605 98.887  -2.443  1.00 39.75 ? 107  ASN A CG  1 
ATOM   796  O OD1 . ASN A 1 107 ? 28.434 99.265  -2.500  1.00 46.68 ? 107  ASN A OD1 1 
ATOM   797  N ND2 . ASN A 1 107 ? 30.545 99.339  -3.277  1.00 42.64 ? 107  ASN A ND2 1 
ATOM   798  N N   . ARG A 1 108 ? 32.248 95.711  -0.263  1.00 29.29 ? 108  ARG A N   1 
ATOM   799  C CA  . ARG A 1 108 ? 32.621 94.797  0.804   1.00 26.05 ? 108  ARG A CA  1 
ATOM   800  C C   . ARG A 1 108 ? 33.059 95.685  1.962   1.00 24.88 ? 108  ARG A C   1 
ATOM   801  O O   . ARG A 1 108 ? 33.245 96.898  1.775   1.00 23.93 ? 108  ARG A O   1 
ATOM   802  C CB  . ARG A 1 108 ? 33.740 93.833  0.341   1.00 26.04 ? 108  ARG A CB  1 
ATOM   803  C CG  . ARG A 1 108 ? 33.316 92.829  -0.752  1.00 24.22 ? 108  ARG A CG  1 
ATOM   804  C CD  . ARG A 1 108 ? 34.402 91.833  -1.113  1.00 22.95 ? 108  ARG A CD  1 
ATOM   805  N NE  . ARG A 1 108 ? 34.922 91.211  0.095   1.00 19.26 ? 108  ARG A NE  1 
ATOM   806  C CZ  . ARG A 1 108 ? 34.416 90.133  0.663   1.00 19.63 ? 108  ARG A CZ  1 
ATOM   807  N NH1 . ARG A 1 108 ? 33.380 89.508  0.124   1.00 23.72 ? 108  ARG A NH1 1 
ATOM   808  N NH2 . ARG A 1 108 ? 34.933 89.681  1.779   1.00 19.76 ? 108  ARG A NH2 1 
ATOM   809  N N   . PHE A 1 109 ? 33.174 95.100  3.158   1.00 24.03 ? 109  PHE A N   1 
ATOM   810  C CA  . PHE A 1 109 ? 33.641 95.854  4.316   1.00 23.21 ? 109  PHE A CA  1 
ATOM   811  C C   . PHE A 1 109 ? 35.064 96.404  4.079   1.00 22.80 ? 109  PHE A C   1 
ATOM   812  O O   . PHE A 1 109 ? 35.934 95.663  3.596   1.00 22.67 ? 109  PHE A O   1 
ATOM   813  C CB  . PHE A 1 109 ? 33.623 95.016  5.597   1.00 22.92 ? 109  PHE A CB  1 
ATOM   814  C CG  . PHE A 1 109 ? 34.252 95.724  6.756   1.00 21.66 ? 109  PHE A CG  1 
ATOM   815  C CD1 . PHE A 1 109 ? 33.536 96.679  7.474   1.00 21.27 ? 109  PHE A CD1 1 
ATOM   816  C CD2 . PHE A 1 109 ? 35.575 95.474  7.101   1.00 20.83 ? 109  PHE A CD2 1 
ATOM   817  C CE1 . PHE A 1 109 ? 34.136 97.385  8.530   1.00 21.92 ? 109  PHE A CE1 1 
ATOM   818  C CE2 . PHE A 1 109 ? 36.171 96.175  8.153   1.00 20.21 ? 109  PHE A CE2 1 
ATOM   819  C CZ  . PHE A 1 109 ? 35.450 97.120  8.860   1.00 20.97 ? 109  PHE A CZ  1 
ATOM   820  N N   . GLU A 1 110 ? 35.270 97.680  4.410   1.00 22.26 ? 110  GLU A N   1 
ATOM   821  C CA  . GLU A 1 110 ? 36.582 98.345  4.364   1.00 24.13 ? 110  GLU A CA  1 
ATOM   822  C C   . GLU A 1 110 ? 36.797 99.104  5.661   1.00 22.94 ? 110  GLU A C   1 
ATOM   823  O O   . GLU A 1 110 ? 35.865 99.755  6.165   1.00 22.63 ? 110  GLU A O   1 
ATOM   824  C CB  . GLU A 1 110 ? 36.672 99.286  3.161   1.00 23.69 ? 110  GLU A CB  1 
ATOM   825  C CG  . GLU A 1 110 ? 36.631 98.510  1.845   1.00 27.22 ? 110  GLU A CG  1 
ATOM   826  C CD  . GLU A 1 110 ? 36.869 99.350  0.597   1.00 29.35 ? 110  GLU A CD  1 
ATOM   827  O OE1 . GLU A 1 110 ? 37.728 100.269 0.620   1.00 37.44 ? 110  GLU A OE1 1 
ATOM   828  O OE2 . GLU A 1 110 ? 36.231 99.044  -0.441  1.00 35.12 ? 110  GLU A OE2 1 
ATOM   829  N N   . VAL A 1 111 ? 38.001 98.989  6.229   1.00 22.17 ? 111  VAL A N   1 
ATOM   830  C CA  . VAL A 1 111 ? 38.291 99.609  7.542   1.00 21.49 ? 111  VAL A CA  1 
ATOM   831  C C   . VAL A 1 111 ? 37.981 101.118 7.491   1.00 22.31 ? 111  VAL A C   1 
ATOM   832  O O   . VAL A 1 111 ? 38.483 101.781 6.614   1.00 22.33 ? 111  VAL A O   1 
ATOM   833  C CB  . VAL A 1 111 ? 39.743 99.348  7.959   1.00 20.70 ? 111  VAL A CB  1 
ATOM   834  C CG1 . VAL A 1 111 ? 40.046 99.957  9.336   1.00 15.89 ? 111  VAL A CG1 1 
ATOM   835  C CG2 . VAL A 1 111 ? 39.990 97.845  7.960   1.00 18.00 ? 111  VAL A CG2 1 
ATOM   836  N N   . PRO A 1 112 ? 37.094 101.637 8.380   1.00 23.07 ? 112  PRO A N   1 
ATOM   837  C CA  . PRO A 1 112 ? 36.859 103.076 8.409   1.00 23.56 ? 112  PRO A CA  1 
ATOM   838  C C   . PRO A 1 112 ? 37.904 103.791 9.276   1.00 24.21 ? 112  PRO A C   1 
ATOM   839  O O   . PRO A 1 112 ? 37.608 104.263 10.375  1.00 24.03 ? 112  PRO A O   1 
ATOM   840  C CB  . PRO A 1 112 ? 35.458 103.180 9.007   1.00 24.43 ? 112  PRO A CB  1 
ATOM   841  C CG  . PRO A 1 112 ? 35.369 102.023 9.929   1.00 23.74 ? 112  PRO A CG  1 
ATOM   842  C CD  . PRO A 1 112 ? 36.254 100.933 9.369   1.00 23.28 ? 112  PRO A CD  1 
ATOM   843  N N   . HIS A 1 113 ? 39.131 103.838 8.762   1.00 23.92 ? 113  HIS A N   1 
ATOM   844  C CA  . HIS A 1 113 ? 40.270 104.281 9.528   1.00 24.34 ? 113  HIS A CA  1 
ATOM   845  C C   . HIS A 1 113 ? 40.086 105.771 9.746   1.00 24.54 ? 113  HIS A C   1 
ATOM   846  O O   . HIS A 1 113 ? 39.600 106.458 8.858   1.00 24.04 ? 113  HIS A O   1 
ATOM   847  C CB  . HIS A 1 113 ? 41.583 103.997 8.778   1.00 23.33 ? 113  HIS A CB  1 
ATOM   848  C CG  . HIS A 1 113 ? 42.785 103.982 9.674   1.00 22.87 ? 113  HIS A CG  1 
ATOM   849  N ND1 . HIS A 1 113 ? 43.662 105.043 9.770   1.00 20.61 ? 113  HIS A ND1 1 
ATOM   850  C CD2 . HIS A 1 113 ? 43.221 103.053 10.558  1.00 20.78 ? 113  HIS A CD2 1 
ATOM   851  C CE1 . HIS A 1 113 ? 44.597 104.759 10.656  1.00 20.07 ? 113  HIS A CE1 1 
ATOM   852  N NE2 . HIS A 1 113 ? 44.343 103.563 11.160  1.00 19.62 ? 113  HIS A NE2 1 
ATOM   853  N N   . GLU A 1 114 ? 40.466 106.247 10.930  1.00 25.10 ? 114  GLU A N   1 
ATOM   854  C CA  . GLU A 1 114 ? 40.311 107.656 11.286  1.00 26.02 ? 114  GLU A CA  1 
ATOM   855  C C   . GLU A 1 114 ? 41.389 108.529 10.577  1.00 26.15 ? 114  GLU A C   1 
ATOM   856  O O   . GLU A 1 114 ? 41.118 109.690 10.219  1.00 26.35 ? 114  GLU A O   1 
ATOM   857  C CB  . GLU A 1 114 ? 40.344 107.807 12.816  1.00 26.88 ? 114  GLU A CB  1 
ATOM   858  C CG  . GLU A 1 114 ? 40.142 109.238 13.385  1.00 29.05 ? 114  GLU A CG  1 
ATOM   859  C CD  . GLU A 1 114 ? 41.420 110.097 13.300  1.00 32.03 ? 114  GLU A CD  1 
ATOM   860  O OE1 . GLU A 1 114 ? 42.554 109.559 13.191  1.00 29.04 ? 114  GLU A OE1 1 
ATOM   861  O OE2 . GLU A 1 114 ? 41.275 111.333 13.324  1.00 35.81 ? 114  GLU A OE2 1 
ATOM   862  N N   . HIS A 1 115 ? 42.574 107.988 10.318  1.00 24.28 ? 115  HIS A N   1 
ATOM   863  C CA  . HIS A 1 115 ? 43.627 108.859 9.763   1.00 24.17 ? 115  HIS A CA  1 
ATOM   864  C C   . HIS A 1 115 ? 43.765 108.776 8.239   1.00 24.19 ? 115  HIS A C   1 
ATOM   865  O O   . HIS A 1 115 ? 43.913 109.802 7.566   1.00 23.82 ? 115  HIS A O   1 
ATOM   866  C CB  . HIS A 1 115 ? 44.995 108.607 10.434  1.00 23.43 ? 115  HIS A CB  1 
ATOM   867  C CG  . HIS A 1 115 ? 46.027 109.637 10.090  1.00 24.45 ? 115  HIS A CG  1 
ATOM   868  N ND1 . HIS A 1 115 ? 46.051 110.888 10.672  1.00 25.17 ? 115  HIS A ND1 1 
ATOM   869  C CD2 . HIS A 1 115 ? 47.065 109.606 9.222   1.00 23.17 ? 115  HIS A CD2 1 
ATOM   870  C CE1 . HIS A 1 115 ? 47.065 111.578 10.180  1.00 25.20 ? 115  HIS A CE1 1 
ATOM   871  N NE2 . HIS A 1 115 ? 47.693 110.823 9.296   1.00 23.15 ? 115  HIS A NE2 1 
ATOM   872  N N   . VAL A 1 116 ? 43.744 107.562 7.702   1.00 24.57 ? 116  VAL A N   1 
ATOM   873  C CA  . VAL A 1 116 ? 44.006 107.385 6.294   1.00 26.53 ? 116  VAL A CA  1 
ATOM   874  C C   . VAL A 1 116 ? 42.863 108.020 5.486   1.00 28.29 ? 116  VAL A C   1 
ATOM   875  O O   . VAL A 1 116 ? 41.695 107.810 5.774   1.00 27.78 ? 116  VAL A O   1 
ATOM   876  C CB  . VAL A 1 116 ? 44.265 105.912 5.931   1.00 25.62 ? 116  VAL A CB  1 
ATOM   877  C CG1 . VAL A 1 116 ? 44.362 105.739 4.418   1.00 24.46 ? 116  VAL A CG1 1 
ATOM   878  C CG2 . VAL A 1 116 ? 45.557 105.430 6.633   1.00 24.90 ? 116  VAL A CG2 1 
ATOM   879  N N   . GLN A 1 117 ? 43.225 108.819 4.493   1.00 30.32 ? 117  GLN A N   1 
ATOM   880  C CA  . GLN A 1 117 ? 42.262 109.455 3.612   1.00 32.64 ? 117  GLN A CA  1 
ATOM   881  C C   . GLN A 1 117 ? 42.275 108.806 2.233   1.00 33.37 ? 117  GLN A C   1 
ATOM   882  O O   . GLN A 1 117 ? 43.317 108.301 1.784   1.00 33.30 ? 117  GLN A O   1 
ATOM   883  C CB  . GLN A 1 117 ? 42.615 110.923 3.480   1.00 33.55 ? 117  GLN A CB  1 
ATOM   884  C CG  . GLN A 1 117 ? 42.054 111.778 4.574   1.00 36.67 ? 117  GLN A CG  1 
ATOM   885  C CD  . GLN A 1 117 ? 41.870 113.199 4.084   1.00 43.30 ? 117  GLN A CD  1 
ATOM   886  O OE1 . GLN A 1 117 ? 42.849 113.951 3.961   1.00 44.70 ? 117  GLN A OE1 1 
ATOM   887  N NE2 . GLN A 1 117 ? 40.606 113.578 3.775   1.00 43.66 ? 117  GLN A NE2 1 
ATOM   888  N N   . SER A 1 118 ? 41.133 108.829 1.539   1.00 34.27 ? 118  SER A N   1 
ATOM   889  C CA  . SER A 1 118 ? 41.121 108.305 0.163   1.00 35.14 ? 118  SER A CA  1 
ATOM   890  C C   . SER A 1 118 ? 42.013 109.173 -0.714  1.00 34.88 ? 118  SER A C   1 
ATOM   891  O O   . SER A 1 118 ? 42.184 110.376 -0.461  1.00 34.19 ? 118  SER A O   1 
ATOM   892  C CB  . SER A 1 118 ? 39.709 108.160 -0.418  1.00 35.69 ? 118  SER A CB  1 
ATOM   893  O OG  . SER A 1 118 ? 39.084 109.427 -0.524  1.00 38.36 ? 118  SER A OG  1 
ATOM   894  N N   . PHE A 1 119 ? 42.624 108.539 -1.707  1.00 35.13 ? 119  PHE A N   1 
ATOM   895  C CA  . PHE A 1 119 ? 43.551 109.233 -2.587  1.00 35.81 ? 119  PHE A CA  1 
ATOM   896  C C   . PHE A 1 119 ? 42.805 109.843 -3.760  1.00 36.82 ? 119  PHE A C   1 
ATOM   897  O O   . PHE A 1 119 ? 41.980 109.201 -4.415  1.00 36.21 ? 119  PHE A O   1 
ATOM   898  C CB  . PHE A 1 119 ? 44.666 108.300 -3.066  1.00 34.86 ? 119  PHE A CB  1 
ATOM   899  C CG  . PHE A 1 119 ? 45.707 108.973 -3.900  1.00 33.81 ? 119  PHE A CG  1 
ATOM   900  C CD1 . PHE A 1 119 ? 46.676 109.790 -3.317  1.00 35.38 ? 119  PHE A CD1 1 
ATOM   901  C CD2 . PHE A 1 119 ? 45.747 108.778 -5.268  1.00 33.67 ? 119  PHE A CD2 1 
ATOM   902  C CE1 . PHE A 1 119 ? 47.672 110.412 -4.109  1.00 33.53 ? 119  PHE A CE1 1 
ATOM   903  C CE2 . PHE A 1 119 ? 46.731 109.400 -6.058  1.00 34.55 ? 119  PHE A CE2 1 
ATOM   904  C CZ  . PHE A 1 119 ? 47.684 110.220 -5.473  1.00 33.21 ? 119  PHE A CZ  1 
ATOM   905  N N   . SER A 1 120 ? 43.079 111.118 -3.976  1.00 38.35 ? 120  SER A N   1 
ATOM   906  C CA  . SER A 1 120 ? 42.659 111.813 -5.186  1.00 39.97 ? 120  SER A CA  1 
ATOM   907  C C   . SER A 1 120 ? 43.941 112.479 -5.705  1.00 40.13 ? 120  SER A C   1 
ATOM   908  O O   . SER A 1 120 ? 44.937 112.559 -4.989  1.00 41.01 ? 120  SER A O   1 
ATOM   909  C CB  . SER A 1 120 ? 41.583 112.847 -4.863  1.00 40.24 ? 120  SER A CB  1 
ATOM   910  O OG  . SER A 1 120 ? 42.004 113.652 -3.764  1.00 41.96 ? 120  SER A OG  1 
ATOM   911  N N   . GLY A 1 121 ? 43.941 112.928 -6.945  1.00 40.01 ? 121  GLY A N   1 
ATOM   912  C CA  . GLY A 1 121 ? 45.184 113.425 -7.520  1.00 39.02 ? 121  GLY A CA  1 
ATOM   913  C C   . GLY A 1 121 ? 45.869 112.413 -8.410  1.00 37.61 ? 121  GLY A C   1 
ATOM   914  O O   . GLY A 1 121 ? 45.367 111.312 -8.624  1.00 37.74 ? 121  GLY A O   1 
ATOM   915  N N   . ASN A 1 122 ? 47.026 112.804 -8.922  1.00 36.30 ? 122  ASN A N   1 
ATOM   916  C CA  . ASN A 1 122 ? 47.684 112.095 -10.004 1.00 35.43 ? 122  ASN A CA  1 
ATOM   917  C C   . ASN A 1 122 ? 48.875 111.310 -9.526  1.00 33.58 ? 122  ASN A C   1 
ATOM   918  O O   . ASN A 1 122 ? 49.453 111.636 -8.511  1.00 34.08 ? 122  ASN A O   1 
ATOM   919  C CB  . ASN A 1 122 ? 48.151 113.100 -11.068 1.00 35.67 ? 122  ASN A CB  1 
ATOM   920  C CG  . ASN A 1 122 ? 47.027 113.995 -11.560 1.00 37.96 ? 122  ASN A CG  1 
ATOM   921  O OD1 . ASN A 1 122 ? 45.851 113.599 -11.589 1.00 40.00 ? 122  ASN A OD1 1 
ATOM   922  N ND2 . ASN A 1 122 ? 47.383 115.218 -11.944 1.00 39.06 ? 122  ASN A ND2 1 
ATOM   923  N N   . ALA A 1 123 ? 49.245 110.295 -10.285 1.00 32.26 ? 123  ALA A N   1 
ATOM   924  C CA  . ALA A 1 123 ? 50.423 109.510 -10.028 1.00 31.59 ? 123  ALA A CA  1 
ATOM   925  C C   . ALA A 1 123 ? 51.594 110.432 -9.700  1.00 32.39 ? 123  ALA A C   1 
ATOM   926  O O   . ALA A 1 123 ? 51.817 111.449 -10.380 1.00 31.87 ? 123  ALA A O   1 
ATOM   927  C CB  . ALA A 1 123 ? 50.727 108.677 -11.233 1.00 31.30 ? 123  ALA A CB  1 
ATOM   928  N N   . ALA A 1 124 ? 52.329 110.105 -8.636  1.00 32.05 ? 124  ALA A N   1 
ATOM   929  C CA  . ALA A 1 124 ? 53.510 110.891 -8.242  1.00 31.53 ? 124  ALA A CA  1 
ATOM   930  C C   . ALA A 1 124 ? 54.578 110.842 -9.308  1.00 31.38 ? 124  ALA A C   1 
ATOM   931  O O   . ALA A 1 124 ? 54.699 109.869 -10.041 1.00 31.67 ? 124  ALA A O   1 
ATOM   932  C CB  . ALA A 1 124 ? 54.083 110.375 -6.957  1.00 30.83 ? 124  ALA A CB  1 
ATOM   933  N N   . ALA A 1 125 ? 55.386 111.892 -9.348  1.00 31.67 ? 125  ALA A N   1 
ATOM   934  C CA  . ALA A 1 125 ? 56.539 111.956 -10.218 1.00 31.65 ? 125  ALA A CA  1 
ATOM   935  C C   . ALA A 1 125 ? 57.728 111.345 -9.493  1.00 31.93 ? 125  ALA A C   1 
ATOM   936  O O   . ALA A 1 125 ? 57.693 111.155 -8.253  1.00 32.41 ? 125  ALA A O   1 
ATOM   937  C CB  . ALA A 1 125 ? 56.821 113.416 -10.572 1.00 31.63 ? 125  ALA A CB  1 
ATOM   938  N N   . SER A 1 126 ? 58.761 111.004 -10.265 1.00 31.22 ? 126  SER A N   1 
ATOM   939  C CA  . SER A 1 126 ? 60.015 110.491 -9.719  1.00 31.26 ? 126  SER A CA  1 
ATOM   940  C C   . SER A 1 126 ? 59.852 109.282 -8.782  1.00 30.35 ? 126  SER A C   1 
ATOM   941  O O   . SER A 1 126 ? 60.419 109.257 -7.671  1.00 30.73 ? 126  SER A O   1 
ATOM   942  C CB  . SER A 1 126 ? 60.789 111.619 -9.027  1.00 31.72 ? 126  SER A CB  1 
ATOM   943  O OG  . SER A 1 126 ? 61.107 112.633 -9.971  1.00 34.81 ? 126  SER A OG  1 
ATOM   944  N N   . LEU A 1 127 ? 59.090 108.281 -9.235  1.00 28.63 ? 127  LEU A N   1 
ATOM   945  C CA  . LEU A 1 127 ? 58.872 107.068 -8.445  1.00 26.85 ? 127  LEU A CA  1 
ATOM   946  C C   . LEU A 1 127 ? 60.197 106.341 -8.187  1.00 25.11 ? 127  LEU A C   1 
ATOM   947  O O   . LEU A 1 127 ? 61.062 106.289 -9.062  1.00 25.93 ? 127  LEU A O   1 
ATOM   948  C CB  . LEU A 1 127 ? 57.913 106.127 -9.178  1.00 26.97 ? 127  LEU A CB  1 
ATOM   949  C CG  . LEU A 1 127 ? 56.620 106.725 -9.714  1.00 26.41 ? 127  LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 127 ? 55.970 105.723 -10.625 1.00 27.64 ? 127  LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 127 ? 55.729 107.133 -8.559  1.00 24.17 ? 127  LEU A CD2 1 
ATOM   952  N N   . THR A 1 128 ? 60.368 105.798 -6.991  1.00 22.98 ? 128  THR A N   1 
ATOM   953  C CA  . THR A 1 128 ? 61.540 104.989 -6.686  1.00 21.25 ? 128  THR A CA  1 
ATOM   954  C C   . THR A 1 128 ? 61.242 103.521 -6.971  1.00 21.62 ? 128  THR A C   1 
ATOM   955  O O   . THR A 1 128 ? 62.091 102.658 -6.771  1.00 21.80 ? 128  THR A O   1 
ATOM   956  C CB  . THR A 1 128 ? 61.971 105.144 -5.208  1.00 22.14 ? 128  THR A CB  1 
ATOM   957  O OG1 . THR A 1 128 ? 60.886 104.778 -4.346  1.00 21.14 ? 128  THR A OG1 1 
ATOM   958  C CG2 . THR A 1 128 ? 62.432 106.606 -4.895  1.00 22.72 ? 128  THR A CG2 1 
ATOM   959  N N   . TYR A 1 129 ? 60.016 103.219 -7.409  1.00 21.03 ? 129  TYR A N   1 
ATOM   960  C CA  . TYR A 1 129 ? 59.618 101.829 -7.636  1.00 21.38 ? 129  TYR A CA  1 
ATOM   961  C C   . TYR A 1 129 ? 58.963 101.712 -9.011  1.00 21.32 ? 129  TYR A C   1 
ATOM   962  O O   . TYR A 1 129 ? 58.519 102.702 -9.565  1.00 21.17 ? 129  TYR A O   1 
ATOM   963  C CB  . TYR A 1 129 ? 58.669 101.335 -6.528  1.00 19.58 ? 129  TYR A CB  1 
ATOM   964  C CG  . TYR A 1 129 ? 57.452 102.214 -6.379  1.00 20.91 ? 129  TYR A CG  1 
ATOM   965  C CD1 . TYR A 1 129 ? 56.311 101.996 -7.156  1.00 19.98 ? 129  TYR A CD1 1 
ATOM   966  C CD2 . TYR A 1 129 ? 57.446 103.294 -5.502  1.00 20.92 ? 129  TYR A CD2 1 
ATOM   967  C CE1 . TYR A 1 129 ? 55.197 102.826 -7.052  1.00 20.50 ? 129  TYR A CE1 1 
ATOM   968  C CE2 . TYR A 1 129 ? 56.334 104.147 -5.409  1.00 18.73 ? 129  TYR A CE2 1 
ATOM   969  C CZ  . TYR A 1 129 ? 55.206 103.889 -6.176  1.00 21.51 ? 129  TYR A CZ  1 
ATOM   970  O OH  . TYR A 1 129 ? 54.074 104.699 -6.071  1.00 19.67 ? 129  TYR A OH  1 
ATOM   971  N N   . GLN A 1 130 ? 58.927 100.504 -9.548  1.00 21.86 ? 130  GLN A N   1 
ATOM   972  C CA  . GLN A 1 130 ? 58.187 100.213 -10.748 1.00 23.72 ? 130  GLN A CA  1 
ATOM   973  C C   . GLN A 1 130 ? 57.195 99.053  -10.452 1.00 22.32 ? 130  GLN A C   1 
ATOM   974  O O   . GLN A 1 130 ? 57.518 98.159  -9.684  1.00 21.76 ? 130  GLN A O   1 
ATOM   975  C CB  . GLN A 1 130 ? 59.171 99.830  -11.861 1.00 22.79 ? 130  GLN A CB  1 
ATOM   976  C CG  . GLN A 1 130 ? 58.456 99.524  -13.184 1.00 27.88 ? 130  GLN A CG  1 
ATOM   977  C CD  . GLN A 1 130 ? 59.387 99.253  -14.347 1.00 30.23 ? 130  GLN A CD  1 
ATOM   978  O OE1 . GLN A 1 130 ? 60.104 98.227  -14.384 1.00 36.58 ? 130  GLN A OE1 1 
ATOM   979  N NE2 . GLN A 1 130 ? 59.379 100.170 -15.319 1.00 34.47 ? 130  GLN A NE2 1 
ATOM   980  N N   . VAL A 1 131 ? 56.031 99.051  -11.093 1.00 21.61 ? 131  VAL A N   1 
ATOM   981  C CA  . VAL A 1 131 ? 55.006 98.020  -10.864 1.00 22.19 ? 131  VAL A CA  1 
ATOM   982  C C   . VAL A 1 131 ? 54.764 97.192  -12.145 1.00 23.63 ? 131  VAL A C   1 
ATOM   983  O O   . VAL A 1 131 ? 54.587 97.746  -13.229 1.00 23.90 ? 131  VAL A O   1 
ATOM   984  C CB  . VAL A 1 131 ? 53.676 98.635  -10.355 1.00 22.54 ? 131  VAL A CB  1 
ATOM   985  C CG1 . VAL A 1 131 ? 52.577 97.557  -10.171 1.00 22.15 ? 131  VAL A CG1 1 
ATOM   986  C CG2 . VAL A 1 131 ? 53.884 99.395  -9.060  1.00 18.93 ? 131  VAL A CG2 1 
ATOM   987  N N   . GLU A 1 132 ? 54.799 95.865  -12.007 1.00 24.28 ? 132  GLU A N   1 
ATOM   988  C CA  A GLU A 1 132 ? 54.676 94.954  -13.134 0.50 24.91 ? 132  GLU A CA  1 
ATOM   989  C CA  B GLU A 1 132 ? 54.694 94.931  -13.137 0.50 24.91 ? 132  GLU A CA  1 
ATOM   990  C C   . GLU A 1 132 ? 53.510 94.012  -12.883 1.00 25.01 ? 132  GLU A C   1 
ATOM   991  O O   . GLU A 1 132 ? 53.390 93.442  -11.802 1.00 24.92 ? 132  GLU A O   1 
ATOM   992  C CB  A GLU A 1 132 ? 55.987 94.176  -13.279 0.50 24.79 ? 132  GLU A CB  1 
ATOM   993  C CB  B GLU A 1 132 ? 55.956 94.055  -13.256 0.50 24.69 ? 132  GLU A CB  1 
ATOM   994  C CG  A GLU A 1 132 ? 55.908 92.877  -14.023 0.50 26.24 ? 132  GLU A CG  1 
ATOM   995  C CG  B GLU A 1 132 ? 57.259 94.746  -13.706 0.50 26.40 ? 132  GLU A CG  1 
ATOM   996  C CD  A GLU A 1 132 ? 55.822 93.062  -15.513 0.50 28.07 ? 132  GLU A CD  1 
ATOM   997  C CD  B GLU A 1 132 ? 58.105 95.356  -12.566 0.50 26.59 ? 132  GLU A CD  1 
ATOM   998  O OE1 A GLU A 1 132 ? 55.146 94.022  -15.978 0.50 28.76 ? 132  GLU A OE1 1 
ATOM   999  O OE1 B GLU A 1 132 ? 57.773 95.211  -11.358 0.50 21.96 ? 132  GLU A OE1 1 
ATOM   1000 O OE2 A GLU A 1 132 ? 56.420 92.226  -16.214 0.50 26.01 ? 132  GLU A OE2 1 
ATOM   1001 O OE2 B GLU A 1 132 ? 59.133 95.999  -12.905 0.50 28.42 ? 132  GLU A OE2 1 
ATOM   1002 N N   . ILE A 1 133 ? 52.641 93.869  -13.873 1.00 26.08 ? 133  ILE A N   1 
ATOM   1003 C CA  . ILE A 1 133 ? 51.460 93.014  -13.773 1.00 26.08 ? 133  ILE A CA  1 
ATOM   1004 C C   . ILE A 1 133 ? 51.548 91.890  -14.808 1.00 27.53 ? 133  ILE A C   1 
ATOM   1005 O O   . ILE A 1 133 ? 51.739 92.150  -16.002 1.00 27.33 ? 133  ILE A O   1 
ATOM   1006 C CB  . ILE A 1 133 ? 50.161 93.829  -14.013 1.00 26.46 ? 133  ILE A CB  1 
ATOM   1007 C CG1 . ILE A 1 133 ? 50.045 94.981  -12.987 1.00 26.89 ? 133  ILE A CG1 1 
ATOM   1008 C CG2 . ILE A 1 133 ? 48.899 92.908  -14.030 1.00 23.12 ? 133  ILE A CG2 1 
ATOM   1009 C CD1 . ILE A 1 133 ? 49.721 94.546  -11.560 1.00 26.10 ? 133  ILE A CD1 1 
ATOM   1010 N N   . SER A 1 134 ? 51.421 90.648  -14.345 1.00 28.37 ? 134  SER A N   1 
ATOM   1011 C CA  . SER A 1 134 ? 51.280 89.502  -15.226 1.00 29.24 ? 134  SER A CA  1 
ATOM   1012 C C   . SER A 1 134 ? 49.839 89.091  -15.363 1.00 29.55 ? 134  SER A C   1 
ATOM   1013 O O   . SER A 1 134 ? 49.022 89.221  -14.430 1.00 30.09 ? 134  SER A O   1 
ATOM   1014 C CB  . SER A 1 134 ? 52.071 88.321  -14.729 1.00 29.77 ? 134  SER A CB  1 
ATOM   1015 O OG  . SER A 1 134 ? 53.398 88.707  -14.620 1.00 31.78 ? 134  SER A OG  1 
ATOM   1016 N N   . ARG A 1 135 ? 49.562 88.567  -16.543 1.00 29.84 ? 135  ARG A N   1 
ATOM   1017 C CA  . ARG A 1 135 ? 48.225 88.372  -17.083 1.00 30.59 ? 135  ARG A CA  1 
ATOM   1018 C C   . ARG A 1 135 ? 47.699 86.986  -16.695 1.00 29.62 ? 135  ARG A C   1 
ATOM   1019 O O   . ARG A 1 135 ? 46.587 86.851  -16.163 1.00 27.63 ? 135  ARG A O   1 
ATOM   1020 C CB  . ARG A 1 135 ? 48.348 88.455  -18.649 1.00 33.46 ? 135  ARG A CB  1 
ATOM   1021 C CG  . ARG A 1 135 ? 47.796 89.694  -19.411 1.00 34.68 ? 135  ARG A CG  1 
ATOM   1022 C CD  . ARG A 1 135 ? 47.695 90.963  -18.522 1.00 38.66 ? 135  ARG A CD  1 
ATOM   1023 N NE  . ARG A 1 135 ? 47.459 92.151  -19.348 1.00 47.81 ? 135  ARG A NE  1 
ATOM   1024 C CZ  . ARG A 1 135 ? 46.382 92.383  -20.111 1.00 50.30 ? 135  ARG A CZ  1 
ATOM   1025 N NH1 . ARG A 1 135 ? 45.357 91.512  -20.180 1.00 52.52 ? 135  ARG A NH1 1 
ATOM   1026 N NH2 . ARG A 1 135 ? 46.337 93.495  -20.830 1.00 51.56 ? 135  ARG A NH2 1 
ATOM   1027 N N   . GLN A 1 136 ? 48.534 85.975  -16.962 1.00 28.98 ? 136  GLN A N   1 
ATOM   1028 C CA  . GLN A 1 136 ? 48.131 84.563  -17.014 1.00 30.28 ? 136  GLN A CA  1 
ATOM   1029 C C   . GLN A 1 136 ? 49.146 83.624  -16.337 1.00 29.19 ? 136  GLN A C   1 
ATOM   1030 O O   . GLN A 1 136 ? 50.100 83.154  -16.964 1.00 29.75 ? 136  GLN A O   1 
ATOM   1031 C CB  . GLN A 1 136 ? 47.859 84.112  -18.463 1.00 31.13 ? 136  GLN A CB  1 
ATOM   1032 C CG  . GLN A 1 136 ? 47.421 85.234  -19.472 1.00 36.10 ? 136  GLN A CG  1 
ATOM   1033 C CD  . GLN A 1 136 ? 45.917 85.538  -19.454 1.00 41.48 ? 136  GLN A CD  1 
ATOM   1034 O OE1 . GLN A 1 136 ? 45.083 84.619  -19.491 1.00 45.80 ? 136  GLN A OE1 1 
ATOM   1035 N NE2 . GLN A 1 136 ? 45.566 86.835  -19.437 1.00 39.99 ? 136  GLN A NE2 1 
ATOM   1036 N N   . PRO A 1 137 ? 48.953 83.358  -15.036 1.00 28.21 ? 137  PRO A N   1 
ATOM   1037 C CA  . PRO A 1 137 ? 47.844 83.871  -14.221 1.00 27.69 ? 137  PRO A CA  1 
ATOM   1038 C C   . PRO A 1 137 ? 48.169 85.254  -13.639 1.00 27.18 ? 137  PRO A C   1 
ATOM   1039 O O   . PRO A 1 137 ? 49.287 85.720  -13.791 1.00 26.83 ? 137  PRO A O   1 
ATOM   1040 C CB  . PRO A 1 137 ? 47.750 82.819  -13.122 1.00 27.91 ? 137  PRO A CB  1 
ATOM   1041 C CG  . PRO A 1 137 ? 49.183 82.396  -12.923 1.00 27.20 ? 137  PRO A CG  1 
ATOM   1042 C CD  . PRO A 1 137 ? 49.856 82.492  -14.260 1.00 28.00 ? 137  PRO A CD  1 
ATOM   1043 N N   . PHE A 1 138 ? 47.205 85.895  -12.997 1.00 26.25 ? 138  PHE A N   1 
ATOM   1044 C CA  . PHE A 1 138 ? 47.444 87.176  -12.367 1.00 26.22 ? 138  PHE A CA  1 
ATOM   1045 C C   . PHE A 1 138 ? 48.573 87.152  -11.324 1.00 26.50 ? 138  PHE A C   1 
ATOM   1046 O O   . PHE A 1 138 ? 48.614 86.281  -10.428 1.00 25.89 ? 138  PHE A O   1 
ATOM   1047 C CB  . PHE A 1 138 ? 46.183 87.751  -11.728 1.00 26.03 ? 138  PHE A CB  1 
ATOM   1048 C CG  . PHE A 1 138 ? 46.463 88.915  -10.795 1.00 27.26 ? 138  PHE A CG  1 
ATOM   1049 C CD1 . PHE A 1 138 ? 46.522 88.722  -9.408  1.00 25.67 ? 138  PHE A CD1 1 
ATOM   1050 C CD2 . PHE A 1 138 ? 46.714 90.190  -11.302 1.00 26.86 ? 138  PHE A CD2 1 
ATOM   1051 C CE1 . PHE A 1 138 ? 46.819 89.762  -8.565  1.00 23.93 ? 138  PHE A CE1 1 
ATOM   1052 C CE2 . PHE A 1 138 ? 47.010 91.251  -10.452 1.00 27.85 ? 138  PHE A CE2 1 
ATOM   1053 C CZ  . PHE A 1 138 ? 47.062 91.036  -9.083  1.00 25.95 ? 138  PHE A CZ  1 
ATOM   1054 N N   . SER A 1 139 ? 49.486 88.122  -11.461 1.00 25.58 ? 139  SER A N   1 
ATOM   1055 C CA  . SER A 1 139 ? 50.465 88.441  -10.421 1.00 25.05 ? 139  SER A CA  1 
ATOM   1056 C C   . SER A 1 139 ? 50.844 89.930  -10.426 1.00 24.52 ? 139  SER A C   1 
ATOM   1057 O O   . SER A 1 139 ? 50.695 90.638  -11.439 1.00 23.65 ? 139  SER A O   1 
ATOM   1058 C CB  . SER A 1 139 ? 51.692 87.504  -10.442 1.00 24.95 ? 139  SER A CB  1 
ATOM   1059 O OG  . SER A 1 139 ? 52.613 87.800  -11.476 1.00 28.02 ? 139  SER A OG  1 
ATOM   1060 N N   . ILE A 1 140 ? 51.268 90.413  -9.262  1.00 23.89 ? 140  ILE A N   1 
ATOM   1061 C CA  . ILE A 1 140 ? 51.673 91.797  -9.112  1.00 23.32 ? 140  ILE A CA  1 
ATOM   1062 C C   . ILE A 1 140 ? 53.065 91.839  -8.522  1.00 24.07 ? 140  ILE A C   1 
ATOM   1063 O O   . ILE A 1 140 ? 53.360 91.124  -7.552  1.00 23.13 ? 140  ILE A O   1 
ATOM   1064 C CB  . ILE A 1 140 ? 50.677 92.658  -8.282  1.00 23.33 ? 140  ILE A CB  1 
ATOM   1065 C CG1 . ILE A 1 140 ? 51.171 94.106  -8.204  1.00 23.35 ? 140  ILE A CG1 1 
ATOM   1066 C CG2 . ILE A 1 140 ? 50.427 92.083  -6.852  1.00 21.89 ? 140  ILE A CG2 1 
ATOM   1067 C CD1 . ILE A 1 140 ? 50.036 95.112  -8.001  1.00 24.16 ? 140  ILE A CD1 1 
ATOM   1068 N N   . LYS A 1 141 ? 53.911 92.670  -9.125  1.00 24.00 ? 141  LYS A N   1 
ATOM   1069 C CA  . LYS A 1 141 ? 55.307 92.781  -8.717  1.00 25.71 ? 141  LYS A CA  1 
ATOM   1070 C C   . LYS A 1 141 ? 55.669 94.271  -8.523  1.00 24.42 ? 141  LYS A C   1 
ATOM   1071 O O   . LYS A 1 141 ? 55.256 95.119  -9.313  1.00 24.62 ? 141  LYS A O   1 
ATOM   1072 C CB  . LYS A 1 141 ? 56.170 92.095  -9.778  1.00 25.37 ? 141  LYS A CB  1 
ATOM   1073 C CG  . LYS A 1 141 ? 57.632 91.957  -9.469  1.00 29.29 ? 141  LYS A CG  1 
ATOM   1074 C CD  . LYS A 1 141 ? 58.445 91.570  -10.741 1.00 29.44 ? 141  LYS A CD  1 
ATOM   1075 C CE  . LYS A 1 141 ? 58.114 90.156  -11.255 1.00 37.65 ? 141  LYS A CE  1 
ATOM   1076 N NZ  . LYS A 1 141 ? 59.195 89.675  -12.218 1.00 41.03 ? 141  LYS A NZ  1 
ATOM   1077 N N   . VAL A 1 142 ? 56.356 94.584  -7.431  1.00 22.62 ? 142  VAL A N   1 
ATOM   1078 C CA  . VAL A 1 142 ? 56.862 95.938  -7.154  1.00 21.28 ? 142  VAL A CA  1 
ATOM   1079 C C   . VAL A 1 142 ? 58.367 95.811  -7.039  1.00 21.47 ? 142  VAL A C   1 
ATOM   1080 O O   . VAL A 1 142 ? 58.863 95.041  -6.214  1.00 21.54 ? 142  VAL A O   1 
ATOM   1081 C CB  . VAL A 1 142 ? 56.270 96.561  -5.856  1.00 20.65 ? 142  VAL A CB  1 
ATOM   1082 C CG1 . VAL A 1 142 ? 56.877 97.929  -5.578  1.00 19.65 ? 142  VAL A CG1 1 
ATOM   1083 C CG2 . VAL A 1 142 ? 54.744 96.684  -5.977  1.00 19.94 ? 142  VAL A CG2 1 
ATOM   1084 N N   . THR A 1 143 ? 59.097 96.518  -7.899  1.00 21.42 ? 143  THR A N   1 
ATOM   1085 C CA  . THR A 1 143 ? 60.539 96.408  -7.866  1.00 21.99 ? 143  THR A CA  1 
ATOM   1086 C C   . THR A 1 143 ? 61.176 97.775  -7.589  1.00 21.41 ? 143  THR A C   1 
ATOM   1087 O O   . THR A 1 143 ? 60.626 98.828  -7.923  1.00 22.29 ? 143  THR A O   1 
ATOM   1088 C CB  . THR A 1 143 ? 61.114 95.725  -9.156  1.00 22.44 ? 143  THR A CB  1 
ATOM   1089 O OG1 . THR A 1 143 ? 61.103 96.659  -10.219 1.00 26.23 ? 143  THR A OG1 1 
ATOM   1090 C CG2 . THR A 1 143 ? 60.264 94.542  -9.579  1.00 20.41 ? 143  THR A CG2 1 
ATOM   1091 N N   . ARG A 1 144 ? 62.351 97.761  -6.995  1.00 20.48 ? 144  ARG A N   1 
ATOM   1092 C CA  . ARG A 1 144 ? 63.057 99.001  -6.710  1.00 19.30 ? 144  ARG A CA  1 
ATOM   1093 C C   . ARG A 1 144 ? 63.713 99.461  -8.031  1.00 20.12 ? 144  ARG A C   1 
ATOM   1094 O O   . ARG A 1 144 ? 64.460 98.715  -8.641  1.00 19.50 ? 144  ARG A O   1 
ATOM   1095 C CB  . ARG A 1 144 ? 64.094 98.741  -5.617  1.00 17.89 ? 144  ARG A CB  1 
ATOM   1096 C CG  . ARG A 1 144 ? 64.919 99.963  -5.205  1.00 17.97 ? 144  ARG A CG  1 
ATOM   1097 C CD  . ARG A 1 144 ? 65.872 99.631  -4.084  1.00 17.51 ? 144  ARG A CD  1 
ATOM   1098 N NE  . ARG A 1 144 ? 65.190 99.542  -2.804  1.00 18.40 ? 144  ARG A NE  1 
ATOM   1099 C CZ  . ARG A 1 144 ? 64.768 100.586 -2.090  1.00 18.05 ? 144  ARG A CZ  1 
ATOM   1100 N NH1 . ARG A 1 144 ? 64.933 101.846 -2.512  1.00 18.19 ? 144  ARG A NH1 1 
ATOM   1101 N NH2 . ARG A 1 144 ? 64.179 100.367 -0.932  1.00 16.24 ? 144  ARG A NH2 1 
ATOM   1102 N N   . ARG A 1 145 ? 63.413 100.667 -8.477  1.00 21.07 ? 145  ARG A N   1 
ATOM   1103 C CA  . ARG A 1 145 ? 63.943 101.148 -9.763  1.00 23.76 ? 145  ARG A CA  1 
ATOM   1104 C C   . ARG A 1 145 ? 65.465 101.140 -9.891  1.00 23.74 ? 145  ARG A C   1 
ATOM   1105 O O   . ARG A 1 145 ? 65.978 100.808 -10.953 1.00 25.15 ? 145  ARG A O   1 
ATOM   1106 C CB  . ARG A 1 145 ? 63.473 102.570 -10.049 1.00 23.66 ? 145  ARG A CB  1 
ATOM   1107 C CG  . ARG A 1 145 ? 62.681 102.708 -11.294 1.00 30.69 ? 145  ARG A CG  1 
ATOM   1108 C CD  . ARG A 1 145 ? 62.128 104.104 -11.477 1.00 37.84 ? 145  ARG A CD  1 
ATOM   1109 N NE  . ARG A 1 145 ? 63.138 104.952 -12.098 1.00 45.26 ? 145  ARG A NE  1 
ATOM   1110 C CZ  . ARG A 1 145 ? 63.049 106.271 -12.243 1.00 48.63 ? 145  ARG A CZ  1 
ATOM   1111 N NH1 . ARG A 1 145 ? 61.985 106.940 -11.790 1.00 49.29 ? 145  ARG A NH1 1 
ATOM   1112 N NH2 . ARG A 1 145 ? 64.043 106.925 -12.842 1.00 51.18 ? 145  ARG A NH2 1 
ATOM   1113 N N   . SER A 1 146 ? 66.175 101.536 -8.836  1.00 23.80 ? 146  SER A N   1 
ATOM   1114 C CA  . SER A 1 146 ? 67.604 101.823 -8.966  1.00 25.26 ? 146  SER A CA  1 
ATOM   1115 C C   . SER A 1 146 ? 68.433 100.569 -9.182  1.00 25.20 ? 146  SER A C   1 
ATOM   1116 O O   . SER A 1 146 ? 69.440 100.583 -9.933  1.00 26.89 ? 146  SER A O   1 
ATOM   1117 C CB  . SER A 1 146 ? 68.136 102.574 -7.733  1.00 25.68 ? 146  SER A CB  1 
ATOM   1118 O OG  . SER A 1 146 ? 67.982 101.807 -6.535  1.00 25.54 ? 146  SER A OG  1 
ATOM   1119 N N   . ASN A 1 147 ? 68.043 99.489  -8.516  1.00 23.08 ? 147  ASN A N   1 
ATOM   1120 C CA  . ASN A 1 147 ? 68.737 98.234  -8.703  1.00 21.70 ? 147  ASN A CA  1 
ATOM   1121 C C   . ASN A 1 147 ? 67.850 97.088  -9.262  1.00 20.89 ? 147  ASN A C   1 
ATOM   1122 O O   . ASN A 1 147 ? 68.287 95.969  -9.351  1.00 21.17 ? 147  ASN A O   1 
ATOM   1123 C CB  . ASN A 1 147 ? 69.481 97.830  -7.419  1.00 21.24 ? 147  ASN A CB  1 
ATOM   1124 C CG  . ASN A 1 147 ? 68.567 97.675  -6.222  1.00 21.85 ? 147  ASN A CG  1 
ATOM   1125 O OD1 . ASN A 1 147 ? 67.356 97.852  -6.318  1.00 21.36 ? 147  ASN A OD1 1 
ATOM   1126 N ND2 . ASN A 1 147 ? 69.143 97.337  -5.089  1.00 16.84 ? 147  ASN A ND2 1 
ATOM   1127 N N   . ASN A 1 148 ? 66.617 97.387  -9.648  1.00 20.28 ? 148  ASN A N   1 
ATOM   1128 C CA  . ASN A 1 148 ? 65.634 96.341  -10.042 1.00 20.00 ? 148  ASN A CA  1 
ATOM   1129 C C   . ASN A 1 148 ? 65.426 95.193  -9.022  1.00 19.87 ? 148  ASN A C   1 
ATOM   1130 O O   . ASN A 1 148 ? 65.050 94.074  -9.406  1.00 19.45 ? 148  ASN A O   1 
ATOM   1131 C CB  . ASN A 1 148 ? 65.975 95.771  -11.439 1.00 20.54 ? 148  ASN A CB  1 
ATOM   1132 C CG  . ASN A 1 148 ? 65.775 96.792  -12.541 1.00 21.03 ? 148  ASN A CG  1 
ATOM   1133 O OD1 . ASN A 1 148 ? 66.293 96.644  -13.646 1.00 26.18 ? 148  ASN A OD1 1 
ATOM   1134 N ND2 . ASN A 1 148 ? 64.988 97.811  -12.259 1.00 19.76 ? 148  ASN A ND2 1 
ATOM   1135 N N   . ARG A 1 149 ? 65.666 95.473  -7.745  1.00 19.10 ? 149  ARG A N   1 
ATOM   1136 C CA  . ARG A 1 149 ? 65.438 94.483  -6.686  1.00 19.84 ? 149  ARG A CA  1 
ATOM   1137 C C   . ARG A 1 149 ? 63.937 94.228  -6.628  1.00 19.77 ? 149  ARG A C   1 
ATOM   1138 O O   . ARG A 1 149 ? 63.146 95.163  -6.489  1.00 18.41 ? 149  ARG A O   1 
ATOM   1139 C CB  . ARG A 1 149 ? 65.898 95.003  -5.333  1.00 19.93 ? 149  ARG A CB  1 
ATOM   1140 C CG  . ARG A 1 149 ? 65.723 94.040  -4.173  1.00 23.19 ? 149  ARG A CG  1 
ATOM   1141 C CD  . ARG A 1 149 ? 66.893 93.048  -4.108  1.00 25.05 ? 149  ARG A CD  1 
ATOM   1142 N NE  . ARG A 1 149 ? 68.084 93.675  -3.541  1.00 29.72 ? 149  ARG A NE  1 
ATOM   1143 C CZ  . ARG A 1 149 ? 69.306 93.151  -3.643  1.00 33.92 ? 149  ARG A CZ  1 
ATOM   1144 N NH1 . ARG A 1 149 ? 69.488 91.999  -4.300  1.00 33.51 ? 149  ARG A NH1 1 
ATOM   1145 N NH2 . ARG A 1 149 ? 70.347 93.773  -3.103  1.00 32.20 ? 149  ARG A NH2 1 
ATOM   1146 N N   . VAL A 1 150 ? 63.562 92.963  -6.767  1.00 19.21 ? 150  VAL A N   1 
ATOM   1147 C CA  . VAL A 1 150 ? 62.190 92.590  -6.613  1.00 19.92 ? 150  VAL A CA  1 
ATOM   1148 C C   . VAL A 1 150 ? 61.832 92.616  -5.131  1.00 19.27 ? 150  VAL A C   1 
ATOM   1149 O O   . VAL A 1 150 ? 62.406 91.865  -4.329  1.00 17.32 ? 150  VAL A O   1 
ATOM   1150 C CB  . VAL A 1 150 ? 61.889 91.220  -7.246  1.00 20.68 ? 150  VAL A CB  1 
ATOM   1151 C CG1 . VAL A 1 150 ? 60.355 90.913  -7.109  1.00 19.80 ? 150  VAL A CG1 1 
ATOM   1152 C CG2 . VAL A 1 150 ? 62.312 91.240  -8.715  1.00 21.37 ? 150  VAL A CG2 1 
ATOM   1153 N N   . LEU A 1 151 ? 60.878 93.482  -4.791  1.00 18.81 ? 151  LEU A N   1 
ATOM   1154 C CA  . LEU A 1 151 ? 60.462 93.673  -3.395  1.00 18.70 ? 151  LEU A CA  1 
ATOM   1155 C C   . LEU A 1 151 ? 59.185 92.859  -3.020  1.00 19.60 ? 151  LEU A C   1 
ATOM   1156 O O   . LEU A 1 151 ? 59.228 91.994  -2.149  1.00 19.21 ? 151  LEU A O   1 
ATOM   1157 C CB  . LEU A 1 151 ? 60.243 95.172  -3.134  1.00 17.81 ? 151  LEU A CB  1 
ATOM   1158 C CG  . LEU A 1 151 ? 61.441 96.070  -3.507  1.00 17.52 ? 151  LEU A CG  1 
ATOM   1159 C CD1 . LEU A 1 151 ? 61.195 97.466  -3.041  1.00 13.78 ? 151  LEU A CD1 1 
ATOM   1160 C CD2 . LEU A 1 151 ? 62.673 95.523  -2.825  1.00 12.90 ? 151  LEU A CD2 1 
ATOM   1161 N N   . PHE A 1 152 ? 58.069 93.197  -3.662  1.00 19.86 ? 152  PHE A N   1 
ATOM   1162 C CA  . PHE A 1 152 ? 56.778 92.497  -3.534  1.00 21.10 ? 152  PHE A CA  1 
ATOM   1163 C C   . PHE A 1 152 ? 56.682 91.686  -4.826  1.00 21.77 ? 152  PHE A C   1 
ATOM   1164 O O   . PHE A 1 152 ? 56.932 92.226  -5.893  1.00 21.15 ? 152  PHE A O   1 
ATOM   1165 C CB  . PHE A 1 152 ? 55.606 93.507  -3.509  1.00 20.69 ? 152  PHE A CB  1 
ATOM   1166 C CG  . PHE A 1 152 ? 54.297 92.937  -2.951  1.00 22.72 ? 152  PHE A CG  1 
ATOM   1167 C CD1 . PHE A 1 152 ? 53.959 93.113  -1.602  1.00 20.24 ? 152  PHE A CD1 1 
ATOM   1168 C CD2 . PHE A 1 152 ? 53.422 92.202  -3.767  1.00 24.12 ? 152  PHE A CD2 1 
ATOM   1169 C CE1 . PHE A 1 152 ? 52.741 92.595  -1.075  1.00 22.90 ? 152  PHE A CE1 1 
ATOM   1170 C CE2 . PHE A 1 152 ? 52.221 91.644  -3.230  1.00 22.79 ? 152  PHE A CE2 1 
ATOM   1171 C CZ  . PHE A 1 152 ? 51.896 91.835  -1.880  1.00 20.93 ? 152  PHE A CZ  1 
ATOM   1172 N N   . ASP A 1 153 ? 56.333 90.407  -4.737  1.00 22.36 ? 153  ASP A N   1 
ATOM   1173 C CA  . ASP A 1 153 ? 56.063 89.602  -5.920  1.00 22.68 ? 153  ASP A CA  1 
ATOM   1174 C C   . ASP A 1 153 ? 55.039 88.507  -5.594  1.00 21.83 ? 153  ASP A C   1 
ATOM   1175 O O   . ASP A 1 153 ? 55.387 87.491  -5.020  1.00 22.58 ? 153  ASP A O   1 
ATOM   1176 C CB  . ASP A 1 153 ? 57.352 88.967  -6.450  1.00 23.53 ? 153  ASP A CB  1 
ATOM   1177 C CG  . ASP A 1 153 ? 57.089 88.022  -7.625  1.00 26.98 ? 153  ASP A CG  1 
ATOM   1178 O OD1 . ASP A 1 153 ? 55.927 87.957  -8.116  1.00 29.43 ? 153  ASP A OD1 1 
ATOM   1179 O OD2 . ASP A 1 153 ? 58.032 87.328  -8.055  1.00 31.27 ? 153  ASP A OD2 1 
ATOM   1180 N N   . SER A 1 154 ? 53.790 88.704  -5.975  1.00 21.04 ? 154  SER A N   1 
ATOM   1181 C CA  . SER A 1 154 ? 52.740 87.745  -5.634  1.00 21.41 ? 154  SER A CA  1 
ATOM   1182 C C   . SER A 1 154 ? 52.764 86.445  -6.433  1.00 21.29 ? 154  SER A C   1 
ATOM   1183 O O   . SER A 1 154 ? 52.012 85.521  -6.122  1.00 21.39 ? 154  SER A O   1 
ATOM   1184 C CB  . SER A 1 154 ? 51.363 88.422  -5.715  1.00 20.46 ? 154  SER A CB  1 
ATOM   1185 O OG  . SER A 1 154 ? 50.909 88.495  -7.060  1.00 21.17 ? 154  SER A OG  1 
ATOM   1186 N N   . SER A 1 155 ? 53.651 86.338  -7.429  1.00 23.31 ? 155  SER A N   1 
ATOM   1187 C CA  . SER A 1 155 ? 53.629 85.191  -8.389  1.00 22.97 ? 155  SER A CA  1 
ATOM   1188 C C   . SER A 1 155 ? 53.945 83.853  -7.743  1.00 22.31 ? 155  SER A C   1 
ATOM   1189 O O   . SER A 1 155 ? 53.785 82.814  -8.365  1.00 22.54 ? 155  SER A O   1 
ATOM   1190 C CB  . SER A 1 155 ? 54.570 85.437  -9.592  1.00 23.45 ? 155  SER A CB  1 
ATOM   1191 O OG  . SER A 1 155 ? 55.927 85.188  -9.225  1.00 24.93 ? 155  SER A OG  1 
ATOM   1192 N N   . ILE A 1 156 ? 54.398 83.863  -6.494  1.00 21.44 ? 156  ILE A N   1 
ATOM   1193 C CA  . ILE A 1 156 ? 54.637 82.601  -5.784  1.00 20.88 ? 156  ILE A CA  1 
ATOM   1194 C C   . ILE A 1 156 ? 53.328 81.811  -5.508  1.00 21.19 ? 156  ILE A C   1 
ATOM   1195 O O   . ILE A 1 156 ? 53.354 80.607  -5.389  1.00 19.90 ? 156  ILE A O   1 
ATOM   1196 C CB  . ILE A 1 156 ? 55.479 82.802  -4.475  1.00 20.80 ? 156  ILE A CB  1 
ATOM   1197 C CG1 . ILE A 1 156 ? 55.976 81.471  -3.907  1.00 21.55 ? 156  ILE A CG1 1 
ATOM   1198 C CG2 . ILE A 1 156 ? 54.749 83.681  -3.435  1.00 19.63 ? 156  ILE A CG2 1 
ATOM   1199 C CD1 . ILE A 1 156 ? 57.084 81.658  -2.855  1.00 21.35 ? 156  ILE A CD1 1 
ATOM   1200 N N   . GLY A 1 157 ? 52.194 82.492  -5.452  1.00 20.83 ? 157  GLY A N   1 
ATOM   1201 C CA  . GLY A 1 157 ? 50.960 81.828  -5.034  1.00 21.01 ? 157  GLY A CA  1 
ATOM   1202 C C   . GLY A 1 157 ? 49.792 82.428  -5.750  1.00 21.16 ? 157  GLY A C   1 
ATOM   1203 O O   . GLY A 1 157 ? 49.963 83.385  -6.518  1.00 20.32 ? 157  GLY A O   1 
ATOM   1204 N N   . PRO A 1 158 ? 48.581 81.876  -5.498  1.00 21.64 ? 158  PRO A N   1 
ATOM   1205 C CA  . PRO A 1 158 ? 47.373 82.397  -6.111  1.00 21.38 ? 158  PRO A CA  1 
ATOM   1206 C C   . PRO A 1 158 ? 46.883 83.668  -5.409  1.00 21.33 ? 158  PRO A C   1 
ATOM   1207 O O   . PRO A 1 158 ? 47.344 83.993  -4.329  1.00 22.35 ? 158  PRO A O   1 
ATOM   1208 C CB  . PRO A 1 158 ? 46.357 81.262  -5.888  1.00 21.39 ? 158  PRO A CB  1 
ATOM   1209 C CG  . PRO A 1 158 ? 46.798 80.623  -4.620  1.00 22.12 ? 158  PRO A CG  1 
ATOM   1210 C CD  . PRO A 1 158 ? 48.306 80.759  -4.567  1.00 21.76 ? 158  PRO A CD  1 
ATOM   1211 N N   . LEU A 1 159 ? 45.962 84.378  -6.042  1.00 20.83 ? 159  LEU A N   1 
ATOM   1212 C CA  . LEU A 1 159 ? 45.113 85.315  -5.369  1.00 21.11 ? 159  LEU A CA  1 
ATOM   1213 C C   . LEU A 1 159 ? 43.877 84.464  -5.057  1.00 21.64 ? 159  LEU A C   1 
ATOM   1214 O O   . LEU A 1 159 ? 43.359 83.792  -5.953  1.00 22.14 ? 159  LEU A O   1 
ATOM   1215 C CB  . LEU A 1 159 ? 44.734 86.465  -6.311  1.00 20.87 ? 159  LEU A CB  1 
ATOM   1216 C CG  . LEU A 1 159 ? 43.483 87.293  -5.958  1.00 20.95 ? 159  LEU A CG  1 
ATOM   1217 C CD1 . LEU A 1 159 ? 43.565 88.023  -4.620  1.00 18.69 ? 159  LEU A CD1 1 
ATOM   1218 C CD2 . LEU A 1 159 ? 43.168 88.278  -7.030  1.00 20.73 ? 159  LEU A CD2 1 
ATOM   1219 N N   . LEU A 1 160 ? 43.434 84.439  -3.803  1.00 21.70 ? 160  LEU A N   1 
ATOM   1220 C CA  . LEU A 1 160 ? 42.167 83.759  -3.446  1.00 21.93 ? 160  LEU A CA  1 
ATOM   1221 C C   . LEU A 1 160 ? 41.296 84.866  -2.900  1.00 22.05 ? 160  LEU A C   1 
ATOM   1222 O O   . LEU A 1 160 ? 41.783 85.750  -2.183  1.00 21.18 ? 160  LEU A O   1 
ATOM   1223 C CB  . LEU A 1 160 ? 42.403 82.646  -2.423  1.00 21.71 ? 160  LEU A CB  1 
ATOM   1224 C CG  . LEU A 1 160 ? 43.490 81.683  -2.922  1.00 22.95 ? 160  LEU A CG  1 
ATOM   1225 C CD1 . LEU A 1 160 ? 43.954 80.782  -1.837  1.00 23.78 ? 160  LEU A CD1 1 
ATOM   1226 C CD2 . LEU A 1 160 ? 43.048 80.861  -4.154  1.00 22.84 ? 160  LEU A CD2 1 
ATOM   1227 N N   . PHE A 1 161 ? 40.027 84.864  -3.285  1.00 22.54 ? 161  PHE A N   1 
ATOM   1228 C CA  . PHE A 1 161 ? 39.116 85.951  -2.961  1.00 23.45 ? 161  PHE A CA  1 
ATOM   1229 C C   . PHE A 1 161 ? 37.699 85.352  -2.865  1.00 23.91 ? 161  PHE A C   1 
ATOM   1230 O O   . PHE A 1 161 ? 36.911 85.532  -3.795  1.00 24.43 ? 161  PHE A O   1 
ATOM   1231 C CB  . PHE A 1 161 ? 39.190 87.027  -4.078  1.00 23.88 ? 161  PHE A CB  1 
ATOM   1232 C CG  . PHE A 1 161 ? 38.852 88.422  -3.623  1.00 25.38 ? 161  PHE A CG  1 
ATOM   1233 C CD1 . PHE A 1 161 ? 39.858 89.378  -3.451  1.00 28.91 ? 161  PHE A CD1 1 
ATOM   1234 C CD2 . PHE A 1 161 ? 37.552 88.785  -3.330  1.00 28.72 ? 161  PHE A CD2 1 
ATOM   1235 C CE1 . PHE A 1 161 ? 39.554 90.677  -2.998  1.00 30.12 ? 161  PHE A CE1 1 
ATOM   1236 C CE2 . PHE A 1 161 ? 37.237 90.075  -2.887  1.00 27.83 ? 161  PHE A CE2 1 
ATOM   1237 C CZ  . PHE A 1 161 ? 38.233 91.016  -2.737  1.00 28.03 ? 161  PHE A CZ  1 
ATOM   1238 N N   . ALA A 1 162 ? 37.394 84.622  -1.785  1.00 23.02 ? 162  ALA A N   1 
ATOM   1239 C CA  . ALA A 1 162 ? 35.987 84.233  -1.453  1.00 23.65 ? 162  ALA A CA  1 
ATOM   1240 C C   . ALA A 1 162 ? 35.450 85.144  -0.329  1.00 23.57 ? 162  ALA A C   1 
ATOM   1241 O O   . ALA A 1 162 ? 36.239 85.865  0.294   1.00 23.61 ? 162  ALA A O   1 
ATOM   1242 C CB  . ALA A 1 162 ? 35.893 82.760  -1.047  1.00 23.27 ? 162  ALA A CB  1 
ATOM   1243 N N   . ASP A 1 163 ? 34.140 85.125  -0.067  1.00 22.63 ? 163  ASP A N   1 
ATOM   1244 C CA  . ASP A 1 163 ? 33.532 86.070  0.872   1.00 23.00 ? 163  ASP A CA  1 
ATOM   1245 C C   . ASP A 1 163 ? 34.224 86.022  2.237   1.00 22.20 ? 163  ASP A C   1 
ATOM   1246 O O   . ASP A 1 163 ? 34.358 87.043  2.895   1.00 22.67 ? 163  ASP A O   1 
ATOM   1247 C CB  . ASP A 1 163 ? 32.026 85.791  1.011   1.00 24.60 ? 163  ASP A CB  1 
ATOM   1248 C CG  . ASP A 1 163 ? 31.283 86.848  1.841   1.00 29.20 ? 163  ASP A CG  1 
ATOM   1249 O OD1 . ASP A 1 163 ? 31.547 88.076  1.664   1.00 32.16 ? 163  ASP A OD1 1 
ATOM   1250 O OD2 . ASP A 1 163 ? 30.404 86.440  2.665   1.00 32.56 ? 163  ASP A OD2 1 
ATOM   1251 N N   . GLN A 1 164 ? 34.693 84.842  2.640   1.00 21.23 ? 164  GLN A N   1 
ATOM   1252 C CA  . GLN A 1 164 ? 35.254 84.635  3.973   1.00 20.16 ? 164  GLN A CA  1 
ATOM   1253 C C   . GLN A 1 164 ? 36.589 83.915  3.919   1.00 19.66 ? 164  GLN A C   1 
ATOM   1254 O O   . GLN A 1 164 ? 36.964 83.195  4.865   1.00 19.84 ? 164  GLN A O   1 
ATOM   1255 C CB  . GLN A 1 164 ? 34.244 83.837  4.846   1.00 20.28 ? 164  GLN A CB  1 
ATOM   1256 C CG  . GLN A 1 164 ? 33.005 84.621  5.151   1.00 19.36 ? 164  GLN A CG  1 
ATOM   1257 C CD  . GLN A 1 164 ? 32.086 83.883  6.079   1.00 22.81 ? 164  GLN A CD  1 
ATOM   1258 O OE1 . GLN A 1 164 ? 32.285 83.861  7.310   1.00 22.90 ? 164  GLN A OE1 1 
ATOM   1259 N NE2 . GLN A 1 164 ? 31.070 83.263  5.503   1.00 20.69 ? 164  GLN A NE2 1 
ATOM   1260 N N   . PHE A 1 165 ? 37.303 84.094  2.817   1.00 19.63 ? 165  PHE A N   1 
ATOM   1261 C CA  . PHE A 1 165 ? 38.631 83.539  2.665   1.00 20.14 ? 165  PHE A CA  1 
ATOM   1262 C C   . PHE A 1 165 ? 39.371 84.234  1.527   1.00 20.23 ? 165  PHE A C   1 
ATOM   1263 O O   . PHE A 1 165 ? 39.046 84.038  0.347   1.00 20.03 ? 165  PHE A O   1 
ATOM   1264 C CB  . PHE A 1 165 ? 38.620 82.023  2.444   1.00 20.24 ? 165  PHE A CB  1 
ATOM   1265 C CG  . PHE A 1 165 ? 39.977 81.393  2.581   1.00 21.18 ? 165  PHE A CG  1 
ATOM   1266 C CD1 . PHE A 1 165 ? 40.423 80.941  3.812   1.00 21.53 ? 165  PHE A CD1 1 
ATOM   1267 C CD2 . PHE A 1 165 ? 40.829 81.289  1.474   1.00 23.55 ? 165  PHE A CD2 1 
ATOM   1268 C CE1 . PHE A 1 165 ? 41.678 80.351  3.939   1.00 22.62 ? 165  PHE A CE1 1 
ATOM   1269 C CE2 . PHE A 1 165 ? 42.078 80.712  1.583   1.00 22.87 ? 165  PHE A CE2 1 
ATOM   1270 C CZ  . PHE A 1 165 ? 42.510 80.236  2.825   1.00 24.11 ? 165  PHE A CZ  1 
ATOM   1271 N N   . LEU A 1 166 ? 40.340 85.080  1.911   1.00 19.21 ? 166  LEU A N   1 
ATOM   1272 C CA  . LEU A 1 166 ? 41.083 85.918  0.971   1.00 18.49 ? 166  LEU A CA  1 
ATOM   1273 C C   . LEU A 1 166 ? 42.541 85.698  1.262   1.00 18.22 ? 166  LEU A C   1 
ATOM   1274 O O   . LEU A 1 166 ? 42.940 85.665  2.415   1.00 19.25 ? 166  LEU A O   1 
ATOM   1275 C CB  . LEU A 1 166 ? 40.745 87.398  1.114   1.00 17.10 ? 166  LEU A CB  1 
ATOM   1276 C CG  . LEU A 1 166 ? 39.314 87.851  0.856   1.00 20.38 ? 166  LEU A CG  1 
ATOM   1277 C CD1 . LEU A 1 166 ? 38.492 87.763  2.133   1.00 18.07 ? 166  LEU A CD1 1 
ATOM   1278 C CD2 . LEU A 1 166 ? 39.367 89.272  0.393   1.00 18.59 ? 166  LEU A CD2 1 
ATOM   1279 N N   . GLN A 1 167 ? 43.342 85.513  0.229   1.00 18.24 ? 167  GLN A N   1 
ATOM   1280 C CA  . GLN A 1 167 ? 44.738 85.231  0.444   1.00 17.79 ? 167  GLN A CA  1 
ATOM   1281 C C   . GLN A 1 167 ? 45.560 85.828  -0.701  1.00 18.03 ? 167  GLN A C   1 
ATOM   1282 O O   . GLN A 1 167 ? 45.131 85.763  -1.852  1.00 17.20 ? 167  GLN A O   1 
ATOM   1283 C CB  . GLN A 1 167 ? 44.948 83.717  0.511   1.00 17.98 ? 167  GLN A CB  1 
ATOM   1284 C CG  . GLN A 1 167 ? 46.345 83.282  0.922   1.00 17.37 ? 167  GLN A CG  1 
ATOM   1285 C CD  . GLN A 1 167 ? 46.510 81.776  1.077   1.00 18.81 ? 167  GLN A CD  1 
ATOM   1286 O OE1 . GLN A 1 167 ? 47.248 81.139  0.331   1.00 25.91 ? 167  GLN A OE1 1 
ATOM   1287 N NE2 . GLN A 1 167 ? 45.837 81.211  2.023   1.00 22.37 ? 167  GLN A NE2 1 
ATOM   1288 N N   . LEU A 1 168 ? 46.740 86.376  -0.371  1.00 17.25 ? 168  LEU A N   1 
ATOM   1289 C CA  . LEU A 1 168 ? 47.753 86.828  -1.334  1.00 17.41 ? 168  LEU A CA  1 
ATOM   1290 C C   . LEU A 1 168 ? 49.126 86.625  -0.683  1.00 18.09 ? 168  LEU A C   1 
ATOM   1291 O O   . LEU A 1 168 ? 49.260 86.860  0.504   1.00 18.18 ? 168  LEU A O   1 
ATOM   1292 C CB  . LEU A 1 168 ? 47.563 88.299  -1.739  1.00 16.95 ? 168  LEU A CB  1 
ATOM   1293 C CG  . LEU A 1 168 ? 48.302 88.788  -3.014  1.00 17.71 ? 168  LEU A CG  1 
ATOM   1294 C CD1 . LEU A 1 168 ? 47.728 88.171  -4.323  1.00 14.86 ? 168  LEU A CD1 1 
ATOM   1295 C CD2 . LEU A 1 168 ? 48.248 90.295  -3.039  1.00 18.33 ? 168  LEU A CD2 1 
ATOM   1296 N N   . SER A 1 169 ? 50.094 86.096  -1.436  1.00 18.34 ? 169  SER A N   1 
ATOM   1297 C CA  . SER A 1 169 ? 51.470 85.859  -0.948  1.00 19.07 ? 169  SER A CA  1 
ATOM   1298 C C   . SER A 1 169 ? 52.428 86.853  -1.616  1.00 19.73 ? 169  SER A C   1 
ATOM   1299 O O   . SER A 1 169 ? 52.035 87.533  -2.568  1.00 19.19 ? 169  SER A O   1 
ATOM   1300 C CB  . SER A 1 169 ? 51.945 84.456  -1.290  1.00 19.35 ? 169  SER A CB  1 
ATOM   1301 O OG  . SER A 1 169 ? 50.960 83.490  -0.998  1.00 20.01 ? 169  SER A OG  1 
ATOM   1302 N N   . THR A 1 170 ? 53.638 87.001  -1.069  1.00 19.11 ? 170  THR A N   1 
ATOM   1303 C CA  . THR A 1 170 ? 54.713 87.700  -1.775  1.00 20.13 ? 170  THR A CA  1 
ATOM   1304 C C   . THR A 1 170 ? 56.073 87.084  -1.471  1.00 19.34 ? 170  THR A C   1 
ATOM   1305 O O   . THR A 1 170 ? 56.351 86.758  -0.322  1.00 19.07 ? 170  THR A O   1 
ATOM   1306 C CB  . THR A 1 170 ? 54.779 89.243  -1.438  1.00 20.56 ? 170  THR A CB  1 
ATOM   1307 O OG1 . THR A 1 170 ? 55.999 89.780  -1.953  1.00 19.51 ? 170  THR A OG1 1 
ATOM   1308 C CG2 . THR A 1 170 ? 54.765 89.535  0.079   1.00 21.28 ? 170  THR A CG2 1 
ATOM   1309 N N   . ARG A 1 171 ? 56.932 86.936  -2.475  1.00 19.97 ? 171  ARG A N   1 
ATOM   1310 C CA  . ARG A 1 171 ? 58.316 86.571  -2.198  1.00 20.36 ? 171  ARG A CA  1 
ATOM   1311 C C   . ARG A 1 171 ? 58.926 87.765  -1.497  1.00 20.10 ? 171  ARG A C   1 
ATOM   1312 O O   . ARG A 1 171 ? 58.396 88.889  -1.586  1.00 19.81 ? 171  ARG A O   1 
ATOM   1313 C CB  . ARG A 1 171 ? 59.111 86.326  -3.496  1.00 20.59 ? 171  ARG A CB  1 
ATOM   1314 C CG  . ARG A 1 171 ? 58.668 85.124  -4.291  1.00 22.47 ? 171  ARG A CG  1 
ATOM   1315 C CD  . ARG A 1 171 ? 59.519 84.965  -5.567  1.00 24.07 ? 171  ARG A CD  1 
ATOM   1316 N NE  . ARG A 1 171 ? 58.634 84.588  -6.659  1.00 30.12 ? 171  ARG A NE  1 
ATOM   1317 C CZ  . ARG A 1 171 ? 58.408 83.347  -7.059  1.00 30.74 ? 171  ARG A CZ  1 
ATOM   1318 N NH1 . ARG A 1 171 ? 59.045 82.337  -6.488  1.00 29.63 ? 171  ARG A NH1 1 
ATOM   1319 N NH2 . ARG A 1 171 ? 57.532 83.137  -8.035  1.00 31.58 ? 171  ARG A NH2 1 
ATOM   1320 N N   . LEU A 1 172 ? 60.046 87.526  -0.831  1.00 20.04 ? 172  LEU A N   1 
ATOM   1321 C CA  . LEU A 1 172 ? 60.791 88.560  -0.128  1.00 20.86 ? 172  LEU A CA  1 
ATOM   1322 C C   . LEU A 1 172 ? 62.236 88.499  -0.617  1.00 20.90 ? 172  LEU A C   1 
ATOM   1323 O O   . LEU A 1 172 ? 62.716 87.404  -0.935  1.00 20.59 ? 172  LEU A O   1 
ATOM   1324 C CB  . LEU A 1 172 ? 60.711 88.296  1.377   1.00 21.03 ? 172  LEU A CB  1 
ATOM   1325 C CG  . LEU A 1 172 ? 59.308 88.460  1.996   1.00 24.08 ? 172  LEU A CG  1 
ATOM   1326 C CD1 . LEU A 1 172 ? 59.382 88.142  3.467   1.00 24.59 ? 172  LEU A CD1 1 
ATOM   1327 C CD2 . LEU A 1 172 ? 58.672 89.865  1.744   1.00 23.72 ? 172  LEU A CD2 1 
ATOM   1328 N N   . PRO A 1 173 ? 62.924 89.668  -0.702  1.00 21.38 ? 173  PRO A N   1 
ATOM   1329 C CA  . PRO A 1 173 ? 64.283 89.722  -1.228  1.00 21.05 ? 173  PRO A CA  1 
ATOM   1330 C C   . PRO A 1 173 ? 65.329 89.327  -0.214  1.00 21.32 ? 173  PRO A C   1 
ATOM   1331 O O   . PRO A 1 173 ? 66.487 89.141  -0.591  1.00 23.01 ? 173  PRO A O   1 
ATOM   1332 C CB  . PRO A 1 173 ? 64.438 91.207  -1.613  1.00 21.74 ? 173  PRO A CB  1 
ATOM   1333 C CG  . PRO A 1 173 ? 63.621 91.940  -0.632  1.00 19.80 ? 173  PRO A CG  1 
ATOM   1334 C CD  . PRO A 1 173 ? 62.449 91.020  -0.321  1.00 21.19 ? 173  PRO A CD  1 
ATOM   1335 N N   . SER A 1 174 ? 64.959 89.207  1.069   1.00 21.16 ? 174  SER A N   1 
ATOM   1336 C CA  . SER A 1 174 ? 65.879 88.728  2.118   1.00 20.58 ? 174  SER A CA  1 
ATOM   1337 C C   . SER A 1 174 ? 65.091 88.115  3.277   1.00 21.03 ? 174  SER A C   1 
ATOM   1338 O O   . SER A 1 174 ? 63.849 88.123  3.279   1.00 20.30 ? 174  SER A O   1 
ATOM   1339 C CB  . SER A 1 174 ? 66.722 89.880  2.664   1.00 20.81 ? 174  SER A CB  1 
ATOM   1340 O OG  . SER A 1 174 ? 65.898 90.686  3.500   1.00 20.21 ? 174  SER A OG  1 
ATOM   1341 N N   . THR A 1 175 ? 65.822 87.599  4.264   1.00 20.67 ? 175  THR A N   1 
ATOM   1342 C CA  . THR A 1 175 ? 65.209 87.105  5.498   1.00 21.15 ? 175  THR A CA  1 
ATOM   1343 C C   . THR A 1 175 ? 65.353 88.091  6.663   1.00 20.54 ? 175  THR A C   1 
ATOM   1344 O O   . THR A 1 175 ? 65.132 87.707  7.807   1.00 20.51 ? 175  THR A O   1 
ATOM   1345 C CB  . THR A 1 175 ? 65.814 85.765  5.940   1.00 21.66 ? 175  THR A CB  1 
ATOM   1346 O OG1 . THR A 1 175 ? 67.205 85.972  6.215   1.00 23.94 ? 175  THR A OG1 1 
ATOM   1347 C CG2 . THR A 1 175 ? 65.628 84.699  4.837   1.00 22.28 ? 175  THR A CG2 1 
ATOM   1348 N N   . ASN A 1 176 ? 65.734 89.350  6.383   1.00 19.32 ? 176  ASN A N   1 
ATOM   1349 C CA  . ASN A 1 176 ? 65.713 90.381  7.432   1.00 18.98 ? 176  ASN A CA  1 
ATOM   1350 C C   . ASN A 1 176 ? 64.323 90.991  7.528   1.00 17.97 ? 176  ASN A C   1 
ATOM   1351 O O   . ASN A 1 176 ? 64.093 92.021  6.951   1.00 18.48 ? 176  ASN A O   1 
ATOM   1352 C CB  . ASN A 1 176 ? 66.743 91.466  7.143   1.00 17.75 ? 176  ASN A CB  1 
ATOM   1353 C CG  . ASN A 1 176 ? 68.042 90.881  6.745   1.00 19.81 ? 176  ASN A CG  1 
ATOM   1354 O OD1 . ASN A 1 176 ? 68.484 89.933  7.373   1.00 19.51 ? 176  ASN A OD1 1 
ATOM   1355 N ND2 . ASN A 1 176 ? 68.656 91.402  5.689   1.00 24.49 ? 176  ASN A ND2 1 
ATOM   1356 N N   . VAL A 1 177 ? 63.436 90.338  8.265   1.00 17.44 ? 177  VAL A N   1 
ATOM   1357 C CA  . VAL A 1 177 ? 62.008 90.692  8.311   1.00 16.72 ? 177  VAL A CA  1 
ATOM   1358 C C   . VAL A 1 177 ? 61.651 90.944  9.783   1.00 15.74 ? 177  VAL A C   1 
ATOM   1359 O O   . VAL A 1 177 ? 61.942 90.089  10.622  1.00 15.23 ? 177  VAL A O   1 
ATOM   1360 C CB  . VAL A 1 177 ? 61.132 89.521  7.733   1.00 17.26 ? 177  VAL A CB  1 
ATOM   1361 C CG1 . VAL A 1 177 ? 59.635 89.759  7.983   1.00 18.13 ? 177  VAL A CG1 1 
ATOM   1362 C CG2 . VAL A 1 177 ? 61.388 89.347  6.244   1.00 17.56 ? 177  VAL A CG2 1 
ATOM   1363 N N   . TYR A 1 178 ? 60.971 92.064  10.073  1.00 13.80 ? 178  TYR A N   1 
ATOM   1364 C CA  . TYR A 1 178 ? 60.712 92.524  11.423  1.00 13.35 ? 178  TYR A CA  1 
ATOM   1365 C C   . TYR A 1 178 ? 59.301 93.071  11.433  1.00 14.50 ? 178  TYR A C   1 
ATOM   1366 O O   . TYR A 1 178 ? 58.958 93.793  10.506  1.00 14.35 ? 178  TYR A O   1 
ATOM   1367 C CB  . TYR A 1 178 ? 61.675 93.695  11.809  1.00 12.94 ? 178  TYR A CB  1 
ATOM   1368 C CG  . TYR A 1 178 ? 63.119 93.384  11.465  1.00 12.14 ? 178  TYR A CG  1 
ATOM   1369 C CD1 . TYR A 1 178 ? 63.902 92.640  12.332  1.00 9.34  ? 178  TYR A CD1 1 
ATOM   1370 C CD2 . TYR A 1 178 ? 63.660 93.783  10.243  1.00 12.55 ? 178  TYR A CD2 1 
ATOM   1371 C CE1 . TYR A 1 178 ? 65.246 92.316  12.011  1.00 14.34 ? 178  TYR A CE1 1 
ATOM   1372 C CE2 . TYR A 1 178 ? 65.025 93.463  9.895   1.00 14.30 ? 178  TYR A CE2 1 
ATOM   1373 C CZ  . TYR A 1 178 ? 65.785 92.720  10.788  1.00 13.68 ? 178  TYR A CZ  1 
ATOM   1374 O OH  . TYR A 1 178 ? 67.081 92.392  10.463  1.00 13.94 ? 178  TYR A OH  1 
ATOM   1375 N N   . GLY A 1 179 ? 58.525 92.765  12.478  1.00 14.36 ? 179  GLY A N   1 
ATOM   1376 C CA  . GLY A 1 179 ? 57.196 93.337  12.621  1.00 16.62 ? 179  GLY A CA  1 
ATOM   1377 C C   . GLY A 1 179 ? 56.152 92.274  12.819  1.00 16.03 ? 179  GLY A C   1 
ATOM   1378 O O   . GLY A 1 179 ? 56.468 91.192  13.290  1.00 17.12 ? 179  GLY A O   1 
ATOM   1379 N N   . LEU A 1 180 ? 54.920 92.589  12.440  1.00 16.67 ? 180  LEU A N   1 
ATOM   1380 C CA  . LEU A 1 180 ? 53.709 91.794  12.775  1.00 17.05 ? 180  LEU A CA  1 
ATOM   1381 C C   . LEU A 1 180 ? 53.383 91.845  14.250  1.00 17.27 ? 180  LEU A C   1 
ATOM   1382 O O   . LEU A 1 180 ? 54.272 91.982  15.084  1.00 18.35 ? 180  LEU A O   1 
ATOM   1383 C CB  . LEU A 1 180 ? 53.848 90.340  12.291  1.00 16.57 ? 180  LEU A CB  1 
ATOM   1384 C CG  . LEU A 1 180 ? 54.347 90.182  10.834  1.00 16.03 ? 180  LEU A CG  1 
ATOM   1385 C CD1 . LEU A 1 180 ? 54.676 88.709  10.519  1.00 16.52 ? 180  LEU A CD1 1 
ATOM   1386 C CD2 . LEU A 1 180 ? 53.307 90.806  9.844   1.00 11.89 ? 180  LEU A CD2 1 
ATOM   1387 N N   . GLY A 1 181 ? 52.106 91.758  14.596  1.00 17.25 ? 181  GLY A N   1 
ATOM   1388 C CA  . GLY A 1 181 ? 51.716 91.833  15.993  1.00 16.37 ? 181  GLY A CA  1 
ATOM   1389 C C   . GLY A 1 181 ? 50.212 91.650  16.152  1.00 16.90 ? 181  GLY A C   1 
ATOM   1390 O O   . GLY A 1 181 ? 49.482 91.705  15.173  1.00 16.47 ? 181  GLY A O   1 
ATOM   1391 N N   . GLU A 1 182 ? 49.747 91.506  17.385  1.00 17.05 ? 182  GLU A N   1 
ATOM   1392 C CA  . GLU A 1 182 ? 50.602 91.560  18.580  1.00 17.27 ? 182  GLU A CA  1 
ATOM   1393 C C   . GLU A 1 182 ? 50.936 90.167  19.045  1.00 17.14 ? 182  GLU A C   1 
ATOM   1394 O O   . GLU A 1 182 ? 50.016 89.338  19.260  1.00 17.35 ? 182  GLU A O   1 
ATOM   1395 C CB  . GLU A 1 182 ? 49.920 92.357  19.713  1.00 17.44 ? 182  GLU A CB  1 
ATOM   1396 C CG  . GLU A 1 182 ? 50.727 92.388  21.018  1.00 15.09 ? 182  GLU A CG  1 
ATOM   1397 C CD  . GLU A 1 182 ? 50.287 93.458  22.007  1.00 19.01 ? 182  GLU A CD  1 
ATOM   1398 O OE1 . GLU A 1 182 ? 49.130 93.952  21.865  1.00 22.45 ? 182  GLU A OE1 1 
ATOM   1399 O OE2 . GLU A 1 182 ? 51.080 93.790  22.957  1.00 17.36 ? 182  GLU A OE2 1 
ATOM   1400 N N   . HIS A 1 183 ? 52.237 89.883  19.183  1.00 16.20 ? 183  HIS A N   1 
ATOM   1401 C CA  . HIS A 1 183 ? 52.693 88.567  19.609  1.00 16.36 ? 183  HIS A CA  1 
ATOM   1402 C C   . HIS A 1 183 ? 53.950 88.667  20.508  1.00 17.39 ? 183  HIS A C   1 
ATOM   1403 O O   . HIS A 1 183 ? 54.624 89.711  20.545  1.00 16.90 ? 183  HIS A O   1 
ATOM   1404 C CB  . HIS A 1 183 ? 53.064 87.648  18.395  1.00 16.70 ? 183  HIS A CB  1 
ATOM   1405 C CG  . HIS A 1 183 ? 52.171 87.771  17.188  1.00 16.01 ? 183  HIS A CG  1 
ATOM   1406 N ND1 . HIS A 1 183 ? 50.887 87.250  17.142  1.00 18.72 ? 183  HIS A ND1 1 
ATOM   1407 C CD2 . HIS A 1 183 ? 52.404 88.288  15.957  1.00 14.26 ? 183  HIS A CD2 1 
ATOM   1408 C CE1 . HIS A 1 183 ? 50.350 87.492  15.956  1.00 10.94 ? 183  HIS A CE1 1 
ATOM   1409 N NE2 . HIS A 1 183 ? 51.248 88.122  15.217  1.00 15.94 ? 183  HIS A NE2 1 
ATOM   1410 N N   . VAL A 1 184 ? 54.288 87.556  21.169  1.00 17.73 ? 184  VAL A N   1 
ATOM   1411 C CA  . VAL A 1 184 ? 55.651 87.314  21.687  1.00 18.32 ? 184  VAL A CA  1 
ATOM   1412 C C   . VAL A 1 184 ? 56.399 86.449  20.657  1.00 19.10 ? 184  VAL A C   1 
ATOM   1413 O O   . VAL A 1 184 ? 56.175 85.227  20.546  1.00 19.38 ? 184  VAL A O   1 
ATOM   1414 C CB  . VAL A 1 184 ? 55.633 86.672  23.088  1.00 18.28 ? 184  VAL A CB  1 
ATOM   1415 C CG1 . VAL A 1 184 ? 57.049 86.272  23.533  1.00 20.56 ? 184  VAL A CG1 1 
ATOM   1416 C CG2 . VAL A 1 184 ? 54.997 87.642  24.102  1.00 17.43 ? 184  VAL A CG2 1 
ATOM   1417 N N   . HIS A 1 185 ? 57.238 87.105  19.852  1.00 18.78 ? 185  HIS A N   1 
ATOM   1418 C CA  . HIS A 1 185 ? 57.957 86.433  18.782  1.00 19.11 ? 185  HIS A CA  1 
ATOM   1419 C C   . HIS A 1 185 ? 59.216 85.819  19.367  1.00 19.44 ? 185  HIS A C   1 
ATOM   1420 O O   . HIS A 1 185 ? 59.779 84.918  18.786  1.00 19.17 ? 185  HIS A O   1 
ATOM   1421 C CB  . HIS A 1 185 ? 58.330 87.412  17.651  1.00 18.69 ? 185  HIS A CB  1 
ATOM   1422 C CG  . HIS A 1 185 ? 57.152 87.980  16.922  1.00 17.05 ? 185  HIS A CG  1 
ATOM   1423 N ND1 . HIS A 1 185 ? 57.068 89.309  16.567  1.00 13.05 ? 185  HIS A ND1 1 
ATOM   1424 C CD2 . HIS A 1 185 ? 56.006 87.402  16.481  1.00 18.36 ? 185  HIS A CD2 1 
ATOM   1425 C CE1 . HIS A 1 185 ? 55.928 89.525  15.930  1.00 18.08 ? 185  HIS A CE1 1 
ATOM   1426 N NE2 . HIS A 1 185 ? 55.266 88.383  15.862  1.00 15.34 ? 185  HIS A NE2 1 
ATOM   1427 N N   . GLN A 1 186 ? 59.666 86.341  20.505  1.00 20.14 ? 186  GLN A N   1 
ATOM   1428 C CA  . GLN A 1 186 ? 60.866 85.838  21.200  1.00 21.90 ? 186  GLN A CA  1 
ATOM   1429 C C   . GLN A 1 186 ? 62.178 86.332  20.596  1.00 23.38 ? 186  GLN A C   1 
ATOM   1430 O O   . GLN A 1 186 ? 63.080 86.734  21.322  1.00 24.19 ? 186  GLN A O   1 
ATOM   1431 C CB  . GLN A 1 186 ? 60.881 84.302  21.346  1.00 21.59 ? 186  GLN A CB  1 
ATOM   1432 C CG  . GLN A 1 186 ? 59.621 83.748  21.998  1.00 21.07 ? 186  GLN A CG  1 
ATOM   1433 C CD  . GLN A 1 186 ? 59.681 82.282  22.370  1.00 22.90 ? 186  GLN A CD  1 
ATOM   1434 O OE1 . GLN A 1 186 ? 60.718 81.767  22.763  1.00 22.60 ? 186  GLN A OE1 1 
ATOM   1435 N NE2 . GLN A 1 186 ? 58.533 81.609  22.292  1.00 24.91 ? 186  GLN A NE2 1 
ATOM   1436 N N   . GLN A 1 187 ? 62.281 86.270  19.274  1.00 24.13 ? 187  GLN A N   1 
ATOM   1437 C CA  . GLN A 1 187 ? 63.415 86.814  18.518  1.00 23.92 ? 187  GLN A CA  1 
ATOM   1438 C C   . GLN A 1 187 ? 62.871 88.073  17.831  1.00 22.85 ? 187  GLN A C   1 
ATOM   1439 O O   . GLN A 1 187 ? 61.669 88.202  17.679  1.00 23.00 ? 187  GLN A O   1 
ATOM   1440 C CB  . GLN A 1 187 ? 63.864 85.773  17.486  1.00 24.22 ? 187  GLN A CB  1 
ATOM   1441 C CG  . GLN A 1 187 ? 64.733 84.616  18.071  1.00 29.77 ? 187  GLN A CG  1 
ATOM   1442 C CD  . GLN A 1 187 ? 63.946 83.565  18.907  1.00 35.95 ? 187  GLN A CD  1 
ATOM   1443 O OE1 . GLN A 1 187 ? 62.949 82.956  18.441  1.00 36.94 ? 187  GLN A OE1 1 
ATOM   1444 N NE2 . GLN A 1 187 ? 64.422 83.327  20.137  1.00 37.75 ? 187  GLN A NE2 1 
ATOM   1445 N N   . TYR A 1 188 ? 63.730 89.019  17.460  1.00 20.80 ? 188  TYR A N   1 
ATOM   1446 C CA  . TYR A 1 188 ? 63.285 90.190  16.742  1.00 19.45 ? 188  TYR A CA  1 
ATOM   1447 C C   . TYR A 1 188 ? 63.250 89.925  15.233  1.00 20.37 ? 188  TYR A C   1 
ATOM   1448 O O   . TYR A 1 188 ? 62.243 90.191  14.559  1.00 19.48 ? 188  TYR A O   1 
ATOM   1449 C CB  . TYR A 1 188 ? 64.135 91.420  17.114  1.00 19.00 ? 188  TYR A CB  1 
ATOM   1450 C CG  . TYR A 1 188 ? 63.690 92.684  16.444  1.00 17.21 ? 188  TYR A CG  1 
ATOM   1451 C CD1 . TYR A 1 188 ? 62.370 93.157  16.599  1.00 15.64 ? 188  TYR A CD1 1 
ATOM   1452 C CD2 . TYR A 1 188 ? 64.575 93.421  15.681  1.00 15.39 ? 188  TYR A CD2 1 
ATOM   1453 C CE1 . TYR A 1 188 ? 61.951 94.296  15.997  1.00 15.68 ? 188  TYR A CE1 1 
ATOM   1454 C CE2 . TYR A 1 188 ? 64.155 94.599  15.063  1.00 14.11 ? 188  TYR A CE2 1 
ATOM   1455 C CZ  . TYR A 1 188 ? 62.861 95.032  15.233  1.00 15.81 ? 188  TYR A CZ  1 
ATOM   1456 O OH  . TYR A 1 188 ? 62.436 96.180  14.605  1.00 16.09 ? 188  TYR A OH  1 
ATOM   1457 N N   . ARG A 1 189 ? 64.337 89.382  14.690  1.00 20.56 ? 189  ARG A N   1 
ATOM   1458 C CA  . ARG A 1 189 ? 64.300 88.982  13.282  1.00 21.93 ? 189  ARG A CA  1 
ATOM   1459 C C   . ARG A 1 189 ? 63.497 87.670  13.149  1.00 22.93 ? 189  ARG A C   1 
ATOM   1460 O O   . ARG A 1 189 ? 63.780 86.696  13.851  1.00 21.31 ? 189  ARG A O   1 
ATOM   1461 C CB  . ARG A 1 189 ? 65.712 88.780  12.726  1.00 20.48 ? 189  ARG A CB  1 
ATOM   1462 C CG  . ARG A 1 189 ? 65.732 88.815  11.215  1.00 21.14 ? 189  ARG A CG  1 
ATOM   1463 C CD  . ARG A 1 189 ? 67.109 88.551  10.700  1.00 21.67 ? 189  ARG A CD  1 
ATOM   1464 N NE  . ARG A 1 189 ? 67.342 87.145  10.867  1.00 27.70 ? 189  ARG A NE  1 
ATOM   1465 C CZ  . ARG A 1 189 ? 68.493 86.530  10.740  1.00 35.18 ? 189  ARG A CZ  1 
ATOM   1466 N NH1 . ARG A 1 189 ? 69.627 87.218  10.457  1.00 38.53 ? 189  ARG A NH1 1 
ATOM   1467 N NH2 . ARG A 1 189 ? 68.486 85.210  10.911  1.00 35.42 ? 189  ARG A NH2 1 
ATOM   1468 N N   . HIS A 1 190 ? 62.493 87.664  12.275  1.00 24.68 ? 190  HIS A N   1 
ATOM   1469 C CA  . HIS A 1 190 ? 61.783 86.412  11.915  1.00 28.31 ? 190  HIS A CA  1 
ATOM   1470 C C   . HIS A 1 190 ? 62.712 85.487  11.105  1.00 29.49 ? 190  HIS A C   1 
ATOM   1471 O O   . HIS A 1 190 ? 63.126 85.863  10.019  1.00 31.81 ? 190  HIS A O   1 
ATOM   1472 C CB  . HIS A 1 190 ? 60.553 86.731  11.061  1.00 25.72 ? 190  HIS A CB  1 
ATOM   1473 C CG  . HIS A 1 190 ? 59.464 87.420  11.806  1.00 24.89 ? 190  HIS A CG  1 
ATOM   1474 N ND1 . HIS A 1 190 ? 59.423 88.790  11.978  1.00 23.26 ? 190  HIS A ND1 1 
ATOM   1475 C CD2 . HIS A 1 190 ? 58.376 86.931  12.441  1.00 25.28 ? 190  HIS A CD2 1 
ATOM   1476 C CE1 . HIS A 1 190 ? 58.353 89.112  12.686  1.00 21.82 ? 190  HIS A CE1 1 
ATOM   1477 N NE2 . HIS A 1 190 ? 57.696 88.005  12.970  1.00 24.02 ? 190  HIS A NE2 1 
ATOM   1478 N N   . ASP A 1 191 ? 63.039 84.314  11.639  1.00 32.02 ? 191  ASP A N   1 
ATOM   1479 C CA  . ASP A 1 191 ? 63.904 83.269  10.989  1.00 33.37 ? 191  ASP A CA  1 
ATOM   1480 C C   . ASP A 1 191 ? 63.537 82.940  9.509   1.00 34.45 ? 191  ASP A C   1 
ATOM   1481 O O   . ASP A 1 191 ? 64.423 82.593  8.693   1.00 34.03 ? 191  ASP A O   1 
ATOM   1482 C CB  . ASP A 1 191 ? 63.795 81.946  11.809  1.00 34.93 ? 191  ASP A CB  1 
ATOM   1483 C CG  . ASP A 1 191 ? 62.312 81.616  12.197  1.00 39.86 ? 191  ASP A CG  1 
ATOM   1484 O OD1 . ASP A 1 191 ? 61.461 82.532  12.026  1.00 42.68 ? 191  ASP A OD1 1 
ATOM   1485 O OD2 . ASP A 1 191 ? 61.984 80.481  12.675  1.00 43.66 ? 191  ASP A OD2 1 
ATOM   1486 N N   . MET A 1 192 ? 62.218 83.011  9.221   1.00 33.91 ? 192  MET A N   1 
ATOM   1487 C CA  . MET A 1 192 ? 61.575 82.669  7.930   1.00 32.16 ? 192  MET A CA  1 
ATOM   1488 C C   . MET A 1 192 ? 61.322 81.175  7.744   1.00 31.57 ? 192  MET A C   1 
ATOM   1489 O O   . MET A 1 192 ? 60.908 80.728  6.684   1.00 31.30 ? 192  MET A O   1 
ATOM   1490 C CB  . MET A 1 192 ? 62.286 83.292  6.719   1.00 32.62 ? 192  MET A CB  1 
ATOM   1491 C CG  . MET A 1 192 ? 62.198 84.813  6.663   1.00 30.20 ? 192  MET A CG  1 
ATOM   1492 S SD  . MET A 1 192 ? 60.569 85.391  7.089   1.00 29.14 ? 192  MET A SD  1 
ATOM   1493 C CE  . MET A 1 192 ? 59.705 85.122  5.539   1.00 26.08 ? 192  MET A CE  1 
ATOM   1494 N N   A ASN A 1 193 ? 61.575 80.398  8.787   0.50 30.89 ? 193  ASN A N   1 
ATOM   1495 N N   B ASN A 1 193 ? 61.574 80.396  8.785   0.50 30.88 ? 193  ASN A N   1 
ATOM   1496 C CA  A ASN A 1 193 ? 61.132 79.019  8.794   0.50 30.07 ? 193  ASN A CA  1 
ATOM   1497 C CA  B ASN A 1 193 ? 61.174 79.006  8.778   0.50 30.07 ? 193  ASN A CA  1 
ATOM   1498 C C   A ASN A 1 193 ? 59.635 78.988  9.011   0.50 29.46 ? 193  ASN A C   1 
ATOM   1499 C C   B ASN A 1 193 ? 59.696 78.980  8.382   0.50 29.57 ? 193  ASN A C   1 
ATOM   1500 O O   A ASN A 1 193 ? 59.058 79.972  9.507   0.50 29.37 ? 193  ASN A O   1 
ATOM   1501 O O   B ASN A 1 193 ? 59.178 79.964  7.846   0.50 30.16 ? 193  ASN A O   1 
ATOM   1502 C CB  A ASN A 1 193 ? 61.883 78.197  9.833   0.50 30.35 ? 193  ASN A CB  1 
ATOM   1503 C CB  B ASN A 1 193 ? 61.408 78.395  10.163  0.50 30.21 ? 193  ASN A CB  1 
ATOM   1504 C CG  A ASN A 1 193 ? 63.225 77.732  9.326   0.50 31.61 ? 193  ASN A CG  1 
ATOM   1505 C CG  B ASN A 1 193 ? 61.816 76.927  10.113  0.50 30.86 ? 193  ASN A CG  1 
ATOM   1506 O OD1 A ASN A 1 193 ? 64.254 78.030  9.924   0.50 33.81 ? 193  ASN A OD1 1 
ATOM   1507 O OD1 B ASN A 1 193 ? 61.996 76.301  11.158  0.50 31.63 ? 193  ASN A OD1 1 
ATOM   1508 N ND2 A ASN A 1 193 ? 63.228 77.019  8.197   0.50 32.61 ? 193  ASN A ND2 1 
ATOM   1509 N ND2 B ASN A 1 193 ? 61.965 76.372  8.907   0.50 30.14 ? 193  ASN A ND2 1 
ATOM   1510 N N   . TRP A 1 194 ? 59.026 77.866  8.624   1.00 28.18 ? 194  TRP A N   1 
ATOM   1511 C CA  . TRP A 1 194 ? 57.591 77.742  8.417   1.00 26.34 ? 194  TRP A CA  1 
ATOM   1512 C C   . TRP A 1 194 ? 56.857 78.118  9.694   1.00 26.26 ? 194  TRP A C   1 
ATOM   1513 O O   . TRP A 1 194 ? 56.901 77.355  10.657  1.00 26.65 ? 194  TRP A O   1 
ATOM   1514 C CB  . TRP A 1 194 ? 57.323 76.264  8.131   1.00 24.58 ? 194  TRP A CB  1 
ATOM   1515 C CG  . TRP A 1 194 ? 58.060 75.749  6.917   1.00 23.41 ? 194  TRP A CG  1 
ATOM   1516 C CD1 . TRP A 1 194 ? 59.335 75.191  6.866   1.00 22.43 ? 194  TRP A CD1 1 
ATOM   1517 C CD2 . TRP A 1 194 ? 57.582 75.778  5.583   1.00 21.74 ? 194  TRP A CD2 1 
ATOM   1518 N NE1 . TRP A 1 194 ? 59.649 74.879  5.568   1.00 21.21 ? 194  TRP A NE1 1 
ATOM   1519 C CE2 . TRP A 1 194 ? 58.590 75.220  4.761   1.00 22.00 ? 194  TRP A CE2 1 
ATOM   1520 C CE3 . TRP A 1 194 ? 56.385 76.222  4.991   1.00 22.64 ? 194  TRP A CE3 1 
ATOM   1521 C CZ2 . TRP A 1 194 ? 58.436 75.086  3.383   1.00 21.16 ? 194  TRP A CZ2 1 
ATOM   1522 C CZ3 . TRP A 1 194 ? 56.242 76.104  3.600   1.00 21.72 ? 194  TRP A CZ3 1 
ATOM   1523 C CH2 . TRP A 1 194 ? 57.268 75.541  2.820   1.00 22.17 ? 194  TRP A CH2 1 
ATOM   1524 N N   . LYS A 1 195 ? 56.178 79.265  9.711   1.00 25.30 ? 195  LYS A N   1 
ATOM   1525 C CA  . LYS A 1 195 ? 55.670 79.851  10.954  1.00 24.56 ? 195  LYS A CA  1 
ATOM   1526 C C   . LYS A 1 195 ? 54.373 80.563  10.580  1.00 23.63 ? 195  LYS A C   1 
ATOM   1527 O O   . LYS A 1 195 ? 54.316 81.223  9.541   1.00 23.55 ? 195  LYS A O   1 
ATOM   1528 C CB  . LYS A 1 195 ? 56.752 80.807  11.488  1.00 25.33 ? 195  LYS A CB  1 
ATOM   1529 C CG  . LYS A 1 195 ? 56.886 81.019  12.984  1.00 30.03 ? 195  LYS A CG  1 
ATOM   1530 C CD  . LYS A 1 195 ? 56.359 79.890  13.920  1.00 35.16 ? 195  LYS A CD  1 
ATOM   1531 C CE  . LYS A 1 195 ? 56.073 80.435  15.353  1.00 34.08 ? 195  LYS A CE  1 
ATOM   1532 N NZ  . LYS A 1 195 ? 54.711 80.065  15.995  1.00 35.97 ? 195  LYS A NZ  1 
ATOM   1533 N N   . THR A 1 196 ? 53.319 80.354  11.363  1.00 21.46 ? 196  THR A N   1 
ATOM   1534 C CA  . THR A 1 196 ? 52.037 80.995  11.153  1.00 21.10 ? 196  THR A CA  1 
ATOM   1535 C C   . THR A 1 196 ? 51.709 81.854  12.390  1.00 19.77 ? 196  THR A C   1 
ATOM   1536 O O   . THR A 1 196 ? 51.729 81.342  13.509  1.00 20.16 ? 196  THR A O   1 
ATOM   1537 C CB  . THR A 1 196 ? 50.911 79.931  10.930  1.00 21.31 ? 196  THR A CB  1 
ATOM   1538 O OG1 . THR A 1 196 ? 51.147 79.213  9.697   1.00 23.49 ? 196  THR A OG1 1 
ATOM   1539 C CG2 . THR A 1 196 ? 49.586 80.584  10.824  1.00 22.61 ? 196  THR A CG2 1 
ATOM   1540 N N   . TRP A 1 197 ? 51.421 83.146  12.186  1.00 17.94 ? 197  TRP A N   1 
ATOM   1541 C CA  . TRP A 1 197 ? 51.096 84.079  13.268  1.00 16.90 ? 197  TRP A CA  1 
ATOM   1542 C C   . TRP A 1 197 ? 49.648 84.537  13.143  1.00 16.46 ? 197  TRP A C   1 
ATOM   1543 O O   . TRP A 1 197 ? 49.351 85.317  12.238  1.00 17.28 ? 197  TRP A O   1 
ATOM   1544 C CB  . TRP A 1 197 ? 52.027 85.308  13.229  1.00 16.13 ? 197  TRP A CB  1 
ATOM   1545 C CG  . TRP A 1 197 ? 53.444 84.921  13.552  1.00 17.75 ? 197  TRP A CG  1 
ATOM   1546 C CD1 . TRP A 1 197 ? 54.485 84.746  12.661  1.00 18.40 ? 197  TRP A CD1 1 
ATOM   1547 C CD2 . TRP A 1 197 ? 53.974 84.594  14.852  1.00 17.97 ? 197  TRP A CD2 1 
ATOM   1548 N NE1 . TRP A 1 197 ? 55.632 84.359  13.341  1.00 18.25 ? 197  TRP A NE1 1 
ATOM   1549 C CE2 . TRP A 1 197 ? 55.339 84.253  14.679  1.00 16.95 ? 197  TRP A CE2 1 
ATOM   1550 C CE3 . TRP A 1 197 ? 53.432 84.583  16.155  1.00 18.99 ? 197  TRP A CE3 1 
ATOM   1551 C CZ2 . TRP A 1 197 ? 56.160 83.893  15.762  1.00 20.04 ? 197  TRP A CZ2 1 
ATOM   1552 C CZ3 . TRP A 1 197 ? 54.259 84.235  17.227  1.00 17.35 ? 197  TRP A CZ3 1 
ATOM   1553 C CH2 . TRP A 1 197 ? 55.598 83.884  17.018  1.00 17.71 ? 197  TRP A CH2 1 
ATOM   1554 N N   . PRO A 1 198 ? 48.758 84.088  14.052  1.00 16.20 ? 198  PRO A N   1 
ATOM   1555 C CA  . PRO A 1 198 ? 47.370 84.544  14.006  1.00 15.62 ? 198  PRO A CA  1 
ATOM   1556 C C   . PRO A 1 198 ? 47.271 85.946  14.560  1.00 16.73 ? 198  PRO A C   1 
ATOM   1557 O O   . PRO A 1 198 ? 48.042 86.319  15.498  1.00 16.66 ? 198  PRO A O   1 
ATOM   1558 C CB  . PRO A 1 198 ? 46.629 83.563  14.943  1.00 15.82 ? 198  PRO A CB  1 
ATOM   1559 C CG  . PRO A 1 198 ? 47.678 83.065  15.895  1.00 16.89 ? 198  PRO A CG  1 
ATOM   1560 C CD  . PRO A 1 198 ? 48.997 83.101  15.134  1.00 15.99 ? 198  PRO A CD  1 
ATOM   1561 N N   . ILE A 1 199 ? 46.345 86.723  13.991  1.00 15.92 ? 199  ILE A N   1 
ATOM   1562 C CA  . ILE A 1 199 ? 46.116 88.077  14.435  1.00 16.29 ? 199  ILE A CA  1 
ATOM   1563 C C   . ILE A 1 199 ? 44.641 88.302  14.684  1.00 17.61 ? 199  ILE A C   1 
ATOM   1564 O O   . ILE A 1 199 ? 43.845 88.319  13.749  1.00 16.55 ? 199  ILE A O   1 
ATOM   1565 C CB  . ILE A 1 199 ? 46.616 89.135  13.397  1.00 17.16 ? 199  ILE A CB  1 
ATOM   1566 C CG1 . ILE A 1 199 ? 48.152 89.015  13.199  1.00 14.54 ? 199  ILE A CG1 1 
ATOM   1567 C CG2 . ILE A 1 199 ? 46.334 90.513  13.915  1.00 16.21 ? 199  ILE A CG2 1 
ATOM   1568 C CD1 . ILE A 1 199 ? 48.722 90.018  12.136  1.00 15.64 ? 199  ILE A CD1 1 
ATOM   1569 N N   . PHE A 1 200 ? 44.288 88.487  15.954  1.00 17.23 ? 200  PHE A N   1 
ATOM   1570 C CA  . PHE A 1 200 ? 42.926 88.711  16.316  1.00 18.55 ? 200  PHE A CA  1 
ATOM   1571 C C   . PHE A 1 200 ? 42.974 89.101  17.781  1.00 18.50 ? 200  PHE A C   1 
ATOM   1572 O O   . PHE A 1 200 ? 43.392 88.305  18.641  1.00 19.36 ? 200  PHE A O   1 
ATOM   1573 C CB  . PHE A 1 200 ? 42.113 87.415  16.089  1.00 18.48 ? 200  PHE A CB  1 
ATOM   1574 C CG  . PHE A 1 200 ? 40.650 87.570  16.286  1.00 20.94 ? 200  PHE A CG  1 
ATOM   1575 C CD1 . PHE A 1 200 ? 39.872 88.325  15.389  1.00 21.64 ? 200  PHE A CD1 1 
ATOM   1576 C CD2 . PHE A 1 200 ? 40.020 86.926  17.351  1.00 22.54 ? 200  PHE A CD2 1 
ATOM   1577 C CE1 . PHE A 1 200 ? 38.510 88.437  15.563  1.00 20.47 ? 200  PHE A CE1 1 
ATOM   1578 C CE2 . PHE A 1 200 ? 38.660 87.051  17.541  1.00 18.85 ? 200  PHE A CE2 1 
ATOM   1579 C CZ  . PHE A 1 200 ? 37.895 87.801  16.640  1.00 19.13 ? 200  PHE A CZ  1 
ATOM   1580 N N   . ASN A 1 201 ? 42.572 90.339  18.048  1.00 17.92 ? 201  ASN A N   1 
ATOM   1581 C CA  . ASN A 1 201 ? 42.635 90.924  19.397  1.00 17.70 ? 201  ASN A CA  1 
ATOM   1582 C C   . ASN A 1 201 ? 41.993 90.043  20.466  1.00 18.29 ? 201  ASN A C   1 
ATOM   1583 O O   . ASN A 1 201 ? 40.803 89.676  20.385  1.00 17.91 ? 201  ASN A O   1 
ATOM   1584 C CB  . ASN A 1 201 ? 42.024 92.308  19.359  1.00 17.32 ? 201  ASN A CB  1 
ATOM   1585 C CG  . ASN A 1 201 ? 42.803 93.236  18.433  1.00 15.77 ? 201  ASN A CG  1 
ATOM   1586 O OD1 . ASN A 1 201 ? 43.781 92.805  17.827  1.00 17.68 ? 201  ASN A OD1 1 
ATOM   1587 N ND2 . ASN A 1 201 ? 42.390 94.475  18.323  1.00 11.71 ? 201  ASN A ND2 1 
ATOM   1588 N N   . ARG A 1 202 ? 42.806 89.667  21.445  1.00 17.97 ? 202  ARG A N   1 
ATOM   1589 C CA  . ARG A 1 202 ? 42.397 88.695  22.413  1.00 18.93 ? 202  ARG A CA  1 
ATOM   1590 C C   . ARG A 1 202 ? 43.110 88.892  23.765  1.00 20.25 ? 202  ARG A C   1 
ATOM   1591 O O   . ARG A 1 202 ? 44.331 89.118  23.835  1.00 19.42 ? 202  ARG A O   1 
ATOM   1592 C CB  . ARG A 1 202 ? 42.593 87.282  21.834  1.00 18.74 ? 202  ARG A CB  1 
ATOM   1593 C CG  . ARG A 1 202 ? 42.586 86.182  22.877  1.00 19.83 ? 202  ARG A CG  1 
ATOM   1594 C CD  . ARG A 1 202 ? 41.165 85.859  23.364  1.00 21.57 ? 202  ARG A CD  1 
ATOM   1595 N NE  . ARG A 1 202 ? 41.203 84.958  24.513  1.00 22.16 ? 202  ARG A NE  1 
ATOM   1596 C CZ  . ARG A 1 202 ? 41.023 83.647  24.442  1.00 24.85 ? 202  ARG A CZ  1 
ATOM   1597 N NH1 . ARG A 1 202 ? 40.758 83.069  23.276  1.00 23.66 ? 202  ARG A NH1 1 
ATOM   1598 N NH2 . ARG A 1 202 ? 41.098 82.913  25.547  1.00 25.51 ? 202  ARG A NH2 1 
ATOM   1599 N N   . ASP A 1 203 ? 42.330 88.835  24.841  1.00 20.70 ? 203  ASP A N   1 
ATOM   1600 C CA  . ASP A 1 203 ? 42.888 88.797  26.180  1.00 21.74 ? 203  ASP A CA  1 
ATOM   1601 C C   . ASP A 1 203 ? 43.521 87.438  26.451  1.00 22.89 ? 203  ASP A C   1 
ATOM   1602 O O   . ASP A 1 203 ? 42.825 86.480  26.782  1.00 23.01 ? 203  ASP A O   1 
ATOM   1603 C CB  . ASP A 1 203 ? 41.774 89.074  27.191  1.00 21.00 ? 203  ASP A CB  1 
ATOM   1604 C CG  . ASP A 1 203 ? 42.257 89.056  28.622  1.00 23.00 ? 203  ASP A CG  1 
ATOM   1605 O OD1 . ASP A 1 203 ? 43.459 88.724  28.875  1.00 20.31 ? 203  ASP A OD1 1 
ATOM   1606 O OD2 . ASP A 1 203 ? 41.405 89.380  29.507  1.00 24.31 ? 203  ASP A OD2 1 
ATOM   1607 N N   . THR A 1 204 ? 44.835 87.340  26.281  1.00 24.18 ? 204  THR A N   1 
ATOM   1608 C CA  . THR A 1 204 ? 45.546 86.124  26.618  1.00 25.88 ? 204  THR A CA  1 
ATOM   1609 C C   . THR A 1 204 ? 46.941 86.479  27.057  1.00 24.94 ? 204  THR A C   1 
ATOM   1610 O O   . THR A 1 204 ? 47.453 87.517  26.670  1.00 25.24 ? 204  THR A O   1 
ATOM   1611 C CB  . THR A 1 204 ? 45.734 85.228  25.435  1.00 26.55 ? 204  THR A CB  1 
ATOM   1612 O OG1 . THR A 1 204 ? 46.384 85.960  24.398  1.00 31.66 ? 204  THR A OG1 1 
ATOM   1613 C CG2 . THR A 1 204 ? 44.411 84.734  24.904  1.00 31.74 ? 204  THR A CG2 1 
ATOM   1614 N N   . THR A 1 205 ? 47.557 85.584  27.822  1.00 23.72 ? 205  THR A N   1 
ATOM   1615 C CA  . THR A 1 205 ? 48.897 85.760  28.365  1.00 23.70 ? 205  THR A CA  1 
ATOM   1616 C C   . THR A 1 205 ? 49.945 85.848  27.267  1.00 23.80 ? 205  THR A C   1 
ATOM   1617 O O   . THR A 1 205 ? 50.019 84.957  26.409  1.00 24.00 ? 205  THR A O   1 
ATOM   1618 C CB  . THR A 1 205 ? 49.249 84.556  29.244  1.00 23.97 ? 205  THR A CB  1 
ATOM   1619 O OG1 . THR A 1 205 ? 48.167 84.299  30.135  1.00 24.22 ? 205  THR A OG1 1 
ATOM   1620 C CG2 . THR A 1 205 ? 50.542 84.777  30.035  1.00 22.91 ? 205  THR A CG2 1 
ATOM   1621 N N   . PRO A 1 206 ? 50.789 86.894  27.314  1.00 23.77 ? 206  PRO A N   1 
ATOM   1622 C CA  . PRO A 1 206 ? 51.947 86.931  26.438  1.00 24.18 ? 206  PRO A CA  1 
ATOM   1623 C C   . PRO A 1 206 ? 53.006 85.939  26.922  1.00 24.49 ? 206  PRO A C   1 
ATOM   1624 O O   . PRO A 1 206 ? 53.861 86.261  27.758  1.00 25.08 ? 206  PRO A O   1 
ATOM   1625 C CB  . PRO A 1 206 ? 52.428 88.388  26.534  1.00 24.11 ? 206  PRO A CB  1 
ATOM   1626 C CG  . PRO A 1 206 ? 51.927 88.890  27.825  1.00 24.69 ? 206  PRO A CG  1 
ATOM   1627 C CD  . PRO A 1 206 ? 50.689 88.090  28.173  1.00 23.84 ? 206  PRO A CD  1 
ATOM   1628 N N   . ASN A 1 207 ? 52.930 84.729  26.396  1.00 24.49 ? 207  ASN A N   1 
ATOM   1629 C CA  . ASN A 1 207 ? 53.799 83.648  26.846  1.00 24.10 ? 207  ASN A CA  1 
ATOM   1630 C C   . ASN A 1 207 ? 54.535 83.072  25.672  1.00 24.03 ? 207  ASN A C   1 
ATOM   1631 O O   . ASN A 1 207 ? 54.560 83.684  24.602  1.00 23.68 ? 207  ASN A O   1 
ATOM   1632 C CB  . ASN A 1 207 ? 52.985 82.573  27.572  1.00 23.47 ? 207  ASN A CB  1 
ATOM   1633 C CG  . ASN A 1 207 ? 51.865 81.989  26.706  1.00 24.61 ? 207  ASN A CG  1 
ATOM   1634 O OD1 . ASN A 1 207 ? 51.887 82.093  25.489  1.00 23.29 ? 207  ASN A OD1 1 
ATOM   1635 N ND2 . ASN A 1 207 ? 50.901 81.340  27.344  1.00 22.68 ? 207  ASN A ND2 1 
ATOM   1636 N N   . GLY A 1 208 ? 55.126 81.894  25.874  1.00 24.21 ? 208  GLY A N   1 
ATOM   1637 C CA  . GLY A 1 208 ? 55.952 81.232  24.875  1.00 24.53 ? 208  GLY A CA  1 
ATOM   1638 C C   . GLY A 1 208 ? 55.219 80.458  23.798  1.00 24.60 ? 208  GLY A C   1 
ATOM   1639 O O   . GLY A 1 208 ? 55.864 79.843  22.971  1.00 24.73 ? 208  GLY A O   1 
ATOM   1640 N N   . ASN A 1 209 ? 53.884 80.504  23.788  1.00 24.99 ? 209  ASN A N   1 
ATOM   1641 C CA  . ASN A 1 209 ? 53.085 79.719  22.848  1.00 25.98 ? 209  ASN A CA  1 
ATOM   1642 C C   . ASN A 1 209 ? 52.776 80.367  21.509  1.00 24.99 ? 209  ASN A C   1 
ATOM   1643 O O   . ASN A 1 209 ? 52.077 79.760  20.682  1.00 25.60 ? 209  ASN A O   1 
ATOM   1644 C CB  . ASN A 1 209 ? 51.754 79.312  23.501  1.00 27.64 ? 209  ASN A CB  1 
ATOM   1645 C CG  . ASN A 1 209 ? 51.923 78.277  24.584  1.00 34.40 ? 209  ASN A CG  1 
ATOM   1646 O OD1 . ASN A 1 209 ? 52.751 77.366  24.463  1.00 40.79 ? 209  ASN A OD1 1 
ATOM   1647 N ND2 . ASN A 1 209 ? 51.116 78.400  25.654  1.00 43.99 ? 209  ASN A ND2 1 
ATOM   1648 N N   . GLY A 1 210 ? 53.191 81.617  21.322  1.00 23.42 ? 210  GLY A N   1 
ATOM   1649 C CA  . GLY A 1 210 ? 53.038 82.281  20.028  1.00 22.70 ? 210  GLY A CA  1 
ATOM   1650 C C   . GLY A 1 210 ? 51.608 82.552  19.565  1.00 21.82 ? 210  GLY A C   1 
ATOM   1651 O O   . GLY A 1 210 ? 51.325 82.499  18.355  1.00 21.70 ? 210  GLY A O   1 
ATOM   1652 N N   . THR A 1 211 ? 50.698 82.820  20.503  1.00 20.56 ? 211  THR A N   1 
ATOM   1653 C CA  . THR A 1 211 ? 49.286 83.025  20.122  1.00 19.38 ? 211  THR A CA  1 
ATOM   1654 C C   . THR A 1 211 ? 49.028 84.484  19.695  1.00 18.39 ? 211  THR A C   1 
ATOM   1655 O O   . THR A 1 211 ? 49.897 85.368  19.899  1.00 17.14 ? 211  THR A O   1 
ATOM   1656 C CB  . THR A 1 211 ? 48.318 82.711  21.289  1.00 20.00 ? 211  THR A CB  1 
ATOM   1657 O OG1 . THR A 1 211 ? 48.368 83.762  22.280  1.00 21.98 ? 211  THR A OG1 1 
ATOM   1658 C CG2 . THR A 1 211 ? 48.640 81.383  21.935  1.00 19.38 ? 211  THR A CG2 1 
ATOM   1659 N N   . ASN A 1 212 ? 47.843 84.738  19.117  1.00 16.29 ? 212  ASN A N   1 
ATOM   1660 C CA  . ASN A 1 212 ? 47.314 86.078  19.018  1.00 16.28 ? 212  ASN A CA  1 
ATOM   1661 C C   . ASN A 1 212 ? 47.210 86.759  20.394  1.00 16.68 ? 212  ASN A C   1 
ATOM   1662 O O   . ASN A 1 212 ? 46.714 86.156  21.397  1.00 17.83 ? 212  ASN A O   1 
ATOM   1663 C CB  . ASN A 1 212 ? 45.925 86.090  18.316  1.00 15.57 ? 212  ASN A CB  1 
ATOM   1664 C CG  . ASN A 1 212 ? 44.963 85.079  18.917  1.00 17.43 ? 212  ASN A CG  1 
ATOM   1665 O OD1 . ASN A 1 212 ? 45.335 83.943  19.143  1.00 15.08 ? 212  ASN A OD1 1 
ATOM   1666 N ND2 . ASN A 1 212 ? 43.720 85.504  19.199  1.00 14.85 ? 212  ASN A ND2 1 
ATOM   1667 N N   . LEU A 1 213 ? 47.648 88.017  20.470  1.00 15.59 ? 213  LEU A N   1 
ATOM   1668 C CA  . LEU A 1 213 ? 47.499 88.764  21.734  1.00 15.45 ? 213  LEU A CA  1 
ATOM   1669 C C   . LEU A 1 213 ? 46.559 89.941  21.574  1.00 15.24 ? 213  LEU A C   1 
ATOM   1670 O O   . LEU A 1 213 ? 45.662 89.851  20.755  1.00 15.08 ? 213  LEU A O   1 
ATOM   1671 C CB  . LEU A 1 213 ? 48.859 89.150  22.369  1.00 15.55 ? 213  LEU A CB  1 
ATOM   1672 C CG  . LEU A 1 213 ? 49.772 87.938  22.589  1.00 15.75 ? 213  LEU A CG  1 
ATOM   1673 C CD1 . LEU A 1 213 ? 51.152 88.461  22.940  1.00 15.68 ? 213  LEU A CD1 1 
ATOM   1674 C CD2 . LEU A 1 213 ? 49.237 87.045  23.716  1.00 17.27 ? 213  LEU A CD2 1 
ATOM   1675 N N   . TYR A 1 214 ? 46.804 91.033  22.309  1.00 14.97 ? 214  TYR A N   1 
ATOM   1676 C CA  . TYR A 1 214 ? 45.833 92.117  22.507  1.00 16.54 ? 214  TYR A CA  1 
ATOM   1677 C C   . TYR A 1 214 ? 45.517 93.002  21.301  1.00 16.61 ? 214  TYR A C   1 
ATOM   1678 O O   . TYR A 1 214 ? 44.386 93.552  21.200  1.00 16.85 ? 214  TYR A O   1 
ATOM   1679 C CB  . TYR A 1 214 ? 46.243 93.015  23.681  1.00 15.04 ? 214  TYR A CB  1 
ATOM   1680 C CG  . TYR A 1 214 ? 46.729 92.253  24.859  1.00 15.67 ? 214  TYR A CG  1 
ATOM   1681 C CD1 . TYR A 1 214 ? 45.822 91.640  25.727  1.00 15.33 ? 214  TYR A CD1 1 
ATOM   1682 C CD2 . TYR A 1 214 ? 48.103 92.131  25.125  1.00 14.96 ? 214  TYR A CD2 1 
ATOM   1683 C CE1 . TYR A 1 214 ? 46.266 90.934  26.827  1.00 16.95 ? 214  TYR A CE1 1 
ATOM   1684 C CE2 . TYR A 1 214 ? 48.548 91.415  26.215  1.00 13.18 ? 214  TYR A CE2 1 
ATOM   1685 C CZ  . TYR A 1 214 ? 47.622 90.847  27.081  1.00 14.85 ? 214  TYR A CZ  1 
ATOM   1686 O OH  . TYR A 1 214 ? 48.036 90.163  28.195  1.00 15.71 ? 214  TYR A OH  1 
ATOM   1687 N N   . GLY A 1 215 ? 46.478 93.112  20.387  1.00 16.26 ? 215  GLY A N   1 
ATOM   1688 C CA  . GLY A 1 215 ? 46.370 94.046  19.264  1.00 16.72 ? 215  GLY A CA  1 
ATOM   1689 C C   . GLY A 1 215 ? 46.602 93.460  17.883  1.00 17.21 ? 215  GLY A C   1 
ATOM   1690 O O   . GLY A 1 215 ? 47.063 92.313  17.731  1.00 17.04 ? 215  GLY A O   1 
ATOM   1691 N N   . ALA A 1 216 ? 46.261 94.242  16.863  1.00 17.01 ? 216  ALA A N   1 
ATOM   1692 C CA  . ALA A 1 216 ? 46.349 93.767  15.482  1.00 16.97 ? 216  ALA A CA  1 
ATOM   1693 C C   . ALA A 1 216 ? 47.278 94.671  14.672  1.00 16.47 ? 216  ALA A C   1 
ATOM   1694 O O   . ALA A 1 216 ? 46.969 95.836  14.432  1.00 16.27 ? 216  ALA A O   1 
ATOM   1695 C CB  . ALA A 1 216 ? 44.971 93.736  14.854  1.00 16.33 ? 216  ALA A CB  1 
ATOM   1696 N N   . GLN A 1 217 ? 48.404 94.125  14.250  1.00 16.41 ? 217  GLN A N   1 
ATOM   1697 C CA  . GLN A 1 217 ? 49.409 94.949  13.538  1.00 16.77 ? 217  GLN A CA  1 
ATOM   1698 C C   . GLN A 1 217 ? 49.936 94.197  12.328  1.00 16.34 ? 217  GLN A C   1 
ATOM   1699 O O   . GLN A 1 217 ? 50.643 93.236  12.471  1.00 16.95 ? 217  GLN A O   1 
ATOM   1700 C CB  . GLN A 1 217 ? 50.563 95.309  14.486  1.00 16.96 ? 217  GLN A CB  1 
ATOM   1701 C CG  . GLN A 1 217 ? 50.174 96.122  15.697  1.00 15.70 ? 217  GLN A CG  1 
ATOM   1702 C CD  . GLN A 1 217 ? 49.779 97.547  15.362  1.00 15.57 ? 217  GLN A CD  1 
ATOM   1703 O OE1 . GLN A 1 217 ? 50.145 98.089  14.302  1.00 17.75 ? 217  GLN A OE1 1 
ATOM   1704 N NE2 . GLN A 1 217 ? 49.041 98.182  16.273  1.00 13.51 ? 217  GLN A NE2 1 
ATOM   1705 N N   . THR A 1 218 ? 49.581 94.625  11.131  1.00 17.42 ? 218  THR A N   1 
ATOM   1706 C CA  . THR A 1 218 ? 49.954 93.852  9.949   1.00 18.35 ? 218  THR A CA  1 
ATOM   1707 C C   . THR A 1 218 ? 51.256 94.317  9.308   1.00 19.38 ? 218  THR A C   1 
ATOM   1708 O O   . THR A 1 218 ? 51.757 93.665  8.396   1.00 20.66 ? 218  THR A O   1 
ATOM   1709 C CB  . THR A 1 218 ? 48.862 93.829  8.891   1.00 18.91 ? 218  THR A CB  1 
ATOM   1710 O OG1 . THR A 1 218 ? 48.646 95.158  8.393   1.00 18.98 ? 218  THR A OG1 1 
ATOM   1711 C CG2 . THR A 1 218 ? 47.525 93.226  9.462   1.00 17.06 ? 218  THR A CG2 1 
ATOM   1712 N N   . PHE A 1 219 ? 51.818 95.413  9.811   1.00 18.71 ? 219  PHE A N   1 
ATOM   1713 C CA  . PHE A 1 219 ? 53.046 95.985  9.232   1.00 17.87 ? 219  PHE A CA  1 
ATOM   1714 C C   . PHE A 1 219 ? 54.274 95.128  9.460   1.00 17.61 ? 219  PHE A C   1 
ATOM   1715 O O   . PHE A 1 219 ? 54.474 94.593  10.558  1.00 16.49 ? 219  PHE A O   1 
ATOM   1716 C CB  . PHE A 1 219 ? 53.292 97.361  9.813   1.00 18.01 ? 219  PHE A CB  1 
ATOM   1717 C CG  . PHE A 1 219 ? 54.595 98.012  9.351   1.00 16.73 ? 219  PHE A CG  1 
ATOM   1718 C CD1 . PHE A 1 219 ? 54.706 98.531  8.043   1.00 18.16 ? 219  PHE A CD1 1 
ATOM   1719 C CD2 . PHE A 1 219 ? 55.667 98.138  10.208  1.00 17.39 ? 219  PHE A CD2 1 
ATOM   1720 C CE1 . PHE A 1 219 ? 55.867 99.161  7.607   1.00 17.21 ? 219  PHE A CE1 1 
ATOM   1721 C CE2 . PHE A 1 219 ? 56.872 98.762  9.750   1.00 17.02 ? 219  PHE A CE2 1 
ATOM   1722 C CZ  . PHE A 1 219 ? 56.935 99.281  8.451   1.00 15.79 ? 219  PHE A CZ  1 
ATOM   1723 N N   . PHE A 1 220 ? 55.089 94.992  8.407   1.00 17.84 ? 220  PHE A N   1 
ATOM   1724 C CA  . PHE A 1 220 ? 56.437 94.458  8.539   1.00 17.56 ? 220  PHE A CA  1 
ATOM   1725 C C   . PHE A 1 220 ? 57.446 95.265  7.701   1.00 18.11 ? 220  PHE A C   1 
ATOM   1726 O O   . PHE A 1 220 ? 57.103 95.850  6.665   1.00 18.77 ? 220  PHE A O   1 
ATOM   1727 C CB  . PHE A 1 220 ? 56.514 92.956  8.234   1.00 18.41 ? 220  PHE A CB  1 
ATOM   1728 C CG  . PHE A 1 220 ? 56.462 92.608  6.767   1.00 18.97 ? 220  PHE A CG  1 
ATOM   1729 C CD1 . PHE A 1 220 ? 57.604 92.680  5.962   1.00 18.47 ? 220  PHE A CD1 1 
ATOM   1730 C CD2 . PHE A 1 220 ? 55.269 92.198  6.182   1.00 21.24 ? 220  PHE A CD2 1 
ATOM   1731 C CE1 . PHE A 1 220 ? 57.557 92.366  4.608   1.00 20.38 ? 220  PHE A CE1 1 
ATOM   1732 C CE2 . PHE A 1 220 ? 55.209 91.879  4.828   1.00 19.41 ? 220  PHE A CE2 1 
ATOM   1733 C CZ  . PHE A 1 220 ? 56.356 91.958  4.035   1.00 19.88 ? 220  PHE A CZ  1 
ATOM   1734 N N   . LEU A 1 221 ? 58.674 95.321  8.184   1.00 17.44 ? 221  LEU A N   1 
ATOM   1735 C CA  . LEU A 1 221 ? 59.763 95.997  7.485   1.00 17.05 ? 221  LEU A CA  1 
ATOM   1736 C C   . LEU A 1 221 ? 60.740 94.922  7.011   1.00 16.96 ? 221  LEU A C   1 
ATOM   1737 O O   . LEU A 1 221 ? 60.956 93.934  7.702   1.00 17.50 ? 221  LEU A O   1 
ATOM   1738 C CB  . LEU A 1 221 ? 60.454 96.949  8.478   1.00 15.84 ? 221  LEU A CB  1 
ATOM   1739 C CG  . LEU A 1 221 ? 61.616 97.881  8.071   1.00 17.56 ? 221  LEU A CG  1 
ATOM   1740 C CD1 . LEU A 1 221 ? 61.624 99.108  8.985   1.00 14.89 ? 221  LEU A CD1 1 
ATOM   1741 C CD2 . LEU A 1 221 ? 62.881 97.147  8.230   1.00 15.55 ? 221  LEU A CD2 1 
ATOM   1742 N N   . CYS A 1 222 ? 61.357 95.111  5.849   1.00 17.11 ? 222  CYS A N   1 
ATOM   1743 C CA  . CYS A 1 222 ? 62.378 94.163  5.401   1.00 16.16 ? 222  CYS A CA  1 
ATOM   1744 C C   . CYS A 1 222 ? 63.666 94.962  5.046   1.00 15.49 ? 222  CYS A C   1 
ATOM   1745 O O   . CYS A 1 222 ? 63.620 95.901  4.268   1.00 15.02 ? 222  CYS A O   1 
ATOM   1746 C CB  . CYS A 1 222 ? 61.856 93.368  4.183   1.00 15.27 ? 222  CYS A CB  1 
ATOM   1747 S SG  . CYS A 1 222 ? 63.088 92.323  3.307   1.00 18.91 ? 222  CYS A SG  1 
ATOM   1748 N N   . LEU A 1 223 ? 64.788 94.595  5.644   1.00 16.42 ? 223  LEU A N   1 
ATOM   1749 C CA  . LEU A 1 223 ? 66.087 95.194  5.273   1.00 16.16 ? 223  LEU A CA  1 
ATOM   1750 C C   . LEU A 1 223 ? 66.625 94.377  4.112   1.00 17.60 ? 223  LEU A C   1 
ATOM   1751 O O   . LEU A 1 223 ? 66.908 93.192  4.278   1.00 17.15 ? 223  LEU A O   1 
ATOM   1752 C CB  . LEU A 1 223 ? 67.073 95.182  6.459   1.00 16.13 ? 223  LEU A CB  1 
ATOM   1753 C CG  . LEU A 1 223 ? 68.566 95.471  6.155   1.00 15.65 ? 223  LEU A CG  1 
ATOM   1754 C CD1 . LEU A 1 223 ? 68.718 96.875  5.554   1.00 13.62 ? 223  LEU A CD1 1 
ATOM   1755 C CD2 . LEU A 1 223 ? 69.444 95.269  7.393   1.00 15.05 ? 223  LEU A CD2 1 
ATOM   1756 N N   . GLU A 1 224 ? 66.762 94.998  2.940   1.00 18.61 ? 224  GLU A N   1 
ATOM   1757 C CA  . GLU A 1 224 ? 67.061 94.253  1.707   1.00 21.13 ? 224  GLU A CA  1 
ATOM   1758 C C   . GLU A 1 224 ? 68.499 93.754  1.633   1.00 21.81 ? 224  GLU A C   1 
ATOM   1759 O O   . GLU A 1 224 ? 68.750 92.648  1.174   1.00 21.99 ? 224  GLU A O   1 
ATOM   1760 C CB  . GLU A 1 224 ? 66.767 95.118  0.465   1.00 21.03 ? 224  GLU A CB  1 
ATOM   1761 C CG  . GLU A 1 224 ? 65.325 95.524  0.316   1.00 21.81 ? 224  GLU A CG  1 
ATOM   1762 C CD  . GLU A 1 224 ? 65.122 96.721  -0.623  1.00 23.14 ? 224  GLU A CD  1 
ATOM   1763 O OE1 . GLU A 1 224 ? 65.824 96.881  -1.669  1.00 25.33 ? 224  GLU A OE1 1 
ATOM   1764 O OE2 . GLU A 1 224 ? 64.235 97.523  -0.294  1.00 25.09 ? 224  GLU A OE2 1 
ATOM   1765 N N   . ASP A 1 225 ? 69.440 94.596  2.064   1.00 23.02 ? 225  ASP A N   1 
ATOM   1766 C CA  . ASP A 1 225 ? 70.885 94.316  1.981   1.00 22.36 ? 225  ASP A CA  1 
ATOM   1767 C C   . ASP A 1 225 ? 71.662 95.275  2.895   1.00 22.58 ? 225  ASP A C   1 
ATOM   1768 O O   . ASP A 1 225 ? 71.067 96.195  3.517   1.00 20.00 ? 225  ASP A O   1 
ATOM   1769 C CB  . ASP A 1 225 ? 71.400 94.408  0.497   1.00 23.41 ? 225  ASP A CB  1 
ATOM   1770 C CG  . ASP A 1 225 ? 71.115 95.775  -0.174  1.00 25.02 ? 225  ASP A CG  1 
ATOM   1771 O OD1 . ASP A 1 225 ? 71.310 96.846  0.478   1.00 28.01 ? 225  ASP A OD1 1 
ATOM   1772 O OD2 . ASP A 1 225 ? 70.673 95.799  -1.365  1.00 25.33 ? 225  ASP A OD2 1 
ATOM   1773 N N   . ALA A 1 226 ? 72.991 95.069  2.969   1.00 21.86 ? 226  ALA A N   1 
ATOM   1774 C CA  . ALA A 1 226 ? 73.897 95.914  3.783   1.00 21.88 ? 226  ALA A CA  1 
ATOM   1775 C C   . ALA A 1 226 ? 73.887 97.402  3.409   1.00 22.11 ? 226  ALA A C   1 
ATOM   1776 O O   . ALA A 1 226 ? 74.263 98.246  4.224   1.00 23.69 ? 226  ALA A O   1 
ATOM   1777 C CB  . ALA A 1 226 ? 75.367 95.364  3.720   1.00 20.99 ? 226  ALA A CB  1 
ATOM   1778 N N   . SER A 1 227 ? 73.496 97.754  2.185   1.00 21.00 ? 227  SER A N   1 
ATOM   1779 C CA  . SER A 1 227 ? 73.479 99.169  1.828   1.00 21.45 ? 227  SER A CA  1 
ATOM   1780 C C   . SER A 1 227 ? 72.423 99.959  2.632   1.00 20.44 ? 227  SER A C   1 
ATOM   1781 O O   . SER A 1 227 ? 72.473 101.171 2.674   1.00 20.57 ? 227  SER A O   1 
ATOM   1782 C CB  . SER A 1 227 ? 73.246 99.377  0.339   1.00 21.92 ? 227  SER A CB  1 
ATOM   1783 O OG  . SER A 1 227 ? 71.879 99.139  0.019   1.00 24.61 ? 227  SER A OG  1 
ATOM   1784 N N   . GLY A 1 228 ? 71.489 99.266  3.279   1.00 19.81 ? 228  GLY A N   1 
ATOM   1785 C CA  . GLY A 1 228 ? 70.430 99.949  4.065   1.00 18.92 ? 228  GLY A CA  1 
ATOM   1786 C C   . GLY A 1 228 ? 69.102 99.966  3.367   1.00 17.81 ? 228  GLY A C   1 
ATOM   1787 O O   . GLY A 1 228 ? 68.069 100.200 3.998   1.00 18.35 ? 228  GLY A O   1 
ATOM   1788 N N   . LEU A 1 229 ? 69.088 99.678  2.069   1.00 17.88 ? 229  LEU A N   1 
ATOM   1789 C CA  . LEU A 1 229 ? 67.841 99.795  1.286   1.00 17.53 ? 229  LEU A CA  1 
ATOM   1790 C C   . LEU A 1 229 ? 66.799 98.854  1.924   1.00 17.62 ? 229  LEU A C   1 
ATOM   1791 O O   . LEU A 1 229 ? 67.121 97.728  2.250   1.00 17.13 ? 229  LEU A O   1 
ATOM   1792 C CB  . LEU A 1 229 ? 68.077 99.474  -0.199  1.00 17.02 ? 229  LEU A CB  1 
ATOM   1793 C CG  . LEU A 1 229 ? 69.049 100.406 -0.967  1.00 18.36 ? 229  LEU A CG  1 
ATOM   1794 C CD1 . LEU A 1 229 ? 69.294 99.954  -2.389  1.00 18.61 ? 229  LEU A CD1 1 
ATOM   1795 C CD2 . LEU A 1 229 ? 68.552 101.812 -1.005  1.00 17.21 ? 229  LEU A CD2 1 
ATOM   1796 N N   . SER A 1 230 ? 65.576 99.340  2.129   1.00 16.88 ? 230  SER A N   1 
ATOM   1797 C CA  . SER A 1 230 ? 64.616 98.632  2.925   1.00 16.51 ? 230  SER A CA  1 
ATOM   1798 C C   . SER A 1 230 ? 63.224 98.950  2.325   1.00 16.76 ? 230  SER A C   1 
ATOM   1799 O O   . SER A 1 230 ? 63.052 99.944  1.616   1.00 15.25 ? 230  SER A O   1 
ATOM   1800 C CB  . SER A 1 230 ? 64.716 99.123  4.400   1.00 15.62 ? 230  SER A CB  1 
ATOM   1801 O OG  . SER A 1 230 ? 65.944 98.748  4.997   1.00 17.66 ? 230  SER A OG  1 
ATOM   1802 N N   . PHE A 1 231 ? 62.234 98.118  2.629   1.00 16.53 ? 231  PHE A N   1 
ATOM   1803 C CA  . PHE A 1 231 ? 60.869 98.407  2.203   1.00 16.76 ? 231  PHE A CA  1 
ATOM   1804 C C   . PHE A 1 231 ? 59.950 97.874  3.322   1.00 17.27 ? 231  PHE A C   1 
ATOM   1805 O O   . PHE A 1 231 ? 60.413 97.150  4.248   1.00 16.88 ? 231  PHE A O   1 
ATOM   1806 C CB  . PHE A 1 231 ? 60.542 97.836  0.772   1.00 16.95 ? 231  PHE A CB  1 
ATOM   1807 C CG  . PHE A 1 231 ? 60.239 96.356  0.745   1.00 16.90 ? 231  PHE A CG  1 
ATOM   1808 C CD1 . PHE A 1 231 ? 58.923 95.903  0.652   1.00 20.24 ? 231  PHE A CD1 1 
ATOM   1809 C CD2 . PHE A 1 231 ? 61.264 95.411  0.804   1.00 19.81 ? 231  PHE A CD2 1 
ATOM   1810 C CE1 . PHE A 1 231 ? 58.634 94.541  0.633   1.00 16.75 ? 231  PHE A CE1 1 
ATOM   1811 C CE2 . PHE A 1 231 ? 60.978 94.045  0.794   1.00 18.59 ? 231  PHE A CE2 1 
ATOM   1812 C CZ  . PHE A 1 231 ? 59.671 93.620  0.731   1.00 19.29 ? 231  PHE A CZ  1 
ATOM   1813 N N   . GLY A 1 232 ? 58.687 98.303  3.297   1.00 16.45 ? 232  GLY A N   1 
ATOM   1814 C CA  . GLY A 1 232 ? 57.736 97.782  4.257   1.00 16.33 ? 232  GLY A CA  1 
ATOM   1815 C C   . GLY A 1 232 ? 56.471 97.447  3.529   1.00 16.36 ? 232  GLY A C   1 
ATOM   1816 O O   . GLY A 1 232 ? 56.277 97.918  2.387   1.00 15.81 ? 232  GLY A O   1 
ATOM   1817 N N   . VAL A 1 233 ? 55.610 96.647  4.175   1.00 16.23 ? 233  VAL A N   1 
ATOM   1818 C CA  . VAL A 1 233 ? 54.314 96.279  3.626   1.00 15.23 ? 233  VAL A CA  1 
ATOM   1819 C C   . VAL A 1 233 ? 53.281 96.462  4.738   1.00 15.48 ? 233  VAL A C   1 
ATOM   1820 O O   . VAL A 1 233 ? 53.527 96.094  5.881   1.00 13.26 ? 233  VAL A O   1 
ATOM   1821 C CB  . VAL A 1 233 ? 54.229 94.787  3.079   1.00 15.87 ? 233  VAL A CB  1 
ATOM   1822 C CG1 . VAL A 1 233 ? 52.747 94.430  2.660   1.00 16.23 ? 233  VAL A CG1 1 
ATOM   1823 C CG2 . VAL A 1 233 ? 55.140 94.568  1.923   1.00 16.94 ? 233  VAL A CG2 1 
ATOM   1824 N N   . PHE A 1 234 ? 52.128 97.040  4.387   1.00 14.77 ? 234  PHE A N   1 
ATOM   1825 C CA  . PHE A 1 234 ? 51.015 97.136  5.328   1.00 15.39 ? 234  PHE A CA  1 
ATOM   1826 C C   . PHE A 1 234 ? 49.698 96.603  4.675   1.00 15.75 ? 234  PHE A C   1 
ATOM   1827 O O   . PHE A 1 234 ? 49.396 96.981  3.546   1.00 14.53 ? 234  PHE A O   1 
ATOM   1828 C CB  . PHE A 1 234 ? 50.841 98.587  5.824   1.00 15.27 ? 234  PHE A CB  1 
ATOM   1829 C CG  . PHE A 1 234 ? 49.630 98.785  6.681   1.00 16.55 ? 234  PHE A CG  1 
ATOM   1830 C CD1 . PHE A 1 234 ? 49.521 98.129  7.909   1.00 15.38 ? 234  PHE A CD1 1 
ATOM   1831 C CD2 . PHE A 1 234 ? 48.583 99.622  6.260   1.00 13.24 ? 234  PHE A CD2 1 
ATOM   1832 C CE1 . PHE A 1 234 ? 48.372 98.271  8.698   1.00 16.92 ? 234  PHE A CE1 1 
ATOM   1833 C CE2 . PHE A 1 234 ? 47.430 99.770  7.059   1.00 17.22 ? 234  PHE A CE2 1 
ATOM   1834 C CZ  . PHE A 1 234 ? 47.338 99.102  8.287   1.00 13.77 ? 234  PHE A CZ  1 
ATOM   1835 N N   . LEU A 1 235 ? 48.947 95.739  5.397   1.00 14.78 ? 235  LEU A N   1 
ATOM   1836 C CA  . LEU A 1 235 ? 47.570 95.349  4.992   1.00 14.93 ? 235  LEU A CA  1 
ATOM   1837 C C   . LEU A 1 235 ? 46.530 96.035  5.853   1.00 14.52 ? 235  LEU A C   1 
ATOM   1838 O O   . LEU A 1 235 ? 46.492 95.821  7.055   1.00 13.25 ? 235  LEU A O   1 
ATOM   1839 C CB  . LEU A 1 235 ? 47.379 93.828  5.104   1.00 14.88 ? 235  LEU A CB  1 
ATOM   1840 C CG  . LEU A 1 235 ? 46.006 93.244  4.830   1.00 14.26 ? 235  LEU A CG  1 
ATOM   1841 C CD1 . LEU A 1 235 ? 45.522 93.639  3.463   1.00 11.80 ? 235  LEU A CD1 1 
ATOM   1842 C CD2 . LEU A 1 235 ? 46.014 91.719  4.987   1.00 15.63 ? 235  LEU A CD2 1 
ATOM   1843 N N   . MET A 1 236 ? 45.701 96.869  5.228   1.00 15.66 ? 236  MET A N   1 
ATOM   1844 C CA  . MET A 1 236 ? 44.602 97.537  5.881   1.00 16.95 ? 236  MET A CA  1 
ATOM   1845 C C   . MET A 1 236 ? 43.381 96.601  5.876   1.00 18.67 ? 236  MET A C   1 
ATOM   1846 O O   . MET A 1 236 ? 42.549 96.623  4.943   1.00 18.49 ? 236  MET A O   1 
ATOM   1847 C CB  . MET A 1 236 ? 44.307 98.803  5.109   1.00 16.90 ? 236  MET A CB  1 
ATOM   1848 C CG  . MET A 1 236 ? 43.209 99.672  5.687   1.00 18.60 ? 236  MET A CG  1 
ATOM   1849 S SD  . MET A 1 236 ? 43.538 100.371 7.302   1.00 22.00 ? 236  MET A SD  1 
ATOM   1850 C CE  . MET A 1 236 ? 44.209 101.975 6.838   1.00 20.94 ? 236  MET A CE  1 
ATOM   1851 N N   . ASN A 1 237 ? 43.277 95.769  6.909   1.00 19.24 ? 237  ASN A N   1 
ATOM   1852 C CA  . ASN A 1 237 ? 42.180 94.788  6.997   1.00 19.74 ? 237  ASN A CA  1 
ATOM   1853 C C   . ASN A 1 237 ? 42.034 94.446  8.480   1.00 20.05 ? 237  ASN A C   1 
ATOM   1854 O O   . ASN A 1 237 ? 43.039 94.116  9.135   1.00 20.05 ? 237  ASN A O   1 
ATOM   1855 C CB  . ASN A 1 237 ? 42.532 93.550  6.128   1.00 19.09 ? 237  ASN A CB  1 
ATOM   1856 C CG  . ASN A 1 237 ? 41.466 92.458  6.154   1.00 22.39 ? 237  ASN A CG  1 
ATOM   1857 O OD1 . ASN A 1 237 ? 41.350 91.743  7.135   1.00 22.32 ? 237  ASN A OD1 1 
ATOM   1858 N ND2 . ASN A 1 237 ? 40.741 92.281  5.040   1.00 20.90 ? 237  ASN A ND2 1 
ATOM   1859 N N   . SER A 1 238 ? 40.810 94.562  9.016   1.00 19.37 ? 238  SER A N   1 
ATOM   1860 C CA  . SER A 1 238 ? 40.551 94.316  10.430  1.00 19.42 ? 238  SER A CA  1 
ATOM   1861 C C   . SER A 1 238 ? 39.901 92.952  10.766  1.00 20.28 ? 238  SER A C   1 
ATOM   1862 O O   . SER A 1 238 ? 39.503 92.709  11.928  1.00 21.47 ? 238  SER A O   1 
ATOM   1863 C CB  . SER A 1 238 ? 39.708 95.459  11.008  1.00 18.85 ? 238  SER A CB  1 
ATOM   1864 O OG  . SER A 1 238 ? 38.491 95.642  10.296  1.00 20.57 ? 238  SER A OG  1 
ATOM   1865 N N   . ASN A 1 239 ? 39.775 92.064  9.773   1.00 19.57 ? 239  ASN A N   1 
ATOM   1866 C CA  . ASN A 1 239 ? 39.201 90.744  10.007  1.00 19.42 ? 239  ASN A CA  1 
ATOM   1867 C C   . ASN A 1 239 ? 40.219 89.832  10.657  1.00 19.34 ? 239  ASN A C   1 
ATOM   1868 O O   . ASN A 1 239 ? 41.415 90.074  10.509  1.00 19.11 ? 239  ASN A O   1 
ATOM   1869 C CB  . ASN A 1 239 ? 38.703 90.141  8.691   1.00 18.46 ? 239  ASN A CB  1 
ATOM   1870 C CG  . ASN A 1 239 ? 37.451 90.844  8.179   1.00 20.62 ? 239  ASN A CG  1 
ATOM   1871 O OD1 . ASN A 1 239 ? 36.329 90.411  8.448   1.00 25.49 ? 239  ASN A OD1 1 
ATOM   1872 N ND2 . ASN A 1 239 ? 37.630 91.949  7.498   1.00 17.25 ? 239  ASN A ND2 1 
ATOM   1873 N N   . ALA A 1 240 ? 39.759 88.791  11.357  1.00 18.44 ? 240  ALA A N   1 
ATOM   1874 C CA  . ALA A 1 240 ? 40.663 87.720  11.818  1.00 19.14 ? 240  ALA A CA  1 
ATOM   1875 C C   . ALA A 1 240 ? 41.532 87.227  10.662  1.00 19.34 ? 240  ALA A C   1 
ATOM   1876 O O   . ALA A 1 240 ? 41.058 86.998  9.537   1.00 19.19 ? 240  ALA A O   1 
ATOM   1877 C CB  . ALA A 1 240 ? 39.865 86.510  12.419  1.00 19.16 ? 240  ALA A CB  1 
ATOM   1878 N N   . MET A 1 241 ? 42.804 87.017  10.935  1.00 18.35 ? 241  MET A N   1 
ATOM   1879 C CA  . MET A 1 241 ? 43.676 86.680  9.864   1.00 19.30 ? 241  MET A CA  1 
ATOM   1880 C C   . MET A 1 241 ? 44.859 85.930  10.463  1.00 18.74 ? 241  MET A C   1 
ATOM   1881 O O   . MET A 1 241 ? 44.993 85.883  11.665  1.00 17.74 ? 241  MET A O   1 
ATOM   1882 C CB  . MET A 1 241 ? 44.100 87.964  9.158   1.00 18.63 ? 241  MET A CB  1 
ATOM   1883 C CG  . MET A 1 241 ? 45.302 88.692  9.833   1.00 20.28 ? 241  MET A CG  1 
ATOM   1884 S SD  . MET A 1 241 ? 45.980 89.966  8.710   1.00 22.47 ? 241  MET A SD  1 
ATOM   1885 C CE  . MET A 1 241 ? 44.564 91.040  8.677   1.00 15.58 ? 241  MET A CE  1 
ATOM   1886 N N   . GLU A 1 242 ? 45.658 85.293  9.621   1.00 19.36 ? 242  GLU A N   1 
ATOM   1887 C CA  . GLU A 1 242 ? 47.002 84.863  10.017  1.00 20.20 ? 242  GLU A CA  1 
ATOM   1888 C C   . GLU A 1 242 ? 47.983 85.173  8.904   1.00 20.23 ? 242  GLU A C   1 
ATOM   1889 O O   . GLU A 1 242 ? 47.597 85.364  7.744   1.00 21.67 ? 242  GLU A O   1 
ATOM   1890 C CB  . GLU A 1 242 ? 47.070 83.383  10.423  1.00 19.88 ? 242  GLU A CB  1 
ATOM   1891 C CG  . GLU A 1 242 ? 46.739 82.398  9.315   1.00 21.14 ? 242  GLU A CG  1 
ATOM   1892 C CD  . GLU A 1 242 ? 46.126 81.083  9.872   1.00 28.09 ? 242  GLU A CD  1 
ATOM   1893 O OE1 . GLU A 1 242 ? 45.767 81.034  11.074  1.00 29.52 ? 242  GLU A OE1 1 
ATOM   1894 O OE2 . GLU A 1 242 ? 46.015 80.099  9.114   1.00 27.58 ? 242  GLU A OE2 1 
ATOM   1895 N N   . VAL A 1 243 ? 49.249 85.249  9.281   1.00 19.64 ? 243  VAL A N   1 
ATOM   1896 C CA  . VAL A 1 243 ? 50.345 85.584  8.379   1.00 19.03 ? 243  VAL A CA  1 
ATOM   1897 C C   . VAL A 1 243 ? 51.290 84.366  8.395   1.00 18.16 ? 243  VAL A C   1 
ATOM   1898 O O   . VAL A 1 243 ? 51.737 83.927  9.451   1.00 17.52 ? 243  VAL A O   1 
ATOM   1899 C CB  . VAL A 1 243 ? 51.071 86.849  8.883   1.00 19.46 ? 243  VAL A CB  1 
ATOM   1900 C CG1 . VAL A 1 243 ? 52.149 87.309  7.895   1.00 20.78 ? 243  VAL A CG1 1 
ATOM   1901 C CG2 . VAL A 1 243 ? 50.079 87.985  9.097   1.00 19.34 ? 243  VAL A CG2 1 
ATOM   1902 N N   . VAL A 1 244 ? 51.560 83.811  7.223   1.00 17.22 ? 244  VAL A N   1 
ATOM   1903 C CA  . VAL A 1 244 ? 52.310 82.555  7.099   1.00 16.94 ? 244  VAL A CA  1 
ATOM   1904 C C   . VAL A 1 244 ? 53.691 82.900  6.535   1.00 17.20 ? 244  VAL A C   1 
ATOM   1905 O O   . VAL A 1 244 ? 53.778 83.547  5.498   1.00 17.12 ? 244  VAL A O   1 
ATOM   1906 C CB  . VAL A 1 244 ? 51.545 81.551  6.164   1.00 16.37 ? 244  VAL A CB  1 
ATOM   1907 C CG1 . VAL A 1 244 ? 52.229 80.176  6.122   1.00 14.69 ? 244  VAL A CG1 1 
ATOM   1908 C CG2 . VAL A 1 244 ? 50.072 81.381  6.671   1.00 15.75 ? 244  VAL A CG2 1 
ATOM   1909 N N   . LEU A 1 245 ? 54.746 82.459  7.204   1.00 17.19 ? 245  LEU A N   1 
ATOM   1910 C CA  . LEU A 1 245 ? 56.111 82.779  6.771   1.00 18.23 ? 245  LEU A CA  1 
ATOM   1911 C C   . LEU A 1 245 ? 56.719 81.481  6.344   1.00 18.06 ? 245  LEU A C   1 
ATOM   1912 O O   . LEU A 1 245 ? 56.528 80.471  7.005   1.00 17.38 ? 245  LEU A O   1 
ATOM   1913 C CB  . LEU A 1 245 ? 56.961 83.388  7.920   1.00 17.88 ? 245  LEU A CB  1 
ATOM   1914 C CG  . LEU A 1 245 ? 56.390 84.600  8.684   1.00 20.14 ? 245  LEU A CG  1 
ATOM   1915 C CD1 . LEU A 1 245 ? 57.436 85.192  9.646   1.00 24.11 ? 245  LEU A CD1 1 
ATOM   1916 C CD2 . LEU A 1 245 ? 56.025 85.610  7.743   1.00 20.76 ? 245  LEU A CD2 1 
ATOM   1917 N N   . GLN A 1 246 ? 57.450 81.483  5.241   1.00 19.18 ? 246  GLN A N   1 
ATOM   1918 C CA  . GLN A 1 246 ? 58.154 80.250  4.819   1.00 19.10 ? 246  GLN A CA  1 
ATOM   1919 C C   . GLN A 1 246 ? 59.511 80.565  4.191   1.00 18.65 ? 246  GLN A C   1 
ATOM   1920 O O   . GLN A 1 246 ? 59.720 81.706  3.839   1.00 18.02 ? 246  GLN A O   1 
ATOM   1921 C CB  . GLN A 1 246 ? 57.268 79.468  3.876   1.00 18.42 ? 246  GLN A CB  1 
ATOM   1922 C CG  . GLN A 1 246 ? 57.006 80.135  2.569   1.00 19.39 ? 246  GLN A CG  1 
ATOM   1923 C CD  . GLN A 1 246 ? 55.888 79.414  1.862   1.00 20.80 ? 246  GLN A CD  1 
ATOM   1924 O OE1 . GLN A 1 246 ? 54.710 79.605  2.182   1.00 20.12 ? 246  GLN A OE1 1 
ATOM   1925 N NE2 . GLN A 1 246 ? 56.246 78.555  0.934   1.00 18.98 ? 246  GLN A NE2 1 
ATOM   1926 N N   . PRO A 1 247 ? 60.448 79.568  4.117   1.00 19.77 ? 247  PRO A N   1 
ATOM   1927 C CA  . PRO A 1 247 ? 61.851 79.816  3.766   1.00 20.27 ? 247  PRO A CA  1 
ATOM   1928 C C   . PRO A 1 247 ? 62.211 80.096  2.317   1.00 20.97 ? 247  PRO A C   1 
ATOM   1929 O O   . PRO A 1 247 ? 63.393 80.132  2.004   1.00 22.84 ? 247  PRO A O   1 
ATOM   1930 C CB  . PRO A 1 247 ? 62.589 78.559  4.257   1.00 20.04 ? 247  PRO A CB  1 
ATOM   1931 C CG  . PRO A 1 247 ? 61.601 77.650  4.761   1.00 20.37 ? 247  PRO A CG  1 
ATOM   1932 C CD  . PRO A 1 247 ? 60.236 78.166  4.498   1.00 20.15 ? 247  PRO A CD  1 
ATOM   1933 N N   . ALA A 1 248 ? 61.220 80.331  1.462   1.00 21.39 ? 248  ALA A N   1 
ATOM   1934 C CA  . ALA A 1 248 ? 61.453 80.667  0.074   1.00 21.44 ? 248  ALA A CA  1 
ATOM   1935 C C   . ALA A 1 248 ? 62.524 81.773  -0.143  1.00 21.87 ? 248  ALA A C   1 
ATOM   1936 O O   . ALA A 1 248 ? 63.365 81.577  -0.988  1.00 23.29 ? 248  ALA A O   1 
ATOM   1937 C CB  . ALA A 1 248 ? 60.162 80.982  -0.642  1.00 20.77 ? 248  ALA A CB  1 
ATOM   1938 N N   . PRO A 1 249 ? 62.517 82.906  0.636   1.00 20.88 ? 249  PRO A N   1 
ATOM   1939 C CA  . PRO A 1 249 ? 61.552 83.373  1.657   1.00 19.54 ? 249  PRO A CA  1 
ATOM   1940 C C   . PRO A 1 249 ? 60.271 83.974  1.105   1.00 19.17 ? 249  PRO A C   1 
ATOM   1941 O O   . PRO A 1 249 ? 60.238 84.527  0.016   1.00 19.74 ? 249  PRO A O   1 
ATOM   1942 C CB  . PRO A 1 249 ? 62.332 84.419  2.451   1.00 19.46 ? 249  PRO A CB  1 
ATOM   1943 C CG  . PRO A 1 249 ? 63.364 84.949  1.467   1.00 20.52 ? 249  PRO A CG  1 
ATOM   1944 C CD  . PRO A 1 249 ? 63.690 83.810  0.521   1.00 20.48 ? 249  PRO A CD  1 
ATOM   1945 N N   . ALA A 1 250 ? 59.210 83.878  1.866   1.00 18.82 ? 250  ALA A N   1 
ATOM   1946 C CA  . ALA A 1 250 ? 57.930 84.429  1.401   1.00 18.33 ? 250  ALA A CA  1 
ATOM   1947 C C   . ALA A 1 250 ? 57.017 84.610  2.589   1.00 18.06 ? 250  ALA A C   1 
ATOM   1948 O O   . ALA A 1 250 ? 57.215 83.974  3.612   1.00 18.12 ? 250  ALA A O   1 
ATOM   1949 C CB  . ALA A 1 250 ? 57.285 83.472  0.384   1.00 17.22 ? 250  ALA A CB  1 
ATOM   1950 N N   . ILE A 1 251 ? 56.011 85.462  2.427   1.00 18.45 ? 251  ILE A N   1 
ATOM   1951 C CA  . ILE A 1 251 ? 55.017 85.729  3.430   1.00 19.44 ? 251  ILE A CA  1 
ATOM   1952 C C   . ILE A 1 251 ? 53.653 85.692  2.769   1.00 19.05 ? 251  ILE A C   1 
ATOM   1953 O O   . ILE A 1 251 ? 53.465 86.236  1.671   1.00 18.90 ? 251  ILE A O   1 
ATOM   1954 C CB  . ILE A 1 251 ? 55.305 87.072  4.109   1.00 20.38 ? 251  ILE A CB  1 
ATOM   1955 C CG1 . ILE A 1 251 ? 54.233 87.476  5.090   1.00 23.34 ? 251  ILE A CG1 1 
ATOM   1956 C CG2 . ILE A 1 251 ? 55.410 88.195  3.109   1.00 23.04 ? 251  ILE A CG2 1 
ATOM   1957 C CD1 . ILE A 1 251 ? 54.852 88.418  6.174   1.00 29.41 ? 251  ILE A CD1 1 
ATOM   1958 N N   . THR A 1 252 ? 52.716 84.982  3.402   1.00 18.74 ? 252  THR A N   1 
ATOM   1959 C CA  . THR A 1 252 ? 51.301 84.955  2.949   1.00 19.14 ? 252  THR A CA  1 
ATOM   1960 C C   . THR A 1 252 ? 50.408 85.617  3.992   1.00 18.78 ? 252  THR A C   1 
ATOM   1961 O O   . THR A 1 252 ? 50.580 85.354  5.164   1.00 19.59 ? 252  THR A O   1 
ATOM   1962 C CB  . THR A 1 252 ? 50.840 83.496  2.705   1.00 18.04 ? 252  THR A CB  1 
ATOM   1963 O OG1 . THR A 1 252 ? 51.690 82.902  1.719   1.00 21.14 ? 252  THR A OG1 1 
ATOM   1964 C CG2 . THR A 1 252 ? 49.428 83.435  2.207   1.00 18.70 ? 252  THR A CG2 1 
ATOM   1965 N N   . TYR A 1 253 ? 49.503 86.497  3.560   1.00 19.02 ? 253  TYR A N   1 
ATOM   1966 C CA  . TYR A 1 253 ? 48.420 87.026  4.385   1.00 19.53 ? 253  TYR A CA  1 
ATOM   1967 C C   . TYR A 1 253 ? 47.143 86.226  4.060   1.00 19.60 ? 253  TYR A C   1 
ATOM   1968 O O   . TYR A 1 253 ? 46.744 86.106  2.884   1.00 17.92 ? 253  TYR A O   1 
ATOM   1969 C CB  . TYR A 1 253 ? 48.160 88.503  4.068   1.00 21.93 ? 253  TYR A CB  1 
ATOM   1970 C CG  . TYR A 1 253 ? 49.224 89.498  4.551   1.00 21.85 ? 253  TYR A CG  1 
ATOM   1971 C CD1 . TYR A 1 253 ? 49.161 90.037  5.820   1.00 24.89 ? 253  TYR A CD1 1 
ATOM   1972 C CD2 . TYR A 1 253 ? 50.271 89.900  3.725   1.00 25.29 ? 253  TYR A CD2 1 
ATOM   1973 C CE1 . TYR A 1 253 ? 50.128 90.949  6.285   1.00 24.26 ? 253  TYR A CE1 1 
ATOM   1974 C CE2 . TYR A 1 253 ? 51.255 90.828  4.177   1.00 24.58 ? 253  TYR A CE2 1 
ATOM   1975 C CZ  . TYR A 1 253 ? 51.156 91.349  5.456   1.00 26.47 ? 253  TYR A CZ  1 
ATOM   1976 O OH  . TYR A 1 253 ? 52.101 92.282  5.927   1.00 28.78 ? 253  TYR A OH  1 
ATOM   1977 N N   . ARG A 1 254 ? 46.516 85.665  5.087   1.00 18.79 ? 254  ARG A N   1 
ATOM   1978 C CA  . ARG A 1 254 ? 45.296 84.860  4.886   1.00 19.28 ? 254  ARG A CA  1 
ATOM   1979 C C   . ARG A 1 254 ? 44.183 85.405  5.782   1.00 18.60 ? 254  ARG A C   1 
ATOM   1980 O O   . ARG A 1 254 ? 44.242 85.259  6.968   1.00 19.48 ? 254  ARG A O   1 
ATOM   1981 C CB  . ARG A 1 254 ? 45.652 83.420  5.245   1.00 19.18 ? 254  ARG A CB  1 
ATOM   1982 C CG  . ARG A 1 254 ? 44.585 82.350  5.006   1.00 20.71 ? 254  ARG A CG  1 
ATOM   1983 C CD  . ARG A 1 254 ? 45.113 81.064  5.670   1.00 17.58 ? 254  ARG A CD  1 
ATOM   1984 N NE  . ARG A 1 254 ? 46.163 80.454  4.870   1.00 16.70 ? 254  ARG A NE  1 
ATOM   1985 C CZ  . ARG A 1 254 ? 47.126 79.693  5.371   1.00 16.39 ? 254  ARG A CZ  1 
ATOM   1986 N NH1 . ARG A 1 254 ? 47.180 79.441  6.680   1.00 19.66 ? 254  ARG A NH1 1 
ATOM   1987 N NH2 . ARG A 1 254 ? 48.022 79.167  4.563   1.00 16.03 ? 254  ARG A NH2 1 
ATOM   1988 N N   . THR A 1 255 ? 43.183 86.075  5.227   1.00 19.30 ? 255  THR A N   1 
ATOM   1989 C CA  . THR A 1 255 ? 42.165 86.729  6.062   1.00 18.03 ? 255  THR A CA  1 
ATOM   1990 C C   . THR A 1 255 ? 40.747 86.193  5.769   1.00 18.56 ? 255  THR A C   1 
ATOM   1991 O O   . THR A 1 255 ? 40.544 85.555  4.737   1.00 17.96 ? 255  THR A O   1 
ATOM   1992 C CB  . THR A 1 255 ? 42.211 88.275  5.914   1.00 17.85 ? 255  THR A CB  1 
ATOM   1993 O OG1 . THR A 1 255 ? 41.310 88.853  6.866   1.00 21.01 ? 255  THR A OG1 1 
ATOM   1994 C CG2 . THR A 1 255 ? 41.795 88.747  4.548   1.00 17.51 ? 255  THR A CG2 1 
ATOM   1995 N N   . ILE A 1 256 ? 39.776 86.459  6.661   1.00 17.96 ? 256  ILE A N   1 
ATOM   1996 C CA  . ILE A 1 256 ? 38.445 85.830  6.518   1.00 18.19 ? 256  ILE A CA  1 
ATOM   1997 C C   . ILE A 1 256 ? 37.322 86.816  6.234   1.00 18.22 ? 256  ILE A C   1 
ATOM   1998 O O   . ILE A 1 256 ? 36.139 86.497  6.393   1.00 19.22 ? 256  ILE A O   1 
ATOM   1999 C CB  . ILE A 1 256 ? 38.108 84.842  7.712   1.00 18.63 ? 256  ILE A CB  1 
ATOM   2000 C CG1 . ILE A 1 256 ? 37.953 85.558  9.047   1.00 17.34 ? 256  ILE A CG1 1 
ATOM   2001 C CG2 . ILE A 1 256 ? 39.188 83.766  7.856   1.00 16.15 ? 256  ILE A CG2 1 
ATOM   2002 C CD1 . ILE A 1 256 ? 37.310 84.623  10.161  1.00 18.93 ? 256  ILE A CD1 1 
ATOM   2003 N N   . GLY A 1 257 ? 37.683 88.031  5.851   1.00 16.97 ? 257  GLY A N   1 
ATOM   2004 C CA  . GLY A 1 257 ? 36.681 88.965  5.357   1.00 18.05 ? 257  GLY A CA  1 
ATOM   2005 C C   . GLY A 1 257 ? 37.344 90.202  4.827   1.00 18.47 ? 257  GLY A C   1 
ATOM   2006 O O   . GLY A 1 257 ? 38.585 90.243  4.707   1.00 17.51 ? 257  GLY A O   1 
ATOM   2007 N N   . GLY A 1 258 ? 36.524 91.217  4.561   1.00 18.32 ? 258  GLY A N   1 
ATOM   2008 C CA  . GLY A 1 258 ? 37.011 92.500  4.096   1.00 18.77 ? 258  GLY A CA  1 
ATOM   2009 C C   . GLY A 1 258 ? 37.561 92.393  2.689   1.00 20.36 ? 258  GLY A C   1 
ATOM   2010 O O   . GLY A 1 258 ? 37.034 91.634  1.832   1.00 20.10 ? 258  GLY A O   1 
ATOM   2011 N N   . ILE A 1 259 ? 38.613 93.168  2.429   1.00 19.84 ? 259  ILE A N   1 
ATOM   2012 C CA  . ILE A 1 259 ? 39.232 93.206  1.110   1.00 19.80 ? 259  ILE A CA  1 
ATOM   2013 C C   . ILE A 1 259 ? 40.755 93.265  1.319   1.00 20.48 ? 259  ILE A C   1 
ATOM   2014 O O   . ILE A 1 259 ? 41.223 93.560  2.420   1.00 21.14 ? 259  ILE A O   1 
ATOM   2015 C CB  . ILE A 1 259 ? 38.815 94.469  0.313   1.00 20.24 ? 259  ILE A CB  1 
ATOM   2016 C CG1 . ILE A 1 259 ? 39.246 95.757  1.034   1.00 18.62 ? 259  ILE A CG1 1 
ATOM   2017 C CG2 . ILE A 1 259 ? 37.298 94.457  -0.015  1.00 18.75 ? 259  ILE A CG2 1 
ATOM   2018 C CD1 . ILE A 1 259 ? 39.337 96.971  0.111   1.00 17.29 ? 259  ILE A CD1 1 
ATOM   2019 N N   . LEU A 1 260 ? 41.513 92.972  0.269   1.00 19.64 ? 260  LEU A N   1 
ATOM   2020 C CA  . LEU A 1 260 ? 42.956 92.997  0.341   1.00 20.45 ? 260  LEU A CA  1 
ATOM   2021 C C   . LEU A 1 260 ? 43.395 94.391  -0.102  1.00 20.52 ? 260  LEU A C   1 
ATOM   2022 O O   . LEU A 1 260 ? 43.357 94.727  -1.284  1.00 22.74 ? 260  LEU A O   1 
ATOM   2023 C CB  . LEU A 1 260 ? 43.553 91.909  -0.556  1.00 19.47 ? 260  LEU A CB  1 
ATOM   2024 C CG  . LEU A 1 260 ? 43.337 90.451  -0.135  1.00 21.18 ? 260  LEU A CG  1 
ATOM   2025 C CD1 . LEU A 1 260 ? 43.783 89.494  -1.222  1.00 17.04 ? 260  LEU A CD1 1 
ATOM   2026 C CD2 . LEU A 1 260 ? 44.028 90.109  1.203   1.00 20.76 ? 260  LEU A CD2 1 
ATOM   2027 N N   . ASP A 1 261 ? 43.738 95.223  0.864   1.00 20.63 ? 261  ASP A N   1 
ATOM   2028 C CA  . ASP A 1 261 ? 44.020 96.631  0.618   1.00 20.59 ? 261  ASP A CA  1 
ATOM   2029 C C   . ASP A 1 261 ? 45.460 96.871  1.096   1.00 20.27 ? 261  ASP A C   1 
ATOM   2030 O O   . ASP A 1 261 ? 45.688 96.969  2.306   1.00 20.05 ? 261  ASP A O   1 
ATOM   2031 C CB  . ASP A 1 261 ? 42.993 97.490  1.388   1.00 20.37 ? 261  ASP A CB  1 
ATOM   2032 C CG  . ASP A 1 261 ? 43.276 98.970  1.309   1.00 22.17 ? 261  ASP A CG  1 
ATOM   2033 O OD1 . ASP A 1 261 ? 44.302 99.336  0.709   1.00 28.54 ? 261  ASP A OD1 1 
ATOM   2034 O OD2 . ASP A 1 261 ? 42.471 99.791  1.817   1.00 24.05 ? 261  ASP A OD2 1 
ATOM   2035 N N   . PHE A 1 262 ? 46.403 96.915  0.150   1.00 19.26 ? 262  PHE A N   1 
ATOM   2036 C CA  . PHE A 1 262 ? 47.853 96.835  0.437   1.00 19.49 ? 262  PHE A CA  1 
ATOM   2037 C C   . PHE A 1 262 ? 48.596 98.168  0.168   1.00 18.48 ? 262  PHE A C   1 
ATOM   2038 O O   . PHE A 1 262 ? 48.251 98.926  -0.760  1.00 18.35 ? 262  PHE A O   1 
ATOM   2039 C CB  . PHE A 1 262 ? 48.516 95.745  -0.420  1.00 18.68 ? 262  PHE A CB  1 
ATOM   2040 C CG  . PHE A 1 262 ? 48.420 94.348  0.152   1.00 20.01 ? 262  PHE A CG  1 
ATOM   2041 C CD1 . PHE A 1 262 ? 49.235 93.961  1.226   1.00 19.04 ? 262  PHE A CD1 1 
ATOM   2042 C CD2 . PHE A 1 262 ? 47.539 93.409  -0.392  1.00 19.30 ? 262  PHE A CD2 1 
ATOM   2043 C CE1 . PHE A 1 262 ? 49.160 92.673  1.758   1.00 21.07 ? 262  PHE A CE1 1 
ATOM   2044 C CE2 . PHE A 1 262 ? 47.462 92.098  0.132   1.00 19.69 ? 262  PHE A CE2 1 
ATOM   2045 C CZ  . PHE A 1 262 ? 48.260 91.733  1.208   1.00 20.13 ? 262  PHE A CZ  1 
ATOM   2046 N N   . TYR A 1 263 ? 49.594 98.436  0.997   1.00 18.09 ? 263  TYR A N   1 
ATOM   2047 C CA  . TYR A 1 263 ? 50.523 99.553  0.798   1.00 17.74 ? 263  TYR A CA  1 
ATOM   2048 C C   . TYR A 1 263 ? 51.946 98.971  0.761   1.00 18.05 ? 263  TYR A C   1 
ATOM   2049 O O   . TYR A 1 263 ? 52.277 98.061  1.527   1.00 17.53 ? 263  TYR A O   1 
ATOM   2050 C CB  . TYR A 1 263 ? 50.421 100.562 1.945   1.00 17.22 ? 263  TYR A CB  1 
ATOM   2051 C CG  . TYR A 1 263 ? 49.103 101.316 1.971   1.00 19.91 ? 263  TYR A CG  1 
ATOM   2052 C CD1 . TYR A 1 263 ? 48.966 102.529 1.293   1.00 17.97 ? 263  TYR A CD1 1 
ATOM   2053 C CD2 . TYR A 1 263 ? 47.998 100.806 2.658   1.00 17.71 ? 263  TYR A CD2 1 
ATOM   2054 C CE1 . TYR A 1 263 ? 47.797 103.233 1.314   1.00 18.85 ? 263  TYR A CE1 1 
ATOM   2055 C CE2 . TYR A 1 263 ? 46.795 101.510 2.690   1.00 22.14 ? 263  TYR A CE2 1 
ATOM   2056 C CZ  . TYR A 1 263 ? 46.702 102.713 2.010   1.00 21.44 ? 263  TYR A CZ  1 
ATOM   2057 O OH  . TYR A 1 263 ? 45.528 103.414 2.037   1.00 21.00 ? 263  TYR A OH  1 
ATOM   2058 N N   . VAL A 1 264 ? 52.778 99.482  -0.139  1.00 16.80 ? 264  VAL A N   1 
ATOM   2059 C CA  . VAL A 1 264 ? 54.158 99.079  -0.175  1.00 16.27 ? 264  VAL A CA  1 
ATOM   2060 C C   . VAL A 1 264 ? 54.978 100.399 -0.049  1.00 16.21 ? 264  VAL A C   1 
ATOM   2061 O O   . VAL A 1 264 ? 54.709 101.368 -0.769  1.00 15.93 ? 264  VAL A O   1 
ATOM   2062 C CB  . VAL A 1 264 ? 54.508 98.216  -1.446  1.00 16.35 ? 264  VAL A CB  1 
ATOM   2063 C CG1 . VAL A 1 264 ? 55.992 97.793  -1.463  1.00 16.92 ? 264  VAL A CG1 1 
ATOM   2064 C CG2 . VAL A 1 264 ? 53.591 96.947  -1.556  1.00 17.18 ? 264  VAL A CG2 1 
ATOM   2065 N N   . PHE A 1 265 ? 55.942 100.425 0.884   1.00 16.05 ? 265  PHE A N   1 
ATOM   2066 C CA  . PHE A 1 265 ? 56.715 101.652 1.244   1.00 15.82 ? 265  PHE A CA  1 
ATOM   2067 C C   . PHE A 1 265 ? 58.175 101.335 0.940   1.00 16.23 ? 265  PHE A C   1 
ATOM   2068 O O   . PHE A 1 265 ? 58.600 100.238 1.269   1.00 16.06 ? 265  PHE A O   1 
ATOM   2069 C CB  . PHE A 1 265 ? 56.593 101.982 2.768   1.00 15.09 ? 265  PHE A CB  1 
ATOM   2070 C CG  . PHE A 1 265 ? 55.149 101.994 3.308   1.00 17.33 ? 265  PHE A CG  1 
ATOM   2071 C CD1 . PHE A 1 265 ? 54.342 103.116 3.137   1.00 15.15 ? 265  PHE A CD1 1 
ATOM   2072 C CD2 . PHE A 1 265 ? 54.634 100.887 4.010   1.00 15.60 ? 265  PHE A CD2 1 
ATOM   2073 C CE1 . PHE A 1 265 ? 53.013 103.146 3.622   1.00 14.63 ? 265  PHE A CE1 1 
ATOM   2074 C CE2 . PHE A 1 265 ? 53.312 100.894 4.482   1.00 16.40 ? 265  PHE A CE2 1 
ATOM   2075 C CZ  . PHE A 1 265 ? 52.506 102.037 4.299   1.00 11.54 ? 265  PHE A CZ  1 
ATOM   2076 N N   . LEU A 1 266 ? 58.914 102.263 0.310   1.00 16.55 ? 266  LEU A N   1 
ATOM   2077 C CA  . LEU A 1 266 ? 60.360 102.098 0.060   1.00 17.73 ? 266  LEU A CA  1 
ATOM   2078 C C   . LEU A 1 266 ? 61.154 103.169 0.797   1.00 17.84 ? 266  LEU A C   1 
ATOM   2079 O O   . LEU A 1 266 ? 60.668 104.273 0.962   1.00 17.93 ? 266  LEU A O   1 
ATOM   2080 C CB  . LEU A 1 266 ? 60.684 102.206 -1.443  1.00 17.24 ? 266  LEU A CB  1 
ATOM   2081 C CG  . LEU A 1 266 ? 60.404 101.028 -2.381  1.00 18.71 ? 266  LEU A CG  1 
ATOM   2082 C CD1 . LEU A 1 266 ? 58.886 100.829 -2.599  1.00 18.22 ? 266  LEU A CD1 1 
ATOM   2083 C CD2 . LEU A 1 266 ? 61.120 101.262 -3.721  1.00 17.30 ? 266  LEU A CD2 1 
ATOM   2084 N N   . GLY A 1 267 ? 62.379 102.833 1.206   1.00 18.59 ? 267  GLY A N   1 
ATOM   2085 C CA  . GLY A 1 267 ? 63.261 103.748 1.880   1.00 17.65 ? 267  GLY A CA  1 
ATOM   2086 C C   . GLY A 1 267 ? 64.740 103.437 1.645   1.00 18.02 ? 267  GLY A C   1 
ATOM   2087 O O   . GLY A 1 267 ? 65.140 102.301 1.276   1.00 16.94 ? 267  GLY A O   1 
ATOM   2088 N N   . ASN A 1 268 ? 65.566 104.449 1.866   1.00 17.81 ? 268  ASN A N   1 
ATOM   2089 C CA  . ASN A 1 268 ? 67.023 104.253 1.759   1.00 18.61 ? 268  ASN A CA  1 
ATOM   2090 C C   . ASN A 1 268 ? 67.626 103.553 2.967   1.00 17.76 ? 268  ASN A C   1 
ATOM   2091 O O   . ASN A 1 268 ? 68.721 102.991 2.890   1.00 18.35 ? 268  ASN A O   1 
ATOM   2092 C CB  . ASN A 1 268 ? 67.730 105.593 1.451   1.00 19.01 ? 268  ASN A CB  1 
ATOM   2093 C CG  . ASN A 1 268 ? 67.398 106.109 0.055   1.00 22.66 ? 268  ASN A CG  1 
ATOM   2094 O OD1 . ASN A 1 268 ? 67.124 105.322 -0.863  1.00 26.00 ? 268  ASN A OD1 1 
ATOM   2095 N ND2 . ASN A 1 268 ? 67.367 107.438 -0.100  1.00 24.46 ? 268  ASN A ND2 1 
ATOM   2096 N N   . THR A 1 269 ? 66.869 103.549 4.062   1.00 17.34 ? 269  THR A N   1 
ATOM   2097 C CA  . THR A 1 269 ? 67.280 103.026 5.367   1.00 16.92 ? 269  THR A CA  1 
ATOM   2098 C C   . THR A 1 269 ? 66.042 102.422 6.086   1.00 15.51 ? 269  THR A C   1 
ATOM   2099 O O   . THR A 1 269 ? 64.943 102.755 5.741   1.00 16.10 ? 269  THR A O   1 
ATOM   2100 C CB  . THR A 1 269 ? 67.845 104.150 6.247   1.00 15.80 ? 269  THR A CB  1 
ATOM   2101 O OG1 . THR A 1 269 ? 66.808 105.111 6.510   1.00 18.89 ? 269  THR A OG1 1 
ATOM   2102 C CG2 . THR A 1 269 ? 69.092 104.874 5.580   1.00 16.65 ? 269  THR A CG2 1 
ATOM   2103 N N   . PRO A 1 270 ? 66.227 101.528 7.072   1.00 15.26 ? 270  PRO A N   1 
ATOM   2104 C CA  . PRO A 1 270 ? 65.059 101.110 7.879   1.00 14.75 ? 270  PRO A CA  1 
ATOM   2105 C C   . PRO A 1 270 ? 64.237 102.244 8.489   1.00 16.23 ? 270  PRO A C   1 
ATOM   2106 O O   . PRO A 1 270 ? 62.998 102.166 8.501   1.00 15.69 ? 270  PRO A O   1 
ATOM   2107 C CB  . PRO A 1 270 ? 65.694 100.249 8.974   1.00 14.22 ? 270  PRO A CB  1 
ATOM   2108 C CG  . PRO A 1 270 ? 66.878 99.611  8.305   1.00 12.40 ? 270  PRO A CG  1 
ATOM   2109 C CD  . PRO A 1 270 ? 67.446 100.785 7.466   1.00 14.21 ? 270  PRO A CD  1 
ATOM   2110 N N   . GLU A 1 271 ? 64.905 103.281 9.007   1.00 16.15 ? 271  GLU A N   1 
ATOM   2111 C CA  . GLU A 1 271 ? 64.202 104.420 9.598   1.00 17.35 ? 271  GLU A CA  1 
ATOM   2112 C C   . GLU A 1 271 ? 63.282 105.120 8.612   1.00 17.68 ? 271  GLU A C   1 
ATOM   2113 O O   . GLU A 1 271 ? 62.185 105.550 8.986   1.00 16.78 ? 271  GLU A O   1 
ATOM   2114 C CB  . GLU A 1 271 ? 65.184 105.420 10.197  1.00 17.30 ? 271  GLU A CB  1 
ATOM   2115 C CG  . GLU A 1 271 ? 65.753 104.963 11.519  1.00 20.33 ? 271  GLU A CG  1 
ATOM   2116 C CD  . GLU A 1 271 ? 64.698 105.025 12.624  1.00 21.51 ? 271  GLU A CD  1 
ATOM   2117 O OE1 . GLU A 1 271 ? 64.191 106.129 12.913  1.00 23.35 ? 271  GLU A OE1 1 
ATOM   2118 O OE2 . GLU A 1 271 ? 64.369 103.959 13.186  1.00 23.01 ? 271  GLU A OE2 1 
ATOM   2119 N N   . GLN A 1 272 ? 63.726 105.255 7.361   1.00 18.46 ? 272  GLN A N   1 
ATOM   2120 C CA  . GLN A 1 272 ? 62.893 105.901 6.335   1.00 20.57 ? 272  GLN A CA  1 
ATOM   2121 C C   . GLN A 1 272 ? 61.660 105.061 5.992   1.00 19.60 ? 272  GLN A C   1 
ATOM   2122 O O   . GLN A 1 272 ? 60.609 105.619 5.704   1.00 19.87 ? 272  GLN A O   1 
ATOM   2123 C CB  . GLN A 1 272 ? 63.682 106.210 5.055   1.00 20.46 ? 272  GLN A CB  1 
ATOM   2124 C CG  . GLN A 1 272 ? 64.791 107.233 5.223   1.00 22.96 ? 272  GLN A CG  1 
ATOM   2125 C CD  . GLN A 1 272 ? 65.467 107.574 3.891   1.00 25.68 ? 272  GLN A CD  1 
ATOM   2126 O OE1 . GLN A 1 272 ? 65.205 106.943 2.842   1.00 31.19 ? 272  GLN A OE1 1 
ATOM   2127 N NE2 . GLN A 1 272 ? 66.308 108.594 3.915   1.00 31.80 ? 272  GLN A NE2 1 
ATOM   2128 N N   . VAL A 1 273 ? 61.771 103.735 6.058   1.00 18.47 ? 273  VAL A N   1 
ATOM   2129 C CA  . VAL A 1 273 ? 60.565 102.864 5.883   1.00 17.35 ? 273  VAL A CA  1 
ATOM   2130 C C   . VAL A 1 273 ? 59.507 103.109 6.985   1.00 17.33 ? 273  VAL A C   1 
ATOM   2131 O O   . VAL A 1 273 ? 58.333 103.260 6.676   1.00 16.52 ? 273  VAL A O   1 
ATOM   2132 C CB  . VAL A 1 273 ? 60.916 101.388 5.752   1.00 17.30 ? 273  VAL A CB  1 
ATOM   2133 C CG1 . VAL A 1 273 ? 59.638 100.483 5.822   1.00 14.05 ? 273  VAL A CG1 1 
ATOM   2134 C CG2 . VAL A 1 273 ? 61.680 101.182 4.463   1.00 15.04 ? 273  VAL A CG2 1 
ATOM   2135 N N   . VAL A 1 274 ? 59.960 103.247 8.233   1.00 17.54 ? 274  VAL A N   1 
ATOM   2136 C CA  . VAL A 1 274 ? 59.073 103.519 9.368   1.00 17.42 ? 274  VAL A CA  1 
ATOM   2137 C C   . VAL A 1 274 ? 58.449 104.895 9.175   1.00 17.79 ? 274  VAL A C   1 
ATOM   2138 O O   . VAL A 1 274 ? 57.248 105.091 9.357   1.00 18.37 ? 274  VAL A O   1 
ATOM   2139 C CB  . VAL A 1 274 ? 59.822 103.386 10.738  1.00 16.80 ? 274  VAL A CB  1 
ATOM   2140 C CG1 . VAL A 1 274 ? 58.931 103.752 11.915  1.00 15.76 ? 274  VAL A CG1 1 
ATOM   2141 C CG2 . VAL A 1 274 ? 60.423 101.972 10.923  1.00 15.74 ? 274  VAL A CG2 1 
ATOM   2142 N N   . GLN A 1 275 ? 59.264 105.862 8.783   1.00 17.75 ? 275  GLN A N   1 
ATOM   2143 C CA  . GLN A 1 275 ? 58.742 107.182 8.489   1.00 18.23 ? 275  GLN A CA  1 
ATOM   2144 C C   . GLN A 1 275 ? 57.653 107.175 7.391   1.00 17.24 ? 275  GLN A C   1 
ATOM   2145 O O   . GLN A 1 275 ? 56.632 107.850 7.522   1.00 17.86 ? 275  GLN A O   1 
ATOM   2146 C CB  . GLN A 1 275 ? 59.873 108.139 8.134   1.00 17.43 ? 275  GLN A CB  1 
ATOM   2147 C CG  . GLN A 1 275 ? 60.858 108.410 9.286   1.00 18.29 ? 275  GLN A CG  1 
ATOM   2148 C CD  . GLN A 1 275 ? 62.138 109.104 8.786   1.00 21.00 ? 275  GLN A CD  1 
ATOM   2149 O OE1 . GLN A 1 275 ? 62.322 109.262 7.565   1.00 22.32 ? 275  GLN A OE1 1 
ATOM   2150 N NE2 . GLN A 1 275 ? 63.020 109.529 9.727   1.00 21.82 ? 275  GLN A NE2 1 
ATOM   2151 N N   . GLU A 1 276 ? 57.877 106.454 6.306   1.00 16.51 ? 276  GLU A N   1 
ATOM   2152 C CA  . GLU A 1 276 ? 56.851 106.325 5.243   1.00 16.71 ? 276  GLU A CA  1 
ATOM   2153 C C   . GLU A 1 276 ? 55.574 105.652 5.744   1.00 15.88 ? 276  GLU A C   1 
ATOM   2154 O O   . GLU A 1 276 ? 54.483 106.106 5.433   1.00 15.77 ? 276  GLU A O   1 
ATOM   2155 C CB  . GLU A 1 276 ? 57.393 105.486 4.085   1.00 16.75 ? 276  GLU A CB  1 
ATOM   2156 C CG  . GLU A 1 276 ? 58.494 106.164 3.301   1.00 19.22 ? 276  GLU A CG  1 
ATOM   2157 C CD  . GLU A 1 276 ? 58.053 107.433 2.600   1.00 25.88 ? 276  GLU A CD  1 
ATOM   2158 O OE1 . GLU A 1 276 ? 56.810 107.675 2.404   1.00 28.33 ? 276  GLU A OE1 1 
ATOM   2159 O OE2 . GLU A 1 276 ? 58.977 108.196 2.233   1.00 28.79 ? 276  GLU A OE2 1 
ATOM   2160 N N   . TYR A 1 277 ? 55.716 104.573 6.515   1.00 15.43 ? 277  TYR A N   1 
ATOM   2161 C CA  . TYR A 1 277 ? 54.560 103.895 7.152   1.00 15.63 ? 277  TYR A CA  1 
ATOM   2162 C C   . TYR A 1 277 ? 53.760 104.816 8.047   1.00 16.80 ? 277  TYR A C   1 
ATOM   2163 O O   . TYR A 1 277 ? 52.526 104.920 7.903   1.00 17.53 ? 277  TYR A O   1 
ATOM   2164 C CB  . TYR A 1 277 ? 55.007 102.645 7.952   1.00 16.29 ? 277  TYR A CB  1 
ATOM   2165 C CG  . TYR A 1 277 ? 53.860 101.991 8.735   1.00 16.82 ? 277  TYR A CG  1 
ATOM   2166 C CD1 . TYR A 1 277 ? 52.667 101.595 8.096   1.00 17.47 ? 277  TYR A CD1 1 
ATOM   2167 C CD2 . TYR A 1 277 ? 53.958 101.805 10.108  1.00 18.04 ? 277  TYR A CD2 1 
ATOM   2168 C CE1 . TYR A 1 277 ? 51.612 100.981 8.829   1.00 17.39 ? 277  TYR A CE1 1 
ATOM   2169 C CE2 . TYR A 1 277 ? 52.921 101.194 10.841  1.00 18.25 ? 277  TYR A CE2 1 
ATOM   2170 C CZ  . TYR A 1 277 ? 51.764 100.796 10.198  1.00 18.01 ? 277  TYR A CZ  1 
ATOM   2171 O OH  . TYR A 1 277 ? 50.767 100.241 10.958  1.00 18.22 ? 277  TYR A OH  1 
ATOM   2172 N N   . LEU A 1 278 ? 54.447 105.542 8.938   1.00 17.41 ? 278  LEU A N   1 
ATOM   2173 C CA  . LEU A 1 278 ? 53.765 106.478 9.851   1.00 17.53 ? 278  LEU A CA  1 
ATOM   2174 C C   . LEU A 1 278 ? 53.171 107.711 9.171   1.00 17.68 ? 278  LEU A C   1 
ATOM   2175 O O   . LEU A 1 278 ? 52.189 108.323 9.666   1.00 17.58 ? 278  LEU A O   1 
ATOM   2176 C CB  . LEU A 1 278 ? 54.692 106.859 11.018  1.00 16.70 ? 278  LEU A CB  1 
ATOM   2177 C CG  . LEU A 1 278 ? 55.224 105.649 11.814  1.00 16.77 ? 278  LEU A CG  1 
ATOM   2178 C CD1 . LEU A 1 278 ? 56.043 106.050 13.026  1.00 12.84 ? 278  LEU A CD1 1 
ATOM   2179 C CD2 . LEU A 1 278 ? 54.121 104.659 12.229  1.00 15.47 ? 278  LEU A CD2 1 
ATOM   2180 N N   . GLU A 1 279 ? 53.738 108.073 8.029   1.00 19.10 ? 279  GLU A N   1 
ATOM   2181 C CA  . GLU A 1 279 ? 53.198 109.157 7.204   1.00 19.52 ? 279  GLU A CA  1 
ATOM   2182 C C   . GLU A 1 279 ? 51.845 108.730 6.685   1.00 20.16 ? 279  GLU A C   1 
ATOM   2183 O O   . GLU A 1 279 ? 50.897 109.536 6.594   1.00 22.41 ? 279  GLU A O   1 
ATOM   2184 C CB  . GLU A 1 279 ? 54.176 109.493 6.064   1.00 19.39 ? 279  GLU A CB  1 
ATOM   2185 C CG  . GLU A 1 279 ? 53.645 110.389 4.920   1.00 23.40 ? 279  GLU A CG  1 
ATOM   2186 C CD  . GLU A 1 279 ? 53.140 111.759 5.372   1.00 30.72 ? 279  GLU A CD  1 
ATOM   2187 O OE1 . GLU A 1 279 ? 53.798 112.374 6.258   1.00 32.47 ? 279  GLU A OE1 1 
ATOM   2188 O OE2 . GLU A 1 279 ? 52.086 112.223 4.824   1.00 32.14 ? 279  GLU A OE2 1 
ATOM   2189 N N   . LEU A 1 280 ? 51.712 107.455 6.357   1.00 20.05 ? 280  LEU A N   1 
ATOM   2190 C CA  . LEU A 1 280 ? 50.377 106.933 6.011   1.00 19.04 ? 280  LEU A CA  1 
ATOM   2191 C C   . LEU A 1 280 ? 49.412 106.782 7.196   1.00 18.41 ? 280  LEU A C   1 
ATOM   2192 O O   . LEU A 1 280 ? 48.362 107.424 7.219   1.00 17.43 ? 280  LEU A O   1 
ATOM   2193 C CB  . LEU A 1 280 ? 50.485 105.616 5.217   1.00 19.02 ? 280  LEU A CB  1 
ATOM   2194 C CG  . LEU A 1 280 ? 49.077 105.060 4.918   1.00 18.99 ? 280  LEU A CG  1 
ATOM   2195 C CD1 . LEU A 1 280 ? 48.494 105.770 3.714   1.00 12.51 ? 280  LEU A CD1 1 
ATOM   2196 C CD2 . LEU A 1 280 ? 49.098 103.556 4.766   1.00 20.31 ? 280  LEU A CD2 1 
ATOM   2197 N N   . ILE A 1 281 ? 49.732 105.952 8.192   1.00 18.47 ? 281  ILE A N   1 
ATOM   2198 C CA  . ILE A 1 281 ? 48.680 105.595 9.165   1.00 19.68 ? 281  ILE A CA  1 
ATOM   2199 C C   . ILE A 1 281 ? 48.560 106.600 10.307  1.00 19.84 ? 281  ILE A C   1 
ATOM   2200 O O   . ILE A 1 281 ? 47.600 106.499 11.096  1.00 18.78 ? 281  ILE A O   1 
ATOM   2201 C CB  . ILE A 1 281 ? 48.797 104.154 9.844   1.00 19.75 ? 281  ILE A CB  1 
ATOM   2202 C CG1 . ILE A 1 281 ? 50.243 103.806 10.025  1.00 21.14 ? 281  ILE A CG1 1 
ATOM   2203 C CG2 . ILE A 1 281 ? 47.788 103.042 9.269   1.00 20.85 ? 281  ILE A CG2 1 
ATOM   2204 C CD1 . ILE A 1 281 ? 50.673 104.299 11.303  1.00 20.68 ? 281  ILE A CD1 1 
ATOM   2205 N N   . GLY A 1 282 ? 49.542 107.513 10.428  1.00 19.02 ? 282  GLY A N   1 
ATOM   2206 C CA  . GLY A 1 282 ? 49.525 108.481 11.520  1.00 19.26 ? 282  GLY A CA  1 
ATOM   2207 C C   . GLY A 1 282 ? 50.700 108.372 12.483  1.00 20.20 ? 282  GLY A C   1 
ATOM   2208 O O   . GLY A 1 282 ? 50.972 107.301 13.050  1.00 19.69 ? 282  GLY A O   1 
ATOM   2209 N N   . ARG A 1 283 ? 51.401 109.502 12.664  1.00 19.55 ? 283  ARG A N   1 
ATOM   2210 C CA  . ARG A 1 283 ? 52.552 109.578 13.540  1.00 19.08 ? 283  ARG A CA  1 
ATOM   2211 C C   . ARG A 1 283 ? 52.100 109.617 14.972  1.00 18.66 ? 283  ARG A C   1 
ATOM   2212 O O   . ARG A 1 283 ? 50.995 110.061 15.253  1.00 17.23 ? 283  ARG A O   1 
ATOM   2213 C CB  . ARG A 1 283 ? 53.406 110.834 13.227  1.00 19.48 ? 283  ARG A CB  1 
ATOM   2214 C CG  . ARG A 1 283 ? 54.299 110.630 12.036  1.00 18.92 ? 283  ARG A CG  1 
ATOM   2215 C CD  . ARG A 1 283 ? 55.146 111.866 11.724  1.00 20.16 ? 283  ARG A CD  1 
ATOM   2216 N NE  . ARG A 1 283 ? 54.296 112.886 11.135  1.00 22.62 ? 283  ARG A NE  1 
ATOM   2217 C CZ  . ARG A 1 283 ? 54.072 113.025 9.833   1.00 27.30 ? 283  ARG A CZ  1 
ATOM   2218 N NH1 . ARG A 1 283 ? 54.672 112.233 8.934   1.00 25.92 ? 283  ARG A NH1 1 
ATOM   2219 N NH2 . ARG A 1 283 ? 53.259 113.986 9.424   1.00 29.21 ? 283  ARG A NH2 1 
ATOM   2220 N N   . PRO A 1 284 ? 52.951 109.128 15.894  1.00 18.52 ? 284  PRO A N   1 
ATOM   2221 C CA  . PRO A 1 284 ? 52.526 109.075 17.290  1.00 18.91 ? 284  PRO A CA  1 
ATOM   2222 C C   . PRO A 1 284 ? 52.326 110.428 17.931  1.00 19.14 ? 284  PRO A C   1 
ATOM   2223 O O   . PRO A 1 284 ? 52.987 111.402 17.561  1.00 20.09 ? 284  PRO A O   1 
ATOM   2224 C CB  . PRO A 1 284 ? 53.693 108.333 17.988  1.00 19.05 ? 284  PRO A CB  1 
ATOM   2225 C CG  . PRO A 1 284 ? 54.832 108.558 17.128  1.00 18.33 ? 284  PRO A CG  1 
ATOM   2226 C CD  . PRO A 1 284 ? 54.285 108.537 15.715  1.00 18.09 ? 284  PRO A CD  1 
ATOM   2227 N N   . ALA A 1 285 ? 51.464 110.471 18.935  1.00 19.34 ? 285  ALA A N   1 
ATOM   2228 C CA  . ALA A 1 285 ? 51.211 111.702 19.678  1.00 20.07 ? 285  ALA A CA  1 
ATOM   2229 C C   . ALA A 1 285 ? 52.484 112.047 20.456  1.00 20.39 ? 285  ALA A C   1 
ATOM   2230 O O   . ALA A 1 285 ? 53.275 111.157 20.789  1.00 20.55 ? 285  ALA A O   1 
ATOM   2231 C CB  . ALA A 1 285 ? 50.021 111.514 20.657  1.00 20.13 ? 285  ALA A CB  1 
ATOM   2232 N N   . LEU A 1 286 ? 52.685 113.319 20.762  1.00 20.46 ? 286  LEU A N   1 
ATOM   2233 C CA  . LEU A 1 286 ? 53.807 113.700 21.630  1.00 20.47 ? 286  LEU A CA  1 
ATOM   2234 C C   . LEU A 1 286 ? 53.390 113.460 23.066  1.00 19.82 ? 286  LEU A C   1 
ATOM   2235 O O   . LEU A 1 286 ? 52.354 113.968 23.484  1.00 20.83 ? 286  LEU A O   1 
ATOM   2236 C CB  . LEU A 1 286 ? 54.173 115.184 21.412  1.00 21.26 ? 286  LEU A CB  1 
ATOM   2237 C CG  . LEU A 1 286 ? 55.493 115.641 22.065  1.00 22.39 ? 286  LEU A CG  1 
ATOM   2238 C CD1 . LEU A 1 286 ? 56.699 114.798 21.643  1.00 23.39 ? 286  LEU A CD1 1 
ATOM   2239 C CD2 . LEU A 1 286 ? 55.712 117.090 21.743  1.00 24.90 ? 286  LEU A CD2 1 
ATOM   2240 N N   . PRO A 1 287 ? 54.164 112.671 23.834  1.00 19.97 ? 287  PRO A N   1 
ATOM   2241 C CA  . PRO A 1 287 ? 53.739 112.439 25.230  1.00 19.88 ? 287  PRO A CA  1 
ATOM   2242 C C   . PRO A 1 287 ? 53.863 113.690 26.099  1.00 19.20 ? 287  PRO A C   1 
ATOM   2243 O O   . PRO A 1 287 ? 54.594 114.601 25.746  1.00 18.84 ? 287  PRO A O   1 
ATOM   2244 C CB  . PRO A 1 287 ? 54.721 111.368 25.741  1.00 19.96 ? 287  PRO A CB  1 
ATOM   2245 C CG  . PRO A 1 287 ? 55.413 110.859 24.525  1.00 20.57 ? 287  PRO A CG  1 
ATOM   2246 C CD  . PRO A 1 287 ? 55.430 111.967 23.540  1.00 18.99 ? 287  PRO A CD  1 
ATOM   2247 N N   . SER A 1 288 ? 53.114 113.741 27.202  1.00 18.65 ? 288  SER A N   1 
ATOM   2248 C CA  . SER A 1 288 ? 53.320 114.776 28.191  1.00 18.38 ? 288  SER A CA  1 
ATOM   2249 C C   . SER A 1 288 ? 54.699 114.463 28.749  1.00 18.40 ? 288  SER A C   1 
ATOM   2250 O O   . SER A 1 288 ? 55.062 113.301 28.856  1.00 18.28 ? 288  SER A O   1 
ATOM   2251 C CB  . SER A 1 288 ? 52.285 114.696 29.325  1.00 18.20 ? 288  SER A CB  1 
ATOM   2252 O OG  . SER A 1 288 ? 50.979 115.030 28.869  1.00 17.79 ? 288  SER A OG  1 
ATOM   2253 N N   . TYR A 1 289 ? 55.473 115.487 29.089  1.00 17.90 ? 289  TYR A N   1 
ATOM   2254 C CA  . TYR A 1 289 ? 56.815 115.245 29.588  1.00 19.25 ? 289  TYR A CA  1 
ATOM   2255 C C   . TYR A 1 289 ? 56.799 114.377 30.863  1.00 18.29 ? 289  TYR A C   1 
ATOM   2256 O O   . TYR A 1 289 ? 57.648 113.489 31.054  1.00 17.94 ? 289  TYR A O   1 
ATOM   2257 C CB  . TYR A 1 289 ? 57.491 116.590 29.818  1.00 19.37 ? 289  TYR A CB  1 
ATOM   2258 C CG  . TYR A 1 289 ? 59.003 116.552 30.034  1.00 20.84 ? 289  TYR A CG  1 
ATOM   2259 C CD1 . TYR A 1 289 ? 59.869 116.808 28.976  1.00 19.06 ? 289  TYR A CD1 1 
ATOM   2260 C CD2 . TYR A 1 289 ? 59.556 116.340 31.313  1.00 22.48 ? 289  TYR A CD2 1 
ATOM   2261 C CE1 . TYR A 1 289 ? 61.237 116.856 29.156  1.00 18.58 ? 289  TYR A CE1 1 
ATOM   2262 C CE2 . TYR A 1 289 ? 60.947 116.343 31.509  1.00 18.81 ? 289  TYR A CE2 1 
ATOM   2263 C CZ  . TYR A 1 289 ? 61.768 116.612 30.419  1.00 19.44 ? 289  TYR A CZ  1 
ATOM   2264 O OH  . TYR A 1 289 ? 63.123 116.655 30.574  1.00 19.98 ? 289  TYR A OH  1 
ATOM   2265 N N   . TRP A 1 290 ? 55.816 114.603 31.726  1.00 17.95 ? 290  TRP A N   1 
ATOM   2266 C CA  . TRP A 1 290 ? 55.690 113.795 32.953  1.00 18.59 ? 290  TRP A CA  1 
ATOM   2267 C C   . TRP A 1 290 ? 55.440 112.302 32.697  1.00 18.32 ? 290  TRP A C   1 
ATOM   2268 O O   . TRP A 1 290 ? 55.858 111.461 33.513  1.00 18.31 ? 290  TRP A O   1 
ATOM   2269 C CB  . TRP A 1 290 ? 54.647 114.376 33.912  1.00 18.44 ? 290  TRP A CB  1 
ATOM   2270 C CG  . TRP A 1 290 ? 53.222 114.438 33.370  1.00 18.71 ? 290  TRP A CG  1 
ATOM   2271 C CD1 . TRP A 1 290 ? 52.577 115.533 32.853  1.00 19.11 ? 290  TRP A CD1 1 
ATOM   2272 C CD2 . TRP A 1 290 ? 52.272 113.377 33.369  1.00 18.44 ? 290  TRP A CD2 1 
ATOM   2273 N NE1 . TRP A 1 290 ? 51.291 115.206 32.508  1.00 16.99 ? 290  TRP A NE1 1 
ATOM   2274 C CE2 . TRP A 1 290 ? 51.075 113.889 32.823  1.00 19.42 ? 290  TRP A CE2 1 
ATOM   2275 C CE3 . TRP A 1 290 ? 52.313 112.025 33.774  1.00 16.35 ? 290  TRP A CE3 1 
ATOM   2276 C CZ2 . TRP A 1 290 ? 49.938 113.111 32.681  1.00 15.77 ? 290  TRP A CZ2 1 
ATOM   2277 C CZ3 . TRP A 1 290 ? 51.182 111.257 33.610  1.00 18.31 ? 290  TRP A CZ3 1 
ATOM   2278 C CH2 . TRP A 1 290 ? 50.013 111.805 33.069  1.00 18.39 ? 290  TRP A CH2 1 
ATOM   2279 N N   . ALA A 1 291 ? 54.832 111.967 31.546  1.00 17.11 ? 291  ALA A N   1 
ATOM   2280 C CA  . ALA A 1 291 ? 54.564 110.545 31.220  1.00 17.48 ? 291  ALA A CA  1 
ATOM   2281 C C   . ALA A 1 291 ? 55.853 109.789 30.906  1.00 17.91 ? 291  ALA A C   1 
ATOM   2282 O O   . ALA A 1 291 ? 55.839 108.554 30.887  1.00 16.56 ? 291  ALA A O   1 
ATOM   2283 C CB  . ALA A 1 291 ? 53.583 110.404 30.066  1.00 15.74 ? 291  ALA A CB  1 
ATOM   2284 N N   . LEU A 1 292 ? 56.958 110.528 30.691  1.00 18.42 ? 292  LEU A N   1 
ATOM   2285 C CA  . LEU A 1 292 ? 58.299 109.926 30.516  1.00 19.03 ? 292  LEU A CA  1 
ATOM   2286 C C   . LEU A 1 292 ? 58.996 109.548 31.840  1.00 19.27 ? 292  LEU A C   1 
ATOM   2287 O O   . LEU A 1 292 ? 60.009 108.816 31.841  1.00 19.09 ? 292  LEU A O   1 
ATOM   2288 C CB  . LEU A 1 292 ? 59.236 110.839 29.713  1.00 19.70 ? 292  LEU A CB  1 
ATOM   2289 C CG  . LEU A 1 292 ? 58.891 111.466 28.350  1.00 22.35 ? 292  LEU A CG  1 
ATOM   2290 C CD1 . LEU A 1 292 ? 60.161 111.870 27.596  1.00 24.15 ? 292  LEU A CD1 1 
ATOM   2291 C CD2 . LEU A 1 292 ? 58.164 110.562 27.496  1.00 25.11 ? 292  LEU A CD2 1 
ATOM   2292 N N   . GLY A 1 293 ? 58.449 109.991 32.972  1.00 19.38 ? 293  GLY A N   1 
ATOM   2293 C CA  . GLY A 1 293 ? 59.010 109.559 34.242  1.00 18.91 ? 293  GLY A CA  1 
ATOM   2294 C C   . GLY A 1 293 ? 58.568 108.165 34.597  1.00 19.36 ? 293  GLY A C   1 
ATOM   2295 O O   . GLY A 1 293 ? 57.897 107.481 33.790  1.00 20.98 ? 293  GLY A O   1 
ATOM   2296 N N   . PHE A 1 294 ? 58.936 107.730 35.800  1.00 18.32 ? 294  PHE A N   1 
ATOM   2297 C CA  . PHE A 1 294 ? 58.618 106.411 36.305  1.00 17.50 ? 294  PHE A CA  1 
ATOM   2298 C C   . PHE A 1 294 ? 57.182 106.363 36.834  1.00 17.80 ? 294  PHE A C   1 
ATOM   2299 O O   . PHE A 1 294 ? 56.748 107.270 37.552  1.00 16.53 ? 294  PHE A O   1 
ATOM   2300 C CB  . PHE A 1 294 ? 59.580 106.097 37.423  1.00 17.64 ? 294  PHE A CB  1 
ATOM   2301 C CG  . PHE A 1 294 ? 59.451 104.709 37.997  1.00 17.90 ? 294  PHE A CG  1 
ATOM   2302 C CD1 . PHE A 1 294 ? 59.692 103.579 37.214  1.00 15.97 ? 294  PHE A CD1 1 
ATOM   2303 C CD2 . PHE A 1 294 ? 59.129 104.550 39.343  1.00 18.91 ? 294  PHE A CD2 1 
ATOM   2304 C CE1 . PHE A 1 294 ? 59.583 102.311 37.751  1.00 16.42 ? 294  PHE A CE1 1 
ATOM   2305 C CE2 . PHE A 1 294 ? 59.031 103.297 39.915  1.00 18.61 ? 294  PHE A CE2 1 
ATOM   2306 C CZ  . PHE A 1 294 ? 59.267 102.163 39.116  1.00 17.90 ? 294  PHE A CZ  1 
ATOM   2307 N N   . HIS A 1 295 ? 56.475 105.292 36.473  1.00 17.25 ? 295  HIS A N   1 
ATOM   2308 C CA  . HIS A 1 295 ? 55.091 105.041 36.873  1.00 17.13 ? 295  HIS A CA  1 
ATOM   2309 C C   . HIS A 1 295 ? 55.118 103.857 37.834  1.00 18.47 ? 295  HIS A C   1 
ATOM   2310 O O   . HIS A 1 295 ? 55.832 102.881 37.597  1.00 18.48 ? 295  HIS A O   1 
ATOM   2311 C CB  . HIS A 1 295 ? 54.250 104.610 35.668  1.00 16.69 ? 295  HIS A CB  1 
ATOM   2312 C CG  . HIS A 1 295 ? 54.094 105.640 34.592  1.00 14.76 ? 295  HIS A CG  1 
ATOM   2313 N ND1 . HIS A 1 295 ? 55.153 106.109 33.837  1.00 18.46 ? 295  HIS A ND1 1 
ATOM   2314 C CD2 . HIS A 1 295 ? 52.989 106.250 34.101  1.00 12.34 ? 295  HIS A CD2 1 
ATOM   2315 C CE1 . HIS A 1 295 ? 54.708 106.981 32.944  1.00 15.29 ? 295  HIS A CE1 1 
ATOM   2316 N NE2 . HIS A 1 295 ? 53.397 107.067 33.065  1.00 14.07 ? 295  HIS A NE2 1 
ATOM   2317 N N   . LEU A 1 296 ? 54.362 103.931 38.918  1.00 18.72 ? 296  LEU A N   1 
ATOM   2318 C CA  . LEU A 1 296 ? 54.252 102.810 39.844  1.00 19.46 ? 296  LEU A CA  1 
ATOM   2319 C C   . LEU A 1 296 ? 52.781 102.406 39.959  1.00 19.46 ? 296  LEU A C   1 
ATOM   2320 O O   . LEU A 1 296 ? 51.920 103.244 39.868  1.00 19.01 ? 296  LEU A O   1 
ATOM   2321 C CB  . LEU A 1 296 ? 54.819 103.203 41.218  1.00 19.93 ? 296  LEU A CB  1 
ATOM   2322 C CG  . LEU A 1 296 ? 54.975 102.117 42.285  1.00 21.42 ? 296  LEU A CG  1 
ATOM   2323 C CD1 . LEU A 1 296 ? 55.861 101.003 41.780  1.00 18.78 ? 296  LEU A CD1 1 
ATOM   2324 C CD2 . LEU A 1 296 ? 55.543 102.763 43.573  1.00 20.19 ? 296  LEU A CD2 1 
ATOM   2325 N N   . SER A 1 297 ? 52.512 101.116 40.174  1.00 20.33 ? 297  SER A N   1 
ATOM   2326 C CA  . SER A 1 297 ? 51.178 100.561 40.045  1.00 20.75 ? 297  SER A CA  1 
ATOM   2327 C C   . SER A 1 297 ? 51.075 99.152  40.643  1.00 20.65 ? 297  SER A C   1 
ATOM   2328 O O   . SER A 1 297 ? 52.070 98.423  40.744  1.00 20.23 ? 297  SER A O   1 
ATOM   2329 C CB  . SER A 1 297 ? 50.808 100.512 38.543  1.00 21.13 ? 297  SER A CB  1 
ATOM   2330 O OG  . SER A 1 297 ? 49.508 99.957  38.350  1.00 23.70 ? 297  SER A OG  1 
ATOM   2331 N N   . ARG A 1 298 ? 49.874 98.763  41.054  1.00 21.06 ? 298  ARG A N   1 
ATOM   2332 C CA  . ARG A 1 298 ? 49.602 97.342  41.249  1.00 22.30 ? 298  ARG A CA  1 
ATOM   2333 C C   . ARG A 1 298 ? 48.141 97.095  41.229  1.00 22.80 ? 298  ARG A C   1 
ATOM   2334 O O   . ARG A 1 298 ? 47.368 97.978  41.523  1.00 23.41 ? 298  ARG A O   1 
ATOM   2335 C CB  . ARG A 1 298 ? 50.221 96.726  42.523  1.00 22.09 ? 298  ARG A CB  1 
ATOM   2336 C CG  . ARG A 1 298 ? 49.391 96.877  43.794  1.00 23.04 ? 298  ARG A CG  1 
ATOM   2337 C CD  . ARG A 1 298 ? 49.859 95.958  44.891  1.00 23.29 ? 298  ARG A CD  1 
ATOM   2338 N NE  . ARG A 1 298 ? 49.607 94.541  44.581  1.00 24.01 ? 298  ARG A NE  1 
ATOM   2339 C CZ  . ARG A 1 298 ? 50.276 93.530  45.136  1.00 23.68 ? 298  ARG A CZ  1 
ATOM   2340 N NH1 . ARG A 1 298 ? 51.240 93.776  46.027  1.00 20.38 ? 298  ARG A NH1 1 
ATOM   2341 N NH2 . ARG A 1 298 ? 50.004 92.275  44.787  1.00 20.82 ? 298  ARG A NH2 1 
ATOM   2342 N N   . TYR A 1 299 ? 47.792 95.870  40.857  1.00 23.17 ? 299  TYR A N   1 
ATOM   2343 C CA  . TYR A 1 299 ? 46.453 95.344  41.006  1.00 23.69 ? 299  TYR A CA  1 
ATOM   2344 C C   . TYR A 1 299 ? 46.254 94.961  42.476  1.00 23.81 ? 299  TYR A C   1 
ATOM   2345 O O   . TYR A 1 299 ? 46.943 94.100  43.008  1.00 24.18 ? 299  TYR A O   1 
ATOM   2346 C CB  . TYR A 1 299 ? 46.276 94.147  40.045  1.00 23.08 ? 299  TYR A CB  1 
ATOM   2347 C CG  . TYR A 1 299 ? 44.888 93.497  39.971  1.00 23.02 ? 299  TYR A CG  1 
ATOM   2348 C CD1 . TYR A 1 299 ? 44.719 92.300  39.251  1.00 24.27 ? 299  TYR A CD1 1 
ATOM   2349 C CD2 . TYR A 1 299 ? 43.779 94.034  40.615  1.00 20.54 ? 299  TYR A CD2 1 
ATOM   2350 C CE1 . TYR A 1 299 ? 43.484 91.661  39.154  1.00 22.10 ? 299  TYR A CE1 1 
ATOM   2351 C CE2 . TYR A 1 299 ? 42.544 93.403  40.539  1.00 20.48 ? 299  TYR A CE2 1 
ATOM   2352 C CZ  . TYR A 1 299 ? 42.413 92.214  39.802  1.00 22.37 ? 299  TYR A CZ  1 
ATOM   2353 O OH  . TYR A 1 299 ? 41.213 91.561  39.685  1.00 24.62 ? 299  TYR A OH  1 
ATOM   2354 N N   . GLU A 1 300 ? 45.325 95.647  43.136  1.00 24.77 ? 300  GLU A N   1 
ATOM   2355 C CA  . GLU A 1 300 ? 44.951 95.334  44.517  1.00 25.36 ? 300  GLU A CA  1 
ATOM   2356 C C   . GLU A 1 300 ? 45.928 95.809  45.564  1.00 24.25 ? 300  GLU A C   1 
ATOM   2357 O O   . GLU A 1 300 ? 46.519 95.027  46.281  1.00 23.58 ? 300  GLU A O   1 
ATOM   2358 C CB  . GLU A 1 300 ? 44.608 93.835  44.747  1.00 26.02 ? 300  GLU A CB  1 
ATOM   2359 C CG  . GLU A 1 300 ? 43.282 93.393  44.108  1.00 28.44 ? 300  GLU A CG  1 
ATOM   2360 C CD  . GLU A 1 300 ? 42.016 93.920  44.797  1.00 33.78 ? 300  GLU A CD  1 
ATOM   2361 O OE1 . GLU A 1 300 ? 42.071 94.288  46.005  1.00 33.33 ? 300  GLU A OE1 1 
ATOM   2362 O OE2 . GLU A 1 300 ? 40.949 93.943  44.107  1.00 36.70 ? 300  GLU A OE2 1 
ATOM   2363 N N   . TYR A 1 301 ? 46.041 97.121  45.671  1.00 25.11 ? 301  TYR A N   1 
ATOM   2364 C CA  . TYR A 1 301 ? 46.500 97.735  46.912  1.00 25.09 ? 301  TYR A CA  1 
ATOM   2365 C C   . TYR A 1 301 ? 45.502 97.343  47.971  1.00 25.94 ? 301  TYR A C   1 
ATOM   2366 O O   . TYR A 1 301 ? 45.875 97.037  49.096  1.00 26.31 ? 301  TYR A O   1 
ATOM   2367 C CB  . TYR A 1 301 ? 46.638 99.250  46.751  1.00 24.86 ? 301  TYR A CB  1 
ATOM   2368 C CG  . TYR A 1 301 ? 47.854 99.635  45.906  1.00 24.05 ? 301  TYR A CG  1 
ATOM   2369 C CD1 . TYR A 1 301 ? 49.149 99.390  46.369  1.00 24.03 ? 301  TYR A CD1 1 
ATOM   2370 C CD2 . TYR A 1 301 ? 47.700 100.259 44.654  1.00 22.77 ? 301  TYR A CD2 1 
ATOM   2371 C CE1 . TYR A 1 301 ? 50.274 99.766  45.594  1.00 25.05 ? 301  TYR A CE1 1 
ATOM   2372 C CE2 . TYR A 1 301 ? 48.808 100.616 43.871  1.00 23.63 ? 301  TYR A CE2 1 
ATOM   2373 C CZ  . TYR A 1 301 ? 50.082 100.374 44.342  1.00 23.77 ? 301  TYR A CZ  1 
ATOM   2374 O OH  . TYR A 1 301 ? 51.186 100.710 43.561  1.00 25.60 ? 301  TYR A OH  1 
ATOM   2375 N N   . GLY A 1 302 ? 44.227 97.280  47.581  1.00 26.29 ? 302  GLY A N   1 
ATOM   2376 C CA  . GLY A 1 302 ? 43.162 96.797  48.461  1.00 26.43 ? 302  GLY A CA  1 
ATOM   2377 C C   . GLY A 1 302 ? 42.464 97.976  49.108  1.00 26.24 ? 302  GLY A C   1 
ATOM   2378 O O   . GLY A 1 302 ? 41.249 98.087  49.067  1.00 24.97 ? 302  GLY A O   1 
ATOM   2379 N N   . THR A 1 303 ? 43.259 98.877  49.686  1.00 25.92 ? 303  THR A N   1 
ATOM   2380 C CA  . THR A 1 303 ? 42.732 100.075 50.343  1.00 26.04 ? 303  THR A CA  1 
ATOM   2381 C C   . THR A 1 303 ? 43.654 101.254 50.021  1.00 26.28 ? 303  THR A C   1 
ATOM   2382 O O   . THR A 1 303 ? 44.837 101.058 49.681  1.00 25.55 ? 303  THR A O   1 
ATOM   2383 C CB  . THR A 1 303 ? 42.731 99.937  51.892  1.00 25.59 ? 303  THR A CB  1 
ATOM   2384 O OG1 . THR A 1 303 ? 44.069 99.729  52.328  1.00 27.74 ? 303  THR A OG1 1 
ATOM   2385 C CG2 . THR A 1 303 ? 41.878 98.776  52.384  1.00 24.67 ? 303  THR A CG2 1 
ATOM   2386 N N   . LEU A 1 304 ? 43.114 102.465 50.147  1.00 26.23 ? 304  LEU A N   1 
ATOM   2387 C CA  . LEU A 1 304 ? 43.915 103.690 50.069  1.00 26.23 ? 304  LEU A CA  1 
ATOM   2388 C C   . LEU A 1 304 ? 45.073 103.767 51.093  1.00 26.22 ? 304  LEU A C   1 
ATOM   2389 O O   . LEU A 1 304 ? 46.149 104.255 50.758  1.00 25.87 ? 304  LEU A O   1 
ATOM   2390 C CB  . LEU A 1 304 ? 43.011 104.924 50.149  1.00 25.81 ? 304  LEU A CB  1 
ATOM   2391 C CG  . LEU A 1 304 ? 43.692 106.283 50.048  1.00 25.83 ? 304  LEU A CG  1 
ATOM   2392 C CD1 . LEU A 1 304 ? 44.245 106.491 48.644  1.00 23.83 ? 304  LEU A CD1 1 
ATOM   2393 C CD2 . LEU A 1 304 ? 42.714 107.409 50.411  1.00 25.79 ? 304  LEU A CD2 1 
ATOM   2394 N N   . ASP A 1 305 ? 44.849 103.290 52.317  1.00 26.15 ? 305  ASP A N   1 
ATOM   2395 C CA  . ASP A 1 305 ? 45.909 103.144 53.322  1.00 27.62 ? 305  ASP A CA  1 
ATOM   2396 C C   . ASP A 1 305 ? 47.126 102.381 52.776  1.00 26.71 ? 305  ASP A C   1 
ATOM   2397 O O   . ASP A 1 305 ? 48.249 102.803 52.962  1.00 26.96 ? 305  ASP A O   1 
ATOM   2398 C CB  . ASP A 1 305 ? 45.415 102.407 54.592  1.00 28.24 ? 305  ASP A CB  1 
ATOM   2399 C CG  . ASP A 1 305 ? 44.628 103.313 55.564  1.00 32.54 ? 305  ASP A CG  1 
ATOM   2400 O OD1 . ASP A 1 305 ? 44.520 104.535 55.330  1.00 36.69 ? 305  ASP A OD1 1 
ATOM   2401 O OD2 . ASP A 1 305 ? 44.119 102.778 56.583  1.00 38.34 ? 305  ASP A OD2 1 
ATOM   2402 N N   . ASN A 1 306 ? 46.883 101.241 52.156  1.00 26.54 ? 306  ASN A N   1 
ATOM   2403 C CA  . ASN A 1 306 ? 47.946 100.411 51.568  1.00 27.33 ? 306  ASN A CA  1 
ATOM   2404 C C   . ASN A 1 306 ? 48.589 101.097 50.388  1.00 26.89 ? 306  ASN A C   1 
ATOM   2405 O O   . ASN A 1 306 ? 49.787 100.994 50.229  1.00 27.60 ? 306  ASN A O   1 
ATOM   2406 C CB  . ASN A 1 306 ? 47.385 99.061  51.111  1.00 27.64 ? 306  ASN A CB  1 
ATOM   2407 C CG  . ASN A 1 306 ? 47.057 98.154  52.271  1.00 30.28 ? 306  ASN A CG  1 
ATOM   2408 O OD1 . ASN A 1 306 ? 47.555 98.343  53.382  1.00 33.04 ? 306  ASN A OD1 1 
ATOM   2409 N ND2 . ASN A 1 306 ? 46.229 97.154  52.021  1.00 30.36 ? 306  ASN A ND2 1 
ATOM   2410 N N   . MET A 1 307 ? 47.797 101.785 49.555  1.00 26.54 ? 307  MET A N   1 
ATOM   2411 C CA  . MET A 1 307 ? 48.357 102.546 48.429  1.00 26.83 ? 307  MET A CA  1 
ATOM   2412 C C   . MET A 1 307 ? 49.263 103.669 48.903  1.00 26.87 ? 307  MET A C   1 
ATOM   2413 O O   . MET A 1 307 ? 50.385 103.773 48.432  1.00 26.36 ? 307  MET A O   1 
ATOM   2414 C CB  . MET A 1 307 ? 47.260 103.110 47.511  1.00 26.49 ? 307  MET A CB  1 
ATOM   2415 C CG  . MET A 1 307 ? 47.800 103.770 46.258  1.00 25.54 ? 307  MET A CG  1 
ATOM   2416 S SD  . MET A 1 307 ? 46.531 104.607 45.299  1.00 29.35 ? 307  MET A SD  1 
ATOM   2417 C CE  . MET A 1 307 ? 45.695 103.242 44.473  1.00 29.59 ? 307  MET A CE  1 
ATOM   2418 N N   . ARG A 1 308 ? 48.757 104.520 49.809  1.00 27.02 ? 308  ARG A N   1 
ATOM   2419 C CA  . ARG A 1 308 ? 49.551 105.582 50.435  1.00 28.24 ? 308  ARG A CA  1 
ATOM   2420 C C   . ARG A 1 308 ? 50.839 105.067 51.089  1.00 27.15 ? 308  ARG A C   1 
ATOM   2421 O O   . ARG A 1 308 ? 51.870 105.709 51.010  1.00 27.36 ? 308  ARG A O   1 
ATOM   2422 C CB  . ARG A 1 308 ? 48.706 106.427 51.419  1.00 28.22 ? 308  ARG A CB  1 
ATOM   2423 C CG  . ARG A 1 308 ? 49.335 107.843 51.671  1.00 31.69 ? 308  ARG A CG  1 
ATOM   2424 C CD  . ARG A 1 308 ? 48.725 108.664 52.832  1.00 32.22 ? 308  ARG A CD  1 
ATOM   2425 N NE  . ARG A 1 308 ? 47.392 109.191 52.516  1.00 38.18 ? 308  ARG A NE  1 
ATOM   2426 C CZ  . ARG A 1 308 ? 46.268 108.548 52.805  1.00 40.57 ? 308  ARG A CZ  1 
ATOM   2427 N NH1 . ARG A 1 308 ? 46.344 107.377 53.431  1.00 39.81 ? 308  ARG A NH1 1 
ATOM   2428 N NH2 . ARG A 1 308 ? 45.085 109.070 52.480  1.00 40.53 ? 308  ARG A NH2 1 
ATOM   2429 N N   . GLU A 1 309 ? 50.779 103.905 51.725  1.00 27.32 ? 309  GLU A N   1 
ATOM   2430 C CA  . GLU A 1 309 ? 51.944 103.308 52.330  1.00 27.79 ? 309  GLU A CA  1 
ATOM   2431 C C   . GLU A 1 309 ? 53.059 103.036 51.288  1.00 26.79 ? 309  GLU A C   1 
ATOM   2432 O O   . GLU A 1 309 ? 54.234 103.350 51.523  1.00 25.58 ? 309  GLU A O   1 
ATOM   2433 C CB  . GLU A 1 309 ? 51.547 102.008 53.028  1.00 28.22 ? 309  GLU A CB  1 
ATOM   2434 C CG  . GLU A 1 309 ? 52.684 101.315 53.820  1.00 30.99 ? 309  GLU A CG  1 
ATOM   2435 C CD  . GLU A 1 309 ? 52.228 100.042 54.535  1.00 32.50 ? 309  GLU A CD  1 
ATOM   2436 O OE1 . GLU A 1 309 ? 50.991 99.839  54.707  1.00 40.61 ? 309  GLU A OE1 1 
ATOM   2437 O OE2 . GLU A 1 309 ? 53.117 99.230  54.928  1.00 39.51 ? 309  GLU A OE2 1 
ATOM   2438 N N   . VAL A 1 310 ? 52.688 102.423 50.166  1.00 25.13 ? 310  VAL A N   1 
ATOM   2439 C CA  . VAL A 1 310 ? 53.614 102.173 49.063  1.00 24.00 ? 310  VAL A CA  1 
ATOM   2440 C C   . VAL A 1 310 ? 54.169 103.495 48.505  1.00 23.54 ? 310  VAL A C   1 
ATOM   2441 O O   . VAL A 1 310 ? 55.372 103.631 48.330  1.00 23.64 ? 310  VAL A O   1 
ATOM   2442 C CB  . VAL A 1 310 ? 52.933 101.342 47.930  1.00 24.17 ? 310  VAL A CB  1 
ATOM   2443 C CG1 . VAL A 1 310 ? 53.912 101.054 46.790  1.00 23.19 ? 310  VAL A CG1 1 
ATOM   2444 C CG2 . VAL A 1 310 ? 52.349 100.023 48.510  1.00 25.00 ? 310  VAL A CG2 1 
ATOM   2445 N N   . VAL A 1 311 ? 53.290 104.456 48.228  1.00 23.28 ? 311  VAL A N   1 
ATOM   2446 C CA  . VAL A 1 311 ? 53.691 105.760 47.691  1.00 23.30 ? 311  VAL A CA  1 
ATOM   2447 C C   . VAL A 1 311 ? 54.717 106.395 48.635  1.00 24.32 ? 311  VAL A C   1 
ATOM   2448 O O   . VAL A 1 311 ? 55.752 106.861 48.209  1.00 24.61 ? 311  VAL A O   1 
ATOM   2449 C CB  . VAL A 1 311 ? 52.471 106.739 47.537  1.00 22.66 ? 311  VAL A CB  1 
ATOM   2450 C CG1 . VAL A 1 311 ? 52.956 108.159 47.234  1.00 22.13 ? 311  VAL A CG1 1 
ATOM   2451 C CG2 . VAL A 1 311 ? 51.453 106.259 46.473  1.00 20.80 ? 311  VAL A CG2 1 
ATOM   2452 N N   . GLU A 1 312 ? 54.423 106.391 49.936  1.00 25.44 ? 312  GLU A N   1 
ATOM   2453 C CA  A GLU A 1 312 ? 55.256 107.133 50.863  0.50 25.62 ? 312  GLU A CA  1 
ATOM   2454 C CA  B GLU A 1 312 ? 55.224 107.091 50.947  0.50 26.06 ? 312  GLU A CA  1 
ATOM   2455 C C   . GLU A 1 312 ? 56.610 106.473 51.112  1.00 25.84 ? 312  GLU A C   1 
ATOM   2456 O O   . GLU A 1 312 ? 57.610 107.183 51.267  1.00 26.46 ? 312  GLU A O   1 
ATOM   2457 C CB  A GLU A 1 312 ? 54.494 107.482 52.152  0.50 26.05 ? 312  GLU A CB  1 
ATOM   2458 C CB  B GLU A 1 312 ? 54.484 107.126 52.304  0.50 26.00 ? 312  GLU A CB  1 
ATOM   2459 C CG  A GLU A 1 312 ? 53.418 108.588 51.955  0.50 26.79 ? 312  GLU A CG  1 
ATOM   2460 C CG  B GLU A 1 312 ? 53.375 108.197 52.407  0.50 27.42 ? 312  GLU A CG  1 
ATOM   2461 C CD  A GLU A 1 312 ? 53.959 109.871 51.318  0.50 29.57 ? 312  GLU A CD  1 
ATOM   2462 C CD  B GLU A 1 312 ? 52.566 108.133 53.716  0.50 27.88 ? 312  GLU A CD  1 
ATOM   2463 O OE1 A GLU A 1 312 ? 54.969 110.439 51.828  0.50 29.51 ? 312  GLU A OE1 1 
ATOM   2464 O OE1 B GLU A 1 312 ? 52.748 107.185 54.520  0.50 29.96 ? 312  GLU A OE1 1 
ATOM   2465 O OE2 A GLU A 1 312 ? 53.359 110.319 50.306  0.50 30.16 ? 312  GLU A OE2 1 
ATOM   2466 O OE2 B GLU A 1 312 ? 51.723 109.033 53.931  0.50 31.07 ? 312  GLU A OE2 1 
ATOM   2467 N N   . ARG A 1 313 ? 56.686 105.138 51.092  1.00 24.86 ? 313  ARG A N   1 
ATOM   2468 C CA  . ARG A 1 313 ? 58.014 104.518 51.224  1.00 24.87 ? 313  ARG A CA  1 
ATOM   2469 C C   . ARG A 1 313 ? 58.918 104.730 49.979  1.00 24.39 ? 313  ARG A C   1 
ATOM   2470 O O   . ARG A 1 313 ? 60.144 104.760 50.092  1.00 24.63 ? 313  ARG A O   1 
ATOM   2471 C CB  . ARG A 1 313 ? 57.958 103.040 51.673  1.00 24.74 ? 313  ARG A CB  1 
ATOM   2472 C CG  . ARG A 1 313 ? 57.257 102.088 50.737  1.00 25.01 ? 313  ARG A CG  1 
ATOM   2473 C CD  . ARG A 1 313 ? 57.679 100.654 50.999  1.00 25.25 ? 313  ARG A CD  1 
ATOM   2474 N NE  . ARG A 1 313 ? 56.927 99.733  50.141  1.00 26.85 ? 313  ARG A NE  1 
ATOM   2475 C CZ  . ARG A 1 313 ? 55.956 98.909  50.545  1.00 27.65 ? 313  ARG A CZ  1 
ATOM   2476 N NH1 . ARG A 1 313 ? 55.591 98.839  51.817  1.00 27.64 ? 313  ARG A NH1 1 
ATOM   2477 N NH2 . ARG A 1 313 ? 55.338 98.135  49.650  1.00 27.61 ? 313  ARG A NH2 1 
ATOM   2478 N N   . ASN A 1 314 ? 58.315 104.910 48.802  1.00 24.07 ? 314  ASN A N   1 
ATOM   2479 C CA  . ASN A 1 314 ? 59.104 105.180 47.604  1.00 23.18 ? 314  ASN A CA  1 
ATOM   2480 C C   . ASN A 1 314 ? 59.518 106.632 47.508  1.00 23.31 ? 314  ASN A C   1 
ATOM   2481 O O   . ASN A 1 314 ? 60.620 106.925 47.063  1.00 22.43 ? 314  ASN A O   1 
ATOM   2482 C CB  . ASN A 1 314 ? 58.375 104.663 46.365  1.00 23.42 ? 314  ASN A CB  1 
ATOM   2483 C CG  . ASN A 1 314 ? 58.423 103.151 46.276  1.00 23.59 ? 314  ASN A CG  1 
ATOM   2484 O OD1 . ASN A 1 314 ? 59.397 102.592 45.766  1.00 21.12 ? 314  ASN A OD1 1 
ATOM   2485 N ND2 . ASN A 1 314 ? 57.414 102.476 46.843  1.00 21.23 ? 314  ASN A ND2 1 
ATOM   2486 N N   . ARG A 1 315 ? 58.643 107.548 47.947  1.00 23.69 ? 315  ARG A N   1 
ATOM   2487 C CA  . ARG A 1 315 ? 59.028 108.946 48.130  1.00 23.99 ? 315  ARG A CA  1 
ATOM   2488 C C   . ARG A 1 315 ? 60.135 109.145 49.181  1.00 24.43 ? 315  ARG A C   1 
ATOM   2489 O O   . ARG A 1 315 ? 61.044 109.929 48.974  1.00 24.16 ? 315  ARG A O   1 
ATOM   2490 C CB  . ARG A 1 315 ? 57.820 109.832 48.464  1.00 24.26 ? 315  ARG A CB  1 
ATOM   2491 C CG  . ARG A 1 315 ? 56.811 109.955 47.336  1.00 23.15 ? 315  ARG A CG  1 
ATOM   2492 C CD  . ARG A 1 315 ? 55.682 110.984 47.643  1.00 24.60 ? 315  ARG A CD  1 
ATOM   2493 N NE  . ARG A 1 315 ? 56.224 112.323 47.782  1.00 30.29 ? 315  ARG A NE  1 
ATOM   2494 C CZ  . ARG A 1 315 ? 56.454 112.957 48.943  1.00 34.08 ? 315  ARG A CZ  1 
ATOM   2495 N NH1 . ARG A 1 315 ? 56.140 112.420 50.127  1.00 34.45 ? 315  ARG A NH1 1 
ATOM   2496 N NH2 . ARG A 1 315 ? 56.970 114.173 48.912  1.00 35.36 ? 315  ARG A NH2 1 
ATOM   2497 N N   . ALA A 1 316 ? 60.050 108.427 50.295  1.00 24.66 ? 316  ALA A N   1 
ATOM   2498 C CA  . ALA A 1 316 ? 61.026 108.552 51.377  1.00 25.16 ? 316  ALA A CA  1 
ATOM   2499 C C   . ALA A 1 316 ? 62.406 108.086 50.886  1.00 25.27 ? 316  ALA A C   1 
ATOM   2500 O O   . ALA A 1 316 ? 63.442 108.589 51.327  1.00 25.72 ? 316  ALA A O   1 
ATOM   2501 C CB  . ALA A 1 316 ? 60.570 107.712 52.582  1.00 24.14 ? 316  ALA A CB  1 
ATOM   2502 N N   . ALA A 1 317 ? 62.403 107.145 49.945  1.00 25.09 ? 317  ALA A N   1 
ATOM   2503 C CA  . ALA A 1 317 ? 63.627 106.602 49.370  1.00 24.87 ? 317  ALA A CA  1 
ATOM   2504 C C   . ALA A 1 317 ? 64.243 107.486 48.270  1.00 24.50 ? 317  ALA A C   1 
ATOM   2505 O O   . ALA A 1 317 ? 65.230 107.092 47.666  1.00 24.01 ? 317  ALA A O   1 
ATOM   2506 C CB  . ALA A 1 317 ? 63.348 105.201 48.824  1.00 24.90 ? 317  ALA A CB  1 
ATOM   2507 N N   . GLN A 1 318 ? 63.646 108.653 48.009  1.00 23.73 ? 318  GLN A N   1 
ATOM   2508 C CA  . GLN A 1 318 ? 64.073 109.579 46.939  1.00 23.50 ? 318  GLN A CA  1 
ATOM   2509 C C   . GLN A 1 318 ? 64.095 108.922 45.547  1.00 23.27 ? 318  GLN A C   1 
ATOM   2510 O O   . GLN A 1 318 ? 64.963 109.201 44.713  1.00 23.83 ? 318  GLN A O   1 
ATOM   2511 C CB  . GLN A 1 318 ? 65.415 110.277 47.268  1.00 24.44 ? 318  GLN A CB  1 
ATOM   2512 C CG  . GLN A 1 318 ? 65.502 110.914 48.692  1.00 24.88 ? 318  GLN A CG  1 
ATOM   2513 C CD  . GLN A 1 318 ? 64.404 111.954 48.926  1.00 27.94 ? 318  GLN A CD  1 
ATOM   2514 O OE1 . GLN A 1 318 ? 64.201 112.874 48.123  1.00 28.21 ? 318  GLN A OE1 1 
ATOM   2515 N NE2 . GLN A 1 318 ? 63.670 111.791 50.019  1.00 33.49 ? 318  GLN A NE2 1 
ATOM   2516 N N   . LEU A 1 319 ? 63.124 108.054 45.291  1.00 21.89 ? 319  LEU A N   1 
ATOM   2517 C CA  . LEU A 1 319 ? 63.001 107.449 43.978  1.00 21.41 ? 319  LEU A CA  1 
ATOM   2518 C C   . LEU A 1 319 ? 62.408 108.459 42.970  1.00 20.69 ? 319  LEU A C   1 
ATOM   2519 O O   . LEU A 1 319 ? 61.438 109.153 43.303  1.00 20.48 ? 319  LEU A O   1 
ATOM   2520 C CB  . LEU A 1 319 ? 62.119 106.214 44.059  1.00 20.80 ? 319  LEU A CB  1 
ATOM   2521 C CG  . LEU A 1 319 ? 62.096 105.294 42.847  1.00 20.85 ? 319  LEU A CG  1 
ATOM   2522 C CD1 . LEU A 1 319 ? 63.323 104.417 42.854  1.00 19.32 ? 319  LEU A CD1 1 
ATOM   2523 C CD2 . LEU A 1 319 ? 60.832 104.434 42.913  1.00 19.21 ? 319  LEU A CD2 1 
ATOM   2524 N N   . PRO A 1 320 ? 63.012 108.561 41.758  1.00 20.32 ? 320  PRO A N   1 
ATOM   2525 C CA  . PRO A 1 320 ? 62.394 109.344 40.707  1.00 20.05 ? 320  PRO A CA  1 
ATOM   2526 C C   . PRO A 1 320 ? 61.075 108.643 40.377  1.00 20.45 ? 320  PRO A C   1 
ATOM   2527 O O   . PRO A 1 320 ? 61.072 107.455 40.036  1.00 19.84 ? 320  PRO A O   1 
ATOM   2528 C CB  . PRO A 1 320 ? 63.414 109.266 39.560  1.00 19.69 ? 320  PRO A CB  1 
ATOM   2529 C CG  . PRO A 1 320 ? 64.706 108.933 40.211  1.00 20.18 ? 320  PRO A CG  1 
ATOM   2530 C CD  . PRO A 1 320 ? 64.298 107.980 41.310  1.00 20.08 ? 320  PRO A CD  1 
ATOM   2531 N N   . TYR A 1 321 ? 59.961 109.371 40.515  1.00 19.71 ? 321  TYR A N   1 
ATOM   2532 C CA  . TYR A 1 321 ? 58.680 108.733 40.633  1.00 19.38 ? 321  TYR A CA  1 
ATOM   2533 C C   . TYR A 1 321 ? 57.612 109.779 40.372  1.00 19.87 ? 321  TYR A C   1 
ATOM   2534 O O   . TYR A 1 321 ? 57.241 110.559 41.271  1.00 19.32 ? 321  TYR A O   1 
ATOM   2535 C CB  . TYR A 1 321 ? 58.623 108.173 42.048  1.00 19.27 ? 321  TYR A CB  1 
ATOM   2536 C CG  . TYR A 1 321 ? 57.325 107.638 42.565  1.00 19.41 ? 321  TYR A CG  1 
ATOM   2537 C CD1 . TYR A 1 321 ? 56.329 107.118 41.712  1.00 18.57 ? 321  TYR A CD1 1 
ATOM   2538 C CD2 . TYR A 1 321 ? 57.106 107.603 43.936  1.00 19.96 ? 321  TYR A CD2 1 
ATOM   2539 C CE1 . TYR A 1 321 ? 55.107 106.610 42.239  1.00 17.82 ? 321  TYR A CE1 1 
ATOM   2540 C CE2 . TYR A 1 321 ? 55.909 107.096 44.469  1.00 20.85 ? 321  TYR A CE2 1 
ATOM   2541 C CZ  . TYR A 1 321 ? 54.930 106.604 43.617  1.00 21.42 ? 321  TYR A CZ  1 
ATOM   2542 O OH  . TYR A 1 321 ? 53.789 106.095 44.185  1.00 21.62 ? 321  TYR A OH  1 
ATOM   2543 N N   . ASP A 1 322 ? 57.133 109.813 39.128  1.00 19.72 ? 322  ASP A N   1 
ATOM   2544 C CA  . ASP A 1 322 ? 56.214 110.857 38.693  1.00 20.05 ? 322  ASP A CA  1 
ATOM   2545 C C   . ASP A 1 322 ? 54.752 110.449 38.757  1.00 19.86 ? 322  ASP A C   1 
ATOM   2546 O O   . ASP A 1 322 ? 53.896 111.314 38.974  1.00 19.07 ? 322  ASP A O   1 
ATOM   2547 C CB  . ASP A 1 322 ? 56.496 111.266 37.256  1.00 20.51 ? 322  ASP A CB  1 
ATOM   2548 C CG  . ASP A 1 322 ? 57.501 112.369 37.152  1.00 23.03 ? 322  ASP A CG  1 
ATOM   2549 O OD1 . ASP A 1 322 ? 57.137 113.459 36.669  1.00 24.93 ? 322  ASP A OD1 1 
ATOM   2550 O OD2 . ASP A 1 322 ? 58.653 112.125 37.543  1.00 23.19 ? 322  ASP A OD2 1 
ATOM   2551 N N   . VAL A 1 323 ? 54.455 109.164 38.514  1.00 19.54 ? 323  VAL A N   1 
ATOM   2552 C CA  . VAL A 1 323 ? 53.023 108.780 38.313  1.00 18.92 ? 323  VAL A CA  1 
ATOM   2553 C C   . VAL A 1 323 ? 52.640 107.572 39.150  1.00 19.26 ? 323  VAL A C   1 
ATOM   2554 O O   . VAL A 1 323 ? 53.375 106.579 39.197  1.00 19.08 ? 323  VAL A O   1 
ATOM   2555 C CB  . VAL A 1 323 ? 52.740 108.423 36.828  1.00 19.15 ? 323  VAL A CB  1 
ATOM   2556 C CG1 . VAL A 1 323 ? 51.260 108.276 36.538  1.00 16.63 ? 323  VAL A CG1 1 
ATOM   2557 C CG2 . VAL A 1 323 ? 53.402 109.419 35.847  1.00 16.29 ? 323  VAL A CG2 1 
ATOM   2558 N N   . GLN A 1 324 ? 51.483 107.663 39.803  1.00 18.68 ? 324  GLN A N   1 
ATOM   2559 C CA  . GLN A 1 324 ? 50.899 106.554 40.489  1.00 18.76 ? 324  GLN A CA  1 
ATOM   2560 C C   . GLN A 1 324 ? 49.655 106.145 39.731  1.00 19.04 ? 324  GLN A C   1 
ATOM   2561 O O   . GLN A 1 324 ? 48.810 106.996 39.395  1.00 19.75 ? 324  GLN A O   1 
ATOM   2562 C CB  . GLN A 1 324 ? 50.553 106.950 41.931  1.00 19.33 ? 324  GLN A CB  1 
ATOM   2563 C CG  . GLN A 1 324 ? 49.837 105.850 42.708  1.00 19.95 ? 324  GLN A CG  1 
ATOM   2564 C CD  . GLN A 1 324 ? 50.697 104.640 42.930  1.00 20.16 ? 324  GLN A CD  1 
ATOM   2565 O OE1 . GLN A 1 324 ? 51.911 104.744 43.114  1.00 19.32 ? 324  GLN A OE1 1 
ATOM   2566 N NE2 . GLN A 1 324 ? 50.079 103.475 42.910  1.00 18.83 ? 324  GLN A NE2 1 
ATOM   2567 N N   . HIS A 1 325 ? 49.525 104.844 39.453  1.00 18.65 ? 325  HIS A N   1 
ATOM   2568 C CA  . HIS A 1 325 ? 48.303 104.310 38.809  1.00 18.96 ? 325  HIS A CA  1 
ATOM   2569 C C   . HIS A 1 325 ? 47.379 103.707 39.854  1.00 19.27 ? 325  HIS A C   1 
ATOM   2570 O O   . HIS A 1 325 ? 47.831 103.216 40.880  1.00 20.01 ? 325  HIS A O   1 
ATOM   2571 C CB  . HIS A 1 325 ? 48.637 103.230 37.763  1.00 18.74 ? 325  HIS A CB  1 
ATOM   2572 C CG  . HIS A 1 325 ? 49.409 103.746 36.581  1.00 19.06 ? 325  HIS A CG  1 
ATOM   2573 N ND1 . HIS A 1 325 ? 49.164 103.326 35.294  1.00 16.88 ? 325  HIS A ND1 1 
ATOM   2574 C CD2 . HIS A 1 325 ? 50.398 104.669 36.491  1.00 18.77 ? 325  HIS A CD2 1 
ATOM   2575 C CE1 . HIS A 1 325 ? 49.954 103.980 34.454  1.00 15.62 ? 325  HIS A CE1 1 
ATOM   2576 N NE2 . HIS A 1 325 ? 50.720 104.794 35.158  1.00 19.01 ? 325  HIS A NE2 1 
ATOM   2577 N N   . ALA A 1 326 ? 46.079 103.737 39.579  1.00 19.36 ? 326  ALA A N   1 
ATOM   2578 C CA  . ALA A 1 326 ? 45.121 103.140 40.471  1.00 19.92 ? 326  ALA A CA  1 
ATOM   2579 C C   . ALA A 1 326 ? 44.300 102.180 39.629  1.00 19.65 ? 326  ALA A C   1 
ATOM   2580 O O   . ALA A 1 326 ? 43.655 102.591 38.669  1.00 19.36 ? 326  ALA A O   1 
ATOM   2581 C CB  . ALA A 1 326 ? 44.227 104.218 41.091  1.00 19.48 ? 326  ALA A CB  1 
ATOM   2582 N N   . ASP A 1 327 ? 44.330 100.919 40.031  1.00 20.54 ? 327  ASP A N   1 
ATOM   2583 C CA  . ASP A 1 327 ? 43.712 99.800  39.341  1.00 21.66 ? 327  ASP A CA  1 
ATOM   2584 C C   . ASP A 1 327 ? 42.271 99.649  39.885  1.00 22.47 ? 327  ASP A C   1 
ATOM   2585 O O   . ASP A 1 327 ? 41.818 100.503 40.652  1.00 22.50 ? 327  ASP A O   1 
ATOM   2586 C CB  . ASP A 1 327 ? 44.548 98.539  39.606  1.00 22.09 ? 327  ASP A CB  1 
ATOM   2587 C CG  . ASP A 1 327 ? 44.440 97.505  38.498  1.00 24.23 ? 327  ASP A CG  1 
ATOM   2588 O OD1 . ASP A 1 327 ? 43.359 97.351  37.881  1.00 26.46 ? 327  ASP A OD1 1 
ATOM   2589 O OD2 . ASP A 1 327 ? 45.447 96.825  38.253  1.00 22.02 ? 327  ASP A OD2 1 
ATOM   2590 N N   . ILE A 1 328 ? 41.565 98.587  39.475  1.00 22.14 ? 328  ILE A N   1 
ATOM   2591 C CA  . ILE A 1 328 ? 40.131 98.418  39.751  1.00 22.15 ? 328  ILE A CA  1 
ATOM   2592 C C   . ILE A 1 328 ? 39.721 98.385  41.223  1.00 22.91 ? 328  ILE A C   1 
ATOM   2593 O O   . ILE A 1 328 ? 38.558 98.624  41.498  1.00 23.57 ? 328  ILE A O   1 
ATOM   2594 C CB  . ILE A 1 328 ? 39.496 97.202  39.007  1.00 21.49 ? 328  ILE A CB  1 
ATOM   2595 C CG1 . ILE A 1 328 ? 40.233 95.882  39.327  1.00 22.27 ? 328  ILE A CG1 1 
ATOM   2596 C CG2 . ILE A 1 328 ? 39.416 97.468  37.536  1.00 19.11 ? 328  ILE A CG2 1 
ATOM   2597 C CD1 . ILE A 1 328 ? 39.534 94.646  38.759  1.00 21.81 ? 328  ILE A CD1 1 
ATOM   2598 N N   . ASP A 1 329 ? 40.663 98.085  42.129  1.00 23.21 ? 329  ASP A N   1 
ATOM   2599 C CA  . ASP A 1 329 ? 40.446 98.191  43.583  1.00 24.79 ? 329  ASP A CA  1 
ATOM   2600 C C   . ASP A 1 329 ? 39.974 99.561  44.131  1.00 24.79 ? 329  ASP A C   1 
ATOM   2601 O O   . ASP A 1 329 ? 39.300 99.587  45.147  1.00 25.50 ? 329  ASP A O   1 
ATOM   2602 C CB  . ASP A 1 329 ? 41.592 97.555  44.444  1.00 24.61 ? 329  ASP A CB  1 
ATOM   2603 C CG  . ASP A 1 329 ? 42.994 98.041  44.072  1.00 26.60 ? 329  ASP A CG  1 
ATOM   2604 O OD1 . ASP A 1 329 ? 43.367 98.019  42.887  1.00 29.01 ? 329  ASP A OD1 1 
ATOM   2605 O OD2 . ASP A 1 329 ? 43.764 98.397  44.979  1.00 30.66 ? 329  ASP A OD2 1 
ATOM   2606 N N   . TYR A 1 330 ? 40.297 100.675 43.455  1.00 25.30 ? 330  TYR A N   1 
ATOM   2607 C CA  . TYR A 1 330 ? 39.735 102.012 43.814  1.00 24.51 ? 330  TYR A CA  1 
ATOM   2608 C C   . TYR A 1 330 ? 38.226 102.086 43.667  1.00 25.04 ? 330  TYR A C   1 
ATOM   2609 O O   . TYR A 1 330 ? 37.559 102.780 44.427  1.00 25.94 ? 330  TYR A O   1 
ATOM   2610 C CB  . TYR A 1 330 ? 40.409 103.194 43.080  1.00 23.74 ? 330  TYR A CB  1 
ATOM   2611 C CG  . TYR A 1 330 ? 39.952 103.502 41.650  1.00 24.24 ? 330  TYR A CG  1 
ATOM   2612 C CD1 . TYR A 1 330 ? 38.742 104.162 41.400  1.00 22.69 ? 330  TYR A CD1 1 
ATOM   2613 C CD2 . TYR A 1 330 ? 40.750 103.156 40.543  1.00 22.19 ? 330  TYR A CD2 1 
ATOM   2614 C CE1 . TYR A 1 330 ? 38.314 104.436 40.111  1.00 20.96 ? 330  TYR A CE1 1 
ATOM   2615 C CE2 . TYR A 1 330 ? 40.332 103.438 39.239  1.00 22.05 ? 330  TYR A CE2 1 
ATOM   2616 C CZ  . TYR A 1 330 ? 39.116 104.085 39.029  1.00 22.13 ? 330  TYR A CZ  1 
ATOM   2617 O OH  . TYR A 1 330 ? 38.692 104.371 37.746  1.00 21.16 ? 330  TYR A OH  1 
ATOM   2618 N N   . MET A 1 331 ? 37.686 101.358 42.702  1.00 24.92 ? 331  MET A N   1 
ATOM   2619 C CA  . MET A 1 331 ? 36.265 101.420 42.393  1.00 24.91 ? 331  MET A CA  1 
ATOM   2620 C C   . MET A 1 331 ? 35.365 100.866 43.511  1.00 25.06 ? 331  MET A C   1 
ATOM   2621 O O   . MET A 1 331 ? 35.785 100.077 44.336  1.00 23.87 ? 331  MET A O   1 
ATOM   2622 C CB  . MET A 1 331 ? 36.004 100.672 41.093  1.00 24.57 ? 331  MET A CB  1 
ATOM   2623 C CG  . MET A 1 331 ? 36.898 101.127 39.916  1.00 24.31 ? 331  MET A CG  1 
ATOM   2624 S SD  . MET A 1 331 ? 36.527 100.195 38.441  1.00 26.01 ? 331  MET A SD  1 
ATOM   2625 C CE  . MET A 1 331 ? 37.542 101.073 37.191  1.00 21.39 ? 331  MET A CE  1 
ATOM   2626 N N   . ASP A 1 332 ? 34.119 101.309 43.526  1.00 26.70 ? 332  ASP A N   1 
ATOM   2627 C CA  . ASP A 1 332 ? 33.100 100.668 44.343  1.00 28.71 ? 332  ASP A CA  1 
ATOM   2628 C C   . ASP A 1 332 ? 32.596 99.394  43.620  1.00 28.74 ? 332  ASP A C   1 
ATOM   2629 O O   . ASP A 1 332 ? 31.831 99.451  42.636  1.00 28.90 ? 332  ASP A O   1 
ATOM   2630 C CB  . ASP A 1 332 ? 31.958 101.656 44.650  1.00 29.32 ? 332  ASP A CB  1 
ATOM   2631 C CG  . ASP A 1 332 ? 30.839 101.026 45.479  1.00 31.65 ? 332  ASP A CG  1 
ATOM   2632 O OD1 . ASP A 1 332 ? 31.046 99.966  46.107  1.00 33.64 ? 332  ASP A OD1 1 
ATOM   2633 O OD2 . ASP A 1 332 ? 29.739 101.611 45.503  1.00 38.93 ? 332  ASP A OD2 1 
ATOM   2634 N N   . GLU A 1 333 ? 33.068 98.250  44.100  1.00 29.03 ? 333  GLU A N   1 
ATOM   2635 C CA  . GLU A 1 333 ? 32.731 96.932  43.500  1.00 29.19 ? 333  GLU A CA  1 
ATOM   2636 C C   . GLU A 1 333 ? 33.147 96.799  42.031  1.00 27.30 ? 333  GLU A C   1 
ATOM   2637 O O   . GLU A 1 333 ? 32.378 96.281  41.222  1.00 25.99 ? 333  GLU A O   1 
ATOM   2638 C CB  . GLU A 1 333 ? 31.237 96.632  43.636  1.00 30.97 ? 333  GLU A CB  1 
ATOM   2639 C CG  . GLU A 1 333 ? 30.647 96.940  45.021  1.00 35.86 ? 333  GLU A CG  1 
ATOM   2640 C CD  . GLU A 1 333 ? 30.795 95.800  45.986  1.00 44.08 ? 333  GLU A CD  1 
ATOM   2641 O OE1 . GLU A 1 333 ? 31.874 95.145  46.013  1.00 47.66 ? 333  GLU A OE1 1 
ATOM   2642 O OE2 . GLU A 1 333 ? 29.814 95.560  46.727  1.00 48.29 ? 333  GLU A OE2 1 
ATOM   2643 N N   . ARG A 1 334 ? 34.342 97.312  41.698  1.00 25.80 ? 334  ARG A N   1 
ATOM   2644 C CA  A ARG A 1 334 ? 34.899 97.184  40.338  0.50 25.32 ? 334  ARG A CA  1 
ATOM   2645 C CA  B ARG A 1 334 ? 34.907 97.198  40.351  0.50 25.31 ? 334  ARG A CA  1 
ATOM   2646 C C   . ARG A 1 334 ? 34.046 97.872  39.258  1.00 25.15 ? 334  ARG A C   1 
ATOM   2647 O O   . ARG A 1 334 ? 34.060 97.478  38.100  1.00 24.49 ? 334  ARG A O   1 
ATOM   2648 C CB  A ARG A 1 334 ? 35.135 95.707  39.965  0.50 24.54 ? 334  ARG A CB  1 
ATOM   2649 C CB  B ARG A 1 334 ? 35.240 95.725  40.055  0.50 24.60 ? 334  ARG A CB  1 
ATOM   2650 C CG  A ARG A 1 334 ? 36.212 94.989  40.780  0.50 24.13 ? 334  ARG A CG  1 
ATOM   2651 C CG  B ARG A 1 334 ? 36.274 95.190  41.054  0.50 23.89 ? 334  ARG A CG  1 
ATOM   2652 C CD  A ARG A 1 334 ? 35.612 94.096  41.840  0.50 23.64 ? 334  ARG A CD  1 
ATOM   2653 C CD  B ARG A 1 334 ? 36.506 93.705  40.964  0.50 23.37 ? 334  ARG A CD  1 
ATOM   2654 N NE  A ARG A 1 334 ? 34.512 93.292  41.311  0.50 22.79 ? 334  ARG A NE  1 
ATOM   2655 N NE  B ARG A 1 334 ? 37.778 93.346  41.590  0.50 23.10 ? 334  ARG A NE  1 
ATOM   2656 C CZ  A ARG A 1 334 ? 33.457 92.900  42.024  0.50 20.32 ? 334  ARG A CZ  1 
ATOM   2657 C CZ  B ARG A 1 334 ? 38.378 92.164  41.464  0.50 22.30 ? 334  ARG A CZ  1 
ATOM   2658 N NH1 A ARG A 1 334 ? 33.358 93.236  43.306  0.50 18.20 ? 334  ARG A NH1 1 
ATOM   2659 N NH1 B ARG A 1 334 ? 37.819 91.194  40.746  0.50 21.87 ? 334  ARG A NH1 1 
ATOM   2660 N NH2 A ARG A 1 334 ? 32.512 92.164  41.453  0.50 18.88 ? 334  ARG A NH2 1 
ATOM   2661 N NH2 B ARG A 1 334 ? 39.528 91.948  42.073  0.50 20.69 ? 334  ARG A NH2 1 
ATOM   2662 N N   . ARG A 1 335 ? 33.315 98.911  39.632  1.00 25.56 ? 335  ARG A N   1 
ATOM   2663 C CA  . ARG A 1 335 ? 32.487 99.607  38.657  1.00 26.73 ? 335  ARG A CA  1 
ATOM   2664 C C   . ARG A 1 335 ? 33.080 100.948 38.270  1.00 26.82 ? 335  ARG A C   1 
ATOM   2665 O O   . ARG A 1 335 ? 33.481 101.725 39.151  1.00 27.42 ? 335  ARG A O   1 
ATOM   2666 C CB  . ARG A 1 335 ? 31.064 99.780  39.188  1.00 26.98 ? 335  ARG A CB  1 
ATOM   2667 C CG  . ARG A 1 335 ? 30.257 98.465  39.220  1.00 29.73 ? 335  ARG A CG  1 
ATOM   2668 C CD  . ARG A 1 335 ? 28.839 98.736  39.671  1.00 34.68 ? 335  ARG A CD  1 
ATOM   2669 N NE  . ARG A 1 335 ? 28.935 99.461  40.921  1.00 37.21 ? 335  ARG A NE  1 
ATOM   2670 C CZ  . ARG A 1 335 ? 27.938 100.047 41.549  1.00 39.89 ? 335  ARG A CZ  1 
ATOM   2671 N NH1 . ARG A 1 335 ? 26.691 99.990  41.053  1.00 36.53 ? 335  ARG A NH1 1 
ATOM   2672 N NH2 . ARG A 1 335 ? 28.221 100.692 42.682  1.00 38.96 ? 335  ARG A NH2 1 
ATOM   2673 N N   . ASP A 1 336 ? 33.167 101.202 36.958  1.00 26.47 ? 336  ASP A N   1 
ATOM   2674 C CA  . ASP A 1 336 ? 33.681 102.465 36.427  1.00 25.75 ? 336  ASP A CA  1 
ATOM   2675 C C   . ASP A 1 336 ? 32.950 103.635 37.061  1.00 26.21 ? 336  ASP A C   1 
ATOM   2676 O O   . ASP A 1 336 ? 31.721 103.569 37.294  1.00 25.41 ? 336  ASP A O   1 
ATOM   2677 C CB  . ASP A 1 336 ? 33.394 102.595 34.923  1.00 25.80 ? 336  ASP A CB  1 
ATOM   2678 C CG  . ASP A 1 336 ? 34.389 101.852 34.032  1.00 26.96 ? 336  ASP A CG  1 
ATOM   2679 O OD1 . ASP A 1 336 ? 35.408 101.360 34.533  1.00 22.88 ? 336  ASP A OD1 1 
ATOM   2680 O OD2 . ASP A 1 336 ? 34.117 101.769 32.803  1.00 28.10 ? 336  ASP A OD2 1 
ATOM   2681 N N   . PHE A 1 337 ? 33.704 104.719 37.257  1.00 25.50 ? 337  PHE A N   1 
ATOM   2682 C CA  . PHE A 1 337 ? 33.178 106.058 37.590  1.00 26.32 ? 337  PHE A CA  1 
ATOM   2683 C C   . PHE A 1 337 ? 32.607 106.135 38.996  1.00 26.06 ? 337  PHE A C   1 
ATOM   2684 O O   . PHE A 1 337 ? 31.730 106.926 39.276  1.00 26.08 ? 337  PHE A O   1 
ATOM   2685 C CB  . PHE A 1 337 ? 32.219 106.616 36.503  1.00 25.26 ? 337  PHE A CB  1 
ATOM   2686 C CG  . PHE A 1 337 ? 32.783 106.523 35.097  1.00 25.63 ? 337  PHE A CG  1 
ATOM   2687 C CD1 . PHE A 1 337 ? 33.956 107.214 34.748  1.00 23.38 ? 337  PHE A CD1 1 
ATOM   2688 C CD2 . PHE A 1 337 ? 32.154 105.723 34.130  1.00 22.91 ? 337  PHE A CD2 1 
ATOM   2689 C CE1 . PHE A 1 337 ? 34.496 107.103 33.446  1.00 22.23 ? 337  PHE A CE1 1 
ATOM   2690 C CE2 . PHE A 1 337 ? 32.693 105.598 32.853  1.00 23.07 ? 337  PHE A CE2 1 
ATOM   2691 C CZ  . PHE A 1 337 ? 33.854 106.310 32.504  1.00 22.32 ? 337  PHE A CZ  1 
ATOM   2692 N N   . THR A 1 338 ? 33.169 105.309 39.873  1.00 26.92 ? 338  THR A N   1 
ATOM   2693 C CA  . THR A 1 338 ? 32.828 105.281 41.297  1.00 27.17 ? 338  THR A CA  1 
ATOM   2694 C C   . THR A 1 338 ? 34.156 105.072 42.037  1.00 27.18 ? 338  THR A C   1 
ATOM   2695 O O   . THR A 1 338 ? 35.108 104.590 41.444  1.00 25.98 ? 338  THR A O   1 
ATOM   2696 C CB  . THR A 1 338 ? 31.960 104.053 41.652  1.00 27.00 ? 338  THR A CB  1 
ATOM   2697 O OG1 . THR A 1 338 ? 32.759 102.871 41.562  1.00 27.22 ? 338  THR A OG1 1 
ATOM   2698 C CG2 . THR A 1 338 ? 30.709 103.918 40.753  1.00 27.17 ? 338  THR A CG2 1 
ATOM   2699 N N   . TYR A 1 339 ? 34.219 105.403 43.321  1.00 27.27 ? 339  TYR A N   1 
ATOM   2700 C CA  . TYR A 1 339 ? 35.302 104.881 44.150  1.00 28.65 ? 339  TYR A CA  1 
ATOM   2701 C C   . TYR A 1 339 ? 34.715 104.340 45.443  1.00 29.39 ? 339  TYR A C   1 
ATOM   2702 O O   . TYR A 1 339 ? 33.602 104.700 45.830  1.00 30.46 ? 339  TYR A O   1 
ATOM   2703 C CB  . TYR A 1 339 ? 36.421 105.911 44.356  1.00 29.00 ? 339  TYR A CB  1 
ATOM   2704 C CG  . TYR A 1 339 ? 36.054 107.083 45.242  1.00 30.92 ? 339  TYR A CG  1 
ATOM   2705 C CD1 . TYR A 1 339 ? 36.372 107.076 46.616  1.00 32.08 ? 339  TYR A CD1 1 
ATOM   2706 C CD2 . TYR A 1 339 ? 35.422 108.198 44.719  1.00 31.03 ? 339  TYR A CD2 1 
ATOM   2707 C CE1 . TYR A 1 339 ? 36.052 108.155 47.438  1.00 34.40 ? 339  TYR A CE1 1 
ATOM   2708 C CE2 . TYR A 1 339 ? 35.081 109.283 45.539  1.00 32.76 ? 339  TYR A CE2 1 
ATOM   2709 C CZ  . TYR A 1 339 ? 35.402 109.247 46.888  1.00 32.91 ? 339  TYR A CZ  1 
ATOM   2710 O OH  . TYR A 1 339 ? 35.084 110.309 47.687  1.00 35.44 ? 339  TYR A OH  1 
ATOM   2711 N N   . ASP A 1 340 ? 35.444 103.444 46.090  1.00 30.05 ? 340  ASP A N   1 
ATOM   2712 C CA  . ASP A 1 340 ? 34.973 102.760 47.278  1.00 30.47 ? 340  ASP A CA  1 
ATOM   2713 C C   . ASP A 1 340 ? 35.040 103.736 48.471  1.00 30.81 ? 340  ASP A C   1 
ATOM   2714 O O   . ASP A 1 340 ? 36.124 104.108 48.941  1.00 30.02 ? 340  ASP A O   1 
ATOM   2715 C CB  . ASP A 1 340 ? 35.839 101.516 47.462  1.00 31.00 ? 340  ASP A CB  1 
ATOM   2716 C CG  . ASP A 1 340 ? 35.391 100.632 48.602  1.00 32.70 ? 340  ASP A CG  1 
ATOM   2717 O OD1 . ASP A 1 340 ? 34.659 101.092 49.485  1.00 37.49 ? 340  ASP A OD1 1 
ATOM   2718 O OD2 . ASP A 1 340 ? 35.796 99.459  48.623  1.00 36.15 ? 340  ASP A OD2 1 
ATOM   2719 N N   . SER A 1 341 ? 33.872 104.175 48.934  1.00 31.19 ? 341  SER A N   1 
ATOM   2720 C CA  . SER A 1 341 ? 33.754 105.174 50.012  1.00 31.75 ? 341  SER A CA  1 
ATOM   2721 C C   . SER A 1 341 ? 34.287 104.699 51.366  1.00 31.63 ? 341  SER A C   1 
ATOM   2722 O O   . SER A 1 341 ? 34.520 105.518 52.251  1.00 33.02 ? 341  SER A O   1 
ATOM   2723 C CB  . SER A 1 341 ? 32.290 105.592 50.164  1.00 32.26 ? 341  SER A CB  1 
ATOM   2724 O OG  . SER A 1 341 ? 31.517 104.463 50.580  1.00 32.37 ? 341  SER A OG  1 
ATOM   2725 N N   . VAL A 1 342 ? 34.483 103.391 51.536  1.00 31.68 ? 342  VAL A N   1 
ATOM   2726 C CA  . VAL A 1 342 ? 35.066 102.836 52.775  1.00 31.55 ? 342  VAL A CA  1 
ATOM   2727 C C   . VAL A 1 342 ? 36.548 102.566 52.545  1.00 31.00 ? 342  VAL A C   1 
ATOM   2728 O O   . VAL A 1 342 ? 37.418 103.217 53.126  1.00 31.11 ? 342  VAL A O   1 
ATOM   2729 C CB  . VAL A 1 342 ? 34.323 101.542 53.277  1.00 31.38 ? 342  VAL A CB  1 
ATOM   2730 C CG1 . VAL A 1 342 ? 35.083 100.847 54.447  1.00 31.23 ? 342  VAL A CG1 1 
ATOM   2731 C CG2 . VAL A 1 342 ? 32.883 101.850 53.659  1.00 32.61 ? 342  VAL A CG2 1 
ATOM   2732 N N   . ASP A 1 343 ? 36.858 101.614 51.678  1.00 30.92 ? 343  ASP A N   1 
ATOM   2733 C CA  . ASP A 1 343 ? 38.265 101.237 51.489  1.00 30.01 ? 343  ASP A CA  1 
ATOM   2734 C C   . ASP A 1 343 ? 39.112 102.351 50.870  1.00 28.71 ? 343  ASP A C   1 
ATOM   2735 O O   . ASP A 1 343 ? 40.316 102.423 51.152  1.00 28.90 ? 343  ASP A O   1 
ATOM   2736 C CB  . ASP A 1 343 ? 38.379 99.938  50.707  1.00 30.79 ? 343  ASP A CB  1 
ATOM   2737 C CG  . ASP A 1 343 ? 38.071 98.707  51.561  1.00 32.88 ? 343  ASP A CG  1 
ATOM   2738 O OD1 . ASP A 1 343 ? 37.657 98.852  52.729  1.00 36.59 ? 343  ASP A OD1 1 
ATOM   2739 O OD2 . ASP A 1 343 ? 38.273 97.580  51.061  1.00 34.45 ? 343  ASP A OD2 1 
ATOM   2740 N N   . PHE A 1 344 ? 38.484 103.220 50.071  1.00 26.70 ? 344  PHE A N   1 
ATOM   2741 C CA  . PHE A 1 344 ? 39.156 104.401 49.482  1.00 26.38 ? 344  PHE A CA  1 
ATOM   2742 C C   . PHE A 1 344 ? 38.520 105.729 49.969  1.00 26.90 ? 344  PHE A C   1 
ATOM   2743 O O   . PHE A 1 344 ? 38.484 106.734 49.237  1.00 26.75 ? 344  PHE A O   1 
ATOM   2744 C CB  . PHE A 1 344 ? 39.205 104.327 47.943  1.00 25.64 ? 344  PHE A CB  1 
ATOM   2745 C CG  . PHE A 1 344 ? 40.323 103.448 47.410  1.00 26.28 ? 344  PHE A CG  1 
ATOM   2746 C CD1 . PHE A 1 344 ? 40.263 102.062 47.534  1.00 25.89 ? 344  PHE A CD1 1 
ATOM   2747 C CD2 . PHE A 1 344 ? 41.451 104.018 46.825  1.00 26.65 ? 344  PHE A CD2 1 
ATOM   2748 C CE1 . PHE A 1 344 ? 41.299 101.245 47.076  1.00 27.11 ? 344  PHE A CE1 1 
ATOM   2749 C CE2 . PHE A 1 344 ? 42.527 103.210 46.382  1.00 27.34 ? 344  PHE A CE2 1 
ATOM   2750 C CZ  . PHE A 1 344 ? 42.442 101.825 46.501  1.00 26.74 ? 344  PHE A CZ  1 
ATOM   2751 N N   . LYS A 1 345 ? 38.026 105.715 51.215  1.00 27.73 ? 345  LYS A N   1 
ATOM   2752 C CA  . LYS A 1 345 ? 37.583 106.932 51.917  1.00 28.39 ? 345  LYS A CA  1 
ATOM   2753 C C   . LYS A 1 345 ? 38.780 107.846 51.951  1.00 27.93 ? 345  LYS A C   1 
ATOM   2754 O O   . LYS A 1 345 ? 39.877 107.436 52.377  1.00 27.58 ? 345  LYS A O   1 
ATOM   2755 C CB  . LYS A 1 345 ? 37.160 106.617 53.360  1.00 28.87 ? 345  LYS A CB  1 
ATOM   2756 C CG  . LYS A 1 345 ? 36.833 107.852 54.211  1.00 30.54 ? 345  LYS A CG  1 
ATOM   2757 C CD  . LYS A 1 345 ? 36.348 107.468 55.606  1.00 30.84 ? 345  LYS A CD  1 
ATOM   2758 C CE  . LYS A 1 345 ? 36.014 108.729 56.442  1.00 35.81 ? 345  LYS A CE  1 
ATOM   2759 N NZ  . LYS A 1 345 ? 35.628 108.388 57.867  1.00 38.77 ? 345  LYS A NZ  1 
ATOM   2760 N N   . GLY A 1 346 ? 38.596 109.074 51.493  1.00 27.47 ? 346  GLY A N   1 
ATOM   2761 C CA  . GLY A 1 346 ? 39.701 110.015 51.560  1.00 28.19 ? 346  GLY A CA  1 
ATOM   2762 C C   . GLY A 1 346 ? 40.464 110.135 50.249  1.00 27.16 ? 346  GLY A C   1 
ATOM   2763 O O   . GLY A 1 346 ? 41.427 110.862 50.196  1.00 26.04 ? 346  GLY A O   1 
ATOM   2764 N N   . PHE A 1 347 ? 39.985 109.464 49.197  1.00 27.56 ? 347  PHE A N   1 
ATOM   2765 C CA  . PHE A 1 347 ? 40.619 109.510 47.858  1.00 27.67 ? 347  PHE A CA  1 
ATOM   2766 C C   . PHE A 1 347 ? 40.926 110.925 47.336  1.00 27.77 ? 347  PHE A C   1 
ATOM   2767 O O   . PHE A 1 347 ? 42.089 111.181 46.970  1.00 27.93 ? 347  PHE A O   1 
ATOM   2768 C CB  . PHE A 1 347 ? 39.831 108.692 46.811  1.00 27.78 ? 347  PHE A CB  1 
ATOM   2769 C CG  . PHE A 1 347 ? 40.691 108.108 45.677  1.00 28.40 ? 347  PHE A CG  1 
ATOM   2770 C CD1 . PHE A 1 347 ? 42.090 108.014 45.790  1.00 29.06 ? 347  PHE A CD1 1 
ATOM   2771 C CD2 . PHE A 1 347 ? 40.081 107.590 44.526  1.00 28.54 ? 347  PHE A CD2 1 
ATOM   2772 C CE1 . PHE A 1 347 ? 42.887 107.446 44.744  1.00 28.62 ? 347  PHE A CE1 1 
ATOM   2773 C CE2 . PHE A 1 347 ? 40.848 107.022 43.504  1.00 27.92 ? 347  PHE A CE2 1 
ATOM   2774 C CZ  . PHE A 1 347 ? 42.266 106.975 43.612  1.00 27.86 ? 347  PHE A CZ  1 
ATOM   2775 N N   . PRO A 1 348 ? 39.923 111.856 47.319  1.00 27.41 ? 348  PRO A N   1 
ATOM   2776 C CA  . PRO A 1 348 ? 40.187 113.209 46.807  1.00 27.19 ? 348  PRO A CA  1 
ATOM   2777 C C   . PRO A 1 348 ? 41.299 113.949 47.565  1.00 27.61 ? 348  PRO A C   1 
ATOM   2778 O O   . PRO A 1 348 ? 42.112 114.656 46.953  1.00 28.70 ? 348  PRO A O   1 
ATOM   2779 C CB  . PRO A 1 348 ? 38.836 113.913 46.975  1.00 27.34 ? 348  PRO A CB  1 
ATOM   2780 C CG  . PRO A 1 348 ? 37.848 112.796 46.963  1.00 25.08 ? 348  PRO A CG  1 
ATOM   2781 C CD  . PRO A 1 348 ? 38.512 111.737 47.747  1.00 27.44 ? 348  PRO A CD  1 
ATOM   2782 N N   . GLU A 1 349 ? 41.365 113.754 48.867  1.00 27.53 ? 349  GLU A N   1 
ATOM   2783 C CA  A GLU A 1 349 ? 42.404 114.369 49.690  0.50 27.77 ? 349  GLU A CA  1 
ATOM   2784 C CA  B GLU A 1 349 ? 42.407 114.372 49.667  0.50 27.98 ? 349  GLU A CA  1 
ATOM   2785 C C   . GLU A 1 349 ? 43.792 113.778 49.353  1.00 27.74 ? 349  GLU A C   1 
ATOM   2786 O O   . GLU A 1 349 ? 44.808 114.507 49.323  1.00 27.76 ? 349  GLU A O   1 
ATOM   2787 C CB  A GLU A 1 349 ? 42.076 114.210 51.186  0.50 27.82 ? 349  GLU A CB  1 
ATOM   2788 C CB  B GLU A 1 349 ? 42.056 114.255 51.152  0.50 28.12 ? 349  GLU A CB  1 
ATOM   2789 C CG  A GLU A 1 349 ? 40.767 114.892 51.677  0.50 28.54 ? 349  GLU A CG  1 
ATOM   2790 C CG  B GLU A 1 349 ? 42.917 115.076 52.082  0.50 30.01 ? 349  GLU A CG  1 
ATOM   2791 C CD  A GLU A 1 349 ? 39.563 113.936 51.830  0.50 30.60 ? 349  GLU A CD  1 
ATOM   2792 C CD  B GLU A 1 349 ? 43.565 116.241 51.396  0.50 32.54 ? 349  GLU A CD  1 
ATOM   2793 O OE1 A GLU A 1 349 ? 39.126 113.319 50.816  0.50 25.93 ? 349  GLU A OE1 1 
ATOM   2794 O OE1 B GLU A 1 349 ? 42.847 117.132 50.899  0.50 35.46 ? 349  GLU A OE1 1 
ATOM   2795 O OE2 A GLU A 1 349 ? 39.040 113.831 52.980  0.50 29.89 ? 349  GLU A OE2 1 
ATOM   2796 O OE2 B GLU A 1 349 ? 44.810 116.264 51.343  0.50 33.77 ? 349  GLU A OE2 1 
ATOM   2797 N N   . PHE A 1 350 ? 43.844 112.466 49.111  1.00 27.38 ? 350  PHE A N   1 
ATOM   2798 C CA  . PHE A 1 350 ? 45.091 111.775 48.675  1.00 27.03 ? 350  PHE A CA  1 
ATOM   2799 C C   . PHE A 1 350 ? 45.588 112.306 47.318  1.00 26.20 ? 350  PHE A C   1 
ATOM   2800 O O   . PHE A 1 350 ? 46.793 112.495 47.109  1.00 25.23 ? 350  PHE A O   1 
ATOM   2801 C CB  . PHE A 1 350 ? 44.879 110.250 48.610  1.00 28.06 ? 350  PHE A CB  1 
ATOM   2802 C CG  . PHE A 1 350 ? 45.974 109.497 47.861  1.00 29.15 ? 350  PHE A CG  1 
ATOM   2803 C CD1 . PHE A 1 350 ? 47.168 109.176 48.478  1.00 30.19 ? 350  PHE A CD1 1 
ATOM   2804 C CD2 . PHE A 1 350 ? 45.799 109.128 46.529  1.00 30.43 ? 350  PHE A CD2 1 
ATOM   2805 C CE1 . PHE A 1 350 ? 48.181 108.466 47.788  1.00 30.18 ? 350  PHE A CE1 1 
ATOM   2806 C CE2 . PHE A 1 350 ? 46.792 108.436 45.845  1.00 29.35 ? 350  PHE A CE2 1 
ATOM   2807 C CZ  . PHE A 1 350 ? 47.984 108.097 46.491  1.00 29.49 ? 350  PHE A CZ  1 
ATOM   2808 N N   . VAL A 1 351 ? 44.651 112.579 46.408  1.00 26.19 ? 351  VAL A N   1 
ATOM   2809 C CA  . VAL A 1 351 ? 45.002 113.133 45.100  1.00 25.28 ? 351  VAL A CA  1 
ATOM   2810 C C   . VAL A 1 351 ? 45.625 114.527 45.236  1.00 24.46 ? 351  VAL A C   1 
ATOM   2811 O O   . VAL A 1 351 ? 46.598 114.841 44.543  1.00 22.70 ? 351  VAL A O   1 
ATOM   2812 C CB  . VAL A 1 351 ? 43.821 113.134 44.142  1.00 26.62 ? 351  VAL A CB  1 
ATOM   2813 C CG1 . VAL A 1 351 ? 44.214 113.779 42.816  1.00 27.24 ? 351  VAL A CG1 1 
ATOM   2814 C CG2 . VAL A 1 351 ? 43.327 111.675 43.900  1.00 26.27 ? 351  VAL A CG2 1 
ATOM   2815 N N   . ASN A 1 352 ? 45.081 115.348 46.150  1.00 23.07 ? 352  ASN A N   1 
ATOM   2816 C CA  . ASN A 1 352 ? 45.653 116.658 46.450  1.00 21.75 ? 352  ASN A CA  1 
ATOM   2817 C C   . ASN A 1 352 ? 47.089 116.482 46.921  1.00 21.57 ? 352  ASN A C   1 
ATOM   2818 O O   . ASN A 1 352 ? 47.969 117.203 46.464  1.00 21.49 ? 352  ASN A O   1 
ATOM   2819 C CB  . ASN A 1 352 ? 44.837 117.387 47.524  1.00 20.95 ? 352  ASN A CB  1 
ATOM   2820 C CG  . ASN A 1 352 ? 43.473 117.890 47.016  1.00 21.84 ? 352  ASN A CG  1 
ATOM   2821 O OD1 . ASN A 1 352 ? 43.175 117.859 45.816  1.00 23.21 ? 352  ASN A OD1 1 
ATOM   2822 N ND2 . ASN A 1 352 ? 42.672 118.408 47.932  1.00 20.01 ? 352  ASN A ND2 1 
ATOM   2823 N N   . GLU A 1 353 ? 47.300 115.541 47.837  1.00 21.39 ? 353  GLU A N   1 
ATOM   2824 C CA  A GLU A 1 353 ? 48.640 115.199 48.356  0.50 22.58 ? 353  GLU A CA  1 
ATOM   2825 C CA  B GLU A 1 353 ? 48.644 115.222 48.348  0.50 22.61 ? 353  GLU A CA  1 
ATOM   2826 C C   . GLU A 1 353 ? 49.600 114.811 47.222  1.00 22.13 ? 353  GLU A C   1 
ATOM   2827 O O   . GLU A 1 353 ? 50.746 115.282 47.176  1.00 22.98 ? 353  GLU A O   1 
ATOM   2828 C CB  A GLU A 1 353 ? 48.561 114.066 49.411  0.50 22.11 ? 353  GLU A CB  1 
ATOM   2829 C CB  B GLU A 1 353 ? 48.593 114.140 49.450  0.50 22.13 ? 353  GLU A CB  1 
ATOM   2830 C CG  A GLU A 1 353 ? 47.758 114.408 50.681  0.50 23.57 ? 353  GLU A CG  1 
ATOM   2831 C CG  B GLU A 1 353 ? 49.964 113.768 50.000  0.50 23.25 ? 353  GLU A CG  1 
ATOM   2832 C CD  A GLU A 1 353 ? 47.393 113.183 51.539  0.50 24.30 ? 353  GLU A CD  1 
ATOM   2833 C CD  B GLU A 1 353 ? 49.923 112.877 51.237  0.50 24.72 ? 353  GLU A CD  1 
ATOM   2834 O OE1 A GLU A 1 353 ? 46.681 113.370 52.548  0.50 27.66 ? 353  GLU A OE1 1 
ATOM   2835 O OE1 B GLU A 1 353 ? 49.505 113.375 52.308  0.50 26.90 ? 353  GLU A OE1 1 
ATOM   2836 O OE2 A GLU A 1 353 ? 47.793 112.042 51.210  0.50 24.94 ? 353  GLU A OE2 1 
ATOM   2837 O OE2 B GLU A 1 353 ? 50.351 111.696 51.148  0.50 27.17 ? 353  GLU A OE2 1 
ATOM   2838 N N   . LEU A 1 354 ? 49.131 113.949 46.325  1.00 21.72 ? 354  LEU A N   1 
ATOM   2839 C CA  . LEU A 1 354 ? 49.893 113.519 45.137  1.00 22.20 ? 354  LEU A CA  1 
ATOM   2840 C C   . LEU A 1 354 ? 50.327 114.694 44.294  1.00 21.98 ? 354  LEU A C   1 
ATOM   2841 O O   . LEU A 1 354 ? 51.504 114.819 43.939  1.00 21.70 ? 354  LEU A O   1 
ATOM   2842 C CB  . LEU A 1 354 ? 49.071 112.610 44.220  1.00 21.89 ? 354  LEU A CB  1 
ATOM   2843 C CG  . LEU A 1 354 ? 49.239 111.095 44.271  1.00 24.47 ? 354  LEU A CG  1 
ATOM   2844 C CD1 . LEU A 1 354 ? 48.431 110.557 43.118  1.00 24.32 ? 354  LEU A CD1 1 
ATOM   2845 C CD2 . LEU A 1 354 ? 50.681 110.606 44.170  1.00 22.12 ? 354  LEU A CD2 1 
ATOM   2846 N N   . HIS A 1 355 ? 49.363 115.539 43.963  1.00 21.98 ? 355  HIS A N   1 
ATOM   2847 C CA  . HIS A 1 355 ? 49.588 116.723 43.159  1.00 23.21 ? 355  HIS A CA  1 
ATOM   2848 C C   . HIS A 1 355 ? 50.556 117.703 43.800  1.00 23.99 ? 355  HIS A C   1 
ATOM   2849 O O   . HIS A 1 355 ? 51.440 118.236 43.116  1.00 24.50 ? 355  HIS A O   1 
ATOM   2850 C CB  . HIS A 1 355 ? 48.236 117.382 42.846  1.00 24.11 ? 355  HIS A CB  1 
ATOM   2851 C CG  . HIS A 1 355 ? 47.420 116.603 41.852  1.00 25.45 ? 355  HIS A CG  1 
ATOM   2852 N ND1 . HIS A 1 355 ? 46.070 116.810 41.652  1.00 26.47 ? 355  HIS A ND1 1 
ATOM   2853 C CD2 . HIS A 1 355 ? 47.780 115.623 40.989  1.00 25.26 ? 355  HIS A CD2 1 
ATOM   2854 C CE1 . HIS A 1 355 ? 45.631 115.981 40.721  1.00 26.44 ? 355  HIS A CE1 1 
ATOM   2855 N NE2 . HIS A 1 355 ? 46.651 115.253 40.295  1.00 26.10 ? 355  HIS A NE2 1 
ATOM   2856 N N   . ASN A 1 356 ? 50.376 117.935 45.103  1.00 23.26 ? 356  ASN A N   1 
ATOM   2857 C CA  A ASN A 1 356 ? 51.241 118.819 45.883  0.50 24.15 ? 356  ASN A CA  1 
ATOM   2858 C CA  B ASN A 1 356 ? 51.255 118.815 45.861  0.50 23.43 ? 356  ASN A CA  1 
ATOM   2859 C C   . ASN A 1 356 ? 52.687 118.299 45.961  1.00 23.98 ? 356  ASN A C   1 
ATOM   2860 O O   . ASN A 1 356 ? 53.613 119.073 46.119  1.00 24.89 ? 356  ASN A O   1 
ATOM   2861 C CB  A ASN A 1 356 ? 50.677 119.008 47.298  0.50 23.58 ? 356  ASN A CB  1 
ATOM   2862 C CB  B ASN A 1 356 ? 50.680 119.044 47.251  0.50 22.20 ? 356  ASN A CB  1 
ATOM   2863 C CG  A ASN A 1 356 ? 51.328 120.167 48.037  0.50 24.42 ? 356  ASN A CG  1 
ATOM   2864 C CG  B ASN A 1 356 ? 49.529 119.994 47.229  0.50 20.08 ? 356  ASN A CG  1 
ATOM   2865 O OD1 A ASN A 1 356 ? 51.151 121.329 47.666  0.50 25.38 ? 356  ASN A OD1 1 
ATOM   2866 O OD1 B ASN A 1 356 ? 49.319 120.705 46.248  0.50 16.52 ? 356  ASN A OD1 1 
ATOM   2867 N ND2 A ASN A 1 356 ? 52.078 119.858 49.097  0.50 23.63 ? 356  ASN A ND2 1 
ATOM   2868 N ND2 B ASN A 1 356 ? 48.777 120.027 48.307  0.50 16.39 ? 356  ASN A ND2 1 
ATOM   2869 N N   . ASN A 1 357 ? 52.858 116.981 45.868  1.00 24.50 ? 357  ASN A N   1 
ATOM   2870 C CA  . ASN A 1 357 ? 54.180 116.354 45.781  1.00 25.02 ? 357  ASN A CA  1 
ATOM   2871 C C   . ASN A 1 357 ? 54.754 116.298 44.337  1.00 24.61 ? 357  ASN A C   1 
ATOM   2872 O O   . ASN A 1 357 ? 55.767 115.642 44.082  1.00 25.93 ? 357  ASN A O   1 
ATOM   2873 C CB  . ASN A 1 357 ? 54.131 114.964 46.409  1.00 25.27 ? 357  ASN A CB  1 
ATOM   2874 C CG  . ASN A 1 357 ? 53.907 115.007 47.944  1.00 28.41 ? 357  ASN A CG  1 
ATOM   2875 O OD1 . ASN A 1 357 ? 53.175 114.207 48.491  1.00 32.39 ? 357  ASN A OD1 1 
ATOM   2876 N ND2 . ASN A 1 357 ? 54.556 115.926 48.616  1.00 29.43 ? 357  ASN A ND2 1 
ATOM   2877 N N   . GLY A 1 358 ? 54.115 116.984 43.398  1.00 24.04 ? 358  GLY A N   1 
ATOM   2878 C CA  . GLY A 1 358 ? 54.536 116.992 41.997  1.00 22.89 ? 358  GLY A CA  1 
ATOM   2879 C C   . GLY A 1 358 ? 54.261 115.710 41.209  1.00 23.05 ? 358  GLY A C   1 
ATOM   2880 O O   . GLY A 1 358 ? 54.821 115.500 40.121  1.00 24.07 ? 358  GLY A O   1 
ATOM   2881 N N   . GLN A 1 359 ? 53.430 114.832 41.750  1.00 21.40 ? 359  GLN A N   1 
ATOM   2882 C CA  . GLN A 1 359 ? 53.131 113.575 41.085  1.00 20.82 ? 359  GLN A CA  1 
ATOM   2883 C C   . GLN A 1 359 ? 51.800 113.617 40.328  1.00 20.12 ? 359  GLN A C   1 
ATOM   2884 O O   . GLN A 1 359 ? 51.090 114.611 40.384  1.00 18.55 ? 359  GLN A O   1 
ATOM   2885 C CB  . GLN A 1 359 ? 53.140 112.478 42.105  1.00 20.99 ? 359  GLN A CB  1 
ATOM   2886 C CG  . GLN A 1 359 ? 54.528 112.200 42.562  1.00 23.64 ? 359  GLN A CG  1 
ATOM   2887 C CD  . GLN A 1 359 ? 54.532 111.221 43.677  1.00 25.05 ? 359  GLN A CD  1 
ATOM   2888 O OE1 . GLN A 1 359 ? 53.831 111.415 44.681  1.00 23.42 ? 359  GLN A OE1 1 
ATOM   2889 N NE2 . GLN A 1 359 ? 55.318 110.148 43.526  1.00 22.98 ? 359  GLN A NE2 1 
ATOM   2890 N N   . LYS A 1 360 ? 51.499 112.550 39.583  1.00 20.44 ? 360  LYS A N   1 
ATOM   2891 C CA  . LYS A 1 360 ? 50.266 112.480 38.791  1.00 20.40 ? 360  LYS A CA  1 
ATOM   2892 C C   . LYS A 1 360 ? 49.501 111.202 39.068  1.00 19.71 ? 360  LYS A C   1 
ATOM   2893 O O   . LYS A 1 360 ? 50.093 110.214 39.488  1.00 20.15 ? 360  LYS A O   1 
ATOM   2894 C CB  . LYS A 1 360 ? 50.584 112.627 37.282  1.00 21.32 ? 360  LYS A CB  1 
ATOM   2895 C CG  . LYS A 1 360 ? 51.296 113.981 36.889  1.00 20.68 ? 360  LYS A CG  1 
ATOM   2896 C CD  . LYS A 1 360 ? 50.295 115.154 36.762  1.00 23.87 ? 360  LYS A CD  1 
ATOM   2897 C CE  . LYS A 1 360 ? 50.884 116.370 36.028  1.00 23.90 ? 360  LYS A CE  1 
ATOM   2898 N NZ  . LYS A 1 360 ? 49.914 117.554 35.966  1.00 23.07 ? 360  LYS A NZ  1 
ATOM   2899 N N   . LEU A 1 361 ? 48.192 111.218 38.827  1.00 18.69 ? 361  LEU A N   1 
ATOM   2900 C CA  . LEU A 1 361 ? 47.343 110.056 39.041  1.00 19.06 ? 361  LEU A CA  1 
ATOM   2901 C C   . LEU A 1 361 ? 46.770 109.586 37.716  1.00 18.78 ? 361  LEU A C   1 
ATOM   2902 O O   . LEU A 1 361 ? 46.121 110.357 37.016  1.00 19.32 ? 361  LEU A O   1 
ATOM   2903 C CB  . LEU A 1 361 ? 46.147 110.377 39.970  1.00 19.22 ? 361  LEU A CB  1 
ATOM   2904 C CG  . LEU A 1 361 ? 45.185 109.188 40.178  1.00 19.05 ? 361  LEU A CG  1 
ATOM   2905 C CD1 . LEU A 1 361 ? 45.872 108.067 40.996  1.00 21.60 ? 361  LEU A CD1 1 
ATOM   2906 C CD2 . LEU A 1 361 ? 43.860 109.622 40.784  1.00 19.99 ? 361  LEU A CD2 1 
ATOM   2907 N N   . VAL A 1 362 ? 46.968 108.312 37.407  1.00 18.77 ? 362  VAL A N   1 
ATOM   2908 C CA  . VAL A 1 362 ? 46.349 107.700 36.242  1.00 18.74 ? 362  VAL A CA  1 
ATOM   2909 C C   . VAL A 1 362 ? 45.374 106.634 36.790  1.00 19.00 ? 362  VAL A C   1 
ATOM   2910 O O   . VAL A 1 362 ? 45.736 105.799 37.640  1.00 20.09 ? 362  VAL A O   1 
ATOM   2911 C CB  . VAL A 1 362 ? 47.386 107.053 35.251  1.00 19.45 ? 362  VAL A CB  1 
ATOM   2912 C CG1 . VAL A 1 362 ? 46.651 106.331 34.086  1.00 17.18 ? 362  VAL A CG1 1 
ATOM   2913 C CG2 . VAL A 1 362 ? 48.371 108.093 34.696  1.00 16.59 ? 362  VAL A CG2 1 
ATOM   2914 N N   . ILE A 1 363 ? 44.140 106.681 36.321  1.00 18.91 ? 363  ILE A N   1 
ATOM   2915 C CA  . ILE A 1 363 ? 43.125 105.713 36.750  1.00 19.44 ? 363  ILE A CA  1 
ATOM   2916 C C   . ILE A 1 363 ? 42.785 104.735 35.638  1.00 20.13 ? 363  ILE A C   1 
ATOM   2917 O O   . ILE A 1 363 ? 42.758 105.111 34.456  1.00 19.48 ? 363  ILE A O   1 
ATOM   2918 C CB  . ILE A 1 363 ? 41.787 106.417 37.185  1.00 20.44 ? 363  ILE A CB  1 
ATOM   2919 C CG1 . ILE A 1 363 ? 41.297 107.410 36.100  1.00 19.86 ? 363  ILE A CG1 1 
ATOM   2920 C CG2 . ILE A 1 363 ? 41.996 107.063 38.566  1.00 18.60 ? 363  ILE A CG2 1 
ATOM   2921 C CD1 . ILE A 1 363 ? 39.737 107.667 36.080  1.00 19.52 ? 363  ILE A CD1 1 
ATOM   2922 N N   . ILE A 1 364 ? 42.555 103.475 36.017  1.00 20.35 ? 364  ILE A N   1 
ATOM   2923 C CA  . ILE A 1 364 ? 42.055 102.494 35.081  1.00 20.53 ? 364  ILE A CA  1 
ATOM   2924 C C   . ILE A 1 364 ? 40.545 102.737 34.835  1.00 21.91 ? 364  ILE A C   1 
ATOM   2925 O O   . ILE A 1 364 ? 39.790 103.136 35.765  1.00 21.30 ? 364  ILE A O   1 
ATOM   2926 C CB  . ILE A 1 364 ? 42.318 101.069 35.557  1.00 20.05 ? 364  ILE A CB  1 
ATOM   2927 C CG1 . ILE A 1 364 ? 42.315 100.118 34.346  1.00 20.46 ? 364  ILE A CG1 1 
ATOM   2928 C CG2 . ILE A 1 364 ? 41.246 100.637 36.591  1.00 20.83 ? 364  ILE A CG2 1 
ATOM   2929 C CD1 . ILE A 1 364 ? 42.882 98.745  34.628  1.00 17.70 ? 364  ILE A CD1 1 
ATOM   2930 N N   . VAL A 1 365 ? 40.135 102.518 33.582  1.00 22.11 ? 365  VAL A N   1 
ATOM   2931 C CA  . VAL A 1 365 ? 38.750 102.585 33.158  1.00 23.36 ? 365  VAL A CA  1 
ATOM   2932 C C   . VAL A 1 365 ? 38.597 101.422 32.182  1.00 23.90 ? 365  VAL A C   1 
ATOM   2933 O O   . VAL A 1 365 ? 39.393 101.244 31.248  1.00 23.89 ? 365  VAL A O   1 
ATOM   2934 C CB  . VAL A 1 365 ? 38.361 103.966 32.518  1.00 23.44 ? 365  VAL A CB  1 
ATOM   2935 C CG1 . VAL A 1 365 ? 36.883 104.046 32.269  1.00 24.40 ? 365  VAL A CG1 1 
ATOM   2936 C CG2 . VAL A 1 365 ? 38.703 105.104 33.462  1.00 23.38 ? 365  VAL A CG2 1 
ATOM   2937 N N   . ASP A 1 366 ? 37.613 100.580 32.464  1.00 23.29 ? 366  ASP A N   1 
ATOM   2938 C CA  . ASP A 1 366 ? 37.317 99.445  31.628  1.00 22.89 ? 366  ASP A CA  1 
ATOM   2939 C C   . ASP A 1 366 ? 36.167 99.871  30.710  1.00 22.51 ? 366  ASP A C   1 
ATOM   2940 O O   . ASP A 1 366 ? 35.452 100.787 31.037  1.00 21.60 ? 366  ASP A O   1 
ATOM   2941 C CB  . ASP A 1 366 ? 36.895 98.279  32.507  1.00 22.76 ? 366  ASP A CB  1 
ATOM   2942 C CG  . ASP A 1 366 ? 37.984 97.815  33.423  1.00 23.75 ? 366  ASP A CG  1 
ATOM   2943 O OD1 . ASP A 1 366 ? 39.131 97.501  32.965  1.00 20.29 ? 366  ASP A OD1 1 
ATOM   2944 O OD2 . ASP A 1 366 ? 37.652 97.730  34.630  1.00 27.15 ? 366  ASP A OD2 1 
ATOM   2945 N N   . PRO A 1 367 ? 36.030 99.243  29.535  1.00 23.05 ? 367  PRO A N   1 
ATOM   2946 C CA  . PRO A 1 367 ? 34.884 99.587  28.689  1.00 23.26 ? 367  PRO A CA  1 
ATOM   2947 C C   . PRO A 1 367 ? 33.531 99.070  29.214  1.00 24.38 ? 367  PRO A C   1 
ATOM   2948 O O   . PRO A 1 367 ? 32.496 99.720  29.011  1.00 24.60 ? 367  PRO A O   1 
ATOM   2949 C CB  . PRO A 1 367 ? 35.213 98.919  27.351  1.00 23.39 ? 367  PRO A CB  1 
ATOM   2950 C CG  . PRO A 1 367 ? 36.191 97.816  27.681  1.00 22.66 ? 367  PRO A CG  1 
ATOM   2951 C CD  . PRO A 1 367 ? 36.926 98.238  28.921  1.00 21.85 ? 367  PRO A CD  1 
ATOM   2952 N N   . ALA A 1 368 ? 33.523 97.904  29.849  1.00 25.11 ? 368  ALA A N   1 
ATOM   2953 C CA  . ALA A 1 368 ? 32.252 97.237  30.124  1.00 25.52 ? 368  ALA A CA  1 
ATOM   2954 C C   . ALA A 1 368 ? 31.559 97.873  31.333  1.00 25.72 ? 368  ALA A C   1 
ATOM   2955 O O   . ALA A 1 368 ? 32.188 98.089  32.373  1.00 25.77 ? 368  ALA A O   1 
ATOM   2956 C CB  . ALA A 1 368 ? 32.446 95.766  30.316  1.00 25.34 ? 368  ALA A CB  1 
ATOM   2957 N N   . ILE A 1 369 ? 30.278 98.184  31.150  1.00 24.90 ? 369  ILE A N   1 
ATOM   2958 C CA  . ILE A 1 369 ? 29.439 98.889  32.126  1.00 25.38 ? 369  ILE A CA  1 
ATOM   2959 C C   . ILE A 1 369 ? 28.389 97.939  32.752  1.00 25.31 ? 369  ILE A C   1 
ATOM   2960 O O   . ILE A 1 369 ? 27.596 97.318  32.049  1.00 25.88 ? 369  ILE A O   1 
ATOM   2961 C CB  . ILE A 1 369 ? 28.735 100.157 31.476  1.00 24.81 ? 369  ILE A CB  1 
ATOM   2962 C CG1 . ILE A 1 369 ? 29.769 101.123 30.843  1.00 24.93 ? 369  ILE A CG1 1 
ATOM   2963 C CG2 . ILE A 1 369 ? 27.818 100.881 32.481  1.00 26.42 ? 369  ILE A CG2 1 
ATOM   2964 C CD1 . ILE A 1 369 ? 30.769 101.801 31.810  1.00 24.43 ? 369  ILE A CD1 1 
ATOM   2965 N N   . SER A 1 370 ? 28.421 97.820  34.077  1.00 26.05 ? 370  SER A N   1 
ATOM   2966 C CA  . SER A 1 370 ? 27.419 97.099  34.848  1.00 26.33 ? 370  SER A CA  1 
ATOM   2967 C C   . SER A 1 370 ? 26.009 97.517  34.432  1.00 27.67 ? 370  SER A C   1 
ATOM   2968 O O   . SER A 1 370 ? 25.691 98.714  34.414  1.00 26.82 ? 370  SER A O   1 
ATOM   2969 C CB  . SER A 1 370 ? 27.586 97.432  36.328  1.00 26.15 ? 370  SER A CB  1 
ATOM   2970 O OG  . SER A 1 370 ? 26.643 96.707  37.111  1.00 25.24 ? 370  SER A OG  1 
ATOM   2971 N N   . ASN A 1 371 ? 25.169 96.532  34.101  1.00 29.69 ? 371  ASN A N   1 
ATOM   2972 C CA  . ASN A 1 371 ? 23.738 96.791  33.789  1.00 31.40 ? 371  ASN A CA  1 
ATOM   2973 C C   . ASN A 1 371 ? 22.846 96.648  35.030  1.00 33.50 ? 371  ASN A C   1 
ATOM   2974 O O   . ASN A 1 371 ? 21.612 96.513  34.919  1.00 33.53 ? 371  ASN A O   1 
ATOM   2975 C CB  . ASN A 1 371 ? 23.238 95.872  32.667  1.00 30.15 ? 371  ASN A CB  1 
ATOM   2976 C CG  . ASN A 1 371 ? 23.206 94.402  33.063  1.00 29.70 ? 371  ASN A CG  1 
ATOM   2977 O OD1 . ASN A 1 371 ? 23.719 94.001  34.113  1.00 26.97 ? 371  ASN A OD1 1 
ATOM   2978 N ND2 . ASN A 1 371 ? 22.590 93.579  32.206  1.00 27.69 ? 371  ASN A ND2 1 
ATOM   2979 N N   . ASN A 1 372 ? 23.483 96.646  36.201  1.00 34.97 ? 372  ASN A N   1 
ATOM   2980 C CA  . ASN A 1 372 ? 22.773 96.502  37.458  1.00 37.34 ? 372  ASN A CA  1 
ATOM   2981 C C   . ASN A 1 372 ? 22.349 97.865  38.003  1.00 37.77 ? 372  ASN A C   1 
ATOM   2982 O O   . ASN A 1 372 ? 23.106 98.545  38.683  1.00 37.47 ? 372  ASN A O   1 
ATOM   2983 C CB  . ASN A 1 372 ? 23.625 95.717  38.463  1.00 38.13 ? 372  ASN A CB  1 
ATOM   2984 C CG  . ASN A 1 372 ? 22.772 94.991  39.512  1.00 42.00 ? 372  ASN A CG  1 
ATOM   2985 O OD1 . ASN A 1 372 ? 22.118 95.624  40.356  1.00 43.20 ? 372  ASN A OD1 1 
ATOM   2986 N ND2 . ASN A 1 372 ? 22.787 93.655  39.466  1.00 44.44 ? 372  ASN A ND2 1 
ATOM   2987 N N   . SER A 1 373 ? 21.132 98.262  37.657  1.00 38.71 ? 373  SER A N   1 
ATOM   2988 C CA  . SER A 1 373 ? 20.585 99.553  38.043  1.00 40.26 ? 373  SER A CA  1 
ATOM   2989 C C   . SER A 1 373 ? 19.080 99.447  38.276  1.00 41.91 ? 373  SER A C   1 
ATOM   2990 O O   . SER A 1 373 ? 18.350 98.901  37.453  1.00 41.43 ? 373  SER A O   1 
ATOM   2991 C CB  . SER A 1 373 ? 20.843 100.601 36.958  1.00 39.67 ? 373  SER A CB  1 
ATOM   2992 O OG  . SER A 1 373 ? 20.561 101.900 37.435  1.00 38.78 ? 373  SER A OG  1 
ATOM   2993 N N   . SER A 1 374 ? 18.641 99.990  39.401  1.00 44.21 ? 374  SER A N   1 
ATOM   2994 C CA  . SER A 1 374 ? 17.221 100.080 39.753  1.00 46.25 ? 374  SER A CA  1 
ATOM   2995 C C   . SER A 1 374 ? 16.971 101.501 40.205  1.00 47.39 ? 374  SER A C   1 
ATOM   2996 O O   . SER A 1 374 ? 17.930 102.244 40.471  1.00 47.85 ? 374  SER A O   1 
ATOM   2997 C CB  . SER A 1 374 ? 16.889 99.096  40.888  1.00 46.29 ? 374  SER A CB  1 
ATOM   2998 O OG  . SER A 1 374 ? 17.846 99.173  41.943  1.00 46.51 ? 374  SER A OG  1 
ATOM   2999 N N   . SER A 1 375 ? 15.698 101.886 40.305  1.00 48.69 ? 375  SER A N   1 
ATOM   3000 C CA  . SER A 1 375 ? 15.322 103.223 40.813  1.00 49.53 ? 375  SER A CA  1 
ATOM   3001 C C   . SER A 1 375 ? 15.722 103.396 42.274  1.00 49.51 ? 375  SER A C   1 
ATOM   3002 O O   . SER A 1 375 ? 16.103 104.496 42.695  1.00 49.73 ? 375  SER A O   1 
ATOM   3003 C CB  . SER A 1 375 ? 13.821 103.457 40.644  1.00 50.26 ? 375  SER A CB  1 
ATOM   3004 O OG  . SER A 1 375 ? 13.398 102.982 39.367  1.00 52.38 ? 375  SER A OG  1 
ATOM   3005 N N   . SER A 1 376 ? 15.649 102.298 43.030  1.00 49.41 ? 376  SER A N   1 
ATOM   3006 C CA  . SER A 1 376 ? 16.093 102.266 44.419  1.00 49.40 ? 376  SER A CA  1 
ATOM   3007 C C   . SER A 1 376 ? 17.576 102.585 44.465  1.00 48.72 ? 376  SER A C   1 
ATOM   3008 O O   . SER A 1 376 ? 17.960 103.566 45.088  1.00 49.01 ? 376  SER A O   1 
ATOM   3009 C CB  . SER A 1 376 ? 15.827 100.897 45.081  1.00 49.70 ? 376  SER A CB  1 
ATOM   3010 O OG  . SER A 1 376 ? 14.780 100.172 44.439  1.00 51.17 ? 376  SER A OG  1 
ATOM   3011 N N   . LYS A 1 377 ? 18.393 101.765 43.784  1.00 47.82 ? 377  LYS A N   1 
ATOM   3012 C CA  . LYS A 1 377 ? 19.862 101.935 43.744  1.00 46.66 ? 377  LYS A CA  1 
ATOM   3013 C C   . LYS A 1 377 ? 20.356 102.216 42.296  1.00 44.58 ? 377  LYS A C   1 
ATOM   3014 O O   . LYS A 1 377 ? 20.608 101.286 41.516  1.00 43.76 ? 377  LYS A O   1 
ATOM   3015 C CB  . LYS A 1 377 ? 20.595 100.733 44.375  1.00 47.49 ? 377  LYS A CB  1 
ATOM   3016 C CG  . LYS A 1 377 ? 19.845 100.032 45.534  1.00 50.29 ? 377  LYS A CG  1 
ATOM   3017 C CD  . LYS A 1 377 ? 20.780 99.574  46.676  1.00 55.06 ? 377  LYS A CD  1 
ATOM   3018 C CE  . LYS A 1 377 ? 21.887 98.596  46.234  1.00 57.77 ? 377  LYS A CE  1 
ATOM   3019 N NZ  . LYS A 1 377 ? 21.375 97.332  45.595  1.00 59.16 ? 377  LYS A NZ  1 
ATOM   3020 N N   . PRO A 1 378 ? 20.448 103.509 41.927  1.00 42.48 ? 378  PRO A N   1 
ATOM   3021 C CA  . PRO A 1 378 ? 20.815 103.948 40.579  1.00 40.96 ? 378  PRO A CA  1 
ATOM   3022 C C   . PRO A 1 378 ? 22.317 103.770 40.287  1.00 39.21 ? 378  PRO A C   1 
ATOM   3023 O O   . PRO A 1 378 ? 23.147 103.984 41.182  1.00 39.21 ? 378  PRO A O   1 
ATOM   3024 C CB  . PRO A 1 378 ? 20.456 105.448 40.585  1.00 41.36 ? 378  PRO A CB  1 
ATOM   3025 C CG  . PRO A 1 378 ? 19.698 105.683 41.861  1.00 42.11 ? 378  PRO A CG  1 
ATOM   3026 C CD  . PRO A 1 378 ? 20.192 104.656 42.811  1.00 42.52 ? 378  PRO A CD  1 
ATOM   3027 N N   . TYR A 1 379 ? 22.643 103.343 39.064  1.00 36.56 ? 379  TYR A N   1 
ATOM   3028 C CA  . TYR A 1 379 ? 24.030 103.358 38.562  1.00 34.00 ? 379  TYR A CA  1 
ATOM   3029 C C   . TYR A 1 379 ? 24.092 104.264 37.330  1.00 32.38 ? 379  TYR A C   1 
ATOM   3030 O O   . TYR A 1 379 ? 23.715 103.867 36.209  1.00 32.70 ? 379  TYR A O   1 
ATOM   3031 C CB  . TYR A 1 379 ? 24.561 101.940 38.283  1.00 32.88 ? 379  TYR A CB  1 
ATOM   3032 C CG  . TYR A 1 379 ? 25.997 101.905 37.785  1.00 32.78 ? 379  TYR A CG  1 
ATOM   3033 C CD1 . TYR A 1 379 ? 27.039 102.504 38.520  1.00 30.97 ? 379  TYR A CD1 1 
ATOM   3034 C CD2 . TYR A 1 379 ? 26.320 101.264 36.576  1.00 31.38 ? 379  TYR A CD2 1 
ATOM   3035 C CE1 . TYR A 1 379 ? 28.353 102.478 38.047  1.00 31.47 ? 379  TYR A CE1 1 
ATOM   3036 C CE2 . TYR A 1 379 ? 27.624 101.216 36.102  1.00 30.09 ? 379  TYR A CE2 1 
ATOM   3037 C CZ  . TYR A 1 379 ? 28.640 101.822 36.834  1.00 31.61 ? 379  TYR A CZ  1 
ATOM   3038 O OH  . TYR A 1 379 ? 29.928 101.778 36.351  1.00 29.92 ? 379  TYR A OH  1 
ATOM   3039 N N   . GLY A 1 380 ? 24.544 105.492 37.568  1.00 30.45 ? 380  GLY A N   1 
ATOM   3040 C CA  . GLY A 1 380 ? 24.478 106.570 36.595  1.00 28.49 ? 380  GLY A CA  1 
ATOM   3041 C C   . GLY A 1 380 ? 25.056 106.298 35.219  1.00 27.50 ? 380  GLY A C   1 
ATOM   3042 O O   . GLY A 1 380 ? 24.399 106.610 34.244  1.00 27.67 ? 380  GLY A O   1 
ATOM   3043 N N   . PRO A 1 381 ? 26.308 105.749 35.122  1.00 27.24 ? 381  PRO A N   1 
ATOM   3044 C CA  . PRO A 1 381 ? 26.869 105.475 33.773  1.00 26.78 ? 381  PRO A CA  1 
ATOM   3045 C C   . PRO A 1 381 ? 25.991 104.534 32.938  1.00 26.36 ? 381  PRO A C   1 
ATOM   3046 O O   . PRO A 1 381 ? 25.823 104.755 31.749  1.00 25.90 ? 381  PRO A O   1 
ATOM   3047 C CB  . PRO A 1 381 ? 28.235 104.834 34.077  1.00 25.84 ? 381  PRO A CB  1 
ATOM   3048 C CG  . PRO A 1 381 ? 28.587 105.311 35.433  1.00 26.61 ? 381  PRO A CG  1 
ATOM   3049 C CD  . PRO A 1 381 ? 27.274 105.381 36.181  1.00 26.10 ? 381  PRO A CD  1 
ATOM   3050 N N   . TYR A 1 382 ? 25.400 103.516 33.560  1.00 27.22 ? 382  TYR A N   1 
ATOM   3051 C CA  . TYR A 1 382 ? 24.452 102.684 32.835  1.00 27.51 ? 382  TYR A CA  1 
ATOM   3052 C C   . TYR A 1 382 ? 23.141 103.393 32.476  1.00 28.46 ? 382  TYR A C   1 
ATOM   3053 O O   . TYR A 1 382 ? 22.641 103.232 31.355  1.00 28.46 ? 382  TYR A O   1 
ATOM   3054 C CB  . TYR A 1 382 ? 24.182 101.398 33.586  1.00 28.20 ? 382  TYR A CB  1 
ATOM   3055 C CG  . TYR A 1 382 ? 23.193 100.514 32.876  1.00 28.71 ? 382  TYR A CG  1 
ATOM   3056 C CD1 . TYR A 1 382 ? 23.552 99.807  31.727  1.00 27.58 ? 382  TYR A CD1 1 
ATOM   3057 C CD2 . TYR A 1 382 ? 21.881 100.406 33.343  1.00 30.03 ? 382  TYR A CD2 1 
ATOM   3058 C CE1 . TYR A 1 382 ? 22.629 99.010  31.075  1.00 29.69 ? 382  TYR A CE1 1 
ATOM   3059 C CE2 . TYR A 1 382 ? 20.952 99.599  32.710  1.00 29.85 ? 382  TYR A CE2 1 
ATOM   3060 C CZ  . TYR A 1 382 ? 21.329 98.900  31.586  1.00 29.72 ? 382  TYR A CZ  1 
ATOM   3061 O OH  . TYR A 1 382 ? 20.387 98.107  30.967  1.00 30.36 ? 382  TYR A OH  1 
ATOM   3062 N N   . ASP A 1 383 ? 22.579 104.166 33.414  1.00 29.08 ? 383  ASP A N   1 
ATOM   3063 C CA  . ASP A 1 383 ? 21.328 104.883 33.126  1.00 30.28 ? 383  ASP A CA  1 
ATOM   3064 C C   . ASP A 1 383 ? 21.521 105.898 32.010  1.00 29.44 ? 383  ASP A C   1 
ATOM   3065 O O   . ASP A 1 383 ? 20.737 105.933 31.092  1.00 29.39 ? 383  ASP A O   1 
ATOM   3066 C CB  . ASP A 1 383 ? 20.748 105.572 34.379  1.00 30.77 ? 383  ASP A CB  1 
ATOM   3067 C CG  . ASP A 1 383 ? 20.391 104.583 35.488  1.00 34.07 ? 383  ASP A CG  1 
ATOM   3068 O OD1 . ASP A 1 383 ? 20.123 103.391 35.200  1.00 36.43 ? 383  ASP A OD1 1 
ATOM   3069 O OD2 . ASP A 1 383 ? 20.393 105.008 36.666  1.00 39.28 ? 383  ASP A OD2 1 
ATOM   3070 N N   . ARG A 1 384 ? 22.580 106.703 32.076  1.00 29.13 ? 384  ARG A N   1 
ATOM   3071 C CA  . ARG A 1 384 ? 22.852 107.680 31.033  1.00 29.06 ? 384  ARG A CA  1 
ATOM   3072 C C   . ARG A 1 384 ? 23.197 107.018 29.694  1.00 29.69 ? 384  ARG A C   1 
ATOM   3073 O O   . ARG A 1 384 ? 22.806 107.512 28.611  1.00 29.35 ? 384  ARG A O   1 
ATOM   3074 C CB  . ARG A 1 384 ? 23.959 108.642 31.474  1.00 29.23 ? 384  ARG A CB  1 
ATOM   3075 C CG  . ARG A 1 384 ? 23.509 109.611 32.570  1.00 29.45 ? 384  ARG A CG  1 
ATOM   3076 C CD  . ARG A 1 384 ? 24.627 110.585 33.013  1.00 29.80 ? 384  ARG A CD  1 
ATOM   3077 N NE  . ARG A 1 384 ? 25.719 109.891 33.688  1.00 31.42 ? 384  ARG A NE  1 
ATOM   3078 C CZ  . ARG A 1 384 ? 25.757 109.622 34.997  1.00 31.37 ? 384  ARG A CZ  1 
ATOM   3079 N NH1 . ARG A 1 384 ? 24.779 110.010 35.806  1.00 28.30 ? 384  ARG A NH1 1 
ATOM   3080 N NH2 . ARG A 1 384 ? 26.791 108.975 35.508  1.00 28.92 ? 384  ARG A NH2 1 
ATOM   3081 N N   . GLY A 1 385 ? 23.919 105.897 29.762  1.00 29.66 ? 385  GLY A N   1 
ATOM   3082 C CA  . GLY A 1 385 ? 24.241 105.129 28.559  1.00 30.13 ? 385  GLY A CA  1 
ATOM   3083 C C   . GLY A 1 385 ? 23.019 104.539 27.876  1.00 30.49 ? 385  GLY A C   1 
ATOM   3084 O O   . GLY A 1 385 ? 22.888 104.606 26.650  1.00 29.67 ? 385  GLY A O   1 
ATOM   3085 N N   . SER A 1 386 ? 22.119 103.961 28.666  1.00 31.08 ? 386  SER A N   1 
ATOM   3086 C CA  . SER A 1 386 ? 20.873 103.414 28.104  1.00 32.45 ? 386  SER A CA  1 
ATOM   3087 C C   . SER A 1 386 ? 19.942 104.500 27.557  1.00 33.30 ? 386  SER A C   1 
ATOM   3088 O O   . SER A 1 386 ? 19.222 104.256 26.593  1.00 33.49 ? 386  SER A O   1 
ATOM   3089 C CB  . SER A 1 386 ? 20.146 102.548 29.122  1.00 32.02 ? 386  SER A CB  1 
ATOM   3090 O OG  . SER A 1 386 ? 21.019 101.540 29.585  1.00 33.29 ? 386  SER A OG  1 
ATOM   3091 N N   . ASP A 1 387 ? 19.979 105.697 28.148  1.00 34.80 ? 387  ASP A N   1 
ATOM   3092 C CA  . ASP A 1 387 ? 19.204 106.833 27.631  1.00 36.71 ? 387  ASP A CA  1 
ATOM   3093 C C   . ASP A 1 387 ? 19.696 107.217 26.244  1.00 36.66 ? 387  ASP A C   1 
ATOM   3094 O O   . ASP A 1 387 ? 18.904 107.596 25.372  1.00 36.11 ? 387  ASP A O   1 
ATOM   3095 C CB  . ASP A 1 387 ? 19.324 108.056 28.539  1.00 37.24 ? 387  ASP A CB  1 
ATOM   3096 C CG  . ASP A 1 387 ? 18.630 107.868 29.857  1.00 42.87 ? 387  ASP A CG  1 
ATOM   3097 O OD1 . ASP A 1 387 ? 17.707 107.009 29.944  1.00 47.13 ? 387  ASP A OD1 1 
ATOM   3098 O OD2 . ASP A 1 387 ? 19.019 108.578 30.822  1.00 48.54 ? 387  ASP A OD2 1 
ATOM   3099 N N   . MET A 1 388 ? 21.013 107.126 26.057  1.00 36.23 ? 388  MET A N   1 
ATOM   3100 C CA  . MET A 1 388 ? 21.630 107.499 24.788  1.00 36.62 ? 388  MET A CA  1 
ATOM   3101 C C   . MET A 1 388 ? 21.612 106.386 23.713  1.00 35.24 ? 388  MET A C   1 
ATOM   3102 O O   . MET A 1 388 ? 21.868 106.646 22.543  1.00 35.53 ? 388  MET A O   1 
ATOM   3103 C CB  . MET A 1 388 ? 23.027 108.062 25.043  1.00 36.29 ? 388  MET A CB  1 
ATOM   3104 C CG  . MET A 1 388 ? 22.956 109.340 25.877  1.00 37.68 ? 388  MET A CG  1 
ATOM   3105 S SD  . MET A 1 388 ? 24.489 110.285 26.014  1.00 39.40 ? 388  MET A SD  1 
ATOM   3106 C CE  . MET A 1 388 ? 24.687 110.881 24.339  1.00 35.27 ? 388  MET A CE  1 
ATOM   3107 N N   . LYS A 1 389 ? 21.263 105.166 24.111  1.00 33.37 ? 389  LYS A N   1 
ATOM   3108 C CA  . LYS A 1 389 ? 21.214 104.038 23.195  1.00 32.45 ? 389  LYS A CA  1 
ATOM   3109 C C   . LYS A 1 389 ? 22.597 103.727 22.539  1.00 30.43 ? 389  LYS A C   1 
ATOM   3110 O O   . LYS A 1 389 ? 22.697 103.374 21.358  1.00 28.92 ? 389  LYS A O   1 
ATOM   3111 C CB  . LYS A 1 389 ? 20.050 104.205 22.195  1.00 32.95 ? 389  LYS A CB  1 
ATOM   3112 C CG  . LYS A 1 389 ? 18.667 103.951 22.890  1.00 33.93 ? 389  LYS A CG  1 
ATOM   3113 C CD  . LYS A 1 389 ? 17.471 104.500 22.120  1.00 35.17 ? 389  LYS A CD  1 
ATOM   3114 C CE  . LYS A 1 389 ? 16.245 104.650 23.064  1.00 39.21 ? 389  LYS A CE  1 
ATOM   3115 N NZ  . LYS A 1 389 ? 15.830 103.288 23.615  1.00 42.58 ? 389  LYS A NZ  1 
ATOM   3116 N N   . ILE A 1 390 ? 23.648 103.837 23.350  1.00 28.56 ? 390  ILE A N   1 
ATOM   3117 C CA  . ILE A 1 390 ? 25.019 103.738 22.838  1.00 27.07 ? 390  ILE A CA  1 
ATOM   3118 C C   . ILE A 1 390 ? 25.760 102.401 23.068  1.00 26.53 ? 390  ILE A C   1 
ATOM   3119 O O   . ILE A 1 390 ? 27.032 102.360 22.976  1.00 25.65 ? 390  ILE A O   1 
ATOM   3120 C CB  . ILE A 1 390 ? 25.887 104.964 23.268  1.00 26.37 ? 390  ILE A CB  1 
ATOM   3121 C CG1 . ILE A 1 390 ? 25.842 105.208 24.782  1.00 25.00 ? 390  ILE A CG1 1 
ATOM   3122 C CG2 . ILE A 1 390 ? 25.448 106.223 22.478  1.00 25.85 ? 390  ILE A CG2 1 
ATOM   3123 C CD1 . ILE A 1 390 ? 26.548 104.149 25.696  1.00 20.11 ? 390  ILE A CD1 1 
ATOM   3124 N N   . TRP A 1 391 ? 25.001 101.327 23.337  1.00 24.59 ? 391  TRP A N   1 
ATOM   3125 C CA  . TRP A 1 391 ? 25.596 100.003 23.611  1.00 24.20 ? 391  TRP A CA  1 
ATOM   3126 C C   . TRP A 1 391 ? 25.771 99.218  22.322  1.00 23.87 ? 391  TRP A C   1 
ATOM   3127 O O   . TRP A 1 391 ? 25.107 99.506  21.340  1.00 23.37 ? 391  TRP A O   1 
ATOM   3128 C CB  . TRP A 1 391 ? 24.778 99.167  24.618  1.00 24.32 ? 391  TRP A CB  1 
ATOM   3129 C CG  . TRP A 1 391 ? 24.341 99.897  25.844  1.00 25.26 ? 391  TRP A CG  1 
ATOM   3130 C CD1 . TRP A 1 391 ? 23.048 100.085 26.268  1.00 25.08 ? 391  TRP A CD1 1 
ATOM   3131 C CD2 . TRP A 1 391 ? 25.179 100.515 26.833  1.00 26.19 ? 391  TRP A CD2 1 
ATOM   3132 N NE1 . TRP A 1 391 ? 23.035 100.788 27.454  1.00 25.48 ? 391  TRP A NE1 1 
ATOM   3133 C CE2 . TRP A 1 391 ? 24.324 101.078 27.815  1.00 26.50 ? 391  TRP A CE2 1 
ATOM   3134 C CE3 . TRP A 1 391 ? 26.574 100.658 26.983  1.00 26.89 ? 391  TRP A CE3 1 
ATOM   3135 C CZ2 . TRP A 1 391 ? 24.815 101.760 28.932  1.00 26.95 ? 391  TRP A CZ2 1 
ATOM   3136 C CZ3 . TRP A 1 391 ? 27.055 101.346 28.075  1.00 25.89 ? 391  TRP A CZ3 1 
ATOM   3137 C CH2 . TRP A 1 391 ? 26.182 101.895 29.035  1.00 26.56 ? 391  TRP A CH2 1 
ATOM   3138 N N   . VAL A 1 392 ? 26.696 98.255  22.326  1.00 23.29 ? 392  VAL A N   1 
ATOM   3139 C CA  . VAL A 1 392 ? 26.789 97.250  21.279  1.00 23.17 ? 392  VAL A CA  1 
ATOM   3140 C C   . VAL A 1 392 ? 25.518 96.362  21.402  1.00 24.19 ? 392  VAL A C   1 
ATOM   3141 O O   . VAL A 1 392 ? 25.186 95.923  22.509  1.00 24.54 ? 392  VAL A O   1 
ATOM   3142 C CB  . VAL A 1 392 ? 28.022 96.312  21.512  1.00 23.40 ? 392  VAL A CB  1 
ATOM   3143 C CG1 . VAL A 1 392 ? 27.995 95.139  20.529  1.00 22.26 ? 392  VAL A CG1 1 
ATOM   3144 C CG2 . VAL A 1 392 ? 29.358 97.093  21.501  1.00 20.76 ? 392  VAL A CG2 1 
ATOM   3145 N N   . ASN A 1 393 ? 24.814 96.122  20.292  1.00 24.50 ? 393  ASN A N   1 
ATOM   3146 C CA  . ASN A 1 393 ? 23.585 95.299  20.290  1.00 24.90 ? 393  ASN A CA  1 
ATOM   3147 C C   . ASN A 1 393 ? 23.837 93.867  19.820  1.00 25.11 ? 393  ASN A C   1 
ATOM   3148 O O   . ASN A 1 393 ? 24.757 93.618  19.050  1.00 24.75 ? 393  ASN A O   1 
ATOM   3149 C CB  . ASN A 1 393 ? 22.549 95.930  19.352  1.00 25.07 ? 393  ASN A CB  1 
ATOM   3150 C CG  . ASN A 1 393 ? 22.105 97.315  19.793  1.00 24.97 ? 393  ASN A CG  1 
ATOM   3151 O OD1 . ASN A 1 393 ? 22.291 97.709  20.945  1.00 25.97 ? 393  ASN A OD1 1 
ATOM   3152 N ND2 . ASN A 1 393 ? 21.517 98.061  18.857  1.00 27.65 ? 393  ASN A ND2 1 
ATOM   3153 N N   . SER A 1 394 ? 22.997 92.927  20.241  1.00 25.98 ? 394  SER A N   1 
ATOM   3154 C CA  . SER A 1 394 ? 23.015 91.589  19.658  1.00 27.09 ? 394  SER A CA  1 
ATOM   3155 C C   . SER A 1 394 ? 22.552 91.631  18.215  1.00 26.68 ? 394  SER A C   1 
ATOM   3156 O O   . SER A 1 394 ? 22.200 92.691  17.725  1.00 26.10 ? 394  SER A O   1 
ATOM   3157 C CB  . SER A 1 394 ? 22.166 90.632  20.484  1.00 27.78 ? 394  SER A CB  1 
ATOM   3158 O OG  . SER A 1 394 ? 22.949 90.167  21.570  1.00 32.72 ? 394  SER A OG  1 
ATOM   3159 N N   . SER A 1 395 ? 22.573 90.490  17.527  1.00 27.54 ? 395  SER A N   1 
ATOM   3160 C CA  . SER A 1 395 ? 22.280 90.468  16.086  1.00 29.31 ? 395  SER A CA  1 
ATOM   3161 C C   . SER A 1 395 ? 20.897 91.006  15.679  1.00 30.43 ? 395  SER A C   1 
ATOM   3162 O O   . SER A 1 395 ? 20.724 91.394  14.522  1.00 30.87 ? 395  SER A O   1 
ATOM   3163 C CB  . SER A 1 395 ? 22.485 89.084  15.480  1.00 28.73 ? 395  SER A CB  1 
ATOM   3164 O OG  . SER A 1 395 ? 21.717 88.123  16.173  1.00 31.36 ? 395  SER A OG  1 
ATOM   3165 N N   . ASP A 1 396 ? 19.926 91.037  16.597  1.00 31.36 ? 396  ASP A N   1 
ATOM   3166 C CA  . ASP A 1 396 ? 18.611 91.589  16.245  1.00 32.70 ? 396  ASP A CA  1 
ATOM   3167 C C   . ASP A 1 396 ? 18.684 93.098  15.918  1.00 33.24 ? 396  ASP A C   1 
ATOM   3168 O O   . ASP A 1 396 ? 17.748 93.682  15.370  1.00 33.67 ? 396  ASP A O   1 
ATOM   3169 C CB  . ASP A 1 396 ? 17.512 91.222  17.274  1.00 33.17 ? 396  ASP A CB  1 
ATOM   3170 C CG  . ASP A 1 396 ? 17.730 91.846  18.671  1.00 34.97 ? 396  ASP A CG  1 
ATOM   3171 O OD1 . ASP A 1 396 ? 18.682 92.644  18.887  1.00 35.55 ? 396  ASP A OD1 1 
ATOM   3172 O OD2 . ASP A 1 396 ? 16.911 91.532  19.575  1.00 38.20 ? 396  ASP A OD2 1 
ATOM   3173 N N   . GLY A 1 397 ? 19.829 93.711  16.210  1.00 33.46 ? 397  GLY A N   1 
ATOM   3174 C CA  . GLY A 1 397 ? 20.034 95.127  15.970  1.00 32.67 ? 397  GLY A CA  1 
ATOM   3175 C C   . GLY A 1 397 ? 19.337 96.037  16.966  1.00 32.88 ? 397  GLY A C   1 
ATOM   3176 O O   . GLY A 1 397 ? 19.431 97.240  16.829  1.00 33.47 ? 397  GLY A O   1 
ATOM   3177 N N   . VAL A 1 398 ? 18.618 95.503  17.951  1.00 32.76 ? 398  VAL A N   1 
ATOM   3178 C CA  . VAL A 1 398 ? 17.921 96.399  18.920  1.00 32.29 ? 398  VAL A CA  1 
ATOM   3179 C C   . VAL A 1 398 ? 18.169 96.158  20.416  1.00 31.23 ? 398  VAL A C   1 
ATOM   3180 O O   . VAL A 1 398 ? 18.015 97.062  21.204  1.00 31.19 ? 398  VAL A O   1 
ATOM   3181 C CB  . VAL A 1 398 ? 16.366 96.569  18.649  1.00 33.03 ? 398  VAL A CB  1 
ATOM   3182 C CG1 . VAL A 1 398 ? 16.109 97.249  17.296  1.00 33.41 ? 398  VAL A CG1 1 
ATOM   3183 C CG2 . VAL A 1 398 ? 15.605 95.250  18.785  1.00 32.45 ? 398  VAL A CG2 1 
ATOM   3184 N N   . THR A 1 399 ? 18.540 94.943  20.798  1.00 30.32 ? 399  THR A N   1 
ATOM   3185 C CA  . THR A 1 399 ? 18.768 94.620  22.212  1.00 30.42 ? 399  THR A CA  1 
ATOM   3186 C C   . THR A 1 399 ? 20.277 94.661  22.533  1.00 29.59 ? 399  THR A C   1 
ATOM   3187 O O   . THR A 1 399 ? 21.057 93.971  21.868  1.00 28.89 ? 399  THR A O   1 
ATOM   3188 C CB  . THR A 1 399 ? 18.218 93.215  22.560  1.00 30.21 ? 399  THR A CB  1 
ATOM   3189 O OG1 . THR A 1 399 ? 17.011 92.975  21.821  1.00 32.03 ? 399  THR A OG1 1 
ATOM   3190 C CG2 . THR A 1 399 ? 17.939 93.086  24.053  1.00 31.58 ? 399  THR A CG2 1 
ATOM   3191 N N   . PRO A 1 400 ? 20.682 95.487  23.520  1.00 28.68 ? 400  PRO A N   1 
ATOM   3192 C CA  . PRO A 1 400 ? 22.067 95.503  23.989  1.00 28.03 ? 400  PRO A CA  1 
ATOM   3193 C C   . PRO A 1 400 ? 22.605 94.116  24.352  1.00 27.78 ? 400  PRO A C   1 
ATOM   3194 O O   . PRO A 1 400 ? 21.943 93.348  25.067  1.00 27.93 ? 400  PRO A O   1 
ATOM   3195 C CB  . PRO A 1 400 ? 22.024 96.440  25.208  1.00 28.02 ? 400  PRO A CB  1 
ATOM   3196 C CG  . PRO A 1 400 ? 20.942 97.414  24.857  1.00 28.48 ? 400  PRO A CG  1 
ATOM   3197 C CD  . PRO A 1 400 ? 19.867 96.520  24.196  1.00 28.69 ? 400  PRO A CD  1 
ATOM   3198 N N   . LEU A 1 401 ? 23.801 93.800  23.858  1.00 26.21 ? 401  LEU A N   1 
ATOM   3199 C CA  . LEU A 1 401 ? 24.465 92.549  24.199  1.00 25.11 ? 401  LEU A CA  1 
ATOM   3200 C C   . LEU A 1 401 ? 24.903 92.548  25.676  1.00 24.76 ? 401  LEU A C   1 
ATOM   3201 O O   . LEU A 1 401 ? 25.540 93.494  26.160  1.00 25.20 ? 401  LEU A O   1 
ATOM   3202 C CB  . LEU A 1 401 ? 25.636 92.290  23.245  1.00 23.96 ? 401  LEU A CB  1 
ATOM   3203 C CG  . LEU A 1 401 ? 26.369 90.948  23.320  1.00 25.53 ? 401  LEU A CG  1 
ATOM   3204 C CD1 . LEU A 1 401 ? 27.131 90.665  22.014  1.00 26.59 ? 401  LEU A CD1 1 
ATOM   3205 C CD2 . LEU A 1 401 ? 27.321 90.846  24.495  1.00 23.56 ? 401  LEU A CD2 1 
ATOM   3206 N N   . ILE A 1 402 ? 24.570 91.475  26.382  1.00 23.90 ? 402  ILE A N   1 
ATOM   3207 C CA  . ILE A 1 402 ? 25.024 91.289  27.753  1.00 24.50 ? 402  ILE A CA  1 
ATOM   3208 C C   . ILE A 1 402 ? 26.152 90.264  27.826  1.00 23.34 ? 402  ILE A C   1 
ATOM   3209 O O   . ILE A 1 402 ? 26.071 89.162  27.275  1.00 23.41 ? 402  ILE A O   1 
ATOM   3210 C CB  . ILE A 1 402 ? 23.877 90.807  28.721  1.00 25.79 ? 402  ILE A CB  1 
ATOM   3211 C CG1 . ILE A 1 402 ? 22.561 91.596  28.519  1.00 27.76 ? 402  ILE A CG1 1 
ATOM   3212 C CG2 . ILE A 1 402 ? 24.337 90.834  30.206  1.00 26.34 ? 402  ILE A CG2 1 
ATOM   3213 C CD1 . ILE A 1 402 ? 22.649 93.005  28.925  1.00 31.60 ? 402  ILE A CD1 1 
ATOM   3214 N N   . GLY A 1 403 ? 27.207 90.641  28.534  1.00 22.91 ? 403  GLY A N   1 
ATOM   3215 C CA  . GLY A 1 403 ? 28.323 89.777  28.795  1.00 22.26 ? 403  GLY A CA  1 
ATOM   3216 C C   . GLY A 1 403 ? 28.639 89.895  30.270  1.00 22.62 ? 403  GLY A C   1 
ATOM   3217 O O   . GLY A 1 403 ? 27.770 90.220  31.072  1.00 22.11 ? 403  GLY A O   1 
ATOM   3218 N N   . GLU A 1 404 ? 29.876 89.618  30.630  1.00 22.02 ? 404  GLU A N   1 
ATOM   3219 C CA  . GLU A 1 404 ? 30.298 89.615  32.008  1.00 22.83 ? 404  GLU A CA  1 
ATOM   3220 C C   . GLU A 1 404 ? 31.782 90.009  32.074  1.00 22.91 ? 404  GLU A C   1 
ATOM   3221 O O   . GLU A 1 404 ? 32.612 89.388  31.389  1.00 22.15 ? 404  GLU A O   1 
ATOM   3222 C CB  . GLU A 1 404 ? 30.152 88.198  32.567  1.00 23.47 ? 404  GLU A CB  1 
ATOM   3223 C CG  . GLU A 1 404 ? 30.277 88.101  34.077  1.00 30.43 ? 404  GLU A CG  1 
ATOM   3224 C CD  . GLU A 1 404 ? 30.597 86.672  34.546  1.00 39.25 ? 404  GLU A CD  1 
ATOM   3225 O OE1 . GLU A 1 404 ? 29.921 85.724  34.053  1.00 42.81 ? 404  GLU A OE1 1 
ATOM   3226 O OE2 . GLU A 1 404 ? 31.517 86.508  35.400  1.00 40.40 ? 404  GLU A OE2 1 
ATOM   3227 N N   . VAL A 1 405 ? 32.103 91.020  32.887  1.00 22.17 ? 405  VAL A N   1 
ATOM   3228 C CA  . VAL A 1 405 ? 33.493 91.383  33.201  1.00 21.11 ? 405  VAL A CA  1 
ATOM   3229 C C   . VAL A 1 405 ? 33.589 91.611  34.734  1.00 20.97 ? 405  VAL A C   1 
ATOM   3230 O O   . VAL A 1 405 ? 32.862 90.950  35.486  1.00 19.81 ? 405  VAL A O   1 
ATOM   3231 C CB  . VAL A 1 405 ? 34.046 92.557  32.355  1.00 21.64 ? 405  VAL A CB  1 
ATOM   3232 C CG1 . VAL A 1 405 ? 35.615 92.493  32.275  1.00 19.83 ? 405  VAL A CG1 1 
ATOM   3233 C CG2 . VAL A 1 405 ? 33.518 92.533  30.937  1.00 21.53 ? 405  VAL A CG2 1 
ATOM   3234 N N   . TRP A 1 406 ? 34.448 92.524  35.195  1.00 20.51 ? 406  TRP A N   1 
ATOM   3235 C CA  . TRP A 1 406 ? 34.769 92.638  36.611  1.00 21.04 ? 406  TRP A CA  1 
ATOM   3236 C C   . TRP A 1 406 ? 33.567 92.881  37.546  1.00 22.92 ? 406  TRP A C   1 
ATOM   3237 O O   . TRP A 1 406 ? 33.525 92.285  38.618  1.00 23.18 ? 406  TRP A O   1 
ATOM   3238 C CB  . TRP A 1 406 ? 35.788 93.744  36.857  1.00 21.05 ? 406  TRP A CB  1 
ATOM   3239 C CG  . TRP A 1 406 ? 37.069 93.585  36.112  1.00 20.19 ? 406  TRP A CG  1 
ATOM   3240 C CD1 . TRP A 1 406 ? 37.571 94.419  35.157  1.00 20.48 ? 406  TRP A CD1 1 
ATOM   3241 C CD2 . TRP A 1 406 ? 38.030 92.542  36.294  1.00 21.15 ? 406  TRP A CD2 1 
ATOM   3242 N NE1 . TRP A 1 406 ? 38.804 93.936  34.699  1.00 19.45 ? 406  TRP A NE1 1 
ATOM   3243 C CE2 . TRP A 1 406 ? 39.102 92.790  35.392  1.00 21.25 ? 406  TRP A CE2 1 
ATOM   3244 C CE3 . TRP A 1 406 ? 38.098 91.414  37.140  1.00 23.36 ? 406  TRP A CE3 1 
ATOM   3245 C CZ2 . TRP A 1 406 ? 40.215 91.945  35.303  1.00 22.44 ? 406  TRP A CZ2 1 
ATOM   3246 C CZ3 . TRP A 1 406 ? 39.220 90.566  37.040  1.00 21.90 ? 406  TRP A CZ3 1 
ATOM   3247 C CH2 . TRP A 1 406 ? 40.263 90.853  36.130  1.00 21.55 ? 406  TRP A CH2 1 
ATOM   3248 N N   . PRO A 1 407 ? 32.635 93.782  37.163  1.00 23.51 ? 407  PRO A N   1 
ATOM   3249 C CA  . PRO A 1 407 ? 31.530 94.044  38.071  1.00 25.59 ? 407  PRO A CA  1 
ATOM   3250 C C   . PRO A 1 407 ? 30.425 93.003  38.104  1.00 26.73 ? 407  PRO A C   1 
ATOM   3251 O O   . PRO A 1 407 ? 29.601 93.065  38.999  1.00 27.91 ? 407  PRO A O   1 
ATOM   3252 C CB  . PRO A 1 407 ? 30.955 95.374  37.564  1.00 24.58 ? 407  PRO A CB  1 
ATOM   3253 C CG  . PRO A 1 407 ? 31.323 95.450  36.144  1.00 24.22 ? 407  PRO A CG  1 
ATOM   3254 C CD  . PRO A 1 407 ? 32.558 94.627  35.946  1.00 23.68 ? 407  PRO A CD  1 
ATOM   3255 N N   . GLY A 1 408 ? 30.430 92.037  37.195  1.00 27.28 ? 408  GLY A N   1 
ATOM   3256 C CA  . GLY A 1 408 ? 29.274 91.158  37.030  1.00 28.18 ? 408  GLY A CA  1 
ATOM   3257 C C   . GLY A 1 408 ? 28.750 91.325  35.616  1.00 28.90 ? 408  GLY A C   1 
ATOM   3258 O O   . GLY A 1 408 ? 29.527 91.663  34.713  1.00 29.34 ? 408  GLY A O   1 
ATOM   3259 N N   . GLN A 1 409 ? 27.453 91.104  35.403  1.00 28.88 ? 409  GLN A N   1 
ATOM   3260 C CA  . GLN A 1 409 ? 26.865 91.283  34.060  1.00 29.18 ? 409  GLN A CA  1 
ATOM   3261 C C   . GLN A 1 409 ? 26.965 92.730  33.564  1.00 28.22 ? 409  GLN A C   1 
ATOM   3262 O O   . GLN A 1 409 ? 26.787 93.686  34.330  1.00 27.36 ? 409  GLN A O   1 
ATOM   3263 C CB  . GLN A 1 409 ? 25.438 90.741  33.953  1.00 30.03 ? 409  GLN A CB  1 
ATOM   3264 C CG  . GLN A 1 409 ? 25.317 89.300  34.419  1.00 34.33 ? 409  GLN A CG  1 
ATOM   3265 C CD  . GLN A 1 409 ? 24.322 88.495  33.606  1.00 40.07 ? 409  GLN A CD  1 
ATOM   3266 O OE1 . GLN A 1 409 ? 23.351 89.029  33.053  1.00 42.00 ? 409  GLN A OE1 1 
ATOM   3267 N NE2 . GLN A 1 409 ? 24.556 87.190  33.532  1.00 42.75 ? 409  GLN A NE2 1 
ATOM   3268 N N   . THR A 1 410 ? 27.267 92.870  32.277  1.00 27.15 ? 410  THR A N   1 
ATOM   3269 C CA  . THR A 1 410 ? 27.635 94.172  31.706  1.00 25.82 ? 410  THR A CA  1 
ATOM   3270 C C   . THR A 1 410 ? 27.135 94.326  30.295  1.00 25.36 ? 410  THR A C   1 
ATOM   3271 O O   . THR A 1 410 ? 26.936 93.348  29.592  1.00 25.71 ? 410  THR A O   1 
ATOM   3272 C CB  . THR A 1 410 ? 29.185 94.387  31.617  1.00 25.41 ? 410  THR A CB  1 
ATOM   3273 O OG1 . THR A 1 410 ? 29.754 93.379  30.771  1.00 25.24 ? 410  THR A OG1 1 
ATOM   3274 C CG2 . THR A 1 410 ? 29.869 94.370  32.964  1.00 22.13 ? 410  THR A CG2 1 
ATOM   3275 N N   . VAL A 1 411 ? 26.972 95.579  29.886  1.00 24.71 ? 411  VAL A N   1 
ATOM   3276 C CA  . VAL A 1 411 ? 26.823 95.964  28.480  1.00 23.53 ? 411  VAL A CA  1 
ATOM   3277 C C   . VAL A 1 411 ? 28.140 96.639  28.040  1.00 23.88 ? 411  VAL A C   1 
ATOM   3278 O O   . VAL A 1 411 ? 29.013 96.922  28.862  1.00 24.93 ? 411  VAL A O   1 
ATOM   3279 C CB  . VAL A 1 411 ? 25.581 96.897  28.264  1.00 22.66 ? 411  VAL A CB  1 
ATOM   3280 C CG1 . VAL A 1 411 ? 24.276 96.105  28.453  1.00 23.18 ? 411  VAL A CG1 1 
ATOM   3281 C CG2 . VAL A 1 411 ? 25.603 98.049  29.226  1.00 20.36 ? 411  VAL A CG2 1 
ATOM   3282 N N   . PHE A 1 412 ? 28.292 96.879  26.750  1.00 24.12 ? 412  PHE A N   1 
ATOM   3283 C CA  . PHE A 1 412 ? 29.561 97.345  26.171  1.00 23.10 ? 412  PHE A CA  1 
ATOM   3284 C C   . PHE A 1 412 ? 29.275 98.571  25.331  1.00 22.73 ? 412  PHE A C   1 
ATOM   3285 O O   . PHE A 1 412 ? 28.411 98.543  24.470  1.00 23.47 ? 412  PHE A O   1 
ATOM   3286 C CB  . PHE A 1 412 ? 30.150 96.240  25.295  1.00 22.59 ? 412  PHE A CB  1 
ATOM   3287 C CG  . PHE A 1 412 ? 30.389 94.943  26.039  1.00 22.16 ? 412  PHE A CG  1 
ATOM   3288 C CD1 . PHE A 1 412 ? 31.594 94.690  26.621  1.00 19.91 ? 412  PHE A CD1 1 
ATOM   3289 C CD2 . PHE A 1 412 ? 29.376 94.004  26.186  1.00 19.70 ? 412  PHE A CD2 1 
ATOM   3290 C CE1 . PHE A 1 412 ? 31.827 93.497  27.324  1.00 21.65 ? 412  PHE A CE1 1 
ATOM   3291 C CE2 . PHE A 1 412 ? 29.595 92.829  26.888  1.00 19.27 ? 412  PHE A CE2 1 
ATOM   3292 C CZ  . PHE A 1 412 ? 30.838 92.574  27.446  1.00 22.31 ? 412  PHE A CZ  1 
ATOM   3293 N N   . PRO A 1 413 ? 29.986 99.663  25.588  1.00 22.33 ? 413  PRO A N   1 
ATOM   3294 C CA  . PRO A 1 413 ? 29.813 100.840 24.737  1.00 21.88 ? 413  PRO A CA  1 
ATOM   3295 C C   . PRO A 1 413 ? 30.237 100.586 23.285  1.00 22.35 ? 413  PRO A C   1 
ATOM   3296 O O   . PRO A 1 413 ? 31.194 99.838  23.014  1.00 22.60 ? 413  PRO A O   1 
ATOM   3297 C CB  . PRO A 1 413 ? 30.677 101.915 25.410  1.00 21.98 ? 413  PRO A CB  1 
ATOM   3298 C CG  . PRO A 1 413 ? 31.170 101.342 26.687  1.00 22.72 ? 413  PRO A CG  1 
ATOM   3299 C CD  . PRO A 1 413 ? 30.985 99.848  26.646  1.00 22.47 ? 413  PRO A CD  1 
ATOM   3300 N N   . ASP A 1 414 ? 29.521 101.188 22.350  1.00 22.33 ? 414  ASP A N   1 
ATOM   3301 C CA  . ASP A 1 414 ? 29.892 101.128 20.955  1.00 23.47 ? 414  ASP A CA  1 
ATOM   3302 C C   . ASP A 1 414 ? 30.643 102.404 20.659  1.00 23.56 ? 414  ASP A C   1 
ATOM   3303 O O   . ASP A 1 414 ? 30.046 103.420 20.317  1.00 24.51 ? 414  ASP A O   1 
ATOM   3304 C CB  . ASP A 1 414 ? 28.650 101.016 20.064  1.00 23.95 ? 414  ASP A CB  1 
ATOM   3305 C CG  . ASP A 1 414 ? 28.948 101.227 18.586  1.00 24.53 ? 414  ASP A CG  1 
ATOM   3306 O OD1 . ASP A 1 414 ? 30.114 101.106 18.165  1.00 26.44 ? 414  ASP A OD1 1 
ATOM   3307 O OD2 . ASP A 1 414 ? 27.992 101.510 17.828  1.00 25.38 ? 414  ASP A OD2 1 
ATOM   3308 N N   . TYR A 1 415 ? 31.952 102.371 20.839  1.00 23.10 ? 415  TYR A N   1 
ATOM   3309 C CA  . TYR A 1 415 ? 32.757 103.589 20.675  1.00 22.03 ? 415  TYR A CA  1 
ATOM   3310 C C   . TYR A 1 415 ? 32.841 104.008 19.227  1.00 22.47 ? 415  TYR A C   1 
ATOM   3311 O O   . TYR A 1 415 ? 33.359 105.076 18.949  1.00 23.42 ? 415  TYR A O   1 
ATOM   3312 C CB  . TYR A 1 415 ? 34.172 103.427 21.295  1.00 20.29 ? 415  TYR A CB  1 
ATOM   3313 C CG  . TYR A 1 415 ? 34.181 103.173 22.794  1.00 17.61 ? 415  TYR A CG  1 
ATOM   3314 C CD1 . TYR A 1 415 ? 33.985 104.209 23.701  1.00 15.22 ? 415  TYR A CD1 1 
ATOM   3315 C CD2 . TYR A 1 415 ? 34.424 101.917 23.300  1.00 16.99 ? 415  TYR A CD2 1 
ATOM   3316 C CE1 . TYR A 1 415 ? 34.012 103.990 25.069  1.00 16.73 ? 415  TYR A CE1 1 
ATOM   3317 C CE2 . TYR A 1 415 ? 34.426 101.683 24.692  1.00 19.60 ? 415  TYR A CE2 1 
ATOM   3318 C CZ  . TYR A 1 415 ? 34.208 102.733 25.563  1.00 17.65 ? 415  TYR A CZ  1 
ATOM   3319 O OH  . TYR A 1 415 ? 34.215 102.528 26.927  1.00 17.36 ? 415  TYR A OH  1 
ATOM   3320 N N   . THR A 1 416 ? 32.319 103.203 18.297  1.00 24.01 ? 416  THR A N   1 
ATOM   3321 C CA  . THR A 1 416 ? 32.284 103.610 16.877  1.00 25.40 ? 416  THR A CA  1 
ATOM   3322 C C   . THR A 1 416 ? 31.191 104.642 16.573  1.00 26.48 ? 416  THR A C   1 
ATOM   3323 O O   . THR A 1 416 ? 31.258 105.361 15.576  1.00 26.99 ? 416  THR A O   1 
ATOM   3324 C CB  . THR A 1 416 ? 32.218 102.429 15.871  1.00 24.78 ? 416  THR A CB  1 
ATOM   3325 O OG1 . THR A 1 416 ? 30.899 101.874 15.829  1.00 27.83 ? 416  THR A OG1 1 
ATOM   3326 C CG2 . THR A 1 416 ? 33.213 101.346 16.213  1.00 24.57 ? 416  THR A CG2 1 
ATOM   3327 N N   . ASN A 1 417 ? 30.192 104.705 17.443  1.00 28.39 ? 417  ASN A N   1 
ATOM   3328 C CA  . ASN A 1 417 ? 29.106 105.660 17.358  1.00 29.19 ? 417  ASN A CA  1 
ATOM   3329 C C   . ASN A 1 417 ? 29.618 106.978 17.930  1.00 30.62 ? 417  ASN A C   1 
ATOM   3330 O O   . ASN A 1 417 ? 30.011 107.009 19.095  1.00 30.79 ? 417  ASN A O   1 
ATOM   3331 C CB  . ASN A 1 417 ? 27.953 105.139 18.212  1.00 29.56 ? 417  ASN A CB  1 
ATOM   3332 C CG  . ASN A 1 417 ? 26.702 106.018 18.131  1.00 30.29 ? 417  ASN A CG  1 
ATOM   3333 O OD1 . ASN A 1 417 ? 26.789 107.208 17.865  1.00 31.12 ? 417  ASN A OD1 1 
ATOM   3334 N ND2 . ASN A 1 417 ? 25.544 105.431 18.403  1.00 29.04 ? 417  ASN A ND2 1 
ATOM   3335 N N   . PRO A 1 418 ? 29.635 108.073 17.125  1.00 31.89 ? 418  PRO A N   1 
ATOM   3336 C CA  . PRO A 1 418 ? 30.131 109.374 17.650  1.00 32.86 ? 418  PRO A CA  1 
ATOM   3337 C C   . PRO A 1 418 ? 29.327 109.922 18.856  1.00 32.91 ? 418  PRO A C   1 
ATOM   3338 O O   . PRO A 1 418 ? 29.854 110.680 19.666  1.00 32.80 ? 418  PRO A O   1 
ATOM   3339 C CB  . PRO A 1 418 ? 30.017 110.304 16.437  1.00 33.59 ? 418  PRO A CB  1 
ATOM   3340 C CG  . PRO A 1 418 ? 28.968 109.634 15.545  1.00 33.78 ? 418  PRO A CG  1 
ATOM   3341 C CD  . PRO A 1 418 ? 29.221 108.176 15.714  1.00 31.81 ? 418  PRO A CD  1 
ATOM   3342 N N   . ASN A 1 419 ? 28.070 109.504 18.977  1.00 32.80 ? 419  ASN A N   1 
ATOM   3343 C CA  . ASN A 1 419 ? 27.264 109.793 20.150  1.00 32.62 ? 419  ASN A CA  1 
ATOM   3344 C C   . ASN A 1 419 ? 27.731 109.054 21.423  1.00 32.09 ? 419  ASN A C   1 
ATOM   3345 O O   . ASN A 1 419 ? 27.389 109.469 22.545  1.00 31.28 ? 419  ASN A O   1 
ATOM   3346 C CB  . ASN A 1 419 ? 25.797 109.477 19.860  1.00 33.41 ? 419  ASN A CB  1 
ATOM   3347 C CG  . ASN A 1 419 ? 24.857 110.334 20.665  1.00 37.24 ? 419  ASN A CG  1 
ATOM   3348 O OD1 . ASN A 1 419 ? 23.922 109.824 21.330  1.00 40.54 ? 419  ASN A OD1 1 
ATOM   3349 N ND2 . ASN A 1 419 ? 25.091 111.658 20.626  1.00 38.89 ? 419  ASN A ND2 1 
ATOM   3350 N N   . CYS A 1 420 ? 28.515 107.978 21.252  1.00 31.37 ? 420  CYS A N   1 
ATOM   3351 C CA  . CYS A 1 420 ? 29.127 107.281 22.379  1.00 30.74 ? 420  CYS A CA  1 
ATOM   3352 C C   . CYS A 1 420 ? 30.227 108.095 23.036  1.00 30.82 ? 420  CYS A C   1 
ATOM   3353 O O   . CYS A 1 420 ? 30.289 108.156 24.267  1.00 31.65 ? 420  CYS A O   1 
ATOM   3354 C CB  . CYS A 1 420 ? 29.681 105.922 21.970  1.00 30.86 ? 420  CYS A CB  1 
ATOM   3355 S SG  . CYS A 1 420 ? 30.191 104.873 23.374  1.00 31.30 ? 420  CYS A SG  1 
ATOM   3356 N N   . ALA A 1 421 ? 31.083 108.738 22.236  1.00 30.48 ? 421  ALA A N   1 
ATOM   3357 C CA  . ALA A 1 421 ? 32.106 109.661 22.754  1.00 29.88 ? 421  ALA A CA  1 
ATOM   3358 C C   . ALA A 1 421 ? 31.476 110.782 23.610  1.00 29.86 ? 421  ALA A C   1 
ATOM   3359 O O   . ALA A 1 421 ? 32.025 111.161 24.646  1.00 30.79 ? 421  ALA A O   1 
ATOM   3360 C CB  . ALA A 1 421 ? 32.938 110.257 21.595  1.00 29.42 ? 421  ALA A CB  1 
ATOM   3361 N N   . VAL A 1 422 ? 30.322 111.292 23.179  1.00 29.21 ? 422  VAL A N   1 
ATOM   3362 C CA  . VAL A 1 422 ? 29.529 112.247 23.977  1.00 28.26 ? 422  VAL A CA  1 
ATOM   3363 C C   . VAL A 1 422 ? 29.199 111.675 25.350  1.00 27.40 ? 422  VAL A C   1 
ATOM   3364 O O   . VAL A 1 422 ? 29.560 112.267 26.373  1.00 27.51 ? 422  VAL A O   1 
ATOM   3365 C CB  . VAL A 1 422 ? 28.263 112.740 23.216  1.00 28.20 ? 422  VAL A CB  1 
ATOM   3366 C CG1 . VAL A 1 422 ? 27.401 113.665 24.112  1.00 27.95 ? 422  VAL A CG1 1 
ATOM   3367 C CG2 . VAL A 1 422 ? 28.678 113.454 21.940  1.00 28.02 ? 422  VAL A CG2 1 
ATOM   3368 N N   . TRP A 1 423 ? 28.560 110.503 25.382  1.00 26.92 ? 423  TRP A N   1 
ATOM   3369 C CA  . TRP A 1 423 ? 28.302 109.786 26.647  1.00 25.71 ? 423  TRP A CA  1 
ATOM   3370 C C   . TRP A 1 423 ? 29.586 109.620 27.508  1.00 25.00 ? 423  TRP A C   1 
ATOM   3371 O O   . TRP A 1 423 ? 29.622 109.930 28.712  1.00 25.16 ? 423  TRP A O   1 
ATOM   3372 C CB  . TRP A 1 423 ? 27.639 108.412 26.359  1.00 26.11 ? 423  TRP A CB  1 
ATOM   3373 C CG  . TRP A 1 423 ? 27.651 107.505 27.551  1.00 25.66 ? 423  TRP A CG  1 
ATOM   3374 C CD1 . TRP A 1 423 ? 26.823 107.580 28.629  1.00 25.58 ? 423  TRP A CD1 1 
ATOM   3375 C CD2 . TRP A 1 423 ? 28.564 106.404 27.817  1.00 24.69 ? 423  TRP A CD2 1 
ATOM   3376 N NE1 . TRP A 1 423 ? 27.147 106.590 29.545  1.00 25.51 ? 423  TRP A NE1 1 
ATOM   3377 C CE2 . TRP A 1 423 ? 28.210 105.861 29.073  1.00 23.92 ? 423  TRP A CE2 1 
ATOM   3378 C CE3 . TRP A 1 423 ? 29.639 105.828 27.113  1.00 25.51 ? 423  TRP A CE3 1 
ATOM   3379 C CZ2 . TRP A 1 423 ? 28.894 104.768 29.654  1.00 24.59 ? 423  TRP A CZ2 1 
ATOM   3380 C CZ3 . TRP A 1 423 ? 30.315 104.743 27.695  1.00 25.52 ? 423  TRP A CZ3 1 
ATOM   3381 C CH2 . TRP A 1 423 ? 29.929 104.223 28.951  1.00 24.78 ? 423  TRP A CH2 1 
ATOM   3382 N N   . TRP A 1 424 ? 30.631 109.109 26.876  1.00 24.19 ? 424  TRP A N   1 
ATOM   3383 C CA  . TRP A 1 424 ? 31.877 108.731 27.539  1.00 23.37 ? 424  TRP A CA  1 
ATOM   3384 C C   . TRP A 1 424 ? 32.522 109.991 28.133  1.00 23.13 ? 424  TRP A C   1 
ATOM   3385 O O   . TRP A 1 424 ? 32.945 110.003 29.282  1.00 24.15 ? 424  TRP A O   1 
ATOM   3386 C CB  . TRP A 1 424 ? 32.773 108.118 26.457  1.00 21.90 ? 424  TRP A CB  1 
ATOM   3387 C CG  . TRP A 1 424 ? 34.051 107.441 26.840  1.00 21.77 ? 424  TRP A CG  1 
ATOM   3388 C CD1 . TRP A 1 424 ? 35.311 107.699 26.303  1.00 19.23 ? 424  TRP A CD1 1 
ATOM   3389 C CD2 . TRP A 1 424 ? 34.226 106.348 27.754  1.00 20.61 ? 424  TRP A CD2 1 
ATOM   3390 N NE1 . TRP A 1 424 ? 36.231 106.852 26.852  1.00 19.97 ? 424  TRP A NE1 1 
ATOM   3391 C CE2 . TRP A 1 424 ? 35.606 106.005 27.733  1.00 20.43 ? 424  TRP A CE2 1 
ATOM   3392 C CE3 . TRP A 1 424 ? 33.363 105.635 28.610  1.00 19.30 ? 424  TRP A CE3 1 
ATOM   3393 C CZ2 . TRP A 1 424 ? 36.135 104.972 28.520  1.00 20.56 ? 424  TRP A CZ2 1 
ATOM   3394 C CZ3 . TRP A 1 424 ? 33.898 104.594 29.387  1.00 20.53 ? 424  TRP A CZ3 1 
ATOM   3395 C CH2 . TRP A 1 424 ? 35.270 104.283 29.343  1.00 20.70 ? 424  TRP A CH2 1 
ATOM   3396 N N   . THR A 1 425 ? 32.575 111.052 27.345  1.00 23.48 ? 425  THR A N   1 
ATOM   3397 C CA  . THR A 1 425 ? 33.081 112.336 27.804  1.00 24.41 ? 425  THR A CA  1 
ATOM   3398 C C   . THR A 1 425 ? 32.371 112.829 29.068  1.00 25.04 ? 425  THR A C   1 
ATOM   3399 O O   . THR A 1 425 ? 33.035 113.208 30.027  1.00 25.20 ? 425  THR A O   1 
ATOM   3400 C CB  . THR A 1 425 ? 33.021 113.380 26.675  1.00 24.42 ? 425  THR A CB  1 
ATOM   3401 O OG1 . THR A 1 425 ? 33.794 112.898 25.555  1.00 23.50 ? 425  THR A OG1 1 
ATOM   3402 C CG2 . THR A 1 425 ? 33.557 114.764 27.142  1.00 23.82 ? 425  THR A CG2 1 
ATOM   3403 N N   . LYS A 1 426 ? 31.035 112.788 29.091  1.00 26.36 ? 426  LYS A N   1 
ATOM   3404 C CA  . LYS A 1 426 ? 30.285 113.244 30.271  1.00 26.49 ? 426  LYS A CA  1 
ATOM   3405 C C   . LYS A 1 426 ? 30.607 112.353 31.486  1.00 26.47 ? 426  LYS A C   1 
ATOM   3406 O O   . LYS A 1 426 ? 30.676 112.836 32.617  1.00 25.94 ? 426  LYS A O   1 
ATOM   3407 C CB  . LYS A 1 426 ? 28.770 113.242 30.013  1.00 27.83 ? 426  LYS A CB  1 
ATOM   3408 C CG  . LYS A 1 426 ? 27.951 113.920 31.142  1.00 29.27 ? 426  LYS A CG  1 
ATOM   3409 C CD  . LYS A 1 426 ? 28.240 115.421 31.131  1.00 33.22 ? 426  LYS A CD  1 
ATOM   3410 C CE  . LYS A 1 426 ? 27.472 116.208 32.191  1.00 37.06 ? 426  LYS A CE  1 
ATOM   3411 N NZ  . LYS A 1 426 ? 28.253 117.471 32.594  1.00 38.29 ? 426  LYS A NZ  1 
ATOM   3412 N N   . GLU A 1 427 ? 30.815 111.057 31.256  1.00 26.36 ? 427  GLU A N   1 
ATOM   3413 C CA  . GLU A 1 427 ? 31.143 110.162 32.370  1.00 26.98 ? 427  GLU A CA  1 
ATOM   3414 C C   . GLU A 1 427 ? 32.460 110.589 32.993  1.00 26.22 ? 427  GLU A C   1 
ATOM   3415 O O   . GLU A 1 427 ? 32.577 110.623 34.216  1.00 25.51 ? 427  GLU A O   1 
ATOM   3416 C CB  . GLU A 1 427 ? 31.194 108.693 31.945  1.00 26.83 ? 427  GLU A CB  1 
ATOM   3417 C CG  . GLU A 1 427 ? 29.845 108.111 31.524  1.00 28.52 ? 427  GLU A CG  1 
ATOM   3418 C CD  . GLU A 1 427 ? 28.777 108.231 32.583  1.00 32.25 ? 427  GLU A CD  1 
ATOM   3419 O OE1 . GLU A 1 427 ? 29.054 108.108 33.798  1.00 34.28 ? 427  GLU A OE1 1 
ATOM   3420 O OE2 . GLU A 1 427 ? 27.630 108.460 32.198  1.00 35.75 ? 427  GLU A OE2 1 
ATOM   3421 N N   . PHE A 1 428 ? 33.419 110.946 32.138  1.00 26.26 ? 428  PHE A N   1 
ATOM   3422 C CA  . PHE A 1 428 ? 34.726 111.446 32.596  1.00 27.32 ? 428  PHE A CA  1 
ATOM   3423 C C   . PHE A 1 428 ? 34.655 112.786 33.297  1.00 27.42 ? 428  PHE A C   1 
ATOM   3424 O O   . PHE A 1 428 ? 35.263 112.953 34.328  1.00 27.81 ? 428  PHE A O   1 
ATOM   3425 C CB  . PHE A 1 428 ? 35.761 111.460 31.467  1.00 27.25 ? 428  PHE A CB  1 
ATOM   3426 C CG  . PHE A 1 428 ? 36.418 110.133 31.258  1.00 27.60 ? 428  PHE A CG  1 
ATOM   3427 C CD1 . PHE A 1 428 ? 37.324 109.635 32.194  1.00 33.04 ? 428  PHE A CD1 1 
ATOM   3428 C CD2 . PHE A 1 428 ? 36.105 109.352 30.180  1.00 27.80 ? 428  PHE A CD2 1 
ATOM   3429 C CE1 . PHE A 1 428 ? 37.939 108.357 32.012  1.00 31.80 ? 428  PHE A CE1 1 
ATOM   3430 C CE2 . PHE A 1 428 ? 36.720 108.102 29.989  1.00 29.37 ? 428  PHE A CE2 1 
ATOM   3431 C CZ  . PHE A 1 428 ? 37.620 107.611 30.906  1.00 28.35 ? 428  PHE A CZ  1 
ATOM   3432 N N   . GLU A 1 429 ? 33.903 113.726 32.730  1.00 28.85 ? 429  GLU A N   1 
ATOM   3433 C CA  . GLU A 1 429 ? 33.590 115.008 33.375  1.00 30.02 ? 429  GLU A CA  1 
ATOM   3434 C C   . GLU A 1 429 ? 33.001 114.811 34.768  1.00 29.29 ? 429  GLU A C   1 
ATOM   3435 O O   . GLU A 1 429 ? 33.516 115.347 35.743  1.00 29.14 ? 429  GLU A O   1 
ATOM   3436 C CB  . GLU A 1 429 ? 32.539 115.730 32.565  1.00 30.52 ? 429  GLU A CB  1 
ATOM   3437 C CG  . GLU A 1 429 ? 33.046 116.651 31.526  1.00 36.95 ? 429  GLU A CG  1 
ATOM   3438 C CD  . GLU A 1 429 ? 31.986 117.726 31.222  1.00 46.26 ? 429  GLU A CD  1 
ATOM   3439 O OE1 . GLU A 1 429 ? 30.779 117.464 31.515  1.00 46.66 ? 429  GLU A OE1 1 
ATOM   3440 O OE2 . GLU A 1 429 ? 32.359 118.820 30.709  1.00 48.81 ? 429  GLU A OE2 1 
ATOM   3441 N N   . LEU A 1 430 ? 31.925 114.032 34.853  1.00 28.49 ? 430  LEU A N   1 
ATOM   3442 C CA  . LEU A 1 430 ? 31.293 113.786 36.140  1.00 29.02 ? 430  LEU A CA  1 
ATOM   3443 C C   . LEU A 1 430 ? 32.270 113.185 37.150  1.00 28.57 ? 430  LEU A C   1 
ATOM   3444 O O   . LEU A 1 430 ? 32.325 113.647 38.293  1.00 29.41 ? 430  LEU A O   1 
ATOM   3445 C CB  . LEU A 1 430 ? 30.002 112.949 36.015  1.00 28.76 ? 430  LEU A CB  1 
ATOM   3446 C CG  . LEU A 1 430 ? 28.824 113.483 35.161  1.00 31.57 ? 430  LEU A CG  1 
ATOM   3447 C CD1 . LEU A 1 430 ? 27.709 112.441 35.062  1.00 33.18 ? 430  LEU A CD1 1 
ATOM   3448 C CD2 . LEU A 1 430 ? 28.229 114.817 35.671  1.00 34.60 ? 430  LEU A CD2 1 
ATOM   3449 N N   . PHE A 1 431 ? 33.056 112.181 36.741  1.00 27.40 ? 431  PHE A N   1 
ATOM   3450 C CA  . PHE A 1 431 ? 34.006 111.538 37.655  1.00 26.59 ? 431  PHE A CA  1 
ATOM   3451 C C   . PHE A 1 431 ? 35.195 112.422 38.061  1.00 27.34 ? 431  PHE A C   1 
ATOM   3452 O O   . PHE A 1 431 ? 35.690 112.330 39.204  1.00 27.26 ? 431  PHE A O   1 
ATOM   3453 C CB  . PHE A 1 431 ? 34.489 110.186 37.085  1.00 25.79 ? 431  PHE A CB  1 
ATOM   3454 C CG  . PHE A 1 431 ? 35.142 109.288 38.109  1.00 26.60 ? 431  PHE A CG  1 
ATOM   3455 C CD1 . PHE A 1 431 ? 34.532 109.058 39.351  1.00 26.19 ? 431  PHE A CD1 1 
ATOM   3456 C CD2 . PHE A 1 431 ? 36.365 108.666 37.837  1.00 23.78 ? 431  PHE A CD2 1 
ATOM   3457 C CE1 . PHE A 1 431 ? 35.136 108.225 40.306  1.00 26.03 ? 431  PHE A CE1 1 
ATOM   3458 C CE2 . PHE A 1 431 ? 36.974 107.842 38.793  1.00 25.74 ? 431  PHE A CE2 1 
ATOM   3459 C CZ  . PHE A 1 431 ? 36.363 107.614 40.021  1.00 25.63 ? 431  PHE A CZ  1 
ATOM   3460 N N   . HIS A 1 432 ? 35.668 113.262 37.139  1.00 28.23 ? 432  HIS A N   1 
ATOM   3461 C CA  . HIS A 1 432 ? 36.819 114.144 37.419  1.00 29.69 ? 432  HIS A CA  1 
ATOM   3462 C C   . HIS A 1 432 ? 36.511 115.201 38.499  1.00 30.92 ? 432  HIS A C   1 
ATOM   3463 O O   . HIS A 1 432 ? 37.393 115.631 39.226  1.00 31.05 ? 432  HIS A O   1 
ATOM   3464 C CB  . HIS A 1 432 ? 37.281 114.830 36.150  1.00 29.40 ? 432  HIS A CB  1 
ATOM   3465 C CG  . HIS A 1 432 ? 38.626 115.479 36.273  1.00 30.47 ? 432  HIS A CG  1 
ATOM   3466 N ND1 . HIS A 1 432 ? 38.784 116.829 36.495  1.00 33.01 ? 432  HIS A ND1 1 
ATOM   3467 C CD2 . HIS A 1 432 ? 39.877 114.964 36.208  1.00 30.90 ? 432  HIS A CD2 1 
ATOM   3468 C CE1 . HIS A 1 432 ? 40.072 117.117 36.581  1.00 31.49 ? 432  HIS A CE1 1 
ATOM   3469 N NE2 . HIS A 1 432 ? 40.758 116.006 36.383  1.00 30.12 ? 432  HIS A NE2 1 
ATOM   3470 N N   . ASN A 1 433 ? 35.246 115.612 38.580  1.00 32.25 ? 433  ASN A N   1 
ATOM   3471 C CA  . ASN A 1 433 ? 34.755 116.433 39.667  1.00 33.91 ? 433  ASN A CA  1 
ATOM   3472 C C   . ASN A 1 433 ? 34.932 115.792 41.051  1.00 34.29 ? 433  ASN A C   1 
ATOM   3473 O O   . ASN A 1 433 ? 35.047 116.490 42.045  1.00 35.58 ? 433  ASN A O   1 
ATOM   3474 C CB  . ASN A 1 433 ? 33.279 116.798 39.407  1.00 34.62 ? 433  ASN A CB  1 
ATOM   3475 C CG  . ASN A 1 433 ? 33.097 117.630 38.145  1.00 37.25 ? 433  ASN A CG  1 
ATOM   3476 O OD1 . ASN A 1 433 ? 34.009 118.355 37.728  1.00 42.16 ? 433  ASN A OD1 1 
ATOM   3477 N ND2 . ASN A 1 433 ? 31.914 117.546 37.534  1.00 39.94 ? 433  ASN A ND2 1 
ATOM   3478 N N   . GLN A 1 434 ? 34.957 114.469 41.120  1.00 35.01 ? 434  GLN A N   1 
ATOM   3479 C CA  . GLN A 1 434 ? 35.161 113.763 42.382  1.00 35.52 ? 434  GLN A CA  1 
ATOM   3480 C C   . GLN A 1 434 ? 36.645 113.424 42.633  1.00 35.32 ? 434  GLN A C   1 
ATOM   3481 O O   . GLN A 1 434 ? 37.196 113.702 43.713  1.00 35.64 ? 434  GLN A O   1 
ATOM   3482 C CB  . GLN A 1 434 ? 34.335 112.475 42.399  1.00 36.29 ? 434  GLN A CB  1 
ATOM   3483 C CG  . GLN A 1 434 ? 32.873 112.658 42.090  1.00 39.58 ? 434  GLN A CG  1 
ATOM   3484 C CD  . GLN A 1 434 ? 32.114 111.385 42.302  1.00 45.54 ? 434  GLN A CD  1 
ATOM   3485 O OE1 . GLN A 1 434 ? 31.656 110.753 41.337  1.00 49.71 ? 434  GLN A OE1 1 
ATOM   3486 N NE2 . GLN A 1 434 ? 31.988 110.969 43.571  1.00 47.63 ? 434  GLN A NE2 1 
ATOM   3487 N N   . VAL A 1 435 ? 37.281 112.807 41.632  1.00 34.30 ? 435  VAL A N   1 
ATOM   3488 C CA  . VAL A 1 435 ? 38.656 112.361 41.742  1.00 32.26 ? 435  VAL A CA  1 
ATOM   3489 C C   . VAL A 1 435 ? 39.387 112.998 40.589  1.00 31.90 ? 435  VAL A C   1 
ATOM   3490 O O   . VAL A 1 435 ? 39.115 112.674 39.440  1.00 31.67 ? 435  VAL A O   1 
ATOM   3491 C CB  . VAL A 1 435 ? 38.751 110.832 41.645  1.00 32.77 ? 435  VAL A CB  1 
ATOM   3492 C CG1 . VAL A 1 435 ? 40.201 110.363 41.889  1.00 33.01 ? 435  VAL A CG1 1 
ATOM   3493 C CG2 . VAL A 1 435 ? 37.785 110.169 42.624  1.00 31.44 ? 435  VAL A CG2 1 
ATOM   3494 N N   . GLU A 1 436 ? 40.305 113.922 40.888  1.00 30.63 ? 436  GLU A N   1 
ATOM   3495 C CA  . GLU A 1 436 ? 41.017 114.681 39.861  1.00 30.31 ? 436  GLU A CA  1 
ATOM   3496 C C   . GLU A 1 436 ? 42.210 113.893 39.287  1.00 28.03 ? 436  GLU A C   1 
ATOM   3497 O O   . GLU A 1 436 ? 43.362 114.205 39.555  1.00 27.79 ? 436  GLU A O   1 
ATOM   3498 C CB  . GLU A 1 436 ? 41.472 116.037 40.419  1.00 29.77 ? 436  GLU A CB  1 
ATOM   3499 C CG  . GLU A 1 436 ? 40.299 116.991 40.714  1.00 33.84 ? 436  GLU A CG  1 
ATOM   3500 C CD  . GLU A 1 436 ? 40.763 118.361 41.241  1.00 34.92 ? 436  GLU A CD  1 
ATOM   3501 O OE1 . GLU A 1 436 ? 41.417 119.120 40.476  1.00 42.86 ? 436  GLU A OE1 1 
ATOM   3502 O OE2 . GLU A 1 436 ? 40.475 118.676 42.415  1.00 39.12 ? 436  GLU A OE2 1 
ATOM   3503 N N   . PHE A 1 437 ? 41.905 112.866 38.503  1.00 26.15 ? 437  PHE A N   1 
ATOM   3504 C CA  . PHE A 1 437 ? 42.916 112.079 37.798  1.00 23.75 ? 437  PHE A CA  1 
ATOM   3505 C C   . PHE A 1 437 ? 43.555 112.920 36.672  1.00 23.29 ? 437  PHE A C   1 
ATOM   3506 O O   . PHE A 1 437 ? 43.005 113.947 36.238  1.00 23.12 ? 437  PHE A O   1 
ATOM   3507 C CB  . PHE A 1 437 ? 42.274 110.795 37.271  1.00 23.11 ? 437  PHE A CB  1 
ATOM   3508 C CG  . PHE A 1 437 ? 41.104 111.040 36.382  1.00 22.84 ? 437  PHE A CG  1 
ATOM   3509 C CD1 . PHE A 1 437 ? 41.289 111.264 35.007  1.00 24.72 ? 437  PHE A CD1 1 
ATOM   3510 C CD2 . PHE A 1 437 ? 39.816 111.072 36.894  1.00 22.76 ? 437  PHE A CD2 1 
ATOM   3511 C CE1 . PHE A 1 437 ? 40.197 111.532 34.159  1.00 24.51 ? 437  PHE A CE1 1 
ATOM   3512 C CE2 . PHE A 1 437 ? 38.734 111.315 36.075  1.00 22.22 ? 437  PHE A CE2 1 
ATOM   3513 C CZ  . PHE A 1 437 ? 38.910 111.561 34.707  1.00 23.35 ? 437  PHE A CZ  1 
ATOM   3514 N N   . ASP A 1 438 ? 44.732 112.511 36.215  1.00 22.35 ? 438  ASP A N   1 
ATOM   3515 C CA  . ASP A 1 438 ? 45.482 113.290 35.250  1.00 21.69 ? 438  ASP A CA  1 
ATOM   3516 C C   . ASP A 1 438 ? 45.591 112.564 33.933  1.00 21.47 ? 438  ASP A C   1 
ATOM   3517 O O   . ASP A 1 438 ? 45.912 113.164 32.908  1.00 22.00 ? 438  ASP A O   1 
ATOM   3518 C CB  . ASP A 1 438 ? 46.890 113.553 35.809  1.00 21.79 ? 438  ASP A CB  1 
ATOM   3519 C CG  . ASP A 1 438 ? 46.838 114.317 37.126  1.00 22.88 ? 438  ASP A CG  1 
ATOM   3520 O OD1 . ASP A 1 438 ? 46.343 115.462 37.039  1.00 22.54 ? 438  ASP A OD1 1 
ATOM   3521 O OD2 . ASP A 1 438 ? 47.233 113.773 38.218  1.00 22.33 ? 438  ASP A OD2 1 
ATOM   3522 N N   . GLY A 1 439 ? 45.391 111.254 33.982  1.00 20.98 ? 439  GLY A N   1 
ATOM   3523 C CA  . GLY A 1 439 ? 45.497 110.418 32.797  1.00 20.67 ? 439  GLY A CA  1 
ATOM   3524 C C   . GLY A 1 439 ? 44.646 109.188 32.979  1.00 20.19 ? 439  GLY A C   1 
ATOM   3525 O O   . GLY A 1 439 ? 44.110 108.939 34.060  1.00 19.12 ? 439  GLY A O   1 
ATOM   3526 N N   . ILE A 1 440 ? 44.564 108.403 31.917  1.00 21.11 ? 440  ILE A N   1 
ATOM   3527 C CA  . ILE A 1 440 ? 43.564 107.336 31.796  1.00 21.13 ? 440  ILE A CA  1 
ATOM   3528 C C   . ILE A 1 440 ? 44.222 106.083 31.235  1.00 21.06 ? 440  ILE A C   1 
ATOM   3529 O O   . ILE A 1 440 ? 44.872 106.144 30.214  1.00 21.39 ? 440  ILE A O   1 
ATOM   3530 C CB  . ILE A 1 440 ? 42.402 107.760 30.863  1.00 21.31 ? 440  ILE A CB  1 
ATOM   3531 C CG1 . ILE A 1 440 ? 41.719 109.023 31.427  1.00 23.26 ? 440  ILE A CG1 1 
ATOM   3532 C CG2 . ILE A 1 440 ? 41.376 106.648 30.759  1.00 21.59 ? 440  ILE A CG2 1 
ATOM   3533 C CD1 . ILE A 1 440 ? 40.961 109.824 30.413  1.00 24.12 ? 440  ILE A CD1 1 
ATOM   3534 N N   . TRP A 1 441 ? 44.028 104.968 31.929  1.00 20.52 ? 441  TRP A N   1 
ATOM   3535 C CA  . TRP A 1 441 ? 44.527 103.665 31.564  1.00 20.34 ? 441  TRP A CA  1 
ATOM   3536 C C   . TRP A 1 441 ? 43.304 102.824 31.125  1.00 20.12 ? 441  TRP A C   1 
ATOM   3537 O O   . TRP A 1 441 ? 42.460 102.496 31.947  1.00 19.92 ? 441  TRP A O   1 
ATOM   3538 C CB  . TRP A 1 441 ? 45.289 103.092 32.762  1.00 20.40 ? 441  TRP A CB  1 
ATOM   3539 C CG  . TRP A 1 441 ? 45.652 101.638 32.721  1.00 21.42 ? 441  TRP A CG  1 
ATOM   3540 C CD1 . TRP A 1 441 ? 45.752 100.836 31.624  1.00 22.39 ? 441  TRP A CD1 1 
ATOM   3541 C CD2 . TRP A 1 441 ? 45.996 100.812 33.857  1.00 22.18 ? 441  TRP A CD2 1 
ATOM   3542 N NE1 . TRP A 1 441 ? 46.099 99.554  32.002  1.00 20.65 ? 441  TRP A NE1 1 
ATOM   3543 C CE2 . TRP A 1 441 ? 46.258 99.518  33.365  1.00 21.27 ? 441  TRP A CE2 1 
ATOM   3544 C CE3 . TRP A 1 441 ? 46.113 101.054 35.244  1.00 20.55 ? 441  TRP A CE3 1 
ATOM   3545 C CZ2 . TRP A 1 441 ? 46.605 98.461  34.210  1.00 23.08 ? 441  TRP A CZ2 1 
ATOM   3546 C CZ3 . TRP A 1 441 ? 46.423 100.030 36.074  1.00 20.62 ? 441  TRP A CZ3 1 
ATOM   3547 C CH2 . TRP A 1 441 ? 46.706 98.742  35.563  1.00 23.01 ? 441  TRP A CH2 1 
ATOM   3548 N N   . ILE A 1 442 ? 43.181 102.576 29.816  1.00 19.95 ? 442  ILE A N   1 
ATOM   3549 C CA  . ILE A 1 442 ? 42.062 101.818 29.242  1.00 20.70 ? 442  ILE A CA  1 
ATOM   3550 C C   . ILE A 1 442 ? 42.470 100.376 28.984  1.00 20.86 ? 442  ILE A C   1 
ATOM   3551 O O   . ILE A 1 442 ? 43.473 100.079 28.310  1.00 20.93 ? 442  ILE A O   1 
ATOM   3552 C CB  . ILE A 1 442 ? 41.387 102.496 28.007  1.00 21.21 ? 442  ILE A CB  1 
ATOM   3553 C CG1 . ILE A 1 442 ? 42.394 102.805 26.870  1.00 21.43 ? 442  ILE A CG1 1 
ATOM   3554 C CG2 . ILE A 1 442 ? 40.714 103.806 28.447  1.00 20.85 ? 442  ILE A CG2 1 
ATOM   3555 C CD1 . ILE A 1 442 ? 41.726 103.264 25.527  1.00 20.67 ? 442  ILE A CD1 1 
ATOM   3556 N N   . ASP A 1 443 ? 41.703 99.479  29.589  1.00 20.91 ? 443  ASP A N   1 
ATOM   3557 C CA  . ASP A 1 443 ? 42.061 98.078  29.677  1.00 21.00 ? 443  ASP A CA  1 
ATOM   3558 C C   . ASP A 1 443 ? 40.884 97.202  29.236  1.00 21.43 ? 443  ASP A C   1 
ATOM   3559 O O   . ASP A 1 443 ? 39.761 97.703  29.028  1.00 20.94 ? 443  ASP A O   1 
ATOM   3560 C CB  . ASP A 1 443 ? 42.435 97.770  31.116  1.00 20.85 ? 443  ASP A CB  1 
ATOM   3561 C CG  . ASP A 1 443 ? 43.172 96.457  31.266  1.00 23.73 ? 443  ASP A CG  1 
ATOM   3562 O OD1 . ASP A 1 443 ? 43.922 96.054  30.359  1.00 22.20 ? 443  ASP A OD1 1 
ATOM   3563 O OD2 . ASP A 1 443 ? 43.000 95.825  32.319  1.00 28.72 ? 443  ASP A OD2 1 
ATOM   3564 N N   . MET A 1 444 ? 41.157 95.904  29.092  1.00 21.45 ? 444  MET A N   1 
ATOM   3565 C CA  . MET A 1 444 ? 40.136 94.903  28.790  1.00 20.88 ? 444  MET A CA  1 
ATOM   3566 C C   . MET A 1 444 ? 39.393 95.226  27.506  1.00 20.99 ? 444  MET A C   1 
ATOM   3567 O O   . MET A 1 444 ? 38.239 94.827  27.339  1.00 20.38 ? 444  MET A O   1 
ATOM   3568 C CB  . MET A 1 444 ? 39.142 94.735  29.966  1.00 20.98 ? 444  MET A CB  1 
ATOM   3569 C CG  . MET A 1 444 ? 39.773 94.476  31.324  1.00 18.21 ? 444  MET A CG  1 
ATOM   3570 S SD  . MET A 1 444 ? 40.610 92.926  31.425  1.00 23.05 ? 444  MET A SD  1 
ATOM   3571 C CE  . MET A 1 444 ? 39.233 91.774  31.409  1.00 21.48 ? 444  MET A CE  1 
ATOM   3572 N N   . ASN A 1 445 ? 40.054 95.939  26.583  1.00 20.51 ? 445  ASN A N   1 
ATOM   3573 C CA  . ASN A 1 445 ? 39.347 96.476  25.406  1.00 20.16 ? 445  ASN A CA  1 
ATOM   3574 C C   . ASN A 1 445 ? 39.599 95.747  24.065  1.00 20.43 ? 445  ASN A C   1 
ATOM   3575 O O   . ASN A 1 445 ? 39.559 96.348  23.013  1.00 20.92 ? 445  ASN A O   1 
ATOM   3576 C CB  . ASN A 1 445 ? 39.569 97.984  25.286  1.00 19.89 ? 445  ASN A CB  1 
ATOM   3577 C CG  . ASN A 1 445 ? 41.061 98.366  25.234  1.00 18.99 ? 445  ASN A CG  1 
ATOM   3578 O OD1 . ASN A 1 445 ? 41.963 97.552  25.431  1.00 18.77 ? 445  ASN A OD1 1 
ATOM   3579 N ND2 . ASN A 1 445 ? 41.303 99.604  24.962  1.00 17.71 ? 445  ASN A ND2 1 
ATOM   3580 N N   . GLU A 1 446 ? 39.800 94.441  24.116  1.00 21.13 ? 446  GLU A N   1 
ATOM   3581 C CA  . GLU A 1 446 ? 39.869 93.613  22.920  1.00 21.81 ? 446  GLU A CA  1 
ATOM   3582 C C   . GLU A 1 446 ? 38.607 93.482  22.063  1.00 23.03 ? 446  GLU A C   1 
ATOM   3583 O O   . GLU A 1 446 ? 38.719 93.432  20.844  1.00 22.82 ? 446  GLU A O   1 
ATOM   3584 C CB  . GLU A 1 446 ? 40.416 92.239  23.281  1.00 22.82 ? 446  GLU A CB  1 
ATOM   3585 C CG  . GLU A 1 446 ? 41.871 92.260  23.752  1.00 19.45 ? 446  GLU A CG  1 
ATOM   3586 C CD  . GLU A 1 446 ? 42.061 92.880  25.146  1.00 23.59 ? 446  GLU A CD  1 
ATOM   3587 O OE1 . GLU A 1 446 ? 41.246 92.634  26.089  1.00 22.83 ? 446  GLU A OE1 1 
ATOM   3588 O OE2 . GLU A 1 446 ? 43.066 93.631  25.301  1.00 26.98 ? 446  GLU A OE2 1 
ATOM   3589 N N   . VAL A 1 447 ? 37.396 93.431  22.617  1.00 24.68 ? 447  VAL A N   1 
ATOM   3590 C CA  . VAL A 1 447 ? 37.011 93.606  24.023  1.00 26.40 ? 447  VAL A CA  1 
ATOM   3591 C C   . VAL A 1 447 ? 37.051 92.235  24.758  1.00 26.77 ? 447  VAL A C   1 
ATOM   3592 O O   . VAL A 1 447 ? 36.822 91.190  24.146  1.00 28.27 ? 447  VAL A O   1 
ATOM   3593 C CB  . VAL A 1 447 ? 35.608 94.341  24.068  1.00 26.44 ? 447  VAL A CB  1 
ATOM   3594 C CG1 . VAL A 1 447 ? 34.503 93.387  23.772  1.00 27.62 ? 447  VAL A CG1 1 
ATOM   3595 C CG2 . VAL A 1 447 ? 35.361 95.046  25.396  1.00 28.01 ? 447  VAL A CG2 1 
ATOM   3596 N N   . SER A 1 448 ? 37.403 92.237  26.041  1.00 26.99 ? 448  SER A N   1 
ATOM   3597 C CA  . SER A 1 448 ? 37.539 91.023  26.848  1.00 26.73 ? 448  SER A CA  1 
ATOM   3598 C C   . SER A 1 448 ? 36.204 90.716  27.554  1.00 26.92 ? 448  SER A C   1 
ATOM   3599 O O   . SER A 1 448 ? 35.655 91.583  28.238  1.00 27.27 ? 448  SER A O   1 
ATOM   3600 C CB  . SER A 1 448 ? 38.640 91.224  27.863  1.00 26.12 ? 448  SER A CB  1 
ATOM   3601 O OG  . SER A 1 448 ? 38.854 90.100  28.719  1.00 29.34 ? 448  SER A OG  1 
ATOM   3602 N N   . ASN A 1 449 ? 35.688 89.496  27.370  1.00 26.32 ? 449  ASN A N   1 
ATOM   3603 C CA  . ASN A 1 449 ? 34.396 89.054  27.927  1.00 25.60 ? 449  ASN A CA  1 
ATOM   3604 C C   . ASN A 1 449 ? 34.731 87.816  28.771  1.00 26.14 ? 449  ASN A C   1 
ATOM   3605 O O   . ASN A 1 449 ? 35.561 86.974  28.351  1.00 25.35 ? 449  ASN A O   1 
ATOM   3606 C CB  . ASN A 1 449 ? 33.479 88.691  26.749  1.00 26.34 ? 449  ASN A CB  1 
ATOM   3607 C CG  . ASN A 1 449 ? 31.970 88.679  27.080  1.00 26.04 ? 449  ASN A CG  1 
ATOM   3608 O OD1 . ASN A 1 449 ? 31.550 88.797  28.214  1.00 26.44 ? 449  ASN A OD1 1 
ATOM   3609 N ND2 . ASN A 1 449 ? 31.161 88.530  26.044  1.00 25.45 ? 449  ASN A ND2 1 
ATOM   3610 N N   . PHE A 1 450 ? 34.154 87.733  29.972  1.00 24.84 ? 450  PHE A N   1 
ATOM   3611 C CA  . PHE A 1 450 ? 34.365 86.587  30.846  1.00 25.49 ? 450  PHE A CA  1 
ATOM   3612 C C   . PHE A 1 450 ? 33.515 85.387  30.418  1.00 26.11 ? 450  PHE A C   1 
ATOM   3613 O O   . PHE A 1 450 ? 33.837 84.250  30.755  1.00 26.86 ? 450  PHE A O   1 
ATOM   3614 C CB  . PHE A 1 450 ? 34.117 86.931  32.320  1.00 24.72 ? 450  PHE A CB  1 
ATOM   3615 C CG  . PHE A 1 450 ? 35.149 87.866  32.929  1.00 24.15 ? 450  PHE A CG  1 
ATOM   3616 C CD1 . PHE A 1 450 ? 36.272 88.277  32.209  1.00 23.76 ? 450  PHE A CD1 1 
ATOM   3617 C CD2 . PHE A 1 450 ? 34.995 88.327  34.238  1.00 23.82 ? 450  PHE A CD2 1 
ATOM   3618 C CE1 . PHE A 1 450 ? 37.239 89.128  32.789  1.00 24.42 ? 450  PHE A CE1 1 
ATOM   3619 C CE2 . PHE A 1 450 ? 35.961 89.182  34.816  1.00 23.34 ? 450  PHE A CE2 1 
ATOM   3620 C CZ  . PHE A 1 450 ? 37.080 89.569  34.083  1.00 22.94 ? 450  PHE A CZ  1 
ATOM   3621 N N   . VAL A 1 451 ? 32.439 85.637  29.681  1.00 26.44 ? 451  VAL A N   1 
ATOM   3622 C CA  . VAL A 1 451 ? 31.717 84.557  28.999  1.00 27.44 ? 451  VAL A CA  1 
ATOM   3623 C C   . VAL A 1 451 ? 32.046 84.554  27.487  1.00 27.93 ? 451  VAL A C   1 
ATOM   3624 O O   . VAL A 1 451 ? 32.506 85.556  26.939  1.00 28.64 ? 451  VAL A O   1 
ATOM   3625 C CB  . VAL A 1 451 ? 30.188 84.685  29.169  1.00 26.94 ? 451  VAL A CB  1 
ATOM   3626 C CG1 . VAL A 1 451 ? 29.780 84.380  30.600  1.00 27.38 ? 451  VAL A CG1 1 
ATOM   3627 C CG2 . VAL A 1 451 ? 29.727 86.077  28.753  1.00 27.36 ? 451  VAL A CG2 1 
ATOM   3628 N N   . ASP A 1 452 ? 31.785 83.440  26.812  1.00 27.45 ? 452  ASP A N   1 
ATOM   3629 C CA  . ASP A 1 452 ? 32.037 83.366  25.395  1.00 26.75 ? 452  ASP A CA  1 
ATOM   3630 C C   . ASP A 1 452 ? 30.863 83.956  24.618  1.00 26.74 ? 452  ASP A C   1 
ATOM   3631 O O   . ASP A 1 452 ? 29.732 83.399  24.596  1.00 26.33 ? 452  ASP A O   1 
ATOM   3632 C CB  . ASP A 1 452 ? 32.332 81.917  24.999  1.00 27.30 ? 452  ASP A CB  1 
ATOM   3633 C CG  . ASP A 1 452 ? 33.650 81.387  25.615  1.00 28.96 ? 452  ASP A CG  1 
ATOM   3634 O OD1 . ASP A 1 452 ? 34.571 82.169  25.906  1.00 29.16 ? 452  ASP A OD1 1 
ATOM   3635 O OD2 . ASP A 1 452 ? 33.782 80.165  25.824  1.00 33.90 ? 452  ASP A OD2 1 
ATOM   3636 N N   . GLY A 1 453 ? 31.115 85.114  24.011  1.00 25.15 ? 453  GLY A N   1 
ATOM   3637 C CA  . GLY A 1 453 ? 30.159 85.762  23.138  1.00 24.24 ? 453  GLY A CA  1 
ATOM   3638 C C   . GLY A 1 453 ? 29.178 86.615  23.902  1.00 25.30 ? 453  GLY A C   1 
ATOM   3639 O O   . GLY A 1 453 ? 29.163 87.828  23.748  1.00 23.96 ? 453  GLY A O   1 
ATOM   3640 N N   . SER A 1 454 ? 28.333 85.974  24.715  1.00 25.49 ? 454  SER A N   1 
ATOM   3641 C CA  . SER A 1 454 ? 27.331 86.695  25.508  1.00 26.00 ? 454  SER A CA  1 
ATOM   3642 C C   . SER A 1 454 ? 26.833 85.735  26.591  1.00 26.68 ? 454  SER A C   1 
ATOM   3643 O O   . SER A 1 454 ? 27.264 84.558  26.640  1.00 26.51 ? 454  SER A O   1 
ATOM   3644 C CB  . SER A 1 454 ? 26.168 87.205  24.639  1.00 25.79 ? 454  SER A CB  1 
ATOM   3645 O OG  . SER A 1 454 ? 25.158 86.207  24.405  1.00 27.31 ? 454  SER A OG  1 
ATOM   3646 N N   . VAL A 1 455 ? 25.933 86.223  27.448  1.00 27.19 ? 455  VAL A N   1 
ATOM   3647 C CA  . VAL A 1 455 ? 25.370 85.382  28.508  1.00 27.65 ? 455  VAL A CA  1 
ATOM   3648 C C   . VAL A 1 455 ? 24.531 84.239  27.938  1.00 28.75 ? 455  VAL A C   1 
ATOM   3649 O O   . VAL A 1 455 ? 24.377 83.221  28.594  1.00 28.72 ? 455  VAL A O   1 
ATOM   3650 C CB  . VAL A 1 455 ? 24.650 86.176  29.656  1.00 27.92 ? 455  VAL A CB  1 
ATOM   3651 C CG1 . VAL A 1 455 ? 25.643 87.034  30.428  1.00 26.39 ? 455  VAL A CG1 1 
ATOM   3652 C CG2 . VAL A 1 455 ? 23.465 87.022  29.136  1.00 27.37 ? 455  VAL A CG2 1 
ATOM   3653 N N   . SER A 1 456 ? 24.049 84.358  26.703  1.00 29.86 ? 456  SER A N   1 
ATOM   3654 C CA  . SER A 1 456 ? 23.387 83.200  26.076  1.00 31.87 ? 456  SER A CA  1 
ATOM   3655 C C   . SER A 1 456 ? 24.226 82.486  25.003  1.00 31.57 ? 456  SER A C   1 
ATOM   3656 O O   . SER A 1 456 ? 23.700 81.741  24.184  1.00 32.52 ? 456  SER A O   1 
ATOM   3657 C CB  . SER A 1 456 ? 21.985 83.560  25.559  1.00 32.17 ? 456  SER A CB  1 
ATOM   3658 O OG  . SER A 1 456 ? 21.969 84.823  24.896  1.00 37.10 ? 456  SER A OG  1 
ATOM   3659 N N   . GLY A 1 457 ? 25.540 82.673  25.043  1.00 31.97 ? 457  GLY A N   1 
ATOM   3660 C CA  . GLY A 1 457 ? 26.413 82.183  23.988  1.00 31.71 ? 457  GLY A CA  1 
ATOM   3661 C C   . GLY A 1 457 ? 26.156 82.855  22.647  1.00 31.96 ? 457  GLY A C   1 
ATOM   3662 O O   . GLY A 1 457 ? 25.690 83.992  22.592  1.00 31.62 ? 457  GLY A O   1 
ATOM   3663 N N   . CYS A 1 458 ? 26.468 82.137  21.563  1.00 32.39 ? 458  CYS A N   1 
ATOM   3664 C CA  . CYS A 1 458 ? 26.339 82.654  20.188  1.00 32.49 ? 458  CYS A CA  1 
ATOM   3665 C C   . CYS A 1 458 ? 25.637 81.660  19.306  1.00 31.56 ? 458  CYS A C   1 
ATOM   3666 O O   . CYS A 1 458 ? 25.990 80.502  19.301  1.00 31.55 ? 458  CYS A O   1 
ATOM   3667 C CB  . CYS A 1 458 ? 27.728 82.886  19.581  1.00 32.02 ? 458  CYS A CB  1 
ATOM   3668 S SG  . CYS A 1 458 ? 28.780 83.967  20.532  1.00 36.27 ? 458  CYS A SG  1 
ATOM   3669 N N   . SER A 1 459 ? 24.672 82.126  18.532  1.00 31.83 ? 459  SER A N   1 
ATOM   3670 C CA  . SER A 1 459 ? 24.029 81.307  17.530  1.00 32.21 ? 459  SER A CA  1 
ATOM   3671 C C   . SER A 1 459 ? 25.030 80.733  16.527  1.00 32.18 ? 459  SER A C   1 
ATOM   3672 O O   . SER A 1 459 ? 26.021 81.399  16.134  1.00 31.65 ? 459  SER A O   1 
ATOM   3673 C CB  . SER A 1 459 ? 23.002 82.140  16.788  1.00 32.23 ? 459  SER A CB  1 
ATOM   3674 O OG  . SER A 1 459 ? 22.271 82.904  17.727  1.00 35.75 ? 459  SER A OG  1 
ATOM   3675 N N   . THR A 1 460 ? 24.790 79.485  16.147  1.00 31.77 ? 460  THR A N   1 
ATOM   3676 C CA  . THR A 1 460 ? 25.543 78.839  15.092  1.00 32.55 ? 460  THR A CA  1 
ATOM   3677 C C   . THR A 1 460 ? 25.175 79.451  13.759  1.00 32.01 ? 460  THR A C   1 
ATOM   3678 O O   . THR A 1 460 ? 23.984 79.488  13.389  1.00 32.63 ? 460  THR A O   1 
ATOM   3679 C CB  . THR A 1 460 ? 25.255 77.365  15.046  1.00 33.01 ? 460  THR A CB  1 
ATOM   3680 O OG1 . THR A 1 460 ? 25.641 76.793  16.298  1.00 35.67 ? 460  THR A OG1 1 
ATOM   3681 C CG2 . THR A 1 460 ? 26.076 76.700  13.897  1.00 33.26 ? 460  THR A CG2 1 
ATOM   3682 N N   . ASN A 1 461 ? 26.182 79.976  13.068  1.00 30.80 ? 461  ASN A N   1 
ATOM   3683 C CA  . ASN A 1 461 ? 26.018 80.641  11.767  1.00 29.63 ? 461  ASN A CA  1 
ATOM   3684 C C   . ASN A 1 461 ? 27.387 80.970  11.153  1.00 29.29 ? 461  ASN A C   1 
ATOM   3685 O O   . ASN A 1 461 ? 28.392 80.731  11.791  1.00 28.98 ? 461  ASN A O   1 
ATOM   3686 C CB  . ASN A 1 461 ? 25.101 81.877  11.859  1.00 28.97 ? 461  ASN A CB  1 
ATOM   3687 C CG  . ASN A 1 461 ? 25.656 82.983  12.752  1.00 30.00 ? 461  ASN A CG  1 
ATOM   3688 O OD1 . ASN A 1 461 ? 26.867 83.217  12.806  1.00 28.07 ? 461  ASN A OD1 1 
ATOM   3689 N ND2 . ASN A 1 461 ? 24.758 83.702  13.426  1.00 25.05 ? 461  ASN A ND2 1 
ATOM   3690 N N   . ASN A 1 462 ? 27.433 81.517  9.936   1.00 28.49 ? 462  ASN A N   1 
ATOM   3691 C CA  . ASN A 1 462 ? 28.717 81.652  9.220   1.00 28.54 ? 462  ASN A CA  1 
ATOM   3692 C C   . ASN A 1 462 ? 29.669 82.732  9.790   1.00 26.90 ? 462  ASN A C   1 
ATOM   3693 O O   . ASN A 1 462 ? 30.864 82.759  9.464   1.00 26.51 ? 462  ASN A O   1 
ATOM   3694 C CB  . ASN A 1 462 ? 28.497 81.858  7.710   1.00 29.19 ? 462  ASN A CB  1 
ATOM   3695 C CG  . ASN A 1 462 ? 27.963 83.246  7.390   1.00 32.56 ? 462  ASN A CG  1 
ATOM   3696 O OD1 . ASN A 1 462 ? 27.065 83.730  8.053   1.00 36.55 ? 462  ASN A OD1 1 
ATOM   3697 N ND2 . ASN A 1 462 ? 28.538 83.900  6.388   1.00 36.41 ? 462  ASN A ND2 1 
ATOM   3698 N N   . LEU A 1 463 ? 29.148 83.598  10.653  1.00 25.67 ? 463  LEU A N   1 
ATOM   3699 C CA  . LEU A 1 463 ? 29.975 84.607  11.338  1.00 24.86 ? 463  LEU A CA  1 
ATOM   3700 C C   . LEU A 1 463 ? 30.610 84.031  12.587  1.00 24.89 ? 463  LEU A C   1 
ATOM   3701 O O   . LEU A 1 463 ? 31.837 84.051  12.724  1.00 23.56 ? 463  LEU A O   1 
ATOM   3702 C CB  . LEU A 1 463 ? 29.177 85.871  11.651  1.00 24.67 ? 463  LEU A CB  1 
ATOM   3703 C CG  . LEU A 1 463 ? 28.521 86.546  10.433  1.00 25.56 ? 463  LEU A CG  1 
ATOM   3704 C CD1 . LEU A 1 463 ? 27.892 87.850  10.828  1.00 27.12 ? 463  LEU A CD1 1 
ATOM   3705 C CD2 . LEU A 1 463 ? 29.496 86.801  9.280   1.00 25.89 ? 463  LEU A CD2 1 
ATOM   3706 N N   . ASN A 1 464 ? 29.792 83.457  13.480  1.00 23.99 ? 464  ASN A N   1 
ATOM   3707 C CA  . ASN A 1 464 ? 30.315 82.817  14.700  1.00 23.97 ? 464  ASN A CA  1 
ATOM   3708 C C   . ASN A 1 464 ? 31.114 81.551  14.426  1.00 22.94 ? 464  ASN A C   1 
ATOM   3709 O O   . ASN A 1 464 ? 32.026 81.216  15.165  1.00 23.20 ? 464  ASN A O   1 
ATOM   3710 C CB  . ASN A 1 464 ? 29.175 82.547  15.695  1.00 23.84 ? 464  ASN A CB  1 
ATOM   3711 C CG  . ASN A 1 464 ? 28.582 83.819  16.230  1.00 25.72 ? 464  ASN A CG  1 
ATOM   3712 O OD1 . ASN A 1 464 ? 27.369 83.984  16.252  1.00 30.88 ? 464  ASN A OD1 1 
ATOM   3713 N ND2 . ASN A 1 464 ? 29.437 84.745  16.633  1.00 24.56 ? 464  ASN A ND2 1 
ATOM   3714 N N   . ASN A 1 465 ? 30.764 80.873  13.340  1.00 22.87 ? 465  ASN A N   1 
ATOM   3715 C CA  . ASN A 1 465 ? 31.334 79.586  12.959  1.00 23.93 ? 465  ASN A CA  1 
ATOM   3716 C C   . ASN A 1 465 ? 31.669 79.589  11.456  1.00 23.72 ? 465  ASN A C   1 
ATOM   3717 O O   . ASN A 1 465 ? 30.899 79.057  10.653  1.00 24.52 ? 465  ASN A O   1 
ATOM   3718 C CB  . ASN A 1 465 ? 30.375 78.438  13.323  1.00 23.52 ? 465  ASN A CB  1 
ATOM   3719 C CG  . ASN A 1 465 ? 29.972 78.469  14.782  1.00 24.77 ? 465  ASN A CG  1 
ATOM   3720 O OD1 . ASN A 1 465 ? 30.637 77.880  15.629  1.00 24.42 ? 465  ASN A OD1 1 
ATOM   3721 N ND2 . ASN A 1 465 ? 28.903 79.197  15.091  1.00 26.88 ? 465  ASN A ND2 1 
ATOM   3722 N N   . PRO A 1 466 ? 32.780 80.258  11.073  1.00 23.24 ? 466  PRO A N   1 
ATOM   3723 C CA  . PRO A 1 466 ? 33.093 80.534  9.650   1.00 22.99 ? 466  PRO A CA  1 
ATOM   3724 C C   . PRO A 1 466 ? 33.698 79.316  8.920   1.00 22.37 ? 466  PRO A C   1 
ATOM   3725 O O   . PRO A 1 466 ? 34.159 78.369  9.571   1.00 22.13 ? 466  PRO A O   1 
ATOM   3726 C CB  . PRO A 1 466 ? 34.154 81.672  9.760   1.00 22.48 ? 466  PRO A CB  1 
ATOM   3727 C CG  . PRO A 1 466 ? 34.927 81.287  10.989  1.00 22.33 ? 466  PRO A CG  1 
ATOM   3728 C CD  . PRO A 1 466 ? 33.795 80.871  11.963  1.00 23.42 ? 466  PRO A CD  1 
ATOM   3729 N N   . PRO A 1 467 ? 33.691 79.319  7.572   1.00 22.48 ? 467  PRO A N   1 
ATOM   3730 C CA  . PRO A 1 467 ? 34.277 78.144  6.879   1.00 22.75 ? 467  PRO A CA  1 
ATOM   3731 C C   . PRO A 1 467 ? 35.724 77.818  7.308   1.00 22.42 ? 467  PRO A C   1 
ATOM   3732 O O   . PRO A 1 467 ? 36.098 76.638  7.366   1.00 23.32 ? 467  PRO A O   1 
ATOM   3733 C CB  . PRO A 1 467 ? 34.236 78.553  5.405   1.00 23.05 ? 467  PRO A CB  1 
ATOM   3734 C CG  . PRO A 1 467 ? 33.146 79.616  5.326   1.00 23.38 ? 467  PRO A CG  1 
ATOM   3735 C CD  . PRO A 1 467 ? 33.113 80.304  6.639   1.00 22.22 ? 467  PRO A CD  1 
ATOM   3736 N N   . PHE A 1 468 ? 36.526 78.848  7.588   1.00 22.05 ? 468  PHE A N   1 
ATOM   3737 C CA  . PHE A 1 468 ? 37.969 78.703  7.943   1.00 21.35 ? 468  PHE A CA  1 
ATOM   3738 C C   . PHE A 1 468 ? 38.244 79.631  9.111   1.00 21.32 ? 468  PHE A C   1 
ATOM   3739 O O   . PHE A 1 468 ? 37.880 80.815  9.075   1.00 20.71 ? 468  PHE A O   1 
ATOM   3740 C CB  . PHE A 1 468 ? 38.908 79.070  6.785   1.00 21.26 ? 468  PHE A CB  1 
ATOM   3741 C CG  . PHE A 1 468 ? 40.384 79.068  7.165   1.00 21.03 ? 468  PHE A CG  1 
ATOM   3742 C CD1 . PHE A 1 468 ? 41.101 77.871  7.223   1.00 20.20 ? 468  PHE A CD1 1 
ATOM   3743 C CD2 . PHE A 1 468 ? 41.024 80.252  7.549   1.00 19.49 ? 468  PHE A CD2 1 
ATOM   3744 C CE1 . PHE A 1 468 ? 42.474 77.860  7.609   1.00 22.88 ? 468  PHE A CE1 1 
ATOM   3745 C CE2 . PHE A 1 468 ? 42.380 80.273  7.913   1.00 18.01 ? 468  PHE A CE2 1 
ATOM   3746 C CZ  . PHE A 1 468 ? 43.115 79.071  7.947   1.00 21.28 ? 468  PHE A CZ  1 
ATOM   3747 N N   . THR A 1 469 ? 38.854 79.088  10.152  1.00 21.13 ? 469  THR A N   1 
ATOM   3748 C CA  . THR A 1 469 ? 39.215 79.875  11.301  1.00 22.37 ? 469  THR A CA  1 
ATOM   3749 C C   . THR A 1 469 ? 40.736 79.861  11.385  1.00 22.10 ? 469  THR A C   1 
ATOM   3750 O O   . THR A 1 469 ? 41.362 78.775  11.440  1.00 22.03 ? 469  THR A O   1 
ATOM   3751 C CB  . THR A 1 469 ? 38.650 79.284  12.606  1.00 23.01 ? 469  THR A CB  1 
ATOM   3752 O OG1 . THR A 1 469 ? 37.294 78.889  12.413  1.00 23.27 ? 469  THR A OG1 1 
ATOM   3753 C CG2 . THR A 1 469 ? 38.742 80.293  13.781  1.00 23.00 ? 469  THR A CG2 1 
ATOM   3754 N N   . PRO A 1 470 ? 41.342 81.055  11.406  1.00 22.14 ? 470  PRO A N   1 
ATOM   3755 C CA  . PRO A 1 470 ? 42.816 81.100  11.631  1.00 22.22 ? 470  PRO A CA  1 
ATOM   3756 C C   . PRO A 1 470 ? 43.151 80.450  12.989  1.00 23.09 ? 470  PRO A C   1 
ATOM   3757 O O   . PRO A 1 470 ? 42.235 80.239  13.799  1.00 23.25 ? 470  PRO A O   1 
ATOM   3758 C CB  . PRO A 1 470 ? 43.133 82.591  11.634  1.00 21.93 ? 470  PRO A CB  1 
ATOM   3759 C CG  . PRO A 1 470 ? 41.954 83.259  10.932  1.00 22.02 ? 470  PRO A CG  1 
ATOM   3760 C CD  . PRO A 1 470 ? 40.744 82.395  11.263  1.00 21.46 ? 470  PRO A CD  1 
ATOM   3761 N N   . ARG A 1 471 ? 44.419 80.140  13.254  1.00 23.08 ? 471  ARG A N   1 
ATOM   3762 C CA  . ARG A 1 471 ? 44.786 79.388  14.458  1.00 24.63 ? 471  ARG A CA  1 
ATOM   3763 C C   . ARG A 1 471 ? 44.870 80.252  15.710  1.00 24.01 ? 471  ARG A C   1 
ATOM   3764 O O   . ARG A 1 471 ? 45.885 80.248  16.407  1.00 24.55 ? 471  ARG A O   1 
ATOM   3765 C CB  . ARG A 1 471 ? 46.098 78.643  14.241  1.00 24.38 ? 471  ARG A CB  1 
ATOM   3766 C CG  . ARG A 1 471 ? 47.293 79.526  13.908  1.00 27.14 ? 471  ARG A CG  1 
ATOM   3767 C CD  . ARG A 1 471 ? 48.573 78.670  13.787  1.00 28.81 ? 471  ARG A CD  1 
ATOM   3768 N NE  . ARG A 1 471 ? 48.460 77.669  12.714  1.00 32.39 ? 471  ARG A NE  1 
ATOM   3769 C CZ  . ARG A 1 471 ? 49.368 76.720  12.476  1.00 36.65 ? 471  ARG A CZ  1 
ATOM   3770 N NH1 . ARG A 1 471 ? 50.481 76.649  13.235  1.00 35.35 ? 471  ARG A NH1 1 
ATOM   3771 N NH2 . ARG A 1 471 ? 49.164 75.853  11.477  1.00 34.74 ? 471  ARG A NH2 1 
ATOM   3772 N N   . ILE A 1 472 ? 43.803 81.012  15.965  1.00 23.71 ? 472  ILE A N   1 
ATOM   3773 C CA  . ILE A 1 472 ? 43.655 81.845  17.148  1.00 23.77 ? 472  ILE A CA  1 
ATOM   3774 C C   . ILE A 1 472 ? 43.472 80.969  18.389  1.00 24.64 ? 472  ILE A C   1 
ATOM   3775 O O   . ILE A 1 472 ? 42.900 79.860  18.303  1.00 24.47 ? 472  ILE A O   1 
ATOM   3776 C CB  . ILE A 1 472 ? 42.408 82.769  17.016  1.00 24.06 ? 472  ILE A CB  1 
ATOM   3777 C CG1 . ILE A 1 472 ? 41.136 81.923  16.861  1.00 23.87 ? 472  ILE A CG1 1 
ATOM   3778 C CG2 . ILE A 1 472 ? 42.566 83.748  15.834  1.00 22.32 ? 472  ILE A CG2 1 
ATOM   3779 C CD1 . ILE A 1 472 ? 39.874 82.699  17.151  1.00 25.72 ? 472  ILE A CD1 1 
ATOM   3780 N N   . LEU A 1 473 ? 43.951 81.464  19.538  1.00 24.23 ? 473  LEU A N   1 
ATOM   3781 C CA  . LEU A 1 473 ? 43.770 80.776  20.816  1.00 23.95 ? 473  LEU A CA  1 
ATOM   3782 C C   . LEU A 1 473 ? 42.345 80.266  21.012  1.00 24.50 ? 473  LEU A C   1 
ATOM   3783 O O   . LEU A 1 473 ? 41.381 81.042  20.880  1.00 24.30 ? 473  LEU A O   1 
ATOM   3784 C CB  . LEU A 1 473 ? 44.166 81.687  21.979  1.00 23.84 ? 473  LEU A CB  1 
ATOM   3785 C CG  . LEU A 1 473 ? 44.234 81.011  23.362  1.00 24.70 ? 473  LEU A CG  1 
ATOM   3786 C CD1 . LEU A 1 473 ? 45.166 79.788  23.369  1.00 23.33 ? 473  LEU A CD1 1 
ATOM   3787 C CD2 . LEU A 1 473 ? 44.636 81.987  24.445  1.00 23.53 ? 473  LEU A CD2 1 
ATOM   3788 N N   . ASP A 1 474 ? 42.234 78.953  21.281  1.00 25.41 ? 474  ASP A N   1 
ATOM   3789 C CA  . ASP A 1 474 ? 40.965 78.236  21.592  1.00 26.74 ? 474  ASP A CA  1 
ATOM   3790 C C   . ASP A 1 474 ? 40.066 77.949  20.389  1.00 26.62 ? 474  ASP A C   1 
ATOM   3791 O O   . ASP A 1 474 ? 39.036 77.268  20.527  1.00 27.43 ? 474  ASP A O   1 
ATOM   3792 C CB  . ASP A 1 474 ? 40.156 78.913  22.723  1.00 27.17 ? 474  ASP A CB  1 
ATOM   3793 C CG  . ASP A 1 474 ? 40.952 79.063  24.015  1.00 29.63 ? 474  ASP A CG  1 
ATOM   3794 O OD1 . ASP A 1 474 ? 41.631 78.096  24.435  1.00 32.56 ? 474  ASP A OD1 1 
ATOM   3795 O OD2 . ASP A 1 474 ? 40.882 80.158  24.630  1.00 32.60 ? 474  ASP A OD2 1 
ATOM   3796 N N   . GLY A 1 475 ? 40.438 78.446  19.212  1.00 25.60 ? 475  GLY A N   1 
ATOM   3797 C CA  . GLY A 1 475 ? 39.815 77.958  17.993  1.00 25.44 ? 475  GLY A CA  1 
ATOM   3798 C C   . GLY A 1 475 ? 38.409 78.450  17.672  1.00 25.22 ? 475  GLY A C   1 
ATOM   3799 O O   . GLY A 1 475 ? 37.848 78.027  16.691  1.00 26.08 ? 475  GLY A O   1 
ATOM   3800 N N   . TYR A 1 476 ? 37.849 79.359  18.463  1.00 24.72 ? 476  TYR A N   1 
ATOM   3801 C CA  . TYR A 1 476 ? 36.582 79.992  18.107  1.00 24.50 ? 476  TYR A CA  1 
ATOM   3802 C C   . TYR A 1 476 ? 36.759 81.474  18.231  1.00 22.99 ? 476  TYR A C   1 
ATOM   3803 O O   . TYR A 1 476 ? 37.252 81.934  19.240  1.00 23.16 ? 476  TYR A O   1 
ATOM   3804 C CB  . TYR A 1 476 ? 35.422 79.592  19.033  1.00 26.28 ? 476  TYR A CB  1 
ATOM   3805 C CG  . TYR A 1 476 ? 35.100 78.129  19.068  1.00 29.53 ? 476  TYR A CG  1 
ATOM   3806 C CD1 . TYR A 1 476 ? 34.100 77.582  18.250  1.00 30.97 ? 476  TYR A CD1 1 
ATOM   3807 C CD2 . TYR A 1 476 ? 35.786 77.282  19.938  1.00 32.29 ? 476  TYR A CD2 1 
ATOM   3808 C CE1 . TYR A 1 476 ? 33.830 76.212  18.288  1.00 32.55 ? 476  TYR A CE1 1 
ATOM   3809 C CE2 . TYR A 1 476 ? 35.526 75.915  19.974  1.00 32.86 ? 476  TYR A CE2 1 
ATOM   3810 C CZ  . TYR A 1 476 ? 34.562 75.398  19.163  1.00 31.75 ? 476  TYR A CZ  1 
ATOM   3811 O OH  . TYR A 1 476 ? 34.341 74.058  19.259  1.00 33.13 ? 476  TYR A OH  1 
ATOM   3812 N N   . LEU A 1 477 ? 36.275 82.216  17.242  1.00 21.61 ? 477  LEU A N   1 
ATOM   3813 C CA  . LEU A 1 477 ? 36.352 83.673  17.226  1.00 20.31 ? 477  LEU A CA  1 
ATOM   3814 C C   . LEU A 1 477 ? 35.723 84.339  18.442  1.00 20.38 ? 477  LEU A C   1 
ATOM   3815 O O   . LEU A 1 477 ? 36.247 85.337  18.932  1.00 19.20 ? 477  LEU A O   1 
ATOM   3816 C CB  . LEU A 1 477 ? 35.735 84.234  15.947  1.00 20.14 ? 477  LEU A CB  1 
ATOM   3817 C CG  . LEU A 1 477 ? 36.305 83.864  14.571  1.00 21.40 ? 477  LEU A CG  1 
ATOM   3818 C CD1 . LEU A 1 477 ? 35.391 84.393  13.463  1.00 16.96 ? 477  LEU A CD1 1 
ATOM   3819 C CD2 . LEU A 1 477 ? 37.694 84.490  14.397  1.00 21.55 ? 477  LEU A CD2 1 
ATOM   3820 N N   . PHE A 1 478 ? 34.610 83.801  18.949  1.00 20.02 ? 478  PHE A N   1 
ATOM   3821 C CA  . PHE A 1 478 ? 33.907 84.485  20.056  1.00 20.63 ? 478  PHE A CA  1 
ATOM   3822 C C   . PHE A 1 478 ? 34.416 84.131  21.448  1.00 21.01 ? 478  PHE A C   1 
ATOM   3823 O O   . PHE A 1 478 ? 33.848 84.588  22.437  1.00 20.52 ? 478  PHE A O   1 
ATOM   3824 C CB  . PHE A 1 478 ? 32.407 84.202  19.972  1.00 21.56 ? 478  PHE A CB  1 
ATOM   3825 C CG  . PHE A 1 478 ? 32.081 82.747  19.907  1.00 20.23 ? 478  PHE A CG  1 
ATOM   3826 C CD1 . PHE A 1 478 ? 31.958 81.997  21.074  1.00 23.78 ? 478  PHE A CD1 1 
ATOM   3827 C CD2 . PHE A 1 478 ? 31.912 82.129  18.682  1.00 19.43 ? 478  PHE A CD2 1 
ATOM   3828 C CE1 . PHE A 1 478 ? 31.639 80.618  21.023  1.00 25.82 ? 478  PHE A CE1 1 
ATOM   3829 C CE2 . PHE A 1 478 ? 31.605 80.774  18.597  1.00 23.27 ? 478  PHE A CE2 1 
ATOM   3830 C CZ  . PHE A 1 478 ? 31.458 80.007  19.765  1.00 24.01 ? 478  PHE A CZ  1 
ATOM   3831 N N   . CYS A 1 479 ? 35.460 83.297  21.519  1.00 22.00 ? 479  CYS A N   1 
ATOM   3832 C CA  A CYS A 1 479 ? 36.068 82.908  22.786  0.50 22.36 ? 479  CYS A CA  1 
ATOM   3833 C CA  B CYS A 1 479 ? 36.080 82.937  22.792  0.50 22.40 ? 479  CYS A CA  1 
ATOM   3834 C C   . CYS A 1 479 ? 36.560 84.149  23.536  1.00 22.45 ? 479  CYS A C   1 
ATOM   3835 O O   . CYS A 1 479 ? 37.381 84.898  23.025  1.00 21.44 ? 479  CYS A O   1 
ATOM   3836 C CB  A CYS A 1 479 ? 37.203 81.910  22.550  0.50 22.65 ? 479  CYS A CB  1 
ATOM   3837 C CB  B CYS A 1 479 ? 37.261 82.020  22.581  0.50 22.75 ? 479  CYS A CB  1 
ATOM   3838 S SG  A CYS A 1 479 ? 38.025 81.294  24.030  0.50 24.17 ? 479  CYS A SG  1 
ATOM   3839 S SG  B CYS A 1 479 ? 36.736 80.391  22.359  0.50 24.37 ? 479  CYS A SG  1 
ATOM   3840 N N   . LYS A 1 480 ? 36.019 84.326  24.742  1.00 22.70 ? 480  LYS A N   1 
ATOM   3841 C CA  . LYS A 1 480 ? 36.327 85.414  25.662  1.00 22.00 ? 480  LYS A CA  1 
ATOM   3842 C C   . LYS A 1 480 ? 36.192 86.792  25.027  1.00 22.16 ? 480  LYS A C   1 
ATOM   3843 O O   . LYS A 1 480 ? 36.949 87.730  25.375  1.00 21.94 ? 480  LYS A O   1 
ATOM   3844 C CB  . LYS A 1 480 ? 37.700 85.210  26.335  1.00 22.62 ? 480  LYS A CB  1 
ATOM   3845 C CG  . LYS A 1 480 ? 37.870 83.862  27.066  1.00 23.56 ? 480  LYS A CG  1 
ATOM   3846 C CD  . LYS A 1 480 ? 36.799 83.575  28.096  1.00 26.29 ? 480  LYS A CD  1 
ATOM   3847 C CE  . LYS A 1 480 ? 37.049 82.221  28.808  1.00 28.55 ? 480  LYS A CE  1 
ATOM   3848 N NZ  . LYS A 1 480 ? 35.830 81.299  28.670  1.00 28.05 ? 480  LYS A NZ  1 
ATOM   3849 N N   . THR A 1 481 ? 35.219 86.931  24.127  1.00 21.18 ? 481  THR A N   1 
ATOM   3850 C CA  . THR A 1 481 ? 34.883 88.247  23.565  1.00 20.59 ? 481  THR A CA  1 
ATOM   3851 C C   . THR A 1 481 ? 33.424 88.273  23.156  1.00 21.18 ? 481  THR A C   1 
ATOM   3852 O O   . THR A 1 481 ? 32.643 87.496  23.685  1.00 20.59 ? 481  THR A O   1 
ATOM   3853 C CB  . THR A 1 481 ? 35.832 88.652  22.364  1.00 21.60 ? 481  THR A CB  1 
ATOM   3854 O OG1 . THR A 1 481 ? 35.549 89.995  21.962  1.00 17.70 ? 481  THR A OG1 1 
ATOM   3855 C CG2 . THR A 1 481 ? 35.695 87.695  21.147  1.00 21.31 ? 481  THR A CG2 1 
ATOM   3856 N N   . LEU A 1 482 ? 33.041 89.151  22.228  1.00 21.82 ? 482  LEU A N   1 
ATOM   3857 C CA  . LEU A 1 482 ? 31.623 89.334  21.860  1.00 22.48 ? 482  LEU A CA  1 
ATOM   3858 C C   . LEU A 1 482 ? 31.254 88.395  20.716  1.00 23.08 ? 482  LEU A C   1 
ATOM   3859 O O   . LEU A 1 482 ? 32.140 87.894  20.009  1.00 22.26 ? 482  LEU A O   1 
ATOM   3860 C CB  . LEU A 1 482 ? 31.315 90.800  21.482  1.00 22.33 ? 482  LEU A CB  1 
ATOM   3861 C CG  . LEU A 1 482 ? 31.689 91.929  22.458  1.00 23.90 ? 482  LEU A CG  1 
ATOM   3862 C CD1 . LEU A 1 482 ? 31.029 93.276  22.028  1.00 26.47 ? 482  LEU A CD1 1 
ATOM   3863 C CD2 . LEU A 1 482 ? 31.322 91.583  23.902  1.00 23.09 ? 482  LEU A CD2 1 
ATOM   3864 N N   . CYS A 1 483 ? 29.944 88.147  20.549  1.00 22.67 ? 483  CYS A N   1 
ATOM   3865 C CA  . CYS A 1 483 ? 29.419 87.412  19.392  1.00 22.85 ? 483  CYS A CA  1 
ATOM   3866 C C   . CYS A 1 483 ? 29.864 88.129  18.127  1.00 22.03 ? 483  CYS A C   1 
ATOM   3867 O O   . CYS A 1 483 ? 29.874 89.353  18.097  1.00 20.52 ? 483  CYS A O   1 
ATOM   3868 C CB  . CYS A 1 483 ? 27.881 87.400  19.435  1.00 23.42 ? 483  CYS A CB  1 
ATOM   3869 S SG  . CYS A 1 483 ? 27.311 86.423  20.799  1.00 29.04 ? 483  CYS A SG  1 
ATOM   3870 N N   . MET A 1 484 ? 30.211 87.355  17.098  1.00 21.61 ? 484  MET A N   1 
ATOM   3871 C CA  . MET A 1 484 ? 30.633 87.885  15.807  1.00 21.25 ? 484  MET A CA  1 
ATOM   3872 C C   . MET A 1 484 ? 29.479 88.537  15.055  1.00 22.21 ? 484  MET A C   1 
ATOM   3873 O O   . MET A 1 484 ? 29.700 89.388  14.174  1.00 21.10 ? 484  MET A O   1 
ATOM   3874 C CB  . MET A 1 484 ? 31.331 86.820  14.964  1.00 21.07 ? 484  MET A CB  1 
ATOM   3875 C CG  . MET A 1 484 ? 32.644 86.314  15.561  1.00 19.51 ? 484  MET A CG  1 
ATOM   3876 S SD  . MET A 1 484 ? 33.903 87.668  15.596  1.00 22.34 ? 484  MET A SD  1 
ATOM   3877 C CE  . MET A 1 484 ? 34.108 87.968  17.340  1.00 18.59 ? 484  MET A CE  1 
ATOM   3878 N N   . ASP A 1 485 ? 28.247 88.191  15.434  1.00 22.21 ? 485  ASP A N   1 
ATOM   3879 C CA  . ASP A 1 485 ? 27.091 88.844  14.828  1.00 23.29 ? 485  ASP A CA  1 
ATOM   3880 C C   . ASP A 1 485 ? 26.557 89.996  15.679  1.00 23.55 ? 485  ASP A C   1 
ATOM   3881 O O   . ASP A 1 485 ? 25.473 90.531  15.406  1.00 23.79 ? 485  ASP A O   1 
ATOM   3882 C CB  . ASP A 1 485 ? 25.988 87.848  14.431  1.00 24.21 ? 485  ASP A CB  1 
ATOM   3883 C CG  . ASP A 1 485 ? 25.562 86.882  15.578  1.00 27.16 ? 485  ASP A CG  1 
ATOM   3884 O OD1 . ASP A 1 485 ? 25.986 86.984  16.764  1.00 27.11 ? 485  ASP A OD1 1 
ATOM   3885 O OD2 . ASP A 1 485 ? 24.776 85.980  15.240  1.00 31.37 ? 485  ASP A OD2 1 
ATOM   3886 N N   . ALA A 1 486 ? 27.322 90.381  16.703  1.00 22.52 ? 486  ALA A N   1 
ATOM   3887 C CA  . ALA A 1 486 ? 27.020 91.593  17.421  1.00 22.78 ? 486  ALA A CA  1 
ATOM   3888 C C   . ALA A 1 486 ? 27.209 92.777  16.476  1.00 24.12 ? 486  ALA A C   1 
ATOM   3889 O O   . ALA A 1 486 ? 27.954 92.712  15.479  1.00 23.70 ? 486  ALA A O   1 
ATOM   3890 C CB  . ALA A 1 486 ? 27.856 91.716  18.636  1.00 22.80 ? 486  ALA A CB  1 
ATOM   3891 N N   . VAL A 1 487 ? 26.493 93.854  16.769  1.00 24.40 ? 487  VAL A N   1 
ATOM   3892 C CA  . VAL A 1 487 ? 26.303 94.895  15.804  1.00 24.80 ? 487  VAL A CA  1 
ATOM   3893 C C   . VAL A 1 487 ? 26.679 96.293  16.371  1.00 24.44 ? 487  VAL A C   1 
ATOM   3894 O O   . VAL A 1 487 ? 26.277 96.659  17.450  1.00 23.16 ? 487  VAL A O   1 
ATOM   3895 C CB  . VAL A 1 487 ? 24.858 94.742  15.248  1.00 26.35 ? 487  VAL A CB  1 
ATOM   3896 C CG1 . VAL A 1 487 ? 24.038 95.987  15.392  1.00 25.96 ? 487  VAL A CG1 1 
ATOM   3897 C CG2 . VAL A 1 487 ? 24.877 94.160  13.836  1.00 26.17 ? 487  VAL A CG2 1 
ATOM   3898 N N   . GLN A 1 488 ? 27.521 97.027  15.640  1.00 24.88 ? 488  GLN A N   1 
ATOM   3899 C CA  . GLN A 1 488 ? 27.945 98.356  15.993  1.00 25.02 ? 488  GLN A CA  1 
ATOM   3900 C C   . GLN A 1 488 ? 27.706 99.343  14.825  1.00 26.06 ? 488  GLN A C   1 
ATOM   3901 O O   . GLN A 1 488 ? 27.319 98.974  13.714  1.00 25.92 ? 488  GLN A O   1 
ATOM   3902 C CB  . GLN A 1 488 ? 29.426 98.326  16.398  1.00 26.26 ? 488  GLN A CB  1 
ATOM   3903 C CG  . GLN A 1 488 ? 29.699 97.678  17.767  1.00 24.99 ? 488  GLN A CG  1 
ATOM   3904 C CD  . GLN A 1 488 ? 31.204 97.640  18.160  1.00 25.77 ? 488  GLN A CD  1 
ATOM   3905 O OE1 . GLN A 1 488 ? 31.800 98.669  18.543  1.00 28.07 ? 488  GLN A OE1 1 
ATOM   3906 N NE2 . GLN A 1 488 ? 31.790 96.458  18.111  1.00 22.92 ? 488  GLN A NE2 1 
ATOM   3907 N N   . HIS A 1 489 ? 27.920 100.614 15.093  1.00 26.83 ? 489  HIS A N   1 
ATOM   3908 C CA  . HIS A 1 489 ? 27.742 101.634 14.093  1.00 28.37 ? 489  HIS A CA  1 
ATOM   3909 C C   . HIS A 1 489 ? 28.648 101.388 12.860  1.00 27.91 ? 489  HIS A C   1 
ATOM   3910 O O   . HIS A 1 489 ? 28.172 101.497 11.739  1.00 28.38 ? 489  HIS A O   1 
ATOM   3911 C CB  . HIS A 1 489 ? 27.930 103.001 14.740  1.00 28.84 ? 489  HIS A CB  1 
ATOM   3912 C CG  . HIS A 1 489 ? 27.663 104.153 13.829  1.00 32.53 ? 489  HIS A CG  1 
ATOM   3913 N ND1 . HIS A 1 489 ? 28.676 104.851 13.198  1.00 36.08 ? 489  HIS A ND1 1 
ATOM   3914 C CD2 . HIS A 1 489 ? 26.505 104.760 13.472  1.00 37.35 ? 489  HIS A CD2 1 
ATOM   3915 C CE1 . HIS A 1 489 ? 28.152 105.825 12.471  1.00 39.07 ? 489  HIS A CE1 1 
ATOM   3916 N NE2 . HIS A 1 489 ? 26.836 105.796 12.625  1.00 41.28 ? 489  HIS A NE2 1 
ATOM   3917 N N   . TRP A 1 490 ? 29.918 101.004 13.058  1.00 27.13 ? 490  TRP A N   1 
ATOM   3918 C CA  . TRP A 1 490 ? 30.792 100.668 11.919  1.00 25.95 ? 490  TRP A CA  1 
ATOM   3919 C C   . TRP A 1 490 ? 30.530 99.336  11.229  1.00 26.02 ? 490  TRP A C   1 
ATOM   3920 O O   . TRP A 1 490 ? 31.074 99.089  10.151  1.00 25.92 ? 490  TRP A O   1 
ATOM   3921 C CB  . TRP A 1 490 ? 32.270 100.736 12.289  1.00 25.37 ? 490  TRP A CB  1 
ATOM   3922 C CG  . TRP A 1 490 ? 32.819 102.106 12.468  1.00 24.65 ? 490  TRP A CG  1 
ATOM   3923 C CD1 . TRP A 1 490 ? 32.225 103.301 12.140  1.00 24.96 ? 490  TRP A CD1 1 
ATOM   3924 C CD2 . TRP A 1 490 ? 34.115 102.435 13.008  1.00 24.10 ? 490  TRP A CD2 1 
ATOM   3925 N NE1 . TRP A 1 490 ? 33.064 104.341 12.472  1.00 24.66 ? 490  TRP A NE1 1 
ATOM   3926 C CE2 . TRP A 1 490 ? 34.221 103.834 13.014  1.00 23.46 ? 490  TRP A CE2 1 
ATOM   3927 C CE3 . TRP A 1 490 ? 35.181 101.667 13.520  1.00 24.74 ? 490  TRP A CE3 1 
ATOM   3928 C CZ2 . TRP A 1 490 ? 35.379 104.499 13.478  1.00 27.37 ? 490  TRP A CZ2 1 
ATOM   3929 C CZ3 . TRP A 1 490 ? 36.312 102.321 13.998  1.00 24.87 ? 490  TRP A CZ3 1 
ATOM   3930 C CH2 . TRP A 1 490 ? 36.405 103.724 13.966  1.00 25.00 ? 490  TRP A CH2 1 
ATOM   3931 N N   . GLY A 1 491 ? 29.740 98.464  11.865  1.00 25.93 ? 491  GLY A N   1 
ATOM   3932 C CA  . GLY A 1 491 ? 29.330 97.222  11.247  1.00 25.97 ? 491  GLY A CA  1 
ATOM   3933 C C   . GLY A 1 491 ? 29.298 96.080  12.231  1.00 25.81 ? 491  GLY A C   1 
ATOM   3934 O O   . GLY A 1 491 ? 29.173 96.287  13.421  1.00 25.42 ? 491  GLY A O   1 
ATOM   3935 N N   . LYS A 1 492 ? 29.411 94.869  11.716  1.00 26.11 ? 492  LYS A N   1 
ATOM   3936 C CA  . LYS A 1 492 ? 29.363 93.664  12.525  1.00 26.92 ? 492  LYS A CA  1 
ATOM   3937 C C   . LYS A 1 492 ? 30.692 93.385  13.205  1.00 26.12 ? 492  LYS A C   1 
ATOM   3938 O O   . LYS A 1 492 ? 31.760 93.650  12.657  1.00 25.77 ? 492  LYS A O   1 
ATOM   3939 C CB  . LYS A 1 492 ? 28.990 92.462  11.646  1.00 28.19 ? 492  LYS A CB  1 
ATOM   3940 C CG  . LYS A 1 492 ? 27.754 92.695  10.842  1.00 33.72 ? 492  LYS A CG  1 
ATOM   3941 C CD  . LYS A 1 492 ? 26.964 91.415  10.539  1.00 41.47 ? 492  LYS A CD  1 
ATOM   3942 C CE  . LYS A 1 492 ? 25.487 91.583  11.014  1.00 44.93 ? 492  LYS A CE  1 
ATOM   3943 N NZ  . LYS A 1 492 ? 25.223 91.056  12.417  1.00 44.76 ? 492  LYS A NZ  1 
ATOM   3944 N N   . GLN A 1 493 ? 30.604 92.807  14.394  1.00 24.94 ? 493  GLN A N   1 
ATOM   3945 C CA  . GLN A 1 493 ? 31.756 92.397  15.181  1.00 23.78 ? 493  GLN A CA  1 
ATOM   3946 C C   . GLN A 1 493 ? 32.740 91.522  14.393  1.00 23.20 ? 493  GLN A C   1 
ATOM   3947 O O   . GLN A 1 493 ? 33.957 91.657  14.543  1.00 22.53 ? 493  GLN A O   1 
ATOM   3948 C CB  . GLN A 1 493 ? 31.255 91.678  16.437  1.00 24.15 ? 493  GLN A CB  1 
ATOM   3949 C CG  . GLN A 1 493 ? 32.301 91.211  17.423  1.00 25.44 ? 493  GLN A CG  1 
ATOM   3950 C CD  . GLN A 1 493 ? 33.002 92.349  18.166  1.00 27.63 ? 493  GLN A CD  1 
ATOM   3951 O OE1 . GLN A 1 493 ? 32.611 93.514  18.078  1.00 27.06 ? 493  GLN A OE1 1 
ATOM   3952 N NE2 . GLN A 1 493 ? 34.050 91.996  18.905  1.00 23.83 ? 493  GLN A NE2 1 
ATOM   3953 N N   . TYR A 1 494 ? 32.220 90.621  13.560  1.00 21.08 ? 494  TYR A N   1 
ATOM   3954 C CA  . TYR A 1 494 ? 33.049 89.845  12.635  1.00 20.43 ? 494  TYR A CA  1 
ATOM   3955 C C   . TYR A 1 494 ? 34.082 90.703  11.878  1.00 20.41 ? 494  TYR A C   1 
ATOM   3956 O O   . TYR A 1 494 ? 35.223 90.271  11.654  1.00 19.24 ? 494  TYR A O   1 
ATOM   3957 C CB  . TYR A 1 494 ? 32.140 89.182  11.616  1.00 19.53 ? 494  TYR A CB  1 
ATOM   3958 C CG  . TYR A 1 494 ? 32.820 88.179  10.726  1.00 19.77 ? 494  TYR A CG  1 
ATOM   3959 C CD1 . TYR A 1 494 ? 33.055 86.872  11.180  1.00 18.18 ? 494  TYR A CD1 1 
ATOM   3960 C CD2 . TYR A 1 494 ? 33.228 88.527  9.432   1.00 18.66 ? 494  TYR A CD2 1 
ATOM   3961 C CE1 . TYR A 1 494 ? 33.657 85.932  10.363  1.00 20.34 ? 494  TYR A CE1 1 
ATOM   3962 C CE2 . TYR A 1 494 ? 33.830 87.597  8.614   1.00 16.55 ? 494  TYR A CE2 1 
ATOM   3963 C CZ  . TYR A 1 494 ? 34.049 86.300  9.086   1.00 18.51 ? 494  TYR A CZ  1 
ATOM   3964 O OH  . TYR A 1 494 ? 34.639 85.350  8.280   1.00 17.90 ? 494  TYR A OH  1 
ATOM   3965 N N   . ASP A 1 495 ? 33.646 91.893  11.453  1.00 20.06 ? 495  ASP A N   1 
ATOM   3966 C CA  . ASP A 1 495 ? 34.461 92.780  10.615  1.00 20.35 ? 495  ASP A CA  1 
ATOM   3967 C C   . ASP A 1 495 ? 35.279 93.789  11.429  1.00 19.96 ? 495  ASP A C   1 
ATOM   3968 O O   . ASP A 1 495 ? 36.345 94.200  11.010  1.00 20.95 ? 495  ASP A O   1 
ATOM   3969 C CB  . ASP A 1 495 ? 33.550 93.576  9.675   1.00 19.73 ? 495  ASP A CB  1 
ATOM   3970 C CG  . ASP A 1 495 ? 33.012 92.746  8.532   1.00 20.52 ? 495  ASP A CG  1 
ATOM   3971 O OD1 . ASP A 1 495 ? 33.682 91.786  8.053   1.00 22.09 ? 495  ASP A OD1 1 
ATOM   3972 O OD2 . ASP A 1 495 ? 31.918 93.106  8.074   1.00 22.56 ? 495  ASP A OD2 1 
ATOM   3973 N N   . ILE A 1 496 ? 34.745 94.229  12.563  1.00 19.38 ? 496  ILE A N   1 
ATOM   3974 C CA  . ILE A 1 496 ? 35.333 95.336  13.304  1.00 19.71 ? 496  ILE A CA  1 
ATOM   3975 C C   . ILE A 1 496 ? 35.837 94.982  14.683  1.00 19.21 ? 496  ILE A C   1 
ATOM   3976 O O   . ILE A 1 496 ? 36.214 95.882  15.442  1.00 21.17 ? 496  ILE A O   1 
ATOM   3977 C CB  . ILE A 1 496 ? 34.356 96.540  13.480  1.00 18.96 ? 496  ILE A CB  1 
ATOM   3978 C CG1 . ILE A 1 496 ? 33.332 96.240  14.569  1.00 19.53 ? 496  ILE A CG1 1 
ATOM   3979 C CG2 . ILE A 1 496 ? 33.784 96.997  12.147  1.00 20.15 ? 496  ILE A CG2 1 
ATOM   3980 C CD1 . ILE A 1 496 ? 32.278 97.272  14.662  1.00 19.45 ? 496  ILE A CD1 1 
ATOM   3981 N N   . HIS A 1 497 ? 35.839 93.702  15.030  1.00 18.74 ? 497  HIS A N   1 
ATOM   3982 C CA  . HIS A 1 497 ? 36.319 93.271  16.328  1.00 18.48 ? 497  HIS A CA  1 
ATOM   3983 C C   . HIS A 1 497 ? 37.733 93.866  16.645  1.00 19.57 ? 497  HIS A C   1 
ATOM   3984 O O   . HIS A 1 497 ? 37.981 94.341  17.766  1.00 21.19 ? 497  HIS A O   1 
ATOM   3985 C CB  . HIS A 1 497 ? 36.395 91.756  16.351  1.00 17.14 ? 497  HIS A CB  1 
ATOM   3986 C CG  . HIS A 1 497 ? 37.106 91.211  17.547  1.00 16.45 ? 497  HIS A CG  1 
ATOM   3987 N ND1 . HIS A 1 497 ? 38.465 90.991  17.568  1.00 19.00 ? 497  HIS A ND1 1 
ATOM   3988 C CD2 . HIS A 1 497 ? 36.652 90.846  18.762  1.00 13.76 ? 497  HIS A CD2 1 
ATOM   3989 C CE1 . HIS A 1 497 ? 38.817 90.495  18.736  1.00 16.12 ? 497  HIS A CE1 1 
ATOM   3990 N NE2 . HIS A 1 497 ? 37.737 90.425  19.489  1.00 20.87 ? 497  HIS A NE2 1 
ATOM   3991 N N   . ASN A 1 498 ? 38.634 93.835  15.667  1.00 19.57 ? 498  ASN A N   1 
ATOM   3992 C CA  . ASN A 1 498 ? 40.038 94.301  15.873  1.00 20.64 ? 498  ASN A CA  1 
ATOM   3993 C C   . ASN A 1 498 ? 40.163 95.815  16.018  1.00 21.01 ? 498  ASN A C   1 
ATOM   3994 O O   . ASN A 1 498 ? 41.217 96.336  16.364  1.00 22.90 ? 498  ASN A O   1 
ATOM   3995 C CB  . ASN A 1 498 ? 40.944 93.808  14.756  1.00 19.20 ? 498  ASN A CB  1 
ATOM   3996 C CG  . ASN A 1 498 ? 41.384 92.378  14.954  1.00 19.73 ? 498  ASN A CG  1 
ATOM   3997 O OD1 . ASN A 1 498 ? 42.036 91.781  14.085  1.00 22.99 ? 498  ASN A OD1 1 
ATOM   3998 N ND2 . ASN A 1 498 ? 41.027 91.814  16.077  1.00 17.38 ? 498  ASN A ND2 1 
ATOM   3999 N N   . LEU A 1 499 ? 39.052 96.501  15.793  1.00 21.37 ? 499  LEU A N   1 
ATOM   4000 C CA  . LEU A 1 499 ? 38.976 97.952  15.877  1.00 21.73 ? 499  LEU A CA  1 
ATOM   4001 C C   . LEU A 1 499 ? 38.356 98.479  17.188  1.00 21.66 ? 499  LEU A C   1 
ATOM   4002 O O   . LEU A 1 499 ? 38.189 99.678  17.328  1.00 21.89 ? 499  LEU A O   1 
ATOM   4003 C CB  . LEU A 1 499 ? 38.156 98.471  14.688  1.00 21.13 ? 499  LEU A CB  1 
ATOM   4004 C CG  . LEU A 1 499 ? 38.678 98.219  13.280  1.00 21.50 ? 499  LEU A CG  1 
ATOM   4005 C CD1 . LEU A 1 499 ? 37.729 98.913  12.282  1.00 21.67 ? 499  LEU A CD1 1 
ATOM   4006 C CD2 . LEU A 1 499 ? 40.058 98.805  13.178  1.00 19.87 ? 499  LEU A CD2 1 
ATOM   4007 N N   . TYR A 1 500 ? 38.011 97.599  18.134  1.00 21.57 ? 500  TYR A N   1 
ATOM   4008 C CA  . TYR A 1 500 ? 37.349 98.032  19.379  1.00 21.10 ? 500  TYR A CA  1 
ATOM   4009 C C   . TYR A 1 500 ? 38.286 98.932  20.221  1.00 20.70 ? 500  TYR A C   1 
ATOM   4010 O O   . TYR A 1 500 ? 37.928 100.062 20.546  1.00 21.14 ? 500  TYR A O   1 
ATOM   4011 C CB  . TYR A 1 500 ? 36.820 96.848  20.210  1.00 20.99 ? 500  TYR A CB  1 
ATOM   4012 C CG  . TYR A 1 500 ? 35.891 97.295  21.337  1.00 23.00 ? 500  TYR A CG  1 
ATOM   4013 C CD1 . TYR A 1 500 ? 34.524 97.222  21.188  1.00 20.02 ? 500  TYR A CD1 1 
ATOM   4014 C CD2 . TYR A 1 500 ? 36.399 97.826  22.538  1.00 20.73 ? 500  TYR A CD2 1 
ATOM   4015 C CE1 . TYR A 1 500 ? 33.651 97.653  22.207  1.00 21.82 ? 500  TYR A CE1 1 
ATOM   4016 C CE2 . TYR A 1 500 ? 35.564 98.238  23.541  1.00 21.60 ? 500  TYR A CE2 1 
ATOM   4017 C CZ  . TYR A 1 500 ? 34.166 98.146  23.368  1.00 22.35 ? 500  TYR A CZ  1 
ATOM   4018 O OH  . TYR A 1 500 ? 33.295 98.579  24.353  1.00 22.21 ? 500  TYR A OH  1 
ATOM   4019 N N   . GLY A 1 501 ? 39.484 98.440  20.543  1.00 20.28 ? 501  GLY A N   1 
ATOM   4020 C CA  . GLY A 1 501 ? 40.438 99.186  21.355  1.00 19.44 ? 501  GLY A CA  1 
ATOM   4021 C C   . GLY A 1 501 ? 40.889 100.454 20.673  1.00 18.72 ? 501  GLY A C   1 
ATOM   4022 O O   . GLY A 1 501 ? 41.105 101.478 21.317  1.00 19.64 ? 501  GLY A O   1 
ATOM   4023 N N   . TYR A 1 502 ? 40.988 100.390 19.355  1.00 18.75 ? 502  TYR A N   1 
ATOM   4024 C CA  . TYR A 1 502 ? 41.284 101.560 18.531  1.00 19.28 ? 502  TYR A CA  1 
ATOM   4025 C C   . TYR A 1 502 ? 40.145 102.620 18.642  1.00 19.41 ? 502  TYR A C   1 
ATOM   4026 O O   . TYR A 1 502 ? 40.395 103.820 18.877  1.00 18.37 ? 502  TYR A O   1 
ATOM   4027 C CB  . TYR A 1 502 ? 41.518 101.078 17.069  1.00 19.12 ? 502  TYR A CB  1 
ATOM   4028 C CG  . TYR A 1 502 ? 41.651 102.145 16.003  1.00 19.73 ? 502  TYR A CG  1 
ATOM   4029 C CD1 . TYR A 1 502 ? 42.827 102.860 15.861  1.00 19.75 ? 502  TYR A CD1 1 
ATOM   4030 C CD2 . TYR A 1 502 ? 40.605 102.404 15.111  1.00 19.19 ? 502  TYR A CD2 1 
ATOM   4031 C CE1 . TYR A 1 502 ? 42.960 103.833 14.885  1.00 21.52 ? 502  TYR A CE1 1 
ATOM   4032 C CE2 . TYR A 1 502 ? 40.721 103.370 14.114  1.00 21.09 ? 502  TYR A CE2 1 
ATOM   4033 C CZ  . TYR A 1 502 ? 41.904 104.083 14.020  1.00 21.64 ? 502  TYR A CZ  1 
ATOM   4034 O OH  . TYR A 1 502 ? 42.061 105.035 13.055  1.00 24.41 ? 502  TYR A OH  1 
ATOM   4035 N N   . SER A 1 503 ? 38.901 102.175 18.518  1.00 18.96 ? 503  SER A N   1 
ATOM   4036 C CA  . SER A 1 503 ? 37.762 103.101 18.547  1.00 20.21 ? 503  SER A CA  1 
ATOM   4037 C C   . SER A 1 503 ? 37.677 103.715 19.953  1.00 20.04 ? 503  SER A C   1 
ATOM   4038 O O   . SER A 1 503 ? 37.372 104.906 20.100  1.00 20.20 ? 503  SER A O   1 
ATOM   4039 C CB  . SER A 1 503 ? 36.451 102.377 18.128  1.00 20.13 ? 503  SER A CB  1 
ATOM   4040 O OG  . SER A 1 503 ? 36.086 101.409 19.105  1.00 22.92 ? 503  SER A OG  1 
ATOM   4041 N N   . MET A 1 504 ? 38.017 102.910 20.961  1.00 19.92 ? 504  MET A N   1 
ATOM   4042 C CA  . MET A 1 504 ? 38.008 103.325 22.355  1.00 20.23 ? 504  MET A CA  1 
ATOM   4043 C C   . MET A 1 504 ? 39.113 104.341 22.695  1.00 20.34 ? 504  MET A C   1 
ATOM   4044 O O   . MET A 1 504 ? 38.853 105.281 23.450  1.00 19.21 ? 504  MET A O   1 
ATOM   4045 C CB  . MET A 1 504 ? 38.052 102.107 23.298  1.00 20.02 ? 504  MET A CB  1 
ATOM   4046 C CG  . MET A 1 504 ? 37.751 102.430 24.766  1.00 20.20 ? 504  MET A CG  1 
ATOM   4047 S SD  . MET A 1 504 ? 38.140 101.092 25.884  1.00 22.07 ? 504  MET A SD  1 
ATOM   4048 C CE  . MET A 1 504 ? 37.786 101.804 27.486  1.00 20.58 ? 504  MET A CE  1 
ATOM   4049 N N   . ALA A 1 505 ? 40.328 104.172 22.145  1.00 20.08 ? 505  ALA A N   1 
ATOM   4050 C CA  . ALA A 1 505 ? 41.380 105.189 22.299  1.00 19.95 ? 505  ALA A CA  1 
ATOM   4051 C C   . ALA A 1 505 ? 41.005 106.500 21.619  1.00 19.90 ? 505  ALA A C   1 
ATOM   4052 O O   . ALA A 1 505 ? 41.325 107.562 22.147  1.00 19.11 ? 505  ALA A O   1 
ATOM   4053 C CB  . ALA A 1 505 ? 42.717 104.705 21.763  1.00 19.95 ? 505  ALA A CB  1 
ATOM   4054 N N   . VAL A 1 506 ? 40.366 106.422 20.442  1.00 20.22 ? 506  VAL A N   1 
ATOM   4055 C CA  . VAL A 1 506 ? 39.898 107.626 19.731  1.00 20.79 ? 506  VAL A CA  1 
ATOM   4056 C C   . VAL A 1 506 ? 38.906 108.413 20.614  1.00 21.49 ? 506  VAL A C   1 
ATOM   4057 O O   . VAL A 1 506 ? 39.114 109.621 20.866  1.00 21.71 ? 506  VAL A O   1 
ATOM   4058 C CB  . VAL A 1 506 ? 39.307 107.285 18.339  1.00 21.15 ? 506  VAL A CB  1 
ATOM   4059 C CG1 . VAL A 1 506 ? 38.672 108.521 17.667  1.00 20.65 ? 506  VAL A CG1 1 
ATOM   4060 C CG2 . VAL A 1 506 ? 40.396 106.693 17.411  1.00 20.92 ? 506  VAL A CG2 1 
ATOM   4061 N N   . ALA A 1 507 ? 37.865 107.718 21.116  1.00 22.20 ? 507  ALA A N   1 
ATOM   4062 C CA  . ALA A 1 507 ? 36.830 108.308 21.990  1.00 21.92 ? 507  ALA A CA  1 
ATOM   4063 C C   . ALA A 1 507 ? 37.404 108.884 23.269  1.00 22.22 ? 507  ALA A C   1 
ATOM   4064 O O   . ALA A 1 507 ? 36.905 109.891 23.760  1.00 23.61 ? 507  ALA A O   1 
ATOM   4065 C CB  . ALA A 1 507 ? 35.743 107.270 22.338  1.00 22.30 ? 507  ALA A CB  1 
ATOM   4066 N N   . THR A 1 508 ? 38.424 108.218 23.817  1.00 21.91 ? 508  THR A N   1 
ATOM   4067 C CA  . THR A 1 508 ? 39.055 108.601 25.058  1.00 22.40 ? 508  THR A CA  1 
ATOM   4068 C C   . THR A 1 508 ? 39.893 109.852 24.858  1.00 23.35 ? 508  THR A C   1 
ATOM   4069 O O   . THR A 1 508 ? 39.868 110.751 25.710  1.00 22.69 ? 508  THR A O   1 
ATOM   4070 C CB  . THR A 1 508 ? 39.915 107.475 25.636  1.00 22.12 ? 508  THR A CB  1 
ATOM   4071 O OG1 . THR A 1 508 ? 39.099 106.320 25.825  1.00 22.65 ? 508  THR A OG1 1 
ATOM   4072 C CG2 . THR A 1 508 ? 40.504 107.888 26.978  1.00 21.83 ? 508  THR A CG2 1 
ATOM   4073 N N   . ALA A 1 509 ? 40.611 109.917 23.733  1.00 23.93 ? 509  ALA A N   1 
ATOM   4074 C CA  . ALA A 1 509 ? 41.258 111.158 23.319  1.00 25.89 ? 509  ALA A CA  1 
ATOM   4075 C C   . ALA A 1 509 ? 40.251 112.298 23.090  1.00 26.78 ? 509  ALA A C   1 
ATOM   4076 O O   . ALA A 1 509 ? 40.542 113.441 23.416  1.00 26.63 ? 509  ALA A O   1 
ATOM   4077 C CB  . ALA A 1 509 ? 42.140 110.951 22.094  1.00 25.56 ? 509  ALA A CB  1 
ATOM   4078 N N   . GLU A 1 510 ? 39.073 111.981 22.544  1.00 28.47 ? 510  GLU A N   1 
ATOM   4079 C CA  . GLU A 1 510 ? 37.979 112.962 22.449  1.00 29.72 ? 510  GLU A CA  1 
ATOM   4080 C C   . GLU A 1 510 ? 37.576 113.507 23.848  1.00 29.46 ? 510  GLU A C   1 
ATOM   4081 O O   . GLU A 1 510 ? 37.491 114.731 24.050  1.00 28.88 ? 510  GLU A O   1 
ATOM   4082 C CB  . GLU A 1 510 ? 36.794 112.348 21.684  1.00 30.57 ? 510  GLU A CB  1 
ATOM   4083 C CG  . GLU A 1 510 ? 35.743 113.323 21.152  1.00 35.68 ? 510  GLU A CG  1 
ATOM   4084 C CD  . GLU A 1 510 ? 36.278 114.338 20.101  1.00 42.09 ? 510  GLU A CD  1 
ATOM   4085 O OE1 . GLU A 1 510 ? 37.428 114.159 19.603  1.00 43.33 ? 510  GLU A OE1 1 
ATOM   4086 O OE2 . GLU A 1 510 ? 35.528 115.316 19.781  1.00 42.59 ? 510  GLU A OE2 1 
ATOM   4087 N N   . ALA A 1 511 ? 37.363 112.601 24.810  1.00 28.77 ? 511  ALA A N   1 
ATOM   4088 C CA  . ALA A 1 511 ? 37.039 112.966 26.194  1.00 27.82 ? 511  ALA A CA  1 
ATOM   4089 C C   . ALA A 1 511 ? 38.088 113.891 26.831  1.00 27.77 ? 511  ALA A C   1 
ATOM   4090 O O   . ALA A 1 511 ? 37.736 114.864 27.515  1.00 26.77 ? 511  ALA A O   1 
ATOM   4091 C CB  . ALA A 1 511 ? 36.847 111.712 27.039  1.00 28.26 ? 511  ALA A CB  1 
ATOM   4092 N N   . ALA A 1 512 ? 39.371 113.589 26.619  1.00 26.64 ? 512  ALA A N   1 
ATOM   4093 C CA  . ALA A 1 512 ? 40.466 114.478 27.064  1.00 26.86 ? 512  ALA A CA  1 
ATOM   4094 C C   . ALA A 1 512 ? 40.361 115.946 26.607  1.00 26.76 ? 512  ALA A C   1 
ATOM   4095 O O   . ALA A 1 512 ? 40.720 116.845 27.369  1.00 27.21 ? 512  ALA A O   1 
ATOM   4096 C CB  . ALA A 1 512 ? 41.878 113.884 26.699  1.00 26.33 ? 512  ALA A CB  1 
ATOM   4097 N N   . LYS A 1 513 ? 39.875 116.194 25.391  1.00 26.84 ? 513  LYS A N   1 
ATOM   4098 C CA  . LYS A 1 513 ? 39.572 117.571 24.928  1.00 28.53 ? 513  LYS A CA  1 
ATOM   4099 C C   . LYS A 1 513 ? 38.637 118.362 25.866  1.00 28.04 ? 513  LYS A C   1 
ATOM   4100 O O   . LYS A 1 513 ? 38.723 119.579 25.936  1.00 28.20 ? 513  LYS A O   1 
ATOM   4101 C CB  . LYS A 1 513 ? 38.950 117.596 23.506  1.00 28.27 ? 513  LYS A CB  1 
ATOM   4102 C CG  . LYS A 1 513 ? 39.722 116.867 22.412  1.00 29.75 ? 513  LYS A CG  1 
ATOM   4103 C CD  . LYS A 1 513 ? 39.100 117.079 21.042  1.00 30.15 ? 513  LYS A CD  1 
ATOM   4104 C CE  . LYS A 1 513 ? 39.905 116.364 19.954  1.00 34.63 ? 513  LYS A CE  1 
ATOM   4105 N NZ  . LYS A 1 513 ? 39.390 116.600 18.561  1.00 36.59 ? 513  LYS A NZ  1 
ATOM   4106 N N   . THR A 1 514 ? 37.732 117.681 26.560  1.00 28.34 ? 514  THR A N   1 
ATOM   4107 C CA  . THR A 1 514 ? 36.798 118.384 27.444  1.00 28.16 ? 514  THR A CA  1 
ATOM   4108 C C   . THR A 1 514 ? 37.346 118.403 28.846  1.00 28.27 ? 514  THR A C   1 
ATOM   4109 O O   . THR A 1 514 ? 37.310 119.429 29.498  1.00 28.31 ? 514  THR A O   1 
ATOM   4110 C CB  . THR A 1 514 ? 35.403 117.738 27.466  1.00 29.10 ? 514  THR A CB  1 
ATOM   4111 O OG1 . THR A 1 514 ? 34.796 117.852 26.174  1.00 29.94 ? 514  THR A OG1 1 
ATOM   4112 C CG2 . THR A 1 514 ? 34.482 118.411 28.537  1.00 28.07 ? 514  THR A CG2 1 
ATOM   4113 N N   . VAL A 1 515 ? 37.866 117.264 29.300  1.00 27.65 ? 515  VAL A N   1 
ATOM   4114 C CA  . VAL A 1 515 ? 38.317 117.098 30.671  1.00 27.68 ? 515  VAL A CA  1 
ATOM   4115 C C   . VAL A 1 515 ? 39.680 117.775 30.938  1.00 26.89 ? 515  VAL A C   1 
ATOM   4116 O O   . VAL A 1 515 ? 39.913 118.295 32.036  1.00 26.66 ? 515  VAL A O   1 
ATOM   4117 C CB  . VAL A 1 515 ? 38.392 115.588 31.017  1.00 27.94 ? 515  VAL A CB  1 
ATOM   4118 C CG1 . VAL A 1 515 ? 38.976 115.352 32.414  1.00 28.54 ? 515  VAL A CG1 1 
ATOM   4119 C CG2 . VAL A 1 515 ? 37.032 114.971 30.900  1.00 29.17 ? 515  VAL A CG2 1 
ATOM   4120 N N   . PHE A 1 516 ? 40.557 117.755 29.939  1.00 25.70 ? 516  PHE A N   1 
ATOM   4121 C CA  . PHE A 1 516 ? 41.896 118.364 30.053  1.00 26.13 ? 516  PHE A CA  1 
ATOM   4122 C C   . PHE A 1 516 ? 42.108 119.370 28.918  1.00 25.74 ? 516  PHE A C   1 
ATOM   4123 O O   . PHE A 1 516 ? 42.912 119.107 28.011  1.00 25.33 ? 516  PHE A O   1 
ATOM   4124 C CB  . PHE A 1 516 ? 43.006 117.266 30.002  1.00 26.09 ? 516  PHE A CB  1 
ATOM   4125 C CG  . PHE A 1 516 ? 42.815 116.157 31.011  1.00 25.43 ? 516  PHE A CG  1 
ATOM   4126 C CD1 . PHE A 1 516 ? 43.080 116.374 32.370  1.00 25.28 ? 516  PHE A CD1 1 
ATOM   4127 C CD2 . PHE A 1 516 ? 42.370 114.893 30.603  1.00 25.05 ? 516  PHE A CD2 1 
ATOM   4128 C CE1 . PHE A 1 516 ? 42.891 115.343 33.306  1.00 27.00 ? 516  PHE A CE1 1 
ATOM   4129 C CE2 . PHE A 1 516 ? 42.172 113.846 31.542  1.00 25.29 ? 516  PHE A CE2 1 
ATOM   4130 C CZ  . PHE A 1 516 ? 42.423 114.074 32.883  1.00 25.45 ? 516  PHE A CZ  1 
ATOM   4131 N N   . PRO A 1 517 ? 41.376 120.517 28.944  1.00 26.07 ? 517  PRO A N   1 
ATOM   4132 C CA  . PRO A 1 517 ? 41.363 121.348 27.733  1.00 26.42 ? 517  PRO A CA  1 
ATOM   4133 C C   . PRO A 1 517 ? 42.781 121.802 27.362  1.00 26.27 ? 517  PRO A C   1 
ATOM   4134 O O   . PRO A 1 517 ? 43.519 122.230 28.241  1.00 25.57 ? 517  PRO A O   1 
ATOM   4135 C CB  . PRO A 1 517 ? 40.477 122.563 28.133  1.00 27.13 ? 517  PRO A CB  1 
ATOM   4136 C CG  . PRO A 1 517 ? 39.693 122.094 29.352  1.00 27.46 ? 517  PRO A CG  1 
ATOM   4137 C CD  . PRO A 1 517 ? 40.558 121.088 30.039  1.00 26.08 ? 517  PRO A CD  1 
ATOM   4138 N N   . ASN A 1 518 ? 43.136 121.659 26.087  1.00 26.24 ? 518  ASN A N   1 
ATOM   4139 C CA  . ASN A 1 518 ? 44.483 121.969 25.534  1.00 26.99 ? 518  ASN A CA  1 
ATOM   4140 C C   . ASN A 1 518 ? 45.683 121.158 26.033  1.00 25.90 ? 518  ASN A C   1 
ATOM   4141 O O   . ASN A 1 518 ? 46.826 121.530 25.756  1.00 25.83 ? 518  ASN A O   1 
ATOM   4142 C CB  . ASN A 1 518 ? 44.815 123.458 25.672  1.00 27.71 ? 518  ASN A CB  1 
ATOM   4143 C CG  . ASN A 1 518 ? 43.778 124.341 24.994  1.00 33.12 ? 518  ASN A CG  1 
ATOM   4144 O OD1 . ASN A 1 518 ? 43.307 124.045 23.867  1.00 37.07 ? 518  ASN A OD1 1 
ATOM   4145 N ND2 . ASN A 1 518 ? 43.388 125.414 25.687  1.00 34.00 ? 518  ASN A ND2 1 
ATOM   4146 N N   . LYS A 1 519 ? 45.439 120.091 26.777  1.00 24.67 ? 519  LYS A N   1 
ATOM   4147 C CA  . LYS A 1 519 ? 46.542 119.272 27.280  1.00 23.85 ? 519  LYS A CA  1 
ATOM   4148 C C   . LYS A 1 519 ? 46.568 117.933 26.590  1.00 23.04 ? 519  LYS A C   1 
ATOM   4149 O O   . LYS A 1 519 ? 45.555 117.464 26.062  1.00 23.56 ? 519  LYS A O   1 
ATOM   4150 C CB  . LYS A 1 519 ? 46.457 119.092 28.799  1.00 24.25 ? 519  LYS A CB  1 
ATOM   4151 C CG  . LYS A 1 519 ? 46.211 120.376 29.591  1.00 24.79 ? 519  LYS A CG  1 
ATOM   4152 C CD  . LYS A 1 519 ? 47.446 121.284 29.612  1.00 28.01 ? 519  LYS A CD  1 
ATOM   4153 C CE  . LYS A 1 519 ? 47.262 122.493 30.549  1.00 29.28 ? 519  LYS A CE  1 
ATOM   4154 N NZ  . LYS A 1 519 ? 48.341 123.513 30.369  1.00 31.12 ? 519  LYS A NZ  1 
ATOM   4155 N N   . ARG A 1 520 ? 47.746 117.327 26.568  1.00 21.89 ? 520  ARG A N   1 
ATOM   4156 C CA  . ARG A 1 520 ? 47.944 115.985 26.041  1.00 20.68 ? 520  ARG A CA  1 
ATOM   4157 C C   . ARG A 1 520 ? 47.374 114.930 26.977  1.00 21.08 ? 520  ARG A C   1 
ATOM   4158 O O   . ARG A 1 520 ? 46.884 113.890 26.517  1.00 22.25 ? 520  ARG A O   1 
ATOM   4159 C CB  . ARG A 1 520 ? 49.454 115.729 25.900  1.00 19.93 ? 520  ARG A CB  1 
ATOM   4160 C CG  . ARG A 1 520 ? 50.120 116.681 24.945  1.00 18.24 ? 520  ARG A CG  1 
ATOM   4161 C CD  . ARG A 1 520 ? 51.642 116.678 25.190  1.00 19.24 ? 520  ARG A CD  1 
ATOM   4162 N NE  . ARG A 1 520 ? 52.227 117.873 24.612  1.00 17.44 ? 520  ARG A NE  1 
ATOM   4163 C CZ  . ARG A 1 520 ? 53.517 118.155 24.654  1.00 19.22 ? 520  ARG A CZ  1 
ATOM   4164 N NH1 . ARG A 1 520 ? 54.375 117.293 25.205  1.00 15.30 ? 520  ARG A NH1 1 
ATOM   4165 N NH2 . ARG A 1 520 ? 53.939 119.289 24.146  1.00 18.22 ? 520  ARG A NH2 1 
ATOM   4166 N N   . SER A 1 521 ? 47.465 115.174 28.291  1.00 21.09 ? 521  SER A N   1 
ATOM   4167 C CA  . SER A 1 521 ? 47.161 114.166 29.289  1.00 20.78 ? 521  SER A CA  1 
ATOM   4168 C C   . SER A 1 521 ? 48.003 112.911 28.988  1.00 21.07 ? 521  SER A C   1 
ATOM   4169 O O   . SER A 1 521 ? 49.120 113.015 28.509  1.00 20.67 ? 521  SER A O   1 
ATOM   4170 C CB  . SER A 1 521 ? 45.655 113.854 29.232  1.00 20.50 ? 521  SER A CB  1 
ATOM   4171 O OG  . SER A 1 521 ? 45.278 112.946 30.253  1.00 23.50 ? 521  SER A OG  1 
ATOM   4172 N N   . PHE A 1 522 ? 47.434 111.730 29.225  1.00 21.17 ? 522  PHE A N   1 
ATOM   4173 C CA  . PHE A 1 522 ? 48.103 110.458 29.007  1.00 20.58 ? 522  PHE A CA  1 
ATOM   4174 C C   . PHE A 1 522 ? 47.030 109.403 28.838  1.00 20.60 ? 522  PHE A C   1 
ATOM   4175 O O   . PHE A 1 522 ? 46.132 109.326 29.671  1.00 20.98 ? 522  PHE A O   1 
ATOM   4176 C CB  . PHE A 1 522 ? 48.980 110.139 30.203  1.00 20.17 ? 522  PHE A CB  1 
ATOM   4177 C CG  . PHE A 1 522 ? 49.617 108.762 30.171  1.00 20.99 ? 522  PHE A CG  1 
ATOM   4178 C CD1 . PHE A 1 522 ? 50.699 108.496 29.351  1.00 20.59 ? 522  PHE A CD1 1 
ATOM   4179 C CD2 . PHE A 1 522 ? 49.159 107.744 31.027  1.00 20.57 ? 522  PHE A CD2 1 
ATOM   4180 C CE1 . PHE A 1 522 ? 51.339 107.208 29.367  1.00 21.85 ? 522  PHE A CE1 1 
ATOM   4181 C CE2 . PHE A 1 522 ? 49.788 106.452 31.048  1.00 22.53 ? 522  PHE A CE2 1 
ATOM   4182 C CZ  . PHE A 1 522 ? 50.880 106.200 30.239  1.00 19.46 ? 522  PHE A CZ  1 
ATOM   4183 N N   . ILE A 1 523 ? 47.081 108.627 27.744  1.00 20.13 ? 523  ILE A N   1 
ATOM   4184 C CA  . ILE A 1 523 ? 46.187 107.478 27.583  1.00 19.24 ? 523  ILE A CA  1 
ATOM   4185 C C   . ILE A 1 523 ? 47.016 106.238 27.366  1.00 19.26 ? 523  ILE A C   1 
ATOM   4186 O O   . ILE A 1 523 ? 47.832 106.218 26.465  1.00 20.39 ? 523  ILE A O   1 
ATOM   4187 C CB  . ILE A 1 523 ? 45.224 107.664 26.424  1.00 19.68 ? 523  ILE A CB  1 
ATOM   4188 C CG1 . ILE A 1 523 ? 44.298 108.870 26.695  1.00 19.88 ? 523  ILE A CG1 1 
ATOM   4189 C CG2 . ILE A 1 523 ? 44.395 106.359 26.167  1.00 19.06 ? 523  ILE A CG2 1 
ATOM   4190 C CD1 . ILE A 1 523 ? 43.740 109.423 25.417  1.00 21.12 ? 523  ILE A CD1 1 
ATOM   4191 N N   . LEU A 1 524 ? 46.818 105.223 28.210  1.00 18.18 ? 524  LEU A N   1 
ATOM   4192 C CA  . LEU A 1 524 ? 47.499 103.947 28.104  1.00 16.62 ? 524  LEU A CA  1 
ATOM   4193 C C   . LEU A 1 524 ? 46.484 102.892 27.691  1.00 17.44 ? 524  LEU A C   1 
ATOM   4194 O O   . LEU A 1 524 ? 45.484 102.651 28.406  1.00 16.99 ? 524  LEU A O   1 
ATOM   4195 C CB  . LEU A 1 524 ? 48.151 103.582 29.432  1.00 15.73 ? 524  LEU A CB  1 
ATOM   4196 C CG  . LEU A 1 524 ? 48.950 102.272 29.503  1.00 17.30 ? 524  LEU A CG  1 
ATOM   4197 C CD1 . LEU A 1 524 ? 50.153 102.311 28.569  1.00 9.09  ? 524  LEU A CD1 1 
ATOM   4198 C CD2 . LEU A 1 524 ? 49.380 101.939 30.929  1.00 14.18 ? 524  LEU A CD2 1 
ATOM   4199 N N   . THR A 1 525 ? 46.713 102.267 26.533  1.00 17.16 ? 525  THR A N   1 
ATOM   4200 C CA  . THR A 1 525 ? 45.754 101.264 26.015  1.00 17.05 ? 525  THR A CA  1 
ATOM   4201 C C   . THR A 1 525 ? 46.375 99.885  25.850  1.00 17.19 ? 525  THR A C   1 
ATOM   4202 O O   . THR A 1 525 ? 47.578 99.776  25.606  1.00 15.98 ? 525  THR A O   1 
ATOM   4203 C CB  . THR A 1 525 ? 45.093 101.707 24.691  1.00 17.08 ? 525  THR A CB  1 
ATOM   4204 O OG1 . THR A 1 525 ? 44.023 100.807 24.382  1.00 18.40 ? 525  THR A OG1 1 
ATOM   4205 C CG2 . THR A 1 525 ? 46.074 101.681 23.544  1.00 17.92 ? 525  THR A CG2 1 
ATOM   4206 N N   . ARG A 1 526 ? 45.550 98.851  26.031  1.00 16.79 ? 526  ARG A N   1 
ATOM   4207 C CA  . ARG A 1 526 ? 45.964 97.480  25.886  1.00 17.45 ? 526  ARG A CA  1 
ATOM   4208 C C   . ARG A 1 526 ? 45.832 97.035  24.435  1.00 18.34 ? 526  ARG A C   1 
ATOM   4209 O O   . ARG A 1 526 ? 46.838 96.756  23.749  1.00 18.77 ? 526  ARG A O   1 
ATOM   4210 C CB  . ARG A 1 526 ? 45.139 96.539  26.790  1.00 16.79 ? 526  ARG A CB  1 
ATOM   4211 C CG  . ARG A 1 526 ? 45.890 95.213  26.965  1.00 16.42 ? 526  ARG A CG  1 
ATOM   4212 C CD  . ARG A 1 526 ? 45.505 94.491  28.196  1.00 19.18 ? 526  ARG A CD  1 
ATOM   4213 N NE  . ARG A 1 526 ? 44.276 93.780  27.906  1.00 19.61 ? 526  ARG A NE  1 
ATOM   4214 C CZ  . ARG A 1 526 ? 43.705 92.964  28.767  1.00 22.04 ? 526  ARG A CZ  1 
ATOM   4215 N NH1 . ARG A 1 526 ? 44.263 92.811  29.958  1.00 21.17 ? 526  ARG A NH1 1 
ATOM   4216 N NH2 . ARG A 1 526 ? 42.606 92.301  28.425  1.00 19.68 ? 526  ARG A NH2 1 
ATOM   4217 N N   . SER A 1 527 ? 44.582 96.963  23.971  1.00 18.14 ? 527  SER A N   1 
ATOM   4218 C CA  . SER A 1 527 ? 44.327 96.626  22.603  1.00 18.79 ? 527  SER A CA  1 
ATOM   4219 C C   . SER A 1 527 ? 44.592 97.800  21.634  1.00 18.33 ? 527  SER A C   1 
ATOM   4220 O O   . SER A 1 527 ? 44.362 98.961  21.955  1.00 18.84 ? 527  SER A O   1 
ATOM   4221 C CB  . SER A 1 527 ? 42.915 96.091  22.463  1.00 19.27 ? 527  SER A CB  1 
ATOM   4222 O OG  . SER A 1 527 ? 42.629 95.960  21.106  1.00 21.34 ? 527  SER A OG  1 
ATOM   4223 N N   . THR A 1 528 ? 45.134 97.475  20.465  1.00 18.83 ? 528  THR A N   1 
ATOM   4224 C CA  . THR A 1 528 ? 45.534 98.454  19.432  1.00 18.21 ? 528  THR A CA  1 
ATOM   4225 C C   . THR A 1 528 ? 45.223 97.913  18.026  1.00 18.20 ? 528  THR A C   1 
ATOM   4226 O O   . THR A 1 528 ? 45.078 96.695  17.818  1.00 18.96 ? 528  THR A O   1 
ATOM   4227 C CB  . THR A 1 528 ? 47.047 98.835  19.486  1.00 18.64 ? 528  THR A CB  1 
ATOM   4228 O OG1 . THR A 1 528 ? 47.856 97.674  19.277  1.00 19.85 ? 528  THR A OG1 1 
ATOM   4229 C CG2 . THR A 1 528 ? 47.435 99.499  20.846  1.00 17.12 ? 528  THR A CG2 1 
ATOM   4230 N N   . PHE A 1 529 ? 45.072 98.841  17.085  1.00 17.43 ? 529  PHE A N   1 
ATOM   4231 C CA  . PHE A 1 529 ? 45.063 98.565  15.675  1.00 17.26 ? 529  PHE A CA  1 
ATOM   4232 C C   . PHE A 1 529 ? 46.159 99.463  15.099  1.00 17.23 ? 529  PHE A C   1 
ATOM   4233 O O   . PHE A 1 529 ? 46.764 100.241 15.832  1.00 18.02 ? 529  PHE A O   1 
ATOM   4234 C CB  . PHE A 1 529 ? 43.700 98.910  15.055  1.00 16.76 ? 529  PHE A CB  1 
ATOM   4235 C CG  . PHE A 1 529 ? 43.535 98.398  13.632  1.00 16.78 ? 529  PHE A CG  1 
ATOM   4236 C CD1 . PHE A 1 529 ? 43.432 97.033  13.381  1.00 16.40 ? 529  PHE A CD1 1 
ATOM   4237 C CD2 . PHE A 1 529 ? 43.523 99.295  12.552  1.00 16.50 ? 529  PHE A CD2 1 
ATOM   4238 C CE1 . PHE A 1 529 ? 43.345 96.549  12.087  1.00 13.66 ? 529  PHE A CE1 1 
ATOM   4239 C CE2 . PHE A 1 529 ? 43.416 98.846  11.260  1.00 16.03 ? 529  PHE A CE2 1 
ATOM   4240 C CZ  . PHE A 1 529 ? 43.324 97.467  11.011  1.00 16.88 ? 529  PHE A CZ  1 
ATOM   4241 N N   . ALA A 1 530 ? 46.400 99.388  13.797  1.00 16.89 ? 530  ALA A N   1 
ATOM   4242 C CA  . ALA A 1 530 ? 47.396 100.269 13.171  1.00 17.23 ? 530  ALA A CA  1 
ATOM   4243 C C   . ALA A 1 530 ? 46.972 101.706 13.257  1.00 16.76 ? 530  ALA A C   1 
ATOM   4244 O O   . ALA A 1 530 ? 45.861 102.054 12.891  1.00 16.52 ? 530  ALA A O   1 
ATOM   4245 C CB  . ALA A 1 530 ? 47.607 99.874  11.738  1.00 17.12 ? 530  ALA A CB  1 
ATOM   4246 N N   . GLY A 1 531 ? 47.866 102.572 13.711  1.00 16.59 ? 531  GLY A N   1 
ATOM   4247 C CA  . GLY A 1 531 ? 47.481 103.963 13.907  1.00 15.09 ? 531  GLY A CA  1 
ATOM   4248 C C   . GLY A 1 531 ? 47.111 104.376 15.327  1.00 15.91 ? 531  GLY A C   1 
ATOM   4249 O O   . GLY A 1 531 ? 46.928 105.560 15.570  1.00 16.08 ? 531  GLY A O   1 
ATOM   4250 N N   . SER A 1 532 ? 47.017 103.421 16.263  1.00 16.44 ? 532  SER A N   1 
ATOM   4251 C CA  . SER A 1 532 ? 46.690 103.685 17.671  1.00 16.99 ? 532  SER A CA  1 
ATOM   4252 C C   . SER A 1 532 ? 47.648 104.611 18.415  1.00 17.31 ? 532  SER A C   1 
ATOM   4253 O O   . SER A 1 532 ? 47.252 105.296 19.380  1.00 16.30 ? 532  SER A O   1 
ATOM   4254 C CB  . SER A 1 532 ? 46.577 102.387 18.468  1.00 17.19 ? 532  SER A CB  1 
ATOM   4255 O OG  . SER A 1 532 ? 45.326 101.751 18.283  1.00 21.23 ? 532  SER A OG  1 
ATOM   4256 N N   . GLY A 1 533 ? 48.910 104.637 17.990  1.00 16.91 ? 533  GLY A N   1 
ATOM   4257 C CA  . GLY A 1 533 ? 49.893 105.516 18.633  1.00 15.94 ? 533  GLY A CA  1 
ATOM   4258 C C   . GLY A 1 533 ? 49.606 106.995 18.450  1.00 16.73 ? 533  GLY A C   1 
ATOM   4259 O O   . GLY A 1 533 ? 50.187 107.851 19.156  1.00 14.70 ? 533  GLY A O   1 
ATOM   4260 N N   . LYS A 1 534 ? 48.750 107.334 17.483  1.00 16.28 ? 534  LYS A N   1 
ATOM   4261 C CA  . LYS A 1 534 ? 48.328 108.731 17.331  1.00 17.14 ? 534  LYS A CA  1 
ATOM   4262 C C   . LYS A 1 534 ? 47.605 109.208 18.585  1.00 18.76 ? 534  LYS A C   1 
ATOM   4263 O O   . LYS A 1 534 ? 47.502 110.411 18.829  1.00 19.84 ? 534  LYS A O   1 
ATOM   4264 C CB  . LYS A 1 534 ? 47.426 108.864 16.114  1.00 17.31 ? 534  LYS A CB  1 
ATOM   4265 C CG  . LYS A 1 534 ? 46.941 110.267 15.802  1.00 18.68 ? 534  LYS A CG  1 
ATOM   4266 C CD  . LYS A 1 534 ? 46.164 110.277 14.485  1.00 20.60 ? 534  LYS A CD  1 
ATOM   4267 C CE  . LYS A 1 534 ? 45.434 111.637 14.256  1.00 24.60 ? 534  LYS A CE  1 
ATOM   4268 N NZ  . LYS A 1 534 ? 44.645 111.658 12.983  1.00 25.19 ? 534  LYS A NZ  1 
ATOM   4269 N N   . PHE A 1 535 ? 47.116 108.256 19.395  1.00 19.02 ? 535  PHE A N   1 
ATOM   4270 C CA  . PHE A 1 535 ? 46.147 108.541 20.470  1.00 18.83 ? 535  PHE A CA  1 
ATOM   4271 C C   . PHE A 1 535 ? 46.615 108.054 21.815  1.00 19.24 ? 535  PHE A C   1 
ATOM   4272 O O   . PHE A 1 535 ? 46.180 108.615 22.800  1.00 20.20 ? 535  PHE A O   1 
ATOM   4273 C CB  . PHE A 1 535 ? 44.759 107.907 20.209  1.00 19.28 ? 535  PHE A CB  1 
ATOM   4274 C CG  . PHE A 1 535 ? 44.130 108.362 18.946  1.00 21.25 ? 535  PHE A CG  1 
ATOM   4275 C CD1 . PHE A 1 535 ? 43.583 109.641 18.841  1.00 22.62 ? 535  PHE A CD1 1 
ATOM   4276 C CD2 . PHE A 1 535 ? 44.129 107.540 17.831  1.00 24.32 ? 535  PHE A CD2 1 
ATOM   4277 C CE1 . PHE A 1 535 ? 43.016 110.075 17.651  1.00 24.39 ? 535  PHE A CE1 1 
ATOM   4278 C CE2 . PHE A 1 535 ? 43.577 107.982 16.613  1.00 23.46 ? 535  PHE A CE2 1 
ATOM   4279 C CZ  . PHE A 1 535 ? 43.017 109.237 16.530  1.00 22.29 ? 535  PHE A CZ  1 
ATOM   4280 N N   . ALA A 1 536 ? 47.498 107.034 21.863  1.00 17.35 ? 536  ALA A N   1 
ATOM   4281 C CA  . ALA A 1 536 ? 47.748 106.309 23.084  1.00 16.68 ? 536  ALA A CA  1 
ATOM   4282 C C   . ALA A 1 536 ? 49.119 105.666 23.198  1.00 16.62 ? 536  ALA A C   1 
ATOM   4283 O O   . ALA A 1 536 ? 49.759 105.336 22.199  1.00 17.08 ? 536  ALA A O   1 
ATOM   4284 C CB  . ALA A 1 536 ? 46.635 105.223 23.296  1.00 16.64 ? 536  ALA A CB  1 
ATOM   4285 N N   . ALA A 1 537 ? 49.553 105.477 24.432  1.00 15.97 ? 537  ALA A N   1 
ATOM   4286 C CA  . ALA A 1 537 ? 50.702 104.620 24.751  1.00 16.66 ? 537  ALA A CA  1 
ATOM   4287 C C   . ALA A 1 537 ? 50.185 103.195 24.888  1.00 16.54 ? 537  ALA A C   1 
ATOM   4288 O O   . ALA A 1 537 ? 48.964 102.985 24.993  1.00 16.40 ? 537  ALA A O   1 
ATOM   4289 C CB  . ALA A 1 537 ? 51.339 105.088 26.089  1.00 16.04 ? 537  ALA A CB  1 
ATOM   4290 N N   . HIS A 1 538 ? 51.093 102.233 24.939  1.00 15.42 ? 538  HIS A N   1 
ATOM   4291 C CA  . HIS A 1 538 ? 50.707 100.836 25.036  1.00 16.40 ? 538  HIS A CA  1 
ATOM   4292 C C   . HIS A 1 538 ? 51.620 100.173 26.067  1.00 16.59 ? 538  HIS A C   1 
ATOM   4293 O O   . HIS A 1 538 ? 52.754 100.613 26.266  1.00 16.01 ? 538  HIS A O   1 
ATOM   4294 C CB  . HIS A 1 538 ? 50.810 100.158 23.656  1.00 16.33 ? 538  HIS A CB  1 
ATOM   4295 C CG  . HIS A 1 538 ? 50.626 98.676  23.688  1.00 19.56 ? 538  HIS A CG  1 
ATOM   4296 N ND1 . HIS A 1 538 ? 49.449 98.072  24.089  1.00 17.94 ? 538  HIS A ND1 1 
ATOM   4297 C CD2 . HIS A 1 538 ? 51.482 97.668  23.376  1.00 21.50 ? 538  HIS A CD2 1 
ATOM   4298 C CE1 . HIS A 1 538 ? 49.579 96.762  23.993  1.00 21.14 ? 538  HIS A CE1 1 
ATOM   4299 N NE2 . HIS A 1 538 ? 50.806 96.490  23.585  1.00 22.79 ? 538  HIS A NE2 1 
ATOM   4300 N N   . TRP A 1 539 ? 51.112 99.148  26.763  1.00 16.50 ? 539  TRP A N   1 
ATOM   4301 C CA  . TRP A 1 539 ? 51.985 98.270  27.517  1.00 15.86 ? 539  TRP A CA  1 
ATOM   4302 C C   . TRP A 1 539 ? 51.800 96.833  27.050  1.00 16.99 ? 539  TRP A C   1 
ATOM   4303 O O   . TRP A 1 539 ? 50.709 96.459  26.552  1.00 17.51 ? 539  TRP A O   1 
ATOM   4304 C CB  . TRP A 1 539 ? 51.813 98.429  29.046  1.00 15.81 ? 539  TRP A CB  1 
ATOM   4305 C CG  . TRP A 1 539 ? 50.788 97.563  29.701  1.00 15.26 ? 539  TRP A CG  1 
ATOM   4306 C CD1 . TRP A 1 539 ? 51.024 96.481  30.510  1.00 16.52 ? 539  TRP A CD1 1 
ATOM   4307 C CD2 . TRP A 1 539 ? 49.349 97.703  29.634  1.00 17.02 ? 539  TRP A CD2 1 
ATOM   4308 N NE1 . TRP A 1 539 ? 49.820 95.947  30.956  1.00 16.10 ? 539  TRP A NE1 1 
ATOM   4309 C CE2 . TRP A 1 539 ? 48.787 96.673  30.428  1.00 15.75 ? 539  TRP A CE2 1 
ATOM   4310 C CE3 . TRP A 1 539 ? 48.487 98.611  28.992  1.00 17.07 ? 539  TRP A CE3 1 
ATOM   4311 C CZ2 . TRP A 1 539 ? 47.405 96.519  30.591  1.00 17.97 ? 539  TRP A CZ2 1 
ATOM   4312 C CZ3 . TRP A 1 539 ? 47.106 98.451  29.146  1.00 15.71 ? 539  TRP A CZ3 1 
ATOM   4313 C CH2 . TRP A 1 539 ? 46.582 97.399  29.936  1.00 13.65 ? 539  TRP A CH2 1 
ATOM   4314 N N   . LEU A 1 540 ? 52.821 96.004  27.269  1.00 15.61 ? 540  LEU A N   1 
ATOM   4315 C CA  . LEU A 1 540 ? 52.851 94.681  26.657  1.00 17.30 ? 540  LEU A CA  1 
ATOM   4316 C C   . LEU A 1 540 ? 51.964 93.633  27.378  1.00 18.83 ? 540  LEU A C   1 
ATOM   4317 O O   . LEU A 1 540 ? 51.944 92.469  26.982  1.00 20.43 ? 540  LEU A O   1 
ATOM   4318 C CB  . LEU A 1 540 ? 54.303 94.189  26.435  1.00 15.37 ? 540  LEU A CB  1 
ATOM   4319 C CG  . LEU A 1 540 ? 55.215 95.148  25.644  1.00 16.24 ? 540  LEU A CG  1 
ATOM   4320 C CD1 . LEU A 1 540 ? 56.638 94.618  25.571  1.00 16.20 ? 540  LEU A CD1 1 
ATOM   4321 C CD2 . LEU A 1 540 ? 54.638 95.302  24.260  1.00 15.73 ? 540  LEU A CD2 1 
ATOM   4322 N N   . GLY A 1 541 ? 51.216 94.059  28.393  1.00 19.29 ? 541  GLY A N   1 
ATOM   4323 C CA  . GLY A 1 541 ? 50.166 93.254  29.010  1.00 19.51 ? 541  GLY A CA  1 
ATOM   4324 C C   . GLY A 1 541 ? 50.598 92.429  30.229  1.00 19.62 ? 541  GLY A C   1 
ATOM   4325 O O   . GLY A 1 541 ? 51.603 92.729  30.889  1.00 18.34 ? 541  GLY A O   1 
ATOM   4326 N N   . ASP A 1 542 ? 49.836 91.365  30.497  1.00 18.65 ? 542  ASP A N   1 
ATOM   4327 C CA  . ASP A 1 542 ? 50.012 90.539  31.700  1.00 18.78 ? 542  ASP A CA  1 
ATOM   4328 C C   . ASP A 1 542 ? 51.145 89.522  31.547  1.00 17.91 ? 542  ASP A C   1 
ATOM   4329 O O   . ASP A 1 542 ? 50.902 88.338  31.297  1.00 17.53 ? 542  ASP A O   1 
ATOM   4330 C CB  . ASP A 1 542 ? 48.712 89.796  32.028  1.00 17.69 ? 542  ASP A CB  1 
ATOM   4331 C CG  . ASP A 1 542 ? 47.511 90.733  32.154  1.00 21.95 ? 542  ASP A CG  1 
ATOM   4332 O OD1 . ASP A 1 542 ? 47.738 91.956  32.366  1.00 22.30 ? 542  ASP A OD1 1 
ATOM   4333 O OD2 . ASP A 1 542 ? 46.338 90.244  32.019  1.00 23.02 ? 542  ASP A OD2 1 
ATOM   4334 N N   . ASN A 1 543 ? 52.379 89.978  31.709  1.00 17.70 ? 543  ASN A N   1 
ATOM   4335 C CA  . ASN A 1 543 ? 53.516 89.091  31.694  1.00 17.49 ? 543  ASN A CA  1 
ATOM   4336 C C   . ASN A 1 543 ? 53.690 88.389  33.062  1.00 18.64 ? 543  ASN A C   1 
ATOM   4337 O O   . ASN A 1 543 ? 52.798 88.430  33.917  1.00 17.98 ? 543  ASN A O   1 
ATOM   4338 C CB  . ASN A 1 543 ? 54.794 89.876  31.256  1.00 17.56 ? 543  ASN A CB  1 
ATOM   4339 C CG  . ASN A 1 543 ? 55.154 90.978  32.232  1.00 17.65 ? 543  ASN A CG  1 
ATOM   4340 O OD1 . ASN A 1 543 ? 54.421 91.217  33.191  1.00 19.21 ? 543  ASN A OD1 1 
ATOM   4341 N ND2 . ASN A 1 543 ? 56.287 91.647  32.013  1.00 16.42 ? 543  ASN A ND2 1 
ATOM   4342 N N   . THR A 1 544 ? 54.861 87.780  33.273  1.00 18.74 ? 544  THR A N   1 
ATOM   4343 C CA  . THR A 1 544 ? 55.107 86.907  34.404  1.00 19.84 ? 544  THR A CA  1 
ATOM   4344 C C   . THR A 1 544 ? 56.497 87.193  34.921  1.00 19.39 ? 544  THR A C   1 
ATOM   4345 O O   . THR A 1 544 ? 57.344 87.558  34.147  1.00 19.67 ? 544  THR A O   1 
ATOM   4346 C CB  . THR A 1 544 ? 55.034 85.435  33.947  1.00 20.05 ? 544  THR A CB  1 
ATOM   4347 O OG1 . THR A 1 544 ? 53.779 85.253  33.270  1.00 24.11 ? 544  THR A OG1 1 
ATOM   4348 C CG2 . THR A 1 544 ? 55.085 84.500  35.128  1.00 17.92 ? 544  THR A CG2 1 
ATOM   4349 N N   . ALA A 1 545 ? 56.735 87.050  36.224  1.00 19.92 ? 545  ALA A N   1 
ATOM   4350 C CA  . ALA A 1 545 ? 58.064 87.319  36.757  1.00 19.89 ? 545  ALA A CA  1 
ATOM   4351 C C   . ALA A 1 545 ? 58.994 86.154  36.449  1.00 20.14 ? 545  ALA A C   1 
ATOM   4352 O O   . ALA A 1 545 ? 59.389 85.433  37.373  1.00 20.06 ? 545  ALA A O   1 
ATOM   4353 C CB  . ALA A 1 545 ? 58.007 87.582  38.270  1.00 19.71 ? 545  ALA A CB  1 
ATOM   4354 N N   . THR A 1 546 ? 59.356 85.989  35.170  1.00 19.59 ? 546  THR A N   1 
ATOM   4355 C CA  . THR A 1 546 ? 60.393 85.005  34.755  1.00 19.82 ? 546  THR A CA  1 
ATOM   4356 C C   . THR A 1 546 ? 61.516 85.691  33.957  1.00 20.35 ? 546  THR A C   1 
ATOM   4357 O O   . THR A 1 546 ? 61.316 86.762  33.389  1.00 20.31 ? 546  THR A O   1 
ATOM   4358 C CB  . THR A 1 546 ? 59.821 83.842  33.878  1.00 20.41 ? 546  THR A CB  1 
ATOM   4359 O OG1 . THR A 1 546 ? 59.351 84.362  32.642  1.00 20.93 ? 546  THR A OG1 1 
ATOM   4360 C CG2 . THR A 1 546 ? 58.651 83.072  34.536  1.00 19.58 ? 546  THR A CG2 1 
ATOM   4361 N N   . TRP A 1 547 ? 62.699 85.076  33.910  1.00 21.01 ? 547  TRP A N   1 
ATOM   4362 C CA  . TRP A 1 547 ? 63.794 85.524  33.030  1.00 20.82 ? 547  TRP A CA  1 
ATOM   4363 C C   . TRP A 1 547 ? 63.461 85.510  31.517  1.00 21.58 ? 547  TRP A C   1 
ATOM   4364 O O   . TRP A 1 547 ? 63.950 86.384  30.751  1.00 21.30 ? 547  TRP A O   1 
ATOM   4365 C CB  . TRP A 1 547 ? 65.061 84.731  33.356  1.00 21.87 ? 547  TRP A CB  1 
ATOM   4366 C CG  . TRP A 1 547 ? 65.542 85.076  34.733  1.00 20.07 ? 547  TRP A CG  1 
ATOM   4367 C CD1 . TRP A 1 547 ? 65.174 84.481  35.923  1.00 21.92 ? 547  TRP A CD1 1 
ATOM   4368 C CD2 . TRP A 1 547 ? 66.435 86.132  35.072  1.00 21.90 ? 547  TRP A CD2 1 
ATOM   4369 N NE1 . TRP A 1 547 ? 65.820 85.097  36.981  1.00 20.93 ? 547  TRP A NE1 1 
ATOM   4370 C CE2 . TRP A 1 547 ? 66.600 86.112  36.480  1.00 20.98 ? 547  TRP A CE2 1 
ATOM   4371 C CE3 . TRP A 1 547 ? 67.130 87.087  34.322  1.00 19.28 ? 547  TRP A CE3 1 
ATOM   4372 C CZ2 . TRP A 1 547 ? 67.418 87.017  37.141  1.00 21.11 ? 547  TRP A CZ2 1 
ATOM   4373 C CZ3 . TRP A 1 547 ? 67.960 87.973  34.982  1.00 22.22 ? 547  TRP A CZ3 1 
ATOM   4374 C CH2 . TRP A 1 547 ? 68.085 87.947  36.376  1.00 21.91 ? 547  TRP A CH2 1 
ATOM   4375 N N   . ASP A 1 548 ? 62.606 84.553  31.105  1.00 20.81 ? 548  ASP A N   1 
ATOM   4376 C CA  . ASP A 1 548 ? 62.064 84.497  29.748  1.00 20.89 ? 548  ASP A CA  1 
ATOM   4377 C C   . ASP A 1 548 ? 61.254 85.755  29.445  1.00 19.88 ? 548  ASP A C   1 
ATOM   4378 O O   . ASP A 1 548 ? 61.458 86.363  28.398  1.00 20.03 ? 548  ASP A O   1 
ATOM   4379 C CB  . ASP A 1 548 ? 61.158 83.267  29.534  1.00 21.07 ? 548  ASP A CB  1 
ATOM   4380 C CG  . ASP A 1 548 ? 61.932 82.007  29.143  1.00 23.96 ? 548  ASP A CG  1 
ATOM   4381 O OD1 . ASP A 1 548 ? 63.086 82.062  28.665  1.00 24.83 ? 548  ASP A OD1 1 
ATOM   4382 O OD2 . ASP A 1 548 ? 61.352 80.934  29.306  1.00 25.53 ? 548  ASP A OD2 1 
ATOM   4383 N N   . ASP A 1 549 ? 60.314 86.130  30.321  1.00 20.04 ? 549  ASP A N   1 
ATOM   4384 C CA  . ASP A 1 549 ? 59.569 87.388  30.106  1.00 19.63 ? 549  ASP A CA  1 
ATOM   4385 C C   . ASP A 1 549 ? 60.451 88.635  30.028  1.00 19.92 ? 549  ASP A C   1 
ATOM   4386 O O   . ASP A 1 549 ? 60.160 89.516  29.215  1.00 20.52 ? 549  ASP A O   1 
ATOM   4387 C CB  . ASP A 1 549 ? 58.431 87.603  31.098  1.00 19.53 ? 549  ASP A CB  1 
ATOM   4388 C CG  . ASP A 1 549 ? 57.327 86.562  30.959  1.00 20.98 ? 549  ASP A CG  1 
ATOM   4389 O OD1 . ASP A 1 549 ? 56.204 86.864  30.531  1.00 20.02 ? 549  ASP A OD1 1 
ATOM   4390 O OD2 . ASP A 1 549 ? 57.594 85.414  31.299  1.00 23.56 ? 549  ASP A OD2 1 
ATOM   4391 N N   . LEU A 1 550 ? 61.494 88.719  30.856  1.00 19.17 ? 550  LEU A N   1 
ATOM   4392 C CA  . LEU A 1 550 ? 62.488 89.812  30.730  1.00 18.89 ? 550  LEU A CA  1 
ATOM   4393 C C   . LEU A 1 550 ? 63.098 89.863  29.320  1.00 19.19 ? 550  LEU A C   1 
ATOM   4394 O O   . LEU A 1 550 ? 63.058 90.918  28.663  1.00 19.59 ? 550  LEU A O   1 
ATOM   4395 C CB  . LEU A 1 550 ? 63.564 89.707  31.831  1.00 18.15 ? 550  LEU A CB  1 
ATOM   4396 C CG  . LEU A 1 550 ? 64.783 90.644  31.788  1.00 19.97 ? 550  LEU A CG  1 
ATOM   4397 C CD1 . LEU A 1 550 ? 64.318 92.070  31.935  1.00 24.59 ? 550  LEU A CD1 1 
ATOM   4398 C CD2 . LEU A 1 550 ? 65.773 90.312  32.874  1.00 18.85 ? 550  LEU A CD2 1 
ATOM   4399 N N   . ARG A 1 551 ? 63.629 88.734  28.830  1.00 19.67 ? 551  ARG A N   1 
ATOM   4400 C CA  . ARG A 1 551 ? 64.238 88.695  27.487  1.00 20.18 ? 551  ARG A CA  1 
ATOM   4401 C C   . ARG A 1 551 ? 63.260 89.104  26.390  1.00 20.35 ? 551  ARG A C   1 
ATOM   4402 O O   . ARG A 1 551 ? 63.604 89.912  25.501  1.00 21.56 ? 551  ARG A O   1 
ATOM   4403 C CB  . ARG A 1 551 ? 64.874 87.325  27.186  1.00 19.66 ? 551  ARG A CB  1 
ATOM   4404 C CG  . ARG A 1 551 ? 66.098 87.097  28.048  1.00 19.75 ? 551  ARG A CG  1 
ATOM   4405 C CD  . ARG A 1 551 ? 66.815 85.745  27.770  1.00 22.29 ? 551  ARG A CD  1 
ATOM   4406 N NE  . ARG A 1 551 ? 66.038 84.595  28.248  1.00 25.50 ? 551  ARG A NE  1 
ATOM   4407 C CZ  . ARG A 1 551 ? 66.179 84.017  29.448  1.00 26.00 ? 551  ARG A CZ  1 
ATOM   4408 N NH1 . ARG A 1 551 ? 67.054 84.483  30.339  1.00 26.51 ? 551  ARG A NH1 1 
ATOM   4409 N NH2 . ARG A 1 551 ? 65.434 82.964  29.767  1.00 21.62 ? 551  ARG A NH2 1 
ATOM   4410 N N   . TRP A 1 552 ? 62.044 88.571  26.473  1.00 18.79 ? 552  TRP A N   1 
ATOM   4411 C CA  . TRP A 1 552 ? 61.051 88.733  25.431  1.00 19.71 ? 552  TRP A CA  1 
ATOM   4412 C C   . TRP A 1 552 ? 60.557 90.134  25.305  1.00 19.34 ? 552  TRP A C   1 
ATOM   4413 O O   . TRP A 1 552 ? 59.984 90.472  24.271  1.00 19.63 ? 552  TRP A O   1 
ATOM   4414 C CB  . TRP A 1 552 ? 59.832 87.829  25.683  1.00 19.39 ? 552  TRP A CB  1 
ATOM   4415 C CG  . TRP A 1 552 ? 60.156 86.380  25.595  1.00 21.14 ? 552  TRP A CG  1 
ATOM   4416 C CD1 . TRP A 1 552 ? 61.224 85.807  24.935  1.00 21.08 ? 552  TRP A CD1 1 
ATOM   4417 C CD2 . TRP A 1 552 ? 59.419 85.298  26.186  1.00 20.43 ? 552  TRP A CD2 1 
ATOM   4418 N NE1 . TRP A 1 552 ? 61.187 84.450  25.111  1.00 21.79 ? 552  TRP A NE1 1 
ATOM   4419 C CE2 . TRP A 1 552 ? 60.075 84.112  25.837  1.00 18.44 ? 552  TRP A CE2 1 
ATOM   4420 C CE3 . TRP A 1 552 ? 58.256 85.228  26.972  1.00 22.20 ? 552  TRP A CE3 1 
ATOM   4421 C CZ2 . TRP A 1 552 ? 59.617 82.854  26.239  1.00 21.57 ? 552  TRP A CZ2 1 
ATOM   4422 C CZ3 . TRP A 1 552 ? 57.803 83.974  27.385  1.00 21.42 ? 552  TRP A CZ3 1 
ATOM   4423 C CH2 . TRP A 1 552 ? 58.491 82.806  27.014  1.00 21.04 ? 552  TRP A CH2 1 
ATOM   4424 N N   . SER A 1 553 ? 60.773 90.941  26.347  1.00 19.13 ? 553  SER A N   1 
ATOM   4425 C CA  . SER A 1 553 ? 60.292 92.319  26.363  1.00 19.18 ? 553  SER A CA  1 
ATOM   4426 C C   . SER A 1 553 ? 60.928 93.174  25.259  1.00 18.59 ? 553  SER A C   1 
ATOM   4427 O O   . SER A 1 553 ? 60.276 94.072  24.719  1.00 17.80 ? 553  SER A O   1 
ATOM   4428 C CB  . SER A 1 553 ? 60.518 92.969  27.738  1.00 19.95 ? 553  SER A CB  1 
ATOM   4429 O OG  . SER A 1 553 ? 61.885 93.201  27.998  1.00 16.97 ? 553  SER A OG  1 
ATOM   4430 N N   . ILE A 1 554 ? 62.200 92.920  24.953  1.00 18.10 ? 554  ILE A N   1 
ATOM   4431 C CA  . ILE A 1 554 ? 62.930 93.810  24.042  1.00 17.83 ? 554  ILE A CA  1 
ATOM   4432 C C   . ILE A 1 554 ? 62.369 93.768  22.604  1.00 18.03 ? 554  ILE A C   1 
ATOM   4433 O O   . ILE A 1 554 ? 62.004 94.816  22.065  1.00 18.66 ? 554  ILE A O   1 
ATOM   4434 C CB  . ILE A 1 554 ? 64.512 93.689  24.136  1.00 18.93 ? 554  ILE A CB  1 
ATOM   4435 C CG1 . ILE A 1 554 ? 65.010 94.023  25.567  1.00 18.79 ? 554  ILE A CG1 1 
ATOM   4436 C CG2 . ILE A 1 554 ? 65.155 94.646  23.108  1.00 15.81 ? 554  ILE A CG2 1 
ATOM   4437 C CD1 . ILE A 1 554 ? 66.504 93.703  25.867  1.00 19.30 ? 554  ILE A CD1 1 
ATOM   4438 N N   . PRO A 1 555 ? 62.278 92.565  21.977  1.00 18.09 ? 555  PRO A N   1 
ATOM   4439 C CA  . PRO A 1 555 ? 61.607 92.532  20.670  1.00 17.93 ? 555  PRO A CA  1 
ATOM   4440 C C   . PRO A 1 555 ? 60.207 93.190  20.689  1.00 17.63 ? 555  PRO A C   1 
ATOM   4441 O O   . PRO A 1 555 ? 59.879 93.917  19.760  1.00 16.45 ? 555  PRO A O   1 
ATOM   4442 C CB  . PRO A 1 555 ? 61.499 91.034  20.367  1.00 18.24 ? 555  PRO A CB  1 
ATOM   4443 C CG  . PRO A 1 555 ? 62.655 90.421  21.090  1.00 17.63 ? 555  PRO A CG  1 
ATOM   4444 C CD  . PRO A 1 555 ? 62.811 91.232  22.353  1.00 17.73 ? 555  PRO A CD  1 
ATOM   4445 N N   . GLY A 1 556 ? 59.415 92.961  21.738  1.00 18.21 ? 556  GLY A N   1 
ATOM   4446 C CA  . GLY A 1 556 ? 58.044 93.569  21.856  1.00 16.81 ? 556  GLY A CA  1 
ATOM   4447 C C   . GLY A 1 556 ? 58.090 95.104  21.878  1.00 17.37 ? 556  GLY A C   1 
ATOM   4448 O O   . GLY A 1 556 ? 57.293 95.764  21.234  1.00 18.45 ? 556  GLY A O   1 
ATOM   4449 N N   . VAL A 1 557 ? 59.030 95.681  22.632  1.00 16.03 ? 557  VAL A N   1 
ATOM   4450 C CA  . VAL A 1 557 ? 59.264 97.132  22.603  1.00 14.10 ? 557  VAL A CA  1 
ATOM   4451 C C   . VAL A 1 557 ? 59.717 97.664  21.214  1.00 13.95 ? 557  VAL A C   1 
ATOM   4452 O O   . VAL A 1 557 ? 59.228 98.692  20.739  1.00 13.75 ? 557  VAL A O   1 
ATOM   4453 C CB  . VAL A 1 557 ? 60.275 97.534  23.709  1.00 14.14 ? 557  VAL A CB  1 
ATOM   4454 C CG1 . VAL A 1 557 ? 60.756 98.987  23.523  1.00 14.87 ? 557  VAL A CG1 1 
ATOM   4455 C CG2 . VAL A 1 557 ? 59.689 97.357  25.078  1.00 12.72 ? 557  VAL A CG2 1 
ATOM   4456 N N   . LEU A 1 558 ? 60.636 96.949  20.554  1.00 13.42 ? 558  LEU A N   1 
ATOM   4457 C CA  . LEU A 1 558 ? 61.143 97.373  19.257  1.00 13.89 ? 558  LEU A CA  1 
ATOM   4458 C C   . LEU A 1 558 ? 60.099 97.333  18.194  1.00 14.89 ? 558  LEU A C   1 
ATOM   4459 O O   . LEU A 1 558 ? 60.016 98.247  17.402  1.00 15.25 ? 558  LEU A O   1 
ATOM   4460 C CB  . LEU A 1 558 ? 62.330 96.499  18.808  1.00 13.31 ? 558  LEU A CB  1 
ATOM   4461 C CG  . LEU A 1 558 ? 63.593 96.624  19.657  1.00 12.19 ? 558  LEU A CG  1 
ATOM   4462 C CD1 . LEU A 1 558 ? 64.639 95.668  19.117  1.00 12.08 ? 558  LEU A CD1 1 
ATOM   4463 C CD2 . LEU A 1 558 ? 64.076 98.056  19.725  1.00 13.62 ? 558  LEU A CD2 1 
ATOM   4464 N N   . GLU A 1 559 ? 59.291 96.272  18.190  1.00 15.13 ? 559  GLU A N   1 
ATOM   4465 C CA  . GLU A 1 559 ? 58.182 96.147  17.258  1.00 16.74 ? 559  GLU A CA  1 
ATOM   4466 C C   . GLU A 1 559 ? 57.142 97.259  17.396  1.00 16.49 ? 559  GLU A C   1 
ATOM   4467 O O   . GLU A 1 559 ? 56.646 97.779  16.380  1.00 17.91 ? 559  GLU A O   1 
ATOM   4468 C CB  . GLU A 1 559 ? 57.552 94.746  17.389  1.00 17.98 ? 559  GLU A CB  1 
ATOM   4469 C CG  . GLU A 1 559 ? 58.509 93.599  16.960  1.00 18.44 ? 559  GLU A CG  1 
ATOM   4470 C CD  . GLU A 1 559 ? 58.199 92.224  17.584  1.00 19.59 ? 559  GLU A CD  1 
ATOM   4471 O OE1 . GLU A 1 559 ? 57.294 92.123  18.473  1.00 20.04 ? 559  GLU A OE1 1 
ATOM   4472 O OE2 . GLU A 1 559 ? 58.869 91.239  17.157  1.00 19.29 ? 559  GLU A OE2 1 
ATOM   4473 N N   . PHE A 1 560 ? 56.782 97.654  18.624  1.00 15.88 ? 560  PHE A N   1 
ATOM   4474 C CA  . PHE A 1 560 ? 55.770 98.701  18.756  1.00 14.08 ? 560  PHE A CA  1 
ATOM   4475 C C   . PHE A 1 560 ? 56.293 100.055 18.330  1.00 14.47 ? 560  PHE A C   1 
ATOM   4476 O O   . PHE A 1 560 ? 55.521 100.936 17.923  1.00 12.50 ? 560  PHE A O   1 
ATOM   4477 C CB  . PHE A 1 560 ? 55.129 98.699  20.145  1.00 14.46 ? 560  PHE A CB  1 
ATOM   4478 C CG  . PHE A 1 560 ? 53.939 97.776  20.203  1.00 14.22 ? 560  PHE A CG  1 
ATOM   4479 C CD1 . PHE A 1 560 ? 54.095 96.443  20.527  1.00 15.54 ? 560  PHE A CD1 1 
ATOM   4480 C CD2 . PHE A 1 560 ? 52.689 98.235  19.781  1.00 17.49 ? 560  PHE A CD2 1 
ATOM   4481 C CE1 . PHE A 1 560 ? 52.986 95.578  20.494  1.00 14.83 ? 560  PHE A CE1 1 
ATOM   4482 C CE2 . PHE A 1 560 ? 51.583 97.400  19.744  1.00 14.73 ? 560  PHE A CE2 1 
ATOM   4483 C CZ  . PHE A 1 560 ? 51.729 96.090  20.102  1.00 14.84 ? 560  PHE A CZ  1 
ATOM   4484 N N   . ASN A 1 561 ? 57.615 100.220 18.394  1.00 13.29 ? 561  ASN A N   1 
ATOM   4485 C CA  . ASN A 1 561 ? 58.248 101.421 17.793  1.00 14.68 ? 561  ASN A CA  1 
ATOM   4486 C C   . ASN A 1 561 ? 58.171 101.434 16.261  1.00 15.06 ? 561  ASN A C   1 
ATOM   4487 O O   . ASN A 1 561 ? 57.920 102.470 15.657  1.00 17.69 ? 561  ASN A O   1 
ATOM   4488 C CB  . ASN A 1 561 ? 59.706 101.550 18.289  1.00 14.19 ? 561  ASN A CB  1 
ATOM   4489 C CG  . ASN A 1 561 ? 59.801 102.294 19.601  1.00 15.12 ? 561  ASN A CG  1 
ATOM   4490 O OD1 . ASN A 1 561 ? 60.177 103.456 19.603  1.00 13.72 ? 561  ASN A OD1 1 
ATOM   4491 N ND2 . ASN A 1 561 ? 59.480 101.634 20.724  1.00 14.00 ? 561  ASN A ND2 1 
ATOM   4492 N N   . LEU A 1 562 ? 58.332 100.290 15.601  1.00 16.19 ? 562  LEU A N   1 
ATOM   4493 C CA  . LEU A 1 562 ? 58.000 100.219 14.169  1.00 16.13 ? 562  LEU A CA  1 
ATOM   4494 C C   . LEU A 1 562 ? 56.535 100.561 13.899  1.00 16.70 ? 562  LEU A C   1 
ATOM   4495 O O   . LEU A 1 562 ? 56.203 101.141 12.863  1.00 17.19 ? 562  LEU A O   1 
ATOM   4496 C CB  . LEU A 1 562 ? 58.216 98.804  13.594  1.00 15.92 ? 562  LEU A CB  1 
ATOM   4497 C CG  . LEU A 1 562 ? 59.508 98.027  13.723  1.00 18.81 ? 562  LEU A CG  1 
ATOM   4498 C CD1 . LEU A 1 562 ? 59.367 96.697  12.933  1.00 18.56 ? 562  LEU A CD1 1 
ATOM   4499 C CD2 . LEU A 1 562 ? 60.692 98.896  13.205  1.00 16.90 ? 562  LEU A CD2 1 
ATOM   4500 N N   . PHE A 1 563 ? 55.659 100.134 14.800  1.00 16.40 ? 563  PHE A N   1 
ATOM   4501 C CA  . PHE A 1 563 ? 54.206 100.360 14.650  1.00 16.40 ? 563  PHE A CA  1 
ATOM   4502 C C   . PHE A 1 563 ? 53.789 101.804 14.976  1.00 16.91 ? 563  PHE A C   1 
ATOM   4503 O O   . PHE A 1 563 ? 52.623 102.173 14.824  1.00 17.62 ? 563  PHE A O   1 
ATOM   4504 C CB  . PHE A 1 563 ? 53.410 99.346  15.502  1.00 15.96 ? 563  PHE A CB  1 
ATOM   4505 C CG  . PHE A 1 563 ? 53.746 97.900  15.224  1.00 14.66 ? 563  PHE A CG  1 
ATOM   4506 C CD1 . PHE A 1 563 ? 54.123 97.474  13.945  1.00 14.58 ? 563  PHE A CD1 1 
ATOM   4507 C CD2 . PHE A 1 563 ? 53.633 96.947  16.250  1.00 13.64 ? 563  PHE A CD2 1 
ATOM   4508 C CE1 . PHE A 1 563 ? 54.457 96.115  13.703  1.00 12.05 ? 563  PHE A CE1 1 
ATOM   4509 C CE2 . PHE A 1 563 ? 53.929 95.627  16.031  1.00 15.03 ? 563  PHE A CE2 1 
ATOM   4510 C CZ  . PHE A 1 563 ? 54.349 95.204  14.739  1.00 14.86 ? 563  PHE A CZ  1 
ATOM   4511 N N   . GLY A 1 564 ? 54.755 102.641 15.383  1.00 17.12 ? 564  GLY A N   1 
ATOM   4512 C CA  . GLY A 1 564 ? 54.474 104.035 15.762  1.00 16.21 ? 564  GLY A CA  1 
ATOM   4513 C C   . GLY A 1 564 ? 53.747 104.212 17.098  1.00 16.53 ? 564  GLY A C   1 
ATOM   4514 O O   . GLY A 1 564 ? 52.965 105.162 17.297  1.00 16.35 ? 564  GLY A O   1 
ATOM   4515 N N   . ILE A 1 565 ? 53.969 103.273 17.994  1.00 15.82 ? 565  ILE A N   1 
ATOM   4516 C CA  . ILE A 1 565 ? 53.592 103.400 19.384  1.00 17.06 ? 565  ILE A CA  1 
ATOM   4517 C C   . ILE A 1 565 ? 54.898 103.371 20.215  1.00 17.19 ? 565  ILE A C   1 
ATOM   4518 O O   . ILE A 1 565 ? 55.180 102.376 20.882  1.00 17.07 ? 565  ILE A O   1 
ATOM   4519 C CB  . ILE A 1 565 ? 52.627 102.261 19.805  1.00 17.76 ? 565  ILE A CB  1 
ATOM   4520 C CG1 . ILE A 1 565 ? 51.452 102.217 18.797  1.00 16.70 ? 565  ILE A CG1 1 
ATOM   4521 C CG2 . ILE A 1 565 ? 52.152 102.555 21.217  1.00 19.21 ? 565  ILE A CG2 1 
ATOM   4522 C CD1 . ILE A 1 565 ? 50.508 101.013 18.848  1.00 16.67 ? 565  ILE A CD1 1 
ATOM   4523 N N   . PRO A 1 566 ? 55.724 104.448 20.120  1.00 17.16 ? 566  PRO A N   1 
ATOM   4524 C CA  . PRO A 1 566 ? 57.031 104.443 20.765  1.00 17.37 ? 566  PRO A CA  1 
ATOM   4525 C C   . PRO A 1 566 ? 57.002 104.395 22.292  1.00 17.43 ? 566  PRO A C   1 
ATOM   4526 O O   . PRO A 1 566 ? 57.943 103.865 22.905  1.00 17.00 ? 566  PRO A O   1 
ATOM   4527 C CB  . PRO A 1 566 ? 57.691 105.736 20.259  1.00 17.02 ? 566  PRO A CB  1 
ATOM   4528 C CG  . PRO A 1 566 ? 56.596 106.617 19.874  1.00 17.93 ? 566  PRO A CG  1 
ATOM   4529 C CD  . PRO A 1 566 ? 55.485 105.712 19.393  1.00 17.26 ? 566  PRO A CD  1 
ATOM   4530 N N   . MET A 1 567 ? 55.960 104.973 22.895  1.00 17.79 ? 567  MET A N   1 
ATOM   4531 C CA  A MET A 1 567 ? 55.786 104.876 24.341  0.50 18.00 ? 567  MET A CA  1 
ATOM   4532 C CA  B MET A 1 567 ? 55.717 104.920 24.327  0.50 17.60 ? 567  MET A CA  1 
ATOM   4533 C C   . MET A 1 567 ? 55.119 103.543 24.673  1.00 17.36 ? 567  MET A C   1 
ATOM   4534 O O   . MET A 1 567 ? 53.907 103.403 24.700  1.00 17.17 ? 567  MET A O   1 
ATOM   4535 C CB  A MET A 1 567 ? 55.030 106.075 24.934  0.50 18.54 ? 567  MET A CB  1 
ATOM   4536 C CB  B MET A 1 567 ? 54.747 106.064 24.691  0.50 18.31 ? 567  MET A CB  1 
ATOM   4537 C CG  A MET A 1 567 ? 54.878 105.964 26.439  0.50 19.66 ? 567  MET A CG  1 
ATOM   4538 C CG  B MET A 1 567 ? 54.505 106.301 26.165  0.50 19.05 ? 567  MET A CG  1 
ATOM   4539 S SD  A MET A 1 567 ? 54.459 107.469 27.311  0.50 19.66 ? 567  MET A SD  1 
ATOM   4540 S SD  B MET A 1 567 ? 55.995 106.481 27.145  0.50 19.34 ? 567  MET A SD  1 
ATOM   4541 C CE  A MET A 1 567 ? 56.095 108.154 27.509  0.50 21.53 ? 567  MET A CE  1 
ATOM   4542 C CE  B MET A 1 567 ? 56.511 108.108 26.659  0.50 20.22 ? 567  MET A CE  1 
ATOM   4543 N N   . VAL A 1 568 ? 55.971 102.554 24.924  1.00 16.31 ? 568  VAL A N   1 
ATOM   4544 C CA  . VAL A 1 568 ? 55.593 101.159 25.125  1.00 15.75 ? 568  VAL A CA  1 
ATOM   4545 C C   . VAL A 1 568 ? 56.643 100.547 26.090  1.00 16.06 ? 568  VAL A C   1 
ATOM   4546 O O   . VAL A 1 568 ? 57.838 100.908 26.067  1.00 14.52 ? 568  VAL A O   1 
ATOM   4547 C CB  . VAL A 1 568 ? 55.557 100.396 23.744  1.00 15.07 ? 568  VAL A CB  1 
ATOM   4548 C CG1 . VAL A 1 568 ? 56.953 100.428 23.069  1.00 14.99 ? 568  VAL A CG1 1 
ATOM   4549 C CG2 . VAL A 1 568 ? 55.104 98.938  23.900  1.00 13.55 ? 568  VAL A CG2 1 
ATOM   4550 N N   . GLY A 1 569 ? 56.171 99.652  26.955  1.00 16.18 ? 569  GLY A N   1 
ATOM   4551 C CA  . GLY A 1 569 ? 57.027 98.849  27.800  1.00 17.24 ? 569  GLY A CA  1 
ATOM   4552 C C   . GLY A 1 569 ? 56.156 97.780  28.416  1.00 17.87 ? 569  GLY A C   1 
ATOM   4553 O O   . GLY A 1 569 ? 54.939 97.808  28.241  1.00 17.19 ? 569  GLY A O   1 
ATOM   4554 N N   . PRO A 1 570 ? 56.769 96.812  29.098  1.00 17.86 ? 570  PRO A N   1 
ATOM   4555 C CA  . PRO A 1 570 ? 56.005 95.804  29.824  1.00 19.29 ? 570  PRO A CA  1 
ATOM   4556 C C   . PRO A 1 570 ? 55.750 96.242  31.268  1.00 19.99 ? 570  PRO A C   1 
ATOM   4557 O O   . PRO A 1 570 ? 56.129 97.372  31.670  1.00 21.32 ? 570  PRO A O   1 
ATOM   4558 C CB  . PRO A 1 570 ? 56.974 94.610  29.814  1.00 18.04 ? 570  PRO A CB  1 
ATOM   4559 C CG  . PRO A 1 570 ? 58.287 95.277  30.071  1.00 18.15 ? 570  PRO A CG  1 
ATOM   4560 C CD  . PRO A 1 570 ? 58.213 96.567  29.215  1.00 18.89 ? 570  PRO A CD  1 
ATOM   4561 N N   . ASP A 1 571 ? 55.157 95.351  32.057  1.00 20.10 ? 571  ASP A N   1 
ATOM   4562 C CA  . ASP A 1 571 ? 55.143 95.477  33.531  1.00 19.26 ? 571  ASP A CA  1 
ATOM   4563 C C   . ASP A 1 571 ? 56.526 95.064  34.104  1.00 19.21 ? 571  ASP A C   1 
ATOM   4564 O O   . ASP A 1 571 ? 56.896 93.885  34.119  1.00 19.14 ? 571  ASP A O   1 
ATOM   4565 C CB  . ASP A 1 571 ? 54.036 94.613  34.121  1.00 18.21 ? 571  ASP A CB  1 
ATOM   4566 C CG  . ASP A 1 571 ? 52.632 95.074  33.683  1.00 20.23 ? 571  ASP A CG  1 
ATOM   4567 O OD1 . ASP A 1 571 ? 52.457 96.261  33.279  1.00 19.61 ? 571  ASP A OD1 1 
ATOM   4568 O OD2 . ASP A 1 571 ? 51.684 94.252  33.734  1.00 22.17 ? 571  ASP A OD2 1 
ATOM   4569 N N   . ILE A 1 572 ? 57.292 96.045  34.557  1.00 18.59 ? 572  ILE A N   1 
ATOM   4570 C CA  . ILE A 1 572 ? 58.639 95.785  35.087  1.00 17.85 ? 572  ILE A CA  1 
ATOM   4571 C C   . ILE A 1 572 ? 58.530 94.899  36.318  1.00 17.98 ? 572  ILE A C   1 
ATOM   4572 O O   . ILE A 1 572 ? 57.687 95.156  37.189  1.00 16.81 ? 572  ILE A O   1 
ATOM   4573 C CB  . ILE A 1 572 ? 59.361 97.096  35.444  1.00 17.39 ? 572  ILE A CB  1 
ATOM   4574 C CG1 . ILE A 1 572 ? 59.646 97.909  34.189  1.00 16.80 ? 572  ILE A CG1 1 
ATOM   4575 C CG2 . ILE A 1 572 ? 60.659 96.813  36.210  1.00 16.66 ? 572  ILE A CG2 1 
ATOM   4576 C CD1 . ILE A 1 572 ? 60.139 99.337  34.523  1.00 15.86 ? 572  ILE A CD1 1 
ATOM   4577 N N   . CYS A 1 573 ? 59.399 93.878  36.370  1.00 17.75 ? 573  CYS A N   1 
ATOM   4578 C CA  . CYS A 1 573 ? 59.441 92.846  37.406  1.00 18.32 ? 573  CYS A CA  1 
ATOM   4579 C C   . CYS A 1 573 ? 58.366 91.747  37.227  1.00 18.72 ? 573  CYS A C   1 
ATOM   4580 O O   . CYS A 1 573 ? 58.425 90.721  37.910  1.00 18.31 ? 573  CYS A O   1 
ATOM   4581 C CB  . CYS A 1 573 ? 59.459 93.430  38.833  1.00 18.53 ? 573  CYS A CB  1 
ATOM   4582 S SG  . CYS A 1 573 ? 60.870 94.545  39.135  1.00 22.50 ? 573  CYS A SG  1 
ATOM   4583 N N   . GLY A 1 574 ? 57.412 91.947  36.311  1.00 17.70 ? 574  GLY A N   1 
ATOM   4584 C CA  . GLY A 1 574 ? 56.510 90.886  35.944  1.00 19.26 ? 574  GLY A CA  1 
ATOM   4585 C C   . GLY A 1 574 ? 55.187 91.005  36.694  1.00 19.87 ? 574  GLY A C   1 
ATOM   4586 O O   . GLY A 1 574 ? 55.154 91.133  37.910  1.00 21.06 ? 574  GLY A O   1 
ATOM   4587 N N   . PHE A 1 575 ? 54.099 90.975  35.955  1.00 20.23 ? 575  PHE A N   1 
ATOM   4588 C CA  . PHE A 1 575 ? 52.759 91.087  36.522  1.00 20.49 ? 575  PHE A CA  1 
ATOM   4589 C C   . PHE A 1 575 ? 52.460 89.863  37.421  1.00 21.67 ? 575  PHE A C   1 
ATOM   4590 O O   . PHE A 1 575 ? 52.351 90.005  38.646  1.00 22.87 ? 575  PHE A O   1 
ATOM   4591 C CB  . PHE A 1 575 ? 51.762 91.216  35.374  1.00 19.60 ? 575  PHE A CB  1 
ATOM   4592 C CG  . PHE A 1 575 ? 50.310 91.279  35.791  1.00 18.25 ? 575  PHE A CG  1 
ATOM   4593 C CD1 . PHE A 1 575 ? 49.771 92.433  36.331  1.00 17.44 ? 575  PHE A CD1 1 
ATOM   4594 C CD2 . PHE A 1 575 ? 49.471 90.196  35.557  1.00 20.80 ? 575  PHE A CD2 1 
ATOM   4595 C CE1 . PHE A 1 575 ? 48.404 92.501  36.670  1.00 19.10 ? 575  PHE A CE1 1 
ATOM   4596 C CE2 . PHE A 1 575 ? 48.103 90.244  35.900  1.00 19.86 ? 575  PHE A CE2 1 
ATOM   4597 C CZ  . PHE A 1 575 ? 47.579 91.397  36.460  1.00 17.07 ? 575  PHE A CZ  1 
ATOM   4598 N N   . ALA A 1 576 ? 52.342 88.683  36.815  1.00 20.99 ? 576  ALA A N   1 
ATOM   4599 C CA  . ALA A 1 576 ? 51.964 87.462  37.499  1.00 21.65 ? 576  ALA A CA  1 
ATOM   4600 C C   . ALA A 1 576 ? 53.163 86.928  38.221  1.00 22.34 ? 576  ALA A C   1 
ATOM   4601 O O   . ALA A 1 576 ? 54.301 87.026  37.703  1.00 21.83 ? 576  ALA A O   1 
ATOM   4602 C CB  . ALA A 1 576 ? 51.448 86.398  36.485  1.00 21.34 ? 576  ALA A CB  1 
ATOM   4603 N N   . LEU A 1 577 ? 52.903 86.391  39.417  1.00 23.09 ? 577  LEU A N   1 
ATOM   4604 C CA  . LEU A 1 577 ? 53.889 85.703  40.273  1.00 24.42 ? 577  LEU A CA  1 
ATOM   4605 C C   . LEU A 1 577 ? 54.656 86.654  41.194  1.00 25.11 ? 577  LEU A C   1 
ATOM   4606 O O   . LEU A 1 577 ? 54.734 87.855  40.918  1.00 25.40 ? 577  LEU A O   1 
ATOM   4607 C CB  . LEU A 1 577 ? 54.856 84.841  39.438  1.00 24.12 ? 577  LEU A CB  1 
ATOM   4608 C CG  . LEU A 1 577 ? 54.504 83.414  39.007  1.00 26.08 ? 577  LEU A CG  1 
ATOM   4609 C CD1 . LEU A 1 577 ? 53.055 83.204  38.664  1.00 28.41 ? 577  LEU A CD1 1 
ATOM   4610 C CD2 . LEU A 1 577 ? 55.401 82.939  37.882  1.00 25.69 ? 577  LEU A CD2 1 
ATOM   4611 N N   . ASP A 1 578 ? 55.208 86.105  42.282  1.00 25.29 ? 578  ASP A N   1 
ATOM   4612 C CA  . ASP A 1 578 ? 56.166 86.789  43.135  1.00 26.55 ? 578  ASP A CA  1 
ATOM   4613 C C   . ASP A 1 578 ? 57.477 87.021  42.355  1.00 27.05 ? 578  ASP A C   1 
ATOM   4614 O O   . ASP A 1 578 ? 58.020 86.074  41.777  1.00 27.91 ? 578  ASP A O   1 
ATOM   4615 C CB  . ASP A 1 578 ? 56.472 85.925  44.364  1.00 26.49 ? 578  ASP A CB  1 
ATOM   4616 C CG  . ASP A 1 578 ? 55.318 85.915  45.411  1.00 28.36 ? 578  ASP A CG  1 
ATOM   4617 O OD1 . ASP A 1 578 ? 54.241 86.529  45.200  1.00 30.38 ? 578  ASP A OD1 1 
ATOM   4618 O OD2 . ASP A 1 578 ? 55.501 85.291  46.473  1.00 33.27 ? 578  ASP A OD2 1 
ATOM   4619 N N   . THR A 1 579 ? 57.996 88.249  42.331  1.00 25.85 ? 579  THR A N   1 
ATOM   4620 C CA  . THR A 1 579 ? 59.239 88.468  41.611  1.00 26.02 ? 579  THR A CA  1 
ATOM   4621 C C   . THR A 1 579 ? 60.438 88.101  42.502  1.00 26.13 ? 579  THR A C   1 
ATOM   4622 O O   . THR A 1 579 ? 60.469 88.470  43.673  1.00 26.25 ? 579  THR A O   1 
ATOM   4623 C CB  . THR A 1 579 ? 59.347 89.902  41.026  1.00 25.39 ? 579  THR A CB  1 
ATOM   4624 O OG1 . THR A 1 579 ? 60.380 89.929  40.023  1.00 27.06 ? 579  THR A OG1 1 
ATOM   4625 C CG2 . THR A 1 579 ? 59.660 90.934  42.122  1.00 24.20 ? 579  THR A CG2 1 
ATOM   4626 N N   . PRO A 1 580 ? 61.400 87.323  41.965  1.00 26.64 ? 580  PRO A N   1 
ATOM   4627 C CA  . PRO A 1 580 ? 62.644 87.094  42.705  1.00 26.72 ? 580  PRO A CA  1 
ATOM   4628 C C   . PRO A 1 580 ? 63.414 88.433  42.799  1.00 26.60 ? 580  PRO A C   1 
ATOM   4629 O O   . PRO A 1 580 ? 63.259 89.264  41.922  1.00 26.96 ? 580  PRO A O   1 
ATOM   4630 C CB  . PRO A 1 580 ? 63.404 86.108  41.798  1.00 27.06 ? 580  PRO A CB  1 
ATOM   4631 C CG  . PRO A 1 580 ? 62.348 85.460  40.963  1.00 26.52 ? 580  PRO A CG  1 
ATOM   4632 C CD  . PRO A 1 580 ? 61.396 86.596  40.684  1.00 26.46 ? 580  PRO A CD  1 
ATOM   4633 N N   . GLU A 1 581 ? 64.208 88.650  43.841  1.00 25.45 ? 581  GLU A N   1 
ATOM   4634 C CA  . GLU A 1 581 ? 64.982 89.897  43.968  1.00 24.45 ? 581  GLU A CA  1 
ATOM   4635 C C   . GLU A 1 581 ? 65.953 90.130  42.796  1.00 23.82 ? 581  GLU A C   1 
ATOM   4636 O O   . GLU A 1 581 ? 66.069 91.263  42.303  1.00 22.56 ? 581  GLU A O   1 
ATOM   4637 C CB  . GLU A 1 581 ? 65.757 89.940  45.297  1.00 23.50 ? 581  GLU A CB  1 
ATOM   4638 C CG  . GLU A 1 581 ? 66.489 91.238  45.592  1.00 23.52 ? 581  GLU A CG  1 
ATOM   4639 C CD  . GLU A 1 581 ? 67.889 91.338  44.979  1.00 24.75 ? 581  GLU A CD  1 
ATOM   4640 O OE1 . GLU A 1 581 ? 68.467 90.306  44.543  1.00 28.27 ? 581  GLU A OE1 1 
ATOM   4641 O OE2 . GLU A 1 581 ? 68.441 92.463  44.919  1.00 24.87 ? 581  GLU A OE2 1 
ATOM   4642 N N   . GLU A 1 582 ? 66.672 89.077  42.388  1.00 23.04 ? 582  GLU A N   1 
ATOM   4643 C CA  . GLU A 1 582 ? 67.670 89.212  41.337  1.00 22.67 ? 582  GLU A CA  1 
ATOM   4644 C C   . GLU A 1 582 ? 67.031 89.626  40.014  1.00 21.59 ? 582  GLU A C   1 
ATOM   4645 O O   . GLU A 1 582 ? 67.531 90.541  39.349  1.00 20.47 ? 582  GLU A O   1 
ATOM   4646 C CB  . GLU A 1 582 ? 68.474 87.923  41.141  1.00 22.14 ? 582  GLU A CB  1 
ATOM   4647 C CG  . GLU A 1 582 ? 69.710 88.106  40.197  1.00 23.33 ? 582  GLU A CG  1 
ATOM   4648 C CD  . GLU A 1 582 ? 70.287 86.773  39.663  1.00 25.71 ? 582  GLU A CD  1 
ATOM   4649 O OE1 . GLU A 1 582 ? 69.778 85.687  40.048  1.00 28.46 ? 582  GLU A OE1 1 
ATOM   4650 O OE2 . GLU A 1 582 ? 71.248 86.820  38.832  1.00 30.80 ? 582  GLU A OE2 1 
ATOM   4651 N N   . LEU A 1 583 ? 65.938 88.940  39.645  1.00 20.92 ? 583  LEU A N   1 
ATOM   4652 C CA  . LEU A 1 583 ? 65.167 89.273  38.443  1.00 20.52 ? 583  LEU A CA  1 
ATOM   4653 C C   . LEU A 1 583 ? 64.665 90.724  38.471  1.00 20.99 ? 583  LEU A C   1 
ATOM   4654 O O   . LEU A 1 583 ? 64.889 91.494  37.536  1.00 20.67 ? 583  LEU A O   1 
ATOM   4655 C CB  . LEU A 1 583 ? 63.958 88.321  38.277  1.00 20.42 ? 583  LEU A CB  1 
ATOM   4656 C CG  . LEU A 1 583 ? 63.110 88.639  37.042  1.00 19.30 ? 583  LEU A CG  1 
ATOM   4657 C CD1 . LEU A 1 583 ? 63.908 88.523  35.749  1.00 16.81 ? 583  LEU A CD1 1 
ATOM   4658 C CD2 . LEU A 1 583 ? 61.879 87.738  36.977  1.00 19.74 ? 583  LEU A CD2 1 
ATOM   4659 N N   . CYS A 1 584 ? 63.965 91.091  39.543  1.00 21.03 ? 584  CYS A N   1 
ATOM   4660 C CA  . CYS A 1 584 ? 63.444 92.451  39.671  1.00 20.67 ? 584  CYS A CA  1 
ATOM   4661 C C   . CYS A 1 584 ? 64.569 93.533  39.611  1.00 20.86 ? 584  CYS A C   1 
ATOM   4662 O O   . CYS A 1 584 ? 64.413 94.581  38.986  1.00 20.75 ? 584  CYS A O   1 
ATOM   4663 C CB  . CYS A 1 584 ? 62.583 92.565  40.918  1.00 20.51 ? 584  CYS A CB  1 
ATOM   4664 S SG  . CYS A 1 584 ? 61.581 94.129  41.014  1.00 21.98 ? 584  CYS A SG  1 
ATOM   4665 N N   . ARG A 1 585 ? 65.724 93.254  40.205  1.00 20.47 ? 585  ARG A N   1 
ATOM   4666 C CA  . ARG A 1 585 ? 66.838 94.197  40.154  1.00 19.60 ? 585  ARG A CA  1 
ATOM   4667 C C   . ARG A 1 585 ? 67.343 94.344  38.713  1.00 19.81 ? 585  ARG A C   1 
ATOM   4668 O O   . ARG A 1 585 ? 67.596 95.463  38.264  1.00 19.95 ? 585  ARG A O   1 
ATOM   4669 C CB  . ARG A 1 585 ? 67.975 93.741  41.100  1.00 20.35 ? 585  ARG A CB  1 
ATOM   4670 C CG  . ARG A 1 585 ? 69.245 94.561  40.972  1.00 18.98 ? 585  ARG A CG  1 
ATOM   4671 C CD  . ARG A 1 585 ? 70.205 94.396  42.175  1.00 19.47 ? 585  ARG A CD  1 
ATOM   4672 N NE  . ARG A 1 585 ? 70.249 93.024  42.682  1.00 23.05 ? 585  ARG A NE  1 
ATOM   4673 C CZ  . ARG A 1 585 ? 70.939 92.021  42.130  1.00 23.46 ? 585  ARG A CZ  1 
ATOM   4674 N NH1 . ARG A 1 585 ? 71.624 92.213  41.020  1.00 24.44 ? 585  ARG A NH1 1 
ATOM   4675 N NH2 . ARG A 1 585 ? 70.897 90.800  42.669  1.00 24.44 ? 585  ARG A NH2 1 
ATOM   4676 N N   . ARG A 1 586 ? 67.467 93.235  37.975  1.00 19.43 ? 586  ARG A N   1 
ATOM   4677 C CA  . ARG A 1 586 ? 67.926 93.318  36.561  1.00 19.75 ? 586  ARG A CA  1 
ATOM   4678 C C   . ARG A 1 586 ? 66.853 93.976  35.705  1.00 19.40 ? 586  ARG A C   1 
ATOM   4679 O O   . ARG A 1 586 ? 67.161 94.706  34.739  1.00 19.68 ? 586  ARG A O   1 
ATOM   4680 C CB  . ARG A 1 586 ? 68.322 91.940  35.966  1.00 19.07 ? 586  ARG A CB  1 
ATOM   4681 C CG  . ARG A 1 586 ? 69.587 91.311  36.546  1.00 18.79 ? 586  ARG A CG  1 
ATOM   4682 C CD  . ARG A 1 586 ? 70.703 92.292  36.562  1.00 20.27 ? 586  ARG A CD  1 
ATOM   4683 N NE  . ARG A 1 586 ? 71.997 91.659  36.734  1.00 20.86 ? 586  ARG A NE  1 
ATOM   4684 C CZ  . ARG A 1 586 ? 73.163 92.295  36.741  1.00 21.94 ? 586  ARG A CZ  1 
ATOM   4685 N NH1 . ARG A 1 586 ? 73.211 93.621  36.601  1.00 15.51 ? 586  ARG A NH1 1 
ATOM   4686 N NH2 . ARG A 1 586 ? 74.286 91.583  36.893  1.00 19.65 ? 586  ARG A NH2 1 
ATOM   4687 N N   . TRP A 1 587 ? 65.597 93.734  36.070  1.00 18.53 ? 587  TRP A N   1 
ATOM   4688 C CA  . TRP A 1 587 ? 64.471 94.294  35.343  1.00 18.26 ? 587  TRP A CA  1 
ATOM   4689 C C   . TRP A 1 587 ? 64.293 95.790  35.577  1.00 18.35 ? 587  TRP A C   1 
ATOM   4690 O O   . TRP A 1 587 ? 63.953 96.554  34.647  1.00 18.25 ? 587  TRP A O   1 
ATOM   4691 C CB  . TRP A 1 587 ? 63.188 93.532  35.692  1.00 18.06 ? 587  TRP A CB  1 
ATOM   4692 C CG  . TRP A 1 587 ? 62.228 93.432  34.531  1.00 18.59 ? 587  TRP A CG  1 
ATOM   4693 C CD1 . TRP A 1 587 ? 62.071 94.340  33.504  1.00 17.07 ? 587  TRP A CD1 1 
ATOM   4694 C CD2 . TRP A 1 587 ? 61.326 92.344  34.247  1.00 16.43 ? 587  TRP A CD2 1 
ATOM   4695 N NE1 . TRP A 1 587 ? 61.133 93.875  32.610  1.00 15.12 ? 587  TRP A NE1 1 
ATOM   4696 C CE2 . TRP A 1 587 ? 60.642 92.670  33.047  1.00 15.87 ? 587  TRP A CE2 1 
ATOM   4697 C CE3 . TRP A 1 587 ? 61.021 91.131  34.894  1.00 19.14 ? 587  TRP A CE3 1 
ATOM   4698 C CZ2 . TRP A 1 587 ? 59.651 91.830  32.481  1.00 16.12 ? 587  TRP A CZ2 1 
ATOM   4699 C CZ3 . TRP A 1 587 ? 60.011 90.292  34.326  1.00 17.06 ? 587  TRP A CZ3 1 
ATOM   4700 C CH2 . TRP A 1 587 ? 59.361 90.656  33.130  1.00 17.85 ? 587  TRP A CH2 1 
ATOM   4701 N N   . MET A 1 588 ? 64.530 96.228  36.807  1.00 18.97 ? 588  MET A N   1 
ATOM   4702 C CA  . MET A 1 588 ? 64.518 97.679  37.095  1.00 19.40 ? 588  MET A CA  1 
ATOM   4703 C C   . MET A 1 588 ? 65.638 98.456  36.381  1.00 19.23 ? 588  MET A C   1 
ATOM   4704 O O   . MET A 1 588 ? 65.411 99.587  35.948  1.00 17.62 ? 588  MET A O   1 
ATOM   4705 C CB  . MET A 1 588 ? 64.531 97.966  38.606  1.00 19.88 ? 588  MET A CB  1 
ATOM   4706 C CG  . MET A 1 588 ? 63.175 97.731  39.303  1.00 19.36 ? 588  MET A CG  1 
ATOM   4707 S SD  . MET A 1 588 ? 61.926 98.938  38.812  1.00 22.11 ? 588  MET A SD  1 
ATOM   4708 C CE  . MET A 1 588 ? 62.737 100.488 39.199  1.00 21.08 ? 588  MET A CE  1 
ATOM   4709 N N   . GLN A 1 589 ? 66.829 97.847  36.265  1.00 19.50 ? 589  GLN A N   1 
ATOM   4710 C CA  . GLN A 1 589 ? 67.986 98.432  35.532  1.00 20.05 ? 589  GLN A CA  1 
ATOM   4711 C C   . GLN A 1 589 ? 67.661 98.628  34.048  1.00 19.44 ? 589  GLN A C   1 
ATOM   4712 O O   . GLN A 1 589 ? 67.837 99.724  33.501  1.00 19.06 ? 589  GLN A O   1 
ATOM   4713 C CB  . GLN A 1 589 ? 69.220 97.536  35.684  1.00 19.56 ? 589  GLN A CB  1 
ATOM   4714 C CG  . GLN A 1 589 ? 69.773 97.515  37.102  1.00 22.43 ? 589  GLN A CG  1 
ATOM   4715 C CD  . GLN A 1 589 ? 70.790 96.377  37.364  1.00 22.77 ? 589  GLN A CD  1 
ATOM   4716 O OE1 . GLN A 1 589 ? 70.993 95.476  36.532  1.00 20.70 ? 589  GLN A OE1 1 
ATOM   4717 N NE2 . GLN A 1 589 ? 71.419 96.427  38.528  1.00 25.79 ? 589  GLN A NE2 1 
ATOM   4718 N N   . LEU A 1 590 ? 67.186 97.559  33.396  1.00 18.64 ? 590  LEU A N   1 
ATOM   4719 C CA  . LEU A 1 590 ? 66.648 97.671  32.045  1.00 18.39 ? 590  LEU A CA  1 
ATOM   4720 C C   . LEU A 1 590 ? 65.417 98.597  31.954  1.00 18.14 ? 590  LEU A C   1 
ATOM   4721 O O   . LEU A 1 590 ? 65.304 99.405  31.008  1.00 17.29 ? 590  LEU A O   1 
ATOM   4722 C CB  . LEU A 1 590 ? 66.313 96.276  31.489  1.00 17.67 ? 590  LEU A CB  1 
ATOM   4723 C CG  . LEU A 1 590 ? 65.719 96.235  30.087  1.00 18.15 ? 590  LEU A CG  1 
ATOM   4724 C CD1 . LEU A 1 590 ? 66.649 96.931  29.002  1.00 17.25 ? 590  LEU A CD1 1 
ATOM   4725 C CD2 . LEU A 1 590 ? 65.366 94.798  29.707  1.00 18.15 ? 590  LEU A CD2 1 
ATOM   4726 N N   . GLY A 1 591 ? 64.505 98.450  32.920  1.00 17.81 ? 591  GLY A N   1 
ATOM   4727 C CA  . GLY A 1 591 ? 63.222 99.174  32.926  1.00 17.84 ? 591  GLY A CA  1 
ATOM   4728 C C   . GLY A 1 591 ? 63.373 100.692 32.987  1.00 18.01 ? 591  GLY A C   1 
ATOM   4729 O O   . GLY A 1 591 ? 62.516 101.410 32.491  1.00 17.94 ? 591  GLY A O   1 
ATOM   4730 N N   . ALA A 1 592 ? 64.466 101.177 33.592  1.00 17.55 ? 592  ALA A N   1 
ATOM   4731 C CA  . ALA A 1 592 ? 64.792 102.596 33.593  1.00 17.50 ? 592  ALA A CA  1 
ATOM   4732 C C   . ALA A 1 592 ? 65.025 103.109 32.165  1.00 17.63 ? 592  ALA A C   1 
ATOM   4733 O O   . ALA A 1 592 ? 64.992 104.293 31.918  1.00 17.37 ? 592  ALA A O   1 
ATOM   4734 C CB  . ALA A 1 592 ? 66.018 102.879 34.503  1.00 17.92 ? 592  ALA A CB  1 
ATOM   4735 N N   . PHE A 1 593 ? 65.186 102.199 31.203  1.00 18.47 ? 593  PHE A N   1 
ATOM   4736 C CA  . PHE A 1 593 ? 65.381 102.582 29.782  1.00 18.65 ? 593  PHE A CA  1 
ATOM   4737 C C   . PHE A 1 593 ? 64.293 102.146 28.783  1.00 19.62 ? 593  PHE A C   1 
ATOM   4738 O O   . PHE A 1 593 ? 64.457 102.347 27.566  1.00 20.45 ? 593  PHE A O   1 
ATOM   4739 C CB  . PHE A 1 593 ? 66.798 102.190 29.340  1.00 18.20 ? 593  PHE A CB  1 
ATOM   4740 C CG  . PHE A 1 593 ? 67.842 102.803 30.230  1.00 19.67 ? 593  PHE A CG  1 
ATOM   4741 C CD1 . PHE A 1 593 ? 68.249 104.130 30.030  1.00 19.73 ? 593  PHE A CD1 1 
ATOM   4742 C CD2 . PHE A 1 593 ? 68.335 102.095 31.329  1.00 17.89 ? 593  PHE A CD2 1 
ATOM   4743 C CE1 . PHE A 1 593 ? 69.157 104.739 30.893  1.00 18.61 ? 593  PHE A CE1 1 
ATOM   4744 C CE2 . PHE A 1 593 ? 69.241 102.698 32.206  1.00 20.48 ? 593  PHE A CE2 1 
ATOM   4745 C CZ  . PHE A 1 593 ? 69.662 104.013 31.987  1.00 18.63 ? 593  PHE A CZ  1 
ATOM   4746 N N   . TYR A 1 594 ? 63.181 101.563 29.266  1.00 18.69 ? 594  TYR A N   1 
ATOM   4747 C CA  . TYR A 1 594 ? 62.029 101.371 28.376  1.00 19.39 ? 594  TYR A CA  1 
ATOM   4748 C C   . TYR A 1 594 ? 61.463 102.777 28.106  1.00 19.94 ? 594  TYR A C   1 
ATOM   4749 O O   . TYR A 1 594 ? 61.507 103.623 29.002  1.00 20.82 ? 594  TYR A O   1 
ATOM   4750 C CB  . TYR A 1 594 ? 60.932 100.533 29.023  1.00 18.27 ? 594  TYR A CB  1 
ATOM   4751 C CG  . TYR A 1 594 ? 61.237 99.079  29.234  1.00 18.46 ? 594  TYR A CG  1 
ATOM   4752 C CD1 . TYR A 1 594 ? 61.737 98.284  28.210  1.00 19.11 ? 594  TYR A CD1 1 
ATOM   4753 C CD2 . TYR A 1 594 ? 60.941 98.471  30.447  1.00 18.88 ? 594  TYR A CD2 1 
ATOM   4754 C CE1 . TYR A 1 594 ? 61.999 96.905  28.428  1.00 17.75 ? 594  TYR A CE1 1 
ATOM   4755 C CE2 . TYR A 1 594 ? 61.167 97.132  30.662  1.00 16.58 ? 594  TYR A CE2 1 
ATOM   4756 C CZ  . TYR A 1 594 ? 61.701 96.354  29.661  1.00 17.04 ? 594  TYR A CZ  1 
ATOM   4757 O OH  . TYR A 1 594 ? 61.899 95.012  29.895  1.00 17.67 ? 594  TYR A OH  1 
ATOM   4758 N N   . PRO A 1 595 ? 60.971 103.044 26.884  1.00 19.80 ? 595  PRO A N   1 
ATOM   4759 C CA  . PRO A 1 595 ? 60.323 104.353 26.622  1.00 20.25 ? 595  PRO A CA  1 
ATOM   4760 C C   . PRO A 1 595 ? 59.130 104.621 27.561  1.00 20.60 ? 595  PRO A C   1 
ATOM   4761 O O   . PRO A 1 595 ? 59.023 105.727 28.113  1.00 21.91 ? 595  PRO A O   1 
ATOM   4762 C CB  . PRO A 1 595 ? 59.888 104.250 25.162  1.00 20.42 ? 595  PRO A CB  1 
ATOM   4763 C CG  . PRO A 1 595 ? 60.796 103.176 24.579  1.00 20.18 ? 595  PRO A CG  1 
ATOM   4764 C CD  . PRO A 1 595 ? 61.007 102.183 25.685  1.00 18.69 ? 595  PRO A CD  1 
ATOM   4765 N N   . PHE A 1 596 ? 58.296 103.607 27.795  1.00 19.36 ? 596  PHE A N   1 
ATOM   4766 C CA  . PHE A 1 596 ? 57.302 103.622 28.887  1.00 17.87 ? 596  PHE A CA  1 
ATOM   4767 C C   . PHE A 1 596 ? 57.809 102.762 30.056  1.00 17.96 ? 596  PHE A C   1 
ATOM   4768 O O   . PHE A 1 596 ? 57.983 101.562 29.897  1.00 18.18 ? 596  PHE A O   1 
ATOM   4769 C CB  . PHE A 1 596 ? 55.944 103.120 28.385  1.00 18.27 ? 596  PHE A CB  1 
ATOM   4770 C CG  . PHE A 1 596 ? 54.904 103.006 29.446  1.00 17.11 ? 596  PHE A CG  1 
ATOM   4771 C CD1 . PHE A 1 596 ? 54.453 104.148 30.126  1.00 17.97 ? 596  PHE A CD1 1 
ATOM   4772 C CD2 . PHE A 1 596 ? 54.386 101.766 29.796  1.00 17.18 ? 596  PHE A CD2 1 
ATOM   4773 C CE1 . PHE A 1 596 ? 53.496 104.062 31.130  1.00 18.34 ? 596  PHE A CE1 1 
ATOM   4774 C CE2 . PHE A 1 596 ? 53.398 101.668 30.819  1.00 17.49 ? 596  PHE A CE2 1 
ATOM   4775 C CZ  . PHE A 1 596 ? 52.953 102.831 31.478  1.00 15.19 ? 596  PHE A CZ  1 
ATOM   4776 N N   . SER A 1 597 ? 58.045 103.390 31.216  1.00 16.56 ? 597  SER A N   1 
ATOM   4777 C CA  . SER A 1 597 ? 58.668 102.760 32.368  1.00 17.43 ? 597  SER A CA  1 
ATOM   4778 C C   . SER A 1 597 ? 57.674 102.647 33.551  1.00 17.63 ? 597  SER A C   1 
ATOM   4779 O O   . SER A 1 597 ? 57.397 103.631 34.241  1.00 16.44 ? 597  SER A O   1 
ATOM   4780 C CB  . SER A 1 597 ? 59.930 103.573 32.774  1.00 16.71 ? 597  SER A CB  1 
ATOM   4781 O OG  . SER A 1 597 ? 60.666 102.907 33.787  1.00 17.09 ? 597  SER A OG  1 
ATOM   4782 N N   . ARG A 1 598 ? 57.102 101.464 33.734  1.00 18.31 ? 598  ARG A N   1 
ATOM   4783 C CA  . ARG A 1 598 ? 56.079 101.241 34.782  1.00 18.28 ? 598  ARG A CA  1 
ATOM   4784 C C   . ARG A 1 598 ? 56.324 99.904  35.453  1.00 18.55 ? 598  ARG A C   1 
ATOM   4785 O O   . ARG A 1 598 ? 56.481 98.878  34.773  1.00 17.86 ? 598  ARG A O   1 
ATOM   4786 C CB  . ARG A 1 598 ? 54.649 101.266 34.235  1.00 18.21 ? 598  ARG A CB  1 
ATOM   4787 C CG  . ARG A 1 598 ? 53.585 100.991 35.359  1.00 17.68 ? 598  ARG A CG  1 
ATOM   4788 C CD  . ARG A 1 598 ? 52.165 101.140 34.872  1.00 18.89 ? 598  ARG A CD  1 
ATOM   4789 N NE  . ARG A 1 598 ? 51.747 99.954  34.147  1.00 19.63 ? 598  ARG A NE  1 
ATOM   4790 C CZ  . ARG A 1 598 ? 50.481 99.618  33.935  1.00 18.69 ? 598  ARG A CZ  1 
ATOM   4791 N NH1 . ARG A 1 598 ? 49.471 100.385 34.374  1.00 17.04 ? 598  ARG A NH1 1 
ATOM   4792 N NH2 . ARG A 1 598 ? 50.232 98.508  33.278  1.00 17.78 ? 598  ARG A NH2 1 
ATOM   4793 N N   . ASN A 1 599 ? 56.390 99.921  36.782  1.00 18.44 ? 599  ASN A N   1 
ATOM   4794 C CA  . ASN A 1 599 ? 56.495 98.701  37.572  1.00 18.41 ? 599  ASN A CA  1 
ATOM   4795 C C   . ASN A 1 599 ? 55.077 98.466  38.011  1.00 19.01 ? 599  ASN A C   1 
ATOM   4796 O O   . ASN A 1 599 ? 54.492 99.317  38.684  1.00 19.43 ? 599  ASN A O   1 
ATOM   4797 C CB  . ASN A 1 599 ? 57.485 98.936  38.734  1.00 19.38 ? 599  ASN A CB  1 
ATOM   4798 C CG  . ASN A 1 599 ? 57.562 97.787  39.725  1.00 19.30 ? 599  ASN A CG  1 
ATOM   4799 O OD1 . ASN A 1 599 ? 56.550 97.169  40.097  1.00 21.45 ? 599  ASN A OD1 1 
ATOM   4800 N ND2 . ASN A 1 599 ? 58.773 97.523  40.191  1.00 16.33 ? 599  ASN A ND2 1 
ATOM   4801 N N   . HIS A 1 600 ? 54.500 97.338  37.571  1.00 18.75 ? 600  HIS A N   1 
ATOM   4802 C CA  . HIS A 1 600 ? 53.121 96.969  37.851  1.00 18.46 ? 600  HIS A CA  1 
ATOM   4803 C C   . HIS A 1 600 ? 53.082 95.499  38.270  1.00 19.52 ? 600  HIS A C   1 
ATOM   4804 O O   . HIS A 1 600 ? 53.947 94.704  37.854  1.00 21.32 ? 600  HIS A O   1 
ATOM   4805 C CB  . HIS A 1 600 ? 52.260 97.258  36.612  1.00 17.99 ? 600  HIS A CB  1 
ATOM   4806 C CG  . HIS A 1 600 ? 50.827 96.844  36.735  1.00 17.91 ? 600  HIS A CG  1 
ATOM   4807 N ND1 . HIS A 1 600 ? 50.017 97.255  37.765  1.00 19.49 ? 600  HIS A ND1 1 
ATOM   4808 C CD2 . HIS A 1 600 ? 50.048 96.083  35.928  1.00 17.95 ? 600  HIS A CD2 1 
ATOM   4809 C CE1 . HIS A 1 600 ? 48.806 96.743  37.609  1.00 20.40 ? 600  HIS A CE1 1 
ATOM   4810 N NE2 . HIS A 1 600 ? 48.794 96.042  36.491  1.00 19.26 ? 600  HIS A NE2 1 
ATOM   4811 N N   . ASN A 1 601 ? 52.089 95.128  39.082  1.00 18.75 ? 601  ASN A N   1 
ATOM   4812 C CA  . ASN A 1 601 ? 52.069 93.845  39.754  1.00 19.15 ? 601  ASN A CA  1 
ATOM   4813 C C   . ASN A 1 601 ? 50.647 93.295  39.822  1.00 19.22 ? 601  ASN A C   1 
ATOM   4814 O O   . ASN A 1 601 ? 49.670 94.055  39.881  1.00 20.15 ? 601  ASN A O   1 
ATOM   4815 C CB  . ASN A 1 601 ? 52.729 94.016  41.142  1.00 18.95 ? 601  ASN A CB  1 
ATOM   4816 C CG  . ASN A 1 601 ? 52.951 92.722  41.880  1.00 19.70 ? 601  ASN A CG  1 
ATOM   4817 O OD1 . ASN A 1 601 ? 52.892 91.622  41.305  1.00 19.85 ? 601  ASN A OD1 1 
ATOM   4818 N ND2 . ASN A 1 601 ? 53.231 92.839  43.198  1.00 19.29 ? 601  ASN A ND2 1 
ATOM   4819 N N   . GLY A 1 602 ? 50.515 91.978  39.734  1.00 19.86 ? 602  GLY A N   1 
ATOM   4820 C CA  . GLY A 1 602 ? 49.206 91.331  39.796  1.00 20.18 ? 602  GLY A CA  1 
ATOM   4821 C C   . GLY A 1 602 ? 48.677 91.206  41.210  1.00 21.85 ? 602  GLY A C   1 
ATOM   4822 O O   . GLY A 1 602 ? 49.383 91.499  42.193  1.00 21.38 ? 602  GLY A O   1 
ATOM   4823 N N   . GLN A 1 603 ? 47.432 90.757  41.307  1.00 21.83 ? 603  GLN A N   1 
ATOM   4824 C CA  . GLN A 1 603 ? 46.742 90.623  42.570  1.00 23.95 ? 603  GLN A CA  1 
ATOM   4825 C C   . GLN A 1 603 ? 47.363 89.562  43.490  1.00 23.88 ? 603  GLN A C   1 
ATOM   4826 O O   . GLN A 1 603 ? 47.644 88.443  43.067  1.00 23.95 ? 603  GLN A O   1 
ATOM   4827 C CB  . GLN A 1 603 ? 45.267 90.287  42.281  1.00 23.74 ? 603  GLN A CB  1 
ATOM   4828 C CG  . GLN A 1 603 ? 44.369 90.212  43.470  1.00 26.79 ? 603  GLN A CG  1 
ATOM   4829 C CD  . GLN A 1 603 ? 42.923 89.818  43.076  1.00 28.40 ? 603  GLN A CD  1 
ATOM   4830 O OE1 . GLN A 1 603 ? 42.711 88.829  42.368  1.00 35.44 ? 603  GLN A OE1 1 
ATOM   4831 N NE2 . GLN A 1 603 ? 41.946 90.609  43.508  1.00 32.87 ? 603  GLN A NE2 1 
ATOM   4832 N N   . GLY A 1 604 ? 47.548 89.912  44.762  1.00 24.32 ? 604  GLY A N   1 
ATOM   4833 C CA  . GLY A 1 604 ? 47.962 88.933  45.757  1.00 26.05 ? 604  GLY A CA  1 
ATOM   4834 C C   . GLY A 1 604 ? 49.453 88.694  45.906  1.00 27.37 ? 604  GLY A C   1 
ATOM   4835 O O   . GLY A 1 604 ? 49.895 88.316  46.982  1.00 29.16 ? 604  GLY A O   1 
ATOM   4836 N N   . TYR A 1 605 ? 50.243 88.926  44.852  1.00 26.94 ? 605  TYR A N   1 
ATOM   4837 C CA  . TYR A 1 605 ? 51.674 88.600  44.872  1.00 26.54 ? 605  TYR A CA  1 
ATOM   4838 C C   . TYR A 1 605 ? 52.413 89.520  45.805  1.00 26.17 ? 605  TYR A C   1 
ATOM   4839 O O   . TYR A 1 605 ? 51.928 90.611  46.084  1.00 26.08 ? 605  TYR A O   1 
ATOM   4840 C CB  . TYR A 1 605 ? 52.281 88.666  43.445  1.00 25.98 ? 605  TYR A CB  1 
ATOM   4841 C CG  . TYR A 1 605 ? 51.484 87.844  42.482  1.00 25.04 ? 605  TYR A CG  1 
ATOM   4842 C CD1 . TYR A 1 605 ? 51.363 86.469  42.658  1.00 25.06 ? 605  TYR A CD1 1 
ATOM   4843 C CD2 . TYR A 1 605 ? 50.775 88.452  41.431  1.00 25.62 ? 605  TYR A CD2 1 
ATOM   4844 C CE1 . TYR A 1 605 ? 50.569 85.693  41.776  1.00 27.81 ? 605  TYR A CE1 1 
ATOM   4845 C CE2 . TYR A 1 605 ? 49.985 87.701  40.557  1.00 25.38 ? 605  TYR A CE2 1 
ATOM   4846 C CZ  . TYR A 1 605 ? 49.890 86.328  40.738  1.00 25.63 ? 605  TYR A CZ  1 
ATOM   4847 O OH  . TYR A 1 605 ? 49.131 85.598  39.882  1.00 27.39 ? 605  TYR A OH  1 
ATOM   4848 N N   . LYS A 1 606 ? 53.582 89.085  46.274  1.00 26.62 ? 606  LYS A N   1 
ATOM   4849 C CA  . LYS A 1 606 ? 54.409 89.922  47.166  1.00 28.51 ? 606  LYS A CA  1 
ATOM   4850 C C   . LYS A 1 606 ? 54.725 91.278  46.546  1.00 27.61 ? 606  LYS A C   1 
ATOM   4851 O O   . LYS A 1 606 ? 54.822 91.386  45.312  1.00 26.96 ? 606  LYS A O   1 
ATOM   4852 C CB  . LYS A 1 606 ? 55.661 89.169  47.626  1.00 28.36 ? 606  LYS A CB  1 
ATOM   4853 C CG  . LYS A 1 606 ? 56.963 89.408  46.892  1.00 31.74 ? 606  LYS A CG  1 
ATOM   4854 C CD  . LYS A 1 606 ? 58.134 88.772  47.723  1.00 31.90 ? 606  LYS A CD  1 
ATOM   4855 C CE  . LYS A 1 606 ? 59.527 89.206  47.210  1.00 38.23 ? 606  LYS A CE  1 
ATOM   4856 N NZ  . LYS A 1 606 ? 60.560 89.060  48.296  1.00 40.24 ? 606  LYS A NZ  1 
ATOM   4857 N N   . ASP A 1 607 ? 54.849 92.313  47.390  1.00 27.00 ? 607  ASP A N   1 
ATOM   4858 C CA  . ASP A 1 607 ? 55.160 93.674  46.916  1.00 26.11 ? 607  ASP A CA  1 
ATOM   4859 C C   . ASP A 1 607 ? 56.363 93.606  46.009  1.00 24.46 ? 607  ASP A C   1 
ATOM   4860 O O   . ASP A 1 607 ? 57.304 92.846  46.304  1.00 24.07 ? 607  ASP A O   1 
ATOM   4861 C CB  . ASP A 1 607 ? 55.541 94.605  48.062  1.00 26.89 ? 607  ASP A CB  1 
ATOM   4862 C CG  . ASP A 1 607 ? 54.403 94.864  49.038  1.00 30.49 ? 607  ASP A CG  1 
ATOM   4863 O OD1 . ASP A 1 607 ? 53.204 94.720  48.668  1.00 30.77 ? 607  ASP A OD1 1 
ATOM   4864 O OD2 . ASP A 1 607 ? 54.743 95.235  50.193  1.00 33.09 ? 607  ASP A OD2 1 
ATOM   4865 N N   . GLN A 1 608 ? 56.345 94.376  44.913  1.00 23.19 ? 608  GLN A N   1 
ATOM   4866 C CA  . GLN A 1 608 ? 57.558 94.492  44.070  1.00 22.20 ? 608  GLN A CA  1 
ATOM   4867 C C   . GLN A 1 608 ? 57.961 95.921  43.707  1.00 21.93 ? 608  GLN A C   1 
ATOM   4868 O O   . GLN A 1 608 ? 58.779 96.097  42.804  1.00 22.21 ? 608  GLN A O   1 
ATOM   4869 C CB  . GLN A 1 608 ? 57.465 93.614  42.814  1.00 21.91 ? 608  GLN A CB  1 
ATOM   4870 C CG  . GLN A 1 608 ? 56.447 94.074  41.782  1.00 20.33 ? 608  GLN A CG  1 
ATOM   4871 C CD  . GLN A 1 608 ? 56.199 93.033  40.688  1.00 20.91 ? 608  GLN A CD  1 
ATOM   4872 O OE1 . GLN A 1 608 ? 56.189 91.824  40.945  1.00 23.46 ? 608  GLN A OE1 1 
ATOM   4873 N NE2 . GLN A 1 608 ? 56.008 93.497  39.467  1.00 17.92 ? 608  GLN A NE2 1 
ATOM   4874 N N   . ASP A 1 609 ? 57.383 96.917  44.391  1.00 21.28 ? 609  ASP A N   1 
ATOM   4875 C CA  . ASP A 1 609 ? 57.810 98.307  44.267  1.00 21.47 ? 609  ASP A CA  1 
ATOM   4876 C C   . ASP A 1 609 ? 59.252 98.417  44.793  1.00 21.70 ? 609  ASP A C   1 
ATOM   4877 O O   . ASP A 1 609 ? 59.644 97.662  45.698  1.00 21.47 ? 609  ASP A O   1 
ATOM   4878 C CB  . ASP A 1 609 ? 56.847 99.264  45.010  1.00 22.51 ? 609  ASP A CB  1 
ATOM   4879 C CG  . ASP A 1 609 ? 56.709 98.941  46.499  1.00 22.07 ? 609  ASP A CG  1 
ATOM   4880 O OD1 . ASP A 1 609 ? 55.924 98.023  46.875  1.00 22.87 ? 609  ASP A OD1 1 
ATOM   4881 O OD2 . ASP A 1 609 ? 57.362 99.635  47.292  1.00 21.80 ? 609  ASP A OD2 1 
ATOM   4882 N N   . PRO A 1 610 ? 60.070 99.304  44.194  1.00 21.51 ? 610  PRO A N   1 
ATOM   4883 C CA  . PRO A 1 610 ? 61.474 99.304  44.583  1.00 21.73 ? 610  PRO A CA  1 
ATOM   4884 C C   . PRO A 1 610 ? 61.779 99.431  46.082  1.00 22.22 ? 610  PRO A C   1 
ATOM   4885 O O   . PRO A 1 610 ? 62.633 98.692  46.576  1.00 21.70 ? 610  PRO A O   1 
ATOM   4886 C CB  . PRO A 1 610 ? 62.070 100.470 43.761  1.00 22.03 ? 610  PRO A CB  1 
ATOM   4887 C CG  . PRO A 1 610 ? 61.141 100.525 42.549  1.00 21.32 ? 610  PRO A CG  1 
ATOM   4888 C CD  . PRO A 1 610 ? 59.797 100.251 43.093  1.00 20.45 ? 610  PRO A CD  1 
ATOM   4889 N N   . ALA A 1 611 ? 61.111 100.343 46.796  1.00 22.62 ? 611  ALA A N   1 
ATOM   4890 C CA  . ALA A 1 611 ? 61.421 100.564 48.218  1.00 23.35 ? 611  ALA A CA  1 
ATOM   4891 C C   . ALA A 1 611 ? 61.024 99.363  49.077  1.00 24.17 ? 611  ALA A C   1 
ATOM   4892 O O   . ALA A 1 611 ? 61.552 99.199  50.171  1.00 24.31 ? 611  ALA A O   1 
ATOM   4893 C CB  . ALA A 1 611 ? 60.753 101.834 48.748  1.00 23.46 ? 611  ALA A CB  1 
ATOM   4894 N N   . SER A 1 612 ? 60.132 98.503  48.567  1.00 23.52 ? 612  SER A N   1 
ATOM   4895 C CA  . SER A 1 612 ? 59.702 97.349  49.314  1.00 23.77 ? 612  SER A CA  1 
ATOM   4896 C C   . SER A 1 612 ? 60.849 96.363  49.574  1.00 24.80 ? 612  SER A C   1 
ATOM   4897 O O   . SER A 1 612 ? 60.764 95.516  50.471  1.00 25.27 ? 612  SER A O   1 
ATOM   4898 C CB  . SER A 1 612 ? 58.481 96.677  48.642  1.00 23.26 ? 612  SER A CB  1 
ATOM   4899 O OG  . SER A 1 612 ? 58.864 95.787  47.614  1.00 23.27 ? 612  SER A OG  1 
ATOM   4900 N N   . PHE A 1 613 ? 61.934 96.487  48.815  1.00 25.40 ? 613  PHE A N   1 
ATOM   4901 C CA  . PHE A 1 613 ? 63.053 95.565  48.919  1.00 25.97 ? 613  PHE A CA  1 
ATOM   4902 C C   . PHE A 1 613 ? 64.006 95.988  50.028  1.00 27.46 ? 613  PHE A C   1 
ATOM   4903 O O   . PHE A 1 613 ? 64.958 95.257  50.353  1.00 27.88 ? 613  PHE A O   1 
ATOM   4904 C CB  . PHE A 1 613 ? 63.761 95.423  47.556  1.00 24.84 ? 613  PHE A CB  1 
ATOM   4905 C CG  . PHE A 1 613 ? 62.955 94.641  46.545  1.00 24.48 ? 613  PHE A CG  1 
ATOM   4906 C CD1 . PHE A 1 613 ? 63.139 93.265  46.400  1.00 22.61 ? 613  PHE A CD1 1 
ATOM   4907 C CD2 . PHE A 1 613 ? 61.984 95.275  45.745  1.00 23.76 ? 613  PHE A CD2 1 
ATOM   4908 C CE1 . PHE A 1 613 ? 62.391 92.524  45.481  1.00 20.22 ? 613  PHE A CE1 1 
ATOM   4909 C CE2 . PHE A 1 613 ? 61.228 94.528  44.806  1.00 21.29 ? 613  PHE A CE2 1 
ATOM   4910 C CZ  . PHE A 1 613 ? 61.427 93.159  44.687  1.00 21.43 ? 613  PHE A CZ  1 
ATOM   4911 N N   . GLY A 1 614 ? 63.743 97.163  50.617  1.00 28.44 ? 614  GLY A N   1 
ATOM   4912 C CA  . GLY A 1 614 ? 64.511 97.637  51.780  1.00 29.70 ? 614  GLY A CA  1 
ATOM   4913 C C   . GLY A 1 614 ? 65.195 98.956  51.500  1.00 30.49 ? 614  GLY A C   1 
ATOM   4914 O O   . GLY A 1 614 ? 65.747 99.149  50.420  1.00 31.09 ? 614  GLY A O   1 
ATOM   4915 N N   . ALA A 1 615 ? 65.186 99.860  52.476  1.00 31.25 ? 615  ALA A N   1 
ATOM   4916 C CA  . ALA A 1 615 ? 65.665 101.240 52.271  1.00 31.45 ? 615  ALA A CA  1 
ATOM   4917 C C   . ALA A 1 615 ? 67.146 101.308 51.985  1.00 31.67 ? 615  ALA A C   1 
ATOM   4918 O O   . ALA A 1 615 ? 67.646 102.318 51.489  1.00 31.83 ? 615  ALA A O   1 
ATOM   4919 C CB  . ALA A 1 615 ? 65.303 102.132 53.453  1.00 32.18 ? 615  ALA A CB  1 
ATOM   4920 N N   . ASP A 1 616 ? 67.860 100.236 52.283  1.00 31.73 ? 616  ASP A N   1 
ATOM   4921 C CA  . ASP A 1 616 ? 69.285 100.220 51.992  1.00 32.41 ? 616  ASP A CA  1 
ATOM   4922 C C   . ASP A 1 616 ? 69.687 99.068  51.079  1.00 30.56 ? 616  ASP A C   1 
ATOM   4923 O O   . ASP A 1 616 ? 70.859 98.736  50.967  1.00 31.17 ? 616  ASP A O   1 
ATOM   4924 C CB  . ASP A 1 616 ? 70.107 100.294 53.301  1.00 34.31 ? 616  ASP A CB  1 
ATOM   4925 C CG  . ASP A 1 616 ? 69.727 101.543 54.162  1.00 40.49 ? 616  ASP A CG  1 
ATOM   4926 O OD1 . ASP A 1 616 ? 69.445 101.390 55.391  1.00 47.83 ? 616  ASP A OD1 1 
ATOM   4927 O OD2 . ASP A 1 616 ? 69.672 102.687 53.602  1.00 45.81 ? 616  ASP A OD2 1 
ATOM   4928 N N   . SER A 1 617 ? 68.706 98.510  50.369  1.00 29.04 ? 617  SER A N   1 
ATOM   4929 C CA  . SER A 1 617 ? 68.928 97.345  49.528  1.00 26.59 ? 617  SER A CA  1 
ATOM   4930 C C   . SER A 1 617 ? 69.639 97.702  48.215  1.00 25.63 ? 617  SER A C   1 
ATOM   4931 O O   . SER A 1 617 ? 69.470 98.804  47.689  1.00 25.85 ? 617  SER A O   1 
ATOM   4932 C CB  . SER A 1 617 ? 67.606 96.659  49.225  1.00 25.68 ? 617  SER A CB  1 
ATOM   4933 O OG  . SER A 1 617 ? 66.796 97.473  48.383  1.00 23.77 ? 617  SER A OG  1 
ATOM   4934 N N   . LEU A 1 618 ? 70.391 96.746  47.684  1.00 24.45 ? 618  LEU A N   1 
ATOM   4935 C CA  . LEU A 1 618 ? 70.999 96.881  46.393  1.00 24.38 ? 618  LEU A CA  1 
ATOM   4936 C C   . LEU A 1 618 ? 69.952 97.186  45.313  1.00 24.00 ? 618  LEU A C   1 
ATOM   4937 O O   . LEU A 1 618 ? 70.233 97.978  44.409  1.00 24.37 ? 618  LEU A O   1 
ATOM   4938 C CB  . LEU A 1 618 ? 71.836 95.650  46.017  1.00 24.09 ? 618  LEU A CB  1 
ATOM   4939 C CG  . LEU A 1 618 ? 72.677 95.859  44.746  1.00 24.75 ? 618  LEU A CG  1 
ATOM   4940 C CD1 . LEU A 1 618 ? 73.812 96.863  45.009  1.00 28.89 ? 618  LEU A CD1 1 
ATOM   4941 C CD2 . LEU A 1 618 ? 73.234 94.564  44.260  1.00 24.80 ? 618  LEU A CD2 1 
ATOM   4942 N N   . LEU A 1 619 ? 68.773 96.561  45.381  1.00 21.80 ? 619  LEU A N   1 
ATOM   4943 C CA  . LEU A 1 619 ? 67.795 96.760  44.332  1.00 21.13 ? 619  LEU A CA  1 
ATOM   4944 C C   . LEU A 1 619 ? 67.351 98.223  44.327  1.00 21.32 ? 619  LEU A C   1 
ATOM   4945 O O   . LEU A 1 619 ? 67.250 98.838  43.270  1.00 21.19 ? 619  LEU A O   1 
ATOM   4946 C CB  . LEU A 1 619 ? 66.583 95.790  44.467  1.00 21.30 ? 619  LEU A CB  1 
ATOM   4947 C CG  . LEU A 1 619 ? 65.445 95.939  43.433  1.00 20.31 ? 619  LEU A CG  1 
ATOM   4948 C CD1 . LEU A 1 619 ? 64.704 94.612  43.248  1.00 19.89 ? 619  LEU A CD1 1 
ATOM   4949 C CD2 . LEU A 1 619 ? 64.465 97.074  43.762  1.00 20.11 ? 619  LEU A CD2 1 
ATOM   4950 N N   . LEU A 1 620 ? 67.061 98.778  45.507  1.00 21.98 ? 620  LEU A N   1 
ATOM   4951 C CA  . LEU A 1 620 ? 66.605 100.154 45.606  1.00 21.14 ? 620  LEU A CA  1 
ATOM   4952 C C   . LEU A 1 620 ? 67.689 101.129 45.178  1.00 21.86 ? 620  LEU A C   1 
ATOM   4953 O O   . LEU A 1 620 ? 67.416 102.106 44.459  1.00 22.49 ? 620  LEU A O   1 
ATOM   4954 C CB  . LEU A 1 620 ? 66.120 100.480 47.027  1.00 21.55 ? 620  LEU A CB  1 
ATOM   4955 C CG  . LEU A 1 620 ? 65.651 101.923 47.233  1.00 21.53 ? 620  LEU A CG  1 
ATOM   4956 C CD1 . LEU A 1 620 ? 64.444 102.296 46.327  1.00 20.46 ? 620  LEU A CD1 1 
ATOM   4957 C CD2 . LEU A 1 620 ? 65.361 102.254 48.674  1.00 20.90 ? 620  LEU A CD2 1 
ATOM   4958 N N   . ASN A 1 621 ? 68.903 100.901 45.641  1.00 21.96 ? 621  ASN A N   1 
ATOM   4959 C CA  . ASN A 1 621 ? 70.032 101.756 45.293  1.00 23.20 ? 621  ASN A CA  1 
ATOM   4960 C C   . ASN A 1 621 ? 70.280 101.754 43.796  1.00 23.03 ? 621  ASN A C   1 
ATOM   4961 O O   . ASN A 1 621 ? 70.425 102.821 43.175  1.00 23.13 ? 621  ASN A O   1 
ATOM   4962 C CB  . ASN A 1 621 ? 71.306 101.304 46.032  1.00 24.58 ? 621  ASN A CB  1 
ATOM   4963 C CG  . ASN A 1 621 ? 71.250 101.626 47.533  1.00 29.32 ? 621  ASN A CG  1 
ATOM   4964 O OD1 . ASN A 1 621 ? 70.416 102.439 47.966  1.00 34.23 ? 621  ASN A OD1 1 
ATOM   4965 N ND2 . ASN A 1 621 ? 72.155 101.028 48.325  1.00 31.60 ? 621  ASN A ND2 1 
ATOM   4966 N N   . SER A 1 622 ? 70.319 100.554 43.220  1.00 22.52 ? 622  SER A N   1 
ATOM   4967 C CA  . SER A 1 622 ? 70.467 100.394 41.764  1.00 23.17 ? 622  SER A CA  1 
ATOM   4968 C C   . SER A 1 622 ? 69.309 101.002 40.951  1.00 23.02 ? 622  SER A C   1 
ATOM   4969 O O   . SER A 1 622 ? 69.568 101.730 39.993  1.00 23.63 ? 622  SER A O   1 
ATOM   4970 C CB  . SER A 1 622 ? 70.668 98.937  41.387  1.00 23.01 ? 622  SER A CB  1 
ATOM   4971 O OG  . SER A 1 622 ? 71.077 98.887  40.046  1.00 24.90 ? 622  SER A OG  1 
ATOM   4972 N N   . SER A 1 623 ? 68.065 100.738 41.358  1.00 22.24 ? 623  SER A N   1 
ATOM   4973 C CA  . SER A 1 623 ? 66.884 101.368 40.745  1.00 23.05 ? 623  SER A CA  1 
ATOM   4974 C C   . SER A 1 623 ? 66.947 102.887 40.800  1.00 22.57 ? 623  SER A C   1 
ATOM   4975 O O   . SER A 1 623 ? 66.645 103.545 39.819  1.00 22.91 ? 623  SER A O   1 
ATOM   4976 C CB  . SER A 1 623 ? 65.560 100.938 41.439  1.00 23.33 ? 623  SER A CB  1 
ATOM   4977 O OG  . SER A 1 623 ? 65.416 99.534  41.474  1.00 24.80 ? 623  SER A OG  1 
ATOM   4978 N N   . ARG A 1 624 ? 67.319 103.453 41.950  1.00 22.21 ? 624  ARG A N   1 
ATOM   4979 C CA  . ARG A 1 624 ? 67.415 104.907 42.051  1.00 21.69 ? 624  ARG A CA  1 
ATOM   4980 C C   . ARG A 1 624 ? 68.508 105.433 41.144  1.00 20.42 ? 624  ARG A C   1 
ATOM   4981 O O   . ARG A 1 624 ? 68.322 106.435 40.491  1.00 20.05 ? 624  ARG A O   1 
ATOM   4982 C CB  . ARG A 1 624 ? 67.637 105.391 43.502  1.00 21.12 ? 624  ARG A CB  1 
ATOM   4983 C CG  . ARG A 1 624 ? 67.594 106.942 43.668  1.00 22.29 ? 624  ARG A CG  1 
ATOM   4984 C CD  . ARG A 1 624 ? 67.828 107.388 45.134  1.00 26.06 ? 624  ARG A CD  1 
ATOM   4985 N NE  . ARG A 1 624 ? 68.767 106.485 45.778  1.00 31.40 ? 624  ARG A NE  1 
ATOM   4986 C CZ  . ARG A 1 624 ? 68.523 105.761 46.857  1.00 31.24 ? 624  ARG A CZ  1 
ATOM   4987 N NH1 . ARG A 1 624 ? 67.389 105.863 47.520  1.00 30.25 ? 624  ARG A NH1 1 
ATOM   4988 N NH2 . ARG A 1 624 ? 69.468 104.955 47.300  1.00 33.29 ? 624  ARG A NH2 1 
ATOM   4989 N N   . HIS A 1 625 ? 69.652 104.764 41.132  1.00 19.77 ? 625  HIS A N   1 
ATOM   4990 C CA  . HIS A 1 625 ? 70.782 105.177 40.303  1.00 19.70 ? 625  HIS A CA  1 
ATOM   4991 C C   . HIS A 1 625 ? 70.439 105.315 38.797  1.00 17.95 ? 625  HIS A C   1 
ATOM   4992 O O   . HIS A 1 625 ? 70.761 106.313 38.170  1.00 16.83 ? 625  HIS A O   1 
ATOM   4993 C CB  . HIS A 1 625 ? 71.919 104.163 40.467  1.00 19.87 ? 625  HIS A CB  1 
ATOM   4994 C CG  . HIS A 1 625 ? 73.200 104.599 39.817  1.00 24.84 ? 625  HIS A CG  1 
ATOM   4995 N ND1 . HIS A 1 625 ? 73.682 104.026 38.661  1.00 26.51 ? 625  HIS A ND1 1 
ATOM   4996 C CD2 . HIS A 1 625 ? 74.080 105.570 40.149  1.00 22.99 ? 625  HIS A CD2 1 
ATOM   4997 C CE1 . HIS A 1 625 ? 74.805 104.616 38.315  1.00 22.16 ? 625  HIS A CE1 1 
ATOM   4998 N NE2 . HIS A 1 625 ? 75.075 105.547 39.207  1.00 26.52 ? 625  HIS A NE2 1 
ATOM   4999 N N   . TYR A 1 626 ? 69.777 104.300 38.233  1.00 17.55 ? 626  TYR A N   1 
ATOM   5000 C CA  . TYR A 1 626 ? 69.498 104.248 36.792  1.00 16.38 ? 626  TYR A CA  1 
ATOM   5001 C C   . TYR A 1 626 ? 68.270 105.058 36.417  1.00 16.70 ? 626  TYR A C   1 
ATOM   5002 O O   . TYR A 1 626 ? 68.192 105.611 35.320  1.00 16.69 ? 626  TYR A O   1 
ATOM   5003 C CB  . TYR A 1 626 ? 69.434 102.778 36.305  1.00 17.56 ? 626  TYR A CB  1 
ATOM   5004 C CG  . TYR A 1 626 ? 70.847 102.232 36.193  1.00 16.04 ? 626  TYR A CG  1 
ATOM   5005 C CD1 . TYR A 1 626 ? 71.303 101.233 37.059  1.00 17.78 ? 626  TYR A CD1 1 
ATOM   5006 C CD2 . TYR A 1 626 ? 71.752 102.791 35.276  1.00 18.69 ? 626  TYR A CD2 1 
ATOM   5007 C CE1 . TYR A 1 626 ? 72.613 100.742 36.973  1.00 18.72 ? 626  TYR A CE1 1 
ATOM   5008 C CE2 . TYR A 1 626 ? 73.092 102.322 35.185  1.00 16.67 ? 626  TYR A CE2 1 
ATOM   5009 C CZ  . TYR A 1 626 ? 73.502 101.319 36.048  1.00 17.03 ? 626  TYR A CZ  1 
ATOM   5010 O OH  . TYR A 1 626 ? 74.760 100.823 35.967  1.00 19.30 ? 626  TYR A OH  1 
ATOM   5011 N N   . LEU A 1 627 ? 67.312 105.149 37.339  1.00 17.11 ? 627  LEU A N   1 
ATOM   5012 C CA  . LEU A 1 627 ? 66.188 106.087 37.157  1.00 16.81 ? 627  LEU A CA  1 
ATOM   5013 C C   . LEU A 1 627 ? 66.704 107.505 37.193  1.00 17.78 ? 627  LEU A C   1 
ATOM   5014 O O   . LEU A 1 627 ? 66.222 108.334 36.453  1.00 18.58 ? 627  LEU A O   1 
ATOM   5015 C CB  . LEU A 1 627 ? 65.109 105.820 38.215  1.00 17.20 ? 627  LEU A CB  1 
ATOM   5016 C CG  . LEU A 1 627 ? 64.231 104.590 37.927  1.00 16.59 ? 627  LEU A CG  1 
ATOM   5017 C CD1 . LEU A 1 627 ? 63.168 104.509 39.024  1.00 16.73 ? 627  LEU A CD1 1 
ATOM   5018 C CD2 . LEU A 1 627 ? 63.572 104.775 36.565  1.00 18.31 ? 627  LEU A CD2 1 
ATOM   5019 N N   . ASN A 1 628 ? 67.719 107.802 38.019  1.00 18.31 ? 628  ASN A N   1 
ATOM   5020 C CA  . ASN A 1 628 ? 68.332 109.148 37.963  1.00 18.78 ? 628  ASN A CA  1 
ATOM   5021 C C   . ASN A 1 628 ? 69.067 109.446 36.639  1.00 18.24 ? 628  ASN A C   1 
ATOM   5022 O O   . ASN A 1 628 ? 69.037 110.576 36.146  1.00 18.95 ? 628  ASN A O   1 
ATOM   5023 C CB  . ASN A 1 628 ? 69.305 109.361 39.133  1.00 19.59 ? 628  ASN A CB  1 
ATOM   5024 C CG  . ASN A 1 628 ? 68.630 109.913 40.373  1.00 22.98 ? 628  ASN A CG  1 
ATOM   5025 O OD1 . ASN A 1 628 ? 68.976 109.513 41.507  1.00 25.94 ? 628  ASN A OD1 1 
ATOM   5026 N ND2 . ASN A 1 628 ? 67.680 110.837 40.186  1.00 20.39 ? 628  ASN A ND2 1 
ATOM   5027 N N   . ILE A 1 629 ? 69.781 108.447 36.101  1.00 18.16 ? 629  ILE A N   1 
ATOM   5028 C CA  . ILE A 1 629 ? 70.314 108.534 34.739  1.00 16.61 ? 629  ILE A CA  1 
ATOM   5029 C C   . ILE A 1 629 ? 69.199 108.735 33.687  1.00 16.72 ? 629  ILE A C   1 
ATOM   5030 O O   . ILE A 1 629 ? 69.294 109.618 32.842  1.00 15.76 ? 629  ILE A O   1 
ATOM   5031 C CB  . ILE A 1 629 ? 71.226 107.343 34.400  1.00 17.08 ? 629  ILE A CB  1 
ATOM   5032 C CG1 . ILE A 1 629 ? 72.487 107.404 35.277  1.00 16.24 ? 629  ILE A CG1 1 
ATOM   5033 C CG2 . ILE A 1 629 ? 71.636 107.376 32.875  1.00 16.07 ? 629  ILE A CG2 1 
ATOM   5034 C CD1 . ILE A 1 629 ? 73.213 106.095 35.314  1.00 17.18 ? 629  ILE A CD1 1 
ATOM   5035 N N   . ARG A 1 630 ? 68.127 107.922 33.741  1.00 16.19 ? 630  ARG A N   1 
ATOM   5036 C CA  . ARG A 1 630 ? 66.999 108.137 32.823  1.00 15.33 ? 630  ARG A CA  1 
ATOM   5037 C C   . ARG A 1 630 ? 66.539 109.578 32.893  1.00 16.47 ? 630  ARG A C   1 
ATOM   5038 O O   . ARG A 1 630 ? 66.370 110.253 31.871  1.00 16.14 ? 630  ARG A O   1 
ATOM   5039 C CB  . ARG A 1 630 ? 65.818 107.234 33.222  1.00 15.97 ? 630  ARG A CB  1 
ATOM   5040 C CG  . ARG A 1 630 ? 64.542 107.536 32.411  1.00 14.00 ? 630  ARG A CG  1 
ATOM   5041 C CD  . ARG A 1 630 ? 63.289 106.887 33.035  1.00 16.38 ? 630  ARG A CD  1 
ATOM   5042 N NE  . ARG A 1 630 ? 62.150 107.039 32.137  1.00 14.88 ? 630  ARG A NE  1 
ATOM   5043 C CZ  . ARG A 1 630 ? 61.899 106.250 31.090  1.00 16.07 ? 630  ARG A CZ  1 
ATOM   5044 N NH1 . ARG A 1 630 ? 62.721 105.220 30.777  1.00 14.08 ? 630  ARG A NH1 1 
ATOM   5045 N NH2 . ARG A 1 630 ? 60.814 106.500 30.348  1.00 15.59 ? 630  ARG A NH2 1 
ATOM   5046 N N   . TYR A 1 631 ? 66.324 110.074 34.112  1.00 16.82 ? 631  TYR A N   1 
ATOM   5047 C CA  . TYR A 1 631 ? 65.823 111.446 34.262  1.00 17.29 ? 631  TYR A CA  1 
ATOM   5048 C C   . TYR A 1 631 ? 66.866 112.464 33.785  1.00 17.23 ? 631  TYR A C   1 
ATOM   5049 O O   . TYR A 1 631 ? 66.531 113.483 33.141  1.00 16.21 ? 631  TYR A O   1 
ATOM   5050 C CB  . TYR A 1 631 ? 65.385 111.702 35.708  1.00 17.64 ? 631  TYR A CB  1 
ATOM   5051 C CG  . TYR A 1 631 ? 63.969 111.271 36.061  1.00 19.52 ? 631  TYR A CG  1 
ATOM   5052 C CD1 . TYR A 1 631 ? 63.504 109.981 35.808  1.00 17.87 ? 631  TYR A CD1 1 
ATOM   5053 C CD2 . TYR A 1 631 ? 63.092 112.163 36.692  1.00 19.73 ? 631  TYR A CD2 1 
ATOM   5054 C CE1 . TYR A 1 631 ? 62.170 109.597 36.179  1.00 17.20 ? 631  TYR A CE1 1 
ATOM   5055 C CE2 . TYR A 1 631 ? 61.794 111.781 37.072  1.00 19.11 ? 631  TYR A CE2 1 
ATOM   5056 C CZ  . TYR A 1 631 ? 61.334 110.510 36.803  1.00 18.08 ? 631  TYR A CZ  1 
ATOM   5057 O OH  . TYR A 1 631 ? 60.028 110.154 37.195  1.00 16.82 ? 631  TYR A OH  1 
ATOM   5058 N N   . THR A 1 632 ? 68.148 112.167 34.009  1.00 17.71 ? 632  THR A N   1 
ATOM   5059 C CA  . THR A 1 632 ? 69.166 113.081 33.480  1.00 17.65 ? 632  THR A CA  1 
ATOM   5060 C C   . THR A 1 632 ? 69.026 113.263 31.968  1.00 18.72 ? 632  THR A C   1 
ATOM   5061 O O   . THR A 1 632 ? 69.224 114.352 31.448  1.00 19.28 ? 632  THR A O   1 
ATOM   5062 C CB  . THR A 1 632 ? 70.561 112.569 33.851  1.00 18.50 ? 632  THR A CB  1 
ATOM   5063 O OG1 . THR A 1 632 ? 70.659 112.571 35.273  1.00 17.24 ? 632  THR A OG1 1 
ATOM   5064 C CG2 . THR A 1 632 ? 71.671 113.440 33.253  1.00 17.10 ? 632  THR A CG2 1 
ATOM   5065 N N   . LEU A 1 633 ? 68.672 112.185 31.270  1.00 18.75 ? 633  LEU A N   1 
ATOM   5066 C CA  . LEU A 1 633 ? 68.660 112.140 29.810  1.00 19.30 ? 633  LEU A CA  1 
ATOM   5067 C C   . LEU A 1 633 ? 67.257 112.370 29.281  1.00 19.78 ? 633  LEU A C   1 
ATOM   5068 O O   . LEU A 1 633 ? 67.018 112.208 28.095  1.00 20.30 ? 633  LEU A O   1 
ATOM   5069 C CB  . LEU A 1 633 ? 69.137 110.766 29.319  1.00 19.20 ? 633  LEU A CB  1 
ATOM   5070 C CG  . LEU A 1 633 ? 70.631 110.489 29.510  1.00 18.97 ? 633  LEU A CG  1 
ATOM   5071 C CD1 . LEU A 1 633 ? 70.930 109.000 29.349  1.00 19.40 ? 633  LEU A CD1 1 
ATOM   5072 C CD2 . LEU A 1 633 ? 71.400 111.313 28.454  1.00 21.08 ? 633  LEU A CD2 1 
ATOM   5073 N N   . LEU A 1 634 ? 66.329 112.752 30.151  1.00 19.36 ? 634  LEU A N   1 
ATOM   5074 C CA  . LEU A 1 634 ? 64.988 113.077 29.658  1.00 19.83 ? 634  LEU A CA  1 
ATOM   5075 C C   . LEU A 1 634 ? 64.948 114.136 28.547  1.00 18.86 ? 634  LEU A C   1 
ATOM   5076 O O   . LEU A 1 634 ? 64.169 114.000 27.624  1.00 19.99 ? 634  LEU A O   1 
ATOM   5077 C CB  . LEU A 1 634 ? 64.025 113.421 30.803  1.00 19.64 ? 634  LEU A CB  1 
ATOM   5078 C CG  . LEU A 1 634 ? 63.339 112.260 31.518  1.00 22.01 ? 634  LEU A CG  1 
ATOM   5079 C CD1 . LEU A 1 634 ? 62.144 112.772 32.308  1.00 23.64 ? 634  LEU A CD1 1 
ATOM   5080 C CD2 . LEU A 1 634 ? 62.908 111.169 30.613  1.00 20.73 ? 634  LEU A CD2 1 
ATOM   5081 N N   . PRO A 1 635 ? 65.751 115.223 28.618  1.00 18.48 ? 635  PRO A N   1 
ATOM   5082 C CA  . PRO A 1 635 ? 65.700 116.072 27.401  1.00 17.53 ? 635  PRO A CA  1 
ATOM   5083 C C   . PRO A 1 635 ? 66.085 115.413 26.053  1.00 16.70 ? 635  PRO A C   1 
ATOM   5084 O O   . PRO A 1 635 ? 65.539 115.793 25.042  1.00 16.91 ? 635  PRO A O   1 
ATOM   5085 C CB  . PRO A 1 635 ? 66.675 117.220 27.734  1.00 18.16 ? 635  PRO A CB  1 
ATOM   5086 C CG  . PRO A 1 635 ? 66.576 117.299 29.270  1.00 18.05 ? 635  PRO A CG  1 
ATOM   5087 C CD  . PRO A 1 635 ? 66.588 115.838 29.666  1.00 18.29 ? 635  PRO A CD  1 
ATOM   5088 N N   . TYR A 1 636 ? 67.048 114.497 26.065  1.00 15.24 ? 636  TYR A N   1 
ATOM   5089 C CA  . TYR A 1 636 ? 67.400 113.641 24.932  1.00 15.07 ? 636  TYR A CA  1 
ATOM   5090 C C   . TYR A 1 636 ? 66.220 112.683 24.561  1.00 14.32 ? 636  TYR A C   1 
ATOM   5091 O O   . TYR A 1 636 ? 65.783 112.659 23.430  1.00 13.33 ? 636  TYR A O   1 
ATOM   5092 C CB  . TYR A 1 636 ? 68.706 112.833 25.272  1.00 14.61 ? 636  TYR A CB  1 
ATOM   5093 C CG  . TYR A 1 636 ? 69.118 111.850 24.179  1.00 15.94 ? 636  TYR A CG  1 
ATOM   5094 C CD1 . TYR A 1 636 ? 69.609 112.302 22.939  1.00 16.08 ? 636  TYR A CD1 1 
ATOM   5095 C CD2 . TYR A 1 636 ? 69.028 110.475 24.387  1.00 15.76 ? 636  TYR A CD2 1 
ATOM   5096 C CE1 . TYR A 1 636 ? 69.948 111.403 21.914  1.00 14.46 ? 636  TYR A CE1 1 
ATOM   5097 C CE2 . TYR A 1 636 ? 69.392 109.578 23.394  1.00 14.57 ? 636  TYR A CE2 1 
ATOM   5098 C CZ  . TYR A 1 636 ? 69.833 110.037 22.157  1.00 15.70 ? 636  TYR A CZ  1 
ATOM   5099 O OH  . TYR A 1 636 ? 70.154 109.089 21.191  1.00 15.97 ? 636  TYR A OH  1 
ATOM   5100 N N   . LEU A 1 637 ? 65.693 111.922 25.526  1.00 15.38 ? 637  LEU A N   1 
ATOM   5101 C CA  . LEU A 1 637 ? 64.503 111.060 25.266  1.00 14.69 ? 637  LEU A CA  1 
ATOM   5102 C C   . LEU A 1 637 ? 63.335 111.871 24.659  1.00 16.00 ? 637  LEU A C   1 
ATOM   5103 O O   . LEU A 1 637 ? 62.756 111.464 23.658  1.00 16.69 ? 637  LEU A O   1 
ATOM   5104 C CB  . LEU A 1 637 ? 64.053 110.328 26.543  1.00 15.05 ? 637  LEU A CB  1 
ATOM   5105 C CG  . LEU A 1 637 ? 62.908 109.314 26.380  1.00 13.78 ? 637  LEU A CG  1 
ATOM   5106 C CD1 . LEU A 1 637 ? 63.385 108.229 25.371  1.00 12.01 ? 637  LEU A CD1 1 
ATOM   5107 C CD2 . LEU A 1 637 ? 62.558 108.678 27.689  1.00 13.48 ? 637  LEU A CD2 1 
ATOM   5108 N N   . TYR A 1 638 ? 63.004 113.012 25.263  1.00 16.25 ? 638  TYR A N   1 
ATOM   5109 C CA  . TYR A 1 638 ? 61.913 113.880 24.812  1.00 16.25 ? 638  TYR A CA  1 
ATOM   5110 C C   . TYR A 1 638 ? 62.085 114.415 23.396  1.00 16.27 ? 638  TYR A C   1 
ATOM   5111 O O   . TYR A 1 638 ? 61.114 114.545 22.636  1.00 15.63 ? 638  TYR A O   1 
ATOM   5112 C CB  . TYR A 1 638 ? 61.818 115.062 25.767  1.00 16.69 ? 638  TYR A CB  1 
ATOM   5113 C CG  . TYR A 1 638 ? 60.575 115.888 25.624  1.00 19.59 ? 638  TYR A CG  1 
ATOM   5114 C CD1 . TYR A 1 638 ? 59.320 115.302 25.772  1.00 19.57 ? 638  TYR A CD1 1 
ATOM   5115 C CD2 . TYR A 1 638 ? 60.641 117.271 25.394  1.00 20.33 ? 638  TYR A CD2 1 
ATOM   5116 C CE1 . TYR A 1 638 ? 58.182 116.048 25.666  1.00 20.56 ? 638  TYR A CE1 1 
ATOM   5117 C CE2 . TYR A 1 638 ? 59.472 118.036 25.279  1.00 19.69 ? 638  TYR A CE2 1 
ATOM   5118 C CZ  . TYR A 1 638 ? 58.242 117.400 25.424  1.00 19.73 ? 638  TYR A CZ  1 
ATOM   5119 O OH  . TYR A 1 638 ? 57.031 118.094 25.354  1.00 19.16 ? 638  TYR A OH  1 
ATOM   5120 N N   . THR A 1 639 ? 63.326 114.745 23.031  1.00 16.68 ? 639  THR A N   1 
ATOM   5121 C CA  . THR A 1 639 ? 63.634 115.198 21.671  1.00 16.07 ? 639  THR A CA  1 
ATOM   5122 C C   . THR A 1 639 ? 63.449 114.014 20.690  1.00 16.61 ? 639  THR A C   1 
ATOM   5123 O O   . THR A 1 639 ? 62.979 114.188 19.557  1.00 16.59 ? 639  THR A O   1 
ATOM   5124 C CB  . THR A 1 639 ? 65.077 115.821 21.568  1.00 17.16 ? 639  THR A CB  1 
ATOM   5125 O OG1 . THR A 1 639 ? 65.220 116.894 22.522  1.00 17.95 ? 639  THR A OG1 1 
ATOM   5126 C CG2 . THR A 1 639 ? 65.379 116.330 20.137  1.00 13.80 ? 639  THR A CG2 1 
ATOM   5127 N N   . LEU A 1 640 ? 63.794 112.803 21.131  1.00 16.52 ? 640  LEU A N   1 
ATOM   5128 C CA  . LEU A 1 640 ? 63.517 111.612 20.343  1.00 15.30 ? 640  LEU A CA  1 
ATOM   5129 C C   . LEU A 1 640 ? 62.004 111.445 20.068  1.00 15.62 ? 640  LEU A C   1 
ATOM   5130 O O   . LEU A 1 640 ? 61.622 111.090 18.941  1.00 16.78 ? 640  LEU A O   1 
ATOM   5131 C CB  . LEU A 1 640 ? 64.076 110.360 21.022  1.00 14.27 ? 640  LEU A CB  1 
ATOM   5132 C CG  . LEU A 1 640 ? 65.616 110.252 21.087  1.00 12.77 ? 640  LEU A CG  1 
ATOM   5133 C CD1 . LEU A 1 640 ? 65.915 108.923 21.693  1.00 13.66 ? 640  LEU A CD1 1 
ATOM   5134 C CD2 . LEU A 1 640 ? 66.253 110.371 19.705  1.00 11.05 ? 640  LEU A CD2 1 
ATOM   5135 N N   . PHE A 1 641 ? 61.171 111.633 21.090  1.00 15.17 ? 641  PHE A N   1 
ATOM   5136 C CA  . PHE A 1 641 ? 59.688 111.567 20.912  1.00 16.03 ? 641  PHE A CA  1 
ATOM   5137 C C   . PHE A 1 641 ? 59.191 112.707 20.017  1.00 16.46 ? 641  PHE A C   1 
ATOM   5138 O O   . PHE A 1 641 ? 58.215 112.552 19.243  1.00 17.24 ? 641  PHE A O   1 
ATOM   5139 C CB  . PHE A 1 641 ? 58.969 111.627 22.271  1.00 14.94 ? 641  PHE A CB  1 
ATOM   5140 C CG  . PHE A 1 641 ? 58.854 110.300 22.958  1.00 16.07 ? 641  PHE A CG  1 
ATOM   5141 C CD1 . PHE A 1 641 ? 57.892 109.351 22.526  1.00 14.85 ? 641  PHE A CD1 1 
ATOM   5142 C CD2 . PHE A 1 641 ? 59.689 109.978 24.028  1.00 14.30 ? 641  PHE A CD2 1 
ATOM   5143 C CE1 . PHE A 1 641 ? 57.776 108.136 23.155  1.00 13.29 ? 641  PHE A CE1 1 
ATOM   5144 C CE2 . PHE A 1 641 ? 59.581 108.742 24.701  1.00 14.35 ? 641  PHE A CE2 1 
ATOM   5145 C CZ  . PHE A 1 641 ? 58.620 107.789 24.241  1.00 15.22 ? 641  PHE A CZ  1 
ATOM   5146 N N   . PHE A 1 642 ? 59.863 113.856 20.099  1.00 16.21 ? 642  PHE A N   1 
ATOM   5147 C CA  . PHE A 1 642 ? 59.583 114.959 19.157  1.00 17.13 ? 642  PHE A CA  1 
ATOM   5148 C C   . PHE A 1 642 ? 59.795 114.503 17.715  1.00 16.57 ? 642  PHE A C   1 
ATOM   5149 O O   . PHE A 1 642 ? 58.950 114.799 16.865  1.00 17.73 ? 642  PHE A O   1 
ATOM   5150 C CB  . PHE A 1 642 ? 60.407 116.254 19.465  1.00 16.18 ? 642  PHE A CB  1 
ATOM   5151 C CG  . PHE A 1 642 ? 60.557 117.183 18.280  1.00 17.78 ? 642  PHE A CG  1 
ATOM   5152 C CD1 . PHE A 1 642 ? 59.459 117.899 17.787  1.00 16.77 ? 642  PHE A CD1 1 
ATOM   5153 C CD2 . PHE A 1 642 ? 61.808 117.361 17.674  1.00 16.01 ? 642  PHE A CD2 1 
ATOM   5154 C CE1 . PHE A 1 642 ? 59.594 118.760 16.701  1.00 18.72 ? 642  PHE A CE1 1 
ATOM   5155 C CE2 . PHE A 1 642 ? 61.964 118.206 16.605  1.00 16.83 ? 642  PHE A CE2 1 
ATOM   5156 C CZ  . PHE A 1 642 ? 60.841 118.942 16.114  1.00 18.16 ? 642  PHE A CZ  1 
ATOM   5157 N N   . ARG A 1 643 ? 60.911 113.813 17.431  1.00 16.46 ? 643  ARG A N   1 
ATOM   5158 C CA  . ARG A 1 643 ? 61.211 113.348 16.053  1.00 16.22 ? 643  ARG A CA  1 
ATOM   5159 C C   . ARG A 1 643 ? 60.203 112.265 15.613  1.00 16.52 ? 643  ARG A C   1 
ATOM   5160 O O   . ARG A 1 643 ? 59.700 112.288 14.496  1.00 17.08 ? 643  ARG A O   1 
ATOM   5161 C CB  . ARG A 1 643 ? 62.685 112.906 15.905  1.00 16.39 ? 643  ARG A CB  1 
ATOM   5162 C CG  . ARG A 1 643 ? 63.725 114.051 16.043  1.00 17.70 ? 643  ARG A CG  1 
ATOM   5163 C CD  . ARG A 1 643 ? 63.501 115.133 14.974  1.00 19.93 ? 643  ARG A CD  1 
ATOM   5164 N NE  . ARG A 1 643 ? 64.669 116.008 14.863  1.00 25.59 ? 643  ARG A NE  1 
ATOM   5165 C CZ  . ARG A 1 643 ? 64.750 117.090 14.092  1.00 26.46 ? 643  ARG A CZ  1 
ATOM   5166 N NH1 . ARG A 1 643 ? 63.727 117.482 13.334  1.00 27.33 ? 643  ARG A NH1 1 
ATOM   5167 N NH2 . ARG A 1 643 ? 65.864 117.793 14.094  1.00 26.81 ? 643  ARG A NH2 1 
ATOM   5168 N N   . ALA A 1 644 ? 59.813 111.391 16.546  1.00 16.33 ? 644  ALA A N   1 
ATOM   5169 C CA  . ALA A 1 644 ? 58.797 110.386 16.279  1.00 15.30 ? 644  ALA A CA  1 
ATOM   5170 C C   . ALA A 1 644 ? 57.473 111.057 15.889  1.00 16.37 ? 644  ALA A C   1 
ATOM   5171 O O   . ALA A 1 644 ? 56.816 110.678 14.906  1.00 15.53 ? 644  ALA A O   1 
ATOM   5172 C CB  . ALA A 1 644 ? 58.633 109.477 17.513  1.00 14.88 ? 644  ALA A CB  1 
ATOM   5173 N N   . HIS A 1 645 ? 57.086 112.056 16.672  1.00 17.28 ? 645  HIS A N   1 
ATOM   5174 C CA  . HIS A 1 645 ? 55.831 112.780 16.476  1.00 17.54 ? 645  HIS A CA  1 
ATOM   5175 C C   . HIS A 1 645 ? 55.803 113.599 15.184  1.00 17.98 ? 645  HIS A C   1 
ATOM   5176 O O   . HIS A 1 645 ? 54.793 113.640 14.472  1.00 17.96 ? 645  HIS A O   1 
ATOM   5177 C CB  . HIS A 1 645 ? 55.591 113.665 17.713  1.00 18.32 ? 645  HIS A CB  1 
ATOM   5178 C CG  . HIS A 1 645 ? 54.456 114.636 17.569  1.00 20.50 ? 645  HIS A CG  1 
ATOM   5179 N ND1 . HIS A 1 645 ? 53.139 114.232 17.478  1.00 20.20 ? 645  HIS A ND1 1 
ATOM   5180 C CD2 . HIS A 1 645 ? 54.441 115.992 17.547  1.00 22.24 ? 645  HIS A CD2 1 
ATOM   5181 C CE1 . HIS A 1 645 ? 52.365 115.302 17.373  1.00 25.05 ? 645  HIS A CE1 1 
ATOM   5182 N NE2 . HIS A 1 645 ? 53.131 116.383 17.420  1.00 24.84 ? 645  HIS A NE2 1 
ATOM   5183 N N   . SER A 1 646 ? 56.916 114.246 14.856  1.00 18.47 ? 646  SER A N   1 
ATOM   5184 C CA  . SER A 1 646 ? 56.952 115.167 13.717  1.00 18.99 ? 646  SER A CA  1 
ATOM   5185 C C   . SER A 1 646 ? 57.506 114.520 12.430  1.00 19.94 ? 646  SER A C   1 
ATOM   5186 O O   . SER A 1 646 ? 57.094 114.873 11.334  1.00 20.69 ? 646  SER A O   1 
ATOM   5187 C CB  . SER A 1 646 ? 57.815 116.384 14.074  1.00 19.16 ? 646  SER A CB  1 
ATOM   5188 O OG  . SER A 1 646 ? 59.143 115.959 14.288  1.00 20.04 ? 646  SER A OG  1 
ATOM   5189 N N   . ARG A 1 647 ? 58.430 113.574 12.553  1.00 20.50 ? 647  ARG A N   1 
ATOM   5190 C CA  . ARG A 1 647 ? 59.076 113.013 11.370  1.00 21.20 ? 647  ARG A CA  1 
ATOM   5191 C C   . ARG A 1 647 ? 58.809 111.504 11.235  1.00 20.68 ? 647  ARG A C   1 
ATOM   5192 O O   . ARG A 1 647 ? 58.926 110.950 10.164  1.00 20.84 ? 647  ARG A O   1 
ATOM   5193 C CB  . ARG A 1 647 ? 60.576 113.337 11.421  1.00 21.60 ? 647  ARG A CB  1 
ATOM   5194 C CG  . ARG A 1 647 ? 61.433 112.721 10.328  1.00 24.53 ? 647  ARG A CG  1 
ATOM   5195 C CD  . ARG A 1 647 ? 62.783 113.438 10.287  1.00 24.31 ? 647  ARG A CD  1 
ATOM   5196 N NE  . ARG A 1 647 ? 63.649 113.001 11.378  1.00 24.77 ? 647  ARG A NE  1 
ATOM   5197 C CZ  . ARG A 1 647 ? 64.748 113.623 11.789  1.00 22.78 ? 647  ARG A CZ  1 
ATOM   5198 N NH1 . ARG A 1 647 ? 65.144 114.746 11.220  1.00 24.77 ? 647  ARG A NH1 1 
ATOM   5199 N NH2 . ARG A 1 647 ? 65.457 113.106 12.784  1.00 23.83 ? 647  ARG A NH2 1 
ATOM   5200 N N   . GLY A 1 648 ? 58.481 110.836 12.324  1.00 19.98 ? 648  GLY A N   1 
ATOM   5201 C CA  . GLY A 1 648 ? 58.214 109.412 12.261  1.00 21.13 ? 648  GLY A CA  1 
ATOM   5202 C C   . GLY A 1 648 ? 59.350 108.456 12.605  1.00 21.14 ? 648  GLY A C   1 
ATOM   5203 O O   . GLY A 1 648 ? 59.239 107.276 12.349  1.00 21.62 ? 648  GLY A O   1 
ATOM   5204 N N   . ASP A 1 649 ? 60.432 108.966 13.186  1.00 21.00 ? 649  ASP A N   1 
ATOM   5205 C CA  . ASP A 1 649 ? 61.551 108.174 13.673  1.00 21.01 ? 649  ASP A CA  1 
ATOM   5206 C C   . ASP A 1 649 ? 61.096 107.198 14.767  1.00 20.91 ? 649  ASP A C   1 
ATOM   5207 O O   . ASP A 1 649 ? 60.106 107.430 15.421  1.00 22.01 ? 649  ASP A O   1 
ATOM   5208 C CB  . ASP A 1 649 ? 62.608 109.120 14.301  1.00 21.31 ? 649  ASP A CB  1 
ATOM   5209 C CG  . ASP A 1 649 ? 63.243 110.120 13.292  1.00 23.00 ? 649  ASP A CG  1 
ATOM   5210 O OD1 . ASP A 1 649 ? 62.643 110.479 12.266  1.00 26.09 ? 649  ASP A OD1 1 
ATOM   5211 O OD2 . ASP A 1 649 ? 64.391 110.541 13.539  1.00 28.45 ? 649  ASP A OD2 1 
ATOM   5212 N N   . THR A 1 650 ? 61.883 106.148 15.020  1.00 20.14 ? 650  THR A N   1 
ATOM   5213 C CA  . THR A 1 650 ? 61.684 105.271 16.186  1.00 18.81 ? 650  THR A CA  1 
ATOM   5214 C C   . THR A 1 650 ? 62.333 105.932 17.391  1.00 18.54 ? 650  THR A C   1 
ATOM   5215 O O   . THR A 1 650 ? 63.200 106.783 17.223  1.00 17.99 ? 650  THR A O   1 
ATOM   5216 C CB  . THR A 1 650 ? 62.334 103.870 15.973  1.00 18.19 ? 650  THR A CB  1 
ATOM   5217 O OG1 . THR A 1 650 ? 63.719 104.064 15.638  1.00 17.23 ? 650  THR A OG1 1 
ATOM   5218 C CG2 . THR A 1 650 ? 61.603 103.109 14.833  1.00 18.27 ? 650  THR A CG2 1 
ATOM   5219 N N   . VAL A 1 651 ? 61.956 105.496 18.592  1.00 17.81 ? 651  VAL A N   1 
ATOM   5220 C CA  . VAL A 1 651 ? 62.567 106.003 19.826  1.00 16.89 ? 651  VAL A CA  1 
ATOM   5221 C C   . VAL A 1 651 ? 63.513 104.941 20.380  1.00 17.08 ? 651  VAL A C   1 
ATOM   5222 O O   . VAL A 1 651 ? 64.745 105.137 20.395  1.00 17.02 ? 651  VAL A O   1 
ATOM   5223 C CB  . VAL A 1 651 ? 61.478 106.479 20.883  1.00 16.81 ? 651  VAL A CB  1 
ATOM   5224 C CG1 . VAL A 1 651 ? 62.155 106.924 22.157  1.00 17.30 ? 651  VAL A CG1 1 
ATOM   5225 C CG2 . VAL A 1 651 ? 60.646 107.603 20.311  1.00 14.18 ? 651  VAL A CG2 1 
ATOM   5226 N N   . ALA A 1 652 ? 62.943 103.825 20.843  1.00 17.57 ? 652  ALA A N   1 
ATOM   5227 C CA  . ALA A 1 652 ? 63.699 102.607 21.118  1.00 16.91 ? 652  ALA A CA  1 
ATOM   5228 C C   . ALA A 1 652 ? 63.910 101.964 19.732  1.00 17.99 ? 652  ALA A C   1 
ATOM   5229 O O   . ALA A 1 652 ? 62.917 101.596 19.008  1.00 17.11 ? 652  ALA A O   1 
ATOM   5230 C CB  . ALA A 1 652 ? 62.947 101.669 22.067  1.00 17.17 ? 652  ALA A CB  1 
ATOM   5231 N N   . ARG A 1 653 ? 65.192 101.828 19.394  1.00 17.14 ? 653  ARG A N   1 
ATOM   5232 C CA  . ARG A 1 653 ? 65.674 101.574 18.038  1.00 17.11 ? 653  ARG A CA  1 
ATOM   5233 C C   . ARG A 1 653 ? 66.564 100.333 18.009  1.00 16.97 ? 653  ARG A C   1 
ATOM   5234 O O   . ARG A 1 653 ? 67.422 100.185 18.862  1.00 18.69 ? 653  ARG A O   1 
ATOM   5235 C CB  . ARG A 1 653 ? 66.493 102.794 17.580  1.00 16.27 ? 653  ARG A CB  1 
ATOM   5236 C CG  . ARG A 1 653 ? 66.752 102.829 16.077  1.00 17.43 ? 653  ARG A CG  1 
ATOM   5237 C CD  . ARG A 1 653 ? 67.324 104.131 15.644  1.00 17.30 ? 653  ARG A CD  1 
ATOM   5238 N NE  . ARG A 1 653 ? 66.340 105.202 15.866  1.00 12.04 ? 653  ARG A NE  1 
ATOM   5239 C CZ  . ARG A 1 653 ? 66.559 106.493 15.639  1.00 16.92 ? 653  ARG A CZ  1 
ATOM   5240 N NH1 . ARG A 1 653 ? 67.754 106.932 15.174  1.00 14.78 ? 653  ARG A NH1 1 
ATOM   5241 N NH2 . ARG A 1 653 ? 65.596 107.362 15.934  1.00 16.88 ? 653  ARG A NH2 1 
ATOM   5242 N N   . PRO A 1 654 ? 66.368 99.433  17.018  1.00 17.04 ? 654  PRO A N   1 
ATOM   5243 C CA  . PRO A 1 654 ? 67.276 98.289  16.826  1.00 15.16 ? 654  PRO A CA  1 
ATOM   5244 C C   . PRO A 1 654 ? 68.686 98.742  16.414  1.00 15.31 ? 654  PRO A C   1 
ATOM   5245 O O   . PRO A 1 654 ? 68.839 99.725  15.717  1.00 15.46 ? 654  PRO A O   1 
ATOM   5246 C CB  . PRO A 1 654 ? 66.605 97.470  15.704  1.00 15.24 ? 654  PRO A CB  1 
ATOM   5247 C CG  . PRO A 1 654 ? 65.133 98.014  15.646  1.00 16.29 ? 654  PRO A CG  1 
ATOM   5248 C CD  . PRO A 1 654 ? 65.254 99.456  16.044  1.00 16.59 ? 654  PRO A CD  1 
ATOM   5249 N N   . LEU A 1 655 ? 69.709 98.022  16.843  1.00 15.20 ? 655  LEU A N   1 
ATOM   5250 C CA  . LEU A 1 655 ? 71.084 98.309  16.369  1.00 15.68 ? 655  LEU A CA  1 
ATOM   5251 C C   . LEU A 1 655 ? 71.154 98.374  14.863  1.00 15.27 ? 655  LEU A C   1 
ATOM   5252 O O   . LEU A 1 655 ? 71.837 99.218  14.312  1.00 14.11 ? 655  LEU A O   1 
ATOM   5253 C CB  . LEU A 1 655 ? 72.081 97.270  16.907  1.00 14.88 ? 655  LEU A CB  1 
ATOM   5254 C CG  . LEU A 1 655 ? 72.668 97.574  18.277  1.00 16.58 ? 655  LEU A CG  1 
ATOM   5255 C CD1 . LEU A 1 655 ? 71.571 97.792  19.332  1.00 13.47 ? 655  LEU A CD1 1 
ATOM   5256 C CD2 . LEU A 1 655 ? 73.725 96.494  18.727  1.00 15.03 ? 655  LEU A CD2 1 
ATOM   5257 N N   . LEU A 1 656 ? 70.386 97.511  14.201  1.00 15.96 ? 656  LEU A N   1 
ATOM   5258 C CA  . LEU A 1 656 ? 70.504 97.346  12.736  1.00 16.16 ? 656  LEU A CA  1 
ATOM   5259 C C   . LEU A 1 656 ? 69.941 98.558  12.006  1.00 16.64 ? 656  LEU A C   1 
ATOM   5260 O O   . LEU A 1 656 ? 70.218 98.723  10.821  1.00 16.46 ? 656  LEU A O   1 
ATOM   5261 C CB  . LEU A 1 656 ? 69.783 96.063  12.246  1.00 16.19 ? 656  LEU A CB  1 
ATOM   5262 C CG  . LEU A 1 656 ? 68.227 96.071  12.275  1.00 17.88 ? 656  LEU A CG  1 
ATOM   5263 C CD1 . LEU A 1 656 ? 67.600 96.281  10.863  1.00 17.87 ? 656  LEU A CD1 1 
ATOM   5264 C CD2 . LEU A 1 656 ? 67.644 94.807  12.915  1.00 16.56 ? 656  LEU A CD2 1 
ATOM   5265 N N   . HIS A 1 657 ? 69.131 99.393  12.684  1.00 16.25 ? 657  HIS A N   1 
ATOM   5266 C CA  . HIS A 1 657 ? 68.665 100.619 12.049  1.00 15.80 ? 657  HIS A CA  1 
ATOM   5267 C C   . HIS A 1 657 ? 69.789 101.648 11.921  1.00 15.92 ? 657  HIS A C   1 
ATOM   5268 O O   . HIS A 1 657 ? 69.756 102.450 10.996  1.00 15.88 ? 657  HIS A O   1 
ATOM   5269 C CB  . HIS A 1 657 ? 67.455 101.228 12.778  1.00 16.27 ? 657  HIS A CB  1 
ATOM   5270 C CG  . HIS A 1 657 ? 66.159 100.533 12.507  1.00 16.81 ? 657  HIS A CG  1 
ATOM   5271 N ND1 . HIS A 1 657 ? 64.948 101.189 12.544  1.00 16.64 ? 657  HIS A ND1 1 
ATOM   5272 C CD2 . HIS A 1 657 ? 65.879 99.248  12.186  1.00 16.48 ? 657  HIS A CD2 1 
ATOM   5273 C CE1 . HIS A 1 657 ? 63.971 100.337 12.278  1.00 16.88 ? 657  HIS A CE1 1 
ATOM   5274 N NE2 . HIS A 1 657 ? 64.508 99.149  12.061  1.00 18.51 ? 657  HIS A NE2 1 
ATOM   5275 N N   . GLU A 1 658 ? 70.807 101.590 12.784  1.00 15.97 ? 658  GLU A N   1 
ATOM   5276 C CA  . GLU A 1 658 ? 71.930 102.539 12.677  1.00 17.22 ? 658  GLU A CA  1 
ATOM   5277 C C   . GLU A 1 658 ? 73.136 101.823 12.066  1.00 18.67 ? 658  GLU A C   1 
ATOM   5278 O O   . GLU A 1 658 ? 74.027 102.462 11.544  1.00 19.31 ? 658  GLU A O   1 
ATOM   5279 C CB  . GLU A 1 658 ? 72.317 103.071 14.049  1.00 16.32 ? 658  GLU A CB  1 
ATOM   5280 C CG  . GLU A 1 658 ? 71.242 104.017 14.683  1.00 18.11 ? 658  GLU A CG  1 
ATOM   5281 C CD  . GLU A 1 658 ? 71.083 105.307 13.877  1.00 21.40 ? 658  GLU A CD  1 
ATOM   5282 O OE1 . GLU A 1 658 ? 72.126 105.955 13.526  1.00 22.21 ? 658  GLU A OE1 1 
ATOM   5283 O OE2 . GLU A 1 658 ? 69.914 105.679 13.603  1.00 22.51 ? 658  GLU A OE2 1 
ATOM   5284 N N   . PHE A 1 659 ? 73.144 100.497 12.156  1.00 18.75 ? 659  PHE A N   1 
ATOM   5285 C CA  . PHE A 1 659 ? 74.327 99.725  11.782  1.00 19.52 ? 659  PHE A CA  1 
ATOM   5286 C C   . PHE A 1 659 ? 74.056 98.635  10.763  1.00 19.60 ? 659  PHE A C   1 
ATOM   5287 O O   . PHE A 1 659 ? 74.676 97.588  10.803  1.00 20.22 ? 659  PHE A O   1 
ATOM   5288 C CB  . PHE A 1 659 ? 75.037 99.206  13.049  1.00 18.79 ? 659  PHE A CB  1 
ATOM   5289 C CG  . PHE A 1 659 ? 75.430 100.305 13.989  1.00 17.56 ? 659  PHE A CG  1 
ATOM   5290 C CD1 . PHE A 1 659 ? 76.477 101.156 13.675  1.00 17.04 ? 659  PHE A CD1 1 
ATOM   5291 C CD2 . PHE A 1 659 ? 74.738 100.519 15.164  1.00 15.77 ? 659  PHE A CD2 1 
ATOM   5292 C CE1 . PHE A 1 659 ? 76.860 102.173 14.538  1.00 13.66 ? 659  PHE A CE1 1 
ATOM   5293 C CE2 . PHE A 1 659 ? 75.131 101.576 16.046  1.00 15.56 ? 659  PHE A CE2 1 
ATOM   5294 C CZ  . PHE A 1 659 ? 76.179 102.395 15.696  1.00 15.63 ? 659  PHE A CZ  1 
ATOM   5295 N N   . TYR A 1 660 ? 73.154 98.934  9.819   1.00 20.57 ? 660  TYR A N   1 
ATOM   5296 C CA  . TYR A 1 660 ? 72.703 97.992  8.797   1.00 20.58 ? 660  TYR A CA  1 
ATOM   5297 C C   . TYR A 1 660 ? 73.810 97.511  7.876   1.00 21.24 ? 660  TYR A C   1 
ATOM   5298 O O   . TYR A 1 660 ? 73.680 96.443  7.296   1.00 21.29 ? 660  TYR A O   1 
ATOM   5299 C CB  . TYR A 1 660 ? 71.526 98.593  7.996   1.00 21.38 ? 660  TYR A CB  1 
ATOM   5300 C CG  . TYR A 1 660 ? 71.773 100.024 7.590   1.00 19.92 ? 660  TYR A CG  1 
ATOM   5301 C CD1 . TYR A 1 660 ? 72.602 100.322 6.518   1.00 20.12 ? 660  TYR A CD1 1 
ATOM   5302 C CD2 . TYR A 1 660 ? 71.230 101.077 8.318   1.00 20.27 ? 660  TYR A CD2 1 
ATOM   5303 C CE1 . TYR A 1 660 ? 72.871 101.638 6.153   1.00 22.07 ? 660  TYR A CE1 1 
ATOM   5304 C CE2 . TYR A 1 660 ? 71.477 102.387 7.970   1.00 21.78 ? 660  TYR A CE2 1 
ATOM   5305 C CZ  . TYR A 1 660 ? 72.286 102.668 6.877   1.00 24.16 ? 660  TYR A CZ  1 
ATOM   5306 O OH  . TYR A 1 660 ? 72.549 103.993 6.537   1.00 25.86 ? 660  TYR A OH  1 
ATOM   5307 N N   . GLU A 1 661 ? 74.902 98.270  7.754   1.00 22.41 ? 661  GLU A N   1 
ATOM   5308 C CA  A GLU A 1 661 ? 76.041 97.864  6.900   0.50 22.88 ? 661  GLU A CA  1 
ATOM   5309 C CA  B GLU A 1 661 ? 76.037 97.862  6.908   0.50 22.53 ? 661  GLU A CA  1 
ATOM   5310 C C   . GLU A 1 661 ? 76.748 96.637  7.505   1.00 22.60 ? 661  GLU A C   1 
ATOM   5311 O O   . GLU A 1 661 ? 77.459 95.912  6.820   1.00 23.08 ? 661  GLU A O   1 
ATOM   5312 C CB  A GLU A 1 661 ? 77.013 99.054  6.611   0.50 22.61 ? 661  GLU A CB  1 
ATOM   5313 C CB  B GLU A 1 661 ? 77.007 99.044  6.615   0.50 22.46 ? 661  GLU A CB  1 
ATOM   5314 C CG  A GLU A 1 661 ? 76.345 100.213 5.787   0.50 22.99 ? 661  GLU A CG  1 
ATOM   5315 C CG  B GLU A 1 661 ? 77.465 99.892  7.813   0.50 23.64 ? 661  GLU A CG  1 
ATOM   5316 C CD  A GLU A 1 661 ? 77.270 101.372 5.381   0.50 24.97 ? 661  GLU A CD  1 
ATOM   5317 C CD  B GLU A 1 661 ? 76.467 100.990 8.287   0.50 23.05 ? 661  GLU A CD  1 
ATOM   5318 O OE1 A GLU A 1 661 ? 78.511 101.233 5.463   0.50 28.76 ? 661  GLU A OE1 1 
ATOM   5319 O OE1 B GLU A 1 661 ? 76.340 102.066 7.660   0.50 22.34 ? 661  GLU A OE1 1 
ATOM   5320 O OE2 A GLU A 1 661 ? 76.752 102.439 4.957   0.50 26.96 ? 661  GLU A OE2 1 
ATOM   5321 O OE2 B GLU A 1 661 ? 75.846 100.795 9.327   0.50 21.24 ? 661  GLU A OE2 1 
ATOM   5322 N N   . ASP A 1 662 ? 76.514 96.391  8.784   1.00 21.97 ? 662  ASP A N   1 
ATOM   5323 C CA  . ASP A 1 662 ? 77.127 95.306  9.515   1.00 21.74 ? 662  ASP A CA  1 
ATOM   5324 C C   . ASP A 1 662 ? 76.138 94.159  9.736   1.00 22.17 ? 662  ASP A C   1 
ATOM   5325 O O   . ASP A 1 662 ? 75.248 94.276  10.589  1.00 21.95 ? 662  ASP A O   1 
ATOM   5326 C CB  . ASP A 1 662 ? 77.521 95.838  10.895  1.00 21.87 ? 662  ASP A CB  1 
ATOM   5327 C CG  . ASP A 1 662 ? 78.440 94.900  11.663  1.00 21.44 ? 662  ASP A CG  1 
ATOM   5328 O OD1 . ASP A 1 662 ? 78.561 93.732  11.289  1.00 18.79 ? 662  ASP A OD1 1 
ATOM   5329 O OD2 . ASP A 1 662 ? 79.044 95.339  12.664  1.00 25.22 ? 662  ASP A OD2 1 
ATOM   5330 N N   . ASN A 1 663 ? 76.304 93.036  9.050   1.00 21.55 ? 663  ASN A N   1 
ATOM   5331 C CA  . ASN A 1 663 ? 75.320 91.981  9.210   1.00 22.53 ? 663  ASN A CA  1 
ATOM   5332 C C   . ASN A 1 663 ? 75.343 91.299  10.580  1.00 21.90 ? 663  ASN A C   1 
ATOM   5333 O O   . ASN A 1 663 ? 74.408 90.572  10.932  1.00 21.56 ? 663  ASN A O   1 
ATOM   5334 C CB  . ASN A 1 663 ? 75.328 90.975  8.033   1.00 23.66 ? 663  ASN A CB  1 
ATOM   5335 C CG  . ASN A 1 663 ? 76.507 90.032  8.058   1.00 27.09 ? 663  ASN A CG  1 
ATOM   5336 O OD1 . ASN A 1 663 ? 77.477 90.217  8.810   1.00 33.50 ? 663  ASN A OD1 1 
ATOM   5337 N ND2 . ASN A 1 663 ? 76.452 89.023  7.197   1.00 31.47 ? 663  ASN A ND2 1 
ATOM   5338 N N   . SER A 1 664 ? 76.362 91.571  11.386  1.00 21.47 ? 664  SER A N   1 
ATOM   5339 C CA  . SER A 1 664 ? 76.317 91.096  12.782  1.00 22.65 ? 664  SER A CA  1 
ATOM   5340 C C   . SER A 1 664 ? 75.213 91.719  13.665  1.00 22.16 ? 664  SER A C   1 
ATOM   5341 O O   . SER A 1 664 ? 74.896 91.167  14.724  1.00 22.29 ? 664  SER A O   1 
ATOM   5342 C CB  . SER A 1 664 ? 77.666 91.247  13.479  1.00 23.32 ? 664  SER A CB  1 
ATOM   5343 O OG  . SER A 1 664 ? 78.618 90.391  12.885  1.00 27.09 ? 664  SER A OG  1 
ATOM   5344 N N   . THR A 1 665 ? 74.629 92.833  13.216  1.00 21.31 ? 665  THR A N   1 
ATOM   5345 C CA  . THR A 1 665 ? 73.574 93.507  13.955  1.00 20.85 ? 665  THR A CA  1 
ATOM   5346 C C   . THR A 1 665 ? 72.185 93.062  13.521  1.00 21.74 ? 665  THR A C   1 
ATOM   5347 O O   . THR A 1 665 ? 71.222 93.450  14.160  1.00 23.25 ? 665  THR A O   1 
ATOM   5348 C CB  . THR A 1 665 ? 73.623 95.020  13.749  1.00 21.17 ? 665  THR A CB  1 
ATOM   5349 O OG1 . THR A 1 665 ? 73.234 95.341  12.408  1.00 19.56 ? 665  THR A OG1 1 
ATOM   5350 C CG2 . THR A 1 665 ? 75.032 95.599  14.061  1.00 16.71 ? 665  THR A CG2 1 
ATOM   5351 N N   . TRP A 1 666 ? 72.077 92.274  12.447  1.00 21.39 ? 666  TRP A N   1 
ATOM   5352 C CA  . TRP A 1 666 ? 70.756 91.995  11.828  1.00 22.24 ? 666  TRP A CA  1 
ATOM   5353 C C   . TRP A 1 666 ? 69.809 91.183  12.712  1.00 22.77 ? 666  TRP A C   1 
ATOM   5354 O O   . TRP A 1 666 ? 68.580 91.282  12.576  1.00 23.63 ? 666  TRP A O   1 
ATOM   5355 C CB  . TRP A 1 666 ? 70.875 91.327  10.446  1.00 21.09 ? 666  TRP A CB  1 
ATOM   5356 C CG  . TRP A 1 666 ? 71.523 92.200  9.361   1.00 21.30 ? 666  TRP A CG  1 
ATOM   5357 C CD1 . TRP A 1 666 ? 71.876 93.517  9.455   1.00 20.57 ? 666  TRP A CD1 1 
ATOM   5358 C CD2 . TRP A 1 666 ? 71.848 91.791  8.025   1.00 20.95 ? 666  TRP A CD2 1 
ATOM   5359 N NE1 . TRP A 1 666 ? 72.394 93.955  8.260   1.00 19.67 ? 666  TRP A NE1 1 
ATOM   5360 C CE2 . TRP A 1 666 ? 72.388 92.909  7.366   1.00 20.93 ? 666  TRP A CE2 1 
ATOM   5361 C CE3 . TRP A 1 666 ? 71.728 90.580  7.321   1.00 21.46 ? 666  TRP A CE3 1 
ATOM   5362 C CZ2 . TRP A 1 666 ? 72.861 92.846  6.036   1.00 20.59 ? 666  TRP A CZ2 1 
ATOM   5363 C CZ3 . TRP A 1 666 ? 72.168 90.525  6.004   1.00 21.76 ? 666  TRP A CZ3 1 
ATOM   5364 C CH2 . TRP A 1 666 ? 72.730 91.659  5.372   1.00 21.04 ? 666  TRP A CH2 1 
ATOM   5365 N N   . ASP A 1 667 ? 70.363 90.367  13.594  1.00 23.61 ? 667  ASP A N   1 
ATOM   5366 C CA  . ASP A 1 667 ? 69.501 89.676  14.545  1.00 25.82 ? 667  ASP A CA  1 
ATOM   5367 C C   . ASP A 1 667 ? 69.752 89.994  16.035  1.00 24.85 ? 667  ASP A C   1 
ATOM   5368 O O   . ASP A 1 667 ? 69.332 89.249  16.901  1.00 25.77 ? 667  ASP A O   1 
ATOM   5369 C CB  . ASP A 1 667 ? 69.493 88.173  14.249  1.00 28.03 ? 667  ASP A CB  1 
ATOM   5370 C CG  . ASP A 1 667 ? 70.852 87.565  14.402  1.00 32.77 ? 667  ASP A CG  1 
ATOM   5371 O OD1 . ASP A 1 667 ? 71.702 88.214  15.066  1.00 37.42 ? 667  ASP A OD1 1 
ATOM   5372 O OD2 . ASP A 1 667 ? 71.070 86.459  13.856  1.00 39.40 ? 667  ASP A OD2 1 
ATOM   5373 N N   . VAL A 1 668 ? 70.379 91.131  16.339  1.00 23.85 ? 668  VAL A N   1 
ATOM   5374 C CA  . VAL A 1 668 ? 70.491 91.574  17.742  1.00 22.42 ? 668  VAL A CA  1 
ATOM   5375 C C   . VAL A 1 668 ? 69.128 92.055  18.301  1.00 23.00 ? 668  VAL A C   1 
ATOM   5376 O O   . VAL A 1 668 ? 68.474 92.955  17.717  1.00 23.21 ? 668  VAL A O   1 
ATOM   5377 C CB  . VAL A 1 668 ? 71.569 92.647  17.915  1.00 22.73 ? 668  VAL A CB  1 
ATOM   5378 C CG1 . VAL A 1 668 ? 71.591 93.161  19.368  1.00 21.62 ? 668  VAL A CG1 1 
ATOM   5379 C CG2 . VAL A 1 668 ? 72.957 92.064  17.516  1.00 20.93 ? 668  VAL A CG2 1 
ATOM   5380 N N   . HIS A 1 669 ? 68.697 91.403  19.386  1.00 21.94 ? 669  HIS A N   1 
ATOM   5381 C CA  . HIS A 1 669 ? 67.473 91.726  20.112  1.00 22.60 ? 669  HIS A CA  1 
ATOM   5382 C C   . HIS A 1 669 ? 67.698 91.793  21.644  1.00 22.07 ? 669  HIS A C   1 
ATOM   5383 O O   . HIS A 1 669 ? 66.769 92.116  22.394  1.00 23.29 ? 669  HIS A O   1 
ATOM   5384 C CB  . HIS A 1 669 ? 66.333 90.734  19.772  1.00 23.15 ? 669  HIS A CB  1 
ATOM   5385 C CG  . HIS A 1 669 ? 66.678 89.302  20.034  1.00 25.27 ? 669  HIS A CG  1 
ATOM   5386 N ND1 . HIS A 1 669 ? 66.419 88.681  21.236  1.00 28.12 ? 669  HIS A ND1 1 
ATOM   5387 C CD2 . HIS A 1 669 ? 67.320 88.384  19.277  1.00 30.59 ? 669  HIS A CD2 1 
ATOM   5388 C CE1 . HIS A 1 669 ? 66.859 87.437  21.200  1.00 28.84 ? 669  HIS A CE1 1 
ATOM   5389 N NE2 . HIS A 1 669 ? 67.419 87.233  20.026  1.00 30.80 ? 669  HIS A NE2 1 
ATOM   5390 N N   A GLN A 1 670 ? 68.903 91.445  22.105  0.50 21.26 ? 670  GLN A N   1 
ATOM   5391 N N   B GLN A 1 670 ? 68.924 91.543  22.073  0.50 20.83 ? 670  GLN A N   1 
ATOM   5392 C CA  A GLN A 1 670 ? 69.267 91.539  23.534  0.50 21.48 ? 670  GLN A CA  1 
ATOM   5393 C CA  B GLN A 1 670 ? 69.273 91.553  23.481  0.50 20.43 ? 670  GLN A CA  1 
ATOM   5394 C C   A GLN A 1 670 ? 69.809 92.935  23.923  0.50 20.48 ? 670  GLN A C   1 
ATOM   5395 C C   B GLN A 1 670 ? 69.928 92.884  23.896  0.50 19.98 ? 670  GLN A C   1 
ATOM   5396 O O   A GLN A 1 670 ? 69.978 93.232  25.113  0.50 20.14 ? 670  GLN A O   1 
ATOM   5397 O O   B GLN A 1 670 ? 70.289 93.085  25.064  0.50 19.60 ? 670  GLN A O   1 
ATOM   5398 C CB  A GLN A 1 670 ? 70.256 90.413  23.974  0.50 21.84 ? 670  GLN A CB  1 
ATOM   5399 C CB  B GLN A 1 670 ? 70.163 90.345  23.800  0.50 20.96 ? 670  GLN A CB  1 
ATOM   5400 C CG  A GLN A 1 670 ? 69.613 89.020  24.272  0.50 21.97 ? 670  GLN A CG  1 
ATOM   5401 C CG  B GLN A 1 670 ? 69.737 89.058  23.085  0.50 19.98 ? 670  GLN A CG  1 
ATOM   5402 C CD  A GLN A 1 670 ? 70.257 88.192  25.445  0.50 23.71 ? 670  GLN A CD  1 
ATOM   5403 C CD  B GLN A 1 670 ? 70.540 88.793  21.807  0.50 21.96 ? 670  GLN A CD  1 
ATOM   5404 O OE1 A GLN A 1 670 ? 69.756 87.105  25.777  0.50 22.56 ? 670  GLN A OE1 1 
ATOM   5405 O OE1 B GLN A 1 670 ? 70.659 89.663  20.911  0.50 18.11 ? 670  GLN A OE1 1 
ATOM   5406 N NE2 A GLN A 1 670 ? 71.342 88.716  26.079  0.50 25.65 ? 670  GLN A NE2 1 
ATOM   5407 N NE2 B GLN A 1 670 ? 71.095 87.575  21.714  0.50 19.71 ? 670  GLN A NE2 1 
ATOM   5408 N N   . GLN A 1 671 ? 70.061 93.787  22.924  1.00 19.92 ? 671  GLN A N   1 
ATOM   5409 C CA  . GLN A 1 671 ? 70.515 95.172  23.149  1.00 19.30 ? 671  GLN A CA  1 
ATOM   5410 C C   . GLN A 1 671 ? 69.617 96.049  22.315  1.00 18.39 ? 671  GLN A C   1 
ATOM   5411 O O   . GLN A 1 671 ? 68.957 95.557  21.372  1.00 19.22 ? 671  GLN A O   1 
ATOM   5412 C CB  . GLN A 1 671 ? 71.962 95.387  22.668  1.00 18.92 ? 671  GLN A CB  1 
ATOM   5413 C CG  . GLN A 1 671 ? 73.023 94.651  23.442  1.00 18.32 ? 671  GLN A CG  1 
ATOM   5414 C CD  . GLN A 1 671 ? 74.328 94.526  22.646  1.00 18.97 ? 671  GLN A CD  1 
ATOM   5415 O OE1 . GLN A 1 671 ? 74.454 93.648  21.818  1.00 18.87 ? 671  GLN A OE1 1 
ATOM   5416 N NE2 . GLN A 1 671 ? 75.279 95.416  22.885  1.00 17.60 ? 671  GLN A NE2 1 
ATOM   5417 N N   . PHE A 1 672 ? 69.545 97.337  22.654  1.00 16.83 ? 672  PHE A N   1 
ATOM   5418 C CA  . PHE A 1 672 ? 68.852 98.313  21.783  1.00 15.64 ? 672  PHE A CA  1 
ATOM   5419 C C   . PHE A 1 672 ? 69.408 99.706  21.967  1.00 15.34 ? 672  PHE A C   1 
ATOM   5420 O O   . PHE A 1 672 ? 70.238 99.930  22.842  1.00 14.53 ? 672  PHE A O   1 
ATOM   5421 C CB  . PHE A 1 672 ? 67.328 98.315  21.988  1.00 15.66 ? 672  PHE A CB  1 
ATOM   5422 C CG  . PHE A 1 672 ? 66.868 98.780  23.356  1.00 16.04 ? 672  PHE A CG  1 
ATOM   5423 C CD1 . PHE A 1 672 ? 66.262 100.030 23.513  1.00 17.00 ? 672  PHE A CD1 1 
ATOM   5424 C CD2 . PHE A 1 672 ? 66.926 97.919  24.449  1.00 16.71 ? 672  PHE A CD2 1 
ATOM   5425 C CE1 . PHE A 1 672 ? 65.790 100.455 24.779  1.00 14.49 ? 672  PHE A CE1 1 
ATOM   5426 C CE2 . PHE A 1 672 ? 66.475 98.318  25.701  1.00 16.76 ? 672  PHE A CE2 1 
ATOM   5427 C CZ  . PHE A 1 672 ? 65.905 99.600  25.877  1.00 14.72 ? 672  PHE A CZ  1 
ATOM   5428 N N   . LEU A 1 673 ? 68.936 100.636 21.155  1.00 15.38 ? 673  LEU A N   1 
ATOM   5429 C CA  . LEU A 1 673 ? 69.361 102.033 21.266  1.00 16.61 ? 673  LEU A CA  1 
ATOM   5430 C C   . LEU A 1 673 ? 68.246 102.955 21.718  1.00 16.42 ? 673  LEU A C   1 
ATOM   5431 O O   . LEU A 1 673 ? 67.064 102.686 21.433  1.00 17.00 ? 673  LEU A O   1 
ATOM   5432 C CB  . LEU A 1 673 ? 69.827 102.512 19.873  1.00 17.16 ? 673  LEU A CB  1 
ATOM   5433 C CG  . LEU A 1 673 ? 70.915 101.681 19.164  1.00 15.98 ? 673  LEU A CG  1 
ATOM   5434 C CD1 . LEU A 1 673 ? 70.940 102.052 17.676  1.00 15.06 ? 673  LEU A CD1 1 
ATOM   5435 C CD2 . LEU A 1 673 ? 72.255 101.938 19.792  1.00 17.58 ? 673  LEU A CD2 1 
ATOM   5436 N N   . TRP A 1 674 ? 68.603 104.063 22.379  1.00 15.92 ? 674  TRP A N   1 
ATOM   5437 C CA  . TRP A 1 674 ? 67.734 105.244 22.392  1.00 15.85 ? 674  TRP A CA  1 
ATOM   5438 C C   . TRP A 1 674 ? 68.197 106.130 21.256  1.00 16.54 ? 674  TRP A C   1 
ATOM   5439 O O   . TRP A 1 674 ? 69.322 106.708 21.320  1.00 16.77 ? 674  TRP A O   1 
ATOM   5440 C CB  . TRP A 1 674 ? 67.870 106.051 23.675  1.00 16.41 ? 674  TRP A CB  1 
ATOM   5441 C CG  . TRP A 1 674 ? 67.037 105.635 24.827  1.00 17.90 ? 674  TRP A CG  1 
ATOM   5442 C CD1 . TRP A 1 674 ? 66.352 104.462 24.983  1.00 19.43 ? 674  TRP A CD1 1 
ATOM   5443 C CD2 . TRP A 1 674 ? 66.829 106.385 26.030  1.00 18.71 ? 674  TRP A CD2 1 
ATOM   5444 N NE1 . TRP A 1 674 ? 65.720 104.441 26.204  1.00 19.66 ? 674  TRP A NE1 1 
ATOM   5445 C CE2 . TRP A 1 674 ? 65.977 105.616 26.861  1.00 18.95 ? 674  TRP A CE2 1 
ATOM   5446 C CE3 . TRP A 1 674 ? 67.270 107.638 26.479  1.00 17.40 ? 674  TRP A CE3 1 
ATOM   5447 C CZ2 . TRP A 1 674 ? 65.563 106.052 28.131  1.00 19.79 ? 674  TRP A CZ2 1 
ATOM   5448 C CZ3 . TRP A 1 674 ? 66.860 108.079 27.735  1.00 18.60 ? 674  TRP A CZ3 1 
ATOM   5449 C CH2 . TRP A 1 674 ? 66.003 107.282 28.550  1.00 18.97 ? 674  TRP A CH2 1 
ATOM   5450 N N   . GLY A 1 675 ? 67.368 106.255 20.226  1.00 15.20 ? 675  GLY A N   1 
ATOM   5451 C CA  . GLY A 1 675 ? 67.719 107.032 19.058  1.00 15.52 ? 675  GLY A CA  1 
ATOM   5452 C C   . GLY A 1 675 ? 69.029 106.539 18.436  1.00 17.45 ? 675  GLY A C   1 
ATOM   5453 O O   . GLY A 1 675 ? 69.305 105.331 18.407  1.00 14.83 ? 675  GLY A O   1 
ATOM   5454 N N   . PRO A 1 676 ? 69.828 107.482 17.885  1.00 18.34 ? 676  PRO A N   1 
ATOM   5455 C CA  . PRO A 1 676 ? 71.088 107.081 17.239  1.00 19.06 ? 676  PRO A CA  1 
ATOM   5456 C C   . PRO A 1 676 ? 72.262 106.825 18.193  1.00 19.66 ? 676  PRO A C   1 
ATOM   5457 O O   . PRO A 1 676 ? 73.213 106.140 17.809  1.00 20.04 ? 676  PRO A O   1 
ATOM   5458 C CB  . PRO A 1 676 ? 71.370 108.262 16.322  1.00 19.60 ? 676  PRO A CB  1 
ATOM   5459 C CG  . PRO A 1 676 ? 70.867 109.459 17.186  1.00 19.36 ? 676  PRO A CG  1 
ATOM   5460 C CD  . PRO A 1 676 ? 69.560 108.925 17.741  1.00 18.54 ? 676  PRO A CD  1 
ATOM   5461 N N   . GLY A 1 677 ? 72.188 107.303 19.434  1.00 19.54 ? 677  GLY A N   1 
ATOM   5462 C CA  . GLY A 1 677 ? 73.413 107.536 20.185  1.00 19.86 ? 677  GLY A CA  1 
ATOM   5463 C C   . GLY A 1 677 ? 73.665 106.796 21.481  1.00 19.79 ? 677  GLY A C   1 
ATOM   5464 O O   . GLY A 1 677 ? 74.802 106.752 21.919  1.00 19.27 ? 677  GLY A O   1 
ATOM   5465 N N   . LEU A 1 678 ? 72.618 106.261 22.117  1.00 18.03 ? 678  LEU A N   1 
ATOM   5466 C CA  . LEU A 1 678 ? 72.758 105.553 23.381  1.00 18.53 ? 678  LEU A CA  1 
ATOM   5467 C C   . LEU A 1 678 ? 72.477 104.049 23.247  1.00 18.95 ? 678  LEU A C   1 
ATOM   5468 O O   . LEU A 1 678 ? 71.339 103.633 22.905  1.00 19.82 ? 678  LEU A O   1 
ATOM   5469 C CB  . LEU A 1 678 ? 71.828 106.154 24.476  1.00 18.64 ? 678  LEU A CB  1 
ATOM   5470 C CG  . LEU A 1 678 ? 71.677 105.389 25.800  1.00 18.04 ? 678  LEU A CG  1 
ATOM   5471 C CD1 . LEU A 1 678 ? 72.976 105.434 26.600  1.00 20.21 ? 678  LEU A CD1 1 
ATOM   5472 C CD2 . LEU A 1 678 ? 70.540 105.999 26.656  1.00 18.05 ? 678  LEU A CD2 1 
ATOM   5473 N N   . LEU A 1 679 ? 73.495 103.256 23.591  1.00 18.44 ? 679  LEU A N   1 
ATOM   5474 C CA  . LEU A 1 679 ? 73.475 101.817 23.515  1.00 18.26 ? 679  LEU A CA  1 
ATOM   5475 C C   . LEU A 1 679 ? 73.217 101.203 24.881  1.00 18.55 ? 679  LEU A C   1 
ATOM   5476 O O   . LEU A 1 679 ? 74.001 101.385 25.820  1.00 17.67 ? 679  LEU A O   1 
ATOM   5477 C CB  . LEU A 1 679 ? 74.817 101.318 22.941  1.00 19.02 ? 679  LEU A CB  1 
ATOM   5478 C CG  . LEU A 1 679 ? 75.050 99.794  22.895  1.00 18.99 ? 679  LEU A CG  1 
ATOM   5479 C CD1 . LEU A 1 679 ? 74.022 99.094  22.006  1.00 17.99 ? 679  LEU A CD1 1 
ATOM   5480 C CD2 . LEU A 1 679 ? 76.474 99.457  22.454  1.00 18.76 ? 679  LEU A CD2 1 
ATOM   5481 N N   . ILE A 1 680 ? 72.131 100.432 24.982  1.00 17.86 ? 680  ILE A N   1 
ATOM   5482 C CA  . ILE A 1 680 ? 71.749 99.810  26.238  1.00 17.17 ? 680  ILE A CA  1 
ATOM   5483 C C   . ILE A 1 680 ? 72.003 98.308  26.201  1.00 18.30 ? 680  ILE A C   1 
ATOM   5484 O O   . ILE A 1 680 ? 71.484 97.619  25.322  1.00 18.07 ? 680  ILE A O   1 
ATOM   5485 C CB  . ILE A 1 680 ? 70.272 100.118 26.553  1.00 16.01 ? 680  ILE A CB  1 
ATOM   5486 C CG1 . ILE A 1 680 ? 70.116 101.632 26.698  1.00 17.77 ? 680  ILE A CG1 1 
ATOM   5487 C CG2 . ILE A 1 680 ? 69.842 99.445  27.859  1.00 16.47 ? 680  ILE A CG2 1 
ATOM   5488 C CD1 . ILE A 1 680 ? 68.964 102.195 26.028  1.00 19.55 ? 680  ILE A CD1 1 
ATOM   5489 N N   . THR A 1 681 ? 72.791 97.802  27.161  1.00 18.73 ? 681  THR A N   1 
ATOM   5490 C CA  . THR A 1 681 ? 73.185 96.395  27.187  1.00 18.57 ? 681  THR A CA  1 
ATOM   5491 C C   . THR A 1 681 ? 72.875 95.813  28.563  1.00 19.02 ? 681  THR A C   1 
ATOM   5492 O O   . THR A 1 681 ? 73.671 95.946  29.500  1.00 19.30 ? 681  THR A O   1 
ATOM   5493 C CB  . THR A 1 681 ? 74.702 96.206  26.905  1.00 19.80 ? 681  THR A CB  1 
ATOM   5494 O OG1 . THR A 1 681 ? 75.080 96.960  25.739  1.00 21.28 ? 681  THR A OG1 1 
ATOM   5495 C CG2 . THR A 1 681 ? 75.025 94.739  26.696  1.00 17.57 ? 681  THR A CG2 1 
ATOM   5496 N N   . PRO A 1 682 ? 71.687 95.201  28.707  1.00 18.63 ? 682  PRO A N   1 
ATOM   5497 C CA  . PRO A 1 682 ? 71.305 94.575  29.960  1.00 18.08 ? 682  PRO A CA  1 
ATOM   5498 C C   . PRO A 1 682 ? 71.843 93.165  30.142  1.00 18.59 ? 682  PRO A C   1 
ATOM   5499 O O   . PRO A 1 682 ? 72.059 92.430  29.156  1.00 18.29 ? 682  PRO A O   1 
ATOM   5500 C CB  . PRO A 1 682 ? 69.780 94.517  29.852  1.00 17.68 ? 682  PRO A CB  1 
ATOM   5501 C CG  . PRO A 1 682 ? 69.554 94.266  28.388  1.00 17.25 ? 682  PRO A CG  1 
ATOM   5502 C CD  . PRO A 1 682 ? 70.586 95.177  27.721  1.00 17.91 ? 682  PRO A CD  1 
ATOM   5503 N N   . VAL A 1 683 ? 72.042 92.792  31.410  1.00 19.23 ? 683  VAL A N   1 
ATOM   5504 C CA  . VAL A 1 683 ? 72.249 91.401  31.780  1.00 20.43 ? 683  VAL A CA  1 
ATOM   5505 C C   . VAL A 1 683 ? 70.845 90.783  31.810  1.00 21.43 ? 683  VAL A C   1 
ATOM   5506 O O   . VAL A 1 683 ? 69.965 91.317  32.461  1.00 21.72 ? 683  VAL A O   1 
ATOM   5507 C CB  . VAL A 1 683 ? 72.958 91.283  33.160  1.00 19.62 ? 683  VAL A CB  1 
ATOM   5508 C CG1 . VAL A 1 683 ? 72.899 89.858  33.687  1.00 19.74 ? 683  VAL A CG1 1 
ATOM   5509 C CG2 . VAL A 1 683 ? 74.425 91.797  33.046  1.00 19.89 ? 683  VAL A CG2 1 
ATOM   5510 N N   . LEU A 1 684 ? 70.643 89.696  31.076  1.00 22.47 ? 684  LEU A N   1 
ATOM   5511 C CA  . LEU A 1 684 ? 69.322 89.114  30.934  1.00 23.90 ? 684  LEU A CA  1 
ATOM   5512 C C   . LEU A 1 684 ? 69.292 87.644  31.362  1.00 25.11 ? 684  LEU A C   1 
ATOM   5513 O O   . LEU A 1 684 ? 68.299 86.968  31.127  1.00 25.09 ? 684  LEU A O   1 
ATOM   5514 C CB  . LEU A 1 684 ? 68.808 89.257  29.478  1.00 23.14 ? 684  LEU A CB  1 
ATOM   5515 C CG  . LEU A 1 684 ? 68.620 90.657  28.882  1.00 21.67 ? 684  LEU A CG  1 
ATOM   5516 C CD1 . LEU A 1 684 ? 68.503 90.611  27.349  1.00 18.78 ? 684  LEU A CD1 1 
ATOM   5517 C CD2 . LEU A 1 684 ? 67.442 91.447  29.521  1.00 18.23 ? 684  LEU A CD2 1 
ATOM   5518 N N   . ASP A 1 685 ? 70.370 87.154  31.972  1.00 27.05 ? 685  ASP A N   1 
ATOM   5519 C CA  . ASP A 1 685 ? 70.432 85.740  32.401  1.00 29.65 ? 685  ASP A CA  1 
ATOM   5520 C C   . ASP A 1 685 ? 70.636 85.617  33.895  1.00 29.33 ? 685  ASP A C   1 
ATOM   5521 O O   . ASP A 1 685 ? 71.446 86.326  34.466  1.00 29.57 ? 685  ASP A O   1 
ATOM   5522 C CB  . ASP A 1 685 ? 71.557 84.957  31.709  1.00 30.08 ? 685  ASP A CB  1 
ATOM   5523 C CG  . ASP A 1 685 ? 71.524 85.068  30.203  1.00 35.45 ? 685  ASP A CG  1 
ATOM   5524 O OD1 . ASP A 1 685 ? 70.617 84.499  29.541  1.00 37.53 ? 685  ASP A OD1 1 
ATOM   5525 O OD2 . ASP A 1 685 ? 72.455 85.724  29.675  1.00 42.31 ? 685  ASP A OD2 1 
ATOM   5526 N N   . GLU A 1 686 ? 69.898 84.707  34.515  1.00 29.71 ? 686  GLU A N   1 
ATOM   5527 C CA  . GLU A 1 686 ? 70.019 84.456  35.945  1.00 30.70 ? 686  GLU A CA  1 
ATOM   5528 C C   . GLU A 1 686 ? 71.465 84.103  36.368  1.00 30.97 ? 686  GLU A C   1 
ATOM   5529 O O   . GLU A 1 686 ? 72.172 83.343  35.687  1.00 30.22 ? 686  GLU A O   1 
ATOM   5530 C CB  . GLU A 1 686 ? 69.064 83.328  36.309  1.00 31.54 ? 686  GLU A CB  1 
ATOM   5531 C CG  . GLU A 1 686 ? 68.882 83.062  37.784  1.00 32.78 ? 686  GLU A CG  1 
ATOM   5532 C CD  . GLU A 1 686 ? 67.802 82.028  38.030  1.00 35.08 ? 686  GLU A CD  1 
ATOM   5533 O OE1 . GLU A 1 686 ? 67.265 81.454  37.065  1.00 37.49 ? 686  GLU A OE1 1 
ATOM   5534 O OE2 . GLU A 1 686 ? 67.483 81.779  39.194  1.00 39.69 ? 686  GLU A OE2 1 
ATOM   5535 N N   . GLY A 1 687 ? 71.919 84.726  37.448  1.00 31.06 ? 687  GLY A N   1 
ATOM   5536 C CA  . GLY A 1 687 ? 73.233 84.435  37.992  1.00 32.22 ? 687  GLY A CA  1 
ATOM   5537 C C   . GLY A 1 687 ? 74.387 85.055  37.236  1.00 32.77 ? 687  GLY A C   1 
ATOM   5538 O O   . GLY A 1 687 ? 75.545 84.924  37.668  1.00 33.67 ? 687  GLY A O   1 
ATOM   5539 N N   . ALA A 1 688 ? 74.105 85.727  36.120  1.00 32.67 ? 688  ALA A N   1 
ATOM   5540 C CA  . ALA A 1 688 ? 75.187 86.343  35.324  1.00 33.21 ? 688  ALA A CA  1 
ATOM   5541 C C   . ALA A 1 688 ? 75.659 87.711  35.856  1.00 33.38 ? 688  ALA A C   1 
ATOM   5542 O O   . ALA A 1 688 ? 74.866 88.509  36.381  1.00 32.14 ? 688  ALA A O   1 
ATOM   5543 C CB  . ALA A 1 688 ? 74.802 86.423  33.826  1.00 33.33 ? 688  ALA A CB  1 
ATOM   5544 N N   . GLU A 1 689 ? 76.957 87.955  35.717  1.00 34.21 ? 689  GLU A N   1 
ATOM   5545 C CA  . GLU A 1 689 ? 77.584 89.247  36.031  1.00 36.65 ? 689  GLU A CA  1 
ATOM   5546 C C   . GLU A 1 689 ? 78.359 89.738  34.795  1.00 35.69 ? 689  GLU A C   1 
ATOM   5547 O O   . GLU A 1 689 ? 79.270 90.562  34.873  1.00 34.79 ? 689  GLU A O   1 
ATOM   5548 C CB  . GLU A 1 689 ? 78.491 89.124  37.269  1.00 36.49 ? 689  GLU A CB  1 
ATOM   5549 C CG  . GLU A 1 689 ? 77.719 88.803  38.565  1.00 39.50 ? 689  GLU A CG  1 
ATOM   5550 C CD  . GLU A 1 689 ? 78.624 88.708  39.781  1.00 41.63 ? 689  GLU A CD  1 
ATOM   5551 O OE1 . GLU A 1 689 ? 78.959 87.561  40.202  1.00 48.89 ? 689  GLU A OE1 1 
ATOM   5552 O OE2 . GLU A 1 689 ? 79.027 89.782  40.305  1.00 48.75 ? 689  GLU A OE2 1 
ATOM   5553 N N   . LYS A 1 690 ? 77.965 89.194  33.651  1.00 36.06 ? 690  LYS A N   1 
ATOM   5554 C CA  . LYS A 1 690 ? 78.574 89.479  32.360  1.00 37.01 ? 690  LYS A CA  1 
ATOM   5555 C C   . LYS A 1 690 ? 77.484 89.304  31.335  1.00 36.34 ? 690  LYS A C   1 
ATOM   5556 O O   . LYS A 1 690 ? 76.544 88.537  31.523  1.00 36.10 ? 690  LYS A O   1 
ATOM   5557 C CB  . LYS A 1 690 ? 79.632 88.431  31.967  1.00 37.31 ? 690  LYS A CB  1 
ATOM   5558 C CG  . LYS A 1 690 ? 80.768 88.180  32.907  1.00 41.90 ? 690  LYS A CG  1 
ATOM   5559 C CD  . LYS A 1 690 ? 81.493 86.915  32.450  1.00 46.92 ? 690  LYS A CD  1 
ATOM   5560 C CE  . LYS A 1 690 ? 82.575 86.487  33.449  1.00 49.81 ? 690  LYS A CE  1 
ATOM   5561 N NZ  . LYS A 1 690 ? 83.439 85.393  32.850  1.00 51.02 ? 690  LYS A NZ  1 
ATOM   5562 N N   . VAL A 1 691 ? 77.656 89.979  30.212  1.00 36.12 ? 691  VAL A N   1 
ATOM   5563 C CA  . VAL A 1 691 ? 76.808 89.734  29.072  1.00 35.76 ? 691  VAL A CA  1 
ATOM   5564 C C   . VAL A 1 691 ? 77.653 89.695  27.782  1.00 35.05 ? 691  VAL A C   1 
ATOM   5565 O O   . VAL A 1 691 ? 78.505 90.583  27.556  1.00 35.00 ? 691  VAL A O   1 
ATOM   5566 C CB  . VAL A 1 691 ? 75.699 90.795  29.027  1.00 35.36 ? 691  VAL A CB  1 
ATOM   5567 C CG1 . VAL A 1 691 ? 76.218 92.121  28.512  1.00 36.28 ? 691  VAL A CG1 1 
ATOM   5568 C CG2 . VAL A 1 691 ? 74.536 90.318  28.191  1.00 38.40 ? 691  VAL A CG2 1 
ATOM   5569 N N   . MET A 1 692 ? 77.454 88.647  26.976  1.00 34.87 ? 692  MET A N   1 
ATOM   5570 C CA  . MET A 1 692 ? 77.969 88.611  25.595  1.00 34.44 ? 692  MET A CA  1 
ATOM   5571 C C   . MET A 1 692 ? 77.131 89.639  24.848  1.00 32.77 ? 692  MET A C   1 
ATOM   5572 O O   . MET A 1 692 ? 75.886 89.580  24.883  1.00 32.18 ? 692  MET A O   1 
ATOM   5573 C CB  . MET A 1 692 ? 77.827 87.215  24.951  1.00 36.59 ? 692  MET A CB  1 
ATOM   5574 C CG  . MET A 1 692 ? 78.794 86.134  25.505  1.00 40.15 ? 692  MET A CG  1 
ATOM   5575 S SD  . MET A 1 692 ? 80.534 86.516  25.146  1.00 51.75 ? 692  MET A SD  1 
ATOM   5576 C CE  . MET A 1 692 ? 81.412 85.192  26.013  1.00 47.01 ? 692  MET A CE  1 
ATOM   5577 N N   . ALA A 1 693 ? 77.804 90.608  24.240  1.00 29.78 ? 693  ALA A N   1 
ATOM   5578 C CA  . ALA A 1 693 ? 77.139 91.772  23.661  1.00 28.20 ? 693  ALA A CA  1 
ATOM   5579 C C   . ALA A 1 693 ? 77.831 92.178  22.364  1.00 27.16 ? 693  ALA A C   1 
ATOM   5580 O O   . ALA A 1 693 ? 79.025 91.968  22.217  1.00 26.22 ? 693  ALA A O   1 
ATOM   5581 C CB  . ALA A 1 693 ? 77.197 92.931  24.642  1.00 28.11 ? 693  ALA A CB  1 
ATOM   5582 N N   . TYR A 1 694 ? 77.092 92.798  21.444  1.00 25.94 ? 694  TYR A N   1 
ATOM   5583 C CA  . TYR A 1 694 ? 77.711 93.340  20.233  1.00 24.09 ? 694  TYR A CA  1 
ATOM   5584 C C   . TYR A 1 694 ? 78.080 94.821  20.383  1.00 23.58 ? 694  TYR A C   1 
ATOM   5585 O O   . TYR A 1 694 ? 77.310 95.636  20.912  1.00 24.13 ? 694  TYR A O   1 
ATOM   5586 C CB  . TYR A 1 694 ? 76.897 93.022  18.958  1.00 24.40 ? 694  TYR A CB  1 
ATOM   5587 C CG  . TYR A 1 694 ? 77.703 93.229  17.697  1.00 24.03 ? 694  TYR A CG  1 
ATOM   5588 C CD1 . TYR A 1 694 ? 78.736 92.347  17.364  1.00 25.42 ? 694  TYR A CD1 1 
ATOM   5589 C CD2 . TYR A 1 694 ? 77.477 94.322  16.865  1.00 20.99 ? 694  TYR A CD2 1 
ATOM   5590 C CE1 . TYR A 1 694 ? 79.520 92.548  16.233  1.00 25.53 ? 694  TYR A CE1 1 
ATOM   5591 C CE2 . TYR A 1 694 ? 78.268 94.529  15.718  1.00 23.17 ? 694  TYR A CE2 1 
ATOM   5592 C CZ  . TYR A 1 694 ? 79.278 93.620  15.416  1.00 23.75 ? 694  TYR A CZ  1 
ATOM   5593 O OH  . TYR A 1 694 ? 80.077 93.797  14.315  1.00 25.46 ? 694  TYR A OH  1 
ATOM   5594 N N   . VAL A 1 695 ? 79.295 95.158  19.986  1.00 21.63 ? 695  VAL A N   1 
ATOM   5595 C CA  . VAL A 1 695 ? 79.729 96.540  19.942  1.00 20.67 ? 695  VAL A CA  1 
ATOM   5596 C C   . VAL A 1 695 ? 79.799 96.918  18.465  1.00 21.23 ? 695  VAL A C   1 
ATOM   5597 O O   . VAL A 1 695 ? 80.685 96.434  17.744  1.00 20.84 ? 695  VAL A O   1 
ATOM   5598 C CB  . VAL A 1 695 ? 81.102 96.702  20.608  1.00 21.27 ? 695  VAL A CB  1 
ATOM   5599 C CG1 . VAL A 1 695 ? 81.614 98.137  20.516  1.00 19.11 ? 695  VAL A CG1 1 
ATOM   5600 C CG2 . VAL A 1 695 ? 81.013 96.242  22.050  1.00 18.83 ? 695  VAL A CG2 1 
ATOM   5601 N N   . PRO A 1 696 ? 78.819 97.716  17.986  1.00 20.56 ? 696  PRO A N   1 
ATOM   5602 C CA  . PRO A 1 696 ? 78.816 98.143  16.593  1.00 20.76 ? 696  PRO A CA  1 
ATOM   5603 C C   . PRO A 1 696 ? 80.045 98.968  16.173  1.00 21.54 ? 696  PRO A C   1 
ATOM   5604 O O   . PRO A 1 696 ? 80.884 99.378  17.011  1.00 21.30 ? 696  PRO A O   1 
ATOM   5605 C CB  . PRO A 1 696 ? 77.550 98.989  16.488  1.00 20.79 ? 696  PRO A CB  1 
ATOM   5606 C CG  . PRO A 1 696 ? 76.680 98.517  17.569  1.00 21.46 ? 696  PRO A CG  1 
ATOM   5607 C CD  . PRO A 1 696 ? 77.645 98.223  18.706  1.00 20.82 ? 696  PRO A CD  1 
ATOM   5608 N N   . ASP A 1 697 ? 80.133 99.178  14.873  1.00 21.25 ? 697  ASP A N   1 
ATOM   5609 C CA  . ASP A 1 697 ? 81.258 99.841  14.224  1.00 22.30 ? 697  ASP A CA  1 
ATOM   5610 C C   . ASP A 1 697 ? 81.203 101.360 14.408  1.00 21.79 ? 697  ASP A C   1 
ATOM   5611 O O   . ASP A 1 697 ? 80.782 102.103 13.528  1.00 22.37 ? 697  ASP A O   1 
ATOM   5612 C CB  . ASP A 1 697 ? 81.287 99.463  12.727  1.00 22.28 ? 697  ASP A CB  1 
ATOM   5613 C CG  . ASP A 1 697 ? 82.573 99.903  12.034  1.00 24.85 ? 697  ASP A CG  1 
ATOM   5614 O OD1 . ASP A 1 697 ? 83.522 100.296 12.729  1.00 26.00 ? 697  ASP A OD1 1 
ATOM   5615 O OD2 . ASP A 1 697 ? 82.618 99.848  10.787  1.00 25.44 ? 697  ASP A OD2 1 
ATOM   5616 N N   . ALA A 1 698 ? 81.636 101.807 15.578  1.00 21.52 ? 698  ALA A N   1 
ATOM   5617 C CA  . ALA A 1 698 ? 81.608 103.229 15.933  1.00 21.04 ? 698  ALA A CA  1 
ATOM   5618 C C   . ALA A 1 698 ? 82.518 103.417 17.120  1.00 20.35 ? 698  ALA A C   1 
ATOM   5619 O O   . ALA A 1 698 ? 82.924 102.442 17.754  1.00 21.08 ? 698  ALA A O   1 
ATOM   5620 C CB  . ALA A 1 698 ? 80.177 103.662 16.301  1.00 20.35 ? 698  ALA A CB  1 
ATOM   5621 N N   . VAL A 1 699 ? 82.836 104.667 17.428  1.00 21.15 ? 699  VAL A N   1 
ATOM   5622 C CA  . VAL A 1 699 ? 83.453 105.012 18.713  1.00 21.22 ? 699  VAL A CA  1 
ATOM   5623 C C   . VAL A 1 699 ? 82.385 104.929 19.825  1.00 21.39 ? 699  VAL A C   1 
ATOM   5624 O O   . VAL A 1 699 ? 81.268 105.449 19.651  1.00 22.12 ? 699  VAL A O   1 
ATOM   5625 C CB  . VAL A 1 699 ? 84.114 106.427 18.667  1.00 21.54 ? 699  VAL A CB  1 
ATOM   5626 C CG1 . VAL A 1 699 ? 84.674 106.796 20.043  1.00 19.68 ? 699  VAL A CG1 1 
ATOM   5627 C CG2 . VAL A 1 699 ? 85.227 106.468 17.602  1.00 21.67 ? 699  VAL A CG2 1 
ATOM   5628 N N   . TRP A 1 700 ? 82.713 104.266 20.936  1.00 20.59 ? 700  TRP A N   1 
ATOM   5629 C CA  . TRP A 1 700 ? 81.805 104.147 22.079  1.00 20.67 ? 700  TRP A CA  1 
ATOM   5630 C C   . TRP A 1 700 ? 82.514 104.594 23.364  1.00 21.56 ? 700  TRP A C   1 
ATOM   5631 O O   . TRP A 1 700 ? 83.723 104.349 23.520  1.00 21.11 ? 700  TRP A O   1 
ATOM   5632 C CB  . TRP A 1 700 ? 81.298 102.711 22.238  1.00 20.17 ? 700  TRP A CB  1 
ATOM   5633 C CG  . TRP A 1 700 ? 80.416 102.242 21.055  1.00 20.32 ? 700  TRP A CG  1 
ATOM   5634 C CD1 . TRP A 1 700 ? 80.793 101.407 20.027  1.00 19.89 ? 700  TRP A CD1 1 
ATOM   5635 C CD2 . TRP A 1 700 ? 79.044 102.604 20.788  1.00 19.58 ? 700  TRP A CD2 1 
ATOM   5636 N NE1 . TRP A 1 700 ? 79.751 101.219 19.154  1.00 19.60 ? 700  TRP A NE1 1 
ATOM   5637 C CE2 . TRP A 1 700 ? 78.661 101.932 19.598  1.00 20.20 ? 700  TRP A CE2 1 
ATOM   5638 C CE3 . TRP A 1 700 ? 78.093 103.400 21.455  1.00 18.21 ? 700  TRP A CE3 1 
ATOM   5639 C CZ2 . TRP A 1 700 ? 77.373 102.059 19.044  1.00 22.24 ? 700  TRP A CZ2 1 
ATOM   5640 C CZ3 . TRP A 1 700 ? 76.817 103.520 20.914  1.00 18.82 ? 700  TRP A CZ3 1 
ATOM   5641 C CH2 . TRP A 1 700 ? 76.465 102.857 19.713  1.00 19.66 ? 700  TRP A CH2 1 
ATOM   5642 N N   . TYR A 1 701 ? 81.767 105.294 24.236  1.00 20.76 ? 701  TYR A N   1 
ATOM   5643 C CA  . TYR A 1 701 ? 82.250 105.758 25.543  1.00 20.80 ? 701  TYR A CA  1 
ATOM   5644 C C   . TYR A 1 701 ? 81.356 105.209 26.624  1.00 21.14 ? 701  TYR A C   1 
ATOM   5645 O O   . TYR A 1 701 ? 80.130 105.250 26.516  1.00 21.34 ? 701  TYR A O   1 
ATOM   5646 C CB  . TYR A 1 701 ? 82.257 107.280 25.612  1.00 20.04 ? 701  TYR A CB  1 
ATOM   5647 C CG  . TYR A 1 701 ? 83.116 107.963 24.546  1.00 21.27 ? 701  TYR A CG  1 
ATOM   5648 C CD1 . TYR A 1 701 ? 84.485 108.188 24.749  1.00 21.24 ? 701  TYR A CD1 1 
ATOM   5649 C CD2 . TYR A 1 701 ? 82.555 108.397 23.349  1.00 23.73 ? 701  TYR A CD2 1 
ATOM   5650 C CE1 . TYR A 1 701 ? 85.271 108.819 23.776  1.00 20.39 ? 701  TYR A CE1 1 
ATOM   5651 C CE2 . TYR A 1 701 ? 83.323 109.022 22.386  1.00 22.35 ? 701  TYR A CE2 1 
ATOM   5652 C CZ  . TYR A 1 701 ? 84.684 109.238 22.614  1.00 21.12 ? 701  TYR A CZ  1 
ATOM   5653 O OH  . TYR A 1 701 ? 85.438 109.860 21.644  1.00 20.21 ? 701  TYR A OH  1 
ATOM   5654 N N   . ASP A 1 702 ? 81.950 104.676 27.668  1.00 21.22 ? 702  ASP A N   1 
ATOM   5655 C CA  . ASP A 1 702 ? 81.182 104.306 28.839  1.00 22.68 ? 702  ASP A CA  1 
ATOM   5656 C C   . ASP A 1 702 ? 80.458 105.532 29.448  1.00 23.06 ? 702  ASP A C   1 
ATOM   5657 O O   . ASP A 1 702 ? 81.079 106.554 29.754  1.00 22.06 ? 702  ASP A O   1 
ATOM   5658 C CB  . ASP A 1 702 ? 82.108 103.691 29.858  1.00 22.20 ? 702  ASP A CB  1 
ATOM   5659 C CG  . ASP A 1 702 ? 81.372 103.127 31.006  1.00 27.25 ? 702  ASP A CG  1 
ATOM   5660 O OD1 . ASP A 1 702 ? 80.746 102.059 30.830  1.00 31.57 ? 702  ASP A OD1 1 
ATOM   5661 O OD2 . ASP A 1 702 ? 81.391 103.763 32.079  1.00 30.81 ? 702  ASP A OD2 1 
ATOM   5662 N N   . TYR A 1 703 ? 79.143 105.432 29.624  1.00 24.01 ? 703  TYR A N   1 
ATOM   5663 C CA  . TYR A 1 703 ? 78.358 106.565 30.147  1.00 24.07 ? 703  TYR A CA  1 
ATOM   5664 C C   . TYR A 1 703 ? 78.855 107.000 31.496  1.00 25.04 ? 703  TYR A C   1 
ATOM   5665 O O   . TYR A 1 703 ? 78.976 108.181 31.745  1.00 25.53 ? 703  TYR A O   1 
ATOM   5666 C CB  . TYR A 1 703 ? 76.850 106.252 30.264  1.00 23.83 ? 703  TYR A CB  1 
ATOM   5667 C CG  . TYR A 1 703 ? 76.058 107.388 30.868  1.00 23.02 ? 703  TYR A CG  1 
ATOM   5668 C CD1 . TYR A 1 703 ? 75.552 108.409 30.073  1.00 24.75 ? 703  TYR A CD1 1 
ATOM   5669 C CD2 . TYR A 1 703 ? 75.859 107.470 32.247  1.00 24.96 ? 703  TYR A CD2 1 
ATOM   5670 C CE1 . TYR A 1 703 ? 74.830 109.496 30.636  1.00 24.52 ? 703  TYR A CE1 1 
ATOM   5671 C CE2 . TYR A 1 703 ? 75.144 108.551 32.825  1.00 25.46 ? 703  TYR A CE2 1 
ATOM   5672 C CZ  . TYR A 1 703 ? 74.643 109.556 32.005  1.00 26.36 ? 703  TYR A CZ  1 
ATOM   5673 O OH  . TYR A 1 703 ? 73.930 110.602 32.559  1.00 26.62 ? 703  TYR A OH  1 
ATOM   5674 N N   . GLU A 1 704 ? 79.092 106.045 32.382  1.00 26.40 ? 704  GLU A N   1 
ATOM   5675 C CA  . GLU A 1 704 ? 79.386 106.353 33.776  1.00 28.70 ? 704  GLU A CA  1 
ATOM   5676 C C   . GLU A 1 704 ? 80.802 106.916 33.983  1.00 28.27 ? 704  GLU A C   1 
ATOM   5677 O O   . GLU A 1 704 ? 80.957 107.932 34.638  1.00 28.02 ? 704  GLU A O   1 
ATOM   5678 C CB  . GLU A 1 704 ? 79.018 105.150 34.676  1.00 28.35 ? 704  GLU A CB  1 
ATOM   5679 C CG  . GLU A 1 704 ? 77.489 104.778 34.450  1.00 31.60 ? 704  GLU A CG  1 
ATOM   5680 C CD  . GLU A 1 704 ? 76.843 103.823 35.471  1.00 32.72 ? 704  GLU A CD  1 
ATOM   5681 O OE1 . GLU A 1 704 ? 77.021 104.016 36.675  1.00 37.28 ? 704  GLU A OE1 1 
ATOM   5682 O OE2 . GLU A 1 704 ? 76.099 102.885 35.051  1.00 39.56 ? 704  GLU A OE2 1 
ATOM   5683 N N   . THR A 1 705 ? 81.823 106.299 33.396  1.00 28.25 ? 705  THR A N   1 
ATOM   5684 C CA  . THR A 1 705 ? 83.181 106.846 33.526  1.00 28.86 ? 705  THR A CA  1 
ATOM   5685 C C   . THR A 1 705 ? 83.589 107.832 32.414  1.00 28.77 ? 705  THR A C   1 
ATOM   5686 O O   . THR A 1 705 ? 84.483 108.660 32.608  1.00 29.00 ? 705  THR A O   1 
ATOM   5687 C CB  . THR A 1 705 ? 84.220 105.736 33.591  1.00 28.79 ? 705  THR A CB  1 
ATOM   5688 O OG1 . THR A 1 705 ? 84.175 105.016 32.367  1.00 29.61 ? 705  THR A OG1 1 
ATOM   5689 C CG2 . THR A 1 705 ? 83.905 104.772 34.751  1.00 29.94 ? 705  THR A CG2 1 
ATOM   5690 N N   . GLY A 1 706 ? 82.945 107.740 31.251  1.00 28.27 ? 706  GLY A N   1 
ATOM   5691 C CA  . GLY A 1 706 ? 83.283 108.597 30.118  1.00 27.50 ? 706  GLY A CA  1 
ATOM   5692 C C   . GLY A 1 706 ? 84.407 107.994 29.281  1.00 27.95 ? 706  GLY A C   1 
ATOM   5693 O O   . GLY A 1 706 ? 84.781 108.521 28.235  1.00 27.15 ? 706  GLY A O   1 
ATOM   5694 N N   . SER A 1 707 ? 84.933 106.873 29.746  1.00 27.92 ? 707  SER A N   1 
ATOM   5695 C CA  . SER A 1 707 ? 86.057 106.208 29.115  1.00 29.22 ? 707  SER A CA  1 
ATOM   5696 C C   . SER A 1 707 ? 85.724 105.575 27.736  1.00 29.33 ? 707  SER A C   1 
ATOM   5697 O O   . SER A 1 707 ? 84.682 104.885 27.575  1.00 27.85 ? 707  SER A O   1 
ATOM   5698 C CB  . SER A 1 707 ? 86.546 105.133 30.080  1.00 29.79 ? 707  SER A CB  1 
ATOM   5699 O OG  . SER A 1 707 ? 87.705 104.509 29.585  1.00 33.23 ? 707  SER A OG  1 
ATOM   5700 N N   . GLN A 1 708 ? 86.606 105.796 26.757  1.00 29.58 ? 708  GLN A N   1 
ATOM   5701 C CA  . GLN A 1 708 ? 86.464 105.158 25.426  1.00 30.95 ? 708  GLN A CA  1 
ATOM   5702 C C   . GLN A 1 708 ? 86.668 103.644 25.485  1.00 31.13 ? 708  GLN A C   1 
ATOM   5703 O O   . GLN A 1 708 ? 87.663 103.171 26.019  1.00 31.38 ? 708  GLN A O   1 
ATOM   5704 C CB  . GLN A 1 708 ? 87.423 105.772 24.392  1.00 31.30 ? 708  GLN A CB  1 
ATOM   5705 C CG  . GLN A 1 708 ? 87.131 105.300 22.972  1.00 30.10 ? 708  GLN A CG  1 
ATOM   5706 C CD  . GLN A 1 708 ? 88.025 105.921 21.915  1.00 32.07 ? 708  GLN A CD  1 
ATOM   5707 O OE1 . GLN A 1 708 ? 88.630 106.971 22.130  1.00 32.07 ? 708  GLN A OE1 1 
ATOM   5708 N NE2 . GLN A 1 708 ? 88.087 105.278 20.736  1.00 32.23 ? 708  GLN A NE2 1 
ATOM   5709 N N   . VAL A 1 709 ? 85.735 102.868 24.944  1.00 31.93 ? 709  VAL A N   1 
ATOM   5710 C CA  . VAL A 1 709 ? 85.915 101.411 25.000  1.00 32.62 ? 709  VAL A CA  1 
ATOM   5711 C C   . VAL A 1 709 ? 86.921 100.949 23.935  1.00 33.91 ? 709  VAL A C   1 
ATOM   5712 O O   . VAL A 1 709 ? 87.078 101.600 22.908  1.00 32.59 ? 709  VAL A O   1 
ATOM   5713 C CB  . VAL A 1 709 ? 84.580 100.634 24.915  1.00 32.79 ? 709  VAL A CB  1 
ATOM   5714 C CG1 . VAL A 1 709 ? 83.561 101.312 25.763  1.00 32.37 ? 709  VAL A CG1 1 
ATOM   5715 C CG2 . VAL A 1 709 ? 84.086 100.551 23.492  1.00 31.36 ? 709  VAL A CG2 1 
ATOM   5716 N N   . ARG A 1 710 ? 87.613 99.845  24.210  1.00 35.91 ? 710  ARG A N   1 
ATOM   5717 C CA  . ARG A 1 710 ? 88.654 99.349  23.315  1.00 39.40 ? 710  ARG A CA  1 
ATOM   5718 C C   . ARG A 1 710 ? 88.028 98.522  22.192  1.00 38.50 ? 710  ARG A C   1 
ATOM   5719 O O   . ARG A 1 710 ? 88.694 98.164  21.230  1.00 39.97 ? 710  ARG A O   1 
ATOM   5720 C CB  . ARG A 1 710 ? 89.702 98.521  24.088  1.00 39.39 ? 710  ARG A CB  1 
ATOM   5721 C CG  . ARG A 1 710 ? 91.044 99.280  24.310  1.00 43.43 ? 710  ARG A CG  1 
ATOM   5722 C CD  . ARG A 1 710 ? 92.048 98.510  25.202  1.00 45.20 ? 710  ARG A CD  1 
ATOM   5723 N NE  . ARG A 1 710 ? 91.729 98.611  26.640  1.00 55.18 ? 710  ARG A NE  1 
ATOM   5724 C CZ  . ARG A 1 710 ? 92.257 97.837  27.602  1.00 58.76 ? 710  ARG A CZ  1 
ATOM   5725 N NH1 . ARG A 1 710 ? 93.146 96.876  27.304  1.00 59.62 ? 710  ARG A NH1 1 
ATOM   5726 N NH2 . ARG A 1 710 ? 91.892 98.022  28.877  1.00 59.68 ? 710  ARG A NH2 1 
ATOM   5727 N N   . TRP A 1 711 ? 86.737 98.252  22.299  1.00 37.54 ? 711  TRP A N   1 
ATOM   5728 C CA  . TRP A 1 711 ? 86.058 97.367  21.355  1.00 36.42 ? 711  TRP A CA  1 
ATOM   5729 C C   . TRP A 1 711 ? 85.431 98.162  20.206  1.00 34.31 ? 711  TRP A C   1 
ATOM   5730 O O   . TRP A 1 711 ? 84.990 99.295  20.395  1.00 33.06 ? 711  TRP A O   1 
ATOM   5731 C CB  . TRP A 1 711 ? 84.986 96.565  22.081  1.00 37.83 ? 711  TRP A CB  1 
ATOM   5732 C CG  . TRP A 1 711 ? 85.423 95.951  23.390  1.00 40.50 ? 711  TRP A CG  1 
ATOM   5733 C CD1 . TRP A 1 711 ? 86.521 95.162  23.602  1.00 42.04 ? 711  TRP A CD1 1 
ATOM   5734 C CD2 . TRP A 1 711 ? 84.742 96.038  24.653  1.00 41.68 ? 711  TRP A CD2 1 
ATOM   5735 N NE1 . TRP A 1 711 ? 86.574 94.773  24.914  1.00 43.69 ? 711  TRP A NE1 1 
ATOM   5736 C CE2 . TRP A 1 711 ? 85.492 95.287  25.583  1.00 43.15 ? 711  TRP A CE2 1 
ATOM   5737 C CE3 . TRP A 1 711 ? 83.571 96.681  25.086  1.00 43.69 ? 711  TRP A CE3 1 
ATOM   5738 C CZ2 . TRP A 1 711 ? 85.113 95.158  26.939  1.00 42.57 ? 711  TRP A CZ2 1 
ATOM   5739 C CZ3 . TRP A 1 711 ? 83.191 96.557  26.441  1.00 43.06 ? 711  TRP A CZ3 1 
ATOM   5740 C CH2 . TRP A 1 711 ? 83.968 95.804  27.346  1.00 42.07 ? 711  TRP A CH2 1 
ATOM   5741 N N   . ARG A 1 712 ? 85.390 97.547  19.025  1.00 32.43 ? 712  ARG A N   1 
ATOM   5742 C CA  . ARG A 1 712 ? 84.766 98.134  17.846  1.00 30.64 ? 712  ARG A CA  1 
ATOM   5743 C C   . ARG A 1 712 ? 84.387 97.047  16.838  1.00 29.94 ? 712  ARG A C   1 
ATOM   5744 O O   . ARG A 1 712 ? 85.243 96.253  16.432  1.00 28.21 ? 712  ARG A O   1 
ATOM   5745 C CB  . ARG A 1 712 ? 85.712 99.144  17.190  1.00 30.18 ? 712  ARG A CB  1 
ATOM   5746 C CG  . ARG A 1 712 ? 85.095 99.815  15.990  1.00 29.58 ? 712  ARG A CG  1 
ATOM   5747 C CD  . ARG A 1 712 ? 85.667 101.184 15.693  1.00 31.19 ? 712  ARG A CD  1 
ATOM   5748 N NE  . ARG A 1 712 ? 84.952 101.825 14.584  1.00 28.71 ? 712  ARG A NE  1 
ATOM   5749 C CZ  . ARG A 1 712 ? 85.030 103.116 14.296  1.00 29.79 ? 712  ARG A CZ  1 
ATOM   5750 N NH1 . ARG A 1 712 ? 85.771 103.915 15.049  1.00 30.24 ? 712  ARG A NH1 1 
ATOM   5751 N NH2 . ARG A 1 712 ? 84.350 103.615 13.276  1.00 28.60 ? 712  ARG A NH2 1 
ATOM   5752 N N   . LYS A 1 713 ? 83.113 97.014  16.433  1.00 29.19 ? 713  LYS A N   1 
ATOM   5753 C CA  . LYS A 1 713 ? 82.646 96.050  15.418  1.00 29.16 ? 713  LYS A CA  1 
ATOM   5754 C C   . LYS A 1 713 ? 83.062 94.640  15.843  1.00 29.02 ? 713  LYS A C   1 
ATOM   5755 O O   . LYS A 1 713 ? 83.792 93.973  15.123  1.00 29.38 ? 713  LYS A O   1 
ATOM   5756 C CB  . LYS A 1 713 ? 83.224 96.402  14.028  1.00 28.82 ? 713  LYS A CB  1 
ATOM   5757 C CG  . LYS A 1 713 ? 82.455 95.831  12.825  1.00 29.54 ? 713  LYS A CG  1 
ATOM   5758 C CD  . LYS A 1 713 ? 83.145 96.107  11.463  1.00 29.85 ? 713  LYS A CD  1 
ATOM   5759 C CE  . LYS A 1 713 ? 82.201 95.733  10.276  1.00 31.32 ? 713  LYS A CE  1 
ATOM   5760 N NZ  . LYS A 1 713 ? 82.934 95.731  8.923   1.00 34.34 ? 713  LYS A NZ  1 
ATOM   5761 N N   . GLN A 1 714 ? 82.643 94.213  17.032  1.00 29.22 ? 714  GLN A N   1 
ATOM   5762 C CA  . GLN A 1 714 ? 82.966 92.872  17.548  1.00 30.44 ? 714  GLN A CA  1 
ATOM   5763 C C   . GLN A 1 714 ? 82.071 92.455  18.720  1.00 30.97 ? 714  GLN A C   1 
ATOM   5764 O O   . GLN A 1 714 ? 81.538 93.308  19.409  1.00 30.30 ? 714  GLN A O   1 
ATOM   5765 C CB  . GLN A 1 714 ? 84.435 92.786  17.972  1.00 30.90 ? 714  GLN A CB  1 
ATOM   5766 C CG  . GLN A 1 714 ? 84.841 93.809  19.014  1.00 32.47 ? 714  GLN A CG  1 
ATOM   5767 C CD  . GLN A 1 714 ? 86.337 93.876  19.182  1.00 38.44 ? 714  GLN A CD  1 
ATOM   5768 O OE1 . GLN A 1 714 ? 87.021 92.846  19.190  1.00 41.29 ? 714  GLN A OE1 1 
ATOM   5769 N NE2 . GLN A 1 714 ? 86.864 95.076  19.306  1.00 38.62 ? 714  GLN A NE2 1 
ATOM   5770 N N   . LYS A 1 715 ? 81.926 91.143  18.918  1.00 31.27 ? 715  LYS A N   1 
ATOM   5771 C CA  . LYS A 1 715 ? 81.263 90.561  20.083  1.00 33.36 ? 715  LYS A CA  1 
ATOM   5772 C C   . LYS A 1 715 ? 82.212 90.551  21.250  1.00 33.77 ? 715  LYS A C   1 
ATOM   5773 O O   . LYS A 1 715 ? 83.379 90.160  21.110  1.00 33.74 ? 715  LYS A O   1 
ATOM   5774 C CB  . LYS A 1 715 ? 80.782 89.122  19.827  1.00 33.58 ? 715  LYS A CB  1 
ATOM   5775 C CG  . LYS A 1 715 ? 79.276 89.015  19.565  1.00 37.12 ? 715  LYS A CG  1 
ATOM   5776 C CD  . LYS A 1 715 ? 78.681 87.653  19.958  1.00 39.79 ? 715  LYS A CD  1 
ATOM   5777 C CE  . LYS A 1 715 ? 77.161 87.806  20.234  1.00 44.65 ? 715  LYS A CE  1 
ATOM   5778 N NZ  . LYS A 1 715 ? 76.337 86.545  20.001  1.00 43.61 ? 715  LYS A NZ  1 
ATOM   5779 N N   . VAL A 1 716 ? 81.718 90.993  22.398  1.00 34.26 ? 716  VAL A N   1 
ATOM   5780 C CA  . VAL A 1 716 ? 82.545 91.078  23.611  1.00 35.23 ? 716  VAL A CA  1 
ATOM   5781 C C   . VAL A 1 716 ? 81.774 90.513  24.801  1.00 35.84 ? 716  VAL A C   1 
ATOM   5782 O O   . VAL A 1 716 ? 80.557 90.420  24.737  1.00 36.20 ? 716  VAL A O   1 
ATOM   5783 C CB  . VAL A 1 716 ? 82.956 92.543  23.914  1.00 35.29 ? 716  VAL A CB  1 
ATOM   5784 C CG1 . VAL A 1 716 ? 83.524 93.236  22.650  1.00 34.62 ? 716  VAL A CG1 1 
ATOM   5785 C CG2 . VAL A 1 716 ? 81.769 93.337  24.464  1.00 34.73 ? 716  VAL A CG2 1 
ATOM   5786 N N   . GLU A 1 717 ? 82.461 90.116  25.875  1.00 36.67 ? 717  GLU A N   1 
ATOM   5787 C CA  . GLU A 1 717 ? 81.747 89.915  27.147  1.00 37.35 ? 717  GLU A CA  1 
ATOM   5788 C C   . GLU A 1 717 ? 81.987 91.114  28.023  1.00 36.05 ? 717  GLU A C   1 
ATOM   5789 O O   . GLU A 1 717 ? 83.122 91.483  28.332  1.00 35.55 ? 717  GLU A O   1 
ATOM   5790 C CB  . GLU A 1 717 ? 82.063 88.597  27.849  1.00 38.18 ? 717  GLU A CB  1 
ATOM   5791 C CG  . GLU A 1 717 ? 83.493 88.401  28.267  1.00 42.80 ? 717  GLU A CG  1 
ATOM   5792 C CD  . GLU A 1 717 ? 83.623 87.260  29.265  1.00 49.18 ? 717  GLU A CD  1 
ATOM   5793 O OE1 . GLU A 1 717 ? 83.191 86.105  28.944  1.00 50.72 ? 717  GLU A OE1 1 
ATOM   5794 O OE2 . GLU A 1 717 ? 84.137 87.541  30.376  1.00 51.72 ? 717  GLU A OE2 1 
ATOM   5795 N N   . MET A 1 718 ? 80.885 91.769  28.349  1.00 35.16 ? 718  MET A N   1 
ATOM   5796 C CA  . MET A 1 718 ? 80.906 93.058  29.027  1.00 34.19 ? 718  MET A CA  1 
ATOM   5797 C C   . MET A 1 718 ? 80.726 92.695  30.482  1.00 32.86 ? 718  MET A C   1 
ATOM   5798 O O   . MET A 1 718 ? 79.799 91.944  30.805  1.00 32.39 ? 718  MET A O   1 
ATOM   5799 C CB  . MET A 1 718 ? 79.709 93.878  28.541  1.00 33.64 ? 718  MET A CB  1 
ATOM   5800 C CG  . MET A 1 718 ? 79.987 95.299  28.256  1.00 35.68 ? 718  MET A CG  1 
ATOM   5801 S SD  . MET A 1 718 ? 78.506 96.126  27.655  1.00 36.41 ? 718  MET A SD  1 
ATOM   5802 C CE  . MET A 1 718 ? 78.899 96.222  25.910  1.00 35.00 ? 718  MET A CE  1 
ATOM   5803 N N   . GLU A 1 719 ? 81.601 93.207  31.348  1.00 32.49 ? 719  GLU A N   1 
ATOM   5804 C CA  . GLU A 1 719 ? 81.533 92.913  32.778  1.00 32.64 ? 719  GLU A CA  1 
ATOM   5805 C C   . GLU A 1 719 ? 80.425 93.773  33.375  1.00 30.69 ? 719  GLU A C   1 
ATOM   5806 O O   . GLU A 1 719 ? 80.493 94.997  33.364  1.00 29.82 ? 719  GLU A O   1 
ATOM   5807 C CB  . GLU A 1 719 ? 82.851 93.225  33.500  1.00 34.04 ? 719  GLU A CB  1 
ATOM   5808 C CG  . GLU A 1 719 ? 82.955 92.520  34.897  1.00 41.13 ? 719  GLU A CG  1 
ATOM   5809 C CD  . GLU A 1 719 ? 83.731 93.314  35.964  1.00 49.41 ? 719  GLU A CD  1 
ATOM   5810 O OE1 . GLU A 1 719 ? 84.791 93.925  35.624  1.00 52.04 ? 719  GLU A OE1 1 
ATOM   5811 O OE2 . GLU A 1 719 ? 83.281 93.301  37.152  1.00 52.07 ? 719  GLU A OE2 1 
ATOM   5812 N N   . LEU A 1 720 ? 79.382 93.121  33.866  1.00 29.20 ? 720  LEU A N   1 
ATOM   5813 C CA  . LEU A 1 720 ? 78.239 93.850  34.412  1.00 27.61 ? 720  LEU A CA  1 
ATOM   5814 C C   . LEU A 1 720 ? 77.781 93.233  35.722  1.00 26.42 ? 720  LEU A C   1 
ATOM   5815 O O   . LEU A 1 720 ? 76.882 92.396  35.730  1.00 26.69 ? 720  LEU A O   1 
ATOM   5816 C CB  . LEU A 1 720 ? 77.086 93.948  33.398  1.00 27.40 ? 720  LEU A CB  1 
ATOM   5817 C CG  . LEU A 1 720 ? 77.342 94.674  32.094  1.00 27.21 ? 720  LEU A CG  1 
ATOM   5818 C CD1 . LEU A 1 720 ? 76.198 94.369  31.146  1.00 25.41 ? 720  LEU A CD1 1 
ATOM   5819 C CD2 . LEU A 1 720 ? 77.549 96.199  32.301  1.00 28.46 ? 720  LEU A CD2 1 
ATOM   5820 N N   . PRO A 1 721 ? 78.399 93.649  36.836  1.00 26.07 ? 721  PRO A N   1 
ATOM   5821 C CA  . PRO A 1 721 ? 78.039 93.150  38.162  1.00 26.02 ? 721  PRO A CA  1 
ATOM   5822 C C   . PRO A 1 721 ? 76.571 93.415  38.531  1.00 26.72 ? 721  PRO A C   1 
ATOM   5823 O O   . PRO A 1 721 ? 75.854 94.129  37.785  1.00 26.66 ? 721  PRO A O   1 
ATOM   5824 C CB  . PRO A 1 721 ? 78.943 93.955  39.091  1.00 26.33 ? 721  PRO A CB  1 
ATOM   5825 C CG  . PRO A 1 721 ? 80.037 94.484  38.245  1.00 26.16 ? 721  PRO A CG  1 
ATOM   5826 C CD  . PRO A 1 721 ? 79.522 94.616  36.876  1.00 26.14 ? 721  PRO A CD  1 
ATOM   5827 N N   . GLY A 1 722 ? 76.140 92.888  39.689  1.00 26.33 ? 722  GLY A N   1 
ATOM   5828 C CA  . GLY A 1 722 ? 74.740 92.981  40.145  1.00 26.06 ? 722  GLY A CA  1 
ATOM   5829 C C   . GLY A 1 722 ? 74.160 94.391  40.142  1.00 26.07 ? 722  GLY A C   1 
ATOM   5830 O O   . GLY A 1 722 ? 72.955 94.578  39.967  1.00 26.69 ? 722  GLY A O   1 
ATOM   5831 N N   . ASP A 1 723 ? 75.028 95.382  40.329  1.00 26.00 ? 723  ASP A N   1 
ATOM   5832 C CA  . ASP A 1 723 ? 74.635 96.780  40.385  1.00 26.52 ? 723  ASP A CA  1 
ATOM   5833 C C   . ASP A 1 723 ? 74.752 97.591  39.056  1.00 25.28 ? 723  ASP A C   1 
ATOM   5834 O O   . ASP A 1 723 ? 74.601 98.815  39.081  1.00 25.70 ? 723  ASP A O   1 
ATOM   5835 C CB  . ASP A 1 723 ? 75.400 97.480  41.523  1.00 27.53 ? 723  ASP A CB  1 
ATOM   5836 C CG  . ASP A 1 723 ? 76.919 97.523  41.292  1.00 31.07 ? 723  ASP A CG  1 
ATOM   5837 O OD1 . ASP A 1 723 ? 77.493 96.708  40.504  1.00 32.79 ? 723  ASP A OD1 1 
ATOM   5838 O OD2 . ASP A 1 723 ? 77.555 98.394  41.918  1.00 34.62 ? 723  ASP A OD2 1 
ATOM   5839 N N   . LYS A 1 724 ? 74.960 96.912  37.917  1.00 23.66 ? 724  LYS A N   1 
ATOM   5840 C CA  . LYS A 1 724 ? 75.192 97.580  36.631  1.00 22.64 ? 724  LYS A CA  1 
ATOM   5841 C C   . LYS A 1 724 ? 74.367 97.058  35.445  1.00 21.55 ? 724  LYS A C   1 
ATOM   5842 O O   . LYS A 1 724 ? 74.031 95.894  35.378  1.00 20.69 ? 724  LYS A O   1 
ATOM   5843 C CB  . LYS A 1 724 ? 76.687 97.487  36.256  1.00 23.44 ? 724  LYS A CB  1 
ATOM   5844 C CG  . LYS A 1 724 ? 77.670 98.058  37.280  1.00 24.48 ? 724  LYS A CG  1 
ATOM   5845 C CD  . LYS A 1 724 ? 77.573 99.600  37.403  1.00 27.76 ? 724  LYS A CD  1 
ATOM   5846 C CE  . LYS A 1 724 ? 78.606 100.186 38.375  1.00 28.47 ? 724  LYS A CE  1 
ATOM   5847 N NZ  . LYS A 1 724 ? 78.287 101.572 38.844  1.00 31.56 ? 724  LYS A NZ  1 
ATOM   5848 N N   . ILE A 1 725 ? 74.078 97.963  34.513  1.00 21.41 ? 725  ILE A N   1 
ATOM   5849 C CA  . ILE A 1 725 ? 73.622 97.693  33.135  1.00 20.20 ? 725  ILE A CA  1 
ATOM   5850 C C   . ILE A 1 725 ? 74.575 98.465  32.205  1.00 20.45 ? 725  ILE A C   1 
ATOM   5851 O O   . ILE A 1 725 ? 75.036 99.529  32.571  1.00 18.96 ? 725  ILE A O   1 
ATOM   5852 C CB  . ILE A 1 725 ? 72.201 98.217  32.948  1.00 20.16 ? 725  ILE A CB  1 
ATOM   5853 C CG1 . ILE A 1 725 ? 71.716 98.075  31.501  1.00 19.44 ? 725  ILE A CG1 1 
ATOM   5854 C CG2 . ILE A 1 725 ? 72.041 99.672  33.437  1.00 17.89 ? 725  ILE A CG2 1 
ATOM   5855 C CD1 . ILE A 1 725 ? 70.209 97.958  31.419  1.00 16.13 ? 725  ILE A CD1 1 
ATOM   5856 N N   . GLY A 1 726 ? 74.892 97.933  31.018  1.00 21.27 ? 726  GLY A N   1 
ATOM   5857 C CA  . GLY A 1 726 ? 75.880 98.624  30.118  1.00 20.07 ? 726  GLY A CA  1 
ATOM   5858 C C   . GLY A 1 726 ? 75.193 99.801  29.468  1.00 19.67 ? 726  GLY A C   1 
ATOM   5859 O O   . GLY A 1 726 ? 74.056 99.688  28.976  1.00 18.52 ? 726  GLY A O   1 
ATOM   5860 N N   . LEU A 1 727 ? 75.838 100.951 29.531  1.00 19.06 ? 727  LEU A N   1 
ATOM   5861 C CA  . LEU A 1 727 ? 75.323 102.137 28.872  1.00 19.31 ? 727  LEU A CA  1 
ATOM   5862 C C   . LEU A 1 727 ? 76.502 102.763 28.148  1.00 18.76 ? 727  LEU A C   1 
ATOM   5863 O O   . LEU A 1 727 ? 77.486 103.116 28.800  1.00 18.08 ? 727  LEU A O   1 
ATOM   5864 C CB  . LEU A 1 727 ? 74.723 103.144 29.890  1.00 18.61 ? 727  LEU A CB  1 
ATOM   5865 C CG  . LEU A 1 727 ? 73.493 102.720 30.710  1.00 19.81 ? 727  LEU A CG  1 
ATOM   5866 C CD1 . LEU A 1 727 ? 73.201 103.781 31.793  1.00 18.88 ? 727  LEU A CD1 1 
ATOM   5867 C CD2 . LEU A 1 727 ? 72.262 102.521 29.811  1.00 15.20 ? 727  LEU A CD2 1 
ATOM   5868 N N   . HIS A 1 728 ? 76.399 102.917 26.824  1.00 17.57 ? 728  HIS A N   1 
ATOM   5869 C CA  . HIS A 1 728 ? 77.453 103.585 26.052  1.00 17.66 ? 728  HIS A CA  1 
ATOM   5870 C C   . HIS A 1 728 ? 76.908 104.652 25.126  1.00 17.95 ? 728  HIS A C   1 
ATOM   5871 O O   . HIS A 1 728 ? 75.812 104.502 24.563  1.00 17.81 ? 728  HIS A O   1 
ATOM   5872 C CB  . HIS A 1 728 ? 78.243 102.562 25.230  1.00 16.96 ? 728  HIS A CB  1 
ATOM   5873 C CG  . HIS A 1 728 ? 78.929 101.546 26.078  1.00 17.96 ? 728  HIS A CG  1 
ATOM   5874 N ND1 . HIS A 1 728 ? 78.275 100.453 26.589  1.00 20.68 ? 728  HIS A ND1 1 
ATOM   5875 C CD2 . HIS A 1 728 ? 80.192 101.494 26.564  1.00 19.75 ? 728  HIS A CD2 1 
ATOM   5876 C CE1 . HIS A 1 728 ? 79.108 99.759  27.349  1.00 22.10 ? 728  HIS A CE1 1 
ATOM   5877 N NE2 . HIS A 1 728 ? 80.283 100.362 27.338  1.00 20.14 ? 728  HIS A NE2 1 
ATOM   5878 N N   . LEU A 1 729 ? 77.697 105.707 24.979  1.00 17.51 ? 729  LEU A N   1 
ATOM   5879 C CA  . LEU A 1 729 ? 77.395 106.863 24.143  1.00 17.85 ? 729  LEU A CA  1 
ATOM   5880 C C   . LEU A 1 729 ? 78.237 106.806 22.906  1.00 18.49 ? 729  LEU A C   1 
ATOM   5881 O O   . LEU A 1 729 ? 79.457 106.516 22.989  1.00 17.93 ? 729  LEU A O   1 
ATOM   5882 C CB  . LEU A 1 729 ? 77.749 108.157 24.867  1.00 17.74 ? 729  LEU A CB  1 
ATOM   5883 C CG  . LEU A 1 729 ? 76.904 108.370 26.117  1.00 18.59 ? 729  LEU A CG  1 
ATOM   5884 C CD1 . LEU A 1 729 ? 77.450 109.541 26.883  1.00 17.69 ? 729  LEU A CD1 1 
ATOM   5885 C CD2 . LEU A 1 729 ? 75.443 108.581 25.784  1.00 17.05 ? 729  LEU A CD2 1 
ATOM   5886 N N   . ARG A 1 730 ? 77.584 107.099 21.776  1.00 17.54 ? 730  ARG A N   1 
ATOM   5887 C CA  . ARG A 1 730 ? 78.183 106.992 20.451  1.00 18.02 ? 730  ARG A CA  1 
ATOM   5888 C C   . ARG A 1 730 ? 79.021 108.247 20.100  1.00 17.90 ? 730  ARG A C   1 
ATOM   5889 O O   . ARG A 1 730 ? 78.545 109.395 20.249  1.00 17.16 ? 730  ARG A O   1 
ATOM   5890 C CB  . ARG A 1 730 ? 77.072 106.752 19.412  1.00 16.98 ? 730  ARG A CB  1 
ATOM   5891 C CG  . ARG A 1 730 ? 77.567 106.336 17.986  1.00 18.22 ? 730  ARG A CG  1 
ATOM   5892 C CD  . ARG A 1 730 ? 76.339 106.011 17.127  1.00 17.40 ? 730  ARG A CD  1 
ATOM   5893 N NE  . ARG A 1 730 ? 76.634 105.941 15.703  1.00 18.93 ? 730  ARG A NE  1 
ATOM   5894 C CZ  . ARG A 1 730 ? 75.711 105.936 14.756  1.00 20.14 ? 730  ARG A CZ  1 
ATOM   5895 N NH1 . ARG A 1 730 ? 74.428 105.964 15.102  1.00 21.33 ? 730  ARG A NH1 1 
ATOM   5896 N NH2 . ARG A 1 730 ? 76.066 105.887 13.466  1.00 17.47 ? 730  ARG A NH2 1 
ATOM   5897 N N   . GLY A 1 731 ? 80.277 108.024 19.692  1.00 17.60 ? 731  GLY A N   1 
ATOM   5898 C CA  . GLY A 1 731 ? 81.096 109.070 19.113  1.00 17.74 ? 731  GLY A CA  1 
ATOM   5899 C C   . GLY A 1 731 ? 80.406 109.724 17.931  1.00 18.49 ? 731  GLY A C   1 
ATOM   5900 O O   . GLY A 1 731 ? 79.919 109.057 17.038  1.00 19.59 ? 731  GLY A O   1 
ATOM   5901 N N   . GLY A 1 732 ? 80.358 111.044 17.925  1.00 18.48 ? 732  GLY A N   1 
ATOM   5902 C CA  . GLY A 1 732 ? 79.687 111.770 16.871  1.00 18.05 ? 732  GLY A CA  1 
ATOM   5903 C C   . GLY A 1 732 ? 78.416 112.459 17.310  1.00 18.40 ? 732  GLY A C   1 
ATOM   5904 O O   . GLY A 1 732 ? 77.827 113.203 16.527  1.00 19.50 ? 732  GLY A O   1 
ATOM   5905 N N   . TYR A 1 733 ? 77.997 112.243 18.555  1.00 18.49 ? 733  TYR A N   1 
ATOM   5906 C CA  . TYR A 1 733 ? 76.666 112.700 19.023  1.00 18.72 ? 733  TYR A CA  1 
ATOM   5907 C C   . TYR A 1 733 ? 76.786 113.527 20.284  1.00 18.58 ? 733  TYR A C   1 
ATOM   5908 O O   . TYR A 1 733 ? 77.638 113.267 21.099  1.00 18.49 ? 733  TYR A O   1 
ATOM   5909 C CB  . TYR A 1 733 ? 75.710 111.477 19.229  1.00 19.38 ? 733  TYR A CB  1 
ATOM   5910 C CG  . TYR A 1 733 ? 75.429 110.819 17.908  1.00 20.71 ? 733  TYR A CG  1 
ATOM   5911 C CD1 . TYR A 1 733 ? 74.282 111.143 17.177  1.00 18.71 ? 733  TYR A CD1 1 
ATOM   5912 C CD2 . TYR A 1 733 ? 76.369 109.953 17.336  1.00 19.43 ? 733  TYR A CD2 1 
ATOM   5913 C CE1 . TYR A 1 733 ? 74.078 110.620 15.921  1.00 18.41 ? 733  TYR A CE1 1 
ATOM   5914 C CE2 . TYR A 1 733 ? 76.161 109.421 16.076  1.00 21.92 ? 733  TYR A CE2 1 
ATOM   5915 C CZ  . TYR A 1 733 ? 75.000 109.760 15.396  1.00 20.14 ? 733  TYR A CZ  1 
ATOM   5916 O OH  . TYR A 1 733 ? 74.796 109.228 14.156  1.00 25.40 ? 733  TYR A OH  1 
ATOM   5917 N N   . ILE A 1 734 ? 75.911 114.512 20.417  1.00 18.72 ? 734  ILE A N   1 
ATOM   5918 C CA  . ILE A 1 734 ? 75.837 115.391 21.565  1.00 18.27 ? 734  ILE A CA  1 
ATOM   5919 C C   . ILE A 1 734 ? 74.454 115.184 22.222  1.00 18.77 ? 734  ILE A C   1 
ATOM   5920 O O   . ILE A 1 734 ? 73.418 115.249 21.541  1.00 17.69 ? 734  ILE A O   1 
ATOM   5921 C CB  . ILE A 1 734 ? 76.021 116.868 21.128  1.00 18.87 ? 734  ILE A CB  1 
ATOM   5922 C CG1 . ILE A 1 734 ? 77.398 117.047 20.484  1.00 18.29 ? 734  ILE A CG1 1 
ATOM   5923 C CG2 . ILE A 1 734 ? 75.835 117.864 22.292  1.00 17.20 ? 734  ILE A CG2 1 
ATOM   5924 C CD1 . ILE A 1 734 ? 77.530 118.442 19.819  1.00 19.27 ? 734  ILE A CD1 1 
ATOM   5925 N N   . PHE A 1 735 ? 74.459 114.921 23.529  1.00 18.40 ? 735  PHE A N   1 
ATOM   5926 C CA  . PHE A 1 735 ? 73.247 114.550 24.277  1.00 18.55 ? 735  PHE A CA  1 
ATOM   5927 C C   . PHE A 1 735 ? 72.863 115.665 25.249  1.00 17.52 ? 735  PHE A C   1 
ATOM   5928 O O   . PHE A 1 735 ? 73.652 116.014 26.119  1.00 18.64 ? 735  PHE A O   1 
ATOM   5929 C CB  . PHE A 1 735 ? 73.482 113.233 25.039  1.00 18.60 ? 735  PHE A CB  1 
ATOM   5930 C CG  . PHE A 1 735 ? 74.017 112.115 24.170  1.00 19.01 ? 735  PHE A CG  1 
ATOM   5931 C CD1 . PHE A 1 735 ? 73.179 111.113 23.702  1.00 18.58 ? 735  PHE A CD1 1 
ATOM   5932 C CD2 . PHE A 1 735 ? 75.360 112.076 23.821  1.00 16.59 ? 735  PHE A CD2 1 
ATOM   5933 C CE1 . PHE A 1 735 ? 73.671 110.069 22.890  1.00 16.66 ? 735  PHE A CE1 1 
ATOM   5934 C CE2 . PHE A 1 735 ? 75.851 111.051 23.003  1.00 17.97 ? 735  PHE A CE2 1 
ATOM   5935 C CZ  . PHE A 1 735 ? 75.009 110.068 22.524  1.00 18.61 ? 735  PHE A CZ  1 
ATOM   5936 N N   . PRO A 1 736 ? 71.686 116.277 25.074  1.00 17.87 ? 736  PRO A N   1 
ATOM   5937 C CA  . PRO A 1 736 ? 71.287 117.234 26.118  1.00 17.23 ? 736  PRO A CA  1 
ATOM   5938 C C   . PRO A 1 736 ? 70.812 116.543 27.417  1.00 17.99 ? 736  PRO A C   1 
ATOM   5939 O O   . PRO A 1 736 ? 70.228 115.425 27.393  1.00 17.90 ? 736  PRO A O   1 
ATOM   5940 C CB  . PRO A 1 736 ? 70.140 118.011 25.466  1.00 17.17 ? 736  PRO A CB  1 
ATOM   5941 C CG  . PRO A 1 736 ? 69.501 117.017 24.504  1.00 17.76 ? 736  PRO A CG  1 
ATOM   5942 C CD  . PRO A 1 736 ? 70.692 116.193 23.978  1.00 17.47 ? 736  PRO A CD  1 
ATOM   5943 N N   . THR A 1 737 ? 71.073 117.197 28.551  1.00 17.79 ? 737  THR A N   1 
ATOM   5944 C CA  . THR A 1 737 ? 70.775 116.638 29.863  1.00 17.86 ? 737  THR A CA  1 
ATOM   5945 C C   . THR A 1 737 ? 70.193 117.736 30.762  1.00 18.22 ? 737  THR A C   1 
ATOM   5946 O O   . THR A 1 737 ? 70.288 118.929 30.461  1.00 19.03 ? 737  THR A O   1 
ATOM   5947 C CB  . THR A 1 737 ? 72.048 116.011 30.531  1.00 19.05 ? 737  THR A CB  1 
ATOM   5948 O OG1 . THR A 1 737 ? 72.959 117.054 30.889  1.00 20.65 ? 737  THR A OG1 1 
ATOM   5949 C CG2 . THR A 1 737 ? 72.797 115.066 29.582  1.00 16.49 ? 737  THR A CG2 1 
ATOM   5950 N N   . GLN A 1 738 ? 69.550 117.328 31.847  1.00 18.47 ? 738  GLN A N   1 
ATOM   5951 C CA  . GLN A 1 738 ? 69.100 118.252 32.847  1.00 18.71 ? 738  GLN A CA  1 
ATOM   5952 C C   . GLN A 1 738 ? 69.267 117.581 34.194  1.00 19.04 ? 738  GLN A C   1 
ATOM   5953 O O   . GLN A 1 738 ? 68.900 116.409 34.334  1.00 19.68 ? 738  GLN A O   1 
ATOM   5954 C CB  . GLN A 1 738 ? 67.656 118.642 32.561  1.00 19.15 ? 738  GLN A CB  1 
ATOM   5955 C CG  . GLN A 1 738 ? 67.086 119.709 33.519  1.00 18.86 ? 738  GLN A CG  1 
ATOM   5956 C CD  . GLN A 1 738 ? 65.804 120.312 32.956  1.00 19.29 ? 738  GLN A CD  1 
ATOM   5957 O OE1 . GLN A 1 738 ? 64.947 119.588 32.433  1.00 18.46 ? 738  GLN A OE1 1 
ATOM   5958 N NE2 . GLN A 1 738 ? 65.669 121.632 33.062  1.00 15.43 ? 738  GLN A NE2 1 
ATOM   5959 N N   . GLN A 1 739 ? 69.837 118.305 35.175  1.00 18.84 ? 739  GLN A N   1 
ATOM   5960 C CA  A GLN A 1 739 ? 70.071 117.766 36.515  0.50 19.42 ? 739  GLN A CA  1 
ATOM   5961 C CA  B GLN A 1 739 ? 70.069 117.750 36.505  0.50 18.49 ? 739  GLN A CA  1 
ATOM   5962 C C   . GLN A 1 739 ? 68.798 117.052 36.973  1.00 19.37 ? 739  GLN A C   1 
ATOM   5963 O O   . GLN A 1 739 ? 67.706 117.619 36.871  1.00 19.82 ? 739  GLN A O   1 
ATOM   5964 C CB  A GLN A 1 739 ? 70.425 118.884 37.506  0.50 19.31 ? 739  GLN A CB  1 
ATOM   5965 C CB  B GLN A 1 739 ? 70.435 118.849 37.495  0.50 18.16 ? 739  GLN A CB  1 
ATOM   5966 C CG  A GLN A 1 739 ? 71.680 119.706 37.156  0.50 20.05 ? 739  GLN A CG  1 
ATOM   5967 C CG  B GLN A 1 739 ? 70.588 118.362 38.922  0.50 15.40 ? 739  GLN A CG  1 
ATOM   5968 C CD  A GLN A 1 739 ? 72.348 120.325 38.393  0.50 20.50 ? 739  GLN A CD  1 
ATOM   5969 C CD  B GLN A 1 739 ? 70.807 119.488 39.893  0.50 13.43 ? 739  GLN A CD  1 
ATOM   5970 O OE1 A GLN A 1 739 ? 71.932 120.068 39.529  0.50 21.38 ? 739  GLN A OE1 1 
ATOM   5971 O OE1 B GLN A 1 739 ? 70.991 120.639 39.481  0.50 15.10 ? 739  GLN A OE1 1 
ATOM   5972 N NE2 A GLN A 1 739 ? 73.397 121.128 38.173  0.50 19.50 ? 739  GLN A NE2 1 
ATOM   5973 N NE2 B GLN A 1 739 ? 70.809 119.173 41.183  0.50 10.00 ? 739  GLN A NE2 1 
ATOM   5974 N N   . PRO A 1 740 ? 68.920 115.810 37.465  1.00 19.70 ? 740  PRO A N   1 
ATOM   5975 C CA  . PRO A 1 740 ? 67.618 115.168 37.780  1.00 20.88 ? 740  PRO A CA  1 
ATOM   5976 C C   . PRO A 1 740 ? 67.059 115.591 39.154  1.00 21.79 ? 740  PRO A C   1 
ATOM   5977 O O   . PRO A 1 740 ? 67.808 116.134 40.021  1.00 21.34 ? 740  PRO A O   1 
ATOM   5978 C CB  . PRO A 1 740 ? 67.969 113.682 37.815  1.00 20.62 ? 740  PRO A CB  1 
ATOM   5979 C CG  . PRO A 1 740 ? 69.403 113.662 38.356  1.00 21.07 ? 740  PRO A CG  1 
ATOM   5980 C CD  . PRO A 1 740 ? 70.068 114.940 37.778  1.00 19.71 ? 740  PRO A CD  1 
ATOM   5981 N N   . ASN A 1 741 ? 65.781 115.284 39.353  1.00 21.54 ? 741  ASN A N   1 
ATOM   5982 C CA  . ASN A 1 741 ? 65.093 115.401 40.646  1.00 22.12 ? 741  ASN A CA  1 
ATOM   5983 C C   . ASN A 1 741 ? 64.067 114.249 40.674  1.00 22.34 ? 741  ASN A C   1 
ATOM   5984 O O   . ASN A 1 741 ? 63.916 113.498 39.687  1.00 21.99 ? 741  ASN A O   1 
ATOM   5985 C CB  . ASN A 1 741 ? 64.381 116.760 40.788  1.00 21.69 ? 741  ASN A CB  1 
ATOM   5986 C CG  . ASN A 1 741 ? 64.242 117.216 42.262  1.00 24.54 ? 741  ASN A CG  1 
ATOM   5987 O OD1 . ASN A 1 741 ? 64.391 116.423 43.196  1.00 27.08 ? 741  ASN A OD1 1 
ATOM   5988 N ND2 . ASN A 1 741 ? 63.963 118.501 42.458  1.00 26.99 ? 741  ASN A ND2 1 
ATOM   5989 N N   . THR A 1 742 ? 63.348 114.114 41.780  1.00 21.47 ? 742  THR A N   1 
ATOM   5990 C CA  . THR A 1 742 ? 62.490 112.951 41.953  1.00 21.98 ? 742  THR A CA  1 
ATOM   5991 C C   . THR A 1 742 ? 61.158 113.093 41.210  1.00 21.28 ? 742  THR A C   1 
ATOM   5992 O O   . THR A 1 742 ? 60.387 112.142 41.173  1.00 23.06 ? 742  THR A O   1 
ATOM   5993 C CB  . THR A 1 742 ? 62.243 112.689 43.431  1.00 22.09 ? 742  THR A CB  1 
ATOM   5994 O OG1 . THR A 1 742 ? 61.597 113.826 43.977  1.00 24.48 ? 742  THR A OG1 1 
ATOM   5995 C CG2 . THR A 1 742 ? 63.547 112.494 44.173  1.00 22.92 ? 742  THR A CG2 1 
ATOM   5996 N N   . THR A 1 743 ? 60.885 114.279 40.655  1.00 20.59 ? 743  THR A N   1 
ATOM   5997 C CA  . THR A 1 743 ? 59.747 114.515 39.723  1.00 20.60 ? 743  THR A CA  1 
ATOM   5998 C C   . THR A 1 743 ? 60.225 115.372 38.542  1.00 19.71 ? 743  THR A C   1 
ATOM   5999 O O   . THR A 1 743 ? 61.158 116.151 38.669  1.00 19.32 ? 743  THR A O   1 
ATOM   6000 C CB  . THR A 1 743 ? 58.510 115.216 40.394  1.00 19.96 ? 743  THR A CB  1 
ATOM   6001 O OG1 . THR A 1 743 ? 58.854 116.570 40.734  1.00 22.44 ? 743  THR A OG1 1 
ATOM   6002 C CG2 . THR A 1 743 ? 58.059 114.486 41.682  1.00 19.19 ? 743  THR A CG2 1 
ATOM   6003 N N   . THR A 1 744 ? 59.596 115.200 37.391  1.00 20.29 ? 744  THR A N   1 
ATOM   6004 C CA  . THR A 1 744 ? 59.847 116.061 36.252  1.00 20.20 ? 744  THR A CA  1 
ATOM   6005 C C   . THR A 1 744 ? 59.244 117.451 36.467  1.00 20.97 ? 744  THR A C   1 
ATOM   6006 O O   . THR A 1 744 ? 59.772 118.412 35.935  1.00 20.76 ? 744  THR A O   1 
ATOM   6007 C CB  . THR A 1 744 ? 59.334 115.446 34.908  1.00 21.49 ? 744  THR A CB  1 
ATOM   6008 O OG1 . THR A 1 744 ? 57.909 115.415 34.923  1.00 20.38 ? 744  THR A OG1 1 
ATOM   6009 C CG2 . THR A 1 744 ? 59.869 113.962 34.676  1.00 17.44 ? 744  THR A CG2 1 
ATOM   6010 N N   . LEU A 1 745 ? 58.152 117.577 37.234  1.00 21.15 ? 745  LEU A N   1 
ATOM   6011 C CA  . LEU A 1 745 ? 57.682 118.930 37.586  1.00 21.26 ? 745  LEU A CA  1 
ATOM   6012 C C   . LEU A 1 745 ? 58.849 119.780 38.122  1.00 21.16 ? 745  LEU A C   1 
ATOM   6013 O O   . LEU A 1 745 ? 59.035 120.913 37.691  1.00 20.77 ? 745  LEU A O   1 
ATOM   6014 C CB  . LEU A 1 745 ? 56.569 118.912 38.622  1.00 21.52 ? 745  LEU A CB  1 
ATOM   6015 C CG  . LEU A 1 745 ? 56.071 120.296 39.092  1.00 23.50 ? 745  LEU A CG  1 
ATOM   6016 C CD1 . LEU A 1 745 ? 55.268 121.006 38.001  1.00 25.12 ? 745  LEU A CD1 1 
ATOM   6017 C CD2 . LEU A 1 745 ? 55.229 120.180 40.349  1.00 22.42 ? 745  LEU A CD2 1 
ATOM   6018 N N   . ALA A 1 746 ? 59.628 119.222 39.041  1.00 20.72 ? 746  ALA A N   1 
ATOM   6019 C CA  . ALA A 1 746 ? 60.799 119.934 39.558  1.00 21.55 ? 746  ALA A CA  1 
ATOM   6020 C C   . ALA A 1 746 ? 62.019 119.870 38.617  1.00 21.87 ? 746  ALA A C   1 
ATOM   6021 O O   . ALA A 1 746 ? 62.768 120.844 38.491  1.00 22.02 ? 746  ALA A O   1 
ATOM   6022 C CB  . ALA A 1 746 ? 61.175 119.373 40.920  1.00 21.42 ? 746  ALA A CB  1 
ATOM   6023 N N   . SER A 1 747 ? 62.249 118.721 37.977  1.00 21.63 ? 747  SER A N   1 
ATOM   6024 C CA  . SER A 1 747 ? 63.538 118.507 37.301  1.00 21.93 ? 747  SER A CA  1 
ATOM   6025 C C   . SER A 1 747 ? 63.619 119.443 36.107  1.00 21.92 ? 747  SER A C   1 
ATOM   6026 O O   . SER A 1 747 ? 64.700 119.911 35.770  1.00 22.01 ? 747  SER A O   1 
ATOM   6027 C CB  . SER A 1 747 ? 63.757 117.033 36.915  1.00 22.14 ? 747  SER A CB  1 
ATOM   6028 O OG  . SER A 1 747 ? 62.948 116.681 35.803  1.00 24.73 ? 747  SER A OG  1 
ATOM   6029 N N   . ARG A 1 748 ? 62.454 119.752 35.518  1.00 21.32 ? 748  ARG A N   1 
ATOM   6030 C CA  . ARG A 1 748 ? 62.337 120.691 34.404  1.00 20.80 ? 748  ARG A CA  1 
ATOM   6031 C C   . ARG A 1 748 ? 62.762 122.126 34.741  1.00 21.05 ? 748  ARG A C   1 
ATOM   6032 O O   . ARG A 1 748 ? 63.042 122.916 33.839  1.00 20.55 ? 748  ARG A O   1 
ATOM   6033 C CB  . ARG A 1 748 ? 60.904 120.718 33.871  1.00 21.17 ? 748  ARG A CB  1 
ATOM   6034 C CG  . ARG A 1 748 ? 60.546 119.576 32.898  1.00 20.90 ? 748  ARG A CG  1 
ATOM   6035 C CD  . ARG A 1 748 ? 59.095 119.657 32.494  1.00 19.55 ? 748  ARG A CD  1 
ATOM   6036 N NE  . ARG A 1 748 ? 58.827 120.899 31.782  1.00 19.66 ? 748  ARG A NE  1 
ATOM   6037 C CZ  . ARG A 1 748 ? 58.996 121.064 30.476  1.00 22.08 ? 748  ARG A CZ  1 
ATOM   6038 N NH1 . ARG A 1 748 ? 59.390 120.043 29.723  1.00 25.70 ? 748  ARG A NH1 1 
ATOM   6039 N NH2 . ARG A 1 748 ? 58.750 122.246 29.913  1.00 21.27 ? 748  ARG A NH2 1 
ATOM   6040 N N   . LYS A 1 749 ? 62.789 122.465 36.025  1.00 21.63 ? 749  LYS A N   1 
ATOM   6041 C CA  . LYS A 1 749 ? 63.305 123.779 36.472  1.00 23.06 ? 749  LYS A CA  1 
ATOM   6042 C C   . LYS A 1 749 ? 64.847 123.832 36.644  1.00 22.03 ? 749  LYS A C   1 
ATOM   6043 O O   . LYS A 1 749 ? 65.390 124.881 36.942  1.00 22.12 ? 749  LYS A O   1 
ATOM   6044 C CB  . LYS A 1 749 ? 62.597 124.225 37.770  1.00 23.32 ? 749  LYS A CB  1 
ATOM   6045 C CG  . LYS A 1 749 ? 61.053 124.338 37.626  1.00 25.73 ? 749  LYS A CG  1 
ATOM   6046 C CD  . LYS A 1 749 ? 60.383 124.489 38.991  1.00 26.20 ? 749  LYS A CD  1 
ATOM   6047 C CE  . LYS A 1 749 ? 58.829 124.475 38.899  1.00 31.45 ? 749  LYS A CE  1 
ATOM   6048 N NZ  . LYS A 1 749 ? 58.119 124.375 40.265  1.00 31.27 ? 749  LYS A NZ  1 
ATOM   6049 N N   . ASN A 1 750 ? 65.542 122.706 36.465  1.00 22.14 ? 750  ASN A N   1 
ATOM   6050 C CA  . ASN A 1 750 ? 66.971 122.591 36.839  1.00 21.75 ? 750  ASN A CA  1 
ATOM   6051 C C   . ASN A 1 750 ? 67.931 123.020 35.734  1.00 21.76 ? 750  ASN A C   1 
ATOM   6052 O O   . ASN A 1 750 ? 67.529 123.118 34.575  1.00 20.88 ? 750  ASN A O   1 
ATOM   6053 C CB  . ASN A 1 750 ? 67.331 121.155 37.296  1.00 22.13 ? 750  ASN A CB  1 
ATOM   6054 C CG  . ASN A 1 750 ? 66.932 120.854 38.757  1.00 21.34 ? 750  ASN A CG  1 
ATOM   6055 O OD1 . ASN A 1 750 ? 66.781 121.745 39.574  1.00 24.54 ? 750  ASN A OD1 1 
ATOM   6056 N ND2 . ASN A 1 750 ? 66.759 119.587 39.069  1.00 20.38 ? 750  ASN A ND2 1 
ATOM   6057 N N   . PRO A 1 751 ? 69.220 123.272 36.089  1.00 23.30 ? 751  PRO A N   1 
ATOM   6058 C CA  . PRO A 1 751 ? 70.267 123.536 35.089  1.00 23.76 ? 751  PRO A CA  1 
ATOM   6059 C C   . PRO A 1 751 ? 70.396 122.409 34.040  1.00 24.44 ? 751  PRO A C   1 
ATOM   6060 O O   . PRO A 1 751 ? 70.263 121.227 34.373  1.00 24.87 ? 751  PRO A O   1 
ATOM   6061 C CB  . PRO A 1 751 ? 71.553 123.579 35.936  1.00 24.44 ? 751  PRO A CB  1 
ATOM   6062 C CG  . PRO A 1 751 ? 71.083 124.073 37.305  1.00 24.57 ? 751  PRO A CG  1 
ATOM   6063 C CD  . PRO A 1 751 ? 69.751 123.347 37.474  1.00 23.53 ? 751  PRO A CD  1 
ATOM   6064 N N   . LEU A 1 752 ? 70.672 122.789 32.798  1.00 24.45 ? 752  LEU A N   1 
ATOM   6065 C CA  . LEU A 1 752 ? 70.912 121.836 31.718  1.00 24.81 ? 752  LEU A CA  1 
ATOM   6066 C C   . LEU A 1 752 ? 72.403 121.531 31.576  1.00 24.55 ? 752  LEU A C   1 
ATOM   6067 O O   . LEU A 1 752 ? 73.266 122.233 32.143  1.00 24.32 ? 752  LEU A O   1 
ATOM   6068 C CB  . LEU A 1 752 ? 70.345 122.378 30.384  1.00 24.67 ? 752  LEU A CB  1 
ATOM   6069 C CG  . LEU A 1 752 ? 68.863 122.775 30.333  1.00 27.20 ? 752  LEU A CG  1 
ATOM   6070 C CD1 . LEU A 1 752 ? 68.640 123.958 29.366  1.00 25.42 ? 752  LEU A CD1 1 
ATOM   6071 C CD2 . LEU A 1 752 ? 68.000 121.587 29.947  1.00 29.68 ? 752  LEU A CD2 1 
ATOM   6072 N N   . GLY A 1 753 ? 72.703 120.490 30.804  1.00 23.77 ? 753  GLY A N   1 
ATOM   6073 C CA  . GLY A 1 753 ? 74.082 120.143 30.468  1.00 22.92 ? 753  GLY A CA  1 
ATOM   6074 C C   . GLY A 1 753 ? 74.188 119.609 29.053  1.00 22.60 ? 753  GLY A C   1 
ATOM   6075 O O   . GLY A 1 753 ? 73.184 119.396 28.377  1.00 21.48 ? 753  GLY A O   1 
ATOM   6076 N N   . LEU A 1 754 ? 75.418 119.424 28.589  1.00 22.40 ? 754  LEU A N   1 
ATOM   6077 C CA  . LEU A 1 754 ? 75.680 118.744 27.299  1.00 22.74 ? 754  LEU A CA  1 
ATOM   6078 C C   . LEU A 1 754 ? 76.697 117.664 27.524  1.00 21.56 ? 754  LEU A C   1 
ATOM   6079 O O   . LEU A 1 754 ? 77.643 117.884 28.232  1.00 21.02 ? 754  LEU A O   1 
ATOM   6080 C CB  . LEU A 1 754 ? 76.231 119.701 26.235  1.00 21.87 ? 754  LEU A CB  1 
ATOM   6081 C CG  . LEU A 1 754 ? 75.251 120.763 25.773  1.00 22.12 ? 754  LEU A CG  1 
ATOM   6082 C CD1 . LEU A 1 754 ? 75.961 121.739 24.840  1.00 22.48 ? 754  LEU A CD1 1 
ATOM   6083 C CD2 . LEU A 1 754 ? 74.024 120.148 25.088  1.00 20.37 ? 754  LEU A CD2 1 
ATOM   6084 N N   . ILE A 1 755 ? 76.459 116.487 26.962  1.00 21.14 ? 755  ILE A N   1 
ATOM   6085 C CA  . ILE A 1 755 ? 77.508 115.479 26.861  1.00 21.15 ? 755  ILE A CA  1 
ATOM   6086 C C   . ILE A 1 755 ? 77.928 115.426 25.384  1.00 21.45 ? 755  ILE A C   1 
ATOM   6087 O O   . ILE A 1 755 ? 77.133 115.041 24.522  1.00 21.55 ? 755  ILE A O   1 
ATOM   6088 C CB  . ILE A 1 755 ? 77.094 114.081 27.374  1.00 19.54 ? 755  ILE A CB  1 
ATOM   6089 C CG1 . ILE A 1 755 ? 76.656 114.175 28.831  1.00 19.84 ? 755  ILE A CG1 1 
ATOM   6090 C CG2 . ILE A 1 755 ? 78.287 113.082 27.246  1.00 21.95 ? 755  ILE A CG2 1 
ATOM   6091 C CD1 . ILE A 1 755 ? 76.030 112.885 29.393  1.00 22.06 ? 755  ILE A CD1 1 
ATOM   6092 N N   . ILE A 1 756 ? 79.159 115.843 25.101  1.00 21.22 ? 756  ILE A N   1 
ATOM   6093 C CA  . ILE A 1 756 ? 79.695 115.766 23.751  1.00 22.13 ? 756  ILE A CA  1 
ATOM   6094 C C   . ILE A 1 756 ? 80.571 114.511 23.596  1.00 22.84 ? 756  ILE A C   1 
ATOM   6095 O O   . ILE A 1 756 ? 81.683 114.447 24.136  1.00 21.95 ? 756  ILE A O   1 
ATOM   6096 C CB  . ILE A 1 756 ? 80.488 117.051 23.435  1.00 21.96 ? 756  ILE A CB  1 
ATOM   6097 C CG1 . ILE A 1 756 ? 79.588 118.293 23.605  1.00 22.68 ? 756  ILE A CG1 1 
ATOM   6098 C CG2 . ILE A 1 756 ? 81.117 116.988 22.027  1.00 24.13 ? 756  ILE A CG2 1 
ATOM   6099 C CD1 . ILE A 1 756 ? 80.320 119.654 23.558  1.00 22.38 ? 756  ILE A CD1 1 
ATOM   6100 N N   . ALA A 1 757 ? 80.084 113.502 22.864  1.00 23.38 ? 757  ALA A N   1 
ATOM   6101 C CA  . ALA A 1 757 ? 80.939 112.337 22.581  1.00 22.99 ? 757  ALA A CA  1 
ATOM   6102 C C   . ALA A 1 757 ? 81.641 112.479 21.216  1.00 23.32 ? 757  ALA A C   1 
ATOM   6103 O O   . ALA A 1 757 ? 81.014 112.373 20.154  1.00 23.50 ? 757  ALA A O   1 
ATOM   6104 C CB  . ALA A 1 757 ? 80.141 111.065 22.637  1.00 22.49 ? 757  ALA A CB  1 
ATOM   6105 N N   . LEU A 1 758 ? 82.942 112.711 21.224  1.00 24.01 ? 758  LEU A N   1 
ATOM   6106 C CA  . LEU A 1 758 ? 83.645 113.025 19.961  1.00 24.27 ? 758  LEU A CA  1 
ATOM   6107 C C   . LEU A 1 758 ? 83.837 111.788 19.090  1.00 24.67 ? 758  LEU A C   1 
ATOM   6108 O O   . LEU A 1 758 ? 84.030 110.677 19.601  1.00 24.64 ? 758  LEU A O   1 
ATOM   6109 C CB  . LEU A 1 758 ? 84.983 113.745 20.232  1.00 24.08 ? 758  LEU A CB  1 
ATOM   6110 C CG  . LEU A 1 758 ? 84.852 115.132 20.903  1.00 23.77 ? 758  LEU A CG  1 
ATOM   6111 C CD1 . LEU A 1 758 ? 86.213 115.716 21.132  1.00 22.88 ? 758  LEU A CD1 1 
ATOM   6112 C CD2 . LEU A 1 758 ? 83.986 116.096 20.090  1.00 21.73 ? 758  LEU A CD2 1 
ATOM   6113 N N   . ASP A 1 759 ? 83.783 111.971 17.777  1.00 26.28 ? 759  ASP A N   1 
ATOM   6114 C CA  . ASP A 1 759 ? 84.156 110.869 16.859  1.00 27.96 ? 759  ASP A CA  1 
ATOM   6115 C C   . ASP A 1 759 ? 85.648 110.953 16.536  1.00 29.40 ? 759  ASP A C   1 
ATOM   6116 O O   . ASP A 1 759 ? 86.352 111.789 17.114  1.00 29.39 ? 759  ASP A O   1 
ATOM   6117 C CB  . ASP A 1 759 ? 83.262 110.863 15.609  1.00 27.62 ? 759  ASP A CB  1 
ATOM   6118 C CG  . ASP A 1 759 ? 83.470 112.076 14.717  1.00 29.86 ? 759  ASP A CG  1 
ATOM   6119 O OD1 . ASP A 1 759 ? 84.479 112.812 14.888  1.00 28.54 ? 759  ASP A OD1 1 
ATOM   6120 O OD2 . ASP A 1 759 ? 82.611 112.295 13.818  1.00 31.41 ? 759  ASP A OD2 1 
ATOM   6121 N N   . GLU A 1 760 ? 86.137 110.105 15.630  1.00 31.10 ? 760  GLU A N   1 
ATOM   6122 C CA  . GLU A 1 760 ? 87.580 110.051 15.296  1.00 32.81 ? 760  GLU A CA  1 
ATOM   6123 C C   . GLU A 1 760 ? 88.133 111.370 14.753  1.00 32.80 ? 760  GLU A C   1 
ATOM   6124 O O   . GLU A 1 760 ? 89.319 111.644 14.892  1.00 32.54 ? 760  GLU A O   1 
ATOM   6125 C CB  . GLU A 1 760 ? 87.900 108.931 14.299  1.00 33.42 ? 760  GLU A CB  1 
ATOM   6126 C CG  . GLU A 1 760 ? 87.275 107.581 14.591  1.00 38.41 ? 760  GLU A CG  1 
ATOM   6127 C CD  . GLU A 1 760 ? 85.940 107.389 13.864  1.00 43.66 ? 760  GLU A CD  1 
ATOM   6128 O OE1 . GLU A 1 760 ? 85.852 106.411 13.093  1.00 45.28 ? 760  GLU A OE1 1 
ATOM   6129 O OE2 . GLU A 1 760 ? 84.994 108.213 14.039  1.00 45.63 ? 760  GLU A OE2 1 
ATOM   6130 N N   . ASN A 1 761 ? 87.270 112.188 14.146  1.00 32.48 ? 761  ASN A N   1 
ATOM   6131 C CA  . ASN A 1 761 ? 87.699 113.476 13.639  1.00 32.40 ? 761  ASN A CA  1 
ATOM   6132 C C   . ASN A 1 761 ? 87.479 114.598 14.636  1.00 31.59 ? 761  ASN A C   1 
ATOM   6133 O O   . ASN A 1 761 ? 87.691 115.769 14.287  1.00 31.72 ? 761  ASN A O   1 
ATOM   6134 C CB  . ASN A 1 761 ? 87.020 113.821 12.307  1.00 33.22 ? 761  ASN A CB  1 
ATOM   6135 C CG  . ASN A 1 761 ? 87.080 112.672 11.301  1.00 36.69 ? 761  ASN A CG  1 
ATOM   6136 O OD1 . ASN A 1 761 ? 88.081 111.941 11.217  1.00 41.27 ? 761  ASN A OD1 1 
ATOM   6137 N ND2 . ASN A 1 761 ? 85.990 112.485 10.556  1.00 40.09 ? 761  ASN A ND2 1 
ATOM   6138 N N   . LYS A 1 762 ? 87.097 114.246 15.876  1.00 29.93 ? 762  LYS A N   1 
ATOM   6139 C CA  . LYS A 1 762 ? 86.837 115.236 16.947  1.00 28.66 ? 762  LYS A CA  1 
ATOM   6140 C C   . LYS A 1 762 ? 85.641 116.111 16.597  1.00 28.50 ? 762  LYS A C   1 
ATOM   6141 O O   . LYS A 1 762 ? 85.605 117.313 16.897  1.00 27.93 ? 762  LYS A O   1 
ATOM   6142 C CB  . LYS A 1 762 ? 88.063 116.103 17.303  1.00 30.31 ? 762  LYS A CB  1 
ATOM   6143 C CG  . LYS A 1 762 ? 89.405 115.367 17.598  1.00 29.31 ? 762  LYS A CG  1 
ATOM   6144 C CD  . LYS A 1 762 ? 89.243 114.172 18.565  1.00 35.02 ? 762  LYS A CD  1 
ATOM   6145 C CE  . LYS A 1 762 ? 90.454 113.197 18.475  1.00 37.39 ? 762  LYS A CE  1 
ATOM   6146 N NZ  . LYS A 1 762 ? 90.140 111.883 19.131  1.00 41.60 ? 762  LYS A NZ  1 
ATOM   6147 N N   . GLU A 1 763 ? 84.639 115.480 15.971  1.00 27.68 ? 763  GLU A N   1 
ATOM   6148 C CA  . GLU A 1 763 ? 83.373 116.140 15.612  1.00 27.05 ? 763  GLU A CA  1 
ATOM   6149 C C   . GLU A 1 763 ? 82.186 115.434 16.280  1.00 24.65 ? 763  GLU A C   1 
ATOM   6150 O O   . GLU A 1 763 ? 82.272 114.264 16.677  1.00 23.15 ? 763  GLU A O   1 
ATOM   6151 C CB  . GLU A 1 763 ? 83.199 116.199 14.072  1.00 26.13 ? 763  GLU A CB  1 
ATOM   6152 C CG  . GLU A 1 763 ? 84.369 116.953 13.425  1.00 30.84 ? 763  GLU A CG  1 
ATOM   6153 C CD  . GLU A 1 763 ? 84.206 117.281 11.942  1.00 31.88 ? 763  GLU A CD  1 
ATOM   6154 O OE1 . GLU A 1 763 ? 83.652 116.472 11.179  1.00 39.22 ? 763  GLU A OE1 1 
ATOM   6155 O OE2 . GLU A 1 763 ? 84.676 118.365 11.530  1.00 40.26 ? 763  GLU A OE2 1 
ATOM   6156 N N   . ALA A 1 764 ? 81.081 116.166 16.400  1.00 23.27 ? 764  ALA A N   1 
ATOM   6157 C CA  . ALA A 1 764 ? 79.877 115.651 17.044  1.00 21.54 ? 764  ALA A CA  1 
ATOM   6158 C C   . ALA A 1 764 ? 78.713 116.583 16.688  1.00 21.30 ? 764  ALA A C   1 
ATOM   6159 O O   . ALA A 1 764 ? 78.931 117.744 16.350  1.00 21.30 ? 764  ALA A O   1 
ATOM   6160 C CB  . ALA A 1 764 ? 80.086 115.554 18.546  1.00 20.47 ? 764  ALA A CB  1 
ATOM   6161 N N   . LYS A 1 765 ? 77.486 116.072 16.751  1.00 20.58 ? 765  LYS A N   1 
ATOM   6162 C CA  . LYS A 1 765 ? 76.306 116.843 16.435  1.00 21.18 ? 765  LYS A CA  1 
ATOM   6163 C C   . LYS A 1 765 ? 75.163 116.361 17.336  1.00 20.19 ? 765  LYS A C   1 
ATOM   6164 O O   . LYS A 1 765 ? 75.113 115.193 17.678  1.00 19.45 ? 765  LYS A O   1 
ATOM   6165 C CB  . LYS A 1 765 ? 75.907 116.600 14.980  1.00 21.90 ? 765  LYS A CB  1 
ATOM   6166 C CG  . LYS A 1 765 ? 75.679 117.851 14.176  1.00 28.76 ? 765  LYS A CG  1 
ATOM   6167 C CD  . LYS A 1 765 ? 76.326 117.694 12.754  1.00 38.49 ? 765  LYS A CD  1 
ATOM   6168 C CE  . LYS A 1 765 ? 76.991 119.000 12.247  1.00 41.84 ? 765  LYS A CE  1 
ATOM   6169 N NZ  . LYS A 1 765 ? 76.133 119.854 11.321  1.00 44.04 ? 765  LYS A NZ  1 
ATOM   6170 N N   . GLY A 1 766 ? 74.249 117.259 17.702  1.00 18.58 ? 766  GLY A N   1 
ATOM   6171 C CA  . GLY A 1 766 ? 73.057 116.837 18.441  1.00 19.08 ? 766  GLY A CA  1 
ATOM   6172 C C   . GLY A 1 766 ? 72.032 117.940 18.340  1.00 19.42 ? 766  GLY A C   1 
ATOM   6173 O O   . GLY A 1 766 ? 72.237 118.911 17.625  1.00 18.97 ? 766  GLY A O   1 
ATOM   6174 N N   . GLU A 1 767 ? 70.929 117.795 19.054  1.00 20.14 ? 767  GLU A N   1 
ATOM   6175 C CA  . GLU A 1 767 ? 69.839 118.775 18.978  1.00 21.21 ? 767  GLU A CA  1 
ATOM   6176 C C   . GLU A 1 767 ? 69.035 118.720 20.281  1.00 19.48 ? 767  GLU A C   1 
ATOM   6177 O O   . GLU A 1 767 ? 69.182 117.783 21.050  1.00 18.78 ? 767  GLU A O   1 
ATOM   6178 C CB  . GLU A 1 767 ? 68.954 118.473 17.774  1.00 21.28 ? 767  GLU A CB  1 
ATOM   6179 C CG  . GLU A 1 767 ? 68.188 117.133 17.900  1.00 24.82 ? 767  GLU A CG  1 
ATOM   6180 C CD  . GLU A 1 767 ? 67.469 116.726 16.608  1.00 26.04 ? 767  GLU A CD  1 
ATOM   6181 O OE1 . GLU A 1 767 ? 67.664 117.435 15.605  1.00 33.90 ? 767  GLU A OE1 1 
ATOM   6182 O OE2 . GLU A 1 767 ? 66.707 115.726 16.587  1.00 26.15 ? 767  GLU A OE2 1 
ATOM   6183 N N   . LEU A 1 768 ? 68.229 119.745 20.532  1.00 19.26 ? 768  LEU A N   1 
ATOM   6184 C CA  . LEU A 1 768 ? 67.331 119.795 21.676  1.00 18.99 ? 768  LEU A CA  1 
ATOM   6185 C C   . LEU A 1 768 ? 65.985 120.452 21.305  1.00 18.64 ? 768  LEU A C   1 
ATOM   6186 O O   . LEU A 1 768 ? 65.923 121.565 20.768  1.00 18.47 ? 768  LEU A O   1 
ATOM   6187 C CB  . LEU A 1 768 ? 67.993 120.546 22.858  1.00 19.09 ? 768  LEU A CB  1 
ATOM   6188 C CG  . LEU A 1 768 ? 67.105 120.857 24.072  1.00 18.89 ? 768  LEU A CG  1 
ATOM   6189 C CD1 . LEU A 1 768 ? 66.561 119.608 24.745  1.00 16.57 ? 768  LEU A CD1 1 
ATOM   6190 C CD2 . LEU A 1 768 ? 67.843 121.676 25.088  1.00 19.71 ? 768  LEU A CD2 1 
ATOM   6191 N N   . PHE A 1 769 ? 64.908 119.737 21.590  1.00 18.29 ? 769  PHE A N   1 
ATOM   6192 C CA  . PHE A 1 769 ? 63.573 120.262 21.442  1.00 17.78 ? 769  PHE A CA  1 
ATOM   6193 C C   . PHE A 1 769 ? 63.108 120.682 22.820  1.00 17.81 ? 769  PHE A C   1 
ATOM   6194 O O   . PHE A 1 769 ? 63.313 119.965 23.794  1.00 18.42 ? 769  PHE A O   1 
ATOM   6195 C CB  . PHE A 1 769 ? 62.643 119.166 20.863  1.00 17.36 ? 769  PHE A CB  1 
ATOM   6196 C CG  . PHE A 1 769 ? 61.173 119.514 20.905  1.00 17.47 ? 769  PHE A CG  1 
ATOM   6197 C CD1 . PHE A 1 769 ? 60.606 120.299 19.912  1.00 17.48 ? 769  PHE A CD1 1 
ATOM   6198 C CD2 . PHE A 1 769 ? 60.358 119.025 21.908  1.00 18.74 ? 769  PHE A CD2 1 
ATOM   6199 C CE1 . PHE A 1 769 ? 59.255 120.587 19.925  1.00 18.77 ? 769  PHE A CE1 1 
ATOM   6200 C CE2 . PHE A 1 769 ? 58.997 119.320 21.923  1.00 18.85 ? 769  PHE A CE2 1 
ATOM   6201 C CZ  . PHE A 1 769 ? 58.460 120.099 20.934  1.00 18.52 ? 769  PHE A CZ  1 
ATOM   6202 N N   . TRP A 1 770 ? 62.439 121.824 22.909  1.00 19.00 ? 770  TRP A N   1 
ATOM   6203 C CA  . TRP A 1 770 ? 61.935 122.279 24.202  1.00 19.79 ? 770  TRP A CA  1 
ATOM   6204 C C   . TRP A 1 770 ? 60.612 122.999 24.029  1.00 19.66 ? 770  TRP A C   1 
ATOM   6205 O O   . TRP A 1 770 ? 60.508 123.900 23.223  1.00 20.29 ? 770  TRP A O   1 
ATOM   6206 C CB  . TRP A 1 770 ? 62.957 123.176 24.929  1.00 20.26 ? 770  TRP A CB  1 
ATOM   6207 C CG  . TRP A 1 770 ? 62.676 123.269 26.408  1.00 22.57 ? 770  TRP A CG  1 
ATOM   6208 C CD1 . TRP A 1 770 ? 62.088 124.314 27.057  1.00 22.12 ? 770  TRP A CD1 1 
ATOM   6209 C CD2 . TRP A 1 770 ? 62.931 122.263 27.407  1.00 23.18 ? 770  TRP A CD2 1 
ATOM   6210 N NE1 . TRP A 1 770 ? 61.978 124.027 28.396  1.00 23.80 ? 770  TRP A NE1 1 
ATOM   6211 C CE2 . TRP A 1 770 ? 62.471 122.774 28.639  1.00 22.06 ? 770  TRP A CE2 1 
ATOM   6212 C CE3 . TRP A 1 770 ? 63.493 120.970 27.376  1.00 25.35 ? 770  TRP A CE3 1 
ATOM   6213 C CZ2 . TRP A 1 770 ? 62.575 122.053 29.852  1.00 21.96 ? 770  TRP A CZ2 1 
ATOM   6214 C CZ3 . TRP A 1 770 ? 63.592 120.242 28.582  1.00 23.18 ? 770  TRP A CZ3 1 
ATOM   6215 C CH2 . TRP A 1 770 ? 63.142 120.795 29.808  1.00 21.69 ? 770  TRP A CH2 1 
ATOM   6216 N N   . ASP A 1 771 ? 59.591 122.555 24.748  1.00 19.90 ? 771  ASP A N   1 
ATOM   6217 C CA  . ASP A 1 771 ? 58.327 123.272 24.749  1.00 20.48 ? 771  ASP A CA  1 
ATOM   6218 C C   . ASP A 1 771 ? 57.847 123.253 26.188  1.00 20.65 ? 771  ASP A C   1 
ATOM   6219 O O   . ASP A 1 771 ? 58.634 122.945 27.082  1.00 20.17 ? 771  ASP A O   1 
ATOM   6220 C CB  . ASP A 1 771 ? 57.352 122.667 23.711  1.00 19.65 ? 771  ASP A CB  1 
ATOM   6221 C CG  . ASP A 1 771 ? 56.820 121.290 24.103  1.00 20.21 ? 771  ASP A CG  1 
ATOM   6222 O OD1 . ASP A 1 771 ? 57.302 120.701 25.084  1.00 20.49 ? 771  ASP A OD1 1 
ATOM   6223 O OD2 . ASP A 1 771 ? 55.890 120.794 23.421  1.00 17.98 ? 771  ASP A OD2 1 
ATOM   6224 N N   . ASP A 1 772 ? 56.575 123.570 26.419  1.00 21.79 ? 772  ASP A N   1 
ATOM   6225 C CA  . ASP A 1 772 ? 56.024 123.597 27.765  1.00 21.98 ? 772  ASP A CA  1 
ATOM   6226 C C   . ASP A 1 772 ? 55.757 122.209 28.393  1.00 21.98 ? 772  ASP A C   1 
ATOM   6227 O O   . ASP A 1 772 ? 55.442 122.108 29.576  1.00 21.99 ? 772  ASP A O   1 
ATOM   6228 C CB  . ASP A 1 772 ? 54.803 124.566 27.840  1.00 21.78 ? 772  ASP A CB  1 
ATOM   6229 C CG  . ASP A 1 772 ? 53.511 123.960 27.299  1.00 24.67 ? 772  ASP A CG  1 
ATOM   6230 O OD1 . ASP A 1 772 ? 53.480 122.762 26.914  1.00 24.33 ? 772  ASP A OD1 1 
ATOM   6231 O OD2 . ASP A 1 772 ? 52.489 124.689 27.280  1.00 27.10 ? 772  ASP A OD2 1 
ATOM   6232 N N   . GLY A 1 773 ? 55.926 121.134 27.615  1.00 22.03 ? 773  GLY A N   1 
ATOM   6233 C CA  . GLY A 1 773 ? 55.889 119.771 28.161  1.00 21.47 ? 773  GLY A CA  1 
ATOM   6234 C C   . GLY A 1 773 ? 54.514 119.161 28.324  1.00 22.00 ? 773  GLY A C   1 
ATOM   6235 O O   . GLY A 1 773 ? 54.378 118.002 28.745  1.00 20.62 ? 773  GLY A O   1 
ATOM   6236 N N   . GLU A 1 774 ? 53.483 119.937 28.000  1.00 22.72 ? 774  GLU A N   1 
ATOM   6237 C CA  . GLU A 1 774 ? 52.120 119.476 28.234  1.00 24.02 ? 774  GLU A CA  1 
ATOM   6238 C C   . GLU A 1 774 ? 51.050 120.003 27.292  1.00 24.24 ? 774  GLU A C   1 
ATOM   6239 O O   . GLU A 1 774 ? 50.015 119.352 27.151  1.00 24.67 ? 774  GLU A O   1 
ATOM   6240 C CB  . GLU A 1 774 ? 51.723 119.736 29.679  1.00 24.99 ? 774  GLU A CB  1 
ATOM   6241 C CG  . GLU A 1 774 ? 51.745 121.186 30.057  1.00 27.55 ? 774  GLU A CG  1 
ATOM   6242 C CD  . GLU A 1 774 ? 51.241 121.406 31.474  1.00 34.36 ? 774  GLU A CD  1 
ATOM   6243 O OE1 . GLU A 1 774 ? 51.979 120.998 32.402  1.00 35.13 ? 774  GLU A OE1 1 
ATOM   6244 O OE2 . GLU A 1 774 ? 50.115 121.974 31.650  1.00 36.00 ? 774  GLU A OE2 1 
ATOM   6245 N N   . THR A 1 775 ? 51.261 121.147 26.633  1.00 24.05 ? 775  THR A N   1 
ATOM   6246 C CA  . THR A 1 775 ? 50.200 121.627 25.719  1.00 23.63 ? 775  THR A CA  1 
ATOM   6247 C C   . THR A 1 775 ? 50.034 120.740 24.473  1.00 23.65 ? 775  THR A C   1 
ATOM   6248 O O   . THR A 1 775 ? 51.040 120.360 23.814  1.00 21.83 ? 775  THR A O   1 
ATOM   6249 C CB  . THR A 1 775 ? 50.388 123.099 25.336  1.00 24.50 ? 775  THR A CB  1 
ATOM   6250 O OG1 . THR A 1 775 ? 50.499 123.878 26.533  1.00 22.98 ? 775  THR A OG1 1 
ATOM   6251 C CG2 . THR A 1 775 ? 49.186 123.632 24.479  1.00 24.52 ? 775  THR A CG2 1 
ATOM   6252 N N   . LYS A 1 776 ? 48.773 120.417 24.142  1.00 23.34 ? 776  LYS A N   1 
ATOM   6253 C CA  . LYS A 1 776 ? 48.493 119.625 22.959  1.00 24.84 ? 776  LYS A CA  1 
ATOM   6254 C C   . LYS A 1 776 ? 48.842 120.423 21.712  1.00 24.90 ? 776  LYS A C   1 
ATOM   6255 O O   . LYS A 1 776 ? 48.475 121.591 21.604  1.00 24.47 ? 776  LYS A O   1 
ATOM   6256 C CB  . LYS A 1 776 ? 47.026 119.161 22.906  1.00 24.60 ? 776  LYS A CB  1 
ATOM   6257 C CG  . LYS A 1 776 ? 46.757 118.033 21.901  1.00 26.56 ? 776  LYS A CG  1 
ATOM   6258 C CD  . LYS A 1 776 ? 45.354 117.432 22.024  1.00 27.27 ? 776  LYS A CD  1 
ATOM   6259 C CE  . LYS A 1 776 ? 45.304 116.178 22.931  1.00 31.49 ? 776  LYS A CE  1 
ATOM   6260 N NZ  . LYS A 1 776 ? 43.941 115.465 22.947  1.00 32.24 ? 776  LYS A NZ  1 
ATOM   6261 N N   . ASP A 1 777 ? 49.544 119.777 20.778  1.00 25.70 ? 777  ASP A N   1 
ATOM   6262 C CA  . ASP A 1 777 ? 49.827 120.334 19.436  1.00 26.89 ? 777  ASP A CA  1 
ATOM   6263 C C   . ASP A 1 777 ? 50.704 121.595 19.433  1.00 26.77 ? 777  ASP A C   1 
ATOM   6264 O O   . ASP A 1 777 ? 50.562 122.461 18.563  1.00 26.25 ? 777  ASP A O   1 
ATOM   6265 C CB  . ASP A 1 777 ? 48.541 120.564 18.638  1.00 27.11 ? 777  ASP A CB  1 
ATOM   6266 C CG  . ASP A 1 777 ? 47.947 119.272 18.121  1.00 31.90 ? 777  ASP A CG  1 
ATOM   6267 O OD1 . ASP A 1 777 ? 48.751 118.384 17.713  1.00 36.08 ? 777  ASP A OD1 1 
ATOM   6268 O OD2 . ASP A 1 777 ? 46.695 119.133 18.124  1.00 33.50 ? 777  ASP A OD2 1 
ATOM   6269 N N   . THR A 1 778 ? 51.634 121.682 20.388  1.00 25.97 ? 778  THR A N   1 
ATOM   6270 C CA  . THR A 1 778 ? 52.682 122.710 20.305  1.00 25.23 ? 778  THR A CA  1 
ATOM   6271 C C   . THR A 1 778 ? 53.472 122.635 18.997  1.00 25.06 ? 778  THR A C   1 
ATOM   6272 O O   . THR A 1 778 ? 53.965 123.648 18.520  1.00 26.11 ? 778  THR A O   1 
ATOM   6273 C CB  . THR A 1 778 ? 53.650 122.625 21.491  1.00 25.22 ? 778  THR A CB  1 
ATOM   6274 O OG1 . THR A 1 778 ? 54.170 121.287 21.603  1.00 26.82 ? 778  THR A OG1 1 
ATOM   6275 C CG2 . THR A 1 778 ? 52.948 123.003 22.757  1.00 23.42 ? 778  THR A CG2 1 
ATOM   6276 N N   . VAL A 1 779 ? 53.621 121.443 18.418  1.00 24.96 ? 779  VAL A N   1 
ATOM   6277 C CA  . VAL A 1 779 ? 54.425 121.280 17.180  1.00 24.59 ? 779  VAL A CA  1 
ATOM   6278 C C   . VAL A 1 779 ? 53.635 121.753 15.949  1.00 25.62 ? 779  VAL A C   1 
ATOM   6279 O O   . VAL A 1 779 ? 54.152 122.530 15.148  1.00 25.40 ? 779  VAL A O   1 
ATOM   6280 C CB  . VAL A 1 779 ? 54.977 119.849 17.011  1.00 24.33 ? 779  VAL A CB  1 
ATOM   6281 C CG1 . VAL A 1 779 ? 55.564 119.637 15.640  1.00 23.46 ? 779  VAL A CG1 1 
ATOM   6282 C CG2 . VAL A 1 779 ? 56.018 119.527 18.105  1.00 23.56 ? 779  VAL A CG2 1 
ATOM   6283 N N   . ALA A 1 780 ? 52.389 121.293 15.810  1.00 25.96 ? 780  ALA A N   1 
ATOM   6284 C CA  . ALA A 1 780 ? 51.531 121.729 14.719  1.00 27.34 ? 780  ALA A CA  1 
ATOM   6285 C C   . ALA A 1 780 ? 51.323 123.258 14.785  1.00 28.22 ? 780  ALA A C   1 
ATOM   6286 O O   . ALA A 1 780 ? 51.384 123.943 13.761  1.00 29.02 ? 780  ALA A O   1 
ATOM   6287 C CB  . ALA A 1 780 ? 50.180 120.982 14.737  1.00 27.42 ? 780  ALA A CB  1 
ATOM   6288 N N   . ASN A 1 781 ? 51.146 123.804 15.984  1.00 28.40 ? 781  ASN A N   1 
ATOM   6289 C CA  . ASN A 1 781 ? 51.006 125.262 16.120  1.00 28.40 ? 781  ASN A CA  1 
ATOM   6290 C C   . ASN A 1 781 ? 52.321 126.032 16.279  1.00 28.46 ? 781  ASN A C   1 
ATOM   6291 O O   . ASN A 1 781 ? 52.314 127.240 16.538  1.00 28.51 ? 781  ASN A O   1 
ATOM   6292 C CB  . ASN A 1 781 ? 50.025 125.604 17.248  1.00 28.63 ? 781  ASN A CB  1 
ATOM   6293 C CG  . ASN A 1 781 ? 48.686 124.942 17.054  1.00 28.25 ? 781  ASN A CG  1 
ATOM   6294 O OD1 . ASN A 1 781 ? 48.111 124.419 17.991  1.00 32.49 ? 781  ASN A OD1 1 
ATOM   6295 N ND2 . ASN A 1 781 ? 48.197 124.934 15.828  1.00 27.94 ? 781  ASN A ND2 1 
ATOM   6296 N N   . LYS A 1 782 ? 53.445 125.326 16.153  1.00 28.51 ? 782  LYS A N   1 
ATOM   6297 C CA  . LYS A 1 782 ? 54.771 125.953 16.172  1.00 28.29 ? 782  LYS A CA  1 
ATOM   6298 C C   . LYS A 1 782 ? 55.103 126.830 17.404  1.00 27.47 ? 782  LYS A C   1 
ATOM   6299 O O   . LYS A 1 782 ? 55.663 127.907 17.272  1.00 28.30 ? 782  LYS A O   1 
ATOM   6300 C CB  . LYS A 1 782 ? 55.009 126.703 14.851  1.00 29.60 ? 782  LYS A CB  1 
ATOM   6301 C CG  . LYS A 1 782 ? 54.955 125.786 13.630  1.00 33.72 ? 782  LYS A CG  1 
ATOM   6302 C CD  . LYS A 1 782 ? 56.065 126.107 12.627  1.00 41.35 ? 782  LYS A CD  1 
ATOM   6303 C CE  . LYS A 1 782 ? 56.165 125.042 11.519  1.00 42.81 ? 782  LYS A CE  1 
ATOM   6304 N NZ  . LYS A 1 782 ? 57.030 123.850 11.920  1.00 44.76 ? 782  LYS A NZ  1 
ATOM   6305 N N   . VAL A 1 783 ? 54.791 126.346 18.604  1.00 26.16 ? 783  VAL A N   1 
ATOM   6306 C CA  . VAL A 1 783 ? 55.185 127.012 19.844  1.00 25.25 ? 783  VAL A CA  1 
ATOM   6307 C C   . VAL A 1 783 ? 56.239 126.151 20.521  1.00 23.73 ? 783  VAL A C   1 
ATOM   6308 O O   . VAL A 1 783 ? 55.939 125.387 21.456  1.00 23.60 ? 783  VAL A O   1 
ATOM   6309 C CB  . VAL A 1 783 ? 53.964 127.286 20.791  1.00 25.01 ? 783  VAL A CB  1 
ATOM   6310 C CG1 . VAL A 1 783 ? 54.368 128.192 21.969  1.00 24.63 ? 783  VAL A CG1 1 
ATOM   6311 C CG2 . VAL A 1 783 ? 52.835 127.927 20.004  1.00 27.93 ? 783  VAL A CG2 1 
ATOM   6312 N N   . TYR A 1 784 ? 57.466 126.234 20.007  1.00 22.92 ? 784  TYR A N   1 
ATOM   6313 C CA  . TYR A 1 784 ? 58.566 125.447 20.559  1.00 22.70 ? 784  TYR A CA  1 
ATOM   6314 C C   . TYR A 1 784 ? 59.946 126.018 20.268  1.00 22.75 ? 784  TYR A C   1 
ATOM   6315 O O   . TYR A 1 784 ? 60.097 126.892 19.410  1.00 23.38 ? 784  TYR A O   1 
ATOM   6316 C CB  . TYR A 1 784 ? 58.474 123.979 20.123  1.00 22.23 ? 784  TYR A CB  1 
ATOM   6317 C CG  . TYR A 1 784 ? 58.658 123.677 18.637  1.00 22.68 ? 784  TYR A CG  1 
ATOM   6318 C CD1 . TYR A 1 784 ? 59.926 123.382 18.111  1.00 23.23 ? 784  TYR A CD1 1 
ATOM   6319 C CD2 . TYR A 1 784 ? 57.576 123.590 17.793  1.00 22.11 ? 784  TYR A CD2 1 
ATOM   6320 C CE1 . TYR A 1 784 ? 60.088 123.063 16.766  1.00 23.34 ? 784  TYR A CE1 1 
ATOM   6321 C CE2 . TYR A 1 784 ? 57.718 123.272 16.445  1.00 23.33 ? 784  TYR A CE2 1 
ATOM   6322 C CZ  . TYR A 1 784 ? 58.967 123.025 15.937  1.00 24.84 ? 784  TYR A CZ  1 
ATOM   6323 O OH  . TYR A 1 784 ? 59.102 122.702 14.614  1.00 24.28 ? 784  TYR A OH  1 
ATOM   6324 N N   . LEU A 1 785 ? 60.936 125.532 21.012  1.00 21.87 ? 785  LEU A N   1 
ATOM   6325 C CA  . LEU A 1 785 ? 62.329 125.821 20.746  1.00 21.99 ? 785  LEU A CA  1 
ATOM   6326 C C   . LEU A 1 785 ? 62.977 124.581 20.152  1.00 22.17 ? 785  LEU A C   1 
ATOM   6327 O O   . LEU A 1 785 ? 62.734 123.474 20.612  1.00 21.61 ? 785  LEU A O   1 
ATOM   6328 C CB  . LEU A 1 785 ? 63.061 126.235 22.024  1.00 21.38 ? 785  LEU A CB  1 
ATOM   6329 C CG  . LEU A 1 785 ? 64.593 126.324 21.892  1.00 22.32 ? 785  LEU A CG  1 
ATOM   6330 C CD1 . LEU A 1 785 ? 65.025 127.494 21.018  1.00 22.56 ? 785  LEU A CD1 1 
ATOM   6331 C CD2 . LEU A 1 785 ? 65.217 126.436 23.258  1.00 21.27 ? 785  LEU A CD2 1 
ATOM   6332 N N   . LEU A 1 786 ? 63.795 124.774 19.119  1.00 23.70 ? 786  LEU A N   1 
ATOM   6333 C CA  . LEU A 1 786 ? 64.642 123.703 18.590  1.00 24.42 ? 786  LEU A CA  1 
ATOM   6334 C C   . LEU A 1 786 ? 66.013 124.262 18.325  1.00 25.34 ? 786  LEU A C   1 
ATOM   6335 O O   . LEU A 1 786 ? 66.165 125.208 17.560  1.00 25.32 ? 786  LEU A O   1 
ATOM   6336 C CB  . LEU A 1 786 ? 64.046 123.059 17.313  1.00 23.23 ? 786  LEU A CB  1 
ATOM   6337 C CG  . LEU A 1 786 ? 64.829 121.891 16.669  1.00 23.81 ? 786  LEU A CG  1 
ATOM   6338 C CD1 . LEU A 1 786 ? 64.941 120.635 17.584  1.00 21.81 ? 786  LEU A CD1 1 
ATOM   6339 C CD2 . LEU A 1 786 ? 64.191 121.507 15.322  1.00 23.38 ? 786  LEU A CD2 1 
ATOM   6340 N N   . CYS A 1 787 ? 67.012 123.685 18.974  1.00 26.50 ? 787  CYS A N   1 
ATOM   6341 C CA  . CYS A 1 787 ? 68.373 124.050 18.689  1.00 28.90 ? 787  CYS A CA  1 
ATOM   6342 C C   . CYS A 1 787 ? 69.268 122.885 18.265  1.00 28.44 ? 787  CYS A C   1 
ATOM   6343 O O   . CYS A 1 787 ? 68.930 121.709 18.473  1.00 27.65 ? 787  CYS A O   1 
ATOM   6344 C CB  . CYS A 1 787 ? 68.983 124.874 19.821  1.00 29.80 ? 787  CYS A CB  1 
ATOM   6345 S SG  . CYS A 1 787 ? 68.990 124.153 21.419  1.00 36.92 ? 787  CYS A SG  1 
ATOM   6346 N N   . GLU A 1 788 ? 70.368 123.237 17.603  1.00 27.88 ? 788  GLU A N   1 
ATOM   6347 C CA  . GLU A 1 788 ? 71.368 122.283 17.141  1.00 28.39 ? 788  GLU A CA  1 
ATOM   6348 C C   . GLU A 1 788 ? 72.690 122.605 17.821  1.00 27.06 ? 788  GLU A C   1 
ATOM   6349 O O   . GLU A 1 788 ? 73.024 123.768 18.028  1.00 27.32 ? 788  GLU A O   1 
ATOM   6350 C CB  . GLU A 1 788 ? 71.550 122.398 15.635  1.00 29.44 ? 788  GLU A CB  1 
ATOM   6351 C CG  . GLU A 1 788 ? 70.255 122.732 14.862  1.00 36.21 ? 788  GLU A CG  1 
ATOM   6352 C CD  . GLU A 1 788 ? 70.431 123.877 13.812  1.00 44.67 ? 788  GLU A CD  1 
ATOM   6353 O OE1 . GLU A 1 788 ? 71.317 123.769 12.907  1.00 45.98 ? 788  GLU A OE1 1 
ATOM   6354 O OE2 . GLU A 1 788 ? 69.658 124.886 13.892  1.00 46.41 ? 788  GLU A OE2 1 
ATOM   6355 N N   . PHE A 1 789 ? 73.415 121.564 18.185  1.00 25.46 ? 789  PHE A N   1 
ATOM   6356 C CA  . PHE A 1 789 ? 74.752 121.662 18.705  1.00 24.21 ? 789  PHE A CA  1 
ATOM   6357 C C   . PHE A 1 789 ? 75.617 121.011 17.642  1.00 24.96 ? 789  PHE A C   1 
ATOM   6358 O O   . PHE A 1 789 ? 75.275 119.942 17.127  1.00 24.57 ? 789  PHE A O   1 
ATOM   6359 C CB  . PHE A 1 789 ? 74.863 120.889 20.028  1.00 23.84 ? 789  PHE A CB  1 
ATOM   6360 C CG  . PHE A 1 789 ? 73.709 121.122 20.965  1.00 24.31 ? 789  PHE A CG  1 
ATOM   6361 C CD1 . PHE A 1 789 ? 73.551 122.361 21.619  1.00 22.15 ? 789  PHE A CD1 1 
ATOM   6362 C CD2 . PHE A 1 789 ? 72.763 120.107 21.202  1.00 25.86 ? 789  PHE A CD2 1 
ATOM   6363 C CE1 . PHE A 1 789 ? 72.469 122.589 22.498  1.00 23.13 ? 789  PHE A CE1 1 
ATOM   6364 C CE2 . PHE A 1 789 ? 71.656 120.336 22.063  1.00 23.62 ? 789  PHE A CE2 1 
ATOM   6365 C CZ  . PHE A 1 789 ? 71.515 121.572 22.702  1.00 22.73 ? 789  PHE A CZ  1 
ATOM   6366 N N   . SER A 1 790 ? 76.701 121.669 17.261  1.00 25.20 ? 790  SER A N   1 
ATOM   6367 C CA  . SER A 1 790 ? 77.713 121.026 16.458  1.00 27.46 ? 790  SER A CA  1 
ATOM   6368 C C   . SER A 1 790 ? 79.087 121.393 16.955  1.00 27.89 ? 790  SER A C   1 
ATOM   6369 O O   . SER A 1 790 ? 79.358 122.541 17.242  1.00 27.37 ? 790  SER A O   1 
ATOM   6370 C CB  . SER A 1 790 ? 77.569 121.350 14.968  1.00 27.62 ? 790  SER A CB  1 
ATOM   6371 O OG  . SER A 1 790 ? 77.598 122.744 14.738  1.00 33.76 ? 790  SER A OG  1 
ATOM   6372 N N   . VAL A 1 791 ? 79.930 120.378 17.051  1.00 28.95 ? 791  VAL A N   1 
ATOM   6373 C CA  . VAL A 1 791 ? 81.313 120.492 17.450  1.00 30.72 ? 791  VAL A CA  1 
ATOM   6374 C C   . VAL A 1 791 ? 82.214 120.117 16.259  1.00 32.50 ? 791  VAL A C   1 
ATOM   6375 O O   . VAL A 1 791 ? 81.959 119.134 15.546  1.00 31.19 ? 791  VAL A O   1 
ATOM   6376 C CB  . VAL A 1 791 ? 81.627 119.574 18.664  1.00 30.64 ? 791  VAL A CB  1 
ATOM   6377 C CG1 . VAL A 1 791 ? 83.115 119.594 18.995  1.00 31.74 ? 791  VAL A CG1 1 
ATOM   6378 C CG2 . VAL A 1 791 ? 80.829 120.024 19.867  1.00 29.77 ? 791  VAL A CG2 1 
ATOM   6379 N N   . THR A 1 792 ? 83.195 120.982 16.011  1.00 34.27 ? 792  THR A N   1 
ATOM   6380 C CA  . THR A 1 792 ? 84.311 120.696 15.118  1.00 37.01 ? 792  THR A CA  1 
ATOM   6381 C C   . THR A 1 792 ? 85.554 120.839 15.976  1.00 38.20 ? 792  THR A C   1 
ATOM   6382 O O   . THR A 1 792 ? 85.453 121.054 17.203  1.00 38.40 ? 792  THR A O   1 
ATOM   6383 C CB  . THR A 1 792 ? 84.388 121.684 13.947  1.00 36.92 ? 792  THR A CB  1 
ATOM   6384 O OG1 . THR A 1 792 ? 84.116 123.012 14.429  1.00 38.57 ? 792  THR A OG1 1 
ATOM   6385 C CG2 . THR A 1 792 ? 83.360 121.315 12.896  1.00 37.26 ? 792  THR A CG2 1 
ATOM   6386 N N   . GLN A 1 793 ? 86.728 120.715 15.363  1.00 39.46 ? 793  GLN A N   1 
ATOM   6387 C CA  . GLN A 1 793 ? 87.939 120.896 16.143  1.00 40.31 ? 793  GLN A CA  1 
ATOM   6388 C C   . GLN A 1 793 ? 87.944 122.327 16.678  1.00 39.55 ? 793  GLN A C   1 
ATOM   6389 O O   . GLN A 1 793 ? 87.608 123.293 15.946  1.00 38.77 ? 793  GLN A O   1 
ATOM   6390 C CB  . GLN A 1 793 ? 89.200 120.478 15.363  1.00 40.71 ? 793  GLN A CB  1 
ATOM   6391 C CG  . GLN A 1 793 ? 89.259 118.930 15.159  1.00 41.57 ? 793  GLN A CG  1 
ATOM   6392 C CD  . GLN A 1 793 ? 90.454 118.437 14.312  1.00 42.25 ? 793  GLN A CD  1 
ATOM   6393 O OE1 . GLN A 1 793 ? 91.013 119.204 13.515  1.00 44.57 ? 793  GLN A OE1 1 
ATOM   6394 N NE2 . GLN A 1 793 ? 90.848 117.148 14.491  1.00 41.92 ? 793  GLN A NE2 1 
ATOM   6395 N N   . ASN A 1 794 ? 88.219 122.427 17.984  1.00 39.04 ? 794  ASN A N   1 
ATOM   6396 C CA  . ASN A 1 794 ? 88.359 123.716 18.683  1.00 39.03 ? 794  ASN A CA  1 
ATOM   6397 C C   . ASN A 1 794 ? 87.066 124.559 18.876  1.00 38.17 ? 794  ASN A C   1 
ATOM   6398 O O   . ASN A 1 794 ? 87.141 125.726 19.271  1.00 38.41 ? 794  ASN A O   1 
ATOM   6399 C CB  . ASN A 1 794 ? 89.443 124.599 17.999  1.00 39.72 ? 794  ASN A CB  1 
ATOM   6400 C CG  . ASN A 1 794 ? 90.784 123.894 17.862  1.00 40.98 ? 794  ASN A CG  1 
ATOM   6401 O OD1 . ASN A 1 794 ? 91.480 123.664 18.842  1.00 44.02 ? 794  ASN A OD1 1 
ATOM   6402 N ND2 . ASN A 1 794 ? 91.154 123.565 16.638  1.00 41.61 ? 794  ASN A ND2 1 
ATOM   6403 N N   . ARG A 1 795 ? 85.893 124.003 18.601  1.00 36.75 ? 795  ARG A N   1 
ATOM   6404 C CA  . ARG A 1 795 ? 84.715 124.849 18.521  1.00 36.32 ? 795  ARG A CA  1 
ATOM   6405 C C   . ARG A 1 795 ? 83.387 124.118 18.763  1.00 35.03 ? 795  ARG A C   1 
ATOM   6406 O O   . ARG A 1 795 ? 83.132 123.073 18.166  1.00 34.90 ? 795  ARG A O   1 
ATOM   6407 C CB  . ARG A 1 795 ? 84.712 125.514 17.147  1.00 36.87 ? 795  ARG A CB  1 
ATOM   6408 C CG  . ARG A 1 795 ? 83.675 126.585 16.905  1.00 40.54 ? 795  ARG A CG  1 
ATOM   6409 C CD  . ARG A 1 795 ? 83.558 126.804 15.406  1.00 48.32 ? 795  ARG A CD  1 
ATOM   6410 N NE  . ARG A 1 795 ? 82.906 128.072 15.091  1.00 55.34 ? 795  ARG A NE  1 
ATOM   6411 C CZ  . ARG A 1 795 ? 83.547 129.162 14.666  1.00 58.20 ? 795  ARG A CZ  1 
ATOM   6412 N NH1 . ARG A 1 795 ? 84.870 129.143 14.494  1.00 59.47 ? 795  ARG A NH1 1 
ATOM   6413 N NH2 . ARG A 1 795 ? 82.862 130.273 14.404  1.00 58.00 ? 795  ARG A NH2 1 
ATOM   6414 N N   . LEU A 1 796 ? 82.552 124.677 19.639  1.00 33.68 ? 796  LEU A N   1 
ATOM   6415 C CA  . LEU A 1 796 ? 81.151 124.269 19.761  1.00 32.43 ? 796  LEU A CA  1 
ATOM   6416 C C   . LEU A 1 796 ? 80.234 125.432 19.365  1.00 32.66 ? 796  LEU A C   1 
ATOM   6417 O O   . LEU A 1 796 ? 80.385 126.543 19.878  1.00 31.80 ? 796  LEU A O   1 
ATOM   6418 C CB  . LEU A 1 796 ? 80.816 123.812 21.200  1.00 32.25 ? 796  LEU A CB  1 
ATOM   6419 C CG  . LEU A 1 796 ? 79.340 123.810 21.646  1.00 31.26 ? 796  LEU A CG  1 
ATOM   6420 C CD1 . LEU A 1 796 ? 78.527 122.648 21.040  1.00 25.96 ? 796  LEU A CD1 1 
ATOM   6421 C CD2 . LEU A 1 796 ? 79.209 123.849 23.161  1.00 31.37 ? 796  LEU A CD2 1 
ATOM   6422 N N   . GLU A 1 797 ? 79.270 125.150 18.487  1.00 32.40 ? 797  GLU A N   1 
ATOM   6423 C CA  . GLU A 1 797 ? 78.222 126.096 18.103  1.00 33.65 ? 797  GLU A CA  1 
ATOM   6424 C C   . GLU A 1 797 ? 76.880 125.659 18.651  1.00 32.67 ? 797  GLU A C   1 
ATOM   6425 O O   . GLU A 1 797 ? 76.457 124.517 18.441  1.00 32.23 ? 797  GLU A O   1 
ATOM   6426 C CB  . GLU A 1 797 ? 78.090 126.186 16.574  1.00 34.33 ? 797  GLU A CB  1 
ATOM   6427 C CG  . GLU A 1 797 ? 79.152 126.988 15.889  1.00 41.64 ? 797  GLU A CG  1 
ATOM   6428 C CD  . GLU A 1 797 ? 79.221 126.698 14.385  1.00 51.34 ? 797  GLU A CD  1 
ATOM   6429 O OE1 . GLU A 1 797 ? 78.212 126.933 13.650  1.00 53.94 ? 797  GLU A OE1 1 
ATOM   6430 O OE2 . GLU A 1 797 ? 80.305 126.240 13.934  1.00 55.17 ? 797  GLU A OE2 1 
ATOM   6431 N N   . VAL A 1 798 ? 76.212 126.574 19.345  1.00 32.22 ? 798  VAL A N   1 
ATOM   6432 C CA  . VAL A 1 798 ? 74.817 126.409 19.694  1.00 31.95 ? 798  VAL A CA  1 
ATOM   6433 C C   . VAL A 1 798 ? 74.027 127.340 18.767  1.00 32.74 ? 798  VAL A C   1 
ATOM   6434 O O   . VAL A 1 798 ? 74.253 128.548 18.736  1.00 32.48 ? 798  VAL A O   1 
ATOM   6435 C CB  . VAL A 1 798 ? 74.511 126.695 21.209  1.00 31.70 ? 798  VAL A CB  1 
ATOM   6436 C CG1 . VAL A 1 798 ? 73.033 126.434 21.514  1.00 31.52 ? 798  VAL A CG1 1 
ATOM   6437 C CG2 . VAL A 1 798 ? 75.383 125.857 22.132  1.00 30.91 ? 798  VAL A CG2 1 
ATOM   6438 N N   . ASN A 1 799 ? 73.062 126.753 18.067  1.00 33.11 ? 799  ASN A N   1 
ATOM   6439 C CA  . ASN A 1 799 ? 72.418 127.313 16.916  1.00 34.15 ? 799  ASN A CA  1 
ATOM   6440 C C   . ASN A 1 799 ? 70.910 127.127 17.090  1.00 34.01 ? 799  ASN A C   1 
ATOM   6441 O O   . ASN A 1 799 ? 70.474 126.058 17.502  1.00 34.19 ? 799  ASN A O   1 
ATOM   6442 C CB  . ASN A 1 799 ? 72.881 126.472 15.739  1.00 34.75 ? 799  ASN A CB  1 
ATOM   6443 C CG  . ASN A 1 799 ? 72.984 127.244 14.477  1.00 38.94 ? 799  ASN A CG  1 
ATOM   6444 O OD1 . ASN A 1 799 ? 72.037 127.947 14.078  1.00 43.99 ? 799  ASN A OD1 1 
ATOM   6445 N ND2 . ASN A 1 799 ? 74.136 127.111 13.794  1.00 42.83 ? 799  ASN A ND2 1 
ATOM   6446 N N   . ILE A 1 800 ? 70.108 128.142 16.791  1.00 33.64 ? 800  ILE A N   1 
ATOM   6447 C CA  . ILE A 1 800 ? 68.661 128.050 17.046  1.00 34.14 ? 800  ILE A CA  1 
ATOM   6448 C C   . ILE A 1 800 ? 67.895 127.991 15.740  1.00 34.30 ? 800  ILE A C   1 
ATOM   6449 O O   . ILE A 1 800 ? 68.013 128.912 14.944  1.00 33.77 ? 800  ILE A O   1 
ATOM   6450 C CB  . ILE A 1 800 ? 68.095 129.282 17.854  1.00 34.08 ? 800  ILE A CB  1 
ATOM   6451 C CG1 . ILE A 1 800 ? 68.897 129.589 19.123  1.00 34.58 ? 800  ILE A CG1 1 
ATOM   6452 C CG2 . ILE A 1 800 ? 66.588 129.092 18.144  1.00 34.39 ? 800  ILE A CG2 1 
ATOM   6453 C CD1 . ILE A 1 800 ? 69.082 128.431 20.094  1.00 35.75 ? 800  ILE A CD1 1 
ATOM   6454 N N   . SER A 1 801 ? 67.072 126.956 15.529  1.00 34.31 ? 801  SER A N   1 
ATOM   6455 C CA  . SER A 1 801 ? 66.316 126.889 14.285  1.00 34.84 ? 801  SER A CA  1 
ATOM   6456 C C   . SER A 1 801 ? 64.839 127.322 14.388  1.00 34.67 ? 801  SER A C   1 
ATOM   6457 O O   . SER A 1 801 ? 64.320 127.957 13.474  1.00 35.56 ? 801  SER A O   1 
ATOM   6458 C CB  . SER A 1 801 ? 66.471 125.533 13.597  1.00 34.72 ? 801  SER A CB  1 
ATOM   6459 O OG  . SER A 1 801 ? 65.676 124.560 14.235  1.00 37.41 ? 801  SER A OG  1 
ATOM   6460 N N   . GLN A 1 802 ? 64.163 126.943 15.467  1.00 33.44 ? 802  GLN A N   1 
ATOM   6461 C CA  . GLN A 1 802 ? 62.796 127.363 15.708  1.00 32.21 ? 802  GLN A CA  1 
ATOM   6462 C C   . GLN A 1 802 ? 62.870 127.966 17.079  1.00 31.55 ? 802  GLN A C   1 
ATOM   6463 O O   . GLN A 1 802 ? 63.523 127.413 17.952  1.00 31.60 ? 802  GLN A O   1 
ATOM   6464 C CB  . GLN A 1 802 ? 61.824 126.182 15.674  1.00 31.80 ? 802  GLN A CB  1 
ATOM   6465 C CG  . GLN A 1 802 ? 60.355 126.497 16.027  1.00 31.72 ? 802  GLN A CG  1 
ATOM   6466 C CD  . GLN A 1 802 ? 59.650 127.316 14.965  1.00 33.13 ? 802  GLN A CD  1 
ATOM   6467 O OE1 . GLN A 1 802 ? 58.837 128.201 15.278  1.00 34.68 ? 802  GLN A OE1 1 
ATOM   6468 N NE2 . GLN A 1 802 ? 59.952 127.038 13.706  1.00 32.17 ? 802  GLN A NE2 1 
ATOM   6469 N N   . SER A 1 803 ? 62.225 129.108 17.258  1.00 30.73 ? 803  SER A N   1 
ATOM   6470 C CA  . SER A 1 803 ? 62.355 129.846 18.497  1.00 30.98 ? 803  SER A CA  1 
ATOM   6471 C C   . SER A 1 803 ? 61.065 130.520 18.902  1.00 30.40 ? 803  SER A C   1 
ATOM   6472 O O   . SER A 1 803 ? 61.001 131.749 19.005  1.00 31.35 ? 803  SER A O   1 
ATOM   6473 C CB  . SER A 1 803 ? 63.426 130.925 18.364  1.00 31.01 ? 803  SER A CB  1 
ATOM   6474 O OG  . SER A 1 803 ? 63.548 131.542 19.627  1.00 32.24 ? 803  SER A OG  1 
ATOM   6475 N N   . THR A 1 804 ? 60.028 129.748 19.137  1.00 29.42 ? 804  THR A N   1 
ATOM   6476 C CA  . THR A 1 804 ? 58.772 130.374 19.508  1.00 28.14 ? 804  THR A CA  1 
ATOM   6477 C C   . THR A 1 804 ? 58.291 129.945 20.878  1.00 27.36 ? 804  THR A C   1 
ATOM   6478 O O   . THR A 1 804 ? 57.122 130.023 21.151  1.00 27.95 ? 804  THR A O   1 
ATOM   6479 C CB  . THR A 1 804 ? 57.695 130.202 18.439  1.00 28.58 ? 804  THR A CB  1 
ATOM   6480 O OG1 . THR A 1 804 ? 57.614 128.820 18.056  1.00 30.02 ? 804  THR A OG1 1 
ATOM   6481 C CG2 . THR A 1 804 ? 58.006 131.081 17.215  1.00 28.04 ? 804  THR A CG2 1 
ATOM   6482 N N   . TYR A 1 805 ? 59.207 129.507 21.730  1.00 26.20 ? 805  TYR A N   1 
ATOM   6483 C CA  . TYR A 1 805 ? 58.920 129.229 23.120  1.00 26.19 ? 805  TYR A CA  1 
ATOM   6484 C C   . TYR A 1 805 ? 60.120 129.607 23.946  1.00 27.14 ? 805  TYR A C   1 
ATOM   6485 O O   . TYR A 1 805 ? 61.211 129.109 23.723  1.00 26.78 ? 805  TYR A O   1 
ATOM   6486 C CB  . TYR A 1 805 ? 58.586 127.740 23.384  1.00 25.68 ? 805  TYR A CB  1 
ATOM   6487 C CG  . TYR A 1 805 ? 58.238 127.471 24.830  1.00 24.66 ? 805  TYR A CG  1 
ATOM   6488 C CD1 . TYR A 1 805 ? 57.053 127.981 25.381  1.00 23.82 ? 805  TYR A CD1 1 
ATOM   6489 C CD2 . TYR A 1 805 ? 59.106 126.759 25.665  1.00 25.13 ? 805  TYR A CD2 1 
ATOM   6490 C CE1 . TYR A 1 805 ? 56.738 127.780 26.725  1.00 25.21 ? 805  TYR A CE1 1 
ATOM   6491 C CE2 . TYR A 1 805 ? 58.795 126.545 27.019  1.00 26.00 ? 805  TYR A CE2 1 
ATOM   6492 C CZ  . TYR A 1 805 ? 57.599 127.057 27.530  1.00 23.97 ? 805  TYR A CZ  1 
ATOM   6493 O OH  . TYR A 1 805 ? 57.244 126.860 28.844  1.00 26.31 ? 805  TYR A OH  1 
ATOM   6494 N N   . LYS A 1 806 ? 59.910 130.495 24.909  1.00 28.28 ? 806  LYS A N   1 
ATOM   6495 C CA  . LYS A 1 806 ? 60.951 130.826 25.860  1.00 29.81 ? 806  LYS A CA  1 
ATOM   6496 C C   . LYS A 1 806 ? 60.463 130.363 27.217  1.00 29.52 ? 806  LYS A C   1 
ATOM   6497 O O   . LYS A 1 806 ? 59.472 130.897 27.727  1.00 30.10 ? 806  LYS A O   1 
ATOM   6498 C CB  . LYS A 1 806 ? 61.242 132.337 25.845  1.00 31.08 ? 806  LYS A CB  1 
ATOM   6499 C CG  . LYS A 1 806 ? 62.361 132.744 26.828  1.00 33.06 ? 806  LYS A CG  1 
ATOM   6500 C CD  . LYS A 1 806 ? 63.622 133.262 26.150  1.00 37.15 ? 806  LYS A CD  1 
ATOM   6501 C CE  . LYS A 1 806 ? 64.554 133.915 27.206  1.00 37.40 ? 806  LYS A CE  1 
ATOM   6502 N NZ  . LYS A 1 806 ? 65.985 134.030 26.755  1.00 40.79 ? 806  LYS A NZ  1 
ATOM   6503 N N   . ASP A 1 807 ? 61.126 129.350 27.779  1.00 29.08 ? 807  ASP A N   1 
ATOM   6504 C CA  . ASP A 1 807 ? 60.758 128.780 29.074  1.00 29.48 ? 807  ASP A CA  1 
ATOM   6505 C C   . ASP A 1 807 ? 60.889 129.885 30.150  1.00 30.26 ? 807  ASP A C   1 
ATOM   6506 O O   . ASP A 1 807 ? 61.927 130.515 30.234  1.00 30.04 ? 807  ASP A O   1 
ATOM   6507 C CB  . ASP A 1 807 ? 61.644 127.550 29.394  1.00 29.29 ? 807  ASP A CB  1 
ATOM   6508 C CG  . ASP A 1 807 ? 61.179 126.789 30.637  1.00 30.01 ? 807  ASP A CG  1 
ATOM   6509 O OD1 . ASP A 1 807 ? 61.200 127.384 31.730  1.00 35.63 ? 807  ASP A OD1 1 
ATOM   6510 O OD2 . ASP A 1 807 ? 60.777 125.610 30.549  1.00 27.02 ? 807  ASP A OD2 1 
ATOM   6511 N N   . PRO A 1 808 ? 59.815 130.154 30.935  1.00 30.81 ? 808  PRO A N   1 
ATOM   6512 C CA  . PRO A 1 808 ? 59.838 131.245 31.943  1.00 30.71 ? 808  PRO A CA  1 
ATOM   6513 C C   . PRO A 1 808 ? 60.776 131.019 33.124  1.00 30.57 ? 808  PRO A C   1 
ATOM   6514 O O   . PRO A 1 808 ? 61.048 131.956 33.890  1.00 30.58 ? 808  PRO A O   1 
ATOM   6515 C CB  . PRO A 1 808 ? 58.381 131.296 32.440  1.00 31.39 ? 808  PRO A CB  1 
ATOM   6516 C CG  . PRO A 1 808 ? 57.838 129.924 32.167  1.00 30.90 ? 808  PRO A CG  1 
ATOM   6517 C CD  . PRO A 1 808 ? 58.490 129.505 30.869  1.00 30.67 ? 808  PRO A CD  1 
ATOM   6518 N N   . ASN A 1 809 ? 61.273 129.793 33.266  1.00 30.30 ? 809  ASN A N   1 
ATOM   6519 C CA  . ASN A 1 809 ? 62.129 129.431 34.391  1.00 30.56 ? 809  ASN A CA  1 
ATOM   6520 C C   . ASN A 1 809 ? 63.596 129.788 34.211  1.00 30.80 ? 809  ASN A C   1 
ATOM   6521 O O   . ASN A 1 809 ? 64.415 129.337 34.996  1.00 31.91 ? 809  ASN A O   1 
ATOM   6522 C CB  . ASN A 1 809 ? 61.992 127.945 34.756  1.00 29.65 ? 809  ASN A CB  1 
ATOM   6523 C CG  . ASN A 1 809 ? 60.600 127.592 35.259  1.00 31.26 ? 809  ASN A CG  1 
ATOM   6524 O OD1 . ASN A 1 809 ? 59.989 126.622 34.804  1.00 31.26 ? 809  ASN A OD1 1 
ATOM   6525 N ND2 . ASN A 1 809 ? 60.088 128.383 36.196  1.00 29.96 ? 809  ASN A ND2 1 
ATOM   6526 N N   . ASN A 1 810 ? 63.943 130.578 33.199  1.00 31.03 ? 810  ASN A N   1 
ATOM   6527 C CA  . ASN A 1 810 ? 65.338 131.076 33.084  1.00 31.98 ? 810  ASN A CA  1 
ATOM   6528 C C   . ASN A 1 810 ? 66.374 129.930 33.036  1.00 30.88 ? 810  ASN A C   1 
ATOM   6529 O O   . ASN A 1 810 ? 67.310 129.886 33.852  1.00 31.40 ? 810  ASN A O   1 
ATOM   6530 C CB  . ASN A 1 810 ? 65.647 132.043 34.267  1.00 33.08 ? 810  ASN A CB  1 
ATOM   6531 C CG  . ASN A 1 810 ? 66.861 132.965 34.013  1.00 35.84 ? 810  ASN A CG  1 
ATOM   6532 O OD1 . ASN A 1 810 ? 67.047 133.527 32.914  1.00 38.56 ? 810  ASN A OD1 1 
ATOM   6533 N ND2 . ASN A 1 810 ? 67.686 133.127 35.049  1.00 40.81 ? 810  ASN A ND2 1 
ATOM   6534 N N   . LEU A 1 811 ? 66.189 128.990 32.103  1.00 29.24 ? 811  LEU A N   1 
ATOM   6535 C CA  . LEU A 1 811 ? 67.043 127.794 32.039  1.00 27.83 ? 811  LEU A CA  1 
ATOM   6536 C C   . LEU A 1 811 ? 68.370 128.059 31.306  1.00 26.58 ? 811  LEU A C   1 
ATOM   6537 O O   . LEU A 1 811 ? 68.419 128.893 30.396  1.00 25.77 ? 811  LEU A O   1 
ATOM   6538 C CB  . LEU A 1 811 ? 66.305 126.639 31.354  1.00 27.54 ? 811  LEU A CB  1 
ATOM   6539 C CG  . LEU A 1 811 ? 64.968 126.158 31.948  1.00 28.53 ? 811  LEU A CG  1 
ATOM   6540 C CD1 . LEU A 1 811 ? 64.503 124.916 31.215  1.00 27.70 ? 811  LEU A CD1 1 
ATOM   6541 C CD2 . LEU A 1 811 ? 65.103 125.890 33.431  1.00 26.35 ? 811  LEU A CD2 1 
ATOM   6542 N N   . ALA A 1 812 ? 69.415 127.308 31.669  1.00 25.06 ? 812  ALA A N   1 
ATOM   6543 C CA  . ALA A 1 812 ? 70.723 127.511 31.072  1.00 25.21 ? 812  ALA A CA  1 
ATOM   6544 C C   . ALA A 1 812 ? 71.598 126.274 31.162  1.00 24.39 ? 812  ALA A C   1 
ATOM   6545 O O   . ALA A 1 812 ? 71.506 125.512 32.116  1.00 23.74 ? 812  ALA A O   1 
ATOM   6546 C CB  . ALA A 1 812 ? 71.433 128.707 31.765  1.00 24.97 ? 812  ALA A CB  1 
ATOM   6547 N N   . PHE A 1 813 ? 72.454 126.082 30.167  1.00 24.68 ? 813  PHE A N   1 
ATOM   6548 C CA  . PHE A 1 813 ? 73.488 125.072 30.252  1.00 25.35 ? 813  PHE A CA  1 
ATOM   6549 C C   . PHE A 1 813 ? 74.583 125.572 31.215  1.00 26.29 ? 813  PHE A C   1 
ATOM   6550 O O   . PHE A 1 813 ? 75.107 126.658 31.028  1.00 27.06 ? 813  PHE A O   1 
ATOM   6551 C CB  . PHE A 1 813 ? 74.070 124.748 28.873  1.00 24.78 ? 813  PHE A CB  1 
ATOM   6552 C CG  . PHE A 1 813 ? 73.055 124.235 27.879  1.00 25.88 ? 813  PHE A CG  1 
ATOM   6553 C CD1 . PHE A 1 813 ? 72.768 122.871 27.787  1.00 25.06 ? 813  PHE A CD1 1 
ATOM   6554 C CD2 . PHE A 1 813 ? 72.373 125.118 27.037  1.00 26.55 ? 813  PHE A CD2 1 
ATOM   6555 C CE1 . PHE A 1 813 ? 71.810 122.410 26.877  1.00 24.35 ? 813  PHE A CE1 1 
ATOM   6556 C CE2 . PHE A 1 813 ? 71.432 124.651 26.120  1.00 26.49 ? 813  PHE A CE2 1 
ATOM   6557 C CZ  . PHE A 1 813 ? 71.147 123.285 26.049  1.00 23.46 ? 813  PHE A CZ  1 
ATOM   6558 N N   . ASN A 1 814 ? 74.900 124.794 32.248  1.00 27.31 ? 814  ASN A N   1 
ATOM   6559 C CA  . ASN A 1 814 ? 75.921 125.167 33.238  1.00 28.56 ? 814  ASN A CA  1 
ATOM   6560 C C   . ASN A 1 814 ? 77.083 124.190 33.283  1.00 28.67 ? 814  ASN A C   1 
ATOM   6561 O O   . ASN A 1 814 ? 78.014 124.393 34.050  1.00 28.76 ? 814  ASN A O   1 
ATOM   6562 C CB  . ASN A 1 814 ? 75.322 125.403 34.656  1.00 29.05 ? 814  ASN A CB  1 
ATOM   6563 C CG  . ASN A 1 814 ? 74.977 124.095 35.401  1.00 33.46 ? 814  ASN A CG  1 
ATOM   6564 O OD1 . ASN A 1 814 ? 74.829 123.018 34.793  1.00 37.08 ? 814  ASN A OD1 1 
ATOM   6565 N ND2 . ASN A 1 814 ? 74.846 124.186 36.734  1.00 34.11 ? 814  ASN A ND2 1 
ATOM   6566 N N   . GLU A 1 815 ? 77.039 123.142 32.443  1.00 28.64 ? 815  GLU A N   1 
ATOM   6567 C CA  . GLU A 1 815 ? 78.113 122.130 32.400  1.00 28.68 ? 815  GLU A CA  1 
ATOM   6568 C C   . GLU A 1 815 ? 78.153 121.465 31.039  1.00 27.35 ? 815  GLU A C   1 
ATOM   6569 O O   . GLU A 1 815 ? 77.117 121.169 30.458  1.00 26.40 ? 815  GLU A O   1 
ATOM   6570 C CB  . GLU A 1 815 ? 77.948 121.049 33.483  1.00 28.79 ? 815  GLU A CB  1 
ATOM   6571 C CG  . GLU A 1 815 ? 79.161 120.117 33.540  1.00 31.59 ? 815  GLU A CG  1 
ATOM   6572 C CD  . GLU A 1 815 ? 79.054 118.909 34.486  1.00 33.56 ? 815  GLU A CD  1 
ATOM   6573 O OE1 . GLU A 1 815 ? 79.255 119.050 35.728  1.00 39.57 ? 815  GLU A OE1 1 
ATOM   6574 O OE2 . GLU A 1 815 ? 78.876 117.773 33.955  1.00 42.47 ? 815  GLU A OE2 1 
ATOM   6575 N N   . ILE A 1 816 ? 79.362 121.207 30.553  1.00 26.50 ? 816  ILE A N   1 
ATOM   6576 C CA  . ILE A 1 816 ? 79.603 120.507 29.286  1.00 25.47 ? 816  ILE A CA  1 
ATOM   6577 C C   . ILE A 1 816 ? 80.680 119.449 29.537  1.00 25.40 ? 816  ILE A C   1 
ATOM   6578 O O   . ILE A 1 816 ? 81.798 119.762 29.971  1.00 24.45 ? 816  ILE A O   1 
ATOM   6579 C CB  . ILE A 1 816 ? 80.066 121.493 28.192  1.00 25.50 ? 816  ILE A CB  1 
ATOM   6580 C CG1 . ILE A 1 816 ? 79.008 122.569 27.953  1.00 25.11 ? 816  ILE A CG1 1 
ATOM   6581 C CG2 . ILE A 1 816 ? 80.377 120.778 26.872  1.00 24.25 ? 816  ILE A CG2 1 
ATOM   6582 C CD1 . ILE A 1 816 ? 79.481 123.711 27.073  1.00 24.70 ? 816  ILE A CD1 1 
ATOM   6583 N N   . LYS A 1 817 ? 80.351 118.191 29.283  1.00 24.20 ? 817  LYS A N   1 
ATOM   6584 C CA  . LYS A 1 817 ? 81.339 117.120 29.414  1.00 24.17 ? 817  LYS A CA  1 
ATOM   6585 C C   . LYS A 1 817 ? 81.774 116.702 28.002  1.00 24.31 ? 817  LYS A C   1 
ATOM   6586 O O   . LYS A 1 817 ? 80.927 116.425 27.154  1.00 24.31 ? 817  LYS A O   1 
ATOM   6587 C CB  . LYS A 1 817 ? 80.722 115.951 30.174  1.00 23.34 ? 817  LYS A CB  1 
ATOM   6588 C CG  . LYS A 1 817 ? 81.619 114.754 30.408  1.00 22.39 ? 817  LYS A CG  1 
ATOM   6589 C CD  . LYS A 1 817 ? 80.804 113.772 31.229  1.00 27.31 ? 817  LYS A CD  1 
ATOM   6590 C CE  . LYS A 1 817 ? 81.585 112.627 31.794  1.00 32.97 ? 817  LYS A CE  1 
ATOM   6591 N NZ  . LYS A 1 817 ? 80.614 111.768 32.551  1.00 35.97 ? 817  LYS A NZ  1 
ATOM   6592 N N   . ILE A 1 818 ? 83.081 116.699 27.743  1.00 23.71 ? 818  ILE A N   1 
ATOM   6593 C CA  . ILE A 1 818 ? 83.575 116.332 26.431  1.00 23.12 ? 818  ILE A CA  1 
ATOM   6594 C C   . ILE A 1 818 ? 84.346 115.027 26.553  1.00 23.28 ? 818  ILE A C   1 
ATOM   6595 O O   . ILE A 1 818 ? 85.332 114.927 27.296  1.00 22.62 ? 818  ILE A O   1 
ATOM   6596 C CB  . ILE A 1 818 ? 84.409 117.451 25.744  1.00 24.04 ? 818  ILE A CB  1 
ATOM   6597 C CG1 . ILE A 1 818 ? 83.719 118.816 25.847  1.00 21.54 ? 818  ILE A CG1 1 
ATOM   6598 C CG2 . ILE A 1 818 ? 84.671 117.088 24.268  1.00 23.52 ? 818  ILE A CG2 1 
ATOM   6599 C CD1 . ILE A 1 818 ? 84.590 119.991 25.336  1.00 23.07 ? 818  ILE A CD1 1 
ATOM   6600 N N   . LEU A 1 819 ? 83.860 114.003 25.851  1.00 23.12 ? 819  LEU A N   1 
ATOM   6601 C CA  . LEU A 1 819 ? 84.541 112.710 25.840  1.00 23.55 ? 819  LEU A CA  1 
ATOM   6602 C C   . LEU A 1 819 ? 85.434 112.548 24.614  1.00 24.11 ? 819  LEU A C   1 
ATOM   6603 O O   . LEU A 1 819 ? 85.084 113.017 23.535  1.00 24.64 ? 819  LEU A O   1 
ATOM   6604 C CB  . LEU A 1 819 ? 83.523 111.587 25.893  1.00 22.92 ? 819  LEU A CB  1 
ATOM   6605 C CG  . LEU A 1 819 ? 82.384 111.818 26.903  1.00 24.42 ? 819  LEU A CG  1 
ATOM   6606 C CD1 . LEU A 1 819 ? 81.376 110.680 26.854  1.00 19.14 ? 819  LEU A CD1 1 
ATOM   6607 C CD2 . LEU A 1 819 ? 82.989 111.917 28.299  1.00 21.44 ? 819  LEU A CD2 1 
ATOM   6608 N N   . GLY A 1 820 ? 86.564 111.861 24.778  1.00 24.83 ? 820  GLY A N   1 
ATOM   6609 C CA  . GLY A 1 820 ? 87.475 111.548 23.661  1.00 25.79 ? 820  GLY A CA  1 
ATOM   6610 C C   . GLY A 1 820 ? 88.219 112.759 23.155  1.00 26.68 ? 820  GLY A C   1 
ATOM   6611 O O   . GLY A 1 820 ? 88.405 112.931 21.948  1.00 26.90 ? 820  GLY A O   1 
ATOM   6612 N N   . THR A 1 821 ? 88.628 113.620 24.080  1.00 26.76 ? 821  THR A N   1 
ATOM   6613 C CA  . THR A 1 821 ? 89.208 114.914 23.723  1.00 27.92 ? 821  THR A CA  1 
ATOM   6614 C C   . THR A 1 821 ? 90.605 115.037 24.314  1.00 28.49 ? 821  THR A C   1 
ATOM   6615 O O   . THR A 1 821 ? 90.921 114.442 25.349  1.00 27.48 ? 821  THR A O   1 
ATOM   6616 C CB  . THR A 1 821 ? 88.297 116.088 24.218  1.00 28.53 ? 821  THR A CB  1 
ATOM   6617 O OG1 . THR A 1 821 ? 88.724 117.341 23.653  1.00 29.13 ? 821  THR A OG1 1 
ATOM   6618 C CG2 . THR A 1 821 ? 88.255 116.162 25.761  1.00 26.95 ? 821  THR A CG2 1 
ATOM   6619 N N   . GLU A 1 822 ? 91.450 115.767 23.604  1.00 29.91 ? 822  GLU A N   1 
ATOM   6620 C CA  . GLU A 1 822 ? 92.699 116.249 24.140  1.00 31.02 ? 822  GLU A CA  1 
ATOM   6621 C C   . GLU A 1 822 ? 92.370 117.435 25.058  1.00 31.59 ? 822  GLU A C   1 
ATOM   6622 O O   . GLU A 1 822 ? 91.274 118.015 24.968  1.00 31.11 ? 822  GLU A O   1 
ATOM   6623 C CB  . GLU A 1 822 ? 93.634 116.669 22.981  1.00 31.89 ? 822  GLU A CB  1 
ATOM   6624 C CG  . GLU A 1 822 ? 94.203 115.484 22.158  1.00 33.65 ? 822  GLU A CG  1 
ATOM   6625 C CD  . GLU A 1 822 ? 94.846 114.405 23.036  1.00 38.07 ? 822  GLU A CD  1 
ATOM   6626 O OE1 . GLU A 1 822 ? 95.561 114.767 23.986  1.00 41.45 ? 822  GLU A OE1 1 
ATOM   6627 O OE2 . GLU A 1 822 ? 94.631 113.191 22.801  1.00 41.86 ? 822  GLU A OE2 1 
ATOM   6628 N N   . GLU A 1 823 ? 93.299 117.802 25.942  1.00 32.47 ? 823  GLU A N   1 
ATOM   6629 C CA  . GLU A 1 823 ? 93.039 118.878 26.901  1.00 33.63 ? 823  GLU A CA  1 
ATOM   6630 C C   . GLU A 1 823 ? 92.625 120.194 26.242  1.00 34.10 ? 823  GLU A C   1 
ATOM   6631 O O   . GLU A 1 823 ? 93.418 120.785 25.506  1.00 34.40 ? 823  GLU A O   1 
ATOM   6632 C CB  . GLU A 1 823 ? 94.261 119.103 27.805  1.00 33.69 ? 823  GLU A CB  1 
ATOM   6633 C CG  . GLU A 1 823 ? 94.068 120.284 28.733  1.00 34.59 ? 823  GLU A CG  1 
ATOM   6634 C CD  . GLU A 1 823 ? 94.918 120.229 29.976  1.00 37.12 ? 823  GLU A CD  1 
ATOM   6635 O OE1 . GLU A 1 823 ? 96.101 119.786 29.899  1.00 36.33 ? 823  GLU A OE1 1 
ATOM   6636 O OE2 . GLU A 1 823 ? 94.379 120.652 31.031  1.00 38.10 ? 823  GLU A OE2 1 
ATOM   6637 N N   . PRO A 1 824 ? 91.381 120.653 26.477  1.00 34.56 ? 824  PRO A N   1 
ATOM   6638 C CA  . PRO A 1 824 ? 91.002 121.964 25.946  1.00 34.95 ? 824  PRO A CA  1 
ATOM   6639 C C   . PRO A 1 824 ? 91.511 123.066 26.867  1.00 36.06 ? 824  PRO A C   1 
ATOM   6640 O O   . PRO A 1 824 ? 91.413 122.948 28.096  1.00 35.35 ? 824  PRO A O   1 
ATOM   6641 C CB  . PRO A 1 824 ? 89.473 121.945 25.976  1.00 35.17 ? 824  PRO A CB  1 
ATOM   6642 C CG  . PRO A 1 824 ? 89.071 120.693 26.649  1.00 34.57 ? 824  PRO A CG  1 
ATOM   6643 C CD  . PRO A 1 824 ? 90.280 120.016 27.212  1.00 34.15 ? 824  PRO A CD  1 
ATOM   6644 N N   . SER A 1 825 ? 92.090 124.114 26.293  1.00 37.07 ? 825  SER A N   1 
ATOM   6645 C CA  . SER A 1 825 ? 92.544 125.245 27.115  1.00 38.90 ? 825  SER A CA  1 
ATOM   6646 C C   . SER A 1 825 ? 92.100 126.584 26.574  1.00 39.41 ? 825  SER A C   1 
ATOM   6647 O O   . SER A 1 825 ? 91.694 126.696 25.403  1.00 39.52 ? 825  SER A O   1 
ATOM   6648 C CB  . SER A 1 825 ? 94.047 125.206 27.376  1.00 38.76 ? 825  SER A CB  1 
ATOM   6649 O OG  . SER A 1 825 ? 94.720 124.535 26.346  1.00 42.16 ? 825  SER A OG  1 
ATOM   6650 N N   . ASN A 1 826 ? 92.142 127.587 27.451  1.00 40.11 ? 826  ASN A N   1 
ATOM   6651 C CA  . ASN A 1 826 ? 91.707 128.945 27.138  1.00 41.18 ? 826  ASN A CA  1 
ATOM   6652 C C   . ASN A 1 826 ? 90.313 128.957 26.546  1.00 40.88 ? 826  ASN A C   1 
ATOM   6653 O O   . ASN A 1 826 ? 90.108 129.450 25.434  1.00 41.65 ? 826  ASN A O   1 
ATOM   6654 C CB  . ASN A 1 826 ? 92.699 129.648 26.192  1.00 42.07 ? 826  ASN A CB  1 
ATOM   6655 C CG  . ASN A 1 826 ? 94.144 129.555 26.674  1.00 44.90 ? 826  ASN A CG  1 
ATOM   6656 O OD1 . ASN A 1 826 ? 94.410 129.541 27.885  1.00 47.59 ? 826  ASN A OD1 1 
ATOM   6657 N ND2 . ASN A 1 826 ? 95.092 129.483 25.724  1.00 48.23 ? 826  ASN A ND2 1 
ATOM   6658 N N   . VAL A 1 827 ? 89.354 128.408 27.291  1.00 40.26 ? 827  VAL A N   1 
ATOM   6659 C CA  . VAL A 1 827 ? 87.976 128.291 26.805  1.00 39.07 ? 827  VAL A CA  1 
ATOM   6660 C C   . VAL A 1 827 ? 87.304 129.661 26.790  1.00 38.92 ? 827  VAL A C   1 
ATOM   6661 O O   . VAL A 1 827 ? 87.350 130.408 27.755  1.00 38.74 ? 827  VAL A O   1 
ATOM   6662 C CB  . VAL A 1 827 ? 87.167 127.196 27.578  1.00 38.74 ? 827  VAL A CB  1 
ATOM   6663 C CG1 . VAL A 1 827 ? 85.681 127.262 27.286  1.00 37.76 ? 827  VAL A CG1 1 
ATOM   6664 C CG2 . VAL A 1 827 ? 87.694 125.846 27.213  1.00 38.92 ? 827  VAL A CG2 1 
ATOM   6665 N N   . THR A 1 828 ? 86.691 129.964 25.662  1.00 38.41 ? 828  THR A N   1 
ATOM   6666 C CA  . THR A 1 828 ? 86.103 131.256 25.390  1.00 38.98 ? 828  THR A CA  1 
ATOM   6667 C C   . THR A 1 828 ? 84.648 131.006 25.036  1.00 38.34 ? 828  THR A C   1 
ATOM   6668 O O   . THR A 1 828 ? 84.338 129.999 24.421  1.00 37.77 ? 828  THR A O   1 
ATOM   6669 C CB  . THR A 1 828 ? 86.846 131.902 24.194  1.00 38.86 ? 828  THR A CB  1 
ATOM   6670 O OG1 . THR A 1 828 ? 88.097 132.432 24.661  1.00 41.94 ? 828  THR A OG1 1 
ATOM   6671 C CG2 . THR A 1 828 ? 86.048 133.016 23.565  1.00 40.05 ? 828  THR A CG2 1 
ATOM   6672 N N   . VAL A 1 829 ? 83.769 131.919 25.433  1.00 38.84 ? 829  VAL A N   1 
ATOM   6673 C CA  . VAL A 1 829 ? 82.343 131.826 25.130  1.00 39.32 ? 829  VAL A CA  1 
ATOM   6674 C C   . VAL A 1 829 ? 81.890 133.130 24.480  1.00 40.92 ? 829  VAL A C   1 
ATOM   6675 O O   . VAL A 1 829 ? 82.040 134.202 25.065  1.00 41.13 ? 829  VAL A O   1 
ATOM   6676 C CB  . VAL A 1 829 ? 81.497 131.558 26.411  1.00 38.97 ? 829  VAL A CB  1 
ATOM   6677 C CG1 . VAL A 1 829 ? 79.977 131.583 26.100  1.00 38.81 ? 829  VAL A CG1 1 
ATOM   6678 C CG2 . VAL A 1 829 ? 81.909 130.253 27.073  1.00 36.86 ? 829  VAL A CG2 1 
ATOM   6679 N N   . LYS A 1 830 ? 81.342 133.040 23.276  1.00 41.99 ? 830  LYS A N   1 
ATOM   6680 C CA  . LYS A 1 830 ? 80.817 134.207 22.597  1.00 44.35 ? 830  LYS A CA  1 
ATOM   6681 C C   . LYS A 1 830 ? 79.316 134.069 22.426  1.00 44.97 ? 830  LYS A C   1 
ATOM   6682 O O   . LYS A 1 830 ? 78.827 132.994 22.123  1.00 44.48 ? 830  LYS A O   1 
ATOM   6683 C CB  . LYS A 1 830 ? 81.497 134.392 21.234  1.00 44.52 ? 830  LYS A CB  1 
ATOM   6684 C CG  . LYS A 1 830 ? 82.947 134.870 21.290  1.00 45.78 ? 830  LYS A CG  1 
ATOM   6685 C CD  . LYS A 1 830 ? 83.599 134.788 19.888  1.00 46.06 ? 830  LYS A CD  1 
ATOM   6686 C CE  . LYS A 1 830 ? 85.086 135.221 19.900  1.00 48.61 ? 830  LYS A CE  1 
ATOM   6687 N NZ  . LYS A 1 830 ? 85.769 135.016 18.556  1.00 48.57 ? 830  LYS A NZ  1 
ATOM   6688 N N   . HIS A 1 831 ? 78.595 135.165 22.627  1.00 46.73 ? 831  HIS A N   1 
ATOM   6689 C CA  . HIS A 1 831 ? 77.142 135.186 22.523  1.00 48.82 ? 831  HIS A CA  1 
ATOM   6690 C C   . HIS A 1 831 ? 76.685 136.132 21.395  1.00 50.49 ? 831  HIS A C   1 
ATOM   6691 O O   . HIS A 1 831 ? 76.790 137.361 21.515  1.00 50.47 ? 831  HIS A O   1 
ATOM   6692 C CB  . HIS A 1 831 ? 76.526 135.571 23.881  1.00 48.45 ? 831  HIS A CB  1 
ATOM   6693 C CG  . HIS A 1 831 ? 75.038 135.748 23.858  1.00 48.63 ? 831  HIS A CG  1 
ATOM   6694 N ND1 . HIS A 1 831 ? 74.382 136.616 24.704  1.00 49.73 ? 831  HIS A ND1 1 
ATOM   6695 C CD2 . HIS A 1 831 ? 74.074 135.164 23.103  1.00 48.92 ? 831  HIS A CD2 1 
ATOM   6696 C CE1 . HIS A 1 831 ? 73.080 136.564 24.470  1.00 49.05 ? 831  HIS A CE1 1 
ATOM   6697 N NE2 . HIS A 1 831 ? 72.868 135.690 23.503  1.00 48.38 ? 831  HIS A NE2 1 
ATOM   6698 N N   . ASN A 1 832 ? 76.164 135.549 20.312  1.00 52.54 ? 832  ASN A N   1 
ATOM   6699 C CA  . ASN A 1 832 ? 75.894 136.290 19.073  1.00 54.71 ? 832  ASN A CA  1 
ATOM   6700 C C   . ASN A 1 832 ? 77.064 137.179 18.656  1.00 55.57 ? 832  ASN A C   1 
ATOM   6701 O O   . ASN A 1 832 ? 76.879 138.346 18.297  1.00 56.13 ? 832  ASN A O   1 
ATOM   6702 C CB  . ASN A 1 832 ? 74.604 137.104 19.189  1.00 55.10 ? 832  ASN A CB  1 
ATOM   6703 C CG  . ASN A 1 832 ? 73.373 136.249 19.036  1.00 57.24 ? 832  ASN A CG  1 
ATOM   6704 O OD1 . ASN A 1 832 ? 73.181 135.579 18.005  1.00 59.79 ? 832  ASN A OD1 1 
ATOM   6705 N ND2 . ASN A 1 832 ? 72.522 136.258 20.062  1.00 58.57 ? 832  ASN A ND2 1 
ATOM   6706 N N   . GLY A 1 833 ? 78.269 136.619 18.735  1.00 56.49 ? 833  GLY A N   1 
ATOM   6707 C CA  . GLY A 1 833 ? 79.466 137.318 18.318  1.00 57.82 ? 833  GLY A CA  1 
ATOM   6708 C C   . GLY A 1 833 ? 80.265 137.913 19.453  1.00 58.89 ? 833  GLY A C   1 
ATOM   6709 O O   . GLY A 1 833 ? 81.487 137.824 19.449  1.00 59.30 ? 833  GLY A O   1 
ATOM   6710 N N   . VAL A 1 834 ? 79.579 138.524 20.419  1.00 60.10 ? 834  VAL A N   1 
ATOM   6711 C CA  . VAL A 1 834 ? 80.228 139.262 21.517  1.00 60.94 ? 834  VAL A CA  1 
ATOM   6712 C C   . VAL A 1 834 ? 80.922 138.305 22.501  1.00 61.55 ? 834  VAL A C   1 
ATOM   6713 O O   . VAL A 1 834 ? 80.270 137.416 23.047  1.00 61.39 ? 834  VAL A O   1 
ATOM   6714 C CB  . VAL A 1 834 ? 79.218 140.148 22.326  1.00 60.87 ? 834  VAL A CB  1 
ATOM   6715 C CG1 . VAL A 1 834 ? 79.957 141.151 23.207  1.00 60.95 ? 834  VAL A CG1 1 
ATOM   6716 C CG2 . VAL A 1 834 ? 78.236 140.879 21.409  1.00 61.34 ? 834  VAL A CG2 1 
ATOM   6717 N N   . PRO A 1 835 ? 82.247 138.480 22.724  1.00 62.26 ? 835  PRO A N   1 
ATOM   6718 C CA  . PRO A 1 835 ? 82.970 137.737 23.766  1.00 62.66 ? 835  PRO A CA  1 
ATOM   6719 C C   . PRO A 1 835 ? 82.383 137.897 25.166  1.00 63.24 ? 835  PRO A C   1 
ATOM   6720 O O   . PRO A 1 835 ? 81.534 138.758 25.398  1.00 63.47 ? 835  PRO A O   1 
ATOM   6721 C CB  . PRO A 1 835 ? 84.375 138.339 23.713  1.00 62.48 ? 835  PRO A CB  1 
ATOM   6722 C CG  . PRO A 1 835 ? 84.523 138.800 22.299  1.00 62.88 ? 835  PRO A CG  1 
ATOM   6723 C CD  . PRO A 1 835 ? 83.159 139.348 21.953  1.00 62.60 ? 835  PRO A CD  1 
ATOM   6724 N N   . SER A 1 836 ? 82.861 137.062 26.086  1.00 63.89 ? 836  SER A N   1 
ATOM   6725 C CA  . SER A 1 836 ? 82.428 137.027 27.489  1.00 64.21 ? 836  SER A CA  1 
ATOM   6726 C C   . SER A 1 836 ? 80.961 136.663 27.616  1.00 64.09 ? 836  SER A C   1 
ATOM   6727 O O   . SER A 1 836 ? 80.651 135.594 28.125  1.00 63.98 ? 836  SER A O   1 
ATOM   6728 C CB  . SER A 1 836 ? 82.753 138.331 28.237  1.00 64.25 ? 836  SER A CB  1 
ATOM   6729 O OG  . SER A 1 836 ? 82.687 138.154 29.647  1.00 65.09 ? 836  SER A OG  1 
ATOM   6730 N N   . THR A 1 838 ? 82.730 134.903 30.694  1.00 49.64 ? 838  THR A N   1 
ATOM   6731 C CA  . THR A 1 838 ? 84.107 135.410 30.682  1.00 49.21 ? 838  THR A CA  1 
ATOM   6732 C C   . THR A 1 838 ? 85.140 134.289 30.492  1.00 48.35 ? 838  THR A C   1 
ATOM   6733 O O   . THR A 1 838 ? 85.662 134.093 29.374  1.00 49.30 ? 838  THR A O   1 
ATOM   6734 C CB  . THR A 1 838 ? 84.454 136.204 31.969  1.00 50.08 ? 838  THR A CB  1 
ATOM   6735 O OG1 . THR A 1 838 ? 83.280 136.362 32.780  1.00 50.15 ? 838  THR A OG1 1 
ATOM   6736 C CG2 . THR A 1 838 ? 85.074 137.593 31.617  1.00 50.66 ? 838  THR A CG2 1 
ATOM   6737 N N   . SER A 1 839 ? 85.468 133.567 31.564  1.00 45.75 ? 839  SER A N   1 
ATOM   6738 C CA  . SER A 1 839 ? 86.328 132.390 31.410  1.00 43.62 ? 839  SER A CA  1 
ATOM   6739 C C   . SER A 1 839 ? 85.885 131.184 32.260  1.00 41.26 ? 839  SER A C   1 
ATOM   6740 O O   . SER A 1 839 ? 86.070 131.178 33.494  1.00 41.13 ? 839  SER A O   1 
ATOM   6741 C CB  . SER A 1 839 ? 87.800 132.717 31.656  1.00 44.00 ? 839  SER A CB  1 
ATOM   6742 O OG  . SER A 1 839 ? 88.596 131.582 31.323  1.00 46.31 ? 839  SER A OG  1 
ATOM   6743 N N   . PRO A 1 840 ? 85.298 130.163 31.596  1.00 38.37 ? 840  PRO A N   1 
ATOM   6744 C CA  . PRO A 1 840 ? 84.828 128.956 32.250  1.00 35.78 ? 840  PRO A CA  1 
ATOM   6745 C C   . PRO A 1 840 ? 85.954 128.152 32.894  1.00 33.51 ? 840  PRO A C   1 
ATOM   6746 O O   . PRO A 1 840 ? 87.112 128.267 32.494  1.00 32.45 ? 840  PRO A O   1 
ATOM   6747 C CB  . PRO A 1 840 ? 84.218 128.157 31.091  1.00 35.80 ? 840  PRO A CB  1 
ATOM   6748 C CG  . PRO A 1 840 ? 83.876 129.184 30.076  1.00 37.37 ? 840  PRO A CG  1 
ATOM   6749 C CD  . PRO A 1 840 ? 85.007 130.132 30.153  1.00 38.00 ? 840  PRO A CD  1 
ATOM   6750 N N   . THR A 1 841 ? 85.594 127.318 33.865  1.00 30.69 ? 841  THR A N   1 
ATOM   6751 C CA  . THR A 1 841 ? 86.528 126.376 34.492  1.00 29.03 ? 841  THR A CA  1 
ATOM   6752 C C   . THR A 1 841 ? 86.555 125.099 33.679  1.00 28.43 ? 841  THR A C   1 
ATOM   6753 O O   . THR A 1 841 ? 85.506 124.636 33.216  1.00 28.54 ? 841  THR A O   1 
ATOM   6754 C CB  . THR A 1 841 ? 86.075 126.078 35.951  1.00 28.87 ? 841  THR A CB  1 
ATOM   6755 O OG1 . THR A 1 841 ? 86.172 127.285 36.707  1.00 28.46 ? 841  THR A OG1 1 
ATOM   6756 C CG2 . THR A 1 841 ? 86.899 124.974 36.627  1.00 27.32 ? 841  THR A CG2 1 
ATOM   6757 N N   . VAL A 1 842 ? 87.737 124.533 33.499  1.00 26.97 ? 842  VAL A N   1 
ATOM   6758 C CA  . VAL A 1 842 ? 87.877 123.233 32.851  1.00 26.29 ? 842  VAL A CA  1 
ATOM   6759 C C   . VAL A 1 842 ? 88.608 122.311 33.777  1.00 26.10 ? 842  VAL A C   1 
ATOM   6760 O O   . VAL A 1 842 ? 89.682 122.652 34.317  1.00 26.05 ? 842  VAL A O   1 
ATOM   6761 C CB  . VAL A 1 842 ? 88.694 123.304 31.544  1.00 26.68 ? 842  VAL A CB  1 
ATOM   6762 C CG1 . VAL A 1 842 ? 88.887 121.909 30.945  1.00 26.38 ? 842  VAL A CG1 1 
ATOM   6763 C CG2 . VAL A 1 842 ? 88.053 124.281 30.581  1.00 25.63 ? 842  VAL A CG2 1 
ATOM   6764 N N   . THR A 1 843 ? 88.021 121.144 33.983  1.00 25.22 ? 843  THR A N   1 
ATOM   6765 C CA  . THR A 1 843 ? 88.688 120.052 34.688  1.00 25.00 ? 843  THR A CA  1 
ATOM   6766 C C   . THR A 1 843 ? 89.016 118.994 33.628  1.00 25.14 ? 843  THR A C   1 
ATOM   6767 O O   . THR A 1 843 ? 88.165 118.666 32.790  1.00 24.71 ? 843  THR A O   1 
ATOM   6768 C CB  . THR A 1 843 ? 87.764 119.453 35.792  1.00 24.41 ? 843  THR A CB  1 
ATOM   6769 O OG1 . THR A 1 843 ? 87.184 120.533 36.547  1.00 27.67 ? 843  THR A OG1 1 
ATOM   6770 C CG2 . THR A 1 843 ? 88.530 118.537 36.751  1.00 23.60 ? 843  THR A CG2 1 
ATOM   6771 N N   . TYR A 1 844 ? 90.237 118.463 33.657  1.00 24.86 ? 844  TYR A N   1 
ATOM   6772 C CA  . TYR A 1 844 ? 90.662 117.532 32.638  1.00 24.35 ? 844  TYR A CA  1 
ATOM   6773 C C   . TYR A 1 844 ? 91.344 116.301 33.225  1.00 24.87 ? 844  TYR A C   1 
ATOM   6774 O O   . TYR A 1 844 ? 92.134 116.404 34.169  1.00 23.51 ? 844  TYR A O   1 
ATOM   6775 C CB  . TYR A 1 844 ? 91.551 118.238 31.604  1.00 25.23 ? 844  TYR A CB  1 
ATOM   6776 C CG  . TYR A 1 844 ? 91.931 117.307 30.466  1.00 24.69 ? 844  TYR A CG  1 
ATOM   6777 C CD1 . TYR A 1 844 ? 90.967 116.880 29.541  1.00 25.18 ? 844  TYR A CD1 1 
ATOM   6778 C CD2 . TYR A 1 844 ? 93.217 116.821 30.346  1.00 24.59 ? 844  TYR A CD2 1 
ATOM   6779 C CE1 . TYR A 1 844 ? 91.289 116.025 28.499  1.00 24.43 ? 844  TYR A CE1 1 
ATOM   6780 C CE2 . TYR A 1 844 ? 93.566 115.932 29.292  1.00 25.67 ? 844  TYR A CE2 1 
ATOM   6781 C CZ  . TYR A 1 844 ? 92.584 115.546 28.381  1.00 26.38 ? 844  TYR A CZ  1 
ATOM   6782 O OH  . TYR A 1 844 ? 92.891 114.693 27.349  1.00 24.99 ? 844  TYR A OH  1 
ATOM   6783 N N   . ASP A 1 845 ? 90.973 115.135 32.694  1.00 24.73 ? 845  ASP A N   1 
ATOM   6784 C CA  . ASP A 1 845 ? 91.462 113.839 33.122  1.00 26.78 ? 845  ASP A CA  1 
ATOM   6785 C C   . ASP A 1 845 ? 92.226 113.286 31.918  1.00 27.49 ? 845  ASP A C   1 
ATOM   6786 O O   . ASP A 1 845 ? 91.613 112.797 30.967  1.00 26.93 ? 845  ASP A O   1 
ATOM   6787 C CB  . ASP A 1 845 ? 90.272 112.911 33.479  1.00 26.95 ? 845  ASP A CB  1 
ATOM   6788 C CG  . ASP A 1 845 ? 90.710 111.528 33.978  1.00 31.46 ? 845  ASP A CG  1 
ATOM   6789 O OD1 . ASP A 1 845 ? 91.809 111.021 33.567  1.00 29.99 ? 845  ASP A OD1 1 
ATOM   6790 O OD2 . ASP A 1 845 ? 89.923 110.924 34.767  1.00 33.37 ? 845  ASP A OD2 1 
ATOM   6791 N N   . SER A 1 846 ? 93.556 113.366 31.942  1.00 28.18 ? 846  SER A N   1 
ATOM   6792 C CA  . SER A 1 846 ? 94.348 112.984 30.769  1.00 29.18 ? 846  SER A CA  1 
ATOM   6793 C C   . SER A 1 846 ? 94.353 111.490 30.510  1.00 29.58 ? 846  SER A C   1 
ATOM   6794 O O   . SER A 1 846 ? 94.551 111.066 29.384  1.00 30.62 ? 846  SER A O   1 
ATOM   6795 C CB  . SER A 1 846 ? 95.781 113.525 30.878  1.00 29.82 ? 846  SER A CB  1 
ATOM   6796 O OG  . SER A 1 846 ? 96.335 113.036 32.092  1.00 31.61 ? 846  SER A OG  1 
ATOM   6797 N N   . ASN A 1 847 ? 94.133 110.693 31.549  1.00 29.77 ? 847  ASN A N   1 
ATOM   6798 C CA  . ASN A 1 847 ? 93.950 109.246 31.440  1.00 31.20 ? 847  ASN A CA  1 
ATOM   6799 C C   . ASN A 1 847 ? 92.689 108.837 30.624  1.00 30.43 ? 847  ASN A C   1 
ATOM   6800 O O   . ASN A 1 847 ? 92.760 107.982 29.738  1.00 30.51 ? 847  ASN A O   1 
ATOM   6801 C CB  . ASN A 1 847 ? 93.868 108.653 32.852  1.00 32.48 ? 847  ASN A CB  1 
ATOM   6802 C CG  . ASN A 1 847 ? 93.748 107.132 32.863  1.00 39.11 ? 847  ASN A CG  1 
ATOM   6803 O OD1 . ASN A 1 847 ? 92.978 106.554 33.670  1.00 43.41 ? 847  ASN A OD1 1 
ATOM   6804 N ND2 . ASN A 1 847 ? 94.533 106.460 31.992  1.00 44.37 ? 847  ASN A ND2 1 
ATOM   6805 N N   . LEU A 1 848 ? 91.557 109.467 30.928  1.00 28.93 ? 848  LEU A N   1 
ATOM   6806 C CA  . LEU A 1 848 ? 90.274 109.091 30.355  1.00 28.31 ? 848  LEU A CA  1 
ATOM   6807 C C   . LEU A 1 848 ? 89.924 109.919 29.128  1.00 26.78 ? 848  LEU A C   1 
ATOM   6808 O O   . LEU A 1 848 ? 89.004 109.588 28.394  1.00 26.34 ? 848  LEU A O   1 
ATOM   6809 C CB  . LEU A 1 848 ? 89.182 109.201 31.423  1.00 28.55 ? 848  LEU A CB  1 
ATOM   6810 C CG  . LEU A 1 848 ? 88.763 107.958 32.230  1.00 29.69 ? 848  LEU A CG  1 
ATOM   6811 C CD1 . LEU A 1 848 ? 89.861 106.915 32.396  1.00 31.67 ? 848  LEU A CD1 1 
ATOM   6812 C CD2 . LEU A 1 848 ? 88.195 108.337 33.563  1.00 28.04 ? 848  LEU A CD2 1 
ATOM   6813 N N   . LYS A 1 849 ? 90.676 110.991 28.911  1.00 25.92 ? 849  LYS A N   1 
ATOM   6814 C CA  . LYS A 1 849 ? 90.424 111.924 27.817  1.00 24.59 ? 849  LYS A CA  1 
ATOM   6815 C C   . LYS A 1 849 ? 89.074 112.655 27.972  1.00 24.28 ? 849  LYS A C   1 
ATOM   6816 O O   . LYS A 1 849 ? 88.412 112.973 26.982  1.00 22.75 ? 849  LYS A O   1 
ATOM   6817 C CB  . LYS A 1 849 ? 90.562 111.198 26.459  1.00 25.54 ? 849  LYS A CB  1 
ATOM   6818 C CG  . LYS A 1 849 ? 91.937 110.465 26.295  1.00 24.21 ? 849  LYS A CG  1 
ATOM   6819 C CD  . LYS A 1 849 ? 93.056 111.496 26.050  1.00 24.92 ? 849  LYS A CD  1 
ATOM   6820 C CE  . LYS A 1 849 ? 94.460 110.860 25.869  1.00 27.48 ? 849  LYS A CE  1 
ATOM   6821 N NZ  . LYS A 1 849 ? 95.527 111.933 25.541  1.00 28.30 ? 849  LYS A NZ  1 
ATOM   6822 N N   . VAL A 1 850 ? 88.711 112.951 29.225  1.00 23.07 ? 850  VAL A N   1 
ATOM   6823 C CA  . VAL A 1 850 ? 87.483 113.680 29.586  1.00 21.97 ? 850  VAL A CA  1 
ATOM   6824 C C   . VAL A 1 850 ? 87.785 115.103 30.071  1.00 22.54 ? 850  VAL A C   1 
ATOM   6825 O O   . VAL A 1 850 ? 88.606 115.296 30.967  1.00 22.15 ? 850  VAL A O   1 
ATOM   6826 C CB  . VAL A 1 850 ? 86.693 112.922 30.696  1.00 21.98 ? 850  VAL A CB  1 
ATOM   6827 C CG1 . VAL A 1 850 ? 85.432 113.699 31.130  1.00 21.92 ? 850  VAL A CG1 1 
ATOM   6828 C CG2 . VAL A 1 850 ? 86.313 111.505 30.222  1.00 21.18 ? 850  VAL A CG2 1 
ATOM   6829 N N   . ALA A 1 851 ? 87.124 116.088 29.468  1.00 22.94 ? 851  ALA A N   1 
ATOM   6830 C CA  . ALA A 1 851 ? 87.143 117.471 29.936  1.00 23.24 ? 851  ALA A CA  1 
ATOM   6831 C C   . ALA A 1 851 ? 85.750 117.790 30.406  1.00 24.06 ? 851  ALA A C   1 
ATOM   6832 O O   . ALA A 1 851 ? 84.779 117.418 29.741  1.00 23.26 ? 851  ALA A O   1 
ATOM   6833 C CB  . ALA A 1 851 ? 87.520 118.429 28.798  1.00 22.97 ? 851  ALA A CB  1 
ATOM   6834 N N   . ILE A 1 852 ? 85.641 118.490 31.537  1.00 24.38 ? 852  ILE A N   1 
ATOM   6835 C CA  . ILE A 1 852 ? 84.348 118.972 32.025  1.00 24.52 ? 852  ILE A CA  1 
ATOM   6836 C C   . ILE A 1 852 ? 84.496 120.451 32.197  1.00 24.56 ? 852  ILE A C   1 
ATOM   6837 O O   . ILE A 1 852 ? 85.398 120.890 32.897  1.00 24.57 ? 852  ILE A O   1 
ATOM   6838 C CB  . ILE A 1 852 ? 83.950 118.333 33.364  1.00 24.61 ? 852  ILE A CB  1 
ATOM   6839 C CG1 . ILE A 1 852 ? 83.700 116.840 33.183  1.00 26.72 ? 852  ILE A CG1 1 
ATOM   6840 C CG2 . ILE A 1 852 ? 82.700 118.992 33.901  1.00 26.49 ? 852  ILE A CG2 1 
ATOM   6841 C CD1 . ILE A 1 852 ? 83.619 116.068 34.476  1.00 33.50 ? 852  ILE A CD1 1 
ATOM   6842 N N   . ILE A 1 853 ? 83.629 121.210 31.539  1.00 24.28 ? 853  ILE A N   1 
ATOM   6843 C CA  . ILE A 1 853 ? 83.654 122.652 31.568  1.00 24.49 ? 853  ILE A CA  1 
ATOM   6844 C C   . ILE A 1 853 ? 82.518 123.091 32.483  1.00 25.42 ? 853  ILE A C   1 
ATOM   6845 O O   . ILE A 1 853 ? 81.370 122.720 32.260  1.00 25.09 ? 853  ILE A O   1 
ATOM   6846 C CB  . ILE A 1 853 ? 83.454 123.269 30.149  1.00 24.67 ? 853  ILE A CB  1 
ATOM   6847 C CG1 . ILE A 1 853 ? 84.525 122.785 29.171  1.00 24.74 ? 853  ILE A CG1 1 
ATOM   6848 C CG2 . ILE A 1 853 ? 83.352 124.808 30.193  1.00 24.51 ? 853  ILE A CG2 1 
ATOM   6849 C CD1 . ILE A 1 853 ? 84.196 123.121 27.710  1.00 23.55 ? 853  ILE A CD1 1 
ATOM   6850 N N   . THR A 1 854 ? 82.843 123.874 33.506  1.00 26.13 ? 854  THR A N   1 
ATOM   6851 C CA  . THR A 1 854 ? 81.853 124.383 34.468  1.00 27.67 ? 854  THR A CA  1 
ATOM   6852 C C   . THR A 1 854 ? 81.991 125.900 34.574  1.00 28.17 ? 854  THR A C   1 
ATOM   6853 O O   . THR A 1 854 ? 82.830 126.501 33.878  1.00 27.11 ? 854  THR A O   1 
ATOM   6854 C CB  . THR A 1 854 ? 82.028 123.759 35.865  1.00 27.87 ? 854  THR A CB  1 
ATOM   6855 O OG1 . THR A 1 854 ? 83.415 123.786 36.227  1.00 29.34 ? 854  THR A OG1 1 
ATOM   6856 C CG2 . THR A 1 854 ? 81.507 122.281 35.910  1.00 27.72 ? 854  THR A CG2 1 
ATOM   6857 N N   . ASP A 1 855 ? 81.171 126.521 35.423  1.00 28.65 ? 855  ASP A N   1 
ATOM   6858 C CA  . ASP A 1 855 ? 81.170 127.978 35.581  1.00 30.47 ? 855  ASP A CA  1 
ATOM   6859 C C   . ASP A 1 855 ? 80.849 128.624 34.237  1.00 30.38 ? 855  ASP A C   1 
ATOM   6860 O O   . ASP A 1 855 ? 81.508 129.559 33.802  1.00 29.99 ? 855  ASP A O   1 
ATOM   6861 C CB  . ASP A 1 855 ? 82.530 128.490 36.110  1.00 30.51 ? 855  ASP A CB  1 
ATOM   6862 C CG  . ASP A 1 855 ? 82.421 129.854 36.795  1.00 33.85 ? 855  ASP A CG  1 
ATOM   6863 O OD1 . ASP A 1 855 ? 81.392 130.128 37.444  1.00 36.67 ? 855  ASP A OD1 1 
ATOM   6864 O OD2 . ASP A 1 855 ? 83.378 130.658 36.693  1.00 37.21 ? 855  ASP A OD2 1 
ATOM   6865 N N   . ILE A 1 856 ? 79.837 128.094 33.573  1.00 30.97 ? 856  ILE A N   1 
ATOM   6866 C CA  . ILE A 1 856 ? 79.443 128.569 32.263  1.00 31.23 ? 856  ILE A CA  1 
ATOM   6867 C C   . ILE A 1 856 ? 77.952 128.780 32.374  1.00 31.12 ? 856  ILE A C   1 
ATOM   6868 O O   . ILE A 1 856 ? 77.312 128.153 33.191  1.00 31.42 ? 856  ILE A O   1 
ATOM   6869 C CB  . ILE A 1 856 ? 79.828 127.514 31.198  1.00 31.71 ? 856  ILE A CB  1 
ATOM   6870 C CG1 . ILE A 1 856 ? 79.963 128.127 29.808  1.00 31.60 ? 856  ILE A CG1 1 
ATOM   6871 C CG2 . ILE A 1 856 ? 78.846 126.305 31.195  1.00 33.02 ? 856  ILE A CG2 1 
ATOM   6872 C CD1 . ILE A 1 856 ? 80.838 127.231 28.874  1.00 31.38 ? 856  ILE A CD1 1 
ATOM   6873 N N   . ASP A 1 857 ? 77.404 129.678 31.579  1.00 31.74 ? 857  ASP A N   1 
ATOM   6874 C CA  . ASP A 1 857 ? 76.007 130.014 31.669  1.00 32.88 ? 857  ASP A CA  1 
ATOM   6875 C C   . ASP A 1 857 ? 75.520 130.273 30.248  1.00 32.02 ? 857  ASP A C   1 
ATOM   6876 O O   . ASP A 1 857 ? 75.504 131.411 29.809  1.00 32.30 ? 857  ASP A O   1 
ATOM   6877 C CB  . ASP A 1 857 ? 75.867 131.263 32.544  1.00 34.10 ? 857  ASP A CB  1 
ATOM   6878 C CG  . ASP A 1 857 ? 74.422 131.576 32.944  1.00 38.57 ? 857  ASP A CG  1 
ATOM   6879 O OD1 . ASP A 1 857 ? 73.528 130.717 32.803  1.00 43.97 ? 857  ASP A OD1 1 
ATOM   6880 O OD2 . ASP A 1 857 ? 74.174 132.713 33.432  1.00 43.84 ? 857  ASP A OD2 1 
ATOM   6881 N N   . LEU A 1 858 ? 75.158 129.212 29.515  1.00 30.99 ? 858  LEU A N   1 
ATOM   6882 C CA  . LEU A 1 858 ? 74.574 129.373 28.169  1.00 29.77 ? 858  LEU A CA  1 
ATOM   6883 C C   . LEU A 1 858 ? 73.063 129.320 28.256  1.00 29.98 ? 858  LEU A C   1 
ATOM   6884 O O   . LEU A 1 858 ? 72.490 128.248 28.441  1.00 31.07 ? 858  LEU A O   1 
ATOM   6885 C CB  . LEU A 1 858 ? 75.086 128.313 27.181  1.00 28.42 ? 858  LEU A CB  1 
ATOM   6886 C CG  . LEU A 1 858 ? 76.558 127.925 27.242  1.00 28.70 ? 858  LEU A CG  1 
ATOM   6887 C CD1 . LEU A 1 858 ? 76.887 126.900 26.183  1.00 27.18 ? 858  LEU A CD1 1 
ATOM   6888 C CD2 . LEU A 1 858 ? 77.501 129.142 27.129  1.00 25.67 ? 858  LEU A CD2 1 
ATOM   6889 N N   . LEU A 1 859 ? 72.412 130.465 28.117  1.00 29.46 ? 859  LEU A N   1 
ATOM   6890 C CA  . LEU A 1 859 ? 70.978 130.515 28.247  1.00 29.88 ? 859  LEU A CA  1 
ATOM   6891 C C   . LEU A 1 859 ? 70.296 129.677 27.178  1.00 29.84 ? 859  LEU A C   1 
ATOM   6892 O O   . LEU A 1 859 ? 70.716 129.655 26.017  1.00 29.80 ? 859  LEU A O   1 
ATOM   6893 C CB  . LEU A 1 859 ? 70.474 131.959 28.190  1.00 30.24 ? 859  LEU A CB  1 
ATOM   6894 C CG  . LEU A 1 859 ? 71.058 132.952 29.207  1.00 30.97 ? 859  LEU A CG  1 
ATOM   6895 C CD1 . LEU A 1 859 ? 70.419 134.339 29.023  1.00 32.32 ? 859  LEU A CD1 1 
ATOM   6896 C CD2 . LEU A 1 859 ? 70.866 132.436 30.630  1.00 31.00 ? 859  LEU A CD2 1 
ATOM   6897 N N   . LEU A 1 860 ? 69.246 128.976 27.584  1.00 29.76 ? 860  LEU A N   1 
ATOM   6898 C CA  . LEU A 1 860 ? 68.509 128.131 26.658  1.00 29.37 ? 860  LEU A CA  1 
ATOM   6899 C C   . LEU A 1 860 ? 67.809 129.025 25.673  1.00 29.24 ? 860  LEU A C   1 
ATOM   6900 O O   . LEU A 1 860 ? 67.149 129.999 26.065  1.00 29.70 ? 860  LEU A O   1 
ATOM   6901 C CB  . LEU A 1 860 ? 67.526 127.248 27.408  1.00 29.24 ? 860  LEU A CB  1 
ATOM   6902 C CG  . LEU A 1 860 ? 66.594 126.410 26.538  1.00 28.83 ? 860  LEU A CG  1 
ATOM   6903 C CD1 . LEU A 1 860 ? 67.361 125.278 25.884  1.00 28.35 ? 860  LEU A CD1 1 
ATOM   6904 C CD2 . LEU A 1 860 ? 65.452 125.888 27.360  1.00 29.14 ? 860  LEU A CD2 1 
ATOM   6905 N N   . GLY A 1 861 ? 67.997 128.733 24.389  1.00 29.67 ? 861  GLY A N   1 
ATOM   6906 C CA  . GLY A 1 861 ? 67.292 129.444 23.327  1.00 29.46 ? 861  GLY A CA  1 
ATOM   6907 C C   . GLY A 1 861 ? 68.100 130.589 22.747  1.00 29.94 ? 861  GLY A C   1 
ATOM   6908 O O   . GLY A 1 861 ? 67.576 131.359 21.929  1.00 30.16 ? 861  GLY A O   1 
ATOM   6909 N N   . GLU A 1 862 ? 69.357 130.695 23.188  1.00 29.28 ? 862  GLU A N   1 
ATOM   6910 C CA  . GLU A 1 862 ? 70.328 131.678 22.715  1.00 29.49 ? 862  GLU A CA  1 
ATOM   6911 C C   . GLU A 1 862 ? 71.489 131.014 21.949  1.00 29.12 ? 862  GLU A C   1 
ATOM   6912 O O   . GLU A 1 862 ? 71.940 129.921 22.320  1.00 28.49 ? 862  GLU A O   1 
ATOM   6913 C CB  . GLU A 1 862 ? 70.917 132.437 23.906  1.00 29.26 ? 862  GLU A CB  1 
ATOM   6914 C CG  . GLU A 1 862 ? 69.970 133.393 24.573  1.00 33.05 ? 862  GLU A CG  1 
ATOM   6915 C CD  . GLU A 1 862 ? 69.552 134.547 23.676  1.00 37.14 ? 862  GLU A CD  1 
ATOM   6916 O OE1 . GLU A 1 862 ? 70.384 135.061 22.882  1.00 37.70 ? 862  GLU A OE1 1 
ATOM   6917 O OE2 . GLU A 1 862 ? 68.374 134.945 23.776  1.00 39.77 ? 862  GLU A OE2 1 
ATOM   6918 N N   . ALA A 1 863 ? 71.951 131.681 20.887  1.00 28.54 ? 863  ALA A N   1 
ATOM   6919 C CA  . ALA A 1 863 ? 73.051 131.207 20.081  1.00 28.88 ? 863  ALA A CA  1 
ATOM   6920 C C   . ALA A 1 863 ? 74.363 131.556 20.779  1.00 29.22 ? 863  ALA A C   1 
ATOM   6921 O O   . ALA A 1 863 ? 74.531 132.681 21.254  1.00 29.86 ? 863  ALA A O   1 
ATOM   6922 C CB  . ALA A 1 863 ? 72.999 131.867 18.714  1.00 29.16 ? 863  ALA A CB  1 
ATOM   6923 N N   . TYR A 1 864 ? 75.267 130.589 20.847  1.00 29.08 ? 864  TYR A N   1 
ATOM   6924 C CA  . TYR A 1 864 ? 76.606 130.730 21.435  1.00 28.98 ? 864  TYR A CA  1 
ATOM   6925 C C   . TYR A 1 864 ? 77.622 130.013 20.583  1.00 29.00 ? 864  TYR A C   1 
ATOM   6926 O O   . TYR A 1 864 ? 77.274 129.052 19.884  1.00 28.21 ? 864  TYR A O   1 
ATOM   6927 C CB  . TYR A 1 864 ? 76.690 130.081 22.824  1.00 28.92 ? 864  TYR A CB  1 
ATOM   6928 C CG  . TYR A 1 864 ? 75.920 130.801 23.886  1.00 29.66 ? 864  TYR A CG  1 
ATOM   6929 C CD1 . TYR A 1 864 ? 76.500 131.838 24.627  1.00 30.02 ? 864  TYR A CD1 1 
ATOM   6930 C CD2 . TYR A 1 864 ? 74.598 130.456 24.146  1.00 31.22 ? 864  TYR A CD2 1 
ATOM   6931 C CE1 . TYR A 1 864 ? 75.759 132.510 25.601  1.00 30.84 ? 864  TYR A CE1 1 
ATOM   6932 C CE2 . TYR A 1 864 ? 73.869 131.102 25.099  1.00 31.07 ? 864  TYR A CE2 1 
ATOM   6933 C CZ  . TYR A 1 864 ? 74.441 132.128 25.837  1.00 29.43 ? 864  TYR A CZ  1 
ATOM   6934 O OH  . TYR A 1 864 ? 73.660 132.743 26.802  1.00 29.53 ? 864  TYR A OH  1 
ATOM   6935 N N   . THR A 1 865 ? 78.875 130.487 20.656  1.00 29.45 ? 865  THR A N   1 
ATOM   6936 C CA  . THR A 1 865 ? 80.038 129.778 20.169  1.00 29.88 ? 865  THR A CA  1 
ATOM   6937 C C   . THR A 1 865 ? 80.979 129.613 21.354  1.00 30.44 ? 865  THR A C   1 
ATOM   6938 O O   . THR A 1 865 ? 81.272 130.584 22.048  1.00 31.11 ? 865  THR A O   1 
ATOM   6939 C CB  . THR A 1 865 ? 80.817 130.561 19.064  1.00 30.25 ? 865  THR A CB  1 
ATOM   6940 O OG1 . THR A 1 865 ? 79.946 130.930 17.994  1.00 29.26 ? 865  THR A OG1 1 
ATOM   6941 C CG2 . THR A 1 865 ? 81.933 129.683 18.483  1.00 30.68 ? 865  THR A CG2 1 
ATOM   6942 N N   . VAL A 1 866 ? 81.484 128.400 21.559  1.00 30.49 ? 866  VAL A N   1 
ATOM   6943 C CA  . VAL A 1 866 ? 82.406 128.085 22.653  1.00 30.25 ? 866  VAL A CA  1 
ATOM   6944 C C   . VAL A 1 866 ? 83.661 127.566 21.980  1.00 31.22 ? 866  VAL A C   1 
ATOM   6945 O O   . VAL A 1 866 ? 83.580 126.686 21.123  1.00 31.24 ? 866  VAL A O   1 
ATOM   6946 C CB  . VAL A 1 866 ? 81.788 127.049 23.654  1.00 29.72 ? 866  VAL A CB  1 
ATOM   6947 C CG1 . VAL A 1 866 ? 82.785 126.626 24.732  1.00 27.53 ? 866  VAL A CG1 1 
ATOM   6948 C CG2 . VAL A 1 866 ? 80.548 127.630 24.296  1.00 29.31 ? 866  VAL A CG2 1 
ATOM   6949 N N   . GLU A 1 867 ? 84.811 128.137 22.329  1.00 31.99 ? 867  GLU A N   1 
ATOM   6950 C CA  . GLU A 1 867 ? 86.057 127.881 21.600  1.00 33.15 ? 867  GLU A CA  1 
ATOM   6951 C C   . GLU A 1 867 ? 87.198 127.567 22.535  1.00 32.71 ? 867  GLU A C   1 
ATOM   6952 O O   . GLU A 1 867 ? 87.231 128.053 23.635  1.00 32.61 ? 867  GLU A O   1 
ATOM   6953 C CB  . GLU A 1 867 ? 86.429 129.086 20.741  1.00 33.68 ? 867  GLU A CB  1 
ATOM   6954 C CG  . GLU A 1 867 ? 85.432 129.355 19.626  1.00 38.44 ? 867  GLU A CG  1 
ATOM   6955 C CD  . GLU A 1 867 ? 85.904 130.438 18.677  1.00 43.39 ? 867  GLU A CD  1 
ATOM   6956 O OE1 . GLU A 1 867 ? 86.009 131.604 19.109  1.00 47.20 ? 867  GLU A OE1 1 
ATOM   6957 O OE2 . GLU A 1 867 ? 86.173 130.120 17.505  1.00 45.81 ? 867  GLU A OE2 1 
ATOM   6958 N N   . TRP A 1 868 ? 88.130 126.736 22.084  1.00 33.39 ? 868  TRP A N   1 
ATOM   6959 C CA  . TRP A 1 868 ? 89.284 126.354 22.898  1.00 33.83 ? 868  TRP A CA  1 
ATOM   6960 C C   . TRP A 1 868 ? 90.516 126.075 22.043  1.00 34.91 ? 868  TRP A C   1 
ATOM   6961 O O   . TRP A 1 868 ? 90.405 125.723 20.871  1.00 35.06 ? 868  TRP A O   1 
ATOM   6962 C CB  . TRP A 1 868 ? 88.972 125.129 23.769  1.00 32.75 ? 868  TRP A CB  1 
ATOM   6963 C CG  . TRP A 1 868 ? 88.540 123.907 23.014  1.00 31.38 ? 868  TRP A CG  1 
ATOM   6964 C CD1 . TRP A 1 868 ? 89.335 122.910 22.542  1.00 30.94 ? 868  TRP A CD1 1 
ATOM   6965 C CD2 . TRP A 1 868 ? 87.194 123.534 22.685  1.00 31.92 ? 868  TRP A CD2 1 
ATOM   6966 N NE1 . TRP A 1 868 ? 88.574 121.935 21.924  1.00 31.92 ? 868  TRP A NE1 1 
ATOM   6967 C CE2 . TRP A 1 868 ? 87.258 122.301 21.993  1.00 30.81 ? 868  TRP A CE2 1 
ATOM   6968 C CE3 . TRP A 1 868 ? 85.937 124.134 22.894  1.00 31.66 ? 868  TRP A CE3 1 
ATOM   6969 C CZ2 . TRP A 1 868 ? 86.112 121.650 21.512  1.00 33.29 ? 868  TRP A CZ2 1 
ATOM   6970 C CZ3 . TRP A 1 868 ? 84.805 123.492 22.408  1.00 31.45 ? 868  TRP A CZ3 1 
ATOM   6971 C CH2 . TRP A 1 868 ? 84.901 122.260 21.726  1.00 30.44 ? 868  TRP A CH2 1 
ATOM   6972 N N   . ALA A 1 869 ? 91.686 126.231 22.656  1.00 36.60 ? 869  ALA A N   1 
ATOM   6973 C CA  . ALA A 1 869 ? 92.959 125.800 22.065  1.00 37.70 ? 869  ALA A CA  1 
ATOM   6974 C C   . ALA A 1 869 ? 93.338 124.422 22.588  1.00 38.18 ? 869  ALA A C   1 
ATOM   6975 O O   . ALA A 1 869 ? 92.775 123.949 23.585  1.00 38.02 ? 869  ALA A O   1 
ATOM   6976 C CB  . ALA A 1 869 ? 94.055 126.800 22.421  1.00 37.88 ? 869  ALA A CB  1 
ATOM   6977 N N   . HIS A 1 870 ? 94.295 123.784 21.922  1.00 38.81 ? 870  HIS A N   1 
ATOM   6978 C CA  . HIS A 1 870 ? 94.870 122.543 22.415  1.00 39.95 ? 870  HIS A CA  1 
ATOM   6979 C C   . HIS A 1 870 ? 96.332 122.736 22.846  1.00 40.88 ? 870  HIS A C   1 
ATOM   6980 O O   . HIS A 1 870 ? 97.223 122.865 22.001  1.00 42.07 ? 870  HIS A O   1 
ATOM   6981 C CB  . HIS A 1 870 ? 94.739 121.425 21.377  1.00 40.02 ? 870  HIS A CB  1 
ATOM   6982 C CG  . HIS A 1 870 ? 93.353 120.855 21.277  1.00 40.40 ? 870  HIS A CG  1 
ATOM   6983 N ND1 . HIS A 1 870 ? 92.707 120.277 22.348  1.00 40.90 ? 870  HIS A ND1 1 
ATOM   6984 C CD2 . HIS A 1 870 ? 92.486 120.789 20.240  1.00 41.43 ? 870  HIS A CD2 1 
ATOM   6985 C CE1 . HIS A 1 870 ? 91.502 119.881 21.979  1.00 40.75 ? 870  HIS A CE1 1 
ATOM   6986 N NE2 . HIS A 1 870 ? 91.346 120.170 20.700  1.00 41.80 ? 870  HIS A NE2 1 
HETATM 6987 O OAA . KTL B 2 .   ? 41.225 84.142  30.767  1.00 36.11 ? 1001 KTL A OAA 1 
HETATM 6988 O OAB . KTL B 2 .   ? 42.374 95.541  36.128  1.00 23.87 ? 1001 KTL A OAB 1 
HETATM 6989 O OAC . KTL B 2 .   ? 43.638 86.119  30.198  1.00 28.82 ? 1001 KTL A OAC 1 
HETATM 6990 O OAD . KTL B 2 .   ? 47.010 95.246  33.925  1.00 25.95 ? 1001 KTL A OAD 1 
HETATM 6991 O OAE . KTL B 2 .   ? 44.050 90.967  31.957  1.00 24.30 ? 1001 KTL A OAE 1 
HETATM 6992 O OAF . KTL B 2 .   ? 44.443 86.319  32.779  1.00 24.99 ? 1001 KTL A OAF 1 
HETATM 6993 O OAG . KTL B 2 .   ? 45.998 95.085  36.657  1.00 20.52 ? 1001 KTL A OAG 1 
HETATM 6994 O OAH . KTL B 2 .   ? 41.683 88.668  32.134  1.00 22.75 ? 1001 KTL A OAH 1 
HETATM 6995 O OAI . KTL B 2 .   ? 44.560 87.097  35.675  1.00 31.15 ? 1001 KTL A OAI 1 
HETATM 6996 O OAJ . KTL B 2 .   ? 44.526 89.281  36.571  1.00 29.78 ? 1001 KTL A OAJ 1 
HETATM 6997 O OAK . KTL B 2 .   ? 42.555 87.837  36.856  1.00 29.74 ? 1001 KTL A OAK 1 
HETATM 6998 C CAL . KTL B 2 .   ? 42.375 84.521  31.558  1.00 32.77 ? 1001 KTL A CAL 1 
HETATM 6999 C CAM . KTL B 2 .   ? 42.984 94.328  36.601  1.00 21.88 ? 1001 KTL A CAM 1 
HETATM 7000 C CAN . KTL B 2 .   ? 45.026 93.736  33.309  1.00 23.48 ? 1001 KTL A CAN 1 
HETATM 7001 C CAO . KTL B 2 .   ? 43.875 91.553  34.349  1.00 24.34 ? 1001 KTL A CAO 1 
HETATM 7002 O OAP . KTL B 2 .   ? 42.912 88.771  34.624  1.00 29.80 ? 1001 KTL A OAP 1 
HETATM 7003 C CAQ . KTL B 2 .   ? 42.666 86.002  31.244  1.00 29.37 ? 1001 KTL A CAQ 1 
HETATM 7004 C CAR . KTL B 2 .   ? 46.026 94.270  34.354  1.00 22.77 ? 1001 KTL A CAR 1 
HETATM 7005 C CAS . KTL B 2 .   ? 43.424 90.632  33.198  1.00 25.78 ? 1001 KTL A CAS 1 
HETATM 7006 C CAT . KTL B 2 .   ? 43.121 86.756  32.495  1.00 27.37 ? 1001 KTL A CAT 1 
HETATM 7007 C CAU . KTL B 2 .   ? 45.201 94.847  35.496  1.00 22.52 ? 1001 KTL A CAU 1 
HETATM 7008 C CAV . KTL B 2 .   ? 43.056 88.284  32.316  1.00 25.81 ? 1001 KTL A CAV 1 
HETATM 7009 C CAW . KTL B 2 .   ? 44.109 93.796  35.721  1.00 22.73 ? 1001 KTL A CAW 1 
HETATM 7010 C CAX . KTL B 2 .   ? 43.642 89.129  33.462  1.00 26.12 ? 1001 KTL A CAX 1 
HETATM 7011 S SAY . KTL B 2 .   ? 43.685 93.226  34.188  1.00 24.99 ? 1001 KTL A SAY 1 
HETATM 7012 S SAZ . KTL B 2 .   ? 43.661 88.237  35.966  1.00 29.17 ? 1001 KTL A SAZ 1 
HETATM 7013 C C1  . NAG C 3 .   ? 63.828 118.866 43.865  1.00 31.77 ? 2001 NAG A C1  1 
HETATM 7014 C C2  . NAG C 3 .   ? 64.333 120.297 44.063  1.00 31.96 ? 2001 NAG A C2  1 
HETATM 7015 C C3  . NAG C 3 .   ? 64.093 120.761 45.508  1.00 34.48 ? 2001 NAG A C3  1 
HETATM 7016 C C4  . NAG C 3 .   ? 62.626 120.649 45.931  1.00 38.76 ? 2001 NAG A C4  1 
HETATM 7017 C C5  . NAG C 3 .   ? 62.048 119.292 45.538  1.00 38.35 ? 2001 NAG A C5  1 
HETATM 7018 C C6  . NAG C 3 .   ? 60.535 119.436 45.437  1.00 39.35 ? 2001 NAG A C6  1 
HETATM 7019 C C7  . NAG C 3 .   ? 66.280 121.370 43.042  1.00 35.26 ? 2001 NAG A C7  1 
HETATM 7020 C C8  . NAG C 3 .   ? 67.747 121.306 42.690  1.00 31.94 ? 2001 NAG A C8  1 
HETATM 7021 N N2  . NAG C 3 .   ? 65.744 120.336 43.718  1.00 31.40 ? 2001 NAG A N2  1 
HETATM 7022 O O3  . NAG C 3 .   ? 64.479 122.102 45.657  1.00 33.45 ? 2001 NAG A O3  1 
HETATM 7023 O O4  . NAG C 3 .   ? 62.462 120.672 47.341  1.00 44.10 ? 2001 NAG A O4  1 
HETATM 7024 O O5  . NAG C 3 .   ? 62.498 118.721 44.315  1.00 33.81 ? 2001 NAG A O5  1 
HETATM 7025 O O6  . NAG C 3 .   ? 60.042 118.186 45.847  1.00 44.11 ? 2001 NAG A O6  1 
HETATM 7026 O O7  . NAG C 3 .   ? 65.630 122.382 42.716  1.00 36.98 ? 2001 NAG A O7  1 
HETATM 7027 C C1  . NAG D 3 .   ? 62.628 121.946 48.015  1.00 50.49 ? 2002 NAG A C1  1 
HETATM 7028 C C2  . NAG D 3 .   ? 61.492 122.121 49.031  1.00 54.00 ? 2002 NAG A C2  1 
HETATM 7029 C C3  . NAG D 3 .   ? 60.867 123.526 49.003  1.00 53.83 ? 2002 NAG A C3  1 
HETATM 7030 C C4  . NAG D 3 .   ? 61.948 124.636 48.912  1.00 55.25 ? 2002 NAG A C4  1 
HETATM 7031 C C5  . NAG D 3 .   ? 63.068 124.350 47.900  1.00 53.97 ? 2002 NAG A C5  1 
HETATM 7032 C C6  . NAG D 3 .   ? 64.442 124.423 48.585  1.00 54.09 ? 2002 NAG A C6  1 
HETATM 7033 C C7  . NAG D 3 .   ? 60.522 120.056 49.826  1.00 57.37 ? 2002 NAG A C7  1 
HETATM 7034 C C8  . NAG D 3 .   ? 61.086 118.692 49.504  1.00 56.70 ? 2002 NAG A C8  1 
HETATM 7035 N N2  . NAG D 3 .   ? 60.539 121.017 48.902  1.00 56.07 ? 2002 NAG A N2  1 
HETATM 7036 O O3  . NAG D 3 .   ? 60.101 123.688 50.183  1.00 51.11 ? 2002 NAG A O3  1 
HETATM 7037 O O4  . NAG D 3 .   ? 61.377 125.896 48.584  1.00 57.64 ? 2002 NAG A O4  1 
HETATM 7038 O O5  . NAG D 3 .   ? 62.842 123.108 47.211  1.00 52.69 ? 2002 NAG A O5  1 
HETATM 7039 O O6  . NAG D 3 .   ? 65.387 125.202 47.870  1.00 51.28 ? 2002 NAG A O6  1 
HETATM 7040 O O7  . NAG D 3 .   ? 60.066 120.292 50.944  1.00 59.63 ? 2002 NAG A O7  1 
HETATM 7041 C C1  . NAG E 3 .   ? 21.066 99.378  19.258  1.00 30.80 ? 2003 NAG A C1  1 
HETATM 7042 C C2  . NAG E 3 .   ? 21.236 100.246 18.005  1.00 32.16 ? 2003 NAG A C2  1 
HETATM 7043 C C3  . NAG E 3 .   ? 20.636 101.657 18.187  1.00 32.81 ? 2003 NAG A C3  1 
HETATM 7044 C C4  . NAG E 3 .   ? 19.190 101.644 18.686  1.00 34.50 ? 2003 NAG A C4  1 
HETATM 7045 C C5  . NAG E 3 .   ? 19.115 100.675 19.874  1.00 33.30 ? 2003 NAG A C5  1 
HETATM 7046 C C6  . NAG E 3 .   ? 17.689 100.523 20.406  1.00 33.76 ? 2003 NAG A C6  1 
HETATM 7047 C C7  . NAG E 3 .   ? 23.142 99.616  16.570  1.00 32.28 ? 2003 NAG A C7  1 
HETATM 7048 C C8  . NAG E 3 .   ? 24.603 99.801  16.277  1.00 34.58 ? 2003 NAG A C8  1 
HETATM 7049 N N2  . NAG E 3 .   ? 22.642 100.314 17.587  1.00 33.26 ? 2003 NAG A N2  1 
HETATM 7050 O O3  . NAG E 3 .   ? 20.634 102.322 16.953  1.00 31.36 ? 2003 NAG A O3  1 
HETATM 7051 O O4  . NAG E 3 .   ? 18.788 102.952 19.105  1.00 37.94 ? 2003 NAG A O4  1 
HETATM 7052 O O5  . NAG E 3 .   ? 19.678 99.389  19.596  1.00 32.09 ? 2003 NAG A O5  1 
HETATM 7053 O O6  . NAG E 3 .   ? 17.708 99.754  21.592  1.00 34.81 ? 2003 NAG A O6  1 
HETATM 7054 O O7  . NAG E 3 .   ? 22.472 98.850  15.879  1.00 35.09 ? 2003 NAG A O7  1 
HETATM 7055 C C1  . NAG F 3 .   ? 18.197 103.788 18.102  1.00 43.26 ? 2004 NAG A C1  1 
HETATM 7056 C C2  . NAG F 3 .   ? 16.703 104.040 18.410  1.00 46.90 ? 2004 NAG A C2  1 
HETATM 7057 C C3  . NAG F 3 .   ? 16.130 105.002 17.387  1.00 48.24 ? 2004 NAG A C3  1 
HETATM 7058 C C4  . NAG F 3 .   ? 16.885 106.328 17.464  1.00 49.37 ? 2004 NAG A C4  1 
HETATM 7059 C C5  . NAG F 3 .   ? 18.382 106.076 17.229  1.00 47.38 ? 2004 NAG A C5  1 
HETATM 7060 C C6  . NAG F 3 .   ? 19.186 107.334 17.528  1.00 48.46 ? 2004 NAG A C6  1 
HETATM 7061 C C7  . NAG F 3 .   ? 15.044 102.509 19.431  1.00 49.17 ? 2004 NAG A C7  1 
HETATM 7062 C C8  . NAG F 3 .   ? 14.301 101.216 19.250  1.00 49.47 ? 2004 NAG A C8  1 
HETATM 7063 N N2  . NAG F 3 .   ? 15.859 102.851 18.423  1.00 47.99 ? 2004 NAG A N2  1 
HETATM 7064 O O3  . NAG F 3 .   ? 14.771 105.178 17.703  1.00 51.64 ? 2004 NAG A O3  1 
HETATM 7065 O O4  . NAG F 3 .   ? 16.340 107.285 16.551  1.00 52.64 ? 2004 NAG A O4  1 
HETATM 7066 O O5  . NAG F 3 .   ? 18.894 105.022 18.056  1.00 45.11 ? 2004 NAG A O5  1 
HETATM 7067 O O6  . NAG F 3 .   ? 20.521 107.149 17.093  1.00 46.92 ? 2004 NAG A O6  1 
HETATM 7068 O O7  . NAG F 3 .   ? 14.885 103.169 20.463  1.00 50.17 ? 2004 NAG A O7  1 
HETATM 7069 C C1  . NAG G 3 .   ? 51.026 77.306  26.610  1.00 53.59 ? 2005 NAG A C1  1 
HETATM 7070 C C2  . NAG G 3 .   ? 52.240 77.606  27.507  1.00 58.51 ? 2005 NAG A C2  1 
HETATM 7071 C C3  . NAG G 3 .   ? 52.193 76.824  28.821  1.00 60.77 ? 2005 NAG A C3  1 
HETATM 7072 C C4  . NAG G 3 .   ? 50.823 76.765  29.509  1.00 61.18 ? 2005 NAG A C4  1 
HETATM 7073 C C5  . NAG G 3 .   ? 49.587 76.896  28.623  1.00 60.73 ? 2005 NAG A C5  1 
HETATM 7074 C C6  . NAG G 3 .   ? 48.630 77.781  29.424  1.00 62.58 ? 2005 NAG A C6  1 
HETATM 7075 C C7  . NAG G 3 .   ? 54.629 78.037  26.929  1.00 59.25 ? 2005 NAG A C7  1 
HETATM 7076 C C8  . NAG G 3 .   ? 55.897 77.301  26.573  1.00 58.43 ? 2005 NAG A C8  1 
HETATM 7077 N N2  . NAG G 3 .   ? 53.495 77.324  26.813  1.00 58.59 ? 2005 NAG A N2  1 
HETATM 7078 O O3  . NAG G 3 .   ? 53.123 77.426  29.704  1.00 62.37 ? 2005 NAG A O3  1 
HETATM 7079 O O4  . NAG G 3 .   ? 50.694 75.554  30.225  1.00 63.34 ? 2005 NAG A O4  1 
HETATM 7080 O O5  . NAG G 3 .   ? 49.796 77.469  27.331  1.00 57.41 ? 2005 NAG A O5  1 
HETATM 7081 O O6  . NAG G 3 .   ? 47.290 77.456  29.123  1.00 65.58 ? 2005 NAG A O6  1 
HETATM 7082 O O7  . NAG G 3 .   ? 54.680 79.216  27.306  1.00 58.51 ? 2005 NAG A O7  1 
HETATM 7083 O O   . HOH H 4 .   ? 43.935 101.488 20.614  1.00 17.17 ? 876  HOH A O   1 
HETATM 7084 O O   . HOH H 4 .   ? 50.492 97.551  11.659  1.00 13.95 ? 877  HOH A O   1 
HETATM 7085 O O   . HOH H 4 .   ? 59.902 110.249 45.023  1.00 18.27 ? 878  HOH A O   1 
HETATM 7086 O O   . HOH H 4 .   ? 50.188 103.595 15.596  1.00 17.94 ? 879  HOH A O   1 
HETATM 7087 O O   . HOH H 4 .   ? 57.794 99.549  31.626  1.00 15.15 ? 880  HOH A O   1 
HETATM 7088 O O   . HOH H 4 .   ? 55.209 125.082 24.262  1.00 23.33 ? 881  HOH A O   1 
HETATM 7089 O O   . HOH H 4 .   ? 65.229 110.302 16.005  1.00 16.71 ? 882  HOH A O   1 
HETATM 7090 O O   . HOH H 4 .   ? 47.988 95.966  21.401  1.00 14.22 ? 883  HOH A O   1 
HETATM 7091 O O   . HOH H 4 .   ? 66.021 115.743 34.364  1.00 17.58 ? 884  HOH A O   1 
HETATM 7092 O O   . HOH H 4 .   ? 63.387 109.518 17.518  1.00 13.35 ? 885  HOH A O   1 
HETATM 7093 O O   . HOH H 4 .   ? 51.004 106.142 15.500  1.00 21.66 ? 886  HOH A O   1 
HETATM 7094 O O   . HOH H 4 .   ? 54.114 93.463  30.375  1.00 17.32 ? 887  HOH A O   1 
HETATM 7095 O O   . HOH H 4 .   ? 36.239 81.794  6.974   1.00 17.45 ? 888  HOH A O   1 
HETATM 7096 O O   . HOH H 4 .   ? 57.752 106.483 31.316  1.00 14.49 ? 889  HOH A O   1 
HETATM 7097 O O   . HOH H 4 .   ? 49.925 85.184  -4.154  1.00 18.34 ? 890  HOH A O   1 
HETATM 7098 O O   . HOH H 4 .   ? 67.846 103.586 9.558   1.00 14.65 ? 891  HOH A O   1 
HETATM 7099 O O   . HOH H 4 .   ? 63.677 96.548  12.227  1.00 24.54 ? 892  HOH A O   1 
HETATM 7100 O O   . HOH H 4 .   ? 64.803 103.347 -6.729  1.00 25.00 ? 893  HOH A O   1 
HETATM 7101 O O   . HOH H 4 .   ? 54.293 91.945  18.169  1.00 15.29 ? 894  HOH A O   1 
HETATM 7102 O O   . HOH H 4 .   ? 34.548 94.938  -2.846  1.00 26.37 ? 895  HOH A O   1 
HETATM 7103 O O   . HOH H 4 .   ? 78.433 98.011  13.270  1.00 19.80 ? 896  HOH A O   1 
HETATM 7104 O O   . HOH H 4 .   ? 52.276 85.494  21.084  1.00 16.35 ? 897  HOH A O   1 
HETATM 7105 O O   . HOH H 4 .   ? 49.499 70.375  2.776   1.00 19.91 ? 898  HOH A O   1 
HETATM 7106 O O   . HOH H 4 .   ? 38.584 95.286  4.567   1.00 15.53 ? 899  HOH A O   1 
HETATM 7107 O O   . HOH H 4 .   ? 58.513 84.024  12.630  1.00 19.76 ? 900  HOH A O   1 
HETATM 7108 O O   . HOH H 4 .   ? 59.925 91.161  14.636  1.00 16.28 ? 901  HOH A O   1 
HETATM 7109 O O   . HOH H 4 .   ? 69.715 94.918  15.752  1.00 20.38 ? 902  HOH A O   1 
HETATM 7110 O O   . HOH H 4 .   ? 53.486 98.420  32.458  1.00 18.86 ? 903  HOH A O   1 
HETATM 7111 O O   . HOH H 4 .   ? 33.774 90.829  5.351   1.00 20.41 ? 904  HOH A O   1 
HETATM 7112 O O   . HOH H 4 .   ? 57.757 91.018  29.494  1.00 19.35 ? 905  HOH A O   1 
HETATM 7113 O O   . HOH H 4 .   ? 53.878 95.586  43.947  1.00 19.42 ? 906  HOH A O   1 
HETATM 7114 O O   . HOH H 4 .   ? 41.901 97.802  18.520  1.00 15.45 ? 907  HOH A O   1 
HETATM 7115 O O   . HOH H 4 .   ? 30.623 99.189  35.789  1.00 21.50 ? 908  HOH A O   1 
HETATM 7116 O O   . HOH H 4 .   ? 47.070 96.488  11.698  1.00 21.94 ? 909  HOH A O   1 
HETATM 7117 O O   . HOH H 4 .   ? 72.043 91.931  26.646  1.00 20.84 ? 910  HOH A O   1 
HETATM 7118 O O   . HOH H 4 .   ? 45.469 78.332  1.770   1.00 17.72 ? 911  HOH A O   1 
HETATM 7119 O O   . HOH H 4 .   ? 40.141 97.617  4.451   1.00 18.58 ? 912  HOH A O   1 
HETATM 7120 O O   . HOH H 4 .   ? 53.501 97.432  45.895  1.00 20.78 ? 913  HOH A O   1 
HETATM 7121 O O   . HOH H 4 .   ? 36.569 97.880  43.269  1.00 25.24 ? 914  HOH A O   1 
HETATM 7122 O O   . HOH H 4 .   ? 52.428 76.433  -4.466  1.00 25.62 ? 915  HOH A O   1 
HETATM 7123 O O   . HOH H 4 .   ? 66.805 110.750 43.809  1.00 27.54 ? 916  HOH A O   1 
HETATM 7124 O O   . HOH H 4 .   ? 51.155 111.595 27.226  1.00 17.85 ? 917  HOH A O   1 
HETATM 7125 O O   . HOH H 4 .   ? 65.957 89.968  24.569  1.00 23.98 ? 918  HOH A O   1 
HETATM 7126 O O   . HOH H 4 .   ? 75.814 99.308  26.368  1.00 18.17 ? 919  HOH A O   1 
HETATM 7127 O O   . HOH H 4 .   ? 46.074 89.574  17.979  1.00 19.67 ? 920  HOH A O   1 
HETATM 7128 O O   . HOH H 4 .   ? 50.711 100.764 13.458  1.00 13.84 ? 921  HOH A O   1 
HETATM 7129 O O   . HOH H 4 .   ? 49.373 117.081 29.379  1.00 21.31 ? 922  HOH A O   1 
HETATM 7130 O O   . HOH H 4 .   ? 35.684 93.618  20.182  1.00 23.92 ? 923  HOH A O   1 
HETATM 7131 O O   . HOH H 4 .   ? 53.211 99.254  43.838  1.00 18.14 ? 924  HOH A O   1 
HETATM 7132 O O   . HOH H 4 .   ? 38.780 94.321  6.967   1.00 19.23 ? 925  HOH A O   1 
HETATM 7133 O O   . HOH H 4 .   ? 59.160 88.923  21.950  1.00 13.64 ? 926  HOH A O   1 
HETATM 7134 O O   . HOH H 4 .   ? 46.420 89.190  38.850  1.00 14.92 ? 927  HOH A O   1 
HETATM 7135 O O   . HOH H 4 .   ? 71.009 115.046 20.246  1.00 17.53 ? 928  HOH A O   1 
HETATM 7136 O O   . HOH H 4 .   ? 54.137 107.078 3.145   1.00 17.48 ? 929  HOH A O   1 
HETATM 7137 O O   . HOH H 4 .   ? 55.685 112.118 -3.968  1.00 27.40 ? 930  HOH A O   1 
HETATM 7138 O O   . HOH H 4 .   ? 54.300 90.169  40.005  1.00 15.63 ? 931  HOH A O   1 
HETATM 7139 O O   . HOH H 4 .   ? 51.382 83.822  23.418  1.00 24.51 ? 932  HOH A O   1 
HETATM 7140 O O   . HOH H 4 .   ? 54.293 97.253  41.785  1.00 18.06 ? 933  HOH A O   1 
HETATM 7141 O O   . HOH H 4 .   ? 58.609 111.667 43.591  1.00 23.08 ? 934  HOH A O   1 
HETATM 7142 O O   . HOH H 4 .   ? 45.834 60.543  1.769   1.00 40.20 ? 935  HOH A O   1 
HETATM 7143 O O   . HOH H 4 .   ? 49.459 103.897 -21.285 1.00 28.09 ? 936  HOH A O   1 
HETATM 7144 O O   . HOH H 4 .   ? 56.495 110.186 9.109   1.00 19.84 ? 937  HOH A O   1 
HETATM 7145 O O   . HOH H 4 .   ? 56.423 90.226  43.398  1.00 23.56 ? 938  HOH A O   1 
HETATM 7146 O O   . HOH H 4 .   ? 71.950 94.809  33.464  1.00 23.32 ? 939  HOH A O   1 
HETATM 7147 O O   . HOH H 4 .   ? 66.351 103.165 -4.784  1.00 20.21 ? 940  HOH A O   1 
HETATM 7148 O O   . HOH H 4 .   ? 45.096 105.486 0.624   1.00 24.68 ? 941  HOH A O   1 
HETATM 7149 O O   . HOH H 4 .   ? 69.379 94.277  33.318  1.00 17.26 ? 942  HOH A O   1 
HETATM 7150 O O   . HOH H 4 .   ? 64.086 117.038 33.269  1.00 19.95 ? 943  HOH A O   1 
HETATM 7151 O O   . HOH H 4 .   ? 87.111 98.363  26.540  1.00 45.51 ? 944  HOH A O   1 
HETATM 7152 O O   . HOH H 4 .   ? 64.267 121.017 40.571  1.00 29.79 ? 945  HOH A O   1 
HETATM 7153 O O   . HOH H 4 .   ? 39.847 97.810  -6.485  1.00 18.49 ? 946  HOH A O   1 
HETATM 7154 O O   . HOH H 4 .   ? 39.553 101.837 4.032   1.00 21.14 ? 947  HOH A O   1 
HETATM 7155 O O   . HOH H 4 .   ? 53.657 78.206  13.478  1.00 23.71 ? 948  HOH A O   1 
HETATM 7156 O O   . HOH H 4 .   ? 52.533 77.834  2.699   1.00 15.51 ? 949  HOH A O   1 
HETATM 7157 O O   . HOH H 4 .   ? 41.364 83.820  20.477  1.00 17.74 ? 950  HOH A O   1 
HETATM 7158 O O   . HOH H 4 .   ? 35.861 94.230  28.723  1.00 22.63 ? 951  HOH A O   1 
HETATM 7159 O O   . HOH H 4 .   ? 67.390 107.431 7.751   1.00 26.30 ? 952  HOH A O   1 
HETATM 7160 O O   . HOH H 4 .   ? 57.283 90.190  20.413  1.00 18.85 ? 953  HOH A O   1 
HETATM 7161 O O   . HOH H 4 .   ? 36.786 88.149  11.044  1.00 24.98 ? 954  HOH A O   1 
HETATM 7162 O O   . HOH H 4 .   ? 34.593 80.824  15.377  1.00 24.94 ? 955  HOH A O   1 
HETATM 7163 O O   . HOH H 4 .   ? 68.595 95.908  18.718  1.00 21.30 ? 956  HOH A O   1 
HETATM 7164 O O   . HOH H 4 .   ? 48.519 79.126  1.855   1.00 17.96 ? 957  HOH A O   1 
HETATM 7165 O O   . HOH H 4 .   ? 54.441 78.273  7.006   1.00 28.75 ? 958  HOH A O   1 
HETATM 7166 O O   . HOH H 4 .   ? 53.981 82.139  2.752   1.00 23.24 ? 959  HOH A O   1 
HETATM 7167 O O   . HOH H 4 .   ? 25.790 98.421  39.267  1.00 35.56 ? 960  HOH A O   1 
HETATM 7168 O O   . HOH H 4 .   ? 51.723 96.401  47.648  1.00 19.89 ? 961  HOH A O   1 
HETATM 7169 O O   . HOH H 4 .   ? 43.198 60.276  1.004   1.00 38.12 ? 962  HOH A O   1 
HETATM 7170 O O   . HOH H 4 .   ? 78.082 99.362  10.803  1.00 18.33 ? 963  HOH A O   1 
HETATM 7171 O O   . HOH H 4 .   ? 43.541 102.090 3.059   1.00 18.10 ? 964  HOH A O   1 
HETATM 7172 O O   . HOH H 4 .   ? 60.419 120.566 27.247  1.00 29.42 ? 965  HOH A O   1 
HETATM 7173 O O   . HOH H 4 .   ? 90.734 116.446 21.001  1.00 30.07 ? 966  HOH A O   1 
HETATM 7174 O O   . HOH H 4 .   ? 58.612 123.292 33.433  1.00 18.82 ? 967  HOH A O   1 
HETATM 7175 O O   . HOH H 4 .   ? 57.396 131.696 24.824  1.00 27.84 ? 968  HOH A O   1 
HETATM 7176 O O   . HOH H 4 .   ? 52.615 91.779  24.190  1.00 26.09 ? 969  HOH A O   1 
HETATM 7177 O O   . HOH H 4 .   ? 47.202 80.597  19.016  1.00 27.86 ? 970  HOH A O   1 
HETATM 7178 O O   . HOH H 4 .   ? 27.148 110.144 30.474  1.00 27.53 ? 971  HOH A O   1 
HETATM 7179 O O   . HOH H 4 .   ? 46.337 107.052 13.421  1.00 18.69 ? 972  HOH A O   1 
HETATM 7180 O O   . HOH H 4 .   ? 58.071 122.239 35.632  1.00 23.82 ? 973  HOH A O   1 
HETATM 7181 O O   . HOH H 4 .   ? 60.800 89.861  -3.385  1.00 22.20 ? 974  HOH A O   1 
HETATM 7182 O O   . HOH H 4 .   ? 66.443 88.636  16.305  1.00 22.51 ? 975  HOH A O   1 
HETATM 7183 O O   . HOH H 4 .   ? 35.102 97.420  35.488  1.00 21.86 ? 976  HOH A O   1 
HETATM 7184 O O   . HOH H 4 .   ? 33.828 100.106 19.986  1.00 21.25 ? 977  HOH A O   1 
HETATM 7185 O O   . HOH H 4 .   ? 68.144 96.258  -2.508  1.00 28.17 ? 978  HOH A O   1 
HETATM 7186 O O   . HOH H 4 .   ? 52.320 118.456 37.997  1.00 38.60 ? 979  HOH A O   1 
HETATM 7187 O O   . HOH H 4 .   ? 67.400 111.768 16.198  1.00 19.91 ? 980  HOH A O   1 
HETATM 7188 O O   . HOH H 4 .   ? 53.986 91.429  28.186  1.00 18.45 ? 981  HOH A O   1 
HETATM 7189 O O   . HOH H 4 .   ? 40.121 95.397  19.707  1.00 16.93 ? 982  HOH A O   1 
HETATM 7190 O O   . HOH H 4 .   ? 66.837 86.445  43.743  1.00 30.20 ? 983  HOH A O   1 
HETATM 7191 O O   . HOH H 4 .   ? 65.210 90.809  -7.086  1.00 24.46 ? 984  HOH A O   1 
HETATM 7192 O O   . HOH H 4 .   ? 48.869 80.483  25.691  1.00 35.63 ? 985  HOH A O   1 
HETATM 7193 O O   . HOH H 4 .   ? 50.690 111.851 11.031  1.00 23.30 ? 986  HOH A O   1 
HETATM 7194 O O   . HOH H 4 .   ? 54.821 117.535 31.737  1.00 32.93 ? 987  HOH A O   1 
HETATM 7195 O O   . HOH H 4 .   ? 60.948 124.439 33.042  1.00 17.93 ? 988  HOH A O   1 
HETATM 7196 O O   . HOH H 4 .   ? 76.875 101.171 33.400  1.00 33.93 ? 989  HOH A O   1 
HETATM 7197 O O   . HOH H 4 .   ? 32.954 99.068  34.760  1.00 20.13 ? 990  HOH A O   1 
HETATM 7198 O O   . HOH H 4 .   ? 56.111 87.786  27.956  1.00 27.26 ? 991  HOH A O   1 
HETATM 7199 O O   . HOH H 4 .   ? 79.052 106.400 14.238  1.00 24.61 ? 992  HOH A O   1 
HETATM 7200 O O   . HOH H 4 .   ? 66.814 112.621 41.996  1.00 28.55 ? 993  HOH A O   1 
HETATM 7201 O O   . HOH H 4 .   ? 65.397 105.487 -8.182  1.00 34.65 ? 994  HOH A O   1 
HETATM 7202 O O   . HOH H 4 .   ? 61.076 111.744 46.988  1.00 23.78 ? 995  HOH A O   1 
HETATM 7203 O O   . HOH H 4 .   ? 72.591 118.020 33.538  1.00 25.86 ? 996  HOH A O   1 
HETATM 7204 O O   . HOH H 4 .   ? 62.499 82.460  35.215  1.00 31.78 ? 997  HOH A O   1 
HETATM 7205 O O   . HOH H 4 .   ? 55.300 101.012 -12.819 1.00 21.87 ? 998  HOH A O   1 
HETATM 7206 O O   . HOH H 4 .   ? 52.597 76.882  5.162   1.00 22.19 ? 999  HOH A O   1 
HETATM 7207 O O   . HOH H 4 .   ? 70.906 103.024 1.615   1.00 26.21 ? 1000 HOH A O   1 
HETATM 7208 O O   . HOH H 4 .   ? 46.040 88.739  29.562  1.00 22.24 ? 1002 HOH A O   1 
HETATM 7209 O O   . HOH H 4 .   ? 59.659 65.281  7.589   1.00 53.25 ? 1003 HOH A O   1 
HETATM 7210 O O   . HOH H 4 .   ? 50.097 77.102  5.604   1.00 27.93 ? 1004 HOH A O   1 
HETATM 7211 O O   . HOH H 4 .   ? 31.042 81.274  28.460  1.00 26.18 ? 1005 HOH A O   1 
HETATM 7212 O O   . HOH H 4 .   ? 26.336 95.725  24.867  1.00 21.05 ? 1006 HOH A O   1 
HETATM 7213 O O   . HOH H 4 .   ? 56.221 117.640 34.464  1.00 30.48 ? 1007 HOH A O   1 
HETATM 7214 O O   . HOH H 4 .   ? 55.709 83.194  22.084  1.00 25.06 ? 1008 HOH A O   1 
HETATM 7215 O O   . HOH H 4 .   ? 46.241 74.429  -7.506  1.00 40.60 ? 1009 HOH A O   1 
HETATM 7216 O O   . HOH H 4 .   ? 54.077 83.338  42.895  1.00 35.85 ? 1010 HOH A O   1 
HETATM 7217 O O   . HOH H 4 .   ? 30.378 94.944  8.912   1.00 22.49 ? 1011 HOH A O   1 
HETATM 7218 O O   . HOH H 4 .   ? 81.615 106.942 16.245  1.00 28.78 ? 1012 HOH A O   1 
HETATM 7219 O O   . HOH H 4 .   ? 46.577 115.738 32.588  1.00 23.86 ? 1013 HOH A O   1 
HETATM 7220 O O   . HOH H 4 .   ? 64.035 104.305 -1.412  1.00 23.79 ? 1014 HOH A O   1 
HETATM 7221 O O   . HOH H 4 .   ? 45.877 109.157 3.624   1.00 24.93 ? 1015 HOH A O   1 
HETATM 7222 O O   . HOH H 4 .   ? 68.802 115.165 21.677  1.00 19.84 ? 1016 HOH A O   1 
HETATM 7223 O O   . HOH H 4 .   ? 48.630 83.125  25.049  1.00 30.83 ? 1017 HOH A O   1 
HETATM 7224 O O   . HOH H 4 .   ? 82.645 99.841  29.114  1.00 46.40 ? 1018 HOH A O   1 
HETATM 7225 O O   . HOH H 4 .   ? 33.020 88.238  4.888   1.00 21.23 ? 1019 HOH A O   1 
HETATM 7226 O O   . HOH H 4 .   ? 43.477 92.463  11.388  1.00 27.64 ? 1020 HOH A O   1 
HETATM 7227 O O   . HOH H 4 .   ? 58.402 103.566 -12.284 1.00 43.61 ? 1021 HOH A O   1 
HETATM 7228 O O   . HOH H 4 .   ? 48.516 82.871  -1.845  1.00 17.59 ? 1022 HOH A O   1 
HETATM 7229 O O   . HOH H 4 .   ? 49.316 77.974  8.411   1.00 21.37 ? 1023 HOH A O   1 
HETATM 7230 O O   . HOH H 4 .   ? 68.902 87.789  45.198  1.00 33.56 ? 1024 HOH A O   1 
HETATM 7231 O O   . HOH H 4 .   ? 45.890 77.687  10.186  1.00 36.94 ? 1025 HOH A O   1 
HETATM 7232 O O   . HOH H 4 .   ? 55.939 109.300 0.795   1.00 23.38 ? 1026 HOH A O   1 
HETATM 7233 O O   . HOH H 4 .   ? 50.340 112.749 15.968  1.00 29.17 ? 1027 HOH A O   1 
HETATM 7234 O O   . HOH H 4 .   ? 45.456 99.935  42.466  1.00 26.17 ? 1028 HOH A O   1 
HETATM 7235 O O   . HOH H 4 .   ? 47.727 109.444 5.595   1.00 21.81 ? 1029 HOH A O   1 
HETATM 7236 O O   . HOH H 4 .   ? 57.176 113.417 45.035  1.00 23.79 ? 1030 HOH A O   1 
HETATM 7237 O O   . HOH H 4 .   ? 73.975 105.083 11.563  1.00 23.54 ? 1031 HOH A O   1 
HETATM 7238 O O   . HOH H 4 .   ? 66.099 93.267  48.939  1.00 30.73 ? 1032 HOH A O   1 
HETATM 7239 O O   . HOH H 4 .   ? 58.229 125.006 30.447  1.00 23.31 ? 1033 HOH A O   1 
HETATM 7240 O O   . HOH H 4 .   ? 72.610 88.435  29.592  1.00 24.30 ? 1034 HOH A O   1 
HETATM 7241 O O   . HOH H 4 .   ? 61.658 103.983 52.037  1.00 31.46 ? 1035 HOH A O   1 
HETATM 7242 O O   . HOH H 4 .   ? 64.290 129.424 29.735  1.00 34.34 ? 1036 HOH A O   1 
HETATM 7243 O O   . HOH H 4 .   ? 62.560 81.717  32.711  1.00 28.69 ? 1037 HOH A O   1 
HETATM 7244 O O   . HOH H 4 .   ? 35.383 95.903  30.770  1.00 23.22 ? 1038 HOH A O   1 
HETATM 7245 O O   . HOH H 4 .   ? 54.892 91.624  50.105  1.00 28.17 ? 1039 HOH A O   1 
HETATM 7246 O O   . HOH H 4 .   ? 40.827 95.929  34.090  1.00 23.69 ? 1040 HOH A O   1 
HETATM 7247 O O   . HOH H 4 .   ? 49.282 93.921  32.927  1.00 21.49 ? 1041 HOH A O   1 
HETATM 7248 O O   . HOH H 4 .   ? 50.181 111.531 8.345   1.00 17.74 ? 1042 HOH A O   1 
HETATM 7249 O O   . HOH H 4 .   ? 55.956 120.394 34.194  1.00 30.98 ? 1043 HOH A O   1 
HETATM 7250 O O   . HOH H 4 .   ? 71.016 130.726 15.933  1.00 37.23 ? 1044 HOH A O   1 
HETATM 7251 O O   . HOH H 4 .   ? 50.847 80.067  2.481   1.00 23.21 ? 1045 HOH A O   1 
HETATM 7252 O O   . HOH H 4 .   ? 71.815 88.586  36.810  1.00 36.85 ? 1046 HOH A O   1 
HETATM 7253 O O   . HOH H 4 .   ? 67.456 91.540  15.272  1.00 43.05 ? 1047 HOH A O   1 
HETATM 7254 O O   . HOH H 4 .   ? 80.190 98.616  9.534   1.00 26.95 ? 1048 HOH A O   1 
HETATM 7255 O O   . HOH H 4 .   ? 76.141 89.501  16.658  1.00 31.91 ? 1049 HOH A O   1 
HETATM 7256 O O   . HOH H 4 .   ? 68.340 82.982  32.842  1.00 26.88 ? 1050 HOH A O   1 
HETATM 7257 O O   . HOH H 4 .   ? 86.785 109.858 26.834  1.00 25.29 ? 1051 HOH A O   1 
HETATM 7258 O O   . HOH H 4 .   ? 54.314 85.401  30.258  1.00 24.14 ? 1052 HOH A O   1 
HETATM 7259 O O   . HOH H 4 .   ? 71.774 127.948 24.255  1.00 25.63 ? 1053 HOH A O   1 
HETATM 7260 O O   . HOH H 4 .   ? 38.685 85.009  20.538  1.00 25.88 ? 1054 HOH A O   1 
HETATM 7261 O O   . HOH H 4 .   ? 39.128 88.035  21.694  1.00 37.85 ? 1055 HOH A O   1 
HETATM 7262 O O   . HOH H 4 .   ? 30.383 90.673  2.222   1.00 34.24 ? 1056 HOH A O   1 
HETATM 7263 O O   . HOH H 4 .   ? 42.947 66.737  4.234   1.00 19.01 ? 1057 HOH A O   1 
HETATM 7264 O O   . HOH H 4 .   ? 36.268 104.818 36.434  1.00 27.32 ? 1058 HOH A O   1 
HETATM 7265 O O   . HOH H 4 .   ? 39.352 87.812  40.065  1.00 36.43 ? 1059 HOH A O   1 
HETATM 7266 O O   . HOH H 4 .   ? 57.584 105.104 16.641  1.00 22.78 ? 1060 HOH A O   1 
HETATM 7267 O O   . HOH H 4 .   ? 49.013 117.004 31.944  1.00 26.39 ? 1061 HOH A O   1 
HETATM 7268 O O   . HOH H 4 .   ? 68.150 94.090  46.987  1.00 22.22 ? 1062 HOH A O   1 
HETATM 7269 O O   . HOH H 4 .   ? 39.425 88.580  24.442  1.00 16.27 ? 1063 HOH A O   1 
HETATM 7270 O O   . HOH H 4 .   ? 61.382 122.172 13.487  1.00 34.53 ? 1064 HOH A O   1 
HETATM 7271 O O   . HOH H 4 .   ? 41.765 103.204 53.205  1.00 30.16 ? 1065 HOH A O   1 
HETATM 7272 O O   . HOH H 4 .   ? 88.997 107.247 27.073  1.00 26.47 ? 1066 HOH A O   1 
HETATM 7273 O O   . HOH H 4 .   ? 57.114 90.986  24.623  1.00 23.84 ? 1067 HOH A O   1 
HETATM 7274 O O   . HOH H 4 .   ? 40.141 99.434  2.790   1.00 24.12 ? 1068 HOH A O   1 
HETATM 7275 O O   . HOH H 4 .   ? 95.708 116.559 25.895  1.00 29.21 ? 1069 HOH A O   1 
HETATM 7276 O O   . HOH H 4 .   ? 26.981 94.259  37.024  1.00 32.41 ? 1070 HOH A O   1 
HETATM 7277 O O   . HOH H 4 .   ? 41.775 94.475  -17.232 1.00 28.09 ? 1071 HOH A O   1 
HETATM 7278 O O   . HOH H 4 .   ? 69.824 126.681 23.494  1.00 28.93 ? 1072 HOH A O   1 
HETATM 7279 O O   . HOH H 4 .   ? 41.590 77.433  14.794  1.00 29.66 ? 1073 HOH A O   1 
HETATM 7280 O O   . HOH H 4 .   ? 51.042 112.027 -5.819  1.00 36.53 ? 1074 HOH A O   1 
HETATM 7281 O O   . HOH H 4 .   ? 64.525 92.616  -11.339 1.00 47.52 ? 1075 HOH A O   1 
HETATM 7282 O O   . HOH H 4 .   ? 49.868 97.193  49.184  1.00 31.37 ? 1076 HOH A O   1 
HETATM 7283 O O   . HOH H 4 .   ? 32.261 92.272  3.489   1.00 21.81 ? 1077 HOH A O   1 
HETATM 7284 O O   . HOH H 4 .   ? 34.792 97.184  -1.351  1.00 33.25 ? 1078 HOH A O   1 
HETATM 7285 O O   . HOH H 4 .   ? 62.213 99.955  16.724  1.00 26.34 ? 1079 HOH A O   1 
HETATM 7286 O O   . HOH H 4 .   ? 62.001 110.464 -5.739  1.00 36.18 ? 1080 HOH A O   1 
HETATM 7287 O O   . HOH H 4 .   ? 19.530 98.876  14.781  1.00 48.91 ? 1081 HOH A O   1 
HETATM 7288 O O   . HOH H 4 .   ? 42.931 117.724 25.323  1.00 24.27 ? 1082 HOH A O   1 
HETATM 7289 O O   . HOH H 4 .   ? 53.048 126.503 25.001  1.00 33.17 ? 1083 HOH A O   1 
HETATM 7290 O O   . HOH H 4 .   ? 74.030 92.696  1.691   1.00 32.28 ? 1084 HOH A O   1 
HETATM 7291 O O   . HOH H 4 .   ? 41.434 88.790  39.160  1.00 27.72 ? 1085 HOH A O   1 
HETATM 7292 O O   . HOH H 4 .   ? 63.951 104.999 52.389  1.00 31.89 ? 1086 HOH A O   1 
HETATM 7293 O O   . HOH H 4 .   ? 30.570 109.482 35.670  1.00 23.83 ? 1087 HOH A O   1 
HETATM 7294 O O   . HOH H 4 .   ? 31.683 107.045 43.925  1.00 31.62 ? 1088 HOH A O   1 
HETATM 7295 O O   . HOH H 4 .   ? 61.052 116.788 42.898  1.00 26.02 ? 1089 HOH A O   1 
HETATM 7296 O O   . HOH H 4 .   ? 44.275 77.166  21.195  1.00 30.43 ? 1090 HOH A O   1 
HETATM 7297 O O   . HOH H 4 .   ? 35.329 116.296 24.048  1.00 33.93 ? 1091 HOH A O   1 
HETATM 7298 O O   . HOH H 4 .   ? 70.260 134.158 19.780  1.00 50.97 ? 1092 HOH A O   1 
HETATM 7299 O O   . HOH H 4 .   ? 78.800 125.820 36.311  1.00 33.57 ? 1093 HOH A O   1 
HETATM 7300 O O   . HOH H 4 .   ? 70.922 113.230 18.322  1.00 24.99 ? 1094 HOH A O   1 
HETATM 7301 O O   . HOH H 4 .   ? 85.210 121.892 35.749  1.00 28.33 ? 1095 HOH A O   1 
HETATM 7302 O O   . HOH H 4 .   ? 43.227 77.493  16.899  1.00 31.43 ? 1096 HOH A O   1 
HETATM 7303 O O   . HOH H 4 .   ? 34.458 96.101  33.461  1.00 27.97 ? 1097 HOH A O   1 
HETATM 7304 O O   . HOH H 4 .   ? 54.959 78.570  -5.620  1.00 27.98 ? 1098 HOH A O   1 
HETATM 7305 O O   . HOH H 4 .   ? 54.919 111.622 1.545   1.00 33.30 ? 1099 HOH A O   1 
HETATM 7306 O O   . HOH H 4 .   ? 47.716 112.628 24.221  1.00 35.89 ? 1100 HOH A O   1 
HETATM 7307 O O   . HOH H 4 .   ? 32.812 114.762 23.463  1.00 36.97 ? 1101 HOH A O   1 
HETATM 7308 O O   . HOH H 4 .   ? 39.996 111.621 19.113  1.00 28.62 ? 1102 HOH A O   1 
HETATM 7309 O O   . HOH H 4 .   ? 30.040 95.213  41.092  1.00 28.23 ? 1103 HOH A O   1 
HETATM 7310 O O   . HOH H 4 .   ? 24.553 88.537  18.579  1.00 25.39 ? 1104 HOH A O   1 
HETATM 7311 O O   . HOH H 4 .   ? 60.175 84.960  14.987  1.00 33.95 ? 1105 HOH A O   1 
HETATM 7312 O O   . HOH H 4 .   ? 55.047 127.915 29.683  1.00 31.04 ? 1106 HOH A O   1 
HETATM 7313 O O   . HOH H 4 .   ? 38.968 101.762 -9.082  1.00 38.32 ? 1107 HOH A O   1 
HETATM 7314 O O   . HOH H 4 .   ? 55.007 91.528  23.016  1.00 27.80 ? 1108 HOH A O   1 
HETATM 7315 O O   . HOH H 4 .   ? 79.941 97.523  40.425  1.00 43.95 ? 1109 HOH A O   1 
HETATM 7316 O O   . HOH H 4 .   ? 39.292 76.257  10.118  1.00 28.86 ? 1110 HOH A O   1 
HETATM 7317 O O   . HOH H 4 .   ? 39.224 76.107  14.776  1.00 32.15 ? 1111 HOH A O   1 
HETATM 7318 O O   . HOH H 4 .   ? 52.943 77.352  9.704   1.00 22.10 ? 1112 HOH A O   1 
HETATM 7319 O O   . HOH H 4 .   ? 49.483 86.249  -7.720  1.00 27.71 ? 1113 HOH A O   1 
HETATM 7320 O O   . HOH H 4 .   ? 44.283 118.044 43.415  1.00 26.95 ? 1114 HOH A O   1 
HETATM 7321 O O   . HOH H 4 .   ? 42.597 110.129 -8.824  1.00 31.99 ? 1115 HOH A O   1 
HETATM 7322 O O   . HOH H 4 .   ? 38.783 99.863  55.113  1.00 36.31 ? 1116 HOH A O   1 
HETATM 7323 O O   . HOH H 4 .   ? 22.418 91.182  40.634  1.00 39.69 ? 1117 HOH A O   1 
HETATM 7324 O O   . HOH H 4 .   ? 56.049 81.548  41.701  1.00 38.36 ? 1118 HOH A O   1 
HETATM 7325 O O   . HOH H 4 .   ? 47.157 92.127  46.402  1.00 23.74 ? 1119 HOH A O   1 
HETATM 7326 O O   . HOH H 4 .   ? 30.914 116.804 28.486  1.00 49.06 ? 1120 HOH A O   1 
HETATM 7327 O O   . HOH H 4 .   ? 49.597 111.213 4.586   1.00 32.98 ? 1121 HOH A O   1 
HETATM 7328 O O   . HOH H 4 .   ? 70.950 105.299 44.567  1.00 30.12 ? 1122 HOH A O   1 
HETATM 7329 O O   . HOH H 4 .   ? 61.540 130.864 14.927  1.00 36.64 ? 1123 HOH A O   1 
HETATM 7330 O O   . HOH H 4 .   ? 80.451 113.897 13.879  1.00 28.48 ? 1124 HOH A O   1 
HETATM 7331 O O   . HOH H 4 .   ? 33.737 112.668 46.560  1.00 35.63 ? 1125 HOH A O   1 
HETATM 7332 O O   . HOH H 4 .   ? 35.413 90.738  39.575  1.00 49.41 ? 1126 HOH A O   1 
HETATM 7333 O O   . HOH H 4 .   ? 81.217 97.513  30.394  1.00 48.27 ? 1127 HOH A O   1 
HETATM 7334 O O   . HOH H 4 .   ? 65.756 108.400 12.457  1.00 30.92 ? 1128 HOH A O   1 
HETATM 7335 O O   . HOH H 4 .   ? 32.326 71.204  -6.455  1.00 32.97 ? 1129 HOH A O   1 
HETATM 7336 O O   . HOH H 4 .   ? 61.056 116.878 12.737  1.00 25.20 ? 1130 HOH A O   1 
HETATM 7337 O O   . HOH H 4 .   ? 83.195 89.275  16.852  1.00 35.01 ? 1131 HOH A O   1 
HETATM 7338 O O   . HOH H 4 .   ? 73.581 91.350  22.011  1.00 34.27 ? 1132 HOH A O   1 
HETATM 7339 O O   . HOH H 4 .   ? 29.869 91.715  -0.792  1.00 24.86 ? 1133 HOH A O   1 
HETATM 7340 O O   . HOH H 4 .   ? 63.252 99.536  54.751  1.00 38.35 ? 1134 HOH A O   1 
HETATM 7341 O O   . HOH H 4 .   ? 22.721 89.258  25.439  1.00 35.53 ? 1135 HOH A O   1 
HETATM 7342 O O   . HOH H 4 .   ? 73.596 100.729 40.360  1.00 29.59 ? 1136 HOH A O   1 
HETATM 7343 O O   . HOH H 4 .   ? 48.442 114.391 22.422  1.00 40.75 ? 1137 HOH A O   1 
HETATM 7344 O O   . HOH H 4 .   ? 53.320 106.126 21.747  1.00 29.56 ? 1138 HOH A O   1 
HETATM 7345 O O   . HOH H 4 .   ? 85.137 89.779  25.265  1.00 49.75 ? 1139 HOH A O   1 
HETATM 7346 O O   . HOH H 4 .   ? 76.364 91.650  3.824   1.00 35.98 ? 1140 HOH A O   1 
HETATM 7347 O O   . HOH H 4 .   ? 50.300 115.056 20.508  1.00 33.11 ? 1141 HOH A O   1 
HETATM 7348 O O   . HOH H 4 .   ? 81.158 123.999 15.237  1.00 39.72 ? 1142 HOH A O   1 
HETATM 7349 O O   . HOH H 4 .   ? 62.006 73.520  5.065   1.00 31.60 ? 1143 HOH A O   1 
HETATM 7350 O O   . HOH H 4 .   ? 63.766 130.404 23.741  1.00 45.51 ? 1144 HOH A O   1 
HETATM 7351 O O   . HOH H 4 .   ? 31.714 90.124  -2.240  1.00 24.14 ? 1145 HOH A O   1 
HETATM 7352 O O   . HOH H 4 .   ? 32.691 99.360  4.608   1.00 33.91 ? 1146 HOH A O   1 
HETATM 7353 O O   . HOH H 4 .   ? 36.799 84.071  31.781  1.00 56.38 ? 1147 HOH A O   1 
HETATM 7354 O O   . HOH H 4 .   ? 57.748 112.487 -2.145  1.00 49.85 ? 1148 HOH A O   1 
HETATM 7355 O O   . HOH H 4 .   ? 60.318 87.674  15.128  1.00 31.81 ? 1149 HOH A O   1 
HETATM 7356 O O   . HOH H 4 .   ? 64.261 83.223  26.537  1.00 42.99 ? 1150 HOH A O   1 
HETATM 7357 O O   . HOH H 4 .   ? 35.088 79.539  23.010  1.00 34.24 ? 1151 HOH A O   1 
HETATM 7358 O O   . HOH H 4 .   ? 60.779 116.705 10.071  1.00 39.03 ? 1152 HOH A O   1 
HETATM 7359 O O   . HOH H 4 .   ? 78.758 85.825  35.306  1.00 38.72 ? 1153 HOH A O   1 
HETATM 7360 O O   . HOH H 4 .   ? 21.075 90.900  24.025  1.00 31.84 ? 1154 HOH A O   1 
HETATM 7361 O O   . HOH H 4 .   ? 20.057 93.992  27.106  1.00 41.10 ? 1155 HOH A O   1 
HETATM 7362 O O   . HOH H 4 .   ? 47.449 109.477 -0.219  1.00 44.54 ? 1156 HOH A O   1 
HETATM 7363 O O   . HOH H 4 .   ? 52.854 111.771 47.331  1.00 30.29 ? 1157 HOH A O   1 
HETATM 7364 O O   . HOH H 4 .   ? 56.665 125.116 32.369  1.00 32.87 ? 1158 HOH A O   1 
HETATM 7365 O O   . HOH H 4 .   ? 30.327 87.334  5.055   1.00 37.38 ? 1159 HOH A O   1 
HETATM 7366 O O   . HOH H 4 .   ? 64.221 75.072  5.635   1.00 35.49 ? 1160 HOH A O   1 
HETATM 7367 O O   . HOH H 4 .   ? 53.054 74.245  5.826   1.00 24.77 ? 1161 HOH A O   1 
HETATM 7368 O O   . HOH H 4 .   ? 53.328 96.642  52.039  1.00 41.26 ? 1162 HOH A O   1 
HETATM 7369 O O   . HOH H 4 .   ? 65.927 108.948 9.048   1.00 46.01 ? 1163 HOH A O   1 
HETATM 7370 O O   . HOH H 4 .   ? 67.286 113.305 20.630  1.00 27.22 ? 1164 HOH A O   1 
HETATM 7371 O O   . HOH H 4 .   ? 61.484 84.135  -2.387  1.00 32.04 ? 1165 HOH A O   1 
HETATM 7372 O O   . HOH H 4 .   ? 31.633 78.813  26.014  1.00 32.43 ? 1166 HOH A O   1 
HETATM 7373 O O   . HOH H 4 .   ? 45.684 111.416 22.932  1.00 22.34 ? 1167 HOH A O   1 
HETATM 7374 O O   . HOH H 4 .   ? 72.894 113.264 36.500  1.00 37.71 ? 1168 HOH A O   1 
HETATM 7375 O O   . HOH H 4 .   ? 51.343 82.561  43.055  1.00 51.37 ? 1169 HOH A O   1 
HETATM 7376 O O   . HOH H 4 .   ? 45.910 112.495 -2.235  1.00 49.48 ? 1170 HOH A O   1 
HETATM 7377 O O   . HOH H 4 .   ? 60.292 104.370 54.376  1.00 40.66 ? 1171 HOH A O   1 
HETATM 7378 O O   . HOH H 4 .   ? 25.830 102.433 18.443  1.00 27.49 ? 1172 HOH A O   1 
HETATM 7379 O O   . HOH H 4 .   ? 71.947 97.567  -5.239  1.00 44.30 ? 1173 HOH A O   1 
HETATM 7380 O O   . HOH H 4 .   ? 23.089 92.787  36.604  1.00 43.97 ? 1174 HOH A O   1 
HETATM 7381 O O   . HOH H 4 .   ? 86.567 118.983 19.208  1.00 27.13 ? 1175 HOH A O   1 
HETATM 7382 O O   . HOH H 4 .   ? 71.049 93.585  49.203  1.00 33.31 ? 1176 HOH A O   1 
HETATM 7383 O O   . HOH H 4 .   ? 51.171 126.836 23.419  1.00 33.28 ? 1177 HOH A O   1 
HETATM 7384 O O   . HOH H 4 .   ? 41.033 113.977 54.361  1.00 48.14 ? 1178 HOH A O   1 
HETATM 7385 O O   . HOH H 4 .   ? 64.618 91.148  48.862  1.00 35.49 ? 1179 HOH A O   1 
HETATM 7386 O O   . HOH H 4 .   ? 65.308 81.000  32.358  1.00 35.61 ? 1180 HOH A O   1 
HETATM 7387 O O   . HOH H 4 .   ? 37.999 98.440  47.153  1.00 25.78 ? 1181 HOH A O   1 
HETATM 7388 O O   . HOH H 4 .   ? 68.043 104.886 -3.678  1.00 40.24 ? 1182 HOH A O   1 
HETATM 7389 O O   . HOH H 4 .   ? 79.032 101.943 11.350  1.00 34.91 ? 1183 HOH A O   1 
HETATM 7390 O O   . HOH H 4 .   ? 39.414 102.635 -14.588 1.00 39.28 ? 1184 HOH A O   1 
HETATM 7391 O O   . HOH H 4 .   ? 50.653 59.392  -2.291  1.00 37.97 ? 1185 HOH A O   1 
HETATM 7392 O O   . HOH H 4 .   ? 61.426 72.075  7.094   1.00 31.21 ? 1186 HOH A O   1 
HETATM 7393 O O   . HOH H 4 .   ? 59.304 93.131  48.189  1.00 29.00 ? 1187 HOH A O   1 
HETATM 7394 O O   . HOH H 4 .   ? 55.688 115.471 37.766  1.00 29.69 ? 1188 HOH A O   1 
HETATM 7395 O O   . HOH H 4 .   ? 20.847 95.218  30.141  1.00 43.24 ? 1189 HOH A O   1 
HETATM 7396 O O   . HOH H 4 .   ? 56.460 67.669  4.744   1.00 29.33 ? 1190 HOH A O   1 
HETATM 7397 O O   . HOH H 4 .   ? 62.286 122.700 41.893  1.00 33.89 ? 1191 HOH A O   1 
HETATM 7398 O O   . HOH H 4 .   ? 39.562 95.490  46.749  1.00 37.16 ? 1192 HOH A O   1 
HETATM 7399 O O   . HOH H 4 .   ? 23.954 101.492 20.058  1.00 24.00 ? 1193 HOH A O   1 
HETATM 7400 O O   . HOH H 4 .   ? 54.101 117.253 36.467  1.00 32.70 ? 1194 HOH A O   1 
HETATM 7401 O O   . HOH H 4 .   ? 48.646 118.018 38.815  1.00 46.80 ? 1195 HOH A O   1 
HETATM 7402 O O   . HOH H 4 .   ? 22.009 82.977  13.582  1.00 30.49 ? 1196 HOH A O   1 
HETATM 7403 O O   . HOH H 4 .   ? 77.015 109.293 12.792  1.00 47.92 ? 1197 HOH A O   1 
HETATM 7404 O O   . HOH H 4 .   ? 45.510 112.249 20.435  1.00 38.56 ? 1198 HOH A O   1 
HETATM 7405 O O   . HOH H 4 .   ? 54.976 114.389 -7.751  1.00 45.52 ? 1199 HOH A O   1 
HETATM 7406 O O   . HOH H 4 .   ? 65.542 86.061  -1.209  1.00 31.27 ? 1200 HOH A O   1 
HETATM 7407 O O   . HOH H 4 .   ? 56.540 100.518 54.391  1.00 44.70 ? 1201 HOH A O   1 
HETATM 7408 O O   . HOH H 4 .   ? 37.519 98.319  -14.953 1.00 51.91 ? 1202 HOH A O   1 
HETATM 7409 O O   . HOH H 4 .   ? 50.223 70.528  5.525   1.00 47.33 ? 1203 HOH A O   1 
HETATM 7410 O O   . HOH H 4 .   ? 37.786 72.396  -5.830  1.00 53.06 ? 1204 HOH A O   1 
HETATM 7411 O O   . HOH H 4 .   ? 52.488 69.091  5.359   1.00 29.40 ? 1205 HOH A O   1 
HETATM 7412 O O   . HOH H 4 .   ? 67.011 87.939  24.751  1.00 49.68 ? 1206 HOH A O   1 
HETATM 7413 O O   . HOH H 4 .   ? 46.578 78.434  20.502  1.00 36.62 ? 1207 HOH A O   1 
HETATM 7414 O O   . HOH H 4 .   ? 61.027 82.310  -4.477  1.00 46.76 ? 1208 HOH A O   1 
HETATM 7415 O O   . HOH H 4 .   ? 72.481 97.233  -2.527  1.00 33.04 ? 1209 HOH A O   1 
HETATM 7416 O O   . HOH H 4 .   ? 63.079 71.866  2.936   1.00 32.89 ? 1210 HOH A O   1 
HETATM 7417 O O   . HOH H 4 .   ? 71.592 105.963 8.217   1.00 29.50 ? 1211 HOH A O   1 
HETATM 7418 O O   . HOH H 4 .   ? 41.568 103.392 4.095   1.00 25.09 ? 1212 HOH A O   1 
HETATM 7419 O O   . HOH H 4 .   ? 22.234 100.385 22.775  1.00 29.49 ? 1213 HOH A O   1 
HETATM 7420 O O   . HOH H 4 .   ? 60.586 119.911 12.384  1.00 56.48 ? 1214 HOH A O   1 
HETATM 7421 O O   . HOH H 4 .   ? 90.824 102.340 24.735  1.00 55.33 ? 1215 HOH A O   1 
HETATM 7422 O O   . HOH H 4 .   ? 62.795 99.046  -12.550 1.00 40.00 ? 1216 HOH A O   1 
HETATM 7423 O O   . HOH H 4 .   ? 42.366 105.297 -9.874  1.00 40.21 ? 1217 HOH A O   1 
HETATM 7424 O O   . HOH H 4 .   ? 85.438 108.889 35.189  1.00 41.32 ? 1218 HOH A O   1 
HETATM 7425 O O   . HOH H 4 .   ? 87.594 103.365 17.021  1.00 38.46 ? 1219 HOH A O   1 
HETATM 7426 O O   . HOH H 4 .   ? 36.489 114.643 49.826  1.00 34.61 ? 1220 HOH A O   1 
HETATM 7427 O O   . HOH H 4 .   ? 53.016 118.765 19.749  1.00 26.39 ? 1221 HOH A O   1 
HETATM 7428 O O   . HOH H 4 .   ? 65.603 84.469  39.536  1.00 40.23 ? 1222 HOH A O   1 
HETATM 7429 O O   . HOH H 4 .   ? 52.177 85.031  46.102  1.00 41.62 ? 1223 HOH A O   1 
HETATM 7430 O O   . HOH H 4 .   ? 51.183 117.573 21.238  1.00 26.20 ? 1224 HOH A O   1 
HETATM 7431 O O   . HOH H 4 .   ? 52.279 111.388 1.986   1.00 42.33 ? 1225 HOH A O   1 
HETATM 7432 O O   . HOH H 4 .   ? 40.664 108.465 -13.525 1.00 37.41 ? 1226 HOH A O   1 
HETATM 7433 O O   . HOH H 4 .   ? 52.677 126.896 28.827  1.00 32.47 ? 1227 HOH A O   1 
HETATM 7434 O O   . HOH H 4 .   ? 36.000 110.357 50.872  1.00 42.78 ? 1228 HOH A O   1 
HETATM 7435 O O   . HOH H 4 .   ? 70.406 101.288 -5.973  1.00 39.35 ? 1229 HOH A O   1 
HETATM 7436 O O   . HOH H 4 .   ? 73.206 116.345 35.470  1.00 37.65 ? 1230 HOH A O   1 
HETATM 7437 O O   . HOH H 4 .   ? 70.186 116.327 41.255  1.00 27.34 ? 1231 HOH A O   1 
HETATM 7438 O O   . HOH H 4 .   ? 43.830 103.711 -10.270 1.00 30.25 ? 1232 HOH A O   1 
HETATM 7439 O O   . HOH H 4 .   ? 55.896 83.055  30.452  1.00 42.28 ? 1233 HOH A O   1 
HETATM 7440 O O   . HOH H 4 .   ? 85.763 130.187 36.060  1.00 29.29 ? 1234 HOH A O   1 
HETATM 7441 O O   . HOH H 4 .   ? 27.932 108.470 38.407  1.00 42.29 ? 1235 HOH A O   1 
HETATM 7442 O O   . HOH H 4 .   ? 25.954 105.743 40.161  1.00 51.36 ? 1236 HOH A O   1 
HETATM 7443 O O   . HOH H 4 .   ? 72.593 108.582 12.904  1.00 26.37 ? 1237 HOH A O   1 
HETATM 7444 O O   . HOH H 4 .   ? 18.310 91.068  26.848  1.00 52.41 ? 1238 HOH A O   1 
HETATM 7445 O O   . HOH H 4 .   ? 52.237 81.136  16.445  1.00 38.50 ? 1239 HOH A O   1 
HETATM 7446 O O   . HOH H 4 .   ? 50.635 112.711 0.251   1.00 38.66 ? 1240 HOH A O   1 
HETATM 7447 O O   . HOH H 4 .   ? 82.004 83.779  31.625  1.00 37.76 ? 1241 HOH A O   1 
HETATM 7448 O O   . HOH H 4 .   ? 39.802 98.051  -15.369 1.00 36.85 ? 1242 HOH A O   1 
HETATM 7449 O O   . HOH H 4 .   ? 69.260 106.103 9.392   1.00 22.53 ? 1243 HOH A O   1 
HETATM 7450 O O   . HOH H 4 .   ? 49.485 86.550  33.067  1.00 42.12 ? 1244 HOH A O   1 
HETATM 7451 O O   . HOH H 4 .   ? 80.237 119.021 13.430  1.00 42.06 ? 1245 HOH A O   1 
HETATM 7452 O O   . HOH H 4 .   ? 78.127 102.991 31.675  1.00 33.62 ? 1246 HOH A O   1 
HETATM 7453 O O   . HOH H 4 .   ? 66.348 124.243 40.583  1.00 27.41 ? 1247 HOH A O   1 
HETATM 7454 O O   . HOH H 4 .   ? 89.435 108.452 24.255  1.00 40.11 ? 1248 HOH A O   1 
HETATM 7455 O O   . HOH H 4 .   ? 63.393 82.528  22.962  1.00 43.99 ? 1249 HOH A O   1 
HETATM 7456 O O   . HOH H 4 .   ? 55.140 120.372 31.596  1.00 29.55 ? 1250 HOH A O   1 
HETATM 7457 O O   . HOH H 4 .   ? 30.789 116.126 24.571  1.00 23.73 ? 1251 HOH A O   1 
HETATM 7458 O O   . HOH H 4 .   ? 60.876 87.589  -7.841  1.00 39.87 ? 1252 HOH A O   1 
HETATM 7459 O O   . HOH H 4 .   ? 37.879 74.939  7.995   1.00 30.09 ? 1253 HOH A O   1 
HETATM 7460 O O   . HOH H 4 .   ? 52.325 66.948  6.626   1.00 30.72 ? 1254 HOH A O   1 
HETATM 7461 O O   . HOH H 4 .   ? 85.787 113.493 34.654  1.00 44.70 ? 1255 HOH A O   1 
HETATM 7462 O O   . HOH H 4 .   ? 59.208 80.852  31.016  1.00 42.46 ? 1256 HOH A O   1 
HETATM 7463 O O   . HOH H 4 .   ? 74.683 86.914  30.334  1.00 32.72 ? 1257 HOH A O   1 
HETATM 7464 O O   . HOH H 4 .   ? 83.536 95.274  30.473  1.00 40.92 ? 1258 HOH A O   1 
HETATM 7465 O O   . HOH H 4 .   ? 57.235 64.379  4.163   1.00 44.71 ? 1259 HOH A O   1 
HETATM 7466 O O   . HOH H 4 .   ? 57.666 105.430 54.364  1.00 36.56 ? 1260 HOH A O   1 
HETATM 7467 O O   . HOH H 4 .   ? 72.699 113.869 15.752  1.00 49.63 ? 1261 HOH A O   1 
HETATM 7468 O O   . HOH H 4 .   ? 51.586 121.073 37.588  1.00 35.51 ? 1262 HOH A O   1 
HETATM 7469 O O   . HOH H 4 .   ? 63.702 107.183 -1.667  1.00 39.53 ? 1263 HOH A O   1 
HETATM 7470 O O   . HOH H 4 .   ? 19.623 88.950  19.034  1.00 39.98 ? 1264 HOH A O   1 
HETATM 7471 O O   . HOH H 4 .   ? 84.051 131.796 21.545  1.00 32.63 ? 1265 HOH A O   1 
HETATM 7472 O O   . HOH H 4 .   ? 37.322 105.389 5.002   1.00 37.19 ? 1266 HOH A O   1 
HETATM 7473 O O   . HOH H 4 .   ? 29.692 115.160 26.633  1.00 36.94 ? 1267 HOH A O   1 
HETATM 7474 O O   . HOH H 4 .   ? 55.300 103.988 53.898  1.00 32.96 ? 1268 HOH A O   1 
HETATM 7475 O O   . HOH H 4 .   ? 61.925 101.217 51.976  1.00 42.87 ? 1269 HOH A O   1 
HETATM 7476 O O   . HOH H 4 .   ? 71.347 116.188 15.227  1.00 44.28 ? 1270 HOH A O   1 
HETATM 7477 O O   . HOH H 4 .   ? 35.556 78.505  14.574  1.00 31.67 ? 1271 HOH A O   1 
HETATM 7478 O O   . HOH H 4 .   ? 80.854 104.894 12.800  1.00 32.89 ? 1272 HOH A O   1 
HETATM 7479 O O   . HOH H 4 .   ? 78.090 112.889 13.899  1.00 32.26 ? 1273 HOH A O   1 
HETATM 7480 O O   . HOH H 4 .   ? 75.209 116.166 32.169  1.00 59.81 ? 1274 HOH A O   1 
HETATM 7481 O O   . HOH H 4 .   ? 68.729 108.764 2.349   1.00 51.63 ? 1275 HOH A O   1 
HETATM 7482 O O   . HOH H 4 .   ? 87.258 111.591 35.355  1.00 38.71 ? 1276 HOH A O   1 
HETATM 7483 O O   . HOH H 4 .   ? 56.946 63.930  7.615   1.00 45.29 ? 1277 HOH A O   1 
HETATM 7484 O O   . HOH H 4 .   ? 23.177 87.328  23.543  1.00 37.12 ? 1278 HOH A O   1 
HETATM 7485 O O   . HOH H 4 .   ? 70.338 90.595  2.485   1.00 37.47 ? 1279 HOH A O   1 
HETATM 7486 O O   . HOH H 4 .   ? 37.884 68.103  3.169   1.00 48.23 ? 1280 HOH A O   1 
HETATM 7487 O O   . HOH H 4 .   ? 51.360 117.507 40.377  1.00 35.97 ? 1281 HOH A O   1 
HETATM 7488 O O   . HOH H 4 .   ? 46.806 86.568  31.101  1.00 25.99 ? 1282 HOH A O   1 
HETATM 7489 O O   . HOH H 4 .   ? 62.067 87.976  -4.782  1.00 30.64 ? 1283 HOH A O   1 
HETATM 7490 O O   . HOH H 4 .   ? 32.251 107.326 46.759  1.00 44.33 ? 1284 HOH A O   1 
HETATM 7491 O O   . HOH H 4 .   ? 56.316 90.505  27.251  1.00 34.44 ? 1285 HOH A O   1 
HETATM 7492 O O   . HOH H 4 .   ? 59.880 82.531  10.711  1.00 18.72 ? 1286 HOH A O   1 
HETATM 7493 O O   . HOH H 4 .   ? 43.767 107.005 13.317  1.00 20.74 ? 1287 HOH A O   1 
HETATM 7494 O O   . HOH H 4 .   ? 39.269 96.845  48.713  1.00 22.48 ? 1288 HOH A O   1 
HETATM 7495 O O   . HOH H 4 .   ? 33.849 82.179  1.913   1.00 21.04 ? 1289 HOH A O   1 
HETATM 7496 O O   . HOH H 4 .   ? 72.689 108.174 38.739  1.00 22.66 ? 1290 HOH A O   1 
HETATM 7497 O O   . HOH H 4 .   ? 48.573 109.436 25.360  1.00 22.90 ? 1291 HOH A O   1 
HETATM 7498 O O   . HOH H 4 .   ? 28.076 79.590  17.752  1.00 29.95 ? 1292 HOH A O   1 
HETATM 7499 O O   . HOH H 4 .   ? 32.595 83.758  -2.065  1.00 24.60 ? 1293 HOH A O   1 
HETATM 7500 O O   . HOH H 4 .   ? 41.444 105.719 53.771  1.00 33.41 ? 1294 HOH A O   1 
HETATM 7501 O O   . HOH H 4 .   ? 39.906 87.251  33.668  1.00 45.00 ? 1295 HOH A O   1 
HETATM 7502 O O   . HOH H 4 .   ? 38.385 87.333  29.017  1.00 23.58 ? 1296 HOH A O   1 
HETATM 7503 O O   . HOH H 4 .   ? 51.311 118.617 16.944  1.00 29.47 ? 1297 HOH A O   1 
HETATM 7504 O O   . HOH H 4 .   ? 38.805 85.715  31.163  1.00 32.79 ? 1298 HOH A O   1 
HETATM 7505 O O   . HOH H 4 .   ? 64.253 103.861 -14.602 1.00 26.36 ? 1299 HOH A O   1 
HETATM 7506 O O   . HOH H 4 .   ? 78.903 99.973  30.659  1.00 31.37 ? 1300 HOH A O   1 
HETATM 7507 O O   . HOH H 4 .   ? 73.937 91.427  25.026  1.00 32.92 ? 1301 HOH A O   1 
HETATM 7508 O O   . HOH H 4 .   ? 45.693 117.193 34.685  1.00 29.80 ? 1302 HOH A O   1 
HETATM 7509 O O   . HOH H 4 .   ? 67.468 118.096 42.026  1.00 28.70 ? 1303 HOH A O   1 
HETATM 7510 O O   . HOH H 4 .   ? 57.432 109.684 52.412  1.00 33.09 ? 1304 HOH A O   1 
HETATM 7511 O O   . HOH H 4 .   ? 50.485 112.067 24.340  1.00 32.92 ? 1305 HOH A O   1 
HETATM 7512 O O   . HOH H 4 .   ? 74.638 102.391 2.285   1.00 33.67 ? 1306 HOH A O   1 
HETATM 7513 O O   . HOH H 4 .   ? 37.581 91.561  13.297  1.00 30.27 ? 1307 HOH A O   1 
HETATM 7514 O O   . HOH H 4 .   ? 74.944 134.561 28.299  1.00 35.50 ? 1308 HOH A O   1 
HETATM 7515 O O   . HOH H 4 .   ? 43.734 122.554 30.738  1.00 36.04 ? 1309 HOH A O   1 
HETATM 7516 O O   . HOH H 4 .   ? 40.125 114.587 43.673  1.00 29.72 ? 1310 HOH A O   1 
HETATM 7517 O O   . HOH H 4 .   ? 29.194 77.382  18.495  1.00 37.52 ? 1311 HOH A O   1 
HETATM 7518 O O   . HOH H 4 .   ? 25.391 97.874  12.147  1.00 39.08 ? 1312 HOH A O   1 
HETATM 7519 O O   . HOH H 4 .   ? 47.909 87.423  37.960  1.00 33.11 ? 1313 HOH A O   1 
HETATM 7520 O O   . HOH H 4 .   ? 74.521 87.840  6.378   1.00 47.25 ? 1314 HOH A O   1 
HETATM 7521 O O   . HOH H 4 .   ? 94.677 115.336 33.949  1.00 43.14 ? 1315 HOH A O   1 
HETATM 7522 O O   . HOH H 4 .   ? 73.333 125.998 11.723  1.00 45.72 ? 1316 HOH A O   1 
HETATM 7523 O O   . HOH H 4 .   ? 89.905 127.331 30.082  1.00 36.30 ? 1317 HOH A O   1 
HETATM 7524 O O   . HOH H 4 .   ? 23.033 107.262 19.053  1.00 38.94 ? 1318 HOH A O   1 
HETATM 7525 O O   . HOH H 4 .   ? 30.322 90.757  7.670   1.00 31.45 ? 1319 HOH A O   1 
HETATM 7526 O O   . HOH H 4 .   ? 37.592 103.831 55.959  1.00 34.83 ? 1320 HOH A O   1 
HETATM 7527 O O   . HOH H 4 .   ? 64.148 119.767 10.904  1.00 44.75 ? 1321 HOH A O   1 
HETATM 7528 O O   . HOH H 4 .   ? 67.827 104.543 55.284  1.00 38.69 ? 1322 HOH A O   1 
HETATM 7529 O O   . HOH H 4 .   ? 84.646 101.750 19.706  1.00 30.78 ? 1323 HOH A O   1 
HETATM 7530 O O   . HOH H 4 .   ? 51.154 102.486 -14.606 1.00 36.06 ? 1324 HOH A O   1 
HETATM 7531 O O   . HOH H 4 .   ? 32.393 77.106  2.580   1.00 48.01 ? 1325 HOH A O   1 
HETATM 7532 O O   . HOH H 4 .   ? 87.988 110.662 19.597  1.00 43.08 ? 1326 HOH A O   1 
HETATM 7533 O O   . HOH H 4 .   ? 48.804 119.685 32.705  1.00 33.36 ? 1327 HOH A O   1 
HETATM 7534 O O   . HOH H 4 .   ? 81.299 91.597  13.059  1.00 38.02 ? 1328 HOH A O   1 
HETATM 7535 O O   . HOH H 4 .   ? 94.758 124.311 18.634  1.00 43.65 ? 1329 HOH A O   1 
HETATM 7536 O O   . HOH H 4 .   ? 97.051 130.193 27.356  1.00 50.80 ? 1330 HOH A O   1 
HETATM 7537 O O   . HOH H 4 .   ? 79.965 97.300  34.655  1.00 39.67 ? 1331 HOH A O   1 
HETATM 7538 O O   . HOH H 4 .   ? 36.547 76.899  10.798  1.00 39.93 ? 1332 HOH A O   1 
HETATM 7539 O O   . HOH H 4 .   ? 43.440 77.131  11.515  1.00 31.10 ? 1333 HOH A O   1 
HETATM 7540 O O   . HOH H 4 .   ? 81.319 118.337 37.417  1.00 45.14 ? 1334 HOH A O   1 
HETATM 7541 O O   . HOH H 4 .   ? 66.632 115.687 44.844  1.00 34.37 ? 1335 HOH A O   1 
HETATM 7542 O O   . HOH H 4 .   ? 35.810 121.966 29.424  1.00 41.65 ? 1336 HOH A O   1 
HETATM 7543 O O   . HOH H 4 .   ? 48.584 106.113 -15.125 1.00 33.38 ? 1337 HOH A O   1 
HETATM 7544 O O   . HOH H 4 .   ? 23.202 86.387  12.693  1.00 29.64 ? 1338 HOH A O   1 
HETATM 7545 O O   . HOH H 4 .   ? 24.723 85.119  18.389  1.00 33.67 ? 1339 HOH A O   1 
HETATM 7546 O O   . HOH H 4 .   ? 66.526 113.698 46.590  1.00 42.84 ? 1340 HOH A O   1 
HETATM 7547 O O   . HOH H 4 .   ? 63.761 105.896 -16.047 1.00 33.17 ? 1341 HOH A O   1 
HETATM 7548 O O   . HOH H 4 .   ? 27.017 96.108  -3.330  1.00 41.35 ? 1342 HOH A O   1 
HETATM 7549 O O   . HOH H 4 .   ? 86.901 119.738 12.743  1.00 33.68 ? 1343 HOH A O   1 
HETATM 7550 O O   . HOH H 4 .   ? 33.645 101.038 6.360   1.00 29.81 ? 1344 HOH A O   1 
HETATM 7551 O O   . HOH H 4 .   ? 47.499 76.260  9.312   1.00 32.32 ? 1345 HOH A O   1 
HETATM 7552 O O   . HOH H 4 .   ? 78.710 109.420 35.309  1.00 39.66 ? 1346 HOH A O   1 
HETATM 7553 O O   . HOH H 4 .   ? 22.060 111.153 35.234  1.00 34.28 ? 1347 HOH A O   1 
HETATM 7554 O O   . HOH H 4 .   ? 25.005 80.895  8.137   1.00 31.84 ? 1348 HOH A O   1 
HETATM 7555 O O   . HOH H 4 .   ? 68.146 94.238  -14.185 1.00 37.62 ? 1349 HOH A O   1 
HETATM 7556 O O   . HOH H 4 .   ? 69.065 93.875  -7.186  1.00 33.35 ? 1350 HOH A O   1 
HETATM 7557 O O   . HOH H 4 .   ? 32.159 89.444  -8.835  1.00 34.54 ? 1351 HOH A O   1 
HETATM 7558 O O   . HOH H 4 .   ? 63.977 116.694 8.791   1.00 42.38 ? 1352 HOH A O   1 
HETATM 7559 O O   . HOH H 4 .   ? 51.883 114.573 11.768  1.00 40.22 ? 1353 HOH A O   1 
HETATM 7560 O O   . HOH H 4 .   ? 48.611 124.171 20.483  1.00 35.16 ? 1354 HOH A O   1 
HETATM 7561 O O   . HOH H 4 .   ? 30.560 81.831  -1.263  1.00 40.34 ? 1355 HOH A O   1 
HETATM 7562 O O   . HOH H 4 .   ? 40.728 86.401  35.911  1.00 40.81 ? 1356 HOH A O   1 
HETATM 7563 O O   . HOH H 4 .   ? 30.801 86.489  -7.714  1.00 31.40 ? 1357 HOH A O   1 
HETATM 7564 O O   . HOH H 4 .   ? 32.052 101.134 8.430   1.00 33.02 ? 1358 HOH A O   1 
HETATM 7565 O O   . HOH H 4 .   ? 32.955 114.685 20.786  1.00 41.17 ? 1359 HOH A O   1 
HETATM 7566 O O   . HOH H 4 .   ? 64.789 116.692 46.590  1.00 47.57 ? 1360 HOH A O   1 
HETATM 7567 O O   . HOH H 4 .   ? 45.871 82.079  -16.647 1.00 48.50 ? 1361 HOH A O   1 
HETATM 7568 O O   . HOH H 4 .   ? 67.786 113.882 14.134  1.00 38.62 ? 1362 HOH A O   1 
HETATM 7569 O O   . HOH H 4 .   ? 62.318 67.429  8.249   1.00 50.31 ? 1363 HOH A O   1 
HETATM 7570 O O   . HOH H 4 .   ? 37.158 111.272 54.214  1.00 41.91 ? 1364 HOH A O   1 
HETATM 7571 O O   . HOH H 4 .   ? 49.226 92.351  48.412  1.00 41.59 ? 1365 HOH A O   1 
HETATM 7572 O O   . HOH H 4 .   ? 18.490 87.545  15.561  1.00 42.42 ? 1366 HOH A O   1 
HETATM 7573 O O   . HOH H 4 .   ? 38.514 109.780 3.118   1.00 43.42 ? 1367 HOH A O   1 
HETATM 7574 O O   . HOH H 4 .   ? 73.914 120.390 34.287  1.00 31.57 ? 1368 HOH A O   1 
HETATM 7575 O O   . HOH H 4 .   ? 69.028 103.740 49.838  1.00 31.63 ? 1369 HOH A O   1 
HETATM 7576 O O   . HOH H 4 .   ? 85.555 102.810 32.631  1.00 45.63 ? 1370 HOH A O   1 
HETATM 7577 O O   . HOH H 4 .   ? 32.412 88.858  36.991  1.00 38.80 ? 1371 HOH A O   1 
HETATM 7578 O O   . HOH H 4 .   ? 57.313 129.960 13.463  1.00 35.80 ? 1372 HOH A O   1 
HETATM 7579 O O   . HOH H 4 .   ? 66.616 130.918 29.059  1.00 35.30 ? 1373 HOH A O   1 
HETATM 7580 O O   . HOH H 4 .   ? 78.988 99.931  33.786  1.00 37.93 ? 1374 HOH A O   1 
HETATM 7581 O O   . HOH H 4 .   ? 33.379 76.610  12.095  1.00 45.53 ? 1375 HOH A O   1 
HETATM 7582 O O   . HOH H 4 .   ? 43.180 117.153 36.604  1.00 48.62 ? 1376 HOH A O   1 
HETATM 7583 O O   . HOH H 4 .   ? 81.299 110.073 12.951  1.00 30.57 ? 1377 HOH A O   1 
HETATM 7584 O O   . HOH H 4 .   ? 72.992 89.972  40.478  1.00 30.88 ? 1378 HOH A O   1 
HETATM 7585 O O   . HOH H 4 .   ? 50.957 81.123  30.298  1.00 42.35 ? 1379 HOH A O   1 
HETATM 7586 O O   . HOH H 4 .   ? 38.188 72.619  6.891   1.00 33.14 ? 1380 HOH A O   1 
HETATM 7587 O O   . HOH H 4 .   ? 61.233 109.117 4.812   1.00 41.61 ? 1381 HOH A O   1 
HETATM 7588 O O   . HOH H 4 .   ? 65.174 81.608  3.880   1.00 37.91 ? 1382 HOH A O   1 
HETATM 7589 O O   . HOH H 4 .   ? 69.885 87.786  6.614   1.00 36.01 ? 1383 HOH A O   1 
HETATM 7590 O O   . HOH H 4 .   ? 33.521 85.058  35.500  1.00 41.23 ? 1384 HOH A O   1 
HETATM 7591 O O   . HOH H 4 .   ? 49.411 80.124  17.072  1.00 40.86 ? 1385 HOH A O   1 
HETATM 7592 O O   . HOH H 4 .   ? 36.189 79.071  -6.341  1.00 40.66 ? 1386 HOH A O   1 
HETATM 7593 O O   . HOH H 4 .   ? 36.528 106.607 10.773  1.00 35.35 ? 1387 HOH A O   1 
HETATM 7594 O O   . HOH H 4 .   ? 20.548 109.089 34.947  1.00 44.38 ? 1388 HOH A O   1 
HETATM 7595 O O   . HOH H 4 .   ? 39.220 81.763  -1.402  1.00 27.75 ? 1389 HOH A O   1 
HETATM 7596 O O   . HOH H 4 .   ? 69.357 107.208 11.708  1.00 26.97 ? 1390 HOH A O   1 
HETATM 7597 O O   . HOH H 4 .   ? 39.588 105.202 56.487  1.00 43.04 ? 1391 HOH A O   1 
HETATM 7598 O O   . HOH H 4 .   ? 95.535 122.241 25.878  1.00 28.56 ? 1392 HOH A O   1 
HETATM 7599 O O   . HOH H 4 .   ? 29.817 75.328  3.232   1.00 51.63 ? 1393 HOH A O   1 
HETATM 7600 O O   . HOH H 4 .   ? 46.052 108.095 1.438   1.00 35.65 ? 1394 HOH A O   1 
HETATM 7601 O O   . HOH H 4 .   ? 21.967 90.982  33.232  1.00 31.41 ? 1395 HOH A O   1 
HETATM 7602 O O   . HOH H 4 .   ? 64.140 87.433  23.345  1.00 31.59 ? 1396 HOH A O   1 
HETATM 7603 O O   . HOH H 4 .   ? 54.483 123.839 31.426  1.00 37.39 ? 1397 HOH A O   1 
HETATM 7604 O O   . HOH H 4 .   ? 48.653 88.908  49.446  1.00 41.50 ? 1398 HOH A O   1 
HETATM 7605 O O   . HOH H 4 .   ? 70.279 130.037 34.997  1.00 35.81 ? 1399 HOH A O   1 
HETATM 7606 O O   . HOH H 4 .   ? 56.184 110.798 19.969  1.00 27.71 ? 1400 HOH A O   1 
HETATM 7607 O O   . HOH H 4 .   ? 48.912 104.424 55.076  1.00 38.35 ? 1401 HOH A O   1 
HETATM 7608 O O   . HOH H 4 .   ? 63.314 85.891  -3.187  1.00 38.96 ? 1402 HOH A O   1 
HETATM 7609 O O   . HOH H 4 .   ? 22.489 110.411 29.101  1.00 43.94 ? 1403 HOH A O   1 
HETATM 7610 O O   . HOH H 4 .   ? 45.192 115.550 -14.216 1.00 44.99 ? 1404 HOH A O   1 
HETATM 7611 O O   . HOH H 4 .   ? 74.307 133.895 16.020  1.00 48.20 ? 1405 HOH A O   1 
HETATM 7612 O O   . HOH H 4 .   ? 29.793 97.938  7.696   1.00 40.59 ? 1406 HOH A O   1 
HETATM 7613 O O   . HOH H 4 .   ? 87.938 103.961 33.871  1.00 50.74 ? 1407 HOH A O   1 
HETATM 7614 O O   . HOH H 4 .   ? 98.748 121.174 23.402  1.00 43.86 ? 1408 HOH A O   1 
HETATM 7615 O O   . HOH H 4 .   ? 34.471 97.801  46.601  1.00 28.77 ? 1409 HOH A O   1 
HETATM 7616 O O   . HOH H 4 .   ? 49.619 86.618  51.327  1.00 46.15 ? 1410 HOH A O   1 
HETATM 7617 O O   . HOH H 4 .   ? 20.242 92.321  39.902  1.00 44.39 ? 1411 HOH A O   1 
HETATM 7618 O O   . HOH H 4 .   ? 65.836 79.840  0.442   1.00 43.67 ? 1412 HOH A O   1 
HETATM 7619 O O   . HOH H 4 .   ? 22.607 93.434  41.958  1.00 47.33 ? 1413 HOH A O   1 
HETATM 7620 O O   . HOH H 4 .   ? 19.186 95.357  34.413  1.00 46.81 ? 1414 HOH A O   1 
HETATM 7621 O O   . HOH H 4 .   ? 28.029 90.522  40.248  1.00 47.17 ? 1415 HOH A O   1 
HETATM 7622 O O   . HOH H 4 .   ? 48.084 94.980  49.222  1.00 36.73 ? 1416 HOH A O   1 
HETATM 7623 O O   . HOH H 4 .   ? 41.572 75.101  10.642  1.00 44.16 ? 1417 HOH A O   1 
HETATM 7624 O O   . HOH H 4 .   ? 92.242 112.239 22.508  1.00 40.75 ? 1418 HOH A O   1 
HETATM 7625 O O   . HOH H 4 .   ? 20.469 110.659 31.026  1.00 49.83 ? 1419 HOH A O   1 
HETATM 7626 O O   . HOH H 4 .   ? 35.775 106.306 18.442  1.00 30.42 ? 1420 HOH A O   1 
HETATM 7627 O O   . HOH H 4 .   ? 68.212 109.498 14.269  1.00 33.88 ? 1421 HOH A O   1 
HETATM 7628 O O   . HOH H 4 .   ? 35.297 97.737  -6.773  1.00 35.85 ? 1422 HOH A O   1 
HETATM 7629 O O   . HOH H 4 .   ? 67.901 84.498  41.433  1.00 36.37 ? 1423 HOH A O   1 
HETATM 7630 O O   . HOH H 4 .   ? 73.838 87.906  25.151  1.00 34.41 ? 1424 HOH A O   1 
HETATM 7631 O O   . HOH H 4 .   ? 55.145 68.504  8.855   1.00 44.14 ? 1425 HOH A O   1 
HETATM 7632 O O   . HOH H 4 .   ? 73.875 131.080 15.230  1.00 37.28 ? 1426 HOH A O   1 
HETATM 7633 O O   . HOH H 4 .   ? 33.731 98.151  -9.995  1.00 44.32 ? 1427 HOH A O   1 
HETATM 7634 O O   . HOH H 4 .   ? 61.423 91.618  49.043  1.00 40.20 ? 1428 HOH A O   1 
HETATM 7635 O O   . HOH H 4 .   ? 38.878 94.326  -19.227 1.00 40.00 ? 1429 HOH A O   1 
HETATM 7636 O O   . HOH H 4 .   ? 42.755 119.704 23.617  1.00 40.96 ? 1430 HOH A O   1 
HETATM 7637 O O   . HOH H 4 .   ? 48.009 85.815  44.202  1.00 35.80 ? 1431 HOH A O   1 
HETATM 7638 O O   . HOH H 4 .   ? 60.608 133.072 21.776  1.00 44.76 ? 1432 HOH A O   1 
HETATM 7639 O O   . HOH H 4 .   ? 72.919 100.307 -2.818  1.00 38.76 ? 1433 HOH A O   1 
HETATM 7640 O O   . HOH H 4 .   ? 70.794 110.413 13.346  1.00 32.94 ? 1434 HOH A O   1 
HETATM 7641 O O   . HOH H 4 .   ? 78.187 134.866 27.208  1.00 41.90 ? 1435 HOH A O   1 
HETATM 7642 O O   . HOH H 4 .   ? 93.212 126.711 30.185  1.00 39.52 ? 1436 HOH A O   1 
HETATM 7643 O O   . HOH H 4 .   ? 23.060 99.671  41.128  1.00 36.87 ? 1437 HOH A O   1 
HETATM 7644 O O   . HOH H 4 .   ? 39.342 78.577  -8.193  1.00 41.86 ? 1438 HOH A O   1 
HETATM 7645 O O   . HOH H 4 .   ? 35.134 117.763 35.220  1.00 47.06 ? 1439 HOH A O   1 
HETATM 7646 O O   . HOH H 4 .   ? 20.650 107.445 37.135  1.00 38.76 ? 1440 HOH A O   1 
HETATM 7647 O O   . HOH H 4 .   ? 56.534 97.799  -15.686 1.00 44.58 ? 1441 HOH A O   1 
HETATM 7648 O O   . HOH H 4 .   ? 23.957 88.482  11.131  1.00 40.42 ? 1442 HOH A O   1 
HETATM 7649 O O   . HOH H 4 .   ? 41.636 119.392 33.616  1.00 37.26 ? 1443 HOH A O   1 
HETATM 7650 O O   . HOH H 4 .   ? 46.582 125.536 22.151  1.00 37.74 ? 1444 HOH A O   1 
HETATM 7651 O O   . HOH H 4 .   ? 63.232 123.714 13.067  1.00 39.59 ? 1445 HOH A O   1 
HETATM 7652 O O   . HOH H 4 .   ? 76.871 103.131 10.364  1.00 40.83 ? 1446 HOH A O   1 
HETATM 7653 O O   . HOH H 4 .   ? 35.047 91.648  -16.421 1.00 49.07 ? 1447 HOH A O   1 
HETATM 7654 O O   . HOH H 4 .   ? 27.252 98.242  8.224   1.00 38.99 ? 1448 HOH A O   1 
HETATM 7655 O O   . HOH H 4 .   ? 19.662 100.535 23.535  1.00 35.88 ? 1449 HOH A O   1 
HETATM 7656 O O   . HOH H 4 .   ? 38.290 69.913  9.247   1.00 40.72 ? 1450 HOH A O   1 
HETATM 7657 O O   . HOH H 4 .   ? 41.306 111.938 -10.315 1.00 50.21 ? 1451 HOH A O   1 
HETATM 7658 O O   . HOH H 4 .   ? 21.788 112.398 27.277  1.00 43.37 ? 1452 HOH A O   1 
HETATM 7659 O O   . HOH H 4 .   ? 58.771 134.117 19.809  1.00 51.98 ? 1453 HOH A O   1 
HETATM 7660 O O   . HOH H 4 .   ? 36.908 85.048  34.778  1.00 54.46 ? 1454 HOH A O   1 
HETATM 7661 O O   . HOH H 4 .   ? 31.453 81.783  2.724   1.00 52.67 ? 1455 HOH A O   1 
HETATM 7662 O O   . HOH H 4 .   ? 42.276 93.637  48.484  1.00 41.44 ? 1456 HOH A O   1 
HETATM 7663 O O   . HOH H 4 .   ? 44.160 98.650  54.806  1.00 36.97 ? 1457 HOH A O   1 
HETATM 7664 O O   . HOH H 4 .   ? 12.111 105.050 16.607  1.00 56.19 ? 1458 HOH A O   1 
HETATM 7665 O O   . HOH H 4 .   ? 68.066 120.273 14.590  1.00 48.04 ? 1459 HOH A O   1 
HETATM 7666 O O   . HOH H 4 .   ? 28.206 79.694  22.217  1.00 48.44 ? 1460 HOH A O   1 
HETATM 7667 O O   . HOH H 4 .   ? 32.009 112.842 19.078  1.00 41.73 ? 1461 HOH A O   1 
HETATM 7668 O O   . HOH H 4 .   ? 33.174 107.201 15.237  1.00 40.85 ? 1462 HOH A O   1 
HETATM 7669 O O   . HOH H 4 .   ? 35.244 103.219 5.018   1.00 50.01 ? 1463 HOH A O   1 
HETATM 7670 O O   . HOH H 4 .   ? 66.363 128.966 36.564  1.00 39.04 ? 1464 HOH A O   1 
HETATM 7671 O O   . HOH H 4 .   ? 47.036 84.345  -9.457  1.00 32.16 ? 1465 HOH A O   1 
HETATM 7672 O O   . HOH H 4 .   ? 61.885 109.992 -2.942  1.00 37.72 ? 1466 HOH A O   1 
HETATM 7673 O O   . HOH H 4 .   ? 76.874 107.685 36.381  1.00 33.52 ? 1467 HOH A O   1 
HETATM 7674 O O   . HOH H 4 .   ? 84.598 133.858 27.317  1.00 39.06 ? 1468 HOH A O   1 
HETATM 7675 O O   . HOH H 4 .   ? 52.352 85.472  -13.070 1.00 40.89 ? 1469 HOH A O   1 
HETATM 7676 O O   . HOH H 4 .   ? 56.763 81.773  19.791  1.00 47.93 ? 1470 HOH A O   1 
HETATM 7677 O O   . HOH H 4 .   ? 48.784 73.450  7.631   1.00 39.26 ? 1471 HOH A O   1 
HETATM 7678 O O   . HOH H 4 .   ? 45.949 111.362 6.249   1.00 38.53 ? 1472 HOH A O   1 
HETATM 7679 O O   . HOH H 4 .   ? 63.546 110.846 52.754  1.00 40.48 ? 1473 HOH A O   1 
HETATM 7680 O O   . HOH H 4 .   ? 52.468 95.816  -15.817 1.00 31.36 ? 1474 HOH A O   1 
HETATM 7681 O O   . HOH H 4 .   ? 51.917 83.357  -11.053 1.00 45.02 ? 1475 HOH A O   1 
HETATM 7682 O O   . HOH H 4 .   ? 74.556 82.485  34.678  1.00 45.48 ? 1476 HOH A O   1 
HETATM 7683 O O   . HOH H 4 .   ? 30.532 109.838 38.188  1.00 41.68 ? 1477 HOH A O   1 
HETATM 7684 O O   . HOH H 4 .   ? 50.342 129.405 17.375  1.00 43.55 ? 1478 HOH A O   1 
HETATM 7685 O O   . HOH H 4 .   ? 21.462 87.203  19.165  1.00 40.48 ? 1479 HOH A O   1 
HETATM 7686 O O   . HOH H 4 .   ? 76.002 129.648 16.937  1.00 37.51 ? 1480 HOH A O   1 
HETATM 7687 O O   . HOH H 4 .   ? 40.354 85.827  28.268  1.00 38.96 ? 1481 HOH A O   1 
HETATM 7688 O O   . HOH H 4 .   ? 55.928 81.030  28.658  1.00 39.58 ? 1482 HOH A O   1 
HETATM 7689 O O   . HOH H 4 .   ? 64.521 129.546 26.206  1.00 42.99 ? 1483 HOH A O   1 
HETATM 7690 O O   . HOH H 4 .   ? 22.486 85.692  16.576  1.00 42.51 ? 1484 HOH A O   1 
HETATM 7691 O O   . HOH H 4 .   ? 75.183 123.951 15.477  1.00 38.18 ? 1485 HOH A O   1 
HETATM 7692 O O   . HOH H 4 .   ? 28.582 77.582  10.503  1.00 41.66 ? 1486 HOH A O   1 
HETATM 7693 O O   . HOH H 4 .   ? 77.142 134.275 15.311  1.00 42.10 ? 1487 HOH A O   1 
HETATM 7694 O O   . HOH H 4 .   ? 48.870 110.734 -13.873 1.00 51.09 ? 1488 HOH A O   1 
HETATM 7695 O O   . HOH H 4 .   ? 39.804 109.181 7.172   1.00 40.73 ? 1489 HOH A O   1 
HETATM 7696 O O   . HOH H 4 .   ? 50.396 78.380  19.394  1.00 45.77 ? 1490 HOH A O   1 
HETATM 7697 O O   . HOH H 4 .   ? 28.752 75.379  12.070  1.00 45.02 ? 1491 HOH A O   1 
HETATM 7698 O O   . HOH H 4 .   ? 59.236 108.208 -12.472 1.00 40.43 ? 1492 HOH A O   1 
HETATM 7699 O O   . HOH H 4 .   ? 19.072 100.696 26.099  1.00 41.18 ? 1493 HOH A O   1 
HETATM 7700 O O   . HOH H 4 .   ? 32.387 99.620  50.387  1.00 37.63 ? 1494 HOH A O   1 
HETATM 7701 O O   . HOH H 4 .   ? 50.667 118.609 50.622  1.00 52.46 ? 1495 HOH A O   1 
HETATM 7702 O O   . HOH H 4 .   ? 63.589 78.934  30.177  1.00 59.05 ? 1496 HOH A O   1 
HETATM 7703 O O   . HOH H 4 .   ? 63.644 107.810 1.053   1.00 36.03 ? 1497 HOH A O   1 
HETATM 7704 O O   . HOH H 4 .   ? 67.142 83.203  8.622   1.00 33.69 ? 1498 HOH A O   1 
HETATM 7705 O O   . HOH H 4 .   ? 54.020 130.238 16.383  1.00 45.33 ? 1499 HOH A O   1 
HETATM 7706 O O   . HOH H 4 .   ? 48.321 82.041  32.022  1.00 40.69 ? 1500 HOH A O   1 
HETATM 7707 O O   . HOH H 4 .   ? 68.388 87.137  4.121   1.00 50.13 ? 1501 HOH A O   1 
HETATM 7708 O O   . HOH H 4 .   ? 38.776 63.256  -3.661  1.00 50.84 ? 1502 HOH A O   1 
HETATM 7709 O O   . HOH H 4 .   ? 42.347 99.708  -21.359 1.00 36.27 ? 1503 HOH A O   1 
HETATM 7710 O O   . HOH H 4 .   ? 23.631 74.370  15.747  1.00 49.03 ? 1504 HOH A O   1 
HETATM 7711 O O   . HOH H 4 .   ? 48.948 76.320  18.405  1.00 48.86 ? 1505 HOH A O   1 
HETATM 7712 O O   . HOH H 4 .   ? 81.041 101.947 33.966  1.00 35.97 ? 1506 HOH A O   1 
HETATM 7713 O O   . HOH H 4 .   ? 31.836 98.203  48.580  1.00 41.93 ? 1507 HOH A O   1 
HETATM 7714 O O   . HOH H 4 .   ? 41.021 116.469 45.018  1.00 39.99 ? 1508 HOH A O   1 
HETATM 7715 O O   . HOH H 4 .   ? 88.419 128.151 17.714  1.00 45.50 ? 1509 HOH A O   1 
HETATM 7716 O O   . HOH H 4 .   ? 61.287 107.355 2.213   1.00 38.94 ? 1510 HOH A O   1 
HETATM 7717 O O   . HOH H 4 .   ? 17.769 103.898 38.123  1.00 45.12 ? 1511 HOH A O   1 
HETATM 7718 O O   . HOH H 4 .   ? 28.898 90.994  43.544  1.00 42.03 ? 1512 HOH A O   1 
HETATM 7719 O O   . HOH H 4 .   ? 49.744 82.925  -9.444  1.00 50.59 ? 1513 HOH A O   1 
HETATM 7720 O O   . HOH H 4 .   ? 83.713 113.402 11.424  1.00 37.64 ? 1514 HOH A O   1 
HETATM 7721 O O   . HOH H 4 .   ? 21.640 112.729 33.110  1.00 37.60 ? 1515 HOH A O   1 
HETATM 7722 O O   . HOH H 4 .   ? 42.096 111.892 8.398   1.00 50.40 ? 1516 HOH A O   1 
HETATM 7723 O O   . HOH H 4 .   ? 27.594 86.110  33.361  1.00 51.40 ? 1517 HOH A O   1 
HETATM 7724 O O   . HOH H 4 .   ? 47.189 86.412  35.419  1.00 48.28 ? 1518 HOH A O   1 
HETATM 7725 O O   . HOH H 4 .   ? 63.917 132.867 30.733  1.00 43.91 ? 1519 HOH A O   1 
HETATM 7726 O O   . HOH H 4 .   ? 31.698 75.137  10.755  1.00 50.93 ? 1520 HOH A O   1 
HETATM 7727 O O   . HOH H 4 .   ? 87.939 96.418  15.760  1.00 38.74 ? 1521 HOH A O   1 
HETATM 7728 O O   . HOH H 4 .   ? 36.989 100.305 -2.905  1.00 49.58 ? 1522 HOH A O   1 
HETATM 7729 O O   . HOH H 4 .   ? 50.685 112.107 -2.447  1.00 38.27 ? 1523 HOH A O   1 
HETATM 7730 O O   . HOH H 4 .   ? 32.124 76.043  0.330   1.00 50.27 ? 1524 HOH A O   1 
HETATM 7731 O O   . HOH H 4 .   ? 74.297 128.648 34.379  1.00 47.76 ? 1525 HOH A O   1 
HETATM 7732 O O   . HOH H 4 .   ? 87.149 95.348  36.538  1.00 51.05 ? 1526 HOH A O   1 
HETATM 7733 O O   . HOH H 4 .   ? 40.465 95.625  -22.757 1.00 34.15 ? 1527 HOH A O   1 
HETATM 7734 O O   . HOH H 4 .   ? 35.986 118.935 42.284  1.00 51.90 ? 1528 HOH A O   1 
HETATM 7735 O O   . HOH H 4 .   ? 35.582 114.706 45.533  1.00 40.57 ? 1529 HOH A O   1 
HETATM 7736 O O   . HOH H 4 .   ? 75.490 129.427 12.937  1.00 51.90 ? 1530 HOH A O   1 
HETATM 7737 O O   . HOH H 4 .   ? 38.415 117.528 46.076  1.00 37.65 ? 1531 HOH A O   1 
HETATM 7738 O O   . HOH H 4 .   ? 62.476 135.517 23.056  1.00 50.26 ? 1532 HOH A O   1 
HETATM 7739 O O   . HOH H 4 .   ? 55.181 122.317 12.577  1.00 46.01 ? 1533 HOH A O   1 
HETATM 7740 O O   . HOH H 4 .   ? 57.091 116.524 51.046  1.00 47.67 ? 1534 HOH A O   1 
HETATM 7741 O O   . HOH H 4 .   ? 74.885 108.781 37.352  1.00 29.11 ? 1535 HOH A O   1 
HETATM 7742 O O   . HOH H 4 .   ? 25.346 111.666 29.636  1.00 28.41 ? 1536 HOH A O   1 
HETATM 7743 O O   . HOH H 4 .   ? 34.989 108.991 18.839  1.00 42.67 ? 1537 HOH A O   1 
HETATM 7744 O O   . HOH H 4 .   ? 36.377 116.184 47.793  1.00 35.79 ? 1538 HOH A O   1 
HETATM 7745 O O   . HOH H 4 .   ? 51.797 75.859  17.972  1.00 51.31 ? 1539 HOH A O   1 
HETATM 7746 O O   . HOH H 4 .   ? 30.317 97.814  5.231   1.00 32.60 ? 1540 HOH A O   1 
HETATM 7747 O O   . HOH H 4 .   ? 43.804 120.472 32.493  1.00 36.05 ? 1541 HOH A O   1 
HETATM 7748 O O   . HOH H 4 .   ? 71.918 102.342 -1.523  1.00 36.26 ? 1542 HOH A O   1 
HETATM 7749 O O   . HOH H 4 .   ? 55.288 66.480  7.212   1.00 44.90 ? 1543 HOH A O   1 
HETATM 7750 O O   . HOH H 4 .   ? 90.889 110.116 22.954  1.00 38.19 ? 1544 HOH A O   1 
HETATM 7751 O O   . HOH H 4 .   ? 47.907 126.765 24.332  1.00 34.28 ? 1545 HOH A O   1 
HETATM 7752 O O   . HOH H 4 .   ? 48.633 80.620  -9.214  1.00 40.71 ? 1546 HOH A O   1 
HETATM 7753 O O   . HOH H 4 .   ? 61.021 109.846 -13.708 1.00 35.27 ? 1547 HOH A O   1 
HETATM 7754 O O   . HOH H 4 .   ? 39.951 98.257  -20.738 1.00 34.38 ? 1548 HOH A O   1 
HETATM 7755 O O   . HOH H 4 .   ? 21.218 84.148  20.893  1.00 40.15 ? 1549 HOH A O   1 
HETATM 7756 O O   . HOH H 4 .   ? 37.247 102.956 2.952   1.00 44.66 ? 1550 HOH A O   1 
HETATM 7757 O O   . HOH H 4 .   ? 38.183 104.889 0.592   1.00 52.25 ? 1551 HOH A O   1 
HETATM 7758 O O   . HOH H 4 .   ? 41.040 105.273 1.700   1.00 39.27 ? 1552 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 KTL 1   1001 1001 KTL KTL 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 3 NAG 2   2004 2004 NAG NAG A . 
G 3 NAG 1   2005 2005 NAG NAG A . 
H 4 HOH 1   876  1    HOH HOH A . 
H 4 HOH 2   877  2    HOH HOH A . 
H 4 HOH 3   878  3    HOH HOH A . 
H 4 HOH 4   879  4    HOH HOH A . 
H 4 HOH 5   880  5    HOH HOH A . 
H 4 HOH 6   881  6    HOH HOH A . 
H 4 HOH 7   882  7    HOH HOH A . 
H 4 HOH 8   883  8    HOH HOH A . 
H 4 HOH 9   884  9    HOH HOH A . 
H 4 HOH 10  885  10   HOH HOH A . 
H 4 HOH 11  886  11   HOH HOH A . 
H 4 HOH 12  887  12   HOH HOH A . 
H 4 HOH 13  888  13   HOH HOH A . 
H 4 HOH 14  889  14   HOH HOH A . 
H 4 HOH 15  890  15   HOH HOH A . 
H 4 HOH 16  891  16   HOH HOH A . 
H 4 HOH 17  892  17   HOH HOH A . 
H 4 HOH 18  893  18   HOH HOH A . 
H 4 HOH 19  894  19   HOH HOH A . 
H 4 HOH 20  895  20   HOH HOH A . 
H 4 HOH 21  896  21   HOH HOH A . 
H 4 HOH 22  897  22   HOH HOH A . 
H 4 HOH 23  898  23   HOH HOH A . 
H 4 HOH 24  899  24   HOH HOH A . 
H 4 HOH 25  900  25   HOH HOH A . 
H 4 HOH 26  901  26   HOH HOH A . 
H 4 HOH 27  902  27   HOH HOH A . 
H 4 HOH 28  903  28   HOH HOH A . 
H 4 HOH 29  904  29   HOH HOH A . 
H 4 HOH 30  905  30   HOH HOH A . 
H 4 HOH 31  906  31   HOH HOH A . 
H 4 HOH 32  907  32   HOH HOH A . 
H 4 HOH 33  908  33   HOH HOH A . 
H 4 HOH 34  909  34   HOH HOH A . 
H 4 HOH 35  910  35   HOH HOH A . 
H 4 HOH 36  911  36   HOH HOH A . 
H 4 HOH 37  912  37   HOH HOH A . 
H 4 HOH 38  913  38   HOH HOH A . 
H 4 HOH 39  914  39   HOH HOH A . 
H 4 HOH 40  915  40   HOH HOH A . 
H 4 HOH 41  916  41   HOH HOH A . 
H 4 HOH 42  917  42   HOH HOH A . 
H 4 HOH 43  918  43   HOH HOH A . 
H 4 HOH 44  919  44   HOH HOH A . 
H 4 HOH 45  920  45   HOH HOH A . 
H 4 HOH 46  921  46   HOH HOH A . 
H 4 HOH 47  922  47   HOH HOH A . 
H 4 HOH 48  923  48   HOH HOH A . 
H 4 HOH 49  924  49   HOH HOH A . 
H 4 HOH 50  925  50   HOH HOH A . 
H 4 HOH 51  926  51   HOH HOH A . 
H 4 HOH 52  927  52   HOH HOH A . 
H 4 HOH 53  928  53   HOH HOH A . 
H 4 HOH 54  929  54   HOH HOH A . 
H 4 HOH 55  930  55   HOH HOH A . 
H 4 HOH 56  931  56   HOH HOH A . 
H 4 HOH 57  932  57   HOH HOH A . 
H 4 HOH 58  933  58   HOH HOH A . 
H 4 HOH 59  934  59   HOH HOH A . 
H 4 HOH 60  935  60   HOH HOH A . 
H 4 HOH 61  936  61   HOH HOH A . 
H 4 HOH 62  937  62   HOH HOH A . 
H 4 HOH 63  938  63   HOH HOH A . 
H 4 HOH 64  939  64   HOH HOH A . 
H 4 HOH 65  940  65   HOH HOH A . 
H 4 HOH 66  941  66   HOH HOH A . 
H 4 HOH 67  942  67   HOH HOH A . 
H 4 HOH 68  943  68   HOH HOH A . 
H 4 HOH 69  944  69   HOH HOH A . 
H 4 HOH 70  945  70   HOH HOH A . 
H 4 HOH 71  946  71   HOH HOH A . 
H 4 HOH 72  947  72   HOH HOH A . 
H 4 HOH 73  948  73   HOH HOH A . 
H 4 HOH 74  949  74   HOH HOH A . 
H 4 HOH 75  950  75   HOH HOH A . 
H 4 HOH 76  951  76   HOH HOH A . 
H 4 HOH 77  952  77   HOH HOH A . 
H 4 HOH 78  953  78   HOH HOH A . 
H 4 HOH 79  954  79   HOH HOH A . 
H 4 HOH 80  955  80   HOH HOH A . 
H 4 HOH 81  956  81   HOH HOH A . 
H 4 HOH 82  957  82   HOH HOH A . 
H 4 HOH 83  958  83   HOH HOH A . 
H 4 HOH 84  959  84   HOH HOH A . 
H 4 HOH 85  960  85   HOH HOH A . 
H 4 HOH 86  961  86   HOH HOH A . 
H 4 HOH 87  962  87   HOH HOH A . 
H 4 HOH 88  963  88   HOH HOH A . 
H 4 HOH 89  964  89   HOH HOH A . 
H 4 HOH 90  965  90   HOH HOH A . 
H 4 HOH 91  966  91   HOH HOH A . 
H 4 HOH 92  967  92   HOH HOH A . 
H 4 HOH 93  968  93   HOH HOH A . 
H 4 HOH 94  969  94   HOH HOH A . 
H 4 HOH 95  970  95   HOH HOH A . 
H 4 HOH 96  971  96   HOH HOH A . 
H 4 HOH 97  972  97   HOH HOH A . 
H 4 HOH 98  973  98   HOH HOH A . 
H 4 HOH 99  974  99   HOH HOH A . 
H 4 HOH 100 975  100  HOH HOH A . 
H 4 HOH 101 976  101  HOH HOH A . 
H 4 HOH 102 977  102  HOH HOH A . 
H 4 HOH 103 978  103  HOH HOH A . 
H 4 HOH 104 979  104  HOH HOH A . 
H 4 HOH 105 980  105  HOH HOH A . 
H 4 HOH 106 981  106  HOH HOH A . 
H 4 HOH 107 982  107  HOH HOH A . 
H 4 HOH 108 983  108  HOH HOH A . 
H 4 HOH 109 984  109  HOH HOH A . 
H 4 HOH 110 985  110  HOH HOH A . 
H 4 HOH 111 986  111  HOH HOH A . 
H 4 HOH 112 987  112  HOH HOH A . 
H 4 HOH 113 988  113  HOH HOH A . 
H 4 HOH 114 989  114  HOH HOH A . 
H 4 HOH 115 990  115  HOH HOH A . 
H 4 HOH 116 991  116  HOH HOH A . 
H 4 HOH 117 992  117  HOH HOH A . 
H 4 HOH 118 993  118  HOH HOH A . 
H 4 HOH 119 994  119  HOH HOH A . 
H 4 HOH 120 995  120  HOH HOH A . 
H 4 HOH 121 996  121  HOH HOH A . 
H 4 HOH 122 997  122  HOH HOH A . 
H 4 HOH 123 998  123  HOH HOH A . 
H 4 HOH 124 999  124  HOH HOH A . 
H 4 HOH 125 1000 125  HOH HOH A . 
H 4 HOH 126 1002 126  HOH HOH A . 
H 4 HOH 127 1003 127  HOH HOH A . 
H 4 HOH 128 1004 128  HOH HOH A . 
H 4 HOH 129 1005 129  HOH HOH A . 
H 4 HOH 130 1006 130  HOH HOH A . 
H 4 HOH 131 1007 131  HOH HOH A . 
H 4 HOH 132 1008 132  HOH HOH A . 
H 4 HOH 133 1009 133  HOH HOH A . 
H 4 HOH 134 1010 134  HOH HOH A . 
H 4 HOH 135 1011 135  HOH HOH A . 
H 4 HOH 136 1012 136  HOH HOH A . 
H 4 HOH 137 1013 137  HOH HOH A . 
H 4 HOH 138 1014 138  HOH HOH A . 
H 4 HOH 139 1015 139  HOH HOH A . 
H 4 HOH 140 1016 140  HOH HOH A . 
H 4 HOH 141 1017 141  HOH HOH A . 
H 4 HOH 142 1018 142  HOH HOH A . 
H 4 HOH 143 1019 143  HOH HOH A . 
H 4 HOH 144 1020 144  HOH HOH A . 
H 4 HOH 145 1021 145  HOH HOH A . 
H 4 HOH 146 1022 146  HOH HOH A . 
H 4 HOH 147 1023 147  HOH HOH A . 
H 4 HOH 148 1024 148  HOH HOH A . 
H 4 HOH 149 1025 149  HOH HOH A . 
H 4 HOH 150 1026 150  HOH HOH A . 
H 4 HOH 151 1027 151  HOH HOH A . 
H 4 HOH 152 1028 152  HOH HOH A . 
H 4 HOH 153 1029 153  HOH HOH A . 
H 4 HOH 154 1030 154  HOH HOH A . 
H 4 HOH 155 1031 155  HOH HOH A . 
H 4 HOH 156 1032 156  HOH HOH A . 
H 4 HOH 157 1033 157  HOH HOH A . 
H 4 HOH 158 1034 158  HOH HOH A . 
H 4 HOH 159 1035 159  HOH HOH A . 
H 4 HOH 160 1036 160  HOH HOH A . 
H 4 HOH 161 1037 161  HOH HOH A . 
H 4 HOH 162 1038 162  HOH HOH A . 
H 4 HOH 163 1039 163  HOH HOH A . 
H 4 HOH 164 1040 164  HOH HOH A . 
H 4 HOH 165 1041 165  HOH HOH A . 
H 4 HOH 166 1042 166  HOH HOH A . 
H 4 HOH 167 1043 167  HOH HOH A . 
H 4 HOH 168 1044 168  HOH HOH A . 
H 4 HOH 169 1045 169  HOH HOH A . 
H 4 HOH 170 1046 170  HOH HOH A . 
H 4 HOH 171 1047 171  HOH HOH A . 
H 4 HOH 172 1048 172  HOH HOH A . 
H 4 HOH 173 1049 173  HOH HOH A . 
H 4 HOH 174 1050 174  HOH HOH A . 
H 4 HOH 175 1051 175  HOH HOH A . 
H 4 HOH 176 1052 176  HOH HOH A . 
H 4 HOH 177 1053 177  HOH HOH A . 
H 4 HOH 178 1054 178  HOH HOH A . 
H 4 HOH 179 1055 179  HOH HOH A . 
H 4 HOH 180 1056 180  HOH HOH A . 
H 4 HOH 181 1057 181  HOH HOH A . 
H 4 HOH 182 1058 182  HOH HOH A . 
H 4 HOH 183 1059 183  HOH HOH A . 
H 4 HOH 184 1060 184  HOH HOH A . 
H 4 HOH 185 1061 185  HOH HOH A . 
H 4 HOH 186 1062 186  HOH HOH A . 
H 4 HOH 187 1063 187  HOH HOH A . 
H 4 HOH 188 1064 188  HOH HOH A . 
H 4 HOH 189 1065 189  HOH HOH A . 
H 4 HOH 190 1066 190  HOH HOH A . 
H 4 HOH 191 1067 191  HOH HOH A . 
H 4 HOH 192 1068 192  HOH HOH A . 
H 4 HOH 193 1069 193  HOH HOH A . 
H 4 HOH 194 1070 194  HOH HOH A . 
H 4 HOH 195 1071 195  HOH HOH A . 
H 4 HOH 196 1072 196  HOH HOH A . 
H 4 HOH 197 1073 197  HOH HOH A . 
H 4 HOH 198 1074 198  HOH HOH A . 
H 4 HOH 199 1075 199  HOH HOH A . 
H 4 HOH 200 1076 200  HOH HOH A . 
H 4 HOH 201 1077 201  HOH HOH A . 
H 4 HOH 202 1078 202  HOH HOH A . 
H 4 HOH 203 1079 203  HOH HOH A . 
H 4 HOH 204 1080 204  HOH HOH A . 
H 4 HOH 205 1081 205  HOH HOH A . 
H 4 HOH 206 1082 206  HOH HOH A . 
H 4 HOH 207 1083 207  HOH HOH A . 
H 4 HOH 208 1084 208  HOH HOH A . 
H 4 HOH 209 1085 209  HOH HOH A . 
H 4 HOH 210 1086 210  HOH HOH A . 
H 4 HOH 211 1087 211  HOH HOH A . 
H 4 HOH 212 1088 212  HOH HOH A . 
H 4 HOH 213 1089 213  HOH HOH A . 
H 4 HOH 214 1090 214  HOH HOH A . 
H 4 HOH 215 1091 215  HOH HOH A . 
H 4 HOH 216 1092 216  HOH HOH A . 
H 4 HOH 217 1093 217  HOH HOH A . 
H 4 HOH 218 1094 218  HOH HOH A . 
H 4 HOH 219 1095 219  HOH HOH A . 
H 4 HOH 220 1096 220  HOH HOH A . 
H 4 HOH 221 1097 221  HOH HOH A . 
H 4 HOH 222 1098 222  HOH HOH A . 
H 4 HOH 223 1099 223  HOH HOH A . 
H 4 HOH 224 1100 224  HOH HOH A . 
H 4 HOH 225 1101 225  HOH HOH A . 
H 4 HOH 226 1102 226  HOH HOH A . 
H 4 HOH 227 1103 227  HOH HOH A . 
H 4 HOH 228 1104 228  HOH HOH A . 
H 4 HOH 229 1105 229  HOH HOH A . 
H 4 HOH 230 1106 230  HOH HOH A . 
H 4 HOH 231 1107 231  HOH HOH A . 
H 4 HOH 232 1108 232  HOH HOH A . 
H 4 HOH 233 1109 233  HOH HOH A . 
H 4 HOH 234 1110 234  HOH HOH A . 
H 4 HOH 235 1111 235  HOH HOH A . 
H 4 HOH 236 1112 236  HOH HOH A . 
H 4 HOH 237 1113 237  HOH HOH A . 
H 4 HOH 238 1114 238  HOH HOH A . 
H 4 HOH 239 1115 239  HOH HOH A . 
H 4 HOH 240 1116 240  HOH HOH A . 
H 4 HOH 241 1117 241  HOH HOH A . 
H 4 HOH 242 1118 242  HOH HOH A . 
H 4 HOH 243 1119 243  HOH HOH A . 
H 4 HOH 244 1120 244  HOH HOH A . 
H 4 HOH 245 1121 245  HOH HOH A . 
H 4 HOH 246 1122 246  HOH HOH A . 
H 4 HOH 247 1123 247  HOH HOH A . 
H 4 HOH 248 1124 248  HOH HOH A . 
H 4 HOH 249 1125 249  HOH HOH A . 
H 4 HOH 250 1126 250  HOH HOH A . 
H 4 HOH 251 1127 251  HOH HOH A . 
H 4 HOH 252 1128 252  HOH HOH A . 
H 4 HOH 253 1129 253  HOH HOH A . 
H 4 HOH 254 1130 254  HOH HOH A . 
H 4 HOH 255 1131 255  HOH HOH A . 
H 4 HOH 256 1132 256  HOH HOH A . 
H 4 HOH 257 1133 257  HOH HOH A . 
H 4 HOH 258 1134 258  HOH HOH A . 
H 4 HOH 259 1135 259  HOH HOH A . 
H 4 HOH 260 1136 260  HOH HOH A . 
H 4 HOH 261 1137 261  HOH HOH A . 
H 4 HOH 262 1138 262  HOH HOH A . 
H 4 HOH 263 1139 263  HOH HOH A . 
H 4 HOH 264 1140 264  HOH HOH A . 
H 4 HOH 265 1141 265  HOH HOH A . 
H 4 HOH 266 1142 266  HOH HOH A . 
H 4 HOH 267 1143 267  HOH HOH A . 
H 4 HOH 268 1144 268  HOH HOH A . 
H 4 HOH 269 1145 269  HOH HOH A . 
H 4 HOH 270 1146 270  HOH HOH A . 
H 4 HOH 271 1147 271  HOH HOH A . 
H 4 HOH 272 1148 272  HOH HOH A . 
H 4 HOH 273 1149 273  HOH HOH A . 
H 4 HOH 274 1150 274  HOH HOH A . 
H 4 HOH 275 1151 275  HOH HOH A . 
H 4 HOH 276 1152 276  HOH HOH A . 
H 4 HOH 277 1153 277  HOH HOH A . 
H 4 HOH 278 1154 278  HOH HOH A . 
H 4 HOH 279 1155 279  HOH HOH A . 
H 4 HOH 280 1156 280  HOH HOH A . 
H 4 HOH 281 1157 281  HOH HOH A . 
H 4 HOH 282 1158 282  HOH HOH A . 
H 4 HOH 283 1159 283  HOH HOH A . 
H 4 HOH 284 1160 284  HOH HOH A . 
H 4 HOH 285 1161 285  HOH HOH A . 
H 4 HOH 286 1162 286  HOH HOH A . 
H 4 HOH 287 1163 287  HOH HOH A . 
H 4 HOH 288 1164 288  HOH HOH A . 
H 4 HOH 289 1165 289  HOH HOH A . 
H 4 HOH 290 1166 290  HOH HOH A . 
H 4 HOH 291 1167 291  HOH HOH A . 
H 4 HOH 292 1168 292  HOH HOH A . 
H 4 HOH 293 1169 293  HOH HOH A . 
H 4 HOH 294 1170 294  HOH HOH A . 
H 4 HOH 295 1171 296  HOH HOH A . 
H 4 HOH 296 1172 297  HOH HOH A . 
H 4 HOH 297 1173 298  HOH HOH A . 
H 4 HOH 298 1174 299  HOH HOH A . 
H 4 HOH 299 1175 300  HOH HOH A . 
H 4 HOH 300 1176 301  HOH HOH A . 
H 4 HOH 301 1177 302  HOH HOH A . 
H 4 HOH 302 1178 303  HOH HOH A . 
H 4 HOH 303 1179 304  HOH HOH A . 
H 4 HOH 304 1180 305  HOH HOH A . 
H 4 HOH 305 1181 306  HOH HOH A . 
H 4 HOH 306 1182 307  HOH HOH A . 
H 4 HOH 307 1183 308  HOH HOH A . 
H 4 HOH 308 1184 309  HOH HOH A . 
H 4 HOH 309 1185 310  HOH HOH A . 
H 4 HOH 310 1186 311  HOH HOH A . 
H 4 HOH 311 1187 312  HOH HOH A . 
H 4 HOH 312 1188 313  HOH HOH A . 
H 4 HOH 313 1189 314  HOH HOH A . 
H 4 HOH 314 1190 315  HOH HOH A . 
H 4 HOH 315 1191 316  HOH HOH A . 
H 4 HOH 316 1192 317  HOH HOH A . 
H 4 HOH 317 1193 318  HOH HOH A . 
H 4 HOH 318 1194 319  HOH HOH A . 
H 4 HOH 319 1195 320  HOH HOH A . 
H 4 HOH 320 1196 321  HOH HOH A . 
H 4 HOH 321 1197 322  HOH HOH A . 
H 4 HOH 322 1198 323  HOH HOH A . 
H 4 HOH 323 1199 324  HOH HOH A . 
H 4 HOH 324 1200 325  HOH HOH A . 
H 4 HOH 325 1201 326  HOH HOH A . 
H 4 HOH 326 1202 327  HOH HOH A . 
H 4 HOH 327 1203 328  HOH HOH A . 
H 4 HOH 328 1204 329  HOH HOH A . 
H 4 HOH 329 1205 330  HOH HOH A . 
H 4 HOH 330 1206 331  HOH HOH A . 
H 4 HOH 331 1207 332  HOH HOH A . 
H 4 HOH 332 1208 333  HOH HOH A . 
H 4 HOH 333 1209 334  HOH HOH A . 
H 4 HOH 334 1210 335  HOH HOH A . 
H 4 HOH 335 1211 336  HOH HOH A . 
H 4 HOH 336 1212 338  HOH HOH A . 
H 4 HOH 337 1213 339  HOH HOH A . 
H 4 HOH 338 1214 340  HOH HOH A . 
H 4 HOH 339 1215 341  HOH HOH A . 
H 4 HOH 340 1216 342  HOH HOH A . 
H 4 HOH 341 1217 343  HOH HOH A . 
H 4 HOH 342 1218 344  HOH HOH A . 
H 4 HOH 343 1219 345  HOH HOH A . 
H 4 HOH 344 1220 346  HOH HOH A . 
H 4 HOH 345 1221 347  HOH HOH A . 
H 4 HOH 346 1222 348  HOH HOH A . 
H 4 HOH 347 1223 349  HOH HOH A . 
H 4 HOH 348 1224 350  HOH HOH A . 
H 4 HOH 349 1225 351  HOH HOH A . 
H 4 HOH 350 1226 353  HOH HOH A . 
H 4 HOH 351 1227 354  HOH HOH A . 
H 4 HOH 352 1228 355  HOH HOH A . 
H 4 HOH 353 1229 356  HOH HOH A . 
H 4 HOH 354 1230 357  HOH HOH A . 
H 4 HOH 355 1231 358  HOH HOH A . 
H 4 HOH 356 1232 359  HOH HOH A . 
H 4 HOH 357 1233 360  HOH HOH A . 
H 4 HOH 358 1234 361  HOH HOH A . 
H 4 HOH 359 1235 362  HOH HOH A . 
H 4 HOH 360 1236 364  HOH HOH A . 
H 4 HOH 361 1237 366  HOH HOH A . 
H 4 HOH 362 1238 367  HOH HOH A . 
H 4 HOH 363 1239 368  HOH HOH A . 
H 4 HOH 364 1240 369  HOH HOH A . 
H 4 HOH 365 1241 370  HOH HOH A . 
H 4 HOH 366 1242 371  HOH HOH A . 
H 4 HOH 367 1243 372  HOH HOH A . 
H 4 HOH 368 1244 373  HOH HOH A . 
H 4 HOH 369 1245 374  HOH HOH A . 
H 4 HOH 370 1246 375  HOH HOH A . 
H 4 HOH 371 1247 376  HOH HOH A . 
H 4 HOH 372 1248 377  HOH HOH A . 
H 4 HOH 373 1249 378  HOH HOH A . 
H 4 HOH 374 1250 379  HOH HOH A . 
H 4 HOH 375 1251 380  HOH HOH A . 
H 4 HOH 376 1252 381  HOH HOH A . 
H 4 HOH 377 1253 382  HOH HOH A . 
H 4 HOH 378 1254 383  HOH HOH A . 
H 4 HOH 379 1255 384  HOH HOH A . 
H 4 HOH 380 1256 385  HOH HOH A . 
H 4 HOH 381 1257 386  HOH HOH A . 
H 4 HOH 382 1258 387  HOH HOH A . 
H 4 HOH 383 1259 388  HOH HOH A . 
H 4 HOH 384 1260 389  HOH HOH A . 
H 4 HOH 385 1261 390  HOH HOH A . 
H 4 HOH 386 1262 391  HOH HOH A . 
H 4 HOH 387 1263 392  HOH HOH A . 
H 4 HOH 388 1264 393  HOH HOH A . 
H 4 HOH 389 1265 394  HOH HOH A . 
H 4 HOH 390 1266 395  HOH HOH A . 
H 4 HOH 391 1267 396  HOH HOH A . 
H 4 HOH 392 1268 397  HOH HOH A . 
H 4 HOH 393 1269 398  HOH HOH A . 
H 4 HOH 394 1270 399  HOH HOH A . 
H 4 HOH 395 1271 400  HOH HOH A . 
H 4 HOH 396 1272 401  HOH HOH A . 
H 4 HOH 397 1273 402  HOH HOH A . 
H 4 HOH 398 1274 403  HOH HOH A . 
H 4 HOH 399 1275 404  HOH HOH A . 
H 4 HOH 400 1276 405  HOH HOH A . 
H 4 HOH 401 1277 406  HOH HOH A . 
H 4 HOH 402 1278 407  HOH HOH A . 
H 4 HOH 403 1279 408  HOH HOH A . 
H 4 HOH 404 1280 409  HOH HOH A . 
H 4 HOH 405 1281 410  HOH HOH A . 
H 4 HOH 406 1282 411  HOH HOH A . 
H 4 HOH 407 1283 412  HOH HOH A . 
H 4 HOH 408 1284 413  HOH HOH A . 
H 4 HOH 409 1285 414  HOH HOH A . 
H 4 HOH 410 1286 415  HOH HOH A . 
H 4 HOH 411 1287 416  HOH HOH A . 
H 4 HOH 412 1288 417  HOH HOH A . 
H 4 HOH 413 1289 418  HOH HOH A . 
H 4 HOH 414 1290 419  HOH HOH A . 
H 4 HOH 415 1291 420  HOH HOH A . 
H 4 HOH 416 1292 421  HOH HOH A . 
H 4 HOH 417 1293 422  HOH HOH A . 
H 4 HOH 418 1294 423  HOH HOH A . 
H 4 HOH 419 1295 424  HOH HOH A . 
H 4 HOH 420 1296 425  HOH HOH A . 
H 4 HOH 421 1297 426  HOH HOH A . 
H 4 HOH 422 1298 427  HOH HOH A . 
H 4 HOH 423 1299 428  HOH HOH A . 
H 4 HOH 424 1300 429  HOH HOH A . 
H 4 HOH 425 1301 430  HOH HOH A . 
H 4 HOH 426 1302 431  HOH HOH A . 
H 4 HOH 427 1303 434  HOH HOH A . 
H 4 HOH 428 1304 435  HOH HOH A . 
H 4 HOH 429 1305 436  HOH HOH A . 
H 4 HOH 430 1306 437  HOH HOH A . 
H 4 HOH 431 1307 438  HOH HOH A . 
H 4 HOH 432 1308 439  HOH HOH A . 
H 4 HOH 433 1309 440  HOH HOH A . 
H 4 HOH 434 1310 441  HOH HOH A . 
H 4 HOH 435 1311 442  HOH HOH A . 
H 4 HOH 436 1312 443  HOH HOH A . 
H 4 HOH 437 1313 444  HOH HOH A . 
H 4 HOH 438 1314 445  HOH HOH A . 
H 4 HOH 439 1315 446  HOH HOH A . 
H 4 HOH 440 1316 447  HOH HOH A . 
H 4 HOH 441 1317 448  HOH HOH A . 
H 4 HOH 442 1318 449  HOH HOH A . 
H 4 HOH 443 1319 450  HOH HOH A . 
H 4 HOH 444 1320 451  HOH HOH A . 
H 4 HOH 445 1321 452  HOH HOH A . 
H 4 HOH 446 1322 453  HOH HOH A . 
H 4 HOH 447 1323 454  HOH HOH A . 
H 4 HOH 448 1324 455  HOH HOH A . 
H 4 HOH 449 1325 456  HOH HOH A . 
H 4 HOH 450 1326 457  HOH HOH A . 
H 4 HOH 451 1327 458  HOH HOH A . 
H 4 HOH 452 1328 459  HOH HOH A . 
H 4 HOH 453 1329 460  HOH HOH A . 
H 4 HOH 454 1330 461  HOH HOH A . 
H 4 HOH 455 1331 462  HOH HOH A . 
H 4 HOH 456 1332 463  HOH HOH A . 
H 4 HOH 457 1333 464  HOH HOH A . 
H 4 HOH 458 1334 465  HOH HOH A . 
H 4 HOH 459 1335 466  HOH HOH A . 
H 4 HOH 460 1336 467  HOH HOH A . 
H 4 HOH 461 1337 468  HOH HOH A . 
H 4 HOH 462 1338 469  HOH HOH A . 
H 4 HOH 463 1339 470  HOH HOH A . 
H 4 HOH 464 1340 471  HOH HOH A . 
H 4 HOH 465 1341 472  HOH HOH A . 
H 4 HOH 466 1342 473  HOH HOH A . 
H 4 HOH 467 1343 474  HOH HOH A . 
H 4 HOH 468 1344 475  HOH HOH A . 
H 4 HOH 469 1345 476  HOH HOH A . 
H 4 HOH 470 1346 477  HOH HOH A . 
H 4 HOH 471 1347 478  HOH HOH A . 
H 4 HOH 472 1348 479  HOH HOH A . 
H 4 HOH 473 1349 480  HOH HOH A . 
H 4 HOH 474 1350 481  HOH HOH A . 
H 4 HOH 475 1351 482  HOH HOH A . 
H 4 HOH 476 1352 483  HOH HOH A . 
H 4 HOH 477 1353 484  HOH HOH A . 
H 4 HOH 478 1354 485  HOH HOH A . 
H 4 HOH 479 1355 486  HOH HOH A . 
H 4 HOH 480 1356 487  HOH HOH A . 
H 4 HOH 481 1357 488  HOH HOH A . 
H 4 HOH 482 1358 489  HOH HOH A . 
H 4 HOH 483 1359 490  HOH HOH A . 
H 4 HOH 484 1360 491  HOH HOH A . 
H 4 HOH 485 1361 492  HOH HOH A . 
H 4 HOH 486 1362 493  HOH HOH A . 
H 4 HOH 487 1363 494  HOH HOH A . 
H 4 HOH 488 1364 495  HOH HOH A . 
H 4 HOH 489 1365 496  HOH HOH A . 
H 4 HOH 490 1366 497  HOH HOH A . 
H 4 HOH 491 1367 498  HOH HOH A . 
H 4 HOH 492 1368 499  HOH HOH A . 
H 4 HOH 493 1369 500  HOH HOH A . 
H 4 HOH 494 1370 501  HOH HOH A . 
H 4 HOH 495 1371 502  HOH HOH A . 
H 4 HOH 496 1372 503  HOH HOH A . 
H 4 HOH 497 1373 504  HOH HOH A . 
H 4 HOH 498 1374 505  HOH HOH A . 
H 4 HOH 499 1375 506  HOH HOH A . 
H 4 HOH 500 1376 507  HOH HOH A . 
H 4 HOH 501 1377 508  HOH HOH A . 
H 4 HOH 502 1378 509  HOH HOH A . 
H 4 HOH 503 1379 510  HOH HOH A . 
H 4 HOH 504 1380 511  HOH HOH A . 
H 4 HOH 505 1381 512  HOH HOH A . 
H 4 HOH 506 1382 513  HOH HOH A . 
H 4 HOH 507 1383 514  HOH HOH A . 
H 4 HOH 508 1384 515  HOH HOH A . 
H 4 HOH 509 1385 516  HOH HOH A . 
H 4 HOH 510 1386 517  HOH HOH A . 
H 4 HOH 511 1387 518  HOH HOH A . 
H 4 HOH 512 1388 519  HOH HOH A . 
H 4 HOH 513 1389 520  HOH HOH A . 
H 4 HOH 514 1390 521  HOH HOH A . 
H 4 HOH 515 1391 522  HOH HOH A . 
H 4 HOH 516 1392 523  HOH HOH A . 
H 4 HOH 517 1393 524  HOH HOH A . 
H 4 HOH 518 1394 525  HOH HOH A . 
H 4 HOH 519 1395 526  HOH HOH A . 
H 4 HOH 520 1396 527  HOH HOH A . 
H 4 HOH 521 1397 528  HOH HOH A . 
H 4 HOH 522 1398 529  HOH HOH A . 
H 4 HOH 523 1399 530  HOH HOH A . 
H 4 HOH 524 1400 531  HOH HOH A . 
H 4 HOH 525 1401 532  HOH HOH A . 
H 4 HOH 526 1402 533  HOH HOH A . 
H 4 HOH 527 1403 534  HOH HOH A . 
H 4 HOH 528 1404 535  HOH HOH A . 
H 4 HOH 529 1405 536  HOH HOH A . 
H 4 HOH 530 1406 537  HOH HOH A . 
H 4 HOH 531 1407 538  HOH HOH A . 
H 4 HOH 532 1408 539  HOH HOH A . 
H 4 HOH 533 1409 540  HOH HOH A . 
H 4 HOH 534 1410 541  HOH HOH A . 
H 4 HOH 535 1411 542  HOH HOH A . 
H 4 HOH 536 1412 543  HOH HOH A . 
H 4 HOH 537 1413 544  HOH HOH A . 
H 4 HOH 538 1414 545  HOH HOH A . 
H 4 HOH 539 1415 546  HOH HOH A . 
H 4 HOH 540 1416 547  HOH HOH A . 
H 4 HOH 541 1417 548  HOH HOH A . 
H 4 HOH 542 1418 549  HOH HOH A . 
H 4 HOH 543 1419 550  HOH HOH A . 
H 4 HOH 544 1420 551  HOH HOH A . 
H 4 HOH 545 1421 552  HOH HOH A . 
H 4 HOH 546 1422 553  HOH HOH A . 
H 4 HOH 547 1423 554  HOH HOH A . 
H 4 HOH 548 1424 555  HOH HOH A . 
H 4 HOH 549 1425 556  HOH HOH A . 
H 4 HOH 550 1426 557  HOH HOH A . 
H 4 HOH 551 1427 558  HOH HOH A . 
H 4 HOH 552 1428 559  HOH HOH A . 
H 4 HOH 553 1429 560  HOH HOH A . 
H 4 HOH 554 1430 561  HOH HOH A . 
H 4 HOH 555 1431 562  HOH HOH A . 
H 4 HOH 556 1432 563  HOH HOH A . 
H 4 HOH 557 1433 564  HOH HOH A . 
H 4 HOH 558 1434 565  HOH HOH A . 
H 4 HOH 559 1435 566  HOH HOH A . 
H 4 HOH 560 1436 567  HOH HOH A . 
H 4 HOH 561 1437 568  HOH HOH A . 
H 4 HOH 562 1438 569  HOH HOH A . 
H 4 HOH 563 1439 570  HOH HOH A . 
H 4 HOH 564 1440 571  HOH HOH A . 
H 4 HOH 565 1441 572  HOH HOH A . 
H 4 HOH 566 1442 573  HOH HOH A . 
H 4 HOH 567 1443 574  HOH HOH A . 
H 4 HOH 568 1444 575  HOH HOH A . 
H 4 HOH 569 1445 576  HOH HOH A . 
H 4 HOH 570 1446 577  HOH HOH A . 
H 4 HOH 571 1447 578  HOH HOH A . 
H 4 HOH 572 1448 579  HOH HOH A . 
H 4 HOH 573 1449 580  HOH HOH A . 
H 4 HOH 574 1450 581  HOH HOH A . 
H 4 HOH 575 1451 582  HOH HOH A . 
H 4 HOH 576 1452 583  HOH HOH A . 
H 4 HOH 577 1453 584  HOH HOH A . 
H 4 HOH 578 1454 585  HOH HOH A . 
H 4 HOH 579 1455 586  HOH HOH A . 
H 4 HOH 580 1456 587  HOH HOH A . 
H 4 HOH 581 1457 588  HOH HOH A . 
H 4 HOH 582 1458 589  HOH HOH A . 
H 4 HOH 583 1459 590  HOH HOH A . 
H 4 HOH 584 1460 591  HOH HOH A . 
H 4 HOH 585 1461 592  HOH HOH A . 
H 4 HOH 586 1462 593  HOH HOH A . 
H 4 HOH 587 1463 594  HOH HOH A . 
H 4 HOH 588 1464 595  HOH HOH A . 
H 4 HOH 589 1465 596  HOH HOH A . 
H 4 HOH 590 1466 597  HOH HOH A . 
H 4 HOH 591 1467 598  HOH HOH A . 
H 4 HOH 592 1468 599  HOH HOH A . 
H 4 HOH 593 1469 600  HOH HOH A . 
H 4 HOH 594 1470 601  HOH HOH A . 
H 4 HOH 595 1471 602  HOH HOH A . 
H 4 HOH 596 1472 603  HOH HOH A . 
H 4 HOH 597 1473 604  HOH HOH A . 
H 4 HOH 598 1474 605  HOH HOH A . 
H 4 HOH 599 1475 606  HOH HOH A . 
H 4 HOH 600 1476 607  HOH HOH A . 
H 4 HOH 601 1477 608  HOH HOH A . 
H 4 HOH 602 1478 609  HOH HOH A . 
H 4 HOH 603 1479 610  HOH HOH A . 
H 4 HOH 604 1480 611  HOH HOH A . 
H 4 HOH 605 1481 612  HOH HOH A . 
H 4 HOH 606 1482 613  HOH HOH A . 
H 4 HOH 607 1483 614  HOH HOH A . 
H 4 HOH 608 1484 615  HOH HOH A . 
H 4 HOH 609 1485 616  HOH HOH A . 
H 4 HOH 610 1486 617  HOH HOH A . 
H 4 HOH 611 1487 618  HOH HOH A . 
H 4 HOH 612 1488 619  HOH HOH A . 
H 4 HOH 613 1489 620  HOH HOH A . 
H 4 HOH 614 1490 621  HOH HOH A . 
H 4 HOH 615 1491 622  HOH HOH A . 
H 4 HOH 616 1492 623  HOH HOH A . 
H 4 HOH 617 1493 624  HOH HOH A . 
H 4 HOH 618 1494 625  HOH HOH A . 
H 4 HOH 619 1495 626  HOH HOH A . 
H 4 HOH 620 1496 627  HOH HOH A . 
H 4 HOH 621 1497 628  HOH HOH A . 
H 4 HOH 622 1498 629  HOH HOH A . 
H 4 HOH 623 1499 630  HOH HOH A . 
H 4 HOH 624 1500 631  HOH HOH A . 
H 4 HOH 625 1501 632  HOH HOH A . 
H 4 HOH 626 1502 633  HOH HOH A . 
H 4 HOH 627 1503 634  HOH HOH A . 
H 4 HOH 628 1504 635  HOH HOH A . 
H 4 HOH 629 1505 636  HOH HOH A . 
H 4 HOH 630 1506 637  HOH HOH A . 
H 4 HOH 631 1507 638  HOH HOH A . 
H 4 HOH 632 1508 639  HOH HOH A . 
H 4 HOH 633 1509 640  HOH HOH A . 
H 4 HOH 634 1510 641  HOH HOH A . 
H 4 HOH 635 1511 642  HOH HOH A . 
H 4 HOH 636 1512 643  HOH HOH A . 
H 4 HOH 637 1513 644  HOH HOH A . 
H 4 HOH 638 1514 645  HOH HOH A . 
H 4 HOH 639 1515 646  HOH HOH A . 
H 4 HOH 640 1516 647  HOH HOH A . 
H 4 HOH 641 1517 648  HOH HOH A . 
H 4 HOH 642 1518 649  HOH HOH A . 
H 4 HOH 643 1519 650  HOH HOH A . 
H 4 HOH 644 1520 651  HOH HOH A . 
H 4 HOH 645 1521 652  HOH HOH A . 
H 4 HOH 646 1522 653  HOH HOH A . 
H 4 HOH 647 1523 654  HOH HOH A . 
H 4 HOH 648 1524 655  HOH HOH A . 
H 4 HOH 649 1525 657  HOH HOH A . 
H 4 HOH 650 1526 658  HOH HOH A . 
H 4 HOH 651 1527 659  HOH HOH A . 
H 4 HOH 652 1528 660  HOH HOH A . 
H 4 HOH 653 1529 662  HOH HOH A . 
H 4 HOH 654 1530 663  HOH HOH A . 
H 4 HOH 655 1531 664  HOH HOH A . 
H 4 HOH 656 1532 665  HOH HOH A . 
H 4 HOH 657 1533 666  HOH HOH A . 
H 4 HOH 658 1534 667  HOH HOH A . 
H 4 HOH 659 1535 668  HOH HOH A . 
H 4 HOH 660 1536 669  HOH HOH A . 
H 4 HOH 661 1537 670  HOH HOH A . 
H 4 HOH 662 1538 671  HOH HOH A . 
H 4 HOH 663 1539 672  HOH HOH A . 
H 4 HOH 664 1540 673  HOH HOH A . 
H 4 HOH 665 1541 674  HOH HOH A . 
H 4 HOH 666 1542 675  HOH HOH A . 
H 4 HOH 667 1543 676  HOH HOH A . 
H 4 HOH 668 1544 677  HOH HOH A . 
H 4 HOH 669 1545 678  HOH HOH A . 
H 4 HOH 670 1546 679  HOH HOH A . 
H 4 HOH 671 1547 680  HOH HOH A . 
H 4 HOH 672 1548 681  HOH HOH A . 
H 4 HOH 673 1549 682  HOH HOH A . 
H 4 HOH 674 1550 683  HOH HOH A . 
H 4 HOH 675 1551 684  HOH HOH A . 
H 4 HOH 676 1552 685  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 209 A ASN 209 ? ASN 'GLYCOSYLATION SITE' 
3 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 
# 
_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++        ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SG  A CYS 479  ? B O   A HOH 1151 ? ? 1.97 
2 1 OD1 A ASP 191  ? ? O   A HOH 1286 ? ? 2.06 
3 1 O   A GLY 56   ? ? NH1 A ARG 135  ? ? 2.07 
4 1 O   A HOH 1217 ? ? O   A HOH 1232 ? ? 2.19 
# 
_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              189 
_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              189 
_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              189 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                116.62 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.68 
_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 34  ? ? -155.72 85.32   
2  1 PRO A 35  ? ? -67.70  7.64    
3  1 SER A 40  ? ? 79.73   -14.23  
4  1 HIS A 50  ? ? 78.24   156.47  
5  1 SER A 51  ? ? 128.70  -126.50 
6  1 VAL A 77  ? ? -88.87  -77.49  
7  1 PHE A 78  ? ? -115.36 76.93   
8  1 LEU A 151 ? ? -97.40  -64.22  
9  1 PHE A 161 ? ? -150.52 74.41   
10 1 PHE A 165 ? ? -162.66 106.62  
11 1 LEU A 180 ? ? 68.20   148.98  
12 1 GLN A 186 ? ? 79.51   -45.98  
13 1 MET A 192 ? ? 81.80   6.53    
14 1 MET A 192 ? ? 81.80   6.53    
15 1 ASN A 193 ? B -50.76  -163.76 
16 1 TRP A 194 ? ? -57.32  108.92  
17 1 PHE A 200 ? ? -170.78 115.56  
18 1 ASN A 207 ? ? -124.88 -165.25 
19 1 LEU A 213 ? ? -115.04 -147.43 
20 1 GLU A 300 ? ? 77.05   65.80   
21 1 TYR A 321 ? ? -163.90 96.69   
22 1 VAL A 342 ? ? -98.97  -66.70  
23 1 VAL A 405 ? ? -134.52 -147.41 
24 1 ASP A 474 ? ? 76.33   -5.04   
25 1 THR A 481 ? ? -152.15 -156.67 
26 1 SER A 521 ? ? 53.93   -144.03 
27 1 ILE A 565 ? ? -116.72 69.93   
28 1 CYS A 573 ? ? 78.65   -9.98   
29 1 LEU A 577 ? ? 87.27   158.00  
30 1 VAL A 651 ? ? -105.09 -68.01  
31 1 PRO A 721 ? ? -59.17  174.73  
32 1 GLU A 774 ? ? -150.61 -22.74  
33 1 VAL A 783 ? ? -110.44 77.70   
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     2002 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
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,3R,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium-1-yl]-1-hydroxyethyl}-2,3,4,5-tetrahydroxypentyl sulfate
;
KTL 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 water HOH 
# 
