data_9E4V
# 
_entry.id   9E4V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9E4V         pdb_00009e4v 10.2210/pdb9e4v/pdb 
WWPDB D_1000288280 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9E4V 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9DKP 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              james.moody@byu.edu 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Moody 
_pdbx_contact_author.name_mi            D 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2266-5348 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Abiodun, W.O.' 1 0000-0003-0312-2858 
'Fullmer, A.'   2 0009-0001-8014-9643 
'Tsubaki, E.'   3 ?                   
'Doukov, T.'    4 0000-0001-8625-2572 
'Moody, J.D.'   5 0000-0003-2266-5348 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Facile Bacterial Production of Human Vacuolar Protein Sorting 34 Enables Structural Characterization of Novel Inhibitors' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Abiodun, W.O.'   1  0000-0003-0312-2858 
primary 'Dass, R.'        2  ?                   
primary 'Fullmer, A.'     3  ?                   
primary 'Singleton, J.D.' 4  ?                   
primary 'Tsubaki, E.'     5  0009-0001-8014-9643 
primary 'Cartwright, J.'  6  ?                   
primary 'Litchfield, C.'  7  0000-0003-1004-0156 
primary 'Doukov, T.'      8  0000-0001-8625-2572 
primary 'Peterson, M.A.'  9  ?                   
primary 'Moody, J.D.'     10 0000-0003-2266-5348 
# 
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 'Phosphatidylinositol 3-kinase catalytic subunit type 3' 68149.867 1  2.7.1.137 ? ? ? 
2 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                   195.237   1  ?         ? ? ? 
3 non-polymer syn 'TETRAETHYLENE GLYCOL'                                   194.226   1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                     78.133    1  ?         ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                  106.120   4  ?         ? ? ? 
6 non-polymer syn GLYCEROL                                                 92.094    1  ?         ? ? ? 
7 non-polymer syn 'CHLORIDE ION'                                           35.453    4  ?         ? ? ? 
8 non-polymer syn 'POTASSIUM ION'                                          39.098    3  ?         ? ? ? 
9 water       nat water                                                    18.015    91 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;PI3-kinase type 3,PI3K type 3,PtdIns-3-kinase type 3,Phosphatidylinositol 3-kinase p100 subunit,Phosphoinositide-3-kinase class 3,hVps34
;
# 
_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       
;MGHHHHHHHHHHAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKP
MDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINS
AEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMY
LNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEP
QVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATST
KHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKL
FHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDK
TVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGHHHHHHHHHHAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKP
MDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINS
AEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMY
LNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEP
QVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATST
KHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKL
FHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDK
TVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALF
;
_entity_poly.pdbx_strand_id                 B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
3 'TETRAETHYLENE GLYCOL'                 PG4 
4 'DIMETHYL SULFOXIDE'                   DMS 
5 'DI(HYDROXYETHYL)ETHER'                PEG 
6 GLYCEROL                               GOL 
7 'CHLORIDE ION'                         CL  
8 'POTASSIUM ION'                        K   
9 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  HIS n 
1 12  HIS n 
1 13  ALA n 
1 14  ALA n 
1 15  THR n 
1 16  ARG n 
1 17  ASP n 
1 18  GLN n 
1 19  LEU n 
1 20  ASN n 
1 21  ILE n 
1 22  ILE n 
1 23  VAL n 
1 24  SER n 
1 25  TYR n 
1 26  PRO n 
1 27  PRO n 
1 28  THR n 
1 29  LYS n 
1 30  GLN n 
1 31  LEU n 
1 32  THR n 
1 33  TYR n 
1 34  GLU n 
1 35  GLU n 
1 36  GLN n 
1 37  ASP n 
1 38  LEU n 
1 39  VAL n 
1 40  TRP n 
1 41  LYS n 
1 42  PHE n 
1 43  ARG n 
1 44  TYR n 
1 45  TYR n 
1 46  LEU n 
1 47  THR n 
1 48  ASN n 
1 49  GLN n 
1 50  GLU n 
1 51  LYS n 
1 52  ALA n 
1 53  LEU n 
1 54  THR n 
1 55  LYS n 
1 56  PHE n 
1 57  LEU n 
1 58  LYS n 
1 59  CYS n 
1 60  VAL n 
1 61  ASN n 
1 62  TRP n 
1 63  ASP n 
1 64  LEU n 
1 65  PRO n 
1 66  GLN n 
1 67  GLU n 
1 68  ALA n 
1 69  LYS n 
1 70  GLN n 
1 71  ALA n 
1 72  LEU n 
1 73  GLU n 
1 74  LEU n 
1 75  LEU n 
1 76  GLY n 
1 77  LYS n 
1 78  TRP n 
1 79  LYS n 
1 80  PRO n 
1 81  MET n 
1 82  ASP n 
1 83  VAL n 
1 84  GLU n 
1 85  ASP n 
1 86  SER n 
1 87  LEU n 
1 88  GLU n 
1 89  LEU n 
1 90  LEU n 
1 91  SER n 
1 92  SER n 
1 93  HIS n 
1 94  TYR n 
1 95  THR n 
1 96  ASN n 
1 97  PRO n 
1 98  THR n 
1 99  VAL n 
1 100 ARG n 
1 101 ARG n 
1 102 TYR n 
1 103 ALA n 
1 104 VAL n 
1 105 ALA n 
1 106 ARG n 
1 107 LEU n 
1 108 ARG n 
1 109 GLN n 
1 110 ALA n 
1 111 ASP n 
1 112 ASP n 
1 113 GLU n 
1 114 ASP n 
1 115 LEU n 
1 116 LEU n 
1 117 MET n 
1 118 TYR n 
1 119 LEU n 
1 120 LEU n 
1 121 GLN n 
1 122 LEU n 
1 123 VAL n 
1 124 GLN n 
1 125 ALA n 
1 126 LEU n 
1 127 LYS n 
1 128 TYR n 
1 129 GLU n 
1 130 ASN n 
1 131 PHE n 
1 132 ASP n 
1 133 ASP n 
1 134 ILE n 
1 135 LYS n 
1 136 ASN n 
1 137 GLY n 
1 138 LEU n 
1 139 GLU n 
1 140 PRO n 
1 141 THR n 
1 142 LYS n 
1 143 LYS n 
1 144 ASP n 
1 145 SER n 
1 146 GLN n 
1 147 SER n 
1 148 SER n 
1 149 VAL n 
1 150 SER n 
1 151 GLU n 
1 152 ASN n 
1 153 VAL n 
1 154 SER n 
1 155 ASN n 
1 156 SER n 
1 157 GLY n 
1 158 ILE n 
1 159 ASN n 
1 160 SER n 
1 161 ALA n 
1 162 GLU n 
1 163 ILE n 
1 164 ASP n 
1 165 SER n 
1 166 SER n 
1 167 GLN n 
1 168 ILE n 
1 169 ILE n 
1 170 THR n 
1 171 SER n 
1 172 PRO n 
1 173 LEU n 
1 174 PRO n 
1 175 SER n 
1 176 VAL n 
1 177 SER n 
1 178 SER n 
1 179 PRO n 
1 180 PRO n 
1 181 PRO n 
1 182 ALA n 
1 183 SER n 
1 184 LYS n 
1 185 THR n 
1 186 LYS n 
1 187 GLU n 
1 188 VAL n 
1 189 PRO n 
1 190 ASP n 
1 191 GLY n 
1 192 GLU n 
1 193 ASN n 
1 194 LEU n 
1 195 GLU n 
1 196 GLN n 
1 197 ASP n 
1 198 LEU n 
1 199 CYS n 
1 200 THR n 
1 201 PHE n 
1 202 LEU n 
1 203 ILE n 
1 204 SER n 
1 205 ARG n 
1 206 ALA n 
1 207 CYS n 
1 208 LYS n 
1 209 ASN n 
1 210 SER n 
1 211 THR n 
1 212 LEU n 
1 213 ALA n 
1 214 ASN n 
1 215 TYR n 
1 216 LEU n 
1 217 TYR n 
1 218 TRP n 
1 219 TYR n 
1 220 VAL n 
1 221 ILE n 
1 222 VAL n 
1 223 GLU n 
1 224 CYS n 
1 225 GLU n 
1 226 ASP n 
1 227 GLN n 
1 228 ASP n 
1 229 THR n 
1 230 GLN n 
1 231 GLN n 
1 232 ARG n 
1 233 ASP n 
1 234 PRO n 
1 235 LYS n 
1 236 THR n 
1 237 HIS n 
1 238 GLU n 
1 239 MET n 
1 240 TYR n 
1 241 LEU n 
1 242 ASN n 
1 243 VAL n 
1 244 MET n 
1 245 ARG n 
1 246 ARG n 
1 247 PHE n 
1 248 SER n 
1 249 GLN n 
1 250 ALA n 
1 251 LEU n 
1 252 LEU n 
1 253 LYS n 
1 254 GLY n 
1 255 ASP n 
1 256 LYS n 
1 257 SER n 
1 258 VAL n 
1 259 ARG n 
1 260 VAL n 
1 261 MET n 
1 262 ARG n 
1 263 SER n 
1 264 LEU n 
1 265 LEU n 
1 266 ALA n 
1 267 ALA n 
1 268 GLN n 
1 269 GLN n 
1 270 THR n 
1 271 PHE n 
1 272 VAL n 
1 273 ASP n 
1 274 ARG n 
1 275 LEU n 
1 276 VAL n 
1 277 HIS n 
1 278 LEU n 
1 279 MET n 
1 280 LYS n 
1 281 ALA n 
1 282 VAL n 
1 283 GLN n 
1 284 ARG n 
1 285 GLU n 
1 286 SER n 
1 287 GLY n 
1 288 ASN n 
1 289 ARG n 
1 290 LYS n 
1 291 LYS n 
1 292 LYS n 
1 293 ASN n 
1 294 GLU n 
1 295 ARG n 
1 296 LEU n 
1 297 GLN n 
1 298 ALA n 
1 299 LEU n 
1 300 LEU n 
1 301 GLY n 
1 302 ASP n 
1 303 ASN n 
1 304 GLU n 
1 305 LYS n 
1 306 MET n 
1 307 ASN n 
1 308 LEU n 
1 309 SER n 
1 310 ASP n 
1 311 VAL n 
1 312 GLU n 
1 313 LEU n 
1 314 ILE n 
1 315 PRO n 
1 316 LEU n 
1 317 PRO n 
1 318 LEU n 
1 319 GLU n 
1 320 PRO n 
1 321 GLN n 
1 322 VAL n 
1 323 LYS n 
1 324 ILE n 
1 325 ARG n 
1 326 GLY n 
1 327 ILE n 
1 328 ILE n 
1 329 PRO n 
1 330 GLU n 
1 331 THR n 
1 332 ALA n 
1 333 THR n 
1 334 LEU n 
1 335 PHE n 
1 336 LYS n 
1 337 SER n 
1 338 ALA n 
1 339 LEU n 
1 340 MET n 
1 341 PRO n 
1 342 ALA n 
1 343 GLN n 
1 344 LEU n 
1 345 PHE n 
1 346 PHE n 
1 347 LYS n 
1 348 THR n 
1 349 GLU n 
1 350 ASP n 
1 351 GLY n 
1 352 GLY n 
1 353 LYS n 
1 354 TYR n 
1 355 PRO n 
1 356 VAL n 
1 357 ILE n 
1 358 PHE n 
1 359 LYS n 
1 360 HIS n 
1 361 GLY n 
1 362 ASP n 
1 363 ASP n 
1 364 LEU n 
1 365 ARG n 
1 366 GLN n 
1 367 ASP n 
1 368 GLN n 
1 369 LEU n 
1 370 ILE n 
1 371 LEU n 
1 372 GLN n 
1 373 ILE n 
1 374 ILE n 
1 375 SER n 
1 376 LEU n 
1 377 MET n 
1 378 ASP n 
1 379 LYS n 
1 380 LEU n 
1 381 LEU n 
1 382 ARG n 
1 383 LYS n 
1 384 GLU n 
1 385 ASN n 
1 386 LEU n 
1 387 ASP n 
1 388 LEU n 
1 389 LYS n 
1 390 LEU n 
1 391 THR n 
1 392 PRO n 
1 393 TYR n 
1 394 LYS n 
1 395 VAL n 
1 396 LEU n 
1 397 ALA n 
1 398 THR n 
1 399 SER n 
1 400 THR n 
1 401 LYS n 
1 402 HIS n 
1 403 GLY n 
1 404 PHE n 
1 405 MET n 
1 406 GLN n 
1 407 PHE n 
1 408 ILE n 
1 409 GLN n 
1 410 SER n 
1 411 VAL n 
1 412 PRO n 
1 413 VAL n 
1 414 ALA n 
1 415 GLU n 
1 416 VAL n 
1 417 LEU n 
1 418 ASP n 
1 419 THR n 
1 420 GLU n 
1 421 GLY n 
1 422 SER n 
1 423 ILE n 
1 424 GLN n 
1 425 ASN n 
1 426 PHE n 
1 427 PHE n 
1 428 ARG n 
1 429 LYS n 
1 430 TYR n 
1 431 ALA n 
1 432 PRO n 
1 433 SER n 
1 434 GLU n 
1 435 ASN n 
1 436 GLY n 
1 437 PRO n 
1 438 ASN n 
1 439 GLY n 
1 440 ILE n 
1 441 SER n 
1 442 ALA n 
1 443 GLU n 
1 444 VAL n 
1 445 MET n 
1 446 ASP n 
1 447 THR n 
1 448 TYR n 
1 449 VAL n 
1 450 LYS n 
1 451 SER n 
1 452 CYS n 
1 453 ALA n 
1 454 GLY n 
1 455 TYR n 
1 456 CYS n 
1 457 VAL n 
1 458 ILE n 
1 459 THR n 
1 460 TYR n 
1 461 ILE n 
1 462 LEU n 
1 463 GLY n 
1 464 VAL n 
1 465 GLY n 
1 466 ASP n 
1 467 ARG n 
1 468 HIS n 
1 469 LEU n 
1 470 ASP n 
1 471 ASN n 
1 472 LEU n 
1 473 LEU n 
1 474 LEU n 
1 475 THR n 
1 476 LYS n 
1 477 THR n 
1 478 GLY n 
1 479 LYS n 
1 480 LEU n 
1 481 PHE n 
1 482 HIS n 
1 483 ILE n 
1 484 ASP n 
1 485 PHE n 
1 486 GLY n 
1 487 TYR n 
1 488 ILE n 
1 489 LEU n 
1 490 GLY n 
1 491 ARG n 
1 492 ASP n 
1 493 PRO n 
1 494 LYS n 
1 495 PRO n 
1 496 LEU n 
1 497 PRO n 
1 498 PRO n 
1 499 PRO n 
1 500 MET n 
1 501 LYS n 
1 502 LEU n 
1 503 ASN n 
1 504 LYS n 
1 505 GLU n 
1 506 MET n 
1 507 VAL n 
1 508 GLU n 
1 509 GLY n 
1 510 MET n 
1 511 GLY n 
1 512 GLY n 
1 513 THR n 
1 514 GLN n 
1 515 SER n 
1 516 GLU n 
1 517 GLN n 
1 518 TYR n 
1 519 GLN n 
1 520 GLU n 
1 521 PHE n 
1 522 ARG n 
1 523 LYS n 
1 524 GLN n 
1 525 CYS n 
1 526 TYR n 
1 527 THR n 
1 528 ALA n 
1 529 PHE n 
1 530 LEU n 
1 531 HIS n 
1 532 LEU n 
1 533 ARG n 
1 534 ARG n 
1 535 TYR n 
1 536 SER n 
1 537 ASN n 
1 538 LEU n 
1 539 ILE n 
1 540 LEU n 
1 541 ASN n 
1 542 LEU n 
1 543 PHE n 
1 544 SER n 
1 545 LEU n 
1 546 MET n 
1 547 VAL n 
1 548 ASP n 
1 549 ALA n 
1 550 ASN n 
1 551 ILE n 
1 552 PRO n 
1 553 ASP n 
1 554 ILE n 
1 555 ALA n 
1 556 LEU n 
1 557 GLU n 
1 558 PRO n 
1 559 ASP n 
1 560 LYS n 
1 561 THR n 
1 562 VAL n 
1 563 LYS n 
1 564 LYS n 
1 565 VAL n 
1 566 GLN n 
1 567 ASP n 
1 568 LYS n 
1 569 PHE n 
1 570 ARG n 
1 571 LEU n 
1 572 ASP n 
1 573 LEU n 
1 574 SER n 
1 575 ASP n 
1 576 GLU n 
1 577 GLU n 
1 578 ALA n 
1 579 VAL n 
1 580 HIS n 
1 581 TYR n 
1 582 MET n 
1 583 GLN n 
1 584 SER n 
1 585 LEU n 
1 586 ILE n 
1 587 ASP n 
1 588 GLU n 
1 589 SER n 
1 590 VAL n 
1 591 HIS n 
1 592 ALA n 
1 593 LEU n 
1 594 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   594 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PIK3C3, VPS34' 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               B 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   Kanamycin 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET42_SUMO 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CL  non-polymer         . 'CHLORIDE ION'                         ?                               'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                               ?                               'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                   ?                               'C2 H6 O S'      78.133  
GLN 'L-peptide linking' y GLUTAMINE                              ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                        ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                               'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                              ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                  ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                             ?                               'C6 H13 N O2'    131.173 
K   non-polymer         . 'POTASSIUM ION'                        ?                               'K 1'            39.098  
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ?                               'C6 H13 N O4 S'  195.237 
MET 'L-peptide linking' y METHIONINE                             ?                               'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                ?                               'C4 H10 O3'      106.120 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'                 ?                               'C8 H18 O5'      194.226 
PHE 'L-peptide linking' y PHENYLALANINE                          ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                 ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                              ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                             ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                               ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                 ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   278 ?   ?   ?   B . n 
A 1 2   GLY 2   279 ?   ?   ?   B . n 
A 1 3   HIS 3   280 ?   ?   ?   B . n 
A 1 4   HIS 4   281 ?   ?   ?   B . n 
A 1 5   HIS 5   282 ?   ?   ?   B . n 
A 1 6   HIS 6   283 ?   ?   ?   B . n 
A 1 7   HIS 7   284 ?   ?   ?   B . n 
A 1 8   HIS 8   285 ?   ?   ?   B . n 
A 1 9   HIS 9   286 ?   ?   ?   B . n 
A 1 10  HIS 10  287 ?   ?   ?   B . n 
A 1 11  HIS 11  288 ?   ?   ?   B . n 
A 1 12  HIS 12  289 ?   ?   ?   B . n 
A 1 13  ALA 13  290 ?   ?   ?   B . n 
A 1 14  ALA 14  291 291 ALA ALA B . n 
A 1 15  THR 15  292 292 THR THR B . n 
A 1 16  ARG 16  293 293 ARG ARG B . n 
A 1 17  ASP 17  294 294 ASP ASP B . n 
A 1 18  GLN 18  295 295 GLN GLN B . n 
A 1 19  LEU 19  296 296 LEU LEU B . n 
A 1 20  ASN 20  297 297 ASN ASN B . n 
A 1 21  ILE 21  298 298 ILE ILE B . n 
A 1 22  ILE 22  299 299 ILE ILE B . n 
A 1 23  VAL 23  300 300 VAL VAL B . n 
A 1 24  SER 24  301 301 SER SER B . n 
A 1 25  TYR 25  302 302 TYR TYR B . n 
A 1 26  PRO 26  303 303 PRO PRO B . n 
A 1 27  PRO 27  304 304 PRO PRO B . n 
A 1 28  THR 28  305 305 THR THR B . n 
A 1 29  LYS 29  306 306 LYS LYS B . n 
A 1 30  GLN 30  307 307 GLN GLN B . n 
A 1 31  LEU 31  308 308 LEU LEU B . n 
A 1 32  THR 32  309 309 THR THR B . n 
A 1 33  TYR 33  310 310 TYR TYR B . n 
A 1 34  GLU 34  311 311 GLU GLU B . n 
A 1 35  GLU 35  312 312 GLU GLU B . n 
A 1 36  GLN 36  313 313 GLN GLN B . n 
A 1 37  ASP 37  314 314 ASP ASP B . n 
A 1 38  LEU 38  315 315 LEU LEU B . n 
A 1 39  VAL 39  316 316 VAL VAL B . n 
A 1 40  TRP 40  317 317 TRP TRP B . n 
A 1 41  LYS 41  318 318 LYS LYS B . n 
A 1 42  PHE 42  319 319 PHE PHE B . n 
A 1 43  ARG 43  320 320 ARG ARG B . n 
A 1 44  TYR 44  321 321 TYR TYR B . n 
A 1 45  TYR 45  322 322 TYR TYR B . n 
A 1 46  LEU 46  323 323 LEU LEU B . n 
A 1 47  THR 47  324 324 THR THR B . n 
A 1 48  ASN 48  325 325 ASN ASN B . n 
A 1 49  GLN 49  326 326 GLN GLN B . n 
A 1 50  GLU 50  327 327 GLU GLU B . n 
A 1 51  LYS 51  328 328 LYS LYS B . n 
A 1 52  ALA 52  329 329 ALA ALA B . n 
A 1 53  LEU 53  330 330 LEU LEU B . n 
A 1 54  THR 54  331 331 THR THR B . n 
A 1 55  LYS 55  332 332 LYS LYS B . n 
A 1 56  PHE 56  333 333 PHE PHE B . n 
A 1 57  LEU 57  334 334 LEU LEU B . n 
A 1 58  LYS 58  335 335 LYS LYS B . n 
A 1 59  CYS 59  336 336 CYS CYS B . n 
A 1 60  VAL 60  337 337 VAL VAL B . n 
A 1 61  ASN 61  338 338 ASN ASN B . n 
A 1 62  TRP 62  339 339 TRP TRP B . n 
A 1 63  ASP 63  340 340 ASP ASP B . n 
A 1 64  LEU 64  341 341 LEU LEU B . n 
A 1 65  PRO 65  342 342 PRO PRO B . n 
A 1 66  GLN 66  343 343 GLN GLN B . n 
A 1 67  GLU 67  344 344 GLU GLU B . n 
A 1 68  ALA 68  345 345 ALA ALA B . n 
A 1 69  LYS 69  346 346 LYS LYS B . n 
A 1 70  GLN 70  347 347 GLN GLN B . n 
A 1 71  ALA 71  348 348 ALA ALA B . n 
A 1 72  LEU 72  349 349 LEU LEU B . n 
A 1 73  GLU 73  350 350 GLU GLU B . n 
A 1 74  LEU 74  351 351 LEU LEU B . n 
A 1 75  LEU 75  352 352 LEU LEU B . n 
A 1 76  GLY 76  353 353 GLY GLY B . n 
A 1 77  LYS 77  354 354 LYS LYS B . n 
A 1 78  TRP 78  355 355 TRP TRP B . n 
A 1 79  LYS 79  356 356 LYS LYS B . n 
A 1 80  PRO 80  357 357 PRO PRO B . n 
A 1 81  MET 81  358 358 MET MET B . n 
A 1 82  ASP 82  359 359 ASP ASP B . n 
A 1 83  VAL 83  360 360 VAL VAL B . n 
A 1 84  GLU 84  361 361 GLU GLU B . n 
A 1 85  ASP 85  362 362 ASP ASP B . n 
A 1 86  SER 86  363 363 SER SER B . n 
A 1 87  LEU 87  364 364 LEU LEU B . n 
A 1 88  GLU 88  365 365 GLU GLU B . n 
A 1 89  LEU 89  366 366 LEU LEU B . n 
A 1 90  LEU 90  367 367 LEU LEU B . n 
A 1 91  SER 91  368 368 SER SER B . n 
A 1 92  SER 92  369 369 SER SER B . n 
A 1 93  HIS 93  370 370 HIS HIS B . n 
A 1 94  TYR 94  371 371 TYR TYR B . n 
A 1 95  THR 95  372 372 THR THR B . n 
A 1 96  ASN 96  373 373 ASN ASN B . n 
A 1 97  PRO 97  374 374 PRO PRO B . n 
A 1 98  THR 98  375 375 THR THR B . n 
A 1 99  VAL 99  376 376 VAL VAL B . n 
A 1 100 ARG 100 377 377 ARG ARG B . n 
A 1 101 ARG 101 378 378 ARG ARG B . n 
A 1 102 TYR 102 379 379 TYR TYR B . n 
A 1 103 ALA 103 380 380 ALA ALA B . n 
A 1 104 VAL 104 381 381 VAL VAL B . n 
A 1 105 ALA 105 382 382 ALA ALA B . n 
A 1 106 ARG 106 383 383 ARG ARG B . n 
A 1 107 LEU 107 384 384 LEU LEU B . n 
A 1 108 ARG 108 385 385 ARG ARG B . n 
A 1 109 GLN 109 386 386 GLN GLN B . n 
A 1 110 ALA 110 387 387 ALA ALA B . n 
A 1 111 ASP 111 388 388 ASP ASP B . n 
A 1 112 ASP 112 389 389 ASP ASP B . n 
A 1 113 GLU 113 390 390 GLU GLU B . n 
A 1 114 ASP 114 391 391 ASP ASP B . n 
A 1 115 LEU 115 392 392 LEU LEU B . n 
A 1 116 LEU 116 393 393 LEU LEU B . n 
A 1 117 MET 117 394 394 MET MET B . n 
A 1 118 TYR 118 395 395 TYR TYR B . n 
A 1 119 LEU 119 396 396 LEU LEU B . n 
A 1 120 LEU 120 397 397 LEU LEU B . n 
A 1 121 GLN 121 398 398 GLN GLN B . n 
A 1 122 LEU 122 399 399 LEU LEU B . n 
A 1 123 VAL 123 400 400 VAL VAL B . n 
A 1 124 GLN 124 401 401 GLN GLN B . n 
A 1 125 ALA 125 402 402 ALA ALA B . n 
A 1 126 LEU 126 403 403 LEU LEU B . n 
A 1 127 LYS 127 404 404 LYS LYS B . n 
A 1 128 TYR 128 405 405 TYR TYR B . n 
A 1 129 GLU 129 406 406 GLU GLU B . n 
A 1 130 ASN 130 407 407 ASN ASN B . n 
A 1 131 PHE 131 408 408 PHE PHE B . n 
A 1 132 ASP 132 409 409 ASP ASP B . n 
A 1 133 ASP 133 410 410 ASP ASP B . n 
A 1 134 ILE 134 411 411 ILE ILE B . n 
A 1 135 LYS 135 412 412 LYS LYS B . n 
A 1 136 ASN 136 413 413 ASN ASN B . n 
A 1 137 GLY 137 414 414 GLY GLY B . n 
A 1 138 LEU 138 415 415 LEU LEU B . n 
A 1 139 GLU 139 416 416 GLU GLU B . n 
A 1 140 PRO 140 417 417 PRO PRO B . n 
A 1 141 THR 141 418 ?   ?   ?   B . n 
A 1 142 LYS 142 419 ?   ?   ?   B . n 
A 1 143 LYS 143 420 ?   ?   ?   B . n 
A 1 144 ASP 144 421 ?   ?   ?   B . n 
A 1 145 SER 145 422 ?   ?   ?   B . n 
A 1 146 GLN 146 423 ?   ?   ?   B . n 
A 1 147 SER 147 424 ?   ?   ?   B . n 
A 1 148 SER 148 425 ?   ?   ?   B . n 
A 1 149 VAL 149 426 ?   ?   ?   B . n 
A 1 150 SER 150 427 ?   ?   ?   B . n 
A 1 151 GLU 151 428 ?   ?   ?   B . n 
A 1 152 ASN 152 429 ?   ?   ?   B . n 
A 1 153 VAL 153 430 ?   ?   ?   B . n 
A 1 154 SER 154 431 ?   ?   ?   B . n 
A 1 155 ASN 155 432 ?   ?   ?   B . n 
A 1 156 SER 156 433 ?   ?   ?   B . n 
A 1 157 GLY 157 434 ?   ?   ?   B . n 
A 1 158 ILE 158 435 ?   ?   ?   B . n 
A 1 159 ASN 159 436 ?   ?   ?   B . n 
A 1 160 SER 160 437 ?   ?   ?   B . n 
A 1 161 ALA 161 438 ?   ?   ?   B . n 
A 1 162 GLU 162 439 ?   ?   ?   B . n 
A 1 163 ILE 163 440 ?   ?   ?   B . n 
A 1 164 ASP 164 441 ?   ?   ?   B . n 
A 1 165 SER 165 442 ?   ?   ?   B . n 
A 1 166 SER 166 443 ?   ?   ?   B . n 
A 1 167 GLN 167 444 ?   ?   ?   B . n 
A 1 168 ILE 168 445 ?   ?   ?   B . n 
A 1 169 ILE 169 446 ?   ?   ?   B . n 
A 1 170 THR 170 447 ?   ?   ?   B . n 
A 1 171 SER 171 448 ?   ?   ?   B . n 
A 1 172 PRO 172 449 ?   ?   ?   B . n 
A 1 173 LEU 173 450 ?   ?   ?   B . n 
A 1 174 PRO 174 451 ?   ?   ?   B . n 
A 1 175 SER 175 452 ?   ?   ?   B . n 
A 1 176 VAL 176 453 ?   ?   ?   B . n 
A 1 177 SER 177 454 ?   ?   ?   B . n 
A 1 178 SER 178 455 ?   ?   ?   B . n 
A 1 179 PRO 179 456 ?   ?   ?   B . n 
A 1 180 PRO 180 457 ?   ?   ?   B . n 
A 1 181 PRO 181 458 ?   ?   ?   B . n 
A 1 182 ALA 182 459 ?   ?   ?   B . n 
A 1 183 SER 183 460 ?   ?   ?   B . n 
A 1 184 LYS 184 461 ?   ?   ?   B . n 
A 1 185 THR 185 462 ?   ?   ?   B . n 
A 1 186 LYS 186 463 ?   ?   ?   B . n 
A 1 187 GLU 187 464 ?   ?   ?   B . n 
A 1 188 VAL 188 465 ?   ?   ?   B . n 
A 1 189 PRO 189 466 ?   ?   ?   B . n 
A 1 190 ASP 190 467 ?   ?   ?   B . n 
A 1 191 GLY 191 468 ?   ?   ?   B . n 
A 1 192 GLU 192 469 ?   ?   ?   B . n 
A 1 193 ASN 193 470 470 ASN ASN B . n 
A 1 194 LEU 194 471 471 LEU LEU B . n 
A 1 195 GLU 195 472 472 GLU GLU B . n 
A 1 196 GLN 196 473 473 GLN GLN B . n 
A 1 197 ASP 197 474 474 ASP ASP B . n 
A 1 198 LEU 198 475 475 LEU LEU B . n 
A 1 199 CYS 199 476 476 CYS CYS B . n 
A 1 200 THR 200 477 477 THR THR B . n 
A 1 201 PHE 201 478 478 PHE PHE B . n 
A 1 202 LEU 202 479 479 LEU LEU B . n 
A 1 203 ILE 203 480 480 ILE ILE B . n 
A 1 204 SER 204 481 481 SER SER B . n 
A 1 205 ARG 205 482 482 ARG ARG B . n 
A 1 206 ALA 206 483 483 ALA ALA B . n 
A 1 207 CYS 207 484 484 CYS CYS B . n 
A 1 208 LYS 208 485 485 LYS LYS B . n 
A 1 209 ASN 209 486 486 ASN ASN B . n 
A 1 210 SER 210 487 487 SER SER B . n 
A 1 211 THR 211 488 488 THR THR B . n 
A 1 212 LEU 212 489 489 LEU LEU B . n 
A 1 213 ALA 213 490 490 ALA ALA B . n 
A 1 214 ASN 214 491 491 ASN ASN B . n 
A 1 215 TYR 215 492 492 TYR TYR B . n 
A 1 216 LEU 216 493 493 LEU LEU B . n 
A 1 217 TYR 217 494 494 TYR TYR B . n 
A 1 218 TRP 218 495 495 TRP TRP B . n 
A 1 219 TYR 219 496 496 TYR TYR B . n 
A 1 220 VAL 220 497 497 VAL VAL B . n 
A 1 221 ILE 221 498 498 ILE ILE B . n 
A 1 222 VAL 222 499 499 VAL VAL B . n 
A 1 223 GLU 223 500 500 GLU GLU B . n 
A 1 224 CYS 224 501 501 CYS CYS B . n 
A 1 225 GLU 225 502 502 GLU GLU B . n 
A 1 226 ASP 226 503 503 ASP ASP B . n 
A 1 227 GLN 227 504 504 GLN GLN B . n 
A 1 228 ASP 228 505 505 ASP ASP B . n 
A 1 229 THR 229 506 506 THR THR B . n 
A 1 230 GLN 230 507 507 GLN GLN B . n 
A 1 231 GLN 231 508 508 GLN GLN B . n 
A 1 232 ARG 232 509 509 ARG ARG B . n 
A 1 233 ASP 233 510 510 ASP ASP B . n 
A 1 234 PRO 234 511 511 PRO PRO B . n 
A 1 235 LYS 235 512 512 LYS LYS B . n 
A 1 236 THR 236 513 513 THR THR B . n 
A 1 237 HIS 237 514 514 HIS HIS B . n 
A 1 238 GLU 238 515 515 GLU GLU B . n 
A 1 239 MET 239 516 516 MET MET B . n 
A 1 240 TYR 240 517 517 TYR TYR B . n 
A 1 241 LEU 241 518 518 LEU LEU B . n 
A 1 242 ASN 242 519 519 ASN ASN B . n 
A 1 243 VAL 243 520 520 VAL VAL B . n 
A 1 244 MET 244 521 521 MET MET B . n 
A 1 245 ARG 245 522 522 ARG ARG B . n 
A 1 246 ARG 246 523 523 ARG ARG B . n 
A 1 247 PHE 247 524 524 PHE PHE B . n 
A 1 248 SER 248 525 525 SER SER B . n 
A 1 249 GLN 249 526 526 GLN GLN B . n 
A 1 250 ALA 250 527 527 ALA ALA B . n 
A 1 251 LEU 251 528 528 LEU LEU B . n 
A 1 252 LEU 252 529 529 LEU LEU B . n 
A 1 253 LYS 253 530 530 LYS LYS B . n 
A 1 254 GLY 254 531 531 GLY GLY B . n 
A 1 255 ASP 255 532 532 ASP ASP B . n 
A 1 256 LYS 256 533 533 LYS LYS B . n 
A 1 257 SER 257 534 534 SER SER B . n 
A 1 258 VAL 258 535 535 VAL VAL B . n 
A 1 259 ARG 259 536 536 ARG ARG B . n 
A 1 260 VAL 260 537 537 VAL VAL B . n 
A 1 261 MET 261 538 538 MET MET B . n 
A 1 262 ARG 262 539 539 ARG ARG B . n 
A 1 263 SER 263 540 540 SER SER B . n 
A 1 264 LEU 264 541 541 LEU LEU B . n 
A 1 265 LEU 265 542 542 LEU LEU B . n 
A 1 266 ALA 266 543 543 ALA ALA B . n 
A 1 267 ALA 267 544 544 ALA ALA B . n 
A 1 268 GLN 268 545 545 GLN GLN B . n 
A 1 269 GLN 269 546 546 GLN GLN B . n 
A 1 270 THR 270 547 547 THR THR B . n 
A 1 271 PHE 271 548 548 PHE PHE B . n 
A 1 272 VAL 272 549 549 VAL VAL B . n 
A 1 273 ASP 273 550 550 ASP ASP B . n 
A 1 274 ARG 274 551 551 ARG ARG B . n 
A 1 275 LEU 275 552 552 LEU LEU B . n 
A 1 276 VAL 276 553 553 VAL VAL B . n 
A 1 277 HIS 277 554 554 HIS HIS B . n 
A 1 278 LEU 278 555 555 LEU LEU B . n 
A 1 279 MET 279 556 556 MET MET B . n 
A 1 280 LYS 280 557 557 LYS LYS B . n 
A 1 281 ALA 281 558 558 ALA ALA B . n 
A 1 282 VAL 282 559 559 VAL VAL B . n 
A 1 283 GLN 283 560 560 GLN GLN B . n 
A 1 284 ARG 284 561 561 ARG ARG B . n 
A 1 285 GLU 285 562 562 GLU GLU B . n 
A 1 286 SER 286 563 563 SER SER B . n 
A 1 287 GLY 287 564 564 GLY GLY B . n 
A 1 288 ASN 288 565 565 ASN ASN B . n 
A 1 289 ARG 289 566 566 ARG ARG B . n 
A 1 290 LYS 290 567 567 LYS LYS B . n 
A 1 291 LYS 291 568 568 LYS LYS B . n 
A 1 292 LYS 292 569 569 LYS LYS B . n 
A 1 293 ASN 293 570 570 ASN ASN B . n 
A 1 294 GLU 294 571 571 GLU GLU B . n 
A 1 295 ARG 295 572 572 ARG ARG B . n 
A 1 296 LEU 296 573 573 LEU LEU B . n 
A 1 297 GLN 297 574 574 GLN GLN B . n 
A 1 298 ALA 298 575 575 ALA ALA B . n 
A 1 299 LEU 299 576 576 LEU LEU B . n 
A 1 300 LEU 300 577 577 LEU LEU B . n 
A 1 301 GLY 301 578 578 GLY GLY B . n 
A 1 302 ASP 302 579 579 ASP ASP B . n 
A 1 303 ASN 303 580 580 ASN ASN B . n 
A 1 304 GLU 304 581 581 GLU GLU B . n 
A 1 305 LYS 305 582 582 LYS LYS B . n 
A 1 306 MET 306 583 583 MET MET B . n 
A 1 307 ASN 307 584 584 ASN ASN B . n 
A 1 308 LEU 308 585 585 LEU LEU B . n 
A 1 309 SER 309 586 586 SER SER B . n 
A 1 310 ASP 310 587 587 ASP ASP B . n 
A 1 311 VAL 311 588 588 VAL VAL B . n 
A 1 312 GLU 312 589 589 GLU GLU B . n 
A 1 313 LEU 313 590 590 LEU LEU B . n 
A 1 314 ILE 314 591 591 ILE ILE B . n 
A 1 315 PRO 315 592 592 PRO PRO B . n 
A 1 316 LEU 316 593 593 LEU LEU B . n 
A 1 317 PRO 317 594 594 PRO PRO B . n 
A 1 318 LEU 318 595 595 LEU LEU B . n 
A 1 319 GLU 319 596 596 GLU GLU B . n 
A 1 320 PRO 320 597 597 PRO PRO B . n 
A 1 321 GLN 321 598 598 GLN GLN B . n 
A 1 322 VAL 322 599 599 VAL VAL B . n 
A 1 323 LYS 323 600 600 LYS LYS B . n 
A 1 324 ILE 324 601 601 ILE ILE B . n 
A 1 325 ARG 325 602 602 ARG ARG B . n 
A 1 326 GLY 326 603 603 GLY GLY B . n 
A 1 327 ILE 327 604 604 ILE ILE B . n 
A 1 328 ILE 328 605 605 ILE ILE B . n 
A 1 329 PRO 329 606 606 PRO PRO B . n 
A 1 330 GLU 330 607 607 GLU GLU B . n 
A 1 331 THR 331 608 608 THR THR B . n 
A 1 332 ALA 332 609 609 ALA ALA B . n 
A 1 333 THR 333 610 610 THR THR B . n 
A 1 334 LEU 334 611 611 LEU LEU B . n 
A 1 335 PHE 335 612 612 PHE PHE B . n 
A 1 336 LYS 336 613 613 LYS LYS B . n 
A 1 337 SER 337 614 614 SER SER B . n 
A 1 338 ALA 338 615 615 ALA ALA B . n 
A 1 339 LEU 339 616 616 LEU LEU B . n 
A 1 340 MET 340 617 617 MET MET B . n 
A 1 341 PRO 341 618 618 PRO PRO B . n 
A 1 342 ALA 342 619 619 ALA ALA B . n 
A 1 343 GLN 343 620 620 GLN GLN B . n 
A 1 344 LEU 344 621 621 LEU LEU B . n 
A 1 345 PHE 345 622 622 PHE PHE B . n 
A 1 346 PHE 346 623 623 PHE PHE B . n 
A 1 347 LYS 347 624 624 LYS LYS B . n 
A 1 348 THR 348 625 625 THR THR B . n 
A 1 349 GLU 349 626 626 GLU GLU B . n 
A 1 350 ASP 350 627 627 ASP ASP B . n 
A 1 351 GLY 351 628 628 GLY GLY B . n 
A 1 352 GLY 352 629 629 GLY GLY B . n 
A 1 353 LYS 353 630 630 LYS LYS B . n 
A 1 354 TYR 354 631 631 TYR TYR B . n 
A 1 355 PRO 355 632 632 PRO PRO B . n 
A 1 356 VAL 356 633 633 VAL VAL B . n 
A 1 357 ILE 357 634 634 ILE ILE B . n 
A 1 358 PHE 358 635 635 PHE PHE B . n 
A 1 359 LYS 359 636 636 LYS LYS B . n 
A 1 360 HIS 360 637 637 HIS HIS B . n 
A 1 361 GLY 361 638 638 GLY GLY B . n 
A 1 362 ASP 362 639 639 ASP ASP B . n 
A 1 363 ASP 363 640 640 ASP ASP B . n 
A 1 364 LEU 364 641 641 LEU LEU B . n 
A 1 365 ARG 365 642 642 ARG ARG B . n 
A 1 366 GLN 366 643 643 GLN GLN B . n 
A 1 367 ASP 367 644 644 ASP ASP B . n 
A 1 368 GLN 368 645 645 GLN GLN B . n 
A 1 369 LEU 369 646 646 LEU LEU B . n 
A 1 370 ILE 370 647 647 ILE ILE B . n 
A 1 371 LEU 371 648 648 LEU LEU B . n 
A 1 372 GLN 372 649 649 GLN GLN B . n 
A 1 373 ILE 373 650 650 ILE ILE B . n 
A 1 374 ILE 374 651 651 ILE ILE B . n 
A 1 375 SER 375 652 652 SER SER B . n 
A 1 376 LEU 376 653 653 LEU LEU B . n 
A 1 377 MET 377 654 654 MET MET B . n 
A 1 378 ASP 378 655 655 ASP ASP B . n 
A 1 379 LYS 379 656 656 LYS LYS B . n 
A 1 380 LEU 380 657 657 LEU LEU B . n 
A 1 381 LEU 381 658 658 LEU LEU B . n 
A 1 382 ARG 382 659 659 ARG ARG B . n 
A 1 383 LYS 383 660 660 LYS LYS B . n 
A 1 384 GLU 384 661 661 GLU GLU B . n 
A 1 385 ASN 385 662 662 ASN ASN B . n 
A 1 386 LEU 386 663 663 LEU LEU B . n 
A 1 387 ASP 387 664 664 ASP ASP B . n 
A 1 388 LEU 388 665 665 LEU LEU B . n 
A 1 389 LYS 389 666 666 LYS LYS B . n 
A 1 390 LEU 390 667 667 LEU LEU B . n 
A 1 391 THR 391 668 668 THR THR B . n 
A 1 392 PRO 392 669 669 PRO PRO B . n 
A 1 393 TYR 393 670 670 TYR TYR B . n 
A 1 394 LYS 394 671 671 LYS LYS B . n 
A 1 395 VAL 395 672 672 VAL VAL B . n 
A 1 396 LEU 396 673 673 LEU LEU B . n 
A 1 397 ALA 397 674 674 ALA ALA B . n 
A 1 398 THR 398 675 675 THR THR B . n 
A 1 399 SER 399 676 676 SER SER B . n 
A 1 400 THR 400 677 677 THR THR B . n 
A 1 401 LYS 401 678 678 LYS LYS B . n 
A 1 402 HIS 402 679 679 HIS HIS B . n 
A 1 403 GLY 403 680 680 GLY GLY B . n 
A 1 404 PHE 404 681 681 PHE PHE B . n 
A 1 405 MET 405 682 682 MET MET B . n 
A 1 406 GLN 406 683 683 GLN GLN B . n 
A 1 407 PHE 407 684 684 PHE PHE B . n 
A 1 408 ILE 408 685 685 ILE ILE B . n 
A 1 409 GLN 409 686 686 GLN GLN B . n 
A 1 410 SER 410 687 687 SER SER B . n 
A 1 411 VAL 411 688 688 VAL VAL B . n 
A 1 412 PRO 412 689 689 PRO PRO B . n 
A 1 413 VAL 413 690 690 VAL VAL B . n 
A 1 414 ALA 414 691 691 ALA ALA B . n 
A 1 415 GLU 415 692 692 GLU GLU B . n 
A 1 416 VAL 416 693 693 VAL VAL B . n 
A 1 417 LEU 417 694 694 LEU LEU B . n 
A 1 418 ASP 418 695 695 ASP ASP B . n 
A 1 419 THR 419 696 696 THR THR B . n 
A 1 420 GLU 420 697 697 GLU GLU B . n 
A 1 421 GLY 421 698 698 GLY GLY B . n 
A 1 422 SER 422 699 699 SER SER B . n 
A 1 423 ILE 423 700 700 ILE ILE B . n 
A 1 424 GLN 424 701 701 GLN GLN B . n 
A 1 425 ASN 425 702 702 ASN ASN B . n 
A 1 426 PHE 426 703 703 PHE PHE B . n 
A 1 427 PHE 427 704 704 PHE PHE B . n 
A 1 428 ARG 428 705 705 ARG ARG B . n 
A 1 429 LYS 429 706 706 LYS LYS B . n 
A 1 430 TYR 430 707 707 TYR TYR B . n 
A 1 431 ALA 431 708 708 ALA ALA B . n 
A 1 432 PRO 432 709 709 PRO PRO B . n 
A 1 433 SER 433 710 710 SER SER B . n 
A 1 434 GLU 434 711 711 GLU GLU B . n 
A 1 435 ASN 435 712 712 ASN ASN B . n 
A 1 436 GLY 436 713 713 GLY GLY B . n 
A 1 437 PRO 437 714 714 PRO PRO B . n 
A 1 438 ASN 438 715 715 ASN ASN B . n 
A 1 439 GLY 439 716 716 GLY GLY B . n 
A 1 440 ILE 440 717 717 ILE ILE B . n 
A 1 441 SER 441 718 718 SER SER B . n 
A 1 442 ALA 442 719 719 ALA ALA B . n 
A 1 443 GLU 443 720 720 GLU GLU B . n 
A 1 444 VAL 444 721 721 VAL VAL B . n 
A 1 445 MET 445 722 722 MET MET B . n 
A 1 446 ASP 446 723 723 ASP ASP B . n 
A 1 447 THR 447 724 724 THR THR B . n 
A 1 448 TYR 448 725 725 TYR TYR B . n 
A 1 449 VAL 449 726 726 VAL VAL B . n 
A 1 450 LYS 450 727 727 LYS LYS B . n 
A 1 451 SER 451 728 728 SER SER B . n 
A 1 452 CYS 452 729 729 CYS CYS B . n 
A 1 453 ALA 453 730 730 ALA ALA B . n 
A 1 454 GLY 454 731 731 GLY GLY B . n 
A 1 455 TYR 455 732 732 TYR TYR B . n 
A 1 456 CYS 456 733 733 CYS CYS B . n 
A 1 457 VAL 457 734 734 VAL VAL B . n 
A 1 458 ILE 458 735 735 ILE ILE B . n 
A 1 459 THR 459 736 736 THR THR B . n 
A 1 460 TYR 460 737 737 TYR TYR B . n 
A 1 461 ILE 461 738 738 ILE ILE B . n 
A 1 462 LEU 462 739 739 LEU LEU B . n 
A 1 463 GLY 463 740 740 GLY GLY B . n 
A 1 464 VAL 464 741 741 VAL VAL B . n 
A 1 465 GLY 465 742 742 GLY GLY B . n 
A 1 466 ASP 466 743 743 ASP ASP B . n 
A 1 467 ARG 467 744 744 ARG ARG B . n 
A 1 468 HIS 468 745 745 HIS HIS B . n 
A 1 469 LEU 469 746 746 LEU LEU B . n 
A 1 470 ASP 470 747 747 ASP ASP B . n 
A 1 471 ASN 471 748 748 ASN ASN B . n 
A 1 472 LEU 472 749 749 LEU LEU B . n 
A 1 473 LEU 473 750 750 LEU LEU B . n 
A 1 474 LEU 474 751 751 LEU LEU B . n 
A 1 475 THR 475 752 752 THR THR B . n 
A 1 476 LYS 476 753 753 LYS LYS B . n 
A 1 477 THR 477 754 754 THR THR B . n 
A 1 478 GLY 478 755 755 GLY GLY B . n 
A 1 479 LYS 479 756 756 LYS LYS B . n 
A 1 480 LEU 480 757 757 LEU LEU B . n 
A 1 481 PHE 481 758 758 PHE PHE B . n 
A 1 482 HIS 482 759 759 HIS HIS B . n 
A 1 483 ILE 483 760 760 ILE ILE B . n 
A 1 484 ASP 484 761 761 ASP ASP B . n 
A 1 485 PHE 485 762 762 PHE PHE B . n 
A 1 486 GLY 486 763 763 GLY GLY B . n 
A 1 487 TYR 487 764 764 TYR TYR B . n 
A 1 488 ILE 488 765 765 ILE ILE B . n 
A 1 489 LEU 489 766 766 LEU LEU B . n 
A 1 490 GLY 490 767 767 GLY GLY B . n 
A 1 491 ARG 491 768 768 ARG ARG B . n 
A 1 492 ASP 492 769 769 ASP ASP B . n 
A 1 493 PRO 493 770 770 PRO PRO B . n 
A 1 494 LYS 494 771 771 LYS LYS B . n 
A 1 495 PRO 495 772 772 PRO PRO B . n 
A 1 496 LEU 496 773 773 LEU LEU B . n 
A 1 497 PRO 497 774 774 PRO PRO B . n 
A 1 498 PRO 498 775 775 PRO PRO B . n 
A 1 499 PRO 499 776 776 PRO PRO B . n 
A 1 500 MET 500 777 777 MET MET B . n 
A 1 501 LYS 501 778 778 LYS LYS B . n 
A 1 502 LEU 502 779 779 LEU LEU B . n 
A 1 503 ASN 503 780 780 ASN ASN B . n 
A 1 504 LYS 504 781 781 LYS LYS B . n 
A 1 505 GLU 505 782 782 GLU GLU B . n 
A 1 506 MET 506 783 783 MET MET B . n 
A 1 507 VAL 507 784 784 VAL VAL B . n 
A 1 508 GLU 508 785 785 GLU GLU B . n 
A 1 509 GLY 509 786 786 GLY GLY B . n 
A 1 510 MET 510 787 787 MET MET B . n 
A 1 511 GLY 511 788 788 GLY GLY B . n 
A 1 512 GLY 512 789 789 GLY GLY B . n 
A 1 513 THR 513 790 790 THR THR B . n 
A 1 514 GLN 514 791 791 GLN GLN B . n 
A 1 515 SER 515 792 792 SER SER B . n 
A 1 516 GLU 516 793 793 GLU GLU B . n 
A 1 517 GLN 517 794 794 GLN GLN B . n 
A 1 518 TYR 518 795 795 TYR TYR B . n 
A 1 519 GLN 519 796 796 GLN GLN B . n 
A 1 520 GLU 520 797 797 GLU GLU B . n 
A 1 521 PHE 521 798 798 PHE PHE B . n 
A 1 522 ARG 522 799 799 ARG ARG B . n 
A 1 523 LYS 523 800 800 LYS LYS B . n 
A 1 524 GLN 524 801 801 GLN GLN B . n 
A 1 525 CYS 525 802 802 CYS CYS B . n 
A 1 526 TYR 526 803 803 TYR TYR B . n 
A 1 527 THR 527 804 804 THR THR B . n 
A 1 528 ALA 528 805 805 ALA ALA B . n 
A 1 529 PHE 529 806 806 PHE PHE B . n 
A 1 530 LEU 530 807 807 LEU LEU B . n 
A 1 531 HIS 531 808 808 HIS HIS B . n 
A 1 532 LEU 532 809 809 LEU LEU B . n 
A 1 533 ARG 533 810 810 ARG ARG B . n 
A 1 534 ARG 534 811 811 ARG ARG B . n 
A 1 535 TYR 535 812 812 TYR TYR B . n 
A 1 536 SER 536 813 813 SER SER B . n 
A 1 537 ASN 537 814 814 ASN ASN B . n 
A 1 538 LEU 538 815 815 LEU LEU B . n 
A 1 539 ILE 539 816 816 ILE ILE B . n 
A 1 540 LEU 540 817 817 LEU LEU B . n 
A 1 541 ASN 541 818 818 ASN ASN B . n 
A 1 542 LEU 542 819 819 LEU LEU B . n 
A 1 543 PHE 543 820 820 PHE PHE B . n 
A 1 544 SER 544 821 821 SER SER B . n 
A 1 545 LEU 545 822 822 LEU LEU B . n 
A 1 546 MET 546 823 823 MET MET B . n 
A 1 547 VAL 547 824 824 VAL VAL B . n 
A 1 548 ASP 548 825 825 ASP ASP B . n 
A 1 549 ALA 549 826 826 ALA ALA B . n 
A 1 550 ASN 550 827 827 ASN ASN B . n 
A 1 551 ILE 551 828 828 ILE ILE B . n 
A 1 552 PRO 552 829 829 PRO PRO B . n 
A 1 553 ASP 553 830 830 ASP ASP B . n 
A 1 554 ILE 554 831 831 ILE ILE B . n 
A 1 555 ALA 555 832 832 ALA ALA B . n 
A 1 556 LEU 556 833 833 LEU LEU B . n 
A 1 557 GLU 557 834 834 GLU GLU B . n 
A 1 558 PRO 558 835 835 PRO PRO B . n 
A 1 559 ASP 559 836 836 ASP ASP B . n 
A 1 560 LYS 560 837 837 LYS LYS B . n 
A 1 561 THR 561 838 838 THR THR B . n 
A 1 562 VAL 562 839 839 VAL VAL B . n 
A 1 563 LYS 563 840 840 LYS LYS B . n 
A 1 564 LYS 564 841 841 LYS LYS B . n 
A 1 565 VAL 565 842 842 VAL VAL B . n 
A 1 566 GLN 566 843 843 GLN GLN B . n 
A 1 567 ASP 567 844 844 ASP ASP B . n 
A 1 568 LYS 568 845 845 LYS LYS B . n 
A 1 569 PHE 569 846 846 PHE PHE B . n 
A 1 570 ARG 570 847 847 ARG ARG B . n 
A 1 571 LEU 571 848 848 LEU LEU B . n 
A 1 572 ASP 572 849 849 ASP ASP B . n 
A 1 573 LEU 573 850 850 LEU LEU B . n 
A 1 574 SER 574 851 851 SER SER B . n 
A 1 575 ASP 575 852 852 ASP ASP B . n 
A 1 576 GLU 576 853 853 GLU GLU B . n 
A 1 577 GLU 577 854 854 GLU GLU B . n 
A 1 578 ALA 578 855 855 ALA ALA B . n 
A 1 579 VAL 579 856 856 VAL VAL B . n 
A 1 580 HIS 580 857 857 HIS HIS B . n 
A 1 581 TYR 581 858 858 TYR TYR B . n 
A 1 582 MET 582 859 859 MET MET B . n 
A 1 583 GLN 583 860 860 GLN GLN B . n 
A 1 584 SER 584 861 861 SER SER B . n 
A 1 585 LEU 585 862 862 LEU LEU B . n 
A 1 586 ILE 586 863 863 ILE ILE B . n 
A 1 587 ASP 587 864 864 ASP ASP B . n 
A 1 588 GLU 588 865 865 GLU GLU B . n 
A 1 589 SER 589 866 866 SER SER B . n 
A 1 590 VAL 590 867 867 VAL VAL B . n 
A 1 591 HIS 591 868 868 HIS HIS B . n 
A 1 592 ALA 592 869 869 ALA ALA B . n 
A 1 593 LEU 593 870 870 LEU LEU B . n 
A 1 594 PHE 594 871 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DMS ? ? DMS ? ? 'SUBJECT OF INVESTIGATION' ? 
3 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
4 K   ? ? K   ? ? 'SUBJECT OF INVESTIGATION' ? 
5 MES ? ? MES ? ? 'SUBJECT OF INVESTIGATION' ? 
6 PEG ? ? PEG ? ? 'SUBJECT OF INVESTIGATION' ? 
7 PG4 ? ? PG4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 MES 1  901  901 MES MES B . 
C 3 PG4 1  902  902 PG4 PG4 B . 
D 4 DMS 1  903  903 DMS DMS B . 
E 5 PEG 1  904  907 PEG PEG B . 
F 5 PEG 1  905  908 PEG PEG B . 
G 6 GOL 1  906  909 GOL GOL B . 
H 7 CL  1  907  2   CL  CL  B . 
I 7 CL  1  908  3   CL  CL  B . 
J 7 CL  1  909  4   CL  CL  B . 
K 7 CL  1  910  5   CL  CL  B . 
L 5 PEG 1  911  9   PEG PEG B . 
M 5 PEG 1  912  10  PEG PEG B . 
N 8 K   1  913  1   K   K   B . 
O 8 K   1  914  2   K   K   B . 
P 8 K   1  915  3   K   K   B . 
Q 9 HOH 1  1001 51  HOH HOH B . 
Q 9 HOH 2  1002 36  HOH HOH B . 
Q 9 HOH 3  1003 41  HOH HOH B . 
Q 9 HOH 4  1004 57  HOH HOH B . 
Q 9 HOH 5  1005 12  HOH HOH B . 
Q 9 HOH 6  1006 16  HOH HOH B . 
Q 9 HOH 7  1007 37  HOH HOH B . 
Q 9 HOH 8  1008 7   HOH HOH B . 
Q 9 HOH 9  1009 3   HOH HOH B . 
Q 9 HOH 10 1010 23  HOH HOH B . 
Q 9 HOH 11 1011 40  HOH HOH B . 
Q 9 HOH 12 1012 44  HOH HOH B . 
Q 9 HOH 13 1013 53  HOH HOH B . 
Q 9 HOH 14 1014 15  HOH HOH B . 
Q 9 HOH 15 1015 20  HOH HOH B . 
Q 9 HOH 16 1016 9   HOH HOH B . 
Q 9 HOH 17 1017 1   HOH HOH B . 
Q 9 HOH 18 1018 4   HOH HOH B . 
Q 9 HOH 19 1019 13  HOH HOH B . 
Q 9 HOH 20 1020 10  HOH HOH B . 
Q 9 HOH 21 1021 19  HOH HOH B . 
Q 9 HOH 22 1022 5   HOH HOH B . 
Q 9 HOH 23 1023 38  HOH HOH B . 
Q 9 HOH 24 1024 11  HOH HOH B . 
Q 9 HOH 25 1025 49  HOH HOH B . 
Q 9 HOH 26 1026 47  HOH HOH B . 
Q 9 HOH 27 1027 46  HOH HOH B . 
Q 9 HOH 28 1028 2   HOH HOH B . 
Q 9 HOH 29 1029 26  HOH HOH B . 
Q 9 HOH 30 1030 21  HOH HOH B . 
Q 9 HOH 31 1031 18  HOH HOH B . 
Q 9 HOH 32 1032 8   HOH HOH B . 
Q 9 HOH 33 1033 22  HOH HOH B . 
Q 9 HOH 34 1034 59  HOH HOH B . 
Q 9 HOH 35 1035 6   HOH HOH B . 
Q 9 HOH 36 1036 34  HOH HOH B . 
Q 9 HOH 37 1037 52  HOH HOH B . 
Q 9 HOH 38 1038 31  HOH HOH B . 
Q 9 HOH 39 1039 43  HOH HOH B . 
Q 9 HOH 40 1040 55  HOH HOH B . 
Q 9 HOH 41 1041 29  HOH HOH B . 
Q 9 HOH 42 1042 24  HOH HOH B . 
Q 9 HOH 43 1043 58  HOH HOH B . 
Q 9 HOH 44 1044 50  HOH HOH B . 
Q 9 HOH 45 1045 32  HOH HOH B . 
Q 9 HOH 46 1046 17  HOH HOH B . 
Q 9 HOH 47 1047 48  HOH HOH B . 
Q 9 HOH 48 1048 33  HOH HOH B . 
Q 9 HOH 49 1049 35  HOH HOH B . 
Q 9 HOH 50 1050 14  HOH HOH B . 
Q 9 HOH 51 1051 39  HOH HOH B . 
Q 9 HOH 52 1052 30  HOH HOH B . 
Q 9 HOH 53 1053 56  HOH HOH B . 
Q 9 HOH 54 1054 27  HOH HOH B . 
Q 9 HOH 55 1055 64  HOH HOH B . 
Q 9 HOH 56 1056 60  HOH HOH B . 
Q 9 HOH 57 1057 28  HOH HOH B . 
Q 9 HOH 58 1058 71  HOH HOH B . 
Q 9 HOH 59 1059 62  HOH HOH B . 
Q 9 HOH 60 1060 69  HOH HOH B . 
Q 9 HOH 61 1061 79  HOH HOH B . 
Q 9 HOH 62 1062 95  HOH HOH B . 
Q 9 HOH 63 1063 73  HOH HOH B . 
Q 9 HOH 64 1064 68  HOH HOH B . 
Q 9 HOH 65 1065 94  HOH HOH B . 
Q 9 HOH 66 1066 67  HOH HOH B . 
Q 9 HOH 67 1067 75  HOH HOH B . 
Q 9 HOH 68 1068 42  HOH HOH B . 
Q 9 HOH 69 1069 81  HOH HOH B . 
Q 9 HOH 70 1070 78  HOH HOH B . 
Q 9 HOH 71 1071 86  HOH HOH B . 
Q 9 HOH 72 1072 85  HOH HOH B . 
Q 9 HOH 73 1073 63  HOH HOH B . 
Q 9 HOH 74 1074 88  HOH HOH B . 
Q 9 HOH 75 1075 74  HOH HOH B . 
Q 9 HOH 76 1076 80  HOH HOH B . 
Q 9 HOH 77 1077 83  HOH HOH B . 
Q 9 HOH 78 1078 91  HOH HOH B . 
Q 9 HOH 79 1079 70  HOH HOH B . 
Q 9 HOH 80 1080 92  HOH HOH B . 
Q 9 HOH 81 1081 65  HOH HOH B . 
Q 9 HOH 82 1082 76  HOH HOH B . 
Q 9 HOH 83 1083 87  HOH HOH B . 
Q 9 HOH 84 1084 84  HOH HOH B . 
Q 9 HOH 85 1085 89  HOH HOH B . 
Q 9 HOH 86 1086 72  HOH HOH B . 
Q 9 HOH 87 1087 96  HOH HOH B . 
Q 9 HOH 88 1088 93  HOH HOH B . 
Q 9 HOH 89 1089 77  HOH HOH B . 
Q 9 HOH 90 1090 66  HOH HOH B . 
Q 9 HOH 91 1091 82  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B ALA 291 ? CB  ? A ALA 14  CB  
2   1 Y 1 B THR 292 ? OG1 ? A THR 15  OG1 
3   1 Y 1 B THR 292 ? CG2 ? A THR 15  CG2 
4   1 Y 1 B ARG 293 ? CG  ? A ARG 16  CG  
5   1 Y 1 B ARG 293 ? CD  ? A ARG 16  CD  
6   1 Y 1 B ARG 293 ? NE  ? A ARG 16  NE  
7   1 Y 1 B ARG 293 ? CZ  ? A ARG 16  CZ  
8   1 Y 1 B ARG 293 ? NH1 ? A ARG 16  NH1 
9   1 Y 1 B ARG 293 ? NH2 ? A ARG 16  NH2 
10  1 Y 1 B ASP 294 ? OD1 ? A ASP 17  OD1 
11  1 Y 1 B ASP 294 ? OD2 ? A ASP 17  OD2 
12  1 Y 1 B ILE 298 ? CD1 ? A ILE 21  CD1 
13  1 Y 1 B ILE 299 ? CD1 ? A ILE 22  CD1 
14  1 Y 1 B THR 305 ? OG1 ? A THR 28  OG1 
15  1 Y 1 B THR 305 ? CG2 ? A THR 28  CG2 
16  1 Y 1 B THR 309 ? OG1 ? A THR 32  OG1 
17  1 Y 1 B THR 309 ? CG2 ? A THR 32  CG2 
18  1 Y 1 B LYS 318 ? CG  ? A LYS 41  CG  
19  1 Y 1 B LYS 318 ? CD  ? A LYS 41  CD  
20  1 Y 1 B LYS 318 ? CE  ? A LYS 41  CE  
21  1 Y 1 B LYS 318 ? NZ  ? A LYS 41  NZ  
22  1 Y 1 B TYR 322 ? CG  ? A TYR 45  CG  
23  1 Y 1 B TYR 322 ? CD1 ? A TYR 45  CD1 
24  1 Y 1 B TYR 322 ? CD2 ? A TYR 45  CD2 
25  1 Y 1 B TYR 322 ? CE1 ? A TYR 45  CE1 
26  1 Y 1 B TYR 322 ? CE2 ? A TYR 45  CE2 
27  1 Y 1 B TYR 322 ? CZ  ? A TYR 45  CZ  
28  1 Y 1 B TYR 322 ? OH  ? A TYR 45  OH  
29  1 Y 1 B LYS 328 ? CG  ? A LYS 51  CG  
30  1 Y 1 B LYS 328 ? CD  ? A LYS 51  CD  
31  1 Y 1 B LYS 328 ? CE  ? A LYS 51  CE  
32  1 Y 1 B LYS 328 ? NZ  ? A LYS 51  NZ  
33  1 Y 1 B LYS 335 ? NZ  ? A LYS 58  NZ  
34  1 Y 1 B CYS 336 ? O   ? A CYS 59  O   
35  1 Y 1 B ASP 340 ? CG  ? A ASP 63  CG  
36  1 Y 1 B ASP 340 ? OD1 ? A ASP 63  OD1 
37  1 Y 1 B ASP 340 ? OD2 ? A ASP 63  OD2 
38  1 Y 1 B LYS 346 ? CG  ? A LYS 69  CG  
39  1 Y 1 B LYS 346 ? CD  ? A LYS 69  CD  
40  1 Y 1 B LYS 346 ? CE  ? A LYS 69  CE  
41  1 Y 1 B LYS 346 ? NZ  ? A LYS 69  NZ  
42  1 Y 1 B GLU 350 ? CD  ? A GLU 73  CD  
43  1 Y 1 B GLU 350 ? OE1 ? A GLU 73  OE1 
44  1 Y 1 B GLU 350 ? OE2 ? A GLU 73  OE2 
45  1 Y 1 B LYS 354 ? CG  ? A LYS 77  CG  
46  1 Y 1 B LYS 354 ? CD  ? A LYS 77  CD  
47  1 Y 1 B LYS 354 ? CE  ? A LYS 77  CE  
48  1 Y 1 B LYS 354 ? NZ  ? A LYS 77  NZ  
49  1 Y 1 B HIS 370 ? CG  ? A HIS 93  CG  
50  1 Y 1 B HIS 370 ? ND1 ? A HIS 93  ND1 
51  1 Y 1 B HIS 370 ? CD2 ? A HIS 93  CD2 
52  1 Y 1 B HIS 370 ? CE1 ? A HIS 93  CE1 
53  1 Y 1 B HIS 370 ? NE2 ? A HIS 93  NE2 
54  1 Y 1 B GLU 390 ? CG  ? A GLU 113 CG  
55  1 Y 1 B GLU 390 ? CD  ? A GLU 113 CD  
56  1 Y 1 B GLU 390 ? OE1 ? A GLU 113 OE1 
57  1 Y 1 B GLU 390 ? OE2 ? A GLU 113 OE2 
58  1 Y 1 B GLU 416 ? CD  ? A GLU 139 CD  
59  1 Y 1 B GLU 416 ? OE1 ? A GLU 139 OE1 
60  1 Y 1 B GLU 416 ? OE2 ? A GLU 139 OE2 
61  1 Y 1 B GLU 472 ? CG  ? A GLU 195 CG  
62  1 Y 1 B GLU 472 ? CD  ? A GLU 195 CD  
63  1 Y 1 B GLU 472 ? OE1 ? A GLU 195 OE1 
64  1 Y 1 B GLU 472 ? OE2 ? A GLU 195 OE2 
65  1 Y 1 B GLU 502 ? OE2 ? A GLU 225 OE2 
66  1 Y 1 B LYS 512 ? CG  ? A LYS 235 CG  
67  1 Y 1 B LYS 512 ? CD  ? A LYS 235 CD  
68  1 Y 1 B LYS 512 ? CE  ? A LYS 235 CE  
69  1 Y 1 B LYS 512 ? NZ  ? A LYS 235 NZ  
70  1 Y 1 B THR 513 ? OG1 ? A THR 236 OG1 
71  1 Y 1 B LYS 530 ? CE  ? A LYS 253 CE  
72  1 Y 1 B LYS 530 ? NZ  ? A LYS 253 NZ  
73  1 Y 1 B ARG 539 ? CZ  ? A ARG 262 CZ  
74  1 Y 1 B ARG 539 ? NH1 ? A ARG 262 NH1 
75  1 Y 1 B ARG 539 ? NH2 ? A ARG 262 NH2 
76  1 Y 1 B LEU 555 ? CD1 ? A LEU 278 CD1 
77  1 Y 1 B GLU 562 ? CD  ? A GLU 285 CD  
78  1 Y 1 B GLU 562 ? OE1 ? A GLU 285 OE1 
79  1 Y 1 B GLU 562 ? OE2 ? A GLU 285 OE2 
80  1 Y 1 B ASP 579 ? OD1 ? A ASP 302 OD1 
81  1 Y 1 B ASP 579 ? OD2 ? A ASP 302 OD2 
82  1 Y 1 B GLU 581 ? CG  ? A GLU 304 CG  
83  1 Y 1 B GLU 581 ? CD  ? A GLU 304 CD  
84  1 Y 1 B GLU 581 ? OE1 ? A GLU 304 OE1 
85  1 Y 1 B GLU 581 ? OE2 ? A GLU 304 OE2 
86  1 Y 1 B LYS 582 ? CD  ? A LYS 305 CD  
87  1 Y 1 B LYS 582 ? CE  ? A LYS 305 CE  
88  1 Y 1 B LYS 582 ? NZ  ? A LYS 305 NZ  
89  1 Y 1 B GLU 626 ? OE2 ? A GLU 349 OE2 
90  1 Y 1 B LYS 636 ? NZ  ? A LYS 359 NZ  
91  1 Y 1 B LYS 660 ? CE  ? A LYS 383 CE  
92  1 Y 1 B LYS 660 ? NZ  ? A LYS 383 NZ  
93  1 Y 1 B LYS 678 ? NZ  ? A LYS 401 NZ  
94  1 Y 1 B GLU 697 ? OE2 ? A GLU 420 OE2 
95  1 Y 1 B GLU 711 ? CG  ? A GLU 434 CG  
96  1 Y 1 B GLU 711 ? CD  ? A GLU 434 CD  
97  1 Y 1 B GLU 711 ? OE1 ? A GLU 434 OE1 
98  1 Y 1 B GLU 711 ? OE2 ? A GLU 434 OE2 
99  1 Y 1 B ASN 712 ? CG  ? A ASN 435 CG  
100 1 Y 1 B ASN 712 ? OD1 ? A ASN 435 OD1 
101 1 Y 1 B ASN 712 ? ND2 ? A ASN 435 ND2 
102 1 Y 1 B GLU 720 ? CD  ? A GLU 443 CD  
103 1 Y 1 B GLU 720 ? OE1 ? A GLU 443 OE1 
104 1 Y 1 B GLU 720 ? OE2 ? A GLU 443 OE2 
105 1 Y 1 B ASP 761 ? OD1 ? A ASP 484 OD1 
106 1 Y 1 B ASP 761 ? OD2 ? A ASP 484 OD2 
107 1 Y 1 B LYS 771 ? CE  ? A LYS 494 CE  
108 1 Y 1 B LYS 771 ? NZ  ? A LYS 494 NZ  
109 1 Y 1 B LEU 773 ? CG  ? A LEU 496 CG  
110 1 Y 1 B LEU 773 ? CD1 ? A LEU 496 CD1 
111 1 Y 1 B LEU 773 ? CD2 ? A LEU 496 CD2 
112 1 Y 1 B LYS 781 ? NZ  ? A LYS 504 NZ  
113 1 Y 1 B GLN 791 ? CD  ? A GLN 514 CD  
114 1 Y 1 B GLN 791 ? OE1 ? A GLN 514 OE1 
115 1 Y 1 B GLN 791 ? NE2 ? A GLN 514 NE2 
116 1 Y 1 B GLU 793 ? CG  ? A GLU 516 CG  
117 1 Y 1 B GLU 793 ? CD  ? A GLU 516 CD  
118 1 Y 1 B GLU 793 ? OE1 ? A GLU 516 OE1 
119 1 Y 1 B GLU 793 ? OE2 ? A GLU 516 OE2 
120 1 Y 1 B GLN 796 ? CB  ? A GLN 519 CB  
121 1 Y 1 B GLN 796 ? CG  ? A GLN 519 CG  
122 1 Y 1 B GLN 796 ? CD  ? A GLN 519 CD  
123 1 Y 1 B GLN 796 ? OE1 ? A GLN 519 OE1 
124 1 Y 1 B GLN 796 ? NE2 ? A GLN 519 NE2 
125 1 Y 1 B GLU 797 ? CG  ? A GLU 520 CG  
126 1 Y 1 B GLU 797 ? CD  ? A GLU 520 CD  
127 1 Y 1 B GLU 797 ? OE1 ? A GLU 520 OE1 
128 1 Y 1 B GLU 797 ? OE2 ? A GLU 520 OE2 
129 1 Y 1 B ARG 799 ? NH1 ? A ARG 522 NH1 
130 1 Y 1 B ARG 799 ? NH2 ? A ARG 522 NH2 
131 1 Y 1 B LYS 800 ? CG  ? A LYS 523 CG  
132 1 Y 1 B LYS 800 ? CD  ? A LYS 523 CD  
133 1 Y 1 B LYS 800 ? CE  ? A LYS 523 CE  
134 1 Y 1 B LYS 800 ? NZ  ? A LYS 523 NZ  
135 1 Y 1 B ARG 811 ? CG  ? A ARG 534 CG  
136 1 Y 1 B ARG 811 ? CD  ? A ARG 534 CD  
137 1 Y 1 B ARG 811 ? NE  ? A ARG 534 NE  
138 1 Y 1 B ARG 811 ? CZ  ? A ARG 534 CZ  
139 1 Y 1 B ARG 811 ? NH1 ? A ARG 534 NH1 
140 1 Y 1 B ARG 811 ? NH2 ? A ARG 534 NH2 
141 1 Y 1 B ASP 825 ? OD2 ? A ASP 548 OD2 
142 1 Y 1 B LYS 841 ? NZ  ? A LYS 564 NZ  
143 1 Y 1 B GLU 853 ? CG  ? A GLU 576 CG  
144 1 Y 1 B GLU 853 ? CD  ? A GLU 576 CD  
145 1 Y 1 B GLU 853 ? OE1 ? A GLU 576 OE1 
146 1 Y 1 B GLU 853 ? OE2 ? A GLU 576 OE2 
147 1 Y 1 B GLU 854 ? OE1 ? A GLU 577 OE1 
148 1 Y 1 B GLN 860 ? CG  ? A GLN 583 CG  
149 1 Y 1 B GLN 860 ? CD  ? A GLN 583 CD  
150 1 Y 1 B GLN 860 ? OE1 ? A GLN 583 OE1 
151 1 Y 1 B GLN 860 ? NE2 ? A GLN 583 NE2 
152 1 Y 1 B VAL 867 ? CG1 ? A VAL 590 CG1 
153 1 Y 1 B VAL 867 ? CG2 ? A VAL 590 CG2 
154 1 Y 1 B HIS 868 ? CG  ? A HIS 591 CG  
155 1 Y 1 B HIS 868 ? ND1 ? A HIS 591 ND1 
156 1 Y 1 B HIS 868 ? CD2 ? A HIS 591 CD2 
157 1 Y 1 B HIS 868 ? CE1 ? A HIS 591 CE1 
158 1 Y 1 B HIS 868 ? NE2 ? A HIS 591 NE2 
159 1 Y 1 B LEU 870 ? CD1 ? A LEU 593 CD1 
160 1 Y 1 B LEU 870 ? CD2 ? A LEU 593 CD2 
161 1 N 1 B PEG 905 ? O1  ? F PEG 1   O1  
162 1 N 1 B PEG 911 ? O1  ? L PEG 1   O1  
163 1 N 1 B PEG 911 ? O4  ? L PEG 1   O4  
164 1 N 1 B PEG 912 ? O1  ? M PEG 1   O1  
165 1 N 1 B PEG 912 ? O4  ? M PEG 1   O4  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASES   ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E4V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.088 
_cell.length_a_esd                 ? 
_cell.length_b                     114.088 
_cell.length_b_esd                 ? 
_cell.length_c                     145.397 
_cell.length_c_esd                 ? 
_cell.volume                       1892497.783 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9E4V 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9E4V 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.53 
_exptl_crystal.description                  Rhombohedral 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100mM MES, pH 6.0, 18% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'Rh coated collimating mirror, K-B focusing mirrors' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Liquid nitrogen-cooled double crystal monochromator, non fixed exit slit' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979460 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979460 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          53.38 
_reflns.entry_id                                       9E4V 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.36 
_reflns.d_resolution_low                               61.31 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     40128 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.96 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                26.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.27 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.209 
_reflns.pdbx_Rpim_I_all                                0.04011 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.2051 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.36 
_reflns_shell.d_res_low                                     2.444 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.13 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3953 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               26.4 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               4.067 
_reflns_shell.pdbx_Rpim_I_all                               0.7858 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.457 
_reflns_shell.pdbx_CC_star                                  0.792 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.95 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.989 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               64.49 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9E4V 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.36 
_refine.ls_d_res_low                             61.31 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     40128 
_refine.ls_number_reflns_R_free                  2065 
_refine.ls_number_reflns_R_work                  38211 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2002 
_refine.ls_R_factor_R_free                       0.2314 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1985 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.1950 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3101 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.36 
_refine_hist.d_res_low                        61.31 
_refine_hist.number_atoms_solvent             91 
_refine_hist.number_atoms_total               4283 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4127 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0078  ? 4288 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9727  ? 5794 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0549  ? 657  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0117  ? 735  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9536 ? 1608 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.36 2.41  . . 137 2500 99.96  . . . . 0.3032 . . . . . . . . . . . 0.3576 
'X-RAY DIFFRACTION' 2.41 2.47  . . 148 2483 100.00 . . . . 0.2950 . . . . . . . . . . . 0.3293 
'X-RAY DIFFRACTION' 2.47 2.54  . . 148 2506 99.96  . . . . 0.2646 . . . . . . . . . . . 0.3309 
'X-RAY DIFFRACTION' 2.54 2.61  . . 134 2498 100.00 . . . . 0.2471 . . . . . . . . . . . 0.2536 
'X-RAY DIFFRACTION' 2.61 2.70  . . 129 2505 100.00 . . . . 0.2437 . . . . . . . . . . . 0.2495 
'X-RAY DIFFRACTION' 2.70 2.79  . . 113 2557 100.00 . . . . 0.2495 . . . . . . . . . . . 0.2648 
'X-RAY DIFFRACTION' 2.79 2.91  . . 130 2513 100.00 . . . . 0.2396 . . . . . . . . . . . 0.3022 
'X-RAY DIFFRACTION' 2.91 3.04  . . 154 2507 100.00 . . . . 0.2146 . . . . . . . . . . . 0.2518 
'X-RAY DIFFRACTION' 3.04 3.20  . . 130 2535 100.00 . . . . 0.1943 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 3.20 3.40  . . 134 2547 100.00 . . . . 0.1955 . . . . . . . . . . . 0.2459 
'X-RAY DIFFRACTION' 3.40 3.66  . . 143 2531 99.96  . . . . 0.1923 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 3.66 4.03  . . 140 2572 100.00 . . . . 0.1674 . . . . . . . . . . . 0.1734 
'X-RAY DIFFRACTION' 4.03 4.61  . . 122 2591 100.00 . . . . 0.1550 . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 4.61 5.81  . . 153 2611 100.00 . . . . 0.1852 . . . . . . . . . . . 0.2445 
'X-RAY DIFFRACTION' 5.81 61.31 . . 150 2755 99.76  . . . . 0.2069 . . . . . . . . . . . 0.2164 
# 
_struct.entry_id                     9E4V 
_struct.title                        'The structure of human vacuolar protein sorting 34 catalytic domain bound to MES' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9E4V 
_struct_keywords.text            
'Phosphatidylinositol 3-phosphate, Lipid regulator, autophagy, membrane trafficking, endocytosis, enzyme, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 7 ? 
J N N 7 ? 
K N N 7 ? 
L N N 5 ? 
M N N 5 ? 
N N N 8 ? 
O N N 8 ? 
P N N 8 ? 
Q N N 9 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PK3C3_HUMAN 
_struct_ref.pdbx_db_accession          Q8NEB9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSS
HYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSP
LPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALL
KGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETA
TLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVP
VAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRD
PKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLD
LSDEEAVHYMQSLIDESVHALF
;
_struct_ref.pdbx_align_begin           290 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9E4V 
_struct_ref_seq.pdbx_strand_id                B 
_struct_ref_seq.seq_align_beg                 13 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 594 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8NEB9 
_struct_ref_seq.db_align_beg                  290 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  871 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       290 
_struct_ref_seq.pdbx_auth_seq_align_end       871 
# 
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 9E4V MET B 1  ? UNP Q8NEB9 ? ? 'expression tag' 278 1  
1 9E4V GLY B 2  ? UNP Q8NEB9 ? ? 'expression tag' 279 2  
1 9E4V HIS B 3  ? UNP Q8NEB9 ? ? 'expression tag' 280 3  
1 9E4V HIS B 4  ? UNP Q8NEB9 ? ? 'expression tag' 281 4  
1 9E4V HIS B 5  ? UNP Q8NEB9 ? ? 'expression tag' 282 5  
1 9E4V HIS B 6  ? UNP Q8NEB9 ? ? 'expression tag' 283 6  
1 9E4V HIS B 7  ? UNP Q8NEB9 ? ? 'expression tag' 284 7  
1 9E4V HIS B 8  ? UNP Q8NEB9 ? ? 'expression tag' 285 8  
1 9E4V HIS B 9  ? UNP Q8NEB9 ? ? 'expression tag' 286 9  
1 9E4V HIS B 10 ? UNP Q8NEB9 ? ? 'expression tag' 287 10 
1 9E4V HIS B 11 ? UNP Q8NEB9 ? ? 'expression tag' 288 11 
1 9E4V HIS B 12 ? UNP Q8NEB9 ? ? 'expression tag' 289 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 14  ? SER A 24  ? ALA B 291 SER B 301 1 ? 11 
HELX_P HELX_P2  AA2 THR A 32  ? PHE A 42  ? THR B 309 PHE B 319 1 ? 11 
HELX_P HELX_P3  AA3 ARG A 43  ? THR A 47  ? ARG B 320 THR B 324 5 ? 5  
HELX_P HELX_P4  AA4 GLN A 49  ? LYS A 51  ? GLN B 326 LYS B 328 5 ? 3  
HELX_P HELX_P5  AA5 ALA A 52  ? CYS A 59  ? ALA B 329 CYS B 336 1 ? 8  
HELX_P HELX_P6  AA6 LEU A 64  ? TRP A 78  ? LEU B 341 TRP B 355 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 82  ? LEU A 90  ? ASP B 359 LEU B 367 1 ? 9  
HELX_P HELX_P8  AA8 ASN A 96  ? ARG A 108 ? ASN B 373 ARG B 385 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 111 ? LEU A 126 ? ASP B 388 LEU B 403 1 ? 16 
HELX_P HELX_P10 AB1 LYS A 127 ? GLU A 129 ? LYS B 404 GLU B 406 5 ? 3  
HELX_P HELX_P11 AB2 ASN A 130 ? GLY A 137 ? ASN B 407 GLY B 414 1 ? 8  
HELX_P HELX_P12 AB3 ASP A 197 ? CYS A 207 ? ASP B 474 CYS B 484 1 ? 11 
HELX_P HELX_P13 AB4 ASN A 209 ? ASP A 226 ? ASN B 486 ASP B 503 1 ? 18 
HELX_P HELX_P14 AB5 ASP A 226 ? ASP A 233 ? ASP B 503 ASP B 510 1 ? 8  
HELX_P HELX_P15 AB6 ASP A 233 ? LYS A 253 ? ASP B 510 LYS B 530 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 255 ? GLN A 283 ? ASP B 532 GLN B 560 1 ? 29 
HELX_P HELX_P17 AB8 ASN A 288 ? ASP A 302 ? ASN B 565 ASP B 579 1 ? 15 
HELX_P HELX_P18 AB9 PRO A 329 ? ALA A 332 ? PRO B 606 ALA B 609 5 ? 4  
HELX_P HELX_P19 AC1 LEU A 364 ? GLU A 384 ? LEU B 641 GLU B 661 1 ? 21 
HELX_P HELX_P20 AC2 VAL A 413 ? GLU A 420 ? VAL B 690 GLU B 697 1 ? 8  
HELX_P HELX_P21 AC3 SER A 422 ? ALA A 431 ? SER B 699 ALA B 708 1 ? 10 
HELX_P HELX_P22 AC4 GLY A 436 ? ILE A 440 ? GLY B 713 ILE B 717 5 ? 5  
HELX_P HELX_P23 AC5 SER A 441 ? GLY A 463 ? SER B 718 GLY B 740 1 ? 23 
HELX_P HELX_P24 AC6 ASN A 503 ? MET A 510 ? ASN B 780 MET B 787 1 ? 8  
HELX_P HELX_P25 AC7 SER A 515 ? TYR A 535 ? SER B 792 TYR B 812 1 ? 21 
HELX_P HELX_P26 AC8 TYR A 535 ? LEU A 545 ? TYR B 812 LEU B 822 1 ? 11 
HELX_P HELX_P27 AC9 ILE A 551 ? LEU A 556 ? ILE B 828 LEU B 833 1 ? 6  
HELX_P HELX_P28 AD1 GLU A 557 ? ASP A 559 ? GLU B 834 ASP B 836 5 ? 3  
HELX_P HELX_P29 AD2 LYS A 560 ? ARG A 570 ? LYS B 837 ARG B 847 1 ? 11 
HELX_P HELX_P30 AD3 SER A 574 ? LEU A 593 ? SER B 851 LEU B 870 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 314 ? LEU A 316 ? ILE B 591 LEU B 593 
AA1 2 GLU A 319 ? ILE A 327 ? GLU B 596 ILE B 604 
AA1 3 ALA A 342 ? THR A 348 ? ALA B 619 THR B 625 
AA1 4 THR A 333 ? LEU A 334 ? THR B 610 LEU B 611 
AA2 1 ILE A 314 ? LEU A 316 ? ILE B 591 LEU B 593 
AA2 2 GLU A 319 ? ILE A 327 ? GLU B 596 ILE B 604 
AA2 3 ALA A 342 ? THR A 348 ? ALA B 619 THR B 625 
AA2 4 LYS A 353 ? HIS A 360 ? LYS B 630 HIS B 637 
AA2 5 HIS A 402 ? GLN A 406 ? HIS B 679 GLN B 683 
AA2 6 VAL A 395 ? ALA A 397 ? VAL B 672 ALA B 674 
AA3 1 VAL A 411 ? PRO A 412 ? VAL B 688 PRO B 689 
AA3 2 LEU A 472 ? LEU A 474 ? LEU B 749 LEU B 751 
AA3 3 LEU A 480 ? HIS A 482 ? LEU B 757 HIS B 759 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 314 ? N ILE B 591 O ILE A 324 ? O ILE B 601 
AA1 2 3 N GLY A 326 ? N GLY B 603 O LYS A 347 ? O LYS B 624 
AA1 3 4 O GLN A 343 ? O GLN B 620 N THR A 333 ? N THR B 610 
AA2 1 2 N ILE A 314 ? N ILE B 591 O ILE A 324 ? O ILE B 601 
AA2 2 3 N GLY A 326 ? N GLY B 603 O LYS A 347 ? O LYS B 624 
AA2 3 4 N ALA A 342 ? N ALA B 619 O PHE A 358 ? O PHE B 635 
AA2 4 5 N ILE A 357 ? N ILE B 634 O MET A 405 ? O MET B 682 
AA2 5 6 O PHE A 404 ? O PHE B 681 N LEU A 396 ? N LEU B 673 
AA3 1 2 N VAL A 411 ? N VAL B 688 O LEU A 474 ? O LEU B 751 
AA3 2 3 N LEU A 473 ? N LEU B 750 O PHE A 481 ? O PHE B 758 
# 
_pdbx_entry_details.entry_id                   9E4V 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 B 338 ? ? -68.67  92.10  
2  1 ASP B 510 ? ? -150.60 73.75  
3  1 ASN B 584 ? ? 71.27   32.31  
4  1 LEU B 590 ? ? 25.37   70.70  
5  1 GLU B 596 ? ? -157.39 87.18  
6  1 SER B 699 ? ? -177.61 149.49 
7  1 ALA B 708 ? ? -152.49 58.45  
8  1 SER B 710 ? ? -166.81 111.60 
9  1 ASP B 761 ? ? 56.77   81.40  
10 1 PHE B 762 ? ? -98.79  59.07  
11 1 GLU B 834 ? ? -150.54 63.76  
12 1 LEU B 848 ? ? -57.66  -8.59  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 536 ? ? 0.076 'SIDE CHAIN' 
2 1 ARG B 602 ? ? 0.112 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 28.6980664039 -15.4617723005 4.93871265794 0.562081632074 ? 0.231031932372  ? 0.062824647767  ? 
0.573712422435 ? 0.0584348935592 ? 0.482320781775 ? 1.82368073271 ? -0.556488700281 ? -1.35937320018 ? 4.4573328977   ? 
0.186672848019  ? 2.03696899933 ? -0.133848881186  ? 0.10004169087   ? -0.321878321236 ? -0.276205727047 ? -0.125979343493  ? 
-0.24475658848     ? 0.651934964978 ? 0.481662067434  ? 0.189641678102  ? 
2 'X-RAY DIFFRACTION' ? refined 12.0196740009 14.8366038684  18.0465070635 0.628395996531 ? 0.0135151014022 ? 0.139377956726  ? 
0.306607705104 ? 0.0890380844243 ? 0.528573442692 ? 1.76402583886 ? -0.55867625277  ? -1.28267650961 ? 0.449865455302 ? 
-0.325453064943 ? 4.69090520588 ? 0.298253070008   ? 0.0368685323838 ? 0.417223209492  ? 0.222938774687  ? -0.0713164645523 ? 
-0.000235225246061 ? -1.00044704825 ? 0.0635013686324 ? -0.269446039207 ? 
3 'X-RAY DIFFRACTION' ? refined 2.68739278381 -13.4758170415 18.9827676731 0.461696303302 ? -0.054584127079 ? 0.0342118656215 ? 
0.338539794198 ? 0.0163680456307 ? 0.397223509749 ? 3.48759705162 ? -0.413257979529 ? -1.17533477535 ? 1.59121617531  ? 
-0.136346340785 ? 2.75118456143 ? -0.0900286906567 ? 0.147024876605  ? -0.526231233673 ? 0.0407007778106 ? -0.0470947691594 ? 
0.209517468868     ? 0.57823341775  ? -0.432662593879 ? 0.114295474039  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 E 1   B 291 ? E 190 B 532 ? ? 
;chain 'B' and (resid 291 through 532 )
;
2 'X-RAY DIFFRACTION' 2 E 191 B 533 ? E 287 B 629 ? ? 
;chain 'B' and (resid 533 through 629 )
;
3 'X-RAY DIFFRACTION' 3 E 288 B 630 ? E 528 B 870 ? ? 
;chain 'B' and (resid 630 through 870 )
;
# 
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 B MET 278 ? A MET 1   
2  1 Y 1 B GLY 279 ? A GLY 2   
3  1 Y 1 B HIS 280 ? A HIS 3   
4  1 Y 1 B HIS 281 ? A HIS 4   
5  1 Y 1 B HIS 282 ? A HIS 5   
6  1 Y 1 B HIS 283 ? A HIS 6   
7  1 Y 1 B HIS 284 ? A HIS 7   
8  1 Y 1 B HIS 285 ? A HIS 8   
9  1 Y 1 B HIS 286 ? A HIS 9   
10 1 Y 1 B HIS 287 ? A HIS 10  
11 1 Y 1 B HIS 288 ? A HIS 11  
12 1 Y 1 B HIS 289 ? A HIS 12  
13 1 Y 1 B ALA 290 ? A ALA 13  
14 1 Y 1 B THR 418 ? A THR 141 
15 1 Y 1 B LYS 419 ? A LYS 142 
16 1 Y 1 B LYS 420 ? A LYS 143 
17 1 Y 1 B ASP 421 ? A ASP 144 
18 1 Y 1 B SER 422 ? A SER 145 
19 1 Y 1 B GLN 423 ? A GLN 146 
20 1 Y 1 B SER 424 ? A SER 147 
21 1 Y 1 B SER 425 ? A SER 148 
22 1 Y 1 B VAL 426 ? A VAL 149 
23 1 Y 1 B SER 427 ? A SER 150 
24 1 Y 1 B GLU 428 ? A GLU 151 
25 1 Y 1 B ASN 429 ? A ASN 152 
26 1 Y 1 B VAL 430 ? A VAL 153 
27 1 Y 1 B SER 431 ? A SER 154 
28 1 Y 1 B ASN 432 ? A ASN 155 
29 1 Y 1 B SER 433 ? A SER 156 
30 1 Y 1 B GLY 434 ? A GLY 157 
31 1 Y 1 B ILE 435 ? A ILE 158 
32 1 Y 1 B ASN 436 ? A ASN 159 
33 1 Y 1 B SER 437 ? A SER 160 
34 1 Y 1 B ALA 438 ? A ALA 161 
35 1 Y 1 B GLU 439 ? A GLU 162 
36 1 Y 1 B ILE 440 ? A ILE 163 
37 1 Y 1 B ASP 441 ? A ASP 164 
38 1 Y 1 B SER 442 ? A SER 165 
39 1 Y 1 B SER 443 ? A SER 166 
40 1 Y 1 B GLN 444 ? A GLN 167 
41 1 Y 1 B ILE 445 ? A ILE 168 
42 1 Y 1 B ILE 446 ? A ILE 169 
43 1 Y 1 B THR 447 ? A THR 170 
44 1 Y 1 B SER 448 ? A SER 171 
45 1 Y 1 B PRO 449 ? A PRO 172 
46 1 Y 1 B LEU 450 ? A LEU 173 
47 1 Y 1 B PRO 451 ? A PRO 174 
48 1 Y 1 B SER 452 ? A SER 175 
49 1 Y 1 B VAL 453 ? A VAL 176 
50 1 Y 1 B SER 454 ? A SER 177 
51 1 Y 1 B SER 455 ? A SER 178 
52 1 Y 1 B PRO 456 ? A PRO 179 
53 1 Y 1 B PRO 457 ? A PRO 180 
54 1 Y 1 B PRO 458 ? A PRO 181 
55 1 Y 1 B ALA 459 ? A ALA 182 
56 1 Y 1 B SER 460 ? A SER 183 
57 1 Y 1 B LYS 461 ? A LYS 184 
58 1 Y 1 B THR 462 ? A THR 185 
59 1 Y 1 B LYS 463 ? A LYS 186 
60 1 Y 1 B GLU 464 ? A GLU 187 
61 1 Y 1 B VAL 465 ? A VAL 188 
62 1 Y 1 B PRO 466 ? A PRO 189 
63 1 Y 1 B ASP 467 ? A ASP 190 
64 1 Y 1 B GLY 468 ? A GLY 191 
65 1 Y 1 B GLU 469 ? A GLU 192 
66 1 Y 1 B PHE 871 ? A PHE 594 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
DMS S    S  N N 89  
DMS O    O  N N 90  
DMS C1   C  N N 91  
DMS C2   C  N N 92  
DMS H11  H  N N 93  
DMS H12  H  N N 94  
DMS H13  H  N N 95  
DMS H21  H  N N 96  
DMS H22  H  N N 97  
DMS H23  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
GOL C1   C  N N 148 
GOL O1   O  N N 149 
GOL C2   C  N N 150 
GOL O2   O  N N 151 
GOL C3   C  N N 152 
GOL O3   O  N N 153 
GOL H11  H  N N 154 
GOL H12  H  N N 155 
GOL HO1  H  N N 156 
GOL H2   H  N N 157 
GOL HO2  H  N N 158 
GOL H31  H  N N 159 
GOL H32  H  N N 160 
GOL HO3  H  N N 161 
HIS N    N  N N 162 
HIS CA   C  N S 163 
HIS C    C  N N 164 
HIS O    O  N N 165 
HIS CB   C  N N 166 
HIS CG   C  Y N 167 
HIS ND1  N  Y N 168 
HIS CD2  C  Y N 169 
HIS CE1  C  Y N 170 
HIS NE2  N  Y N 171 
HIS OXT  O  N N 172 
HIS H    H  N N 173 
HIS H2   H  N N 174 
HIS HA   H  N N 175 
HIS HB2  H  N N 176 
HIS HB3  H  N N 177 
HIS HD1  H  N N 178 
HIS HD2  H  N N 179 
HIS HE1  H  N N 180 
HIS HE2  H  N N 181 
HIS HXT  H  N N 182 
HOH O    O  N N 183 
HOH H1   H  N N 184 
HOH H2   H  N N 185 
ILE N    N  N N 186 
ILE CA   C  N S 187 
ILE C    C  N N 188 
ILE O    O  N N 189 
ILE CB   C  N S 190 
ILE CG1  C  N N 191 
ILE CG2  C  N N 192 
ILE CD1  C  N N 193 
ILE OXT  O  N N 194 
ILE H    H  N N 195 
ILE H2   H  N N 196 
ILE HA   H  N N 197 
ILE HB   H  N N 198 
ILE HG12 H  N N 199 
ILE HG13 H  N N 200 
ILE HG21 H  N N 201 
ILE HG22 H  N N 202 
ILE HG23 H  N N 203 
ILE HD11 H  N N 204 
ILE HD12 H  N N 205 
ILE HD13 H  N N 206 
ILE HXT  H  N N 207 
K   K    K  N N 208 
LEU N    N  N N 209 
LEU CA   C  N S 210 
LEU C    C  N N 211 
LEU O    O  N N 212 
LEU CB   C  N N 213 
LEU CG   C  N N 214 
LEU CD1  C  N N 215 
LEU CD2  C  N N 216 
LEU OXT  O  N N 217 
LEU H    H  N N 218 
LEU H2   H  N N 219 
LEU HA   H  N N 220 
LEU HB2  H  N N 221 
LEU HB3  H  N N 222 
LEU HG   H  N N 223 
LEU HD11 H  N N 224 
LEU HD12 H  N N 225 
LEU HD13 H  N N 226 
LEU HD21 H  N N 227 
LEU HD22 H  N N 228 
LEU HD23 H  N N 229 
LEU HXT  H  N N 230 
LYS N    N  N N 231 
LYS CA   C  N S 232 
LYS C    C  N N 233 
LYS O    O  N N 234 
LYS CB   C  N N 235 
LYS CG   C  N N 236 
LYS CD   C  N N 237 
LYS CE   C  N N 238 
LYS NZ   N  N N 239 
LYS OXT  O  N N 240 
LYS H    H  N N 241 
LYS H2   H  N N 242 
LYS HA   H  N N 243 
LYS HB2  H  N N 244 
LYS HB3  H  N N 245 
LYS HG2  H  N N 246 
LYS HG3  H  N N 247 
LYS HD2  H  N N 248 
LYS HD3  H  N N 249 
LYS HE2  H  N N 250 
LYS HE3  H  N N 251 
LYS HZ1  H  N N 252 
LYS HZ2  H  N N 253 
LYS HZ3  H  N N 254 
LYS HXT  H  N N 255 
MES O1   O  N N 256 
MES C2   C  N N 257 
MES C3   C  N N 258 
MES N4   N  N N 259 
MES C5   C  N N 260 
MES C6   C  N N 261 
MES C7   C  N N 262 
MES C8   C  N N 263 
MES S    S  N N 264 
MES O1S  O  N N 265 
MES O2S  O  N N 266 
MES O3S  O  N N 267 
MES H21  H  N N 268 
MES H22  H  N N 269 
MES H31  H  N N 270 
MES H32  H  N N 271 
MES HN4  H  N N 272 
MES H51  H  N N 273 
MES H52  H  N N 274 
MES H61  H  N N 275 
MES H62  H  N N 276 
MES H71  H  N N 277 
MES H72  H  N N 278 
MES H81  H  N N 279 
MES H82  H  N N 280 
MET N    N  N N 281 
MET CA   C  N S 282 
MET C    C  N N 283 
MET O    O  N N 284 
MET CB   C  N N 285 
MET CG   C  N N 286 
MET SD   S  N N 287 
MET CE   C  N N 288 
MET OXT  O  N N 289 
MET H    H  N N 290 
MET H2   H  N N 291 
MET HA   H  N N 292 
MET HB2  H  N N 293 
MET HB3  H  N N 294 
MET HG2  H  N N 295 
MET HG3  H  N N 296 
MET HE1  H  N N 297 
MET HE2  H  N N 298 
MET HE3  H  N N 299 
MET HXT  H  N N 300 
PEG C1   C  N N 301 
PEG O1   O  N N 302 
PEG C2   C  N N 303 
PEG O2   O  N N 304 
PEG C3   C  N N 305 
PEG C4   C  N N 306 
PEG O4   O  N N 307 
PEG H11  H  N N 308 
PEG H12  H  N N 309 
PEG HO1  H  N N 310 
PEG H21  H  N N 311 
PEG H22  H  N N 312 
PEG H31  H  N N 313 
PEG H32  H  N N 314 
PEG H41  H  N N 315 
PEG H42  H  N N 316 
PEG HO4  H  N N 317 
PG4 O1   O  N N 318 
PG4 C1   C  N N 319 
PG4 C2   C  N N 320 
PG4 O2   O  N N 321 
PG4 C3   C  N N 322 
PG4 C4   C  N N 323 
PG4 O3   O  N N 324 
PG4 C5   C  N N 325 
PG4 C6   C  N N 326 
PG4 O4   O  N N 327 
PG4 C7   C  N N 328 
PG4 C8   C  N N 329 
PG4 O5   O  N N 330 
PG4 HO1  H  N N 331 
PG4 H11  H  N N 332 
PG4 H12  H  N N 333 
PG4 H21  H  N N 334 
PG4 H22  H  N N 335 
PG4 H31  H  N N 336 
PG4 H32  H  N N 337 
PG4 H41  H  N N 338 
PG4 H42  H  N N 339 
PG4 H51  H  N N 340 
PG4 H52  H  N N 341 
PG4 H61  H  N N 342 
PG4 H62  H  N N 343 
PG4 H71  H  N N 344 
PG4 H72  H  N N 345 
PG4 H81  H  N N 346 
PG4 H82  H  N N 347 
PG4 HO5  H  N N 348 
PHE N    N  N N 349 
PHE CA   C  N S 350 
PHE C    C  N N 351 
PHE O    O  N N 352 
PHE CB   C  N N 353 
PHE CG   C  Y N 354 
PHE CD1  C  Y N 355 
PHE CD2  C  Y N 356 
PHE CE1  C  Y N 357 
PHE CE2  C  Y N 358 
PHE CZ   C  Y N 359 
PHE OXT  O  N N 360 
PHE H    H  N N 361 
PHE H2   H  N N 362 
PHE HA   H  N N 363 
PHE HB2  H  N N 364 
PHE HB3  H  N N 365 
PHE HD1  H  N N 366 
PHE HD2  H  N N 367 
PHE HE1  H  N N 368 
PHE HE2  H  N N 369 
PHE HZ   H  N N 370 
PHE HXT  H  N N 371 
PRO N    N  N N 372 
PRO CA   C  N S 373 
PRO C    C  N N 374 
PRO O    O  N N 375 
PRO CB   C  N N 376 
PRO CG   C  N N 377 
PRO CD   C  N N 378 
PRO OXT  O  N N 379 
PRO H    H  N N 380 
PRO HA   H  N N 381 
PRO HB2  H  N N 382 
PRO HB3  H  N N 383 
PRO HG2  H  N N 384 
PRO HG3  H  N N 385 
PRO HD2  H  N N 386 
PRO HD3  H  N N 387 
PRO HXT  H  N N 388 
SER N    N  N N 389 
SER CA   C  N S 390 
SER C    C  N N 391 
SER O    O  N N 392 
SER CB   C  N N 393 
SER OG   O  N N 394 
SER OXT  O  N N 395 
SER H    H  N N 396 
SER H2   H  N N 397 
SER HA   H  N N 398 
SER HB2  H  N N 399 
SER HB3  H  N N 400 
SER HG   H  N N 401 
SER HXT  H  N N 402 
THR N    N  N N 403 
THR CA   C  N S 404 
THR C    C  N N 405 
THR O    O  N N 406 
THR CB   C  N R 407 
THR OG1  O  N N 408 
THR CG2  C  N N 409 
THR OXT  O  N N 410 
THR H    H  N N 411 
THR H2   H  N N 412 
THR HA   H  N N 413 
THR HB   H  N N 414 
THR HG1  H  N N 415 
THR HG21 H  N N 416 
THR HG22 H  N N 417 
THR HG23 H  N N 418 
THR HXT  H  N N 419 
TRP N    N  N N 420 
TRP CA   C  N S 421 
TRP C    C  N N 422 
TRP O    O  N N 423 
TRP CB   C  N N 424 
TRP CG   C  Y N 425 
TRP CD1  C  Y N 426 
TRP CD2  C  Y N 427 
TRP NE1  N  Y N 428 
TRP CE2  C  Y N 429 
TRP CE3  C  Y N 430 
TRP CZ2  C  Y N 431 
TRP CZ3  C  Y N 432 
TRP CH2  C  Y N 433 
TRP OXT  O  N N 434 
TRP H    H  N N 435 
TRP H2   H  N N 436 
TRP HA   H  N N 437 
TRP HB2  H  N N 438 
TRP HB3  H  N N 439 
TRP HD1  H  N N 440 
TRP HE1  H  N N 441 
TRP HE3  H  N N 442 
TRP HZ2  H  N N 443 
TRP HZ3  H  N N 444 
TRP HH2  H  N N 445 
TRP HXT  H  N N 446 
TYR N    N  N N 447 
TYR CA   C  N S 448 
TYR C    C  N N 449 
TYR O    O  N N 450 
TYR CB   C  N N 451 
TYR CG   C  Y N 452 
TYR CD1  C  Y N 453 
TYR CD2  C  Y N 454 
TYR CE1  C  Y N 455 
TYR CE2  C  Y N 456 
TYR CZ   C  Y N 457 
TYR OH   O  N N 458 
TYR OXT  O  N N 459 
TYR H    H  N N 460 
TYR H2   H  N N 461 
TYR HA   H  N N 462 
TYR HB2  H  N N 463 
TYR HB3  H  N N 464 
TYR HD1  H  N N 465 
TYR HD2  H  N N 466 
TYR HE1  H  N N 467 
TYR HE2  H  N N 468 
TYR HH   H  N N 469 
TYR HXT  H  N N 470 
VAL N    N  N N 471 
VAL CA   C  N S 472 
VAL C    C  N N 473 
VAL O    O  N N 474 
VAL CB   C  N N 475 
VAL CG1  C  N N 476 
VAL CG2  C  N N 477 
VAL OXT  O  N N 478 
VAL H    H  N N 479 
VAL H2   H  N N 480 
VAL HA   H  N N 481 
VAL HB   H  N N 482 
VAL HG11 H  N N 483 
VAL HG12 H  N N 484 
VAL HG13 H  N N 485 
VAL HG21 H  N N 486 
VAL HG22 H  N N 487 
VAL HG23 H  N N 488 
VAL HXT  H  N N 489 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
GOL C1  O1   sing N N 138 
GOL C1  C2   sing N N 139 
GOL C1  H11  sing N N 140 
GOL C1  H12  sing N N 141 
GOL O1  HO1  sing N N 142 
GOL C2  O2   sing N N 143 
GOL C2  C3   sing N N 144 
GOL C2  H2   sing N N 145 
GOL O2  HO2  sing N N 146 
GOL C3  O3   sing N N 147 
GOL C3  H31  sing N N 148 
GOL C3  H32  sing N N 149 
GOL O3  HO3  sing N N 150 
HIS N   CA   sing N N 151 
HIS N   H    sing N N 152 
HIS N   H2   sing N N 153 
HIS CA  C    sing N N 154 
HIS CA  CB   sing N N 155 
HIS CA  HA   sing N N 156 
HIS C   O    doub N N 157 
HIS C   OXT  sing N N 158 
HIS CB  CG   sing N N 159 
HIS CB  HB2  sing N N 160 
HIS CB  HB3  sing N N 161 
HIS CG  ND1  sing Y N 162 
HIS CG  CD2  doub Y N 163 
HIS ND1 CE1  doub Y N 164 
HIS ND1 HD1  sing N N 165 
HIS CD2 NE2  sing Y N 166 
HIS CD2 HD2  sing N N 167 
HIS CE1 NE2  sing Y N 168 
HIS CE1 HE1  sing N N 169 
HIS NE2 HE2  sing N N 170 
HIS OXT HXT  sing N N 171 
HOH O   H1   sing N N 172 
HOH O   H2   sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MES O1  C2   sing N N 240 
MES O1  C6   sing N N 241 
MES C2  C3   sing N N 242 
MES C2  H21  sing N N 243 
MES C2  H22  sing N N 244 
MES C3  N4   sing N N 245 
MES C3  H31  sing N N 246 
MES C3  H32  sing N N 247 
MES N4  C5   sing N N 248 
MES N4  C7   sing N N 249 
MES N4  HN4  sing N N 250 
MES C5  C6   sing N N 251 
MES C5  H51  sing N N 252 
MES C5  H52  sing N N 253 
MES C6  H61  sing N N 254 
MES C6  H62  sing N N 255 
MES C7  C8   sing N N 256 
MES C7  H71  sing N N 257 
MES C7  H72  sing N N 258 
MES C8  S    sing N N 259 
MES C8  H81  sing N N 260 
MES C8  H82  sing N N 261 
MES S   O1S  doub N N 262 
MES S   O2S  doub N N 263 
MES S   O3S  sing N N 264 
MET N   CA   sing N N 265 
MET N   H    sing N N 266 
MET N   H2   sing N N 267 
MET CA  C    sing N N 268 
MET CA  CB   sing N N 269 
MET CA  HA   sing N N 270 
MET C   O    doub N N 271 
MET C   OXT  sing N N 272 
MET CB  CG   sing N N 273 
MET CB  HB2  sing N N 274 
MET CB  HB3  sing N N 275 
MET CG  SD   sing N N 276 
MET CG  HG2  sing N N 277 
MET CG  HG3  sing N N 278 
MET SD  CE   sing N N 279 
MET CE  HE1  sing N N 280 
MET CE  HE2  sing N N 281 
MET CE  HE3  sing N N 282 
MET OXT HXT  sing N N 283 
PEG C1  O1   sing N N 284 
PEG C1  C2   sing N N 285 
PEG C1  H11  sing N N 286 
PEG C1  H12  sing N N 287 
PEG O1  HO1  sing N N 288 
PEG C2  O2   sing N N 289 
PEG C2  H21  sing N N 290 
PEG C2  H22  sing N N 291 
PEG O2  C3   sing N N 292 
PEG C3  C4   sing N N 293 
PEG C3  H31  sing N N 294 
PEG C3  H32  sing N N 295 
PEG C4  O4   sing N N 296 
PEG C4  H41  sing N N 297 
PEG C4  H42  sing N N 298 
PEG O4  HO4  sing N N 299 
PG4 O1  C1   sing N N 300 
PG4 O1  HO1  sing N N 301 
PG4 C1  C2   sing N N 302 
PG4 C1  H11  sing N N 303 
PG4 C1  H12  sing N N 304 
PG4 C2  O2   sing N N 305 
PG4 C2  H21  sing N N 306 
PG4 C2  H22  sing N N 307 
PG4 O2  C3   sing N N 308 
PG4 C3  C4   sing N N 309 
PG4 C3  H31  sing N N 310 
PG4 C3  H32  sing N N 311 
PG4 C4  O3   sing N N 312 
PG4 C4  H41  sing N N 313 
PG4 C4  H42  sing N N 314 
PG4 O3  C5   sing N N 315 
PG4 C5  C6   sing N N 316 
PG4 C5  H51  sing N N 317 
PG4 C5  H52  sing N N 318 
PG4 C6  O4   sing N N 319 
PG4 C6  H61  sing N N 320 
PG4 C6  H62  sing N N 321 
PG4 O4  C7   sing N N 322 
PG4 C7  C8   sing N N 323 
PG4 C7  H71  sing N N 324 
PG4 C7  H72  sing N N 325 
PG4 C8  O5   sing N N 326 
PG4 C8  H81  sing N N 327 
PG4 C8  H82  sing N N 328 
PG4 O5  HO5  sing N N 329 
PHE N   CA   sing N N 330 
PHE N   H    sing N N 331 
PHE N   H2   sing N N 332 
PHE CA  C    sing N N 333 
PHE CA  CB   sing N N 334 
PHE CA  HA   sing N N 335 
PHE C   O    doub N N 336 
PHE C   OXT  sing N N 337 
PHE CB  CG   sing N N 338 
PHE CB  HB2  sing N N 339 
PHE CB  HB3  sing N N 340 
PHE CG  CD1  doub Y N 341 
PHE CG  CD2  sing Y N 342 
PHE CD1 CE1  sing Y N 343 
PHE CD1 HD1  sing N N 344 
PHE CD2 CE2  doub Y N 345 
PHE CD2 HD2  sing N N 346 
PHE CE1 CZ   doub Y N 347 
PHE CE1 HE1  sing N N 348 
PHE CE2 CZ   sing Y N 349 
PHE CE2 HE2  sing N N 350 
PHE CZ  HZ   sing N N 351 
PHE OXT HXT  sing N N 352 
PRO N   CA   sing N N 353 
PRO N   CD   sing N N 354 
PRO N   H    sing N N 355 
PRO CA  C    sing N N 356 
PRO CA  CB   sing N N 357 
PRO CA  HA   sing N N 358 
PRO C   O    doub N N 359 
PRO C   OXT  sing N N 360 
PRO CB  CG   sing N N 361 
PRO CB  HB2  sing N N 362 
PRO CB  HB3  sing N N 363 
PRO CG  CD   sing N N 364 
PRO CG  HG2  sing N N 365 
PRO CG  HG3  sing N N 366 
PRO CD  HD2  sing N N 367 
PRO CD  HD3  sing N N 368 
PRO OXT HXT  sing N N 369 
SER N   CA   sing N N 370 
SER N   H    sing N N 371 
SER N   H2   sing N N 372 
SER CA  C    sing N N 373 
SER CA  CB   sing N N 374 
SER CA  HA   sing N N 375 
SER C   O    doub N N 376 
SER C   OXT  sing N N 377 
SER CB  OG   sing N N 378 
SER CB  HB2  sing N N 379 
SER CB  HB3  sing N N 380 
SER OG  HG   sing N N 381 
SER OXT HXT  sing N N 382 
THR N   CA   sing N N 383 
THR N   H    sing N N 384 
THR N   H2   sing N N 385 
THR CA  C    sing N N 386 
THR CA  CB   sing N N 387 
THR CA  HA   sing N N 388 
THR C   O    doub N N 389 
THR C   OXT  sing N N 390 
THR CB  OG1  sing N N 391 
THR CB  CG2  sing N N 392 
THR CB  HB   sing N N 393 
THR OG1 HG1  sing N N 394 
THR CG2 HG21 sing N N 395 
THR CG2 HG22 sing N N 396 
THR CG2 HG23 sing N N 397 
THR OXT HXT  sing N N 398 
TRP N   CA   sing N N 399 
TRP N   H    sing N N 400 
TRP N   H2   sing N N 401 
TRP CA  C    sing N N 402 
TRP CA  CB   sing N N 403 
TRP CA  HA   sing N N 404 
TRP C   O    doub N N 405 
TRP C   OXT  sing N N 406 
TRP CB  CG   sing N N 407 
TRP CB  HB2  sing N N 408 
TRP CB  HB3  sing N N 409 
TRP CG  CD1  doub Y N 410 
TRP CG  CD2  sing Y N 411 
TRP CD1 NE1  sing Y N 412 
TRP CD1 HD1  sing N N 413 
TRP CD2 CE2  doub Y N 414 
TRP CD2 CE3  sing Y N 415 
TRP NE1 CE2  sing Y N 416 
TRP NE1 HE1  sing N N 417 
TRP CE2 CZ2  sing Y N 418 
TRP CE3 CZ3  doub Y N 419 
TRP CE3 HE3  sing N N 420 
TRP CZ2 CH2  doub Y N 421 
TRP CZ2 HZ2  sing N N 422 
TRP CZ3 CH2  sing Y N 423 
TRP CZ3 HZ3  sing N N 424 
TRP CH2 HH2  sing N N 425 
TRP OXT HXT  sing N N 426 
TYR N   CA   sing N N 427 
TYR N   H    sing N N 428 
TYR N   H2   sing N N 429 
TYR CA  C    sing N N 430 
TYR CA  CB   sing N N 431 
TYR CA  HA   sing N N 432 
TYR C   O    doub N N 433 
TYR C   OXT  sing N N 434 
TYR CB  CG   sing N N 435 
TYR CB  HB2  sing N N 436 
TYR CB  HB3  sing N N 437 
TYR CG  CD1  doub Y N 438 
TYR CG  CD2  sing Y N 439 
TYR CD1 CE1  sing Y N 440 
TYR CD1 HD1  sing N N 441 
TYR CD2 CE2  doub Y N 442 
TYR CD2 HD2  sing N N 443 
TYR CE1 CZ   doub Y N 444 
TYR CE1 HE1  sing N N 445 
TYR CE2 CZ   sing Y N 446 
TYR CE2 HE2  sing N N 447 
TYR CZ  OH   sing N N 448 
TYR OH  HH   sing N N 449 
TYR OXT HXT  sing N N 450 
VAL N   CA   sing N N 451 
VAL N   H    sing N N 452 
VAL N   H2   sing N N 453 
VAL CA  C    sing N N 454 
VAL CA  CB   sing N N 455 
VAL CA  HA   sing N N 456 
VAL C   O    doub N N 457 
VAL C   OXT  sing N N 458 
VAL CB  CG1  sing N N 459 
VAL CB  CG2  sing N N 460 
VAL CB  HB   sing N N 461 
VAL CG1 HG11 sing N N 462 
VAL CG1 HG12 sing N N 463 
VAL CG1 HG13 sing N N 464 
VAL CG2 HG21 sing N N 465 
VAL CG2 HG22 sing N N 466 
VAL CG2 HG23 sing N N 467 
VAL OXT HXT  sing N N 468 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R15GM146209 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7RSP 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9E4V 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008765 
_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]   0.008765 
_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]   0.006878 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL  ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H   ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
K   ? ? 16.37977 2.54835 ? ? 4.54127  84.28225 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ALA A 1 14  ? 18.43400  -47.79400 1.31700   1.000 125.22332 ?  291  ALA B N   1 
ATOM   2    C  CA  . ALA A 1 14  ? 19.40100  -48.07000 2.37400   1.000 119.25989 ?  291  ALA B CA  1 
ATOM   3    C  C   . ALA A 1 14  ? 20.37200  -46.90300 2.47700   1.000 116.24859 ?  291  ALA B C   1 
ATOM   4    O  O   . ALA A 1 14  ? 20.05000  -45.86700 3.05900   1.000 112.37001 ?  291  ALA B O   1 
ATOM   5    N  N   . THR A 1 15  ? 21.56300  -47.07500 1.89800   1.000 122.72585 ?  292  THR B N   1 
ATOM   6    C  CA  . THR A 1 15  ? 22.52900  -45.98300 1.86700   1.000 113.58545 ?  292  THR B CA  1 
ATOM   7    C  C   . THR A 1 15  ? 21.89200  -44.70700 1.33200   1.000 112.23250 ?  292  THR B C   1 
ATOM   8    O  O   . THR A 1 15  ? 22.14300  -43.61200 1.85300   1.000 114.02287 ?  292  THR B O   1 
ATOM   9    C  CB  . THR A 1 15  ? 23.74300  -46.37400 1.02400   1.000 103.79708 ?  292  THR B CB  1 
ATOM   10   N  N   . ARG A 1 16  ? 21.04600  -44.82600 0.30300   1.000 113.48568 ?  293  ARG B N   1 
ATOM   11   C  CA  . ARG A 1 16  ? 20.38900  -43.64000 -0.24400  1.000 104.89882 ?  293  ARG B CA  1 
ATOM   12   C  C   . ARG A 1 16  ? 19.43700  -43.01900 0.77200   1.000 109.77364 ?  293  ARG B C   1 
ATOM   13   O  O   . ARG A 1 16  ? 19.35800  -41.79100 0.89100   1.000 104.93301 ?  293  ARG B O   1 
ATOM   14   C  CB  . ARG A 1 16  ? 19.64200  -43.98600 -1.53200  1.000 108.21187 ?  293  ARG B CB  1 
ATOM   15   N  N   . ASP A 1 17  ? 18.70700  -43.85000 1.52000   1.000 116.81879 ?  294  ASP B N   1 
ATOM   16   C  CA  . ASP A 1 17  ? 17.79600  -43.31000 2.52400   1.000 109.67156 ?  294  ASP B CA  1 
ATOM   17   C  C   . ASP A 1 17  ? 18.56000  -42.59700 3.63900   1.000 109.65199 ?  294  ASP B C   1 
ATOM   18   O  O   . ASP A 1 17  ? 18.14500  -41.52300 4.09100   1.000 105.45777 ?  294  ASP B O   1 
ATOM   19   C  CB  . ASP A 1 17  ? 16.91400  -44.42700 3.08500   1.000 113.90682 ?  294  ASP B CB  1 
ATOM   20   C  CG  . ASP A 1 17  ? 16.23600  -45.24100 1.99300   1.000 118.12737 ?  294  ASP B CG  1 
ATOM   21   N  N   . GLN A 1 18  ? 19.68789  -43.16419 4.07880   1.000 113.26405 ?  295  GLN B N   1 
ATOM   22   C  CA  . GLN A 1 18  ? 20.46130  -42.54371 5.15263   1.000 110.72944 ?  295  GLN B CA  1 
ATOM   23   C  C   . GLN A 1 18  ? 21.01814  -41.18550 4.73844   1.000 106.09660 ?  295  GLN B C   1 
ATOM   24   O  O   . GLN A 1 18  ? 21.21681  -40.30903 5.58794   1.000 100.66576 ?  295  GLN B O   1 
ATOM   25   C  CB  . GLN A 1 18  ? 21.59301  -43.47824 5.58558   1.000 116.57910 ?  295  GLN B CB  1 
ATOM   26   C  CG  . GLN A 1 18  ? 22.37895  -43.00078 6.79920   1.000 121.79707 ?  295  GLN B CG  1 
ATOM   27   C  CD  . GLN A 1 18  ? 23.37921  -44.03453 7.28810   1.000 132.68215 ?  295  GLN B CD  1 
ATOM   28   O  OE1 . GLN A 1 18  ? 23.51390  -45.11150 6.70367   1.000 124.31153 ?  295  GLN B OE1 1 
ATOM   29   N  NE2 . GLN A 1 18  ? 24.08504  -43.71169 8.36722   1.000 134.53002 ?  295  GLN B NE2 1 
ATOM   30   N  N   . LEU A 1 19  ? 21.28300  -40.99600 3.44500   1.000 107.96372 ?  296  LEU B N   1 
ATOM   31   C  CA  . LEU A 1 19  ? 21.74800  -39.67600 2.94200   1.000 95.66462  ?  296  LEU B CA  1 
ATOM   32   C  C   . LEU A 1 19  ? 20.60500  -38.65900 3.00500   1.000 94.52390  ?  296  LEU B C   1 
ATOM   33   O  O   . LEU A 1 19  ? 20.84200  -37.54600 3.50900   1.000 95.32739  ?  296  LEU B O   1 
ATOM   34   C  CB  . LEU A 1 19  ? 22.24200  -39.84600 1.50200   1.000 96.55434  ?  296  LEU B CB  1 
ATOM   35   C  CG  . LEU A 1 19  ? 23.63600  -40.45200 1.35200   1.000 105.15523 ?  296  LEU B CG  1 
ATOM   36   C  CD1 . LEU A 1 19  ? 24.00700  -40.58900 -0.11600  1.000 99.28963  ?  296  LEU B CD1 1 
ATOM   37   C  CD2 . LEU A 1 19  ? 24.66800  -39.60400 2.07900   1.000 96.90204  ?  296  LEU B CD2 1 
ATOM   38   N  N   . ASN A 1 20  ? 19.41900  -39.02100 2.51300   1.000 95.13260  ?  297  ASN B N   1 
ATOM   39   C  CA  . ASN A 1 20  ? 18.32200  -38.06000 2.46500   1.000 98.10315  ?  297  ASN B CA  1 
ATOM   40   C  C   . ASN A 1 20  ? 18.01200  -37.52300 3.85500   1.000 92.33750  ?  297  ASN B C   1 
ATOM   41   O  O   . ASN A 1 20  ? 17.66100  -36.34800 4.00700   1.000 88.55823  ?  297  ASN B O   1 
ATOM   42   C  CB  . ASN A 1 20  ? 17.09100  -38.70400 1.83400   1.000 92.41125  ?  297  ASN B CB  1 
ATOM   43   C  CG  . ASN A 1 20  ? 17.34600  -39.15800 0.40600   1.000 105.75344 ?  297  ASN B CG  1 
ATOM   44   O  OD1 . ASN A 1 20  ? 17.25500  -40.35500 0.08800   1.000 107.18953 ?  297  ASN B OD1 1 
ATOM   45   N  ND2 . ASN A 1 20  ? 17.68300  -38.20400 -0.46300  1.000 99.36975  ?  297  ASN B ND2 1 
ATOM   46   N  N   . ILE A 1 21  ? 18.15600  -38.36500 4.88200   1.000 92.14380  ?  298  ILE B N   1 
ATOM   47   C  CA  . ILE A 1 21  ? 17.99200  -37.90100 6.25700   1.000 93.04072  ?  298  ILE B CA  1 
ATOM   48   C  C   . ILE A 1 21  ? 19.07500  -36.88500 6.61300   1.000 92.31415  ?  298  ILE B C   1 
ATOM   49   O  O   . ILE A 1 21  ? 18.79000  -35.81400 7.16400   1.000 87.72967  ?  298  ILE B O   1 
ATOM   50   C  CB  . ILE A 1 21  ? 18.00400  -39.08700 7.23500   1.000 94.37953  ?  298  ILE B CB  1 
ATOM   51   C  CG1 . ILE A 1 21  ? 17.02000  -40.17400 6.78800   1.000 91.34964  ?  298  ILE B CG1 1 
ATOM   52   C  CG2 . ILE A 1 21  ? 17.70000  -38.58100 8.64600   1.000 84.61695  ?  298  ILE B CG2 1 
ATOM   53   N  N   . ILE A 1 22  ? 20.33800  -37.21300 6.32700   1.000 90.69732  ?  299  ILE B N   1 
ATOM   54   C  CA  . ILE A 1 22  ? 21.41200  -36.25700 6.58500   1.000 86.51948  ?  299  ILE B CA  1 
ATOM   55   C  C   . ILE A 1 22  ? 21.13300  -34.95000 5.85500   1.000 88.18469  ?  299  ILE B C   1 
ATOM   56   O  O   . ILE A 1 22  ? 21.10100  -33.87200 6.46200   1.000 83.18738  ?  299  ILE B O   1 
ATOM   57   C  CB  . ILE A 1 22  ? 22.77900  -36.84000 6.18300   1.000 91.12093  ?  299  ILE B CB  1 
ATOM   58   C  CG1 . ILE A 1 22  ? 23.05300  -38.17500 6.90000   1.000 91.30152  ?  299  ILE B CG1 1 
ATOM   59   C  CG2 . ILE A 1 22  ? 23.87700  -35.81800 6.45700   1.000 81.43774  ?  299  ILE B CG2 1 
ATOM   60   N  N   . VAL A 1 23  ? 20.90200  -35.02800 4.54200   1.000 88.47753  ?  300  VAL B N   1 
ATOM   61   C  CA  . VAL A 1 23  ? 20.75700  -33.81400 3.74300   1.000 80.77455  ?  300  VAL B CA  1 
ATOM   62   C  C   . VAL A 1 23  ? 19.64800  -32.93100 4.29300   1.000 88.73133  ?  300  VAL B C   1 
ATOM   63   O  O   . VAL A 1 23  ? 19.75900  -31.69800 4.30400   1.000 86.43431  ?  300  VAL B O   1 
ATOM   64   C  CB  . VAL A 1 23  ? 20.50600  -34.16300 2.26700   1.000 86.72100  ?  300  VAL B CB  1 
ATOM   65   C  CG1 . VAL A 1 23  ? 20.00400  -32.93900 1.52800   1.000 93.14022  ?  300  VAL B CG1 1 
ATOM   66   C  CG2 . VAL A 1 23  ? 21.78200  -34.67300 1.62500   1.000 87.56952  ?  300  VAL B CG2 1 
ATOM   67   N  N   . SER A 1 24  ? 18.56600  -33.53900 4.76600   1.000 87.58010  ?  301  SER B N   1 
ATOM   68   C  CA  . SER A 1 24  ? 17.42600  -32.75000 5.20500   1.000 92.94405  ?  301  SER B CA  1 
ATOM   69   C  C   . SER A 1 24  ? 17.57500  -32.19500 6.61900   1.000 87.70747  ?  301  SER B C   1 
ATOM   70   O  O   . SER A 1 24  ? 16.65500  -31.52300 7.08400   1.000 93.55432  ?  301  SER B O   1 
ATOM   71   C  CB  . SER A 1 24  ? 16.14500  -33.57900 5.10600   1.000 92.89247  ?  301  SER B CB  1 
ATOM   72   O  OG  . SER A 1 24  ? 16.21700  -34.72000 5.93500   1.000 92.79154  ?  301  SER B OG  1 
ATOM   73   N  N   . TYR A 1 25  ? 18.69900  -32.44500 7.30500   1.000 83.51542  ?  302  TYR B N   1 
ATOM   74   C  CA  . TYR A 1 25  ? 18.94500  -31.92300 8.65100   1.000 82.12680  ?  302  TYR B CA  1 
ATOM   75   C  C   . TYR A 1 25  ? 18.79400  -30.40500 8.69900   1.000 83.74121  ?  302  TYR B C   1 
ATOM   76   O  O   . TYR A 1 25  ? 19.04700  -29.71800 7.69900   1.000 81.22263  ?  302  TYR B O   1 
ATOM   77   C  CB  . TYR A 1 25  ? 20.35100  -32.27600 9.13800   1.000 80.31242  ?  302  TYR B CB  1 
ATOM   78   C  CG  . TYR A 1 25  ? 20.52600  -33.66000 9.71200   1.000 83.90039  ?  302  TYR B CG  1 
ATOM   79   C  CD1 . TYR A 1 25  ? 19.43900  -34.41400 10.12500  1.000 85.77647  ?  302  TYR B CD1 1 
ATOM   80   C  CD2 . TYR A 1 25  ? 21.79500  -34.20800 9.85900   1.000 84.11275  ?  302  TYR B CD2 1 
ATOM   81   C  CE1 . TYR A 1 25  ? 19.61500  -35.68100 10.65600  1.000 85.57987  ?  302  TYR B CE1 1 
ATOM   82   C  CE2 . TYR A 1 25  ? 21.97600  -35.46400 10.38400  1.000 84.22726  ?  302  TYR B CE2 1 
ATOM   83   C  CZ  . TYR A 1 25  ? 20.88700  -36.19400 10.78100  1.000 86.04044  ?  302  TYR B CZ  1 
ATOM   84   O  OH  . TYR A 1 25  ? 21.09100  -37.44500 11.30300  1.000 90.06291  ?  302  TYR B OH  1 
ATOM   85   N  N   . PRO A 1 26  ? 18.39900  -29.84500 9.84900   1.000 79.27084  ?  303  PRO B N   1 
ATOM   86   C  CA  . PRO A 1 26  ? 18.47100  -28.40000 10.01200  1.000 78.22427  ?  303  PRO B CA  1 
ATOM   87   C  C   . PRO A 1 26  ? 19.92000  -27.93200 9.97800   1.000 77.10959  ?  303  PRO B C   1 
ATOM   88   O  O   . PRO A 1 26  ? 20.83100  -28.67300 10.37600  1.000 78.90538  ?  303  PRO B O   1 
ATOM   89   C  CB  . PRO A 1 26  ? 17.83900  -28.16400 11.39500  1.000 71.21677  ?  303  PRO B CB  1 
ATOM   90   C  CG  . PRO A 1 26  ? 18.08700  -29.43300 12.12200  1.000 72.84602  ?  303  PRO B CG  1 
ATOM   91   C  CD  . PRO A 1 26  ? 17.93200  -30.50800 11.07900  1.000 79.98322  ?  303  PRO B CD  1 
ATOM   92   N  N   . PRO A 1 27  ? 20.15900  -26.68900 9.55900   1.000 75.03472  ?  304  PRO B N   1 
ATOM   93   C  CA  . PRO A 1 27  ? 21.53800  -26.28100 9.21900   1.000 72.81928  ?  304  PRO B CA  1 
ATOM   94   C  C   . PRO A 1 27  ? 22.49600  -26.29900 10.39800  1.000 71.45550  ?  304  PRO B C   1 
ATOM   95   O  O   . PRO A 1 27  ? 23.71500  -26.30900 10.19200  1.000 77.25127  ?  304  PRO B O   1 
ATOM   96   C  CB  . PRO A 1 27  ? 21.35200  -24.86300 8.66700   1.000 65.74937  ?  304  PRO B CB  1 
ATOM   97   C  CG  . PRO A 1 27  ? 20.11100  -24.35400 9.34900   1.000 66.47910  ?  304  PRO B CG  1 
ATOM   98   C  CD  . PRO A 1 27  ? 19.22300  -25.55100 9.60900   1.000 69.89117  ?  304  PRO B CD  1 
ATOM   99   N  N   . THR A 1 28  ? 21.98700  -26.33400 11.62100  1.000 72.99515  ?  305  THR B N   1 
ATOM   100  C  CA  . THR A 1 28  ? 22.80500  -26.23300 12.81500  1.000 74.49158  ?  305  THR B CA  1 
ATOM   101  C  C   . THR A 1 28  ? 23.07800  -27.58000 13.46800  1.000 75.90070  ?  305  THR B C   1 
ATOM   102  O  O   . THR A 1 28  ? 23.90600  -27.65200 14.38400  1.000 78.02280  ?  305  THR B O   1 
ATOM   103  C  CB  . THR A 1 28  ? 22.11800  -25.30100 13.82000  1.000 69.45714  ?  305  THR B CB  1 
ATOM   104  N  N   . LYS A 1 29  ? 22.40900  -28.64300 13.03400  1.000 74.76309  ?  306  LYS B N   1 
ATOM   105  C  CA  . LYS A 1 29  ? 22.66800  -29.94900 13.62100  1.000 76.19540  ?  306  LYS B CA  1 
ATOM   106  C  C   . LYS A 1 29  ? 24.05700  -30.44000 13.21700  1.000 81.36290  ?  306  LYS B C   1 
ATOM   107  O  O   . LYS A 1 29  ? 24.50400  -30.24900 12.07800  1.000 79.99823  ?  306  LYS B O   1 
ATOM   108  C  CB  . LYS A 1 29  ? 21.59500  -30.95900 13.19900  1.000 77.71804  ?  306  LYS B CB  1 
ATOM   109  C  CG  . LYS A 1 29  ? 21.75000  -32.32900 13.86700  1.000 77.16855  ?  306  LYS B CG  1 
ATOM   110  C  CD  . LYS A 1 29  ? 20.57000  -33.24900 13.59800  1.000 80.27712  ?  306  LYS B CD  1 
ATOM   111  C  CE  . LYS A 1 29  ? 20.56600  -34.44200 14.56400  1.000 85.09783  ?  306  LYS B CE  1 
ATOM   112  N  NZ  . LYS A 1 29  ? 21.78300  -35.29800 14.40000  1.000 101.25435 ?  306  LYS B NZ  1 
ATOM   113  N  N   . GLN A 1 30  ? 24.75000  -31.05200 14.17300  1.000 82.85213  ?  307  GLN B N   1 
ATOM   114  C  CA  . GLN A 1 30  ? 26.08600  -31.57700 13.94800  1.000 82.38429  ?  307  GLN B CA  1 
ATOM   115  C  C   . GLN A 1 30  ? 25.97400  -32.97100 13.35300  1.000 82.89909  ?  307  GLN B C   1 
ATOM   116  O  O   . GLN A 1 30  ? 25.27700  -33.83300 13.90100  1.000 87.56096  ?  307  GLN B O   1 
ATOM   117  C  CB  . GLN A 1 30  ? 26.88300  -31.61400 15.25500  1.000 81.96467  ?  307  GLN B CB  1 
ATOM   118  C  CG  . GLN A 1 30  ? 26.95400  -30.27100 16.00500  1.000 95.26422  ?  307  GLN B CG  1 
ATOM   119  C  CD  . GLN A 1 30  ? 25.79800  -30.05500 16.99800  1.000 106.59745 ?  307  GLN B CD  1 
ATOM   120  O  OE1 . GLN A 1 30  ? 25.18500  -31.01300 17.47800  1.000 104.55836 ?  307  GLN B OE1 1 
ATOM   121  N  NE2 . GLN A 1 30  ? 25.50200  -28.78600 17.30700  1.000 100.81631 ?  307  GLN B NE2 1 
ATOM   122  N  N   . LEU A 1 31  ? 26.64600  -33.18800 12.22900  1.000 82.15486  ?  308  LEU B N   1 
ATOM   123  C  CA  . LEU A 1 31  ? 26.75700  -34.52800 11.67900  1.000 82.78065  ?  308  LEU B CA  1 
ATOM   124  C  C   . LEU A 1 31  ? 27.81000  -35.30700 12.45300  1.000 81.22265  ?  308  LEU B C   1 
ATOM   125  O  O   . LEU A 1 31  ? 28.84000  -34.75800 12.85700  1.000 81.30222  ?  308  LEU B O   1 
ATOM   126  C  CB  . LEU A 1 31  ? 27.12900  -34.48000 10.19600  1.000 84.20419  ?  308  LEU B CB  1 
ATOM   127  C  CG  . LEU A 1 31  ? 26.50000  -33.39800 9.31600   1.000 86.73833  ?  308  LEU B CG  1 
ATOM   128  C  CD1 . LEU A 1 31  ? 26.82800  -33.68500 7.86000   1.000 84.12437  ?  308  LEU B CD1 1 
ATOM   129  C  CD2 . LEU A 1 31  ? 25.00100  -33.29800 9.52500   1.000 82.19646  ?  308  LEU B CD2 1 
ATOM   130  N  N   . THR A 1 32  ? 27.54000  -36.58800 12.67700  1.000 80.99335  ?  309  THR B N   1 
ATOM   131  C  CA  . THR A 1 32  ? 28.52500  -37.44600 13.30900  1.000 86.53110  ?  309  THR B CA  1 
ATOM   132  C  C   . THR A 1 32  ? 29.70900  -37.68300 12.36800  1.000 86.82387  ?  309  THR B C   1 
ATOM   133  O  O   . THR A 1 32  ? 29.67300  -37.35300 11.17700  1.000 82.56272  ?  309  THR B O   1 
ATOM   134  C  CB  . THR A 1 32  ? 27.90100  -38.78400 13.68900  1.000 81.24457  ?  309  THR B CB  1 
ATOM   135  N  N   . TYR A 1 33  ? 30.77600  -38.26400 12.92200  1.000 84.68021  ?  310  TYR B N   1 
ATOM   136  C  CA  . TYR A 1 33  ? 31.88900  -38.70500 12.08800  1.000 83.58025  ?  310  TYR B CA  1 
ATOM   137  C  C   . TYR A 1 33  ? 31.40000  -39.65300 11.00900  1.000 84.49751  ?  310  TYR B C   1 
ATOM   138  O  O   . TYR A 1 33  ? 31.68400  -39.46000 9.82200   1.000 86.41378  ?  310  TYR B O   1 
ATOM   139  C  CB  . TYR A 1 33  ? 32.96000  -39.37500 12.94300  1.000 86.33708  ?  310  TYR B CB  1 
ATOM   140  C  CG  . TYR A 1 33  ? 33.67300  -38.41300 13.84900  1.000 85.67285  ?  310  TYR B CG  1 
ATOM   141  C  CD1 . TYR A 1 33  ? 33.94200  -37.10500 13.43600  1.000 83.18154  ?  310  TYR B CD1 1 
ATOM   142  C  CD2 . TYR A 1 33  ? 34.06200  -38.79700 15.12500  1.000 87.88539  ?  310  TYR B CD2 1 
ATOM   143  C  CE1 . TYR A 1 33  ? 34.59400  -36.21300 14.27500  1.000 86.24734  ?  310  TYR B CE1 1 
ATOM   144  C  CE2 . TYR A 1 33  ? 34.70500  -37.92000 15.96700  1.000 87.47198  ?  310  TYR B CE2 1 
ATOM   145  C  CZ  . TYR A 1 33  ? 34.97500  -36.63500 15.54500  1.000 86.34818  ?  310  TYR B CZ  1 
ATOM   146  O  OH  . TYR A 1 33  ? 35.61900  -35.78000 16.41500  1.000 95.50598  ?  310  TYR B OH  1 
ATOM   147  N  N   . GLU A 1 34  ? 30.62200  -40.65400 11.42000  1.000 86.44842  ?  311  GLU B N   1 
ATOM   148  C  CA  . GLU A 1 34  ? 30.05000  -41.61200 10.43900  1.000 88.22508  ?  311  GLU B CA  1 
ATOM   149  C  C   . GLU A 1 34  ? 29.27200  -40.83300 9.37500   1.000 87.47951  ?  311  GLU B C   1 
ATOM   150  O  O   . GLU A 1 34  ? 29.40500  -41.17500 8.18600   1.000 86.09981  ?  311  GLU B O   1 
ATOM   151  C  CB  . GLU A 1 34  ? 29.14500  -42.61900 11.14800  1.000 98.10322  ?  311  GLU B CB  1 
ATOM   152  C  CG  . GLU A 1 34  ? 29.85700  -43.40400 12.23300  1.000 108.93560 ?  311  GLU B CG  1 
ATOM   153  C  CD  . GLU A 1 34  ? 28.98000  -44.40600 12.96500  1.000 127.57190 ?  311  GLU B CD  1 
ATOM   154  O  OE1 . GLU A 1 34  ? 27.78400  -44.49900 12.62800  1.000 131.97888 ?  311  GLU B OE1 1 
ATOM   155  O  OE2 . GLU A 1 34  ? 29.49700  -45.09000 13.87100  1.000 126.21028 ?  311  GLU B OE2 1 
ATOM   156  N  N   . GLU A 1 35  ? 28.49400  -39.82600 9.78700   1.000 87.03070  ?  312  GLU B N   1 
ATOM   157  C  CA  . GLU A 1 35  ? 27.67600  -39.10900 8.81600   1.000 86.54161  ?  312  GLU B CA  1 
ATOM   158  C  C   . GLU A 1 35  ? 28.54000  -38.30100 7.86200   1.000 79.96014  ?  312  GLU B C   1 
ATOM   159  O  O   . GLU A 1 35  ? 28.25000  -38.23800 6.66400   1.000 81.47922  ?  312  GLU B O   1 
ATOM   160  C  CB  . GLU A 1 35  ? 26.66300  -38.21900 9.53600   1.000 82.37803  ?  312  GLU B CB  1 
ATOM   161  C  CG  . GLU A 1 35  ? 25.73300  -39.00400 10.45000  1.000 89.30749  ?  312  GLU B CG  1 
ATOM   162  C  CD  . GLU A 1 35  ? 24.63400  -38.15500 11.04100  1.000 90.13789  ?  312  GLU B CD  1 
ATOM   163  O  OE1 . GLU A 1 35  ? 24.89100  -36.98400 11.38600  1.000 86.46870  ?  312  GLU B OE1 1 
ATOM   164  O  OE2 . GLU A 1 35  ? 23.50100  -38.66300 11.14500  1.000 95.26608  -1 312  GLU B OE2 1 
ATOM   165  N  N   . GLN A 1 36  ? 29.61000  -37.68800 8.37300   1.000 81.15302  ?  313  GLN B N   1 
ATOM   166  C  CA  . GLN A 1 36  ? 30.47500  -36.86800 7.52900   1.000 76.98080  ?  313  GLN B CA  1 
ATOM   167  C  C   . GLN A 1 36  ? 31.13800  -37.71300 6.45400   1.000 86.00750  ?  313  GLN B C   1 
ATOM   168  O  O   . GLN A 1 36  ? 31.15700  -37.34400 5.27600   1.000 86.75196  ?  313  GLN B O   1 
ATOM   169  C  CB  . GLN A 1 36  ? 31.53600  -36.16800 8.37700   1.000 78.35294  ?  313  GLN B CB  1 
ATOM   170  C  CG  . GLN A 1 36  ? 30.99200  -35.10400 9.31000   1.000 77.79697  ?  313  GLN B CG  1 
ATOM   171  C  CD  . GLN A 1 36  ? 32.04400  -34.60000 10.27400  1.000 82.46609  ?  313  GLN B CD  1 
ATOM   172  O  OE1 . GLN A 1 36  ? 33.17300  -34.30400 9.88200   1.000 87.22516  ?  313  GLN B OE1 1 
ATOM   173  N  NE2 . GLN A 1 36  ? 31.68000  -34.51100 11.55400  1.000 85.76065  ?  313  GLN B NE2 1 
ATOM   174  N  N   . ASP A 1 37  ? 31.69000  -38.86200 6.84400   1.000 82.09029  ?  314  ASP B N   1 
ATOM   175  C  CA  . ASP A 1 37  ? 32.38200  -39.69700 5.87700   1.000 87.17410  ?  314  ASP B CA  1 
ATOM   176  C  C   . ASP A 1 37  ? 31.40500  -40.32500 4.88500   1.000 88.58294  ?  314  ASP B C   1 
ATOM   177  O  O   . ASP A 1 37  ? 31.78400  -40.61500 3.74300   1.000 89.51458  ?  314  ASP B O   1 
ATOM   178  C  CB  . ASP A 1 37  ? 33.21000  -40.75200 6.61800   1.000 87.91618  ?  314  ASP B CB  1 
ATOM   179  C  CG  . ASP A 1 37  ? 34.21600  -40.13100 7.59500   1.000 87.49955  ?  314  ASP B CG  1 
ATOM   180  O  OD1 . ASP A 1 37  ? 34.98400  -39.23200 7.18000   1.000 87.36676  ?  314  ASP B OD1 1 
ATOM   181  O  OD2 . ASP A 1 37  ? 34.23100  -40.54300 8.78300   1.000 88.71241  -1 314  ASP B OD2 1 
ATOM   182  N  N   . LEU A 1 38  ? 30.14500  -40.51900 5.28800   1.000 85.11170  ?  315  LEU B N   1 
ATOM   183  C  CA  . LEU A 1 38  ? 29.13200  -40.97600 4.33900   1.000 89.03432  ?  315  LEU B CA  1 
ATOM   184  C  C   . LEU A 1 38  ? 28.81200  -39.89600 3.31200   1.000 89.99168  ?  315  LEU B C   1 
ATOM   185  O  O   . LEU A 1 38  ? 28.64800  -40.19100 2.12000   1.000 91.89667  ?  315  LEU B O   1 
ATOM   186  C  CB  . LEU A 1 38  ? 27.86400  -41.40500 5.07700   1.000 87.29288  ?  315  LEU B CB  1 
ATOM   187  C  CG  . LEU A 1 38  ? 26.67200  -41.78100 4.19300   1.000 88.02891  ?  315  LEU B CG  1 
ATOM   188  C  CD1 . LEU A 1 38  ? 26.99800  -42.98600 3.33700   1.000 95.55074  ?  315  LEU B CD1 1 
ATOM   189  C  CD2 . LEU A 1 38  ? 25.42000  -42.04200 5.02300   1.000 100.72310 ?  315  LEU B CD2 1 
ATOM   190  N  N   . VAL A 1 39  ? 28.72000  -38.63800 3.75400   1.000 88.51104  ?  316  VAL B N   1 
ATOM   191  C  CA  . VAL A 1 39  ? 28.51100  -37.53400 2.82000   1.000 86.27147  ?  316  VAL B CA  1 
ATOM   192  C  C   . VAL A 1 39  ? 29.70300  -37.39400 1.88000   1.000 85.90037  ?  316  VAL B C   1 
ATOM   193  O  O   . VAL A 1 39  ? 29.54000  -37.21000 0.66700   1.000 83.40642  ?  316  VAL B O   1 
ATOM   194  C  CB  . VAL A 1 39  ? 28.24400  -36.22600 3.58500   1.000 82.66647  ?  316  VAL B CB  1 
ATOM   195  C  CG1 . VAL A 1 39  ? 28.30700  -35.05100 2.63300   1.000 76.99104  ?  316  VAL B CG1 1 
ATOM   196  C  CG2 . VAL A 1 39  ? 26.89200  -36.28800 4.28300   1.000 84.28477  ?  316  VAL B CG2 1 
ATOM   197  N  N   . TRP A 1 40  ? 30.91900  -37.46400 2.42200   1.000 81.14376  ?  317  TRP B N   1 
ATOM   198  C  CA  . TRP A 1 40  ? 32.09700  -37.35500 1.57600   1.000 85.39326  ?  317  TRP B CA  1 
ATOM   199  C  C   . TRP A 1 40  ? 32.11500  -38.45200 0.51100   1.000 93.11113  ?  317  TRP B C   1 
ATOM   200  O  O   . TRP A 1 40  ? 32.28200  -38.16800 -0.68300  1.000 88.16424  ?  317  TRP B O   1 
ATOM   201  C  CB  . TRP A 1 40  ? 33.37200  -37.39400 2.41900   1.000 84.16689  ?  317  TRP B CB  1 
ATOM   202  C  CG  . TRP A 1 40  ? 34.57700  -37.39200 1.54900   1.000 88.32969  ?  317  TRP B CG  1 
ATOM   203  C  CD1 . TRP A 1 40  ? 35.29400  -38.48300 1.13600   1.000 86.13273  ?  317  TRP B CD1 1 
ATOM   204  C  CD2 . TRP A 1 40  ? 35.17600  -36.25400 0.91600   1.000 87.33347  ?  317  TRP B CD2 1 
ATOM   205  N  NE1 . TRP A 1 40  ? 36.31700  -38.08900 0.31400   1.000 86.84053  ?  317  TRP B NE1 1 
ATOM   206  C  CE2 . TRP A 1 40  ? 36.27100  -36.72800 0.16100   1.000 86.60587  ?  317  TRP B CE2 1 
ATOM   207  C  CE3 . TRP A 1 40  ? 34.90400  -34.88000 0.92800   1.000 82.55307  ?  317  TRP B CE3 1 
ATOM   208  C  CZ2 . TRP A 1 40  ? 37.09200  -35.87600 -0.58300  1.000 85.94692  ?  317  TRP B CZ2 1 
ATOM   209  C  CZ3 . TRP A 1 40  ? 35.71900  -34.04000 0.20400   1.000 82.64691  ?  317  TRP B CZ3 1 
ATOM   210  C  CH2 . TRP A 1 40  ? 36.80100  -34.53900 -0.54600  1.000 86.00921  ?  317  TRP B CH2 1 
ATOM   211  N  N   . LYS A 1 41  ? 31.93000  -39.71400 0.91800   1.000 88.10469  ?  318  LYS B N   1 
ATOM   212  C  CA  . LYS A 1 41  ? 31.99700  -40.80400 -0.05400  1.000 91.74257  ?  318  LYS B CA  1 
ATOM   213  C  C   . LYS A 1 41  ? 31.10200  -40.53300 -1.26100  1.000 91.67654  ?  318  LYS B C   1 
ATOM   214  O  O   . LYS A 1 41  ? 31.48600  -40.81000 -2.40100  1.000 99.60734  ?  318  LYS B O   1 
ATOM   215  C  CB  . LYS A 1 41  ? 31.63300  -42.14100 0.59800   1.000 93.19302  ?  318  LYS B CB  1 
ATOM   216  N  N   . PHE A 1 42  ? 29.92300  -39.95600 -1.04300  1.000 90.49206  ?  319  PHE B N   1 
ATOM   217  C  CA  . PHE A 1 42  ? 28.99300  -39.71700 -2.13900  1.000 93.85861  ?  319  PHE B CA  1 
ATOM   218  C  C   . PHE A 1 42  ? 29.03800  -38.28300 -2.64800  1.000 89.96542  ?  319  PHE B C   1 
ATOM   219  O  O   . PHE A 1 42  ? 28.07900  -37.83300 -3.28100  1.000 96.33476  ?  319  PHE B O   1 
ATOM   220  C  CB  . PHE A 1 42  ? 27.57500  -40.09900 -1.71900  1.000 96.20139  ?  319  PHE B CB  1 
ATOM   221  C  CG  . PHE A 1 42  ? 27.40600  -41.57300 -1.45800  1.000 100.82142 ?  319  PHE B CG  1 
ATOM   222  C  CD1 . PHE A 1 42  ? 27.18900  -42.45800 -2.50400  1.000 103.13720 ?  319  PHE B CD1 1 
ATOM   223  C  CD2 . PHE A 1 42  ? 27.48400  -42.07500 -0.16800  1.000 102.46344 ?  319  PHE B CD2 1 
ATOM   224  C  CE1 . PHE A 1 42  ? 27.04500  -43.82400 -2.26700  1.000 101.12750 ?  319  PHE B CE1 1 
ATOM   225  C  CE2 . PHE A 1 42  ? 27.33600  -43.43300 0.07600   1.000 107.94327 ?  319  PHE B CE2 1 
ATOM   226  C  CZ  . PHE A 1 42  ? 27.11900  -44.31000 -0.97900  1.000 104.98578 ?  319  PHE B CZ  1 
ATOM   227  N  N   . ARG A 1 43  ? 30.14600  -37.56700 -2.44800  1.000 89.55377  ?  320  ARG B N   1 
ATOM   228  C  CA  . ARG A 1 43  ? 30.15000  -36.15800 -2.83000  1.000 90.11651  ?  320  ARG B CA  1 
ATOM   229  C  C   . ARG A 1 43  ? 29.74800  -35.97300 -4.28800  1.000 88.71510  ?  320  ARG B C   1 
ATOM   230  O  O   . ARG A 1 43  ? 28.96000  -35.07800 -4.61400  1.000 84.48829  ?  320  ARG B O   1 
ATOM   231  C  CB  . ARG A 1 43  ? 31.51200  -35.52800 -2.54700  1.000 83.80066  ?  320  ARG B CB  1 
ATOM   232  C  CG  . ARG A 1 43  ? 32.68600  -36.13700 -3.24400  1.000 82.81632  ?  320  ARG B CG  1 
ATOM   233  C  CD  . ARG A 1 43  ? 33.93200  -35.78100 -2.45200  1.000 84.40735  ?  320  ARG B CD  1 
ATOM   234  N  NE  . ARG A 1 43  ? 35.15800  -36.35800 -2.99200  1.000 88.47046  ?  320  ARG B NE  1 
ATOM   235  C  CZ  . ARG A 1 43  ? 35.41800  -37.65700 -3.05600  1.000 87.47650  ?  320  ARG B CZ  1 
ATOM   236  N  NH1 . ARG A 1 43  ? 34.52500  -38.56100 -2.69500  1.000 88.29905  ?  320  ARG B NH1 1 
ATOM   237  N  NH2 . ARG A 1 43  ? 36.60300  -38.05700 -3.50400  1.000 90.12732  ?  320  ARG B NH2 1 
ATOM   238  N  N   . TYR A 1 44  ? 30.24100  -36.83500 -5.17800  1.000 89.33198  ?  321  TYR B N   1 
ATOM   239  C  CA  . TYR A 1 44  ? 29.91500  -36.66600 -6.59200  1.000 94.54496  ?  321  TYR B CA  1 
ATOM   240  C  C   . TYR A 1 44  ? 28.47700  -37.06900 -6.91300  1.000 92.22799  ?  321  TYR B C   1 
ATOM   241  O  O   . TYR A 1 44  ? 27.89900  -36.56200 -7.88100  1.000 96.76137  ?  321  TYR B O   1 
ATOM   242  C  CB  . TYR A 1 44  ? 30.90900  -37.45300 -7.45400  1.000 94.25223  ?  321  TYR B CB  1 
ATOM   243  C  CG  . TYR A 1 44  ? 32.30200  -36.85800 -7.41300  1.000 91.65544  ?  321  TYR B CG  1 
ATOM   244  C  CD1 . TYR A 1 44  ? 32.61400  -35.73500 -8.16800  1.000 95.31241  ?  321  TYR B CD1 1 
ATOM   245  C  CD2 . TYR A 1 44  ? 33.29100  -37.39700 -6.59800  1.000 89.14604  ?  321  TYR B CD2 1 
ATOM   246  C  CE1 . TYR A 1 44  ? 33.88000  -35.17300 -8.13300  1.000 96.59665  ?  321  TYR B CE1 1 
ATOM   247  C  CE2 . TYR A 1 44  ? 34.56000  -36.84000 -6.54800  1.000 88.85388  ?  321  TYR B CE2 1 
ATOM   248  C  CZ  . TYR A 1 44  ? 34.84800  -35.72500 -7.31900  1.000 94.43328  ?  321  TYR B CZ  1 
ATOM   249  O  OH  . TYR A 1 44  ? 36.10500  -35.15500 -7.28500  1.000 96.46446  ?  321  TYR B OH  1 
ATOM   250  N  N   . TYR A 1 45  ? 27.87900  -37.95000 -6.11500  1.000 91.56964  ?  322  TYR B N   1 
ATOM   251  C  CA  . TYR A 1 45  ? 26.49000  -38.34300 -6.31100  1.000 92.96589  ?  322  TYR B CA  1 
ATOM   252  C  C   . TYR A 1 45  ? 25.50100  -37.31400 -5.76200  1.000 96.95193  ?  322  TYR B C   1 
ATOM   253  O  O   . TYR A 1 45  ? 24.29400  -37.57600 -5.77000  1.000 105.38416 ?  322  TYR B O   1 
ATOM   254  C  CB  . TYR A 1 45  ? 26.23000  -39.71200 -5.66700  1.000 96.06689  ?  322  TYR B CB  1 
ATOM   255  N  N   . LEU A 1 46  ? 25.96600  -36.15300 -5.29800  1.000 93.20434  ?  323  LEU B N   1 
ATOM   256  C  CA  . LEU A 1 46  ? 25.08500  -35.18200 -4.66600  1.000 89.95845  ?  323  LEU B CA  1 
ATOM   257  C  C   . LEU A 1 46  ? 25.13300  -33.79400 -5.29300  1.000 90.83533  ?  323  LEU B C   1 
ATOM   258  O  O   . LEU A 1 46  ? 24.47200  -32.88400 -4.77500  1.000 90.35271  ?  323  LEU B O   1 
ATOM   259  C  CB  . LEU A 1 46  ? 25.42200  -35.06300 -3.17100  1.000 87.00184  ?  323  LEU B CB  1 
ATOM   260  C  CG  . LEU A 1 46  ? 25.18900  -36.31400 -2.32200  1.000 87.92771  ?  323  LEU B CG  1 
ATOM   261  C  CD1 . LEU A 1 46  ? 25.98800  -36.24400 -1.03900  1.000 85.42746  ?  323  LEU B CD1 1 
ATOM   262  C  CD2 . LEU A 1 46  ? 23.71200  -36.47400 -2.01200  1.000 93.58583  ?  323  LEU B CD2 1 
ATOM   263  N  N   . THR A 1 47  ? 25.86300  -33.60500 -6.39800  1.000 91.80241  ?  324  THR B N   1 
ATOM   264  C  CA  . THR A 1 47  ? 26.13700  -32.25500 -6.88100  1.000 85.16685  ?  324  THR B CA  1 
ATOM   265  C  C   . THR A 1 47  ? 24.91600  -31.57700 -7.48100  1.000 90.18111  ?  324  THR B C   1 
ATOM   266  O  O   . THR A 1 47  ? 24.93500  -30.35000 -7.65000  1.000 92.17403  ?  324  THR B O   1 
ATOM   267  C  CB  . THR A 1 47  ? 27.26400  -32.26500 -7.91100  1.000 85.97671  ?  324  THR B CB  1 
ATOM   268  O  OG1 . THR A 1 47  ? 26.97200  -33.23500 -8.92200  1.000 96.44104  ?  324  THR B OG1 1 
ATOM   269  C  CG2 . THR A 1 47  ? 28.58900  -32.59400 -7.24700  1.000 85.16969  ?  324  THR B CG2 1 
ATOM   270  N  N   . ASN A 1 48  ? 23.85700  -32.32000 -7.80400  1.000 89.48041  ?  325  ASN B N   1 
ATOM   271  C  CA  . ASN A 1 48  ? 22.63600  -31.69500 -8.29900  1.000 99.91377  ?  325  ASN B CA  1 
ATOM   272  C  C   . ASN A 1 48  ? 21.55100  -31.57500 -7.22600  1.000 99.36099  ?  325  ASN B C   1 
ATOM   273  O  O   . ASN A 1 48  ? 20.36800  -31.43600 -7.56300  1.000 100.11514 ?  325  ASN B O   1 
ATOM   274  C  CB  . ASN A 1 48  ? 22.09500  -32.45400 -9.50500  1.000 110.38769 ?  325  ASN B CB  1 
ATOM   275  C  CG  . ASN A 1 48  ? 21.28300  -33.66300 -9.10800  1.000 120.40016 ?  325  ASN B CG  1 
ATOM   276  O  OD1 . ASN A 1 48  ? 21.75900  -34.54400 -8.37800  1.000 118.94835 ?  325  ASN B OD1 1 
ATOM   277  N  ND2 . ASN A 1 48  ? 20.03500  -33.70700 -9.56900  1.000 128.97688 ?  325  ASN B ND2 1 
ATOM   278  N  N   . GLN A 1 49  ? 21.92700  -31.62400 -5.94700  1.000 95.29392  ?  326  GLN B N   1 
ATOM   279  C  CA  . GLN A 1 49  ? 21.01900  -31.35900 -4.83100  1.000 95.07697  ?  326  GLN B CA  1 
ATOM   280  C  C   . GLN A 1 49  ? 21.54500  -30.13500 -4.09200  1.000 85.36929  ?  326  GLN B C   1 
ATOM   281  O  O   . GLN A 1 49  ? 22.45900  -30.24200 -3.26800  1.000 81.73848  ?  326  GLN B O   1 
ATOM   282  C  CB  . GLN A 1 49  ? 20.91000  -32.55600 -3.89400  1.000 93.09488  ?  326  GLN B CB  1 
ATOM   283  C  CG  . GLN A 1 49  ? 20.35200  -33.80800 -4.52200  1.000 93.77768  ?  326  GLN B CG  1 
ATOM   284  C  CD  . GLN A 1 49  ? 20.32100  -34.96400 -3.53900  1.000 101.76817 ?  326  GLN B CD  1 
ATOM   285  O  OE1 . GLN A 1 49  ? 20.88100  -36.02900 -3.79500  1.000 104.28474 ?  326  GLN B OE1 1 
ATOM   286  N  NE2 . GLN A 1 49  ? 19.67000  -34.75300 -2.39700  1.000 104.37502 ?  326  GLN B NE2 1 
ATOM   287  N  N   . GLU A 1 50  ? 20.96000  -28.97000 -4.37200  1.000 87.79264  ?  327  GLU B N   1 
ATOM   288  C  CA  . GLU A 1 50  ? 21.44700  -27.71200 -3.74300  1.000 89.27049  ?  327  GLU B CA  1 
ATOM   289  C  C   . GLU A 1 50  ? 21.38300  -27.82600 -2.21500  1.000 84.57346  ?  327  GLU B C   1 
ATOM   290  O  O   . GLU A 1 50  ? 22.25100  -27.22800 -1.55200  1.000 82.19611  ?  327  GLU B O   1 
ATOM   291  C  CB  . GLU A 1 50  ? 20.63200  -26.52300 -4.25600  1.000 94.76224  ?  327  GLU B CB  1 
ATOM   292  C  CG  . GLU A 1 50  ? 19.13300  -26.71800 -4.13200  1.000 99.62448  ?  327  GLU B CG  1 
ATOM   293  C  CD  . GLU A 1 50  ? 18.30500  -25.66400 -4.84700  1.000 115.88435 ?  327  GLU B CD  1 
ATOM   294  O  OE1 . GLU A 1 50  ? 18.90600  -24.76800 -5.47200  1.000 121.70200 ?  327  GLU B OE1 1 
ATOM   295  O  OE2 . GLU A 1 50  ? 17.06300  -25.74200 -4.77600  1.000 119.59435 -1 327  GLU B OE2 1 
ATOM   296  N  N   . LYS A 1 51  ? 20.40700  -28.56600 -1.67900  1.000 81.56294  ?  328  LYS B N   1 
ATOM   297  C  CA  . LYS A 1 51  ? 20.24300  -28.65600 -0.23100  1.000 81.18759  ?  328  LYS B CA  1 
ATOM   298  C  C   . LYS A 1 51  ? 21.31800  -29.50800 0.43600   1.000 81.33045  ?  328  LYS B C   1 
ATOM   299  O  O   . LYS A 1 51  ? 21.40200  -29.51800 1.66800   1.000 78.80008  ?  328  LYS B O   1 
ATOM   300  C  CB  . LYS A 1 51  ? 18.85600  -29.21000 0.10800   1.000 78.24698  ?  328  LYS B CB  1 
ATOM   301  N  N   . ALA A 1 52  ? 22.14400  -30.21000 -0.34300  1.000 83.69258  ?  329  ALA B N   1 
ATOM   302  C  CA  . ALA A 1 52  ? 23.22400  -31.02400 0.19500   1.000 75.18643  ?  329  ALA B CA  1 
ATOM   303  C  C   . ALA A 1 52  ? 24.57000  -30.31300 0.20400   1.000 71.81919  ?  329  ALA B C   1 
ATOM   304  O  O   . ALA A 1 52  ? 25.50200  -30.80100 0.84800   1.000 70.63313  ?  329  ALA B O   1 
ATOM   305  C  CB  . ALA A 1 52  ? 23.34600  -32.32900 -0.60000  1.000 77.46856  ?  329  ALA B CB  1 
ATOM   306  N  N   . LEU A 1 53  ? 24.69200  -29.17100 -0.47500  1.000 72.46305  ?  330  LEU B N   1 
ATOM   307  C  CA  . LEU A 1 53  ? 25.98200  -28.49200 -0.56700  1.000 67.77650  ?  330  LEU B CA  1 
ATOM   308  C  C   . LEU A 1 53  ? 26.50400  -28.04200 0.80400   1.000 65.43746  ?  330  LEU B C   1 
ATOM   309  O  O   . LEU A 1 53  ? 27.69700  -28.19300 1.09000   1.000 68.14355  ?  330  LEU B O   1 
ATOM   310  C  CB  . LEU A 1 53  ? 25.86700  -27.31300 -1.52800  1.000 64.65517  ?  330  LEU B CB  1 
ATOM   311  C  CG  . LEU A 1 53  ? 27.07600  -26.40200 -1.70300  1.000 64.33519  ?  330  LEU B CG  1 
ATOM   312  C  CD1 . LEU A 1 53  ? 28.29400  -27.20000 -2.16900  1.000 65.03221  ?  330  LEU B CD1 1 
ATOM   313  C  CD2 . LEU A 1 53  ? 26.71500  -25.27600 -2.68400  1.000 65.56829  ?  330  LEU B CD2 1 
ATOM   314  N  N   . THR A 1 54  ? 25.64400  -27.48500 1.66900   1.000 62.63470  ?  331  THR B N   1 
ATOM   315  C  CA  . THR A 1 54  ? 26.14300  -27.07500 2.98700   1.000 65.50169  ?  331  THR B CA  1 
ATOM   316  C  C   . THR A 1 54  ? 26.58800  -28.28500 3.80700   1.000 69.95059  ?  331  THR B C   1 
ATOM   317  O  O   . THR A 1 54  ? 27.56300  -28.20300 4.57000   1.000 64.55823  ?  331  THR B O   1 
ATOM   318  C  CB  . THR A 1 54  ? 25.09800  -26.26200 3.77800   1.000 66.69757  ?  331  THR B CB  1 
ATOM   319  O  OG1 . THR A 1 54  ? 23.91400  -27.04100 3.99600   1.000 68.30778  ?  331  THR B OG1 1 
ATOM   320  C  CG2 . THR A 1 54  ? 24.73700  -24.95800 3.06800   1.000 64.45619  ?  331  THR B CG2 1 
ATOM   321  N  N   . LYS A 1 55  ? 25.88200  -29.41600 3.67300   1.000 67.92761  ?  332  LYS B N   1 
ATOM   322  C  CA  . LYS A 1 55  ? 26.29800  -30.63000 4.37100   1.000 65.82336  ?  332  LYS B CA  1 
ATOM   323  C  C   . LYS A 1 55  ? 27.66300  -31.10100 3.88800   1.000 71.05987  ?  332  LYS B C   1 
ATOM   324  O  O   . LYS A 1 55  ? 28.49600  -31.54600 4.68900   1.000 71.41993  ?  332  LYS B O   1 
ATOM   325  C  CB  . LYS A 1 55  ? 25.25400  -31.73500 4.19500   1.000 69.80276  ?  332  LYS B CB  1 
ATOM   326  C  CG  . LYS A 1 55  ? 24.20000  -31.77000 5.28500   1.000 74.73733  ?  332  LYS B CG  1 
ATOM   327  C  CD  . LYS A 1 55  ? 23.33000  -30.51500 5.25700   1.000 73.80468  ?  332  LYS B CD  1 
ATOM   328  C  CE  . LYS A 1 55  ? 22.13900  -30.63800 6.18500   1.000 72.23160  ?  332  LYS B CE  1 
ATOM   329  N  NZ  . LYS A 1 55  ? 21.15500  -29.55600 5.91600   1.000 83.48818  ?  332  LYS B NZ  1 
ATOM   330  N  N   . PHE A 1 56  ? 27.91500  -31.00500 2.58100   1.000 67.40333  ?  333  PHE B N   1 
ATOM   331  C  CA  . PHE A 1 56  ? 29.21700  -31.39400 2.05700   1.000 69.97857  ?  333  PHE B CA  1 
ATOM   332  C  C   . PHE A 1 56  ? 30.30900  -30.48200 2.59900   1.000 69.40394  ?  333  PHE B C   1 
ATOM   333  O  O   . PHE A 1 56  ? 31.32100  -30.95600 3.13800   1.000 69.37904  ?  333  PHE B O   1 
ATOM   334  C  CB  . PHE A 1 56  ? 29.20100  -31.37800 0.52500   1.000 73.14039  ?  333  PHE B CB  1 
ATOM   335  C  CG  . PHE A 1 56  ? 30.57100  -31.46700 -0.09700  1.000 71.32427  ?  333  PHE B CG  1 
ATOM   336  C  CD1 . PHE A 1 56  ? 31.34300  -32.62000 0.04500   1.000 75.20211  ?  333  PHE B CD1 1 
ATOM   337  C  CD2 . PHE A 1 56  ? 31.09000  -30.40400 -0.82000  1.000 67.54372  ?  333  PHE B CD2 1 
ATOM   338  C  CE1 . PHE A 1 56  ? 32.61200  -32.70200 -0.51800  1.000 72.65666  ?  333  PHE B CE1 1 
ATOM   339  C  CE2 . PHE A 1 56  ? 32.34900  -30.47500 -1.38000  1.000 69.04439  ?  333  PHE B CE2 1 
ATOM   340  C  CZ  . PHE A 1 56  ? 33.11200  -31.62900 -1.22600  1.000 76.86860  ?  333  PHE B CZ  1 
ATOM   341  N  N   . LEU A 1 57  ? 30.11300  -29.16600 2.47300   1.000 62.51725  ?  334  LEU B N   1 
ATOM   342  C  CA  . LEU A 1 57  ? 31.10600  -28.21000 2.95300   1.000 65.52552  ?  334  LEU B CA  1 
ATOM   343  C  C   . LEU A 1 57  ? 31.43700  -28.41800 4.42800   1.000 67.35619  ?  334  LEU B C   1 
ATOM   344  O  O   . LEU A 1 57  ? 32.57100  -28.16900 4.84700   1.000 65.82910  ?  334  LEU B O   1 
ATOM   345  C  CB  . LEU A 1 57  ? 30.60900  -26.78300 2.70900   1.000 59.26851  ?  334  LEU B CB  1 
ATOM   346  C  CG  . LEU A 1 57  ? 30.34800  -26.39200 1.25300   1.000 64.02163  ?  334  LEU B CG  1 
ATOM   347  C  CD1 . LEU A 1 57  ? 29.81900  -24.99300 1.17300   1.000 58.28775  ?  334  LEU B CD1 1 
ATOM   348  C  CD2 . LEU A 1 57  ? 31.62100  -26.53600 0.41200   1.000 60.99724  ?  334  LEU B CD2 1 
ATOM   349  N  N   . LYS A 1 58  ? 30.45500  -28.86400 5.22500   1.000 67.74661  ?  335  LYS B N   1 
ATOM   350  C  CA  . LYS A 1 58  ? 30.66000  -29.10700 6.64900   1.000 69.37763  ?  335  LYS B CA  1 
ATOM   351  C  C   . LYS A 1 58  ? 31.65900  -30.22200 6.89600   1.000 71.90694  ?  335  LYS B C   1 
ATOM   352  O  O   . LYS A 1 58  ? 32.34600  -30.21100 7.91900   1.000 77.88337  ?  335  LYS B O   1 
ATOM   353  C  CB  . LYS A 1 58  ? 29.33400  -29.48100 7.32600   1.000 75.01421  ?  335  LYS B CB  1 
ATOM   354  C  CG  . LYS A 1 58  ? 28.46300  -28.32500 7.79400   1.000 66.27665  ?  335  LYS B CG  1 
ATOM   355  C  CD  . LYS A 1 58  ? 27.07100  -28.82300 8.23700   1.000 73.28652  ?  335  LYS B CD  1 
ATOM   356  C  CE  . LYS A 1 58  ? 26.16800  -27.69100 8.75200   1.000 62.26605  ?  335  LYS B CE  1 
ATOM   357  N  N   . CYS A 1 59  ? 31.73300  -31.20400 6.00100   1.000 75.00264  ?  336  CYS B N   1 
ATOM   358  C  CA  . CYS A 1 59  ? 32.47900  -32.43200 6.24700   1.000 79.75532  ?  336  CYS B CA  1 
ATOM   359  C  C   . CYS A 1 59  ? 33.86600  -32.41700 5.60000   1.000 79.43011  ?  336  CYS B C   1 
ATOM   360  C  CB  . CYS A 1 59  ? 31.66900  -33.62300 5.74200   1.000 73.17429  ?  336  CYS B CB  1 
ATOM   361  S  SG  . CYS A 1 59  ? 31.98800  -33.90800 3.98900   1.000 100.44672 ?  336  CYS B SG  1 
ATOM   362  N  N   . VAL A 1 60  ? 34.31600  -31.24200 5.16500   1.000 82.36341  ?  337  VAL B N   1 
ATOM   363  C  CA  . VAL A 1 60  ? 35.56600  -31.08700 4.43000   1.000 84.00293  ?  337  VAL B CA  1 
ATOM   364  C  C   . VAL A 1 60  ? 36.66200  -30.72800 5.42400   1.000 80.87199  ?  337  VAL B C   1 
ATOM   365  O  O   . VAL A 1 60  ? 36.55800  -29.72700 6.13900   1.000 83.84616  ?  337  VAL B O   1 
ATOM   366  C  CB  . VAL A 1 60  ? 35.43400  -30.00600 3.33900   1.000 78.43516  ?  337  VAL B CB  1 
ATOM   367  C  CG1 . VAL A 1 60  ? 36.80200  -29.49300 2.91600   1.000 69.50976  ?  337  VAL B CG1 1 
ATOM   368  C  CG2 . VAL A 1 60  ? 34.66600  -30.52900 2.13200   1.000 74.21740  ?  337  VAL B CG2 1 
ATOM   369  N  N   . ASN A 1 61  ? 37.71100  -31.54000 5.47600   1.000 84.07126  ?  338  ASN B N   1 
ATOM   370  C  CA  . ASN A 1 61  ? 38.89100  -31.12700 6.22600   1.000 86.84729  ?  338  ASN B CA  1 
ATOM   371  C  C   . ASN A 1 61  ? 39.53900  -29.96400 5.49000   1.000 85.78673  ?  338  ASN B C   1 
ATOM   372  O  O   . ASN A 1 61  ? 40.34600  -30.18000 4.58000   1.000 84.93956  ?  338  ASN B O   1 
ATOM   373  C  CB  . ASN A 1 61  ? 39.88800  -32.27800 6.39600   1.000 86.44171  ?  338  ASN B CB  1 
ATOM   374  C  CG  . ASN A 1 61  ? 39.26900  -33.50900 7.04500   1.000 94.29970  ?  338  ASN B CG  1 
ATOM   375  O  OD1 . ASN A 1 61  ? 38.77100  -34.40400 6.35600   1.000 91.09222  ?  338  ASN B OD1 1 
ATOM   376  N  ND2 . ASN A 1 61  ? 39.31600  -33.56900 8.37600   1.000 102.88143 ?  338  ASN B ND2 1 
ATOM   377  N  N   . TRP A 1 62  ? 39.17600  -28.72600 5.83800   1.000 85.25319  ?  339  TRP B N   1 
ATOM   378  C  CA  . TRP A 1 62  ? 39.80100  -27.59200 5.16600   1.000 85.20796  ?  339  TRP B CA  1 
ATOM   379  C  C   . TRP A 1 62  ? 41.28400  -27.49500 5.49200   1.000 95.04986  ?  339  TRP B C   1 
ATOM   380  O  O   . TRP A 1 62  ? 42.04400  -26.90800 4.71500   1.000 100.10399 ?  339  TRP B O   1 
ATOM   381  C  CB  . TRP A 1 62  ? 39.05600  -26.31600 5.52300   1.000 86.40044  ?  339  TRP B CB  1 
ATOM   382  C  CG  . TRP A 1 62  ? 37.64300  -26.41100 5.05000   1.000 84.34436  ?  339  TRP B CG  1 
ATOM   383  C  CD1 . TRP A 1 62  ? 36.55700  -26.80100 5.77900   1.000 77.11274  ?  339  TRP B CD1 1 
ATOM   384  C  CD2 . TRP A 1 62  ? 37.17100  -26.16900 3.72200   1.000 74.32247  ?  339  TRP B CD2 1 
ATOM   385  N  NE1 . TRP A 1 62  ? 35.43400  -26.79400 4.99000   1.000 72.77622  ?  339  TRP B NE1 1 
ATOM   386  C  CE2 . TRP A 1 62  ? 35.78700  -26.41000 3.72200   1.000 72.10647  ?  339  TRP B CE2 1 
ATOM   387  C  CE3 . TRP A 1 62  ? 37.78700  -25.76900 2.53300   1.000 71.58239  ?  339  TRP B CE3 1 
ATOM   388  C  CZ2 . TRP A 1 62  ? 35.00800  -26.26400 2.58100   1.000 72.28672  ?  339  TRP B CZ2 1 
ATOM   389  C  CZ3 . TRP A 1 62  ? 37.01200  -25.62700 1.40000   1.000 69.64678  ?  339  TRP B CZ3 1 
ATOM   390  C  CH2 . TRP A 1 62  ? 35.64000  -25.88000 1.42900   1.000 67.49014  ?  339  TRP B CH2 1 
ATOM   391  N  N   . ASP A 1 63  ? 41.71100  -28.10500 6.59500   1.000 88.59376  ?  340  ASP B N   1 
ATOM   392  C  CA  . ASP A 1 63  ? 43.12600  -28.16800 6.92600   1.000 95.55564  ?  340  ASP B CA  1 
ATOM   393  C  C   . ASP A 1 63  ? 43.96700  -28.74200 5.77600   1.000 104.26452 ?  340  ASP B C   1 
ATOM   394  O  O   . ASP A 1 63  ? 45.09100  -28.28300 5.53500   1.000 108.57090 ?  340  ASP B O   1 
ATOM   395  C  CB  . ASP A 1 63  ? 43.29300  -29.00400 8.20200   1.000 95.70850  ?  340  ASP B CB  1 
ATOM   396  N  N   . LEU A 1 64  ? 43.43300  -29.77100 5.10700   1.000 104.10111 ?  341  LEU B N   1 
ATOM   397  C  CA  . LEU A 1 64  ? 44.19800  -30.47300 4.03800   1.000 94.59612  ?  341  LEU B CA  1 
ATOM   398  C  C   . LEU A 1 64  ? 44.10800  -29.70400 2.71800   1.000 93.58841  ?  341  LEU B C   1 
ATOM   399  O  O   . LEU A 1 64  ? 42.98600  -29.53800 2.20500   1.000 94.72784  ?  341  LEU B O   1 
ATOM   400  C  CB  . LEU A 1 64  ? 43.61900  -31.88200 3.87900   1.000 95.50598  ?  341  LEU B CB  1 
ATOM   401  C  CG  . LEU A 1 64  ? 43.52600  -32.70300 5.16300   1.000 95.29815  ?  341  LEU B CG  1 
ATOM   402  C  CD1 . LEU A 1 64  ? 43.05500  -34.11800 4.86700   1.000 92.77884  ?  341  LEU B CD1 1 
ATOM   403  C  CD2 . LEU A 1 64  ? 44.86300  -32.72900 5.88700   1.000 90.96144  ?  341  LEU B CD2 1 
ATOM   404  N  N   . PRO A 1 65  ? 45.24400  -29.26500 2.13600   1.000 95.60225  ?  342  PRO B N   1 
ATOM   405  C  CA  . PRO A 1 65  ? 45.23200  -28.49100 0.89400   1.000 94.77750  ?  342  PRO B CA  1 
ATOM   406  C  C   . PRO A 1 65  ? 44.60600  -29.27700 -0.26500  1.000 90.43454  ?  342  PRO B C   1 
ATOM   407  O  O   . PRO A 1 65  ? 43.79100  -28.71600 -0.97200  1.000 91.10088  ?  342  PRO B O   1 
ATOM   408  C  CB  . PRO A 1 65  ? 46.72100  -28.26200 0.60300   1.000 87.41030  ?  342  PRO B CB  1 
ATOM   409  C  CG  . PRO A 1 65  ? 47.39100  -28.40000 1.95100   1.000 99.44833  ?  342  PRO B CG  1 
ATOM   410  C  CD  . PRO A 1 65  ? 46.59600  -29.47800 2.65400   1.000 90.26957  ?  342  PRO B CD  1 
ATOM   411  N  N   . GLN A 1 66  ? 44.99400  -30.54300 -0.42900  1.000 87.27076  ?  343  GLN B N   1 
ATOM   412  C  CA  . GLN A 1 66  ? 44.48600  -31.34700 -1.57300  1.000 87.72119  ?  343  GLN B CA  1 
ATOM   413  C  C   . GLN A 1 66  ? 42.96600  -31.49300 -1.45600  1.000 88.21683  ?  343  GLN B C   1 
ATOM   414  O  O   . GLN A 1 66  ? 42.27100  -31.24900 -2.46000  1.000 84.55872  ?  343  GLN B O   1 
ATOM   415  C  CB  . GLN A 1 66  ? 45.17000  -32.71400 -1.62300  1.000 91.55967  ?  343  GLN B CB  1 
ATOM   416  C  CG  . GLN A 1 66  ? 44.71300  -33.57400 -2.79200  1.000 92.96233  ?  343  GLN B CG  1 
ATOM   417  C  CD  . GLN A 1 66  ? 45.65500  -34.72200 -3.06400  1.000 101.10356 ?  343  GLN B CD  1 
ATOM   418  O  OE1 . GLN A 1 66  ? 46.67700  -34.88200 -2.40100  1.000 105.30891 ?  343  GLN B OE1 1 
ATOM   419  N  NE2 . GLN A 1 66  ? 45.31700  -35.53000 -4.05500  1.000 98.88527  ?  343  GLN B NE2 1 
ATOM   420  N  N   . GLU A 1 67  ? 42.47500  -31.87500 -0.27400  1.000 90.85922  ?  344  GLU B N   1 
ATOM   421  C  CA  . GLU A 1 67  ? 41.03500  -32.00800 -0.09400  1.000 82.82551  ?  344  GLU B CA  1 
ATOM   422  C  C   . GLU A 1 67  ? 40.33500  -30.65900 -0.21400  1.000 80.87514  ?  344  GLU B C   1 
ATOM   423  O  O   . GLU A 1 67  ? 39.21100  -30.58800 -0.72000  1.000 76.56863  ?  344  GLU B O   1 
ATOM   424  C  CB  . GLU A 1 67  ? 40.71500  -32.66900 1.25400   1.000 84.64345  ?  344  GLU B CB  1 
ATOM   425  C  CG  . GLU A 1 67  ? 39.28000  -33.20700 1.34600   1.000 83.88669  ?  344  GLU B CG  1 
ATOM   426  C  CD  . GLU A 1 67  ? 38.93500  -33.80200 2.69900   1.000 85.60570  ?  344  GLU B CD  1 
ATOM   427  O  OE1 . GLU A 1 67  ? 39.71400  -34.62400 3.23400   1.000 97.37526  ?  344  GLU B OE1 1 
ATOM   428  O  OE2 . GLU A 1 67  ? 37.87100  -33.44200 3.23300   1.000 86.73908  -1 344  GLU B OE2 1 
ATOM   429  N  N   . ALA A 1 68  ? 40.97200  -29.57700 0.24700   1.000 82.44438  ?  345  ALA B N   1 
ATOM   430  C  CA  . ALA A 1 68  ? 40.36400  -28.26100 0.07300   1.000 79.00008  ?  345  ALA B CA  1 
ATOM   431  C  C   . ALA A 1 68  ? 40.28300  -27.89700 -1.40500  1.000 82.74998  ?  345  ALA B C   1 
ATOM   432  O  O   . ALA A 1 68  ? 39.26100  -27.37700 -1.86500  1.000 81.67374  ?  345  ALA B O   1 
ATOM   433  C  CB  . ALA A 1 68  ? 41.14100  -27.20200 0.85300   1.000 80.10313  ?  345  ALA B CB  1 
ATOM   434  N  N   . LYS A 1 69  ? 41.34200  -28.18400 -2.16800  1.000 77.85435  ?  346  LYS B N   1 
ATOM   435  C  CA  . LYS A 1 69  ? 41.28100  -27.99000 -3.61100  1.000 80.93253  ?  346  LYS B CA  1 
ATOM   436  C  C   . LYS A 1 69  ? 40.08900  -28.73300 -4.20400  1.000 83.74897  ?  346  LYS B C   1 
ATOM   437  O  O   . LYS A 1 69  ? 39.19500  -28.12300 -4.80300  1.000 82.43489  ?  346  LYS B O   1 
ATOM   438  C  CB  . LYS A 1 69  ? 42.58600  -28.44600 -4.26500  1.000 81.42630  ?  346  LYS B CB  1 
ATOM   439  N  N   . GLN A 1 70  ? 40.05400  -30.05800 -4.03100  1.000 79.59353  ?  347  GLN B N   1 
ATOM   440  C  CA  . GLN A 1 70  ? 38.94500  -30.85000 -4.55400  1.000 79.84332  ?  347  GLN B CA  1 
ATOM   441  C  C   . GLN A 1 70  ? 37.59400  -30.30400 -4.10600  1.000 82.06379  ?  347  GLN B C   1 
ATOM   442  O  O   . GLN A 1 70  ? 36.62500  -30.31900 -4.87500  1.000 85.17387  ?  347  GLN B O   1 
ATOM   443  C  CB  . GLN A 1 70  ? 39.08300  -32.30000 -4.11100  1.000 82.15999  ?  347  GLN B CB  1 
ATOM   444  C  CG  . GLN A 1 70  ? 38.35700  -33.28500 -5.01400  1.000 93.16585  ?  347  GLN B CG  1 
ATOM   445  C  CD  . GLN A 1 70  ? 38.14000  -34.65100 -4.36400  1.000 100.72261 ?  347  GLN B CD  1 
ATOM   446  O  OE1 . GLN A 1 70  ? 36.99900  -35.04100 -4.09200  1.000 97.76696  ?  347  GLN B OE1 1 
ATOM   447  N  NE2 . GLN A 1 70  ? 39.23100  -35.38500 -4.11800  1.000 98.82846  ?  347  GLN B NE2 1 
ATOM   448  N  N   . ALA A 1 71  ? 37.50500  -29.83000 -2.85800  1.000 80.13538  ?  348  ALA B N   1 
ATOM   449  C  CA  . ALA A 1 71  ? 36.23300  -29.33600 -2.34200  1.000 76.26100  ?  348  ALA B CA  1 
ATOM   450  C  C   . ALA A 1 71  ? 35.80300  -28.07300 -3.07000  1.000 78.61430  ?  348  ALA B C   1 
ATOM   451  O  O   . ALA A 1 71  ? 34.62400  -27.91600 -3.39800  1.000 81.08403  ?  348  ALA B O   1 
ATOM   452  C  CB  . ALA A 1 71  ? 36.33100  -29.07700 -0.83400  1.000 75.78817  ?  348  ALA B CB  1 
ATOM   453  N  N   . LEU A 1 72  ? 36.74600  -27.15900 -3.32600  1.000 79.63328  ?  349  LEU B N   1 
ATOM   454  C  CA  . LEU A 1 72  ? 36.42800  -25.95000 -4.07900  1.000 79.86146  ?  349  LEU B CA  1 
ATOM   455  C  C   . LEU A 1 72  ? 36.10400  -26.26300 -5.53600  1.000 80.07585  ?  349  LEU B C   1 
ATOM   456  O  O   . LEU A 1 72  ? 35.23100  -25.61800 -6.12300  1.000 80.32763  ?  349  LEU B O   1 
ATOM   457  C  CB  . LEU A 1 72  ? 37.57800  -24.94600 -3.96600  1.000 73.05989  ?  349  LEU B CB  1 
ATOM   458  C  CG  . LEU A 1 72  ? 37.86100  -24.49000 -2.52100  1.000 74.33505  ?  349  LEU B CG  1 
ATOM   459  C  CD1 . LEU A 1 72  ? 38.97600  -23.46400 -2.45300  1.000 70.43172  ?  349  LEU B CD1 1 
ATOM   460  C  CD2 . LEU A 1 72  ? 36.60600  -23.94600 -1.82000  1.000 70.00392  ?  349  LEU B CD2 1 
ATOM   461  N  N   . GLU A 1 73  ? 36.76400  -27.25500 -6.13600  1.000 80.22707  ?  350  GLU B N   1 
ATOM   462  C  CA  . GLU A 1 73  ? 36.33900  -27.68700 -7.46500  1.000 82.37352  ?  350  GLU B CA  1 
ATOM   463  C  C   . GLU A 1 73  ? 34.86300  -28.07700 -7.44800  1.000 85.13306  ?  350  GLU B C   1 
ATOM   464  O  O   . GLU A 1 73  ? 34.07600  -27.62100 -8.28800  1.000 86.70874  ?  350  GLU B O   1 
ATOM   465  C  CB  . GLU A 1 73  ? 37.20500  -28.84700 -7.96000  1.000 80.20779  ?  350  GLU B CB  1 
ATOM   466  C  CG  . GLU A 1 73  ? 38.59400  -28.46000 -8.44900  1.000 86.94170  ?  350  GLU B CG  1 
ATOM   467  N  N   . LEU A 1 74  ? 34.46500  -28.90200 -6.47200  1.000 82.73361  ?  351  LEU B N   1 
ATOM   468  C  CA  . LEU A 1 74  ? 33.07700  -29.34400 -6.38100  1.000 80.87011  ?  351  LEU B CA  1 
ATOM   469  C  C   . LEU A 1 74  ? 32.12900  -28.18000 -6.10300  1.000 80.86172  ?  351  LEU B C   1 
ATOM   470  O  O   . LEU A 1 74  ? 30.99100  -28.16900 -6.58800  1.000 83.62125  ?  351  LEU B O   1 
ATOM   471  C  CB  . LEU A 1 74  ? 32.94200  -30.41000 -5.30000  1.000 78.26959  ?  351  LEU B CB  1 
ATOM   472  C  CG  . LEU A 1 74  ? 33.08100  -31.85300 -5.75700  1.000 86.32150  ?  351  LEU B CG  1 
ATOM   473  C  CD1 . LEU A 1 74  ? 33.00400  -32.80200 -4.56200  1.000 82.29284  ?  351  LEU B CD1 1 
ATOM   474  C  CD2 . LEU A 1 74  ? 31.98000  -32.13200 -6.75300  1.000 86.70694  ?  351  LEU B CD2 1 
ATOM   475  N  N   . LEU A 1 75  ? 32.57100  -27.20100 -5.30800  1.000 77.57858  ?  352  LEU B N   1 
ATOM   476  C  CA  . LEU A 1 75  ? 31.77100  -25.99900 -5.10500  1.000 80.57531  ?  352  LEU B CA  1 
ATOM   477  C  C   . LEU A 1 75  ? 31.48800  -25.30700 -6.42600  1.000 82.61450  ?  352  LEU B C   1 
ATOM   478  O  O   . LEU A 1 75  ? 30.40400  -24.74700 -6.61300  1.000 80.56613  ?  352  LEU B O   1 
ATOM   479  C  CB  . LEU A 1 75  ? 32.48800  -25.05100 -4.14600  1.000 79.75866  ?  352  LEU B CB  1 
ATOM   480  C  CG  . LEU A 1 75  ? 31.82500  -23.72300 -3.79600  1.000 76.18856  ?  352  LEU B CG  1 
ATOM   481  C  CD1 . LEU A 1 75  ? 30.51100  -23.93100 -3.01400  1.000 75.49665  ?  352  LEU B CD1 1 
ATOM   482  C  CD2 . LEU A 1 75  ? 32.81100  -22.87000 -3.00900  1.000 73.16364  ?  352  LEU B CD2 1 
ATOM   483  N  N   . GLY A 1 76  ? 32.44300  -25.35900 -7.35900  1.000 84.88156  ?  353  GLY B N   1 
ATOM   484  C  CA  . GLY A 1 76  ? 32.22400  -24.76400 -8.66400  1.000 81.15777  ?  353  GLY B CA  1 
ATOM   485  C  C   . GLY A 1 76  ? 31.22100  -25.54300 -9.48800  1.000 82.21688  ?  353  GLY B C   1 
ATOM   486  O  O   . GLY A 1 76  ? 30.32300  -24.96100 -10.09900 1.000 91.86601  ?  353  GLY B O   1 
ATOM   487  N  N   . LYS A 1 77  ? 31.35000  -26.86600 -9.51400  1.000 87.89636  ?  354  LYS B N   1 
ATOM   488  C  CA  . LYS A 1 77  ? 30.42500  -27.68600 -10.28500 1.000 85.20215  ?  354  LYS B CA  1 
ATOM   489  C  C   . LYS A 1 77  ? 29.08100  -27.89700 -9.58900  1.000 79.32840  ?  354  LYS B C   1 
ATOM   490  O  O   . LYS A 1 77  ? 28.20800  -28.55700 -10.16000 1.000 80.91053  ?  354  LYS B O   1 
ATOM   491  C  CB  . LYS A 1 77  ? 31.07200  -29.04400 -10.60900 1.000 85.87315  ?  354  LYS B CB  1 
ATOM   492  N  N   . TRP A 1 78  ? 28.87000  -27.34900 -8.39300  1.000 70.72769  ?  355  TRP B N   1 
ATOM   493  C  CA  . TRP A 1 78  ? 27.69900  -27.70600 -7.60600  1.000 78.82599  ?  355  TRP B CA  1 
ATOM   494  C  C   . TRP A 1 78  ? 26.48700  -26.86700 -7.99500  1.000 83.26528  ?  355  TRP B C   1 
ATOM   495  O  O   . TRP A 1 78  ? 26.59700  -25.66100 -8.24300  1.000 82.10622  ?  355  TRP B O   1 
ATOM   496  C  CB  . TRP A 1 78  ? 27.97800  -27.52800 -6.11200  1.000 79.89423  ?  355  TRP B CB  1 
ATOM   497  C  CG  . TRP A 1 78  ? 27.16200  -28.44500 -5.28200  1.000 75.72636  ?  355  TRP B CG  1 
ATOM   498  C  CD1 . TRP A 1 78  ? 25.81600  -28.39700 -5.09200  1.000 73.93588  ?  355  TRP B CD1 1 
ATOM   499  C  CD2 . TRP A 1 78  ? 27.63600  -29.58000 -4.54600  1.000 80.34354  ?  355  TRP B CD2 1 
ATOM   500  N  NE1 . TRP A 1 78  ? 25.41900  -29.43400 -4.28000  1.000 77.16493  ?  355  TRP B NE1 1 
ATOM   501  C  CE2 . TRP A 1 78  ? 26.51900  -30.17100 -3.92900  1.000 77.77029  ?  355  TRP B CE2 1 
ATOM   502  C  CE3 . TRP A 1 78  ? 28.89900  -30.15000 -4.34300  1.000 75.90325  ?  355  TRP B CE3 1 
ATOM   503  C  CZ2 . TRP A 1 78  ? 26.62800  -31.30200 -3.12000  1.000 80.67810  ?  355  TRP B CZ2 1 
ATOM   504  C  CZ3 . TRP A 1 78  ? 29.00300  -31.26700 -3.54500  1.000 74.47103  ?  355  TRP B CZ3 1 
ATOM   505  C  CH2 . TRP A 1 78  ? 27.87700  -31.83600 -2.94700  1.000 75.27529  ?  355  TRP B CH2 1 
ATOM   506  N  N   . LYS A 1 79  ? 25.32200  -27.51100 -8.03100  1.000 80.94182  ?  356  LYS B N   1 
ATOM   507  C  CA  . LYS A 1 79  ? 24.06000  -26.79700 -8.18600  1.000 81.16724  ?  356  LYS B CA  1 
ATOM   508  C  C   . LYS A 1 79  ? 23.98300  -25.65800 -7.17100  1.000 79.21723  ?  356  LYS B C   1 
ATOM   509  O  O   . LYS A 1 79  ? 23.99100  -25.91600 -5.96000  1.000 74.27682  ?  356  LYS B O   1 
ATOM   510  C  CB  . LYS A 1 79  ? 22.88200  -27.75200 -8.00200  1.000 88.55156  ?  356  LYS B CB  1 
ATOM   511  C  CG  . LYS A 1 79  ? 21.50000  -27.14600 -8.26800  1.000 88.74700  ?  356  LYS B CG  1 
ATOM   512  C  CD  . LYS A 1 79  ? 20.50200  -28.24400 -8.68700  1.000 96.59330  ?  356  LYS B CD  1 
ATOM   513  C  CE  . LYS A 1 79  ? 19.06100  -27.74000 -8.77700  1.000 92.57002  ?  356  LYS B CE  1 
ATOM   514  N  NZ  . LYS A 1 79  ? 18.35100  -27.80900 -7.46100  1.000 105.21357 ?  356  LYS B NZ  1 
ATOM   515  N  N   . PRO A 1 80  ? 23.91700  -24.40600 -7.61800  1.000 72.56668  ?  357  PRO B N   1 
ATOM   516  C  CA  . PRO A 1 80  ? 24.06600  -23.27200 -6.69100  1.000 80.15326  ?  357  PRO B CA  1 
ATOM   517  C  C   . PRO A 1 80  ? 23.01300  -23.29300 -5.59400  1.000 78.40759  ?  357  PRO B C   1 
ATOM   518  O  O   . PRO A 1 80  ? 21.85100  -23.63900 -5.82500  1.000 78.32132  ?  357  PRO B O   1 
ATOM   519  C  CB  . PRO A 1 80  ? 23.90900  -22.04500 -7.59400  1.000 77.20600  ?  357  PRO B CB  1 
ATOM   520  C  CG  . PRO A 1 80  ? 24.19500  -22.54200 -8.96800  1.000 74.92557  ?  357  PRO B CG  1 
ATOM   521  C  CD  . PRO A 1 80  ? 23.69800  -23.95600 -8.99900  1.000 74.72144  ?  357  PRO B CD  1 
ATOM   522  N  N   . MET A 1 81  ? 23.42800  -22.90900 -4.39300  1.000 74.52061  ?  358  MET B N   1 
ATOM   523  C  CA  . MET A 1 81  ? 22.53500  -23.00200 -3.25200  1.000 79.66655  ?  358  MET B CA  1 
ATOM   524  C  C   . MET A 1 81  ? 21.67600  -21.74700 -3.13400  1.000 74.22728  ?  358  MET B C   1 
ATOM   525  O  O   . MET A 1 81  ? 22.03100  -20.66400 -3.61600  1.000 70.09538  ?  358  MET B O   1 
ATOM   526  C  CB  . MET A 1 81  ? 23.31400  -23.24300 -1.95600  1.000 75.64932  ?  358  MET B CB  1 
ATOM   527  C  CG  . MET A 1 81  ? 24.02800  -22.04200 -1.40400  1.000 66.60813  ?  358  MET B CG  1 
ATOM   528  S  SD  . MET A 1 81  ? 24.52000  -22.33200 0.31100   1.000 74.27998  ?  358  MET B SD  1 
ATOM   529  C  CE  . MET A 1 81  ? 25.97400  -23.35700 0.06000   1.000 74.29997  ?  358  MET B CE  1 
ATOM   530  N  N   . ASP A 1 82  ? 20.51500  -21.92000 -2.50800  1.000 75.04738  ?  359  ASP B N   1 
ATOM   531  C  CA  . ASP A 1 82  ? 19.60000  -20.81000 -2.30500  1.000 70.56990  ?  359  ASP B CA  1 
ATOM   532  C  C   . ASP A 1 82  ? 20.25400  -19.72600 -1.46600  1.000 69.25034  ?  359  ASP B C   1 
ATOM   533  O  O   . ASP A 1 82  ? 21.16200  -19.98700 -0.66900  1.000 67.07001  ?  359  ASP B O   1 
ATOM   534  C  CB  . ASP A 1 82  ? 18.33300  -21.29200 -1.61200  1.000 72.03345  ?  359  ASP B CB  1 
ATOM   535  C  CG  . ASP A 1 82  ? 17.77100  -22.53100 -2.24900  1.000 85.01814  ?  359  ASP B CG  1 
ATOM   536  O  OD1 . ASP A 1 82  ? 17.88900  -22.67700 -3.48600  1.000 88.91569  ?  359  ASP B OD1 1 
ATOM   537  O  OD2 . ASP A 1 82  ? 17.22100  -23.37500 -1.51300  1.000 95.61195  -1 359  ASP B OD2 1 
ATOM   538  N  N   . VAL A 1 83  ? 19.77200  -18.49500 -1.65300  1.000 67.42349  ?  360  VAL B N   1 
ATOM   539  C  CA  . VAL A 1 83  ? 20.14800  -17.39100 -0.77300  1.000 66.09191  ?  360  VAL B CA  1 
ATOM   540  C  C   . VAL A 1 83  ? 19.89500  -17.74700 0.69100   1.000 65.02718  ?  360  VAL B C   1 
ATOM   541  O  O   . VAL A 1 83  ? 20.72800  -17.46600 1.56100   1.000 61.42277  ?  360  VAL B O   1 
ATOM   542  C  CB  . VAL A 1 83  ? 19.39000  -16.11200 -1.17100  1.000 64.13415  ?  360  VAL B CB  1 
ATOM   543  C  CG1 . VAL A 1 83  ? 19.68600  -15.00700 -0.18000  1.000 64.71634  ?  360  VAL B CG1 1 
ATOM   544  C  CG2 . VAL A 1 83  ? 19.76700  -15.69200 -2.56900  1.000 62.43913  ?  360  VAL B CG2 1 
ATOM   545  N  N   . GLU A 1 84  ? 18.74300  -18.35900 0.99100   1.000 62.22933  ?  361  GLU B N   1 
ATOM   546  C  CA  . GLU A 1 84  ? 18.41600  -18.65000 2.38800   1.000 65.34671  ?  361  GLU B CA  1 
ATOM   547  C  C   . GLU A 1 84  ? 19.43600  -19.58600 3.01400   1.000 63.30408  ?  361  GLU B C   1 
ATOM   548  O  O   . GLU A 1 84  ? 19.78400  -19.43400 4.19200   1.000 63.22636  ?  361  GLU B O   1 
ATOM   549  C  CB  . GLU A 1 84  ? 17.01700  -19.25900 2.52100   1.000 66.81836  ?  361  GLU B CB  1 
ATOM   550  C  CG  . GLU A 1 84  ? 15.88800  -18.39300 2.01900   1.000 71.64868  ?  361  GLU B CG  1 
ATOM   551  C  CD  . GLU A 1 84  ? 15.75700  -18.42700 0.50700   1.000 78.17920  ?  361  GLU B CD  1 
ATOM   552  O  OE1 . GLU A 1 84  ? 16.42200  -19.27300 -0.13600  1.000 74.61360  ?  361  GLU B OE1 1 
ATOM   553  O  OE2 . GLU A 1 84  ? 14.99300  -17.59900 -0.03300  1.000 82.38428  -1 361  GLU B OE2 1 
ATOM   554  N  N   . ASP A 1 85  ? 19.90300  -20.58000 2.25500   1.000 61.92718  ?  362  ASP B N   1 
ATOM   555  C  CA  . ASP A 1 85  ? 20.90100  -21.49900 2.78700   1.000 65.54019  ?  362  ASP B CA  1 
ATOM   556  C  C   . ASP A 1 85  ? 22.29200  -20.89000 2.80200   1.000 64.07684  ?  362  ASP B C   1 
ATOM   557  O  O   . ASP A 1 85  ? 23.13800  -21.30000 3.60400   1.000 67.71964  ?  362  ASP B O   1 
ATOM   558  C  CB  . ASP A 1 85  ? 20.91700  -22.79500 1.97900   1.000 67.24803  ?  362  ASP B CB  1 
ATOM   559  C  CG  . ASP A 1 85  ? 19.59500  -23.52000 2.03900   1.000 78.59276  ?  362  ASP B CG  1 
ATOM   560  O  OD1 . ASP A 1 85  ? 18.97800  -23.54700 3.13100   1.000 85.42516  ?  362  ASP B OD1 1 
ATOM   561  O  OD2 . ASP A 1 85  ? 19.15900  -24.05400 0.99700   1.000 84.88922  -1 362  ASP B OD2 1 
ATOM   562  N  N   . SER A 1 86  ? 22.55700  -19.92800 1.92400   1.000 59.79191  ?  363  SER B N   1 
ATOM   563  C  CA  . SER A 1 86  ? 23.87500  -19.31400 1.91500   1.000 61.82438  ?  363  SER B CA  1 
ATOM   564  C  C   . SER A 1 86  ? 24.13800  -18.54200 3.20500   1.000 63.24836  ?  363  SER B C   1 
ATOM   565  O  O   . SER A 1 86  ? 25.29700  -18.42500 3.62900   1.000 62.85967  ?  363  SER B O   1 
ATOM   566  C  CB  . SER A 1 86  ? 24.01700  -18.40400 0.70000   1.000 59.76586  ?  363  SER B CB  1 
ATOM   567  O  OG  . SER A 1 86  ? 23.29900  -17.19400 0.88900   1.000 61.10218  ?  363  SER B OG  1 
ATOM   568  N  N   . LEU A 1 87  ? 23.08600  -18.01300 3.84400   1.000 57.36133  ?  364  LEU B N   1 
ATOM   569  C  CA  . LEU A 1 87  ? 23.27800  -17.35200 5.12900   1.000 56.76029  ?  364  LEU B CA  1 
ATOM   570  C  C   . LEU A 1 87  ? 24.10300  -18.22200 6.07300   1.000 57.74916  ?  364  LEU B C   1 
ATOM   571  O  O   . LEU A 1 87  ? 24.91900  -17.70000 6.84000   1.000 53.47603  ?  364  LEU B O   1 
ATOM   572  C  CB  . LEU A 1 87  ? 21.92100  -16.99900 5.75200   1.000 52.21113  ?  364  LEU B CB  1 
ATOM   573  C  CG  . LEU A 1 87  ? 21.08000  -15.96600 4.98200   1.000 54.31040  ?  364  LEU B CG  1 
ATOM   574  C  CD1 . LEU A 1 87  ? 19.65000  -15.81600 5.54900   1.000 50.97669  ?  364  LEU B CD1 1 
ATOM   575  C  CD2 . LEU A 1 87  ? 21.79300  -14.61700 4.92600   1.000 50.91235  ?  364  LEU B CD2 1 
ATOM   576  N  N   . GLU A 1 88  ? 23.92600  -19.54900 6.00900   1.000 59.37329  ?  365  GLU B N   1 
ATOM   577  C  CA  . GLU A 1 88  ? 24.69200  -20.45600 6.86000   1.000 59.08384  ?  365  GLU B CA  1 
ATOM   578  C  C   . GLU A 1 88  ? 26.19900  -20.26900 6.67700   1.000 58.68280  ?  365  GLU B C   1 
ATOM   579  O  O   . GLU A 1 88  ? 26.95400  -20.27900 7.65700   1.000 59.45533  ?  365  GLU B O   1 
ATOM   580  C  CB  . GLU A 1 88  ? 24.29400  -21.90500 6.57500   1.000 61.15872  ?  365  GLU B CB  1 
ATOM   581  C  CG  . GLU A 1 88  ? 25.23300  -22.95100 7.21900   1.000 66.44147  ?  365  GLU B CG  1 
ATOM   582  C  CD  . GLU A 1 88  ? 24.67400  -24.37800 7.17200   1.000 72.68486  ?  365  GLU B CD  1 
ATOM   583  O  OE1 . GLU A 1 88  ? 23.47800  -24.55400 6.84200   1.000 73.69369  ?  365  GLU B OE1 1 
ATOM   584  O  OE2 . GLU A 1 88  ? 25.43300  -25.33100 7.46300   1.000 80.46724  -1 365  GLU B OE2 1 
ATOM   585  N  N   . LEU A 1 89  ? 26.65600  -20.09200 5.43400   1.000 56.90966  ?  366  LEU B N   1 
ATOM   586  C  CA  . LEU A 1 89  ? 28.08700  -19.97700 5.16300   1.000 59.77751  ?  366  LEU B CA  1 
ATOM   587  C  C   . LEU A 1 89  ? 28.71700  -18.70400 5.73000   1.000 59.58642  ?  366  LEU B C   1 
ATOM   588  O  O   . LEU A 1 89  ? 29.94900  -18.61300 5.75700   1.000 60.18512  ?  366  LEU B O   1 
ATOM   589  C  CB  . LEU A 1 89  ? 28.35300  -20.05000 3.64700   1.000 65.52450  ?  366  LEU B CB  1 
ATOM   590  C  CG  . LEU A 1 89  ? 27.81900  -21.26200 2.86200   1.000 61.69465  ?  366  LEU B CG  1 
ATOM   591  C  CD1 . LEU A 1 89  ? 28.29400  -21.24000 1.43100   1.000 62.73575  ?  366  LEU B CD1 1 
ATOM   592  C  CD2 . LEU A 1 89  ? 28.20600  -22.57000 3.53300   1.000 60.75862  ?  366  LEU B CD2 1 
ATOM   593  N  N   . LEU A 1 90  ? 27.92100  -17.71900 6.16500   1.000 56.12688  ?  367  LEU B N   1 
ATOM   594  C  CA  . LEU A 1 90  ? 28.46500  -16.52500 6.80500   1.000 54.60937  ?  367  LEU B CA  1 
ATOM   595  C  C   . LEU A 1 90  ? 28.58400  -16.65900 8.31900   1.000 56.58472  ?  367  LEU B C   1 
ATOM   596  O  O   . LEU A 1 90  ? 29.13600  -15.75600 8.96600   1.000 53.15450  ?  367  LEU B O   1 
ATOM   597  C  CB  . LEU A 1 90  ? 27.60800  -15.29800 6.46400   1.000 52.56441  ?  367  LEU B CB  1 
ATOM   598  C  CG  . LEU A 1 90  ? 27.67500  -14.94300 4.97400   1.000 56.81304  ?  367  LEU B CG  1 
ATOM   599  C  CD1 . LEU A 1 90  ? 26.73400  -13.81000 4.65900   1.000 54.64378  ?  367  LEU B CD1 1 
ATOM   600  C  CD2 . LEU A 1 90  ? 29.11200  -14.61100 4.52900   1.000 51.30909  ?  367  LEU B CD2 1 
ATOM   601  N  N   . SER A 1 91  ? 28.09200  -17.75400 8.89800   1.000 55.00795  ?  368  SER B N   1 
ATOM   602  C  CA  . SER A 1 91  ? 28.14500  -17.91700 10.34100  1.000 55.95276  ?  368  SER B CA  1 
ATOM   603  C  C   . SER A 1 91  ? 29.58500  -18.16400 10.78200  1.000 58.59061  ?  368  SER B C   1 
ATOM   604  O  O   . SER A 1 91  ? 30.51400  -18.25100 9.97600   1.000 63.13368  ?  368  SER B O   1 
ATOM   605  C  CB  . SER A 1 91  ? 27.23700  -19.06000 10.79400  1.000 52.36353  ?  368  SER B CB  1 
ATOM   606  O  OG  . SER A 1 91  ? 27.84400  -20.33300 10.59600  1.000 60.34115  ?  368  SER B OG  1 
ATOM   607  N  N   . SER A 1 92  ? 29.76400  -18.27700 12.08800  1.000 55.93806  ?  369  SER B N   1 
ATOM   608  C  CA  . SER A 1 92  ? 31.10100  -18.38600 12.64600  1.000 58.90808  ?  369  SER B CA  1 
ATOM   609  C  C   . SER A 1 92  ? 31.75900  -19.72600 12.34800  1.000 69.22982  ?  369  SER B C   1 
ATOM   610  O  O   . SER A 1 92  ? 32.97600  -19.84700 12.52100  1.000 65.28711  ?  369  SER B O   1 
ATOM   611  C  CB  . SER A 1 92  ? 31.04200  -18.18400 14.15300  1.000 65.08083  ?  369  SER B CB  1 
ATOM   612  O  OG  . SER A 1 92  ? 30.47100  -19.32900 14.75100  1.000 66.69467  ?  369  SER B OG  1 
ATOM   613  N  N   . HIS A 1 93  ? 30.99600  -20.73600 11.92600  1.000 66.36961  ?  370  HIS B N   1 
ATOM   614  C  CA  . HIS A 1 93  ? 31.60100  -22.03800 11.67500  1.000 65.41487  ?  370  HIS B CA  1 
ATOM   615  C  C   . HIS A 1 93  ? 32.34500  -22.09900 10.35400  1.000 68.52968  ?  370  HIS B C   1 
ATOM   616  O  O   . HIS A 1 93  ? 32.92100  -23.14300 10.05000  1.000 73.95238  ?  370  HIS B O   1 
ATOM   617  C  CB  . HIS A 1 93  ? 30.54400  -23.15200 11.70500  1.000 66.73417  ?  370  HIS B CB  1 
ATOM   618  N  N   . TYR A 1 94  ? 32.35200  -21.03600 9.55400   1.000 62.49847  ?  371  TYR B N   1 
ATOM   619  C  CA  . TYR A 1 94  ? 33.00700  -21.08000 8.25300   1.000 65.11029  ?  371  TYR B CA  1 
ATOM   620  C  C   . TYR A 1 94  ? 34.05300  -19.98000 8.17400   1.000 64.36822  ?  371  TYR B C   1 
ATOM   621  O  O   . TYR A 1 94  ? 33.73800  -18.79700 8.34800   1.000 58.91253  ?  371  TYR B O   1 
ATOM   622  C  CB  . TYR A 1 94  ? 32.00400  -20.95500 7.11700   1.000 60.73977  ?  371  TYR B CB  1 
ATOM   623  C  CG  . TYR A 1 94  ? 31.02700  -22.09600 7.00500   1.000 63.28526  ?  371  TYR B CG  1 
ATOM   624  C  CD1 . TYR A 1 94  ? 29.82900  -22.08100 7.71500   1.000 63.97246  ?  371  TYR B CD1 1 
ATOM   625  C  CD2 . TYR A 1 94  ? 31.28600  -23.17600 6.16700   1.000 68.00529  ?  371  TYR B CD2 1 
ATOM   626  C  CE1 . TYR A 1 94  ? 28.91600  -23.11700 7.60400   1.000 63.85676  ?  371  TYR B CE1 1 
ATOM   627  C  CE2 . TYR A 1 94  ? 30.38600  -24.22000 6.04400   1.000 68.30509  ?  371  TYR B CE2 1 
ATOM   628  C  CZ  . TYR A 1 94  ? 29.19600  -24.17800 6.76100   1.000 69.79769  ?  371  TYR B CZ  1 
ATOM   629  O  OH  . TYR A 1 94  ? 28.28400  -25.20500 6.64000   1.000 73.92041  ?  371  TYR B OH  1 
ATOM   630  N  N   . THR A 1 95  ? 35.29600  -20.38200 7.90800   1.000 66.67634  ?  372  THR B N   1 
ATOM   631  C  CA  . THR A 1 95  ? 36.43600  -19.48500 7.87200   1.000 61.37491  ?  372  THR B CA  1 
ATOM   632  C  C   . THR A 1 95  ? 37.18600  -19.49300 6.54500   1.000 65.47389  ?  372  THR B C   1 
ATOM   633  O  O   . THR A 1 95  ? 37.87900  -18.51600 6.25100   1.000 70.21047  ?  372  THR B O   1 
ATOM   634  C  CB  . THR A 1 95  ? 37.41100  -19.83800 8.99600   1.000 63.09656  ?  372  THR B CB  1 
ATOM   635  O  OG1 . THR A 1 95  ? 37.90000  -21.17200 8.79400   1.000 73.97295  ?  372  THR B OG1 1 
ATOM   636  C  CG2 . THR A 1 95  ? 36.70000  -19.78800 10.34000  1.000 61.95430  ?  372  THR B CG2 1 
ATOM   637  N  N   . ASN A 1 96  ? 37.07200  -20.55000 5.74500   1.000 61.31121  ?  373  ASN B N   1 
ATOM   638  C  CA  . ASN A 1 96  ? 37.65600  -20.57000 4.41400   1.000 64.66250  ?  373  ASN B CA  1 
ATOM   639  C  C   . ASN A 1 96  ? 37.19200  -19.34800 3.61600   1.000 67.20082  ?  373  ASN B C   1 
ATOM   640  O  O   . ASN A 1 96  ? 35.98300  -19.13600 3.46600   1.000 70.08909  ?  373  ASN B O   1 
ATOM   641  C  CB  . ASN A 1 96  ? 37.26200  -21.85700 3.69300   1.000 63.27466  ?  373  ASN B CB  1 
ATOM   642  C  CG  . ASN A 1 96  ? 37.89600  -21.97500 2.32200   1.000 71.93466  ?  373  ASN B CG  1 
ATOM   643  O  OD1 . ASN A 1 96  ? 37.30400  -21.58100 1.31700   1.000 72.30237  ?  373  ASN B OD1 1 
ATOM   644  N  ND2 . ASN A 1 96  ? 39.10400  -22.52500 2.27100   1.000 77.12440  ?  373  ASN B ND2 1 
ATOM   645  N  N   . PRO A 1 97  ? 38.10800  -18.52800 3.10300   1.000 70.53468  ?  374  PRO B N   1 
ATOM   646  C  CA  . PRO A 1 97  ? 37.67800  -17.31100 2.39500   1.000 62.85653  ?  374  PRO B CA  1 
ATOM   647  C  C   . PRO A 1 97  ? 36.84700  -17.59500 1.15500   1.000 66.85999  ?  374  PRO B C   1 
ATOM   648  O  O   . PRO A 1 97  ? 35.88100  -16.86500 0.88700   1.000 64.83709  ?  374  PRO B O   1 
ATOM   649  C  CB  . PRO A 1 97  ? 39.00300  -16.62500 2.03500   1.000 65.14130  ?  374  PRO B CB  1 
ATOM   650  C  CG  . PRO A 1 97  ? 40.01500  -17.22100 2.95000   1.000 67.46362  ?  374  PRO B CG  1 
ATOM   651  C  CD  . PRO A 1 97  ? 39.57500  -18.63900 3.19200   1.000 69.41679  ?  374  PRO B CD  1 
ATOM   652  N  N   . THR A 1 98  ? 37.19900  -18.63200 0.38100   1.000 64.10815  ?  375  THR B N   1 
ATOM   653  C  CA  . THR A 1 98  ? 36.45400  -18.91300 -0.84500  1.000 65.20525  ?  375  THR B CA  1 
ATOM   654  C  C   . THR A 1 98  ? 35.01800  -19.31000 -0.53600  1.000 67.59002  ?  375  THR B C   1 
ATOM   655  O  O   . THR A 1 98  ? 34.09200  -18.93600 -1.26700  1.000 63.04807  ?  375  THR B O   1 
ATOM   656  C  CB  . THR A 1 98  ? 37.13100  -20.01400 -1.65700  1.000 68.55563  ?  375  THR B CB  1 
ATOM   657  O  OG1 . THR A 1 98  ? 38.51300  -19.68800 -1.86100  1.000 71.05655  ?  375  THR B OG1 1 
ATOM   658  C  CG2 . THR A 1 98  ? 36.44700  -20.15200 -3.00900  1.000 61.97434  ?  375  THR B CG2 1 
ATOM   659  N  N   . VAL A 1 99  ? 34.81800  -20.08000 0.53900   1.000 64.89211  ?  376  VAL B N   1 
ATOM   660  C  CA  . VAL A 1 99  ? 33.46600  -20.40200 0.97800   1.000 65.19548  ?  376  VAL B CA  1 
ATOM   661  C  C   . VAL A 1 99  ? 32.71500  -19.12800 1.34700   1.000 63.16172  ?  376  VAL B C   1 
ATOM   662  O  O   . VAL A 1 99  ? 31.55700  -18.93900 0.95900   1.000 65.67535  ?  376  VAL B O   1 
ATOM   663  C  CB  . VAL A 1 99  ? 33.49400  -21.40400 2.15000   1.000 57.80977  ?  376  VAL B CB  1 
ATOM   664  C  CG1 . VAL A 1 99  ? 32.14300  -21.46700 2.83200   1.000 56.65339  ?  376  VAL B CG1 1 
ATOM   665  C  CG2 . VAL A 1 99  ? 33.88800  -22.79500 1.66000   1.000 58.96753  ?  376  VAL B CG2 1 
ATOM   666  N  N   . ARG A 1 100 ? 33.36400  -18.22400 2.08800   1.000 57.88790  ?  377  ARG B N   1 
ATOM   667  C  CA  . ARG A 1 100 ? 32.65200  -17.02200 2.52200   1.000 60.50213  ?  377  ARG B CA  1 
ATOM   668  C  C   . ARG A 1 100 ? 32.37600  -16.08000 1.34500   1.000 62.84133  ?  377  ARG B C   1 
ATOM   669  O  O   . ARG A 1 100 ? 31.31600  -15.44200 1.29400   1.000 61.84866  ?  377  ARG B O   1 
ATOM   670  C  CB  . ARG A 1 100 ? 33.42500  -16.31600 3.63900   1.000 59.40871  ?  377  ARG B CB  1 
ATOM   671  C  CG  . ARG A 1 100 ? 33.56000  -17.16000 4.90600   1.000 58.83131  ?  377  ARG B CG  1 
ATOM   672  C  CD  . ARG A 1 100 ? 34.05000  -16.35900 6.10100   1.000 60.11966  ?  377  ARG B CD  1 
ATOM   673  N  NE  . ARG A 1 100 ? 33.09400  -15.33900 6.52100   1.000 58.94642  ?  377  ARG B NE  1 
ATOM   674  C  CZ  . ARG A 1 100 ? 32.13900  -15.53300 7.42200   1.000 58.93121  ?  377  ARG B CZ  1 
ATOM   675  N  NH1 . ARG A 1 100 ? 31.99000  -16.70000 8.03300   1.000 55.85207  ?  377  ARG B NH1 1 
ATOM   676  N  NH2 . ARG A 1 100 ? 31.30500  -14.53400 7.70900   1.000 57.06533  ?  377  ARG B NH2 1 
ATOM   677  N  N   . ARG A 1 101 ? 33.30500  -15.98800 0.38500   1.000 54.11644  ?  378  ARG B N   1 
ATOM   678  C  CA  . ARG A 1 101 ? 33.03000  -15.21200 -0.82300  1.000 59.90287  ?  378  ARG B CA  1 
ATOM   679  C  C   . ARG A 1 101 ? 31.92400  -15.84800 -1.66200  1.000 62.90944  ?  378  ARG B C   1 
ATOM   680  O  O   . ARG A 1 101 ? 31.13300  -15.13700 -2.29300  1.000 62.76564  ?  378  ARG B O   1 
ATOM   681  C  CB  . ARG A 1 101 ? 34.29500  -15.05000 -1.66800  1.000 63.61274  ?  378  ARG B CB  1 
ATOM   682  C  CG  . ARG A 1 101 ? 35.45200  -14.36200 -0.95100  1.000 65.56492  ?  378  ARG B CG  1 
ATOM   683  C  CD  . ARG A 1 101 ? 35.22000  -12.87500 -0.76800  1.000 68.18779  ?  378  ARG B CD  1 
ATOM   684  N  NE  . ARG A 1 101 ? 36.35400  -12.10400 -1.26500  1.000 78.95292  ?  378  ARG B NE  1 
ATOM   685  C  CZ  . ARG A 1 101 ? 37.24100  -11.49300 -0.49200  1.000 81.98528  ?  378  ARG B CZ  1 
ATOM   686  N  NH1 . ARG A 1 101 ? 37.14900  -11.52600 0.83200   1.000 90.54448  ?  378  ARG B NH1 1 
ATOM   687  N  NH2 . ARG A 1 101 ? 38.23900  -10.82300 -1.05700  1.000 82.55783  ?  378  ARG B NH2 1 
ATOM   688  N  N   . TYR A 1 102 ? 31.84100  -17.17800 -1.68100  1.000 62.18311  ?  379  TYR B N   1 
ATOM   689  C  CA  . TYR A 1 102 ? 30.73900  -17.82100 -2.39000  1.000 62.45610  ?  379  TYR B CA  1 
ATOM   690  C  C   . TYR A 1 102 ? 29.39500  -17.48800 -1.74200  1.000 61.35228  ?  379  TYR B C   1 
ATOM   691  O  O   . TYR A 1 102 ? 28.40100  -17.26500 -2.44700  1.000 59.69434  ?  379  TYR B O   1 
ATOM   692  C  CB  . TYR A 1 102 ? 30.97200  -19.32900 -2.44500  1.000 64.34418  ?  379  TYR B CB  1 
ATOM   693  C  CG  . TYR A 1 102 ? 29.85000  -20.13000 -3.04600  1.000 57.42166  ?  379  TYR B CG  1 
ATOM   694  C  CD1 . TYR A 1 102 ? 28.78500  -20.56400 -2.26500  1.000 56.89365  ?  379  TYR B CD1 1 
ATOM   695  C  CD2 . TYR A 1 102 ? 29.87100  -20.48600 -4.38100  1.000 61.39932  ?  379  TYR B CD2 1 
ATOM   696  C  CE1 . TYR A 1 102 ? 27.75900  -21.31100 -2.80800  1.000 59.09355  ?  379  TYR B CE1 1 
ATOM   697  C  CE2 . TYR A 1 102 ? 28.85500  -21.23500 -4.93500  1.000 63.66182  ?  379  TYR B CE2 1 
ATOM   698  C  CZ  . TYR A 1 102 ? 27.80100  -21.64700 -4.14900  1.000 62.99247  ?  379  TYR B CZ  1 
ATOM   699  O  OH  . TYR A 1 102 ? 26.78400  -22.38900 -4.71500  1.000 68.61128  ?  379  TYR B OH  1 
ATOM   700  N  N   . ALA A 1 103 ? 29.34200  -17.44500 -0.40500  1.000 56.08335  ?  380  ALA B N   1 
ATOM   701  C  CA  . ALA A 1 103 ? 28.12400  -17.00600 0.27600   1.000 58.71859  ?  380  ALA B CA  1 
ATOM   702  C  C   . ALA A 1 103 ? 27.69000  -15.62500 -0.21000  1.000 57.30015  ?  380  ALA B C   1 
ATOM   703  O  O   . ALA A 1 103 ? 26.51600  -15.40900 -0.53500  1.000 58.37862  ?  380  ALA B O   1 
ATOM   704  C  CB  . ALA A 1 103 ? 28.33400  -16.99800 1.79100   1.000 56.48169  ?  380  ALA B CB  1 
ATOM   705  N  N   . VAL A 1 104 ? 28.63100  -14.67700 -0.27200  1.000 49.94523  ?  381  VAL B N   1 
ATOM   706  C  CA  . VAL A 1 104 ? 28.30200  -13.33300 -0.73000  1.000 60.29409  ?  381  VAL B CA  1 
ATOM   707  C  C   . VAL A 1 104 ? 27.79700  -13.36100 -2.16900  1.000 60.16845  ?  381  VAL B C   1 
ATOM   708  O  O   . VAL A 1 104 ? 26.79000  -12.72400 -2.49900  1.000 56.35224  ?  381  VAL B O   1 
ATOM   709  C  CB  . VAL A 1 104 ? 29.51500  -12.40200 -0.58200  1.000 56.77672  ?  381  VAL B CB  1 
ATOM   710  C  CG1 . VAL A 1 104 ? 29.19000  -11.03100 -1.19500  1.000 56.30122  ?  381  VAL B CG1 1 
ATOM   711  C  CG2 . VAL A 1 104 ? 29.88100  -12.27900 0.86500   1.000 54.45029  ?  381  VAL B CG2 1 
ATOM   712  N  N   . ALA A 1 105 ? 28.49800  -14.09300 -3.04800  1.000 59.01920  ?  382  ALA B N   1 
ATOM   713  C  CA  . ALA A 1 105 ? 28.04600  -14.23300 -4.42900  1.000 57.92885  ?  382  ALA B CA  1 
ATOM   714  C  C   . ALA A 1 105 ? 26.61000  -14.74900 -4.50100  1.000 58.91082  ?  382  ALA B C   1 
ATOM   715  O  O   . ALA A 1 105 ? 25.80700  -14.25400 -5.29900  1.000 59.94343  ?  382  ALA B O   1 
ATOM   716  C  CB  . ALA A 1 105 ? 28.98300  -15.15800 -5.20500  1.000 61.49345  ?  382  ALA B CB  1 
ATOM   717  N  N   . ARG A 1 106 ? 26.26500  -15.75400 -3.69400  1.000 51.71482  ?  383  ARG B N   1 
ATOM   718  C  CA  . ARG A 1 106 ? 24.87500  -16.19700 -3.68800  1.000 56.98334  ?  383  ARG B CA  1 
ATOM   719  C  C   . ARG A 1 106 ? 23.94700  -15.10700 -3.14400  1.000 61.72940  ?  383  ARG B C   1 
ATOM   720  O  O   . ARG A 1 106 ? 22.83700  -14.92000 -3.65900  1.000 61.97179  ?  383  ARG B O   1 
ATOM   721  C  CB  . ARG A 1 106 ? 24.72800  -17.49400 -2.88900  1.000 64.39975  ?  383  ARG B CB  1 
ATOM   722  C  CG  . ARG A 1 106 ? 25.51100  -18.67300 -3.46200  1.000 63.76638  ?  383  ARG B CG  1 
ATOM   723  C  CD  . ARG A 1 106 ? 25.34500  -18.75900 -4.97700  1.000 64.95793  ?  383  ARG B CD  1 
ATOM   724  N  NE  . ARG A 1 106 ? 23.95600  -18.98700 -5.35800  1.000 70.98849  ?  383  ARG B NE  1 
ATOM   725  C  CZ  . ARG A 1 106 ? 23.45100  -18.73700 -6.56100  1.000 75.72686  ?  383  ARG B CZ  1 
ATOM   726  N  NH1 . ARG A 1 106 ? 24.18800  -18.21800 -7.53200  1.000 71.97384  ?  383  ARG B NH1 1 
ATOM   727  N  NH2 . ARG A 1 106 ? 22.16900  -19.00300 -6.79400  1.000 74.57289  ?  383  ARG B NH2 1 
ATOM   728  N  N   . LEU A 1 107 ? 24.38700  -14.36600 -2.11500  1.000 58.41277  ?  384  LEU B N   1 
ATOM   729  C  CA  . LEU A 1 107 ? 23.57900  -13.26900 -1.57500  1.000 58.00072  ?  384  LEU B CA  1 
ATOM   730  C  C   . LEU A 1 107 ? 23.27400  -12.20500 -2.61700  1.000 57.80555  ?  384  LEU B C   1 
ATOM   731  O  O   . LEU A 1 107 ? 22.21400  -11.56800 -2.56800  1.000 62.68948  ?  384  LEU B O   1 
ATOM   732  C  CB  . LEU A 1 107 ? 24.29700  -12.60600 -0.40700  1.000 58.93733  ?  384  LEU B CB  1 
ATOM   733  C  CG  . LEU A 1 107 ? 23.81500  -13.01500 0.96800   1.000 61.59537  ?  384  LEU B CG  1 
ATOM   734  C  CD1 . LEU A 1 107 ? 24.38300  -12.04100 1.98300   1.000 60.68639  ?  384  LEU B CD1 1 
ATOM   735  C  CD2 . LEU A 1 107 ? 22.29700  -13.03400 0.97100   1.000 62.82066  ?  384  LEU B CD2 1 
ATOM   736  N  N   . ARG A 1 108 ? 24.20600  -11.96800 -3.53700  1.000 59.20472  ?  385  ARG B N   1 
ATOM   737  C  CA  . ARG A 1 108 ? 23.98600  -10.98600 -4.58400  1.000 64.41414  ?  385  ARG B CA  1 
ATOM   738  C  C   . ARG A 1 108 ? 22.73300  -11.28600 -5.40900  1.000 63.67090  ?  385  ARG B C   1 
ATOM   739  O  O   . ARG A 1 108 ? 22.20100  -10.37400 -6.05000  1.000 66.45439  ?  385  ARG B O   1 
ATOM   740  C  CB  . ARG A 1 108 ? 25.22900  -10.91700 -5.47700  1.000 64.78534  ?  385  ARG B CB  1 
ATOM   741  C  CG  . ARG A 1 108 ? 25.78400  -9.51100  -5.66100  1.000 72.05069  ?  385  ARG B CG  1 
ATOM   742  C  CD  . ARG A 1 108 ? 27.02600  -9.47900  -6.55000  1.000 68.07100  ?  385  ARG B CD  1 
ATOM   743  N  NE  . ARG A 1 108 ? 28.21500  -9.86200  -5.80600  1.000 73.16487  ?  385  ARG B NE  1 
ATOM   744  C  CZ  . ARG A 1 108 ? 29.10600  -10.74800 -6.22900  1.000 82.97943  ?  385  ARG B CZ  1 
ATOM   745  N  NH1 . ARG A 1 108 ? 28.97700  -11.35100 -7.40300  1.000 87.08042  ?  385  ARG B NH1 1 
ATOM   746  N  NH2 . ARG A 1 108 ? 30.16300  -11.02600 -5.46200  1.000 79.49042  ?  385  ARG B NH2 1 
ATOM   747  N  N   . GLN A 1 109 ? 22.25400  -12.53900 -5.40900  1.000 61.15561  ?  386  GLN B N   1 
ATOM   748  C  CA  . GLN A 1 109 ? 21.06800  -12.91400 -6.17800  1.000 62.10222  ?  386  GLN B CA  1 
ATOM   749  C  C   . GLN A 1 109 ? 19.77100  -12.50900 -5.49500  1.000 59.04000  ?  386  GLN B C   1 
ATOM   750  O  O   . GLN A 1 109 ? 18.73200  -12.44400 -6.15600  1.000 64.91673  ?  386  GLN B O   1 
ATOM   751  C  CB  . GLN A 1 109 ? 21.04500  -14.42500 -6.42500  1.000 67.69472  ?  386  GLN B CB  1 
ATOM   752  C  CG  . GLN A 1 109 ? 22.35500  -15.00700 -6.94200  1.000 67.80978  ?  386  GLN B CG  1 
ATOM   753  C  CD  . GLN A 1 109 ? 22.76400  -14.43000 -8.28100  1.000 70.62515  ?  386  GLN B CD  1 
ATOM   754  O  OE1 . GLN A 1 109 ? 21.93100  -14.23900 -9.16600  1.000 71.29653  ?  386  GLN B OE1 1 
ATOM   755  N  NE2 . GLN A 1 109 ? 24.05500  -14.13700 -8.43300  1.000 76.52375  ?  386  GLN B NE2 1 
ATOM   756  N  N   . ALA A 1 110 ? 19.80500  -12.25200 -4.19700  1.000 58.52607  ?  387  ALA B N   1 
ATOM   757  C  CA  . ALA A 1 110 ? 18.64200  -11.74400 -3.48400  1.000 60.29397  ?  387  ALA B CA  1 
ATOM   758  C  C   . ALA A 1 110 ? 18.28200  -10.33600 -3.94600  1.000 58.53252  ?  387  ALA B C   1 
ATOM   759  O  O   . ALA A 1 110 ? 19.15800  -9.50200  -4.18800  1.000 58.22534  ?  387  ALA B O   1 
ATOM   760  C  CB  . ALA A 1 110 ? 18.92500  -11.72600 -1.98200  1.000 58.24460  ?  387  ALA B CB  1 
ATOM   761  N  N   . ASP A 1 111 ? 16.98800  -10.05300 -4.04300  1.000 53.78150  ?  388  ASP B N   1 
ATOM   762  C  CA  . ASP A 1 111 ? 16.62100  -8.66200  -4.25200  1.000 57.25827  ?  388  ASP B CA  1 
ATOM   763  C  C   . ASP A 1 111 ? 16.61500  -7.90600  -2.92500  1.000 56.58968  ?  388  ASP B C   1 
ATOM   764  O  O   . ASP A 1 111 ? 16.76700  -8.47500  -1.83900  1.000 54.51835  ?  388  ASP B O   1 
ATOM   765  C  CB  . ASP A 1 111 ? 15.26600  -8.54400  -4.93700  1.000 68.38074  ?  388  ASP B CB  1 
ATOM   766  C  CG  . ASP A 1 111 ? 14.17700  -9.20500  -4.15200  1.000 75.30860  ?  388  ASP B CG  1 
ATOM   767  O  OD1 . ASP A 1 111 ? 14.52800  -10.03700 -3.28700  1.000 80.63041  ?  388  ASP B OD1 1 
ATOM   768  O  OD2 . ASP A 1 111 ? 12.98400  -8.91100  -4.40100  1.000 91.41011  -1 388  ASP B OD2 1 
ATOM   769  N  N   . ASP A 1 112 ? 16.42800  -6.59400  -3.01800  1.000 58.02618  ?  389  ASP B N   1 
ATOM   770  C  CA  . ASP A 1 112 ? 16.66000  -5.75400  -1.85300  1.000 56.20595  ?  389  ASP B CA  1 
ATOM   771  C  C   . ASP A 1 112 ? 15.60700  -5.95400  -0.76300  1.000 54.29893  ?  389  ASP B C   1 
ATOM   772  O  O   . ASP A 1 112 ? 15.92200  -5.80900  0.42000   1.000 55.07413  ?  389  ASP B O   1 
ATOM   773  C  CB  . ASP A 1 112 ? 16.76700  -4.29100  -2.28800  1.000 54.08774  ?  389  ASP B CB  1 
ATOM   774  C  CG  . ASP A 1 112 ? 18.18500  -3.93300  -2.75400  1.000 56.98761  ?  389  ASP B CG  1 
ATOM   775  O  OD1 . ASP A 1 112 ? 19.10000  -4.77900  -2.60100  1.000 53.49085  ?  389  ASP B OD1 1 
ATOM   776  O  OD2 . ASP A 1 112 ? 18.38800  -2.81000  -3.27300  1.000 61.89088  -1 389  ASP B OD2 1 
ATOM   777  N  N   . GLU A 1 113 ? 14.36800  -6.29600  -1.11800  1.000 55.52272  ?  390  GLU B N   1 
ATOM   778  C  CA  . GLU A 1 113 ? 13.37800  -6.59800  -0.08900  1.000 49.39365  ?  390  GLU B CA  1 
ATOM   779  C  C   . GLU A 1 113 ? 13.82600  -7.77700  0.78200   1.000 59.40600  ?  390  GLU B C   1 
ATOM   780  O  O   . GLU A 1 113 ? 13.71300  -7.72700  2.01400   1.000 62.00593  ?  390  GLU B O   1 
ATOM   781  C  CB  . GLU A 1 113 ? 12.01200  -6.87200  -0.72600  1.000 48.34940  ?  390  GLU B CB  1 
ATOM   782  N  N   . ASP A 1 114 ? 14.35700  -8.84000  0.17200   1.000 54.12554  ?  391  ASP B N   1 
ATOM   783  C  CA  . ASP A 1 114 ? 14.84400  -9.96100  0.97200   1.000 50.57605  ?  391  ASP B CA  1 
ATOM   784  C  C   . ASP A 1 114 ? 16.08900  -9.57400  1.75600   1.000 53.68298  ?  391  ASP B C   1 
ATOM   785  O  O   . ASP A 1 114 ? 16.21300  -9.86800  2.95800   1.000 47.42482  ?  391  ASP B O   1 
ATOM   786  C  CB  . ASP A 1 114 ? 15.13100  -11.15700 0.07600   1.000 53.28392  ?  391  ASP B CB  1 
ATOM   787  C  CG  . ASP A 1 114 ? 13.87400  -11.72300 -0.52400  1.000 63.83541  ?  391  ASP B CG  1 
ATOM   788  O  OD1 . ASP A 1 114 ? 12.78800  -11.33100 -0.04300  1.000 62.53557  ?  391  ASP B OD1 1 
ATOM   789  O  OD2 . ASP A 1 114 ? 13.96500  -12.53700 -1.46800  1.000 64.26237  -1 391  ASP B OD2 1 
ATOM   790  N  N   . LEU A 1 115 ? 17.02600  -8.91300  1.08800   1.000 49.70743  ?  392  LEU B N   1 
ATOM   791  C  CA  . LEU A 1 115 ? 18.25700  -8.50600  1.74300   1.000 50.24694  ?  392  LEU B CA  1 
ATOM   792  C  C   . LEU A 1 115 ? 17.95700  -7.68400  2.99500   1.000 48.61573  ?  392  LEU B C   1 
ATOM   793  O  O   . LEU A 1 115 ? 18.47000  -7.97300  4.07900   1.000 50.84850  ?  392  LEU B O   1 
ATOM   794  C  CB  . LEU A 1 115 ? 19.10400  -7.73100  0.74000   1.000 46.97712  ?  392  LEU B CB  1 
ATOM   795  C  CG  . LEU A 1 115 ? 20.51500  -7.35400  1.10700   1.000 50.81880  ?  392  LEU B CG  1 
ATOM   796  C  CD1 . LEU A 1 115 ? 21.17700  -8.57000  1.67500   1.000 57.56172  ?  392  LEU B CD1 1 
ATOM   797  C  CD2 . LEU A 1 115 ? 21.16500  -6.93900  -0.19600  1.000 57.81879  ?  392  LEU B CD2 1 
ATOM   798  N  N   . LEU A 1 116 ? 17.07500  -6.68800  2.87100   1.000 48.97396  ?  393  LEU B N   1 
ATOM   799  C  CA  . LEU A 1 116 ? 16.70200  -5.86200  4.01800   1.000 52.68684  ?  393  LEU B CA  1 
ATOM   800  C  C   . LEU A 1 116 ? 16.20600  -6.70500  5.20000   1.000 52.01600  ?  393  LEU B C   1 
ATOM   801  O  O   . LEU A 1 116 ? 16.52700  -6.40600  6.35800   1.000 44.59810  ?  393  LEU B O   1 
ATOM   802  C  CB  . LEU A 1 116 ? 15.64500  -4.82700  3.59900   1.000 43.06379  ?  393  LEU B CB  1 
ATOM   803  C  CG  . LEU A 1 116 ? 15.30700  -3.73200  4.61900   1.000 56.29227  ?  393  LEU B CG  1 
ATOM   804  C  CD1 . LEU A 1 116 ? 16.53500  -2.90900  4.98100   1.000 51.97726  ?  393  LEU B CD1 1 
ATOM   805  C  CD2 . LEU A 1 116 ? 14.19800  -2.82500  4.08800   1.000 61.14167  ?  393  LEU B CD2 1 
ATOM   806  N  N   . MET A 1 117 ? 15.45700  -7.77100  4.93000   1.000 47.26741  ?  394  MET B N   1 
ATOM   807  C  CA  A MET A 1 117 ? 14.95700  -8.62100  6.00400   0.804 47.14839  ?  394  MET B CA  1 
ATOM   808  C  CA  B MET A 1 117 ? 14.95800  -8.62000  6.00700   0.196 46.75964  ?  394  MET B CA  1 
ATOM   809  C  C   . MET A 1 117 ? 16.05800  -9.41100  6.69800   1.000 51.60389  ?  394  MET B C   1 
ATOM   810  O  O   . MET A 1 117 ? 15.82000  -9.95900  7.78000   1.000 49.52451  ?  394  MET B O   1 
ATOM   811  C  CB  A MET A 1 117 ? 13.89400  -9.57300  5.45400   0.804 46.04654  ?  394  MET B CB  1 
ATOM   812  C  CB  B MET A 1 117 ? 13.89400  -9.57600  5.46700   0.196 46.26120  ?  394  MET B CB  1 
ATOM   813  C  CG  A MET A 1 117 ? 12.59600  -8.87800  5.06500   0.804 57.57430  ?  394  MET B CG  1 
ATOM   814  C  CG  B MET A 1 117 ? 12.60800  -8.88100  5.07300   0.196 57.39994  ?  394  MET B CG  1 
ATOM   815  S  SD  . MET A 1 117 ? 11.95400  -7.80300  6.36700   1.000 80.85347  ?  394  MET B SD  1 
ATOM   816  C  CE  . MET A 1 117 ? 11.83700  -8.94400  7.74700   1.000 59.66150  ?  394  MET B CE  1 
ATOM   817  N  N   . TYR A 1 118 ? 17.24500  -9.49500  6.10200   1.000 46.84079  ?  395  TYR B N   1 
ATOM   818  C  CA  . TYR A 1 118 ? 18.37100  -10.19300 6.72200   1.000 45.45672  ?  395  TYR B CA  1 
ATOM   819  C  C   . TYR A 1 118 ? 19.41500  -9.23900  7.26800   1.000 41.83981  ?  395  TYR B C   1 
ATOM   820  O  O   . TYR A 1 118 ? 20.38800  -9.69900  7.87700   1.000 42.98684  ?  395  TYR B O   1 
ATOM   821  C  CB  . TYR A 1 118 ? 19.06300  -11.15900 5.72200   1.000 46.52631  ?  395  TYR B CB  1 
ATOM   822  C  CG  . TYR A 1 118 ? 18.12000  -12.02000 4.91100   1.000 47.42447  ?  395  TYR B CG  1 
ATOM   823  C  CD1 . TYR A 1 118 ? 16.95400  -12.53000 5.47200   1.000 50.24591  ?  395  TYR B CD1 1 
ATOM   824  C  CD2 . TYR A 1 118 ? 18.37500  -12.28600 3.57800   1.000 49.91979  ?  395  TYR B CD2 1 
ATOM   825  C  CE1 . TYR A 1 118 ? 16.07100  -13.29200 4.72400   1.000 51.45652  ?  395  TYR B CE1 1 
ATOM   826  C  CE2 . TYR A 1 118 ? 17.50200  -13.03700 2.81800   1.000 50.94272  ?  395  TYR B CE2 1 
ATOM   827  C  CZ  . TYR A 1 118 ? 16.35200  -13.54500 3.39800   1.000 53.58702  ?  395  TYR B CZ  1 
ATOM   828  O  OH  . TYR A 1 118 ? 15.48200  -14.30400 2.64700   1.000 61.83533  ?  395  TYR B OH  1 
ATOM   829  N  N   . LEU A 1 119 ? 19.23400  -7.93200  7.07300   1.000 38.41889  ?  396  LEU B N   1 
ATOM   830  C  CA  . LEU A 1 119 ? 20.34200  -6.99900  7.26200   1.000 39.72307  ?  396  LEU B CA  1 
ATOM   831  C  C   . LEU A 1 119 ? 20.83800  -6.99100  8.70100   1.000 41.22585  ?  396  LEU B C   1 
ATOM   832  O  O   . LEU A 1 119 ? 22.04500  -6.94900  8.94600   1.000 42.89894  ?  396  LEU B O   1 
ATOM   833  C  CB  . LEU A 1 119 ? 19.94200  -5.57900  6.84600   1.000 40.75132  ?  396  LEU B CB  1 
ATOM   834  C  CG  . LEU A 1 119 ? 21.13300  -4.62100  6.77200   1.000 41.30121  ?  396  LEU B CG  1 
ATOM   835  C  CD1 . LEU A 1 119 ? 22.17900  -5.16000  5.79500   1.000 40.65352  ?  396  LEU B CD1 1 
ATOM   836  C  CD2 . LEU A 1 119 ? 20.70800  -3.24900  6.33900   1.000 43.82636  ?  396  LEU B CD2 1 
ATOM   837  N  N   A LEU A 1 120 ? 19.92300  -7.00700  9.67000   0.611 43.93074  ?  397  LEU B N   1 
ATOM   838  N  N   B LEU A 1 120 ? 19.92300  -7.00600  9.66800   0.389 42.82387  ?  397  LEU B N   1 
ATOM   839  C  CA  A LEU A 1 120 ? 20.34800  -7.00900  11.06300  0.611 43.36426  ?  397  LEU B CA  1 
ATOM   840  C  CA  B LEU A 1 120 ? 20.35800  -7.00700  11.05700  0.389 42.69034  ?  397  LEU B CA  1 
ATOM   841  C  C   A LEU A 1 120 ? 21.31100  -8.16000  11.34000  0.611 45.36050  ?  397  LEU B C   1 
ATOM   842  C  C   B LEU A 1 120 ? 21.32500  -8.15800  11.32100  0.389 45.35451  ?  397  LEU B C   1 
ATOM   843  O  O   A LEU A 1 120 ? 22.33200  -7.97600  12.01500  0.611 45.47901  ?  397  LEU B O   1 
ATOM   844  O  O   B LEU A 1 120 ? 22.35600  -7.97300  11.98000  0.389 45.48331  ?  397  LEU B O   1 
ATOM   845  C  CB  A LEU A 1 120 ? 19.12700  -7.07600  11.98200  0.611 44.78224  ?  397  LEU B CB  1 
ATOM   846  C  CB  B LEU A 1 120 ? 19.14600  -7.07200  11.98800  0.389 44.84907  ?  397  LEU B CB  1 
ATOM   847  C  CG  A LEU A 1 120 ? 19.31500  -7.01800  13.49700  0.611 45.81805  ?  397  LEU B CG  1 
ATOM   848  C  CG  B LEU A 1 120 ? 19.42100  -6.86600  13.47700  0.389 45.76693  ?  397  LEU B CG  1 
ATOM   849  C  CD1 A LEU A 1 120 ? 19.87100  -5.67100  13.95000  0.611 44.85735  ?  397  LEU B CD1 1 
ATOM   850  C  CD1 B LEU A 1 120 ? 18.12500  -6.60600  14.23500  0.389 44.82513  ?  397  LEU B CD1 1 
ATOM   851  C  CD2 A LEU A 1 120 ? 17.97900  -7.30200  14.17100  0.611 44.01349  ?  397  LEU B CD2 1 
ATOM   852  C  CD2 B LEU A 1 120 ? 20.13700  -8.07300  14.04800  0.389 43.93262  ?  397  LEU B CD2 1 
ATOM   853  N  N   . GLN A 1 121 ? 21.02000  -9.34900  10.79600  1.000 49.13032  ?  398  GLN B N   1 
ATOM   854  C  CA  . GLN A 1 121 ? 21.89000  -10.50300 11.02100  1.000 44.88789  ?  398  GLN B CA  1 
ATOM   855  C  C   . GLN A 1 121 ? 23.18700  -10.39300 10.22600  1.000 50.38150  ?  398  GLN B C   1 
ATOM   856  O  O   . GLN A 1 121 ? 24.25600  -10.79500 10.71300  1.000 50.04845  ?  398  GLN B O   1 
ATOM   857  C  CB  . GLN A 1 121 ? 21.16800  -11.80000 10.66600  1.000 44.59745  ?  398  GLN B CB  1 
ATOM   858  C  CG  . GLN A 1 121 ? 20.14000  -12.22300 11.68000  1.000 41.28835  ?  398  GLN B CG  1 
ATOM   859  C  CD  . GLN A 1 121 ? 18.81600  -11.48300 11.52300  1.000 49.16819  ?  398  GLN B CD  1 
ATOM   860  O  OE1 . GLN A 1 121 ? 18.53700  -10.85700 10.48000  1.000 49.94366  ?  398  GLN B OE1 1 
ATOM   861  N  NE2 . GLN A 1 121 ? 17.98700  -11.55600 12.55400  1.000 49.56128  ?  398  GLN B NE2 1 
ATOM   862  N  N   . LEU A 1 122 ? 23.11400  -9.87000  8.99400   1.000 44.12975  ?  399  LEU B N   1 
ATOM   863  C  CA  . LEU A 1 122 ? 24.32600  -9.73500  8.19000   1.000 47.75132  ?  399  LEU B CA  1 
ATOM   864  C  C   . LEU A 1 122 ? 25.31700  -8.78100  8.84100   1.000 46.66827  ?  399  LEU B C   1 
ATOM   865  O  O   . LEU A 1 122 ? 26.53300  -8.98700  8.74700   1.000 52.98658  ?  399  LEU B O   1 
ATOM   866  C  CB  . LEU A 1 122 ? 23.97200  -9.26100  6.77700   1.000 43.91640  ?  399  LEU B CB  1 
ATOM   867  C  CG  . LEU A 1 122 ? 23.22500  -10.28900 5.91400   1.000 43.59160  ?  399  LEU B CG  1 
ATOM   868  C  CD1 . LEU A 1 122 ? 22.71100  -9.69400  4.59400   1.000 40.26787  ?  399  LEU B CD1 1 
ATOM   869  C  CD2 . LEU A 1 122 ? 24.08500  -11.52000 5.65200   1.000 44.43561  ?  399  LEU B CD2 1 
ATOM   870  N  N   . VAL A 1 123 ? 24.82000  -7.74900  9.52300   1.000 43.70256  ?  400  VAL B N   1 
ATOM   871  C  CA  . VAL A 1 123 ? 25.70100  -6.82500  10.22400  1.000 48.17753  ?  400  VAL B CA  1 
ATOM   872  C  C   . VAL A 1 123 ? 26.41000  -7.53000  11.37800  1.000 50.70653  ?  400  VAL B C   1 
ATOM   873  O  O   . VAL A 1 123 ? 27.57400  -7.23200  11.67600  1.000 48.04501  ?  400  VAL B O   1 
ATOM   874  C  CB  . VAL A 1 123 ? 24.90800  -5.58500  10.69900  1.000 45.58249  ?  400  VAL B CB  1 
ATOM   875  C  CG1 . VAL A 1 123 ? 25.65600  -4.83200  11.80100  1.000 41.02982  ?  400  VAL B CG1 1 
ATOM   876  C  CG2 . VAL A 1 123 ? 24.59900  -4.66000  9.51200   1.000 35.55726  ?  400  VAL B CG2 1 
ATOM   877  N  N   . GLN A 1 124 ? 25.72100  -8.44500  12.07200  1.000 45.14301  ?  401  GLN B N   1 
ATOM   878  C  CA  . GLN A 1 124 ? 26.39600  -9.23600  13.10000  1.000 45.91185  ?  401  GLN B CA  1 
ATOM   879  C  C   . GLN A 1 124 ? 27.42900  -10.17600 12.48700  1.000 53.83155  ?  401  GLN B C   1 
ATOM   880  O  O   . GLN A 1 124 ? 28.47100  -10.43900 13.09900  1.000 53.47492  ?  401  GLN B O   1 
ATOM   881  C  CB  . GLN A 1 124 ? 25.38700  -10.04900 13.90400  1.000 48.77397  ?  401  GLN B CB  1 
ATOM   882  C  CG  . GLN A 1 124 ? 24.41200  -9.21700  14.70700  1.000 47.54666  ?  401  GLN B CG  1 
ATOM   883  C  CD  . GLN A 1 124 ? 25.09200  -8.40300  15.79200  1.000 50.00501  ?  401  GLN B CD  1 
ATOM   884  O  OE1 . GLN A 1 124 ? 25.88700  -8.91100  16.58600  1.000 53.21424  ?  401  GLN B OE1 1 
ATOM   885  N  NE2 . GLN A 1 124 ? 24.78600  -7.12100  15.81900  1.000 57.27441  ?  401  GLN B NE2 1 
ATOM   886  N  N   . ALA A 1 125 ? 27.16600  -10.68200 11.27700  1.000 50.82975  ?  402  ALA B N   1 
ATOM   887  C  CA  . ALA A 1 125 ? 28.08700  -11.62300 10.66500  1.000 52.93219  ?  402  ALA B CA  1 
ATOM   888  C  C   . ALA A 1 125 ? 29.41900  -10.97700 10.31000  1.000 55.03165  ?  402  ALA B C   1 
ATOM   889  O  O   . ALA A 1 125 ? 30.39300  -11.69500 10.06800  1.000 53.50126  ?  402  ALA B O   1 
ATOM   890  C  CB  . ALA A 1 125 ? 27.45100  -12.24900 9.42500   1.000 49.03454  ?  402  ALA B CB  1 
ATOM   891  N  N   . LEU A 1 126 ? 29.49500  -9.64500  10.28500  1.000 49.69273  ?  403  LEU B N   1 
ATOM   892  C  CA  . LEU A 1 126 ? 30.78600  -9.01500  10.04200  1.000 49.72605  ?  403  LEU B CA  1 
ATOM   893  C  C   . LEU A 1 126 ? 31.80500  -9.38400  11.11500  1.000 52.49186  ?  403  LEU B C   1 
ATOM   894  O  O   . LEU A 1 126 ? 33.01300  -9.31500  10.85200  1.000 55.88921  ?  403  LEU B O   1 
ATOM   895  C  CB  . LEU A 1 126 ? 30.61300  -7.49600  9.93200   1.000 47.77275  ?  403  LEU B CB  1 
ATOM   896  C  CG  . LEU A 1 126 ? 29.77900  -7.02500  8.72700   1.000 47.22710  ?  403  LEU B CG  1 
ATOM   897  C  CD1 . LEU A 1 126 ? 29.27000  -5.59900  8.94000   1.000 43.30154  ?  403  LEU B CD1 1 
ATOM   898  C  CD2 . LEU A 1 126 ? 30.59100  -7.12600  7.42500   1.000 44.82951  ?  403  LEU B CD2 1 
ATOM   899  N  N   . LYS A 1 127 ? 31.34900  -9.78000  12.31600  1.000 49.20582  ?  404  LYS B N   1 
ATOM   900  C  CA  . LYS A 1 127 ? 32.27300  -10.31700 13.31300  1.000 53.89866  ?  404  LYS B CA  1 
ATOM   901  C  C   . LYS A 1 127 ? 33.08600  -11.48100 12.74800  1.000 56.39325  ?  404  LYS B C   1 
ATOM   902  O  O   . LYS A 1 127 ? 34.20700  -11.72300 13.19300  1.000 57.59588  ?  404  LYS B O   1 
ATOM   903  C  CB  . LYS A 1 127 ? 31.52000  -10.78800 14.56800  1.000 47.57956  ?  404  LYS B CB  1 
ATOM   904  C  CG  . LYS A 1 127 ? 30.78700  -9.71600  15.37000  1.000 54.41793  ?  404  LYS B CG  1 
ATOM   905  C  CD  . LYS A 1 127 ? 29.92100  -10.37800 16.44000  1.000 53.04028  ?  404  LYS B CD  1 
ATOM   906  C  CE  . LYS A 1 127 ? 28.69600  -9.54500  16.79000  1.000 62.01336  ?  404  LYS B CE  1 
ATOM   907  N  NZ  . LYS A 1 127 ? 28.98500  -8.33300  17.66000  1.000 64.77275  ?  404  LYS B NZ  1 
ATOM   908  N  N   . TYR A 1 128 ? 32.53200  -12.22600 11.79200  1.000 56.17516  ?  405  TYR B N   1 
ATOM   909  C  CA  . TYR A 1 128 ? 33.15500  -13.44600 11.29200  1.000 56.23256  ?  405  TYR B CA  1 
ATOM   910  C  C   . TYR A 1 128 ? 33.93100  -13.21300 10.00800  1.000 59.72621  ?  405  TYR B C   1 
ATOM   911  O  O   . TYR A 1 128 ? 34.43900  -14.17500 9.42400   1.000 63.04175  ?  405  TYR B O   1 
ATOM   912  C  CB  . TYR A 1 128 ? 32.09200  -14.52900 11.06900  1.000 56.57077  ?  405  TYR B CB  1 
ATOM   913  C  CG  . TYR A 1 128 ? 31.16400  -14.65100 12.24500  1.000 58.07920  ?  405  TYR B CG  1 
ATOM   914  C  CD1 . TYR A 1 128 ? 31.67200  -14.75000 13.53900  1.000 53.40112  ?  405  TYR B CD1 1 
ATOM   915  C  CD2 . TYR A 1 128 ? 29.78000  -14.60400 12.07600  1.000 55.24681  ?  405  TYR B CD2 1 
ATOM   916  C  CE1 . TYR A 1 128 ? 30.83500  -14.84100 14.62300  1.000 53.45330  ?  405  TYR B CE1 1 
ATOM   917  C  CE2 . TYR A 1 128 ? 28.93200  -14.68600 13.15900  1.000 55.09664  ?  405  TYR B CE2 1 
ATOM   918  C  CZ  . TYR A 1 128 ? 29.46800  -14.80500 14.43300  1.000 57.06797  ?  405  TYR B CZ  1 
ATOM   919  O  OH  . TYR A 1 128 ? 28.64200  -14.89600 15.52900  1.000 55.72323  ?  405  TYR B OH  1 
ATOM   920  N  N   . GLU A 1 129 ? 34.02600  -11.96900 9.55700   1.000 57.51769  ?  406  GLU B N   1 
ATOM   921  C  CA  . GLU A 1 129 ? 34.78900  -11.63300 8.37000   1.000 58.55384  ?  406  GLU B CA  1 
ATOM   922  C  C   . GLU A 1 129 ? 36.23800  -11.33600 8.75200   1.000 62.39105  ?  406  GLU B C   1 
ATOM   923  O  O   . GLU A 1 129 ? 36.61100  -11.31200 9.92900   1.000 64.60766  ?  406  GLU B O   1 
ATOM   924  C  CB  . GLU A 1 129 ? 34.15400  -10.44300 7.65300   1.000 54.19789  ?  406  GLU B CB  1 
ATOM   925  C  CG  . GLU A 1 129 ? 32.80400  -10.77500 6.99900   1.000 55.59391  ?  406  GLU B CG  1 
ATOM   926  C  CD  . GLU A 1 129 ? 32.94300  -11.57000 5.69000   1.000 59.47346  ?  406  GLU B CD  1 
ATOM   927  O  OE1 . GLU A 1 129 ? 33.50500  -11.01900 4.70800   1.000 57.33655  ?  406  GLU B OE1 1 
ATOM   928  O  OE2 . GLU A 1 129 ? 32.49000  -12.74500 5.64600   1.000 59.62754  -1 406  GLU B OE2 1 
ATOM   929  N  N   . ASN A 1 130 ? 37.05400  -11.11400 7.73000   1.000 65.85562  ?  407  ASN B N   1 
ATOM   930  C  CA  . ASN A 1 130 ? 38.45800  -10.77200 7.90400   1.000 65.00679  ?  407  ASN B CA  1 
ATOM   931  C  C   . ASN A 1 130 ? 38.57400  -9.28600  8.23700   1.000 65.72809  ?  407  ASN B C   1 
ATOM   932  O  O   . ASN A 1 130 ? 38.21300  -8.42800  7.42000   1.000 72.55368  ?  407  ASN B O   1 
ATOM   933  C  CB  . ASN A 1 130 ? 39.23700  -11.12700 6.63800   1.000 64.20452  ?  407  ASN B CB  1 
ATOM   934  C  CG  . ASN A 1 130 ? 40.72400  -10.92200 6.79600   1.000 71.78034  ?  407  ASN B CG  1 
ATOM   935  O  OD1 . ASN A 1 130 ? 41.19200  -9.82900  7.14100   1.000 71.73471  ?  407  ASN B OD1 1 
ATOM   936  N  ND2 . ASN A 1 130 ? 41.48300  -11.98500 6.57000   1.000 74.45568  ?  407  ASN B ND2 1 
ATOM   937  N  N   . PHE A 1 131 ? 39.07000  -8.98100  9.43500   1.000 66.08042  ?  408  PHE B N   1 
ATOM   938  C  CA  . PHE A 1 131 ? 39.13300  -7.59800  9.89300   1.000 62.31423  ?  408  PHE B CA  1 
ATOM   939  C  C   . PHE A 1 131 ? 40.18500  -6.79700  9.14100   1.000 66.47614  ?  408  PHE B C   1 
ATOM   940  O  O   . PHE A 1 131 ? 40.01100  -5.58700  8.94800   1.000 68.93743  ?  408  PHE B O   1 
ATOM   941  C  CB  . PHE A 1 131 ? 39.41500  -7.54800  11.40000  1.000 64.68497  ?  408  PHE B CB  1 
ATOM   942  C  CG  . PHE A 1 131 ? 38.27300  -8.04100  12.25700  1.000 62.43298  ?  408  PHE B CG  1 
ATOM   943  C  CD1 . PHE A 1 131 ? 37.12000  -8.56200  11.68000  1.000 63.52855  ?  408  PHE B CD1 1 
ATOM   944  C  CD2 . PHE A 1 131 ? 38.35400  -7.98300  13.63800  1.000 62.21625  ?  408  PHE B CD2 1 
ATOM   945  C  CE1 . PHE A 1 131 ? 36.07700  -9.02000  12.46500  1.000 59.90505  ?  408  PHE B CE1 1 
ATOM   946  C  CE2 . PHE A 1 131 ? 37.30900  -8.44000  14.42800  1.000 60.84417  ?  408  PHE B CE2 1 
ATOM   947  C  CZ  . PHE A 1 131 ? 36.17400  -8.95800  13.84400  1.000 56.60089  ?  408  PHE B CZ  1 
ATOM   948  N  N   . ASP A 1 132 ? 41.28000  -7.44300  8.72400   1.000 65.30380  ?  409  ASP B N   1 
ATOM   949  C  CA  . ASP A 1 132 ? 42.32900  -6.73700  7.99000   1.000 72.18291  ?  409  ASP B CA  1 
ATOM   950  C  C   . ASP A 1 132 ? 41.84700  -6.27900  6.62100   1.000 72.24957  ?  409  ASP B C   1 
ATOM   951  O  O   . ASP A 1 132 ? 42.15800  -5.16100  6.19800   1.000 70.10473  ?  409  ASP B O   1 
ATOM   952  C  CB  . ASP A 1 132 ? 43.55700  -7.62400  7.83000   1.000 74.40954  ?  409  ASP B CB  1 
ATOM   953  C  CG  . ASP A 1 132 ? 44.37200  -7.72000  9.09700   1.000 84.86753  ?  409  ASP B CG  1 
ATOM   954  O  OD1 . ASP A 1 132 ? 44.36800  -6.74500  9.88000   1.000 84.44344  ?  409  ASP B OD1 1 
ATOM   955  O  OD2 . ASP A 1 132 ? 45.02100  -8.77000  9.30500   1.000 96.11266  -1 409  ASP B OD2 1 
ATOM   956  N  N   . ASP A 1 133 ? 41.10500  -7.13700  5.90700   1.000 71.13873  ?  410  ASP B N   1 
ATOM   957  C  CA  . ASP A 1 133 ? 40.51500  -6.73100  4.63200   1.000 69.71400  ?  410  ASP B CA  1 
ATOM   958  C  C   . ASP A 1 133 ? 39.64900  -5.49400  4.80400   1.000 67.29934  ?  410  ASP B C   1 
ATOM   959  O  O   . ASP A 1 133 ? 39.75300  -4.53200  4.02900   1.000 62.73008  ?  410  ASP B O   1 
ATOM   960  C  CB  . ASP A 1 133 ? 39.67600  -7.86200  4.03800   1.000 66.19776  ?  410  ASP B CB  1 
ATOM   961  C  CG  . ASP A 1 133 ? 40.46700  -9.12400  3.82000   1.000 74.93259  ?  410  ASP B CG  1 
ATOM   962  O  OD1 . ASP A 1 133 ? 41.70500  -9.03300  3.63300   1.000 73.00518  ?  410  ASP B OD1 1 
ATOM   963  O  OD2 . ASP A 1 133 ? 39.83900  -10.20800 3.83200   1.000 83.12662  -1 410  ASP B OD2 1 
ATOM   964  N  N   . ILE A 1 134 ? 38.77100  -5.51400  5.80900   1.000 64.42740  ?  411  ILE B N   1 
ATOM   965  C  CA  . ILE A 1 134 ? 37.89800  -4.37400  6.05400   1.000 65.36280  ?  411  ILE B CA  1 
ATOM   966  C  C   . ILE A 1 134 ? 38.73400  -3.12200  6.29000   1.000 70.04783  ?  411  ILE B C   1 
ATOM   967  O  O   . ILE A 1 134 ? 38.51000  -2.07400  5.66500   1.000 65.34125  ?  411  ILE B O   1 
ATOM   968  C  CB  . ILE A 1 134 ? 36.94900  -4.67100  7.22700   1.000 62.26699  ?  411  ILE B CB  1 
ATOM   969  C  CG1 . ILE A 1 134 ? 35.94100  -5.75700  6.81300   1.000 61.88959  ?  411  ILE B CG1 1 
ATOM   970  C  CG2 . ILE A 1 134 ? 36.25100  -3.40000  7.68100   1.000 58.11129  ?  411  ILE B CG2 1 
ATOM   971  C  CD1 . ILE A 1 134 ? 35.21600  -6.42200  7.96500   1.000 55.15460  ?  411  ILE B CD1 1 
ATOM   972  N  N   . LYS A 1 135 ? 39.73900  -3.22300  7.16200   1.000 64.18536  ?  412  LYS B N   1 
ATOM   973  C  CA  . LYS A 1 135 ? 40.60400  -2.07600  7.39600   1.000 64.79041  ?  412  LYS B CA  1 
ATOM   974  C  C   . LYS A 1 135 ? 41.34200  -1.67700  6.12200   1.000 68.49702  ?  412  LYS B C   1 
ATOM   975  O  O   . LYS A 1 135 ? 41.44000  -0.48900  5.79000   1.000 70.28224  ?  412  LYS B O   1 
ATOM   976  C  CB  . LYS A 1 135 ? 41.60100  -2.39000  8.51100   1.000 66.05728  ?  412  LYS B CB  1 
ATOM   977  C  CG  . LYS A 1 135 ? 42.64000  -1.32100  8.72700   1.000 60.85897  ?  412  LYS B CG  1 
ATOM   978  C  CD  . LYS A 1 135 ? 43.76400  -1.85100  9.60200   1.000 74.19306  ?  412  LYS B CD  1 
ATOM   979  C  CE  . LYS A 1 135 ? 45.00200  -0.97800  9.52400   1.000 75.27078  ?  412  LYS B CE  1 
ATOM   980  N  NZ  . LYS A 1 135 ? 46.25600  -1.75500  9.83600   1.000 95.88011  ?  412  LYS B NZ  1 
ATOM   981  N  N   . ASN A 1 136 ? 41.87500  -2.66200  5.39200   1.000 67.58351  ?  413  ASN B N   1 
ATOM   982  C  CA  . ASN A 1 136 ? 42.77100  -2.36000  4.27800   1.000 69.20538  ?  413  ASN B CA  1 
ATOM   983  C  C   . ASN A 1 136 ? 42.05300  -1.71800  3.10400   1.000 69.72450  ?  413  ASN B C   1 
ATOM   984  O  O   . ASN A 1 136 ? 42.71400  -1.18600  2.21000   1.000 70.31276  ?  413  ASN B O   1 
ATOM   985  C  CB  . ASN A 1 136 ? 43.47900  -3.62300  3.78900   1.000 69.13431  ?  413  ASN B CB  1 
ATOM   986  C  CG  . ASN A 1 136 ? 44.57700  -4.07200  4.72100   1.000 77.44628  ?  413  ASN B CG  1 
ATOM   987  O  OD1 . ASN A 1 136 ? 45.14100  -3.27300  5.47800   1.000 74.08616  ?  413  ASN B OD1 1 
ATOM   988  N  ND2 . ASN A 1 136 ? 44.90400  -5.36400  4.66000   1.000 77.16583  ?  413  ASN B ND2 1 
ATOM   989  N  N   . GLY A 1 137 ? 40.73000  -1.78100  3.06800   1.000 68.88427  ?  414  GLY B N   1 
ATOM   990  C  CA  . GLY A 1 137 ? 40.00000  -1.09100  2.03400   1.000 64.85089  ?  414  GLY B CA  1 
ATOM   991  C  C   . GLY A 1 137 ? 39.86300  0.39300   2.23900   1.000 67.51046  ?  414  GLY B C   1 
ATOM   992  O  O   . GLY A 1 137 ? 39.24200  1.06300   1.40900   1.000 70.69864  ?  414  GLY B O   1 
ATOM   993  N  N   . LEU A 1 138 ? 40.42100  0.93000   3.31900   1.000 70.01045  ?  415  LEU B N   1 
ATOM   994  C  CA  . LEU A 1 138 ? 40.33800  2.35400   3.62400   1.000 69.39933  ?  415  LEU B CA  1 
ATOM   995  C  C   . LEU A 1 138 ? 41.41700  3.11800   2.86600   1.000 73.38974  ?  415  LEU B C   1 
ATOM   996  O  O   . LEU A 1 138 ? 42.58600  2.71600   2.86100   1.000 72.56869  ?  415  LEU B O   1 
ATOM   997  C  CB  . LEU A 1 138 ? 40.49200  2.57900   5.12900   1.000 65.19700  ?  415  LEU B CB  1 
ATOM   998  C  CG  . LEU A 1 138 ? 39.32300  2.12300   6.00500   1.000 68.82678  ?  415  LEU B CG  1 
ATOM   999  C  CD1 . LEU A 1 138 ? 39.68200  2.23300   7.48100   1.000 59.06047  ?  415  LEU B CD1 1 
ATOM   1000 C  CD2 . LEU A 1 138 ? 38.07500  2.94700   5.68900   1.000 65.17958  ?  415  LEU B CD2 1 
ATOM   1001 N  N   . GLU A 1 139 ? 41.02200  4.21900   2.22000   1.000 76.65544  ?  416  GLU B N   1 
ATOM   1002 C  CA  . GLU A 1 139 ? 42.00300  5.06500   1.55400   1.000 86.76151  ?  416  GLU B CA  1 
ATOM   1003 C  C   . GLU A 1 139 ? 42.83400  5.79800   2.60300   1.000 94.91099  ?  416  GLU B C   1 
ATOM   1004 O  O   . GLU A 1 139 ? 42.28400  6.30700   3.58300   1.000 96.58069  ?  416  GLU B O   1 
ATOM   1005 C  CB  . GLU A 1 139 ? 41.32400  6.08000   0.62300   1.000 90.63575  ?  416  GLU B CB  1 
ATOM   1006 C  CG  . GLU A 1 139 ? 41.08300  5.58900   -0.80800  1.000 85.59081  ?  416  GLU B CG  1 
ATOM   1007 N  N   . PRO A 1 140 ? 44.16300  5.85800   2.43700   1.000 97.52713  ?  417  PRO B N   1 
ATOM   1008 C  CA  . PRO A 1 140 ? 45.02400  6.59300   3.37400   1.000 103.01978 ?  417  PRO B CA  1 
ATOM   1009 C  C   . PRO A 1 140 ? 44.53000  8.01300   3.64000   1.000 110.14858 ?  417  PRO B C   1 
ATOM   1010 O  O   . PRO A 1 140 ? 44.83300  8.56000   4.70200   1.000 118.57381 ?  417  PRO B O   1 
ATOM   1011 C  CB  . PRO A 1 140 ? 46.38800  6.61800   2.66600   1.000 113.33656 ?  417  PRO B CB  1 
ATOM   1012 C  CG  . PRO A 1 140 ? 46.11500  6.19000   1.24200   1.000 111.61893 ?  417  PRO B CG  1 
ATOM   1013 C  CD  . PRO A 1 140 ? 44.93000  5.26900   1.33100   1.000 97.91908  ?  417  PRO B CD  1 
ATOM   1014 N  N   . ASN A 1 193 ? 32.87900  -12.31900 -9.72400  1.000 89.01501  ?  470  ASN B N   1 
ATOM   1015 C  CA  . ASN A 1 193 ? 32.19900  -13.47400 -9.14200  1.000 87.16079  ?  470  ASN B CA  1 
ATOM   1016 C  C   . ASN A 1 193 ? 32.48300  -13.57100 -7.65300  1.000 87.88709  ?  470  ASN B C   1 
ATOM   1017 O  O   . ASN A 1 193 ? 31.63600  -13.20900 -6.83700  1.000 89.10785  ?  470  ASN B O   1 
ATOM   1018 C  CB  . ASN A 1 193 ? 32.61800  -14.77500 -9.83200  1.000 93.42328  ?  470  ASN B CB  1 
ATOM   1019 C  CG  . ASN A 1 193 ? 31.70200  -15.95100 -9.47900  1.000 97.27559  ?  470  ASN B CG  1 
ATOM   1020 O  OD1 . ASN A 1 193 ? 30.68800  -15.78100 -8.79300  1.000 107.00497 ?  470  ASN B OD1 1 
ATOM   1021 N  ND2 . ASN A 1 193 ? 32.04900  -17.14200 -9.96200  1.000 94.36707  ?  470  ASN B ND2 1 
ATOM   1022 N  N   . LEU A 1 194 ? 33.66700  -14.06500 -7.28100  1.000 84.80904  ?  471  LEU B N   1 
ATOM   1023 C  CA  . LEU A 1 194 ? 34.01800  -14.20900 -5.87900  1.000 83.03844  ?  471  LEU B CA  1 
ATOM   1024 C  C   . LEU A 1 194 ? 34.82900  -13.02600 -5.35200  1.000 76.71577  ?  471  LEU B C   1 
ATOM   1025 O  O   . LEU A 1 194 ? 35.51500  -13.15300 -4.33300  1.000 79.45804  ?  471  LEU B O   1 
ATOM   1026 C  CB  . LEU A 1 194 ? 34.77100  -15.53400 -5.69600  1.000 73.79338  ?  471  LEU B CB  1 
ATOM   1027 C  CG  . LEU A 1 194 ? 33.87300  -16.69800 -6.14100  1.000 81.60595  ?  471  LEU B CG  1 
ATOM   1028 C  CD1 . LEU A 1 194 ? 34.68600  -17.77600 -6.83600  1.000 94.47424  ?  471  LEU B CD1 1 
ATOM   1029 C  CD2 . LEU A 1 194 ? 33.08100  -17.28400 -4.96900  1.000 79.33132  ?  471  LEU B CD2 1 
ATOM   1030 N  N   . GLU A 1 195 ? 34.73300  -11.86400 -5.99700  1.000 78.35729  ?  472  GLU B N   1 
ATOM   1031 C  CA  . GLU A 1 195 ? 35.61300  -10.74000 -5.70800  1.000 79.38415  ?  472  GLU B CA  1 
ATOM   1032 C  C   . GLU A 1 195 ? 35.04600  -9.76100  -4.66900  1.000 78.80121  ?  472  GLU B C   1 
ATOM   1033 O  O   . GLU A 1 195 ? 35.48800  -8.61200  -4.62600  1.000 86.03234  ?  472  GLU B O   1 
ATOM   1034 C  CB  . GLU A 1 195 ? 35.93400  -9.99200  -7.00500  1.000 80.28327  ?  472  GLU B CB  1 
ATOM   1035 N  N   . GLN A 1 196 ? 34.09600  -10.17300 -3.83300  1.000 69.92115  ?  473  GLN B N   1 
ATOM   1036 C  CA  . GLN A 1 196 ? 33.46400  -9.24500  -2.89800  1.000 71.84211  ?  473  GLN B CA  1 
ATOM   1037 C  C   . GLN A 1 196 ? 33.25800  -9.92100  -1.55100  1.000 64.73828  ?  473  GLN B C   1 
ATOM   1038 O  O   . GLN A 1 196 ? 32.56600  -10.94000 -1.47400  1.000 67.72415  ?  473  GLN B O   1 
ATOM   1039 C  CB  . GLN A 1 196 ? 32.11900  -8.74600  -3.44600  1.000 71.02203  ?  473  GLN B CB  1 
ATOM   1040 C  CG  . GLN A 1 196 ? 32.07500  -7.25800  -3.76300  1.000 69.53937  ?  473  GLN B CG  1 
ATOM   1041 C  CD  . GLN A 1 196 ? 30.68800  -6.75900  -4.20800  1.000 67.20632  ?  473  GLN B CD  1 
ATOM   1042 O  OE1 . GLN A 1 196 ? 29.67800  -7.46200  -4.07800  1.000 67.18421  ?  473  GLN B OE1 1 
ATOM   1043 N  NE2 . GLN A 1 196 ? 30.64300  -5.53800  -4.72200  1.000 57.42372  ?  473  GLN B NE2 1 
ATOM   1044 N  N   . ASP A 1 197 ? 33.82100  -9.34100  -0.49100  1.000 57.74938  ?  474  ASP B N   1 
ATOM   1045 C  CA  . ASP A 1 197 ? 33.52100  -9.80300  0.85900   1.000 62.82140  ?  474  ASP B CA  1 
ATOM   1046 C  C   . ASP A 1 197 ? 32.20900  -9.18400  1.34900   1.000 56.64092  ?  474  ASP B C   1 
ATOM   1047 O  O   . ASP A 1 197 ? 31.57900  -8.37500  0.66500   1.000 54.13277  ?  474  ASP B O   1 
ATOM   1048 C  CB  . ASP A 1 197 ? 34.67800  -9.49000  1.81500   1.000 57.23964  ?  474  ASP B CB  1 
ATOM   1049 C  CG  . ASP A 1 197 ? 34.89800  -7.99200  2.01900   1.000 63.61066  ?  474  ASP B CG  1 
ATOM   1050 O  OD1 . ASP A 1 197 ? 34.11500  -7.17200  1.47900   1.000 61.68014  ?  474  ASP B OD1 1 
ATOM   1051 O  OD2 . ASP A 1 197 ? 35.87000  -7.62600  2.71300   1.000 66.04135  -1 474  ASP B OD2 1 
ATOM   1052 N  N   . LEU A 1 198 ? 31.81700  -9.53100  2.58000   1.000 54.88258  ?  475  LEU B N   1 
ATOM   1053 C  CA  . LEU A 1 198 ? 30.50600  -9.12900  3.08400   1.000 55.30892  ?  475  LEU B CA  1 
ATOM   1054 C  C   . LEU A 1 198 ? 30.39400  -7.61400  3.23400   1.000 53.50753  ?  475  LEU B C   1 
ATOM   1055 O  O   . LEU A 1 198 ? 29.37100  -7.01600  2.87100   1.000 53.53705  ?  475  LEU B O   1 
ATOM   1056 C  CB  . LEU A 1 198 ? 30.22700  -9.81600  4.41400   1.000 50.72645  ?  475  LEU B CB  1 
ATOM   1057 C  CG  . LEU A 1 198 ? 28.86800  -9.49100  5.02400   1.000 51.58813  ?  475  LEU B CG  1 
ATOM   1058 C  CD1 . LEU A 1 198 ? 27.74600  -9.86900  4.05700   1.000 45.66146  ?  475  LEU B CD1 1 
ATOM   1059 C  CD2 . LEU A 1 198 ? 28.72200  -10.22800 6.35800   1.000 52.88776  ?  475  LEU B CD2 1 
ATOM   1060 N  N   . CYS A 1 199 ? 31.43200  -6.98600  3.77700   1.000 51.78092  ?  476  CYS B N   1 
ATOM   1061 C  CA  . CYS A 1 199 ? 31.41900  -5.54400  3.99000   1.000 52.07624  ?  476  CYS B CA  1 
ATOM   1062 C  C   . CYS A 1 199 ? 31.30400  -4.78100  2.66600   1.000 55.69650  ?  476  CYS B C   1 
ATOM   1063 O  O   . CYS A 1 199 ? 30.46600  -3.87700  2.52600   1.000 53.51250  ?  476  CYS B O   1 
ATOM   1064 C  CB  . CYS A 1 199 ? 32.68800  -5.15200  4.75400   1.000 59.58600  ?  476  CYS B CB  1 
ATOM   1065 S  SG  . CYS A 1 199 ? 32.92100  -3.40200  4.99500   1.000 60.51338  ?  476  CYS B SG  1 
ATOM   1066 N  N   . THR A 1 200 ? 32.16100  -5.11900  1.69300   1.000 53.95249  ?  477  THR B N   1 
ATOM   1067 C  CA  . THR A 1 200 ? 32.11000  -4.49400  0.37700   1.000 49.97303  ?  477  THR B CA  1 
ATOM   1068 C  C   . THR A 1 200 ? 30.74800  -4.68900  -0.26900  1.000 53.85466  ?  477  THR B C   1 
ATOM   1069 O  O   . THR A 1 200 ? 30.19500  -3.75800  -0.87700  1.000 48.26944  ?  477  THR B O   1 
ATOM   1070 C  CB  . THR A 1 200 ? 33.20400  -5.08000  -0.50500  1.000 57.10599  ?  477  THR B CB  1 
ATOM   1071 O  OG1 . THR A 1 200 ? 34.48200  -4.86400  0.11400   1.000 58.23265  ?  477  THR B OG1 1 
ATOM   1072 C  CG2 . THR A 1 200 ? 33.19200  -4.45200  -1.89100  1.000 45.24688  ?  477  THR B CG2 1 
ATOM   1073 N  N   . PHE A 1 201 ? 30.18200  -5.89300  -0.12400  1.000 55.08779  ?  478  PHE B N   1 
ATOM   1074 C  CA  . PHE A 1 201 ? 28.86800  -6.17800  -0.69200  1.000 52.95496  ?  478  PHE B CA  1 
ATOM   1075 C  C   . PHE A 1 201 ? 27.79800  -5.26100  -0.10000  1.000 48.53414  ?  478  PHE B C   1 
ATOM   1076 O  O   . PHE A 1 201 ? 27.04300  -4.61900  -0.83900  1.000 50.94283  ?  478  PHE B O   1 
ATOM   1077 C  CB  . PHE A 1 201 ? 28.49200  -7.64900  -0.47700  1.000 53.02785  ?  478  PHE B CB  1 
ATOM   1078 C  CG  . PHE A 1 201 ? 27.05100  -7.95100  -0.81500  1.000 54.25684  ?  478  PHE B CG  1 
ATOM   1079 C  CD1 . PHE A 1 201 ? 26.59900  -7.84000  -2.12500  1.000 46.71474  ?  478  PHE B CD1 1 
ATOM   1080 C  CD2 . PHE A 1 201 ? 26.14600  -8.30700  0.17500   1.000 46.77548  ?  478  PHE B CD2 1 
ATOM   1081 C  CE1 . PHE A 1 201 ? 25.27700  -8.08300  -2.44100  1.000 56.12182  ?  478  PHE B CE1 1 
ATOM   1082 C  CE2 . PHE A 1 201 ? 24.81800  -8.55800  -0.15000  1.000 53.28215  ?  478  PHE B CE2 1 
ATOM   1083 C  CZ  . PHE A 1 201 ? 24.38700  -8.44100  -1.46400  1.000 49.93668  ?  478  PHE B CZ  1 
ATOM   1084 N  N   . LEU A 1 202 ? 27.71700  -5.19400  1.23400   1.000 47.05011  ?  479  LEU B N   1 
ATOM   1085 C  CA  . LEU A 1 202 ? 26.68400  -4.39600  1.89800   1.000 47.14466  ?  479  LEU B CA  1 
ATOM   1086 C  C   . LEU A 1 202 ? 26.82000  -2.91000  1.57600   1.000 48.59973  ?  479  LEU B C   1 
ATOM   1087 O  O   . LEU A 1 202 ? 25.82200  -2.22900  1.32000   1.000 47.43204  ?  479  LEU B O   1 
ATOM   1088 C  CB  . LEU A 1 202 ? 26.74600  -4.59600  3.41200   1.000 45.50550  ?  479  LEU B CB  1 
ATOM   1089 C  CG  . LEU A 1 202 ? 26.48500  -6.00600  3.93100   1.000 45.36198  ?  479  LEU B CG  1 
ATOM   1090 C  CD1 . LEU A 1 202 ? 26.64400  -6.10700  5.48100   1.000 36.98558  ?  479  LEU B CD1 1 
ATOM   1091 C  CD2 . LEU A 1 202 ? 25.10800  -6.49400  3.46300   1.000 44.41874  ?  479  LEU B CD2 1 
ATOM   1092 N  N   . ILE A 1 203 ? 28.04300  -2.37200  1.63300   1.000 49.86957  ?  480  ILE B N   1 
ATOM   1093 C  CA  . ILE A 1 203 ? 28.23700  -0.97200  1.27600   1.000 45.76120  ?  480  ILE B CA  1 
ATOM   1094 C  C   . ILE A 1 203 ? 27.82000  -0.73700  -0.17800  1.000 51.22337  ?  480  ILE B C   1 
ATOM   1095 O  O   . ILE A 1 203 ? 27.17600  0.26800   -0.50600  1.000 50.29561  ?  480  ILE B O   1 
ATOM   1096 C  CB  . ILE A 1 203 ? 29.69800  -0.55200  1.52500   1.000 49.70282  ?  480  ILE B CB  1 
ATOM   1097 C  CG1 . ILE A 1 203 ? 29.99000  -0.51800  3.03000   1.000 45.17461  ?  480  ILE B CG1 1 
ATOM   1098 C  CG2 . ILE A 1 203 ? 30.01100  0.80000   0.82400   1.000 43.74187  ?  480  ILE B CG2 1 
ATOM   1099 C  CD1 . ILE A 1 203 ? 31.46500  -0.29200  3.36100   1.000 49.74134  ?  480  ILE B CD1 1 
ATOM   1100 N  N   . SER A 1 204 ? 28.14100  -1.68100  -1.05900  1.000 48.06566  ?  481  SER B N   1 
ATOM   1101 C  CA  . SER A 1 204 ? 27.77300  -1.52700  -2.46000  1.000 44.78315  ?  481  SER B CA  1 
ATOM   1102 C  C   . SER A 1 204 ? 26.26000  -1.52600  -2.64000  1.000 50.53470  ?  481  SER B C   1 
ATOM   1103 O  O   . SER A 1 204 ? 25.72100  -0.72400  -3.40900  1.000 49.37605  ?  481  SER B O   1 
ATOM   1104 C  CB  . SER A 1 204 ? 28.41200  -2.63500  -3.28800  1.000 44.35917  ?  481  SER B CB  1 
ATOM   1105 O  OG  . SER A 1 204 ? 27.63400  -2.88900  -4.43500  1.000 65.84018  ?  481  SER B OG  1 
ATOM   1106 N  N   . ARG A 1 205 ? 25.55500  -2.42300  -1.94500  1.000 49.30455  ?  482  ARG B N   1 
ATOM   1107 C  CA  . ARG A 1 205 ? 24.10400  -2.45900  -2.06600  1.000 46.97385  ?  482  ARG B CA  1 
ATOM   1108 C  C   . ARG A 1 205 ? 23.46800  -1.23800  -1.39900  1.000 49.27116  ?  482  ARG B C   1 
ATOM   1109 O  O   . ARG A 1 205 ? 22.51700  -0.65800  -1.93900  1.000 48.22866  ?  482  ARG B O   1 
ATOM   1110 C  CB  . ARG A 1 205 ? 23.57300  -3.77500  -1.49000  1.000 47.73339  ?  482  ARG B CB  1 
ATOM   1111 C  CG  . ARG A 1 205 ? 23.90300  -4.99000  -2.38100  1.000 52.01131  ?  482  ARG B CG  1 
ATOM   1112 C  CD  . ARG A 1 205 ? 23.16100  -4.93700  -3.74600  1.000 52.26216  ?  482  ARG B CD  1 
ATOM   1113 N  NE  . ARG A 1 205 ? 21.84000  -5.55500  -3.64200  1.000 60.31240  ?  482  ARG B NE  1 
ATOM   1114 C  CZ  . ARG A 1 205 ? 21.53900  -6.79000  -4.02800  1.000 57.55113  ?  482  ARG B CZ  1 
ATOM   1115 N  NH1 . ARG A 1 205 ? 22.39800  -7.53700  -4.70800  1.000 60.09226  ?  482  ARG B NH1 1 
ATOM   1116 N  NH2 . ARG A 1 205 ? 20.34600  -7.29200  -3.71700  1.000 53.46944  ?  482  ARG B NH2 1 
ATOM   1117 N  N   . ALA A 1 206 ? 24.01300  -0.80200  -0.25400  1.000 44.24128  ?  483  ALA B N   1 
ATOM   1118 C  CA  . ALA A 1 206 ? 23.50500  0.39300   0.42400   1.000 48.41536  ?  483  ALA B CA  1 
ATOM   1119 C  C   . ALA A 1 206 ? 23.61900  1.65600   -0.43800  1.000 49.65615  ?  483  ALA B C   1 
ATOM   1120 O  O   . ALA A 1 206 ? 22.77500  2.54900   -0.33600  1.000 48.34074  ?  483  ALA B O   1 
ATOM   1121 C  CB  . ALA A 1 206 ? 24.25000  0.59600   1.74700   1.000 40.37968  ?  483  ALA B CB  1 
ATOM   1122 N  N   . CYS A 1 207 ? 24.64800  1.73100   -1.28600  1.000 44.35023  ?  484  CYS B N   1 
ATOM   1123 C  CA  . CYS A 1 207 ? 24.87000  2.95800   -2.10000  1.000 50.22851  ?  484  CYS B CA  1 
ATOM   1124 C  C   . CYS A 1 207 ? 23.83600  3.04500   -3.23000  1.000 52.46877  ?  484  CYS B C   1 
ATOM   1125 O  O   . CYS A 1 207 ? 23.72800  4.12200   -3.83900  1.000 50.33027  ?  484  CYS B O   1 
ATOM   1126 C  CB  . CYS A 1 207 ? 26.28000  2.97800   -2.67700  1.000 47.69670  ?  484  CYS B CB  1 
ATOM   1127 S  SG  . CYS A 1 207 ? 27.57100  3.17900   -1.42200  1.000 61.36701  ?  484  CYS B SG  1 
ATOM   1128 N  N   . LYS A 1 208 ? 23.10400  1.96000   -3.49300  1.000 50.72308  ?  485  LYS B N   1 
ATOM   1129 C  CA  . LYS A 1 208 ? 22.10700  1.94500   -4.55400  1.000 51.38205  ?  485  LYS B CA  1 
ATOM   1130 C  C   . LYS A 1 208 ? 20.67900  2.04900   -4.03500  1.000 51.35580  ?  485  LYS B C   1 
ATOM   1131 O  O   . LYS A 1 208 ? 19.75100  2.07400   -4.84600  1.000 55.91685  ?  485  LYS B O   1 
ATOM   1132 C  CB  . LYS A 1 208 ? 22.23900  0.66900   -5.39000  1.000 56.44491  ?  485  LYS B CB  1 
ATOM   1133 C  CG  . LYS A 1 208 ? 23.52800  0.53700   -6.20200  1.000 55.76437  ?  485  LYS B CG  1 
ATOM   1134 C  CD  . LYS A 1 208 ? 23.69500  -0.91200  -6.65400  1.000 65.93414  ?  485  LYS B CD  1 
ATOM   1135 C  CE  . LYS A 1 208 ? 25.07600  -1.19500  -7.27100  1.000 78.10062  ?  485  LYS B CE  1 
ATOM   1136 N  NZ  . LYS A 1 208 ? 26.18900  -1.10100  -6.25700  1.000 82.49531  ?  485  LYS B NZ  1 
ATOM   1137 N  N   . ASN A 1 209 ? 20.50500  1.90200   -2.71900  1.000 43.20562  ?  486  ASN B N   1 
ATOM   1138 C  CA  . ASN A 1 209 ? 19.14400  1.88500   -2.11900  1.000 46.79556  ?  486  ASN B CA  1 
ATOM   1139 C  C   . ASN A 1 209 ? 19.19800  2.67700   -0.81600  1.000 49.54051  ?  486  ASN B C   1 
ATOM   1140 O  O   . ASN A 1 209 ? 19.91700  2.24800   0.10400   1.000 47.65264  ?  486  ASN B O   1 
ATOM   1141 C  CB  . ASN A 1 209 ? 18.65100  0.45500   -1.88500  1.000 47.61330  ?  486  ASN B CB  1 
ATOM   1142 C  CG  . ASN A 1 209 ? 17.27100  0.37500   -1.26700  1.000 52.47444  ?  486  ASN B CG  1 
ATOM   1143 O  OD1 . ASN A 1 209 ? 16.61800  1.39100   -1.04000  1.000 66.87736  ?  486  ASN B OD1 1 
ATOM   1144 N  ND2 . ASN A 1 209 ? 16.81200  -0.83700  -0.99900  1.000 53.95993  ?  486  ASN B ND2 1 
ATOM   1145 N  N   . SER A 1 210 ? 18.44700  3.77300   -0.73400  1.000 47.28130  ?  487  SER B N   1 
ATOM   1146 C  CA  . SER A 1 210 ? 18.55800  4.62200   0.44400   1.000 52.08540  ?  487  SER B CA  1 
ATOM   1147 C  C   . SER A 1 210 ? 17.93000  3.97600   1.67700   1.000 47.56271  ?  487  SER B C   1 
ATOM   1148 O  O   . SER A 1 210 ? 18.34500  4.27300   2.79900   1.000 47.29971  ?  487  SER B O   1 
ATOM   1149 C  CB  . SER A 1 210 ? 17.93400  5.98400   0.16700   1.000 51.86073  ?  487  SER B CB  1 
ATOM   1150 O  OG  . SER A 1 210 ? 16.60000  5.78800   -0.22500  1.000 59.54445  ?  487  SER B OG  1 
ATOM   1151 N  N   . THR A 1 211 ? 16.94500  3.09600   1.49700   1.000 46.11739  ?  488  THR B N   1 
ATOM   1152 C  CA  . THR A 1 211 ? 16.37700  2.38600   2.64000   1.000 39.38297  ?  488  THR B CA  1 
ATOM   1153 C  C   . THR A 1 211 ? 17.40600  1.42300   3.24100   1.000 45.82296  ?  488  THR B C   1 
ATOM   1154 O  O   . THR A 1 211 ? 17.61800  1.40700   4.45900   1.000 48.70822  ?  488  THR B O   1 
ATOM   1155 C  CB  . THR A 1 211 ? 15.09700  1.65100   2.22400   1.000 47.95566  ?  488  THR B CB  1 
ATOM   1156 O  OG1 . THR A 1 211 ? 14.11800  2.60000   1.72800   1.000 53.72380  ?  488  THR B OG1 1 
ATOM   1157 C  CG2 . THR A 1 211 ? 14.50900  0.90700   3.41400   1.000 36.36709  ?  488  THR B CG2 1 
ATOM   1158 N  N   . LEU A 1 212 ? 18.08100  0.63700   2.39000   1.000 48.88703  ?  489  LEU B N   1 
ATOM   1159 C  CA  . LEU A 1 212 ? 19.20100  -0.18600  2.83900   1.000 43.50016  ?  489  LEU B CA  1 
ATOM   1160 C  C   . LEU A 1 212 ? 20.26700  0.65600   3.52700   1.000 40.84352  ?  489  LEU B C   1 
ATOM   1161 O  O   . LEU A 1 212 ? 20.78300  0.28000   4.58300   1.000 42.23999  ?  489  LEU B O   1 
ATOM   1162 C  CB  . LEU A 1 212 ? 19.81600  -0.93800  1.66000   1.000 45.14279  ?  489  LEU B CB  1 
ATOM   1163 C  CG  . LEU A 1 212 ? 19.38200  -2.38800  1.46800   1.000 56.14952  ?  489  LEU B CG  1 
ATOM   1164 C  CD1 . LEU A 1 212 ? 19.78900  -2.92000  0.06900   1.000 55.57759  ?  489  LEU B CD1 1 
ATOM   1165 C  CD2 . LEU A 1 212 ? 20.00600  -3.22700  2.56200   1.000 50.26058  ?  489  LEU B CD2 1 
ATOM   1166 N  N   . ALA A 1 213 ? 20.63300  1.79200   2.92900   1.000 46.49307  ?  490  ALA B N   1 
ATOM   1167 C  CA  . ALA A 1 213 ? 21.65900  2.63100   3.54500   1.000 42.23133  ?  490  ALA B CA  1 
ATOM   1168 C  C   . ALA A 1 213 ? 21.23400  3.09900   4.93400   1.000 42.37567  ?  490  ALA B C   1 
ATOM   1169 O  O   . ALA A 1 213 ? 22.05900  3.15400   5.84800   1.000 42.25717  ?  490  ALA B O   1 
ATOM   1170 C  CB  . ALA A 1 213 ? 21.97000  3.82800   2.65100   1.000 36.49115  ?  490  ALA B CB  1 
ATOM   1171 N  N   . ASN A 1 214 ? 19.95100  3.42900   5.11300   1.000 38.47342  ?  491  ASN B N   1 
ATOM   1172 C  CA  . ASN A 1 214 ? 19.49000  3.92700   6.40600   1.000 40.81320  ?  491  ASN B CA  1 
ATOM   1173 C  C   . ASN A 1 214 ? 19.72400  2.89600   7.49900   1.000 42.38356  ?  491  ASN B C   1 
ATOM   1174 O  O   . ASN A 1 214 ? 20.27700  3.22100   8.55600   1.000 41.04835  ?  491  ASN B O   1 
ATOM   1175 C  CB  . ASN A 1 214 ? 18.00400  4.29600   6.35800   1.000 43.68700  ?  491  ASN B CB  1 
ATOM   1176 C  CG  . ASN A 1 214 ? 17.46800  4.75300   7.72700   1.000 54.51284  ?  491  ASN B CG  1 
ATOM   1177 O  OD1 . ASN A 1 214 ? 17.47100  5.96100   8.03500   1.000 53.20784  ?  491  ASN B OD1 1 
ATOM   1178 N  ND2 . ASN A 1 214 ? 17.01500  3.78200   8.56300   1.000 47.48580  ?  491  ASN B ND2 1 
ATOM   1179 N  N   . TYR A 1 215 ? 19.29700  1.64400   7.25900   1.000 41.29452  ?  492  TYR B N   1 
ATOM   1180 C  CA  . TYR A 1 215 ? 19.39700  0.60000   8.27000   1.000 42.44464  ?  492  TYR B CA  1 
ATOM   1181 C  C   . TYR A 1 215 ? 20.82700  0.12700   8.44600   1.000 41.43528  ?  492  TYR B C   1 
ATOM   1182 O  O   . TYR A 1 215 ? 21.22100  -0.23900  9.56200   1.000 39.36854  ?  492  TYR B O   1 
ATOM   1183 C  CB  . TYR A 1 215 ? 18.49500  -0.59000  7.92200   1.000 42.08936  ?  492  TYR B CB  1 
ATOM   1184 C  CG  . TYR A 1 215 ? 17.03600  -0.27400  8.13800   1.000 43.90605  ?  492  TYR B CG  1 
ATOM   1185 C  CD1 . TYR A 1 215 ? 16.52600  -0.09800  9.42800   1.000 41.51460  ?  492  TYR B CD1 1 
ATOM   1186 C  CD2 . TYR A 1 215 ? 16.16800  -0.11200  7.05300   1.000 38.48417  ?  492  TYR B CD2 1 
ATOM   1187 C  CE1 . TYR A 1 215 ? 15.18900  0.22000   9.62900   1.000 36.62965  ?  492  TYR B CE1 1 
ATOM   1188 C  CE2 . TYR A 1 215 ? 14.84500  0.18000   7.23600   1.000 38.10649  ?  492  TYR B CE2 1 
ATOM   1189 C  CZ  . TYR A 1 215 ? 14.34800  0.34500   8.52600   1.000 44.78668  ?  492  TYR B CZ  1 
ATOM   1190 O  OH  . TYR A 1 215 ? 13.01000  0.64100   8.68600   1.000 46.02766  ?  492  TYR B OH  1 
ATOM   1191 N  N   . LEU A 1 216 ? 21.61200  0.12900   7.37100   1.000 38.55397  ?  493  LEU B N   1 
ATOM   1192 C  CA  . LEU A 1 216 ? 23.01600  -0.20800  7.52400   1.000 40.59851  ?  493  LEU B CA  1 
ATOM   1193 C  C   . LEU A 1 216 ? 23.68200  0.78500   8.45700   1.000 40.57627  ?  493  LEU B C   1 
ATOM   1194 O  O   . LEU A 1 216 ? 24.41100  0.39300   9.37500   1.000 45.08669  ?  493  LEU B O   1 
ATOM   1195 C  CB  . LEU A 1 216 ? 23.71100  -0.24000  6.16800   1.000 38.22442  ?  493  LEU B CB  1 
ATOM   1196 C  CG  . LEU A 1 216 ? 25.21100  -0.51100  6.25100   1.000 42.05699  ?  493  LEU B CG  1 
ATOM   1197 C  CD1 . LEU A 1 216 ? 25.43600  -1.91600  6.80500   1.000 37.21153  ?  493  LEU B CD1 1 
ATOM   1198 C  CD2 . LEU A 1 216 ? 25.92900  -0.32500  4.88000   1.000 37.63048  ?  493  LEU B CD2 1 
ATOM   1199 N  N   . TYR A 1 217 ? 23.40000  2.07800   8.26700   1.000 41.65510  ?  494  TYR B N   1 
ATOM   1200 C  CA  . TYR A 1 217 ? 24.01700  3.10000   9.10600   1.000 37.60642  ?  494  TYR B CA  1 
ATOM   1201 C  C   . TYR A 1 217 ? 23.66900  2.87900   10.58200  1.000 43.42482  ?  494  TYR B C   1 
ATOM   1202 O  O   . TYR A 1 217 ? 24.55500  2.80600   11.43300  1.000 40.58652  ?  494  TYR B O   1 
ATOM   1203 C  CB  . TYR A 1 217 ? 23.57500  4.49400   8.65400   1.000 40.90141  ?  494  TYR B CB  1 
ATOM   1204 C  CG  . TYR A 1 217 ? 24.08400  5.58000   9.59300   1.000 43.18425  ?  494  TYR B CG  1 
ATOM   1205 C  CD1 . TYR A 1 217 ? 25.38400  6.08600   9.47600   1.000 42.51628  ?  494  TYR B CD1 1 
ATOM   1206 C  CD2 . TYR A 1 217 ? 23.27300  6.08200   10.61900  1.000 44.10162  ?  494  TYR B CD2 1 
ATOM   1207 C  CE1 . TYR A 1 217 ? 25.85100  7.05200   10.33900  1.000 45.39247  ?  494  TYR B CE1 1 
ATOM   1208 C  CE2 . TYR A 1 217 ? 23.73700  7.05500   11.49100  1.000 40.96258  ?  494  TYR B CE2 1 
ATOM   1209 C  CZ  . TYR A 1 217 ? 25.02300  7.52800   11.35600  1.000 49.22674  ?  494  TYR B CZ  1 
ATOM   1210 O  OH  . TYR A 1 217 ? 25.48500  8.47900   12.24000  1.000 55.24002  ?  494  TYR B OH  1 
ATOM   1211 N  N   . TRP A 1 218 ? 22.37300  2.74300   10.89700  1.000 41.22513  ?  495  TRP B N   1 
ATOM   1212 C  CA  . TRP A 1 218 ? 21.95500  2.67400   12.29700  1.000 44.35273  ?  495  TRP B CA  1 
ATOM   1213 C  C   . TRP A 1 218 ? 22.38200  1.35900   12.94600  1.000 46.60422  ?  495  TRP B C   1 
ATOM   1214 O  O   . TRP A 1 218 ? 22.82900  1.35500   14.10200  1.000 44.91698  ?  495  TRP B O   1 
ATOM   1215 C  CB  . TRP A 1 218 ? 20.43900  2.89000   12.40500  1.000 37.18918  ?  495  TRP B CB  1 
ATOM   1216 C  CG  . TRP A 1 218 ? 20.10700  4.33100   12.20600  1.000 43.99278  ?  495  TRP B CG  1 
ATOM   1217 C  CD1 . TRP A 1 218 ? 19.46400  4.89800   11.12600  1.000 41.28415  ?  495  TRP B CD1 1 
ATOM   1218 C  CD2 . TRP A 1 218 ? 20.45200  5.41200   13.08200  1.000 43.61202  ?  495  TRP B CD2 1 
ATOM   1219 N  NE1 . TRP A 1 218 ? 19.38200  6.25000   11.29500  1.000 47.20944  ?  495  TRP B NE1 1 
ATOM   1220 C  CE2 . TRP A 1 218 ? 19.96800  6.59700   12.48700  1.000 43.91908  ?  495  TRP B CE2 1 
ATOM   1221 C  CE3 . TRP A 1 218 ? 21.08800  5.48800   14.33700  1.000 45.10586  ?  495  TRP B CE3 1 
ATOM   1222 C  CZ2 . TRP A 1 218 ? 20.10800  7.84600   13.09000  1.000 39.57887  ?  495  TRP B CZ2 1 
ATOM   1223 C  CZ3 . TRP A 1 218 ? 21.23700  6.73400   14.93600  1.000 40.10733  ?  495  TRP B CZ3 1 
ATOM   1224 C  CH2 . TRP A 1 218 ? 20.74000  7.89300   14.31300  1.000 44.17021  ?  495  TRP B CH2 1 
ATOM   1225 N  N   . TYR A 1 219 ? 22.27500  0.24300   12.21300  1.000 38.10630  ?  496  TYR B N   1 
ATOM   1226 C  CA  . TYR A 1 219 ? 22.75900  -1.03700  12.72200  1.000 41.03807  ?  496  TYR B CA  1 
ATOM   1227 C  C   . TYR A 1 219 ? 24.24600  -0.96700  13.10000  1.000 41.87588  ?  496  TYR B C   1 
ATOM   1228 O  O   . TYR A 1 219 ? 24.65400  -1.42900  14.17500  1.000 42.54050  ?  496  TYR B O   1 
ATOM   1229 C  CB  . TYR A 1 219 ? 22.50300  -2.12200  11.68100  1.000 40.92679  ?  496  TYR B CB  1 
ATOM   1230 C  CG  . TYR A 1 219 ? 21.03100  -2.47800  11.49800  1.000 46.95810  ?  496  TYR B CG  1 
ATOM   1231 C  CD1 . TYR A 1 219 ? 20.05900  -2.00600  12.37300  1.000 43.45283  ?  496  TYR B CD1 1 
ATOM   1232 C  CD2 . TYR A 1 219 ? 20.62200  -3.32200  10.46300  1.000 44.84022  ?  496  TYR B CD2 1 
ATOM   1233 C  CE1 . TYR A 1 219 ? 18.71700  -2.35800  12.21500  1.000 45.34938  ?  496  TYR B CE1 1 
ATOM   1234 C  CE2 . TYR A 1 219 ? 19.28800  -3.67900  10.30700  1.000 39.98173  ?  496  TYR B CE2 1 
ATOM   1235 C  CZ  . TYR A 1 219 ? 18.34900  -3.20100  11.18800  1.000 44.69592  ?  496  TYR B CZ  1 
ATOM   1236 O  OH  . TYR A 1 219 ? 17.03400  -3.56900  11.04000  1.000 51.26234  ?  496  TYR B OH  1 
ATOM   1237 N  N   . VAL A 1 220 ? 25.07200  -0.37500  12.23300  1.000 41.54354  ?  497  VAL B N   1 
ATOM   1238 C  CA  . VAL A 1 220 ? 26.50900  -0.36600  12.47600  1.000 41.87458  ?  497  VAL B CA  1 
ATOM   1239 C  C   . VAL A 1 220 ? 26.85900  0.67300   13.53400  1.000 47.39500  ?  497  VAL B C   1 
ATOM   1240 O  O   . VAL A 1 220 ? 27.79500  0.47600   14.32500  1.000 46.64623  ?  497  VAL B O   1 
ATOM   1241 C  CB  . VAL A 1 220 ? 27.26700  -0.11200  11.15500  1.000 45.32610  ?  497  VAL B CB  1 
ATOM   1242 C  CG1 . VAL A 1 220 ? 28.73600  0.13100   11.42200  1.000 45.80645  ?  497  VAL B CG1 1 
ATOM   1243 C  CG2 . VAL A 1 220 ? 27.07300  -1.28400  10.20500  1.000 40.80935  ?  497  VAL B CG2 1 
ATOM   1244 N  N   . ILE A 1 221 ? 26.09200  1.76400   13.58100  1.000 44.32320  ?  498  ILE B N   1 
ATOM   1245 C  CA  . ILE A 1 221 ? 26.38100  2.85300   14.56200  1.000 46.65077  ?  498  ILE B CA  1 
ATOM   1246 C  C   . ILE A 1 221 ? 26.14700  2.31600   15.98000  1.000 47.76759  ?  498  ILE B C   1 
ATOM   1247 O  O   . ILE A 1 221 ? 26.93500  2.67000   16.87600  1.000 50.35001  ?  498  ILE B O   1 
ATOM   1248 C  CB  . ILE A 1 221 ? 25.54300  4.11500   14.26700  1.000 51.67783  ?  498  ILE B CB  1 
ATOM   1249 C  CG1 . ILE A 1 221 ? 26.21600  5.38000   14.80700  1.000 59.45304  ?  498  ILE B CG1 1 
ATOM   1250 C  CG2 . ILE A 1 221 ? 24.12100  3.96600   14.78700  1.000 50.68674  ?  498  ILE B CG2 1 
ATOM   1251 C  CD1 . ILE A 1 221 ? 27.59000  5.63500   14.23200  1.000 62.76538  ?  498  ILE B CD1 1 
ATOM   1252 N  N   . VAL A 1 222 ? 25.11500  1.48800   16.17200  1.000 45.44549  ?  499  VAL B N   1 
ATOM   1253 C  CA  . VAL A 1 222 ? 24.86200  0.91300   17.48600  1.000 45.12557  ?  499  VAL B CA  1 
ATOM   1254 C  C   . VAL A 1 222 ? 25.94600  -0.09300  17.85900  1.000 49.59510  ?  499  VAL B C   1 
ATOM   1255 O  O   . VAL A 1 222 ? 26.36200  -0.15900  19.02200  1.000 48.38468  ?  499  VAL B O   1 
ATOM   1256 C  CB  . VAL A 1 222 ? 23.45900  0.28200   17.55300  1.000 42.02659  ?  499  VAL B CB  1 
ATOM   1257 C  CG1 . VAL A 1 222 ? 23.27700  -0.44400  18.87000  1.000 42.55279  ?  499  VAL B CG1 1 
ATOM   1258 C  CG2 . VAL A 1 222 ? 22.37200  1.36300   17.33100  1.000 42.52937  ?  499  VAL B CG2 1 
ATOM   1259 N  N   . GLU A 1 223 ? 26.42100  -0.89600  16.90000  1.000 44.28818  ?  500  GLU B N   1 
ATOM   1260 C  CA  . GLU A 1 223 ? 27.53800  -1.78300  17.22800  1.000 49.29048  ?  500  GLU B CA  1 
ATOM   1261 C  C   . GLU A 1 223 ? 28.80300  -0.99800  17.55300  1.000 48.11254  ?  500  GLU B C   1 
ATOM   1262 O  O   . GLU A 1 223 ? 29.67500  -1.50800  18.25700  1.000 52.13046  ?  500  GLU B O   1 
ATOM   1263 C  CB  . GLU A 1 223 ? 27.82300  -2.77600  16.08900  1.000 44.84652  ?  500  GLU B CB  1 
ATOM   1264 C  CG  . GLU A 1 223 ? 26.69100  -3.75300  15.80600  1.000 51.79510  ?  500  GLU B CG  1 
ATOM   1265 C  CD  . GLU A 1 223 ? 26.13800  -4.40900  17.06500  1.000 58.26247  ?  500  GLU B CD  1 
ATOM   1266 O  OE1 . GLU A 1 223 ? 26.94200  -4.83500  17.93200  1.000 60.15802  ?  500  GLU B OE1 1 
ATOM   1267 O  OE2 . GLU A 1 223 ? 24.88700  -4.47800  17.19900  1.000 64.19792  -1 500  GLU B OE2 1 
ATOM   1268 N  N   . CYS A 1 224 ? 28.92900  0.22900   17.03700  1.000 53.17949  ?  501  CYS B N   1 
ATOM   1269 C  CA  . CYS A 1 224 ? 30.10400  1.04800   17.32600  1.000 49.74473  ?  501  CYS B CA  1 
ATOM   1270 C  C   . CYS A 1 224 ? 30.07000  1.57600   18.74500  1.000 55.38984  ?  501  CYS B C   1 
ATOM   1271 O  O   . CYS A 1 224 ? 31.11200  1.65200   19.40500  1.000 59.95939  ?  501  CYS B O   1 
ATOM   1272 C  CB  . CYS A 1 224 ? 30.19200  2.23000   16.36800  1.000 52.09025  ?  501  CYS B CB  1 
ATOM   1273 S  SG  . CYS A 1 224 ? 30.68800  1.84100   14.69300  1.000 55.06139  ?  501  CYS B SG  1 
ATOM   1274 N  N   . GLU A 1 225 ? 28.89300  1.98000   19.22200  1.000 52.20712  ?  502  GLU B N   1 
ATOM   1275 C  CA  . GLU A 1 225 ? 28.80000  2.56000   20.55400  1.000 57.20058  ?  502  GLU B CA  1 
ATOM   1276 C  C   . GLU A 1 225 ? 28.69400  1.50500   21.64600  1.000 51.77185  ?  502  GLU B C   1 
ATOM   1277 O  O   . GLU A 1 225 ? 28.61200  1.87300   22.81700  1.000 60.43927  ?  502  GLU B O   1 
ATOM   1278 C  CB  . GLU A 1 225 ? 27.62200  3.55500   20.64200  1.000 52.02690  ?  502  GLU B CB  1 
ATOM   1279 C  CG  . GLU A 1 225 ? 26.23200  2.96200   20.87800  1.000 66.88622  ?  502  GLU B CG  1 
ATOM   1280 C  CD  . GLU A 1 225 ? 25.87900  2.71800   22.37200  1.000 58.63345  ?  502  GLU B CD  1 
ATOM   1281 O  OE1 . GLU A 1 225 ? 26.32500  3.47100   23.28300  1.000 69.03865  ?  502  GLU B OE1 1 
ATOM   1282 N  N   . ASP A 1 226 ? 28.73400  0.21400   21.30800  1.000 55.47412  ?  503  ASP B N   1 
ATOM   1283 C  CA  . ASP A 1 226 ? 28.51700  -0.83000  22.30700  1.000 56.66717  ?  503  ASP B CA  1 
ATOM   1284 C  C   . ASP A 1 226 ? 29.71500  -0.88200  23.25700  1.000 56.41962  ?  503  ASP B C   1 
ATOM   1285 O  O   . ASP A 1 226 ? 30.81900  -1.27500  22.87100  1.000 55.38528  ?  503  ASP B O   1 
ATOM   1286 C  CB  . ASP A 1 226 ? 28.27800  -2.17900  21.63400  1.000 52.36109  ?  503  ASP B CB  1 
ATOM   1287 C  CG  . ASP A 1 226 ? 27.73400  -3.23900  22.60600  1.000 59.39372  ?  503  ASP B CG  1 
ATOM   1288 O  OD1 . ASP A 1 226 ? 28.19900  -3.30400  23.77600  1.000 57.07843  ?  503  ASP B OD1 1 
ATOM   1289 O  OD2 . ASP A 1 226 ? 26.83700  -4.01500  22.19800  1.000 59.54694  -1 503  ASP B OD2 1 
ATOM   1290 N  N   . GLN A 1 227 ? 29.49800  -0.48400  24.50700  1.000 61.64696  ?  504  GLN B N   1 
ATOM   1291 C  CA  . GLN A 1 227 ? 30.59800  -0.44200  25.46400  1.000 63.78177  ?  504  GLN B CA  1 
ATOM   1292 C  C   . GLN A 1 227 ? 31.01700  -1.83100  25.94800  1.000 63.19996  ?  504  GLN B C   1 
ATOM   1293 O  O   . GLN A 1 227 ? 32.18100  -2.01400  26.31100  1.000 68.19517  ?  504  GLN B O   1 
ATOM   1294 C  CB  . GLN A 1 227 ? 30.22400  0.45600   26.63800  1.000 67.45472  ?  504  GLN B CB  1 
ATOM   1295 C  CG  . GLN A 1 227 ? 30.07000  1.92800   26.26600  1.000 63.88842  ?  504  GLN B CG  1 
ATOM   1296 C  CD  . GLN A 1 227 ? 29.56200  2.74100   27.44300  1.000 78.41553  ?  504  GLN B CD  1 
ATOM   1297 O  OE1 . GLN A 1 227 ? 28.49300  3.35400   27.38200  1.000 75.53982  ?  504  GLN B OE1 1 
ATOM   1298 N  NE2 . GLN A 1 227 ? 30.31500  2.72200   28.53900  1.000 86.78374  ?  504  GLN B NE2 1 
ATOM   1299 N  N   . ASP A 1 228 ? 30.11900  -2.82500  25.94300  1.000 64.33205  ?  505  ASP B N   1 
ATOM   1300 C  CA  . ASP A 1 228 ? 30.54700  -4.19100  26.25800  1.000 65.45312  ?  505  ASP B CA  1 
ATOM   1301 C  C   . ASP A 1 228 ? 31.53000  -4.70800  25.21500  1.000 68.22646  ?  505  ASP B C   1 
ATOM   1302 O  O   . ASP A 1 228 ? 32.58100  -5.25800  25.56100  1.000 71.92309  ?  505  ASP B O   1 
ATOM   1303 C  CB  . ASP A 1 228 ? 29.35400  -5.14200  26.35100  1.000 67.74944  ?  505  ASP B CB  1 
ATOM   1304 C  CG  . ASP A 1 228 ? 28.62200  -5.04400  27.67500  1.000 81.51213  ?  505  ASP B CG  1 
ATOM   1305 O  OD1 . ASP A 1 228 ? 29.28200  -5.17400  28.73200  1.000 94.94995  ?  505  ASP B OD1 1 
ATOM   1306 O  OD2 . ASP A 1 228 ? 27.38000  -4.84900  27.65700  1.000 90.00736  -1 505  ASP B OD2 1 
ATOM   1307 N  N   . THR A 1 229 ? 31.18500  -4.56100  23.92800  1.000 61.96603  ?  506  THR B N   1 
ATOM   1308 C  CA  . THR A 1 229 ? 32.08900  -4.96000  22.85500  1.000 66.20277  ?  506  THR B CA  1 
ATOM   1309 C  C   . THR A 1 229 ? 33.41000  -4.21700  22.95900  1.000 67.45452  ?  506  THR B C   1 
ATOM   1310 O  O   . THR A 1 229 ? 34.48600  -4.80200  22.77800  1.000 64.46117  ?  506  THR B O   1 
ATOM   1311 C  CB  . THR A 1 229 ? 31.45000  -4.68600  21.48500  1.000 55.13593  ?  506  THR B CB  1 
ATOM   1312 O  OG1 . THR A 1 229 ? 30.10300  -5.15600  21.47100  1.000 58.67306  ?  506  THR B OG1 1 
ATOM   1313 C  CG2 . THR A 1 229 ? 32.23900  -5.36000  20.36900  1.000 52.21271  ?  506  THR B CG2 1 
ATOM   1314 N  N   . GLN A 1 230 ? 33.34100  -2.91700  23.24300  1.000 69.12416  ?  507  GLN B N   1 
ATOM   1315 C  CA  . GLN A 1 230 ? 34.54200  -2.09400  23.29700  1.000 66.83511  ?  507  GLN B CA  1 
ATOM   1316 C  C   . GLN A 1 230 ? 35.50100  -2.57700  24.38100  1.000 73.92885  ?  507  GLN B C   1 
ATOM   1317 O  O   . GLN A 1 230 ? 36.70200  -2.74600  24.13400  1.000 75.16703  ?  507  GLN B O   1 
ATOM   1318 C  CB  . GLN A 1 230 ? 34.14000  -0.64200  23.52200  1.000 68.02773  ?  507  GLN B CB  1 
ATOM   1319 C  CG  . GLN A 1 230 ? 35.29200  0.30000   23.69200  1.000 75.42440  ?  507  GLN B CG  1 
ATOM   1320 C  CD  . GLN A 1 230 ? 34.83900  1.73800   23.63900  1.000 81.87205  ?  507  GLN B CD  1 
ATOM   1321 O  OE1 . GLN A 1 230 ? 33.64200  2.01800   23.53000  1.000 80.42553  ?  507  GLN B OE1 1 
ATOM   1322 N  NE2 . GLN A 1 230 ? 35.79100  2.66300   23.70600  1.000 85.37025  ?  507  GLN B NE2 1 
ATOM   1323 N  N   . GLN A 1 231 ? 34.98800  -2.81300  25.59100  1.000 72.85337  ?  508  GLN B N   1 
ATOM   1324 C  CA  . GLN A 1 231 ? 35.86100  -3.26000  26.67000  1.000 70.73007  ?  508  GLN B CA  1 
ATOM   1325 C  C   . GLN A 1 231 ? 36.24400  -4.72800  26.51200  1.000 72.52208  ?  508  GLN B C   1 
ATOM   1326 O  O   . GLN A 1 231 ? 37.39400  -5.10300  26.76000  1.000 76.98364  ?  508  GLN B O   1 
ATOM   1327 C  CB  . GLN A 1 231 ? 35.18900  -3.00600  28.01800  1.000 77.63422  ?  508  GLN B CB  1 
ATOM   1328 C  CG  . GLN A 1 231 ? 34.61800  -1.58700  28.12600  1.000 84.38756  ?  508  GLN B CG  1 
ATOM   1329 C  CD  . GLN A 1 231 ? 34.02600  -1.27100  29.50100  1.000 100.80809 ?  508  GLN B CD  1 
ATOM   1330 O  OE1 . GLN A 1 231 ? 34.06300  -2.10000  30.41700  1.000 101.24988 ?  508  GLN B OE1 1 
ATOM   1331 N  NE2 . GLN A 1 231 ? 33.48000  -0.06200  29.64800  1.000 102.57974 ?  508  GLN B NE2 1 
ATOM   1332 N  N   . ARG A 1 232 ? 35.31200  -5.57200  26.07400  1.000 73.12627  ?  509  ARG B N   1 
ATOM   1333 C  CA  . ARG A 1 232 ? 35.52400  -7.01300  26.10400  1.000 70.47380  ?  509  ARG B CA  1 
ATOM   1334 C  C   . ARG A 1 232 ? 36.09100  -7.59100  24.80600  1.000 75.32662  ?  509  ARG B C   1 
ATOM   1335 O  O   . ARG A 1 232 ? 36.67100  -8.68100  24.83800  1.000 77.73721  ?  509  ARG B O   1 
ATOM   1336 C  CB  . ARG A 1 232 ? 34.20700  -7.70700  26.46800  1.000 72.20473  ?  509  ARG B CB  1 
ATOM   1337 C  CG  . ARG A 1 232 ? 33.74600  -7.37700  27.90000  1.000 85.04906  ?  509  ARG B CG  1 
ATOM   1338 C  CD  . ARG A 1 232 ? 32.27700  -7.70400  28.12300  1.000 89.89255  ?  509  ARG B CD  1 
ATOM   1339 N  NE  . ARG A 1 232 ? 31.87600  -8.78800  27.23900  1.000 97.79199  ?  509  ARG B NE  1 
ATOM   1340 C  CZ  . ARG A 1 232 ? 32.11000  -10.07100 27.47500  1.000 98.93561  ?  509  ARG B CZ  1 
ATOM   1341 N  NH1 . ARG A 1 232 ? 32.68100  -10.47900 28.60400  1.000 98.59695  ?  509  ARG B NH1 1 
ATOM   1342 N  NH2 . ARG A 1 232 ? 31.76700  -10.96900 26.55500  1.000 92.63950  ?  509  ARG B NH2 1 
ATOM   1343 N  N   . ASP A 1 233 ? 35.95800  -6.89500  23.67400  1.000 69.44171  ?  510  ASP B N   1 
ATOM   1344 C  CA  . ASP A 1 233 ? 36.49200  -7.37400  22.39800  1.000 66.26167  ?  510  ASP B CA  1 
ATOM   1345 C  C   . ASP A 1 233 ? 36.85000  -6.17500  21.52500  1.000 70.25762  ?  510  ASP B C   1 
ATOM   1346 O  O   . ASP A 1 233 ? 36.16100  -5.85700  20.54500  1.000 64.94195  ?  510  ASP B O   1 
ATOM   1347 C  CB  . ASP A 1 233 ? 35.49100  -8.29000  21.69600  1.000 68.31627  ?  510  ASP B CB  1 
ATOM   1348 C  CG  . ASP A 1 233 ? 36.06800  -8.94400  20.44400  1.000 77.37898  ?  510  ASP B CG  1 
ATOM   1349 O  OD1 . ASP A 1 233 ? 37.32300  -9.04400  20.31600  1.000 80.67098  ?  510  ASP B OD1 1 
ATOM   1350 O  OD2 . ASP A 1 233 ? 35.25600  -9.34400  19.57500  1.000 88.25173  -1 510  ASP B OD2 1 
ATOM   1351 N  N   . PRO A 1 234 ? 37.94400  -5.48600  21.85600  1.000 67.96162  ?  511  PRO B N   1 
ATOM   1352 C  CA  . PRO A 1 234 ? 38.31800  -4.26800  21.11500  1.000 68.34558  ?  511  PRO B CA  1 
ATOM   1353 C  C   . PRO A 1 234 ? 38.57000  -4.49200  19.63700  1.000 69.04295  ?  511  PRO B C   1 
ATOM   1354 O  O   . PRO A 1 234 ? 38.30600  -3.58900  18.83500  1.000 63.52502  ?  511  PRO B O   1 
ATOM   1355 C  CB  . PRO A 1 234 ? 39.60300  -3.81600  21.82000  1.000 73.74828  ?  511  PRO B CB  1 
ATOM   1356 C  CG  . PRO A 1 234 ? 39.58500  -4.49200  23.14100  1.000 65.65114  ?  511  PRO B CG  1 
ATOM   1357 C  CD  . PRO A 1 234 ? 38.87200  -5.78400  22.95400  1.000 71.36443  ?  511  PRO B CD  1 
ATOM   1358 N  N   . LYS A 1 235 ? 39.12600  -5.64100  19.25000  1.000 68.86749  ?  512  LYS B N   1 
ATOM   1359 C  CA  . LYS A 1 235 ? 39.33300  -5.89500  17.83100  1.000 61.51990  ?  512  LYS B CA  1 
ATOM   1360 C  C   . LYS A 1 235 ? 38.01200  -5.82000  17.08700  1.000 65.94365  ?  512  LYS B C   1 
ATOM   1361 O  O   . LYS A 1 235 ? 37.90400  -5.15900  16.05100  1.000 66.02526  ?  512  LYS B O   1 
ATOM   1362 C  CB  . LYS A 1 235 ? 39.99800  -7.25600  17.62900  1.000 64.51929  ?  512  LYS B CB  1 
ATOM   1363 N  N   . THR A 1 236 ? 36.97500  -6.46000  17.63000  1.000 65.41373  ?  513  THR B N   1 
ATOM   1364 C  CA  . THR A 1 236 ? 35.68800  -6.45300  16.95500  1.000 62.80950  ?  513  THR B CA  1 
ATOM   1365 C  C   . THR A 1 236 ? 35.05000  -5.05900  16.99200  1.000 60.69014  ?  513  THR B C   1 
ATOM   1366 O  O   . THR A 1 236 ? 34.40300  -4.64400  16.02000  1.000 55.97053  ?  513  THR B O   1 
ATOM   1367 C  CB  . THR A 1 236 ? 34.79400  -7.52800  17.57500  1.000 51.32751  ?  513  THR B CB  1 
ATOM   1368 C  CG2 . THR A 1 236 ? 33.32400  -7.20700  17.28200  1.000 56.64650  ?  513  THR B CG2 1 
ATOM   1369 N  N   . HIS A 1 237 ? 35.25200  -4.30600  18.08000  1.000 63.62994  ?  514  HIS B N   1 
ATOM   1370 C  CA  . HIS A 1 237 ? 34.79100  -2.91700  18.11200  1.000 60.86292  ?  514  HIS B CA  1 
ATOM   1371 C  C   . HIS A 1 237 ? 35.47700  -2.08000  17.03300  1.000 62.11369  ?  514  HIS B C   1 
ATOM   1372 O  O   . HIS A 1 237 ? 34.83000  -1.26800  16.35700  1.000 56.19267  ?  514  HIS B O   1 
ATOM   1373 C  CB  . HIS A 1 237 ? 35.04100  -2.30800  19.49500  1.000 59.05419  ?  514  HIS B CB  1 
ATOM   1374 C  CG  . HIS A 1 237 ? 34.68300  -0.85400  19.58700  1.000 62.99683  ?  514  HIS B CG  1 
ATOM   1375 N  ND1 . HIS A 1 237 ? 35.63200  0.14700   19.60900  1.000 57.19416  ?  514  HIS B ND1 1 
ATOM   1376 C  CD2 . HIS A 1 237 ? 33.47900  -0.23200  19.63900  1.000 62.38229  ?  514  HIS B CD2 1 
ATOM   1377 C  CE1 . HIS A 1 237 ? 35.02900  1.32100   19.67900  1.000 56.32168  ?  514  HIS B CE1 1 
ATOM   1378 N  NE2 . HIS A 1 237 ? 33.72500  1.11800   19.70100  1.000 58.04132  ?  514  HIS B NE2 1 
ATOM   1379 N  N   . GLU A 1 238 ? 36.79400  -2.25900  16.86900  1.000 60.61049  ?  515  GLU B N   1 
ATOM   1380 C  CA  . GLU A 1 238 ? 37.55000  -1.51100  15.86800  1.000 59.62537  ?  515  GLU B CA  1 
ATOM   1381 C  C   . GLU A 1 238 ? 37.10200  -1.86200  14.45300  1.000 58.02899  ?  515  GLU B C   1 
ATOM   1382 O  O   . GLU A 1 238 ? 37.04700  -0.99300  13.57500  1.000 56.92736  ?  515  GLU B O   1 
ATOM   1383 C  CB  . GLU A 1 238 ? 39.04500  -1.78900  16.05300  1.000 68.14186  ?  515  GLU B CB  1 
ATOM   1384 C  CG  . GLU A 1 238 ? 39.96400  -1.01800  15.10500  1.000 79.45630  ?  515  GLU B CG  1 
ATOM   1385 C  CD  . GLU A 1 238 ? 39.97900  0.49000   15.38000  1.000 89.62974  ?  515  GLU B CD  1 
ATOM   1386 O  OE1 . GLU A 1 238 ? 39.76700  0.88100   16.56000  1.000 95.42693  ?  515  GLU B OE1 1 
ATOM   1387 O  OE2 . GLU A 1 238 ? 40.19700  1.27600   14.41700  1.000 86.33500  -1 515  GLU B OE2 1 
ATOM   1388 N  N   . MET A 1 239 ? 36.77500  -3.13000  14.20900  1.000 57.04454  ?  516  MET B N   1 
ATOM   1389 C  CA  . MET A 1 239 ? 36.23900  -3.50400  12.90800  1.000 54.83631  ?  516  MET B CA  1 
ATOM   1390 C  C   . MET A 1 239 ? 34.99700  -2.68700  12.58500  1.000 52.47925  ?  516  MET B C   1 
ATOM   1391 O  O   . MET A 1 239 ? 34.85700  -2.16700  11.47200  1.000 57.43831  ?  516  MET B O   1 
ATOM   1392 C  CB  . MET A 1 239 ? 35.94400  -5.00200  12.87100  1.000 55.41348  ?  516  MET B CB  1 
ATOM   1393 C  CG  . MET A 1 239 ? 35.31600  -5.49300  11.56800  1.000 54.36779  ?  516  MET B CG  1 
ATOM   1394 S  SD  . MET A 1 239 ? 33.53100  -5.36900  11.60300  1.000 54.21863  ?  516  MET B SD  1 
ATOM   1395 C  CE  . MET A 1 239 ? 33.10700  -6.48700  12.92500  1.000 52.77612  ?  516  MET B CE  1 
ATOM   1396 N  N   . TYR A 1 240 ? 34.08700  -2.54100  13.55000  1.000 52.46062  ?  517  TYR B N   1 
ATOM   1397 C  CA  . TYR A 1 240 ? 32.85300  -1.81500  13.24900  1.000 53.10030  ?  517  TYR B CA  1 
ATOM   1398 C  C   . TYR A 1 240 ? 33.11400  -0.32800  13.01300  1.000 53.98356  ?  517  TYR B C   1 
ATOM   1399 O  O   . TYR A 1 240 ? 32.46300  0.28300   12.15900  1.000 49.19020  ?  517  TYR B O   1 
ATOM   1400 C  CB  . TYR A 1 240 ? 31.81500  -2.02500  14.35500  1.000 52.47356  ?  517  TYR B CB  1 
ATOM   1401 C  CG  . TYR A 1 240 ? 31.04500  -3.34000  14.25800  1.000 50.22649  ?  517  TYR B CG  1 
ATOM   1402 C  CD1 . TYR A 1 240 ? 30.22200  -3.60600  13.17000  1.000 48.84890  ?  517  TYR B CD1 1 
ATOM   1403 C  CD2 . TYR A 1 240 ? 31.13400  -4.30600  15.25800  1.000 47.25501  ?  517  TYR B CD2 1 
ATOM   1404 C  CE1 . TYR A 1 240 ? 29.49600  -4.78800  13.07800  1.000 45.32868  ?  517  TYR B CE1 1 
ATOM   1405 C  CE2 . TYR A 1 240 ? 30.41900  -5.49200  15.17300  1.000 48.34345  ?  517  TYR B CE2 1 
ATOM   1406 C  CZ  . TYR A 1 240 ? 29.60200  -5.72100  14.07600  1.000 45.78358  ?  517  TYR B CZ  1 
ATOM   1407 O  OH  . TYR A 1 240 ? 28.88100  -6.88600  13.96600  1.000 53.34318  ?  517  TYR B OH  1 
ATOM   1408 N  N   . LEU A 1 241 ? 34.08400  0.26800   13.70900  1.000 52.52151  ?  518  LEU B N   1 
ATOM   1409 C  CA  . LEU A 1 241 ? 34.48200  1.62200   13.33200  1.000 57.02246  ?  518  LEU B CA  1 
ATOM   1410 C  C   . LEU A 1 241 ? 34.93300  1.65800   11.87300  1.000 60.09703  ?  518  LEU B C   1 
ATOM   1411 O  O   . LEU A 1 241 ? 34.45600  2.48600   11.08100  1.000 55.25687  ?  518  LEU B O   1 
ATOM   1412 C  CB  . LEU A 1 241 ? 35.58400  2.14600   14.25100  1.000 51.26097  ?  518  LEU B CB  1 
ATOM   1413 C  CG  . LEU A 1 241 ? 35.20700  2.37700   15.71800  1.000 58.48481  ?  518  LEU B CG  1 
ATOM   1414 C  CD1 . LEU A 1 241 ? 36.34300  3.05300   16.45700  1.000 52.42461  ?  518  LEU B CD1 1 
ATOM   1415 C  CD2 . LEU A 1 241 ? 33.94000  3.17700   15.84400  1.000 51.59506  ?  518  LEU B CD2 1 
ATOM   1416 N  N   . ASN A 1 242 ? 35.83700  0.74300   11.49600  1.000 54.23212  ?  519  ASN B N   1 
ATOM   1417 C  CA  . ASN A 1 242 ? 36.30300  0.67200   10.11600  1.000 51.76117  ?  519  ASN B CA  1 
ATOM   1418 C  C   . ASN A 1 242 ? 35.16700  0.41800   9.14000   1.000 53.48469  ?  519  ASN B C   1 
ATOM   1419 O  O   . ASN A 1 242 ? 35.16400  0.98600   8.04500   1.000 55.49415  ?  519  ASN B O   1 
ATOM   1420 C  CB  . ASN A 1 242 ? 37.36600  -0.41000  9.96700   1.000 54.78772  ?  519  ASN B CB  1 
ATOM   1421 C  CG  . ASN A 1 242 ? 38.63400  -0.02500  10.62300  1.000 53.23439  ?  519  ASN B CG  1 
ATOM   1422 O  OD1 . ASN A 1 242 ? 38.85300  1.15700   10.86100  1.000 58.22662  ?  519  ASN B OD1 1 
ATOM   1423 N  ND2 . ASN A 1 242 ? 39.48000  -1.00700  10.95400  1.000 55.31226  ?  519  ASN B ND2 1 
ATOM   1424 N  N   . VAL A 1 243 ? 34.20600  -0.44800  9.49600   1.000 52.93668  ?  520  VAL B N   1 
ATOM   1425 C  CA  . VAL A 1 243 ? 33.04800  -0.62600  8.62400   1.000 50.85579  ?  520  VAL B CA  1 
ATOM   1426 C  C   . VAL A 1 243 ? 32.34500  0.70100   8.41100   1.000 52.32195  ?  520  VAL B C   1 
ATOM   1427 O  O   . VAL A 1 243 ? 31.94100  1.03700   7.29000   1.000 53.99142  ?  520  VAL B O   1 
ATOM   1428 C  CB  . VAL A 1 243 ? 32.05900  -1.66500  9.18200   1.000 51.12797  ?  520  VAL B CB  1 
ATOM   1429 C  CG1 . VAL A 1 243 ? 30.72900  -1.49000  8.47700   1.000 47.37508  ?  520  VAL B CG1 1 
ATOM   1430 C  CG2 . VAL A 1 243 ? 32.56700  -3.07200  8.97300   1.000 49.58383  ?  520  VAL B CG2 1 
ATOM   1431 N  N   . MET A 1 244 ? 32.16400  1.47000   9.48200   1.000 52.06622  ?  521  MET B N   1 
ATOM   1432 C  CA  . MET A 1 244 ? 31.52400  2.77400   9.33600   1.000 51.00310  ?  521  MET B CA  1 
ATOM   1433 C  C   . MET A 1 244 ? 32.39400  3.74400   8.52500   1.000 54.77937  ?  521  MET B C   1 
ATOM   1434 O  O   . MET A 1 244 ? 31.86700  4.55700   7.75700   1.000 53.39556  ?  521  MET B O   1 
ATOM   1435 C  CB  . MET A 1 244 ? 31.19500  3.34600   10.71000  1.000 48.06435  ?  521  MET B CB  1 
ATOM   1436 C  CG  . MET A 1 244 ? 30.53900  4.70900   10.67200  1.000 57.02175  ?  521  MET B CG  1 
ATOM   1437 S  SD  . MET A 1 244 ? 28.91000  4.70100   9.86600   1.000 57.28791  ?  521  MET B SD  1 
ATOM   1438 C  CE  . MET A 1 244 ? 27.97200  3.60600   10.95400  1.000 50.27332  ?  521  MET B CE  1 
ATOM   1439 N  N   . ARG A 1 245 ? 33.71600  3.64900   8.68100   1.000 49.94520  ?  522  ARG B N   1 
ATOM   1440 C  CA  . ARG A 1 245 ? 34.64300  4.52800   7.91900   1.000 52.58297  ?  522  ARG B CA  1 
ATOM   1441 C  C   . ARG A 1 245 ? 34.57400  4.16200   6.43300   1.000 54.67180  ?  522  ARG B C   1 
ATOM   1442 O  O   . ARG A 1 245 ? 34.58600  5.08500   5.59900   1.000 56.54719  ?  522  ARG B O   1 
ATOM   1443 C  CB  . ARG A 1 245 ? 36.06800  4.39200   8.46200   1.000 55.35411  ?  522  ARG B CB  1 
ATOM   1444 C  CG  . ARG A 1 245 ? 36.23000  4.86500   9.89900   1.000 60.86838  ?  522  ARG B CG  1 
ATOM   1445 C  CD  . ARG A 1 245 ? 37.62600  4.61500   10.43700  1.000 55.21729  ?  522  ARG B CD  1 
ATOM   1446 N  NE  . ARG A 1 245 ? 37.81800  5.20100   11.75500  1.000 71.84862  ?  522  ARG B NE  1 
ATOM   1447 C  CZ  . ARG A 1 245 ? 38.12700  4.51300   12.84800  1.000 71.46175  ?  522  ARG B CZ  1 
ATOM   1448 N  NH1 . ARG A 1 245 ? 38.24900  3.19900   12.79100  1.000 68.36600  ?  522  ARG B NH1 1 
ATOM   1449 N  NH2 . ARG A 1 245 ? 38.31100  5.14200   13.99600  1.000 73.47513  ?  522  ARG B NH2 1 
ATOM   1450 N  N   . ARG A 1 246 ? 34.50900  2.86400   6.12200   1.000 52.24822  ?  523  ARG B N   1 
ATOM   1451 C  CA  . ARG A 1 246 ? 34.40700  2.41600   4.70700   1.000 48.72259  ?  523  ARG B CA  1 
ATOM   1452 C  C   . ARG A 1 246 ? 33.08400  2.91200   4.12100   1.000 51.21046  ?  523  ARG B C   1 
ATOM   1453 O  O   . ARG A 1 246 ? 33.09200  3.38600   2.97100   1.000 57.21433  ?  523  ARG B O   1 
ATOM   1454 C  CB  . ARG A 1 246 ? 34.50100  0.89100   4.60300   1.000 56.75065  ?  523  ARG B CB  1 
ATOM   1455 C  CG  . ARG A 1 246 ? 35.90200  0.33200   4.80100   1.000 60.20085  ?  523  ARG B CG  1 
ATOM   1456 C  CD  . ARG A 1 246 ? 36.06700  -1.05300  4.20600   1.000 77.29135  ?  523  ARG B CD  1 
ATOM   1457 N  NE  . ARG A 1 246 ? 36.15200  -1.05300  2.75300   1.000 53.74020  ?  523  ARG B NE  1 
ATOM   1458 C  CZ  . ARG A 1 246 ? 35.36500  -1.76200  1.95300   1.000 63.24021  ?  523  ARG B CZ  1 
ATOM   1459 N  NH1 . ARG A 1 246 ? 34.59900  -2.71500  2.45200   1.000 79.78242  ?  523  ARG B NH1 1 
ATOM   1460 N  NH2 . ARG A 1 246 ? 35.35600  -1.52500  0.65300   1.000 75.44895  ?  523  ARG B NH2 1 
ATOM   1461 N  N   . PHE A 1 247 ? 31.99400  2.79600   4.88300   1.000 54.28139  ?  524  PHE B N   1 
ATOM   1462 C  CA  . PHE A 1 247 ? 30.70400  3.29500   4.41200   1.000 43.32528  ?  524  PHE B CA  1 
ATOM   1463 C  C   . PHE A 1 247 ? 30.79700  4.77400   4.06800   1.000 49.59845  ?  524  PHE B C   1 
ATOM   1464 O  O   . PHE A 1 247 ? 30.45000  5.19700   2.96200   1.000 52.41707  ?  524  PHE B O   1 
ATOM   1465 C  CB  . PHE A 1 247 ? 29.63100  3.06900   5.48400   1.000 45.96100  ?  524  PHE B CB  1 
ATOM   1466 C  CG  . PHE A 1 247 ? 28.18600  3.25300   4.99200   1.000 48.67730  ?  524  PHE B CG  1 
ATOM   1467 C  CD1 . PHE A 1 247 ? 27.86400  3.20500   3.63700   1.000 46.73092  ?  524  PHE B CD1 1 
ATOM   1468 C  CD2 . PHE A 1 247 ? 27.15700  3.45600   5.90500   1.000 44.55155  ?  524  PHE B CD2 1 
ATOM   1469 C  CE1 . PHE A 1 247 ? 26.55300  3.36300   3.21000   1.000 43.31605  ?  524  PHE B CE1 1 
ATOM   1470 C  CE2 . PHE A 1 247 ? 25.83700  3.59600   5.48500   1.000 43.12708  ?  524  PHE B CE2 1 
ATOM   1471 C  CZ  . PHE A 1 247 ? 25.54500  3.56300   4.12600   1.000 44.53374  ?  524  PHE B CZ  1 
ATOM   1472 N  N   . SER A 1 248 ? 31.26100  5.58000   5.01200   1.000 50.83586  ?  525  SER B N   1 
ATOM   1473 C  CA  . SER A 1 248 ? 31.38900  7.00200   4.74500   1.000 53.95988  ?  525  SER B CA  1 
ATOM   1474 C  C   . SER A 1 248 ? 32.20800  7.23800   3.48400   1.000 57.50719  ?  525  SER B C   1 
ATOM   1475 O  O   . SER A 1 248 ? 31.83700  8.04600   2.62900   1.000 58.66910  ?  525  SER B O   1 
ATOM   1476 C  CB  . SER A 1 248 ? 32.02600  7.69800   5.94900   1.000 48.82990  ?  525  SER B CB  1 
ATOM   1477 O  OG  . SER A 1 248 ? 32.10400  9.09300   5.72200   1.000 64.82806  ?  525  SER B OG  1 
ATOM   1478 N  N   . GLN A 1 249 ? 33.32900  6.52000   3.35200   1.000 56.39150  ?  526  GLN B N   1 
ATOM   1479 C  CA  . GLN A 1 249 ? 34.20600  6.68500   2.19400   1.000 55.38727  ?  526  GLN B CA  1 
ATOM   1480 C  C   . GLN A 1 249 ? 33.47800  6.34700   0.89600   1.000 58.86527  ?  526  GLN B C   1 
ATOM   1481 O  O   . GLN A 1 249 ? 33.59100  7.07400   -0.09600  1.000 56.68646  ?  526  GLN B O   1 
ATOM   1482 C  CB  . GLN A 1 249 ? 35.44600  5.81200   2.38300   1.000 50.52894  ?  526  GLN B CB  1 
ATOM   1483 C  CG  . GLN A 1 249 ? 36.43500  5.75800   1.23700   1.000 71.25860  ?  526  GLN B CG  1 
ATOM   1484 C  CD  . GLN A 1 249 ? 37.62900  4.85200   1.57100   1.000 79.70768  ?  526  GLN B CD  1 
ATOM   1485 O  OE1 . GLN A 1 249 ? 38.42000  5.15000   2.48300   1.000 81.00729  ?  526  GLN B OE1 1 
ATOM   1486 N  NE2 . GLN A 1 249 ? 37.73900  3.72700   0.85800   1.000 68.14415  ?  526  GLN B NE2 1 
ATOM   1487 N  N   . ALA A 1 250 ? 32.72300  5.25100   0.88800   1.000 56.23245  ?  527  ALA B N   1 
ATOM   1488 C  CA  . ALA A 1 250 ? 32.05300  4.85600   -0.36900  1.000 54.45446  ?  527  ALA B CA  1 
ATOM   1489 C  C   . ALA A 1 250 ? 30.99900  5.90900   -0.72600  1.000 60.59709  ?  527  ALA B C   1 
ATOM   1490 O  O   . ALA A 1 250 ? 30.78100  6.14400   -1.92900  1.000 58.12457  ?  527  ALA B O   1 
ATOM   1491 C  CB  . ALA A 1 250 ? 31.44500  3.49100   -0.22200  1.000 50.98667  ?  527  ALA B CB  1 
ATOM   1492 N  N   . LEU A 1 251 ? 30.38300  6.52400   0.28800   1.000 54.20585  ?  528  LEU B N   1 
ATOM   1493 C  CA  . LEU A 1 251 ? 29.32200  7.53800   0.04900   1.000 50.80781  ?  528  LEU B CA  1 
ATOM   1494 C  C   . LEU A 1 251 ? 29.94200  8.80100   -0.55700  1.000 60.55710  ?  528  LEU B C   1 
ATOM   1495 O  O   . LEU A 1 251 ? 29.33400  9.37100   -1.47900  1.000 63.60181  ?  528  LEU B O   1 
ATOM   1496 C  CB  . LEU A 1 251 ? 28.62000  7.84900   1.37400   1.000 50.90387  ?  528  LEU B CB  1 
ATOM   1497 C  CG  . LEU A 1 251 ? 27.67800  6.76200   1.88700   1.000 53.86784  ?  528  LEU B CG  1 
ATOM   1498 C  CD1 . LEU A 1 251 ? 26.92300  7.23800   3.11700   1.000 55.38229  ?  528  LEU B CD1 1 
ATOM   1499 C  CD2 . LEU A 1 251 ? 26.70500  6.33500   0.79900   1.000 49.89806  ?  528  LEU B CD2 1 
ATOM   1500 N  N   . LEU A 1 252 ? 31.10500  9.22200   -0.05400  1.000 57.62934  ?  529  LEU B N   1 
ATOM   1501 C  CA  . LEU A 1 252 ? 31.75600  10.40100  -0.62000  1.000 57.69343  ?  529  LEU B CA  1 
ATOM   1502 C  C   . LEU A 1 252 ? 32.31200  10.14000  -2.01300  1.000 60.98371  ?  529  LEU B C   1 
ATOM   1503 O  O   . LEU A 1 252 ? 32.46300  11.08000  -2.79500  1.000 66.28264  ?  529  LEU B O   1 
ATOM   1504 C  CB  . LEU A 1 252 ? 32.87500  10.89500  0.29500   1.000 58.22868  ?  529  LEU B CB  1 
ATOM   1505 C  CG  . LEU A 1 252 ? 32.34200  11.33500  1.65400   1.000 66.53197  ?  529  LEU B CG  1 
ATOM   1506 C  CD1 . LEU A 1 252 ? 33.43300  11.94400  2.49800   1.000 59.64511  ?  529  LEU B CD1 1 
ATOM   1507 C  CD2 . LEU A 1 252 ? 31.18300  12.30900  1.46300   1.000 60.95476  ?  529  LEU B CD2 1 
ATOM   1508 N  N   . LYS A 1 253 ? 32.65300  8.89700   -2.34300  1.000 58.56127  ?  530  LYS B N   1 
ATOM   1509 C  CA  . LYS A 1 253 ? 33.13900  8.62500   -3.69500  1.000 62.05667  ?  530  LYS B CA  1 
ATOM   1510 C  C   . LYS A 1 253 ? 32.00400  8.40000   -4.69500  1.000 65.90642  ?  530  LYS B C   1 
ATOM   1511 O  O   . LYS A 1 253 ? 32.28300  8.20400   -5.88200  1.000 69.31651  ?  530  LYS B O   1 
ATOM   1512 C  CB  . LYS A 1 253 ? 34.08400  7.40800   -3.71000  1.000 59.00956  ?  530  LYS B CB  1 
ATOM   1513 C  CG  . LYS A 1 253 ? 35.39100  7.58800   -2.94900  1.000 71.16658  ?  530  LYS B CG  1 
ATOM   1514 C  CD  . LYS A 1 253 ? 36.29900  6.35900   -3.10000  1.000 72.27709  ?  530  LYS B CD  1 
ATOM   1515 N  N   . GLY A 1 254 ? 30.75600  8.40500   -4.22900  1.000 62.35424  ?  531  GLY B N   1 
ATOM   1516 C  CA  . GLY A 1 254 ? 29.64000  8.09200   -5.14100  1.000 63.22953  ?  531  GLY B CA  1 
ATOM   1517 C  C   . GLY A 1 254 ? 29.17600  9.30000   -5.93000  1.000 63.38178  ?  531  GLY B C   1 
ATOM   1518 O  O   . GLY A 1 254 ? 29.83400  10.35400  -5.84500  1.000 63.86434  ?  531  GLY B O   1 
ATOM   1519 N  N   . ASP A 1 255 ? 28.07300  9.15300   -6.66800  1.000 65.97305  ?  532  ASP B N   1 
ATOM   1520 C  CA  . ASP A 1 255 ? 27.51300  10.28400  -7.45300  1.000 65.56081  ?  532  ASP B CA  1 
ATOM   1521 C  C   . ASP A 1 255 ? 26.73000  11.20900  -6.51600  1.000 57.79894  ?  532  ASP B C   1 
ATOM   1522 O  O   . ASP A 1 255 ? 26.70700  10.94000  -5.30000  1.000 64.97724  ?  532  ASP B O   1 
ATOM   1523 C  CB  . ASP A 1 255 ? 26.65900  9.78300   -8.62100  1.000 71.43187  ?  532  ASP B CB  1 
ATOM   1524 C  CG  . ASP A 1 255 ? 25.48800  8.90900   -8.20700  1.000 80.51081  ?  532  ASP B CG  1 
ATOM   1525 O  OD1 . ASP A 1 255 ? 25.32100  8.68400   -6.99400  1.000 82.42076  ?  532  ASP B OD1 1 
ATOM   1526 O  OD2 . ASP A 1 255 ? 24.75200  8.45700   -9.10500  1.000 87.29738  -1 532  ASP B OD2 1 
ATOM   1527 N  N   . LYS A 1 256 ? 26.09900  12.24500  -7.07000  1.000 63.92989  ?  533  LYS B N   1 
ATOM   1528 C  CA  . LYS A 1 256 ? 25.35500  13.22700  -6.23900  1.000 70.74003  ?  533  LYS B CA  1 
ATOM   1529 C  C   . LYS A 1 256 ? 24.31300  12.48900  -5.39200  1.000 62.15674  ?  533  LYS B C   1 
ATOM   1530 O  O   . LYS A 1 256 ? 24.12700  12.87500  -4.22400  1.000 64.12141  ?  533  LYS B O   1 
ATOM   1531 C  CB  . LYS A 1 256 ? 24.69500  14.27000  -7.14400  1.000 67.78809  ?  533  LYS B CB  1 
ATOM   1532 C  CG  . LYS A 1 256 ? 25.62100  14.90900  -8.16900  1.000 71.59193  ?  533  LYS B CG  1 
ATOM   1533 C  CD  . LYS A 1 256 ? 24.91400  15.86200  -9.10700  1.000 73.09608  ?  533  LYS B CD  1 
ATOM   1534 C  CE  . LYS A 1 256 ? 25.83300  16.44800  -10.15700 1.000 73.71033  ?  533  LYS B CE  1 
ATOM   1535 N  NZ  . LYS A 1 256 ? 25.11000  17.36300  -11.07100 1.000 89.23756  ?  533  LYS B NZ  1 
ATOM   1536 N  N   . SER A 1 257 ? 23.67800  11.46000  -5.95800  1.000 62.35256  ?  534  SER B N   1 
ATOM   1537 C  CA  . SER A 1 257 ? 22.62100  10.71000  -5.23200  1.000 66.45642  ?  534  SER B CA  1 
ATOM   1538 C  C   . SER A 1 257 ? 23.17100  10.12900  -3.92500  1.000 64.45278  ?  534  SER B C   1 
ATOM   1539 O  O   . SER A 1 257 ? 22.59400  10.42200  -2.86000  1.000 73.89440  ?  534  SER B O   1 
ATOM   1540 C  CB  . SER A 1 257 ? 22.05200  9.62600   -6.10600  1.000 63.26116  ?  534  SER B CB  1 
ATOM   1541 O  OG  . SER A 1 257 ? 21.58500  10.16200  -7.33400  1.000 75.61220  ?  534  SER B OG  1 
ATOM   1542 N  N   . VAL A 1 258 ? 24.24300  9.33800   -4.02400  1.000 58.32125  ?  535  VAL B N   1 
ATOM   1543 C  CA  . VAL A 1 258 ? 24.85000  8.64800   -2.84800  1.000 67.54593  ?  535  VAL B CA  1 
ATOM   1544 C  C   . VAL A 1 258 ? 25.50600  9.67400   -1.92300  1.000 56.61612  ?  535  VAL B C   1 
ATOM   1545 O  O   . VAL A 1 258 ? 25.56400  9.42100   -0.70700  1.000 65.79199  ?  535  VAL B O   1 
ATOM   1546 C  CB  . VAL A 1 258 ? 25.88000  7.63000   -3.37300  1.000 62.21260  ?  535  VAL B CB  1 
ATOM   1547 C  CG1 . VAL A 1 258 ? 26.40000  6.70400   -2.29500  1.000 61.77849  ?  535  VAL B CG1 1 
ATOM   1548 C  CG2 . VAL A 1 258 ? 25.33300  6.82900   -4.54200  1.000 50.09987  ?  535  VAL B CG2 1 
ATOM   1549 N  N   . ARG A 1 259 ? 25.97800  10.78600  -2.47900  1.000 57.34416  ?  536  ARG B N   1 
ATOM   1550 C  CA  . ARG A 1 259 ? 26.69900  11.82800  -1.70000  1.000 58.54849  ?  536  ARG B CA  1 
ATOM   1551 C  C   . ARG A 1 259 ? 25.69900  12.58800  -0.82100  1.000 58.77959  ?  536  ARG B C   1 
ATOM   1552 O  O   . ARG A 1 259 ? 26.06000  12.91900  0.32200   1.000 64.16927  ?  536  ARG B O   1 
ATOM   1553 C  CB  . ARG A 1 259 ? 27.48400  12.74900  -2.63900  1.000 59.32422  ?  536  ARG B CB  1 
ATOM   1554 C  CG  . ARG A 1 259 ? 28.99200  12.57000  -2.54600  1.000 66.11206  ?  536  ARG B CG  1 
ATOM   1555 C  CD  . ARG A 1 259 ? 29.74100  12.94500  -3.81000  1.000 61.85764  ?  536  ARG B CD  1 
ATOM   1556 N  NE  . ARG A 1 259 ? 29.35400  14.24000  -4.34900  1.000 71.22864  ?  536  ARG B NE  1 
ATOM   1557 C  CZ  . ARG A 1 259 ? 28.90400  14.43400  -5.58300  1.000 81.11519  ?  536  ARG B CZ  1 
ATOM   1558 N  NH1 . ARG A 1 259 ? 29.07400  13.50000  -6.50200  1.000 76.98607  ?  536  ARG B NH1 1 
ATOM   1559 N  NH2 . ARG A 1 259 ? 28.29600  15.56500  -5.89600  1.000 81.36186  ?  536  ARG B NH2 1 
ATOM   1560 N  N   . VAL A 1 260 ? 24.49200  12.84600  -1.33300  1.000 55.49884  ?  537  VAL B N   1 
ATOM   1561 C  CA  . VAL A 1 260 ? 23.44600  13.52800  -0.51300  1.000 60.01373  ?  537  VAL B CA  1 
ATOM   1562 C  C   . VAL A 1 260 ? 22.96000  12.55600  0.57000   1.000 57.94342  ?  537  VAL B C   1 
ATOM   1563 O  O   . VAL A 1 260 ? 22.59200  13.03000  1.66000   1.000 56.73565  ?  537  VAL B O   1 
ATOM   1564 C  CB  . VAL A 1 260 ? 22.28500  14.06800  -1.37300  1.000 65.72647  ?  537  VAL B CB  1 
ATOM   1565 C  CG1 . VAL A 1 260 ? 21.33400  12.97000  -1.82000  1.000 68.15122  ?  537  VAL B CG1 1 
ATOM   1566 C  CG2 . VAL A 1 260 ? 21.52000  15.16700  -0.65300  1.000 73.60408  ?  537  VAL B CG2 1 
ATOM   1567 N  N   . MET A 1 261 ? 22.99200  11.24900  0.28900   1.000 57.47256  ?  538  MET B N   1 
ATOM   1568 C  CA  . MET A 1 261 ? 22.60100  10.24100  1.30900   1.000 57.90818  ?  538  MET B CA  1 
ATOM   1569 C  C   . MET A 1 261 ? 23.46800  10.45500  2.55200   1.000 57.00012  ?  538  MET B C   1 
ATOM   1570 O  O   . MET A 1 261 ? 22.92500  10.39100  3.66900   1.000 47.91056  ?  538  MET B O   1 
ATOM   1571 C  CB  . MET A 1 261 ? 22.81800  8.81700   0.79000   1.000 59.40037  ?  538  MET B CB  1 
ATOM   1572 C  CG  . MET A 1 261 ? 21.72200  8.32200   -0.13200  1.000 69.48041  ?  538  MET B CG  1 
ATOM   1573 S  SD  . MET A 1 261 ? 22.01200  6.61400   -0.66100  1.000 70.95700  ?  538  MET B SD  1 
ATOM   1574 C  CE  . MET A 1 261 ? 21.38900  6.67500   -2.34000  1.000 76.37245  ?  538  MET B CE  1 
ATOM   1575 N  N   . ARG A 1 262 ? 24.76400  10.70700  2.35200   1.000 53.36898  ?  539  ARG B N   1 
ATOM   1576 C  CA  . ARG A 1 262 ? 25.69000  10.92900  3.49400   1.000 57.34009  ?  539  ARG B CA  1 
ATOM   1577 C  C   . ARG A 1 262 ? 25.15500  12.06300  4.37600   1.000 52.77448  ?  539  ARG B C   1 
ATOM   1578 O  O   . ARG A 1 262 ? 25.08600  11.86600  5.60200   1.000 50.50788  ?  539  ARG B O   1 
ATOM   1579 C  CB  . ARG A 1 262 ? 27.10000  11.24500  2.98700   1.000 58.41589  ?  539  ARG B CB  1 
ATOM   1580 C  CG  . ARG A 1 262 ? 28.10300  11.55300  4.08900   1.000 62.33871  ?  539  ARG B CG  1 
ATOM   1581 C  CD  . ARG A 1 262 ? 29.28000  10.59700  4.07400   1.000 74.33305  ?  539  ARG B CD  1 
ATOM   1582 N  NE  . ARG A 1 262 ? 30.31800  10.99400  5.01400   1.000 80.02725  ?  539  ARG B NE  1 
ATOM   1583 N  N   . SER A 1 263 ? 24.80200  13.20500  3.77900   1.000 47.76741  ?  540  SER B N   1 
ATOM   1584 C  CA  . SER A 1 263 ? 24.34800  14.32700  4.58800   1.000 57.49620  ?  540  SER B CA  1 
ATOM   1585 C  C   . SER A 1 263 ? 22.95100  14.08900  5.16400   1.000 54.31547  ?  540  SER B C   1 
ATOM   1586 O  O   . SER A 1 263 ? 22.65500  14.56200  6.26700   1.000 49.78556  ?  540  SER B O   1 
ATOM   1587 C  CB  . SER A 1 263 ? 24.39800  15.61800  3.77400   1.000 58.78538  ?  540  SER B CB  1 
ATOM   1588 O  OG  . SER A 1 263 ? 23.64000  15.47700  2.60500   1.000 66.86205  ?  540  SER B OG  1 
ATOM   1589 N  N   . LEU A 1 264 ? 22.09200  13.33500  4.47300   1.000 52.06390  ?  541  LEU B N   1 
ATOM   1590 C  CA  . LEU A 1 264 ? 20.84600  12.92500  5.11200   1.000 52.76866  ?  541  LEU B CA  1 
ATOM   1591 C  C   . LEU A 1 264 ? 21.12900  12.09800  6.36000   1.000 53.18248  ?  541  LEU B C   1 
ATOM   1592 O  O   . LEU A 1 264 ? 20.53400  12.33700  7.41900   1.000 52.30893  ?  541  LEU B O   1 
ATOM   1593 C  CB  . LEU A 1 264 ? 19.96000  12.16300  4.13100   1.000 53.08032  ?  541  LEU B CB  1 
ATOM   1594 C  CG  . LEU A 1 264 ? 19.52100  13.08600  2.99500   1.000 54.31813  ?  541  LEU B CG  1 
ATOM   1595 C  CD1 . LEU A 1 264 ? 18.79300  12.33100  1.88700   1.000 52.81876  ?  541  LEU B CD1 1 
ATOM   1596 C  CD2 . LEU A 1 264 ? 18.68200  14.21100  3.56200   1.000 52.14112  ?  541  LEU B CD2 1 
ATOM   1597 N  N   . LEU A 1 265 ? 22.05700  11.13300  6.26600   1.000 48.77612  ?  542  LEU B N   1 
ATOM   1598 C  CA  . LEU A 1 265 ? 22.42900  10.36600  7.45700   1.000 50.25004  ?  542  LEU B CA  1 
ATOM   1599 C  C   . LEU A 1 265 ? 22.96100  11.28200  8.54800   1.000 47.85961  ?  542  LEU B C   1 
ATOM   1600 O  O   . LEU A 1 265 ? 22.59600  11.14400  9.72100   1.000 46.33649  ?  542  LEU B O   1 
ATOM   1601 C  CB  . LEU A 1 265 ? 23.46700  9.29300   7.12400   1.000 46.18060  ?  542  LEU B CB  1 
ATOM   1602 C  CG  . LEU A 1 265 ? 22.96300  8.19100   6.20600   1.000 50.41636  ?  542  LEU B CG  1 
ATOM   1603 C  CD1 . LEU A 1 265 ? 24.15000  7.36700   5.72100   1.000 50.50892  ?  542  LEU B CD1 1 
ATOM   1604 C  CD2 . LEU A 1 265 ? 21.93400  7.33500   6.93800   1.000 43.29499  ?  542  LEU B CD2 1 
ATOM   1605 N  N   . ALA A 1 266 ? 23.81800  12.23200  8.17600   1.000 47.81279  ?  543  ALA B N   1 
ATOM   1606 C  CA  . ALA A 1 266 ? 24.32900  13.17700  9.15500   1.000 44.42707  ?  543  ALA B CA  1 
ATOM   1607 C  C   . ALA A 1 266 ? 23.19200  13.95800  9.80800   1.000 47.91547  ?  543  ALA B C   1 
ATOM   1608 O  O   . ALA A 1 266 ? 23.17900  14.13300  11.03400  1.000 49.62220  ?  543  ALA B O   1 
ATOM   1609 C  CB  . ALA A 1 266 ? 25.33800  14.11600  8.49200   1.000 43.01848  ?  543  ALA B CB  1 
ATOM   1610 N  N   . ALA A 1 267 ? 22.22400  14.42500  9.00900   1.000 44.06662  ?  544  ALA B N   1 
ATOM   1611 C  CA  . ALA A 1 267 ? 21.09500  15.17500  9.56200   1.000 49.75266  ?  544  ALA B CA  1 
ATOM   1612 C  C   . ALA A 1 267 ? 20.27600  14.32600  10.53700  1.000 52.18652  ?  544  ALA B C   1 
ATOM   1613 O  O   . ALA A 1 267 ? 19.85400  14.81600  11.59600  1.000 51.29608  ?  544  ALA B O   1 
ATOM   1614 C  CB  . ALA A 1 267 ? 20.19200  15.69600  8.43800   1.000 44.21872  ?  544  ALA B CB  1 
ATOM   1615 N  N   . GLN A 1 268 ? 20.02300  13.05800  10.19000  1.000 45.71355  ?  545  GLN B N   1 
ATOM   1616 C  CA  . GLN A 1 268 ? 19.32700  12.17000  11.12400  1.000 50.74680  ?  545  GLN B CA  1 
ATOM   1617 C  C   . GLN A 1 268 ? 20.10800  12.01300  12.41700  1.000 47.60809  ?  545  GLN B C   1 
ATOM   1618 O  O   . GLN A 1 268 ? 19.52100  11.97700  13.50100  1.000 47.70804  ?  545  GLN B O   1 
ATOM   1619 C  CB  . GLN A 1 268 ? 19.10500  10.78100  10.53100  1.000 47.73318  ?  545  GLN B CB  1 
ATOM   1620 C  CG  . GLN A 1 268 ? 18.19900  10.62400  9.33900   1.000 44.90509  ?  545  GLN B CG  1 
ATOM   1621 C  CD  . GLN A 1 268 ? 18.06900  9.14900   8.99000   1.000 49.16960  ?  545  GLN B CD  1 
ATOM   1622 O  OE1 . GLN A 1 268 ? 19.05500  8.48200   8.73400   1.000 59.82664  ?  545  GLN B OE1 1 
ATOM   1623 N  NE2 . GLN A 1 268 ? 16.86000  8.62600   9.03100   1.000 59.17481  ?  545  GLN B NE2 1 
ATOM   1624 N  N   . GLN A 1 269 ? 21.43400  11.87300  12.32500  1.000 45.99791  ?  546  GLN B N   1 
ATOM   1625 C  CA  . GLN A 1 269 ? 22.21900  11.63200  13.53100  1.000 48.82450  ?  546  GLN B CA  1 
ATOM   1626 C  C   . GLN A 1 269 ? 22.14000  12.81200  14.48700  1.000 50.14169  ?  546  GLN B C   1 
ATOM   1627 O  O   . GLN A 1 269 ? 21.96500  12.62100  15.69000  1.000 49.34161  ?  546  GLN B O   1 
ATOM   1628 C  CB  . GLN A 1 269 ? 23.67400  11.33600  13.18300  1.000 49.59840  ?  546  GLN B CB  1 
ATOM   1629 C  CG  . GLN A 1 269 ? 24.54300  11.01500  14.40400  1.000 44.84660  ?  546  GLN B CG  1 
ATOM   1630 C  CD  . GLN A 1 269 ? 24.09400  9.75100   15.11700  1.000 55.50332  ?  546  GLN B CD  1 
ATOM   1631 O  OE1 . GLN A 1 269 ? 24.23000  8.64600   14.58200  1.000 52.35290  ?  546  GLN B OE1 1 
ATOM   1632 N  NE2 . GLN A 1 269 ? 23.55200  9.90400   16.33600  1.000 50.16426  ?  546  GLN B NE2 1 
ATOM   1633 N  N   . THR A 1 270 ? 22.25400  14.04600  13.97300  1.000 53.74446  ?  547  THR B N   1 
ATOM   1634 C  CA  . THR A 1 270 ? 22.19900  15.21300  14.85900  1.000 53.19572  ?  547  THR B CA  1 
ATOM   1635 C  C   . THR A 1 270 ? 20.79600  15.43100  15.41500  1.000 53.45008  ?  547  THR B C   1 
ATOM   1636 O  O   . THR A 1 270 ? 20.64400  15.91400  16.54200  1.000 53.73698  ?  547  THR B O   1 
ATOM   1637 C  CB  . THR A 1 270 ? 22.67100  16.48300  14.12500  1.000 54.71292  ?  547  THR B CB  1 
ATOM   1638 O  OG1 . THR A 1 270 ? 21.77200  16.77900  13.05500  1.000 56.20740  ?  547  THR B OG1 1 
ATOM   1639 C  CG2 . THR A 1 270 ? 24.05200  16.28800  13.55400  1.000 53.44998  ?  547  THR B CG2 1 
ATOM   1640 N  N   . PHE A 1 271 ? 19.77800  15.04500  14.64200  1.000 45.29285  ?  548  PHE B N   1 
ATOM   1641 C  CA  . PHE A 1 271 ? 18.38100  15.14600  15.13800  1.000 48.64613  ?  548  PHE B CA  1 
ATOM   1642 C  C   . PHE A 1 271 ? 18.22600  14.22700  16.35700  1.000 50.94438  ?  548  PHE B C   1 
ATOM   1643 O  O   . PHE A 1 271 ? 17.67300  14.67600  17.37700  1.000 49.63273  ?  548  PHE B O   1 
ATOM   1644 C  CB  . PHE A 1 271 ? 17.39300  14.81500  14.01400  1.000 46.61871  ?  548  PHE B CB  1 
ATOM   1645 C  CG  . PHE A 1 271 ? 15.93500  15.04100  14.33100  1.000 55.46277  ?  548  PHE B CG  1 
ATOM   1646 C  CD1 . PHE A 1 271 ? 15.26900  14.24500  15.25000  1.000 49.67396  ?  548  PHE B CD1 1 
ATOM   1647 C  CD2 . PHE A 1 271 ? 15.22600  16.05500  13.70800  1.000 49.49757  ?  548  PHE B CD2 1 
ATOM   1648 C  CE1 . PHE A 1 271 ? 13.92900  14.45700  15.53500  1.000 49.75349  ?  548  PHE B CE1 1 
ATOM   1649 C  CE2 . PHE A 1 271 ? 13.88600  16.26600  13.99400  1.000 53.82079  ?  548  PHE B CE2 1 
ATOM   1650 C  CZ  . PHE A 1 271 ? 13.24000  15.46700  14.90600  1.000 52.25543  ?  548  PHE B CZ  1 
ATOM   1651 N  N   . VAL A 1 272 ? 18.71100  12.98500  16.25500  1.000 45.40300  ?  549  VAL B N   1 
ATOM   1652 C  CA  . VAL A 1 272 ? 18.60500  12.06500  17.38000  1.000 48.60907  ?  549  VAL B CA  1 
ATOM   1653 C  C   . VAL A 1 272 ? 19.41900  12.57700  18.57100  1.000 47.05033  ?  549  VAL B C   1 
ATOM   1654 O  O   . VAL A 1 272 ? 18.97300  12.49700  19.71500  1.000 47.77049  ?  549  VAL B O   1 
ATOM   1655 C  CB  . VAL A 1 272 ? 19.01300  10.63300  16.95000  1.000 43.97183  ?  549  VAL B CB  1 
ATOM   1656 C  CG1 . VAL A 1 272 ? 19.15000  9.71400   18.15000  1.000 41.11273  ?  549  VAL B CG1 1 
ATOM   1657 C  CG2 . VAL A 1 272 ? 18.00200  10.06500  15.99800  1.000 35.81783  ?  549  VAL B CG2 1 
ATOM   1658 N  N   . ASP A 1 273 ? 20.60500  13.13900  18.32900  1.000 50.04188  ?  550  ASP B N   1 
ATOM   1659 C  CA  . ASP A 1 273 ? 21.37400  13.70400  19.43500  1.000 49.35714  ?  550  ASP B CA  1 
ATOM   1660 C  C   . ASP A 1 273 ? 20.60300  14.81000  20.14500  1.000 53.94482  ?  550  ASP B C   1 
ATOM   1661 O  O   . ASP A 1 273 ? 20.65900  14.91600  21.37700  1.000 53.35799  ?  550  ASP B O   1 
ATOM   1662 C  CB  . ASP A 1 273 ? 22.70700  14.25100  18.94400  1.000 47.12314  ?  550  ASP B CB  1 
ATOM   1663 C  CG  . ASP A 1 273 ? 23.53800  13.20500  18.25700  1.000 61.48148  ?  550  ASP B CG  1 
ATOM   1664 O  OD1 . ASP A 1 273 ? 23.37900  12.00400  18.58600  1.000 64.75712  ?  550  ASP B OD1 1 
ATOM   1665 O  OD2 . ASP A 1 273 ? 24.35000  13.58800  17.38200  1.000 67.10623  -1 550  ASP B OD2 1 
ATOM   1666 N  N   . ARG A 1 274 ? 19.91900  15.66800  19.37200  1.000 51.75302  ?  551  ARG B N   1 
ATOM   1667 C  CA  . ARG A 1 274 ? 19.11300  16.74600  19.94000  1.000 60.19909  ?  551  ARG B CA  1 
ATOM   1668 C  C   . ARG A 1 274 ? 17.91800  16.19100  20.70800  1.000 60.75067  ?  551  ARG B C   1 
ATOM   1669 O  O   . ARG A 1 274 ? 17.58200  16.68400  21.79600  1.000 58.87070  ?  551  ARG B O   1 
ATOM   1670 C  CB  . ARG A 1 274 ? 18.63500  17.69600  18.83600  1.000 58.83412  ?  551  ARG B CB  1 
ATOM   1671 C  CG  . ARG A 1 274 ? 19.72100  18.55000  18.19200  1.000 67.12875  ?  551  ARG B CG  1 
ATOM   1672 C  CD  . ARG A 1 274 ? 19.17200  19.75500  17.38200  1.000 77.17193  ?  551  ARG B CD  1 
ATOM   1673 N  NE  . ARG A 1 274 ? 18.34200  19.39700  16.23100  1.000 76.39375  ?  551  ARG B NE  1 
ATOM   1674 C  CZ  . ARG A 1 274 ? 18.79700  19.19800  14.99900  1.000 76.72140  ?  551  ARG B CZ  1 
ATOM   1675 N  NH1 . ARG A 1 274 ? 20.08900  19.30000  14.71400  1.000 78.79061  ?  551  ARG B NH1 1 
ATOM   1676 N  NH2 . ARG A 1 274 ? 17.93700  18.87500  14.03100  1.000 62.24988  ?  551  ARG B NH2 1 
ATOM   1677 N  N   . LEU A 1 275 ? 17.26500  15.16800  20.15600  1.000 53.20498  ?  552  LEU B N   1 
ATOM   1678 C  CA  . LEU A 1 275 ? 16.17900  14.51800  20.87600  1.000 56.35953  ?  552  LEU B CA  1 
ATOM   1679 C  C   . LEU A 1 275 ? 16.68300  13.92400  22.18900  1.000 55.03140  ?  552  LEU B C   1 
ATOM   1680 O  O   . LEU A 1 275 ? 16.08300  14.13300  23.25500  1.000 54.75807  ?  552  LEU B O   1 
ATOM   1681 C  CB  . LEU A 1 275 ? 15.54400  13.45100  19.99100  1.000 50.39799  ?  552  LEU B CB  1 
ATOM   1682 C  CG  . LEU A 1 275 ? 14.16700  12.97100  20.43000  1.000 55.26318  ?  552  LEU B CG  1 
ATOM   1683 C  CD1 . LEU A 1 275 ? 13.25100  14.17500  20.60100  1.000 56.05302  ?  552  LEU B CD1 1 
ATOM   1684 C  CD2 . LEU A 1 275 ? 13.58600  11.99100  19.41600  1.000 53.34062  ?  552  LEU B CD2 1 
ATOM   1685 N  N   . VAL A 1 276 ? 17.80100  13.19600  22.13700  1.000 49.13900  ?  553  VAL B N   1 
ATOM   1686 C  CA  . VAL A 1 276 ? 18.36900  12.65200  23.36500  1.000 51.62937  ?  553  VAL B CA  1 
ATOM   1687 C  C   . VAL A 1 276 ? 18.60200  13.77000  24.37200  1.000 56.18480  ?  553  VAL B C   1 
ATOM   1688 O  O   . VAL A 1 276 ? 18.22600  13.67000  25.54300  1.000 58.33365  ?  553  VAL B O   1 
ATOM   1689 C  CB  . VAL A 1 276 ? 19.66600  11.88100  23.06900  1.000 47.60465  ?  553  VAL B CB  1 
ATOM   1690 C  CG1 . VAL A 1 276 ? 20.41600  11.61200  24.36200  1.000 46.65535  ?  553  VAL B CG1 1 
ATOM   1691 C  CG2 . VAL A 1 276 ? 19.36400  10.57300  22.33700  1.000 47.20616  ?  553  VAL B CG2 1 
ATOM   1692 N  N   . HIS A 1 277 ? 19.20700  14.86300  23.92300  1.000 55.25379  ?  554  HIS B N   1 
ATOM   1693 C  CA  . HIS A 1 277 ? 19.48600  15.97800  24.81900  1.000 60.50764  ?  554  HIS B CA  1 
ATOM   1694 C  C   . HIS A 1 277 ? 18.20000  16.57000  25.39800  1.000 61.00172  ?  554  HIS B C   1 
ATOM   1695 O  O   . HIS A 1 277 ? 18.17100  17.00200  26.55600  1.000 55.08279  ?  554  HIS B O   1 
ATOM   1696 C  CB  . HIS A 1 277 ? 20.29300  17.03600  24.06600  1.000 60.30604  ?  554  HIS B CB  1 
ATOM   1697 C  CG  . HIS A 1 277 ? 20.62300  18.24100  24.88600  1.000 69.90814  ?  554  HIS B CG  1 
ATOM   1698 N  ND1 . HIS A 1 277 ? 19.89800  19.41100  24.81000  1.000 73.04824  ?  554  HIS B ND1 1 
ATOM   1699 C  CD2 . HIS A 1 277 ? 21.60400  18.46200  25.79200  1.000 74.78488  ?  554  HIS B CD2 1 
ATOM   1700 C  CE1 . HIS A 1 277 ? 20.41800  20.30200  25.63500  1.000 80.69060  ?  554  HIS B CE1 1 
ATOM   1701 N  NE2 . HIS A 1 277 ? 21.45900  19.75500  26.23700  1.000 80.19008  ?  554  HIS B NE2 1 
ATOM   1702 N  N   . LEU A 1 278 ? 17.12800  16.60600  24.60700  1.000 56.00342  ?  555  LEU B N   1 
ATOM   1703 C  CA  . LEU A 1 278 ? 15.87000  17.13800  25.11300  1.000 58.93796  ?  555  LEU B CA  1 
ATOM   1704 C  C   . LEU A 1 278 ? 15.29400  16.25000  26.22100  1.000 60.93371  ?  555  LEU B C   1 
ATOM   1705 O  O   . LEU A 1 278 ? 14.93300  16.73600  27.30300  1.000 63.39211  ?  555  LEU B O   1 
ATOM   1706 C  CB  . LEU A 1 278 ? 14.88600  17.29700  23.95500  1.000 63.68097  ?  555  LEU B CB  1 
ATOM   1707 C  CG  . LEU A 1 278 ? 13.56700  18.00500  24.27200  1.000 70.64752  ?  555  LEU B CG  1 
ATOM   1708 C  CD2 . LEU A 1 278 ? 12.41900  17.19600  23.70300  1.000 66.30399  ?  555  LEU B CD2 1 
ATOM   1709 N  N   . MET A 1 279 ? 15.21800  14.93900  25.98100  1.000 55.84501  ?  556  MET B N   1 
ATOM   1710 C  CA  . MET A 1 279 ? 14.74500  14.02400  27.01500  1.000 55.20185  ?  556  MET B CA  1 
ATOM   1711 C  C   . MET A 1 279 ? 15.47100  14.24400  28.33700  1.000 59.16552  ?  556  MET B C   1 
ATOM   1712 O  O   . MET A 1 279 ? 14.85600  14.20100  29.41300  1.000 56.64801  ?  556  MET B O   1 
ATOM   1713 C  CB  . MET A 1 279 ? 14.91900  12.58300  26.54600  1.000 53.64487  ?  556  MET B CB  1 
ATOM   1714 C  CG  . MET A 1 279 ? 14.04400  12.21400  25.35800  1.000 54.28020  ?  556  MET B CG  1 
ATOM   1715 S  SD  . MET A 1 279 ? 12.31200  12.07100  25.82200  1.000 64.87286  ?  556  MET B SD  1 
ATOM   1716 C  CE  . MET A 1 279 ? 11.59600  13.32400  24.78600  1.000 56.55166  ?  556  MET B CE  1 
ATOM   1717 N  N   . LYS A 1 280 ? 16.78600  14.47600  28.28300  1.000 57.42181  ?  557  LYS B N   1 
ATOM   1718 C  CA  . LYS A 1 280 ? 17.52500  14.67700  29.52400  1.000 60.23611  ?  557  LYS B CA  1 
ATOM   1719 C  C   . LYS A 1 280 ? 17.14000  15.99300  30.18500  1.000 62.70408  ?  557  LYS B C   1 
ATOM   1720 O  O   . LYS A 1 280 ? 17.09200  16.08400  31.42200  1.000 62.40925  ?  557  LYS B O   1 
ATOM   1721 C  CB  . LYS A 1 280 ? 19.02700  14.62600  29.26500  1.000 58.78257  ?  557  LYS B CB  1 
ATOM   1722 C  CG  . LYS A 1 280 ? 19.53900  13.26100  28.90800  1.000 63.55472  ?  557  LYS B CG  1 
ATOM   1723 C  CD  . LYS A 1 280 ? 21.00700  13.32600  28.52400  1.000 63.44145  ?  557  LYS B CD  1 
ATOM   1724 C  CE  . LYS A 1 280 ? 21.46100  12.02700  27.87700  1.000 60.54425  ?  557  LYS B CE  1 
ATOM   1725 N  NZ  . LYS A 1 280 ? 22.81200  12.18200  27.28900  1.000 75.76369  ?  557  LYS B NZ  1 
ATOM   1726 N  N   . ALA A 1 281 ? 16.86500  17.02100  29.37400  1.000 55.83878  ?  558  ALA B N   1 
ATOM   1727 C  CA  . ALA A 1 281 ? 16.50900  18.33000  29.90400  1.000 59.18400  ?  558  ALA B CA  1 
ATOM   1728 C  C   . ALA A 1 281 ? 15.19100  18.27200  30.66400  1.000 62.09678  ?  558  ALA B C   1 
ATOM   1729 O  O   . ALA A 1 281 ? 15.05300  18.87200  31.73600  1.000 57.60534  ?  558  ALA B O   1 
ATOM   1730 C  CB  . ALA A 1 281 ? 16.43700  19.34900  28.76500  1.000 55.46959  ?  558  ALA B CB  1 
ATOM   1731 N  N   . VAL A 1 282 ? 14.21300  17.53500  30.13200  1.000 60.23897  ?  559  VAL B N   1 
ATOM   1732 C  CA  . VAL A 1 282 ? 12.95000  17.37000  30.84100  1.000 60.36788  ?  559  VAL B CA  1 
ATOM   1733 C  C   . VAL A 1 282 ? 13.16500  16.78000  32.23200  1.000 58.06884  ?  559  VAL B C   1 
ATOM   1734 O  O   . VAL A 1 282 ? 12.46800  17.15000  33.18300  1.000 61.33072  ?  559  VAL B O   1 
ATOM   1735 C  CB  . VAL A 1 282 ? 11.99400  16.51700  29.99500  1.000 53.68341  ?  559  VAL B CB  1 
ATOM   1736 C  CG1 . VAL A 1 282 ? 10.71500  16.28500  30.73500  1.000 56.39650  ?  559  VAL B CG1 1 
ATOM   1737 C  CG2 . VAL A 1 282 ? 11.72900  17.22400  28.69800  1.000 53.28928  ?  559  VAL B CG2 1 
ATOM   1738 N  N   . GLN A 1 283 ? 14.15700  15.91100  32.39100  1.000 56.07692  ?  560  GLN B N   1 
ATOM   1739 C  CA  . GLN A 1 283 ? 14.35600  15.13800  33.60900  1.000 58.26360  ?  560  GLN B CA  1 
ATOM   1740 C  C   . GLN A 1 283 ? 15.36500  15.75300  34.56600  1.000 67.29778  ?  560  GLN B C   1 
ATOM   1741 O  O   . GLN A 1 283 ? 15.69700  15.12800  35.57800  1.000 71.60302  ?  560  GLN B O   1 
ATOM   1742 C  CB  . GLN A 1 283 ? 14.80300  13.72800  33.24400  1.000 52.31463  ?  560  GLN B CB  1 
ATOM   1743 C  CG  . GLN A 1 283 ? 13.81000  13.02500  32.33300  1.000 50.48213  ?  560  GLN B CG  1 
ATOM   1744 C  CD  . GLN A 1 283 ? 12.52800  12.70000  33.06600  1.000 57.22841  ?  560  GLN B CD  1 
ATOM   1745 O  OE1 . GLN A 1 283 ? 12.43800  12.86900  34.29400  1.000 55.84809  ?  560  GLN B OE1 1 
ATOM   1746 N  NE2 . GLN A 1 283 ? 11.53100  12.22600  32.33300  1.000 53.49734  ?  560  GLN B NE2 1 
ATOM   1747 N  N   . ARG A 1 284 ? 15.86200  16.95400  34.27700  1.000 69.08592  ?  561  ARG B N   1 
ATOM   1748 C  CA  . ARG A 1 284 ? 16.94800  17.52500  35.07100  1.000 72.71126  ?  561  ARG B CA  1 
ATOM   1749 C  C   . ARG A 1 284 ? 16.49700  17.83100  36.48900  1.000 77.52713  ?  561  ARG B C   1 
ATOM   1750 O  O   . ARG A 1 284 ? 17.19200  17.50900  37.46000  1.000 72.43262  ?  561  ARG B O   1 
ATOM   1751 C  CB  . ARG A 1 284 ? 17.46300  18.80200  34.41200  1.000 71.83567  ?  561  ARG B CB  1 
ATOM   1752 C  CG  . ARG A 1 284 ? 18.80100  18.66300  33.79100  1.000 74.76372  ?  561  ARG B CG  1 
ATOM   1753 C  CD  . ARG A 1 284 ? 19.17700  19.91600  33.06200  1.000 79.45662  ?  561  ARG B CD  1 
ATOM   1754 N  NE  . ARG A 1 284 ? 20.27100  19.63100  32.14800  1.000 84.84160  ?  561  ARG B NE  1 
ATOM   1755 C  CZ  . ARG A 1 284 ? 20.88600  20.53300  31.40100  1.000 84.80846  ?  561  ARG B CZ  1 
ATOM   1756 N  NH1 . ARG A 1 284 ? 20.55600  21.81400  31.45300  1.000 88.21982  ?  561  ARG B NH1 1 
ATOM   1757 N  NH2 . ARG A 1 284 ? 21.85500  20.13800  30.58200  1.000 86.47777  ?  561  ARG B NH2 1 
ATOM   1758 N  N   . GLU A 1 285 ? 15.36500  18.50900  36.61800  1.000 76.84563  ?  562  GLU B N   1 
ATOM   1759 C  CA  . GLU A 1 285 ? 14.75200  18.83500  37.88700  1.000 72.70651  ?  562  GLU B CA  1 
ATOM   1760 C  C   . GLU A 1 285 ? 13.50300  17.97200  38.07000  1.000 75.99627  ?  562  GLU B C   1 
ATOM   1761 O  O   . GLU A 1 285 ? 13.00300  17.33400  37.13500  1.000 70.47479  ?  562  GLU B O   1 
ATOM   1762 C  CB  . GLU A 1 285 ? 14.42400  20.33200  37.95100  1.000 73.05867  ?  562  GLU B CB  1 
ATOM   1763 C  CG  . GLU A 1 285 ? 15.64900  21.24000  37.88300  1.000 79.96157  ?  562  GLU B CG  1 
ATOM   1764 N  N   . SER A 1 286 ? 13.00500  17.94100  39.29800  1.000 75.63115  ?  563  SER B N   1 
ATOM   1765 C  CA  . SER A 1 286 ? 11.82200  17.14600  39.57300  1.000 71.44353  ?  563  SER B CA  1 
ATOM   1766 C  C   . SER A 1 286 ? 10.56100  17.92000  39.19700  1.000 69.98714  ?  563  SER B C   1 
ATOM   1767 O  O   . SER A 1 286 ? 10.53700  19.15400  39.16400  1.000 75.40402  ?  563  SER B O   1 
ATOM   1768 C  CB  . SER A 1 286 ? 11.77700  16.73300  41.04700  1.000 67.71284  ?  563  SER B CB  1 
ATOM   1769 O  OG  . SER A 1 286 ? 11.74400  17.88300  41.88700  1.000 72.55832  ?  563  SER B OG  1 
ATOM   1770 N  N   . GLY A 1 287 ? 9.51700   17.16400  38.90200  1.000 64.11280  ?  564  GLY B N   1 
ATOM   1771 C  CA  . GLY A 1 287 ? 8.20300   17.72200  38.65500  1.000 60.36424  ?  564  GLY B CA  1 
ATOM   1772 C  C   . GLY A 1 287 ? 7.26700   16.57100  38.36000  1.000 57.85811  ?  564  GLY B C   1 
ATOM   1773 O  O   . GLY A 1 287 ? 7.70600   15.46100  38.03900  1.000 54.37357  ?  564  GLY B O   1 
ATOM   1774 N  N   . ASN A 1 288 ? 5.96800   16.84500  38.50000  1.000 56.74351  ?  565  ASN B N   1 
ATOM   1775 C  CA  . ASN A 1 288 ? 4.99900   15.79900  38.20200  1.000 53.97991  ?  565  ASN B CA  1 
ATOM   1776 C  C   . ASN A 1 288 ? 4.85200   15.65400  36.68900  1.000 53.65383  ?  565  ASN B C   1 
ATOM   1777 O  O   . ASN A 1 288 ? 5.48100   16.37100  35.90800  1.000 55.16061  ?  565  ASN B O   1 
ATOM   1778 C  CB  . ASN A 1 288 ? 3.66200   16.06700  38.89900  1.000 53.62906  ?  565  ASN B CB  1 
ATOM   1779 C  CG  . ASN A 1 288 ? 2.98900   17.34900  38.43100  1.000 63.89421  ?  565  ASN B CG  1 
ATOM   1780 O  OD1 . ASN A 1 288 ? 3.07800   17.72900  37.26400  1.000 56.13208  ?  565  ASN B OD1 1 
ATOM   1781 N  ND2 . ASN A 1 288 ? 2.29000   18.01600  39.35700  1.000 61.40142  ?  565  ASN B ND2 1 
ATOM   1782 N  N   . ARG A 1 289 ? 4.03000   14.69900  36.25600  1.000 52.62415  ?  566  ARG B N   1 
ATOM   1783 C  CA  . ARG A 1 289 ? 4.00400   14.37200  34.83800  1.000 52.21187  ?  566  ARG B CA  1 
ATOM   1784 C  C   . ARG A 1 289 ? 3.49200   15.54500  34.01200  1.000 54.35553  ?  566  ARG B C   1 
ATOM   1785 O  O   . ARG A 1 289 ? 3.97500   15.79400  32.90100  1.000 56.75889  ?  566  ARG B O   1 
ATOM   1786 C  CB  . ARG A 1 289 ? 3.16800   13.11700  34.59600  1.000 50.90298  ?  566  ARG B CB  1 
ATOM   1787 C  CG  . ARG A 1 289 ? 3.27500   12.60100  33.16800  1.000 52.28100  ?  566  ARG B CG  1 
ATOM   1788 C  CD  . ARG A 1 289 ? 3.01100   11.11100  33.09100  1.000 54.55791  ?  566  ARG B CD  1 
ATOM   1789 N  NE  . ARG A 1 289 ? 1.90100   10.75100  33.95500  1.000 53.90785  ?  566  ARG B NE  1 
ATOM   1790 C  CZ  . ARG A 1 289 ? 0.62900   10.76900  33.58600  1.000 58.94178  ?  566  ARG B CZ  1 
ATOM   1791 N  NH1 . ARG A 1 289 ? 0.27900   11.03500  32.33800  1.000 55.71454  ?  566  ARG B NH1 1 
ATOM   1792 N  NH2 . ARG A 1 289 ? -0.31500  10.53400  34.49900  1.000 55.73818  ?  566  ARG B NH2 1 
ATOM   1793 N  N   . LYS A 1 290 ? 2.52700   16.28600  34.54400  1.000 52.35051  ?  567  LYS B N   1 
ATOM   1794 C  CA  . LYS A 1 290 ? 2.02700   17.47000  33.85800  1.000 57.89238  ?  567  LYS B CA  1 
ATOM   1795 C  C   . LYS A 1 290 ? 3.14200   18.49600  33.66600  1.000 60.92941  ?  567  LYS B C   1 
ATOM   1796 O  O   . LYS A 1 290 ? 3.35100   19.00100  32.55700  1.000 64.76424  ?  567  LYS B O   1 
ATOM   1797 C  CB  . LYS A 1 290 ? 0.85400   18.05200  34.65400  1.000 60.05027  ?  567  LYS B CB  1 
ATOM   1798 C  CG  . LYS A 1 290 ? 0.12100   19.23100  34.03500  1.000 69.61264  ?  567  LYS B CG  1 
ATOM   1799 C  CD  . LYS A 1 290 ? -0.97100  19.71900  34.98800  1.000 76.10843  ?  567  LYS B CD  1 
ATOM   1800 C  CE  . LYS A 1 290 ? -1.66000  20.99300  34.50300  1.000 81.51670  ?  567  LYS B CE  1 
ATOM   1801 N  NZ  . LYS A 1 290 ? -2.66100  21.45900  35.51700  1.000 97.32470  ?  567  LYS B NZ  1 
ATOM   1802 N  N   . LYS A 1 291 ? 3.88500   18.80200  34.73800  1.000 59.19967  ?  568  LYS B N   1 
ATOM   1803 C  CA  . LYS A 1 291 ? 5.01400   19.72800  34.64100  1.000 58.75891  ?  568  LYS B CA  1 
ATOM   1804 C  C   . LYS A 1 291 ? 6.06400   19.23900  33.64700  1.000 60.47023  ?  568  LYS B C   1 
ATOM   1805 O  O   . LYS A 1 291 ? 6.66500   20.04100  32.92400  1.000 62.10914  ?  568  LYS B O   1 
ATOM   1806 C  CB  . LYS A 1 291 ? 5.64500   19.93000  36.02000  1.000 59.46998  ?  568  LYS B CB  1 
ATOM   1807 C  CG  . LYS A 1 291 ? 7.12600   20.27700  36.00700  1.000 65.77381  ?  568  LYS B CG  1 
ATOM   1808 C  CD  . LYS A 1 291 ? 7.35300   21.76200  35.83400  1.000 70.57717  ?  568  LYS B CD  1 
ATOM   1809 C  CE  . LYS A 1 291 ? 6.53800   22.55400  36.87100  1.000 85.17591  ?  568  LYS B CE  1 
ATOM   1810 N  NZ  . LYS A 1 291 ? 6.62800   24.06200  36.69400  1.000 86.97267  ?  568  LYS B NZ  1 
ATOM   1811 N  N   . LYS A 1 292 ? 6.31000   17.92900  33.60300  1.000 55.15967  ?  569  LYS B N   1 
ATOM   1812 C  CA  . LYS A 1 292 ? 7.33800   17.41800  32.70900  1.000 54.35747  ?  569  LYS B CA  1 
ATOM   1813 C  C   . LYS A 1 292 ? 6.87000   17.46900  31.26000  1.000 57.74660  ?  569  LYS B C   1 
ATOM   1814 O  O   . LYS A 1 292 ? 7.66200   17.77100  30.36000  1.000 51.61836  ?  569  LYS B O   1 
ATOM   1815 C  CB  . LYS A 1 292 ? 7.75000   15.99800  33.11800  1.000 45.93519  ?  569  LYS B CB  1 
ATOM   1816 C  CG  . LYS A 1 292 ? 8.83400   15.98300  34.22100  1.000 52.24578  ?  569  LYS B CG  1 
ATOM   1817 C  CD  . LYS A 1 292 ? 8.80000   14.72200  35.06300  1.000 54.35208  ?  569  LYS B CD  1 
ATOM   1818 C  CE  . LYS A 1 292 ? 10.18100  14.13700  35.27200  1.000 54.24804  ?  569  LYS B CE  1 
ATOM   1819 N  NZ  . LYS A 1 292 ? 10.84300  14.69500  36.46000  1.000 59.11844  ?  569  LYS B NZ  1 
ATOM   1820 N  N   . ASN A 1 293 ? 5.58400   17.20000  31.01300  1.000 52.87517  ?  570  ASN B N   1 
ATOM   1821 C  CA  . ASN A 1 293 ? 5.05200   17.36400  29.66500  1.000 52.85653  ?  570  ASN B CA  1 
ATOM   1822 C  C   . ASN A 1 293 ? 5.21500   18.80900  29.18600  1.000 62.68637  ?  570  ASN B C   1 
ATOM   1823 O  O   . ASN A 1 293 ? 5.65800   19.05900  28.05700  1.000 58.33010  ?  570  ASN B O   1 
ATOM   1824 C  CB  . ASN A 1 293 ? 3.58300   16.94200  29.62400  1.000 49.14370  ?  570  ASN B CB  1 
ATOM   1825 C  CG  . ASN A 1 293 ? 3.39600   15.40300  29.69700  1.000 53.63129  ?  570  ASN B CG  1 
ATOM   1826 O  OD1 . ASN A 1 293 ? 4.29100   14.62500  29.35100  1.000 49.51015  ?  570  ASN B OD1 1 
ATOM   1827 N  ND2 . ASN A 1 293 ? 2.22100   14.97600  30.13300  1.000 48.92619  ?  570  ASN B ND2 1 
ATOM   1828 N  N   . GLU A 1 294 ? 4.90400   19.77600  30.04900  1.000 54.96791  ?  571  GLU B N   1 
ATOM   1829 C  CA  . GLU A 1 294 ? 5.04500   21.16600  29.64600  1.000 57.18780  ?  571  GLU B CA  1 
ATOM   1830 C  C   . GLU A 1 294 ? 6.49800   21.50800  29.34300  1.000 59.04806  ?  571  GLU B C   1 
ATOM   1831 O  O   . GLU A 1 294 ? 6.77500   22.28100  28.41900  1.000 63.36001  ?  571  GLU B O   1 
ATOM   1832 C  CB  . GLU A 1 294 ? 4.47300   22.07700  30.72700  1.000 55.61134  ?  571  GLU B CB  1 
ATOM   1833 C  CG  . GLU A 1 294 ? 2.99400   21.87500  30.89700  1.000 60.28848  ?  571  GLU B CG  1 
ATOM   1834 C  CD  . GLU A 1 294 ? 2.45800   22.48100  32.19500  1.000 80.56654  ?  571  GLU B CD  1 
ATOM   1835 O  OE1 . GLU A 1 294 ? 3.22300   23.15600  32.93400  1.000 72.31089  ?  571  GLU B OE1 1 
ATOM   1836 O  OE2 . GLU A 1 294 ? 1.25300   22.28500  32.47500  1.000 82.37253  -1 571  GLU B OE2 1 
ATOM   1837 N  N   . ARG A 1 295 ? 7.44700   20.95400  30.10300  1.000 57.72642  ?  572  ARG B N   1 
ATOM   1838 C  CA  . ARG A 1 295 ? 8.84700   21.14400  29.73200  1.000 56.13778  ?  572  ARG B CA  1 
ATOM   1839 C  C   . ARG A 1 295 ? 9.10900   20.55100  28.35900  1.000 60.59270  ?  572  ARG B C   1 
ATOM   1840 O  O   . ARG A 1 295 ? 9.69200   21.20600  27.48300  1.000 67.30306  ?  572  ARG B O   1 
ATOM   1841 C  CB  . ARG A 1 295 ? 9.78100   20.50800  30.75800  1.000 58.42836  ?  572  ARG B CB  1 
ATOM   1842 C  CG  . ARG A 1 295 ? 9.75800   21.12000  32.15600  1.000 64.36472  ?  572  ARG B CG  1 
ATOM   1843 C  CD  . ARG A 1 295 ? 10.62800  20.27500  33.05900  1.000 63.20116  ?  572  ARG B CD  1 
ATOM   1844 N  NE  . ARG A 1 295 ? 10.51800  20.64900  34.45900  1.000 68.76864  ?  572  ARG B NE  1 
ATOM   1845 C  CZ  . ARG A 1 295 ? 10.90000  19.87900  35.46500  1.000 66.44565  ?  572  ARG B CZ  1 
ATOM   1846 N  NH1 . ARG A 1 295 ? 11.33300  18.64500  35.26000  1.000 60.87517  ?  572  ARG B NH1 1 
ATOM   1847 N  NH2 . ARG A 1 295 ? 10.84000  20.35900  36.70300  1.000 68.86931  ?  572  ARG B NH2 1 
ATOM   1848 N  N   . LEU A 1 296 ? 8.67900   19.30000  28.15700  1.000 56.17567  ?  573  LEU B N   1 
ATOM   1849 C  CA  . LEU A 1 296 ? 8.80700   18.64700  26.85800  1.000 57.21610  ?  573  LEU B CA  1 
ATOM   1850 C  C   . LEU A 1 296 ? 8.21800   19.50500  25.74100  1.000 63.46589  ?  573  LEU B C   1 
ATOM   1851 O  O   . LEU A 1 296 ? 8.85200   19.71900  24.70200  1.000 58.71853  ?  573  LEU B O   1 
ATOM   1852 C  CB  . LEU A 1 296 ? 8.11800   17.28400  26.88900  1.000 53.43743  ?  573  LEU B CB  1 
ATOM   1853 C  CG  . LEU A 1 296 ? 8.18500   16.48200  25.58000  1.000 56.65344  ?  573  LEU B CG  1 
ATOM   1854 C  CD1 . LEU A 1 296 ? 9.62100   16.11700  25.22400  1.000 53.08964  ?  573  LEU B CD1 1 
ATOM   1855 C  CD2 . LEU A 1 296 ? 7.33100   15.23700  25.67600  1.000 51.57571  ?  573  LEU B CD2 1 
ATOM   1856 N  N   . GLN A 1 297 ? 6.99900   20.00700  25.93700  1.000 56.20166  ?  574  GLN B N   1 
ATOM   1857 C  CA  . GLN A 1 297 ? 6.36000   20.74300  24.85800  1.000 64.47323  ?  574  GLN B CA  1 
ATOM   1858 C  C   . GLN A 1 297 ? 7.05300   22.06900  24.60400  1.000 65.82594  ?  574  GLN B C   1 
ATOM   1859 O  O   . GLN A 1 297 ? 7.32700   22.41900  23.44900  1.000 65.50187  ?  574  GLN B O   1 
ATOM   1860 C  CB  . GLN A 1 297 ? 4.88300   20.92400  25.16200  1.000 57.37644  ?  574  GLN B CB  1 
ATOM   1861 C  CG  . GLN A 1 297 ? 4.19400   19.61400  24.89800  1.000 59.56542  ?  574  GLN B CG  1 
ATOM   1862 C  CD  . GLN A 1 297 ? 2.80000   19.55400  25.41200  1.000 68.90130  ?  574  GLN B CD  1 
ATOM   1863 O  OE1 . GLN A 1 297 ? 2.17000   20.58800  25.66300  1.000 76.49335  ?  574  GLN B OE1 1 
ATOM   1864 N  NE2 . GLN A 1 297 ? 2.29600   18.33700  25.59500  1.000 62.97581  ?  574  GLN B NE2 1 
ATOM   1865 N  N   . ALA A 1 298 ? 7.38400   22.80400  25.66400  1.000 66.35831  ?  575  ALA B N   1 
ATOM   1866 C  CA  . ALA A 1 298 ? 8.09200   24.06600  25.48100  1.000 67.16280  ?  575  ALA B CA  1 
ATOM   1867 C  C   . ALA A 1 298 ? 9.40300   23.85400  24.72100  1.000 68.43314  ?  575  ALA B C   1 
ATOM   1868 O  O   . ALA A 1 298 ? 9.67700   24.54700  23.73800  1.000 73.67877  ?  575  ALA B O   1 
ATOM   1869 C  CB  . ALA A 1 298 ? 8.33100   24.72600  26.83900  1.000 59.14115  ?  575  ALA B CB  1 
ATOM   1870 N  N   . LEU A 1 299 ? 10.21900  22.87900  25.15100  1.000 67.43778  ?  576  LEU B N   1 
ATOM   1871 C  CA  . LEU A 1 299 ? 11.53100  22.68400  24.53800  1.000 63.59041  ?  576  LEU B CA  1 
ATOM   1872 C  C   . LEU A 1 299 ? 11.41500  22.27300  23.07500  1.000 75.61052  ?  576  LEU B C   1 
ATOM   1873 O  O   . LEU A 1 299 ? 12.29000  22.60900  22.26500  1.000 74.63637  ?  576  LEU B O   1 
ATOM   1874 C  CB  . LEU A 1 299 ? 12.32400  21.62900  25.30300  1.000 66.83957  ?  576  LEU B CB  1 
ATOM   1875 C  CG  . LEU A 1 299 ? 12.90000  21.95300  26.68700  1.000 73.10358  ?  576  LEU B CG  1 
ATOM   1876 C  CD1 . LEU A 1 299 ? 13.28100  20.68100  27.42000  1.000 61.02559  ?  576  LEU B CD1 1 
ATOM   1877 C  CD2 . LEU A 1 299 ? 14.11400  22.87300  26.56800  1.000 70.76581  ?  576  LEU B CD2 1 
ATOM   1878 N  N   . LEU A 1 300 ? 10.35800  21.52500  22.72500  1.000 71.97718  ?  577  LEU B N   1 
ATOM   1879 C  CA  . LEU A 1 300 ? 10.16200  21.10400  21.34100  1.000 67.09981  ?  577  LEU B CA  1 
ATOM   1880 C  C   . LEU A 1 300 ? 9.78100   22.28600  20.45700  1.000 77.17137  ?  577  LEU B C   1 
ATOM   1881 O  O   . LEU A 1 300 ? 10.25300  22.40000  19.31600  1.000 79.35724  ?  577  LEU B O   1 
ATOM   1882 C  CB  . LEU A 1 300 ? 9.09100   20.01700  21.27700  1.000 58.89424  ?  577  LEU B CB  1 
ATOM   1883 C  CG  . LEU A 1 300 ? 9.51100   18.61100  21.72900  1.000 59.34302  ?  577  LEU B CG  1 
ATOM   1884 C  CD1 . LEU A 1 300 ? 8.31200   17.68600  21.93400  1.000 52.38714  ?  577  LEU B CD1 1 
ATOM   1885 C  CD2 . LEU A 1 300 ? 10.47900  18.01100  20.73900  1.000 51.45073  ?  577  LEU B CD2 1 
ATOM   1886 N  N   . GLY A 1 301 ? 8.92100   23.16900  20.96900  1.000 72.64153  ?  578  GLY B N   1 
ATOM   1887 C  CA  . GLY A 1 301 ? 8.45300   24.31400  20.22200  1.000 73.96476  ?  578  GLY B CA  1 
ATOM   1888 C  C   . GLY A 1 301 ? 9.49500   25.39300  20.03100  1.000 88.80512  ?  578  GLY B C   1 
ATOM   1889 O  O   . GLY A 1 301 ? 9.29500   26.28500  19.19700  1.000 89.27410  ?  578  GLY B O   1 
ATOM   1890 N  N   . ASP A 1 302 ? 10.59800  25.33900  20.78700  1.000 88.88045  ?  579  ASP B N   1 
ATOM   1891 C  CA  . ASP A 1 302 ? 11.67100  26.32800  20.66500  1.000 92.05061  ?  579  ASP B CA  1 
ATOM   1892 C  C   . ASP A 1 302 ? 12.63000  25.80500  19.60900  1.000 89.65536  ?  579  ASP B C   1 
ATOM   1893 O  O   . ASP A 1 302 ? 13.64200  25.16200  19.90800  1.000 87.45682  ?  579  ASP B O   1 
ATOM   1894 C  CB  . ASP A 1 302 ? 12.36200  26.57100  22.00200  1.000 87.96529  ?  579  ASP B CB  1 
ATOM   1895 C  CG  . ASP A 1 302 ? 13.23500  27.82300  21.99000  1.000 95.10053  ?  579  ASP B CG  1 
ATOM   1896 N  N   . ASN A 1 303 ? 12.30600  26.09400  18.34800  1.000 94.33889  ?  580  ASN B N   1 
ATOM   1897 C  CA  . ASN A 1 303 ? 13.07200  25.53900  17.23800  1.000 97.83436  ?  580  ASN B CA  1 
ATOM   1898 C  C   . ASN A 1 303 ? 14.40400  26.25500  17.01900  1.000 99.07300  ?  580  ASN B C   1 
ATOM   1899 O  O   . ASN A 1 303 ? 15.34000  25.65100  16.48000  1.000 102.47250 ?  580  ASN B O   1 
ATOM   1900 C  CB  . ASN A 1 303 ? 12.25200  25.56600  15.94700  1.000 89.74040  ?  580  ASN B CB  1 
ATOM   1901 C  CG  . ASN A 1 303 ? 12.73600  24.53700  14.94700  1.000 90.45140  ?  580  ASN B CG  1 
ATOM   1902 O  OD1 . ASN A 1 303 ? 13.06200  23.40400  15.31600  1.000 86.32995  ?  580  ASN B OD1 1 
ATOM   1903 N  ND2 . ASN A 1 303 ? 12.80600  24.92500  13.67700  1.000 94.67784  ?  580  ASN B ND2 1 
ATOM   1904 N  N   . GLU A 1 304 ? 14.52700  27.52700  17.40100  1.000 88.45958  ?  581  GLU B N   1 
ATOM   1905 C  CA  . GLU A 1 304 ? 15.85700  28.12600  17.40300  1.000 87.76083  ?  581  GLU B CA  1 
ATOM   1906 C  C   . GLU A 1 304 ? 16.78700  27.33100  18.31900  1.000 94.65932  ?  581  GLU B C   1 
ATOM   1907 O  O   . GLU A 1 304 ? 17.80800  26.78300  17.88000  1.000 94.95688  ?  581  GLU B O   1 
ATOM   1908 C  CB  . GLU A 1 304 ? 15.77600  29.59500  17.81900  1.000 83.72194  ?  581  GLU B CB  1 
ATOM   1909 N  N   . LYS A 1 305 ? 16.40900  27.20300  19.59300  1.000 101.02471 ?  582  LYS B N   1 
ATOM   1910 C  CA  . LYS A 1 305 ? 17.15600  26.40700  20.56200  1.000 100.76864 ?  582  LYS B CA  1 
ATOM   1911 C  C   . LYS A 1 305 ? 17.28500  24.95200  20.11200  1.000 98.92226  ?  582  LYS B C   1 
ATOM   1912 O  O   . LYS A 1 305 ? 18.37900  24.51600  19.72600  1.000 95.93682  ?  582  LYS B O   1 
ATOM   1913 C  CB  . LYS A 1 305 ? 16.48000  26.49300  21.94000  1.000 95.50796  ?  582  LYS B CB  1 
ATOM   1914 C  CG  . LYS A 1 305 ? 17.17100  25.70000  23.03900  1.000 96.31014  ?  582  LYS B CG  1 
ATOM   1915 N  N   . MET A 1 306 ? 16.16700  24.20900  20.11800  1.000 105.72189 ?  583  MET B N   1 
ATOM   1916 C  CA  . MET A 1 306 ? 16.15600  22.74300  20.05200  1.000 102.95473 ?  583  MET B CA  1 
ATOM   1917 C  C   . MET A 1 306 ? 16.10300  22.18400  18.63400  1.000 99.71898  ?  583  MET B C   1 
ATOM   1918 O  O   . MET A 1 306 ? 16.67000  21.11200  18.38200  1.000 98.04248  ?  583  MET B O   1 
ATOM   1919 C  CB  . MET A 1 306 ? 14.97700  22.19100  20.85300  1.000 102.05250 ?  583  MET B CB  1 
ATOM   1920 C  CG  . MET A 1 306 ? 15.25000  22.14300  22.35000  1.000 105.83128 ?  583  MET B CG  1 
ATOM   1921 S  SD  . MET A 1 306 ? 16.61700  21.01900  22.71400  1.000 126.66360 ?  583  MET B SD  1 
ATOM   1922 C  CE  . MET A 1 306 ? 16.54300  20.92200  24.50200  1.000 104.48349 ?  583  MET B CE  1 
ATOM   1923 N  N   . ASN A 1 307 ? 15.38900  22.84800  17.71400  1.000 96.18345  ?  584  ASN B N   1 
ATOM   1924 C  CA  . ASN A 1 307 ? 15.47700  22.57800  16.27100  1.000 82.71788  ?  584  ASN B CA  1 
ATOM   1925 C  C   . ASN A 1 307 ? 14.83900  21.24000  15.87300  1.000 76.38315  ?  584  ASN B C   1 
ATOM   1926 O  O   . ASN A 1 307 ? 15.27900  20.59700  14.91700  1.000 77.91325  ?  584  ASN B O   1 
ATOM   1927 C  CB  . ASN A 1 307 ? 16.93300  22.64000  15.81500  1.000 78.60505  ?  584  ASN B CB  1 
ATOM   1928 C  CG  . ASN A 1 307 ? 17.07700  22.66800  14.32000  1.000 89.57970  ?  584  ASN B CG  1 
ATOM   1929 O  OD1 . ASN A 1 307 ? 17.93900  21.97500  13.76400  1.000 94.49622  ?  584  ASN B OD1 1 
ATOM   1930 N  ND2 . ASN A 1 307 ? 16.24500  23.47100  13.65000  1.000 84.90660  ?  584  ASN B ND2 1 
ATOM   1931 N  N   . LEU A 1 308 ? 13.79200  20.82000  16.57300  1.000 63.92858  ?  585  LEU B N   1 
ATOM   1932 C  CA  . LEU A 1 308 ? 13.16400  19.52600  16.35300  1.000 60.87702  ?  585  LEU B CA  1 
ATOM   1933 C  C   . LEU A 1 308 ? 11.75000  19.62400  15.80100  1.000 51.92942  ?  585  LEU B C   1 
ATOM   1934 O  O   . LEU A 1 308 ? 11.17500  18.59500  15.46200  1.000 57.66946  ?  585  LEU B O   1 
ATOM   1935 C  CB  . LEU A 1 308 ? 13.13400  18.71200  17.66700  1.000 57.30354  ?  585  LEU B CB  1 
ATOM   1936 C  CG  . LEU A 1 308 ? 14.50100  18.33400  18.23700  1.000 58.51065  ?  585  LEU B CG  1 
ATOM   1937 C  CD1 . LEU A 1 308 ? 14.38800  17.67600  19.58200  1.000 62.59263  ?  585  LEU B CD1 1 
ATOM   1938 C  CD2 . LEU A 1 308 ? 15.24100  17.41400  17.28900  1.000 57.86172  ?  585  LEU B CD2 1 
ATOM   1939 N  N   . SER A 1 309 ? 11.17300  20.81400  15.70700  1.000 59.98893  ?  586  SER B N   1 
ATOM   1940 C  CA  . SER A 1 309 ? 9.82900   20.98100  15.17400  1.000 62.16409  ?  586  SER B CA  1 
ATOM   1941 C  C   . SER A 1 309 ? 9.80600   21.47300  13.72700  1.000 66.65192  ?  586  SER B C   1 
ATOM   1942 O  O   . SER A 1 309 ? 8.72200   21.52800  13.13100  1.000 60.90068  ?  586  SER B O   1 
ATOM   1943 C  CB  . SER A 1 309 ? 9.03200   21.96000  16.04600  1.000 66.90339  ?  586  SER B CB  1 
ATOM   1944 O  OG  . SER A 1 309 ? 9.61600   23.25500  16.04300  1.000 70.02048  ?  586  SER B OG  1 
ATOM   1945 N  N   . ASP A 1 310 ? 10.96100  21.84600  13.15700  1.000 61.24637  ?  587  ASP B N   1 
ATOM   1946 C  CA  . ASP A 1 310 ? 11.02100  22.32600  11.77400  1.000 68.23087  ?  587  ASP B CA  1 
ATOM   1947 C  C   . ASP A 1 310 ? 12.39100  21.99300  11.18500  1.000 65.53512  ?  587  ASP B C   1 
ATOM   1948 O  O   . ASP A 1 310 ? 13.35300  22.74700  11.37400  1.000 66.22480  ?  587  ASP B O   1 
ATOM   1949 C  CB  . ASP A 1 310 ? 10.76000  23.81700  11.68100  1.000 69.41068  ?  587  ASP B CB  1 
ATOM   1950 C  CG  . ASP A 1 310 ? 11.25700  24.39600  10.36200  1.000 75.71494  ?  587  ASP B CG  1 
ATOM   1951 O  OD1 . ASP A 1 310 ? 11.35200  23.61300  9.37100   1.000 76.20619  ?  587  ASP B OD1 1 
ATOM   1952 O  OD2 . ASP A 1 310 ? 11.58500  25.61100  10.31500  1.000 79.60624  -1 587  ASP B OD2 1 
ATOM   1953 N  N   . VAL A 1 311 ? 12.45500  20.88900  10.44500  1.000 57.88776  ?  588  VAL B N   1 
ATOM   1954 C  CA  . VAL A 1 311 ? 13.66400  20.44000  9.77600   1.000 58.27283  ?  588  VAL B CA  1 
ATOM   1955 C  C   . VAL A 1 311 ? 13.33200  20.23200  8.30300   1.000 59.86183  ?  588  VAL B C   1 
ATOM   1956 O  O   . VAL A 1 311 ? 12.16600  20.18200  7.91400   1.000 53.78594  ?  588  VAL B O   1 
ATOM   1957 C  CB  . VAL A 1 311 ? 14.22000  19.14400  10.39500  1.000 58.94343  ?  588  VAL B CB  1 
ATOM   1958 C  CG1 . VAL A 1 311 ? 14.78000  19.42600  11.78600  1.000 65.50154  ?  588  VAL B CG1 1 
ATOM   1959 C  CG2 . VAL A 1 311 ? 13.11800  18.07800  10.45600  1.000 42.85642  ?  588  VAL B CG2 1 
ATOM   1960 N  N   . GLU A 1 312 ? 14.38900  20.20300  7.48500   1.000 66.86420  ?  589  GLU B N   1 
ATOM   1961 C  CA  . GLU A 1 312 ? 14.21100  20.09200  6.01500   1.000 68.21999  ?  589  GLU B CA  1 
ATOM   1962 C  C   . GLU A 1 312 ? 13.89100  18.64700  5.63700   1.000 68.94660  ?  589  GLU B C   1 
ATOM   1963 O  O   . GLU A 1 312 ? 14.84300  17.89100  5.37800   1.000 83.70884  ?  589  GLU B O   1 
ATOM   1964 C  CB  . GLU A 1 312 ? 15.48800  20.54800  5.30700   1.000 74.49694  ?  589  GLU B CB  1 
ATOM   1965 C  CG  . GLU A 1 312 ? 16.01800  21.87500  5.81700   1.000 82.82882  ?  589  GLU B CG  1 
ATOM   1966 C  CD  . GLU A 1 312 ? 17.25600  22.37900  5.09500   1.000 95.05513  ?  589  GLU B CD  1 
ATOM   1967 O  OE1 . GLU A 1 312 ? 18.27800  21.66600  5.10900   1.000 106.82227 ?  589  GLU B OE1 1 
ATOM   1968 O  OE2 . GLU A 1 312 ? 17.19500  23.48400  4.52300   1.000 95.57074  -1 589  GLU B OE2 1 
ATOM   1969 N  N   . LEU A 1 313 ? 12.62300  18.24000  5.66000   1.000 67.25516  ?  590  LEU B N   1 
ATOM   1970 C  CA  . LEU A 1 313 ? 12.18700  16.92200  5.18700   1.000 56.53625  ?  590  LEU B CA  1 
ATOM   1971 C  C   . LEU A 1 313 ? 13.25700  15.83200  5.22900   1.000 58.79890  ?  590  LEU B C   1 
ATOM   1972 O  O   . LEU A 1 313 ? 13.72300  15.38300  4.18000   1.000 64.56491  ?  590  LEU B O   1 
ATOM   1973 C  CB  . LEU A 1 313 ? 11.65800  17.03500  3.75600   1.000 49.80271  ?  590  LEU B CB  1 
ATOM   1974 C  CG  . LEU A 1 313 ? 10.93300  18.36700  3.52700   1.000 69.14687  ?  590  LEU B CG  1 
ATOM   1975 C  CD1 . LEU A 1 313 ? 10.41200  18.55400  2.10500   1.000 69.35330  ?  590  LEU B CD1 1 
ATOM   1976 C  CD2 . LEU A 1 313 ? 9.80900   18.54000  4.54000   1.000 70.27031  ?  590  LEU B CD2 1 
ATOM   1977 N  N   . ILE A 1 314 ? 13.63900  15.37400  6.41600   1.000 62.10788  ?  591  ILE B N   1 
ATOM   1978 C  CA  . ILE A 1 314 ? 14.69500  14.32300  6.52900   1.000 52.26419  ?  591  ILE B CA  1 
ATOM   1979 C  C   . ILE A 1 314 ? 14.02000  12.95800  6.70500   1.000 46.75735  ?  591  ILE B C   1 
ATOM   1980 O  O   . ILE A 1 314 ? 12.91200  12.91300  7.25900   1.000 52.20533  ?  591  ILE B O   1 
ATOM   1981 C  CB  . ILE A 1 314 ? 15.66300  14.63300  7.68800   1.000 61.96869  ?  591  ILE B CB  1 
ATOM   1982 C  CG1 . ILE A 1 314 ? 14.96500  14.55500  9.04800   1.000 53.20255  ?  591  ILE B CG1 1 
ATOM   1983 C  CG2 . ILE A 1 314 ? 16.34400  15.97600  7.47800   1.000 72.16243  ?  591  ILE B CG2 1 
ATOM   1984 C  CD1 . ILE A 1 314 ? 15.88400  14.79800  10.22100  1.000 62.27890  ?  591  ILE B CD1 1 
ATOM   1985 N  N   . PRO A 1 315 ? 14.64500  11.84600  6.26200   1.000 49.13345  ?  592  PRO B N   1 
ATOM   1986 C  CA  . PRO A 1 315 ? 14.07800  10.50700  6.44600   1.000 54.52312  ?  592  PRO B CA  1 
ATOM   1987 C  C   . PRO A 1 315 ? 13.90800  10.17700  7.93700   1.000 50.81808  ?  592  PRO B C   1 
ATOM   1988 O  O   . PRO A 1 315 ? 14.76600  10.55000  8.71000   1.000 47.38020  ?  592  PRO B O   1 
ATOM   1989 C  CB  . PRO A 1 315 ? 15.13100  9.57500   5.83200   1.000 52.83314  ?  592  PRO B CB  1 
ATOM   1990 C  CG  . PRO A 1 315 ? 15.92500  10.46200  4.90000   1.000 48.91885  ?  592  PRO B CG  1 
ATOM   1991 C  CD  . PRO A 1 315 ? 15.93300  11.81900  5.56900   1.000 51.69023  ?  592  PRO B CD  1 
ATOM   1992 N  N   . LEU A 1 316 ? 12.81400  9.49800   8.30000   1.000 48.44678  ?  593  LEU B N   1 
ATOM   1993 C  CA  . LEU A 1 316 ? 12.61800  9.09100   9.71700   1.000 46.52844  ?  593  LEU B CA  1 
ATOM   1994 C  C   . LEU A 1 316 ? 13.38800  7.78700   9.92200   1.000 50.28308  ?  593  LEU B C   1 
ATOM   1995 O  O   . LEU A 1 316 ? 13.10400  6.82100   9.20000   1.000 45.09266  ?  593  LEU B O   1 
ATOM   1996 C  CB  . LEU A 1 316 ? 11.12400  8.88700   9.97700   1.000 40.34114  ?  593  LEU B CB  1 
ATOM   1997 C  CG  . LEU A 1 316 ? 10.77400  8.16000   11.27400  1.000 47.89177  ?  593  LEU B CG  1 
ATOM   1998 C  CD1 . LEU A 1 316 ? 10.86700  9.09800   12.46700  1.000 42.90267  ?  593  LEU B CD1 1 
ATOM   1999 C  CD2 . LEU A 1 316 ? 9.38800   7.54000   11.18800  1.000 47.02489  ?  593  LEU B CD2 1 
ATOM   2000 N  N   . PRO A 1 317 ? 14.36400  7.71400   10.84900  1.000 51.23138  ?  594  PRO B N   1 
ATOM   2001 C  CA  . PRO A 1 317 ? 15.20700  6.50300   10.98100  1.000 43.76686  ?  594  PRO B CA  1 
ATOM   2002 C  C   . PRO A 1 317 ? 14.38400  5.25100   11.18100  1.000 49.33385  ?  594  PRO B C   1 
ATOM   2003 O  O   . PRO A 1 317 ? 14.65000  4.21800   10.55700  1.000 45.41509  ?  594  PRO B O   1 
ATOM   2004 C  CB  . PRO A 1 317 ? 16.09300  6.80800   12.19800  1.000 43.91084  ?  594  PRO B CB  1 
ATOM   2005 C  CG  . PRO A 1 317 ? 16.12700  8.30100   12.27800  1.000 51.04741  ?  594  PRO B CG  1 
ATOM   2006 C  CD  . PRO A 1 317 ? 14.79300  8.80200   11.74600  1.000 46.58898  ?  594  PRO B CD  1 
ATOM   2007 N  N   . LEU A 1 318 ? 13.37000  5.33300   12.04700  1.000 47.19113  ?  595  LEU B N   1 
ATOM   2008 C  CA  . LEU A 1 318 ? 12.47500  4.21300   12.29200  1.000 47.32542  ?  595  LEU B CA  1 
ATOM   2009 C  C   . LEU A 1 318 ? 11.92600  3.62300   10.98900  1.000 49.57557  ?  595  LEU B C   1 
ATOM   2010 O  O   . LEU A 1 318 ? 11.69700  2.40700   10.89100  1.000 47.05514  ?  595  LEU B O   1 
ATOM   2011 C  CB  . LEU A 1 318 ? 11.33800  4.68700   13.19800  1.000 40.91242  ?  595  LEU B CB  1 
ATOM   2012 C  CG  . LEU A 1 318 ? 10.37300  3.58800   13.58400  1.000 48.19750  ?  595  LEU B CG  1 
ATOM   2013 C  CD1 . LEU A 1 318 ? 11.13000  2.54500   14.42800  1.000 43.29352  ?  595  LEU B CD1 1 
ATOM   2014 C  CD2 . LEU A 1 318 ? 9.21500   4.20100   14.35900  1.000 46.63952  ?  595  LEU B CD2 1 
ATOM   2015 N  N   . GLU A 1 319 ? 11.69600  4.47500   9.97600   1.000 43.41529  ?  596  GLU B N   1 
ATOM   2016 C  CA  . GLU A 1 319 ? 11.07400  4.05100   8.72500   1.000 48.81413  ?  596  GLU B CA  1 
ATOM   2017 C  C   . GLU A 1 319 ? 11.44000  5.02600   7.60500   1.000 47.14219  ?  596  GLU B C   1 
ATOM   2018 O  O   . GLU A 1 319 ? 10.70800  5.97900   7.33700   1.000 46.09901  ?  596  GLU B O   1 
ATOM   2019 C  CB  . GLU A 1 319 ? 9.55200   3.95100   8.88600   1.000 48.76101  ?  596  GLU B CB  1 
ATOM   2020 C  CG  . GLU A 1 319 ? 8.85000   3.57400   7.58800   1.000 55.39288  ?  596  GLU B CG  1 
ATOM   2021 C  CD  . GLU A 1 319 ? 7.48500   2.94100   7.79500   1.000 71.60087  ?  596  GLU B CD  1 
ATOM   2022 O  OE1 . GLU A 1 319 ? 7.07900   2.69800   8.96100   1.000 73.64327  ?  596  GLU B OE1 1 
ATOM   2023 O  OE2 . GLU A 1 319 ? 6.79900   2.69200   6.77900   1.000 82.58590  -1 596  GLU B OE2 1 
ATOM   2024 N  N   . PRO A 1 320 ? 12.56700  4.81500   6.92900   1.000 50.02398  ?  597  PRO B N   1 
ATOM   2025 C  CA  . PRO A 1 320 ? 13.13900  5.88700   6.09600   1.000 48.33318  ?  597  PRO B CA  1 
ATOM   2026 C  C   . PRO A 1 320 ? 12.29500  6.29000   4.88700   1.000 50.81076  ?  597  PRO B C   1 
ATOM   2027 O  O   . PRO A 1 320 ? 12.54300  7.36800   4.33000   1.000 47.10426  ?  597  PRO B O   1 
ATOM   2028 C  CB  . PRO A 1 320 ? 14.49400  5.30500   5.67100   1.000 47.23254  ?  597  PRO B CB  1 
ATOM   2029 C  CG  . PRO A 1 320 ? 14.35400  3.83100   5.84000   1.000 46.98242  ?  597  PRO B CG  1 
ATOM   2030 C  CD  . PRO A 1 320 ? 13.47400  3.66000   7.03800   1.000 44.89356  ?  597  PRO B CD  1 
ATOM   2031 N  N   . GLN A 1 321 ? 11.31800  5.48200   4.45900   1.000 47.04245  ?  598  GLN B N   1 
ATOM   2032 C  CA  . GLN A 1 321 ? 10.40500  5.93400   3.41700   1.000 46.33850  ?  598  GLN B CA  1 
ATOM   2033 C  C   . GLN A 1 321 ? 9.61300   7.16900   3.85700   1.000 49.30817  ?  598  GLN B C   1 
ATOM   2034 O  O   . GLN A 1 321 ? 9.21500   7.98500   3.01600   1.000 58.88274  ?  598  GLN B O   1 
ATOM   2035 C  CB  . GLN A 1 321 ? 9.44900   4.80600   3.01100   1.000 50.48295  ?  598  GLN B CB  1 
ATOM   2036 C  CG  . GLN A 1 321 ? 10.16800  3.55100   2.48400   1.000 61.01994  ?  598  GLN B CG  1 
ATOM   2037 C  CD  . GLN A 1 321 ? 10.69200  2.61000   3.61000   1.000 76.94865  ?  598  GLN B CD  1 
ATOM   2038 O  OE1 . GLN A 1 321 ? 10.71200  2.96200   4.81100   1.000 61.00180  ?  598  GLN B OE1 1 
ATOM   2039 N  NE2 . GLN A 1 321 ? 11.10900  1.39900   3.20900   1.000 75.74860  ?  598  GLN B NE2 1 
ATOM   2040 N  N   . VAL A 1 322 ? 9.41500   7.31200   5.16900   1.000 42.49485  ?  599  VAL B N   1 
ATOM   2041 C  CA  . VAL A 1 322 ? 8.64600   8.47400   5.70400   1.000 41.78979  ?  599  VAL B CA  1 
ATOM   2042 C  C   . VAL A 1 322 ? 9.58900   9.67100   5.85000   1.000 47.28464  ?  599  VAL B C   1 
ATOM   2043 O  O   . VAL A 1 322 ? 10.57300  9.55400   6.60500   1.000 51.62612  ?  599  VAL B O   1 
ATOM   2044 C  CB  . VAL A 1 322 ? 7.96300   8.13200   7.04200   1.000 49.69222  ?  599  VAL B CB  1 
ATOM   2045 C  CG1 . VAL A 1 322 ? 7.28200   9.34500   7.65800   1.000 46.75180  ?  599  VAL B CG1 1 
ATOM   2046 C  CG2 . VAL A 1 322 ? 6.98100   6.98000   6.89600   1.000 46.89534  ?  599  VAL B CG2 1 
ATOM   2047 N  N   . LYS A 1 323 ? 9.30300   10.76900  5.14600   1.000 48.54799  ?  600  LYS B N   1 
ATOM   2048 C  CA  . LYS A 1 323 ? 10.11700  12.00500  5.29300   1.000 51.52984  ?  600  LYS B CA  1 
ATOM   2049 C  C   . LYS A 1 323 ? 9.43900   12.88000  6.34900   1.000 50.66047  ?  600  LYS B C   1 
ATOM   2050 O  O   . LYS A 1 323 ? 8.20500   13.02200  6.28100   1.000 48.94262  ?  600  LYS B O   1 
ATOM   2051 C  CB  . LYS A 1 323 ? 10.26300  12.71300  3.94400   1.000 47.39229  ?  600  LYS B CB  1 
ATOM   2052 C  CG  . LYS A 1 323 ? 10.73200  11.82100  2.80300   1.000 43.16604  ?  600  LYS B CG  1 
ATOM   2053 C  CD  . LYS A 1 323 ? 11.96600  11.01500  3.14400   1.000 54.82614  ?  600  LYS B CD  1 
ATOM   2054 C  CE  . LYS A 1 323 ? 12.30600  9.98600   2.08600   1.000 51.30798  ?  600  LYS B CE  1 
ATOM   2055 N  NZ  . LYS A 1 323 ? 13.48500  9.17500   2.47000   1.000 65.38193  ?  600  LYS B NZ  1 
ATOM   2056 N  N   . ILE A 1 324 ? 10.21400  13.44400  7.27900   1.000 48.60892  ?  601  ILE B N   1 
ATOM   2057 C  CA  . ILE A 1 324 ? 9.59800   14.19600  8.41200   1.000 55.04180  ?  601  ILE B CA  1 
ATOM   2058 C  C   . ILE A 1 324 ? 9.91300   15.69100  8.31700   1.000 51.66742  ?  601  ILE B C   1 
ATOM   2059 O  O   . ILE A 1 324 ? 11.04800  16.03500  7.94300   1.000 54.53367  ?  601  ILE B O   1 
ATOM   2060 C  CB  . ILE A 1 324 ? 10.08100  13.61800  9.75700   1.000 47.29166  ?  601  ILE B CB  1 
ATOM   2061 C  CG1 . ILE A 1 324 ? 11.59500  13.77100  9.92000   1.000 48.99222  ?  601  ILE B CG1 1 
ATOM   2062 C  CG2 . ILE A 1 324 ? 9.63800   12.17200  9.90900   1.000 43.24616  ?  601  ILE B CG2 1 
ATOM   2063 C  CD1 . ILE A 1 324 ? 12.09500  13.59500  11.33000  1.000 56.39267  ?  601  ILE B CD1 1 
ATOM   2064 N  N   . ARG A 1 325 ? 8.93800   16.54000  8.64700   1.000 47.90164  ?  602  ARG B N   1 
ATOM   2065 C  CA  . ARG A 1 325 ? 9.18600   18.00400  8.69500   1.000 55.64836  ?  602  ARG B CA  1 
ATOM   2066 C  C   . ARG A 1 325 ? 9.58600   18.36800  10.12500  1.000 62.01316  ?  602  ARG B C   1 
ATOM   2067 O  O   . ARG A 1 325 ? 10.17400  19.44800  10.31900  1.000 57.29108  ?  602  ARG B O   1 
ATOM   2068 C  CB  . ARG A 1 325 ? 7.92000   18.77100  8.30900   1.000 56.80460  ?  602  ARG B CB  1 
ATOM   2069 C  CG  . ARG A 1 325 ? 7.32900   18.38100  6.96200   1.000 65.51620  ?  602  ARG B CG  1 
ATOM   2070 C  CD  . ARG A 1 325 ? 5.99000   19.05500  6.73000   1.000 63.06884  ?  602  ARG B CD  1 
ATOM   2071 N  NE  . ARG A 1 325 ? 5.59800   19.07700  5.32800   1.000 73.64771  ?  602  ARG B NE  1 
ATOM   2072 C  CZ  . ARG A 1 325 ? 6.24800   19.73400  4.37400   1.000 72.99117  ?  602  ARG B CZ  1 
ATOM   2073 N  NH1 . ARG A 1 325 ? 7.00600   20.77100  4.68000   1.000 73.71221  ?  602  ARG B NH1 1 
ATOM   2074 N  NH2 . ARG A 1 325 ? 6.12400   19.36100  3.11200   1.000 74.48702  ?  602  ARG B NH2 1 
ATOM   2075 N  N   . GLY A 1 326 ? 9.26500   17.49500  11.08400  1.000 52.75330  ?  603  GLY B N   1 
ATOM   2076 C  CA  . GLY A 1 326 ? 9.59300   17.75600  12.49800  1.000 56.82799  ?  603  GLY B CA  1 
ATOM   2077 C  C   . GLY A 1 326 ? 8.59500   17.11400  13.44200  1.000 55.23305  ?  603  GLY B C   1 
ATOM   2078 O  O   . GLY A 1 326 ? 7.70200   16.39900  12.95600  1.000 55.14350  ?  603  GLY B O   1 
ATOM   2079 N  N   . ILE A 1 327 ? 8.74100   17.35800  14.74500  1.000 54.10690  ?  604  ILE B N   1 
ATOM   2080 C  CA  . ILE A 1 327 ? 7.84700   16.79400  15.74800  1.000 50.19688  ?  604  ILE B CA  1 
ATOM   2081 C  C   . ILE A 1 327 ? 6.80500   17.84700  16.10100  1.000 53.29586  ?  604  ILE B C   1 
ATOM   2082 O  O   . ILE A 1 327 ? 7.11500   19.04100  16.18500  1.000 55.32713  ?  604  ILE B O   1 
ATOM   2083 C  CB  . ILE A 1 327 ? 8.63500   16.34400  16.99500  1.000 51.56700  ?  604  ILE B CB  1 
ATOM   2084 C  CG1 . ILE A 1 327 ? 9.57500   15.18700  16.64400  1.000 49.04388  ?  604  ILE B CG1 1 
ATOM   2085 C  CG2 . ILE A 1 327 ? 7.68500   15.97100  18.12700  1.000 47.95246  ?  604  ILE B CG2 1 
ATOM   2086 C  CD1 . ILE A 1 327 ? 10.60100  14.89100  17.69900  1.000 48.38193  ?  604  ILE B CD1 1 
ATOM   2087 N  N   . ILE A 1 328 ? 5.56500   17.42300  16.29100  1.000 51.55907  ?  605  ILE B N   1 
ATOM   2088 C  CA  . ILE A 1 328 ? 4.53600   18.38600  16.67900  1.000 58.40536  ?  605  ILE B CA  1 
ATOM   2089 C  C   . ILE A 1 328 ? 4.69400   18.73700  18.15700  1.000 59.09462  ?  605  ILE B C   1 
ATOM   2090 O  O   . ILE A 1 328 ? 4.50800   17.86800  19.02200  1.000 55.81337  ?  605  ILE B O   1 
ATOM   2091 C  CB  . ILE A 1 328 ? 3.14100   17.83800  16.36600  1.000 62.28680  ?  605  ILE B CB  1 
ATOM   2092 C  CG1 . ILE A 1 328 ? 3.08500   17.50700  14.86600  1.000 59.12460  ?  605  ILE B CG1 1 
ATOM   2093 C  CG2 . ILE A 1 328 ? 2.08000   18.83400  16.80100  1.000 54.42603  ?  605  ILE B CG2 1 
ATOM   2094 C  CD1 . ILE A 1 328 ? 1.83200   16.79800  14.44500  1.000 57.21026  ?  605  ILE B CD1 1 
ATOM   2095 N  N   . PRO A 1 329 ? 5.06300   19.98100  18.49500  1.000 60.28059  ?  606  PRO B N   1 
ATOM   2096 C  CA  . PRO A 1 329 ? 5.38500   20.28500  19.89900  1.000 56.88967  ?  606  PRO B CA  1 
ATOM   2097 C  C   . PRO A 1 329 ? 4.23800   20.06100  20.86200  1.000 64.21829  ?  606  PRO B C   1 
ATOM   2098 O  O   . PRO A 1 329 ? 4.47200   19.54900  21.96800  1.000 62.67614  ?  606  PRO B O   1 
ATOM   2099 C  CB  . PRO A 1 329 ? 5.78900   21.76800  19.85300  1.000 58.23468  ?  606  PRO B CB  1 
ATOM   2100 C  CG  . PRO A 1 329 ? 6.26800   21.98300  18.46400  1.000 57.67290  ?  606  PRO B CG  1 
ATOM   2101 C  CD  . PRO A 1 329 ? 5.39700   21.10600  17.60400  1.000 55.31035  ?  606  PRO B CD  1 
ATOM   2102 N  N   . GLU A 1 330 ? 3.00700   20.41600  20.48700  1.000 60.57606  ?  607  GLU B N   1 
ATOM   2103 C  CA  . GLU A 1 330 ? 1.94500   20.55300  21.48200  1.000 61.70510  ?  607  GLU B CA  1 
ATOM   2104 C  C   . GLU A 1 330 ? 1.22200   19.24700  21.79600  1.000 65.76565  ?  607  GLU B C   1 
ATOM   2105 O  O   . GLU A 1 330 ? 0.38400   19.23200  22.70600  1.000 60.05069  ?  607  GLU B O   1 
ATOM   2106 C  CB  . GLU A 1 330 ? 0.91900   21.60300  21.04200  1.000 64.09980  ?  607  GLU B CB  1 
ATOM   2107 C  CG  . GLU A 1 330 ? 0.12900   21.24300  19.78700  1.000 73.87395  ?  607  GLU B CG  1 
ATOM   2108 C  CD  . GLU A 1 330 ? 0.75100   21.79900  18.49700  1.000 84.50649  ?  607  GLU B CD  1 
ATOM   2109 O  OE1 . GLU A 1 330 ? 1.86800   22.37800  18.55300  1.000 77.37864  ?  607  GLU B OE1 1 
ATOM   2110 O  OE2 . GLU A 1 330 ? 0.11600   21.64900  17.42300  1.000 94.43061  -1 607  GLU B OE2 1 
ATOM   2111 N  N   . THR A 1 331 ? 1.52500   18.15500  21.08900  1.000 59.35972  ?  608  THR B N   1 
ATOM   2112 C  CA  . THR A 1 331 ? 0.90100   16.87300  21.36300  1.000 52.63374  ?  608  THR B CA  1 
ATOM   2113 C  C   . THR A 1 331 ? 1.89900   15.84300  21.86800  1.000 58.79472  ?  608  THR B C   1 
ATOM   2114 O  O   . THR A 1 331 ? 1.55900   14.66600  21.94700  1.000 54.11638  ?  608  THR B O   1 
ATOM   2115 C  CB  . THR A 1 331 ? 0.19200   16.33300  20.12000  1.000 54.75795  ?  608  THR B CB  1 
ATOM   2116 O  OG1 . THR A 1 331 ? 1.14300   16.17100  19.06000  1.000 56.63128  ?  608  THR B OG1 1 
ATOM   2117 C  CG2 . THR A 1 331 ? -0.94600  17.26100  19.68300  1.000 54.28076  ?  608  THR B CG2 1 
ATOM   2118 N  N   . ALA A 1 332 ? 3.12500   16.25600  22.18100  1.000 56.95141  ?  609  ALA B N   1 
ATOM   2119 C  CA  . ALA A 1 332 ? 4.11700   15.37100  22.77400  1.000 54.11422  ?  609  ALA B CA  1 
ATOM   2120 C  C   . ALA A 1 332 ? 3.83800   15.20200  24.27300  1.000 54.05616  ?  609  ALA B C   1 
ATOM   2121 O  O   . ALA A 1 332 ? 3.53800   16.17600  24.96400  1.000 51.73654  ?  609  ALA B O   1 
ATOM   2122 C  CB  . ALA A 1 332 ? 5.50900   15.94900  22.53900  1.000 47.83314  ?  609  ALA B CB  1 
ATOM   2123 N  N   . THR A 1 333 ? 3.89800   13.96400  24.77300  1.000 47.71184  ?  610  THR B N   1 
ATOM   2124 C  CA  . THR A 1 333 ? 3.74200   13.73600  26.20800  1.000 54.92736  ?  610  THR B CA  1 
ATOM   2125 C  C   . THR A 1 333 ? 4.58600   12.54300  26.62800  1.000 50.72650  ?  610  THR B C   1 
ATOM   2126 O  O   . THR A 1 333 ? 5.09300   11.79100  25.79400  1.000 50.57701  ?  610  THR B O   1 
ATOM   2127 C  CB  . THR A 1 333 ? 2.27900   13.50300  26.63700  1.000 52.24503  ?  610  THR B CB  1 
ATOM   2128 O  OG1 . THR A 1 333 ? 1.76400   12.33000  26.00800  1.000 59.05239  ?  610  THR B OG1 1 
ATOM   2129 C  CG2 . THR A 1 333 ? 1.38400   14.69000  26.30800  1.000 53.32584  ?  610  THR B CG2 1 
ATOM   2130 N  N   . LEU A 1 334 ? 4.72200   12.37200  27.94300  1.000 48.40438  ?  611  LEU B N   1 
ATOM   2131 C  CA  . LEU A 1 334 ? 5.51000   11.29200  28.52000  1.000 52.46306  ?  611  LEU B CA  1 
ATOM   2132 C  C   . LEU A 1 334 ? 4.59400   10.18900  29.04000  1.000 52.53641  ?  611  LEU B C   1 
ATOM   2133 O  O   . LEU A 1 334 ? 3.50100   10.46300  29.53300  1.000 49.76680  ?  611  LEU B O   1 
ATOM   2134 C  CB  . LEU A 1 334 ? 6.39400   11.81300  29.65300  1.000 49.09746  ?  611  LEU B CB  1 
ATOM   2135 C  CG  . LEU A 1 334 ? 7.37000   12.90700  29.22700  1.000 48.57752  ?  611  LEU B CG  1 
ATOM   2136 C  CD1 . LEU A 1 334 ? 8.11900   13.44000  30.43300  1.000 45.76203  ?  611  LEU B CD1 1 
ATOM   2137 C  CD2 . LEU A 1 334 ? 8.34700   12.37200  28.18600  1.000 48.21690  ?  611  LEU B CD2 1 
ATOM   2138 N  N   . PHE A 1 335 ? 5.03500   8.93500   28.90400  1.000 50.07831  ?  612  PHE B N   1 
ATOM   2139 C  CA  . PHE A 1 335 ? 4.28000   7.82000   29.46600  1.000 52.14636  ?  612  PHE B CA  1 
ATOM   2140 C  C   . PHE A 1 335 ? 4.48300   7.73900   30.96500  1.000 51.66870  ?  612  PHE B C   1 
ATOM   2141 O  O   . PHE A 1 335 ? 5.57000   8.02700   31.47200  1.000 54.20922  ?  612  PHE B O   1 
ATOM   2142 C  CB  . PHE A 1 335 ? 4.70100   6.50000   28.83600  1.000 47.17358  ?  612  PHE B CB  1 
ATOM   2143 C  CG  . PHE A 1 335 ? 4.20900   6.32800   27.45600  1.000 52.71504  ?  612  PHE B CG  1 
ATOM   2144 C  CD1 . PHE A 1 335 ? 4.94000   6.82100   26.37700  1.000 51.87783  ?  612  PHE B CD1 1 
ATOM   2145 C  CD2 . PHE A 1 335 ? 3.01200   5.69900   27.21500  1.000 49.20130  ?  612  PHE B CD2 1 
ATOM   2146 C  CE1 . PHE A 1 335 ? 4.47400   6.67400   25.08800  1.000 47.14694  ?  612  PHE B CE1 1 
ATOM   2147 C  CE2 . PHE A 1 335 ? 2.54500   5.54400   25.93200  1.000 50.75378  ?  612  PHE B CE2 1 
ATOM   2148 C  CZ  . PHE A 1 335 ? 3.27000   6.03200   24.86800  1.000 50.78119  ?  612  PHE B CZ  1 
ATOM   2149 N  N   . LYS A 1 336 ? 3.42900   7.34300   31.67200  1.000 51.50108  ?  613  LYS B N   1 
ATOM   2150 C  CA  . LYS A 1 336 ? 3.54500   7.06300   33.10200  1.000 56.01359  ?  613  LYS B CA  1 
ATOM   2151 C  C   . LYS A 1 336 ? 4.27700   5.74500   33.32100  1.000 58.24161  ?  613  LYS B C   1 
ATOM   2152 O  O   . LYS A 1 336 ? 3.64600   4.69200   33.43800  1.000 66.96874  ?  613  LYS B O   1 
ATOM   2153 C  CB  . LYS A 1 336 ? 2.16700   7.00700   33.77100  1.000 53.55294  ?  613  LYS B CB  1 
ATOM   2154 C  CG  . LYS A 1 336 ? 2.22700   6.82400   35.27600  1.000 63.61192  ?  613  LYS B CG  1 
ATOM   2155 C  CD  . LYS A 1 336 ? 0.84900   6.58300   35.85400  1.000 61.62868  ?  613  LYS B CD  1 
ATOM   2156 C  CE  . LYS A 1 336 ? 0.91900   6.35200   37.35900  1.000 82.06413  ?  613  LYS B CE  1 
ATOM   2157 N  NZ  . LYS A 1 336 ? -0.35600  6.73800   38.06500  1.000 82.06819  ?  613  LYS B NZ  1 
ATOM   2158 N  N   . SER A 1 337 ? 5.60000   5.78100   33.36300  1.000 55.96407  ?  614  SER B N   1 
ATOM   2159 C  CA  . SER A 1 337 ? 6.36400   4.58100   33.68400  1.000 58.86831  ?  614  SER B CA  1 
ATOM   2160 C  C   . SER A 1 337 ? 7.74200   5.00100   34.18200  1.000 58.01799  ?  614  SER B C   1 
ATOM   2161 O  O   . SER A 1 337 ? 8.05000   6.19000   34.29000  1.000 58.83482  ?  614  SER B O   1 
ATOM   2162 C  CB  . SER A 1 337 ? 6.44000   3.65000   32.47900  1.000 54.84941  ?  614  SER B CB  1 
ATOM   2163 O  OG  . SER A 1 337 ? 7.22400   4.21500   31.46700  1.000 62.65385  ?  614  SER B OG  1 
ATOM   2164 N  N   . ALA A 1 338 ? 8.56800   4.01400   34.50600  1.000 52.67054  ?  615  ALA B N   1 
ATOM   2165 C  CA  . ALA A 1 338 ? 9.83200   4.33000   35.16400  1.000 59.31252  ?  615  ALA B CA  1 
ATOM   2166 C  C   . ALA A 1 338 ? 10.71400  5.19500   34.26900  1.000 59.47950  ?  615  ALA B C   1 
ATOM   2167 O  O   . ALA A 1 338 ? 11.22100  6.23400   34.69900  1.000 62.71164  ?  615  ALA B O   1 
ATOM   2168 C  CB  . ALA A 1 338 ? 10.55200  3.04400   35.57900  1.000 51.68458  ?  615  ALA B CB  1 
ATOM   2169 N  N   . LEU A 1 339 ? 10.88900  4.80000   33.01100  1.000 56.56253  ?  616  LEU B N   1 
ATOM   2170 C  CA  . LEU A 1 339 ? 11.77500  5.55600   32.13300  1.000 58.23728  ?  616  LEU B CA  1 
ATOM   2171 C  C   . LEU A 1 339 ? 11.12800  6.79600   31.52400  1.000 50.09499  ?  616  LEU B C   1 
ATOM   2172 O  O   . LEU A 1 339 ? 11.84300  7.62700   30.96700  1.000 51.47705  ?  616  LEU B O   1 
ATOM   2173 C  CB  . LEU A 1 339 ? 12.29900  4.64400   31.02100  1.000 58.78064  ?  616  LEU B CB  1 
ATOM   2174 C  CG  . LEU A 1 339 ? 13.08000  3.47000   31.60100  1.000 62.64304  ?  616  LEU B CG  1 
ATOM   2175 C  CD1 . LEU A 1 339 ? 13.82100  2.73900   30.51000  1.000 64.78424  ?  616  LEU B CD1 1 
ATOM   2176 C  CD2 . LEU A 1 339 ? 14.04600  3.97400   32.68800  1.000 57.47195  ?  616  LEU B CD2 1 
ATOM   2177 N  N   . MET A 1 340 ? 9.81400   6.95300   31.62600  1.000 48.45849  ?  617  MET B N   1 
ATOM   2178 C  CA  . MET A 1 340 ? 9.09900   8.07800   31.03600  1.000 53.41468  ?  617  MET B CA  1 
ATOM   2179 C  C   . MET A 1 340 ? 9.50200   8.25100   29.56100  1.000 51.76613  ?  617  MET B C   1 
ATOM   2180 O  O   . MET A 1 340 ? 9.99500   9.29400   29.16600  1.000 51.56757  ?  617  MET B O   1 
ATOM   2181 C  CB  . MET A 1 340 ? 9.33200   9.36900   31.81400  1.000 47.04659  ?  617  MET B CB  1 
ATOM   2182 C  CG  . MET A 1 340 ? 8.74800   9.31700   33.23100  1.000 53.45921  ?  617  MET B CG  1 
ATOM   2183 S  SD  . MET A 1 340 ? 8.64400   10.90700  34.10200  1.000 50.50358  ?  617  MET B SD  1 
ATOM   2184 C  CE  . MET A 1 340 ? 7.12300   11.61100  33.44300  1.000 46.39651  ?  617  MET B CE  1 
ATOM   2185 N  N   . PRO A 1 341 ? 9.30800   7.21100   28.74200  1.000 48.96148  ?  618  PRO B N   1 
ATOM   2186 C  CA  . PRO A 1 341 ? 9.50200   7.38800   27.30600  1.000 41.59087  ?  618  PRO B CA  1 
ATOM   2187 C  C   . PRO A 1 341 ? 8.47300   8.37600   26.78900  1.000 45.70581  ?  618  PRO B C   1 
ATOM   2188 O  O   . PRO A 1 341 ? 7.37600   8.50800   27.34500  1.000 50.49630  ?  618  PRO B O   1 
ATOM   2189 C  CB  . PRO A 1 341 ? 9.27700   5.97900   26.74000  1.000 42.52954  ?  618  PRO B CB  1 
ATOM   2190 C  CG  . PRO A 1 341 ? 8.36600   5.34200   27.70700  1.000 45.60228  ?  618  PRO B CG  1 
ATOM   2191 C  CD  . PRO A 1 341 ? 8.81900   5.86100   29.05700  1.000 45.30116  ?  618  PRO B CD  1 
ATOM   2192 N  N   . ALA A 1 342 ? 8.83600   9.08400   25.72800  1.000 41.34083  ?  619  ALA B N   1 
ATOM   2193 C  CA  . ALA A 1 342 ? 7.94900   10.09000  25.17200  1.000 46.66646  ?  619  ALA B CA  1 
ATOM   2194 C  C   . ALA A 1 342 ? 7.13400   9.50100   24.03100  1.000 44.68381  ?  619  ALA B C   1 
ATOM   2195 O  O   . ALA A 1 342 ? 7.64900   8.73800   23.21000  1.000 45.71332  ?  619  ALA B O   1 
ATOM   2196 C  CB  . ALA A 1 342 ? 8.74100   11.31900  24.67900  1.000 46.40840  ?  619  ALA B CB  1 
ATOM   2197 N  N   . GLN A 1 343 ? 5.86500   9.87600   23.97100  1.000 44.28396  ?  620  GLN B N   1 
ATOM   2198 C  CA  . GLN A 1 343 ? 5.10200   9.73300   22.74400  1.000 44.66605  ?  620  GLN B CA  1 
ATOM   2199 C  C   . GLN A 1 343 ? 5.21700   11.01300  21.92300  1.000 48.16400  ?  620  GLN B C   1 
ATOM   2200 O  O   . GLN A 1 343 ? 4.94600   12.10800  22.42800  1.000 48.33019  ?  620  GLN B O   1 
ATOM   2201 C  CB  . GLN A 1 343 ? 3.64300   9.43300   23.02000  1.000 41.77851  ?  620  GLN B CB  1 
ATOM   2202 C  CG  . GLN A 1 343 ? 2.92000   9.11600   21.75700  1.000 48.86276  ?  620  GLN B CG  1 
ATOM   2203 C  CD  . GLN A 1 343 ? 1.42600   9.01800   21.96200  1.000 62.24916  ?  620  GLN B CD  1 
ATOM   2204 O  OE1 . GLN A 1 343 ? 0.78800   9.94200   22.48600  1.000 60.75312  ?  620  GLN B OE1 1 
ATOM   2205 N  NE2 . GLN A 1 343 ? 0.85700   7.88900   21.56000  1.000 63.39940  ?  620  GLN B NE2 1 
ATOM   2206 N  N   . LEU A 1 344 ? 5.61400   10.86900  20.65600  1.000 46.07934  ?  621  LEU B N   1 
ATOM   2207 C  CA  . LEU A 1 344 ? 5.91300   11.99500  19.77300  1.000 41.12519  ?  621  LEU B CA  1 
ATOM   2208 C  C   . LEU A 1 344 ? 5.21900   11.79500  18.43400  1.000 43.98980  ?  621  LEU B C   1 
ATOM   2209 O  O   . LEU A 1 344 ? 5.28200   10.70900  17.85400  1.000 49.10370  ?  621  LEU B O   1 
ATOM   2210 C  CB  . LEU A 1 344 ? 7.42800   12.12000  19.54600  1.000 39.85283  ?  621  LEU B CB  1 
ATOM   2211 C  CG  . LEU A 1 344 ? 8.30200   12.18600  20.79900  1.000 43.25035  ?  621  LEU B CG  1 
ATOM   2212 C  CD1 . LEU A 1 344 ? 9.75400   12.02500  20.39800  1.000 44.72793  ?  621  LEU B CD1 1 
ATOM   2213 C  CD2 . LEU A 1 344 ? 8.06700   13.54500  21.46800  1.000 42.12375  ?  621  LEU B CD2 1 
ATOM   2214 N  N   . PHE A 1 345 ? 4.59600   12.83700  17.92700  1.000 46.32402  ?  622  PHE B N   1 
ATOM   2215 C  CA  . PHE A 1 345 ? 3.98000   12.80000  16.60800  1.000 46.83438  ?  622  PHE B CA  1 
ATOM   2216 C  C   . PHE A 1 345 ? 4.87800   13.50700  15.60500  1.000 50.16259  ?  622  PHE B C   1 
ATOM   2217 O  O   . PHE A 1 345 ? 5.13200   14.71300  15.72900  1.000 52.72335  ?  622  PHE B O   1 
ATOM   2218 C  CB  . PHE A 1 345 ? 2.58700   13.42800  16.63900  1.000 47.61483  ?  622  PHE B CB  1 
ATOM   2219 C  CG  . PHE A 1 345 ? 1.61100   12.62200  17.42100  1.000 51.60079  ?  622  PHE B CG  1 
ATOM   2220 C  CD1 . PHE A 1 345 ? 1.51600   12.78000  18.80200  1.000 53.59619  ?  622  PHE B CD1 1 
ATOM   2221 C  CD2 . PHE A 1 345 ? 0.83000   11.66700  16.79600  1.000 49.05621  ?  622  PHE B CD2 1 
ATOM   2222 C  CE1 . PHE A 1 345 ? 0.64100   12.01700  19.53200  1.000 56.81080  ?  622  PHE B CE1 1 
ATOM   2223 C  CE2 . PHE A 1 345 ? -0.04800  10.90700  17.51400  1.000 47.34704  ?  622  PHE B CE2 1 
ATOM   2224 C  CZ  . PHE A 1 345 ? -0.14900  11.07600  18.88700  1.000 50.58041  ?  622  PHE B CZ  1 
ATOM   2225 N  N   . PHE A 1 346 ? 5.34100   12.76500  14.59800  1.000 46.23235  ?  623  PHE B N   1 
ATOM   2226 C  CA  . PHE A 1 346 ? 6.22400   13.36300  13.56300  1.000 49.14095  ?  623  PHE B CA  1 
ATOM   2227 C  C   . PHE A 1 346 ? 5.38200   13.88900  12.39700  1.000 49.01746  ?  623  PHE B C   1 
ATOM   2228 O  O   . PHE A 1 346 ? 4.51700   13.14400  11.90300  1.000 46.83254  ?  623  PHE B O   1 
ATOM   2229 C  CB  . PHE A 1 346 ? 7.26200   12.35000  13.07000  1.000 43.08615  ?  623  PHE B CB  1 
ATOM   2230 C  CG  . PHE A 1 346 ? 8.46500   12.18200  13.96200  1.000 50.72049  ?  623  PHE B CG  1 
ATOM   2231 C  CD1 . PHE A 1 346 ? 8.34200   11.64600  15.23400  1.000 55.04310  ?  623  PHE B CD1 1 
ATOM   2232 C  CD2 . PHE A 1 346 ? 9.72300   12.57300  13.53400  1.000 51.02692  ?  623  PHE B CD2 1 
ATOM   2233 C  CE1 . PHE A 1 346 ? 9.45200   11.49400  16.04900  1.000 57.33101  ?  623  PHE B CE1 1 
ATOM   2234 C  CE2 . PHE A 1 346 ? 10.83200  12.42300  14.35100  1.000 52.24992  ?  623  PHE B CE2 1 
ATOM   2235 C  CZ  . PHE A 1 346 ? 10.69500  11.88200  15.60700  1.000 51.05038  ?  623  PHE B CZ  1 
ATOM   2236 N  N   . LYS A 1 347 ? 5.65900   15.10400  11.94700  1.000 55.97782  ?  624  LYS B N   1 
ATOM   2237 C  CA  . LYS A 1 347 ? 4.96400   15.66300  10.79800  1.000 52.21206  ?  624  LYS B CA  1 
ATOM   2238 C  C   . LYS A 1 347 ? 5.55100   15.11000  9.50300   1.000 52.29167  ?  624  LYS B C   1 
ATOM   2239 O  O   . LYS A 1 347 ? 6.75100   15.24800  9.24600   1.000 59.95479  ?  624  LYS B O   1 
ATOM   2240 C  CB  . LYS A 1 347 ? 5.06000   17.18600  10.82800  1.000 55.20602  ?  624  LYS B CB  1 
ATOM   2241 C  CG  . LYS A 1 347 ? 4.16700   17.84500  11.86200  1.000 68.38103  ?  624  LYS B CG  1 
ATOM   2242 C  CD  . LYS A 1 347 ? 4.43700   19.33600  11.91900  1.000 83.84131  ?  624  LYS B CD  1 
ATOM   2243 C  CE  . LYS A 1 347 ? 5.83800   19.60700  12.42800  1.000 77.31056  ?  624  LYS B CE  1 
ATOM   2244 N  NZ  . LYS A 1 347 ? 6.04500   21.06500  12.62200  1.000 74.41186  ?  624  LYS B NZ  1 
ATOM   2245 N  N   . THR A 1 348 ? 4.70900   14.49100  8.68200   1.000 50.86233  ?  625  THR B N   1 
ATOM   2246 C  CA  . THR A 1 348 ? 5.20900   13.90000  7.41400   1.000 54.66369  ?  625  THR B CA  1 
ATOM   2247 C  C   . THR A 1 348 ? 5.25900   14.98600  6.33500   1.000 59.84722  ?  625  THR B C   1 
ATOM   2248 O  O   . THR A 1 348 ? 4.51400   15.97600  6.46400   1.000 58.39089  ?  625  THR B O   1 
ATOM   2249 C  CB  . THR A 1 348 ? 4.34000   12.71700  6.97300   1.000 55.60391  ?  625  THR B CB  1 
ATOM   2250 O  OG1 . THR A 1 348 ? 3.10600   13.23900  6.48100   1.000 63.87962  ?  625  THR B OG1 1 
ATOM   2251 C  CG2 . THR A 1 348 ? 4.08300   11.72800  8.08900   1.000 59.93603  ?  625  THR B CG2 1 
ATOM   2252 N  N   . GLU A 1 349 ? 6.09800   14.79900  5.31400   1.000 58.12451  ?  626  GLU B N   1 
ATOM   2253 C  CA  . GLU A 1 349 ? 6.20500   15.78600  4.23700   1.000 61.24559  ?  626  GLU B CA  1 
ATOM   2254 C  C   . GLU A 1 349 ? 4.85800   16.06800  3.58600   1.000 61.18471  ?  626  GLU B C   1 
ATOM   2255 O  O   . GLU A 1 349 ? 4.63800   17.16500  3.05900   1.000 54.51243  ?  626  GLU B O   1 
ATOM   2256 C  CB  . GLU A 1 349 ? 7.19100   15.30900  3.17200   1.000 58.33539  ?  626  GLU B CB  1 
ATOM   2257 C  CG  . GLU A 1 349 ? 6.76700   14.01100  2.50800   1.000 61.83492  ?  626  GLU B CG  1 
ATOM   2258 C  CD  . GLU A 1 349 ? 7.67500   13.61800  1.34900   1.000 59.66615  ?  626  GLU B CD  1 
ATOM   2259 O  OE1 . GLU A 1 349 ? 8.22800   14.51500  0.66600   1.000 71.22492  ?  626  GLU B OE1 1 
ATOM   2260 N  N   . ASP A 1 350 ? 3.96000   15.08000  3.60000   1.000 61.23234  ?  627  ASP B N   1 
ATOM   2261 C  CA  . ASP A 1 350 ? 2.65000   15.16700  2.97400   1.000 57.70306  ?  627  ASP B CA  1 
ATOM   2262 C  C   . ASP A 1 350 ? 1.56000   15.56100  3.96800   1.000 62.00135  ?  627  ASP B C   1 
ATOM   2263 O  O   . ASP A 1 350 ? 0.37600   15.33900  3.69800   1.000 69.06302  ?  627  ASP B O   1 
ATOM   2264 C  CB  . ASP A 1 350 ? 2.30100   13.83600  2.31400   1.000 59.61291  ?  627  ASP B CB  1 
ATOM   2265 C  CG  . ASP A 1 350 ? 2.28900   12.70700  3.30100   1.000 77.71478  ?  627  ASP B CG  1 
ATOM   2266 O  OD1 . ASP A 1 350 ? 1.37800   12.70700  4.15900   1.000 78.30694  ?  627  ASP B OD1 1 
ATOM   2267 O  OD2 . ASP A 1 350 ? 3.20400   11.83800  3.24600   1.000 92.54909  -1 627  ASP B OD2 1 
ATOM   2268 N  N   . GLY A 1 351 ? 1.93500   16.11600  5.12000   1.000 64.14385  ?  628  GLY B N   1 
ATOM   2269 C  CA  . GLY A 1 351 ? 0.98000   16.68500  6.04500   1.000 56.57913  ?  628  GLY B CA  1 
ATOM   2270 C  C   . GLY A 1 351 ? 0.39100   15.72400  7.05000   1.000 59.26896  ?  628  GLY B C   1 
ATOM   2271 O  O   . GLY A 1 351 ? -0.41100  16.14400  7.88700   1.000 64.30449  ?  628  GLY B O   1 
ATOM   2272 N  N   . GLY A 1 352 ? 0.75100   14.45000  7.00300   1.000 62.24254  ?  629  GLY B N   1 
ATOM   2273 C  CA  . GLY A 1 352 ? 0.25700   13.48800  7.95500   1.000 51.08718  ?  629  GLY B CA  1 
ATOM   2274 C  C   . GLY A 1 352 ? 1.09900   13.45100  9.20900   1.000 56.24409  ?  629  GLY B C   1 
ATOM   2275 O  O   . GLY A 1 352 ? 2.01600   14.24700  9.40700   1.000 55.99835  ?  629  GLY B O   1 
ATOM   2276 N  N   . LYS A 1 353 ? 0.78900   12.47800  10.05600  1.000 57.34576  ?  630  LYS B N   1 
ATOM   2277 C  CA  . LYS A 1 353 ? 1.37200   12.34400  11.38000  1.000 54.42475  ?  630  LYS B CA  1 
ATOM   2278 C  C   . LYS A 1 353 ? 1.83500   10.91100  11.56200  1.000 54.22023  ?  630  LYS B C   1 
ATOM   2279 O  O   . LYS A 1 353 ? 1.07000   9.98000   11.30700  1.000 60.63159  ?  630  LYS B O   1 
ATOM   2280 C  CB  . LYS A 1 353 ? 0.36000   12.67100  12.48200  1.000 53.00301  ?  630  LYS B CB  1 
ATOM   2281 C  CG  . LYS A 1 353 ? -0.14300  14.10100  12.54500  1.000 61.21371  ?  630  LYS B CG  1 
ATOM   2282 C  CD  . LYS A 1 353 ? -1.07300  14.26000  13.76200  1.000 72.16693  ?  630  LYS B CD  1 
ATOM   2283 C  CE  . LYS A 1 353 ? -2.51000  13.79900  13.47900  1.000 82.53127  ?  630  LYS B CE  1 
ATOM   2284 N  NZ  . LYS A 1 353 ? -3.28900  14.86600  12.74300  1.000 90.96712  ?  630  LYS B NZ  1 
ATOM   2285 N  N   . TYR A 1 354 ? 3.06000   10.72800  12.02600  1.000 47.71232  ?  631  TYR B N   1 
ATOM   2286 C  CA  . TYR A 1 354 ? 3.56300   9.38900   12.33300  1.000 49.32231  ?  631  TYR B CA  1 
ATOM   2287 C  C   . TYR A 1 354 ? 3.89700   9.32500   13.82100  1.000 51.60364  ?  631  TYR B C   1 
ATOM   2288 O  O   . TYR A 1 354 ? 4.88600   9.94800   14.26100  1.000 48.82836  ?  631  TYR B O   1 
ATOM   2289 C  CB  . TYR A 1 354 ? 4.78700   9.07100   11.47700  1.000 40.37496  ?  631  TYR B CB  1 
ATOM   2290 C  CG  . TYR A 1 354 ? 5.24900   7.63500   11.47700  1.000 45.39916  ?  631  TYR B CG  1 
ATOM   2291 C  CD1 . TYR A 1 354 ? 5.78700   7.06100   12.61700  1.000 46.90591  ?  631  TYR B CD1 1 
ATOM   2292 C  CD2 . TYR A 1 354 ? 5.20200   6.86700   10.32100  1.000 52.60843  ?  631  TYR B CD2 1 
ATOM   2293 C  CE1 . TYR A 1 354 ? 6.24600   5.76200   12.61600  1.000 50.89454  ?  631  TYR B CE1 1 
ATOM   2294 C  CE2 . TYR A 1 354 ? 5.65700   5.54700   10.31500  1.000 54.48283  ?  631  TYR B CE2 1 
ATOM   2295 C  CZ  . TYR A 1 354 ? 6.17400   5.00500   11.46700  1.000 50.61220  ?  631  TYR B CZ  1 
ATOM   2296 O  OH  . TYR A 1 354 ? 6.62600   3.70500   11.48500  1.000 50.44249  ?  631  TYR B OH  1 
ATOM   2297 N  N   . PRO A 1 355 ? 3.09700   8.63200   14.63400  1.000 48.21879  ?  632  PRO B N   1 
ATOM   2298 C  CA  . PRO A 1 355 ? 3.38100   8.56100   16.07600  1.000 45.69621  ?  632  PRO B CA  1 
ATOM   2299 C  C   . PRO A 1 355 ? 4.45000   7.53500   16.39800  1.000 43.40760  ?  632  PRO B C   1 
ATOM   2300 O  O   . PRO A 1 355 ? 4.44600   6.41800   15.87900  1.000 47.79476  ?  632  PRO B O   1 
ATOM   2301 C  CB  . PRO A 1 355 ? 2.02900   8.15400   16.68200  1.000 49.75752  ?  632  PRO B CB  1 
ATOM   2302 C  CG  . PRO A 1 355 ? 1.37000   7.36500   15.61200  1.000 46.08005  ?  632  PRO B CG  1 
ATOM   2303 C  CD  . PRO A 1 355 ? 1.81600   7.99500   14.28500  1.000 50.27511  ?  632  PRO B CD  1 
ATOM   2304 N  N   . VAL A 1 356 ? 5.36900   7.92100   17.28100  1.000 46.57715  ?  633  VAL B N   1 
ATOM   2305 C  CA  . VAL A 1 356 ? 6.42800   7.03400   17.75300  1.000 43.97515  ?  633  VAL B CA  1 
ATOM   2306 C  C   . VAL A 1 356 ? 6.49900   7.12400   19.27400  1.000 44.76354  ?  633  VAL B C   1 
ATOM   2307 O  O   . VAL A 1 356 ? 6.00500   8.06700   19.89600  1.000 40.58351  ?  633  VAL B O   1 
ATOM   2308 C  CB  . VAL A 1 356 ? 7.82900   7.37400   17.16100  1.000 46.11650  ?  633  VAL B CB  1 
ATOM   2309 C  CG1 . VAL A 1 356 ? 7.80200   7.47200   15.63700  1.000 41.11996  ?  633  VAL B CG1 1 
ATOM   2310 C  CG2 . VAL A 1 356 ? 8.37200   8.67500   17.80600  1.000 45.12804  ?  633  VAL B CG2 1 
ATOM   2311 N  N   . ILE A 1 357 ? 7.14300   6.12300   19.86700  1.000 44.01918  ?  634  ILE B N   1 
ATOM   2312 C  CA  . ILE A 1 357 ? 7.63700   6.20100   21.23300  1.000 40.99691  ?  634  ILE B CA  1 
ATOM   2313 C  C   . ILE A 1 357 ? 9.13300   6.38800   21.14500  1.000 40.91781  ?  634  ILE B C   1 
ATOM   2314 O  O   . ILE A 1 357 ? 9.81200   5.61900   20.45500  1.000 41.96229  ?  634  ILE B O   1 
ATOM   2315 C  CB  . ILE A 1 357 ? 7.31900   4.92600   22.03100  1.000 47.12260  ?  634  ILE B CB  1 
ATOM   2316 C  CG1 . ILE A 1 357 ? 5.81200   4.69200   22.08100  1.000 49.96166  ?  634  ILE B CG1 1 
ATOM   2317 C  CG2 . ILE A 1 357 ? 7.93700   5.02400   23.43100  1.000 38.14491  ?  634  ILE B CG2 1 
ATOM   2318 C  CD1 . ILE A 1 357 ? 5.44800   3.26400   22.42400  1.000 47.49054  ?  634  ILE B CD1 1 
ATOM   2319 N  N   . PHE A 1 358 ? 9.65900   7.39600   21.81900  1.000 43.64509  ?  635  PHE B N   1 
ATOM   2320 C  CA  . PHE A 1 358 ? 11.10200  7.51700   21.95600  1.000 40.96719  ?  635  PHE B CA  1 
ATOM   2321 C  C   . PHE A 1 358 ? 11.48300  7.11000   23.37400  1.000 41.55796  ?  635  PHE B C   1 
ATOM   2322 O  O   . PHE A 1 358 ? 10.96800  7.67800   24.34200  1.000 44.66856  ?  635  PHE B O   1 
ATOM   2323 C  CB  . PHE A 1 358 ? 11.60300  8.92700   21.63800  1.000 40.99309  ?  635  PHE B CB  1 
ATOM   2324 C  CG  . PHE A 1 358 ? 13.09300  9.01500   21.61900  1.000 43.97517  ?  635  PHE B CG  1 
ATOM   2325 C  CD1 . PHE A 1 358 ? 13.82400  8.28800   20.66900  1.000 45.30101  ?  635  PHE B CD1 1 
ATOM   2326 C  CD2 . PHE A 1 358 ? 13.77500  9.74900   22.57400  1.000 43.05702  ?  635  PHE B CD2 1 
ATOM   2327 C  CE1 . PHE A 1 358 ? 15.20900  8.31900   20.65300  1.000 43.79404  ?  635  PHE B CE1 1 
ATOM   2328 C  CE2 . PHE A 1 358 ? 15.17200  9.79800   22.56800  1.000 46.46961  ?  635  PHE B CE2 1 
ATOM   2329 C  CZ  . PHE A 1 358 ? 15.89200  9.08600   21.60900  1.000 47.65687  ?  635  PHE B CZ  1 
ATOM   2330 N  N   . LYS A 1 359 ? 12.35900  6.11800   23.48900  1.000 42.78987  ?  636  LYS B N   1 
ATOM   2331 C  CA  . LYS A 1 359 ? 12.81900  5.60500   24.77100  1.000 42.50723  ?  636  LYS B CA  1 
ATOM   2332 C  C   . LYS A 1 359 ? 14.27300  5.98900   24.95400  1.000 46.27068  ?  636  LYS B C   1 
ATOM   2333 O  O   . LYS A 1 359 ? 15.08600  5.82900   24.03100  1.000 50.99106  ?  636  LYS B O   1 
ATOM   2334 C  CB  . LYS A 1 359 ? 12.69000  4.08200   24.86000  1.000 48.39530  ?  636  LYS B CB  1 
ATOM   2335 C  CG  . LYS A 1 359 ? 11.31000  3.50200   24.60000  1.000 53.97889  ?  636  LYS B CG  1 
ATOM   2336 C  CD  . LYS A 1 359 ? 11.25600  2.03500   25.07500  1.000 58.72629  ?  636  LYS B CD  1 
ATOM   2337 C  CE  . LYS A 1 359 ? 9.89400   1.38000   24.81200  1.000 60.71701  ?  636  LYS B CE  1 
ATOM   2338 N  N   . HIS A 1 360 ? 14.59500  6.49600   26.13300  1.000 43.71740  ?  637  HIS B N   1 
ATOM   2339 C  CA  . HIS A 1 360 ? 15.95500  6.81300   26.51800  1.000 46.04992  ?  637  HIS B CA  1 
ATOM   2340 C  C   . HIS A 1 360 ? 16.27100  6.07000   27.80900  1.000 53.40467  ?  637  HIS B C   1 
ATOM   2341 O  O   . HIS A 1 360 ? 15.42800  5.98800   28.70500  1.000 54.34886  ?  637  HIS B O   1 
ATOM   2342 C  CB  . HIS A 1 360 ? 16.14600  8.32100   26.72600  1.000 45.84419  ?  637  HIS B CB  1 
ATOM   2343 C  CG  . HIS A 1 360 ? 17.53700  8.68300   27.14600  1.000 58.44365  ?  637  HIS B CG  1 
ATOM   2344 N  ND1 . HIS A 1 360 ? 18.65300  8.27800   26.44000  1.000 60.69487  ?  637  HIS B ND1 1 
ATOM   2345 C  CD2 . HIS A 1 360 ? 18.00100  9.38300   28.20800  1.000 59.78196  ?  637  HIS B CD2 1 
ATOM   2346 C  CE1 . HIS A 1 360 ? 19.74200  8.71900   27.04200  1.000 59.17747  ?  637  HIS B CE1 1 
ATOM   2347 N  NE2 . HIS A 1 360 ? 19.37400  9.39700   28.11500  1.000 66.66571  ?  637  HIS B NE2 1 
ATOM   2348 N  N   . GLY A 1 361 ? 17.48600  5.54200   27.91100  1.000 54.88607  ?  638  GLY B N   1 
ATOM   2349 C  CA  . GLY A 1 361 ? 17.85800  4.74200   29.06500  1.000 45.17401  ?  638  GLY B CA  1 
ATOM   2350 C  C   . GLY A 1 361 ? 17.43600  3.29000   28.98700  1.000 54.54360  ?  638  GLY B C   1 
ATOM   2351 O  O   . GLY A 1 361 ? 17.19700  2.67100   30.01600  1.000 58.92788  ?  638  GLY B O   1 
ATOM   2352 N  N   . ASP A 1 362 ? 17.36800  2.71500   27.79200  1.000 54.15456  ?  639  ASP B N   1 
ATOM   2353 C  CA  . ASP A 1 362 ? 16.88600  1.35700   27.60500  1.000 52.26766  ?  639  ASP B CA  1 
ATOM   2354 C  C   . ASP A 1 362 ? 17.57000  0.75600   26.38200  1.000 51.41499  ?  639  ASP B C   1 
ATOM   2355 O  O   . ASP A 1 362 ? 17.81300  1.46000   25.40600  1.000 52.45592  ?  639  ASP B O   1 
ATOM   2356 C  CB  . ASP A 1 362 ? 15.36700  1.36200   27.41400  1.000 67.01683  ?  639  ASP B CB  1 
ATOM   2357 C  CG  . ASP A 1 362 ? 14.73100  0.09100   27.86200  1.000 72.10114  ?  639  ASP B CG  1 
ATOM   2358 O  OD1 . ASP A 1 362 ? 15.42300  -0.67900  28.57500  1.000 77.59637  ?  639  ASP B OD1 1 
ATOM   2359 O  OD2 . ASP A 1 362 ? 13.55200  -0.13800  27.50100  1.000 83.07558  -1 639  ASP B OD2 1 
ATOM   2360 N  N   . ASP A 1 363 ? 17.88600  -0.53400  26.43400  1.000 45.10655  ?  640  ASP B N   1 
ATOM   2361 C  CA  . ASP A 1 363 ? 18.51800  -1.22200  25.30900  1.000 46.63984  ?  640  ASP B CA  1 
ATOM   2362 C  C   . ASP A 1 363 ? 17.41900  -1.91600  24.51800  1.000 40.92532  ?  640  ASP B C   1 
ATOM   2363 O  O   . ASP A 1 363 ? 16.90800  -2.95400  24.92700  1.000 50.63404  ?  640  ASP B O   1 
ATOM   2364 C  CB  . ASP A 1 363 ? 19.58000  -2.21000  25.78300  1.000 40.28608  ?  640  ASP B CB  1 
ATOM   2365 C  CG  . ASP A 1 363 ? 20.43300  -2.75800  24.63500  1.000 51.39471  ?  640  ASP B CG  1 
ATOM   2366 O  OD1 . ASP A 1 363 ? 19.97200  -2.79000  23.45700  1.000 50.79820  ?  640  ASP B OD1 1 
ATOM   2367 O  OD2 . ASP A 1 363 ? 21.59000  -3.15500  24.90400  1.000 57.93747  -1 640  ASP B OD2 1 
ATOM   2368 N  N   . LEU A 1 364 ? 17.06100  -1.35100  23.38100  1.000 44.61533  ?  641  LEU B N   1 
ATOM   2369 C  CA  . LEU A 1 364 ? 15.97000  -1.88100  22.57100  1.000 44.48419  ?  641  LEU B CA  1 
ATOM   2370 C  C   . LEU A 1 364 ? 16.36300  -3.08700  21.72700  1.000 42.03559  ?  641  LEU B C   1 
ATOM   2371 O  O   . LEU A 1 364 ? 15.51400  -3.59600  20.98900  1.000 42.23828  ?  641  LEU B O   1 
ATOM   2372 C  CB  . LEU A 1 364 ? 15.43000  -0.79000  21.64600  1.000 36.97676  ?  641  LEU B CB  1 
ATOM   2373 C  CG  . LEU A 1 364 ? 14.33500  0.08100   22.25700  1.000 44.83251  ?  641  LEU B CG  1 
ATOM   2374 C  CD1 . LEU A 1 364 ? 14.67800  0.47400   23.63100  1.000 51.30523  ?  641  LEU B CD1 1 
ATOM   2375 C  CD2 . LEU A 1 364 ? 14.16300  1.31100   21.39000  1.000 42.59650  ?  641  LEU B CD2 1 
ATOM   2376 N  N   . ARG A 1 365 ? 17.61200  -3.55500  21.79700  1.000 41.82945  ?  642  ARG B N   1 
ATOM   2377 C  CA  . ARG A 1 365 ? 18.07500  -4.47800  20.76100  1.000 41.10626  ?  642  ARG B CA  1 
ATOM   2378 C  C   . ARG A 1 365 ? 17.36500  -5.82900  20.83300  1.000 40.41688  ?  642  ARG B C   1 
ATOM   2379 O  O   . ARG A 1 365 ? 17.13600  -6.45400  19.79300  1.000 43.12538  ?  642  ARG B O   1 
ATOM   2380 C  CB  . ARG A 1 365 ? 19.59900  -4.63100  20.82600  1.000 44.50659  ?  642  ARG B CB  1 
ATOM   2381 C  CG  . ARG A 1 365 ? 20.34600  -3.49300  20.10300  1.000 46.15517  ?  642  ARG B CG  1 
ATOM   2382 C  CD  . ARG A 1 365 ? 21.83500  -3.60700  20.24100  1.000 44.65094  ?  642  ARG B CD  1 
ATOM   2383 N  NE  . ARG A 1 365 ? 22.24100  -3.52600  21.63700  1.000 50.17029  ?  642  ARG B NE  1 
ATOM   2384 C  CZ  . ARG A 1 365 ? 23.49300  -3.64500  22.06000  1.000 52.32417  ?  642  ARG B CZ  1 
ATOM   2385 N  NH1 . ARG A 1 365 ? 24.48700  -3.88100  21.21600  1.000 49.45900  ?  642  ARG B NH1 1 
ATOM   2386 N  NH2 . ARG A 1 365 ? 23.75300  -3.52300  23.36200  1.000 51.83948  ?  642  ARG B NH2 1 
ATOM   2387 N  N   . GLN A 1 366 ? 16.96600  -6.28400  22.02900  1.000 43.70499  ?  643  GLN B N   1 
ATOM   2388 C  CA  . GLN A 1 366 ? 16.24300  -7.54400  22.06200  1.000 40.94813  ?  643  GLN B CA  1 
ATOM   2389 C  C   . GLN A 1 366 ? 14.87200  -7.38300  21.42600  1.000 42.19236  ?  643  GLN B C   1 
ATOM   2390 O  O   . GLN A 1 366 ? 14.46600  -8.21500  20.60100  1.000 43.76890  ?  643  GLN B O   1 
ATOM   2391 C  CB  . GLN A 1 366 ? 16.12700  -8.09400  23.48000  1.000 38.42946  ?  643  GLN B CB  1 
ATOM   2392 C  CG  . GLN A 1 366 ? 15.43000  -9.45300  23.53800  1.000 34.21254  ?  643  GLN B CG  1 
ATOM   2393 C  CD  . GLN A 1 366 ? 15.74200  -10.21100 24.82000  1.000 44.78892  ?  643  GLN B CD  1 
ATOM   2394 O  OE1 . GLN A 1 366 ? 16.90300  -10.54600 25.10400  1.000 47.92508  ?  643  GLN B OE1 1 
ATOM   2395 N  NE2 . GLN A 1 366 ? 14.70700  -10.47600 25.61000  1.000 40.76909  ?  643  GLN B NE2 1 
ATOM   2396 N  N   . ASP A 1 367 ? 14.17800  -6.28600  21.73700  1.000 36.43735  ?  644  ASP B N   1 
ATOM   2397 C  CA  . ASP A 1 367 ? 12.91700  -6.00200  21.05800  1.000 38.76063  ?  644  ASP B CA  1 
ATOM   2398 C  C   . ASP A 1 367 ? 13.11400  -5.84700  19.55700  1.000 37.66854  ?  644  ASP B C   1 
ATOM   2399 O  O   . ASP A 1 367 ? 12.32200  -6.36700  18.76700  1.000 39.40635  ?  644  ASP B O   1 
ATOM   2400 C  CB  . ASP A 1 367 ? 12.27200  -4.75700  21.65100  1.000 37.95022  ?  644  ASP B CB  1 
ATOM   2401 C  CG  . ASP A 1 367 ? 11.66700  -5.03100  23.02500  1.000 54.07783  ?  644  ASP B CG  1 
ATOM   2402 O  OD1 . ASP A 1 367 ? 10.53100  -5.56700  23.08600  1.000 48.81464  ?  644  ASP B OD1 1 
ATOM   2403 O  OD2 . ASP A 1 367 ? 12.36500  -4.75100  24.04700  1.000 61.57973  -1 644  ASP B OD2 1 
ATOM   2404 N  N   . GLN A 1 368 ? 14.17100  -5.14500  19.15100  1.000 37.74892  ?  645  GLN B N   1 
ATOM   2405 C  CA  . GLN A 1 368 ? 14.46500  -4.97000  17.73600  1.000 34.61834  ?  645  GLN B CA  1 
ATOM   2406 C  C   . GLN A 1 368 ? 14.59400  -6.31000  17.01800  1.000 39.79222  ?  645  GLN B C   1 
ATOM   2407 O  O   . GLN A 1 368 ? 14.05000  -6.48800  15.91900  1.000 35.67664  ?  645  GLN B O   1 
ATOM   2408 C  CB  . GLN A 1 368 ? 15.74300  -4.15900  17.58800  1.000 37.62483  ?  645  GLN B CB  1 
ATOM   2409 C  CG  . GLN A 1 368 ? 16.14800  -3.86100  16.17400  1.000 36.02966  ?  645  GLN B CG  1 
ATOM   2410 C  CD  . GLN A 1 368 ? 17.39200  -3.01000  16.13000  1.000 40.89085  ?  645  GLN B CD  1 
ATOM   2411 O  OE1 . GLN A 1 368 ? 17.33300  -1.83000  15.80200  1.000 39.67129  ?  645  GLN B OE1 1 
ATOM   2412 N  NE2 . GLN A 1 368 ? 18.53400  -3.60200  16.49600  1.000 39.77099  ?  645  GLN B NE2 1 
ATOM   2413 N  N   . LEU A 1 369 ? 15.29600  -7.27600  17.62900  1.000 37.50199  ?  646  LEU B N   1 
ATOM   2414 C  CA  . LEU A 1 369 ? 15.44700  -8.57400  16.98800  1.000 36.19703  ?  646  LEU B CA  1 
ATOM   2415 C  C   . LEU A 1 369 ? 14.10900  -9.30000  16.86400  1.000 36.86683  ?  646  LEU B C   1 
ATOM   2416 O  O   . LEU A 1 369 ? 13.77800  -9.82200  15.79300  1.000 41.54274  ?  646  LEU B O   1 
ATOM   2417 C  CB  . LEU A 1 369 ? 16.46200  -9.42200  17.74900  1.000 39.17427  ?  646  LEU B CB  1 
ATOM   2418 C  CG  . LEU A 1 369 ? 16.44100  -10.91100 17.36600  1.000 42.34819  ?  646  LEU B CG  1 
ATOM   2419 C  CD1 . LEU A 1 369 ? 16.88400  -11.19900 15.89400  1.000 35.30766  ?  646  LEU B CD1 1 
ATOM   2420 C  CD2 . LEU A 1 369 ? 17.30600  -11.69400 18.33400  1.000 39.54722  ?  646  LEU B CD2 1 
ATOM   2421 N  N   . ILE A 1 370 ? 13.31700  -9.32800  17.93600  1.000 37.03669  ?  647  ILE B N   1 
ATOM   2422 C  CA  . ILE A 1 370 ? 12.04900  -10.05900 17.90900  1.000 36.69785  ?  647  ILE B CA  1 
ATOM   2423 C  C   . ILE A 1 370 ? 11.10400  -9.46100  16.87600  1.000 41.38859  ?  647  ILE B C   1 
ATOM   2424 O  O   . ILE A 1 370 ? 10.49000  -10.18900 16.07900  1.000 41.84490  ?  647  ILE B O   1 
ATOM   2425 C  CB  . ILE A 1 370 ? 11.40100  -10.07400 19.30400  1.000 39.86184  ?  647  ILE B CB  1 
ATOM   2426 C  CG1 . ILE A 1 370 ? 12.19200  -10.97200 20.24700  1.000 40.43358  ?  647  ILE B CG1 1 
ATOM   2427 C  CG2 . ILE A 1 370 ? 9.94200   -10.50000 19.22100  1.000 37.69812  ?  647  ILE B CG2 1 
ATOM   2428 C  CD1 . ILE A 1 370 ? 12.41400  -12.37900 19.70200  1.000 46.10831  ?  647  ILE B CD1 1 
ATOM   2429 N  N   . LEU A 1 371 ? 10.96100  -8.12100  16.87900  1.000 38.68681  ?  648  LEU B N   1 
ATOM   2430 C  CA  . LEU A 1 371 ? 10.08500  -7.49100  15.89500  1.000 42.89647  ?  648  LEU B CA  1 
ATOM   2431 C  C   . LEU A 1 371 ? 10.61300  -7.67400  14.46800  1.000 41.53732  ?  648  LEU B C   1 
ATOM   2432 O  O   . LEU A 1 371 ? 9.81600   -7.79700  13.53400  1.000 38.76842  ?  648  LEU B O   1 
ATOM   2433 C  CB  . LEU A 1 371 ? 9.88900   -6.00800  16.20600  1.000 31.50243  ?  648  LEU B CB  1 
ATOM   2434 C  CG  . LEU A 1 371 ? 8.68400   -5.71700  17.09300  1.000 42.57901  ?  648  LEU B CG  1 
ATOM   2435 C  CD1 . LEU A 1 371 ? 7.34500   -6.14900  16.45100  1.000 38.43668  ?  648  LEU B CD1 1 
ATOM   2436 C  CD2 . LEU A 1 371 ? 8.89400   -6.41900  18.41300  1.000 42.37765  ?  648  LEU B CD2 1 
ATOM   2437 N  N   . GLN A 1 372 ? 11.93300  -7.71600  14.28100  1.000 36.98450  ?  649  GLN B N   1 
ATOM   2438 C  CA  . GLN A 1 372 ? 12.46600  -8.02700  12.95500  1.000 42.87891  ?  649  GLN B CA  1 
ATOM   2439 C  C   . GLN A 1 372 ? 12.07000  -9.44100  12.52900  1.000 43.70811  ?  649  GLN B C   1 
ATOM   2440 O  O   . GLN A 1 372 ? 11.61500  -9.65800  11.39100  1.000 45.28767  ?  649  GLN B O   1 
ATOM   2441 C  CB  . GLN A 1 372 ? 13.98600  -7.85900  12.94200  1.000 34.45993  ?  649  GLN B CB  1 
ATOM   2442 C  CG  . GLN A 1 372 ? 14.61200  -7.83600  11.56000  1.000 43.51470  ?  649  GLN B CG  1 
ATOM   2443 C  CD  . GLN A 1 372 ? 15.59100  -8.99500  11.36400  1.000 51.75959  ?  649  GLN B CD  1 
ATOM   2444 O  OE1 . GLN A 1 372 ? 15.70000  -9.86700  12.22700  1.000 48.27313  ?  649  GLN B OE1 1 
ATOM   2445 N  NE2 . GLN A 1 372 ? 16.31500  -8.99900  10.24000  1.000 54.24673  ?  649  GLN B NE2 1 
ATOM   2446 N  N   . ILE A 1 373 ? 12.19900  -10.40700 13.44600  1.000 41.28118  ?  650  ILE B N   1 
ATOM   2447 C  CA  . ILE A 1 373 ? 11.82000  -11.78400 13.14200  1.000 43.00466  ?  650  ILE B CA  1 
ATOM   2448 C  C   . ILE A 1 373 ? 10.31400  -11.88700 12.90600  1.000 47.38155  ?  650  ILE B C   1 
ATOM   2449 O  O   . ILE A 1 373 ? 9.85600   -12.56800 11.97200  1.000 48.52301  ?  650  ILE B O   1 
ATOM   2450 C  CB  . ILE A 1 373 ? 12.27900  -12.73900 14.25800  1.000 44.85759  ?  650  ILE B CB  1 
ATOM   2451 C  CG1 . ILE A 1 373 ? 13.80700  -12.77200 14.35800  1.000 46.75685  ?  650  ILE B CG1 1 
ATOM   2452 C  CG2 . ILE A 1 373 ? 11.77200  -14.14500 13.98300  1.000 49.23415  ?  650  ILE B CG2 1 
ATOM   2453 C  CD1 . ILE A 1 373 ? 14.48300  -13.20100 13.05400  1.000 49.74778  ?  650  ILE B CD1 1 
ATOM   2454 N  N   . ILE A 1 374 ? 9.51300   -11.21600 13.74000  1.000 45.94524  ?  651  ILE B N   1 
ATOM   2455 C  CA  . ILE A 1 374 ? 8.06900   -11.28100 13.53200  1.000 42.57707  ?  651  ILE B CA  1 
ATOM   2456 C  C   . ILE A 1 374 ? 7.71000   -10.69800 12.17500  1.000 43.16927  ?  651  ILE B C   1 
ATOM   2457 O  O   . ILE A 1 374 ? 6.86400   -11.24100 11.45600  1.000 45.64875  ?  651  ILE B O   1 
ATOM   2458 C  CB  . ILE A 1 374 ? 7.31800   -10.57900 14.66500  1.000 39.26183  ?  651  ILE B CB  1 
ATOM   2459 C  CG1 . ILE A 1 374 ? 7.48700   -11.36400 15.96900  1.000 44.08070  ?  651  ILE B CG1 1 
ATOM   2460 C  CG2 . ILE A 1 374 ? 5.84700   -10.42700 14.31100  1.000 40.59570  ?  651  ILE B CG2 1 
ATOM   2461 C  CD1 . ILE A 1 374 ? 6.87800   -10.59700 17.16700  1.000 40.97416  ?  651  ILE B CD1 1 
ATOM   2462 N  N   . SER A 1 375 ? 8.35500   -9.59300  11.79700  1.000 41.76276  ?  652  SER B N   1 
ATOM   2463 C  CA  . SER A 1 375 ? 8.14800   -9.04000  10.47000  1.000 44.06076  ?  652  SER B CA  1 
ATOM   2464 C  C   . SER A 1 375 ? 8.48100   -10.07200 9.39900   1.000 44.70663  ?  652  SER B C   1 
ATOM   2465 O  O   . SER A 1 375 ? 7.70000   -10.29200 8.46800   1.000 49.53212  ?  652  SER B O   1 
ATOM   2466 C  CB  . SER A 1 375 ? 8.98500   -7.77100  10.29400  1.000 41.06782  ?  652  SER B CB  1 
ATOM   2467 O  OG  . SER A 1 375 ? 8.87400   -7.27300  8.96300   1.000 47.40192  ?  652  SER B OG  1 
ATOM   2468 N  N   . LEU A 1 376 ? 9.63000   -10.73500 9.52100   1.000 47.94306  ?  653  LEU B N   1 
ATOM   2469 C  CA  . LEU A 1 376 ? 9.98800   -11.75200 8.53900   1.000 47.72489  ?  653  LEU B CA  1 
ATOM   2470 C  C   . LEU A 1 376 ? 8.92400   -12.84200 8.47700   1.000 47.98598  ?  653  LEU B C   1 
ATOM   2471 O  O   . LEU A 1 376 ? 8.43100   -13.18100 7.39400   1.000 46.06679  ?  653  LEU B O   1 
ATOM   2472 C  CB  . LEU A 1 376 ? 11.34900  -12.35000 8.87700   1.000 48.41306  ?  653  LEU B CB  1 
ATOM   2473 C  CG  . LEU A 1 376 ? 11.76400  -13.61400 8.13400   1.000 47.85534  ?  653  LEU B CG  1 
ATOM   2474 C  CD1 . LEU A 1 376 ? 12.18100  -13.26300 6.72300   1.000 51.12706  ?  653  LEU B CD1 1 
ATOM   2475 C  CD2 . LEU A 1 376 ? 12.91200  -14.27000 8.87700   1.000 50.52981  ?  653  LEU B CD2 1 
ATOM   2476 N  N   . MET A 1 377 ? 8.55800   -13.40500 9.63600   1.000 49.20279  ?  654  MET B N   1 
ATOM   2477 C  CA  . MET A 1 377 ? 7.55800   -14.46700 9.64100   1.000 48.44460  ?  654  MET B CA  1 
ATOM   2478 C  C   . MET A 1 377 ? 6.24500   -13.98600 9.04700   1.000 52.52803  ?  654  MET B C   1 
ATOM   2479 O  O   . MET A 1 377 ? 5.58700   -14.73000 8.30900   1.000 56.55503  ?  654  MET B O   1 
ATOM   2480 C  CB  . MET A 1 377 ? 7.34600   -14.99700 11.05000  1.000 49.21149  ?  654  MET B CB  1 
ATOM   2481 C  CG  . MET A 1 377 ? 8.50800   -15.84900 11.57400  1.000 51.27281  ?  654  MET B CG  1 
ATOM   2482 S  SD  . MET A 1 377 ? 8.30100   -16.16100 13.34100  1.000 57.39932  ?  654  MET B SD  1 
ATOM   2483 C  CE  . MET A 1 377 ? 9.64000   -17.31800 13.68000  1.000 44.51556  ?  654  MET B CE  1 
ATOM   2484 N  N   . ASP A 1 378 ? 5.86300   -12.72900 9.31800   1.000 44.39119  ?  655  ASP B N   1 
ATOM   2485 C  CA  . ASP A 1 378 ? 4.66600   -12.19000 8.68700   1.000 49.88927  ?  655  ASP B CA  1 
ATOM   2486 C  C   . ASP A 1 378 ? 4.79000   -12.20600 7.16100   1.000 56.84201  ?  655  ASP B C   1 
ATOM   2487 O  O   . ASP A 1 378 ? 3.84200   -12.59300 6.46400   1.000 55.58344  ?  655  ASP B O   1 
ATOM   2488 C  CB  . ASP A 1 378 ? 4.37600   -10.77900 9.18600   1.000 47.64327  ?  655  ASP B CB  1 
ATOM   2489 C  CG  . ASP A 1 378 ? 3.14900   -10.16600 8.50800   1.000 54.53372  ?  655  ASP B CG  1 
ATOM   2490 O  OD1 . ASP A 1 378 ? 2.07600   -10.80300 8.55100   1.000 55.89507  ?  655  ASP B OD1 1 
ATOM   2491 O  OD2 . ASP A 1 378 ? 3.25200   -9.06000  7.92200   1.000 58.87716  -1 655  ASP B OD2 1 
ATOM   2492 N  N   . LYS A 1 379 ? 5.95200   -11.80500 6.62400   1.000 53.65237  ?  656  LYS B N   1 
ATOM   2493 C  CA  . LYS A 1 379 ? 6.13500   -11.81700 5.17300   1.000 53.16734  ?  656  LYS B CA  1 
ATOM   2494 C  C   . LYS A 1 379 ? 6.15500   -13.23800 4.61100   1.000 55.49038  ?  656  LYS B C   1 
ATOM   2495 O  O   . LYS A 1 379 ? 5.55100   -13.49800 3.56300   1.000 59.69984  ?  656  LYS B O   1 
ATOM   2496 C  CB  . LYS A 1 379 ? 7.41500   -11.07300 4.78200   1.000 48.35184  ?  656  LYS B CB  1 
ATOM   2497 C  CG  . LYS A 1 379 ? 7.33100   -9.55200  4.94600   1.000 54.89149  ?  656  LYS B CG  1 
ATOM   2498 C  CD  . LYS A 1 379 ? 8.71900   -8.90900  5.01200   1.000 59.42422  ?  656  LYS B CD  1 
ATOM   2499 C  CE  . LYS A 1 379 ? 8.66900   -7.44000  5.44800   1.000 55.39261  ?  656  LYS B CE  1 
ATOM   2500 N  NZ  . LYS A 1 379 ? 8.18000   -6.54700  4.34700   1.000 70.85384  ?  656  LYS B NZ  1 
ATOM   2501 N  N   . LEU A 1 380 ? 6.85300   -14.17100 5.26900   1.000 56.19281  ?  657  LEU B N   1 
ATOM   2502 C  CA  . LEU A 1 380 ? 6.85500   -15.54800 4.77500   1.000 58.62379  ?  657  LEU B CA  1 
ATOM   2503 C  C   . LEU A 1 380 ? 5.42900   -16.07300 4.65100   1.000 59.66588  ?  657  LEU B C   1 
ATOM   2504 O  O   . LEU A 1 380 ? 5.05200   -16.65000 3.62400   1.000 62.21130  ?  657  LEU B O   1 
ATOM   2505 C  CB  . LEU A 1 380 ? 7.68400   -16.45000 5.69400   1.000 57.50120  ?  657  LEU B CB  1 
ATOM   2506 C  CG  . LEU A 1 380 ? 9.16800   -16.09800 5.80200   1.000 59.52083  ?  657  LEU B CG  1 
ATOM   2507 C  CD1 . LEU A 1 380 ? 9.89200   -16.94000 6.85700   1.000 50.91742  ?  657  LEU B CD1 1 
ATOM   2508 C  CD2 . LEU A 1 380 ? 9.82100   -16.25700 4.44600   1.000 60.91996  ?  657  LEU B CD2 1 
ATOM   2509 N  N   . LEU A 1 381 ? 4.61600   -15.85000 5.68700   1.000 57.48866  ?  658  LEU B N   1 
ATOM   2510 C  CA  . LEU A 1 381 ? 3.22600   -16.28700 5.66100   1.000 62.17283  ?  658  LEU B CA  1 
ATOM   2511 C  C   . LEU A 1 381 ? 2.45600   -15.61600 4.53300   1.000 63.63286  ?  658  LEU B C   1 
ATOM   2512 O  O   . LEU A 1 381 ? 1.63900   -16.25900 3.86000   1.000 57.13729  ?  658  LEU B O   1 
ATOM   2513 C  CB  . LEU A 1 381 ? 2.56500   -16.00000 7.00700   1.000 58.86462  ?  658  LEU B CB  1 
ATOM   2514 C  CG  . LEU A 1 381 ? 3.03200   -16.89500 8.16300   1.000 61.14268  ?  658  LEU B CG  1 
ATOM   2515 C  CD1 . LEU A 1 381 ? 2.68100   -16.27100 9.49300   1.000 53.47059  ?  658  LEU B CD1 1 
ATOM   2516 C  CD2 . LEU A 1 381 ? 2.38300   -18.26900 8.05000   1.000 58.68451  ?  658  LEU B CD2 1 
ATOM   2517 N  N   . ARG A 1 382 ? 2.69500   -14.32400 4.30700   1.000 60.67333  ?  659  ARG B N   1 
ATOM   2518 C  CA  . ARG A 1 382 ? 2.01500   -13.66200 3.20000   1.000 59.33080  ?  659  ARG B CA  1 
ATOM   2519 C  C   . ARG A 1 382 ? 2.48400   -14.21100 1.85900   1.000 67.93563  ?  659  ARG B C   1 
ATOM   2520 O  O   . ARG A 1 382 ? 1.66800   -14.42000 0.95700   1.000 72.96116  ?  659  ARG B O   1 
ATOM   2521 C  CB  . ARG A 1 382 ? 2.23100   -12.15800 3.25600   1.000 59.34285  ?  659  ARG B CB  1 
ATOM   2522 C  CG  . ARG A 1 382 ? 1.51300   -11.43400 4.37400   1.000 57.01197  ?  659  ARG B CG  1 
ATOM   2523 C  CD  . ARG A 1 382 ? 2.21200   -10.10100 4.52500   1.000 60.42901  ?  659  ARG B CD  1 
ATOM   2524 N  NE  . ARG A 1 382 ? 1.59400   -9.25300  5.52300   1.000 66.44281  ?  659  ARG B NE  1 
ATOM   2525 C  CZ  . ARG A 1 382 ? 0.58700   -8.42700  5.28000   1.000 74.60032  ?  659  ARG B CZ  1 
ATOM   2526 N  NH1 . ARG A 1 382 ? 0.03500   -8.34400  4.08200   1.000 72.76900  ?  659  ARG B NH1 1 
ATOM   2527 N  NH2 . ARG A 1 382 ? 0.12800   -7.65400  6.26400   1.000 73.71912  ?  659  ARG B NH2 1 
ATOM   2528 N  N   . LYS A 1 383 ? 3.79400   -14.45700 1.70100   1.000 65.83014  ?  660  LYS B N   1 
ATOM   2529 C  CA  . LYS A 1 383 ? 4.26400   -15.13100 0.48900   1.000 69.21800  ?  660  LYS B CA  1 
ATOM   2530 C  C   . LYS A 1 383 ? 3.46900   -16.40300 0.21600   1.000 70.58674  ?  660  LYS B C   1 
ATOM   2531 O  O   . LYS A 1 383 ? 3.30800   -16.80000 -0.94000  1.000 81.10856  ?  660  LYS B O   1 
ATOM   2532 C  CB  . LYS A 1 383 ? 5.76100   -15.47000 0.58700   1.000 68.65522  ?  660  LYS B CB  1 
ATOM   2533 C  CG  . LYS A 1 383 ? 6.69800   -14.45000 -0.04100  1.000 75.51714  ?  660  LYS B CG  1 
ATOM   2534 C  CD  . LYS A 1 383 ? 8.14500   -14.94400 -0.07700  1.000 75.13867  ?  660  LYS B CD  1 
ATOM   2535 N  N   . GLU A 1 384 ? 2.95500   -17.02800 1.28200   1.000 72.84111  ?  661  GLU B N   1 
ATOM   2536 C  CA  . GLU A 1 384 ? 2.19000   -18.29800 1.13900   1.000 74.31545  ?  661  GLU B CA  1 
ATOM   2537 C  C   . GLU A 1 384 ? 0.68700   -18.00400 1.13500   1.000 74.50723  ?  661  GLU B C   1 
ATOM   2538 O  O   . GLU A 1 384 ? -0.08600  -18.94100 1.40900   1.000 76.87707  ?  661  GLU B O   1 
ATOM   2539 C  CB  . GLU A 1 384 ? 2.54900   -19.27000 2.26500   1.000 77.26861  ?  661  GLU B CB  1 
ATOM   2540 C  CG  . GLU A 1 384 ? 4.04200   -19.46000 2.46600   1.000 81.28774  ?  661  GLU B CG  1 
ATOM   2541 C  CD  . GLU A 1 384 ? 4.79000   -20.13400 1.32800   1.000 96.41274  ?  661  GLU B CD  1 
ATOM   2542 O  OE1 . GLU A 1 384 ? 4.84300   -19.55700 0.22400   1.000 95.81629  ?  661  GLU B OE1 1 
ATOM   2543 O  OE2 . GLU A 1 384 ? 5.32000   -21.24100 1.55000   1.000 105.69517 -1 661  GLU B OE2 1 
ATOM   2544 N  N   . ASN A 1 385 ? 0.29400   -16.75600 0.86400   1.000 75.29699  ?  662  ASN B N   1 
ATOM   2545 C  CA  . ASN A 1 385 ? -1.11800  -16.38800 0.76200   1.000 78.72095  ?  662  ASN B CA  1 
ATOM   2546 C  C   . ASN A 1 385 ? -1.85300  -16.61100 2.08400   1.000 76.51109  ?  662  ASN B C   1 
ATOM   2547 O  O   . ASN A 1 385 ? -3.01100  -17.03100 2.11000   1.000 83.10954  ?  662  ASN B O   1 
ATOM   2548 C  CB  . ASN A 1 385 ? -1.79900  -17.14400 -0.38000  1.000 87.79255  ?  662  ASN B CB  1 
ATOM   2549 C  CG  . ASN A 1 385 ? -3.08200  -16.47200 -0.83500  1.000 98.23154  ?  662  ASN B CG  1 
ATOM   2550 O  OD1 . ASN A 1 385 ? -3.07000  -15.30500 -1.23500  1.000 101.91451 ?  662  ASN B OD1 1 
ATOM   2551 N  ND2 . ASN A 1 385 ? -4.19400  -17.20800 -0.79100  1.000 104.21909 ?  662  ASN B ND2 1 
ATOM   2552 N  N   . LEU A 1 386 ? -1.17600  -16.31700 3.19000   1.000 74.75042  ?  663  LEU B N   1 
ATOM   2553 C  CA  . LEU A 1 386 ? -1.73400  -16.45800 4.53400   1.000 65.93464  ?  663  LEU B CA  1 
ATOM   2554 C  C   . LEU A 1 386 ? -1.43000  -15.16200 5.27600   1.000 58.87846  ?  663  LEU B C   1 
ATOM   2555 O  O   . LEU A 1 386 ? -0.29600  -14.93500 5.70600   1.000 65.35846  ?  663  LEU B O   1 
ATOM   2556 C  CB  . LEU A 1 386 ? -1.15200  -17.67600 5.24800   1.000 67.41274  ?  663  LEU B CB  1 
ATOM   2557 C  CG  . LEU A 1 386 ? -1.84200  -18.18400 6.52100   1.000 73.58020  ?  663  LEU B CG  1 
ATOM   2558 C  CD1 . LEU A 1 386 ? -3.30300  -18.58700 6.28000   1.000 64.37906  ?  663  LEU B CD1 1 
ATOM   2559 C  CD2 . LEU A 1 386 ? -1.05700  -19.35800 7.09500   1.000 71.28811  ?  663  LEU B CD2 1 
ATOM   2560 N  N   . ASP A 1 387 ? -2.43600  -14.30300 5.40800   1.000 61.95729  ?  664  ASP B N   1 
ATOM   2561 C  CA  . ASP A 1 387 ? -2.29500  -13.00500 6.07000   1.000 60.40005  ?  664  ASP B CA  1 
ATOM   2562 C  C   . ASP A 1 387 ? -3.04900  -13.10000 7.39300   1.000 62.47215  ?  664  ASP B C   1 
ATOM   2563 O  O   . ASP A 1 387 ? -4.28300  -13.04100 7.42400   1.000 67.12937  ?  664  ASP B O   1 
ATOM   2564 C  CB  . ASP A 1 387 ? -2.81300  -11.87300 5.17900   1.000 54.36770  ?  664  ASP B CB  1 
ATOM   2565 C  CG  . ASP A 1 387 ? -3.04400  -10.56600 5.94400   1.000 62.51369  ?  664  ASP B CG  1 
ATOM   2566 O  OD1 . ASP A 1 387 ? -2.44600  -10.34900 7.02600   1.000 56.34055  ?  664  ASP B OD1 1 
ATOM   2567 O  OD2 . ASP A 1 387 ? -3.85100  -9.75100  5.45500   1.000 67.04276  -1 664  ASP B OD2 1 
ATOM   2568 N  N   . LEU A 1 388 ? -2.30600  -13.25900 8.48500   1.000 55.74758  ?  665  LEU B N   1 
ATOM   2569 C  CA  . LEU A 1 388 ? -2.89900  -13.45900 9.79600   1.000 59.29309  ?  665  LEU B CA  1 
ATOM   2570 C  C   . LEU A 1 388 ? -3.08600  -12.15500 10.56200  1.000 59.59276  ?  665  LEU B C   1 
ATOM   2571 O  O   . LEU A 1 388 ? -3.27600  -12.19000 11.77900  1.000 60.32007  ?  665  LEU B O   1 
ATOM   2572 C  CB  . LEU A 1 388 ? -2.05600  -14.45100 10.60200  1.000 56.66172  ?  665  LEU B CB  1 
ATOM   2573 C  CG  . LEU A 1 388 ? -2.06000  -15.84500 9.94800   1.000 64.12387  ?  665  LEU B CG  1 
ATOM   2574 C  CD1 . LEU A 1 388 ? -1.25800  -16.84100 10.76700  1.000 56.90124  ?  665  LEU B CD1 1 
ATOM   2575 C  CD2 . LEU A 1 388 ? -3.48300  -16.37900 9.67700   1.000 55.03049  ?  665  LEU B CD2 1 
ATOM   2576 N  N   . LYS A 1 389 ? -3.04100  -11.01100 9.87700   1.000 57.96772  ?  666  LYS B N   1 
ATOM   2577 C  CA  . LYS A 1 389 ? -3.35700  -9.71700  10.48500  1.000 54.42787  ?  666  LYS B CA  1 
ATOM   2578 C  C   . LYS A 1 389 ? -2.43900  -9.40200  11.67000  1.000 56.43283  ?  666  LYS B C   1 
ATOM   2579 O  O   . LYS A 1 389 ? -2.88700  -8.91100  12.71200  1.000 53.20724  ?  666  LYS B O   1 
ATOM   2580 C  CB  . LYS A 1 389 ? -4.82900  -9.65700  10.91500  1.000 58.94721  ?  666  LYS B CB  1 
ATOM   2581 C  CG  . LYS A 1 389 ? -5.80600  -10.06800 9.82700   1.000 62.05186  ?  666  LYS B CG  1 
ATOM   2582 C  CD  . LYS A 1 389 ? -5.71100  -9.16400  8.60100   1.000 58.15550  ?  666  LYS B CD  1 
ATOM   2583 C  CE  . LYS A 1 389 ? -6.47900  -9.77400  7.43500   1.000 67.96301  ?  666  LYS B CE  1 
ATOM   2584 N  NZ  . LYS A 1 389 ? -6.54700  -8.92000  6.22100   1.000 65.44917  ?  666  LYS B NZ  1 
ATOM   2585 N  N   . LEU A 1 390 ? -1.14800  -9.69000  11.49800  1.000 48.91818  ?  667  LEU B N   1 
ATOM   2586 C  CA  . LEU A 1 390 ? -0.16700  -9.46200  12.59100  1.000 47.29992  ?  667  LEU B CA  1 
ATOM   2587 C  C   . LEU A 1 390 ? 0.17800   -7.97200  12.67000  1.000 47.82559  ?  667  LEU B C   1 
ATOM   2588 O  O   . LEU A 1 390 ? -0.15100  -7.23600  11.72100  1.000 44.97650  ?  667  LEU B O   1 
ATOM   2589 C  CB  . LEU A 1 390 ? 1.07900   -10.30200 12.29800  1.000 46.26895  ?  667  LEU B CB  1 
ATOM   2590 C  CG  . LEU A 1 390 ? 0.81100   -11.77500 11.99500  1.000 51.08121  ?  667  LEU B CG  1 
ATOM   2591 C  CD1 . LEU A 1 390 ? 2.11300   -12.54800 11.86300  1.000 48.51943  ?  667  LEU B CD1 1 
ATOM   2592 C  CD2 . LEU A 1 390 ? -0.07200  -12.39600 13.06700  1.000 50.49358  ?  667  LEU B CD2 1 
ATOM   2593 N  N   . THR A 1 391 ? 0.81700   -7.55400  13.76400  1.000 43.97847  ?  668  THR B N   1 
ATOM   2594 C  CA  . THR A 1 391 ? 1.22300   -6.13400  13.93200  1.000 42.70682  ?  668  THR B CA  1 
ATOM   2595 C  C   . THR A 1 391 ? 2.73400   -6.08500  14.17900  1.000 46.41213  ?  668  THR B C   1 
ATOM   2596 O  O   . THR A 1 391 ? 3.13800   -5.87900  15.33900  1.000 41.98546  ?  668  THR B O   1 
ATOM   2597 C  CB  . THR A 1 391 ? 0.41600   -5.45500  15.04600  1.000 44.26598  ?  668  THR B CB  1 
ATOM   2598 O  OG1 . THR A 1 391 ? -0.96400  -5.49400  14.68400  1.000 47.48809  ?  668  THR B OG1 1 
ATOM   2599 C  CG2 . THR A 1 391 ? 0.83100   -4.02000  15.29000  1.000 38.20741  ?  668  THR B CG2 1 
ATOM   2600 N  N   . PRO A 1 392 ? 3.58100   -6.28800  13.14800  1.000 40.09535  ?  669  PRO B N   1 
ATOM   2601 C  CA  . PRO A 1 392 ? 5.03000   -6.17500  13.31000  1.000 48.51377  ?  669  PRO B CA  1 
ATOM   2602 C  C   . PRO A 1 392 ? 5.43000   -4.69400  13.34300  1.000 46.76637  ?  669  PRO B C   1 
ATOM   2603 O  O   . PRO A 1 392 ? 5.92000   -4.19900  12.34800  1.000 44.12939  ?  669  PRO B O   1 
ATOM   2604 C  CB  . PRO A 1 392 ? 5.57400   -6.87000  12.05600  1.000 44.75350  ?  669  PRO B CB  1 
ATOM   2605 C  CG  . PRO A 1 392 ? 4.49900   -6.64700  11.01500  1.000 45.13737  ?  669  PRO B CG  1 
ATOM   2606 C  CD  . PRO A 1 392 ? 3.19400   -6.65500  11.78400  1.000 47.78233  ?  669  PRO B CD  1 
ATOM   2607 N  N   . TYR A 1 393 ? 5.20800   -4.03100  14.48100  1.000 40.72014  ?  670  TYR B N   1 
ATOM   2608 C  CA  . TYR A 1 393 ? 5.51700   -2.58200  14.60300  1.000 43.29381  ?  670  TYR B CA  1 
ATOM   2609 C  C   . TYR A 1 393 ? 7.03000   -2.36800  14.50000  1.000 43.96755  ?  670  TYR B C   1 
ATOM   2610 O  O   . TYR A 1 393 ? 7.79600   -3.23600  14.95800  1.000 41.47785  ?  670  TYR B O   1 
ATOM   2611 C  CB  . TYR A 1 393 ? 4.91300   -2.01400  15.89200  1.000 36.00250  ?  670  TYR B CB  1 
ATOM   2612 C  CG  . TYR A 1 393 ? 5.28300   -2.73500  17.16300  1.000 40.06082  ?  670  TYR B CG  1 
ATOM   2613 C  CD1 . TYR A 1 393 ? 6.55000   -2.62800  17.71000  1.000 41.52489  ?  670  TYR B CD1 1 
ATOM   2614 C  CD2 . TYR A 1 393 ? 4.36300   -3.53800  17.81700  1.000 40.03663  ?  670  TYR B CD2 1 
ATOM   2615 C  CE1 . TYR A 1 393 ? 6.89200   -3.28900  18.87800  1.000 41.25099  ?  670  TYR B CE1 1 
ATOM   2616 C  CE2 . TYR A 1 393 ? 4.68800   -4.21000  18.98300  1.000 40.40773  ?  670  TYR B CE2 1 
ATOM   2617 C  CZ  . TYR A 1 393 ? 5.95800   -4.08400  19.51600  1.000 39.24925  ?  670  TYR B CZ  1 
ATOM   2618 O  OH  . TYR A 1 393 ? 6.28500   -4.74800  20.67200  1.000 43.62536  ?  670  TYR B OH  1 
ATOM   2619 N  N   . LYS A 1 394 ? 7.44000   -1.24300  13.91100  1.000 37.79569  ?  671  LYS B N   1 
ATOM   2620 C  CA  . LYS A 1 394 ? 8.86100   -0.96000  13.73800  1.000 40.02429  ?  671  LYS B CA  1 
ATOM   2621 C  C   . LYS A 1 394 ? 9.54800   -0.73400  15.08900  1.000 40.21274  ?  671  LYS B C   1 
ATOM   2622 O  O   . LYS A 1 394 ? 8.99600   -0.08500  15.98500  1.000 35.60327  ?  671  LYS B O   1 
ATOM   2623 C  CB  . LYS A 1 394 ? 9.05400   0.26000   12.85000  1.000 41.83807  ?  671  LYS B CB  1 
ATOM   2624 C  CG  . LYS A 1 394 ? 8.57300   0.06900   11.41300  1.000 46.67954  ?  671  LYS B CG  1 
ATOM   2625 C  CD  . LYS A 1 394 ? 9.18500   -1.18700  10.86000  1.000 52.40576  ?  671  LYS B CD  1 
ATOM   2626 C  CE  . LYS A 1 394 ? 9.47200   -1.02800  9.38700   1.000 60.47895  ?  671  LYS B CE  1 
ATOM   2627 N  NZ  . LYS A 1 394 ? 8.19800   -0.60700  8.75400   1.000 67.46330  ?  671  LYS B NZ  1 
ATOM   2628 N  N   . VAL A 1 395 ? 10.75300  -1.27800  15.23100  1.000 39.25055  ?  672  VAL B N   1 
ATOM   2629 C  CA  . VAL A 1 395 ? 11.63900  -0.96700  16.34500  1.000 34.65800  ?  672  VAL B CA  1 
ATOM   2630 C  C   . VAL A 1 395 ? 13.01700  -0.67000  15.77800  1.000 40.82032  ?  672  VAL B C   1 
ATOM   2631 O  O   . VAL A 1 395 ? 13.54800  -1.46200  14.99300  1.000 41.43733  ?  672  VAL B O   1 
ATOM   2632 C  CB  . VAL A 1 395 ? 11.73100  -2.12200  17.35900  1.000 37.26105  ?  672  VAL B CB  1 
ATOM   2633 C  CG1 . VAL A 1 395 ? 12.78000  -1.79800  18.47700  1.000 35.89632  ?  672  VAL B CG1 1 
ATOM   2634 C  CG2 . VAL A 1 395 ? 10.35500  -2.43600  17.92400  1.000 36.27400  ?  672  VAL B CG2 1 
ATOM   2635 N  N   . LEU A 1 396 ? 13.60600  0.45100   16.18700  1.000 41.63083  ?  673  LEU B N   1 
ATOM   2636 C  CA  . LEU A 1 396 ? 14.96000  0.79700   15.76100  1.000 40.24719  ?  673  LEU B CA  1 
ATOM   2637 C  C   . LEU A 1 396 ? 15.72800  1.34300   16.95700  1.000 40.66947  ?  673  LEU B C   1 
ATOM   2638 O  O   . LEU A 1 396 ? 15.35500  2.38300   17.51600  1.000 36.80534  ?  673  LEU B O   1 
ATOM   2639 C  CB  . LEU A 1 396 ? 14.95400  1.83100   14.63200  1.000 38.79921  ?  673  LEU B CB  1 
ATOM   2640 C  CG  . LEU A 1 396 ? 16.37200  2.27600   14.23000  1.000 45.36214  ?  673  LEU B CG  1 
ATOM   2641 C  CD1 . LEU A 1 396 ? 17.04600  1.22300   13.38700  1.000 42.13566  ?  673  LEU B CD1 1 
ATOM   2642 C  CD2 . LEU A 1 396 ? 16.36000  3.58700   13.48400  1.000 40.03930  ?  673  LEU B CD2 1 
ATOM   2643 N  N   . ALA A 1 397 ? 16.80300  0.64900   17.33000  1.000 37.97981  ?  674  ALA B N   1 
ATOM   2644 C  CA  . ALA A 1 397 ? 17.76000  1.15000   18.31200  1.000 36.93290  ?  674  ALA B CA  1 
ATOM   2645 C  C   . ALA A 1 397 ? 18.65500  2.20700   17.66200  1.000 38.56292  ?  674  ALA B C   1 
ATOM   2646 O  O   . ALA A 1 397 ? 19.27600  1.95100   16.62500  1.000 40.42268  ?  674  ALA B O   1 
ATOM   2647 C  CB  . ALA A 1 397 ? 18.60500  -0.00500  18.85400  1.000 34.98697  ?  674  ALA B CB  1 
ATOM   2648 N  N   . THR A 1 398 ? 18.70200  3.40200   18.24300  1.000 37.35450  ?  675  THR B N   1 
ATOM   2649 C  CA  . THR A 1 398 ? 19.58900  4.45200   17.74700  1.000 40.05495  ?  675  THR B CA  1 
ATOM   2650 C  C   . THR A 1 398 ? 20.84300  4.56400   18.60000  1.000 41.87361  ?  675  THR B C   1 
ATOM   2651 O  O   . THR A 1 398 ? 21.71800  5.38800   18.32400  1.000 42.88322  ?  675  THR B O   1 
ATOM   2652 C  CB  . THR A 1 398 ? 18.84700  5.79700   17.67000  1.000 42.76929  ?  675  THR B CB  1 
ATOM   2653 O  OG1 . THR A 1 398 ? 18.09900  6.01600   18.87500  1.000 44.44581  ?  675  THR B OG1 1 
ATOM   2654 C  CG2 . THR A 1 398 ? 17.86900  5.81900   16.45200  1.000 36.20206  ?  675  THR B CG2 1 
ATOM   2655 N  N   . SER A 1 399 ? 20.95700  3.69800   19.59600  1.000 44.85457  ?  676  SER B N   1 
ATOM   2656 C  CA  . SER A 1 399 ? 22.08200  3.58500   20.50900  1.000 45.08299  ?  676  SER B CA  1 
ATOM   2657 C  C   . SER A 1 399 ? 21.85000  2.31400   21.31800  1.000 47.55410  ?  676  SER B C   1 
ATOM   2658 O  O   . SER A 1 399 ? 20.77300  1.70900   21.26100  1.000 44.65652  ?  676  SER B O   1 
ATOM   2659 C  CB  . SER A 1 399 ? 22.18300  4.80500   21.42400  1.000 44.84883  ?  676  SER B CB  1 
ATOM   2660 O  OG  . SER A 1 399 ? 23.28700  4.64700   22.27000  1.000 57.96278  ?  676  SER B OG  1 
ATOM   2661 N  N   . THR A 1 400 ? 22.86100  1.91600   22.08100  1.000 47.71573  ?  677  THR B N   1 
ATOM   2662 C  CA  . THR A 1 400 ? 22.57000  0.87700   23.05900  1.000 51.54798  ?  677  THR B CA  1 
ATOM   2663 C  C   . THR A 1 400 ? 21.70800  1.40600   24.19800  1.000 49.36896  ?  677  THR B C   1 
ATOM   2664 O  O   . THR A 1 400 ? 21.24900  0.60900   25.02100  1.000 43.78764  ?  677  THR B O   1 
ATOM   2665 C  CB  . THR A 1 400 ? 23.85800  0.25500   23.62200  1.000 46.87471  ?  677  THR B CB  1 
ATOM   2666 O  OG1 . THR A 1 400 ? 24.61600  1.25400   24.30000  1.000 52.89311  ?  677  THR B OG1 1 
ATOM   2667 C  CG2 . THR A 1 400 ? 24.72400  -0.34900  22.49900  1.000 49.86914  ?  677  THR B CG2 1 
ATOM   2668 N  N   . LYS A 1 401 ? 21.45000  2.72000   24.23300  1.000 47.27807  ?  678  LYS B N   1 
ATOM   2669 C  CA  . LYS A 1 401 ? 20.75900  3.36800   25.33700  1.000 45.73998  ?  678  LYS B CA  1 
ATOM   2670 C  C   . LYS A 1 401 ? 19.48600  4.11100   24.93600  1.000 47.51019  ?  678  LYS B C   1 
ATOM   2671 O  O   . LYS A 1 401 ? 18.84300  4.70400   25.81100  1.000 44.68162  ?  678  LYS B O   1 
ATOM   2672 C  CB  . LYS A 1 401 ? 21.70900  4.34800   26.04900  1.000 49.47556  ?  678  LYS B CB  1 
ATOM   2673 C  CG  . LYS A 1 401 ? 22.99100  3.70500   26.60500  1.000 55.33848  ?  678  LYS B CG  1 
ATOM   2674 C  CD  . LYS A 1 401 ? 24.12200  4.74300   26.76900  1.000 71.68489  ?  678  LYS B CD  1 
ATOM   2675 C  CE  . LYS A 1 401 ? 25.50000  4.11900   27.12700  1.000 62.11660  ?  678  LYS B CE  1 
ATOM   2676 N  N   . HIS A 1 402 ? 19.09500  4.10700   23.65600  1.000 40.56732  ?  679  HIS B N   1 
ATOM   2677 C  CA  . HIS A 1 402 ? 17.85300  4.77800   23.26900  1.000 39.12411  ?  679  HIS B CA  1 
ATOM   2678 C  C   . HIS A 1 402 ? 17.40700  4.27200   21.90700  1.000 39.40617  ?  679  HIS B C   1 
ATOM   2679 O  O   . HIS A 1 402 ? 18.17600  3.65500   21.16600  1.000 39.81520  ?  679  HIS B O   1 
ATOM   2680 C  CB  . HIS A 1 402 ? 17.97400  6.31700   23.26900  1.000 41.27298  ?  679  HIS B CB  1 
ATOM   2681 C  CG  . HIS A 1 402 ? 19.18300  6.86600   22.56500  1.000 42.30691  ?  679  HIS B CG  1 
ATOM   2682 N  ND1 . HIS A 1 402 ? 19.31700  6.86200   21.18700  1.000 48.02828  ?  679  HIS B ND1 1 
ATOM   2683 C  CD2 . HIS A 1 402 ? 20.28700  7.49500   23.04300  1.000 48.70450  ?  679  HIS B CD2 1 
ATOM   2684 C  CE1 . HIS A 1 402 ? 20.46200  7.43100   20.84800  1.000 39.61744  ?  679  HIS B CE1 1 
ATOM   2685 N  NE2 . HIS A 1 402 ? 21.06800  7.82600   21.95300  1.000 47.71906  ?  679  HIS B NE2 1 
ATOM   2686 N  N   . GLY A 1 403 ? 16.15300  4.54900   21.58200  1.000 37.61197  ?  680  GLY B N   1 
ATOM   2687 C  CA  . GLY A 1 403 ? 15.63400  4.12200   20.30000  1.000 37.69284  ?  680  GLY B CA  1 
ATOM   2688 C  C   . GLY A 1 403 ? 14.16600  4.46200   20.14900  1.000 39.44734  ?  680  GLY B C   1 
ATOM   2689 O  O   . GLY A 1 403 ? 13.52400  5.02000   21.05000  1.000 41.00537  ?  680  GLY B O   1 
ATOM   2690 N  N   . PHE A 1 404 ? 13.64700  4.09300   18.98600  1.000 37.00554  ?  681  PHE B N   1 
ATOM   2691 C  CA  . PHE A 1 404 ? 12.30600  4.40300   18.53900  1.000 36.93996  ?  681  PHE B CA  1 
ATOM   2692 C  C   . PHE A 1 404 ? 11.48300  3.13600   18.42100  1.000 37.86491  ?  681  PHE B C   1 
ATOM   2693 O  O   . PHE A 1 404 ? 11.99400  2.06700   18.07700  1.000 36.60065  ?  681  PHE B O   1 
ATOM   2694 C  CB  . PHE A 1 404 ? 12.32100  5.06300   17.14900  1.000 40.02961  ?  681  PHE B CB  1 
ATOM   2695 C  CG  . PHE A 1 404 ? 12.84600  6.45300   17.13100  1.000 41.68296  ?  681  PHE B CG  1 
ATOM   2696 C  CD1 . PHE A 1 404 ? 12.00900  7.52100   17.40900  1.000 46.13000  ?  681  PHE B CD1 1 
ATOM   2697 C  CD2 . PHE A 1 404 ? 14.16700  6.70400   16.78800  1.000 41.76012  ?  681  PHE B CD2 1 
ATOM   2698 C  CE1 . PHE A 1 404 ? 12.49300  8.83100   17.36600  1.000 47.44255  ?  681  PHE B CE1 1 
ATOM   2699 C  CE2 . PHE A 1 404 ? 14.65500  8.00400   16.72900  1.000 47.39688  ?  681  PHE B CE2 1 
ATOM   2700 C  CZ  . PHE A 1 404 ? 13.82000  9.06400   17.01800  1.000 45.96732  ?  681  PHE B CZ  1 
ATOM   2701 N  N   . MET A 1 405 ? 10.19100  3.29800   18.62500  1.000 42.02817  ?  682  MET B N   1 
ATOM   2702 C  CA  . MET A 1 405 ? 9.21200   2.28200   18.29000  1.000 42.33343  ?  682  MET B CA  1 
ATOM   2703 C  C   . MET A 1 405 ? 8.03700   2.97700   17.63700  1.000 38.83924  ?  682  MET B C   1 
ATOM   2704 O  O   . MET A 1 405 ? 7.65400   4.07300   18.04200  1.000 38.10966  ?  682  MET B O   1 
ATOM   2705 C  CB  . MET A 1 405 ? 8.71200   1.50600   19.51600  1.000 38.33159  ?  682  MET B CB  1 
ATOM   2706 C  CG  . MET A 1 405 ? 9.75800   0.64400   20.16100  1.000 47.13474  ?  682  MET B CG  1 
ATOM   2707 S  SD  . MET A 1 405 ? 9.03600   -0.19500  21.58700  1.000 51.02548  ?  682  MET B SD  1 
ATOM   2708 C  CE  . MET A 1 405 ? 10.41500  -1.26000  21.98600  1.000 45.85009  ?  682  MET B CE  1 
ATOM   2709 N  N   . GLN A 1 406 ? 7.48900   2.33600   16.62000  1.000 39.50649  ?  683  GLN B N   1 
ATOM   2710 C  CA  . GLN A 1 406 ? 6.26700   2.80400   16.00100  1.000 42.85078  ?  683  GLN B CA  1 
ATOM   2711 C  C   . GLN A 1 406 ? 5.10100   2.63700   16.96700  1.000 43.50765  ?  683  GLN B C   1 
ATOM   2712 O  O   . GLN A 1 406 ? 4.87200   1.54100   17.47000  1.000 40.43518  ?  683  GLN B O   1 
ATOM   2713 C  CB  . GLN A 1 406 ? 6.03200   1.99700   14.73400  1.000 42.22465  ?  683  GLN B CB  1 
ATOM   2714 C  CG  . GLN A 1 406 ? 4.75800   2.30000   14.01200  1.000 38.11029  ?  683  GLN B CG  1 
ATOM   2715 C  CD  . GLN A 1 406 ? 4.62000   1.40100   12.81200  1.000 47.51183  ?  683  GLN B CD  1 
ATOM   2716 O  OE1 . GLN A 1 406 ? 5.32000   0.37400   12.69000  1.000 44.26943  ?  683  GLN B OE1 1 
ATOM   2717 N  NE2 . GLN A 1 406 ? 3.72500   1.76600   11.91300  1.000 44.18749  ?  683  GLN B NE2 1 
ATOM   2718 N  N   . PHE A 1 407 ? 4.36700   3.72400   17.22100  1.000 45.65140  ?  684  PHE B N   1 
ATOM   2719 C  CA  . PHE A 1 407 ? 3.19100   3.65100   18.12700  1.000 41.14434  ?  684  PHE B CA  1 
ATOM   2720 C  C   . PHE A 1 407 ? 1.97600   3.11200   17.36700  1.000 44.17066  ?  684  PHE B C   1 
ATOM   2721 O  O   . PHE A 1 407 ? 1.65200   3.65100   16.29700  1.000 48.15194  ?  684  PHE B O   1 
ATOM   2722 C  CB  . PHE A 1 407 ? 2.85300   5.01700   18.72500  1.000 41.52984  ?  684  PHE B CB  1 
ATOM   2723 C  CG  . PHE A 1 407 ? 1.66200   4.98700   19.65000  1.000 42.64445  ?  684  PHE B CG  1 
ATOM   2724 C  CD1 . PHE A 1 407 ? 1.72300   4.31600   20.86000  1.000 45.75014  ?  684  PHE B CD1 1 
ATOM   2725 C  CD2 . PHE A 1 407 ? 0.46600   5.58700   19.29100  1.000 44.57510  ?  684  PHE B CD2 1 
ATOM   2726 C  CE1 . PHE A 1 407 ? 0.62600   4.27300   21.70500  1.000 53.63235  ?  684  PHE B CE1 1 
ATOM   2727 C  CE2 . PHE A 1 407 ? -0.63200  5.54100   20.13500  1.000 49.92340  ?  684  PHE B CE2 1 
ATOM   2728 C  CZ  . PHE A 1 407 ? -0.55000  4.88600   21.34100  1.000 46.35147  ?  684  PHE B CZ  1 
ATOM   2729 N  N   . ILE A 1 408 ? 1.32100   2.08800   17.91500  1.000 44.48858  ?  685  ILE B N   1 
ATOM   2730 C  CA  . ILE A 1 408 ? 0.09100   1.53100   17.27800  1.000 46.98931  ?  685  ILE B CA  1 
ATOM   2731 C  C   . ILE A 1 408 ? -1.10700  1.87600   18.16700  1.000 45.52051  ?  685  ILE B C   1 
ATOM   2732 O  O   . ILE A 1 408 ? -1.04800  1.56500   19.36900  1.000 47.57931  ?  685  ILE B O   1 
ATOM   2733 C  CB  . ILE A 1 408 ? 0.22400   0.00900   17.06800  1.000 46.96421  ?  685  ILE B CB  1 
ATOM   2734 C  CG1 . ILE A 1 408 ? 1.50900   -0.35400  16.31900  1.000 47.06159  ?  685  ILE B CG1 1 
ATOM   2735 C  CG2 . ILE A 1 408 ? -1.01100  -0.54900  16.37800  1.000 45.46929  ?  685  ILE B CG2 1 
ATOM   2736 C  CD1 . ILE A 1 408 ? 1.64000   0.30300   14.96600  1.000 44.10802  ?  685  ILE B CD1 1 
ATOM   2737 N  N   . GLN A 1 409 ? -2.13800  2.51100   17.60100  1.000 49.21306  ?  686  GLN B N   1 
ATOM   2738 C  CA  . GLN A 1 409 ? -3.36800  2.79400   18.38800  1.000 51.97783  ?  686  GLN B CA  1 
ATOM   2739 C  C   . GLN A 1 409 ? -3.91000  1.45700   18.89200  1.000 57.07948  ?  686  GLN B C   1 
ATOM   2740 O  O   . GLN A 1 409 ? -4.13500  0.56700   18.05400  1.000 52.22929  ?  686  GLN B O   1 
ATOM   2741 C  CB  . GLN A 1 409 ? -4.40100  3.54700   17.54900  1.000 58.27524  ?  686  GLN B CB  1 
ATOM   2742 C  CG  . GLN A 1 409 ? -5.60200  4.00600   18.36000  1.000 75.82866  ?  686  GLN B CG  1 
ATOM   2743 C  CD  . GLN A 1 409 ? -5.17200  4.77400   19.58700  1.000 84.52271  ?  686  GLN B CD  1 
ATOM   2744 O  OE1 . GLN A 1 409 ? -5.44700  4.38000   20.71800  1.000 82.86072  ?  686  GLN B OE1 1 
ATOM   2745 N  NE2 . GLN A 1 409 ? -4.47700  5.87800   19.36900  1.000 70.53521  ?  686  GLN B NE2 1 
ATOM   2746 N  N   . SER A 1 410 ? -4.11700  1.32300   20.20300  1.000 49.36665  ?  687  SER B N   1 
ATOM   2747 C  CA  . SER A 1 410 ? -4.51000  0.02400   20.74700  1.000 49.01557  ?  687  SER B CA  1 
ATOM   2748 C  C   . SER A 1 410 ? -4.80500  0.17600   22.23700  1.000 53.53286  ?  687  SER B C   1 
ATOM   2749 O  O   . SER A 1 410 ? -4.55000  1.22200   22.83500  1.000 49.28985  ?  687  SER B O   1 
ATOM   2750 C  CB  . SER A 1 410 ? -3.40400  -1.00700  20.52400  1.000 45.62488  ?  687  SER B CB  1 
ATOM   2751 O  OG  . SER A 1 410 ? -2.15400  -0.49200  20.99100  1.000 44.84790  ?  687  SER B OG  1 
ATOM   2752 N  N   . VAL A 1 411 ? -5.32900  -0.88800  22.83800  1.000 46.35231  ?  688  VAL B N   1 
ATOM   2753 C  CA  . VAL A 1 411 ? -5.61300  -0.87300  24.27400  1.000 47.93248  ?  688  VAL B CA  1 
ATOM   2754 C  C   . VAL A 1 411 ? -5.22400  -2.21900  24.87900  1.000 43.41018  ?  688  VAL B C   1 
ATOM   2755 O  O   . VAL A 1 411 ? -5.49900  -3.27000  24.28400  1.000 44.81578  ?  688  VAL B O   1 
ATOM   2756 C  CB  . VAL A 1 411 ? -7.08900  -0.52100  24.54200  1.000 46.07377  ?  688  VAL B CB  1 
ATOM   2757 C  CG1 . VAL A 1 411 ? -7.98600  -1.34200  23.66500  1.000 48.60249  ?  688  VAL B CG1 1 
ATOM   2758 C  CG2 . VAL A 1 411 ? -7.42700  -0.76600  25.97300  1.000 47.60982  ?  688  VAL B CG2 1 
ATOM   2759 N  N   . PRO A 1 412 ? -4.53800  -2.24300  26.01800  1.000 44.56191  ?  689  PRO B N   1 
ATOM   2760 C  CA  . PRO A 1 412 ? -4.14400  -3.53200  26.61000  1.000 44.56884  ?  689  PRO B CA  1 
ATOM   2761 C  C   . PRO A 1 412 ? -5.37700  -4.33200  27.01500  1.000 48.72375  ?  689  PRO B C   1 
ATOM   2762 O  O   . PRO A 1 412 ? -6.39800  -3.77000  27.42500  1.000 48.93724  ?  689  PRO B O   1 
ATOM   2763 C  CB  . PRO A 1 412 ? -3.30200  -3.13500  27.83200  1.000 41.91193  ?  689  PRO B CB  1 
ATOM   2764 C  CG  . PRO A 1 412 ? -2.98300  -1.68900  27.65500  1.000 43.14862  ?  689  PRO B CG  1 
ATOM   2765 C  CD  . PRO A 1 412 ? -4.08300  -1.09600  26.82000  1.000 46.99174  ?  689  PRO B CD  1 
ATOM   2766 N  N   . VAL A 1 413 ? -5.28200  -5.65700  26.88200  1.000 42.34367  ?  690  VAL B N   1 
ATOM   2767 C  CA  . VAL A 1 413 ? -6.40900  -6.49700  27.24900  1.000 48.96274  ?  690  VAL B CA  1 
ATOM   2768 C  C   . VAL A 1 413 ? -6.78000  -6.28400  28.70600  1.000 50.56934  ?  690  VAL B C   1 
ATOM   2769 O  O   . VAL A 1 413 ? -7.96500  -6.32300  29.06200  1.000 48.41948  ?  690  VAL B O   1 
ATOM   2770 C  CB  . VAL A 1 413 ? -6.11700  -7.97700  26.96600  1.000 52.76542  ?  690  VAL B CB  1 
ATOM   2771 C  CG1 . VAL A 1 413 ? -7.17300  -8.84100  27.64200  1.000 46.44295  ?  690  VAL B CG1 1 
ATOM   2772 C  CG2 . VAL A 1 413 ? -6.08700  -8.23000  25.47400  1.000 46.65678  ?  690  VAL B CG2 1 
ATOM   2773 N  N   . ALA A 1 414 ? -5.79100  -6.03000  29.56700  1.000 47.92792  ?  691  ALA B N   1 
ATOM   2774 C  CA  . ALA A 1 414 ? -6.10200  -5.80600  30.97800  1.000 51.30361  ?  691  ALA B CA  1 
ATOM   2775 C  C   . ALA A 1 414 ? -7.05500  -4.62900  31.14800  1.000 51.13779  ?  691  ALA B C   1 
ATOM   2776 O  O   . ALA A 1 414 ? -7.95500  -4.66700  31.99200  1.000 54.37105  ?  691  ALA B O   1 
ATOM   2777 C  CB  . ALA A 1 414 ? -4.81900  -5.58100  31.77200  1.000 40.57684  ?  691  ALA B CB  1 
ATOM   2778 N  N   . GLU A 1 415 ? -6.88500  -3.58200  30.34000  1.000 49.03405  ?  692  GLU B N   1 
ATOM   2779 C  CA  . GLU A 1 415 ? -7.76500  -2.42400  30.42600  1.000 51.14002  ?  692  GLU B CA  1 
ATOM   2780 C  C   . GLU A 1 415 ? -9.13100  -2.72600  29.80900  1.000 53.34927  ?  692  GLU B C   1 
ATOM   2781 O  O   . GLU A 1 415 ? -10.16000 -2.26500  30.31800  1.000 57.08405  ?  692  GLU B O   1 
ATOM   2782 C  CB  . GLU A 1 415 ? -7.10000  -1.22100  29.75400  1.000 56.55006  ?  692  GLU B CB  1 
ATOM   2783 C  CG  . GLU A 1 415 ? -7.65300  0.11100   30.17900  1.000 60.56420  ?  692  GLU B CG  1 
ATOM   2784 C  CD  . GLU A 1 415 ? -7.43000  0.40000   31.66200  1.000 83.30255  ?  692  GLU B CD  1 
ATOM   2785 O  OE1 . GLU A 1 415 ? -6.25200  0.45200   32.09500  1.000 93.43831  ?  692  GLU B OE1 1 
ATOM   2786 O  OE2 . GLU A 1 415 ? -8.43200  0.57200   32.40100  1.000 88.38170  -1 692  GLU B OE2 1 
ATOM   2787 N  N   . VAL A 1 416 ? -9.16400  -3.51700  28.73200  1.000 51.85589  ?  693  VAL B N   1 
ATOM   2788 C  CA  . VAL A 1 416 ? -10.43500 -4.00500  28.20000  1.000 49.83561  ?  693  VAL B CA  1 
ATOM   2789 C  C   . VAL A 1 416 ? -11.24100 -4.70100  29.29200  1.000 54.59448  ?  693  VAL B C   1 
ATOM   2790 O  O   . VAL A 1 416 ? -12.43300 -4.42300  29.49100  1.000 58.06012  ?  693  VAL B O   1 
ATOM   2791 C  CB  . VAL A 1 416 ? -10.20000 -4.95200  27.00900  1.000 56.34447  ?  693  VAL B CB  1 
ATOM   2792 C  CG1 . VAL A 1 416 ? -11.48800 -5.65600  26.64900  1.000 55.77586  ?  693  VAL B CG1 1 
ATOM   2793 C  CG2 . VAL A 1 416 ? -9.63200  -4.19900  25.79800  1.000 50.81458  ?  693  VAL B CG2 1 
ATOM   2794 N  N   . LEU A 1 417 ? -10.61100 -5.64200  30.00300  1.000 51.29760  ?  694  LEU B N   1 
ATOM   2795 C  CA  . LEU A 1 417 ? -11.32900 -6.34600  31.06200  1.000 60.88285  ?  694  LEU B CA  1 
ATOM   2796 C  C   . LEU A 1 417 ? -11.72500 -5.40400  32.19000  1.000 54.29631  ?  694  LEU B C   1 
ATOM   2797 O  O   . LEU A 1 417 ? -12.79200 -5.56900  32.79000  1.000 48.03181  ?  694  LEU B O   1 
ATOM   2798 C  CB  . LEU A 1 417 ? -10.49000 -7.50300  31.61800  1.000 63.83977  ?  694  LEU B CB  1 
ATOM   2799 C  CG  . LEU A 1 417 ? -9.99000  -8.58800  30.65500  1.000 59.91391  ?  694  LEU B CG  1 
ATOM   2800 C  CD1 . LEU A 1 417 ? -9.44200  -9.74100  31.47500  1.000 65.09981  ?  694  LEU B CD1 1 
ATOM   2801 C  CD2 . LEU A 1 417 ? -11.09100 -9.07800  29.73600  1.000 58.81622  ?  694  LEU B CD2 1 
ATOM   2802 N  N   . ASP A 1 418 ? -10.89700 -4.40200  32.47600  1.000 53.31414  ?  695  ASP B N   1 
ATOM   2803 C  CA  . ASP A 1 418 ? -11.20700 -3.50600  33.57900  1.000 54.81466  ?  695  ASP B CA  1 
ATOM   2804 C  C   . ASP A 1 418 ? -12.42800 -2.65200  33.26700  1.000 57.98027  ?  695  ASP B C   1 
ATOM   2805 O  O   . ASP A 1 418 ? -13.24800 -2.39800  34.15100  1.000 54.15171  ?  695  ASP B O   1 
ATOM   2806 C  CB  . ASP A 1 418 ? -10.00000 -2.63000  33.90200  1.000 56.76732  ?  695  ASP B CB  1 
ATOM   2807 C  CG  . ASP A 1 418 ? -10.10900 -1.99000  35.26000  1.000 60.60905  ?  695  ASP B CG  1 
ATOM   2808 O  OD1 . ASP A 1 418 ? -10.11200 -2.73500  36.26100  1.000 56.70793  ?  695  ASP B OD1 1 
ATOM   2809 O  OD2 . ASP A 1 418 ? -10.20800 -0.74900  35.32500  1.000 68.62148  -1 695  ASP B OD2 1 
ATOM   2810 N  N   . THR A 1 419 ? -12.57200 -2.21300  32.01300  1.000 55.74363  ?  696  THR B N   1 
ATOM   2811 C  CA  . THR A 1 419 ? -13.59000 -1.24500  31.61800  1.000 53.96604  ?  696  THR B CA  1 
ATOM   2812 C  C   . THR A 1 419 ? -14.80200 -1.87600  30.94000  1.000 54.54952  ?  696  THR B C   1 
ATOM   2813 O  O   . THR A 1 419 ? -15.93400 -1.48400  31.22500  1.000 57.92161  ?  696  THR B O   1 
ATOM   2814 C  CB  . THR A 1 419 ? -12.98300 -0.19200  30.67000  1.000 62.34131  ?  696  THR B CB  1 
ATOM   2815 O  OG1 . THR A 1 419 ? -12.49200 -0.83700  29.48300  1.000 59.10035  ?  696  THR B OG1 1 
ATOM   2816 C  CG2 . THR A 1 419 ? -11.83400 0.55600   31.33500  1.000 56.30854  ?  696  THR B CG2 1 
ATOM   2817 N  N   . GLU A 1 420 ? -14.60500 -2.82800  30.03100  1.000 57.21836  ?  697  GLU B N   1 
ATOM   2818 C  CA  . GLU A 1 420 ? -15.72700 -3.44200  29.33800  1.000 55.06442  ?  697  GLU B CA  1 
ATOM   2819 C  C   . GLU A 1 420 ? -16.05100 -4.84900  29.83100  1.000 59.27315  ?  697  GLU B C   1 
ATOM   2820 O  O   . GLU A 1 420 ? -17.13100 -5.36400  29.52300  1.000 59.47526  ?  697  GLU B O   1 
ATOM   2821 C  CB  . GLU A 1 420 ? -15.46300 -3.47200  27.82400  1.000 57.50390  ?  697  GLU B CB  1 
ATOM   2822 C  CG  . GLU A 1 420 ? -14.83000 -2.18500  27.26200  1.000 59.41965  ?  697  GLU B CG  1 
ATOM   2823 C  CD  . GLU A 1 420 ? -15.75500 -0.97700  27.31500  1.000 62.26735  ?  697  GLU B CD  1 
ATOM   2824 O  OE1 . GLU A 1 420 ? -16.96800 -1.15800  27.60300  1.000 72.65913  ?  697  GLU B OE1 1 
ATOM   2825 N  N   . GLY A 1 421 ? -15.15500 -5.48200  30.58800  1.000 61.12861  ?  698  GLY B N   1 
ATOM   2826 C  CA  . GLY A 1 421 ? -15.43600 -6.76400  31.20300  1.000 58.08446  ?  698  GLY B CA  1 
ATOM   2827 C  C   . GLY A 1 421 ? -15.05300 -7.96700  30.36900  1.000 61.47105  ?  698  GLY B C   1 
ATOM   2828 O  O   . GLY A 1 421 ? -15.01400 -9.08200  30.90300  1.000 65.27076  ?  698  GLY B O   1 
ATOM   2829 N  N   . SER A 1 422 ? -14.77900 -7.79100  29.08400  1.000 59.80604  ?  699  SER B N   1 
ATOM   2830 C  CA  . SER A 1 422 ? -14.49900 -8.93800  28.23500  1.000 61.34003  ?  699  SER B CA  1 
ATOM   2831 C  C   . SER A 1 422 ? -14.15700 -8.49400  26.82400  1.000 59.81965  ?  699  SER B C   1 
ATOM   2832 O  O   . SER A 1 422 ? -14.66500 -7.47300  26.35100  1.000 58.09008  ?  699  SER B O   1 
ATOM   2833 C  CB  . SER A 1 422 ? -15.70000 -9.88000  28.19500  1.000 60.28722  ?  699  SER B CB  1 
ATOM   2834 O  OG  . SER A 1 422 ? -16.65000 -9.41800  27.24900  1.000 64.34535  ?  699  SER B OG  1 
ATOM   2835 N  N   . ILE A 1 423 ? -13.31600 -9.26200  26.13600  1.000 59.43034  ?  700  ILE B N   1 
ATOM   2836 C  CA  . ILE A 1 423 ? -12.98900 -8.94100  24.75400  1.000 55.67297  ?  700  ILE B CA  1 
ATOM   2837 C  C   . ILE A 1 423 ? -14.25500 -8.88500  23.90800  1.000 62.82813  ?  700  ILE B C   1 
ATOM   2838 O  O   . ILE A 1 423 ? -14.39600 -8.01900  23.03700  1.000 60.40711  ?  700  ILE B O   1 
ATOM   2839 C  CB  . ILE A 1 423 ? -11.96600 -9.95000  24.21000  1.000 56.53429  ?  700  ILE B CB  1 
ATOM   2840 C  CG1 . ILE A 1 423 ? -10.60700 -9.72900  24.90100  1.000 49.59426  ?  700  ILE B CG1 1 
ATOM   2841 C  CG2 . ILE A 1 423 ? -11.88600 -9.87900  22.65900  1.000 55.10804  ?  700  ILE B CG2 1 
ATOM   2842 C  CD1 . ILE A 1 423 ? -9.57200  -10.79200 24.60100  1.000 47.49171  ?  700  ILE B CD1 1 
ATOM   2843 N  N   . GLN A 1 424 ? -15.21000 -9.78100  24.16400  1.000 61.53726  ?  701  GLN B N   1 
ATOM   2844 C  CA  . GLN A 1 424 ? -16.43000 -9.77700  23.36400  1.000 67.07548  ?  701  GLN B CA  1 
ATOM   2845 C  C   . GLN A 1 424 ? -17.23000 -8.50100  23.58000  1.000 69.26766  ?  701  GLN B C   1 
ATOM   2846 O  O   . GLN A 1 424 ? -17.77300 -7.93000  22.62600  1.000 66.34394  ?  701  GLN B O   1 
ATOM   2847 C  CB  . GLN A 1 424 ? -17.28700 -10.99200 23.69400  1.000 67.85855  ?  701  GLN B CB  1 
ATOM   2848 C  CG  . GLN A 1 424 ? -16.74600 -12.27600 23.12900  1.000 72.08665  ?  701  GLN B CG  1 
ATOM   2849 C  CD  . GLN A 1 424 ? -17.71100 -12.92800 22.15800  1.000 80.17006  ?  701  GLN B CD  1 
ATOM   2850 O  OE1 . GLN A 1 424 ? -18.93700 -12.88200 22.33500  1.000 79.02050  ?  701  GLN B OE1 1 
ATOM   2851 N  NE2 . GLN A 1 424 ? -17.15900 -13.54100 21.11600  1.000 77.53286  ?  701  GLN B NE2 1 
ATOM   2852 N  N   . ASN A 1 425 ? -17.33800 -8.05000  24.83100  1.000 63.41682  ?  702  ASN B N   1 
ATOM   2853 C  CA  . ASN A 1 425 ? -18.00800 -6.78200  25.09100  1.000 63.05536  ?  702  ASN B CA  1 
ATOM   2854 C  C   . ASN A 1 425 ? -17.33500 -5.64900  24.32600  1.000 65.46472  ?  702  ASN B C   1 
ATOM   2855 O  O   . ASN A 1 425 ? -18.00000 -4.85800  23.64500  1.000 66.58055  ?  702  ASN B O   1 
ATOM   2856 C  CB  . ASN A 1 425 ? -18.01200 -6.49800  26.58400  1.000 58.98270  ?  702  ASN B CB  1 
ATOM   2857 C  CG  . ASN A 1 425 ? -18.99800 -7.36000  27.31800  1.000 68.17812  ?  702  ASN B CG  1 
ATOM   2858 O  OD1 . ASN A 1 425 ? -19.86000 -7.97800  26.69700  1.000 69.69649  ?  702  ASN B OD1 1 
ATOM   2859 N  ND2 . ASN A 1 425 ? -18.89800 -7.39700  28.64700  1.000 62.55161  ?  702  ASN B ND2 1 
ATOM   2860 N  N   . PHE A 1 426 ? -16.01000 -5.56800  24.42000  1.000 58.62320  ?  703  PHE B N   1 
ATOM   2861 C  CA  . PHE A 1 426 ? -15.25300 -4.57200  23.67700  1.000 58.33568  ?  703  PHE B CA  1 
ATOM   2862 C  C   . PHE A 1 426 ? -15.66000 -4.55700  22.20400  1.000 61.80651  ?  703  PHE B C   1 
ATOM   2863 O  O   . PHE A 1 426 ? -16.05600 -3.51500  21.66600  1.000 62.00269  ?  703  PHE B O   1 
ATOM   2864 C  CB  . PHE A 1 426 ? -13.76100 -4.86500  23.85800  1.000 58.22248  ?  703  PHE B CB  1 
ATOM   2865 C  CG  . PHE A 1 426 ? -12.83200 -3.91400  23.14500  1.000 57.75405  ?  703  PHE B CG  1 
ATOM   2866 C  CD1 . PHE A 1 426 ? -12.60400 -2.63800  23.63900  1.000 59.39160  ?  703  PHE B CD1 1 
ATOM   2867 C  CD2 . PHE A 1 426 ? -12.13100 -4.32600  22.02000  1.000 55.22638  ?  703  PHE B CD2 1 
ATOM   2868 C  CE1 . PHE A 1 426 ? -11.73000 -1.78000  23.01800  1.000 50.13391  ?  703  PHE B CE1 1 
ATOM   2869 C  CE2 . PHE A 1 426 ? -11.24300 -3.47100  21.39400  1.000 57.63401  ?  703  PHE B CE2 1 
ATOM   2870 C  CZ  . PHE A 1 426 ? -11.04600 -2.19300  21.89600  1.000 56.04588  ?  703  PHE B CZ  1 
ATOM   2871 N  N   . PHE A 1 427 ? -15.59600 -5.71700  21.54400  1.000 60.27659  ?  704  PHE B N   1 
ATOM   2872 C  CA  . PHE A 1 427 ? -15.93700 -5.78700  20.12600  1.000 61.27058  ?  704  PHE B CA  1 
ATOM   2873 C  C   . PHE A 1 427 ? -17.38400 -5.36400  19.88100  1.000 69.94842  ?  704  PHE B C   1 
ATOM   2874 O  O   . PHE A 1 427 ? -17.68300 -4.69700  18.88100  1.000 68.04195  ?  704  PHE B O   1 
ATOM   2875 C  CB  . PHE A 1 427 ? -15.68400 -7.20100  19.58800  1.000 56.43160  ?  704  PHE B CB  1 
ATOM   2876 C  CG  . PHE A 1 427 ? -14.22000 -7.54200  19.41000  1.000 60.09738  ?  704  PHE B CG  1 
ATOM   2877 C  CD1 . PHE A 1 427 ? -13.26800 -6.54100  19.25000  1.000 60.13927  ?  704  PHE B CD1 1 
ATOM   2878 C  CD2 . PHE A 1 427 ? -13.79700 -8.86700  19.38900  1.000 55.50985  ?  704  PHE B CD2 1 
ATOM   2879 C  CE1 . PHE A 1 427 ? -11.91100 -6.85100  19.06600  1.000 56.51353  ?  704  PHE B CE1 1 
ATOM   2880 C  CE2 . PHE A 1 427 ? -12.44600 -9.18500  19.22000  1.000 58.65275  ?  704  PHE B CE2 1 
ATOM   2881 C  CZ  . PHE A 1 427 ? -11.49700 -8.17000  19.05700  1.000 53.60178  ?  704  PHE B CZ  1 
ATOM   2882 N  N   . ARG A 1 428 ? -18.30000 -5.74500  20.77400  1.000 64.31435  ?  705  ARG B N   1 
ATOM   2883 C  CA  . ARG A 1 428 ? -19.69600 -5.39200  20.57400  1.000 68.75561  ?  705  ARG B CA  1 
ATOM   2884 C  C   . ARG A 1 428 ? -19.93900 -3.90200  20.76300  1.000 70.88299  ?  705  ARG B C   1 
ATOM   2885 O  O   . ARG A 1 428 ? -20.95000 -3.38500  20.26900  1.000 76.31619  ?  705  ARG B O   1 
ATOM   2886 C  CB  . ARG A 1 428 ? -20.59300 -6.19800  21.52000  1.000 70.58955  ?  705  ARG B CB  1 
ATOM   2887 C  CG  . ARG A 1 428 ? -21.12500 -7.49800  20.92300  1.000 70.63211  ?  705  ARG B CG  1 
ATOM   2888 C  CD  . ARG A 1 428 ? -22.18400 -8.14400  21.81200  1.000 68.51859  ?  705  ARG B CD  1 
ATOM   2889 N  NE  . ARG A 1 428 ? -21.65600 -8.53800  23.11200  1.000 72.51440  ?  705  ARG B NE  1 
ATOM   2890 C  CZ  . ARG A 1 428 ? -21.02800 -9.68200  23.35000  1.000 78.15952  ?  705  ARG B CZ  1 
ATOM   2891 N  NH1 . ARG A 1 428 ? -20.87200 -10.59500 22.40300  1.000 73.77029  ?  705  ARG B NH1 1 
ATOM   2892 N  NH2 . ARG A 1 428 ? -20.53400 -9.91100  24.56400  1.000 79.33816  ?  705  ARG B NH2 1 
ATOM   2893 N  N   . LYS A 1 429 ? -19.03600 -3.20400  21.45500  1.000 63.39350  ?  706  LYS B N   1 
ATOM   2894 C  CA  . LYS A 1 429 ? -19.19200 -1.77200  21.68800  1.000 63.87715  ?  706  LYS B CA  1 
ATOM   2895 C  C   . LYS A 1 429 ? -18.64400 -0.94200  20.52600  1.000 71.95480  ?  706  LYS B C   1 
ATOM   2896 O  O   . LYS A 1 429 ? -19.21000 0.10400   20.18700  1.000 73.95505  ?  706  LYS B O   1 
ATOM   2897 C  CB  . LYS A 1 429 ? -18.50500 -1.38600  22.99800  1.000 65.70508  ?  706  LYS B CB  1 
ATOM   2898 C  CG  . LYS A 1 429 ? -18.27300 0.09500   23.22600  1.000 67.05206  ?  706  LYS B CG  1 
ATOM   2899 C  CD  . LYS A 1 429 ? -18.15800 0.39800   24.71900  1.000 75.24441  ?  706  LYS B CD  1 
ATOM   2900 C  CE  . LYS A 1 429 ? -17.39700 1.69200   24.98100  1.000 81.91703  ?  706  LYS B CE  1 
ATOM   2901 N  NZ  . LYS A 1 429 ? -17.22100 1.96900   26.43500  1.000 78.45531  ?  706  LYS B NZ  1 
ATOM   2902 N  N   . TYR A 1 430 ? -17.55400 -1.38000  19.89700  1.000 68.71509  ?  707  TYR B N   1 
ATOM   2903 C  CA  . TYR A 1 430 ? -16.92600 -0.59800  18.84400  1.000 68.78785  ?  707  TYR B CA  1 
ATOM   2904 C  C   . TYR A 1 430 ? -17.13000 -1.16300  17.44400  1.000 66.83706  ?  707  TYR B C   1 
ATOM   2905 O  O   . TYR A 1 430 ? -16.79200 -0.48400  16.47300  1.000 71.96838  ?  707  TYR B O   1 
ATOM   2906 C  CB  . TYR A 1 430 ? -15.42100 -0.44200  19.12800  1.000 65.11441  ?  707  TYR B CB  1 
ATOM   2907 C  CG  . TYR A 1 430 ? -15.17500 0.35700   20.38500  1.000 67.68213  ?  707  TYR B CG  1 
ATOM   2908 C  CD1 . TYR A 1 430 ? -15.52100 1.69700   20.45100  1.000 68.27229  ?  707  TYR B CD1 1 
ATOM   2909 C  CD2 . TYR A 1 430 ? -14.62700 -0.23600  21.51900  1.000 69.29888  ?  707  TYR B CD2 1 
ATOM   2910 C  CE1 . TYR A 1 430 ? -15.31700 2.43100   21.60100  1.000 74.22637  ?  707  TYR B CE1 1 
ATOM   2911 C  CE2 . TYR A 1 430 ? -14.41300 0.49100   22.67400  1.000 70.26280  ?  707  TYR B CE2 1 
ATOM   2912 C  CZ  . TYR A 1 430 ? -14.76700 1.82600   22.71400  1.000 72.99042  ?  707  TYR B CZ  1 
ATOM   2913 O  OH  . TYR A 1 430 ? -14.56700 2.55600   23.86900  1.000 68.40601  ?  707  TYR B OH  1 
ATOM   2914 N  N   . ALA A 1 431 ? -17.68000 -2.36300  17.30700  1.000 68.51155  ?  708  ALA B N   1 
ATOM   2915 C  CA  . ALA A 1 431 ? -17.88000 -2.95300  15.98800  1.000 69.24306  ?  708  ALA B CA  1 
ATOM   2916 C  C   . ALA A 1 431 ? -19.05500 -3.92300  15.98900  1.000 71.74744  ?  708  ALA B C   1 
ATOM   2917 O  O   . ALA A 1 431 ? -18.88800 -5.10300  15.65100  1.000 71.40131  ?  708  ALA B O   1 
ATOM   2918 C  CB  . ALA A 1 431 ? -16.60700 -3.66100  15.52600  1.000 68.65953  ?  708  ALA B CB  1 
ATOM   2919 N  N   . PRO A 1 432 ? -20.25200 -3.47000  16.34200  1.000 72.89306  ?  709  PRO B N   1 
ATOM   2920 C  CA  . PRO A 1 432 ? -21.41000 -4.37100  16.39800  1.000 75.21602  ?  709  PRO B CA  1 
ATOM   2921 C  C   . PRO A 1 432 ? -21.94500 -4.72000  15.01400  1.000 82.85382  ?  709  PRO B C   1 
ATOM   2922 O  O   . PRO A 1 432 ? -21.60200 -4.10000  13.99700  1.000 85.58854  ?  709  PRO B O   1 
ATOM   2923 C  CB  . PRO A 1 432 ? -22.43900 -3.56000  17.18600  1.000 71.44053  ?  709  PRO B CB  1 
ATOM   2924 C  CG  . PRO A 1 432 ? -22.11700 -2.15200  16.82500  1.000 70.83498  ?  709  PRO B CG  1 
ATOM   2925 C  CD  . PRO A 1 432 ? -20.61100 -2.09600  16.72500  1.000 69.20234  ?  709  PRO B CD  1 
ATOM   2926 N  N   . SER A 1 433 ? -22.82000 -5.72600  15.00000  1.000 82.57474  ?  710  SER B N   1 
ATOM   2927 C  CA  . SER A 1 433 ? -23.41200 -6.24700  13.77000  1.000 84.45926  ?  710  SER B CA  1 
ATOM   2928 C  C   . SER A 1 433 ? -24.58500 -7.14300  14.13200  1.000 91.08253  ?  710  SER B C   1 
ATOM   2929 O  O   . SER A 1 433 ? -24.38400 -8.21400  14.71200  1.000 88.98796  ?  710  SER B O   1 
ATOM   2930 C  CB  . SER A 1 433 ? -22.37700 -7.02800  12.95600  1.000 82.61249  ?  710  SER B CB  1 
ATOM   2931 O  OG  . SER A 1 433 ? -22.68300 -7.00500  11.57400  1.000 89.16368  ?  710  SER B OG  1 
ATOM   2932 N  N   . GLU A 1 434 ? -25.80900 -6.71000  13.81100  1.000 96.01399  ?  711  GLU B N   1 
ATOM   2933 C  CA  . GLU A 1 434 ? -26.98700 -7.50300  14.15600  1.000 96.62214  ?  711  GLU B CA  1 
ATOM   2934 C  C   . GLU A 1 434 ? -26.79600 -8.96200  13.76100  1.000 97.76492  ?  711  GLU B C   1 
ATOM   2935 O  O   . GLU A 1 434 ? -26.93700 -9.86800  14.59000  1.000 97.85730  ?  711  GLU B O   1 
ATOM   2936 C  CB  . GLU A 1 434 ? -28.22900 -6.91300  13.48500  1.000 96.86601  ?  711  GLU B CB  1 
ATOM   2937 N  N   . ASN A 1 435 ? -26.43700 -9.20400  12.50200  1.000 99.71622  ?  712  ASN B N   1 
ATOM   2938 C  CA  . ASN A 1 435 ? -26.27800 -10.55600 11.98300  1.000 109.13804 ?  712  ASN B CA  1 
ATOM   2939 C  C   . ASN A 1 435 ? -24.82900 -11.04000 12.03300  1.000 101.65024 ?  712  ASN B C   1 
ATOM   2940 O  O   . ASN A 1 435 ? -24.52700 -12.10800 11.49500  1.000 106.45308 ?  712  ASN B O   1 
ATOM   2941 C  CB  . ASN A 1 435 ? -26.82700 -10.64100 10.55100  1.000 104.15537 ?  712  ASN B CB  1 
ATOM   2942 N  N   . GLY A 1 436 ? -23.93600 -10.29800 12.68100  1.000 94.58098  ?  713  GLY B N   1 
ATOM   2943 C  CA  . GLY A 1 436 ? -22.56600 -10.73400 12.84300  1.000 93.20638  ?  713  GLY B CA  1 
ATOM   2944 C  C   . GLY A 1 436 ? -22.42800 -11.75700 13.95300  1.000 87.64967  ?  713  GLY B C   1 
ATOM   2945 O  O   . GLY A 1 436 ? -23.32200 -11.91000 14.78800  1.000 90.85242  ?  713  GLY B O   1 
ATOM   2946 N  N   . PRO A 1 437 ? -21.30700 -12.48200 13.98700  1.000 88.29874  ?  714  PRO B N   1 
ATOM   2947 C  CA  . PRO A 1 437 ? -21.11600 -13.50300 15.03300  1.000 86.10886  ?  714  PRO B CA  1 
ATOM   2948 C  C   . PRO A 1 437 ? -21.10300 -12.88200 16.41900  1.000 85.27844  ?  714  PRO B C   1 
ATOM   2949 O  O   . PRO A 1 437 ? -20.26900 -12.02700 16.72800  1.000 84.65002  ?  714  PRO B O   1 
ATOM   2950 C  CB  . PRO A 1 437 ? -19.75600 -14.11600 14.68200  1.000 80.18497  ?  714  PRO B CB  1 
ATOM   2951 C  CG  . PRO A 1 437 ? -19.04700 -13.03500 13.94100  1.000 84.52929  ?  714  PRO B CG  1 
ATOM   2952 C  CD  . PRO A 1 437 ? -20.12600 -12.37500 13.11300  1.000 91.18320  ?  714  PRO B CD  1 
ATOM   2953 N  N   . ASN A 1 438 ? -22.03600 -13.32500 17.26000  1.000 87.81136  ?  715  ASN B N   1 
ATOM   2954 C  CA  . ASN A 1 438 ? -22.11700 -12.86300 18.64500  1.000 86.14880  ?  715  ASN B CA  1 
ATOM   2955 C  C   . ASN A 1 438 ? -22.44800 -11.37500 18.71600  1.000 82.82995  ?  715  ASN B C   1 
ATOM   2956 O  O   . ASN A 1 438 ? -22.13600 -10.70600 19.70700  1.000 75.27922  ?  715  ASN B O   1 
ATOM   2957 C  CB  . ASN A 1 438 ? -20.81200 -13.15700 19.39900  1.000 83.99487  ?  715  ASN B CB  1 
ATOM   2958 C  CG  . ASN A 1 438 ? -20.89300 -14.41500 20.23700  1.000 87.74430  ?  715  ASN B CG  1 
ATOM   2959 O  OD1 . ASN A 1 438 ? -20.94100 -14.34500 21.46000  1.000 100.93326 ?  715  ASN B OD1 1 
ATOM   2960 N  ND2 . ASN A 1 438 ? -20.92100 -15.56900 19.58800  1.000 90.57810  ?  715  ASN B ND2 1 
ATOM   2961 N  N   . GLY A 1 439 ? -23.07800 -10.84800 17.66300  1.000 80.20847  ?  716  GLY B N   1 
ATOM   2962 C  CA  . GLY A 1 439 ? -23.29400 -9.41900  17.55200  1.000 80.42297  ?  716  GLY B CA  1 
ATOM   2963 C  C   . GLY A 1 439 ? -22.06600 -8.61600  17.19400  1.000 81.13226  ?  716  GLY B C   1 
ATOM   2964 O  O   . GLY A 1 439 ? -22.09100 -7.38800  17.30800  1.000 82.54573  ?  716  GLY B O   1 
ATOM   2965 N  N   . ILE A 1 440 ? -20.98700 -9.26800  16.76700  1.000 77.24455  ?  717  ILE B N   1 
ATOM   2966 C  CA  . ILE A 1 440 ? -19.74900 -8.59400  16.40100  1.000 77.15391  ?  717  ILE B CA  1 
ATOM   2967 C  C   . ILE A 1 440 ? -19.55900 -8.66700  14.89300  1.000 80.99766  ?  717  ILE B C   1 
ATOM   2968 O  O   . ILE A 1 440 ? -19.83200 -9.70100  14.26800  1.000 78.89950  ?  717  ILE B O   1 
ATOM   2969 C  CB  . ILE A 1 440 ? -18.54000 -9.21300  17.13100  1.000 74.53819  ?  717  ILE B CB  1 
ATOM   2970 C  CG1 . ILE A 1 440 ? -18.71100 -9.07800  18.64500  1.000 71.35324  ?  717  ILE B CG1 1 
ATOM   2971 C  CG2 . ILE A 1 440 ? -17.24900 -8.55500  16.66100  1.000 69.48941  ?  717  ILE B CG2 1 
ATOM   2972 C  CD1 . ILE A 1 440 ? -17.78500 -9.96300  19.41900  1.000 70.64334  ?  717  ILE B CD1 1 
ATOM   2973 N  N   . SER A 1 441 ? -19.08100 -7.56500  14.31300  1.000 74.05026  ?  718  SER B N   1 
ATOM   2974 C  CA  . SER A 1 441 ? -18.69500 -7.51600  12.90900  1.000 75.30926  ?  718  SER B CA  1 
ATOM   2975 C  C   . SER A 1 441 ? -17.92600 -8.76600  12.51200  1.000 77.01386  ?  718  SER B C   1 
ATOM   2976 O  O   . SER A 1 441 ? -16.88300 -9.08000  13.09600  1.000 77.36752  ?  718  SER B O   1 
ATOM   2977 C  CB  . SER A 1 441 ? -17.83900 -6.26900  12.65300  1.000 75.93187  ?  718  SER B CB  1 
ATOM   2978 O  OG  . SER A 1 441 ? -17.21600 -6.30800  11.37300  1.000 78.48285  ?  718  SER B OG  1 
ATOM   2979 N  N   . ALA A 1 442 ? -18.44500 -9.49000  11.51700  1.000 80.28043  ?  719  ALA B N   1 
ATOM   2980 C  CA  . ALA A 1 442 ? -17.72100 -10.64800 11.00000  1.000 78.90064  ?  719  ALA B CA  1 
ATOM   2981 C  C   . ALA A 1 442 ? -16.30900 -10.27000 10.55900  1.000 77.73206  ?  719  ALA B C   1 
ATOM   2982 O  O   . ALA A 1 442 ? -15.37200 -11.06200 10.71200  1.000 74.70072  ?  719  ALA B O   1 
ATOM   2983 C  CB  . ALA A 1 442 ? -18.48600 -11.27900 9.84200   1.000 81.20891  ?  719  ALA B CB  1 
ATOM   2984 N  N   . GLU A 1 443 ? -16.13400 -9.07000  9.99800   1.000 78.54537  ?  720  GLU B N   1 
ATOM   2985 C  CA  . GLU A 1 443 ? -14.79100 -8.63800  9.61300   1.000 74.81041  ?  720  GLU B CA  1 
ATOM   2986 C  C   . GLU A 1 443 ? -13.87300 -8.56600  10.83800  1.000 75.77621  ?  720  GLU B C   1 
ATOM   2987 O  O   . GLU A 1 443 ? -12.74600 -9.09000  10.82700  1.000 65.52952  ?  720  GLU B O   1 
ATOM   2988 C  CB  . GLU A 1 443 ? -14.86500 -7.28900  8.88800   1.000 79.71488  ?  720  GLU B CB  1 
ATOM   2989 C  CG  . GLU A 1 443 ? -13.62800 -6.90100  8.08700   1.000 79.97659  ?  720  GLU B CG  1 
ATOM   2990 N  N   . VAL A 1 444 ? -14.35400 -7.94500  11.91900  1.000 70.06894  ?  721  VAL B N   1 
ATOM   2991 C  CA  . VAL A 1 444 ? -13.54000 -7.81700  13.12400  1.000 66.39794  ?  721  VAL B CA  1 
ATOM   2992 C  C   . VAL A 1 444 ? -13.26800 -9.18900  13.73900  1.000 66.27610  ?  721  VAL B C   1 
ATOM   2993 O  O   . VAL A 1 444 ? -12.14700 -9.48200  14.17100  1.000 62.34071  ?  721  VAL B O   1 
ATOM   2994 C  CB  . VAL A 1 444 ? -14.22700 -6.85600  14.11400  1.000 68.24152  ?  721  VAL B CB  1 
ATOM   2995 C  CG1 . VAL A 1 444 ? -13.62800 -6.97900  15.51600  1.000 57.64660  ?  721  VAL B CG1 1 
ATOM   2996 C  CG2 . VAL A 1 444 ? -14.11900 -5.41900  13.60600  1.000 60.87717  ?  721  VAL B CG2 1 
ATOM   2997 N  N   . MET A 1 445 ? -14.27700 -10.06100 13.76500  1.000 70.73418  ?  722  MET B N   1 
ATOM   2998 C  CA  . MET A 1 445 ? -14.08300 -11.38800 14.33800  1.000 66.43049  ?  722  MET B CA  1 
ATOM   2999 C  C   . MET A 1 445 ? -13.05200 -12.19600 13.55600  1.000 63.68531  ?  722  MET B C   1 
ATOM   3000 O  O   . MET A 1 445 ? -12.25800 -12.92800 14.15400  1.000 62.30865  ?  722  MET B O   1 
ATOM   3001 C  CB  . MET A 1 445 ? -15.41400 -12.13400 14.40200  1.000 61.33947  ?  722  MET B CB  1 
ATOM   3002 C  CG  . MET A 1 445 ? -15.31800 -13.45300 15.16500  1.000 69.78671  ?  722  MET B CG  1 
ATOM   3003 S  SD  . MET A 1 445 ? -14.53500 -13.26100 16.79200  1.000 67.87606  ?  722  MET B SD  1 
ATOM   3004 C  CE  . MET A 1 445 ? -15.65900 -12.08800 17.55900  1.000 65.91159  ?  722  MET B CE  1 
ATOM   3005 N  N   . ASP A 1 446 ? -13.04800 -12.07900 12.21900  1.000 65.27388  ?  723  ASP B N   1 
ATOM   3006 C  CA  . ASP A 1 446 ? -12.08200 -12.81700 11.40700  1.000 64.10755  ?  723  ASP B CA  1 
ATOM   3007 C  C   . ASP A 1 446 ? -10.66200 -12.31200 11.62300  1.000 62.19560  ?  723  ASP B C   1 
ATOM   3008 O  O   . ASP A 1 446 ? -9.70900  -13.09800 11.56900  1.000 62.87331  ?  723  ASP B O   1 
ATOM   3009 C  CB  . ASP A 1 446 ? -12.45100 -12.72400 9.92600   1.000 68.52941  ?  723  ASP B CB  1 
ATOM   3010 C  CG  . ASP A 1 446 ? -11.51300 -13.54000 9.03300   1.000 82.07821  ?  723  ASP B CG  1 
ATOM   3011 O  OD1 . ASP A 1 446 ? -11.71700 -14.76900 8.92800   1.000 87.81335  ?  723  ASP B OD1 1 
ATOM   3012 O  OD2 . ASP A 1 446 ? -10.57000 -12.96200 8.43600   1.000 84.62148  -1 723  ASP B OD2 1 
ATOM   3013 N  N   . THR A 1 447 ? -10.51300 -11.00400 11.85200  1.000 61.32133  ?  724  THR B N   1 
ATOM   3014 C  CA  . THR A 1 447 ? -9.22200  -10.40600 12.16300  1.000 54.29934  ?  724  THR B CA  1 
ATOM   3015 C  C   . THR A 1 447 ? -8.69900  -10.89500 13.50600  1.000 60.27981  ?  724  THR B C   1 
ATOM   3016 O  O   . THR A 1 447 ? -7.48900  -11.10700 13.67900  1.000 55.68246  ?  724  THR B O   1 
ATOM   3017 C  CB  . THR A 1 447 ? -9.36800  -8.87900  12.17400  1.000 59.96426  ?  724  THR B CB  1 
ATOM   3018 O  OG1 . THR A 1 447 ? -9.90100  -8.43100  10.91400  1.000 64.13356  ?  724  THR B OG1 1 
ATOM   3019 C  CG2 . THR A 1 447 ? -8.04100  -8.19100  12.45600  1.000 59.02287  ?  724  THR B CG2 1 
ATOM   3020 N  N   . TYR A 1 448 ? -9.60100  -11.07000 14.47700  1.000 59.36872  ?  725  TYR B N   1 
ATOM   3021 C  CA  . TYR A 1 448 ? -9.18700  -11.47000 15.81600  1.000 52.51028  ?  725  TYR B CA  1 
ATOM   3022 C  C   . TYR A 1 448 ? -8.76900  -12.93600 15.84700  1.000 59.00508  ?  725  TYR B C   1 
ATOM   3023 O  O   . TYR A 1 448 ? -7.73900  -13.27600 16.44600  1.000 56.07730  ?  725  TYR B O   1 
ATOM   3024 C  CB  . TYR A 1 448 ? -10.31100 -11.19100 16.81500  1.000 56.48317  ?  725  TYR B CB  1 
ATOM   3025 C  CG  . TYR A 1 448 ? -10.04800 -11.69100 18.21700  1.000 57.07913  ?  725  TYR B CG  1 
ATOM   3026 C  CD1 . TYR A 1 448 ? -9.11300  -11.07600 19.03500  1.000 55.01753  ?  725  TYR B CD1 1 
ATOM   3027 C  CD2 . TYR A 1 448 ? -10.74000 -12.77600 18.72000  1.000 60.91590  ?  725  TYR B CD2 1 
ATOM   3028 C  CE1 . TYR A 1 448 ? -8.87400  -11.53000 20.32000  1.000 54.49047  ?  725  TYR B CE1 1 
ATOM   3029 C  CE2 . TYR A 1 448 ? -10.50800 -13.24600 20.01100  1.000 60.25063  ?  725  TYR B CE2 1 
ATOM   3030 C  CZ  . TYR A 1 448 ? -9.57300  -12.61600 20.80800  1.000 60.68127  ?  725  TYR B CZ  1 
ATOM   3031 O  OH  . TYR A 1 448 ? -9.33700  -13.07300 22.09600  1.000 58.78169  ?  725  TYR B OH  1 
ATOM   3032 N  N   . VAL A 1 449 ? -9.53900  -13.81700 15.19300  1.000 55.09677  ?  726  VAL B N   1 
ATOM   3033 C  CA  . VAL A 1 449 ? -9.16900  -15.23200 15.14600  1.000 60.60591  ?  726  VAL B CA  1 
ATOM   3034 C  C   . VAL A 1 449 ? -7.79900  -15.40900 14.49400  1.000 57.64700  ?  726  VAL B C   1 
ATOM   3035 O  O   . VAL A 1 449 ? -6.94000  -16.13900 15.00100  1.000 56.61352  ?  726  VAL B O   1 
ATOM   3036 C  CB  . VAL A 1 449 ? -10.24300 -16.06000 14.41400  1.000 62.40741  ?  726  VAL B CB  1 
ATOM   3037 C  CG1 . VAL A 1 449 ? -9.71900  -17.45500 14.13900  1.000 62.88186  ?  726  VAL B CG1 1 
ATOM   3038 C  CG2 . VAL A 1 449 ? -11.50600 -16.13500 15.23200  1.000 66.19820  ?  726  VAL B CG2 1 
ATOM   3039 N  N   . LYS A 1 450 ? -7.58000  -14.75400 13.35100  1.000 59.33136  ?  727  LYS B N   1 
ATOM   3040 C  CA  . LYS A 1 450 ? -6.31000  -14.89700 12.64600  1.000 59.59762  ?  727  LYS B CA  1 
ATOM   3041 C  C   . LYS A 1 450 ? -5.14500  -14.36600 13.47600  1.000 59.43770  ?  727  LYS B C   1 
ATOM   3042 O  O   . LYS A 1 450 ? -4.10700  -15.02900 13.59300  1.000 58.38722  ?  727  LYS B O   1 
ATOM   3043 C  CB  . LYS A 1 450 ? -6.37000  -14.18700 11.29400  1.000 63.08793  ?  727  LYS B CB  1 
ATOM   3044 C  CG  . LYS A 1 450 ? -7.31100  -14.86200 10.30800  1.000 64.59766  ?  727  LYS B CG  1 
ATOM   3045 C  CD  . LYS A 1 450 ? -7.38500  -14.12000 8.99900   1.000 63.78983  ?  727  LYS B CD  1 
ATOM   3046 C  CE  . LYS A 1 450 ? -8.33400  -14.82200 8.04800   1.000 71.81676  ?  727  LYS B CE  1 
ATOM   3047 N  NZ  . LYS A 1 450 ? -8.34600  -14.11800 6.74700   1.000 83.26116  ?  727  LYS B NZ  1 
ATOM   3048 N  N   . SER A 1 451 ? -5.28100  -13.16300 14.05500  1.000 56.64231  ?  728  SER B N   1 
ATOM   3049 C  CA  . SER A 1 451 ? -4.12700  -12.61700 14.77200  1.000 56.04436  ?  728  SER B CA  1 
ATOM   3050 C  C   . SER A 1 451 ? -3.83300  -13.42300 16.03800  1.000 58.57537  ?  728  SER B C   1 
ATOM   3051 O  O   . SER A 1 451 ? -2.65600  -13.58200 16.40100  1.000 57.46663  ?  728  SER B O   1 
ATOM   3052 C  CB  . SER A 1 451 ? -4.31900  -11.12800 15.08800  1.000 49.54775  ?  728  SER B CB  1 
ATOM   3053 O  OG  . SER A 1 451 ? -5.49000  -10.89600 15.85700  1.000 52.62066  ?  728  SER B OG  1 
ATOM   3054 N  N   . CYS A 1 452 ? -4.87100  -13.97000 16.69400  1.000 51.48673  ?  729  CYS B N   1 
ATOM   3055 C  CA  . CYS A 1 452 ? -4.64700  -14.90600 17.79500  1.000 53.59639  ?  729  CYS B CA  1 
ATOM   3056 C  C   . CYS A 1 452 ? -3.86000  -16.12000 17.33000  1.000 52.98428  ?  729  CYS B C   1 
ATOM   3057 O  O   . CYS A 1 452 ? -2.87500  -16.51500 17.95900  1.000 50.31258  ?  729  CYS B O   1 
ATOM   3058 C  CB  . CYS A 1 452 ? -5.97200  -15.37400 18.40600  1.000 58.41653  ?  729  CYS B CB  1 
ATOM   3059 S  SG  . CYS A 1 452 ? -6.90000  -14.16400 19.35300  1.000 58.60685  ?  729  CYS B SG  1 
ATOM   3060 N  N   . ALA A 1 453 ? -4.29700  -16.75000 16.24100  1.000 55.31046  ?  730  ALA B N   1 
ATOM   3061 C  CA  . ALA A 1 453 ? -3.56600  -17.90800 15.73400  1.000 57.00887  ?  730  ALA B CA  1 
ATOM   3062 C  C   . ALA A 1 453 ? -2.12200  -17.54000 15.40300  1.000 54.89146  ?  730  ALA B C   1 
ATOM   3063 O  O   . ALA A 1 453 ? -1.18000  -18.24300 15.79800  1.000 54.55805  ?  730  ALA B O   1 
ATOM   3064 C  CB  . ALA A 1 453 ? -4.27300  -18.48200 14.51300  1.000 60.06107  ?  730  ALA B CB  1 
ATOM   3065 N  N   . GLY A 1 454 ? -1.92700  -16.42400 14.69500  1.000 55.44245  ?  731  GLY B N   1 
ATOM   3066 C  CA  . GLY A 1 454 ? -0.57900  -16.02600 14.32000  1.000 52.95912  ?  731  GLY B CA  1 
ATOM   3067 C  C   . GLY A 1 454 ? 0.31700   -15.82900 15.52800  1.000 50.50091  ?  731  GLY B C   1 
ATOM   3068 O  O   . GLY A 1 454 ? 1.45300   -16.31700 15.56800  1.000 52.41628  ?  731  GLY B O   1 
ATOM   3069 N  N   . TYR A 1 455 ? -0.18500  -15.12200 16.54200  1.000 51.00728  ?  732  TYR B N   1 
ATOM   3070 C  CA  . TYR A 1 455 ? 0.68400   -14.83300 17.67600  1.000 49.43825  ?  732  TYR B CA  1 
ATOM   3071 C  C   . TYR A 1 455 ? 0.88200   -16.05300 18.56300  1.000 50.55420  ?  732  TYR B C   1 
ATOM   3072 O  O   . TYR A 1 455 ? 1.97200   -16.22800 19.11700  1.000 49.90287  ?  732  TYR B O   1 
ATOM   3073 C  CB  . TYR A 1 455 ? 0.16000   -13.62700 18.44900  1.000 47.25077  ?  732  TYR B CB  1 
ATOM   3074 C  CG  . TYR A 1 455 ? 0.64200   -12.33700 17.79600  1.000 47.95119  ?  732  TYR B CG  1 
ATOM   3075 C  CD1 . TYR A 1 455 ? 1.91700   -11.84600 18.04000  1.000 43.13546  ?  732  TYR B CD1 1 
ATOM   3076 C  CD2 . TYR A 1 455 ? -0.16500  -11.63800 16.90100  1.000 41.22386  ?  732  TYR B CD2 1 
ATOM   3077 C  CE1 . TYR A 1 455 ? 2.37700   -10.67300 17.41100  1.000 38.58877  ?  732  TYR B CE1 1 
ATOM   3078 C  CE2 . TYR A 1 455 ? 0.27700   -10.48300 16.29100  1.000 39.90408  ?  732  TYR B CE2 1 
ATOM   3079 C  CZ  . TYR A 1 455 ? 1.54600   -10.00700 16.55100  1.000 41.40762  ?  732  TYR B CZ  1 
ATOM   3080 O  OH  . TYR A 1 455 ? 1.97900   -8.85400  15.93900  1.000 45.89318  ?  732  TYR B OH  1 
ATOM   3081 N  N   . CYS A 1 456 ? -0.12300  -16.93100 18.66400  1.000 50.98018  ?  733  CYS B N   1 
ATOM   3082 C  CA  . CYS A 1 456 ? 0.06400   -18.17300 19.40400  1.000 47.43643  ?  733  CYS B CA  1 
ATOM   3083 C  C   . CYS A 1 456 ? 1.18900   -19.00600 18.81000  1.000 55.32784  ?  733  CYS B C   1 
ATOM   3084 O  O   . CYS A 1 456 ? 1.96600   -19.62600 19.54600  1.000 58.04456  ?  733  CYS B O   1 
ATOM   3085 C  CB  . CYS A 1 456 ? -1.23000  -18.98600 19.44000  1.000 56.77732  ?  733  CYS B CB  1 
ATOM   3086 S  SG  . CYS A 1 456 ? -2.40300  -18.35800 20.68300  1.000 72.25635  ?  733  CYS B SG  1 
ATOM   3087 N  N   . VAL A 1 457 ? 1.28900   -19.04800 17.48000  1.000 56.28402  ?  734  VAL B N   1 
ATOM   3088 C  CA  . VAL A 1 457 ? 2.32800   -19.86200 16.86300  1.000 54.69451  ?  734  VAL B CA  1 
ATOM   3089 C  C   . VAL A 1 457 ? 3.67300   -19.16000 16.96800  1.000 53.67024  ?  734  VAL B C   1 
ATOM   3090 O  O   . VAL A 1 457 ? 4.68500   -19.78400 17.32400  1.000 48.50402  ?  734  VAL B O   1 
ATOM   3091 C  CB  . VAL A 1 457 ? 1.94800   -20.19600 15.40100  1.000 57.74978  ?  734  VAL B CB  1 
ATOM   3092 C  CG1 . VAL A 1 457 ? 3.08100   -20.92800 14.66500  1.000 45.97005  ?  734  VAL B CG1 1 
ATOM   3093 C  CG2 . VAL A 1 457 ? 0.67000   -21.02700 15.38100  1.000 59.22562  ?  734  VAL B CG2 1 
ATOM   3094 N  N   . ILE A 1 458 ? 3.69800   -17.84600 16.70400  1.000 50.35347  ?  735  ILE B N   1 
ATOM   3095 C  CA  . ILE A 1 458 ? 4.97400   -17.13900 16.63800  1.000 52.01913  ?  735  ILE B CA  1 
ATOM   3096 C  C   . ILE A 1 458 ? 5.60700   -17.02200 18.02500  1.000 52.42070  ?  735  ILE B C   1 
ATOM   3097 O  O   . ILE A 1 458 ? 6.81600   -17.24400 18.19400  1.000 55.28429  ?  735  ILE B O   1 
ATOM   3098 C  CB  . ILE A 1 458 ? 4.79000   -15.77600 15.95400  1.000 53.26046  ?  735  ILE B CB  1 
ATOM   3099 C  CG1 . ILE A 1 458 ? 4.55000   -15.99000 14.45900  1.000 48.44877  ?  735  ILE B CG1 1 
ATOM   3100 C  CG2 . ILE A 1 458 ? 6.01400   -14.89500 16.16900  1.000 44.83319  ?  735  ILE B CG2 1 
ATOM   3101 C  CD1 . ILE A 1 458 ? 3.99000   -14.76200 13.73600  1.000 45.44891  ?  735  ILE B CD1 1 
ATOM   3102 N  N   . THR A 1 459 ? 4.81300   -16.71800 19.04700  1.000 52.91268  ?  736  THR B N   1 
ATOM   3103 C  CA  . THR A 1 459 ? 5.40400   -16.63100 20.38000  1.000 51.92859  ?  736  THR B CA  1 
ATOM   3104 C  C   . THR A 1 459 ? 5.80500   -18.00400 20.90700  1.000 52.48577  ?  736  THR B C   1 
ATOM   3105 O  O   . THR A 1 459 ? 6.80400   -18.12400 21.62800  1.000 52.41922  ?  736  THR B O   1 
ATOM   3106 C  CB  . THR A 1 459 ? 4.45700   -15.93600 21.35800  1.000 49.89724  ?  736  THR B CB  1 
ATOM   3107 O  OG1 . THR A 1 459 ? 3.22200   -16.65400 21.43400  1.000 47.26055  ?  736  THR B OG1 1 
ATOM   3108 C  CG2 . THR A 1 459 ? 4.19900   -14.49500 20.90500  1.000 45.57233  ?  736  THR B CG2 1 
ATOM   3109 N  N   . TYR A 1 460 ? 5.06400   -19.05100 20.54900  1.000 53.82739  ?  737  TYR B N   1 
ATOM   3110 C  CA  . TYR A 1 460 ? 5.51900   -20.40100 20.86800  1.000 51.44528  ?  737  TYR B CA  1 
ATOM   3111 C  C   . TYR A 1 460 ? 6.89300   -20.67000 20.25400  1.000 53.18003  ?  737  TYR B C   1 
ATOM   3112 O  O   . TYR A 1 460 ? 7.83300   -21.05400 20.95500  1.000 53.80111  ?  737  TYR B O   1 
ATOM   3113 C  CB  . TYR A 1 460 ? 4.47800   -21.43000 20.40500  1.000 54.01611  ?  737  TYR B CB  1 
ATOM   3114 C  CG  . TYR A 1 460 ? 5.02300   -22.82600 20.19300  1.000 59.31373  ?  737  TYR B CG  1 
ATOM   3115 C  CD1 . TYR A 1 460 ? 5.25600   -23.67300 21.26700  1.000 62.81621  ?  737  TYR B CD1 1 
ATOM   3116 C  CD2 . TYR A 1 460 ? 5.30300   -23.29700 18.91600  1.000 58.82247  ?  737  TYR B CD2 1 
ATOM   3117 C  CE1 . TYR A 1 460 ? 5.75800   -24.95300 21.07600  1.000 66.62309  ?  737  TYR B CE1 1 
ATOM   3118 C  CE2 . TYR A 1 460 ? 5.80700   -24.57600 18.71100  1.000 59.50163  ?  737  TYR B CE2 1 
ATOM   3119 C  CZ  . TYR A 1 460 ? 6.02900   -25.40000 19.79500  1.000 65.30859  ?  737  TYR B CZ  1 
ATOM   3120 O  OH  . TYR A 1 460 ? 6.52000   -26.67400 19.59900  1.000 65.09445  ?  737  TYR B OH  1 
ATOM   3121 N  N   . ILE A 1 461 ? 7.04000   -20.44000 18.94600  1.000 51.98298  ?  738  ILE B N   1 
ATOM   3122 C  CA  . ILE A 1 461 ? 8.31400   -20.71700 18.27800  1.000 52.27778  ?  738  ILE B CA  1 
ATOM   3123 C  C   . ILE A 1 461 ? 9.45600   -19.91400 18.91400  1.000 52.50604  ?  738  ILE B C   1 
ATOM   3124 O  O   . ILE A 1 461 ? 10.55800  -20.44000 19.13500  1.000 45.33015  ?  738  ILE B O   1 
ATOM   3125 C  CB  . ILE A 1 461 ? 8.17700   -20.43500 16.76800  1.000 53.30294  ?  738  ILE B CB  1 
ATOM   3126 C  CG1 . ILE A 1 461 ? 7.36600   -21.54900 16.08900  1.000 53.02492  ?  738  ILE B CG1 1 
ATOM   3127 C  CG2 . ILE A 1 461 ? 9.54300   -20.24600 16.10900  1.000 52.41750  ?  738  ILE B CG2 1 
ATOM   3128 C  CD1 . ILE A 1 461 ? 6.91000   -21.18600 14.69700  1.000 52.57057  ?  738  ILE B CD1 1 
ATOM   3129 N  N   . LEU A 1 462 ? 9.22500   -18.62500 19.19900  1.000 47.95849  ?  739  LEU B N   1 
ATOM   3130 C  CA  . LEU A 1 462 ? 10.26200  -17.78200 19.79400  1.000 48.77784  ?  739  LEU B CA  1 
ATOM   3131 C  C   . LEU A 1 462 ? 10.33900  -17.90900 21.31300  1.000 48.35909  ?  739  LEU B C   1 
ATOM   3132 O  O   . LEU A 1 462 ? 11.17200  -17.23400 21.93400  1.000 42.00155  ?  739  LEU B O   1 
ATOM   3133 C  CB  . LEU A 1 462 ? 10.04300  -16.31100 19.42700  1.000 44.10875  ?  739  LEU B CB  1 
ATOM   3134 C  CG  . LEU A 1 462 ? 9.98500   -16.00400 17.93200  1.000 50.46594  ?  739  LEU B CG  1 
ATOM   3135 C  CD1 . LEU A 1 462 ? 9.70500   -14.52700 17.68500  1.000 46.94792  ?  739  LEU B CD1 1 
ATOM   3136 C  CD2 . LEU A 1 462 ? 11.28700  -16.42300 17.26000  1.000 47.17904  ?  739  LEU B CD2 1 
ATOM   3137 N  N   . GLY A 1 463 ? 9.50800   -18.74500 21.92100  1.000 45.95070  ?  740  GLY B N   1 
ATOM   3138 C  CA  . GLY A 1 463 ? 9.60400   -18.95900 23.35500  1.000 48.55858  ?  740  GLY B CA  1 
ATOM   3139 C  C   . GLY A 1 463 ? 9.48200   -17.69200 24.16900  1.000 48.76131  ?  740  GLY B C   1 
ATOM   3140 O  O   . GLY A 1 463 ? 10.22900  -17.51500 25.13500  1.000 51.02337  ?  740  GLY B O   1 
ATOM   3141 N  N   . VAL A 1 464 ? 8.57200   -16.79000 23.78600  1.000 44.25549  ?  741  VAL B N   1 
ATOM   3142 C  CA  . VAL A 1 464 ? 8.37600   -15.53900 24.51300  1.000 44.39338  ?  741  VAL B CA  1 
ATOM   3143 C  C   . VAL A 1 464 ? 7.74300   -15.81900 25.87200  1.000 47.81295  ?  741  VAL B C   1 
ATOM   3144 O  O   . VAL A 1 464 ? 6.78600   -16.59900 25.97600  1.000 55.57124  ?  741  VAL B O   1 
ATOM   3145 C  CB  . VAL A 1 464 ? 7.49300   -14.58000 23.69300  1.000 48.06211  ?  741  VAL B CB  1 
ATOM   3146 C  CG1 . VAL A 1 464 ? 7.10300   -13.33200 24.54300  1.000 40.89817  ?  741  VAL B CG1 1 
ATOM   3147 C  CG2 . VAL A 1 464 ? 8.17700   -14.17900 22.36100  1.000 42.86372  ?  741  VAL B CG2 1 
ATOM   3148 N  N   . GLY A 1 465 ? 8.27200   -15.19600 26.93100  1.000 46.19973  ?  742  GLY B N   1 
ATOM   3149 C  CA  . GLY A 1 465 ? 7.74200   -15.36500 28.26500  1.000 48.57726  ?  742  GLY B CA  1 
ATOM   3150 C  C   . GLY A 1 465 ? 7.17700   -14.08300 28.85900  1.000 46.98632  ?  742  GLY B C   1 
ATOM   3151 O  O   . GLY A 1 465 ? 7.02400   -13.06800 28.18200  1.000 44.75118  ?  742  GLY B O   1 
ATOM   3152 N  N   . ASP A 1 466 ? 6.88000   -14.14600 30.15000  1.000 55.60380  ?  743  ASP B N   1 
ATOM   3153 C  CA  . ASP A 1 466 ? 6.34500   -12.99900 30.88400  1.000 47.71865  ?  743  ASP B CA  1 
ATOM   3154 C  C   . ASP A 1 466 ? 5.10300   -12.41700 30.21200  1.000 49.90711  ?  743  ASP B C   1 
ATOM   3155 O  O   . ASP A 1 466 ? 4.95300   -11.20600 30.08100  1.000 54.00518  ?  743  ASP B O   1 
ATOM   3156 C  CB  . ASP A 1 466 ? 7.41500   -11.92100 31.06600  1.000 55.28561  ?  743  ASP B CB  1 
ATOM   3157 C  CG  . ASP A 1 466 ? 7.02900   -10.88100 32.11200  1.000 54.89310  ?  743  ASP B CG  1 
ATOM   3158 O  OD1 . ASP A 1 466 ? 6.32300   -11.23800 33.08000  1.000 56.00152  ?  743  ASP B OD1 1 
ATOM   3159 O  OD2 . ASP A 1 466 ? 7.42900   -9.70400  31.95100  1.000 58.29149  -1 743  ASP B OD2 1 
ATOM   3160 N  N   . ARG A 1 467 ? 4.21300   -13.30000 29.76400  1.000 50.08317  ?  744  ARG B N   1 
ATOM   3161 C  CA  . ARG A 1 467 ? 2.99500   -12.91000 29.06800  1.000 44.62961  ?  744  ARG B CA  1 
ATOM   3162 C  C   . ARG A 1 467 ? 1.88600   -12.63800 30.08200  1.000 48.91389  ?  744  ARG B C   1 
ATOM   3163 O  O   . ARG A 1 467 ? 1.53700   -13.52300 30.86400  1.000 55.64046  ?  744  ARG B O   1 
ATOM   3164 C  CB  . ARG A 1 467 ? 2.57000   -14.01300 28.10500  1.000 52.54754  ?  744  ARG B CB  1 
ATOM   3165 C  CG  . ARG A 1 467 ? 3.53800   -14.27800 26.94900  1.000 47.81986  ?  744  ARG B CG  1 
ATOM   3166 C  CD  . ARG A 1 467 ? 3.66900   -13.05800 26.05900  1.000 47.19034  ?  744  ARG B CD  1 
ATOM   3167 N  NE  . ARG A 1 467 ? 4.71500   -12.15100 26.51700  1.000 41.82930  ?  744  ARG B NE  1 
ATOM   3168 C  CZ  . ARG A 1 467 ? 4.87000   -10.91200 26.07300  1.000 45.21651  ?  744  ARG B CZ  1 
ATOM   3169 N  NH1 . ARG A 1 467 ? 4.06100   -10.40000 25.14900  1.000 41.72149  ?  744  ARG B NH1 1 
ATOM   3170 N  NH2 . ARG A 1 467 ? 5.85000   -10.16500 26.57300  1.000 41.35085  ?  744  ARG B NH2 1 
ATOM   3171 N  N   . HIS A 1 468 ? 1.34200   -11.41900 30.08200  1.000 46.80974  ?  745  HIS B N   1 
ATOM   3172 C  CA  . HIS A 1 468 ? 0.21300   -11.05900 30.93900  1.000 47.65725  ?  745  HIS B CA  1 
ATOM   3173 C  C   . HIS A 1 468 ? -0.68100  -10.08900 30.17000  1.000 47.84379  ?  745  HIS B C   1 
ATOM   3174 O  O   . HIS A 1 468 ? -0.36400  -9.67200  29.04200  1.000 50.83397  ?  745  HIS B O   1 
ATOM   3175 C  CB  . HIS A 1 468 ? 0.68400   -10.49300 32.29200  1.000 42.17635  ?  745  HIS B CB  1 
ATOM   3176 C  CG  . HIS A 1 468 ? 1.77000   -9.46200  32.18200  1.000 59.02449  ?  745  HIS B CG  1 
ATOM   3177 N  ND1 . HIS A 1 468 ? 1.58600   -8.23800  31.55900  1.000 58.00560  ?  745  HIS B ND1 1 
ATOM   3178 C  CD2 . HIS A 1 468 ? 3.06300   -9.48000  32.59700  1.000 60.00415  ?  745  HIS B CD2 1 
ATOM   3179 C  CE1 . HIS A 1 468 ? 2.71700   -7.55100  31.59400  1.000 60.41795  ?  745  HIS B CE1 1 
ATOM   3180 N  NE2 . HIS A 1 468 ? 3.63200   -8.28500  32.21000  1.000 65.68566  ?  745  HIS B NE2 1 
ATOM   3181 N  N   . LEU A 1 469 ? -1.81500  -9.72100  30.77300  1.000 45.80571  ?  746  LEU B N   1 
ATOM   3182 C  CA  . LEU A 1 469 ? -2.82200  -8.96200  30.03400  1.000 48.69711  ?  746  LEU B CA  1 
ATOM   3183 C  C   . LEU A 1 469 ? -2.43400  -7.49700  29.82400  1.000 54.45650  ?  746  LEU B C   1 
ATOM   3184 O  O   . LEU A 1 469 ? -3.15000  -6.77000  29.13000  1.000 50.29892  ?  746  LEU B O   1 
ATOM   3185 C  CB  . LEU A 1 469 ? -4.18300  -9.08600  30.73300  1.000 50.18717  ?  746  LEU B CB  1 
ATOM   3186 C  CG  . LEU A 1 469 ? -4.61400  -10.55400 30.86000  1.000 49.30240  ?  746  LEU B CG  1 
ATOM   3187 C  CD1 . LEU A 1 469 ? -5.90700  -10.71100 31.65100  1.000 55.42628  ?  746  LEU B CD1 1 
ATOM   3188 C  CD2 . LEU A 1 469 ? -4.75600  -11.17300 29.47900  1.000 45.12550  ?  746  LEU B CD2 1 
ATOM   3189 N  N   . ASP A 1 470 ? -1.30500  -7.05800  30.36900  1.000 49.61752  ?  747  ASP B N   1 
ATOM   3190 C  CA  . ASP A 1 470 ? -0.76800  -5.74200  30.08200  1.000 45.89025  ?  747  ASP B CA  1 
ATOM   3191 C  C   . ASP A 1 470 ? 0.14300   -5.70600  28.87500  1.000 50.38479  ?  747  ASP B C   1 
ATOM   3192 O  O   . ASP A 1 470 ? 0.38800   -4.61600  28.35800  1.000 51.26733  ?  747  ASP B O   1 
ATOM   3193 C  CB  . ASP A 1 470 ? 0.02400   -5.20800  31.27300  1.000 54.09438  ?  747  ASP B CB  1 
ATOM   3194 C  CG  . ASP A 1 470 ? -0.87300  -4.67500  32.35300  1.000 70.65229  ?  747  ASP B CG  1 
ATOM   3195 O  OD1 . ASP A 1 470 ? -1.83800  -3.96500  31.98300  1.000 74.46429  ?  747  ASP B OD1 1 
ATOM   3196 O  OD2 . ASP A 1 470 ? -0.63700  -4.98500  33.55300  1.000 86.87743  -1 747  ASP B OD2 1 
ATOM   3197 N  N   . ASN A 1 471 ? 0.69700   -6.83400  28.43300  1.000 45.99005  ?  748  ASN B N   1 
ATOM   3198 C  CA  . ASN A 1 471 ? 1.48200   -6.80000  27.20300  1.000 48.40154  ?  748  ASN B CA  1 
ATOM   3199 C  C   . ASN A 1 471 ? 0.82100   -7.61900  26.09900  1.000 45.01028  ?  748  ASN B C   1 
ATOM   3200 O  O   . ASN A 1 471 ? 1.47900   -8.02500  25.13600  1.000 44.90712  ?  748  ASN B O   1 
ATOM   3201 C  CB  . ASN A 1 471 ? 2.94000   -7.23000  27.43300  1.000 44.65569  ?  748  ASN B CB  1 
ATOM   3202 C  CG  . ASN A 1 471 ? 3.07400   -8.52900  28.18800  1.000 48.87941  ?  748  ASN B CG  1 
ATOM   3203 O  OD1 . ASN A 1 471 ? 2.25400   -9.45000  28.05400  1.000 53.85199  ?  748  ASN B OD1 1 
ATOM   3204 N  ND2 . ASN A 1 471 ? 4.10900   -8.60800  29.01100  1.000 52.95800  ?  748  ASN B ND2 1 
ATOM   3205 N  N   . LEU A 1 472 ? -0.47700  -7.85200  26.23500  1.000 47.72098  ?  749  LEU B N   1 
ATOM   3206 C  CA  . LEU A 1 472 ? -1.35400  -8.30500  25.16400  1.000 47.31667  ?  749  LEU B CA  1 
ATOM   3207 C  C   . LEU A 1 472 ? -2.24900  -7.13200  24.79000  1.000 48.01550  ?  749  LEU B C   1 
ATOM   3208 O  O   . LEU A 1 472 ? -2.98100  -6.62500  25.65300  1.000 46.82252  ?  749  LEU B O   1 
ATOM   3209 C  CB  . LEU A 1 472 ? -2.18700  -9.49000  25.63600  1.000 42.88216  ?  749  LEU B CB  1 
ATOM   3210 C  CG  . LEU A 1 472 ? -2.85300  -10.35600 24.58200  1.000 56.61746  ?  749  LEU B CG  1 
ATOM   3211 C  CD1 . LEU A 1 472 ? -1.77700  -11.01100 23.72900  1.000 52.58399  ?  749  LEU B CD1 1 
ATOM   3212 C  CD2 . LEU A 1 472 ? -3.77800  -11.40000 25.23400  1.000 56.40964  ?  749  LEU B CD2 1 
ATOM   3213 N  N   . LEU A 1 473 ? -2.19200  -6.70200  23.52600  1.000 39.89901  ?  750  LEU B N   1 
ATOM   3214 C  CA  . LEU A 1 473 ? -2.86100  -5.47800  23.08700  1.000 45.58260  ?  750  LEU B CA  1 
ATOM   3215 C  C   . LEU A 1 473 ? -3.93000  -5.73100  22.02100  1.000 48.99340  ?  750  LEU B C   1 
ATOM   3216 O  O   . LEU A 1 473 ? -3.86400  -6.68600  21.23400  1.000 48.41014  ?  750  LEU B O   1 
ATOM   3217 C  CB  . LEU A 1 473 ? -1.84500  -4.46200  22.54600  1.000 40.76615  ?  750  LEU B CB  1 
ATOM   3218 C  CG  . LEU A 1 473 ? -1.35200  -3.45700  23.60300  1.000 44.37012  ?  750  LEU B CG  1 
ATOM   3219 C  CD1 . LEU A 1 473 ? -0.80000  -4.13900  24.81800  1.000 42.37964  ?  750  LEU B CD1 1 
ATOM   3220 C  CD2 . LEU A 1 473 ? -0.28800  -2.50300  23.01900  1.000 52.18153  ?  750  LEU B CD2 1 
ATOM   3221 N  N   . LEU A 1 474 ? -4.91000  -4.83000  21.96700  1.000 46.42016  ?  751  LEU B N   1 
ATOM   3222 C  CA  . LEU A 1 474 ? -6.06500  -5.03900  21.10700  1.000 48.00727  ?  751  LEU B CA  1 
ATOM   3223 C  C   . LEU A 1 474 ? -6.39900  -3.76200  20.34200  1.000 47.83635  ?  751  LEU B C   1 
ATOM   3224 O  O   . LEU A 1 474 ? -6.21800  -2.66000  20.86300  1.000 53.65587  ?  751  LEU B O   1 
ATOM   3225 C  CB  . LEU A 1 474 ? -7.25800  -5.49000  21.95700  1.000 52.50459  ?  751  LEU B CB  1 
ATOM   3226 C  CG  . LEU A 1 474 ? -8.33900  -6.27700  21.24200  1.000 58.09373  ?  751  LEU B CG  1 
ATOM   3227 C  CD1 . LEU A 1 474 ? -7.68700  -7.47700  20.56800  1.000 56.80700  ?  751  LEU B CD1 1 
ATOM   3228 C  CD2 . LEU A 1 474 ? -9.40700  -6.69300  22.24600  1.000 55.46992  ?  751  LEU B CD2 1 
ATOM   3229 N  N   . THR A 1 475 ? -6.88800  -3.90900  19.11000  1.000 47.23244  ?  752  THR B N   1 
ATOM   3230 C  CA  . THR A 1 475 ? -7.41400  -2.78400  18.34500  1.000 52.93699  ?  752  THR B CA  1 
ATOM   3231 C  C   . THR A 1 475 ? -8.91600  -2.95000  18.11200  1.000 56.71045  ?  752  THR B C   1 
ATOM   3232 O  O   . THR A 1 475 ? -9.46700  -4.05100  18.18900  1.000 58.05261  ?  752  THR B O   1 
ATOM   3233 C  CB  . THR A 1 475 ? -6.71300  -2.62200  16.98700  1.000 51.31425  ?  752  THR B CB  1 
ATOM   3234 O  OG1 . THR A 1 475 ? -7.20900  -3.60500  16.06400  1.000 54.65328  ?  752  THR B OG1 1 
ATOM   3235 C  CG2 . THR A 1 475 ? -5.19600  -2.72700  17.10700  1.000 44.99815  ?  752  THR B CG2 1 
ATOM   3236 N  N   . LYS A 1 476 ? -9.58100  -1.82700  17.83400  1.000 54.76722  ?  753  LYS B N   1 
ATOM   3237 C  CA  . LYS A 1 476 ? -10.99900 -1.84000  17.50900  1.000 61.93972  ?  753  LYS B CA  1 
ATOM   3238 C  C   . LYS A 1 476 ? -11.27900 -2.57400  16.20300  1.000 59.45055  ?  753  LYS B C   1 
ATOM   3239 O  O   . LYS A 1 476 ? -12.40100 -3.04600  16.00200  1.000 61.21267  ?  753  LYS B O   1 
ATOM   3240 C  CB  . LYS A 1 476 ? -11.54000 -0.40500  17.45200  1.000 64.63837  ?  753  LYS B CB  1 
ATOM   3241 C  CG  . LYS A 1 476 ? -11.58600 0.27400   18.81400  1.000 66.54992  ?  753  LYS B CG  1 
ATOM   3242 C  CD  . LYS A 1 476 ? -11.67800 1.79500   18.71800  1.000 73.67352  ?  753  LYS B CD  1 
ATOM   3243 C  CE  . LYS A 1 476 ? -11.50000 2.45100   20.10000  1.000 80.68962  ?  753  LYS B CE  1 
ATOM   3244 N  NZ  . LYS A 1 476 ? -12.09600 3.82600   20.18600  1.000 88.45084  ?  753  LYS B NZ  1 
ATOM   3245 N  N   . THR A 1 477 ? -10.28500 -2.71400  15.33100  1.000 57.13793  ?  754  THR B N   1 
ATOM   3246 C  CA  . THR A 1 477 ? -10.44500 -3.51500  14.12300  1.000 60.98124  ?  754  THR B CA  1 
ATOM   3247 C  C   . THR A 1 477 ? -10.33800 -5.01400  14.39000  1.000 59.67153  ?  754  THR B C   1 
ATOM   3248 O  O   . THR A 1 477 ? -10.49500 -5.80900  13.45200  1.000 60.07965  ?  754  THR B O   1 
ATOM   3249 C  CB  . THR A 1 477 ? -9.39900  -3.10600  13.07700  1.000 52.78055  ?  754  THR B CB  1 
ATOM   3250 O  OG1 . THR A 1 477 ? -8.09000  -3.29400  13.62200  1.000 61.44154  ?  754  THR B OG1 1 
ATOM   3251 C  CG2 . THR A 1 477 ? -9.56200  -1.65900  12.70300  1.000 48.67326  ?  754  THR B CG2 1 
ATOM   3252 N  N   . GLY A 1 478 ? -10.05900 -5.41800  15.62900  1.000 53.89865  ?  755  GLY B N   1 
ATOM   3253 C  CA  . GLY A 1 478 ? -9.97500  -6.81900  15.98200  1.000 52.98932  ?  755  GLY B CA  1 
ATOM   3254 C  C   . GLY A 1 478 ? -8.57600  -7.40100  16.04100  1.000 54.38088  ?  755  GLY B C   1 
ATOM   3255 O  O   . GLY A 1 478 ? -8.44000  -8.60500  16.28300  1.000 53.81738  ?  755  GLY B O   1 
ATOM   3256 N  N   . LYS A 1 479 ? -7.53500  -6.59500  15.82200  1.000 51.23233  ?  756  LYS B N   1 
ATOM   3257 C  CA  . LYS A 1 479 ? -6.17200  -7.10400  15.86600  1.000 49.45727  ?  756  LYS B CA  1 
ATOM   3258 C  C   . LYS A 1 479 ? -5.72500  -7.29000  17.32200  1.000 51.14348  ?  756  LYS B C   1 
ATOM   3259 O  O   . LYS A 1 479 ? -5.84800  -6.38100  18.15300  1.000 54.35109  ?  756  LYS B O   1 
ATOM   3260 C  CB  . LYS A 1 479 ? -5.19800  -6.16500  15.13800  1.000 49.65419  ?  756  LYS B CB  1 
ATOM   3261 C  CG  . LYS A 1 479 ? -5.37400  -6.00900  13.61500  1.000 53.63491  ?  756  LYS B CG  1 
ATOM   3262 C  CD  . LYS A 1 479 ? -4.09200  -5.46500  12.94400  1.000 56.10699  ?  756  LYS B CD  1 
ATOM   3263 C  CE  . LYS A 1 479 ? -4.29400  -5.27400  11.45100  1.000 81.68915  ?  756  LYS B CE  1 
ATOM   3264 N  NZ  . LYS A 1 479 ? -3.03700  -4.84100  10.73800  1.000 87.98478  ?  756  LYS B NZ  1 
ATOM   3265 N  N   . LEU A 1 480 ? -5.22200  -8.47600  17.62300  1.000 44.88129  ?  757  LEU B N   1 
ATOM   3266 C  CA  . LEU A 1 480 ? -4.54400  -8.76200  18.86900  1.000 45.09668  ?  757  LEU B CA  1 
ATOM   3267 C  C   . LEU A 1 480 ? -3.06500  -8.89900  18.56700  1.000 47.83552  ?  757  LEU B C   1 
ATOM   3268 O  O   . LEU A 1 480 ? -2.69300  -9.45300  17.52700  1.000 50.07590  ?  757  LEU B O   1 
ATOM   3269 C  CB  . LEU A 1 480 ? -5.07400  -10.04400 19.51000  1.000 50.08895  ?  757  LEU B CB  1 
ATOM   3270 C  CG  . LEU A 1 480 ? -4.30800  -10.53500 20.73200  1.000 55.96730  ?  757  LEU B CG  1 
ATOM   3271 C  CD1 . LEU A 1 480 ? -5.24700  -11.12700 21.79200  1.000 55.25906  ?  757  LEU B CD1 1 
ATOM   3272 C  CD2 . LEU A 1 480 ? -3.26100  -11.53400 20.28100  1.000 50.02271  ?  757  LEU B CD2 1 
ATOM   3273 N  N   . PHE A 1 481 ? -2.22000  -8.37700  19.45600  1.000 43.10894  ?  758  PHE B N   1 
ATOM   3274 C  CA  . PHE A 1 481 ? -0.78900  -8.51800  19.24800  1.000 39.60061  ?  758  PHE B CA  1 
ATOM   3275 C  C   . PHE A 1 481 ? -0.07000  -8.35000  20.58200  1.000 44.48412  ?  758  PHE B C   1 
ATOM   3276 O  O   . PHE A 1 481 ? -0.65300  -7.91200  21.57500  1.000 42.75880  ?  758  PHE B O   1 
ATOM   3277 C  CB  . PHE A 1 481 ? -0.28700  -7.53300  18.17400  1.000 41.82092  ?  758  PHE B CB  1 
ATOM   3278 C  CG  . PHE A 1 481 ? -0.39600  -6.07500  18.56600  1.000 40.85044  ?  758  PHE B CG  1 
ATOM   3279 C  CD1 . PHE A 1 481 ? -1.58300  -5.38200  18.37300  1.000 41.04970  ?  758  PHE B CD1 1 
ATOM   3280 C  CD2 . PHE A 1 481 ? 0.69300   -5.39500  19.10400  1.000 39.05251  ?  758  PHE B CD2 1 
ATOM   3281 C  CE1 . PHE A 1 481 ? -1.69400  -4.04900  18.72600  1.000 41.76372  ?  758  PHE B CE1 1 
ATOM   3282 C  CE2 . PHE A 1 481 ? 0.59400   -4.03900  19.44400  1.000 40.41955  ?  758  PHE B CE2 1 
ATOM   3283 C  CZ  . PHE A 1 481 ? -0.60800  -3.37000  19.25300  1.000 41.76711  ?  758  PHE B CZ  1 
ATOM   3284 N  N   . HIS A 1 482 ? 1.21000   -8.73900  20.60200  1.000 38.87679  ?  759  HIS B N   1 
ATOM   3285 C  CA  . HIS A 1 482 ? 1.99700   -8.70400  21.86400  1.000 39.88394  ?  759  HIS B CA  1 
ATOM   3286 C  C   . HIS A 1 482 ? 3.04500   -7.59000  21.82700  1.000 44.70426  ?  759  HIS B C   1 
ATOM   3287 O  O   . HIS A 1 482 ? 3.38100   -7.10400  20.72800  1.000 43.13352  ?  759  HIS B O   1 
ATOM   3288 C  CB  . HIS A 1 482 ? 2.71100   -10.04200 22.08400  1.000 41.83943  ?  759  HIS B CB  1 
ATOM   3289 C  CG  . HIS A 1 482 ? 1.81100   -11.22400 22.21200  1.000 48.71364  ?  759  HIS B CG  1 
ATOM   3290 N  ND1 . HIS A 1 482 ? 1.80400   -12.02700 23.33200  1.000 47.45663  ?  759  HIS B ND1 1 
ATOM   3291 C  CD2 . HIS A 1 482 ? 0.91000   -11.75000 21.37400  1.000 52.76612  ?  759  HIS B CD2 1 
ATOM   3292 C  CE1 . HIS A 1 482 ? 0.91900   -12.99800 23.16700  1.000 49.39719  ?  759  HIS B CE1 1 
ATOM   3293 N  NE2 . HIS A 1 482 ? 0.36400   -12.84900 21.98400  1.000 49.73559  ?  759  HIS B NE2 1 
ATOM   3294 N  N   . ILE A 1 483 ? 3.56000   -7.21100  23.00000  1.000 41.74177  ?  760  ILE B N   1 
ATOM   3295 C  CA  . ILE A 1 483 ? 4.60300   -6.14700  23.09000  1.000 40.22038  ?  760  ILE B CA  1 
ATOM   3296 C  C   . ILE A 1 483 ? 5.55400   -6.49300  24.24100  1.000 48.44770  ?  760  ILE B C   1 
ATOM   3297 O  O   . ILE A 1 483 ? 5.28000   -7.48600  24.94000  1.000 42.67992  ?  760  ILE B O   1 
ATOM   3298 C  CB  . ILE A 1 483 ? 3.95600   -4.76300  23.29500  1.000 40.71899  ?  760  ILE B CB  1 
ATOM   3299 C  CG1 . ILE A 1 483 ? 3.17600   -4.69300  24.61100  1.000 45.73307  ?  760  ILE B CG1 1 
ATOM   3300 C  CG2 . ILE A 1 483 ? 3.09000   -4.37800  22.10400  1.000 34.41822  ?  760  ILE B CG2 1 
ATOM   3301 C  CD1 . ILE A 1 483 ? 2.61400   -3.32600  24.92000  1.000 49.84974  ?  760  ILE B CD1 1 
ATOM   3302 N  N   . ASP A 1 484 ? 6.62300   -5.71000  24.42200  1.000 46.24783  ?  761  ASP B N   1 
ATOM   3303 C  CA  . ASP A 1 484 ? 7.57200   -5.91600  25.55300  1.000 47.95244  ?  761  ASP B CA  1 
ATOM   3304 C  C   . ASP A 1 484 ? 8.14000   -7.33900  25.52200  1.000 48.66799  ?  761  ASP B C   1 
ATOM   3305 O  O   . ASP A 1 484 ? 7.65600   -8.18100  26.29500  1.000 47.56922  ?  761  ASP B O   1 
ATOM   3306 C  CB  . ASP A 1 484 ? 6.91800   -5.59700  26.90000  1.000 47.97298  ?  761  ASP B CB  1 
ATOM   3307 C  CG  . ASP A 1 484 ? 7.88200   -5.67100  28.07100  1.000 46.65989  ?  761  ASP B CG  1 
ATOM   3308 N  N   . PHE A 1 485 ? 9.15500   -7.57800  24.69100  1.000 41.04988  ?  762  PHE B N   1 
ATOM   3309 C  CA  . PHE A 1 485 ? 9.75000   -8.90000  24.58600  1.000 42.86584  ?  762  PHE B CA  1 
ATOM   3310 C  C   . PHE A 1 485 ? 11.02700  -8.98400  25.42100  1.000 37.04116  ?  762  PHE B C   1 
ATOM   3311 O  O   . PHE A 1 485 ? 12.10800  -9.26000  24.92700  1.000 47.14631  ?  762  PHE B O   1 
ATOM   3312 C  CB  . PHE A 1 485 ? 9.99200   -9.22700  23.11200  1.000 44.64779  ?  762  PHE B CB  1 
ATOM   3313 C  CG  . PHE A 1 485 ? 8.72900   -9.20700  22.29200  1.000 44.66770  ?  762  PHE B CG  1 
ATOM   3314 C  CD1 . PHE A 1 485 ? 7.85200   -10.28800 22.32800  1.000 38.88797  ?  762  PHE B CD1 1 
ATOM   3315 C  CD2 . PHE A 1 485 ? 8.40200   -8.10100  21.51100  1.000 39.43021  ?  762  PHE B CD2 1 
ATOM   3316 C  CE1 . PHE A 1 485 ? 6.68800   -10.28300 21.59200  1.000 38.15486  ?  762  PHE B CE1 1 
ATOM   3317 C  CE2 . PHE A 1 485 ? 7.23300   -8.08700  20.75700  1.000 41.42795  ?  762  PHE B CE2 1 
ATOM   3318 C  CZ  . PHE A 1 485 ? 6.36900   -9.18300  20.79600  1.000 41.34649  ?  762  PHE B CZ  1 
ATOM   3319 N  N   . GLY A 1 486 ? 10.88600  -8.74200  26.72300  1.000 44.58172  ?  763  GLY B N   1 
ATOM   3320 C  CA  . GLY A 1 486 ? 12.03900  -8.82500  27.60200  1.000 41.54933  ?  763  GLY B CA  1 
ATOM   3321 C  C   . GLY A 1 486 ? 12.43000  -10.22700 27.98900  1.000 43.40944  ?  763  GLY B C   1 
ATOM   3322 O  O   . GLY A 1 486 ? 13.50800  -10.41800 28.54700  1.000 43.89531  ?  763  GLY B O   1 
ATOM   3323 N  N   . TYR A 1 487 ? 11.58000  -11.21200 27.70600  1.000 42.48190  ?  764  TYR B N   1 
ATOM   3324 C  CA  . TYR A 1 487 ? 11.81400  -12.60700 28.05600  1.000 46.44861  ?  764  TYR B CA  1 
ATOM   3325 C  C   . TYR A 1 487 ? 11.53400  -13.45500 26.82100  1.000 48.72411  ?  764  TYR B C   1 
ATOM   3326 O  O   . TYR A 1 487 ? 10.37100  -13.59200 26.41900  1.000 46.33922  ?  764  TYR B O   1 
ATOM   3327 C  CB  . TYR A 1 487 ? 10.90700  -13.04900 29.20700  1.000 42.83086  ?  764  TYR B CB  1 
ATOM   3328 C  CG  . TYR A 1 487 ? 11.24600  -12.46100 30.53700  1.000 53.97250  ?  764  TYR B CG  1 
ATOM   3329 C  CD1 . TYR A 1 487 ? 10.82000  -11.18200 30.88500  1.000 55.00097  ?  764  TYR B CD1 1 
ATOM   3330 C  CD2 . TYR A 1 487 ? 11.95900  -13.19600 31.47300  1.000 56.30110  ?  764  TYR B CD2 1 
ATOM   3331 C  CE1 . TYR A 1 487 ? 11.10900  -10.65400 32.12500  1.000 54.20615  ?  764  TYR B CE1 1 
ATOM   3332 C  CE2 . TYR A 1 487 ? 12.25100  -12.68200 32.70600  1.000 61.07327  ?  764  TYR B CE2 1 
ATOM   3333 C  CZ  . TYR A 1 487 ? 11.83000  -11.40900 33.03000  1.000 61.90442  ?  764  TYR B CZ  1 
ATOM   3334 O  OH  . TYR A 1 487 ? 12.13000  -10.89300 34.26500  1.000 66.59709  ?  764  TYR B OH  1 
ATOM   3335 N  N   . ILE A 1 488 ? 12.57800  -14.05500 26.24500  1.000 45.68152  ?  765  ILE B N   1 
ATOM   3336 C  CA  . ILE A 1 488 ? 12.46000  -14.81800 25.01100  1.000 48.11307  ?  765  ILE B CA  1 
ATOM   3337 C  C   . ILE A 1 488 ? 13.24400  -16.12200 25.14300  1.000 53.37819  ?  765  ILE B C   1 
ATOM   3338 O  O   . ILE A 1 488 ? 13.90000  -16.38900 26.15700  1.000 49.63276  ?  765  ILE B O   1 
ATOM   3339 C  CB  . ILE A 1 488 ? 12.92900  -14.01600 23.77600  1.000 46.12394  ?  765  ILE B CB  1 
ATOM   3340 C  CG1 . ILE A 1 488 ? 14.43700  -13.76600 23.82100  1.000 47.61626  ?  765  ILE B CG1 1 
ATOM   3341 C  CG2 . ILE A 1 488 ? 12.17300  -12.69700 23.64000  1.000 41.60297  ?  765  ILE B CG2 1 
ATOM   3342 C  CD1 . ILE A 1 488 ? 14.94700  -12.96300 22.64500  1.000 42.02125  ?  765  ILE B CD1 1 
ATOM   3343 N  N   . LEU A 1 489 ? 13.15900  -16.95100 24.10000  1.000 49.52709  ?  766  LEU B N   1 
ATOM   3344 C  CA  . LEU A 1 489 ? 13.88700  -18.21400 24.03600  1.000 49.55476  ?  766  LEU B CA  1 
ATOM   3345 C  C   . LEU A 1 489 ? 13.73300  -19.00500 25.32300  1.000 54.45406  ?  766  LEU B C   1 
ATOM   3346 O  O   . LEU A 1 489 ? 14.68600  -19.60400 25.83100  1.000 56.20059  ?  766  LEU B O   1 
ATOM   3347 C  CB  . LEU A 1 489 ? 15.36300  -17.97900 23.71700  1.000 53.65052  ?  766  LEU B CB  1 
ATOM   3348 C  CG  . LEU A 1 489 ? 15.56100  -17.26200 22.38200  1.000 53.66360  ?  766  LEU B CG  1 
ATOM   3349 C  CD1 . LEU A 1 489 ? 16.94800  -16.64600 22.30400  1.000 53.41120  ?  766  LEU B CD1 1 
ATOM   3350 C  CD2 . LEU A 1 489 ? 15.31500  -18.23500 21.22800  1.000 51.54117  ?  766  LEU B CD2 1 
ATOM   3351 N  N   . GLY A 1 490 ? 12.52600  -18.98600 25.88100  1.000 52.99494  ?  767  GLY B N   1 
ATOM   3352 C  CA  . GLY A 1 490 ? 12.19500  -19.86300 26.98000  1.000 48.67952  ?  767  GLY B CA  1 
ATOM   3353 C  C   . GLY A 1 490 ? 12.45600  -19.30500 28.36000  1.000 58.60189  ?  767  GLY B C   1 
ATOM   3354 O  O   . GLY A 1 490 ? 12.09900  -19.95600 29.35300  1.000 57.71644  ?  767  GLY B O   1 
ATOM   3355 N  N   . ARG A 1 491 ? 13.07500  -18.13500 28.47300  1.000 56.92989  ?  768  ARG B N   1 
ATOM   3356 C  CA  . ARG A 1 491 ? 13.20900  -17.55200 29.79600  1.000 54.43923  ?  768  ARG B CA  1 
ATOM   3357 C  C   . ARG A 1 491 ? 11.86300  -16.98300 30.23300  1.000 56.35522  ?  768  ARG B C   1 
ATOM   3358 O  O   . ARG A 1 491 ? 11.05900  -16.51300 29.41900  1.000 58.04146  ?  768  ARG B O   1 
ATOM   3359 C  CB  . ARG A 1 491 ? 14.29200  -16.47400 29.82200  1.000 56.43218  ?  768  ARG B CB  1 
ATOM   3360 C  CG  . ARG A 1 491 ? 14.86600  -16.24000 31.22400  1.000 60.89663  ?  768  ARG B CG  1 
ATOM   3361 C  CD  . ARG A 1 491 ? 16.09100  -15.34100 31.18100  1.000 63.38665  ?  768  ARG B CD  1 
ATOM   3362 N  NE  . ARG A 1 491 ? 15.73300  -14.02000 30.67900  1.000 69.92880  ?  768  ARG B NE  1 
ATOM   3363 C  CZ  . ARG A 1 491 ? 15.43200  -12.97700 31.44700  1.000 68.01195  ?  768  ARG B CZ  1 
ATOM   3364 N  NH1 . ARG A 1 491 ? 15.52600  -13.03300 32.76300  1.000 69.65520  ?  768  ARG B NH1 1 
ATOM   3365 N  NH2 . ARG A 1 491 ? 15.02100  -11.84800 30.88000  1.000 56.96871  ?  768  ARG B NH2 1 
ATOM   3366 N  N   . ASP A 1 492 ? 11.60400  -17.06500 31.53500  1.000 58.50143  ?  769  ASP B N   1 
ATOM   3367 C  CA  . ASP A 1 492 ? 10.33400  -16.62300 32.07900  1.000 59.40622  ?  769  ASP B CA  1 
ATOM   3368 C  C   . ASP A 1 492 ? 10.51200  -16.30700 33.55000  1.000 66.93765  ?  769  ASP B C   1 
ATOM   3369 O  O   . ASP A 1 492 ? 11.31300  -16.97600 34.21900  1.000 65.46506  ?  769  ASP B O   1 
ATOM   3370 C  CB  . ASP A 1 492 ? 9.24800   -17.69000 31.90300  1.000 60.56256  ?  769  ASP B CB  1 
ATOM   3371 C  CG  . ASP A 1 492 ? 7.86200   -17.14800 32.18100  1.000 65.81879  ?  769  ASP B CG  1 
ATOM   3372 O  OD1 . ASP A 1 492 ? 7.53200   -17.00000 33.38100  1.000 70.16274  ?  769  ASP B OD1 1 
ATOM   3373 O  OD2 . ASP A 1 492 ? 7.13000   -16.83700 31.21000  1.000 59.09742  -1 769  ASP B OD2 1 
ATOM   3374 N  N   . PRO A 1 493 ? 9.81000   -15.30700 34.08500  1.000 65.70241  ?  770  PRO B N   1 
ATOM   3375 C  CA  . PRO A 1 493 ? 9.86800   -15.08400 35.53800  1.000 63.08884  ?  770  PRO B CA  1 
ATOM   3376 C  C   . PRO A 1 493 ? 9.40900   -16.28200 36.34300  1.000 67.56671  ?  770  PRO B C   1 
ATOM   3377 O  O   . PRO A 1 493 ? 9.95800   -16.53900 37.42300  1.000 73.13120  ?  770  PRO B O   1 
ATOM   3378 C  CB  . PRO A 1 493 ? 8.94700   -13.87700 35.73800  1.000 63.31951  ?  770  PRO B CB  1 
ATOM   3379 C  CG  . PRO A 1 493 ? 8.95500   -13.16800 34.42600  1.000 62.21813  ?  770  PRO B CG  1 
ATOM   3380 C  CD  . PRO A 1 493 ? 9.12900   -14.21500 33.36500  1.000 64.41155  ?  770  PRO B CD  1 
ATOM   3381 N  N   . LYS A 1 494 ? 8.43900   -17.04400 35.84500  1.000 68.55976  ?  771  LYS B N   1 
ATOM   3382 C  CA  . LYS A 1 494 ? 7.97500   -18.20000 36.59900  1.000 75.33154  ?  771  LYS B CA  1 
ATOM   3383 C  C   . LYS A 1 494 ? 8.60000   -19.49700 36.08800  1.000 76.03379  ?  771  LYS B C   1 
ATOM   3384 O  O   . LYS A 1 494 ? 8.93300   -19.62100 34.90700  1.000 81.10469  ?  771  LYS B O   1 
ATOM   3385 C  CB  . LYS A 1 494 ? 6.45200   -18.31300 36.51200  1.000 78.56617  ?  771  LYS B CB  1 
ATOM   3386 C  CG  . LYS A 1 494 ? 5.72300   -17.20400 37.22300  1.000 76.00108  ?  771  LYS B CG  1 
ATOM   3387 C  CD  . LYS A 1 494 ? 4.56200   -16.70500 36.38000  1.000 81.46725  ?  771  LYS B CD  1 
ATOM   3388 N  N   . PRO A 1 495 ? 8.77600   -20.49700 36.94000  1.000 80.79362  ?  772  PRO B N   1 
ATOM   3389 C  CA  . PRO A 1 495 ? 9.21800   -21.80400 36.45500  1.000 80.30489  ?  772  PRO B CA  1 
ATOM   3390 C  C   . PRO A 1 495 ? 8.02600   -22.60900 35.96900  1.000 85.54651  ?  772  PRO B C   1 
ATOM   3391 O  O   . PRO A 1 495 ? 6.91300   -22.49300 36.48800  1.000 94.94184  ?  772  PRO B O   1 
ATOM   3392 C  CB  . PRO A 1 495 ? 9.82900   -22.44200 37.70300  1.000 85.55081  ?  772  PRO B CB  1 
ATOM   3393 C  CG  . PRO A 1 495 ? 8.91500   -21.94300 38.79900  1.000 83.94791  ?  772  PRO B CG  1 
ATOM   3394 C  CD  . PRO A 1 495 ? 8.49600   -20.52000 38.38700  1.000 79.42454  ?  772  PRO B CD  1 
ATOM   3395 N  N   . LEU A 1 496 ? 8.26600   -23.42900 34.95000  1.000 88.97947  ?  773  LEU B N   1 
ATOM   3396 C  CA  . LEU A 1 496 ? 7.19800   -24.25100 34.38200  1.000 89.96746  ?  773  LEU B CA  1 
ATOM   3397 C  C   . LEU A 1 496 ? 6.13000   -23.38800 33.70800  1.000 89.83653  ?  773  LEU B C   1 
ATOM   3398 O  O   . LEU A 1 496 ? 4.93300   -23.55000 33.99000  1.000 93.22544  ?  773  LEU B O   1 
ATOM   3399 C  CB  . LEU A 1 496 ? 6.56700   -25.13300 35.47200  1.000 91.21748  ?  773  LEU B CB  1 
ATOM   3400 N  N   . PRO A 1 497 ? 6.50600   -22.45800 32.82700  1.000 81.04667  ?  774  PRO B N   1 
ATOM   3401 C  CA  . PRO A 1 497 ? 5.49100   -21.71900 32.07900  1.000 82.75735  ?  774  PRO B CA  1 
ATOM   3402 C  C   . PRO A 1 497 ? 4.82800   -22.61000 31.04000  1.000 83.70106  ?  774  PRO B C   1 
ATOM   3403 O  O   . PRO A 1 497 ? 5.43500   -23.58200 30.55800  1.000 81.59493  ?  774  PRO B O   1 
ATOM   3404 C  CB  . PRO A 1 497 ? 6.29500   -20.58600 31.41600  1.000 75.66187  ?  774  PRO B CB  1 
ATOM   3405 C  CG  . PRO A 1 497 ? 7.67500   -21.15600 31.27300  1.000 75.45175  ?  774  PRO B CG  1 
ATOM   3406 C  CD  . PRO A 1 497 ? 7.87300   -22.00100 32.50400  1.000 75.76155  ?  774  PRO B CD  1 
ATOM   3407 N  N   . PRO A 1 498 ? 3.58200   -22.31400 30.66000  1.000 82.87464  ?  775  PRO B N   1 
ATOM   3408 C  CA  . PRO A 1 498 ? 2.91400   -23.14300 29.64900  1.000 82.54004  ?  775  PRO B CA  1 
ATOM   3409 C  C   . PRO A 1 498 ? 3.51600   -22.91100 28.28000  1.000 81.87582  ?  775  PRO B C   1 
ATOM   3410 O  O   . PRO A 1 498 ? 3.95300   -21.79200 27.95300  1.000 76.43386  ?  775  PRO B O   1 
ATOM   3411 C  CB  . PRO A 1 498 ? 1.45100   -22.66400 29.71500  1.000 80.30387  ?  775  PRO B CB  1 
ATOM   3412 C  CG  . PRO A 1 498 ? 1.53800   -21.25100 30.16100  1.000 81.32584  ?  775  PRO B CG  1 
ATOM   3413 C  CD  . PRO A 1 498 ? 2.74400   -21.17300 31.08400  1.000 80.41148  ?  775  PRO B CD  1 
ATOM   3414 N  N   . PRO A 1 499 ? 3.57700   -23.94400 27.43400  1.000 83.49127  ?  776  PRO B N   1 
ATOM   3415 C  CA  . PRO A 1 499 ? 4.28300   -23.79000 26.15000  1.000 77.37686  ?  776  PRO B CA  1 
ATOM   3416 C  C   . PRO A 1 499 ? 3.51000   -22.95300 25.15500  1.000 74.36152  ?  776  PRO B C   1 
ATOM   3417 O  O   . PRO A 1 499 ? 4.11400   -22.18100 24.39900  1.000 79.29106  ?  776  PRO B O   1 
ATOM   3418 C  CB  . PRO A 1 499 ? 4.44700   -25.23700 25.67300  1.000 86.71866  ?  776  PRO B CB  1 
ATOM   3419 C  CG  . PRO A 1 499 ? 3.23300   -25.96000 26.27400  1.000 83.42223  ?  776  PRO B CG  1 
ATOM   3420 C  CD  . PRO A 1 499 ? 2.94700   -25.27400 27.58900  1.000 80.57013  ?  776  PRO B CD  1 
ATOM   3421 N  N   . MET A 1 500 ? 2.18700   -23.09500 25.12400  1.000 77.58410  ?  777  MET B N   1 
ATOM   3422 C  CA  . MET A 1 500 ? 1.32400   -22.26300 24.29400  1.000 77.21092  ?  777  MET B CA  1 
ATOM   3423 C  C   . MET A 1 500 ? 0.87500   -21.05600 25.10900  1.000 76.17916  ?  777  MET B C   1 
ATOM   3424 O  O   . MET A 1 500 ? 0.20200   -21.20700 26.13800  1.000 85.05010  ?  777  MET B O   1 
ATOM   3425 C  CB  . MET A 1 500 ? 0.11400   -23.05900 23.80500  1.000 79.04493  ?  777  MET B CB  1 
ATOM   3426 C  CG  . MET A 1 500 ? 0.19600   -23.50600 22.37600  1.000 81.65954  ?  777  MET B CG  1 
ATOM   3427 S  SD  . MET A 1 500 ? 0.09100   -22.09900 21.25800  1.000 92.48643  ?  777  MET B SD  1 
ATOM   3428 C  CE  . MET A 1 500 ? 0.57200   -22.89500 19.72700  1.000 74.16655  ?  777  MET B CE  1 
ATOM   3429 N  N   . LYS A 1 501 ? 1.24800   -19.86300 24.65800  1.000 80.08765  ?  778  LYS B N   1 
ATOM   3430 C  CA  . LYS A 1 501 ? 0.87500   -18.62500 25.34700  1.000 78.70767  ?  778  LYS B CA  1 
ATOM   3431 C  C   . LYS A 1 501 ? -0.55400  -18.24400 24.95300  1.000 73.96486  ?  778  LYS B C   1 
ATOM   3432 O  O   . LYS A 1 501 ? -0.81000  -17.30000 24.20400  1.000 79.92350  ?  778  LYS B O   1 
ATOM   3433 C  CB  . LYS A 1 501 ? 1.88100   -17.51800 25.03900  1.000 74.83160  ?  778  LYS B CB  1 
ATOM   3434 C  CG  . LYS A 1 501 ? 3.21600   -17.71500 25.76700  1.000 71.66962  ?  778  LYS B CG  1 
ATOM   3435 C  CD  . LYS A 1 501 ? 2.96100   -18.14100 27.21300  1.000 65.41738  ?  778  LYS B CD  1 
ATOM   3436 C  CE  . LYS A 1 501 ? 4.24800   -18.27600 27.98700  1.000 66.96921  ?  778  LYS B CE  1 
ATOM   3437 N  NZ  . LYS A 1 501 ? 5.04500   -19.39100 27.46500  1.000 73.34444  ?  778  LYS B NZ  1 
ATOM   3438 N  N   . LEU A 1 502 ? -1.50000  -19.02200 25.48200  1.000 80.64968  ?  779  LEU B N   1 
ATOM   3439 C  CA  . LEU A 1 502 ? -2.92700  -18.85100 25.24300  1.000 80.24057  ?  779  LEU B CA  1 
ATOM   3440 C  C   . LEU A 1 502 ? -3.64200  -18.80100 26.58400  1.000 77.42039  ?  779  LEU B C   1 
ATOM   3441 O  O   . LEU A 1 502 ? -3.33000  -19.59700 27.47500  1.000 81.58544  ?  779  LEU B O   1 
ATOM   3442 C  CB  . LEU A 1 502 ? -3.47300  -20.01000 24.39700  1.000 78.95288  ?  779  LEU B CB  1 
ATOM   3443 C  CG  . LEU A 1 502 ? -4.91500  -19.92300 23.90000  1.000 78.39113  ?  779  LEU B CG  1 
ATOM   3444 C  CD1 . LEU A 1 502 ? -5.12100  -18.74300 22.93300  1.000 74.08840  ?  779  LEU B CD1 1 
ATOM   3445 C  CD2 . LEU A 1 502 ? -5.27800  -21.22000 23.22200  1.000 78.61835  ?  779  LEU B CD2 1 
ATOM   3446 N  N   . ASN A 1 503 ? -4.60200  -17.88100 26.73700  1.000 73.43171  ?  780  ASN B N   1 
ATOM   3447 C  CA  . ASN A 1 503 ? -5.28000  -17.70000 28.02500  1.000 72.07155  ?  780  ASN B CA  1 
ATOM   3448 C  C   . ASN A 1 503 ? -6.80200  -17.69000 27.87000  1.000 67.10015  ?  780  ASN B C   1 
ATOM   3449 O  O   . ASN A 1 503 ? -7.34800  -17.67200 26.76100  1.000 68.25023  ?  780  ASN B O   1 
ATOM   3450 C  CB  . ASN A 1 503 ? -4.81200  -16.41500 28.72600  1.000 65.43797  ?  780  ASN B CB  1 
ATOM   3451 C  CG  . ASN A 1 503 ? -5.03000  -15.18000 27.88400  1.000 70.68059  ?  780  ASN B CG  1 
ATOM   3452 O  OD1 . ASN A 1 503 ? -6.09200  -15.00700 27.27800  1.000 73.14200  ?  780  ASN B OD1 1 
ATOM   3453 N  ND2 . ASN A 1 503 ? -4.01800  -14.31800 27.82400  1.000 62.59714  ?  780  ASN B ND2 1 
ATOM   3454 N  N   . LYS A 1 504 ? -7.49500  -17.68900 29.01400  1.000 69.03695  ?  781  LYS B N   1 
ATOM   3455 C  CA  . LYS A 1 504 ? -8.95300  -17.81400 28.98200  1.000 72.43595  ?  781  LYS B CA  1 
ATOM   3456 C  C   . LYS A 1 504 ? -9.62300  -16.57900 28.38700  1.000 69.45403  ?  781  LYS B C   1 
ATOM   3457 O  O   . LYS A 1 504 ? -10.73000 -16.68200 27.84100  1.000 68.64698  ?  781  LYS B O   1 
ATOM   3458 C  CB  . LYS A 1 504 ? -9.51100  -18.10200 30.38600  1.000 65.21696  ?  781  LYS B CB  1 
ATOM   3459 C  CG  . LYS A 1 504 ? -9.24100  -17.04000 31.45600  1.000 71.72284  ?  781  LYS B CG  1 
ATOM   3460 C  CD  . LYS A 1 504 ? -9.85300  -17.44100 32.81500  1.000 80.81921  ?  781  LYS B CD  1 
ATOM   3461 C  CE  . LYS A 1 504 ? -9.32100  -16.56900 33.94700  1.000 82.82001  ?  781  LYS B CE  1 
ATOM   3462 N  N   . GLU A 1 505 ? -8.98100  -15.41200 28.46300  1.000 66.70289  ?  782  GLU B N   1 
ATOM   3463 C  CA  . GLU A 1 505 ? -9.61700  -14.21200 27.92900  1.000 64.76825  ?  782  GLU B CA  1 
ATOM   3464 C  C   . GLU A 1 505 ? -9.63900  -14.22700 26.40500  1.000 64.27917  ?  782  GLU B C   1 
ATOM   3465 O  O   . GLU A 1 505 ? -10.59000 -13.71900 25.79200  1.000 60.99180  ?  782  GLU B O   1 
ATOM   3466 C  CB  . GLU A 1 505 ? -8.92000  -12.94900 28.45200  1.000 64.70752  ?  782  GLU B CB  1 
ATOM   3467 C  CG  . GLU A 1 505 ? -9.15000  -12.68400 29.94600  1.000 67.04273  ?  782  GLU B CG  1 
ATOM   3468 C  CD  . GLU A 1 505 ? -8.30100  -13.58100 30.85300  1.000 74.62338  ?  782  GLU B CD  1 
ATOM   3469 O  OE1 . GLU A 1 505 ? -7.38900  -14.27400 30.33400  1.000 70.49400  ?  782  GLU B OE1 1 
ATOM   3470 O  OE2 . GLU A 1 505 ? -8.54500  -13.59200 32.08200  1.000 74.30757  -1 782  GLU B OE2 1 
ATOM   3471 N  N   . MET A 1 506 ? -8.59800  -14.79300 25.77700  1.000 58.93427  ?  783  MET B N   1 
ATOM   3472 C  CA  . MET A 1 506 ? -8.57000  -14.87800 24.31700  1.000 64.06809  ?  783  MET B CA  1 
ATOM   3473 C  C   . MET A 1 506 ? -9.62200  -15.84800 23.80900  1.000 64.30686  ?  783  MET B C   1 
ATOM   3474 O  O   . MET A 1 506 ? -10.32700 -15.56000 22.83700  1.000 64.04415  ?  783  MET B O   1 
ATOM   3475 C  CB  . MET A 1 506 ? -7.18700  -15.31300 23.82900  1.000 62.42605  ?  783  MET B CB  1 
ATOM   3476 C  CG  . MET A 1 506 ? -6.08300  -14.33600 24.15900  1.000 63.12429  ?  783  MET B CG  1 
ATOM   3477 S  SD  . MET A 1 506 ? -4.46400  -15.05700 23.82200  1.000 75.56313  ?  783  MET B SD  1 
ATOM   3478 C  CE  . MET A 1 506 ? -4.57200  -15.34300 22.05400  1.000 66.53414  ?  783  MET B CE  1 
ATOM   3479 N  N   . VAL A 1 507 ? -9.74500  -16.99700 24.46900  1.000 65.54354  ?  784  VAL B N   1 
ATOM   3480 C  CA  . VAL A 1 507 ? -10.67500 -18.02300 24.02500  1.000 68.25705  ?  784  VAL B CA  1 
ATOM   3481 C  C   . VAL A 1 507 ? -12.11400 -17.55800 24.19800  1.000 69.55462  ?  784  VAL B C   1 
ATOM   3482 O  O   . VAL A 1 507 ? -12.96800 -17.81100 23.33900  1.000 72.09116  ?  784  VAL B O   1 
ATOM   3483 C  CB  . VAL A 1 507 ? -10.39800 -19.32800 24.78300  1.000 67.42277  ?  784  VAL B CB  1 
ATOM   3484 C  CG1 . VAL A 1 507 ? -11.24400 -20.45800 24.21600  1.000 66.34294  ?  784  VAL B CG1 1 
ATOM   3485 C  CG2 . VAL A 1 507 ? -8.91200  -19.64100 24.70600  1.000 68.24268  ?  784  VAL B CG2 1 
ATOM   3486 N  N   . GLU A 1 508 ? -12.41500 -16.87900 25.30600  1.000 64.89485  ?  785  GLU B N   1 
ATOM   3487 C  CA  . GLU A 1 508 ? -13.74600 -16.30000 25.43600  1.000 65.95818  ?  785  GLU B CA  1 
ATOM   3488 C  C   . GLU A 1 508 ? -13.96400 -15.21000 24.39800  1.000 69.92742  ?  785  GLU B C   1 
ATOM   3489 O  O   . GLU A 1 508 ? -15.08700 -15.03600 23.89900  1.000 67.15345  ?  785  GLU B O   1 
ATOM   3490 C  CB  . GLU A 1 508 ? -13.94100 -15.76100 26.84600  1.000 65.86070  ?  785  GLU B CB  1 
ATOM   3491 C  CG  . GLU A 1 508 ? -14.18300 -16.86400 27.85100  1.000 77.44993  ?  785  GLU B CG  1 
ATOM   3492 C  CD  . GLU A 1 508 ? -13.99800 -16.40400 29.28300  1.000 87.66853  ?  785  GLU B CD  1 
ATOM   3493 O  OE1 . GLU A 1 508 ? -13.37400 -15.33900 29.48800  1.000 82.49342  ?  785  GLU B OE1 1 
ATOM   3494 O  OE2 . GLU A 1 508 ? -14.47800 -17.10800 30.20000  1.000 92.69951  -1 785  GLU B OE2 1 
ATOM   3495 N  N   . GLY A 1 509 ? -12.89200 -14.49600 24.03800  1.000 64.20110  ?  786  GLY B N   1 
ATOM   3496 C  CA  . GLY A 1 509 ? -12.99600 -13.46500 23.02200  1.000 61.01319  ?  786  GLY B CA  1 
ATOM   3497 C  C   . GLY A 1 509 ? -13.50100 -13.99000 21.69500  1.000 65.12241  ?  786  GLY B C   1 
ATOM   3498 O  O   . GLY A 1 509 ? -14.23500 -13.30100 20.98300  1.000 67.80251  ?  786  GLY B O   1 
ATOM   3499 N  N   . MET A 1 510 ? -13.12900 -15.21900 21.34300  1.000 63.08193  ?  787  MET B N   1 
ATOM   3500 C  CA  . MET A 1 510 ? -13.58800 -15.80200 20.09000  1.000 68.57479  ?  787  MET B CA  1 
ATOM   3501 C  C   . MET A 1 510 ? -14.78200 -16.72300 20.27800  1.000 75.96821  ?  787  MET B C   1 
ATOM   3502 O  O   . MET A 1 510 ? -15.08200 -17.52400 19.38600  1.000 84.15600  ?  787  MET B O   1 
ATOM   3503 C  CB  . MET A 1 510 ? -12.45200 -16.53800 19.37700  1.000 69.35341  ?  787  MET B CB  1 
ATOM   3504 C  CG  . MET A 1 510 ? -11.81300 -17.65300 20.17100  1.000 70.52918  ?  787  MET B CG  1 
ATOM   3505 S  SD  . MET A 1 510 ? -10.46100 -18.41300 19.24700  1.000 76.64608  ?  787  MET B SD  1 
ATOM   3506 C  CE  . MET A 1 510 ? -9.12600  -17.25400 19.46600  1.000 62.38501  ?  787  MET B CE  1 
ATOM   3507 N  N   . GLY A 1 511 ? -15.48100 -16.61800 21.40300  1.000 71.74810  ?  788  GLY B N   1 
ATOM   3508 C  CA  . GLY A 1 511 ? -16.72100 -17.34200 21.59300  1.000 72.92963  ?  788  GLY B CA  1 
ATOM   3509 C  C   . GLY A 1 511 ? -16.62200 -18.63500 22.36500  1.000 77.03680  ?  788  GLY B C   1 
ATOM   3510 O  O   . GLY A 1 511 ? -17.62200 -19.36100 22.44600  1.000 86.76792  ?  788  GLY B O   1 
ATOM   3511 N  N   . GLY A 1 512 ? -15.47100 -18.94600 22.95500  1.000 77.20051  ?  789  GLY B N   1 
ATOM   3512 C  CA  . GLY A 1 512 ? -15.34100 -20.17700 23.70300  1.000 78.99992  ?  789  GLY B CA  1 
ATOM   3513 C  C   . GLY A 1 512 ? -14.99500 -21.34100 22.80200  1.000 82.61424  ?  789  GLY B C   1 
ATOM   3514 O  O   . GLY A 1 512 ? -14.91100 -21.22200 21.57700  1.000 81.96544  ?  789  GLY B O   1 
ATOM   3515 N  N   . THR A 1 513 ? -14.79800 -22.50100 23.42600  1.000 83.19102  ?  790  THR B N   1 
ATOM   3516 C  CA  . THR A 1 513 ? -14.21300 -23.61900 22.69700  1.000 85.38294  ?  790  THR B CA  1 
ATOM   3517 C  C   . THR A 1 513 ? -15.23000 -24.44000 21.92100  1.000 85.06913  ?  790  THR B C   1 
ATOM   3518 O  O   . THR A 1 513 ? -14.82900 -25.35000 21.18900  1.000 87.04612  ?  790  THR B O   1 
ATOM   3519 C  CB  . THR A 1 513 ? -13.43400 -24.53000 23.64700  1.000 86.07914  ?  790  THR B CB  1 
ATOM   3520 O  OG1 . THR A 1 513 ? -14.29500 -24.98500 24.69200  1.000 80.40659  ?  790  THR B OG1 1 
ATOM   3521 C  CG2 . THR A 1 513 ? -12.25100 -23.77200 24.25300  1.000 81.24257  ?  790  THR B CG2 1 
ATOM   3522 N  N   . GLN A 1 514 ? -16.52500 -24.15700 22.04500  1.000 91.33533  ?  791  GLN B N   1 
ATOM   3523 C  CA  . GLN A 1 514 ? -17.52600 -24.83700 21.23300  1.000 92.75810  ?  791  GLN B CA  1 
ATOM   3524 C  C   . GLN A 1 514 ? -17.90800 -24.03900 19.98500  1.000 93.44745  ?  791  GLN B C   1 
ATOM   3525 O  O   . GLN A 1 514 ? -18.84700 -24.42300 19.28200  1.000 98.65151  ?  791  GLN B O   1 
ATOM   3526 C  CB  . GLN A 1 514 ? -18.78000 -25.14400 22.06500  1.000 93.94535  ?  791  GLN B CB  1 
ATOM   3527 C  CG  . GLN A 1 514 ? -18.68900 -26.37100 22.96900  1.000 93.18626  ?  791  GLN B CG  1 
ATOM   3528 N  N   . SER A 1 515 ? -17.19600 -22.95500 19.68300  1.000 90.67971  ?  792  SER B N   1 
ATOM   3529 C  CA  . SER A 1 515 ? -17.58800 -22.03600 18.62300  1.000 90.03978  ?  792  SER B CA  1 
ATOM   3530 C  C   . SER A 1 515 ? -16.92100 -22.38100 17.29400  1.000 90.63200  ?  792  SER B C   1 
ATOM   3531 O  O   . SER A 1 515 ? -15.84100 -22.97900 17.24600  1.000 86.92465  ?  792  SER B O   1 
ATOM   3532 C  CB  . SER A 1 515 ? -17.24400 -20.59100 19.00400  1.000 83.34342  ?  792  SER B CB  1 
ATOM   3533 O  OG  . SER A 1 515 ? -15.86500 -20.42900 19.26400  1.000 82.93804  ?  792  SER B OG  1 
ATOM   3534 N  N   . GLU A 1 516 ? -17.58500 -21.98600 16.20100  1.000 90.97882  ?  793  GLU B N   1 
ATOM   3535 C  CA  . GLU A 1 516 ? -16.95500 -22.07300 14.88900  1.000 85.47237  ?  793  GLU B CA  1 
ATOM   3536 C  C   . GLU A 1 516 ? -15.64900 -21.28800 14.84900  1.000 88.48339  ?  793  GLU B C   1 
ATOM   3537 O  O   . GLU A 1 516 ? -14.71300 -21.67200 14.14000  1.000 86.64963  ?  793  GLU B O   1 
ATOM   3538 C  CB  . GLU A 1 516 ? -17.91700 -21.57300 13.80900  1.000 86.40341  ?  793  GLU B CB  1 
ATOM   3539 N  N   . GLN A 1 517 ? -15.55500 -20.20000 15.61400  1.000 90.87723  ?  794  GLN B N   1 
ATOM   3540 C  CA  . GLN A 1 517 ? -14.33300 -19.40900 15.61400  1.000 81.33686  ?  794  GLN B CA  1 
ATOM   3541 C  C   . GLN A 1 517 ? -13.16400 -20.20300 16.17400  1.000 79.76080  ?  794  GLN B C   1 
ATOM   3542 O  O   . GLN A 1 517 ? -12.05400 -20.15500 15.63000  1.000 80.36668  ?  794  GLN B O   1 
ATOM   3543 C  CB  . GLN A 1 517 ? -14.53300 -18.12500 16.41400  1.000 83.58437  ?  794  GLN B CB  1 
ATOM   3544 C  CG  . GLN A 1 517 ? -15.28300 -17.03200 15.67800  1.000 79.11173  ?  794  GLN B CG  1 
ATOM   3545 C  CD  . GLN A 1 517 ? -16.74900 -17.34800 15.53400  1.000 88.26544  ?  794  GLN B CD  1 
ATOM   3546 O  OE1 . GLN A 1 517 ? -17.25200 -18.30400 16.13100  1.000 86.75944  ?  794  GLN B OE1 1 
ATOM   3547 N  NE2 . GLN A 1 517 ? -17.45100 -16.55300 14.73400  1.000 91.37812  ?  794  GLN B NE2 1 
ATOM   3548 N  N   . TYR A 1 518 ? -13.38500 -20.93000 17.27000  1.000 77.86660  ?  795  TYR B N   1 
ATOM   3549 C  CA  . TYR A 1 518 ? -12.28800 -21.69100 17.85400  1.000 78.91369  ?  795  TYR B CA  1 
ATOM   3550 C  C   . TYR A 1 518 ? -11.77800 -22.73300 16.87300  1.000 81.19671  ?  795  TYR B C   1 
ATOM   3551 O  O   . TYR A 1 518 ? -10.56500 -22.90800 16.71500  1.000 82.70545  ?  795  TYR B O   1 
ATOM   3552 C  CB  . TYR A 1 518 ? -12.73300 -22.34100 19.16300  1.000 78.71126  ?  795  TYR B CB  1 
ATOM   3553 C  CG  . TYR A 1 518 ? -11.63800 -23.10100 19.88000  1.000 79.73272  ?  795  TYR B CG  1 
ATOM   3554 C  CD1 . TYR A 1 518 ? -10.60100 -22.42700 20.51600  1.000 73.26828  ?  795  TYR B CD1 1 
ATOM   3555 C  CD2 . TYR A 1 518 ? -11.64800 -24.49200 19.93300  1.000 79.56247  ?  795  TYR B CD2 1 
ATOM   3556 C  CE1 . TYR A 1 518 ? -9.60400  -23.11700 21.18000  1.000 74.01186  ?  795  TYR B CE1 1 
ATOM   3557 C  CE2 . TYR A 1 518 ? -10.65200 -25.18900 20.59100  1.000 82.38021  ?  795  TYR B CE2 1 
ATOM   3558 C  CZ  . TYR A 1 518 ? -9.63400  -24.49600 21.21300  1.000 79.18699  ?  795  TYR B CZ  1 
ATOM   3559 O  OH  . TYR A 1 518 ? -8.64000  -25.18400 21.86900  1.000 90.28389  ?  795  TYR B OH  1 
ATOM   3560 N  N   . GLN A 1 519 ? -12.69100 -23.42700 16.19400  1.000 81.33121  ?  796  GLN B N   1 
ATOM   3561 C  CA  . GLN A 1 519 ? -12.28900 -24.33600 15.12800  1.000 84.69100  ?  796  GLN B CA  1 
ATOM   3562 C  C   . GLN A 1 519 ? -11.43000 -23.61500 14.09600  1.000 82.47079  ?  796  GLN B C   1 
ATOM   3563 O  O   . GLN A 1 519 ? -10.34700 -24.08600 13.73100  1.000 79.00926  ?  796  GLN B O   1 
ATOM   3564 N  N   . GLU A 1 520 ? -11.90000 -22.46000 13.61200  1.000 78.52437  ?  797  GLU B N   1 
ATOM   3565 C  CA  . GLU A 1 520 ? -11.12000 -21.70800 12.63900  1.000 75.04353  ?  797  GLU B CA  1 
ATOM   3566 C  C   . GLU A 1 520 ? -9.76900  -21.34200 13.22100  1.000 75.98920  ?  797  GLU B C   1 
ATOM   3567 O  O   . GLU A 1 520 ? -8.73000  -21.52000 12.57600  1.000 77.82469  ?  797  GLU B O   1 
ATOM   3568 C  CB  . GLU A 1 520 ? -11.87700 -20.45600 12.19800  1.000 80.76694  ?  797  GLU B CB  1 
ATOM   3569 N  N   . PHE A 1 521 ? -9.76300  -20.85300 14.46000  1.000 76.16498  ?  798  PHE B N   1 
ATOM   3570 C  CA  . PHE A 1 521 ? -8.50900  -20.51800 15.12200  1.000 72.80624  ?  798  PHE B CA  1 
ATOM   3571 C  C   . PHE A 1 521 ? -7.55800  -21.70900 15.15300  1.000 70.95840  ?  798  PHE B C   1 
ATOM   3572 O  O   . PHE A 1 521 ? -6.36000  -21.56100 14.87800  1.000 69.62443  ?  798  PHE B O   1 
ATOM   3573 C  CB  . PHE A 1 521 ? -8.79700  -20.01500 16.53000  1.000 69.94006  ?  798  PHE B CB  1 
ATOM   3574 C  CG  . PHE A 1 521 ? -7.63000  -20.10300 17.45100  1.000 68.06123  ?  798  PHE B CG  1 
ATOM   3575 C  CD1 . PHE A 1 521 ? -6.69500  -19.08500 17.49900  1.000 62.04589  ?  798  PHE B CD1 1 
ATOM   3576 C  CD2 . PHE A 1 521 ? -7.47800  -21.19200 18.28900  1.000 68.66758  ?  798  PHE B CD2 1 
ATOM   3577 C  CE1 . PHE A 1 521 ? -5.61800  -19.15700 18.35700  1.000 61.70933  ?  798  PHE B CE1 1 
ATOM   3578 C  CE2 . PHE A 1 521 ? -6.40900  -21.27200 19.15200  1.000 70.26834  ?  798  PHE B CE2 1 
ATOM   3579 C  CZ  . PHE A 1 521 ? -5.47600  -20.25500 19.19100  1.000 60.74532  ?  798  PHE B CZ  1 
ATOM   3580 N  N   . ARG A 1 522 ? -8.06900  -22.89700 15.49100  1.000 72.10561  ?  799  ARG B N   1 
ATOM   3581 C  CA  . ARG A 1 522 ? -7.20700  -24.07500 15.52100  1.000 75.08516  ?  799  ARG B CA  1 
ATOM   3582 C  C   . ARG A 1 522 ? -6.63100  -24.36200 14.14100  1.000 74.12539  ?  799  ARG B C   1 
ATOM   3583 O  O   . ARG A 1 522 ? -5.43300  -24.62800 14.00600  1.000 74.30059  ?  799  ARG B O   1 
ATOM   3584 C  CB  . ARG A 1 522 ? -7.97500  -25.28900 16.05100  1.000 76.96905  ?  799  ARG B CB  1 
ATOM   3585 C  CG  . ARG A 1 522 ? -8.19100  -25.28800 17.56800  1.000 82.01195  ?  799  ARG B CG  1 
ATOM   3586 C  CD  . ARG A 1 522 ? -8.03400  -26.69000 18.18600  1.000 81.88770  ?  799  ARG B CD  1 
ATOM   3587 N  NE  . ARG A 1 522 ? -9.13100  -27.57700 17.82800  1.000 85.38872  ?  799  ARG B NE  1 
ATOM   3588 C  CZ  . ARG A 1 522 ? -9.16000  -28.88100 18.07500  1.000 93.44948  ?  799  ARG B CZ  1 
ATOM   3589 N  N   . LYS A 1 523 ? -7.46300  -24.29200 13.09900  1.000 71.32770  ?  800  LYS B N   1 
ATOM   3590 C  CA  . LYS A 1 523 ? -6.96900  -24.56700 11.75400  1.000 74.28401  ?  800  LYS B CA  1 
ATOM   3591 C  C   . LYS A 1 523 ? -5.92500  -23.53500 11.33400  1.000 73.51790  ?  800  LYS B C   1 
ATOM   3592 O  O   . LYS A 1 523 ? -4.89000  -23.89300 10.75700  1.000 73.25020  ?  800  LYS B O   1 
ATOM   3593 C  CB  . LYS A 1 523 ? -8.13600  -24.62200 10.75800  1.000 69.71332  ?  800  LYS B CB  1 
ATOM   3594 N  N   . GLN A 1 524 ? -6.16600  -22.24800 11.62600  1.000 69.91548  ?  801  GLN B N   1 
ATOM   3595 C  CA  . GLN A 1 524 ? -5.16900  -21.23000 11.30000  1.000 67.57909  ?  801  GLN B CA  1 
ATOM   3596 C  C   . GLN A 1 524 ? -3.85900  -21.48900 12.02500  1.000 68.56937  ?  801  GLN B C   1 
ATOM   3597 O  O   . GLN A 1 524 ? -2.78900  -21.18700 11.49000  1.000 69.62260  ?  801  GLN B O   1 
ATOM   3598 C  CB  . GLN A 1 524 ? -5.67800  -19.82500 11.63200  1.000 66.06311  ?  801  GLN B CB  1 
ATOM   3599 C  CG  . GLN A 1 524 ? -6.92300  -19.35100 10.86900  1.000 72.62272  ?  801  GLN B CG  1 
ATOM   3600 C  CD  . GLN A 1 524 ? -6.69600  -19.22400 9.36600   1.000 78.46107  ?  801  GLN B CD  1 
ATOM   3601 O  OE1 . GLN A 1 524 ? -5.74500  -19.78400 8.82500   1.000 79.82085  ?  801  GLN B OE1 1 
ATOM   3602 N  NE2 . GLN A 1 524 ? -7.57600  -18.49000 8.68800   1.000 76.84250  ?  801  GLN B NE2 1 
ATOM   3603 N  N   . CYS A 1 525 ? -3.91800  -22.05500 13.23500  1.000 70.74184  ?  802  CYS B N   1 
ATOM   3604 C  CA  . CYS A 1 525 ? -2.69800  -22.39900 13.96300  1.000 69.10821  ?  802  CYS B CA  1 
ATOM   3605 C  C   . CYS A 1 525 ? -1.91900  -23.50600 13.25400  1.000 70.93700  ?  802  CYS B C   1 
ATOM   3606 O  O   . CYS A 1 525 ? -0.69500  -23.41500 13.11600  1.000 67.25453  ?  802  CYS B O   1 
ATOM   3607 C  CB  . CYS A 1 525 ? -3.03700  -22.82600 15.38900  1.000 68.65400  ?  802  CYS B CB  1 
ATOM   3608 S  SG  . CYS A 1 525 ? -3.41800  -21.48100 16.52200  1.000 65.93165  ?  802  CYS B SG  1 
ATOM   3609 N  N   . TYR A 1 526 ? -2.61400  -24.57100 12.82200  1.000 72.70933  ?  803  TYR B N   1 
ATOM   3610 C  CA  . TYR A 1 526 ? -1.96500  -25.66000 12.08800  1.000 72.08125  ?  803  TYR B CA  1 
ATOM   3611 C  C   . TYR A 1 526 ? -1.33200  -25.15300 10.79600  1.000 72.12222  ?  803  TYR B C   1 
ATOM   3612 O  O   . TYR A 1 526 ? -0.20400  -25.52200 10.44900  1.000 70.36794  ?  803  TYR B O   1 
ATOM   3613 C  CB  . TYR A 1 526 ? -2.97400  -26.77400 11.75300  1.000 76.09700  ?  803  TYR B CB  1 
ATOM   3614 C  CG  . TYR A 1 526 ? -3.78700  -27.28900 12.91000  1.000 82.97112  ?  803  TYR B CG  1 
ATOM   3615 C  CD1 . TYR A 1 526 ? -3.38400  -27.06800 14.22300  1.000 88.74815  ?  803  TYR B CD1 1 
ATOM   3616 C  CD2 . TYR A 1 526 ? -4.96200  -28.00400 12.69500  1.000 84.99631  ?  803  TYR B CD2 1 
ATOM   3617 C  CE1 . TYR A 1 526 ? -4.13400  -27.53800 15.30300  1.000 89.26955  ?  803  TYR B CE1 1 
ATOM   3618 C  CE2 . TYR A 1 526 ? -5.71800  -28.48500 13.76700  1.000 90.10469  ?  803  TYR B CE2 1 
ATOM   3619 C  CZ  . TYR A 1 526 ? -5.29700  -28.24500 15.07100  1.000 92.54704  ?  803  TYR B CZ  1 
ATOM   3620 O  OH  . TYR A 1 526 ? -6.03200  -28.71800 16.14500  1.000 97.10801  ?  803  TYR B OH  1 
ATOM   3621 N  N   . THR A 1 527 ? -2.07100  -24.34500 10.03900  1.000 66.87339  ?  804  THR B N   1 
ATOM   3622 C  CA  . THR A 1 527 ? -1.53900  -23.81900 8.79000   1.000 66.77115  ?  804  THR B CA  1 
ATOM   3623 C  C   . THR A 1 527 ? -0.26900  -23.02100 9.03800   1.000 66.66930  ?  804  THR B C   1 
ATOM   3624 O  O   . THR A 1 527 ? 0.77400   -23.28500 8.42800   1.000 65.96421  ?  804  THR B O   1 
ATOM   3625 C  CB  . THR A 1 527 ? -2.60100  -22.96300 8.11000   1.000 71.51136  ?  804  THR B CB  1 
ATOM   3626 O  OG1 . THR A 1 527 ? -3.78300  -23.75200 7.94300   1.000 77.34891  ?  804  THR B OG1 1 
ATOM   3627 C  CG2 . THR A 1 527 ? -2.11600  -22.48500 6.75700   1.000 69.41994  ?  804  THR B CG2 1 
ATOM   3628 N  N   . ALA A 1 528 ? -0.33400  -22.05100 9.95500   1.000 61.88417  ?  805  ALA B N   1 
ATOM   3629 C  CA  . ALA A 1 528 ? 0.83000   -21.22700 10.25500  1.000 60.89452  ?  805  ALA B CA  1 
ATOM   3630 C  C   . ALA A 1 528 ? 2.03500   -22.08400 10.63500  1.000 63.29505  ?  805  ALA B C   1 
ATOM   3631 O  O   . ALA A 1 528 ? 3.13700   -21.89500 10.10500  1.000 58.46592  ?  805  ALA B O   1 
ATOM   3632 C  CB  . ALA A 1 528 ? 0.48900   -20.23900 11.36700  1.000 57.07934  ?  805  ALA B CB  1 
ATOM   3633 N  N   . PHE A 1 529 ? 1.83900   -23.04000 11.54700  1.000 60.67320  ?  806  PHE B N   1 
ATOM   3634 C  CA  . PHE A 1 529 ? 2.94500   -23.88300 11.99300  1.000 62.26412  ?  806  PHE B CA  1 
ATOM   3635 C  C   . PHE A 1 529 ? 3.56600   -24.65800 10.83400  1.000 66.47312  ?  806  PHE B C   1 
ATOM   3636 O  O   . PHE A 1 529 ? 4.79600   -24.77600 10.74300  1.000 65.59589  ?  806  PHE B O   1 
ATOM   3637 C  CB  . PHE A 1 529 ? 2.46100   -24.84500 13.07800  1.000 65.74639  ?  806  PHE B CB  1 
ATOM   3638 C  CG  . PHE A 1 529 ? 3.56900   -25.58400 13.77100  1.000 65.62955  ?  806  PHE B CG  1 
ATOM   3639 C  CD1 . PHE A 1 529 ? 4.69700   -24.91100 14.21700  1.000 60.01592  ?  806  PHE B CD1 1 
ATOM   3640 C  CD2 . PHE A 1 529 ? 3.47600   -26.94900 13.99900  1.000 71.15822  ?  806  PHE B CD2 1 
ATOM   3641 C  CE1 . PHE A 1 529 ? 5.72000   -25.59100 14.86500  1.000 63.99813  ?  806  PHE B CE1 1 
ATOM   3642 C  CE2 . PHE A 1 529 ? 4.49800   -27.64000 14.65600  1.000 69.65604  ?  806  PHE B CE2 1 
ATOM   3643 C  CZ  . PHE A 1 529 ? 5.62400   -26.95600 15.08500  1.000 64.69985  ?  806  PHE B CZ  1 
ATOM   3644 N  N   . LEU A 1 530 ? 2.73500   -25.20800 9.94300   1.000 62.03402  ?  807  LEU B N   1 
ATOM   3645 C  CA  . LEU A 1 530 ? 3.27500   -25.98600 8.83400   1.000 62.91702  ?  807  LEU B CA  1 
ATOM   3646 C  C   . LEU A 1 530 ? 4.01900   -25.10200 7.83600   1.000 65.93463  ?  807  LEU B C   1 
ATOM   3647 O  O   . LEU A 1 530 ? 5.01200   -25.53500 7.23800   1.000 68.35223  ?  807  LEU B O   1 
ATOM   3648 C  CB  . LEU A 1 530 ? 2.16000   -26.76000 8.13300   1.000 66.92154  ?  807  LEU B CB  1 
ATOM   3649 C  CG  . LEU A 1 530 ? 1.57600   -27.96000 8.86800   1.000 71.46763  ?  807  LEU B CG  1 
ATOM   3650 C  CD1 . LEU A 1 530 ? 0.58000   -28.63500 7.96200   1.000 81.08023  ?  807  LEU B CD1 1 
ATOM   3651 C  CD2 . LEU A 1 530 ? 2.66600   -28.93800 9.26500   1.000 81.46565  ?  807  LEU B CD2 1 
ATOM   3652 N  N   . HIS A 1 531 ? 3.54600   -23.87400 7.61800   1.000 60.82053  ?  808  HIS B N   1 
ATOM   3653 C  CA  . HIS A 1 531 ? 4.22800   -22.98100 6.68400   1.000 61.19756  ?  808  HIS B CA  1 
ATOM   3654 C  C   . HIS A 1 531 ? 5.59000   -22.54700 7.22200   1.000 62.29407  ?  808  HIS B C   1 
ATOM   3655 O  O   . HIS A 1 531 ? 6.60300   -22.63600 6.51700   1.000 61.23765  ?  808  HIS B O   1 
ATOM   3656 C  CB  . HIS A 1 531 ? 3.36200   -21.75600 6.38900   1.000 58.14374  ?  808  HIS B CB  1 
ATOM   3657 C  CG  . HIS A 1 531 ? 2.24500   -22.01300 5.42700   1.000 67.60803  ?  808  HIS B CG  1 
ATOM   3658 N  ND1 . HIS A 1 531 ? 1.11500   -21.22300 5.37400   1.000 72.66249  ?  808  HIS B ND1 1 
ATOM   3659 C  CD2 . HIS A 1 531 ? 2.09000   -22.95600 4.46800   1.000 73.70385  ?  808  HIS B CD2 1 
ATOM   3660 C  CE1 . HIS A 1 531 ? 0.30700   -21.67900 4.43200   1.000 74.49728  ?  808  HIS B CE1 1 
ATOM   3661 N  NE2 . HIS A 1 531 ? 0.87300   -22.73300 3.87200   1.000 75.61147  ?  808  HIS B NE2 1 
ATOM   3662 N  N   . LEU A 1 532 ? 5.63000   -22.07900 8.47700   1.000 60.20671  ?  809  LEU B N   1 
ATOM   3663 C  CA  . LEU A 1 532 ? 6.88400   -21.63700 9.08200   1.000 58.99866  ?  809  LEU B CA  1 
ATOM   3664 C  C   . LEU A 1 532 ? 7.89100   -22.77600 9.21600   1.000 58.86060  ?  809  LEU B C   1 
ATOM   3665 O  O   . LEU A 1 532 ? 9.09800   -22.54800 9.07800   1.000 56.35007  ?  809  LEU B O   1 
ATOM   3666 C  CB  . LEU A 1 532 ? 6.59800   -21.00200 10.43900  1.000 55.65769  ?  809  LEU B CB  1 
ATOM   3667 C  CG  . LEU A 1 532 ? 5.67600   -19.78900 10.32700  1.000 56.45558  ?  809  LEU B CG  1 
ATOM   3668 C  CD1 . LEU A 1 532 ? 5.26900   -19.27400 11.69600  1.000 57.66696  ?  809  LEU B CD1 1 
ATOM   3669 C  CD2 . LEU A 1 532 ? 6.35900   -18.68800 9.54000   1.000 53.16497  ?  809  LEU B CD2 1 
ATOM   3670 N  N   . ARG A 1 533 ? 7.41600   -23.99900 9.48500   1.000 57.57919  ?  810  ARG B N   1 
ATOM   3671 C  CA  . ARG A 1 533 ? 8.27900   -25.17400 9.44100   1.000 65.86566  ?  810  ARG B CA  1 
ATOM   3672 C  C   . ARG A 1 533 ? 8.99700   -25.27700 8.10600   1.000 64.13947  ?  810  ARG B C   1 
ATOM   3673 O  O   . ARG A 1 533 ? 10.16900  -25.66900 8.05500   1.000 63.57864  ?  810  ARG B O   1 
ATOM   3674 C  CB  . ARG A 1 533 ? 7.46400   -26.45300 9.66000   1.000 66.08417  ?  810  ARG B CB  1 
ATOM   3675 C  CG  . ARG A 1 533 ? 7.13400   -26.78800 11.08800  1.000 65.47237  ?  810  ARG B CG  1 
ATOM   3676 C  CD  . ARG A 1 533 ? 6.03400   -27.84900 11.13700  1.000 72.53859  ?  810  ARG B CD  1 
ATOM   3677 N  NE  . ARG A 1 533 ? 6.28800   -29.02200 10.29900  1.000 76.38353  ?  810  ARG B NE  1 
ATOM   3678 C  CZ  . ARG A 1 533 ? 6.94400   -30.10400 10.70100  1.000 78.78280  ?  810  ARG B CZ  1 
ATOM   3679 N  NH1 . ARG A 1 533 ? 7.54200   -30.15100 11.88100  1.000 79.71985  ?  810  ARG B NH1 1 
ATOM   3680 N  NH2 . ARG A 1 533 ? 6.99000   -31.17100 9.90700   1.000 82.31365  ?  810  ARG B NH2 1 
ATOM   3681 N  N   . ARG A 1 534 ? 8.29300   -24.97300 7.00700   1.000 62.21073  ?  811  ARG B N   1 
ATOM   3682 C  CA  . ARG A 1 534 ? 8.92400   -25.04200 5.69300   1.000 62.78448  ?  811  ARG B CA  1 
ATOM   3683 C  C   . ARG A 1 534 ? 10.03800  -24.01800 5.55400   1.000 60.57184  ?  811  ARG B C   1 
ATOM   3684 O  O   . ARG A 1 534 ? 10.89500  -24.17300 4.68600   1.000 64.85427  ?  811  ARG B O   1 
ATOM   3685 C  CB  . ARG A 1 534 ? 7.88900   -24.84600 4.58600   1.000 62.91382  ?  811  ARG B CB  1 
ATOM   3686 N  N   . TYR A 1 535 ? 10.06800  -23.00100 6.41100   1.000 58.74310  ?  812  TYR B N   1 
ATOM   3687 C  CA  . TYR A 1 535 ? 11.13300  -22.00700 6.39800   1.000 60.14582  ?  812  TYR B CA  1 
ATOM   3688 C  C   . TYR A 1 535 ? 12.09300  -22.16300 7.56900   1.000 55.95321  ?  812  TYR B C   1 
ATOM   3689 O  O   . TYR A 1 535 ? 12.77400  -21.19800 7.93400   1.000 54.83472  ?  812  TYR B O   1 
ATOM   3690 C  CB  . TYR A 1 535 ? 10.54700  -20.59300 6.37600   1.000 58.01408  ?  812  TYR B CB  1 
ATOM   3691 C  CG  . TYR A 1 535 ? 9.95300   -20.27500 5.03400   1.000 59.03108  ?  812  TYR B CG  1 
ATOM   3692 C  CD1 . TYR A 1 535 ? 10.73900  -19.78700 4.00500   1.000 62.60667  ?  812  TYR B CD1 1 
ATOM   3693 C  CD2 . TYR A 1 535 ? 8.61700   -20.50800 4.78300   1.000 65.79412  ?  812  TYR B CD2 1 
ATOM   3694 C  CE1 . TYR A 1 535 ? 10.19400  -19.52400 2.75600   1.000 67.63429  ?  812  TYR B CE1 1 
ATOM   3695 C  CE2 . TYR A 1 535 ? 8.06000   -20.25800 3.54600   1.000 66.34392  ?  812  TYR B CE2 1 
ATOM   3696 C  CZ  . TYR A 1 535 ? 8.84700   -19.76000 2.53700   1.000 74.25300  ?  812  TYR B CZ  1 
ATOM   3697 O  OH  . TYR A 1 535 ? 8.27500   -19.51600 1.30400   1.000 84.61343  ?  812  TYR B OH  1 
ATOM   3698 N  N   . SER A 1 536 ? 12.18700  -23.36600 8.14800   1.000 54.95781  ?  813  SER B N   1 
ATOM   3699 C  CA  . SER A 1 536 ? 13.01100  -23.51700 9.34800   1.000 57.47752  ?  813  SER B CA  1 
ATOM   3700 C  C   . SER A 1 536 ? 14.49000  -23.27400 9.04500   1.000 54.12088  ?  813  SER B C   1 
ATOM   3701 O  O   . SER A 1 536 ? 15.18800  -22.64400 9.84500   1.000 57.90783  ?  813  SER B O   1 
ATOM   3702 C  CB  . SER A 1 536 ? 12.78600  -24.88800 9.99500   1.000 55.19469  ?  813  SER B CB  1 
ATOM   3703 O  OG  . SER A 1 536 ? 13.10900  -25.94800 9.11400   1.000 65.97145  ?  813  SER B OG  1 
ATOM   3704 N  N   . ASN A 1 537 ? 14.98000  -23.71900 7.88000   1.000 51.82699  ?  814  ASN B N   1 
ATOM   3705 C  CA  . ASN A 1 537 ? 16.37700  -23.45400 7.52600   1.000 58.77646  ?  814  ASN B CA  1 
ATOM   3706 C  C   . ASN A 1 537 ? 16.69100  -21.95900 7.55700   1.000 59.23293  ?  814  ASN B C   1 
ATOM   3707 O  O   . ASN A 1 537 ? 17.65100  -21.52800 8.20900   1.000 51.96290  ?  814  ASN B O   1 
ATOM   3708 C  CB  . ASN A 1 537 ? 16.71200  -24.03700 6.15600   1.000 57.75315  ?  814  ASN B CB  1 
ATOM   3709 C  CG  . ASN A 1 537 ? 16.79800  -25.55200 6.17400   1.000 77.46813  ?  814  ASN B CG  1 
ATOM   3710 O  OD1 . ASN A 1 537 ? 16.54200  -26.19100 7.20100   1.000 82.80310  ?  814  ASN B OD1 1 
ATOM   3711 N  ND2 . ASN A 1 537 ? 17.14400  -26.14100 5.02800   1.000 86.82475  ?  814  ASN B ND2 1 
ATOM   3712 N  N   . LEU A 1 538 ? 15.88400  -21.14400 6.87200   1.000 54.18100  ?  815  LEU B N   1 
ATOM   3713 C  CA  . LEU A 1 538 ? 16.12800  -19.70700 6.89200   1.000 53.59804  ?  815  LEU B CA  1 
ATOM   3714 C  C   . LEU A 1 538 ? 16.06600  -19.14600 8.31300   1.000 55.53549  ?  815  LEU B C   1 
ATOM   3715 O  O   . LEU A 1 538 ? 16.93400  -18.36600 8.72600   1.000 54.43940  ?  815  LEU B O   1 
ATOM   3716 C  CB  . LEU A 1 538 ? 15.13300  -18.98500 5.98500   1.000 57.36228  ?  815  LEU B CB  1 
ATOM   3717 C  CG  . LEU A 1 538 ? 15.15300  -17.45600 6.13000   1.000 60.26538  ?  815  LEU B CG  1 
ATOM   3718 C  CD1 . LEU A 1 538 ? 16.46900  -16.87100 5.60300   1.000 53.23864  ?  815  LEU B CD1 1 
ATOM   3719 C  CD2 . LEU A 1 538 ? 13.93700  -16.83500 5.44300   1.000 57.76394  ?  815  LEU B CD2 1 
ATOM   3720 N  N   . ILE A 1 539 ? 15.04100  -19.51100 9.08100   1.000 56.54644  ?  816  ILE B N   1 
ATOM   3721 C  CA  . ILE A 1 539 ? 14.91200  -18.91600 10.41400  1.000 56.98443  ?  816  ILE B CA  1 
ATOM   3722 C  C   . ILE A 1 539 ? 16.04100  -19.39300 11.33300  1.000 50.46916  ?  816  ILE B C   1 
ATOM   3723 O  O   . ILE A 1 539 ? 16.65100  -18.60000 12.05800  1.000 50.79757  ?  816  ILE B O   1 
ATOM   3724 C  CB  . ILE A 1 539 ? 13.51500  -19.21000 10.99600  1.000 55.92693  ?  816  ILE B CB  1 
ATOM   3725 C  CG1 . ILE A 1 539 ? 12.46300  -18.40900 10.22700  1.000 54.33905  ?  816  ILE B CG1 1 
ATOM   3726 C  CG2 . ILE A 1 539 ? 13.45300  -18.85900 12.46700  1.000 51.41733  ?  816  ILE B CG2 1 
ATOM   3727 C  CD1 . ILE A 1 539 ? 11.07100  -18.95600 10.34600  1.000 60.09447  ?  816  ILE B CD1 1 
ATOM   3728 N  N   . LEU A 1 540 ? 16.36400  -20.68400 11.29700  1.000 52.11009  ?  817  LEU B N   1 
ATOM   3729 C  CA  . LEU A 1 540 ? 17.48500  -21.16900 12.09700  1.000 55.17725  ?  817  LEU B CA  1 
ATOM   3730 C  C   . LEU A 1 540 ? 18.79700  -20.51400 11.66500  1.000 56.82307  ?  817  LEU B C   1 
ATOM   3731 O  O   . LEU A 1 540 ? 19.62500  -20.15000 12.51200  1.000 56.92905  ?  817  LEU B O   1 
ATOM   3732 C  CB  . LEU A 1 540 ? 17.56500  -22.69700 12.01900  1.000 48.37908  ?  817  LEU B CB  1 
ATOM   3733 C  CG  . LEU A 1 540 ? 16.33100  -23.39300 12.62400  1.000 54.47785  ?  817  LEU B CG  1 
ATOM   3734 C  CD1 . LEU A 1 540 ? 16.38800  -24.90400 12.48500  1.000 57.54439  ?  817  LEU B CD1 1 
ATOM   3735 C  CD2 . LEU A 1 540 ? 16.17800  -23.02000 14.08600  1.000 52.64459  ?  817  LEU B CD2 1 
ATOM   3736 N  N   . ASN A 1 541 ? 19.00000  -20.34000 10.35200  1.000 55.16430  ?  818  ASN B N   1 
ATOM   3737 C  CA  . ASN A 1 541 ? 20.20500  -19.67400 9.85700   1.000 51.33627  ?  818  ASN B CA  1 
ATOM   3738 C  C   . ASN A 1 541 ? 20.33200  -18.25900 10.41700  1.000 50.10207  ?  818  ASN B C   1 
ATOM   3739 O  O   . ASN A 1 541 ? 21.40700  -17.85200 10.87600  1.000 48.63097  ?  818  ASN B O   1 
ATOM   3740 C  CB  . ASN A 1 541 ? 20.20900  -19.62900 8.32800   1.000 50.84987  ?  818  ASN B CB  1 
ATOM   3741 C  CG  . ASN A 1 541 ? 20.74600  -20.89500 7.71000   1.000 56.92563  ?  818  ASN B CG  1 
ATOM   3742 O  OD1 . ASN A 1 541 ? 21.26500  -21.75300 8.40000   1.000 59.17853  ?  818  ASN B OD1 1 
ATOM   3743 N  ND2 . ASN A 1 541 ? 20.63800  -21.00700 6.39500   1.000 59.50991  ?  818  ASN B ND2 1 
ATOM   3744 N  N   . LEU A 1 542 ? 19.25500  -17.48100 10.36000  1.000 44.24348  ?  819  LEU B N   1 
ATOM   3745 C  CA  . LEU A 1 542 ? 19.33700  -16.12300 10.87100  1.000 44.80291  ?  819  LEU B CA  1 
ATOM   3746 C  C   . LEU A 1 542 ? 19.70500  -16.12200 12.34900  1.000 54.14832  ?  819  LEU B C   1 
ATOM   3747 O  O   . LEU A 1 542 ? 20.58000  -15.35800 12.77500  1.000 50.29521  ?  819  LEU B O   1 
ATOM   3748 C  CB  . LEU A 1 542 ? 18.01700  -15.38500 10.63400  1.000 44.13653  ?  819  LEU B CB  1 
ATOM   3749 C  CG  . LEU A 1 542 ? 17.73500  -15.09300 9.15700   1.000 46.47430  ?  819  LEU B CG  1 
ATOM   3750 C  CD1 . LEU A 1 542 ? 16.33100  -14.55600 8.91500   1.000 50.16509  ?  819  LEU B CD1 1 
ATOM   3751 C  CD2 . LEU A 1 542 ? 18.77200  -14.11000 8.62900   1.000 48.83660  ?  819  LEU B CD2 1 
ATOM   3752 N  N   . PHE A 1 543 ? 19.05300  -16.97900 13.15000  1.000 49.13790  ?  820  PHE B N   1 
ATOM   3753 C  CA  . PHE A 1 543 ? 19.39500  -17.05100 14.56700  1.000 50.63804  ?  820  PHE B CA  1 
ATOM   3754 C  C   . PHE A 1 543 ? 20.84300  -17.45300 14.78000  1.000 49.69007  ?  820  PHE B C   1 
ATOM   3755 O  O   . PHE A 1 543 ? 21.48200  -16.97400 15.72200  1.000 47.38802  ?  820  PHE B O   1 
ATOM   3756 C  CB  . PHE A 1 543 ? 18.47000  -18.01800 15.30200  1.000 53.34759  ?  820  PHE B CB  1 
ATOM   3757 C  CG  . PHE A 1 543 ? 17.28300  -17.35200 15.87000  1.000 50.92494  ?  820  PHE B CG  1 
ATOM   3758 C  CD1 . PHE A 1 543 ? 17.37300  -16.66900 17.06900  1.000 49.35232  ?  820  PHE B CD1 1 
ATOM   3759 C  CD2 . PHE A 1 543 ? 16.07600  -17.35800 15.17700  1.000 49.98056  ?  820  PHE B CD2 1 
ATOM   3760 C  CE1 . PHE A 1 543 ? 16.26600  -16.01600 17.58700  1.000 53.04327  ?  820  PHE B CE1 1 
ATOM   3761 C  CE2 . PHE A 1 543 ? 14.96200  -16.71400 15.68400  1.000 52.07929  ?  820  PHE B CE2 1 
ATOM   3762 C  CZ  . PHE A 1 543 ? 15.05400  -16.03400 16.88700  1.000 54.85702  ?  820  PHE B CZ  1 
ATOM   3763 N  N   . SER A 1 544 ? 21.38300  -18.31500 13.92000  1.000 47.15768  ?  821  SER B N   1 
ATOM   3764 C  CA  . SER A 1 544 ? 22.77700  -18.69900 14.10300  1.000 53.54380  ?  821  SER B CA  1 
ATOM   3765 C  C   . SER A 1 544 ? 23.73300  -17.53800 13.83300  1.000 50.70434  ?  821  SER B C   1 
ATOM   3766 O  O   . SER A 1 544 ? 24.86800  -17.55700 14.32300  1.000 57.39027  ?  821  SER B O   1 
ATOM   3767 C  CB  . SER A 1 544 ? 23.11700  -19.90500 13.22600  1.000 46.52499  ?  821  SER B CB  1 
ATOM   3768 O  OG  . SER A 1 544 ? 23.41600  -19.49600 11.90500  1.000 61.92530  ?  821  SER B OG  1 
ATOM   3769 N  N   . LEU A 1 545 ? 23.30000  -16.52000 13.09400  1.000 45.15653  ?  822  LEU B N   1 
ATOM   3770 C  CA  . LEU A 1 545 ? 24.12100  -15.32800 12.92800  1.000 51.16790  ?  822  LEU B CA  1 
ATOM   3771 C  C   . LEU A 1 545 ? 24.05600  -14.39900 14.14600  1.000 47.65196  ?  822  LEU B C   1 
ATOM   3772 O  O   . LEU A 1 545 ? 24.85700  -13.45900 14.23900  1.000 49.07038  ?  822  LEU B O   1 
ATOM   3773 C  CB  . LEU A 1 545 ? 23.70500  -14.58800 11.63800  1.000 43.91932  ?  822  LEU B CB  1 
ATOM   3774 C  CG  . LEU A 1 545 ? 23.98000  -15.35700 10.33700  1.000 49.37698  ?  822  LEU B CG  1 
ATOM   3775 C  CD1 . LEU A 1 545 ? 23.49000  -14.62900 9.07300   1.000 46.35614  ?  822  LEU B CD1 1 
ATOM   3776 C  CD2 . LEU A 1 545 ? 25.46000  -15.66900 10.21000  1.000 49.67726  ?  822  LEU B CD2 1 
ATOM   3777 N  N   . MET A 1 546 ? 23.16300  -14.66900 15.09400  1.000 46.19941  ?  823  MET B N   1 
ATOM   3778 C  CA  . MET A 1 546 ? 22.95000  -13.82900 16.26400  1.000 44.62256  ?  823  MET B CA  1 
ATOM   3779 C  C   . MET A 1 546 ? 23.61400  -14.35200 17.54400  1.000 50.41645  ?  823  MET B C   1 
ATOM   3780 O  O   . MET A 1 546 ? 23.49700  -13.70600 18.59500  1.000 46.80364  ?  823  MET B O   1 
ATOM   3781 C  CB  . MET A 1 546 ? 21.44900  -13.67200 16.51000  1.000 43.94499  ?  823  MET B CB  1 
ATOM   3782 C  CG  . MET A 1 546 ? 20.69100  -12.95800 15.40800  1.000 47.38348  ?  823  MET B CG  1 
ATOM   3783 S  SD  . MET A 1 546 ? 21.23100  -11.25600 15.08300  1.000 49.92199  ?  823  MET B SD  1 
ATOM   3784 C  CE  . MET A 1 546 ? 20.84200  -10.37700 16.61000  1.000 43.88292  ?  823  MET B CE  1 
ATOM   3785 N  N   . VAL A 1 547 ? 24.29700  -15.50200 17.49600  1.000 47.13091  ?  824  VAL B N   1 
ATOM   3786 C  CA  . VAL A 1 547 ? 24.71300  -16.13700 18.74600  1.000 49.81737  ?  824  VAL B CA  1 
ATOM   3787 C  C   . VAL A 1 547 ? 25.79400  -15.34600 19.49500  1.000 53.72236  ?  824  VAL B C   1 
ATOM   3788 O  O   . VAL A 1 547 ? 25.93900  -15.52800 20.70500  1.000 59.87084  ?  824  VAL B O   1 
ATOM   3789 C  CB  . VAL A 1 547 ? 25.19200  -17.58500 18.51000  1.000 55.08487  ?  824  VAL B CB  1 
ATOM   3790 C  CG1 . VAL A 1 547 ? 24.04000  -18.45800 17.98900  1.000 56.65713  ?  824  VAL B CG1 1 
ATOM   3791 C  CG2 . VAL A 1 547 ? 26.40400  -17.60700 17.57300  1.000 49.01760  ?  824  VAL B CG2 1 
ATOM   3792 N  N   . ASP A 1 548 ? 26.56200  -14.47900 18.83500  1.000 48.92923  ?  825  ASP B N   1 
ATOM   3793 C  CA  . ASP A 1 548 ? 27.52200  -13.63200 19.53400  1.000 48.67503  ?  825  ASP B CA  1 
ATOM   3794 C  C   . ASP A 1 548 ? 27.00400  -12.21400 19.77800  1.000 52.98948  ?  825  ASP B C   1 
ATOM   3795 O  O   . ASP A 1 548 ? 27.77800  -11.35100 20.19300  1.000 56.88814  ?  825  ASP B O   1 
ATOM   3796 C  CB  . ASP A 1 548 ? 28.84100  -13.54300 18.76000  1.000 60.48743  ?  825  ASP B CB  1 
ATOM   3797 C  CG  . ASP A 1 548 ? 29.38500  -14.90100 18.33300  1.000 52.46998  ?  825  ASP B CG  1 
ATOM   3798 O  OD1 . ASP A 1 548 ? 29.48400  -15.77000 19.21200  1.000 61.66987  ?  825  ASP B OD1 1 
ATOM   3799 N  N   . ALA A 1 549 ? 25.73000  -11.94100 19.53400  1.000 46.59938  ?  826  ALA B N   1 
ATOM   3800 C  CA  . ALA A 1 549 ? 25.23800  -10.58400 19.72400  1.000 53.97241  ?  826  ALA B CA  1 
ATOM   3801 C  C   . ALA A 1 549 ? 25.05700  -10.26200 21.21000  1.000 55.62328  ?  826  ALA B C   1 
ATOM   3802 O  O   . ALA A 1 549 ? 24.82600  -11.14400 22.04500  1.000 50.86125  ?  826  ALA B O   1 
ATOM   3803 C  CB  . ALA A 1 549 ? 23.91000  -10.38000 18.98800  1.000 47.30413  ?  826  ALA B CB  1 
ATOM   3804 N  N   A ASN A 1 550 ? 25.15700  -8.96900  21.52900  0.558 52.48599  ?  827  ASN B N   1 
ATOM   3805 N  N   B ASN A 1 550 ? 25.16200  -8.97500  21.53800  0.442 51.80834  ?  827  ASN B N   1 
ATOM   3806 C  CA  A ASN A 1 550 ? 24.89800  -8.46500  22.87900  0.558 52.73228  ?  827  ASN B CA  1 
ATOM   3807 C  CA  B ASN A 1 550 ? 24.92100  -8.52000  22.90600  0.442 52.68286  ?  827  ASN B CA  1 
ATOM   3808 C  C   A ASN A 1 550 ? 23.38400  -8.31800  23.05200  0.558 53.69500  ?  827  ASN B C   1 
ATOM   3809 C  C   B ASN A 1 550 ? 23.41200  -8.33600  23.09400  0.442 53.69537  ?  827  ASN B C   1 
ATOM   3810 O  O   A ASN A 1 550 ? 22.82500  -7.22100  23.13800  0.558 55.51304  ?  827  ASN B O   1 
ATOM   3811 O  O   B ASN A 1 550 ? 22.88500  -7.23000  23.23500  0.442 55.34989  ?  827  ASN B O   1 
ATOM   3812 C  CB  A ASN A 1 550 ? 25.64000  -7.15100  23.10400  0.558 51.98170  ?  827  ASN B CB  1 
ATOM   3813 C  CB  B ASN A 1 550 ? 25.71300  -7.24800  23.19300  0.442 51.99954  ?  827  ASN B CB  1 
ATOM   3814 C  CG  A ASN A 1 550 ? 25.64500  -6.71000  24.56000  0.558 56.00989  ?  827  ASN B CG  1 
ATOM   3815 C  CG  B ASN A 1 550 ? 27.22400  -7.49100  23.23200  0.442 53.01234  ?  827  ASN B CG  1 
ATOM   3816 O  OD1 A ASN A 1 550 ? 25.30300  -7.48500  25.45500  0.558 60.14907  ?  827  ASN B OD1 1 
ATOM   3817 O  OD1 B ASN A 1 550 ? 27.69000  -8.62300  23.09900  0.442 53.19603  ?  827  ASN B OD1 1 
ATOM   3818 N  ND2 A ASN A 1 550 ? 26.05000  -5.46100  24.80400  0.558 52.76230  ?  827  ASN B ND2 1 
ATOM   3819 N  ND2 B ASN A 1 550 ? 27.99000  -6.42200  23.40800  0.442 55.05756  ?  827  ASN B ND2 1 
ATOM   3820 N  N   . ILE A 1 551 ? 22.71400  -9.46400  23.06200  1.000 50.62044  ?  828  ILE B N   1 
ATOM   3821 C  CA  . ILE A 1 551 ? 21.27400  -9.54600  23.27700  1.000 50.38810  ?  828  ILE B CA  1 
ATOM   3822 C  C   . ILE A 1 551 ? 21.05300  -10.41300 24.51300  1.000 47.92496  ?  828  ILE B C   1 
ATOM   3823 O  O   . ILE A 1 551 ? 21.39100  -11.60000 24.50100  1.000 47.98539  ?  828  ILE B O   1 
ATOM   3824 C  CB  . ILE A 1 551 ? 20.54500  -10.12900 22.05600  1.000 49.96485  ?  828  ILE B CB  1 
ATOM   3825 C  CG1 . ILE A 1 551 ? 20.85100  -9.25200  20.81900  1.000 51.05634  ?  828  ILE B CG1 1 
ATOM   3826 C  CG2 . ILE A 1 551 ? 19.03600  -10.34800 22.36500  1.000 46.71231  ?  828  ILE B CG2 1 
ATOM   3827 C  CD1 . ILE A 1 551 ? 19.66900  -8.80900  20.01900  1.000 46.46058  ?  828  ILE B CD1 1 
ATOM   3828 N  N   . PRO A 1 552 ? 20.47000  -9.88700  25.59100  1.000 49.45409  ?  829  PRO B N   1 
ATOM   3829 C  CA  . PRO A 1 552 ? 20.56000  -10.59900 26.88700  1.000 49.32014  ?  829  PRO B CA  1 
ATOM   3830 C  C   . PRO A 1 552 ? 20.07500  -12.03800 26.85000  1.000 49.73071  ?  829  PRO B C   1 
ATOM   3831 O  O   . PRO A 1 552 ? 20.76900  -12.91800 27.36300  1.000 48.79625  ?  829  PRO B O   1 
ATOM   3832 C  CB  . PRO A 1 552 ? 19.70300  -9.73500  27.82700  1.000 44.87001  ?  829  PRO B CB  1 
ATOM   3833 C  CG  . PRO A 1 552 ? 19.61700  -8.42100  27.17400  1.000 48.84275  ?  829  PRO B CG  1 
ATOM   3834 C  CD  . PRO A 1 552 ? 19.63500  -8.68500  25.67900  1.000 48.78838  ?  829  PRO B CD  1 
ATOM   3835 N  N   . ASP A 1 553 ? 18.90700  -12.31500 26.26500  1.000 46.85944  ?  830  ASP B N   1 
ATOM   3836 C  CA  . ASP A 1 553 ? 18.42500  -13.69300 26.36300  1.000 53.20406  ?  830  ASP B CA  1 
ATOM   3837 C  C   . ASP A 1 553 ? 19.20100  -14.65700 25.46300  1.000 54.40261  ?  830  ASP B C   1 
ATOM   3838 O  O   . ASP A 1 553 ? 19.09600  -15.87300 25.65700  1.000 52.54677  ?  830  ASP B O   1 
ATOM   3839 C  CB  . ASP A 1 553 ? 16.91200  -13.74700 26.09700  1.000 52.09679  ?  830  ASP B CB  1 
ATOM   3840 C  CG  . ASP A 1 553 ? 16.08900  -13.26400 27.32000  1.000 58.61623  ?  830  ASP B CG  1 
ATOM   3841 O  OD1 . ASP A 1 553 ? 16.70800  -12.94800 28.35200  1.000 61.76177  ?  830  ASP B OD1 1 
ATOM   3842 O  OD2 . ASP A 1 553 ? 14.83900  -13.19300 27.27500  1.000 57.08058  -1 830  ASP B OD2 1 
ATOM   3843 N  N   . ILE A 1 554 ? 20.01700  -14.15000 24.53500  1.000 50.08714  ?  831  ILE B N   1 
ATOM   3844 C  CA  . ILE A 1 554 ? 20.93700  -14.99200 23.77600  1.000 50.22014  ?  831  ILE B CA  1 
ATOM   3845 C  C   . ILE A 1 554 ? 22.26800  -15.15600 24.50300  1.000 58.59460  ?  831  ILE B C   1 
ATOM   3846 O  O   . ILE A 1 554 ? 22.82400  -16.25800 24.56300  1.000 60.00069  ?  831  ILE B O   1 
ATOM   3847 C  CB  . ILE A 1 554 ? 21.15300  -14.42400 22.35400  1.000 52.84387  ?  831  ILE B CB  1 
ATOM   3848 C  CG1 . ILE A 1 554 ? 19.85900  -14.46300 21.54400  1.000 51.85986  ?  831  ILE B CG1 1 
ATOM   3849 C  CG2 . ILE A 1 554 ? 22.26500  -15.18500 21.65800  1.000 50.84499  ?  831  ILE B CG2 1 
ATOM   3850 C  CD1 . ILE A 1 554 ? 19.95700  -13.77300 20.15700  1.000 42.89939  ?  831  ILE B CD1 1 
ATOM   3851 N  N   . ALA A 1 555 ? 22.81400  -14.06500 25.05200  1.000 55.39052  ?  832  ALA B N   1 
ATOM   3852 C  CA  . ALA A 1 555 ? 24.11700  -14.13400 25.71100  1.000 53.52746  ?  832  ALA B CA  1 
ATOM   3853 C  C   . ALA A 1 555 ? 24.09000  -15.01700 26.96300  1.000 59.43757  ?  832  ALA B C   1 
ATOM   3854 O  O   . ALA A 1 555 ? 25.15400  -15.43300 27.44400  1.000 62.63389  ?  832  ALA B O   1 
ATOM   3855 C  CB  . ALA A 1 555 ? 24.59900  -12.71900 26.05700  1.000 48.31913  ?  832  ALA B CB  1 
ATOM   3856 N  N   . LEU A 1 556 ? 22.89900  -15.31800 27.48500  1.000 57.92084  ?  833  LEU B N   1 
ATOM   3857 C  CA  . LEU A 1 556 ? 22.76700  -16.24000 28.60700  1.000 61.99721  ?  833  LEU B CA  1 
ATOM   3858 C  C   . LEU A 1 556 ? 23.22500  -17.64800 28.24000  1.000 61.92032  ?  833  LEU B C   1 
ATOM   3859 O  O   . LEU A 1 556 ? 23.79400  -18.35700 29.07300  1.000 70.33798  ?  833  LEU B O   1 
ATOM   3860 C  CB  . LEU A 1 556 ? 21.31300  -16.27700 29.07500  1.000 61.47706  ?  833  LEU B CB  1 
ATOM   3861 C  CG  . LEU A 1 556 ? 20.90100  -15.37200 30.22100  1.000 71.46195  ?  833  LEU B CG  1 
ATOM   3862 C  CD1 . LEU A 1 556 ? 19.41000  -15.56600 30.51700  1.000 76.99708  ?  833  LEU B CD1 1 
ATOM   3863 C  CD2 . LEU A 1 556 ? 21.73300  -15.71500 31.41900  1.000 70.09779  ?  833  LEU B CD2 1 
ATOM   3864 N  N   . GLU A 1 557 ? 22.95000  -18.07900 27.00500  1.000 64.30152  ?  834  GLU B N   1 
ATOM   3865 C  CA  . GLU A 1 557 ? 23.26100  -19.43700 26.53900  1.000 66.44882  ?  834  GLU B CA  1 
ATOM   3866 C  C   . GLU A 1 557 ? 23.52000  -19.40000 25.04100  1.000 63.92040  ?  834  GLU B C   1 
ATOM   3867 O  O   . GLU A 1 557 ? 22.78700  -20.00900 24.25300  1.000 64.45611  ?  834  GLU B O   1 
ATOM   3868 C  CB  . GLU A 1 557 ? 22.10200  -20.38400 26.83000  1.000 71.44595  ?  834  GLU B CB  1 
ATOM   3869 C  CG  . GLU A 1 557 ? 22.15800  -21.13300 28.12800  1.000 82.59512  ?  834  GLU B CG  1 
ATOM   3870 C  CD  . GLU A 1 557 ? 20.83100  -21.79900 28.41700  1.000 88.59942  ?  834  GLU B CD  1 
ATOM   3871 O  OE1 . GLU A 1 557 ? 19.80800  -21.34000 27.83800  1.000 84.51708  ?  834  GLU B OE1 1 
ATOM   3872 O  OE2 . GLU A 1 557 ? 20.81400  -22.77200 29.20400  1.000 101.51981 -1 834  GLU B OE2 1 
ATOM   3873 N  N   . PRO A 1 558 ? 24.56600  -18.69900 24.60600  1.000 65.56538  ?  835  PRO B N   1 
ATOM   3874 C  CA  . PRO A 1 558 ? 24.78400  -18.57500 23.15500  1.000 64.93805  ?  835  PRO B CA  1 
ATOM   3875 C  C   . PRO A 1 558 ? 24.78800  -19.92500 22.44300  1.000 66.06617  ?  835  PRO B C   1 
ATOM   3876 O  O   . PRO A 1 558 ? 24.30700  -20.02300 21.30800  1.000 62.77183  ?  835  PRO B O   1 
ATOM   3877 C  CB  . PRO A 1 558 ? 26.14800  -17.87800 23.06000  1.000 64.72337  ?  835  PRO B CB  1 
ATOM   3878 C  CG  . PRO A 1 558 ? 26.45700  -17.39100 24.43800  1.000 58.74361  ?  835  PRO B CG  1 
ATOM   3879 C  CD  . PRO A 1 558 ? 25.73800  -18.27000 25.38500  1.000 62.16913  ?  835  PRO B CD  1 
ATOM   3880 N  N   . ASP A 1 559 ? 25.29100  -20.97900 23.09000  1.000 60.67224  ?  836  ASP B N   1 
ATOM   3881 C  CA  . ASP A 1 559 ? 25.42700  -22.27900 22.44200  1.000 71.96157  ?  836  ASP B CA  1 
ATOM   3882 C  C   . ASP A 1 559 ? 24.13800  -23.09500 22.43500  1.000 70.98431  ?  836  ASP B C   1 
ATOM   3883 O  O   . ASP A 1 559 ? 24.08600  -24.13000 21.76300  1.000 74.53156  ?  836  ASP B O   1 
ATOM   3884 C  CB  . ASP A 1 559 ? 26.53500  -23.08500 23.12100  1.000 65.60820  ?  836  ASP B CB  1 
ATOM   3885 C  CG  . ASP A 1 559 ? 26.34400  -23.17500 24.61900  1.000 81.42572  ?  836  ASP B CG  1 
ATOM   3886 O  OD1 . ASP A 1 559 ? 25.80400  -22.21400 25.21000  1.000 69.57476  ?  836  ASP B OD1 1 
ATOM   3887 O  OD2 . ASP A 1 559 ? 26.73100  -24.20300 25.21000  1.000 88.75051  -1 836  ASP B OD2 1 
ATOM   3888 N  N   . LYS A 1 560 ? 23.10800  -22.67500 23.16800  1.000 66.26517  ?  837  LYS B N   1 
ATOM   3889 C  CA  . LYS A 1 560 ? 21.82600  -23.36800 23.19600  1.000 65.34471  ?  837  LYS B CA  1 
ATOM   3890 C  C   . LYS A 1 560 ? 20.72600  -22.58800 22.49300  1.000 65.29211  ?  837  LYS B C   1 
ATOM   3891 O  O   . LYS A 1 560 ? 19.58000  -23.04800 22.45600  1.000 65.01768  ?  837  LYS B O   1 
ATOM   3892 C  CB  . LYS A 1 560 ? 21.40400  -23.64600 24.64400  1.000 72.28185  ?  837  LYS B CB  1 
ATOM   3893 C  CG  . LYS A 1 560 ? 22.53900  -24.07800 25.56000  1.000 75.53480  ?  837  LYS B CG  1 
ATOM   3894 C  CD  . LYS A 1 560 ? 23.14600  -25.39900 25.11800  1.000 85.39800  ?  837  LYS B CD  1 
ATOM   3895 C  CE  . LYS A 1 560 ? 24.27200  -25.82900 26.04600  1.000 88.01556  ?  837  LYS B CE  1 
ATOM   3896 N  NZ  . LYS A 1 560 ? 24.91400  -27.09000 25.58400  1.000 96.60684  ?  837  LYS B NZ  1 
ATOM   3897 N  N   . THR A 1 561 ? 21.04900  -21.42400 21.93000  1.000 59.85980  ?  838  THR B N   1 
ATOM   3898 C  CA  . THR A 1 561 ? 20.03200  -20.54400 21.35900  1.000 61.51030  ?  838  THR B CA  1 
ATOM   3899 C  C   . THR A 1 561 ? 19.33900  -21.16300 20.14600  1.000 60.48235  ?  838  THR B C   1 
ATOM   3900 O  O   . THR A 1 561 ? 18.10500  -21.23900 20.09900  1.000 64.17984  ?  838  THR B O   1 
ATOM   3901 C  CB  . THR A 1 561 ? 20.67500  -19.21600 20.98000  1.000 62.64222  ?  838  THR B CB  1 
ATOM   3902 O  OG1 . THR A 1 561 ? 21.18500  -18.59200 22.16500  1.000 67.95443  ?  838  THR B OG1 1 
ATOM   3903 C  CG2 . THR A 1 561 ? 19.66500  -18.29500 20.26800  1.000 52.40147  ?  838  THR B CG2 1 
ATOM   3904 N  N   . VAL A 1 562 ? 20.10900  -21.58300 19.14200  1.000 58.19622  ?  839  VAL B N   1 
ATOM   3905 C  CA  . VAL A 1 562 ? 19.49600  -22.10000 17.92100  1.000 57.80134  ?  839  VAL B CA  1 
ATOM   3906 C  C   . VAL A 1 562 ? 18.68500  -23.35400 18.22500  1.000 58.53355  ?  839  VAL B C   1 
ATOM   3907 O  O   . VAL A 1 562 ? 17.52700  -23.47500 17.81000  1.000 56.14215  ?  839  VAL B O   1 
ATOM   3908 C  CB  . VAL A 1 562 ? 20.57300  -22.34300 16.84200  1.000 57.24370  ?  839  VAL B CB  1 
ATOM   3909 C  CG1 . VAL A 1 562 ? 19.96900  -23.03200 15.62600  1.000 59.14297  ?  839  VAL B CG1 1 
ATOM   3910 C  CG2 . VAL A 1 562 ? 21.18400  -21.01000 16.41000  1.000 52.93862  ?  839  VAL B CG2 1 
ATOM   3911 N  N   . LYS A 1 563 ? 19.26100  -24.26700 19.01200  1.000 54.80285  ?  840  LYS B N   1 
ATOM   3912 C  CA  . LYS A 1 563 ? 18.54900  -25.47900 19.41000  1.000 62.41760  ?  840  LYS B CA  1 
ATOM   3913 C  C   . LYS A 1 563 ? 17.21400  -25.15000 20.06500  1.000 68.42166  ?  840  LYS B C   1 
ATOM   3914 O  O   . LYS A 1 563 ? 16.20400  -25.81800 19.80300  1.000 65.53956  ?  840  LYS B O   1 
ATOM   3915 C  CB  . LYS A 1 563 ? 19.42900  -26.30800 20.35200  1.000 54.32890  ?  840  LYS B CB  1 
ATOM   3916 C  CG  . LYS A 1 563 ? 18.88700  -27.68700 20.69400  1.000 71.28676  ?  840  LYS B CG  1 
ATOM   3917 C  CD  . LYS A 1 563 ? 18.83900  -28.59400 19.47400  1.000 76.66339  ?  840  LYS B CD  1 
ATOM   3918 C  CE  . LYS A 1 563 ? 18.79200  -30.06100 19.87700  1.000 79.93799  ?  840  LYS B CE  1 
ATOM   3919 N  NZ  . LYS A 1 563 ? 17.71000  -30.35300 20.85800  1.000 76.80506  ?  840  LYS B NZ  1 
ATOM   3920 N  N   . LYS A 1 564 ? 17.18200  -24.12100 20.91700  1.000 61.60245  ?  841  LYS B N   1 
ATOM   3921 C  CA  . LYS A 1 564 ? 15.93100  -23.73000 21.55700  1.000 63.58946  ?  841  LYS B CA  1 
ATOM   3922 C  C   . LYS A 1 564 ? 14.85300  -23.43400 20.51900  1.000 63.28481  ?  841  LYS B C   1 
ATOM   3923 O  O   . LYS A 1 564 ? 13.68600  -23.79200 20.71300  1.000 66.92292  ?  841  LYS B O   1 
ATOM   3924 C  CB  . LYS A 1 564 ? 16.14300  -22.50700 22.45700  1.000 66.90427  ?  841  LYS B CB  1 
ATOM   3925 C  CG  . LYS A 1 564 ? 16.85500  -22.73400 23.79500  1.000 62.22953  ?  841  LYS B CG  1 
ATOM   3926 C  CD  . LYS A 1 564 ? 17.13100  -21.36400 24.44300  1.000 58.92259  ?  841  LYS B CD  1 
ATOM   3927 C  CE  . LYS A 1 564 ? 17.99900  -21.46000 25.67400  1.000 64.34301  ?  841  LYS B CE  1 
ATOM   3928 N  N   . VAL A 1 565 ? 15.22000  -22.76500 19.41400  1.000 59.10271  ?  842  VAL B N   1 
ATOM   3929 C  CA  . VAL A 1 565 ? 14.25800  -22.47600 18.34800  1.000 57.93879  ?  842  VAL B CA  1 
ATOM   3930 C  C   . VAL A 1 565 ? 14.02300  -23.71400 17.48800  1.000 62.25398  ?  842  VAL B C   1 
ATOM   3931 O  O   . VAL A 1 565 ? 12.89100  -23.99500 17.07600  1.000 62.92063  ?  842  VAL B O   1 
ATOM   3932 C  CB  . VAL A 1 565 ? 14.73200  -21.29000 17.48100  1.000 59.00895  ?  842  VAL B CB  1 
ATOM   3933 C  CG1 . VAL A 1 565 ? 13.73700  -21.02500 16.35900  1.000 52.83001  ?  842  VAL B CG1 1 
ATOM   3934 C  CG2 . VAL A 1 565 ? 14.96900  -20.02100 18.31500  1.000 54.22958  ?  842  VAL B CG2 1 
ATOM   3935 N  N   . GLN A 1 566 ? 15.09100  -24.45800 17.19400  1.000 57.58250  ?  843  GLN B N   1 
ATOM   3936 C  CA  . GLN A 1 566 ? 14.99100  -25.65000 16.35900  1.000 59.64982  ?  843  GLN B CA  1 
ATOM   3937 C  C   . GLN A 1 566 ? 13.99400  -26.65300 16.94200  1.000 64.74963  ?  843  GLN B C   1 
ATOM   3938 O  O   . GLN A 1 566 ? 13.11400  -27.15200 16.23000  1.000 64.05756  ?  843  GLN B O   1 
ATOM   3939 C  CB  . GLN A 1 566 ? 16.38800  -26.26800 16.20700  1.000 60.97169  ?  843  GLN B CB  1 
ATOM   3940 C  CG  . GLN A 1 566 ? 16.51800  -27.40000 15.19000  1.000 56.53626  ?  843  GLN B CG  1 
ATOM   3941 C  CD  . GLN A 1 566 ? 17.81800  -28.18900 15.36100  1.000 68.25262  ?  843  GLN B CD  1 
ATOM   3942 O  OE1 . GLN A 1 566 ? 18.90800  -27.70500 15.03900  1.000 72.85830  ?  843  GLN B OE1 1 
ATOM   3943 N  NE2 . GLN A 1 566 ? 17.70300  -29.40800 15.88100  1.000 68.01115  ?  843  GLN B NE2 1 
ATOM   3944 N  N   . ASP A 1 567 ? 14.10600  -26.94800 18.24600  1.000 63.75294  ?  844  ASP B N   1 
ATOM   3945 C  CA  . ASP A 1 567 ? 13.19300  -27.88600 18.90200  1.000 65.72180  ?  844  ASP B CA  1 
ATOM   3946 C  C   . ASP A 1 567 ? 11.72500  -27.50900 18.69800  1.000 67.37393  ?  844  ASP B C   1 
ATOM   3947 O  O   . ASP A 1 567 ? 10.86600  -28.39000 18.56200  1.000 67.17217  ?  844  ASP B O   1 
ATOM   3948 C  CB  . ASP A 1 567 ? 13.48300  -27.95700 20.40600  1.000 70.66987  ?  844  ASP B CB  1 
ATOM   3949 C  CG  . ASP A 1 567 ? 14.80500  -28.62200 20.72500  1.000 78.80908  ?  844  ASP B CG  1 
ATOM   3950 O  OD1 . ASP A 1 567 ? 15.29200  -29.41500 19.88700  1.000 73.67744  ?  844  ASP B OD1 1 
ATOM   3951 O  OD2 . ASP A 1 567 ? 15.35000  -28.34900 21.82400  1.000 78.80569  -1 844  ASP B OD2 1 
ATOM   3952 N  N   . LYS A 1 568 ? 11.40800  -26.20600 18.72200  1.000 63.15488  ?  845  LYS B N   1 
ATOM   3953 C  CA  . LYS A 1 568 ? 10.01000  -25.78900 18.60900  1.000 61.91436  ?  845  LYS B CA  1 
ATOM   3954 C  C   . LYS A 1 568 ? 9.39000   -26.20800 17.27500  1.000 63.37747  ?  845  LYS B C   1 
ATOM   3955 O  O   . LYS A 1 568 ? 8.17800   -26.43800 17.19600  1.000 62.96610  ?  845  LYS B O   1 
ATOM   3956 C  CB  . LYS A 1 568 ? 9.89500   -24.27500 18.79400  1.000 63.21971  ?  845  LYS B CB  1 
ATOM   3957 C  CG  . LYS A 1 568 ? 10.26600  -23.77400 20.18000  1.000 63.84155  ?  845  LYS B CG  1 
ATOM   3958 C  CD  . LYS A 1 568 ? 9.15800   -24.08500 21.17300  1.000 62.94814  ?  845  LYS B CD  1 
ATOM   3959 C  CE  . LYS A 1 568 ? 9.61500   -23.87200 22.61000  1.000 62.76291  ?  845  LYS B CE  1 
ATOM   3960 N  NZ  . LYS A 1 568 ? 9.96400   -22.44000 22.87100  1.000 69.22320  ?  845  LYS B NZ  1 
ATOM   3961 N  N   . PHE A 1 569 ? 10.19000  -26.29700 16.21200  1.000 64.71753  ?  846  PHE B N   1 
ATOM   3962 C  CA  . PHE A 1 569 ? 9.65200   -26.71200 14.92000  1.000 64.49611  ?  846  PHE B CA  1 
ATOM   3963 C  C   . PHE A 1 569 ? 9.27800   -28.19500 14.88400  1.000 71.01755  ?  846  PHE B C   1 
ATOM   3964 O  O   . PHE A 1 569 ? 8.50500   -28.60600 14.00800  1.000 69.75627  ?  846  PHE B O   1 
ATOM   3965 C  CB  . PHE A 1 569 ? 10.65700  -26.40000 13.80300  1.000 60.45465  ?  846  PHE B CB  1 
ATOM   3966 C  CG  . PHE A 1 569 ? 10.78100  -24.93200 13.47700  1.000 60.10462  ?  846  PHE B CG  1 
ATOM   3967 C  CD1 . PHE A 1 569 ? 9.67800   -24.19900 13.06300  1.000 58.81294  ?  846  PHE B CD1 1 
ATOM   3968 C  CD2 . PHE A 1 569 ? 12.01200  -24.29200 13.55300  1.000 60.84074  ?  846  PHE B CD2 1 
ATOM   3969 C  CE1 . PHE A 1 569 ? 9.80300   -22.85000 12.74300  1.000 58.74036  ?  846  PHE B CE1 1 
ATOM   3970 C  CE2 . PHE A 1 569 ? 12.13900  -22.94600 13.23600  1.000 56.76047  ?  846  PHE B CE2 1 
ATOM   3971 C  CZ  . PHE A 1 569 ? 11.03100  -22.22400 12.82700  1.000 57.88236  ?  846  PHE B CZ  1 
ATOM   3972 N  N   . ARG A 1 570 ? 9.79600   -29.00700 15.80200  1.000 72.61337  ?  847  ARG B N   1 
ATOM   3973 C  CA  . ARG A 1 570 ? 9.53700   -30.44100 15.79100  1.000 72.43947  ?  847  ARG B CA  1 
ATOM   3974 C  C   . ARG A 1 570 ? 9.76000   -31.00300 14.39100  1.000 78.14301  ?  847  ARG B C   1 
ATOM   3975 O  O   . ARG A 1 570 ? 8.92800   -31.72400 13.83700  1.000 79.34831  ?  847  ARG B O   1 
ATOM   3976 C  CB  . ARG A 1 570 ? 8.12000   -30.75600 16.28400  1.000 77.58154  ?  847  ARG B CB  1 
ATOM   3977 C  CG  . ARG A 1 570 ? 7.79900   -30.31100 17.71500  1.000 73.77132  ?  847  ARG B CG  1 
ATOM   3978 C  CD  . ARG A 1 570 ? 8.66800   -31.02000 18.73500  1.000 72.88065  ?  847  ARG B CD  1 
ATOM   3979 N  NE  . ARG A 1 570 ? 8.82100   -32.43300 18.42100  1.000 79.51107  ?  847  ARG B NE  1 
ATOM   3980 C  CZ  . ARG A 1 570 ? 8.12200   -33.40900 18.98300  1.000 83.24833  ?  847  ARG B CZ  1 
ATOM   3981 N  NH1 . ARG A 1 570 ? 7.23000   -33.16400 19.92700  1.000 82.57033  ?  847  ARG B NH1 1 
ATOM   3982 N  NH2 . ARG A 1 570 ? 8.31800   -34.66300 18.58200  1.000 76.31197  ?  847  ARG B NH2 1 
ATOM   3983 N  N   . LEU A 1 571 ? 10.90100  -30.64500 13.80500  1.000 79.07328  ?  848  LEU B N   1 
ATOM   3984 C  CA  . LEU A 1 571 ? 11.24800  -31.13800 12.47700  1.000 77.75552  ?  848  LEU B CA  1 
ATOM   3985 C  C   . LEU A 1 571 ? 11.29200  -32.66300 12.39500  1.000 84.27283  ?  848  LEU B C   1 
ATOM   3986 O  O   . LEU A 1 571 ? 11.35500  -33.20800 11.28500  1.000 80.63225  ?  848  LEU B O   1 
ATOM   3987 C  CB  . LEU A 1 571 ? 12.58300  -30.53400 12.05900  1.000 67.78609  ?  848  LEU B CB  1 
ATOM   3988 C  CG  . LEU A 1 571 ? 12.43900  -29.01900 11.95100  1.000 70.07307  ?  848  LEU B CG  1 
ATOM   3989 C  CD1 . LEU A 1 571 ? 13.77900  -28.36500 11.75700  1.000 65.96111  ?  848  LEU B CD1 1 
ATOM   3990 C  CD2 . LEU A 1 571 ? 11.50100  -28.69200 10.80700  1.000 72.92792  ?  848  LEU B CD2 1 
ATOM   3991 N  N   . ASP A 1 572 ? 11.19200  -33.34000 13.54300  1.000 87.94830  ?  849  ASP B N   1 
ATOM   3992 C  CA  . ASP A 1 572 ? 11.21200  -34.82900 13.57600  1.000 91.36773  ?  849  ASP B CA  1 
ATOM   3993 C  C   . ASP A 1 572 ? 9.84400   -35.38500 13.16800  1.000 93.47168  ?  849  ASP B C   1 
ATOM   3994 O  O   . ASP A 1 572 ? 9.77900   -36.58000 12.82600  1.000 97.93391  ?  849  ASP B O   1 
ATOM   3995 C  CB  . ASP A 1 572 ? 11.62600  -35.34100 14.95800  1.000 93.21383  ?  849  ASP B CB  1 
ATOM   3996 C  CG  . ASP A 1 572 ? 10.82000  -34.74600 16.10000  1.000 99.03019  ?  849  ASP B CG  1 
ATOM   3997 O  OD1 . ASP A 1 572 ? 9.94400   -33.90300 15.82700  1.000 91.85785  ?  849  ASP B OD1 1 
ATOM   3998 O  OD2 . ASP A 1 572 ? 11.07400  -35.13300 17.25700  1.000 101.64818 -1 849  ASP B OD2 1 
ATOM   3999 N  N   . LEU A 1 573 ? 8.79700   -34.55900 13.20400  1.000 89.23524  ?  850  LEU B N   1 
ATOM   4000 C  CA  . LEU A 1 573 ? 7.45200   -35.00200 12.88200  1.000 89.10893  ?  850  LEU B CA  1 
ATOM   4001 C  C   . LEU A 1 573 ? 7.14100   -34.73700 11.41800  1.000 85.02804  ?  850  LEU B C   1 
ATOM   4002 O  O   . LEU A 1 573 ? 7.54700   -33.71100 10.86100  1.000 83.85791  ?  850  LEU B O   1 
ATOM   4003 C  CB  . LEU A 1 573 ? 6.43500   -34.27900 13.76700  1.000 88.09753  ?  850  LEU B CB  1 
ATOM   4004 C  CG  . LEU A 1 573 ? 6.68700   -34.30100 15.28000  1.000 86.31253  ?  850  LEU B CG  1 
ATOM   4005 C  CD1 . LEU A 1 573 ? 5.54200   -33.62800 16.01300  1.000 79.78885  ?  850  LEU B CD1 1 
ATOM   4006 C  CD2 . LEU A 1 573 ? 6.89300   -35.73400 15.79200  1.000 86.02839  ?  850  LEU B CD2 1 
ATOM   4007 N  N   . SER A 1 574 ? 6.41100   -35.66100 10.79900  1.000 86.20995  ?  851  SER B N   1 
ATOM   4008 C  CA  . SER A 1 574 ? 5.85100   -35.38200 9.49000   1.000 84.60783  ?  851  SER B CA  1 
ATOM   4009 C  C   . SER A 1 574 ? 4.81700   -34.26700 9.61100   1.000 91.16800  ?  851  SER B C   1 
ATOM   4010 O  O   . SER A 1 574 ? 4.45100   -33.84100 10.71000  1.000 91.94107  ?  851  SER B O   1 
ATOM   4011 C  CB  . SER A 1 574 ? 5.20600   -36.63100 8.89400   1.000 91.66661  ?  851  SER B CB  1 
ATOM   4012 O  OG  . SER A 1 574 ? 3.87800   -36.78400 9.36800   1.000 93.50727  ?  851  SER B OG  1 
ATOM   4013 N  N   . ASP A 1 575 ? 4.34100   -33.78000 8.46300   1.000 91.43505  ?  852  ASP B N   1 
ATOM   4014 C  CA  . ASP A 1 575 ? 3.30100   -32.75400 8.49100   1.000 91.09417  ?  852  ASP B CA  1 
ATOM   4015 C  C   . ASP A 1 575 ? 2.05500   -33.26700 9.20200   1.000 92.47147  ?  852  ASP B C   1 
ATOM   4016 O  O   . ASP A 1 575 ? 1.50800   -32.59500 10.08500  1.000 87.59778  ?  852  ASP B O   1 
ATOM   4017 C  CB  . ASP A 1 575 ? 2.97100   -32.29300 7.07100   1.000 98.19768  ?  852  ASP B CB  1 
ATOM   4018 C  CG  . ASP A 1 575 ? 4.03800   -31.38700 6.50000   1.000 102.38750 ?  852  ASP B CG  1 
ATOM   4019 O  OD1 . ASP A 1 575 ? 4.93000   -30.99100 7.27700   1.000 100.59582 ?  852  ASP B OD1 1 
ATOM   4020 O  OD2 . ASP A 1 575 ? 3.99400   -31.08200 5.28800   1.000 112.16294 -1 852  ASP B OD2 1 
ATOM   4021 N  N   . GLU A 1 576 ? 1.59700   -34.46800 8.82900   1.000 99.76566  ?  853  GLU B N   1 
ATOM   4022 C  CA  . GLU A 1 576 ? 0.49300   -35.11200 9.53400   1.000 90.72330  ?  853  GLU B CA  1 
ATOM   4023 C  C   . GLU A 1 576 ? 0.72800   -35.09700 11.03800  1.000 89.06261  ?  853  GLU B C   1 
ATOM   4024 O  O   . GLU A 1 576 ? -0.11900  -34.63400 11.81000  1.000 89.44650  ?  853  GLU B O   1 
ATOM   4025 C  CB  . GLU A 1 576 ? 0.32200   -36.54400 9.02600   1.000 89.44624  ?  853  GLU B CB  1 
ATOM   4026 N  N   . GLU A 1 577 ? 1.89600   -35.57700 11.47000  1.000 87.59670  ?  854  GLU B N   1 
ATOM   4027 C  CA  . GLU A 1 577 ? 2.20100   -35.63900 12.89600  1.000 86.94472  ?  854  GLU B CA  1 
ATOM   4028 C  C   . GLU A 1 577 ? 2.32200   -34.24400 13.50900  1.000 92.95128  ?  854  GLU B C   1 
ATOM   4029 O  O   . GLU A 1 577 ? 1.88800   -34.01900 14.64400  1.000 93.55764  ?  854  GLU B O   1 
ATOM   4030 C  CB  . GLU A 1 577 ? 3.47900   -36.44900 13.10800  1.000 91.25288  ?  854  GLU B CB  1 
ATOM   4031 C  CG  . GLU A 1 577 ? 3.38800   -37.87100 12.54000  1.000 91.69200  ?  854  GLU B CG  1 
ATOM   4032 C  CD  . GLU A 1 577 ? 4.68600   -38.63700 12.65800  1.000 92.36152  ?  854  GLU B CD  1 
ATOM   4033 O  OE2 . GLU A 1 577 ? 5.75100   -37.98800 12.59500  1.000 100.46911 -1 854  GLU B OE2 1 
ATOM   4034 N  N   . ALA A 1 578 ? 2.90000   -33.29100 12.77700  1.000 92.75124  ?  855  ALA B N   1 
ATOM   4035 C  CA  . ALA A 1 578 ? 3.03100   -31.94100 13.30900  1.000 88.23322  ?  855  ALA B CA  1 
ATOM   4036 C  C   . ALA A 1 578 ? 1.66900   -31.33600 13.62000  1.000 88.20804  ?  855  ALA B C   1 
ATOM   4037 O  O   . ALA A 1 578 ? 1.51400   -30.60500 14.60500  1.000 87.90377  ?  855  ALA B O   1 
ATOM   4038 C  CB  . ALA A 1 578 ? 3.79400   -31.06000 12.32000  1.000 86.77055  ?  855  ALA B CB  1 
ATOM   4039 N  N   . VAL A 1 579 ? 0.67200   -31.62100 12.78800  1.000 87.86731  ?  856  VAL B N   1 
ATOM   4040 C  CA  . VAL A 1 579 ? -0.64900  -31.03900 12.99200  1.000 89.26524  ?  856  VAL B CA  1 
ATOM   4041 C  C   . VAL A 1 579 ? -1.30000  -31.61200 14.24800  1.000 94.27676  ?  856  VAL B C   1 
ATOM   4042 O  O   . VAL A 1 579 ? -1.91500  -30.87900 15.03700  1.000 94.64661  ?  856  VAL B O   1 
ATOM   4043 C  CB  . VAL A 1 579 ? -1.51300  -31.26600 11.73900  1.000 90.70795  ?  856  VAL B CB  1 
ATOM   4044 C  CG1 . VAL A 1 579 ? -2.95700  -30.91100 12.01900  1.000 86.35789  ?  856  VAL B CG1 1 
ATOM   4045 C  CG2 . VAL A 1 579 ? -0.95900  -30.44500 10.56700  1.000 82.37256  ?  856  VAL B CG2 1 
ATOM   4046 N  N   . HIS A 1 580 ? -1.17800  -32.92700 14.45300  1.000 91.23265  ?  857  HIS B N   1 
ATOM   4047 C  CA  . HIS A 1 580 ? -1.66300  -33.53700 15.68900  1.000 95.77693  ?  857  HIS B CA  1 
ATOM   4048 C  C   . HIS A 1 580 ? -0.97700  -32.92200 16.90500  1.000 95.01510  ?  857  HIS B C   1 
ATOM   4049 O  O   . HIS A 1 580 ? -1.63300  -32.56600 17.89400  1.000 95.41272  ?  857  HIS B O   1 
ATOM   4050 C  CB  . HIS A 1 580 ? -1.43600  -35.05200 15.64300  1.000 102.93984 ?  857  HIS B CB  1 
ATOM   4051 C  CG  . HIS A 1 580 ? -1.91500  -35.77900 16.86100  1.000 110.76445 ?  857  HIS B CG  1 
ATOM   4052 N  ND1 . HIS A 1 580 ? -1.18100  -35.84500 18.02600  1.000 117.38118 ?  857  HIS B ND1 1 
ATOM   4053 C  CD2 . HIS A 1 580 ? -3.05400  -36.47400 17.09500  1.000 115.74376 ?  857  HIS B CD2 1 
ATOM   4054 C  CE1 . HIS A 1 580 ? -1.84700  -36.54800 18.92600  1.000 115.85491 ?  857  HIS B CE1 1 
ATOM   4055 N  NE2 . HIS A 1 580 ? -2.98700  -36.94100 18.38700  1.000 119.40842 ?  857  HIS B NE2 1 
ATOM   4056 N  N   . TYR A 1 581 ? 0.34900   -32.77500 16.83900  1.000 92.45198  ?  858  TYR B N   1 
ATOM   4057 C  CA  . TYR A 1 581 ? 1.09600   -32.19200 17.94900  1.000 90.22044  ?  858  TYR B CA  1 
ATOM   4058 C  C   . TYR A 1 581 ? 0.58800   -30.79200 18.27600  1.000 92.76429  ?  858  TYR B C   1 
ATOM   4059 O  O   . TYR A 1 581 ? 0.28600   -30.48200 19.43600  1.000 94.14638  ?  858  TYR B O   1 
ATOM   4060 C  CB  . TYR A 1 581 ? 2.58600   -32.17700 17.60700  1.000 84.26352  ?  858  TYR B CB  1 
ATOM   4061 C  CG  . TYR A 1 581 ? 3.43700   -31.27300 18.46900  1.000 86.67086  ?  858  TYR B CG  1 
ATOM   4062 C  CD1 . TYR A 1 581 ? 3.93800   -31.70800 19.69000  1.000 82.74899  ?  858  TYR B CD1 1 
ATOM   4063 C  CD2 . TYR A 1 581 ? 3.76200   -29.99000 18.04800  1.000 79.93449  ?  858  TYR B CD2 1 
ATOM   4064 C  CE1 . TYR A 1 581 ? 4.73000   -30.88500 20.47500  1.000 84.27215  ?  858  TYR B CE1 1 
ATOM   4065 C  CE2 . TYR A 1 581 ? 4.55400   -29.15700 18.82300  1.000 82.72801  ?  858  TYR B CE2 1 
ATOM   4066 C  CZ  . TYR A 1 581 ? 5.03400   -29.60900 20.03600  1.000 82.49234  ?  858  TYR B CZ  1 
ATOM   4067 O  OH  . TYR A 1 581 ? 5.82200   -28.78100 20.80700  1.000 79.83595  ?  858  TYR B OH  1 
ATOM   4068 N  N   . MET A 1 582 ? 0.47900   -29.93400 17.25600  1.000 89.77258  ?  859  MET B N   1 
ATOM   4069 C  CA  . MET A 1 582 ? -0.04100  -28.58600 17.46500  1.000 86.71445  ?  859  MET B CA  1 
ATOM   4070 C  C   . MET A 1 582 ? -1.47100  -28.61000 17.99300  1.000 89.08157  ?  859  MET B C   1 
ATOM   4071 O  O   . MET A 1 582 ? -1.86400  -27.72000 18.75400  1.000 86.72376  ?  859  MET B O   1 
ATOM   4072 C  CB  . MET A 1 582 ? 0.03800   -27.79500 16.16000  1.000 74.06212  ?  859  MET B CB  1 
ATOM   4073 C  CG  . MET A 1 582 ? -0.46200  -26.37000 16.25900  1.000 76.60516  ?  859  MET B CG  1 
ATOM   4074 S  SD  . MET A 1 582 ? 0.48500   -25.37500 17.42400  1.000 76.02248  ?  859  MET B SD  1 
ATOM   4075 C  CE  . MET A 1 582 ? 2.05000   -25.19200 16.56400  1.000 66.84493  ?  859  MET B CE  1 
ATOM   4076 N  N   . GLN A 1 583 ? -2.26500  -29.61200 17.59800  1.000 92.72161  ?  860  GLN B N   1 
ATOM   4077 C  CA  . GLN A 1 583 ? -3.60700  -29.74600 18.15200  1.000 92.26711  ?  860  GLN B CA  1 
ATOM   4078 C  C   . GLN A 1 583 ? -3.54900  -30.03500 19.64700  1.000 93.55845  ?  860  GLN B C   1 
ATOM   4079 O  O   . GLN A 1 583 ? -4.29000  -29.43500 20.43300  1.000 91.74839  ?  860  GLN B O   1 
ATOM   4080 C  CB  . GLN A 1 583 ? -4.37700  -30.84700 17.42000  1.000 91.13296  ?  860  GLN B CB  1 
ATOM   4081 N  N   A SER A 1 584 ? -2.66600  -30.94900 20.06200  0.569 93.70640  ?  861  SER B N   1 
ATOM   4082 N  N   B SER A 1 584 ? -2.67900  -30.96600 20.05300  0.431 93.65963  ?  861  SER B N   1 
ATOM   4083 C  CA  A SER A 1 584 ? -2.53200  -31.25300 21.48300  0.569 92.37733  ?  861  SER B CA  1 
ATOM   4084 C  CA  B SER A 1 584 ? -2.51200  -31.25600 21.47300  0.431 92.42485  ?  861  SER B CA  1 
ATOM   4085 C  C   A SER A 1 584 ? -1.91800  -30.09100 22.25300  0.569 92.94774  ?  861  SER B C   1 
ATOM   4086 C  C   B SER A 1 584 ? -1.98200  -30.04000 22.22000  0.431 92.96447  ?  861  SER B C   1 
ATOM   4087 O  O   A SER A 1 584 ? -2.24400  -29.88700 23.42800  0.569 95.64453  ?  861  SER B O   1 
ATOM   4088 O  O   B SER A 1 584 ? -2.42200  -29.74500 23.33800  0.431 95.51068  ?  861  SER B O   1 
ATOM   4089 C  CB  A SER A 1 584 ? -1.69800  -32.51800 21.67400  0.569 93.54899  ?  861  SER B CB  1 
ATOM   4090 C  CB  B SER A 1 584 ? -1.56900  -32.44200 21.66100  0.431 93.57641  ?  861  SER B CB  1 
ATOM   4091 O  OG  A SER A 1 584 ? -2.30300  -33.62300 21.02600  0.569 97.35117  ?  861  SER B OG  1 
ATOM   4092 O  OG  B SER A 1 584 ? -0.22800  -32.06300 21.39800  0.431 93.74513  ?  861  SER B OG  1 
ATOM   4093 N  N   . LEU A 1 585 ? -1.03300  -29.32000 21.61800  1.000 93.91189  ?  862  LEU B N   1 
ATOM   4094 C  CA  . LEU A 1 585 ? -0.46700  -28.15300 22.28100  1.000 87.47723  ?  862  LEU B CA  1 
ATOM   4095 C  C   . LEU A 1 585 ? -1.55400  -27.15000 22.64500  1.000 86.42810  ?  862  LEU B C   1 
ATOM   4096 O  O   . LEU A 1 585 ? -1.51800  -26.54600 23.72300  1.000 88.70498  ?  862  LEU B O   1 
ATOM   4097 C  CB  . LEU A 1 585 ? 0.57800   -27.50800 21.37800  1.000 87.57198  ?  862  LEU B CB  1 
ATOM   4098 C  CG  . LEU A 1 585 ? 1.76200   -26.86900 22.08300  1.000 84.67611  ?  862  LEU B CG  1 
ATOM   4099 C  CD1 . LEU A 1 585 ? 2.45000   -27.91700 22.93600  1.000 87.77788  ?  862  LEU B CD1 1 
ATOM   4100 C  CD2 . LEU A 1 585 ? 2.70400   -26.32300 21.04300  1.000 81.67449  ?  862  LEU B CD2 1 
ATOM   4101 N  N   . ILE A 1 586 ? -2.53100  -26.96300 21.75700  1.000 85.83816  ?  863  ILE B N   1 
ATOM   4102 C  CA  . ILE A 1 586 ? -3.62400  -26.02600 22.00000  1.000 85.45241  ?  863  ILE B CA  1 
ATOM   4103 C  C   . ILE A 1 586 ? -4.61500  -26.59100 23.01100  1.000 92.86656  ?  863  ILE B C   1 
ATOM   4104 O  O   . ILE A 1 586 ? -5.00500  -25.90900 23.96500  1.000 89.48795  ?  863  ILE B O   1 
ATOM   4105 C  CB  . ILE A 1 586 ? -4.32200  -25.68400 20.67300  1.000 81.75207  ?  863  ILE B CB  1 
ATOM   4106 C  CG1 . ILE A 1 586 ? -3.33500  -25.01700 19.71400  1.000 77.55374  ?  863  ILE B CG1 1 
ATOM   4107 C  CG2 . ILE A 1 586 ? -5.55800  -24.82700 20.91800  1.000 76.90330  ?  863  ILE B CG2 1 
ATOM   4108 C  CD1 . ILE A 1 586 ? -3.92400  -24.72700 18.38800  1.000 69.81437  ?  863  ILE B CD1 1 
ATOM   4109 N  N   . ASP A 1 587 ? -5.05500  -27.83600 22.80000  1.000 92.81736  ?  864  ASP B N   1 
ATOM   4110 C  CA  . ASP A 1 587 ? -6.01100  -28.46100 23.71200  1.000 94.35648  ?  864  ASP B CA  1 
ATOM   4111 C  C   . ASP A 1 587 ? -5.43800  -28.58300 25.12000  1.000 95.19502  ?  864  ASP B C   1 
ATOM   4112 O  O   . ASP A 1 587 ? -6.12900  -28.30000 26.10500  1.000 98.93912  ?  864  ASP B O   1 
ATOM   4113 C  CB  . ASP A 1 587 ? -6.42300  -29.84400 23.18800  1.000 95.76017  ?  864  ASP B CB  1 
ATOM   4114 C  CG  . ASP A 1 587 ? -7.16400  -29.78800 21.84500  1.000 99.23663  ?  864  ASP B CG  1 
ATOM   4115 O  OD1 . ASP A 1 587 ? -7.59600  -28.68700 21.41300  1.000 90.66703  ?  864  ASP B OD1 1 
ATOM   4116 O  OD2 . ASP A 1 587 ? -7.31400  -30.87200 21.22700  1.000 108.60130 -1 864  ASP B OD2 1 
ATOM   4117 N  N   . GLU A 1 588 ? -4.17900  -29.01800 25.23700  1.000 99.77073  ?  865  GLU B N   1 
ATOM   4118 C  CA  . GLU A 1 588 ? -3.54700  -29.13000 26.55100  1.000 101.18804 ?  865  GLU B CA  1 
ATOM   4119 C  C   . GLU A 1 588 ? -3.44500  -27.76700 27.22600  1.000 96.85314  ?  865  GLU B C   1 
ATOM   4120 O  O   . GLU A 1 588 ? -3.73900  -27.62400 28.41900  1.000 98.72870  ?  865  GLU B O   1 
ATOM   4121 C  CB  . GLU A 1 588 ? -2.16700  -29.78400 26.41100  1.000 103.90624 ?  865  GLU B CB  1 
ATOM   4122 C  CG  . GLU A 1 588 ? -1.27900  -29.71100 27.65600  1.000 108.64788 ?  865  GLU B CG  1 
ATOM   4123 C  CD  . GLU A 1 588 ? -0.11200  -28.73500 27.50200  1.000 110.91632 ?  865  GLU B CD  1 
ATOM   4124 O  OE1 . GLU A 1 588 ? -0.06100  -28.00100 26.49100  1.000 117.25388 ?  865  GLU B OE1 1 
ATOM   4125 O  OE2 . GLU A 1 588 ? 0.76500   -28.70400 28.39200  1.000 111.91116 -1 865  GLU B OE2 1 
ATOM   4126 N  N   . SER A 1 589 ? -3.03800  -26.74500 26.47000  1.000 96.53835  ?  866  SER B N   1 
ATOM   4127 C  CA  . SER A 1 589 ? -3.04200  -25.38800 27.00200  1.000 92.38653  ?  866  SER B CA  1 
ATOM   4128 C  C   . SER A 1 589 ? -4.45300  -24.95700 27.38700  1.000 90.88787  ?  866  SER B C   1 
ATOM   4129 O  O   . SER A 1 589 ? -4.65500  -24.33600 28.43500  1.000 88.07845  ?  866  SER B O   1 
ATOM   4130 C  CB  . SER A 1 589 ? -2.44100  -24.42200 25.97300  1.000 95.03397  ?  866  SER B CB  1 
ATOM   4131 O  OG  . SER A 1 589 ? -1.11500  -24.79800 25.61400  1.000 89.35221  ?  866  SER B OG  1 
ATOM   4132 N  N   . VAL A 1 590 ? -5.44300  -25.26900 26.54700  1.000 93.30335  ?  867  VAL B N   1 
ATOM   4133 C  CA  . VAL A 1 590 ? -6.82600  -24.92900 26.86700  1.000 88.77758  ?  867  VAL B CA  1 
ATOM   4134 C  C   . VAL A 1 590 ? -7.29500  -25.71200 28.08400  1.000 94.53413  ?  867  VAL B C   1 
ATOM   4135 O  O   . VAL A 1 590 ? -7.84900  -25.13900 29.03000  1.000 94.99494  ?  867  VAL B O   1 
ATOM   4136 C  CB  . VAL A 1 590 ? -7.74500  -25.17700 25.65900  1.000 88.51423  ?  867  VAL B CB  1 
ATOM   4137 N  N   . HIS A 1 591 ? -7.07600  -27.02900 28.07100  1.000 96.47476  ?  868  HIS B N   1 
ATOM   4138 C  CA  . HIS A 1 591 ? -7.51200  -27.88300 29.21100  1.000 100.48782 ?  868  HIS B CA  1 
ATOM   4139 C  C   . HIS A 1 591 ? -6.96200  -27.29200 30.51100  1.000 94.16892  ?  868  HIS B C   1 
ATOM   4140 O  O   . HIS A 1 591 ? -7.67700  -27.29900 31.53500  1.000 99.67600  ?  868  HIS B O   1 
ATOM   4141 C  CB  . HIS A 1 591 ? -7.05400  -29.33200 29.01100  1.000 96.47644  ?  868  HIS B CB  1 
ATOM   4142 N  N   . ALA A 1 592 ? -5.72800  -26.78700 30.46900  1.000 93.62108  ?  869  ALA B N   1 
ATOM   4143 C  CA  . ALA A 1 592 ? -5.10000  -26.21700 31.65300  1.000 96.44001  ?  869  ALA B CA  1 
ATOM   4144 C  C   . ALA A 1 592 ? -5.63000  -24.83300 32.01300  1.000 95.36648  ?  869  ALA B C   1 
ATOM   4145 O  O   . ALA A 1 592 ? -5.38100  -24.37000 33.12900  1.000 94.86954  ?  869  ALA B O   1 
ATOM   4146 C  CB  . ALA A 1 592 ? -3.58300  -26.13000 31.45300  1.000 97.64470  ?  869  ALA B CB  1 
ATOM   4147 N  N   . LEU A 1 593 ? -6.32000  -24.15200 31.10200  1.000 95.98580  ?  870  LEU B N   1 
ATOM   4148 C  CA  . LEU A 1 593 ? -6.76300  -22.77900 31.35300  1.000 93.64509  ?  870  LEU B CA  1 
ATOM   4149 C  C   . LEU A 1 593 ? -8.08900  -22.77600 32.10500  1.000 96.11369  ?  870  LEU B C   1 
ATOM   4150 O  O   . LEU A 1 593 ? -8.20800  -23.38200 33.17300  1.000 98.92140  ?  870  LEU B O   1 
ATOM   4151 C  CB  . LEU A 1 593 ? -6.88400  -21.98900 30.03600  1.000 90.18453  ?  870  LEU B CB  1 
ATOM   4152 C  CG  . LEU A 1 593 ? -5.63500  -21.24600 29.53400  1.000 77.96509  ?  870  LEU B CG  1 
HETATM 4153 O  O1  . MES B 2 .   ? 1.94100   0.15000   20.25500  1.000 45.58866  ?  901  MES B O1  1 
HETATM 4154 C  C2  . MES B 2 .   ? 3.21500   0.22800   19.60700  1.000 44.95847  ?  901  MES B C2  1 
HETATM 4155 C  C3  . MES B 2 .   ? 4.23500   -0.63600  20.31600  1.000 39.84300  ?  901  MES B C3  1 
HETATM 4156 N  N4  . MES B 2 .   ? 4.16500   -0.27700  21.74000  1.000 51.02757  ?  901  MES B N4  1 
HETATM 4157 C  C5  . MES B 2 .   ? 2.87000   -0.16400  22.40800  1.000 49.83071  ?  901  MES B C5  1 
HETATM 4158 C  C6  . MES B 2 .   ? 1.96100   0.70000   21.56100  1.000 51.20657  ?  901  MES B C6  1 
HETATM 4159 C  C7  . MES B 2 .   ? 5.02000   -1.14000  22.56700  1.000 47.84281  ?  901  MES B C7  1 
HETATM 4160 C  C8  . MES B 2 .   ? 5.80300   -0.33300  23.58500  1.000 64.64088  ?  901  MES B C8  1 
HETATM 4161 S  S   . MES B 2 .   ? 6.72700   -1.23000  24.65800  1.000 62.39703  ?  901  MES B S   1 
HETATM 4162 O  O1S . MES B 2 .   ? 7.63400   -2.24000  24.07000  1.000 48.68786  ?  901  MES B O1S 1 
HETATM 4163 O  O2S . MES B 2 .   ? 5.84300   -1.98900  25.58900  1.000 64.62120  ?  901  MES B O2S 1 
HETATM 4164 O  O3S . MES B 2 .   ? 7.54300   -0.19300  25.32900  1.000 63.24582  ?  901  MES B O3S 1 
HETATM 4165 H  H21 . MES B 2 .   ? 3.55700   1.26500   19.60000  1.000 53.95017  ?  901  MES B H21 1 
HETATM 4166 H  H22 . MES B 2 .   ? 3.11800   -0.10100  18.57000  1.000 53.95017  ?  901  MES B H22 1 
HETATM 4167 H  H31 . MES B 2 .   ? 4.00800   -1.69400  20.17500  1.000 47.81160  ?  901  MES B H31 1 
HETATM 4168 H  H32 . MES B 2 .   ? 5.23600   -0.45100  19.92200  1.000 47.81160  ?  901  MES B H32 1 
HETATM 4169 H  HN4 . MES B 2 .   ? 4.49000   0.67600   21.67500  1.000 61.23309  ?  901  MES B HN4 1 
HETATM 4170 H  H51 . MES B 2 .   ? 2.99700   0.28200   23.39700  1.000 59.79685  ?  901  MES B H51 1 
HETATM 4171 H  H52 . MES B 2 .   ? 2.42900   -1.15400  22.54100  1.000 59.79685  ?  901  MES B H52 1 
HETATM 4172 H  H61 . MES B 2 .   ? 0.95300   0.71600   21.98200  1.000 61.44788  ?  901  MES B H61 1 
HETATM 4173 H  H62 . MES B 2 .   ? 2.33000   1.72800   21.53500  1.000 61.44788  ?  901  MES B H62 1 
HETATM 4174 H  H71 . MES B 2 .   ? 4.40000   -1.87400  23.08700  1.000 57.41137  ?  901  MES B H71 1 
HETATM 4175 H  H72 . MES B 2 .   ? 5.71600   -1.68400  21.92400  1.000 57.41137  ?  901  MES B H72 1 
HETATM 4176 H  H81 . MES B 2 .   ? 6.46600   0.34700   23.04600  1.000 77.56905  ?  901  MES B H81 1 
HETATM 4177 H  H82 . MES B 2 .   ? 5.09700   0.27100   24.15900  1.000 77.56905  ?  901  MES B H82 1 
HETATM 4178 O  O1  . PG4 C 3 .   ? -1.69200  2.14300   23.57500  1.000 82.17365  ?  902  PG4 B O1  1 
HETATM 4179 C  C1  . PG4 C 3 .   ? -1.46900  0.79900   23.96200  1.000 65.27156  ?  902  PG4 B C1  1 
HETATM 4180 C  C2  . PG4 C 3 .   ? -0.70700  0.74900   25.24200  1.000 69.07696  ?  902  PG4 B C2  1 
HETATM 4181 O  O2  . PG4 C 3 .   ? 0.64400   1.13100   25.03700  1.000 78.64903  ?  902  PG4 B O2  1 
HETATM 4182 C  C3  . PG4 C 3 .   ? 1.45500   0.80500   26.16100  1.000 78.04831  ?  902  PG4 B C3  1 
HETATM 4183 C  C4  . PG4 C 3 .   ? 2.89400   1.12800   25.90300  1.000 77.97919  ?  902  PG4 B C4  1 
HETATM 4184 O  O3  . PG4 C 3 .   ? 3.50800   1.57700   27.10300  1.000 87.45121  ?  902  PG4 B O3  1 
HETATM 4185 C  C5  . PG4 C 3 .   ? 4.89300   1.80300   26.88300  1.000 78.93444  ?  902  PG4 B C5  1 
HETATM 4186 C  C6  . PG4 C 3 .   ? 5.40800   2.36100   28.16800  1.000 69.31140  ?  902  PG4 B C6  1 
HETATM 4187 O  O4  . PG4 C 3 .   ? 6.78400   2.60200   28.01200  1.000 77.87621  ?  902  PG4 B O4  1 
HETATM 4188 C  C7  . PG4 C 3 .   ? 7.43900   1.56300   28.72000  1.000 80.64201  ?  902  PG4 B C7  1 
HETATM 4189 C  C8  . PG4 C 3 .   ? 8.90600   1.86300   28.76500  1.000 79.12720  ?  902  PG4 B C8  1 
HETATM 4190 O  O5  . PG4 C 3 .   ? 9.61900   0.78600   29.34900  1.000 98.14270  ?  902  PG4 B O5  1 
HETATM 4191 H  HO1 . PG4 C 3 .   ? -1.76700  2.13000   22.72400  1.000 98.60837  ?  902  PG4 B HO1 1 
HETATM 4192 H  H11 . PG4 C 3 .   ? -2.32300  0.35400   24.08100  1.000 78.32587  ?  902  PG4 B H11 1 
HETATM 4193 H  H12 . PG4 C 3 .   ? -0.96200  0.34600   23.27000  1.000 78.32587  ?  902  PG4 B H12 1 
HETATM 4194 H  H21 . PG4 C 3 .   ? -1.11600  1.35500   25.88000  1.000 82.89236  ?  902  PG4 B H21 1 
HETATM 4195 H  H22 . PG4 C 3 .   ? -0.73300  -0.15500  25.59300  1.000 82.89236  ?  902  PG4 B H22 1 
HETATM 4196 H  H31 . PG4 C 3 .   ? 1.15000   1.31200   26.92900  1.000 93.65797  ?  902  PG4 B H31 1 
HETATM 4197 H  H32 . PG4 C 3 .   ? 1.37200   -0.14300  26.34600  1.000 93.65797  ?  902  PG4 B H32 1 
HETATM 4198 H  H41 . PG4 C 3 .   ? 3.35000   0.33300   25.58600  1.000 93.57503  ?  902  PG4 B H41 1 
HETATM 4199 H  H42 . PG4 C 3 .   ? 2.95200   1.82500   25.23100  1.000 93.57503  ?  902  PG4 B H42 1 
HETATM 4200 H  H51 . PG4 C 3 .   ? 5.34300   0.97100   26.66900  1.000 94.72133  ?  902  PG4 B H51 1 
HETATM 4201 H  H52 . PG4 C 3 .   ? 5.02400   2.43600   26.16000  1.000 94.72133  ?  902  PG4 B H52 1 
HETATM 4202 H  H61 . PG4 C 3 .   ? 4.94900   3.19000   28.37500  1.000 83.17368  ?  902  PG4 B H61 1 
HETATM 4203 H  H62 . PG4 C 3 .   ? 5.26500   1.72300   28.88500  1.000 83.17368  ?  902  PG4 B H62 1 
HETATM 4204 H  H71 . PG4 C 3 .   ? 7.08900   1.51100   29.62300  1.000 96.77041  ?  902  PG4 B H71 1 
HETATM 4205 H  H72 . PG4 C 3 .   ? 7.29300   0.71700   28.26900  1.000 96.77041  ?  902  PG4 B H72 1 
HETATM 4206 H  H81 . PG4 C 3 .   ? 9.23000   2.00700   27.86200  1.000 94.95264  ?  902  PG4 B H81 1 
HETATM 4207 H  H82 . PG4 C 3 .   ? 9.05200   2.66400   29.29200  1.000 94.95264  ?  902  PG4 B H82 1 
HETATM 4208 H  HO5 . PG4 C 3 .   ? 9.45800   0.09300   28.88200  1.000 117.77124 ?  902  PG4 B HO5 1 
HETATM 4209 S  S   . DMS D 4 .   ? 6.30600   8.33400   37.40000  1.000 94.61754  ?  903  DMS B S   1 
HETATM 4210 O  O   . DMS D 4 .   ? 5.93200   9.25900   36.25000  1.000 68.46175  ?  903  DMS B O   1 
HETATM 4211 C  C1  . DMS D 4 .   ? 5.42600   6.75100   37.34400  1.000 75.41935  ?  903  DMS B C1  1 
HETATM 4212 C  C2  . DMS D 4 .   ? 8.00100   7.68100   37.30100  1.000 67.31934  ?  903  DMS B C2  1 
HETATM 4213 H  H11 . DMS D 4 .   ? 4.47500   6.85900   37.79900  1.000 90.50322  ?  903  DMS B H11 1 
HETATM 4214 H  H12 . DMS D 4 .   ? 5.98400   6.01700   37.86400  1.000 90.50322  ?  903  DMS B H12 1 
HETATM 4215 H  H13 . DMS D 4 .   ? 5.30200   6.45100   36.33600  1.000 90.50322  ?  903  DMS B H13 1 
HETATM 4216 H  H21 . DMS D 4 .   ? 8.67600   8.38700   37.71000  1.000 80.78321  ?  903  DMS B H21 1 
HETATM 4217 H  H22 . DMS D 4 .   ? 8.25100   7.49900   36.28900  1.000 80.78321  ?  903  DMS B H22 1 
HETATM 4218 H  H23 . DMS D 4 .   ? 8.06300   6.77600   37.84800  1.000 80.78321  ?  903  DMS B H23 1 
HETATM 4219 C  C1  . PEG E 5 .   ? -1.28900  7.43200   25.45000  1.000 72.91319  ?  904  PEG B C1  1 
HETATM 4220 O  O1  . PEG E 5 .   ? -1.96400  7.08900   24.25300  1.000 72.31657  ?  904  PEG B O1  1 
HETATM 4221 C  C2  . PEG E 5 .   ? 0.00900   8.13600   25.17700  1.000 70.69556  ?  904  PEG B C2  1 
HETATM 4222 O  O2  . PEG E 5 .   ? 0.30200   9.03400   26.24500  1.000 74.33361  ?  904  PEG B O2  1 
HETATM 4223 C  C3  . PEG E 5 .   ? 0.85500   8.42100   27.40300  1.000 68.35188  ?  904  PEG B C3  1 
HETATM 4224 C  C4  . PEG E 5 .   ? -0.03400  8.68300   28.58400  1.000 74.28039  ?  904  PEG B C4  1 
HETATM 4225 O  O4  . PEG E 5 .   ? 0.43600   8.06100   29.77700  1.000 73.25958  ?  904  PEG B O4  1 
HETATM 4226 H  H11 . PEG E 5 .   ? -1.10600  6.62200   25.95100  1.000 87.49583  ?  904  PEG B H11 1 
HETATM 4227 H  H12 . PEG E 5 .   ? -1.85800  8.01600   25.97600  1.000 87.49583  ?  904  PEG B H12 1 
HETATM 4228 H  HO1 . PEG E 5 .   ? -1.45400  6.89100   23.60000  1.000 86.77988  ?  904  PEG B HO1 1 
HETATM 4229 H  H21 . PEG E 5 .   ? -0.06300  8.63400   24.34700  1.000 84.83467  ?  904  PEG B H21 1 
HETATM 4230 H  H22 . PEG E 5 .   ? 0.72100   7.48200   25.10000  1.000 84.83467  ?  904  PEG B H22 1 
HETATM 4231 H  H31 . PEG E 5 .   ? 1.73600   8.79000   27.57400  1.000 82.02225  ?  904  PEG B H31 1 
HETATM 4232 H  H32 . PEG E 5 .   ? 0.92800   7.46500   27.25900  1.000 82.02225  ?  904  PEG B H32 1 
HETATM 4233 H  H41 . PEG E 5 .   ? -0.92100  8.34300   28.38600  1.000 89.13647  ?  904  PEG B H41 1 
HETATM 4234 H  H42 . PEG E 5 .   ? -0.08100  9.64100   28.73100  1.000 89.13647  ?  904  PEG B H42 1 
HETATM 4235 H  HO4 . PEG E 5 .   ? 1.03500   7.46900   29.66700  1.000 87.91150  ?  904  PEG B HO4 1 
HETATM 4236 C  C1  . PEG F 5 .   ? -7.74700  1.88400   20.75000  1.000 64.70527  ?  905  PEG B C1  1 
HETATM 4237 C  C2  . PEG F 5 .   ? -8.39400  1.04600   19.68000  1.000 66.84982  ?  905  PEG B C2  1 
HETATM 4238 O  O2  . PEG F 5 .   ? -8.07600  1.56500   18.38800  1.000 73.37893  ?  905  PEG B O2  1 
HETATM 4239 C  C3  . PEG F 5 .   ? -7.64400  0.56900   17.47500  1.000 72.02260  ?  905  PEG B C3  1 
HETATM 4240 C  C4  . PEG F 5 .   ? -7.68900  1.08300   16.07100  1.000 73.57414  ?  905  PEG B C4  1 
HETATM 4241 O  O4  . PEG F 5 .   ? -9.02200  1.04500   15.57800  1.000 76.50469  ?  905  PEG B O4  1 
HETATM 4242 H  H11 . PEG F 5 .   ? -7.96300  1.50900   21.61800  1.000 77.64632  ?  905  PEG B H11 1 
HETATM 4243 H  H12 . PEG F 5 .   ? -6.78600  1.87100   20.62300  1.000 77.64632  ?  905  PEG B H12 1 
HETATM 4244 H  H32 . PEG F 5 .   ? -6.73300  0.31200   17.69000  1.000 86.42712  ?  905  PEG B H32 1 
HETATM 4245 H  H41 . PEG F 5 .   ? -7.12400  0.53000   15.50900  1.000 88.28897  ?  905  PEG B H41 1 
HETATM 4246 H  H42 . PEG F 5 .   ? -7.36700  1.99700   16.05400  1.000 88.28897  ?  905  PEG B H42 1 
HETATM 4247 H  HO4 . PEG F 5 .   ? -9.61000  1.09200   16.19400  1.000 91.80563  ?  905  PEG B HO4 1 
HETATM 4248 C  C1  . GOL G 6 .   ? 21.06000  18.46800  3.26700   1.000 97.26183  ?  906  GOL B C1  1 
HETATM 4249 O  O1  . GOL G 6 .   ? 20.14300  17.60300  2.60000   1.000 97.34943  ?  906  GOL B O1  1 
HETATM 4250 C  C2  . GOL G 6 .   ? 20.97400  18.32500  4.77100   1.000 91.18351  ?  906  GOL B C2  1 
HETATM 4251 O  O2  . GOL G 6 .   ? 22.05200  19.03400  5.37900   1.000 95.68059  ?  906  GOL B O2  1 
HETATM 4252 C  C3  . GOL G 6 .   ? 19.66200  18.81800  5.34200   1.000 94.74321  ?  906  GOL B C3  1 
HETATM 4253 O  O3  . GOL G 6 .   ? 19.65700  18.76000  6.76600   1.000 93.88537  ?  906  GOL B O3  1 
HETATM 4254 H  H11 . GOL G 6 .   ? 20.86300  19.40300  3.01900   1.000 116.71420 ?  906  GOL B H11 1 
HETATM 4255 H  H12 . GOL G 6 .   ? 21.97900  18.25600  2.97400   1.000 116.71420 ?  906  GOL B H12 1 
HETATM 4256 H  HO1 . GOL G 6 .   ? 19.35600  17.82900  2.81000   1.000 116.81932 ?  906  GOL B HO1 1 
HETATM 4257 H  H2  . GOL G 6 .   ? 21.06400  17.36900  4.99400   1.000 109.42021 ?  906  GOL B H2  1 
HETATM 4258 H  HO2 . GOL G 6 .   ? 22.77700  18.71100  5.07900   1.000 114.81671 ?  906  GOL B HO2 1 
HETATM 4259 H  H31 . GOL G 6 .   ? 18.92500  18.26200  4.99100   1.000 113.69185 ?  906  GOL B H31 1 
HETATM 4260 H  H32 . GOL G 6 .   ? 19.51200  19.75000  5.05300   1.000 113.69185 ?  906  GOL B H32 1 
HETATM 4261 H  HO3 . GOL G 6 .   ? 20.30100  19.23000  7.04900   1.000 112.66244 ?  906  GOL B HO3 1 
HETATM 4262 CL CL  . CL  H 7 .   ? 30.63800  -41.47900 14.99600  1.000 93.92270  ?  907  CL  B CL  1 
HETATM 4263 CL CL  . CL  I 7 .   ? 13.40000  -2.67100  -4.23900  1.000 91.96093  ?  908  CL  B CL  1 
HETATM 4264 CL CL  . CL  J 7 .   ? 36.13600  -12.68000 3.89100   1.000 99.32279  ?  909  CL  B CL  1 
HETATM 4265 CL CL  . CL  K 7 .   ? 46.75600  -33.05700 1.33100   1.000 85.19705  ?  910  CL  B CL  1 
HETATM 4266 C  C1  . PEG L 5 .   ? 33.79800  7.01700   13.06100  1.000 75.89296  ?  911  PEG B C1  1 
HETATM 4267 C  C2  . PEG L 5 .   ? 33.09900  6.10200   14.00900  1.000 76.46440  ?  911  PEG B C2  1 
HETATM 4268 O  O2  . PEG L 5 .   ? 31.70000  6.34900   13.97000  1.000 78.96718  ?  911  PEG B O2  1 
HETATM 4269 C  C3  . PEG L 5 .   ? 31.27600  7.26600   14.97000  1.000 87.27535  ?  911  PEG B C3  1 
HETATM 4270 C  C4  . PEG L 5 .   ? 30.82500  6.51600   16.17800  1.000 74.15470  ?  911  PEG B C4  1 
HETATM 4271 H  H21 . PEG L 5 .   ? 33.43700  6.24700   14.91900  1.000 91.75728  ?  911  PEG B H21 1 
HETATM 4272 H  H31 . PEG L 5 .   ? 30.53900  7.81400   14.62500  1.000 104.73041 ?  911  PEG B H31 1 
HETATM 4273 H  H32 . PEG L 5 .   ? 32.01700  7.86300   15.20900  1.000 104.73041 ?  911  PEG B H32 1 
HETATM 4274 H  H41 . PEG L 5 .   ? 30.76200  5.56300   15.95900  1.000 88.98564  ?  911  PEG B H41 1 
HETATM 4275 C  C1  . PEG M 5 .   ? 41.85800  -10.88400 10.76600  1.000 81.41013  ?  912  PEG B C1  1 
HETATM 4276 C  C2  . PEG M 5 .   ? 41.49700  -10.51500 12.17000  1.000 89.62328  ?  912  PEG B C2  1 
HETATM 4277 O  O2  . PEG M 5 .   ? 40.70500  -11.54000 12.75900  1.000 99.22779  ?  912  PEG B O2  1 
HETATM 4278 C  C3  . PEG M 5 .   ? 39.37300  -11.57300 12.26000  1.000 83.03625  ?  912  PEG B C3  1 
HETATM 4279 C  C4  . PEG M 5 .   ? 38.57300  -12.57400 13.02600  1.000 85.01094  ?  912  PEG B C4  1 
HETATM 4280 H  H21 . PEG M 5 .   ? 40.99600  -9.67100  12.17100  1.000 107.54793 ?  912  PEG B H21 1 
HETATM 4281 H  H22 . PEG M 5 .   ? 42.31500  -10.38700 12.69700  1.000 107.54793 ?  912  PEG B H22 1 
HETATM 4282 H  H31 . PEG M 5 .   ? 39.38000  -11.81500 11.30900  1.000 99.64350  ?  912  PEG B H31 1 
HETATM 4283 H  H32 . PEG M 5 .   ? 38.96500  -10.68400 12.34800  1.000 99.64350  ?  912  PEG B H32 1 
HETATM 4284 H  H41 . PEG M 5 .   ? 38.56900  -12.32500 13.97400  1.000 102.01313 ?  912  PEG B H41 1 
HETATM 4285 K  K   . K   N 8 .   ? 13.63600  -3.85600  8.58700   1.000 83.22997  ?  913  K   B K   1 
HETATM 4286 K  K   . K   O 8 .   ? 19.28800  8.02000   3.73800   1.000 88.48536  ?  914  K   B K   1 
HETATM 4287 K  K   . K   P 8 .   ? 2.09400   -2.42400  11.44400  1.000 93.00243  ?  915  K   B K   1 
HETATM 4288 O  O   . HOH Q 9 .   ? 20.51600  -2.28200  -3.73400  1.000 51.70568  ?  1001 HOH B O   1 
HETATM 4289 O  O   . HOH Q 9 .   ? 22.11600  -23.66500 5.16500   1.000 64.05954  ?  1002 HOH B O   1 
HETATM 4290 O  O   . HOH Q 9 .   ? 6.89500   -18.76500 28.76000  1.000 64.07951  ?  1003 HOH B O   1 
HETATM 4291 O  O   . HOH Q 9 .   ? 1.71700   12.37200  23.62900  1.000 58.67197  ?  1004 HOH B O   1 
HETATM 4292 O  O   . HOH Q 9 .   ? 25.69000  -13.96700 22.55700  1.000 54.37042  ?  1005 HOH B O   1 
HETATM 4293 O  O   . HOH Q 9 .   ? 14.86400  -4.85400  24.28100  1.000 43.25803  ?  1006 HOH B O   1 
HETATM 4294 O  O   . HOH Q 9 .   ? 2.93000   5.03500   14.39500  1.000 54.82993  ?  1007 HOH B O   1 
HETATM 4295 O  O   . HOH Q 9 .   ? 20.95800  -5.92700  24.30100  1.000 47.54647  ?  1008 HOH B O   1 
HETATM 4296 O  O   . HOH Q 9 .   ? 8.52600   -4.01900  22.41900  1.000 47.15748  ?  1009 HOH B O   1 
HETATM 4297 O  O   . HOH Q 9 .   ? 32.76600  -12.61300 2.80500   1.000 56.03085  ?  1010 HOH B O   1 
HETATM 4298 O  O   . HOH Q 9 .   ? -0.39800  -9.82200  8.52200   1.000 53.57000  ?  1011 HOH B O   1 
HETATM 4299 O  O   . HOH Q 9 .   ? 1.28300   -6.86200  8.45400   1.000 60.73045  ?  1012 HOH B O   1 
HETATM 4300 O  O   . HOH Q 9 .   ? 39.04400  -3.57600  10.97300  1.000 60.02437  ?  1013 HOH B O   1 
HETATM 4301 O  O   . HOH Q 9 .   ? 3.86600   15.35300  19.42000  1.000 49.04085  ?  1014 HOH B O   1 
HETATM 4302 O  O   . HOH Q 9 .   ? 26.47000  -12.87900 16.24800  1.000 55.07339  ?  1015 HOH B O   1 
HETATM 4303 O  O   . HOH Q 9 .   ? 19.83000  -0.26500  15.27900  1.000 38.74817  ?  1016 HOH B O   1 
HETATM 4304 O  O   . HOH Q 9 .   ? 29.31500  -4.33600  19.04700  1.000 58.01622  ?  1017 HOH B O   1 
HETATM 4305 O  O   . HOH Q 9 .   ? 3.62600   -7.79400  17.75700  1.000 41.05657  ?  1018 HOH B O   1 
HETATM 4306 O  O   . HOH Q 9 .   ? -2.00200  -8.09800  15.32200  1.000 41.24209  ?  1019 HOH B O   1 
HETATM 4307 O  O   . HOH Q 9 .   ? 16.98900  -6.35500  9.00700   1.000 47.76383  ?  1020 HOH B O   1 
HETATM 4308 O  O   . HOH Q 9 .   ? 0.62400   -13.03100 8.11800   1.000 52.57587  ?  1021 HOH B O   1 
HETATM 4309 O  O   . HOH Q 9 .   ? 33.82200  -8.34200  5.00900   1.000 52.41845  ?  1022 HOH B O   1 
HETATM 4310 O  O   . HOH Q 9 .   ? 8.50100   -8.51700  29.74200  1.000 59.92922  ?  1023 HOH B O   1 
HETATM 4311 O  O   . HOH Q 9 .   ? 18.46000  0.81200   22.40800  1.000 47.18123  ?  1024 HOH B O   1 
HETATM 4312 O  O   . HOH Q 9 .   ? 33.19300  -0.61300  -0.74700  1.000 66.09755  ?  1025 HOH B O   1 
HETATM 4313 O  O   . HOH Q 9 .   ? 14.62500  5.75600   1.67200   1.000 52.34981  ?  1026 HOH B O   1 
HETATM 4314 O  O   . HOH Q 9 .   ? -0.39100  15.19900  17.00200  1.000 55.93456  ?  1027 HOH B O   1 
HETATM 4315 O  O   . HOH Q 9 .   ? 20.07300  -24.80400 -1.49300  1.000 67.35610  ?  1028 HOH B O   1 
HETATM 4316 O  O   . HOH Q 9 .   ? 23.11700  -3.72000  15.22400  1.000 45.18269  ?  1029 HOH B O   1 
HETATM 4317 O  O   . HOH Q 9 .   ? 21.95500  -24.08800 19.67600  1.000 53.35235  ?  1030 HOH B O   1 
HETATM 4318 O  O   . HOH Q 9 .   ? 1.23200   12.38400  29.87900  1.000 54.37866  ?  1031 HOH B O   1 
HETATM 4319 O  O   . HOH Q 9 .   ? 18.19600  -5.38700  24.46500  1.000 48.28482  ?  1032 HOH B O   1 
HETATM 4320 O  O   . HOH Q 9 .   ? 8.80000   -10.98400 27.28400  1.000 47.87326  ?  1033 HOH B O   1 
HETATM 4321 O  O   . HOH Q 9 .   ? 12.26200  11.18100  29.81400  1.000 61.29298  ?  1034 HOH B O   1 
HETATM 4322 O  O   . HOH Q 9 .   ? 23.02900  -21.77400 19.49000  1.000 54.63690  ?  1035 HOH B O   1 
HETATM 4323 O  O   . HOH Q 9 .   ? -12.60600 -11.93900 26.80800  1.000 64.72320  ?  1036 HOH B O   1 
HETATM 4324 O  O   . HOH Q 9 .   ? -13.71000 -10.54800 32.97300  1.000 55.36067  ?  1037 HOH B O   1 
HETATM 4325 O  O   . HOH Q 9 .   ? 31.77600  -12.67200 -3.60800  1.000 62.77107  ?  1038 HOH B O   1 
HETATM 4326 O  O   . HOH Q 9 .   ? 14.89900  -2.51300  12.62900  1.000 50.33277  ?  1039 HOH B O   1 
HETATM 4327 O  O   . HOH Q 9 .   ? -4.35600  0.92900   15.21900  1.000 64.35610  ?  1040 HOH B O   1 
HETATM 4328 O  O   . HOH Q 9 .   ? 12.15200  -20.93300 21.48300  1.000 56.28959  ?  1041 HOH B O   1 
HETATM 4329 O  O   . HOH Q 9 .   ? 18.78400  -6.34900  17.39900  1.000 44.88254  ?  1042 HOH B O   1 
HETATM 4330 O  O   . HOH Q 9 .   ? 19.93100  2.97300   -7.61800  1.000 65.76907  ?  1043 HOH B O   1 
HETATM 4331 O  O   . HOH Q 9 .   ? 7.19800   10.50800  3.11000   1.000 62.42151  ?  1044 HOH B O   1 
HETATM 4332 O  O   . HOH Q 9 .   ? 23.74000  7.52600   18.27000  1.000 51.65872  ?  1045 HOH B O   1 
HETATM 4333 O  O   . HOH Q 9 .   ? 21.19300  -2.32600  16.34500  1.000 44.38888  ?  1046 HOH B O   1 
HETATM 4334 O  O   . HOH Q 9 .   ? -0.99800  -15.60900 21.78900  1.000 60.68744  ?  1047 HOH B O   1 
HETATM 4335 O  O   . HOH Q 9 .   ? 24.49600  -6.67900  -6.63500  1.000 63.92095  ?  1048 HOH B O   1 
HETATM 4336 O  O   . HOH Q 9 .   ? 0.67900   -11.17500 26.18700  1.000 56.05829  ?  1049 HOH B O   1 
HETATM 4337 O  O   . HOH Q 9 .   ? 18.91400  14.37500  33.08600  1.000 59.59539  ?  1050 HOH B O   1 
HETATM 4338 O  O   . HOH Q 9 .   ? -2.49700  -10.31700 33.64400  1.000 59.44113  ?  1051 HOH B O   1 
HETATM 4339 O  O   . HOH Q 9 .   ? 8.94800   -5.01200  12.63000  1.000 47.46455  ?  1052 HOH B O   1 
HETATM 4340 O  O   . HOH Q 9 .   ? 26.70700  -0.14300  26.12500  1.000 57.95423  ?  1053 HOH B O   1 
HETATM 4341 O  O   . HOH Q 9 .   ? 34.71500  1.50900   0.94400   1.000 61.20947  ?  1054 HOH B O   1 
HETATM 4342 O  O   . HOH Q 9 .   ? 30.70500  4.27100   -4.43700  1.000 71.41837  ?  1055 HOH B O   1 
HETATM 4343 O  O   . HOH Q 9 .   ? 7.16300   1.25200   35.17400  1.000 65.64969  ?  1056 HOH B O   1 
HETATM 4344 O  O   . HOH Q 9 .   ? 11.34300  -3.50000  13.01500  1.000 52.86468  ?  1057 HOH B O   1 
HETATM 4345 O  O   . HOH Q 9 .   ? -1.78900  3.69800   14.58200  1.000 61.55970  ?  1058 HOH B O   1 
HETATM 4346 O  O   . HOH Q 9 .   ? 37.66100  -0.80300  -1.56800  1.000 72.27579  ?  1059 HOH B O   1 
HETATM 4347 O  O   . HOH Q 9 .   ? 21.74900  -41.44700 10.77500  1.000 89.70508  ?  1060 HOH B O   1 
HETATM 4348 O  O   . HOH Q 9 .   ? 27.36500  -17.69800 -8.40600  1.000 76.31190  ?  1061 HOH B O   1 
HETATM 4349 O  O   . HOH Q 9 .   ? -11.58700 0.85700   26.73100  1.000 70.46388  ?  1062 HOH B O   1 
HETATM 4350 O  O   . HOH Q 9 .   ? 20.07500  -31.36600 17.29000  1.000 74.37482  ?  1063 HOH B O   1 
HETATM 4351 O  O   . HOH Q 9 .   ? 17.54200  20.96500  8.59300   1.000 76.73881  ?  1064 HOH B O   1 
HETATM 4352 O  O   . HOH Q 9 .   ? 5.69000   19.81400  40.22800  1.000 68.36319  ?  1065 HOH B O   1 
HETATM 4353 O  O   . HOH Q 9 .   ? 23.20700  18.43400  10.36500  1.000 66.15522  ?  1066 HOH B O   1 
HETATM 4354 O  O   . HOH Q 9 .   ? 35.50100  -23.79200 7.09500   1.000 67.43178  ?  1067 HOH B O   1 
HETATM 4355 O  O   . HOH Q 9 .   ? 21.66100  -6.60900  17.38200  1.000 57.88501  ?  1068 HOH B O   1 
HETATM 4356 O  O   . HOH Q 9 .   ? 0.05400   -14.38700 -2.62000  1.000 76.35651  ?  1069 HOH B O   1 
HETATM 4357 O  O   . HOH Q 9 .   ? 14.47700  -22.18700 3.78400   1.000 71.95488  ?  1070 HOH B O   1 
HETATM 4358 O  O   . HOH Q 9 .   ? 15.28400  8.38800   31.57200  1.000 77.97064  ?  1071 HOH B O   1 
HETATM 4359 O  O   . HOH Q 9 .   ? 29.67100  9.15700   12.70000  1.000 71.20134  ?  1072 HOH B O   1 
HETATM 4360 O  O   . HOH Q 9 .   ? 35.50700  2.73400   -1.95500  1.000 70.05240  ?  1073 HOH B O   1 
HETATM 4361 O  O   . HOH Q 9 .   ? 16.43700  -5.73900  27.35700  1.000 75.96812  ?  1074 HOH B O   1 
HETATM 4362 O  O   . HOH Q 9 .   ? 29.35400  -19.50400 19.51100  1.000 77.54951  ?  1075 HOH B O   1 
HETATM 4363 O  O   . HOH Q 9 .   ? 17.65000  -18.40800 -4.75800  1.000 76.55902  ?  1076 HOH B O   1 
HETATM 4364 O  O   . HOH Q 9 .   ? 13.22700  -1.76200  -0.25800  1.000 74.04512  ?  1077 HOH B O   1 
HETATM 4365 O  O   . HOH Q 9 .   ? 1.58500   3.32600   30.56700  1.000 73.98950  ?  1078 HOH B O   1 
HETATM 4366 O  O   . HOH Q 9 .   ? 29.45100  -30.65900 11.68900  1.000 75.74367  ?  1079 HOH B O   1 
HETATM 4367 O  O   . HOH Q 9 .   ? -1.91300  14.34100  23.70800  1.000 78.37366  ?  1080 HOH B O   1 
HETATM 4368 O  O   . HOH Q 9 .   ? 28.23700  9.05800   7.74500   1.000 62.93197  ?  1081 HOH B O   1 
HETATM 4369 O  O   . HOH Q 9 .   ? 38.73400  -14.79300 9.59200   1.000 77.54239  ?  1082 HOH B O   1 
HETATM 4370 O  O   . HOH Q 9 .   ? 4.22000   -3.79600  29.54700  1.000 70.14246  ?  1083 HOH B O   1 
HETATM 4371 O  O   . HOH Q 9 .   ? 3.02000   -27.06800 3.94300   1.000 80.37625  ?  1084 HOH B O   1 
HETATM 4372 O  O   . HOH Q 9 .   ? 14.78600  12.71800  0.66800   1.000 77.74447  ?  1085 HOH B O   1 
HETATM 4373 O  O   . HOH Q 9 .   ? 15.51600  -33.69300 11.63800  1.000 77.07240  ?  1086 HOH B O   1 
HETATM 4374 O  O   . HOH Q 9 .   ? -4.98600  3.04600   26.72600  1.000 73.67351  ?  1087 HOH B O   1 
HETATM 4375 O  O   . HOH Q 9 .   ? -2.61600  13.07900  21.96000  1.000 81.73997  ?  1088 HOH B O   1 
HETATM 4376 O  O   . HOH Q 9 .   ? 42.79700  -3.27000  13.13400  1.000 80.98798  ?  1089 HOH B O   1 
HETATM 4377 O  O   . HOH Q 9 .   ? 27.01100  17.12000  6.20200   1.000 82.70710  ?  1090 HOH B O   1 
HETATM 4378 O  O   . HOH Q 9 .   ? 9.29600   -13.92100 -3.70800  1.000 86.40618  ?  1091 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 14  ? 2.09291 0.89771 1.76729 0.10462  0.52764  -0.23910 291 ALA B N   
2    C CA  . ALA A 14  ? 2.02223 0.82618 1.68292 0.13640  0.55259  -0.19645 291 ALA B CA  
3    C C   . ALA A 14  ? 1.97336 0.82236 1.62119 0.16300  0.53208  -0.17391 291 ALA B C   
4    O O   . ALA A 14  ? 1.90498 0.79139 1.57318 0.16137  0.51299  -0.16555 291 ALA B O   
5    N N   . THR A 15  ? 2.06723 0.91274 1.68305 0.18711  0.53728  -0.16435 292 THR B N   
6    C CA  . THR A 15  ? 1.93992 0.82971 1.54610 0.21164  0.51827  -0.14527 292 THR B CA  
7    C C   . THR A 15  ? 1.90680 0.83167 1.52585 0.19435  0.48299  -0.16704 292 THR B C   
8    O O   . THR A 15  ? 1.91200 0.87929 1.54105 0.20576  0.46574  -0.14955 292 THR B O   
9    C CB  . THR A 15  ? 1.83028 0.70930 1.40424 0.23356  0.52854  -0.14069 292 THR B CB  
10   N N   . ARG A 16  ? 1.92880 0.83603 1.54711 0.16655  0.47091  -0.20576 293 ARG B N   
11   C CA  . ARG A 16  ? 1.80643 0.74437 1.43488 0.14949  0.43619  -0.22794 293 ARG B CA  
12   C C   . ARG A 16  ? 1.84618 0.80828 1.51645 0.13516  0.42613  -0.22247 293 ARG B C   
13   O O   . ARG A 16  ? 1.76850 0.76959 1.44889 0.13676  0.40277  -0.21859 293 ARG B O   
14   C CB  . ARG A 16  ? 1.86097 0.77264 1.47795 0.12194  0.42309  -0.27185 293 ARG B CB  
15   N N   . ASP A 17  ? 1.93514 0.87364 1.62980 0.12114  0.44574  -0.22138 294 ASP B N   
16   C CA  . ASP A 17  ? 1.82416 0.78386 1.55900 0.10754  0.44052  -0.21463 294 ASP B CA  
17   C C   . ASP A 17  ? 1.81487 0.80517 1.54624 0.13533  0.44282  -0.17484 294 ASP B C   
18   O O   . ASP A 17  ? 1.74312 0.76753 1.49627 0.13056  0.42461  -0.17045 294 ASP B O   
19   C CB  . ASP A 17  ? 1.88109 0.80677 1.64008 0.08805  0.46602  -0.22024 294 ASP B CB  
20   C CG  . ASP A 17  ? 1.94437 0.83799 1.70594 0.06142  0.46434  -0.25964 294 ASP B CG  
21   N N   . GLN A 18  ? 1.87330 0.85259 1.57763 0.16451  0.46362  -0.14611 295 GLN B N   
22   C CA  . GLN A 18  ? 1.83323 0.84161 1.53238 0.19156  0.46313  -0.10899 295 GLN B CA  
23   C C   . GLN A 18  ? 1.76059 0.81486 1.45574 0.20326  0.43397  -0.10636 295 GLN B C   
24   O O   . GLN A 18  ? 1.67834 0.76529 1.38121 0.21475  0.42381  -0.08476 295 GLN B O   
25   C CB  . GLN A 18  ? 1.92341 0.91101 1.59506 0.22060  0.48855  -0.08128 295 GLN B CB  
26   C CG  . GLN A 18  ? 1.98310 0.99686 1.64778 0.24875  0.48802  -0.04304 295 GLN B CG  
27   C CD  . GLN A 18  ? 2.13723 1.12700 1.77709 0.27609  0.51350  -0.01681 295 GLN B CD  
28   O OE1 . GLN A 18  ? 2.04753 1.00013 1.67561 0.27448  0.53393  -0.02614 295 GLN B OE1 
29   N NE2 . GLN A 18  ? 2.15680 1.16703 1.78770 0.30165  0.51183  0.01565  295 GLN B NE2 
30   N N   . LEU A 19  ? 1.78877 0.84446 1.46889 0.20076  0.42135  -0.12801 296 LEU B N   
31   C CA  . LEU A 19  ? 1.62090 0.71854 1.29538 0.21021  0.39508  -0.12789 296 LEU B CA  
32   C C   . LEU A 19  ? 1.59024 0.70918 1.29206 0.18623  0.37191  -0.14479 296 LEU B C   
33   O O   . LEU A 19  ? 1.58506 0.74214 1.29481 0.19688  0.35739  -0.12830 296 LEU B O   
34   C CB  . LEU A 19  ? 1.64583 0.73180 1.29100 0.21197  0.39137  -0.14836 296 LEU B CB  
35   C CG  . LEU A 19  ? 1.76503 0.84491 1.38548 0.24145  0.41012  -0.12722 296 LEU B CG  
36   C CD1 . LEU A 19  ? 1.70581 0.77109 1.29565 0.24010  0.40803  -0.14965 296 LEU B CD1 
37   C CD2 . LEU A 19  ? 1.64343 0.76913 1.26928 0.27017  0.40340  -0.09328 296 LEU B CD2 
38   N N   . ASN A 20  ? 1.59991 0.69657 1.31812 0.15483  0.36794  -0.17666 297 ASN B N   
39   C CA  . ASN A 20  ? 1.62012 0.73853 1.36882 0.13075  0.34436  -0.19491 297 ASN B CA  
40   C C   . ASN A 20  ? 1.52987 0.67060 1.30793 0.13340  0.34814  -0.16978 297 ASN B C   
41   O O   . ASN A 20  ? 1.46548 0.63818 1.26115 0.12853  0.32861  -0.16987 297 ASN B O   
42   C CB  . ASN A 20  ? 1.54978 0.64215 1.31927 0.09579  0.34028  -0.23203 297 ASN B CB  
43   C CG  . ASN A 20  ? 1.73826 0.80743 1.47245 0.09149  0.33267  -0.25985 297 ASN B CG  
44   O OD1 . ASN A 20  ? 1.77162 0.80366 1.49742 0.08425  0.34922  -0.27191 297 ASN B OD1 
45   N ND2 . ASN A 20  ? 1.65928 0.74808 1.36824 0.09651  0.30879  -0.26963 297 ASN B ND2 
46   N N   . ILE A 21  ? 1.53314 0.65530 1.31260 0.14178  0.37403  -0.14763 298 ILE B N   
47   C CA  . ILE A 21  ? 1.53342 0.67272 1.32898 0.14770  0.37956  -0.12109 298 ILE B CA  
48   C C   . ILE A 21  ? 1.51835 0.69412 1.29505 0.17653  0.36652  -0.09480 298 ILE B C   
49   O O   . ILE A 21  ? 1.44509 0.65044 1.23780 0.17490  0.35294  -0.08674 298 ILE B O   
50   C CB  . ILE A 21  ? 1.56324 0.66957 1.35317 0.15290  0.41149  -0.10272 298 ILE B CB  
51   C CG1 . ILE A 21  ? 1.53084 0.60062 1.33941 0.12527  0.42635  -0.12953 298 ILE B CG1 
52   C CG2 . ILE A 21  ? 1.43113 0.55134 1.23259 0.15616  0.41707  -0.07834 298 ILE B CG2 
53   N N   . ILE A 22  ? 1.50835 0.68394 1.25379 0.20315  0.37112  -0.08067 299 ILE B N   
54   C CA  . ILE A 22  ? 1.44633 0.66166 1.17936 0.23005  0.35708  -0.05732 299 ILE B CA  
55   C C   . ILE A 22  ? 1.45350 0.70109 1.19603 0.22154  0.33060  -0.07328 299 ILE B C   
56   O O   . ILE A 22  ? 1.37341 0.65859 1.12874 0.22413  0.31496  -0.05997 299 ILE B O   
57   C CB  . ILE A 22  ? 1.51443 0.72745 1.22030 0.25724  0.36574  -0.04396 299 ILE B CB  
58   C CG1 . ILE A 22  ? 1.53240 0.70986 1.22678 0.26683  0.39324  -0.02767 299 ILE B CG1 
59   C CG2 . ILE A 22  ? 1.37733 0.63794 1.07899 0.28343  0.34962  -0.02076 299 ILE B CG2 
60   N N   . VAL A 23  ? 1.46366 0.70000 1.19808 0.20909  0.32306  -0.10191 300 VAL B N   
61   C CA  . VAL A 23  ? 1.34448 0.63697 1.08761 0.19606  0.28689  -0.11153 300 VAL B CA  
62   C C   . VAL A 23  ? 1.42169 0.74689 1.20281 0.17246  0.26750  -0.11402 300 VAL B C   
63   O O   . VAL A 23  ? 1.37091 0.75041 1.16279 0.17179  0.24196  -0.10500 300 VAL B O   
64   C CB  . VAL A 23  ? 1.43168 0.70628 1.15704 0.18137  0.27859  -0.14311 300 VAL B CB  
65   C CG1 . VAL A 23  ? 1.49192 0.81805 1.22893 0.16325  0.24033  -0.15514 300 VAL B CG1 
66   C CG2 . VAL A 23  ? 1.46172 0.71759 1.14793 0.20774  0.29411  -0.13728 300 VAL B CG2 
67   N N   . SER A 24  ? 1.41060 0.70214 1.21490 0.15285  0.28176  -0.12604 301 SER B N   
68   C CA  . SER A 24  ? 1.45498 0.77562 1.30085 0.12897  0.26584  -0.13101 301 SER B CA  
69   C C   . SER A 24  ? 1.38058 0.71683 1.23507 0.14094  0.27367  -0.10156 301 SER B C   
70   O O   . SER A 24  ? 1.43610 0.79386 1.32467 0.12287  0.26470  -0.10347 301 SER B O   
71   C CB  . SER A 24  ? 1.45765 0.73896 1.33288 0.10055  0.27829  -0.15788 301 SER B CB  
72   O OG  . SER A 24  ? 1.47868 0.70159 1.34539 0.10931  0.31810  -0.14926 301 SER B OG  
73   N N   . TYR A 25  ? 1.34095 0.66694 1.16532 0.17123  0.28924  -0.07492 302 TYR B N   
74   C CA  . TYR A 25  ? 1.31943 0.65820 1.14281 0.18491  0.29391  -0.04693 302 TYR B CA  
75   C C   . TYR A 25  ? 1.31230 0.71421 1.15528 0.17619  0.26266  -0.04256 302 TYR B C   
76   O O   . TYR A 25  ? 1.26663 0.70758 1.11187 0.17214  0.23729  -0.05183 302 TYR B O   
77   C CB  . TYR A 25  ? 1.31097 0.64204 1.09850 0.22113  0.30479  -0.02045 302 TYR B CB  
78   C CG  . TYR A 25  ? 1.37849 0.66126 1.14808 0.23077  0.33445  -0.01074 302 TYR B CG  
79   C CD1 . TYR A 25  ? 1.40823 0.65786 1.19302 0.20855  0.35329  -0.01976 302 TYR B CD1 
80   C CD2 . TYR A 25  ? 1.39034 0.67297 1.13259 0.25905  0.34037  0.00929  302 TYR B CD2 
81   C CE1 . TYR A 25  ? 1.42330 0.63723 1.19111 0.21515  0.37878  -0.00883 302 TYR B CE1 
82   C CE2 . TYR A 25  ? 1.40898 0.65606 1.13521 0.26601  0.36430  0.02014  302 TYR B CE2 
83   C CZ  . TYR A 25  ? 1.44042 0.65177 1.17696 0.24442  0.38407  0.01131  302 TYR B CZ  
84   O OH  . TYR A 25  ? 1.50986 0.68436 1.22776 0.25279  0.41007  0.02319  302 TYR B OH  
85   N N   . PRO A 26  ? 1.24949 0.65903 1.10340 0.17397  0.26575  -0.02801 303 PRO B N   
86   C CA  . PRO A 26  ? 1.21316 0.67955 1.07946 0.17062  0.23917  -0.02000 303 PRO B CA  
87   C C   . PRO A 26  ? 1.19708 0.69549 1.03724 0.19656  0.22600  -0.00144 303 PRO B C   
88   O O   . PRO A 26  ? 1.23675 0.71169 1.04961 0.22116  0.24089  0.01354  303 PRO B O   
89   C CB  . PRO A 26  ? 1.12672 0.57864 1.00055 0.16659  0.25392  -0.00697 303 PRO B CB  
90   C CG  . PRO A 26  ? 1.17623 0.56850 1.02309 0.18271  0.28675  0.00383  303 PRO B CG  
91   C CD  . PRO A 26  ? 1.27569 0.63761 1.12569 0.17624  0.29645  -0.01697 303 PRO B CD  
92   N N   . PRO A 27  ? 1.14925 0.70156 1.00017 0.19226  0.19907  -0.00105 304 PRO B N   
93   C CA  . PRO A 27  ? 1.11593 0.70112 0.94974 0.21357  0.18670  0.01130  304 PRO B CA  
94   C C   . PRO A 27  ? 1.10438 0.69100 0.91960 0.23824  0.19252  0.03701  304 PRO B C   
95   O O   . PRO A 27  ? 1.17534 0.78074 0.97912 0.25949  0.18789  0.04775  304 PRO B O   
96   C CB  . PRO A 27  ? 1.00235 0.64028 0.85555 0.19945  0.15973  0.00595  304 PRO B CB  
97   C CG  . PRO A 27  ? 1.00389 0.64117 0.88084 0.17869  0.15884  0.00226  304 PRO B CG  
98   C CD  . PRO A 27  ? 1.06342 0.64791 0.94422 0.17005  0.18218  -0.00776 304 PRO B CD  
99   N N   . THR A 28  ? 1.13208 0.69793 0.94347 0.23682  0.20293  0.04699  305 THR B N   
100  C CA  . THR A 28  ? 1.15793 0.72549 0.94692 0.25923  0.20383  0.07093  305 THR B CA  
101  C C   . THR A 28  ? 1.20355 0.71603 0.96430 0.28028  0.22985  0.08290  305 THR B C   
102  O O   . THR A 28  ? 1.23862 0.75024 0.97564 0.30426  0.22896  0.10408  305 THR B O   
103  C CB  . THR A 28  ? 1.08949 0.66637 0.88319 0.24616  0.19870  0.07602  305 THR B CB  
104  N N   . LYS A 29  ? 1.20433 0.66990 0.96643 0.27236  0.25237  0.06988  306 LYS B N   
105  C CA  . LYS A 29  ? 1.25091 0.65905 0.98512 0.29308  0.28049  0.08182  306 LYS B CA  
106  C C   . LYS A 29  ? 1.31853 0.73544 1.03745 0.32292  0.27804  0.09292  306 LYS B C   
107  O O   . LYS A 29  ? 1.28705 0.73310 1.01942 0.32077  0.26633  0.08152  306 LYS B O   
108  C CB  . LYS A 29  ? 1.28330 0.64182 1.02782 0.27285  0.30550  0.06248  306 LYS B CB  
109  C CG  . LYS A 29  ? 1.29770 0.61571 1.01864 0.28103  0.33047  0.07435  306 LYS B CG  
110  C CD  . LYS A 29  ? 1.34473 0.62306 1.08238 0.25452  0.35336  0.05515  306 LYS B CD  
111  C CE  . LYS A 29  ? 1.42778 0.66513 1.14043 0.26189  0.38130  0.07066  306 LYS B CE  
112  N NZ  . LYS A 29  ? 1.64405 0.87344 1.32971 0.28883  0.38610  0.08403  306 LYS B NZ  
113  N N   . GLN A 30  ? 1.34921 0.75577 1.04302 0.34314  0.28446  0.11461  307 GLN B N   
114  C CA  . GLN A 30  ? 1.34109 0.76312 1.02602 0.36914  0.28122  0.12703  307 GLN B CA  
115  C C   . GLN A 30  ? 1.36342 0.74368 1.04269 0.36657  0.30633  0.11850  307 GLN B C   
116  O O   . GLN A 30  ? 1.44155 0.77743 1.10794 0.35798  0.32842  0.11880  307 GLN B O   
117  C CB  . GLN A 30  ? 1.34088 0.77168 1.00172 0.39265  0.27441  0.15302  307 GLN B CB  
118  C CG  . GLN A 30  ? 1.49704 0.96446 1.15811 0.39367  0.24943  0.16146  307 GLN B CG  
119  C CD  . GLN A 30  ? 1.65711 1.09156 1.30155 0.37756  0.25976  0.16185  307 GLN B CD  
120  O OE1 . GLN A 30  ? 1.65321 1.03977 1.27976 0.37241  0.28527  0.16274  307 GLN B OE1 
121  N NE2 . GLN A 30  ? 1.57305 1.03320 1.22430 0.36907  0.24184  0.16133  307 GLN B NE2 
122  N N   . LEU A 31  ? 1.34656 0.73996 1.03498 0.37319  0.30460  0.11058  308 LEU B N   
123  C CA  . LEU A 31  ? 1.37027 0.72528 1.04973 0.37462  0.32786  0.10481  308 LEU B CA  
124  C C   . LEU A 31  ? 1.35822 0.70894 1.01893 0.40303  0.33552  0.12987  308 LEU B C   
125  O O   . LEU A 31  ? 1.34471 0.73664 1.00776 0.42455  0.31732  0.14691  308 LEU B O   
126  C CB  . LEU A 31  ? 1.38056 0.74758 1.07123 0.37234  0.32499  0.08722  308 LEU B CB  
127  C CG  . LEU A 31  ? 1.39986 0.78852 1.10728 0.35321  0.30873  0.06543  308 LEU B CG  
128  C CD1 . LEU A 31  ? 1.36873 0.75308 1.07453 0.35167  0.31290  0.04720  308 LEU B CD1 
129  C CD2 . LEU A 31  ? 1.34873 0.71076 1.06360 0.32450  0.31259  0.04869  308 LEU B CD2 
130  N N   . THR A 32  ? 1.37716 0.67907 1.02114 0.40271  0.36199  0.13157  309 THR B N   
131  C CA  . THR A 32  ? 1.45654 0.74970 1.08154 0.43083  0.37181  0.15421  309 THR B CA  
132  C C   . THR A 32  ? 1.44905 0.76463 1.08523 0.44830  0.36932  0.15533  309 THR B C   
133  O O   . THR A 32  ? 1.38569 0.71326 1.03806 0.43699  0.36531  0.13699  309 THR B O   
134  C CB  . THR A 32  ? 1.41661 0.64920 1.02112 0.42528  0.40417  0.15482  309 THR B CB  
135  N N   . TYR A 33  ? 1.42335 0.74401 1.05011 0.47685  0.37243  0.17708  310 TYR B N   
136  C CA  . TYR A 33  ? 1.40082 0.73545 1.03940 0.49400  0.37676  0.17953  310 TYR B CA  
137  C C   . TYR A 33  ? 1.42970 0.71784 1.06298 0.47884  0.40334  0.16041  310 TYR B C   
138  O O   . TYR A 33  ? 1.44551 0.74583 1.09198 0.47389  0.40221  0.14604  310 TYR B O   
139  C CB  . TYR A 33  ? 1.43754 0.77605 1.06682 0.52612  0.37961  0.20542  310 TYR B CB  
140  C CG  . TYR A 33  ? 1.40793 0.80040 1.04685 0.54260  0.34839  0.22189  310 TYR B CG  
141  C CD1 . TYR A 33  ? 1.34838 0.79661 1.01553 0.53601  0.32135  0.21511  310 TYR B CD1 
142  C CD2 . TYR A 33  ? 1.44456 0.83160 1.06309 0.56406  0.34530  0.24324  310 TYR B CD2 
143  C CE1 . TYR A 33  ? 1.36670 0.86546 1.04485 0.54861  0.29141  0.22852  310 TYR B CE1 
144  C CE2 . TYR A 33  ? 1.42054 0.85629 1.04671 0.57755  0.31382  0.25600  310 TYR B CE2 
145  C CZ  . TYR A 33  ? 1.37705 0.86925 1.03454 0.56890  0.28661  0.24828  310 TYR B CZ  
146  O OH  . TYR A 33  ? 1.47404 1.01451 1.14024 0.58029  0.25439  0.25978  310 TYR B OH  
147  N N   . GLU A 34  ? 1.47943 0.71310 1.09211 0.46994  0.42762  0.15893  311 GLU B N   
148  C CA  . GLU A 34  ? 1.51943 0.70549 1.12723 0.45203  0.45281  0.13821  311 GLU B CA  
149  C C   . GLU A 34  ? 1.50143 0.69775 1.12465 0.42373  0.44030  0.10907  311 GLU B C   
150  O O   . GLU A 34  ? 1.48774 0.67190 1.11176 0.41749  0.44816  0.09185  311 GLU B O   
151  C CB  . GLU A 34  ? 1.66930 0.80006 1.25811 0.44154  0.47870  0.13928  311 GLU B CB  
152  C CG  . GLU A 34  ? 1.81849 0.93466 1.38591 0.47077  0.49232  0.16815  311 GLU B CG  
153  C CD  . GLU A 34  ? 2.08052 1.14018 1.62645 0.46161  0.52157  0.17070  311 GLU B CD  
154  O OE1 . GLU A 34  ? 2.14247 1.17641 1.69572 0.43026  0.53108  0.14896  311 GLU B OE1 
155  O OE2 . GLU A 34  ? 2.07651 1.11902 1.59989 0.48607  0.53487  0.19404  311 GLU B OE2 
156  N N   . GLU A 35  ? 1.48595 0.70220 1.11862 0.40801  0.42187  0.10358  312 GLU B N   
157  C CA  . GLU A 35  ? 1.47252 0.69637 1.11929 0.38148  0.40993  0.07546  312 GLU B CA  
158  C C   . GLU A 35  ? 1.37181 0.63804 1.02828 0.39131  0.39265  0.07156  312 GLU B C   
159  O O   . GLU A 35  ? 1.39364 0.65188 1.05032 0.37676  0.39270  0.04764  312 GLU B O   
160  C CB  . GLU A 35  ? 1.41257 0.64801 1.06941 0.36385  0.39600  0.07241  312 GLU B CB  
161  C CG  . GLU A 35  ? 1.51730 0.70973 1.16625 0.35164  0.41658  0.07510  312 GLU B CG  
162  C CD  . GLU A 35  ? 1.52051 0.72139 1.18293 0.33078  0.40632  0.06901  312 GLU B CD  
163  O OE1 . GLU A 35  ? 1.45846 0.70013 1.12682 0.33749  0.38353  0.07754  312 GLU B OE1 
164  O OE2 . GLU A 35  ? 1.59419 0.76148 1.26400 0.30681  0.42195  0.05509  312 GLU B OE2 
165  N N   . GLN A 36  ? 1.36938 0.68071 1.03336 0.41565  0.37800  0.09413  313 GLN B N   
166  C CA  . GLN A 36  ? 1.29687 0.65301 0.97504 0.42487  0.36324  0.09219  313 GLN B CA  
167  C C   . GLN A 36  ? 1.42025 0.75637 1.09127 0.43220  0.38215  0.08540  313 GLN B C   
168  O O   . GLN A 36  ? 1.42786 0.76946 1.09886 0.42371  0.38008  0.06728  313 GLN B O   
169  C CB  . GLN A 36  ? 1.29149 0.70085 0.98471 0.44888  0.34467  0.11793  313 GLN B CB  
170  C CG  . GLN A 36  ? 1.27363 0.70932 0.97298 0.44175  0.32264  0.12327  313 GLN B CG  
171  C CD  . GLN A 36  ? 1.31346 0.79607 1.02381 0.46520  0.30418  0.14811  313 GLN B CD  
172  O OE1 . GLN A 36  ? 1.35360 0.87677 1.08380 0.48072  0.29601  0.15504  313 GLN B OE1 
173  N NE2 . GLN A 36  ? 1.36134 0.83809 1.05909 0.46709  0.29772  0.16076  313 GLN B NE2 
174  N N   . ASP A 37  ? 1.38241 0.69257 1.04407 0.44870  0.40201  0.10004  314 ASP B N   
175  C CA  . ASP A 37  ? 1.45591 0.74550 1.11081 0.45735  0.42223  0.09559  314 ASP B CA  
176  C C   . ASP A 37  ? 1.49727 0.73520 1.13329 0.43172  0.43780  0.06607  314 ASP B C   
177  O O   . ASP A 37  ? 1.51602 0.74155 1.14357 0.43142  0.44832  0.05328  314 ASP B O   
178  C CB  . ASP A 37  ? 1.47150 0.74679 1.12212 0.48289  0.43937  0.12003  314 ASP B CB  
179  C CG  . ASP A 37  ? 1.44161 0.77101 1.11196 0.50851  0.41989  0.14711  314 ASP B CG  
180  O OD1 . ASP A 37  ? 1.41528 0.79525 1.10901 0.51604  0.40353  0.14917  314 ASP B OD1 
181  O OD2 . ASP A 37  ? 1.46260 0.78353 1.12454 0.52055  0.42086  0.16553  314 ASP B OD2 
182  N N   . LEU A 38  ? 1.46519 0.67337 1.09530 0.40917  0.43903  0.05383  315 LEU B N   
183  C CA  . LEU A 38  ? 1.53285 0.69897 1.15108 0.38138  0.44790  0.02191  315 LEU B CA  
184  C C   . LEU A 38  ? 1.53631 0.72629 1.15667 0.36658  0.42729  -0.00096 315 LEU B C   
185  O O   . LEU A 38  ? 1.57381 0.73979 1.17805 0.35511  0.43310  -0.02477 315 LEU B O   
186  C CB  . LEU A 38  ? 1.52099 0.65495 1.14079 0.35995  0.45397  0.01468  315 LEU B CB  
187  C CG  . LEU A 38  ? 1.54402 0.64066 1.16002 0.32738  0.45807  -0.02110 315 LEU B CG  
188  C CD1 . LEU A 38  ? 1.66021 0.71370 1.25659 0.32833  0.48185  -0.03208 315 LEU B CD1 
189  C CD2 . LEU A 38  ? 1.70803 0.78286 1.33613 0.30552  0.46267  -0.02652 315 LEU B CD2 
190  N N   . VAL A 39  ? 1.49707 0.73233 1.13362 0.36706  0.40332  0.00574  316 VAL B N   
191  C CA  . VAL A 39  ? 1.46018 0.72086 1.09688 0.35657  0.38410  -0.01268 316 VAL B CA  
192  C C   . VAL A 39  ? 1.45212 0.73051 1.08119 0.37415  0.38827  -0.00916 316 VAL B C   
193  O O   . VAL A 39  ? 1.43028 0.69768 1.04110 0.36366  0.38714  -0.03166 316 VAL B O   
194  C CB  . VAL A 39  ? 1.39266 0.69875 1.04954 0.35578  0.35988  -0.00285 316 VAL B CB  
195  C CG1 . VAL A 39  ? 1.31074 0.64810 0.96647 0.35169  0.34203  -0.01614 316 VAL B CG1 
196  C CG2 . VAL A 39  ? 1.41804 0.70237 1.08203 0.33306  0.35722  -0.01226 316 VAL B CG2 
197  N N   . TRP A 40  ? 1.37811 0.68426 1.02072 0.40084  0.39289  0.01873  317 TRP B N   
198  C CA  . TRP A 40  ? 1.42577 0.75054 1.06825 0.41741  0.39972  0.02357  317 TRP B CA  
199  C C   . TRP A 40  ? 1.55016 0.82286 1.16477 0.41234  0.42381  0.00635  317 TRP B C   
200  O O   . TRP A 40  ? 1.49439 0.76335 1.09210 0.40759  0.42567  -0.00969 317 TRP B O   
201  C CB  . TRP A 40  ? 1.38951 0.75136 1.05709 0.44612  0.40086  0.05557  317 TRP B CB  
202  C CG  . TRP A 40  ? 1.43482 0.81321 1.10810 0.46195  0.41179  0.06021  317 TRP B CG  
203  C CD1 . TRP A 40  ? 1.41929 0.76890 1.08445 0.47491  0.43722  0.06475  317 TRP B CD1 
204  C CD2 . TRP A 40  ? 1.40202 0.82621 1.09004 0.46514  0.40077  0.05980  317 TRP B CD2 
205  N NE1 . TRP A 40  ? 1.41617 0.79154 1.09183 0.48622  0.44278  0.06769  317 TRP B NE1 
206  C CE2 . TRP A 40  ? 1.39314 0.81440 1.08308 0.48013  0.42122  0.06479  317 TRP B CE2 
207  C CE3 . TRP A 40  ? 1.32309 0.78983 1.02372 0.45691  0.37739  0.05650  317 TRP B CE3 
208  C CZ2 . TRP A 40  ? 1.36733 0.82614 1.07211 0.48604  0.42006  0.06636  317 TRP B CZ2 
209  C CZ3 . TRP A 40  ? 1.30713 0.81160 1.02147 0.46316  0.37567  0.05841  317 TRP B CZ3 
210  C CH2 . TRP A 40  ? 1.35038 0.85047 1.06711 0.47709  0.39737  0.06320  317 TRP B CH2 
211  N N   . LYS A 41  ? 1.50393 0.73353 1.11012 0.41291  0.44334  0.00920  318 LYS B N   
212  C CA  . LYS A 41  ? 1.57564 0.75459 1.15556 0.40871  0.46758  -0.00639 318 LYS B CA  
213  C C   . LYS A 41  ? 1.59143 0.74656 1.14530 0.38252  0.46042  -0.04185 318 LYS B C   
214  O O   . LYS A 41  ? 1.70677 0.84132 1.23654 0.38267  0.47205  -0.05482 318 LYS B O   
215  C CB  . LYS A 41  ? 1.61153 0.74393 1.18545 0.40729  0.48834  -0.00207 318 LYS B CB  
216  N N   . PHE A 42  ? 1.57436 0.73245 1.13148 0.36030  0.44047  -0.05800 319 PHE B N   
217  C CA  . PHE A 42  ? 1.63283 0.76828 1.16509 0.33472  0.42986  -0.09334 319 PHE B CA  
218  C C   . PHE A 42  ? 1.57060 0.74709 1.10058 0.33374  0.40631  -0.09821 319 PHE B C   
219  O O   . PHE A 42  ? 1.66024 0.82649 1.17355 0.31170  0.38944  -0.12546 319 PHE B O   
220  C CB  . PHE A 42  ? 1.66987 0.77715 1.20820 0.30782  0.42397  -0.11265 319 PHE B CB  
221  C CG  . PHE A 42  ? 1.74582 0.80462 1.28031 0.30433  0.44956  -0.11384 319 PHE B CG  
222  C CD1 . PHE A 42  ? 1.80022 0.81208 1.30644 0.29173  0.46249  -0.13944 319 PHE B CD1 
223  C CD2 . PHE A 42  ? 1.75969 0.81822 1.31523 0.31423  0.46127  -0.08897 319 PHE B CD2 
224  C CE1 . PHE A 42  ? 1.79104 0.75724 1.29411 0.28854  0.48796  -0.14032 319 PHE B CE1 
225  C CE2 . PHE A 42  ? 1.84655 0.85863 1.39617 0.31181  0.48712  -0.08876 319 PHE B CE2 
226  C CZ  . PHE A 42  ? 1.83247 0.79876 1.35775 0.29877  0.50115  -0.11446 319 PHE B CZ  
227  N N   . ARG A 43  ? 1.54488 0.76707 1.09068 0.35679  0.40472  -0.07345 320 ARG B N   
228  C CA  . ARG A 43  ? 1.53829 0.80112 1.08461 0.35550  0.38342  -0.07626 320 ARG B CA  
229  C C   . ARG A 43  ? 1.54363 0.78017 1.04697 0.34038  0.37944  -0.10605 320 ARG B C   
230  O O   . ARG A 43  ? 1.49067 0.73661 0.98289 0.32550  0.35716  -0.12252 320 ARG B O   
231  C CB  . ARG A 43  ? 1.43273 0.74687 1.00444 0.38156  0.38580  -0.04710 320 ARG B CB  
232  C CG  . ARG A 43  ? 1.42651 0.73057 0.98956 0.39826  0.40954  -0.03932 320 ARG B CG  
233  C CD  . ARG A 43  ? 1.41526 0.77152 1.02031 0.42357  0.41089  -0.00672 320 ARG B CD  
234  N NE  . ARG A 43  ? 1.46759 0.81948 1.07440 0.44178  0.43469  0.00408  320 ARG B NE  
235  C CZ  . ARG A 43  ? 1.47256 0.78292 1.06823 0.44818  0.45785  0.00563  320 ARG B CZ  
236  N NH1 . ARG A 43  ? 1.50295 0.76949 1.08252 0.43630  0.46181  -0.00455 320 ARG B NH1 
237  N NH2 . ARG A 43  ? 1.50317 0.81546 1.10580 0.46649  0.47911  0.01763  320 ARG B NH2 
238  N N   . TYR A 44  ? 1.57288 0.77330 1.04803 0.34368  0.40012  -0.11390 321 TYR B N   
239  C CA  . TYR A 44  ? 1.66401 0.83728 1.09099 0.33021  0.39547  -0.14164 321 TYR B CA  
240  C C   . TYR A 44  ? 1.65560 0.78862 1.06002 0.30076  0.38080  -0.17596 321 TYR B C   
241  O O   . TYR A 44  ? 1.72878 0.85108 1.09663 0.28573  0.36289  -0.20058 321 TYR B O   
242  C CB  . TYR A 44  ? 1.67787 0.82315 1.08013 0.34287  0.42328  -0.13916 321 TYR B CB  
243  C CG  . TYR A 44  ? 1.62364 0.81144 1.04740 0.36858  0.43465  -0.11029 321 TYR B CG  
244  C CD1 . TYR A 44  ? 1.66686 0.87951 1.07507 0.37050  0.42603  -0.11128 321 TYR B CD1 
245  C CD2 . TYR A 44  ? 1.57367 0.77818 1.03530 0.39032  0.45294  -0.08200 321 TYR B CD2 
246  C CE1 . TYR A 44  ? 1.66071 0.91415 1.09537 0.39172  0.43741  -0.08592 321 TYR B CE1 
247  C CE2 . TYR A 44  ? 1.54668 0.79408 1.03528 0.41216  0.46108  -0.05734 321 TYR B CE2 
248  C CZ  . TYR A 44  ? 1.61268 0.88501 1.09034 0.41187  0.45406  -0.05988 321 TYR B CZ  
249  O OH  . TYR A 44  ? 1.61290 0.92916 1.12315 0.43130  0.46332  -0.03657 321 TYR B OH  
250  N N   . TYR A 45  ? 1.64703 0.75877 1.07344 0.29163  0.38679  -0.17799 322 TYR B N   
251  C CA  . TYR A 45  ? 1.67888 0.75711 1.09629 0.26163  0.37291  -0.21046 322 TYR B CA  
252  C C   . TYR A 45  ? 1.71229 0.81938 1.15206 0.24694  0.34390  -0.21639 322 TYR B C   
253  O O   . TYR A 45  ? 1.82473 0.91028 1.26911 0.22068  0.33067  -0.24190 322 TYR B O   
254  C CB  . TYR A 45  ? 1.72389 0.76693 1.15928 0.25656  0.39412  -0.20955 322 TYR B CB  
255  N N   . LEU A 46  ? 1.64311 0.79860 1.09963 0.26216  0.33375  -0.19435 323 LEU B N   
256  C CA  . LEU A 46  ? 1.58314 0.76926 1.06561 0.24935  0.30779  -0.19563 323 LEU B CA  
257  C C   . LEU A 46  ? 1.57871 0.81721 1.05540 0.24477  0.27686  -0.19323 323 LEU B C   
258  O O   . LEU A 46  ? 1.54599 0.83064 1.05636 0.23064  0.24911  -0.18749 323 LEU B O   
259  C CB  . LEU A 46  ? 1.52036 0.73656 1.04875 0.26441  0.31608  -0.16342 323 LEU B CB  
260  C CG  . LEU A 46  ? 1.53572 0.72102 1.08411 0.26165  0.33686  -0.15777 323 LEU B CG  
261  C CD1 . LEU A 46  ? 1.48357 0.70006 1.06222 0.28508  0.34651  -0.12013 323 LEU B CD1 
262  C CD2 . LEU A 46  ? 1.60845 0.77358 1.17380 0.23176  0.32588  -0.18035 323 LEU B CD2 
263  N N   . THR A 47  ? 1.60851 0.83752 1.04205 0.25626  0.28297  -0.19749 324 THR B N   
264  C CA  . THR A 47  ? 1.50954 0.78791 0.93851 0.25797  0.26083  -0.18811 324 THR B CA  
265  C C   . THR A 47  ? 1.57228 0.86286 0.99133 0.22989  0.22167  -0.21014 324 THR B C   
266  O O   . THR A 47  ? 1.58008 0.91688 1.00523 0.22883  0.19964  -0.19977 324 THR B O   
267  C CB  . THR A 47  ? 1.54123 0.80078 0.92472 0.27888  0.28292  -0.18591 324 THR B CB  
268  O OG1 . THR A 47  ? 1.71456 0.90702 1.04273 0.27178  0.29414  -0.21587 324 THR B OG1 
269  C CG2 . THR A 47  ? 1.51978 0.78836 0.92792 0.30978  0.31652  -0.15765 324 THR B CG2 
270  N N   . ASN A 48  ? 1.58046 0.83215 0.98724 0.20736  0.21190  -0.24011 325 ASN B N   
271  C CA  . ASN A 48  ? 1.70711 0.97561 1.11355 0.18093  0.17102  -0.26092 325 ASN B CA  
272  C C   . ASN A 48  ? 1.66999 0.96614 1.13914 0.16090  0.15383  -0.26038 325 ASN B C   
273  O O   . ASN A 48  ? 1.67557 0.97504 1.15331 0.13597  0.12381  -0.28342 325 ASN B O   
274  C CB  . ASN A 48  ? 1.87659 1.08912 1.22852 0.16630  0.16429  -0.29829 325 ASN B CB  
275  C CG  . ASN A 48  ? 2.01029 1.18227 1.38211 0.14750  0.17224  -0.32089 325 ASN B CG  
276  O OD1 . ASN A 48  ? 1.99538 1.14130 1.38282 0.15859  0.20714  -0.31082 325 ASN B OD1 
277  N ND2 . ASN A 48  ? 2.11977 1.28667 1.49409 0.11899  0.13971  -0.35133 325 ASN B ND2 
278  N N   . GLN A 49  ? 1.59754 0.91293 1.11026 0.17188  0.17222  -0.23469 326 GLN B N   
279  C CA  . GLN A 49  ? 1.56614 0.90982 1.13653 0.15634  0.16017  -0.22882 326 GLN B CA  
280  C C   . GLN A 49  ? 1.41401 0.81722 1.01242 0.16925  0.15269  -0.19702 326 GLN B C   
281  O O   . GLN A 49  ? 1.36174 0.77242 0.97153 0.19005  0.17498  -0.17195 326 GLN B O   
282  C CB  . GLN A 49  ? 1.54687 0.85210 1.13821 0.15691  0.19004  -0.22759 326 GLN B CB  
283  C CG  . GLN A 49  ? 1.58354 0.82687 1.15272 0.14178  0.20051  -0.26012 326 GLN B CG  
284  C CD  . GLN A 49  ? 1.69165 0.89400 1.28107 0.14488  0.23498  -0.25518 326 GLN B CD  
285  O OE1 . GLN A 49  ? 1.75118 0.90084 1.31032 0.15646  0.26492  -0.26059 326 GLN B OE1 
286  N NE2 . GLN A 49  ? 1.70131 0.92446 1.34000 0.13569  0.23329  -0.24385 326 GLN B NE2 
287  N N   . GLU A 50  ? 1.42676 0.87199 1.03697 0.15712  0.12047  -0.19833 327 GLU B N   
288  C CA  . GLU A 50  ? 1.41870 0.91952 1.05366 0.16752  0.11282  -0.17008 327 GLU B CA  
289  C C   . GLU A 50  ? 1.33972 0.85369 1.02000 0.16966  0.12547  -0.15110 327 GLU B C   
290  O O   . GLU A 50  ? 1.29548 0.84047 0.98714 0.18652  0.13220  -0.12528 327 GLU B O   
291  C CB  . GLU A 50  ? 1.47350 1.01087 1.11616 0.15205  0.07702  -0.17656 327 GLU B CB  
292  C CG  . GLU A 50  ? 1.52567 1.06016 1.19944 0.12537  0.05628  -0.19780 327 GLU B CG  
293  C CD  . GLU A 50  ? 1.72020 1.28594 1.39694 0.11208  0.01874  -0.20709 327 GLU B CD  
294  O OE1 . GLU A 50  ? 1.79679 1.38224 1.44509 0.12392  0.01024  -0.19653 327 GLU B OE1 
295  O OE2 . GLU A 50  ? 1.75487 1.32487 1.46431 0.09058  -0.00097 -0.22430 327 GLU B OE2 
296  N N   . LYS A 51  ? 1.30179 0.79139 1.00583 0.15316  0.12925  -0.16383 328 LYS B N   
297  C CA  . LYS A 51  ? 1.28243 0.77871 1.02362 0.15458  0.14233  -0.14614 328 LYS B CA  
298  C C   . LYS A 51  ? 1.29742 0.76746 1.02531 0.17934  0.17475  -0.12787 328 LYS B C   
299  O O   . LYS A 51  ? 1.25630 0.73211 1.00564 0.18623  0.18566  -0.10869 328 LYS B O   
300  C CB  . LYS A 51  ? 1.24208 0.71670 1.01425 0.12916  0.14063  -0.16547 328 LYS B CB  
301  N N   . ALA A 52  ? 1.34947 0.78964 1.04082 0.19418  0.19048  -0.13273 329 ALA B N   
302  C CA  . ALA A 52  ? 1.25339 0.66984 0.93351 0.22078  0.22098  -0.11464 329 ALA B CA  
303  C C   . ALA A 52  ? 1.19946 0.65452 0.87483 0.24601  0.22155  -0.09062 329 ALA B C   
304  O O   . ALA A 52  ? 1.18627 0.63482 0.86265 0.27023  0.24212  -0.07081 329 ALA B O   
305  C CB  . ALA A 52  ? 1.31371 0.66926 0.96048 0.22335  0.24344  -0.13410 329 ALA B CB  
306  N N   . LEU A 53  ? 1.19510 0.69034 0.86782 0.24134  0.19975  -0.09145 330 LEU B N   
307  C CA  . LEU A 53  ? 1.12412 0.65515 0.79593 0.26323  0.20263  -0.07100 330 LEU B CA  
308  C C   . LEU A 53  ? 1.07126 0.63879 0.77627 0.27600  0.20232  -0.04367 330 LEU B C   
309  O O   . LEU A 53  ? 1.10076 0.67910 0.80928 0.30067  0.21622  -0.02536 330 LEU B O   
310  C CB  . LEU A 53  ? 1.07722 0.63994 0.73945 0.25314  0.18045  -0.07768 330 LEU B CB  
311  C CG  . LEU A 53  ? 1.05808 0.66180 0.72456 0.27062  0.18217  -0.05859 330 LEU B CG  
312  C CD1 . LEU A 53  ? 1.08140 0.66134 0.72819 0.29537  0.21118  -0.05352 330 LEU B CD1 
313  C CD2 . LEU A 53  ? 1.07137 0.69653 0.72340 0.25758  0.16105  -0.06728 330 LEU B CD2 
314  N N   . THR A 54  ? 1.02108 0.60790 0.75086 0.26022  0.18641  -0.04076 331 THR B N   
315  C CA  . THR A 54  ? 1.03967 0.65607 0.79303 0.27245  0.18556  -0.01611 331 THR B CA  
316  C C   . THR A 54  ? 1.10969 0.69041 0.85770 0.29222  0.20952  -0.00445 331 THR B C   
317  O O   . THR A 54  ? 1.03170 0.63287 0.78835 0.31430  0.21315  0.01773  331 THR B O   
318  C CB  . THR A 54  ? 1.03996 0.67762 0.81662 0.25185  0.16735  -0.01569 331 THR B CB  
319  O OG1 . THR A 54  ? 1.07339 0.67055 0.85144 0.23532  0.17405  -0.03036 331 THR B OG1 
320  C CG2 . THR A 54  ? 0.99602 0.67258 0.78044 0.23585  0.14338  -0.02292 331 THR B CG2 
321  N N   . LYS A 55  ? 1.10658 0.63330 0.84106 0.28490  0.22557  -0.01914 332 LYS B N   
322  C CA  . LYS A 55  ? 1.09682 0.58209 0.82208 0.30514  0.25193  -0.00782 332 LYS B CA  
323  C C   . LYS A 55  ? 1.16826 0.65092 0.88077 0.33398  0.26772  0.00218  332 LYS B C   
324  O O   . LYS A 55  ? 1.17250 0.65312 0.88802 0.36025  0.27999  0.02400  332 LYS B O   
325  C CB  . LYS A 55  ? 1.17086 0.59578 0.88555 0.28900  0.26853  -0.02839 332 LYS B CB  
326  C CG  . LYS A 55  ? 1.23188 0.64439 0.96340 0.27375  0.26909  -0.02651 332 LYS B CG  
327  C CD  . LYS A 55  ? 1.19770 0.65371 0.95283 0.24831  0.24058  -0.03436 332 LYS B CD  
328  C CE  . LYS A 55  ? 1.17763 0.61490 0.95194 0.23002  0.24549  -0.03700 332 LYS B CE  
329  N NZ  . LYS A 55  ? 1.29937 0.77306 1.09974 0.20330  0.21978  -0.04983 332 LYS B NZ  
330  N N   . PHE A 56  ? 1.12714 0.60911 0.82477 0.33078  0.26793  -0.01297 333 PHE B N   
331  C CA  . PHE A 56  ? 1.16349 0.64354 0.85184 0.35792  0.28599  -0.00392 333 PHE B CA  
332  C C   . PHE A 56  ? 1.12693 0.66755 0.84255 0.37648  0.27499  0.02090  333 PHE B C   
333  O O   . PHE A 56  ? 1.12161 0.66691 0.84757 0.40357  0.28763  0.04075  333 PHE B O   
334  C CB  . PHE A 56  ? 1.21782 0.68205 0.87913 0.34900  0.28901  -0.02611 333 PHE B CB  
335  C CG  . PHE A 56  ? 1.19395 0.66611 0.84993 0.37519  0.30685  -0.01615 333 PHE B CG  
336  C CD1 . PHE A 56  ? 1.25067 0.70022 0.90645 0.39127  0.32944  -0.00531 333 PHE B CD1 
337  C CD2 . PHE A 56  ? 1.13142 0.64460 0.79033 0.37445  0.29616  -0.01489 333 PHE B CD2 
338  C CE1 . PHE A 56  ? 1.21130 0.67753 0.87179 0.40868  0.34246  0.00558  333 PHE B CE1 
339  C CE2 . PHE A 56  ? 1.14794 0.66851 0.80693 0.39810  0.31603  -0.00554 333 PHE B CE2 
340  C CZ  . PHE A 56  ? 1.25176 0.75341 0.91549 0.41153  0.33634  0.00522  333 PHE B CZ  
341  N N   . LEU A 57  ? 1.01867 0.60784 0.74886 0.36087  0.25001  0.01992  334 LEU B N   
342  C CA  . LEU A 57  ? 1.02738 0.67569 0.78660 0.37429  0.23826  0.04036  334 LEU B CA  
343  C C   . LEU A 57  ? 1.04085 0.70043 0.81794 0.39029  0.23550  0.06222  334 LEU B C   
344  O O   . LEU A 57  ? 1.00197 0.69792 0.80132 0.41195  0.23355  0.08075  334 LEU B O   
345  C CB  . LEU A 57  ? 0.93046 0.62096 0.70051 0.35121  0.21270  0.03446  334 LEU B CB  
346  C CG  . LEU A 57  ? 0.99984 0.68402 0.74867 0.33765  0.21150  0.01572  334 LEU B CG  
347  C CD1 . LEU A 57  ? 0.90997 0.63401 0.67068 0.31732  0.18646  0.01331  334 LEU B CD1 
348  C CD2 . LEU A 57  ? 0.96156 0.64999 0.70607 0.35881  0.23075  0.02066  334 LEU B CD2 
349  N N   . LYS A 58  ? 1.05939 0.68770 0.82698 0.37997  0.23516  0.06009  335 LYS B N   
350  C CA  . LYS A 58  ? 1.07769 0.70694 0.85140 0.39526  0.23371  0.08069  335 LYS B CA  
351  C C   . LYS A 58  ? 1.11714 0.72803 0.88696 0.42373  0.25235  0.09582  335 LYS B C   
352  O O   . LYS A 58  ? 1.18109 0.81647 0.96166 0.43853  0.24356  0.11650  335 LYS B O   
353  C CB  . LYS A 58  ? 1.16689 0.75604 0.92727 0.37689  0.23651  0.07365  335 LYS B CB  
354  C CG  . LYS A 58  ? 1.04231 0.66092 0.81498 0.35156  0.21370  0.06969  335 LYS B CG  
355  C CD  . LYS A 58  ? 1.14920 0.72238 0.91298 0.33159  0.22261  0.05892  335 LYS B CD  
356  C CE  . LYS A 58  ? 0.99549 0.59594 0.77440 0.30760  0.20306  0.05583  335 LYS B CE  
357  N N   . CYS A 59  ? 1.17402 0.74734 0.92840 0.42364  0.27350  0.08487  336 CYS B N   
358  C CA  . CYS A 59  ? 1.24305 0.79510 0.99218 0.44028  0.29097  0.09734  336 CYS B CA  
359  C C   . CYS A 59  ? 1.22247 0.80641 0.98911 0.45836  0.29551  0.10549  336 CYS B C   
360  C CB  . CYS A 59  ? 1.19052 0.67709 0.91268 0.42762  0.31380  0.08043  336 CYS B CB  
361  S SG  . CYS A 59  ? 1.54598 1.01530 1.25523 0.42389  0.32910  0.05965  336 CYS B SG  
362  N N   . VAL A 60  ? 1.23610 0.86927 1.02406 0.45806  0.28126  0.10476  337 VAL B N   
363  C CA  . VAL A 60  ? 1.23939 0.90409 1.04825 0.47128  0.28762  0.10998  337 VAL B CA  
364  C C   . VAL A 60  ? 1.16932 0.88839 1.01505 0.48881  0.27174  0.13305  337 VAL B C   
365  O O   . VAL A 60  ? 1.18816 0.94688 1.05073 0.48467  0.24804  0.13873  337 VAL B O   
366  C CB  . VAL A 60  ? 1.16139 0.84683 0.97196 0.45955  0.28369  0.09528  337 VAL B CB  
367  C CG1 . VAL A 60  ? 1.02075 0.75507 0.86523 0.47242  0.28547  0.10565  337 VAL B CG1 
368  C CG2 . VAL A 60  ? 1.13939 0.76995 0.91058 0.44615  0.30119  0.07132  337 VAL B CG2 
369  N N   . ASN A 61  ? 1.20490 0.92584 1.06358 0.50792  0.28372  0.14540  338 ASN B N   
370  C CA  . ASN A 61  ? 1.20703 0.98572 1.10705 0.52425  0.26689  0.16412  338 ASN B CA  
371  C C   . ASN A 61  ? 1.16479 0.99540 1.09931 0.51969  0.26026  0.16010  338 ASN B C   
372  O O   . ASN A 61  ? 1.14778 0.98267 1.09686 0.52672  0.27822  0.15881  338 ASN B O   
373  C CB  . ASN A 61  ? 1.20181 0.97114 1.11144 0.54701  0.28174  0.17778  338 ASN B CB  
374  C CG  . ASN A 61  ? 1.33243 1.04514 1.20539 0.55186  0.29340  0.18214  338 ASN B CG  
375  O OD1 . ASN A 61  ? 1.31989 0.97791 1.16329 0.54684  0.31849  0.17173  338 ASN B OD1 
376  N ND2 . ASN A 61  ? 1.43729 1.16121 1.31053 0.56120  0.27588  0.19715  338 ASN B ND2 
377  N N   . TRP A 62  ? 1.14175 1.00907 1.08841 0.50712  0.23718  0.15785  339 TRP B N   
378  C CA  . TRP A 62  ? 1.11336 1.02994 1.09422 0.50177  0.23270  0.15462  339 TRP B CA  
379  C C   . TRP A 62  ? 1.20338 1.17180 1.23628 0.51733  0.22658  0.16863  339 TRP B C   
380  O O   . TRP A 62  ? 1.24634 1.24633 1.31082 0.51627  0.23403  0.16631  339 TRP B O   
381  C CB  . TRP A 62  ? 1.11930 1.06194 1.10158 0.48460  0.20994  0.14956  339 TRP B CB  
382  C CG  . TRP A 62  ? 1.12504 1.01774 1.06192 0.46990  0.21737  0.13390  339 TRP B CG  
383  C CD1 . TRP A 62  ? 1.05543 0.91199 0.96251 0.46388  0.21151  0.13183  339 TRP B CD1 
384  C CD2 . TRP A 62  ? 1.01279 0.88288 0.92825 0.45944  0.23289  0.11690  339 TRP B CD2 
385  N NE1 . TRP A 62  ? 1.02456 0.84104 0.89956 0.44928  0.22088  0.11342  339 TRP B NE1 
386  C CE2 . TRP A 62  ? 1.01299 0.83717 0.88956 0.44596  0.23209  0.10356  339 TRP B CE2 
387  C CE3 . TRP A 62  ? 0.97135 0.85366 0.89479 0.45926  0.24757  0.11119  339 TRP B CE3 
388  C CZ2 . TRP A 62  ? 1.03502 0.83084 0.88071 0.42516  0.23786  0.08315  339 TRP B CZ2 
389  C CZ3 . TRP A 62  ? 0.97124 0.81820 0.85682 0.44789  0.25933  0.09282  339 TRP B CZ3 
390  C CH2 . TRP A 62  ? 0.97034 0.77667 0.81731 0.42756  0.25058  0.07830  339 TRP B CH2 
391  N N   . ASP A 63  ? 1.11661 1.09125 1.15830 0.53213  0.21467  0.18258  340 ASP B N   
392  C CA  . ASP A 63  ? 1.17255 1.19321 1.26491 0.54906  0.20776  0.19497  340 ASP B CA  
393  C C   . ASP A 63  ? 1.28005 1.29237 1.38916 0.55906  0.23787  0.19356  340 ASP B C   
394  O O   . ASP A 63  ? 1.30138 1.36122 1.46260 0.56465  0.23659  0.19719  340 ASP B O   
395  C CB  . ASP A 63  ? 1.18024 1.19180 1.26444 0.56594  0.19437  0.20945  340 ASP B CB  
396  N N   . LEU A 64  ? 1.31311 1.26348 1.37878 0.56087  0.26531  0.18784  341 LEU B N   
397  C CA  . LEU A 64  ? 1.19620 1.12875 1.26927 0.57131  0.29677  0.18675  341 LEU B CA  
398  C C   . LEU A 64  ? 1.18445 1.11741 1.25407 0.55645  0.31248  0.17258  341 LEU B C   
399  O O   . LEU A 64  ? 1.22658 1.12220 1.25045 0.54037  0.31693  0.15853  341 LEU B O   
400  C CB  . LEU A 64  ? 1.24752 1.10985 1.27142 0.57719  0.31929  0.18492  341 LEU B CB  
401  C CG  . LEU A 64  ? 1.25181 1.10190 1.26718 0.59093  0.30770  0.19880  341 LEU B CG  
402  C CD1 . LEU A 64  ? 1.25822 1.03773 1.22922 0.59592  0.33553  0.19645  341 LEU B CD1 
403  C CD2 . LEU A 64  ? 1.16172 1.06378 1.23062 0.61246  0.29378  0.21635  341 LEU B CD2 
404  N N   . PRO A 65  ? 1.18217 1.15302 1.29726 0.56161  0.32213  0.17540  342 PRO B N   
405  C CA  . PRO A 65  ? 1.17372 1.14384 1.28355 0.54832  0.33903  0.16360  342 PRO B CA  
406  C C   . PRO A 65  ? 1.16268 1.06170 1.21172 0.54442  0.36925  0.15079  342 PRO B C   
407  O O   . PRO A 65  ? 1.19036 1.06818 1.20288 0.52816  0.37192  0.13691  342 PRO B O   
408  C CB  . PRO A 65  ? 1.04458 1.05996 1.21665 0.55949  0.34946  0.17182  342 PRO B CB  
409  C CG  . PRO A 65  ? 1.16536 1.22711 1.38611 0.57347  0.32249  0.18625  342 PRO B CG  
410  C CD  . PRO A 65  ? 1.07993 1.09549 1.25441 0.58056  0.31738  0.18982  342 PRO B CD  
411  N N   . GLN A 66  ? 1.13801 1.00137 1.17652 0.55921  0.39017  0.15507  343 GLN B N   
412  C CA  . GLN A 66  ? 1.18633 0.97982 1.16685 0.55480  0.41968  0.14144  343 GLN B CA  
413  C C   . GLN A 66  ? 1.22628 0.97529 1.15026 0.53875  0.40904  0.12720  343 GLN B C   
414  O O   . GLN A 66  ? 1.20614 0.92041 1.08629 0.52403  0.41822  0.10973  343 GLN B O   
415  C CB  . GLN A 66  ? 1.24422 1.00828 1.22635 0.57383  0.44306  0.14985  343 GLN B CB  
416  C CG  . GLN A 66  ? 1.30606 0.99719 1.22889 0.56859  0.47354  0.13510  343 GLN B CG  
417  C CD  . GLN A 66  ? 1.41309 1.08238 1.34601 0.58794  0.50205  0.14435  343 GLN B CD  
418  O OE1 . GLN A 66  ? 1.43484 1.14501 1.42141 0.60655  0.49911  0.16208  343 GLN B OE1 
419  N NE2 . GLN A 66  ? 1.42402 1.02808 1.30509 0.58361  0.52922  0.13161  343 GLN B NE2 
420  N N   . GLU A 67  ? 1.25957 1.00861 1.18406 0.54150  0.39028  0.13405  344 GLU B N   
421  C CA  . GLU A 67  ? 1.18695 0.89536 1.06469 0.52552  0.38092  0.12058  344 GLU B CA  
422  C C   . GLU A 67  ? 1.15472 0.88866 1.02950 0.50781  0.36092  0.11090  344 GLU B C   
423  O O   . GLU A 67  ? 1.12727 0.82329 0.95870 0.49162  0.36061  0.09290  344 GLU B O   
424  C CB  . GLU A 67  ? 1.21112 0.91382 1.09113 0.53272  0.36749  0.13210  344 GLU B CB  
425  C CG  . GLU A 67  ? 1.23697 0.88255 1.06780 0.51730  0.36782  0.11754  344 GLU B CG  
426  C CD  . GLU A 67  ? 1.26171 0.89880 1.09212 0.52345  0.35720  0.12989  344 GLU B CD  
427  O OE1 . GLU A 67  ? 1.40605 1.04330 1.25046 0.54279  0.36498  0.14610  344 GLU B OE1 
428  O OE2 . GLU A 67  ? 1.28411 0.91274 1.09884 0.50927  0.34184  0.12364  344 GLU B OE2 
429  N N   . ALA A 68  ? 1.13764 0.93570 1.05917 0.51001  0.34345  0.12170  345 ALA B N   
430  C CA  . ALA A 68  ? 1.08649 0.90900 1.00616 0.49361  0.32715  0.11333  345 ALA B CA  
431  C C   . ALA A 68  ? 1.15111 0.95104 1.04198 0.48480  0.34670  0.09856  345 ALA B C   
432  O O   . ALA A 68  ? 1.15619 0.93623 1.01082 0.46964  0.34066  0.08355  345 ALA B O   
433  C CB  . ALA A 68  ? 1.05679 0.95214 1.03462 0.49646  0.30583  0.12728  345 ALA B CB  
434  N N   . LYS A 69  ? 1.08481 0.88475 0.98855 0.49459  0.37048  0.10246  346 LYS B N   
435  C CA  . LYS A 69  ? 1.14714 0.91482 1.01310 0.48728  0.39219  0.08883  346 LYS B CA  
436  C C   . LYS A 69  ? 1.22898 0.92708 1.02602 0.47699  0.39771  0.06891  346 LYS B C   
437  O O   . LYS A 69  ? 1.23127 0.91164 0.98924 0.46213  0.39079  0.05327  346 LYS B O   
438  C CB  . LYS A 69  ? 1.14614 0.91437 1.03332 0.50092  0.42048  0.09678  346 LYS B CB  
439  N N   . GLN A 70  ? 1.19464 0.85276 0.97680 0.48419  0.40925  0.06857  347 GLN B N   
440  C CA  . GLN A 70  ? 1.24015 0.83175 0.96178 0.47236  0.41430  0.04785  347 GLN B CA  
441  C C   . GLN A 70  ? 1.27523 0.86438 0.97844 0.45564  0.38830  0.03569  347 GLN B C   
442  O O   . GLN A 70  ? 1.34505 0.89282 0.99835 0.44026  0.38670  0.01357  347 GLN B O   
443  C CB  . GLN A 70  ? 1.28176 0.83879 1.00116 0.48216  0.42751  0.05257  347 GLN B CB  
444  C CG  . GLN A 70  ? 1.46523 0.94943 1.12521 0.47157  0.44361  0.03063  347 GLN B CG  
445  C CD  . GLN A 70  ? 1.57430 1.02221 1.23049 0.47637  0.45212  0.03341  347 GLN B CD  
446  O OE1 . GLN A 70  ? 1.55622 0.97111 1.18737 0.46192  0.44302  0.01940  347 GLN B OE1 
447  N NE2 . GLN A 70  ? 1.53980 0.99307 1.22216 0.49640  0.47055  0.05145  347 GLN B NE2 
448  N N   . ALA A 71  ? 1.22344 0.85564 0.96570 0.45817  0.36678  0.04922  348 ALA B N   
449  C CA  . ALA A 71  ? 1.17970 0.80929 0.90858 0.44319  0.34370  0.03925  348 ALA B CA  
450  C C   . ALA A 71  ? 1.20956 0.85461 0.92281 0.43127  0.33376  0.02796  348 ALA B C   
451  O O   . ALA A 71  ? 1.26218 0.87944 0.93920 0.41379  0.32209  0.00902  348 ALA B O   
452  C CB  . ALA A 71  ? 1.14528 0.81708 0.91724 0.44956  0.32398  0.05811  348 ALA B CB  
453  N N   . LEU A 72  ? 1.19741 0.88841 0.93988 0.43760  0.33638  0.03955  349 LEU B N   
454  C CA  . LEU A 72  ? 1.20165 0.90573 0.92699 0.42688  0.33023  0.03096  349 LEU B CA  
455  C C   . LEU A 72  ? 1.24365 0.89274 0.90613 0.42024  0.34626  0.01117  349 LEU B C   
456  O O   . LEU A 72  ? 1.26158 0.90115 0.88936 0.40051  0.32937  -0.00256 349 LEU B O   
457  C CB  . LEU A 72  ? 1.07828 0.84320 0.85447 0.43433  0.33249  0.04874  349 LEU B CB  
458  C CG  . LEU A 72  ? 1.05551 0.87797 0.89092 0.43855  0.31092  0.06614  349 LEU B CG  
459  C CD1 . LEU A 72  ? 0.96811 0.85138 0.85660 0.44160  0.31111  0.08019  349 LEU B CD1 
460  C CD2 . LEU A 72  ? 1.00108 0.83079 0.82796 0.41400  0.27695  0.06033  349 LEU B CD2 
461  N N   . GLU A 73  ? 1.26092 0.87743 0.90991 0.42802  0.37033  0.01079  350 GLU B N   
462  C CA  . GLU A 73  ? 1.33005 0.88733 0.91244 0.41966  0.38250  -0.01004 350 GLU B CA  
463  C C   . GLU A 73  ? 1.39340 0.90896 0.93231 0.40346  0.36429  -0.03324 350 GLU B C   
464  O O   . GLU A 73  ? 1.43812 0.92945 0.92697 0.39032  0.35389  -0.05206 350 GLU B O   
465  C CB  . GLU A 73  ? 1.31527 0.84043 0.89183 0.43060  0.41134  -0.00694 350 GLU B CB  
466  C CG  . GLU A 73  ? 1.38248 0.93414 0.98676 0.44331  0.43369  0.00931  350 GLU B CG  
467  N N   . LEU A 74  ? 1.35927 0.86644 0.91779 0.40361  0.35906  -0.03196 351 LEU B N   
468  C CA  . LEU A 74  ? 1.35965 0.82700 0.88605 0.38648  0.34375  -0.05435 351 LEU B CA  
469  C C   . LEU A 74  ? 1.34300 0.84871 0.88067 0.36291  0.30605  -0.05689 351 LEU B C   
470  O O   . LEU A 74  ? 1.39685 0.87822 0.90216 0.34081  0.28669  -0.07819 351 LEU B O   
471  C CB  . LEU A 74  ? 1.32145 0.77742 0.87502 0.38970  0.34730  -0.04737 351 LEU B CB  
472  C CG  . LEU A 74  ? 1.44950 0.85164 0.97869 0.39014  0.36927  -0.05607 351 LEU B CG  
473  C CD1 . LEU A 74  ? 1.39066 0.78642 0.94967 0.39502  0.37324  -0.04451 351 LEU B CD1 
474  C CD2 . LEU A 74  ? 1.49084 0.84047 0.96316 0.36892  0.36273  -0.08870 351 LEU B CD2 
475  N N   . LEU A 75  ? 1.26475 0.83172 0.85116 0.36632  0.29390  -0.03567 352 LEU B N   
476  C CA  . LEU A 75  ? 1.28643 0.89068 0.88438 0.34481  0.26105  -0.03639 352 LEU B CA  
477  C C   . LEU A 75  ? 1.33115 0.92329 0.88454 0.33478  0.25513  -0.04966 352 LEU B C   
478  O O   . LEU A 75  ? 1.30853 0.90364 0.84898 0.31383  0.22757  -0.06104 352 LEU B O   
479  C CB  . LEU A 75  ? 1.23619 0.90449 0.88979 0.35203  0.25378  -0.01215 352 LEU B CB  
480  C CG  . LEU A 75  ? 1.17066 0.88125 0.84292 0.33239  0.22362  -0.00932 352 LEU B CG  
481  C CD1 . LEU A 75  ? 1.16256 0.86555 0.84042 0.31330  0.20072  -0.01762 352 LEU B CD1 
482  C CD2 . LEU A 75  ? 1.09592 0.86464 0.81933 0.34239  0.22290  0.01303  352 LEU B CD2 
483  N N   . GLY A 76  ? 1.37361 0.94965 0.90186 0.35077  0.28177  -0.04797 353 GLY B N   
484  C CA  . GLY A 76  ? 1.35082 0.90665 0.82616 0.34408  0.27948  -0.05977 353 GLY B CA  
485  C C   . GLY A 76  ? 1.40457 0.90080 0.81849 0.33128  0.27129  -0.08768 353 GLY B C   
486  O O   . GLY A 76  ? 1.53952 1.03006 0.92091 0.31468  0.24562  -0.10066 353 GLY B O   
487  N N   . LYS A 77  ? 1.49687 0.94778 0.89501 0.33884  0.29194  -0.09776 354 LYS B N   
488  C CA  . LYS A 77  ? 1.50160 0.89305 0.84264 0.32518  0.28500  -0.12716 354 LYS B CA  
489  C C   . LYS A 77  ? 1.41831 0.81481 0.78100 0.30154  0.25286  -0.13977 354 LYS B C   
490  O O   . LYS A 77  ? 1.46610 0.81811 0.79002 0.28668  0.24275  -0.16632 354 LYS B O   
491  C CB  . LYS A 77  ? 1.53757 0.87297 0.85224 0.34153  0.32288  -0.13466 354 LYS B CB  
492  N N   . TRP A 78  ? 1.27212 0.72002 0.69520 0.29673  0.23693  -0.12286 355 TRP B N   
493  C CA  . TRP A 78  ? 1.36585 0.81409 0.81509 0.27707  0.21545  -0.13272 355 TRP B CA  
494  C C   . TRP A 78  ? 1.41937 0.88333 0.86100 0.25323  0.17724  -0.14654 355 TRP B C   
495  O O   . TRP A 78  ? 1.39198 0.89215 0.83554 0.25312  0.16298  -0.13608 355 TRP B O   
496  C CB  . TRP A 78  ? 1.34427 0.83501 0.85634 0.28330  0.21684  -0.10861 355 TRP B CB  
497  C CG  . TRP A 78  ? 1.29245 0.76110 0.82371 0.27257  0.21541  -0.11677 355 TRP B CG  
498  C CD1 . TRP A 78  ? 1.26724 0.73368 0.80831 0.24744  0.19082  -0.13280 355 TRP B CD1 
499  C CD2 . TRP A 78  ? 1.35543 0.79802 0.89924 0.28740  0.24224  -0.10902 355 TRP B CD2 
500  N NE1 . TRP A 78  ? 1.31132 0.75021 0.87039 0.24427  0.20297  -0.13609 355 TRP B NE1 
501  C CE2 . TRP A 78  ? 1.32492 0.74710 0.88290 0.26920  0.23434  -0.12102 355 TRP B CE2 
502  C CE3 . TRP A 78  ? 1.30083 0.73551 0.84764 0.31540  0.27296  -0.09220 355 TRP B CE3 
503  C CZ2 . TRP A 78  ? 1.36869 0.75869 0.93802 0.27829  0.25758  -0.11600 355 TRP B CZ2 
504  C CZ3 . TRP A 78  ? 1.28849 0.69383 0.84724 0.32572  0.29308  -0.08683 355 TRP B CZ3 
505  C CH2 . TRP A 78  ? 1.30412 0.68504 0.87097 0.30736  0.28617  -0.09842 355 TRP B CH2 
506  N N   . LYS A 79  ? 1.40057 0.83755 0.83730 0.23318  0.16123  -0.16993 356 LYS B N   
507  C CA  . LYS A 79  ? 1.39368 0.85143 0.83887 0.21018  0.12274  -0.18228 356 LYS B CA  
508  C C   . LYS A 79  ? 1.33023 0.84905 0.83062 0.20858  0.10921  -0.15859 356 LYS B C   
509  O O   . LYS A 79  ? 1.24756 0.78121 0.79341 0.20920  0.11761  -0.14637 356 LYS B O   
510  C CB  . LYS A 79  ? 1.49380 0.92172 0.94904 0.18885  0.11197  -0.20752 356 LYS B CB  
511  C CG  . LYS A 79  ? 1.48572 0.93301 0.95324 0.16443  0.07091  -0.22424 356 LYS B CG  
512  C CD  . LYS A 79  ? 1.60396 1.00677 1.05937 0.14405  0.06180  -0.25851 356 LYS B CD  
513  C CE  . LYS A 79  ? 1.53509 0.96271 1.01944 0.11896  0.02046  -0.27519 356 LYS B CE  
514  N NZ  . LYS A 79  ? 1.66253 1.11512 1.21999 0.10608  0.02099  -0.26825 356 LYS B NZ  
515  N N   . PRO A 80  ? 1.23729 0.78832 0.73159 0.20720  0.08988  -0.15149 357 PRO B N   
516  C CA  . PRO A 80  ? 1.29879 0.90519 0.84147 0.20832  0.08261  -0.12752 357 PRO B CA  
517  C C   . PRO A 80  ? 1.25349 0.87852 0.84712 0.19116  0.06686  -0.12894 357 PRO B C   
518  O O   . PRO A 80  ? 1.25706 0.86699 0.85181 0.17303  0.04787  -0.14966 357 PRO B O   
519  C CB  . PRO A 80  ? 1.26368 0.88833 0.78146 0.20647  0.06277  -0.12608 357 PRO B CB  
520  C CG  . PRO A 80  ? 1.27279 0.85145 0.72259 0.21319  0.07002  -0.14204 357 PRO B CG  
521  C CD  . PRO A 80  ? 1.28860 0.82323 0.72724 0.20515  0.07422  -0.16496 357 PRO B CD  
522  N N   . MET A 81  ? 1.17905 0.83681 0.81558 0.19682  0.07510  -0.10725 358 MET B N   
523  C CA  . MET A 81  ? 1.22544 0.89479 0.90675 0.18300  0.06709  -0.10651 358 MET B CA  
524  C C   . MET A 81  ? 1.13542 0.84283 0.84205 0.16873  0.03994  -0.10405 358 MET B C   
525  O O   . MET A 81  ? 1.07783 0.81074 0.77474 0.17343  0.03117  -0.09488 358 MET B O   
526  C CB  . MET A 81  ? 1.16142 0.84218 0.87072 0.19619  0.08774  -0.08523 358 MET B CB  
527  C CG  . MET A 81  ? 1.02402 0.75205 0.75474 0.20449  0.08500  -0.06231 358 MET B CG  
528  S SD  . MET A 81  ? 1.10535 0.84592 0.87103 0.21437  0.09919  -0.04151 358 MET B SD  
529  C CE  . MET A 81  ? 1.12011 0.83849 0.86446 0.24123  0.12724  -0.03408 358 MET B CE  
530  N N   . ASP A 82  ? 1.13421 0.84261 0.87464 0.15135  0.02895  -0.11252 359 ASP B N   
531  C CA  . ASP A 82  ? 1.05573 0.79864 0.82697 0.13788  0.00522  -0.11041 359 ASP B CA  
532  C C   . ASP A 82  ? 1.01918 0.80036 0.81165 0.14630  0.01029  -0.08515 359 ASP B C   
533  O O   . ASP A 82  ? 0.98951 0.77216 0.78669 0.15862  0.03028  -0.07033 359 ASP B O   
534  C CB  . ASP A 82  ? 1.06308 0.79920 0.87466 0.11903  -0.00025 -0.12220 359 ASP B CB  
535  C CG  . ASP A 82  ? 1.24606 0.94135 1.04289 0.10939  -0.00074 -0.14818 359 ASP B CG  
536  O OD1 . ASP A 82  ? 1.31438 0.99386 1.07016 0.11119  -0.01167 -0.16242 359 ASP B OD1 
537  O OD2 . ASP A 82  ? 1.37787 1.05340 1.20155 0.09985  0.01133  -0.15492 359 ASP B OD2 
538  N N   . VAL A 83  ? 0.98147 0.79333 0.78699 0.13969  -0.00913 -0.08082 360 VAL B N   
539  C CA  . VAL A 83  ? 0.94410 0.79153 0.77556 0.14269  -0.00643 -0.05998 360 VAL B CA  
540  C C   . VAL A 83  ? 0.91891 0.76685 0.78497 0.13818  0.00512  -0.05316 360 VAL B C   
541  O O   . VAL A 83  ? 0.86618 0.72826 0.73935 0.14748  0.01748  -0.03626 360 VAL B O   
542  C CB  . VAL A 83  ? 0.90640 0.78026 0.75015 0.13391  -0.02885 -0.05898 360 VAL B CB  
543  C CG1 . VAL A 83  ? 0.89353 0.79970 0.76570 0.13453  -0.02427 -0.03966 360 VAL B CG1 
544  C CG2 . VAL A 83  ? 0.90027 0.77030 0.70183 0.14169  -0.03777 -0.06200 360 VAL B CG2 
545  N N   . GLU A 84  ? 0.88169 0.71337 0.76937 0.12382  0.00142  -0.06643 361 GLU B N   
546  C CA  . GLU A 84  ? 0.91283 0.74006 0.82999 0.11938  0.01514  -0.05925 361 GLU B CA  
547  C C   . GLU A 84  ? 0.90015 0.70574 0.79938 0.13470  0.03840  -0.05007 361 GLU B C   
548  O O   . GLU A 84  ? 0.89369 0.70537 0.80325 0.14017  0.04934  -0.03468 361 GLU B O   
549  C CB  . GLU A 84  ? 0.92784 0.73726 0.87370 0.10098  0.01152  -0.07645 361 GLU B CB  
550  C CG  . GLU A 84  ? 0.97196 0.80515 0.94521 0.08624  -0.01286 -0.08532 361 GLU B CG  
551  C CD  . GLU A 84  ? 1.06400 0.89501 1.01144 0.08544  -0.03453 -0.10121 361 GLU B CD  
552  O OE1 . GLU A 84  ? 1.04025 0.84518 0.94955 0.09356  -0.02768 -0.10864 361 GLU B OE1 
553  O OE2 . GLU A 84  ? 1.10460 0.95812 1.06750 0.07786  -0.05808 -0.10577 361 GLU B OE2 
554  N N   . ASP A 85  ? 0.90149 0.67934 0.77212 0.14256  0.04609  -0.05947 362 ASP B N   
555  C CA  . ASP A 85  ? 0.95963 0.71631 0.81428 0.15992  0.06870  -0.04971 362 ASP B CA  
556  C C   . ASP A 85  ? 0.93604 0.71947 0.77912 0.17865  0.07200  -0.03168 362 ASP B C   
557  O O   . ASP A 85  ? 0.98349 0.76421 0.82533 0.19402  0.08640  -0.01748 362 ASP B O   
558  C CB  . ASP A 85  ? 1.00377 0.71821 0.83314 0.16214  0.07891  -0.06642 362 ASP B CB  
559  C CG  . ASP A 85  ? 1.15128 0.83754 0.99735 0.14253  0.07796  -0.08576 362 ASP B CG  
560  O OD1 . ASP A 85  ? 1.22883 0.91358 1.10335 0.13489  0.08445  -0.08030 362 ASP B OD1 
561  O OD2 . ASP A 85  ? 1.24323 0.90789 1.07428 0.13407  0.07115  -0.10725 362 ASP B OD2 
562  N N   . SER A 86  ? 0.87579 0.68459 0.71144 0.17829  0.05919  -0.03177 363 SER B N   
563  C CA  . SER A 86  ? 0.89405 0.72962 0.72538 0.19415  0.06438  -0.01571 363 SER B CA  
564  C C   . SER A 86  ? 0.89307 0.75903 0.75105 0.19483  0.06250  0.00131  363 SER B C   
565  O O   . SER A 86  ? 0.88129 0.76473 0.74236 0.20975  0.06989  0.01526  363 SER B O   
566  C CB  . SER A 86  ? 0.86763 0.71920 0.68400 0.19238  0.05389  -0.01928 363 SER B CB  
567  O OG  . SER A 86  ? 0.86897 0.74747 0.70516 0.17892  0.03690  -0.01683 363 SER B OG  
568  N N   . LEU A 87  ? 0.80960 0.68204 0.68783 0.17898  0.05267  -0.00027 364 LEU B N   
569  C CA  . LEU A 87  ? 0.78862 0.68236 0.68565 0.17902  0.05239  0.01417  364 LEU B CA  
570  C C   . LEU A 87  ? 0.80750 0.68871 0.69799 0.19546  0.06628  0.02522  364 LEU B C   
571  O O   . LEU A 87  ? 0.74318 0.64845 0.64022 0.20383  0.06490  0.03903  364 LEU B O   
572  C CB  . LEU A 87  ? 0.72571 0.61521 0.64287 0.16081  0.04651  0.00939  364 LEU B CB  
573  C CG  . LEU A 87  ? 0.74193 0.64984 0.67177 0.14620  0.03016  0.00168  364 LEU B CG  
574  C CD1 . LEU A 87  ? 0.69314 0.59416 0.64958 0.12899  0.02680  -0.00461 364 LEU B CD1 
575  C CD2 . LEU A 87  ? 0.68566 0.62955 0.61923 0.14899  0.02363  0.01304  364 LEU B CD2 
576  N N   . GLU A 88  ? 0.84525 0.68833 0.72234 0.20085  0.07903  0.01910  365 GLU B N   
577  C CA  . GLU A 88  ? 0.85019 0.67668 0.71804 0.21944  0.09316  0.03097  365 GLU B CA  
578  C C   . GLU A 88  ? 0.83665 0.69012 0.70291 0.23952  0.09395  0.04303  365 GLU B C   
579  O O   . GLU A 88  ? 0.84116 0.70671 0.71116 0.25325  0.09465  0.05798  365 GLU B O   
580  C CB  . GLU A 88  ? 0.89773 0.67571 0.75031 0.22211  0.10925  0.02095  365 GLU B CB  
581  C CG  . GLU A 88  ? 0.97624 0.73320 0.81503 0.24628  0.12616  0.03423  365 GLU B CG  
582  C CD  . GLU A 88  ? 1.07842 0.78023 0.90304 0.24682  0.14569  0.02512  365 GLU B CD  
583  O OE1 . GLU A 88  ? 1.09626 0.77743 0.92633 0.22610  0.14536  0.00820  365 GLU B OE1 
584  O OE2 . GLU A 88  ? 1.18925 0.86832 0.99981 0.26813  0.16169  0.03469  365 GLU B OE2 
585  N N   . LEU A 89  ? 0.81275 0.67571 0.67385 0.24186  0.09386  0.03668  366 LEU B N   
586  C CA  . LEU A 89  ? 0.83963 0.72692 0.70472 0.26078  0.09890  0.04712  366 LEU B CA  
587  C C   . LEU A 89  ? 0.81315 0.74888 0.70198 0.25982  0.08658  0.05879  366 LEU B C   
588  O O   . LEU A 89  ? 0.80817 0.76898 0.70962 0.27555  0.08995  0.06876  366 LEU B O   
589  C CB  . LEU A 89  ? 0.91991 0.80010 0.76962 0.26237  0.10540  0.03681  366 LEU B CB  
590  C CG  . LEU A 89  ? 0.89701 0.72812 0.71899 0.26219  0.11701  0.02157  366 LEU B CG  
591  C CD1 . LEU A 89  ? 0.91936 0.74412 0.72019 0.26685  0.12416  0.01344  366 LEU B CD1 
592  C CD2 . LEU A 89  ? 0.89647 0.69834 0.71374 0.27906  0.13379  0.02768  366 LEU B CD2 
593  N N   . LEU A 90  ? 0.76159 0.71124 0.65974 0.24159  0.07332  0.05709  367 LEU B N   
594  C CA  . LEU A 90  ? 0.72161 0.71256 0.64074 0.23881  0.06244  0.06656  367 LEU B CA  
595  C C   . LEU A 90  ? 0.74516 0.73759 0.66722 0.24377  0.05787  0.07682  367 LEU B C   
596  O O   . LEU A 90  ? 0.68557 0.71101 0.62304 0.24246  0.04759  0.08390  367 LEU B O   
597  C CB  . LEU A 90  ? 0.68912 0.69303 0.61506 0.21777  0.05214  0.06010  367 LEU B CB  
598  C CG  . LEU A 90  ? 0.74423 0.75114 0.66327 0.21535  0.05430  0.05281  367 LEU B CG  
599  C CD1 . LEU A 90  ? 0.71237 0.72789 0.63596 0.19701  0.04348  0.04781  367 LEU B CD1 
600  C CD2 . LEU A 90  ? 0.66169 0.69647 0.59136 0.22848  0.06133  0.06047  367 LEU B CD2 
601  N N   . SER A 91  ? 0.74331 0.69830 0.64844 0.24937  0.06579  0.07745  368 SER B N   
602  C CA  . SER A 91  ? 0.75952 0.70825 0.65818 0.25555  0.06283  0.08807  368 SER B CA  
603  C C   . SER A 91  ? 0.78316 0.75520 0.68781 0.27875  0.05923  0.10136  368 SER B C   
604  O O   . SER A 91  ? 0.82930 0.82180 0.74769 0.28962  0.06212  0.10226  368 SER B O   
605  C CB  . SER A 91  ? 0.73815 0.63564 0.61579 0.25625  0.07634  0.08606  368 SER B CB  
606  O OG  . SER A 91  ? 0.85098 0.72510 0.71661 0.27702  0.08930  0.09032  368 SER B OG  
607  N N   . SER A 92  ? 0.75432 0.72258 0.64849 0.28710  0.05294  0.11193  369 SER B N   
608  C CA  . SER A 92  ? 0.77963 0.77591 0.68270 0.30883  0.04339  0.12477  369 SER B CA  
609  C C   . SER A 92  ? 0.91848 0.89578 0.81616 0.33450  0.05658  0.13180  369 SER B C   
610  O O   . SER A 92  ? 0.85303 0.85980 0.76779 0.35461  0.04968  0.14188  369 SER B O   
611  C CB  . SER A 92  ? 0.86562 0.85711 0.75005 0.31182  0.03110  0.13383  369 SER B CB  
612  O OG  . SER A 92  ? 0.91448 0.85377 0.76584 0.32234  0.04464  0.13954  369 SER B OG  
613  N N   . HIS A 93  ? 0.90511 0.83427 0.78236 0.33445  0.07557  0.12642  370 HIS B N   
614  C CA  . HIS A 93  ? 0.90346 0.80881 0.77319 0.35927  0.09101  0.13306  370 HIS B CA  
615  C C   . HIS A 93  ? 0.92958 0.85444 0.81980 0.36507  0.09902  0.12771  370 HIS B C   
616  O O   . HIS A 93  ? 1.00571 0.91188 0.89226 0.38640  0.11406  0.13274  370 HIS B O   
617  C CB  . HIS A 93  ? 0.95089 0.79328 0.79143 0.35644  0.11120  0.12792  370 HIS B CB  
618  N N   . TYR A 94  ? 0.83601 0.79356 0.74510 0.34796  0.09220  0.11834  371 TYR B N   
619  C CA  . TYR A 94  ? 0.86075 0.83019 0.78295 0.35315  0.10350  0.11315  371 TYR B CA  
620  C C   . TYR A 94  ? 0.81963 0.84778 0.77829 0.35422  0.09190  0.11835  371 TYR B C   
621  O O   . TYR A 94  ? 0.73859 0.79249 0.70732 0.33497  0.07772  0.11462  371 TYR B O   
622  C CB  . TYR A 94  ? 0.81942 0.76388 0.72454 0.33256  0.11091  0.09567  371 TYR B CB  
623  C CG  . TYR A 94  ? 0.88048 0.76806 0.75602 0.32985  0.12394  0.08703  371 TYR B CG  
624  C CD1 . TYR A 94  ? 0.90048 0.76550 0.76468 0.31367  0.11847  0.08279  371 TYR B CD1 
625  C CD2 . TYR A 94  ? 0.95617 0.81089 0.81682 0.34225  0.14385  0.08190  371 TYR B CD2 
626  C CE1 . TYR A 94  ? 0.92311 0.73672 0.76644 0.30895  0.13193  0.07343  371 TYR B CE1 
627  C CE2 . TYR A 94  ? 0.98621 0.78734 0.82173 0.33751  0.15645  0.07174  371 TYR B CE2 
628  C CZ  . TYR A 94  ? 1.01353 0.79568 0.84279 0.32011  0.15000  0.06726  371 TYR B CZ  
629  O OH  . TYR A 94  ? 1.08945 0.81927 0.89992 0.31327  0.16381  0.05584  371 TYR B OH  
630  N N   . THR A 95  ? 0.83454 0.88287 0.81599 0.37668  0.09981  0.12672  372 THR B N   
631  C CA  . THR A 95  ? 0.73372 0.83959 0.75866 0.38025  0.09135  0.13219  372 THR B CA  
632  C C   . THR A 95  ? 0.77647 0.89205 0.81919 0.38685  0.11195  0.12893  372 THR B C   
633  O O   . THR A 95  ? 0.81026 0.96947 0.88794 0.38139  0.10905  0.12930  372 THR B O   
634  C CB  . THR A 95  ? 0.73890 0.87166 0.78682 0.40333  0.07834  0.14760  372 THR B CB  
635  O OG1 . THR A 95  ? 0.88689 0.99426 0.92948 0.43053  0.09603  0.15524  372 THR B OG1 
636  C CG2 . THR A 95  ? 0.73755 0.85633 0.76010 0.39775  0.05911  0.15145  372 THR B CG2 
637  N N   . ASN A 96  ? 0.74575 0.81939 0.76441 0.39783  0.13454  0.12526  373 ASN B N   
638  C CA  . ASN A 96  ? 0.78659 0.85915 0.81113 0.40289  0.15748  0.12058  373 ASN B CA  
639  C C   . ASN A 96  ? 0.81697 0.90011 0.83625 0.37818  0.15488  0.11003  373 ASN B C   
640  O O   . ASN A 96  ? 0.87378 0.92977 0.85951 0.35873  0.14720  0.09968  373 ASN B O   
641  C CB  . ASN A 96  ? 0.80197 0.81535 0.78684 0.41241  0.18033  0.11383  373 ASN B CB  
642  C CG  . ASN A 96  ? 0.91518 0.91983 0.89818 0.41999  0.20705  0.10891  373 ASN B CG  
643  O OD1 . ASN A 96  ? 0.93671 0.92041 0.89004 0.40385  0.21290  0.09592  373 ASN B OD1 
644  N ND2 . ASN A 96  ? 0.96608 0.98511 0.97918 0.44477  0.22339  0.11953  373 ASN B ND2 
645  N N   . PRO A 97  ? 0.83499 0.95651 0.88850 0.37879  0.16185  0.11285  374 PRO B N   
646  C CA  . PRO A 97  ? 0.73751 0.86673 0.78402 0.35656  0.16038  0.10493  374 PRO B CA  
647  C C   . PRO A 97  ? 0.82234 0.90144 0.81659 0.34929  0.17432  0.09249  374 PRO B C   
648  O O   . PRO A 97  ? 0.80752 0.87724 0.77876 0.32903  0.16320  0.08460  374 PRO B O   
649  C CB  . PRO A 97  ? 0.73492 0.90938 0.83077 0.36343  0.17283  0.11160  374 PRO B CB  
650  C CG  . PRO A 97  ? 0.73936 0.94513 0.87882 0.38461  0.16808  0.12323  374 PRO B CG  
651  C CD  . PRO A 97  ? 0.79066 0.95172 0.89514 0.39985  0.17162  0.12404  374 PRO B CD  
652  N N   . THR A 98  ? 0.80525 0.85114 0.77943 0.36584  0.19784  0.09013  375 THR B N   
653  C CA  . THR A 98  ? 0.85390 0.85005 0.77356 0.35896  0.20957  0.07632  375 THR B CA  
654  C C   . THR A 98  ? 0.90744 0.86938 0.79128 0.34402  0.19128  0.06548  375 THR B C   
655  O O   . THR A 98  ? 0.86902 0.80851 0.71801 0.32809  0.18494  0.05363  375 THR B O   
656  C CB  . THR A 98  ? 0.91301 0.87599 0.81580 0.37995  0.23976  0.07482  375 THR B CB  
657  O OG1 . THR A 98  ? 0.91855 0.91681 0.86446 0.39519  0.25901  0.08599  375 THR B OG1 
658  C CG2 . THR A 98  ? 0.86675 0.77922 0.70878 0.37186  0.25070  0.05914  375 THR B CG2 
659  N N   . VAL A 99  ? 0.87198 0.82884 0.76479 0.34976  0.18319  0.06971  376 VAL B N   
660  C CA  . VAL A 99  ? 0.89369 0.82167 0.76178 0.33437  0.16776  0.06046  376 VAL B CA  
661  C C   . VAL A 99  ? 0.85587 0.81040 0.73359 0.31212  0.14481  0.05922  376 VAL B C   
662  O O   . VAL A 99  ? 0.90300 0.83611 0.75625 0.29472  0.13504  0.04715  376 VAL B O   
663  C CB  . VAL A 99  ? 0.80107 0.71790 0.67754 0.34655  0.16704  0.06824  376 VAL B CB  
664  C CG1 . VAL A 99  ? 0.79781 0.69460 0.66015 0.32836  0.15116  0.06140  376 VAL B CG1 
665  C CG2 . VAL A 99  ? 0.83616 0.71137 0.69296 0.36580  0.19137  0.06591  376 VAL B CG2 
666  N N   . ARG A 100 ? 0.76077 0.76259 0.67612 0.31231  0.13563  0.07099  377 ARG B N   
667  C CA  . ARG A 100 ? 0.78361 0.80737 0.70783 0.29152  0.11592  0.06995  377 ARG B CA  
668  C C   . ARG A 100 ? 0.81770 0.84210 0.72788 0.27951  0.11775  0.06311  377 ARG B C   
669  O O   . ARG A 100 ? 0.81054 0.82991 0.70951 0.26186  0.10385  0.05687  377 ARG B O   
670  C CB  . ARG A 100 ? 0.74050 0.81126 0.70550 0.29380  0.10526  0.08230  377 ARG B CB  
671  C CG  . ARG A 100 ? 0.73234 0.79962 0.70335 0.30572  0.09900  0.09010  377 ARG B CG  
672  C CD  . ARG A 100 ? 0.72421 0.83377 0.72630 0.30362  0.08162  0.09932  377 ARG B CD  
673  N NE  . ARG A 100 ? 0.70946 0.82328 0.70696 0.28064  0.06697  0.09453  377 ARG B NE  
674  C CZ  . ARG A 100 ? 0.72206 0.81464 0.70242 0.27288  0.05771  0.09351  377 ARG B CZ  
675  N NH1 . ARG A 100 ? 0.69816 0.76208 0.66189 0.28564  0.06121  0.09730  377 ARG B NH1 
676  N NH2 . ARG A 100 ? 0.69701 0.79442 0.67679 0.25242  0.04744  0.08913  377 ARG B NH2 
677  N N   . ARG A 101 ? 0.70603 0.73440 0.61575 0.29008  0.13616  0.06498  378 ARG B N   
678  C CA  . ARG A 101 ? 0.79067 0.80952 0.67585 0.28156  0.14083  0.05919  378 ARG B CA  
679  C C   . ARG A 101 ? 0.86173 0.83228 0.69627 0.27597  0.13770  0.04452  378 ARG B C   
680  O O   . ARG A 101 ? 0.87014 0.83244 0.68223 0.26336  0.12762  0.03840  378 ARG B O   
681  C CB  . ARG A 101 ? 0.83210 0.85996 0.72493 0.29534  0.16607  0.06477  378 ARG B CB  
682  C CG  . ARG A 101 ? 0.82025 0.90029 0.77062 0.29952  0.16902  0.07742  378 ARG B CG  
683  C CD  . ARG A 101 ? 0.83809 0.94676 0.80597 0.28176  0.15764  0.07991  378 ARG B CD  
684  N NE  . ARG A 101 ? 0.95566 1.09107 0.95312 0.28556  0.17731  0.08664  378 ARG B NE  
685  C CZ  . ARG A 101 ? 0.95941 1.14258 1.01308 0.28438  0.17503  0.09403  378 ARG B CZ  
686  N NH1 . ARG A 101 ? 1.05032 1.25894 1.13101 0.28048  0.15223  0.09617  378 ARG B NH1 
687  N NH2 . ARG A 101 ? 0.94990 1.15439 1.03252 0.28667  0.19637  0.09874  378 ARG B NH2 
688  N N   . TYR A 102 ? 0.86936 0.80728 0.68604 0.28520  0.14528  0.03830  379 TYR B N   
689  C CA  . TYR A 102 ? 0.90257 0.79538 0.67510 0.27716  0.13959  0.02157  379 TYR B CA  
690  C C   . TYR A 102 ? 0.88534 0.78113 0.66463 0.25765  0.11429  0.01589  379 TYR B C   
691  O O   . TYR A 102 ? 0.87902 0.75681 0.63228 0.24532  0.10147  0.00380  379 TYR B O   
692  C CB  . TYR A 102 ? 0.94420 0.80018 0.70041 0.29032  0.15555  0.01584  379 TYR B CB  
693  C CG  . TYR A 102 ? 0.88592 0.69436 0.60147 0.28047  0.14945  -0.00381 379 TYR B CG  
694  C CD1 . TYR A 102 ? 0.87950 0.67807 0.60413 0.26774  0.13445  -0.01049 379 TYR B CD1 
695  C CD2 . TYR A 102 ? 0.96442 0.73591 0.63256 0.28370  0.15983  -0.01659 379 TYR B CD2 
696  C CE1 . TYR A 102 ? 0.93106 0.68851 0.62571 0.25687  0.12850  -0.03035 379 TYR B CE1 
697  C CE2 . TYR A 102 ? 1.01961 0.74810 0.65115 0.27339  0.15162  -0.03709 379 TYR B CE2 
698  C CZ  . TYR A 102 ? 1.00714 0.73070 0.65558 0.25932  0.13538  -0.04441 379 TYR B CZ  
699  O OH  . TYR A 102 ? 1.10180 0.78489 0.72022 0.24709  0.12663  -0.06676 379 TYR B OH  
700  N N   . ALA A 103 ? 0.79983 0.71756 0.61351 0.25535  0.10681  0.02449  380 ALA B N   
701  C CA  . ALA A 103 ? 0.82802 0.75051 0.65251 0.23715  0.08677  0.02084  380 ALA B CA  
702  C C   . ALA A 103 ? 0.80282 0.74587 0.62846 0.22457  0.07391  0.02096  380 ALA B C   
703  O O   . ALA A 103 ? 0.82391 0.75517 0.63905 0.21096  0.05915  0.01100  380 ALA B O   
704  C CB  . ALA A 103 ? 0.78210 0.72546 0.63849 0.23877  0.08370  0.03250  380 ALA B CB  
705  N N   . VAL A 104 ? 0.69421 0.66819 0.53529 0.22930  0.07984  0.03231  381 VAL B N   
706  C CA  . VAL A 104 ? 0.81967 0.81021 0.66102 0.21895  0.07133  0.03430  381 VAL B CA  
707  C C   . VAL A 104 ? 0.84220 0.80362 0.64030 0.21843  0.06996  0.02405  381 VAL B C   
708  O O   . VAL A 104 ? 0.79777 0.75655 0.58680 0.20714  0.05358  0.01945  381 VAL B O   
709  C CB  . VAL A 104 ? 0.75488 0.78042 0.62196 0.22420  0.08233  0.04734  381 VAL B CB  
710  C CG1 . VAL A 104 ? 0.74734 0.78255 0.60931 0.21465  0.07791  0.04972  381 VAL B CG1 
711  C CG2 . VAL A 104 ? 0.70264 0.75734 0.60889 0.22275  0.07721  0.05545  381 VAL B CG2 
712  N N   . ALA A 105 ? 0.84504 0.78311 0.61432 0.23175  0.08702  0.02052  382 ALA B N   
713  C CA  . ALA A 105 ? 0.85969 0.76339 0.57795 0.23248  0.08549  0.00923  382 ALA B CA  
714  C C   . ALA A 105 ? 0.88465 0.76581 0.58788 0.21992  0.06269  -0.00665 382 ALA B C   
715  O O   . ALA A 105 ? 0.90987 0.78073 0.58698 0.21331  0.04664  -0.01362 382 ALA B O   
716  C CB  . ALA A 105 ? 0.92412 0.79978 0.61257 0.24883  0.10993  0.00606  382 ALA B CB  
717  N N   . ARG A 106 ? 0.79073 0.66324 0.51096 0.21696  0.06111  -0.01255 383 ARG B N   
718  C CA  . ARG A 106 ? 0.86470 0.71934 0.58107 0.20265  0.04083  -0.02816 383 ARG B CA  
719  C C   . ARG A 106 ? 0.90516 0.78827 0.65200 0.18837  0.02031  -0.02385 383 ARG B C   
720  O O   . ARG A 106 ? 0.91363 0.78922 0.65180 0.17790  -0.00011 -0.03498 383 ARG B O   
721  C CB  . ARG A 106 ? 0.96029 0.79640 0.69021 0.20243  0.04837  -0.03416 383 ARG B CB  
722  C CG  . ARG A 106 ? 0.97405 0.77588 0.67290 0.21657  0.06934  -0.04017 383 ARG B CG  
723  C CD  . ARG A 106 ? 1.01657 0.78843 0.66310 0.21740  0.06612  -0.05462 383 ARG B CD  
724  N NE  . ARG A 106 ? 1.10258 0.85669 0.73798 0.20064  0.04182  -0.07414 383 ARG B NE  
725  C CZ  . ARG A 106 ? 1.18216 0.91891 0.77620 0.19687  0.02626  -0.08705 383 ARG B CZ  
726  N NH1 . ARG A 106 ? 1.15028 0.88031 0.70409 0.20879  0.03495  -0.08174 383 ARG B NH1 
727  N NH2 . ARG A 106 ? 1.17155 0.89707 0.76481 0.18104  0.00125  -0.10569 383 ARG B NH2 
728  N N   . LEU A 107 ? 0.84013 0.75602 0.62327 0.18809  0.02490  -0.00827 384 LEU B N   
729  C CA  . LEU A 107 ? 0.81731 0.75795 0.62851 0.17542  0.00941  -0.00336 384 LEU B CA  
730  C C   . LEU A 107 ? 0.81991 0.76501 0.61143 0.17406  -0.00151 -0.00248 384 LEU B C   
731  O O   . LEU A 107 ? 0.87445 0.82797 0.67949 0.16358  -0.01941 -0.00455 384 LEU B O   
732  C CB  . LEU A 107 ? 0.80762 0.77915 0.65259 0.17652  0.01813  0.01235  384 LEU B CB  
733  C CG  . LEU A 107 ? 0.83077 0.80495 0.70462 0.16957  0.01656  0.01322  384 LEU B CG  
734  C CD1 . LEU A 107 ? 0.79986 0.80530 0.70065 0.16832  0.01955  0.02726  384 LEU B CD1 
735  C CD2 . LEU A 107 ? 0.84673 0.81066 0.72951 0.15499  0.00094  0.00243  384 LEU B CD2 
736  N N   . ARG A 108 ? 0.84992 0.78889 0.61069 0.18573  0.01086  0.00202  385 ARG B N   
737  C CA  . ARG A 108 ? 0.92579 0.86240 0.65925 0.18714  0.00343  0.00457  385 ARG B CA  
738  C C   . ARG A 108 ? 0.93295 0.84725 0.63901 0.18164  -0.02110 -0.01074 385 ARG B C   
739  O O   . ARG A 108 ? 0.97227 0.88890 0.66379 0.18102  -0.03513 -0.00792 385 ARG B O   
740  C CB  . ARG A 108 ? 0.94573 0.87057 0.64524 0.20175  0.02599  0.01051  385 ARG B CB  
741  C CG  . ARG A 108 ? 1.02927 0.97372 0.73461 0.20407  0.03560  0.02616  385 ARG B CG  
742  C CD  . ARG A 108 ? 0.99349 0.92424 0.66866 0.21827  0.06256  0.03199  385 ARG B CD  
743  N NE  . ARG A 108 ? 1.03958 0.98997 0.75038 0.22344  0.08390  0.03825  385 ARG B NE  
744  C CZ  . ARG A 108 ? 1.17493 1.10852 0.86940 0.23600  0.10453  0.03588  385 ARG B CZ  
745  N NH1 . ARG A 108 ? 1.25938 1.15210 0.89718 0.24387  0.10898  0.02645  385 ARG B NH1 
746  N NH2 . ARG A 108 ? 1.10909 1.06681 0.84438 0.24153  0.12086  0.04301  385 ARG B NH2 
747  N N   . GLN A 109 ? 0.91047 0.80299 0.61018 0.17787  -0.02706 -0.02705 386 GLN B N   
748  C CA  . GLN A 109 ? 0.93614 0.80908 0.61438 0.17083  -0.05276 -0.04485 386 GLN B CA  
749  C C   . GLN A 109 ? 0.87452 0.76943 0.59930 0.15606  -0.07506 -0.04743 386 GLN B C   
750  O O   . GLN A 109 ? 0.95367 0.84318 0.66969 0.15042  -0.10095 -0.05907 386 GLN B O   
751  C CB  . GLN A 109 ? 1.02511 0.86454 0.68244 0.17031  -0.04874 -0.06337 386 GLN B CB  
752  C CG  . GLN A 109 ? 1.04756 0.86323 0.66567 0.18564  -0.02161 -0.06109 386 GLN B CG  
753  C CD  . GLN A 109 ? 1.10806 0.90651 0.66886 0.19655  -0.02051 -0.05918 386 GLN B CD  
754  O OE1 . GLN A 109 ? 1.13244 0.91635 0.66015 0.19324  -0.04447 -0.07001 386 GLN B OE1 
755  N NE2 . GLN A 109 ? 1.18621 0.98594 0.73540 0.21022  0.00754  -0.04500 386 GLN B NE2 
756  N N   . ALA A 110 ? 0.84385 0.76249 0.61738 0.15023  -0.06577 -0.03733 387 ALA B N   
757  C CA  . ALA A 110 ? 0.84396 0.78317 0.66376 0.13721  -0.08131 -0.03734 387 ALA B CA  
758  C C   . ALA A 110 ? 0.81551 0.77317 0.63529 0.13883  -0.09474 -0.02712 387 ALA B C   
759  O O   . ALA A 110 ? 0.81531 0.77957 0.61742 0.14800  -0.08265 -0.01285 387 ALA B O   
760  C CB  . ALA A 110 ? 0.79884 0.75387 0.66032 0.13280  -0.06414 -0.02715 387 ALA B CB  
761  N N   . ASP A 111 ? 0.74446 0.71086 0.58813 0.13016  -0.11848 -0.03384 388 ASP B N   
762  C CA  . ASP A 111 ? 0.77923 0.76490 0.63142 0.13265  -0.12849 -0.02103 388 ASP B CA  
763  C C   . ASP A 111 ? 0.74650 0.75606 0.64759 0.12609  -0.11424 -0.00751 388 ASP B C   
764  O O   . ASP A 111 ? 0.71093 0.72205 0.63847 0.11933  -0.10004 -0.00876 388 ASP B O   
765  C CB  . ASP A 111 ? 0.91648 0.90507 0.77661 0.12871  -0.16127 -0.03173 388 ASP B CB  
766  C CG  . ASP A 111 ? 0.98314 0.98021 0.89803 0.11340  -0.16988 -0.04464 388 ASP B CG  
767  O OD1 . ASP A 111 ? 1.04792 1.03768 0.97800 0.10734  -0.15050 -0.04828 388 ASP B OD1 
768  O OD2 . ASP A 111 ? 1.17310 1.18337 1.11670 0.10822  -0.19503 -0.05071 388 ASP B OD2 
769  N N   . ASP A 112 ? 0.75685 0.78172 0.66615 0.12879  -0.11749 0.00574  389 ASP B N   
770  C CA  . ASP A 112 ? 0.71596 0.75900 0.66061 0.12380  -0.10035 0.01909  389 ASP B CA  
771  C C   . ASP A 112 ? 0.67106 0.72371 0.66834 0.11080  -0.10306 0.01411  389 ASP B C   
772  O O   . ASP A 112 ? 0.67137 0.73001 0.69118 0.10522  -0.08521 0.02010  389 ASP B O   
773  C CB  . ASP A 112 ? 0.68861 0.74064 0.62584 0.13026  -0.09987 0.03433  389 ASP B CB  
774  C CG  . ASP A 112 ? 0.74028 0.78573 0.63926 0.14000  -0.08084 0.04402  389 ASP B CG  
775  O OD1 . ASP A 112 ? 0.70290 0.74142 0.58809 0.14171  -0.06782 0.03980  389 ASP B OD1 
776  O OD2 . ASP A 112 ? 0.80665 0.85319 0.69173 0.14644  -0.07721 0.05630  389 ASP B OD2 
777  N N   . GLU A 113 ? 0.67947 0.73294 0.69720 0.10574  -0.12448 0.00276  390 GLU B N   
778  C CA  . GLU A 113 ? 0.58181 0.64198 0.65295 0.09289  -0.12267 -0.00291 390 GLU B CA  
779  C C   . GLU A 113 ? 0.71323 0.75843 0.78550 0.08722  -0.10448 -0.00963 390 GLU B C   
780  O O   . GLU A 113 ? 0.73617 0.78296 0.83682 0.08033  -0.08756 -0.00503 390 GLU B O   
781  C CB  . GLU A 113 ? 0.55792 0.62363 0.65550 0.08808  -0.15012 -0.01622 390 GLU B CB  
782  N N   . ASP A 114 ? 0.66387 0.69097 0.70168 0.09127  -0.10615 -0.01977 391 ASP B N   
783  C CA  . ASP A 114 ? 0.62516 0.63538 0.66112 0.08872  -0.08753 -0.02408 391 ASP B CA  
784  C C   . ASP A 114 ? 0.66777 0.68194 0.69000 0.09545  -0.06600 -0.00876 391 ASP B C   
785  O O   . ASP A 114 ? 0.58448 0.59469 0.62275 0.09167  -0.05005 -0.00498 391 ASP B O   
786  C CB  . ASP A 114 ? 0.67850 0.66608 0.67997 0.09247  -0.09306 -0.03856 391 ASP B CB  
787  C CG  . ASP A 114 ? 0.80775 0.79012 0.82758 0.08269  -0.11484 -0.05747 391 ASP B CG  
788  O OD1 . ASP A 114 ? 0.77019 0.76756 0.83832 0.07261  -0.12177 -0.05865 391 ASP B OD1 
789  O OD2 . ASP A 114 ? 0.83004 0.79361 0.81803 0.08475  -0.12482 -0.07175 391 ASP B OD2 
790  N N   . LEU A 115 ? 0.62514 0.64626 0.61726 0.10558  -0.06533 -0.00006 392 LEU B N   
791  C CA  . LEU A 115 ? 0.63189 0.66115 0.61611 0.11121  -0.04728 0.01289  392 LEU B CA  
792  C C   . LEU A 115 ? 0.59587 0.63855 0.61276 0.10309  -0.03958 0.02166  392 LEU B C   
793  O O   . LEU A 115 ? 0.62320 0.66407 0.64474 0.10240  -0.02624 0.02566  392 LEU B O   
794  C CB  . LEU A 115 ? 0.59792 0.63391 0.55309 0.12104  -0.04727 0.02042  392 LEU B CB  
795  C CG  . LEU A 115 ? 0.64566 0.69207 0.59315 0.12754  -0.02982 0.03157  392 LEU B CG  
796  C CD1 . LEU A 115 ? 0.73575 0.77254 0.67879 0.13175  -0.01964 0.02807  392 LEU B CD1 
797  C CD2 . LEU A 115 ? 0.74637 0.78976 0.66072 0.13759  -0.02879 0.03486  392 LEU B CD2 
798  N N   . LEU A 116 ? 0.58970 0.64333 0.62777 0.09762  -0.04814 0.02442  393 LEU B N   
799  C CA  . LEU A 116 ? 0.62396 0.68627 0.69164 0.08960  -0.03892 0.03179  393 LEU B CA  
800  C C   . LEU A 116 ? 0.61341 0.66265 0.70031 0.08207  -0.02910 0.02678  393 LEU B C   
801  O O   . LEU A 116 ? 0.51824 0.56661 0.60967 0.07904  -0.01517 0.03327  393 LEU B O   
802  C CB  . LEU A 116 ? 0.49071 0.56362 0.58191 0.08626  -0.04984 0.03433  393 LEU B CB  
803  C CG  . LEU A 116 ? 0.64662 0.72700 0.76523 0.07929  -0.03809 0.04315  393 LEU B CG  
804  C CD1 . LEU A 116 ? 0.59597 0.68268 0.69625 0.08160  -0.02506 0.05329  393 LEU B CD1 
805  C CD2 . LEU A 116 ? 0.69621 0.78617 0.84072 0.07867  -0.04949 0.04588  393 LEU B CD2 
806  N N   . MET A 117 ? 0.55483 0.59098 0.65014 0.07894  -0.03526 0.01487  394 MET B N   
807  C CA  A MET A 117 ? 0.55333 0.57208 0.66601 0.07199  -0.02230 0.01046  394 MET B CA  
808  C CA  B MET A 117 ? 0.54841 0.56715 0.66109 0.07199  -0.02226 0.01048  394 MET B CA  
809  C C   . MET A 117 ? 0.62393 0.62829 0.70849 0.07889  -0.00800 0.01421  394 MET B C   
810  O O   . MET A 117 ? 0.60126 0.58818 0.69227 0.07542  0.00634  0.01472  394 MET B O   
811  C CB  A MET A 117 ? 0.53635 0.54454 0.66867 0.06560  -0.03196 -0.00483 394 MET B CB  
812  C CB  B MET A 117 ? 0.53908 0.54714 0.67150 0.06556  -0.03176 -0.00479 394 MET B CB  
813  C CG  A MET A 117 ? 0.66353 0.68741 0.83662 0.05781  -0.04603 -0.00875 394 MET B CG  
814  C CG  B MET A 117 ? 0.66147 0.68523 0.83424 0.05786  -0.04583 -0.00866 394 MET B CG  
815  S SD  . MET A 117 ? 0.94349 0.97404 1.15454 0.05035  -0.02900 0.00222  394 MET B SD  
816  C CE  . MET A 117 ? 0.68361 0.68393 0.89933 0.04403  -0.00271 -0.00074 394 MET B CE  
817  N N   . TYR A 118 ? 0.57195 0.58192 0.62587 0.08971  -0.01058 0.01751  395 TYR B N   
818  C CA  . TYR A 118 ? 0.56495 0.56603 0.59616 0.09884  0.00103  0.02248  395 TYR B CA  
819  C C   . TYR A 118 ? 0.51505 0.53536 0.53931 0.10294  0.00502  0.03451  395 TYR B C   
820  O O   . TYR A 118 ? 0.53521 0.55335 0.54475 0.11121  0.01193  0.03968  395 TYR B O   
821  C CB  . TYR A 118 ? 0.59009 0.58222 0.59548 0.10934  -0.00155 0.01676  395 TYR B CB  
822  C CG  . TYR A 118 ? 0.60654 0.58078 0.61459 0.10438  -0.00925 0.00178  395 TYR B CG  
823  C CD1 . TYR A 118 ? 0.63876 0.59794 0.67241 0.09324  -0.00637 -0.00592 395 TYR B CD1 
824  C CD2 . TYR A 118 ? 0.64660 0.61809 0.63203 0.10993  -0.01898 -0.00564 395 TYR B CD2 
825  C CE1 . TYR A 118 ? 0.65583 0.60139 0.69790 0.08644  -0.01525 -0.02193 395 TYR B CE1 
826  C CE2 . TYR A 118 ? 0.66482 0.61995 0.65082 0.10405  -0.02923 -0.02169 395 TYR B CE2 
827  C CZ  . TYR A 118 ? 0.69164 0.63565 0.70877 0.09162  -0.02843 -0.03046 395 TYR B CZ  
828  O OH  . TYR A 118 ? 0.79888 0.72868 0.82190 0.08381  -0.04004 -0.04867 395 TYR B OH  
829  N N   . LEU A 119 ? 0.46160 0.50043 0.49772 0.09753  0.00047  0.03876  396 LEU B N   
830  C CA  . LEU A 119 ? 0.47358 0.53230 0.50341 0.10068  0.00313  0.04768  396 LEU B CA  
831  C C   . LEU A 119 ? 0.49381 0.55078 0.52181 0.09974  0.01134  0.05280  396 LEU B C   
832  O O   . LEU A 119 ? 0.51401 0.58356 0.53239 0.10654  0.01235  0.05752  396 LEU B O   
833  C CB  . LEU A 119 ? 0.47722 0.55063 0.52052 0.09414  -0.00043 0.05128  396 LEU B CB  
834  C CG  . LEU A 119 ? 0.47935 0.57242 0.51749 0.09651  0.00350  0.05874  396 LEU B CG  
835  C CD1 . LEU A 119 ? 0.47569 0.57373 0.49523 0.10820  0.00317  0.05877  396 LEU B CD1 
836  C CD2 . LEU A 119 ? 0.50461 0.60661 0.55398 0.09081  0.00292  0.06300  396 LEU B CD2 
837  N N   A LEU A 120 ? 0.53025 0.57147 0.56745 0.09166  0.01719  0.05185  397 LEU B N   
838  N N   B LEU A 120 ? 0.51622 0.55747 0.55343 0.09166  0.01718  0.05185  397 LEU B N   
839  C CA  A LEU A 120 ? 0.52921 0.56284 0.55560 0.09161  0.02456  0.05655  397 LEU B CA  
840  C CA  B LEU A 120 ? 0.52063 0.55446 0.54696 0.09168  0.02450  0.05657  397 LEU B CA  
841  C C   A LEU A 120 ? 0.56383 0.59085 0.56882 0.10485  0.02499  0.05869  397 LEU B C   
842  C C   B LEU A 120 ? 0.56362 0.59102 0.56863 0.10496  0.02485  0.05868  397 LEU B C   
843  O O   A LEU A 120 ? 0.56568 0.60306 0.55926 0.11020  0.02315  0.06403  397 LEU B O   
844  O O   B LEU A 120 ? 0.56542 0.60354 0.55919 0.11038  0.02293  0.06402  397 LEU B O   
845  C CB  A LEU A 120 ? 0.55247 0.56163 0.58742 0.08252  0.03505  0.05484  397 LEU B CB  
846  C CB  B LEU A 120 ? 0.55336 0.56269 0.58801 0.08261  0.03501  0.05492  397 LEU B CB  
847  C CG  A LEU A 120 ? 0.57740 0.56939 0.59409 0.08155  0.04482  0.05934  397 LEU B CG  
848  C CG  B LEU A 120 ? 0.57554 0.57113 0.59226 0.08133  0.04374  0.05972  397 LEU B CG  
849  C CD1 A LEU A 120 ? 0.56017 0.56949 0.57472 0.07586  0.04233  0.06254  397 LEU B CD1 
850  C CD1 B LEU A 120 ? 0.56758 0.53947 0.59611 0.07063  0.05795  0.05827  397 LEU B CD1 
851  C CD2 A LEU A 120 ? 0.56123 0.52331 0.58777 0.07364  0.05984  0.05698  397 LEU B CD2 
852  C CD2 B LEU A 120 ? 0.56658 0.54653 0.55613 0.09377  0.04536  0.06272  397 LEU B CD2 
853  N N   . GLN A 121 ? 0.61854 0.62891 0.61928 0.11064  0.02659  0.05413  398 GLN B N   
854  C CA  . GLN A 121 ? 0.57474 0.57512 0.55568 0.12509  0.02932  0.05703  398 GLN B CA  
855  C C   . GLN A 121 ? 0.63677 0.66300 0.61449 0.13576  0.02292  0.05977  398 GLN B C   
856  O O   . GLN A 121 ? 0.63376 0.66622 0.60163 0.14795  0.02278  0.06595  398 GLN B O   
857  C CB  . GLN A 121 ? 0.58193 0.55272 0.55986 0.12689  0.03588  0.05015  398 GLN B CB  
858  C CG  . GLN A 121 ? 0.54970 0.48979 0.52928 0.11993  0.04792  0.04930  398 GLN B CG  
859  C CD  . GLN A 121 ? 0.63969 0.58129 0.64718 0.10324  0.04795  0.04303  398 GLN B CD  
860  O OE1 . GLN A 121 ? 0.63712 0.59932 0.66118 0.09794  0.03678  0.03806  398 GLN B OE1 
861  N NE2 . GLN A 121 ? 0.65081 0.56909 0.66320 0.09620  0.06147  0.04402  398 GLN B NE2 
862  N N   . LEU A 122 ? 0.55007 0.59058 0.53609 0.13253  0.01824  0.05578  399 LEU B N   
863  C CA  . LEU A 122 ? 0.58974 0.65155 0.57305 0.14240  0.01681  0.05861  399 LEU B CA  
864  C C   . LEU A 122 ? 0.56332 0.65335 0.55652 0.14199  0.01464  0.06571  399 LEU B C   
865  O O   . LEU A 122 ? 0.63699 0.74422 0.63204 0.15297  0.01521  0.06979  399 LEU B O   
866  C CB  . LEU A 122 ? 0.53967 0.60565 0.52330 0.13892  0.01370  0.05377  399 LEU B CB  
867  C CG  . LEU A 122 ? 0.54816 0.58886 0.51926 0.14074  0.01260  0.04421  399 LEU B CG  
868  C CD1 . LEU A 122 ? 0.50676 0.54985 0.47339 0.13676  0.00515  0.03927  399 LEU B CD1 
869  C CD2 . LEU A 122 ? 0.56833 0.59723 0.52279 0.15552  0.01985  0.04358  399 LEU B CD2 
870  N N   . VAL A 123 ? 0.52115 0.61614 0.52321 0.12917  0.01263  0.06644  400 VAL B N   
871  C CA  . VAL A 123 ? 0.56679 0.68602 0.57772 0.12604  0.00964  0.07056  400 VAL B CA  
872  C C   . VAL A 123 ? 0.60276 0.72057 0.60329 0.13551  0.00615  0.07439  400 VAL B C   
873  O O   . VAL A 123 ? 0.55747 0.70129 0.56673 0.14003  0.00048  0.07733  400 VAL B O   
874  C CB  . VAL A 123 ? 0.53153 0.64978 0.55061 0.10972  0.01035  0.06930  400 VAL B CB  
875  C CG1 . VAL A 123 ? 0.46800 0.60144 0.48950 0.10466  0.00674  0.07094  400 VAL B CG1 
876  C CG2 . VAL A 123 ? 0.39727 0.52526 0.42848 0.10371  0.01219  0.06850  400 VAL B CG2 
877  N N   . GLN A 124 ? 0.54837 0.63572 0.53114 0.13880  0.00934  0.07465  401 GLN B N   
878  C CA  . GLN A 124 ? 0.56583 0.64664 0.53197 0.15170  0.00622  0.08024  401 GLN B CA  
879  C C   . GLN A 124 ? 0.66182 0.75337 0.63016 0.16995  0.00557  0.08367  401 GLN B C   
880  O O   . GLN A 124 ? 0.65276 0.75914 0.61990 0.18226  -0.00169 0.08953  401 GLN B O   
881  C CB  . GLN A 124 ? 0.62327 0.66261 0.56731 0.15205  0.01457  0.08083  401 GLN B CB  
882  C CG  . GLN A 124 ? 0.61381 0.63847 0.55427 0.13625  0.01866  0.07860  401 GLN B CG  
883  C CD  . GLN A 124 ? 0.64423 0.68155 0.57419 0.13396  0.00992  0.08133  401 GLN B CD  
884  O OE1 . GLN A 124 ? 0.69189 0.72796 0.60206 0.14654  0.00275  0.08672  401 GLN B OE1 
885  N NE2 . GLN A 124 ? 0.72819 0.77719 0.67079 0.11821  0.00954  0.07722  401 GLN B NE2 
886  N N   . ALA A 125 ? 0.62526 0.70933 0.59671 0.17255  0.01261  0.07979  402 ALA B N   
887  C CA  . ALA A 125 ? 0.65056 0.73887 0.62175 0.19031  0.01603  0.08252  402 ALA B CA  
888  C C   . ALA A 125 ? 0.65585 0.78533 0.64977 0.19540  0.01171  0.08589  402 ALA B C   
889  O O   . ALA A 125 ? 0.63165 0.77031 0.63084 0.21235  0.01436  0.09023  402 ALA B O   
890  C CB  . ALA A 125 ? 0.61069 0.67747 0.57493 0.19006  0.02477  0.07536  402 ALA B CB  
891  N N   . LEU A 126 ? 0.57457 0.72838 0.58514 0.18127  0.00708  0.08404  403 LEU B N   
892  C CA  . LEU A 126 ? 0.55274 0.74616 0.59046 0.18434  0.00472  0.08652  403 LEU B CA  
893  C C   . LEU A 126 ? 0.57858 0.79136 0.62451 0.19644  -0.00639 0.09219  403 LEU B C   
894  O O   . LEU A 126 ? 0.60146 0.84720 0.67487 0.20514  -0.00752 0.09488  403 LEU B O   
895  C CB  . LEU A 126 ? 0.51693 0.72808 0.57014 0.16538  0.00341  0.08305  403 LEU B CB  
896  C CG  . LEU A 126 ? 0.51662 0.71378 0.56402 0.15670  0.01290  0.07943  403 LEU B CG  
897  C CD1 . LEU A 126 ? 0.46182 0.66550 0.51794 0.13818  0.01153  0.07732  403 LEU B CD1 
898  C CD2 . LEU A 126 ? 0.47946 0.68831 0.53555 0.16578  0.02382  0.08065  403 LEU B CD2 
899  N N   . LYS A 127 ? 0.55140 0.74390 0.57430 0.19808  -0.01438 0.09441  404 LYS B N   
900  C CA  . LYS A 127 ? 0.60677 0.81202 0.62911 0.21395  -0.02701 0.10118  404 LYS B CA  
901  C C   . LYS A 127 ? 0.63431 0.84343 0.66496 0.23714  -0.02098 0.10740  404 LYS B C   
902  O O   . LYS A 127 ? 0.63446 0.87122 0.68270 0.25199  -0.03158 0.11332  404 LYS B O   
903  C CB  . LYS A 127 ? 0.55147 0.72074 0.53559 0.21562  -0.03155 0.10417  404 LYS B CB  
904  C CG  . LYS A 127 ? 0.64480 0.80625 0.61658 0.19535  -0.03654 0.09893  404 LYS B CG  
905  C CD  . LYS A 127 ? 0.65666 0.77233 0.58630 0.19894  -0.03330 0.10263  404 LYS B CD  
906  C CE  . LYS A 127 ? 0.78197 0.87464 0.69961 0.17768  -0.02582 0.09639  404 LYS B CE  
907  N NZ  . LYS A 127 ? 0.81219 0.92113 0.72775 0.16493  -0.03829 0.09243  404 LYS B NZ  
908  N N   . TYR A 128 ? 0.64491 0.82600 0.66349 0.24097  -0.00460 0.10566  405 TYR B N   
909  C CA  . TYR A 128 ? 0.64785 0.82168 0.66705 0.26325  0.00490  0.11089  405 TYR B CA  
910  C C   . TYR A 128 ? 0.67463 0.87309 0.72160 0.26621  0.01576  0.10882  405 TYR B C   
911  O O   . TYR A 128 ? 0.71906 0.90934 0.76690 0.28405  0.02766  0.11203  405 TYR B O   
912  C CB  . TYR A 128 ? 0.68070 0.80266 0.66607 0.26587  0.01791  0.10869  405 TYR B CB  
913  C CG  . TYR A 128 ? 0.71866 0.81126 0.67683 0.25966  0.01285  0.10998  405 TYR B CG  
914  C CD1 . TYR A 128 ? 0.66028 0.75871 0.61001 0.27021  0.00010  0.11890  405 TYR B CD1 
915  C CD2 . TYR A 128 ? 0.69928 0.75900 0.64084 0.24308  0.02049  0.10215  405 TYR B CD2 
916  C CE1 . TYR A 128 ? 0.68186 0.74827 0.60085 0.26522  -0.00139 0.12066  405 TYR B CE1 
917  C CE2 . TYR A 128 ? 0.71413 0.74566 0.63363 0.23711  0.02007  0.10360  405 TYR B CE2 
918  C CZ  . TYR A 128 ? 0.74356 0.77601 0.64875 0.24838  0.01069  0.11316  405 TYR B CZ  
919  O OH  . TYR A 128 ? 0.74726 0.74596 0.62401 0.24361  0.01335  0.11532  405 TYR B OH  
920  N N   . GLU A 129 ? 0.63124 0.85548 0.69870 0.24972  0.01475  0.10390  406 GLU B N   
921  C CA  . GLU A 129 ? 0.62897 0.87452 0.72128 0.25190  0.02801  0.10280  406 GLU B CA  
922  C C   . GLU A 129 ? 0.64618 0.94057 0.78382 0.26095  0.02165  0.10810  406 GLU B C   
923  O O   . GLU A 129 ? 0.66481 0.97785 0.81215 0.26439  0.00301  0.11164  406 GLU B O   
924  C CB  . GLU A 129 ? 0.57460 0.81961 0.66506 0.23075  0.03262  0.09608  406 GLU B CB  
925  C CG  . GLU A 129 ? 0.61943 0.82095 0.67193 0.22390  0.03868  0.09011  406 GLU B CG  
926  C CD  . GLU A 129 ? 0.68066 0.86115 0.71790 0.23553  0.05572  0.08800  406 GLU B CD  
927  O OE1 . GLU A 129 ? 0.64599 0.83914 0.69340 0.23547  0.06752  0.08786  406 GLU B OE1 
928  O OE2 . GLU A 129 ? 0.70160 0.84954 0.71443 0.24449  0.05909  0.08608  406 GLU B OE2 
929  N N   . ASN A 130 ? 0.67421 0.98847 0.83953 0.26502  0.03748  0.10826  407 ASN B N   
930  C CA  . ASN A 130 ? 0.62867 0.99331 0.84798 0.27204  0.03504  0.11200  407 ASN B CA  
931  C C   . ASN A 130 ? 0.61857 1.01449 0.86431 0.24936  0.02549  0.10661  407 ASN B C   
932  O O   . ASN A 130 ? 0.70839 1.09740 0.95091 0.23414  0.03904  0.10217  407 ASN B O   
933  C CB  . ASN A 130 ? 0.61078 0.97931 0.84938 0.28485  0.06140  0.11415  407 ASN B CB  
934  C CG  . ASN A 130 ? 0.66737 1.08957 0.97038 0.29445  0.06155  0.11847  407 ASN B CG  
935  O OD1 . ASN A 130 ? 0.64100 1.10190 0.98269 0.27973  0.05262  0.11520  407 ASN B OD1 
936  N ND2 . ASN A 130 ? 0.69501 1.12045 1.01351 0.31921  0.07185  0.12537  407 ASN B ND2 
937  N N   . PHE A 131 ? 0.60478 1.03233 0.87364 0.24749  0.00204  0.10681  408 PHE B N   
938  C CA  . PHE A 131 ? 0.54130 0.99454 0.83181 0.22439  -0.00859 0.09969  408 PHE B CA  
939  C C   . PHE A 131 ? 0.56195 1.05498 0.90886 0.21837  0.00575  0.09739  408 PHE B C   
940  O O   . PHE A 131 ? 0.58757 1.08686 0.94488 0.19689  0.01082  0.09116  408 PHE B O   
941  C CB  . PHE A 131 ? 0.56300 1.03671 0.85803 0.22455  -0.03942 0.09892  408 PHE B CB  
942  C CG  . PHE A 131 ? 0.56839 0.99884 0.80494 0.22509  -0.05077 0.10030  408 PHE B CG  
943  C CD1 . PHE A 131 ? 0.61286 0.99489 0.80604 0.22540  -0.03474 0.10150  408 PHE B CD1 
944  C CD2 . PHE A 131 ? 0.56734 1.00440 0.79220 0.22508  -0.07699 0.09980  408 PHE B CD2 
945  C CE1 . PHE A 131 ? 0.59581 0.93848 0.74183 0.22506  -0.04175 0.10252  408 PHE B CE1 
946  C CE2 . PHE A 131 ? 0.58311 0.97609 0.75260 0.22609  -0.08283 0.10187  408 PHE B CE2 
947  C CZ  . PHE A 131 ? 0.55684 0.90346 0.69027 0.22572  -0.06380 0.10339  408 PHE B CZ  
948  N N   . ASP A 132 ? 0.52567 1.04433 0.91125 0.23727  0.01476  0.10271  409 ASP B N   
949  C CA  . ASP A 132 ? 0.58059 1.13677 1.02526 0.23233  0.03285  0.10094  409 ASP B CA  
950  C C   . ASP A 132 ? 0.59922 1.12400 1.02194 0.22410  0.06506  0.10030  409 ASP B C   
951  O O   . ASP A 132 ? 0.55709 1.09800 1.00857 0.20759  0.07816  0.09634  409 ASP B O   
952  C CB  . ASP A 132 ? 0.58248 1.17041 1.07434 0.25682  0.03814  0.10777  409 ASP B CB  
953  C CG  . ASP A 132 ? 0.68474 1.32066 1.21918 0.26288  0.00519  0.10771  409 ASP B CG  
954  O OD1 . ASP A 132 ? 0.66709 1.32558 1.21579 0.24268  -0.01584 0.09935  409 ASP B OD1 
955  O OD2 . ASP A 132 ? 0.81672 1.46632 1.36880 0.28843  -0.00010 0.11581  409 ASP B OD2 
956  N N   . ASP A 133 ? 0.61801 1.09627 0.98866 0.23577  0.07819  0.10392  410 ASP B N   
957  C CA  . ASP A 133 ? 0.62257 1.06565 0.96060 0.22895  0.10392  0.10297  410 ASP B CA  
958  C C   . ASP A 133 ? 0.60113 1.03426 0.92168 0.20457  0.09728  0.09780  410 ASP B C   
959  O O   . ASP A 133 ? 0.54084 0.97305 0.86956 0.19352  0.11658  0.09709  410 ASP B O   
960  C CB  . ASP A 133 ? 0.61436 1.00730 0.89355 0.24257  0.11062  0.10464  410 ASP B CB  
961  C CG  . ASP A 133 ? 0.72023 1.11539 1.01148 0.26763  0.12074  0.10987  410 ASP B CG  
962  O OD1 . ASP A 133 ? 0.66579 1.09733 1.01074 0.27572  0.13328  0.11320  410 ASP B OD1 
963  O OD2 . ASP A 133 ? 0.84972 1.20945 1.09926 0.27908  0.11765  0.11043  410 ASP B OD2 
964  N N   . ILE A 134 ? 0.57716 0.99907 0.87172 0.19700  0.07262  0.09496  411 ILE B N   
965  C CA  . ILE A 134 ? 0.59809 1.00873 0.87667 0.17503  0.06691  0.09035  411 ILE B CA  
966  C C   . ILE A 134 ? 0.62763 1.07680 0.95707 0.15901  0.06950  0.08658  411 ILE B C   
967  O O   . ILE A 134 ? 0.57084 1.01168 0.90015 0.14519  0.08540  0.08548  411 ILE B O   
968  C CB  . ILE A 134 ? 0.57459 0.96881 0.82246 0.17101  0.04214  0.08803  411 ILE B CB  
969  C CG1 . ILE A 134 ? 0.60096 0.95135 0.79921 0.18234  0.04453  0.09018  411 ILE B CG1 
970  C CG2 . ILE A 134 ? 0.52512 0.91510 0.76774 0.14818  0.03634  0.08291  411 ILE B CG2 
971  C CD1 . ILE A 134 ? 0.53002 0.86331 0.70229 0.18440  0.02497  0.08975  411 ILE B CD1 
972  N N   . LYS A 135 ? 0.52405 1.01566 0.89904 0.16120  0.05423  0.08448  412 LYS B N   
973  C CA  . LYS A 135 ? 0.50001 1.03145 0.93028 0.14449  0.05571  0.07850  412 LYS B CA  
974  C C   . LYS A 135 ? 0.53357 1.07318 0.99583 0.14536  0.08952  0.08143  412 LYS B C   
975  O O   . LYS A 135 ? 0.54875 1.09207 1.02959 0.12734  0.10453  0.07801  412 LYS B O   
976  C CB  . LYS A 135 ? 0.48524 1.06377 0.96087 0.14924  0.02980  0.07515  412 LYS B CB  
977  C CG  . LYS A 135 ? 0.38107 1.00706 0.92424 0.13224  0.02991  0.06688  412 LYS B CG  
978  C CD  . LYS A 135 ? 0.51590 1.19310 1.11000 0.14284  0.00423  0.06486  412 LYS B CD  
979  C CE  . LYS A 135 ? 0.48402 1.21494 1.16099 0.12920  0.00985  0.05680  412 LYS B CE  
980  N NZ  . LYS A 135 ? 0.70713 1.49032 1.44555 0.14809  -0.00428 0.05906  412 LYS B NZ  
981  N N   . ASN A 136 ? 0.52059 1.05936 0.98792 0.16674  0.10480  0.08811  413 ASN B N   
982  C CA  . ASN A 136 ? 0.52536 1.07503 1.02910 0.16965  0.13912  0.09113  413 ASN B CA  
983  C C   . ASN A 136 ? 0.56143 1.06668 1.02110 0.16293  0.16681  0.09407  413 ASN B C   
984  O O   . ASN A 136 ? 0.55930 1.06803 1.04423 0.16119  0.19826  0.09651  413 ASN B O   
985  C CB  . ASN A 136 ? 0.51901 1.07341 1.03436 0.19585  0.15102  0.09773  413 ASN B CB  
986  C CG  . ASN A 136 ? 0.58448 1.19372 1.16440 0.20455  0.13116  0.09676  413 ASN B CG  
987  O OD1 . ASN A 136 ? 0.51021 1.16242 1.14231 0.18921  0.11580  0.08995  413 ASN B OD1 
988  N ND2 . ASN A 136 ? 0.58227 1.19003 1.15965 0.22988  0.13090  0.10326  413 ASN B ND2 
989  N N   . GLY A 137 ? 0.58635 1.04943 0.98151 0.16044  0.15658  0.09447  414 GLY B N   
990  C CA  . GLY A 137 ? 0.56252 0.98576 0.91576 0.15449  0.17738  0.09755  414 GLY B CA  
991  C C   . GLY A 137 ? 0.58847 1.01771 0.95891 0.13182  0.18158  0.09463  414 GLY B C   
992  O O   . GLY A 137 ? 0.65182 1.04717 0.98723 0.12764  0.19859  0.09870  414 GLY B O   
993  N N   . LEU A 138 ? 0.58975 1.05925 1.01108 0.11752  0.16610  0.08748  415 LEU B N   
994  C CA  . LEU A 138 ? 0.57362 1.04870 1.01453 0.09397  0.17012  0.08257  415 LEU B CA  
995  C C   . LEU A 138 ? 0.60210 1.09417 1.09221 0.08782  0.20404  0.08368  415 LEU B C   
996  O O   . LEU A 138 ? 0.56138 1.09039 1.10551 0.09404  0.21052  0.08239  415 LEU B O   
997  C CB  . LEU A 138 ? 0.49936 1.00758 0.97024 0.08028  0.13815  0.07212  415 LEU B CB  
998  C CG  . LEU A 138 ? 0.56944 1.05522 0.99045 0.08139  0.10877  0.07055  415 LEU B CG  
999  C CD1 . LEU A 138 ? 0.42587 0.94412 0.87403 0.07107  0.07850  0.06051  415 LEU B CD1 
1000 C CD2 . LEU A 138 ? 0.55203 0.99609 0.92841 0.07074  0.11659  0.07259  415 LEU B CD2 
1001 N N   . GLU A 139 ? 0.65840 1.12253 1.13163 0.07644  0.22737  0.08684  416 GLU B N   
1002 C CA  . GLU A 139 ? 0.76700 1.24265 1.28689 0.06808  0.26331  0.08792  416 GLU B CA  
1003 C C   . GLU A 139 ? 0.82902 1.35393 1.42323 0.04597  0.25237  0.07499  416 GLU B C   
1004 O O   . GLU A 139 ? 0.85128 1.37879 1.43956 0.03040  0.22759  0.06687  416 GLU B O   
1005 C CB  . GLU A 139 ? 0.84616 1.27409 1.32350 0.06280  0.29148  0.09601  416 GLU B CB  
1006 C CG  . GLU A 139 ? 0.81501 1.19960 1.23745 0.08407  0.31790  0.10889  416 GLU B CG  
1007 N N   . PRO A 140 ? 0.82487 1.38954 1.49117 0.04379  0.27011  0.07180  417 PRO B N   
1008 C CA  . PRO A 140 ? 0.85416 1.46657 1.59355 0.02079  0.25755  0.05666  417 PRO B CA  
1009 C C   . PRO A 140 ? 0.95275 1.54606 1.68633 -0.00530 0.26415  0.05045  417 PRO B C   
1010 O O   . PRO A 140 ? 1.03443 1.66048 1.81036 -0.02567 0.24268  0.03594  417 PRO B O   
1011 C CB  . PRO A 140 ? 0.96622 1.59279 1.74725 0.02179  0.28043  0.05394  417 PRO B CB  
1012 C CG  . PRO A 140 ? 0.97977 1.55593 1.70531 0.04154  0.31347  0.06856  417 PRO B CG  
1013 C CD  . PRO A 140 ? 0.83228 1.38787 1.50032 0.06057  0.29762  0.07824  417 PRO B CD  
1014 N N   . ASN A 193 ? 1.32049 1.16000 0.90168 0.29406  0.21991  0.03926  470 ASN B N   
1015 C CA  . ASN A 193 ? 1.29895 1.13017 0.88260 0.29030  0.19990  0.02670  470 ASN B CA  
1016 C C   . ASN A 193 ? 1.26818 1.14634 0.92480 0.28606  0.19250  0.03401  470 ASN B C   
1017 O O   . ASN A 193 ? 1.26881 1.16798 0.94890 0.27232  0.16576  0.03337  470 ASN B O   
1018 C CB  . ASN A 193 ? 1.40621 1.19365 0.94980 0.30405  0.22078  0.01651  470 ASN B CB  
1019 C CG  . ASN A 193 ? 1.46617 1.23213 0.99773 0.29811  0.19988  0.00033  470 ASN B CG  
1020 O OD1 . ASN A 193 ? 1.57751 1.35988 1.12831 0.28346  0.16963  -0.00363 470 ASN B OD1 
1021 N ND2 . ASN A 193 ? 1.45282 1.17951 0.95319 0.30916  0.21858  -0.00940 470 ASN B ND2 
1022 N N   . LEU A 194 ? 1.21214 1.10605 0.90417 0.29877  0.21592  0.04118  471 LEU B N   
1023 C CA  . LEU A 194 ? 1.15418 1.09075 0.91016 0.29759  0.20754  0.04859  471 LEU B CA  
1024 C C   . LEU A 194 ? 1.03929 1.02573 0.84983 0.29438  0.21282  0.06246  471 LEU B C   
1025 O O   . LEU A 194 ? 1.04362 1.06718 0.90824 0.29799  0.21198  0.06973  471 LEU B O   
1026 C CB  . LEU A 194 ? 1.03772 0.96316 0.80293 0.31473  0.22556  0.04806  471 LEU B CB  
1027 C CG  . LEU A 194 ? 1.17156 1.04519 0.88391 0.31463  0.21939  0.03212  471 LEU B CG  
1028 C CD1 . LEU A 194 ? 1.35342 1.19306 1.04312 0.33381  0.25043  0.02908  471 LEU B CD1 
1029 C CD2 . LEU A 194 ? 1.13367 1.01379 0.86677 0.30651  0.19562  0.02865  471 LEU B CD2 
1030 N N   . GLU A 195 ? 1.06436 1.05157 0.86129 0.28729  0.21678  0.06590  472 GLU B N   
1031 C CA  . GLU A 195 ? 1.04739 1.07547 0.89338 0.28414  0.22877  0.07760  472 GLU B CA  
1032 C C   . GLU A 195 ? 1.01673 1.07979 0.89756 0.26642  0.20291  0.08065  472 GLU B C   
1033 O O   . GLU A 195 ? 1.09084 1.17856 0.99944 0.25948  0.21071  0.08791  472 GLU B O   
1034 C CB  . GLU A 195 ? 1.07808 1.08287 0.88945 0.28750  0.25420  0.08119  472 GLU B CB  
1035 N N   . GLN A 196 ? 0.90433 0.96764 0.78472 0.25863  0.17534  0.07506  473 GLN B N   
1036 C CA  . GLN A 196 ? 0.91126 1.00068 0.81773 0.24200  0.15322  0.07719  473 GLN B CA  
1037 C C   . GLN A 196 ? 0.80661 0.91255 0.74060 0.24012  0.13488  0.07570  473 GLN B C   
1038 O O   . GLN A 196 ? 0.86133 0.94122 0.77066 0.24286  0.12585  0.06857  473 GLN B O   
1039 C CB  . GLN A 196 ? 0.92350 0.98663 0.78839 0.23170  0.13746  0.07206  473 GLN B CB  
1040 C CG  . GLN A 196 ? 0.89973 0.97343 0.76901 0.22283  0.14135  0.07913  473 GLN B CG  
1041 C CD  . GLN A 196 ? 0.88981 0.94092 0.72281 0.21462  0.12225  0.07555  473 GLN B CD  
1042 O OE1 . GLN A 196 ? 0.90093 0.93578 0.71598 0.21198  0.10227  0.06662  473 GLN B OE1 
1043 N NE2 . GLN A 196 ? 0.76849 0.81915 0.59420 0.21089  0.12892  0.08282  473 GLN B NE2 
1044 N N   . ASP A 197 ? 0.68859 0.83483 0.67079 0.23484  0.12936  0.08182  474 ASP B N   
1045 C CA  . ASP A 197 ? 0.74246 0.90116 0.74330 0.23211  0.11006  0.08141  474 ASP B CA  
1046 C C   . ASP A 197 ? 0.67042 0.82172 0.65996 0.21484  0.09046  0.07770  474 ASP B C   
1047 O O   . ASP A 197 ? 0.64802 0.78878 0.62000 0.20592  0.09009  0.07618  474 ASP B O   
1048 C CB  . ASP A 197 ? 0.63945 0.84295 0.69244 0.23460  0.10929  0.08829  474 ASP B CB  
1049 C CG  . ASP A 197 ? 0.70092 0.93374 0.78225 0.21909  0.10787  0.09064  474 ASP B CG  
1050 O OD1 . ASP A 197 ? 0.68885 0.90611 0.74861 0.20748  0.10808  0.08879  474 ASP B OD1 
1051 O OD2 . ASP A 197 ? 0.70375 0.97524 0.83028 0.21874  0.10632  0.09410  474 ASP B OD2 
1052 N N   . LEU A 198 ? 0.64272 0.79932 0.64325 0.21118  0.07516  0.07735  475 LEU B N   
1053 C CA  . LEU A 198 ? 0.65534 0.80034 0.64581 0.19626  0.05975  0.07341  475 LEU B CA  
1054 C C   . LEU A 198 ? 0.61994 0.78551 0.62759 0.18173  0.05681  0.07623  475 LEU B C   
1055 O O   . LEU A 198 ? 0.62960 0.78148 0.62308 0.17176  0.05158  0.07365  475 LEU B O   
1056 C CB  . LEU A 198 ? 0.59591 0.73895 0.59252 0.19677  0.04893  0.07371  475 LEU B CB  
1057 C CG  . LEU A 198 ? 0.61395 0.74280 0.60337 0.18195  0.03697  0.06978  475 LEU B CG  
1058 C CD1 . LEU A 198 ? 0.55766 0.65580 0.52147 0.17859  0.03592  0.06159  475 LEU B CD1 
1059 C CD2 . LEU A 198 ? 0.63219 0.75431 0.62299 0.18469  0.03096  0.07152  475 LEU B CD2 
1060 N N   . CYS A 199 ? 0.57615 0.77471 0.61658 0.18048  0.05978  0.08110  476 CYS B N   
1061 C CA  . CYS A 199 ? 0.56756 0.78443 0.62668 0.16564  0.05921  0.08281  476 CYS B CA  
1062 C C   . CYS A 199 ? 0.62165 0.82780 0.66677 0.16390  0.07269  0.08444  476 CYS B C   
1063 O O   . CYS A 199 ? 0.59962 0.79705 0.63656 0.15304  0.06932  0.08460  476 CYS B O   
1064 C CB  . CYS A 199 ? 0.63634 0.89160 0.73606 0.16496  0.05969  0.08551  476 CYS B CB  
1065 S SG  . CYS A 199 ? 0.63094 0.90945 0.75884 0.14584  0.06276  0.08572  476 CYS B SG  
1066 N N   . THR A 200 ? 0.60138 0.80613 0.64243 0.17586  0.08960  0.08662  477 THR B N   
1067 C CA  . THR A 200 ? 0.56413 0.75198 0.58264 0.17717  0.10495  0.08921  477 THR B CA  
1068 C C   . THR A 200 ? 0.63976 0.79261 0.61387 0.17660  0.09425  0.08538  477 THR B C   
1069 O O   . THR A 200 ? 0.57804 0.71973 0.53625 0.17143  0.09554  0.08818  477 THR B O   
1070 C CB  . THR A 200 ? 0.65626 0.84163 0.67188 0.19228  0.12664  0.09135  477 THR B CB  
1071 O OG1 . THR A 200 ? 0.64067 0.86452 0.70739 0.19259  0.13505  0.09463  477 THR B OG1 
1072 C CG2 . THR A 200 ? 0.52448 0.68615 0.50855 0.19527  0.14544  0.09489  477 THR B CG2 
1073 N N   . PHE A 201 ? 0.66724 0.80271 0.62314 0.18195  0.08299  0.07887  478 PHE B N   
1074 C CA  . PHE A 201 ? 0.66207 0.76757 0.58241 0.18013  0.06985  0.07270  478 PHE B CA  
1075 C C   . PHE A 201 ? 0.60018 0.71131 0.53258 0.16589  0.05504  0.07342  478 PHE B C   
1076 O O   . PHE A 201 ? 0.64165 0.73944 0.55451 0.16353  0.05033  0.07422  478 PHE B O   
1077 C CB  . PHE A 201 ? 0.67341 0.76080 0.58060 0.18582  0.06213  0.06424  478 PHE B CB  
1078 C CG  . PHE A 201 ? 0.70526 0.76780 0.58845 0.18008  0.04497  0.05550  478 PHE B CG  
1079 C CD1 . PHE A 201 ? 0.63029 0.66945 0.47521 0.18363  0.04265  0.05170  478 PHE B CD1 
1080 C CD2 . PHE A 201 ? 0.60506 0.66757 0.50463 0.17117  0.03114  0.05105  478 PHE B CD2 
1081 C CE1 . PHE A 201 ? 0.76090 0.78205 0.58943 0.17794  0.02322  0.04258  478 PHE B CE1 
1082 C CE2 . PHE A 201 ? 0.69808 0.74164 0.58476 0.16483  0.01578  0.04218  478 PHE B CE2 
1083 C CZ  . PHE A 201 ? 0.67282 0.69817 0.52638 0.16799  0.00999  0.03746  478 PHE B CZ  
1084 N N   . LEU A 202 ? 0.56543 0.69430 0.52795 0.15758  0.04797  0.07358  479 LEU B N   
1085 C CA  . LEU A 202 ? 0.56174 0.69299 0.53656 0.14435  0.03690  0.07376  479 LEU B CA  
1086 C C   . LEU A 202 ? 0.57432 0.71513 0.55712 0.13806  0.04437  0.08075  479 LEU B C   
1087 O O   . LEU A 202 ? 0.56465 0.69595 0.54160 0.13282  0.03783  0.08197  479 LEU B O   
1088 C CB  . LEU A 202 ? 0.52840 0.67291 0.52769 0.13786  0.03173  0.07296  479 LEU B CB  
1089 C CG  . LEU A 202 ? 0.53360 0.66451 0.52544 0.14345  0.02591  0.06768  479 LEU B CG  
1090 C CD1 . LEU A 202 ? 0.41828 0.55933 0.42768 0.13890  0.02213  0.06907  479 LEU B CD1 
1091 C CD2 . LEU A 202 ? 0.53555 0.64106 0.51111 0.14072  0.01673  0.06068  479 LEU B CD2 
1092 N N   . ILE A 203 ? 0.57808 0.73830 0.57844 0.13830  0.05871  0.08551  480 ILE B N   
1093 C CA  . ILE A 203 ? 0.52170 0.68726 0.52976 0.13197  0.06995  0.09200  480 ILE B CA  
1094 C C   . ILE A 203 ? 0.61139 0.75197 0.58290 0.14047  0.07499  0.09589  480 ILE B C   
1095 O O   . ILE A 203 ? 0.60477 0.73654 0.56970 0.13655  0.07503  0.10102  480 ILE B O   
1096 C CB  . ILE A 203 ? 0.55300 0.74447 0.59101 0.13021  0.08595  0.09465  480 ILE B CB  
1097 C CG1 . ILE A 203 ? 0.47644 0.69239 0.54760 0.12015  0.07628  0.09068  480 ILE B CG1 
1098 C CG2 . ILE A 203 ? 0.47709 0.66687 0.51803 0.12572  0.10439  0.10170  480 ILE B CG2 
1099 C CD1 . ILE A 203 ? 0.51188 0.75917 0.61889 0.11881  0.08633  0.09091  480 ILE B CD1 
1100 N N   . SER A 204 ? 0.58559 0.71144 0.52925 0.15330  0.07875  0.09356  481 SER B N   
1101 C CA  . SER A 204 ? 0.56804 0.66580 0.46771 0.16271  0.08208  0.09638  481 SER B CA  
1102 C C   . SER A 204 ? 0.65256 0.73413 0.53340 0.16070  0.05900  0.09305  481 SER B C   
1103 O O   . SER A 204 ? 0.65016 0.71720 0.50871 0.16351  0.05743  0.09902  481 SER B O   
1104 C CB  . SER A 204 ? 0.57772 0.65946 0.44826 0.17640  0.09107  0.09242  481 SER B CB  
1105 O OG  . SER A 204 ? 0.87759 0.92679 0.69724 0.18451  0.08248  0.08982  481 SER B OG  
1106 N N   . ARG A 205 ? 0.63289 0.71640 0.52406 0.15657  0.04140  0.08397  482 ARG B N   
1107 C CA  . ARG A 205 ? 0.60959 0.68192 0.49329 0.15342  0.01962  0.07953  482 ARG B CA  
1108 C C   . ARG A 205 ? 0.62498 0.70981 0.53729 0.14326  0.01678  0.08616  482 ARG B C   
1109 O O   . ARG A 205 ? 0.61809 0.69380 0.52058 0.14468  0.00577  0.08910  482 ARG B O   
1110 C CB  . ARG A 205 ? 0.61790 0.68692 0.50884 0.15074  0.00643  0.06768  482 ARG B CB  
1111 C CG  . ARG A 205 ? 0.69112 0.73901 0.54607 0.16141  0.00692  0.05943  482 ARG B CG  
1112 C CD  . ARG A 205 ? 0.71652 0.74037 0.52884 0.16789  -0.00633 0.05575  482 ARG B CD  
1113 N NE  . ARG A 205 ? 0.81881 0.83610 0.63668 0.16172  -0.03036 0.04406  482 ARG B NE  
1114 C CZ  . ARG A 205 ? 0.79669 0.79512 0.59487 0.16344  -0.03934 0.03010  482 ARG B CZ  
1115 N NH1 . ARG A 205 ? 0.84711 0.82648 0.60965 0.17327  -0.02718 0.02624  482 ARG B NH1 
1116 N NH2 . ARG A 205 ? 0.73903 0.73651 0.55606 0.15456  -0.05901 0.01915  482 ARG B NH2 
1117 N N   . ALA A 206 ? 0.54332 0.64799 0.48965 0.13386  0.02665  0.08867  483 ALA B N   
1118 C CA  . ALA A 206 ? 0.58499 0.69803 0.55655 0.12356  0.02785  0.09414  483 ALA B CA  
1119 C C   . ALA A 206 ? 0.60728 0.71314 0.56629 0.12711  0.03861  0.10495  483 ALA B C   
1120 O O   . ALA A 206 ? 0.58864 0.69135 0.55673 0.12353  0.03500  0.11003  483 ALA B O   
1121 C CB  . ALA A 206 ? 0.46629 0.59897 0.46899 0.11307  0.03681  0.09311  483 ALA B CB  
1122 N N   . CYS A 207 ? 0.54861 0.64951 0.48699 0.13509  0.05411  0.10929  484 CYS B N   
1123 C CA  . CYS A 207 ? 0.63169 0.72125 0.55552 0.13903  0.06976  0.12110  484 CYS B CA  
1124 C C   . CYS A 207 ? 0.68125 0.74637 0.56595 0.15101  0.05553  0.12528  484 CYS B C   
1125 O O   . CYS A 207 ? 0.66340 0.71528 0.53364 0.15576  0.06499  0.13685  484 CYS B O   
1126 C CB  . CYS A 207 ? 0.60283 0.69199 0.51744 0.14415  0.09407  0.12459  484 CYS B CB  
1127 S SG  . CYS A 207 ? 0.74702 0.86997 0.71468 0.13003  0.10954  0.12094  484 CYS B SG  
1128 N N   . LYS A 208 ? 0.66676 0.72536 0.53512 0.15580  0.03317  0.11600  485 LYS B N   
1129 C CA  . LYS A 208 ? 0.69394 0.73219 0.52615 0.16685  0.01400  0.11734  485 LYS B CA  
1130 C C   . LYS A 208 ? 0.68163 0.72850 0.54116 0.16129  -0.00990 0.11418  485 LYS B C   
1131 O O   . LYS A 208 ? 0.75065 0.78579 0.58815 0.17008  -0.03036 0.11473  485 LYS B O   
1132 C CB  . LYS A 208 ? 0.77699 0.79874 0.56892 0.17603  0.00446  0.10710  485 LYS B CB  
1133 C CG  . LYS A 208 ? 0.78569 0.79160 0.54150 0.18562  0.02886  0.11095  485 LYS B CG  
1134 C CD  . LYS A 208 ? 0.92847 0.92101 0.65572 0.19129  0.02162  0.09761  485 LYS B CD  
1135 C CE  . LYS A 208 ? 1.09577 1.07515 0.79656 0.20019  0.05032  0.10029  485 LYS B CE  
1136 N NZ  . LYS A 208 ? 1.12530 1.13307 0.87607 0.19200  0.07235  0.10284  485 LYS B NZ  
1137 N N   . ASN A 209 ? 0.55676 0.62306 0.46180 0.14763  -0.00915 0.10889  486 ASN B N   
1138 C CA  . ASN A 209 ? 0.58891 0.66314 0.52597 0.14134  -0.02789 0.10476  486 ASN B CA  
1139 C C   . ASN A 209 ? 0.60528 0.69327 0.58376 0.12853  -0.01311 0.10875  486 ASN B C   
1140 O O   . ASN A 209 ? 0.57355 0.67073 0.56631 0.11990  -0.00264 0.10345  486 ASN B O   
1141 C CB  . ASN A 209 ? 0.59694 0.67241 0.53974 0.13796  -0.04469 0.08943  486 ASN B CB  
1142 C CG  . ASN A 209 ? 0.64286 0.72665 0.62428 0.13057  -0.06063 0.08437  486 ASN B CG  
1143 O OD1 . ASN A 209 ? 0.81585 0.90512 0.82007 0.12930  -0.06062 0.09266  486 ASN B OD1 
1144 N ND2 . ASN A 209 ? 0.65857 0.74190 0.64976 0.12584  -0.07202 0.07080  486 ASN B ND2 
1145 N N   . SER A 210 ? 0.57117 0.65886 0.56644 0.12820  -0.01299 0.11756  487 SER B N   
1146 C CA  . SER A 210 ? 0.61845 0.71379 0.64677 0.11596  0.00401  0.12088  487 SER B CA  
1147 C C   . SER A 210 ? 0.54748 0.65120 0.60849 0.10458  -0.00110 0.11089  487 SER B C   
1148 O O   . SER A 210 ? 0.53683 0.64505 0.61529 0.09333  0.01319  0.10937  487 SER B O   
1149 C CB  . SER A 210 ? 0.61534 0.70383 0.65131 0.12001  0.00889  0.13374  487 SER B CB  
1150 O OG  . SER A 210 ? 0.70947 0.79802 0.75493 0.12706  -0.01330 0.13356  487 SER B OG  
1151 N N   . THR A 211 ? 0.52666 0.63059 0.59500 0.10691  -0.02053 0.10345  488 THR B N   
1152 C CA  . THR A 211 ? 0.43044 0.53803 0.52791 0.09643  -0.02148 0.09414  488 THR B CA  
1153 C C   . THR A 211 ? 0.51608 0.62418 0.60080 0.09212  -0.01433 0.08672  488 THR B C   
1154 O O   . THR A 211 ? 0.54754 0.65671 0.64644 0.08275  -0.00309 0.08459  488 THR B O   
1155 C CB  . THR A 211 ? 0.53366 0.64181 0.64663 0.09905  -0.04296 0.08689  488 THR B CB  
1156 O OG1 . THR A 211 ? 0.59991 0.71107 0.73028 0.10468  -0.05147 0.09500  488 THR B OG1 
1157 C CG2 . THR A 211 ? 0.37653 0.48461 0.52065 0.08784  -0.03893 0.07783  488 THR B CG2 
1158 N N   . LEU A 212 ? 0.56560 0.67107 0.62081 0.10023  -0.02027 0.08331  489 LEU B N   
1159 C CA  . LEU A 212 ? 0.50077 0.60794 0.54410 0.09945  -0.01221 0.07874  489 LEU B CA  
1160 C C   . LEU A 212 ? 0.46225 0.57881 0.51081 0.09417  0.00501  0.08473  489 LEU B C   
1161 O O   . LEU A 212 ? 0.47572 0.59702 0.53218 0.08840  0.01068  0.08129  489 LEU B O   
1162 C CB  . LEU A 212 ? 0.53490 0.63569 0.54464 0.11066  -0.01724 0.07602  489 LEU B CB  
1163 C CG  . LEU A 212 ? 0.68026 0.77118 0.68199 0.11289  -0.02945 0.06426  489 LEU B CG  
1164 C CD1 . LEU A 212 ? 0.69020 0.76911 0.65239 0.12467  -0.03527 0.06132  489 LEU B CD1 
1165 C CD2 . LEU A 212 ? 0.60242 0.69499 0.61227 0.10911  -0.02017 0.06031  489 LEU B CD2 
1166 N N   . ALA A 213 ? 0.53507 0.65327 0.57818 0.09625  0.01321  0.09340  490 ALA B N   
1167 C CA  . ALA A 213 ? 0.47480 0.60257 0.52723 0.08900  0.02979  0.09706  490 ALA B CA  
1168 C C   . ALA A 213 ? 0.46807 0.59739 0.54462 0.07607  0.03408  0.09480  490 ALA B C   
1169 O O   . ALA A 213 ? 0.46159 0.59941 0.54458 0.06860  0.04083  0.09163  490 ALA B O   
1170 C CB  . ALA A 213 ? 0.40608 0.53023 0.45018 0.09257  0.04091  0.10703  490 ALA B CB  
1171 N N   . ASN A 214 ? 0.41710 0.53777 0.50695 0.07381  0.03000  0.09600  491 ASN B N   
1172 C CA  . ASN A 214 ? 0.44147 0.55820 0.55105 0.06206  0.03798  0.09412  491 ASN B CA  
1173 C C   . ASN A 214 ? 0.46214 0.57831 0.56994 0.05751  0.03590  0.08587  491 ASN B C   
1174 O O   . ASN A 214 ? 0.44474 0.56157 0.55334 0.04878  0.04390  0.08341  491 ASN B O   
1175 C CB  . ASN A 214 ? 0.47435 0.58228 0.60328 0.06242  0.03494  0.09688  491 ASN B CB  
1176 C CG  . ASN A 214 ? 0.60822 0.70715 0.75587 0.05076  0.04715  0.09460  491 ASN B CG  
1177 O OD1 . ASN A 214 ? 0.59081 0.68474 0.74611 0.04504  0.06060  0.09911  491 ASN B OD1 
1178 N ND2 . ASN A 214 ? 0.51979 0.61244 0.67201 0.04726  0.04503  0.08750  491 ASN B ND2 
1179 N N   . TYR A 215 ? 0.45115 0.56367 0.55419 0.06360  0.02497  0.08125  492 TYR B N   
1180 C CA  . TYR A 215 ? 0.46911 0.57548 0.56812 0.06129  0.02473  0.07503  492 TYR B CA  
1181 C C   . TYR A 215 ? 0.45831 0.57507 0.54097 0.06492  0.02465  0.07395  492 TYR B C   
1182 O O   . TYR A 215 ? 0.43479 0.54869 0.51235 0.06176  0.02693  0.07136  492 TYR B O   
1183 C CB  . TYR A 215 ? 0.46687 0.56379 0.56854 0.06588  0.01547  0.06988  492 TYR B CB  
1184 C CG  . TYR A 215 ? 0.48401 0.57253 0.61169 0.06049  0.01645  0.06934  492 TYR B CG  
1185 C CD1 . TYR A 215 ? 0.45394 0.53004 0.59338 0.05178  0.02902  0.06848  492 TYR B CD1 
1186 C CD2 . TYR A 215 ? 0.40962 0.50228 0.55032 0.06487  0.00502  0.06992  492 TYR B CD2 
1187 C CE1 . TYR A 215 ? 0.38449 0.45359 0.55369 0.04725  0.03326  0.06843  492 TYR B CE1 
1188 C CE2 . TYR A 215 ? 0.39531 0.48487 0.56769 0.06089  0.00487  0.06962  492 TYR B CE2 
1189 C CZ  . TYR A 215 ? 0.47785 0.55621 0.66763 0.05188  0.02056  0.06900  492 TYR B CZ  
1190 O OH  . TYR A 215 ? 0.48181 0.55789 0.70914 0.04847  0.02315  0.06902  492 TYR B OH  
1191 N N   . LEU A 216 ? 0.42101 0.54888 0.49499 0.07254  0.02250  0.07635  493 LEU B N   
1192 C CA  . LEU A 216 ? 0.44457 0.58631 0.51168 0.07625  0.02426  0.07597  493 LEU B CA  
1193 C C   . LEU A 216 ? 0.43724 0.58967 0.51480 0.06585  0.03092  0.07634  493 LEU B C   
1194 O O   . LEU A 216 ? 0.49255 0.65208 0.56846 0.06488  0.02840  0.07342  493 LEU B O   
1195 C CB  . LEU A 216 ? 0.41507 0.56431 0.47298 0.08575  0.02572  0.07900  493 LEU B CB  
1196 C CG  . LEU A 216 ? 0.45707 0.62428 0.51662 0.09011  0.03016  0.07920  493 LEU B CG  
1197 C CD1 . LEU A 216 ? 0.39915 0.56346 0.45127 0.09749  0.02350  0.07529  493 LEU B CD1 
1198 C CD2 . LEU A 216 ? 0.40212 0.57392 0.45374 0.09865  0.03815  0.08328  493 LEU B CD2 
1199 N N   . TYR A 217 ? 0.44783 0.59968 0.53519 0.05812  0.03871  0.07953  494 TYR B N   
1200 C CA  . TYR A 217 ? 0.39066 0.55014 0.48807 0.04602  0.04602  0.07780  494 TYR B CA  
1201 C C   . TYR A 217 ? 0.46946 0.61830 0.56219 0.03856  0.04349  0.07237  494 TYR B C   
1202 O O   . TYR A 217 ? 0.43114 0.58972 0.52125 0.03467  0.03990  0.06794  494 TYR B O   
1203 C CB  . TYR A 217 ? 0.43127 0.58452 0.53827 0.03948  0.05751  0.08253  494 TYR B CB  
1204 C CG  . TYR A 217 ? 0.45592 0.61189 0.57299 0.02442  0.06650  0.07848  494 TYR B CG  
1205 C CD1 . TYR A 217 ? 0.43759 0.61262 0.56522 0.01926  0.07146  0.07641  494 TYR B CD1 
1206 C CD2 . TYR A 217 ? 0.47337 0.61177 0.59052 0.01454  0.07102  0.07540  494 TYR B CD2 
1207 C CE1 . TYR A 217 ? 0.46975 0.64728 0.60768 0.00361  0.07785  0.07006  494 TYR B CE1 
1208 C CE2 . TYR A 217 ? 0.43261 0.56963 0.55415 -0.00016 0.07893  0.06956  494 TYR B CE2 
1209 C CZ  . TYR A 217 ? 0.52716 0.68427 0.65896 -0.00620 0.08080  0.06614  494 TYR B CZ  
1210 O OH  . TYR A 217 ? 0.60197 0.75773 0.73917 -0.02273 0.08684  0.05776  494 TYR B OH  
1211 N N   . TRP A 218 ? 0.44902 0.57706 0.54029 0.03725  0.04527  0.07264  495 TRP B N   
1212 C CA  . TRP A 218 ? 0.49704 0.60804 0.58013 0.02984  0.04827  0.06836  495 TRP B CA  
1213 C C   . TRP A 218 ? 0.53227 0.64092 0.59756 0.03700  0.03955  0.06573  495 TRP B C   
1214 O O   . TRP A 218 ? 0.51749 0.62101 0.56814 0.03275  0.03823  0.06218  495 TRP B O   
1215 C CB  . TRP A 218 ? 0.41041 0.49986 0.50275 0.02706  0.05636  0.07003  495 TRP B CB  
1216 C CG  . TRP A 218 ? 0.49251 0.57980 0.59921 0.01924  0.06731  0.07286  495 TRP B CG  
1217 C CD1 . TRP A 218 ? 0.45195 0.54169 0.57497 0.02339  0.06917  0.07927  495 TRP B CD1 
1218 C CD2 . TRP A 218 ? 0.49096 0.57140 0.59470 0.00669  0.07786  0.06947  495 TRP B CD2 
1219 N NE1 . TRP A 218 ? 0.52614 0.60991 0.65769 0.01522  0.08229  0.08152  495 TRP B NE1 
1220 C CE2 . TRP A 218 ? 0.49024 0.56751 0.61097 0.00375  0.08872  0.07465  495 TRP B CE2 
1221 C CE3 . TRP A 218 ? 0.51799 0.59211 0.60372 -0.00208 0.07846  0.06204  495 TRP B CE3 
1222 C CZ2 . TRP A 218 ? 0.43823 0.50498 0.56061 -0.00869 0.10288  0.07212  495 TRP B CZ2 
1223 C CZ3 . TRP A 218 ? 0.45781 0.52271 0.54338 -0.01551 0.08989  0.05790  495 TRP B CZ3 
1224 C CH2 . TRP A 218 ? 0.50434 0.56476 0.60916 -0.01924 0.10342  0.06267  495 TRP B CH2 
1225 N N   . TYR A 219 ? 0.42478 0.53494 0.48815 0.04852  0.03335  0.06735  496 TYR B N   
1226 C CA  . TYR A 219 ? 0.46871 0.57527 0.51528 0.05757  0.02686  0.06629  496 TYR B CA  
1227 C C   . TYR A 219 ? 0.47338 0.60205 0.51566 0.05993  0.01952  0.06565  496 TYR B C   
1228 O O   . TYR A 219 ? 0.48925 0.61235 0.51474 0.06220  0.01451  0.06449  496 TYR B O   
1229 C CB  . TYR A 219 ? 0.46764 0.57271 0.51468 0.06869  0.02296  0.06704  496 TYR B CB  
1230 C CG  . TYR A 219 ? 0.54878 0.63270 0.60272 0.06648  0.02663  0.06542  496 TYR B CG  
1231 C CD1 . TYR A 219 ? 0.50842 0.57454 0.56805 0.05706  0.03558  0.06473  496 TYR B CD1 
1232 C CD2 . TYR A 219 ? 0.52204 0.60334 0.57834 0.07354  0.02154  0.06348  496 TYR B CD2 
1233 C CE1 . TYR A 219 ? 0.53267 0.58292 0.60748 0.05482  0.03970  0.06282  496 TYR B CE1 
1234 C CE2 . TYR A 219 ? 0.46149 0.52710 0.53053 0.07026  0.02262  0.06010  496 TYR B CE2 
1235 C CZ  . TYR A 219 ? 0.52150 0.57358 0.60316 0.06101  0.03185  0.06011  496 TYR B CZ  
1236 O OH  . TYR A 219 ? 0.60177 0.64156 0.70441 0.05746  0.03382  0.05639  496 TYR B OH  
1237 N N   . VAL A 220 ? 0.45552 0.60922 0.51372 0.05984  0.01892  0.06659  497 VAL B N   
1238 C CA  . VAL A 220 ? 0.44888 0.62886 0.51331 0.06234  0.01195  0.06540  497 VAL B CA  
1239 C C   . VAL A 220 ? 0.51657 0.70129 0.58294 0.04826  0.01045  0.06024  497 VAL B C   
1240 O O   . VAL A 220 ? 0.50317 0.70224 0.56693 0.04950  -0.00062 0.05716  497 VAL B O   
1241 C CB  . VAL A 220 ? 0.47877 0.68144 0.56198 0.06673  0.01612  0.06800  497 VAL B CB  
1242 C CG1 . VAL A 220 ? 0.46826 0.70236 0.56981 0.06618  0.01142  0.06589  497 VAL B CG1 
1243 C CG2 . VAL A 220 ? 0.42705 0.62245 0.50107 0.08167  0.01597  0.07120  497 VAL B CG2 
1244 N N   . ILE A 221 ? 0.48089 0.65230 0.55089 0.03535  0.02065  0.05883  498 ILE B N   
1245 C CA  . ILE A 221 ? 0.51059 0.68170 0.58023 0.01980  0.02159  0.05201  498 ILE B CA  
1246 C C   . ILE A 221 ? 0.54173 0.69205 0.58117 0.01999  0.01447  0.04847  498 ILE B C   
1247 O O   . ILE A 221 ? 0.57398 0.73279 0.60630 0.01335  0.00495  0.04167  498 ILE B O   
1248 C CB  . ILE A 221 ? 0.57602 0.73243 0.65508 0.00762  0.03745  0.05233  498 ILE B CB  
1249 C CG1 . ILE A 221 ? 0.66891 0.83306 0.75698 -0.00902 0.04082  0.04452  498 ILE B CG1 
1250 C CG2 . ILE A 221 ? 0.57978 0.70255 0.64354 0.00681  0.04521  0.05385  498 ILE B CG2 
1251 C CD1 . ILE A 221 ? 0.69073 0.89005 0.80402 -0.01028 0.03655  0.04246  498 ILE B CD1 
1252 N N   . VAL A 222 ? 0.52735 0.65032 0.54905 0.02726  0.01899  0.05248  499 VAL B N   
1253 C CA  . VAL A 222 ? 0.54324 0.64012 0.53120 0.02930  0.01621  0.05088  499 VAL B CA  
1254 C C   . VAL A 222 ? 0.59920 0.71110 0.57408 0.04259  -0.00121 0.05212  499 VAL B C   
1255 O O   . VAL A 222 ? 0.59577 0.69920 0.54343 0.04243  -0.01067 0.04889  499 VAL B O   
1256 C CB  . VAL A 222 ? 0.51859 0.58141 0.49681 0.03296  0.02952  0.05498  499 VAL B CB  
1257 C CG1 . VAL A 222 ? 0.54863 0.58037 0.48781 0.03750  0.02983  0.05504  499 VAL B CG1 
1258 C CG2 . VAL A 222 ? 0.52408 0.57320 0.51865 0.02059  0.04605  0.05409  499 VAL B CG2 
1259 N N   . GLU A 223 ? 0.51961 0.65203 0.51110 0.05546  -0.00591 0.05700  500 GLU B N   
1260 C CA  . GLU A 223 ? 0.57940 0.72926 0.56415 0.06956  -0.02181 0.05907  500 GLU B CA  
1261 C C   . GLU A 223 ? 0.54751 0.73201 0.54854 0.06292  -0.03595 0.05305  500 GLU B C   
1262 O O   . GLU A 223 ? 0.59751 0.79439 0.58883 0.07207  -0.05300 0.05305  500 GLU B O   
1263 C CB  . GLU A 223 ? 0.51346 0.67652 0.51398 0.08480  -0.02091 0.06496  500 GLU B CB  
1264 C CG  . GLU A 223 ? 0.61741 0.74767 0.60289 0.09193  -0.01025 0.06893  500 GLU B CG  
1265 C CD  . GLU A 223 ? 0.72321 0.81772 0.67278 0.09587  -0.00885 0.07077  500 GLU B CD  
1266 O OE1 . GLU A 223 ? 0.75292 0.84996 0.68286 0.10522  -0.02089 0.07287  500 GLU B OE1 
1267 O OE2 . GLU A 223 ? 0.81160 0.87468 0.75294 0.09005  0.00480  0.07045  500 GLU B OE2 
1268 N N   . CYS A 224 ? 0.59735 0.79808 0.62514 0.04753  -0.02937 0.04792  501 CYS B N   
1269 C CA  . CYS A 224 ? 0.53553 0.76936 0.58518 0.03785  -0.04088 0.04003  501 CYS B CA  
1270 C C   . CYS A 224 ? 0.62192 0.83980 0.64284 0.02679  -0.05067 0.03131  501 CYS B C   
1271 O O   . CYS A 224 ? 0.67069 0.91239 0.69510 0.02593  -0.07068 0.02495  501 CYS B O   
1272 C CB  . CYS A 224 ? 0.54858 0.79773 0.63289 0.02386  -0.02671 0.03730  501 CYS B CB  
1273 S SG  . CYS A 224 ? 0.56646 0.84092 0.68470 0.03554  -0.01717 0.04531  501 CYS B SG  
1274 N N   . GLU A 225 ? 0.60414 0.78202 0.59747 0.01806  -0.03694 0.03017  502 GLU B N   
1275 C CA  . GLU A 225 ? 0.68598 0.84165 0.64574 0.00659  -0.04249 0.02095  502 GLU B CA  
1276 C C   . GLU A 225 ? 0.64193 0.77196 0.55320 0.02062  -0.05390 0.02446  502 GLU B C   
1277 O O   . GLU A 225 ? 0.77263 0.87833 0.64546 0.01347  -0.05917 0.01727  502 GLU B O   
1278 C CB  . GLU A 225 ? 0.63455 0.75587 0.58637 -0.00904 -0.01920 0.01799  502 GLU B CB  
1279 C CG  . GLU A 225 ? 0.84647 0.92409 0.77081 -0.00230 -0.00218 0.02554  502 GLU B CG  
1280 C CD  . GLU A 225 ? 0.77409 0.81061 0.64310 -0.00219 -0.00320 0.02217  502 GLU B CD  
1281 O OE1 . GLU A 225 ? 0.91552 0.94546 0.76218 -0.01398 -0.01096 0.01129  502 GLU B OE1 
1282 N N   . ASP A 226 ? 0.68912 0.82097 0.59768 0.04076  -0.05715 0.03513  503 ASP B N   
1283 C CA  . ASP A 226 ? 0.73133 0.83116 0.59060 0.05572  -0.06308 0.04079  503 ASP B CA  
1284 C C   . ASP A 226 ? 0.72810 0.84660 0.56899 0.06070  -0.09240 0.03592  503 ASP B C   
1285 O O   . ASP A 226 ? 0.69113 0.85189 0.56137 0.07102  -0.11074 0.03774  503 ASP B O   
1286 C CB  . ASP A 226 ? 0.67642 0.77235 0.54071 0.07537  -0.05711 0.05289  503 ASP B CB  
1287 C CG  . ASP A 226 ? 0.79836 0.84850 0.60983 0.08957  -0.05356 0.06029  503 ASP B CG  
1288 O OD1 . ASP A 226 ? 0.78679 0.82456 0.55738 0.09428  -0.06878 0.05899  503 ASP B OD1 
1289 O OD2 . ASP A 226 ? 0.80940 0.83410 0.61900 0.09608  -0.03536 0.06717  503 ASP B OD2 
1290 N N   . GLN A 227 ? 0.82123 0.90778 0.61330 0.05391  -0.09718 0.02944  504 GLN B N   
1291 C CA  . GLN A 227 ? 0.84994 0.95317 0.62031 0.05747  -0.12907 0.02287  504 GLN B CA  
1292 C C   . GLN A 227 ? 0.85520 0.95206 0.59405 0.08511  -0.14536 0.03514  504 GLN B C   
1293 O O   . GLN A 227 ? 0.90540 1.03624 0.64947 0.09414  -0.17633 0.03307  504 GLN B O   
1294 C CB  . GLN A 227 ? 0.92535 0.99149 0.64612 0.04116  -0.12909 0.01072  504 GLN B CB  
1295 C CG  . GLN A 227 ? 0.86578 0.94239 0.61930 0.01377  -0.11717 -0.00313 504 GLN B CG  
1296 C CD  . GLN A 227 ? 1.08377 1.11381 0.78185 -0.00150 -0.11196 -0.01495 504 GLN B CD  
1297 O OE1 . GLN A 227 ? 1.06127 1.05612 0.75278 -0.01374 -0.08227 -0.01623 504 GLN B OE1 
1298 N NE2 . GLN A 227 ? 1.20464 1.23242 0.86033 0.00045  -0.14111 -0.02354 504 GLN B NE2 
1299 N N   . ASP A 228 ? 0.89295 0.94833 0.60304 0.09929  -0.12525 0.04801  505 ASP B N   
1300 C CA  . ASP A 228 ? 0.91763 0.96657 0.60272 0.12711  -0.13724 0.06134  505 ASP B CA  
1301 C C   . ASP A 228 ? 0.91460 1.01899 0.65870 0.13941  -0.14934 0.06626  505 ASP B C   
1302 O O   . ASP A 228 ? 0.95319 1.08294 0.69662 0.15719  -0.17569 0.07052  505 ASP B O   
1303 C CB  . ASP A 228 ? 0.97737 0.96967 0.62712 0.13750  -0.10843 0.07320  505 ASP B CB  
1304 C CG  . ASP A 228 ? 1.19661 1.12730 0.77317 0.13565  -0.09915 0.07288  505 ASP B CG  
1305 O OD1 . ASP A 228 ? 1.38604 1.30763 0.91399 0.14613  -0.12288 0.07315  505 ASP B OD1 
1306 O OD2 . ASP A 228 ? 1.32074 1.21117 0.88796 0.12457  -0.06787 0.07255  505 ASP B OD2 
1307 N N   . THR A 229 ? 0.81290 0.93466 0.60687 0.13157  -0.12967 0.06632  506 THR B N   
1308 C CA  . THR A 229 ? 0.83190 1.00259 0.68092 0.14165  -0.13621 0.07003  506 THR B CA  
1309 C C   . THR A 229 ? 0.81714 1.04287 0.70296 0.13568  -0.16297 0.06087  506 THR B C   
1310 O O   . THR A 229 ? 0.75762 1.02095 0.67066 0.15252  -0.18059 0.06564  506 THR B O   
1311 C CB  . THR A 229 ? 0.67676 0.85263 0.56553 0.13080  -0.11091 0.06926  506 THR B CB  
1312 O OG1 . THR A 229 ? 0.74796 0.87406 0.60729 0.13077  -0.08745 0.07407  506 THR B OG1 
1313 C CG2 . THR A 229 ? 0.61296 0.82532 0.54557 0.14525  -0.11175 0.07522  506 THR B CG2 
1314 N N   . GLN A 230 ? 0.83478 1.06594 0.72568 0.11132  -0.16502 0.04712  507 GLN B N   
1315 C CA  . GLN A 230 ? 0.77434 1.05802 0.70707 0.10081  -0.18811 0.03545  507 GLN B CA  
1316 C C   . GLN A 230 ? 0.86614 1.16540 0.77742 0.11627  -0.22429 0.03545  507 GLN B C   
1317 O O   . GLN A 230 ? 0.84831 1.20074 0.80696 0.12482  -0.24520 0.03494  507 GLN B O   
1318 C CB  . GLN A 230 ? 0.79254 1.06731 0.72489 0.07113  -0.18062 0.02014  507 GLN B CB  
1319 C CG  . GLN A 230 ? 0.85645 1.17967 0.82966 0.05589  -0.20302 0.00503  507 GLN B CG  
1320 C CD  . GLN A 230 ? 0.93926 1.25152 0.91998 0.02597  -0.18758 -0.00916 507 GLN B CD  
1321 O OE1 . GLN A 230 ? 0.94472 1.21295 0.89813 0.01852  -0.16131 -0.00660 507 GLN B OE1 
1322 N NE2 . GLN A 230 ? 0.95652 1.30902 0.97813 0.00860  -0.20275 -0.02435 507 GLN B NE2 
1323 N N   . GLN A 231 ? 0.89192 1.14454 0.73163 0.12126  -0.23187 0.03656  508 GLN B N   
1324 C CA  . GLN A 231 ? 0.87143 1.13446 0.68153 0.13782  -0.26899 0.03726  508 GLN B CA  
1325 C C   . GLN A 231 ? 0.89346 1.16051 0.70154 0.17163  -0.27468 0.05617  508 GLN B C   
1326 O O   . GLN A 231 ? 0.92880 1.23774 0.75848 0.18791  -0.30606 0.05833  508 GLN B O   
1327 C CB  . GLN A 231 ? 1.00619 1.21164 0.73191 0.13295  -0.27335 0.03258  508 GLN B CB  
1328 C CG  . GLN A 231 ? 1.09730 1.28802 0.82102 0.09970  -0.25955 0.01479  508 GLN B CG  
1329 C CD  . GLN A 231 ? 1.35358 1.48544 0.99122 0.09420  -0.26301 0.00834  508 GLN B CD  
1330 O OE1 . GLN A 231 ? 1.39049 1.49128 0.96526 0.11561  -0.27726 0.01741  508 GLN B OE1 
1331 N NE2 . GLN A 231 ? 1.38438 1.49716 1.01602 0.06633  -0.24803 -0.00687 508 GLN B NE2 
1332 N N   . ARG A 232 ? 0.92202 1.14750 0.70895 0.18258  -0.24454 0.06959  509 ARG B N   
1333 C CA  . ARG A 232 ? 0.89781 1.11184 0.66804 0.21490  -0.24637 0.08769  509 ARG B CA  
1334 C C   . ARG A 232 ? 0.92307 1.17853 0.76047 0.22612  -0.23746 0.09460  509 ARG B C   
1335 O O   . ARG A 232 ? 0.95122 1.21355 0.78889 0.25421  -0.24652 0.10790  509 ARG B O   
1336 C CB  . ARG A 232 ? 0.96594 1.10593 0.67158 0.22116  -0.21788 0.09775  509 ARG B CB  
1337 C CG  . ARG A 232 ? 1.17102 1.26209 0.79836 0.21743  -0.22594 0.09441  509 ARG B CG  
1338 C CD  . ARG A 232 ? 1.27293 1.29240 0.85018 0.21385  -0.18892 0.10012  509 ARG B CD  
1339 N NE  . ARG A 232 ? 1.36910 1.37845 0.96809 0.22769  -0.16478 0.11272  509 ARG B NE  
1340 C CZ  . ARG A 232 ? 1.39882 1.38831 0.97197 0.25638  -0.16596 0.12862  509 ARG B CZ  
1341 N NH1 . ARG A 232 ? 1.41754 1.39166 0.93703 0.27687  -0.18987 0.13630  509 ARG B NH1 
1342 N NH2 . ARG A 232 ? 1.31255 1.29539 0.91194 0.26536  -0.14299 0.13694  509 ARG B NH2 
1343 N N   . ASP A 233 ? 0.82234 1.10266 0.71347 0.20638  -0.21904 0.08656  510 ASP B N   
1344 C CA  . ASP A 233 ? 0.75071 1.06611 0.70082 0.21595  -0.20778 0.09205  510 ASP B CA  
1345 C C   . ASP A 233 ? 0.76662 1.12515 0.77769 0.19156  -0.20222 0.07910  510 ASP B C   
1346 O O   . ASP A 233 ? 0.69834 1.04541 0.72374 0.17871  -0.17513 0.07727  510 ASP B O   
1347 C CB  . ASP A 233 ? 0.79785 1.06932 0.72854 0.22442  -0.17615 0.10198  510 ASP B CB  
1348 C CG  . ASP A 233 ? 0.88670 1.18652 0.86683 0.23783  -0.16463 0.10806  510 ASP B CG  
1349 O OD1 . ASP A 233 ? 0.89751 1.24672 0.92089 0.24974  -0.18199 0.10965  510 ASP B OD1 
1350 O OD2 . ASP A 233 ? 1.03467 1.30707 1.01142 0.23603  -0.13784 0.11043  510 ASP B OD2 
1351 N N   . PRO A 234 ? 0.70831 1.11686 0.75706 0.18499  -0.22795 0.06983  511 PRO B N   
1352 C CA  . PRO A 234 ? 0.68112 1.12791 0.78779 0.16002  -0.22079 0.05681  511 PRO B CA  
1353 C C   . PRO A 234 ? 0.66527 1.13389 0.82417 0.16407  -0.19611 0.06208  511 PRO B C   
1354 O O   . PRO A 234 ? 0.58537 1.05841 0.76988 0.14368  -0.17619 0.05516  511 PRO B O   
1355 C CB  . PRO A 234 ? 0.72033 1.21996 0.86180 0.15810  -0.25663 0.04727  511 PRO B CB  
1356 C CG  . PRO A 234 ? 0.64558 1.12171 0.72715 0.17584  -0.28412 0.05244  511 PRO B CG  
1357 C CD  . PRO A 234 ? 0.74704 1.17810 0.78639 0.20006  -0.26562 0.07047  511 PRO B CD  
1358 N N   . LYS A 235 ? 0.65362 1.13496 0.82807 0.19055  -0.19621 0.07423  512 LYS B N   
1359 C CA  . LYS A 235 ? 0.54211 1.03716 0.75820 0.19516  -0.17010 0.07886  512 LYS B CA  
1360 C C   . LYS A 235 ? 0.62509 1.07222 0.80825 0.18485  -0.14030 0.07986  512 LYS B C   
1361 O O   . LYS A 235 ? 0.61455 1.06915 0.82496 0.17119  -0.12002 0.07580  512 LYS B O   
1362 C CB  . LYS A 235 ? 0.57297 1.07821 0.80026 0.22717  -0.17250 0.09233  512 LYS B CB  
1363 N N   . THR A 236 ? 0.65480 1.05149 0.77914 0.19102  -0.13754 0.08516  513 THR B N   
1364 C CA  . THR A 236 ? 0.64472 0.99876 0.74300 0.18184  -0.11192 0.08551  513 THR B CA  
1365 C C   . THR A 236 ? 0.61998 0.96826 0.71771 0.15357  -0.10616 0.07479  513 THR B C   
1366 O O   . THR A 236 ? 0.56161 0.89854 0.66648 0.14300  -0.08553 0.07328  513 THR B O   
1367 C CB  . THR A 236 ? 0.53461 0.83808 0.57753 0.19536  -0.10905 0.09343  513 THR B CB  
1368 C CG2 . THR A 236 ? 0.62511 0.88592 0.64128 0.17916  -0.08873 0.09003  513 THR B CG2 
1369 N N   . HIS A 237 ? 0.65786 1.01325 0.74654 0.14173  -0.12447 0.06711  514 HIS B N   
1370 C CA  . HIS A 237 ? 0.62247 0.97447 0.71557 0.11483  -0.11775 0.05620  514 HIS B CA  
1371 C C   . HIS A 237 ? 0.60631 0.99717 0.75656 0.10348  -0.10755 0.05141  514 HIS B C   
1372 O O   . HIS A 237 ? 0.53395 0.91204 0.68907 0.08802  -0.08808 0.04857  514 HIS B O   
1373 C CB  . HIS A 237 ? 0.60624 0.95923 0.67832 0.10474  -0.14059 0.04703  514 HIS B CB  
1374 C CG  . HIS A 237 ? 0.65530 1.00468 0.73361 0.07685  -0.13324 0.03456  514 HIS B CG  
1375 N ND1 . HIS A 237 ? 0.55416 0.94408 0.67488 0.06102  -0.14356 0.02279  514 HIS B ND1 
1376 C CD2 . HIS A 237 ? 0.66990 0.97946 0.72088 0.06216  -0.11476 0.03207  514 HIS B CD2 
1377 C CE1 . HIS A 237 ? 0.55102 0.92287 0.66608 0.03778  -0.13091 0.01365  514 HIS B CE1 
1378 N NE2 . HIS A 237 ? 0.60277 0.92658 0.67596 0.03897  -0.11360 0.01967  514 HIS B NE2 
1379 N N   . GLU A 238 ? 0.55667 0.99447 0.75178 0.11187  -0.11941 0.05116  515 GLU B N   
1380 C CA  . GLU A 238 ? 0.51271 0.98734 0.76544 0.10196  -0.10664 0.04710  515 GLU B CA  
1381 C C   . GLU A 238 ? 0.49722 0.95551 0.75211 0.10903  -0.07816 0.05544  515 GLU B C   
1382 O O   . GLU A 238 ? 0.47490 0.93671 0.75137 0.09563  -0.05876 0.05281  515 GLU B O   
1383 C CB  . GLU A 238 ? 0.58536 1.11430 0.88942 0.11212  -0.12517 0.04584  515 GLU B CB  
1384 C CG  . GLU A 238 ? 0.69252 1.26271 1.06375 0.10145  -0.11030 0.04104  515 GLU B CG  
1385 C CD  . GLU A 238 ? 0.81255 1.39117 1.20180 0.07128  -0.10956 0.02666  515 GLU B CD  
1386 O OE1 . GLU A 238 ? 0.89697 1.46816 1.26067 0.06051  -0.13172 0.01760  515 GLU B OE1 
1387 O OE2 . GLU A 238 ? 0.75547 1.34406 1.18081 0.05877  -0.08516 0.02451  515 GLU B OE2 
1388 N N   . MET A 239 ? 0.50023 0.93749 0.72971 0.13022  -0.07498 0.06528  516 MET B N   
1389 C CA  . MET A 239 ? 0.48180 0.89756 0.70417 0.13618  -0.05044 0.07116  516 MET B CA  
1390 C C   . MET A 239 ? 0.47134 0.85406 0.66857 0.11863  -0.03705 0.06811  516 MET B C   
1391 O O   . MET A 239 ? 0.53098 0.91171 0.73970 0.11299  -0.01825 0.06869  516 MET B O   
1392 C CB  . MET A 239 ? 0.50698 0.89849 0.69999 0.15919  -0.05049 0.07985  516 MET B CB  
1393 C CG  . MET A 239 ? 0.50744 0.87207 0.68621 0.16508  -0.02796 0.08369  516 MET B CG  
1394 S SD  . MET A 239 ? 0.53850 0.85202 0.66954 0.15333  -0.02187 0.08169  516 MET B SD  
1395 C CE  . MET A 239 ? 0.54116 0.82850 0.63559 0.16543  -0.03606 0.08538  516 MET B CE  
1396 N N   . TYR A 240 ? 0.49190 0.84715 0.65422 0.11084  -0.04554 0.06550  517 TYR B N   
1397 C CA  . TYR A 240 ? 0.51680 0.84119 0.65958 0.09625  -0.03218 0.06361  517 TYR B CA  
1398 C C   . TYR A 240 ? 0.51343 0.85446 0.68323 0.07618  -0.02485 0.05725  517 TYR B C   
1399 O O   . TYR A 240 ? 0.45799 0.78422 0.62679 0.06903  -0.00821 0.05873  517 TYR B O   
1400 C CB  . TYR A 240 ? 0.53412 0.82340 0.63624 0.09315  -0.03885 0.06263  517 TYR B CB  
1401 C CG  . TYR A 240 ? 0.52610 0.78388 0.59840 0.10865  -0.03534 0.06920  517 TYR B CG  
1402 C CD1 . TYR A 240 ? 0.51618 0.75521 0.58464 0.11041  -0.02080 0.07169  517 TYR B CD1 
1403 C CD2 . TYR A 240 ? 0.50129 0.74614 0.54805 0.12133  -0.04673 0.07249  517 TYR B CD2 
1404 C CE1 . TYR A 240 ? 0.48923 0.69904 0.53401 0.12184  -0.01732 0.07524  517 TYR B CE1 
1405 C CE2 . TYR A 240 ? 0.53429 0.74700 0.55554 0.13407  -0.04018 0.07798  517 TYR B CE2 
1406 C CZ  . TYR A 240 ? 0.50676 0.70306 0.52974 0.13299  -0.02529 0.07832  517 TYR B CZ  
1407 O OH  . TYR A 240 ? 0.62022 0.78477 0.62181 0.14314  -0.01860 0.08142  517 TYR B OH  
1408 N N   . LEU A 241 ? 0.47620 0.84785 0.67152 0.06732  -0.03700 0.05006  518 LEU B N   
1409 C CA  . LEU A 241 ? 0.51655 0.90547 0.74457 0.04840  -0.02628 0.04366  518 LEU B CA  
1410 C C   . LEU A 241 ? 0.54199 0.94368 0.79774 0.05423  -0.00576 0.04958  518 LEU B C   
1411 O O   . LEU A 241 ? 0.48558 0.87248 0.74145 0.04515  0.01358  0.05114  518 LEU B O   
1412 C CB  . LEU A 241 ? 0.42171 0.84630 0.67967 0.03786  -0.04433 0.03300  518 LEU B CB  
1413 C CG  . LEU A 241 ? 0.52921 0.93811 0.75483 0.02863  -0.06390 0.02476  518 LEU B CG  
1414 C CD1 . LEU A 241 ? 0.42872 0.87536 0.68782 0.01532  -0.08245 0.01162  518 LEU B CD1 
1415 C CD2 . LEU A 241 ? 0.46615 0.83367 0.66056 0.01410  -0.04922 0.02291  518 LEU B CD2 
1416 N N   . ASN A 242 ? 0.45286 0.87865 0.72907 0.07110  -0.00837 0.05387  519 ASN B N   
1417 C CA  . ASN A 242 ? 0.41197 0.84543 0.70929 0.07871  0.01366  0.05973  519 ASN B CA  
1418 C C   . ASN A 242 ? 0.46043 0.85346 0.71828 0.08489  0.02900  0.06674  519 ASN B C   
1419 O O   . ASN A 242 ? 0.48637 0.87290 0.74925 0.08239  0.04985  0.06994  519 ASN B O   
1420 C CB  . ASN A 242 ? 0.43280 0.89408 0.75480 0.09829  0.00893  0.06360  519 ASN B CB  
1421 C CG  . ASN A 242 ? 0.37968 0.88884 0.75414 0.09228  -0.00379 0.05678  519 ASN B CG  
1422 O OD1 . ASN A 242 ? 0.43049 0.95294 0.82892 0.07158  -0.00209 0.04849  519 ASN B OD1 
1423 N ND2 . ASN A 242 ? 0.39032 0.92622 0.78507 0.11014  -0.01763 0.05962  519 ASN B ND2 
1424 N N   . VAL A 243 ? 0.47606 0.84085 0.69444 0.09342  0.01911  0.06911  520 VAL B N   
1425 C CA  . VAL A 243 ? 0.47286 0.80167 0.65776 0.09685  0.02989  0.07344  520 VAL B CA  
1426 C C   . VAL A 243 ? 0.49679 0.81225 0.67896 0.08008  0.03934  0.07223  520 VAL B C   
1427 O O   . VAL A 243 ? 0.52637 0.82635 0.69871 0.08166  0.05388  0.07669  520 VAL B O   
1428 C CB  . VAL A 243 ? 0.49726 0.79839 0.64698 0.10472  0.01827  0.07421  520 VAL B CB  
1429 C CG1 . VAL A 243 ? 0.46925 0.73770 0.59309 0.10162  0.02581  0.07572  520 VAL B CG1 
1430 C CG2 . VAL A 243 ? 0.47860 0.78163 0.62372 0.12466  0.01574  0.07767  520 VAL B CG2 
1431 N N   . MET A 244 ? 0.49110 0.80905 0.67813 0.06488  0.03142  0.06647  521 MET B N   
1432 C CA  . MET A 244 ? 0.48258 0.78627 0.66903 0.04929  0.04253  0.06556  521 MET B CA  
1433 C C   . MET A 244 ? 0.51457 0.83555 0.73125 0.04249  0.06046  0.06632  521 MET B C   
1434 O O   . MET A 244 ? 0.50537 0.80818 0.71523 0.03832  0.07638  0.07086  521 MET B O   
1435 C CB  . MET A 244 ? 0.44825 0.74730 0.63068 0.03451  0.03216  0.05797  521 MET B CB  
1436 C CG  . MET A 244 ? 0.56721 0.84924 0.75012 0.01844  0.04527  0.05666  521 MET B CG  
1437 S SD  . MET A 244 ? 0.59220 0.83699 0.74749 0.02500  0.05459  0.06561  521 MET B SD  
1438 C CE  . MET A 244 ? 0.51889 0.74435 0.64692 0.03028  0.03887  0.06336  521 MET B CE  
1439 N N   . ARG A 245 ? 0.43029 0.78565 0.68175 0.04231  0.05879  0.06256  522 ARG B N   
1440 C CA  . ARG A 245 ? 0.44590 0.81902 0.73300 0.03514  0.07947  0.06279  522 ARG B CA  
1441 C C   . ARG A 245 ? 0.48254 0.84001 0.75473 0.05031  0.09906  0.07317  522 ARG B C   
1442 O O   . ARG A 245 ? 0.50902 0.85525 0.78426 0.04500  0.12133  0.07740  522 ARG B O   
1443 C CB  . ARG A 245 ? 0.45027 0.86791 0.78503 0.03229  0.07132  0.05558  522 ARG B CB  
1444 C CG  . ARG A 245 ? 0.51105 0.94388 0.85779 0.01608  0.05026  0.04354  522 ARG B CG  
1445 C CD  . ARG A 245 ? 0.40737 0.88811 0.80252 0.01558  0.03617  0.03610  522 ARG B CD  
1446 N NE  . ARG A 245 ? 0.61065 1.10467 1.01460 -0.00180 0.01493  0.02267  522 ARG B NE  
1447 C CZ  . ARG A 245 ? 0.60196 1.11245 1.00081 0.00404  -0.01487 0.01778  522 ARG B CZ  
1448 N NH1 . ARG A 245 ? 0.56515 1.08015 0.95229 0.02736  -0.02523 0.02634  522 ARG B NH1 
1449 N NH2 . ARG A 245 ? 0.62350 1.14277 1.02545 -0.01287 -0.03390 0.00432  522 ARG B NH2 
1450 N N   . ARG A 246 ? 0.45961 0.81286 0.71273 0.06883  0.09198  0.07698  523 ARG B N   
1451 C CA  . ARG A 246 ? 0.42920 0.76253 0.65950 0.08399  0.10915  0.08520  523 ARG B CA  
1452 C C   . ARG A 246 ? 0.48655 0.78226 0.67695 0.08249  0.11301  0.08995  523 ARG B C   
1453 O O   . ARG A 246 ? 0.57227 0.85166 0.74996 0.08645  0.13275  0.09655  523 ARG B O   
1454 C CB  . ARG A 246 ? 0.53654 0.86845 0.75127 0.10284  0.09958  0.08635  523 ARG B CB  
1455 C CG  . ARG A 246 ? 0.55491 0.92257 0.80989 0.11046  0.10110  0.08506  523 ARG B CG  
1456 C CD  . ARG A 246 ? 0.78086 1.13855 1.01731 0.13192  0.10360  0.08882  523 ARG B CD  
1457 N NE  . ARG A 246 ? 0.49619 0.83235 0.71334 0.14070  0.12863  0.09413  523 ARG B NE  
1458 C CZ  . ARG A 246 ? 0.64475 0.94471 0.81337 0.15196  0.13046  0.09622  523 ARG B CZ  
1459 N NH1 . ARG A 246 ? 0.86730 1.15300 1.01106 0.15734  0.11117  0.09343  523 ARG B NH1 
1460 N NH2 . ARG A 246 ? 0.81562 1.09182 0.95928 0.15769  0.15204  0.10060  523 ARG B NH2 
1461 N N   . PHE A 247 ? 0.53635 0.81817 0.70793 0.07811  0.09538  0.08725  524 PHE B N   
1462 C CA  . PHE A 247 ? 0.41766 0.66859 0.55992 0.07684  0.09680  0.09159  524 PHE B CA  
1463 C C   . PHE A 247 ? 0.49475 0.74135 0.64841 0.06565  0.11507  0.09527  524 PHE B C   
1464 O O   . PHE A 247 ? 0.54440 0.76990 0.67732 0.07194  0.12818  0.10331  524 PHE B O   
1465 C CB  . PHE A 247 ? 0.45757 0.69874 0.59001 0.07111  0.07844  0.08723  524 PHE B CB  
1466 C CG  . PHE A 247 ? 0.51030 0.72246 0.61675 0.07342  0.07589  0.09137  524 PHE B CG  
1467 C CD1 . PHE A 247 ? 0.49886 0.69426 0.58245 0.08451  0.08215  0.09782  524 PHE B CD1 
1468 C CD2 . PHE A 247 ? 0.46195 0.66362 0.56719 0.06519  0.06674  0.08855  524 PHE B CD2 
1469 C CE1 . PHE A 247 ? 0.46955 0.64282 0.53345 0.08738  0.07545  0.10106  524 PHE B CE1 
1470 C CE2 . PHE A 247 ? 0.45608 0.63603 0.54652 0.06783  0.06341  0.09211  524 PHE B CE2 
1471 C CZ  . PHE A 247 ? 0.48415 0.65213 0.55579 0.07899  0.06598  0.09829  524 PHE B CZ  
1472 N N   . SER A 248 ? 0.49466 0.75835 0.67853 0.04923  0.11618  0.08925  525 SER B N   
1473 C CA  . SER A 248 ? 0.53192 0.78923 0.72908 0.03705  0.13612  0.09175  525 SER B CA  
1474 C C   . SER A 248 ? 0.57571 0.83222 0.77708 0.04425  0.16042  0.09905  525 SER B C   
1475 O O   . SER A 248 ? 0.60418 0.83610 0.78888 0.04600  0.17838  0.10792  525 SER B O   
1476 C CB  . SER A 248 ? 0.44765 0.72717 0.68049 0.01719  0.13338  0.08084  525 SER B CB  
1477 O OG  . SER A 248 ? 0.64920 0.91869 0.89528 0.00387  0.15472  0.08222  525 SER B OG  
1478 N N   . GLN A 249 ? 0.54621 0.82759 0.76882 0.05000  0.16266  0.09633  526 GLN B N   
1479 C CA  . GLN A 249 ? 0.53153 0.81188 0.76106 0.05705  0.18980  0.10287  526 GLN B CA  
1480 C C   . GLN A 249 ? 0.60555 0.84890 0.78216 0.07502  0.19735  0.11378  526 GLN B C   
1481 O O   . GLN A 249 ? 0.58975 0.81162 0.75246 0.07802  0.22233  0.12263  526 GLN B O   
1482 C CB  . GLN A 249 ? 0.44675 0.76197 0.71114 0.06219  0.18830  0.09775  526 GLN B CB  
1483 C CG  . GLN A 249 ? 0.70543 1.02137 0.98070 0.07152  0.21813  0.10389  526 GLN B CG  
1484 C CD  . GLN A 249 ? 0.78520 1.14021 1.10312 0.07739  0.21431  0.09856  526 GLN B CD  
1485 O OE1 . GLN A 249 ? 0.77079 1.16450 1.14261 0.06433  0.20687  0.08991  526 GLN B OE1 
1486 N NE2 . GLN A 249 ? 0.65031 0.99496 0.94389 0.09753  0.21770  0.10316  526 GLN B NE2 
1487 N N   . ALA A 250 ? 0.58614 0.81953 0.73091 0.08702  0.17597  0.11288  527 ALA B N   
1488 C CA  . ALA A 250 ? 0.59239 0.79138 0.68526 0.10380  0.17934  0.12074  527 ALA B CA  
1489 C C   . ALA A 250 ? 0.68755 0.85896 0.75590 0.10110  0.18141  0.12822  527 ALA B C   
1490 O O   . ALA A 250 ? 0.67841 0.82099 0.70906 0.11286  0.19419  0.13758  527 ALA B O   
1491 C CB  . ALA A 250 ? 0.55758 0.75253 0.62716 0.11416  0.15542  0.11578  527 ALA B CB  
1492 N N   . LEU A 251 ? 0.59814 0.77619 0.68525 0.08731  0.16999  0.12467  528 LEU B N   
1493 C CA  . LEU A 251 ? 0.56944 0.72240 0.63862 0.08565  0.17176  0.13235  528 LEU B CA  
1494 C C   . LEU A 251 ? 0.69468 0.83620 0.77001 0.08168  0.20296  0.14095  528 LEU B C   
1495 O O   . LEU A 251 ? 0.75462 0.86566 0.79631 0.09157  0.21149  0.15269  528 LEU B O   
1496 C CB  . LEU A 251 ? 0.56022 0.72252 0.65138 0.07140  0.15613  0.12545  528 LEU B CB  
1497 C CG  . LEU A 251 ? 0.60142 0.76446 0.68085 0.07609  0.12874  0.11970  528 LEU B CG  
1498 C CD1 . LEU A 251 ? 0.61420 0.77890 0.71117 0.06263  0.11978  0.11481  528 LEU B CD1 
1499 C CD2 . LEU A 251 ? 0.57201 0.71119 0.61270 0.09224  0.11949  0.12631  528 LEU B CD2 
1500 N N   . LEU A 252 ? 0.63578 0.80047 0.75340 0.06794  0.21904  0.13526  529 LEU B N   
1501 C CA  . LEU A 252 ? 0.63688 0.78984 0.76537 0.06237  0.25253  0.14242  529 LEU B CA  
1502 C C   . LEU A 252 ? 0.69452 0.82836 0.79423 0.07903  0.27499  0.15249  529 LEU B C   
1503 O O   . LEU A 252 ? 0.77480 0.88241 0.86123 0.08116  0.30337  0.16346  529 LEU B O   
1504 C CB  . LEU A 252 ? 0.61311 0.79871 0.80061 0.04127  0.26270  0.13119  529 LEU B CB  
1505 C CG  . LEU A 252 ? 0.70768 0.90429 0.91594 0.02378  0.24437  0.12104  529 LEU B CG  
1506 C CD1 . LEU A 252 ? 0.59253 0.81834 0.85537 0.00172  0.25319  0.10857  529 LEU B CD1 
1507 C CD2 . LEU A 252 ? 0.65744 0.81892 0.83964 0.02408  0.25020  0.13029  529 LEU B CD2 
1508 N N   . LYS A 253 ? 0.66492 0.80757 0.75257 0.09128  0.26598  0.14933  530 LYS B N   
1509 C CA  . LYS A 253 ? 0.72885 0.84723 0.78179 0.10809  0.28925  0.15850  530 LYS B CA  
1510 C C   . LYS A 253 ? 0.81457 0.89206 0.79752 0.12689  0.27843  0.16805  530 LYS B C   
1511 O O   . LYS A 253 ? 0.88120 0.93039 0.82212 0.14243  0.29655  0.17608  530 LYS B O   
1512 C CB  . LYS A 253 ? 0.67693 0.81876 0.74640 0.11438  0.28896  0.15117  530 LYS B CB  
1513 C CG  . LYS A 253 ? 0.79320 0.97722 0.93359 0.09944  0.30168  0.14296  530 LYS B CG  
1514 C CD  . LYS A 253 ? 0.79550 1.00007 0.95063 0.11018  0.30317  0.13839  530 LYS B CD  
1515 N N   . GLY A 254 ? 0.77472 0.84895 0.74551 0.12585  0.24930  0.16663  531 GLY B N   
1516 C CA  . GLY A 254 ? 0.81693 0.85837 0.72713 0.14359  0.23271  0.17354  531 GLY B CA  
1517 C C   . GLY A 254 ? 0.84119 0.84753 0.71949 0.15064  0.24866  0.18930  531 GLY B C   
1518 O O   . GLY A 254 ? 0.84008 0.84415 0.74232 0.14155  0.27845  0.19509  531 GLY B O   
1519 N N   . ASP A 255 ? 0.89997 0.87961 0.72710 0.16650  0.22886  0.19583  532 ASP B N   
1520 C CA  . ASP A 255 ? 0.91879 0.86245 0.70977 0.17732  0.24003  0.21309  532 ASP B CA  
1521 C C   . ASP A 255 ? 0.80425 0.75898 0.63286 0.16546  0.23176  0.21481  532 ASP B C   
1522 O O   . ASP A 255 ? 0.86765 0.85565 0.74554 0.14851  0.21936  0.20186  532 ASP B O   
1523 C CB  . ASP A 255 ? 1.02696 0.93902 0.74810 0.20017  0.21892  0.21916  532 ASP B CB  
1524 C CG  . ASP A 255 ? 1.13508 1.06424 0.85973 0.20072  0.17456  0.20815  532 ASP B CG  
1525 O OD1 . ASP A 255 ? 1.13020 1.09284 0.90858 0.18432  0.16253  0.19717  532 ASP B OD1 
1526 O OD2 . ASP A 255 ? 1.24562 1.15300 0.91829 0.21737  0.15268  0.21014  532 ASP B OD2 
1527 N N   . LYS A 256 ? 0.70216 0.96681 0.76007 0.10167  0.10457  0.29114  533 LYS B N   
1528 C CA  . LYS A 256 ? 0.80989 1.01979 0.85812 0.08697  0.11370  0.28875  533 LYS B CA  
1529 C C   . LYS A 256 ? 0.70650 0.89842 0.75675 0.09444  0.10526  0.27054  533 LYS B C   
1530 O O   . LYS A 256 ? 0.74406 0.90273 0.78953 0.07594  0.10775  0.26329  533 LYS B O   
1531 C CB  . LYS A 256 ? 0.78431 0.96966 0.82166 0.09963  0.12713  0.30308  533 LYS B CB  
1532 C CG  . LYS A 256 ? 0.82690 1.03167 0.86160 0.09668  0.13632  0.32270  533 LYS B CG  
1533 C CD  . LYS A 256 ? 0.85846 1.03885 0.88001 0.11455  0.15054  0.33827  533 LYS B CD  
1534 C CE  . LYS A 256 ? 0.86067 1.06094 0.87905 0.11240  0.16045  0.35887  533 LYS B CE  
1535 N NZ  . LYS A 256 ? 1.07093 1.24586 1.07383 0.13352  0.17569  0.37560  533 LYS B NZ  
1536 N N   . SER A 257 ? 0.69992 0.91342 0.75577 0.11891  0.09608  0.26293  534 SER B N   
1537 C CA  . SER A 257 ? 0.75645 0.95468 0.81391 0.12479  0.08886  0.24572  534 SER B CA  
1538 C C   . SER A 257 ? 0.73173 0.92562 0.79157 0.10678  0.08276  0.23467  534 SER B C   
1539 O O   . SER A 257 ? 0.86323 1.02449 0.91993 0.09556  0.08468  0.22707  534 SER B O   
1540 C CB  . SER A 257 ? 0.70558 0.93128 0.76678 0.14872  0.08026  0.23833  534 SER B CB  
1541 O OG  . SER A 257 ? 0.85899 1.09597 0.91796 0.16662  0.08546  0.24897  534 SER B OG  
1542 N N   . VAL A 258 ? 0.64141 0.86931 0.70522 0.10680  0.07630  0.23479  535 VAL B N   
1543 C CA  . VAL A 258 ? 0.75641 0.98882 0.82121 0.09493  0.07038  0.22584  535 VAL B CA  
1544 C C   . VAL A 258 ? 0.62265 0.84270 0.68581 0.06633  0.07634  0.23017  535 VAL B C   
1545 O O   . VAL A 258 ? 0.74260 0.95242 0.80477 0.05415  0.07337  0.22083  535 VAL B O   
1546 C CB  . VAL A 258 ? 0.67378 0.95000 0.74002 0.10757  0.06409  0.22838  535 VAL B CB  
1547 C CG1 . VAL A 258 ? 0.66642 0.95023 0.73064 0.10453  0.05833  0.21996  535 VAL B CG1 
1548 C CG2 . VAL A 258 ? 0.51739 0.80464 0.58153 0.13393  0.06032  0.22542  535 VAL B CG2 
1549 N N   . ARG A 259 ? 0.63258 0.85257 0.69367 0.05508  0.08515  0.24347  536 ARG B N   
1550 C CA  . ARG A 259 ? 0.65349 0.86116 0.70992 0.02289  0.09229  0.24705  536 ARG B CA  
1551 C C   . ARG A 259 ? 0.67875 0.82949 0.72512 0.01240  0.09879  0.23952  536 ARG B C   
1552 O O   . ARG A 259 ? 0.75269 0.89072 0.79473 -0.01186 0.09967  0.23289  536 ARG B O   
1553 C CB  . ARG A 259 ? 0.65944 0.88068 0.71392 0.01302  0.10155  0.26388  536 ARG B CB  
1554 C CG  . ARG A 259 ? 0.72580 0.99920 0.78695 -0.00395 0.09842  0.26942  536 ARG B CG  
1555 C CD  . ARG A 259 ? 0.66028 0.96605 0.72398 -0.00140 0.10394  0.28678  536 ARG B CD  
1556 N NE  . ARG A 259 ? 0.79649 1.06068 0.84919 -0.01064 0.11864  0.29737  536 ARG B NE  
1557 C CZ  . ARG A 259 ? 0.92347 1.18445 0.97408 0.01213  0.12388  0.30869  536 ARG B CZ  
1558 N NH1 . ARG A 259 ? 0.85306 1.15901 0.91305 0.03937  0.11561  0.31198  536 ARG B NH1 
1559 N NH2 . ARG A 259 ? 0.94754 1.15973 0.98411 0.00900  0.13822  0.31697  536 ARG B NH2 
1560 N N   . VAL A 260 ? 0.64844 0.77000 0.69027 0.03122  0.10325  0.24053  537 VAL B N   
1561 C CA  . VAL A 260 ? 0.72687 0.79590 0.75747 0.02668  0.11008  0.23414  537 VAL B CA  
1562 C C   . VAL A 260 ? 0.69874 0.76789 0.73495 0.02875  0.09990  0.21785  537 VAL B C   
1563 O O   . VAL A 260 ? 0.69775 0.73239 0.72555 0.01521  0.10362  0.21060  537 VAL B O   
1564 C CB  . VAL A 260 ? 0.80927 0.85515 0.83289 0.04977  0.11826  0.24151  537 VAL B CB  
1565 C CG1 . VAL A 260 ? 0.82864 0.89788 0.86292 0.07696  0.10824  0.23416  537 VAL B CG1 
1566 C CG2 . VAL A 260 ? 0.93414 0.92265 0.93983 0.04293  0.13065  0.24089  537 VAL B CG2 
1567 N N   . MET A 261 ? 0.67753 0.78137 0.72480 0.04478  0.08866  0.21248  538 MET B N   
1568 C CA  . MET A 261 ? 0.68253 0.78479 0.73293 0.04647  0.08040  0.19813  538 MET B CA  
1569 C C   . MET A 261 ? 0.67243 0.77343 0.71989 0.02201  0.07996  0.19425  538 MET B C   
1570 O O   . MET A 261 ? 0.56643 0.64370 0.61026 0.01579  0.07939  0.18432  538 MET B O   
1571 C CB  . MET A 261 ? 0.68766 0.82437 0.74491 0.06439  0.07071  0.19435  538 MET B CB  
1572 C CG  . MET A 261 ? 0.81463 0.95156 0.87376 0.08635  0.06885  0.19128  538 MET B CG  
1573 S SD  . MET A 261 ? 0.82302 0.98978 0.88324 0.10421  0.05920  0.18399  538 MET B SD  
1574 C CE  . MET A 261 ? 0.88561 1.06887 0.94733 0.12438  0.05966  0.18847  538 MET B CE  
1575 N N   . ARG A 262 ? 0.61619 0.74637 0.66522 0.00842  0.08026  0.20193  539 ARG B N   
1576 C CA  . ARG A 262 ? 0.66395 0.80416 0.71056 -0.01711 0.07927  0.19806  539 ARG B CA  
1577 C C   . ARG A 262 ? 0.62670 0.71739 0.66110 -0.03774 0.08767  0.19265  539 ARG B C   
1578 O O   . ARG A 262 ? 0.60166 0.68438 0.63303 -0.04758 0.08465  0.18216  539 ARG B O   
1579 C CB  . ARG A 262 ? 0.66224 0.84501 0.71228 -0.03132 0.08017  0.20872  539 ARG B CB  
1580 C CG  . ARG A 262 ? 0.70598 0.90878 0.75383 -0.06068 0.07917  0.20473  539 ARG B CG  
1581 C CD  . ARG A 262 ? 0.83278 1.10199 0.88954 -0.05449 0.07066  0.20851  539 ARG B CD  
1582 N NE  . ARG A 262 ? 0.89497 1.19518 0.95053 -0.08422 0.06991  0.20611  539 ARG B NE  
1583 N N   . SER A 263 ? 0.57769 0.63463 0.60263 -0.04241 0.09888  0.20004  540 SER B N   
1584 C CA  . SER A 263 ? 0.72441 0.72810 0.73208 -0.06080 0.10909  0.19530  540 SER B CA  
1585 C C   . SER A 263 ? 0.69658 0.66639 0.70076 -0.04332 0.10873  0.18651  540 SER B C   
1586 O O   . SER A 263 ? 0.65420 0.59093 0.64650 -0.05696 0.11246  0.17769  540 SER B O   
1587 C CB  . SER A 263 ? 0.75618 0.72775 0.74966 -0.06871 0.12382  0.20732  540 SER B CB  
1588 O OG  . SER A 263 ? 0.85730 0.82850 0.85466 -0.03890 0.12579  0.21666  540 SER B OG  
1589 N N   . LEU A 264 ? 0.66119 0.64189 0.67511 -0.01459 0.10412  0.18784  541 LEU B N   
1590 C CA  . LEU A 264 ? 0.67684 0.63763 0.69051 -0.00081 0.10210  0.17848  541 LEU B CA  
1591 C C   . LEU A 264 ? 0.67653 0.64955 0.69461 -0.01019 0.09342  0.16653  541 LEU B C   
1592 O O   . LEU A 264 ? 0.67754 0.62220 0.68776 -0.01561 0.09581  0.15832  541 LEU B O   
1593 C CB  . LEU A 264 ? 0.67122 0.65028 0.69531 0.02730  0.09774  0.18044  541 LEU B CB  
1594 C CG  . LEU A 264 ? 0.69362 0.65936 0.71087 0.03978  0.10769  0.19291  541 LEU B CG  
1595 C CD1 . LEU A 264 ? 0.66131 0.65615 0.68941 0.06598  0.10237  0.19475  541 LEU B CD1 
1596 C CD2 . LEU A 264 ? 0.68861 0.60444 0.68807 0.03899  0.12003  0.19360  541 LEU B CD2 
1597 N N   . LEU A 265 ? 0.60306 0.61856 0.63165 -0.01024 0.08425  0.16637  542 LEU B N   
1598 C CA  . LEU A 265 ? 0.61669 0.64577 0.64681 -0.01697 0.07741  0.15725  542 LEU B CA  
1599 C C   . LEU A 265 ? 0.59503 0.60899 0.61443 -0.04429 0.08155  0.15281  542 LEU B C   
1600 O O   . LEU A 265 ? 0.58225 0.58156 0.59676 -0.04905 0.08045  0.14338  542 LEU B O   
1601 C CB  . LEU A 265 ? 0.54610 0.62372 0.58483 -0.01005 0.06920  0.16044  542 LEU B CB  
1602 C CG  . LEU A 265 ? 0.59374 0.68295 0.63891 0.01605  0.06476  0.16132  542 LEU B CG  
1603 C CD1 . LEU A 265 ? 0.57878 0.71277 0.62755 0.02366  0.05936  0.16700  542 LEU B CD1 
1604 C CD2 . LEU A 265 ? 0.51043 0.58018 0.55440 0.02600  0.06236  0.15094  542 LEU B CD2 
1605 N N   . ALA A 266 ? 0.59516 0.61211 0.60939 -0.06395 0.08692  0.15900  543 ALA B N   
1606 C CA  . ALA A 266 ? 0.56244 0.56230 0.56329 -0.09450 0.09189  0.15298  543 ALA B CA  
1607 C C   . ALA A 266 ? 0.63217 0.57161 0.61678 -0.09558 0.10054  0.14610  543 ALA B C   
1608 O O   . ALA A 266 ? 0.66137 0.58728 0.63677 -0.10991 0.10039  0.13542  543 ALA B O   
1609 C CB  . ALA A 266 ? 0.54350 0.55150 0.53951 -0.11744 0.09841  0.16127  543 ALA B CB  
1610 N N   . ALA A 267 ? 0.59633 0.50194 0.57606 -0.07832 0.10842  0.15253  544 ALA B N   
1611 C CA  . ALA A 267 ? 0.69262 0.54282 0.65494 -0.07398 0.11798  0.14800  544 ALA B CA  
1612 C C   . ALA A 267 ? 0.72058 0.57342 0.68885 -0.06138 0.11097  0.13786  544 ALA B C   
1613 O O   . ALA A 267 ? 0.72530 0.54494 0.67878 -0.06938 0.11565  0.12939  544 ALA B O   
1614 C CB  . ALA A 267 ? 0.63255 0.45762 0.58994 -0.05147 0.12725  0.15904  544 ALA B CB  
1615 N N   . GLN A 268 ? 0.62010 0.50923 0.60758 -0.04197 0.10085  0.13847  545 GLN B N   
1616 C CA  . GLN A 268 ? 0.68106 0.57351 0.67358 -0.03267 0.09503  0.12948  545 GLN B CA  
1617 C C   . GLN A 268 ? 0.63964 0.54148 0.62777 -0.05194 0.09096  0.12086  545 GLN B C   
1618 O O   . GLN A 268 ? 0.64915 0.53285 0.63069 -0.05251 0.09178  0.11270  545 GLN B O   
1619 C CB  . GLN A 268 ? 0.62560 0.55250 0.63554 -0.01319 0.08605  0.13080  545 GLN B CB  
1620 C CG  . GLN A 268 ? 0.58711 0.51533 0.60375 0.00755  0.08740  0.13635  545 GLN B CG  
1621 C CD  . GLN A 268 ? 0.62682 0.58507 0.65633 0.02103  0.07853  0.13361  545 GLN B CD  
1622 O OE1 . GLN A 268 ? 0.75138 0.73636 0.78540 0.01980  0.07291  0.13538  545 GLN B OE1 
1623 N NE2 . GLN A 268 ? 0.75397 0.70726 0.78714 0.03327  0.07816  0.12895  545 GLN B NE2 
1624 N N   . GLN A 269 ? 0.60647 0.54268 0.59856 -0.06653 0.08630  0.12297  546 GLN B N   
1625 C CA  . GLN A 269 ? 0.63640 0.59336 0.62535 -0.08281 0.08144  0.11530  546 GLN B CA  
1626 C C   . GLN A 269 ? 0.67204 0.59166 0.64146 -0.10580 0.08880  0.10659  546 GLN B C   
1627 O O   . GLN A 269 ? 0.66499 0.58119 0.62858 -0.10977 0.08681  0.09736  546 GLN B O   
1628 C CB  . GLN A 269 ? 0.62639 0.63516 0.62296 -0.09344 0.07567  0.12045  546 GLN B CB  
1629 C CG  . GLN A 269 ? 0.55578 0.59838 0.54981 -0.10770 0.06997  0.11362  546 GLN B CG  
1630 C CD  . GLN A 269 ? 0.68568 0.73903 0.68417 -0.08589 0.06430  0.11076  546 GLN B CD  
1631 O OE1 . GLN A 269 ? 0.63420 0.71286 0.64211 -0.06461 0.05975  0.11711  546 GLN B OE1 
1632 N NE2 . GLN A 269 ? 0.62867 0.65957 0.61777 -0.09091 0.06571  0.10123  546 GLN B NE2 
1633 N N   . THR A 270 ? 0.73274 0.62039 0.68892 -0.12078 0.09854  0.10930  547 THR B N   
1634 C CA  . THR A 270 ? 0.74874 0.59209 0.68037 -0.14414 0.10756  0.09979  547 THR B CA  
1635 C C   . THR A 270 ? 0.77183 0.56719 0.69183 -0.12679 0.11374  0.09511  547 THR B C   
1636 O O   . THR A 270 ? 0.79012 0.55918 0.69247 -0.13954 0.11729  0.08409  547 THR B O   
1637 C CB  . THR A 270 ? 0.78346 0.59639 0.69900 -0.16478 0.11918  0.10470  547 THR B CB  
1638 O OG1 . THR A 270 ? 0.81327 0.59490 0.72745 -0.14094 0.12717  0.11567  547 THR B OG1 
1639 C CG2 . THR A 270 ? 0.74560 0.61154 0.67372 -0.18283 0.11349  0.11024  547 THR B CG2 
1640 N N   . PHE A 271 ? 0.66734 0.45644 0.59715 -0.09767 0.11471  0.10310  548 PHE B N   
1641 C CA  . PHE A 271 ? 0.72398 0.47866 0.64569 -0.07833 0.12000  0.10001  548 PHE B CA  
1642 C C   . PHE A 271 ? 0.74366 0.51949 0.67251 -0.07675 0.11143  0.09062  548 PHE B C   
1643 O O   . PHE A 271 ? 0.74263 0.48789 0.65530 -0.07899 0.11651  0.08256  548 PHE B O   
1644 C CB  . PHE A 271 ? 0.69311 0.45137 0.62682 -0.04923 0.12125  0.11034  548 PHE B CB  
1645 C CG  . PHE A 271 ? 0.81739 0.54699 0.74295 -0.02817 0.12809  0.10968  548 PHE B CG  
1646 C CD1 . PHE A 271 ? 0.73752 0.47925 0.67061 -0.02020 0.12261  0.10265  548 PHE B CD1 
1647 C CD2 . PHE A 271 ? 0.75975 0.45214 0.66879 -0.01477 0.14109  0.11741  548 PHE B CD2 
1648 C CE1 . PHE A 271 ? 0.74727 0.46934 0.67380 -0.00099 0.12910  0.10284  548 PHE B CE1 
1649 C CE2 . PHE A 271 ? 0.82360 0.49665 0.72469 0.00748  0.14779  0.11810  548 PHE B CE2 
1650 C CZ  . PHE A 271 ? 0.79474 0.48503 0.70569 0.01350  0.14136  0.11056  548 PHE B CZ  
1651 N N   . VAL A 272 ? 0.65039 0.47469 0.60003 -0.07157 0.10002  0.09226  549 VAL B N   
1652 C CA  . VAL A 272 ? 0.68320 0.52622 0.63750 -0.06823 0.09345  0.08541  549 VAL B CA  
1653 C C   . VAL A 272 ? 0.66833 0.51142 0.60795 -0.09255 0.09320  0.07560  549 VAL B C   
1654 O O   . VAL A 272 ? 0.68372 0.51614 0.61520 -0.09197 0.09370  0.06777  549 VAL B O   
1655 C CB  . VAL A 272 ? 0.60262 0.49128 0.57683 -0.05569 0.08372  0.09049  549 VAL B CB  
1656 C CG1 . VAL A 272 ? 0.55978 0.46758 0.53474 -0.05365 0.07854  0.08509  549 VAL B CG1 
1657 C CG2 . VAL A 272 ? 0.49659 0.38205 0.48228 -0.03354 0.08411  0.09617  549 VAL B CG2 
1658 N N   . ASP A 273 ? 0.70297 0.56016 0.63823 -0.11555 0.09273  0.07542  550 ASP B N   
1659 C CA  . ASP A 273 ? 0.69840 0.55875 0.61820 -0.14273 0.09263  0.06424  550 ASP B CA  
1660 C C   . ASP A 273 ? 0.78517 0.58543 0.67906 -0.15055 0.10329  0.05478  550 ASP B C   
1661 O O   . ASP A 273 ? 0.78262 0.58052 0.66422 -0.16096 0.10242  0.04346  550 ASP B O   
1662 C CB  . ASP A 273 ? 0.66240 0.54725 0.58081 -0.16990 0.09195  0.06552  550 ASP B CB  
1663 C CG  . ASP A 273 ? 0.81604 0.76261 0.75736 -0.16040 0.08223  0.07544  550 ASP B CG  
1664 O OD1 . ASP A 273 ? 0.84378 0.81933 0.79736 -0.13915 0.07496  0.07758  550 ASP B OD1 
1665 O OD2 . ASP A 273 ? 0.88036 0.84416 0.82521 -0.17355 0.08308  0.08162  550 ASP B OD2 
1666 N N   . ARG A 274 ? 0.77739 0.52890 0.66010 -0.14444 0.11425  0.05971  551 ARG B N   
1667 C CA  . ARG A 274 ? 0.91521 0.60320 0.76889 -0.14616 0.12690  0.05268  551 ARG B CA  
1668 C C   . ARG A 274 ? 0.92360 0.60493 0.77971 -0.12132 0.12599  0.05023  551 ARG B C   
1669 O O   . ARG A 274 ? 0.91669 0.56860 0.75152 -0.12691 0.13093  0.03960  551 ARG B O   
1670 C CB  . ARG A 274 ? 0.91812 0.55871 0.75860 -0.13858 0.14006  0.06201  551 ARG B CB  
1671 C CG  . ARG A 274 ? 1.03050 0.66061 0.85947 -0.16720 0.14576  0.06368  551 ARG B CG  
1672 C CD  . ARG A 274 ? 1.18831 0.75228 0.99159 -0.16098 0.16381  0.07151  551 ARG B CD  
1673 N NE  . ARG A 274 ? 1.17078 0.74160 0.99023 -0.12649 0.16484  0.08712  551 ARG B NE  
1674 C CZ  . ARG A 274 ? 1.16064 0.75787 0.99656 -0.12342 0.16259  0.09929  551 ARG B CZ  
1675 N NH1 . ARG A 274 ? 1.17737 0.79878 1.01753 -0.15193 0.15934  0.09921  551 ARG B NH1 
1676 N NH2 . ARG A 274 ? 0.97067 0.57522 0.81933 -0.09109 0.16341  0.11170  551 ARG B NH2 
1677 N N   . LEU A 275 ? 0.81080 0.51938 0.69137 -0.09514 0.12023  0.05943  552 LEU B N   
1678 C CA  . LEU A 275 ? 0.84859 0.55864 0.73418 -0.07457 0.11897  0.05765  552 LEU B CA  
1679 C C   . LEU A 275 ? 0.82325 0.55870 0.70899 -0.08506 0.11159  0.04818  552 LEU B C   
1680 O O   . LEU A 275 ? 0.83104 0.54661 0.70290 -0.08222 0.11530  0.04074  552 LEU B O   
1681 C CB  . LEU A 275 ? 0.75469 0.49388 0.66632 -0.05104 0.11371  0.06784  552 LEU B CB  
1682 C CG  . LEU A 275 ? 0.81619 0.55147 0.73209 -0.02936 0.11572  0.06819  552 LEU B CG  
1683 C CD1 . LEU A 275 ? 0.84973 0.53755 0.74248 -0.02111 0.12862  0.06751  552 LEU B CD1 
1684 C CD2 . LEU A 275 ? 0.77445 0.53822 0.71403 -0.01152 0.11117  0.07669  552 LEU B CD2 
1685 N N   . VAL A 276 ? 0.72854 0.51019 0.62833 -0.09532 0.10172  0.04909  553 VAL B N   
1686 C CA  . VAL A 276 ? 0.75075 0.56189 0.64904 -0.10341 0.09522  0.04157  553 VAL B CA  
1687 C C   . VAL A 276 ? 0.82693 0.60979 0.69804 -0.12569 0.10055  0.02799  553 VAL B C   
1688 O O   . VAL A 276 ? 0.85891 0.63732 0.72018 -0.12320 0.10087  0.02027  553 VAL B O   
1689 C CB  . VAL A 276 ? 0.67616 0.54310 0.58950 -0.11054 0.08543  0.04586  553 VAL B CB  
1690 C CG1 . VAL A 276 ? 0.65557 0.55505 0.56207 -0.12208 0.08007  0.03766  553 VAL B CG1 
1691 C CG2 . VAL A 276 ? 0.65571 0.54691 0.59099 -0.08577 0.08070  0.05715  553 VAL B CG2 
1692 N N   . HIS A 277 ? 0.82750 0.58804 0.68385 -0.14856 0.10580  0.02452  554 HIS B N   
1693 C CA  . HIS A 277 ? 0.91518 0.64280 0.74104 -0.17421 0.11218  0.00961  554 HIS B CA  
1694 C C   . HIS A 277 ? 0.94806 0.61767 0.75206 -0.15933 0.12291  0.00486  554 HIS B C   
1695 O O   . HIS A 277 ? 0.88612 0.53878 0.66800 -0.17028 0.12546  -0.00850 554 HIS B O   
1696 C CB  . HIS A 277 ? 0.92407 0.63092 0.73637 -0.20216 0.11833  0.00824  554 HIS B CB  
1697 C CG  . HIS A 277 ? 1.07135 0.73702 0.84782 -0.23342 0.12668  -0.00858 554 HIS B CG  
1698 N ND1 . HIS A 277 ? 1.14804 0.73523 0.89223 -0.23383 0.14266  -0.01229 554 HIS B ND1 
1699 C CD2 . HIS A 277 ? 1.12829 0.81983 0.89337 -0.26559 0.12202  -0.02326 554 HIS B CD2 
1700 C CE1 . HIS A 277 ? 1.26451 0.82439 0.97698 -0.26644 0.14810  -0.02959 554 HIS B CE1 
1701 N NE2 . HIS A 277 ? 1.23203 0.85716 0.95768 -0.28792 0.13510  -0.03719 554 HIS B NE2 
1702 N N   . LEU A 278 ? 0.89230 0.53448 0.70110 -0.13341 0.12945  0.01564  555 LEU B N   
1703 C CA  . LEU A 278 ? 0.95227 0.54621 0.74090 -0.11506 0.14016  0.01324  555 LEU B CA  
1704 C C   . LEU A 278 ? 0.96592 0.58574 0.76355 -0.10036 0.13425  0.01002  555 LEU B C   
1705 O O   . LEU A 278 ? 1.01375 0.60700 0.78785 -0.10203 0.13959  -0.00042 555 LEU B O   
1706 C CB  . LEU A 278 ? 1.01751 0.58998 0.81210 -0.08887 0.14762  0.02718  555 LEU B CB  
1707 C CG  . LEU A 278 ? 1.13016 0.65290 0.90122 -0.06624 0.16113  0.02762  555 LEU B CG  
1708 C CD2 . LEU A 278 ? 1.05772 0.60733 0.85420 -0.03390 0.15893  0.04037  555 LEU B CD2 
1709 N N   . MET A 279 ? 0.87451 0.54375 0.70360 -0.08621 0.12420  0.01877  556 MET B N   
1710 C CA  . MET A 279 ? 0.85555 0.54926 0.69260 -0.07374 0.11966  0.01716  556 MET B CA  
1711 C C   . MET A 279 ? 0.90913 0.61024 0.72864 -0.09266 0.11699  0.00356  556 MET B C   
1712 O O   . MET A 279 ? 0.88365 0.57653 0.69219 -0.08443 0.11962  -0.00195 556 MET B O   
1713 C CB  . MET A 279 ? 0.80901 0.55200 0.67725 -0.06276 0.10992  0.02731  556 MET B CB  
1714 C CG  . MET A 279 ? 0.81195 0.55272 0.69773 -0.04338 0.11188  0.03888  556 MET B CG  
1715 S SD  . MET A 279 ? 0.95188 0.67624 0.83675 -0.01906 0.11928  0.04134  556 MET B SD  
1716 C CE  . MET A 279 ? 0.86408 0.54802 0.73660 -0.00980 0.13009  0.04587  556 MET B CE  
1717 N N   . LYS A 280 ? 0.88116 0.60277 0.69784 -0.11844 0.11165  -0.00208 557 LYS B N   
1718 C CA  . LYS A 280 ? 0.91692 0.65457 0.71721 -0.13834 0.10820  -0.01602 557 LYS B CA  
1719 C C   . LYS A 280 ? 0.97980 0.65922 0.74346 -0.15050 0.11903  -0.03035 557 LYS B C   
1720 O O   . LYS A 280 ? 0.98120 0.66166 0.72840 -0.15455 0.11886  -0.04177 557 LYS B O   
1721 C CB  . LYS A 280 ? 0.88170 0.66344 0.68833 -0.16431 0.09993  -0.01849 557 LYS B CB  
1722 C CG  . LYS A 280 ? 0.91173 0.75481 0.74825 -0.15050 0.08950  -0.00596 557 LYS B CG  
1723 C CD  . LYS A 280 ? 0.89327 0.78196 0.73525 -0.17439 0.08255  -0.00685 557 LYS B CD  
1724 C CE  . LYS A 280 ? 0.83006 0.77095 0.69940 -0.15569 0.07454  0.00825  557 LYS B CE  
1725 N NZ  . LYS A 280 ? 1.00627 0.99066 0.88174 -0.17643 0.06911  0.00966  557 LYS B NZ  
1726 N N   . ALA A 281 ? 0.91598 0.54199 0.66365 -0.15497 0.12958  -0.02965 558 ALA B N   
1727 C CA  . ALA A 281 ? 0.99417 0.55383 0.70073 -0.16517 0.14275  -0.04270 558 ALA B CA  
1728 C C   . ALA A 281 ? 1.04280 0.57756 0.73903 -0.13643 0.14915  -0.04261 558 ALA B C   
1729 O O   . ALA A 281 ? 1.00556 0.51182 0.67136 -0.14352 0.15457  -0.05691 558 ALA B O   
1730 C CB  . ALA A 281 ? 0.97043 0.47583 0.66134 -0.17028 0.15477  -0.03801 558 ALA B CB  
1731 N N   . VAL A 282 ? 1.00649 0.55491 0.72740 -0.10470 0.14860  -0.02706 559 VAL B N   
1732 C CA  . VAL A 282 ? 1.01403 0.55027 0.72941 -0.07742 0.15405  -0.02531 559 VAL B CA  
1733 C C   . VAL A 282 ? 0.97437 0.54286 0.68912 -0.08145 0.14701  -0.03444 559 VAL B C   
1734 O O   . VAL A 282 ? 1.03129 0.57515 0.72385 -0.07136 0.15388  -0.04127 559 VAL B O   
1735 C CB  . VAL A 282 ? 0.91094 0.47094 0.65784 -0.04843 0.15256  -0.00754 559 VAL B CB  
1736 C CG1 . VAL A 282 ? 0.94730 0.50427 0.69125 -0.02259 0.15783  -0.00503 559 VAL B CG1 
1737 C CG2 . VAL A 282 ? 0.91815 0.44567 0.66093 -0.04209 0.16074  0.00094  559 VAL B CG2 
1738 N N   . GLN A 283 ? 0.92379 0.54728 0.65960 -0.09485 0.13425  -0.03447 560 GLN B N   
1739 C CA  . GLN A 283 ? 0.93673 0.60056 0.67647 -0.09322 0.12717  -0.03888 560 GLN B CA  
1740 C C   . GLN A 283 ? 1.05819 0.72621 0.77261 -0.12180 0.12457  -0.05738 560 GLN B C   
1741 O O   . GLN A 283 ? 1.09831 0.80711 0.81517 -0.12171 0.11789  -0.06122 560 GLN B O   
1742 C CB  . GLN A 283 ? 0.82972 0.55316 0.60483 -0.08578 0.11618  -0.02607 560 GLN B CB  
1743 C CG  . GLN A 283 ? 0.79868 0.52127 0.59814 -0.06094 0.11825  -0.00988 560 GLN B CG  
1744 C CD  . GLN A 283 ? 0.88745 0.60167 0.68529 -0.03815 0.12406  -0.00669 560 GLN B CD  
1745 O OE1 . GLN A 283 ? 0.87639 0.58894 0.65665 -0.03849 0.12575  -0.01532 560 GLN B OE1 
1746 N NE2 . GLN A 283 ? 0.83457 0.54755 0.65053 -0.01903 0.12713  0.00541  560 GLN B NE2 
1747 N N   . ARG A 284 ? 1.10287 0.73053 0.79155 -0.14702 0.13032  -0.06902 561 ARG B N   
1748 C CA  . ARG A 284 ? 1.15311 0.79087 0.81872 -0.18114 0.12700  -0.08823 561 ARG B CA  
1749 C C   . ARG A 284 ? 1.22877 0.85065 0.86626 -0.17798 0.13079  -0.10247 561 ARG B C   
1750 O O   . ARG A 284 ? 1.14998 0.81735 0.78479 -0.19082 0.12250  -0.11237 561 ARG B O   
1751 C CB  . ARG A 284 ? 1.16742 0.75463 0.80738 -0.21094 0.13523  -0.09790 561 ARG B CB  
1752 C CG  . ARG A 284 ? 1.18412 0.81646 0.84010 -0.23971 0.12627  -0.09769 561 ARG B CG  
1753 C CD  . ARG A 284 ? 1.27089 0.84686 0.90124 -0.26798 0.13680  -0.10487 561 ARG B CD  
1754 N NE  . ARG A 284 ? 1.31543 0.93818 0.96998 -0.28747 0.12877  -0.09781 561 ARG B NE  
1755 C CZ  . ARG A 284 ? 1.32995 0.92257 0.96981 -0.31703 0.13554  -0.10159 561 ARG B CZ  
1756 N NH1 . ARG A 284 ? 1.41504 0.92432 1.01259 -0.33216 0.15158  -0.11307 561 ARG B NH1 
1757 N NH2 . ARG A 284 ? 1.32481 0.97014 0.99082 -0.33090 0.12726  -0.09302 561 ARG B NH2 
1758 N N   . GLU A 285 ? 1.24906 0.80783 0.86289 -0.16042 0.14388  -0.10383 562 GLU B N   
1759 C CA  . GLU A 285 ? 1.21352 0.75026 0.79873 -0.15159 0.14955  -0.11567 562 GLU B CA  
1760 C C   . GLU A 285 ? 1.24349 0.79427 0.84975 -0.11090 0.15089  -0.09917 562 GLU B C   
1761 O O   . GLU A 285 ? 1.15910 0.72271 0.79592 -0.09153 0.14987  -0.08070 562 GLU B O   
1762 C CB  . GLU A 285 ? 1.26319 0.71372 0.79899 -0.16188 0.16563  -0.13041 562 GLU B CB  
1763 C CG  . GLU A 285 ? 1.36570 0.79726 0.87522 -0.20791 0.16610  -0.14943 562 GLU B CG  
1764 N N   . SER A 286 ? 1.24449 0.79544 0.83371 -0.09957 0.15328  -0.10651 563 SER B N   
1765 C CA  . SER A 286 ? 1.18017 0.74682 0.78754 -0.06393 0.15548  -0.09150 563 SER B CA  
1766 C C   . SER A 286 ? 1.18779 0.69477 0.77664 -0.04072 0.17052  -0.08686 563 SER B C   
1767 O O   . SER A 286 ? 1.28988 0.73500 0.84013 -0.04907 0.18133  -0.09888 563 SER B O   
1768 C CB  . SER A 286 ? 1.12604 0.72261 0.72412 -0.05851 0.15240  -0.09887 563 SER B CB  
1769 O OG  . SER A 286 ? 1.21842 0.76826 0.77021 -0.06862 0.16053  -0.11943 563 SER B OG  
1770 N N   . GLY A 287 ? 1.09785 0.62501 0.71314 -0.01133 0.17195  -0.06884 564 GLY B N   
1771 C CA  . GLY A 287 ? 1.06798 0.55575 0.66984 0.01661  0.18560  -0.06163 564 GLY B CA  
1772 C C   . GLY A 287 ? 1.00797 0.54159 0.64879 0.04136  0.18291  -0.04190 564 GLY B C   
1773 O O   . GLY A 287 ? 0.93612 0.51782 0.61200 0.03473  0.17192  -0.03356 564 GLY B O   
1774 N N   . ASN A 288 ? 1.00193 0.52026 0.63381 0.06981  0.19400  -0.03480 565 ASN B N   
1775 C CA  . ASN A 288 ? 0.93988 0.50344 0.60767 0.09027  0.19256  -0.01686 565 ASN B CA  
1776 C C   . ASN A 288 ? 0.92585 0.49470 0.61805 0.09233  0.19124  -0.00479 565 ASN B C   
1777 O O   . ASN A 288 ? 0.95929 0.49618 0.64037 0.08028  0.19207  -0.00897 565 ASN B O   
1778 C CB  . ASN A 288 ? 0.94226 0.50031 0.59509 0.11953  0.20422  -0.01250 565 ASN B CB  
1779 C CG  . ASN A 288 ? 1.10040 0.60584 0.72145 0.13831  0.21869  -0.01250 565 ASN B CG  
1780 O OD1 . ASN A 288 ? 1.00670 0.49463 0.63143 0.13761  0.22053  -0.00735 565 ASN B OD1 
1781 N ND2 . ASN A 288 ? 1.08872 0.56823 0.67602 0.15800  0.23019  -0.01732 565 ASN B ND2 
1782 N N   . ARG A 289 ? 0.88774 0.49864 0.61311 0.10598  0.18939  0.01005  566 ARG B N   
1783 C CA  . ARG A 289 ? 0.86900 0.49413 0.62069 0.10474  0.18573  0.02025  566 ARG B CA  
1784 C C   . ARG A 289 ? 0.91572 0.50210 0.64745 0.11974  0.19651  0.02306  566 ARG B C   
1785 O O   . ARG A 289 ? 0.94789 0.52341 0.68528 0.11196  0.19447  0.02545  566 ARG B O   
1786 C CB  . ARG A 289 ? 0.82309 0.50019 0.61080 0.11374  0.18255  0.03350  566 ARG B CB  
1787 C CG  . ARG A 289 ? 0.82455 0.52135 0.64054 0.10844  0.17674  0.04185  566 ARG B CG  
1788 C CD  . ARG A 289 ? 0.82665 0.57051 0.67579 0.10380  0.17043  0.04967  566 ARG B CD  
1789 N NE  . ARG A 289 ? 0.81077 0.57582 0.66167 0.11746  0.17678  0.05437  566 ARG B NE  
1790 C CZ  . ARG A 289 ? 0.86420 0.65092 0.72440 0.13382  0.18324  0.06305  566 ARG B CZ  
1791 N NH1 . ARG A 289 ? 0.81786 0.61093 0.68810 0.13939  0.18362  0.06839  566 ARG B NH1 
1792 N NH2 . ARG A 289 ? 0.81738 0.62406 0.67636 0.14555  0.18969  0.06689  566 ARG B NH2 
1793 N N   . LYS A 290 ? 0.90620 0.47073 0.61216 0.14341  0.20911  0.02373  567 LYS B N   
1794 C CA  . LYS A 290 ? 0.99945 0.52128 0.67892 0.16264  0.22222  0.02743  567 LYS B CA  
1795 C C   . LYS A 290 ? 1.06914 0.52968 0.71623 0.14308  0.22513  0.01516  567 LYS B C   
1796 O O   . LYS A 290 ? 1.12602 0.56460 0.77013 0.14295  0.22853  0.02009  567 LYS B O   
1797 C CB  . LYS A 290 ? 1.04005 0.54890 0.69269 0.19355  0.23615  0.02975  567 LYS B CB  
1798 C CG  . LYS A 290 ? 1.18517 0.65300 0.80679 0.22291  0.25273  0.03684  567 LYS B CG  
1799 C CD  . LYS A 290 ? 1.27984 0.73870 0.87323 0.25463  0.26629  0.03862  567 LYS B CD  
1800 C CE  . LYS A 290 ? 1.37844 0.78773 0.93109 0.28857  0.28574  0.04565  567 LYS B CE  
1801 N NZ  . LYS A 290 ? 1.59199 0.99207 1.11384 0.32091  0.29936  0.04679  567 LYS B NZ  
1802 N N   . LYS A 291 ? 1.06412 0.49883 0.68637 0.12460  0.22399  -0.00116 568 LYS B N   
1803 C CA  . LYS A 291 ? 1.08689 0.46750 0.67819 0.09902  0.22627  -0.01520 568 LYS B CA  
1804 C C   . LYS A 291 ? 1.09094 0.49492 0.71173 0.07326  0.21406  -0.01289 568 LYS B C   
1805 O O   . LYS A 291 ? 1.13130 0.49424 0.73432 0.06042  0.21894  -0.01572 568 LYS B O   
1806 C CB  . LYS A 291 ? 1.10941 0.47525 0.67494 0.08021  0.22427  -0.03423 568 LYS B CB  
1807 C CG  . LYS A 291 ? 1.19925 0.54674 0.75311 0.04056  0.21783  -0.04973 568 LYS B CG  
1808 C CD  . LYS A 291 ? 1.30493 0.56958 0.80710 0.03272  0.23330  -0.06064 568 LYS B CD  
1809 C CE  . LYS A 291 ? 1.52148 0.73756 0.97726 0.05348  0.24825  -0.06918 568 LYS B CE  
1810 N NZ  . LYS A 291 ? 1.59551 0.71693 0.99212 0.05016  0.26753  -0.07918 568 LYS B NZ  
1811 N N   . LYS A 292 ? 0.98838 0.45571 0.65172 0.06587  0.19935  -0.00735 569 LYS B N   
1812 C CA  . LYS A 292 ? 0.96148 0.45291 0.65095 0.04370  0.18796  -0.00512 569 LYS B CA  
1813 C C   . LYS A 292 ? 0.99851 0.49136 0.70424 0.05753  0.19095  0.00931  569 LYS B C   
1814 O O   . LYS A 292 ? 0.92441 0.40524 0.63161 0.04221  0.18902  0.00969  569 LYS B O   
1815 C CB  . LYS A 292 ? 0.82277 0.37557 0.54699 0.03485  0.17343  -0.00308 569 LYS B CB  
1816 C CG  . LYS A 292 ? 0.90562 0.46346 0.61601 0.01115  0.16700  -0.01811 569 LYS B CG  
1817 C CD  . LYS A 292 ? 0.90793 0.51697 0.64023 0.01505  0.15859  -0.01495 569 LYS B CD  
1818 C CE  . LYS A 292 ? 0.89191 0.53481 0.63446 -0.00821 0.14650  -0.02015 569 LYS B CE  
1819 N NZ  . LYS A 292 ? 0.96579 0.60061 0.67983 -0.02392 0.14599  -0.03678 569 LYS B NZ  
1820 N N   . ASN A 293 ? 0.92682 0.43786 0.64433 0.08628  0.19594  0.02140  570 ASN B N   
1821 C CA  . ASN A 293 ? 0.92169 0.43603 0.65059 0.10212  0.19995  0.03468  570 ASN B CA  
1822 C C   . ASN A 293 ? 1.08109 0.52975 0.77095 0.10605  0.21392  0.03323  570 ASN B C   
1823 O O   . ASN A 293 ? 1.02714 0.46734 0.72180 0.10058  0.21396  0.03877  570 ASN B O   
1824 C CB  . ASN A 293 ? 0.85822 0.40708 0.60193 0.13217  0.20419  0.04652  570 ASN B CB  
1825 C CG  . ASN A 293 ? 0.87917 0.49315 0.66542 0.12578  0.19133  0.05082  570 ASN B CG  
1826 O OD1 . ASN A 293 ? 0.81282 0.44741 0.62093 0.10479  0.17970  0.04901  570 ASN B OD1 
1827 N ND2 . ASN A 293 ? 0.80622 0.45100 0.60175 0.14439  0.19482  0.05703  570 ASN B ND2 
1828 N N   . GLU A 294 ? 1.01430 0.41205 0.66218 0.11491  0.22692  0.02557  571 GLU B N   
1829 C CA  . GLU A 294 ? 1.08136 0.40623 0.68528 0.11878  0.24311  0.02398  571 GLU B CA  
1830 C C   . GLU A 294 ? 1.11657 0.41448 0.71250 0.08076  0.23873  0.01360  571 GLU B C   
1831 O O   . GLU A 294 ? 1.19020 0.44811 0.76908 0.07926  0.24782  0.01829  571 GLU B O   
1832 C CB  . GLU A 294 ? 1.09508 0.36656 0.65134 0.13453  0.25845  0.01580  571 GLU B CB  
1833 C CG  . GLU A 294 ? 1.14335 0.44237 0.70497 0.17546  0.26512  0.02854  571 GLU B CG  
1834 C CD  . GLU A 294 ? 1.42609 0.68795 0.94713 0.19040  0.27681  0.01943  571 GLU B CD  
1835 O OE1 . GLU A 294 ? 1.35229 0.55896 0.83623 0.16875  0.28097  0.00187  571 GLU B OE1 
1836 O OE2 . GLU A 294 ? 1.43798 0.72836 0.96344 0.22362  0.28211  0.02952  571 GLU B OE2 
1837 N N   . ARG A 295 ? 1.08805 0.41004 0.69526 0.05017  0.22559  0.00035  572 ARG B N   
1838 C CA  . ARG A 295 ? 1.07095 0.38450 0.67753 0.01326  0.21956  -0.00786 572 ARG B CA  
1839 C C   . ARG A 295 ? 1.10233 0.45389 0.74603 0.01330  0.21153  0.00631  572 ARG B C   
1840 O O   . ARG A 295 ? 1.20113 0.52250 0.83358 0.00126  0.21688  0.00851  572 ARG B O   
1841 C CB  . ARG A 295 ? 1.08457 0.43384 0.70160 -0.01538 0.20548  -0.02223 572 ARG B CB  
1842 C CG  . ARG A 295 ? 1.18448 0.49836 0.76272 -0.02226 0.21184  -0.03967 572 ARG B CG  
1843 C CD  . ARG A 295 ? 1.14574 0.51301 0.74261 -0.04571 0.19586  -0.05017 572 ARG B CD  
1844 N NE  . ARG A 295 ? 1.23324 0.58091 0.79874 -0.04909 0.19964  -0.06609 572 ARG B NE  
1845 C CZ  . ARG A 295 ? 1.18338 0.57931 0.76193 -0.05756 0.18810  -0.07306 572 ARG B CZ  
1846 N NH1 . ARG A 295 ? 1.07591 0.53983 0.69724 -0.06003 0.17328  -0.06414 572 ARG B NH1 
1847 N NH2 . ARG A 295 ? 1.23261 0.60628 0.77783 -0.06188 0.19256  -0.08899 572 ARG B NH2 
1848 N N   . LEU A 296 ? 1.01059 0.42690 0.69693 0.02610  0.19946  0.01579  573 LEU B N   
1849 C CA  . LEU A 296 ? 0.99951 0.45392 0.72052 0.02895  0.19182  0.02863  573 LEU B CA  
1850 C C   . LEU A 296 ? 1.09490 0.51511 0.80140 0.04939  0.20510  0.04038  573 LEU B C   
1851 O O   . LEU A 296 ? 1.03477 0.45019 0.74608 0.03952  0.20464  0.04548  573 LEU B O   
1852 C CB  . LEU A 296 ? 0.91775 0.43489 0.67774 0.04381  0.18129  0.03630  573 LEU B CB  
1853 C CG  . LEU A 296 ? 0.93286 0.49162 0.72810 0.04675  0.17288  0.04783  573 LEU B CG  
1854 C CD1 . LEU A 296 ? 0.87841 0.45272 0.68604 0.01896  0.16216  0.04387  573 LEU B CD1 
1855 C CD2 . LEU A 296 ? 0.84094 0.45151 0.66720 0.06067  0.16589  0.05383  573 LEU B CD2 
1856 N N   . GLN A 297 ? 1.01637 0.41503 0.70401 0.08023  0.21778  0.04601  574 GLN B N   
1857 C CA  . GLN A 297 ? 1.13374 0.50776 0.80819 0.10562  0.23089  0.05979  574 GLN B CA  
1858 C C   . GLN A 297 ? 1.19066 0.48868 0.82175 0.09327  0.24536  0.05597  574 GLN B C   
1859 O O   . GLN A 297 ? 1.19014 0.47723 0.82140 0.09452  0.24961  0.06571  574 GLN B O   
1860 C CB  . GLN A 297 ? 1.04617 0.42327 0.71061 0.14429  0.24129  0.06792  574 GLN B CB  
1861 C CG  . GLN A 297 ? 1.03136 0.48856 0.74329 0.15461  0.22799  0.07569  574 GLN B CG  
1862 C CD  . GLN A 297 ? 1.14362 0.62128 0.85304 0.18630  0.23486  0.08179  574 GLN B CD  
1863 O OE1 . GLN A 297 ? 1.26702 0.70074 0.93864 0.21114  0.25176  0.08501  574 GLN B OE1 
1864 N NE2 . GLN A 297 ? 1.03384 0.57761 0.78134 0.18602  0.22299  0.08370  574 GLN B NE2 
1865 N N   . ALA A 298 ? 1.22822 0.47243 0.82067 0.07893  0.25339  0.04124  575 ALA B N   
1866 C CA  . ALA A 298 ? 1.27423 0.45209 0.82556 0.06039  0.26591  0.03475  575 ALA B CA  
1867 C C   . ALA A 298 ? 1.28109 0.46911 0.84995 0.02555  0.25735  0.03358  575 ALA B C   
1868 O O   . ALA A 298 ? 1.35525 0.52800 0.91621 0.02423  0.26350  0.04046  575 ALA B O   
1869 C CB  . ALA A 298 ? 1.20095 0.33332 0.71282 0.04381  0.27188  0.01552  575 ALA B CB  
1870 N N   . LEU A 299 ? 1.24052 0.48054 0.84127 -0.00156 0.23881  0.02482  576 LEU B N   
1871 C CA  . LEU A 299 ? 1.17915 0.44000 0.79700 -0.03546 0.22939  0.02283  576 LEU B CA  
1872 C C   . LEU A 299 ? 1.31049 0.60390 0.95847 -0.02018 0.22598  0.04107  576 LEU B C   
1873 O O   . LEU A 299 ? 1.30146 0.58588 0.94850 -0.03993 0.22721  0.04396  576 LEU B O   
1874 C CB  . LEU A 299 ? 1.18949 0.51260 0.83751 -0.05960 0.20956  0.01208  576 LEU B CB  
1875 C CG  . LEU A 299 ? 1.28307 0.58873 0.90580 -0.08650 0.20881  -0.00840 576 LEU B CG  
1876 C CD1 . LEU A 299 ? 1.09405 0.47296 0.75168 -0.09361 0.18968  -0.01306 576 LEU B CD1 
1877 C CD2 . LEU A 299 ? 1.27498 0.54332 0.87047 -0.12715 0.21432  -0.01951 576 LEU B CD2 
1878 N N   . LEU A 300 ? 1.24156 0.57659 0.91666 0.01309  0.22145  0.05291  577 LEU B N   
1879 C CA  . LEU A 300 ? 1.15901 0.52863 0.86185 0.02878  0.21787  0.06896  577 LEU B CA  
1880 C C   . LEU A 300 ? 1.31586 0.62952 0.98678 0.04714  0.23738  0.08064  577 LEU B C   
1881 O O   . LEU A 300 ? 1.33927 0.65762 1.01832 0.04363  0.23792  0.09021  577 LEU B O   
1882 C CB  . LEU A 300 ? 1.02398 0.45287 0.76087 0.05593  0.20868  0.07620  577 LEU B CB  
1883 C CG  . LEU A 300 ? 0.99608 0.48762 0.77107 0.04071  0.18913  0.06989  577 LEU B CG  
1884 C CD1 . LEU A 300 ? 0.88531 0.42118 0.68398 0.06479  0.18422  0.07462  577 LEU B CD1 
1885 C CD2 . LEU A 300 ? 0.87561 0.40209 0.67719 0.02483  0.17800  0.07392  577 LEU B CD2 
1886 N N   . GLY A 301 ? 1.28476 0.55464 0.92064 0.06854  0.25227  0.07968  578 GLY B N   
1887 C CA  . GLY A 301 ? 1.32020 0.56053 0.92960 0.08939  0.26719  0.08812  578 GLY B CA  
1888 C C   . GLY A 301 ? 1.53448 0.72550 1.11420 0.06087  0.27528  0.08081  578 GLY B C   
1889 O O   . GLY A 301 ? 1.55485 0.72211 1.11505 0.07522  0.28782  0.08965  578 GLY B O   
1890 N N   . ASP A 302 ? 1.54173 0.71878 1.11655 0.02044  0.26916  0.06492  579 ASP B N   
1891 C CA  . ASP A 302 ? 1.60483 0.74007 1.15261 -0.01241 0.27610  0.05632  579 ASP B CA  
1892 C C   . ASP A 302 ? 1.55199 0.72324 1.13127 -0.03175 0.26614  0.06386  579 ASP B C   
1893 O O   . ASP A 302 ? 1.50925 0.70652 1.10719 -0.06529 0.25392  0.05601  579 ASP B O   
1894 C CB  . ASP A 302 ? 1.56936 0.67818 1.09474 -0.04739 0.27477  0.03483  579 ASP B CB  
1895 C CG  . ASP A 302 ? 1.68948 0.74681 1.17710 -0.07795 0.28606  0.02473  579 ASP B CG  
1896 N N   . ASN A 303 ? 1.60846 0.78371 1.19228 -0.00934 0.27217  0.07995  580 ASN B N   
1897 C CA  . ASN A 303 ? 1.62955 0.84315 1.24456 -0.02099 0.26313  0.08992  580 ASN B CA  
1898 C C   . ASN A 303 ? 1.65810 0.84794 1.25828 -0.06095 0.26622  0.08322  580 ASN B C   
1899 O O   . ASN A 303 ? 1.67967 0.90712 1.30670 -0.08289 0.25575  0.08665  580 ASN B O   
1900 C CB  . ASN A 303 ? 1.51796 0.74858 1.14318 0.01751  0.26822  0.10942  580 ASN B CB  
1901 C CG  . ASN A 303 ? 1.49460 0.78115 1.16099 0.01432  0.25503  0.12059  580 ASN B CG  
1902 O OD1 . ASN A 303 ? 1.41962 0.74575 1.11478 0.00180  0.24086  0.11741  580 ASN B OD1 
1903 N ND2 . ASN A 303 ? 1.54692 0.83617 1.21424 0.02603  0.26069  0.13405  580 ASN B ND2 
1904 N N   . GLU A 304 ? 1.55793 0.68801 1.11512 -0.07143 0.28112  0.07421  581 GLU B N   
1905 C CA  . GLU A 304 ? 1.55955 0.67162 1.10334 -0.11598 0.28270  0.06457  581 GLU B CA  
1906 C C   . GLU A 304 ? 1.62865 0.77684 1.19113 -0.15430 0.26693  0.04982  581 GLU B C   
1907 O O   . GLU A 304 ? 1.60941 0.80030 1.19822 -0.18038 0.25625  0.05189  581 GLU B O   
1908 C CB  . GLU A 304 ? 1.55089 0.58897 1.04119 -0.12199 0.30236  0.05517  581 GLU B CB  
1909 N N   . LYS A 305 ? 1.71734 0.85405 1.26709 -0.15574 0.26539  0.03589  582 LYS B N   
1910 C CA  . LYS A 305 ? 1.69676 0.86980 1.26219 -0.18790 0.25109  0.02174  582 LYS B CA  
1911 C C   . LYS A 305 ? 1.63465 0.87569 1.24826 -0.18155 0.23507  0.03301  582 LYS B C   
1912 O O   . LYS A 305 ? 1.57614 0.85819 1.21083 -0.21002 0.22609  0.03401  582 LYS B O   
1913 C CB  . LYS A 305 ? 1.64645 0.79333 1.18908 -0.18092 0.25368  0.00757  582 LYS B CB  
1914 C CG  . LYS A 305 ? 1.64053 0.82340 1.19542 -0.21220 0.23999  -0.00798 582 LYS B CG  
1915 N N   . MET A 306 ? 1.71051 0.96578 1.34066 -0.14375 0.23244  0.04233  583 MET B N   
1916 C CA  . MET A 306 ? 1.63365 0.96681 1.31135 -0.13347 0.21309  0.04727  583 MET B CA  
1917 C C   . MET A 306 ? 1.56872 0.94191 1.27824 -0.11445 0.20789  0.06560  583 MET B C   
1918 O O   . MET A 306 ? 1.51205 0.95386 1.25926 -0.11946 0.19073  0.06735  583 MET B O   
1919 C CB  . MET A 306 ? 1.61682 0.96006 1.30066 -0.10300 0.20960  0.04517  583 MET B CB  
1920 C CG  . MET A 306 ? 1.66939 1.01126 1.34046 -0.12298 0.20503  0.02618  583 MET B CG  
1921 S SD  . MET A 306 ? 1.89310 1.31862 1.60092 -0.15403 0.18241  0.01837  583 MET B SD  
1922 C CE  . MET A 306 ? 1.61765 1.04286 1.30939 -0.16434 0.17859  -0.00115 583 MET B CE  
1923 N N   . ASN A 307 ? 1.54256 0.87569 1.23629 -0.08945 0.22271  0.07966  584 ASN B N   
1924 C CA  . ASN A 307 ? 1.35487 0.71714 1.07090 -0.07571 0.22084  0.09672  584 ASN B CA  
1925 C C   . ASN A 307 ? 1.23650 0.66968 0.99604 -0.04774 0.20455  0.10358  584 ASN B C   
1926 O O   . ASN A 307 ? 1.23088 0.71082 1.01866 -0.04670 0.19508  0.11182  584 ASN B O   
1927 C CB  . ASN A 307 ? 1.29396 0.67515 1.01752 -0.11258 0.21625  0.09560  584 ASN B CB  
1928 C CG  . ASN A 307 ? 1.42413 0.81939 1.16010 -0.10039 0.21909  0.11343  584 ASN B CG  
1929 O OD1 . ASN A 307 ? 1.45772 0.90945 1.22325 -0.11293 0.20619  0.11644  584 ASN B OD1 
1930 N ND2 . ASN A 307 ? 1.38385 0.74157 1.10065 -0.07209 0.23260  0.12353  584 ASN B ND2 
1931 N N   . LEU A 308 ? 1.07504 0.51550 0.83846 -0.02564 0.20213  0.10015  585 LEU B N   
1932 C CA  . LEU A 308 ? 1.00252 0.50652 0.80400 -0.00462 0.18759  0.10391  585 LEU B CA  
1933 C C   . LEU A 308 ? 0.88985 0.39262 0.69061 0.03425  0.19515  0.11539  585 LEU B C   
1934 O O   . LEU A 308 ? 0.93477 0.49044 0.76597 0.05002  0.18431  0.11873  585 LEU B O   
1935 C CB  . LEU A 308 ? 0.94513 0.47425 0.75789 -0.01332 0.17631  0.09057  585 LEU B CB  
1936 C CG  . LEU A 308 ? 0.95048 0.50190 0.77075 -0.04762 0.16552  0.07994  585 LEU B CG  
1937 C CD1 . LEU A 308 ? 0.99444 0.56423 0.81956 -0.05216 0.15743  0.06822  585 LEU B CD1 
1938 C CD2 . LEU A 308 ? 0.91332 0.51958 0.76558 -0.05146 0.15291  0.08671  585 LEU B CD2 
1939 N N   . SER A 309 ? 1.02293 0.46822 0.78816 0.05020  0.21404  0.12145  586 SER B N   
1940 C CA  . SER A 309 ? 1.05009 0.49956 0.81230 0.09040  0.22246  0.13401  586 SER B CA  
1941 C C   . SER A 309 ? 1.10962 0.55503 0.86782 0.10709  0.23107  0.15078  586 SER B C   
1942 O O   . SER A 309 ? 1.03076 0.49298 0.79021 0.14227  0.23662  0.16271  586 SER B O   
1943 C CB  . SER A 309 ? 1.14297 0.53409 0.86496 0.10665  0.23964  0.13194  586 SER B CB  
1944 O OG  . SER A 309 ? 1.21253 0.54908 0.89885 0.09237  0.25167  0.12685  586 SER B OG  
1945 N N   . ASP A 310 ? 1.04900 0.47623 0.80186 0.08332  0.23282  0.15257  587 ASP B N   
1946 C CA  . ASP A 310 ? 1.13629 0.56838 0.88779 0.09709  0.23886  0.16628  587 ASP B CA  
1947 C C   . ASP A 310 ? 1.09238 0.53843 0.85922 0.06693  0.23165  0.16802  587 ASP B C   
1948 O O   . ASP A 310 ? 1.11929 0.53003 0.86692 0.03820  0.23676  0.16163  587 ASP B O   
1949 C CB  . ASP A 310 ? 1.18270 0.56065 0.89394 0.10672  0.25706  0.16679  587 ASP B CB  
1950 C CG  . ASP A 310 ? 1.26542 0.63928 0.97212 0.10866  0.26374  0.17852  587 ASP B CG  
1951 O OD1 . ASP A 310 ? 1.24543 0.66838 0.98168 0.11703  0.25484  0.18940  587 ASP B OD1 
1952 O OD2 . ASP A 310 ? 1.34340 0.66487 1.01640 0.10102  0.27812  0.17678  587 ASP B OD2 
1953 N N   . VAL A 311 ? 0.95985 0.47419 0.76543 0.07261  0.21553  0.17138  588 VAL B N   
1954 C CA  . VAL A 311 ? 0.94739 0.49351 0.77320 0.04987  0.20548  0.17229  588 VAL B CA  
1955 C C   . VAL A 311 ? 0.95128 0.53164 0.79155 0.07532  0.20514  0.18773  588 VAL B C   
1956 O O   . VAL A 311 ? 0.86944 0.46307 0.71111 0.10806  0.20836  0.19492  588 VAL B O   
1957 C CB  . VAL A 311 ? 0.92747 0.52674 0.78537 0.03064  0.18456  0.15890  588 VAL B CB  
1958 C CG1 . VAL A 311 ? 1.02562 0.59513 0.86801 0.00212  0.18496  0.14427  588 VAL B CG1 
1959 C CG2 . VAL A 311 ? 0.70055 0.34498 0.58281 0.05486  0.17393  0.15678  588 VAL B CG2 
1960 N N   . GLU A 312 ? 1.03233 0.62737 0.88084 0.05976  0.20246  0.19327  589 GLU B N   
1961 C CA  . GLU A 312 ? 1.03554 0.66147 0.89503 0.08253  0.20310  0.20852  589 GLU B CA  
1962 C C   . GLU A 312 ? 1.00775 0.70672 0.90518 0.09346  0.18327  0.20369  589 GLU B C   
1963 O O   . GLU A 312 ? 1.17595 0.91067 1.09394 0.07620  0.17072  0.19989  589 GLU B O   
1964 C CB  . GLU A 312 ? 1.11952 0.73694 0.97408 0.06092  0.20751  0.21613  589 GLU B CB  
1965 C CG  . GLU A 312 ? 1.26263 0.80560 1.07889 0.03850  0.22630  0.21693  589 GLU B CG  
1966 C CD  . GLU A 312 ? 1.42176 0.95760 1.23230 0.01426  0.23216  0.22503  589 GLU B CD  
1967 O OE1 . GLU A 312 ? 1.54749 1.12898 1.38228 -0.00992 0.21780  0.21908  589 GLU B OE1 
1968 O OE2 . GLU A 312 ? 1.44781 0.94854 1.23491 0.02026  0.24483  0.23067  589 GLU B OE2 
1969 N N   . LEU A 313 ? 0.97647 0.69741 0.88151 0.11949  0.18080  0.20295  590 LEU B N   
1970 C CA  . LEU A 313 ? 0.80846 0.59450 0.74516 0.12956  0.16442  0.19821  590 LEU B CA  
1971 C C   . LEU A 313 ? 0.81852 0.63763 0.77795 0.10624  0.14835  0.18888  590 LEU B C   
1972 O O   . LEU A 313 ? 0.87607 0.72846 0.84864 0.10930  0.14237  0.19375  590 LEU B O   
1973 C CB  . LEU A 313 ? 0.71214 0.52768 0.65245 0.15722  0.16760  0.21182  590 LEU B CB  
1974 C CG  . LEU A 313 ? 0.98067 0.75562 0.89097 0.18205  0.18784  0.22647  590 LEU B CG  
1975 C CD1 . LEU A 313 ? 0.97226 0.77912 0.88373 0.21270  0.19234  0.24196  590 LEU B CD1 
1976 C CD2 . LEU A 313 ? 1.00312 0.76326 0.90357 0.19446  0.19257  0.22126  590 LEU B CD2 
1977 N N   . ILE A 314 ? 0.86148 0.67400 0.82434 0.08575  0.14172  0.17616  591 ILE B N   
1978 C CA  . ILE A 314 ? 0.72012 0.56435 0.70133 0.06694  0.12776  0.16862  591 ILE B CA  
1979 C C   . ILE A 314 ? 0.63143 0.51275 0.63240 0.07501  0.11566  0.15926  591 ILE B C   
1980 O O   . ILE A 314 ? 0.70270 0.57870 0.70216 0.08475  0.11772  0.15517  591 ILE B O   
1981 C CB  . ILE A 314 ? 0.85462 0.67391 0.82599 0.03918  0.12828  0.16134  591 ILE B CB  
1982 C CG1 . ILE A 314 ? 0.75220 0.55186 0.71740 0.03704  0.12869  0.15072  591 ILE B CG1 
1983 C CG2 . ILE A 314 ? 1.00410 0.78421 0.95353 0.02612  0.14137  0.16916  591 ILE B CG2 
1984 C CD1 . ILE A 314 ? 0.87654 0.65780 0.83198 0.01007  0.12813  0.14202  591 ILE B CD1 
1985 N N   . PRO A 315 ? 0.64431 0.56115 0.66138 0.07115  0.10431  0.15588  592 PRO B N   
1986 C CA  . PRO A 315 ? 0.69896 0.64266 0.73001 0.07558  0.09466  0.14611  592 PRO B CA  
1987 C C   . PRO A 315 ? 0.65827 0.58580 0.68679 0.06437  0.09332  0.13626  592 PRO B C   
1988 O O   . PRO A 315 ? 0.62308 0.53319 0.64396 0.04910  0.09449  0.13501  592 PRO B O   
1989 C CB  . PRO A 315 ? 0.66532 0.63651 0.70558 0.07124  0.08580  0.14544  592 PRO B CB  
1990 C CG  . PRO A 315 ? 0.61734 0.58831 0.65304 0.07141  0.09056  0.15737  592 PRO B CG  
1991 C CD  . PRO A 315 ? 0.67103 0.60203 0.69093 0.06251  0.10155  0.16154  592 PRO B CD  
1992 N N   . LEU A 316 ? 0.62317 0.55980 0.65778 0.07109  0.09115  0.12950  593 LEU B N   
1993 C CA  . LEU A 316 ? 0.60400 0.52745 0.63642 0.06168  0.09020  0.12088  593 LEU B CA  
1994 C C   . LEU A 316 ? 0.64406 0.58321 0.68325 0.05358  0.08162  0.11502  593 LEU B C   
1995 O O   . LEU A 316 ? 0.56852 0.52893 0.61587 0.05951  0.07693  0.11240  593 LEU B O   
1996 C CB  . LEU A 316 ? 0.52227 0.45222 0.55829 0.07179  0.09250  0.11737  593 LEU B CB  
1997 C CG  . LEU A 316 ? 0.61943 0.54397 0.65627 0.06377  0.09079  0.10861  593 LEU B CG  
1998 C CD1 . LEU A 316 ? 0.57153 0.46417 0.59440 0.05869  0.09717  0.10835  593 LEU B CD1 
1999 C CD2 . LEU A 316 ? 0.59826 0.54448 0.64399 0.07102  0.09067  0.10465  593 LEU B CD2 
2000 N N   . PRO A 317 ? 0.66087 0.59104 0.69466 0.04122  0.08006  0.11289  594 PRO B N   
2001 C CA  . PRO A 317 ? 0.55994 0.50631 0.59670 0.03835  0.07345  0.11005  594 PRO B CA  
2002 C C   . PRO A 317 ? 0.62792 0.57822 0.66832 0.04344  0.07151  0.10325  594 PRO B C   
2003 O O   . PRO A 317 ? 0.57353 0.53638 0.61565 0.04800  0.06783  0.10182  594 PRO B O   
2004 C CB  . PRO A 317 ? 0.56718 0.50520 0.59603 0.02558  0.07366  0.10864  594 PRO B CB  
2005 C CG  . PRO A 317 ? 0.66670 0.58496 0.68791 0.01789  0.07969  0.11162  594 PRO B CG  
2006 C CD  . PRO A 317 ? 0.61409 0.51999 0.63609 0.02996  0.08511  0.11335  594 PRO B CD  
2007 N N   . LEU A 318 ? 0.60525 0.54307 0.64472 0.04216  0.07500  0.09888  595 LEU B N   
2008 C CA  . LEU A 318 ? 0.60510 0.54562 0.64744 0.04338  0.07478  0.09238  595 LEU B CA  
2009 C C   . LEU A 318 ? 0.62527 0.58398 0.67439 0.04909  0.07245  0.09042  595 LEU B C   
2010 O O   . LEU A 318 ? 0.59316 0.55367 0.64105 0.04708  0.07124  0.08428  595 LEU B O   
2011 C CB  . LEU A 318 ? 0.52718 0.45800 0.56931 0.04250  0.07975  0.09000  595 LEU B CB  
2012 C CG  . LEU A 318 ? 0.61717 0.55186 0.66225 0.04010  0.08075  0.08358  595 LEU B CG  
2013 C CD1 . LEU A 318 ? 0.56180 0.48428 0.59888 0.03492  0.08012  0.08125  595 LEU B CD1 
2014 C CD2 . LEU A 318 ? 0.59792 0.53013 0.64404 0.04140  0.08597  0.08295  595 LEU B CD2 
2015 N N   . GLU A 319 ? 0.54164 0.51245 0.59549 0.05607  0.07272  0.09534  596 GLU B N   
2016 C CA  . GLU A 319 ? 0.60010 0.59420 0.66042 0.06216  0.07036  0.09312  596 GLU B CA  
2017 C C   . GLU A 319 ? 0.57462 0.57986 0.63670 0.07166  0.07053  0.10207  596 GLU B C   
2018 O O   . GLU A 319 ? 0.55927 0.56946 0.62282 0.07977  0.07477  0.10715  596 GLU B O   
2019 C CB  . GLU A 319 ? 0.59325 0.60008 0.65936 0.06245  0.07281  0.08812  596 GLU B CB  
2020 C CG  . GLU A 319 ? 0.66432 0.70311 0.73724 0.06710  0.06995  0.08467  596 GLU B CG  
2021 C CD  . GLU A 319 ? 0.86134 0.91929 0.93987 0.06055  0.07084  0.07587  596 GLU B CD  
2022 O OE1 . GLU A 319 ? 0.89226 0.93641 0.96943 0.05265  0.07408  0.07289  596 GLU B OE1 
2023 O OE2 . GLU A 319 ? 0.98758 1.07837 1.07193 0.06252  0.06841  0.07184  596 GLU B OE2 
2024 N N   . PRO A 320 ? 0.61019 0.61997 0.67052 0.07272  0.06709  0.10540  597 PRO B N   
2025 C CA  . PRO A 320 ? 0.58734 0.60180 0.64730 0.07913  0.06896  0.11611  597 PRO B CA  
2026 C C   . PRO A 320 ? 0.60980 0.64635 0.67443 0.09231  0.07015  0.11973  597 PRO B C   
2027 O O   . PRO A 320 ? 0.56441 0.59908 0.62626 0.09942  0.07467  0.13042  597 PRO B O   
2028 C CB  . PRO A 320 ? 0.57164 0.59335 0.62963 0.07741  0.06439  0.11795  597 PRO B CB  
2029 C CG  . PRO A 320 ? 0.56835 0.59223 0.62455 0.07609  0.06038  0.10774  597 PRO B CG  
2030 C CD  . PRO A 320 ? 0.54742 0.55513 0.60320 0.06888  0.06299  0.10123  597 PRO B CD  
2031 N N   . GLN A 321 ? 0.55296 0.61134 0.62310 0.09521  0.06702  0.11143  598 GLN B N   
2032 C CA  . GLN A 321 ? 0.53299 0.61998 0.60768 0.10859  0.06826  0.11486  598 GLN B CA  
2033 C C   . GLN A 321 ? 0.57400 0.65331 0.64617 0.11756  0.07646  0.12306  598 GLN B C   
2034 O O   . GLN A 321 ? 0.69053 0.78523 0.76152 0.13360  0.08068  0.13246  598 GLN B O   
2035 C CB  . GLN A 321 ? 0.57401 0.68964 0.65447 0.10537  0.06329  0.10201  598 GLN B CB  
2036 C CG  . GLN A 321 ? 0.70818 0.82509 0.78522 0.09861  0.05705  0.09302  598 GLN B CG  
2037 C CD  . GLN A 321 ? 0.92262 1.00811 0.99297 0.08477  0.05667  0.08562  598 GLN B CD  
2038 O OE1 . GLN A 321 ? 0.72826 0.79173 0.79780 0.07938  0.06011  0.08803  598 GLN B OE1 
2039 N NE2 . GLN A 321 ? 0.91099 0.99333 0.97378 0.08075  0.05337  0.07677  598 GLN B NE2 
2040 N N   . VAL A 322 ? 0.49723 0.55140 0.56597 0.10943  0.07969  0.12028  599 VAL B N   
2041 C CA  . VAL A 322 ? 0.49484 0.53608 0.55690 0.11953  0.08885  0.12744  599 VAL B CA  
2042 C C   . VAL A 322 ? 0.58120 0.58556 0.62985 0.12017  0.09593  0.13791  599 VAL B C   
2043 O O   . VAL A 322 ? 0.64567 0.62539 0.69050 0.10453  0.09422  0.13481  599 VAL B O   
2044 C CB  . VAL A 322 ? 0.59814 0.62931 0.66063 0.11125  0.08994  0.11964  599 VAL B CB  
2045 C CG1 . VAL A 322 ? 0.57053 0.58357 0.62226 0.12335  0.10027  0.12705  599 VAL B CG1 
2046 C CG2 . VAL A 322 ? 0.54684 0.61376 0.62121 0.10692  0.08460  0.10928  599 VAL B CG2 
2047 N N   . LYS A 323 ? 0.60090 0.60264 0.64107 0.13722  0.10435  0.14999  600 LYS B N   
2048 C CA  . LYS A 323 ? 0.65865 0.61782 0.68143 0.13560  0.11401  0.15997  600 LYS B CA  
2049 C C   . LYS A 323 ? 0.66438 0.58916 0.67133 0.14033  0.12450  0.16122  600 LYS B C   
2050 O O   . LYS A 323 ? 0.63686 0.57903 0.64372 0.15890  0.12845  0.16353  600 LYS B O   
2051 C CB  . LYS A 323 ? 0.60523 0.57261 0.62285 0.15186  0.11971  0.17368  600 LYS B CB  
2052 C CG  . LYS A 323 ? 0.53330 0.54083 0.56597 0.15175  0.10946  0.17220  600 LYS B CG  
2053 C CD  . LYS A 323 ? 0.67993 0.68401 0.71921 0.12998  0.10050  0.16442  600 LYS B CD  
2054 C CE  . LYS A 323 ? 0.61850 0.66103 0.66994 0.13238  0.09065  0.16109  600 LYS B CE  
2055 N NZ  . LYS A 323 ? 0.79663 0.83614 0.85145 0.11563  0.08331  0.15479  600 LYS B NZ  
2056 N N   . ILE A 324 ? 0.65763 0.53864 0.65065 0.12439  0.12898  0.15943  601 ILE B N   
2057 C CA  . ILE A 324 ? 0.75720 0.60175 0.73239 0.12751  0.13873  0.15805  601 ILE B CA  
2058 C C   . ILE A 324 ? 0.74127 0.53408 0.68778 0.13201  0.15452  0.16828  601 ILE B C   
2059 O O   . ILE A 324 ? 0.78490 0.56097 0.72616 0.11712  0.15558  0.17141  601 ILE B O   
2060 C CB  . ILE A 324 ? 0.66195 0.49491 0.64001 0.10496  0.13221  0.14517  601 ILE B CB  
2061 C CG1 . ILE A 324 ? 0.69125 0.50548 0.66475 0.08140  0.12975  0.14328  601 ILE B CG1 
2062 C CG2 . ILE A 324 ? 0.58903 0.46413 0.59000 0.10235  0.12005  0.13618  601 ILE B CG2 
2063 C CD1 . ILE A 324 ? 0.79257 0.58904 0.76105 0.06150  0.12699  0.13259  601 ILE B CD1 
2064 N N   . ARG A 325 ? 0.70856 0.47630 0.63518 0.15199  0.16743  0.17362  602 ARG B N   
2065 C CA  . ARG A 325 ? 0.83937 0.54422 0.73080 0.15646  0.18569  0.18258  602 ARG B CA  
2066 C C   . ARG A 325 ? 0.94163 0.59934 0.81525 0.13517  0.18909  0.17130  602 ARG B C   
2067 O O   . ARG A 325 ? 0.91104 0.51080 0.75495 0.12531  0.20212  0.17367  602 ARG B O   
2068 C CB  . ARG A 325 ? 0.86206 0.56075 0.73550 0.19374  0.20013  0.19537  602 ARG B CB  
2069 C CG  . ARG A 325 ? 0.94744 0.70309 0.83879 0.21785  0.19628  0.20572  602 ARG B CG  
2070 C CD  . ARG A 325 ? 0.92030 0.68104 0.79499 0.25715  0.20980  0.21812  602 ARG B CD  
2071 N NE  . ARG A 325 ? 1.03763 0.84137 0.91928 0.28240  0.21100  0.23163  602 ARG B NE  
2072 C CZ  . ARG A 325 ? 1.04126 0.82276 0.90931 0.28760  0.21954  0.24433  602 ARG B CZ  
2073 N NH1 . ARG A 325 ? 1.08332 0.79549 0.92192 0.27430  0.23274  0.24504  602 ARG B NH1 
2074 N NH2 . ARG A 325 ? 1.03706 0.87155 0.92156 0.30152  0.21393  0.25191  602 ARG B NH2 
2075 N N   . GLY A 326 ? 0.81122 0.49244 0.70072 0.12762  0.17850  0.15923  603 GLY B N   
2076 C CA  . GLY A 326 ? 0.88067 0.52417 0.75436 0.10880  0.18055  0.14768  603 GLY B CA  
2077 C C   . GLY A 326 ? 0.85013 0.51522 0.73325 0.11778  0.17602  0.14050  603 GLY B C   
2078 O O   . GLY A 326 ? 0.82621 0.53873 0.73026 0.13499  0.17048  0.14386  603 GLY B O   
2079 N N   . ILE A 327 ? 0.85152 0.48511 0.71918 0.10511  0.17850  0.13053  604 ILE B N   
2080 C CA  . ILE A 327 ? 0.79379 0.44514 0.66832 0.11241  0.17532  0.12407  604 ILE B CA  
2081 C C   . ILE A 327 ? 0.85480 0.47047 0.69973 0.13814  0.19197  0.12956  604 ILE B C   
2082 O O   . ILE A 327 ? 0.91166 0.46824 0.72228 0.13871  0.20604  0.13171  604 ILE B O   
2083 C CB  . ILE A 327 ? 0.81314 0.45741 0.68876 0.08547  0.16754  0.11023  604 ILE B CB  
2084 C CG1 . ILE A 327 ? 0.75802 0.44322 0.66220 0.06627  0.15185  0.10672  604 ILE B CG1 
2085 C CG2 . ILE A 327 ? 0.76428 0.41726 0.64044 0.09445  0.16766  0.10475  604 ILE B CG2 
2086 C CD1 . ILE A 327 ? 0.75222 0.43185 0.65422 0.04056  0.14534  0.09561  604 ILE B CD1 
2087 N N   . ILE A 328 ? 0.81762 0.46809 0.67330 0.15971  0.19170  0.13218  605 ILE B N   
2088 C CA  . ILE A 328 ? 0.92357 0.54538 0.75018 0.18823  0.20802  0.13840  605 ILE B CA  
2089 C C   . ILE A 328 ? 0.95417 0.53316 0.75800 0.17714  0.21245  0.12703  605 ILE B C   
2090 O O   . ILE A 328 ? 0.89678 0.50520 0.71867 0.16730  0.20274  0.11844  605 ILE B O   
2091 C CB  . ILE A 328 ? 0.94590 0.62842 0.79229 0.21511  0.20642  0.14572  605 ILE B CB  
2092 C CG1 . ILE A 328 ? 0.88447 0.61028 0.75172 0.22340  0.20134  0.15515  605 ILE B CG1 
2093 C CG2 . ILE A 328 ? 0.86516 0.52266 0.68011 0.24843  0.22403  0.15356  605 ILE B CG2 
2094 C CD1 . ILE A 328 ? 0.82802 0.62589 0.71982 0.24234  0.19667  0.15985  605 ILE B CD1 
2095 N N   . PRO A 329 ? 1.00684 0.51443 0.76911 0.17697  0.22752  0.12605  606 PRO B N   
2096 C CA  . PRO A 329 ? 0.98510 0.45178 0.72467 0.16089  0.23028  0.11223  606 PRO B CA  
2097 C C   . PRO A 329 ? 1.07280 0.55644 0.81076 0.18131  0.23273  0.11075  606 PRO B C   
2098 O O   . PRO A 329 ? 1.04908 0.53946 0.79287 0.16394  0.22504  0.09867  606 PRO B O   
2099 C CB  . PRO A 329 ? 1.04668 0.42949 0.73649 0.16147  0.24961  0.11318  606 PRO B CB  
2100 C CG  . PRO A 329 ? 1.03625 0.42235 0.73271 0.16070  0.25061  0.12391  606 PRO B CG  
2101 C CD  . PRO A 329 ? 0.97007 0.42810 0.70336 0.18522  0.24216  0.13585  606 PRO B CD  
2102 N N   . GLU A 330 ? 1.02533 0.52068 0.75560 0.21869  0.24342  0.12346  607 GLU B N   
2103 C CA  . GLU A 330 ? 1.04355 0.54077 0.76019 0.24099  0.25084  0.12297  607 GLU B CA  
2104 C C   . GLU A 330 ? 1.05490 0.63066 0.81324 0.24097  0.23686  0.12207  607 GLU B C   
2105 O O   . GLU A 330 ? 0.98188 0.56667 0.73311 0.25591  0.24149  0.12117  607 GLU B O   
2106 C CB  . GLU A 330 ? 1.09117 0.56820 0.77613 0.28340  0.27030  0.13755  607 GLU B CB  
2107 C CG  . GLU A 330 ? 1.18533 0.72551 0.89604 0.30885  0.26841  0.15371  607 GLU B CG  
2108 C CD  . GLU A 330 ? 1.32741 0.85177 1.03168 0.30481  0.27098  0.16051  607 GLU B CD  
2109 O OE1 . GLU A 330 ? 1.26290 0.73008 0.94706 0.27904  0.27327  0.15238  607 GLU B OE1 
2110 O OE2 . GLU A 330 ? 1.43141 1.00521 1.15131 0.32685  0.27071  0.17370  607 GLU B OE2 
2111 N N   . THR A 331 ? 0.94217 0.57204 0.74118 0.22402  0.22103  0.12206  608 THR B N   
2112 C CA  . THR A 331 ? 0.82233 0.51968 0.65784 0.21925  0.20906  0.12015  608 THR B CA  
2113 C C   . THR A 331 ? 0.89047 0.59622 0.74724 0.18384  0.19402  0.10800  608 THR B C   
2114 O O   . THR A 331 ? 0.80436 0.56062 0.69119 0.17554  0.18404  0.10639  608 THR B O   
2115 C CB  . THR A 331 ? 0.81918 0.57876 0.68261 0.23225  0.20457  0.13032  608 THR B CB  
2116 O OG1 . THR A 331 ? 0.84036 0.59670 0.71467 0.21690  0.19734  0.13061  608 THR B OG1 
2117 C CG2 . THR A 331 ? 0.81767 0.58316 0.66159 0.27259  0.21969  0.14432  608 THR B CG2 
2118 N N   . ALA A 332 ? 0.88836 0.54690 0.72863 0.16289  0.19306  0.09988  609 ALA B N   
2119 C CA  . ALA A 332 ? 0.84437 0.51161 0.70012 0.13297  0.18023  0.08926  609 ALA B CA  
2120 C C   . ALA A 332 ? 0.84861 0.51018 0.69510 0.13084  0.18148  0.08141  609 ALA B C   
2121 O O   . ALA A 332 ? 0.84305 0.46465 0.65805 0.14208  0.19292  0.07914  609 ALA B O   
2122 C CB  . ALA A 332 ? 0.78307 0.41030 0.62407 0.11172  0.17925  0.08405  609 ALA B CB  
2123 N N   . THR A 333 ? 0.74738 0.44681 0.61864 0.11819  0.17103  0.07778  610 THR B N   
2124 C CA  . THR A 333 ? 0.84260 0.53872 0.70567 0.11515  0.17182  0.07094  610 THR B CA  
2125 C C   . THR A 333 ? 0.77529 0.49427 0.65781 0.09269  0.15970  0.06551  610 THR B C   
2126 O O   . THR A 333 ? 0.75896 0.50000 0.66274 0.08248  0.15128  0.06780  610 THR B O   
2127 C CB  . THR A 333 ? 0.79731 0.52206 0.66570 0.13643  0.17784  0.07681  610 THR B CB  
2128 O OG1 . THR A 333 ? 0.85469 0.63234 0.75669 0.13396  0.17077  0.08231  610 THR B OG1 
2129 C CG2 . THR A 333 ? 0.82504 0.53038 0.67072 0.16467  0.19148  0.08388  610 THR B CG2 
2130 N N   . LEU A 334 ? 0.75102 0.46440 0.62372 0.08749  0.15978  0.05886  611 LEU B N   
2131 C CA  . LEU A 334 ? 0.79154 0.52471 0.67711 0.07051  0.15046  0.05491  611 LEU B CA  
2132 C C   . LEU A 334 ? 0.77545 0.54245 0.67824 0.07673  0.15053  0.05949  611 LEU B C   
2133 O O   . LEU A 334 ? 0.74104 0.51161 0.63825 0.09156  0.15813  0.06200  611 LEU B O   
2134 C CB  . LEU A 334 ? 0.76518 0.47328 0.62702 0.05904  0.15031  0.04432  611 LEU B CB  
2135 C CG  . LEU A 334 ? 0.77677 0.44993 0.61903 0.04676  0.15110  0.03809  611 LEU B CG  
2136 C CD1 . LEU A 334 ? 0.75664 0.40869 0.57343 0.03315  0.15149  0.02543  611 LEU B CD1 
2137 C CD2 . LEU A 334 ? 0.75948 0.45127 0.62128 0.03299  0.14187  0.04116  611 LEU B CD2 
2138 N N   . PHE A 335 ? 0.72994 0.52088 0.65193 0.06570  0.14323  0.06122  612 PHE B N   
2139 C CA  . PHE A 335 ? 0.74321 0.56000 0.67811 0.06744  0.14473  0.06521  612 PHE B CA  
2140 C C   . PHE A 335 ? 0.74414 0.55443 0.66460 0.06710  0.14692  0.06144  612 PHE B C   
2141 O O   . PHE A 335 ? 0.78564 0.58141 0.69266 0.05930  0.14319  0.05524  612 PHE B O   
2142 C CB  . PHE A 335 ? 0.66775 0.50298 0.62165 0.05655  0.13863  0.06823  612 PHE B CB  
2143 C CG  . PHE A 335 ? 0.72744 0.57776 0.69773 0.05731  0.13713  0.07187  612 PHE B CG  
2144 C CD1 . PHE A 335 ? 0.71946 0.56110 0.69056 0.05494  0.13234  0.07116  612 PHE B CD1 
2145 C CD2 . PHE A 335 ? 0.66943 0.54599 0.65400 0.05940  0.14067  0.07582  612 PHE B CD2 
2146 C CE1 . PHE A 335 ? 0.64912 0.50768 0.63458 0.05705  0.13088  0.07451  612 PHE B CE1 
2147 C CE2 . PHE A 335 ? 0.67769 0.57383 0.67690 0.05920  0.13875  0.07796  612 PHE B CE2 
2148 C CZ  . PHE A 335 ? 0.68104 0.56798 0.68043 0.05927  0.13374  0.07738  612 PHE B CZ  
2149 N N   . LYS A 336 ? 0.73594 0.56154 0.65933 0.07504  0.15304  0.06528  613 LYS B N   
2150 C CA  . LYS A 336 ? 0.79722 0.62209 0.70895 0.07581  0.15552  0.06340  613 LYS B CA  
2151 C C   . LYS A 336 ? 0.81882 0.65490 0.73920 0.06537  0.15126  0.06618  613 LYS B C   
2152 O O   . LYS A 336 ? 0.91994 0.77250 0.85207 0.06441  0.15493  0.07277  613 LYS B O   
2153 C CB  . LYS A 336 ? 0.76053 0.60116 0.67308 0.08812  0.16437  0.06826  613 LYS B CB  
2154 C CG  . LYS A 336 ? 0.89294 0.73265 0.79137 0.09132  0.16789  0.06676  613 LYS B CG  
2155 C CD  . LYS A 336 ? 0.85895 0.72074 0.76192 0.10222  0.17686  0.07357  613 LYS B CD  
2156 C CE  . LYS A 336 ? 1.12238 0.98463 1.01105 0.10635  0.18077  0.07305  613 LYS B CE  
2157 N NZ  . LYS A 336 ? 1.11968 0.99584 1.00270 0.12235  0.19045  0.07697  613 LYS B NZ  
2158 N N   . SER A 337 ? 0.79527 0.62288 0.70823 0.05765  0.14464  0.06175  614 SER B N   
2159 C CA  . SER A 337 ? 0.82762 0.66562 0.74349 0.05293  0.14207  0.06566  614 SER B CA  
2160 C C   . SER A 337 ? 0.82257 0.65811 0.72374 0.04807  0.13589  0.05923  614 SER B C   
2161 O O   . SER A 337 ? 0.84133 0.66416 0.72997 0.04477  0.13405  0.05057  614 SER B O   
2162 C CB  . SER A 337 ? 0.76910 0.61286 0.70207 0.04757  0.13971  0.07106  614 SER B CB  
2163 O OG  . SER A 337 ? 0.86887 0.70740 0.80429 0.04240  0.13273  0.06743  614 SER B OG  
2164 N N   . ALA A 338 ? 0.75082 0.59909 0.65133 0.04757  0.13370  0.06357  615 ALA B N   
2165 C CA  . ALA A 338 ? 0.83645 0.69428 0.72287 0.04395  0.12810  0.05808  615 ALA B CA  
2166 C C   . ALA A 338 ? 0.83961 0.69393 0.72641 0.03237  0.12061  0.05115  615 ALA B C   
2167 O O   . ALA A 338 ? 0.88672 0.73675 0.75929 0.02425  0.11800  0.04103  615 ALA B O   
2168 C CB  . ALA A 338 ? 0.73427 0.61036 0.61915 0.05004  0.12826  0.06670  615 ALA B CB  
2169 N N   . LEU A 339 ? 0.79773 0.65231 0.69909 0.03011  0.11783  0.05596  616 LEU B N   
2170 C CA  . LEU A 339 ? 0.81895 0.67264 0.72116 0.01916  0.11135  0.05111  616 LEU B CA  
2171 C C   . LEU A 339 ? 0.72484 0.55321 0.62533 0.01526  0.11373  0.04570  616 LEU B C   
2172 O O   . LEU A 339 ? 0.74603 0.56774 0.64212 0.00446  0.11028  0.04074  616 LEU B O   
2173 C CB  . LEU A 339 ? 0.81730 0.68251 0.73358 0.02027  0.10769  0.05881  616 LEU B CB  
2174 C CG  . LEU A 339 ? 0.86030 0.74720 0.77264 0.02743  0.10693  0.06531  616 LEU B CG  
2175 C CD1 . LEU A 339 ? 0.88136 0.77814 0.80200 0.02934  0.10335  0.07164  616 LEU B CD1 
2176 C CD2 . LEU A 339 ? 0.79306 0.70012 0.69049 0.02287  0.10315  0.05935  616 LEU B CD2 
2177 N N   . MET A 340 ? 0.70794 0.52321 0.61005 0.02451  0.12052  0.04738  617 MET B N   
2178 C CA  . MET A 340 ? 0.77974 0.57192 0.67785 0.02679  0.12477  0.04480  617 MET B CA  
2179 C C   . MET A 340 ? 0.75560 0.54634 0.66494 0.02188  0.12094  0.04762  617 MET B C   
2180 O O   . MET A 340 ? 0.76269 0.53522 0.66143 0.01461  0.12087  0.04297  617 MET B O   
2181 C CB  . MET A 340 ? 0.71570 0.48353 0.58832 0.02204  0.12777  0.03429  617 MET B CB  
2182 C CG  . MET A 340 ? 0.80117 0.56904 0.66100 0.02992  0.13264  0.03130  617 MET B CG  
2183 S SD  . MET A 340 ? 0.78810 0.51802 0.61279 0.02819  0.13931  0.01784  617 MET B SD  
2184 C CE  . MET A 340 ? 0.74484 0.45044 0.56758 0.04793  0.15008  0.02387  617 MET B CE  
2185 N N   . PRO A 341 ? 0.70774 0.51596 0.63661 0.02499  0.11851  0.05502  618 PRO B N   
2186 C CA  . PRO A 341 ? 0.61083 0.41916 0.55028 0.02306  0.11561  0.05799  618 PRO B CA  
2187 C C   . PRO A 341 ? 0.66912 0.46170 0.60579 0.03162  0.12182  0.05877  618 PRO B C   
2188 O O   . PRO A 341 ? 0.73141 0.52213 0.66509 0.04163  0.12807  0.05949  618 PRO B O   
2189 C CB  . PRO A 341 ? 0.61023 0.43838 0.56732 0.02575  0.11344  0.06417  618 PRO B CB  
2190 C CG  . PRO A 341 ? 0.64782 0.48012 0.60474 0.03117  0.11875  0.06557  618 PRO B CG  
2191 C CD  . PRO A 341 ? 0.65230 0.47711 0.59183 0.03002  0.11979  0.06067  618 PRO B CD  
2192 N N   . ALA A 342 ? 0.61721 0.40006 0.55349 0.02950  0.12099  0.05980  619 ALA B N   
2193 C CA  . ALA A 342 ? 0.69237 0.45854 0.62220 0.04101  0.12830  0.06236  619 ALA B CA  
2194 C C   . ALA A 342 ? 0.65224 0.44293 0.60261 0.05036  0.12744  0.06961  619 ALA B C   
2195 O O   . ALA A 342 ? 0.65452 0.46262 0.61976 0.04428  0.12080  0.07163  619 ALA B O   
2196 C CB  . ALA A 342 ? 0.70455 0.44110 0.61766 0.03416  0.13051  0.06018  619 ALA B CB  
2197 N N   . GLN A 343 ? 0.64616 0.44059 0.59584 0.06571  0.13442  0.07324  620 GLN B N   
2198 C CA  . GLN A 343 ? 0.63823 0.45609 0.60278 0.07556  0.13470  0.07970  620 GLN B CA  
2199 C C   . GLN A 343 ? 0.69470 0.48978 0.64553 0.08533  0.14005  0.08370  620 GLN B C   
2200 O O   . GLN A 343 ? 0.71448 0.47926 0.64258 0.09522  0.14915  0.08371  620 GLN B O   
2201 C CB  . GLN A 343 ? 0.59020 0.43466 0.56254 0.08785  0.13962  0.08290  620 GLN B CB  
2202 C CG  . GLN A 343 ? 0.66253 0.54159 0.65243 0.09441  0.13820  0.08807  620 GLN B CG  
2203 C CD  . GLN A 343 ? 0.81862 0.73127 0.81529 0.10723  0.14393  0.09190  620 GLN B CD  
2204 O OE1 . GLN A 343 ? 0.80789 0.71113 0.78932 0.12465  0.15264  0.09526  620 GLN B OE1 
2205 N NE2 . GLN A 343 ? 0.81289 0.76533 0.83066 0.09817  0.13981  0.09114  620 GLN B NE2 
2206 N N   . LEU A 344 ? 0.66070 0.46746 0.62265 0.08348  0.13561  0.08743  621 LEU B N   
2207 C CA  . LEU A 344 ? 0.60991 0.39383 0.55883 0.09083  0.14080  0.09257  621 LEU B CA  
2208 C C   . LEU A 344 ? 0.63003 0.44698 0.59440 0.10432  0.14008  0.10032  621 LEU B C   
2209 O O   . LEU A 344 ? 0.67639 0.52695 0.66238 0.09681  0.13135  0.09907  621 LEU B O   
2210 C CB  . LEU A 344 ? 0.60139 0.36661 0.54622 0.07186  0.13562  0.08942  621 LEU B CB  
2211 C CG  . LEU A 344 ? 0.65582 0.39959 0.58790 0.05469  0.13395  0.08057  621 LEU B CG  
2212 C CD1 . LEU A 344 ? 0.67284 0.41829 0.60832 0.03597  0.12672  0.07874  621 LEU B CD1 
2213 C CD2 . LEU A 344 ? 0.66686 0.36532 0.56833 0.05966  0.14566  0.07826  621 LEU B CD2 
2214 N N   . PHE A 345 ? 0.66767 0.47402 0.61841 0.12474  0.14986  0.10817  622 PHE B N   
2215 C CA  . PHE A 345 ? 0.65886 0.49914 0.62150 0.14010  0.14991  0.11651  622 PHE B CA  
2216 C C   . PHE A 345 ? 0.71197 0.52865 0.66534 0.13989  0.15180  0.12199  622 PHE B C   
2217 O O   . PHE A 345 ? 0.76866 0.53927 0.69532 0.14687  0.16274  0.12604  622 PHE B O   
2218 C CB  . PHE A 345 ? 0.66693 0.52127 0.62094 0.16812  0.16048  0.12431  622 PHE B CB  
2219 C CG  . PHE A 345 ? 0.70054 0.59147 0.66858 0.16769  0.15808  0.12032  622 PHE B CG  
2220 C CD1 . PHE A 345 ? 0.73852 0.60436 0.69353 0.16495  0.16226  0.11542  622 PHE B CD1 
2221 C CD2 . PHE A 345 ? 0.63984 0.59061 0.63346 0.16713  0.15169  0.12054  622 PHE B CD2 
2222 C CE1 . PHE A 345 ? 0.76346 0.66360 0.73149 0.16359  0.16076  0.11274  622 PHE B CE1 
2223 C CE2 . PHE A 345 ? 0.60287 0.58714 0.60897 0.16285  0.15041  0.11685  622 PHE B CE2 
2224 C CZ  . PHE A 345 ? 0.65623 0.61548 0.65012 0.16172  0.15518  0.11379  622 PHE B CZ  
2225 N N   . PHE A 346 ? 0.64585 0.49183 0.61894 0.13185  0.14232  0.12221  623 PHE B N   
2226 C CA  . PHE A 346 ? 0.69039 0.51982 0.65692 0.13133  0.14376  0.12850  623 PHE B CA  
2227 C C   . PHE A 346 ? 0.68220 0.53272 0.64752 0.15754  0.15022  0.14025  623 PHE B C   
2228 O O   . PHE A 346 ? 0.63099 0.53281 0.61562 0.16567  0.14486  0.14025  623 PHE B O   
2229 C CB  . PHE A 346 ? 0.60090 0.45001 0.58616 0.11157  0.13101  0.12354  623 PHE B CB  
2230 C CG  . PHE A 346 ? 0.70767 0.53161 0.68787 0.08855  0.12688  0.11600  623 PHE B CG  
2231 C CD1 . PHE A 346 ? 0.76308 0.58432 0.74398 0.07946  0.12432  0.10763  623 PHE B CD1 
2232 C CD2 . PHE A 346 ? 0.71893 0.52646 0.69340 0.07625  0.12591  0.11792  623 PHE B CD2 
2233 C CE1 . PHE A 346 ? 0.79916 0.60426 0.77490 0.06024  0.12041  0.10125  623 PHE B CE1 
2234 C CE2 . PHE A 346 ? 0.74022 0.53442 0.71062 0.05507  0.12176  0.11110  623 PHE B CE2 
2235 C CZ  . PHE A 346 ? 0.72491 0.51901 0.69576 0.04794  0.11881  0.10272  623 PHE B CZ  
2236 N N   . LYS A 347 ? 0.79043 0.60377 0.73271 0.16918  0.16176  0.14985  624 LYS B N   
2237 C CA  . LYS A 347 ? 0.73804 0.56983 0.67595 0.19710  0.16929  0.16325  624 LYS B CA  
2238 C C   . LYS A 347 ? 0.72197 0.58633 0.67854 0.19165  0.16012  0.16569  624 LYS B C   
2239 O O   . LYS A 347 ? 0.82846 0.66782 0.78173 0.17492  0.15823  0.16535  624 LYS B O   
2240 C CB  . LYS A 347 ? 0.80858 0.57959 0.70941 0.21287  0.18780  0.17377  624 LYS B CB  
2241 C CG  . LYS A 347 ? 0.99214 0.73611 0.86992 0.22991  0.19992  0.17441  624 LYS B CG  
2242 C CD  . LYS A 347 ? 1.22699 0.89687 1.06173 0.24176  0.21977  0.18309  624 LYS B CD  
2243 C CE  . LYS A 347 ? 1.16626 0.78231 0.98889 0.20695  0.21880  0.17361  624 LYS B CE  
2244 N NZ  . LYS A 347 ? 1.17181 0.70784 0.94766 0.21410  0.23989  0.17949  624 LYS B NZ  
2245 N N   . THR A 348 ? 0.67798 0.60114 0.65342 0.20522  0.15456  0.16779  625 THR B N   
2246 C CA  . THR A 348 ? 0.70920 0.66635 0.70142 0.20111  0.14543  0.16879  625 THR B CA  
2247 C C   . THR A 348 ? 0.78387 0.73050 0.75955 0.22456  0.15666  0.18517  625 THR B C   
2248 O O   . THR A 348 ? 0.77797 0.70770 0.73291 0.24961  0.17076  0.19572  625 THR B O   
2249 C CB  . THR A 348 ? 0.69024 0.71462 0.70784 0.20139  0.13437  0.16157  625 THR B CB  
2250 O OG1 . THR A 348 ? 0.78452 0.84399 0.79862 0.23050  0.14178  0.17128  625 THR B OG1 
2251 C CG2 . THR A 348 ? 0.73891 0.76990 0.76848 0.18146  0.12704  0.14763  625 THR B CG2 
2252 N N   . GLU A 349 ? 0.75674 0.71244 0.73929 0.21869  0.15169  0.18812  626 GLU B N   
2253 C CA  . GLU A 349 ? 0.80475 0.75087 0.77143 0.24057  0.16289  0.20489  626 GLU B CA  
2254 C C   . GLU A 349 ? 0.78995 0.77971 0.75508 0.27535  0.16890  0.21506  626 GLU B C   
2255 O O   . GLU A 349 ? 0.71970 0.68956 0.66196 0.30195  0.18410  0.23177  626 GLU B O   
2256 C CB  . GLU A 349 ? 0.75730 0.72230 0.73687 0.22979  0.15422  0.20553  626 GLU B CB  
2257 C CG  . GLU A 349 ? 0.76997 0.80263 0.77685 0.22816  0.13878  0.19618  626 GLU B CG  
2258 C CD  . GLU A 349 ? 0.73321 0.78490 0.74893 0.22317  0.13183  0.19817  626 GLU B CD  
2259 O OE1 . GLU A 349 ? 0.89137 0.92175 0.89311 0.23314  0.14119  0.21242  626 GLU B OE1 
2260 N N   . ASP A 350 ? 0.76262 0.81345 0.75048 0.27531  0.15789  0.20556  627 ASP B N   
2261 C CA  . ASP A 350 ? 0.69696 0.80714 0.68836 0.30501  0.16077  0.21301  627 ASP B CA  
2262 C C   . ASP A 350 ? 0.75488 0.86431 0.73659 0.32010  0.16929  0.21466  627 ASP B C   
2263 O O   . ASP A 350 ? 0.82008 0.99283 0.81117 0.33847  0.16836  0.21664  627 ASP B O   
2264 C CB  . ASP A 350 ? 0.68684 0.87011 0.70806 0.29272  0.14388  0.20044  627 ASP B CB  
2265 C CG  . ASP A 350 ? 0.90938 1.09588 0.94755 0.26179  0.13249  0.18147  627 ASP B CG  
2266 O OD1 . ASP A 350 ? 0.91326 1.11037 0.95168 0.26550  0.13556  0.17903  627 ASP B OD1 
2267 O OD2 . ASP A 350 ? 1.09688 1.27355 1.14602 0.23547  0.12171  0.17015  627 ASP B OD2 
2268 N N   . GLY A 351 ? 0.81021 0.85364 0.77332 0.31198  0.17727  0.21321  628 GLY B N   
2269 C CA  . GLY A 351 ? 0.72321 0.75611 0.67043 0.33085  0.18830  0.21703  628 GLY B CA  
2270 C C   . GLY A 351 ? 0.74038 0.80392 0.70765 0.31297  0.17827  0.20219  628 GLY B C   
2271 O O   . GLY A 351 ? 0.81000 0.86814 0.76513 0.32811  0.18700  0.20494  628 GLY B O   
2272 N N   . GLY A 352 ? 0.75883 0.85218 0.75392 0.28246  0.16157  0.18723  629 GLY B N   
2273 C CA  . GLY A 352 ? 0.60408 0.72077 0.61623 0.26307  0.15338  0.17361  629 GLY B CA  
2274 C C   . GLY A 352 ? 0.69294 0.74741 0.69666 0.24006  0.15315  0.16507  629 GLY B C   
2275 O O   . GLY A 352 ? 0.71676 0.71065 0.70027 0.23829  0.15977  0.16891  629 GLY B O   
2276 N N   . LYS A 353 ? 0.68202 0.68711 0.80975 0.24439  0.16311  0.25290  630 LYS B N   
2277 C CA  . LYS A 353 ? 0.65589 0.62317 0.78883 0.22702  0.16494  0.22809  630 LYS B CA  
2278 C C   . LYS A 353 ? 0.65418 0.63832 0.76762 0.20429  0.14450  0.20698  630 LYS B C   
2279 O O   . LYS A 353 ? 0.72579 0.74978 0.82816 0.20362  0.12950  0.20426  630 LYS B O   
2280 C CB  . LYS A 353 ? 0.63567 0.59898 0.77922 0.23105  0.16979  0.21696  630 LYS B CB  
2281 C CG  . LYS A 353 ? 0.74116 0.68395 0.90074 0.24563  0.18954  0.22827  630 LYS B CG  
2282 C CD  . LYS A 353 ? 0.87822 0.81691 1.04689 0.24909  0.19403  0.21351  630 LYS B CD  
2283 C CE  . LYS A 353 ? 0.99165 0.98396 1.16021 0.26399  0.18481  0.22350  630 LYS B CE  
2284 N NZ  . LYS A 353 ? 1.09274 1.09558 1.26802 0.28228  0.19526  0.24587  630 LYS B NZ  
2285 N N   . TYR A 354 ? 0.58245 0.53704 0.69336 0.18566  0.14437  0.19177  631 TYR B N   
2286 C CA  . TYR A 354 ? 0.60495 0.57016 0.69891 0.16540  0.12693  0.17191  631 TYR B CA  
2287 C C   . TYR A 354 ? 0.64177 0.58062 0.73831 0.14857  0.12691  0.14736  631 TYR B C   
2288 O O   . TYR A 354 ? 0.61453 0.52076 0.71997 0.14062  0.13578  0.14075  631 TYR B O   
2289 C CB  . TYR A 354 ? 0.49503 0.45741 0.58163 0.15990  0.12487  0.17705  631 TYR B CB  
2290 C CG  . TYR A 354 ? 0.55972 0.53711 0.62813 0.14436  0.10783  0.16151  631 TYR B CG  
2291 C CD1 . TYR A 354 ? 0.58517 0.54617 0.65087 0.12639  0.10169  0.13955  631 TYR B CD1 
2292 C CD2 . TYR A 354 ? 0.64612 0.65322 0.69954 0.14848  0.09888  0.16899  631 TYR B CD2 
2293 C CE1 . TYR A 354 ? 0.63748 0.60842 0.68787 0.11435  0.08819  0.12769  631 TYR B CE1 
2294 C CE2 . TYR A 354 ? 0.67232 0.68786 0.70992 0.13476  0.08543  0.15367  631 TYR B CE2 
2295 C CZ  . TYR A 354 ? 0.63002 0.62584 0.66717 0.11845  0.08078  0.13427  631 TYR B CZ  
2296 O OH  . TYR A 354 ? 0.63096 0.63188 0.65374 0.10700  0.06928  0.12124  631 TYR B OH  
2297 N N   . PRO A 355 ? 0.59629 0.54985 0.68595 0.14252  0.11795  0.13360  632 PRO B N   
2298 C CA  . PRO A 355 ? 0.57168 0.50407 0.66050 0.12792  0.11800  0.11130  632 PRO B CA  
2299 C C   . PRO A 355 ? 0.54824 0.47723 0.62382 0.10937  0.10577  0.09735  632 PRO B C   
2300 O O   . PRO A 355 ? 0.60113 0.55099 0.66386 0.10529  0.09340  0.09845  632 PRO B O   
2301 C CB  . PRO A 355 ? 0.61651 0.57151 0.70253 0.13074  0.11414  0.10642  632 PRO B CB  
2302 C CG  . PRO A 355 ? 0.55962 0.55213 0.63909 0.13638  0.10353  0.11863  632 PRO B CG  
2303 C CD  . PRO A 355 ? 0.61114 0.60365 0.69544 0.14964  0.10907  0.13889  632 PRO B CD  
2304 N N   . VAL A 356 ? 0.59572 0.49886 0.67514 0.09828  0.10958  0.08328  633 VAL B N   
2305 C CA  . VAL A 356 ? 0.56688 0.46813 0.63585 0.08224  0.09857  0.07022  633 VAL B CA  
2306 C C   . VAL A 356 ? 0.58156 0.47160 0.64765 0.07167  0.09828  0.05014  633 VAL B C   
2307 O O   . VAL A 356 ? 0.53021 0.40709 0.60468 0.07530  0.10903  0.04429  633 VAL B O   
2308 C CB  . VAL A 356 ? 0.59561 0.48378 0.67283 0.07795  0.10175  0.07392  633 VAL B CB  
2309 C CG1 . VAL A 356 ? 0.52815 0.42669 0.60753 0.09013  0.10507  0.09518  633 VAL B CG1 
2310 C CG2 . VAL A 356 ? 0.58668 0.44654 0.68144 0.07343  0.11502  0.06547  633 VAL B CG2 
2311 N N   . ILE A 357 ? 0.57447 0.47037 0.62769 0.05959  0.08638  0.03976  634 ILE B N   
2312 C CA  . ILE A 357 ? 0.54032 0.42810 0.58928 0.04834  0.08452  0.02115  634 ILE B CA  
2313 C C   . ILE A 357 ? 0.53958 0.41910 0.59601 0.03942  0.08258  0.01642  634 ILE B C   
2314 O O   . ILE A 357 ? 0.55091 0.43931 0.60416 0.03837  0.07510  0.02401  634 ILE B O   
2315 C CB  . ILE A 357 ? 0.61924 0.52259 0.64862 0.04247  0.07291  0.01548  634 ILE B CB  
2316 C CG1 . ILE A 357 ? 0.65264 0.56805 0.67763 0.04954  0.07533  0.02055  634 ILE B CG1 
2317 C CG2 . ILE A 357 ? 0.50913 0.40853 0.53168 0.03210  0.07023  -0.00242 634 ILE B CG2 
2318 C CD1 . ILE A 357 ? 0.62168 0.55256 0.63018 0.04401  0.06502  0.02118  634 ILE B CD1 
2319 N N   . PHE A 358 ? 0.57568 0.43946 0.64318 0.03256  0.08977  0.00293  635 PHE B N   
2320 C CA  . PHE A 358 ? 0.53956 0.40140 0.61561 0.02078  0.08634  -0.00516 635 PHE B CA  
2321 C C   . PHE A 358 ? 0.54789 0.41960 0.61152 0.00964  0.07651  -0.02471 635 PHE B C   
2322 O O   . PHE A 358 ? 0.59068 0.45571 0.65081 0.00712  0.08122  -0.03940 635 PHE B O   
2323 C CB  . PHE A 358 ? 0.53941 0.37847 0.63967 0.01777  0.10120  -0.00748 635 PHE B CB  
2324 C CG  . PHE A 358 ? 0.57195 0.41387 0.68504 0.00462  0.09792  -0.01399 635 PHE B CG  
2325 C CD1 . PHE A 358 ? 0.58372 0.43963 0.69788 0.00673  0.09198  0.00053  635 PHE B CD1 
2326 C CD2 . PHE A 358 ? 0.55920 0.39384 0.68293 -0.01031 0.10001  -0.03611 635 PHE B CD2 
2327 C CE1 . PHE A 358 ? 0.55746 0.42103 0.68549 -0.00464 0.08903  -0.00461 635 PHE B CE1 
2328 C CE2 . PHE A 358 ? 0.59448 0.43825 0.73290 -0.02378 0.09585  -0.04268 635 PHE B CE2 
2329 C CZ  . PHE A 358 ? 0.60337 0.46238 0.74499 -0.02044 0.09059  -0.02590 635 PHE B CZ  
2330 N N   . LYS A 359 ? 0.56029 0.44928 0.61625 0.00468  0.06348  -0.02412 636 LYS B N   
2331 C CA  . LYS A 359 ? 0.55615 0.46026 0.59868 -0.00368 0.05253  -0.03860 636 LYS B CA  
2332 C C   . LYS A 359 ? 0.59649 0.50756 0.65403 -0.01519 0.04877  -0.04894 636 LYS B C   
2333 O O   . LYS A 359 ? 0.65089 0.56500 0.72154 -0.01477 0.04821  -0.03859 636 LYS B O   
2334 C CB  . LYS A 359 ? 0.63191 0.55254 0.65436 0.00113  0.04058  -0.02819 636 LYS B CB  
2335 C CG  . LYS A 359 ? 0.70770 0.62592 0.71734 0.00998  0.04296  -0.01749 636 LYS B CG  
2336 C CD  . LYS A 359 ? 0.77011 0.70157 0.75965 0.01087  0.03233  -0.01182 636 LYS B CD  
2337 C CE  . LYS A 359 ? 0.79892 0.72966 0.77839 0.01650  0.03482  -0.00226 636 LYS B CE  
2338 N N   . HIS A 360 ? 0.56288 0.47933 0.61885 -0.02577 0.04640  -0.07011 637 HIS B N   
2339 C CA  . HIS A 360 ? 0.58301 0.51384 0.65284 -0.03916 0.04040  -0.08377 637 HIS B CA  
2340 C C   . HIS A 360 ? 0.67359 0.63294 0.72260 -0.04273 0.02527  -0.09450 637 HIS B C   
2341 O O   . HIS A 360 ? 0.69229 0.65199 0.72072 -0.04056 0.02502  -0.10210 637 HIS B O   
2342 C CB  . HIS A 360 ? 0.57980 0.49146 0.67061 -0.05142 0.05271  -0.10324 637 HIS B CB  
2343 C CG  . HIS A 360 ? 0.72753 0.65744 0.83563 -0.06845 0.04627  -0.12013 637 HIS B CG  
2344 N ND1 . HIS A 360 ? 0.74496 0.69183 0.86934 -0.07069 0.04077  -0.10908 637 HIS B ND1 
2345 C CD2 . HIS A 360 ? 0.74045 0.67838 0.85262 -0.08453 0.04396  -0.14841 637 HIS B CD2 
2346 C CE1 . HIS A 360 ? 0.71398 0.68043 0.85407 -0.08763 0.03508  -0.12860 637 HIS B CE1 
2347 N NE2 . HIS A 360 ? 0.81294 0.77444 0.94561 -0.09709 0.03637  -0.15359 637 HIS B NE2 
2348 N N   . GLY A 361 ? 0.68174 0.66741 0.73627 -0.04704 0.01333  -0.09394 638 GLY B N   
2349 C CA  . GLY A 361 ? 0.55498 0.57207 0.58936 -0.04729 -0.00184 -0.09929 638 GLY B CA  
2350 C C   . GLY A 361 ? 0.67901 0.70221 0.69119 -0.03245 -0.00842 -0.07757 638 GLY B C   
2351 O O   . GLY A 361 ? 0.73694 0.77635 0.72570 -0.02941 -0.01617 -0.07877 638 GLY B O   
2352 N N   . ASP A 362 ? 0.67608 0.68679 0.69476 -0.02343 -0.00485 -0.05793 639 ASP B N   
2353 C CA  . ASP A 362 ? 0.65876 0.66861 0.65856 -0.01084 -0.00857 -0.03904 639 ASP B CA  
2354 C C   . ASP A 362 ? 0.64408 0.65254 0.65692 -0.00426 -0.00864 -0.02367 639 ASP B C   
2355 O O   . ASP A 362 ? 0.65412 0.65211 0.68686 -0.00685 -0.00094 -0.02321 639 ASP B O   
2356 C CB  . ASP A 362 ? 0.85724 0.84427 0.84482 -0.00621 0.00065  -0.03440 639 ASP B CB  
2357 C CG  . ASP A 362 ? 0.92851 0.91853 0.89248 0.00148  -0.00355 -0.02246 639 ASP B CG  
2358 O OD1 . ASP A 362 ? 0.99522 1.00428 0.94880 0.00374  -0.01330 -0.01915 639 ASP B OD1 
2359 O OD2 . ASP A 362 ? 1.07486 1.04960 1.03204 0.00533  0.00328  -0.01557 639 ASP B OD2 
2360 N N   . ASP A 363 ? 0.56478 0.58286 0.56620 0.00503  -0.01588 -0.01065 640 ASP B N   
2361 C CA  . ASP A 363 ? 0.58158 0.59779 0.59274 0.01301  -0.01508 0.00281  640 ASP B CA  
2362 C C   . ASP A 363 ? 0.52137 0.51344 0.52016 0.02037  -0.00865 0.01404  640 ASP B C   
2363 O O   . ASP A 363 ? 0.65185 0.63978 0.63223 0.02599  -0.01129 0.02143  640 ASP B O   
2364 C CB  . ASP A 363 ? 0.49402 0.53396 0.50271 0.02020  -0.02537 0.00991  640 ASP B CB  
2365 C CG  . ASP A 363 ? 0.62960 0.67062 0.65255 0.02845  -0.02323 0.02084  640 ASP B CG  
2366 O OD1 . ASP A 363 ? 0.62829 0.64811 0.65370 0.03130  -0.01436 0.02621  640 ASP B OD1 
2367 O OD2 . ASP A 363 ? 0.70108 0.76746 0.73282 0.03294  -0.03039 0.02399  640 ASP B OD2 
2368 N N   . LEU A 364 ? 0.56940 0.54702 0.57876 0.01999  0.00005  0.01566  641 LEU B N   
2369 C CA  . LEU A 364 ? 0.57702 0.53707 0.57610 0.02539  0.00533  0.02377  641 LEU B CA  
2370 C C   . LEU A 364 ? 0.54831 0.50546 0.54339 0.03405  0.00431  0.03409  641 LEU B C   
2371 O O   . LEU A 364 ? 0.55784 0.50242 0.54460 0.03711  0.00798  0.03855  641 LEU B O   
2372 C CB  . LEU A 364 ? 0.48144 0.43124 0.49228 0.02372  0.01481  0.02305  641 LEU B CB  
2373 C CG  . LEU A 364 ? 0.58423 0.52682 0.59238 0.01933  0.01933  0.01582  641 LEU B CG  
2374 C CD1 . LEU A 364 ? 0.66398 0.61525 0.67013 0.01226  0.01493  0.00359  641 LEU B CD1 
2375 C CD2 . LEU A 364 ? 0.55337 0.48688 0.57823 0.01932  0.02960  0.01674  641 LEU B CD2 
2376 N N   . ARG A 365 ? 0.53934 0.50910 0.54089 0.03823  -0.00022 0.03695  642 ARG B N   
2377 C CA  . ARG A 365 ? 0.53168 0.49676 0.53340 0.04749  0.00207  0.04508  642 ARG B CA  
2378 C C   . ARG A 365 ? 0.53469 0.48387 0.51709 0.05285  0.00156  0.05049  642 ARG B C   
2379 O O   . ARG A 365 ? 0.57438 0.51135 0.55283 0.05740  0.00612  0.05311  642 ARG B O   
2380 C CB  . ARG A 365 ? 0.56333 0.54826 0.57945 0.05220  -0.00149 0.04745  642 ARG B CB  
2381 C CG  . ARG A 365 ? 0.57278 0.56886 0.61204 0.04745  0.00355  0.04452  642 ARG B CG  
2382 C CD  . ARG A 365 ? 0.53940 0.56078 0.59635 0.05051  -0.00013 0.04616  642 ARG B CD  
2383 N NE  . ARG A 365 ? 0.60235 0.64382 0.66007 0.04610  -0.01054 0.04078  642 ARG B NE  
2384 C CZ  . ARG A 365 ? 0.61463 0.68609 0.68736 0.04822  -0.01702 0.04130  642 ARG B CZ  
2385 N NH1 . ARG A 365 ? 0.56857 0.65228 0.65837 0.05519  -0.01317 0.04755  642 ARG B NH1 
2386 N NH2 . ARG A 365 ? 0.60196 0.69524 0.67246 0.04372  -0.02764 0.03531  642 ARG B NH2 
2387 N N   . GLN A 366 ? 0.58073 0.52933 0.55052 0.05157  -0.00289 0.05166  643 GLN B N   
2388 C CA  . GLN A 366 ? 0.55731 0.48734 0.51119 0.05485  -0.00095 0.05764  643 GLN B CA  
2389 C C   . GLN A 366 ? 0.57921 0.49584 0.52807 0.04819  0.00424  0.05364  643 GLN B C   
2390 O O   . GLN A 366 ? 0.60575 0.50781 0.54946 0.04979  0.00793  0.05473  643 GLN B O   
2391 C CB  . GLN A 366 ? 0.52867 0.46175 0.46973 0.05581  -0.00520 0.06298  643 GLN B CB  
2392 C CG  . GLN A 366 ? 0.48760 0.39789 0.41443 0.05849  -0.00091 0.07111  643 GLN B CG  
2393 C CD  . GLN A 366 ? 0.62419 0.53808 0.53951 0.06477  -0.00395 0.08231  643 GLN B CD  
2394 O OE1 . GLN A 366 ? 0.65875 0.58455 0.57764 0.07537  -0.00821 0.08929  643 GLN B OE1 
2395 N NE2 . GLN A 366 ? 0.58016 0.48689 0.48199 0.05922  -0.00137 0.08552  643 GLN B NE2 
2396 N N   . ASP A 367 ? 0.50322 0.42632 0.45492 0.04105  0.00486  0.04794  644 ASP B N   
2397 C CA  . ASP A 367 ? 0.53513 0.45202 0.48558 0.03668  0.00948  0.04532  644 ASP B CA  
2398 C C   . ASP A 367 ? 0.51921 0.43525 0.47677 0.04024  0.01274  0.04537  644 ASP B C   
2399 O O   . ASP A 367 ? 0.54499 0.45533 0.49694 0.03941  0.01484  0.04483  644 ASP B O   
2400 C CB  . ASP A 367 ? 0.52096 0.44532 0.47566 0.03145  0.01102  0.04003  644 ASP B CB  
2401 C CG  . ASP A 367 ? 0.72875 0.65435 0.67161 0.02761  0.00963  0.03940  644 ASP B CG  
2402 O OD1 . ASP A 367 ? 0.66636 0.58671 0.60167 0.02455  0.01242  0.04139  644 ASP B OD1 
2403 O OD2 . ASP A 367 ? 0.82140 0.75593 0.76242 0.02737  0.00570  0.03693  644 ASP B OD2 
2404 N N   . GLN A 368 ? 0.51344 0.43754 0.48331 0.04359  0.01340  0.04571  645 GLN B N   
2405 C CA  . GLN A 368 ? 0.47141 0.39711 0.44682 0.04822  0.01776  0.04762  645 GLN B CA  
2406 C C   . GLN A 368 ? 0.54324 0.46019 0.50850 0.05321  0.01811  0.04824  645 GLN B C   
2407 O O   . GLN A 368 ? 0.49314 0.40905 0.45336 0.05431  0.02099  0.04676  645 GLN B O   
2408 C CB  . GLN A 368 ? 0.50055 0.43668 0.49234 0.05020  0.01939  0.04907  645 GLN B CB  
2409 C CG  . GLN A 368 ? 0.47692 0.41704 0.47501 0.05553  0.02571  0.05316  645 GLN B CG  
2410 C CD  . GLN A 368 ? 0.52824 0.47950 0.54593 0.05519  0.02876  0.05518  645 GLN B CD  
2411 O OE1 . GLN A 368 ? 0.50818 0.46140 0.53776 0.05231  0.03472  0.05719  645 GLN B OE1 
2412 N NE2 . GLN A 368 ? 0.50959 0.46883 0.53270 0.05812  0.02531  0.05527  645 GLN B NE2 
2413 N N   . LEU A 369 ? 0.51742 0.42840 0.47908 0.05690  0.01557  0.05006  646 LEU B N   
2414 C CA  . LEU A 369 ? 0.50837 0.40571 0.46125 0.06235  0.01799  0.04961  646 LEU B CA  
2415 C C   . LEU A 369 ? 0.52575 0.40898 0.46605 0.05540  0.01890  0.04513  646 LEU B C   
2416 O O   . LEU A 369 ? 0.58887 0.46627 0.52330 0.05551  0.02189  0.03954  646 LEU B O   
2417 C CB  . LEU A 369 ? 0.54736 0.44044 0.50065 0.07001  0.01628  0.05507  646 LEU B CB  
2418 C CG  . LEU A 369 ? 0.59853 0.46897 0.54154 0.07555  0.02055  0.05475  646 LEU B CG  
2419 C CD1 . LEU A 369 ? 0.51016 0.37805 0.45333 0.08202  0.02646  0.04928  646 LEU B CD1 
2420 C CD2 . LEU A 369 ? 0.56428 0.43054 0.50780 0.08495  0.01919  0.06396  646 LEU B CD2 
2421 N N   . ILE A 370 ? 0.53023 0.41041 0.46659 0.04843  0.01666  0.04649  647 ILE B N   
2422 C CA  . ILE A 370 ? 0.53259 0.40148 0.46028 0.03996  0.01827  0.04272  647 ILE B CA  
2423 C C   . ILE A 370 ? 0.58744 0.46844 0.51670 0.03510  0.01864  0.03644  647 ILE B C   
2424 O O   . ILE A 370 ? 0.59683 0.47261 0.52048 0.03073  0.02001  0.02956  647 ILE B O   
2425 C CB  . ILE A 370 ? 0.57421 0.44191 0.49845 0.03395  0.01713  0.04709  647 ILE B CB  
2426 C CG1 . ILE A 370 ? 0.58737 0.44264 0.50628 0.03982  0.01719  0.05532  647 ILE B CG1 
2427 C CG2 . ILE A 370 ? 0.54943 0.41311 0.46981 0.02287  0.01948  0.04300  647 ILE B CG2 
2428 C CD1 . ILE A 370 ? 0.66905 0.49994 0.58291 0.04295  0.02208  0.05545  647 ILE B CD1 
2429 N N   . LEU A 371 ? 0.54484 0.44296 0.48212 0.03596  0.01769  0.03853  648 LEU B N   
2430 C CA  . LEU A 371 ? 0.59263 0.50531 0.53193 0.03461  0.01832  0.03608  648 LEU B CA  
2431 C C   . LEU A 371 ? 0.57508 0.49168 0.51146 0.04072  0.01985  0.03375  648 LEU B C   
2432 O O   . LEU A 371 ? 0.53812 0.46510 0.46980 0.03866  0.01930  0.02920  648 LEU B O   
2433 C CB  . LEU A 371 ? 0.44061 0.36620 0.39014 0.03656  0.01937  0.04063  648 LEU B CB  
2434 C CG  . LEU A 371 ? 0.57904 0.50916 0.52961 0.03029  0.01924  0.04004  648 LEU B CG  
2435 C CD1 . LEU A 371 ? 0.52384 0.46480 0.47178 0.02519  0.01845  0.03677  648 LEU B CD1 
2436 C CD2 . LEU A 371 ? 0.58251 0.50033 0.52731 0.02584  0.01797  0.03983  648 LEU B CD2 
2437 N N   . GLN A 372 ? 0.51813 0.43013 0.45699 0.04835  0.02176  0.03642  649 GLN B N   
2438 C CA  . GLN A 372 ? 0.59326 0.50867 0.52727 0.05486  0.02474  0.03364  649 GLN B CA  
2439 C C   . GLN A 372 ? 0.61254 0.51441 0.53377 0.05109  0.02484  0.02300  649 GLN B C   
2440 O O   . GLN A 372 ? 0.63242 0.54299 0.54532 0.05054  0.02528  0.01557  649 GLN B O   
2441 C CB  . GLN A 372 ? 0.48428 0.39901 0.42602 0.06372  0.02784  0.03885  649 GLN B CB  
2442 C CG  . GLN A 372 ? 0.59695 0.52061 0.53581 0.07202  0.03301  0.03845  649 GLN B CG  
2443 C CD  . GLN A 372 ? 0.70701 0.61803 0.64159 0.07892  0.03616  0.03424  649 GLN B CD  
2444 O OE1 . GLN A 372 ? 0.66902 0.56288 0.60225 0.07770  0.03435  0.03261  649 GLN B OE1 
2445 N NE2 . GLN A 372 ? 0.73634 0.65596 0.66883 0.08766  0.04213  0.03382  649 GLN B NE2 
2446 N N   . ILE A 373 ? 0.58949 0.47025 0.50876 0.04810  0.02487  0.02196  650 ILE B N   
2447 C CA  . ILE A 373 ? 0.62115 0.48232 0.53050 0.04308  0.02714  0.01157  650 ILE B CA  
2448 C C   . ILE A 373 ? 0.67506 0.54419 0.58104 0.02970  0.02435  0.00332  650 ILE B C   
2449 O O   . ILE A 373 ? 0.69245 0.56060 0.59060 0.02446  0.02507  -0.00975 650 ILE B O   
2450 C CB  . ILE A 373 ? 0.65327 0.48846 0.56266 0.04425  0.02951  0.01640  650 ILE B CB  
2451 C CG1 . ILE A 373 ? 0.67672 0.50914 0.59069 0.05892  0.03180  0.02372  650 ILE B CG1 
2452 C CG2 . ILE A 373 ? 0.72006 0.52939 0.62122 0.03723  0.03414  0.00571  650 ILE B CG2 
2453 C CD1 . ILE A 373 ? 0.71688 0.54688 0.62643 0.06729  0.03706  0.01570  650 ILE B CD1 
2454 N N   . ILE A 374 ? 0.65118 0.53091 0.56361 0.02370  0.02126  0.00946  651 ILE B N   
2455 C CA  . ILE A 374 ? 0.60406 0.49703 0.51664 0.01156  0.01871  0.00262  651 ILE B CA  
2456 C C   . ILE A 374 ? 0.60332 0.52352 0.51340 0.01431  0.01587  -0.00243 651 ILE B C   
2457 O O   . ILE A 374 ? 0.63287 0.56311 0.53846 0.00544  0.01362  -0.01439 651 ILE B O   
2458 C CB  . ILE A 374 ? 0.55632 0.45842 0.47703 0.00720  0.01736  0.01093  651 ILE B CB  
2459 C CG1 . ILE A 374 ? 0.62592 0.50364 0.54531 0.00307  0.02040  0.01545  651 ILE B CG1 
2460 C CG2 . ILE A 374 ? 0.56428 0.48935 0.48882 -0.00279 0.01467  0.00540  651 ILE B CG2 
2461 C CD1 . ILE A 374 ? 0.58123 0.46945 0.50616 0.00058  0.01999  0.02347  651 ILE B CD1 
2462 N N   . SER A 375 ? 0.57990 0.51388 0.49302 0.02629  0.01625  0.00678  652 SER B N   
2463 C CA  . SER A 375 ? 0.60183 0.56173 0.51054 0.03192  0.01494  0.00566  652 SER B CA  
2464 C C   . SER A 375 ? 0.61613 0.57141 0.51111 0.03143  0.01591  -0.00831 652 SER B C   
2465 O O   . SER A 375 ? 0.67299 0.64876 0.56024 0.02688  0.01231  -0.01839 652 SER B O   
2466 C CB  . SER A 375 ? 0.55893 0.52726 0.47420 0.04495  0.01827  0.01979  652 SER B CB  
2467 O OG  . SER A 375 ? 0.63302 0.62589 0.54214 0.05249  0.01864  0.02183  652 SER B OG  
2468 N N   . LEU A 376 ? 0.66653 0.59678 0.55830 0.03642  0.02082  -0.01017 653 LEU B N   
2469 C CA  . LEU A 376 ? 0.67101 0.59291 0.54941 0.03708  0.02377  -0.02522 653 LEU B CA  
2470 C C   . LEU A 376 ? 0.67877 0.59272 0.55176 0.02096  0.02143  -0.04292 653 LEU B C   
2471 O O   . LEU A 376 ? 0.65281 0.58257 0.51495 0.01640  0.01924  -0.05807 653 LEU B O   
2472 C CB  . LEU A 376 ? 0.68877 0.58282 0.56789 0.04615  0.03055  -0.02298 653 LEU B CB  
2473 C CG  . LEU A 376 ? 0.69236 0.56681 0.55912 0.04727  0.03624  -0.03977 653 LEU B CG  
2474 C CD1 . LEU A 376 ? 0.72995 0.62724 0.58541 0.05664  0.03847  -0.04472 653 LEU B CD1 
2475 C CD2 . LEU A 376 ? 0.73453 0.57857 0.60680 0.05611  0.04278  -0.03388 653 LEU B CD2 
2476 N N   . MET A 377 ? 0.69933 0.59030 0.57985 0.01136  0.02225  -0.04153 654 MET B N   
2477 C CA  . MET A 377 ? 0.69375 0.57436 0.57256 -0.00631 0.02196  -0.05771 654 MET B CA  
2478 C C   . MET A 377 ? 0.73202 0.65163 0.61218 -0.01638 0.01404  -0.06452 654 MET B C   
2479 O O   . MET A 377 ? 0.78283 0.70878 0.65722 -0.02891 0.01212  -0.08423 654 MET B O   
2480 C CB  . MET A 377 ? 0.70973 0.56263 0.59745 -0.01393 0.02544  -0.05014 654 MET B CB  
2481 C CG  . MET A 377 ? 0.75006 0.56269 0.63538 -0.00533 0.03367  -0.04595 654 MET B CG  
2482 S SD  . MET A 377 ? 0.83241 0.62206 0.72644 -0.00990 0.03689  -0.02969 654 MET B SD  
2483 C CE  . MET A 377 ? 0.68538 0.43070 0.57531 0.00276  0.04681  -0.02527 654 MET B CE  
2484 N N   . ASP A 378 ? 0.61683 0.56468 0.50515 -0.01051 0.00954  -0.04917 655 ASP B N   
2485 C CA  . ASP A 378 ? 0.67163 0.66166 0.56228 -0.01582 0.00209  -0.05265 655 ASP B CA  
2486 C C   . ASP A 378 ? 0.75636 0.77108 0.63230 -0.01087 -0.00114 -0.06389 655 ASP B C   
2487 O O   . ASP A 378 ? 0.73286 0.77369 0.60537 -0.02221 -0.00725 -0.07938 655 ASP B O   
2488 C CB  . ASP A 378 ? 0.63211 0.64417 0.53394 -0.00611 0.00026  -0.03262 655 ASP B CB  
2489 C CG  . ASP A 378 ? 0.70241 0.76153 0.60809 -0.00764 -0.00698 -0.03296 655 ASP B CG  
2490 O OD1 . ASP A 378 ? 0.71356 0.78602 0.62418 -0.02360 -0.01105 -0.04513 655 ASP B OD1 
2491 O OD2 . ASP A 378 ? 0.74930 0.83341 0.65435 0.00723  -0.00809 -0.02028 655 ASP B OD2 
2492 N N   . LYS A 379 ? 0.72052 0.73042 0.58761 0.00544  0.00300  -0.05685 656 LYS B N   
2493 C CA  . LYS A 379 ? 0.71184 0.74622 0.56206 0.01178  0.00140  -0.06635 656 LYS B CA  
2494 C C   . LYS A 379 ? 0.75125 0.76865 0.58848 0.00004  0.00282  -0.09376 656 LYS B C   
2495 O O   . LYS A 379 ? 0.79881 0.84558 0.62394 -0.00571 -0.00276 -0.11055 656 LYS B O   
2496 C CB  . LYS A 379 ? 0.65315 0.68529 0.49871 0.03150  0.00783  -0.05113 656 LYS B CB  
2497 C CG  . LYS A 379 ? 0.72488 0.77966 0.58108 0.04335  0.00731  -0.02646 656 LYS B CG  
2498 C CD  . LYS A 379 ? 0.78605 0.82625 0.64555 0.05813  0.01593  -0.01080 656 LYS B CD  
2499 C CE  . LYS A 379 ? 0.72633 0.77745 0.60089 0.06663  0.01761  0.01232  656 LYS B CE  
2500 N NZ  . LYS A 379 ? 0.91151 1.00081 0.77981 0.07692  0.01666  0.02287  656 LYS B NZ  
2501 N N   . LEU A 380 ? 0.77503 0.74588 0.61416 -0.00301 0.01064  -0.09916 657 LEU B N   
2502 C CA  . LEU A 380 ? 0.81705 0.76495 0.64544 -0.01425 0.01440  -0.12605 657 LEU B CA  
2503 C C   . LEU A 380 ? 0.82340 0.78840 0.65523 -0.03714 0.00722  -0.14485 657 LEU B C   
2504 O O   . LEU A 380 ? 0.85487 0.83503 0.67385 -0.04616 0.00434  -0.16954 657 LEU B O   
2505 C CB  . LEU A 380 ? 0.81924 0.71237 0.65317 -0.01328 0.02485  -0.12452 657 LEU B CB  
2506 C CG  . LEU A 380 ? 0.85024 0.72841 0.68287 0.00843  0.03203  -0.10872 657 LEU B CG  
2507 C CD1 . LEU A 380 ? 0.75471 0.58462 0.59530 0.01089  0.04088  -0.10326 657 LEU B CD1 
2508 C CD2 . LEU A 380 ? 0.87042 0.75927 0.68500 0.01858  0.03578  -0.12203 657 LEU B CD2 
2509 N N   . LEU A 381 ? 0.78942 0.75587 0.63902 -0.04716 0.00430  -0.13415 658 LEU B N   
2510 C CA  . LEU A 381 ? 0.83911 0.82626 0.69692 -0.06986 -0.00208 -0.14980 658 LEU B CA  
2511 C C   . LEU A 381 ? 0.83934 0.88781 0.69061 -0.06925 -0.01387 -0.15603 658 LEU B C   
2512 O O   . LEU A 381 ? 0.75089 0.82089 0.59918 -0.08690 -0.01964 -0.18075 658 LEU B O   
2513 C CB  . LEU A 381 ? 0.79199 0.77427 0.67033 -0.07694 -0.00173 -0.13290 658 LEU B CB  
2514 C CG  . LEU A 381 ? 0.83756 0.76328 0.72230 -0.08240 0.00934  -0.12908 658 LEU B CG  
2515 C CD1 . LEU A 381 ? 0.73524 0.66127 0.63513 -0.08104 0.01002  -0.10618 658 LEU B CD1 
2516 C CD2 . LEU A 381 ? 0.81255 0.71678 0.70041 -0.10712 0.01341  -0.15393 658 LEU B CD2 
2517 N N   . ARG A 382 ? 0.79244 0.87092 0.64195 -0.04924 -0.01735 -0.13378 659 ARG B N   
2518 C CA  . ARG A 382 ? 0.75808 0.89634 0.59988 -0.04484 -0.02779 -0.13571 659 ARG B CA  
2519 C C   . ARG A 382 ? 0.87218 1.01988 0.68919 -0.04288 -0.02843 -0.15731 659 ARG B C   
2520 O O   . ARG A 382 ? 0.92414 1.11501 0.73305 -0.05227 -0.03801 -0.17559 659 ARG B O   
2521 C CB  . ARG A 382 ? 0.74904 0.91089 0.59482 -0.02226 -0.02842 -0.10482 659 ARG B CB  
2522 C CG  . ARG A 382 ? 0.71012 0.87735 0.57873 -0.02312 -0.02944 -0.08590 659 ARG B CG  
2523 C CD  . ARG A 382 ? 0.75270 0.91995 0.62337 0.00011  -0.02474 -0.05773 659 ARG B CD  
2524 N NE  . ARG A 382 ? 0.82038 0.99314 0.71101 0.00260  -0.02437 -0.03970 659 ARG B NE  
2525 C CZ  . ARG A 382 ? 0.90587 1.12329 0.80531 0.00817  -0.03009 -0.02943 659 ARG B CZ  
2526 N NH1 . ARG A 382 ? 0.87000 1.13486 0.76003 0.01133  -0.03827 -0.03442 659 ARG B NH1 
2527 N NH2 . ARG A 382 ? 0.88900 1.10534 0.80665 0.01203  -0.02726 -0.01356 659 ARG B NH2 
2528 N N   . LYS A 383 ? 0.86182 0.97304 0.66639 -0.03055 -0.01835 -0.15648 660 LYS B N   
2529 C CA  . LYS A 383 ? 0.91170 1.02646 0.69181 -0.02954 -0.01660 -0.18048 660 LYS B CA  
2530 C C   . LYS A 383 ? 0.93127 1.04191 0.70879 -0.05567 -0.02001 -0.21666 660 LYS B C   
2531 O O   . LYS A 383 ? 1.06244 1.19936 0.81995 -0.05985 -0.02421 -0.24119 660 LYS B O   
2532 C CB  . LYS A 383 ? 0.92297 0.99023 0.69539 -0.01546 -0.00287 -0.17709 660 LYS B CB  
2533 C CG  . LYS A 383 ? 1.00698 1.09382 0.76850 0.00965  0.00081  -0.15598 660 LYS B CG  
2534 C CD  . LYS A 383 ? 1.01818 1.06406 0.77270 0.02187  0.01446  -0.15743 660 LYS B CD  
2535 N N   . GLU A 384 ? 0.96362 1.04258 0.76143 -0.07405 -0.01769 -0.22032 661 GLU B N   
2536 C CA  . GLU A 384 ? 0.98521 1.05301 0.78543 -0.10249 -0.01848 -0.25487 661 GLU B CA  
2537 C C   . GLU A 384 ? 0.96476 1.08641 0.77976 -0.12025 -0.03219 -0.25904 661 GLU B C   
2538 O O   . GLU A 384 ? 0.99441 1.10473 0.82184 -0.14725 -0.03207 -0.28126 661 GLU B O   
2539 C CB  . GLU A 384 ? 1.04113 1.03960 0.85513 -0.11253 -0.00518 -0.25598 661 GLU B CB  
2540 C CG  . GLU A 384 ? 1.11173 1.06045 0.91639 -0.09180 0.00814  -0.24554 661 GLU B CG  
2541 C CD  . GLU A 384 ? 1.31524 1.25189 1.09611 -0.08645 0.01420  -0.27112 661 GLU B CD  
2542 O OE1 . GLU A 384 ? 1.29860 1.28081 1.06118 -0.07669 0.00722  -0.27581 661 GLU B OE1 
2543 O OE2 . GLU A 384 ? 1.45150 1.33281 1.23163 -0.09089 0.02702  -0.28563 661 GLU B OE2 
2544 N N   . ASN A 385 ? 0.95599 1.13304 0.77191 -0.10542 -0.04231 -0.23733 662 ASN B N   
2545 C CA  . ASN A 385 ? 0.97457 1.21156 0.80491 -0.11800 -0.05588 -0.23916 662 ASN B CA  
2546 C C   . ASN A 385 ? 0.94322 1.16063 0.80323 -0.13488 -0.05286 -0.23167 662 ASN B C   
2547 O O   . ASN A 385 ? 1.01190 1.25856 0.88732 -0.15819 -0.05982 -0.24778 662 ASN B O   
2548 C CB  . ASN A 385 ? 1.08044 1.35636 0.89892 -0.13770 -0.06578 -0.27675 662 ASN B CB  
2549 C CG  . ASN A 385 ? 1.18239 1.53994 1.01003 -0.14134 -0.08268 -0.27417 662 ASN B CG  
2550 O OD1 . ASN A 385 ? 1.21675 1.61749 1.03805 -0.11710 -0.08869 -0.24886 662 ASN B OD1 
2551 N ND2 . ASN A 385 ? 1.24520 1.62540 1.08926 -0.17141 -0.08974 -0.29971 662 ASN B ND2 
2552 N N   . LEU A 386 ? 0.93360 1.10472 0.80185 -0.12326 -0.04232 -0.20705 663 LEU B N   
2553 C CA  . LEU A 386 ? 0.82081 0.97061 0.71380 -0.13540 -0.03741 -0.19593 663 LEU B CA  
2554 C C   . LEU A 386 ? 0.72793 0.88159 0.62760 -0.11193 -0.03584 -0.16053 663 LEU B C   
2555 O O   . LEU A 386 ? 0.82574 0.93945 0.71814 -0.09570 -0.02749 -0.14567 663 LEU B O   
2556 C CB  . LEU A 386 ? 0.86246 0.94203 0.75689 -0.14795 -0.02381 -0.20599 663 LEU B CB  
2557 C CG  . LEU A 386 ? 0.94067 0.99642 0.85862 -0.16686 -0.01717 -0.20095 663 LEU B CG  
2558 C CD1 . LEU A 386 ? 0.80426 0.90213 0.73972 -0.19491 -0.02470 -0.22070 663 LEU B CD1 
2559 C CD2 . LEU A 386 ? 0.93689 0.91991 0.85181 -0.17325 -0.00218 -0.20714 663 LEU B CD2 
2560 N N   . ASP A 387 ? 0.74547 0.94869 0.65994 -0.10997 -0.04356 -0.14802 664 ASP B N   
2561 C CA  . ASP A 387 ? 0.72095 0.93068 0.64330 -0.08853 -0.04158 -0.11681 664 ASP B CA  
2562 C C   . ASP A 387 ? 0.74277 0.94280 0.68809 -0.10081 -0.03712 -0.10916 664 ASP B C   
2563 O O   . ASP A 387 ? 0.78197 1.02446 0.74418 -0.11250 -0.04305 -0.11279 664 ASP B O   
2564 C CB  . ASP A 387 ? 0.62425 0.89645 0.54503 -0.07219 -0.05144 -0.10562 664 ASP B CB  
2565 C CG  . ASP A 387 ? 0.71891 1.00179 0.65453 -0.05436 -0.04866 -0.07611 664 ASP B CG  
2566 O OD1 . ASP A 387 ? 0.65362 0.89298 0.59408 -0.04945 -0.03914 -0.06310 664 ASP B OD1 
2567 O OD2 . ASP A 387 ? 0.75598 1.09284 0.69850 -0.04477 -0.05593 -0.06645 664 ASP B OD2 
2568 N N   . LEU A 388 ? 0.67485 0.82251 0.62080 -0.09779 -0.02655 -0.09830 665 LEU B N   
2569 C CA  . LEU A 388 ? 0.71859 0.85201 0.68226 -0.10909 -0.02033 -0.09089 665 LEU B CA  
2570 C C   . LEU A 388 ? 0.71397 0.86302 0.68726 -0.09191 -0.01894 -0.06634 665 LEU B C   
2571 O O   . LEU A 388 ? 0.72630 0.85629 0.70930 -0.09596 -0.01174 -0.05701 665 LEU B O   
2572 C CB  . LEU A 388 ? 0.70828 0.77842 0.66619 -0.11571 -0.00935 -0.09277 665 LEU B CB  
2573 C CG  . LEU A 388 ? 0.81125 0.86145 0.76371 -0.13575 -0.00800 -0.11919 665 LEU B CG  
2574 C CD1 . LEU A 388 ? 0.74261 0.72841 0.69097 -0.13984 0.00462  -0.11797 665 LEU B CD1 
2575 C CD2 . LEU A 388 ? 0.67850 0.76466 0.64775 -0.16192 -0.01288 -0.13715 665 LEU B CD2 
2576 N N   . LYS A 389 ? 0.68333 0.86563 0.65355 -0.07247 -0.02448 -0.05566 666 LYS B N   
2577 C CA  . LYS A 389 ? 0.62899 0.82860 0.61043 -0.05613 -0.02234 -0.03435 666 LYS B CA  
2578 C C   . LYS A 389 ? 0.67096 0.82370 0.64952 -0.04769 -0.01265 -0.02133 666 LYS B C   
2579 O O   . LYS A 389 ? 0.62618 0.77914 0.61632 -0.04600 -0.00768 -0.01102 666 LYS B O   
2580 C CB  . LYS A 389 ? 0.66579 0.90481 0.66912 -0.06689 -0.02419 -0.03438 666 LYS B CB  
2581 C CG  . LYS A 389 ? 0.68576 0.97708 0.69484 -0.07868 -0.03515 -0.04957 666 LYS B CG  
2582 C CD  . LYS A 389 ? 0.62624 0.95692 0.62648 -0.05824 -0.04335 -0.04245 666 LYS B CD  
2583 C CE  . LYS A 389 ? 0.73381 1.11479 0.73368 -0.07166 -0.05579 -0.06194 666 LYS B CE  
2584 N NZ  . LYS A 389 ? 0.68892 1.11818 0.67967 -0.05126 -0.06458 -0.05331 666 LYS B NZ  
2585 N N   . LEU A 390 ? 0.59329 0.70911 0.55627 -0.04214 -0.01006 -0.02269 667 LEU B N   
2586 C CA  . LEU A 390 ? 0.58748 0.66245 0.54725 -0.03470 -0.00242 -0.01182 667 LEU B CA  
2587 C C   . LEU A 390 ? 0.59001 0.67435 0.55279 -0.01471 -0.00080 0.00457  667 LEU B C   
2588 O O   . LEU A 390 ? 0.54275 0.65910 0.50706 -0.00470 -0.00468 0.00878  667 LEU B O   
2589 C CB  . LEU A 390 ? 0.59171 0.62971 0.53659 -0.03481 -0.00040 -0.01893 667 LEU B CB  
2590 C CG  . LEU A 390 ? 0.65844 0.68285 0.59957 -0.05338 -0.00044 -0.03721 667 LEU B CG  
2591 C CD1 . LEU A 390 ? 0.64419 0.62741 0.57192 -0.04969 0.00409  -0.04178 667 LEU B CD1 
2592 C CD2 . LEU A 390 ? 0.64959 0.66651 0.60243 -0.07020 0.00369  -0.03795 667 LEU B CD2 
2593 N N   . THR A 391 ? 0.54994 0.60759 0.51345 -0.00928 0.00515  0.01333  668 THR B N   
2594 C CA  . THR A 391 ? 0.53160 0.59158 0.49948 0.00748  0.00850  0.02651  668 THR B CA  
2595 C C   . THR A 391 ? 0.59226 0.61940 0.55179 0.01343  0.01143  0.02899  668 THR B C   
2596 O O   . THR A 391 ? 0.54215 0.54999 0.50311 0.01338  0.01525  0.03224  668 THR B O   
2597 C CB  . THR A 391 ? 0.54498 0.61220 0.52473 0.00826  0.01306  0.03265  668 THR B CB  
2598 O OG1 . THR A 391 ? 0.57013 0.67394 0.56026 0.00400  0.01017  0.03109  668 THR B OG1 
2599 C CG2 . THR A 391 ? 0.46767 0.53125 0.45279 0.02396  0.01835  0.04341  668 THR B CG2 
2600 N N   . PRO A 392 ? 0.51636 0.53981 0.46727 0.01847  0.00978  0.02704  669 PRO B N   
2601 C CA  . PRO A 392 ? 0.63280 0.63124 0.57927 0.02504  0.01289  0.03031  669 PRO B CA  
2602 C C   . PRO A 392 ? 0.60635 0.60907 0.56148 0.03738  0.01717  0.04218  669 PRO B C   
2603 O O   . PRO A 392 ? 0.57077 0.58133 0.52462 0.04646  0.01859  0.04742  669 PRO B O   
2604 C CB  . PRO A 392 ? 0.58847 0.58806 0.52390 0.02651  0.01093  0.02363  669 PRO B CB  
2605 C CG  . PRO A 392 ? 0.58202 0.61607 0.51692 0.02700  0.00674  0.02187  669 PRO B CG  
2606 C CD  . PRO A 392 ? 0.60801 0.65467 0.55283 0.01800  0.00495  0.02078  669 PRO B CD  
2607 N N   . TYR A 393 ? 0.52905 0.52564 0.49248 0.03710  0.02032  0.04570  670 TYR B N   
2608 C CA  . TYR A 393 ? 0.55836 0.55448 0.53212 0.04713  0.02622  0.05474  670 TYR B CA  
2609 C C   . TYR A 393 ? 0.57262 0.55166 0.54628 0.05050  0.02857  0.05653  670 TYR B C   
2610 O O   . TYR A 393 ? 0.54793 0.51273 0.51531 0.04509  0.02579  0.05083  670 TYR B O   
2611 C CB  . TYR A 393 ? 0.46482 0.45724 0.44587 0.04491  0.02966  0.05412  670 TYR B CB  
2612 C CG  . TYR A 393 ? 0.52395 0.49943 0.49876 0.03560  0.02803  0.04722  670 TYR B CG  
2613 C CD1 . TYR A 393 ? 0.54873 0.50698 0.52205 0.03560  0.02832  0.04584  670 TYR B CD1 
2614 C CD2 . TYR A 393 ? 0.52351 0.50321 0.49449 0.02694  0.02643  0.04326  670 TYR B CD2 
2615 C CE1 . TYR A 393 ? 0.55132 0.49859 0.51745 0.02920  0.02618  0.04165  670 TYR B CE1 
2616 C CE2 . TYR A 393 ? 0.53556 0.50061 0.49914 0.02004  0.02602  0.04011  670 TYR B CE2 
2617 C CZ  . TYR A 393 ? 0.52723 0.47679 0.48728 0.02217  0.02543  0.03979  670 TYR B CZ  
2618 O OH  . TYR A 393 ? 0.58895 0.52834 0.54027 0.01741  0.02440  0.03871  670 TYR B OH  
2619 N N   . LYS A 394 ? 0.49085 0.47234 0.47287 0.05968  0.03445  0.06553  671 LYS B N   
2620 C CA  . LYS A 394 ? 0.52186 0.49128 0.50760 0.06186  0.03786  0.06790  671 LYS B CA  
2621 C C   . LYS A 394 ? 0.52760 0.48067 0.51963 0.05548  0.03827  0.06209  671 LYS B C   
2622 O O   . LYS A 394 ? 0.46850 0.41805 0.46621 0.05345  0.04059  0.05992  671 LYS B O   
2623 C CB  . LYS A 394 ? 0.53985 0.51459 0.53522 0.07202  0.04625  0.08054  671 LYS B CB  
2624 C CG  . LYS A 394 ? 0.59703 0.59297 0.58361 0.08039  0.04553  0.08796  671 LYS B CG  
2625 C CD  . LYS A 394 ? 0.67372 0.67113 0.64633 0.07702  0.04007  0.08005  671 LYS B CD  
2626 C CE  . LYS A 394 ? 0.77281 0.78654 0.73857 0.08698  0.04351  0.08876  671 LYS B CE  
2627 N NZ  . LYS A 394 ? 0.85406 0.89212 0.81712 0.09375  0.04211  0.09597  671 LYS B NZ  
2628 N N   . VAL A 395 ? 0.51825 0.46416 0.50892 0.05308  0.03602  0.05905  672 VAL B N   
2629 C CA  . VAL A 395 ? 0.46051 0.39780 0.45853 0.04807  0.03558  0.05429  672 VAL B CA  
2630 C C   . VAL A 395 ? 0.53501 0.47295 0.54303 0.05047  0.03882  0.05785  672 VAL B C   
2631 O O   . VAL A 395 ? 0.54357 0.48506 0.54581 0.05437  0.03757  0.06003  672 VAL B O   
2632 C CB  . VAL A 395 ? 0.49856 0.43167 0.48552 0.04270  0.02816  0.04774  672 VAL B CB  
2633 C CG1 . VAL A 395 ? 0.47959 0.41109 0.47322 0.03866  0.02604  0.04309  672 VAL B CG1 
2634 C CG2 . VAL A 395 ? 0.48864 0.42239 0.46721 0.03909  0.02665  0.04520  672 VAL B CG2 
2635 N N   . LEU A 396 ? 0.54107 0.47569 0.56502 0.04743  0.04384  0.05725  673 LEU B N   
2636 C CA  . LEU A 396 ? 0.51789 0.45558 0.55574 0.04725  0.04774  0.06023  673 LEU B CA  
2637 C C   . LEU A 396 ? 0.51926 0.45596 0.57004 0.03782  0.04597  0.05081  673 LEU B C   
2638 O O   . LEU A 396 ? 0.47007 0.39888 0.52949 0.03293  0.05061  0.04611  673 LEU B O   
2639 C CB  . LEU A 396 ? 0.49608 0.43313 0.54499 0.05263  0.05924  0.07162  673 LEU B CB  
2640 C CG  . LEU A 396 ? 0.57195 0.51290 0.63871 0.05061  0.06549  0.07546  673 LEU B CG  
2641 C CD1 . LEU A 396 ? 0.53006 0.48250 0.58840 0.05698  0.06316  0.07935  673 LEU B CD1 
2642 C CD2 . LEU A 396 ? 0.50144 0.43632 0.58355 0.05314  0.07954  0.08699  673 LEU B CD2 
2643 N N   . ALA A 397 ? 0.48148 0.42766 0.53391 0.03587  0.03954  0.04745  674 ALA B N   
2644 C CA  . ALA A 397 ? 0.46084 0.41460 0.52784 0.02671  0.03663  0.03840  674 ALA B CA  
2645 C C   . ALA A 397 ? 0.47246 0.42853 0.56423 0.02265  0.04635  0.04141  674 ALA B C   
2646 O O   . ALA A 397 ? 0.49209 0.45462 0.58917 0.02844  0.05076  0.05101  674 ALA B O   
2647 C CB  . ALA A 397 ? 0.43327 0.40141 0.49466 0.02869  0.02630  0.03679  674 ALA B CB  
2648 N N   . THR A 398 ? 0.45420 0.40377 0.56133 0.01244  0.05129  0.03301  675 THR B N   
2649 C CA  . THR A 398 ? 0.47946 0.42881 0.61363 0.00549  0.06201  0.03491  675 THR B CA  
2650 C C   . THR A 398 ? 0.49026 0.45872 0.64203 -0.00712 0.05554  0.02216  675 THR B C   
2651 O O   . THR A 398 ? 0.49306 0.46516 0.67116 -0.01640 0.06363  0.02120  675 THR B O   
2652 C CB  . THR A 398 ? 0.51847 0.44433 0.66224 0.00220  0.07504  0.03461  675 THR B CB  
2653 O OG1 . THR A 398 ? 0.54546 0.46332 0.67996 -0.00287 0.07021  0.01970  675 THR B OG1 
2654 C CG2 . THR A 398 ? 0.44249 0.35748 0.57554 0.01683  0.08357  0.05286  675 THR B CG2 
2655 N N   . SER A 399 ? 0.52757 0.51103 0.66567 -0.00720 0.04120  0.01374  676 SER B N   
2656 C CA  . SER A 399 ? 0.51762 0.52759 0.66774 -0.01644 0.03122  0.00229  676 SER B CA  
2657 C C   . SER A 399 ? 0.55332 0.57508 0.67844 -0.00816 0.01690  0.00206  676 SER B C   
2658 O O   . SER A 399 ? 0.52979 0.53556 0.63139 0.00071  0.01632  0.00773  676 SER B O   
2659 C CB  . SER A 399 ? 0.51047 0.51813 0.67546 -0.03384 0.03297  -0.01683 676 SER B CB  
2660 O OG  . SER A 399 ? 0.66197 0.70211 0.83824 -0.04302 0.02151  -0.02855 676 SER B OG  
2661 N N   . THR A 400 ? 0.54336 0.59476 0.67486 -0.01112 0.00581  -0.00362 677 THR B N   
2662 C CA  . THR A 400 ? 0.59682 0.65780 0.70396 -0.00387 -0.00666 -0.00355 677 THR B CA  
2663 C C   . THR A 400 ? 0.57648 0.63014 0.66918 -0.01205 -0.00955 -0.01765 677 THR B C   
2664 O O   . THR A 400 ? 0.51214 0.57011 0.58149 -0.00599 -0.01760 -0.01611 677 THR B O   
2665 C CB  . THR A 400 ? 0.52202 0.62095 0.63805 -0.00156 -0.01850 -0.00322 677 THR B CB  
2666 O OG1 . THR A 400 ? 0.58330 0.70590 0.72050 -0.01809 -0.02243 -0.02005 677 THR B OG1 
2667 C CG2 . THR A 400 ? 0.55242 0.65972 0.68266 0.00896  -0.01432 0.01101  677 THR B CG2 
2668 N N   . LYS A 401 ? 0.54999 0.59056 0.65580 -0.02473 -0.00129 -0.03044 678 LYS B N   
2669 C CA  . LYS A 401 ? 0.53602 0.57085 0.63104 -0.03336 -0.00237 -0.04752 678 LYS B CA  
2670 C C   . LYS A 401 ? 0.57153 0.57130 0.66234 -0.03255 0.01114  -0.04769 678 LYS B C   
2671 O O   . LYS A 401 ? 0.54097 0.53339 0.62333 -0.03844 0.01266  -0.06241 678 LYS B O   
2672 C CB  . LYS A 401 ? 0.56972 0.62435 0.68578 -0.05125 -0.00547 -0.06892 678 LYS B CB  
2673 C CG  . LYS A 401 ? 0.62725 0.72589 0.74947 -0.05257 -0.02076 -0.07064 678 LYS B CG  
2674 C CD  . LYS A 401 ? 0.81639 0.93583 0.97147 -0.07221 -0.02091 -0.08890 678 LYS B CD  
2675 C CE  . LYS A 401 ? 0.67406 0.84428 0.84181 -0.07244 -0.03590 -0.08805 678 LYS B CE  
2676 N N   . HIS A 402 ? 0.48832 0.46886 0.58419 -0.02435 0.02113  -0.03189 679 HIS B N   
2677 C CA  . HIS A 402 ? 0.48068 0.43300 0.57286 -0.02088 0.03318  -0.02953 679 HIS B CA  
2678 C C   . HIS A 402 ? 0.48856 0.43121 0.57749 -0.00805 0.03861  -0.00899 679 HIS B C   
2679 O O   . HIS A 402 ? 0.48857 0.44192 0.58231 -0.00383 0.03623  0.00115  679 HIS B O   
2680 C CB  . HIS A 402 ? 0.50595 0.44134 0.62089 -0.03199 0.04581  -0.04132 679 HIS B CB  
2681 C CG  . HIS A 402 ? 0.50802 0.44778 0.65167 -0.03996 0.05134  -0.03918 679 HIS B CG  
2682 N ND1 . HIS A 402 ? 0.57969 0.51188 0.73328 -0.03193 0.06046  -0.01957 679 HIS B ND1 
2683 C CD2 . HIS A 402 ? 0.57748 0.52984 0.74324 -0.05625 0.05018  -0.05467 679 HIS B CD2 
2684 C CE1 . HIS A 402 ? 0.46183 0.40096 0.64249 -0.04226 0.06560  -0.02123 679 HIS B CE1 
2685 N NE2 . HIS A 402 ? 0.55715 0.50867 0.74729 -0.05795 0.05934  -0.04283 679 HIS B NE2 
2686 N N   . GLY A 403 ? 0.47443 0.39944 0.55521 -0.00141 0.04607  -0.00376 680 GLY B N   
2687 C CA  . GLY A 403 ? 0.47861 0.39871 0.55483 0.01022  0.05029  0.01387  680 GLY B CA  
2688 C C   . GLY A 403 ? 0.50785 0.41515 0.57582 0.01716  0.05673  0.01786  680 GLY B C   
2689 O O   . GLY A 403 ? 0.53074 0.43075 0.59653 0.01394  0.05923  0.00733  680 GLY B O   
2690 N N   . PHE A 404 ? 0.47831 0.38623 0.54150 0.02730  0.05927  0.03270  681 PHE B N   
2691 C CA  . PHE A 404 ? 0.48072 0.38344 0.53940 0.03609  0.06524  0.04034  681 PHE B CA  
2692 C C   . PHE A 404 ? 0.49525 0.40922 0.53422 0.04034  0.05635  0.04355  681 PHE B C   
2693 O O   . PHE A 404 ? 0.47955 0.40123 0.50988 0.04030  0.04901  0.04568  681 PHE B O   
2694 C CB  . PHE A 404 ? 0.51732 0.41674 0.58689 0.04491  0.07564  0.05632  681 PHE B CB  
2695 C CG  . PHE A 404 ? 0.53641 0.41943 0.62793 0.04180  0.08876  0.05654  681 PHE B CG  
2696 C CD1 . PHE A 404 ? 0.59533 0.46253 0.69487 0.04559  0.09958  0.05625  681 PHE B CD1 
2697 C CD2 . PHE A 404 ? 0.53258 0.41532 0.63879 0.03538  0.09199  0.05766  681 PHE B CD2 
2698 C CE1 . PHE A 404 ? 0.61155 0.45786 0.73318 0.04220  0.11419  0.05628  681 PHE B CE1 
2699 C CE2 . PHE A 404 ? 0.60201 0.46744 0.73141 0.03037  0.10599  0.05800  681 PHE B CE2 
2700 C CZ  . PHE A 404 ? 0.58828 0.43315 0.72512 0.03346  0.11741  0.05707  681 PHE B CZ  
2701 N N   . MET A 405 ? 0.54942 0.46389 0.58356 0.04433  0.05864  0.04424  682 MET B N   
2702 C CA  . MET A 405 ? 0.55392 0.48035 0.57421 0.04773  0.05277  0.04854  682 MET B CA  
2703 C C   . MET A 405 ? 0.50600 0.43781 0.53190 0.05733  0.05980  0.05753  682 MET B C   
2704 O O   . MET A 405 ? 0.49612 0.41944 0.53244 0.06052  0.06865  0.05667  682 MET B O   
2705 C CB  . MET A 405 ? 0.50660 0.43546 0.51437 0.04115  0.04654  0.03938  682 MET B CB  
2706 C CG  . MET A 405 ? 0.62119 0.54872 0.62100 0.03448  0.03862  0.03376  682 MET B CG  
2707 S SD  . MET A 405 ? 0.67475 0.60556 0.65843 0.02885  0.03385  0.02744  682 MET B SD  
2708 C CE  . MET A 405 ? 0.61187 0.54266 0.58756 0.02582  0.02491  0.02693  682 MET B CE  
2709 N N   . GLN A 406 ? 0.51162 0.45858 0.53086 0.06243  0.05603  0.06557  683 GLN B N   
2710 C CA  . GLN A 406 ? 0.54796 0.50902 0.57115 0.07235  0.05998  0.07485  683 GLN B CA  
2711 C C   . GLN A 406 ? 0.55461 0.52230 0.57618 0.06969  0.05903  0.06840  683 GLN B C   
2712 O O   . GLN A 406 ? 0.51758 0.49030 0.52847 0.06079  0.05143  0.06104  683 GLN B O   
2713 C CB  . GLN A 406 ? 0.53645 0.51738 0.55051 0.07586  0.05369  0.08137  683 GLN B CB  
2714 C CG  . GLN A 406 ? 0.47542 0.48042 0.49217 0.08596  0.05463  0.09094  683 GLN B CG  
2715 C CD  . GLN A 406 ? 0.59103 0.61814 0.59606 0.08670  0.04668  0.09297  683 GLN B CD  
2716 O OE1 . GLN A 406 ? 0.55563 0.57680 0.54960 0.07817  0.04059  0.08449  683 GLN B OE1 
2717 N NE2 . GLN A 406 ? 0.53934 0.59326 0.54633 0.09761  0.04683  0.10367  683 GLN B NE2 
2718 N N   . PHE A 407 ? 0.57825 0.54506 0.61123 0.07808  0.06835  0.07206  684 PHE B N   
2719 C CA  . PHE A 407 ? 0.51798 0.49423 0.55109 0.07732  0.06954  0.06662  684 PHE B CA  
2720 C C   . PHE A 407 ? 0.54594 0.55331 0.57903 0.08205  0.06487  0.07438  684 PHE B C   
2721 O O   . PHE A 407 ? 0.58952 0.61034 0.62970 0.09441  0.06742  0.08723  684 PHE B O   
2722 C CB  . PHE A 407 ? 0.52290 0.48602 0.56902 0.08569  0.08277  0.06596  684 PHE B CB  
2723 C CG  . PHE A 407 ? 0.53306 0.50762 0.57962 0.08653  0.08579  0.06040  684 PHE B CG  
2724 C CD1 . PHE A 407 ? 0.57725 0.54893 0.61212 0.07438  0.08194  0.04709  684 PHE B CD1 
2725 C CD2 . PHE A 407 ? 0.54773 0.53954 0.60638 0.10060  0.09280  0.07018  684 PHE B CD2 
2726 C CE1 . PHE A 407 ? 0.67291 0.65710 0.70777 0.07521  0.08621  0.04294  684 PHE B CE1 
2727 C CE2 . PHE A 407 ? 0.61015 0.61578 0.67094 0.10177  0.09658  0.06534  684 PHE B CE2 
2728 C CZ  . PHE A 407 ? 0.57041 0.57169 0.61905 0.08850  0.09377  0.05141  684 PHE B CZ  
2729 N N   . ILE A 408 ? 0.54803 0.56829 0.57404 0.07221  0.05857  0.06727  685 ILE B N   
2730 C CA  . ILE A 408 ? 0.56750 0.62151 0.59637 0.07325  0.05365  0.07172  685 ILE B CA  
2731 C C   . ILE A 408 ? 0.54127 0.60883 0.57947 0.07570  0.05994  0.07044  685 ILE B C   
2732 O O   . ILE A 408 ? 0.57347 0.62845 0.60588 0.06667  0.06194  0.06121  685 ILE B O   
2733 C CB  . ILE A 408 ? 0.56961 0.62872 0.58609 0.05830  0.04295  0.06445  685 ILE B CB  
2734 C CG1 . ILE A 408 ? 0.57948 0.62255 0.58610 0.05685  0.03845  0.06412  685 ILE B CG1 
2735 C CG2 . ILE A 408 ? 0.53686 0.63258 0.55819 0.05633  0.03745  0.06597  685 ILE B CG2 
2736 C CD1 . ILE A 408 ? 0.53663 0.59247 0.54680 0.06965  0.03914  0.07495  685 ILE B CD1 
2737 N N   . GLN A 409 ? 0.57449 0.66898 0.62640 0.08893  0.06346  0.08040  686 GLN B N   
2738 C CA  . GLN A 409 ? 0.59956 0.71262 0.66273 0.09264  0.07017  0.07981  686 GLN B CA  
2739 C C   . GLN A 409 ? 0.66090 0.78953 0.71833 0.07455  0.06317  0.07109  686 GLN B C   
2740 O O   . GLN A 409 ? 0.59321 0.74248 0.64879 0.06672  0.05314  0.07123  686 GLN B O   
2741 C CB  . GLN A 409 ? 0.66241 0.80905 0.74273 0.11105  0.07342  0.09403  686 GLN B CB  
2742 C CG  . GLN A 409 ? 0.87367 1.03893 0.96854 0.11848  0.08282  0.09451  686 GLN B CG  
2743 C CD  . GLN A 409 ? 0.99676 1.12524 1.08948 0.12086  0.09577  0.08628  686 GLN B CD  
2744 O OE1 . GLN A 409 ? 0.97811 1.10415 1.06607 0.11106  0.09867  0.07558  686 GLN B OE1 
2745 N NE2 . GLN A 409 ? 0.82815 0.92790 0.92396 0.13321  0.10425  0.09073  686 GLN B NE2 
2746 N N   . SER A 410 ? 0.56743 0.68642 0.62185 0.06787  0.06918  0.06351  687 SER B N   
2747 C CA  . SER A 410 ? 0.56210 0.68997 0.61030 0.04986  0.06470  0.05731  687 SER B CA  
2748 C C   . SER A 410 ? 0.62301 0.74306 0.66793 0.04749  0.07451  0.05202  687 SER B C   
2749 O O   . SER A 410 ? 0.57454 0.67887 0.61938 0.05815  0.08332  0.04981  687 SER B O   
2750 C CB  . SER A 410 ? 0.53259 0.63685 0.56410 0.03671  0.05569  0.05243  687 SER B CB  
2751 O OG  . SER A 410 ? 0.53757 0.60800 0.55845 0.04036  0.05792  0.04957  687 SER B OG  
2752 N N   . VAL A 411 ? 0.52979 0.66001 0.57137 0.03281  0.07389  0.04943  688 VAL B N   
2753 C CA  . VAL A 411 ? 0.55344 0.67916 0.58861 0.02992  0.08360  0.04562  688 VAL B CA  
2754 C C   . VAL A 411 ? 0.50588 0.61821 0.52530 0.01218  0.08009  0.04381  688 VAL B C   
2755 O O   . VAL A 411 ? 0.51948 0.64075 0.54257 -0.00017 0.07394  0.04561  688 VAL B O   
2756 C CB  . VAL A 411 ? 0.51162 0.67358 0.56539 0.03525  0.09275  0.04888  688 VAL B CB  
2757 C CG1 . VAL A 411 ? 0.52697 0.72348 0.59622 0.02587  0.08597  0.05322  688 VAL B CG1 
2758 C CG2 . VAL A 411 ? 0.53434 0.69524 0.57937 0.02957  0.10283  0.04545  688 VAL B CG2 
2759 N N   . PRO A 412 ? 0.53385 0.62407 0.53523 0.01066  0.08377  0.04025  689 PRO B N   
2760 C CA  . PRO A 412 ? 0.54351 0.62049 0.52941 -0.00346 0.08146  0.04222  689 PRO B CA  
2761 C C   . PRO A 412 ? 0.58582 0.68560 0.57985 -0.01459 0.08821  0.04690  689 PRO B C   
2762 O O   . PRO A 412 ? 0.57663 0.70094 0.58182 -0.00993 0.09731  0.04720  689 PRO B O   
2763 C CB  . PRO A 412 ? 0.52285 0.58101 0.48860 0.00089  0.08486  0.03804  689 PRO B CB  
2764 C CG  . PRO A 412 ? 0.53819 0.59201 0.50924 0.01462  0.08671  0.03089  689 PRO B CG  
2765 C CD  . PRO A 412 ? 0.57147 0.64849 0.56551 0.02189  0.09046  0.03386  689 PRO B CD  
2766 N N   . VAL A 413 ? 0.50919 0.60027 0.49940 -0.02947 0.08497  0.05061  690 VAL B N   
2767 C CA  . VAL A 413 ? 0.58332 0.69360 0.58344 -0.04322 0.09249  0.05529  690 VAL B CA  
2768 C C   . VAL A 413 ? 0.60506 0.72100 0.59534 -0.04079 0.10514  0.05908  690 VAL B C   
2769 O O   . VAL A 413 ? 0.56382 0.70791 0.56799 -0.04523 0.11473  0.06196  690 VAL B O   
2770 C CB  . VAL A 413 ? 0.63923 0.73019 0.63542 -0.06013 0.08924  0.05826  690 VAL B CB  
2771 C CG1 . VAL A 413 ? 0.55174 0.65663 0.55625 -0.07569 0.10043  0.06460  690 VAL B CG1 
2772 C CG2 . VAL A 413 ? 0.55640 0.65130 0.56505 -0.06461 0.07847  0.05191  690 VAL B CG2 
2773 N N   . ALA A 414 ? 0.58699 0.68051 0.55354 -0.03347 0.10547  0.05858  691 ALA B N   
2774 C CA  . ALA A 414 ? 0.63170 0.73292 0.58468 -0.03033 0.11730  0.06084  691 ALA B CA  
2775 C C   . ALA A 414 ? 0.61593 0.74440 0.58267 -0.01973 0.12604  0.05486  691 ALA B C   
2776 O O   . ALA A 414 ? 0.64957 0.79869 0.61759 -0.02113 0.13878  0.05819  691 ALA B O   
2777 C CB  . ALA A 414 ? 0.51278 0.59088 0.43807 -0.02305 0.11361  0.05833  691 ALA B CB  
2778 N N   . GLU A 415 ? 0.58542 0.71420 0.56345 -0.00807 0.12085  0.04731  692 GLU B N   
2779 C CA  . GLU A 415 ? 0.59951 0.75099 0.59258 0.00494  0.13025  0.04282  692 GLU B CA  
2780 C C   . GLU A 415 ? 0.60593 0.79393 0.62718 0.00031  0.13360  0.04914  692 GLU B C   
2781 O O   . GLU A 415 ? 0.64028 0.85554 0.67311 0.00634  0.14591  0.04969  692 GLU B O   
2782 C CB  . GLU A 415 ? 0.67182 0.80824 0.66859 0.01950  0.12520  0.03523  692 GLU B CB  
2783 C CG  . GLU A 415 ? 0.71704 0.86270 0.72142 0.03592  0.13753  0.02852  692 GLU B CG  
2784 C CD  . GLU A 415 ? 1.01535 1.15280 0.99697 0.03782  0.14755  0.01965  692 GLU B CD  
2785 O OE1 . GLU A 415 ? 1.15954 1.27120 1.11949 0.03567  0.14174  0.01243  692 GLU B OE1 
2786 O OE2 . GLU A 415 ? 1.07091 1.23105 1.05614 0.04162  0.16122  0.01949  692 GLU B OE2 
2787 N N   . VAL A 416 ? 0.58191 0.77357 0.61481 -0.01077 0.12299  0.05285  693 VAL B N   
2788 C CA  . VAL A 416 ? 0.53464 0.76479 0.59410 -0.01997 0.12460  0.05727  693 VAL B CA  
2789 C C   . VAL A 416 ? 0.58943 0.83530 0.64961 -0.03178 0.13787  0.06257  693 VAL B C   
2790 O O   . VAL A 416 ? 0.61366 0.89776 0.69459 -0.02979 0.14756  0.06494  693 VAL B O   
2791 C CB  . VAL A 416 ? 0.61602 0.84271 0.68210 -0.03429 0.11102  0.05709  693 VAL B CB  
2792 C CG1 . VAL A 416 ? 0.58671 0.85356 0.67896 -0.04950 0.11294  0.05929  693 VAL B CG1 
2793 C CG2 . VAL A 416 ? 0.54653 0.76855 0.61564 -0.02128 0.09940  0.05378  693 VAL B CG2 
2794 N N   . LEU A 417 ? 0.56403 0.78244 0.60260 -0.04361 0.13937  0.06630  694 LEU B N   
2795 C CA  . LEU A 417 ? 0.68154 0.91277 0.71895 -0.05483 0.15365  0.07430  694 LEU B CA  
2796 C C   . LEU A 417 ? 0.59587 0.84184 0.62530 -0.03999 0.16775  0.07303  694 LEU B C   
2797 O O   . LEU A 417 ? 0.50249 0.77866 0.54384 -0.04439 0.18167  0.07840  694 LEU B O   
2798 C CB  . LEU A 417 ? 0.73872 0.93469 0.75221 -0.06705 0.15334  0.08155  694 LEU B CB  
2799 C CG  . LEU A 417 ? 0.69530 0.86845 0.71271 -0.08207 0.14219  0.08223  694 LEU B CG  
2800 C CD1 . LEU A 417 ? 0.77792 0.92086 0.77471 -0.09223 0.14815  0.09353  694 LEU B CD1 
2801 C CD2 . LEU A 417 ? 0.66057 0.86348 0.71070 -0.09781 0.14119  0.08011  694 LEU B CD2 
2802 N N   . ASP A 418 ? 0.59631 0.82244 0.60695 -0.02305 0.16526  0.06470  695 ASP B N   
2803 C CA  . ASP A 418 ? 0.61535 0.85187 0.61549 -0.00935 0.17925  0.05988  695 ASP B CA  
2804 C C   . ASP A 418 ? 0.63325 0.90696 0.66277 0.00172  0.18820  0.05773  695 ASP B C   
2805 O O   . ASP A 418 ? 0.57621 0.87377 0.60754 0.00640  0.20436  0.05854  695 ASP B O   
2806 C CB  . ASP A 418 ? 0.65871 0.86424 0.63395 0.00372  0.17399  0.04831  695 ASP B CB  
2807 C CG  . ASP A 418 ? 0.71257 0.92289 0.66741 0.01345  0.18805  0.04122  695 ASP B CG  
2808 O OD1 . ASP A 418 ? 0.66900 0.88201 0.60363 0.00583  0.19475  0.04817  695 ASP B OD1 
2809 O OD2 . ASP A 418 ? 0.81253 1.02364 0.77114 0.02907  0.19345  0.02889  695 ASP B OD2 
2810 N N   . THR A 419 ? 0.59460 0.87619 0.64722 0.00735  0.17850  0.05620  696 THR B N   
2811 C CA  . THR A 419 ? 0.55149 0.86703 0.63195 0.02313  0.18555  0.05546  696 THR B CA  
2812 C C   . THR A 419 ? 0.53231 0.89397 0.64636 0.01251  0.18488  0.06403  696 THR B C   
2813 O O   . THR A 419 ? 0.55475 0.95589 0.69012 0.02013  0.19744  0.06679  696 THR B O   
2814 C CB  . THR A 419 ? 0.66204 0.95987 0.74678 0.04001  0.17647  0.05026  696 THR B CB  
2815 O OG1 . THR A 419 ? 0.62202 0.91218 0.71134 0.02930  0.15899  0.05377  696 THR B OG1 
2816 C CG2 . THR A 419 ? 0.60921 0.86467 0.66559 0.04945  0.17815  0.03929  696 THR B CG2 
2817 N N   . GLU A 420 ? 0.56443 0.92448 0.68513 -0.00492 0.17072  0.06698  697 GLU B N   
2818 C CA  . GLU A 420 ? 0.51083 0.91702 0.66435 -0.01783 0.16845  0.07187  697 GLU B CA  
2819 C C   . GLU A 420 ? 0.56283 0.97226 0.71702 -0.04519 0.17310  0.07652  697 GLU B C   
2820 O O   . GLU A 420 ? 0.54117 0.99351 0.72511 -0.05866 0.17540  0.07960  697 GLU B O   
2821 C CB  . GLU A 420 ? 0.53659 0.94666 0.70164 -0.01858 0.14979  0.06981  697 GLU B CB  
2822 C CG  . GLU A 420 ? 0.56847 0.96182 0.72739 0.00703  0.14456  0.06756  697 GLU B CG  
2823 C CD  . GLU A 420 ? 0.58549 1.01408 0.76631 0.03094  0.15511  0.07103  697 GLU B CD  
2824 O OE1 . GLU A 420 ? 0.69353 1.16876 0.89842 0.02781  0.16400  0.07520  697 GLU B OE1 
2825 N N   . GLY A 421 ? 0.61071 0.97740 0.73450 -0.05372 0.17512  0.07790  698 GLY B N   
2826 C CA  . GLY A 421 ? 0.57341 0.93774 0.69579 -0.07707 0.18337  0.08549  698 GLY B CA  
2827 C C   . GLY A 421 ? 0.62170 0.96642 0.74750 -0.09933 0.17155  0.08489  698 GLY B C   
2828 O O   . GLY A 421 ? 0.67758 1.00540 0.79701 -0.11804 0.17878  0.09199  698 GLY B O   
2829 N N   . SER A 422 ? 0.59720 0.94281 0.73234 -0.09753 0.15500  0.07700  699 SER B N   
2830 C CA  . SER A 422 ? 0.62047 0.95022 0.75995 -0.11912 0.14466  0.07333  699 SER B CA  
2831 C C   . SER A 422 ? 0.59741 0.93251 0.74296 -0.11152 0.12658  0.06397  699 SER B C   
2832 O O   . SER A 422 ? 0.55880 0.92887 0.71948 -0.09525 0.12332  0.06256  699 SER B O   
2833 C CB  . SER A 422 ? 0.58557 0.94981 0.75526 -0.14483 0.15201  0.07493  699 SER B CB  
2834 O OG  . SER A 422 ? 0.60818 1.02661 0.81004 -0.14391 0.14450  0.06864  699 SER B OG  
2835 N N   . ILE A 423 ? 0.60755 0.90910 0.74144 -0.12199 0.11588  0.05859  700 ILE B N   
2836 C CA  . ILE A 423 ? 0.55643 0.86474 0.69415 -0.11607 0.09935  0.04985  700 ILE B CA  
2837 C C   . ILE A 423 ? 0.61579 0.98418 0.78721 -0.12360 0.09443  0.04516  700 ILE B C   
2838 O O   . ILE A 423 ? 0.57320 0.96932 0.75268 -0.10760 0.08486  0.04339  700 ILE B O   
2839 C CB  . ILE A 423 ? 0.58776 0.85176 0.70852 -0.12860 0.09116  0.04379  700 ILE B CB  
2840 C CG1 . ILE A 423 ? 0.52762 0.74050 0.61623 -0.11454 0.09288  0.04912  700 ILE B CG1 
2841 C CG2 . ILE A 423 ? 0.56150 0.84244 0.68991 -0.12862 0.07486  0.03279  700 ILE B CG2 
2842 C CD1 . ILE A 423 ? 0.52194 0.68887 0.59365 -0.12482 0.08826  0.04611  700 ILE B CD1 
2843 N N   . GLN A 424 ? 0.58434 0.97663 0.77717 -0.14763 0.10140  0.04421  701 GLN B N   
2844 C CA  . GLN A 424 ? 0.62162 1.07773 0.84922 -0.15695 0.09554  0.03846  701 GLN B CA  
2845 C C   . GLN A 424 ? 0.62767 1.13207 0.87211 -0.13327 0.09993  0.04650  701 GLN B C   
2846 O O   . GLN A 424 ? 0.56866 1.12025 0.83185 -0.12384 0.08939  0.04421  701 GLN B O   
2847 C CB  . GLN A 424 ? 0.61897 1.09040 0.86894 -0.18979 0.10419  0.03554  701 GLN B CB  
2848 C CG  . GLN A 424 ? 0.68725 1.12176 0.92996 -0.21527 0.09834  0.02394  701 GLN B CG  
2849 C CD  . GLN A 424 ? 0.76269 1.24562 1.03779 -0.24123 0.08989  0.00894  701 GLN B CD  
2850 O OE1 . GLN A 424 ? 0.71836 1.25782 1.02624 -0.25135 0.09502  0.01018  701 GLN B OE1 
2851 N NE2 . GLN A 424 ? 0.73854 1.20224 1.00512 -0.25247 0.07686  -0.00664 701 GLN B NE2 
2852 N N   . ASN A 425 ? 0.55882 1.05397 0.79676 -0.12246 0.11614  0.05621  702 ASN B N   
2853 C CA  . ASN A 425 ? 0.53688 1.07040 0.78854 -0.09691 0.12263  0.06297  702 ASN B CA  
2854 C C   . ASN A 425 ? 0.57475 1.09800 0.81462 -0.06915 0.11198  0.06295  702 ASN B C   
2855 O O   . ASN A 425 ? 0.56644 1.13569 0.82763 -0.05303 0.10748  0.06585  702 ASN B O   
2856 C CB  . ASN A 425 ? 0.49580 1.01087 0.73441 -0.08923 0.14207  0.07050  702 ASN B CB  
2857 C CG  . ASN A 425 ? 0.59655 1.13895 0.85496 -0.11186 0.15595  0.07450  702 ASN B CG  
2858 O OD1 . ASN A 425 ? 0.59142 1.17624 0.88049 -0.13142 0.15158  0.07117  702 ASN B OD1 
2859 N ND2 . ASN A 425 ? 0.53787 1.05929 0.77951 -0.10993 0.17318  0.08150  702 ASN B ND2 
2860 N N   . PHE A 426 ? 0.51856 0.98305 0.72581 -0.06303 0.10842  0.06106  703 PHE B N   
2861 C CA  . PHE A 426 ? 0.52395 0.97295 0.71960 -0.03971 0.09940  0.06140  703 PHE B CA  
2862 C C   . PHE A 426 ? 0.54835 1.03794 0.76207 -0.03937 0.08397  0.05933  703 PHE B C   
2863 O O   . PHE A 426 ? 0.53618 1.05676 0.76288 -0.01662 0.08214  0.06568  703 PHE B O   
2864 C CB  . PHE A 426 ? 0.55534 0.93988 0.71697 -0.04192 0.09560  0.05780  703 PHE B CB  
2865 C CG  . PHE A 426 ? 0.56103 0.92366 0.70970 -0.02091 0.08775  0.05822  703 PHE B CG  
2866 C CD1 . PHE A 426 ? 0.58734 0.93824 0.73102 0.00293  0.09623  0.06218  703 PHE B CD1 
2867 C CD2 . PHE A 426 ? 0.53593 0.88600 0.67642 -0.02605 0.07349  0.05390  703 PHE B CD2 
2868 C CE1 . PHE A 426 ? 0.48121 0.80881 0.61484 0.02014  0.09108  0.06328  703 PHE B CE1 
2869 C CE2 . PHE A 426 ? 0.57722 0.90664 0.70597 -0.00752 0.06813  0.05596  703 PHE B CE2 
2870 C CZ  . PHE A 426 ? 0.56175 0.87955 0.68818 0.01502  0.07716  0.06135  703 PHE B CZ  
2871 N N   . PHE A 427 ? 0.52815 1.01925 0.74283 -0.06405 0.07345  0.05047  704 PHE B N   
2872 C CA  . PHE A 427 ? 0.52273 1.05449 0.75078 -0.06571 0.05747  0.04573  704 PHE B CA  
2873 C C   . PHE A 427 ? 0.59555 1.20280 0.85937 -0.06053 0.05774  0.05045  704 PHE B C   
2874 O O   . PHE A 427 ? 0.55472 1.20180 0.82877 -0.04384 0.04763  0.05441  704 PHE B O   
2875 C CB  . PHE A 427 ? 0.46735 0.98612 0.69067 -0.09640 0.04839  0.03162  704 PHE B CB  
2876 C CG  . PHE A 427 ? 0.54641 1.00036 0.73666 -0.09659 0.04421  0.02717  704 PHE B CG  
2877 C CD1 . PHE A 427 ? 0.56285 0.98876 0.73341 -0.07079 0.04268  0.03407  704 PHE B CD1 
2878 C CD2 . PHE A 427 ? 0.50230 0.92354 0.68329 -0.12254 0.04291  0.01627  704 PHE B CD2 
2879 C CE1 . PHE A 427 ? 0.54430 0.91570 0.68725 -0.07092 0.03887  0.03024  704 PHE B CE1 
2880 C CE2 . PHE A 427 ? 0.57062 0.93495 0.72296 -0.12052 0.03972  0.01303  704 PHE B CE2 
2881 C CZ  . PHE A 427 ? 0.52036 0.86227 0.65400 -0.09464 0.03719  0.02007  704 PHE B CZ  
2882 N N   . ARG A 428 ? 0.50961 1.14056 0.79347 -0.07369 0.06964  0.05158  705 ARG B N   
2883 C CA  . ARG A 428 ? 0.52782 1.23546 0.84912 -0.06941 0.07044  0.05617  705 ARG B CA  
2884 C C   . ARG A 428 ? 0.54740 1.27135 0.87448 -0.03179 0.07803  0.07032  705 ARG B C   
2885 O O   . ARG A 428 ? 0.58432 1.37441 0.94094 -0.01925 0.07517  0.07672  705 ARG B O   
2886 C CB  . ARG A 428 ? 0.53700 1.26542 0.87967 -0.09403 0.08348  0.05448  705 ARG B CB  
2887 C CG  . ARG A 428 ? 0.52129 1.27910 0.88330 -0.13077 0.07416  0.04097  705 ARG B CG  
2888 C CD  . ARG A 428 ? 0.47450 1.26362 0.86528 -0.15354 0.08898  0.04207  705 ARG B CD  
2889 N NE  . ARG A 428 ? 0.55220 1.28168 0.92134 -0.16012 0.10691  0.04734  705 ARG B NE  
2890 C CZ  . ARG A 428 ? 0.64659 1.32431 0.99881 -0.18583 0.10899  0.04097  705 ARG B CZ  
2891 N NH1 . ARG A 428 ? 0.59086 1.26569 0.94638 -0.20986 0.09564  0.02645  705 ARG B NH1 
2892 N NH2 . ARG A 428 ? 0.68541 1.31314 1.01594 -0.18628 0.12529  0.04933  705 ARG B NH2 
2893 N N   . LYS A 429 ? 0.48063 1.14671 0.78132 -0.01349 0.08784  0.07486  706 LYS B N   
2894 C CA  . LYS A 429 ? 0.48353 1.15492 0.78859 0.02166  0.09763  0.08628  706 LYS B CA  
2895 C C   . LYS A 429 ? 0.58946 1.25722 0.88728 0.04475  0.08619  0.09234  706 LYS B C   
2896 O O   . LYS A 429 ? 0.59761 1.29927 0.91308 0.07250  0.08943  0.10420  706 LYS B O   
2897 C CB  . LYS A 429 ? 0.53425 1.14711 0.81513 0.02875  0.11412  0.08566  706 LYS B CB  
2898 C CG  . LYS A 429 ? 0.55860 1.15390 0.83517 0.06327  0.12443  0.09288  706 LYS B CG  
2899 C CD  . LYS A 429 ? 0.67726 1.24099 0.94070 0.06709  0.14386  0.08973  706 LYS B CD  
2900 C CE  . LYS A 429 ? 0.78213 1.30136 1.02899 0.09402  0.15224  0.09014  706 LYS B CE  
2901 N NZ  . LYS A 429 ? 0.75389 1.24285 0.98420 0.09635  0.16997  0.08338  706 LYS B NZ  
2902 N N   . TYR A 430 ? 0.57014 1.19790 0.84281 0.03527  0.07411  0.08598  707 TYR B N   
2903 C CA  . TYR A 430 ? 0.57715 1.19657 0.83991 0.05682  0.06535  0.09304  707 TYR B CA  
2904 C C   . TYR A 430 ? 0.53651 1.19812 0.80487 0.04755  0.04587  0.09008  707 TYR B C   
2905 O O   . TYR A 430 ? 0.60133 1.26894 0.86420 0.06758  0.03871  0.09888  707 TYR B O   
2906 C CB  . TYR A 430 ? 0.56743 1.11030 0.79631 0.05843  0.06759  0.08937  707 TYR B CB  
2907 C CG  . TYR A 430 ? 0.61476 1.12001 0.83684 0.07207  0.08566  0.09157  707 TYR B CG  
2908 C CD1 . TYR A 430 ? 0.61545 1.12909 0.84949 0.10227  0.09641  0.10263  707 TYR B CD1 
2909 C CD2 . TYR A 430 ? 0.65556 1.11833 0.85915 0.05528  0.09263  0.08235  707 TYR B CD2 
2910 C CE1 . TYR A 430 ? 0.70463 1.18365 0.93198 0.11372  0.11360  0.10103  707 TYR B CE1 
2911 C CE2 . TYR A 430 ? 0.68056 1.11336 0.87574 0.06711  0.10835  0.08196  707 TYR B CE2 
2912 C CZ  . TYR A 430 ? 0.70852 1.14914 0.91564 0.09546  0.11889  0.08960  707 TYR B CZ  
2913 O OH  . TYR A 430 ? 0.66366 1.07368 0.86177 0.10629  0.13529  0.08570  707 TYR B OH  
2914 N N   . ALA A 431 ? 0.54421 1.23570 0.82322 0.01782  0.03791  0.07776  708 ALA B N   
2915 C CA  . ALA A 431 ? 0.53828 1.27139 0.82125 0.00630  0.01890  0.07052  708 ALA B CA  
2916 C C   . ALA A 431 ? 0.54103 1.33254 0.85251 -0.02139 0.01418  0.05966  708 ALA B C   
2917 O O   . ALA A 431 ? 0.54059 1.32568 0.84666 -0.05180 0.00543  0.04248  708 ALA B O   
2918 C CB  . ALA A 431 ? 0.56008 1.23782 0.81085 -0.00819 0.01066  0.05868  708 ALA B CB  
2919 N N   . PRO A 432 ? 0.52553 1.37478 0.86929 -0.01233 0.02052  0.06851  709 PRO B N   
2920 C CA  . PRO A 432 ? 0.52443 1.43351 0.89993 -0.04041 0.01735  0.05834  709 PRO B CA  
2921 C C   . PRO A 432 ? 0.59359 1.57142 0.98305 -0.04892 -0.00412 0.05022  709 PRO B C   
2922 O O   . PRO A 432 ? 0.62773 1.61905 1.00519 -0.02696 -0.01582 0.05699  709 PRO B O   
2923 C CB  . PRO A 432 ? 0.45290 1.40351 0.85800 -0.02092 0.03209  0.07319  709 PRO B CB  
2924 C CG  . PRO A 432 ? 0.44981 1.39518 0.84641 0.02149  0.03376  0.09119  709 PRO B CG  
2925 C CD  . PRO A 432 ? 0.47073 1.33306 0.82559 0.02438  0.03250  0.08807  709 PRO B CD  
2926 N N   . SER A 433 ? 0.56591 1.58990 0.98165 -0.08198 -0.00860 0.03546  710 SER B N   
2927 C CA  . SER A 433 ? 0.57270 1.64393 0.99244 -0.09586 -0.02886 0.02151  710 SER B CA  
2928 C C   . SER A 433 ? 0.63746 1.73890 1.08436 -0.12696 -0.02661 0.00881  710 SER B C   
2929 O O   . SER A 433 ? 0.62027 1.69065 1.07022 -0.16097 -0.01964 -0.00545 710 SER B O   
2930 C CB  . SER A 433 ? 0.56638 1.61063 0.96189 -0.11518 -0.04207 0.00319  710 SER B CB  
2931 O OG  . SER A 433 ? 0.63875 1.72354 1.02553 -0.11051 -0.06157 -0.00370 710 SER B OG  
2932 N N   . GLU A 434 ? 0.67373 1.83355 1.14081 -0.11528 -0.03119 0.01514  711 GLU B N   
2933 C CA  . GLU A 434 ? 0.66041 1.85376 1.15704 -0.14347 -0.02858 0.00433  711 GLU B CA  
2934 C C   . GLU A 434 ? 0.68069 1.85910 1.17484 -0.18767 -0.03664 -0.02335 711 GLU B C   
2935 O O   . GLU A 434 ? 0.68613 1.83902 1.19298 -0.21782 -0.02453 -0.03210 711 GLU B O   
2936 C CB  . GLU A 434 ? 0.63338 1.89864 1.14844 -0.12611 -0.03834 0.01155  711 GLU B CB  
2937 N N   . ASN A 435 ? 0.70810 1.89699 1.18367 -0.19114 -0.05545 -0.03706 712 ASN B N   
2938 C CA  . ASN A 435 ? 0.83404 2.00770 1.30501 -0.23109 -0.06361 -0.06611 712 ASN B CA  
2939 C C   . ASN A 435 ? 0.77221 1.87593 1.21411 -0.24131 -0.06138 -0.07529 712 ASN B C   
2940 O O   . ASN A 435 ? 0.84349 1.92554 1.27570 -0.27070 -0.06802 -0.10009 712 ASN B O   
2941 C CB  . ASN A 435 ? 0.75373 1.98285 1.22085 -0.23149 -0.08476 -0.07941 712 ASN B CB  
2942 N N   . GLY A 436 ? 0.69953 1.76622 1.12790 -0.21804 -0.05128 -0.05670 713 GLY B N   
2943 C CA  . GLY A 436 ? 0.71215 1.71382 1.11544 -0.22767 -0.04776 -0.06368 713 GLY B CA  
2944 C C   . GLY A 436 ? 0.65601 1.60711 1.06716 -0.26035 -0.03026 -0.07091 713 GLY B C   
2945 O O   . GLY A 436 ? 0.68389 1.64846 1.11963 -0.26923 -0.01793 -0.06472 713 GLY B O   
2946 N N   . PRO A 437 ? 0.69970 1.57405 1.08121 -0.27305 -0.02709 -0.08148 714 PRO B N   
2947 C CA  . PRO A 437 ? 0.69216 1.50501 1.07457 -0.30050 -0.00883 -0.08516 714 PRO B CA  
2948 C C   . PRO A 437 ? 0.69053 1.47709 1.07257 -0.28144 0.01072  -0.05964 714 PRO B C   
2949 O O   . PRO A 437 ? 0.70466 1.45239 1.05926 -0.24948 0.01398  -0.04368 714 PRO B O   
2950 C CB  . PRO A 437 ? 0.65698 1.38941 1.00027 -0.30385 -0.01062 -0.09623 714 PRO B CB  
2951 C CG  . PRO A 437 ? 0.71958 1.45566 1.03649 -0.26690 -0.02290 -0.08707 714 PRO B CG  
2952 C CD  . PRO A 437 ? 0.76274 1.59629 1.10551 -0.25877 -0.03803 -0.08745 714 PRO B CD  
2953 N N   . ASN A 438 ? 0.70480 1.51384 1.11779 -0.30242 0.02443  -0.05692 715 ASN B N   
2954 C CA  . ASN A 438 ? 0.69095 1.47838 1.10392 -0.28806 0.04490  -0.03475 715 ASN B CA  
2955 C C   . ASN A 438 ? 0.63280 1.46407 1.05029 -0.24840 0.04336  -0.01661 715 ASN B C   
2956 O O   . ASN A 438 ? 0.55212 1.35228 0.95587 -0.22593 0.05758  0.00066  715 ASN B O   
2957 C CB  . ASN A 438 ? 0.70903 1.40028 1.08212 -0.28236 0.05623  -0.02784 715 ASN B CB  
2958 C CG  . ASN A 438 ? 0.76796 1.41884 1.14708 -0.31542 0.07315  -0.03020 715 ASN B CG  
2959 O OD1 . ASN A 438 ? 0.94321 1.57219 1.31960 -0.31099 0.09156  -0.01359 715 ASN B OD1 
2960 N ND2 . ASN A 438 ? 0.80461 1.44530 1.19165 -0.34852 0.06810  -0.05075 715 ASN B ND2 
2961 N N   . GLY A 439 ? 0.56912 1.47299 1.00545 -0.23896 0.02651  -0.02063 716 GLY B N   
2962 C CA  . GLY A 439 ? 0.55874 1.49944 0.99752 -0.19810 0.02433  -0.00264 716 GLY B CA  
2963 C C   . GLY A 439 ? 0.59835 1.48684 0.99746 -0.16655 0.01907  0.00500  716 GLY B C   
2964 O O   . GLY A 439 ? 0.61273 1.51331 1.01032 -0.13124 0.02226  0.02206  716 GLY B O   
2965 N N   . ILE A 440 ? 0.57888 1.40877 0.94729 -0.17813 0.01247  -0.00706 717 ILE B N   
2966 C CA  . ILE A 440 ? 0.60678 1.38620 0.93851 -0.15135 0.00795  -0.00073 717 ILE B CA  
2967 C C   . ILE A 440 ? 0.64820 1.45671 0.97263 -0.15083 -0.01291 -0.01208 717 ILE B C   
2968 O O   . ILE A 440 ? 0.61277 1.44021 0.94485 -0.18088 -0.02259 -0.03261 717 ILE B O   
2969 C CB  . ILE A 440 ? 0.61449 1.30329 0.91433 -0.16055 0.01782  -0.00340 717 ILE B CB  
2970 C CG1 . ILE A 440 ? 0.58135 1.24525 0.88450 -0.15847 0.03826  0.00913  717 ILE B CG1 
2971 C CG2 . ILE A 440 ? 0.57750 1.21999 0.84279 -0.13530 0.01212  0.00151  717 ILE B CG2 
2972 C CD1 . ILE A 440 ? 0.60565 1.19422 0.88425 -0.17422 0.04796  0.00622  717 ILE B CD1 
2973 N N   . SER A 441 ? 0.56453 1.37557 0.87348 -0.11690 -0.01878 0.00093  718 SER B N   
2974 C CA  . SER A 441 ? 0.57895 1.40953 0.87293 -0.11092 -0.03682 -0.00615 718 SER B CA  
2975 C C   . SER A 441 ? 0.62268 1.40805 0.89544 -0.13989 -0.04232 -0.02926 718 SER B C   
2976 O O   . SER A 441 ? 0.66060 1.36975 0.90927 -0.14237 -0.03293 -0.02965 718 SER B O   
2977 C CB  . SER A 441 ? 0.60367 1.40700 0.87439 -0.07211 -0.03542 0.01330  718 SER B CB  
2978 O OG  . SER A 441 ? 0.64188 1.44923 0.89088 -0.06694 -0.05012 0.00729  718 SER B OG  
2979 N N   . ALA A 442 ? 0.64471 1.47867 0.92691 -0.16164 -0.05742 -0.04946 719 ALA B N   
2980 C CA  . ALA A 442 ? 0.64811 1.44026 0.90950 -0.18747 -0.06256 -0.07388 719 ALA B CA  
2981 C C   . ALA A 442 ? 0.66540 1.40068 0.88738 -0.16541 -0.06376 -0.06851 719 ALA B C   
2982 O O   . ALA A 442 ? 0.65618 1.32526 0.85684 -0.17872 -0.05876 -0.07991 719 ALA B O   
2983 C CB  . ALA A 442 ? 0.64977 1.51082 0.92497 -0.20988 -0.08051 -0.09778 719 ALA B CB  
2984 N N   . GLU A 443 ? 0.67019 1.43071 0.88347 -0.13119 -0.06933 -0.05019 720 GLU B N   
2985 C CA  . GLU A 443 ? 0.65191 1.35993 0.83061 -0.11012 -0.06860 -0.04297 720 GLU B CA  
2986 C C   . GLU A 443 ? 0.69524 1.32252 0.86140 -0.10553 -0.05161 -0.03308 720 GLU B C   
2987 O O   . GLU A 443 ? 0.59383 1.16075 0.73524 -0.11065 -0.04885 -0.04062 720 GLU B O   
2988 C CB  . GLU A 443 ? 0.70098 1.45099 0.87683 -0.07373 -0.07457 -0.02119 720 GLU B CB  
2989 C CG  . GLU A 443 ? 0.72677 1.44281 0.86916 -0.05465 -0.07732 -0.01610 720 GLU B CG  
2990 N N   . VAL A 444 ? 0.61699 1.24513 0.80018 -0.09584 -0.04000 -0.01695 721 VAL B N   
2991 C CA  . VAL A 444 ? 0.59772 1.15676 0.76834 -0.09081 -0.02475 -0.00803 721 VAL B CA  
2992 C C   . VAL A 444 ? 0.61253 1.12684 0.77882 -0.12181 -0.01893 -0.02368 721 VAL B C   
2993 O O   . VAL A 444 ? 0.59156 1.04173 0.73537 -0.12126 -0.01269 -0.02349 721 VAL B O   
2994 C CB  . VAL A 444 ? 0.60900 1.18520 0.79867 -0.07400 -0.01334 0.01010  721 VAL B CB  
2995 C CG1 . VAL A 444 ? 0.49892 1.01305 0.67834 -0.07672 0.00230  0.01456  721 VAL B CG1 
2996 C CG2 . VAL A 444 ? 0.50985 1.10569 0.69752 -0.03851 -0.01494 0.02848  721 VAL B CG2 
2997 N N   . MET A 445 ? 0.65013 1.19830 0.83915 -0.14923 -0.02044 -0.03686 722 MET B N   
2998 C CA  . MET A 445 ? 0.61095 1.11475 0.79836 -0.17925 -0.01266 -0.05014 722 MET B CA  
2999 C C   . MET A 445 ? 0.59882 1.05976 0.76117 -0.18830 -0.01863 -0.06667 722 MET B C   
3000 O O   . MET A 445 ? 0.60733 1.00490 0.75521 -0.19715 -0.00920 -0.06869 722 MET B O   
3001 C CB  . MET A 445 ? 0.51930 1.07172 0.73960 -0.20881 -0.01276 -0.06206 722 MET B CB  
3002 C CG  . MET A 445 ? 0.64178 1.14537 0.86443 -0.23963 -0.00034 -0.07148 722 MET B CG  
3003 S SD  . MET A 445 ? 0.64647 1.08048 0.85202 -0.22611 0.01952  -0.04918 722 MET B SD  
3004 C CE  . MET A 445 ? 0.59399 1.08576 0.82459 -0.20911 0.02587  -0.03023 722 MET B CE  
3005 N N   . ASP A 446 ? 0.60918 1.10548 0.76546 -0.18477 -0.03367 -0.07797 723 ASP B N   
3006 C CA  . ASP A 446 ? 0.61511 1.07409 0.74659 -0.19182 -0.03866 -0.09525 723 ASP B CA  
3007 C C   . ASP A 446 ? 0.61982 1.02056 0.72277 -0.16721 -0.03325 -0.08147 723 ASP B C   
3008 O O   . ASP A 446 ? 0.65261 0.99934 0.73695 -0.17436 -0.02954 -0.09115 723 ASP B O   
3009 C CB  . ASP A 446 ? 0.65216 1.16986 0.78178 -0.19186 -0.05606 -0.10999 723 ASP B CB  
3010 C CG  . ASP A 446 ? 0.84425 1.32676 0.94759 -0.20023 -0.06043 -0.13125 723 ASP B CG  
3011 O OD1 . ASP A 446 ? 0.92015 1.38784 1.02852 -0.23081 -0.05921 -0.15571 723 ASP B OD1 
3012 O OD2 . ASP A 446 ? 0.88944 1.35789 0.96791 -0.17656 -0.06369 -0.12391 723 ASP B OD2 
3013 N N   . THR A 447 ? 0.60561 1.01759 0.70673 -0.13833 -0.03215 -0.05943 724 THR B N   
3014 C CA  . THR A 447 ? 0.54110 0.90219 0.61984 -0.11609 -0.02628 -0.04568 724 THR B CA  
3015 C C   . THR A 447 ? 0.63750 0.94052 0.71234 -0.12324 -0.01280 -0.04085 724 THR B C   
3016 O O   . THR A 447 ? 0.60332 0.85445 0.65790 -0.11737 -0.00891 -0.03950 724 THR B O   
3017 C CB  . THR A 447 ? 0.60225 0.99080 0.68532 -0.08656 -0.02633 -0.02434 724 THR B CB  
3018 O OG1 . THR A 447 ? 0.63445 1.08131 0.72102 -0.07781 -0.03871 -0.02549 724 THR B OG1 
3019 C CG2 . THR A 447 ? 0.61359 0.95257 0.67644 -0.06552 -0.02023 -0.01160 724 THR B CG2 
3020 N N   . TYR A 448 ? 0.61566 0.93015 0.70993 -0.13490 -0.00525 -0.03695 725 TYR B N   
3021 C CA  . TYR A 448 ? 0.54675 0.81221 0.63618 -0.13971 0.00812  -0.02935 725 TYR B CA  
3022 C C   . TYR A 448 ? 0.64569 0.86830 0.72794 -0.16294 0.01190  -0.04294 725 TYR B C   
3023 O O   . TYR A 448 ? 0.63237 0.80110 0.69721 -0.15856 0.01889  -0.03747 725 TYR B O   
3024 C CB  . TYR A 448 ? 0.58019 0.87419 0.69173 -0.14405 0.01653  -0.02011 725 TYR B CB  
3025 C CG  . TYR A 448 ? 0.60380 0.85472 0.71023 -0.15100 0.03091  -0.01193 725 TYR B CG  
3026 C CD1 . TYR A 448 ? 0.59603 0.81061 0.68378 -0.13180 0.03679  0.00093  725 TYR B CD1 
3027 C CD2 . TYR A 448 ? 0.64843 0.89718 0.76892 -0.17720 0.03889  -0.01682 725 TYR B CD2 
3028 C CE1 . TYR A 448 ? 0.60308 0.78363 0.68368 -0.13678 0.04906  0.00926  725 TYR B CE1 
3029 C CE2 . TYR A 448 ? 0.65479 0.86557 0.76889 -0.18209 0.05313  -0.00625 725 TYR B CE2 
3030 C CZ  . TYR A 448 ? 0.67810 0.85663 0.77089 -0.16083 0.05754  0.00709  725 TYR B CZ  
3031 O OH  . TYR A 448 ? 0.66789 0.81379 0.75176 -0.16418 0.07079  0.01845  725 TYR B OH  
3032 N N   . VAL A 449 ? 0.58375 0.82974 0.67993 -0.18747 0.00764  -0.06112 726 VAL B N   
3033 C CA  . VAL A 449 ? 0.67017 0.87152 0.76105 -0.21028 0.01291  -0.07600 726 VAL B CA  
3034 C C   . VAL A 449 ? 0.65574 0.81500 0.71958 -0.19789 0.00950  -0.08137 726 VAL B C   
3035 O O   . VAL A 449 ? 0.66595 0.76799 0.71712 -0.19972 0.01861  -0.07941 726 VAL B O   
3036 C CB  . VAL A 449 ? 0.67388 0.91169 0.78563 -0.24007 0.00782  -0.09880 726 VAL B CB  
3037 C CG1 . VAL A 449 ? 0.69978 0.88613 0.80332 -0.26128 0.01315  -0.11754 726 VAL B CG1 
3038 C CG2 . VAL A 449 ? 0.70129 0.97172 0.84221 -0.25636 0.01503  -0.09298 726 VAL B CG2 
3039 N N   . LYS A 450 ? 0.67003 0.85916 0.72513 -0.18406 -0.00292 -0.08690 727 LYS B N   
3040 C CA  . LYS A 450 ? 0.69300 0.84799 0.72345 -0.17212 -0.00551 -0.09237 727 LYS B CA  
3041 C C   . LYS A 450 ? 0.71026 0.82226 0.72584 -0.15005 0.00164  -0.07226 727 LYS B C   
3042 O O   . LYS A 450 ? 0.71840 0.78080 0.71925 -0.14863 0.00711  -0.07433 727 LYS B O   
3043 C CB  . LYS A 450 ? 0.72390 0.92546 0.74769 -0.15993 -0.01918 -0.09867 727 LYS B CB  
3044 C CG  . LYS A 450 ? 0.72587 0.96932 0.75923 -0.18251 -0.02835 -0.12351 727 LYS B CG  
3045 C CD  . LYS A 450 ? 0.70145 0.99656 0.72571 -0.16795 -0.04226 -0.12697 727 LYS B CD  
3046 C CE  . LYS A 450 ? 0.78448 1.12669 0.81754 -0.19183 -0.05284 -0.15403 727 LYS B CE  
3047 N NZ  . LYS A 450 ? 0.91619 1.31106 0.93629 -0.17546 -0.06672 -0.15596 727 LYS B NZ  
3048 N N   . SER A 451 ? 0.66702 0.79821 0.68692 -0.13227 0.00191  -0.05348 728 SER B N   
3049 C CA  . SER A 451 ? 0.67651 0.77059 0.68233 -0.11279 0.00730  -0.03776 728 SER B CA  
3050 C C   . SER A 451 ? 0.72390 0.77398 0.72772 -0.12156 0.01859  -0.03187 728 SER B C   
3051 O O   . SER A 451 ? 0.72824 0.73818 0.71705 -0.11155 0.02225  -0.02584 728 SER B O   
3052 C CB  . SER A 451 ? 0.58353 0.70468 0.59439 -0.09265 0.00622  -0.02170 728 SER B CB  
3053 O OG  . SER A 451 ? 0.60746 0.75544 0.63645 -0.09924 0.01025  -0.01633 728 SER B OG  
3054 N N   . CYS A 452 ? 0.62601 0.68502 0.64523 -0.13991 0.02458  -0.03257 729 CYS B N   
3055 C CA  . CYS A 452 ? 0.66767 0.68448 0.68428 -0.14988 0.03661  -0.02622 729 CYS B CA  
3056 C C   . CYS A 452 ? 0.67832 0.65054 0.68430 -0.15805 0.03929  -0.03707 729 CYS B C   
3057 O O   . CYS A 452 ? 0.66337 0.59220 0.65608 -0.14982 0.04592  -0.02751 729 CYS B O   
3058 C CB  . CYS A 452 ? 0.71523 0.75182 0.75251 -0.17107 0.04383  -0.02620 729 CYS B CB  
3059 S SG  . CYS A 452 ? 0.69904 0.77856 0.74919 -0.16153 0.04675  -0.01065 729 CYS B SG  
3060 N N   . ALA A 453 ? 0.70205 0.68547 0.71403 -0.17408 0.03460  -0.05778 730 ALA B N   
3061 C CA  . ALA A 453 ? 0.74178 0.68065 0.74364 -0.18150 0.03857  -0.07110 730 ALA B CA  
3062 C C   . ALA A 453 ? 0.72994 0.64491 0.71077 -0.15719 0.03558  -0.06606 730 ALA B C   
3063 O O   . ALA A 453 ? 0.74522 0.61202 0.71571 -0.15212 0.04370  -0.06121 730 ALA B O   
3064 C CB  . ALA A 453 ? 0.77008 0.73185 0.78011 -0.20197 0.03229  -0.09806 730 ALA B CB  
3065 N N   . GLY A 454 ? 0.72713 0.67655 0.70288 -0.14106 0.02486  -0.06532 731 GLY B N   
3066 C CA  . GLY A 454 ? 0.70746 0.63868 0.66607 -0.11943 0.02270  -0.06059 731 GLY B CA  
3067 C C   . GLY A 454 ? 0.68882 0.58876 0.64123 -0.10529 0.02935  -0.04045 731 GLY B C   
3068 O O   . GLY A 454 ? 0.72879 0.59277 0.67002 -0.09618 0.03335  -0.03828 731 GLY B O   
3069 N N   . TYR A 455 ? 0.68756 0.60333 0.64715 -0.10277 0.03072  -0.02601 732 TYR B N   
3070 C CA  . TYR A 455 ? 0.67799 0.57080 0.62964 -0.08884 0.03529  -0.00858 732 TYR B CA  
3071 C C   . TYR A 455 ? 0.70652 0.55908 0.65523 -0.09688 0.04586  -0.00268 732 TYR B C   
3072 O O   . TYR A 455 ? 0.71092 0.53620 0.64896 -0.08400 0.04885  0.00796  732 TYR B O   
3073 C CB  . TYR A 455 ? 0.63862 0.56053 0.59616 -0.08200 0.03398  0.00282  732 TYR B CB  
3074 C CG  . TYR A 455 ? 0.64098 0.58456 0.59638 -0.06500 0.02636  0.00395  732 TYR B CG  
3075 C CD1 . TYR A 455 ? 0.58875 0.51573 0.53447 -0.04907 0.02569  0.01143  732 TYR B CD1 
3076 C CD2 . TYR A 455 ? 0.54011 0.52183 0.50439 -0.06499 0.02037  -0.00168 732 TYR B CD2 
3077 C CE1 . TYR A 455 ? 0.52543 0.46947 0.47130 -0.03513 0.02074  0.01306  732 TYR B CE1 
3078 C CE2 . TYR A 455 ? 0.51848 0.51664 0.48106 -0.04875 0.01559  0.00214  732 TYR B CE2 
3079 C CZ  . TYR A 455 ? 0.54745 0.52460 0.50125 -0.03476 0.01657  0.00935  732 TYR B CZ  
3080 O OH  . TYR A 455 ? 0.59935 0.59071 0.55367 -0.02026 0.01377  0.01386  732 TYR B OH  
3081 N N   . CYS A 456 ? 0.70969 0.55855 0.66877 -0.11783 0.05204  -0.00889 733 CYS B N   
3082 C CA  . CYS A 456 ? 0.67989 0.48554 0.63694 -0.12576 0.06441  -0.00214 733 CYS B CA  
3083 C C   . CYS A 456 ? 0.79674 0.56210 0.74337 -0.11889 0.06693  -0.00815 733 CYS B C   
3084 O O   . CYS A 456 ? 0.84592 0.57475 0.78475 -0.11031 0.07516  0.00560  733 CYS B O   
3085 C CB  . CYS A 456 ? 0.79190 0.60016 0.76522 -0.15247 0.07167  -0.01036 733 CYS B CB  
3086 S SG  . CYS A 456 ? 0.97285 0.81479 0.95778 -0.15868 0.07614  0.00518  733 CYS B SG  
3087 N N   . VAL A 457 ? 0.80653 0.57961 0.75239 -0.12123 0.06052  -0.02810 734 VAL B N   
3088 C CA  . VAL A 457 ? 0.80229 0.53750 0.73835 -0.11426 0.06447  -0.03594 734 VAL B CA  
3089 C C   . VAL A 457 ? 0.79361 0.52775 0.71786 -0.08788 0.06000  -0.02342 734 VAL B C   
3090 O O   . VAL A 457 ? 0.74235 0.44092 0.65966 -0.07600 0.06680  -0.01465 734 VAL B O   
3091 C CB  . VAL A 457 ? 0.83707 0.58283 0.77433 -0.12675 0.05993  -0.06381 734 VAL B CB  
3092 C CG1 . VAL A 457 ? 0.70402 0.41327 0.62936 -0.11677 0.06447  -0.07406 734 VAL B CG1 
3093 C CG2 . VAL A 457 ? 0.85133 0.59589 0.80308 -0.15584 0.06525  -0.07767 734 VAL B CG2 
3094 N N   . ILE A 458 ? 0.73859 0.51227 0.66235 -0.07821 0.04937  -0.02119 735 ILE B N   
3095 C CA  . ILE A 458 ? 0.76182 0.53731 0.67736 -0.05607 0.04521  -0.01245 735 ILE B CA  
3096 C C   . ILE A 458 ? 0.77224 0.53454 0.68496 -0.04492 0.04855  0.00866  735 ILE B C   
3097 O O   . ILE A 458 ? 0.81673 0.56050 0.72332 -0.02978 0.05027  0.01626  735 ILE B O   
3098 C CB  . ILE A 458 ? 0.76278 0.58072 0.68015 -0.05003 0.03507  -0.01528 735 ILE B CB  
3099 C CG1 . ILE A 458 ? 0.69865 0.52871 0.61347 -0.05538 0.03142  -0.03484 735 ILE B CG1 
3100 C CG2 . ILE A 458 ? 0.65629 0.47781 0.56936 -0.02992 0.03214  -0.00334 735 ILE B CG2 
3101 C CD1 . ILE A 458 ? 0.64426 0.52034 0.56225 -0.05234 0.02232  -0.03657 735 ILE B CD1 
3102 N N   . THR A 459 ? 0.77321 0.54719 0.69004 -0.05172 0.04980  0.01833  736 THR B N   
3103 C CA  . THR A 459 ? 0.76567 0.53070 0.67669 -0.04110 0.05254  0.03742  736 THR B CA  
3104 C C   . THR A 459 ? 0.78796 0.51184 0.69442 -0.04071 0.06310  0.04640  736 THR B C   
3105 O O   . THR A 459 ? 0.79337 0.50585 0.69247 -0.02529 0.06419  0.06122  736 THR B O   
3106 C CB  . THR A 459 ? 0.73080 0.52000 0.64507 -0.04725 0.05244  0.04493  736 THR B CB  
3107 O OG1 . THR A 459 ? 0.69607 0.48146 0.61815 -0.06644 0.05943  0.04118  736 THR B OG1 
3108 C CG2 . THR A 459 ? 0.66202 0.48829 0.58123 -0.04325 0.04348  0.03863  736 THR B CG2 
3109 N N   . TYR A 460 ? 0.81061 0.51226 0.72232 -0.05714 0.07133  0.03787  737 TYR B N   
3110 C CA  . TYR A 460 ? 0.79687 0.45231 0.70551 -0.05556 0.08359  0.04557  737 TYR B CA  
3111 C C   . TYR A 460 ? 0.82713 0.46389 0.72958 -0.03690 0.08274  0.04371  737 TYR B C   
3112 O O   . TYR A 460 ? 0.84318 0.46124 0.73977 -0.02030 0.08696  0.06124  737 TYR B O   
3113 C CB  . TYR A 460 ? 0.83358 0.46711 0.75167 -0.07938 0.09311  0.03171  737 TYR B CB  
3114 C CG  . TYR A 460 ? 0.91896 0.49899 0.83570 -0.07829 0.10631  0.03071  737 TYR B CG  
3115 C CD1 . TYR A 460 ? 0.97587 0.52067 0.89019 -0.07325 0.11957  0.05310  737 TYR B CD1 
3116 C CD2 . TYR A 460 ? 0.91787 0.48214 0.83497 -0.08110 0.10665  0.00777  737 TYR B CD2 
3117 C CE1 . TYR A 460 ? 1.04175 0.53349 0.95613 -0.07027 0.13372  0.05374  737 TYR B CE1 
3118 C CE2 . TYR A 460 ? 0.94432 0.45586 0.86062 -0.07914 0.12059  0.00512  737 TYR B CE2 
3119 C CZ  . TYR A 460 ? 1.03056 0.50426 0.94661 -0.07346 0.13455  0.02865  737 TYR B CZ  
3120 O OH  . TYR A 460 ? 1.04641 0.46385 0.96303 -0.06985 0.15041  0.02755  737 TYR B OH  
3121 N N   . ILE A 461 ? 0.80857 0.45445 0.71209 -0.03796 0.07726  0.02354  738 ILE B N   
3122 C CA  . ILE A 461 ? 0.81932 0.44926 0.71774 -0.02046 0.07809  0.02038  738 ILE B CA  
3123 C C   . ILE A 461 ? 0.81722 0.46563 0.71215 0.00144  0.07150  0.03807  738 ILE B C   
3124 O O   . ILE A 461 ? 0.73380 0.36244 0.62609 0.01864  0.07598  0.04837  738 ILE B O   
3125 C CB  . ILE A 461 ? 0.82723 0.47273 0.72532 -0.02577 0.07268  -0.00410 738 ILE B CB  
3126 C CG1 . ILE A 461 ? 0.83170 0.45082 0.73219 -0.04559 0.08084  -0.02457 738 ILE B CG1 
3127 C CG2 . ILE A 461 ? 0.81773 0.46323 0.71067 -0.00488 0.07111  -0.00498 738 ILE B CG2 
3128 C CD1 . ILE A 461 ? 0.81767 0.46323 0.71654 -0.05489 0.07336  -0.04963 738 ILE B CD1 
3129 N N   . LEU A 462 ? 0.74613 0.43362 0.64245 0.00123  0.06112  0.04099  739 LEU B N   
3130 C CA  . LEU A 462 ? 0.75021 0.45803 0.64510 0.01836  0.05432  0.05412  739 LEU B CA  
3131 C C   . LEU A 462 ? 0.74695 0.45284 0.63763 0.02298  0.05598  0.07430  739 LEU B C   
3132 O O   . LEU A 462 ? 0.66026 0.38615 0.54946 0.03563  0.04952  0.08415  739 LEU B O   
3133 C CB  . LEU A 462 ? 0.67680 0.42358 0.57554 0.01639  0.04417  0.04746  739 LEU B CB  
3134 C CG  . LEU A 462 ? 0.75329 0.50998 0.65420 0.01415  0.04165  0.03065  739 LEU B CG  
3135 C CD1 . LEU A 462 ? 0.69517 0.48800 0.60064 0.01361  0.03359  0.02870  739 LEU B CD1 
3136 C CD2 . LEU A 462 ? 0.71638 0.46053 0.61567 0.02907  0.04419  0.02925  739 LEU B CD2 
3137 N N   . GLY A 463 ? 0.72420 0.40877 0.61294 0.01258  0.06467  0.08049  740 GLY B N   
3138 C CA  . GLY A 463 ? 0.76016 0.44280 0.64205 0.01861  0.06772  0.10192  740 GLY B CA  
3139 C C   . GLY A 463 ? 0.75081 0.47233 0.62956 0.01979  0.05829  0.10600  740 GLY B C   
3140 O O   . GLY A 463 ? 0.77828 0.51052 0.64985 0.03290  0.05511  0.12058  740 GLY B O   
3141 N N   . VAL A 464 ? 0.68436 0.42866 0.56849 0.00715  0.05378  0.09267  741 VAL B N   
3142 C CA  . VAL A 464 ? 0.67562 0.45337 0.55776 0.00785  0.04677  0.09386  741 VAL B CA  
3143 C C   . VAL A 464 ? 0.72154 0.50011 0.59503 0.00414  0.05271  0.10795  741 VAL B C   
3144 O O   . VAL A 464 ? 0.82457 0.58714 0.69974 -0.00805 0.06214  0.11064  741 VAL B O   
3145 C CB  . VAL A 464 ? 0.71191 0.51082 0.60341 -0.00273 0.04274  0.07778  741 VAL B CB  
3146 C CG1 . VAL A 464 ? 0.61182 0.44014 0.50198 -0.00272 0.03882  0.07864  741 VAL B CG1 
3147 C CG2 . VAL A 464 ? 0.64280 0.44531 0.54051 0.00279  0.03710  0.06606  741 VAL B CG2 
3148 N N   . GLY A 465 ? 0.69749 0.49626 0.56163 0.01380  0.04779  0.11658  742 GLY B N   
3149 C CA  . GLY A 465 ? 0.72950 0.53429 0.58192 0.01230  0.05319  0.13023  742 GLY B CA  
3150 C C   . GLY A 465 ? 0.69936 0.53660 0.54930 0.00841  0.04905  0.12256  742 GLY B C   
3151 O O   . GLY A 465 ? 0.66284 0.51490 0.52259 0.00533  0.04333  0.10699  742 GLY B O   
3152 N N   . ASP A 466 ? 0.80982 0.65718 0.64569 0.00982  0.05325  0.13449  743 ASP B N   
3153 C CA  . ASP A 466 ? 0.70191 0.57869 0.53249 0.00738  0.05144  0.12708  743 ASP B CA  
3154 C C   . ASP A 466 ? 0.72247 0.60585 0.56792 -0.00545 0.05501  0.11327  743 ASP B C   
3155 O O   . ASP A 466 ? 0.76624 0.66901 0.61670 -0.00513 0.05046  0.09985  743 ASP B O   
3156 C CB  . ASP A 466 ? 0.79169 0.68972 0.61919 0.01704  0.03938  0.11768  743 ASP B CB  
3157 C CG  . ASP A 466 ? 0.78114 0.70647 0.59807 0.01636  0.03888  0.11095  743 ASP B CG  
3158 O OD1 . ASP A 466 ? 0.79790 0.72839 0.60151 0.01434  0.04695  0.12094  743 ASP B OD1 
3159 O OD2 . ASP A 466 ? 0.81737 0.75779 0.63965 0.01758  0.03170  0.09522  743 ASP B OD2 
3160 N N   . ARG A 467 ? 0.72715 0.59455 0.58123 -0.01674 0.06364  0.11666  744 ARG B N   
3161 C CA  . ARG A 467 ? 0.64917 0.52702 0.51953 -0.02916 0.06651  0.10493  744 ARG B CA  
3162 C C   . ARG A 467 ? 0.69815 0.59525 0.56510 -0.03492 0.07547  0.10939  744 ARG B C   
3163 O O   . ARG A 467 ? 0.78884 0.67716 0.64809 -0.03915 0.08536  0.12402  744 ARG B O   
3164 C CB  . ARG A 467 ? 0.75283 0.60830 0.63544 -0.04077 0.07102  0.10371  744 ARG B CB  
3165 C CG  . ARG A 467 ? 0.69753 0.53525 0.58416 -0.03552 0.06370  0.09642  744 ARG B CG  
3166 C CD  . ARG A 467 ? 0.67982 0.53822 0.57497 -0.03161 0.05404  0.08147  744 ARG B CD  
3167 N NE  . ARG A 467 ? 0.61125 0.47971 0.49836 -0.01778 0.04693  0.08217  744 ARG B NE  
3168 C CZ  . ARG A 467 ? 0.64610 0.53236 0.53956 -0.01340 0.04076  0.07202  744 ARG B CZ  
3169 N NH1 . ARG A 467 ? 0.59365 0.49153 0.50005 -0.01877 0.04031  0.06266  744 ARG B NH1 
3170 N NH2 . ARG A 467 ? 0.59661 0.49036 0.48417 -0.00349 0.03529  0.07169  744 ARG B NH2 
3171 N N   . HIS A 468 ? 0.66107 0.58356 0.53392 -0.03404 0.07359  0.09795  745 HIS B N   
3172 C CA  . HIS A 468 ? 0.66492 0.60880 0.53703 -0.03846 0.08315  0.09985  745 HIS B CA  
3173 C C   . HIS A 468 ? 0.65374 0.61857 0.54554 -0.04130 0.08216  0.08602  745 HIS B C   
3174 O O   . HIS A 468 ? 0.68854 0.65130 0.59161 -0.03908 0.07381  0.07646  745 HIS B O   
3175 C CB  . HIS A 468 ? 0.59887 0.55481 0.44883 -0.02810 0.08384  0.10331  745 HIS B CB  
3176 C CG  . HIS A 468 ? 0.81255 0.77254 0.65757 -0.01709 0.07234  0.09154  745 HIS B CG  
3177 N ND1 . HIS A 468 ? 0.79159 0.76238 0.64997 -0.01499 0.06870  0.07565  745 HIS B ND1 
3178 C CD2 . HIS A 468 ? 0.83132 0.78688 0.66168 -0.00803 0.06421  0.09390  745 HIS B CD2 
3179 C CE1 . HIS A 468 ? 0.82432 0.79419 0.67710 -0.00699 0.05979  0.06800  745 HIS B CE1 
3180 N NE2 . HIS A 468 ? 0.89872 0.86187 0.73517 -0.00313 0.05607  0.07798  745 HIS B NE2 
3181 N N   . LEU A 469 ? 0.61902 0.60618 0.51521 -0.04481 0.09155  0.08636  746 LEU B N   
3182 C CA  . LEU A 469 ? 0.64079 0.65070 0.55878 -0.04693 0.09220  0.07657  746 LEU B CA  
3183 C C   . LEU A 469 ? 0.71046 0.72907 0.62957 -0.03344 0.08661  0.06499  746 LEU B C   
3184 O O   . LEU A 469 ? 0.64594 0.68209 0.58310 -0.03139 0.08675  0.05860  746 LEU B O   
3185 C CB  . LEU A 469 ? 0.64938 0.68267 0.57483 -0.05442 0.10545  0.08158  746 LEU B CB  
3186 C CG  . LEU A 469 ? 0.64083 0.66313 0.56931 -0.07049 0.11286  0.09338  746 LEU B CG  
3187 C CD1 . LEU A 469 ? 0.70765 0.75441 0.64389 -0.07885 0.12777  0.10025  746 LEU B CD1 
3188 C CD2 . LEU A 469 ? 0.58412 0.59876 0.53168 -0.08162 0.10619  0.08734  746 LEU B CD2 
3189 N N   . ASP A 470 ? 0.65875 0.66593 0.56056 -0.02436 0.08189  0.06250  747 ASP B N   
3190 C CA  . ASP A 470 ? 0.61002 0.61887 0.51472 -0.01397 0.07690  0.05074  747 ASP B CA  
3191 C C   . ASP A 470 ? 0.66936 0.66359 0.58144 -0.01176 0.06635  0.04784  747 ASP B C   
3192 O O   . ASP A 470 ? 0.67708 0.67313 0.59772 -0.00457 0.06395  0.03980  747 ASP B O   
3193 C CB  . ASP A 470 ? 0.72126 0.72870 0.60538 -0.00737 0.07673  0.04625  747 ASP B CB  
3194 C CG  . ASP A 470 ? 0.92699 0.95274 0.80474 -0.00543 0.08803  0.04303  747 ASP B CG  
3195 O OD1 . ASP A 470 ? 0.96538 1.00394 0.85999 -0.00317 0.09438  0.03793  747 ASP B OD1 
3196 O OD2 . ASP A 470 ? 1.13856 1.16803 0.99436 -0.00500 0.09108  0.04652  747 ASP B OD2 
3197 N N   . ASN A 471 ? 0.62014 0.59843 0.52884 -0.01680 0.06141  0.05439  748 ASN B N   
3198 C CA  . ASN A 471 ? 0.65190 0.61908 0.56805 -0.01416 0.05285  0.05101  748 ASN B CA  
3199 C C   . ASN A 471 ? 0.60493 0.57200 0.53325 -0.02269 0.05227  0.05221  748 ASN B C   
3200 O O   . ASN A 471 ? 0.60710 0.56198 0.53719 -0.02242 0.04625  0.05071  748 ASN B O   
3201 C CB  . ASN A 471 ? 0.61468 0.56416 0.51788 -0.00986 0.04639  0.05392  748 ASN B CB  
3202 C CG  . ASN A 471 ? 0.67651 0.61438 0.56630 -0.01382 0.04921  0.06535  748 ASN B CG  
3203 O OD1 . ASN A 471 ? 0.73973 0.67319 0.63321 -0.02285 0.05491  0.07095  748 ASN B OD1 
3204 N ND2 . ASN A 471 ? 0.73440 0.66840 0.60936 -0.00717 0.04572  0.06948  748 ASN B ND2 
3205 N N   . LEU A 472 ? 0.63098 0.61405 0.56814 -0.03073 0.05874  0.05358  749 LEU B N   
3206 C CA  . LEU A 472 ? 0.61670 0.61125 0.56987 -0.03977 0.05771  0.05076  749 LEU B CA  
3207 C C   . LEU A 472 ? 0.61065 0.63463 0.57909 -0.03366 0.05877  0.04681  749 LEU B C   
3208 O O   . LEU A 472 ? 0.58956 0.62901 0.56047 -0.03170 0.06646  0.04844  749 LEU B O   
3209 C CB  . LEU A 472 ? 0.55993 0.55398 0.51542 -0.05499 0.06508  0.05588  749 LEU B CB  
3210 C CG  . LEU A 472 ? 0.72752 0.72634 0.69734 -0.06928 0.06329  0.05080  749 LEU B CG  
3211 C CD1 . LEU A 472 ? 0.68809 0.65949 0.65037 -0.06872 0.05640  0.04694  749 LEU B CD1 
3212 C CD2 . LEU A 472 ? 0.72279 0.72219 0.69832 -0.08627 0.07349  0.05616  749 LEU B CD2 
3213 N N   . LEU A 473 ? 0.50183 0.53431 0.47984 -0.02907 0.05211  0.04271  750 LEU B N   
3214 C CA  . LEU A 473 ? 0.56062 0.61869 0.55262 -0.01861 0.05310  0.04191  750 LEU B CA  
3215 C C   . LEU A 473 ? 0.58797 0.67658 0.59698 -0.02408 0.04970  0.04057  750 LEU B C   
3216 O O   . LEU A 473 ? 0.58135 0.66787 0.59014 -0.03468 0.04376  0.03673  750 LEU B O   
3217 C CB  . LEU A 473 ? 0.50459 0.55070 0.49364 -0.00458 0.04930  0.04104  750 LEU B CB  
3218 C CG  . LEU A 473 ? 0.55622 0.59069 0.53895 0.00457  0.05509  0.03986  750 LEU B CG  
3219 C CD1 . LEU A 473 ? 0.54229 0.55973 0.50821 -0.00199 0.05658  0.03955  750 LEU B CD1 
3220 C CD2 . LEU A 473 ? 0.65974 0.68020 0.64272 0.01533  0.05229  0.03855  750 LEU B CD2 
3221 N N   . LEU A 474 ? 0.54014 0.65918 0.56444 -0.01586 0.05348  0.04289  751 LEU B N   
3222 C CA  . LEU A 474 ? 0.54121 0.69896 0.58388 -0.02080 0.05006  0.04231  751 LEU B CA  
3223 C C   . LEU A 474 ? 0.52681 0.70929 0.58147 -0.00192 0.04890  0.04712  751 LEU B C   
3224 O O   . LEU A 474 ? 0.60331 0.77742 0.65795 0.01321  0.05597  0.05104  751 LEU B O   
3225 C CB  . LEU A 474 ? 0.58675 0.76690 0.64128 -0.03202 0.05797  0.04323  751 LEU B CB  
3226 C CG  . LEU A 474 ? 0.63948 0.85557 0.71225 -0.04743 0.05364  0.03946  751 LEU B CG  
3227 C CD1 . LEU A 474 ? 0.63422 0.82736 0.69682 -0.06305 0.04584  0.03168  751 LEU B CD1 
3228 C CD2 . LEU A 474 ? 0.59576 0.83086 0.68098 -0.05917 0.06407  0.04176  751 LEU B CD2 
3229 N N   . THR A 475 ? 0.50573 0.71862 0.57027 -0.00249 0.04056  0.04676  752 THR B N   
3230 C CA  . THR A 475 ? 0.56295 0.80746 0.64095 0.01647  0.03982  0.05481  752 THR B CA  
3231 C C   . THR A 475 ? 0.58519 0.88386 0.68568 0.01246  0.03854  0.05586  752 THR B C   
3232 O O   . THR A 475 ? 0.59566 0.90876 0.70132 -0.00831 0.03540  0.04807  752 THR B O   
3233 C CB  . THR A 475 ? 0.54521 0.78904 0.61546 0.02400  0.03061  0.05652  752 THR B CB  
3234 O OG1 . THR A 475 ? 0.57684 0.84993 0.64981 0.00995  0.02000  0.04908  752 THR B OG1 
3235 C CG2 . THR A 475 ? 0.48833 0.68303 0.53836 0.02368  0.03059  0.05385  752 THR B CG2 
3236 N N   . LYS A 476 ? 0.54527 0.87444 0.66119 0.03285  0.04192  0.06612  753 LYS B N   
3237 C CA  . LYS A 476 ? 0.60815 0.99685 0.74843 0.03309  0.03988  0.06916  753 LYS B CA  
3238 C C   . LYS A 476 ? 0.56370 0.98839 0.70676 0.02252  0.02462  0.06383  753 LYS B C   
3239 O O   . LYS A 476 ? 0.56301 1.03733 0.72546 0.01193  0.02028  0.06041  753 LYS B O   
3240 C CB  . LYS A 476 ? 0.62990 1.04054 0.78553 0.06179  0.04775  0.08361  753 LYS B CB  
3241 C CG  . LYS A 476 ? 0.66209 1.04737 0.81913 0.07028  0.06419  0.08510  753 LYS B CG  
3242 C CD  . LYS A 476 ? 0.74960 1.13397 0.91569 0.10070  0.07417  0.09786  753 LYS B CD  
3243 C CE  . LYS A 476 ? 0.85149 1.20075 1.01360 0.10715  0.09088  0.09423  753 LYS B CE  
3244 N NZ  . LYS A 476 ? 0.94034 1.30045 1.11994 0.13560  0.10432  0.10506  753 LYS B NZ  
3245 N N   . THR A 477 ? 0.54796 0.95073 0.67229 0.02381  0.01666  0.06150  754 THR B N   
3246 C CA  . THR A 477 ? 0.58738 1.02020 0.70943 0.01174  0.00239  0.05246  754 THR B CA  
3247 C C   . THR A 477 ? 0.57871 0.99359 0.69494 -0.01913 -0.00077 0.03428  754 THR B C   
3248 O O   . THR A 477 ? 0.57723 1.01392 0.69160 -0.03317 -0.01180 0.02213  754 THR B O   
3249 C CB  . THR A 477 ? 0.49556 0.91160 0.59825 0.02571  -0.00309 0.05689  754 THR B CB  
3250 O OG1 . THR A 477 ? 0.63277 0.98599 0.71575 0.02224  0.00244  0.05343  754 THR B OG1 
3251 C CG2 . THR A 477 ? 0.43499 0.86924 0.54513 0.05597  0.00116  0.07684  754 THR B CG2 
3252 N N   . GLY A 478 ? 0.52015 0.89521 0.63254 -0.02950 0.00925  0.03211  755 GLY B N   
3253 C CA  . GLY A 478 ? 0.51724 0.87065 0.62546 -0.05701 0.00931  0.01845  755 GLY B CA  
3254 C C   . GLY A 478 ? 0.56295 0.85739 0.64589 -0.06113 0.00962  0.01330  755 GLY B C   
3255 O O   . GLY A 478 ? 0.56479 0.83639 0.64363 -0.08232 0.01077  0.00303  755 GLY B O   
3256 N N   . LYS A 479 ? 0.53645 0.80589 0.60425 -0.04151 0.00958  0.02069  756 LYS B N   
3257 C CA  . LYS A 479 ? 0.53816 0.75663 0.58436 -0.04372 0.00984  0.01670  756 LYS B CA  
3258 C C   . LYS A 479 ? 0.57465 0.75398 0.61459 -0.04696 0.01997  0.02067  756 LYS B C   
3259 O O   . LYS A 479 ? 0.61412 0.79334 0.65764 -0.03512 0.02696  0.02958  756 LYS B O   
3260 C CB  . LYS A 479 ? 0.54778 0.75637 0.58249 -0.02286 0.00714  0.02373  756 LYS B CB  
3261 C CG  . LYS A 479 ? 0.58694 0.83012 0.62082 -0.01695 -0.00276 0.02169  756 LYS B CG  
3262 C CD  . LYS A 479 ? 0.63154 0.85117 0.64911 -0.00131 -0.00334 0.02726  756 LYS B CD  
3263 C CE  . LYS A 479 ? 0.94417 1.20137 0.95827 0.00631  -0.01214 0.02733  756 LYS B CE  
3264 N NZ  . LYS A 479 ? 1.03652 1.27208 1.03443 0.02018  -0.01127 0.03315  756 LYS B NZ  
3265 N N   . LEU A 480 ? 0.50944 0.65638 0.53946 -0.06231 0.02127  0.01390  757 LEU B N   
3266 C CA  . LEU A 480 ? 0.52892 0.63671 0.54784 -0.06333 0.02928  0.01901  757 LEU B CA  
3267 C C   . LEU A 480 ? 0.58196 0.65293 0.58264 -0.05572 0.02631  0.01832  757 LEU B C   
3268 O O   . LEU A 480 ? 0.61329 0.68015 0.60921 -0.05942 0.02040  0.01021  757 LEU B O   
3269 C CB  . LEU A 480 ? 0.59432 0.69189 0.61694 -0.08472 0.03513  0.01569  757 LEU B CB  
3270 C CG  . LEU A 480 ? 0.68722 0.74395 0.69533 -0.08537 0.04315  0.02296  757 LEU B CG  
3271 C CD1 . LEU A 480 ? 0.67374 0.73560 0.69025 -0.09964 0.05353  0.02777  757 LEU B CD1 
3272 C CD2 . LEU A 480 ? 0.62892 0.64802 0.62370 -0.08967 0.04074  0.01805  757 LEU B CD2 
3273 N N   . PHE A 481 ? 0.53320 0.58064 0.52410 -0.04502 0.03038  0.02571  758 PHE B N   
3274 C CA  . PHE A 481 ? 0.50390 0.52038 0.48036 -0.03801 0.02779  0.02574  758 PHE B CA  
3275 C C   . PHE A 481 ? 0.57664 0.57010 0.54346 -0.03309 0.03280  0.03257  758 PHE B C   
3276 O O   . PHE A 481 ? 0.55085 0.55335 0.52044 -0.03272 0.03824  0.03660  758 PHE B O   
3277 C CB  . PHE A 481 ? 0.52820 0.55554 0.50526 -0.02381 0.02262  0.02613  758 PHE B CB  
3278 C CG  . PHE A 481 ? 0.50995 0.54881 0.49337 -0.00993 0.02586  0.03330  758 PHE B CG  
3279 C CD1 . PHE A 481 ? 0.49692 0.56849 0.49430 -0.00635 0.02718  0.03585  758 PHE B CD1 
3280 C CD2 . PHE A 481 ? 0.49638 0.51402 0.47342 -0.00043 0.02808  0.03673  758 PHE B CD2 
3281 C CE1 . PHE A 481 ? 0.50172 0.57934 0.50577 0.00763  0.03230  0.04213  758 PHE B CE1 
3282 C CE2 . PHE A 481 ? 0.50925 0.53328 0.49323 0.01096  0.03260  0.04084  758 PHE B CE2 
3283 C CZ  . PHE A 481 ? 0.51278 0.56429 0.50989 0.01565  0.03551  0.04377  758 PHE B CZ  
3284 N N   . HIS A 482 ? 0.51858 0.48493 0.47363 -0.02896 0.03092  0.03339  759 HIS B N   
3285 C CA  . HIS A 482 ? 0.54089 0.48914 0.48538 -0.02439 0.03384  0.03970  759 HIS B CA  
3286 C C   . HIS A 482 ? 0.60309 0.54978 0.54569 -0.01118 0.03074  0.04008  759 HIS B C   
3287 O O   . HIS A 482 ? 0.57989 0.53151 0.52748 -0.00551 0.02721  0.03745  759 HIS B O   
3288 C CB  . HIS A 482 ? 0.57836 0.49868 0.51266 -0.02876 0.03476  0.04239  759 HIS B CB  
3289 C CG  . HIS A 482 ? 0.66665 0.58081 0.60344 -0.04352 0.04007  0.04236  759 HIS B CG  
3290 N ND1 . HIS A 482 ? 0.65880 0.55627 0.58807 -0.04794 0.04687  0.05147  759 HIS B ND1 
3291 C CD2 . HIS A 482 ? 0.71179 0.63471 0.65837 -0.05571 0.04011  0.03442  759 HIS B CD2 
3292 C CE1 . HIS A 482 ? 0.68264 0.57550 0.61873 -0.06318 0.05233  0.04958  759 HIS B CE1 
3293 N NE2 . HIS A 482 ? 0.67778 0.58695 0.62499 -0.06908 0.04770  0.03770  759 HIS B NE2 
3294 N N   . ILE A 483 ? 0.56976 0.51104 0.50520 -0.00717 0.03240  0.04304  760 ILE B N   
3295 C CA  . ILE A 483 ? 0.55089 0.49075 0.48656 0.00242  0.02986  0.04121  760 ILE B CA  
3296 C C   . ILE A 483 ? 0.66258 0.59235 0.58586 0.00395  0.02842  0.04407  760 ILE B C   
3297 O O   . ILE A 483 ? 0.59464 0.51835 0.50866 -0.00069 0.03063  0.04965  760 ILE B O   
3298 C CB  . ILE A 483 ? 0.54940 0.50395 0.49379 0.00664  0.03388  0.03792  760 ILE B CB  
3299 C CG1 . ILE A 483 ? 0.61238 0.57395 0.55132 0.00347  0.03951  0.03778  760 ILE B CG1 
3300 C CG2 . ILE A 483 ? 0.46057 0.42945 0.41772 0.00846  0.03457  0.03804  760 ILE B CG2 
3301 C CD1 . ILE A 483 ? 0.65818 0.63081 0.60507 0.00927  0.04528  0.03301  760 ILE B CD1 
3302 N N   . ASP A 484 ? 0.63445 0.56431 0.55845 0.00995  0.02515  0.04104  761 ASP B N   
3303 C CA  . ASP A 484 ? 0.66022 0.58872 0.57304 0.01209  0.02192  0.04278  761 ASP B CA  
3304 C C   . ASP A 484 ? 0.67623 0.59199 0.58095 0.01318  0.01968  0.05184  761 ASP B C   
3305 O O   . ASP A 484 ? 0.66721 0.57885 0.56136 0.01033  0.02289  0.05899  761 ASP B O   
3306 C CB  . ASP A 484 ? 0.66053 0.59862 0.56360 0.00977  0.02567  0.04123  761 ASP B CB  
3307 C CG  . ASP A 484 ? 0.64650 0.59006 0.53631 0.01265  0.02113  0.04187  761 ASP B CG  
3308 N N   . PHE A 485 ? 0.58021 0.48938 0.49012 0.01805  0.01585  0.05239  762 PHE B N   
3309 C CA  . PHE A 485 ? 0.61013 0.50455 0.51402 0.02149  0.01529  0.06056  762 PHE B CA  
3310 C C   . PHE A 485 ? 0.53598 0.43672 0.43470 0.02956  0.01002  0.06583  762 PHE B C   
3311 O O   . PHE A 485 ? 0.66303 0.56165 0.56666 0.03665  0.00696  0.06786  762 PHE B O   
3312 C CB  . PHE A 485 ? 0.63322 0.51802 0.54517 0.02292  0.01562  0.05735  762 PHE B CB  
3313 C CG  . PHE A 485 ? 0.63204 0.51690 0.54822 0.01498  0.01908  0.05190  762 PHE B CG  
3314 C CD1 . PHE A 485 ? 0.56423 0.43728 0.47606 0.00719  0.02338  0.05359  762 PHE B CD1 
3315 C CD2 . PHE A 485 ? 0.55798 0.45650 0.48369 0.01517  0.01844  0.04586  762 PHE B CD2 
3316 C CE1 . PHE A 485 ? 0.55091 0.43026 0.46854 -0.00141 0.02526  0.04732  762 PHE B CE1 
3317 C CE2 . PHE A 485 ? 0.57968 0.48479 0.50960 0.00942  0.02037  0.04202  762 PHE B CE2 
3318 C CZ  . PHE A 485 ? 0.58225 0.48021 0.50852 0.00045  0.02293  0.04167  762 PHE B CZ  
3319 N N   . GLY A 486 ? 0.63101 0.54342 0.51947 0.02897  0.00896  0.06795  763 GLY B N   
3320 C CA  . GLY A 486 ? 0.59035 0.51581 0.47253 0.03657  0.00247  0.07286  763 GLY B CA  
3321 C C   . GLY A 486 ? 0.62106 0.53527 0.49303 0.04459  0.00359  0.08923  763 GLY B C   
3322 O O   . GLY A 486 ? 0.62393 0.55120 0.49269 0.05389  -0.00249 0.09577  763 GLY B O   
3323 N N   . TYR A 487 ? 0.61833 0.50924 0.48656 0.04121  0.01173  0.09622  764 TYR B N   
3324 C CA  . TYR A 487 ? 0.67764 0.55010 0.53709 0.04834  0.01627  0.11310  764 TYR B CA  
3325 C C   . TYR A 487 ? 0.71346 0.55647 0.58137 0.04537  0.02287  0.11114  764 TYR B C   
3326 O O   . TYR A 487 ? 0.68611 0.51823 0.55633 0.03330  0.02886  0.10557  764 TYR B O   
3327 C CB  . TYR A 487 ? 0.63736 0.50835 0.48166 0.04442  0.02270  0.12413  764 TYR B CB  
3328 C CG  . TYR A 487 ? 0.77343 0.67326 0.60402 0.04933  0.01696  0.12764  764 TYR B CG  
3329 C CD1 . TYR A 487 ? 0.77909 0.70131 0.60939 0.04214  0.01362  0.11260  764 TYR B CD1 
3330 C CD2 . TYR A 487 ? 0.80564 0.71099 0.62255 0.06186  0.01554  0.14596  764 TYR B CD2 
3331 C CE1 . TYR A 487 ? 0.76488 0.71409 0.58062 0.04552  0.00865  0.11250  764 TYR B CE1 
3332 C CE2 . TYR A 487 ? 0.86076 0.79725 0.66249 0.06620  0.00938  0.14818  764 TYR B CE2 
3333 C CZ  . TYR A 487 ? 0.86434 0.82278 0.66497 0.05709  0.00573  0.12978  764 TYR B CZ  
3334 O OH  . TYR A 487 ? 0.91875 0.90907 0.70257 0.06050  -0.00039 0.12859  764 TYR B OH  
3335 N N   . ILE A 488 ? 0.67696 0.50910 0.54962 0.05626  0.02211  0.11492  765 ILE B N   
3336 C CA  . ILE A 488 ? 0.71451 0.51955 0.59402 0.05444  0.02829  0.10955  765 ILE B CA  
3337 C C   . ILE A 488 ? 0.79028 0.57128 0.66656 0.06791  0.03393  0.12386  765 ILE B C   
3338 O O   . ILE A 488 ? 0.74245 0.53146 0.61190 0.07995  0.03207  0.13983  765 ILE B O   
3339 C CB  . ILE A 488 ? 0.68164 0.49779 0.57307 0.05470  0.02347  0.09484  765 ILE B CB  
3340 C CG1 . ILE A 488 ? 0.69345 0.52525 0.59049 0.06937  0.01750  0.09913  765 ILE B CG1 
3341 C CG2 . ILE A 488 ? 0.61581 0.45336 0.51156 0.04392  0.01946  0.08332  765 ILE B CG2 
3342 C CD1 . ILE A 488 ? 0.61456 0.45808 0.52399 0.06964  0.01470  0.08708  765 ILE B CD1 
3343 N N   . LEU A 489 ? 0.74973 0.50150 0.63058 0.06662  0.04136  0.11785  766 LEU B N   
3344 C CA  . LEU A 489 ? 0.76014 0.48266 0.64006 0.08036  0.04934  0.12915  766 LEU B CA  
3345 C C   . LEU A 489 ? 0.82983 0.53961 0.69957 0.08577  0.05542  0.15129  766 LEU B C   
3346 O O   . LEU A 489 ? 0.85411 0.55977 0.72148 0.10450  0.05698  0.16866  766 LEU B O   
3347 C CB  . LEU A 489 ? 0.80425 0.54309 0.69114 0.09868  0.04360  0.13125  766 LEU B CB  
3348 C CG  . LEU A 489 ? 0.79763 0.54730 0.69404 0.09439  0.04007  0.11176  766 LEU B CG  
3349 C CD1 . LEU A 489 ? 0.78159 0.56048 0.68732 0.10896  0.03264  0.11444  766 LEU B CD1 
3350 C CD2 . LEU A 489 ? 0.78240 0.49651 0.67943 0.09225  0.05053  0.10130  766 LEU B CD2 
3351 N N   . GLY A 490 ? 0.81429 0.52104 0.67823 0.07048  0.05930  0.15249  767 GLY B N   
3352 C CA  . GLY A 490 ? 0.76884 0.45797 0.62280 0.07320  0.06873  0.17419  767 GLY B CA  
3353 C C   . GLY A 490 ? 0.88745 0.61008 0.72908 0.08157  0.06168  0.18983  767 GLY B C   
3354 O O   . GLY A 490 ? 0.88324 0.59583 0.71389 0.08389  0.06986  0.20987  767 GLY B O   
3355 N N   . ARG A 491 ? 0.85273 0.61499 0.69535 0.08581  0.04757  0.18135  768 ARG B N   
3356 C CA  . ARG A 491 ? 0.81424 0.61057 0.64363 0.09064  0.04057  0.19151  768 ARG B CA  
3357 C C   . ARG A 491 ? 0.83782 0.64213 0.66129 0.07270  0.04341  0.18414  768 ARG B C   
3358 O O   . ARG A 491 ? 0.85735 0.65718 0.69079 0.05753  0.04447  0.16603  768 ARG B O   
3359 C CB  . ARG A 491 ? 0.82469 0.66069 0.65879 0.09837  0.02528  0.18228  768 ARG B CB  
3360 C CG  . ARG A 491 ? 0.87450 0.74543 0.69386 0.10962  0.01741  0.19625  768 ARG B CG  
3361 C CD  . ARG A 491 ? 0.89030 0.79970 0.71841 0.11678  0.00259  0.18671  768 ARG B CD  
3362 N NE  . ARG A 491 ? 0.96536 0.88875 0.80287 0.10084  -0.00288 0.16150  768 ARG B NE  
3363 C CZ  . ARG A 491 ? 0.93414 0.88578 0.76422 0.09255  -0.00920 0.15097  768 ARG B CZ  
3364 N NH1 . ARG A 491 ? 0.95316 0.92859 0.76483 0.09826  -0.01296 0.16140  768 ARG B NH1 
3365 N NH2 . ARG A 491 ? 0.78935 0.74531 0.62989 0.07906  -0.01095 0.12955  768 ARG B NH2 
3366 N N   . ASP A 492 ? 0.86595 0.68417 0.67266 0.07584  0.04537  0.19965  769 ASP B N   
3367 C CA  . ASP A 492 ? 0.87672 0.70365 0.67680 0.06099  0.05034  0.19539  769 ASP B CA  
3368 C C   . ASP A 492 ? 0.96870 0.82699 0.74763 0.06923  0.04688  0.20799  769 ASP B C   
3369 O O   . ASP A 492 ? 0.95300 0.81381 0.72056 0.08561  0.04633  0.22907  769 ASP B O   
3370 C CB  . ASP A 492 ? 0.90240 0.69327 0.70543 0.04964  0.06678  0.20417  769 ASP B CB  
3371 C CG  . ASP A 492 ? 0.96499 0.76777 0.76806 0.03217  0.07197  0.19561  769 ASP B CG  
3372 O OD1 . ASP A 492 ? 1.01922 0.84059 0.80605 0.03416  0.07513  0.20736  769 ASP B OD1 
3373 O OD2 . ASP A 492 ? 0.87635 0.67388 0.69520 0.01782  0.07260  0.17732  769 ASP B OD2 
3374 N N   . PRO A 493 ? 0.94660 0.83073 0.71906 0.05986  0.04472  0.19589  770 PRO B N   
3375 C CA  . PRO A 493 ? 0.91144 0.82560 0.66004 0.06692  0.04316  0.20698  770 PRO B CA  
3376 C C   . PRO A 493 ? 0.97861 0.87651 0.71211 0.07141  0.05722  0.23592  770 PRO B C   
3377 O O   . PRO A 493 ? 1.04938 0.96731 0.76196 0.08560  0.05503  0.25455  770 PRO B O   
3378 C CB  . PRO A 493 ? 0.90760 0.84255 0.65570 0.05361  0.04280  0.18582  770 PRO B CB  
3379 C CG  . PRO A 493 ? 0.88847 0.81520 0.66033 0.04525  0.03745  0.16285  770 PRO B CG  
3380 C CD  . PRO A 493 ? 0.92321 0.81463 0.70951 0.04561  0.04198  0.17034  770 PRO B CD  
3381 N N   . LYS A 494 ? 0.99927 0.86248 0.74320 0.05966  0.07191  0.24101  771 LYS B N   
3382 C CA  . LYS A 494 ? 1.09548 0.93928 0.82749 0.06223  0.08796  0.26983  771 LYS B CA  
3383 C C   . LYS A 494 ? 1.11540 0.91824 0.85530 0.07178  0.09484  0.28792  771 LYS B C   
3384 O O   . LYS A 494 ? 1.18053 0.96154 0.93953 0.06897  0.09159  0.27374  771 LYS B O   
3385 C CB  . LYS A 494 ? 1.13789 0.96944 0.87783 0.04158  0.10264  0.26594  771 LYS B CB  
3386 C CG  . LYS A 494 ? 1.09605 0.96584 0.82581 0.03498  0.10070  0.25380  771 LYS B CG  
3387 C CD  . LYS A 494 ? 1.15908 1.02550 0.91080 0.01492  0.10455  0.23178  771 LYS B CD  
3388 N N   . PRO A 495 ? 1.18477 0.97507 0.90995 0.08432  0.10569  0.31988  772 PRO B N   
3389 C CA  . PRO A 495 ? 1.18783 0.93609 0.92730 0.09011  0.11334  0.33079  772 PRO B CA  
3390 C C   . PRO A 495 ? 1.26314 0.96935 1.01788 0.06909  0.13166  0.32952  772 PRO B C   
3391 O O   . PRO A 495 ? 1.38134 1.09411 1.13191 0.05453  0.14113  0.33221  772 PRO B O   
3392 C CB  . PRO A 495 ? 1.25345 1.01827 0.97882 0.10771  0.11237  0.35403  772 PRO B CB  
3393 C CG  . PRO A 495 ? 1.22988 1.02342 0.93634 0.09962  0.11629  0.35895  772 PRO B CG  
3394 C CD  . PRO A 495 ? 1.16538 0.98391 0.86848 0.08907  0.10858  0.33648  772 PRO B CD  
3395 N N   . LEU A 496 ? 1.31406 0.97902 1.08773 0.06684  0.13675  0.32357  773 LEU B N   
3396 C CA  . LEU A 496 ? 1.33424 0.95897 1.12514 0.04490  0.15307  0.31826  773 LEU B CA  
3397 C C   . LEU A 496 ? 1.32820 0.95881 1.12637 0.02220  0.15472  0.29780  773 LEU B C   
3398 O O   . LEU A 496 ? 1.37001 0.99891 1.17322 0.00306  0.16640  0.29893  773 LEU B O   
3399 C CB  . LEU A 496 ? 1.35389 0.97196 1.13999 0.04128  0.16671  0.33998  773 LEU B CB  
3400 N N   . PRO A 497 ? 1.20772 0.85838 1.01330 0.02170  0.13807  0.27109  774 PRO B N   
3401 C CA  . PRO A 497 ? 1.21920 0.88548 1.03972 -0.00064 0.13387  0.24318  774 PRO B CA  
3402 C C   . PRO A 497 ? 1.23758 0.86424 1.07844 -0.01988 0.14503  0.23150  774 PRO B C   
3403 O O   . PRO A 497 ? 1.22304 0.80917 1.06803 -0.01380 0.15169  0.23611  774 PRO B O   
3404 C CB  . PRO A 497 ? 1.11932 0.81399 0.94150 0.00819  0.11386  0.22191  774 PRO B CB  
3405 C CG  . PRO A 497 ? 1.12418 0.80055 0.94210 0.02933  0.11094  0.23289  774 PRO B CG  
3406 C CD  . PRO A 497 ? 1.13721 0.80208 0.93930 0.04193  0.12215  0.26593  774 PRO B CD  
3407 N N   . PRO A 498 ? 1.21855 0.85700 1.07330 -0.04324 0.14754  0.21501  775 PRO B N   
3408 C CA  . PRO A 498 ? 1.21833 0.82447 1.09335 -0.06433 0.15674  0.20028  775 PRO B CA  
3409 C C   . PRO A 498 ? 1.20879 0.81046 1.09165 -0.06198 0.14453  0.17526  775 PRO B C   
3410 O O   . PRO A 498 ? 1.12986 0.76515 1.00913 -0.05270 0.12817  0.16314  775 PRO B O   
3411 C CB  . PRO A 498 ? 1.17605 0.81154 1.06359 -0.08757 0.15936  0.18981  775 PRO B CB  
3412 C CG  . PRO A 498 ? 1.17610 0.86076 1.05315 -0.07663 0.14517  0.18619  775 PRO B CG  
3413 C CD  . PRO A 498 ? 1.17229 0.85680 1.02618 -0.05095 0.14156  0.20697  775 PRO B CD  
3414 N N   . PRO A 499 ? 1.23979 0.79934 1.13315 -0.07016 0.15310  0.16639  776 PRO B N   
3415 C CA  . PRO A 499 ? 1.16275 0.71733 1.05990 -0.06475 0.14271  0.14395  776 PRO B CA  
3416 C C   . PRO A 499 ? 1.10949 0.69797 1.01794 -0.08116 0.13115  0.11571  776 PRO B C   
3417 O O   . PRO A 499 ? 1.16595 0.77464 1.07210 -0.07120 0.11735  0.10201  776 PRO B O   
3418 C CB  . PRO A 499 ? 1.29814 0.79467 1.20210 -0.06997 0.15864  0.14294  776 PRO B CB  
3419 C CG  . PRO A 499 ? 1.25879 0.73839 1.17249 -0.09306 0.17559  0.15171  776 PRO B CG  
3420 C CD  . PRO A 499 ? 1.21456 0.72917 1.11757 -0.08646 0.17394  0.17466  776 PRO B CD  
3421 N N   . MET A 500 ? 1.14299 0.74015 1.06470 -0.10568 0.13701  0.10791  777 MET B N   
3422 C CA  . MET A 500 ? 1.12104 0.75814 1.05448 -0.12020 0.12597  0.08450  777 MET B CA  
3423 C C   . MET A 500 ? 1.09376 0.77702 1.02368 -0.11523 0.11918  0.09331  777 MET B C   
3424 O O   . MET A 500 ? 1.20434 0.89231 1.13487 -0.12180 0.12898  0.10864  777 MET B O   
3425 C CB  . MET A 500 ? 1.14100 0.76865 1.09369 -0.14999 0.13536  0.06990  777 MET B CB  
3426 C CG  . MET A 500 ? 1.17625 0.79035 1.13609 -0.15988 0.13152  0.04232  777 MET B CG  
3427 S SD  . MET A 500 ? 1.29430 0.96512 1.25464 -0.15504 0.10959  0.02064  777 MET B SD  
3428 C CE  . MET A 500 ? 1.07159 0.71456 1.03184 -0.16056 0.10836  -0.00707 777 MET B CE  
3429 N N   . LYS A 501 ? 1.13364 0.84942 1.05990 -0.10342 0.10406  0.08381  778 LYS B N   
3430 C CA  . LYS A 501 ? 1.10340 0.86037 1.02677 -0.09750 0.09801  0.08884  778 LYS B CA  
3431 C C   . LYS A 501 ? 1.02659 0.81588 0.96786 -0.11630 0.09771  0.07613  778 LYS B C   
3432 O O   . LYS A 501 ? 1.08946 0.91005 1.03723 -0.11472 0.08700  0.06250  778 LYS B O   
3433 C CB  . LYS A 501 ? 1.05147 0.82579 0.96600 -0.07786 0.08412  0.08451  778 LYS B CB  
3434 C CG  . LYS A 501 ? 1.02318 0.77874 0.92119 -0.05836 0.08386  0.10042  778 LYS B CG  
3435 C CD  . LYS A 501 ? 0.94896 0.69933 0.83728 -0.05763 0.09420  0.12183  778 LYS B CD  
3436 C CE  . LYS A 501 ? 0.97752 0.71812 0.84888 -0.03696 0.09225  0.13870  778 LYS B CE  
3437 N NZ  . LYS A 501 ? 1.07110 0.77274 0.94292 -0.03123 0.09674  0.14268  778 LYS B NZ  
3438 N N   . LEU A 502 ? 1.11044 0.89282 1.06106 -0.13396 0.11072  0.08250  779 LEU B N   
3439 C CA  . LEU A 502 ? 1.08770 0.90229 1.05879 -0.15399 0.11277  0.07270  779 LEU B CA  
3440 C C   . LEU A 502 ? 1.04780 0.87504 1.01878 -0.15746 0.12478  0.09082  779 LEU B C   
3441 O O   . LEU A 502 ? 1.11402 0.91088 1.07497 -0.15623 0.13701  0.10928  779 LEU B O   
3442 C CB  . LEU A 502 ? 1.07248 0.86701 1.06035 -0.17803 0.11853  0.05847  779 LEU B CB  
3443 C CG  . LEU A 502 ? 1.04424 0.87699 1.05728 -0.20144 0.11811  0.04378  779 LEU B CG  
3444 C CD1 . LEU A 502 ? 0.97273 0.85181 0.99049 -0.19397 0.10088  0.02782  779 LEU B CD1 
3445 C CD2 . LEU A 502 ? 1.05160 0.85649 1.07905 -0.22655 0.12548  0.02950  779 LEU B CD2 
3446 N N   . ASN A 503 ? 0.97860 0.85117 0.96031 -0.16037 0.12252  0.08696  780 ASN B N   
3447 C CA  . ASN A 503 ? 0.95620 0.84592 0.93627 -0.16136 0.13440  0.10319  780 ASN B CA  
3448 C C   . ASN A 503 ? 0.87218 0.79797 0.87935 -0.18217 0.14045  0.09650  780 ASN B C   
3449 O O   . ASN A 503 ? 0.87401 0.81816 0.90102 -0.19447 0.13292  0.07838  780 ASN B O   
3450 C CB  . ASN A 503 ? 0.87077 0.78249 0.83308 -0.13840 0.12802  0.10827  780 ASN B CB  
3451 C CG  . ASN A 503 ? 0.92254 0.86854 0.89446 -0.13143 0.11470  0.09146  780 ASN B CG  
3452 O OD1 . ASN A 503 ? 0.93649 0.91195 0.93063 -0.14356 0.11403  0.08145  780 ASN B OD1 
3453 N ND2 . ASN A 503 ? 0.82608 0.76967 0.78266 -0.11175 0.10434  0.08907  780 ASN B ND2 
3454 N N   . LYS A 504 ? 0.89162 0.83198 0.89949 -0.18556 0.15423  0.11165  781 LYS B N   
3455 C CA  . LYS A 504 ? 0.91351 0.88887 0.94985 -0.20670 0.16276  0.10793  781 LYS B CA  
3456 C C   . LYS A 504 ? 0.85318 0.88123 0.90453 -0.20083 0.15130  0.09339  781 LYS B C   
3457 O O   . LYS A 504 ? 0.82225 0.88381 0.90222 -0.21864 0.15193  0.08357  781 LYS B O   
3458 C CB  . LYS A 504 ? 0.82189 0.80153 0.85452 -0.21034 0.18230  0.12954  781 LYS B CB  
3459 C CG  . LYS A 504 ? 0.90561 0.90455 0.91498 -0.18648 0.18292  0.14008  781 LYS B CG  
3460 C CD  . LYS A 504 ? 1.02041 1.02546 1.02489 -0.19147 0.20397  0.16175  781 LYS B CD  
3461 C CE  . LYS A 504 ? 1.05285 1.06792 1.02602 -0.16682 0.20454  0.17175  781 LYS B CE  
3462 N N   . GLU A 505 ? 0.82099 0.85805 0.85536 -0.17631 0.14118  0.09195  782 GLU B N   
3463 C CA  . GLU A 505 ? 0.77610 0.85968 0.82511 -0.16820 0.13259  0.08098  782 GLU B CA  
3464 C C   . GLU A 505 ? 0.76195 0.85479 0.82558 -0.17412 0.11795  0.06341  782 GLU B C   
3465 O O   . GLU A 505 ? 0.69775 0.83546 0.78420 -0.17784 0.11343  0.05490  782 GLU B O   
3466 C CB  . GLU A 505 ? 0.78154 0.86763 0.80942 -0.14146 0.12800  0.08369  782 GLU B CB  
3467 C CG  . GLU A 505 ? 0.81339 0.90585 0.82808 -0.13459 0.14200  0.09732  782 GLU B CG  
3468 C CD  . GLU A 505 ? 0.93124 0.98341 0.92070 -0.13475 0.14918  0.11214  782 GLU B CD  
3469 O OE1 . GLU A 505 ? 0.89358 0.90996 0.87491 -0.13632 0.14252  0.11154  782 GLU B OE1 
3470 O OE2 . GLU A 505 ? 0.92938 0.98730 0.90667 -0.13184 0.16201  0.12518  782 GLU B OE2 
3471 N N   . MET A 506 ? 0.71167 0.76564 0.76193 -0.17359 0.11059  0.05823  783 MET B N   
3472 C CA  . MET A 506 ? 0.77056 0.83278 0.83096 -0.17926 0.09737  0.04068  783 MET B CA  
3473 C C   . MET A 506 ? 0.75996 0.83734 0.84607 -0.20808 0.10105  0.03051  783 MET B C   
3474 O O   . MET A 506 ? 0.73695 0.85466 0.84177 -0.21468 0.09157  0.01675  783 MET B O   
3475 C CB  . MET A 506 ? 0.77213 0.78819 0.81159 -0.17155 0.09100  0.03745  783 MET B CB  
3476 C CG  . MET A 506 ? 0.79192 0.79712 0.80940 -0.14518 0.08530  0.04444  783 MET B CG  
3477 S SD  . MET A 506 ? 0.97471 0.92608 0.97027 -0.13742 0.08142  0.04432  783 MET B SD  
3478 C CE  . MET A 506 ? 0.85387 0.81374 0.86038 -0.14684 0.07022  0.02268  783 MET B CE  
3479 N N   . VAL A 507 ? 0.78516 0.83204 0.87316 -0.22568 0.11518  0.03760  784 VAL B N   
3480 C CA  . VAL A 507 ? 0.80836 0.86284 0.92226 -0.25671 0.12059  0.02655  784 VAL B CA  
3481 C C   . VAL A 507 ? 0.79480 0.91046 0.93749 -0.26726 0.12353  0.02600  784 VAL B C   
3482 O O   . VAL A 507 ? 0.80670 0.95729 0.97514 -0.28695 0.11779  0.00945  784 VAL B O   
3483 C CB  . VAL A 507 ? 0.81729 0.81834 0.92613 -0.27113 0.13806  0.03786  784 VAL B CB  
3484 C CG1 . VAL A 507 ? 0.79456 0.79504 0.93113 -0.30595 0.14428  0.02296  784 VAL B CG1 
3485 C CG2 . VAL A 507 ? 0.85592 0.80123 0.93576 -0.25433 0.13508  0.04165  784 VAL B CG2 
3486 N N   . GLU A 508 ? 0.73121 0.86396 0.87053 -0.25433 0.13256  0.04311  785 GLU B N   
3487 C CA  . GLU A 508 ? 0.71466 0.90967 0.88178 -0.25965 0.13531  0.04287  785 GLU B CA  
3488 C C   . GLU A 508 ? 0.74690 0.98774 0.92228 -0.24507 0.11748  0.03062  785 GLU B C   
3489 O O   . GLU A 508 ? 0.68330 0.97964 0.88859 -0.25588 0.11404  0.02271  785 GLU B O   
3490 C CB  . GLU A 508 ? 0.71435 0.91561 0.87245 -0.24596 0.14977  0.06269  785 GLU B CB  
3491 C CG  . GLU A 508 ? 0.86949 1.04432 1.02894 -0.26481 0.17009  0.07699  785 GLU B CG  
3492 C CD  . GLU A 508 ? 1.00802 1.17712 1.14587 -0.24702 0.18348  0.09756  785 GLU B CD  
3493 O OE1 . GLU A 508 ? 0.94913 1.11994 1.06530 -0.22005 0.17567  0.09847  785 GLU B OE1 
3494 O OE2 . GLU A 508 ? 1.07213 1.23548 1.21454 -0.26067 0.20242  0.11232  785 GLU B OE2 
3495 N N   . GLY A 509 ? 0.68975 0.90950 0.84010 -0.22071 0.10635  0.02987  786 GLY B N   
3496 C CA  . GLY A 509 ? 0.63493 0.89258 0.79071 -0.20494 0.09079  0.02127  786 GLY B CA  
3497 C C   . GLY A 509 ? 0.67133 0.95684 0.84619 -0.22354 0.07887  0.00282  786 GLY B C   
3498 O O   . GLY A 509 ? 0.68082 1.02167 0.87369 -0.21828 0.06935  -0.00238 786 GLY B O   
3499 N N   . MET A 510 ? 0.65888 0.90787 0.83008 -0.24498 0.07954  -0.00769 787 MET B N   
3500 C CA  . MET A 510 ? 0.71470 0.98861 0.90222 -0.26548 0.06847  -0.02931 787 MET B CA  
3501 C C   . MET A 510 ? 0.78936 1.08805 1.00903 -0.29932 0.07715  -0.03655 787 MET B C   
3502 O O   . MET A 510 ? 0.88608 1.19292 1.11854 -0.32356 0.07092  -0.05745 787 MET B O   
3503 C CB  . MET A 510 ? 0.74961 0.97086 0.91464 -0.26835 0.06302  -0.04159 787 MET B CB  
3504 C CG  . MET A 510 ? 0.79082 0.94504 0.94393 -0.27967 0.07813  -0.03557 787 MET B CG  
3505 S SD  . MET A 510 ? 0.89600 0.99216 1.02404 -0.27815 0.07197  -0.05039 787 MET B SD  
3506 C CE  . MET A 510 ? 0.73227 0.80930 0.82878 -0.23846 0.06560  -0.03440 787 MET B CE  
3507 N N   . GLY A 511 ? 0.72654 1.03938 0.96018 -0.30241 0.09186  -0.02100 788 GLY B N   
3508 C CA  . GLY A 511 ? 0.71847 1.06495 0.98758 -0.33400 0.10093  -0.02610 788 GLY B CA  
3509 C C   . GLY A 511 ? 0.78772 1.08135 1.05798 -0.35897 0.12000  -0.02131 788 GLY B C   
3510 O O   . GLY A 511 ? 0.89255 1.20955 1.19468 -0.38983 0.12873  -0.02738 788 GLY B O   
3511 N N   . GLY A 512 ? 0.82321 1.04838 1.06167 -0.34665 0.12761  -0.00927 789 GLY B N   
3512 C CA  . GLY A 512 ? 0.86367 1.03592 1.10204 -0.36718 0.14714  -0.00088 789 GLY B CA  
3513 C C   . GLY A 512 ? 0.92169 1.05456 1.16271 -0.39072 0.14481  -0.02198 789 GLY B C   
3514 O O   . GLY A 512 ? 0.90670 1.05811 1.14950 -0.39305 0.12739  -0.04511 789 GLY B O   
3515 N N   . THR A 513 ? 0.94783 1.02454 1.18851 -0.40805 0.16398  -0.01362 790 THR B N   
3516 C CA  . THR A 513 ? 0.99509 1.01741 1.23166 -0.42479 0.16490  -0.03147 790 THR B CA  
3517 C C   . THR A 513 ? 0.97177 1.01675 1.24372 -0.46308 0.16441  -0.05787 790 THR B C   
3518 O O   . THR A 513 ? 1.01199 1.01569 1.27967 -0.47245 0.16157  -0.07660 790 THR B O   
3519 C CB  . THR A 513 ? 1.03561 0.98066 1.25434 -0.42229 0.18583  -0.00976 790 THR B CB  
3520 O OG1 . THR A 513 ? 0.95574 0.90570 1.19364 -0.43672 0.20501  0.00931  790 THR B OG1 
3521 C CG2 . THR A 513 ? 0.99469 0.91714 1.17501 -0.38185 0.18147  0.01208  790 THR B CG2 
3522 N N   . GLN A 514 ? 1.01927 1.12869 1.32237 -0.47510 0.16289  -0.05864 791 GLN B N   
3523 C CA  . GLN A 514 ? 1.01731 1.15631 1.35077 -0.50082 0.15514  -0.08323 791 GLN B CA  
3524 C C   . GLN A 514 ? 0.99995 1.20898 1.34165 -0.50007 0.13059  -0.10847 791 GLN B C   
3525 O O   . GLN A 514 ? 1.04436 1.29263 1.41132 -0.51927 0.12157  -0.12888 791 GLN B O   
3526 C CB  . GLN A 514 ? 1.01170 1.18017 1.37762 -0.51588 0.16816  -0.06928 791 GLN B CB  
3527 C CG  . GLN A 514 ? 1.02375 1.12633 1.39058 -0.52658 0.19031  -0.05187 791 GLN B CG  
3528 N N   . SER A 515 ? 0.96612 1.19263 1.28667 -0.47781 0.11938  -0.10669 792 SER B N   
3529 C CA  . SER A 515 ? 0.93082 1.23160 1.25868 -0.47096 0.09634  -0.12335 792 SER B CA  
3530 C C   . SER A 515 ? 0.94959 1.23377 1.26024 -0.47372 0.08047  -0.15173 792 SER B C   
3531 O O   . SER A 515 ? 0.93555 1.14723 1.21996 -0.46907 0.08604  -0.15391 792 SER B O   
3532 C CB  . SER A 515 ? 0.84479 1.16911 1.15277 -0.42822 0.08912  -0.09984 792 SER B CB  
3533 O OG  . SER A 515 ? 0.87451 1.13377 1.14298 -0.40129 0.09071  -0.08770 792 SER B OG  
3534 N N   . GLU A 516 ? 0.92703 1.27989 1.24987 -0.47564 0.05998  -0.17148 793 GLU B N   
3535 C CA  . GLU A 516 ? 0.86508 1.21503 1.16745 -0.47270 0.04295  -0.19690 793 GLU B CA  
3536 C C   . GLU A 516 ? 0.92787 1.24314 1.19095 -0.43434 0.03819  -0.18177 793 GLU B C   
3537 O O   . GLU A 516 ? 0.92682 1.20079 1.16468 -0.42999 0.03364  -0.19635 793 GLU B O   
3538 C CB  . GLU A 516 ? 0.84254 1.28009 1.16030 -0.47254 0.02107  -0.21324 793 GLU B CB  
3539 N N   . GLN A 517 ? 0.95602 1.28441 1.21249 -0.40402 0.03996  -0.15238 794 GLN B N   
3540 C CA  . GLN A 517 ? 0.85813 1.15358 1.07873 -0.36642 0.03561  -0.13710 794 GLN B CA  
3541 C C   . GLN A 517 ? 0.87584 1.08223 1.07248 -0.36445 0.04969  -0.13108 794 GLN B C   
3542 O O   . GLN A 517 ? 0.90446 1.07585 1.07326 -0.34748 0.04401  -0.13520 794 GLN B O   
3543 C CB  . GLN A 517 ? 0.87659 1.20141 1.09783 -0.33778 0.03695  -0.10913 794 GLN B CB  
3544 C CG  . GLN A 517 ? 0.78849 1.19452 1.02288 -0.32413 0.02060  -0.11032 794 GLN B CG  
3545 C CD  . GLN A 517 ? 0.86899 1.34161 1.14309 -0.35170 0.01883  -0.12162 794 GLN B CD  
3546 O OE1 . GLN A 517 ? 0.84853 1.30567 1.14226 -0.38136 0.03214  -0.12606 794 GLN B OE1 
3547 N NE2 . GLN A 517 ? 0.87832 1.42759 1.16605 -0.34214 0.00288  -0.12530 794 GLN B NE2 
3548 N N   . TYR A 518 ? 0.86021 1.03083 1.06754 -0.38011 0.06889  -0.11936 795 TYR B N   
3549 C CA  . TYR A 518 ? 0.90838 0.99643 1.09355 -0.37556 0.08298  -0.10994 795 TYR B CA  
3550 C C   . TYR A 518 ? 0.95279 1.00143 1.13089 -0.39198 0.08134  -0.13712 795 TYR B C   
3551 O O   . TYR A 518 ? 0.99826 0.99507 1.14910 -0.37427 0.08213  -0.13524 795 TYR B O   
3552 C CB  . TYR A 518 ? 0.91003 0.97123 1.10941 -0.39089 0.10498  -0.09133 795 TYR B CB  
3553 C CG  . TYR A 518 ? 0.95776 0.93712 1.13460 -0.38300 0.12059  -0.07620 795 TYR B CG  
3554 C CD1 . TYR A 518 ? 0.89350 0.84906 1.04130 -0.34877 0.12010  -0.05335 795 TYR B CD1 
3555 C CD2 . TYR A 518 ? 0.97001 0.89694 1.15606 -0.40965 0.13635  -0.08443 795 TYR B CD2 
3556 C CE1 . TYR A 518 ? 0.93219 0.81960 1.06033 -0.33979 0.13332  -0.03796 795 TYR B CE1 
3557 C CE2 . TYR A 518 ? 1.03689 0.89008 1.20310 -0.39943 0.15141  -0.06764 795 TYR B CE2 
3558 C CZ  . TYR A 518 ? 1.01168 0.84826 1.14880 -0.36371 0.14906  -0.04378 795 TYR B CZ  
3559 O OH  . TYR A 518 ? 1.18090 0.95045 1.29903 -0.35179 0.16290  -0.02572 795 TYR B OH  
3560 N N   . GLN A 519 ? 0.93747 1.01209 1.14066 -0.42601 0.07921  -0.16407 796 GLN B N   
3561 C CA  . GLN A 519 ? 0.99232 1.03697 1.18858 -0.44245 0.07603  -0.19571 796 GLN B CA  
3562 C C   . GLN A 519 ? 0.96960 1.02698 1.13693 -0.41484 0.05775  -0.20422 796 GLN B C   
3563 O O   . GLN A 519 ? 0.95207 0.95438 1.09555 -0.40541 0.06070  -0.21127 796 GLN B O   
3564 N N   . GLU A 520 ? 0.89444 1.02489 1.06423 -0.40040 0.03996  -0.20212 797 GLU B N   
3565 C CA  . GLU A 520 ? 0.85432 0.99971 0.99728 -0.37337 0.02397  -0.20670 797 GLU B CA  
3566 C C   . GLU A 520 ? 0.89462 0.98356 1.00906 -0.34116 0.03077  -0.18261 797 GLU B C   
3567 O O   . GLU A 520 ? 0.93703 0.99275 1.02721 -0.32865 0.02820  -0.19125 797 GLU B O   
3568 C CB  . GLU A 520 ? 0.89531 1.12604 1.04742 -0.35983 0.00678  -0.20103 797 GLU B CB  
3569 N N   . PHE A 521 ? 0.89908 0.97836 1.01648 -0.32802 0.03994  -0.15311 798 PHE B N   
3570 C CA  . PHE A 521 ? 0.88134 0.91125 0.97372 -0.29938 0.04607  -0.13051 798 PHE B CA  
3571 C C   . PHE A 521 ? 0.88731 0.84292 0.96586 -0.30479 0.05790  -0.13715 798 PHE B C   
3572 O O   . PHE A 521 ? 0.88872 0.81329 0.94340 -0.28263 0.05587  -0.13389 798 PHE B O   
3573 C CB  . PHE A 521 ? 0.84224 0.87362 0.94155 -0.29080 0.05584  -0.10186 798 PHE B CB  
3574 C CG  . PHE A 521 ? 0.84501 0.81818 0.92282 -0.27120 0.06616  -0.08071 798 PHE B CG  
3575 C CD1 . PHE A 521 ? 0.77572 0.74873 0.83301 -0.24013 0.05897  -0.06760 798 PHE B CD1 
3576 C CD2 . PHE A 521 ? 0.86964 0.79040 0.94901 -0.28385 0.08345  -0.07285 798 PHE B CD2 
3577 C CE1 . PHE A 521 ? 0.79321 0.71933 0.83213 -0.22276 0.06698  -0.04912 798 PHE B CE1 
3578 C CE2 . PHE A 521 ? 0.91245 0.78563 0.97180 -0.26402 0.09193  -0.05169 798 PHE B CE2 
3579 C CZ  . PHE A 521 ? 0.79686 0.67506 0.83613 -0.23380 0.08281  -0.04069 798 PHE B CZ  
3580 N N   . ARG A 522 ? 0.90632 0.83212 1.00124 -0.33363 0.07166  -0.14561 799 ARG B N   
3581 C CA  . ARG A 522 ? 0.97260 0.82392 1.05637 -0.33801 0.08525  -0.15121 799 ARG B CA  
3582 C C   . ARG A 522 ? 0.96755 0.81205 1.03682 -0.33727 0.07600  -0.18038 799 ARG B C   
3583 O O   . ARG A 522 ? 0.99288 0.78954 1.04067 -0.31881 0.08019  -0.17780 799 ARG B O   
3584 C CB  . ARG A 522 ? 0.99857 0.82002 1.10588 -0.37177 0.10312  -0.15626 799 ARG B CB  
3585 C CG  . ARG A 522 ? 1.06558 0.87060 1.17989 -0.36869 0.11865  -0.12270 799 ARG B CG  
3586 C CD  . ARG A 522 ? 1.08601 0.81888 1.20647 -0.38594 0.14247  -0.11754 799 ARG B CD  
3587 N NE  . ARG A 522 ? 1.11824 0.85892 1.26723 -0.42248 0.14791  -0.13953 799 ARG B NE  
3588 C CZ  . ARG A 522 ? 1.23499 0.92488 1.39078 -0.43075 0.16202  -0.13816 799 ARG B CZ  
3589 N N   . LYS A 523 ? 0.91124 0.80740 0.99149 -0.35603 0.06315  -0.20822 800 LYS B N   
3590 C CA  . LYS A 523 ? 0.95455 0.84930 1.01861 -0.35599 0.05428  -0.23797 800 LYS B CA  
3591 C C   . LYS A 523 ? 0.95019 0.85613 0.98703 -0.31872 0.04325  -0.22535 800 LYS B C   
3592 O O   . LYS A 523 ? 0.96621 0.83491 0.98206 -0.30679 0.04539  -0.23503 800 LYS B O   
3593 C CB  . LYS A 523 ? 0.86985 0.82834 0.95060 -0.38325 0.04079  -0.26950 800 LYS B CB  
3594 N N   . GLN A 524 ? 0.88767 0.84311 0.92569 -0.29977 0.03301  -0.20349 801 GLN B N   
3595 C CA  . GLN A 524 ? 0.86322 0.82625 0.87823 -0.26564 0.02468  -0.18949 801 GLN B CA  
3596 C C   . GLN A 524 ? 0.90289 0.80051 0.90192 -0.24610 0.03690  -0.17111 801 GLN B C   
3597 O O   . GLN A 524 ? 0.92710 0.81242 0.90582 -0.22441 0.03365  -0.17027 801 GLN B O   
3598 C CB  . GLN A 524 ? 0.82292 0.84236 0.84482 -0.24944 0.01499  -0.16777 801 GLN B CB  
3599 C CG  . GLN A 524 ? 0.87562 0.97057 0.91315 -0.26136 0.00088  -0.18097 801 GLN B CG  
3600 C CD  . GLN A 524 ? 0.94481 1.06991 0.96644 -0.25699 -0.01261 -0.20262 801 GLN B CD  
3601 O OE1 . GLN A 524 ? 0.98197 1.06726 0.98360 -0.25302 -0.00948 -0.21517 801 GLN B OE1 
3602 N NE2 . GLN A 524 ? 0.89722 1.09512 0.92733 -0.25640 -0.02711 -0.20624 801 GLN B NE2 
3603 N N   . CYS A 525 ? 0.94049 0.79865 0.94873 -0.25290 0.05129  -0.15532 802 CYS B N   
3604 C CA  . CYS A 525 ? 0.94438 0.74311 0.93831 -0.23434 0.06283  -0.13694 802 CYS B CA  
3605 C C   . CYS A 525 ? 0.98809 0.73615 0.97105 -0.23736 0.07038  -0.15682 802 CYS B C   
3606 O O   . CYS A 525 ? 0.95612 0.67792 0.92132 -0.21371 0.07158  -0.14990 802 CYS B O   
3607 C CB  . CYS A 525 ? 0.94379 0.71551 0.94924 -0.24177 0.07708  -0.11513 802 CYS B CB  
3608 S SG  . CYS A 525 ? 0.89401 0.70776 0.90333 -0.22637 0.07244  -0.08517 802 CYS B SG  
3609 N N   . TYR A 526 ? 1.01146 0.74482 1.00635 -0.26683 0.07663  -0.18235 803 TYR B N   
3610 C CA  . TYR A 526 ? 1.02331 0.70685 1.00859 -0.27164 0.08528  -0.20586 803 TYR B CA  
3611 C C   . TYR A 526 ? 1.02202 0.73112 0.98718 -0.25595 0.07231  -0.22355 803 TYR B C   
3612 O O   . TYR A 526 ? 1.01844 0.68832 0.96690 -0.23898 0.07842  -0.22666 803 TYR B O   
3613 C CB  . TYR A 526 ? 1.07198 0.74347 1.07589 -0.31019 0.09276  -0.23528 803 TYR B CB  
3614 C CG  . TYR A 526 ? 1.15732 0.81065 1.18455 -0.33076 0.10635  -0.22001 803 TYR B CG  
3615 C CD1 . TYR A 526 ? 1.23881 0.86866 1.26456 -0.31273 0.11557  -0.18213 803 TYR B CD1 
3616 C CD2 . TYR A 526 ? 1.17211 0.83428 1.22308 -0.36906 0.11039  -0.24372 803 TYR B CD2 
3617 C CE1 . TYR A 526 ? 1.24387 0.85878 1.28919 -0.33063 0.12948  -0.16599 803 TYR B CE1 
3618 C CE2 . TYR A 526 ? 1.23353 0.88314 1.30690 -0.38477 0.12339  -0.22554 803 TYR B CE2 
3619 C CZ  . TYR A 526 ? 1.27480 0.89679 1.34478 -0.36850 0.13492  -0.18801 803 TYR B CZ  
3620 O OH  . TYR A 526 ? 1.32906 0.94201 1.41860 -0.38098 0.14801  -0.16760 803 TYR B OH  
3621 N N   . THR A 527 ? 0.93247 0.70898 0.89943 -0.26123 0.05526  -0.23518 804 THR B N   
3622 C CA  . THR A 527 ? 0.92806 0.73418 0.87476 -0.24607 0.04328  -0.24971 804 THR B CA  
3623 C C   . THR A 527 ? 0.93599 0.73125 0.86589 -0.21036 0.04304  -0.22326 804 THR B C   
3624 O O   . THR A 527 ? 0.94153 0.71109 0.85372 -0.19549 0.04671  -0.23100 804 THR B O   
3625 C CB  . THR A 527 ? 0.95960 0.84497 0.91254 -0.25423 0.02511  -0.25847 804 THR B CB  
3626 O OG1 . THR A 527 ? 1.02287 0.92107 0.99497 -0.28972 0.02532  -0.28378 804 THR B OG1 
3627 C CG2 . THR A 527 ? 0.92969 0.84791 0.86005 -0.23958 0.01357  -0.27342 804 THR B CG2 
3628 N N   . ALA A 528 ? 0.86672 0.68148 0.80312 -0.19690 0.03963  -0.19284 805 ALA B N   
3629 C CA  . ALA A 528 ? 0.86062 0.66879 0.78430 -0.16577 0.03888  -0.16858 805 ALA B CA  
3630 C C   . ALA A 528 ? 0.91527 0.65936 0.83030 -0.15431 0.05289  -0.16351 805 ALA B C   
3631 O O   . ALA A 528 ? 0.86190 0.59743 0.76211 -0.13378 0.05287  -0.16287 805 ALA B O   
3632 C CB  . ALA A 528 ? 0.80143 0.63180 0.73553 -0.15784 0.03590  -0.13995 805 ALA B CB  
3633 N N   . PHE A 529 ? 0.89345 0.59328 0.81858 -0.16650 0.06594  -0.15842 806 PHE B N   
3634 C CA  . PHE A 529 ? 0.93609 0.57496 0.85470 -0.15338 0.08033  -0.14980 806 PHE B CA  
3635 C C   . PHE A 529 ? 1.00210 0.61489 0.90868 -0.15200 0.08530  -0.17670 806 PHE B C   
3636 O O   . PHE A 529 ? 1.00341 0.59007 0.89887 -0.12891 0.09079  -0.16954 806 PHE B O   
3637 C CB  . PHE A 529 ? 0.98974 0.58646 0.92187 -0.16901 0.09493  -0.14017 806 PHE B CB  
3638 C CG  . PHE A 529 ? 1.00957 0.54780 0.93625 -0.15106 0.10975  -0.12234 806 PHE B CG  
3639 C CD1 . PHE A 529 ? 0.94036 0.48280 0.85717 -0.12122 0.10625  -0.09858 806 PHE B CD1 
3640 C CD2 . PHE A 529 ? 1.09686 0.57685 1.02997 -0.16395 0.12773  -0.12845 806 PHE B CD2 
3641 C CE1 . PHE A 529 ? 1.00792 0.50282 0.92090 -0.10297 0.11888  -0.08068 806 PHE B CE1 
3642 C CE2 . PHE A 529 ? 1.09708 0.52376 1.02577 -0.14428 0.14223  -0.10870 806 PHE B CE2 
3643 C CZ  . PHE A 529 ? 1.03428 0.47138 0.95264 -0.11291 0.13695  -0.08443 806 PHE B CZ  
3644 N N   . LEU A 530 ? 0.94222 0.56352 0.85127 -0.17667 0.08380  -0.20903 807 LEU B N   
3645 C CA  . LEU A 530 ? 0.96630 0.56207 0.86219 -0.17681 0.08953  -0.23854 807 LEU B CA  
3646 C C   . LEU A 530 ? 0.99823 0.63193 0.87505 -0.15446 0.07851  -0.24176 807 LEU B C   
3647 O O   . LEU A 530 ? 1.04263 0.64894 0.90551 -0.13970 0.08606  -0.25174 807 LEU B O   
3648 C CB  . LEU A 530 ? 1.01311 0.61335 0.91625 -0.21124 0.08955  -0.27540 807 LEU B CB  
3649 C CG  . LEU A 530 ? 1.08200 0.62976 1.00369 -0.23629 0.10599  -0.28004 807 LEU B CG  
3650 C CD1 . LEU A 530 ? 1.19788 0.75684 1.12596 -0.27085 0.10417  -0.32219 807 LEU B CD1 
3651 C CD2 . LEU A 530 ? 1.23594 0.70656 1.15283 -0.22104 0.12656  -0.27241 807 LEU B CD2 
3652 N N   . HIS A 531 ? 0.91272 0.60900 0.78918 -0.15112 0.06220  -0.23302 808 HIS B N   
3653 C CA  . HIS A 531 ? 0.91112 0.64381 0.77030 -0.12978 0.05325  -0.23250 808 HIS B CA  
3654 C C   . HIS A 531 ? 0.93356 0.64523 0.78811 -0.09990 0.05878  -0.20486 808 HIS B C   
3655 O O   . HIS A 531 ? 0.92800 0.63036 0.76839 -0.08281 0.06298  -0.21073 808 HIS B O   
3656 C CB  . HIS A 531 ? 0.84841 0.65026 0.71052 -0.13207 0.03628  -0.22607 808 HIS B CB  
3657 C CG  . HIS A 531 ? 0.95587 0.79582 0.81711 -0.15539 0.02726  -0.25651 808 HIS B CG  
3658 N ND1 . HIS A 531 ? 0.99687 0.89559 0.86838 -0.16468 0.01362  -0.25252 808 HIS B ND1 
3659 C CD2 . HIS A 531 ? 1.03927 0.87036 0.89079 -0.17093 0.02956  -0.29248 808 HIS B CD2 
3660 C CE1 . HIS A 531 ? 1.01117 0.93928 0.88010 -0.18534 0.00668  -0.28390 808 HIS B CE1 
3661 N NE2 . HIS A 531 ? 1.04314 0.93041 0.89935 -0.19068 0.01603  -0.30994 808 HIS B NE2 
3662 N N   . LEU A 532 ? 0.90464 0.61157 0.77137 -0.09369 0.05897  -0.17544 809 LEU B N   
3663 C CA  . LEU A 532 ? 0.89475 0.58747 0.75946 -0.06744 0.06262  -0.14963 809 LEU B CA  
3664 C C   . LEU A 532 ? 0.91317 0.54908 0.77419 -0.05746 0.07785  -0.15212 809 LEU B C   
3665 O O   . LEU A 532 ? 0.88502 0.51604 0.73999 -0.03426 0.08075  -0.14221 809 LEU B O   
3666 C CB  . LEU A 532 ? 0.84575 0.54585 0.72314 -0.06613 0.05963  -0.12178 809 LEU B CB  
3667 C CG  . LEU A 532 ? 0.83586 0.59116 0.71803 -0.07183 0.04618  -0.11739 809 LEU B CG  
3668 C CD1 . LEU A 532 ? 0.84573 0.60540 0.73996 -0.07289 0.04518  -0.09402 809 LEU B CD1 
3669 C CD2 . LEU A 532 ? 0.78590 0.57509 0.65903 -0.05288 0.03887  -0.11244 809 LEU B CD2 
3670 N N   . ARG A 533 ? 0.90948 0.50233 0.77594 -0.07431 0.08874  -0.16445 810 ARG B N   
3671 C CA  . ARG A 533 ? 1.03474 0.57018 0.89768 -0.06511 0.10525  -0.17046 810 ARG B CA  
3672 C C   . ARG A 533 ? 1.01667 0.55648 0.86386 -0.05398 0.10680  -0.19294 810 ARG B C   
3673 O O   . ARG A 533 ? 1.02063 0.53167 0.86340 -0.03217 0.11715  -0.18751 810 ARG B O   
3674 C CB  . ARG A 533 ? 1.04982 0.53993 0.92115 -0.08994 0.11740  -0.18698 810 ARG B CB  
3675 C CG  . ARG A 533 ? 1.04639 0.50931 0.93195 -0.09487 0.12465  -0.16122 810 ARG B CG  
3676 C CD  . ARG A 533 ? 1.14278 0.57402 1.03934 -0.12645 0.13462  -0.18063 810 ARG B CD  
3677 N NE  . ARG A 533 ? 1.20880 0.59266 1.10076 -0.13278 0.14855  -0.21061 810 ARG B NE  
3678 C CZ  . ARG A 533 ? 1.25933 0.57993 1.15413 -0.12269 0.16758  -0.20355 810 ARG B CZ  
3679 N NH1 . ARG A 533 ? 1.27646 0.57628 1.17625 -0.10280 0.17409  -0.16636 810 ARG B NH1 
3680 N NH2 . ARG A 533 ? 1.31138 0.60921 1.20696 -0.12832 0.17439  -0.22827 810 ARG B NH2 
3681 N N   . ARG A 534 ? 0.98262 0.56011 0.82099 -0.06825 0.09723  -0.21855 811 ARG B N   
3682 C CA  . ARG A 534 ? 0.99291 0.57959 0.81303 -0.05785 0.09875  -0.24074 811 ARG B CA  
3683 C C   . ARG A 534 ? 0.95746 0.57238 0.77161 -0.02901 0.09471  -0.21837 811 ARG B C   
3684 O O   . ARG A 534 ? 1.01692 0.62949 0.81776 -0.01381 0.10075  -0.22947 811 ARG B O   
3685 C CB  . ARG A 534 ? 0.98334 0.61330 0.79380 -0.07858 0.08738  -0.27049 811 ARG B CB  
3686 N N   . TYR A 535 ? 0.92244 0.56247 0.74706 -0.02165 0.08606  -0.18791 812 TYR B N   
3687 C CA  . TYR A 535 ? 0.93241 0.59722 0.75564 0.00309  0.08307  -0.16588 812 TYR B CA  
3688 C C   . TYR A 535 ? 0.88521 0.52050 0.72026 0.02002  0.09020  -0.13941 812 TYR B C   
3689 O O   . TYR A 535 ? 0.86108 0.52105 0.70134 0.03534  0.08512  -0.11700 812 TYR B O   
3690 C CB  . TYR A 535 ? 0.88623 0.60605 0.71200 0.00042  0.06794  -0.15267 812 TYR B CB  
3691 C CG  . TYR A 535 ? 0.89100 0.64972 0.70219 -0.00691 0.06079  -0.17395 812 TYR B CG  
3692 C CD1 . TYR A 535 ? 0.93300 0.71534 0.73044 0.00978  0.06167  -0.17586 812 TYR B CD1 
3693 C CD2 . TYR A 535 ? 0.97146 0.74578 0.78264 -0.03041 0.05363  -0.19213 812 TYR B CD2 
3694 C CE1 . TYR A 535 ? 0.98925 0.81028 0.77026 0.00446  0.05519  -0.19439 812 TYR B CE1 
3695 C CE2 . TYR A 535 ? 0.96960 0.78478 0.76639 -0.03665 0.04584  -0.21208 812 TYR B CE2 
3696 C CZ  . TYR A 535 ? 1.06749 0.90605 0.84774 -0.01851 0.04645  -0.21261 812 TYR B CZ  
3697 O OH  . TYR A 535 ? 1.18958 1.07249 0.95285 -0.02355 0.03844  -0.23117 812 TYR B OH  
3698 N N   . SER A 536 ? 0.88827 0.47188 0.72799 0.01791  0.10238  -0.14148 813 SER B N   
3699 C CA  . SER A 536 ? 0.92422 0.48480 0.77486 0.03461  0.10789  -0.11341 813 SER B CA  
3700 C C   . SER A 536 ? 0.87987 0.44708 0.72940 0.06245  0.11210  -0.10359 813 SER B C   
3701 O O   . SER A 536 ? 0.91953 0.50241 0.77829 0.07680  0.10794  -0.07799 813 SER B O   
3702 C CB  . SER A 536 ? 0.91304 0.41539 0.76872 0.02822  0.12191  -0.11504 813 SER B CB  
3703 O OG  . SER A 536 ? 1.06437 0.52980 0.91244 0.03041  0.13562  -0.13954 813 SER B OG  
3704 N N   . ASN A 537 ? 0.85686 0.41679 0.69554 0.06980  0.12012  -0.12465 814 ASN B N   
3705 C CA  . ASN A 537 ? 0.94087 0.51227 0.78010 0.09622  0.12510  -0.11546 814 ASN B CA  
3706 C C   . ASN A 537 ? 0.92695 0.55277 0.77085 0.10205  0.11217  -0.09747 814 ASN B C   
3707 O O   . ASN A 537 ? 0.82722 0.46386 0.68327 0.11878  0.11155  -0.07457 814 ASN B O   
3708 C CB  . ASN A 537 ? 0.93601 0.49826 0.76008 0.10140  0.13544  -0.14352 814 ASN B CB  
3709 C CG  . ASN A 537 ? 1.20660 0.70768 1.02916 0.10262  0.15265  -0.15919 814 ASN B CG  
3710 O OD1 . ASN A 537 ? 1.28289 0.74728 1.11597 0.09865  0.15716  -0.14748 814 ASN B OD1 
3711 N ND2 . ASN A 537 ? 1.33394 0.82233 1.14268 0.10828  0.16370  -0.18595 814 ASN B ND2 
3712 N N   . LEU A 538 ? 0.85388 0.51525 0.68950 0.08828  0.10198  -0.10719 815 LEU B N   
3713 C CA  . LEU A 538 ? 0.82911 0.53710 0.67027 0.09331  0.09182  -0.08955 815 LEU B CA  
3714 C C   . LEU A 538 ? 0.84701 0.55886 0.70423 0.09179  0.08441  -0.06487 815 LEU B C   
3715 O O   . LEU A 538 ? 0.82272 0.55494 0.69079 0.10432  0.08194  -0.04610 815 LEU B O   
3716 C CB  . LEU A 538 ? 0.86890 0.61194 0.69866 0.07949  0.08279  -0.10186 815 LEU B CB  
3717 C CG  . LEU A 538 ? 0.88883 0.67470 0.72628 0.08225  0.07309  -0.08177 815 LEU B CG  
3718 C CD1 . LEU A 538 ? 0.79265 0.59762 0.63255 0.10198  0.07869  -0.07133 815 LEU B CD1 
3719 C CD2 . LEU A 538 ? 0.84971 0.66723 0.67782 0.06823  0.06374  -0.09080 815 LEU B CD2 
3720 N N   . ILE A 539 ? 0.86485 0.55964 0.72402 0.07561  0.08106  -0.06540 816 ILE B N   
3721 C CA  . ILE A 539 ? 0.86377 0.56631 0.73506 0.07392  0.07403  -0.04331 816 ILE B CA  
3722 C C   . ILE A 539 ? 0.78483 0.46768 0.66509 0.09139  0.07985  -0.02567 816 ILE B C   
3723 O O   . ILE A 539 ? 0.77837 0.48319 0.66851 0.09977  0.07406  -0.00729 816 ILE B O   
3724 C CB  . ILE A 539 ? 0.85404 0.54577 0.72516 0.05266  0.07055  -0.04756 816 ILE B CB  
3725 C CG1 . ILE A 539 ? 0.82404 0.55015 0.69045 0.03842  0.06157  -0.05916 816 ILE B CG1 
3726 C CG2 . ILE A 539 ? 0.79341 0.48593 0.67428 0.05280  0.06645  -0.02555 816 ILE B CG2 
3727 C CD1 . ILE A 539 ? 0.90012 0.61738 0.76581 0.01612  0.06020  -0.07186 816 ILE B CD1 
3728 N N   . LEU A 540 ? 0.81990 0.46253 0.69751 0.09784  0.09164  -0.03130 817 LEU B N   
3729 C CA  . LEU A 540 ? 0.86095 0.48809 0.74744 0.11814  0.09766  -0.01264 817 LEU B CA  
3730 C C   . LEU A 540 ? 0.86930 0.52696 0.76276 0.13758  0.09701  -0.00561 817 LEU B C   
3731 O O   . LEU A 540 ? 0.86122 0.53516 0.76666 0.15020  0.09331  0.01457  817 LEU B O   
3732 C CB  . LEU A 540 ? 0.79365 0.36804 0.67650 0.12310  0.11301  -0.02029 817 LEU B CB  
3733 C CG  . LEU A 540 ? 0.88263 0.42449 0.76279 0.10297  0.11553  -0.02351 817 LEU B CG  
3734 C CD1 . LEU A 540 ? 0.94140 0.42557 0.81945 0.10616  0.13309  -0.03242 817 LEU B CD1 
3735 C CD2 . LEU A 540 ? 0.85388 0.40527 0.74110 0.10276  0.10866  0.00260  817 LEU B CD2 
3736 N N   . ASN A 541 ? 0.84678 0.51608 0.73314 0.13960  0.10058  -0.02214 818 ASN B N   
3737 C CA  . ASN A 541 ? 0.78519 0.48608 0.67927 0.15643  0.10160  -0.01538 818 ASN B CA  
3738 C C   . ASN A 541 ? 0.75180 0.49425 0.65760 0.15252  0.08912  0.00080  818 ASN B C   
3739 O O   . ASN A 541 ? 0.72131 0.48421 0.64223 0.16574  0.08797  0.01617  818 ASN B O   
3740 C CB  . ASN A 541 ? 0.78039 0.49025 0.66143 0.15672  0.10747  -0.03574 818 ASN B CB  
3741 C CG  . ASN A 541 ? 0.87089 0.54698 0.74504 0.16998  0.12299  -0.04985 818 ASN B CG  
3742 O OD1 . ASN A 541 ? 0.90648 0.55350 0.78853 0.18224  0.13032  -0.04126 818 ASN B OD1 
3743 N ND2 . ASN A 541 ? 0.90729 0.58787 0.76594 0.16896  0.12880  -0.07134 818 ASN B ND2 
3744 N N   . LEU A 542 ? 0.67467 0.43134 0.57504 0.13445  0.08019  -0.00339 819 LEU B N   
3745 C CA  . LEU A 542 ? 0.66653 0.45761 0.57817 0.13052  0.07032  0.01009  819 LEU B CA  
3746 C C   . LEU A 542 ? 0.78134 0.57119 0.70485 0.13389  0.06524  0.02708  819 LEU B C   
3747 O O   . LEU A 542 ? 0.71889 0.53529 0.65681 0.14063  0.06130  0.03898  819 LEU B O   
3748 C CB  . LEU A 542 ? 0.65675 0.45943 0.56081 0.11236  0.06291  0.00349  819 LEU B CB  
3749 C CG  . LEU A 542 ? 0.68525 0.50272 0.57784 0.11070  0.06562  -0.00980 819 LEU B CG  
3750 C CD1 . LEU A 542 ? 0.73065 0.55992 0.61548 0.09433  0.05823  -0.01626 819 LEU B CD1 
3751 C CD2 . LEU A 542 ? 0.70204 0.54962 0.60391 0.12181  0.06790  -0.00025 819 LEU B CD2 
3752 N N   . PHE A 543 ? 0.72944 0.49041 0.64716 0.12873  0.06562  0.02839  820 PHE B N   
3753 C CA  . PHE A 543 ? 0.74563 0.50727 0.67112 0.13365  0.06120  0.04585  820 PHE B CA  
3754 C C   . PHE A 543 ? 0.72808 0.49515 0.66477 0.15538  0.06526  0.05733  820 PHE B C   
3755 O O   . PHE A 543 ? 0.68734 0.47818 0.63500 0.16113  0.05819  0.07168  820 PHE B O   
3756 C CB  . PHE A 543 ? 0.79443 0.52166 0.71088 0.12585  0.06397  0.04721  820 PHE B CB  
3757 C CG  . PHE A 543 ? 0.76183 0.49840 0.67468 0.10731  0.05606  0.04676  820 PHE B CG  
3758 C CD1 . PHE A 543 ? 0.73352 0.49034 0.65130 0.10682  0.04789  0.06061  820 PHE B CD1 
3759 C CD2 . PHE A 543 ? 0.75489 0.48436 0.65979 0.09058  0.05657  0.03127  820 PHE B CD2 
3760 C CE1 . PHE A 543 ? 0.77830 0.54432 0.69279 0.09089  0.04202  0.05931  820 PHE B CE1 
3761 C CE2 . PHE A 543 ? 0.77780 0.51940 0.68158 0.07491  0.04995  0.03146  820 PHE B CE2 
3762 C CZ  . PHE A 543 ? 0.80582 0.56421 0.71429 0.07556  0.04345  0.04556  820 PHE B CZ  
3763 N N   . SER A 544 ? 0.70295 0.45123 0.63759 0.16796  0.07654  0.05036  821 SER B N   
3764 C CA  . SER A 544 ? 0.77663 0.53343 0.72435 0.19095  0.08124  0.06233  821 SER B CA  
3765 C C   . SER A 544 ? 0.71954 0.52363 0.68336 0.19527  0.07589  0.06674  821 SER B C   
3766 O O   . SER A 544 ? 0.79181 0.61712 0.77164 0.21104  0.07502  0.08006  821 SER B O   
3767 C CB  . SER A 544 ? 0.70083 0.42408 0.64282 0.20461  0.09674  0.05253  821 SER B CB  
3768 O OG  . SER A 544 ? 0.89132 0.63003 0.83153 0.20557  0.10138  0.03829  821 SER B OG  
3769 N N   . LEU A 545 ? 0.64386 0.46648 0.60541 0.18162  0.07261  0.05709  822 LEU B N   
3770 C CA  . LEU A 545 ? 0.70017 0.56505 0.67893 0.18246  0.06856  0.06264  822 LEU B CA  
3771 C C   . LEU A 545 ? 0.64433 0.53261 0.63362 0.17265  0.05567  0.07258  822 LEU B C   
3772 O O   . LEU A 545 ? 0.64461 0.56765 0.65219 0.17264  0.05202  0.07773  822 LEU B O   
3773 C CB  . LEU A 545 ? 0.60754 0.48175 0.57945 0.17349  0.07204  0.05110  822 LEU B CB  
3774 C CG  . LEU A 545 ? 0.68453 0.54548 0.64609 0.18442  0.08504  0.03966  822 LEU B CG  
3775 C CD1 . LEU A 545 ? 0.64548 0.51953 0.59632 0.17616  0.08773  0.02965  822 LEU B CD1 
3776 C CD2 . LEU A 545 ? 0.67752 0.55404 0.65595 0.20506  0.09286  0.04751  822 LEU B CD2 
3777 N N   . MET A 546 ? 0.63535 0.50586 0.61416 0.16416  0.04971  0.07468  823 MET B N   
3778 C CA  . MET A 546 ? 0.60703 0.49726 0.59116 0.15408  0.03820  0.08117  823 MET B CA  
3779 C C   . MET A 546 ? 0.67584 0.57427 0.66549 0.16534  0.03303  0.09539  823 MET B C   
3780 O O   . MET A 546 ? 0.62287 0.54049 0.61496 0.15774  0.02304  0.09974  823 MET B O   
3781 C CB  . MET A 546 ? 0.61019 0.48116 0.57836 0.13703  0.03521  0.07474  823 MET B CB  
3782 C CG  . MET A 546 ? 0.65511 0.52679 0.61846 0.12547  0.03744  0.06294  823 MET B CG  
3783 S SD  . MET A 546 ? 0.66897 0.57789 0.64994 0.11992  0.03417  0.06371  823 MET B SD  
3784 C CE  . MET A 546 ? 0.58657 0.50851 0.57227 0.10824  0.02326  0.06768  823 MET B CE  
3785 N N   . VAL A 547 ? 0.63822 0.52348 0.62906 0.18432  0.03994  0.10291  824 VAL B N   
3786 C CA  . VAL A 547 ? 0.67069 0.55960 0.66254 0.19655  0.03567  0.11930  824 VAL B CA  
3787 C C   . VAL A 547 ? 0.69672 0.63671 0.70778 0.20097  0.02452  0.12774  824 VAL B C   
3788 O O   . VAL A 547 ? 0.77082 0.72403 0.77997 0.20583  0.01665  0.13993  824 VAL B O   
3789 C CB  . VAL A 547 ? 0.74778 0.60754 0.73765 0.21842  0.04759  0.12726  824 VAL B CB  
3790 C CG1 . VAL A 547 ? 0.79184 0.59841 0.76246 0.21093  0.05813  0.11755  824 VAL B CG1 
3791 C CG2 . VAL A 547 ? 0.65906 0.53738 0.66600 0.23418  0.05424  0.12554  824 VAL B CG2 
3792 N N   . ASP A 548 ? 0.61934 0.59065 0.64910 0.19884  0.02374  0.12173  825 ASP B N   
3793 C CA  . ASP A 548 ? 0.59230 0.61415 0.64297 0.19803  0.01275  0.12625  825 ASP B CA  
3794 C C   . ASP A 548 ? 0.64067 0.67886 0.69382 0.17415  0.00464  0.11517  825 ASP B C   
3795 O O   . ASP A 548 ? 0.66987 0.74892 0.74270 0.16891  -0.00325 0.11411  825 ASP B O   
3796 C CB  . ASP A 548 ? 0.72389 0.77494 0.79942 0.21040  0.01798  0.12800  825 ASP B CB  
3797 C CG  . ASP A 548 ? 0.62881 0.66132 0.70350 0.23593  0.02912  0.13701  825 ASP B CG  
3798 O OD1 . ASP A 548 ? 0.74939 0.77556 0.81822 0.25016  0.02664  0.15036  825 ASP B OD1 
3799 N N   . ALA A 549 ? 0.57552 0.58393 0.61111 0.15954  0.00689  0.10635  826 ALA B N   
3800 C CA  . ALA A 549 ? 0.66350 0.68456 0.70264 0.13935  0.00135  0.09649  826 ALA B CA  
3801 C C   . ALA A 549 ? 0.68031 0.71824 0.71488 0.13285  -0.01061 0.09816  826 ALA B C   
3802 O O   . ALA A 549 ? 0.62777 0.65682 0.64791 0.14129  -0.01352 0.10741  826 ALA B O   
3803 C CB  . ALA A 549 ? 0.59538 0.58366 0.61831 0.12791  0.00753  0.08775  826 ALA B CB  
3804 N N   A ASN A 550 ? 0.62872 0.69035 0.67516 0.11759  -0.01642 0.08888  827 ASN B N   
3805 N N   B ASN A 550 ? 0.62009 0.68188 0.66651 0.11768  -0.01649 0.08896  827 ASN B N   
3806 C CA  A ASN A 550 ? 0.62822 0.70672 0.66865 0.10838  -0.02722 0.08543  827 ASN B CA  
3807 C CA  B ASN A 550 ? 0.62759 0.70640 0.66772 0.10917  -0.02739 0.08605  827 ASN B CA  
3808 C C   A ASN A 550 ? 0.65840 0.70492 0.67684 0.09790  -0.02443 0.08019  827 ASN B C   
3809 C C   B ASN A 550 ? 0.65809 0.70557 0.67652 0.09822  -0.02478 0.08048  827 ASN B C   
3810 O O   A ASN A 550 ? 0.68083 0.72736 0.70105 0.08283  -0.02475 0.06893  827 ASN B O   
3811 O O   B ASN A 550 ? 0.67791 0.72684 0.69829 0.08308  -0.02559 0.06914  827 ASN B O   
3812 C CB  A ASN A 550 ? 0.59903 0.71324 0.66280 0.09512  -0.03294 0.07455  827 ASN B CB  
3813 C CB  B ASN A 550 ? 0.59859 0.71509 0.66206 0.09662  -0.03380 0.07567  827 ASN B CB  
3814 C CG  A ASN A 550 ? 0.64317 0.78316 0.70179 0.08729  -0.04540 0.06884  827 ASN B CG  
3815 C CG  B ASN A 550 ? 0.59021 0.74694 0.67708 0.10719  -0.03842 0.08193  827 ASN B CG  
3816 O OD1 A ASN A 550 ? 0.70296 0.84111 0.74132 0.09551  -0.05054 0.07702  827 ASN B OD1 
3817 O OD1 B ASN A 550 ? 0.59347 0.74967 0.67807 0.12650  -0.03674 0.09536  827 ASN B OD1 
3818 N ND2 A ASN A 550 ? 0.58789 0.75219 0.66465 0.07107  -0.04944 0.05446  827 ASN B ND2 
3819 N ND2 B ASN A 550 ? 0.59626 0.78808 0.70759 0.09442  -0.04335 0.07190  827 ASN B ND2 
3820 N N   . ILE A 551 ? 0.63532 0.65333 0.63469 0.10639  -0.02023 0.08874  828 ILE B N   
3821 C CA  . ILE A 551 ? 0.64821 0.63850 0.62780 0.09764  -0.01718 0.08587  828 ILE B CA  
3822 C C   . ILE A 551 ? 0.62321 0.61207 0.58565 0.10446  -0.02109 0.09716  828 ILE B C   
3823 O O   . ILE A 551 ? 0.62948 0.60640 0.58735 0.11891  -0.01786 0.10998  828 ILE B O   
3824 C CB  . ILE A 551 ? 0.65626 0.61258 0.62959 0.09835  -0.00687 0.08461  828 ILE B CB  
3825 C CG1 . ILE A 551 ? 0.66291 0.62538 0.65161 0.09396  -0.00266 0.07627  828 ILE B CG1 
3826 C CG2 . ILE A 551 ? 0.62927 0.56129 0.58430 0.08906  -0.00419 0.08262  828 ILE B CG2 
3827 C CD1 . ILE A 551 ? 0.61308 0.55710 0.59511 0.08407  0.00280  0.06871  828 ILE B CD1 
3828 N N   . PRO A 552 ? 0.64277 0.64180 0.59446 0.09557  -0.02647 0.09374  829 PRO B N   
3829 C CA  . PRO A 552 ? 0.64279 0.65210 0.57906 0.10420  -0.03150 0.10673  829 PRO B CA  
3830 C C   . PRO A 552 ? 0.66376 0.63987 0.58591 0.11475  -0.02310 0.12259  829 PRO B C   
3831 O O   . PRO A 552 ? 0.65082 0.63335 0.56987 0.13081  -0.02454 0.13883  829 PRO B O   
3832 C CB  . PRO A 552 ? 0.58739 0.60592 0.51154 0.09042  -0.03511 0.09705  829 PRO B CB  
3833 C CG  . PRO A 552 ? 0.63113 0.65405 0.57062 0.07672  -0.03474 0.07882  829 PRO B CG  
3834 C CD  . PRO A 552 ? 0.63429 0.63397 0.58547 0.07905  -0.02653 0.07915  829 PRO B CD  
3835 N N   . ASP A 553 ? 0.64139 0.58284 0.55621 0.10629  -0.01390 0.11872  830 ASP B N   
3836 C CA  . ASP A 553 ? 0.73677 0.64548 0.63926 0.11360  -0.00506 0.13279  830 ASP B CA  
3837 C C   . ASP A 553 ? 0.75525 0.64528 0.66652 0.12794  0.00126  0.13892  830 ASP B C   
3838 O O   . ASP A 553 ? 0.74334 0.60655 0.64665 0.13766  0.00909  0.15275  830 ASP B O   
3839 C CB  . ASP A 553 ? 0.73483 0.61613 0.62848 0.09835  0.00258  0.12584  830 ASP B CB  
3840 C CG  . ASP A 553 ? 0.81753 0.71210 0.69752 0.08961  -0.00014 0.12708  830 ASP B CG  
3841 O OD1 . ASP A 553 ? 0.84952 0.77274 0.72440 0.09554  -0.00808 0.13258  830 ASP B OD1 
3842 O OD2 . ASP A 553 ? 0.80481 0.68486 0.67913 0.07715  0.00553  0.12205  830 ASP B OD2 
3843 N N   . ILE A 554 ? 0.69062 0.59407 0.61839 0.13039  -0.00064 0.12987  831 ILE B N   
3844 C CA  . ILE A 554 ? 0.69276 0.58567 0.62971 0.14678  0.00527  0.13563  831 ILE B CA  
3845 C C   . ILE A 554 ? 0.78498 0.71074 0.73060 0.16471  -0.00170 0.14966  831 ILE B C   
3846 O O   . ILE A 554 ? 0.80701 0.72008 0.75266 0.18357  0.00393  0.16447  831 ILE B O   
3847 C CB  . ILE A 554 ? 0.72163 0.61477 0.67142 0.14180  0.00846  0.12026  831 ILE B CB  
3848 C CG1 . ILE A 554 ? 0.72248 0.58506 0.66290 0.12729  0.01535  0.10803  831 ILE B CG1 
3849 C CG2 . ILE A 554 ? 0.69386 0.58378 0.65423 0.16050  0.01449  0.12566  831 ILE B CG2 
3850 C CD1 . ILE A 554 ? 0.60426 0.47180 0.55392 0.12210  0.01788  0.09396  831 ILE B CD1 
3851 N N   . ALA A 555 ? 0.72687 0.69632 0.68139 0.15942  -0.01370 0.14480  832 ALA B N   
3852 C CA  . ALA A 555 ? 0.68604 0.69612 0.65165 0.17487  -0.02239 0.15605  832 ALA B CA  
3853 C C   . ALA A 555 ? 0.76562 0.77784 0.71490 0.18872  -0.02472 0.17692  832 ALA B C   
3854 O O   . ALA A 555 ? 0.79393 0.83517 0.75070 0.20761  -0.02991 0.19166  832 ALA B O   
3855 C CB  . ALA A 555 ? 0.60027 0.65645 0.57919 0.16161  -0.03478 0.14254  832 ALA B CB  
3856 N N   . LEU A 556 ? 0.76282 0.74714 0.69077 0.18063  -0.02031 0.18002  833 LEU B N   
3857 C CA  . LEU A 556 ? 0.82161 0.80193 0.73208 0.19407  -0.01918 0.20278  833 LEU B CA  
3858 C C   . LEU A 556 ? 0.83003 0.77958 0.74308 0.21664  -0.00749 0.22201  833 LEU B C   
3859 O O   . LEU A 556 ? 0.93409 0.89630 0.84213 0.23707  -0.00875 0.24528  833 LEU B O   
3860 C CB  . LEU A 556 ? 0.83113 0.78395 0.72077 0.17866  -0.01359 0.20122  833 LEU B CB  
3861 C CG  . LEU A 556 ? 0.95090 0.93705 0.82727 0.16730  -0.02392 0.19629  833 LEU B CG  
3862 C CD1 . LEU A 556 ? 1.03769 0.99187 0.89598 0.15370  -0.01464 0.19617  833 LEU B CD1 
3863 C CD2 . LEU A 556 ? 0.92392 0.94749 0.79199 0.18538  -0.03270 0.21618  833 LEU B CD2 
3864 N N   . GLU A 557 ? 0.87171 0.78002 0.79144 0.21390  0.00472  0.21260  834 GLU B N   
3865 C CA  . GLU A 557 ? 0.91121 0.78049 0.83305 0.23333  0.01900  0.22639  834 GLU B CA  
3866 C C   . GLU A 557 ? 0.88024 0.73204 0.81640 0.23112  0.02609  0.20824  834 GLU B C   
3867 O O   . GLU A 557 ? 0.90456 0.70900 0.83548 0.22435  0.03883  0.19967  834 GLU B O   
3868 C CB  . GLU A 557 ? 0.99755 0.81538 0.90169 0.22830  0.03214  0.23522  834 GLU B CB  
3869 C CG  . GLU A 557 ? 1.14139 0.96277 1.03408 0.24004  0.03318  0.26008  834 GLU B CG  
3870 C CD  . GLU A 557 ? 1.23751 1.01376 1.11510 0.22625  0.04553  0.26361  834 GLU B CD  
3871 O OE1 . GLU A 557 ? 1.19433 0.94931 1.06762 0.20679  0.04862  0.24784  834 GLU B OE1 
3872 O OE2 . GLU A 557 ? 1.40679 1.17164 1.27886 0.23342  0.05225  0.28082  834 GLU B OE2 
3873 N N   . PRO A 558 ? 0.88181 0.77304 0.83633 0.23614  0.01852  0.20147  835 PRO B N   
3874 C CA  . PRO A 558 ? 0.87435 0.75245 0.84055 0.23344  0.02597  0.18426  835 PRO B CA  
3875 C C   . PRO A 558 ? 0.90616 0.73438 0.86967 0.24812  0.04329  0.18805  835 PRO B C   
3876 O O   . PRO A 558 ? 0.87484 0.67396 0.83624 0.23857  0.05209  0.17037  835 PRO B O   
3877 C CB  . PRO A 558 ? 0.84630 0.77787 0.83503 0.24309  0.01703  0.18481  835 PRO B CB  
3878 C CG  . PRO A 558 ? 0.75613 0.73168 0.74418 0.24382  0.00199  0.19600  835 PRO B CG  
3879 C CD  . PRO A 558 ? 0.81584 0.76376 0.78254 0.24927  0.00541  0.21264  835 PRO B CD  
3880 N N   . ASP A 559 ? 0.84148 0.65938 0.80441 0.26988  0.04872  0.20934  836 ASP B N   
3881 C CA  . ASP A 559 ? 0.99842 0.77342 0.96237 0.27829  0.06508  0.20708  836 ASP B CA  
3882 C C   . ASP A 559 ? 1.01067 0.72849 0.95791 0.26470  0.07659  0.20333  836 ASP B C   
3883 O O   . ASP A 559 ? 1.06908 0.74610 1.01668 0.26775  0.09100  0.19666  836 ASP B O   
3884 C CB  . ASP A 559 ? 0.90867 0.70216 0.88198 0.29964  0.06570  0.22581  836 ASP B CB  
3885 C CG  . ASP A 559 ? 1.10639 0.91746 1.06995 0.30075  0.05740  0.24578  836 ASP B CG  
3886 O OD1 . ASP A 559 ? 0.95135 0.78546 0.90672 0.28821  0.04538  0.24532  836 ASP B OD1 
3887 O OD2 . ASP A 559 ? 1.20218 1.00457 1.16536 0.31482  0.06350  0.26212  836 ASP B OD2 
3888 N N   . LYS A 560 ? 0.95642 0.67129 0.89006 0.24929  0.07124  0.20682  837 LYS B N   
3889 C CA  . LYS A 560 ? 0.96566 0.63105 0.88609 0.23347  0.08200  0.20313  837 LYS B CA  
3890 C C   . LYS A 560 ? 0.97046 0.62617 0.88418 0.20941  0.08025  0.18160  837 LYS B C   
3891 O O   . LYS A 560 ? 0.98192 0.60178 0.88667 0.19271  0.08813  0.17570  837 LYS B O   
3892 C CB  . LYS A 560 ? 1.05506 0.72604 0.96529 0.23203  0.07920  0.22391  837 LYS B CB  
3893 C CG  . LYS A 560 ? 1.08431 0.78547 1.00020 0.25392  0.07496  0.24539  837 LYS B CG  
3894 C CD  . LYS A 560 ? 1.21666 0.88680 1.14128 0.26878  0.08922  0.24884  837 LYS B CD  
3895 C CE  . LYS A 560 ? 1.23731 0.93929 1.16759 0.29182  0.08540  0.27178  837 LYS B CE  
3896 N NZ  . LYS A 560 ? 1.35310 1.02491 1.29261 0.30830  0.10027  0.27575  837 LYS B NZ  
3897 N N   . THR A 561 ? 0.88603 0.58114 0.80723 0.20245  0.06885  0.16641  838 THR B N   
3898 C CA  . THR A 561 ? 0.90625 0.60732 0.82354 0.17662  0.06372  0.14486  838 THR B CA  
3899 C C   . THR A 561 ? 0.90786 0.56868 0.82151 0.16613  0.07532  0.12527  838 THR B C   
3900 O O   . THR A 561 ? 0.96343 0.60588 0.86924 0.14608  0.07742  0.11603  838 THR B O   
3901 C CB  . THR A 561 ? 0.90113 0.64989 0.82910 0.17474  0.05161  0.13588  838 THR B CB  
3902 O OG1 . THR A 561 ? 0.95455 0.74208 0.88533 0.17982  0.03981  0.14992  838 THR B OG1 
3903 C CG2 . THR A 561 ? 0.77075 0.52469 0.69558 0.15141  0.04787  0.11549  838 THR B CG2 
3904 N N   . VAL A 562 ? 0.88040 0.53083 0.79996 0.17885  0.08278  0.11724  839 VAL B N   
3905 C CA  . VAL A 562 ? 0.88816 0.50559 0.80244 0.16822  0.09273  0.09468  839 VAL B CA  
3906 C C   . VAL A 562 ? 0.91751 0.48206 0.82444 0.16204  0.10567  0.09628  839 VAL B C   
3907 O O   . VAL A 562 ? 0.89525 0.44196 0.79594 0.13984  0.10794  0.07966  839 VAL B O   
3908 C CB  . VAL A 562 ? 0.87891 0.49654 0.79955 0.18564  0.09974  0.08618  839 VAL B CB  
3909 C CG1 . VAL A 562 ? 0.91801 0.49903 0.83012 0.17589  0.11118  0.06133  839 VAL B CG1 
3910 C CG2 . VAL A 562 ? 0.80432 0.47389 0.73321 0.18592  0.08827  0.08238  839 VAL B CG2 
3911 N N   . LYS A 563 ? 0.87726 0.41878 0.78621 0.18119  0.11425  0.11795  840 LYS B N   
3912 C CA  . LYS A 563 ? 0.99233 0.48260 0.89666 0.17541  0.12823  0.12307  840 LYS B CA  
3913 C C   . LYS A 563 ? 1.07072 0.56107 0.96792 0.15082  0.12394  0.12398  840 LYS B C   
3914 O O   . LYS A 563 ? 1.04768 0.50051 0.94202 0.13230  0.13391  0.11236  840 LYS B O   
3915 C CB  . LYS A 563 ? 0.88624 0.38037 0.79763 0.19537  0.13082  0.14759  840 LYS B CB  
3916 C CG  . LYS A 563 ? 1.11613 0.56515 1.02729 0.18948  0.14497  0.15199  840 LYS B CG  
3917 C CD  . LYS A 563 ? 1.19705 0.60474 1.11107 0.18582  0.15885  0.12820  840 LYS B CD  
3918 C CE  . LYS A 563 ? 1.25065 0.61781 1.16882 0.18916  0.17356  0.13746  840 LYS B CE  
3919 N NZ  . LYS A 563 ? 1.21714 0.56960 1.13151 0.17228  0.17602  0.14994  840 LYS B NZ  
3920 N N   . LYS A 564 ? 0.96980 0.50525 0.86556 0.14875  0.10917  0.13573  841 LYS B N   
3921 C CA  . LYS A 564 ? 0.99468 0.53697 0.88447 0.12625  0.10496  0.13594  841 LYS B CA  
3922 C C   . LYS A 564 ? 0.99188 0.53087 0.88178 0.10067  0.10407  0.10746  841 LYS B C   
3923 O O   . LYS A 564 ? 1.04490 0.56510 0.93277 0.08088  0.10946  0.10336  841 LYS B O   
3924 C CB  . LYS A 564 ? 1.01968 0.61469 0.90769 0.12827  0.08870  0.14684  841 LYS B CB  
3925 C CG  . LYS A 564 ? 0.95782 0.56457 0.84206 0.14805  0.08715  0.17641  841 LYS B CG  
3926 C CD  . LYS A 564 ? 0.89726 0.56093 0.78060 0.14709  0.06940  0.17800  841 LYS B CD  
3927 C CE  . LYS A 564 ? 0.95933 0.64664 0.83877 0.16763  0.06442  0.20393  841 LYS B CE  
3928 N N   . VAL A 565 ? 0.93065 0.49152 0.82346 0.10087  0.09733  0.08857  842 VAL B N   
3929 C CA  . VAL A 565 ? 0.91545 0.47886 0.80710 0.07933  0.09552  0.06234  842 VAL B CA  
3930 C C   . VAL A 565 ? 0.98615 0.50267 0.87654 0.07415  0.10992  0.04558  842 VAL B C   
3931 O O   . VAL A 565 ? 0.99914 0.50307 0.88849 0.05156  0.11268  0.02856  842 VAL B O   
3932 C CB  . VAL A 565 ? 0.91453 0.51937 0.80817 0.08255  0.08420  0.05078  842 VAL B CB  
3933 C CG1 . VAL A 565 ? 0.83522 0.44614 0.72594 0.06284  0.08212  0.02597  842 VAL B CG1 
3934 C CG2 . VAL A 565 ? 0.83855 0.48670 0.73523 0.08564  0.07110  0.06436  842 VAL B CG2 
3935 N N   . GLN A 566 ? 0.93485 0.42661 0.82642 0.09477  0.11952  0.04872  843 GLN B N   
3936 C CA  . GLN A 566 ? 0.97766 0.42101 0.86775 0.09199  0.13505  0.03063  843 GLN B CA  
3937 C C   . GLN A 566 ? 1.05682 0.45558 0.94779 0.07520  0.14711  0.03315  843 GLN B C   
3938 O O   . GLN A 566 ? 1.05572 0.43215 0.94603 0.05348  0.15302  0.00870  843 GLN B O   
3939 C CB  . GLN A 566 ? 0.99979 0.42414 0.89272 0.12172  0.14487  0.03971  843 GLN B CB  
3940 C CG  . GLN A 566 ? 0.96044 0.33639 0.85129 0.12348  0.16191  0.01766  843 GLN B CG  
3941 C CD  . GLN A 566 ? 1.10830 0.47709 1.00790 0.15109  0.16932  0.03235  843 GLN B CD  
3942 O OE1 . GLN A 566 ? 1.15658 0.55273 1.05897 0.17203  0.16572  0.03665  843 GLN B OE1 
3943 N NE2 . GLN A 566 ? 1.11433 0.44996 1.01982 0.15062  0.17960  0.04074  843 GLN B NE2 
3944 N N   . ASP A 567 ? 1.04723 0.43515 0.93994 0.08415  0.15102  0.06275  844 ASP B N   
3945 C CA  . ASP A 567 ? 1.08314 0.43516 0.97883 0.06835  0.16263  0.06939  844 ASP B CA  
3946 C C   . ASP A 567 ? 1.10127 0.46153 0.99710 0.03542  0.15890  0.05168  844 ASP B C   
3947 O O   . ASP A 567 ? 1.10914 0.43331 1.00978 0.01510  0.17088  0.04061  844 ASP B O   
3948 C CB  . ASP A 567 ? 1.14102 0.50667 1.03744 0.08170  0.16071  0.10485  844 ASP B CB  
3949 C CG  . ASP A 567 ? 1.24328 0.60722 1.14389 0.11065  0.16386  0.12241  844 ASP B CG  
3950 O OD1 . ASP A 567 ? 1.18520 0.52368 1.09052 0.11707  0.17265  0.10846  844 ASP B OD1 
3951 O OD2 . ASP A 567 ? 1.23506 0.62531 1.13388 0.12673  0.15750  0.14946  844 ASP B OD2 
3952 N N   . LYS A 568 ? 1.02989 0.44585 0.92386 0.02905  0.14085  0.04901  845 LYS B N   
3953 C CA  . LYS A 568 ? 1.00656 0.44234 0.90356 0.00010  0.13523  0.03485  845 LYS B CA  
3954 C C   . LYS A 568 ? 1.02850 0.45180 0.92776 -0.01979 0.13808  0.00032  845 LYS B C   
3955 O O   . LYS A 568 ? 1.02193 0.44328 0.92722 -0.04623 0.14012  -0.01229 845 LYS B O   
3956 C CB  . LYS A 568 ? 1.00370 0.49963 0.89874 0.00103  0.11661  0.03813  845 LYS B CB  
3957 C CG  . LYS A 568 ? 1.00646 0.52075 0.89848 0.01466  0.11240  0.06759  845 LYS B CG  
3958 C CD  . LYS A 568 ? 0.99727 0.50351 0.89097 -0.00189 0.11889  0.07928  845 LYS B CD  
3959 C CE  . LYS A 568 ? 0.99359 0.51056 0.88055 0.01401  0.11803  0.10996  845 LYS B CE  
3960 N NZ  . LYS A 568 ? 1.05912 0.62857 0.94247 0.02195  0.10095  0.11149  845 LYS B NZ  
3961 N N   . PHE A 569 ? 1.04849 0.46740 0.94308 -0.00804 0.13803  -0.01620 846 PHE B N   
3962 C CA  . PHE A 569 ? 1.04911 0.45886 0.94258 -0.02604 0.14038  -0.05107 846 PHE B CA  
3963 C C   . PHE A 569 ? 1.15086 0.49812 1.04937 -0.03936 0.15999  -0.06201 846 PHE B C   
3964 O O   . PHE A 569 ? 1.13682 0.47685 1.03675 -0.06272 0.16204  -0.09284 846 PHE B O   
3965 C CB  . PHE A 569 ? 0.99631 0.41949 0.88120 -0.00819 0.13651  -0.06515 846 PHE B CB  
3966 C CG  . PHE A 569 ? 0.97257 0.45729 0.85384 -0.00275 0.11825  -0.06306 846 PHE B CG  
3967 C CD1 . PHE A 569 ? 0.94313 0.46667 0.82482 -0.02322 0.10646  -0.07640 846 PHE B CD1 
3968 C CD2 . PHE A 569 ? 0.97614 0.48015 0.85538 0.02309  0.11384  -0.04757 846 PHE B CD2 
3969 C CE1 . PHE A 569 ? 0.92571 0.50139 0.80477 -0.01653 0.09189  -0.07269 846 PHE B CE1 
3970 C CE2 . PHE A 569 ? 0.90764 0.46362 0.78537 0.02692  0.09933  -0.04555 846 PHE B CE2 
3971 C CZ  . PHE A 569 ? 0.91092 0.50036 0.78799 0.00774  0.08901  -0.05751 846 PHE B CZ  
3972 N N   . ARG A 570 ? 1.18491 0.48750 1.08657 -0.02546 0.17479  -0.03785 847 ARG B N   
3973 C CA  . ARG A 570 ? 1.19311 0.45472 1.10454 -0.03449 0.18877  -0.04413 847 ARG B CA  
3974 C C   . ARG A 570 ? 1.27140 0.51795 1.17973 -0.03805 0.19242  -0.07950 847 ARG B C   
3975 O O   . ARG A 570 ? 1.28974 0.52114 1.20400 -0.06275 0.19701  -0.10481 847 ARG B O   
3976 C CB  . ARG A 570 ? 1.25564 0.51415 1.17795 -0.06598 0.19169  -0.04617 847 ARG B CB  
3977 C CG  . ARG A 570 ? 1.20177 0.47480 1.12640 -0.06385 0.19016  -0.01148 847 ARG B CG  
3978 C CD  . ARG A 570 ? 1.19691 0.44978 1.12245 -0.03811 0.19829  0.02171  847 ARG B CD  
3979 N NE  . ARG A 570 ? 1.29246 0.50279 1.22581 -0.03875 0.21221  0.01352  847 ARG B NE  
3980 C CZ  . ARG A 570 ? 1.34504 0.52906 1.28895 -0.05321 0.22396  0.02063  847 ARG B CZ  
3981 N NH1 . ARG A 570 ? 1.33048 0.52818 1.27864 -0.06752 0.22384  0.03737  847 ARG B NH1 
3982 N NH2 . ARG A 570 ? 1.26883 0.41142 1.21926 -0.05327 0.23714  0.01061  847 ARG B NH2 
3983 N N   . LEU A 571 ? 1.28364 0.53822 1.18256 -0.01307 0.19004  -0.08175 848 LEU B N   
3984 C CA  . LEU A 571 ? 1.27254 0.51606 1.16575 -0.01232 0.19404  -0.11403 848 LEU B CA  
3985 C C   . LEU A 571 ? 1.36700 0.56575 1.26923 -0.01472 0.20866  -0.12071 848 LEU B C   
3986 O O   . LEU A 571 ? 1.32643 0.51291 1.22432 -0.01979 0.21275  -0.15168 848 LEU B O   
3987 C CB  . LEU A 571 ? 1.14371 0.40428 1.02757 0.01896  0.19119  -0.10810 848 LEU B CB  
3988 C CG  . LEU A 571 ? 1.15929 0.46882 1.03435 0.01816  0.17546  -0.10601 848 LEU B CG  
3989 C CD1 . LEU A 571 ? 1.09924 0.43655 0.97043 0.04929  0.17047  -0.09251 848 LEU B CD1 
3990 C CD2 . LEU A 571 ? 1.18828 0.52621 1.05644 -0.00741 0.16611  -0.14128 848 LEU B CD2 
3991 N N   . ASP A 572 ? 1.41766 0.59289 1.33108 -0.01239 0.21669  -0.09315 849 ASP B N   
3992 C CA  . ASP A 572 ? 1.47372 0.60149 1.39635 -0.01425 0.23269  -0.09620 849 ASP B CA  
3993 C C   . ASP A 572 ? 1.50240 0.61704 1.43205 -0.05176 0.23549  -0.12394 849 ASP B C   
3994 O O   . ASP A 572 ? 1.56995 0.64546 1.50563 -0.05790 0.24821  -0.13797 849 ASP B O   
3995 C CB  . ASP A 572 ? 1.50037 0.61040 1.43094 0.00329  0.24075  -0.05521 849 ASP B CB  
3996 C CG  . ASP A 572 ? 1.56603 0.69684 1.49982 -0.00873 0.23457  -0.03148 849 ASP B CG  
3997 O OD1 . ASP A 572 ? 1.46673 0.62525 1.39820 -0.03056 0.22421  -0.04627 849 ASP B OD1 
3998 O OD2 . ASP A 572 ? 1.60109 0.72198 1.53909 0.00433  0.24043  0.00167  849 ASP B OD2 
3999 N N   . LEU A 573 ? 1.43769 0.58509 1.36775 -0.07596 0.22426  -0.13173 850 LEU B N   
4000 C CA  . LEU A 573 ? 1.43365 0.57874 1.37334 -0.11265 0.22499  -0.15648 850 LEU B CA  
4001 C C   . LEU A 573 ? 1.37754 0.54478 1.30835 -0.12806 0.21610  -0.19990 850 LEU B C   
4002 O O   . LEU A 573 ? 1.35602 0.55720 1.27299 -0.11781 0.20469  -0.20699 850 LEU B O   
4003 C CB  . LEU A 573 ? 1.40874 0.58265 1.35591 -0.13080 0.21781  -0.14014 850 LEU B CB  
4004 C CG  . LEU A 573 ? 1.38778 0.55202 1.33968 -0.11505 0.22364  -0.09551 850 LEU B CG  
4005 C CD1 . LEU A 573 ? 1.29273 0.48701 1.25188 -0.13679 0.21741  -0.08518 850 LEU B CD1 
4006 C CD2 . LEU A 573 ? 1.39768 0.51180 1.35920 -0.10999 0.24157  -0.08243 850 LEU B CD2 
4007 N N   . SER A 574 ? 1.39582 0.54582 1.33394 -0.15277 0.22129  -0.22886 851 SER B N   
4008 C CA  . SER A 574 ? 1.36770 0.54906 1.29795 -0.17280 0.21024  -0.27050 851 SER B CA  
4009 C C   . SER A 574 ? 1.43191 0.66730 1.36476 -0.19386 0.19431  -0.27258 851 SER B C   
4010 O O   . SER A 574 ? 1.43615 0.67870 1.37849 -0.19587 0.19386  -0.24404 851 SER B O   
4011 C CB  . SER A 574 ? 1.46329 0.61705 1.40257 -0.19697 0.21864  -0.30043 851 SER B CB  
4012 O OG  . SER A 574 ? 1.47684 0.64176 1.43425 -0.22897 0.21712  -0.30159 851 SER B OG  
4013 N N   . ASP A 575 ? 1.42445 0.70158 1.34809 -0.20878 0.18088  -0.30639 852 ASP B N   
4014 C CA  . ASP A 575 ? 1.40000 0.73362 1.32754 -0.22944 0.16510  -0.31043 852 ASP B CA  
4015 C C   . ASP A 575 ? 1.40994 0.74184 1.36172 -0.25872 0.16859  -0.30595 852 ASP B C   
4016 O O   . ASP A 575 ? 1.33766 0.69158 1.29907 -0.26481 0.16467  -0.28395 852 ASP B O   
4017 C CB  . ASP A 575 ? 1.47832 0.86089 1.39185 -0.24007 0.14986  -0.34807 852 ASP B CB  
4018 C CG  . ASP A 575 ? 1.53340 0.93408 1.42277 -0.21220 0.14386  -0.34719 852 ASP B CG  
4019 O OD1 . ASP A 575 ? 1.51866 0.89861 1.40491 -0.18714 0.14994  -0.31676 852 ASP B OD1 
4020 O OD2 . ASP A 575 ? 1.65031 1.08770 1.52367 -0.21456 0.13338  -0.37563 852 ASP B OD2 
4021 N N   . GLU A 576 ? 1.50769 0.81315 1.46979 -0.27715 0.17694  -0.32686 853 GLU B N   
4022 C CA  . GLU A 576 ? 1.38795 0.68452 1.37461 -0.30394 0.18371  -0.32141 853 GLU B CA  
4023 C C   . GLU A 576 ? 1.37316 0.64226 1.36856 -0.29065 0.19480  -0.27708 853 GLU B C   
4024 O O   . GLU A 576 ? 1.36491 0.65993 1.37371 -0.30467 0.19157  -0.26118 853 GLU B O   
4025 C CB  . GLU A 576 ? 1.38327 0.63767 1.37761 -0.31840 0.19608  -0.34547 853 GLU B CB  
4026 N N   . GLU A 577 ? 1.37338 0.59422 1.36067 -0.26189 0.20747  -0.25579 854 GLU B N   
4027 C CA  . GLU A 577 ? 1.37121 0.56802 1.36427 -0.24620 0.21764  -0.21234 854 GLU B CA  
4028 C C   . GLU A 577 ? 1.43640 0.67336 1.42196 -0.23398 0.20597  -0.18867 854 GLU B C   
4029 O O   . GLU A 577 ? 1.43933 0.68170 1.43374 -0.23661 0.20881  -0.16018 854 GLU B O   
4030 C CB  . GLU A 577 ? 1.44586 0.58985 1.43148 -0.21604 0.23185  -0.19642 854 GLU B CB  
4031 C CG  . GLU A 577 ? 1.46407 0.56254 1.45727 -0.22748 0.24566  -0.21934 854 GLU B CG  
4032 C CD  . GLU A 577 ? 1.49118 0.54082 1.47731 -0.19608 0.25954  -0.20517 854 GLU B CD  
4033 O OE2 . GLU A 577 ? 1.59508 0.65570 1.56658 -0.16662 0.25413  -0.19323 854 GLU B OE2 
4034 N N   . ALA A 578 ? 1.43001 0.69547 1.39865 -0.22067 0.19351  -0.20010 855 ALA B N   
4035 C CA  . ALA A 578 ? 1.36344 0.66446 1.32455 -0.20975 0.18307  -0.17952 855 ALA B CA  
4036 C C   . ALA A 578 ? 1.34437 0.68820 1.31894 -0.23831 0.17486  -0.18191 855 ALA B C   
4037 O O   . ALA A 578 ? 1.33476 0.69416 1.31102 -0.23376 0.17330  -0.15440 855 ALA B O   
4038 C CB  . ALA A 578 ? 1.34364 0.66844 1.28481 -0.19388 0.17178  -0.19589 855 ALA B CB  
4039 N N   . VAL A 579 ? 1.32894 0.69610 1.31352 -0.26726 0.16918  -0.21455 856 VAL B N   
4040 C CA  . VAL A 579 ? 1.32499 0.74153 1.32515 -0.29416 0.16016  -0.21842 856 VAL B CA  
4041 C C   . VAL A 579 ? 1.38834 0.78583 1.40792 -0.30466 0.17295  -0.19219 856 VAL B C   
4042 O O   . VAL A 579 ? 1.38008 0.80840 1.40766 -0.31080 0.16987  -0.17346 856 VAL B O   
4043 C CB  . VAL A 579 ? 1.32941 0.78122 1.33586 -0.32058 0.14962  -0.25998 856 VAL B CB  
4044 C CG1 . VAL A 579 ? 1.25011 0.75239 1.27871 -0.34919 0.14227  -0.26246 856 VAL B CG1 
4045 C CG2 . VAL A 579 ? 1.22011 0.70502 1.20465 -0.30891 0.13461  -0.28216 856 VAL B CG2 
4046 N N   . HIS A 580 ? 1.36407 0.71132 1.39104 -0.30648 0.18824  -0.19014 857 HIS B N   
4047 C CA  . HIS A 580 ? 1.42398 0.74850 1.46660 -0.31275 0.20227  -0.16191 857 HIS B CA  
4048 C C   . HIS A 580 ? 1.41987 0.73853 1.45174 -0.28573 0.20552  -0.12006 857 HIS B C   
4049 O O   . HIS A 580 ? 1.41557 0.75331 1.45637 -0.29256 0.20763  -0.09736 857 HIS B O   
4050 C CB  . HIS A 580 ? 1.53203 0.79822 1.58100 -0.31470 0.21896  -0.16599 857 HIS B CB  
4051 C CG  . HIS A 580 ? 1.63479 0.87479 1.69896 -0.32109 0.23470  -0.13732 857 HIS B CG  
4052 N ND1 . HIS A 580 ? 1.73007 0.94400 1.78589 -0.29479 0.24425  -0.09700 857 HIS B ND1 
4053 C CD2 . HIS A 580 ? 1.69083 0.92925 1.77765 -0.35049 0.24250  -0.14268 857 HIS B CD2 
4054 C CE1 . HIS A 580 ? 1.71138 0.90816 1.78242 -0.30722 0.25760  -0.07823 857 HIS B CE1 
4055 N NE2 . HIS A 580 ? 1.74554 0.95506 1.83637 -0.34138 0.25744  -0.10517 857 HIS B NE2 
4056 N N   . TYR A 581 ? 1.40139 0.69750 1.41386 -0.25432 0.20563  -0.10970 858 TYR B N   
4057 C CA  . TYR A 581 ? 1.37764 0.67187 1.37846 -0.22666 0.20698  -0.07102 858 TYR B CA  
4058 C C   . TYR A 581 ? 1.39364 0.73884 1.39214 -0.23171 0.19498  -0.06395 858 TYR B C   
4059 O O   . TYR A 581 ? 1.40699 0.76242 1.40773 -0.22911 0.19858  -0.03487 858 TYR B O   
4060 C CB  . TYR A 581 ? 1.31586 0.58744 1.29832 -0.19355 0.20625  -0.06675 858 TYR B CB  
4061 C CG  . TYR A 581 ? 1.34686 0.63123 1.31501 -0.16455 0.20164  -0.03403 858 TYR B CG  
4062 C CD1 . TYR A 581 ? 1.30434 0.56919 1.27055 -0.14478 0.21053  0.00245  858 TYR B CD1 
4063 C CD2 . TYR A 581 ? 1.25457 0.57225 1.21032 -0.15658 0.18802  -0.04007 858 TYR B CD2 
4064 C CE1 . TYR A 581 ? 1.32230 0.60472 1.27493 -0.11831 0.20452  0.03080  858 TYR B CE1 
4065 C CE2 . TYR A 581 ? 1.29011 0.62013 1.23305 -0.13055 0.18342  -0.01132 858 TYR B CE2 
4066 C CZ  . TYR A 581 ? 1.29272 0.60726 1.23436 -0.11167 0.19094  0.02337  858 TYR B CZ  
4067 O OH  . TYR A 581 ? 1.25707 0.59049 1.18584 -0.08622 0.18444  0.05017  858 TYR B OH  
4068 N N   . MET A 582 ? 1.34624 0.72536 1.33935 -0.23874 0.18102  -0.09056 859 MET B N   
4069 C CA  . MET A 582 ? 1.28736 0.72765 1.27975 -0.24000 0.16564  -0.08445 859 MET B CA  
4070 C C   . MET A 582 ? 1.30182 0.76729 1.31558 -0.26973 0.16906  -0.08317 859 MET B C   
4071 O O   . MET A 582 ? 1.25761 0.76501 1.27248 -0.26379 0.16212  -0.06286 859 MET B O   
4072 C CB  . MET A 582 ? 1.11413 0.60111 1.09878 -0.23714 0.14566  -0.11199 859 MET B CB  
4073 C CG  . MET A 582 ? 1.12244 0.68093 1.10728 -0.23181 0.12687  -0.10438 859 MET B CG  
4074 S SD  . MET A 582 ? 1.11680 0.68467 1.08704 -0.19627 0.12286  -0.06488 859 MET B SD  
4075 C CE  . MET A 582 ? 1.01217 0.56543 0.96220 -0.16703 0.11679  -0.07092 859 MET B CE  
4076 N N   . GLN A 583 ? 1.34668 0.79783 1.37849 -0.29722 0.17664  -0.10378 860 GLN B N   
4077 C CA  . GLN A 583 ? 1.32417 0.80224 1.37932 -0.32322 0.18020  -0.09993 860 GLN B CA  
4078 C C   . GLN A 583 ? 1.34800 0.80288 1.40391 -0.31228 0.19457  -0.06000 860 GLN B C   
4079 O O   . GLN A 583 ? 1.31107 0.79974 1.37521 -0.31967 0.19515  -0.04369 860 GLN B O   
4080 C CB  . GLN A 583 ? 1.30603 0.77667 1.37994 -0.34991 0.18311  -0.12854 860 GLN B CB  
4081 N N   A SER A 584 ? 1.37091 0.77184 1.41767 -0.29326 0.20625  -0.04333 861 SER B N   
4082 N N   B SER A 584 ? 1.37027 0.77101 1.41736 -0.29369 0.20634  -0.04370 861 SER B N   
4083 C CA  A SER A 584 ? 1.36115 0.74333 1.40543 -0.28002 0.21872  -0.00417 861 SER B CA  
4084 C CA  B SER A 584 ? 1.36201 0.74369 1.40602 -0.27966 0.21867  -0.00428 861 SER B CA  
4085 C C   A SER A 584 ? 1.36755 0.77140 1.39265 -0.25533 0.21282  0.02219  861 SER B C   
4086 C C   B SER A 584 ? 1.36653 0.77332 1.39238 -0.25685 0.21224  0.02085  861 SER B C   
4087 O O   A SER A 584 ? 1.39791 0.81371 1.42244 -0.25176 0.21875  0.05048  861 SER B O   
4088 O O   B SER A 584 ? 1.39281 0.81662 1.41955 -0.25596 0.21727  0.04681  861 SER B O   
4089 C CB  A SER A 584 ? 1.39720 0.72074 1.43650 -0.26429 0.23151  0.00664  861 SER B CB  
4090 C CB  B SER A 584 ? 1.39834 0.72189 1.43525 -0.26111 0.23060  0.00741  861 SER B CB  
4091 O OG  A SER A 584 ? 1.44714 0.74758 1.50418 -0.28827 0.23881  -0.01739 861 SER B OG  
4092 O OG  B SER A 584 ? 1.41146 0.72314 1.42729 -0.23068 0.22447  0.01168  861 SER B OG  
4093 N N   . LEU A 585 ? 1.38321 0.79330 1.39171 -0.23812 0.20154  0.01318  862 LEU B N   
4094 C CA  . LEU A 585 ? 1.29854 0.73583 1.28936 -0.21445 0.19304  0.03543  862 LEU B CA  
4095 C C   . LEU A 585 ? 1.26146 0.76151 1.26090 -0.22625 0.18320  0.03642  862 LEU B C   
4096 O O   . LEU A 585 ? 1.28619 0.80719 1.27700 -0.21240 0.18269  0.06223  862 LEU B O   
4097 C CB  . LEU A 585 ? 1.30016 0.75114 1.27603 -0.19188 0.17605  0.02151  862 LEU B CB  
4098 C CG  . LEU A 585 ? 1.26788 0.72539 1.22403 -0.15693 0.16963  0.04757  862 LEU B CG  
4099 C CD1 . LEU A 585 ? 1.32783 0.72924 1.27810 -0.14350 0.18825  0.07440  862 LEU B CD1 
4100 C CD2 . LEU A 585 ? 1.22895 0.69909 1.17522 -0.13970 0.15508  0.03057  862 LEU B CD2 
4101 N N   . ILE A 586 ? 1.23743 0.77024 1.25380 -0.25103 0.17547  0.00797  863 ILE B N   
4102 C CA  . ILE A 586 ? 1.20788 0.80311 1.23581 -0.26168 0.16658  0.00750  863 ILE B CA  
4103 C C   . ILE A 586 ? 1.29826 0.88751 1.34273 -0.28238 0.18464  0.02399  863 ILE B C   
4104 O O   . ILE A 586 ? 1.24531 0.86681 1.28800 -0.27563 0.18493  0.04434  863 ILE B O   
4105 C CB  . ILE A 586 ? 1.14283 0.77920 1.18418 -0.27972 0.15192  -0.02715 863 ILE B CB  
4106 C CG1 . ILE A 586 ? 1.09234 0.73902 1.11533 -0.25694 0.13492  -0.03975 863 ILE B CG1 
4107 C CG2 . ILE A 586 ? 1.05431 0.75544 1.11222 -0.29150 0.14489  -0.02684 863 ILE B CG2 
4108 C CD1 . ILE A 586 ? 0.97808 0.66458 1.00997 -0.27157 0.12082  -0.07164 863 ILE B CD1 
4109 N N   . ASP A 587 ? 1.30568 0.85382 1.36714 -0.30879 0.20104  0.01432  864 ASP B N   
4110 C CA  . ASP A 587 ? 1.31847 0.86898 1.39767 -0.32384 0.21439  0.03060  864 ASP B CA  
4111 C C   . ASP A 587 ? 1.34243 0.87054 1.40401 -0.29985 0.22548  0.07060  864 ASP B C   
4112 O O   . ASP A 587 ? 1.37969 0.93369 1.44586 -0.30351 0.23227  0.09062  864 ASP B O   
4113 C CB  . ASP A 587 ? 1.34056 0.85941 1.43847 -0.34409 0.22142  0.01334  864 ASP B CB  
4114 C CG  . ASP A 587 ? 1.36796 0.91808 1.48450 -0.37041 0.20953  -0.02753 864 ASP B CG  
4115 O OD1 . ASP A 587 ? 1.24007 0.84477 1.36010 -0.37627 0.19632  -0.04026 864 ASP B OD1 
4116 O OD2 . ASP A 587 ? 1.49249 1.01412 1.61975 -0.38475 0.21337  -0.04685 864 ASP B OD2 
4117 N N   . GLU A 588 ? 1.42177 0.90605 1.46301 -0.27421 0.22702  0.08258  865 GLU B N   
4118 C CA  . GLU A 588 ? 1.45089 0.92036 1.47343 -0.24893 0.23468  0.12018  865 GLU B CA  
4119 C C   . GLU A 588 ? 1.38771 0.89844 1.39383 -0.23457 0.22817  0.13551  865 GLU B C   
4120 O O   . GLU A 588 ? 1.40845 0.93451 1.40828 -0.22860 0.23524  0.16162  865 GLU B O   
4121 C CB  . GLU A 588 ? 1.50624 0.92943 1.51229 -0.22288 0.23492  0.12711  865 GLU B CB  
4122 C CG  . GLU A 588 ? 1.57581 0.99343 1.55888 -0.19166 0.23751  0.16385  865 GLU B CG  
4123 C CD  . GLU A 588 ? 1.60784 1.03757 1.56890 -0.16433 0.22398  0.16622  865 GLU B CD  
4124 O OE1 . GLU A 588 ? 1.68313 1.12641 1.64558 -0.16999 0.21362  0.14154  865 GLU B OE1 
4125 O OE2 . GLU A 588 ? 1.62730 1.05515 1.56966 -0.13729 0.22327  0.19262  865 GLU B OE2 
4126 N N   . SER A 589 ? 1.37782 0.91410 1.37609 -0.22622 0.21143  0.11778  866 SER B N   
4127 C CA  . SER A 589 ? 1.31100 0.90216 1.29710 -0.20934 0.19710  0.12523  866 SER B CA  
4128 C C   . SER A 589 ? 1.27123 0.90720 1.27490 -0.22982 0.20056  0.12397  866 SER B C   
4129 O O   . SER A 589 ? 1.22975 0.89312 1.22372 -0.21955 0.20253  0.14319  866 SER B O   
4130 C CB  . SER A 589 ? 1.33770 0.95579 1.31737 -0.19577 0.17439  0.10279  866 SER B CB  
4131 O OG  . SER A 589 ? 1.28318 0.86373 1.24807 -0.17610 0.17183  0.10412  866 SER B OG  
4132 N N   . VAL A 590 ? 1.28930 0.93660 1.31920 -0.25868 0.20125  0.10037  867 VAL B N   
4133 C CA  . VAL A 590 ? 1.20954 0.90285 1.26075 -0.27922 0.20537  0.09893  867 VAL B CA  
4134 C C   . VAL A 590 ? 1.28855 0.95962 1.34369 -0.28920 0.22968  0.12662  867 VAL B C   
4135 O O   . VAL A 590 ? 1.28339 0.98939 1.33660 -0.28539 0.23434  0.14327  867 VAL B O   
4136 C CB  . VAL A 590 ? 1.18988 0.90319 1.27007 -0.30906 0.19997  0.06669  867 VAL B CB  
4137 N N   . HIS A 591 ? 1.32874 0.94805 1.38881 -0.29651 0.24118  0.13108  868 HIS B N   
4138 C CA  . HIS A 591 ? 1.38283 0.98875 1.44650 -0.29889 0.25689  0.15766  868 HIS B CA  
4139 C C   . HIS A 591 ? 1.30928 0.92481 1.34390 -0.27139 0.26005  0.18993  868 HIS B C   
4140 O O   . HIS A 591 ? 1.37114 1.00838 1.40772 -0.27512 0.27046  0.20949  868 HIS B O   
4141 C CB  . HIS A 591 ? 1.35057 0.89804 1.41705 -0.30027 0.26413  0.15885  868 HIS B CB  
4142 N N   . ALA A 592 ? 1.31544 0.91829 1.32345 -0.24449 0.25082  0.19445  869 ALA B N   
4143 C CA  . ALA A 592 ? 1.35698 0.97185 1.33545 -0.21709 0.25094  0.22205  869 ALA B CA  
4144 C C   . ALA A 592 ? 1.32651 0.99700 1.29998 -0.21483 0.24621  0.22007  869 ALA B C   
4145 O O   . ALA A 592 ? 1.32199 1.00986 1.27276 -0.19623 0.24843  0.24172  869 ALA B O   
4146 C CB  . ALA A 592 ? 1.38917 0.97740 1.34348 -0.18879 0.24059  0.22583  869 ALA B CB  
4147 N N   . LEU A 593 ? 1.31523 1.02310 1.30869 -0.22827 0.23327  0.19146  870 LEU B N   
4148 C CA  . LEU A 593 ? 1.26679 1.03409 1.25720 -0.21930 0.22153  0.18493  870 LEU B CA  
4149 C C   . LEU A 593 ? 1.28213 1.08121 1.28854 -0.23649 0.23743  0.19477  870 LEU B C   
4150 O O   . LEU A 593 ? 1.32590 1.10889 1.32377 -0.23707 0.25640  0.22134  870 LEU B O   
4151 C CB  . LEU A 593 ? 1.20888 1.00469 1.21303 -0.22201 0.20087  0.15318  870 LEU B CB  
4152 C CG  . LEU A 593 ? 1.06217 0.85443 1.04572 -0.19652 0.18133  0.14446  870 LEU B CG  
# 
