data_9N48
# 
_entry.id   9N48 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9N48         pdb_00009n48 10.2210/pdb9n48/pdb 
WWPDB D_1000292120 ?            ?                   
# 
_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       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9N48 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-02 
_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           N 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              hsu.peter@gene.com 
_pdbx_contact_author.name_first         Peter 
_pdbx_contact_author.name_last          Hsu 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9381-6564 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, W.'     1 ?                   
'Oh, A.'       2 ?                   
'Kiefer, J.R.' 3 0000-0001-6317-0902 
'Hsu, P.L.'    4 0000-0002-9381-6564 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Chem.Inf.Model. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1549-960X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Integrating Hydrogen Exchange with Molecular Dynamics for Improved Ligand Binding Predictions.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jcim.5c00397 
_citation.pdbx_database_id_PubMed   40495786 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Walters, B.T.'  1 ? 
primary 'Patapoff, A.W.' 2 ? 
primary 'Kiefer, J.R.'   3 ? 
primary 'Wu, P.'         4 ? 
primary 'Wang, W.'       5 ? 
# 
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 'Glutathione S-transferase class-mu 26 kDa isozyme,Serine/threonine-protein kinase PAK 1' 61334.492 2   
2.5.1.18,2.7.11.1 ? ? ? 
2 non-polymer syn 
'(6M)-8-[2-(2-aminoethoxy)ethyl]-6-[2-chloro-3-fluoro-4-(2-oxopyrrolidin-1-yl)phenyl]-2-(ethylamino)pyrido[2,3-d]pyrimidin-7(8H)-one' 
488.942   2   ?                 ? ? ? 
3 water       nat water 18.015    388 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'GST 26,Sj26 antigen,SjGST,Alpha-PAK,p21-activated kinase 1,PAK-1,p65-PAK' 
# 
_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       
;MHHHHHHHHGSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAI
IRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFKDRLCHKTYLNGDHVTHP
DFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDGENLYFQGSDE
EILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYL
DSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRNIKSDNILLGMDGSVKLTDFGFC
AQITPEQSKRSEMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLS
AIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNHGNS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHHHGSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAI
IRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFKDRLCHKTYLNGDHVTHP
DFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDGENLYFQGSDE
EILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYL
DSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRNIKSDNILLGMDGSVKLTDFGFC
AQITPEQSKRSEMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLS
AIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNHGNS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
'(6M)-8-[2-(2-aminoethoxy)ethyl]-6-[2-chloro-3-fluoro-4-(2-oxopyrrolidin-1-yl)phenyl]-2-(ethylamino)pyrido[2,3-d]pyrimidin-7(8H)-one' 
A1BV1 
3 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   HIS 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  GLY n 
1 11  SER n 
1 12  PRO n 
1 13  ILE n 
1 14  LEU n 
1 15  GLY n 
1 16  TYR n 
1 17  TRP n 
1 18  LYS n 
1 19  ILE n 
1 20  LYS n 
1 21  GLY n 
1 22  LEU n 
1 23  VAL n 
1 24  GLN n 
1 25  PRO n 
1 26  THR n 
1 27  ARG n 
1 28  LEU n 
1 29  LEU n 
1 30  LEU n 
1 31  GLU n 
1 32  TYR n 
1 33  LEU n 
1 34  GLU n 
1 35  GLU n 
1 36  LYS n 
1 37  TYR n 
1 38  GLU n 
1 39  GLU n 
1 40  HIS n 
1 41  LEU n 
1 42  TYR n 
1 43  GLU n 
1 44  ARG n 
1 45  ASP n 
1 46  GLU n 
1 47  GLY n 
1 48  ASP n 
1 49  LYS n 
1 50  TRP n 
1 51  ARG n 
1 52  ASN n 
1 53  LYS n 
1 54  LYS n 
1 55  PHE n 
1 56  GLU n 
1 57  LEU n 
1 58  GLY n 
1 59  LEU n 
1 60  GLU n 
1 61  PHE n 
1 62  PRO n 
1 63  ASN n 
1 64  LEU n 
1 65  PRO n 
1 66  TYR n 
1 67  TYR n 
1 68  ILE n 
1 69  ASP n 
1 70  GLY n 
1 71  ASP n 
1 72  VAL n 
1 73  LYS n 
1 74  LEU n 
1 75  THR n 
1 76  GLN n 
1 77  SER n 
1 78  MET n 
1 79  ALA n 
1 80  ILE n 
1 81  ILE n 
1 82  ARG n 
1 83  TYR n 
1 84  ILE n 
1 85  ALA n 
1 86  ASP n 
1 87  LYS n 
1 88  HIS n 
1 89  ASN n 
1 90  MET n 
1 91  LEU n 
1 92  GLY n 
1 93  GLY n 
1 94  CYS n 
1 95  PRO n 
1 96  LYS n 
1 97  GLU n 
1 98  ARG n 
1 99  ALA n 
1 100 GLU n 
1 101 ILE n 
1 102 SER n 
1 103 MET n 
1 104 LEU n 
1 105 GLU n 
1 106 GLY n 
1 107 ALA n 
1 108 VAL n 
1 109 LEU n 
1 110 ASP n 
1 111 ILE n 
1 112 ARG n 
1 113 TYR n 
1 114 GLY n 
1 115 VAL n 
1 116 SER n 
1 117 ARG n 
1 118 ILE n 
1 119 ALA n 
1 120 TYR n 
1 121 SER n 
1 122 LYS n 
1 123 ASP n 
1 124 PHE n 
1 125 GLU n 
1 126 THR n 
1 127 LEU n 
1 128 LYS n 
1 129 VAL n 
1 130 ASP n 
1 131 PHE n 
1 132 LEU n 
1 133 SER n 
1 134 LYS n 
1 135 LEU n 
1 136 PRO n 
1 137 GLU n 
1 138 MET n 
1 139 LEU n 
1 140 LYS n 
1 141 MET n 
1 142 PHE n 
1 143 LYS n 
1 144 ASP n 
1 145 ARG n 
1 146 LEU n 
1 147 CYS n 
1 148 HIS n 
1 149 LYS n 
1 150 THR n 
1 151 TYR n 
1 152 LEU n 
1 153 ASN n 
1 154 GLY n 
1 155 ASP n 
1 156 HIS n 
1 157 VAL n 
1 158 THR n 
1 159 HIS n 
1 160 PRO n 
1 161 ASP n 
1 162 PHE n 
1 163 MET n 
1 164 LEU n 
1 165 TYR n 
1 166 ASP n 
1 167 ALA n 
1 168 LEU n 
1 169 ASP n 
1 170 VAL n 
1 171 VAL n 
1 172 LEU n 
1 173 TYR n 
1 174 MET n 
1 175 ASP n 
1 176 PRO n 
1 177 MET n 
1 178 CYS n 
1 179 LEU n 
1 180 ASP n 
1 181 ALA n 
1 182 PHE n 
1 183 PRO n 
1 184 LYS n 
1 185 LEU n 
1 186 VAL n 
1 187 CYS n 
1 188 PHE n 
1 189 LYS n 
1 190 LYS n 
1 191 ARG n 
1 192 ILE n 
1 193 GLU n 
1 194 ALA n 
1 195 ILE n 
1 196 PRO n 
1 197 GLN n 
1 198 ILE n 
1 199 ASP n 
1 200 LYS n 
1 201 TYR n 
1 202 LEU n 
1 203 LYS n 
1 204 SER n 
1 205 SER n 
1 206 LYS n 
1 207 TYR n 
1 208 ILE n 
1 209 ALA n 
1 210 TRP n 
1 211 PRO n 
1 212 LEU n 
1 213 GLN n 
1 214 GLY n 
1 215 TRP n 
1 216 GLN n 
1 217 ALA n 
1 218 THR n 
1 219 PHE n 
1 220 GLY n 
1 221 GLY n 
1 222 GLY n 
1 223 ASP n 
1 224 HIS n 
1 225 PRO n 
1 226 PRO n 
1 227 LYS n 
1 228 SER n 
1 229 ASP n 
1 230 GLY n 
1 231 GLU n 
1 232 ASN n 
1 233 LEU n 
1 234 TYR n 
1 235 PHE n 
1 236 GLN n 
1 237 GLY n 
1 238 SER n 
1 239 ASP n 
1 240 GLU n 
1 241 GLU n 
1 242 ILE n 
1 243 LEU n 
1 244 GLU n 
1 245 LYS n 
1 246 LEU n 
1 247 ARG n 
1 248 SER n 
1 249 ILE n 
1 250 VAL n 
1 251 SER n 
1 252 VAL n 
1 253 GLY n 
1 254 ASP n 
1 255 PRO n 
1 256 LYS n 
1 257 LYS n 
1 258 LYS n 
1 259 TYR n 
1 260 THR n 
1 261 ARG n 
1 262 PHE n 
1 263 GLU n 
1 264 LYS n 
1 265 ILE n 
1 266 GLY n 
1 267 GLN n 
1 268 GLY n 
1 269 ALA n 
1 270 SER n 
1 271 GLY n 
1 272 THR n 
1 273 VAL n 
1 274 TYR n 
1 275 THR n 
1 276 ALA n 
1 277 MET n 
1 278 ASP n 
1 279 VAL n 
1 280 ALA n 
1 281 THR n 
1 282 GLY n 
1 283 GLN n 
1 284 GLU n 
1 285 VAL n 
1 286 ALA n 
1 287 ILE n 
1 288 LYS n 
1 289 GLN n 
1 290 MET n 
1 291 ASN n 
1 292 LEU n 
1 293 GLN n 
1 294 GLN n 
1 295 GLN n 
1 296 PRO n 
1 297 LYS n 
1 298 LYS n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 ILE n 
1 303 ASN n 
1 304 GLU n 
1 305 ILE n 
1 306 LEU n 
1 307 VAL n 
1 308 MET n 
1 309 ARG n 
1 310 GLU n 
1 311 ASN n 
1 312 LYS n 
1 313 ASN n 
1 314 PRO n 
1 315 ASN n 
1 316 ILE n 
1 317 VAL n 
1 318 ASN n 
1 319 TYR n 
1 320 LEU n 
1 321 ASP n 
1 322 SER n 
1 323 TYR n 
1 324 LEU n 
1 325 VAL n 
1 326 GLY n 
1 327 ASP n 
1 328 GLU n 
1 329 LEU n 
1 330 TRP n 
1 331 VAL n 
1 332 VAL n 
1 333 MET n 
1 334 GLU n 
1 335 TYR n 
1 336 LEU n 
1 337 ALA n 
1 338 GLY n 
1 339 GLY n 
1 340 SER n 
1 341 LEU n 
1 342 THR n 
1 343 ASP n 
1 344 VAL n 
1 345 VAL n 
1 346 THR n 
1 347 GLU n 
1 348 THR n 
1 349 CYS n 
1 350 MET n 
1 351 ASP n 
1 352 GLU n 
1 353 GLY n 
1 354 GLN n 
1 355 ILE n 
1 356 ALA n 
1 357 ALA n 
1 358 VAL n 
1 359 CYS n 
1 360 ARG n 
1 361 GLU n 
1 362 CYS n 
1 363 LEU n 
1 364 GLN n 
1 365 ALA n 
1 366 LEU n 
1 367 GLU n 
1 368 PHE n 
1 369 LEU n 
1 370 HIS n 
1 371 SER n 
1 372 ASN n 
1 373 GLN n 
1 374 VAL n 
1 375 ILE n 
1 376 HIS n 
1 377 ARG n 
1 378 ASN n 
1 379 ILE n 
1 380 LYS n 
1 381 SER n 
1 382 ASP n 
1 383 ASN n 
1 384 ILE n 
1 385 LEU n 
1 386 LEU n 
1 387 GLY n 
1 388 MET n 
1 389 ASP n 
1 390 GLY n 
1 391 SER n 
1 392 VAL n 
1 393 LYS n 
1 394 LEU n 
1 395 THR n 
1 396 ASP n 
1 397 PHE n 
1 398 GLY n 
1 399 PHE n 
1 400 CYS n 
1 401 ALA n 
1 402 GLN n 
1 403 ILE n 
1 404 THR n 
1 405 PRO n 
1 406 GLU n 
1 407 GLN n 
1 408 SER n 
1 409 LYS n 
1 410 ARG n 
1 411 SER n 
1 412 GLU n 
1 413 MET n 
1 414 VAL n 
1 415 GLY n 
1 416 THR n 
1 417 PRO n 
1 418 TYR n 
1 419 TRP n 
1 420 MET n 
1 421 ALA n 
1 422 PRO n 
1 423 GLU n 
1 424 VAL n 
1 425 VAL n 
1 426 THR n 
1 427 ARG n 
1 428 LYS n 
1 429 ALA n 
1 430 TYR n 
1 431 GLY n 
1 432 PRO n 
1 433 LYS n 
1 434 VAL n 
1 435 ASP n 
1 436 ILE n 
1 437 TRP n 
1 438 SER n 
1 439 LEU n 
1 440 GLY n 
1 441 ILE n 
1 442 MET n 
1 443 ALA n 
1 444 ILE n 
1 445 GLU n 
1 446 MET n 
1 447 ILE n 
1 448 GLU n 
1 449 GLY n 
1 450 GLU n 
1 451 PRO n 
1 452 PRO n 
1 453 TYR n 
1 454 LEU n 
1 455 ASN n 
1 456 GLU n 
1 457 ASN n 
1 458 PRO n 
1 459 LEU n 
1 460 ARG n 
1 461 ALA n 
1 462 LEU n 
1 463 TYR n 
1 464 LEU n 
1 465 ILE n 
1 466 ALA n 
1 467 THR n 
1 468 ASN n 
1 469 GLY n 
1 470 THR n 
1 471 PRO n 
1 472 GLU n 
1 473 LEU n 
1 474 GLN n 
1 475 ASN n 
1 476 PRO n 
1 477 GLU n 
1 478 LYS n 
1 479 LEU n 
1 480 SER n 
1 481 ALA n 
1 482 ILE n 
1 483 PHE n 
1 484 ARG n 
1 485 ASP n 
1 486 PHE n 
1 487 LEU n 
1 488 ASN n 
1 489 ARG n 
1 490 CYS n 
1 491 LEU n 
1 492 GLU n 
1 493 MET n 
1 494 ASP n 
1 495 VAL n 
1 496 GLU n 
1 497 LYS n 
1 498 ARG n 
1 499 GLY n 
1 500 SER n 
1 501 ALA n 
1 502 LYS n 
1 503 GLU n 
1 504 LEU n 
1 505 LEU n 
1 506 GLN n 
1 507 HIS n 
1 508 GLN n 
1 509 PHE n 
1 510 LEU n 
1 511 LYS n 
1 512 ILE n 
1 513 ALA n 
1 514 LYS n 
1 515 PRO n 
1 516 LEU n 
1 517 SER n 
1 518 SER n 
1 519 LEU n 
1 520 THR n 
1 521 PRO n 
1 522 LEU n 
1 523 ILE n 
1 524 ALA n 
1 525 ALA n 
1 526 ALA n 
1 527 LYS n 
1 528 GLU n 
1 529 ALA n 
1 530 THR n 
1 531 LYS n 
1 532 ASN n 
1 533 ASN n 
1 534 HIS n 
1 535 GLY n 
1 536 ASN n 
1 537 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_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 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   237 human ? ?    ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 238 537 human ? PAK1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BV1 non-polymer         . 
'(6M)-8-[2-(2-aminoethoxy)ethyl]-6-[2-chloro-3-fluoro-4-(2-oxopyrrolidin-1-yl)phenyl]-2-(ethylamino)pyrido[2,3-d]pyrimidin-7(8H)-one' 
? 'C23 H26 Cl F N6 O3' 488.942 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ? 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'      149.211 
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   12  ?   ?   ?   A . n 
A 1 2   HIS 2   13  ?   ?   ?   A . n 
A 1 3   HIS 3   14  ?   ?   ?   A . n 
A 1 4   HIS 4   15  ?   ?   ?   A . n 
A 1 5   HIS 5   16  ?   ?   ?   A . n 
A 1 6   HIS 6   17  ?   ?   ?   A . n 
A 1 7   HIS 7   18  ?   ?   ?   A . n 
A 1 8   HIS 8   19  ?   ?   ?   A . n 
A 1 9   HIS 9   20  ?   ?   ?   A . n 
A 1 10  GLY 10  21  ?   ?   ?   A . n 
A 1 11  SER 11  22  ?   ?   ?   A . n 
A 1 12  PRO 12  23  ?   ?   ?   A . n 
A 1 13  ILE 13  24  ?   ?   ?   A . n 
A 1 14  LEU 14  25  ?   ?   ?   A . n 
A 1 15  GLY 15  26  ?   ?   ?   A . n 
A 1 16  TYR 16  27  ?   ?   ?   A . n 
A 1 17  TRP 17  28  ?   ?   ?   A . n 
A 1 18  LYS 18  29  ?   ?   ?   A . n 
A 1 19  ILE 19  30  ?   ?   ?   A . n 
A 1 20  LYS 20  31  ?   ?   ?   A . n 
A 1 21  GLY 21  32  ?   ?   ?   A . n 
A 1 22  LEU 22  33  ?   ?   ?   A . n 
A 1 23  VAL 23  34  ?   ?   ?   A . n 
A 1 24  GLN 24  35  ?   ?   ?   A . n 
A 1 25  PRO 25  36  ?   ?   ?   A . n 
A 1 26  THR 26  37  ?   ?   ?   A . n 
A 1 27  ARG 27  38  ?   ?   ?   A . n 
A 1 28  LEU 28  39  ?   ?   ?   A . n 
A 1 29  LEU 29  40  ?   ?   ?   A . n 
A 1 30  LEU 30  41  ?   ?   ?   A . n 
A 1 31  GLU 31  42  ?   ?   ?   A . n 
A 1 32  TYR 32  43  ?   ?   ?   A . n 
A 1 33  LEU 33  44  ?   ?   ?   A . n 
A 1 34  GLU 34  45  ?   ?   ?   A . n 
A 1 35  GLU 35  46  ?   ?   ?   A . n 
A 1 36  LYS 36  47  ?   ?   ?   A . n 
A 1 37  TYR 37  48  ?   ?   ?   A . n 
A 1 38  GLU 38  49  ?   ?   ?   A . n 
A 1 39  GLU 39  50  ?   ?   ?   A . n 
A 1 40  HIS 40  51  ?   ?   ?   A . n 
A 1 41  LEU 41  52  ?   ?   ?   A . n 
A 1 42  TYR 42  53  ?   ?   ?   A . n 
A 1 43  GLU 43  54  ?   ?   ?   A . n 
A 1 44  ARG 44  55  ?   ?   ?   A . n 
A 1 45  ASP 45  56  ?   ?   ?   A . n 
A 1 46  GLU 46  57  ?   ?   ?   A . n 
A 1 47  GLY 47  58  ?   ?   ?   A . n 
A 1 48  ASP 48  59  ?   ?   ?   A . n 
A 1 49  LYS 49  60  ?   ?   ?   A . n 
A 1 50  TRP 50  61  ?   ?   ?   A . n 
A 1 51  ARG 51  62  ?   ?   ?   A . n 
A 1 52  ASN 52  63  ?   ?   ?   A . n 
A 1 53  LYS 53  64  ?   ?   ?   A . n 
A 1 54  LYS 54  65  ?   ?   ?   A . n 
A 1 55  PHE 55  66  ?   ?   ?   A . n 
A 1 56  GLU 56  67  ?   ?   ?   A . n 
A 1 57  LEU 57  68  ?   ?   ?   A . n 
A 1 58  GLY 58  69  ?   ?   ?   A . n 
A 1 59  LEU 59  70  ?   ?   ?   A . n 
A 1 60  GLU 60  71  ?   ?   ?   A . n 
A 1 61  PHE 61  72  ?   ?   ?   A . n 
A 1 62  PRO 62  73  ?   ?   ?   A . n 
A 1 63  ASN 63  74  ?   ?   ?   A . n 
A 1 64  LEU 64  75  ?   ?   ?   A . n 
A 1 65  PRO 65  76  ?   ?   ?   A . n 
A 1 66  TYR 66  77  ?   ?   ?   A . n 
A 1 67  TYR 67  78  ?   ?   ?   A . n 
A 1 68  ILE 68  79  ?   ?   ?   A . n 
A 1 69  ASP 69  80  ?   ?   ?   A . n 
A 1 70  GLY 70  81  ?   ?   ?   A . n 
A 1 71  ASP 71  82  ?   ?   ?   A . n 
A 1 72  VAL 72  83  ?   ?   ?   A . n 
A 1 73  LYS 73  84  ?   ?   ?   A . n 
A 1 74  LEU 74  85  ?   ?   ?   A . n 
A 1 75  THR 75  86  ?   ?   ?   A . n 
A 1 76  GLN 76  87  ?   ?   ?   A . n 
A 1 77  SER 77  88  ?   ?   ?   A . n 
A 1 78  MET 78  89  ?   ?   ?   A . n 
A 1 79  ALA 79  90  ?   ?   ?   A . n 
A 1 80  ILE 80  91  ?   ?   ?   A . n 
A 1 81  ILE 81  92  ?   ?   ?   A . n 
A 1 82  ARG 82  93  ?   ?   ?   A . n 
A 1 83  TYR 83  94  ?   ?   ?   A . n 
A 1 84  ILE 84  95  ?   ?   ?   A . n 
A 1 85  ALA 85  96  ?   ?   ?   A . n 
A 1 86  ASP 86  97  ?   ?   ?   A . n 
A 1 87  LYS 87  98  ?   ?   ?   A . n 
A 1 88  HIS 88  99  ?   ?   ?   A . n 
A 1 89  ASN 89  100 ?   ?   ?   A . n 
A 1 90  MET 90  101 ?   ?   ?   A . n 
A 1 91  LEU 91  102 ?   ?   ?   A . n 
A 1 92  GLY 92  103 ?   ?   ?   A . n 
A 1 93  GLY 93  104 ?   ?   ?   A . n 
A 1 94  CYS 94  105 ?   ?   ?   A . n 
A 1 95  PRO 95  106 ?   ?   ?   A . n 
A 1 96  LYS 96  107 ?   ?   ?   A . n 
A 1 97  GLU 97  108 ?   ?   ?   A . n 
A 1 98  ARG 98  109 ?   ?   ?   A . n 
A 1 99  ALA 99  110 ?   ?   ?   A . n 
A 1 100 GLU 100 111 ?   ?   ?   A . n 
A 1 101 ILE 101 112 ?   ?   ?   A . n 
A 1 102 SER 102 113 ?   ?   ?   A . n 
A 1 103 MET 103 114 ?   ?   ?   A . n 
A 1 104 LEU 104 115 ?   ?   ?   A . n 
A 1 105 GLU 105 116 ?   ?   ?   A . n 
A 1 106 GLY 106 117 ?   ?   ?   A . n 
A 1 107 ALA 107 118 ?   ?   ?   A . n 
A 1 108 VAL 108 119 ?   ?   ?   A . n 
A 1 109 LEU 109 120 ?   ?   ?   A . n 
A 1 110 ASP 110 121 ?   ?   ?   A . n 
A 1 111 ILE 111 122 ?   ?   ?   A . n 
A 1 112 ARG 112 123 ?   ?   ?   A . n 
A 1 113 TYR 113 124 ?   ?   ?   A . n 
A 1 114 GLY 114 125 ?   ?   ?   A . n 
A 1 115 VAL 115 126 ?   ?   ?   A . n 
A 1 116 SER 116 127 ?   ?   ?   A . n 
A 1 117 ARG 117 128 ?   ?   ?   A . n 
A 1 118 ILE 118 129 ?   ?   ?   A . n 
A 1 119 ALA 119 130 ?   ?   ?   A . n 
A 1 120 TYR 120 131 ?   ?   ?   A . n 
A 1 121 SER 121 132 ?   ?   ?   A . n 
A 1 122 LYS 122 133 ?   ?   ?   A . n 
A 1 123 ASP 123 134 ?   ?   ?   A . n 
A 1 124 PHE 124 135 ?   ?   ?   A . n 
A 1 125 GLU 125 136 ?   ?   ?   A . n 
A 1 126 THR 126 137 ?   ?   ?   A . n 
A 1 127 LEU 127 138 ?   ?   ?   A . n 
A 1 128 LYS 128 139 ?   ?   ?   A . n 
A 1 129 VAL 129 140 ?   ?   ?   A . n 
A 1 130 ASP 130 141 ?   ?   ?   A . n 
A 1 131 PHE 131 142 ?   ?   ?   A . n 
A 1 132 LEU 132 143 ?   ?   ?   A . n 
A 1 133 SER 133 144 ?   ?   ?   A . n 
A 1 134 LYS 134 145 ?   ?   ?   A . n 
A 1 135 LEU 135 146 ?   ?   ?   A . n 
A 1 136 PRO 136 147 ?   ?   ?   A . n 
A 1 137 GLU 137 148 ?   ?   ?   A . n 
A 1 138 MET 138 149 ?   ?   ?   A . n 
A 1 139 LEU 139 150 ?   ?   ?   A . n 
A 1 140 LYS 140 151 ?   ?   ?   A . n 
A 1 141 MET 141 152 ?   ?   ?   A . n 
A 1 142 PHE 142 153 ?   ?   ?   A . n 
A 1 143 LYS 143 154 ?   ?   ?   A . n 
A 1 144 ASP 144 155 ?   ?   ?   A . n 
A 1 145 ARG 145 156 ?   ?   ?   A . n 
A 1 146 LEU 146 157 ?   ?   ?   A . n 
A 1 147 CYS 147 158 ?   ?   ?   A . n 
A 1 148 HIS 148 159 ?   ?   ?   A . n 
A 1 149 LYS 149 160 ?   ?   ?   A . n 
A 1 150 THR 150 161 ?   ?   ?   A . n 
A 1 151 TYR 151 162 ?   ?   ?   A . n 
A 1 152 LEU 152 163 ?   ?   ?   A . n 
A 1 153 ASN 153 164 ?   ?   ?   A . n 
A 1 154 GLY 154 165 ?   ?   ?   A . n 
A 1 155 ASP 155 166 ?   ?   ?   A . n 
A 1 156 HIS 156 167 ?   ?   ?   A . n 
A 1 157 VAL 157 168 ?   ?   ?   A . n 
A 1 158 THR 158 169 ?   ?   ?   A . n 
A 1 159 HIS 159 170 ?   ?   ?   A . n 
A 1 160 PRO 160 171 ?   ?   ?   A . n 
A 1 161 ASP 161 172 ?   ?   ?   A . n 
A 1 162 PHE 162 173 ?   ?   ?   A . n 
A 1 163 MET 163 174 ?   ?   ?   A . n 
A 1 164 LEU 164 175 ?   ?   ?   A . n 
A 1 165 TYR 165 176 ?   ?   ?   A . n 
A 1 166 ASP 166 177 ?   ?   ?   A . n 
A 1 167 ALA 167 178 ?   ?   ?   A . n 
A 1 168 LEU 168 179 ?   ?   ?   A . n 
A 1 169 ASP 169 180 ?   ?   ?   A . n 
A 1 170 VAL 170 181 ?   ?   ?   A . n 
A 1 171 VAL 171 182 ?   ?   ?   A . n 
A 1 172 LEU 172 183 ?   ?   ?   A . n 
A 1 173 TYR 173 184 ?   ?   ?   A . n 
A 1 174 MET 174 185 ?   ?   ?   A . n 
A 1 175 ASP 175 186 ?   ?   ?   A . n 
A 1 176 PRO 176 187 ?   ?   ?   A . n 
A 1 177 MET 177 188 ?   ?   ?   A . n 
A 1 178 CYS 178 189 ?   ?   ?   A . n 
A 1 179 LEU 179 190 ?   ?   ?   A . n 
A 1 180 ASP 180 191 ?   ?   ?   A . n 
A 1 181 ALA 181 192 ?   ?   ?   A . n 
A 1 182 PHE 182 193 ?   ?   ?   A . n 
A 1 183 PRO 183 194 ?   ?   ?   A . n 
A 1 184 LYS 184 195 ?   ?   ?   A . n 
A 1 185 LEU 185 196 ?   ?   ?   A . n 
A 1 186 VAL 186 197 ?   ?   ?   A . n 
A 1 187 CYS 187 198 ?   ?   ?   A . n 
A 1 188 PHE 188 199 ?   ?   ?   A . n 
A 1 189 LYS 189 200 ?   ?   ?   A . n 
A 1 190 LYS 190 201 ?   ?   ?   A . n 
A 1 191 ARG 191 202 ?   ?   ?   A . n 
A 1 192 ILE 192 203 ?   ?   ?   A . n 
A 1 193 GLU 193 204 ?   ?   ?   A . n 
A 1 194 ALA 194 205 ?   ?   ?   A . n 
A 1 195 ILE 195 206 ?   ?   ?   A . n 
A 1 196 PRO 196 207 ?   ?   ?   A . n 
A 1 197 GLN 197 208 ?   ?   ?   A . n 
A 1 198 ILE 198 209 ?   ?   ?   A . n 
A 1 199 ASP 199 210 ?   ?   ?   A . n 
A 1 200 LYS 200 211 ?   ?   ?   A . n 
A 1 201 TYR 201 212 ?   ?   ?   A . n 
A 1 202 LEU 202 213 ?   ?   ?   A . n 
A 1 203 LYS 203 214 ?   ?   ?   A . n 
A 1 204 SER 204 215 ?   ?   ?   A . n 
A 1 205 SER 205 216 ?   ?   ?   A . n 
A 1 206 LYS 206 217 ?   ?   ?   A . n 
A 1 207 TYR 207 218 ?   ?   ?   A . n 
A 1 208 ILE 208 219 ?   ?   ?   A . n 
A 1 209 ALA 209 220 ?   ?   ?   A . n 
A 1 210 TRP 210 221 ?   ?   ?   A . n 
A 1 211 PRO 211 222 ?   ?   ?   A . n 
A 1 212 LEU 212 223 ?   ?   ?   A . n 
A 1 213 GLN 213 224 ?   ?   ?   A . n 
A 1 214 GLY 214 225 ?   ?   ?   A . n 
A 1 215 TRP 215 226 ?   ?   ?   A . n 
A 1 216 GLN 216 227 ?   ?   ?   A . n 
A 1 217 ALA 217 228 ?   ?   ?   A . n 
A 1 218 THR 218 229 ?   ?   ?   A . n 
A 1 219 PHE 219 230 ?   ?   ?   A . n 
A 1 220 GLY 220 231 ?   ?   ?   A . n 
A 1 221 GLY 221 232 ?   ?   ?   A . n 
A 1 222 GLY 222 233 ?   ?   ?   A . n 
A 1 223 ASP 223 234 ?   ?   ?   A . n 
A 1 224 HIS 224 235 ?   ?   ?   A . n 
A 1 225 PRO 225 236 ?   ?   ?   A . n 
A 1 226 PRO 226 237 ?   ?   ?   A . n 
A 1 227 LYS 227 238 ?   ?   ?   A . n 
A 1 228 SER 228 239 ?   ?   ?   A . n 
A 1 229 ASP 229 240 ?   ?   ?   A . n 
A 1 230 GLY 230 241 ?   ?   ?   A . n 
A 1 231 GLU 231 242 ?   ?   ?   A . n 
A 1 232 ASN 232 243 ?   ?   ?   A . n 
A 1 233 LEU 233 244 ?   ?   ?   A . n 
A 1 234 TYR 234 245 ?   ?   ?   A . n 
A 1 235 PHE 235 246 ?   ?   ?   A . n 
A 1 236 GLN 236 247 ?   ?   ?   A . n 
A 1 237 GLY 237 248 ?   ?   ?   A . n 
A 1 238 SER 238 249 249 SER SER A . n 
A 1 239 ASP 239 250 250 ASP ASP A . n 
A 1 240 GLU 240 251 251 GLU GLU A . n 
A 1 241 GLU 241 252 252 GLU GLU A . n 
A 1 242 ILE 242 253 253 ILE ILE A . n 
A 1 243 LEU 243 254 254 LEU LEU A . n 
A 1 244 GLU 244 255 255 GLU GLU A . n 
A 1 245 LYS 245 256 256 LYS LYS A . n 
A 1 246 LEU 246 257 257 LEU LEU A . n 
A 1 247 ARG 247 258 258 ARG ARG A . n 
A 1 248 SER 248 259 259 SER SER A . n 
A 1 249 ILE 249 260 260 ILE ILE A . n 
A 1 250 VAL 250 261 261 VAL VAL A . n 
A 1 251 SER 251 262 262 SER SER A . n 
A 1 252 VAL 252 263 263 VAL VAL A . n 
A 1 253 GLY 253 264 264 GLY GLY A . n 
A 1 254 ASP 254 265 265 ASP ASP A . n 
A 1 255 PRO 255 266 266 PRO PRO A . n 
A 1 256 LYS 256 267 267 LYS LYS A . n 
A 1 257 LYS 257 268 268 LYS LYS A . n 
A 1 258 LYS 258 269 269 LYS LYS A . n 
A 1 259 TYR 259 270 270 TYR TYR A . n 
A 1 260 THR 260 271 271 THR THR A . n 
A 1 261 ARG 261 272 272 ARG ARG A . n 
A 1 262 PHE 262 273 273 PHE PHE A . n 
A 1 263 GLU 263 274 274 GLU GLU A . n 
A 1 264 LYS 264 275 275 LYS LYS A . n 
A 1 265 ILE 265 276 276 ILE ILE A . n 
A 1 266 GLY 266 277 277 GLY GLY A . n 
A 1 267 GLN 267 278 278 GLN GLN A . n 
A 1 268 GLY 268 279 279 GLY GLY A . n 
A 1 269 ALA 269 280 280 ALA ALA A . n 
A 1 270 SER 270 281 281 SER SER A . n 
A 1 271 GLY 271 282 282 GLY GLY A . n 
A 1 272 THR 272 283 283 THR THR A . n 
A 1 273 VAL 273 284 284 VAL VAL A . n 
A 1 274 TYR 274 285 285 TYR TYR A . n 
A 1 275 THR 275 286 286 THR THR A . n 
A 1 276 ALA 276 287 287 ALA ALA A . n 
A 1 277 MET 277 288 288 MET MET A . n 
A 1 278 ASP 278 289 289 ASP ASP A . n 
A 1 279 VAL 279 290 290 VAL VAL A . n 
A 1 280 ALA 280 291 291 ALA ALA A . n 
A 1 281 THR 281 292 292 THR THR A . n 
A 1 282 GLY 282 293 293 GLY GLY A . n 
A 1 283 GLN 283 294 294 GLN GLN A . n 
A 1 284 GLU 284 295 295 GLU GLU A . n 
A 1 285 VAL 285 296 296 VAL VAL A . n 
A 1 286 ALA 286 297 297 ALA ALA A . n 
A 1 287 ILE 287 298 298 ILE ILE A . n 
A 1 288 LYS 288 299 299 LYS LYS A . n 
A 1 289 GLN 289 300 300 GLN GLN A . n 
A 1 290 MET 290 301 301 MET MET A . n 
A 1 291 ASN 291 302 302 ASN ASN A . n 
A 1 292 LEU 292 303 303 LEU LEU A . n 
A 1 293 GLN 293 304 304 GLN GLN A . n 
A 1 294 GLN 294 305 305 GLN GLN A . n 
A 1 295 GLN 295 306 306 GLN GLN A . n 
A 1 296 PRO 296 307 307 PRO PRO A . n 
A 1 297 LYS 297 308 308 LYS LYS A . n 
A 1 298 LYS 298 309 309 LYS LYS A . n 
A 1 299 GLU 299 310 310 GLU GLU A . n 
A 1 300 LEU 300 311 311 LEU LEU A . n 
A 1 301 ILE 301 312 312 ILE ILE A . n 
A 1 302 ILE 302 313 313 ILE ILE A . n 
A 1 303 ASN 303 314 314 ASN ASN A . n 
A 1 304 GLU 304 315 315 GLU GLU A . n 
A 1 305 ILE 305 316 316 ILE ILE A . n 
A 1 306 LEU 306 317 317 LEU LEU A . n 
A 1 307 VAL 307 318 318 VAL VAL A . n 
A 1 308 MET 308 319 319 MET MET A . n 
A 1 309 ARG 309 320 320 ARG ARG A . n 
A 1 310 GLU 310 321 321 GLU GLU A . n 
A 1 311 ASN 311 322 322 ASN ASN A . n 
A 1 312 LYS 312 323 323 LYS LYS A . n 
A 1 313 ASN 313 324 324 ASN ASN A . n 
A 1 314 PRO 314 325 325 PRO PRO A . n 
A 1 315 ASN 315 326 326 ASN ASN A . n 
A 1 316 ILE 316 327 327 ILE ILE A . n 
A 1 317 VAL 317 328 328 VAL VAL A . n 
A 1 318 ASN 318 329 329 ASN ASN A . n 
A 1 319 TYR 319 330 330 TYR TYR A . n 
A 1 320 LEU 320 331 331 LEU LEU A . n 
A 1 321 ASP 321 332 332 ASP ASP A . n 
A 1 322 SER 322 333 333 SER SER A . n 
A 1 323 TYR 323 334 334 TYR TYR A . n 
A 1 324 LEU 324 335 335 LEU LEU A . n 
A 1 325 VAL 325 336 336 VAL VAL A . n 
A 1 326 GLY 326 337 337 GLY GLY A . n 
A 1 327 ASP 327 338 338 ASP ASP A . n 
A 1 328 GLU 328 339 339 GLU GLU A . n 
A 1 329 LEU 329 340 340 LEU LEU A . n 
A 1 330 TRP 330 341 341 TRP TRP A . n 
A 1 331 VAL 331 342 342 VAL VAL A . n 
A 1 332 VAL 332 343 343 VAL VAL A . n 
A 1 333 MET 333 344 344 MET MET A . n 
A 1 334 GLU 334 345 345 GLU GLU A . n 
A 1 335 TYR 335 346 346 TYR TYR A . n 
A 1 336 LEU 336 347 347 LEU LEU A . n 
A 1 337 ALA 337 348 348 ALA ALA A . n 
A 1 338 GLY 338 349 349 GLY GLY A . n 
A 1 339 GLY 339 350 350 GLY GLY A . n 
A 1 340 SER 340 351 351 SER SER A . n 
A 1 341 LEU 341 352 352 LEU LEU A . n 
A 1 342 THR 342 353 353 THR THR A . n 
A 1 343 ASP 343 354 354 ASP ASP A . n 
A 1 344 VAL 344 355 355 VAL VAL A . n 
A 1 345 VAL 345 356 356 VAL VAL A . n 
A 1 346 THR 346 357 357 THR THR A . n 
A 1 347 GLU 347 358 358 GLU GLU A . n 
A 1 348 THR 348 359 359 THR THR A . n 
A 1 349 CYS 349 360 360 CYS CYS A . n 
A 1 350 MET 350 361 361 MET MET A . n 
A 1 351 ASP 351 362 362 ASP ASP A . n 
A 1 352 GLU 352 363 363 GLU GLU A . n 
A 1 353 GLY 353 364 364 GLY GLY A . n 
A 1 354 GLN 354 365 365 GLN GLN A . n 
A 1 355 ILE 355 366 366 ILE ILE A . n 
A 1 356 ALA 356 367 367 ALA ALA A . n 
A 1 357 ALA 357 368 368 ALA ALA A . n 
A 1 358 VAL 358 369 369 VAL VAL A . n 
A 1 359 CYS 359 370 370 CYS CYS A . n 
A 1 360 ARG 360 371 371 ARG ARG A . n 
A 1 361 GLU 361 372 372 GLU GLU A . n 
A 1 362 CYS 362 373 373 CYS CYS A . n 
A 1 363 LEU 363 374 374 LEU LEU A . n 
A 1 364 GLN 364 375 375 GLN GLN A . n 
A 1 365 ALA 365 376 376 ALA ALA A . n 
A 1 366 LEU 366 377 377 LEU LEU A . n 
A 1 367 GLU 367 378 378 GLU GLU A . n 
A 1 368 PHE 368 379 379 PHE PHE A . n 
A 1 369 LEU 369 380 380 LEU LEU A . n 
A 1 370 HIS 370 381 381 HIS HIS A . n 
A 1 371 SER 371 382 382 SER SER A . n 
A 1 372 ASN 372 383 383 ASN ASN A . n 
A 1 373 GLN 373 384 384 GLN GLN A . n 
A 1 374 VAL 374 385 385 VAL VAL A . n 
A 1 375 ILE 375 386 386 ILE ILE A . n 
A 1 376 HIS 376 387 387 HIS HIS A . n 
A 1 377 ARG 377 388 388 ARG ARG A . n 
A 1 378 ASN 378 389 389 ASN ASN A . n 
A 1 379 ILE 379 390 390 ILE ILE A . n 
A 1 380 LYS 380 391 391 LYS LYS A . n 
A 1 381 SER 381 392 392 SER SER A . n 
A 1 382 ASP 382 393 393 ASP ASP A . n 
A 1 383 ASN 383 394 394 ASN ASN A . n 
A 1 384 ILE 384 395 395 ILE ILE A . n 
A 1 385 LEU 385 396 396 LEU LEU A . n 
A 1 386 LEU 386 397 397 LEU LEU A . n 
A 1 387 GLY 387 398 398 GLY GLY A . n 
A 1 388 MET 388 399 399 MET MET A . n 
A 1 389 ASP 389 400 400 ASP ASP A . n 
A 1 390 GLY 390 401 401 GLY GLY A . n 
A 1 391 SER 391 402 402 SER SER A . n 
A 1 392 VAL 392 403 403 VAL VAL A . n 
A 1 393 LYS 393 404 404 LYS LYS A . n 
A 1 394 LEU 394 405 405 LEU LEU A . n 
A 1 395 THR 395 406 406 THR THR A . n 
A 1 396 ASP 396 407 407 ASP ASP A . n 
A 1 397 PHE 397 408 408 PHE PHE A . n 
A 1 398 GLY 398 409 409 GLY GLY A . n 
A 1 399 PHE 399 410 410 PHE PHE A . n 
A 1 400 CYS 400 411 411 CYS CYS A . n 
A 1 401 ALA 401 412 412 ALA ALA A . n 
A 1 402 GLN 402 413 413 GLN GLN A . n 
A 1 403 ILE 403 414 414 ILE ILE A . n 
A 1 404 THR 404 415 415 THR THR A . n 
A 1 405 PRO 405 416 416 PRO PRO A . n 
A 1 406 GLU 406 417 417 GLU GLU A . n 
A 1 407 GLN 407 418 418 GLN GLN A . n 
A 1 408 SER 408 419 419 SER SER A . n 
A 1 409 LYS 409 420 420 LYS LYS A . n 
A 1 410 ARG 410 421 421 ARG ARG A . n 
A 1 411 SER 411 422 422 SER SER A . n 
A 1 412 GLU 412 423 423 GLU GLU A . n 
A 1 413 MET 413 424 424 MET MET A . n 
A 1 414 VAL 414 425 425 VAL VAL A . n 
A 1 415 GLY 415 426 426 GLY GLY A . n 
A 1 416 THR 416 427 427 THR THR A . n 
A 1 417 PRO 417 428 428 PRO PRO A . n 
A 1 418 TYR 418 429 429 TYR TYR A . n 
A 1 419 TRP 419 430 430 TRP TRP A . n 
A 1 420 MET 420 431 431 MET MET A . n 
A 1 421 ALA 421 432 432 ALA ALA A . n 
A 1 422 PRO 422 433 433 PRO PRO A . n 
A 1 423 GLU 423 434 434 GLU GLU A . n 
A 1 424 VAL 424 435 435 VAL VAL A . n 
A 1 425 VAL 425 436 436 VAL VAL A . n 
A 1 426 THR 426 437 437 THR THR A . n 
A 1 427 ARG 427 438 438 ARG ARG A . n 
A 1 428 LYS 428 439 439 LYS LYS A . n 
A 1 429 ALA 429 440 440 ALA ALA A . n 
A 1 430 TYR 430 441 441 TYR TYR A . n 
A 1 431 GLY 431 442 442 GLY GLY A . n 
A 1 432 PRO 432 443 443 PRO PRO A . n 
A 1 433 LYS 433 444 444 LYS LYS A . n 
A 1 434 VAL 434 445 445 VAL VAL A . n 
A 1 435 ASP 435 446 446 ASP ASP A . n 
A 1 436 ILE 436 447 447 ILE ILE A . n 
A 1 437 TRP 437 448 448 TRP TRP A . n 
A 1 438 SER 438 449 449 SER SER A . n 
A 1 439 LEU 439 450 450 LEU LEU A . n 
A 1 440 GLY 440 451 451 GLY GLY A . n 
A 1 441 ILE 441 452 452 ILE ILE A . n 
A 1 442 MET 442 453 453 MET MET A . n 
A 1 443 ALA 443 454 454 ALA ALA A . n 
A 1 444 ILE 444 455 455 ILE ILE A . n 
A 1 445 GLU 445 456 456 GLU GLU A . n 
A 1 446 MET 446 457 457 MET MET A . n 
A 1 447 ILE 447 458 458 ILE ILE A . n 
A 1 448 GLU 448 459 459 GLU GLU A . n 
A 1 449 GLY 449 460 460 GLY GLY A . n 
A 1 450 GLU 450 461 461 GLU GLU A . n 
A 1 451 PRO 451 462 462 PRO PRO A . n 
A 1 452 PRO 452 463 463 PRO PRO A . n 
A 1 453 TYR 453 464 464 TYR TYR A . n 
A 1 454 LEU 454 465 465 LEU LEU A . n 
A 1 455 ASN 455 466 466 ASN ASN A . n 
A 1 456 GLU 456 467 467 GLU GLU A . n 
A 1 457 ASN 457 468 468 ASN ASN A . n 
A 1 458 PRO 458 469 469 PRO PRO A . n 
A 1 459 LEU 459 470 470 LEU LEU A . n 
A 1 460 ARG 460 471 471 ARG ARG A . n 
A 1 461 ALA 461 472 472 ALA ALA A . n 
A 1 462 LEU 462 473 473 LEU LEU A . n 
A 1 463 TYR 463 474 474 TYR TYR A . n 
A 1 464 LEU 464 475 475 LEU LEU A . n 
A 1 465 ILE 465 476 476 ILE ILE A . n 
A 1 466 ALA 466 477 477 ALA ALA A . n 
A 1 467 THR 467 478 478 THR THR A . n 
A 1 468 ASN 468 479 479 ASN ASN A . n 
A 1 469 GLY 469 480 480 GLY GLY A . n 
A 1 470 THR 470 481 481 THR THR A . n 
A 1 471 PRO 471 482 482 PRO PRO A . n 
A 1 472 GLU 472 483 483 GLU GLU A . n 
A 1 473 LEU 473 484 484 LEU LEU A . n 
A 1 474 GLN 474 485 485 GLN GLN A . n 
A 1 475 ASN 475 486 486 ASN ASN A . n 
A 1 476 PRO 476 487 487 PRO PRO A . n 
A 1 477 GLU 477 488 488 GLU GLU A . n 
A 1 478 LYS 478 489 489 LYS LYS A . n 
A 1 479 LEU 479 490 490 LEU LEU A . n 
A 1 480 SER 480 491 491 SER SER A . n 
A 1 481 ALA 481 492 492 ALA ALA A . n 
A 1 482 ILE 482 493 493 ILE ILE A . n 
A 1 483 PHE 483 494 494 PHE PHE A . n 
A 1 484 ARG 484 495 495 ARG ARG A . n 
A 1 485 ASP 485 496 496 ASP ASP A . n 
A 1 486 PHE 486 497 497 PHE PHE A . n 
A 1 487 LEU 487 498 498 LEU LEU A . n 
A 1 488 ASN 488 499 499 ASN ASN A . n 
A 1 489 ARG 489 500 500 ARG ARG A . n 
A 1 490 CYS 490 501 501 CYS CYS A . n 
A 1 491 LEU 491 502 502 LEU LEU A . n 
A 1 492 GLU 492 503 503 GLU GLU A . n 
A 1 493 MET 493 504 504 MET MET A . n 
A 1 494 ASP 494 505 505 ASP ASP A . n 
A 1 495 VAL 495 506 506 VAL VAL A . n 
A 1 496 GLU 496 507 507 GLU GLU A . n 
A 1 497 LYS 497 508 508 LYS LYS A . n 
A 1 498 ARG 498 509 509 ARG ARG A . n 
A 1 499 GLY 499 510 510 GLY GLY A . n 
A 1 500 SER 500 511 511 SER SER A . n 
A 1 501 ALA 501 512 512 ALA ALA A . n 
A 1 502 LYS 502 513 513 LYS LYS A . n 
A 1 503 GLU 503 514 514 GLU GLU A . n 
A 1 504 LEU 504 515 515 LEU LEU A . n 
A 1 505 LEU 505 516 516 LEU LEU A . n 
A 1 506 GLN 506 517 517 GLN GLN A . n 
A 1 507 HIS 507 518 518 HIS HIS A . n 
A 1 508 GLN 508 519 519 GLN GLN A . n 
A 1 509 PHE 509 520 520 PHE PHE A . n 
A 1 510 LEU 510 521 521 LEU LEU A . n 
A 1 511 LYS 511 522 522 LYS LYS A . n 
A 1 512 ILE 512 523 523 ILE ILE A . n 
A 1 513 ALA 513 524 524 ALA ALA A . n 
A 1 514 LYS 514 525 525 LYS LYS A . n 
A 1 515 PRO 515 526 526 PRO PRO A . n 
A 1 516 LEU 516 527 527 LEU LEU A . n 
A 1 517 SER 517 528 528 SER SER A . n 
A 1 518 SER 518 529 529 SER SER A . n 
A 1 519 LEU 519 530 530 LEU LEU A . n 
A 1 520 THR 520 531 531 THR THR A . n 
A 1 521 PRO 521 532 532 PRO PRO A . n 
A 1 522 LEU 522 533 533 LEU LEU A . n 
A 1 523 ILE 523 534 534 ILE ILE A . n 
A 1 524 ALA 524 535 535 ALA ALA A . n 
A 1 525 ALA 525 536 536 ALA ALA A . n 
A 1 526 ALA 526 537 537 ALA ALA A . n 
A 1 527 LYS 527 538 538 LYS LYS A . n 
A 1 528 GLU 528 539 539 GLU GLU A . n 
A 1 529 ALA 529 540 540 ALA ALA A . n 
A 1 530 THR 530 541 541 THR THR A . n 
A 1 531 LYS 531 542 542 LYS LYS A . n 
A 1 532 ASN 532 543 543 ASN ASN A . n 
A 1 533 ASN 533 544 544 ASN ASN A . n 
A 1 534 HIS 534 545 545 HIS HIS A . n 
A 1 535 GLY 535 546 ?   ?   ?   A . n 
A 1 536 ASN 536 547 ?   ?   ?   A . n 
A 1 537 SER 537 548 ?   ?   ?   A . n 
B 1 1   MET 1   12  ?   ?   ?   B . n 
B 1 2   HIS 2   13  ?   ?   ?   B . n 
B 1 3   HIS 3   14  ?   ?   ?   B . n 
B 1 4   HIS 4   15  ?   ?   ?   B . n 
B 1 5   HIS 5   16  ?   ?   ?   B . n 
B 1 6   HIS 6   17  ?   ?   ?   B . n 
B 1 7   HIS 7   18  ?   ?   ?   B . n 
B 1 8   HIS 8   19  ?   ?   ?   B . n 
B 1 9   HIS 9   20  ?   ?   ?   B . n 
B 1 10  GLY 10  21  ?   ?   ?   B . n 
B 1 11  SER 11  22  ?   ?   ?   B . n 
B 1 12  PRO 12  23  ?   ?   ?   B . n 
B 1 13  ILE 13  24  ?   ?   ?   B . n 
B 1 14  LEU 14  25  ?   ?   ?   B . n 
B 1 15  GLY 15  26  ?   ?   ?   B . n 
B 1 16  TYR 16  27  ?   ?   ?   B . n 
B 1 17  TRP 17  28  ?   ?   ?   B . n 
B 1 18  LYS 18  29  ?   ?   ?   B . n 
B 1 19  ILE 19  30  ?   ?   ?   B . n 
B 1 20  LYS 20  31  ?   ?   ?   B . n 
B 1 21  GLY 21  32  ?   ?   ?   B . n 
B 1 22  LEU 22  33  ?   ?   ?   B . n 
B 1 23  VAL 23  34  ?   ?   ?   B . n 
B 1 24  GLN 24  35  ?   ?   ?   B . n 
B 1 25  PRO 25  36  ?   ?   ?   B . n 
B 1 26  THR 26  37  ?   ?   ?   B . n 
B 1 27  ARG 27  38  ?   ?   ?   B . n 
B 1 28  LEU 28  39  ?   ?   ?   B . n 
B 1 29  LEU 29  40  ?   ?   ?   B . n 
B 1 30  LEU 30  41  ?   ?   ?   B . n 
B 1 31  GLU 31  42  ?   ?   ?   B . n 
B 1 32  TYR 32  43  ?   ?   ?   B . n 
B 1 33  LEU 33  44  ?   ?   ?   B . n 
B 1 34  GLU 34  45  ?   ?   ?   B . n 
B 1 35  GLU 35  46  ?   ?   ?   B . n 
B 1 36  LYS 36  47  ?   ?   ?   B . n 
B 1 37  TYR 37  48  ?   ?   ?   B . n 
B 1 38  GLU 38  49  ?   ?   ?   B . n 
B 1 39  GLU 39  50  ?   ?   ?   B . n 
B 1 40  HIS 40  51  ?   ?   ?   B . n 
B 1 41  LEU 41  52  ?   ?   ?   B . n 
B 1 42  TYR 42  53  ?   ?   ?   B . n 
B 1 43  GLU 43  54  ?   ?   ?   B . n 
B 1 44  ARG 44  55  ?   ?   ?   B . n 
B 1 45  ASP 45  56  ?   ?   ?   B . n 
B 1 46  GLU 46  57  ?   ?   ?   B . n 
B 1 47  GLY 47  58  ?   ?   ?   B . n 
B 1 48  ASP 48  59  ?   ?   ?   B . n 
B 1 49  LYS 49  60  ?   ?   ?   B . n 
B 1 50  TRP 50  61  ?   ?   ?   B . n 
B 1 51  ARG 51  62  ?   ?   ?   B . n 
B 1 52  ASN 52  63  ?   ?   ?   B . n 
B 1 53  LYS 53  64  ?   ?   ?   B . n 
B 1 54  LYS 54  65  ?   ?   ?   B . n 
B 1 55  PHE 55  66  ?   ?   ?   B . n 
B 1 56  GLU 56  67  ?   ?   ?   B . n 
B 1 57  LEU 57  68  ?   ?   ?   B . n 
B 1 58  GLY 58  69  ?   ?   ?   B . n 
B 1 59  LEU 59  70  ?   ?   ?   B . n 
B 1 60  GLU 60  71  ?   ?   ?   B . n 
B 1 61  PHE 61  72  ?   ?   ?   B . n 
B 1 62  PRO 62  73  ?   ?   ?   B . n 
B 1 63  ASN 63  74  ?   ?   ?   B . n 
B 1 64  LEU 64  75  ?   ?   ?   B . n 
B 1 65  PRO 65  76  ?   ?   ?   B . n 
B 1 66  TYR 66  77  ?   ?   ?   B . n 
B 1 67  TYR 67  78  ?   ?   ?   B . n 
B 1 68  ILE 68  79  ?   ?   ?   B . n 
B 1 69  ASP 69  80  ?   ?   ?   B . n 
B 1 70  GLY 70  81  ?   ?   ?   B . n 
B 1 71  ASP 71  82  ?   ?   ?   B . n 
B 1 72  VAL 72  83  ?   ?   ?   B . n 
B 1 73  LYS 73  84  ?   ?   ?   B . n 
B 1 74  LEU 74  85  ?   ?   ?   B . n 
B 1 75  THR 75  86  ?   ?   ?   B . n 
B 1 76  GLN 76  87  ?   ?   ?   B . n 
B 1 77  SER 77  88  ?   ?   ?   B . n 
B 1 78  MET 78  89  ?   ?   ?   B . n 
B 1 79  ALA 79  90  ?   ?   ?   B . n 
B 1 80  ILE 80  91  ?   ?   ?   B . n 
B 1 81  ILE 81  92  ?   ?   ?   B . n 
B 1 82  ARG 82  93  ?   ?   ?   B . n 
B 1 83  TYR 83  94  ?   ?   ?   B . n 
B 1 84  ILE 84  95  ?   ?   ?   B . n 
B 1 85  ALA 85  96  ?   ?   ?   B . n 
B 1 86  ASP 86  97  ?   ?   ?   B . n 
B 1 87  LYS 87  98  ?   ?   ?   B . n 
B 1 88  HIS 88  99  ?   ?   ?   B . n 
B 1 89  ASN 89  100 ?   ?   ?   B . n 
B 1 90  MET 90  101 ?   ?   ?   B . n 
B 1 91  LEU 91  102 ?   ?   ?   B . n 
B 1 92  GLY 92  103 ?   ?   ?   B . n 
B 1 93  GLY 93  104 ?   ?   ?   B . n 
B 1 94  CYS 94  105 ?   ?   ?   B . n 
B 1 95  PRO 95  106 ?   ?   ?   B . n 
B 1 96  LYS 96  107 ?   ?   ?   B . n 
B 1 97  GLU 97  108 ?   ?   ?   B . n 
B 1 98  ARG 98  109 ?   ?   ?   B . n 
B 1 99  ALA 99  110 ?   ?   ?   B . n 
B 1 100 GLU 100 111 ?   ?   ?   B . n 
B 1 101 ILE 101 112 ?   ?   ?   B . n 
B 1 102 SER 102 113 ?   ?   ?   B . n 
B 1 103 MET 103 114 ?   ?   ?   B . n 
B 1 104 LEU 104 115 ?   ?   ?   B . n 
B 1 105 GLU 105 116 ?   ?   ?   B . n 
B 1 106 GLY 106 117 ?   ?   ?   B . n 
B 1 107 ALA 107 118 ?   ?   ?   B . n 
B 1 108 VAL 108 119 ?   ?   ?   B . n 
B 1 109 LEU 109 120 ?   ?   ?   B . n 
B 1 110 ASP 110 121 ?   ?   ?   B . n 
B 1 111 ILE 111 122 ?   ?   ?   B . n 
B 1 112 ARG 112 123 ?   ?   ?   B . n 
B 1 113 TYR 113 124 ?   ?   ?   B . n 
B 1 114 GLY 114 125 ?   ?   ?   B . n 
B 1 115 VAL 115 126 ?   ?   ?   B . n 
B 1 116 SER 116 127 ?   ?   ?   B . n 
B 1 117 ARG 117 128 ?   ?   ?   B . n 
B 1 118 ILE 118 129 ?   ?   ?   B . n 
B 1 119 ALA 119 130 ?   ?   ?   B . n 
B 1 120 TYR 120 131 ?   ?   ?   B . n 
B 1 121 SER 121 132 ?   ?   ?   B . n 
B 1 122 LYS 122 133 ?   ?   ?   B . n 
B 1 123 ASP 123 134 ?   ?   ?   B . n 
B 1 124 PHE 124 135 ?   ?   ?   B . n 
B 1 125 GLU 125 136 ?   ?   ?   B . n 
B 1 126 THR 126 137 ?   ?   ?   B . n 
B 1 127 LEU 127 138 ?   ?   ?   B . n 
B 1 128 LYS 128 139 ?   ?   ?   B . n 
B 1 129 VAL 129 140 ?   ?   ?   B . n 
B 1 130 ASP 130 141 ?   ?   ?   B . n 
B 1 131 PHE 131 142 ?   ?   ?   B . n 
B 1 132 LEU 132 143 ?   ?   ?   B . n 
B 1 133 SER 133 144 ?   ?   ?   B . n 
B 1 134 LYS 134 145 ?   ?   ?   B . n 
B 1 135 LEU 135 146 ?   ?   ?   B . n 
B 1 136 PRO 136 147 ?   ?   ?   B . n 
B 1 137 GLU 137 148 ?   ?   ?   B . n 
B 1 138 MET 138 149 ?   ?   ?   B . n 
B 1 139 LEU 139 150 ?   ?   ?   B . n 
B 1 140 LYS 140 151 ?   ?   ?   B . n 
B 1 141 MET 141 152 ?   ?   ?   B . n 
B 1 142 PHE 142 153 ?   ?   ?   B . n 
B 1 143 LYS 143 154 ?   ?   ?   B . n 
B 1 144 ASP 144 155 ?   ?   ?   B . n 
B 1 145 ARG 145 156 ?   ?   ?   B . n 
B 1 146 LEU 146 157 ?   ?   ?   B . n 
B 1 147 CYS 147 158 ?   ?   ?   B . n 
B 1 148 HIS 148 159 ?   ?   ?   B . n 
B 1 149 LYS 149 160 ?   ?   ?   B . n 
B 1 150 THR 150 161 ?   ?   ?   B . n 
B 1 151 TYR 151 162 ?   ?   ?   B . n 
B 1 152 LEU 152 163 ?   ?   ?   B . n 
B 1 153 ASN 153 164 ?   ?   ?   B . n 
B 1 154 GLY 154 165 ?   ?   ?   B . n 
B 1 155 ASP 155 166 ?   ?   ?   B . n 
B 1 156 HIS 156 167 ?   ?   ?   B . n 
B 1 157 VAL 157 168 ?   ?   ?   B . n 
B 1 158 THR 158 169 ?   ?   ?   B . n 
B 1 159 HIS 159 170 ?   ?   ?   B . n 
B 1 160 PRO 160 171 ?   ?   ?   B . n 
B 1 161 ASP 161 172 ?   ?   ?   B . n 
B 1 162 PHE 162 173 ?   ?   ?   B . n 
B 1 163 MET 163 174 ?   ?   ?   B . n 
B 1 164 LEU 164 175 ?   ?   ?   B . n 
B 1 165 TYR 165 176 ?   ?   ?   B . n 
B 1 166 ASP 166 177 ?   ?   ?   B . n 
B 1 167 ALA 167 178 ?   ?   ?   B . n 
B 1 168 LEU 168 179 ?   ?   ?   B . n 
B 1 169 ASP 169 180 ?   ?   ?   B . n 
B 1 170 VAL 170 181 ?   ?   ?   B . n 
B 1 171 VAL 171 182 ?   ?   ?   B . n 
B 1 172 LEU 172 183 ?   ?   ?   B . n 
B 1 173 TYR 173 184 ?   ?   ?   B . n 
B 1 174 MET 174 185 ?   ?   ?   B . n 
B 1 175 ASP 175 186 ?   ?   ?   B . n 
B 1 176 PRO 176 187 ?   ?   ?   B . n 
B 1 177 MET 177 188 ?   ?   ?   B . n 
B 1 178 CYS 178 189 ?   ?   ?   B . n 
B 1 179 LEU 179 190 ?   ?   ?   B . n 
B 1 180 ASP 180 191 ?   ?   ?   B . n 
B 1 181 ALA 181 192 ?   ?   ?   B . n 
B 1 182 PHE 182 193 ?   ?   ?   B . n 
B 1 183 PRO 183 194 ?   ?   ?   B . n 
B 1 184 LYS 184 195 ?   ?   ?   B . n 
B 1 185 LEU 185 196 ?   ?   ?   B . n 
B 1 186 VAL 186 197 ?   ?   ?   B . n 
B 1 187 CYS 187 198 ?   ?   ?   B . n 
B 1 188 PHE 188 199 ?   ?   ?   B . n 
B 1 189 LYS 189 200 ?   ?   ?   B . n 
B 1 190 LYS 190 201 ?   ?   ?   B . n 
B 1 191 ARG 191 202 ?   ?   ?   B . n 
B 1 192 ILE 192 203 ?   ?   ?   B . n 
B 1 193 GLU 193 204 ?   ?   ?   B . n 
B 1 194 ALA 194 205 ?   ?   ?   B . n 
B 1 195 ILE 195 206 ?   ?   ?   B . n 
B 1 196 PRO 196 207 ?   ?   ?   B . n 
B 1 197 GLN 197 208 ?   ?   ?   B . n 
B 1 198 ILE 198 209 ?   ?   ?   B . n 
B 1 199 ASP 199 210 ?   ?   ?   B . n 
B 1 200 LYS 200 211 ?   ?   ?   B . n 
B 1 201 TYR 201 212 ?   ?   ?   B . n 
B 1 202 LEU 202 213 ?   ?   ?   B . n 
B 1 203 LYS 203 214 ?   ?   ?   B . n 
B 1 204 SER 204 215 ?   ?   ?   B . n 
B 1 205 SER 205 216 ?   ?   ?   B . n 
B 1 206 LYS 206 217 ?   ?   ?   B . n 
B 1 207 TYR 207 218 ?   ?   ?   B . n 
B 1 208 ILE 208 219 ?   ?   ?   B . n 
B 1 209 ALA 209 220 ?   ?   ?   B . n 
B 1 210 TRP 210 221 ?   ?   ?   B . n 
B 1 211 PRO 211 222 ?   ?   ?   B . n 
B 1 212 LEU 212 223 ?   ?   ?   B . n 
B 1 213 GLN 213 224 ?   ?   ?   B . n 
B 1 214 GLY 214 225 ?   ?   ?   B . n 
B 1 215 TRP 215 226 ?   ?   ?   B . n 
B 1 216 GLN 216 227 ?   ?   ?   B . n 
B 1 217 ALA 217 228 ?   ?   ?   B . n 
B 1 218 THR 218 229 ?   ?   ?   B . n 
B 1 219 PHE 219 230 ?   ?   ?   B . n 
B 1 220 GLY 220 231 ?   ?   ?   B . n 
B 1 221 GLY 221 232 ?   ?   ?   B . n 
B 1 222 GLY 222 233 ?   ?   ?   B . n 
B 1 223 ASP 223 234 ?   ?   ?   B . n 
B 1 224 HIS 224 235 ?   ?   ?   B . n 
B 1 225 PRO 225 236 ?   ?   ?   B . n 
B 1 226 PRO 226 237 ?   ?   ?   B . n 
B 1 227 LYS 227 238 ?   ?   ?   B . n 
B 1 228 SER 228 239 ?   ?   ?   B . n 
B 1 229 ASP 229 240 ?   ?   ?   B . n 
B 1 230 GLY 230 241 ?   ?   ?   B . n 
B 1 231 GLU 231 242 ?   ?   ?   B . n 
B 1 232 ASN 232 243 ?   ?   ?   B . n 
B 1 233 LEU 233 244 ?   ?   ?   B . n 
B 1 234 TYR 234 245 ?   ?   ?   B . n 
B 1 235 PHE 235 246 ?   ?   ?   B . n 
B 1 236 GLN 236 247 ?   ?   ?   B . n 
B 1 237 GLY 237 248 ?   ?   ?   B . n 
B 1 238 SER 238 249 ?   ?   ?   B . n 
B 1 239 ASP 239 250 ?   ?   ?   B . n 
B 1 240 GLU 240 251 ?   ?   ?   B . n 
B 1 241 GLU 241 252 ?   ?   ?   B . n 
B 1 242 ILE 242 253 ?   ?   ?   B . n 
B 1 243 LEU 243 254 ?   ?   ?   B . n 
B 1 244 GLU 244 255 255 GLU GLU B . n 
B 1 245 LYS 245 256 256 LYS LYS B . n 
B 1 246 LEU 246 257 257 LEU LEU B . n 
B 1 247 ARG 247 258 258 ARG ARG B . n 
B 1 248 SER 248 259 259 SER SER B . n 
B 1 249 ILE 249 260 260 ILE ILE B . n 
B 1 250 VAL 250 261 261 VAL VAL B . n 
B 1 251 SER 251 262 262 SER SER B . n 
B 1 252 VAL 252 263 263 VAL VAL B . n 
B 1 253 GLY 253 264 264 GLY GLY B . n 
B 1 254 ASP 254 265 265 ASP ASP B . n 
B 1 255 PRO 255 266 266 PRO PRO B . n 
B 1 256 LYS 256 267 267 LYS LYS B . n 
B 1 257 LYS 257 268 268 LYS LYS B . n 
B 1 258 LYS 258 269 269 LYS LYS B . n 
B 1 259 TYR 259 270 270 TYR TYR B . n 
B 1 260 THR 260 271 271 THR THR B . n 
B 1 261 ARG 261 272 272 ARG ARG B . n 
B 1 262 PHE 262 273 273 PHE PHE B . n 
B 1 263 GLU 263 274 274 GLU GLU B . n 
B 1 264 LYS 264 275 275 LYS LYS B . n 
B 1 265 ILE 265 276 276 ILE ILE B . n 
B 1 266 GLY 266 277 277 GLY GLY B . n 
B 1 267 GLN 267 278 278 GLN GLN B . n 
B 1 268 GLY 268 279 279 GLY GLY B . n 
B 1 269 ALA 269 280 280 ALA ALA B . n 
B 1 270 SER 270 281 281 SER SER B . n 
B 1 271 GLY 271 282 282 GLY GLY B . n 
B 1 272 THR 272 283 283 THR THR B . n 
B 1 273 VAL 273 284 284 VAL VAL B . n 
B 1 274 TYR 274 285 285 TYR TYR B . n 
B 1 275 THR 275 286 286 THR THR B . n 
B 1 276 ALA 276 287 287 ALA ALA B . n 
B 1 277 MET 277 288 288 MET MET B . n 
B 1 278 ASP 278 289 289 ASP ASP B . n 
B 1 279 VAL 279 290 290 VAL VAL B . n 
B 1 280 ALA 280 291 291 ALA ALA B . n 
B 1 281 THR 281 292 292 THR THR B . n 
B 1 282 GLY 282 293 293 GLY GLY B . n 
B 1 283 GLN 283 294 294 GLN GLN B . n 
B 1 284 GLU 284 295 295 GLU GLU B . n 
B 1 285 VAL 285 296 296 VAL VAL B . n 
B 1 286 ALA 286 297 297 ALA ALA B . n 
B 1 287 ILE 287 298 298 ILE ILE B . n 
B 1 288 LYS 288 299 299 LYS LYS B . n 
B 1 289 GLN 289 300 300 GLN GLN B . n 
B 1 290 MET 290 301 301 MET MET B . n 
B 1 291 ASN 291 302 302 ASN ASN B . n 
B 1 292 LEU 292 303 303 LEU LEU B . n 
B 1 293 GLN 293 304 304 GLN GLN B . n 
B 1 294 GLN 294 305 305 GLN GLN B . n 
B 1 295 GLN 295 306 306 GLN GLN B . n 
B 1 296 PRO 296 307 307 PRO PRO B . n 
B 1 297 LYS 297 308 308 LYS LYS B . n 
B 1 298 LYS 298 309 309 LYS LYS B . n 
B 1 299 GLU 299 310 310 GLU GLU B . n 
B 1 300 LEU 300 311 311 LEU LEU B . n 
B 1 301 ILE 301 312 312 ILE ILE B . n 
B 1 302 ILE 302 313 313 ILE ILE B . n 
B 1 303 ASN 303 314 314 ASN ASN B . n 
B 1 304 GLU 304 315 315 GLU GLU B . n 
B 1 305 ILE 305 316 316 ILE ILE B . n 
B 1 306 LEU 306 317 317 LEU LEU B . n 
B 1 307 VAL 307 318 318 VAL VAL B . n 
B 1 308 MET 308 319 319 MET MET B . n 
B 1 309 ARG 309 320 320 ARG ARG B . n 
B 1 310 GLU 310 321 321 GLU GLU B . n 
B 1 311 ASN 311 322 322 ASN ASN B . n 
B 1 312 LYS 312 323 323 LYS LYS B . n 
B 1 313 ASN 313 324 324 ASN ASN B . n 
B 1 314 PRO 314 325 325 PRO PRO B . n 
B 1 315 ASN 315 326 326 ASN ASN B . n 
B 1 316 ILE 316 327 327 ILE ILE B . n 
B 1 317 VAL 317 328 328 VAL VAL B . n 
B 1 318 ASN 318 329 329 ASN ASN B . n 
B 1 319 TYR 319 330 330 TYR TYR B . n 
B 1 320 LEU 320 331 331 LEU LEU B . n 
B 1 321 ASP 321 332 332 ASP ASP B . n 
B 1 322 SER 322 333 333 SER SER B . n 
B 1 323 TYR 323 334 334 TYR TYR B . n 
B 1 324 LEU 324 335 335 LEU LEU B . n 
B 1 325 VAL 325 336 336 VAL VAL B . n 
B 1 326 GLY 326 337 337 GLY GLY B . n 
B 1 327 ASP 327 338 338 ASP ASP B . n 
B 1 328 GLU 328 339 339 GLU GLU B . n 
B 1 329 LEU 329 340 340 LEU LEU B . n 
B 1 330 TRP 330 341 341 TRP TRP B . n 
B 1 331 VAL 331 342 342 VAL VAL B . n 
B 1 332 VAL 332 343 343 VAL VAL B . n 
B 1 333 MET 333 344 344 MET MET B . n 
B 1 334 GLU 334 345 345 GLU GLU B . n 
B 1 335 TYR 335 346 346 TYR TYR B . n 
B 1 336 LEU 336 347 347 LEU LEU B . n 
B 1 337 ALA 337 348 348 ALA ALA B . n 
B 1 338 GLY 338 349 349 GLY GLY B . n 
B 1 339 GLY 339 350 350 GLY GLY B . n 
B 1 340 SER 340 351 351 SER SER B . n 
B 1 341 LEU 341 352 352 LEU LEU B . n 
B 1 342 THR 342 353 353 THR THR B . n 
B 1 343 ASP 343 354 354 ASP ASP B . n 
B 1 344 VAL 344 355 355 VAL VAL B . n 
B 1 345 VAL 345 356 356 VAL VAL B . n 
B 1 346 THR 346 357 357 THR THR B . n 
B 1 347 GLU 347 358 358 GLU GLU B . n 
B 1 348 THR 348 359 359 THR THR B . n 
B 1 349 CYS 349 360 360 CYS CYS B . n 
B 1 350 MET 350 361 361 MET MET B . n 
B 1 351 ASP 351 362 362 ASP ASP B . n 
B 1 352 GLU 352 363 363 GLU GLU B . n 
B 1 353 GLY 353 364 364 GLY GLY B . n 
B 1 354 GLN 354 365 365 GLN GLN B . n 
B 1 355 ILE 355 366 366 ILE ILE B . n 
B 1 356 ALA 356 367 367 ALA ALA B . n 
B 1 357 ALA 357 368 368 ALA ALA B . n 
B 1 358 VAL 358 369 369 VAL VAL B . n 
B 1 359 CYS 359 370 370 CYS CYS B . n 
B 1 360 ARG 360 371 371 ARG ARG B . n 
B 1 361 GLU 361 372 372 GLU GLU B . n 
B 1 362 CYS 362 373 373 CYS CYS B . n 
B 1 363 LEU 363 374 374 LEU LEU B . n 
B 1 364 GLN 364 375 375 GLN GLN B . n 
B 1 365 ALA 365 376 376 ALA ALA B . n 
B 1 366 LEU 366 377 377 LEU LEU B . n 
B 1 367 GLU 367 378 378 GLU GLU B . n 
B 1 368 PHE 368 379 379 PHE PHE B . n 
B 1 369 LEU 369 380 380 LEU LEU B . n 
B 1 370 HIS 370 381 381 HIS HIS B . n 
B 1 371 SER 371 382 382 SER SER B . n 
B 1 372 ASN 372 383 383 ASN ASN B . n 
B 1 373 GLN 373 384 384 GLN GLN B . n 
B 1 374 VAL 374 385 385 VAL VAL B . n 
B 1 375 ILE 375 386 386 ILE ILE B . n 
B 1 376 HIS 376 387 387 HIS HIS B . n 
B 1 377 ARG 377 388 388 ARG ARG B . n 
B 1 378 ASN 378 389 389 ASN ASN B . n 
B 1 379 ILE 379 390 390 ILE ILE B . n 
B 1 380 LYS 380 391 391 LYS LYS B . n 
B 1 381 SER 381 392 392 SER SER B . n 
B 1 382 ASP 382 393 393 ASP ASP B . n 
B 1 383 ASN 383 394 394 ASN ASN B . n 
B 1 384 ILE 384 395 395 ILE ILE B . n 
B 1 385 LEU 385 396 396 LEU LEU B . n 
B 1 386 LEU 386 397 397 LEU LEU B . n 
B 1 387 GLY 387 398 398 GLY GLY B . n 
B 1 388 MET 388 399 399 MET MET B . n 
B 1 389 ASP 389 400 400 ASP ASP B . n 
B 1 390 GLY 390 401 401 GLY GLY B . n 
B 1 391 SER 391 402 402 SER SER B . n 
B 1 392 VAL 392 403 403 VAL VAL B . n 
B 1 393 LYS 393 404 404 LYS LYS B . n 
B 1 394 LEU 394 405 405 LEU LEU B . n 
B 1 395 THR 395 406 406 THR THR B . n 
B 1 396 ASP 396 407 407 ASP ASP B . n 
B 1 397 PHE 397 408 408 PHE PHE B . n 
B 1 398 GLY 398 409 409 GLY GLY B . n 
B 1 399 PHE 399 410 410 PHE PHE B . n 
B 1 400 CYS 400 411 ?   ?   ?   B . n 
B 1 401 ALA 401 412 ?   ?   ?   B . n 
B 1 402 GLN 402 413 ?   ?   ?   B . n 
B 1 403 ILE 403 414 ?   ?   ?   B . n 
B 1 404 THR 404 415 ?   ?   ?   B . n 
B 1 405 PRO 405 416 ?   ?   ?   B . n 
B 1 406 GLU 406 417 ?   ?   ?   B . n 
B 1 407 GLN 407 418 ?   ?   ?   B . n 
B 1 408 SER 408 419 419 SER SER B . n 
B 1 409 LYS 409 420 420 LYS LYS B . n 
B 1 410 ARG 410 421 421 ARG ARG B . n 
B 1 411 SER 411 422 422 SER SER B . n 
B 1 412 GLU 412 423 423 GLU GLU B . n 
B 1 413 MET 413 424 424 MET MET B . n 
B 1 414 VAL 414 425 425 VAL VAL B . n 
B 1 415 GLY 415 426 426 GLY GLY B . n 
B 1 416 THR 416 427 427 THR THR B . n 
B 1 417 PRO 417 428 428 PRO PRO B . n 
B 1 418 TYR 418 429 429 TYR TYR B . n 
B 1 419 TRP 419 430 430 TRP TRP B . n 
B 1 420 MET 420 431 431 MET MET B . n 
B 1 421 ALA 421 432 432 ALA ALA B . n 
B 1 422 PRO 422 433 433 PRO PRO B . n 
B 1 423 GLU 423 434 434 GLU GLU B . n 
B 1 424 VAL 424 435 435 VAL VAL B . n 
B 1 425 VAL 425 436 436 VAL VAL B . n 
B 1 426 THR 426 437 437 THR THR B . n 
B 1 427 ARG 427 438 438 ARG ARG B . n 
B 1 428 LYS 428 439 439 LYS LYS B . n 
B 1 429 ALA 429 440 440 ALA ALA B . n 
B 1 430 TYR 430 441 441 TYR TYR B . n 
B 1 431 GLY 431 442 442 GLY GLY B . n 
B 1 432 PRO 432 443 443 PRO PRO B . n 
B 1 433 LYS 433 444 444 LYS LYS B . n 
B 1 434 VAL 434 445 445 VAL VAL B . n 
B 1 435 ASP 435 446 446 ASP ASP B . n 
B 1 436 ILE 436 447 447 ILE ILE B . n 
B 1 437 TRP 437 448 448 TRP TRP B . n 
B 1 438 SER 438 449 449 SER SER B . n 
B 1 439 LEU 439 450 450 LEU LEU B . n 
B 1 440 GLY 440 451 451 GLY GLY B . n 
B 1 441 ILE 441 452 452 ILE ILE B . n 
B 1 442 MET 442 453 453 MET MET B . n 
B 1 443 ALA 443 454 454 ALA ALA B . n 
B 1 444 ILE 444 455 455 ILE ILE B . n 
B 1 445 GLU 445 456 456 GLU GLU B . n 
B 1 446 MET 446 457 457 MET MET B . n 
B 1 447 ILE 447 458 458 ILE ILE B . n 
B 1 448 GLU 448 459 459 GLU GLU B . n 
B 1 449 GLY 449 460 460 GLY GLY B . n 
B 1 450 GLU 450 461 461 GLU GLU B . n 
B 1 451 PRO 451 462 462 PRO PRO B . n 
B 1 452 PRO 452 463 463 PRO PRO B . n 
B 1 453 TYR 453 464 464 TYR TYR B . n 
B 1 454 LEU 454 465 465 LEU LEU B . n 
B 1 455 ASN 455 466 466 ASN ASN B . n 
B 1 456 GLU 456 467 467 GLU GLU B . n 
B 1 457 ASN 457 468 468 ASN ASN B . n 
B 1 458 PRO 458 469 469 PRO PRO B . n 
B 1 459 LEU 459 470 470 LEU LEU B . n 
B 1 460 ARG 460 471 471 ARG ARG B . n 
B 1 461 ALA 461 472 472 ALA ALA B . n 
B 1 462 LEU 462 473 473 LEU LEU B . n 
B 1 463 TYR 463 474 474 TYR TYR B . n 
B 1 464 LEU 464 475 475 LEU LEU B . n 
B 1 465 ILE 465 476 476 ILE ILE B . n 
B 1 466 ALA 466 477 477 ALA ALA B . n 
B 1 467 THR 467 478 478 THR THR B . n 
B 1 468 ASN 468 479 479 ASN ASN B . n 
B 1 469 GLY 469 480 480 GLY GLY B . n 
B 1 470 THR 470 481 481 THR THR B . n 
B 1 471 PRO 471 482 482 PRO PRO B . n 
B 1 472 GLU 472 483 483 GLU GLU B . n 
B 1 473 LEU 473 484 484 LEU LEU B . n 
B 1 474 GLN 474 485 485 GLN GLN B . n 
B 1 475 ASN 475 486 486 ASN ASN B . n 
B 1 476 PRO 476 487 487 PRO PRO B . n 
B 1 477 GLU 477 488 488 GLU GLU B . n 
B 1 478 LYS 478 489 489 LYS LYS B . n 
B 1 479 LEU 479 490 490 LEU LEU B . n 
B 1 480 SER 480 491 491 SER SER B . n 
B 1 481 ALA 481 492 492 ALA ALA B . n 
B 1 482 ILE 482 493 493 ILE ILE B . n 
B 1 483 PHE 483 494 494 PHE PHE B . n 
B 1 484 ARG 484 495 495 ARG ARG B . n 
B 1 485 ASP 485 496 496 ASP ASP B . n 
B 1 486 PHE 486 497 497 PHE PHE B . n 
B 1 487 LEU 487 498 498 LEU LEU B . n 
B 1 488 ASN 488 499 499 ASN ASN B . n 
B 1 489 ARG 489 500 500 ARG ARG B . n 
B 1 490 CYS 490 501 501 CYS CYS B . n 
B 1 491 LEU 491 502 502 LEU LEU B . n 
B 1 492 GLU 492 503 503 GLU GLU B . n 
B 1 493 MET 493 504 504 MET MET B . n 
B 1 494 ASP 494 505 505 ASP ASP B . n 
B 1 495 VAL 495 506 506 VAL VAL B . n 
B 1 496 GLU 496 507 507 GLU GLU B . n 
B 1 497 LYS 497 508 508 LYS LYS B . n 
B 1 498 ARG 498 509 509 ARG ARG B . n 
B 1 499 GLY 499 510 510 GLY GLY B . n 
B 1 500 SER 500 511 511 SER SER B . n 
B 1 501 ALA 501 512 512 ALA ALA B . n 
B 1 502 LYS 502 513 513 LYS LYS B . n 
B 1 503 GLU 503 514 514 GLU GLU B . n 
B 1 504 LEU 504 515 515 LEU LEU B . n 
B 1 505 LEU 505 516 516 LEU LEU B . n 
B 1 506 GLN 506 517 517 GLN GLN B . n 
B 1 507 HIS 507 518 518 HIS HIS B . n 
B 1 508 GLN 508 519 519 GLN GLN B . n 
B 1 509 PHE 509 520 520 PHE PHE B . n 
B 1 510 LEU 510 521 521 LEU LEU B . n 
B 1 511 LYS 511 522 522 LYS LYS B . n 
B 1 512 ILE 512 523 523 ILE ILE B . n 
B 1 513 ALA 513 524 524 ALA ALA B . n 
B 1 514 LYS 514 525 525 LYS LYS B . n 
B 1 515 PRO 515 526 526 PRO PRO B . n 
B 1 516 LEU 516 527 527 LEU LEU B . n 
B 1 517 SER 517 528 528 SER SER B . n 
B 1 518 SER 518 529 529 SER SER B . n 
B 1 519 LEU 519 530 530 LEU LEU B . n 
B 1 520 THR 520 531 531 THR THR B . n 
B 1 521 PRO 521 532 532 PRO PRO B . n 
B 1 522 LEU 522 533 533 LEU LEU B . n 
B 1 523 ILE 523 534 534 ILE ILE B . n 
B 1 524 ALA 524 535 535 ALA ALA B . n 
B 1 525 ALA 525 536 536 ALA ALA B . n 
B 1 526 ALA 526 537 537 ALA ALA B . n 
B 1 527 LYS 527 538 538 LYS LYS B . n 
B 1 528 GLU 528 539 539 GLU GLU B . n 
B 1 529 ALA 529 540 540 ALA ALA B . n 
B 1 530 THR 530 541 541 THR THR B . n 
B 1 531 LYS 531 542 542 LYS LYS B . n 
B 1 532 ASN 532 543 ?   ?   ?   B . n 
B 1 533 ASN 533 544 ?   ?   ?   B . n 
B 1 534 HIS 534 545 ?   ?   ?   B . n 
B 1 535 GLY 535 546 ?   ?   ?   B . n 
B 1 536 ASN 536 547 ?   ?   ?   B . n 
B 1 537 SER 537 548 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BV1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BV1 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 2 A1BV1 1   601 1   A1BV1 LIG A . 
D 2 A1BV1 1   601 1   A1BV1 LIG B . 
E 3 HOH   1   701 87  HOH   HOH A . 
E 3 HOH   2   702 103 HOH   HOH A . 
E 3 HOH   3   703 416 HOH   HOH A . 
E 3 HOH   4   704 71  HOH   HOH A . 
E 3 HOH   5   705 276 HOH   HOH A . 
E 3 HOH   6   706 81  HOH   HOH A . 
E 3 HOH   7   707 202 HOH   HOH A . 
E 3 HOH   8   708 215 HOH   HOH A . 
E 3 HOH   9   709 16  HOH   HOH A . 
E 3 HOH   10  710 254 HOH   HOH A . 
E 3 HOH   11  711 408 HOH   HOH A . 
E 3 HOH   12  712 75  HOH   HOH A . 
E 3 HOH   13  713 90  HOH   HOH A . 
E 3 HOH   14  714 30  HOH   HOH A . 
E 3 HOH   15  715 382 HOH   HOH A . 
E 3 HOH   16  716 50  HOH   HOH A . 
E 3 HOH   17  717 157 HOH   HOH A . 
E 3 HOH   18  718 170 HOH   HOH A . 
E 3 HOH   19  719 11  HOH   HOH A . 
E 3 HOH   20  720 195 HOH   HOH A . 
E 3 HOH   21  721 319 HOH   HOH A . 
E 3 HOH   22  722 240 HOH   HOH A . 
E 3 HOH   23  723 286 HOH   HOH A . 
E 3 HOH   24  724 145 HOH   HOH A . 
E 3 HOH   25  725 252 HOH   HOH A . 
E 3 HOH   26  726 196 HOH   HOH A . 
E 3 HOH   27  727 93  HOH   HOH A . 
E 3 HOH   28  728 99  HOH   HOH A . 
E 3 HOH   29  729 27  HOH   HOH A . 
E 3 HOH   30  730 74  HOH   HOH A . 
E 3 HOH   31  731 112 HOH   HOH A . 
E 3 HOH   32  732 147 HOH   HOH A . 
E 3 HOH   33  733 241 HOH   HOH A . 
E 3 HOH   34  734 389 HOH   HOH A . 
E 3 HOH   35  735 39  HOH   HOH A . 
E 3 HOH   36  736 180 HOH   HOH A . 
E 3 HOH   37  737 296 HOH   HOH A . 
E 3 HOH   38  738 347 HOH   HOH A . 
E 3 HOH   39  739 77  HOH   HOH A . 
E 3 HOH   40  740 205 HOH   HOH A . 
E 3 HOH   41  741 402 HOH   HOH A . 
E 3 HOH   42  742 181 HOH   HOH A . 
E 3 HOH   43  743 216 HOH   HOH A . 
E 3 HOH   44  744 227 HOH   HOH A . 
E 3 HOH   45  745 238 HOH   HOH A . 
E 3 HOH   46  746 108 HOH   HOH A . 
E 3 HOH   47  747 88  HOH   HOH A . 
E 3 HOH   48  748 236 HOH   HOH A . 
E 3 HOH   49  749 61  HOH   HOH A . 
E 3 HOH   50  750 403 HOH   HOH A . 
E 3 HOH   51  751 350 HOH   HOH A . 
E 3 HOH   52  752 141 HOH   HOH A . 
E 3 HOH   53  753 182 HOH   HOH A . 
E 3 HOH   54  754 98  HOH   HOH A . 
E 3 HOH   55  755 56  HOH   HOH A . 
E 3 HOH   56  756 123 HOH   HOH A . 
E 3 HOH   57  757 64  HOH   HOH A . 
E 3 HOH   58  758 44  HOH   HOH A . 
E 3 HOH   59  759 420 HOH   HOH A . 
E 3 HOH   60  760 137 HOH   HOH A . 
E 3 HOH   61  761 128 HOH   HOH A . 
E 3 HOH   62  762 18  HOH   HOH A . 
E 3 HOH   63  763 51  HOH   HOH A . 
E 3 HOH   64  764 62  HOH   HOH A . 
E 3 HOH   65  765 115 HOH   HOH A . 
E 3 HOH   66  766 116 HOH   HOH A . 
E 3 HOH   67  767 113 HOH   HOH A . 
E 3 HOH   68  768 235 HOH   HOH A . 
E 3 HOH   69  769 10  HOH   HOH A . 
E 3 HOH   70  770 307 HOH   HOH A . 
E 3 HOH   71  771 31  HOH   HOH A . 
E 3 HOH   72  772 374 HOH   HOH A . 
E 3 HOH   73  773 278 HOH   HOH A . 
E 3 HOH   74  774 183 HOH   HOH A . 
E 3 HOH   75  775 193 HOH   HOH A . 
E 3 HOH   76  776 104 HOH   HOH A . 
E 3 HOH   77  777 139 HOH   HOH A . 
E 3 HOH   78  778 26  HOH   HOH A . 
E 3 HOH   79  779 135 HOH   HOH A . 
E 3 HOH   80  780 38  HOH   HOH A . 
E 3 HOH   81  781 84  HOH   HOH A . 
E 3 HOH   82  782 239 HOH   HOH A . 
E 3 HOH   83  783 32  HOH   HOH A . 
E 3 HOH   84  784 48  HOH   HOH A . 
E 3 HOH   85  785 257 HOH   HOH A . 
E 3 HOH   86  786 155 HOH   HOH A . 
E 3 HOH   87  787 174 HOH   HOH A . 
E 3 HOH   88  788 110 HOH   HOH A . 
E 3 HOH   89  789 245 HOH   HOH A . 
E 3 HOH   90  790 411 HOH   HOH A . 
E 3 HOH   91  791 190 HOH   HOH A . 
E 3 HOH   92  792 173 HOH   HOH A . 
E 3 HOH   93  793 5   HOH   HOH A . 
E 3 HOH   94  794 118 HOH   HOH A . 
E 3 HOH   95  795 268 HOH   HOH A . 
E 3 HOH   96  796 125 HOH   HOH A . 
E 3 HOH   97  797 17  HOH   HOH A . 
E 3 HOH   98  798 33  HOH   HOH A . 
E 3 HOH   99  799 261 HOH   HOH A . 
E 3 HOH   100 800 277 HOH   HOH A . 
E 3 HOH   101 801 96  HOH   HOH A . 
E 3 HOH   102 802 94  HOH   HOH A . 
E 3 HOH   103 803 109 HOH   HOH A . 
E 3 HOH   104 804 7   HOH   HOH A . 
E 3 HOH   105 805 3   HOH   HOH A . 
E 3 HOH   106 806 24  HOH   HOH A . 
E 3 HOH   107 807 146 HOH   HOH A . 
E 3 HOH   108 808 163 HOH   HOH A . 
E 3 HOH   109 809 37  HOH   HOH A . 
E 3 HOH   110 810 262 HOH   HOH A . 
E 3 HOH   111 811 142 HOH   HOH A . 
E 3 HOH   112 812 343 HOH   HOH A . 
E 3 HOH   113 813 34  HOH   HOH A . 
E 3 HOH   114 814 315 HOH   HOH A . 
E 3 HOH   115 815 85  HOH   HOH A . 
E 3 HOH   116 816 138 HOH   HOH A . 
E 3 HOH   117 817 19  HOH   HOH A . 
E 3 HOH   118 818 54  HOH   HOH A . 
E 3 HOH   119 819 67  HOH   HOH A . 
E 3 HOH   120 820 250 HOH   HOH A . 
E 3 HOH   121 821 70  HOH   HOH A . 
E 3 HOH   122 822 111 HOH   HOH A . 
E 3 HOH   123 823 36  HOH   HOH A . 
E 3 HOH   124 824 1   HOH   HOH A . 
E 3 HOH   125 825 316 HOH   HOH A . 
E 3 HOH   126 826 92  HOH   HOH A . 
E 3 HOH   127 827 218 HOH   HOH A . 
E 3 HOH   128 828 246 HOH   HOH A . 
E 3 HOH   129 829 282 HOH   HOH A . 
E 3 HOH   130 830 45  HOH   HOH A . 
E 3 HOH   131 831 130 HOH   HOH A . 
E 3 HOH   132 832 121 HOH   HOH A . 
E 3 HOH   133 833 318 HOH   HOH A . 
E 3 HOH   134 834 284 HOH   HOH A . 
E 3 HOH   135 835 311 HOH   HOH A . 
E 3 HOH   136 836 184 HOH   HOH A . 
E 3 HOH   137 837 206 HOH   HOH A . 
E 3 HOH   138 838 136 HOH   HOH A . 
E 3 HOH   139 839 35  HOH   HOH A . 
E 3 HOH   140 840 86  HOH   HOH A . 
E 3 HOH   141 841 162 HOH   HOH A . 
E 3 HOH   142 842 149 HOH   HOH A . 
E 3 HOH   143 843 46  HOH   HOH A . 
E 3 HOH   144 844 187 HOH   HOH A . 
E 3 HOH   145 845 214 HOH   HOH A . 
E 3 HOH   146 846 297 HOH   HOH A . 
E 3 HOH   147 847 6   HOH   HOH A . 
E 3 HOH   148 848 152 HOH   HOH A . 
E 3 HOH   149 849 263 HOH   HOH A . 
E 3 HOH   150 850 300 HOH   HOH A . 
E 3 HOH   151 851 397 HOH   HOH A . 
E 3 HOH   152 852 358 HOH   HOH A . 
E 3 HOH   153 853 355 HOH   HOH A . 
E 3 HOH   154 854 312 HOH   HOH A . 
E 3 HOH   155 855 148 HOH   HOH A . 
E 3 HOH   156 856 260 HOH   HOH A . 
E 3 HOH   157 857 244 HOH   HOH A . 
E 3 HOH   158 858 89  HOH   HOH A . 
E 3 HOH   159 859 298 HOH   HOH A . 
E 3 HOH   160 860 334 HOH   HOH A . 
E 3 HOH   161 861 197 HOH   HOH A . 
E 3 HOH   162 862 287 HOH   HOH A . 
E 3 HOH   163 863 208 HOH   HOH A . 
E 3 HOH   164 864 95  HOH   HOH A . 
E 3 HOH   165 865 79  HOH   HOH A . 
E 3 HOH   166 866 143 HOH   HOH A . 
E 3 HOH   167 867 331 HOH   HOH A . 
E 3 HOH   168 868 423 HOH   HOH A . 
E 3 HOH   169 869 375 HOH   HOH A . 
E 3 HOH   170 870 225 HOH   HOH A . 
E 3 HOH   171 871 309 HOH   HOH A . 
E 3 HOH   172 872 222 HOH   HOH A . 
E 3 HOH   173 873 337 HOH   HOH A . 
E 3 HOH   174 874 198 HOH   HOH A . 
E 3 HOH   175 875 295 HOH   HOH A . 
E 3 HOH   176 876 158 HOH   HOH A . 
E 3 HOH   177 877 151 HOH   HOH A . 
E 3 HOH   178 878 332 HOH   HOH A . 
E 3 HOH   179 879 405 HOH   HOH A . 
E 3 HOH   180 880 394 HOH   HOH A . 
E 3 HOH   181 881 22  HOH   HOH A . 
E 3 HOH   182 882 340 HOH   HOH A . 
E 3 HOH   183 883 419 HOH   HOH A . 
E 3 HOH   184 884 412 HOH   HOH A . 
E 3 HOH   185 885 169 HOH   HOH A . 
E 3 HOH   186 886 362 HOH   HOH A . 
E 3 HOH   187 887 248 HOH   HOH A . 
E 3 HOH   188 888 192 HOH   HOH A . 
E 3 HOH   189 889 228 HOH   HOH A . 
E 3 HOH   190 890 329 HOH   HOH A . 
E 3 HOH   191 891 265 HOH   HOH A . 
E 3 HOH   192 892 247 HOH   HOH A . 
E 3 HOH   193 893 279 HOH   HOH A . 
E 3 HOH   194 894 191 HOH   HOH A . 
E 3 HOH   195 895 275 HOH   HOH A . 
E 3 HOH   196 896 258 HOH   HOH A . 
E 3 HOH   197 897 237 HOH   HOH A . 
E 3 HOH   198 898 303 HOH   HOH A . 
E 3 HOH   199 899 273 HOH   HOH A . 
E 3 HOH   200 900 220 HOH   HOH A . 
E 3 HOH   201 901 354 HOH   HOH A . 
E 3 HOH   202 902 357 HOH   HOH A . 
F 3 HOH   1   701 166 HOH   HOH B . 
F 3 HOH   2   702 321 HOH   HOH B . 
F 3 HOH   3   703 418 HOH   HOH B . 
F 3 HOH   4   704 165 HOH   HOH B . 
F 3 HOH   5   705 13  HOH   HOH B . 
F 3 HOH   6   706 172 HOH   HOH B . 
F 3 HOH   7   707 80  HOH   HOH B . 
F 3 HOH   8   708 4   HOH   HOH B . 
F 3 HOH   9   709 20  HOH   HOH B . 
F 3 HOH   10  710 232 HOH   HOH B . 
F 3 HOH   11  711 322 HOH   HOH B . 
F 3 HOH   12  712 41  HOH   HOH B . 
F 3 HOH   13  713 369 HOH   HOH B . 
F 3 HOH   14  714 49  HOH   HOH B . 
F 3 HOH   15  715 341 HOH   HOH B . 
F 3 HOH   16  716 323 HOH   HOH B . 
F 3 HOH   17  717 401 HOH   HOH B . 
F 3 HOH   18  718 259 HOH   HOH B . 
F 3 HOH   19  719 176 HOH   HOH B . 
F 3 HOH   20  720 114 HOH   HOH B . 
F 3 HOH   21  721 352 HOH   HOH B . 
F 3 HOH   22  722 255 HOH   HOH B . 
F 3 HOH   23  723 42  HOH   HOH B . 
F 3 HOH   24  724 424 HOH   HOH B . 
F 3 HOH   25  725 161 HOH   HOH B . 
F 3 HOH   26  726 269 HOH   HOH B . 
F 3 HOH   27  727 413 HOH   HOH B . 
F 3 HOH   28  728 242 HOH   HOH B . 
F 3 HOH   29  729 363 HOH   HOH B . 
F 3 HOH   30  730 126 HOH   HOH B . 
F 3 HOH   31  731 124 HOH   HOH B . 
F 3 HOH   32  732 308 HOH   HOH B . 
F 3 HOH   33  733 421 HOH   HOH B . 
F 3 HOH   34  734 185 HOH   HOH B . 
F 3 HOH   35  735 203 HOH   HOH B . 
F 3 HOH   36  736 302 HOH   HOH B . 
F 3 HOH   37  737 219 HOH   HOH B . 
F 3 HOH   38  738 78  HOH   HOH B . 
F 3 HOH   39  739 69  HOH   HOH B . 
F 3 HOH   40  740 105 HOH   HOH B . 
F 3 HOH   41  741 194 HOH   HOH B . 
F 3 HOH   42  742 370 HOH   HOH B . 
F 3 HOH   43  743 338 HOH   HOH B . 
F 3 HOH   44  744 29  HOH   HOH B . 
F 3 HOH   45  745 52  HOH   HOH B . 
F 3 HOH   46  746 68  HOH   HOH B . 
F 3 HOH   47  747 47  HOH   HOH B . 
F 3 HOH   48  748 266 HOH   HOH B . 
F 3 HOH   49  749 21  HOH   HOH B . 
F 3 HOH   50  750 290 HOH   HOH B . 
F 3 HOH   51  751 43  HOH   HOH B . 
F 3 HOH   52  752 9   HOH   HOH B . 
F 3 HOH   53  753 100 HOH   HOH B . 
F 3 HOH   54  754 177 HOH   HOH B . 
F 3 HOH   55  755 14  HOH   HOH B . 
F 3 HOH   56  756 398 HOH   HOH B . 
F 3 HOH   57  757 73  HOH   HOH B . 
F 3 HOH   58  758 2   HOH   HOH B . 
F 3 HOH   59  759 117 HOH   HOH B . 
F 3 HOH   60  760 8   HOH   HOH B . 
F 3 HOH   61  761 164 HOH   HOH B . 
F 3 HOH   62  762 346 HOH   HOH B . 
F 3 HOH   63  763 253 HOH   HOH B . 
F 3 HOH   64  764 422 HOH   HOH B . 
F 3 HOH   65  765 119 HOH   HOH B . 
F 3 HOH   66  766 160 HOH   HOH B . 
F 3 HOH   67  767 57  HOH   HOH B . 
F 3 HOH   68  768 72  HOH   HOH B . 
F 3 HOH   69  769 179 HOH   HOH B . 
F 3 HOH   70  770 12  HOH   HOH B . 
F 3 HOH   71  771 58  HOH   HOH B . 
F 3 HOH   72  772 83  HOH   HOH B . 
F 3 HOH   73  773 40  HOH   HOH B . 
F 3 HOH   74  774 230 HOH   HOH B . 
F 3 HOH   75  775 122 HOH   HOH B . 
F 3 HOH   76  776 294 HOH   HOH B . 
F 3 HOH   77  777 133 HOH   HOH B . 
F 3 HOH   78  778 410 HOH   HOH B . 
F 3 HOH   79  779 127 HOH   HOH B . 
F 3 HOH   80  780 59  HOH   HOH B . 
F 3 HOH   81  781 212 HOH   HOH B . 
F 3 HOH   82  782 150 HOH   HOH B . 
F 3 HOH   83  783 132 HOH   HOH B . 
F 3 HOH   84  784 378 HOH   HOH B . 
F 3 HOH   85  785 271 HOH   HOH B . 
F 3 HOH   86  786 367 HOH   HOH B . 
F 3 HOH   87  787 65  HOH   HOH B . 
F 3 HOH   88  788 60  HOH   HOH B . 
F 3 HOH   89  789 159 HOH   HOH B . 
F 3 HOH   90  790 293 HOH   HOH B . 
F 3 HOH   91  791 186 HOH   HOH B . 
F 3 HOH   92  792 91  HOH   HOH B . 
F 3 HOH   93  793 106 HOH   HOH B . 
F 3 HOH   94  794 292 HOH   HOH B . 
F 3 HOH   95  795 28  HOH   HOH B . 
F 3 HOH   96  796 217 HOH   HOH B . 
F 3 HOH   97  797 66  HOH   HOH B . 
F 3 HOH   98  798 120 HOH   HOH B . 
F 3 HOH   99  799 396 HOH   HOH B . 
F 3 HOH   100 800 364 HOH   HOH B . 
F 3 HOH   101 801 427 HOH   HOH B . 
F 3 HOH   102 802 376 HOH   HOH B . 
F 3 HOH   103 803 53  HOH   HOH B . 
F 3 HOH   104 804 229 HOH   HOH B . 
F 3 HOH   105 805 324 HOH   HOH B . 
F 3 HOH   106 806 168 HOH   HOH B . 
F 3 HOH   107 807 101 HOH   HOH B . 
F 3 HOH   108 808 97  HOH   HOH B . 
F 3 HOH   109 809 264 HOH   HOH B . 
F 3 HOH   110 810 223 HOH   HOH B . 
F 3 HOH   111 811 82  HOH   HOH B . 
F 3 HOH   112 812 23  HOH   HOH B . 
F 3 HOH   113 813 131 HOH   HOH B . 
F 3 HOH   114 814 55  HOH   HOH B . 
F 3 HOH   115 815 107 HOH   HOH B . 
F 3 HOH   116 816 144 HOH   HOH B . 
F 3 HOH   117 817 175 HOH   HOH B . 
F 3 HOH   118 818 373 HOH   HOH B . 
F 3 HOH   119 819 391 HOH   HOH B . 
F 3 HOH   120 820 234 HOH   HOH B . 
F 3 HOH   121 821 188 HOH   HOH B . 
F 3 HOH   122 822 15  HOH   HOH B . 
F 3 HOH   123 823 289 HOH   HOH B . 
F 3 HOH   124 824 154 HOH   HOH B . 
F 3 HOH   125 825 140 HOH   HOH B . 
F 3 HOH   126 826 305 HOH   HOH B . 
F 3 HOH   127 827 320 HOH   HOH B . 
F 3 HOH   128 828 349 HOH   HOH B . 
F 3 HOH   129 829 63  HOH   HOH B . 
F 3 HOH   130 830 25  HOH   HOH B . 
F 3 HOH   131 831 415 HOH   HOH B . 
F 3 HOH   132 832 328 HOH   HOH B . 
F 3 HOH   133 833 171 HOH   HOH B . 
F 3 HOH   134 834 314 HOH   HOH B . 
F 3 HOH   135 835 361 HOH   HOH B . 
F 3 HOH   136 836 330 HOH   HOH B . 
F 3 HOH   137 837 371 HOH   HOH B . 
F 3 HOH   138 838 211 HOH   HOH B . 
F 3 HOH   139 839 156 HOH   HOH B . 
F 3 HOH   140 840 356 HOH   HOH B . 
F 3 HOH   141 841 327 HOH   HOH B . 
F 3 HOH   142 842 270 HOH   HOH B . 
F 3 HOH   143 843 285 HOH   HOH B . 
F 3 HOH   144 844 342 HOH   HOH B . 
F 3 HOH   145 845 351 HOH   HOH B . 
F 3 HOH   146 846 400 HOH   HOH B . 
F 3 HOH   147 847 310 HOH   HOH B . 
F 3 HOH   148 848 153 HOH   HOH B . 
F 3 HOH   149 849 380 HOH   HOH B . 
F 3 HOH   150 850 404 HOH   HOH B . 
F 3 HOH   151 851 167 HOH   HOH B . 
F 3 HOH   152 852 299 HOH   HOH B . 
F 3 HOH   153 853 201 HOH   HOH B . 
F 3 HOH   154 854 344 HOH   HOH B . 
F 3 HOH   155 855 251 HOH   HOH B . 
F 3 HOH   156 856 102 HOH   HOH B . 
F 3 HOH   157 857 291 HOH   HOH B . 
F 3 HOH   158 858 204 HOH   HOH B . 
F 3 HOH   159 859 425 HOH   HOH B . 
F 3 HOH   160 860 407 HOH   HOH B . 
F 3 HOH   161 861 272 HOH   HOH B . 
F 3 HOH   162 862 221 HOH   HOH B . 
F 3 HOH   163 863 224 HOH   HOH B . 
F 3 HOH   164 864 306 HOH   HOH B . 
F 3 HOH   165 865 348 HOH   HOH B . 
F 3 HOH   166 866 313 HOH   HOH B . 
F 3 HOH   167 867 366 HOH   HOH B . 
F 3 HOH   168 868 213 HOH   HOH B . 
F 3 HOH   169 869 226 HOH   HOH B . 
F 3 HOH   170 870 426 HOH   HOH B . 
F 3 HOH   171 871 134 HOH   HOH B . 
F 3 HOH   172 872 199 HOH   HOH B . 
F 3 HOH   173 873 387 HOH   HOH B . 
F 3 HOH   174 874 339 HOH   HOH B . 
F 3 HOH   175 875 409 HOH   HOH B . 
F 3 HOH   176 876 189 HOH   HOH B . 
F 3 HOH   177 877 288 HOH   HOH B . 
F 3 HOH   178 878 129 HOH   HOH B . 
F 3 HOH   179 879 406 HOH   HOH B . 
F 3 HOH   180 880 381 HOH   HOH B . 
F 3 HOH   181 881 207 HOH   HOH B . 
F 3 HOH   182 882 301 HOH   HOH B . 
F 3 HOH   183 883 231 HOH   HOH B . 
F 3 HOH   184 884 325 HOH   HOH B . 
F 3 HOH   185 885 178 HOH   HOH B . 
F 3 HOH   186 886 428 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 A SER 249 ? OG  ? A SER 238 OG  
2  1 Y 1 A ASP 250 ? CG  ? A ASP 239 CG  
3  1 Y 1 A ASP 250 ? OD1 ? A ASP 239 OD1 
4  1 Y 1 A ASP 250 ? OD2 ? A ASP 239 OD2 
5  1 Y 1 A GLN 304 ? CG  ? A GLN 293 CG  
6  1 Y 1 A GLN 304 ? CD  ? A GLN 293 CD  
7  1 Y 1 A GLN 304 ? OE1 ? A GLN 293 OE1 
8  1 Y 1 A GLN 304 ? NE2 ? A GLN 293 NE2 
9  1 Y 1 A GLN 305 ? CG  ? A GLN 294 CG  
10 1 Y 1 A GLN 305 ? CD  ? A GLN 294 CD  
11 1 Y 1 A GLN 305 ? OE1 ? A GLN 294 OE1 
12 1 Y 1 A GLN 305 ? NE2 ? A GLN 294 NE2 
13 1 Y 1 A ASN 543 ? CG  ? A ASN 532 CG  
14 1 Y 1 A ASN 543 ? OD1 ? A ASN 532 OD1 
15 1 Y 1 A ASN 543 ? ND2 ? A ASN 532 ND2 
16 1 Y 1 A ASN 544 ? CG  ? A ASN 533 CG  
17 1 Y 1 A ASN 544 ? OD1 ? A ASN 533 OD1 
18 1 Y 1 A ASN 544 ? ND2 ? A ASN 533 ND2 
19 1 Y 1 B GLU 255 ? CG  ? B GLU 244 CG  
20 1 Y 1 B GLU 255 ? CD  ? B GLU 244 CD  
21 1 Y 1 B GLU 255 ? OE1 ? B GLU 244 OE1 
22 1 Y 1 B GLU 255 ? OE2 ? B GLU 244 OE2 
23 1 Y 1 B LYS 256 ? CG  ? B LYS 245 CG  
24 1 Y 1 B LYS 256 ? CD  ? B LYS 245 CD  
25 1 Y 1 B LYS 256 ? CE  ? B LYS 245 CE  
26 1 Y 1 B LYS 256 ? NZ  ? B LYS 245 NZ  
27 1 Y 1 B ARG 258 ? CG  ? B ARG 247 CG  
28 1 Y 1 B ARG 258 ? CD  ? B ARG 247 CD  
29 1 Y 1 B ARG 258 ? NE  ? B ARG 247 NE  
30 1 Y 1 B ARG 258 ? CZ  ? B ARG 247 CZ  
31 1 Y 1 B ARG 258 ? NH1 ? B ARG 247 NH1 
32 1 Y 1 B ARG 258 ? NH2 ? B ARG 247 NH2 
33 1 Y 1 B GLN 304 ? CG  ? B GLN 293 CG  
34 1 Y 1 B GLN 304 ? CD  ? B GLN 293 CD  
35 1 Y 1 B GLN 304 ? OE1 ? B GLN 293 OE1 
36 1 Y 1 B GLN 304 ? NE2 ? B GLN 293 NE2 
37 1 Y 1 B GLN 306 ? CG  ? B GLN 295 CG  
38 1 Y 1 B GLN 306 ? CD  ? B GLN 295 CD  
39 1 Y 1 B GLN 306 ? OE1 ? B GLN 295 OE1 
40 1 Y 1 B GLN 306 ? NE2 ? B GLN 295 NE2 
41 1 Y 1 B LYS 309 ? CG  ? B LYS 298 CG  
42 1 Y 1 B LYS 309 ? CD  ? B LYS 298 CD  
43 1 Y 1 B LYS 309 ? CE  ? B LYS 298 CE  
44 1 Y 1 B LYS 309 ? NZ  ? B LYS 298 NZ  
45 1 Y 1 B LYS 542 ? CG  ? B LYS 531 CG  
46 1 Y 1 B LYS 542 ? CD  ? B LYS 531 CD  
47 1 Y 1 B LYS 542 ? CE  ? B LYS 531 CE  
48 1 Y 1 B LYS 542 ? NZ  ? B LYS 531 NZ  
# 
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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.23 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9N48 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.215 
_cell.length_a_esd                 ? 
_cell.length_b                     80.961 
_cell.length_b_esd                 ? 
_cell.length_c                     65.955 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9N48 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9N48 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '0.2 M Lithium Sulfate, 0.1 M Tris pH8.5, 30% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     93 
_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                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-11-20 
_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                    ? 
_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   1 
_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                        'APS BEAMLINE 21-ID-G' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-G 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9N48 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               50.00 
_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                                     52895 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.051 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       203038 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.057 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_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 
_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 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
1.85 1.92  ? ? ? ? ? ? 5219 ? ? ? ? ? ? ? ? ? ? ? 3.6 1.066 ? ? ? ? ? 1  1 ? ? ? 97.5 ? 0.667 ? ? ? ? ? ? ? ? ? 
1.92 1.99  ? ? ? ? ? ? 5231 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.091 ? ? ? ? ? 2  1 ? ? ? 97.4 ? 0.484 ? ? ? ? ? ? ? ? ? 
1.99 2.08  ? ? ? ? ? ? 5266 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.084 ? ? ? ? ? 3  1 ? ? ? 98.0 ? 0.321 ? ? ? ? ? ? ? ? ? 
2.08 2.19  ? ? ? ? ? ? 5225 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.045 ? ? ? ? ? 4  1 ? ? ? 98.0 ? 0.214 ? ? ? ? ? ? ? ? ? 
2.19 2.33  ? ? ? ? ? ? 5294 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.050 ? ? ? ? ? 5  1 ? ? ? 98.4 ? 0.150 ? ? ? ? ? ? ? ? ? 
2.33 2.51  ? ? ? ? ? ? 5255 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.042 ? ? ? ? ? 6  1 ? ? ? 98.5 ? 0.109 ? ? ? ? ? ? ? ? ? 
2.51 2.76  ? ? ? ? ? ? 5307 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.075 ? ? ? ? ? 7  1 ? ? ? 98.5 ? 0.082 ? ? ? ? ? ? ? ? ? 
2.76 3.16  ? ? ? ? ? ? 5320 ? ? ? ? ? ? ? ? ? ? ? 3.9 1.023 ? ? ? ? ? 8  1 ? ? ? 98.9 ? 0.061 ? ? ? ? ? ? ? ? ? 
3.16 3.99  ? ? ? ? ? ? 5353 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.015 ? ? ? ? ? 9  1 ? ? ? 99.1 ? 0.041 ? ? ? ? ? ? ? ? ? 
3.99 50.00 ? ? ? ? ? ? 5425 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.017 ? ? ? ? ? 10 1 ? ? ? 98.8 ? 0.030 ? ? ? ? ? ? ? ? ? 
# 
_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                               ? 
_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                                 9N48 
_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                            1.85 
_refine.ls_d_res_low                             34.11 
_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                     52866 
_refine.ls_number_reflns_R_free                  2694 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.25 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1783 
_refine.ls_R_factor_R_free                       0.2161 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1763 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 23.44 
_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                            0.22 
_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.pdbx_number_atoms_protein        4474 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_refine_hist.number_atoms_solvent             388 
_refine_hist.number_atoms_total               4930 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        34.11 
# 
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' ? 0.006  ? 4675 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.916  ? 6340 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.196 ? 1762 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058  ? 718  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 818  ? f_plane_restr      ? ? 
# 
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' 1.85 1.88  . . 134 2605 96.00 . . . . 0.3074 . . . . . . . . . . . 0.3623 
'X-RAY DIFFRACTION' 1.88 1.92  . . 139 2591 98.00 . . . . 0.2630 . . . . . . . . . . . 0.3044 
'X-RAY DIFFRACTION' 1.92 1.96  . . 155 2600 97.00 . . . . 0.2328 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 1.96 2.00  . . 138 2623 97.00 . . . . 0.2086 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 2.00 2.05  . . 134 2600 98.00 . . . . 0.2018 . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 2.05 2.10  . . 142 2619 98.00 . . . . 0.1972 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 2.10 2.15  . . 125 2650 98.00 . . . . 0.1859 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 2.15 2.22  . . 168 2610 98.00 . . . . 0.1885 . . . . . . . . . . . 0.2323 
'X-RAY DIFFRACTION' 2.22 2.29  . . 128 2625 98.00 . . . . 0.1917 . . . . . . . . . . . 0.2504 
'X-RAY DIFFRACTION' 2.29 2.37  . . 165 2632 98.00 . . . . 0.1803 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 2.37 2.47  . . 132 2646 99.00 . . . . 0.1791 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 2.47 2.58  . . 151 2621 99.00 . . . . 0.1801 . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 2.58 2.71  . . 147 2655 99.00 . . . . 0.1798 . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 2.71 2.88  . . 132 2642 99.00 . . . . 0.1834 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 2.88 3.11  . . 126 2718 99.00 . . . . 0.1846 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 3.11 3.42  . . 119 2665 99.00 . . . . 0.1807 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 3.42 3.91  . . 176 2656 99.00 . . . . 0.1574 . . . . . . . . . . . 0.1832 
'X-RAY DIFFRACTION' 3.91 4.93  . . 147 2677 99.00 . . . . 0.1456 . . . . . . . . . . . 0.1878 
'X-RAY DIFFRACTION' 4.93 34.11 . . 136 2737 99.00 . . . . 0.1642 . . . . . . . . . . . 0.1860 
# 
_struct.entry_id                     9N48 
_struct.title                        'Crystal structure of PAK1 bound to compound C1' 
_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        9N48 
_struct_keywords.text            'Kinase, inhibitor, 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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP GST26_SCHJA P08515 ? 1 
;SPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNM
LGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDV
VLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK
;
2   
2 UNP PAK1_HUMAN  Q13153 ? 1 
;SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV
NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF
GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE
KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH
;
249 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9N48 A 11  ? 227 ? P08515 2   ? 218 ? 22  238 
2 2 9N48 A 238 ? 534 ? Q13153 249 ? 545 ? 249 545 
3 1 9N48 B 11  ? 227 ? P08515 2   ? 218 ? 22  238 
4 2 9N48 B 238 ? 534 ? Q13153 249 ? 545 ? 249 545 
# 
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 9N48 MET A 1   ? UNP P08515 ?   ?   'expression tag' 12  1  
1 9N48 HIS A 2   ? UNP P08515 ?   ?   'expression tag' 13  2  
1 9N48 HIS A 3   ? UNP P08515 ?   ?   'expression tag' 14  3  
1 9N48 HIS A 4   ? UNP P08515 ?   ?   'expression tag' 15  4  
1 9N48 HIS A 5   ? UNP P08515 ?   ?   'expression tag' 16  5  
1 9N48 HIS A 6   ? UNP P08515 ?   ?   'expression tag' 17  6  
1 9N48 HIS A 7   ? UNP P08515 ?   ?   'expression tag' 18  7  
1 9N48 HIS A 8   ? UNP P08515 ?   ?   'expression tag' 19  8  
1 9N48 HIS A 9   ? UNP P08515 ?   ?   'expression tag' 20  9  
1 9N48 GLY A 10  ? UNP P08515 ?   ?   'expression tag' 21  10 
1 9N48 LYS A 143 ? UNP P08515 GLU 134 conflict         154 11 
1 9N48 SER A 228 ? UNP P08515 ?   ?   linker           239 12 
1 9N48 ASP A 229 ? UNP P08515 ?   ?   linker           240 13 
1 9N48 GLY A 230 ? UNP P08515 ?   ?   linker           241 14 
1 9N48 GLU A 231 ? UNP P08515 ?   ?   linker           242 15 
1 9N48 ASN A 232 ? UNP P08515 ?   ?   linker           243 16 
1 9N48 LEU A 233 ? UNP P08515 ?   ?   linker           244 17 
1 9N48 TYR A 234 ? UNP P08515 ?   ?   linker           245 18 
1 9N48 PHE A 235 ? UNP P08515 ?   ?   linker           246 19 
1 9N48 GLN A 236 ? UNP P08515 ?   ?   linker           247 20 
1 9N48 GLY A 237 ? UNP P08515 ?   ?   linker           248 21 
2 9N48 ASN A 378 ? UNP Q13153 ASP 389 conflict         389 22 
2 9N48 GLU A 412 ? UNP Q13153 THR 423 conflict         423 23 
2 9N48 GLY A 535 ? UNP Q13153 ?   ?   'expression tag' 546 24 
2 9N48 ASN A 536 ? UNP Q13153 ?   ?   'expression tag' 547 25 
2 9N48 SER A 537 ? UNP Q13153 ?   ?   'expression tag' 548 26 
3 9N48 MET B 1   ? UNP P08515 ?   ?   'expression tag' 12  27 
3 9N48 HIS B 2   ? UNP P08515 ?   ?   'expression tag' 13  28 
3 9N48 HIS B 3   ? UNP P08515 ?   ?   'expression tag' 14  29 
3 9N48 HIS B 4   ? UNP P08515 ?   ?   'expression tag' 15  30 
3 9N48 HIS B 5   ? UNP P08515 ?   ?   'expression tag' 16  31 
3 9N48 HIS B 6   ? UNP P08515 ?   ?   'expression tag' 17  32 
3 9N48 HIS B 7   ? UNP P08515 ?   ?   'expression tag' 18  33 
3 9N48 HIS B 8   ? UNP P08515 ?   ?   'expression tag' 19  34 
3 9N48 HIS B 9   ? UNP P08515 ?   ?   'expression tag' 20  35 
3 9N48 GLY B 10  ? UNP P08515 ?   ?   'expression tag' 21  36 
3 9N48 LYS B 143 ? UNP P08515 GLU 134 conflict         154 37 
3 9N48 SER B 228 ? UNP P08515 ?   ?   linker           239 38 
3 9N48 ASP B 229 ? UNP P08515 ?   ?   linker           240 39 
3 9N48 GLY B 230 ? UNP P08515 ?   ?   linker           241 40 
3 9N48 GLU B 231 ? UNP P08515 ?   ?   linker           242 41 
3 9N48 ASN B 232 ? UNP P08515 ?   ?   linker           243 42 
3 9N48 LEU B 233 ? UNP P08515 ?   ?   linker           244 43 
3 9N48 TYR B 234 ? UNP P08515 ?   ?   linker           245 44 
3 9N48 PHE B 235 ? UNP P08515 ?   ?   linker           246 45 
3 9N48 GLN B 236 ? UNP P08515 ?   ?   linker           247 46 
3 9N48 GLY B 237 ? UNP P08515 ?   ?   linker           248 47 
4 9N48 ASN B 378 ? UNP Q13153 ASP 389 conflict         389 48 
4 9N48 GLU B 412 ? UNP Q13153 THR 423 conflict         423 49 
4 9N48 GLY B 535 ? UNP Q13153 ?   ?   'expression tag' 546 50 
4 9N48 ASN B 536 ? UNP Q13153 ?   ?   'expression tag' 547 51 
4 9N48 SER B 537 ? UNP Q13153 ?   ?   'expression tag' 548 52 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 SER A 238 ? ILE A 249 ? SER A 249 ILE A 260 1 ? 12 
HELX_P HELX_P2  AA2 ASP A 254 ? LYS A 258 ? ASP A 265 LYS A 269 1 ? 5  
HELX_P HELX_P3  AA3 GLN A 293 ? GLN A 295 ? GLN A 304 GLN A 306 5 ? 3  
HELX_P HELX_P4  AA4 LYS A 297 ? ASN A 311 ? LYS A 308 ASN A 322 1 ? 15 
HELX_P HELX_P5  AA5 SER A 340 ? THR A 348 ? SER A 351 THR A 359 1 ? 9  
HELX_P HELX_P6  AA6 ASP A 351 ? ASN A 372 ? ASP A 362 ASN A 383 1 ? 22 
HELX_P HELX_P7  AA7 LYS A 380 ? ASP A 382 ? LYS A 391 ASP A 393 5 ? 3  
HELX_P HELX_P8  AA8 ASP A 396 ? CYS A 400 ? ASP A 407 CYS A 411 5 ? 5  
HELX_P HELX_P9  AA9 THR A 404 ? SER A 408 ? THR A 415 SER A 419 5 ? 5  
HELX_P HELX_P10 AB1 THR A 416 ? MET A 420 ? THR A 427 MET A 431 5 ? 5  
HELX_P HELX_P11 AB2 ALA A 421 ? THR A 426 ? ALA A 432 THR A 437 1 ? 6  
HELX_P HELX_P12 AB3 PRO A 432 ? GLY A 449 ? PRO A 443 GLY A 460 1 ? 18 
HELX_P HELX_P13 AB4 ASN A 457 ? GLY A 469 ? ASN A 468 GLY A 480 1 ? 13 
HELX_P HELX_P14 AB5 ASN A 475 ? LEU A 479 ? ASN A 486 LEU A 490 5 ? 5  
HELX_P HELX_P15 AB6 SER A 480 ? LEU A 491 ? SER A 491 LEU A 502 1 ? 12 
HELX_P HELX_P16 AB7 SER A 500 ? LEU A 505 ? SER A 511 LEU A 516 1 ? 6  
HELX_P HELX_P17 AB8 GLN A 506 ? ALA A 513 ? GLN A 517 ALA A 524 5 ? 8  
HELX_P HELX_P18 AB9 PRO A 515 ? SER A 518 ? PRO A 526 SER A 529 5 ? 4  
HELX_P HELX_P19 AC1 LEU A 519 ? ASN A 533 ? LEU A 530 ASN A 544 1 ? 15 
HELX_P HELX_P20 AC2 LYS B 245 ? VAL B 250 ? LYS B 256 VAL B 261 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 254 ? LYS B 258 ? ASP B 265 LYS B 269 1 ? 5  
HELX_P HELX_P22 AC4 LYS B 297 ? ASN B 311 ? LYS B 308 ASN B 322 1 ? 15 
HELX_P HELX_P23 AC5 SER B 340 ? THR B 348 ? SER B 351 THR B 359 1 ? 9  
HELX_P HELX_P24 AC6 ASP B 351 ? ASN B 372 ? ASP B 362 ASN B 383 1 ? 22 
HELX_P HELX_P25 AC7 LYS B 380 ? ASP B 382 ? LYS B 391 ASP B 393 5 ? 3  
HELX_P HELX_P26 AC8 ALA B 421 ? THR B 426 ? ALA B 432 THR B 437 1 ? 6  
HELX_P HELX_P27 AC9 PRO B 432 ? GLY B 449 ? PRO B 443 GLY B 460 1 ? 18 
HELX_P HELX_P28 AD1 ASN B 457 ? GLY B 469 ? ASN B 468 GLY B 480 1 ? 13 
HELX_P HELX_P29 AD2 ASN B 475 ? LEU B 479 ? ASN B 486 LEU B 490 5 ? 5  
HELX_P HELX_P30 AD3 SER B 480 ? LEU B 491 ? SER B 491 LEU B 502 1 ? 12 
HELX_P HELX_P31 AD4 SER B 500 ? LEU B 505 ? SER B 511 LEU B 516 1 ? 6  
HELX_P HELX_P32 AD5 GLN B 506 ? ALA B 513 ? GLN B 517 ALA B 524 5 ? 8  
HELX_P HELX_P33 AD6 PRO B 515 ? SER B 518 ? PRO B 526 SER B 529 5 ? 4  
HELX_P HELX_P34 AD7 LEU B 519 ? LYS B 531 ? LEU B 530 LYS B 542 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            349 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            349 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             360 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             360 
_struct_conn.ptnr2_symmetry                1_556 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.066 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       349 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      349 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        360 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       360 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_556 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? 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 SER A 251 ? VAL A 252 ? SER A 262 VAL A 263 
AA1 2 TYR A 319 ? VAL A 325 ? TYR A 330 VAL A 336 
AA1 3 GLU A 328 ? GLU A 334 ? GLU A 339 GLU A 345 
AA1 4 GLU A 284 ? ASN A 291 ? GLU A 295 ASN A 302 
AA1 5 GLY A 271 ? ASP A 278 ? GLY A 282 ASP A 289 
AA1 6 TYR A 259 ? GLY A 268 ? TYR A 270 GLY A 279 
AA2 1 VAL A 374 ? ILE A 375 ? VAL A 385 ILE A 386 
AA2 2 ALA A 401 ? GLN A 402 ? ALA A 412 GLN A 413 
AA3 1 ILE A 384 ? LEU A 386 ? ILE A 395 LEU A 397 
AA3 2 VAL A 392 ? LEU A 394 ? VAL A 403 LEU A 405 
AA4 1 TYR B 259 ? GLY B 268 ? TYR B 270 GLY B 279 
AA4 2 GLY B 271 ? ASP B 278 ? GLY B 282 ASP B 289 
AA4 3 GLU B 284 ? ASN B 291 ? GLU B 295 ASN B 302 
AA4 4 GLU B 328 ? GLU B 334 ? GLU B 339 GLU B 345 
AA4 5 TYR B 319 ? LEU B 324 ? TYR B 330 LEU B 335 
AA5 1 ILE B 384 ? LEU B 386 ? ILE B 395 LEU B 397 
AA5 2 VAL B 392 ? LEU B 394 ? VAL B 403 LEU B 405 
# 
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 SER A 251 ? N SER A 262 O LEU A 324 ? O LEU A 335 
AA1 2 3 N VAL A 325 ? N VAL A 336 O GLU A 328 ? O GLU A 339 
AA1 3 4 O MET A 333 ? O MET A 344 N ALA A 286 ? N ALA A 297 
AA1 4 5 O GLN A 289 ? O GLN A 300 N THR A 272 ? N THR A 283 
AA1 5 6 O GLY A 271 ? O GLY A 282 N GLY A 268 ? N GLY A 279 
AA2 1 2 N ILE A 375 ? N ILE A 386 O ALA A 401 ? O ALA A 412 
AA3 1 2 N LEU A 385 ? N LEU A 396 O LYS A 393 ? O LYS A 404 
AA4 1 2 N GLU B 263 ? N GLU B 274 O THR B 275 ? O THR B 286 
AA4 2 3 N THR B 272 ? N THR B 283 O GLN B 289 ? O GLN B 300 
AA4 3 4 N ALA B 286 ? N ALA B 297 O MET B 333 ? O MET B 344 
AA4 4 5 O TRP B 330 ? O TRP B 341 N TYR B 323 ? N TYR B 334 
AA5 1 2 N LEU B 385 ? N LEU B 396 O LYS B 393 ? O LYS B 404 
# 
_pdbx_entry_details.entry_id                   9N48 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 B GLU 503 ? ? O B HOH 701 ? ? 2.07 
2 1 O   A HOH 811 ? ? O A HOH 868 ? ? 2.13 
3 1 O   A HOH 880 ? ? O B HOH 867 ? ? 2.13 
4 1 OE1 A GLU 315 ? ? O A HOH 701 ? ? 2.18 
5 1 O   A HOH 853 ? ? O A HOH 854 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     826 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     826 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_545 
_pdbx_validate_symm_contact.dist              2.13 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB B LEU 303 ? ? CA B LEU 303 ? ? C  B LEU 303 ? ? 96.85  110.20 -13.35 1.90 N 
2 1 N  B LEU 303 ? ? CA B LEU 303 ? ? C  B LEU 303 ? ? 92.88  111.00 -18.12 2.70 N 
3 1 N  B GLN 304 ? ? CA B GLN 304 ? ? CB B GLN 304 ? ? 124.23 110.60 13.63  1.80 N 
4 1 N  B GLN 304 ? ? CA B GLN 304 ? ? C  B GLN 304 ? ? 89.89  111.00 -21.11 2.70 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 LYS A 308 ? ? -118.26 73.37  
2 1 ARG A 388 ? ? 72.35   -5.11  
3 1 GLN A 418 ? ? -153.55 71.63  
4 1 PRO B 307 ? ? -38.41  131.66 
5 1 ASP B 338 ? ? 53.93   13.95  
6 1 ARG B 388 ? ? 78.31   -10.52 
# 
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 22.2637 -21.7837 6.9516   0.4534 ? 0.0251  ? 0.0073  ? 0.4117 ? -0.0517 ? 0.3971 ? 3.0470 ? 0.6721 
? -1.9347 ? 2.2861 ? -0.9948 ? 4.6458 ? -0.1553 ? 0.6660  ? -0.2643 ? -0.6082 ? 0.1399  ? 0.2117  ? 0.3793  ? -0.6471 ? 0.0268  ? 
2 'X-RAY DIFFRACTION' ? refined 24.3993 0.4330   21.3910  0.1887 ? 0.0073  ? -0.0248 ? 0.1811 ? 0.0039  ? 0.1517 ? 2.2979 ? 0.2618 
? -0.9585 ? 1.6159 ? 0.1029  ? 3.0582 ? -0.0756 ? -0.0343 ? 0.0020  ? -0.0498 ? 0.0502  ? -0.1629 ? -0.1974 ? 0.3249  ? 0.0337  ? 
3 'X-RAY DIFFRACTION' ? refined -1.8572 -15.6337 -15.1976 0.4787 ? -0.0838 ? 0.1236  ? 0.3755 ? -0.0527 ? 0.4432 ? 2.3155 ? 0.0035 
? 0.4149  ? 3.7718 ? -0.8469 ? 2.6502 ? 0.0203  ? -0.3487 ? -0.0915 ? 0.9372  ? 0.0375  ? 0.5414  ? 0.1262  ? -0.2150 ? -0.0093 ? 
4 'X-RAY DIFFRACTION' ? refined 15.0082 5.5839   -16.9908 0.1424 ? 0.0103  ? -0.0200 ? 0.1540 ? -0.0211 ? 0.2132 ? 1.5252 ? 0.3798 
? -0.6756 ? 1.0988 ? 0.0325  ? 3.0530 ? -0.0325 ? -0.0857 ? 0.1638  ? 0.1315  ? -0.0330 ? 0.1545  ? 0.0316  ? -0.0543 ? 0.0675  ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 'chain A and resid 249:346' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain A and resid 347:541' 
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 'chain B and resid 255:346' 
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 'chain B and resid 347:541' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 902 ? 5.85 . 
2 1 O ? B HOH 886 ? 5.91 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 12  ? A MET 1   
2   1 Y 1 A HIS 13  ? A HIS 2   
3   1 Y 1 A HIS 14  ? A HIS 3   
4   1 Y 1 A HIS 15  ? A HIS 4   
5   1 Y 1 A HIS 16  ? A HIS 5   
6   1 Y 1 A HIS 17  ? A HIS 6   
7   1 Y 1 A HIS 18  ? A HIS 7   
8   1 Y 1 A HIS 19  ? A HIS 8   
9   1 Y 1 A HIS 20  ? A HIS 9   
10  1 Y 1 A GLY 21  ? A GLY 10  
11  1 Y 1 A SER 22  ? A SER 11  
12  1 Y 1 A PRO 23  ? A PRO 12  
13  1 Y 1 A ILE 24  ? A ILE 13  
14  1 Y 1 A LEU 25  ? A LEU 14  
15  1 Y 1 A GLY 26  ? A GLY 15  
16  1 Y 1 A TYR 27  ? A TYR 16  
17  1 Y 1 A TRP 28  ? A TRP 17  
18  1 Y 1 A LYS 29  ? A LYS 18  
19  1 Y 1 A ILE 30  ? A ILE 19  
20  1 Y 1 A LYS 31  ? A LYS 20  
21  1 Y 1 A GLY 32  ? A GLY 21  
22  1 Y 1 A LEU 33  ? A LEU 22  
23  1 Y 1 A VAL 34  ? A VAL 23  
24  1 Y 1 A GLN 35  ? A GLN 24  
25  1 Y 1 A PRO 36  ? A PRO 25  
26  1 Y 1 A THR 37  ? A THR 26  
27  1 Y 1 A ARG 38  ? A ARG 27  
28  1 Y 1 A LEU 39  ? A LEU 28  
29  1 Y 1 A LEU 40  ? A LEU 29  
30  1 Y 1 A LEU 41  ? A LEU 30  
31  1 Y 1 A GLU 42  ? A GLU 31  
32  1 Y 1 A TYR 43  ? A TYR 32  
33  1 Y 1 A LEU 44  ? A LEU 33  
34  1 Y 1 A GLU 45  ? A GLU 34  
35  1 Y 1 A GLU 46  ? A GLU 35  
36  1 Y 1 A LYS 47  ? A LYS 36  
37  1 Y 1 A TYR 48  ? A TYR 37  
38  1 Y 1 A GLU 49  ? A GLU 38  
39  1 Y 1 A GLU 50  ? A GLU 39  
40  1 Y 1 A HIS 51  ? A HIS 40  
41  1 Y 1 A LEU 52  ? A LEU 41  
42  1 Y 1 A TYR 53  ? A TYR 42  
43  1 Y 1 A GLU 54  ? A GLU 43  
44  1 Y 1 A ARG 55  ? A ARG 44  
45  1 Y 1 A ASP 56  ? A ASP 45  
46  1 Y 1 A GLU 57  ? A GLU 46  
47  1 Y 1 A GLY 58  ? A GLY 47  
48  1 Y 1 A ASP 59  ? A ASP 48  
49  1 Y 1 A LYS 60  ? A LYS 49  
50  1 Y 1 A TRP 61  ? A TRP 50  
51  1 Y 1 A ARG 62  ? A ARG 51  
52  1 Y 1 A ASN 63  ? A ASN 52  
53  1 Y 1 A LYS 64  ? A LYS 53  
54  1 Y 1 A LYS 65  ? A LYS 54  
55  1 Y 1 A PHE 66  ? A PHE 55  
56  1 Y 1 A GLU 67  ? A GLU 56  
57  1 Y 1 A LEU 68  ? A LEU 57  
58  1 Y 1 A GLY 69  ? A GLY 58  
59  1 Y 1 A LEU 70  ? A LEU 59  
60  1 Y 1 A GLU 71  ? A GLU 60  
61  1 Y 1 A PHE 72  ? A PHE 61  
62  1 Y 1 A PRO 73  ? A PRO 62  
63  1 Y 1 A ASN 74  ? A ASN 63  
64  1 Y 1 A LEU 75  ? A LEU 64  
65  1 Y 1 A PRO 76  ? A PRO 65  
66  1 Y 1 A TYR 77  ? A TYR 66  
67  1 Y 1 A TYR 78  ? A TYR 67  
68  1 Y 1 A ILE 79  ? A ILE 68  
69  1 Y 1 A ASP 80  ? A ASP 69  
70  1 Y 1 A GLY 81  ? A GLY 70  
71  1 Y 1 A ASP 82  ? A ASP 71  
72  1 Y 1 A VAL 83  ? A VAL 72  
73  1 Y 1 A LYS 84  ? A LYS 73  
74  1 Y 1 A LEU 85  ? A LEU 74  
75  1 Y 1 A THR 86  ? A THR 75  
76  1 Y 1 A GLN 87  ? A GLN 76  
77  1 Y 1 A SER 88  ? A SER 77  
78  1 Y 1 A MET 89  ? A MET 78  
79  1 Y 1 A ALA 90  ? A ALA 79  
80  1 Y 1 A ILE 91  ? A ILE 80  
81  1 Y 1 A ILE 92  ? A ILE 81  
82  1 Y 1 A ARG 93  ? A ARG 82  
83  1 Y 1 A TYR 94  ? A TYR 83  
84  1 Y 1 A ILE 95  ? A ILE 84  
85  1 Y 1 A ALA 96  ? A ALA 85  
86  1 Y 1 A ASP 97  ? A ASP 86  
87  1 Y 1 A LYS 98  ? A LYS 87  
88  1 Y 1 A HIS 99  ? A HIS 88  
89  1 Y 1 A ASN 100 ? A ASN 89  
90  1 Y 1 A MET 101 ? A MET 90  
91  1 Y 1 A LEU 102 ? A LEU 91  
92  1 Y 1 A GLY 103 ? A GLY 92  
93  1 Y 1 A GLY 104 ? A GLY 93  
94  1 Y 1 A CYS 105 ? A CYS 94  
95  1 Y 1 A PRO 106 ? A PRO 95  
96  1 Y 1 A LYS 107 ? A LYS 96  
97  1 Y 1 A GLU 108 ? A GLU 97  
98  1 Y 1 A ARG 109 ? A ARG 98  
99  1 Y 1 A ALA 110 ? A ALA 99  
100 1 Y 1 A GLU 111 ? A GLU 100 
101 1 Y 1 A ILE 112 ? A ILE 101 
102 1 Y 1 A SER 113 ? A SER 102 
103 1 Y 1 A MET 114 ? A MET 103 
104 1 Y 1 A LEU 115 ? A LEU 104 
105 1 Y 1 A GLU 116 ? A GLU 105 
106 1 Y 1 A GLY 117 ? A GLY 106 
107 1 Y 1 A ALA 118 ? A ALA 107 
108 1 Y 1 A VAL 119 ? A VAL 108 
109 1 Y 1 A LEU 120 ? A LEU 109 
110 1 Y 1 A ASP 121 ? A ASP 110 
111 1 Y 1 A ILE 122 ? A ILE 111 
112 1 Y 1 A ARG 123 ? A ARG 112 
113 1 Y 1 A TYR 124 ? A TYR 113 
114 1 Y 1 A GLY 125 ? A GLY 114 
115 1 Y 1 A VAL 126 ? A VAL 115 
116 1 Y 1 A SER 127 ? A SER 116 
117 1 Y 1 A ARG 128 ? A ARG 117 
118 1 Y 1 A ILE 129 ? A ILE 118 
119 1 Y 1 A ALA 130 ? A ALA 119 
120 1 Y 1 A TYR 131 ? A TYR 120 
121 1 Y 1 A SER 132 ? A SER 121 
122 1 Y 1 A LYS 133 ? A LYS 122 
123 1 Y 1 A ASP 134 ? A ASP 123 
124 1 Y 1 A PHE 135 ? A PHE 124 
125 1 Y 1 A GLU 136 ? A GLU 125 
126 1 Y 1 A THR 137 ? A THR 126 
127 1 Y 1 A LEU 138 ? A LEU 127 
128 1 Y 1 A LYS 139 ? A LYS 128 
129 1 Y 1 A VAL 140 ? A VAL 129 
130 1 Y 1 A ASP 141 ? A ASP 130 
131 1 Y 1 A PHE 142 ? A PHE 131 
132 1 Y 1 A LEU 143 ? A LEU 132 
133 1 Y 1 A SER 144 ? A SER 133 
134 1 Y 1 A LYS 145 ? A LYS 134 
135 1 Y 1 A LEU 146 ? A LEU 135 
136 1 Y 1 A PRO 147 ? A PRO 136 
137 1 Y 1 A GLU 148 ? A GLU 137 
138 1 Y 1 A MET 149 ? A MET 138 
139 1 Y 1 A LEU 150 ? A LEU 139 
140 1 Y 1 A LYS 151 ? A LYS 140 
141 1 Y 1 A MET 152 ? A MET 141 
142 1 Y 1 A PHE 153 ? A PHE 142 
143 1 Y 1 A LYS 154 ? A LYS 143 
144 1 Y 1 A ASP 155 ? A ASP 144 
145 1 Y 1 A ARG 156 ? A ARG 145 
146 1 Y 1 A LEU 157 ? A LEU 146 
147 1 Y 1 A CYS 158 ? A CYS 147 
148 1 Y 1 A HIS 159 ? A HIS 148 
149 1 Y 1 A LYS 160 ? A LYS 149 
150 1 Y 1 A THR 161 ? A THR 150 
151 1 Y 1 A TYR 162 ? A TYR 151 
152 1 Y 1 A LEU 163 ? A LEU 152 
153 1 Y 1 A ASN 164 ? A ASN 153 
154 1 Y 1 A GLY 165 ? A GLY 154 
155 1 Y 1 A ASP 166 ? A ASP 155 
156 1 Y 1 A HIS 167 ? A HIS 156 
157 1 Y 1 A VAL 168 ? A VAL 157 
158 1 Y 1 A THR 169 ? A THR 158 
159 1 Y 1 A HIS 170 ? A HIS 159 
160 1 Y 1 A PRO 171 ? A PRO 160 
161 1 Y 1 A ASP 172 ? A ASP 161 
162 1 Y 1 A PHE 173 ? A PHE 162 
163 1 Y 1 A MET 174 ? A MET 163 
164 1 Y 1 A LEU 175 ? A LEU 164 
165 1 Y 1 A TYR 176 ? A TYR 165 
166 1 Y 1 A ASP 177 ? A ASP 166 
167 1 Y 1 A ALA 178 ? A ALA 167 
168 1 Y 1 A LEU 179 ? A LEU 168 
169 1 Y 1 A ASP 180 ? A ASP 169 
170 1 Y 1 A VAL 181 ? A VAL 170 
171 1 Y 1 A VAL 182 ? A VAL 171 
172 1 Y 1 A LEU 183 ? A LEU 172 
173 1 Y 1 A TYR 184 ? A TYR 173 
174 1 Y 1 A MET 185 ? A MET 174 
175 1 Y 1 A ASP 186 ? A ASP 175 
176 1 Y 1 A PRO 187 ? A PRO 176 
177 1 Y 1 A MET 188 ? A MET 177 
178 1 Y 1 A CYS 189 ? A CYS 178 
179 1 Y 1 A LEU 190 ? A LEU 179 
180 1 Y 1 A ASP 191 ? A ASP 180 
181 1 Y 1 A ALA 192 ? A ALA 181 
182 1 Y 1 A PHE 193 ? A PHE 182 
183 1 Y 1 A PRO 194 ? A PRO 183 
184 1 Y 1 A LYS 195 ? A LYS 184 
185 1 Y 1 A LEU 196 ? A LEU 185 
186 1 Y 1 A VAL 197 ? A VAL 186 
187 1 Y 1 A CYS 198 ? A CYS 187 
188 1 Y 1 A PHE 199 ? A PHE 188 
189 1 Y 1 A LYS 200 ? A LYS 189 
190 1 Y 1 A LYS 201 ? A LYS 190 
191 1 Y 1 A ARG 202 ? A ARG 191 
192 1 Y 1 A ILE 203 ? A ILE 192 
193 1 Y 1 A GLU 204 ? A GLU 193 
194 1 Y 1 A ALA 205 ? A ALA 194 
195 1 Y 1 A ILE 206 ? A ILE 195 
196 1 Y 1 A PRO 207 ? A PRO 196 
197 1 Y 1 A GLN 208 ? A GLN 197 
198 1 Y 1 A ILE 209 ? A ILE 198 
199 1 Y 1 A ASP 210 ? A ASP 199 
200 1 Y 1 A LYS 211 ? A LYS 200 
201 1 Y 1 A TYR 212 ? A TYR 201 
202 1 Y 1 A LEU 213 ? A LEU 202 
203 1 Y 1 A LYS 214 ? A LYS 203 
204 1 Y 1 A SER 215 ? A SER 204 
205 1 Y 1 A SER 216 ? A SER 205 
206 1 Y 1 A LYS 217 ? A LYS 206 
207 1 Y 1 A TYR 218 ? A TYR 207 
208 1 Y 1 A ILE 219 ? A ILE 208 
209 1 Y 1 A ALA 220 ? A ALA 209 
210 1 Y 1 A TRP 221 ? A TRP 210 
211 1 Y 1 A PRO 222 ? A PRO 211 
212 1 Y 1 A LEU 223 ? A LEU 212 
213 1 Y 1 A GLN 224 ? A GLN 213 
214 1 Y 1 A GLY 225 ? A GLY 214 
215 1 Y 1 A TRP 226 ? A TRP 215 
216 1 Y 1 A GLN 227 ? A GLN 216 
217 1 Y 1 A ALA 228 ? A ALA 217 
218 1 Y 1 A THR 229 ? A THR 218 
219 1 Y 1 A PHE 230 ? A PHE 219 
220 1 Y 1 A GLY 231 ? A GLY 220 
221 1 Y 1 A GLY 232 ? A GLY 221 
222 1 Y 1 A GLY 233 ? A GLY 222 
223 1 Y 1 A ASP 234 ? A ASP 223 
224 1 Y 1 A HIS 235 ? A HIS 224 
225 1 Y 1 A PRO 236 ? A PRO 225 
226 1 Y 1 A PRO 237 ? A PRO 226 
227 1 Y 1 A LYS 238 ? A LYS 227 
228 1 Y 1 A SER 239 ? A SER 228 
229 1 Y 1 A ASP 240 ? A ASP 229 
230 1 Y 1 A GLY 241 ? A GLY 230 
231 1 Y 1 A GLU 242 ? A GLU 231 
232 1 Y 1 A ASN 243 ? A ASN 232 
233 1 Y 1 A LEU 244 ? A LEU 233 
234 1 Y 1 A TYR 245 ? A TYR 234 
235 1 Y 1 A PHE 246 ? A PHE 235 
236 1 Y 1 A GLN 247 ? A GLN 236 
237 1 Y 1 A GLY 248 ? A GLY 237 
238 1 Y 1 A GLY 546 ? A GLY 535 
239 1 Y 1 A ASN 547 ? A ASN 536 
240 1 Y 1 A SER 548 ? A SER 537 
241 1 Y 1 B MET 12  ? B MET 1   
242 1 Y 1 B HIS 13  ? B HIS 2   
243 1 Y 1 B HIS 14  ? B HIS 3   
244 1 Y 1 B HIS 15  ? B HIS 4   
245 1 Y 1 B HIS 16  ? B HIS 5   
246 1 Y 1 B HIS 17  ? B HIS 6   
247 1 Y 1 B HIS 18  ? B HIS 7   
248 1 Y 1 B HIS 19  ? B HIS 8   
249 1 Y 1 B HIS 20  ? B HIS 9   
250 1 Y 1 B GLY 21  ? B GLY 10  
251 1 Y 1 B SER 22  ? B SER 11  
252 1 Y 1 B PRO 23  ? B PRO 12  
253 1 Y 1 B ILE 24  ? B ILE 13  
254 1 Y 1 B LEU 25  ? B LEU 14  
255 1 Y 1 B GLY 26  ? B GLY 15  
256 1 Y 1 B TYR 27  ? B TYR 16  
257 1 Y 1 B TRP 28  ? B TRP 17  
258 1 Y 1 B LYS 29  ? B LYS 18  
259 1 Y 1 B ILE 30  ? B ILE 19  
260 1 Y 1 B LYS 31  ? B LYS 20  
261 1 Y 1 B GLY 32  ? B GLY 21  
262 1 Y 1 B LEU 33  ? B LEU 22  
263 1 Y 1 B VAL 34  ? B VAL 23  
264 1 Y 1 B GLN 35  ? B GLN 24  
265 1 Y 1 B PRO 36  ? B PRO 25  
266 1 Y 1 B THR 37  ? B THR 26  
267 1 Y 1 B ARG 38  ? B ARG 27  
268 1 Y 1 B LEU 39  ? B LEU 28  
269 1 Y 1 B LEU 40  ? B LEU 29  
270 1 Y 1 B LEU 41  ? B LEU 30  
271 1 Y 1 B GLU 42  ? B GLU 31  
272 1 Y 1 B TYR 43  ? B TYR 32  
273 1 Y 1 B LEU 44  ? B LEU 33  
274 1 Y 1 B GLU 45  ? B GLU 34  
275 1 Y 1 B GLU 46  ? B GLU 35  
276 1 Y 1 B LYS 47  ? B LYS 36  
277 1 Y 1 B TYR 48  ? B TYR 37  
278 1 Y 1 B GLU 49  ? B GLU 38  
279 1 Y 1 B GLU 50  ? B GLU 39  
280 1 Y 1 B HIS 51  ? B HIS 40  
281 1 Y 1 B LEU 52  ? B LEU 41  
282 1 Y 1 B TYR 53  ? B TYR 42  
283 1 Y 1 B GLU 54  ? B GLU 43  
284 1 Y 1 B ARG 55  ? B ARG 44  
285 1 Y 1 B ASP 56  ? B ASP 45  
286 1 Y 1 B GLU 57  ? B GLU 46  
287 1 Y 1 B GLY 58  ? B GLY 47  
288 1 Y 1 B ASP 59  ? B ASP 48  
289 1 Y 1 B LYS 60  ? B LYS 49  
290 1 Y 1 B TRP 61  ? B TRP 50  
291 1 Y 1 B ARG 62  ? B ARG 51  
292 1 Y 1 B ASN 63  ? B ASN 52  
293 1 Y 1 B LYS 64  ? B LYS 53  
294 1 Y 1 B LYS 65  ? B LYS 54  
295 1 Y 1 B PHE 66  ? B PHE 55  
296 1 Y 1 B GLU 67  ? B GLU 56  
297 1 Y 1 B LEU 68  ? B LEU 57  
298 1 Y 1 B GLY 69  ? B GLY 58  
299 1 Y 1 B LEU 70  ? B LEU 59  
300 1 Y 1 B GLU 71  ? B GLU 60  
301 1 Y 1 B PHE 72  ? B PHE 61  
302 1 Y 1 B PRO 73  ? B PRO 62  
303 1 Y 1 B ASN 74  ? B ASN 63  
304 1 Y 1 B LEU 75  ? B LEU 64  
305 1 Y 1 B PRO 76  ? B PRO 65  
306 1 Y 1 B TYR 77  ? B TYR 66  
307 1 Y 1 B TYR 78  ? B TYR 67  
308 1 Y 1 B ILE 79  ? B ILE 68  
309 1 Y 1 B ASP 80  ? B ASP 69  
310 1 Y 1 B GLY 81  ? B GLY 70  
311 1 Y 1 B ASP 82  ? B ASP 71  
312 1 Y 1 B VAL 83  ? B VAL 72  
313 1 Y 1 B LYS 84  ? B LYS 73  
314 1 Y 1 B LEU 85  ? B LEU 74  
315 1 Y 1 B THR 86  ? B THR 75  
316 1 Y 1 B GLN 87  ? B GLN 76  
317 1 Y 1 B SER 88  ? B SER 77  
318 1 Y 1 B MET 89  ? B MET 78  
319 1 Y 1 B ALA 90  ? B ALA 79  
320 1 Y 1 B ILE 91  ? B ILE 80  
321 1 Y 1 B ILE 92  ? B ILE 81  
322 1 Y 1 B ARG 93  ? B ARG 82  
323 1 Y 1 B TYR 94  ? B TYR 83  
324 1 Y 1 B ILE 95  ? B ILE 84  
325 1 Y 1 B ALA 96  ? B ALA 85  
326 1 Y 1 B ASP 97  ? B ASP 86  
327 1 Y 1 B LYS 98  ? B LYS 87  
328 1 Y 1 B HIS 99  ? B HIS 88  
329 1 Y 1 B ASN 100 ? B ASN 89  
330 1 Y 1 B MET 101 ? B MET 90  
331 1 Y 1 B LEU 102 ? B LEU 91  
332 1 Y 1 B GLY 103 ? B GLY 92  
333 1 Y 1 B GLY 104 ? B GLY 93  
334 1 Y 1 B CYS 105 ? B CYS 94  
335 1 Y 1 B PRO 106 ? B PRO 95  
336 1 Y 1 B LYS 107 ? B LYS 96  
337 1 Y 1 B GLU 108 ? B GLU 97  
338 1 Y 1 B ARG 109 ? B ARG 98  
339 1 Y 1 B ALA 110 ? B ALA 99  
340 1 Y 1 B GLU 111 ? B GLU 100 
341 1 Y 1 B ILE 112 ? B ILE 101 
342 1 Y 1 B SER 113 ? B SER 102 
343 1 Y 1 B MET 114 ? B MET 103 
344 1 Y 1 B LEU 115 ? B LEU 104 
345 1 Y 1 B GLU 116 ? B GLU 105 
346 1 Y 1 B GLY 117 ? B GLY 106 
347 1 Y 1 B ALA 118 ? B ALA 107 
348 1 Y 1 B VAL 119 ? B VAL 108 
349 1 Y 1 B LEU 120 ? B LEU 109 
350 1 Y 1 B ASP 121 ? B ASP 110 
351 1 Y 1 B ILE 122 ? B ILE 111 
352 1 Y 1 B ARG 123 ? B ARG 112 
353 1 Y 1 B TYR 124 ? B TYR 113 
354 1 Y 1 B GLY 125 ? B GLY 114 
355 1 Y 1 B VAL 126 ? B VAL 115 
356 1 Y 1 B SER 127 ? B SER 116 
357 1 Y 1 B ARG 128 ? B ARG 117 
358 1 Y 1 B ILE 129 ? B ILE 118 
359 1 Y 1 B ALA 130 ? B ALA 119 
360 1 Y 1 B TYR 131 ? B TYR 120 
361 1 Y 1 B SER 132 ? B SER 121 
362 1 Y 1 B LYS 133 ? B LYS 122 
363 1 Y 1 B ASP 134 ? B ASP 123 
364 1 Y 1 B PHE 135 ? B PHE 124 
365 1 Y 1 B GLU 136 ? B GLU 125 
366 1 Y 1 B THR 137 ? B THR 126 
367 1 Y 1 B LEU 138 ? B LEU 127 
368 1 Y 1 B LYS 139 ? B LYS 128 
369 1 Y 1 B VAL 140 ? B VAL 129 
370 1 Y 1 B ASP 141 ? B ASP 130 
371 1 Y 1 B PHE 142 ? B PHE 131 
372 1 Y 1 B LEU 143 ? B LEU 132 
373 1 Y 1 B SER 144 ? B SER 133 
374 1 Y 1 B LYS 145 ? B LYS 134 
375 1 Y 1 B LEU 146 ? B LEU 135 
376 1 Y 1 B PRO 147 ? B PRO 136 
377 1 Y 1 B GLU 148 ? B GLU 137 
378 1 Y 1 B MET 149 ? B MET 138 
379 1 Y 1 B LEU 150 ? B LEU 139 
380 1 Y 1 B LYS 151 ? B LYS 140 
381 1 Y 1 B MET 152 ? B MET 141 
382 1 Y 1 B PHE 153 ? B PHE 142 
383 1 Y 1 B LYS 154 ? B LYS 143 
384 1 Y 1 B ASP 155 ? B ASP 144 
385 1 Y 1 B ARG 156 ? B ARG 145 
386 1 Y 1 B LEU 157 ? B LEU 146 
387 1 Y 1 B CYS 158 ? B CYS 147 
388 1 Y 1 B HIS 159 ? B HIS 148 
389 1 Y 1 B LYS 160 ? B LYS 149 
390 1 Y 1 B THR 161 ? B THR 150 
391 1 Y 1 B TYR 162 ? B TYR 151 
392 1 Y 1 B LEU 163 ? B LEU 152 
393 1 Y 1 B ASN 164 ? B ASN 153 
394 1 Y 1 B GLY 165 ? B GLY 154 
395 1 Y 1 B ASP 166 ? B ASP 155 
396 1 Y 1 B HIS 167 ? B HIS 156 
397 1 Y 1 B VAL 168 ? B VAL 157 
398 1 Y 1 B THR 169 ? B THR 158 
399 1 Y 1 B HIS 170 ? B HIS 159 
400 1 Y 1 B PRO 171 ? B PRO 160 
401 1 Y 1 B ASP 172 ? B ASP 161 
402 1 Y 1 B PHE 173 ? B PHE 162 
403 1 Y 1 B MET 174 ? B MET 163 
404 1 Y 1 B LEU 175 ? B LEU 164 
405 1 Y 1 B TYR 176 ? B TYR 165 
406 1 Y 1 B ASP 177 ? B ASP 166 
407 1 Y 1 B ALA 178 ? B ALA 167 
408 1 Y 1 B LEU 179 ? B LEU 168 
409 1 Y 1 B ASP 180 ? B ASP 169 
410 1 Y 1 B VAL 181 ? B VAL 170 
411 1 Y 1 B VAL 182 ? B VAL 171 
412 1 Y 1 B LEU 183 ? B LEU 172 
413 1 Y 1 B TYR 184 ? B TYR 173 
414 1 Y 1 B MET 185 ? B MET 174 
415 1 Y 1 B ASP 186 ? B ASP 175 
416 1 Y 1 B PRO 187 ? B PRO 176 
417 1 Y 1 B MET 188 ? B MET 177 
418 1 Y 1 B CYS 189 ? B CYS 178 
419 1 Y 1 B LEU 190 ? B LEU 179 
420 1 Y 1 B ASP 191 ? B ASP 180 
421 1 Y 1 B ALA 192 ? B ALA 181 
422 1 Y 1 B PHE 193 ? B PHE 182 
423 1 Y 1 B PRO 194 ? B PRO 183 
424 1 Y 1 B LYS 195 ? B LYS 184 
425 1 Y 1 B LEU 196 ? B LEU 185 
426 1 Y 1 B VAL 197 ? B VAL 186 
427 1 Y 1 B CYS 198 ? B CYS 187 
428 1 Y 1 B PHE 199 ? B PHE 188 
429 1 Y 1 B LYS 200 ? B LYS 189 
430 1 Y 1 B LYS 201 ? B LYS 190 
431 1 Y 1 B ARG 202 ? B ARG 191 
432 1 Y 1 B ILE 203 ? B ILE 192 
433 1 Y 1 B GLU 204 ? B GLU 193 
434 1 Y 1 B ALA 205 ? B ALA 194 
435 1 Y 1 B ILE 206 ? B ILE 195 
436 1 Y 1 B PRO 207 ? B PRO 196 
437 1 Y 1 B GLN 208 ? B GLN 197 
438 1 Y 1 B ILE 209 ? B ILE 198 
439 1 Y 1 B ASP 210 ? B ASP 199 
440 1 Y 1 B LYS 211 ? B LYS 200 
441 1 Y 1 B TYR 212 ? B TYR 201 
442 1 Y 1 B LEU 213 ? B LEU 202 
443 1 Y 1 B LYS 214 ? B LYS 203 
444 1 Y 1 B SER 215 ? B SER 204 
445 1 Y 1 B SER 216 ? B SER 205 
446 1 Y 1 B LYS 217 ? B LYS 206 
447 1 Y 1 B TYR 218 ? B TYR 207 
448 1 Y 1 B ILE 219 ? B ILE 208 
449 1 Y 1 B ALA 220 ? B ALA 209 
450 1 Y 1 B TRP 221 ? B TRP 210 
451 1 Y 1 B PRO 222 ? B PRO 211 
452 1 Y 1 B LEU 223 ? B LEU 212 
453 1 Y 1 B GLN 224 ? B GLN 213 
454 1 Y 1 B GLY 225 ? B GLY 214 
455 1 Y 1 B TRP 226 ? B TRP 215 
456 1 Y 1 B GLN 227 ? B GLN 216 
457 1 Y 1 B ALA 228 ? B ALA 217 
458 1 Y 1 B THR 229 ? B THR 218 
459 1 Y 1 B PHE 230 ? B PHE 219 
460 1 Y 1 B GLY 231 ? B GLY 220 
461 1 Y 1 B GLY 232 ? B GLY 221 
462 1 Y 1 B GLY 233 ? B GLY 222 
463 1 Y 1 B ASP 234 ? B ASP 223 
464 1 Y 1 B HIS 235 ? B HIS 224 
465 1 Y 1 B PRO 236 ? B PRO 225 
466 1 Y 1 B PRO 237 ? B PRO 226 
467 1 Y 1 B LYS 238 ? B LYS 227 
468 1 Y 1 B SER 239 ? B SER 228 
469 1 Y 1 B ASP 240 ? B ASP 229 
470 1 Y 1 B GLY 241 ? B GLY 230 
471 1 Y 1 B GLU 242 ? B GLU 231 
472 1 Y 1 B ASN 243 ? B ASN 232 
473 1 Y 1 B LEU 244 ? B LEU 233 
474 1 Y 1 B TYR 245 ? B TYR 234 
475 1 Y 1 B PHE 246 ? B PHE 235 
476 1 Y 1 B GLN 247 ? B GLN 236 
477 1 Y 1 B GLY 248 ? B GLY 237 
478 1 Y 1 B SER 249 ? B SER 238 
479 1 Y 1 B ASP 250 ? B ASP 239 
480 1 Y 1 B GLU 251 ? B GLU 240 
481 1 Y 1 B GLU 252 ? B GLU 241 
482 1 Y 1 B ILE 253 ? B ILE 242 
483 1 Y 1 B LEU 254 ? B LEU 243 
484 1 Y 1 B CYS 411 ? B CYS 400 
485 1 Y 1 B ALA 412 ? B ALA 401 
486 1 Y 1 B GLN 413 ? B GLN 402 
487 1 Y 1 B ILE 414 ? B ILE 403 
488 1 Y 1 B THR 415 ? B THR 404 
489 1 Y 1 B PRO 416 ? B PRO 405 
490 1 Y 1 B GLU 417 ? B GLU 406 
491 1 Y 1 B GLN 418 ? B GLN 407 
492 1 Y 1 B ASN 543 ? B ASN 532 
493 1 Y 1 B ASN 544 ? B ASN 533 
494 1 Y 1 B HIS 545 ? B HIS 534 
495 1 Y 1 B GLY 546 ? B GLY 535 
496 1 Y 1 B ASN 547 ? B ASN 536 
497 1 Y 1 B SER 548 ? B SER 537 
# 
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 
A1BV1 N3   N  N N 1   
A1BV1 C4   C  Y N 2   
A1BV1 C6   C  Y N 3   
A1BV1 C7   C  Y N 4   
A1BV1 C8   C  N N 5   
A1BV1 C10  C  N N 6   
A1BV1 N12  N  N N 7   
A1BV1 C13  C  Y N 8   
A1BV1 C15  C  N N 9   
A1BV1 C21  C  Y N 10  
A1BV1 C22  C  Y N 11  
A1BV1 C24  C  Y N 12  
A1BV1 C26  C  Y N 13  
A1BV1 C1   C  N N 14  
A1BV1 C16  C  N N 15  
A1BV1 C18  C  N N 16  
A1BV1 C19  C  N N 17  
A1BV1 C2   C  N N 18  
A1BV1 C23  C  Y N 19  
A1BV1 C25  C  Y N 20  
A1BV1 C30  C  N N 21  
A1BV1 C31  C  N N 22  
A1BV1 C32  C  N N 23  
A1BV1 C33  C  N N 24  
A1BV1 C9   C  N N 25  
A1BV1 F28  F  N N 26  
A1BV1 N14  N  Y N 27  
A1BV1 N20  N  N N 28  
A1BV1 N29  N  N N 29  
A1BV1 N5   N  Y N 30  
A1BV1 O11  O  N N 31  
A1BV1 O17  O  N N 32  
A1BV1 O34  O  N N 33  
A1BV1 CL27 CL N N 34  
A1BV1 H1   H  N N 35  
A1BV1 H2   H  N N 36  
A1BV1 H3   H  N N 37  
A1BV1 H4   H  N N 38  
A1BV1 H5   H  N N 39  
A1BV1 H6   H  N N 40  
A1BV1 H7   H  N N 41  
A1BV1 H8   H  N N 42  
A1BV1 H9   H  N N 43  
A1BV1 H10  H  N N 44  
A1BV1 H11  H  N N 45  
A1BV1 H12  H  N N 46  
A1BV1 H13  H  N N 47  
A1BV1 H14  H  N N 48  
A1BV1 H15  H  N N 49  
A1BV1 H16  H  N N 50  
A1BV1 H17  H  N N 51  
A1BV1 H18  H  N N 52  
A1BV1 H19  H  N N 53  
A1BV1 H20  H  N N 54  
A1BV1 H21  H  N N 55  
A1BV1 H22  H  N N 56  
A1BV1 H23  H  N N 57  
A1BV1 H24  H  N N 58  
A1BV1 H25  H  N N 59  
A1BV1 H26  H  N N 60  
ALA   N    N  N N 61  
ALA   CA   C  N S 62  
ALA   C    C  N N 63  
ALA   O    O  N N 64  
ALA   CB   C  N N 65  
ALA   OXT  O  N N 66  
ALA   H    H  N N 67  
ALA   H2   H  N N 68  
ALA   HA   H  N N 69  
ALA   HB1  H  N N 70  
ALA   HB2  H  N N 71  
ALA   HB3  H  N N 72  
ALA   HXT  H  N N 73  
ARG   N    N  N N 74  
ARG   CA   C  N S 75  
ARG   C    C  N N 76  
ARG   O    O  N N 77  
ARG   CB   C  N N 78  
ARG   CG   C  N N 79  
ARG   CD   C  N N 80  
ARG   NE   N  N N 81  
ARG   CZ   C  N N 82  
ARG   NH1  N  N N 83  
ARG   NH2  N  N N 84  
ARG   OXT  O  N N 85  
ARG   H    H  N N 86  
ARG   H2   H  N N 87  
ARG   HA   H  N N 88  
ARG   HB2  H  N N 89  
ARG   HB3  H  N N 90  
ARG   HG2  H  N N 91  
ARG   HG3  H  N N 92  
ARG   HD2  H  N N 93  
ARG   HD3  H  N N 94  
ARG   HE   H  N N 95  
ARG   HH11 H  N N 96  
ARG   HH12 H  N N 97  
ARG   HH21 H  N N 98  
ARG   HH22 H  N N 99  
ARG   HXT  H  N N 100 
ASN   N    N  N N 101 
ASN   CA   C  N S 102 
ASN   C    C  N N 103 
ASN   O    O  N N 104 
ASN   CB   C  N N 105 
ASN   CG   C  N N 106 
ASN   OD1  O  N N 107 
ASN   ND2  N  N N 108 
ASN   OXT  O  N N 109 
ASN   H    H  N N 110 
ASN   H2   H  N N 111 
ASN   HA   H  N N 112 
ASN   HB2  H  N N 113 
ASN   HB3  H  N N 114 
ASN   HD21 H  N N 115 
ASN   HD22 H  N N 116 
ASN   HXT  H  N N 117 
ASP   N    N  N N 118 
ASP   CA   C  N S 119 
ASP   C    C  N N 120 
ASP   O    O  N N 121 
ASP   CB   C  N N 122 
ASP   CG   C  N N 123 
ASP   OD1  O  N N 124 
ASP   OD2  O  N N 125 
ASP   OXT  O  N N 126 
ASP   H    H  N N 127 
ASP   H2   H  N N 128 
ASP   HA   H  N N 129 
ASP   HB2  H  N N 130 
ASP   HB3  H  N N 131 
ASP   HD2  H  N N 132 
ASP   HXT  H  N N 133 
CYS   N    N  N N 134 
CYS   CA   C  N R 135 
CYS   C    C  N N 136 
CYS   O    O  N N 137 
CYS   CB   C  N N 138 
CYS   SG   S  N N 139 
CYS   OXT  O  N N 140 
CYS   H    H  N N 141 
CYS   H2   H  N N 142 
CYS   HA   H  N N 143 
CYS   HB2  H  N N 144 
CYS   HB3  H  N N 145 
CYS   HG   H  N N 146 
CYS   HXT  H  N N 147 
GLN   N    N  N N 148 
GLN   CA   C  N S 149 
GLN   C    C  N N 150 
GLN   O    O  N N 151 
GLN   CB   C  N N 152 
GLN   CG   C  N N 153 
GLN   CD   C  N N 154 
GLN   OE1  O  N N 155 
GLN   NE2  N  N N 156 
GLN   OXT  O  N N 157 
GLN   H    H  N N 158 
GLN   H2   H  N N 159 
GLN   HA   H  N N 160 
GLN   HB2  H  N N 161 
GLN   HB3  H  N N 162 
GLN   HG2  H  N N 163 
GLN   HG3  H  N N 164 
GLN   HE21 H  N N 165 
GLN   HE22 H  N N 166 
GLN   HXT  H  N N 167 
GLU   N    N  N N 168 
GLU   CA   C  N S 169 
GLU   C    C  N N 170 
GLU   O    O  N N 171 
GLU   CB   C  N N 172 
GLU   CG   C  N N 173 
GLU   CD   C  N N 174 
GLU   OE1  O  N N 175 
GLU   OE2  O  N N 176 
GLU   OXT  O  N N 177 
GLU   H    H  N N 178 
GLU   H2   H  N N 179 
GLU   HA   H  N N 180 
GLU   HB2  H  N N 181 
GLU   HB3  H  N N 182 
GLU   HG2  H  N N 183 
GLU   HG3  H  N N 184 
GLU   HE2  H  N N 185 
GLU   HXT  H  N N 186 
GLY   N    N  N N 187 
GLY   CA   C  N N 188 
GLY   C    C  N N 189 
GLY   O    O  N N 190 
GLY   OXT  O  N N 191 
GLY   H    H  N N 192 
GLY   H2   H  N N 193 
GLY   HA2  H  N N 194 
GLY   HA3  H  N N 195 
GLY   HXT  H  N N 196 
HIS   N    N  N N 197 
HIS   CA   C  N S 198 
HIS   C    C  N N 199 
HIS   O    O  N N 200 
HIS   CB   C  N N 201 
HIS   CG   C  Y N 202 
HIS   ND1  N  Y N 203 
HIS   CD2  C  Y N 204 
HIS   CE1  C  Y N 205 
HIS   NE2  N  Y N 206 
HIS   OXT  O  N N 207 
HIS   H    H  N N 208 
HIS   H2   H  N N 209 
HIS   HA   H  N N 210 
HIS   HB2  H  N N 211 
HIS   HB3  H  N N 212 
HIS   HD1  H  N N 213 
HIS   HD2  H  N N 214 
HIS   HE1  H  N N 215 
HIS   HE2  H  N N 216 
HIS   HXT  H  N N 217 
HOH   O    O  N N 218 
HOH   H1   H  N N 219 
HOH   H2   H  N N 220 
ILE   N    N  N N 221 
ILE   CA   C  N S 222 
ILE   C    C  N N 223 
ILE   O    O  N N 224 
ILE   CB   C  N S 225 
ILE   CG1  C  N N 226 
ILE   CG2  C  N N 227 
ILE   CD1  C  N N 228 
ILE   OXT  O  N N 229 
ILE   H    H  N N 230 
ILE   H2   H  N N 231 
ILE   HA   H  N N 232 
ILE   HB   H  N N 233 
ILE   HG12 H  N N 234 
ILE   HG13 H  N N 235 
ILE   HG21 H  N N 236 
ILE   HG22 H  N N 237 
ILE   HG23 H  N N 238 
ILE   HD11 H  N N 239 
ILE   HD12 H  N N 240 
ILE   HD13 H  N N 241 
ILE   HXT  H  N N 242 
LEU   N    N  N N 243 
LEU   CA   C  N S 244 
LEU   C    C  N N 245 
LEU   O    O  N N 246 
LEU   CB   C  N N 247 
LEU   CG   C  N N 248 
LEU   CD1  C  N N 249 
LEU   CD2  C  N N 250 
LEU   OXT  O  N N 251 
LEU   H    H  N N 252 
LEU   H2   H  N N 253 
LEU   HA   H  N N 254 
LEU   HB2  H  N N 255 
LEU   HB3  H  N N 256 
LEU   HG   H  N N 257 
LEU   HD11 H  N N 258 
LEU   HD12 H  N N 259 
LEU   HD13 H  N N 260 
LEU   HD21 H  N N 261 
LEU   HD22 H  N N 262 
LEU   HD23 H  N N 263 
LEU   HXT  H  N N 264 
LYS   N    N  N N 265 
LYS   CA   C  N S 266 
LYS   C    C  N N 267 
LYS   O    O  N N 268 
LYS   CB   C  N N 269 
LYS   CG   C  N N 270 
LYS   CD   C  N N 271 
LYS   CE   C  N N 272 
LYS   NZ   N  N N 273 
LYS   OXT  O  N N 274 
LYS   H    H  N N 275 
LYS   H2   H  N N 276 
LYS   HA   H  N N 277 
LYS   HB2  H  N N 278 
LYS   HB3  H  N N 279 
LYS   HG2  H  N N 280 
LYS   HG3  H  N N 281 
LYS   HD2  H  N N 282 
LYS   HD3  H  N N 283 
LYS   HE2  H  N N 284 
LYS   HE3  H  N N 285 
LYS   HZ1  H  N N 286 
LYS   HZ2  H  N N 287 
LYS   HZ3  H  N N 288 
LYS   HXT  H  N N 289 
MET   N    N  N N 290 
MET   CA   C  N S 291 
MET   C    C  N N 292 
MET   O    O  N N 293 
MET   CB   C  N N 294 
MET   CG   C  N N 295 
MET   SD   S  N N 296 
MET   CE   C  N N 297 
MET   OXT  O  N N 298 
MET   H    H  N N 299 
MET   H2   H  N N 300 
MET   HA   H  N N 301 
MET   HB2  H  N N 302 
MET   HB3  H  N N 303 
MET   HG2  H  N N 304 
MET   HG3  H  N N 305 
MET   HE1  H  N N 306 
MET   HE2  H  N N 307 
MET   HE3  H  N N 308 
MET   HXT  H  N N 309 
PHE   N    N  N N 310 
PHE   CA   C  N S 311 
PHE   C    C  N N 312 
PHE   O    O  N N 313 
PHE   CB   C  N N 314 
PHE   CG   C  Y N 315 
PHE   CD1  C  Y N 316 
PHE   CD2  C  Y N 317 
PHE   CE1  C  Y N 318 
PHE   CE2  C  Y N 319 
PHE   CZ   C  Y N 320 
PHE   OXT  O  N N 321 
PHE   H    H  N N 322 
PHE   H2   H  N N 323 
PHE   HA   H  N N 324 
PHE   HB2  H  N N 325 
PHE   HB3  H  N N 326 
PHE   HD1  H  N N 327 
PHE   HD2  H  N N 328 
PHE   HE1  H  N N 329 
PHE   HE2  H  N N 330 
PHE   HZ   H  N N 331 
PHE   HXT  H  N N 332 
PRO   N    N  N N 333 
PRO   CA   C  N S 334 
PRO   C    C  N N 335 
PRO   O    O  N N 336 
PRO   CB   C  N N 337 
PRO   CG   C  N N 338 
PRO   CD   C  N N 339 
PRO   OXT  O  N N 340 
PRO   H    H  N N 341 
PRO   HA   H  N N 342 
PRO   HB2  H  N N 343 
PRO   HB3  H  N N 344 
PRO   HG2  H  N N 345 
PRO   HG3  H  N N 346 
PRO   HD2  H  N N 347 
PRO   HD3  H  N N 348 
PRO   HXT  H  N N 349 
SER   N    N  N N 350 
SER   CA   C  N S 351 
SER   C    C  N N 352 
SER   O    O  N N 353 
SER   CB   C  N N 354 
SER   OG   O  N N 355 
SER   OXT  O  N N 356 
SER   H    H  N N 357 
SER   H2   H  N N 358 
SER   HA   H  N N 359 
SER   HB2  H  N N 360 
SER   HB3  H  N N 361 
SER   HG   H  N N 362 
SER   HXT  H  N N 363 
THR   N    N  N N 364 
THR   CA   C  N S 365 
THR   C    C  N N 366 
THR   O    O  N N 367 
THR   CB   C  N R 368 
THR   OG1  O  N N 369 
THR   CG2  C  N N 370 
THR   OXT  O  N N 371 
THR   H    H  N N 372 
THR   H2   H  N N 373 
THR   HA   H  N N 374 
THR   HB   H  N N 375 
THR   HG1  H  N N 376 
THR   HG21 H  N N 377 
THR   HG22 H  N N 378 
THR   HG23 H  N N 379 
THR   HXT  H  N N 380 
TRP   N    N  N N 381 
TRP   CA   C  N S 382 
TRP   C    C  N N 383 
TRP   O    O  N N 384 
TRP   CB   C  N N 385 
TRP   CG   C  Y N 386 
TRP   CD1  C  Y N 387 
TRP   CD2  C  Y N 388 
TRP   NE1  N  Y N 389 
TRP   CE2  C  Y N 390 
TRP   CE3  C  Y N 391 
TRP   CZ2  C  Y N 392 
TRP   CZ3  C  Y N 393 
TRP   CH2  C  Y N 394 
TRP   OXT  O  N N 395 
TRP   H    H  N N 396 
TRP   H2   H  N N 397 
TRP   HA   H  N N 398 
TRP   HB2  H  N N 399 
TRP   HB3  H  N N 400 
TRP   HD1  H  N N 401 
TRP   HE1  H  N N 402 
TRP   HE3  H  N N 403 
TRP   HZ2  H  N N 404 
TRP   HZ3  H  N N 405 
TRP   HH2  H  N N 406 
TRP   HXT  H  N N 407 
TYR   N    N  N N 408 
TYR   CA   C  N S 409 
TYR   C    C  N N 410 
TYR   O    O  N N 411 
TYR   CB   C  N N 412 
TYR   CG   C  Y N 413 
TYR   CD1  C  Y N 414 
TYR   CD2  C  Y N 415 
TYR   CE1  C  Y N 416 
TYR   CE2  C  Y N 417 
TYR   CZ   C  Y N 418 
TYR   OH   O  N N 419 
TYR   OXT  O  N N 420 
TYR   H    H  N N 421 
TYR   H2   H  N N 422 
TYR   HA   H  N N 423 
TYR   HB2  H  N N 424 
TYR   HB3  H  N N 425 
TYR   HD1  H  N N 426 
TYR   HD2  H  N N 427 
TYR   HE1  H  N N 428 
TYR   HE2  H  N N 429 
TYR   HH   H  N N 430 
TYR   HXT  H  N N 431 
VAL   N    N  N N 432 
VAL   CA   C  N S 433 
VAL   C    C  N N 434 
VAL   O    O  N N 435 
VAL   CB   C  N N 436 
VAL   CG1  C  N N 437 
VAL   CG2  C  N N 438 
VAL   OXT  O  N N 439 
VAL   H    H  N N 440 
VAL   H2   H  N N 441 
VAL   HA   H  N N 442 
VAL   HB   H  N N 443 
VAL   HG11 H  N N 444 
VAL   HG12 H  N N 445 
VAL   HG13 H  N N 446 
VAL   HG21 H  N N 447 
VAL   HG22 H  N N 448 
VAL   HG23 H  N N 449 
VAL   HXT  H  N N 450 
# 
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 
A1BV1 N3   C2   sing N N 1   
A1BV1 N3   C4   sing N N 2   
A1BV1 N5   C4   doub Y N 3   
A1BV1 N5   C6   sing Y N 4   
A1BV1 C2   C1   sing N N 5   
A1BV1 C4   N14  sing Y N 6   
A1BV1 C6   C7   doub Y N 7   
A1BV1 N14  C13  doub Y N 8   
A1BV1 C7   C13  sing Y N 9   
A1BV1 C7   C8   sing N N 10  
A1BV1 C13  N12  sing N N 11  
A1BV1 C8   C9   doub N N 12  
A1BV1 N12  C15  sing N N 13  
A1BV1 N12  C10  sing N N 14  
A1BV1 C9   C10  sing N N 15  
A1BV1 C9   C21  sing N N 16  
A1BV1 C15  C16  sing N N 17  
A1BV1 C16  O17  sing N N 18  
A1BV1 C10  O11  doub N N 19  
A1BV1 C21  C22  doub Y N 20  
A1BV1 C21  C26  sing Y N 21  
A1BV1 C22  C23  sing Y N 22  
A1BV1 O17  C18  sing N N 23  
A1BV1 C18  C19  sing N N 24  
A1BV1 CL27 C26  sing N N 25  
A1BV1 C26  C25  doub Y N 26  
A1BV1 C23  C24  doub Y N 27  
A1BV1 C25  C24  sing Y N 28  
A1BV1 C25  F28  sing N N 29  
A1BV1 C19  N20  sing N N 30  
A1BV1 C24  N29  sing N N 31  
A1BV1 C30  N29  sing N N 32  
A1BV1 C30  C31  sing N N 33  
A1BV1 N29  C33  sing N N 34  
A1BV1 C31  C32  sing N N 35  
A1BV1 C33  C32  sing N N 36  
A1BV1 C33  O34  doub N N 37  
A1BV1 N3   H1   sing N N 38  
A1BV1 C6   H2   sing N N 39  
A1BV1 C8   H3   sing N N 40  
A1BV1 C15  H4   sing N N 41  
A1BV1 C15  H5   sing N N 42  
A1BV1 C22  H6   sing N N 43  
A1BV1 C1   H7   sing N N 44  
A1BV1 C1   H8   sing N N 45  
A1BV1 C1   H9   sing N N 46  
A1BV1 C16  H10  sing N N 47  
A1BV1 C16  H11  sing N N 48  
A1BV1 C18  H12  sing N N 49  
A1BV1 C18  H13  sing N N 50  
A1BV1 C19  H14  sing N N 51  
A1BV1 C19  H15  sing N N 52  
A1BV1 C2   H16  sing N N 53  
A1BV1 C2   H17  sing N N 54  
A1BV1 C23  H18  sing N N 55  
A1BV1 C30  H19  sing N N 56  
A1BV1 C30  H20  sing N N 57  
A1BV1 C31  H21  sing N N 58  
A1BV1 C31  H22  sing N N 59  
A1BV1 C32  H23  sing N N 60  
A1BV1 C32  H24  sing N N 61  
A1BV1 N20  H25  sing N N 62  
A1BV1 N20  H26  sing N N 63  
ALA   N    CA   sing N N 64  
ALA   N    H    sing N N 65  
ALA   N    H2   sing N N 66  
ALA   CA   C    sing N N 67  
ALA   CA   CB   sing N N 68  
ALA   CA   HA   sing N N 69  
ALA   C    O    doub N N 70  
ALA   C    OXT  sing N N 71  
ALA   CB   HB1  sing N N 72  
ALA   CB   HB2  sing N N 73  
ALA   CB   HB3  sing N N 74  
ALA   OXT  HXT  sing N N 75  
ARG   N    CA   sing N N 76  
ARG   N    H    sing N N 77  
ARG   N    H2   sing N N 78  
ARG   CA   C    sing N N 79  
ARG   CA   CB   sing N N 80  
ARG   CA   HA   sing N N 81  
ARG   C    O    doub N N 82  
ARG   C    OXT  sing N N 83  
ARG   CB   CG   sing N N 84  
ARG   CB   HB2  sing N N 85  
ARG   CB   HB3  sing N N 86  
ARG   CG   CD   sing N N 87  
ARG   CG   HG2  sing N N 88  
ARG   CG   HG3  sing N N 89  
ARG   CD   NE   sing N N 90  
ARG   CD   HD2  sing N N 91  
ARG   CD   HD3  sing N N 92  
ARG   NE   CZ   sing N N 93  
ARG   NE   HE   sing N N 94  
ARG   CZ   NH1  sing N N 95  
ARG   CZ   NH2  doub N N 96  
ARG   NH1  HH11 sing N N 97  
ARG   NH1  HH12 sing N N 98  
ARG   NH2  HH21 sing N N 99  
ARG   NH2  HH22 sing N N 100 
ARG   OXT  HXT  sing N N 101 
ASN   N    CA   sing N N 102 
ASN   N    H    sing N N 103 
ASN   N    H2   sing N N 104 
ASN   CA   C    sing N N 105 
ASN   CA   CB   sing N N 106 
ASN   CA   HA   sing N N 107 
ASN   C    O    doub N N 108 
ASN   C    OXT  sing N N 109 
ASN   CB   CG   sing N N 110 
ASN   CB   HB2  sing N N 111 
ASN   CB   HB3  sing N N 112 
ASN   CG   OD1  doub N N 113 
ASN   CG   ND2  sing N N 114 
ASN   ND2  HD21 sing N N 115 
ASN   ND2  HD22 sing N N 116 
ASN   OXT  HXT  sing N N 117 
ASP   N    CA   sing N N 118 
ASP   N    H    sing N N 119 
ASP   N    H2   sing N N 120 
ASP   CA   C    sing N N 121 
ASP   CA   CB   sing N N 122 
ASP   CA   HA   sing N N 123 
ASP   C    O    doub N N 124 
ASP   C    OXT  sing N N 125 
ASP   CB   CG   sing N N 126 
ASP   CB   HB2  sing N N 127 
ASP   CB   HB3  sing N N 128 
ASP   CG   OD1  doub N N 129 
ASP   CG   OD2  sing N N 130 
ASP   OD2  HD2  sing N N 131 
ASP   OXT  HXT  sing N N 132 
CYS   N    CA   sing N N 133 
CYS   N    H    sing N N 134 
CYS   N    H2   sing N N 135 
CYS   CA   C    sing N N 136 
CYS   CA   CB   sing N N 137 
CYS   CA   HA   sing N N 138 
CYS   C    O    doub N N 139 
CYS   C    OXT  sing N N 140 
CYS   CB   SG   sing N N 141 
CYS   CB   HB2  sing N N 142 
CYS   CB   HB3  sing N N 143 
CYS   SG   HG   sing N N 144 
CYS   OXT  HXT  sing N N 145 
GLN   N    CA   sing N N 146 
GLN   N    H    sing N N 147 
GLN   N    H2   sing N N 148 
GLN   CA   C    sing N N 149 
GLN   CA   CB   sing N N 150 
GLN   CA   HA   sing N N 151 
GLN   C    O    doub N N 152 
GLN   C    OXT  sing N N 153 
GLN   CB   CG   sing N N 154 
GLN   CB   HB2  sing N N 155 
GLN   CB   HB3  sing N N 156 
GLN   CG   CD   sing N N 157 
GLN   CG   HG2  sing N N 158 
GLN   CG   HG3  sing N N 159 
GLN   CD   OE1  doub N N 160 
GLN   CD   NE2  sing N N 161 
GLN   NE2  HE21 sing N N 162 
GLN   NE2  HE22 sing N N 163 
GLN   OXT  HXT  sing N N 164 
GLU   N    CA   sing N N 165 
GLU   N    H    sing N N 166 
GLU   N    H2   sing N N 167 
GLU   CA   C    sing N N 168 
GLU   CA   CB   sing N N 169 
GLU   CA   HA   sing N N 170 
GLU   C    O    doub N N 171 
GLU   C    OXT  sing N N 172 
GLU   CB   CG   sing N N 173 
GLU   CB   HB2  sing N N 174 
GLU   CB   HB3  sing N N 175 
GLU   CG   CD   sing N N 176 
GLU   CG   HG2  sing N N 177 
GLU   CG   HG3  sing N N 178 
GLU   CD   OE1  doub N N 179 
GLU   CD   OE2  sing N N 180 
GLU   OE2  HE2  sing N N 181 
GLU   OXT  HXT  sing N N 182 
GLY   N    CA   sing N N 183 
GLY   N    H    sing N N 184 
GLY   N    H2   sing N N 185 
GLY   CA   C    sing N N 186 
GLY   CA   HA2  sing N N 187 
GLY   CA   HA3  sing N N 188 
GLY   C    O    doub N N 189 
GLY   C    OXT  sing N N 190 
GLY   OXT  HXT  sing N N 191 
HIS   N    CA   sing N N 192 
HIS   N    H    sing N N 193 
HIS   N    H2   sing N N 194 
HIS   CA   C    sing N N 195 
HIS   CA   CB   sing N N 196 
HIS   CA   HA   sing N N 197 
HIS   C    O    doub N N 198 
HIS   C    OXT  sing N N 199 
HIS   CB   CG   sing N N 200 
HIS   CB   HB2  sing N N 201 
HIS   CB   HB3  sing N N 202 
HIS   CG   ND1  sing Y N 203 
HIS   CG   CD2  doub Y N 204 
HIS   ND1  CE1  doub Y N 205 
HIS   ND1  HD1  sing N N 206 
HIS   CD2  NE2  sing Y N 207 
HIS   CD2  HD2  sing N N 208 
HIS   CE1  NE2  sing Y N 209 
HIS   CE1  HE1  sing N N 210 
HIS   NE2  HE2  sing N N 211 
HIS   OXT  HXT  sing N N 212 
HOH   O    H1   sing N N 213 
HOH   O    H2   sing N N 214 
ILE   N    CA   sing N N 215 
ILE   N    H    sing N N 216 
ILE   N    H2   sing N N 217 
ILE   CA   C    sing N N 218 
ILE   CA   CB   sing N N 219 
ILE   CA   HA   sing N N 220 
ILE   C    O    doub N N 221 
ILE   C    OXT  sing N N 222 
ILE   CB   CG1  sing N N 223 
ILE   CB   CG2  sing N N 224 
ILE   CB   HB   sing N N 225 
ILE   CG1  CD1  sing N N 226 
ILE   CG1  HG12 sing N N 227 
ILE   CG1  HG13 sing N N 228 
ILE   CG2  HG21 sing N N 229 
ILE   CG2  HG22 sing N N 230 
ILE   CG2  HG23 sing N N 231 
ILE   CD1  HD11 sing N N 232 
ILE   CD1  HD12 sing N N 233 
ILE   CD1  HD13 sing N N 234 
ILE   OXT  HXT  sing N N 235 
LEU   N    CA   sing N N 236 
LEU   N    H    sing N N 237 
LEU   N    H2   sing N N 238 
LEU   CA   C    sing N N 239 
LEU   CA   CB   sing N N 240 
LEU   CA   HA   sing N N 241 
LEU   C    O    doub N N 242 
LEU   C    OXT  sing N N 243 
LEU   CB   CG   sing N N 244 
LEU   CB   HB2  sing N N 245 
LEU   CB   HB3  sing N N 246 
LEU   CG   CD1  sing N N 247 
LEU   CG   CD2  sing N N 248 
LEU   CG   HG   sing N N 249 
LEU   CD1  HD11 sing N N 250 
LEU   CD1  HD12 sing N N 251 
LEU   CD1  HD13 sing N N 252 
LEU   CD2  HD21 sing N N 253 
LEU   CD2  HD22 sing N N 254 
LEU   CD2  HD23 sing N N 255 
LEU   OXT  HXT  sing N N 256 
LYS   N    CA   sing N N 257 
LYS   N    H    sing N N 258 
LYS   N    H2   sing N N 259 
LYS   CA   C    sing N N 260 
LYS   CA   CB   sing N N 261 
LYS   CA   HA   sing N N 262 
LYS   C    O    doub N N 263 
LYS   C    OXT  sing N N 264 
LYS   CB   CG   sing N N 265 
LYS   CB   HB2  sing N N 266 
LYS   CB   HB3  sing N N 267 
LYS   CG   CD   sing N N 268 
LYS   CG   HG2  sing N N 269 
LYS   CG   HG3  sing N N 270 
LYS   CD   CE   sing N N 271 
LYS   CD   HD2  sing N N 272 
LYS   CD   HD3  sing N N 273 
LYS   CE   NZ   sing N N 274 
LYS   CE   HE2  sing N N 275 
LYS   CE   HE3  sing N N 276 
LYS   NZ   HZ1  sing N N 277 
LYS   NZ   HZ2  sing N N 278 
LYS   NZ   HZ3  sing N N 279 
LYS   OXT  HXT  sing N N 280 
MET   N    CA   sing N N 281 
MET   N    H    sing N N 282 
MET   N    H2   sing N N 283 
MET   CA   C    sing N N 284 
MET   CA   CB   sing N N 285 
MET   CA   HA   sing N N 286 
MET   C    O    doub N N 287 
MET   C    OXT  sing N N 288 
MET   CB   CG   sing N N 289 
MET   CB   HB2  sing N N 290 
MET   CB   HB3  sing N N 291 
MET   CG   SD   sing N N 292 
MET   CG   HG2  sing N N 293 
MET   CG   HG3  sing N N 294 
MET   SD   CE   sing N N 295 
MET   CE   HE1  sing N N 296 
MET   CE   HE2  sing N N 297 
MET   CE   HE3  sing N N 298 
MET   OXT  HXT  sing N N 299 
PHE   N    CA   sing N N 300 
PHE   N    H    sing N N 301 
PHE   N    H2   sing N N 302 
PHE   CA   C    sing N N 303 
PHE   CA   CB   sing N N 304 
PHE   CA   HA   sing N N 305 
PHE   C    O    doub N N 306 
PHE   C    OXT  sing N N 307 
PHE   CB   CG   sing N N 308 
PHE   CB   HB2  sing N N 309 
PHE   CB   HB3  sing N N 310 
PHE   CG   CD1  doub Y N 311 
PHE   CG   CD2  sing Y N 312 
PHE   CD1  CE1  sing Y N 313 
PHE   CD1  HD1  sing N N 314 
PHE   CD2  CE2  doub Y N 315 
PHE   CD2  HD2  sing N N 316 
PHE   CE1  CZ   doub Y N 317 
PHE   CE1  HE1  sing N N 318 
PHE   CE2  CZ   sing Y N 319 
PHE   CE2  HE2  sing N N 320 
PHE   CZ   HZ   sing N N 321 
PHE   OXT  HXT  sing N N 322 
PRO   N    CA   sing N N 323 
PRO   N    CD   sing N N 324 
PRO   N    H    sing N N 325 
PRO   CA   C    sing N N 326 
PRO   CA   CB   sing N N 327 
PRO   CA   HA   sing N N 328 
PRO   C    O    doub N N 329 
PRO   C    OXT  sing N N 330 
PRO   CB   CG   sing N N 331 
PRO   CB   HB2  sing N N 332 
PRO   CB   HB3  sing N N 333 
PRO   CG   CD   sing N N 334 
PRO   CG   HG2  sing N N 335 
PRO   CG   HG3  sing N N 336 
PRO   CD   HD2  sing N N 337 
PRO   CD   HD3  sing N N 338 
PRO   OXT  HXT  sing N N 339 
SER   N    CA   sing N N 340 
SER   N    H    sing N N 341 
SER   N    H2   sing N N 342 
SER   CA   C    sing N N 343 
SER   CA   CB   sing N N 344 
SER   CA   HA   sing N N 345 
SER   C    O    doub N N 346 
SER   C    OXT  sing N N 347 
SER   CB   OG   sing N N 348 
SER   CB   HB2  sing N N 349 
SER   CB   HB3  sing N N 350 
SER   OG   HG   sing N N 351 
SER   OXT  HXT  sing N N 352 
THR   N    CA   sing N N 353 
THR   N    H    sing N N 354 
THR   N    H2   sing N N 355 
THR   CA   C    sing N N 356 
THR   CA   CB   sing N N 357 
THR   CA   HA   sing N N 358 
THR   C    O    doub N N 359 
THR   C    OXT  sing N N 360 
THR   CB   OG1  sing N N 361 
THR   CB   CG2  sing N N 362 
THR   CB   HB   sing N N 363 
THR   OG1  HG1  sing N N 364 
THR   CG2  HG21 sing N N 365 
THR   CG2  HG22 sing N N 366 
THR   CG2  HG23 sing N N 367 
THR   OXT  HXT  sing N N 368 
TRP   N    CA   sing N N 369 
TRP   N    H    sing N N 370 
TRP   N    H2   sing N N 371 
TRP   CA   C    sing N N 372 
TRP   CA   CB   sing N N 373 
TRP   CA   HA   sing N N 374 
TRP   C    O    doub N N 375 
TRP   C    OXT  sing N N 376 
TRP   CB   CG   sing N N 377 
TRP   CB   HB2  sing N N 378 
TRP   CB   HB3  sing N N 379 
TRP   CG   CD1  doub Y N 380 
TRP   CG   CD2  sing Y N 381 
TRP   CD1  NE1  sing Y N 382 
TRP   CD1  HD1  sing N N 383 
TRP   CD2  CE2  doub Y N 384 
TRP   CD2  CE3  sing Y N 385 
TRP   NE1  CE2  sing Y N 386 
TRP   NE1  HE1  sing N N 387 
TRP   CE2  CZ2  sing Y N 388 
TRP   CE3  CZ3  doub Y N 389 
TRP   CE3  HE3  sing N N 390 
TRP   CZ2  CH2  doub Y N 391 
TRP   CZ2  HZ2  sing N N 392 
TRP   CZ3  CH2  sing Y N 393 
TRP   CZ3  HZ3  sing N N 394 
TRP   CH2  HH2  sing N N 395 
TRP   OXT  HXT  sing N N 396 
TYR   N    CA   sing N N 397 
TYR   N    H    sing N N 398 
TYR   N    H2   sing N N 399 
TYR   CA   C    sing N N 400 
TYR   CA   CB   sing N N 401 
TYR   CA   HA   sing N N 402 
TYR   C    O    doub N N 403 
TYR   C    OXT  sing N N 404 
TYR   CB   CG   sing N N 405 
TYR   CB   HB2  sing N N 406 
TYR   CB   HB3  sing N N 407 
TYR   CG   CD1  doub Y N 408 
TYR   CG   CD2  sing Y N 409 
TYR   CD1  CE1  sing Y N 410 
TYR   CD1  HD1  sing N N 411 
TYR   CD2  CE2  doub Y N 412 
TYR   CD2  HD2  sing N N 413 
TYR   CE1  CZ   doub Y N 414 
TYR   CE1  HE1  sing N N 415 
TYR   CE2  CZ   sing Y N 416 
TYR   CE2  HE2  sing N N 417 
TYR   CZ   OH   sing N N 418 
TYR   OH   HH   sing N N 419 
TYR   OXT  HXT  sing N N 420 
VAL   N    CA   sing N N 421 
VAL   N    H    sing N N 422 
VAL   N    H2   sing N N 423 
VAL   CA   C    sing N N 424 
VAL   CA   CB   sing N N 425 
VAL   CA   HA   sing N N 426 
VAL   C    O    doub N N 427 
VAL   C    OXT  sing N N 428 
VAL   CB   CG1  sing N N 429 
VAL   CB   CG2  sing N N 430 
VAL   CB   HB   sing N N 431 
VAL   CG1  HG11 sing N N 432 
VAL   CG1  HG12 sing N N 433 
VAL   CG1  HG13 sing N N 434 
VAL   CG2  HG21 sing N N 435 
VAL   CG2  HG22 sing N N 436 
VAL   CG2  HG23 sing N N 437 
VAL   OXT  HXT  sing N N 438 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'In-house structure' 
# 
_atom_sites.entry_id                    9N48 
_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]   0.016073 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004679 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012352 
_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]   0.015791 
_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 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . SER   A 1 238 ? 32.970  -14.566 -12.508 1.00 73.03  ? 249 SER   A N    1 
ATOM   2    C  CA   . SER   A 1 238 ? 32.512  -13.333 -11.878 1.00 83.52  ? 249 SER   A CA   1 
ATOM   3    C  C    . SER   A 1 238 ? 31.355  -13.605 -10.917 1.00 79.50  ? 249 SER   A C    1 
ATOM   4    O  O    . SER   A 1 238 ? 31.567  -13.985 -9.760  1.00 71.94  ? 249 SER   A O    1 
ATOM   5    C  CB   . SER   A 1 238 ? 32.091  -12.317 -12.943 1.00 85.35  ? 249 SER   A CB   1 
ATOM   6    N  N    . ASP   A 1 239 ? 30.126  -13.407 -11.403 1.00 72.71  ? 250 ASP   A N    1 
ATOM   7    C  CA   . ASP   A 1 239 ? 28.955  -13.733 -10.596 1.00 73.06  ? 250 ASP   A CA   1 
ATOM   8    C  C    . ASP   A 1 239 ? 28.835  -15.238 -10.386 1.00 75.58  ? 250 ASP   A C    1 
ATOM   9    O  O    . ASP   A 1 239 ? 28.479  -15.690 -9.291  1.00 73.76  ? 250 ASP   A O    1 
ATOM   10   C  CB   . ASP   A 1 239 ? 27.691  -13.175 -11.248 1.00 73.78  ? 250 ASP   A CB   1 
ATOM   11   N  N    . GLU   A 1 240 ? 29.122  -16.031 -11.424 1.00 77.20  ? 251 GLU   A N    1 
ATOM   12   C  CA   . GLU   A 1 240 ? 29.199  -17.477 -11.240 1.00 72.03  ? 251 GLU   A CA   1 
ATOM   13   C  C    . GLU   A 1 240 ? 30.371  -17.855 -10.347 1.00 69.79  ? 251 GLU   A C    1 
ATOM   14   O  O    . GLU   A 1 240 ? 30.285  -18.832 -9.593  1.00 58.61  ? 251 GLU   A O    1 
ATOM   15   C  CB   . GLU   A 1 240 ? 29.310  -18.189 -12.590 1.00 77.17  ? 251 GLU   A CB   1 
ATOM   16   C  CG   . GLU   A 1 240 ? 28.049  -18.122 -13.440 1.00 92.32  ? 251 GLU   A CG   1 
ATOM   17   C  CD   . GLU   A 1 240 ? 27.874  -16.779 -14.132 1.00 97.34  ? 251 GLU   A CD   1 
ATOM   18   O  OE1  . GLU   A 1 240 ? 28.893  -16.148 -14.483 1.00 91.70  ? 251 GLU   A OE1  1 
ATOM   19   O  OE2  . GLU   A 1 240 ? 26.716  -16.349 -14.320 1.00 100.87 ? 251 GLU   A OE2  1 
ATOM   20   N  N    . GLU   A 1 241 ? 31.464  -17.090 -10.407 1.00 60.49  ? 252 GLU   A N    1 
ATOM   21   C  CA   . GLU   A 1 241 ? 32.615  -17.367 -9.553  1.00 67.71  ? 252 GLU   A CA   1 
ATOM   22   C  C    . GLU   A 1 241 ? 32.259  -17.212 -8.078  1.00 56.80  ? 252 GLU   A C    1 
ATOM   23   O  O    . GLU   A 1 241 ? 32.573  -18.081 -7.256  1.00 54.59  ? 252 GLU   A O    1 
ATOM   24   C  CB   . GLU   A 1 241 ? 33.781  -16.449 -9.928  1.00 71.02  ? 252 GLU   A CB   1 
ATOM   25   C  CG   . GLU   A 1 241 ? 34.956  -16.492 -8.951  1.00 79.08  ? 252 GLU   A CG   1 
ATOM   26   C  CD   . GLU   A 1 241 ? 36.236  -17.034 -9.573  1.00 88.35  ? 252 GLU   A CD   1 
ATOM   27   O  OE1  . GLU   A 1 241 ? 36.378  -16.969 -10.817 1.00 89.70  ? 252 GLU   A OE1  1 
ATOM   28   O  OE2  . GLU   A 1 241 ? 37.101  -17.523 -8.811  1.00 78.42  ? 252 GLU   A OE2  1 
ATOM   29   N  N    . ILE   A 1 242 ? 31.608  -16.104 -7.719  1.00 56.04  ? 253 ILE   A N    1 
ATOM   30   C  CA   . ILE   A 1 242 ? 31.270  -15.895 -6.315  1.00 47.70  ? 253 ILE   A CA   1 
ATOM   31   C  C    . ILE   A 1 242 ? 30.196  -16.884 -5.863  1.00 49.12  ? 253 ILE   A C    1 
ATOM   32   O  O    . ILE   A 1 242 ? 30.158  -17.272 -4.689  1.00 44.39  ? 253 ILE   A O    1 
ATOM   33   C  CB   . ILE   A 1 242 ? 30.853  -14.430 -6.072  1.00 51.92  ? 253 ILE   A CB   1 
ATOM   34   C  CG1  . ILE   A 1 242 ? 30.869  -14.108 -4.576  1.00 63.65  ? 253 ILE   A CG1  1 
ATOM   35   C  CG2  . ILE   A 1 242 ? 29.481  -14.132 -6.659  1.00 67.48  ? 253 ILE   A CG2  1 
ATOM   36   C  CD1  . ILE   A 1 242 ? 32.267  -13.913 -4.011  1.00 66.95  ? 253 ILE   A CD1  1 
ATOM   37   N  N    . LEU   A 1 243 ? 29.314  -17.311 -6.770  1.00 48.80  ? 254 LEU   A N    1 
ATOM   38   C  CA   . LEU   A 1 243 ? 28.348  -18.349 -6.422  1.00 56.73  ? 254 LEU   A CA   1 
ATOM   39   C  C    . LEU   A 1 243 ? 29.054  -19.660 -6.098  1.00 49.75  ? 254 LEU   A C    1 
ATOM   40   O  O    . LEU   A 1 243 ? 28.775  -20.291 -5.070  1.00 47.13  ? 254 LEU   A O    1 
ATOM   41   C  CB   . LEU   A 1 243 ? 27.344  -18.548 -7.558  1.00 52.15  ? 254 LEU   A CB   1 
ATOM   42   C  CG   . LEU   A 1 243 ? 26.517  -19.831 -7.430  1.00 53.19  ? 254 LEU   A CG   1 
ATOM   43   C  CD1  . LEU   A 1 243 ? 25.638  -19.810 -6.177  1.00 51.14  ? 254 LEU   A CD1  1 
ATOM   44   C  CD2  . LEU   A 1 243 ? 25.687  -20.095 -8.680  1.00 56.95  ? 254 LEU   A CD2  1 
ATOM   45   N  N    . GLU   A 1 244 ? 29.982  -20.083 -6.963  1.00 50.33  ? 255 GLU   A N    1 
ATOM   46   C  CA   . GLU   A 1 244 ? 30.719  -21.310 -6.684  1.00 50.44  ? 255 GLU   A CA   1 
ATOM   47   C  C    . GLU   A 1 244 ? 31.589  -21.170 -5.445  1.00 47.67  ? 255 GLU   A C    1 
ATOM   48   O  O    . GLU   A 1 244 ? 31.801  -22.153 -4.727  1.00 47.13  ? 255 GLU   A O    1 
ATOM   49   C  CB   . GLU   A 1 244 ? 31.588  -21.715 -7.880  1.00 53.11  ? 255 GLU   A CB   1 
ATOM   50   C  CG   . GLU   A 1 244 ? 30.828  -22.345 -9.047  1.00 56.51  ? 255 GLU   A CG   1 
ATOM   51   C  CD   . GLU   A 1 244 ? 29.894  -23.481 -8.637  1.00 60.52  ? 255 GLU   A CD   1 
ATOM   52   O  OE1  . GLU   A 1 244 ? 30.159  -24.185 -7.635  1.00 56.12  ? 255 GLU   A OE1  1 
ATOM   53   O  OE2  . GLU   A 1 244 ? 28.870  -23.662 -9.326  1.00 65.01  ? 255 GLU   A OE2  1 
ATOM   54   N  N    . LYS   A 1 245 ? 32.094  -19.964 -5.172  1.00 46.20  ? 256 LYS   A N    1 
ATOM   55   C  CA   . LYS   A 1 245 ? 32.814  -19.751 -3.923  1.00 43.78  ? 256 LYS   A CA   1 
ATOM   56   C  C    . LYS   A 1 245 ? 31.909  -19.966 -2.711  1.00 45.06  ? 256 LYS   A C    1 
ATOM   57   O  O    . LYS   A 1 245 ? 32.300  -20.634 -1.746  1.00 40.72  ? 256 LYS   A O    1 
ATOM   58   C  CB   . LYS   A 1 245 ? 33.411  -18.342 -3.903  1.00 50.53  ? 256 LYS   A CB   1 
ATOM   59   C  CG   . LYS   A 1 245 ? 34.060  -17.959 -2.591  1.00 49.52  ? 256 LYS   A CG   1 
ATOM   60   C  CD   . LYS   A 1 245 ? 35.320  -18.770 -2.316  1.00 62.04  ? 256 LYS   A CD   1 
ATOM   61   C  CE   . LYS   A 1 245 ? 35.767  -18.620 -0.861  1.00 71.07  ? 256 LYS   A CE   1 
ATOM   62   N  NZ   . LYS   A 1 245 ? 35.895  -17.187 -0.450  1.00 70.46  ? 256 LYS   A NZ   1 
ATOM   63   N  N    . LEU   A 1 246 ? 30.680  -19.449 -2.758  1.00 41.76  ? 257 LEU   A N    1 
ATOM   64   C  CA   . LEU   A 1 246 ? 29.732  -19.715 -1.676  1.00 40.30  ? 257 LEU   A CA   1 
ATOM   65   C  C    . LEU   A 1 246 ? 29.415  -21.202 -1.559  1.00 41.14  ? 257 LEU   A C    1 
ATOM   66   O  O    . LEU   A 1 246 ? 29.398  -21.767 -0.456  1.00 39.78  ? 257 LEU   A O    1 
ATOM   67   C  CB   . LEU   A 1 246 ? 28.455  -18.900 -1.874  1.00 40.64  ? 257 LEU   A CB   1 
ATOM   68   C  CG   . LEU   A 1 246 ? 27.379  -19.125 -0.804  1.00 40.34  ? 257 LEU   A CG   1 
ATOM   69   C  CD1  . LEU   A 1 246 ? 27.899  -18.831 0.604   1.00 39.36  ? 257 LEU   A CD1  1 
ATOM   70   C  CD2  . LEU   A 1 246 ? 26.182  -18.230 -1.090  1.00 44.58  ? 257 LEU   A CD2  1 
ATOM   71   N  N    . ARG   A 1 247 ? 29.130  -21.847 -2.687  1.00 43.68  ? 258 ARG   A N    1 
ATOM   72   C  CA   . ARG   A 1 247 ? 28.786  -23.264 -2.639  1.00 51.36  ? 258 ARG   A CA   1 
ATOM   73   C  C    . ARG   A 1 247 ? 29.922  -24.106 -2.071  1.00 48.35  ? 258 ARG   A C    1 
ATOM   74   O  O    . ARG   A 1 247 ? 29.668  -25.066 -1.336  1.00 44.46  ? 258 ARG   A O    1 
ATOM   75   C  CB   . ARG   A 1 247 ? 28.417  -23.771 -4.033  1.00 48.29  ? 258 ARG   A CB   1 
ATOM   76   C  CG   . ARG   A 1 247 ? 27.193  -23.111 -4.640  1.00 49.43  ? 258 ARG   A CG   1 
ATOM   77   C  CD   . ARG   A 1 247 ? 26.768  -23.785 -5.936  1.00 53.12  ? 258 ARG   A CD   1 
ATOM   78   N  NE   . ARG   A 1 247 ? 26.286  -25.139 -5.701  1.00 54.52  ? 258 ARG   A NE   1 
ATOM   79   C  CZ   . ARG   A 1 247 ? 26.990  -26.236 -5.942  1.00 56.04  ? 258 ARG   A CZ   1 
ATOM   80   N  NH1  . ARG   A 1 247 ? 28.207  -26.174 -6.462  1.00 56.42  ? 258 ARG   A NH1  1 
ATOM   81   N  NH2  . ARG   A 1 247 ? 26.456  -27.424 -5.665  1.00 57.51  ? 258 ARG   A NH2  1 
ATOM   82   N  N    . SER   A 1 248 ? 31.175  -23.726 -2.339  1.00 44.45  ? 259 SER   A N    1 
ATOM   83   C  CA   . SER   A 1 248 ? 32.306  -24.538 -1.899  1.00 44.69  ? 259 SER   A CA   1 
ATOM   84   C  C    . SER   A 1 248 ? 32.464  -24.555 -0.377  1.00 42.30  ? 259 SER   A C    1 
ATOM   85   O  O    . SER   A 1 248 ? 33.054  -25.500 0.160   1.00 42.71  ? 259 SER   A O    1 
ATOM   86   C  CB   . SER   A 1 248 ? 33.596  -24.036 -2.548  1.00 45.32  ? 259 SER   A CB   1 
ATOM   87   O  OG   . SER   A 1 248 ? 33.972  -22.797 -1.972  1.00 48.44  ? 259 SER   A OG   1 
ATOM   88   N  N    . ILE   A 1 249 ? 31.945  -23.549 0.334   1.00 40.03  ? 260 ILE   A N    1 
ATOM   89   C  CA   . ILE   A 1 249 ? 32.146  -23.499 1.776   1.00 37.99  ? 260 ILE   A CA   1 
ATOM   90   C  C    . ILE   A 1 249 ? 31.006  -24.152 2.539   1.00 37.51  ? 260 ILE   A C    1 
ATOM   91   O  O    . ILE   A 1 249 ? 31.008  -24.124 3.776   1.00 40.89  ? 260 ILE   A O    1 
ATOM   92   C  CB   . ILE   A 1 249 ? 32.354  -22.056 2.280   1.00 41.33  ? 260 ILE   A CB   1 
ATOM   93   C  CG1  . ILE   A 1 249 ? 31.076  -21.230 2.124   1.00 35.51  ? 260 ILE   A CG1  1 
ATOM   94   C  CG2  . ILE   A 1 249 ? 33.534  -21.406 1.558   1.00 41.17  ? 260 ILE   A CG2  1 
ATOM   95   C  CD1  . ILE   A 1 249 ? 31.156  -19.849 2.769   1.00 41.76  ? 260 ILE   A CD1  1 
ATOM   96   N  N    . VAL   A 1 250 ? 29.996  -24.667 1.846   1.00 39.00  ? 261 VAL   A N    1 
ATOM   97   C  CA   . VAL   A 1 250 ? 28.846  -25.315 2.467   1.00 42.63  ? 261 VAL   A CA   1 
ATOM   98   C  C    . VAL   A 1 250 ? 28.848  -26.791 2.073   1.00 45.75  ? 261 VAL   A C    1 
ATOM   99   O  O    . VAL   A 1 250 ? 29.049  -27.122 0.898   1.00 43.62  ? 261 VAL   A O    1 
ATOM   100  C  CB   . VAL   A 1 250 ? 27.534  -24.635 2.046   1.00 39.15  ? 261 VAL   A CB   1 
ATOM   101  C  CG1  . VAL   A 1 250 ? 26.358  -25.293 2.753   1.00 46.87  ? 261 VAL   A CG1  1 
ATOM   102  C  CG2  . VAL   A 1 250 ? 27.599  -23.148 2.329   1.00 37.25  ? 261 VAL   A CG2  1 
ATOM   103  N  N    A SER   A 1 251 ? 28.617  -27.669 3.051   0.48 41.28  ? 262 SER   A N    1 
ATOM   104  N  N    B SER   A 1 251 ? 28.619  -27.671 3.046   0.52 41.29  ? 262 SER   A N    1 
ATOM   105  C  CA   A SER   A 1 251 ? 28.511  -29.094 2.767   0.48 45.17  ? 262 SER   A CA   1 
ATOM   106  C  CA   B SER   A 1 251 ? 28.533  -29.090 2.737   0.52 45.17  ? 262 SER   A CA   1 
ATOM   107  C  C    A SER   A 1 251 ? 27.215  -29.403 2.025   0.48 45.81  ? 262 SER   A C    1 
ATOM   108  C  C    B SER   A 1 251 ? 27.220  -29.407 2.029   0.52 45.81  ? 262 SER   A C    1 
ATOM   109  O  O    A SER   A 1 251 ? 26.175  -28.782 2.266   0.48 44.81  ? 262 SER   A O    1 
ATOM   110  O  O    B SER   A 1 251 ? 26.179  -28.796 2.290   0.52 44.80  ? 262 SER   A O    1 
ATOM   111  C  CB   A SER   A 1 251 ? 28.573  -29.908 4.064   0.48 47.25  ? 262 SER   A CB   1 
ATOM   112  C  CB   B SER   A 1 251 ? 28.655  -29.934 4.007   0.52 47.26  ? 262 SER   A CB   1 
ATOM   113  O  OG   A SER   A 1 251 ? 29.836  -29.794 4.696   0.48 44.93  ? 262 SER   A OG   1 
ATOM   114  O  OG   B SER   A 1 251 ? 28.586  -31.315 3.697   0.52 46.46  ? 262 SER   A OG   1 
ATOM   115  N  N    . VAL   A 1 252 ? 27.280  -30.372 1.116   1.00 48.93  ? 263 VAL   A N    1 
ATOM   116  C  CA   . VAL   A 1 252 ? 26.101  -30.837 0.397   1.00 51.47  ? 263 VAL   A CA   1 
ATOM   117  C  C    . VAL   A 1 252 ? 25.453  -31.938 1.224   1.00 55.99  ? 263 VAL   A C    1 
ATOM   118  O  O    . VAL   A 1 252 ? 26.080  -32.966 1.505   1.00 63.38  ? 263 VAL   A O    1 
ATOM   119  C  CB   . VAL   A 1 252 ? 26.457  -31.333 -1.014  1.00 54.80  ? 263 VAL   A CB   1 
ATOM   120  C  CG1  . VAL   A 1 252 ? 25.373  -32.248 -1.547  1.00 58.23  ? 263 VAL   A CG1  1 
ATOM   121  C  CG2  . VAL   A 1 252 ? 26.657  -30.152 -1.952  1.00 54.28  ? 263 VAL   A CG2  1 
ATOM   122  N  N    . GLY   A 1 253 ? 24.207  -31.721 1.630   1.00 52.03  ? 264 GLY   A N    1 
ATOM   123  C  CA   . GLY   A 1 253 ? 23.502  -32.728 2.403   1.00 60.83  ? 264 GLY   A CA   1 
ATOM   124  C  C    . GLY   A 1 253 ? 22.052  -32.347 2.607   1.00 60.07  ? 264 GLY   A C    1 
ATOM   125  O  O    . GLY   A 1 253 ? 21.620  -31.242 2.269   1.00 52.01  ? 264 GLY   A O    1 
ATOM   126  N  N    . ASP   A 1 254 ? 21.317  -33.270 3.232   1.00 56.92  ? 265 ASP   A N    1 
ATOM   127  C  CA   . ASP   A 1 254 ? 19.900  -33.092 3.530   1.00 55.05  ? 265 ASP   A CA   1 
ATOM   128  C  C    . ASP   A 1 254 ? 19.726  -32.607 4.960   1.00 53.74  ? 265 ASP   A C    1 
ATOM   129  O  O    . ASP   A 1 254 ? 20.083  -33.337 5.899   1.00 54.34  ? 265 ASP   A O    1 
ATOM   130  C  CB   . ASP   A 1 254 ? 19.146  -34.402 3.322   1.00 58.97  ? 265 ASP   A CB   1 
ATOM   131  C  CG   . ASP   A 1 254 ? 17.641  -34.265 3.531   1.00 64.09  ? 265 ASP   A CG   1 
ATOM   132  O  OD1  . ASP   A 1 254 ? 17.166  -33.198 3.983   1.00 58.86  ? 265 ASP   A OD1  1 
ATOM   133  O  OD2  . ASP   A 1 254 ? 16.927  -35.247 3.237   1.00 71.31  ? 265 ASP   A OD2  1 
ATOM   134  N  N    . PRO   A 1 255 ? 19.198  -31.400 5.178   1.00 52.44  ? 266 PRO   A N    1 
ATOM   135  C  CA   . PRO   A 1 255 ? 18.992  -30.933 6.560   1.00 48.01  ? 266 PRO   A CA   1 
ATOM   136  C  C    . PRO   A 1 255 ? 18.021  -31.798 7.338   1.00 49.39  ? 266 PRO   A C    1 
ATOM   137  O  O    . PRO   A 1 255 ? 18.089  -31.825 8.576   1.00 49.45  ? 266 PRO   A O    1 
ATOM   138  C  CB   . PRO   A 1 255 ? 18.442  -29.509 6.381   1.00 47.13  ? 266 PRO   A CB   1 
ATOM   139  C  CG   . PRO   A 1 255 ? 18.633  -29.165 4.934   1.00 48.41  ? 266 PRO   A CG   1 
ATOM   140  C  CD   . PRO   A 1 255 ? 18.664  -30.455 4.184   1.00 53.34  ? 266 PRO   A CD   1 
ATOM   141  N  N    . LYS   A 1 256 ? 17.131  -32.515 6.649   1.00 52.04  ? 267 LYS   A N    1 
ATOM   142  C  CA   . LYS   A 1 256 ? 16.170  -33.408 7.288   1.00 56.78  ? 267 LYS   A CA   1 
ATOM   143  C  C    . LYS   A 1 256 ? 16.801  -34.631 7.935   1.00 55.37  ? 267 LYS   A C    1 
ATOM   144  O  O    . LYS   A 1 256 ? 16.117  -35.303 8.713   1.00 61.67  ? 267 LYS   A O    1 
ATOM   145  C  CB   . LYS   A 1 256 ? 15.106  -33.883 6.301   1.00 58.01  ? 267 LYS   A CB   1 
ATOM   146  C  CG   . LYS   A 1 256 ? 14.133  -32.820 5.860   1.00 58.17  ? 267 LYS   A CG   1 
ATOM   147  C  CD   . LYS   A 1 256 ? 13.130  -33.411 4.888   1.00 76.63  ? 267 LYS   A CD   1 
ATOM   148  C  CE   . LYS   A 1 256 ? 12.083  -32.395 4.478   1.00 91.67  ? 267 LYS   A CE   1 
ATOM   149  N  NZ   . LYS   A 1 256 ? 11.059  -33.016 3.591   1.00 83.32  ? 267 LYS   A NZ   1 
ATOM   150  N  N    . LYS   A 1 257 ? 18.064  -34.955 7.647   1.00 58.63  ? 268 LYS   A N    1 
ATOM   151  C  CA   . LYS   A 1 257 ? 18.634  -36.090 8.366   1.00 72.03  ? 268 LYS   A CA   1 
ATOM   152  C  C    . LYS   A 1 257 ? 19.008  -35.722 9.797   1.00 70.46  ? 268 LYS   A C    1 
ATOM   153  O  O    . LYS   A 1 257 ? 18.934  -36.578 10.686  1.00 70.50  ? 268 LYS   A O    1 
ATOM   154  C  CB   . LYS   A 1 257 ? 19.854  -36.660 7.635   1.00 62.70  ? 268 LYS   A CB   1 
ATOM   155  C  CG   . LYS   A 1 257 ? 19.518  -37.496 6.404   1.00 83.12  ? 268 LYS   A CG   1 
ATOM   156  C  CD   . LYS   A 1 257 ? 20.755  -38.237 5.910   1.00 92.66  ? 268 LYS   A CD   1 
ATOM   157  C  CE   . LYS   A 1 257 ? 20.540  -38.863 4.545   1.00 90.65  ? 268 LYS   A CE   1 
ATOM   158  N  NZ   . LYS   A 1 257 ? 21.818  -39.371 3.975   1.00 99.18  ? 268 LYS   A NZ   1 
ATOM   159  N  N    . LYS   A 1 258 ? 19.432  -34.484 10.042  1.00 48.86  ? 269 LYS   A N    1 
ATOM   160  C  CA   . LYS   A 1 258 ? 19.785  -34.077 11.394  1.00 46.21  ? 269 LYS   A CA   1 
ATOM   161  C  C    . LYS   A 1 258 ? 18.672  -33.302 12.104  1.00 55.24  ? 269 LYS   A C    1 
ATOM   162  O  O    . LYS   A 1 258 ? 18.634  -33.296 13.341  1.00 46.80  ? 269 LYS   A O    1 
ATOM   163  C  CB   . LYS   A 1 258 ? 21.082  -33.252 11.369  1.00 45.23  ? 269 LYS   A CB   1 
ATOM   164  C  CG   . LYS   A 1 258 ? 21.646  -32.905 12.737  1.00 49.16  ? 269 LYS   A CG   1 
ATOM   165  C  CD   . LYS   A 1 258 ? 22.997  -32.222 12.627  1.00 49.77  ? 269 LYS   A CD   1 
ATOM   166  C  CE   . LYS   A 1 258 ? 23.546  -31.875 14.004  1.00 57.38  ? 269 LYS   A CE   1 
ATOM   167  N  NZ   . LYS   A 1 258 ? 24.846  -31.142 13.914  1.00 61.62  ? 269 LYS   A NZ   1 
ATOM   168  N  N    . TYR   A 1 259 ? 17.755  -32.671 11.365  1.00 45.41  ? 270 TYR   A N    1 
ATOM   169  C  CA   . TYR   A 1 259 ? 16.757  -31.792 11.964  1.00 44.30  ? 270 TYR   A CA   1 
ATOM   170  C  C    . TYR   A 1 259 ? 15.354  -32.170 11.516  1.00 47.64  ? 270 TYR   A C    1 
ATOM   171  O  O    . TYR   A 1 259 ? 15.138  -32.630 10.391  1.00 49.62  ? 270 TYR   A O    1 
ATOM   172  C  CB   . TYR   A 1 259 ? 17.043  -30.322 11.617  1.00 41.99  ? 270 TYR   A CB   1 
ATOM   173  C  CG   . TYR   A 1 259 ? 18.378  -29.864 12.143  1.00 41.68  ? 270 TYR   A CG   1 
ATOM   174  C  CD1  . TYR   A 1 259 ? 18.530  -29.516 13.478  1.00 37.51  ? 270 TYR   A CD1  1 
ATOM   175  C  CD2  . TYR   A 1 259 ? 19.505  -29.831 11.321  1.00 39.10  ? 270 TYR   A CD2  1 
ATOM   176  C  CE1  . TYR   A 1 259 ? 19.746  -29.111 13.974  1.00 35.52  ? 270 TYR   A CE1  1 
ATOM   177  C  CE2  . TYR   A 1 259 ? 20.740  -29.422 11.816  1.00 37.28  ? 270 TYR   A CE2  1 
ATOM   178  C  CZ   . TYR   A 1 259 ? 20.850  -29.069 13.145  1.00 40.58  ? 270 TYR   A CZ   1 
ATOM   179  O  OH   . TYR   A 1 259 ? 22.057  -28.667 13.663  1.00 36.02  ? 270 TYR   A OH   1 
ATOM   180  N  N    . THR   A 1 260 ? 14.395  -31.948 12.414  1.00 47.05  ? 271 THR   A N    1 
ATOM   181  C  CA   . THR   A 1 260 ? 12.991  -32.222 12.155  1.00 49.86  ? 271 THR   A CA   1 
ATOM   182  C  C    . THR   A 1 260 ? 12.158  -31.115 12.792  1.00 48.66  ? 271 THR   A C    1 
ATOM   183  O  O    . THR   A 1 260 ? 12.696  -30.147 13.342  1.00 46.51  ? 271 THR   A O    1 
ATOM   184  C  CB   . THR   A 1 260 ? 12.603  -33.609 12.682  1.00 52.31  ? 271 THR   A CB   1 
ATOM   185  O  OG1  . THR   A 1 260 ? 11.296  -33.948 12.213  1.00 55.77  ? 271 THR   A OG1  1 
ATOM   186  C  CG2  . THR   A 1 260 ? 12.612  -33.621 14.204  1.00 50.64  ? 271 THR   A CG2  1 
ATOM   187  N  N    . ARG   A 1 261 ? 10.830  -31.249 12.693  1.00 51.24  ? 272 ARG   A N    1 
ATOM   188  C  CA   . ARG   A 1 261 ? 9.892   -30.298 13.301  1.00 50.85  ? 272 ARG   A CA   1 
ATOM   189  C  C    . ARG   A 1 261 ? 10.060  -28.889 12.737  1.00 51.79  ? 272 ARG   A C    1 
ATOM   190  O  O    . ARG   A 1 261 ? 10.062  -27.903 13.480  1.00 53.44  ? 272 ARG   A O    1 
ATOM   191  C  CB   . ARG   A 1 261 ? 10.040  -30.257 14.819  1.00 49.69  ? 272 ARG   A CB   1 
ATOM   192  C  CG   . ARG   A 1 261 ? 9.384   -31.360 15.594  1.00 59.97  ? 272 ARG   A CG   1 
ATOM   193  C  CD   . ARG   A 1 261 ? 9.420   -30.932 17.045  1.00 63.11  ? 272 ARG   A CD   1 
ATOM   194  N  NE   . ARG   A 1 261 ? 8.761   -31.850 17.959  1.00 63.87  ? 272 ARG   A NE   1 
ATOM   195  C  CZ   . ARG   A 1 261 ? 8.427   -31.530 19.200  1.00 74.70  ? 272 ARG   A CZ   1 
ATOM   196  N  NH1  . ARG   A 1 261 ? 8.659   -30.320 19.685  1.00 70.36  ? 272 ARG   A NH1  1 
ATOM   197  N  NH2  . ARG   A 1 261 ? 7.838   -32.441 19.971  1.00 83.14  ? 272 ARG   A NH2  1 
ATOM   198  N  N    . PHE   A 1 262 ? 10.222  -28.784 11.423  1.00 51.95  ? 273 PHE   A N    1 
ATOM   199  C  CA   . PHE   A 1 262 ? 10.352  -27.472 10.811  1.00 49.47  ? 273 PHE   A CA   1 
ATOM   200  C  C    . PHE   A 1 262 ? 9.035   -26.714 10.929  1.00 51.17  ? 273 PHE   A C    1 
ATOM   201  O  O    . PHE   A 1 262 ? 7.978   -27.228 10.556  1.00 54.46  ? 273 PHE   A O    1 
ATOM   202  C  CB   . PHE   A 1 262 ? 10.753  -27.608 9.345   1.00 50.84  ? 273 PHE   A CB   1 
ATOM   203  C  CG   . PHE   A 1 262 ? 12.204  -27.952 9.135   1.00 48.86  ? 273 PHE   A CG   1 
ATOM   204  C  CD1  . PHE   A 1 262 ? 12.648  -29.257 9.289   1.00 53.24  ? 273 PHE   A CD1  1 
ATOM   205  C  CD2  . PHE   A 1 262 ? 13.112  -26.980 8.754   1.00 46.69  ? 273 PHE   A CD2  1 
ATOM   206  C  CE1  . PHE   A 1 262 ? 13.977  -29.582 9.082   1.00 52.12  ? 273 PHE   A CE1  1 
ATOM   207  C  CE2  . PHE   A 1 262 ? 14.447  -27.298 8.538   1.00 45.18  ? 273 PHE   A CE2  1 
ATOM   208  C  CZ   . PHE   A 1 262 ? 14.880  -28.599 8.709   1.00 46.14  ? 273 PHE   A CZ   1 
ATOM   209  N  N    . GLU   A 1 263 ? 9.094   -25.491 11.452  1.00 49.25  ? 274 GLU   A N    1 
ATOM   210  C  CA   . GLU   A 1 263 ? 7.903   -24.664 11.607  1.00 56.17  ? 274 GLU   A CA   1 
ATOM   211  C  C    . GLU   A 1 263 ? 8.282   -23.226 11.283  1.00 52.82  ? 274 GLU   A C    1 
ATOM   212  O  O    . GLU   A 1 263 ? 9.233   -22.692 11.861  1.00 46.62  ? 274 GLU   A O    1 
ATOM   213  C  CB   . GLU   A 1 263 ? 7.314   -24.787 13.023  1.00 52.79  ? 274 GLU   A CB   1 
ATOM   214  C  CG   . GLU   A 1 263 ? 5.979   -24.065 13.219  1.00 67.99  ? 274 GLU   A CG   1 
ATOM   215  C  CD   . GLU   A 1 263 ? 5.408   -24.234 14.625  1.00 68.15  ? 274 GLU   A CD   1 
ATOM   216  O  OE1  . GLU   A 1 263 ? 6.196   -24.319 15.591  1.00 69.16  ? 274 GLU   A OE1  1 
ATOM   217  O  OE2  . GLU   A 1 263 ? 4.167   -24.308 14.762  1.00 77.26  ? 274 GLU   A OE2  1 
ATOM   218  N  N    . LYS   A 1 264 ? 7.546   -22.610 10.359  1.00 53.98  ? 275 LYS   A N    1 
ATOM   219  C  CA   . LYS   A 1 264 ? 7.871   -21.263 9.903   1.00 54.63  ? 275 LYS   A CA   1 
ATOM   220  C  C    . LYS   A 1 264 ? 7.539   -20.220 10.961  1.00 56.90  ? 275 LYS   A C    1 
ATOM   221  O  O    . LYS   A 1 264 ? 6.476   -20.262 11.582  1.00 58.57  ? 275 LYS   A O    1 
ATOM   222  C  CB   . LYS   A 1 264 ? 7.113   -20.947 8.616   1.00 55.02  ? 275 LYS   A CB   1 
ATOM   223  C  CG   . LYS   A 1 264 ? 7.384   -19.561 8.056   1.00 55.82  ? 275 LYS   A CG   1 
ATOM   224  C  CD   . LYS   A 1 264 ? 6.542   -19.299 6.810   1.00 75.03  ? 275 LYS   A CD   1 
ATOM   225  C  CE   . LYS   A 1 264 ? 6.426   -17.807 6.511   1.00 82.87  ? 275 LYS   A CE   1 
ATOM   226  N  NZ   . LYS   A 1 264 ? 5.625   -17.531 5.279   1.00 84.93  ? 275 LYS   A NZ   1 
ATOM   227  N  N    . ILE   A 1 265 ? 8.466   -19.283 11.178  1.00 55.22  ? 276 ILE   A N    1 
ATOM   228  C  CA   . ILE   A 1 265 ? 8.254   -18.187 12.115  1.00 59.36  ? 276 ILE   A CA   1 
ATOM   229  C  C    . ILE   A 1 265 ? 8.457   -16.822 11.478  1.00 68.75  ? 276 ILE   A C    1 
ATOM   230  O  O    . ILE   A 1 265 ? 8.304   -15.807 12.160  1.00 69.25  ? 276 ILE   A O    1 
ATOM   231  C  CB   . ILE   A 1 265 ? 9.156   -18.314 13.359  1.00 44.29  ? 276 ILE   A CB   1 
ATOM   232  C  CG1  . ILE   A 1 265 ? 10.623  -18.155 12.959  1.00 45.59  ? 276 ILE   A CG1  1 
ATOM   233  C  CG2  . ILE   A 1 265 ? 8.919   -19.640 14.061  1.00 51.24  ? 276 ILE   A CG2  1 
ATOM   234  C  CD1  . ILE   A 1 265 ? 11.548  -17.860 14.119  1.00 40.54  ? 276 ILE   A CD1  1 
ATOM   235  N  N    . GLY   A 1 266 ? 8.792   -16.754 10.193  1.00 65.38  ? 277 GLY   A N    1 
ATOM   236  C  CA   . GLY   A 1 266 ? 9.005   -15.464 9.567   1.00 72.06  ? 277 GLY   A CA   1 
ATOM   237  C  C    . GLY   A 1 266 ? 9.595   -15.520 8.174   1.00 67.24  ? 277 GLY   A C    1 
ATOM   238  O  O    . GLY   A 1 266 ? 10.251  -16.496 7.797   1.00 70.35  ? 277 GLY   A O    1 
ATOM   239  N  N    . GLN   A 1 267 ? 9.367   -14.460 7.405   1.00 74.69  ? 278 GLN   A N    1 
ATOM   240  C  CA   . GLN   A 1 267 ? 9.857   -14.345 6.040   1.00 83.19  ? 278 GLN   A CA   1 
ATOM   241  C  C    . GLN   A 1 267 ? 10.472  -12.975 5.807   1.00 95.12  ? 278 GLN   A C    1 
ATOM   242  O  O    . GLN   A 1 267 ? 9.842   -11.949 6.085   1.00 86.83  ? 278 GLN   A O    1 
ATOM   243  C  CB   . GLN   A 1 267 ? 8.733   -14.593 5.027   1.00 90.49  ? 278 GLN   A CB   1 
ATOM   244  C  CG   . GLN   A 1 267 ? 9.098   -14.226 3.594   1.00 96.09  ? 278 GLN   A CG   1 
ATOM   245  C  CD   . GLN   A 1 267 ? 10.189  -15.098 3.012   1.00 94.35  ? 278 GLN   A CD   1 
ATOM   246  O  OE1  . GLN   A 1 267 ? 10.271  -16.290 3.305   1.00 100.00 ? 278 GLN   A OE1  1 
ATOM   247  N  NE2  . GLN   A 1 267 ? 11.040  -14.504 2.180   1.00 93.58  ? 278 GLN   A NE2  1 
ATOM   248  N  N    . GLY   A 1 268 ? 11.709  -12.968 5.309   1.00 97.61  ? 279 GLY   A N    1 
ATOM   249  C  CA   . GLY   A 1 268 ? 12.401  -11.744 4.967   1.00 96.04  ? 279 GLY   A CA   1 
ATOM   250  C  C    . GLY   A 1 268 ? 12.967  -11.831 3.560   1.00 95.39  ? 279 GLY   A C    1 
ATOM   251  O  O    . GLY   A 1 268 ? 12.866  -12.862 2.891   1.00 95.23  ? 279 GLY   A O    1 
ATOM   252  N  N    . ALA   A 1 269 ? 13.557  -10.716 3.125   1.00 98.74  ? 280 ALA   A N    1 
ATOM   253  C  CA   . ALA   A 1 269 ? 14.280  -10.723 1.859   1.00 94.10  ? 280 ALA   A CA   1 
ATOM   254  C  C    . ALA   A 1 269 ? 15.484  -11.650 1.921   1.00 88.63  ? 280 ALA   A C    1 
ATOM   255  O  O    . ALA   A 1 269 ? 15.951  -12.125 0.879   1.00 86.44  ? 280 ALA   A O    1 
ATOM   256  C  CB   . ALA   A 1 269 ? 14.716  -9.307  1.481   1.00 85.11  ? 280 ALA   A CB   1 
ATOM   257  N  N    . SER   A 1 270 ? 15.990  -11.924 3.124   1.00 92.28  ? 281 SER   A N    1 
ATOM   258  C  CA   . SER   A 1 270 ? 17.088  -12.865 3.273   1.00 86.36  ? 281 SER   A CA   1 
ATOM   259  C  C    . SER   A 1 270 ? 16.629  -14.305 3.105   1.00 79.26  ? 281 SER   A C    1 
ATOM   260  O  O    . SER   A 1 270 ? 17.463  -15.182 2.868   1.00 76.41  ? 281 SER   A O    1 
ATOM   261  C  CB   . SER   A 1 270 ? 17.740  -12.699 4.649   1.00 80.21  ? 281 SER   A CB   1 
ATOM   262  O  OG   . SER   A 1 270 ? 17.701  -11.351 5.081   1.00 85.94  ? 281 SER   A OG   1 
ATOM   263  N  N    . GLY   A 1 271 ? 15.336  -14.571 3.214   1.00 73.51  ? 282 GLY   A N    1 
ATOM   264  C  CA   . GLY   A 1 271 ? 14.831  -15.912 3.048   1.00 62.22  ? 282 GLY   A CA   1 
ATOM   265  C  C    . GLY   A 1 271 ? 13.751  -16.199 4.064   1.00 68.79  ? 282 GLY   A C    1 
ATOM   266  O  O    . GLY   A 1 271 ? 13.199  -15.291 4.682   1.00 69.85  ? 282 GLY   A O    1 
ATOM   267  N  N    . THR   A 1 272 ? 13.450  -17.484 4.216   1.00 62.31  ? 283 THR   A N    1 
ATOM   268  C  CA   . THR   A 1 272 ? 12.441  -17.961 5.152   1.00 54.73  ? 283 THR   A CA   1 
ATOM   269  C  C    . THR   A 1 272 ? 13.130  -18.488 6.405   1.00 46.75  ? 283 THR   A C    1 
ATOM   270  O  O    . THR   A 1 272 ? 14.117  -19.226 6.308   1.00 44.25  ? 283 THR   A O    1 
ATOM   271  C  CB   . THR   A 1 272 ? 11.595  -19.062 4.511   1.00 54.91  ? 283 THR   A CB   1 
ATOM   272  O  OG1  . THR   A 1 272 ? 11.140  -18.621 3.226   1.00 70.91  ? 283 THR   A OG1  1 
ATOM   273  C  CG2  . THR   A 1 272 ? 10.396  -19.402 5.383   1.00 55.08  ? 283 THR   A CG2  1 
ATOM   274  N  N    . VAL   A 1 273 ? 12.612  -18.115 7.573   1.00 47.99  ? 284 VAL   A N    1 
ATOM   275  C  CA   . VAL   A 1 273 ? 13.196  -18.504 8.855   1.00 47.79  ? 284 VAL   A CA   1 
ATOM   276  C  C    . VAL   A 1 273 ? 12.263  -19.489 9.539   1.00 42.43  ? 284 VAL   A C    1 
ATOM   277  O  O    . VAL   A 1 273 ? 11.064  -19.225 9.686   1.00 44.51  ? 284 VAL   A O    1 
ATOM   278  C  CB   . VAL   A 1 273 ? 13.475  -17.292 9.762   1.00 47.61  ? 284 VAL   A CB   1 
ATOM   279  C  CG1  . VAL   A 1 273 ? 13.965  -17.767 11.129  1.00 43.00  ? 284 VAL   A CG1  1 
ATOM   280  C  CG2  . VAL   A 1 273 ? 14.527  -16.394 9.128   1.00 45.25  ? 284 VAL   A CG2  1 
ATOM   281  N  N    . TYR   A 1 274 ? 12.818  -20.622 9.953   1.00 41.19  ? 285 TYR   A N    1 
ATOM   282  C  CA   . TYR   A 1 274 ? 12.093  -21.677 10.638  1.00 42.94  ? 285 TYR   A CA   1 
ATOM   283  C  C    . TYR   A 1 274 ? 12.690  -21.915 12.017  1.00 39.58  ? 285 TYR   A C    1 
ATOM   284  O  O    . TYR   A 1 274 ? 13.852  -21.587 12.279  1.00 37.29  ? 285 TYR   A O    1 
ATOM   285  C  CB   . TYR   A 1 274 ? 12.166  -23.002 9.858   1.00 45.21  ? 285 TYR   A CB   1 
ATOM   286  C  CG   . TYR   A 1 274 ? 11.595  -22.967 8.462   1.00 52.74  ? 285 TYR   A CG   1 
ATOM   287  C  CD1  . TYR   A 1 274 ? 12.402  -22.651 7.379   1.00 50.41  ? 285 TYR   A CD1  1 
ATOM   288  C  CD2  . TYR   A 1 274 ? 10.261  -23.270 8.219   1.00 55.99  ? 285 TYR   A CD2  1 
ATOM   289  C  CE1  . TYR   A 1 274 ? 11.894  -22.624 6.089   1.00 54.36  ? 285 TYR   A CE1  1 
ATOM   290  C  CE2  . TYR   A 1 274 ? 9.742   -23.243 6.930   1.00 57.50  ? 285 TYR   A CE2  1 
ATOM   291  C  CZ   . TYR   A 1 274 ? 10.565  -22.919 5.873   1.00 60.07  ? 285 TYR   A CZ   1 
ATOM   292  O  OH   . TYR   A 1 274 ? 10.066  -22.888 4.594   1.00 65.49  ? 285 TYR   A OH   1 
ATOM   293  N  N    . THR   A 1 275 ? 11.888  -22.509 12.895  1.00 40.34  ? 286 THR   A N    1 
ATOM   294  C  CA   . THR   A 1 275 ? 12.427  -23.258 14.020  1.00 41.36  ? 286 THR   A CA   1 
ATOM   295  C  C    . THR   A 1 275 ? 12.424  -24.737 13.659  1.00 40.04  ? 286 THR   A C    1 
ATOM   296  O  O    . THR   A 1 275 ? 11.651  -25.186 12.810  1.00 42.55  ? 286 THR   A O    1 
ATOM   297  C  CB   . THR   A 1 275 ? 11.621  -23.041 15.301  1.00 38.89  ? 286 THR   A CB   1 
ATOM   298  O  OG1  . THR   A 1 275 ? 10.243  -23.332 15.044  1.00 41.70  ? 286 THR   A OG1  1 
ATOM   299  C  CG2  . THR   A 1 275 ? 11.780  -21.607 15.787  1.00 37.66  ? 286 THR   A CG2  1 
ATOM   300  N  N    . ALA   A 1 276 ? 13.307  -25.489 14.307  1.00 38.65  ? 287 ALA   A N    1 
ATOM   301  C  CA   . ALA   A 1 276 ? 13.411  -26.926 14.085  1.00 40.02  ? 287 ALA   A CA   1 
ATOM   302  C  C    . ALA   A 1 276 ? 14.092  -27.528 15.303  1.00 38.63  ? 287 ALA   A C    1 
ATOM   303  O  O    . ALA   A 1 276 ? 14.486  -26.814 16.230  1.00 36.67  ? 287 ALA   A O    1 
ATOM   304  C  CB   . ALA   A 1 276 ? 14.171  -27.245 12.793  1.00 40.48  ? 287 ALA   A CB   1 
ATOM   305  N  N    . MET   A 1 277 ? 14.234  -28.853 15.297  1.00 39.97  ? 288 MET   A N    1 
ATOM   306  C  CA   . MET   A 1 277 ? 14.810  -29.551 16.438  1.00 39.25  ? 288 MET   A CA   1 
ATOM   307  C  C    . MET   A 1 277 ? 15.864  -30.558 15.999  1.00 39.72  ? 288 MET   A C    1 
ATOM   308  O  O    . MET   A 1 277 ? 15.654  -31.309 15.041  1.00 41.85  ? 288 MET   A O    1 
ATOM   309  C  CB   . MET   A 1 277 ? 13.720  -30.256 17.251  1.00 41.03  ? 288 MET   A CB   1 
ATOM   310  C  CG   . MET   A 1 277 ? 14.255  -30.958 18.481  1.00 40.56  ? 288 MET   A CG   1 
ATOM   311  S  SD   . MET   A 1 277 ? 12.952  -31.799 19.397  1.00 55.21  ? 288 MET   A SD   1 
ATOM   312  C  CE   . MET   A 1 277 ? 12.320  -30.376 20.295  1.00 50.93  ? 288 MET   A CE   1 
ATOM   313  N  N    . ASP   A 1 278 ? 16.994  -30.558 16.705  1.00 38.05  ? 289 ASP   A N    1 
ATOM   314  C  CA   . ASP   A 1 278 ? 18.012  -31.587 16.539  1.00 38.80  ? 289 ASP   A CA   1 
ATOM   315  C  C    . ASP   A 1 278 ? 17.422  -32.936 16.927  1.00 46.01  ? 289 ASP   A C    1 
ATOM   316  O  O    . ASP   A 1 278 ? 16.972  -33.127 18.063  1.00 41.38  ? 289 ASP   A O    1 
ATOM   317  C  CB   . ASP   A 1 278 ? 19.233  -31.243 17.393  1.00 36.80  ? 289 ASP   A CB   1 
ATOM   318  C  CG   . ASP   A 1 278 ? 20.413  -32.177 17.164  1.00 42.19  ? 289 ASP   A CG   1 
ATOM   319  O  OD1  . ASP   A 1 278 ? 20.231  -33.411 17.237  1.00 42.62  ? 289 ASP   A OD1  1 
ATOM   320  O  OD2  . ASP   A 1 278 ? 21.532  -31.664 16.937  1.00 39.99  ? 289 ASP   A OD2  1 
ATOM   321  N  N    A VAL   A 1 279 ? 17.406  -33.870 15.972  0.39 43.71  ? 290 VAL   A N    1 
ATOM   322  N  N    B VAL   A 1 279 ? 17.433  -33.874 15.975  0.61 43.69  ? 290 VAL   A N    1 
ATOM   323  C  CA   A VAL   A 1 279 ? 16.754  -35.155 16.208  0.39 49.20  ? 290 VAL   A CA   1 
ATOM   324  C  CA   B VAL   A 1 279 ? 16.761  -35.153 16.176  0.61 49.24  ? 290 VAL   A CA   1 
ATOM   325  C  C    A VAL   A 1 279 ? 17.440  -35.920 17.333  0.39 46.83  ? 290 VAL   A C    1 
ATOM   326  C  C    B VAL   A 1 279 ? 17.478  -36.030 17.196  0.61 47.12  ? 290 VAL   A C    1 
ATOM   327  O  O    A VAL   A 1 279 ? 16.779  -36.617 18.113  0.39 50.74  ? 290 VAL   A O    1 
ATOM   328  O  O    B VAL   A 1 279 ? 16.863  -36.943 17.757  0.61 50.72  ? 290 VAL   A O    1 
ATOM   329  C  CB   A VAL   A 1 279 ? 16.713  -35.974 14.901  0.39 49.50  ? 290 VAL   A CB   1 
ATOM   330  C  CB   B VAL   A 1 279 ? 16.614  -35.888 14.829  0.61 49.48  ? 290 VAL   A CB   1 
ATOM   331  C  CG1  A VAL   A 1 279 ? 16.175  -37.370 15.157  0.39 53.95  ? 290 VAL   A CG1  1 
ATOM   332  C  CG1  B VAL   A 1 279 ? 17.945  -36.487 14.391  0.61 49.92  ? 290 VAL   A CG1  1 
ATOM   333  C  CG2  A VAL   A 1 279 ? 15.862  -35.264 13.862  0.39 49.89  ? 290 VAL   A CG2  1 
ATOM   334  C  CG2  B VAL   A 1 279 ? 15.535  -36.949 14.913  0.61 54.50  ? 290 VAL   A CG2  1 
ATOM   335  N  N    . ALA   A 1 280 ? 18.760  -35.778 17.463  1.00 46.26  ? 291 ALA   A N    1 
ATOM   336  C  CA   . ALA   A 1 280 ? 19.514  -36.589 18.416  1.00 46.16  ? 291 ALA   A CA   1 
ATOM   337  C  C    . ALA   A 1 280 ? 19.617  -35.959 19.799  1.00 46.77  ? 291 ALA   A C    1 
ATOM   338  O  O    . ALA   A 1 280 ? 19.694  -36.686 20.795  1.00 46.88  ? 291 ALA   A O    1 
ATOM   339  C  CB   . ALA   A 1 280 ? 20.925  -36.861 17.884  1.00 47.18  ? 291 ALA   A CB   1 
ATOM   340  N  N    . THR   A 1 281 ? 19.614  -34.629 19.893  1.00 41.40  ? 292 THR   A N    1 
ATOM   341  C  CA   . THR   A 1 281 ? 19.801  -33.973 21.177  1.00 39.69  ? 292 THR   A CA   1 
ATOM   342  C  C    . THR   A 1 281 ? 18.584  -33.214 21.670  1.00 43.59  ? 292 THR   A C    1 
ATOM   343  O  O    . THR   A 1 281 ? 18.549  -32.852 22.851  1.00 38.13  ? 292 THR   A O    1 
ATOM   344  C  CB   . THR   A 1 281 ? 20.967  -32.988 21.104  1.00 37.44  ? 292 THR   A CB   1 
ATOM   345  O  OG1  . THR   A 1 281 ? 20.580  -31.890 20.265  1.00 35.95  ? 292 THR   A OG1  1 
ATOM   346  C  CG2  . THR   A 1 281 ? 22.212  -33.684 20.535  1.00 40.96  ? 292 THR   A CG2  1 
ATOM   347  N  N    . GLY   A 1 282 ? 17.607  -32.938 20.802  1.00 39.33  ? 293 GLY   A N    1 
ATOM   348  C  CA   . GLY   A 1 282 ? 16.468  -32.131 21.183  1.00 39.97  ? 293 GLY   A CA   1 
ATOM   349  C  C    . GLY   A 1 282 ? 16.700  -30.635 21.180  1.00 36.40  ? 293 GLY   A C    1 
ATOM   350  O  O    . GLY   A 1 282 ? 15.790  -29.887 21.564  1.00 36.27  ? 293 GLY   A O    1 
ATOM   351  N  N    . GLN   A 1 283 ? 17.878  -30.167 20.770  1.00 34.90  ? 294 GLN   A N    1 
ATOM   352  C  CA   . GLN   A 1 283 ? 18.129  -28.729 20.719  1.00 41.78  ? 294 GLN   A CA   1 
ATOM   353  C  C    . GLN   A 1 283 ? 17.209  -28.049 19.710  1.00 35.07  ? 294 GLN   A C    1 
ATOM   354  O  O    . GLN   A 1 283 ? 17.096  -28.490 18.562  1.00 34.21  ? 294 GLN   A O    1 
ATOM   355  C  CB   . GLN   A 1 283 ? 19.588  -28.447 20.355  1.00 33.53  ? 294 GLN   A CB   1 
ATOM   356  C  CG   . GLN   A 1 283 ? 19.868  -26.941 20.198  1.00 36.63  ? 294 GLN   A CG   1 
ATOM   357  C  CD   . GLN   A 1 283 ? 21.322  -26.606 19.883  1.00 51.60  ? 294 GLN   A CD   1 
ATOM   358  O  OE1  . GLN   A 1 283 ? 22.102  -27.464 19.458  1.00 49.01  ? 294 GLN   A OE1  1 
ATOM   359  N  NE2  . GLN   A 1 283 ? 21.688  -25.340 20.080  1.00 41.69  ? 294 GLN   A NE2  1 
ATOM   360  N  N    . GLU   A 1 284 ? 16.562  -26.963 20.146  1.00 32.50  ? 295 GLU   A N    1 
ATOM   361  C  CA   . GLU   A 1 284 ? 15.799  -26.105 19.245  1.00 32.80  ? 295 GLU   A CA   1 
ATOM   362  C  C    . GLU   A 1 284 ? 16.762  -25.206 18.471  1.00 31.71  ? 295 GLU   A C    1 
ATOM   363  O  O    . GLU   A 1 284 ? 17.696  -24.641 19.046  1.00 31.30  ? 295 GLU   A O    1 
ATOM   364  C  CB   . GLU   A 1 284 ? 14.824  -25.232 20.043  1.00 32.92  ? 295 GLU   A CB   1 
ATOM   365  C  CG   . GLU   A 1 284 ? 13.919  -26.023 20.968  1.00 49.32  ? 295 GLU   A CG   1 
ATOM   366  C  CD   . GLU   A 1 284 ? 12.971  -25.137 21.758  1.00 56.69  ? 295 GLU   A CD   1 
ATOM   367  O  OE1  . GLU   A 1 284 ? 13.052  -23.892 21.621  1.00 42.35  ? 295 GLU   A OE1  1 
ATOM   368  O  OE2  . GLU   A 1 284 ? 12.183  -25.686 22.557  1.00 60.25  ? 295 GLU   A OE2  1 
ATOM   369  N  N    . VAL   A 1 285 ? 16.527  -25.056 17.167  1.00 32.12  ? 296 VAL   A N    1 
ATOM   370  C  CA   . VAL   A 1 285 ? 17.424  -24.291 16.307  1.00 31.09  ? 296 VAL   A CA   1 
ATOM   371  C  C    . VAL   A 1 285 ? 16.606  -23.395 15.391  1.00 31.94  ? 296 VAL   A C    1 
ATOM   372  O  O    . VAL   A 1 285 ? 15.423  -23.632 15.151  1.00 33.68  ? 296 VAL   A O    1 
ATOM   373  C  CB   . VAL   A 1 285 ? 18.346  -25.192 15.455  1.00 31.39  ? 296 VAL   A CB   1 
ATOM   374  C  CG1  . VAL   A 1 285 ? 19.253  -26.028 16.351  1.00 30.84  ? 296 VAL   A CG1  1 
ATOM   375  C  CG2  . VAL   A 1 285 ? 17.494  -26.075 14.552  1.00 33.63  ? 296 VAL   A CG2  1 
ATOM   376  N  N    . ALA   A 1 286 ? 17.268  -22.363 14.869  1.00 30.99  ? 297 ALA   A N    1 
ATOM   377  C  CA   . ALA   A 1 286 ? 16.713  -21.471 13.859  1.00 31.95  ? 297 ALA   A CA   1 
ATOM   378  C  C    . ALA   A 1 286 ? 17.407  -21.756 12.538  1.00 32.30  ? 297 ALA   A C    1 
ATOM   379  O  O    . ALA   A 1 286 ? 18.638  -21.782 12.481  1.00 35.72  ? 297 ALA   A O    1 
ATOM   380  C  CB   . ALA   A 1 286 ? 16.923  -20.006 14.238  1.00 31.00  ? 297 ALA   A CB   1 
ATOM   381  N  N    . ILE   A 1 287 ? 16.620  -21.969 11.486  1.00 34.31  ? 298 ILE   A N    1 
ATOM   382  C  CA   . ILE   A 1 287 ? 17.140  -22.342 10.176  1.00 36.30  ? 298 ILE   A CA   1 
ATOM   383  C  C    . ILE   A 1 287 ? 16.593  -21.371 9.147   1.00 36.54  ? 298 ILE   A C    1 
ATOM   384  O  O    . ILE   A 1 287 ? 15.372  -21.231 9.012   1.00 38.38  ? 298 ILE   A O    1 
ATOM   385  C  CB   . ILE   A 1 287 ? 16.772  -23.786 9.797   1.00 36.98  ? 298 ILE   A CB   1 
ATOM   386  C  CG1  . ILE   A 1 287 ? 17.258  -24.749 10.877  1.00 35.96  ? 298 ILE   A CG1  1 
ATOM   387  C  CG2  . ILE   A 1 287 ? 17.395  -24.151 8.454   1.00 38.05  ? 298 ILE   A CG2  1 
ATOM   388  C  CD1  . ILE   A 1 287 ? 17.024  -26.231 10.542  1.00 37.99  ? 298 ILE   A CD1  1 
ATOM   389  N  N    . LYS   A 1 288 ? 17.486  -20.700 8.424   1.00 37.78  ? 299 LYS   A N    1 
ATOM   390  C  CA   . LYS   A 1 288 ? 17.089  -19.808 7.343   1.00 37.47  ? 299 LYS   A CA   1 
ATOM   391  C  C    . LYS   A 1 288 ? 17.312  -20.502 6.006   1.00 39.17  ? 299 LYS   A C    1 
ATOM   392  O  O    . LYS   A 1 288 ? 18.378  -21.080 5.769   1.00 38.34  ? 299 LYS   A O    1 
ATOM   393  C  CB   . LYS   A 1 288 ? 17.858  -18.488 7.382   1.00 38.21  ? 299 LYS   A CB   1 
ATOM   394  C  CG   . LYS   A 1 288 ? 17.318  -17.460 6.383   1.00 38.03  ? 299 LYS   A CG   1 
ATOM   395  C  CD   . LYS   A 1 288 ? 18.151  -16.181 6.387   1.00 46.00  ? 299 LYS   A CD   1 
ATOM   396  C  CE   . LYS   A 1 288 ? 17.987  -15.395 7.686   1.00 47.96  ? 299 LYS   A CE   1 
ATOM   397  N  NZ   . LYS   A 1 288 ? 18.941  -14.245 7.752   1.00 42.49  ? 299 LYS   A NZ   1 
ATOM   398  N  N    . GLN   A 1 289 ? 16.299  -20.459 5.151   1.00 42.63  ? 300 GLN   A N    1 
ATOM   399  C  CA   . GLN   A 1 289 ? 16.325  -21.070 3.828   1.00 50.68  ? 300 GLN   A CA   1 
ATOM   400  C  C    . GLN   A 1 289 ? 16.478  -19.972 2.780   1.00 48.55  ? 300 GLN   A C    1 
ATOM   401  O  O    . GLN   A 1 289 ? 15.682  -19.027 2.752   1.00 46.20  ? 300 GLN   A O    1 
ATOM   402  C  CB   . GLN   A 1 289 ? 15.048  -21.882 3.593   1.00 47.03  ? 300 GLN   A CB   1 
ATOM   403  C  CG   . GLN   A 1 289 ? 14.826  -22.336 2.162   1.00 53.60  ? 300 GLN   A CG   1 
ATOM   404  C  CD   . GLN   A 1 289 ? 13.379  -22.735 1.911   1.00 67.53  ? 300 GLN   A CD   1 
ATOM   405  O  OE1  . GLN   A 1 289 ? 12.504  -22.517 2.755   1.00 58.10  ? 300 GLN   A OE1  1 
ATOM   406  N  NE2  . GLN   A 1 289 ? 13.120  -23.321 0.747   1.00 66.31  ? 300 GLN   A NE2  1 
ATOM   407  N  N    . MET   A 1 290 ? 17.494  -20.100 1.916   1.00 48.34  ? 301 MET   A N    1 
ATOM   408  C  CA   . MET   A 1 290 ? 17.818  -19.079 0.923   1.00 52.96  ? 301 MET   A CA   1 
ATOM   409  C  C    . MET   A 1 290 ? 17.994  -19.690 -0.462  1.00 62.75  ? 301 MET   A C    1 
ATOM   410  O  O    . MET   A 1 290 ? 18.690  -20.700 -0.615  1.00 48.24  ? 301 MET   A O    1 
ATOM   411  C  CB   . MET   A 1 290 ? 19.117  -18.351 1.307   1.00 60.41  ? 301 MET   A CB   1 
ATOM   412  C  CG   . MET   A 1 290 ? 19.188  -17.855 2.744   1.00 67.48  ? 301 MET   A CG   1 
ATOM   413  S  SD   . MET   A 1 290 ? 20.664  -16.873 3.128   1.00 72.62  ? 301 MET   A SD   1 
ATOM   414  C  CE   . MET   A 1 290 ? 20.405  -15.369 2.204   1.00 70.40  ? 301 MET   A CE   1 
ATOM   415  N  N    . ASN   A 1 291 ? 17.359  -19.077 -1.465  1.00 69.75  ? 302 ASN   A N    1 
ATOM   416  C  CA   . ASN   A 1 291 ? 17.587  -19.404 -2.874  1.00 71.97  ? 302 ASN   A CA   1 
ATOM   417  C  C    . ASN   A 1 291 ? 18.790  -18.600 -3.361  1.00 70.61  ? 302 ASN   A C    1 
ATOM   418  O  O    . ASN   A 1 291 ? 18.705  -17.375 -3.503  1.00 70.06  ? 302 ASN   A O    1 
ATOM   419  C  CB   . ASN   A 1 291 ? 16.349  -19.111 -3.718  1.00 85.90  ? 302 ASN   A CB   1 
ATOM   420  C  CG   . ASN   A 1 291 ? 15.402  -20.294 -3.791  1.00 96.17  ? 302 ASN   A CG   1 
ATOM   421  O  OD1  . ASN   A 1 291 ? 15.801  -21.436 -3.562  1.00 94.10  ? 302 ASN   A OD1  1 
ATOM   422  N  ND2  . ASN   A 1 291 ? 14.143  -20.028 -4.119  1.00 110.32 ? 302 ASN   A ND2  1 
ATOM   423  N  N    . LEU   A 1 292 ? 19.912  -19.284 -3.614  1.00 52.87  ? 303 LEU   A N    1 
ATOM   424  C  CA   . LEU   A 1 292 ? 21.125  -18.584 -4.033  1.00 59.58  ? 303 LEU   A CA   1 
ATOM   425  C  C    . LEU   A 1 292 ? 20.972  -17.908 -5.390  1.00 64.07  ? 303 LEU   A C    1 
ATOM   426  O  O    . LEU   A 1 292 ? 21.533  -16.829 -5.613  1.00 69.64  ? 303 LEU   A O    1 
ATOM   427  C  CB   . LEU   A 1 292 ? 22.299  -19.563 -4.095  1.00 50.28  ? 303 LEU   A CB   1 
ATOM   428  C  CG   . LEU   A 1 292 ? 22.622  -20.385 -2.852  1.00 56.84  ? 303 LEU   A CG   1 
ATOM   429  C  CD1  . LEU   A 1 292 ? 23.782  -21.336 -3.121  1.00 53.41  ? 303 LEU   A CD1  1 
ATOM   430  C  CD2  . LEU   A 1 292 ? 22.938  -19.448 -1.716  1.00 48.92  ? 303 LEU   A CD2  1 
ATOM   431  N  N    . GLN   A 1 293 ? 20.199  -18.508 -6.302  1.00 65.08  ? 304 GLN   A N    1 
ATOM   432  C  CA   . GLN   A 1 293 ? 19.924  -17.881 -7.593  1.00 77.62  ? 304 GLN   A CA   1 
ATOM   433  C  C    . GLN   A 1 293 ? 19.215  -16.536 -7.469  1.00 76.43  ? 304 GLN   A C    1 
ATOM   434  O  O    . GLN   A 1 293 ? 19.176  -15.777 -8.444  1.00 77.28  ? 304 GLN   A O    1 
ATOM   435  C  CB   . GLN   A 1 293 ? 19.107  -18.828 -8.475  1.00 66.92  ? 304 GLN   A CB   1 
ATOM   436  N  N    . GLN   A 1 294 ? 18.634  -16.233 -6.309  1.00 79.76  ? 305 GLN   A N    1 
ATOM   437  C  CA   . GLN   A 1 294 ? 17.894  -14.996 -6.111  1.00 81.42  ? 305 GLN   A CA   1 
ATOM   438  C  C    . GLN   A 1 294 ? 18.471  -14.106 -5.021  1.00 85.31  ? 305 GLN   A C    1 
ATOM   439  O  O    . GLN   A 1 294 ? 17.850  -13.090 -4.686  1.00 89.13  ? 305 GLN   A O    1 
ATOM   440  C  CB   . GLN   A 1 294 ? 16.429  -15.313 -5.780  1.00 84.78  ? 305 GLN   A CB   1 
ATOM   441  N  N    . GLN   A 1 295 ? 19.615  -14.462 -4.440  1.00 80.61  ? 306 GLN   A N    1 
ATOM   442  C  CA   . GLN   A 1 295 ? 20.299  -13.590 -3.483  1.00 82.73  ? 306 GLN   A CA   1 
ATOM   443  C  C    . GLN   A 1 295 ? 21.131  -12.516 -4.179  1.00 86.33  ? 306 GLN   A C    1 
ATOM   444  O  O    . GLN   A 1 295 ? 21.953  -12.837 -5.043  1.00 89.45  ? 306 GLN   A O    1 
ATOM   445  C  CB   . GLN   A 1 295 ? 21.184  -14.413 -2.557  1.00 77.78  ? 306 GLN   A CB   1 
ATOM   446  C  CG   . GLN   A 1 295 ? 20.393  -15.303 -1.627  1.00 73.63  ? 306 GLN   A CG   1 
ATOM   447  C  CD   . GLN   A 1 295 ? 19.333  -14.539 -0.853  1.00 79.24  ? 306 GLN   A CD   1 
ATOM   448  O  OE1  . GLN   A 1 295 ? 19.515  -13.370 -0.509  1.00 86.65  ? 306 GLN   A OE1  1 
ATOM   449  N  NE2  . GLN   A 1 295 ? 18.219  -15.201 -0.570  1.00 78.21  ? 306 GLN   A NE2  1 
ATOM   450  N  N    . PRO   A 1 296 ? 20.935  -11.233 -3.832  1.00 86.71  ? 307 PRO   A N    1 
ATOM   451  C  CA   . PRO   A 1 296 ? 21.637  -10.142 -4.528  1.00 84.78  ? 307 PRO   A CA   1 
ATOM   452  C  C    . PRO   A 1 296 ? 23.138  -10.108 -4.270  1.00 80.53  ? 307 PRO   A C    1 
ATOM   453  O  O    . PRO   A 1 296 ? 23.939  -10.016 -5.205  1.00 84.74  ? 307 PRO   A O    1 
ATOM   454  C  CB   . PRO   A 1 296 ? 20.961  -8.882  -3.970  1.00 85.92  ? 307 PRO   A CB   1 
ATOM   455  C  CG   . PRO   A 1 296 ? 20.419  -9.297  -2.641  1.00 82.09  ? 307 PRO   A CG   1 
ATOM   456  C  CD   . PRO   A 1 296 ? 20.017  -10.734 -2.793  1.00 88.23  ? 307 PRO   A CD   1 
ATOM   457  N  N    . LYS   A 1 297 ? 23.520  -10.169 -2.997  1.00 75.23  ? 308 LYS   A N    1 
ATOM   458  C  CA   . LYS   A 1 297 ? 24.882  -9.888  -2.539  1.00 66.13  ? 308 LYS   A CA   1 
ATOM   459  C  C    . LYS   A 1 297 ? 25.451  -11.149 -1.890  1.00 60.92  ? 308 LYS   A C    1 
ATOM   460  O  O    . LYS   A 1 297 ? 25.588  -11.225 -0.665  1.00 46.28  ? 308 LYS   A O    1 
ATOM   461  C  CB   . LYS   A 1 297 ? 24.889  -8.691  -1.570  1.00 71.63  ? 308 LYS   A CB   1 
ATOM   462  C  CG   . LYS   A 1 297 ? 24.359  -7.407  -2.201  1.00 66.26  ? 308 LYS   A CG   1 
ATOM   463  C  CD   . LYS   A 1 297 ? 25.196  -6.957  -3.394  1.00 81.19  ? 308 LYS   A CD   1 
ATOM   464  C  CE   . LYS   A 1 297 ? 26.587  -6.490  -3.006  1.00 85.99  ? 308 LYS   A CE   1 
ATOM   465  N  NZ   . LYS   A 1 297 ? 26.534  -5.268  -2.155  1.00 91.90  ? 308 LYS   A NZ   1 
ATOM   466  N  N    . LYS   A 1 298 ? 25.789  -12.140 -2.723  1.00 59.13  ? 309 LYS   A N    1 
ATOM   467  C  CA   . LYS   A 1 298 ? 26.308  -13.407 -2.213  1.00 56.11  ? 309 LYS   A CA   1 
ATOM   468  C  C    . LYS   A 1 298 ? 27.618  -13.227 -1.456  1.00 47.18  ? 309 LYS   A C    1 
ATOM   469  O  O    . LYS   A 1 298 ? 27.885  -13.965 -0.498  1.00 45.13  ? 309 LYS   A O    1 
ATOM   470  C  CB   . LYS   A 1 298 ? 26.500  -14.392 -3.367  1.00 52.35  ? 309 LYS   A CB   1 
ATOM   471  C  CG   . LYS   A 1 298 ? 25.222  -15.084 -3.811  1.00 57.49  ? 309 LYS   A CG   1 
ATOM   472  C  CD   . LYS   A 1 298 ? 25.447  -15.901 -5.076  1.00 68.13  ? 309 LYS   A CD   1 
ATOM   473  C  CE   . LYS   A 1 298 ? 25.213  -15.065 -6.326  1.00 66.51  ? 309 LYS   A CE   1 
ATOM   474  N  NZ   . LYS   A 1 298 ? 23.794  -14.617 -6.425  1.00 65.96  ? 309 LYS   A NZ   1 
ATOM   475  N  N    . GLU   A 1 299 ? 28.431  -12.246 -1.850  1.00 45.98  ? 310 GLU   A N    1 
ATOM   476  C  CA   . GLU   A 1 299 ? 29.684  -11.982 -1.151  1.00 46.34  ? 310 GLU   A CA   1 
ATOM   477  C  C    . GLU   A 1 299 ? 29.428  -11.715 0.326   1.00 39.64  ? 310 GLU   A C    1 
ATOM   478  O  O    . GLU   A 1 299 ? 30.234  -12.085 1.189   1.00 38.83  ? 310 GLU   A O    1 
ATOM   479  C  CB   . GLU   A 1 299 ? 30.372  -10.769 -1.773  1.00 50.87  ? 310 GLU   A CB   1 
ATOM   480  C  CG   . GLU   A 1 299 ? 30.367  -10.772 -3.280  1.00 70.48  ? 310 GLU   A CG   1 
ATOM   481  C  CD   . GLU   A 1 299 ? 29.094  -10.126 -3.822  1.00 71.81  ? 310 GLU   A CD   1 
ATOM   482  O  OE1  . GLU   A 1 299 ? 28.399  -9.446  -3.034  1.00 73.12  ? 310 GLU   A OE1  1 
ATOM   483  O  OE2  . GLU   A 1 299 ? 28.774  -10.313 -5.015  1.00 79.17  ? 310 GLU   A OE2  1 
ATOM   484  N  N    . LEU   A 1 300 ? 28.307  -11.056 0.634   1.00 44.70  ? 311 LEU   A N    1 
ATOM   485  C  CA   . LEU   A 1 300 ? 27.950  -10.786 2.024   1.00 35.89  ? 311 LEU   A CA   1 
ATOM   486  C  C    . LEU   A 1 300 ? 27.604  -12.067 2.772   1.00 37.34  ? 311 LEU   A C    1 
ATOM   487  O  O    . LEU   A 1 300 ? 27.919  -12.198 3.960   1.00 34.96  ? 311 LEU   A O    1 
ATOM   488  C  CB   . LEU   A 1 300 ? 26.784  -9.801  2.081   1.00 37.08  ? 311 LEU   A CB   1 
ATOM   489  C  CG   . LEU   A 1 300 ? 27.102  -8.387  1.579   1.00 47.50  ? 311 LEU   A CG   1 
ATOM   490  C  CD1  . LEU   A 1 300 ? 25.911  -7.464  1.780   1.00 50.95  ? 311 LEU   A CD1  1 
ATOM   491  C  CD2  . LEU   A 1 300 ? 28.340  -7.820  2.261   1.00 39.46  ? 311 LEU   A CD2  1 
ATOM   492  N  N    . ILE   A 1 301 ? 26.926  -13.011 2.107   1.00 35.55  ? 312 ILE   A N    1 
ATOM   493  C  CA   . ILE   A 1 301 ? 26.619  -14.285 2.752   1.00 34.12  ? 312 ILE   A CA   1 
ATOM   494  C  C    . ILE   A 1 301 ? 27.901  -15.023 3.093   1.00 37.53  ? 312 ILE   A C    1 
ATOM   495  O  O    . ILE   A 1 301 ? 28.030  -15.608 4.176   1.00 33.79  ? 312 ILE   A O    1 
ATOM   496  C  CB   . ILE   A 1 301 ? 25.707  -15.149 1.861   1.00 39.51  ? 312 ILE   A CB   1 
ATOM   497  C  CG1  . ILE   A 1 301 ? 24.524  -14.341 1.333   1.00 44.09  ? 312 ILE   A CG1  1 
ATOM   498  C  CG2  . ILE   A 1 301 ? 25.291  -16.422 2.595   1.00 34.90  ? 312 ILE   A CG2  1 
ATOM   499  C  CD1  . ILE   A 1 301 ? 23.705  -13.721 2.416   1.00 52.07  ? 312 ILE   A CD1  1 
ATOM   500  N  N    . ILE   A 1 302 ? 28.866  -15.004 2.170   1.00 35.40  ? 313 ILE   A N    1 
ATOM   501  C  CA   . ILE   A 1 302 ? 30.147  -15.673 2.384   1.00 33.59  ? 313 ILE   A CA   1 
ATOM   502  C  C    . ILE   A 1 302 ? 30.833  -15.099 3.613   1.00 33.53  ? 313 ILE   A C    1 
ATOM   503  O  O    . ILE   A 1 302 ? 31.296  -15.833 4.494   1.00 34.53  ? 313 ILE   A O    1 
ATOM   504  C  CB   . ILE   A 1 302 ? 31.034  -15.520 1.135   1.00 34.79  ? 313 ILE   A CB   1 
ATOM   505  C  CG1  . ILE   A 1 302 ? 30.451  -16.310 -0.040  1.00 36.50  ? 313 ILE   A CG1  1 
ATOM   506  C  CG2  . ILE   A 1 302 ? 32.474  -15.961 1.437   1.00 34.46  ? 313 ILE   A CG2  1 
ATOM   507  C  CD1  . ILE   A 1 302 ? 31.208  -16.121 -1.338  1.00 43.02  ? 313 ILE   A CD1  1 
ATOM   508  N  N    A ASN   A 1 303 ? 30.897  -13.769 3.694   0.69 33.67  ? 314 ASN   A N    1 
ATOM   509  N  N    B ASN   A 1 303 ? 30.898  -13.769 3.697   0.31 33.69  ? 314 ASN   A N    1 
ATOM   510  C  CA   A ASN   A 1 303 ? 31.564  -13.121 4.818   0.69 35.40  ? 314 ASN   A CA   1 
ATOM   511  C  CA   B ASN   A 1 303 ? 31.563  -13.128 4.827   0.31 35.40  ? 314 ASN   A CA   1 
ATOM   512  C  C    A ASN   A 1 303 ? 30.888  -13.470 6.139   0.69 33.52  ? 314 ASN   A C    1 
ATOM   513  C  C    B ASN   A 1 303 ? 30.887  -13.488 6.142   0.31 33.55  ? 314 ASN   A C    1 
ATOM   514  O  O    A ASN   A 1 303 ? 31.565  -13.805 7.116   0.69 32.59  ? 314 ASN   A O    1 
ATOM   515  O  O    B ASN   A 1 303 ? 31.557  -13.836 7.120   0.31 32.64  ? 314 ASN   A O    1 
ATOM   516  C  CB   A ASN   A 1 303 ? 31.597  -11.605 4.599   0.69 38.46  ? 314 ASN   A CB   1 
ATOM   517  C  CB   B ASN   A 1 303 ? 31.589  -11.612 4.632   0.31 38.40  ? 314 ASN   A CB   1 
ATOM   518  C  CG   A ASN   A 1 303 ? 32.431  -10.876 5.638   0.69 36.93  ? 314 ASN   A CG   1 
ATOM   519  C  CG   B ASN   A 1 303 ? 32.564  -11.186 3.562   0.31 34.05  ? 314 ASN   A CG   1 
ATOM   520  O  OD1  A ASN   A 1 303 ? 31.913  -10.060 6.401   0.69 42.00  ? 314 ASN   A OD1  1 
ATOM   521  O  OD1  B ASN   A 1 303 ? 33.532  -11.888 3.282   0.31 42.30  ? 314 ASN   A OD1  1 
ATOM   522  N  ND2  A ASN   A 1 303 ? 33.728  -11.165 5.673   0.69 31.74  ? 314 ASN   A ND2  1 
ATOM   523  N  ND2  B ASN   A 1 303 ? 32.317  -10.031 2.956   0.31 46.34  ? 314 ASN   A ND2  1 
ATOM   524  N  N    . GLU   A 1 304 ? 29.554  -13.427 6.183   1.00 32.37  ? 315 GLU   A N    1 
ATOM   525  C  CA   . GLU   A 1 304 ? 28.865  -13.682 7.446   1.00 33.34  ? 315 GLU   A CA   1 
ATOM   526  C  C    . GLU   A 1 304 ? 29.074  -15.120 7.907   1.00 31.13  ? 315 GLU   A C    1 
ATOM   527  O  O    . GLU   A 1 304 ? 29.359  -15.359 9.084   1.00 32.57  ? 315 GLU   A O    1 
ATOM   528  C  CB   . GLU   A 1 304 ? 27.371  -13.355 7.336   1.00 33.44  ? 315 GLU   A CB   1 
ATOM   529  C  CG   . GLU   A 1 304 ? 26.601  -13.640 8.642   1.00 30.03  ? 315 GLU   A CG   1 
ATOM   530  C  CD   . GLU   A 1 304 ? 25.178  -13.080 8.672   1.00 33.27  ? 315 GLU   A CD   1 
ATOM   531  O  OE1  . GLU   A 1 304 ? 24.676  -12.632 7.620   1.00 37.54  ? 315 GLU   A OE1  1 
ATOM   532  O  OE2  . GLU   A 1 304 ? 24.566  -13.075 9.771   1.00 38.94  ? 315 GLU   A OE2  1 
ATOM   533  N  N    . ILE   A 1 305 ? 29.003  -16.089 6.988   1.00 32.19  ? 316 ILE   A N    1 
ATOM   534  C  CA   . ILE   A 1 305 ? 29.229  -17.480 7.377   1.00 29.38  ? 316 ILE   A CA   1 
ATOM   535  C  C    . ILE   A 1 305 ? 30.657  -17.669 7.868   1.00 30.19  ? 316 ILE   A C    1 
ATOM   536  O  O    . ILE   A 1 305 ? 30.897  -18.285 8.914   1.00 30.27  ? 316 ILE   A O    1 
ATOM   537  C  CB   . ILE   A 1 305 ? 28.912  -18.433 6.208   1.00 29.60  ? 316 ILE   A CB   1 
ATOM   538  C  CG1  . ILE   A 1 305 ? 27.410  -18.431 5.900   1.00 30.21  ? 316 ILE   A CG1  1 
ATOM   539  C  CG2  . ILE   A 1 305 ? 29.436  -19.835 6.496   1.00 29.78  ? 316 ILE   A CG2  1 
ATOM   540  C  CD1  . ILE   A 1 305 ? 27.049  -19.312 4.713   1.00 36.39  ? 316 ILE   A CD1  1 
ATOM   541  N  N    . LEU   A 1 306 ? 31.625  -17.133 7.126   1.00 31.70  ? 317 LEU   A N    1 
ATOM   542  C  CA   . LEU   A 1 306 ? 33.020  -17.281 7.525   1.00 32.68  ? 317 LEU   A CA   1 
ATOM   543  C  C    . LEU   A 1 306 ? 33.282  -16.649 8.892   1.00 35.40  ? 317 LEU   A C    1 
ATOM   544  O  O    . LEU   A 1 306 ? 33.980  -17.232 9.732   1.00 35.49  ? 317 LEU   A O    1 
ATOM   545  C  CB   . LEU   A 1 306 ? 33.927  -16.694 6.440   1.00 31.25  ? 317 LEU   A CB   1 
ATOM   546  C  CG   . LEU   A 1 306 ? 34.001  -17.652 5.243   1.00 32.86  ? 317 LEU   A CG   1 
ATOM   547  C  CD1  . LEU   A 1 306 ? 34.862  -17.140 4.073   1.00 36.87  ? 317 LEU   A CD1  1 
ATOM   548  C  CD2  . LEU   A 1 306 ? 34.455  -19.044 5.681   1.00 39.36  ? 317 LEU   A CD2  1 
ATOM   549  N  N    . VAL   A 1 307 ? 32.736  -15.454 9.131   1.00 32.08  ? 318 VAL   A N    1 
ATOM   550  C  CA   . VAL   A 1 307 ? 32.957  -14.773 10.404  1.00 31.58  ? 318 VAL   A CA   1 
ATOM   551  C  C    . VAL   A 1 307 ? 32.325  -15.556 11.548  1.00 33.04  ? 318 VAL   A C    1 
ATOM   552  O  O    . VAL   A 1 307 ? 32.938  -15.730 12.608  1.00 32.83  ? 318 VAL   A O    1 
ATOM   553  C  CB   . VAL   A 1 307 ? 32.434  -13.328 10.338  1.00 38.39  ? 318 VAL   A CB   1 
ATOM   554  C  CG1  . VAL   A 1 307 ? 32.446  -12.697 11.716  1.00 35.05  ? 318 VAL   A CG1  1 
ATOM   555  C  CG2  . VAL   A 1 307 ? 33.304  -12.504 9.408   1.00 43.47  ? 318 VAL   A CG2  1 
ATOM   556  N  N    . MET   A 1 308 ? 31.097  -16.050 11.355  1.00 32.07  ? 319 MET   A N    1 
ATOM   557  C  CA   . MET   A 1 308 ? 30.433  -16.796 12.424  1.00 38.88  ? 319 MET   A CA   1 
ATOM   558  C  C    . MET   A 1 308 ? 31.188  -18.078 12.759  1.00 37.39  ? 319 MET   A C    1 
ATOM   559  O  O    . MET   A 1 308 ? 31.319  -18.442 13.934  1.00 34.81  ? 319 MET   A O    1 
ATOM   560  C  CB   . MET   A 1 308 ? 28.992  -17.132 12.031  1.00 32.48  ? 319 MET   A CB   1 
ATOM   561  C  CG   . MET   A 1 308 ? 28.095  -15.941 11.794  1.00 28.80  ? 319 MET   A CG   1 
ATOM   562  S  SD   . MET   A 1 308 ? 28.340  -14.640 12.992  1.00 39.35  ? 319 MET   A SD   1 
ATOM   563  C  CE   . MET   A 1 308 ? 27.582  -15.385 14.431  1.00 33.95  ? 319 MET   A CE   1 
ATOM   564  N  N    . ARG   A 1 309 ? 31.701  -18.780 11.738  1.00 29.43  ? 320 ARG   A N    1 
ATOM   565  C  CA   . ARG   A 1 309 ? 32.426  -20.022 11.982  1.00 30.38  ? 320 ARG   A CA   1 
ATOM   566  C  C    . ARG   A 1 309 ? 33.680  -19.782 12.800  1.00 38.09  ? 320 ARG   A C    1 
ATOM   567  O  O    . ARG   A 1 309 ? 34.089  -20.646 13.584  1.00 38.11  ? 320 ARG   A O    1 
ATOM   568  C  CB   . ARG   A 1 309 ? 32.817  -20.653 10.647  1.00 32.87  ? 320 ARG   A CB   1 
ATOM   569  C  CG   . ARG   A 1 309 ? 31.673  -21.230 9.880   1.00 38.80  ? 320 ARG   A CG   1 
ATOM   570  C  CD   . ARG   A 1 309 ? 32.207  -21.941 8.652   1.00 36.78  ? 320 ARG   A CD   1 
ATOM   571  N  NE   . ARG   A 1 309 ? 31.146  -22.633 7.939   1.00 38.82  ? 320 ARG   A NE   1 
ATOM   572  C  CZ   . ARG   A 1 309 ? 31.276  -23.121 6.715   1.00 40.31  ? 320 ARG   A CZ   1 
ATOM   573  N  NH1  . ARG   A 1 309 ? 32.398  -22.969 6.028   1.00 36.98  ? 320 ARG   A NH1  1 
ATOM   574  N  NH2  . ARG   A 1 309 ? 30.247  -23.750 6.158   1.00 38.86  ? 320 ARG   A NH2  1 
ATOM   575  N  N    . GLU   A 1 310 ? 34.321  -18.638 12.594  1.00 31.51  ? 321 GLU   A N    1 
ATOM   576  C  CA   . GLU   A 1 310 ? 35.600  -18.321 13.210  1.00 37.52  ? 321 GLU   A CA   1 
ATOM   577  C  C    . GLU   A 1 310 ? 35.474  -17.613 14.551  1.00 43.03  ? 321 GLU   A C    1 
ATOM   578  O  O    . GLU   A 1 310 ? 36.483  -17.467 15.245  1.00 45.15  ? 321 GLU   A O    1 
ATOM   579  C  CB   . GLU   A 1 310 ? 36.430  -17.479 12.236  1.00 36.46  ? 321 GLU   A CB   1 
ATOM   580  C  CG   . GLU   A 1 310 ? 36.751  -18.250 10.957  1.00 43.86  ? 321 GLU   A CG   1 
ATOM   581  C  CD   . GLU   A 1 310 ? 37.277  -17.375 9.841   1.00 58.82  ? 321 GLU   A CD   1 
ATOM   582  O  OE1  . GLU   A 1 310 ? 37.558  -16.184 10.097  1.00 60.50  ? 321 GLU   A OE1  1 
ATOM   583  O  OE2  . GLU   A 1 310 ? 37.394  -17.879 8.702   1.00 58.51  ? 321 GLU   A OE2  1 
ATOM   584  N  N    . ASN   A 1 311 ? 34.270  -17.158 14.938  1.00 35.62  ? 322 ASN   A N    1 
ATOM   585  C  CA   . ASN   A 1 311 ? 34.119  -16.333 16.133  1.00 33.44  ? 322 ASN   A CA   1 
ATOM   586  C  C    . ASN   A 1 311 ? 32.902  -16.785 16.951  1.00 42.14  ? 322 ASN   A C    1 
ATOM   587  O  O    . ASN   A 1 311 ? 31.892  -16.096 17.059  1.00 46.04  ? 322 ASN   A O    1 
ATOM   588  C  CB   . ASN   A 1 311 ? 34.020  -14.851 15.762  1.00 37.63  ? 322 ASN   A CB   1 
ATOM   589  C  CG   . ASN   A 1 311 ? 35.210  -14.378 14.959  1.00 43.27  ? 322 ASN   A CG   1 
ATOM   590  O  OD1  . ASN   A 1 311 ? 36.261  -14.062 15.518  1.00 44.08  ? 322 ASN   A OD1  1 
ATOM   591  N  ND2  . ASN   A 1 311 ? 35.049  -14.306 13.632  1.00 34.98  ? 322 ASN   A ND2  1 
ATOM   592  N  N    . LYS   A 1 312 ? 32.994  -17.959 17.567  1.00 34.12  ? 323 LYS   A N    1 
ATOM   593  C  CA   . LYS   A 1 312 ? 31.917  -18.431 18.424  1.00 34.56  ? 323 LYS   A CA   1 
ATOM   594  C  C    . LYS   A 1 312 ? 32.109  -17.904 19.845  1.00 38.03  ? 323 LYS   A C    1 
ATOM   595  O  O    . LYS   A 1 312 ? 33.237  -17.815 20.342  1.00 35.10  ? 323 LYS   A O    1 
ATOM   596  C  CB   . LYS   A 1 312 ? 31.867  -19.958 18.386  1.00 42.00  ? 323 LYS   A CB   1 
ATOM   597  C  CG   . LYS   A 1 312 ? 31.520  -20.453 16.988  1.00 40.54  ? 323 LYS   A CG   1 
ATOM   598  C  CD   . LYS   A 1 312 ? 31.370  -21.946 16.895  1.00 39.79  ? 323 LYS   A CD   1 
ATOM   599  C  CE   . LYS   A 1 312 ? 30.800  -22.321 15.541  1.00 40.83  ? 323 LYS   A CE   1 
ATOM   600  N  NZ   . LYS   A 1 312 ? 30.699  -23.804 15.375  1.00 50.54  ? 323 LYS   A NZ   1 
ATOM   601  N  N    . ASN   A 1 313 ? 30.988  -17.570 20.502  1.00 31.44  ? 324 ASN   A N    1 
ATOM   602  C  CA   . ASN   A 1 313 ? 31.046  -16.900 21.795  1.00 36.26  ? 324 ASN   A CA   1 
ATOM   603  C  C    . ASN   A 1 313 ? 29.689  -17.001 22.468  1.00 32.78  ? 324 ASN   A C    1 
ATOM   604  O  O    . ASN   A 1 313 ? 28.670  -16.957 21.768  1.00 31.67  ? 324 ASN   A O    1 
ATOM   605  C  CB   . ASN   A 1 313 ? 31.447  -15.433 21.611  1.00 32.65  ? 324 ASN   A CB   1 
ATOM   606  C  CG   . ASN   A 1 313 ? 31.605  -14.711 22.903  1.00 35.76  ? 324 ASN   A CG   1 
ATOM   607  O  OD1  . ASN   A 1 313 ? 30.654  -14.133 23.428  1.00 33.07  ? 324 ASN   A OD1  1 
ATOM   608  N  ND2  . ASN   A 1 313 ? 32.821  -14.717 23.431  1.00 37.41  ? 324 ASN   A ND2  1 
ATOM   609  N  N    . PRO   A 1 314 ? 29.626  -17.148 23.796  1.00 28.54  ? 325 PRO   A N    1 
ATOM   610  C  CA   . PRO   A 1 314 ? 28.315  -17.262 24.465  1.00 35.78  ? 325 PRO   A CA   1 
ATOM   611  C  C    . PRO   A 1 314 ? 27.387  -16.061 24.255  1.00 31.94  ? 325 PRO   A C    1 
ATOM   612  O  O    . PRO   A 1 314 ? 26.171  -16.216 24.428  1.00 29.20  ? 325 PRO   A O    1 
ATOM   613  C  CB   . PRO   A 1 314 ? 28.691  -17.422 25.946  1.00 36.76  ? 325 PRO   A CB   1 
ATOM   614  C  CG   . PRO   A 1 314 ? 30.092  -17.979 25.914  1.00 34.50  ? 325 PRO   A CG   1 
ATOM   615  C  CD   . PRO   A 1 314 ? 30.746  -17.335 24.731  1.00 38.21  ? 325 PRO   A CD   1 
ATOM   616  N  N    . ASN   A 1 315 ? 27.905  -14.872 23.939  1.00 30.18  ? 326 ASN   A N    1 
ATOM   617  C  CA   . ASN   A 1 315 ? 27.051  -13.699 23.754  1.00 27.86  ? 326 ASN   A CA   1 
ATOM   618  C  C    . ASN   A 1 315 ? 26.800  -13.400 22.280  1.00 26.06  ? 326 ASN   A C    1 
ATOM   619  O  O    . ASN   A 1 315 ? 26.465  -12.258 21.921  1.00 27.04  ? 326 ASN   A O    1 
ATOM   620  C  CB   . ASN   A 1 315 ? 27.648  -12.476 24.450  1.00 28.01  ? 326 ASN   A CB   1 
ATOM   621  C  CG   . ASN   A 1 315 ? 27.559  -12.560 25.979  1.00 30.40  ? 326 ASN   A CG   1 
ATOM   622  O  OD1  . ASN   A 1 315 ? 28.585  -12.595 26.661  1.00 33.30  ? 326 ASN   A OD1  1 
ATOM   623  N  ND2  . ASN   A 1 315 ? 26.334  -12.565 26.518  1.00 29.13  ? 326 ASN   A ND2  1 
ATOM   624  N  N    . ILE   A 1 316 ? 26.980  -14.395 21.422  1.00 26.94  ? 327 ILE   A N    1 
ATOM   625  C  CA   . ILE   A 1 316 ? 26.689  -14.295 19.998  1.00 25.80  ? 327 ILE   A CA   1 
ATOM   626  C  C    . ILE   A 1 316 ? 25.729  -15.412 19.612  1.00 28.56  ? 327 ILE   A C    1 
ATOM   627  O  O    . ILE   A 1 316 ? 25.812  -16.517 20.160  1.00 35.74  ? 327 ILE   A O    1 
ATOM   628  C  CB   . ILE   A 1 316 ? 27.990  -14.379 19.176  1.00 26.33  ? 327 ILE   A CB   1 
ATOM   629  C  CG1  . ILE   A 1 316 ? 28.845  -13.136 19.413  1.00 26.82  ? 327 ILE   A CG1  1 
ATOM   630  C  CG2  . ILE   A 1 316 ? 27.696  -14.562 17.722  1.00 34.29  ? 327 ILE   A CG2  1 
ATOM   631  C  CD1  . ILE   A 1 316 ? 30.207  -13.216 18.736  1.00 36.95  ? 327 ILE   A CD1  1 
ATOM   632  N  N    . VAL   A 1 317 ? 24.758  -15.105 18.751  1.00 24.53  ? 328 VAL   A N    1 
ATOM   633  C  CA   . VAL   A 1 317 ? 23.890  -16.152 18.217  1.00 24.43  ? 328 VAL   A CA   1 
ATOM   634  C  C    . VAL   A 1 317 ? 24.759  -17.026 17.316  1.00 28.57  ? 328 VAL   A C    1 
ATOM   635  O  O    . VAL   A 1 317 ? 25.132  -16.615 16.214  1.00 30.90  ? 328 VAL   A O    1 
ATOM   636  C  CB   . VAL   A 1 317 ? 22.696  -15.570 17.450  1.00 25.17  ? 328 VAL   A CB   1 
ATOM   637  C  CG1  . VAL   A 1 317 ? 21.858  -16.689 16.841  1.00 28.04  ? 328 VAL   A CG1  1 
ATOM   638  C  CG2  . VAL   A 1 317 ? 21.837  -14.691 18.364  1.00 26.94  ? 328 VAL   A CG2  1 
ATOM   639  N  N    . ASN   A 1 318 ? 25.069  -18.231 17.762  1.00 26.65  ? 329 ASN   A N    1 
ATOM   640  C  CA   . ASN   A 1 318 ? 26.118  -18.997 17.098  1.00 28.76  ? 329 ASN   A CA   1 
ATOM   641  C  C    . ASN   A 1 318 ? 25.628  -19.779 15.883  1.00 28.14  ? 329 ASN   A C    1 
ATOM   642  O  O    . ASN   A 1 318 ? 24.464  -20.173 15.783  1.00 30.27  ? 329 ASN   A O    1 
ATOM   643  C  CB   . ASN   A 1 318 ? 26.823  -19.906 18.095  1.00 32.98  ? 329 ASN   A CB   1 
ATOM   644  C  CG   . ASN   A 1 318 ? 27.691  -19.118 19.061  1.00 39.74  ? 329 ASN   A CG   1 
ATOM   645  O  OD1  . ASN   A 1 318 ? 28.587  -18.370 18.651  1.00 32.92  ? 329 ASN   A OD1  1 
ATOM   646  N  ND2  . ASN   A 1 318 ? 27.402  -19.246 20.349  1.00 44.53  ? 329 ASN   A ND2  1 
ATOM   647  N  N    . TYR   A 1 319 ? 26.540  -19.944 14.928  1.00 28.85  ? 330 TYR   A N    1 
ATOM   648  C  CA   . TYR   A 1 319 ? 26.338  -20.792 13.765  1.00 27.17  ? 330 TYR   A CA   1 
ATOM   649  C  C    . TYR   A 1 319 ? 26.568  -22.249 14.146  1.00 32.39  ? 330 TYR   A C    1 
ATOM   650  O  O    . TYR   A 1 319 ? 27.555  -22.576 14.814  1.00 37.09  ? 330 TYR   A O    1 
ATOM   651  C  CB   . TYR   A 1 319 ? 27.310  -20.375 12.650  1.00 36.69  ? 330 TYR   A CB   1 
ATOM   652  C  CG   . TYR   A 1 319 ? 27.519  -21.393 11.536  1.00 42.12  ? 330 TYR   A CG   1 
ATOM   653  C  CD1  . TYR   A 1 319 ? 28.401  -22.465 11.703  1.00 38.32  ? 330 TYR   A CD1  1 
ATOM   654  C  CD2  . TYR   A 1 319 ? 26.869  -21.265 10.315  1.00 34.65  ? 330 TYR   A CD2  1 
ATOM   655  C  CE1  . TYR   A 1 319 ? 28.601  -23.402 10.696  1.00 42.42  ? 330 TYR   A CE1  1 
ATOM   656  C  CE2  . TYR   A 1 319 ? 27.068  -22.185 9.300   1.00 34.11  ? 330 TYR   A CE2  1 
ATOM   657  C  CZ   . TYR   A 1 319 ? 27.935  -23.253 9.495   1.00 42.67  ? 330 TYR   A CZ   1 
ATOM   658  O  OH   . TYR   A 1 319 ? 28.129  -24.175 8.495   1.00 40.20  ? 330 TYR   A OH   1 
ATOM   659  N  N    . LEU   A 1 320 ? 25.649  -23.121 13.730  1.00 30.65  ? 331 LEU   A N    1 
ATOM   660  C  CA   . LEU   A 1 320 ? 25.713  -24.552 14.017  1.00 27.68  ? 331 LEU   A CA   1 
ATOM   661  C  C    . LEU   A 1 320 ? 26.094  -25.374 12.800  1.00 40.26  ? 331 LEU   A C    1 
ATOM   662  O  O    . LEU   A 1 320 ? 26.984  -26.224 12.887  1.00 39.09  ? 331 LEU   A O    1 
ATOM   663  C  CB   . LEU   A 1 320 ? 24.380  -25.062 14.575  1.00 28.14  ? 331 LEU   A CB   1 
ATOM   664  C  CG   . LEU   A 1 320 ? 23.969  -24.332 15.850  1.00 38.84  ? 331 LEU   A CG   1 
ATOM   665  C  CD1  . LEU   A 1 320 ? 22.592  -24.787 16.290  1.00 31.65  ? 331 LEU   A CD1  1 
ATOM   666  C  CD2  . LEU   A 1 320 ? 25.011  -24.562 16.941  1.00 41.17  ? 331 LEU   A CD2  1 
ATOM   667  N  N    . ASP   A 1 321 ? 25.400  -25.180 11.682  1.00 33.59  ? 332 ASP   A N    1 
ATOM   668  C  CA   . ASP   A 1 321 ? 25.596  -26.022 10.509  1.00 38.30  ? 332 ASP   A CA   1 
ATOM   669  C  C    . ASP   A 1 321 ? 25.005  -25.309 9.300   1.00 36.58  ? 332 ASP   A C    1 
ATOM   670  O  O    . ASP   A 1 321 ? 24.291  -24.314 9.430   1.00 31.21  ? 332 ASP   A O    1 
ATOM   671  C  CB   . ASP   A 1 321 ? 24.944  -27.392 10.709  1.00 38.65  ? 332 ASP   A CB   1 
ATOM   672  C  CG   . ASP   A 1 321 ? 25.875  -28.536 10.365  1.00 54.78  ? 332 ASP   A CG   1 
ATOM   673  O  OD1  . ASP   A 1 321 ? 26.628  -28.439 9.365   1.00 48.96  ? 332 ASP   A OD1  1 
ATOM   674  O  OD2  . ASP   A 1 321 ? 25.848  -29.538 11.108  1.00 60.68  ? 332 ASP   A OD2  1 
ATOM   675  N  N    . SER   A 1 322 ? 25.323  -25.823 8.115   1.00 34.52  ? 333 SER   A N    1 
ATOM   676  C  CA   . SER   A 1 322 ? 24.718  -25.308 6.891   1.00 39.28  ? 333 SER   A CA   1 
ATOM   677  C  C    . SER   A 1 322 ? 24.728  -26.414 5.843   1.00 44.92  ? 333 SER   A C    1 
ATOM   678  O  O    . SER   A 1 322 ? 25.558  -27.326 5.905   1.00 42.45  ? 333 SER   A O    1 
ATOM   679  C  CB   . SER   A 1 322 ? 25.444  -24.053 6.379   1.00 33.66  ? 333 SER   A CB   1 
ATOM   680  O  OG   . SER   A 1 322 ? 26.830  -24.315 6.192   1.00 40.41  ? 333 SER   A OG   1 
ATOM   681  N  N    . TYR   A 1 323 ? 23.797  -26.323 4.883   1.00 38.83  ? 334 TYR   A N    1 
ATOM   682  C  CA   . TYR   A 1 323 ? 23.585  -27.373 3.891   1.00 41.72  ? 334 TYR   A CA   1 
ATOM   683  C  C    . TYR   A 1 323 ? 23.265  -26.768 2.533   1.00 43.24  ? 334 TYR   A C    1 
ATOM   684  O  O    . TYR   A 1 323 ? 22.518  -25.789 2.440   1.00 42.79  ? 334 TYR   A O    1 
ATOM   685  C  CB   . TYR   A 1 323 ? 22.430  -28.317 4.270   1.00 43.31  ? 334 TYR   A CB   1 
ATOM   686  C  CG   . TYR   A 1 323 ? 22.571  -28.971 5.618   1.00 43.73  ? 334 TYR   A CG   1 
ATOM   687  C  CD1  . TYR   A 1 323 ? 22.153  -28.317 6.773   1.00 40.50  ? 334 TYR   A CD1  1 
ATOM   688  C  CD2  . TYR   A 1 323 ? 23.108  -30.246 5.739   1.00 50.24  ? 334 TYR   A CD2  1 
ATOM   689  C  CE1  . TYR   A 1 323 ? 22.277  -28.915 8.015   1.00 39.24  ? 334 TYR   A CE1  1 
ATOM   690  C  CE2  . TYR   A 1 323 ? 23.234  -30.855 6.977   1.00 44.34  ? 334 TYR   A CE2  1 
ATOM   691  C  CZ   . TYR   A 1 323 ? 22.822  -30.186 8.109   1.00 45.29  ? 334 TYR   A CZ   1 
ATOM   692  O  OH   . TYR   A 1 323 ? 22.949  -30.793 9.341   1.00 53.24  ? 334 TYR   A OH   1 
ATOM   693  N  N    . LEU   A 1 324 ? 23.823  -27.375 1.486   1.00 45.35  ? 335 LEU   A N    1 
ATOM   694  C  CA   . LEU   A 1 324 ? 23.464  -27.086 0.103   1.00 52.06  ? 335 LEU   A CA   1 
ATOM   695  C  C    . LEU   A 1 324 ? 22.457  -28.119 -0.389  1.00 53.00  ? 335 LEU   A C    1 
ATOM   696  O  O    . LEU   A 1 324 ? 22.780  -29.311 -0.466  1.00 52.62  ? 335 LEU   A O    1 
ATOM   697  C  CB   . LEU   A 1 324 ? 24.692  -27.109 -0.806  1.00 52.96  ? 335 LEU   A CB   1 
ATOM   698  C  CG   . LEU   A 1 324 ? 25.609  -25.901 -0.940  1.00 57.12  ? 335 LEU   A CG   1 
ATOM   699  C  CD1  . LEU   A 1 324 ? 26.563  -26.145 -2.113  1.00 49.17  ? 335 LEU   A CD1  1 
ATOM   700  C  CD2  . LEU   A 1 324 ? 24.805  -24.617 -1.127  1.00 50.08  ? 335 LEU   A CD2  1 
ATOM   701  N  N    . VAL   A 1 325 ? 21.251  -27.669 -0.722  1.00 52.09  ? 336 VAL   A N    1 
ATOM   702  C  CA   . VAL   A 1 325 ? 20.214  -28.529 -1.298  1.00 63.46  ? 336 VAL   A CA   1 
ATOM   703  C  C    . VAL   A 1 325 ? 19.892  -27.963 -2.678  1.00 68.10  ? 336 VAL   A C    1 
ATOM   704  O  O    . VAL   A 1 325 ? 19.017  -27.103 -2.832  1.00 58.43  ? 336 VAL   A O    1 
ATOM   705  C  CB   . VAL   A 1 325 ? 18.965  -28.619 -0.421  1.00 59.04  ? 336 VAL   A CB   1 
ATOM   706  C  CG1  . VAL   A 1 325 ? 18.003  -29.656 -0.988  1.00 65.07  ? 336 VAL   A CG1  1 
ATOM   707  C  CG2  . VAL   A 1 325 ? 19.348  -28.970 1.004   1.00 57.48  ? 336 VAL   A CG2  1 
ATOM   708  N  N    . GLY   A 1 326 ? 20.584  -28.466 -3.696  1.00 68.76  ? 337 GLY   A N    1 
ATOM   709  C  CA   . GLY   A 1 326 ? 20.397  -27.955 -5.045  1.00 65.47  ? 337 GLY   A CA   1 
ATOM   710  C  C    . GLY   A 1 326 ? 20.768  -26.483 -5.080  1.00 75.36  ? 337 GLY   A C    1 
ATOM   711  O  O    . GLY   A 1 326 ? 21.916  -26.099 -4.815  1.00 65.81  ? 337 GLY   A O    1 
ATOM   712  N  N    . ASP   A 1 327 ? 19.792  -25.636 -5.405  1.00 67.15  ? 338 ASP   A N    1 
ATOM   713  C  CA   . ASP   A 1 327 ? 19.994  -24.194 -5.423  1.00 59.40  ? 338 ASP   A CA   1 
ATOM   714  C  C    . ASP   A 1 327 ? 19.556  -23.549 -4.118  1.00 60.82  ? 338 ASP   A C    1 
ATOM   715  O  O    . ASP   A 1 327 ? 19.454  -22.319 -4.049  1.00 65.34  ? 338 ASP   A O    1 
ATOM   716  C  CB   . ASP   A 1 327 ? 19.227  -23.561 -6.585  1.00 62.65  ? 338 ASP   A CB   1 
ATOM   717  C  CG   . ASP   A 1 327 ? 19.925  -23.750 -7.916  1.00 77.87  ? 338 ASP   A CG   1 
ATOM   718  O  OD1  . ASP   A 1 327 ? 21.173  -23.696 -7.952  1.00 76.31  ? 338 ASP   A OD1  1 
ATOM   719  O  OD2  . ASP   A 1 327 ? 19.221  -23.953 -8.929  1.00 87.99  ? 338 ASP   A OD2  1 
ATOM   720  N  N    . GLU   A 1 328 ? 19.306  -24.346 -3.084  1.00 59.36  ? 339 GLU   A N    1 
ATOM   721  C  CA   . GLU   A 1 328 ? 18.922  -23.842 -1.772  1.00 56.37  ? 339 GLU   A CA   1 
ATOM   722  C  C    . GLU   A 1 328 ? 20.067  -23.965 -0.772  1.00 49.14  ? 339 GLU   A C    1 
ATOM   723  O  O    . GLU   A 1 328 ? 20.724  -25.009 -0.689  1.00 49.90  ? 339 GLU   A O    1 
ATOM   724  C  CB   . GLU   A 1 328 ? 17.693  -24.615 -1.292  1.00 64.25  ? 339 GLU   A CB   1 
ATOM   725  C  CG   . GLU   A 1 328 ? 16.419  -24.185 -2.012  1.00 76.18  ? 339 GLU   A CG   1 
ATOM   726  C  CD   . GLU   A 1 328 ? 15.174  -24.892 -1.514  1.00 77.37  ? 339 GLU   A CD   1 
ATOM   727  O  OE1  . GLU   A 1 328 ? 15.292  -25.776 -0.639  1.00 71.06  ? 339 GLU   A OE1  1 
ATOM   728  O  OE2  . GLU   A 1 328 ? 14.076  -24.570 -2.016  1.00 80.41  ? 339 GLU   A OE2  1 
ATOM   729  N  N    . LEU   A 1 329 ? 20.298  -22.894 -0.019  1.00 46.48  ? 340 LEU   A N    1 
ATOM   730  C  CA   . LEU   A 1 329 ? 21.206  -22.873 1.119   1.00 43.40  ? 340 LEU   A CA   1 
ATOM   731  C  C    . LEU   A 1 329 ? 20.379  -22.849 2.398   1.00 47.07  ? 340 LEU   A C    1 
ATOM   732  O  O    . LEU   A 1 329 ? 19.506  -21.989 2.553   1.00 42.30  ? 340 LEU   A O    1 
ATOM   733  C  CB   . LEU   A 1 329 ? 22.129  -21.653 1.060   1.00 41.64  ? 340 LEU   A CB   1 
ATOM   734  C  CG   . LEU   A 1 329 ? 23.003  -21.407 2.288   1.00 41.18  ? 340 LEU   A CG   1 
ATOM   735  C  CD1  . LEU   A 1 329 ? 23.939  -22.576 2.538   1.00 38.40  ? 340 LEU   A CD1  1 
ATOM   736  C  CD2  . LEU   A 1 329 ? 23.785  -20.100 2.141   1.00 48.69  ? 340 LEU   A CD2  1 
ATOM   737  N  N    . TRP   A 1 330 ? 20.625  -23.805 3.293   1.00 41.23  ? 341 TRP   A N    1 
ATOM   738  C  CA   . TRP   A 1 330 ? 19.986  -23.838 4.606   1.00 39.95  ? 341 TRP   A CA   1 
ATOM   739  C  C    . TRP   A 1 330 ? 21.043  -23.562 5.672   1.00 37.14  ? 341 TRP   A C    1 
ATOM   740  O  O    . TRP   A 1 330 ? 22.041  -24.284 5.764   1.00 36.76  ? 341 TRP   A O    1 
ATOM   741  C  CB   . TRP   A 1 330 ? 19.309  -25.191 4.829   1.00 41.64  ? 341 TRP   A CB   1 
ATOM   742  C  CG   . TRP   A 1 330 ? 18.209  -25.461 3.843   1.00 48.40  ? 341 TRP   A CG   1 
ATOM   743  C  CD1  . TRP   A 1 330 ? 18.356  -25.783 2.519   1.00 52.21  ? 341 TRP   A CD1  1 
ATOM   744  C  CD2  . TRP   A 1 330 ? 16.799  -25.442 4.095   1.00 46.31  ? 341 TRP   A CD2  1 
ATOM   745  N  NE1  . TRP   A 1 330 ? 17.124  -25.959 1.936   1.00 55.56  ? 341 TRP   A NE1  1 
ATOM   746  C  CE2  . TRP   A 1 330 ? 16.152  -25.754 2.881   1.00 49.68  ? 341 TRP   A CE2  1 
ATOM   747  C  CE3  . TRP   A 1 330 ? 16.020  -25.180 5.225   1.00 50.48  ? 341 TRP   A CE3  1 
ATOM   748  C  CZ2  . TRP   A 1 330 ? 14.765  -25.817 2.769   1.00 52.21  ? 341 TRP   A CZ2  1 
ATOM   749  C  CZ3  . TRP   A 1 330 ? 14.643  -25.244 5.112   1.00 49.07  ? 341 TRP   A CZ3  1 
ATOM   750  C  CH2  . TRP   A 1 330 ? 14.030  -25.563 3.893   1.00 51.31  ? 341 TRP   A CH2  1 
ATOM   751  N  N    . VAL   A 1 331 ? 20.834  -22.528 6.476   1.00 35.52  ? 342 VAL   A N    1 
ATOM   752  C  CA   . VAL   A 1 331 ? 21.780  -22.134 7.512   1.00 33.17  ? 342 VAL   A CA   1 
ATOM   753  C  C    . VAL   A 1 331 ? 21.144  -22.377 8.872   1.00 32.36  ? 342 VAL   A C    1 
ATOM   754  O  O    . VAL   A 1 331 ? 20.018  -21.939 9.111   1.00 32.88  ? 342 VAL   A O    1 
ATOM   755  C  CB   . VAL   A 1 331 ? 22.198  -20.664 7.349   1.00 36.56  ? 342 VAL   A CB   1 
ATOM   756  C  CG1  . VAL   A 1 331 ? 23.041  -20.218 8.529   1.00 32.50  ? 342 VAL   A CG1  1 
ATOM   757  C  CG2  . VAL   A 1 331 ? 22.982  -20.509 6.047   1.00 38.28  ? 342 VAL   A CG2  1 
ATOM   758  N  N    . VAL   A 1 332 ? 21.867  -23.061 9.757   1.00 31.35  ? 343 VAL   A N    1 
ATOM   759  C  CA   . VAL   A 1 332 ? 21.358  -23.465 11.064  1.00 30.81  ? 343 VAL   A CA   1 
ATOM   760  C  C    . VAL   A 1 332 ? 22.079  -22.665 12.141  1.00 28.99  ? 343 VAL   A C    1 
ATOM   761  O  O    . VAL   A 1 332 ? 23.312  -22.730 12.255  1.00 28.28  ? 343 VAL   A O    1 
ATOM   762  C  CB   . VAL   A 1 332 ? 21.545  -24.968 11.307  1.00 31.80  ? 343 VAL   A CB   1 
ATOM   763  C  CG1  . VAL   A 1 332 ? 20.865  -25.368 12.629  1.00 31.45  ? 343 VAL   A CG1  1 
ATOM   764  C  CG2  . VAL   A 1 332 ? 21.004  -25.771 10.149  1.00 33.95  ? 343 VAL   A CG2  1 
ATOM   765  N  N    . MET   A 1 333 ? 21.301  -21.931 12.946  1.00 28.44  ? 344 MET   A N    1 
ATOM   766  C  CA   . MET   A 1 333 ? 21.786  -21.090 14.028  1.00 34.73  ? 344 MET   A CA   1 
ATOM   767  C  C    . MET   A 1 333 ? 21.138  -21.510 15.342  1.00 31.48  ? 344 MET   A C    1 
ATOM   768  O  O    . MET   A 1 333 ? 20.115  -22.205 15.359  1.00 29.29  ? 344 MET   A O    1 
ATOM   769  C  CB   . MET   A 1 333 ? 21.473  -19.605 13.765  1.00 34.12  ? 344 MET   A CB   1 
ATOM   770  C  CG   . MET   A 1 333 ? 21.845  -19.155 12.371  1.00 32.94  ? 344 MET   A CG   1 
ATOM   771  S  SD   . MET   A 1 333 ? 23.635  -19.151 12.144  1.00 31.49  ? 344 MET   A SD   1 
ATOM   772  C  CE   . MET   A 1 333 ? 24.116  -17.734 13.152  1.00 31.28  ? 344 MET   A CE   1 
ATOM   773  N  N    . GLU   A 1 334 ? 21.750  -21.093 16.450  1.00 28.11  ? 345 GLU   A N    1 
ATOM   774  C  CA   . GLU   A 1 334 ? 21.069  -21.209 17.739  1.00 30.25  ? 345 GLU   A CA   1 
ATOM   775  C  C    . GLU   A 1 334 ? 19.741  -20.464 17.678  1.00 26.67  ? 345 GLU   A C    1 
ATOM   776  O  O    . GLU   A 1 334 ? 19.604  -19.459 16.977  1.00 31.37  ? 345 GLU   A O    1 
ATOM   777  C  CB   . GLU   A 1 334 ? 21.916  -20.602 18.863  1.00 30.98  ? 345 GLU   A CB   1 
ATOM   778  C  CG   . GLU   A 1 334 ? 23.245  -21.289 19.151  1.00 35.43  ? 345 GLU   A CG   1 
ATOM   779  C  CD   . GLU   A 1 334 ? 24.047  -20.554 20.225  1.00 53.75  ? 345 GLU   A CD   1 
ATOM   780  O  OE1  . GLU   A 1 334 ? 23.974  -19.302 20.290  1.00 33.54  ? 345 GLU   A OE1  1 
ATOM   781  O  OE2  . GLU   A 1 334 ? 24.744  -21.230 21.012  1.00 60.91  ? 345 GLU   A OE2  1 
ATOM   782  N  N    . TYR   A 1 335 ? 18.746  -20.959 18.417  1.00 27.37  ? 346 TYR   A N    1 
ATOM   783  C  CA   . TYR   A 1 335 ? 17.438  -20.324 18.473  1.00 29.93  ? 346 TYR   A CA   1 
ATOM   784  C  C    . TYR   A 1 335 ? 17.241  -19.664 19.834  1.00 30.01  ? 346 TYR   A C    1 
ATOM   785  O  O    . TYR   A 1 335 ? 17.436  -20.304 20.872  1.00 30.20  ? 346 TYR   A O    1 
ATOM   786  C  CB   . TYR   A 1 335 ? 16.314  -21.330 18.199  1.00 34.98  ? 346 TYR   A CB   1 
ATOM   787  C  CG   . TYR   A 1 335 ? 14.933  -20.755 18.428  1.00 31.30  ? 346 TYR   A CG   1 
ATOM   788  C  CD1  . TYR   A 1 335 ? 14.432  -19.742 17.621  1.00 32.16  ? 346 TYR   A CD1  1 
ATOM   789  C  CD2  . TYR   A 1 335 ? 14.111  -21.254 19.441  1.00 32.54  ? 346 TYR   A CD2  1 
ATOM   790  C  CE1  . TYR   A 1 335 ? 13.160  -19.217 17.839  1.00 33.84  ? 346 TYR   A CE1  1 
ATOM   791  C  CE2  . TYR   A 1 335 ? 12.845  -20.743 19.654  1.00 38.65  ? 346 TYR   A CE2  1 
ATOM   792  C  CZ   . TYR   A 1 335 ? 12.374  -19.731 18.852  1.00 37.18  ? 346 TYR   A CZ   1 
ATOM   793  O  OH   . TYR   A 1 335 ? 11.116  -19.225 19.073  1.00 36.51  ? 346 TYR   A OH   1 
ATOM   794  N  N    . LEU   A 1 336 ? 16.872  -18.392 19.821  1.00 30.91  ? 347 LEU   A N    1 
ATOM   795  C  CA   . LEU   A 1 336 ? 16.672  -17.602 21.035  1.00 31.84  ? 347 LEU   A CA   1 
ATOM   796  C  C    . LEU   A 1 336 ? 15.173  -17.368 21.194  1.00 29.38  ? 347 LEU   A C    1 
ATOM   797  O  O    . LEU   A 1 336 ? 14.583  -16.572 20.458  1.00 32.05  ? 347 LEU   A O    1 
ATOM   798  C  CB   . LEU   A 1 336 ? 17.450  -16.289 20.953  1.00 29.91  ? 347 LEU   A CB   1 
ATOM   799  C  CG   . LEU   A 1 336 ? 18.925  -16.362 21.383  1.00 31.87  ? 347 LEU   A CG   1 
ATOM   800  C  CD1  . LEU   A 1 336 ? 19.038  -16.743 22.842  1.00 40.79  ? 347 LEU   A CD1  1 
ATOM   801  C  CD2  . LEU   A 1 336 ? 19.727  -17.368 20.534  1.00 30.35  ? 347 LEU   A CD2  1 
ATOM   802  N  N    . ALA   A 1 337 ? 14.549  -18.070 22.137  1.00 29.87  ? 348 ALA   A N    1 
ATOM   803  C  CA   . ALA   A 1 337 ? 13.093  -18.067 22.207  1.00 29.96  ? 348 ALA   A CA   1 
ATOM   804  C  C    . ALA   A 1 337 ? 12.521  -16.822 22.879  1.00 30.99  ? 348 ALA   A C    1 
ATOM   805  O  O    . ALA   A 1 337 ? 11.301  -16.617 22.834  1.00 36.26  ? 348 ALA   A O    1 
ATOM   806  C  CB   . ALA   A 1 337 ? 12.609  -19.311 22.957  1.00 33.53  ? 348 ALA   A CB   1 
ATOM   807  N  N    . GLY   A 1 338 ? 13.359  -15.985 23.482  1.00 25.68  ? 349 GLY   A N    1 
ATOM   808  C  CA   . GLY   A 1 338 ? 12.841  -14.783 24.131  1.00 28.82  ? 349 GLY   A CA   1 
ATOM   809  C  C    . GLY   A 1 338 ? 12.509  -13.628 23.213  1.00 29.61  ? 349 GLY   A C    1 
ATOM   810  O  O    . GLY   A 1 338 ? 12.000  -12.609 23.691  1.00 28.21  ? 349 GLY   A O    1 
ATOM   811  N  N    . GLY   A 1 339 ? 12.821  -13.733 21.922  1.00 28.52  ? 350 GLY   A N    1 
ATOM   812  C  CA   . GLY   A 1 339 ? 12.532  -12.660 20.998  1.00 27.66  ? 350 GLY   A CA   1 
ATOM   813  C  C    . GLY   A 1 339 ? 13.624  -11.607 20.994  1.00 24.08  ? 350 GLY   A C    1 
ATOM   814  O  O    . GLY   A 1 339 ? 14.685  -11.756 21.604  1.00 25.49  ? 350 GLY   A O    1 
ATOM   815  N  N    . SER   A 1 340 ? 13.346  -10.515 20.295  1.00 25.70  ? 351 SER   A N    1 
ATOM   816  C  CA   . SER   A 1 340 ? 14.316  -9.432  20.155  1.00 21.78  ? 351 SER   A CA   1 
ATOM   817  C  C    . SER   A 1 340 ? 14.241  -8.432  21.310  1.00 19.84  ? 351 SER   A C    1 
ATOM   818  O  O    . SER   A 1 340 ? 13.205  -8.256  21.955  1.00 22.49  ? 351 SER   A O    1 
ATOM   819  C  CB   . SER   A 1 340 ? 14.079  -8.677  18.849  1.00 25.33  ? 351 SER   A CB   1 
ATOM   820  O  OG   . SER   A 1 340 ? 12.869  -7.926  18.952  1.00 27.05  ? 351 SER   A OG   1 
ATOM   821  N  N    . LEU   A 1 341 ? 15.359  -7.735  21.530  1.00 20.32  ? 352 LEU   A N    1 
ATOM   822  C  CA   . LEU   A 1 341 ? 15.358  -6.617  22.460  1.00 21.13  ? 352 LEU   A CA   1 
ATOM   823  C  C    . LEU   A 1 341 ? 14.428  -5.499  21.979  1.00 20.72  ? 352 LEU   A C    1 
ATOM   824  O  O    . LEU   A 1 341 ? 13.857  -4.785  22.803  1.00 19.19  ? 352 LEU   A O    1 
ATOM   825  C  CB   . LEU   A 1 341 ? 16.792  -6.113  22.671  1.00 21.86  ? 352 LEU   A CB   1 
ATOM   826  C  CG   . LEU   A 1 341 ? 16.977  -4.906  23.605  1.00 18.41  ? 352 LEU   A CG   1 
ATOM   827  C  CD1  . LEU   A 1 341 ? 16.473  -5.251  25.027  1.00 22.39  ? 352 LEU   A CD1  1 
ATOM   828  C  CD2  . LEU   A 1 341 ? 18.454  -4.466  23.630  1.00 23.99  ? 352 LEU   A CD2  1 
ATOM   829  N  N    . THR   A 1 342 ? 14.236  -5.352  20.654  1.00 21.31  ? 353 THR   A N    1 
ATOM   830  C  CA   . THR   A 1 342 ? 13.315  -4.329  20.141  1.00 24.40  ? 353 THR   A CA   1 
ATOM   831  C  C    . THR   A 1 342 ? 11.915  -4.479  20.733  1.00 24.59  ? 353 THR   A C    1 
ATOM   832  O  O    . THR   A 1 342 ? 11.285  -3.486  21.121  1.00 22.43  ? 353 THR   A O    1 
ATOM   833  C  CB   . THR   A 1 342 ? 13.231  -4.384  18.613  1.00 25.27  ? 353 THR   A CB   1 
ATOM   834  O  OG1  . THR   A 1 342 ? 14.535  -4.289  18.056  1.00 22.91  ? 353 THR   A OG1  1 
ATOM   835  C  CG2  . THR   A 1 342 ? 12.396  -3.243  18.072  1.00 25.99  ? 353 THR   A CG2  1 
ATOM   836  N  N    . ASP   A 1 343 ? 11.396  -5.714  20.784  1.00 22.39  ? 354 ASP   A N    1 
ATOM   837  C  CA   . ASP   A 1 343 ? 10.068  -5.916  21.349  1.00 23.57  ? 354 ASP   A CA   1 
ATOM   838  C  C    . ASP   A 1 343 ? 10.028  -5.441  22.797  1.00 27.32  ? 354 ASP   A C    1 
ATOM   839  O  O    . ASP   A 1 343 ? 9.038   -4.847  23.234  1.00 23.15  ? 354 ASP   A O    1 
ATOM   840  C  CB   . ASP   A 1 343 ? 9.660   -7.391  21.271  1.00 21.48  ? 354 ASP   A CB   1 
ATOM   841  C  CG   . ASP   A 1 343 ? 9.462   -7.890  19.843  1.00 34.79  ? 354 ASP   A CG   1 
ATOM   842  O  OD1  . ASP   A 1 343 ? 9.416   -7.078  18.889  1.00 31.34  ? 354 ASP   A OD1  1 
ATOM   843  O  OD2  . ASP   A 1 343 ? 9.352   -9.118  19.683  1.00 35.97  ? 354 ASP   A OD2  1 
ATOM   844  N  N    . VAL   A 1 344 ? 11.100  -5.690  23.555  1.00 22.54  ? 355 VAL   A N    1 
ATOM   845  C  CA   . VAL   A 1 344 ? 11.162  -5.233  24.948  1.00 22.63  ? 355 VAL   A CA   1 
ATOM   846  C  C    . VAL   A 1 344 ? 11.232  -3.703  25.034  1.00 22.11  ? 355 VAL   A C    1 
ATOM   847  O  O    . VAL   A 1 344 ? 10.508  -3.076  25.822  1.00 21.05  ? 355 VAL   A O    1 
ATOM   848  C  CB   . VAL   A 1 344 ? 12.358  -5.897  25.659  1.00 21.22  ? 355 VAL   A CB   1 
ATOM   849  C  CG1  . VAL   A 1 344 ? 12.698  -5.183  26.965  1.00 23.97  ? 355 VAL   A CG1  1 
ATOM   850  C  CG2  . VAL   A 1 344 ? 12.092  -7.403  25.887  1.00 23.44  ? 355 VAL   A CG2  1 
ATOM   851  N  N    . VAL   A 1 345 ? 12.123  -3.066  24.259  1.00 22.68  ? 356 VAL   A N    1 
ATOM   852  C  CA   . VAL   A 1 345 ? 12.300  -1.618  24.453  1.00 20.94  ? 356 VAL   A CA   1 
ATOM   853  C  C    . VAL   A 1 345 ? 11.070  -0.842  23.996  1.00 22.50  ? 356 VAL   A C    1 
ATOM   854  O  O    . VAL   A 1 345 ? 10.790  0.254   24.504  1.00 22.46  ? 356 VAL   A O    1 
ATOM   855  C  CB   . VAL   A 1 345 ? 13.578  -1.083  23.778  1.00 23.08  ? 356 VAL   A CB   1 
ATOM   856  C  CG1  . VAL   A 1 345 ? 14.820  -1.810  24.307  1.00 24.34  ? 356 VAL   A CG1  1 
ATOM   857  C  CG2  . VAL   A 1 345 ? 13.471  -1.173  22.283  1.00 24.31  ? 356 VAL   A CG2  1 
ATOM   858  N  N    . THR   A 1 346 ? 10.342  -1.350  23.015  1.00 20.44  ? 357 THR   A N    1 
ATOM   859  C  CA   . THR   A 1 346 ? 9.198   -0.604  22.516  1.00 24.61  ? 357 THR   A CA   1 
ATOM   860  C  C    . THR   A 1 346 ? 7.929   -0.854  23.323  1.00 27.35  ? 357 THR   A C    1 
ATOM   861  O  O    . THR   A 1 346 ? 6.946   -0.141  23.124  1.00 25.17  ? 357 THR   A O    1 
ATOM   862  C  CB   . THR   A 1 346 ? 8.929   -0.935  21.043  1.00 34.68  ? 357 THR   A CB   1 
ATOM   863  O  OG1  . THR   A 1 346 ? 8.655   -2.330  20.908  1.00 26.49  ? 357 THR   A OG1  1 
ATOM   864  C  CG2  . THR   A 1 346 ? 10.137  -0.580  20.163  1.00 22.35  ? 357 THR   A CG2  1 
ATOM   865  N  N    . GLU   A 1 347 ? 7.897   -1.880  24.172  1.00 24.79  ? 358 GLU   A N    1 
ATOM   866  C  CA   . GLU   A 1 347 ? 6.677   -2.250  24.884  1.00 31.05  ? 358 GLU   A CA   1 
ATOM   867  C  C    . GLU   A 1 347 ? 6.790   -2.249  26.403  1.00 28.43  ? 358 GLU   A C    1 
ATOM   868  O  O    . GLU   A 1 347 ? 5.782   -2.520  27.081  1.00 28.30  ? 358 GLU   A O    1 
ATOM   869  C  CB   . GLU   A 1 347 ? 6.211   -3.644  24.434  1.00 28.08  ? 358 GLU   A CB   1 
ATOM   870  C  CG   . GLU   A 1 347 ? 5.917   -3.769  22.947  1.00 24.04  ? 358 GLU   A CG   1 
ATOM   871  C  CD   . GLU   A 1 347 ? 4.750   -2.907  22.467  1.00 35.90  ? 358 GLU   A CD   1 
ATOM   872  O  OE1  . GLU   A 1 347 ? 3.989   -2.376  23.294  1.00 34.12  ? 358 GLU   A OE1  1 
ATOM   873  O  OE2  . GLU   A 1 347 ? 4.572   -2.782  21.241  1.00 36.54  ? 358 GLU   A OE2  1 
ATOM   874  N  N    . THR   A 1 348 ? 7.973   -1.992  26.968  1.00 22.91  ? 359 THR   A N    1 
ATOM   875  C  CA   . THR   A 1 348 ? 8.151   -2.057  28.414  1.00 27.11  ? 359 THR   A CA   1 
ATOM   876  C  C    . THR   A 1 348 ? 8.982   -0.880  28.905  1.00 28.60  ? 359 THR   A C    1 
ATOM   877  O  O    . THR   A 1 348 ? 9.650   -0.186  28.137  1.00 27.24  ? 359 THR   A O    1 
ATOM   878  C  CB   . THR   A 1 348 ? 8.840   -3.354  28.884  1.00 29.33  ? 359 THR   A CB   1 
ATOM   879  O  OG1  . THR   A 1 348 ? 10.236  -3.303  28.563  1.00 24.36  ? 359 THR   A OG1  1 
ATOM   880  C  CG2  . THR   A 1 348 ? 8.220   -4.596  28.268  1.00 27.13  ? 359 THR   A CG2  1 
ATOM   881  N  N    . CYS   A 1 349 ? 8.959   -0.691  30.215  1.00 25.91  ? 360 CYS   A N    1 
ATOM   882  C  CA   . CYS   A 1 349 ? 9.873   0.208   30.903  1.00 28.43  ? 360 CYS   A CA   1 
ATOM   883  C  C    . CYS   A 1 349 ? 10.944  -0.629  31.600  1.00 29.07  ? 360 CYS   A C    1 
ATOM   884  O  O    . CYS   A 1 349 ? 10.620  -1.508  32.405  1.00 32.90  ? 360 CYS   A O    1 
ATOM   885  C  CB   . CYS   A 1 349 ? 9.092   1.075   31.900  1.00 39.15  ? 360 CYS   A CB   1 
ATOM   886  S  SG   . CYS   A 1 349 ? 10.050  1.714   33.270  1.00 44.21  ? 360 CYS   A SG   1 
ATOM   887  N  N    . MET   A 1 350 ? 12.205  -0.429  31.217  1.00 21.64  ? 361 MET   A N    1 
ATOM   888  C  CA   . MET   A 1 350 ? 13.331  -1.129  31.837  1.00 22.18  ? 361 MET   A CA   1 
ATOM   889  C  C    . MET   A 1 350 ? 13.923  -0.273  32.945  1.00 25.87  ? 361 MET   A C    1 
ATOM   890  O  O    . MET   A 1 350 ? 14.076  0.937   32.780  1.00 26.27  ? 361 MET   A O    1 
ATOM   891  C  CB   . MET   A 1 350 ? 14.411  -1.435  30.797  1.00 25.74  ? 361 MET   A CB   1 
ATOM   892  C  CG   . MET   A 1 350 ? 13.904  -2.188  29.602  1.00 23.56  ? 361 MET   A CG   1 
ATOM   893  S  SD   . MET   A 1 350 ? 15.219  -2.524  28.392  1.00 26.85  ? 361 MET   A SD   1 
ATOM   894  C  CE   . MET   A 1 350 ? 16.299  -3.588  29.318  1.00 22.97  ? 361 MET   A CE   1 
ATOM   895  N  N    . ASP   A 1 351 ? 14.267  -0.891  34.069  1.00 20.19  ? 362 ASP   A N    1 
ATOM   896  C  CA   . ASP   A 1 351 ? 14.940  -0.118  35.104  1.00 23.17  ? 362 ASP   A CA   1 
ATOM   897  C  C    . ASP   A 1 351 ? 16.448  -0.157  34.865  1.00 28.16  ? 362 ASP   A C    1 
ATOM   898  O  O    . ASP   A 1 351 ? 16.941  -0.903  34.019  1.00 22.45  ? 362 ASP   A O    1 
ATOM   899  C  CB   . ASP   A 1 351 ? 14.571  -0.620  36.509  1.00 23.54  ? 362 ASP   A CB   1 
ATOM   900  C  CG   . ASP   A 1 351 ? 15.043  -2.051  36.797  1.00 29.27  ? 362 ASP   A CG   1 
ATOM   901  O  OD1  . ASP   A 1 351 ? 16.189  -2.426  36.459  1.00 31.15  ? 362 ASP   A OD1  1 
ATOM   902  O  OD2  . ASP   A 1 351 ? 14.275  -2.796  37.450  1.00 31.85  ? 362 ASP   A OD2  1 
ATOM   903  N  N    . GLU   A 1 352 ? 17.193  0.655   35.622  1.00 24.34  ? 363 GLU   A N    1 
ATOM   904  C  CA   . GLU   A 1 352 ? 18.622  0.778   35.328  1.00 23.18  ? 363 GLU   A CA   1 
ATOM   905  C  C    . GLU   A 1 352 ? 19.379  -0.526  35.561  1.00 25.82  ? 363 GLU   A C    1 
ATOM   906  O  O    . GLU   A 1 352 ? 20.357  -0.804  34.856  1.00 26.40  ? 363 GLU   A O    1 
ATOM   907  C  CB   . GLU   A 1 352 ? 19.256  1.905   36.144  1.00 22.59  ? 363 GLU   A CB   1 
ATOM   908  C  CG   . GLU   A 1 352 ? 18.879  3.290   35.625  1.00 28.80  ? 363 GLU   A CG   1 
ATOM   909  C  CD   . GLU   A 1 352 ? 19.741  4.401   36.194  1.00 33.52  ? 363 GLU   A CD   1 
ATOM   910  O  OE1  . GLU   A 1 352 ? 20.783  4.116   36.832  1.00 27.60  ? 363 GLU   A OE1  1 
ATOM   911  O  OE2  . GLU   A 1 352 ? 19.374  5.574   35.993  1.00 28.92  ? 363 GLU   A OE2  1 
ATOM   912  N  N    . GLY   A 1 353 ? 18.946  -1.344  36.519  1.00 25.69  ? 364 GLY   A N    1 
ATOM   913  C  CA   . GLY   A 1 353 ? 19.603  -2.627  36.712  1.00 28.95  ? 364 GLY   A CA   1 
ATOM   914  C  C    . GLY   A 1 353 ? 19.422  -3.570  35.532  1.00 24.56  ? 364 GLY   A C    1 
ATOM   915  O  O    . GLY   A 1 353 ? 20.337  -4.322  35.181  1.00 25.33  ? 364 GLY   A O    1 
ATOM   916  N  N    . GLN   A 1 354 ? 18.242  -3.556  34.909  1.00 24.09  ? 365 GLN   A N    1 
ATOM   917  C  CA   . GLN   A 1 354 ? 18.033  -4.381  33.717  1.00 21.80  ? 365 GLN   A CA   1 
ATOM   918  C  C    . GLN   A 1 354 ? 18.826  -3.840  32.534  1.00 24.77  ? 365 GLN   A C    1 
ATOM   919  O  O    . GLN   A 1 354 ? 19.375  -4.611  31.731  1.00 23.97  ? 365 GLN   A O    1 
ATOM   920  C  CB   . GLN   A 1 354 ? 16.543  -4.443  33.376  1.00 20.83  ? 365 GLN   A CB   1 
ATOM   921  C  CG   . GLN   A 1 354 ? 15.692  -5.141  34.466  1.00 25.33  ? 365 GLN   A CG   1 
ATOM   922  C  CD   . GLN   A 1 354 ? 14.193  -4.851  34.356  1.00 24.15  ? 365 GLN   A CD   1 
ATOM   923  O  OE1  . GLN   A 1 354 ? 13.779  -3.715  34.117  1.00 23.11  ? 365 GLN   A OE1  1 
ATOM   924  N  NE2  . GLN   A 1 354 ? 13.372  -5.890  34.519  1.00 26.43  ? 365 GLN   A NE2  1 
ATOM   925  N  N    . ILE   A 1 355 ? 18.867  -2.521  32.393  1.00 20.93  ? 366 ILE   A N    1 
ATOM   926  C  CA   . ILE   A 1 355 ? 19.646  -1.921  31.312  1.00 23.55  ? 366 ILE   A CA   1 
ATOM   927  C  C    . ILE   A 1 355 ? 21.125  -2.237  31.492  1.00 28.18  ? 366 ILE   A C    1 
ATOM   928  O  O    . ILE   A 1 355 ? 21.823  -2.607  30.537  1.00 22.71  ? 366 ILE   A O    1 
ATOM   929  C  CB   . ILE   A 1 355 ? 19.398  -0.408  31.247  1.00 22.55  ? 366 ILE   A CB   1 
ATOM   930  C  CG1  . ILE   A 1 355 ? 17.943  -0.118  30.853  1.00 19.89  ? 366 ILE   A CG1  1 
ATOM   931  C  CG2  . ILE   A 1 355 ? 20.389  0.246   30.257  1.00 24.98  ? 366 ILE   A CG2  1 
ATOM   932  C  CD1  . ILE   A 1 355 ? 17.621  1.379   30.856  1.00 25.78  ? 366 ILE   A CD1  1 
ATOM   933  N  N    . ALA   A 1 356 ? 21.622  -2.097  32.725  1.00 21.49  ? 367 ALA   A N    1 
ATOM   934  C  CA   . ALA   A 1 356 ? 23.024  -2.405  33.002  1.00 26.26  ? 367 ALA   A CA   1 
ATOM   935  C  C    . ALA   A 1 356 ? 23.358  -3.856  32.660  1.00 29.21  ? 367 ALA   A C    1 
ATOM   936  O  O    . ALA   A 1 356 ? 24.425  -4.136  32.098  1.00 27.56  ? 367 ALA   A O    1 
ATOM   937  C  CB   . ALA   A 1 356 ? 23.338  -2.119  34.473  1.00 24.97  ? 367 ALA   A CB   1 
ATOM   938  N  N    . ALA   A 1 357 ? 22.447  -4.790  32.962  1.00 23.58  ? 368 ALA   A N    1 
ATOM   939  C  CA   . ALA   A 1 357 ? 22.701  -6.198  32.640  1.00 24.03  ? 368 ALA   A CA   1 
ATOM   940  C  C    . ALA   A 1 357 ? 22.815  -6.408  31.136  1.00 26.08  ? 368 ALA   A C    1 
ATOM   941  O  O    . ALA   A 1 357 ? 23.734  -7.088  30.665  1.00 25.28  ? 368 ALA   A O    1 
ATOM   942  C  CB   . ALA   A 1 357 ? 21.604  -7.095  33.217  1.00 22.93  ? 368 ALA   A CB   1 
ATOM   943  N  N    . VAL   A 1 358 ? 21.888  -5.832  30.368  1.00 22.99  ? 369 VAL   A N    1 
ATOM   944  C  CA   . VAL   A 1 358 ? 21.933  -5.952  28.909  1.00 24.11  ? 369 VAL   A CA   1 
ATOM   945  C  C    . VAL   A 1 358 ? 23.220  -5.342  28.360  1.00 26.52  ? 369 VAL   A C    1 
ATOM   946  O  O    . VAL   A 1 358 ? 23.883  -5.928  27.497  1.00 26.42  ? 369 VAL   A O    1 
ATOM   947  C  CB   . VAL   A 1 358 ? 20.687  -5.307  28.274  1.00 21.78  ? 369 VAL   A CB   1 
ATOM   948  C  CG1  . VAL   A 1 358 ? 20.842  -5.257  26.732  1.00 20.65  ? 369 VAL   A CG1  1 
ATOM   949  C  CG2  . VAL   A 1 358 ? 19.437  -6.090  28.640  1.00 22.33  ? 369 VAL   A CG2  1 
ATOM   950  N  N    . CYS   A 1 359 ? 23.584  -4.149  28.841  1.00 20.97  ? 370 CYS   A N    1 
ATOM   951  C  CA   . CYS   A 1 359 ? 24.809  -3.499  28.367  1.00 22.45  ? 370 CYS   A CA   1 
ATOM   952  C  C    . CYS   A 1 359 ? 26.044  -4.355  28.634  1.00 24.67  ? 370 CYS   A C    1 
ATOM   953  O  O    . CYS   A 1 359 ? 26.934  -4.467  27.774  1.00 22.74  ? 370 CYS   A O    1 
ATOM   954  C  CB   . CYS   A 1 359 ? 24.970  -2.127  29.021  1.00 22.46  ? 370 CYS   A CB   1 
ATOM   955  S  SG   . CYS   A 1 359 ? 23.775  -0.907  28.408  1.00 25.85  ? 370 CYS   A SG   1 
ATOM   956  N  N    . ARG   A 1 360 ? 26.124  -4.960  29.817  1.00 20.07  ? 371 ARG   A N    1 
ATOM   957  C  CA   . ARG   A 1 360 ? 27.289  -5.781  30.132  1.00 23.07  ? 371 ARG   A CA   1 
ATOM   958  C  C    . ARG   A 1 360 ? 27.393  -6.983  29.201  1.00 25.53  ? 371 ARG   A C    1 
ATOM   959  O  O    . ARG   A 1 360 ? 28.487  -7.326  28.744  1.00 25.59  ? 371 ARG   A O    1 
ATOM   960  C  CB   . ARG   A 1 360 ? 27.255  -6.254  31.584  1.00 25.63  ? 371 ARG   A CB   1 
ATOM   961  C  CG   . ARG   A 1 360 ? 28.513  -7.068  31.929  1.00 27.41  ? 371 ARG   A CG   1 
ATOM   962  C  CD   . ARG   A 1 360 ? 28.322  -7.887  33.198  1.00 33.30  ? 371 ARG   A CD   1 
ATOM   963  N  NE   . ARG   A 1 360 ? 27.259  -8.855  32.971  1.00 36.39  ? 371 ARG   A NE   1 
ATOM   964  C  CZ   . ARG   A 1 360 ? 26.182  -8.981  33.731  1.00 48.24  ? 371 ARG   A CZ   1 
ATOM   965  N  NH1  . ARG   A 1 360 ? 26.074  -8.338  34.883  1.00 46.61  ? 371 ARG   A NH1  1 
ATOM   966  N  NH2  . ARG   A 1 360 ? 25.189  -9.765  33.319  1.00 41.85  ? 371 ARG   A NH2  1 
ATOM   967  N  N    . GLU   A 1 361 ? 26.274  -7.657  28.933  1.00 25.09  ? 372 GLU   A N    1 
ATOM   968  C  CA   . GLU   A 1 361 ? 26.325  -8.805  28.031  1.00 25.73  ? 372 GLU   A CA   1 
ATOM   969  C  C    . GLU   A 1 361 ? 26.748  -8.378  26.627  1.00 26.93  ? 372 GLU   A C    1 
ATOM   970  O  O    . GLU   A 1 361 ? 27.529  -9.073  25.963  1.00 22.52  ? 372 GLU   A O    1 
ATOM   971  C  CB   . GLU   A 1 361 ? 24.965  -9.505  27.993  1.00 25.13  ? 372 GLU   A CB   1 
ATOM   972  C  CG   . GLU   A 1 361 ? 24.530  -10.109 29.360  1.00 25.96  ? 372 GLU   A CG   1 
ATOM   973  C  CD   . GLU   A 1 361 ? 25.526  -11.130 29.899  1.00 33.70  ? 372 GLU   A CD   1 
ATOM   974  O  OE1  . GLU   A 1 361 ? 25.749  -12.185 29.260  1.00 28.08  ? 372 GLU   A OE1  1 
ATOM   975  O  OE2  . GLU   A 1 361 ? 26.112  -10.872 30.971  1.00 36.49  ? 372 GLU   A OE2  1 
ATOM   976  N  N    . CYS   A 1 362 ? 26.248  -7.233  26.159  1.00 19.21  ? 373 CYS   A N    1 
ATOM   977  C  CA   . CYS   A 1 362 ? 26.640  -6.748  24.833  1.00 26.75  ? 373 CYS   A CA   1 
ATOM   978  C  C    . CYS   A 1 362 ? 28.108  -6.335  24.790  1.00 27.92  ? 373 CYS   A C    1 
ATOM   979  O  O    . CYS   A 1 362 ? 28.805  -6.594  23.800  1.00 22.07  ? 373 CYS   A O    1 
ATOM   980  C  CB   . CYS   A 1 362 ? 25.753  -5.579  24.417  1.00 24.17  ? 373 CYS   A CB   1 
ATOM   981  S  SG   . CYS   A 1 362 ? 24.030  -6.058  24.106  1.00 28.71  ? 373 CYS   A SG   1 
ATOM   982  N  N    . LEU   A 1 363 ? 28.598  -5.692  25.853  1.00 22.55  ? 374 LEU   A N    1 
ATOM   983  C  CA   . LEU   A 1 363 ? 30.014  -5.328  25.903  1.00 25.81  ? 374 LEU   A CA   1 
ATOM   984  C  C    . LEU   A 1 363 ? 30.915  -6.555  25.944  1.00 27.94  ? 374 LEU   A C    1 
ATOM   985  O  O    . LEU   A 1 363 ? 32.044  -6.515  25.440  1.00 28.81  ? 374 LEU   A O    1 
ATOM   986  C  CB   . LEU   A 1 363 ? 30.280  -4.427  27.114  1.00 29.87  ? 374 LEU   A CB   1 
ATOM   987  C  CG   . LEU   A 1 363 ? 29.854  -2.968  26.933  1.00 25.30  ? 374 LEU   A CG   1 
ATOM   988  C  CD1  . LEU   A 1 363 ? 29.829  -2.227  28.277  1.00 26.41  ? 374 LEU   A CD1  1 
ATOM   989  C  CD2  . LEU   A 1 363 ? 30.785  -2.268  25.948  1.00 29.54  ? 374 LEU   A CD2  1 
ATOM   990  N  N    . GLN   A 1 364 ? 30.457  -7.647  26.561  1.00 24.59  ? 375 GLN   A N    1 
ATOM   991  C  CA   . GLN   A 1 364 ? 31.243  -8.883  26.518  1.00 25.04  ? 375 GLN   A CA   1 
ATOM   992  C  C    . GLN   A 1 364 ? 31.384  -9.404  25.091  1.00 33.35  ? 375 GLN   A C    1 
ATOM   993  O  O    . GLN   A 1 364 ? 32.476  -9.830  24.686  1.00 28.66  ? 375 GLN   A O    1 
ATOM   994  C  CB   . GLN   A 1 364 ? 30.614  -9.937  27.437  1.00 27.29  ? 375 GLN   A CB   1 
ATOM   995  C  CG   . GLN   A 1 364 ? 30.745  -9.565  28.902  1.00 28.42  ? 375 GLN   A CG   1 
ATOM   996  C  CD   . GLN   A 1 364 ? 29.910  -10.414 29.857  1.00 34.37  ? 375 GLN   A CD   1 
ATOM   997  O  OE1  . GLN   A 1 364 ? 29.176  -11.316 29.452  1.00 35.63  ? 375 GLN   A OE1  1 
ATOM   998  N  NE2  . GLN   A 1 364 ? 30.012  -10.108 31.138  1.00 30.09  ? 375 GLN   A NE2  1 
ATOM   999  N  N    . ALA   A 1 365 ? 30.303  -9.361  24.304  1.00 26.50  ? 376 ALA   A N    1 
ATOM   1000 C  CA   . ALA   A 1 365 ? 30.400  -9.768  22.900  1.00 27.12  ? 376 ALA   A CA   1 
ATOM   1001 C  C    . ALA   A 1 365 ? 31.338  -8.855  22.123  1.00 27.97  ? 376 ALA   A C    1 
ATOM   1002 O  O    . ALA   A 1 365 ? 32.155  -9.325  21.318  1.00 27.40  ? 376 ALA   A O    1 
ATOM   1003 C  CB   . ALA   A 1 365 ? 29.018  -9.767  22.235  1.00 25.79  ? 376 ALA   A CB   1 
ATOM   1004 N  N    . LEU   A 1 366 ? 31.243  -7.548  22.359  1.00 29.33  ? 377 LEU   A N    1 
ATOM   1005 C  CA   . LEU   A 1 366 ? 32.073  -6.594  21.625  1.00 27.21  ? 377 LEU   A CA   1 
ATOM   1006 C  C    . LEU   A 1 366 ? 33.543  -6.709  22.014  1.00 28.31  ? 377 LEU   A C    1 
ATOM   1007 O  O    . LEU   A 1 366 ? 34.425  -6.592  21.158  1.00 28.42  ? 377 LEU   A O    1 
ATOM   1008 C  CB   . LEU   A 1 366 ? 31.573  -5.171  21.864  1.00 24.14  ? 377 LEU   A CB   1 
ATOM   1009 C  CG   . LEU   A 1 366 ? 30.192  -4.827  21.292  1.00 22.88  ? 377 LEU   A CG   1 
ATOM   1010 C  CD1  . LEU   A 1 366 ? 29.881  -3.392  21.561  1.00 22.41  ? 377 LEU   A CD1  1 
ATOM   1011 C  CD2  . LEU   A 1 366 ? 30.119  -5.096  19.785  1.00 22.86  ? 377 LEU   A CD2  1 
ATOM   1012 N  N    . GLU   A 1 367 ? 33.836  -6.892  23.303  1.00 26.56  ? 378 GLU   A N    1 
ATOM   1013 C  CA   . GLU   A 1 367 ? 35.227  -7.087  23.694  1.00 27.07  ? 378 GLU   A CA   1 
ATOM   1014 C  C    . GLU   A 1 367 ? 35.826  -8.277  22.966  1.00 30.82  ? 378 GLU   A C    1 
ATOM   1015 O  O    . GLU   A 1 367 ? 36.949  -8.203  22.450  1.00 31.47  ? 378 GLU   A O    1 
ATOM   1016 C  CB   . GLU   A 1 367 ? 35.338  -7.294  25.197  1.00 26.89  ? 378 GLU   A CB   1 
ATOM   1017 C  CG   . GLU   A 1 367 ? 36.771  -7.525  25.679  1.00 34.19  ? 378 GLU   A CG   1 
ATOM   1018 C  CD   . GLU   A 1 367 ? 36.815  -8.055  27.107  1.00 57.31  ? 378 GLU   A CD   1 
ATOM   1019 O  OE1  . GLU   A 1 367 ? 35.900  -8.822  27.485  1.00 60.76  ? 378 GLU   A OE1  1 
ATOM   1020 O  OE2  . GLU   A 1 367 ? 37.753  -7.705  27.855  1.00 57.36  ? 378 GLU   A OE2  1 
ATOM   1021 N  N    . PHE   A 1 368 ? 35.075  -9.379  22.905  1.00 29.20  ? 379 PHE   A N    1 
ATOM   1022 C  CA   . PHE   A 1 368 ? 35.539  -10.570 22.203  1.00 33.11  ? 379 PHE   A CA   1 
ATOM   1023 C  C    . PHE   A 1 368 ? 35.746  -10.287 20.718  1.00 30.28  ? 379 PHE   A C    1 
ATOM   1024 O  O    . PHE   A 1 368 ? 36.802  -10.593 20.154  1.00 34.69  ? 379 PHE   A O    1 
ATOM   1025 C  CB   . PHE   A 1 368 ? 34.530  -11.703 22.408  1.00 29.40  ? 379 PHE   A CB   1 
ATOM   1026 C  CG   . PHE   A 1 368 ? 34.740  -12.866 21.493  1.00 34.56  ? 379 PHE   A CG   1 
ATOM   1027 C  CD1  . PHE   A 1 368 ? 35.769  -13.761 21.722  1.00 35.37  ? 379 PHE   A CD1  1 
ATOM   1028 C  CD2  . PHE   A 1 368 ? 33.923  -13.058 20.395  1.00 38.63  ? 379 PHE   A CD2  1 
ATOM   1029 C  CE1  . PHE   A 1 368 ? 35.983  -14.841 20.874  1.00 39.89  ? 379 PHE   A CE1  1 
ATOM   1030 C  CE2  . PHE   A 1 368 ? 34.140  -14.139 19.538  1.00 35.73  ? 379 PHE   A CE2  1 
ATOM   1031 C  CZ   . PHE   A 1 368 ? 35.166  -15.027 19.784  1.00 40.43  ? 379 PHE   A CZ   1 
ATOM   1032 N  N    . LEU   A 1 369 ? 34.750  -9.687  20.070  1.00 25.44  ? 380 LEU   A N    1 
ATOM   1033 C  CA   . LEU   A 1 369 ? 34.850  -9.428  18.634  1.00 29.58  ? 380 LEU   A CA   1 
ATOM   1034 C  C    . LEU   A 1 369 ? 36.000  -8.480  18.316  1.00 31.41  ? 380 LEU   A C    1 
ATOM   1035 O  O    . LEU   A 1 369 ? 36.789  -8.726  17.396  1.00 28.71  ? 380 LEU   A O    1 
ATOM   1036 C  CB   . LEU   A 1 369 ? 33.529  -8.849  18.129  1.00 29.40  ? 380 LEU   A CB   1 
ATOM   1037 C  CG   . LEU   A 1 369 ? 32.321  -9.778  18.130  1.00 28.93  ? 380 LEU   A CG   1 
ATOM   1038 C  CD1  . LEU   A 1 369 ? 31.069  -8.995  17.767  1.00 24.10  ? 380 LEU   A CD1  1 
ATOM   1039 C  CD2  . LEU   A 1 369 ? 32.566  -10.902 17.129  1.00 28.64  ? 380 LEU   A CD2  1 
ATOM   1040 N  N    . HIS   A 1 370 ? 36.110  -7.382  19.069  1.00 28.39  ? 381 HIS   A N    1 
ATOM   1041 C  CA   . HIS   A 1 370 ? 37.145  -6.398  18.770  1.00 33.39  ? 381 HIS   A CA   1 
ATOM   1042 C  C    . HIS   A 1 370 ? 38.533  -6.980  19.000  1.00 36.86  ? 381 HIS   A C    1 
ATOM   1043 O  O    . HIS   A 1 370 ? 39.454  -6.741  18.208  1.00 31.91  ? 381 HIS   A O    1 
ATOM   1044 C  CB   . HIS   A 1 370 ? 36.923  -5.139  19.606  1.00 28.07  ? 381 HIS   A CB   1 
ATOM   1045 C  CG   . HIS   A 1 370 ? 35.652  -4.419  19.282  1.00 28.61  ? 381 HIS   A CG   1 
ATOM   1046 N  ND1  . HIS   A 1 370 ? 35.207  -3.332  20.006  1.00 23.81  ? 381 HIS   A ND1  1 
ATOM   1047 C  CD2  . HIS   A 1 370 ? 34.725  -4.632  18.316  1.00 27.53  ? 381 HIS   A CD2  1 
ATOM   1048 C  CE1  . HIS   A 1 370 ? 34.064  -2.904  19.497  1.00 29.21  ? 381 HIS   A CE1  1 
ATOM   1049 N  NE2  . HIS   A 1 370 ? 33.747  -3.679  18.473  1.00 24.37  ? 381 HIS   A NE2  1 
ATOM   1050 N  N    . SER   A 1 371 ? 38.696  -7.772  20.060  1.00 33.64  ? 382 SER   A N    1 
ATOM   1051 C  CA   . SER   A 1 371 ? 39.958  -8.464  20.272  1.00 33.12  ? 382 SER   A CA   1 
ATOM   1052 C  C    . SER   A 1 371 ? 40.299  -9.395  19.111  1.00 36.20  ? 382 SER   A C    1 
ATOM   1053 O  O    . SER   A 1 371 ? 41.470  -9.755  18.939  1.00 42.26  ? 382 SER   A O    1 
ATOM   1054 C  CB   . SER   A 1 371 ? 39.916  -9.234  21.594  1.00 42.96  ? 382 SER   A CB   1 
ATOM   1055 O  OG   . SER   A 1 371 ? 39.094  -10.380 21.491  1.00 48.49  ? 382 SER   A OG   1 
ATOM   1056 N  N    . ASN   A 1 372 ? 39.303  -9.800  18.319  1.00 35.42  ? 383 ASN   A N    1 
ATOM   1057 C  CA   . ASN   A 1 372 ? 39.517  -10.607 17.122  1.00 39.54  ? 383 ASN   A CA   1 
ATOM   1058 C  C    . ASN   A 1 372 ? 39.449  -9.787  15.830  1.00 38.31  ? 383 ASN   A C    1 
ATOM   1059 O  O    . ASN   A 1 372 ? 39.315  -10.365 14.747  1.00 35.54  ? 383 ASN   A O    1 
ATOM   1060 C  CB   . ASN   A 1 372 ? 38.510  -11.758 17.070  1.00 42.46  ? 383 ASN   A CB   1 
ATOM   1061 C  CG   . ASN   A 1 372 ? 38.876  -12.897 18.008  1.00 39.21  ? 383 ASN   A CG   1 
ATOM   1062 O  OD1  . ASN   A 1 372 ? 40.015  -13.345 18.030  1.00 49.72  ? 383 ASN   A OD1  1 
ATOM   1063 N  ND2  . ASN   A 1 372 ? 37.907  -13.363 18.791  1.00 52.30  ? 383 ASN   A ND2  1 
ATOM   1064 N  N    . GLN   A 1 373 ? 39.523  -8.459  15.927  1.00 36.05  ? 384 GLN   A N    1 
ATOM   1065 C  CA   . GLN   A 1 373 ? 39.549  -7.558  14.768  1.00 32.49  ? 384 GLN   A CA   1 
ATOM   1066 C  C    . GLN   A 1 373 ? 38.271  -7.631  13.934  1.00 33.39  ? 384 GLN   A C    1 
ATOM   1067 O  O    . GLN   A 1 373 ? 38.310  -7.456  12.713  1.00 37.56  ? 384 GLN   A O    1 
ATOM   1068 C  CB   . GLN   A 1 373 ? 40.754  -7.826  13.860  1.00 38.36  ? 384 GLN   A CB   1 
ATOM   1069 C  CG   . GLN   A 1 373 ? 42.083  -7.396  14.423  1.00 42.07  ? 384 GLN   A CG   1 
ATOM   1070 C  CD   . GLN   A 1 373 ? 42.661  -8.420  15.376  1.00 49.74  ? 384 GLN   A CD   1 
ATOM   1071 O  OE1  . GLN   A 1 373 ? 42.350  -8.428  16.565  1.00 59.24  ? 384 GLN   A OE1  1 
ATOM   1072 N  NE2  . GLN   A 1 373 ? 43.521  -9.289  14.854  1.00 73.16  ? 384 GLN   A NE2  1 
ATOM   1073 N  N    . VAL   A 1 374 ? 37.131  -7.909  14.564  1.00 30.41  ? 385 VAL   A N    1 
ATOM   1074 C  CA   . VAL   A 1 374 ? 35.834  -7.870  13.897  1.00 28.54  ? 385 VAL   A CA   1 
ATOM   1075 C  C    . VAL   A 1 374 ? 35.058  -6.665  14.416  1.00 29.28  ? 385 VAL   A C    1 
ATOM   1076 O  O    . VAL   A 1 374 ? 34.886  -6.512  15.631  1.00 34.76  ? 385 VAL   A O    1 
ATOM   1077 C  CB   . VAL   A 1 374 ? 35.035  -9.166  14.124  1.00 32.91  ? 385 VAL   A CB   1 
ATOM   1078 C  CG1  . VAL   A 1 374 ? 33.629  -9.024  13.530  1.00 34.84  ? 385 VAL   A CG1  1 
ATOM   1079 C  CG2  . VAL   A 1 374 ? 35.778  -10.371 13.550  1.00 36.20  ? 385 VAL   A CG2  1 
ATOM   1080 N  N    . ILE   A 1 375 ? 34.576  -5.819  13.502  1.00 31.17  ? 386 ILE   A N    1 
ATOM   1081 C  CA   . ILE   A 1 375 ? 33.660  -4.726  13.833  1.00 26.51  ? 386 ILE   A CA   1 
ATOM   1082 C  C    . ILE   A 1 375 ? 32.270  -5.088  13.319  1.00 27.75  ? 386 ILE   A C    1 
ATOM   1083 O  O    . ILE   A 1 375 ? 32.111  -5.407  12.137  1.00 27.48  ? 386 ILE   A O    1 
ATOM   1084 C  CB   . ILE   A 1 375 ? 34.124  -3.384  13.236  1.00 25.89  ? 386 ILE   A CB   1 
ATOM   1085 C  CG1  . ILE   A 1 375 ? 35.576  -3.107  13.610  1.00 29.05  ? 386 ILE   A CG1  1 
ATOM   1086 C  CG2  . ILE   A 1 375 ? 33.235  -2.244  13.756  1.00 26.40  ? 386 ILE   A CG2  1 
ATOM   1087 C  CD1  . ILE   A 1 375 ? 36.158  -1.899  12.924  1.00 34.00  ? 386 ILE   A CD1  1 
ATOM   1088 N  N    . HIS   A 1 376 ? 31.261  -5.050  14.202  1.00 25.45  ? 387 HIS   A N    1 
ATOM   1089 C  CA   . HIS   A 1 376 ? 29.926  -5.475  13.784  1.00 21.61  ? 387 HIS   A CA   1 
ATOM   1090 C  C    . HIS   A 1 376 ? 29.282  -4.452  12.846  1.00 27.33  ? 387 HIS   A C    1 
ATOM   1091 O  O    . HIS   A 1 376 ? 28.707  -4.822  11.813  1.00 24.89  ? 387 HIS   A O    1 
ATOM   1092 C  CB   . HIS   A 1 376 ? 29.049  -5.746  15.020  1.00 20.74  ? 387 HIS   A CB   1 
ATOM   1093 C  CG   . HIS   A 1 376 ? 27.709  -6.343  14.705  1.00 24.50  ? 387 HIS   A CG   1 
ATOM   1094 N  ND1  . HIS   A 1 376 ? 26.666  -5.600  14.190  1.00 20.85  ? 387 HIS   A ND1  1 
ATOM   1095 C  CD2  . HIS   A 1 376 ? 27.238  -7.609  14.846  1.00 24.60  ? 387 HIS   A CD2  1 
ATOM   1096 C  CE1  . HIS   A 1 376 ? 25.612  -6.383  14.023  1.00 23.01  ? 387 HIS   A CE1  1 
ATOM   1097 N  NE2  . HIS   A 1 376 ? 25.932  -7.606  14.416  1.00 24.99  ? 387 HIS   A NE2  1 
ATOM   1098 N  N    . ARG   A 1 377 ? 29.315  -3.165  13.223  1.00 22.49  ? 388 ARG   A N    1 
ATOM   1099 C  CA   . ARG   A 1 377 ? 28.844  -2.020  12.434  1.00 20.47  ? 388 ARG   A CA   1 
ATOM   1100 C  C    . ARG   A 1 377 ? 27.326  -1.910  12.316  1.00 22.73  ? 388 ARG   A C    1 
ATOM   1101 O  O    . ARG   A 1 377 ? 26.833  -0.940  11.725  1.00 23.31  ? 388 ARG   A O    1 
ATOM   1102 C  CB   . ARG   A 1 377 ? 29.471  -1.960  11.021  1.00 21.08  ? 388 ARG   A CB   1 
ATOM   1103 C  CG   . ARG   A 1 377 ? 30.981  -1.847  11.055  1.00 24.47  ? 388 ARG   A CG   1 
ATOM   1104 C  CD   . ARG   A 1 377 ? 31.616  -1.501  9.704   1.00 25.70  ? 388 ARG   A CD   1 
ATOM   1105 N  NE   . ARG   A 1 377 ? 31.344  -2.448  8.629   1.00 28.56  ? 388 ARG   A NE   1 
ATOM   1106 C  CZ   . ARG   A 1 377 ? 31.893  -2.359  7.426   1.00 40.77  ? 388 ARG   A CZ   1 
ATOM   1107 N  NH1  . ARG   A 1 377 ? 32.715  -1.372  7.115   1.00 32.56  ? 388 ARG   A NH1  1 
ATOM   1108 N  NH2  . ARG   A 1 377 ? 31.626  -3.293  6.520   1.00 33.22  ? 388 ARG   A NH2  1 
ATOM   1109 N  N    . ASN   A 1 378 ? 26.565  -2.879  12.825  1.00 22.66  ? 389 ASN   A N    1 
ATOM   1110 C  CA   . ASN   A 1 378 ? 25.111  -2.770  12.741  1.00 22.61  ? 389 ASN   A CA   1 
ATOM   1111 C  C    . ASN   A 1 378 ? 24.462  -3.177  14.077  1.00 20.84  ? 389 ASN   A C    1 
ATOM   1112 O  O    . ASN   A 1 378 ? 23.428  -3.853  14.105  1.00 24.06  ? 389 ASN   A O    1 
ATOM   1113 C  CB   . ASN   A 1 378 ? 24.575  -3.596  11.562  1.00 21.98  ? 389 ASN   A CB   1 
ATOM   1114 C  CG   . ASN   A 1 378 ? 23.144  -3.227  11.166  1.00 27.21  ? 389 ASN   A CG   1 
ATOM   1115 O  OD1  . ASN   A 1 378 ? 22.666  -2.109  11.414  1.00 25.66  ? 389 ASN   A OD1  1 
ATOM   1116 N  ND2  . ASN   A 1 378 ? 22.455  -4.175  10.545  1.00 23.84  ? 389 ASN   A ND2  1 
ATOM   1117 N  N    . ILE   A 1 379 ? 25.027  -2.698  15.190  1.00 22.17  ? 390 ILE   A N    1 
ATOM   1118 C  CA   . ILE   A 1 379 ? 24.448  -2.891  16.524  1.00 19.12  ? 390 ILE   A CA   1 
ATOM   1119 C  C    . ILE   A 1 379 ? 23.169  -2.071  16.661  1.00 23.19  ? 390 ILE   A C    1 
ATOM   1120 O  O    . ILE   A 1 379 ? 23.151  -0.871  16.360  1.00 24.46  ? 390 ILE   A O    1 
ATOM   1121 C  CB   . ILE   A 1 379 ? 25.451  -2.498  17.625  1.00 19.15  ? 390 ILE   A CB   1 
ATOM   1122 C  CG1  . ILE   A 1 379 ? 26.759  -3.307  17.527  1.00 24.98  ? 390 ILE   A CG1  1 
ATOM   1123 C  CG2  . ILE   A 1 379 ? 24.818  -2.645  19.032  1.00 23.56  ? 390 ILE   A CG2  1 
ATOM   1124 C  CD1  . ILE   A 1 379 ? 26.598  -4.745  17.792  1.00 28.91  ? 390 ILE   A CD1  1 
ATOM   1125 N  N    . LYS   A 1 380 ? 22.074  -2.736  17.036  1.00 20.82  ? 391 LYS   A N    1 
ATOM   1126 C  CA   . LYS   A 1 380 ? 20.797  -2.097  17.352  1.00 19.11  ? 391 LYS   A CA   1 
ATOM   1127 C  C    . LYS   A 1 380 ? 19.951  -3.130  18.090  1.00 22.17  ? 391 LYS   A C    1 
ATOM   1128 O  O    . LYS   A 1 380 ? 20.276  -4.317  18.111  1.00 19.47  ? 391 LYS   A O    1 
ATOM   1129 C  CB   . LYS   A 1 380 ? 20.069  -1.578  16.106  1.00 18.62  ? 391 LYS   A CB   1 
ATOM   1130 C  CG   . LYS   A 1 380 ? 19.932  -2.636  14.974  1.00 20.61  ? 391 LYS   A CG   1 
ATOM   1131 C  CD   . LYS   A 1 380 ? 19.503  -2.007  13.631  1.00 20.39  ? 391 LYS   A CD   1 
ATOM   1132 C  CE   . LYS   A 1 380 ? 19.348  -3.086  12.560  1.00 24.15  ? 391 LYS   A CE   1 
ATOM   1133 N  NZ   . LYS   A 1 380 ? 18.752  -2.584  11.301  1.00 25.06  ? 391 LYS   A NZ   1 
ATOM   1134 N  N    . SER   A 1 381 ? 18.873  -2.670  18.720  1.00 19.82  ? 392 SER   A N    1 
ATOM   1135 C  CA   . SER   A 1 381 ? 18.098  -3.613  19.521  1.00 16.30  ? 392 SER   A CA   1 
ATOM   1136 C  C    . SER   A 1 381 ? 17.531  -4.741  18.657  1.00 21.20  ? 392 SER   A C    1 
ATOM   1137 O  O    . SER   A 1 381 ? 17.317  -5.855  19.152  1.00 21.35  ? 392 SER   A O    1 
ATOM   1138 C  CB   . SER   A 1 381 ? 16.969  -2.891  20.257  1.00 18.05  ? 392 SER   A CB   1 
ATOM   1139 O  OG   . SER   A 1 381 ? 15.987  -2.432  19.346  1.00 20.43  ? 392 SER   A OG   1 
ATOM   1140 N  N    . ASP   A 1 382 ? 17.303  -4.483  17.361  1.00 19.55  ? 393 ASP   A N    1 
ATOM   1141 C  CA   . ASP   A 1 382 ? 16.760  -5.490  16.451  1.00 23.42  ? 393 ASP   A CA   1 
ATOM   1142 C  C    . ASP   A 1 382 ? 17.682  -6.694  16.290  1.00 22.69  ? 393 ASP   A C    1 
ATOM   1143 O  O    . ASP   A 1 382 ? 17.215  -7.785  15.920  1.00 20.81  ? 393 ASP   A O    1 
ATOM   1144 C  CB   . ASP   A 1 382 ? 16.504  -4.856  15.078  1.00 22.37  ? 393 ASP   A CB   1 
ATOM   1145 C  CG   . ASP   A 1 382 ? 15.770  -3.510  15.175  1.00 23.54  ? 393 ASP   A CG   1 
ATOM   1146 O  OD1  . ASP   A 1 382 ? 16.310  -2.551  15.786  1.00 22.02  ? 393 ASP   A OD1  1 
ATOM   1147 O  OD2  . ASP   A 1 382 ? 14.658  -3.409  14.614  1.00 23.56  ? 393 ASP   A OD2  1 
ATOM   1148 N  N    . ASN   A 1 383 ? 18.974  -6.513  16.546  1.00 18.65  ? 394 ASN   A N    1 
ATOM   1149 C  CA   . ASN   A 1 383 ? 19.987  -7.544  16.370  1.00 18.46  ? 394 ASN   A CA   1 
ATOM   1150 C  C    . ASN   A 1 383 ? 20.487  -8.082  17.697  1.00 20.08  ? 394 ASN   A C    1 
ATOM   1151 O  O    . ASN   A 1 383 ? 21.552  -8.708  17.741  1.00 20.85  ? 394 ASN   A O    1 
ATOM   1152 C  CB   . ASN   A 1 383 ? 21.153  -7.001  15.522  1.00 21.01  ? 394 ASN   A CB   1 
ATOM   1153 C  CG   . ASN   A 1 383 ? 20.765  -6.818  14.075  1.00 26.10  ? 394 ASN   A CG   1 
ATOM   1154 O  OD1  . ASN   A 1 383 ? 19.828  -7.451  13.618  1.00 22.44  ? 394 ASN   A OD1  1 
ATOM   1155 N  ND2  . ASN   A 1 383 ? 21.482  -5.956  13.339  1.00 23.93  ? 394 ASN   A ND2  1 
ATOM   1156 N  N    . ILE   A 1 384 ? 19.772  -7.795  18.788  1.00 21.62  ? 395 ILE   A N    1 
ATOM   1157 C  CA   . ILE   A 1 384 ? 19.997  -8.406  20.095  1.00 21.14  ? 395 ILE   A CA   1 
ATOM   1158 C  C    . ILE   A 1 384 ? 18.822  -9.347  20.365  1.00 21.16  ? 395 ILE   A C    1 
ATOM   1159 O  O    . ILE   A 1 384 ? 17.672  -8.896  20.430  1.00 22.06  ? 395 ILE   A O    1 
ATOM   1160 C  CB   . ILE   A 1 384 ? 20.110  -7.342  21.201  1.00 23.86  ? 395 ILE   A CB   1 
ATOM   1161 C  CG1  . ILE   A 1 384 ? 21.246  -6.343  20.893  1.00 21.30  ? 395 ILE   A CG1  1 
ATOM   1162 C  CG2  . ILE   A 1 384 ? 20.252  -8.024  22.583  1.00 26.51  ? 395 ILE   A CG2  1 
ATOM   1163 C  CD1  . ILE   A 1 384 ? 22.597  -6.994  20.735  1.00 23.03  ? 395 ILE   A CD1  1 
ATOM   1164 N  N    . LEU   A 1 385 ? 19.100  -10.647 20.502  1.00 19.00  ? 396 LEU   A N    1 
ATOM   1165 C  CA   . LEU   A 1 385 ? 18.074  -11.647 20.781  1.00 22.30  ? 396 LEU   A CA   1 
ATOM   1166 C  C    . LEU   A 1 385 ? 18.237  -12.146 22.212  1.00 25.52  ? 396 LEU   A C    1 
ATOM   1167 O  O    . LEU   A 1 385 ? 19.349  -12.169 22.752  1.00 24.94  ? 396 LEU   A O    1 
ATOM   1168 C  CB   . LEU   A 1 385 ? 18.148  -12.813 19.777  1.00 22.30  ? 396 LEU   A CB   1 
ATOM   1169 C  CG   . LEU   A 1 385 ? 18.119  -12.362 18.309  1.00 26.63  ? 396 LEU   A CG   1 
ATOM   1170 C  CD1  . LEU   A 1 385 ? 18.054  -13.553 17.363  1.00 24.85  ? 396 LEU   A CD1  1 
ATOM   1171 C  CD2  . LEU   A 1 385 ? 16.942  -11.430 18.048  1.00 29.08  ? 396 LEU   A CD2  1 
ATOM   1172 N  N    . LEU   A 1 386 ? 17.114  -12.527 22.833  1.00 22.72  ? 397 LEU   A N    1 
ATOM   1173 C  CA   . LEU   A 1 386 ? 17.074  -12.907 24.236  1.00 23.64  ? 397 LEU   A CA   1 
ATOM   1174 C  C    . LEU   A 1 386 ? 16.657  -14.363 24.397  1.00 27.52  ? 397 LEU   A C    1 
ATOM   1175 O  O    . LEU   A 1 386 ? 15.780  -14.858 23.678  1.00 26.22  ? 397 LEU   A O    1 
ATOM   1176 C  CB   . LEU   A 1 386 ? 16.101  -11.997 25.012  1.00 22.52  ? 397 LEU   A CB   1 
ATOM   1177 C  CG   . LEU   A 1 386 ? 16.359  -10.509 24.759  1.00 25.87  ? 397 LEU   A CG   1 
ATOM   1178 C  CD1  . LEU   A 1 386 ? 15.184  -9.670  25.246  1.00 21.62  ? 397 LEU   A CD1  1 
ATOM   1179 C  CD2  . LEU   A 1 386 ? 17.648  -10.082 25.446  1.00 24.43  ? 397 LEU   A CD2  1 
ATOM   1180 N  N    . GLY   A 1 387 ? 17.287  -15.051 25.339  1.00 24.92  ? 398 GLY   A N    1 
ATOM   1181 C  CA   . GLY   A 1 387 ? 16.850  -16.386 25.688  1.00 29.44  ? 398 GLY   A CA   1 
ATOM   1182 C  C    . GLY   A 1 387 ? 15.756  -16.366 26.732  1.00 34.44  ? 398 GLY   A C    1 
ATOM   1183 O  O    . GLY   A 1 387 ? 15.531  -15.353 27.387  1.00 29.71  ? 398 GLY   A O    1 
ATOM   1184 N  N    . MET   A 1 388 ? 15.046  -17.491 26.859  1.00 34.96  ? 399 MET   A N    1 
ATOM   1185 C  CA   . MET   A 1 388 ? 13.987  -17.571 27.864  1.00 35.30  ? 399 MET   A CA   1 
ATOM   1186 C  C    . MET   A 1 388 ? 14.521  -17.493 29.284  1.00 35.02  ? 399 MET   A C    1 
ATOM   1187 O  O    . MET   A 1 388 ? 13.734  -17.281 30.212  1.00 37.89  ? 399 MET   A O    1 
ATOM   1188 C  CB   . MET   A 1 388 ? 13.171  -18.858 27.703  1.00 40.29  ? 399 MET   A CB   1 
ATOM   1189 C  CG   . MET   A 1 388 ? 12.216  -18.863 26.521  1.00 42.71  ? 399 MET   A CG   1 
ATOM   1190 S  SD   . MET   A 1 388 ? 11.233  -17.345 26.391  1.00 44.56  ? 399 MET   A SD   1 
ATOM   1191 C  CE   . MET   A 1 388 ? 10.235  -17.424 27.873  1.00 54.73  ? 399 MET   A CE   1 
ATOM   1192 N  N    . ASP   A 1 389 ? 15.826  -17.659 29.475  1.00 34.80  ? 400 ASP   A N    1 
ATOM   1193 C  CA   . ASP   A 1 389 ? 16.474  -17.464 30.764  1.00 32.71  ? 400 ASP   A CA   1 
ATOM   1194 C  C    . ASP   A 1 389 ? 17.067  -16.062 30.904  1.00 33.50  ? 400 ASP   A C    1 
ATOM   1195 O  O    . ASP   A 1 389 ? 17.802  -15.795 31.857  1.00 34.23  ? 400 ASP   A O    1 
ATOM   1196 C  CB   . ASP   A 1 389 ? 17.552  -18.542 30.975  1.00 38.62  ? 400 ASP   A CB   1 
ATOM   1197 C  CG   . ASP   A 1 389 ? 18.641  -18.528 29.884  1.00 38.47  ? 400 ASP   A CG   1 
ATOM   1198 O  OD1  . ASP   A 1 389 ? 18.496  -17.808 28.874  1.00 32.46  ? 400 ASP   A OD1  1 
ATOM   1199 O  OD2  . ASP   A 1 389 ? 19.657  -19.241 30.042  1.00 44.28  ? 400 ASP   A OD2  1 
ATOM   1200 N  N    . GLY   A 1 390 ? 16.775  -15.164 29.974  1.00 25.80  ? 401 GLY   A N    1 
ATOM   1201 C  CA   . GLY   A 1 390 ? 17.368  -13.846 30.023  1.00 29.46  ? 401 GLY   A CA   1 
ATOM   1202 C  C    . GLY   A 1 390 ? 18.735  -13.718 29.384  1.00 33.56  ? 401 GLY   A C    1 
ATOM   1203 O  O    . GLY   A 1 390 ? 19.359  -12.661 29.517  1.00 24.83  ? 401 GLY   A O    1 
ATOM   1204 N  N    . SER   A 1 391 ? 19.235  -14.752 28.706  1.00 26.49  ? 402 SER   A N    1 
ATOM   1205 C  CA   . SER   A 1 391 ? 20.515  -14.603 28.027  1.00 25.98  ? 402 SER   A CA   1 
ATOM   1206 C  C    . SER   A 1 391 ? 20.394  -13.585 26.903  1.00 24.12  ? 402 SER   A C    1 
ATOM   1207 O  O    . SER   A 1 391 ? 19.315  -13.366 26.346  1.00 28.03  ? 402 SER   A O    1 
ATOM   1208 C  CB   . SER   A 1 391 ? 20.994  -15.944 27.475  1.00 34.21  ? 402 SER   A CB   1 
ATOM   1209 O  OG   . SER   A 1 391 ? 20.013  -16.490 26.621  1.00 41.26  ? 402 SER   A OG   1 
ATOM   1210 N  N    . VAL   A 1 392 ? 21.512  -12.941 26.584  1.00 23.62  ? 403 VAL   A N    1 
ATOM   1211 C  CA   . VAL   A 1 392 ? 21.535  -11.811 25.660  1.00 25.19  ? 403 VAL   A CA   1 
ATOM   1212 C  C    . VAL   A 1 392 ? 22.601  -12.101 24.609  1.00 25.09  ? 403 VAL   A C    1 
ATOM   1213 O  O    . VAL   A 1 392 ? 23.773  -12.291 24.961  1.00 26.92  ? 403 VAL   A O    1 
ATOM   1214 C  CB   . VAL   A 1 392 ? 21.847  -10.497 26.392  1.00 22.46  ? 403 VAL   A CB   1 
ATOM   1215 C  CG1  . VAL   A 1 392 ? 21.922  -9.321  25.397  1.00 26.14  ? 403 VAL   A CG1  1 
ATOM   1216 C  CG2  . VAL   A 1 392 ? 20.803  -10.197 27.499  1.00 20.78  ? 403 VAL   A CG2  1 
ATOM   1217 N  N    . LYS   A 1 393 ? 22.211  -12.120 23.324  1.00 24.24  ? 404 LYS   A N    1 
ATOM   1218 C  CA   . LYS   A 1 393 ? 23.147  -12.501 22.268  1.00 21.09  ? 404 LYS   A CA   1 
ATOM   1219 C  C    . LYS   A 1 393 ? 22.996  -11.622 21.035  1.00 24.03  ? 404 LYS   A C    1 
ATOM   1220 O  O    . LYS   A 1 393 ? 21.889  -11.243 20.649  1.00 24.49  ? 404 LYS   A O    1 
ATOM   1221 C  CB   . LYS   A 1 393 ? 22.973  -13.957 21.836  1.00 24.86  ? 404 LYS   A CB   1 
ATOM   1222 C  CG   . LYS   A 1 393 ? 23.122  -14.964 22.945  1.00 28.23  ? 404 LYS   A CG   1 
ATOM   1223 C  CD   . LYS   A 1 393 ? 23.133  -16.359 22.387  1.00 33.20  ? 404 LYS   A CD   1 
ATOM   1224 C  CE   . LYS   A 1 393 ? 23.299  -17.375 23.508  1.00 39.18  ? 404 LYS   A CE   1 
ATOM   1225 N  NZ   . LYS   A 1 393 ? 24.280  -18.383 23.022  1.00 45.22  ? 404 LYS   A NZ   1 
ATOM   1226 N  N    . LEU   A 1 394 ? 24.130  -11.314 20.426  1.00 23.55  ? 405 LEU   A N    1 
ATOM   1227 C  CA   . LEU   A 1 394 ? 24.197  -10.487 19.230  1.00 20.83  ? 405 LEU   A CA   1 
ATOM   1228 C  C    . LEU   A 1 394 ? 24.111  -11.325 17.955  1.00 22.36  ? 405 LEU   A C    1 
ATOM   1229 O  O    . LEU   A 1 394 ? 24.707  -12.401 17.872  1.00 23.92  ? 405 LEU   A O    1 
ATOM   1230 C  CB   . LEU   A 1 394 ? 25.504  -9.701  19.273  1.00 26.82  ? 405 LEU   A CB   1 
ATOM   1231 C  CG   . LEU   A 1 394 ? 25.898  -8.784  18.132  1.00 31.99  ? 405 LEU   A CG   1 
ATOM   1232 C  CD1  . LEU   A 1 394 ? 24.824  -7.715  17.959  1.00 27.37  ? 405 LEU   A CD1  1 
ATOM   1233 C  CD2  . LEU   A 1 394 ? 27.258  -8.193  18.485  1.00 29.38  ? 405 LEU   A CD2  1 
ATOM   1234 N  N    . THR   A 1 395 ? 23.405  -10.807 16.945  1.00 23.31  ? 406 THR   A N    1 
ATOM   1235 C  CA   . THR   A 1 395 ? 23.199  -11.531 15.690  1.00 25.16  ? 406 THR   A CA   1 
ATOM   1236 C  C    . THR   A 1 395 ? 23.407  -10.582 14.500  1.00 25.85  ? 406 THR   A C    1 
ATOM   1237 O  O    . THR   A 1 395 ? 23.784  -9.417  14.670  1.00 26.11  ? 406 THR   A O    1 
ATOM   1238 C  CB   . THR   A 1 395 ? 21.808  -12.200 15.657  1.00 22.16  ? 406 THR   A CB   1 
ATOM   1239 O  OG1  . THR   A 1 395 ? 21.764  -13.117 14.558  1.00 30.16  ? 406 THR   A OG1  1 
ATOM   1240 C  CG2  . THR   A 1 395 ? 20.699  -11.188 15.480  1.00 24.07  ? 406 THR   A CG2  1 
ATOM   1241 N  N    . ASP   A 1 396 ? 23.196  -11.118 13.289  1.00 25.70  ? 407 ASP   A N    1 
ATOM   1242 C  CA   . ASP   A 1 396 ? 23.218  -10.404 11.995  1.00 25.70  ? 407 ASP   A CA   1 
ATOM   1243 C  C    . ASP   A 1 396 ? 24.494  -9.708  11.507  1.00 28.34  ? 407 ASP   A C    1 
ATOM   1244 O  O    . ASP   A 1 396 ? 24.523  -8.513  11.194  1.00 27.71  ? 407 ASP   A O    1 
ATOM   1245 C  CB   . ASP   A 1 396 ? 22.049  -9.421  11.888  1.00 23.51  ? 407 ASP   A CB   1 
ATOM   1246 C  CG   . ASP   A 1 396 ? 20.802  -10.068 11.315  1.00 35.36  ? 407 ASP   A CG   1 
ATOM   1247 O  OD1  . ASP   A 1 396 ? 20.701  -11.324 11.343  1.00 34.49  ? 407 ASP   A OD1  1 
ATOM   1248 O  OD2  . ASP   A 1 396 ? 19.934  -9.323  10.812  1.00 33.45  ? 407 ASP   A OD2  1 
ATOM   1249 N  N    . PHE   A 1 397 ? 25.543  -10.516 11.407  1.00 23.94  ? 408 PHE   A N    1 
ATOM   1250 C  CA   . PHE   A 1 397 ? 26.896  -10.055 11.147  1.00 28.89  ? 408 PHE   A CA   1 
ATOM   1251 C  C    . PHE   A 1 397 ? 27.168  -9.707  9.681   1.00 25.35  ? 408 PHE   A C    1 
ATOM   1252 O  O    . PHE   A 1 397 ? 28.336  -9.540  9.311   1.00 30.31  ? 408 PHE   A O    1 
ATOM   1253 C  CB   . PHE   A 1 397 ? 27.888  -11.105 11.656  1.00 31.31  ? 408 PHE   A CB   1 
ATOM   1254 C  CG   . PHE   A 1 397 ? 28.032  -11.110 13.162  1.00 25.44  ? 408 PHE   A CG   1 
ATOM   1255 C  CD1  . PHE   A 1 397 ? 26.986  -11.520 13.972  1.00 28.78  ? 408 PHE   A CD1  1 
ATOM   1256 C  CD2  . PHE   A 1 397 ? 29.220  -10.695 13.757  1.00 30.51  ? 408 PHE   A CD2  1 
ATOM   1257 C  CE1  . PHE   A 1 397 ? 27.117  -11.522 15.357  1.00 30.82  ? 408 PHE   A CE1  1 
ATOM   1258 C  CE2  . PHE   A 1 397 ? 29.366  -10.692 15.126  1.00 31.15  ? 408 PHE   A CE2  1 
ATOM   1259 C  CZ   . PHE   A 1 397 ? 28.311  -11.108 15.939  1.00 27.19  ? 408 PHE   A CZ   1 
ATOM   1260 N  N    . GLY   A 1 398 ? 26.136  -9.595  8.839   1.00 25.20  ? 409 GLY   A N    1 
ATOM   1261 C  CA   . GLY   A 1 398 ? 26.437  -9.432  7.421   1.00 24.75  ? 409 GLY   A CA   1 
ATOM   1262 C  C    . GLY   A 1 398 ? 26.987  -8.067  7.048   1.00 28.23  ? 409 GLY   A C    1 
ATOM   1263 O  O    . GLY   A 1 398 ? 27.509  -7.909  5.937   1.00 28.07  ? 409 GLY   A O    1 
ATOM   1264 N  N    . PHE   A 1 399 ? 26.976  -7.112  7.972   1.00 25.39  ? 410 PHE   A N    1 
ATOM   1265 C  CA   . PHE   A 1 399 ? 27.567  -5.802  7.724   1.00 29.59  ? 410 PHE   A CA   1 
ATOM   1266 C  C    . PHE   A 1 399 ? 28.945  -5.680  8.346   1.00 26.98  ? 410 PHE   A C    1 
ATOM   1267 O  O    . PHE   A 1 399 ? 29.574  -4.628  8.226   1.00 29.48  ? 410 PHE   A O    1 
ATOM   1268 C  CB   . PHE   A 1 399 ? 26.664  -4.674  8.259   1.00 25.54  ? 410 PHE   A CB   1 
ATOM   1269 C  CG   . PHE   A 1 399 ? 25.665  -4.160  7.251   1.00 29.25  ? 410 PHE   A CG   1 
ATOM   1270 C  CD1  . PHE   A 1 399 ? 25.256  -4.948  6.187   1.00 29.91  ? 410 PHE   A CD1  1 
ATOM   1271 C  CD2  . PHE   A 1 399 ? 25.135  -2.883  7.372   1.00 36.55  ? 410 PHE   A CD2  1 
ATOM   1272 C  CE1  . PHE   A 1 399 ? 24.334  -4.476  5.261   1.00 37.85  ? 410 PHE   A CE1  1 
ATOM   1273 C  CE2  . PHE   A 1 399 ? 24.221  -2.404  6.449   1.00 38.99  ? 410 PHE   A CE2  1 
ATOM   1274 C  CZ   . PHE   A 1 399 ? 23.815  -3.200  5.393   1.00 33.37  ? 410 PHE   A CZ   1 
ATOM   1275 N  N    . CYS   A 1 400 ? 29.432  -6.737  8.988   1.00 29.32  ? 411 CYS   A N    1 
ATOM   1276 C  CA   . CYS   A 1 400 ? 30.649  -6.646  9.777   1.00 29.04  ? 411 CYS   A CA   1 
ATOM   1277 C  C    . CYS   A 1 400 ? 31.877  -6.447  8.891   1.00 37.85  ? 411 CYS   A C    1 
ATOM   1278 O  O    . CYS   A 1 400 ? 31.879  -6.732  7.689   1.00 33.32  ? 411 CYS   A O    1 
ATOM   1279 C  CB   . CYS   A 1 400 ? 30.818  -7.894  10.658  1.00 30.29  ? 411 CYS   A CB   1 
ATOM   1280 S  SG   . CYS   A 1 400 ? 31.427  -9.399  9.817   1.00 35.80  ? 411 CYS   A SG   1 
ATOM   1281 N  N    . ALA   A 1 401 ? 32.935  -5.931  9.509   1.00 37.66  ? 412 ALA   A N    1 
ATOM   1282 C  CA   . ALA   A 1 401 ? 34.209  -5.716  8.837   1.00 43.64  ? 412 ALA   A CA   1 
ATOM   1283 C  C    . ALA   A 1 401 ? 35.326  -6.390  9.621   1.00 33.42  ? 412 ALA   A C    1 
ATOM   1284 O  O    . ALA   A 1 401 ? 35.329  -6.381  10.853  1.00 34.96  ? 412 ALA   A O    1 
ATOM   1285 C  CB   . ALA   A 1 401 ? 34.515  -4.223  8.689   1.00 39.62  ? 412 ALA   A CB   1 
ATOM   1286 N  N    . GLN   A 1 402 ? 36.279  -6.968  8.910   1.00 36.43  ? 413 GLN   A N    1 
ATOM   1287 C  CA   . GLN   A 1 402 ? 37.466  -7.517  9.541   1.00 41.65  ? 413 GLN   A CA   1 
ATOM   1288 C  C    . GLN   A 1 402 ? 38.625  -6.575  9.254   1.00 48.31  ? 413 GLN   A C    1 
ATOM   1289 O  O    . GLN   A 1 402 ? 38.916  -6.284  8.089   1.00 49.56  ? 413 GLN   A O    1 
ATOM   1290 C  CB   . GLN   A 1 402 ? 37.750  -8.929  9.034   1.00 50.64  ? 413 GLN   A CB   1 
ATOM   1291 C  CG   . GLN   A 1 402 ? 36.549  -9.852  9.188   1.00 56.71  ? 413 GLN   A CG   1 
ATOM   1292 C  CD   . GLN   A 1 402 ? 36.928  -11.322 9.221   1.00 64.66  ? 413 GLN   A CD   1 
ATOM   1293 O  OE1  . GLN   A 1 402 ? 37.619  -11.779 10.136  1.00 58.28  ? 413 GLN   A OE1  1 
ATOM   1294 N  NE2  . GLN   A 1 402 ? 36.476  -12.073 8.221   1.00 61.53  ? 413 GLN   A NE2  1 
ATOM   1295 N  N    . ILE   A 1 403 ? 39.262  -6.076  10.308  1.00 40.12  ? 414 ILE   A N    1 
ATOM   1296 C  CA   . ILE   A 1 403 ? 40.358  -5.138  10.150  1.00 45.23  ? 414 ILE   A CA   1 
ATOM   1297 C  C    . ILE   A 1 403 ? 41.676  -5.874  10.343  1.00 45.76  ? 414 ILE   A C    1 
ATOM   1298 O  O    . ILE   A 1 403 ? 41.743  -6.955  10.934  1.00 46.30  ? 414 ILE   A O    1 
ATOM   1299 C  CB   . ILE   A 1 403 ? 40.248  -3.931  11.110  1.00 52.51  ? 414 ILE   A CB   1 
ATOM   1300 C  CG1  . ILE   A 1 403 ? 40.213  -4.394  12.565  1.00 44.95  ? 414 ILE   A CG1  1 
ATOM   1301 C  CG2  . ILE   A 1 403 ? 39.019  -3.094  10.775  1.00 46.86  ? 414 ILE   A CG2  1 
ATOM   1302 C  CD1  . ILE   A 1 403 ? 40.279  -3.254  13.551  1.00 46.21  ? 414 ILE   A CD1  1 
ATOM   1303 N  N    . THR   A 1 404 ? 42.743  -5.278  9.826   1.00 47.19  ? 415 THR   A N    1 
ATOM   1304 C  CA   . THR   A 1 404 ? 44.074  -5.864  9.848   1.00 57.63  ? 415 THR   A CA   1 
ATOM   1305 C  C    . THR   A 1 404 ? 45.077  -4.767  10.196  1.00 64.66  ? 415 THR   A C    1 
ATOM   1306 O  O    . THR   A 1 404 ? 44.716  -3.585  10.182  1.00 62.01  ? 415 THR   A O    1 
ATOM   1307 C  CB   . THR   A 1 404 ? 44.376  -6.505  8.485   1.00 54.00  ? 415 THR   A CB   1 
ATOM   1308 O  OG1  . THR   A 1 404 ? 45.577  -7.284  8.556   1.00 79.65  ? 415 THR   A OG1  1 
ATOM   1309 C  CG2  . THR   A 1 404 ? 44.526  -5.430  7.425   1.00 51.43  ? 415 THR   A CG2  1 
ATOM   1310 N  N    . PRO   A 1 405 ? 46.320  -5.105  10.560  1.00 82.23  ? 416 PRO   A N    1 
ATOM   1311 C  CA   . PRO   A 1 405 ? 47.325  -4.046  10.778  1.00 83.03  ? 416 PRO   A CA   1 
ATOM   1312 C  C    . PRO   A 1 405 ? 47.482  -3.055  9.629   1.00 81.52  ? 416 PRO   A C    1 
ATOM   1313 O  O    . PRO   A 1 405 ? 47.464  -1.841  9.867   1.00 78.93  ? 416 PRO   A O    1 
ATOM   1314 C  CB   . PRO   A 1 405 ? 48.601  -4.855  11.025  1.00 94.10  ? 416 PRO   A CB   1 
ATOM   1315 C  CG   . PRO   A 1 405 ? 48.109  -6.065  11.748  1.00 99.28  ? 416 PRO   A CG   1 
ATOM   1316 C  CD   . PRO   A 1 405 ? 46.737  -6.378  11.179  1.00 86.20  ? 416 PRO   A CD   1 
ATOM   1317 N  N    . GLU   A 1 406 ? 47.638  -3.528  8.393   1.00 79.70  ? 417 GLU   A N    1 
ATOM   1318 C  CA   . GLU   A 1 406 ? 47.836  -2.627  7.261   1.00 87.34  ? 417 GLU   A CA   1 
ATOM   1319 C  C    . GLU   A 1 406 ? 46.545  -1.974  6.775   1.00 80.82  ? 417 GLU   A C    1 
ATOM   1320 O  O    . GLU   A 1 406 ? 46.590  -1.175  5.832   1.00 72.70  ? 417 GLU   A O    1 
ATOM   1321 C  CB   . GLU   A 1 406 ? 48.509  -3.366  6.097   1.00 91.54  ? 417 GLU   A CB   1 
ATOM   1322 C  CG   . GLU   A 1 406 ? 47.868  -4.696  5.736   1.00 98.30  ? 417 GLU   A CG   1 
ATOM   1323 C  CD   . GLU   A 1 406 ? 48.371  -5.835  6.599   1.00 101.05 ? 417 GLU   A CD   1 
ATOM   1324 O  OE1  . GLU   A 1 406 ? 49.577  -5.839  6.930   1.00 104.32 ? 417 GLU   A OE1  1 
ATOM   1325 O  OE2  . GLU   A 1 406 ? 47.559  -6.716  6.955   1.00 98.08  ? 417 GLU   A OE2  1 
ATOM   1326 N  N    . GLN   A 1 407 ? 45.404  -2.290  7.391   1.00 72.82  ? 418 GLN   A N    1 
ATOM   1327 C  CA   . GLN   A 1 407 ? 44.105  -1.709  7.075   1.00 63.21  ? 418 GLN   A CA   1 
ATOM   1328 C  C    . GLN   A 1 407 ? 43.263  -1.799  8.349   1.00 54.20  ? 418 GLN   A C    1 
ATOM   1329 O  O    . GLN   A 1 407 ? 42.336  -2.600  8.465   1.00 50.54  ? 418 GLN   A O    1 
ATOM   1330 C  CB   . GLN   A 1 407 ? 43.426  -2.412  5.897   1.00 65.61  ? 418 GLN   A CB   1 
ATOM   1331 C  CG   . GLN   A 1 407 ? 43.594  -1.690  4.571   1.00 71.06  ? 418 GLN   A CG   1 
ATOM   1332 C  CD   . GLN   A 1 407 ? 42.882  -0.345  4.556   1.00 82.55  ? 418 GLN   A CD   1 
ATOM   1333 O  OE1  . GLN   A 1 407 ? 43.465  0.675   4.186   1.00 83.10  ? 418 GLN   A OE1  1 
ATOM   1334 N  NE2  . GLN   A 1 407 ? 41.614  -0.340  4.963   1.00 70.09  ? 418 GLN   A NE2  1 
ATOM   1335 N  N    . SER   A 1 408 ? 43.618  -0.971  9.330   1.00 53.52  ? 419 SER   A N    1 
ATOM   1336 C  CA   . SER   A 1 408 ? 42.989  -0.994  10.646  1.00 51.89  ? 419 SER   A CA   1 
ATOM   1337 C  C    . SER   A 1 408 ? 41.766  -0.099  10.744  1.00 45.23  ? 419 SER   A C    1 
ATOM   1338 O  O    . SER   A 1 408 ? 41.117  -0.086  11.795  1.00 48.75  ? 419 SER   A O    1 
ATOM   1339 C  CB   . SER   A 1 408 ? 43.995  -0.583  11.724  1.00 57.10  ? 419 SER   A CB   1 
ATOM   1340 O  OG   . SER   A 1 408 ? 44.427  0.753   11.535  1.00 63.19  ? 419 SER   A OG   1 
ATOM   1341 N  N    . LYS   A 1 409 ? 41.430  0.639   9.686   1.00 44.79  ? 420 LYS   A N    1 
ATOM   1342 C  CA   . LYS   A 1 409 ? 40.245  1.487   9.679   1.00 45.40  ? 420 LYS   A CA   1 
ATOM   1343 C  C    . LYS   A 1 409 ? 39.452  1.302   8.390   1.00 47.91  ? 420 LYS   A C    1 
ATOM   1344 O  O    . LYS   A 1 409 ? 39.971  0.828   7.374   1.00 48.09  ? 420 LYS   A O    1 
ATOM   1345 C  CB   . LYS   A 1 409 ? 40.616  2.970   9.853   1.00 47.63  ? 420 LYS   A CB   1 
ATOM   1346 C  CG   . LYS   A 1 409 ? 41.261  3.295   11.189  1.00 56.18  ? 420 LYS   A CG   1 
ATOM   1347 C  CD   . LYS   A 1 409 ? 41.755  4.726   11.236  1.00 63.63  ? 420 LYS   A CD   1 
ATOM   1348 C  CE   . LYS   A 1 409 ? 42.261  5.095   12.629  1.00 78.71  ? 420 LYS   A CE   1 
ATOM   1349 N  NZ   . LYS   A 1 409 ? 42.507  6.564   12.772  1.00 77.01  ? 420 LYS   A NZ   1 
ATOM   1350 N  N    . ARG   A 1 410 ? 38.157  1.598   8.483   1.00 40.43  ? 421 ARG   A N    1 
ATOM   1351 C  CA   . ARG   A 1 410 ? 37.209  1.616   7.375   1.00 41.54  ? 421 ARG   A CA   1 
ATOM   1352 C  C    . ARG   A 1 410 ? 36.694  3.034   7.143   1.00 43.95  ? 421 ARG   A C    1 
ATOM   1353 O  O    . ARG   A 1 410 ? 36.879  3.931   7.968   1.00 45.19  ? 421 ARG   A O    1 
ATOM   1354 C  CB   . ARG   A 1 410 ? 36.049  0.648   7.630   1.00 45.79  ? 421 ARG   A CB   1 
ATOM   1355 C  CG   . ARG   A 1 410 ? 36.512  -0.791  7.773   1.00 44.14  ? 421 ARG   A CG   1 
ATOM   1356 C  CD   . ARG   A 1 410 ? 37.306  -1.173  6.526   1.00 53.00  ? 421 ARG   A CD   1 
ATOM   1357 N  NE   . ARG   A 1 410 ? 37.626  -2.592  6.447   1.00 52.35  ? 421 ARG   A NE   1 
ATOM   1358 C  CZ   . ARG   A 1 410 ? 36.822  -3.509  5.927   1.00 61.83  ? 421 ARG   A CZ   1 
ATOM   1359 N  NH1  . ARG   A 1 410 ? 35.648  -3.183  5.408   1.00 55.65  ? 421 ARG   A NH1  1 
ATOM   1360 N  NH2  . ARG   A 1 410 ? 37.213  -4.781  5.912   1.00 58.13  ? 421 ARG   A NH2  1 
ATOM   1361 N  N    . SER   A 1 411 ? 36.033  3.238   6.000   1.00 41.75  ? 422 SER   A N    1 
ATOM   1362 C  CA   . SER   A 1 411 ? 35.546  4.574   5.664   1.00 46.62  ? 422 SER   A CA   1 
ATOM   1363 C  C    . SER   A 1 411 ? 34.136  4.626   5.083   1.00 56.68  ? 422 SER   A C    1 
ATOM   1364 O  O    . SER   A 1 411 ? 33.573  5.725   5.014   1.00 49.00  ? 422 SER   A O    1 
ATOM   1365 C  CB   . SER   A 1 411 ? 36.508  5.247   4.670   1.00 53.36  ? 422 SER   A CB   1 
ATOM   1366 O  OG   . SER   A 1 411 ? 36.445  6.660   4.788   1.00 60.66  ? 422 SER   A OG   1 
ATOM   1367 N  N    . GLU   A 1 412 ? 33.556  3.461   4.784   1.00 54.59  ? 423 GLU   A N    1 
ATOM   1368 C  CA   . GLU   A 1 412 ? 32.228  3.365   4.116   1.00 51.37  ? 423 GLU   A CA   1 
ATOM   1369 C  C    . GLU   A 1 412 ? 31.031  3.628   5.043   1.00 46.41  ? 423 GLU   A C    1 
ATOM   1370 O  O    . GLU   A 1 412 ? 31.094  3.228   6.207   1.00 39.67  ? 423 GLU   A O    1 
ATOM   1371 C  CB   . GLU   A 1 412 ? 32.113  1.973   3.510   1.00 45.73  ? 423 GLU   A CB   1 
ATOM   1372 C  CG   . GLU   A 1 412 ? 33.413  1.443   2.938   1.00 81.33  ? 423 GLU   A CG   1 
ATOM   1373 C  CD   . GLU   A 1 412 ? 34.370  0.853   3.959   1.00 92.99  ? 423 GLU   A CD   1 
ATOM   1374 O  OE1  . GLU   A 1 412 ? 34.049  -0.211  4.531   1.00 81.76  ? 423 GLU   A OE1  1 
ATOM   1375 O  OE2  . GLU   A 1 412 ? 35.430  1.463   4.184   1.00 86.29  ? 423 GLU   A OE2  1 
ATOM   1376 N  N    . MET   A 1 413 ? 29.987  4.278   4.517   1.00 34.63  ? 424 MET   A N    1 
ATOM   1377 C  CA   . MET   A 1 413 ? 28.759  4.550   5.275   1.00 33.62  ? 424 MET   A CA   1 
ATOM   1378 C  C    . MET   A 1 413 ? 27.942  3.268   5.375   1.00 35.75  ? 424 MET   A C    1 
ATOM   1379 O  O    . MET   A 1 413 ? 26.953  3.063   4.668   1.00 40.42  ? 424 MET   A O    1 
ATOM   1380 C  CB   . MET   A 1 413 ? 27.921  5.624   4.592   1.00 34.65  ? 424 MET   A CB   1 
ATOM   1381 C  CG   . MET   A 1 413 ? 28.450  7.014   4.579   1.00 42.61  ? 424 MET   A CG   1 
ATOM   1382 S  SD   . MET   A 1 413 ? 27.262  8.073   3.720   1.00 45.21  ? 424 MET   A SD   1 
ATOM   1383 C  CE   . MET   A 1 413 ? 26.023  8.330   4.965   1.00 36.47  ? 424 MET   A CE   1 
ATOM   1384 N  N    . VAL   A 1 414 ? 28.355  2.409   6.298   1.00 33.19  ? 425 VAL   A N    1 
ATOM   1385 C  CA   . VAL   A 1 414 ? 27.716  1.123   6.554   1.00 28.59  ? 425 VAL   A CA   1 
ATOM   1386 C  C    . VAL   A 1 414 ? 26.999  1.194   7.896   1.00 30.08  ? 425 VAL   A C    1 
ATOM   1387 O  O    . VAL   A 1 414 ? 27.582  1.650   8.887   1.00 27.85  ? 425 VAL   A O    1 
ATOM   1388 C  CB   . VAL   A 1 414 ? 28.753  -0.012  6.526   1.00 32.67  ? 425 VAL   A CB   1 
ATOM   1389 C  CG1  . VAL   A 1 414 ? 28.130  -1.326  6.981   1.00 31.50  ? 425 VAL   A CG1  1 
ATOM   1390 C  CG2  . VAL   A 1 414 ? 29.342  -0.125  5.125   1.00 38.10  ? 425 VAL   A CG2  1 
ATOM   1391 N  N    . GLY   A 1 415 ? 25.747  0.725   7.940   1.00 30.46  ? 426 GLY   A N    1 
ATOM   1392 C  CA   . GLY   A 1 415 ? 25.010  0.701   9.189   1.00 25.09  ? 426 GLY   A CA   1 
ATOM   1393 C  C    . GLY   A 1 415 ? 23.546  1.032   8.968   1.00 29.13  ? 426 GLY   A C    1 
ATOM   1394 O  O    . GLY   A 1 415 ? 23.053  1.056   7.843   1.00 30.57  ? 426 GLY   A O    1 
ATOM   1395 N  N    . THR   A 1 416 ? 22.818  1.180   10.070  1.00 22.39  ? 427 THR   A N    1 
ATOM   1396 C  CA   . THR   A 1 416 ? 21.448  1.651   10.046  1.00 25.23  ? 427 THR   A CA   1 
ATOM   1397 C  C    . THR   A 1 416 ? 21.455  3.082   10.547  1.00 27.80  ? 427 THR   A C    1 
ATOM   1398 O  O    . THR   A 1 416 ? 21.961  3.321   11.653  1.00 24.39  ? 427 THR   A O    1 
ATOM   1399 C  CB   . THR   A 1 416 ? 20.545  0.792   10.918  1.00 24.96  ? 427 THR   A CB   1 
ATOM   1400 O  OG1  . THR   A 1 416 ? 20.614  -0.565  10.462  1.00 26.18  ? 427 THR   A OG1  1 
ATOM   1401 C  CG2  . THR   A 1 416 ? 19.103  1.278   10.779  1.00 26.83  ? 427 THR   A CG2  1 
ATOM   1402 N  N    . PRO   A 1 417 ? 20.909  4.042   9.781   1.00 26.67  ? 428 PRO   A N    1 
ATOM   1403 C  CA   . PRO   A 1 417 ? 21.205  5.467   10.051  1.00 22.15  ? 428 PRO   A CA   1 
ATOM   1404 C  C    . PRO   A 1 417 ? 21.108  5.898   11.507  1.00 25.05  ? 428 PRO   A C    1 
ATOM   1405 O  O    . PRO   A 1 417 ? 22.057  6.504   12.029  1.00 25.93  ? 428 PRO   A O    1 
ATOM   1406 C  CB   . PRO   A 1 417 ? 20.177  6.178   9.162   1.00 26.54  ? 428 PRO   A CB   1 
ATOM   1407 C  CG   . PRO   A 1 417 ? 20.151  5.308   7.913   1.00 31.28  ? 428 PRO   A CG   1 
ATOM   1408 C  CD   . PRO   A 1 417 ? 20.177  3.870   8.507   1.00 25.69  ? 428 PRO   A CD   1 
ATOM   1409 N  N    . TYR   A 1 418 ? 20.016  5.573   12.194  1.00 25.25  ? 429 TYR   A N    1 
ATOM   1410 C  CA   . TYR   A 1 418 ? 19.809  6.129   13.529  1.00 27.00  ? 429 TYR   A CA   1 
ATOM   1411 C  C    . TYR   A 1 418 ? 20.872  5.667   14.514  1.00 25.47  ? 429 TYR   A C    1 
ATOM   1412 O  O    . TYR   A 1 418 ? 21.128  6.364   15.500  1.00 23.90  ? 429 TYR   A O    1 
ATOM   1413 C  CB   . TYR   A 1 418 ? 18.404  5.749   14.036  1.00 25.73  ? 429 TYR   A CB   1 
ATOM   1414 C  CG   . TYR   A 1 418 ? 17.356  6.097   13.013  1.00 25.16  ? 429 TYR   A CG   1 
ATOM   1415 C  CD1  . TYR   A 1 418 ? 16.815  7.382   12.951  1.00 24.20  ? 429 TYR   A CD1  1 
ATOM   1416 C  CD2  . TYR   A 1 418 ? 16.956  5.165   12.053  1.00 22.04  ? 429 TYR   A CD2  1 
ATOM   1417 C  CE1  . TYR   A 1 418 ? 15.879  7.720   11.983  1.00 26.94  ? 429 TYR   A CE1  1 
ATOM   1418 C  CE2  . TYR   A 1 418 ? 16.027  5.505   11.066  1.00 26.63  ? 429 TYR   A CE2  1 
ATOM   1419 C  CZ   . TYR   A 1 418 ? 15.486  6.785   11.043  1.00 37.50  ? 429 TYR   A CZ   1 
ATOM   1420 O  OH   . TYR   A 1 418 ? 14.563  7.146   10.072  1.00 32.54  ? 429 TYR   A OH   1 
ATOM   1421 N  N    . TRP   A 1 419 ? 21.512  4.522   14.262  1.00 22.81  ? 430 TRP   A N    1 
ATOM   1422 C  CA   . TRP   A 1 419 ? 22.511  3.974   15.169  1.00 23.73  ? 430 TRP   A CA   1 
ATOM   1423 C  C    . TRP   A 1 419 ? 23.955  4.283   14.764  1.00 21.91  ? 430 TRP   A C    1 
ATOM   1424 O  O    . TRP   A 1 419 ? 24.882  3.885   15.476  1.00 21.62  ? 430 TRP   A O    1 
ATOM   1425 C  CB   . TRP   A 1 419 ? 22.310  2.459   15.298  1.00 21.70  ? 430 TRP   A CB   1 
ATOM   1426 C  CG   . TRP   A 1 419 ? 21.036  2.080   16.051  1.00 21.74  ? 430 TRP   A CG   1 
ATOM   1427 C  CD1  . TRP   A 1 419 ? 20.932  1.813   17.379  1.00 20.94  ? 430 TRP   A CD1  1 
ATOM   1428 C  CD2  . TRP   A 1 419 ? 19.710  1.929   15.508  1.00 20.85  ? 430 TRP   A CD2  1 
ATOM   1429 N  NE1  . TRP   A 1 419 ? 19.625  1.505   17.709  1.00 21.24  ? 430 TRP   A NE1  1 
ATOM   1430 C  CE2  . TRP   A 1 419 ? 18.860  1.563   16.577  1.00 21.06  ? 430 TRP   A CE2  1 
ATOM   1431 C  CE3  . TRP   A 1 419 ? 19.166  2.056   14.230  1.00 21.22  ? 430 TRP   A CE3  1 
ATOM   1432 C  CZ2  . TRP   A 1 419 ? 17.493  1.333   16.408  1.00 22.35  ? 430 TRP   A CZ2  1 
ATOM   1433 C  CZ3  . TRP   A 1 419 ? 17.800  1.825   14.060  1.00 24.62  ? 430 TRP   A CZ3  1 
ATOM   1434 C  CH2  . TRP   A 1 419 ? 16.983  1.467   15.149  1.00 21.10  ? 430 TRP   A CH2  1 
ATOM   1435 N  N    . MET   A 1 420 ? 24.179  4.948   13.634  1.00 21.62  ? 431 MET   A N    1 
ATOM   1436 C  CA   . MET   A 1 420 ? 25.530  5.110   13.113  1.00 27.41  ? 431 MET   A CA   1 
ATOM   1437 C  C    . MET   A 1 420 ? 26.284  6.228   13.835  1.00 24.19  ? 431 MET   A C    1 
ATOM   1438 O  O    . MET   A 1 420 ? 25.747  7.310   14.075  1.00 24.44  ? 431 MET   A O    1 
ATOM   1439 C  CB   . MET   A 1 420 ? 25.452  5.400   11.610  1.00 26.61  ? 431 MET   A CB   1 
ATOM   1440 C  CG   . MET   A 1 420 ? 24.894  4.195   10.847  1.00 30.29  ? 431 MET   A CG   1 
ATOM   1441 S  SD   . MET   A 1 420 ? 24.530  4.428   9.103   1.00 28.22  ? 431 MET   A SD   1 
ATOM   1442 C  CE   . MET   A 1 420 ? 26.045  5.189   8.543   1.00 27.84  ? 431 MET   A CE   1 
ATOM   1443 N  N    . ALA   A 1 421 ? 27.550  5.970   14.150  1.00 25.18  ? 432 ALA   A N    1 
ATOM   1444 C  CA   . ALA   A 1 421 ? 28.391  6.977   14.784  1.00 24.51  ? 432 ALA   A CA   1 
ATOM   1445 C  C    . ALA   A 1 421 ? 28.683  8.120   13.808  1.00 31.12  ? 432 ALA   A C    1 
ATOM   1446 O  O    . ALA   A 1 421 ? 28.694  7.909   12.596  1.00 26.61  ? 432 ALA   A O    1 
ATOM   1447 C  CB   . ALA   A 1 421 ? 29.698  6.338   15.239  1.00 25.63  ? 432 ALA   A CB   1 
ATOM   1448 N  N    . PRO   A 1 422 ? 28.952  9.335   14.315  1.00 29.43  ? 433 PRO   A N    1 
ATOM   1449 C  CA   . PRO   A 1 422 ? 29.182  10.474  13.403  1.00 27.07  ? 433 PRO   A CA   1 
ATOM   1450 C  C    . PRO   A 1 422 ? 30.343  10.272  12.442  1.00 33.04  ? 433 PRO   A C    1 
ATOM   1451 O  O    . PRO   A 1 422 ? 30.279  10.730  11.291  1.00 31.35  ? 433 PRO   A O    1 
ATOM   1452 C  CB   . PRO   A 1 422 ? 29.449  11.653  14.357  1.00 30.60  ? 433 PRO   A CB   1 
ATOM   1453 C  CG   . PRO   A 1 422 ? 28.866  11.213  15.697  1.00 29.14  ? 433 PRO   A CG   1 
ATOM   1454 C  CD   . PRO   A 1 422 ? 29.091  9.728   15.733  1.00 26.90  ? 433 PRO   A CD   1 
ATOM   1455 N  N    . GLU   A 1 423 ? 31.418  9.621   12.889  1.00 33.17  ? 434 GLU   A N    1 
ATOM   1456 C  CA   . GLU   A 1 423 ? 32.550  9.424   11.999  1.00 29.90  ? 434 GLU   A CA   1 
ATOM   1457 C  C    . GLU   A 1 423 ? 32.197  8.508   10.834  1.00 32.05  ? 434 GLU   A C    1 
ATOM   1458 O  O    . GLU   A 1 423 ? 32.799  8.631   9.759   1.00 31.33  ? 434 GLU   A O    1 
ATOM   1459 C  CB   . GLU   A 1 423 ? 33.752  8.879   12.775  1.00 31.18  ? 434 GLU   A CB   1 
ATOM   1460 C  CG   . GLU   A 1 423 ? 33.560  7.499   13.410  1.00 30.64  ? 434 GLU   A CG   1 
ATOM   1461 C  CD   . GLU   A 1 423 ? 33.153  7.572   14.881  1.00 33.35  ? 434 GLU   A CD   1 
ATOM   1462 O  OE1  . GLU   A 1 423 ? 32.525  8.569   15.299  1.00 26.54  ? 434 GLU   A OE1  1 
ATOM   1463 O  OE2  . GLU   A 1 423 ? 33.474  6.624   15.621  1.00 31.39  ? 434 GLU   A OE2  1 
ATOM   1464 N  N    . VAL   A 1 424 ? 31.222  7.609   11.015  1.00 25.91  ? 435 VAL   A N    1 
ATOM   1465 C  CA   . VAL   A 1 424 ? 30.736  6.783   9.907   1.00 28.49  ? 435 VAL   A CA   1 
ATOM   1466 C  C    . VAL   A 1 424 ? 29.876  7.621   8.972   1.00 30.21  ? 435 VAL   A C    1 
ATOM   1467 O  O    . VAL   A 1 424 ? 30.044  7.595   7.743   1.00 30.07  ? 435 VAL   A O    1 
ATOM   1468 C  CB   . VAL   A 1 424 ? 29.955  5.563   10.427  1.00 29.19  ? 435 VAL   A CB   1 
ATOM   1469 C  CG1  . VAL   A 1 424 ? 29.458  4.718   9.241   1.00 28.14  ? 435 VAL   A CG1  1 
ATOM   1470 C  CG2  . VAL   A 1 424 ? 30.817  4.727   11.344  1.00 29.63  ? 435 VAL   A CG2  1 
ATOM   1471 N  N    . VAL   A 1 425 ? 28.945  8.387   9.550   1.00 26.94  ? 436 VAL   A N    1 
ATOM   1472 C  CA   . VAL   A 1 425 ? 28.019  9.172   8.742   1.00 30.18  ? 436 VAL   A CA   1 
ATOM   1473 C  C    . VAL   A 1 425 ? 28.788  10.158  7.872   1.00 28.16  ? 436 VAL   A C    1 
ATOM   1474 O  O    . VAL   A 1 425 ? 28.430  10.378  6.708   1.00 31.16  ? 436 VAL   A O    1 
ATOM   1475 C  CB   . VAL   A 1 425 ? 27.009  9.918   9.648   1.00 26.68  ? 436 VAL   A CB   1 
ATOM   1476 C  CG1  . VAL   A 1 425 ? 26.219  10.942  8.832   1.00 27.84  ? 436 VAL   A CG1  1 
ATOM   1477 C  CG2  . VAL   A 1 425 ? 26.057  8.946   10.407  1.00 23.55  ? 436 VAL   A CG2  1 
ATOM   1478 N  N    . THR   A 1 426 ? 29.881  10.732  8.397   1.00 30.29  ? 437 THR   A N    1 
ATOM   1479 C  CA   . THR   A 1 426 ? 30.677  11.716  7.661   1.00 30.29  ? 437 THR   A CA   1 
ATOM   1480 C  C    . THR   A 1 426 ? 31.883  11.124  6.924   1.00 31.07  ? 437 THR   A C    1 
ATOM   1481 O  O    . THR   A 1 426 ? 32.739  11.887  6.453   1.00 33.06  ? 437 THR   A O    1 
ATOM   1482 C  CB   . THR   A 1 426 ? 31.144  12.847  8.590   1.00 34.24  ? 437 THR   A CB   1 
ATOM   1483 O  OG1  . THR   A 1 426 ? 31.945  12.325  9.656   1.00 32.30  ? 437 THR   A OG1  1 
ATOM   1484 C  CG2  . THR   A 1 426 ? 29.943  13.541  9.195   1.00 36.72  ? 437 THR   A CG2  1 
ATOM   1485 N  N    . ARG   A 1 427 ? 31.954  9.799   6.795   1.00 30.23  ? 438 ARG   A N    1 
ATOM   1486 C  CA   . ARG   A 1 427 ? 32.947  9.124   5.962   1.00 30.70  ? 438 ARG   A CA   1 
ATOM   1487 C  C    . ARG   A 1 427 ? 34.384  9.425   6.384   1.00 35.93  ? 438 ARG   A C    1 
ATOM   1488 O  O    . ARG   A 1 427 ? 35.266  9.630   5.546   1.00 35.73  ? 438 ARG   A O    1 
ATOM   1489 C  CB   . ARG   A 1 427 ? 32.702  9.487   4.494   1.00 33.73  ? 438 ARG   A CB   1 
ATOM   1490 C  CG   . ARG   A 1 427 ? 31.430  8.835   4.006   1.00 35.96  ? 438 ARG   A CG   1 
ATOM   1491 C  CD   . ARG   A 1 427 ? 31.000  9.267   2.625   1.00 35.28  ? 438 ARG   A CD   1 
ATOM   1492 N  NE   . ARG   A 1 427 ? 30.968  10.721  2.553   1.00 44.95  ? 438 ARG   A NE   1 
ATOM   1493 C  CZ   . ARG   A 1 427 ? 31.627  11.468  1.682   1.00 39.90  ? 438 ARG   A CZ   1 
ATOM   1494 N  NH1  . ARG   A 1 427 ? 32.293  10.934  0.667   1.00 45.08  ? 438 ARG   A NH1  1 
ATOM   1495 N  NH2  . ARG   A 1 427 ? 31.607  12.794  1.823   1.00 44.70  ? 438 ARG   A NH2  1 
ATOM   1496 N  N    . LYS   A 1 428 ? 34.617  9.492   7.692   1.00 31.17  ? 439 LYS   A N    1 
ATOM   1497 C  CA   . LYS   A 1 428 ? 35.977  9.556   8.208   1.00 44.64  ? 439 LYS   A CA   1 
ATOM   1498 C  C    . LYS   A 1 428 ? 36.507  8.146   8.461   1.00 40.15  ? 439 LYS   A C    1 
ATOM   1499 O  O    . LYS   A 1 428 ? 35.753  7.176   8.504   1.00 37.78  ? 439 LYS   A O    1 
ATOM   1500 C  CB   . LYS   A 1 428 ? 36.032  10.423  9.464   1.00 39.42  ? 439 LYS   A CB   1 
ATOM   1501 C  CG   . LYS   A 1 428 ? 35.458  11.814  9.188   1.00 42.03  ? 439 LYS   A CG   1 
ATOM   1502 C  CD   . LYS   A 1 428 ? 35.480  12.745  10.384  1.00 49.99  ? 439 LYS   A CD   1 
ATOM   1503 C  CE   . LYS   A 1 428 ? 34.803  14.065  10.026  1.00 49.33  ? 439 LYS   A CE   1 
ATOM   1504 N  NZ   . LYS   A 1 428 ? 34.601  14.956  11.206  1.00 60.78  ? 439 LYS   A NZ   1 
ATOM   1505 N  N    . ALA   A 1 429 ? 37.829  8.031   8.587   1.00 40.85  ? 440 ALA   A N    1 
ATOM   1506 C  CA   . ALA   A 1 429 ? 38.405  6.749   8.973   1.00 38.38  ? 440 ALA   A CA   1 
ATOM   1507 C  C    . ALA   A 1 429 ? 37.914  6.367   10.357  1.00 31.19  ? 440 ALA   A C    1 
ATOM   1508 O  O    . ALA   A 1 429 ? 37.964  7.180   11.284  1.00 37.43  ? 440 ALA   A O    1 
ATOM   1509 C  CB   . ALA   A 1 429 ? 39.931  6.824   8.957   1.00 43.59  ? 440 ALA   A CB   1 
ATOM   1510 N  N    . TYR   A 1 430 ? 37.450  5.124   10.508  1.00 38.10  ? 441 TYR   A N    1 
ATOM   1511 C  CA   . TYR   A 1 430 ? 36.850  4.713   11.773  1.00 37.23  ? 441 TYR   A CA   1 
ATOM   1512 C  C    . TYR   A 1 430 ? 37.259  3.288   12.128  1.00 40.42  ? 441 TYR   A C    1 
ATOM   1513 O  O    . TYR   A 1 430 ? 37.719  2.511   11.282  1.00 32.57  ? 441 TYR   A O    1 
ATOM   1514 C  CB   . TYR   A 1 430 ? 35.315  4.834   11.741  1.00 30.15  ? 441 TYR   A CB   1 
ATOM   1515 C  CG   . TYR   A 1 430 ? 34.600  3.953   10.732  1.00 28.95  ? 441 TYR   A CG   1 
ATOM   1516 C  CD1  . TYR   A 1 430 ? 34.302  2.623   11.026  1.00 32.59  ? 441 TYR   A CD1  1 
ATOM   1517 C  CD2  . TYR   A 1 430 ? 34.184  4.460   9.505   1.00 32.80  ? 441 TYR   A CD2  1 
ATOM   1518 C  CE1  . TYR   A 1 430 ? 33.634  1.817   10.119  1.00 35.41  ? 441 TYR   A CE1  1 
ATOM   1519 C  CE2  . TYR   A 1 430 ? 33.512  3.659   8.586   1.00 35.45  ? 441 TYR   A CE2  1 
ATOM   1520 C  CZ   . TYR   A 1 430 ? 33.240  2.337   8.901   1.00 35.73  ? 441 TYR   A CZ   1 
ATOM   1521 O  OH   . TYR   A 1 430 ? 32.571  1.535   8.000   1.00 34.27  ? 441 TYR   A OH   1 
ATOM   1522 N  N    . GLY   A 1 431 ? 37.061  2.950   13.401  1.00 33.56  ? 442 GLY   A N    1 
ATOM   1523 C  CA   . GLY   A 1 431 ? 37.439  1.659   13.917  1.00 33.85  ? 442 GLY   A CA   1 
ATOM   1524 C  C    . GLY   A 1 431 ? 36.376  1.034   14.794  1.00 30.22  ? 442 GLY   A C    1 
ATOM   1525 O  O    . GLY   A 1 431 ? 35.187  1.368   14.720  1.00 26.94  ? 442 GLY   A O    1 
ATOM   1526 N  N    . PRO   A 1 432 ? 36.807  0.106   15.653  1.00 29.04  ? 443 PRO   A N    1 
ATOM   1527 C  CA   . PRO   A 1 432 ? 35.854  -0.667  16.470  1.00 27.97  ? 443 PRO   A CA   1 
ATOM   1528 C  C    . PRO   A 1 432 ? 34.955  0.165   17.362  1.00 26.76  ? 443 PRO   A C    1 
ATOM   1529 O  O    . PRO   A 1 432 ? 33.872  -0.309  17.733  1.00 26.31  ? 443 PRO   A O    1 
ATOM   1530 C  CB   . PRO   A 1 432 ? 36.768  -1.574  17.308  1.00 30.13  ? 443 PRO   A CB   1 
ATOM   1531 C  CG   . PRO   A 1 432 ? 38.057  -1.641  16.558  1.00 33.84  ? 443 PRO   A CG   1 
ATOM   1532 C  CD   . PRO   A 1 432 ? 38.204  -0.318  15.860  1.00 31.53  ? 443 PRO   A CD   1 
ATOM   1533 N  N    . LYS   A 1 433 ? 35.357  1.378   17.735  1.00 24.61  ? 444 LYS   A N    1 
ATOM   1534 C  CA   . LYS   A 1 433 ? 34.541  2.146   18.666  1.00 25.79  ? 444 LYS   A CA   1 
ATOM   1535 C  C    . LYS   A 1 433 ? 33.243  2.638   18.051  1.00 25.91  ? 444 LYS   A C    1 
ATOM   1536 O  O    . LYS   A 1 433 ? 32.416  3.204   18.776  1.00 24.51  ? 444 LYS   A O    1 
ATOM   1537 C  CB   . LYS   A 1 433 ? 35.337  3.325   19.224  1.00 30.22  ? 444 LYS   A CB   1 
ATOM   1538 C  CG   . LYS   A 1 433 ? 36.309  2.903   20.322  1.00 36.83  ? 444 LYS   A CG   1 
ATOM   1539 C  CD   . LYS   A 1 433 ? 37.198  4.047   20.746  1.00 34.81  ? 444 LYS   A CD   1 
ATOM   1540 C  CE   . LYS   A 1 433 ? 38.127  3.658   21.894  1.00 35.67  ? 444 LYS   A CE   1 
ATOM   1541 N  NZ   . LYS   A 1 433 ? 38.965  4.817   22.341  1.00 32.72  ? 444 LYS   A NZ   1 
ATOM   1542 N  N    . VAL   A 1 434 ? 33.038  2.453   16.743  1.00 23.03  ? 445 VAL   A N    1 
ATOM   1543 C  CA   . VAL   A 1 434 ? 31.718  2.743   16.194  1.00 22.99  ? 445 VAL   A CA   1 
ATOM   1544 C  C    . VAL   A 1 434 ? 30.669  1.816   16.796  1.00 23.40  ? 445 VAL   A C    1 
ATOM   1545 O  O    . VAL   A 1 434 ? 29.493  2.184   16.884  1.00 22.55  ? 445 VAL   A O    1 
ATOM   1546 C  CB   . VAL   A 1 434 ? 31.718  2.656   14.656  1.00 25.25  ? 445 VAL   A CB   1 
ATOM   1547 C  CG1  . VAL   A 1 434 ? 32.794  3.584   14.072  1.00 24.33  ? 445 VAL   A CG1  1 
ATOM   1548 C  CG2  . VAL   A 1 434 ? 31.888  1.196   14.190  1.00 25.52  ? 445 VAL   A CG2  1 
ATOM   1549 N  N    . ASP   A 1 435 ? 31.064  0.592   17.183  1.00 21.31  ? 446 ASP   A N    1 
ATOM   1550 C  CA   . ASP   A 1 435 ? 30.128  -0.320  17.830  1.00 22.48  ? 446 ASP   A CA   1 
ATOM   1551 C  C    . ASP   A 1 435 ? 29.774  0.167   19.221  1.00 21.67  ? 446 ASP   A C    1 
ATOM   1552 O  O    . ASP   A 1 435 ? 28.661  -0.083  19.690  1.00 21.48  ? 446 ASP   A O    1 
ATOM   1553 C  CB   . ASP   A 1 435 ? 30.711  -1.729  17.937  1.00 21.35  ? 446 ASP   A CB   1 
ATOM   1554 C  CG   . ASP   A 1 435 ? 30.770  -2.452  16.602  1.00 21.24  ? 446 ASP   A CG   1 
ATOM   1555 O  OD1  . ASP   A 1 435 ? 29.963  -2.135  15.703  1.00 23.83  ? 446 ASP   A OD1  1 
ATOM   1556 O  OD2  . ASP   A 1 435 ? 31.577  -3.399  16.505  1.00 23.95  ? 446 ASP   A OD2  1 
ATOM   1557 N  N    . ILE   A 1 436 ? 30.712  0.845   19.888  1.00 20.49  ? 447 ILE   A N    1 
ATOM   1558 C  CA   . ILE   A 1 436 ? 30.450  1.415   21.213  1.00 24.26  ? 447 ILE   A CA   1 
ATOM   1559 C  C    . ILE   A 1 436 ? 29.438  2.551   21.112  1.00 26.18  ? 447 ILE   A C    1 
ATOM   1560 O  O    . ILE   A 1 436 ? 28.520  2.666   21.935  1.00 22.82  ? 447 ILE   A O    1 
ATOM   1561 C  CB   . ILE   A 1 436 ? 31.771  1.885   21.846  1.00 29.44  ? 447 ILE   A CB   1 
ATOM   1562 C  CG1  . ILE   A 1 436 ? 32.694  0.687   22.107  1.00 25.87  ? 447 ILE   A CG1  1 
ATOM   1563 C  CG2  . ILE   A 1 436 ? 31.495  2.706   23.117  1.00 26.65  ? 447 ILE   A CG2  1 
ATOM   1564 C  CD1  . ILE   A 1 436 ? 32.135  -0.323  23.114  1.00 26.25  ? 447 ILE   A CD1  1 
ATOM   1565 N  N    . TRP   A 1 437 ? 29.585  3.405   20.094  1.00 21.28  ? 448 TRP   A N    1 
ATOM   1566 C  CA   . TRP   A 1 437 ? 28.580  4.424   19.808  1.00 20.29  ? 448 TRP   A CA   1 
ATOM   1567 C  C    . TRP   A 1 437 ? 27.202  3.801   19.612  1.00 22.81  ? 448 TRP   A C    1 
ATOM   1568 O  O    . TRP   A 1 437 ? 26.217  4.251   20.205  1.00 20.85  ? 448 TRP   A O    1 
ATOM   1569 C  CB   . TRP   A 1 437 ? 28.975  5.225   18.560  1.00 18.45  ? 448 TRP   A CB   1 
ATOM   1570 C  CG   . TRP   A 1 437 ? 27.914  6.232   18.188  1.00 21.42  ? 448 TRP   A CG   1 
ATOM   1571 C  CD1  . TRP   A 1 437 ? 26.747  5.991   17.530  1.00 22.71  ? 448 TRP   A CD1  1 
ATOM   1572 C  CD2  . TRP   A 1 437 ? 27.926  7.630   18.483  1.00 21.31  ? 448 TRP   A CD2  1 
ATOM   1573 N  NE1  . TRP   A 1 437 ? 26.020  7.155   17.410  1.00 22.44  ? 448 TRP   A NE1  1 
ATOM   1574 C  CE2  . TRP   A 1 437 ? 26.727  8.176   17.984  1.00 23.04  ? 448 TRP   A CE2  1 
ATOM   1575 C  CE3  . TRP   A 1 437 ? 28.834  8.474   19.125  1.00 22.95  ? 448 TRP   A CE3  1 
ATOM   1576 C  CZ2  . TRP   A 1 437 ? 26.416  9.530   18.103  1.00 22.90  ? 448 TRP   A CZ2  1 
ATOM   1577 C  CZ3  . TRP   A 1 437 ? 28.524  9.804   19.248  1.00 29.94  ? 448 TRP   A CZ3  1 
ATOM   1578 C  CH2  . TRP   A 1 437 ? 27.328  10.324  18.737  1.00 31.86  ? 448 TRP   A CH2  1 
ATOM   1579 N  N    . SER   A 1 438 ? 27.107  2.780   18.750  1.00 19.29  ? 449 SER   A N    1 
ATOM   1580 C  CA   . SER   A 1 438 ? 25.813  2.157   18.481  1.00 18.20  ? 449 SER   A CA   1 
ATOM   1581 C  C    . SER   A 1 438 ? 25.225  1.537   19.750  1.00 19.62  ? 449 SER   A C    1 
ATOM   1582 O  O    . SER   A 1 438 ? 24.007  1.571   19.955  1.00 18.74  ? 449 SER   A O    1 
ATOM   1583 C  CB   . SER   A 1 438 ? 25.955  1.111   17.373  1.00 17.13  ? 449 SER   A CB   1 
ATOM   1584 O  OG   . SER   A 1 438 ? 26.439  1.730   16.174  1.00 21.87  ? 449 SER   A OG   1 
ATOM   1585 N  N    . LEU   A 1 439 ? 26.077  0.963   20.608  1.00 20.04  ? 450 LEU   A N    1 
ATOM   1586 C  CA   . LEU   A 1 439 ? 25.595  0.467   21.899  1.00 21.01  ? 450 LEU   A CA   1 
ATOM   1587 C  C    . LEU   A 1 439 ? 25.005  1.596   22.735  1.00 18.87  ? 450 LEU   A C    1 
ATOM   1588 O  O    . LEU   A 1 439 ? 24.005  1.400   23.437  1.00 21.65  ? 450 LEU   A O    1 
ATOM   1589 C  CB   . LEU   A 1 439 ? 26.724  -0.217  22.664  1.00 23.74  ? 450 LEU   A CB   1 
ATOM   1590 C  CG   . LEU   A 1 439 ? 26.368  -0.626  24.102  1.00 27.51  ? 450 LEU   A CG   1 
ATOM   1591 C  CD1  . LEU   A 1 439 ? 25.322  -1.745  24.123  1.00 25.09  ? 450 LEU   A CD1  1 
ATOM   1592 C  CD2  . LEU   A 1 439 ? 27.619  -1.053  24.850  1.00 27.62  ? 450 LEU   A CD2  1 
ATOM   1593 N  N    . GLY   A 1 440 ? 25.647  2.767   22.714  1.00 20.69  ? 451 GLY   A N    1 
ATOM   1594 C  CA   . GLY   A 1 440 ? 25.096  3.931   23.391  1.00 21.47  ? 451 GLY   A CA   1 
ATOM   1595 C  C    . GLY   A 1 440 ? 23.725  4.308   22.870  1.00 23.89  ? 451 GLY   A C    1 
ATOM   1596 O  O    . GLY   A 1 440 ? 22.827  4.639   23.650  1.00 22.02  ? 451 GLY   A O    1 
ATOM   1597 N  N    . ILE   A 1 441 ? 23.546  4.281   21.544  1.00 18.02  ? 452 ILE   A N    1 
ATOM   1598 C  CA   . ILE   A 1 441 ? 22.222  4.528   20.971  1.00 18.81  ? 452 ILE   A CA   1 
ATOM   1599 C  C    . ILE   A 1 441 ? 21.232  3.464   21.437  1.00 21.72  ? 452 ILE   A C    1 
ATOM   1600 O  O    . ILE   A 1 441 ? 20.056  3.760   21.690  1.00 20.52  ? 452 ILE   A O    1 
ATOM   1601 C  CB   . ILE   A 1 441 ? 22.291  4.600   19.436  1.00 18.70  ? 452 ILE   A CB   1 
ATOM   1602 C  CG1  . ILE   A 1 441 ? 23.251  5.721   19.006  1.00 20.85  ? 452 ILE   A CG1  1 
ATOM   1603 C  CG2  . ILE   A 1 441 ? 20.900  4.877   18.852  1.00 19.16  ? 452 ILE   A CG2  1 
ATOM   1604 C  CD1  . ILE   A 1 441 ? 22.757  7.117   19.353  1.00 27.31  ? 452 ILE   A CD1  1 
ATOM   1605 N  N    . MET   A 1 442 ? 21.677  2.207   21.541  1.00 17.72  ? 453 MET   A N    1 
ATOM   1606 C  CA   . MET   A 1 442 ? 20.779  1.157   22.032  1.00 18.29  ? 453 MET   A CA   1 
ATOM   1607 C  C    . MET   A 1 442 ? 20.406  1.383   23.500  1.00 22.58  ? 453 MET   A C    1 
ATOM   1608 O  O    . MET   A 1 442 ? 19.295  1.047   23.926  1.00 20.27  ? 453 MET   A O    1 
ATOM   1609 C  CB   . MET   A 1 442 ? 21.443  -0.210  21.831  1.00 22.46  ? 453 MET   A CB   1 
ATOM   1610 C  CG   . MET   A 1 442 ? 20.504  -1.393  21.882  1.00 30.49  ? 453 MET   A CG   1 
ATOM   1611 S  SD   . MET   A 1 442 ? 21.325  -2.871  21.200  1.00 28.51  ? 453 MET   A SD   1 
ATOM   1612 C  CE   . MET   A 1 442 ? 22.568  -3.178  22.446  1.00 32.61  ? 453 MET   A CE   1 
ATOM   1613 N  N    . ALA   A 1 443 ? 21.312  1.945   24.291  1.00 18.67  ? 454 ALA   A N    1 
ATOM   1614 C  CA   . ALA   A 1 443 ? 20.943  2.303   25.659  1.00 23.96  ? 454 ALA   A CA   1 
ATOM   1615 C  C    . ALA   A 1 443 ? 19.898  3.418   25.675  1.00 25.94  ? 454 ALA   A C    1 
ATOM   1616 O  O    . ALA   A 1 443 ? 18.996  3.416   26.520  1.00 21.88  ? 454 ALA   A O    1 
ATOM   1617 C  CB   . ALA   A 1 443 ? 22.188  2.680   26.449  1.00 23.60  ? 454 ALA   A CB   1 
ATOM   1618 N  N    . ILE   A 1 444 ? 19.982  4.368   24.739  1.00 20.14  ? 455 ILE   A N    1 
ATOM   1619 C  CA   . ILE   A 1 444 ? 18.920  5.361   24.601  1.00 19.40  ? 455 ILE   A CA   1 
ATOM   1620 C  C    . ILE   A 1 444 ? 17.603  4.686   24.228  1.00 21.16  ? 455 ILE   A C    1 
ATOM   1621 O  O    . ILE   A 1 444 ? 16.528  5.078   24.714  1.00 22.64  ? 455 ILE   A O    1 
ATOM   1622 C  CB   . ILE   A 1 444 ? 19.322  6.461   23.598  1.00 20.09  ? 455 ILE   A CB   1 
ATOM   1623 C  CG1  . ILE   A 1 444 ? 20.470  7.290   24.189  1.00 20.20  ? 455 ILE   A CG1  1 
ATOM   1624 C  CG2  . ILE   A 1 444 ? 18.136  7.371   23.296  1.00 21.93  ? 455 ILE   A CG2  1 
ATOM   1625 C  CD1  . ILE   A 1 444 ? 20.942  8.463   23.284  1.00 27.57  ? 455 ILE   A CD1  1 
ATOM   1626 N  N    . GLU   A 1 445 ? 17.654  3.675   23.354  1.00 19.81  ? 456 GLU   A N    1 
ATOM   1627 C  CA   . GLU   A 1 445 ? 16.447  2.894   23.086  1.00 20.14  ? 456 GLU   A CA   1 
ATOM   1628 C  C    . GLU   A 1 445 ? 15.877  2.320   24.372  1.00 20.09  ? 456 GLU   A C    1 
ATOM   1629 O  O    . GLU   A 1 445 ? 14.659  2.288   24.557  1.00 21.87  ? 456 GLU   A O    1 
ATOM   1630 C  CB   . GLU   A 1 445 ? 16.734  1.723   22.147  1.00 19.31  ? 456 GLU   A CB   1 
ATOM   1631 C  CG   . GLU   A 1 445 ? 17.061  2.033   20.679  1.00 20.16  ? 456 GLU   A CG   1 
ATOM   1632 C  CD   . GLU   A 1 445 ? 17.095  0.721   19.914  1.00 20.36  ? 456 GLU   A CD   1 
ATOM   1633 O  OE1  . GLU   A 1 445 ? 16.006  0.217   19.573  1.00 20.16  ? 456 GLU   A OE1  1 
ATOM   1634 O  OE2  . GLU   A 1 445 ? 18.194  0.157   19.729  1.00 20.32  ? 456 GLU   A OE2  1 
ATOM   1635 N  N    . MET   A 1 446 ? 16.743  1.787   25.234  1.00 17.48  ? 457 MET   A N    1 
ATOM   1636 C  CA   . MET   A 1 446 ? 16.268  1.166   26.467  1.00 23.28  ? 457 MET   A CA   1 
ATOM   1637 C  C    . MET   A 1 446 ? 15.659  2.201   27.405  1.00 24.73  ? 457 MET   A C    1 
ATOM   1638 O  O    . MET   A 1 446 ? 14.738  1.876   28.166  1.00 26.50  ? 457 MET   A O    1 
ATOM   1639 C  CB   . MET   A 1 446 ? 17.400  0.394   27.144  1.00 19.60  ? 457 MET   A CB   1 
ATOM   1640 C  CG   . MET   A 1 446 ? 17.786  -0.881  26.357  1.00 24.34  ? 457 MET   A CG   1 
ATOM   1641 S  SD   . MET   A 1 446 ? 18.973  -1.968  27.169  1.00 24.96  ? 457 MET   A SD   1 
ATOM   1642 C  CE   . MET   A 1 446 ? 20.512  -1.497  26.363  1.00 28.48  ? 457 MET   A CE   1 
ATOM   1643 N  N    . ILE   A 1 447 ? 16.183  3.430   27.392  1.00 21.55  ? 458 ILE   A N    1 
ATOM   1644 C  CA   . ILE   A 1 447 ? 15.666  4.501   28.248  1.00 26.97  ? 458 ILE   A CA   1 
ATOM   1645 C  C    . ILE   A 1 447 ? 14.381  5.094   27.688  1.00 28.26  ? 458 ILE   A C    1 
ATOM   1646 O  O    . ILE   A 1 447 ? 13.396  5.286   28.416  1.00 27.90  ? 458 ILE   A O    1 
ATOM   1647 C  CB   . ILE   A 1 447 ? 16.701  5.640   28.366  1.00 26.49  ? 458 ILE   A CB   1 
ATOM   1648 C  CG1  . ILE   A 1 447 ? 17.971  5.223   29.079  1.00 30.67  ? 458 ILE   A CG1  1 
ATOM   1649 C  CG2  . ILE   A 1 447 ? 16.063  6.888   29.017  1.00 31.29  ? 458 ILE   A CG2  1 
ATOM   1650 C  CD1  . ILE   A 1 447 ? 19.088  6.208   28.806  1.00 34.14  ? 458 ILE   A CD1  1 
ATOM   1651 N  N    . GLU   A 1 448 ? 14.403  5.469   26.404  1.00 24.62  ? 459 GLU   A N    1 
ATOM   1652 C  CA   . GLU   A 1 448 ? 13.340  6.270   25.799  1.00 23.72  ? 459 GLU   A CA   1 
ATOM   1653 C  C    . GLU   A 1 448 ? 12.410  5.500   24.879  1.00 25.69  ? 459 GLU   A C    1 
ATOM   1654 O  O    . GLU   A 1 448 ? 11.341  6.024   24.531  1.00 29.86  ? 459 GLU   A O    1 
ATOM   1655 C  CB   . GLU   A 1 448 ? 13.950  7.456   25.022  1.00 27.06  ? 459 GLU   A CB   1 
ATOM   1656 C  CG   . GLU   A 1 448 ? 14.762  8.391   25.909  1.00 34.89  ? 459 GLU   A CG   1 
ATOM   1657 C  CD   . GLU   A 1 448 ? 15.199  9.679   25.214  1.00 39.12  ? 459 GLU   A CD   1 
ATOM   1658 O  OE1  . GLU   A 1 448 ? 15.198  9.745   23.964  1.00 32.66  ? 459 GLU   A OE1  1 
ATOM   1659 O  OE2  . GLU   A 1 448 ? 15.559  10.630  25.930  1.00 40.25  ? 459 GLU   A OE2  1 
ATOM   1660 N  N    . GLY   A 1 449 ? 12.780  4.285   24.473  1.00 22.19  ? 460 GLY   A N    1 
ATOM   1661 C  CA   . GLY   A 1 449 ? 11.983  3.459   23.589  1.00 22.19  ? 460 GLY   A CA   1 
ATOM   1662 C  C    . GLY   A 1 449 ? 12.343  3.554   22.119  1.00 26.44  ? 460 GLY   A C    1 
ATOM   1663 O  O    . GLY   A 1 449 ? 11.898  2.708   21.337  1.00 22.54  ? 460 GLY   A O    1 
ATOM   1664 N  N    . GLU   A 1 450 ? 13.211  4.486   21.743  1.00 26.52  ? 461 GLU   A N    1 
ATOM   1665 C  CA   . GLU   A 1 450 ? 13.565  4.713   20.349  1.00 24.78  ? 461 GLU   A CA   1 
ATOM   1666 C  C    . GLU   A 1 450 ? 14.954  5.318   20.308  1.00 26.08  ? 461 GLU   A C    1 
ATOM   1667 O  O    . GLU   A 1 450 ? 15.377  5.963   21.276  1.00 23.13  ? 461 GLU   A O    1 
ATOM   1668 C  CB   . GLU   A 1 450 ? 12.586  5.679   19.650  1.00 29.51  ? 461 GLU   A CB   1 
ATOM   1669 C  CG   . GLU   A 1 450 ? 11.184  5.159   19.363  1.00 30.89  ? 461 GLU   A CG   1 
ATOM   1670 C  CD   . GLU   A 1 450 ? 10.303  6.199   18.674  1.00 44.93  ? 461 GLU   A CD   1 
ATOM   1671 O  OE1  . GLU   A 1 450 ? 10.761  7.347   18.496  1.00 35.75  ? 461 GLU   A OE1  1 
ATOM   1672 O  OE2  . GLU   A 1 450 ? 9.159   5.870   18.295  1.00 38.34  ? 461 GLU   A OE2  1 
ATOM   1673 N  N    . PRO   A 1 451 ? 15.684  5.133   19.214  1.00 19.46  ? 462 PRO   A N    1 
ATOM   1674 C  CA   . PRO   A 1 451 ? 16.914  5.888   19.005  1.00 22.91  ? 462 PRO   A CA   1 
ATOM   1675 C  C    . PRO   A 1 451 ? 16.573  7.341   18.729  1.00 21.27  ? 462 PRO   A C    1 
ATOM   1676 O  O    . PRO   A 1 451 ? 15.436  7.656   18.338  1.00 22.43  ? 462 PRO   A O    1 
ATOM   1677 C  CB   . PRO   A 1 451 ? 17.542  5.218   17.765  1.00 23.61  ? 462 PRO   A CB   1 
ATOM   1678 C  CG   . PRO   A 1 451 ? 16.367  4.655   17.012  1.00 21.91  ? 462 PRO   A CG   1 
ATOM   1679 C  CD   . PRO   A 1 451 ? 15.333  4.285   18.057  1.00 21.98  ? 462 PRO   A CD   1 
ATOM   1680 N  N    . PRO   A 1 452 ? 17.509  8.266   18.906  1.00 23.71  ? 463 PRO   A N    1 
ATOM   1681 C  CA   . PRO   A 1 452 ? 17.213  9.649   18.519  1.00 27.14  ? 463 PRO   A CA   1 
ATOM   1682 C  C    . PRO   A 1 452 ? 16.835  9.746   17.050  1.00 27.49  ? 463 PRO   A C    1 
ATOM   1683 O  O    . PRO   A 1 452 ? 17.351  9.019   16.198  1.00 25.27  ? 463 PRO   A O    1 
ATOM   1684 C  CB   . PRO   A 1 452 ? 18.526  10.395  18.797  1.00 29.05  ? 463 PRO   A CB   1 
ATOM   1685 C  CG   . PRO   A 1 452 ? 19.297  9.494   19.743  1.00 27.77  ? 463 PRO   A CG   1 
ATOM   1686 C  CD   . PRO   A 1 452 ? 18.885  8.092   19.402  1.00 24.81  ? 463 PRO   A CD   1 
ATOM   1687 N  N    . TYR   A 1 453 ? 15.943  10.692  16.766  1.00 24.52  ? 464 TYR   A N    1 
ATOM   1688 C  CA   . TYR   A 1 453 ? 15.508  11.120  15.437  1.00 31.99  ? 464 TYR   A CA   1 
ATOM   1689 C  C    . TYR   A 1 453 ? 14.679  10.072  14.694  1.00 25.32  ? 464 TYR   A C    1 
ATOM   1690 O  O    . TYR   A 1 453 ? 14.495  10.208  13.499  1.00 27.20  ? 464 TYR   A O    1 
ATOM   1691 C  CB   . TYR   A 1 453 ? 16.692  11.532  14.542  1.00 27.57  ? 464 TYR   A CB   1 
ATOM   1692 C  CG   . TYR   A 1 453 ? 17.785  12.291  15.271  1.00 31.69  ? 464 TYR   A CG   1 
ATOM   1693 C  CD1  . TYR   A 1 453 ? 17.506  13.440  16.011  1.00 36.53  ? 464 TYR   A CD1  1 
ATOM   1694 C  CD2  . TYR   A 1 453 ? 19.104  11.846  15.219  1.00 29.90  ? 464 TYR   A CD2  1 
ATOM   1695 C  CE1  . TYR   A 1 453 ? 18.516  14.117  16.690  1.00 33.98  ? 464 TYR   A CE1  1 
ATOM   1696 C  CE2  . TYR   A 1 453 ? 20.113  12.511  15.883  1.00 30.21  ? 464 TYR   A CE2  1 
ATOM   1697 C  CZ   . TYR   A 1 453 ? 19.818  13.636  16.624  1.00 31.71  ? 464 TYR   A CZ   1 
ATOM   1698 O  OH   . TYR   A 1 453 ? 20.840  14.281  17.281  1.00 33.47  ? 464 TYR   A OH   1 
ATOM   1699 N  N    . LEU   A 1 454 ? 14.167  9.030   15.368  1.00 26.56  ? 465 LEU   A N    1 
ATOM   1700 C  CA   . LEU   A 1 454 ? 13.418  7.977   14.663  1.00 27.89  ? 465 LEU   A CA   1 
ATOM   1701 C  C    . LEU   A 1 454 ? 12.217  8.517   13.892  1.00 31.78  ? 465 LEU   A C    1 
ATOM   1702 O  O    . LEU   A 1 454 ? 11.836  7.952   12.858  1.00 34.39  ? 465 LEU   A O    1 
ATOM   1703 C  CB   . LEU   A 1 454 ? 12.950  6.889   15.640  1.00 27.53  ? 465 LEU   A CB   1 
ATOM   1704 C  CG   . LEU   A 1 454 ? 12.486  5.596   14.940  1.00 28.39  ? 465 LEU   A CG   1 
ATOM   1705 C  CD1  . LEU   A 1 454 ? 13.558  5.019   14.012  1.00 33.31  ? 465 LEU   A CD1  1 
ATOM   1706 C  CD2  . LEU   A 1 454 ? 12.011  4.562   15.940  1.00 30.26  ? 465 LEU   A CD2  1 
ATOM   1707 N  N    . ASN   A 1 455 ? 11.611  9.612   14.350  1.00 34.49  ? 466 ASN   A N    1 
ATOM   1708 C  CA   . ASN   A 1 455 ? 10.462  10.122  13.612  1.00 31.49  ? 466 ASN   A CA   1 
ATOM   1709 C  C    . ASN   A 1 455 ? 10.861  10.826  12.319  1.00 34.84  ? 466 ASN   A C    1 
ATOM   1710 O  O    . ASN   A 1 455 ? 9.988   11.106  11.489  1.00 38.37  ? 466 ASN   A O    1 
ATOM   1711 C  CB   . ASN   A 1 455 ? 9.689   11.098  14.506  1.00 37.83  ? 466 ASN   A CB   1 
ATOM   1712 C  CG   . ASN   A 1 455 ? 10.551  12.267  14.943  1.00 41.09  ? 466 ASN   A CG   1 
ATOM   1713 O  OD1  . ASN   A 1 455 ? 11.555  12.078  15.631  1.00 45.18  ? 466 ASN   A OD1  1 
ATOM   1714 N  ND2  . ASN   A 1 455 ? 10.185  13.472  14.527  1.00 38.61  ? 466 ASN   A ND2  1 
ATOM   1715 N  N    . GLU   A 1 456 ? 12.154  11.035  12.092  1.00 35.72  ? 467 GLU   A N    1 
ATOM   1716 C  CA   . GLU   A 1 456 ? 12.669  11.698  10.902  1.00 31.48  ? 467 GLU   A CA   1 
ATOM   1717 C  C    . GLU   A 1 456 ? 12.996  10.652  9.838   1.00 37.10  ? 467 GLU   A C    1 
ATOM   1718 O  O    . GLU   A 1 456 ? 13.160  9.467   10.138  1.00 32.48  ? 467 GLU   A O    1 
ATOM   1719 C  CB   . GLU   A 1 456 ? 13.928  12.500  11.233  1.00 35.20  ? 467 GLU   A CB   1 
ATOM   1720 C  CG   . GLU   A 1 456 ? 13.788  13.445  12.409  1.00 39.42  ? 467 GLU   A CG   1 
ATOM   1721 C  CD   . GLU   A 1 456 ? 12.918  14.654  12.115  1.00 43.44  ? 467 GLU   A CD   1 
ATOM   1722 O  OE1  . GLU   A 1 456 ? 12.495  14.828  10.953  1.00 43.58  ? 467 GLU   A OE1  1 
ATOM   1723 O  OE2  . GLU   A 1 456 ? 12.668  15.437  13.054  1.00 48.75  ? 467 GLU   A OE2  1 
ATOM   1724 N  N    . ASN   A 1 457 ? 13.078  11.103  8.582   1.00 37.28  ? 468 ASN   A N    1 
ATOM   1725 C  CA   . ASN   A 1 457 ? 13.527  10.222  7.515   1.00 47.99  ? 468 ASN   A CA   1 
ATOM   1726 C  C    . ASN   A 1 457 ? 14.992  9.841   7.718   1.00 36.87  ? 468 ASN   A C    1 
ATOM   1727 O  O    . ASN   A 1 457 ? 15.755  10.589  8.336   1.00 40.23  ? 468 ASN   A O    1 
ATOM   1728 C  CB   . ASN   A 1 457 ? 13.328  10.870  6.134   1.00 48.13  ? 468 ASN   A CB   1 
ATOM   1729 C  CG   . ASN   A 1 457 ? 14.370  11.915  5.784   1.00 57.87  ? 468 ASN   A CG   1 
ATOM   1730 O  OD1  . ASN   A 1 457 ? 15.537  11.599  5.553   1.00 56.68  ? 468 ASN   A OD1  1 
ATOM   1731 N  ND2  . ASN   A 1 457 ? 13.931  13.164  5.669   1.00 58.03  ? 468 ASN   A ND2  1 
ATOM   1732 N  N    . PRO   A 1 458 ? 15.404  8.667   7.219   1.00 42.79  ? 469 PRO   A N    1 
ATOM   1733 C  CA   . PRO   A 1 458 ? 16.790  8.225   7.449   1.00 32.68  ? 469 PRO   A CA   1 
ATOM   1734 C  C    . PRO   A 1 458 ? 17.830  9.208   6.946   1.00 30.41  ? 469 PRO   A C    1 
ATOM   1735 O  O    . PRO   A 1 458 ? 18.877  9.355   7.589   1.00 36.31  ? 469 PRO   A O    1 
ATOM   1736 C  CB   . PRO   A 1 458 ? 16.854  6.883   6.707   1.00 42.49  ? 469 PRO   A CB   1 
ATOM   1737 C  CG   . PRO   A 1 458 ? 15.445  6.388   6.727   1.00 47.98  ? 469 PRO   A CG   1 
ATOM   1738 C  CD   . PRO   A 1 458 ? 14.596  7.623   6.565   1.00 42.54  ? 469 PRO   A CD   1 
ATOM   1739 N  N    . LEU   A 1 459 ? 17.585  9.881   5.816   1.00 31.71  ? 470 LEU   A N    1 
ATOM   1740 C  CA   . LEU   A 1 459 ? 18.556  10.864  5.342   1.00 36.23  ? 470 LEU   A CA   1 
ATOM   1741 C  C    . LEU   A 1 459 ? 18.607  12.071  6.261   1.00 31.80  ? 470 LEU   A C    1 
ATOM   1742 O  O    . LEU   A 1 459 ? 19.694  12.566  6.579   1.00 36.54  ? 470 LEU   A O    1 
ATOM   1743 C  CB   . LEU   A 1 459 ? 18.245  11.304  3.911   1.00 44.35  ? 470 LEU   A CB   1 
ATOM   1744 C  CG   . LEU   A 1 459 ? 18.916  10.461  2.839   1.00 54.75  ? 470 LEU   A CG   1 
ATOM   1745 C  CD1  . LEU   A 1 459 ? 20.398  10.785  2.913   1.00 53.94  ? 470 LEU   A CD1  1 
ATOM   1746 C  CD2  . LEU   A 1 459 ? 18.678  8.964   3.022   1.00 46.48  ? 470 LEU   A CD2  1 
ATOM   1747 N  N    . ARG   A 1 460 ? 17.446  12.546  6.717   1.00 43.27  ? 471 ARG   A N    1 
ATOM   1748 C  CA   . ARG   A 1 460 ? 17.424  13.650  7.671   1.00 36.38  ? 471 ARG   A CA   1 
ATOM   1749 C  C    . ARG   A 1 460 ? 18.110  13.254  8.973   1.00 37.42  ? 471 ARG   A C    1 
ATOM   1750 O  O    . ARG   A 1 460 ? 18.840  14.056  9.572   1.00 36.11  ? 471 ARG   A O    1 
ATOM   1751 C  CB   . ARG   A 1 460 ? 15.984  14.095  7.926   1.00 42.60  ? 471 ARG   A CB   1 
ATOM   1752 C  CG   . ARG   A 1 460 ? 15.837  15.187  8.971   1.00 49.56  ? 471 ARG   A CG   1 
ATOM   1753 C  CD   . ARG   A 1 460 ? 16.490  16.487  8.534   1.00 54.98  ? 471 ARG   A CD   1 
ATOM   1754 N  NE   . ARG   A 1 460 ? 16.312  17.523  9.548   1.00 74.38  ? 471 ARG   A NE   1 
ATOM   1755 C  CZ   . ARG   A 1 460 ? 16.856  18.732  9.506   1.00 67.71  ? 471 ARG   A CZ   1 
ATOM   1756 N  NH1  . ARG   A 1 460 ? 17.652  19.100  8.512   1.00 66.05  ? 471 ARG   A NH1  1 
ATOM   1757 N  NH2  . ARG   A 1 460 ? 16.607  19.590  10.495  1.00 63.40  ? 471 ARG   A NH2  1 
ATOM   1758 N  N    . ALA   A 1 461 ? 17.888  12.016  9.428   1.00 33.89  ? 472 ALA   A N    1 
ATOM   1759 C  CA   . ALA   A 1 461 ? 18.567  11.547  10.631  1.00 33.06  ? 472 ALA   A CA   1 
ATOM   1760 C  C    . ALA   A 1 461 ? 20.079  11.529  10.440  1.00 35.16  ? 472 ALA   A C    1 
ATOM   1761 O  O    . ALA   A 1 461 ? 20.828  11.897  11.353  1.00 32.33  ? 472 ALA   A O    1 
ATOM   1762 C  CB   . ALA   A 1 461 ? 18.048  10.162  11.029  1.00 30.84  ? 472 ALA   A CB   1 
ATOM   1763 N  N    . LEU   A 1 462 ? 20.552  11.122  9.252   1.00 33.77  ? 473 LEU   A N    1 
ATOM   1764 C  CA   . LEU   A 1 462 ? 21.984  11.188  8.971   1.00 27.80  ? 473 LEU   A CA   1 
ATOM   1765 C  C    . LEU   A 1 462 ? 22.501  12.617  9.085   1.00 34.99  ? 473 LEU   A C    1 
ATOM   1766 O  O    . LEU   A 1 462 ? 23.567  12.862  9.667   1.00 32.17  ? 473 LEU   A O    1 
ATOM   1767 C  CB   . LEU   A 1 462 ? 22.280  10.640  7.569   1.00 34.81  ? 473 LEU   A CB   1 
ATOM   1768 C  CG   . LEU   A 1 462 ? 22.151  9.136   7.325   1.00 33.52  ? 473 LEU   A CG   1 
ATOM   1769 C  CD1  . LEU   A 1 462 ? 22.445  8.835   5.847   1.00 33.83  ? 473 LEU   A CD1  1 
ATOM   1770 C  CD2  . LEU   A 1 462 ? 23.073  8.340   8.243   1.00 29.78  ? 473 LEU   A CD2  1 
ATOM   1771 N  N    . TYR   A 1 463 ? 21.764  13.574  8.524   1.00 37.10  ? 474 TYR   A N    1 
ATOM   1772 C  CA   . TYR   A 1 463 ? 22.155  14.972  8.647   1.00 35.99  ? 474 TYR   A CA   1 
ATOM   1773 C  C    . TYR   A 1 463 ? 22.213  15.410  10.106  1.00 36.96  ? 474 TYR   A C    1 
ATOM   1774 O  O    . TYR   A 1 463 ? 23.149  16.109  10.517  1.00 38.14  ? 474 TYR   A O    1 
ATOM   1775 C  CB   . TYR   A 1 463 ? 21.181  15.858  7.875   1.00 40.14  ? 474 TYR   A CB   1 
ATOM   1776 C  CG   . TYR   A 1 463 ? 21.437  17.328  8.114   1.00 40.92  ? 474 TYR   A CG   1 
ATOM   1777 C  CD1  . TYR   A 1 463 ? 22.379  18.031  7.377   1.00 41.58  ? 474 TYR   A CD1  1 
ATOM   1778 C  CD2  . TYR   A 1 463 ? 20.738  18.009  9.110   1.00 46.90  ? 474 TYR   A CD2  1 
ATOM   1779 C  CE1  . TYR   A 1 463 ? 22.609  19.379  7.617   1.00 47.80  ? 474 TYR   A CE1  1 
ATOM   1780 C  CE2  . TYR   A 1 463 ? 20.958  19.354  9.356   1.00 52.59  ? 474 TYR   A CE2  1 
ATOM   1781 C  CZ   . TYR   A 1 463 ? 21.892  20.035  8.612   1.00 51.92  ? 474 TYR   A CZ   1 
ATOM   1782 O  OH   . TYR   A 1 463 ? 22.099  21.373  8.873   1.00 57.89  ? 474 TYR   A OH   1 
ATOM   1783 N  N    . LEU   A 1 464 ? 21.217  15.020  10.898  1.00 34.77  ? 475 LEU   A N    1 
ATOM   1784 C  CA   . LEU   A 1 464 ? 21.189  15.418  12.306  1.00 35.79  ? 475 LEU   A CA   1 
ATOM   1785 C  C    . LEU   A 1 464 ? 22.351  14.816  13.087  1.00 37.29  ? 475 LEU   A C    1 
ATOM   1786 O  O    . LEU   A 1 464 ? 22.913  15.466  13.976  1.00 33.14  ? 475 LEU   A O    1 
ATOM   1787 C  CB   . LEU   A 1 464 ? 19.846  15.040  12.929  1.00 35.96  ? 475 LEU   A CB   1 
ATOM   1788 C  CG   . LEU   A 1 464 ? 18.679  15.874  12.392  1.00 41.01  ? 475 LEU   A CG   1 
ATOM   1789 C  CD1  . LEU   A 1 464 ? 17.325  15.314  12.801  1.00 35.21  ? 475 LEU   A CD1  1 
ATOM   1790 C  CD2  . LEU   A 1 464 ? 18.817  17.317  12.873  1.00 39.85  ? 475 LEU   A CD2  1 
ATOM   1791 N  N    . ILE   A 1 465 ? 22.720  13.574  12.785  1.00 31.62  ? 476 ILE   A N    1 
ATOM   1792 C  CA   . ILE   A 1 465 ? 23.852  12.959  13.471  1.00 33.98  ? 476 ILE   A CA   1 
ATOM   1793 C  C    . ILE   A 1 465 ? 25.137  13.708  13.148  1.00 35.22  ? 476 ILE   A C    1 
ATOM   1794 O  O    . ILE   A 1 465 ? 25.945  14.003  14.037  1.00 36.39  ? 476 ILE   A O    1 
ATOM   1795 C  CB   . ILE   A 1 465 ? 23.954  11.473  13.101  1.00 30.95  ? 476 ILE   A CB   1 
ATOM   1796 C  CG1  . ILE   A 1 465 ? 22.752  10.717  13.659  1.00 30.42  ? 476 ILE   A CG1  1 
ATOM   1797 C  CG2  . ILE   A 1 465 ? 25.237  10.875  13.634  1.00 31.37  ? 476 ILE   A CG2  1 
ATOM   1798 C  CD1  . ILE   A 1 465 ? 22.625  9.344   13.072  1.00 27.60  ? 476 ILE   A CD1  1 
ATOM   1799 N  N    . ALA   A 1 466 ? 25.342  14.033  11.866  1.00 33.86  ? 477 ALA   A N    1 
ATOM   1800 C  CA   . ALA   A 1 466 ? 26.566  14.716  11.461  1.00 31.95  ? 477 ALA   A CA   1 
ATOM   1801 C  C    . ALA   A 1 466 ? 26.669  16.101  12.090  1.00 42.44  ? 477 ALA   A C    1 
ATOM   1802 O  O    . ALA   A 1 466 ? 27.771  16.556  12.413  1.00 42.80  ? 477 ALA   A O    1 
ATOM   1803 C  CB   . ALA   A 1 466 ? 26.638  14.826  9.936   1.00 37.25  ? 477 ALA   A CB   1 
ATOM   1804 N  N    . THR   A 1 467 ? 25.540  16.773  12.293  1.00 36.78  ? 478 THR   A N    1 
ATOM   1805 C  CA   . THR   A 1 467 ? 25.536  18.162  12.731  1.00 36.55  ? 478 THR   A CA   1 
ATOM   1806 C  C    . THR   A 1 467 ? 25.332  18.324  14.240  1.00 45.80  ? 478 THR   A C    1 
ATOM   1807 O  O    . THR   A 1 467 ? 25.858  19.277  14.820  1.00 49.65  ? 478 THR   A O    1 
ATOM   1808 C  CB   . THR   A 1 467 ? 24.474  18.951  11.953  1.00 42.37  ? 478 THR   A CB   1 
ATOM   1809 O  OG1  . THR   A 1 467 ? 23.193  18.335  12.108  1.00 55.41  ? 478 THR   A OG1  1 
ATOM   1810 C  CG2  . THR   A 1 467 ? 24.804  18.959  10.489  1.00 44.88  ? 478 THR   A CG2  1 
ATOM   1811 N  N    . ASN   A 1 468 ? 24.580  17.435  14.896  1.00 38.69  ? 479 ASN   A N    1 
ATOM   1812 C  CA   . ASN   A 1 468 ? 24.407  17.500  16.348  1.00 44.00  ? 479 ASN   A CA   1 
ATOM   1813 C  C    . ASN   A 1 468 ? 25.522  16.804  17.128  1.00 43.61  ? 479 ASN   A C    1 
ATOM   1814 O  O    . ASN   A 1 468 ? 25.843  17.223  18.244  1.00 46.62  ? 479 ASN   A O    1 
ATOM   1815 C  CB   . ASN   A 1 468 ? 23.065  16.875  16.739  1.00 39.05  ? 479 ASN   A CB   1 
ATOM   1816 C  CG   . ASN   A 1 468 ? 21.888  17.728  16.316  1.00 42.46  ? 479 ASN   A CG   1 
ATOM   1817 O  OD1  . ASN   A 1 468 ? 22.065  18.834  15.820  1.00 45.01  ? 479 ASN   A OD1  1 
ATOM   1818 N  ND2  . ASN   A 1 468 ? 20.679  17.194  16.465  1.00 45.13  ? 479 ASN   A ND2  1 
ATOM   1819 N  N    . GLY   A 1 469 ? 26.087  15.727  16.589  1.00 41.45  ? 480 GLY   A N    1 
ATOM   1820 C  CA   . GLY   A 1 469 ? 27.061  14.939  17.334  1.00 39.52  ? 480 GLY   A CA   1 
ATOM   1821 C  C    . GLY   A 1 469 ? 26.407  14.127  18.444  1.00 35.35  ? 480 GLY   A C    1 
ATOM   1822 O  O    . GLY   A 1 469 ? 25.440  13.402  18.200  1.00 41.64  ? 480 GLY   A O    1 
ATOM   1823 N  N    . THR   A 1 470 ? 26.892  14.274  19.680  1.00 38.59  ? 481 THR   A N    1 
ATOM   1824 C  CA   . THR   A 1 470 ? 26.314  13.513  20.790  1.00 35.67  ? 481 THR   A CA   1 
ATOM   1825 C  C    . THR   A 1 470 ? 24.842  13.896  20.921  1.00 37.46  ? 481 THR   A C    1 
ATOM   1826 O  O    . THR   A 1 470 ? 24.537  15.082  21.123  1.00 35.55  ? 481 THR   A O    1 
ATOM   1827 C  CB   . THR   A 1 470 ? 27.068  13.795  22.098  1.00 43.41  ? 481 THR   A CB   1 
ATOM   1828 O  OG1  . THR   A 1 470 ? 28.441  13.399  21.959  1.00 40.89  ? 481 THR   A OG1  1 
ATOM   1829 C  CG2  . THR   A 1 470 ? 26.449  13.034  23.277  1.00 30.20  ? 481 THR   A CG2  1 
ATOM   1830 N  N    . PRO   A 1 471 ? 23.913  12.943  20.869  1.00 33.93  ? 482 PRO   A N    1 
ATOM   1831 C  CA   . PRO   A 1 471 ? 22.491  13.293  20.955  1.00 32.44  ? 482 PRO   A CA   1 
ATOM   1832 C  C    . PRO   A 1 471 ? 22.081  13.673  22.369  1.00 32.83  ? 482 PRO   A C    1 
ATOM   1833 O  O    . PRO   A 1 471 ? 22.734  13.314  23.349  1.00 34.12  ? 482 PRO   A O    1 
ATOM   1834 C  CB   . PRO   A 1 471 ? 21.792  12.009  20.503  1.00 30.40  ? 482 PRO   A CB   1 
ATOM   1835 C  CG   . PRO   A 1 471 ? 22.716  10.939  20.973  1.00 29.19  ? 482 PRO   A CG   1 
ATOM   1836 C  CD   . PRO   A 1 471 ? 24.116  11.487  20.813  1.00 32.84  ? 482 PRO   A CD   1 
ATOM   1837 N  N    . GLU   A 1 472 ? 21.002  14.453  22.445  1.00 31.87  ? 483 GLU   A N    1 
ATOM   1838 C  CA   . GLU   A 1 472 ? 20.381  14.876  23.695  1.00 33.90  ? 483 GLU   A CA   1 
ATOM   1839 C  C    . GLU   A 1 472 ? 19.323  13.882  24.158  1.00 43.81  ? 483 GLU   A C    1 
ATOM   1840 O  O    . GLU   A 1 472 ? 18.572  13.338  23.342  1.00 36.91  ? 483 GLU   A O    1 
ATOM   1841 C  CB   . GLU   A 1 472 ? 19.732  16.253  23.527  1.00 35.04  ? 483 GLU   A CB   1 
ATOM   1842 C  CG   . GLU   A 1 472 ? 20.658  17.338  23.006  1.00 57.98  ? 483 GLU   A CG   1 
ATOM   1843 C  CD   . GLU   A 1 472 ? 21.590  17.881  24.077  1.00 70.08  ? 483 GLU   A CD   1 
ATOM   1844 O  OE1  . GLU   A 1 472 ? 21.349  17.609  25.273  1.00 79.12  ? 483 GLU   A OE1  1 
ATOM   1845 O  OE2  . GLU   A 1 472 ? 22.552  18.600  23.725  1.00 78.75  ? 483 GLU   A OE2  1 
ATOM   1846 N  N    . LEU   A 1 473 ? 19.316  13.592  25.458  1.00 37.49  ? 484 LEU   A N    1 
ATOM   1847 C  CA   . LEU   A 1 473 ? 18.202  12.881  26.077  1.00 36.31  ? 484 LEU   A CA   1 
ATOM   1848 C  C    . LEU   A 1 473 ? 17.036  13.830  26.322  1.00 39.73  ? 484 LEU   A C    1 
ATOM   1849 O  O    . LEU   A 1 473 ? 17.221  15.035  26.524  1.00 34.98  ? 484 LEU   A O    1 
ATOM   1850 C  CB   . LEU   A 1 473 ? 18.604  12.202  27.394  1.00 33.05  ? 484 LEU   A CB   1 
ATOM   1851 C  CG   . LEU   A 1 473 ? 19.461  10.929  27.341  1.00 43.49  ? 484 LEU   A CG   1 
ATOM   1852 C  CD1  . LEU   A 1 473 ? 18.773  9.904   26.438  1.00 39.78  ? 484 LEU   A CD1  1 
ATOM   1853 C  CD2  . LEU   A 1 473 ? 20.889  11.184  26.877  1.00 52.48  ? 484 LEU   A CD2  1 
ATOM   1854 N  N    . GLN   A 1 474 ? 15.821  13.281  26.254  1.00 38.03  ? 485 GLN   A N    1 
ATOM   1855 C  CA   . GLN   A 1 474 ? 14.636  14.089  26.525  1.00 39.03  ? 485 GLN   A CA   1 
ATOM   1856 C  C    . GLN   A 1 474 ? 14.570  14.512  27.990  1.00 41.80  ? 485 GLN   A C    1 
ATOM   1857 O  O    . GLN   A 1 474 ? 14.194  15.647  28.292  1.00 39.41  ? 485 GLN   A O    1 
ATOM   1858 C  CB   . GLN   A 1 474 ? 13.375  13.312  26.144  1.00 50.42  ? 485 GLN   A CB   1 
ATOM   1859 C  CG   . GLN   A 1 474 ? 13.319  12.899  24.674  1.00 69.94  ? 485 GLN   A CG   1 
ATOM   1860 C  CD   . GLN   A 1 474 ? 11.990  12.268  24.286  1.00 84.06  ? 485 GLN   A CD   1 
ATOM   1861 O  OE1  . GLN   A 1 474 ? 10.930  12.875  24.446  1.00 99.84  ? 485 GLN   A OE1  1 
ATOM   1862 N  NE2  . GLN   A 1 474 ? 12.043  11.038  23.779  1.00 67.92  ? 485 GLN   A NE2  1 
ATOM   1863 N  N    . ASN   A 1 475 ? 14.936  13.622  28.915  1.00 42.52  ? 486 ASN   A N    1 
ATOM   1864 C  CA   . ASN   A 1 475 ? 14.855  13.904  30.354  1.00 46.16  ? 486 ASN   A CA   1 
ATOM   1865 C  C    . ASN   A 1 475 ? 16.077  13.340  31.063  1.00 36.05  ? 486 ASN   A C    1 
ATOM   1866 O  O    . ASN   A 1 475 ? 15.994  12.333  31.778  1.00 36.96  ? 486 ASN   A O    1 
ATOM   1867 C  CB   . ASN   A 1 475 ? 13.575  13.321  30.962  1.00 48.97  ? 486 ASN   A CB   1 
ATOM   1868 C  CG   . ASN   A 1 475 ? 12.313  13.966  30.424  1.00 47.28  ? 486 ASN   A CG   1 
ATOM   1869 O  OD1  . ASN   A 1 475 ? 11.686  13.449  29.501  1.00 56.08  ? 486 ASN   A OD1  1 
ATOM   1870 N  ND2  . ASN   A 1 475 ? 11.929  15.093  31.011  1.00 45.30  ? 486 ASN   A ND2  1 
ATOM   1871 N  N    . PRO   A 1 476 ? 17.235  13.977  30.899  1.00 33.34  ? 487 PRO   A N    1 
ATOM   1872 C  CA   . PRO   A 1 476 ? 18.458  13.427  31.502  1.00 37.86  ? 487 PRO   A CA   1 
ATOM   1873 C  C    . PRO   A 1 476 ? 18.412  13.400  33.014  1.00 43.33  ? 487 PRO   A C    1 
ATOM   1874 O  O    . PRO   A 1 476 ? 19.082  12.557  33.634  1.00 34.70  ? 487 PRO   A O    1 
ATOM   1875 C  CB   . PRO   A 1 476 ? 19.554  14.365  30.981  1.00 34.12  ? 487 PRO   A CB   1 
ATOM   1876 C  CG   . PRO   A 1 476 ? 18.836  15.644  30.685  1.00 37.84  ? 487 PRO   A CG   1 
ATOM   1877 C  CD   . PRO   A 1 476 ? 17.479  15.249  30.199  1.00 40.11  ? 487 PRO   A CD   1 
ATOM   1878 N  N    . GLU   A 1 477 ? 17.595  14.264  33.621  1.00 29.40  ? 488 GLU   A N    1 
ATOM   1879 C  CA   . GLU   A 1 477 ? 17.488  14.324  35.069  1.00 39.52  ? 488 GLU   A CA   1 
ATOM   1880 C  C    . GLU   A 1 477 ? 16.915  13.040  35.649  1.00 35.24  ? 488 GLU   A C    1 
ATOM   1881 O  O    . GLU   A 1 477 ? 17.100  12.782  36.840  1.00 43.13  ? 488 GLU   A O    1 
ATOM   1882 C  CB   . GLU   A 1 477 ? 16.651  15.542  35.480  1.00 40.91  ? 488 GLU   A CB   1 
ATOM   1883 C  CG   . GLU   A 1 477 ? 15.166  15.458  35.166  1.00 45.45  ? 488 GLU   A CG   1 
ATOM   1884 C  CD   . GLU   A 1 477 ? 14.842  15.728  33.704  1.00 48.08  ? 488 GLU   A CD   1 
ATOM   1885 O  OE1  . GLU   A 1 477 ? 15.760  16.103  32.942  1.00 44.29  ? 488 GLU   A OE1  1 
ATOM   1886 O  OE2  . GLU   A 1 477 ? 13.658  15.603  33.325  1.00 48.99  ? 488 GLU   A OE2  1 
ATOM   1887 N  N    . LYS   A 1 478 ? 16.249  12.215  34.837  1.00 28.59  ? 489 LYS   A N    1 
ATOM   1888 C  CA   . LYS   A 1 478 ? 15.722  10.943  35.327  1.00 31.85  ? 489 LYS   A CA   1 
ATOM   1889 C  C    . LYS   A 1 478 ? 16.782  9.852   35.450  1.00 35.15  ? 489 LYS   A C    1 
ATOM   1890 O  O    . LYS   A 1 478 ? 16.470  8.767   35.948  1.00 35.06  ? 489 LYS   A O    1 
ATOM   1891 C  CB   . LYS   A 1 478 ? 14.625  10.424  34.406  1.00 34.83  ? 489 LYS   A CB   1 
ATOM   1892 C  CG   . LYS   A 1 478 ? 13.432  11.331  34.216  1.00 42.29  ? 489 LYS   A CG   1 
ATOM   1893 C  CD   . LYS   A 1 478 ? 12.350  10.495  33.533  1.00 42.46  ? 489 LYS   A CD   1 
ATOM   1894 C  CE   . LYS   A 1 478 ? 11.025  11.223  33.389  1.00 54.82  ? 489 LYS   A CE   1 
ATOM   1895 N  NZ   . LYS   A 1 478 ? 9.991   10.231  32.965  1.00 52.24  ? 489 LYS   A NZ   1 
ATOM   1896 N  N    . LEU   A 1 479 ? 18.014  10.101  35.018  1.00 34.16  ? 490 LEU   A N    1 
ATOM   1897 C  CA   . LEU   A 1 479 ? 19.071  9.100   35.015  1.00 31.17  ? 490 LEU   A CA   1 
ATOM   1898 C  C    . LEU   A 1 479 ? 20.000  9.273   36.214  1.00 33.40  ? 490 LEU   A C    1 
ATOM   1899 O  O    . LEU   A 1 479 ? 20.284  10.392  36.643  1.00 33.15  ? 490 LEU   A O    1 
ATOM   1900 C  CB   . LEU   A 1 479 ? 19.891  9.209   33.728  1.00 28.74  ? 490 LEU   A CB   1 
ATOM   1901 C  CG   . LEU   A 1 479 ? 19.213  8.873   32.398  1.00 32.63  ? 490 LEU   A CG   1 
ATOM   1902 C  CD1  . LEU   A 1 479 ? 20.273  8.454   31.410  1.00 34.07  ? 490 LEU   A CD1  1 
ATOM   1903 C  CD2  . LEU   A 1 479 ? 18.150  7.810   32.531  1.00 43.39  ? 490 LEU   A CD2  1 
ATOM   1904 N  N    . SER   A 1 480 ? 20.496  8.160   36.744  1.00 29.33  ? 491 SER   A N    1 
ATOM   1905 C  CA   . SER   A 1 480 ? 21.489  8.279   37.802  1.00 28.11  ? 491 SER   A CA   1 
ATOM   1906 C  C    . SER   A 1 480 ? 22.758  8.927   37.256  1.00 32.31  ? 491 SER   A C    1 
ATOM   1907 O  O    . SER   A 1 480 ? 23.047  8.869   36.056  1.00 33.58  ? 491 SER   A O    1 
ATOM   1908 C  CB   . SER   A 1 480 ? 21.837  6.909   38.370  1.00 27.70  ? 491 SER   A CB   1 
ATOM   1909 O  OG   . SER   A 1 480 ? 22.526  6.136   37.404  1.00 29.64  ? 491 SER   A OG   1 
ATOM   1910 N  N    . ALA   A 1 481 ? 23.545  9.503   38.167  1.00 30.93  ? 492 ALA   A N    1 
ATOM   1911 C  CA   . ALA   A 1 481 ? 24.809  10.104  37.765  1.00 32.51  ? 492 ALA   A CA   1 
ATOM   1912 C  C    . ALA   A 1 481 ? 25.694  9.084   37.063  1.00 33.96  ? 492 ALA   A C    1 
ATOM   1913 O  O    . ALA   A 1 481 ? 26.296  9.391   36.028  1.00 29.30  ? 492 ALA   A O    1 
ATOM   1914 C  CB   . ALA   A 1 481 ? 25.524  10.710  38.975  1.00 33.75  ? 492 ALA   A CB   1 
ATOM   1915 N  N    . ILE   A 1 482 ? 25.761  7.853   37.585  1.00 31.85  ? 493 ILE   A N    1 
ATOM   1916 C  CA   . ILE   A 1 482 ? 26.673  6.868   36.992  1.00 29.73  ? 493 ILE   A CA   1 
ATOM   1917 C  C    . ILE   A 1 482 ? 26.176  6.411   35.624  1.00 28.46  ? 493 ILE   A C    1 
ATOM   1918 O  O    . ILE   A 1 482 ? 26.980  6.146   34.719  1.00 30.28  ? 493 ILE   A O    1 
ATOM   1919 C  CB   . ILE   A 1 482 ? 26.893  5.668   37.937  1.00 34.23  ? 493 ILE   A CB   1 
ATOM   1920 C  CG1  . ILE   A 1 482 ? 25.560  5.006   38.288  1.00 39.32  ? 493 ILE   A CG1  1 
ATOM   1921 C  CG2  . ILE   A 1 482 ? 27.648  6.105   39.181  1.00 42.40  ? 493 ILE   A CG2  1 
ATOM   1922 C  CD1  . ILE   A 1 482 ? 25.710  3.691   39.017  1.00 46.71  ? 493 ILE   A CD1  1 
ATOM   1923 N  N    . PHE   A 1 483 ? 24.854  6.295   35.442  1.00 26.90  ? 494 PHE   A N    1 
ATOM   1924 C  CA   . PHE   A 1 483 ? 24.325  5.937   34.124  1.00 28.76  ? 494 PHE   A CA   1 
ATOM   1925 C  C    . PHE   A 1 483 ? 24.622  7.038   33.106  1.00 30.26  ? 494 PHE   A C    1 
ATOM   1926 O  O    . PHE   A 1 483 ? 25.042  6.758   31.973  1.00 24.46  ? 494 PHE   A O    1 
ATOM   1927 C  CB   . PHE   A 1 483 ? 22.815  5.646   34.219  1.00 28.84  ? 494 PHE   A CB   1 
ATOM   1928 C  CG   . PHE   A 1 483 ? 22.196  5.046   32.961  1.00 34.27  ? 494 PHE   A CG   1 
ATOM   1929 C  CD1  . PHE   A 1 483 ? 22.978  4.514   31.940  1.00 29.47  ? 494 PHE   A CD1  1 
ATOM   1930 C  CD2  . PHE   A 1 483 ? 20.818  5.004   32.817  1.00 30.07  ? 494 PHE   A CD2  1 
ATOM   1931 C  CE1  . PHE   A 1 483 ? 22.394  3.953   30.796  1.00 28.72  ? 494 PHE   A CE1  1 
ATOM   1932 C  CE2  . PHE   A 1 483 ? 20.231  4.465   31.684  1.00 26.12  ? 494 PHE   A CE2  1 
ATOM   1933 C  CZ   . PHE   A 1 483 ? 21.027  3.941   30.659  1.00 24.55  ? 494 PHE   A CZ   1 
ATOM   1934 N  N    . ARG   A 1 484 ? 24.426  8.299   33.492  1.00 29.02  ? 495 ARG   A N    1 
ATOM   1935 C  CA   . ARG   A 1 484 ? 24.733  9.380   32.563  1.00 29.23  ? 495 ARG   A CA   1 
ATOM   1936 C  C    . ARG   A 1 484 ? 26.203  9.348   32.160  1.00 28.87  ? 495 ARG   A C    1 
ATOM   1937 O  O    . ARG   A 1 484 ? 26.545  9.618   31.005  1.00 26.36  ? 495 ARG   A O    1 
ATOM   1938 C  CB   . ARG   A 1 484 ? 24.397  10.737  33.183  1.00 30.54  ? 495 ARG   A CB   1 
ATOM   1939 C  CG   . ARG   A 1 484 ? 22.908  11.034  33.305  1.00 38.24  ? 495 ARG   A CG   1 
ATOM   1940 C  CD   . ARG   A 1 484 ? 22.680  12.535  33.582  1.00 34.25  ? 495 ARG   A CD   1 
ATOM   1941 N  NE   . ARG   A 1 484 ? 23.320  12.983  34.812  1.00 49.34  ? 495 ARG   A NE   1 
ATOM   1942 C  CZ   . ARG   A 1 484 ? 22.795  12.895  36.027  1.00 52.49  ? 495 ARG   A CZ   1 
ATOM   1943 N  NH1  . ARG   A 1 484 ? 21.599  12.372  36.227  1.00 51.73  ? 495 ARG   A NH1  1 
ATOM   1944 N  NH2  . ARG   A 1 484 ? 23.491  13.346  37.067  1.00 53.70  ? 495 ARG   A NH2  1 
ATOM   1945 N  N    . ASP   A 1 485 ? 27.090  9.039   33.106  1.00 28.77  ? 496 ASP   A N    1 
ATOM   1946 C  CA   . ASP   A 1 485 ? 28.512  9.003   32.781  1.00 32.87  ? 496 ASP   A CA   1 
ATOM   1947 C  C    . ASP   A 1 485 ? 28.804  7.873   31.805  1.00 35.05  ? 496 ASP   A C    1 
ATOM   1948 O  O    . ASP   A 1 485 ? 29.559  8.053   30.841  1.00 30.37  ? 496 ASP   A O    1 
ATOM   1949 C  CB   . ASP   A 1 485 ? 29.334  8.851   34.060  1.00 28.92  ? 496 ASP   A CB   1 
ATOM   1950 C  CG   . ASP   A 1 485 ? 30.826  8.979   33.821  1.00 43.22  ? 496 ASP   A CG   1 
ATOM   1951 O  OD1  . ASP   A 1 485 ? 31.315  10.127  33.763  1.00 45.63  ? 496 ASP   A OD1  1 
ATOM   1952 O  OD2  . ASP   A 1 485 ? 31.510  7.939   33.694  1.00 41.59  ? 496 ASP   A OD2  1 
ATOM   1953 N  N    . PHE   A 1 486 ? 28.197  6.707   32.039  1.00 27.20  ? 497 PHE   A N    1 
ATOM   1954 C  CA   . PHE   A 1 486 ? 28.323  5.586   31.112  1.00 28.35  ? 497 PHE   A CA   1 
ATOM   1955 C  C    . PHE   A 1 486 ? 27.865  5.971   29.708  1.00 28.18  ? 497 PHE   A C    1 
ATOM   1956 O  O    . PHE   A 1 486 ? 28.550  5.685   28.724  1.00 27.73  ? 497 PHE   A O    1 
ATOM   1957 C  CB   . PHE   A 1 486 ? 27.523  4.391   31.632  1.00 26.87  ? 497 PHE   A CB   1 
ATOM   1958 C  CG   . PHE   A 1 486 ? 27.551  3.191   30.715  1.00 23.51  ? 497 PHE   A CG   1 
ATOM   1959 C  CD1  . PHE   A 1 486 ? 28.588  2.269   30.783  1.00 27.54  ? 497 PHE   A CD1  1 
ATOM   1960 C  CD2  . PHE   A 1 486 ? 26.556  2.993   29.791  1.00 22.31  ? 497 PHE   A CD2  1 
ATOM   1961 C  CE1  . PHE   A 1 486 ? 28.612  1.159   29.948  1.00 25.43  ? 497 PHE   A CE1  1 
ATOM   1962 C  CE2  . PHE   A 1 486 ? 26.583  1.886   28.945  1.00 25.98  ? 497 PHE   A CE2  1 
ATOM   1963 C  CZ   . PHE   A 1 486 ? 27.610  0.970   29.038  1.00 25.97  ? 497 PHE   A CZ   1 
ATOM   1964 N  N    . LEU   A 1 487 ? 26.700  6.616   29.596  1.00 27.57  ? 498 LEU   A N    1 
ATOM   1965 C  CA   . LEU   A 1 487 ? 26.238  7.081   28.294  1.00 30.96  ? 498 LEU   A CA   1 
ATOM   1966 C  C    . LEU   A 1 487 ? 27.220  8.059   27.660  1.00 30.72  ? 498 LEU   A C    1 
ATOM   1967 O  O    . LEU   A 1 487 ? 27.519  7.959   26.465  1.00 29.09  ? 498 LEU   A O    1 
ATOM   1968 C  CB   . LEU   A 1 487 ? 24.863  7.734   28.398  1.00 27.85  ? 498 LEU   A CB   1 
ATOM   1969 C  CG   . LEU   A 1 487 ? 23.606  6.894   28.540  1.00 37.80  ? 498 LEU   A CG   1 
ATOM   1970 C  CD1  . LEU   A 1 487 ? 22.403  7.828   28.584  1.00 40.82  ? 498 LEU   A CD1  1 
ATOM   1971 C  CD2  . LEU   A 1 487 ? 23.493  5.958   27.344  1.00 34.96  ? 498 LEU   A CD2  1 
ATOM   1972 N  N    . ASN   A 1 488 ? 27.705  9.030   28.436  1.00 27.60  ? 499 ASN   A N    1 
ATOM   1973 C  CA   . ASN   A 1 488 ? 28.631  10.016  27.883  1.00 31.30  ? 499 ASN   A CA   1 
ATOM   1974 C  C    . ASN   A 1 488 ? 29.871  9.347   27.304  1.00 33.78  ? 499 ASN   A C    1 
ATOM   1975 O  O    . ASN   A 1 488 ? 30.369  9.746   26.242  1.00 31.97  ? 499 ASN   A O    1 
ATOM   1976 C  CB   . ASN   A 1 488 ? 29.036  11.019  28.959  1.00 30.63  ? 499 ASN   A CB   1 
ATOM   1977 C  CG   . ASN   A 1 488 ? 27.898  11.950  29.359  1.00 41.28  ? 499 ASN   A CG   1 
ATOM   1978 O  OD1  . ASN   A 1 488 ? 26.956  12.176  28.598  1.00 55.64  ? 499 ASN   A OD1  1 
ATOM   1979 N  ND2  . ASN   A 1 488 ? 28.010  12.530  30.539  1.00 39.45  ? 499 ASN   A ND2  1 
ATOM   1980 N  N    . ARG   A 1 489 ? 30.383  8.323   27.992  1.00 28.47  ? 500 ARG   A N    1 
ATOM   1981 C  CA   . ARG   A 1 489 ? 31.577  7.627   27.521  1.00 28.52  ? 500 ARG   A CA   1 
ATOM   1982 C  C    . ARG   A 1 489 ? 31.310  6.791   26.277  1.00 32.76  ? 500 ARG   A C    1 
ATOM   1983 O  O    . ARG   A 1 489 ? 32.230  6.595   25.470  1.00 32.15  ? 500 ARG   A O    1 
ATOM   1984 C  CB   . ARG   A 1 489 ? 32.153  6.757   28.634  1.00 25.39  ? 500 ARG   A CB   1 
ATOM   1985 C  CG   . ARG   A 1 489 ? 32.618  7.590   29.819  1.00 32.90  ? 500 ARG   A CG   1 
ATOM   1986 C  CD   . ARG   A 1 489 ? 33.350  6.759   30.854  1.00 51.69  ? 500 ARG   A CD   1 
ATOM   1987 N  NE   . ARG   A 1 489 ? 34.777  7.055   30.864  1.00 73.83  ? 500 ARG   A NE   1 
ATOM   1988 C  CZ   . ARG   A 1 489 ? 35.338  8.003   31.602  1.00 70.07  ? 500 ARG   A CZ   1 
ATOM   1989 N  NH1  . ARG   A 1 489 ? 34.622  8.752   32.425  1.00 71.96  ? 500 ARG   A NH1  1 
ATOM   1990 N  NH2  . ARG   A 1 489 ? 36.650  8.202   31.514  1.00 76.72  ? 500 ARG   A NH2  1 
ATOM   1991 N  N    . CYS   A 1 490 ? 30.083  6.272   26.108  1.00 25.79  ? 501 CYS   A N    1 
ATOM   1992 C  CA   . CYS   A 1 490 ? 29.749  5.561   24.873  1.00 28.64  ? 501 CYS   A CA   1 
ATOM   1993 C  C    . CYS   A 1 490 ? 29.542  6.516   23.711  1.00 30.11  ? 501 CYS   A C    1 
ATOM   1994 O  O    . CYS   A 1 490 ? 29.853  6.163   22.572  1.00 26.37  ? 501 CYS   A O    1 
ATOM   1995 C  CB   . CYS   A 1 490 ? 28.471  4.717   25.023  1.00 25.48  ? 501 CYS   A CB   1 
ATOM   1996 S  SG   . CYS   A 1 490 ? 28.515  3.308   26.140  1.00 27.30  ? 501 CYS   A SG   1 
ATOM   1997 N  N    . LEU   A 1 491 ? 29.006  7.712   23.971  1.00 28.07  ? 502 LEU   A N    1 
ATOM   1998 C  CA   . LEU   A 1 491 ? 28.590  8.617   22.910  1.00 30.89  ? 502 LEU   A CA   1 
ATOM   1999 C  C    . LEU   A 1 491 ? 29.530  9.809   22.762  1.00 32.51  ? 502 LEU   A C    1 
ATOM   2000 O  O    . LEU   A 1 491 ? 29.135  10.851  22.228  1.00 29.80  ? 502 LEU   A O    1 
ATOM   2001 C  CB   . LEU   A 1 491 ? 27.157  9.082   23.166  1.00 25.26  ? 502 LEU   A CB   1 
ATOM   2002 C  CG   . LEU   A 1 491 ? 26.155  7.931   23.104  1.00 29.50  ? 502 LEU   A CG   1 
ATOM   2003 C  CD1  . LEU   A 1 491 ? 24.793  8.370   23.615  1.00 33.67  ? 502 LEU   A CD1  1 
ATOM   2004 C  CD2  . LEU   A 1 491 ? 26.051  7.337   21.676  1.00 24.59  ? 502 LEU   A CD2  1 
ATOM   2005 N  N    . GLU   A 1 492 ? 30.782  9.648   23.175  1.00 29.67  ? 503 GLU   A N    1 
ATOM   2006 C  CA   . GLU   A 1 492 ? 31.782  10.702  23.059  1.00 29.51  ? 503 GLU   A CA   1 
ATOM   2007 C  C    . GLU   A 1 492 ? 32.151  10.953  21.592  1.00 33.69  ? 503 GLU   A C    1 
ATOM   2008 O  O    . GLU   A 1 492 ? 32.361  10.011  20.817  1.00 33.01  ? 503 GLU   A O    1 
ATOM   2009 C  CB   . GLU   A 1 492 ? 33.000  10.309  23.896  1.00 35.22  ? 503 GLU   A CB   1 
ATOM   2010 C  CG   . GLU   A 1 492 ? 34.219  11.177  23.752  1.00 45.21  ? 503 GLU   A CG   1 
ATOM   2011 C  CD   . GLU   A 1 492 ? 33.948  12.646  23.977  1.00 53.69  ? 503 GLU   A CD   1 
ATOM   2012 O  OE1  . GLU   A 1 492 ? 33.468  13.016  25.076  1.00 49.90  ? 503 GLU   A OE1  1 
ATOM   2013 O  OE2  . GLU   A 1 492 ? 34.224  13.426  23.040  1.00 45.66  ? 503 GLU   A OE2  1 
ATOM   2014 N  N    . MET   A 1 493 ? 32.198  12.231  21.204  1.00 32.55  ? 504 MET   A N    1 
ATOM   2015 C  CA   . MET   A 1 493 ? 32.566  12.579  19.833  1.00 33.98  ? 504 MET   A CA   1 
ATOM   2016 C  C    . MET   A 1 493 ? 34.028  12.262  19.549  1.00 42.83  ? 504 MET   A C    1 
ATOM   2017 O  O    . MET   A 1 493 ? 34.374  11.813  18.449  1.00 40.95  ? 504 MET   A O    1 
ATOM   2018 C  CB   . MET   A 1 493 ? 32.311  14.067  19.583  1.00 43.28  ? 504 MET   A CB   1 
ATOM   2019 C  CG   . MET   A 1 493 ? 30.854  14.451  19.514  1.00 46.04  ? 504 MET   A CG   1 
ATOM   2020 S  SD   . MET   A 1 493 ? 30.081  13.669  18.096  1.00 50.45  ? 504 MET   A SD   1 
ATOM   2021 C  CE   . MET   A 1 493 ? 31.094  14.310  16.762  1.00 36.96  ? 504 MET   A CE   1 
ATOM   2022 N  N    . ASP   A 1 494 ? 34.898  12.510  20.519  1.00 36.72  ? 505 ASP   A N    1 
ATOM   2023 C  CA   . ASP   A 1 494 ? 36.318  12.229  20.381  1.00 41.10  ? 505 ASP   A CA   1 
ATOM   2024 C  C    . ASP   A 1 494 ? 36.527  10.728  20.492  1.00 39.18  ? 505 ASP   A C    1 
ATOM   2025 O  O    . ASP   A 1 494 ? 36.382  10.156  21.577  1.00 38.52  ? 505 ASP   A O    1 
ATOM   2026 C  CB   . ASP   A 1 494 ? 37.091  12.985  21.458  1.00 42.20  ? 505 ASP   A CB   1 
ATOM   2027 C  CG   . ASP   A 1 494 ? 38.595  12.926  21.260  1.00 50.40  ? 505 ASP   A CG   1 
ATOM   2028 O  OD1  . ASP   A 1 494 ? 39.104  11.899  20.767  1.00 49.32  ? 505 ASP   A OD1  1 
ATOM   2029 O  OD2  . ASP   A 1 494 ? 39.274  13.917  21.609  1.00 54.45  ? 505 ASP   A OD2  1 
ATOM   2030 N  N    . VAL   A 1 495 ? 36.877  10.090  19.372  1.00 37.22  ? 506 VAL   A N    1 
ATOM   2031 C  CA   . VAL   A 1 495 ? 37.023  8.634   19.348  1.00 38.38  ? 506 VAL   A CA   1 
ATOM   2032 C  C    . VAL   A 1 495 ? 38.083  8.183   20.346  1.00 39.17  ? 506 VAL   A C    1 
ATOM   2033 O  O    . VAL   A 1 495 ? 37.950  7.129   20.982  1.00 38.29  ? 506 VAL   A O    1 
ATOM   2034 C  CB   . VAL   A 1 495 ? 37.330  8.155   17.916  1.00 35.52  ? 506 VAL   A CB   1 
ATOM   2035 C  CG1  . VAL   A 1 495 ? 37.622  6.662   17.897  1.00 38.99  ? 506 VAL   A CG1  1 
ATOM   2036 C  CG2  . VAL   A 1 495 ? 36.140  8.467   17.014  1.00 36.70  ? 506 VAL   A CG2  1 
ATOM   2037 N  N    . GLU   A 1 496 ? 39.150  8.974   20.505  1.00 37.36  ? 507 GLU   A N    1 
ATOM   2038 C  CA   . GLU   A 1 496 ? 40.176  8.654   21.493  1.00 36.81  ? 507 GLU   A CA   1 
ATOM   2039 C  C    . GLU   A 1 496 ? 39.603  8.639   22.904  1.00 44.82  ? 507 GLU   A C    1 
ATOM   2040 O  O    . GLU   A 1 496 ? 40.001  7.814   23.735  1.00 47.45  ? 507 GLU   A O    1 
ATOM   2041 C  CB   . GLU   A 1 496 ? 41.319  9.666   21.405  1.00 47.52  ? 507 GLU   A CB   1 
ATOM   2042 C  CG   . GLU   A 1 496 ? 42.533  9.337   22.267  1.00 62.82  ? 507 GLU   A CG   1 
ATOM   2043 C  CD   . GLU   A 1 496 ? 43.336  8.150   21.773  1.00 80.16  ? 507 GLU   A CD   1 
ATOM   2044 O  OE1  . GLU   A 1 496 ? 43.068  7.657   20.652  1.00 67.27  ? 507 GLU   A OE1  1 
ATOM   2045 O  OE2  . GLU   A 1 496 ? 44.247  7.717   22.516  1.00 78.67  ? 507 GLU   A OE2  1 
ATOM   2046 N  N    . LYS   A 1 497 ? 38.669  9.545   23.194  1.00 40.04  ? 508 LYS   A N    1 
ATOM   2047 C  CA   . LYS   A 1 497 ? 38.081  9.615   24.527  1.00 45.67  ? 508 LYS   A CA   1 
ATOM   2048 C  C    . LYS   A 1 497 ? 36.960  8.612   24.725  1.00 37.74  ? 508 LYS   A C    1 
ATOM   2049 O  O    . LYS   A 1 497 ? 36.670  8.259   25.873  1.00 37.12  ? 508 LYS   A O    1 
ATOM   2050 C  CB   . LYS   A 1 497 ? 37.573  11.028  24.813  1.00 40.56  ? 508 LYS   A CB   1 
ATOM   2051 C  CG   . LYS   A 1 497 ? 38.682  12.018  25.098  1.00 49.76  ? 508 LYS   A CG   1 
ATOM   2052 C  CD   . LYS   A 1 497 ? 38.137  13.409  25.379  1.00 57.77  ? 508 LYS   A CD   1 
ATOM   2053 C  CE   . LYS   A 1 497 ? 39.258  14.362  25.770  1.00 64.21  ? 508 LYS   A CE   1 
ATOM   2054 N  NZ   . LYS   A 1 497 ? 38.736  15.702  26.139  1.00 71.57  ? 508 LYS   A NZ   1 
ATOM   2055 N  N    . ARG   A 1 498 ? 36.313  8.173   23.643  1.00 32.65  ? 509 ARG   A N    1 
ATOM   2056 C  CA   . ARG   A 1 498 ? 35.230  7.205   23.748  1.00 32.57  ? 509 ARG   A CA   1 
ATOM   2057 C  C    . ARG   A 1 498 ? 35.775  5.913   24.336  1.00 34.96  ? 509 ARG   A C    1 
ATOM   2058 O  O    . ARG   A 1 498 ? 36.919  5.537   24.078  1.00 36.32  ? 509 ARG   A O    1 
ATOM   2059 C  CB   . ARG   A 1 498 ? 34.610  6.955   22.365  1.00 28.69  ? 509 ARG   A CB   1 
ATOM   2060 C  CG   . ARG   A 1 498 ? 33.255  6.247   22.375  1.00 30.60  ? 509 ARG   A CG   1 
ATOM   2061 C  CD   . ARG   A 1 498 ? 32.701  6.027   20.958  1.00 30.16  ? 509 ARG   A CD   1 
ATOM   2062 N  NE   . ARG   A 1 498 ? 32.585  7.272   20.204  1.00 26.90  ? 509 ARG   A NE   1 
ATOM   2063 C  CZ   . ARG   A 1 498 ? 32.600  7.351   18.878  1.00 36.11  ? 509 ARG   A CZ   1 
ATOM   2064 N  NH1  . ARG   A 1 498 ? 32.669  6.265   18.124  1.00 27.77  ? 509 ARG   A NH1  1 
ATOM   2065 N  NH2  . ARG   A 1 498 ? 32.555  8.551   18.293  1.00 28.94  ? 509 ARG   A NH2  1 
ATOM   2066 N  N    . GLY   A 1 499 ? 34.967  5.249   25.158  1.00 29.48  ? 510 GLY   A N    1 
ATOM   2067 C  CA   . GLY   A 1 499 ? 35.430  4.035   25.806  1.00 31.34  ? 510 GLY   A CA   1 
ATOM   2068 C  C    . GLY   A 1 499 ? 35.599  2.879   24.834  1.00 27.11  ? 510 GLY   A C    1 
ATOM   2069 O  O    . GLY   A 1 499 ? 34.840  2.720   23.877  1.00 30.81  ? 510 GLY   A O    1 
ATOM   2070 N  N    . SER   A 1 500 ? 36.607  2.055   25.094  1.00 29.30  ? 511 SER   A N    1 
ATOM   2071 C  CA   . SER   A 1 500 ? 36.655  0.759   24.437  1.00 34.91  ? 511 SER   A CA   1 
ATOM   2072 C  C    . SER   A 1 500 ? 35.728  -0.208  25.166  1.00 32.48  ? 511 SER   A C    1 
ATOM   2073 O  O    . SER   A 1 500 ? 35.307  0.035   26.302  1.00 31.42  ? 511 SER   A O    1 
ATOM   2074 C  CB   . SER   A 1 500 ? 38.082  0.210   24.421  1.00 28.97  ? 511 SER   A CB   1 
ATOM   2075 O  OG   . SER   A 1 500 ? 38.491  -0.118  25.737  1.00 33.68  ? 511 SER   A OG   1 
ATOM   2076 N  N    . ALA   A 1 501 ? 35.428  -1.335  24.518  1.00 31.89  ? 512 ALA   A N    1 
ATOM   2077 C  CA   . ALA   A 1 501 ? 34.610  -2.334  25.199  1.00 31.26  ? 512 ALA   A CA   1 
ATOM   2078 C  C    . ALA   A 1 501 ? 35.304  -2.829  26.457  1.00 30.69  ? 512 ALA   A C    1 
ATOM   2079 O  O    . ALA   A 1 501 ? 34.669  -2.987  27.506  1.00 29.44  ? 512 ALA   A O    1 
ATOM   2080 C  CB   . ALA   A 1 501 ? 34.296  -3.500  24.266  1.00 29.59  ? 512 ALA   A CB   1 
ATOM   2081 N  N    . LYS   A 1 502 ? 36.611  -3.084  26.371  1.00 31.73  ? 513 LYS   A N    1 
ATOM   2082 C  CA   . LYS   A 1 502 ? 37.342  -3.545  27.545  1.00 37.77  ? 513 LYS   A CA   1 
ATOM   2083 C  C    . LYS   A 1 502 ? 37.261  -2.524  28.673  1.00 40.20  ? 513 LYS   A C    1 
ATOM   2084 O  O    . LYS   A 1 502 ? 37.082  -2.890  29.841  1.00 34.43  ? 513 LYS   A O    1 
ATOM   2085 C  CB   . LYS   A 1 502 ? 38.794  -3.838  27.169  1.00 35.89  ? 513 LYS   A CB   1 
ATOM   2086 C  CG   . LYS   A 1 502 ? 39.631  -4.414  28.290  1.00 36.25  ? 513 LYS   A CG   1 
ATOM   2087 C  CD   . LYS   A 1 502 ? 41.035  -4.744  27.790  1.00 49.27  ? 513 LYS   A CD   1 
ATOM   2088 C  CE   . LYS   A 1 502 ? 41.921  -5.252  28.921  1.00 54.80  ? 513 LYS   A CE   1 
ATOM   2089 N  NZ   . LYS   A 1 502 ? 43.326  -5.456  28.460  1.00 71.71  ? 513 LYS   A NZ   1 
ATOM   2090 N  N    . GLU   A 1 503 ? 37.370  -1.235  28.339  1.00 35.62  ? 514 GLU   A N    1 
ATOM   2091 C  CA   . GLU   A 1 503 ? 37.301  -0.194  29.358  1.00 36.73  ? 514 GLU   A CA   1 
ATOM   2092 C  C    . GLU   A 1 503 ? 35.906  -0.107  29.967  1.00 33.51  ? 514 GLU   A C    1 
ATOM   2093 O  O    . GLU   A 1 503 ? 35.758  -0.023  31.195  1.00 33.30  ? 514 GLU   A O    1 
ATOM   2094 C  CB   . GLU   A 1 503 ? 37.704  1.156   28.764  1.00 31.43  ? 514 GLU   A CB   1 
ATOM   2095 C  CG   . GLU   A 1 503 ? 39.196  1.314   28.519  1.00 39.00  ? 514 GLU   A CG   1 
ATOM   2096 C  CD   . GLU   A 1 503 ? 39.522  2.535   27.672  1.00 45.36  ? 514 GLU   A CD   1 
ATOM   2097 O  OE1  . GLU   A 1 503 ? 38.577  3.193   27.187  1.00 40.14  ? 514 GLU   A OE1  1 
ATOM   2098 O  OE2  . GLU   A 1 503 ? 40.723  2.830   27.491  1.00 48.78  ? 514 GLU   A OE2  1 
ATOM   2099 N  N    . LEU   A 1 504 ? 34.871  -0.125  29.127  1.00 30.85  ? 515 LEU   A N    1 
ATOM   2100 C  CA   . LEU   A 1 504 ? 33.509  0.057   29.618  1.00 29.11  ? 515 LEU   A CA   1 
ATOM   2101 C  C    . LEU   A 1 504 ? 33.021  -1.126  30.444  1.00 32.23  ? 515 LEU   A C    1 
ATOM   2102 O  O    . LEU   A 1 504 ? 32.108  -0.957  31.256  1.00 30.25  ? 515 LEU   A O    1 
ATOM   2103 C  CB   . LEU   A 1 504 ? 32.569  0.330   28.442  1.00 29.03  ? 515 LEU   A CB   1 
ATOM   2104 C  CG   . LEU   A 1 504 ? 32.783  1.736   27.873  1.00 29.80  ? 515 LEU   A CG   1 
ATOM   2105 C  CD1  . LEU   A 1 504 ? 32.062  1.915   26.544  1.00 27.72  ? 515 LEU   A CD1  1 
ATOM   2106 C  CD2  . LEU   A 1 504 ? 32.336  2.791   28.878  1.00 31.35  ? 515 LEU   A CD2  1 
ATOM   2107 N  N    . LEU   A 1 505 ? 33.610  -2.313  30.269  1.00 30.44  ? 516 LEU   A N    1 
ATOM   2108 C  CA   . LEU   A 1 505 ? 33.269  -3.444  31.130  1.00 31.01  ? 516 LEU   A CA   1 
ATOM   2109 C  C    . LEU   A 1 505 ? 33.673  -3.217  32.584  1.00 38.89  ? 516 LEU   A C    1 
ATOM   2110 O  O    . LEU   A 1 505 ? 33.206  -3.949  33.462  1.00 34.05  ? 516 LEU   A O    1 
ATOM   2111 C  CB   . LEU   A 1 505 ? 33.925  -4.725  30.611  1.00 31.51  ? 516 LEU   A CB   1 
ATOM   2112 C  CG   . LEU   A 1 505 ? 33.191  -5.374  29.434  1.00 31.57  ? 516 LEU   A CG   1 
ATOM   2113 C  CD1  . LEU   A 1 505 ? 34.102  -6.379  28.731  1.00 34.82  ? 516 LEU   A CD1  1 
ATOM   2114 C  CD2  . LEU   A 1 505 ? 31.902  -6.050  29.914  1.00 33.12  ? 516 LEU   A CD2  1 
ATOM   2115 N  N    . GLN   A 1 506 ? 34.547  -2.248  32.855  1.00 30.77  ? 517 GLN   A N    1 
ATOM   2116 C  CA   . GLN   A 1 506 ? 34.912  -1.876  34.216  1.00 35.66  ? 517 GLN   A CA   1 
ATOM   2117 C  C    . GLN   A 1 506 ? 34.090  -0.717  34.768  1.00 33.35  ? 517 GLN   A C    1 
ATOM   2118 O  O    . GLN   A 1 506 ? 34.312  -0.312  35.913  1.00 36.52  ? 517 GLN   A O    1 
ATOM   2119 C  CB   . GLN   A 1 506 ? 36.402  -1.530  34.284  1.00 39.46  ? 517 GLN   A CB   1 
ATOM   2120 C  CG   . GLN   A 1 506 ? 37.288  -2.689  33.854  1.00 42.10  ? 517 GLN   A CG   1 
ATOM   2121 C  CD   . GLN   A 1 506 ? 36.965  -3.966  34.620  1.00 58.23  ? 517 GLN   A CD   1 
ATOM   2122 O  OE1  . GLN   A 1 506 ? 36.813  -3.952  35.848  1.00 58.60  ? 517 GLN   A OE1  1 
ATOM   2123 N  NE2  . GLN   A 1 506 ? 36.820  -5.070  33.893  1.00 57.17  ? 517 GLN   A NE2  1 
ATOM   2124 N  N    . HIS   A 1 507 ? 33.156  -0.175  33.995  1.00 33.04  ? 518 HIS   A N    1 
ATOM   2125 C  CA   . HIS   A 1 507 ? 32.455  1.037   34.409  1.00 32.55  ? 518 HIS   A CA   1 
ATOM   2126 C  C    . HIS   A 1 507 ? 31.552  0.765   35.609  1.00 36.39  ? 518 HIS   A C    1 
ATOM   2127 O  O    . HIS   A 1 507 ? 30.929  -0.299  35.707  1.00 33.42  ? 518 HIS   A O    1 
ATOM   2128 C  CB   . HIS   A 1 507 ? 31.629  1.599   33.244  1.00 33.53  ? 518 HIS   A CB   1 
ATOM   2129 C  CG   . HIS   A 1 507 ? 31.179  3.012   33.457  1.00 38.97  ? 518 HIS   A CG   1 
ATOM   2130 N  ND1  . HIS   A 1 507 ? 30.107  3.339   34.261  1.00 33.02  ? 518 HIS   A ND1  1 
ATOM   2131 C  CD2  . HIS   A 1 507 ? 31.669  4.185   32.986  1.00 34.37  ? 518 HIS   A CD2  1 
ATOM   2132 C  CE1  . HIS   A 1 507 ? 29.953  4.652   34.273  1.00 37.03  ? 518 HIS   A CE1  1 
ATOM   2133 N  NE2  . HIS   A 1 507 ? 30.889  5.190   33.508  1.00 37.89  ? 518 HIS   A NE2  1 
ATOM   2134 N  N    . GLN   A 1 508 ? 31.481  1.746   36.526  1.00 33.29  ? 519 GLN   A N    1 
ATOM   2135 C  CA   . GLN   A 1 508 ? 30.678  1.581   37.740  1.00 35.31  ? 519 GLN   A CA   1 
ATOM   2136 C  C    . GLN   A 1 508 ? 29.216  1.277   37.430  1.00 39.81  ? 519 GLN   A C    1 
ATOM   2137 O  O    . GLN   A 1 508 ? 28.540  0.620   38.234  1.00 32.79  ? 519 GLN   A O    1 
ATOM   2138 C  CB   . GLN   A 1 508 ? 30.714  2.841   38.622  1.00 34.66  ? 519 GLN   A CB   1 
ATOM   2139 C  CG   . GLN   A 1 508 ? 32.013  3.242   39.296  1.00 49.16  ? 519 GLN   A CG   1 
ATOM   2140 C  CD   . GLN   A 1 508 ? 32.434  2.259   40.366  1.00 68.52  ? 519 GLN   A CD   1 
ATOM   2141 O  OE1  . GLN   A 1 508 ? 33.470  1.600   40.247  1.00 75.05  ? 519 GLN   A OE1  1 
ATOM   2142 N  NE2  . GLN   A 1 508 ? 31.572  2.071   41.363  1.00 66.55  ? 519 GLN   A NE2  1 
ATOM   2143 N  N    . PHE   A 1 509 ? 28.696  1.792   36.311  1.00 31.09  ? 520 PHE   A N    1 
ATOM   2144 C  CA   . PHE   A 1 509 ? 27.285  1.583   35.980  1.00 28.84  ? 520 PHE   A CA   1 
ATOM   2145 C  C    . PHE   A 1 509 ? 26.952  0.102   35.890  1.00 35.76  ? 520 PHE   A C    1 
ATOM   2146 O  O    . PHE   A 1 509 ? 25.869  -0.325  36.302  1.00 30.63  ? 520 PHE   A O    1 
ATOM   2147 C  CB   . PHE   A 1 509 ? 26.934  2.289   34.664  1.00 27.74  ? 520 PHE   A CB   1 
ATOM   2148 C  CG   . PHE   A 1 509 ? 25.544  1.974   34.143  1.00 28.18  ? 520 PHE   A CG   1 
ATOM   2149 C  CD1  . PHE   A 1 509 ? 24.416  2.336   34.872  1.00 31.13  ? 520 PHE   A CD1  1 
ATOM   2150 C  CD2  . PHE   A 1 509 ? 25.372  1.353   32.920  1.00 23.16  ? 520 PHE   A CD2  1 
ATOM   2151 C  CE1  . PHE   A 1 509 ? 23.132  2.051   34.396  1.00 24.72  ? 520 PHE   A CE1  1 
ATOM   2152 C  CE2  . PHE   A 1 509 ? 24.098  1.067   32.427  1.00 26.41  ? 520 PHE   A CE2  1 
ATOM   2153 C  CZ   . PHE   A 1 509 ? 22.973  1.411   33.173  1.00 31.89  ? 520 PHE   A CZ   1 
ATOM   2154 N  N    . LEU   A 1 510 ? 27.873  -0.705  35.355  1.00 30.06  ? 521 LEU   A N    1 
ATOM   2155 C  CA   . LEU   A 1 510 ? 27.591  -2.128  35.241  1.00 29.93  ? 521 LEU   A CA   1 
ATOM   2156 C  C    . LEU   A 1 510 ? 27.495  -2.808  36.596  1.00 32.27  ? 521 LEU   A C    1 
ATOM   2157 O  O    . LEU   A 1 510 ? 26.935  -3.904  36.680  1.00 32.37  ? 521 LEU   A O    1 
ATOM   2158 C  CB   . LEU   A 1 510 ? 28.643  -2.816  34.375  1.00 31.24  ? 521 LEU   A CB   1 
ATOM   2159 C  CG   . LEU   A 1 510 ? 28.721  -2.218  32.968  1.00 25.58  ? 521 LEU   A CG   1 
ATOM   2160 C  CD1  . LEU   A 1 510 ? 29.647  -3.040  32.066  1.00 31.62  ? 521 LEU   A CD1  1 
ATOM   2161 C  CD2  . LEU   A 1 510 ? 27.332  -2.083  32.334  1.00 25.30  ? 521 LEU   A CD2  1 
ATOM   2162 N  N    . LYS   A 1 511 ? 28.012  -2.186  37.659  1.00 34.82  ? 522 LYS   A N    1 
ATOM   2163 C  CA   . LYS   A 1 511 ? 27.974  -2.851  38.949  1.00 32.26  ? 522 LYS   A CA   1 
ATOM   2164 C  C    . LYS   A 1 511 ? 26.583  -2.856  39.567  1.00 35.77  ? 522 LYS   A C    1 
ATOM   2165 O  O    . LYS   A 1 511 ? 26.367  -3.602  40.525  1.00 37.29  ? 522 LYS   A O    1 
ATOM   2166 C  CB   . LYS   A 1 511 ? 28.953  -2.194  39.926  1.00 32.02  ? 522 LYS   A CB   1 
ATOM   2167 C  CG   . LYS   A 1 511 ? 30.421  -2.165  39.479  1.00 46.79  ? 522 LYS   A CG   1 
ATOM   2168 C  CD   . LYS   A 1 511 ? 31.306  -1.573  40.573  1.00 49.13  ? 522 LYS   A CD   1 
ATOM   2169 C  CE   . LYS   A 1 511 ? 32.748  -1.385  40.119  1.00 59.74  ? 522 LYS   A CE   1 
ATOM   2170 N  NZ   . LYS   A 1 511 ? 33.151  -2.316  39.030  1.00 61.76  ? 522 LYS   A NZ   1 
ATOM   2171 N  N    . ILE   A 1 512 ? 25.632  -2.084  39.038  1.00 30.32  ? 523 ILE   A N    1 
ATOM   2172 C  CA   . ILE   A 1 512 ? 24.258  -2.122  39.540  1.00 28.61  ? 523 ILE   A CA   1 
ATOM   2173 C  C    . ILE   A 1 512 ? 23.409  -3.103  38.745  1.00 31.39  ? 523 ILE   A C    1 
ATOM   2174 O  O    . ILE   A 1 512 ? 22.185  -3.145  38.910  1.00 30.74  ? 523 ILE   A O    1 
ATOM   2175 C  CB   . ILE   A 1 512 ? 23.602  -0.726  39.536  1.00 30.51  ? 523 ILE   A CB   1 
ATOM   2176 C  CG1  . ILE   A 1 512 ? 23.289  -0.256  38.124  1.00 36.03  ? 523 ILE   A CG1  1 
ATOM   2177 C  CG2  . ILE   A 1 512 ? 24.474  0.283   40.282  1.00 44.12  ? 523 ILE   A CG2  1 
ATOM   2178 C  CD1  . ILE   A 1 512 ? 22.438  0.987   38.076  1.00 38.92  ? 523 ILE   A CD1  1 
ATOM   2179 N  N    . ALA   A 1 513 ? 24.037  -3.870  37.855  1.00 28.88  ? 524 ALA   A N    1 
ATOM   2180 C  CA   . ALA   A 1 513 ? 23.292  -4.800  37.014  1.00 32.69  ? 524 ALA   A CA   1 
ATOM   2181 C  C    . ALA   A 1 513 ? 22.537  -5.824  37.855  1.00 31.03  ? 524 ALA   A C    1 
ATOM   2182 O  O    . ALA   A 1 513 ? 23.075  -6.379  38.815  1.00 33.47  ? 524 ALA   A O    1 
ATOM   2183 C  CB   . ALA   A 1 513 ? 24.235  -5.504  36.036  1.00 32.19  ? 524 ALA   A CB   1 
ATOM   2184 N  N    . LYS   A 1 514 ? 21.272  -6.048  37.512  1.00 32.82  ? 525 LYS   A N    1 
ATOM   2185 C  CA   . LYS   A 1 514 ? 20.498  -7.139  38.088  1.00 30.34  ? 525 LYS   A CA   1 
ATOM   2186 C  C    . LYS   A 1 514 ? 20.858  -8.450  37.391  1.00 33.32  ? 525 LYS   A C    1 
ATOM   2187 O  O    . LYS   A 1 514 ? 21.456  -8.439  36.310  1.00 31.58  ? 525 LYS   A O    1 
ATOM   2188 C  CB   . LYS   A 1 514 ? 19.005  -6.855  37.934  1.00 30.83  ? 525 LYS   A CB   1 
ATOM   2189 C  CG   . LYS   A 1 514 ? 18.465  -5.738  38.806  1.00 32.90  ? 525 LYS   A CG   1 
ATOM   2190 C  CD   . LYS   A 1 514 ? 16.967  -5.607  38.597  1.00 31.51  ? 525 LYS   A CD   1 
ATOM   2191 C  CE   . LYS   A 1 514 ? 16.346  -4.617  39.558  1.00 36.59  ? 525 LYS   A CE   1 
ATOM   2192 N  NZ   . LYS   A 1 514 ? 14.871  -4.554  39.332  1.00 36.59  ? 525 LYS   A NZ   1 
ATOM   2193 N  N    . PRO   A 1 515 ? 20.543  -9.598  37.999  1.00 30.50  ? 526 PRO   A N    1 
ATOM   2194 C  CA   . PRO   A 1 515 ? 20.771  -10.879 37.313  1.00 29.35  ? 526 PRO   A CA   1 
ATOM   2195 C  C    . PRO   A 1 515 ? 19.934  -10.968 36.047  1.00 33.84  ? 526 PRO   A C    1 
ATOM   2196 O  O    . PRO   A 1 515 ? 18.901  -10.310 35.912  1.00 29.74  ? 526 PRO   A O    1 
ATOM   2197 C  CB   . PRO   A 1 515 ? 20.331  -11.926 38.345  1.00 38.28  ? 526 PRO   A CB   1 
ATOM   2198 C  CG   . PRO   A 1 515 ? 19.434  -11.202 39.260  1.00 38.35  ? 526 PRO   A CG   1 
ATOM   2199 C  CD   . PRO   A 1 515 ? 19.959  -9.798  39.340  1.00 32.35  ? 526 PRO   A CD   1 
ATOM   2200 N  N    . LEU   A 1 516 ? 20.400  -11.781 35.093  1.00 26.87  ? 527 LEU   A N    1 
ATOM   2201 C  CA   . LEU   A 1 516 ? 19.698  -11.841 33.812  1.00 26.92  ? 527 LEU   A CA   1 
ATOM   2202 C  C    . LEU   A 1 516 ? 18.285  -12.402 33.950  1.00 29.48  ? 527 LEU   A C    1 
ATOM   2203 O  O    . LEU   A 1 516 ? 17.432  -12.121 33.102  1.00 24.38  ? 527 LEU   A O    1 
ATOM   2204 C  CB   . LEU   A 1 516 ? 20.510  -12.664 32.808  1.00 31.44  ? 527 LEU   A CB   1 
ATOM   2205 C  CG   . LEU   A 1 516 ? 21.822  -11.991 32.392  1.00 34.50  ? 527 LEU   A CG   1 
ATOM   2206 C  CD1  . LEU   A 1 516 ? 22.653  -12.911 31.525  1.00 33.00  ? 527 LEU   A CD1  1 
ATOM   2207 C  CD2  . LEU   A 1 516 ? 21.537  -10.695 31.660  1.00 26.89  ? 527 LEU   A CD2  1 
ATOM   2208 N  N    . SER   A 1 517 ? 18.006  -13.165 35.008  1.00 28.59  ? 528 SER   A N    1 
ATOM   2209 C  CA   . SER   A 1 517 ? 16.635  -13.610 35.246  1.00 33.50  ? 528 SER   A CA   1 
ATOM   2210 C  C    . SER   A 1 517 ? 15.663  -12.435 35.375  1.00 32.75  ? 528 SER   A C    1 
ATOM   2211 O  O    . SER   A 1 517 ? 14.470  -12.583 35.078  1.00 27.79  ? 528 SER   A O    1 
ATOM   2212 C  CB   . SER   A 1 517 ? 16.582  -14.482 36.500  1.00 37.86  ? 528 SER   A CB   1 
ATOM   2213 O  OG   . SER   A 1 517 ? 17.018  -13.758 37.639  1.00 33.37  ? 528 SER   A OG   1 
ATOM   2214 N  N    . SER   A 1 518 ? 16.151  -11.259 35.791  1.00 27.37  ? 529 SER   A N    1 
ATOM   2215 C  CA   . SER   A 1 518 ? 15.289  -10.081 35.882  1.00 29.26  ? 529 SER   A CA   1 
ATOM   2216 C  C    . SER   A 1 518 ? 14.694  -9.685  34.543  1.00 29.35  ? 529 SER   A C    1 
ATOM   2217 O  O    . SER   A 1 518 ? 13.722  -8.930  34.516  1.00 26.54  ? 529 SER   A O    1 
ATOM   2218 C  CB   . SER   A 1 518 ? 16.055  -8.873  36.451  1.00 27.40  ? 529 SER   A CB   1 
ATOM   2219 O  OG   . SER   A 1 518 ? 16.991  -8.337  35.506  1.00 29.90  ? 529 SER   A OG   1 
ATOM   2220 N  N    . LEU   A 1 519 ? 15.239  -10.178 33.430  1.00 24.39  ? 530 LEU   A N    1 
ATOM   2221 C  CA   . LEU   A 1 519 ? 14.700  -9.812  32.132  1.00 23.28  ? 530 LEU   A CA   1 
ATOM   2222 C  C    . LEU   A 1 519 ? 13.492  -10.649 31.730  1.00 23.73  ? 530 LEU   A C    1 
ATOM   2223 O  O    . LEU   A 1 519 ? 12.779  -10.261 30.801  1.00 25.56  ? 530 LEU   A O    1 
ATOM   2224 C  CB   . LEU   A 1 519 ? 15.792  -9.937  31.048  1.00 24.16  ? 530 LEU   A CB   1 
ATOM   2225 C  CG   . LEU   A 1 519 ? 17.086  -9.117  31.211  1.00 24.81  ? 530 LEU   A CG   1 
ATOM   2226 C  CD1  . LEU   A 1 519 ? 18.025  -9.342  30.017  1.00 24.02  ? 530 LEU   A CD1  1 
ATOM   2227 C  CD2  . LEU   A 1 519 ? 16.833  -7.596  31.426  1.00 22.61  ? 530 LEU   A CD2  1 
ATOM   2228 N  N    . THR   A 1 520 ? 13.251  -11.790 32.371  1.00 25.89  ? 531 THR   A N    1 
ATOM   2229 C  CA   . THR   A 1 520 ? 12.197  -12.650 31.840  1.00 26.91  ? 531 THR   A CA   1 
ATOM   2230 C  C    . THR   A 1 520 ? 10.804  -12.054 32.034  1.00 28.55  ? 531 THR   A C    1 
ATOM   2231 O  O    . THR   A 1 520 ? 9.928   -12.312 31.197  1.00 25.42  ? 531 THR   A O    1 
ATOM   2232 C  CB   . THR   A 1 520 ? 12.275  -14.087 32.403  1.00 33.22  ? 531 THR   A CB   1 
ATOM   2233 O  OG1  . THR   A 1 520 ? 11.932  -14.141 33.791  1.00 32.10  ? 531 THR   A OG1  1 
ATOM   2234 C  CG2  . THR   A 1 520 ? 13.664  -14.692 32.193  1.00 32.21  ? 531 THR   A CG2  1 
ATOM   2235 N  N    . PRO   A 1 521 ? 10.532  -11.247 33.074  1.00 25.20  ? 532 PRO   A N    1 
ATOM   2236 C  CA   . PRO   A 1 521 ? 9.228   -10.577 33.090  1.00 23.06  ? 532 PRO   A CA   1 
ATOM   2237 C  C    . PRO   A 1 521 ? 9.065   -9.604  31.949  1.00 21.14  ? 532 PRO   A C    1 
ATOM   2238 O  O    . PRO   A 1 521 ? 7.950   -9.471  31.435  1.00 21.87  ? 532 PRO   A O    1 
ATOM   2239 C  CB   . PRO   A 1 521 ? 9.195   -9.877  34.462  1.00 25.23  ? 532 PRO   A CB   1 
ATOM   2240 C  CG   . PRO   A 1 521 ? 10.072  -10.739 35.324  1.00 25.01  ? 532 PRO   A CG   1 
ATOM   2241 C  CD   . PRO   A 1 521 ? 11.207  -11.115 34.376  1.00 25.42  ? 532 PRO   A CD   1 
ATOM   2242 N  N    . LEU   A 1 522 ? 10.144  -8.935  31.528  1.00 22.78  ? 533 LEU   A N    1 
ATOM   2243 C  CA   . LEU   A 1 522 ? 10.076  -8.051  30.369  1.00 24.77  ? 533 LEU   A CA   1 
ATOM   2244 C  C    . LEU   A 1 522 ? 9.762   -8.835  29.100  1.00 21.90  ? 533 LEU   A C    1 
ATOM   2245 O  O    . LEU   A 1 522 ? 8.997   -8.372  28.247  1.00 21.76  ? 533 LEU   A O    1 
ATOM   2246 C  CB   . LEU   A 1 522 ? 11.403  -7.301  30.198  1.00 22.57  ? 533 LEU   A CB   1 
ATOM   2247 C  CG   . LEU   A 1 522 ? 11.872  -6.375  31.325  1.00 23.27  ? 533 LEU   A CG   1 
ATOM   2248 C  CD1  . LEU   A 1 522 ? 13.257  -5.780  30.973  1.00 23.53  ? 533 LEU   A CD1  1 
ATOM   2249 C  CD2  . LEU   A 1 522 ? 10.850  -5.267  31.610  1.00 24.78  ? 533 LEU   A CD2  1 
ATOM   2250 N  N    . ILE   A 1 523 ? 10.385  -10.004 28.939  1.00 21.99  ? 534 ILE   A N    1 
ATOM   2251 C  CA   . ILE   A 1 523 ? 10.084  -10.852 27.788  1.00 25.86  ? 534 ILE   A CA   1 
ATOM   2252 C  C    . ILE   A 1 523 ? 8.613   -11.237 27.783  1.00 20.87  ? 534 ILE   A C    1 
ATOM   2253 O  O    . ILE   A 1 523 ? 7.954   -11.211 26.735  1.00 23.22  ? 534 ILE   A O    1 
ATOM   2254 C  CB   . ILE   A 1 523 ? 11.004  -12.087 27.789  1.00 25.57  ? 534 ILE   A CB   1 
ATOM   2255 C  CG1  . ILE   A 1 523 ? 12.456  -11.650 27.574  1.00 25.81  ? 534 ILE   A CG1  1 
ATOM   2256 C  CG2  . ILE   A 1 523 ? 10.539  -13.125 26.753  1.00 28.73  ? 534 ILE   A CG2  1 
ATOM   2257 C  CD1  . ILE   A 1 523 ? 13.489  -12.694 27.967  1.00 28.74  ? 534 ILE   A CD1  1 
ATOM   2258 N  N    . ALA   A 1 524 ? 8.066   -11.579 28.957  1.00 23.05  ? 535 ALA   A N    1 
ATOM   2259 C  CA   . ALA   A 1 524 ? 6.655   -11.938 29.039  1.00 27.07  ? 535 ALA   A CA   1 
ATOM   2260 C  C    . ALA   A 1 524 ? 5.768   -10.759 28.657  1.00 26.82  ? 535 ALA   A C    1 
ATOM   2261 O  O    . ALA   A 1 524 ? 4.742   -10.938 27.992  1.00 25.04  ? 535 ALA   A O    1 
ATOM   2262 C  CB   . ALA   A 1 524 ? 6.302   -12.437 30.446  1.00 24.10  ? 535 ALA   A CB   1 
ATOM   2263 N  N    . ALA   A 1 525 ? 6.125   -9.549  29.109  1.00 22.30  ? 536 ALA   A N    1 
ATOM   2264 C  CA   . ALA   A 1 525 ? 5.337   -8.367  28.762  1.00 23.78  ? 536 ALA   A CA   1 
ATOM   2265 C  C    . ALA   A 1 525 ? 5.401   -8.083  27.266  1.00 22.08  ? 536 ALA   A C    1 
ATOM   2266 O  O    . ALA   A 1 525 ? 4.382   -7.763  26.641  1.00 25.15  ? 536 ALA   A O    1 
ATOM   2267 C  CB   . ALA   A 1 525 ? 5.818   -7.151  29.568  1.00 19.23  ? 536 ALA   A CB   1 
ATOM   2268 N  N    . ALA   A 1 526 ? 6.590   -8.189  26.679  1.00 22.69  ? 537 ALA   A N    1 
ATOM   2269 C  CA   . ALA   A 1 526 ? 6.733   -7.945  25.247  1.00 29.20  ? 537 ALA   A CA   1 
ATOM   2270 C  C    . ALA   A 1 526 ? 5.914   -8.942  24.432  1.00 27.64  ? 537 ALA   A C    1 
ATOM   2271 O  O    . ALA   A 1 526 ? 5.268   -8.565  23.446  1.00 26.54  ? 537 ALA   A O    1 
ATOM   2272 C  CB   . ALA   A 1 526 ? 8.206   -8.008  24.854  1.00 24.81  ? 537 ALA   A CB   1 
ATOM   2273 N  N    . LYS   A 1 527 ? 5.927   -10.221 24.827  1.00 29.12  ? 538 LYS   A N    1 
ATOM   2274 C  CA   . LYS   A 1 527 ? 5.123   -11.215 24.115  1.00 28.14  ? 538 LYS   A CA   1 
ATOM   2275 C  C    . LYS   A 1 527 ? 3.636   -10.901 24.219  1.00 31.61  ? 538 LYS   A C    1 
ATOM   2276 O  O    . LYS   A 1 527 ? 2.907   -10.971 23.221  1.00 29.78  ? 538 LYS   A O    1 
ATOM   2277 C  CB   . LYS   A 1 527 ? 5.417   -12.619 24.649  1.00 34.95  ? 538 LYS   A CB   1 
ATOM   2278 C  CG   . LYS   A 1 527 ? 6.855   -13.092 24.345  1.00 42.51  ? 538 LYS   A CG   1 
ATOM   2279 C  CD   . LYS   A 1 527 ? 7.101   -14.532 24.811  1.00 43.84  ? 538 LYS   A CD   1 
ATOM   2280 C  CE   . LYS   A 1 527 ? 8.412   -15.104 24.263  1.00 50.63  ? 538 LYS   A CE   1 
ATOM   2281 N  NZ   . LYS   A 1 527 ? 8.491   -15.131 22.770  1.00 51.07  ? 538 LYS   A NZ   1 
ATOM   2282 N  N    . GLU   A 1 528 ? 3.166   -10.529 25.417  1.00 26.26  ? 539 GLU   A N    1 
ATOM   2283 C  CA   . GLU   A 1 528 ? 1.766   -10.155 25.572  1.00 28.35  ? 539 GLU   A CA   1 
ATOM   2284 C  C    . GLU   A 1 528 ? 1.432   -8.929  24.739  1.00 29.87  ? 539 GLU   A C    1 
ATOM   2285 O  O    . GLU   A 1 528 ? 0.357   -8.854  24.131  1.00 32.18  ? 539 GLU   A O    1 
ATOM   2286 C  CB   . GLU   A 1 528 ? 1.448   -9.894  27.051  1.00 26.66  ? 539 GLU   A CB   1 
ATOM   2287 C  CG   . GLU   A 1 528 ? 0.088   -9.261  27.327  1.00 29.80  ? 539 GLU   A CG   1 
ATOM   2288 C  CD   . GLU   A 1 528 ? -1.102  -10.182 27.060  1.00 45.73  ? 539 GLU   A CD   1 
ATOM   2289 O  OE1  . GLU   A 1 528 ? -0.910  -11.415 26.910  1.00 37.05  ? 539 GLU   A OE1  1 
ATOM   2290 O  OE2  . GLU   A 1 528 ? -2.243  -9.661  27.033  1.00 38.97  ? 539 GLU   A OE2  1 
ATOM   2291 N  N    . ALA   A 1 529 ? 2.332   -7.947  24.713  1.00 23.87  ? 540 ALA   A N    1 
ATOM   2292 C  CA   . ALA   A 1 529 ? 2.037   -6.718  23.989  1.00 33.05  ? 540 ALA   A CA   1 
ATOM   2293 C  C    . ALA   A 1 529 ? 2.005   -6.951  22.488  1.00 35.30  ? 540 ALA   A C    1 
ATOM   2294 O  O    . ALA   A 1 529 ? 1.234   -6.298  21.773  1.00 33.20  ? 540 ALA   A O    1 
ATOM   2295 C  CB   . ALA   A 1 529 ? 3.082   -5.648  24.303  1.00 29.78  ? 540 ALA   A CB   1 
ATOM   2296 N  N    . THR   A 1 530 ? 2.826   -7.868  21.997  1.00 25.53  ? 541 THR   A N    1 
ATOM   2297 C  CA   . THR   A 1 530 ? 2.917   -8.109  20.562  1.00 37.68  ? 541 THR   A CA   1 
ATOM   2298 C  C    . THR   A 1 530 ? 1.874   -9.100  20.073  1.00 55.52  ? 541 THR   A C    1 
ATOM   2299 O  O    . THR   A 1 530 ? 1.888   -9.462  18.893  1.00 58.67  ? 541 THR   A O    1 
ATOM   2300 C  CB   . THR   A 1 530 ? 4.332   -8.559  20.167  1.00 32.03  ? 541 THR   A CB   1 
ATOM   2301 O  OG1  . THR   A 1 530 ? 4.722   -9.713  20.918  1.00 48.51  ? 541 THR   A OG1  1 
ATOM   2302 C  CG2  . THR   A 1 530 ? 5.327   -7.432  20.404  1.00 44.64  ? 541 THR   A CG2  1 
ATOM   2303 N  N    . LYS   A 1 531 ? 0.992   -9.555  20.965  1.00 47.42  ? 542 LYS   A N    1 
ATOM   2304 C  CA   . LYS   A 1 531 ? -0.201  -10.305 20.609  1.00 65.34  ? 542 LYS   A CA   1 
ATOM   2305 C  C    . LYS   A 1 531 ? -1.459  -9.452  20.735  1.00 69.12  ? 542 LYS   A C    1 
ATOM   2306 O  O    . LYS   A 1 531 ? -2.493  -9.805  20.154  1.00 80.96  ? 542 LYS   A O    1 
ATOM   2307 C  CB   . LYS   A 1 531 ? -0.336  -11.561 21.493  1.00 47.92  ? 542 LYS   A CB   1 
ATOM   2308 C  CG   . LYS   A 1 531 ? -1.422  -11.481 22.554  1.00 55.58  ? 542 LYS   A CG   1 
ATOM   2309 C  CD   . LYS   A 1 531 ? -1.280  -12.584 23.596  1.00 59.97  ? 542 LYS   A CD   1 
ATOM   2310 C  CE   . LYS   A 1 531 ? -1.258  -13.973 22.965  1.00 72.34  ? 542 LYS   A CE   1 
ATOM   2311 N  NZ   . LYS   A 1 531 ? -0.786  -15.022 23.928  1.00 61.80  ? 542 LYS   A NZ   1 
ATOM   2312 N  N    . ASN   A 1 532 ? -1.376  -8.319  21.443  1.00 68.78  ? 543 ASN   A N    1 
ATOM   2313 C  CA   . ASN   A 1 532 ? -2.466  -7.354  21.555  1.00 68.90  ? 543 ASN   A CA   1 
ATOM   2314 C  C    . ASN   A 1 532 ? -2.404  -6.270  20.487  1.00 73.25  ? 543 ASN   A C    1 
ATOM   2315 O  O    . ASN   A 1 532 ? -3.437  -5.676  20.158  1.00 68.25  ? 543 ASN   A O    1 
ATOM   2316 C  CB   . ASN   A 1 532 ? -2.455  -6.702  22.940  1.00 60.71  ? 543 ASN   A CB   1 
ATOM   2317 N  N    . ASN   A 1 533 ? -1.214  -5.989  19.948  1.00 71.09  ? 544 ASN   A N    1 
ATOM   2318 C  CA   . ASN   A 1 533 ? -1.111  -5.189  18.735  1.00 76.30  ? 544 ASN   A CA   1 
ATOM   2319 C  C    . ASN   A 1 533 ? -1.623  -5.940  17.511  1.00 83.08  ? 544 ASN   A C    1 
ATOM   2320 O  O    . ASN   A 1 533 ? -1.757  -5.339  16.438  1.00 76.31  ? 544 ASN   A O    1 
ATOM   2321 C  CB   . ASN   A 1 533 ? 0.342   -4.753  18.520  1.00 57.61  ? 544 ASN   A CB   1 
ATOM   2322 N  N    . HIS   A 1 534 ? -1.921  -7.229  17.656  1.00 88.60  ? 545 HIS   A N    1 
ATOM   2323 C  CA   . HIS   A 1 534 ? -2.378  -8.069  16.559  1.00 90.33  ? 545 HIS   A CA   1 
ATOM   2324 C  C    . HIS   A 1 534 ? -3.842  -8.460  16.749  1.00 92.91  ? 545 HIS   A C    1 
ATOM   2325 O  O    . HIS   A 1 534 ? -4.695  -7.612  17.014  1.00 89.19  ? 545 HIS   A O    1 
ATOM   2326 C  CB   . HIS   A 1 534 ? -1.505  -9.324  16.452  1.00 84.19  ? 545 HIS   A CB   1 
ATOM   2327 C  CG   . HIS   A 1 534 ? -0.093  -9.049  16.033  1.00 93.53  ? 545 HIS   A CG   1 
ATOM   2328 N  ND1  . HIS   A 1 534 ? 0.603   -7.928  16.436  1.00 90.32  ? 545 HIS   A ND1  1 
ATOM   2329 C  CD2  . HIS   A 1 534 ? 0.756   -9.755  15.250  1.00 94.73  ? 545 HIS   A CD2  1 
ATOM   2330 C  CE1  . HIS   A 1 534 ? 1.817   -7.954  15.916  1.00 86.11  ? 545 HIS   A CE1  1 
ATOM   2331 N  NE2  . HIS   A 1 534 ? 1.936   -9.053  15.192  1.00 94.98  ? 545 HIS   A NE2  1 
ATOM   2332 N  N    . GLU   B 1 244 ? -17.030 -13.185 -4.448  1.00 110.83 ? 255 GLU   B N    1 
ATOM   2333 C  CA   . GLU   B 1 244 ? -16.824 -13.993 -5.643  1.00 101.63 ? 255 GLU   B CA   1 
ATOM   2334 C  C    . GLU   B 1 244 ? -16.479 -13.119 -6.845  1.00 94.84  ? 255 GLU   B C    1 
ATOM   2335 O  O    . GLU   B 1 244 ? -16.698 -13.515 -7.989  1.00 97.99  ? 255 GLU   B O    1 
ATOM   2336 C  CB   . GLU   B 1 244 ? -18.057 -14.847 -5.944  1.00 93.31  ? 255 GLU   B CB   1 
ATOM   2337 N  N    . LYS   B 1 245 ? -15.942 -11.925 -6.572  1.00 101.22 ? 256 LYS   B N    1 
ATOM   2338 C  CA   . LYS   B 1 245 ? -15.383 -11.101 -7.640  1.00 94.58  ? 256 LYS   B CA   1 
ATOM   2339 C  C    . LYS   B 1 245 ? -14.278 -11.849 -8.368  1.00 102.73 ? 256 LYS   B C    1 
ATOM   2340 O  O    . LYS   B 1 245 ? -14.026 -11.599 -9.553  1.00 97.50  ? 256 LYS   B O    1 
ATOM   2341 C  CB   . LYS   B 1 245 ? -14.855 -9.781  -7.078  1.00 99.10  ? 256 LYS   B CB   1 
ATOM   2342 N  N    . LEU   B 1 246 ? -13.599 -12.751 -7.656  1.00 97.47  ? 257 LEU   B N    1 
ATOM   2343 C  CA   . LEU   B 1 246 ? -12.614 -13.630 -8.267  1.00 89.50  ? 257 LEU   B CA   1 
ATOM   2344 C  C    . LEU   B 1 246 ? -13.206 -14.357 -9.469  1.00 92.41  ? 257 LEU   B C    1 
ATOM   2345 O  O    . LEU   B 1 246 ? -12.572 -14.440 -10.526 1.00 92.68  ? 257 LEU   B O    1 
ATOM   2346 C  CB   . LEU   B 1 246 ? -12.127 -14.632 -7.220  1.00 84.96  ? 257 LEU   B CB   1 
ATOM   2347 C  CG   . LEU   B 1 246 ? -11.072 -15.682 -7.551  1.00 85.54  ? 257 LEU   B CG   1 
ATOM   2348 C  CD1  . LEU   B 1 246 ? -9.775  -15.020 -7.956  1.00 86.85  ? 257 LEU   B CD1  1 
ATOM   2349 C  CD2  . LEU   B 1 246 ? -10.863 -16.614 -6.366  1.00 98.92  ? 257 LEU   B CD2  1 
ATOM   2350 N  N    . ARG   B 1 247 ? -14.440 -14.859 -9.337  1.00 95.84  ? 258 ARG   B N    1 
ATOM   2351 C  CA   . ARG   B 1 247 ? -15.071 -15.601 -10.429 1.00 97.26  ? 258 ARG   B CA   1 
ATOM   2352 C  C    . ARG   B 1 247 ? -15.203 -14.761 -11.696 1.00 96.96  ? 258 ARG   B C    1 
ATOM   2353 O  O    . ARG   B 1 247 ? -15.154 -15.303 -12.808 1.00 91.53  ? 258 ARG   B O    1 
ATOM   2354 C  CB   . ARG   B 1 247 ? -16.445 -16.111 -9.989  1.00 95.89  ? 258 ARG   B CB   1 
ATOM   2355 N  N    . SER   B 1 248 ? -15.375 -13.444 -11.556 1.00 95.36  ? 259 SER   B N    1 
ATOM   2356 C  CA   . SER   B 1 248 ? -15.539 -12.601 -12.737 1.00 96.83  ? 259 SER   B CA   1 
ATOM   2357 C  C    . SER   B 1 248 ? -14.247 -12.493 -13.539 1.00 99.68  ? 259 SER   B C    1 
ATOM   2358 O  O    . SER   B 1 248 ? -14.288 -12.292 -14.759 1.00 92.22  ? 259 SER   B O    1 
ATOM   2359 C  CB   . SER   B 1 248 ? -16.007 -11.208 -12.320 1.00 97.79  ? 259 SER   B CB   1 
ATOM   2360 O  OG   . SER   B 1 248 ? -14.952 -10.495 -11.692 1.00 90.99  ? 259 SER   B OG   1 
ATOM   2361 N  N    . ILE   B 1 249 ? -13.096 -12.627 -12.875 1.00 92.75  ? 260 ILE   B N    1 
ATOM   2362 C  CA   . ILE   B 1 249 ? -11.798 -12.493 -13.524 1.00 84.38  ? 260 ILE   B CA   1 
ATOM   2363 C  C    . ILE   B 1 249 ? -11.188 -13.830 -13.895 1.00 86.97  ? 260 ILE   B C    1 
ATOM   2364 O  O    . ILE   B 1 249 ? -10.092 -13.860 -14.467 1.00 92.16  ? 260 ILE   B O    1 
ATOM   2365 C  CB   . ILE   B 1 249 ? -10.813 -11.714 -12.636 1.00 87.77  ? 260 ILE   B CB   1 
ATOM   2366 C  CG1  . ILE   B 1 249 ? -11.556 -11.080 -11.466 1.00 100.77 ? 260 ILE   B CG1  1 
ATOM   2367 C  CG2  . ILE   B 1 249 ? -10.096 -10.658 -13.451 1.00 90.36  ? 260 ILE   B CG2  1 
ATOM   2368 C  CD1  . ILE   B 1 249 ? -10.646 -10.445 -10.464 1.00 98.03  ? 260 ILE   B CD1  1 
ATOM   2369 N  N    . VAL   B 1 250 ? -11.855 -14.937 -13.595 1.00 74.12  ? 261 VAL   B N    1 
ATOM   2370 C  CA   . VAL   B 1 250 ? -11.306 -16.269 -13.814 1.00 71.15  ? 261 VAL   B CA   1 
ATOM   2371 C  C    . VAL   B 1 250 ? -12.037 -16.913 -14.980 1.00 64.98  ? 261 VAL   B C    1 
ATOM   2372 O  O    . VAL   B 1 250 ? -13.266 -17.045 -14.958 1.00 87.70  ? 261 VAL   B O    1 
ATOM   2373 C  CB   . VAL   B 1 250 ? -11.407 -17.137 -12.548 1.00 78.32  ? 261 VAL   B CB   1 
ATOM   2374 C  CG1  . VAL   B 1 250 ? -10.890 -18.536 -12.810 1.00 78.43  ? 261 VAL   B CG1  1 
ATOM   2375 C  CG2  . VAL   B 1 250 ? -10.587 -16.524 -11.431 1.00 76.89  ? 261 VAL   B CG2  1 
ATOM   2376 N  N    . SER   B 1 251 ? -11.278 -17.302 -15.998 1.00 66.55  ? 262 SER   B N    1 
ATOM   2377 C  CA   . SER   B 1 251 ? -11.796 -18.157 -17.051 1.00 74.23  ? 262 SER   B CA   1 
ATOM   2378 C  C    . SER   B 1 251 ? -12.095 -19.549 -16.494 1.00 74.30  ? 262 SER   B C    1 
ATOM   2379 O  O    . SER   B 1 251 ? -11.570 -19.958 -15.455 1.00 70.24  ? 262 SER   B O    1 
ATOM   2380 C  CB   . SER   B 1 251 ? -10.792 -18.240 -18.202 1.00 65.70  ? 262 SER   B CB   1 
ATOM   2381 O  OG   . SER   B 1 251 ? -11.270 -19.063 -19.253 1.00 84.93  ? 262 SER   B OG   1 
ATOM   2382 N  N    . VAL   B 1 252 ? -12.948 -20.290 -17.202 1.00 70.02  ? 263 VAL   B N    1 
ATOM   2383 C  CA   . VAL   B 1 252 ? -13.423 -21.570 -16.682 1.00 81.60  ? 263 VAL   B CA   1 
ATOM   2384 C  C    . VAL   B 1 252 ? -12.698 -22.772 -17.278 1.00 72.06  ? 263 VAL   B C    1 
ATOM   2385 O  O    . VAL   B 1 252 ? -12.855 -23.891 -16.761 1.00 94.27  ? 263 VAL   B O    1 
ATOM   2386 C  CB   . VAL   B 1 252 ? -14.946 -21.723 -16.887 1.00 86.73  ? 263 VAL   B CB   1 
ATOM   2387 C  CG1  . VAL   B 1 252 ? -15.702 -20.737 -16.000 1.00 82.88  ? 263 VAL   B CG1  1 
ATOM   2388 C  CG2  . VAL   B 1 252 ? -15.303 -21.515 -18.345 1.00 93.82  ? 263 VAL   B CG2  1 
ATOM   2389 N  N    . GLY   B 1 253 ? -11.906 -22.585 -18.331 1.00 79.35  ? 264 GLY   B N    1 
ATOM   2390 C  CA   . GLY   B 1 253 ? -11.191 -23.690 -18.944 1.00 77.59  ? 264 GLY   B CA   1 
ATOM   2391 C  C    . GLY   B 1 253 ? -10.134 -24.330 -18.063 1.00 70.60  ? 264 GLY   B C    1 
ATOM   2392 O  O    . GLY   B 1 253 ? -9.935  -23.934 -16.910 1.00 68.97  ? 264 GLY   B O    1 
ATOM   2393 N  N    . ASP   B 1 254 ? -9.478  -25.373 -18.582 1.00 58.88  ? 265 ASP   B N    1 
ATOM   2394 C  CA   . ASP   B 1 254 ? -8.360  -25.994 -17.887 1.00 45.86  ? 265 ASP   B CA   1 
ATOM   2395 C  C    . ASP   B 1 254 ? -7.071  -25.451 -18.485 1.00 44.19  ? 265 ASP   B C    1 
ATOM   2396 O  O    . ASP   B 1 254 ? -6.726  -25.821 -19.617 1.00 50.00  ? 265 ASP   B O    1 
ATOM   2397 C  CB   . ASP   B 1 254 ? -8.417  -27.514 -18.027 1.00 50.09  ? 265 ASP   B CB   1 
ATOM   2398 C  CG   . ASP   B 1 254 ? -7.307  -28.227 -17.258 1.00 51.02  ? 265 ASP   B CG   1 
ATOM   2399 O  OD1  . ASP   B 1 254 ? -6.394  -27.563 -16.720 1.00 51.18  ? 265 ASP   B OD1  1 
ATOM   2400 O  OD2  . ASP   B 1 254 ? -7.343  -29.470 -17.190 1.00 54.76  ? 265 ASP   B OD2  1 
ATOM   2401 N  N    . PRO   B 1 255 ? -6.313  -24.613 -17.772 1.00 44.77  ? 266 PRO   B N    1 
ATOM   2402 C  CA   . PRO   B 1 255 ? -5.062  -24.091 -18.348 1.00 45.79  ? 266 PRO   B CA   1 
ATOM   2403 C  C    . PRO   B 1 255 ? -4.032  -25.169 -18.606 1.00 38.36  ? 266 PRO   B C    1 
ATOM   2404 O  O    . PRO   B 1 255 ? -3.138  -24.967 -19.438 1.00 38.99  ? 266 PRO   B O    1 
ATOM   2405 C  CB   . PRO   B 1 255 ? -4.581  -23.083 -17.296 1.00 46.20  ? 266 PRO   B CB   1 
ATOM   2406 C  CG   . PRO   B 1 255 ? -5.148  -23.585 -16.030 1.00 43.57  ? 266 PRO   B CG   1 
ATOM   2407 C  CD   . PRO   B 1 255 ? -6.493  -24.179 -16.377 1.00 50.69  ? 266 PRO   B CD   1 
ATOM   2408 N  N    . LYS   B 1 256 ? -4.117  -26.302 -17.906 1.00 40.98  ? 267 LYS   B N    1 
ATOM   2409 C  CA   . LYS   B 1 256 ? -3.192  -27.398 -18.157 1.00 48.94  ? 267 LYS   B CA   1 
ATOM   2410 C  C    . LYS   B 1 256 ? -3.448  -28.047 -19.510 1.00 43.32  ? 267 LYS   B C    1 
ATOM   2411 O  O    . LYS   B 1 256 ? -2.558  -28.718 -20.044 1.00 49.25  ? 267 LYS   B O    1 
ATOM   2412 C  CB   . LYS   B 1 256 ? -3.323  -28.434 -17.041 1.00 47.16  ? 267 LYS   B CB   1 
ATOM   2413 C  CG   . LYS   B 1 256 ? -2.873  -27.925 -15.679 1.00 57.01  ? 267 LYS   B CG   1 
ATOM   2414 C  CD   . LYS   B 1 256 ? -3.088  -28.969 -14.587 1.00 52.31  ? 267 LYS   B CD   1 
ATOM   2415 C  CE   . LYS   B 1 256 ? -2.593  -28.463 -13.240 1.00 64.47  ? 267 LYS   B CE   1 
ATOM   2416 N  NZ   . LYS   B 1 256 ? -2.724  -29.482 -12.164 1.00 73.49  ? 267 LYS   B NZ   1 
ATOM   2417 N  N    . LYS   B 1 257 ? -4.654  -27.876 -20.056 1.00 41.67  ? 268 LYS   B N    1 
ATOM   2418 C  CA   . LYS   B 1 257 ? -5.018  -28.312 -21.399 1.00 46.18  ? 268 LYS   B CA   1 
ATOM   2419 C  C    . LYS   B 1 257 ? -4.695  -27.275 -22.462 1.00 43.43  ? 268 LYS   B C    1 
ATOM   2420 O  O    . LYS   B 1 257 ? -4.346  -27.633 -23.587 1.00 40.88  ? 268 LYS   B O    1 
ATOM   2421 C  CB   . LYS   B 1 257 ? -6.516  -28.605 -21.476 1.00 47.35  ? 268 LYS   B CB   1 
ATOM   2422 C  CG   . LYS   B 1 257 ? -6.981  -29.850 -20.759 1.00 48.67  ? 268 LYS   B CG   1 
ATOM   2423 C  CD   . LYS   B 1 257 ? -8.439  -30.074 -21.105 1.00 58.66  ? 268 LYS   B CD   1 
ATOM   2424 C  CE   . LYS   B 1 257 ? -9.086  -31.088 -20.202 1.00 53.69  ? 268 LYS   B CE   1 
ATOM   2425 N  NZ   . LYS   B 1 257 ? -10.565 -31.090 -20.406 1.00 72.00  ? 268 LYS   B NZ   1 
ATOM   2426 N  N    . LYS   B 1 258 ? -4.774  -25.995 -22.113 1.00 43.51  ? 269 LYS   B N    1 
ATOM   2427 C  CA   . LYS   B 1 258 ? -4.643  -24.916 -23.083 1.00 40.56  ? 269 LYS   B CA   1 
ATOM   2428 C  C    . LYS   B 1 258 ? -3.195  -24.530 -23.338 1.00 34.63  ? 269 LYS   B C    1 
ATOM   2429 O  O    . LYS   B 1 258 ? -2.899  -23.939 -24.383 1.00 33.95  ? 269 LYS   B O    1 
ATOM   2430 C  CB   . LYS   B 1 258 ? -5.436  -23.704 -22.576 1.00 41.53  ? 269 LYS   B CB   1 
ATOM   2431 C  CG   . LYS   B 1 258 ? -5.470  -22.478 -23.484 1.00 52.70  ? 269 LYS   B CG   1 
ATOM   2432 C  CD   . LYS   B 1 258 ? -6.357  -21.388 -22.880 1.00 51.90  ? 269 LYS   B CD   1 
ATOM   2433 C  CE   . LYS   B 1 258 ? -6.372  -20.119 -23.727 1.00 50.42  ? 269 LYS   B CE   1 
ATOM   2434 N  NZ   . LYS   B 1 258 ? -7.118  -20.287 -25.008 1.00 53.68  ? 269 LYS   B NZ   1 
ATOM   2435 N  N    . TYR   B 1 259 ? -2.290  -24.856 -22.418 1.00 34.59  ? 270 TYR   B N    1 
ATOM   2436 C  CA   . TYR   B 1 259 ? -0.895  -24.442 -22.488 1.00 33.76  ? 270 TYR   B CA   1 
ATOM   2437 C  C    . TYR   B 1 259 ? -0.000  -25.664 -22.333 1.00 34.16  ? 270 TYR   B C    1 
ATOM   2438 O  O    . TYR   B 1 259 ? -0.353  -26.617 -21.639 1.00 35.66  ? 270 TYR   B O    1 
ATOM   2439 C  CB   . TYR   B 1 259 ? -0.563  -23.388 -21.398 1.00 33.36  ? 270 TYR   B CB   1 
ATOM   2440 C  CG   . TYR   B 1 259 ? -1.382  -22.119 -21.541 1.00 34.21  ? 270 TYR   B CG   1 
ATOM   2441 C  CD1  . TYR   B 1 259 ? -1.065  -21.188 -22.516 1.00 32.11  ? 270 TYR   B CD1  1 
ATOM   2442 C  CD2  . TYR   B 1 259 ? -2.480  -21.860 -20.714 1.00 36.08  ? 270 TYR   B CD2  1 
ATOM   2443 C  CE1  . TYR   B 1 259 ? -1.811  -20.035 -22.681 1.00 37.59  ? 270 TYR   B CE1  1 
ATOM   2444 C  CE2  . TYR   B 1 259 ? -3.232  -20.700 -20.869 1.00 39.78  ? 270 TYR   B CE2  1 
ATOM   2445 C  CZ   . TYR   B 1 259 ? -2.880  -19.791 -21.855 1.00 36.31  ? 270 TYR   B CZ   1 
ATOM   2446 O  OH   . TYR   B 1 259 ? -3.602  -18.637 -22.034 1.00 54.62  ? 270 TYR   B OH   1 
ATOM   2447 N  N    . THR   B 1 260 ? 1.167   -25.629 -22.979 1.00 33.55  ? 271 THR   B N    1 
ATOM   2448 C  CA   . THR   B 1 260 ? 2.122   -26.724 -22.874 1.00 38.02  ? 271 THR   B CA   1 
ATOM   2449 C  C    . THR   B 1 260 ? 3.537   -26.153 -22.813 1.00 43.50  ? 271 THR   B C    1 
ATOM   2450 O  O    . THR   B 1 260 ? 3.744   -24.937 -22.911 1.00 36.38  ? 271 THR   B O    1 
ATOM   2451 C  CB   . THR   B 1 260 ? 1.967   -27.712 -24.039 1.00 38.13  ? 271 THR   B CB   1 
ATOM   2452 O  OG1  . THR   B 1 260 ? 2.753   -28.881 -23.778 1.00 37.94  ? 271 THR   B OG1  1 
ATOM   2453 C  CG2  . THR   B 1 260 ? 2.425   -27.076 -25.345 1.00 37.77  ? 271 THR   B CG2  1 
ATOM   2454 N  N    A ARG   B 1 261 ? 4.518   -27.043 -22.649 0.50 40.18  ? 272 ARG   B N    1 
ATOM   2455 N  N    B ARG   B 1 261 ? 4.509   -27.058 -22.669 0.50 40.17  ? 272 ARG   B N    1 
ATOM   2456 C  CA   A ARG   B 1 261 ? 5.928   -26.664 -22.526 0.50 40.47  ? 272 ARG   B CA   1 
ATOM   2457 C  CA   B ARG   B 1 261 ? 5.926   -26.734 -22.480 0.50 40.47  ? 272 ARG   B CA   1 
ATOM   2458 C  C    A ARG   B 1 261 ? 6.138   -25.653 -21.397 0.50 39.96  ? 272 ARG   B C    1 
ATOM   2459 C  C    B ARG   B 1 261 ? 6.117   -25.666 -21.404 0.50 39.95  ? 272 ARG   B C    1 
ATOM   2460 O  O    A ARG   B 1 261 ? 6.698   -24.571 -21.594 0.50 43.40  ? 272 ARG   B O    1 
ATOM   2461 O  O    B ARG   B 1 261 ? 6.640   -24.576 -21.643 0.50 43.40  ? 272 ARG   B O    1 
ATOM   2462 C  CB   A ARG   B 1 261 ? 6.478   -26.116 -23.850 0.50 40.07  ? 272 ARG   B CB   1 
ATOM   2463 C  CB   B ARG   B 1 261 ? 6.588   -26.315 -23.794 0.50 40.39  ? 272 ARG   B CB   1 
ATOM   2464 C  CG   A ARG   B 1 261 ? 6.865   -27.176 -24.880 0.50 45.68  ? 272 ARG   B CG   1 
ATOM   2465 C  CG   B ARG   B 1 261 ? 7.435   -27.425 -24.415 0.50 47.67  ? 272 ARG   B CG   1 
ATOM   2466 C  CD   A ARG   B 1 261 ? 8.032   -26.701 -25.744 0.50 41.80  ? 272 ARG   B CD   1 
ATOM   2467 C  CD   B ARG   B 1 261 ? 6.901   -27.802 -25.774 0.50 44.59  ? 272 ARG   B CD   1 
ATOM   2468 N  NE   A ARG   B 1 261 ? 8.525   -27.753 -26.627 0.50 48.66  ? 272 ARG   B NE   1 
ATOM   2469 N  NE   B ARG   B 1 261 ? 7.273   -29.147 -26.203 0.50 37.99  ? 272 ARG   B NE   1 
ATOM   2470 C  CZ   A ARG   B 1 261 ? 9.642   -27.674 -27.339 0.50 46.38  ? 272 ARG   B CZ   1 
ATOM   2471 C  CZ   B ARG   B 1 261 ? 8.318   -29.428 -26.969 0.50 44.62  ? 272 ARG   B CZ   1 
ATOM   2472 N  NH1  A ARG   B 1 261 ? 10.423  -26.607 -27.280 0.50 42.76  ? 272 ARG   B NH1  1 
ATOM   2473 N  NH1  B ARG   B 1 261 ? 9.172   -28.490 -27.343 0.50 44.23  ? 272 ARG   B NH1  1 
ATOM   2474 N  NH2  A ARG   B 1 261 ? 9.982   -28.690 -28.130 0.50 48.95  ? 272 ARG   B NH2  1 
ATOM   2475 N  NH2  B ARG   B 1 261 ? 8.505   -30.681 -27.379 0.50 43.18  ? 272 ARG   B NH2  1 
ATOM   2476 N  N    . PHE   B 1 262 ? 5.681   -26.013 -20.198 1.00 34.47  ? 273 PHE   B N    1 
ATOM   2477 C  CA   . PHE   B 1 262 ? 5.893   -25.155 -19.038 1.00 45.39  ? 273 PHE   B CA   1 
ATOM   2478 C  C    . PHE   B 1 262 ? 7.367   -25.157 -18.650 1.00 47.86  ? 273 PHE   B C    1 
ATOM   2479 O  O    . PHE   B 1 262 ? 7.978   -26.219 -18.499 1.00 40.55  ? 273 PHE   B O    1 
ATOM   2480 C  CB   . PHE   B 1 262 ? 5.034   -25.620 -17.857 1.00 40.87  ? 273 PHE   B CB   1 
ATOM   2481 C  CG   . PHE   B 1 262 ? 3.584   -25.236 -17.966 1.00 38.41  ? 273 PHE   B CG   1 
ATOM   2482 C  CD1  . PHE   B 1 262 ? 2.713   -25.969 -18.759 1.00 42.62  ? 273 PHE   B CD1  1 
ATOM   2483 C  CD2  . PHE   B 1 262 ? 3.094   -24.141 -17.270 1.00 44.14  ? 273 PHE   B CD2  1 
ATOM   2484 C  CE1  . PHE   B 1 262 ? 1.375   -25.614 -18.860 1.00 47.33  ? 273 PHE   B CE1  1 
ATOM   2485 C  CE2  . PHE   B 1 262 ? 1.757   -23.776 -17.362 1.00 38.02  ? 273 PHE   B CE2  1 
ATOM   2486 C  CZ   . PHE   B 1 262 ? 0.895   -24.512 -18.154 1.00 36.68  ? 273 PHE   B CZ   1 
ATOM   2487 N  N    . GLU   B 1 263 ? 7.934   -23.966 -18.469 1.00 45.22  ? 274 GLU   B N    1 
ATOM   2488 C  CA   . GLU   B 1 263 ? 9.343   -23.809 -18.121 1.00 49.21  ? 274 GLU   B CA   1 
ATOM   2489 C  C    . GLU   B 1 263 ? 9.475   -22.722 -17.071 1.00 48.08  ? 274 GLU   B C    1 
ATOM   2490 O  O    . GLU   B 1 263 ? 9.049   -21.585 -17.301 1.00 46.79  ? 274 GLU   B O    1 
ATOM   2491 C  CB   . GLU   B 1 263 ? 10.175  -23.436 -19.355 1.00 49.64  ? 274 GLU   B CB   1 
ATOM   2492 C  CG   . GLU   B 1 263 ? 11.667  -23.310 -19.088 1.00 69.04  ? 274 GLU   B CG   1 
ATOM   2493 C  CD   . GLU   B 1 263 ? 12.451  -22.872 -20.316 1.00 83.09  ? 274 GLU   B CD   1 
ATOM   2494 O  OE1  . GLU   B 1 263 ? 11.902  -22.100 -21.134 1.00 82.23  ? 274 GLU   B OE1  1 
ATOM   2495 O  OE2  . GLU   B 1 263 ? 13.623  -23.283 -20.452 1.00 92.81  ? 274 GLU   B OE2  1 
ATOM   2496 N  N    . LYS   B 1 264 ? 10.077  -23.056 -15.932 1.00 50.89  ? 275 LYS   B N    1 
ATOM   2497 C  CA   . LYS   B 1 264 ? 10.245  -22.064 -14.880 1.00 50.08  ? 275 LYS   B CA   1 
ATOM   2498 C  C    . LYS   B 1 264 ? 11.340  -21.087 -15.289 1.00 55.26  ? 275 LYS   B C    1 
ATOM   2499 O  O    . LYS   B 1 264 ? 12.408  -21.496 -15.751 1.00 61.37  ? 275 LYS   B O    1 
ATOM   2500 C  CB   . LYS   B 1 264 ? 10.584  -22.740 -13.555 1.00 55.68  ? 275 LYS   B CB   1 
ATOM   2501 C  CG   . LYS   B 1 264 ? 10.760  -21.775 -12.395 1.00 59.56  ? 275 LYS   B CG   1 
ATOM   2502 C  CD   . LYS   B 1 264 ? 11.128  -22.513 -11.115 1.00 65.03  ? 275 LYS   B CD   1 
ATOM   2503 C  CE   . LYS   B 1 264 ? 10.068  -23.551 -10.753 1.00 70.56  ? 275 LYS   B CE   1 
ATOM   2504 N  NZ   . LYS   B 1 264 ? 10.397  -24.298 -9.506  1.00 76.93  ? 275 LYS   B NZ   1 
ATOM   2505 N  N    . ILE   B 1 265 ? 11.068  -19.790 -15.140 1.00 56.00  ? 276 ILE   B N    1 
ATOM   2506 C  CA   . ILE   B 1 265 ? 12.031  -18.752 -15.486 1.00 57.51  ? 276 ILE   B CA   1 
ATOM   2507 C  C    . ILE   B 1 265 ? 12.307  -17.799 -14.337 1.00 68.48  ? 276 ILE   B C    1 
ATOM   2508 O  O    . ILE   B 1 265 ? 13.051  -16.832 -14.516 1.00 67.79  ? 276 ILE   B O    1 
ATOM   2509 C  CB   . ILE   B 1 265 ? 11.589  -17.961 -16.735 1.00 55.84  ? 276 ILE   B CB   1 
ATOM   2510 C  CG1  . ILE   B 1 265 ? 10.295  -17.196 -16.455 1.00 49.45  ? 276 ILE   B CG1  1 
ATOM   2511 C  CG2  . ILE   B 1 265 ? 11.426  -18.892 -17.925 1.00 46.82  ? 276 ILE   B CG2  1 
ATOM   2512 C  CD1  . ILE   B 1 265 ? 9.991   -16.121 -17.465 1.00 43.09  ? 276 ILE   B CD1  1 
ATOM   2513 N  N    . GLY   B 1 266 ? 11.719  -18.026 -13.168 1.00 53.55  ? 277 GLY   B N    1 
ATOM   2514 C  CA   . GLY   B 1 266 ? 11.940  -17.145 -12.044 1.00 66.97  ? 277 GLY   B CA   1 
ATOM   2515 C  C    . GLY   B 1 266 ? 11.029  -17.425 -10.869 1.00 71.40  ? 277 GLY   B C    1 
ATOM   2516 O  O    . GLY   B 1 266 ? 9.948   -18.004 -11.019 1.00 66.52  ? 277 GLY   B O    1 
ATOM   2517 N  N    . GLN   B 1 267 ? 11.462  -17.000 -9.687  1.00 83.61  ? 278 GLN   B N    1 
ATOM   2518 C  CA   . GLN   B 1 267 ? 10.702  -17.168 -8.458  1.00 84.83  ? 278 GLN   B CA   1 
ATOM   2519 C  C    . GLN   B 1 267 ? 10.704  -15.813 -7.772  1.00 90.22  ? 278 GLN   B C    1 
ATOM   2520 O  O    . GLN   B 1 267 ? 11.773  -15.246 -7.523  1.00 87.35  ? 278 GLN   B O    1 
ATOM   2521 C  CB   . GLN   B 1 267 ? 11.333  -18.246 -7.566  1.00 90.38  ? 278 GLN   B CB   1 
ATOM   2522 C  CG   . GLN   B 1 267 ? 10.697  -18.409 -6.199  1.00 95.82  ? 278 GLN   B CG   1 
ATOM   2523 C  CD   . GLN   B 1 267 ? 9.304   -18.997 -6.286  1.00 91.73  ? 278 GLN   B CD   1 
ATOM   2524 O  OE1  . GLN   B 1 267 ? 9.030   -19.837 -7.142  1.00 91.90  ? 278 GLN   B OE1  1 
ATOM   2525 N  NE2  . GLN   B 1 267 ? 8.418   -18.565 -5.395  1.00 93.68  ? 278 GLN   B NE2  1 
ATOM   2526 N  N    . GLY   B 1 268 ? 9.515   -15.292 -7.468  1.00 83.34  ? 279 GLY   B N    1 
ATOM   2527 C  CA   . GLY   B 1 268 ? 9.390   -13.990 -6.851  1.00 82.15  ? 279 GLY   B CA   1 
ATOM   2528 C  C    . GLY   B 1 268 ? 8.527   -14.034 -5.604  1.00 81.94  ? 279 GLY   B C    1 
ATOM   2529 O  O    . GLY   B 1 268 ? 7.960   -15.070 -5.247  1.00 71.27  ? 279 GLY   B O    1 
ATOM   2530 N  N    . ALA   B 1 269 ? 8.455   -12.877 -4.942  1.00 92.15  ? 280 ALA   B N    1 
ATOM   2531 C  CA   . ALA   B 1 269 ? 7.574   -12.747 -3.787  1.00 86.75  ? 280 ALA   B CA   1 
ATOM   2532 C  C    . ALA   B 1 269 ? 6.108   -12.858 -4.181  1.00 87.86  ? 280 ALA   B C    1 
ATOM   2533 O  O    . ALA   B 1 269 ? 5.281   -13.293 -3.372  1.00 97.25  ? 280 ALA   B O    1 
ATOM   2534 C  CB   . ALA   B 1 269 ? 7.835   -11.418 -3.078  1.00 84.67  ? 280 ALA   B CB   1 
ATOM   2535 N  N    . SER   B 1 270 ? 5.770   -12.488 -5.416  1.00 69.11  ? 281 SER   B N    1 
ATOM   2536 C  CA   . SER   B 1 270 ? 4.410   -12.624 -5.923  1.00 75.75  ? 281 SER   B CA   1 
ATOM   2537 C  C    . SER   B 1 270 ? 4.059   -14.048 -6.344  1.00 70.51  ? 281 SER   B C    1 
ATOM   2538 O  O    . SER   B 1 270 ? 2.874   -14.341 -6.526  1.00 72.31  ? 281 SER   B O    1 
ATOM   2539 C  CB   . SER   B 1 270 ? 4.190   -11.658 -7.093  1.00 71.59  ? 281 SER   B CB   1 
ATOM   2540 O  OG   . SER   B 1 270 ? 5.290   -11.666 -7.989  1.00 61.46  ? 281 SER   B OG   1 
ATOM   2541 N  N    . GLY   B 1 271 ? 5.044   -14.926 -6.522  1.00 66.52  ? 282 GLY   B N    1 
ATOM   2542 C  CA   . GLY   B 1 271 ? 4.813   -16.303 -6.899  1.00 56.99  ? 282 GLY   B CA   1 
ATOM   2543 C  C    . GLY   B 1 271 ? 5.863   -16.780 -7.883  1.00 62.40  ? 282 GLY   B C    1 
ATOM   2544 O  O    . GLY   B 1 271 ? 6.888   -16.133 -8.095  1.00 65.40  ? 282 GLY   B O    1 
ATOM   2545 N  N    . THR   B 1 272 ? 5.587   -17.926 -8.503  1.00 52.01  ? 283 THR   B N    1 
ATOM   2546 C  CA   . THR   B 1 272 ? 6.494   -18.554 -9.457  1.00 60.09  ? 283 THR   B CA   1 
ATOM   2547 C  C    . THR   B 1 272 ? 6.042   -18.233 -10.875 1.00 51.54  ? 283 THR   B C    1 
ATOM   2548 O  O    . THR   B 1 272 ? 4.850   -18.322 -11.187 1.00 47.40  ? 283 THR   B O    1 
ATOM   2549 C  CB   . THR   B 1 272 ? 6.545   -20.072 -9.259  1.00 59.44  ? 283 THR   B CB   1 
ATOM   2550 O  OG1  . THR   B 1 272 ? 6.775   -20.369 -7.878  1.00 61.79  ? 283 THR   B OG1  1 
ATOM   2551 C  CG2  . THR   B 1 272 ? 7.669   -20.677 -10.086 1.00 58.62  ? 283 THR   B CG2  1 
ATOM   2552 N  N    . VAL   B 1 273 ? 6.993   -17.863 -11.728 1.00 45.72  ? 284 VAL   B N    1 
ATOM   2553 C  CA   . VAL   B 1 273 ? 6.705   -17.448 -13.094 1.00 45.42  ? 284 VAL   B CA   1 
ATOM   2554 C  C    . VAL   B 1 273 ? 7.238   -18.505 -14.049 1.00 49.21  ? 284 VAL   B C    1 
ATOM   2555 O  O    . VAL   B 1 273 ? 8.413   -18.886 -13.971 1.00 46.67  ? 284 VAL   B O    1 
ATOM   2556 C  CB   . VAL   B 1 273 ? 7.313   -16.068 -13.401 1.00 45.62  ? 284 VAL   B CB   1 
ATOM   2557 C  CG1  . VAL   B 1 273 ? 7.081   -15.691 -14.860 1.00 41.56  ? 284 VAL   B CG1  1 
ATOM   2558 C  CG2  . VAL   B 1 273 ? 6.729   -15.007 -12.466 1.00 49.76  ? 284 VAL   B CG2  1 
ATOM   2559 N  N    . TYR   B 1 274 ? 6.374   -18.972 -14.948 1.00 44.93  ? 285 TYR   B N    1 
ATOM   2560 C  CA   . TYR   B 1 274 ? 6.739   -19.930 -15.980 1.00 38.93  ? 285 TYR   B CA   1 
ATOM   2561 C  C    . TYR   B 1 274 ? 6.546   -19.313 -17.355 1.00 39.02  ? 285 TYR   B C    1 
ATOM   2562 O  O    . TYR   B 1 274 ? 5.778   -18.363 -17.537 1.00 40.72  ? 285 TYR   B O    1 
ATOM   2563 C  CB   . TYR   B 1 274 ? 5.903   -21.215 -15.903 1.00 39.03  ? 285 TYR   B CB   1 
ATOM   2564 C  CG   . TYR   B 1 274 ? 6.098   -22.039 -14.661 1.00 50.22  ? 285 TYR   B CG   1 
ATOM   2565 C  CD1  . TYR   B 1 274 ? 5.482   -21.694 -13.466 1.00 47.32  ? 285 TYR   B CD1  1 
ATOM   2566 C  CD2  . TYR   B 1 274 ? 6.879   -23.189 -14.691 1.00 54.60  ? 285 TYR   B CD2  1 
ATOM   2567 C  CE1  . TYR   B 1 274 ? 5.654   -22.463 -12.328 1.00 53.25  ? 285 TYR   B CE1  1 
ATOM   2568 C  CE2  . TYR   B 1 274 ? 7.056   -23.961 -13.561 1.00 60.09  ? 285 TYR   B CE2  1 
ATOM   2569 C  CZ   . TYR   B 1 274 ? 6.441   -23.594 -12.382 1.00 60.33  ? 285 TYR   B CZ   1 
ATOM   2570 O  OH   . TYR   B 1 274 ? 6.618   -24.364 -11.255 1.00 69.61  ? 285 TYR   B OH   1 
ATOM   2571 N  N    . THR   B 1 275 ? 7.255   -19.863 -18.332 1.00 43.05  ? 286 THR   B N    1 
ATOM   2572 C  CA   . THR   B 1 275 ? 6.879   -19.686 -19.724 1.00 35.59  ? 286 THR   B CA   1 
ATOM   2573 C  C    . THR   B 1 275 ? 6.131   -20.925 -20.186 1.00 35.73  ? 286 THR   B C    1 
ATOM   2574 O  O    . THR   B 1 275 ? 6.318   -22.020 -19.650 1.00 37.89  ? 286 THR   B O    1 
ATOM   2575 C  CB   . THR   B 1 275 ? 8.096   -19.444 -20.621 1.00 41.90  ? 286 THR   B CB   1 
ATOM   2576 O  OG1  . THR   B 1 275 ? 9.044   -20.503 -20.452 1.00 40.19  ? 286 THR   B OG1  1 
ATOM   2577 C  CG2  . THR   B 1 275 ? 8.750   -18.125 -20.267 1.00 43.87  ? 286 THR   B CG2  1 
ATOM   2578 N  N    . ALA   B 1 276 ? 5.273   -20.738 -21.180 1.00 29.25  ? 287 ALA   B N    1 
ATOM   2579 C  CA   . ALA   B 1 276 ? 4.480   -21.830 -21.731 1.00 32.64  ? 287 ALA   B CA   1 
ATOM   2580 C  C    . ALA   B 1 276 ? 4.028   -21.404 -23.119 1.00 32.57  ? 287 ALA   B C    1 
ATOM   2581 O  O    . ALA   B 1 276 ? 4.272   -20.272 -23.539 1.00 30.56  ? 287 ALA   B O    1 
ATOM   2582 C  CB   . ALA   B 1 276 ? 3.294   -22.165 -20.832 1.00 30.53  ? 287 ALA   B CB   1 
ATOM   2583 N  N    . MET   B 1 277 ? 3.337   -22.300 -23.821 1.00 29.55  ? 288 MET   B N    1 
ATOM   2584 C  CA   . MET   B 1 277 ? 2.879   -22.005 -25.171 1.00 29.15  ? 288 MET   B CA   1 
ATOM   2585 C  C    . MET   B 1 277 ? 1.409   -22.372 -25.311 1.00 30.94  ? 288 MET   B C    1 
ATOM   2586 O  O    . MET   B 1 277 ? 0.996   -23.464 -24.905 1.00 33.35  ? 288 MET   B O    1 
ATOM   2587 C  CB   . MET   B 1 277 ? 3.701   -22.763 -26.222 1.00 29.71  ? 288 MET   B CB   1 
ATOM   2588 C  CG   . MET   B 1 277 ? 3.292   -22.424 -27.641 1.00 29.56  ? 288 MET   B CG   1 
ATOM   2589 S  SD   . MET   B 1 277 ? 4.152   -23.416 -28.870 1.00 31.15  ? 288 MET   B SD   1 
ATOM   2590 C  CE   . MET   B 1 277 ? 3.173   -24.907 -28.802 1.00 32.37  ? 288 MET   B CE   1 
ATOM   2591 N  N    . ASP   B 1 278 ? 0.633   -21.468 -25.912 1.00 30.96  ? 289 ASP   B N    1 
ATOM   2592 C  CA   . ASP   B 1 278 ? -0.754  -21.745 -26.269 1.00 35.73  ? 289 ASP   B CA   1 
ATOM   2593 C  C    . ASP   B 1 278 ? -0.819  -22.875 -27.296 1.00 31.42  ? 289 ASP   B C    1 
ATOM   2594 O  O    . ASP   B 1 278 ? -0.246  -22.770 -28.384 1.00 30.94  ? 289 ASP   B O    1 
ATOM   2595 C  CB   . ASP   B 1 278 ? -1.396  -20.467 -26.813 1.00 31.09  ? 289 ASP   B CB   1 
ATOM   2596 C  CG   . ASP   B 1 278 ? -2.888  -20.596 -27.033 1.00 37.76  ? 289 ASP   B CG   1 
ATOM   2597 O  OD1  . ASP   B 1 278 ? -3.340  -21.546 -27.714 1.00 37.54  ? 289 ASP   B OD1  1 
ATOM   2598 O  OD2  . ASP   B 1 278 ? -3.618  -19.725 -26.510 1.00 34.43  ? 289 ASP   B OD2  1 
ATOM   2599 N  N    . VAL   B 1 279 ? -1.535  -23.952 -26.951 1.00 32.56  ? 290 VAL   B N    1 
ATOM   2600 C  CA   . VAL   B 1 279 ? -1.573  -25.148 -27.786 1.00 33.97  ? 290 VAL   B CA   1 
ATOM   2601 C  C    . VAL   B 1 279 ? -2.332  -24.929 -29.095 1.00 34.51  ? 290 VAL   B C    1 
ATOM   2602 O  O    . VAL   B 1 279 ? -2.078  -25.629 -30.090 1.00 35.51  ? 290 VAL   B O    1 
ATOM   2603 C  CB   . VAL   B 1 279 ? -2.186  -26.299 -26.949 1.00 37.10  ? 290 VAL   B CB   1 
ATOM   2604 C  CG1  . VAL   B 1 279 ? -2.884  -27.303 -27.811 1.00 44.30  ? 290 VAL   B CG1  1 
ATOM   2605 C  CG2  . VAL   B 1 279 ? -1.113  -26.964 -26.094 1.00 35.69  ? 290 VAL   B CG2  1 
ATOM   2606 N  N    . ALA   B 1 280 ? -3.257  -23.973 -29.128 1.00 34.12  ? 291 ALA   B N    1 
ATOM   2607 C  CA   . ALA   B 1 280 ? -4.037  -23.730 -30.333 1.00 34.88  ? 291 ALA   B CA   1 
ATOM   2608 C  C    . ALA   B 1 280 ? -3.426  -22.666 -31.241 1.00 33.71  ? 291 ALA   B C    1 
ATOM   2609 O  O    . ALA   B 1 280 ? -3.628  -22.719 -32.459 1.00 34.56  ? 291 ALA   B O    1 
ATOM   2610 C  CB   . ALA   B 1 280 ? -5.462  -23.317 -29.962 1.00 35.59  ? 291 ALA   B CB   1 
ATOM   2611 N  N    . THR   B 1 281 ? -2.707  -21.689 -30.694 1.00 32.05  ? 292 THR   B N    1 
ATOM   2612 C  CA   . THR   B 1 281 ? -2.163  -20.605 -31.508 1.00 32.70  ? 292 THR   B CA   1 
ATOM   2613 C  C    . THR   B 1 281 ? -0.646  -20.550 -31.571 1.00 33.17  ? 292 THR   B C    1 
ATOM   2614 O  O    . THR   B 1 281 ? -0.112  -19.855 -32.444 1.00 35.00  ? 292 THR   B O    1 
ATOM   2615 C  CB   . THR   B 1 281 ? -2.649  -19.240 -30.999 1.00 31.05  ? 292 THR   B CB   1 
ATOM   2616 O  OG1  . THR   B 1 281 ? -2.005  -18.949 -29.749 1.00 31.09  ? 292 THR   B OG1  1 
ATOM   2617 C  CG2  . THR   B 1 281 ? -4.163  -19.255 -30.824 1.00 35.94  ? 292 THR   B CG2  1 
ATOM   2618 N  N    . GLY   B 1 282 ? 0.064   -21.232 -30.678 1.00 31.81  ? 293 GLY   B N    1 
ATOM   2619 C  CA   . GLY   B 1 282 ? 1.509   -21.131 -30.635 1.00 29.59  ? 293 GLY   B CA   1 
ATOM   2620 C  C    . GLY   B 1 282 ? 2.043   -19.895 -29.940 1.00 28.22  ? 293 GLY   B C    1 
ATOM   2621 O  O    . GLY   B 1 282 ? 3.266   -19.710 -29.891 1.00 31.21  ? 293 GLY   B O    1 
ATOM   2622 N  N    . GLN   B 1 283 ? 1.175   -19.039 -29.414 1.00 28.75  ? 294 GLN   B N    1 
ATOM   2623 C  CA   . GLN   B 1 283 ? 1.638   -17.869 -28.681 1.00 29.66  ? 294 GLN   B CA   1 
ATOM   2624 C  C    . GLN   B 1 283 ? 2.373   -18.289 -27.418 1.00 32.32  ? 294 GLN   B C    1 
ATOM   2625 O  O    . GLN   B 1 283 ? 1.884   -19.126 -26.648 1.00 29.15  ? 294 GLN   B O    1 
ATOM   2626 C  CB   . GLN   B 1 283 ? 0.463   -16.957 -28.308 1.00 28.03  ? 294 GLN   B CB   1 
ATOM   2627 C  CG   . GLN   B 1 283 ? 0.928   -15.754 -27.470 1.00 34.47  ? 294 GLN   B CG   1 
ATOM   2628 C  CD   . GLN   B 1 283 ? -0.192  -14.778 -27.134 1.00 33.31  ? 294 GLN   B CD   1 
ATOM   2629 O  OE1  . GLN   B 1 283 ? -1.372  -15.113 -27.228 1.00 39.81  ? 294 GLN   B OE1  1 
ATOM   2630 N  NE2  . GLN   B 1 283 ? 0.181   -13.553 -26.756 1.00 40.05  ? 294 GLN   B NE2  1 
ATOM   2631 N  N    . GLU   B 1 284 ? 3.542   -17.694 -27.199 1.00 27.14  ? 295 GLU   B N    1 
ATOM   2632 C  CA   . GLU   B 1 284 ? 4.252   -17.853 -25.940 1.00 27.36  ? 295 GLU   B CA   1 
ATOM   2633 C  C    . GLU   B 1 284 ? 3.643   -16.952 -24.879 1.00 30.05  ? 295 GLU   B C    1 
ATOM   2634 O  O    . GLU   B 1 284 ? 3.245   -15.817 -25.158 1.00 28.15  ? 295 GLU   B O    1 
ATOM   2635 C  CB   . GLU   B 1 284 ? 5.747   -17.563 -26.111 1.00 29.06  ? 295 GLU   B CB   1 
ATOM   2636 C  CG   . GLU   B 1 284 ? 6.419   -18.519 -27.113 1.00 34.10  ? 295 GLU   B CG   1 
ATOM   2637 C  CD   . GLU   B 1 284 ? 7.903   -18.248 -27.351 1.00 44.39  ? 295 GLU   B CD   1 
ATOM   2638 O  OE1  . GLU   B 1 284 ? 8.432   -17.220 -26.887 1.00 41.93  ? 295 GLU   B OE1  1 
ATOM   2639 O  OE2  . GLU   B 1 284 ? 8.557   -19.104 -27.978 1.00 68.03  ? 295 GLU   B OE2  1 
ATOM   2640 N  N    . VAL   B 1 285 ? 3.542   -17.480 -23.659 1.00 29.00  ? 296 VAL   B N    1 
ATOM   2641 C  CA   . VAL   B 1 285 ? 2.923   -16.760 -22.557 1.00 28.01  ? 296 VAL   B CA   1 
ATOM   2642 C  C    . VAL   B 1 285 ? 3.807   -16.871 -21.326 1.00 33.54  ? 296 VAL   B C    1 
ATOM   2643 O  O    . VAL   B 1 285 ? 4.645   -17.766 -21.205 1.00 30.24  ? 296 VAL   B O    1 
ATOM   2644 C  CB   . VAL   B 1 285 ? 1.500   -17.268 -22.227 1.00 30.39  ? 296 VAL   B CB   1 
ATOM   2645 C  CG1  . VAL   B 1 285 ? 0.556   -17.057 -23.403 1.00 27.29  ? 296 VAL   B CG1  1 
ATOM   2646 C  CG2  . VAL   B 1 285 ? 1.529   -18.757 -21.794 1.00 30.47  ? 296 VAL   B CG2  1 
ATOM   2647 N  N    . ALA   B 1 286 ? 3.617   -15.922 -20.416 1.00 29.23  ? 297 ALA   B N    1 
ATOM   2648 C  CA   . ALA   B 1 286 ? 4.211   -15.955 -19.089 1.00 35.23  ? 297 ALA   B CA   1 
ATOM   2649 C  C    . ALA   B 1 286 ? 3.091   -16.193 -18.084 1.00 30.59  ? 297 ALA   B C    1 
ATOM   2650 O  O    . ALA   B 1 286 ? 2.055   -15.522 -18.143 1.00 29.21  ? 297 ALA   B O    1 
ATOM   2651 C  CB   . ALA   B 1 286 ? 4.945   -14.647 -18.785 1.00 32.80  ? 297 ALA   B CB   1 
ATOM   2652 N  N    . ILE   B 1 287 ? 3.285   -17.153 -17.180 1.00 30.29  ? 298 ILE   B N    1 
ATOM   2653 C  CA   . ILE   B 1 287 ? 2.253   -17.540 -16.225 1.00 31.86  ? 298 ILE   B CA   1 
ATOM   2654 C  C    . ILE   B 1 287 ? 2.831   -17.433 -14.823 1.00 39.84  ? 298 ILE   B C    1 
ATOM   2655 O  O    . ILE   B 1 287 ? 3.823   -18.100 -14.501 1.00 37.12  ? 298 ILE   B O    1 
ATOM   2656 C  CB   . ILE   B 1 287 ? 1.723   -18.962 -16.483 1.00 34.14  ? 298 ILE   B CB   1 
ATOM   2657 C  CG1  . ILE   B 1 287 ? 1.199   -19.082 -17.920 1.00 32.28  ? 298 ILE   B CG1  1 
ATOM   2658 C  CG2  . ILE   B 1 287 ? 0.637   -19.317 -15.468 1.00 36.62  ? 298 ILE   B CG2  1 
ATOM   2659 C  CD1  . ILE   B 1 287 ? 0.566   -20.449 -18.223 1.00 32.83  ? 298 ILE   B CD1  1 
ATOM   2660 N  N    . LYS   B 1 288 ? 2.214   -16.604 -13.993 1.00 33.85  ? 299 LYS   B N    1 
ATOM   2661 C  CA   . LYS   B 1 288 ? 2.613   -16.472 -12.603 1.00 40.17  ? 299 LYS   B CA   1 
ATOM   2662 C  C    . LYS   B 1 288 ? 1.628   -17.254 -11.752 1.00 43.87  ? 299 LYS   B C    1 
ATOM   2663 O  O    . LYS   B 1 288 ? 0.414   -17.038 -11.837 1.00 39.50  ? 299 LYS   B O    1 
ATOM   2664 C  CB   . LYS   B 1 288 ? 2.651   -15.003 -12.173 1.00 37.53  ? 299 LYS   B CB   1 
ATOM   2665 C  CG   . LYS   B 1 288 ? 3.193   -14.789 -10.747 1.00 44.00  ? 299 LYS   B CG   1 
ATOM   2666 C  CD   . LYS   B 1 288 ? 3.155   -13.320 -10.305 1.00 50.14  ? 299 LYS   B CD   1 
ATOM   2667 C  CE   . LYS   B 1 288 ? 4.164   -12.459 -11.066 1.00 49.96  ? 299 LYS   B CE   1 
ATOM   2668 N  NZ   . LYS   B 1 288 ? 4.006   -10.999 -10.745 1.00 44.12  ? 299 LYS   B NZ   1 
ATOM   2669 N  N    . GLN   B 1 289 ? 2.152   -18.148 -10.928 1.00 45.28  ? 300 GLN   B N    1 
ATOM   2670 C  CA   . GLN   B 1 289 ? 1.337   -18.982 -10.065 1.00 47.78  ? 300 GLN   B CA   1 
ATOM   2671 C  C    . GLN   B 1 289 ? 1.485   -18.473 -8.646  1.00 52.62  ? 300 GLN   B C    1 
ATOM   2672 O  O    . GLN   B 1 289 ? 2.600   -18.407 -8.119  1.00 61.60  ? 300 GLN   B O    1 
ATOM   2673 C  CB   . GLN   B 1 289 ? 1.760   -20.447 -10.155 1.00 57.65  ? 300 GLN   B CB   1 
ATOM   2674 C  CG   . GLN   B 1 289 ? 1.907   -20.950 -11.575 1.00 51.54  ? 300 GLN   B CG   1 
ATOM   2675 C  CD   . GLN   B 1 289 ? 2.318   -22.417 -11.645 1.00 63.68  ? 300 GLN   B CD   1 
ATOM   2676 O  OE1  . GLN   B 1 289 ? 2.845   -22.983 -10.682 1.00 66.70  ? 300 GLN   B OE1  1 
ATOM   2677 N  NE2  . GLN   B 1 289 ? 2.077   -23.037 -12.792 1.00 59.16  ? 300 GLN   B NE2  1 
ATOM   2678 N  N    . MET   B 1 290 ? 0.339   -18.076 -8.092  1.00 54.86  ? 301 MET   B N    1 
ATOM   2679 C  CA   . MET   B 1 290 ? 0.309   -17.533 -6.714  1.00 69.40  ? 301 MET   B CA   1 
ATOM   2680 C  C    . MET   B 1 290 ? -0.824  -18.178 -5.909  1.00 71.18  ? 301 MET   B C    1 
ATOM   2681 O  O    . MET   B 1 290 ? -1.957  -18.215 -6.400  1.00 70.64  ? 301 MET   B O    1 
ATOM   2682 C  CB   . MET   B 1 290 ? 0.109   -16.016 -6.737  1.00 60.59  ? 301 MET   B CB   1 
ATOM   2683 C  CG   . MET   B 1 290 ? -0.957  -15.531 -7.682  1.00 66.46  ? 301 MET   B CG   1 
ATOM   2684 S  SD   . MET   B 1 290 ? -0.578  -13.826 -8.131  1.00 91.24  ? 301 MET   B SD   1 
ATOM   2685 C  CE   . MET   B 1 290 ? -2.124  -13.315 -8.875  1.00 75.97  ? 301 MET   B CE   1 
ATOM   2686 N  N    . ASN   B 1 291 ? -0.506  -18.682 -4.723  1.00 83.06  ? 302 ASN   B N    1 
ATOM   2687 C  CA   . ASN   B 1 291 ? -1.552  -19.229 -3.827  1.00 94.57  ? 302 ASN   B CA   1 
ATOM   2688 C  C    . ASN   B 1 291 ? -2.256  -18.048 -3.173  1.00 102.97 ? 302 ASN   B C    1 
ATOM   2689 O  O    . ASN   B 1 291 ? -1.684  -17.452 -2.250  1.00 104.93 ? 302 ASN   B O    1 
ATOM   2690 C  CB   . ASN   B 1 291 ? -0.964  -20.143 -2.755  1.00 103.85 ? 302 ASN   B CB   1 
ATOM   2691 C  CG   . ASN   B 1 291 ? 0.370   -19.658 -2.232  1.00 112.21 ? 302 ASN   B CG   1 
ATOM   2692 O  OD1  . ASN   B 1 291 ? 0.905   -18.661 -2.710  1.00 111.87 ? 302 ASN   B OD1  1 
ATOM   2693 N  ND2  . ASN   B 1 291 ? 0.917   -20.360 -1.254  1.00 110.17 ? 302 ASN   B ND2  1 
ATOM   2694 N  N    . LEU   B 1 292 ? -3.446  -17.719 -3.662  1.00 98.98  ? 303 LEU   B N    1 
ATOM   2695 C  CA   . LEU   B 1 292 ? -4.203  -16.578 -3.112  1.00 105.36 ? 303 LEU   B CA   1 
ATOM   2696 C  C    . LEU   B 1 292 ? -4.910  -17.447 -2.077  1.00 114.92 ? 303 LEU   B C    1 
ATOM   2697 O  O    . LEU   B 1 292 ? -6.090  -17.772 -2.278  1.00 112.59 ? 303 LEU   B O    1 
ATOM   2698 C  CB   . LEU   B 1 292 ? -5.414  -16.354 -4.020  1.00 95.39  ? 303 LEU   B CB   1 
ATOM   2699 C  CG   . LEU   B 1 292 ? -5.814  -14.899 -4.248  1.00 92.06  ? 303 LEU   B CG   1 
ATOM   2700 C  CD1  . LEU   B 1 292 ? -4.641  -14.095 -4.789  1.00 87.55  ? 303 LEU   B CD1  1 
ATOM   2701 C  CD2  . LEU   B 1 292 ? -6.999  -14.814 -5.196  1.00 82.65  ? 303 LEU   B CD2  1 
ATOM   2702 N  N    . GLN   B 1 293 ? -4.195  -17.804 -1.013  1.00 134.31 ? 304 GLN   B N    1 
ATOM   2703 C  CA   . GLN   B 1 293 ? -4.763  -18.742 -0.010  1.00 145.51 ? 304 GLN   B CA   1 
ATOM   2704 C  C    . GLN   B 1 293 ? -4.343  -17.792 1.112   1.00 144.60 ? 304 GLN   B C    1 
ATOM   2705 O  O    . GLN   B 1 293 ? -3.210  -17.933 1.603   1.00 140.92 ? 304 GLN   B O    1 
ATOM   2706 C  CB   . GLN   B 1 293 ? -4.253  -20.169 0.222   1.00 139.80 ? 304 GLN   B CB   1 
ATOM   2707 N  N    . GLN   B 1 294 ? -5.220  -16.855 1.471   1.00 132.92 ? 305 GLN   B N    1 
ATOM   2708 C  CA   . GLN   B 1 294 ? -4.969  -15.949 2.621   1.00 132.38 ? 305 GLN   B CA   1 
ATOM   2709 C  C    . GLN   B 1 294 ? -3.613  -15.247 2.517   1.00 134.82 ? 305 GLN   B C    1 
ATOM   2710 O  O    . GLN   B 1 294 ? -3.110  -14.816 3.567   1.00 138.41 ? 305 GLN   B O    1 
ATOM   2711 C  CB   . GLN   B 1 294 ? -5.054  -16.725 3.937   1.00 133.07 ? 305 GLN   B CB   1 
ATOM   2712 C  CG   . GLN   B 1 294 ? -6.429  -17.314 4.216   1.00 131.95 ? 305 GLN   B CG   1 
ATOM   2713 C  CD   . GLN   B 1 294 ? -7.483  -16.258 4.442   1.00 140.30 ? 305 GLN   B CD   1 
ATOM   2714 O  OE1  . GLN   B 1 294 ? -7.210  -15.059 4.407   1.00 144.37 ? 305 GLN   B OE1  1 
ATOM   2715 N  NE2  . GLN   B 1 294 ? -8.707  -16.700 4.680   1.00 136.27 ? 305 GLN   B NE2  1 
ATOM   2716 N  N    . GLN   B 1 295 ? -3.033  -15.138 1.323   1.00 136.84 ? 306 GLN   B N    1 
ATOM   2717 C  CA   . GLN   B 1 295 ? -1.796  -14.321 1.220   1.00 136.70 ? 306 GLN   B CA   1 
ATOM   2718 C  C    . GLN   B 1 295 ? -2.206  -12.891 1.566   1.00 137.90 ? 306 GLN   B C    1 
ATOM   2719 O  O    . GLN   B 1 295 ? -3.218  -12.423 1.016   1.00 133.57 ? 306 GLN   B O    1 
ATOM   2720 C  CB   . GLN   B 1 295 ? -1.160  -14.388 -0.166  1.00 123.45 ? 306 GLN   B CB   1 
ATOM   2721 N  N    . PRO   B 1 296 ? -1.477  -12.189 2.454   1.00 142.26 ? 307 PRO   B N    1 
ATOM   2722 C  CA   . PRO   B 1 296 ? -1.872  -10.857 2.905   1.00 142.60 ? 307 PRO   B CA   1 
ATOM   2723 C  C    . PRO   B 1 296 ? -2.477  -9.964  1.825   1.00 143.96 ? 307 PRO   B C    1 
ATOM   2724 O  O    . PRO   B 1 296 ? -1.875  -9.864  0.773   1.00 142.75 ? 307 PRO   B O    1 
ATOM   2725 C  CB   . PRO   B 1 296 ? -0.501  -10.257 3.245   1.00 148.81 ? 307 PRO   B CB   1 
ATOM   2726 C  CG   . PRO   B 1 296 ? 0.263   -11.419 3.830   1.00 153.85 ? 307 PRO   B CG   1 
ATOM   2727 C  CD   . PRO   B 1 296 ? -0.221  -12.632 3.063   1.00 145.81 ? 307 PRO   B CD   1 
ATOM   2728 N  N    . LYS   B 1 297 ? -3.621  -9.325  2.105   1.00 145.99 ? 308 LYS   B N    1 
ATOM   2729 C  CA   . LYS   B 1 297 ? -4.112  -8.366  1.114   1.00 141.62 ? 308 LYS   B CA   1 
ATOM   2730 C  C    . LYS   B 1 297 ? -4.199  -9.003  -0.275  1.00 134.82 ? 308 LYS   B C    1 
ATOM   2731 O  O    . LYS   B 1 297 ? -3.501  -8.622  -1.221  1.00 123.72 ? 308 LYS   B O    1 
ATOM   2732 C  CB   . LYS   B 1 297 ? -3.249  -7.100  1.099   1.00 138.65 ? 308 LYS   B CB   1 
ATOM   2733 C  CG   . LYS   B 1 297 ? -3.324  -6.301  2.381   1.00 132.43 ? 308 LYS   B CG   1 
ATOM   2734 C  CD   . LYS   B 1 297 ? -4.729  -5.765  2.575   1.00 130.83 ? 308 LYS   B CD   1 
ATOM   2735 C  CE   . LYS   B 1 297 ? -5.054  -4.767  1.476   1.00 125.58 ? 308 LYS   B CE   1 
ATOM   2736 N  NZ   . LYS   B 1 297 ? -4.134  -3.597  1.532   1.00 128.44 ? 308 LYS   B NZ   1 
ATOM   2737 N  N    . LYS   B 1 298 ? -5.072  -10.010 -0.370  1.00 128.01 ? 309 LYS   B N    1 
ATOM   2738 C  CA   . LYS   B 1 298 ? -5.352  -10.631 -1.659  1.00 117.43 ? 309 LYS   B CA   1 
ATOM   2739 C  C    . LYS   B 1 298 ? -6.179  -9.709  -2.546  1.00 110.69 ? 309 LYS   B C    1 
ATOM   2740 O  O    . LYS   B 1 298 ? -6.026  -9.732  -3.772  1.00 104.02 ? 309 LYS   B O    1 
ATOM   2741 C  CB   . LYS   B 1 298 ? -6.067  -11.970 -1.463  1.00 103.06 ? 309 LYS   B CB   1 
ATOM   2742 N  N    . GLU   B 1 299 ? -7.061  -8.900  -1.945  1.00 115.48 ? 310 GLU   B N    1 
ATOM   2743 C  CA   . GLU   B 1 299 ? -7.900  -7.986  -2.720  1.00 114.27 ? 310 GLU   B CA   1 
ATOM   2744 C  C    . GLU   B 1 299 ? -7.086  -7.005  -3.560  1.00 112.62 ? 310 GLU   B C    1 
ATOM   2745 O  O    . GLU   B 1 299 ? -7.510  -6.637  -4.662  1.00 106.96 ? 310 GLU   B O    1 
ATOM   2746 C  CB   . GLU   B 1 299 ? -8.883  -7.243  -1.809  1.00 118.52 ? 310 GLU   B CB   1 
ATOM   2747 C  CG   . GLU   B 1 299 ? -9.831  -8.141  -1.005  1.00 126.12 ? 310 GLU   B CG   1 
ATOM   2748 C  CD   . GLU   B 1 299 ? -9.278  -8.619  0.321   1.00 135.23 ? 310 GLU   B CD   1 
ATOM   2749 O  OE1  . GLU   B 1 299 ? -8.258  -8.071  0.785   1.00 139.88 ? 310 GLU   B OE1  1 
ATOM   2750 O  OE2  . GLU   B 1 299 ? -9.885  -9.540  0.911   1.00 143.29 ? 310 GLU   B OE2  1 
ATOM   2751 N  N    . LEU   B 1 300 ? -5.929  -6.548  -3.067  1.00 119.45 ? 311 LEU   B N    1 
ATOM   2752 C  CA   . LEU   B 1 300 ? -5.120  -5.665  -3.905  1.00 111.15 ? 311 LEU   B CA   1 
ATOM   2753 C  C    . LEU   B 1 300 ? -4.610  -6.409  -5.129  1.00 103.72 ? 311 LEU   B C    1 
ATOM   2754 O  O    . LEU   B 1 300 ? -4.608  -5.867  -6.240  1.00 94.45  ? 311 LEU   B O    1 
ATOM   2755 C  CB   . LEU   B 1 300 ? -3.940  -5.081  -3.127  1.00 117.91 ? 311 LEU   B CB   1 
ATOM   2756 C  CG   . LEU   B 1 300 ? -4.160  -4.060  -2.010  1.00 125.05 ? 311 LEU   B CG   1 
ATOM   2757 C  CD1  . LEU   B 1 300 ? -2.813  -3.550  -1.511  1.00 124.28 ? 311 LEU   B CD1  1 
ATOM   2758 C  CD2  . LEU   B 1 300 ? -5.028  -2.909  -2.494  1.00 124.46 ? 311 LEU   B CD2  1 
ATOM   2759 N  N    . ILE   B 1 301 ? -4.200  -7.662  -4.946  1.00 99.62  ? 312 ILE   B N    1 
ATOM   2760 C  CA   . ILE   B 1 301 ? -3.755  -8.472  -6.072  1.00 93.72  ? 312 ILE   B CA   1 
ATOM   2761 C  C    . ILE   B 1 301 ? -4.913  -8.706  -7.036  1.00 86.87  ? 312 ILE   B C    1 
ATOM   2762 O  O    . ILE   B 1 301 ? -4.752  -8.625  -8.260  1.00 77.54  ? 312 ILE   B O    1 
ATOM   2763 C  CB   . ILE   B 1 301 ? -3.161  -9.793  -5.554  1.00 92.51  ? 312 ILE   B CB   1 
ATOM   2764 C  CG1  . ILE   B 1 301 ? -2.256  -9.522  -4.351  1.00 98.10  ? 312 ILE   B CG1  1 
ATOM   2765 C  CG2  . ILE   B 1 301 ? -2.350  -10.464 -6.635  1.00 80.42  ? 312 ILE   B CG2  1 
ATOM   2766 C  CD1  . ILE   B 1 301 ? -1.917  -10.761 -3.543  1.00 102.21 ? 312 ILE   B CD1  1 
ATOM   2767 N  N    . ILE   B 1 302 ? -6.098  -8.995  -6.493  1.00 88.86  ? 313 ILE   B N    1 
ATOM   2768 C  CA   . ILE   B 1 302 ? -7.285  -9.218  -7.316  1.00 86.76  ? 313 ILE   B CA   1 
ATOM   2769 C  C    . ILE   B 1 302 ? -7.660  -7.951  -8.079  1.00 86.70  ? 313 ILE   B C    1 
ATOM   2770 O  O    . ILE   B 1 302 ? -7.839  -7.974  -9.302  1.00 83.99  ? 313 ILE   B O    1 
ATOM   2771 C  CB   . ILE   B 1 302 ? -8.449  -9.726  -6.445  1.00 87.65  ? 313 ILE   B CB   1 
ATOM   2772 C  CG1  . ILE   B 1 302 ? -8.165  -11.152 -5.960  1.00 90.61  ? 313 ILE   B CG1  1 
ATOM   2773 C  CG2  . ILE   B 1 302 ? -9.759  -9.660  -7.199  1.00 82.41  ? 313 ILE   B CG2  1 
ATOM   2774 C  CD1  . ILE   B 1 302 ? -9.218  -11.703 -5.026  1.00 86.39  ? 313 ILE   B CD1  1 
ATOM   2775 N  N    . ASN   B 1 303 ? -7.795  -6.828  -7.366  1.00 90.63  ? 314 ASN   B N    1 
ATOM   2776 C  CA   . ASN   B 1 303 ? -8.193  -5.582  -8.018  1.00 92.70  ? 314 ASN   B CA   1 
ATOM   2777 C  C    . ASN   B 1 303 ? -7.185  -5.167  -9.083  1.00 82.85  ? 314 ASN   B C    1 
ATOM   2778 O  O    . ASN   B 1 303 ? -7.571  -4.737  -10.177 1.00 73.98  ? 314 ASN   B O    1 
ATOM   2779 C  CB   . ASN   B 1 303 ? -8.361  -4.471  -6.981  1.00 91.77  ? 314 ASN   B CB   1 
ATOM   2780 C  CG   . ASN   B 1 303 ? -9.561  -4.688  -6.080  1.00 101.54 ? 314 ASN   B CG   1 
ATOM   2781 O  OD1  . ASN   B 1 303 ? -10.589 -5.215  -6.507  1.00 107.06 ? 314 ASN   B OD1  1 
ATOM   2782 N  ND2  . ASN   B 1 303 ? -9.436  -4.279  -4.824  1.00 107.39 ? 314 ASN   B ND2  1 
ATOM   2783 N  N    . GLU   B 1 304 ? -5.888  -5.284  -8.776  1.00 86.37  ? 315 GLU   B N    1 
ATOM   2784 C  CA   . GLU   B 1 304 ? -4.846  -5.026  -9.767  1.00 78.02  ? 315 GLU   B CA   1 
ATOM   2785 C  C    . GLU   B 1 304 ? -5.085  -5.808  -11.050 1.00 75.81  ? 315 GLU   B C    1 
ATOM   2786 O  O    . GLU   B 1 304 ? -4.893  -5.285  -12.154 1.00 68.35  ? 315 GLU   B O    1 
ATOM   2787 C  CB   . GLU   B 1 304 ? -3.477  -5.374  -9.181  1.00 87.09  ? 315 GLU   B CB   1 
ATOM   2788 C  CG   . GLU   B 1 304 ? -2.316  -5.280  -10.168 1.00 82.71  ? 315 GLU   B CG   1 
ATOM   2789 C  CD   . GLU   B 1 304 ? -2.011  -3.864  -10.621 1.00 93.06  ? 315 GLU   B CD   1 
ATOM   2790 O  OE1  . GLU   B 1 304 ? -2.508  -2.907  -9.987  1.00 100.85 ? 315 GLU   B OE1  1 
ATOM   2791 O  OE2  . GLU   B 1 304 ? -1.264  -3.711  -11.614 1.00 87.39  ? 315 GLU   B OE2  1 
ATOM   2792 N  N    . ILE   B 1 305 ? -5.488  -7.072  -10.926 1.00 68.89  ? 316 ILE   B N    1 
ATOM   2793 C  CA   . ILE   B 1 305 ? -5.803  -7.857  -12.112 1.00 62.47  ? 316 ILE   B CA   1 
ATOM   2794 C  C    . ILE   B 1 305 ? -7.023  -7.279  -12.817 1.00 60.21  ? 316 ILE   B C    1 
ATOM   2795 O  O    . ILE   B 1 305 ? -7.046  -7.159  -14.048 1.00 59.33  ? 316 ILE   B O    1 
ATOM   2796 C  CB   . ILE   B 1 305 ? -5.994  -9.334  -11.736 1.00 61.01  ? 316 ILE   B CB   1 
ATOM   2797 C  CG1  . ILE   B 1 305 ? -4.671  -9.910  -11.236 1.00 49.63  ? 316 ILE   B CG1  1 
ATOM   2798 C  CG2  . ILE   B 1 305 ? -6.487  -10.121 -12.936 1.00 54.62  ? 316 ILE   B CG2  1 
ATOM   2799 C  CD1  . ILE   B 1 305 ? -4.769  -11.341 -10.786 1.00 65.67  ? 316 ILE   B CD1  1 
ATOM   2800 N  N    . LEU   B 1 306 ? -8.052  -6.907  -12.050 1.00 65.73  ? 317 LEU   B N    1 
ATOM   2801 C  CA   . LEU   B 1 306 ? -9.237  -6.290  -12.642 1.00 75.81  ? 317 LEU   B CA   1 
ATOM   2802 C  C    . LEU   B 1 306 ? -8.867  -5.059  -13.451 1.00 65.47  ? 317 LEU   B C    1 
ATOM   2803 O  O    . LEU   B 1 306 ? -9.379  -4.858  -14.559 1.00 63.41  ? 317 LEU   B O    1 
ATOM   2804 C  CB   . LEU   B 1 306 ? -10.236 -5.894  -11.553 1.00 68.75  ? 317 LEU   B CB   1 
ATOM   2805 C  CG   . LEU   B 1 306 ? -11.158 -6.936  -10.936 1.00 80.21  ? 317 LEU   B CG   1 
ATOM   2806 C  CD1  . LEU   B 1 306 ? -11.987 -6.304  -9.840  1.00 72.21  ? 317 LEU   B CD1  1 
ATOM   2807 C  CD2  . LEU   B 1 306 ? -12.060 -7.494  -12.021 1.00 88.04  ? 317 LEU   B CD2  1 
ATOM   2808 N  N    . VAL   B 1 307 ? -7.970  -4.233  -12.918 1.00 59.04  ? 318 VAL   B N    1 
ATOM   2809 C  CA   . VAL   B 1 307 ? -7.596  -2.999  -13.599 1.00 65.27  ? 318 VAL   B CA   1 
ATOM   2810 C  C    . VAL   B 1 307 ? -6.904  -3.298  -14.927 1.00 54.69  ? 318 VAL   B C    1 
ATOM   2811 O  O    . VAL   B 1 307 ? -7.204  -2.671  -15.949 1.00 58.27  ? 318 VAL   B O    1 
ATOM   2812 C  CB   . VAL   B 1 307 ? -6.719  -2.134  -12.674 1.00 65.88  ? 318 VAL   B CB   1 
ATOM   2813 C  CG1  . VAL   B 1 307 ? -6.150  -0.945  -13.430 1.00 71.32  ? 318 VAL   B CG1  1 
ATOM   2814 C  CG2  . VAL   B 1 307 ? -7.518  -1.675  -11.464 1.00 70.69  ? 318 VAL   B CG2  1 
ATOM   2815 N  N    . MET   B 1 308 ? -5.979  -4.263  -14.942 1.00 53.75  ? 319 MET   B N    1 
ATOM   2816 C  CA   . MET   B 1 308 ? -5.243  -4.539  -16.174 1.00 53.52  ? 319 MET   B CA   1 
ATOM   2817 C  C    . MET   B 1 308 ? -6.157  -5.050  -17.288 1.00 60.85  ? 319 MET   B C    1 
ATOM   2818 O  O    . MET   B 1 308 ? -5.953  -4.704  -18.459 1.00 54.24  ? 319 MET   B O    1 
ATOM   2819 C  CB   . MET   B 1 308 ? -4.083  -5.506  -15.917 1.00 50.98  ? 319 MET   B CB   1 
ATOM   2820 C  CG   . MET   B 1 308 ? -2.986  -4.929  -15.018 1.00 60.37  ? 319 MET   B CG   1 
ATOM   2821 S  SD   . MET   B 1 308 ? -1.378  -5.765  -15.155 1.00 61.76  ? 319 MET   B SD   1 
ATOM   2822 C  CE   . MET   B 1 308 ? -0.794  -5.248  -16.778 1.00 48.71  ? 319 MET   B CE   1 
ATOM   2823 N  N    . ARG   B 1 309 ? -7.159  -5.885  -16.963 1.00 54.40  ? 320 ARG   B N    1 
ATOM   2824 C  CA   . ARG   B 1 309 ? -8.044  -6.365  -18.029 1.00 57.25  ? 320 ARG   B CA   1 
ATOM   2825 C  C    . ARG   B 1 309 ? -8.812  -5.236  -18.691 1.00 58.97  ? 320 ARG   B C    1 
ATOM   2826 O  O    . ARG   B 1 309 ? -9.065  -5.286  -19.899 1.00 57.52  ? 320 ARG   B O    1 
ATOM   2827 C  CB   . ARG   B 1 309 ? -9.075  -7.389  -17.546 1.00 67.40  ? 320 ARG   B CB   1 
ATOM   2828 C  CG   . ARG   B 1 309 ? -8.547  -8.756  -17.313 1.00 70.94  ? 320 ARG   B CG   1 
ATOM   2829 C  CD   . ARG   B 1 309 ? -9.654  -9.821  -17.267 1.00 82.47  ? 320 ARG   B CD   1 
ATOM   2830 N  NE   . ARG   B 1 309 ? -9.048  -11.148 -17.230 1.00 92.95  ? 320 ARG   B NE   1 
ATOM   2831 C  CZ   . ARG   B 1 309 ? -9.687  -12.301 -17.087 1.00 83.76  ? 320 ARG   B CZ   1 
ATOM   2832 N  NH1  . ARG   B 1 309 ? -11.003 -12.354 -16.962 1.00 91.57  ? 320 ARG   B NH1  1 
ATOM   2833 N  NH2  . ARG   B 1 309 ? -8.982  -13.432 -17.065 1.00 68.24  ? 320 ARG   B NH2  1 
ATOM   2834 N  N    . GLU   B 1 310 ? -9.190  -4.221  -17.930 1.00 52.27  ? 321 GLU   B N    1 
ATOM   2835 C  CA   . GLU   B 1 310 ? -10.041 -3.170  -18.455 1.00 63.04  ? 321 GLU   B CA   1 
ATOM   2836 C  C    . GLU   B 1 310 ? -9.249  -2.045  -19.103 1.00 66.35  ? 321 GLU   B C    1 
ATOM   2837 O  O    . GLU   B 1 310 ? -9.840  -1.214  -19.799 1.00 70.53  ? 321 GLU   B O    1 
ATOM   2838 C  CB   . GLU   B 1 310 ? -10.913 -2.606  -17.325 1.00 69.56  ? 321 GLU   B CB   1 
ATOM   2839 C  CG   . GLU   B 1 310 ? -11.824 -3.639  -16.666 1.00 76.26  ? 321 GLU   B CG   1 
ATOM   2840 C  CD   . GLU   B 1 310 ? -12.445 -3.131  -15.370 1.00 103.63 ? 321 GLU   B CD   1 
ATOM   2841 O  OE1  . GLU   B 1 310 ? -12.315 -1.923  -15.077 1.00 107.44 ? 321 GLU   B OE1  1 
ATOM   2842 O  OE2  . GLU   B 1 310 ? -13.047 -3.941  -14.631 1.00 101.54 ? 321 GLU   B OE2  1 
ATOM   2843 N  N    . ASN   B 1 311 ? -7.919  -2.015  -18.916 1.00 53.86  ? 322 ASN   B N    1 
ATOM   2844 C  CA   . ASN   B 1 311 ? -7.096  -0.882  -19.318 1.00 49.81  ? 322 ASN   B CA   1 
ATOM   2845 C  C    . ASN   B 1 311 ? -5.822  -1.377  -20.005 1.00 46.87  ? 322 ASN   B C    1 
ATOM   2846 O  O    . ASN   B 1 311 ? -4.706  -1.237  -19.507 1.00 48.72  ? 322 ASN   B O    1 
ATOM   2847 C  CB   . ASN   B 1 311 ? -6.762  -0.008  -18.113 1.00 47.84  ? 322 ASN   B CB   1 
ATOM   2848 C  CG   . ASN   B 1 311 ? -8.001  0.476   -17.394 1.00 63.15  ? 322 ASN   B CG   1 
ATOM   2849 O  OD1  . ASN   B 1 311 ? -8.610  1.474   -17.779 1.00 66.17  ? 322 ASN   B OD1  1 
ATOM   2850 N  ND2  . ASN   B 1 311 ? -8.392  -0.243  -16.350 1.00 65.81  ? 322 ASN   B ND2  1 
ATOM   2851 N  N    . LYS   B 1 312 ? -5.987  -1.925  -21.198 1.00 46.08  ? 323 LYS   B N    1 
ATOM   2852 C  CA   . LYS   B 1 312 ? -4.856  -2.394  -21.980 1.00 47.10  ? 323 LYS   B CA   1 
ATOM   2853 C  C    . LYS   B 1 312 ? -4.237  -1.251  -22.781 1.00 37.19  ? 323 LYS   B C    1 
ATOM   2854 O  O    . LYS   B 1 312 ? -4.854  -0.203  -23.004 1.00 42.17  ? 323 LYS   B O    1 
ATOM   2855 C  CB   . LYS   B 1 312 ? -5.278  -3.533  -22.899 1.00 50.91  ? 323 LYS   B CB   1 
ATOM   2856 C  CG   . LYS   B 1 312 ? -5.715  -4.757  -22.127 1.00 50.10  ? 323 LYS   B CG   1 
ATOM   2857 C  CD   . LYS   B 1 312 ? -6.025  -5.893  -23.051 1.00 58.79  ? 323 LYS   B CD   1 
ATOM   2858 C  CE   . LYS   B 1 312 ? -6.233  -7.176  -22.282 1.00 49.95  ? 323 LYS   B CE   1 
ATOM   2859 N  NZ   . LYS   B 1 312 ? -6.541  -8.285  -23.220 1.00 58.57  ? 323 LYS   B NZ   1 
ATOM   2860 N  N    . ASN   B 1 313 ? -2.969  -1.441  -23.165 1.00 41.02  ? 324 ASN   B N    1 
ATOM   2861 C  CA   . ASN   B 1 313 ? -2.236  -0.387  -23.855 1.00 32.24  ? 324 ASN   B CA   1 
ATOM   2862 C  C    . ASN   B 1 313 ? -1.113  -1.022  -24.654 1.00 34.56  ? 324 ASN   B C    1 
ATOM   2863 O  O    . ASN   B 1 313 ? -0.502  -1.992  -24.182 1.00 31.35  ? 324 ASN   B O    1 
ATOM   2864 C  CB   . ASN   B 1 313 ? -1.682  0.643   -22.865 1.00 35.77  ? 324 ASN   B CB   1 
ATOM   2865 C  CG   . ASN   B 1 313 ? -0.929  1.761   -23.553 1.00 37.97  ? 324 ASN   B CG   1 
ATOM   2866 O  OD1  . ASN   B 1 313 ? 0.281   1.667   -23.756 1.00 33.84  ? 324 ASN   B OD1  1 
ATOM   2867 N  ND2  . ASN   B 1 313 ? -1.640  2.821   -23.924 1.00 35.10  ? 324 ASN   B ND2  1 
ATOM   2868 N  N    . PRO   B 1 314 ? -0.825  -0.526  -25.856 1.00 34.51  ? 325 PRO   B N    1 
ATOM   2869 C  CA   . PRO   B 1 314 ? 0.212   -1.172  -26.675 1.00 32.39  ? 325 PRO   B CA   1 
ATOM   2870 C  C    . PRO   B 1 314 ? 1.584   -1.218  -26.023 1.00 32.35  ? 325 PRO   B C    1 
ATOM   2871 O  O    . PRO   B 1 314 ? 2.357   -2.135  -26.323 1.00 31.98  ? 325 PRO   B O    1 
ATOM   2872 C  CB   . PRO   B 1 314 ? 0.226   -0.314  -27.950 1.00 37.45  ? 325 PRO   B CB   1 
ATOM   2873 C  CG   . PRO   B 1 314 ? -1.141  0.280   -28.013 1.00 44.84  ? 325 PRO   B CG   1 
ATOM   2874 C  CD   . PRO   B 1 314 ? -1.524  0.545   -26.585 1.00 39.51  ? 325 PRO   B CD   1 
ATOM   2875 N  N    . ASN   B 1 315 ? 1.911   -0.288  -25.120 1.00 29.83  ? 326 ASN   B N    1 
ATOM   2876 C  CA   . ASN   B 1 315 ? 3.233   -0.267  -24.500 1.00 29.87  ? 326 ASN   B CA   1 
ATOM   2877 C  C    . ASN   B 1 315 ? 3.239   -0.844  -23.087 1.00 30.09  ? 326 ASN   B C    1 
ATOM   2878 O  O    . ASN   B 1 315 ? 4.169   -0.582  -22.313 1.00 30.73  ? 326 ASN   B O    1 
ATOM   2879 C  CB   . ASN   B 1 315 ? 3.793   1.147   -24.518 1.00 31.17  ? 326 ASN   B CB   1 
ATOM   2880 C  CG   . ASN   B 1 315 ? 4.168   1.571   -25.912 1.00 35.68  ? 326 ASN   B CG   1 
ATOM   2881 O  OD1  . ASN   B 1 315 ? 3.583   2.498   -26.466 1.00 31.87  ? 326 ASN   B OD1  1 
ATOM   2882 N  ND2  . ASN   B 1 315 ? 5.127   0.862   -26.507 1.00 30.21  ? 326 ASN   B ND2  1 
ATOM   2883 N  N    . ILE   B 1 316 ? 2.234   -1.640  -22.750 1.00 29.79  ? 327 ILE   B N    1 
ATOM   2884 C  CA   . ILE   B 1 316 ? 2.199   -2.384  -21.500 1.00 31.17  ? 327 ILE   B CA   1 
ATOM   2885 C  C    . ILE   B 1 316 ? 2.017   -3.847  -21.866 1.00 33.80  ? 327 ILE   B C    1 
ATOM   2886 O  O    . ILE   B 1 316 ? 1.204   -4.171  -22.737 1.00 31.57  ? 327 ILE   B O    1 
ATOM   2887 C  CB   . ILE   B 1 316 ? 1.072   -1.880  -20.570 1.00 31.50  ? 327 ILE   B CB   1 
ATOM   2888 C  CG1  . ILE   B 1 316 ? 1.373   -0.449  -20.127 1.00 33.56  ? 327 ILE   B CG1  1 
ATOM   2889 C  CG2  . ILE   B 1 316 ? 0.920   -2.789  -19.352 1.00 38.61  ? 327 ILE   B CG2  1 
ATOM   2890 C  CD1  . ILE   B 1 316 ? 0.273   0.181   -19.347 1.00 42.39  ? 327 ILE   B CD1  1 
ATOM   2891 N  N    . VAL   B 1 317 ? 2.736   -4.730  -21.170 1.00 28.57  ? 328 VAL   B N    1 
ATOM   2892 C  CA   . VAL   B 1 317 ? 2.651   -6.168  -21.406 1.00 29.05  ? 328 VAL   B CA   1 
ATOM   2893 C  C    . VAL   B 1 317 ? 1.206   -6.641  -21.284 1.00 34.17  ? 328 VAL   B C    1 
ATOM   2894 O  O    . VAL   B 1 317 ? 0.538   -6.407  -20.271 1.00 35.31  ? 328 VAL   B O    1 
ATOM   2895 C  CB   . VAL   B 1 317 ? 3.569   -6.957  -20.450 1.00 33.50  ? 328 VAL   B CB   1 
ATOM   2896 C  CG1  . VAL   B 1 317 ? 3.298   -8.458  -20.572 1.00 32.64  ? 328 VAL   B CG1  1 
ATOM   2897 C  CG2  . VAL   B 1 317 ? 5.020   -6.692  -20.783 1.00 32.93  ? 328 VAL   B CG2  1 
ATOM   2898 N  N    . ASN   B 1 318 ? 0.703   -7.276  -22.338 1.00 33.88  ? 329 ASN   B N    1 
ATOM   2899 C  CA   . ASN   B 1 318 ? -0.724  -7.536  -22.423 1.00 38.61  ? 329 ASN   B CA   1 
ATOM   2900 C  C    . ASN   B 1 318 ? -1.110  -8.654  -21.457 1.00 37.00  ? 329 ASN   B C    1 
ATOM   2901 O  O    . ASN   B 1 318 ? -0.478  -9.713  -21.417 1.00 29.55  ? 329 ASN   B O    1 
ATOM   2902 C  CB   . ASN   B 1 318 ? -1.076  -7.932  -23.859 1.00 39.82  ? 329 ASN   B CB   1 
ATOM   2903 C  CG   . ASN   B 1 318 ? -2.565  -8.077  -24.083 1.00 50.63  ? 329 ASN   B CG   1 
ATOM   2904 O  OD1  . ASN   B 1 318 ? -3.361  -7.292  -23.571 1.00 45.58  ? 329 ASN   B OD1  1 
ATOM   2905 N  ND2  . ASN   B 1 318 ? -2.951  -9.085  -24.859 1.00 48.45  ? 329 ASN   B ND2  1 
ATOM   2906 N  N    . TYR   B 1 319 ? -2.159  -8.409  -20.682 1.00 33.85  ? 330 TYR   B N    1 
ATOM   2907 C  CA   . TYR   B 1 319 ? -2.725  -9.424  -19.809 1.00 32.59  ? 330 TYR   B CA   1 
ATOM   2908 C  C    . TYR   B 1 319 ? -3.707  -10.262 -20.618 1.00 41.08  ? 330 TYR   B C    1 
ATOM   2909 O  O    . TYR   B 1 319 ? -4.550  -9.714  -21.337 1.00 39.35  ? 330 TYR   B O    1 
ATOM   2910 C  CB   . TYR   B 1 319 ? -3.404  -8.759  -18.613 1.00 38.73  ? 330 TYR   B CB   1 
ATOM   2911 C  CG   . TYR   B 1 319 ? -4.234  -9.697  -17.780 1.00 43.36  ? 330 TYR   B CG   1 
ATOM   2912 C  CD1  . TYR   B 1 319 ? -3.741  -10.230 -16.597 1.00 46.12  ? 330 TYR   B CD1  1 
ATOM   2913 C  CD2  . TYR   B 1 319 ? -5.505  -10.050 -18.169 1.00 46.95  ? 330 TYR   B CD2  1 
ATOM   2914 C  CE1  . TYR   B 1 319 ? -4.507  -11.092 -15.830 1.00 56.23  ? 330 TYR   B CE1  1 
ATOM   2915 C  CE2  . TYR   B 1 319 ? -6.249  -10.924 -17.435 1.00 52.83  ? 330 TYR   B CE2  1 
ATOM   2916 C  CZ   . TYR   B 1 319 ? -5.774  -11.427 -16.260 1.00 53.03  ? 330 TYR   B CZ   1 
ATOM   2917 O  OH   . TYR   B 1 319 ? -6.584  -12.278 -15.542 1.00 55.57  ? 330 TYR   B OH   1 
ATOM   2918 N  N    . LEU   B 1 320 ? -3.627  -11.590 -20.489 1.00 35.68  ? 331 LEU   B N    1 
ATOM   2919 C  CA   . LEU   B 1 320 ? -4.492  -12.462 -21.283 1.00 37.27  ? 331 LEU   B CA   1 
ATOM   2920 C  C    . LEU   B 1 320 ? -5.638  -13.069 -20.480 1.00 49.14  ? 331 LEU   B C    1 
ATOM   2921 O  O    . LEU   B 1 320 ? -6.805  -12.861 -20.817 1.00 46.54  ? 331 LEU   B O    1 
ATOM   2922 C  CB   . LEU   B 1 320 ? -3.659  -13.580 -21.929 1.00 31.60  ? 331 LEU   B CB   1 
ATOM   2923 C  CG   . LEU   B 1 320 ? -2.524  -13.094 -22.823 1.00 41.41  ? 331 LEU   B CG   1 
ATOM   2924 C  CD1  . LEU   B 1 320 ? -1.669  -14.257 -23.298 1.00 35.21  ? 331 LEU   B CD1  1 
ATOM   2925 C  CD2  . LEU   B 1 320 ? -3.099  -12.322 -24.000 1.00 43.48  ? 331 LEU   B CD2  1 
ATOM   2926 N  N    . ASP   B 1 321 ? -5.338  -13.792 -19.407 1.00 35.55  ? 332 ASP   B N    1 
ATOM   2927 C  CA   . ASP   B 1 321 ? -6.385  -14.556 -18.745 1.00 45.29  ? 332 ASP   B CA   1 
ATOM   2928 C  C    . ASP   B 1 321 ? -5.889  -14.960 -17.365 1.00 45.23  ? 332 ASP   B C    1 
ATOM   2929 O  O    . ASP   B 1 321 ? -4.713  -14.800 -17.037 1.00 45.52  ? 332 ASP   B O    1 
ATOM   2930 C  CB   . ASP   B 1 321 ? -6.758  -15.782 -19.588 1.00 49.70  ? 332 ASP   B CB   1 
ATOM   2931 C  CG   . ASP   B 1 321 ? -8.243  -15.899 -19.832 1.00 61.84  ? 332 ASP   B CG   1 
ATOM   2932 O  OD1  . ASP   B 1 321 ? -9.034  -15.631 -18.901 1.00 70.06  ? 332 ASP   B OD1  1 
ATOM   2933 O  OD2  . ASP   B 1 321 ? -8.618  -16.238 -20.976 1.00 68.12  ? 332 ASP   B OD2  1 
ATOM   2934 N  N    . SER   B 1 322 ? -6.796  -15.504 -16.559 1.00 50.14  ? 333 SER   B N    1 
ATOM   2935 C  CA   . SER   B 1 322 ? -6.395  -16.051 -15.274 1.00 44.00  ? 333 SER   B CA   1 
ATOM   2936 C  C    . SER   B 1 322 ? -7.292  -17.232 -14.942 1.00 49.71  ? 333 SER   B C    1 
ATOM   2937 O  O    . SER   B 1 322 ? -8.409  -17.355 -15.452 1.00 46.55  ? 333 SER   B O    1 
ATOM   2938 C  CB   . SER   B 1 322 ? -6.439  -15.005 -14.157 1.00 48.20  ? 333 SER   B CB   1 
ATOM   2939 O  OG   . SER   B 1 322 ? -7.713  -14.407 -14.068 1.00 66.77  ? 333 SER   B OG   1 
ATOM   2940 N  N    . TYR   B 1 323 ? -6.764  -18.119 -14.105 1.00 44.72  ? 334 TYR   B N    1 
ATOM   2941 C  CA   . TYR   B 1 323 ? -7.406  -19.382 -13.784 1.00 47.68  ? 334 TYR   B CA   1 
ATOM   2942 C  C    . TYR   B 1 323 ? -7.180  -19.685 -12.314 1.00 45.85  ? 334 TYR   B C    1 
ATOM   2943 O  O    . TYR   B 1 323 ? -6.115  -19.382 -11.772 1.00 49.24  ? 334 TYR   B O    1 
ATOM   2944 C  CB   . TYR   B 1 323 ? -6.842  -20.528 -14.633 1.00 41.49  ? 334 TYR   B CB   1 
ATOM   2945 C  CG   . TYR   B 1 323 ? -6.912  -20.287 -16.124 1.00 54.84  ? 334 TYR   B CG   1 
ATOM   2946 C  CD1  . TYR   B 1 323 ? -5.914  -19.575 -16.776 1.00 47.70  ? 334 TYR   B CD1  1 
ATOM   2947 C  CD2  . TYR   B 1 323 ? -7.970  -20.776 -16.881 1.00 60.58  ? 334 TYR   B CD2  1 
ATOM   2948 C  CE1  . TYR   B 1 323 ? -5.973  -19.345 -18.131 1.00 52.92  ? 334 TYR   B CE1  1 
ATOM   2949 C  CE2  . TYR   B 1 323 ? -8.033  -20.554 -18.245 1.00 55.93  ? 334 TYR   B CE2  1 
ATOM   2950 C  CZ   . TYR   B 1 323 ? -7.032  -19.836 -18.864 1.00 59.70  ? 334 TYR   B CZ   1 
ATOM   2951 O  OH   . TYR   B 1 323 ? -7.079  -19.602 -20.220 1.00 60.23  ? 334 TYR   B OH   1 
ATOM   2952 N  N    . LEU   B 1 324 ? -8.185  -20.264 -11.663 1.00 47.13  ? 335 LEU   B N    1 
ATOM   2953 C  CA   . LEU   B 1 324 ? -8.008  -20.823 -10.332 1.00 49.24  ? 335 LEU   B CA   1 
ATOM   2954 C  C    . LEU   B 1 324 ? -7.732  -22.307 -10.530 1.00 53.11  ? 335 LEU   B C    1 
ATOM   2955 O  O    . LEU   B 1 324 ? -8.594  -23.044 -11.018 1.00 60.51  ? 335 LEU   B O    1 
ATOM   2956 C  CB   . LEU   B 1 324 ? -9.238  -20.587 -9.460  1.00 58.02  ? 335 LEU   B CB   1 
ATOM   2957 C  CG   . LEU   B 1 324 ? -8.985  -20.590 -7.953  1.00 71.93  ? 335 LEU   B CG   1 
ATOM   2958 C  CD1  . LEU   B 1 324 ? -8.081  -19.422 -7.568  1.00 73.03  ? 335 LEU   B CD1  1 
ATOM   2959 C  CD2  . LEU   B 1 324 ? -10.296 -20.536 -7.188  1.00 77.85  ? 335 LEU   B CD2  1 
ATOM   2960 N  N    . VAL   B 1 325 ? -6.526  -22.736 -10.178 1.00 52.01  ? 336 VAL   B N    1 
ATOM   2961 C  CA   . VAL   B 1 325 ? -6.114  -24.133 -10.284 1.00 55.75  ? 336 VAL   B CA   1 
ATOM   2962 C  C    . VAL   B 1 325 ? -5.809  -24.599 -8.865  1.00 58.69  ? 336 VAL   B C    1 
ATOM   2963 O  O    . VAL   B 1 325 ? -4.684  -24.452 -8.375  1.00 60.03  ? 336 VAL   B O    1 
ATOM   2964 C  CB   . VAL   B 1 325 ? -4.903  -24.322 -11.201 1.00 57.43  ? 336 VAL   B CB   1 
ATOM   2965 C  CG1  . VAL   B 1 325 ? -4.641  -25.806 -11.432 1.00 58.82  ? 336 VAL   B CG1  1 
ATOM   2966 C  CG2  . VAL   B 1 325 ? -5.089  -23.575 -12.524 1.00 45.49  ? 336 VAL   B CG2  1 
ATOM   2967 N  N    . GLY   B 1 326 ? -6.816  -25.156 -8.195  1.00 66.57  ? 337 GLY   B N    1 
ATOM   2968 C  CA   . GLY   B 1 326 ? -6.663  -25.630 -6.832  1.00 60.41  ? 337 GLY   B CA   1 
ATOM   2969 C  C    . GLY   B 1 326 ? -6.256  -24.533 -5.870  1.00 58.64  ? 337 GLY   B C    1 
ATOM   2970 O  O    . GLY   B 1 326 ? -5.188  -24.602 -5.256  1.00 59.36  ? 337 GLY   B O    1 
ATOM   2971 N  N    . ASP   B 1 327 ? -7.099  -23.511 -5.737  1.00 65.67  ? 338 ASP   B N    1 
ATOM   2972 C  CA   . ASP   B 1 327 ? -6.831  -22.365 -4.871  1.00 85.78  ? 338 ASP   B CA   1 
ATOM   2973 C  C    . ASP   B 1 327 ? -5.497  -21.688 -5.144  1.00 71.63  ? 338 ASP   B C    1 
ATOM   2974 O  O    . ASP   B 1 327 ? -5.017  -20.895 -4.329  1.00 79.74  ? 338 ASP   B O    1 
ATOM   2975 C  CB   . ASP   B 1 327 ? -6.938  -22.747 -3.403  1.00 86.95  ? 338 ASP   B CB   1 
ATOM   2976 C  CG   . ASP   B 1 327 ? -8.357  -22.731 -2.928  1.00 92.61  ? 338 ASP   B CG   1 
ATOM   2977 O  OD1  . ASP   B 1 327 ? -9.116  -21.827 -3.341  1.00 97.82  ? 338 ASP   B OD1  1 
ATOM   2978 O  OD2  . ASP   B 1 327 ? -8.727  -23.628 -2.175  1.00 103.63 ? 338 ASP   B OD2  1 
ATOM   2979 N  N    . GLU   B 1 328 ? -4.887  -22.008 -6.272  1.00 72.62  ? 339 GLU   B N    1 
ATOM   2980 C  CA   . GLU   B 1 328 ? -3.800  -21.208 -6.795  1.00 63.56  ? 339 GLU   B CA   1 
ATOM   2981 C  C    . GLU   B 1 328 ? -4.402  -20.366 -7.900  1.00 59.17  ? 339 GLU   B C    1 
ATOM   2982 O  O    . GLU   B 1 328 ? -5.278  -20.827 -8.639  1.00 56.27  ? 339 GLU   B O    1 
ATOM   2983 C  CB   . GLU   B 1 328 ? -2.632  -22.028 -7.343  1.00 72.00  ? 339 GLU   B CB   1 
ATOM   2984 C  CG   . GLU   B 1 328 ? -1.689  -22.581 -6.308  1.00 73.29  ? 339 GLU   B CG   1 
ATOM   2985 C  CD   . GLU   B 1 328 ? -0.447  -23.161 -6.949  1.00 74.63  ? 339 GLU   B CD   1 
ATOM   2986 O  OE1  . GLU   B 1 328 ? -0.358  -23.146 -8.196  1.00 73.04  ? 339 GLU   B OE1  1 
ATOM   2987 O  OE2  . GLU   B 1 328 ? 0.445   -23.625 -6.210  1.00 81.17  ? 339 GLU   B OE2  1 
ATOM   2988 N  N    . LEU   B 1 329 ? -3.977  -19.119 -7.976  1.00 55.18  ? 340 LEU   B N    1 
ATOM   2989 C  CA   . LEU   B 1 329 ? -4.384  -18.252 -9.061  1.00 46.19  ? 340 LEU   B CA   1 
ATOM   2990 C  C    . LEU   B 1 329 ? -3.236  -18.225 -10.056 1.00 44.10  ? 340 LEU   B C    1 
ATOM   2991 O  O    . LEU   B 1 329 ? -2.097  -17.920 -9.686  1.00 49.07  ? 340 LEU   B O    1 
ATOM   2992 C  CB   . LEU   B 1 329 ? -4.709  -16.850 -8.552  1.00 51.13  ? 340 LEU   B CB   1 
ATOM   2993 C  CG   . LEU   B 1 329 ? -5.065  -15.839 -9.636  1.00 52.24  ? 340 LEU   B CG   1 
ATOM   2994 C  CD1  . LEU   B 1 329 ? -6.317  -16.301 -10.361 1.00 53.09  ? 340 LEU   B CD1  1 
ATOM   2995 C  CD2  . LEU   B 1 329 ? -5.268  -14.463 -9.037  1.00 62.26  ? 340 LEU   B CD2  1 
ATOM   2996 N  N    . TRP   B 1 330 ? -3.528  -18.564 -11.304 1.00 41.61  ? 341 TRP   B N    1 
ATOM   2997 C  CA   . TRP   B 1 330 ? -2.546  -18.467 -12.375 1.00 39.17  ? 341 TRP   B CA   1 
ATOM   2998 C  C    . TRP   B 1 330 ? -2.899  -17.261 -13.222 1.00 37.85  ? 341 TRP   B C    1 
ATOM   2999 O  O    . TRP   B 1 330 ? -4.024  -17.154 -13.714 1.00 43.57  ? 341 TRP   B O    1 
ATOM   3000 C  CB   . TRP   B 1 330 ? -2.515  -19.718 -13.252 1.00 40.45  ? 341 TRP   B CB   1 
ATOM   3001 C  CG   . TRP   B 1 330 ? -2.030  -20.947 -12.599 1.00 47.70  ? 341 TRP   B CG   1 
ATOM   3002 C  CD1  . TRP   B 1 330 ? -1.827  -21.154 -11.267 1.00 45.60  ? 341 TRP   B CD1  1 
ATOM   3003 C  CD2  . TRP   B 1 330 ? -1.666  -22.165 -13.257 1.00 42.00  ? 341 TRP   B CD2  1 
ATOM   3004 N  NE1  . TRP   B 1 330 ? -1.362  -22.432 -11.053 1.00 45.82  ? 341 TRP   B NE1  1 
ATOM   3005 C  CE2  . TRP   B 1 330 ? -1.251  -23.071 -12.260 1.00 48.84  ? 341 TRP   B CE2  1 
ATOM   3006 C  CE3  . TRP   B 1 330 ? -1.649  -22.577 -14.594 1.00 52.34  ? 341 TRP   B CE3  1 
ATOM   3007 C  CZ2  . TRP   B 1 330 ? -0.827  -24.368 -12.559 1.00 50.03  ? 341 TRP   B CZ2  1 
ATOM   3008 C  CZ3  . TRP   B 1 330 ? -1.225  -23.872 -14.890 1.00 43.98  ? 341 TRP   B CZ3  1 
ATOM   3009 C  CH2  . TRP   B 1 330 ? -0.825  -24.747 -13.873 1.00 45.82  ? 341 TRP   B CH2  1 
ATOM   3010 N  N    . VAL   B 1 331 ? -1.947  -16.352 -13.380 1.00 36.67  ? 342 VAL   B N    1 
ATOM   3011 C  CA   . VAL   B 1 331 ? -2.137  -15.152 -14.176 1.00 35.53  ? 342 VAL   B CA   1 
ATOM   3012 C  C    . VAL   B 1 331 ? -1.338  -15.359 -15.453 1.00 33.45  ? 342 VAL   B C    1 
ATOM   3013 O  O    . VAL   B 1 331 ? -0.151  -15.698 -15.392 1.00 38.28  ? 342 VAL   B O    1 
ATOM   3014 C  CB   . VAL   B 1 331 ? -1.667  -13.898 -13.419 1.00 36.32  ? 342 VAL   B CB   1 
ATOM   3015 C  CG1  . VAL   B 1 331 ? -1.753  -12.682 -14.305 1.00 37.23  ? 342 VAL   B CG1  1 
ATOM   3016 C  CG2  . VAL   B 1 331 ? -2.483  -13.710 -12.150 1.00 38.51  ? 342 VAL   B CG2  1 
ATOM   3017 N  N    . VAL   B 1 332 ? -1.985  -15.189 -16.603 1.00 32.58  ? 343 VAL   B N    1 
ATOM   3018 C  CA   . VAL   B 1 332 ? -1.360  -15.479 -17.892 1.00 31.70  ? 343 VAL   B CA   1 
ATOM   3019 C  C    . VAL   B 1 332 ? -1.152  -14.166 -18.629 1.00 33.45  ? 343 VAL   B C    1 
ATOM   3020 O  O    . VAL   B 1 332 ? -2.108  -13.408 -18.850 1.00 30.30  ? 343 VAL   B O    1 
ATOM   3021 C  CB   . VAL   B 1 332 ? -2.194  -16.455 -18.730 1.00 33.72  ? 343 VAL   B CB   1 
ATOM   3022 C  CG1  . VAL   B 1 332 ? -1.434  -16.826 -20.011 1.00 31.49  ? 343 VAL   B CG1  1 
ATOM   3023 C  CG2  . VAL   B 1 332 ? -2.510  -17.712 -17.919 1.00 32.42  ? 343 VAL   B CG2  1 
ATOM   3024 N  N    . MET   B 1 333 ? 0.098   -13.893 -18.980 1.00 28.95  ? 344 MET   B N    1 
ATOM   3025 C  CA   . MET   B 1 333 ? 0.487   -12.692 -19.697 1.00 28.12  ? 344 MET   B CA   1 
ATOM   3026 C  C    . MET   B 1 333 ? 1.135   -13.109 -21.007 1.00 28.48  ? 344 MET   B C    1 
ATOM   3027 O  O    . MET   B 1 333 ? 1.645   -14.225 -21.135 1.00 30.83  ? 344 MET   B O    1 
ATOM   3028 C  CB   . MET   B 1 333 ? 1.486   -11.850 -18.885 1.00 29.52  ? 344 MET   B CB   1 
ATOM   3029 C  CG   . MET   B 1 333 ? 1.105   -11.620 -17.428 1.00 29.93  ? 344 MET   B CG   1 
ATOM   3030 S  SD   . MET   B 1 333 ? -0.319  -10.544 -17.277 1.00 36.83  ? 344 MET   B SD   1 
ATOM   3031 C  CE   . MET   B 1 333 ? 0.390   -8.967  -17.768 1.00 30.37  ? 344 MET   B CE   1 
ATOM   3032 N  N    . GLU   B 1 334 ? 1.124   -12.204 -21.983 1.00 30.41  ? 345 GLU   B N    1 
ATOM   3033 C  CA   . GLU   B 1 334 ? 1.929   -12.428 -23.181 1.00 28.43  ? 345 GLU   B CA   1 
ATOM   3034 C  C    . GLU   B 1 334 ? 3.408   -12.489 -22.807 1.00 29.17  ? 345 GLU   B C    1 
ATOM   3035 O  O    . GLU   B 1 334 ? 3.859   -11.828 -21.873 1.00 29.49  ? 345 GLU   B O    1 
ATOM   3036 C  CB   . GLU   B 1 334 ? 1.675   -11.326 -24.210 1.00 33.60  ? 345 GLU   B CB   1 
ATOM   3037 C  CG   . GLU   B 1 334 ? 2.206   -9.958  -23.801 1.00 29.91  ? 345 GLU   B CG   1 
ATOM   3038 C  CD   . GLU   B 1 334 ? 2.194   -8.958  -24.943 1.00 36.99  ? 345 GLU   B CD   1 
ATOM   3039 O  OE1  . GLU   B 1 334 ? 2.242   -9.387  -26.115 1.00 47.13  ? 345 GLU   B OE1  1 
ATOM   3040 O  OE2  . GLU   B 1 334 ? 2.135   -7.742  -24.675 1.00 34.81  ? 345 GLU   B OE2  1 
ATOM   3041 N  N    . TYR   B 1 335 ? 4.179   -13.276 -23.555 1.00 29.00  ? 346 TYR   B N    1 
ATOM   3042 C  CA   . TYR   B 1 335 ? 5.602   -13.429 -23.284 1.00 29.43  ? 346 TYR   B CA   1 
ATOM   3043 C  C    . TYR   B 1 335 ? 6.391   -12.621 -24.308 1.00 29.92  ? 346 TYR   B C    1 
ATOM   3044 O  O    . TYR   B 1 335 ? 6.118   -12.701 -25.510 1.00 29.51  ? 346 TYR   B O    1 
ATOM   3045 C  CB   . TYR   B 1 335 ? 6.014   -14.902 -23.346 1.00 30.29  ? 346 TYR   B CB   1 
ATOM   3046 C  CG   . TYR   B 1 335 ? 7.494   -15.144 -23.129 1.00 34.69  ? 346 TYR   B CG   1 
ATOM   3047 C  CD1  . TYR   B 1 335 ? 8.071   -14.925 -21.891 1.00 31.64  ? 346 TYR   B CD1  1 
ATOM   3048 C  CD2  . TYR   B 1 335 ? 8.313   -15.600 -24.158 1.00 42.57  ? 346 TYR   B CD2  1 
ATOM   3049 C  CE1  . TYR   B 1 335 ? 9.416   -15.146 -21.677 1.00 35.31  ? 346 TYR   B CE1  1 
ATOM   3050 C  CE2  . TYR   B 1 335 ? 9.669   -15.825 -23.948 1.00 35.28  ? 346 TYR   B CE2  1 
ATOM   3051 C  CZ   . TYR   B 1 335 ? 10.212  -15.597 -22.705 1.00 39.73  ? 346 TYR   B CZ   1 
ATOM   3052 O  OH   . TYR   B 1 335 ? 11.554  -15.820 -22.475 1.00 40.70  ? 346 TYR   B OH   1 
ATOM   3053 N  N    . LEU   B 1 336 ? 7.338   -11.827 -23.832 1.00 29.92  ? 347 LEU   B N    1 
ATOM   3054 C  CA   . LEU   B 1 336 ? 8.178   -10.994 -24.694 1.00 28.96  ? 347 LEU   B CA   1 
ATOM   3055 C  C    . LEU   B 1 336 ? 9.550   -11.656 -24.742 1.00 32.13  ? 347 LEU   B C    1 
ATOM   3056 O  O    . LEU   B 1 336 ? 10.331  -11.562 -23.792 1.00 32.00  ? 347 LEU   B O    1 
ATOM   3057 C  CB   . LEU   B 1 336 ? 8.246   -9.555  -24.191 1.00 28.64  ? 347 LEU   B CB   1 
ATOM   3058 C  CG   . LEU   B 1 336 ? 7.135   -8.667  -24.767 1.00 36.28  ? 347 LEU   B CG   1 
ATOM   3059 C  CD1  . LEU   B 1 336 ? 5.769   -9.085  -24.263 1.00 37.79  ? 347 LEU   B CD1  1 
ATOM   3060 C  CD2  . LEU   B 1 336 ? 7.389   -7.197  -24.474 1.00 41.79  ? 347 LEU   B CD2  1 
ATOM   3061 N  N    . ALA   B 1 337 ? 9.833   -12.335 -25.856 1.00 29.92  ? 348 ALA   B N    1 
ATOM   3062 C  CA   . ALA   B 1 337 ? 10.990  -13.215 -25.971 1.00 34.87  ? 348 ALA   B CA   1 
ATOM   3063 C  C    . ALA   B 1 337 ? 12.286  -12.464 -26.252 1.00 34.59  ? 348 ALA   B C    1 
ATOM   3064 O  O    . ALA   B 1 337 ? 13.350  -13.092 -26.303 1.00 35.66  ? 348 ALA   B O    1 
ATOM   3065 C  CB   . ALA   B 1 337 ? 10.749  -14.270 -27.064 1.00 36.62  ? 348 ALA   B CB   1 
ATOM   3066 N  N    . GLY   B 1 338 ? 12.229  -11.154 -26.466 1.00 30.98  ? 349 GLY   B N    1 
ATOM   3067 C  CA   . GLY   B 1 338 ? 13.465  -10.421 -26.664 1.00 30.46  ? 349 GLY   B CA   1 
ATOM   3068 C  C    . GLY   B 1 338 ? 14.241  -10.146 -25.397 1.00 30.12  ? 349 GLY   B C    1 
ATOM   3069 O  O    . GLY   B 1 338 ? 15.355  -9.626  -25.466 1.00 28.55  ? 349 GLY   B O    1 
ATOM   3070 N  N    . GLY   B 1 339 ? 13.684  -10.473 -24.242 1.00 30.04  ? 350 GLY   B N    1 
ATOM   3071 C  CA   . GLY   B 1 339 ? 14.369  -10.225 -22.994 1.00 28.47  ? 350 GLY   B CA   1 
ATOM   3072 C  C    . GLY   B 1 339 ? 14.164  -8.816  -22.471 1.00 28.90  ? 350 GLY   B C    1 
ATOM   3073 O  O    . GLY   B 1 339 ? 13.369  -8.012  -22.979 1.00 28.45  ? 350 GLY   B O    1 
ATOM   3074 N  N    . SER   B 1 340 ? 14.922  -8.516  -21.422 1.00 25.32  ? 351 SER   B N    1 
ATOM   3075 C  CA   . SER   B 1 340 ? 14.850  -7.228  -20.748 1.00 24.31  ? 351 SER   B CA   1 
ATOM   3076 C  C    . SER   B 1 340 ? 15.754  -6.207  -21.421 1.00 22.11  ? 351 SER   B C    1 
ATOM   3077 O  O    . SER   B 1 340 ? 16.736  -6.543  -22.082 1.00 25.95  ? 351 SER   B O    1 
ATOM   3078 C  CB   . SER   B 1 340 ? 15.270  -7.349  -19.286 1.00 24.75  ? 351 SER   B CB   1 
ATOM   3079 O  OG   . SER   B 1 340 ? 16.672  -7.574  -19.200 1.00 35.01  ? 351 SER   B OG   1 
ATOM   3080 N  N    . LEU   B 1 341 ? 15.436  -4.935  -21.194 1.00 21.00  ? 352 LEU   B N    1 
ATOM   3081 C  CA   . LEU   B 1 341 ? 16.332  -3.877  -21.640 1.00 21.30  ? 352 LEU   B CA   1 
ATOM   3082 C  C    . LEU   B 1 341 ? 17.689  -3.970  -20.946 1.00 20.81  ? 352 LEU   B C    1 
ATOM   3083 O  O    . LEU   B 1 341 ? 18.715  -3.634  -21.551 1.00 23.08  ? 352 LEU   B O    1 
ATOM   3084 C  CB   . LEU   B 1 341 ? 15.668  -2.527  -21.398 1.00 18.01  ? 352 LEU   B CB   1 
ATOM   3085 C  CG   . LEU   B 1 341 ? 16.431  -1.265  -21.777 1.00 18.86  ? 352 LEU   B CG   1 
ATOM   3086 C  CD1  . LEU   B 1 341 ? 16.733  -1.303  -23.276 1.00 17.62  ? 352 LEU   B CD1  1 
ATOM   3087 C  CD2  . LEU   B 1 341 ? 15.614  -0.015  -21.440 1.00 21.35  ? 352 LEU   B CD2  1 
ATOM   3088 N  N    . THR   B 1 342 ? 17.724  -4.473  -19.705 1.00 20.78  ? 353 THR   B N    1 
ATOM   3089 C  CA   . THR   B 1 342 ? 18.987  -4.578  -18.971 1.00 20.58  ? 353 THR   B CA   1 
ATOM   3090 C  C    . THR   B 1 342 ? 20.015  -5.395  -19.744 1.00 23.95  ? 353 THR   B C    1 
ATOM   3091 O  O    . THR   B 1 342 ? 21.187  -5.013  -19.830 1.00 26.55  ? 353 THR   B O    1 
ATOM   3092 C  CB   . THR   B 1 342 ? 18.775  -5.223  -17.600 1.00 25.63  ? 353 THR   B CB   1 
ATOM   3093 O  OG1  . THR   B 1 342 ? 17.732  -4.551  -16.900 1.00 27.11  ? 353 THR   B OG1  1 
ATOM   3094 C  CG2  . THR   B 1 342 ? 20.066  -5.140  -16.781 1.00 29.42  ? 353 THR   B CG2  1 
ATOM   3095 N  N    . ASP   B 1 343 ? 19.600  -6.546  -20.280 1.00 23.76  ? 354 ASP   B N    1 
ATOM   3096 C  CA   . ASP   B 1 343 ? 20.520  -7.384  -21.047 1.00 26.80  ? 354 ASP   B CA   1 
ATOM   3097 C  C    . ASP   B 1 343 ? 21.056  -6.656  -22.280 1.00 24.18  ? 354 ASP   B C    1 
ATOM   3098 O  O    . ASP   B 1 343 ? 22.231  -6.796  -22.633 1.00 26.77  ? 354 ASP   B O    1 
ATOM   3099 C  CB   . ASP   B 1 343 ? 19.825  -8.677  -21.461 1.00 26.76  ? 354 ASP   B CB   1 
ATOM   3100 C  CG   . ASP   B 1 343 ? 19.498  -9.570  -20.280 1.00 40.61  ? 354 ASP   B CG   1 
ATOM   3101 O  OD1  . ASP   B 1 343 ? 19.983  -9.293  -19.159 1.00 39.06  ? 354 ASP   B OD1  1 
ATOM   3102 O  OD2  . ASP   B 1 343 ? 18.748  -10.546 -20.477 1.00 44.45  ? 354 ASP   B OD2  1 
ATOM   3103 N  N    . VAL   B 1 344 ? 20.201  -5.903  -22.970 1.00 23.87  ? 355 VAL   B N    1 
ATOM   3104 C  CA   . VAL   B 1 344 ? 20.668  -5.130  -24.120 1.00 22.83  ? 355 VAL   B CA   1 
ATOM   3105 C  C    . VAL   B 1 344 ? 21.665  -4.070  -23.672 1.00 24.61  ? 355 VAL   B C    1 
ATOM   3106 O  O    . VAL   B 1 344 ? 22.721  -3.880  -24.294 1.00 26.20  ? 355 VAL   B O    1 
ATOM   3107 C  CB   . VAL   B 1 344 ? 19.468  -4.514  -24.867 1.00 24.04  ? 355 VAL   B CB   1 
ATOM   3108 C  CG1  . VAL   B 1 344 ? 19.903  -3.374  -25.785 1.00 24.79  ? 355 VAL   B CG1  1 
ATOM   3109 C  CG2  . VAL   B 1 344 ? 18.733  -5.608  -25.668 1.00 22.33  ? 355 VAL   B CG2  1 
ATOM   3110 N  N    . VAL   B 1 345 ? 21.357  -3.378  -22.573 1.00 22.35  ? 356 VAL   B N    1 
ATOM   3111 C  CA   . VAL   B 1 345 ? 22.197  -2.268  -22.132 1.00 22.62  ? 356 VAL   B CA   1 
ATOM   3112 C  C    . VAL   B 1 345 ? 23.581  -2.770  -21.737 1.00 26.80  ? 356 VAL   B C    1 
ATOM   3113 O  O    . VAL   B 1 345 ? 24.595  -2.130  -22.036 1.00 27.98  ? 356 VAL   B O    1 
ATOM   3114 C  CB   . VAL   B 1 345 ? 21.514  -1.529  -20.963 1.00 26.07  ? 356 VAL   B CB   1 
ATOM   3115 C  CG1  . VAL   B 1 345 ? 22.518  -0.650  -20.222 1.00 31.74  ? 356 VAL   B CG1  1 
ATOM   3116 C  CG2  . VAL   B 1 345 ? 20.351  -0.680  -21.482 1.00 29.92  ? 356 VAL   B CG2  1 
ATOM   3117 N  N    . THR   B 1 346 ? 23.657  -3.955  -21.133 1.00 23.32  ? 357 THR   B N    1 
ATOM   3118 C  CA   . THR   B 1 346 ? 24.942  -4.432  -20.637 1.00 30.62  ? 357 THR   B CA   1 
ATOM   3119 C  C    . THR   B 1 346 ? 25.771  -5.135  -21.700 1.00 32.36  ? 357 THR   B C    1 
ATOM   3120 O  O    . THR   B 1 346 ? 26.984  -5.269  -21.528 1.00 34.78  ? 357 THR   B O    1 
ATOM   3121 C  CB   . THR   B 1 346 ? 24.761  -5.390  -19.458 1.00 31.55  ? 357 THR   B CB   1 
ATOM   3122 O  OG1  . THR   B 1 346 ? 23.965  -6.505  -19.864 1.00 42.71  ? 357 THR   B OG1  1 
ATOM   3123 C  CG2  . THR   B 1 346 ? 24.097  -4.704  -18.272 1.00 27.96  ? 357 THR   B CG2  1 
ATOM   3124 N  N    . GLU   B 1 347 ? 25.172  -5.531  -22.813 1.00 29.34  ? 358 GLU   B N    1 
ATOM   3125 C  CA   . GLU   B 1 347 ? 25.888  -6.321  -23.799 1.00 27.91  ? 358 GLU   B CA   1 
ATOM   3126 C  C    . GLU   B 1 347 ? 26.067  -5.605  -25.125 1.00 26.91  ? 358 GLU   B C    1 
ATOM   3127 O  O    . GLU   B 1 347 ? 26.711  -6.154  -26.022 1.00 29.36  ? 358 GLU   B O    1 
ATOM   3128 C  CB   . GLU   B 1 347 ? 25.181  -7.665  -24.013 1.00 30.37  ? 358 GLU   B CB   1 
ATOM   3129 C  CG   . GLU   B 1 347 ? 25.091  -8.510  -22.748 1.00 27.74  ? 358 GLU   B CG   1 
ATOM   3130 C  CD   . GLU   B 1 347 ? 26.456  -8.933  -22.205 1.00 37.88  ? 358 GLU   B CD   1 
ATOM   3131 O  OE1  . GLU   B 1 347 ? 27.477  -8.811  -22.921 1.00 37.38  ? 358 GLU   B OE1  1 
ATOM   3132 O  OE2  . GLU   B 1 347 ? 26.506  -9.394  -21.048 1.00 49.09  ? 358 GLU   B OE2  1 
ATOM   3133 N  N    . THR   B 1 348 ? 25.523  -4.398  -25.281 1.00 24.06  ? 359 THR   B N    1 
ATOM   3134 C  CA   . THR   B 1 348 ? 25.665  -3.636  -26.516 1.00 26.18  ? 359 THR   B CA   1 
ATOM   3135 C  C    . THR   B 1 348 ? 25.943  -2.191  -26.153 1.00 27.61  ? 359 THR   B C    1 
ATOM   3136 O  O    . THR   B 1 348 ? 25.727  -1.775  -25.018 1.00 26.77  ? 359 THR   B O    1 
ATOM   3137 C  CB   . THR   B 1 348 ? 24.399  -3.682  -27.387 1.00 29.03  ? 359 THR   B CB   1 
ATOM   3138 O  OG1  . THR   B 1 348 ? 23.389  -2.843  -26.801 1.00 25.56  ? 359 THR   B OG1  1 
ATOM   3139 C  CG2  . THR   B 1 348 ? 23.863  -5.105  -27.505 1.00 29.63  ? 359 THR   B CG2  1 
ATOM   3140 N  N    . CYS   B 1 349 ? 26.399  -1.394  -27.114 1.00 25.93  ? 360 CYS   B N    1 
ATOM   3141 C  CA   . CYS   B 1 349 ? 26.309  0.049   -26.932 1.00 34.59  ? 360 CYS   B CA   1 
ATOM   3142 C  C    . CYS   B 1 349 ? 25.197  0.543   -27.844 1.00 33.10  ? 360 CYS   B C    1 
ATOM   3143 O  O    . CYS   B 1 349 ? 25.244  0.349   -29.062 1.00 33.67  ? 360 CYS   B O    1 
ATOM   3144 C  CB   . CYS   B 1 349 ? 27.634  0.780   -27.168 1.00 41.99  ? 360 CYS   B CB   1 
ATOM   3145 S  SG   . CYS   B 1 349 ? 28.602  0.294   -28.561 1.00 50.00  ? 360 CYS   B SG   1 
ATOM   3146 N  N    . MET   B 1 350 ? 24.182  1.141   -27.245 1.00 25.03  ? 361 MET   B N    1 
ATOM   3147 C  CA   . MET   B 1 350 ? 23.050  1.642   -28.002 1.00 27.71  ? 361 MET   B CA   1 
ATOM   3148 C  C    . MET   B 1 350 ? 23.402  3.013   -28.536 1.00 22.86  ? 361 MET   B C    1 
ATOM   3149 O  O    . MET   B 1 350 ? 24.117  3.774   -27.880 1.00 25.84  ? 361 MET   B O    1 
ATOM   3150 C  CB   . MET   B 1 350 ? 21.818  1.742   -27.106 1.00 20.31  ? 361 MET   B CB   1 
ATOM   3151 C  CG   . MET   B 1 350 ? 21.451  0.431   -26.423 1.00 21.23  ? 361 MET   B CG   1 
ATOM   3152 S  SD   . MET   B 1 350 ? 20.011  0.636   -25.361 1.00 24.62  ? 361 MET   B SD   1 
ATOM   3153 C  CE   . MET   B 1 350 ? 18.757  1.108   -26.546 1.00 19.95  ? 361 MET   B CE   1 
ATOM   3154 N  N    . ASP   B 1 351 ? 22.977  3.297   -29.759 1.00 22.05  ? 362 ASP   B N    1 
ATOM   3155 C  CA   . ASP   B 1 351 ? 23.173  4.643   -30.275 1.00 27.24  ? 362 ASP   B CA   1 
ATOM   3156 C  C    . ASP   B 1 351 ? 21.982  5.521   -29.888 1.00 25.09  ? 362 ASP   B C    1 
ATOM   3157 O  O    . ASP   B 1 351 ? 20.958  5.037   -29.401 1.00 22.74  ? 362 ASP   B O    1 
ATOM   3158 C  CB   . ASP   B 1 351 ? 23.420  4.627   -31.795 1.00 26.19  ? 362 ASP   B CB   1 
ATOM   3159 C  CG   . ASP   B 1 351 ? 22.241  4.098   -32.616 1.00 32.49  ? 362 ASP   B CG   1 
ATOM   3160 O  OD1  . ASP   B 1 351 ? 21.079  4.458   -32.353 1.00 26.76  ? 362 ASP   B OD1  1 
ATOM   3161 O  OD2  . ASP   B 1 351 ? 22.488  3.347   -33.588 1.00 30.10  ? 362 ASP   B OD2  1 
ATOM   3162 N  N    . GLU   B 1 352 ? 22.122  6.832   -30.114 1.00 24.77  ? 363 GLU   B N    1 
ATOM   3163 C  CA   . GLU   B 1 352 ? 21.104  7.757   -29.623 1.00 19.44  ? 363 GLU   B CA   1 
ATOM   3164 C  C    . GLU   B 1 352 ? 19.770  7.537   -30.317 1.00 23.12  ? 363 GLU   B C    1 
ATOM   3165 O  O    . GLU   B 1 352 ? 18.725  7.742   -29.698 1.00 24.03  ? 363 GLU   B O    1 
ATOM   3166 C  CB   . GLU   B 1 352 ? 21.568  9.211   -29.789 1.00 23.60  ? 363 GLU   B CB   1 
ATOM   3167 C  CG   . GLU   B 1 352 ? 22.646  9.624   -28.804 1.00 27.29  ? 363 GLU   B CG   1 
ATOM   3168 C  CD   . GLU   B 1 352 ? 22.885  11.133  -28.765 1.00 29.91  ? 363 GLU   B CD   1 
ATOM   3169 O  OE1  . GLU   B 1 352 ? 22.073  11.894  -29.342 1.00 29.33  ? 363 GLU   B OE1  1 
ATOM   3170 O  OE2  . GLU   B 1 352 ? 23.900  11.546  -28.167 1.00 25.93  ? 363 GLU   B OE2  1 
ATOM   3171 N  N    . GLY   B 1 353 ? 19.778  7.093   -31.581 1.00 20.90  ? 364 GLY   B N    1 
ATOM   3172 C  CA   . GLY   B 1 353 ? 18.519  6.806   -32.262 1.00 23.08  ? 364 GLY   B CA   1 
ATOM   3173 C  C    . GLY   B 1 353 ? 17.772  5.625   -31.665 1.00 21.74  ? 364 GLY   B C    1 
ATOM   3174 O  O    . GLY   B 1 353 ? 16.541  5.635   -31.576 1.00 22.81  ? 364 GLY   B O    1 
ATOM   3175 N  N    . GLN   B 1 354 ? 18.504  4.594   -31.245 1.00 23.48  ? 365 GLN   B N    1 
ATOM   3176 C  CA   . GLN   B 1 354 ? 17.871  3.465   -30.567 1.00 20.17  ? 365 GLN   B CA   1 
ATOM   3177 C  C    . GLN   B 1 354 ? 17.376  3.865   -29.184 1.00 23.11  ? 365 GLN   B C    1 
ATOM   3178 O  O    . GLN   B 1 354 ? 16.292  3.445   -28.762 1.00 20.41  ? 365 GLN   B O    1 
ATOM   3179 C  CB   . GLN   B 1 354 ? 18.861  2.305   -30.454 1.00 18.71  ? 365 GLN   B CB   1 
ATOM   3180 C  CG   . GLN   B 1 354 ? 19.260  1.748   -31.837 1.00 23.23  ? 365 GLN   B CG   1 
ATOM   3181 C  CD   . GLN   B 1 354 ? 20.483  0.861   -31.822 1.00 26.56  ? 365 GLN   B CD   1 
ATOM   3182 O  OE1  . GLN   B 1 354 ? 21.449  1.116   -31.102 1.00 25.46  ? 365 GLN   B OE1  1 
ATOM   3183 N  NE2  . GLN   B 1 354 ? 20.477  -0.161  -32.674 1.00 22.70  ? 365 GLN   B NE2  1 
ATOM   3184 N  N    . ILE   B 1 355 ? 18.162  4.673   -28.465 1.00 20.96  ? 366 ILE   B N    1 
ATOM   3185 C  CA   . ILE   B 1 355 ? 17.738  5.159   -27.152 1.00 21.31  ? 366 ILE   B CA   1 
ATOM   3186 C  C    . ILE   B 1 355 ? 16.478  6.012   -27.273 1.00 23.89  ? 366 ILE   B C    1 
ATOM   3187 O  O    . ILE   B 1 355 ? 15.542  5.877   -26.472 1.00 23.97  ? 366 ILE   B O    1 
ATOM   3188 C  CB   . ILE   B 1 355 ? 18.882  5.931   -26.472 1.00 20.58  ? 366 ILE   B CB   1 
ATOM   3189 C  CG1  . ILE   B 1 355 ? 20.024  4.978   -26.107 1.00 23.94  ? 366 ILE   B CG1  1 
ATOM   3190 C  CG2  . ILE   B 1 355 ? 18.348  6.702   -25.234 1.00 23.95  ? 366 ILE   B CG2  1 
ATOM   3191 C  CD1  . ILE   B 1 355 ? 21.268  5.679   -25.563 1.00 22.95  ? 366 ILE   B CD1  1 
ATOM   3192 N  N    . ALA   B 1 356 ? 16.438  6.906   -28.269 1.00 20.46  ? 367 ALA   B N    1 
ATOM   3193 C  CA   . ALA   B 1 356 ? 15.261  7.751   -28.470 1.00 21.49  ? 367 ALA   B CA   1 
ATOM   3194 C  C    . ALA   B 1 356 ? 14.019  6.916   -28.725 1.00 23.08  ? 367 ALA   B C    1 
ATOM   3195 O  O    . ALA   B 1 356 ? 12.934  7.245   -28.240 1.00 21.05  ? 367 ALA   B O    1 
ATOM   3196 C  CB   . ALA   B 1 356 ? 15.488  8.724   -29.634 1.00 19.25  ? 367 ALA   B CB   1 
ATOM   3197 N  N    . ALA   B 1 357 ? 14.158  5.828   -29.486 1.00 19.63  ? 368 ALA   B N    1 
ATOM   3198 C  CA   . ALA   B 1 357 ? 13.017  4.963   -29.763 1.00 23.01  ? 368 ALA   B CA   1 
ATOM   3199 C  C    . ALA   B 1 357 ? 12.489  4.321   -28.481 1.00 24.85  ? 368 ALA   B C    1 
ATOM   3200 O  O    . ALA   B 1 357 ? 11.275  4.331   -28.222 1.00 22.86  ? 368 ALA   B O    1 
ATOM   3201 C  CB   . ALA   B 1 357 ? 13.415  3.906   -30.800 1.00 22.64  ? 368 ALA   B CB   1 
ATOM   3202 N  N    . VAL   B 1 358 ? 13.395  3.786   -27.649 1.00 18.75  ? 369 VAL   B N    1 
ATOM   3203 C  CA   . VAL   B 1 358 ? 12.991  3.191   -26.369 1.00 19.93  ? 369 VAL   B CA   1 
ATOM   3204 C  C    . VAL   B 1 358 ? 12.312  4.237   -25.488 1.00 19.00  ? 369 VAL   B C    1 
ATOM   3205 O  O    . VAL   B 1 358 ? 11.252  3.990   -24.907 1.00 20.75  ? 369 VAL   B O    1 
ATOM   3206 C  CB   . VAL   B 1 358 ? 14.205  2.579   -25.649 1.00 18.64  ? 369 VAL   B CB   1 
ATOM   3207 C  CG1  . VAL   B 1 358 ? 13.829  2.158   -24.210 1.00 19.06  ? 369 VAL   B CG1  1 
ATOM   3208 C  CG2  . VAL   B 1 358 ? 14.743  1.355   -26.428 1.00 20.17  ? 369 VAL   B CG2  1 
ATOM   3209 N  N    . CYS   B 1 359 ? 12.924  5.420   -25.371 1.00 20.29  ? 370 CYS   B N    1 
ATOM   3210 C  CA   . CYS   B 1 359 ? 12.342  6.483   -24.545 1.00 22.54  ? 370 CYS   B CA   1 
ATOM   3211 C  C    . CYS   B 1 359 ? 10.935  6.855   -25.009 1.00 23.84  ? 370 CYS   B C    1 
ATOM   3212 O  O    . CYS   B 1 359 ? 10.034  7.064   -24.183 1.00 22.18  ? 370 CYS   B O    1 
ATOM   3213 C  CB   . CYS   B 1 359 ? 13.241  7.725   -24.559 1.00 21.88  ? 370 CYS   B CB   1 
ATOM   3214 S  SG   . CYS   B 1 359 ? 14.771  7.517   -23.607 1.00 24.69  ? 370 CYS   B SG   1 
ATOM   3215 N  N    . ARG   B 1 360 ? 10.725  6.949   -26.325 1.00 22.17  ? 371 ARG   B N    1 
ATOM   3216 C  CA   . ARG   B 1 360 ? 9.401   7.302   -26.824 1.00 25.19  ? 371 ARG   B CA   1 
ATOM   3217 C  C    . ARG   B 1 360 ? 8.366   6.247   -26.446 1.00 25.84  ? 371 ARG   B C    1 
ATOM   3218 O  O    . ARG   B 1 360 ? 7.263   6.579   -25.988 1.00 22.83  ? 371 ARG   B O    1 
ATOM   3219 C  CB   . ARG   B 1 360 ? 9.427   7.485   -28.345 1.00 25.25  ? 371 ARG   B CB   1 
ATOM   3220 C  CG   . ARG   B 1 360 ? 8.069   7.935   -28.900 1.00 24.78  ? 371 ARG   B CG   1 
ATOM   3221 C  CD   . ARG   B 1 360 ? 7.925   7.741   -30.396 1.00 28.53  ? 371 ARG   B CD   1 
ATOM   3222 N  NE   . ARG   B 1 360 ? 8.032   6.330   -30.747 1.00 36.28  ? 371 ARG   B NE   1 
ATOM   3223 C  CZ   . ARG   B 1 360 ? 8.858   5.853   -31.668 1.00 43.01  ? 371 ARG   B CZ   1 
ATOM   3224 N  NH1  . ARG   B 1 360 ? 9.534   6.659   -32.471 1.00 31.86  ? 371 ARG   B NH1  1 
ATOM   3225 N  NH2  . ARG   B 1 360 ? 8.983   4.537   -31.807 1.00 36.82  ? 371 ARG   B NH2  1 
ATOM   3226 N  N    . GLU   B 1 361 ? 8.704   4.972   -26.620 1.00 19.22  ? 372 GLU   B N    1 
ATOM   3227 C  CA   . GLU   B 1 361 ? 7.744   3.916   -26.313 1.00 23.41  ? 372 GLU   B CA   1 
ATOM   3228 C  C    . GLU   B 1 361 ? 7.406   3.907   -24.829 1.00 25.89  ? 372 GLU   B C    1 
ATOM   3229 O  O    . GLU   B 1 361 ? 6.242   3.725   -24.447 1.00 25.03  ? 372 GLU   B O    1 
ATOM   3230 C  CB   . GLU   B 1 361 ? 8.303   2.562   -26.756 1.00 19.69  ? 372 GLU   B CB   1 
ATOM   3231 C  CG   . GLU   B 1 361 ? 8.535   2.430   -28.284 1.00 22.22  ? 372 GLU   B CG   1 
ATOM   3232 C  CD   . GLU   B 1 361 ? 7.259   2.608   -29.105 1.00 29.58  ? 372 GLU   B CD   1 
ATOM   3233 O  OE1  . GLU   B 1 361 ? 6.314   1.797   -28.953 1.00 30.41  ? 372 GLU   B OE1  1 
ATOM   3234 O  OE2  . GLU   B 1 361 ? 7.200   3.556   -29.915 1.00 28.00  ? 372 GLU   B OE2  1 
ATOM   3235 N  N    . CYS   B 1 362 ? 8.413   4.120   -23.976 1.00 20.12  ? 373 CYS   B N    1 
ATOM   3236 C  CA   . CYS   B 1 362 ? 8.167   4.184   -22.536 1.00 24.93  ? 373 CYS   B CA   1 
ATOM   3237 C  C    . CYS   B 1 362 ? 7.338   5.405   -22.175 1.00 25.87  ? 373 CYS   B C    1 
ATOM   3238 O  O    . CYS   B 1 362 ? 6.471   5.338   -21.297 1.00 22.63  ? 373 CYS   B O    1 
ATOM   3239 C  CB   . CYS   B 1 362 ? 9.486   4.204   -21.765 1.00 24.90  ? 373 CYS   B CB   1 
ATOM   3240 S  SG   . CYS   B 1 362 ? 10.413  2.651   -21.810 1.00 26.17  ? 373 CYS   B SG   1 
ATOM   3241 N  N    . LEU   B 1 363 ? 7.589   6.532   -22.841 1.00 21.85  ? 374 LEU   B N    1 
ATOM   3242 C  CA   . LEU   B 1 363 ? 6.786   7.723   -22.582 1.00 23.44  ? 374 LEU   B CA   1 
ATOM   3243 C  C    . LEU   B 1 363 ? 5.334   7.528   -22.984 1.00 27.22  ? 374 LEU   B C    1 
ATOM   3244 O  O    . LEU   B 1 363 ? 4.432   8.061   -22.329 1.00 25.54  ? 374 LEU   B O    1 
ATOM   3245 C  CB   . LEU   B 1 363 ? 7.388   8.923   -23.311 1.00 21.02  ? 374 LEU   B CB   1 
ATOM   3246 C  CG   . LEU   B 1 363 ? 8.598   9.513   -22.586 1.00 22.91  ? 374 LEU   B CG   1 
ATOM   3247 C  CD1  . LEU   B 1 363 ? 9.372   10.473  -23.479 1.00 21.14  ? 374 LEU   B CD1  1 
ATOM   3248 C  CD2  . LEU   B 1 363 ? 8.145   10.237  -21.321 1.00 24.68  ? 374 LEU   B CD2  1 
ATOM   3249 N  N    . GLN   B 1 364 ? 5.077   6.760   -24.040 1.00 22.37  ? 375 GLN   B N    1 
ATOM   3250 C  CA   . GLN   B 1 364 ? 3.695   6.474   -24.406 1.00 27.65  ? 375 GLN   B CA   1 
ATOM   3251 C  C    . GLN   B 1 364 ? 2.997   5.674   -23.312 1.00 29.93  ? 375 GLN   B C    1 
ATOM   3252 O  O    . GLN   B 1 364 ? 1.839   5.947   -22.967 1.00 29.01  ? 375 GLN   B O    1 
ATOM   3253 C  CB   . GLN   B 1 364 ? 3.662   5.740   -25.744 1.00 24.39  ? 375 GLN   B CB   1 
ATOM   3254 C  CG   . GLN   B 1 364 ? 4.135   6.640   -26.907 1.00 24.20  ? 375 GLN   B CG   1 
ATOM   3255 C  CD   . GLN   B 1 364 ? 4.425   5.870   -28.181 1.00 33.41  ? 375 GLN   B CD   1 
ATOM   3256 O  OE1  . GLN   B 1 364 ? 4.301   4.640   -28.225 1.00 36.28  ? 375 GLN   B OE1  1 
ATOM   3257 N  NE2  . GLN   B 1 364 ? 4.838   6.589   -29.224 1.00 24.69  ? 375 GLN   B NE2  1 
ATOM   3258 N  N    . ALA   B 1 365 ? 3.693   4.687   -22.745 1.00 26.92  ? 376 ALA   B N    1 
ATOM   3259 C  CA   . ALA   B 1 365 ? 3.117   3.932   -21.638 1.00 26.51  ? 376 ALA   B CA   1 
ATOM   3260 C  C    . ALA   B 1 365 ? 2.872   4.829   -20.432 1.00 24.08  ? 376 ALA   B C    1 
ATOM   3261 O  O    . ALA   B 1 365 ? 1.837   4.718   -19.766 1.00 29.41  ? 376 ALA   B O    1 
ATOM   3262 C  CB   . ALA   B 1 365 ? 4.037   2.767   -21.269 1.00 24.80  ? 376 ALA   B CB   1 
ATOM   3263 N  N    . LEU   B 1 366 ? 3.820   5.725   -20.131 1.00 27.85  ? 377 LEU   B N    1 
ATOM   3264 C  CA   . LEU   B 1 366 ? 3.671   6.594   -18.965 1.00 29.50  ? 377 LEU   B CA   1 
ATOM   3265 C  C    . LEU   B 1 366 ? 2.532   7.593   -19.141 1.00 31.63  ? 377 LEU   B C    1 
ATOM   3266 O  O    . LEU   B 1 366 ? 1.794   7.867   -18.188 1.00 27.71  ? 377 LEU   B O    1 
ATOM   3267 C  CB   . LEU   B 1 366 ? 4.984   7.326   -18.681 1.00 25.83  ? 377 LEU   B CB   1 
ATOM   3268 C  CG   . LEU   B 1 366 ? 6.115   6.429   -18.161 1.00 22.07  ? 377 LEU   B CG   1 
ATOM   3269 C  CD1  . LEU   B 1 366 ? 7.357   7.236   -17.863 1.00 26.02  ? 377 LEU   B CD1  1 
ATOM   3270 C  CD2  . LEU   B 1 366 ? 5.646   5.677   -16.904 1.00 29.17  ? 377 LEU   B CD2  1 
ATOM   3271 N  N    . GLU   B 1 367 ? 2.388   8.174   -20.335 1.00 27.29  ? 378 GLU   B N    1 
ATOM   3272 C  CA   . GLU   B 1 367 ? 1.255   9.072   -20.564 1.00 31.39  ? 378 GLU   B CA   1 
ATOM   3273 C  C    . GLU   B 1 367 ? -0.060  8.353   -20.297 1.00 37.04  ? 378 GLU   B C    1 
ATOM   3274 O  O    . GLU   B 1 367 ? -0.970  8.904   -19.658 1.00 32.03  ? 378 GLU   B O    1 
ATOM   3275 C  CB   . GLU   B 1 367 ? 1.291   9.621   -21.993 1.00 28.22  ? 378 GLU   B CB   1 
ATOM   3276 C  CG   . GLU   B 1 367 ? 0.132   10.563  -22.318 1.00 35.34  ? 378 GLU   B CG   1 
ATOM   3277 C  CD   . GLU   B 1 367 ? 0.022   10.863  -23.799 1.00 47.51  ? 378 GLU   B CD   1 
ATOM   3278 O  OE1  . GLU   B 1 367 ? 0.328   9.966   -24.614 1.00 51.79  ? 378 GLU   B OE1  1 
ATOM   3279 O  OE2  . GLU   B 1 367 ? -0.369  11.997  -24.147 1.00 60.95  ? 378 GLU   B OE2  1 
ATOM   3280 N  N    . PHE   B 1 368 ? -0.166  7.110   -20.770 1.00 31.10  ? 379 PHE   B N    1 
ATOM   3281 C  CA   . PHE   B 1 368 ? -1.366  6.318   -20.536 1.00 32.63  ? 379 PHE   B CA   1 
ATOM   3282 C  C    . PHE   B 1 368 ? -1.585  6.090   -19.043 1.00 32.57  ? 379 PHE   B C    1 
ATOM   3283 O  O    . PHE   B 1 368 ? -2.674  6.352   -18.516 1.00 34.74  ? 379 PHE   B O    1 
ATOM   3284 C  CB   . PHE   B 1 368 ? -1.267  4.988   -21.295 1.00 29.84  ? 379 PHE   B CB   1 
ATOM   3285 C  CG   . PHE   B 1 368 ? -2.300  3.971   -20.867 1.00 37.56  ? 379 PHE   B CG   1 
ATOM   3286 C  CD1  . PHE   B 1 368 ? -3.624  4.097   -21.268 1.00 32.90  ? 379 PHE   B CD1  1 
ATOM   3287 C  CD2  . PHE   B 1 368 ? -1.947  2.903   -20.054 1.00 30.19  ? 379 PHE   B CD2  1 
ATOM   3288 C  CE1  . PHE   B 1 368 ? -4.583  3.174   -20.867 1.00 41.32  ? 379 PHE   B CE1  1 
ATOM   3289 C  CE2  . PHE   B 1 368 ? -2.898  1.973   -19.645 1.00 36.65  ? 379 PHE   B CE2  1 
ATOM   3290 C  CZ   . PHE   B 1 368 ? -4.216  2.108   -20.055 1.00 43.78  ? 379 PHE   B CZ   1 
ATOM   3291 N  N    . LEU   B 1 369 ? -0.546  5.641   -18.333 1.00 29.29  ? 380 LEU   B N    1 
ATOM   3292 C  CA   . LEU   B 1 369 ? -0.693  5.376   -16.901 1.00 26.79  ? 380 LEU   B CA   1 
ATOM   3293 C  C    . LEU   B 1 369 ? -1.021  6.650   -16.128 1.00 34.40  ? 380 LEU   B C    1 
ATOM   3294 O  O    . LEU   B 1 369 ? -1.902  6.657   -15.265 1.00 31.90  ? 380 LEU   B O    1 
ATOM   3295 C  CB   . LEU   B 1 369 ? 0.578   4.735   -16.345 1.00 29.43  ? 380 LEU   B CB   1 
ATOM   3296 C  CG   . LEU   B 1 369 ? 0.902   3.321   -16.837 1.00 25.60  ? 380 LEU   B CG   1 
ATOM   3297 C  CD1  . LEU   B 1 369 ? 2.225   2.886   -16.243 1.00 27.13  ? 380 LEU   B CD1  1 
ATOM   3298 C  CD2  . LEU   B 1 369 ? -0.226  2.357   -16.467 1.00 33.96  ? 380 LEU   B CD2  1 
ATOM   3299 N  N    . HIS   B 1 370 ? -0.299  7.733   -16.408 1.00 29.65  ? 381 HIS   B N    1 
ATOM   3300 C  CA   . HIS   B 1 370 ? -0.515  8.974   -15.673 1.00 36.76  ? 381 HIS   B CA   1 
ATOM   3301 C  C    . HIS   B 1 370 ? -1.898  9.552   -15.945 1.00 38.42  ? 381 HIS   B C    1 
ATOM   3302 O  O    . HIS   B 1 370 ? -2.554  10.060  -15.026 1.00 34.33  ? 381 HIS   B O    1 
ATOM   3303 C  CB   . HIS   B 1 370 ? 0.602   9.955   -16.027 1.00 30.70  ? 381 HIS   B CB   1 
ATOM   3304 C  CG   . HIS   B 1 370 ? 1.948   9.497   -15.566 1.00 25.32  ? 381 HIS   B CG   1 
ATOM   3305 N  ND1  . HIS   B 1 370 ? 3.120   10.149  -15.891 1.00 25.49  ? 381 HIS   B ND1  1 
ATOM   3306 C  CD2  . HIS   B 1 370 ? 2.306   8.443   -14.794 1.00 27.18  ? 381 HIS   B CD2  1 
ATOM   3307 C  CE1  . HIS   B 1 370 ? 4.138   9.520   -15.329 1.00 34.34  ? 381 HIS   B CE1  1 
ATOM   3308 N  NE2  . HIS   B 1 370 ? 3.669   8.484   -14.655 1.00 27.60  ? 381 HIS   B NE2  1 
ATOM   3309 N  N    . SER   B 1 371 ? -2.376  9.460   -17.190 1.00 36.08  ? 382 SER   B N    1 
ATOM   3310 C  CA   . SER   B 1 371 ? -3.730  9.919   -17.483 1.00 32.53  ? 382 SER   B CA   1 
ATOM   3311 C  C    . SER   B 1 371 ? -4.772  9.182   -16.661 1.00 42.37  ? 382 SER   B C    1 
ATOM   3312 O  O    . SER   B 1 371 ? -5.861  9.719   -16.432 1.00 47.23  ? 382 SER   B O    1 
ATOM   3313 C  CB   . SER   B 1 371 ? -4.053  9.720   -18.961 1.00 48.22  ? 382 SER   B CB   1 
ATOM   3314 O  OG   . SER   B 1 371 ? -4.283  8.343   -19.233 1.00 46.21  ? 382 SER   B OG   1 
ATOM   3315 N  N    . ASN   B 1 372 ? -4.455  7.974   -16.206 1.00 37.97  ? 383 ASN   B N    1 
ATOM   3316 C  CA   . ASN   B 1 372 ? -5.327  7.179   -15.356 1.00 43.05  ? 383 ASN   B CA   1 
ATOM   3317 C  C    . ASN   B 1 372 ? -4.910  7.223   -13.891 1.00 43.77  ? 383 ASN   B C    1 
ATOM   3318 O  O    . ASN   B 1 372 ? -5.368  6.389   -13.108 1.00 42.41  ? 383 ASN   B O    1 
ATOM   3319 C  CB   . ASN   B 1 372 ? -5.353  5.732   -15.857 1.00 45.02  ? 383 ASN   B CB   1 
ATOM   3320 C  CG   . ASN   B 1 372 ? -6.189  5.566   -17.114 1.00 51.43  ? 383 ASN   B CG   1 
ATOM   3321 O  OD1  . ASN   B 1 372 ? -7.331  6.018   -17.177 1.00 56.79  ? 383 ASN   B OD1  1 
ATOM   3322 N  ND2  . ASN   B 1 372 ? -5.603  4.960   -18.140 1.00 45.96  ? 383 ASN   B ND2  1 
ATOM   3323 N  N    . GLN   B 1 373 ? -4.043  8.168   -13.510 1.00 38.92  ? 384 GLN   B N    1 
ATOM   3324 C  CA   . GLN   B 1 373 ? -3.636  8.367   -12.118 1.00 38.08  ? 384 GLN   B CA   1 
ATOM   3325 C  C    . GLN   B 1 373 ? -2.906  7.158   -11.536 1.00 42.49  ? 384 GLN   B C    1 
ATOM   3326 O  O    . GLN   B 1 373 ? -2.982  6.890   -10.337 1.00 41.97  ? 384 GLN   B O    1 
ATOM   3327 C  CB   . GLN   B 1 373 ? -4.833  8.756   -11.248 1.00 43.55  ? 384 GLN   B CB   1 
ATOM   3328 C  CG   . GLN   B 1 373 ? -5.254  10.209  -11.457 1.00 60.95  ? 384 GLN   B CG   1 
ATOM   3329 C  CD   . GLN   B 1 373 ? -6.031  10.409  -12.743 1.00 65.72  ? 384 GLN   B CD   1 
ATOM   3330 O  OE1  . GLN   B 1 373 ? -6.790  9.534   -13.161 1.00 70.80  ? 384 GLN   B OE1  1 
ATOM   3331 N  NE2  . GLN   B 1 373 ? -5.824  11.553  -13.395 1.00 67.60  ? 384 GLN   B NE2  1 
ATOM   3332 N  N    . VAL   B 1 374 ? -2.156  6.443   -12.364 1.00 35.49  ? 385 VAL   B N    1 
ATOM   3333 C  CA   . VAL   B 1 374 ? -1.312  5.344   -11.905 1.00 35.30  ? 385 VAL   B CA   1 
ATOM   3334 C  C    . VAL   B 1 374 ? 0.124   5.830   -11.891 1.00 31.71  ? 385 VAL   B C    1 
ATOM   3335 O  O    . VAL   B 1 374 ? 0.614   6.351   -12.898 1.00 39.02  ? 385 VAL   B O    1 
ATOM   3336 C  CB   . VAL   B 1 374 ? -1.446  4.106   -12.811 1.00 32.94  ? 385 VAL   B CB   1 
ATOM   3337 C  CG1  . VAL   B 1 374 ? -0.437  3.051   -12.393 1.00 39.12  ? 385 VAL   B CG1  1 
ATOM   3338 C  CG2  . VAL   B 1 374 ? -2.845  3.540   -12.752 1.00 37.48  ? 385 VAL   B CG2  1 
ATOM   3339 N  N    . ILE   B 1 375 ? 0.807   5.645   -10.766 1.00 29.80  ? 386 ILE   B N    1 
ATOM   3340 C  CA   . ILE   B 1 375 ? 2.237   5.912   -10.669 1.00 30.16  ? 386 ILE   B CA   1 
ATOM   3341 C  C    . ILE   B 1 375 ? 2.968   4.578   -10.695 1.00 36.68  ? 386 ILE   B C    1 
ATOM   3342 O  O    . ILE   B 1 375 ? 2.733   3.720   -9.835  1.00 38.22  ? 386 ILE   B O    1 
ATOM   3343 C  CB   . ILE   B 1 375 ? 2.575   6.694   -9.394  1.00 34.66  ? 386 ILE   B CB   1 
ATOM   3344 C  CG1  . ILE   B 1 375 ? 1.723   7.969   -9.321  1.00 33.64  ? 386 ILE   B CG1  1 
ATOM   3345 C  CG2  . ILE   B 1 375 ? 4.084   6.961   -9.319  1.00 29.74  ? 386 ILE   B CG2  1 
ATOM   3346 C  CD1  . ILE   B 1 375 ? 1.863   8.720   -8.024  1.00 43.94  ? 386 ILE   B CD1  1 
ATOM   3347 N  N    . HIS   B 1 376 ? 3.886   4.411   -11.651 1.00 29.52  ? 387 HIS   B N    1 
ATOM   3348 C  CA   . HIS   B 1 376 ? 4.528   3.111   -11.806 1.00 27.86  ? 387 HIS   B CA   1 
ATOM   3349 C  C    . HIS   B 1 376 ? 5.488   2.829   -10.660 1.00 31.78  ? 387 HIS   B C    1 
ATOM   3350 O  O    . HIS   B 1 376 ? 5.418   1.767   -10.035 1.00 29.46  ? 387 HIS   B O    1 
ATOM   3351 C  CB   . HIS   B 1 376 ? 5.264   3.036   -13.141 1.00 24.72  ? 387 HIS   B CB   1 
ATOM   3352 C  CG   . HIS   B 1 376 ? 5.805   1.677   -13.447 1.00 29.96  ? 387 HIS   B CG   1 
ATOM   3353 N  ND1  . HIS   B 1 376 ? 6.911   1.155   -12.810 1.00 28.54  ? 387 HIS   B ND1  1 
ATOM   3354 C  CD2  . HIS   B 1 376 ? 5.397   0.735   -14.332 1.00 32.18  ? 387 HIS   B CD2  1 
ATOM   3355 C  CE1  . HIS   B 1 376 ? 7.162   -0.051  -13.291 1.00 34.18  ? 387 HIS   B CE1  1 
ATOM   3356 N  NE2  . HIS   B 1 376 ? 6.260   -0.327  -14.217 1.00 31.03  ? 387 HIS   B NE2  1 
ATOM   3357 N  N    . ARG   B 1 377 ? 6.390   3.773   -10.373 1.00 27.27  ? 388 ARG   B N    1 
ATOM   3358 C  CA   . ARG   B 1 377 ? 7.373   3.788   -9.295  1.00 30.53  ? 388 ARG   B CA   1 
ATOM   3359 C  C    . ARG   B 1 377 ? 8.612   2.935   -9.539  1.00 30.86  ? 388 ARG   B C    1 
ATOM   3360 O  O    . ARG   B 1 377 ? 9.579   3.082   -8.786  1.00 31.59  ? 388 ARG   B O    1 
ATOM   3361 C  CB   . ARG   B 1 377 ? 6.783   3.331   -7.950  1.00 33.06  ? 388 ARG   B CB   1 
ATOM   3362 C  CG   . ARG   B 1 377 ? 5.621   4.147   -7.502  1.00 33.18  ? 388 ARG   B CG   1 
ATOM   3363 C  CD   . ARG   B 1 377 ? 5.153   3.702   -6.125  1.00 36.91  ? 388 ARG   B CD   1 
ATOM   3364 N  NE   . ARG   B 1 377 ? 4.136   4.602   -5.602  1.00 44.64  ? 388 ARG   B NE   1 
ATOM   3365 C  CZ   . ARG   B 1 377 ? 2.855   4.568   -5.944  1.00 49.53  ? 388 ARG   B CZ   1 
ATOM   3366 N  NH1  . ARG   B 1 377 ? 2.396   3.695   -6.826  1.00 42.97  ? 388 ARG   B NH1  1 
ATOM   3367 N  NH2  . ARG   B 1 377 ? 2.015   5.441   -5.393  1.00 46.24  ? 388 ARG   B NH2  1 
ATOM   3368 N  N    . ASN   B 1 378 ? 8.657   2.084   -10.563 1.00 26.05  ? 389 ASN   B N    1 
ATOM   3369 C  CA   . ASN   B 1 378 ? 9.839   1.248   -10.778 1.00 26.86  ? 389 ASN   B CA   1 
ATOM   3370 C  C    . ASN   B 1 378 ? 10.201  1.211   -12.256 1.00 29.69  ? 389 ASN   B C    1 
ATOM   3371 O  O    . ASN   B 1 378 ? 10.466  0.156   -12.841 1.00 28.96  ? 389 ASN   B O    1 
ATOM   3372 C  CB   . ASN   B 1 378 ? 9.643   -0.148  -10.184 1.00 29.64  ? 389 ASN   B CB   1 
ATOM   3373 C  CG   . ASN   B 1 378 ? 9.575   -0.103  -8.665  1.00 42.21  ? 389 ASN   B CG   1 
ATOM   3374 O  OD1  . ASN   B 1 378 ? 10.578  0.157   -7.989  1.00 39.12  ? 389 ASN   B OD1  1 
ATOM   3375 N  ND2  . ASN   B 1 378 ? 8.382   -0.296  -8.124  1.00 41.67  ? 389 ASN   B ND2  1 
ATOM   3376 N  N    . ILE   B 1 379 ? 10.211  2.388   -12.877 1.00 22.69  ? 390 ILE   B N    1 
ATOM   3377 C  CA   . ILE   B 1 379 ? 10.719  2.487   -14.239 1.00 21.79  ? 390 ILE   B CA   1 
ATOM   3378 C  C    . ILE   B 1 379 ? 12.226  2.270   -14.171 1.00 25.64  ? 390 ILE   B C    1 
ATOM   3379 O  O    . ILE   B 1 379 ? 12.987  3.154   -13.765 1.00 25.54  ? 390 ILE   B O    1 
ATOM   3380 C  CB   . ILE   B 1 379 ? 10.365  3.835   -14.872 1.00 22.43  ? 390 ILE   B CB   1 
ATOM   3381 C  CG1  . ILE   B 1 379 ? 8.846   3.996   -14.904 1.00 26.59  ? 390 ILE   B CG1  1 
ATOM   3382 C  CG2  . ILE   B 1 379 ? 10.991  3.946   -16.290 1.00 26.42  ? 390 ILE   B CG2  1 
ATOM   3383 C  CD1  . ILE   B 1 379 ? 8.167   2.971   -15.805 1.00 24.40  ? 390 ILE   B CD1  1 
ATOM   3384 N  N    . LYS   B 1 380 ? 12.665  1.116   -14.648 1.00 22.59  ? 391 LYS   B N    1 
ATOM   3385 C  CA   . LYS   B 1 380 ? 14.076  0.778   -14.666 1.00 20.48  ? 391 LYS   B CA   1 
ATOM   3386 C  C    . LYS   B 1 380 ? 14.233  -0.344  -15.676 1.00 21.29  ? 391 LYS   B C    1 
ATOM   3387 O  O    . LYS   B 1 380 ? 13.255  -0.984  -16.069 1.00 21.49  ? 391 LYS   B O    1 
ATOM   3388 C  CB   . LYS   B 1 380 ? 14.591  0.372   -13.275 1.00 25.65  ? 391 LYS   B CB   1 
ATOM   3389 C  CG   . LYS   B 1 380 ? 13.838  -0.754  -12.589 1.00 31.92  ? 391 LYS   B CG   1 
ATOM   3390 C  CD   . LYS   B 1 380 ? 14.157  -0.740  -11.071 1.00 29.34  ? 391 LYS   B CD   1 
ATOM   3391 C  CE   . LYS   B 1 380 ? 13.594  -1.943  -10.364 1.00 38.96  ? 391 LYS   B CE   1 
ATOM   3392 N  NZ   . LYS   B 1 380 ? 14.527  -3.098  -10.543 1.00 46.20  ? 391 LYS   B NZ   1 
ATOM   3393 N  N    . SER   B 1 381 ? 15.476  -0.581  -16.081 1.00 23.46  ? 392 SER   B N    1 
ATOM   3394 C  CA   . SER   B 1 381 ? 15.719  -1.422  -17.255 1.00 21.53  ? 392 SER   B CA   1 
ATOM   3395 C  C    . SER   B 1 381 ? 15.218  -2.865  -17.100 1.00 24.24  ? 392 SER   B C    1 
ATOM   3396 O  O    . SER   B 1 381 ? 14.850  -3.494  -18.105 1.00 22.16  ? 392 SER   B O    1 
ATOM   3397 C  CB   . SER   B 1 381 ? 17.208  -1.358  -17.615 1.00 21.60  ? 392 SER   B CB   1 
ATOM   3398 O  OG   . SER   B 1 381 ? 18.016  -1.939  -16.619 1.00 25.21  ? 392 SER   B OG   1 
ATOM   3399 N  N    A ASP   B 1 382 ? 15.203  -3.403  -15.869 0.48 22.54  ? 393 ASP   B N    1 
ATOM   3400 N  N    B ASP   B 1 382 ? 15.182  -3.413  -15.887 0.52 22.52  ? 393 ASP   B N    1 
ATOM   3401 C  CA   A ASP   B 1 382 ? 14.704  -4.761  -15.640 0.48 25.51  ? 393 ASP   B CA   1 
ATOM   3402 C  CA   B ASP   B 1 382 ? 14.724  -4.795  -15.771 0.52 25.36  ? 393 ASP   B CA   1 
ATOM   3403 C  C    A ASP   B 1 382 ? 13.230  -4.890  -15.992 0.48 25.57  ? 393 ASP   B C    1 
ATOM   3404 C  C    B ASP   B 1 382 ? 13.203  -4.922  -15.795 0.52 25.68  ? 393 ASP   B C    1 
ATOM   3405 O  O    A ASP   B 1 382 ? 12.768  -5.984  -16.337 0.48 29.16  ? 393 ASP   B O    1 
ATOM   3406 O  O    B ASP   B 1 382 ? 12.694  -6.050  -15.758 0.52 27.05  ? 393 ASP   B O    1 
ATOM   3407 C  CB   A ASP   B 1 382 ? 14.875  -5.181  -14.172 0.48 28.79  ? 393 ASP   B CB   1 
ATOM   3408 C  CB   B ASP   B 1 382 ? 15.299  -5.459  -14.506 0.52 29.72  ? 393 ASP   B CB   1 
ATOM   3409 C  CG   A ASP   B 1 382 ? 16.313  -5.449  -13.787 0.48 31.38  ? 393 ASP   B CG   1 
ATOM   3410 C  CG   B ASP   B 1 382 ? 14.629  -4.997  -13.227 0.52 29.26  ? 393 ASP   B CG   1 
ATOM   3411 O  OD1  A ASP   B 1 382 ? 17.125  -5.810  -14.658 0.48 34.81  ? 393 ASP   B OD1  1 
ATOM   3412 O  OD1  B ASP   B 1 382 ? 14.012  -3.915  -13.216 0.52 29.85  ? 393 ASP   B OD1  1 
ATOM   3413 O  OD2  A ASP   B 1 382 ? 16.633  -5.300  -12.589 0.48 44.26  ? 393 ASP   B OD2  1 
ATOM   3414 O  OD2  B ASP   B 1 382 ? 14.739  -5.722  -12.215 0.52 39.51  ? 393 ASP   B OD2  1 
ATOM   3415 N  N    . ASN   B 1 383 ? 12.472  -3.804  -15.857 1.00 24.47  ? 394 ASN   B N    1 
ATOM   3416 C  CA   . ASN   B 1 383 ? 11.027  -3.813  -16.037 1.00 24.30  ? 394 ASN   B CA   1 
ATOM   3417 C  C    . ASN   B 1 383 ? 10.604  -3.346  -17.430 1.00 26.11  ? 394 ASN   B C    1 
ATOM   3418 O  O    . ASN   B 1 383 ? 9.409   -3.208  -17.687 1.00 29.12  ? 394 ASN   B O    1 
ATOM   3419 C  CB   . ASN   B 1 383 ? 10.371  -2.931  -14.971 1.00 23.36  ? 394 ASN   B CB   1 
ATOM   3420 C  CG   . ASN   B 1 383 ? 10.481  -3.532  -13.583 1.00 25.90  ? 394 ASN   B CG   1 
ATOM   3421 O  OD1  . ASN   B 1 383 ? 10.651  -4.742  -13.433 1.00 33.05  ? 394 ASN   B OD1  1 
ATOM   3422 N  ND2  . ASN   B 1 383 ? 10.415  -2.689  -12.564 1.00 34.68  ? 394 ASN   B ND2  1 
ATOM   3423 N  N    . ILE   B 1 384 ? 11.544  -3.164  -18.347 1.00 22.89  ? 395 ILE   B N    1 
ATOM   3424 C  CA   . ILE   B 1 384 ? 11.248  -2.881  -19.748 1.00 20.88  ? 395 ILE   B CA   1 
ATOM   3425 C  C    . ILE   B 1 384 ? 11.532  -4.168  -20.512 1.00 21.29  ? 395 ILE   B C    1 
ATOM   3426 O  O    . ILE   B 1 384 ? 12.675  -4.638  -20.513 1.00 24.00  ? 395 ILE   B O    1 
ATOM   3427 C  CB   . ILE   B 1 384 ? 12.131  -1.750  -20.296 1.00 23.76  ? 395 ILE   B CB   1 
ATOM   3428 C  CG1  . ILE   B 1 384 ? 12.035  -0.484  -19.429 1.00 30.66  ? 395 ILE   B CG1  1 
ATOM   3429 C  CG2  . ILE   B 1 384 ? 11.783  -1.479  -21.769 1.00 23.06  ? 395 ILE   B CG2  1 
ATOM   3430 C  CD1  . ILE   B 1 384 ? 10.662  0.013   -19.255 1.00 31.23  ? 395 ILE   B CD1  1 
ATOM   3431 N  N    . LEU   B 1 385 ? 10.515  -4.736  -21.165 1.00 21.39  ? 396 LEU   B N    1 
ATOM   3432 C  CA   . LEU   B 1 385 ? 10.687  -5.971  -21.923 1.00 24.48  ? 396 LEU   B CA   1 
ATOM   3433 C  C    . LEU   B 1 385 ? 10.595  -5.697  -23.418 1.00 25.59  ? 396 LEU   B C    1 
ATOM   3434 O  O    . LEU   B 1 385 ? 9.885   -4.786  -23.853 1.00 24.77  ? 396 LEU   B O    1 
ATOM   3435 C  CB   . LEU   B 1 385 ? 9.641   -7.016  -21.523 1.00 25.79  ? 396 LEU   B CB   1 
ATOM   3436 C  CG   . LEU   B 1 385 ? 9.585   -7.264  -20.007 1.00 30.78  ? 396 LEU   B CG   1 
ATOM   3437 C  CD1  . LEU   B 1 385 ? 8.631   -8.385  -19.670 1.00 33.26  ? 396 LEU   B CD1  1 
ATOM   3438 C  CD2  . LEU   B 1 385 ? 10.965  -7.565  -19.451 1.00 32.33  ? 396 LEU   B CD2  1 
ATOM   3439 N  N    . LEU   B 1 386 ? 11.320  -6.493  -24.207 1.00 25.19  ? 397 LEU   B N    1 
ATOM   3440 C  CA   . LEU   B 1 386 ? 11.394  -6.308  -25.654 1.00 22.02  ? 397 LEU   B CA   1 
ATOM   3441 C  C    . LEU   B 1 386 ? 10.765  -7.481  -26.413 1.00 25.80  ? 397 LEU   B C    1 
ATOM   3442 O  O    . LEU   B 1 386 ? 10.962  -8.650  -26.064 1.00 27.18  ? 397 LEU   B O    1 
ATOM   3443 C  CB   . LEU   B 1 386 ? 12.848  -6.138  -26.097 1.00 22.74  ? 397 LEU   B CB   1 
ATOM   3444 C  CG   . LEU   B 1 386 ? 13.596  -5.054  -25.312 1.00 25.66  ? 397 LEU   B CG   1 
ATOM   3445 C  CD1  . LEU   B 1 386 ? 15.086  -5.145  -25.625 1.00 27.51  ? 397 LEU   B CD1  1 
ATOM   3446 C  CD2  . LEU   B 1 386 ? 13.040  -3.667  -25.643 1.00 25.40  ? 397 LEU   B CD2  1 
ATOM   3447 N  N    . GLY   B 1 387 ? 10.010  -7.161  -27.461 1.00 26.42  ? 398 GLY   B N    1 
ATOM   3448 C  CA   . GLY   B 1 387 ? 9.491   -8.178  -28.342 1.00 31.46  ? 398 GLY   B CA   1 
ATOM   3449 C  C    . GLY   B 1 387 ? 10.474  -8.484  -29.453 1.00 30.96  ? 398 GLY   B C    1 
ATOM   3450 O  O    . GLY   B 1 387 ? 11.353  -7.682  -29.760 1.00 26.38  ? 398 GLY   B O    1 
ATOM   3451 N  N    . MET   B 1 388 ? 10.304  -9.651  -30.073 1.00 27.25  ? 399 MET   B N    1 
ATOM   3452 C  CA   . MET   B 1 388 ? 11.200  -10.046 -31.156 1.00 30.82  ? 399 MET   B CA   1 
ATOM   3453 C  C    . MET   B 1 388 ? 11.065  -9.156  -32.387 1.00 37.74  ? 399 MET   B C    1 
ATOM   3454 O  O    . MET   B 1 388 ? 11.935  -9.198  -33.265 1.00 36.88  ? 399 MET   B O    1 
ATOM   3455 C  CB   . MET   B 1 388 ? 10.961  -11.510 -31.528 1.00 36.53  ? 399 MET   B CB   1 
ATOM   3456 C  CG   . MET   B 1 388 ? 11.448  -12.517 -30.472 1.00 35.47  ? 399 MET   B CG   1 
ATOM   3457 S  SD   . MET   B 1 388 ? 13.114  -12.246 -29.821 1.00 39.16  ? 399 MET   B SD   1 
ATOM   3458 C  CE   . MET   B 1 388 ? 14.138  -12.565 -31.259 1.00 39.28  ? 399 MET   B CE   1 
ATOM   3459 N  N    . ASP   B 1 389 ? 10.011  -8.352  -32.473 1.00 30.14  ? 400 ASP   B N    1 
ATOM   3460 C  CA   . ASP   B 1 389 ? 9.878   -7.362  -33.529 1.00 27.67  ? 400 ASP   B CA   1 
ATOM   3461 C  C    . ASP   B 1 389 ? 10.384  -5.992  -33.109 1.00 28.85  ? 400 ASP   B C    1 
ATOM   3462 O  O    . ASP   B 1 389 ? 10.213  -5.022  -33.855 1.00 35.25  ? 400 ASP   B O    1 
ATOM   3463 C  CB   . ASP   B 1 389 ? 8.418   -7.264  -33.987 1.00 37.87  ? 400 ASP   B CB   1 
ATOM   3464 C  CG   . ASP   B 1 389 ? 7.476   -6.865  -32.870 1.00 40.17  ? 400 ASP   B CG   1 
ATOM   3465 O  OD1  . ASP   B 1 389 ? 7.899   -6.823  -31.688 1.00 33.01  ? 400 ASP   B OD1  1 
ATOM   3466 O  OD2  . ASP   B 1 389 ? 6.297   -6.603  -33.187 1.00 41.40  ? 400 ASP   B OD2  1 
ATOM   3467 N  N    . GLY   B 1 390 ? 11.046  -5.894  -31.964 1.00 27.20  ? 401 GLY   B N    1 
ATOM   3468 C  CA   . GLY   B 1 390 ? 11.476  -4.610  -31.444 1.00 27.06  ? 401 GLY   B CA   1 
ATOM   3469 C  C    . GLY   B 1 390 ? 10.456  -3.880  -30.595 1.00 30.50  ? 401 GLY   B C    1 
ATOM   3470 O  O    . GLY   B 1 390 ? 10.708  -2.730  -30.215 1.00 27.40  ? 401 GLY   B O    1 
ATOM   3471 N  N    A SER   B 1 391 ? 9.319   -4.499  -30.281 0.46 28.10  ? 402 SER   B N    1 
ATOM   3472 N  N    B SER   B 1 391 ? 9.316   -4.505  -30.290 0.54 28.07  ? 402 SER   B N    1 
ATOM   3473 C  CA   A SER   B 1 391 ? 8.336   -3.834  -29.438 0.46 29.94  ? 402 SER   B CA   1 
ATOM   3474 C  CA   B SER   B 1 391 ? 8.335   -3.886  -29.408 0.54 29.96  ? 402 SER   B CA   1 
ATOM   3475 C  C    A SER   B 1 391 ? 8.895   -3.627  -28.033 0.46 27.17  ? 402 SER   B C    1 
ATOM   3476 C  C    B SER   B 1 391 ? 8.956   -3.593  -28.046 0.54 27.14  ? 402 SER   B C    1 
ATOM   3477 O  O    A SER   B 1 391 ? 9.697   -4.422  -27.535 0.46 27.01  ? 402 SER   B O    1 
ATOM   3478 O  O    B SER   B 1 391 ? 9.858   -4.297  -27.585 0.54 26.96  ? 402 SER   B O    1 
ATOM   3479 C  CB   A SER   B 1 391 ? 7.036   -4.641  -29.379 0.46 29.11  ? 402 SER   B CB   1 
ATOM   3480 C  CB   B SER   B 1 391 ? 7.113   -4.793  -29.238 0.54 29.33  ? 402 SER   B CB   1 
ATOM   3481 O  OG   A SER   B 1 391 ? 7.208   -5.831  -28.633 0.46 28.65  ? 402 SER   B OG   1 
ATOM   3482 O  OG   B SER   B 1 391 ? 6.338   -4.855  -30.418 0.54 30.15  ? 402 SER   B OG   1 
ATOM   3483 N  N    . VAL   B 1 392 ? 8.464   -2.538  -27.400 1.00 24.63  ? 403 VAL   B N    1 
ATOM   3484 C  CA   . VAL   B 1 392 ? 8.967   -2.097  -26.103 1.00 27.10  ? 403 VAL   B CA   1 
ATOM   3485 C  C    . VAL   B 1 392 ? 7.770   -1.918  -25.177 1.00 24.24  ? 403 VAL   B C    1 
ATOM   3486 O  O    . VAL   B 1 392 ? 6.860   -1.142  -25.491 1.00 24.77  ? 403 VAL   B O    1 
ATOM   3487 C  CB   . VAL   B 1 392 ? 9.750   -0.779  -26.224 1.00 23.85  ? 403 VAL   B CB   1 
ATOM   3488 C  CG1  . VAL   B 1 392 ? 10.231  -0.283  -24.841 1.00 22.97  ? 403 VAL   B CG1  1 
ATOM   3489 C  CG2  . VAL   B 1 392 ? 10.922  -0.912  -27.224 1.00 26.64  ? 403 VAL   B CG2  1 
ATOM   3490 N  N    . LYS   B 1 393 ? 7.757   -2.631  -24.047 1.00 20.61  ? 404 LYS   B N    1 
ATOM   3491 C  CA   . LYS   B 1 393 ? 6.599   -2.592  -23.147 1.00 24.99  ? 404 LYS   B CA   1 
ATOM   3492 C  C    . LYS   B 1 393 ? 7.030   -2.635  -21.685 1.00 28.94  ? 404 LYS   B C    1 
ATOM   3493 O  O    . LYS   B 1 393 ? 8.017   -3.291  -21.335 1.00 25.75  ? 404 LYS   B O    1 
ATOM   3494 C  CB   . LYS   B 1 393 ? 5.640   -3.773  -23.401 1.00 30.55  ? 404 LYS   B CB   1 
ATOM   3495 C  CG   . LYS   B 1 393 ? 5.123   -3.876  -24.844 1.00 28.51  ? 404 LYS   B CG   1 
ATOM   3496 C  CD   . LYS   B 1 393 ? 4.149   -5.036  -25.008 1.00 32.96  ? 404 LYS   B CD   1 
ATOM   3497 C  CE   . LYS   B 1 393 ? 3.712   -5.193  -26.472 1.00 31.93  ? 404 LYS   B CE   1 
ATOM   3498 N  NZ   . LYS   B 1 393 ? 2.517   -6.062  -26.631 1.00 36.16  ? 404 LYS   B NZ   1 
ATOM   3499 N  N    . LEU   B 1 394 ? 6.261   -1.947  -20.827 1.00 25.66  ? 405 LEU   B N    1 
ATOM   3500 C  CA   . LEU   B 1 394 ? 6.452   -2.018  -19.379 1.00 26.80  ? 405 LEU   B CA   1 
ATOM   3501 C  C    . LEU   B 1 394 ? 5.782   -3.295  -18.890 1.00 27.23  ? 405 LEU   B C    1 
ATOM   3502 O  O    . LEU   B 1 394 ? 4.720   -3.665  -19.389 1.00 30.05  ? 405 LEU   B O    1 
ATOM   3503 C  CB   . LEU   B 1 394 ? 5.788   -0.840  -18.659 1.00 29.81  ? 405 LEU   B CB   1 
ATOM   3504 C  CG   . LEU   B 1 394 ? 5.983   0.611   -19.074 1.00 38.19  ? 405 LEU   B CG   1 
ATOM   3505 C  CD1  . LEU   B 1 394 ? 5.323   1.524   -18.040 1.00 30.68  ? 405 LEU   B CD1  1 
ATOM   3506 C  CD2  . LEU   B 1 394 ? 7.434   0.932   -19.192 1.00 33.36  ? 405 LEU   B CD2  1 
ATOM   3507 N  N    . THR   B 1 395 ? 6.387   -3.966  -17.905 1.00 31.52  ? 406 THR   B N    1 
ATOM   3508 C  CA   . THR   B 1 395 ? 5.874   -5.302  -17.586 1.00 38.27  ? 406 THR   B CA   1 
ATOM   3509 C  C    . THR   B 1 395 ? 4.554   -5.268  -16.828 1.00 45.73  ? 406 THR   B C    1 
ATOM   3510 O  O    . THR   B 1 395 ? 3.733   -6.179  -16.995 1.00 40.91  ? 406 THR   B O    1 
ATOM   3511 C  CB   . THR   B 1 395 ? 6.907   -6.145  -16.825 1.00 33.43  ? 406 THR   B CB   1 
ATOM   3512 O  OG1  . THR   B 1 395 ? 6.240   -7.216  -16.137 1.00 41.89  ? 406 THR   B OG1  1 
ATOM   3513 C  CG2  . THR   B 1 395 ? 7.673   -5.350  -15.839 1.00 50.22  ? 406 THR   B CG2  1 
ATOM   3514 N  N    . ASP   B 1 396 ? 4.301   -4.244  -16.020 1.00 42.48  ? 407 ASP   B N    1 
ATOM   3515 C  CA   . ASP   B 1 396 ? 2.998   -4.146  -15.367 1.00 41.42  ? 407 ASP   B CA   1 
ATOM   3516 C  C    . ASP   B 1 396 ? 2.713   -2.680  -15.064 1.00 49.93  ? 407 ASP   B C    1 
ATOM   3517 O  O    . ASP   B 1 396 ? 3.398   -1.781  -15.560 1.00 40.88  ? 407 ASP   B O    1 
ATOM   3518 C  CB   . ASP   B 1 396 ? 2.947   -5.027  -14.107 1.00 52.74  ? 407 ASP   B CB   1 
ATOM   3519 C  CG   . ASP   B 1 396 ? 4.151   -4.826  -13.185 1.00 62.26  ? 407 ASP   B CG   1 
ATOM   3520 O  OD1  . ASP   B 1 396 ? 4.475   -3.665  -12.834 1.00 45.45  ? 407 ASP   B OD1  1 
ATOM   3521 O  OD2  . ASP   B 1 396 ? 4.759   -5.844  -12.786 1.00 64.91  ? 407 ASP   B OD2  1 
ATOM   3522 N  N    . PHE   B 1 397 ? 1.703   -2.440  -14.234 1.00 49.97  ? 408 PHE   B N    1 
ATOM   3523 C  CA   . PHE   B 1 397 ? 1.376   -1.088  -13.802 1.00 51.31  ? 408 PHE   B CA   1 
ATOM   3524 C  C    . PHE   B 1 397 ? 2.224   -0.647  -12.625 1.00 51.07  ? 408 PHE   B C    1 
ATOM   3525 O  O    . PHE   B 1 397 ? 1.894   0.361   -11.993 1.00 55.21  ? 408 PHE   B O    1 
ATOM   3526 C  CB   . PHE   B 1 397 ? -0.098  -0.980  -13.387 1.00 52.35  ? 408 PHE   B CB   1 
ATOM   3527 C  CG   . PHE   B 1 397 ? -1.077  -0.918  -14.529 1.00 50.37  ? 408 PHE   B CG   1 
ATOM   3528 C  CD1  . PHE   B 1 397 ? -0.757  -1.401  -15.784 1.00 55.44  ? 408 PHE   B CD1  1 
ATOM   3529 C  CD2  . PHE   B 1 397 ? -2.331  -0.358  -14.333 1.00 51.87  ? 408 PHE   B CD2  1 
ATOM   3530 C  CE1  . PHE   B 1 397 ? -1.677  -1.332  -16.821 1.00 48.93  ? 408 PHE   B CE1  1 
ATOM   3531 C  CE2  . PHE   B 1 397 ? -3.250  -0.282  -15.362 1.00 54.62  ? 408 PHE   B CE2  1 
ATOM   3532 C  CZ   . PHE   B 1 397 ? -2.924  -0.766  -16.607 1.00 49.67  ? 408 PHE   B CZ   1 
ATOM   3533 N  N    . GLY   B 1 398 ? 3.299   -1.365  -12.306 1.00 43.30  ? 409 GLY   B N    1 
ATOM   3534 C  CA   . GLY   B 1 398 ? 4.004   -1.084  -11.080 1.00 46.44  ? 409 GLY   B CA   1 
ATOM   3535 C  C    . GLY   B 1 398 ? 3.554   -1.925  -9.909  1.00 66.74  ? 409 GLY   B C    1 
ATOM   3536 O  O    . GLY   B 1 398 ? 3.954   -1.632  -8.777  1.00 69.14  ? 409 GLY   B O    1 
ATOM   3537 N  N    . PHE   B 1 399 ? 2.651   -2.880  -10.137 1.00 69.67  ? 410 PHE   B N    1 
ATOM   3538 C  CA   . PHE   B 1 399 ? 2.111   -3.797  -9.123  1.00 76.90  ? 410 PHE   B CA   1 
ATOM   3539 C  C    . PHE   B 1 399 ? 1.505   -3.020  -7.956  1.00 79.92  ? 410 PHE   B C    1 
ATOM   3540 O  O    . PHE   B 1 399 ? 0.789   -3.584  -7.130  1.00 91.58  ? 410 PHE   B O    1 
ATOM   3541 C  CB   . PHE   B 1 399 ? 3.179   -4.808  -8.630  1.00 77.23  ? 410 PHE   B CB   1 
ATOM   3542 C  CG   . PHE   B 1 399 ? 4.158   -4.259  -7.606  1.00 75.57  ? 410 PHE   B CG   1 
ATOM   3543 C  CD1  . PHE   B 1 399 ? 3.802   -4.130  -6.268  1.00 78.67  ? 410 PHE   B CD1  1 
ATOM   3544 C  CD2  . PHE   B 1 399 ? 5.453   -3.923  -7.977  1.00 76.73  ? 410 PHE   B CD2  1 
ATOM   3545 C  CE1  . PHE   B 1 399 ? 4.698   -3.632  -5.337  1.00 78.15  ? 410 PHE   B CE1  1 
ATOM   3546 C  CE2  . PHE   B 1 399 ? 6.352   -3.423  -7.048  1.00 74.09  ? 410 PHE   B CE2  1 
ATOM   3547 C  CZ   . PHE   B 1 399 ? 5.975   -3.283  -5.727  1.00 75.16  ? 410 PHE   B CZ   1 
ATOM   3548 N  N    . SER   B 1 408 ? 11.057  -0.448  6.115   1.00 48.00  ? 419 SER   B N    1 
ATOM   3549 C  CA   . SER   B 1 408 ? 11.069  0.024   7.499   1.00 36.06  ? 419 SER   B CA   1 
ATOM   3550 C  C    . SER   B 1 408 ? 12.271  0.917   7.749   1.00 32.26  ? 419 SER   B C    1 
ATOM   3551 O  O    . SER   B 1 408 ? 13.376  0.617   7.300   1.00 38.36  ? 419 SER   B O    1 
ATOM   3552 C  CB   . SER   B 1 408 ? 11.092  -1.148  8.483   1.00 40.54  ? 419 SER   B CB   1 
ATOM   3553 O  OG   . SER   B 1 408 ? 11.255  -0.691  9.820   1.00 46.89  ? 419 SER   B OG   1 
ATOM   3554 N  N    . LYS   B 1 409 ? 12.044  2.029   8.450   1.00 33.83  ? 420 LYS   B N    1 
ATOM   3555 C  CA   . LYS   B 1 409 ? 13.144  2.896   8.859   1.00 45.55  ? 420 LYS   B CA   1 
ATOM   3556 C  C    . LYS   B 1 409 ? 14.165  2.162   9.714   1.00 42.84  ? 420 LYS   B C    1 
ATOM   3557 O  O    . LYS   B 1 409 ? 15.321  2.591   9.789   1.00 39.44  ? 420 LYS   B O    1 
ATOM   3558 C  CB   . LYS   B 1 409 ? 12.626  4.070   9.687   1.00 42.00  ? 420 LYS   B CB   1 
ATOM   3559 C  CG   . LYS   B 1 409 ? 11.677  5.017   9.006   1.00 57.06  ? 420 LYS   B CG   1 
ATOM   3560 C  CD   . LYS   B 1 409 ? 11.123  5.966   10.055  1.00 53.66  ? 420 LYS   B CD   1 
ATOM   3561 C  CE   . LYS   B 1 409 ? 10.273  7.050   9.444   1.00 63.18  ? 420 LYS   B CE   1 
ATOM   3562 N  NZ   . LYS   B 1 409 ? 9.993   8.083   10.465  1.00 54.47  ? 420 LYS   B NZ   1 
ATOM   3563 N  N    . ARG   B 1 410 ? 13.772  1.047   10.332  1.00 37.51  ? 421 ARG   B N    1 
ATOM   3564 C  CA   . ARG   B 1 410 ? 14.660  0.291   11.205  1.00 41.41  ? 421 ARG   B CA   1 
ATOM   3565 C  C    . ARG   B 1 410 ? 15.510  -0.724  10.449  1.00 35.59  ? 421 ARG   B C    1 
ATOM   3566 O  O    . ARG   B 1 410 ? 16.446  -1.279  11.032  1.00 43.05  ? 421 ARG   B O    1 
ATOM   3567 C  CB   . ARG   B 1 410 ? 13.836  -0.470  12.241  1.00 37.78  ? 421 ARG   B CB   1 
ATOM   3568 C  CG   . ARG   B 1 410 ? 12.909  0.393   13.075  1.00 38.67  ? 421 ARG   B CG   1 
ATOM   3569 C  CD   . ARG   B 1 410 ? 12.305  -0.419  14.205  1.00 40.55  ? 421 ARG   B CD   1 
ATOM   3570 N  NE   . ARG   B 1 410 ? 13.340  -0.858  15.130  1.00 42.14  ? 421 ARG   B NE   1 
ATOM   3571 C  CZ   . ARG   B 1 410 ? 13.603  -0.277  16.288  1.00 43.78  ? 421 ARG   B CZ   1 
ATOM   3572 N  NH1  . ARG   B 1 410 ? 12.880  0.743   16.730  1.00 44.14  ? 421 ARG   B NH1  1 
ATOM   3573 N  NH2  . ARG   B 1 410 ? 14.632  -0.711  17.008  1.00 45.24  ? 421 ARG   B NH2  1 
ATOM   3574 N  N    . SER   B 1 411 ? 15.243  -0.942  9.173   1.00 33.93  ? 422 SER   B N    1 
ATOM   3575 C  CA   . SER   B 1 411 ? 15.948  -1.957  8.403   1.00 42.63  ? 422 SER   B CA   1 
ATOM   3576 C  C    . SER   B 1 411 ? 17.134  -1.362  7.659   1.00 36.61  ? 422 SER   B C    1 
ATOM   3577 O  O    . SER   B 1 411 ? 17.155  -0.173  7.327   1.00 46.71  ? 422 SER   B O    1 
ATOM   3578 C  CB   . SER   B 1 411 ? 15.009  -2.616  7.386   1.00 40.49  ? 422 SER   B CB   1 
ATOM   3579 O  OG   . SER   B 1 411 ? 13.947  -3.290  8.038   1.00 61.20  ? 422 SER   B OG   1 
ATOM   3580 N  N    . GLU   B 1 412 ? 18.127  -2.212  7.396   1.00 42.73  ? 423 GLU   B N    1 
ATOM   3581 C  CA   . GLU   B 1 412 ? 19.303  -1.816  6.632   1.00 45.35  ? 423 GLU   B CA   1 
ATOM   3582 C  C    . GLU   B 1 412 ? 18.950  -1.750  5.160   1.00 36.99  ? 423 GLU   B C    1 
ATOM   3583 O  O    . GLU   B 1 412 ? 18.114  -2.515  4.672   1.00 39.34  ? 423 GLU   B O    1 
ATOM   3584 C  CB   . GLU   B 1 412 ? 20.434  -2.837  6.762   1.00 39.07  ? 423 GLU   B CB   1 
ATOM   3585 C  CG   . GLU   B 1 412 ? 20.753  -3.199  8.133   1.00 56.75  ? 423 GLU   B CG   1 
ATOM   3586 C  CD   . GLU   B 1 412 ? 19.864  -4.331  8.599   1.00 36.32  ? 423 GLU   B CD   1 
ATOM   3587 O  OE1  . GLU   B 1 412 ? 19.320  -5.066  7.739   1.00 42.50  ? 423 GLU   B OE1  1 
ATOM   3588 O  OE2  . GLU   B 1 412 ? 19.685  -4.446  9.807   1.00 45.15  ? 423 GLU   B OE2  1 
ATOM   3589 N  N    . MET   B 1 413 ? 19.587  -0.828  4.445   1.00 38.16  ? 424 MET   B N    1 
ATOM   3590 C  CA   . MET   B 1 413 ? 19.502  -0.814  2.991   1.00 39.48  ? 424 MET   B CA   1 
ATOM   3591 C  C    . MET   B 1 413 ? 20.588  -1.714  2.422   1.00 44.26  ? 424 MET   B C    1 
ATOM   3592 O  O    . MET   B 1 413 ? 21.774  -1.520  2.713   1.00 38.20  ? 424 MET   B O    1 
ATOM   3593 C  CB   . MET   B 1 413 ? 19.648  0.584   2.410   1.00 36.88  ? 424 MET   B CB   1 
ATOM   3594 C  CG   . MET   B 1 413 ? 18.514  1.511   2.725   1.00 44.78  ? 424 MET   B CG   1 
ATOM   3595 S  SD   . MET   B 1 413 ? 18.806  2.966   1.713   1.00 65.82  ? 424 MET   B SD   1 
ATOM   3596 C  CE   . MET   B 1 413 ? 18.213  2.310   0.176   1.00 37.88  ? 424 MET   B CE   1 
ATOM   3597 N  N    . VAL   B 1 414 ? 20.194  -2.681  1.603   1.00 45.89  ? 425 VAL   B N    1 
ATOM   3598 C  CA   . VAL   B 1 414 ? 21.139  -3.617  1.011   1.00 39.50  ? 425 VAL   B CA   1 
ATOM   3599 C  C    . VAL   B 1 414 ? 21.422  -3.270  -0.445  1.00 43.05  ? 425 VAL   B C    1 
ATOM   3600 O  O    . VAL   B 1 414 ? 22.578  -3.230  -0.867  1.00 41.87  ? 425 VAL   B O    1 
ATOM   3601 C  CB   . VAL   B 1 414 ? 20.623  -5.066  1.157   1.00 47.52  ? 425 VAL   B CB   1 
ATOM   3602 C  CG1  . VAL   B 1 414 ? 21.556  -6.027  0.429   1.00 53.59  ? 425 VAL   B CG1  1 
ATOM   3603 C  CG2  . VAL   B 1 414 ? 20.463  -5.439  2.637   1.00 48.77  ? 425 VAL   B CG2  1 
ATOM   3604 N  N    . GLY   B 1 415 ? 20.387  -2.986  -1.233  1.00 36.76  ? 426 GLY   B N    1 
ATOM   3605 C  CA   . GLY   B 1 415 ? 20.592  -2.530  -2.590  1.00 32.90  ? 426 GLY   B CA   1 
ATOM   3606 C  C    . GLY   B 1 415 ? 20.450  -1.014  -2.701  1.00 32.69  ? 426 GLY   B C    1 
ATOM   3607 O  O    . GLY   B 1 415 ? 19.998  -0.332  -1.782  1.00 31.20  ? 426 GLY   B O    1 
ATOM   3608 N  N    . THR   B 1 416 ? 20.770  -0.502  -3.883  1.00 31.01  ? 427 THR   B N    1 
ATOM   3609 C  CA   . THR   B 1 416 ? 20.664  0.927   -4.127  1.00 33.81  ? 427 THR   B CA   1 
ATOM   3610 C  C    . THR   B 1 416 ? 19.480  1.254   -5.023  1.00 31.71  ? 427 THR   B C    1 
ATOM   3611 O  O    . THR   B 1 416 ? 19.445  0.810   -6.179  1.00 29.84  ? 427 THR   B O    1 
ATOM   3612 C  CB   . THR   B 1 416 ? 21.957  1.434   -4.772  1.00 31.93  ? 427 THR   B CB   1 
ATOM   3613 O  OG1  . THR   B 1 416 ? 23.069  1.165   -3.904  1.00 39.47  ? 427 THR   B OG1  1 
ATOM   3614 C  CG2  . THR   B 1 416 ? 21.864  2.927   -5.052  1.00 29.97  ? 427 THR   B CG2  1 
ATOM   3615 N  N    . PRO   B 1 417 ? 18.507  2.021   -4.543  1.00 33.87  ? 428 PRO   B N    1 
ATOM   3616 C  CA   . PRO   B 1 417 ? 17.344  2.443   -5.347  1.00 30.46  ? 428 PRO   B CA   1 
ATOM   3617 C  C    . PRO   B 1 417 ? 17.706  3.574   -6.308  1.00 26.93  ? 428 PRO   B C    1 
ATOM   3618 O  O    . PRO   B 1 417 ? 17.186  4.695   -6.222  1.00 27.06  ? 428 PRO   B O    1 
ATOM   3619 C  CB   . PRO   B 1 417 ? 16.345  2.874   -4.269  1.00 34.95  ? 428 PRO   B CB   1 
ATOM   3620 C  CG   . PRO   B 1 417 ? 17.215  3.430   -3.215  1.00 34.87  ? 428 PRO   B CG   1 
ATOM   3621 C  CD   . PRO   B 1 417 ? 18.434  2.542   -3.171  1.00 39.52  ? 428 PRO   B CD   1 
ATOM   3622 N  N    . TYR   B 1 418 ? 18.609  3.268   -7.246  1.00 23.26  ? 429 TYR   B N    1 
ATOM   3623 C  CA   . TYR   B 1 418 ? 19.246  4.290   -8.070  1.00 27.57  ? 429 TYR   B CA   1 
ATOM   3624 C  C    . TYR   B 1 418 ? 18.264  5.027   -8.962  1.00 23.34  ? 429 TYR   B C    1 
ATOM   3625 O  O    . TYR   B 1 418 ? 18.594  6.107   -9.459  1.00 25.32  ? 429 TYR   B O    1 
ATOM   3626 C  CB   . TYR   B 1 418 ? 20.347  3.658   -8.927  1.00 23.74  ? 429 TYR   B CB   1 
ATOM   3627 C  CG   . TYR   B 1 418 ? 19.842  2.664   -9.937  1.00 22.76  ? 429 TYR   B CG   1 
ATOM   3628 C  CD1  . TYR   B 1 418 ? 19.412  3.083   -11.185 1.00 28.31  ? 429 TYR   B CD1  1 
ATOM   3629 C  CD2  . TYR   B 1 418 ? 19.820  1.297   -9.656  1.00 30.97  ? 429 TYR   B CD2  1 
ATOM   3630 C  CE1  . TYR   B 1 418 ? 18.959  2.179   -12.130 1.00 37.12  ? 429 TYR   B CE1  1 
ATOM   3631 C  CE2  . TYR   B 1 418 ? 19.362  0.378   -10.599 1.00 36.89  ? 429 TYR   B CE2  1 
ATOM   3632 C  CZ   . TYR   B 1 418 ? 18.935  0.832   -11.835 1.00 34.36  ? 429 TYR   B CZ   1 
ATOM   3633 O  OH   . TYR   B 1 418 ? 18.486  -0.048  -12.797 1.00 41.73  ? 429 TYR   B OH   1 
ATOM   3634 N  N    . TRP   B 1 419 ? 17.078  4.472   -9.188  1.00 21.67  ? 430 TRP   B N    1 
ATOM   3635 C  CA   . TRP   B 1 419 ? 16.108  5.065   -10.096 1.00 22.79  ? 430 TRP   B CA   1 
ATOM   3636 C  C    . TRP   B 1 419 ? 15.165  6.040   -9.404  1.00 23.74  ? 430 TRP   B C    1 
ATOM   3637 O  O    . TRP   B 1 419 ? 14.353  6.682   -10.080 1.00 24.26  ? 430 TRP   B O    1 
ATOM   3638 C  CB   . TRP   B 1 419 ? 15.282  3.957   -10.774 1.00 24.47  ? 430 TRP   B CB   1 
ATOM   3639 C  CG   . TRP   B 1 419 ? 14.462  3.172   -9.780  1.00 27.37  ? 430 TRP   B CG   1 
ATOM   3640 C  CD1  . TRP   B 1 419 ? 13.171  3.414   -9.413  1.00 29.13  ? 430 TRP   B CD1  1 
ATOM   3641 C  CD2  . TRP   B 1 419 ? 14.900  2.055   -9.001  1.00 27.10  ? 430 TRP   B CD2  1 
ATOM   3642 N  NE1  . TRP   B 1 419 ? 12.770  2.501   -8.467  1.00 27.47  ? 430 TRP   B NE1  1 
ATOM   3643 C  CE2  . TRP   B 1 419 ? 13.817  1.656   -8.195  1.00 34.76  ? 430 TRP   B CE2  1 
ATOM   3644 C  CE3  . TRP   B 1 419 ? 16.104  1.342   -8.918  1.00 29.21  ? 430 TRP   B CE3  1 
ATOM   3645 C  CZ2  . TRP   B 1 419 ? 13.901  0.577   -7.305  1.00 29.69  ? 430 TRP   B CZ2  1 
ATOM   3646 C  CZ3  . TRP   B 1 419 ? 16.189  0.271   -8.034  1.00 31.86  ? 430 TRP   B CZ3  1 
ATOM   3647 C  CH2  . TRP   B 1 419 ? 15.094  -0.101  -7.241  1.00 29.82  ? 430 TRP   B CH2  1 
ATOM   3648 N  N    . MET   B 1 420 ? 15.248  6.182   -8.087  1.00 25.23  ? 431 MET   B N    1 
ATOM   3649 C  CA   . MET   B 1 420 ? 14.249  6.973   -7.372  1.00 25.95  ? 431 MET   B CA   1 
ATOM   3650 C  C    . MET   B 1 420 ? 14.533  8.469   -7.414  1.00 29.88  ? 431 MET   B C    1 
ATOM   3651 O  O    . MET   B 1 420 ? 15.677  8.914   -7.260  1.00 27.48  ? 431 MET   B O    1 
ATOM   3652 C  CB   . MET   B 1 420 ? 14.117  6.509   -5.922  1.00 27.36  ? 431 MET   B CB   1 
ATOM   3653 C  CG   . MET   B 1 420 ? 13.532  5.130   -5.825  1.00 30.37  ? 431 MET   B CG   1 
ATOM   3654 S  SD   . MET   B 1 420 ? 13.325  4.596   -4.106  1.00 35.47  ? 431 MET   B SD   1 
ATOM   3655 C  CE   . MET   B 1 420 ? 12.699  2.942   -4.365  1.00 38.69  ? 431 MET   B CE   1 
ATOM   3656 N  N    . ALA   B 1 421 ? 13.461  9.236   -7.615  1.00 27.54  ? 432 ALA   B N    1 
ATOM   3657 C  CA   . ALA   B 1 421 ? 13.528  10.690  -7.659  1.00 31.43  ? 432 ALA   B CA   1 
ATOM   3658 C  C    . ALA   B 1 421 ? 13.874  11.269  -6.284  1.00 29.13  ? 432 ALA   B C    1 
ATOM   3659 O  O    . ALA   B 1 421 ? 13.601  10.646  -5.252  1.00 28.34  ? 432 ALA   B O    1 
ATOM   3660 C  CB   . ALA   B 1 421 ? 12.191  11.261  -8.130  1.00 28.69  ? 432 ALA   B CB   1 
ATOM   3661 N  N    . PRO   B 1 422 ? 14.469  12.466  -6.244  1.00 28.12  ? 433 PRO   B N    1 
ATOM   3662 C  CA   . PRO   B 1 422 ? 14.852  13.029  -4.940  1.00 35.73  ? 433 PRO   B CA   1 
ATOM   3663 C  C    . PRO   B 1 422 ? 13.672  13.180  -4.003  1.00 38.34  ? 433 PRO   B C    1 
ATOM   3664 O  O    . PRO   B 1 422 ? 13.803  12.901  -2.807  1.00 34.65  ? 433 PRO   B O    1 
ATOM   3665 C  CB   . PRO   B 1 422 ? 15.469  14.387  -5.306  1.00 32.61  ? 433 PRO   B CB   1 
ATOM   3666 C  CG   . PRO   B 1 422 ? 15.840  14.274  -6.769  1.00 31.96  ? 433 PRO   B CG   1 
ATOM   3667 C  CD   . PRO   B 1 422 ? 14.784  13.387  -7.353  1.00 30.03  ? 433 PRO   B CD   1 
ATOM   3668 N  N    . GLU   B 1 423 ? 12.506  13.571  -4.521  1.00 30.61  ? 434 GLU   B N    1 
ATOM   3669 C  CA   . GLU   B 1 423 ? 11.352  13.739  -3.645  1.00 45.24  ? 434 GLU   B CA   1 
ATOM   3670 C  C    . GLU   B 1 423 ? 10.892  12.407  -3.064  1.00 36.76  ? 434 GLU   B C    1 
ATOM   3671 O  O    . GLU   B 1 423 ? 10.265  12.394  -2.002  1.00 40.05  ? 434 GLU   B O    1 
ATOM   3672 C  CB   . GLU   B 1 423 ? 10.209  14.440  -4.388  1.00 34.83  ? 434 GLU   B CB   1 
ATOM   3673 C  CG   . GLU   B 1 423 ? 9.640   13.650  -5.556  1.00 39.96  ? 434 GLU   B CG   1 
ATOM   3674 C  CD   . GLU   B 1 423 ? 10.230  14.058  -6.897  1.00 33.23  ? 434 GLU   B CD   1 
ATOM   3675 O  OE1  . GLU   B 1 423 ? 11.382  14.554  -6.942  1.00 28.77  ? 434 GLU   B OE1  1 
ATOM   3676 O  OE2  . GLU   B 1 423 ? 9.520   13.886  -7.908  1.00 33.99  ? 434 GLU   B OE2  1 
ATOM   3677 N  N    . VAL   B 1 424 ? 11.203  11.290  -3.731  1.00 33.82  ? 435 VAL   B N    1 
ATOM   3678 C  CA   . VAL   B 1 424 ? 10.905  9.974   -3.172  1.00 30.80  ? 435 VAL   B CA   1 
ATOM   3679 C  C    . VAL   B 1 424 ? 11.843  9.649   -2.019  1.00 43.92  ? 435 VAL   B C    1 
ATOM   3680 O  O    . VAL   B 1 424 ? 11.403  9.232   -0.941  1.00 42.31  ? 435 VAL   B O    1 
ATOM   3681 C  CB   . VAL   B 1 424 ? 11.006  8.894   -4.267  1.00 35.06  ? 435 VAL   B CB   1 
ATOM   3682 C  CG1  . VAL   B 1 424 ? 10.779  7.533   -3.674  1.00 33.68  ? 435 VAL   B CG1  1 
ATOM   3683 C  CG2  . VAL   B 1 424 ? 10.012  9.158   -5.363  1.00 27.98  ? 435 VAL   B CG2  1 
ATOM   3684 N  N    . VAL   B 1 425 ? 13.153  9.801   -2.242  1.00 37.73  ? 436 VAL   B N    1 
ATOM   3685 C  CA   . VAL   B 1 425 ? 14.139  9.401   -1.239  1.00 43.72  ? 436 VAL   B CA   1 
ATOM   3686 C  C    . VAL   B 1 425 ? 14.014  10.253  0.015   1.00 42.05  ? 436 VAL   B C    1 
ATOM   3687 O  O    . VAL   B 1 425 ? 14.369  9.809   1.113   1.00 45.45  ? 436 VAL   B O    1 
ATOM   3688 C  CB   . VAL   B 1 425 ? 15.564  9.417   -1.829  1.00 40.33  ? 436 VAL   B CB   1 
ATOM   3689 C  CG1  . VAL   B 1 425 ? 15.626  8.501   -3.055  1.00 41.67  ? 436 VAL   B CG1  1 
ATOM   3690 C  CG2  . VAL   B 1 425 ? 16.010  10.820  -2.166  1.00 38.55  ? 436 VAL   B CG2  1 
ATOM   3691 N  N    . THR   B 1 426 ? 13.533  11.482  -0.121  1.00 45.11  ? 437 THR   B N    1 
ATOM   3692 C  CA   . THR   B 1 426 ? 13.308  12.347  1.022   1.00 40.39  ? 437 THR   B CA   1 
ATOM   3693 C  C    . THR   B 1 426 ? 11.916  12.130  1.619   1.00 56.95  ? 437 THR   B C    1 
ATOM   3694 O  O    . THR   B 1 426 ? 11.443  12.969  2.393   1.00 57.06  ? 437 THR   B O    1 
ATOM   3695 C  CB   . THR   B 1 426 ? 13.505  13.808  0.612   1.00 46.76  ? 437 THR   B CB   1 
ATOM   3696 O  OG1  . THR   B 1 426 ? 12.625  14.118  -0.472  1.00 56.94  ? 437 THR   B OG1  1 
ATOM   3697 C  CG2  . THR   B 1 426 ? 14.939  14.053  0.147   1.00 46.31  ? 437 THR   B CG2  1 
ATOM   3698 N  N    . ARG   B 1 427 ? 11.254  11.029  1.232   1.00 72.81  ? 438 ARG   B N    1 
ATOM   3699 C  CA   . ARG   B 1 427 ? 9.974   10.562  1.785   1.00 74.65  ? 438 ARG   B CA   1 
ATOM   3700 C  C    . ARG   B 1 427 ? 8.915   11.656  1.758   1.00 75.74  ? 438 ARG   B C    1 
ATOM   3701 O  O    . ARG   B 1 427 ? 8.083   11.773  2.661   1.00 79.22  ? 438 ARG   B O    1 
ATOM   3702 C  CB   . ARG   B 1 427 ? 10.093  9.996   3.199   1.00 78.31  ? 438 ARG   B CB   1 
ATOM   3703 C  CG   . ARG   B 1 427 ? 10.844  8.688   3.343   1.00 82.65  ? 438 ARG   B CG   1 
ATOM   3704 C  CD   . ARG   B 1 427 ? 10.712  8.228   4.788   1.00 90.21  ? 438 ARG   B CD   1 
ATOM   3705 N  NE   . ARG   B 1 427 ? 10.903  9.349   5.699   1.00 94.17  ? 438 ARG   B NE   1 
ATOM   3706 C  CZ   . ARG   B 1 427 ? 10.021  9.770   6.598   1.00 94.03  ? 438 ARG   B CZ   1 
ATOM   3707 N  NH1  . ARG   B 1 427 ? 8.906   9.101   6.841   1.00 97.31  ? 438 ARG   B NH1  1 
ATOM   3708 N  NH2  . ARG   B 1 427 ? 10.272  10.887  7.280   1.00 84.54  ? 438 ARG   B NH2  1 
ATOM   3709 N  N    . LYS   B 1 428 ? 8.926   12.448  0.705   1.00 58.01  ? 439 LYS   B N    1 
ATOM   3710 C  CA   . LYS   B 1 428 ? 7.874   13.425  0.525   1.00 58.05  ? 439 LYS   B CA   1 
ATOM   3711 C  C    . LYS   B 1 428 ? 6.697   12.777  -0.192  1.00 65.17  ? 439 LYS   B C    1 
ATOM   3712 O  O    . LYS   B 1 428 ? 6.819   11.709  -0.799  1.00 62.29  ? 439 LYS   B O    1 
ATOM   3713 C  CB   . LYS   B 1 428 ? 8.378   14.606  -0.301  1.00 52.28  ? 439 LYS   B CB   1 
ATOM   3714 C  CG   . LYS   B 1 428 ? 9.688   15.194  0.172   1.00 64.28  ? 439 LYS   B CG   1 
ATOM   3715 C  CD   . LYS   B 1 428 ? 10.086  16.401  -0.667  1.00 55.94  ? 439 LYS   B CD   1 
ATOM   3716 C  CE   . LYS   B 1 428 ? 11.431  16.963  -0.226  1.00 61.10  ? 439 LYS   B CE   1 
ATOM   3717 N  NZ   . LYS   B 1 428 ? 11.930  18.016  -1.154  1.00 67.28  ? 439 LYS   B NZ   1 
ATOM   3718 N  N    . ALA   B 1 429 ? 5.540   13.423  -0.099  1.00 53.66  ? 440 ALA   B N    1 
ATOM   3719 C  CA   . ALA   B 1 429 ? 4.451   13.057  -0.987  1.00 48.08  ? 440 ALA   B CA   1 
ATOM   3720 C  C    . ALA   B 1 429 ? 4.895   13.329  -2.420  1.00 37.10  ? 440 ALA   B C    1 
ATOM   3721 O  O    . ALA   B 1 429 ? 5.529   14.347  -2.709  1.00 43.44  ? 440 ALA   B O    1 
ATOM   3722 C  CB   . ALA   B 1 429 ? 3.183   13.841  -0.649  1.00 53.26  ? 440 ALA   B CB   1 
ATOM   3723 N  N    . TYR   B 1 430 ? 4.604   12.402  -3.318  1.00 36.87  ? 441 TYR   B N    1 
ATOM   3724 C  CA   . TYR   B 1 430 ? 5.104   12.529  -4.681  1.00 37.59  ? 441 TYR   B CA   1 
ATOM   3725 C  C    . TYR   B 1 430 ? 4.014   12.120  -5.654  1.00 41.75  ? 441 TYR   B C    1 
ATOM   3726 O  O    . TYR   B 1 430 ? 2.990   11.551  -5.266  1.00 38.57  ? 441 TYR   B O    1 
ATOM   3727 C  CB   . TYR   B 1 430 ? 6.376   11.711  -4.869  1.00 36.93  ? 441 TYR   B CB   1 
ATOM   3728 C  CG   . TYR   B 1 430 ? 6.196   10.243  -4.604  1.00 38.24  ? 441 TYR   B CG   1 
ATOM   3729 C  CD1  . TYR   B 1 430 ? 5.683   9.398   -5.578  1.00 36.74  ? 441 TYR   B CD1  1 
ATOM   3730 C  CD2  . TYR   B 1 430 ? 6.555   9.697   -3.381  1.00 40.93  ? 441 TYR   B CD2  1 
ATOM   3731 C  CE1  . TYR   B 1 430 ? 5.528   8.048   -5.337  1.00 45.55  ? 441 TYR   B CE1  1 
ATOM   3732 C  CE2  . TYR   B 1 430 ? 6.401   8.354   -3.130  1.00 43.55  ? 441 TYR   B CE2  1 
ATOM   3733 C  CZ   . TYR   B 1 430 ? 5.890   7.534   -4.113  1.00 48.26  ? 441 TYR   B CZ   1 
ATOM   3734 O  OH   . TYR   B 1 430 ? 5.738   6.193   -3.872  1.00 56.01  ? 441 TYR   B OH   1 
ATOM   3735 N  N    . GLY   B 1 431 ? 4.225   12.445  -6.930  1.00 38.13  ? 442 GLY   B N    1 
ATOM   3736 C  CA   . GLY   B 1 431 ? 3.241   12.152  -7.945  1.00 34.85  ? 442 GLY   B CA   1 
ATOM   3737 C  C    . GLY   B 1 431 ? 3.831   11.495  -9.178  1.00 33.02  ? 442 GLY   B C    1 
ATOM   3738 O  O    . GLY   B 1 431 ? 4.937   10.952  -9.153  1.00 31.74  ? 442 GLY   B O    1 
ATOM   3739 N  N    . PRO   B 1 432 ? 3.099   11.564  -10.291 1.00 34.25  ? 443 PRO   B N    1 
ATOM   3740 C  CA   . PRO   B 1 432 ? 3.517   10.844  -11.511 1.00 30.41  ? 443 PRO   B CA   1 
ATOM   3741 C  C    . PRO   B 1 432 ? 4.894   11.227  -12.026 1.00 31.38  ? 443 PRO   B C    1 
ATOM   3742 O  O    . PRO   B 1 432 ? 5.519   10.422  -12.732 1.00 28.97  ? 443 PRO   B O    1 
ATOM   3743 C  CB   . PRO   B 1 432 ? 2.435   11.229  -12.532 1.00 30.94  ? 443 PRO   B CB   1 
ATOM   3744 C  CG   . PRO   B 1 432 ? 1.268   11.725  -11.711 1.00 37.97  ? 443 PRO   B CG   1 
ATOM   3745 C  CD   . PRO   B 1 432 ? 1.850   12.324  -10.475 1.00 39.62  ? 443 PRO   B CD   1 
ATOM   3746 N  N    . LYS   B 1 433 ? 5.389   12.432  -11.727 1.00 30.69  ? 444 LYS   B N    1 
ATOM   3747 C  CA   . LYS   B 1 433 ? 6.654   12.830  -12.342 1.00 34.05  ? 444 LYS   B CA   1 
ATOM   3748 C  C    . LYS   B 1 433 ? 7.864   12.101  -11.773 1.00 28.73  ? 444 LYS   B C    1 
ATOM   3749 O  O    . LYS   B 1 433 ? 8.960   12.238  -12.330 1.00 28.29  ? 444 LYS   B O    1 
ATOM   3750 C  CB   . LYS   B 1 433 ? 6.844   14.336  -12.224 1.00 34.55  ? 444 LYS   B CB   1 
ATOM   3751 C  CG   . LYS   B 1 433 ? 6.016   15.115  -13.232 1.00 32.13  ? 444 LYS   B CG   1 
ATOM   3752 C  CD   . LYS   B 1 433 ? 6.139   16.590  -13.007 1.00 42.62  ? 444 LYS   B CD   1 
ATOM   3753 C  CE   . LYS   B 1 433 ? 5.395   17.370  -14.070 1.00 40.39  ? 444 LYS   B CE   1 
ATOM   3754 N  NZ   . LYS   B 1 433 ? 5.584   18.824  -13.846 1.00 37.46  ? 444 LYS   B NZ   1 
ATOM   3755 N  N    . VAL   B 1 434 ? 7.703   11.320  -10.704 1.00 27.86  ? 445 VAL   B N    1 
ATOM   3756 C  CA   . VAL   B 1 434 ? 8.808   10.472  -10.269 1.00 23.20  ? 445 VAL   B CA   1 
ATOM   3757 C  C    . VAL   B 1 434 ? 9.153   9.464   -11.358 1.00 24.16  ? 445 VAL   B C    1 
ATOM   3758 O  O    . VAL   B 1 434 ? 10.306  9.038   -11.466 1.00 25.07  ? 445 VAL   B O    1 
ATOM   3759 C  CB   . VAL   B 1 434 ? 8.479   9.760   -8.939  1.00 30.37  ? 445 VAL   B CB   1 
ATOM   3760 C  CG1  . VAL   B 1 434 ? 8.054   10.768  -7.884  1.00 28.46  ? 445 VAL   B CG1  1 
ATOM   3761 C  CG2  . VAL   B 1 434 ? 7.396   8.680   -9.112  1.00 29.78  ? 445 VAL   B CG2  1 
ATOM   3762 N  N    . ASP   B 1 435 ? 8.165   9.065   -12.172 1.00 24.23  ? 446 ASP   B N    1 
ATOM   3763 C  CA   . ASP   B 1 435 ? 8.415   8.125   -13.266 1.00 22.40  ? 446 ASP   B CA   1 
ATOM   3764 C  C    . ASP   B 1 435 ? 9.226   8.770   -14.381 1.00 25.32  ? 446 ASP   B C    1 
ATOM   3765 O  O    . ASP   B 1 435 ? 9.967   8.074   -15.091 1.00 24.11  ? 446 ASP   B O    1 
ATOM   3766 C  CB   . ASP   B 1 435 ? 7.095   7.613   -13.850 1.00 27.54  ? 446 ASP   B CB   1 
ATOM   3767 C  CG   . ASP   B 1 435 ? 6.338   6.679   -12.907 1.00 26.33  ? 446 ASP   B CG   1 
ATOM   3768 O  OD1  . ASP   B 1 435 ? 6.979   6.029   -12.054 1.00 24.54  ? 446 ASP   B OD1  1 
ATOM   3769 O  OD2  . ASP   B 1 435 ? 5.098   6.579   -13.054 1.00 25.43  ? 446 ASP   B OD2  1 
ATOM   3770 N  N    . ILE   B 1 436 ? 9.038   10.075  -14.591 1.00 25.33  ? 447 ILE   B N    1 
ATOM   3771 C  CA   . ILE   B 1 436 ? 9.820   10.806  -15.584 1.00 21.10  ? 447 ILE   B CA   1 
ATOM   3772 C  C    . ILE   B 1 436 ? 11.269  10.898  -15.141 1.00 25.11  ? 447 ILE   B C    1 
ATOM   3773 O  O    . ILE   B 1 436 ? 12.192  10.753  -15.954 1.00 23.31  ? 447 ILE   B O    1 
ATOM   3774 C  CB   . ILE   B 1 436 ? 9.220   12.206  -15.835 1.00 22.17  ? 447 ILE   B CB   1 
ATOM   3775 C  CG1  . ILE   B 1 436 ? 7.846   12.116  -16.513 1.00 26.00  ? 447 ILE   B CG1  1 
ATOM   3776 C  CG2  . ILE   B 1 436 ? 10.207  13.086  -16.614 1.00 25.87  ? 447 ILE   B CG2  1 
ATOM   3777 C  CD1  . ILE   B 1 436 ? 7.869   11.515  -17.886 1.00 32.39  ? 447 ILE   B CD1  1 
ATOM   3778 N  N    . TRP   B 1 437 ? 11.491  11.157  -13.852 1.00 25.33  ? 448 TRP   B N    1 
ATOM   3779 C  CA   . TRP   B 1 437 ? 12.842  11.108  -13.306 1.00 24.58  ? 448 TRP   B CA   1 
ATOM   3780 C  C    . TRP   B 1 437 ? 13.478  9.749   -13.560 1.00 22.35  ? 448 TRP   B C    1 
ATOM   3781 O  O    . TRP   B 1 437 ? 14.600  9.660   -14.077 1.00 20.83  ? 448 TRP   B O    1 
ATOM   3782 C  CB   . TRP   B 1 437 ? 12.822  11.409  -11.803 1.00 23.22  ? 448 TRP   B CB   1 
ATOM   3783 C  CG   . TRP   B 1 437 ? 14.194  11.322  -11.182 1.00 23.96  ? 448 TRP   B CG   1 
ATOM   3784 C  CD1  . TRP   B 1 437 ? 14.866  10.184  -10.814 1.00 27.51  ? 448 TRP   B CD1  1 
ATOM   3785 C  CD2  . TRP   B 1 437 ? 15.069  12.409  -10.903 1.00 24.96  ? 448 TRP   B CD2  1 
ATOM   3786 N  NE1  . TRP   B 1 437 ? 16.096  10.507  -10.307 1.00 22.65  ? 448 TRP   B NE1  1 
ATOM   3787 C  CE2  . TRP   B 1 437 ? 16.248  11.867  -10.354 1.00 22.94  ? 448 TRP   B CE2  1 
ATOM   3788 C  CE3  . TRP   B 1 437 ? 14.968  13.795  -11.050 1.00 25.69  ? 448 TRP   B CE3  1 
ATOM   3789 C  CZ2  . TRP   B 1 437 ? 17.310  12.661  -9.948  1.00 29.26  ? 448 TRP   B CZ2  1 
ATOM   3790 C  CZ3  . TRP   B 1 437 ? 16.026  14.582  -10.650 1.00 32.47  ? 448 TRP   B CZ3  1 
ATOM   3791 C  CH2  . TRP   B 1 437 ? 17.183  14.015  -10.109 1.00 32.38  ? 448 TRP   B CH2  1 
ATOM   3792 N  N    . SER   B 1 438 ? 12.774  8.673   -13.196 1.00 20.74  ? 449 SER   B N    1 
ATOM   3793 C  CA   . SER   B 1 438 ? 13.335  7.335   -13.371 1.00 20.29  ? 449 SER   B CA   1 
ATOM   3794 C  C    . SER   B 1 438 ? 13.644  7.059   -14.838 1.00 23.04  ? 449 SER   B C    1 
ATOM   3795 O  O    . SER   B 1 438 ? 14.631  6.386   -15.153 1.00 20.68  ? 449 SER   B O    1 
ATOM   3796 C  CB   . SER   B 1 438 ? 12.365  6.283   -12.820 1.00 20.55  ? 449 SER   B CB   1 
ATOM   3797 O  OG   . SER   B 1 438 ? 12.094  6.502   -11.434 1.00 23.32  ? 449 SER   B OG   1 
ATOM   3798 N  N    . LEU   B 1 439 ? 12.806  7.563   -15.749 1.00 20.92  ? 450 LEU   B N    1 
ATOM   3799 C  CA   . LEU   B 1 439 ? 13.086  7.405   -17.178 1.00 21.95  ? 450 LEU   B CA   1 
ATOM   3800 C  C    . LEU   B 1 439 ? 14.391  8.094   -17.566 1.00 22.28  ? 450 LEU   B C    1 
ATOM   3801 O  O    . LEU   B 1 439 ? 15.178  7.563   -18.367 1.00 20.39  ? 450 LEU   B O    1 
ATOM   3802 C  CB   . LEU   B 1 439 ? 11.923  7.963   -18.006 1.00 20.72  ? 450 LEU   B CB   1 
ATOM   3803 C  CG   . LEU   B 1 439 ? 12.239  7.954   -19.511 1.00 31.68  ? 450 LEU   B CG   1 
ATOM   3804 C  CD1  . LEU   B 1 439 ? 12.309  6.512   -20.030 1.00 28.13  ? 450 LEU   B CD1  1 
ATOM   3805 C  CD2  . LEU   B 1 439 ? 11.234  8.765   -20.292 1.00 37.57  ? 450 LEU   B CD2  1 
ATOM   3806 N  N    . GLY   B 1 440 ? 14.627  9.292   -17.023 1.00 21.52  ? 451 GLY   B N    1 
ATOM   3807 C  CA   . GLY   B 1 440 ? 15.893  9.972   -17.262 1.00 23.19  ? 451 GLY   B CA   1 
ATOM   3808 C  C    . GLY   B 1 440 ? 17.085  9.159   -16.791 1.00 26.08  ? 451 GLY   B C    1 
ATOM   3809 O  O    . GLY   B 1 440 ? 18.096  9.058   -17.490 1.00 19.44  ? 451 GLY   B O    1 
ATOM   3810 N  N    . ILE   B 1 441 ? 16.969  8.551   -15.605 1.00 17.95  ? 452 ILE   B N    1 
ATOM   3811 C  CA   . ILE   B 1 441 ? 18.021  7.675   -15.090 1.00 19.24  ? 452 ILE   B CA   1 
ATOM   3812 C  C    . ILE   B 1 441 ? 18.243  6.497   -16.027 1.00 18.28  ? 452 ILE   B C    1 
ATOM   3813 O  O    . ILE   B 1 441 ? 19.380  6.068   -16.252 1.00 17.65  ? 452 ILE   B O    1 
ATOM   3814 C  CB   . ILE   B 1 441 ? 17.650  7.183   -13.673 1.00 19.39  ? 452 ILE   B CB   1 
ATOM   3815 C  CG1  . ILE   B 1 441 ? 17.505  8.371   -12.714 1.00 21.34  ? 452 ILE   B CG1  1 
ATOM   3816 C  CG2  . ILE   B 1 441 ? 18.681  6.163   -13.165 1.00 21.11  ? 452 ILE   B CG2  1 
ATOM   3817 C  CD1  . ILE   B 1 441 ? 18.813  9.090   -12.463 1.00 26.85  ? 452 ILE   B CD1  1 
ATOM   3818 N  N    . MET   B 1 442 ? 17.158  5.933   -16.567 1.00 19.26  ? 453 MET   B N    1 
ATOM   3819 C  CA   . MET   B 1 442 ? 17.292  4.789   -17.468 1.00 16.36  ? 453 MET   B CA   1 
ATOM   3820 C  C    . MET   B 1 442 ? 17.956  5.187   -18.790 1.00 17.97  ? 453 MET   B C    1 
ATOM   3821 O  O    . MET   B 1 442 ? 18.701  4.398   -19.385 1.00 19.82  ? 453 MET   B O    1 
ATOM   3822 C  CB   . MET   B 1 442 ? 15.908  4.181   -17.745 1.00 22.10  ? 453 MET   B CB   1 
ATOM   3823 C  CG   . MET   B 1 442 ? 15.958  2.776   -18.386 1.00 20.07  ? 453 MET   B CG   1 
ATOM   3824 S  SD   . MET   B 1 442 ? 14.357  1.964   -18.344 1.00 23.70  ? 453 MET   B SD   1 
ATOM   3825 C  CE   . MET   B 1 442 ? 13.440  2.981   -19.502 1.00 25.51  ? 453 MET   B CE   1 
ATOM   3826 N  N    . ALA   B 1 443 ? 17.672  6.394   -19.279 1.00 19.11  ? 454 ALA   B N    1 
ATOM   3827 C  CA   . ALA   B 1 443 ? 18.344  6.867   -20.486 1.00 22.07  ? 454 ALA   B CA   1 
ATOM   3828 C  C    . ALA   B 1 443 ? 19.838  7.061   -20.250 1.00 25.19  ? 454 ALA   B C    1 
ATOM   3829 O  O    . ALA   B 1 443 ? 20.653  6.768   -21.129 1.00 20.58  ? 454 ALA   B O    1 
ATOM   3830 C  CB   . ALA   B 1 443 ? 17.697  8.160   -20.967 1.00 20.54  ? 454 ALA   B CB   1 
ATOM   3831 N  N    . ILE   B 1 444 ? 20.221  7.554   -19.075 1.00 18.84  ? 455 ILE   B N    1 
ATOM   3832 C  CA   . ILE   B 1 444 ? 21.634  7.581   -18.720 1.00 16.27  ? 455 ILE   B CA   1 
ATOM   3833 C  C    . ILE   B 1 444 ? 22.191  6.159   -18.648 1.00 21.75  ? 455 ILE   B C    1 
ATOM   3834 O  O    . ILE   B 1 444 ? 23.284  5.875   -19.158 1.00 21.66  ? 455 ILE   B O    1 
ATOM   3835 C  CB   . ILE   B 1 444 ? 21.832  8.322   -17.385 1.00 21.80  ? 455 ILE   B CB   1 
ATOM   3836 C  CG1  . ILE   B 1 444 ? 21.547  9.828   -17.527 1.00 24.32  ? 455 ILE   B CG1  1 
ATOM   3837 C  CG2  . ILE   B 1 444 ? 23.259  8.074   -16.856 1.00 23.69  ? 455 ILE   B CG2  1 
ATOM   3838 C  CD1  . ILE   B 1 444 ? 21.712  10.576  -16.191 1.00 27.78  ? 455 ILE   B CD1  1 
ATOM   3839 N  N    . GLU   B 1 445 ? 21.443  5.236   -18.032 1.00 20.06  ? 456 GLU   B N    1 
ATOM   3840 C  CA   . GLU   B 1 445 ? 21.877  3.839   -18.028 1.00 19.79  ? 456 GLU   B CA   1 
ATOM   3841 C  C    . GLU   B 1 445 ? 22.104  3.328   -19.451 1.00 21.01  ? 456 GLU   B C    1 
ATOM   3842 O  O    . GLU   B 1 445 ? 23.092  2.634   -19.720 1.00 21.59  ? 456 GLU   B O    1 
ATOM   3843 C  CB   . GLU   B 1 445 ? 20.850  2.960   -17.302 1.00 20.43  ? 456 GLU   B CB   1 
ATOM   3844 C  CG   . GLU   B 1 445 ? 21.251  1.480   -17.249 1.00 23.97  ? 456 GLU   B CG   1 
ATOM   3845 C  CD   . GLU   B 1 445 ? 20.258  0.625   -16.476 1.00 36.65  ? 456 GLU   B CD   1 
ATOM   3846 O  OE1  . GLU   B 1 445 ? 19.508  1.182   -15.648 1.00 38.33  ? 456 GLU   B OE1  1 
ATOM   3847 O  OE2  . GLU   B 1 445 ? 20.234  -0.608  -16.686 1.00 32.09  ? 456 GLU   B OE2  1 
ATOM   3848 N  N    . MET   B 1 446 ? 21.207  3.666   -20.379 1.00 21.46  ? 457 MET   B N    1 
ATOM   3849 C  CA   . MET   B 1 446 ? 21.340  3.124   -21.736 1.00 21.22  ? 457 MET   B CA   1 
ATOM   3850 C  C    . MET   B 1 446 ? 22.593  3.639   -22.437 1.00 21.48  ? 457 MET   B C    1 
ATOM   3851 O  O    . MET   B 1 446 ? 23.295  2.863   -23.104 1.00 22.29  ? 457 MET   B O    1 
ATOM   3852 C  CB   . MET   B 1 446 ? 20.109  3.464   -22.577 1.00 17.92  ? 457 MET   B CB   1 
ATOM   3853 C  CG   . MET   B 1 446 ? 18.857  2.638   -22.227 1.00 20.65  ? 457 MET   B CG   1 
ATOM   3854 S  SD   . MET   B 1 446 ? 17.548  2.983   -23.412 1.00 21.37  ? 457 MET   B SD   1 
ATOM   3855 C  CE   . MET   B 1 446 ? 16.536  4.139   -22.463 1.00 18.02  ? 457 MET   B CE   1 
ATOM   3856 N  N    . ILE   B 1 447 ? 22.914  4.924   -22.265 1.00 19.16  ? 458 ILE   B N    1 
ATOM   3857 C  CA   . ILE   B 1 447 ? 24.081  5.494   -22.956 1.00 20.89  ? 458 ILE   B CA   1 
ATOM   3858 C  C    . ILE   B 1 447 ? 25.378  5.113   -22.241 1.00 23.67  ? 458 ILE   B C    1 
ATOM   3859 O  O    . ILE   B 1 447 ? 26.418  4.977   -22.879 1.00 22.15  ? 458 ILE   B O    1 
ATOM   3860 C  CB   . ILE   B 1 447 ? 23.944  7.018   -23.168 1.00 24.71  ? 458 ILE   B CB   1 
ATOM   3861 C  CG1  . ILE   B 1 447 ? 24.957  7.496   -24.224 1.00 26.01  ? 458 ILE   B CG1  1 
ATOM   3862 C  CG2  . ILE   B 1 447 ? 24.113  7.801   -21.870 1.00 23.03  ? 458 ILE   B CG2  1 
ATOM   3863 C  CD1  . ILE   B 1 447 ? 24.708  6.936   -25.598 1.00 26.83  ? 458 ILE   B CD1  1 
ATOM   3864 N  N    . GLU   B 1 448 ? 25.359  4.924   -20.926 1.00 20.55  ? 459 GLU   B N    1 
ATOM   3865 C  CA   . GLU   B 1 448 ? 26.596  4.617   -20.223 1.00 23.42  ? 459 GLU   B CA   1 
ATOM   3866 C  C    . GLU   B 1 448 ? 26.821  3.122   -20.047 1.00 26.16  ? 459 GLU   B C    1 
ATOM   3867 O  O    . GLU   B 1 448 ? 27.928  2.724   -19.679 1.00 25.44  ? 459 GLU   B O    1 
ATOM   3868 C  CB   . GLU   B 1 448 ? 26.634  5.289   -18.843 1.00 30.72  ? 459 GLU   B CB   1 
ATOM   3869 C  CG   . GLU   B 1 448 ? 26.635  6.816   -18.894 1.00 29.16  ? 459 GLU   B CG   1 
ATOM   3870 C  CD   . GLU   B 1 448 ? 26.908  7.446   -17.536 1.00 49.19  ? 459 GLU   B CD   1 
ATOM   3871 O  OE1  . GLU   B 1 448 ? 26.737  6.761   -16.494 1.00 44.12  ? 459 GLU   B OE1  1 
ATOM   3872 O  OE2  . GLU   B 1 448 ? 27.312  8.629   -17.511 1.00 52.73  ? 459 GLU   B OE2  1 
ATOM   3873 N  N    . GLY   B 1 449 ? 25.806  2.284   -20.258 1.00 23.24  ? 460 GLY   B N    1 
ATOM   3874 C  CA   . GLY   B 1 449 ? 26.012  0.850   -20.163 1.00 26.59  ? 460 GLY   B CA   1 
ATOM   3875 C  C    . GLY   B 1 449 ? 25.806  0.240   -18.792 1.00 28.37  ? 460 GLY   B C    1 
ATOM   3876 O  O    . GLY   B 1 449 ? 25.978  -0.977  -18.644 1.00 34.38  ? 460 GLY   B O    1 
ATOM   3877 N  N    . GLU   B 1 450 ? 25.546  1.048   -17.771 1.00 26.10  ? 461 GLU   B N    1 
ATOM   3878 C  CA   . GLU   B 1 450 ? 25.402  0.553   -16.412 1.00 34.17  ? 461 GLU   B CA   1 
ATOM   3879 C  C    . GLU   B 1 450 ? 24.563  1.551   -15.637 1.00 29.99  ? 461 GLU   B C    1 
ATOM   3880 O  O    . GLU   B 1 450 ? 24.504  2.734   -16.000 1.00 29.58  ? 461 GLU   B O    1 
ATOM   3881 C  CB   . GLU   B 1 450 ? 26.770  0.358   -15.739 1.00 41.67  ? 461 GLU   B CB   1 
ATOM   3882 C  CG   . GLU   B 1 450 ? 27.579  1.633   -15.652 1.00 39.57  ? 461 GLU   B CG   1 
ATOM   3883 C  CD   . GLU   B 1 450 ? 28.990  1.391   -15.164 1.00 58.83  ? 461 GLU   B CD   1 
ATOM   3884 O  OE1  . GLU   B 1 450 ? 29.484  0.252   -15.313 1.00 52.58  ? 461 GLU   B OE1  1 
ATOM   3885 O  OE2  . GLU   B 1 450 ? 29.604  2.339   -14.630 1.00 67.59  ? 461 GLU   B OE2  1 
ATOM   3886 N  N    . PRO   B 1 451 ? 23.903  1.121   -14.563 1.00 37.75  ? 462 PRO   B N    1 
ATOM   3887 C  CA   . PRO   B 1 451 ? 23.177  2.083   -13.743 1.00 30.30  ? 462 PRO   B CA   1 
ATOM   3888 C  C    . PRO   B 1 451 ? 24.131  2.996   -12.997 1.00 32.56  ? 462 PRO   B C    1 
ATOM   3889 O  O    . PRO   B 1 451 ? 25.265  2.605   -12.669 1.00 33.81  ? 462 PRO   B O    1 
ATOM   3890 C  CB   . PRO   B 1 451 ? 22.373  1.193   -12.778 1.00 33.83  ? 462 PRO   B CB   1 
ATOM   3891 C  CG   . PRO   B 1 451 ? 23.131  -0.094  -12.710 1.00 42.35  ? 462 PRO   B CG   1 
ATOM   3892 C  CD   . PRO   B 1 451 ? 23.790  -0.264  -14.057 1.00 35.46  ? 462 PRO   B CD   1 
ATOM   3893 N  N    . PRO   B 1 452 ? 23.717  4.231   -12.712 1.00 31.34  ? 463 PRO   B N    1 
ATOM   3894 C  CA   . PRO   B 1 452 ? 24.505  5.135   -11.866 1.00 43.23  ? 463 PRO   B CA   1 
ATOM   3895 C  C    . PRO   B 1 452 ? 24.650  4.601   -10.445 1.00 44.26  ? 463 PRO   B C    1 
ATOM   3896 O  O    . PRO   B 1 452 ? 23.893  3.734   -10.003 1.00 37.28  ? 463 PRO   B O    1 
ATOM   3897 C  CB   . PRO   B 1 452 ? 23.700  6.443   -11.885 1.00 40.82  ? 463 PRO   B CB   1 
ATOM   3898 C  CG   . PRO   B 1 452 ? 22.766  6.328   -13.047 1.00 50.25  ? 463 PRO   B CG   1 
ATOM   3899 C  CD   . PRO   B 1 452 ? 22.472  4.858   -13.187 1.00 39.23  ? 463 PRO   B CD   1 
ATOM   3900 N  N    . TYR   B 1 453 ? 25.673  5.103   -9.742  1.00 36.05  ? 464 TYR   B N    1 
ATOM   3901 C  CA   . TYR   B 1 453 ? 25.928  4.812   -8.327  1.00 33.22  ? 464 TYR   B CA   1 
ATOM   3902 C  C    . TYR   B 1 453 ? 26.375  3.378   -8.076  1.00 52.74  ? 464 TYR   B C    1 
ATOM   3903 O  O    . TYR   B 1 453 ? 26.371  2.926   -6.925  1.00 45.99  ? 464 TYR   B O    1 
ATOM   3904 C  CB   . TYR   B 1 453 ? 24.707  5.112   -7.445  1.00 38.66  ? 464 TYR   B CB   1 
ATOM   3905 C  CG   . TYR   B 1 453 ? 24.122  6.489   -7.626  1.00 31.88  ? 464 TYR   B CG   1 
ATOM   3906 C  CD1  . TYR   B 1 453 ? 24.892  7.619   -7.385  1.00 38.04  ? 464 TYR   B CD1  1 
ATOM   3907 C  CD2  . TYR   B 1 453 ? 22.820  6.667   -8.055  1.00 32.74  ? 464 TYR   B CD2  1 
ATOM   3908 C  CE1  . TYR   B 1 453 ? 24.373  8.883   -7.534  1.00 35.22  ? 464 TYR   B CE1  1 
ATOM   3909 C  CE2  . TYR   B 1 453 ? 22.298  7.935   -8.223  1.00 33.01  ? 464 TYR   B CE2  1 
ATOM   3910 C  CZ   . TYR   B 1 453 ? 23.081  9.036   -7.954  1.00 34.63  ? 464 TYR   B CZ   1 
ATOM   3911 O  OH   . TYR   B 1 453 ? 22.582  10.304  -8.113  1.00 42.60  ? 464 TYR   B OH   1 
ATOM   3912 N  N    . LEU   B 1 454 ? 26.790  2.658   -9.116  1.00 45.55  ? 465 LEU   B N    1 
ATOM   3913 C  CA   . LEU   B 1 454 ? 27.091  1.240   -8.968  1.00 47.44  ? 465 LEU   B CA   1 
ATOM   3914 C  C    . LEU   B 1 454 ? 28.190  0.991   -7.939  1.00 52.46  ? 465 LEU   B C    1 
ATOM   3915 O  O    . LEU   B 1 454 ? 28.162  -0.018  -7.226  1.00 54.52  ? 465 LEU   B O    1 
ATOM   3916 C  CB   . LEU   B 1 454 ? 27.479  0.678   -10.336 1.00 47.71  ? 465 LEU   B CB   1 
ATOM   3917 C  CG   . LEU   B 1 454 ? 27.341  -0.821  -10.549 1.00 58.06  ? 465 LEU   B CG   1 
ATOM   3918 C  CD1  . LEU   B 1 454 ? 25.916  -1.218  -10.208 1.00 53.90  ? 465 LEU   B CD1  1 
ATOM   3919 C  CD2  . LEU   B 1 454 ? 27.664  -1.158  -11.999 1.00 58.24  ? 465 LEU   B CD2  1 
ATOM   3920 N  N    . ASN   B 1 455 ? 29.178  1.880   -7.857  1.00 40.56  ? 466 ASN   B N    1 
ATOM   3921 C  CA   . ASN   B 1 455 ? 30.258  1.746   -6.887  1.00 57.16  ? 466 ASN   B CA   1 
ATOM   3922 C  C    . ASN   B 1 455 ? 29.965  2.382   -5.527  1.00 52.57  ? 466 ASN   B C    1 
ATOM   3923 O  O    . ASN   B 1 455 ? 30.838  2.341   -4.653  1.00 59.30  ? 466 ASN   B O    1 
ATOM   3924 C  CB   . ASN   B 1 455 ? 31.573  2.288   -7.467  1.00 65.95  ? 466 ASN   B CB   1 
ATOM   3925 C  CG   . ASN   B 1 455 ? 31.495  3.747   -7.868  1.00 73.34  ? 466 ASN   B CG   1 
ATOM   3926 O  OD1  . ASN   B 1 455 ? 30.549  4.457   -7.530  1.00 75.09  ? 466 ASN   B OD1  1 
ATOM   3927 N  ND2  . ASN   B 1 455 ? 32.506  4.203   -8.606  1.00 81.99  ? 466 ASN   B ND2  1 
ATOM   3928 N  N    . GLU   B 1 456 ? 28.799  3.002   -5.330  1.00 44.96  ? 467 GLU   B N    1 
ATOM   3929 C  CA   . GLU   B 1 456 ? 28.500  3.669   -4.068  1.00 45.16  ? 467 GLU   B CA   1 
ATOM   3930 C  C    . GLU   B 1 456 ? 27.747  2.766   -3.098  1.00 42.11  ? 467 GLU   B C    1 
ATOM   3931 O  O    . GLU   B 1 456 ? 26.945  1.918   -3.500  1.00 39.53  ? 467 GLU   B O    1 
ATOM   3932 C  CB   . GLU   B 1 456 ? 27.655  4.927   -4.305  1.00 42.25  ? 467 GLU   B CB   1 
ATOM   3933 C  CG   . GLU   B 1 456 ? 28.234  5.918   -5.291  1.00 53.25  ? 467 GLU   B CG   1 
ATOM   3934 C  CD   . GLU   B 1 456 ? 29.445  6.644   -4.743  1.00 49.33  ? 467 GLU   B CD   1 
ATOM   3935 O  OE1  . GLU   B 1 456 ? 29.773  6.458   -3.552  1.00 53.64  ? 467 GLU   B OE1  1 
ATOM   3936 O  OE2  . GLU   B 1 456 ? 30.074  7.403   -5.506  1.00 64.97  ? 467 GLU   B OE2  1 
ATOM   3937 N  N    . ASN   B 1 457 ? 27.957  3.007   -1.804  1.00 39.99  ? 468 ASN   B N    1 
ATOM   3938 C  CA   . ASN   B 1 457 ? 27.125  2.358   -0.810  1.00 34.29  ? 468 ASN   B CA   1 
ATOM   3939 C  C    . ASN   B 1 457 ? 25.719  2.938   -0.902  1.00 32.62  ? 468 ASN   B C    1 
ATOM   3940 O  O    . ASN   B 1 457 ? 25.545  4.088   -1.316  1.00 35.08  ? 468 ASN   B O    1 
ATOM   3941 C  CB   . ASN   B 1 457 ? 27.695  2.545   0.591   1.00 40.25  ? 468 ASN   B CB   1 
ATOM   3942 C  CG   . ASN   B 1 457 ? 29.014  1.835   0.767   1.00 55.86  ? 468 ASN   B CG   1 
ATOM   3943 O  OD1  . ASN   B 1 457 ? 30.012  2.450   1.127   1.00 56.65  ? 468 ASN   B OD1  1 
ATOM   3944 N  ND2  . ASN   B 1 457 ? 29.033  0.533   0.488   1.00 53.48  ? 468 ASN   B ND2  1 
ATOM   3945 N  N    . PRO   B 1 458 ? 24.695  2.156   -0.549  1.00 35.08  ? 469 PRO   B N    1 
ATOM   3946 C  CA   . PRO   B 1 458 ? 23.317  2.651   -0.721  1.00 30.51  ? 469 PRO   B CA   1 
ATOM   3947 C  C    . PRO   B 1 458 ? 23.032  3.937   0.024   1.00 31.96  ? 469 PRO   B C    1 
ATOM   3948 O  O    . PRO   B 1 458 ? 22.329  4.810   -0.505  1.00 32.77  ? 469 PRO   B O    1 
ATOM   3949 C  CB   . PRO   B 1 458 ? 22.463  1.488   -0.191  1.00 38.90  ? 469 PRO   B CB   1 
ATOM   3950 C  CG   . PRO   B 1 458 ? 23.326  0.272   -0.416  1.00 43.38  ? 469 PRO   B CG   1 
ATOM   3951 C  CD   . PRO   B 1 458 ? 24.732  0.739   -0.144  1.00 40.72  ? 469 PRO   B CD   1 
ATOM   3952 N  N    . LEU   B 1 459 ? 23.572  4.092   1.235   1.00 27.13  ? 470 LEU   B N    1 
ATOM   3953 C  CA   . LEU   B 1 459 ? 23.287  5.292   2.007   1.00 28.63  ? 470 LEU   B CA   1 
ATOM   3954 C  C    . LEU   B 1 459 ? 23.935  6.510   1.359   1.00 35.02  ? 470 LEU   B C    1 
ATOM   3955 O  O    . LEU   B 1 459 ? 23.336  7.590   1.323   1.00 32.30  ? 470 LEU   B O    1 
ATOM   3956 C  CB   . LEU   B 1 459 ? 23.764  5.111   3.451   1.00 36.53  ? 470 LEU   B CB   1 
ATOM   3957 C  CG   . LEU   B 1 459 ? 22.799  4.323   4.348   1.00 29.56  ? 470 LEU   B CG   1 
ATOM   3958 C  CD1  . LEU   B 1 459 ? 23.357  4.175   5.767   1.00 31.62  ? 470 LEU   B CD1  1 
ATOM   3959 C  CD2  . LEU   B 1 459 ? 21.397  4.913   4.369   1.00 35.60  ? 470 LEU   B CD2  1 
ATOM   3960 N  N    . ARG   B 1 460 ? 25.162  6.356   0.855   1.00 32.24  ? 471 ARG   B N    1 
ATOM   3961 C  CA   . ARG   B 1 460 ? 25.811  7.449   0.132   1.00 34.49  ? 471 ARG   B CA   1 
ATOM   3962 C  C    . ARG   B 1 460 ? 25.041  7.809   -1.132  1.00 31.38  ? 471 ARG   B C    1 
ATOM   3963 O  O    . ARG   B 1 460 ? 24.824  8.991   -1.420  1.00 31.97  ? 471 ARG   B O    1 
ATOM   3964 C  CB   . ARG   B 1 460 ? 27.253  7.073   -0.207  1.00 32.92  ? 471 ARG   B CB   1 
ATOM   3965 C  CG   . ARG   B 1 460 ? 28.013  8.102   -1.062  1.00 36.68  ? 471 ARG   B CG   1 
ATOM   3966 C  CD   . ARG   B 1 460 ? 28.193  9.439   -0.347  1.00 37.35  ? 471 ARG   B CD   1 
ATOM   3967 N  NE   . ARG   B 1 460 ? 28.956  10.388  -1.156  1.00 35.74  ? 471 ARG   B NE   1 
ATOM   3968 C  CZ   . ARG   B 1 460 ? 29.161  11.658  -0.827  1.00 41.51  ? 471 ARG   B CZ   1 
ATOM   3969 N  NH1  . ARG   B 1 460 ? 28.638  12.181  0.268   1.00 36.20  ? 471 ARG   B NH1  1 
ATOM   3970 N  NH2  . ARG   B 1 460 ? 29.925  12.416  -1.608  1.00 37.65  ? 471 ARG   B NH2  1 
ATOM   3971 N  N    . ALA   B 1 461 ? 24.586  6.803   -1.881  1.00 30.22  ? 472 ALA   B N    1 
ATOM   3972 C  CA   . ALA   B 1 461 ? 23.804  7.079   -3.081  1.00 26.18  ? 472 ALA   B CA   1 
ATOM   3973 C  C    . ALA   B 1 461 ? 22.501  7.791   -2.740  1.00 31.58  ? 472 ALA   B C    1 
ATOM   3974 O  O    . ALA   B 1 461 ? 22.073  8.699   -3.462  1.00 26.62  ? 472 ALA   B O    1 
ATOM   3975 C  CB   . ALA   B 1 461 ? 23.536  5.779   -3.836  1.00 25.86  ? 472 ALA   B CB   1 
ATOM   3976 N  N    . LEU   B 1 462 ? 21.854  7.402   -1.638  1.00 30.49  ? 473 LEU   B N    1 
ATOM   3977 C  CA   . LEU   B 1 462 ? 20.644  8.107   -1.225  1.00 30.20  ? 473 LEU   B CA   1 
ATOM   3978 C  C    . LEU   B 1 462 ? 20.911  9.576   -0.962  1.00 28.82  ? 473 LEU   B C    1 
ATOM   3979 O  O    . LEU   B 1 462 ? 20.132  10.440  -1.376  1.00 33.39  ? 473 LEU   B O    1 
ATOM   3980 C  CB   . LEU   B 1 462 ? 20.038  7.458   0.018   1.00 37.96  ? 473 LEU   B CB   1 
ATOM   3981 C  CG   . LEU   B 1 462 ? 19.063  6.312   -0.227  1.00 47.68  ? 473 LEU   B CG   1 
ATOM   3982 C  CD1  . LEU   B 1 462 ? 17.678  6.911   -0.353  1.00 50.39  ? 473 LEU   B CD1  1 
ATOM   3983 C  CD2  . LEU   B 1 462 ? 19.398  5.529   -1.474  1.00 55.02  ? 473 LEU   B CD2  1 
ATOM   3984 N  N    . TYR   B 1 463 ? 22.002  9.882   -0.264  1.00 32.74  ? 474 TYR   B N    1 
ATOM   3985 C  CA   . TYR   B 1 463 ? 22.338  11.274  -0.006  1.00 31.16  ? 474 TYR   B CA   1 
ATOM   3986 C  C    . TYR   B 1 463 ? 22.609  12.022  -1.310  1.00 38.67  ? 474 TYR   B C    1 
ATOM   3987 O  O    . TYR   B 1 463 ? 22.161  13.161  -1.494  1.00 37.41  ? 474 TYR   B O    1 
ATOM   3988 C  CB   . TYR   B 1 463 ? 23.544  11.338  0.929   1.00 31.14  ? 474 TYR   B CB   1 
ATOM   3989 C  CG   . TYR   B 1 463 ? 23.910  12.738  1.314   1.00 40.30  ? 474 TYR   B CG   1 
ATOM   3990 C  CD1  . TYR   B 1 463 ? 23.284  13.349  2.396   1.00 50.63  ? 474 TYR   B CD1  1 
ATOM   3991 C  CD2  . TYR   B 1 463 ? 24.851  13.463  0.603   1.00 45.31  ? 474 TYR   B CD2  1 
ATOM   3992 C  CE1  . TYR   B 1 463 ? 23.593  14.637  2.765   1.00 53.65  ? 474 TYR   B CE1  1 
ATOM   3993 C  CE2  . TYR   B 1 463 ? 25.171  14.761  0.967   1.00 43.40  ? 474 TYR   B CE2  1 
ATOM   3994 C  CZ   . TYR   B 1 463 ? 24.533  15.344  2.044   1.00 52.38  ? 474 TYR   B CZ   1 
ATOM   3995 O  OH   . TYR   B 1 463 ? 24.845  16.634  2.414   1.00 57.75  ? 474 TYR   B OH   1 
ATOM   3996 N  N    . LEU   B 1 464 ? 23.338  11.390  -2.235  1.00 28.37  ? 475 LEU   B N    1 
ATOM   3997 C  CA   . LEU   B 1 464 ? 23.652  12.038  -3.503  1.00 34.85  ? 475 LEU   B CA   1 
ATOM   3998 C  C    . LEU   B 1 464 ? 22.388  12.308  -4.313  1.00 29.82  ? 475 LEU   B C    1 
ATOM   3999 O  O    . LEU   B 1 464 ? 22.250  13.372  -4.926  1.00 37.85  ? 475 LEU   B O    1 
ATOM   4000 C  CB   . LEU   B 1 464 ? 24.621  11.165  -4.303  1.00 27.08  ? 475 LEU   B CB   1 
ATOM   4001 C  CG   . LEU   B 1 464 ? 26.008  11.016  -3.678  1.00 31.38  ? 475 LEU   B CG   1 
ATOM   4002 C  CD1  . LEU   B 1 464 ? 26.785  9.927   -4.408  1.00 34.06  ? 475 LEU   B CD1  1 
ATOM   4003 C  CD2  . LEU   B 1 464 ? 26.765  12.353  -3.711  1.00 31.41  ? 475 LEU   B CD2  1 
ATOM   4004 N  N    . ILE   B 1 465 ? 21.446  11.364  -4.315  1.00 30.62  ? 476 ILE   B N    1 
ATOM   4005 C  CA   . ILE   B 1 465 ? 20.202  11.583  -5.045  1.00 28.24  ? 476 ILE   B CA   1 
ATOM   4006 C  C    . ILE   B 1 465 ? 19.453  12.765  -4.456  1.00 33.27  ? 476 ILE   B C    1 
ATOM   4007 O  O    . ILE   B 1 465 ? 18.954  13.631  -5.185  1.00 33.95  ? 476 ILE   B O    1 
ATOM   4008 C  CB   . ILE   B 1 465 ? 19.325  10.323  -5.027  1.00 30.59  ? 476 ILE   B CB   1 
ATOM   4009 C  CG1  . ILE   B 1 465 ? 19.968  9.184   -5.813  1.00 25.31  ? 476 ILE   B CG1  1 
ATOM   4010 C  CG2  . ILE   B 1 465 ? 17.938  10.651  -5.594  1.00 30.61  ? 476 ILE   B CG2  1 
ATOM   4011 C  CD1  . ILE   B 1 465 ? 19.290  7.869   -5.557  1.00 31.07  ? 476 ILE   B CD1  1 
ATOM   4012 N  N    . ALA   B 1 466 ? 19.376  12.826  -3.125  1.00 32.74  ? 477 ALA   B N    1 
ATOM   4013 C  CA   . ALA   B 1 466 ? 18.617  13.886  -2.473  1.00 35.60  ? 477 ALA   B CA   1 
ATOM   4014 C  C    . ALA   B 1 466 ? 19.227  15.259  -2.721  1.00 48.22  ? 477 ALA   B C    1 
ATOM   4015 O  O    . ALA   B 1 466 ? 18.496  16.247  -2.857  1.00 46.87  ? 477 ALA   B O    1 
ATOM   4016 C  CB   . ALA   B 1 466 ? 18.529  13.601  -0.973  1.00 31.61  ? 477 ALA   B CB   1 
ATOM   4017 N  N    . THR   B 1 467 ? 20.559  15.350  -2.780  1.00 42.41  ? 478 THR   B N    1 
ATOM   4018 C  CA   . THR   B 1 467 ? 21.226  16.650  -2.792  1.00 43.24  ? 478 THR   B CA   1 
ATOM   4019 C  C    . THR   B 1 467 ? 21.736  17.071  -4.159  1.00 52.73  ? 478 THR   B C    1 
ATOM   4020 O  O    . THR   B 1 467 ? 21.632  18.246  -4.515  1.00 58.29  ? 478 THR   B O    1 
ATOM   4021 C  CB   . THR   B 1 467 ? 22.399  16.655  -1.802  1.00 42.78  ? 478 THR   B CB   1 
ATOM   4022 O  OG1  . THR   B 1 467 ? 23.331  15.624  -2.148  1.00 50.81  ? 478 THR   B OG1  1 
ATOM   4023 C  CG2  . THR   B 1 467 ? 21.897  16.372  -0.409  1.00 40.21  ? 478 THR   B CG2  1 
ATOM   4024 N  N    . ASN   B 1 468 ? 22.293  16.145  -4.937  1.00 55.31  ? 479 ASN   B N    1 
ATOM   4025 C  CA   . ASN   B 1 468 ? 22.718  16.486  -6.286  1.00 44.33  ? 479 ASN   B CA   1 
ATOM   4026 C  C    . ASN   B 1 468 ? 21.570  16.370  -7.269  1.00 60.11  ? 479 ASN   B C    1 
ATOM   4027 O  O    . ASN   B 1 468 ? 21.526  17.110  -8.260  1.00 57.99  ? 479 ASN   B O    1 
ATOM   4028 C  CB   . ASN   B 1 468 ? 23.867  15.591  -6.754  1.00 53.89  ? 479 ASN   B CB   1 
ATOM   4029 C  CG   . ASN   B 1 468 ? 25.174  15.894  -6.054  1.00 62.03  ? 479 ASN   B CG   1 
ATOM   4030 O  OD1  . ASN   B 1 468 ? 25.254  16.790  -5.211  1.00 71.86  ? 479 ASN   B OD1  1 
ATOM   4031 N  ND2  . ASN   B 1 468 ? 26.220  15.162  -6.420  1.00 67.94  ? 479 ASN   B ND2  1 
ATOM   4032 N  N    . GLY   B 1 469 ? 20.629  15.469  -7.002  1.00 57.33  ? 480 GLY   B N    1 
ATOM   4033 C  CA   . GLY   B 1 469 ? 19.632  15.167  -7.996  1.00 52.71  ? 480 GLY   B CA   1 
ATOM   4034 C  C    . GLY   B 1 469 ? 20.250  14.265  -9.039  1.00 66.87  ? 480 GLY   B C    1 
ATOM   4035 O  O    . GLY   B 1 469 ? 20.557  13.100  -8.755  1.00 58.42  ? 480 GLY   B O    1 
ATOM   4036 N  N    . THR   B 1 470 ? 20.413  14.797  -10.248 1.00 68.63  ? 481 THR   B N    1 
ATOM   4037 C  CA   . THR   B 1 470 ? 20.960  14.029  -11.356 1.00 63.93  ? 481 THR   B CA   1 
ATOM   4038 C  C    . THR   B 1 470 ? 22.328  13.458  -10.999 1.00 67.36  ? 481 THR   B C    1 
ATOM   4039 O  O    . THR   B 1 470 ? 23.147  14.138  -10.364 1.00 67.69  ? 481 THR   B O    1 
ATOM   4040 C  CB   . THR   B 1 470 ? 21.097  14.892  -12.615 1.00 57.13  ? 481 THR   B CB   1 
ATOM   4041 O  OG1  . THR   B 1 470 ? 21.610  14.088  -13.686 1.00 57.98  ? 481 THR   B OG1  1 
ATOM   4042 C  CG2  . THR   B 1 470 ? 22.057  16.063  -12.378 1.00 48.81  ? 481 THR   B CG2  1 
ATOM   4043 N  N    . PRO   B 1 471 ? 22.588  12.199  -11.327 1.00 74.04  ? 482 PRO   B N    1 
ATOM   4044 C  CA   . PRO   B 1 471 ? 23.942  11.680  -11.164 1.00 79.74  ? 482 PRO   B CA   1 
ATOM   4045 C  C    . PRO   B 1 471 ? 24.826  12.386  -12.175 1.00 74.38  ? 482 PRO   B C    1 
ATOM   4046 O  O    . PRO   B 1 471 ? 24.358  12.926  -13.180 1.00 70.04  ? 482 PRO   B O    1 
ATOM   4047 C  CB   . PRO   B 1 471 ? 23.797  10.188  -11.482 1.00 67.08  ? 482 PRO   B CB   1 
ATOM   4048 C  CG   . PRO   B 1 471 ? 22.673  10.151  -12.473 1.00 69.16  ? 482 PRO   B CG   1 
ATOM   4049 C  CD   . PRO   B 1 471 ? 21.717  11.254  -12.049 1.00 56.99  ? 482 PRO   B CD   1 
ATOM   4050 N  N    . GLU   B 1 472 ? 26.118  12.396  -11.905 1.00 72.67  ? 483 GLU   B N    1 
ATOM   4051 C  CA   . GLU   B 1 472 ? 27.011  13.047  -12.842 1.00 78.85  ? 483 GLU   B CA   1 
ATOM   4052 C  C    . GLU   B 1 472 ? 27.219  12.090  -14.002 1.00 77.86  ? 483 GLU   B C    1 
ATOM   4053 O  O    . GLU   B 1 472 ? 27.411  10.887  -13.796 1.00 77.08  ? 483 GLU   B O    1 
ATOM   4054 C  CB   . GLU   B 1 472 ? 28.334  13.413  -12.172 1.00 90.08  ? 483 GLU   B CB   1 
ATOM   4055 C  CG   . GLU   B 1 472 ? 28.162  14.239  -10.893 1.00 105.74 ? 483 GLU   B CG   1 
ATOM   4056 C  CD   . GLU   B 1 472 ? 27.807  15.694  -11.162 1.00 111.61 ? 483 GLU   B CD   1 
ATOM   4057 O  OE1  . GLU   B 1 472 ? 27.968  16.152  -12.317 1.00 105.26 ? 483 GLU   B OE1  1 
ATOM   4058 O  OE2  . GLU   B 1 472 ? 27.350  16.374  -10.216 1.00 103.98 ? 483 GLU   B OE2  1 
ATOM   4059 N  N    . LEU   B 1 473 ? 27.157  12.613  -15.221 1.00 62.64  ? 484 LEU   B N    1 
ATOM   4060 C  CA   . LEU   B 1 473 ? 27.439  11.770  -16.369 1.00 51.68  ? 484 LEU   B CA   1 
ATOM   4061 C  C    . LEU   B 1 473 ? 28.922  11.438  -16.360 1.00 52.16  ? 484 LEU   B C    1 
ATOM   4062 O  O    . LEU   B 1 473 ? 29.759  12.294  -16.066 1.00 48.56  ? 484 LEU   B O    1 
ATOM   4063 C  CB   . LEU   B 1 473 ? 27.058  12.496  -17.660 1.00 52.93  ? 484 LEU   B CB   1 
ATOM   4064 C  CG   . LEU   B 1 473 ? 25.569  12.756  -17.920 1.00 49.76  ? 484 LEU   B CG   1 
ATOM   4065 C  CD1  . LEU   B 1 473 ? 25.383  13.674  -19.121 1.00 51.73  ? 484 LEU   B CD1  1 
ATOM   4066 C  CD2  . LEU   B 1 473 ? 24.809  11.464  -18.115 1.00 50.14  ? 484 LEU   B CD2  1 
ATOM   4067 N  N    . GLN   B 1 474 ? 29.250  10.185  -16.673 1.00 39.93  ? 485 GLN   B N    1 
ATOM   4068 C  CA   . GLN   B 1 474 ? 30.656  9.799   -16.702 1.00 52.38  ? 485 GLN   B CA   1 
ATOM   4069 C  C    . GLN   B 1 474 ? 31.390  10.475  -17.851 1.00 50.86  ? 485 GLN   B C    1 
ATOM   4070 O  O    . GLN   B 1 474 ? 32.554  10.865  -17.706 1.00 52.62  ? 485 GLN   B O    1 
ATOM   4071 C  CB   . GLN   B 1 474 ? 30.792  8.282   -16.789 1.00 45.74  ? 485 GLN   B CB   1 
ATOM   4072 C  CG   . GLN   B 1 474 ? 30.194  7.542   -15.608 1.00 62.16  ? 485 GLN   B CG   1 
ATOM   4073 C  CD   . GLN   B 1 474 ? 30.492  6.057   -15.655 1.00 69.36  ? 485 GLN   B CD   1 
ATOM   4074 O  OE1  . GLN   B 1 474 ? 31.654  5.650   -15.719 1.00 71.08  ? 485 GLN   B OE1  1 
ATOM   4075 N  NE2  . GLN   B 1 474 ? 29.442  5.237   -15.616 1.00 62.39  ? 485 GLN   B NE2  1 
ATOM   4076 N  N    . ASN   B 1 475 ? 30.729  10.626  -18.994 1.00 44.97  ? 486 ASN   B N    1 
ATOM   4077 C  CA   . ASN   B 1 475 ? 31.333  11.223  -20.185 1.00 48.12  ? 486 ASN   B CA   1 
ATOM   4078 C  C    . ASN   B 1 475 ? 30.307  12.126  -20.852 1.00 47.60  ? 486 ASN   B C    1 
ATOM   4079 O  O    . ASN   B 1 475 ? 29.751  11.793  -21.904 1.00 41.28  ? 486 ASN   B O    1 
ATOM   4080 C  CB   . ASN   B 1 475 ? 31.820  10.134  -21.144 1.00 52.50  ? 486 ASN   B CB   1 
ATOM   4081 C  CG   . ASN   B 1 475 ? 32.924  9.284   -20.546 1.00 61.67  ? 486 ASN   B CG   1 
ATOM   4082 O  OD1  . ASN   B 1 475 ? 32.670  8.208   -19.999 1.00 57.18  ? 486 ASN   B OD1  1 
ATOM   4083 N  ND2  . ASN   B 1 475 ? 34.158  9.769   -20.637 1.00 56.77  ? 486 ASN   B ND2  1 
ATOM   4084 N  N    . PRO   B 1 476 ? 30.032  13.293  -20.264 1.00 47.96  ? 487 PRO   B N    1 
ATOM   4085 C  CA   . PRO   B 1 476 ? 28.990  14.167  -20.833 1.00 48.45  ? 487 PRO   B CA   1 
ATOM   4086 C  C    . PRO   B 1 476 ? 29.315  14.664  -22.232 1.00 48.45  ? 487 PRO   B C    1 
ATOM   4087 O  O    . PRO   B 1 476 ? 28.393  14.995  -22.995 1.00 46.44  ? 487 PRO   B O    1 
ATOM   4088 C  CB   . PRO   B 1 476 ? 28.917  15.324  -19.831 1.00 43.24  ? 487 PRO   B CB   1 
ATOM   4089 C  CG   . PRO   B 1 476 ? 30.276  15.346  -19.195 1.00 48.22  ? 487 PRO   B CG   1 
ATOM   4090 C  CD   . PRO   B 1 476 ? 30.710  13.910  -19.111 1.00 43.90  ? 487 PRO   B CD   1 
ATOM   4091 N  N    . GLU   B 1 477 ? 30.596  14.716  -22.598 1.00 52.31  ? 488 GLU   B N    1 
ATOM   4092 C  CA   . GLU   B 1 477 ? 30.975  15.190  -23.924 1.00 52.58  ? 488 GLU   B CA   1 
ATOM   4093 C  C    . GLU   B 1 477 ? 30.508  14.251  -25.027 1.00 41.70  ? 488 GLU   B C    1 
ATOM   4094 O  O    . GLU   B 1 477 ? 30.374  14.681  -26.177 1.00 46.69  ? 488 GLU   B O    1 
ATOM   4095 C  CB   . GLU   B 1 477 ? 32.498  15.357  -24.007 1.00 55.45  ? 488 GLU   B CB   1 
ATOM   4096 C  CG   . GLU   B 1 477 ? 33.272  14.034  -24.047 1.00 53.86  ? 488 GLU   B CG   1 
ATOM   4097 C  CD   . GLU   B 1 477 ? 33.398  13.355  -22.687 1.00 66.96  ? 488 GLU   B CD   1 
ATOM   4098 O  OE1  . GLU   B 1 477 ? 33.035  13.978  -21.660 1.00 57.85  ? 488 GLU   B OE1  1 
ATOM   4099 O  OE2  . GLU   B 1 477 ? 33.839  12.181  -22.656 1.00 62.24  ? 488 GLU   B OE2  1 
ATOM   4100 N  N    . LYS   B 1 478 ? 30.235  12.991  -24.696 1.00 39.80  ? 489 LYS   B N    1 
ATOM   4101 C  CA   . LYS   B 1 478 ? 29.816  12.000  -25.672 1.00 38.36  ? 489 LYS   B CA   1 
ATOM   4102 C  C    . LYS   B 1 478 ? 28.340  12.082  -26.041 1.00 36.86  ? 489 LYS   B C    1 
ATOM   4103 O  O    . LYS   B 1 478 ? 27.906  11.341  -26.927 1.00 35.01  ? 489 LYS   B O    1 
ATOM   4104 C  CB   . LYS   B 1 478 ? 30.145  10.603  -25.145 1.00 42.51  ? 489 LYS   B CB   1 
ATOM   4105 C  CG   . LYS   B 1 478 ? 31.628  10.435  -24.827 1.00 51.99  ? 489 LYS   B CG   1 
ATOM   4106 C  CD   . LYS   B 1 478 ? 32.010  8.979   -24.631 1.00 56.98  ? 489 LYS   B CD   1 
ATOM   4107 C  CE   . LYS   B 1 478 ? 33.507  8.835   -24.433 1.00 65.23  ? 489 LYS   B CE   1 
ATOM   4108 N  NZ   . LYS   B 1 478 ? 33.941  7.414   -24.506 1.00 76.37  ? 489 LYS   B NZ   1 
ATOM   4109 N  N    . LEU   B 1 479 ? 27.557  12.935  -25.388 1.00 29.78  ? 490 LEU   B N    1 
ATOM   4110 C  CA   . LEU   B 1 479 ? 26.131  13.043  -25.667 1.00 32.77  ? 490 LEU   B CA   1 
ATOM   4111 C  C    . LEU   B 1 479 ? 25.860  14.259  -26.542 1.00 26.23  ? 490 LEU   B C    1 
ATOM   4112 O  O    . LEU   B 1 479 ? 26.464  15.312  -26.350 1.00 29.63  ? 490 LEU   B O    1 
ATOM   4113 C  CB   . LEU   B 1 479 ? 25.315  13.136  -24.367 1.00 28.69  ? 490 LEU   B CB   1 
ATOM   4114 C  CG   . LEU   B 1 479 ? 25.122  11.876  -23.508 1.00 32.39  ? 490 LEU   B CG   1 
ATOM   4115 C  CD1  . LEU   B 1 479 ? 26.406  11.264  -23.013 1.00 39.18  ? 490 LEU   B CD1  1 
ATOM   4116 C  CD2  . LEU   B 1 479 ? 24.231  12.221  -22.333 1.00 37.63  ? 490 LEU   B CD2  1 
ATOM   4117 N  N    . SER   B 1 480 ? 24.934  14.115  -27.492 1.00 27.36  ? 491 SER   B N    1 
ATOM   4118 C  CA   . SER   B 1 480 ? 24.552  15.235  -28.342 1.00 28.61  ? 491 SER   B CA   1 
ATOM   4119 C  C    . SER   B 1 480 ? 23.849  16.308  -27.520 1.00 30.31  ? 491 SER   B C    1 
ATOM   4120 O  O    . SER   B 1 480 ? 23.379  16.068  -26.406 1.00 28.11  ? 491 SER   B O    1 
ATOM   4121 C  CB   . SER   B 1 480 ? 23.631  14.783  -29.474 1.00 26.17  ? 491 SER   B CB   1 
ATOM   4122 O  OG   . SER   B 1 480 ? 22.375  14.403  -28.952 1.00 26.55  ? 491 SER   B OG   1 
ATOM   4123 N  N    . ALA   B 1 481 ? 23.802  17.516  -28.080 1.00 28.04  ? 492 ALA   B N    1 
ATOM   4124 C  CA   . ALA   B 1 481 ? 23.088  18.601  -27.418 1.00 32.17  ? 492 ALA   B CA   1 
ATOM   4125 C  C    . ALA   B 1 481 ? 21.622  18.248  -27.183 1.00 31.20  ? 492 ALA   B C    1 
ATOM   4126 O  O    . ALA   B 1 481 ? 21.070  18.523  -26.111 1.00 27.14  ? 492 ALA   B O    1 
ATOM   4127 C  CB   . ALA   B 1 481 ? 23.205  19.878  -28.249 1.00 31.15  ? 492 ALA   B CB   1 
ATOM   4128 N  N    . ILE   B 1 482 ? 20.971  17.637  -28.170 1.00 27.91  ? 493 ILE   B N    1 
ATOM   4129 C  CA   . ILE   B 1 482 ? 19.533  17.418  -28.050 1.00 32.48  ? 493 ILE   B CA   1 
ATOM   4130 C  C    . ILE   B 1 482 ? 19.238  16.331  -27.020 1.00 31.03  ? 493 ILE   B C    1 
ATOM   4131 O  O    . ILE   B 1 482 ? 18.248  16.417  -26.282 1.00 27.30  ? 493 ILE   B O    1 
ATOM   4132 C  CB   . ILE   B 1 482 ? 18.914  17.114  -29.430 1.00 30.93  ? 493 ILE   B CB   1 
ATOM   4133 C  CG1  . ILE   B 1 482 ? 17.386  17.175  -29.360 1.00 30.21  ? 493 ILE   B CG1  1 
ATOM   4134 C  CG2  . ILE   B 1 482 ? 19.409  15.806  -30.003 1.00 28.69  ? 493 ILE   B CG2  1 
ATOM   4135 C  CD1  . ILE   B 1 482 ? 16.874  18.528  -28.882 1.00 44.24  ? 493 ILE   B CD1  1 
ATOM   4136 N  N    . PHE   B 1 483 ? 20.101  15.309  -26.938 1.00 24.60  ? 494 PHE   B N    1 
ATOM   4137 C  CA   . PHE   B 1 483 ? 19.961  14.267  -25.911 1.00 25.06  ? 494 PHE   B CA   1 
ATOM   4138 C  C    . PHE   B 1 483 ? 20.194  14.844  -24.519 1.00 24.65  ? 494 PHE   B C    1 
ATOM   4139 O  O    . PHE   B 1 483 ? 19.427  14.576  -23.585 1.00 23.98  ? 494 PHE   B O    1 
ATOM   4140 C  CB   . PHE   B 1 483 ? 20.948  13.121  -26.209 1.00 21.41  ? 494 PHE   B CB   1 
ATOM   4141 C  CG   . PHE   B 1 483 ? 20.781  11.883  -25.346 1.00 21.76  ? 494 PHE   B CG   1 
ATOM   4142 C  CD1  . PHE   B 1 483 ? 19.634  11.662  -24.612 1.00 21.94  ? 494 PHE   B CD1  1 
ATOM   4143 C  CD2  . PHE   B 1 483 ? 21.805  10.939  -25.276 1.00 21.27  ? 494 PHE   B CD2  1 
ATOM   4144 C  CE1  . PHE   B 1 483 ? 19.500  10.513  -23.832 1.00 26.34  ? 494 PHE   B CE1  1 
ATOM   4145 C  CE2  . PHE   B 1 483 ? 21.684  9.795   -24.493 1.00 26.82  ? 494 PHE   B CE2  1 
ATOM   4146 C  CZ   . PHE   B 1 483 ? 20.526  9.582   -23.771 1.00 23.48  ? 494 PHE   B CZ   1 
ATOM   4147 N  N    . ARG   B 1 484 ? 21.251  15.650  -24.358 1.00 27.69  ? 495 ARG   B N    1 
ATOM   4148 C  CA   . ARG   B 1 484 ? 21.506  16.277  -23.062 1.00 26.39  ? 495 ARG   B CA   1 
ATOM   4149 C  C    . ARG   B 1 484 ? 20.331  17.148  -22.620 1.00 28.43  ? 495 ARG   B C    1 
ATOM   4150 O  O    . ARG   B 1 484 ? 19.984  17.179  -21.432 1.00 28.40  ? 495 ARG   B O    1 
ATOM   4151 C  CB   . ARG   B 1 484 ? 22.824  17.073  -23.098 1.00 30.15  ? 495 ARG   B CB   1 
ATOM   4152 C  CG   . ARG   B 1 484 ? 24.042  16.170  -22.859 1.00 40.44  ? 495 ARG   B CG   1 
ATOM   4153 C  CD   . ARG   B 1 484 ? 25.383  16.891  -22.679 1.00 41.94  ? 495 ARG   B CD   1 
ATOM   4154 N  NE   . ARG   B 1 484 ? 25.888  17.423  -23.939 1.00 44.60  ? 495 ARG   B NE   1 
ATOM   4155 C  CZ   . ARG   B 1 484 ? 25.664  18.640  -24.411 1.00 54.64  ? 495 ARG   B CZ   1 
ATOM   4156 N  NH1  . ARG   B 1 484 ? 24.922  19.514  -23.749 1.00 60.12  ? 495 ARG   B NH1  1 
ATOM   4157 N  NH2  . ARG   B 1 484 ? 26.208  18.992  -25.573 1.00 55.63  ? 495 ARG   B NH2  1 
ATOM   4158 N  N    . ASP   B 1 485 ? 19.691  17.844  -23.559 1.00 28.86  ? 496 ASP   B N    1 
ATOM   4159 C  CA   . ASP   B 1 485 ? 18.541  18.664  -23.185 1.00 29.61  ? 496 ASP   B CA   1 
ATOM   4160 C  C    . ASP   B 1 485 ? 17.382  17.797  -22.709 1.00 29.95  ? 496 ASP   B C    1 
ATOM   4161 O  O    . ASP   B 1 485 ? 16.722  18.120  -21.713 1.00 28.61  ? 496 ASP   B O    1 
ATOM   4162 C  CB   . ASP   B 1 485 ? 18.094  19.527  -24.358 1.00 25.88  ? 496 ASP   B CB   1 
ATOM   4163 C  CG   . ASP   B 1 485 ? 16.979  20.471  -23.975 1.00 38.48  ? 496 ASP   B CG   1 
ATOM   4164 O  OD1  . ASP   B 1 485 ? 17.283  21.540  -23.417 1.00 42.68  ? 496 ASP   B OD1  1 
ATOM   4165 O  OD2  . ASP   B 1 485 ? 15.800  20.130  -24.204 1.00 37.98  ? 496 ASP   B OD2  1 
ATOM   4166 N  N    . PHE   B 1 486 ? 17.117  16.700  -23.418 1.00 24.87  ? 497 PHE   B N    1 
ATOM   4167 C  CA   . PHE   B 1 486 ? 16.086  15.753  -22.996 1.00 31.03  ? 497 PHE   B CA   1 
ATOM   4168 C  C    . PHE   B 1 486 ? 16.345  15.252  -21.578 1.00 28.31  ? 497 PHE   B C    1 
ATOM   4169 O  O    . PHE   B 1 486 ? 15.443  15.251  -20.729 1.00 25.85  ? 497 PHE   B O    1 
ATOM   4170 C  CB   . PHE   B 1 486 ? 16.034  14.585  -23.990 1.00 27.58  ? 497 PHE   B CB   1 
ATOM   4171 C  CG   . PHE   B 1 486 ? 15.056  13.501  -23.612 1.00 26.68  ? 497 PHE   B CG   1 
ATOM   4172 C  CD1  . PHE   B 1 486 ? 13.716  13.610  -23.954 1.00 25.73  ? 497 PHE   B CD1  1 
ATOM   4173 C  CD2  . PHE   B 1 486 ? 15.484  12.366  -22.923 1.00 24.58  ? 497 PHE   B CD2  1 
ATOM   4174 C  CE1  . PHE   B 1 486 ? 12.798  12.597  -23.599 1.00 25.70  ? 497 PHE   B CE1  1 
ATOM   4175 C  CE2  . PHE   B 1 486 ? 14.577  11.346  -22.577 1.00 25.07  ? 497 PHE   B CE2  1 
ATOM   4176 C  CZ   . PHE   B 1 486 ? 13.245  11.469  -22.914 1.00 26.32  ? 497 PHE   B CZ   1 
ATOM   4177 N  N    . LEU   B 1 487 ? 17.587  14.847  -21.299 1.00 25.10  ? 498 LEU   B N    1 
ATOM   4178 C  CA   . LEU   B 1 487 ? 17.958  14.417  -19.953 1.00 24.20  ? 498 LEU   B CA   1 
ATOM   4179 C  C    . LEU   B 1 487 ? 17.707  15.525  -18.932 1.00 28.24  ? 498 LEU   B C    1 
ATOM   4180 O  O    . LEU   B 1 487 ? 17.186  15.272  -17.838 1.00 30.14  ? 498 LEU   B O    1 
ATOM   4181 C  CB   . LEU   B 1 487 ? 19.430  14.004  -19.933 1.00 26.28  ? 498 LEU   B CB   1 
ATOM   4182 C  CG   . LEU   B 1 487 ? 19.763  12.707  -20.677 1.00 27.17  ? 498 LEU   B CG   1 
ATOM   4183 C  CD1  . LEU   B 1 487 ? 21.251  12.411  -20.546 1.00 26.29  ? 498 LEU   B CD1  1 
ATOM   4184 C  CD2  . LEU   B 1 487 ? 18.925  11.534  -20.167 1.00 25.66  ? 498 LEU   B CD2  1 
ATOM   4185 N  N    . ASN   B 1 488 ? 18.112  16.758  -19.254 1.00 25.59  ? 499 ASN   B N    1 
ATOM   4186 C  CA   . ASN   B 1 488 ? 17.876  17.873  -18.334 1.00 24.89  ? 499 ASN   B CA   1 
ATOM   4187 C  C    . ASN   B 1 488 ? 16.391  18.045  -18.032 1.00 34.94  ? 499 ASN   B C    1 
ATOM   4188 O  O    . ASN   B 1 488 ? 16.017  18.369  -16.897 1.00 31.47  ? 499 ASN   B O    1 
ATOM   4189 C  CB   . ASN   B 1 488 ? 18.457  19.171  -18.897 1.00 33.51  ? 499 ASN   B CB   1 
ATOM   4190 C  CG   . ASN   B 1 488 ? 19.977  19.195  -18.850 1.00 38.77  ? 499 ASN   B CG   1 
ATOM   4191 O  OD1  . ASN   B 1 488 ? 20.595  18.534  -18.013 1.00 43.98  ? 499 ASN   B OD1  1 
ATOM   4192 N  ND2  . ASN   B 1 488 ? 20.585  19.931  -19.767 1.00 45.24  ? 499 ASN   B ND2  1 
ATOM   4193 N  N    . ARG   B 1 489 ? 15.530  17.851  -19.037 1.00 26.75  ? 500 ARG   B N    1 
ATOM   4194 C  CA   . ARG   B 1 489 ? 14.096  18.014  -18.811 1.00 33.60  ? 500 ARG   B CA   1 
ATOM   4195 C  C    . ARG   B 1 489 ? 13.517  16.891  -17.950 1.00 33.60  ? 500 ARG   B C    1 
ATOM   4196 O  O    . ARG   B 1 489 ? 12.591  17.135  -17.168 1.00 30.00  ? 500 ARG   B O    1 
ATOM   4197 C  CB   . ARG   B 1 489 ? 13.363  18.079  -20.149 1.00 30.52  ? 500 ARG   B CB   1 
ATOM   4198 C  CG   . ARG   B 1 489 ? 13.760  19.251  -21.008 1.00 35.98  ? 500 ARG   B CG   1 
ATOM   4199 C  CD   . ARG   B 1 489 ? 13.167  20.539  -20.474 1.00 38.96  ? 500 ARG   B CD   1 
ATOM   4200 N  NE   . ARG   B 1 489 ? 11.708  20.480  -20.431 1.00 55.57  ? 500 ARG   B NE   1 
ATOM   4201 C  CZ   . ARG   B 1 489 ? 10.976  20.544  -19.324 1.00 56.01  ? 500 ARG   B CZ   1 
ATOM   4202 N  NH1  . ARG   B 1 489 ? 11.532  20.705  -18.133 1.00 45.10  ? 500 ARG   B NH1  1 
ATOM   4203 N  NH2  . ARG   B 1 489 ? 9.652   20.445  -19.415 1.00 53.61  ? 500 ARG   B NH2  1 
ATOM   4204 N  N    . CYS   B 1 490 ? 14.055  15.667  -18.059 1.00 27.51  ? 501 CYS   B N    1 
ATOM   4205 C  CA   . CYS   B 1 490 ? 13.608  14.559  -17.210 1.00 22.56  ? 501 CYS   B CA   1 
ATOM   4206 C  C    . CYS   B 1 490 ? 14.135  14.682  -15.795 1.00 26.79  ? 501 CYS   B C    1 
ATOM   4207 O  O    . CYS   B 1 490 ? 13.472  14.244  -14.851 1.00 27.02  ? 501 CYS   B O    1 
ATOM   4208 C  CB   . CYS   B 1 490 ? 14.076  13.205  -17.771 1.00 22.18  ? 501 CYS   B CB   1 
ATOM   4209 S  SG   . CYS   B 1 490 ? 13.366  12.757  -19.345 1.00 26.33  ? 501 CYS   B SG   1 
ATOM   4210 N  N    . LEU   B 1 491 ? 15.331  15.243  -15.623 1.00 29.64  ? 502 LEU   B N    1 
ATOM   4211 C  CA   . LEU   B 1 491 ? 16.027  15.184  -14.346 1.00 31.80  ? 502 LEU   B CA   1 
ATOM   4212 C  C    . LEU   B 1 491 ? 16.025  16.527  -13.618 1.00 28.65  ? 502 LEU   B C    1 
ATOM   4213 O  O    . LEU   B 1 491 ? 16.972  16.846  -12.901 1.00 31.55  ? 502 LEU   B O    1 
ATOM   4214 C  CB   . LEU   B 1 491 ? 17.446  14.657  -14.550 1.00 29.45  ? 502 LEU   B CB   1 
ATOM   4215 C  CG   . LEU   B 1 491 ? 17.468  13.207  -15.067 1.00 25.63  ? 502 LEU   B CG   1 
ATOM   4216 C  CD1  . LEU   B 1 491 ? 18.846  12.812  -15.536 1.00 29.01  ? 502 LEU   B CD1  1 
ATOM   4217 C  CD2  . LEU   B 1 491 ? 16.979  12.200  -14.011 1.00 23.68  ? 502 LEU   B CD2  1 
ATOM   4218 N  N    . GLU   B 1 492 ? 14.990  17.337  -13.838 1.00 32.18  ? 503 GLU   B N    1 
ATOM   4219 C  CA   . GLU   B 1 492 ? 14.831  18.577  -13.090 1.00 39.93  ? 503 GLU   B CA   1 
ATOM   4220 C  C    . GLU   B 1 492 ? 14.503  18.248  -11.643 1.00 31.23  ? 503 GLU   B C    1 
ATOM   4221 O  O    . GLU   B 1 492 ? 13.614  17.437  -11.371 1.00 34.18  ? 503 GLU   B O    1 
ATOM   4222 C  CB   . GLU   B 1 492 ? 13.711  19.433  -13.685 1.00 38.96  ? 503 GLU   B CB   1 
ATOM   4223 C  CG   . GLU   B 1 492 ? 14.050  20.139  -14.984 1.00 49.15  ? 503 GLU   B CG   1 
ATOM   4224 C  CD   . GLU   B 1 492 ? 14.851  21.418  -14.784 1.00 58.08  ? 503 GLU   B CD   1 
ATOM   4225 O  OE1  . GLU   B 1 492 ? 15.105  21.795  -13.619 1.00 45.04  ? 503 GLU   B OE1  1 
ATOM   4226 O  OE2  . GLU   B 1 492 ? 15.217  22.051  -15.801 1.00 59.06  ? 503 GLU   B OE2  1 
ATOM   4227 N  N    . MET   B 1 493 ? 15.220  18.881  -10.710 1.00 34.89  ? 504 MET   B N    1 
ATOM   4228 C  CA   . MET   B 1 493 ? 14.923  18.673  -9.296  1.00 38.82  ? 504 MET   B CA   1 
ATOM   4229 C  C    . MET   B 1 493 ? 13.581  19.295  -8.929  1.00 41.54  ? 504 MET   B C    1 
ATOM   4230 O  O    . MET   B 1 493 ? 12.836  18.745  -8.109  1.00 42.99  ? 504 MET   B O    1 
ATOM   4231 C  CB   . MET   B 1 493 ? 16.044  19.245  -8.432  1.00 42.30  ? 504 MET   B CB   1 
ATOM   4232 C  CG   . MET   B 1 493 ? 15.898  18.944  -6.946  1.00 46.27  ? 504 MET   B CG   1 
ATOM   4233 S  SD   . MET   B 1 493 ? 17.165  17.800  -6.363  1.00 77.65  ? 504 MET   B SD   1 
ATOM   4234 C  CE   . MET   B 1 493 ? 18.624  18.500  -7.135  1.00 42.93  ? 504 MET   B CE   1 
ATOM   4235 N  N    . ASP   B 1 494 ? 13.257  20.438  -9.536  1.00 40.56  ? 505 ASP   B N    1 
ATOM   4236 C  CA   . ASP   B 1 494 ? 11.985  21.123  -9.319  1.00 40.90  ? 505 ASP   B CA   1 
ATOM   4237 C  C    . ASP   B 1 494 ? 10.874  20.324  -9.988  1.00 44.05  ? 505 ASP   B C    1 
ATOM   4238 O  O    . ASP   B 1 494 ? 10.810  20.247  -11.221 1.00 38.63  ? 505 ASP   B O    1 
ATOM   4239 C  CB   . ASP   B 1 494 ? 12.064  22.541  -9.878  1.00 42.82  ? 505 ASP   B CB   1 
ATOM   4240 C  CG   . ASP   B 1 494 ? 10.824  23.374  -9.582  1.00 47.69  ? 505 ASP   B CG   1 
ATOM   4241 O  OD1  . ASP   B 1 494 ? 9.703   22.824  -9.554  1.00 47.76  ? 505 ASP   B OD1  1 
ATOM   4242 O  OD2  . ASP   B 1 494 ? 10.973  24.598  -9.387  1.00 53.44  ? 505 ASP   B OD2  1 
ATOM   4243 N  N    . VAL   B 1 495 ? 10.000  19.726  -9.173  1.00 35.92  ? 506 VAL   B N    1 
ATOM   4244 C  CA   . VAL   B 1 495 ? 8.967   18.839  -9.704  1.00 38.53  ? 506 VAL   B CA   1 
ATOM   4245 C  C    . VAL   B 1 495 ? 8.077   19.583  -10.685 1.00 45.28  ? 506 VAL   B C    1 
ATOM   4246 O  O    . VAL   B 1 495 ? 7.695   19.043  -11.732 1.00 41.44  ? 506 VAL   B O    1 
ATOM   4247 C  CB   . VAL   B 1 495 ? 8.146   18.218  -8.558  1.00 42.32  ? 506 VAL   B CB   1 
ATOM   4248 C  CG1  . VAL   B 1 495 ? 6.987   17.377  -9.113  1.00 39.69  ? 506 VAL   B CG1  1 
ATOM   4249 C  CG2  . VAL   B 1 495 ? 9.034   17.366  -7.676  1.00 43.51  ? 506 VAL   B CG2  1 
ATOM   4250 N  N    . GLU   B 1 496 ? 7.761   20.846  -10.382 1.00 38.91  ? 507 GLU   B N    1 
ATOM   4251 C  CA   . GLU   B 1 496 ? 6.929   21.631  -11.284 1.00 41.50  ? 507 GLU   B CA   1 
ATOM   4252 C  C    . GLU   B 1 496 ? 7.617   21.865  -12.626 1.00 43.39  ? 507 GLU   B C    1 
ATOM   4253 O  O    . GLU   B 1 496 ? 6.953   21.908  -13.668 1.00 46.57  ? 507 GLU   B O    1 
ATOM   4254 C  CB   . GLU   B 1 496 ? 6.559   22.960  -10.624 1.00 52.38  ? 507 GLU   B CB   1 
ATOM   4255 C  CG   . GLU   B 1 496 ? 5.416   23.661  -11.313 1.00 57.60  ? 507 GLU   B CG   1 
ATOM   4256 C  CD   . GLU   B 1 496 ? 4.096   22.932  -11.079 1.00 80.94  ? 507 GLU   B CD   1 
ATOM   4257 O  OE1  . GLU   B 1 496 ? 4.067   21.991  -10.251 1.00 75.30  ? 507 GLU   B OE1  1 
ATOM   4258 O  OE2  . GLU   B 1 496 ? 3.087   23.298  -11.719 1.00 92.65  ? 507 GLU   B OE2  1 
ATOM   4259 N  N    . LYS   B 1 497 ? 8.942   22.010  -12.621 1.00 39.06  ? 508 LYS   B N    1 
ATOM   4260 C  CA   . LYS   B 1 497 ? 9.681   22.274  -13.852 1.00 39.46  ? 508 LYS   B CA   1 
ATOM   4261 C  C    . LYS   B 1 497 ? 9.928   21.009  -14.663 1.00 40.01  ? 508 LYS   B C    1 
ATOM   4262 O  O    . LYS   B 1 497 ? 10.074  21.082  -15.891 1.00 38.32  ? 508 LYS   B O    1 
ATOM   4263 C  CB   . LYS   B 1 497 ? 11.014  22.931  -13.505 1.00 51.10  ? 508 LYS   B CB   1 
ATOM   4264 C  CG   . LYS   B 1 497 ? 11.719  23.632  -14.647 1.00 63.20  ? 508 LYS   B CG   1 
ATOM   4265 C  CD   . LYS   B 1 497 ? 12.635  24.721  -14.089 1.00 65.19  ? 508 LYS   B CD   1 
ATOM   4266 C  CE   . LYS   B 1 497 ? 13.402  25.452  -15.181 1.00 75.51  ? 508 LYS   B CE   1 
ATOM   4267 N  NZ   . LYS   B 1 497 ? 14.541  24.638  -15.683 1.00 68.99  ? 508 LYS   B NZ   1 
ATOM   4268 N  N    . ARG   B 1 498 ? 9.974   19.854  -14.002 1.00 37.42  ? 509 ARG   B N    1 
ATOM   4269 C  CA   . ARG   B 1 498 ? 10.219  18.595  -14.695 1.00 32.29  ? 509 ARG   B CA   1 
ATOM   4270 C  C    . ARG   B 1 498 ? 9.112   18.338  -15.704 1.00 30.35  ? 509 ARG   B C    1 
ATOM   4271 O  O    . ARG   B 1 498 ? 7.946   18.661  -15.463 1.00 33.64  ? 509 ARG   B O    1 
ATOM   4272 C  CB   . ARG   B 1 498 ? 10.293  17.445  -13.686 1.00 28.47  ? 509 ARG   B CB   1 
ATOM   4273 C  CG   . ARG   B 1 498 ? 10.860  16.130  -14.216 1.00 27.37  ? 509 ARG   B CG   1 
ATOM   4274 C  CD   . ARG   B 1 498 ? 10.847  15.073  -13.114 1.00 33.42  ? 509 ARG   B CD   1 
ATOM   4275 N  NE   . ARG   B 1 498 ? 11.570  15.518  -11.928 1.00 30.97  ? 509 ARG   B NE   1 
ATOM   4276 C  CZ   . ARG   B 1 498 ? 11.338  15.084  -10.695 1.00 30.46  ? 509 ARG   B CZ   1 
ATOM   4277 N  NH1  . ARG   B 1 498 ? 10.436  14.145  -10.448 1.00 25.73  ? 509 ARG   B NH1  1 
ATOM   4278 N  NH2  . ARG   B 1 498 ? 12.015  15.618  -9.683  1.00 29.58  ? 509 ARG   B NH2  1 
ATOM   4279 N  N    . GLY   B 1 499 ? 9.483   17.763  -16.847 1.00 29.30  ? 510 GLY   B N    1 
ATOM   4280 C  CA   . GLY   B 1 499 ? 8.507   17.518  -17.886 1.00 31.14  ? 510 GLY   B CA   1 
ATOM   4281 C  C    . GLY   B 1 499 ? 7.495   16.463  -17.484 1.00 30.79  ? 510 GLY   B C    1 
ATOM   4282 O  O    . GLY   B 1 499 ? 7.791   15.517  -16.751 1.00 28.25  ? 510 GLY   B O    1 
ATOM   4283 N  N    . SER   B 1 500 ? 6.272   16.642  -17.967 1.00 30.33  ? 511 SER   B N    1 
ATOM   4284 C  CA   . SER   B 1 500 ? 5.299   15.568  -17.914 1.00 29.33  ? 511 SER   B CA   1 
ATOM   4285 C  C    . SER   B 1 500 ? 5.547   14.596  -19.064 1.00 34.31  ? 511 SER   B C    1 
ATOM   4286 O  O    . SER   B 1 500 ? 6.293   14.886  -20.005 1.00 27.35  ? 511 SER   B O    1 
ATOM   4287 C  CB   . SER   B 1 500 ? 3.885   16.119  -18.004 1.00 34.48  ? 511 SER   B CB   1 
ATOM   4288 O  OG   . SER   B 1 500 ? 3.647   16.609  -19.310 1.00 34.71  ? 511 SER   B OG   1 
ATOM   4289 N  N    . ALA   B 1 501 ? 4.915   13.422  -18.985 1.00 30.16  ? 512 ALA   B N    1 
ATOM   4290 C  CA   . ALA   B 1 501 ? 5.022   12.481  -20.096 1.00 30.73  ? 512 ALA   B CA   1 
ATOM   4291 C  C    . ALA   B 1 501 ? 4.439   13.081  -21.367 1.00 25.98  ? 512 ALA   B C    1 
ATOM   4292 O  O    . ALA   B 1 501 ? 5.026   12.966  -22.449 1.00 30.67  ? 512 ALA   B O    1 
ATOM   4293 C  CB   . ALA   B 1 501 ? 4.316   11.167  -19.753 1.00 33.16  ? 512 ALA   B CB   1 
ATOM   4294 N  N    . LYS   B 1 502 ? 3.278   13.718  -21.253 1.00 28.52  ? 513 LYS   B N    1 
ATOM   4295 C  CA   . LYS   B 1 502 ? 2.658   14.340  -22.417 1.00 32.17  ? 513 LYS   B CA   1 
ATOM   4296 C  C    . LYS   B 1 502 ? 3.572   15.396  -23.031 1.00 34.17  ? 513 LYS   B C    1 
ATOM   4297 O  O    . LYS   B 1 502 ? 3.697   15.486  -24.261 1.00 35.13  ? 513 LYS   B O    1 
ATOM   4298 C  CB   . LYS   B 1 502 ? 1.314   14.950  -22.008 1.00 36.12  ? 513 LYS   B CB   1 
ATOM   4299 C  CG   . LYS   B 1 502 ? 0.516   15.567  -23.145 1.00 47.69  ? 513 LYS   B CG   1 
ATOM   4300 C  CD   . LYS   B 1 502 ? -0.827  16.115  -22.647 1.00 54.65  ? 513 LYS   B CD   1 
ATOM   4301 C  CE   . LYS   B 1 502 ? -1.593  16.804  -23.770 1.00 55.28  ? 513 LYS   B CE   1 
ATOM   4302 N  NZ   . LYS   B 1 502 ? -2.843  17.460  -23.275 1.00 78.02  ? 513 LYS   B NZ   1 
ATOM   4303 N  N    . GLU   B 1 503 ? 4.225   16.204  -22.192 1.00 33.86  ? 514 GLU   B N    1 
ATOM   4304 C  CA   . GLU   B 1 503 ? 5.121   17.237  -22.707 1.00 30.75  ? 514 GLU   B CA   1 
ATOM   4305 C  C    . GLU   B 1 503 ? 6.347   16.616  -23.358 1.00 31.41  ? 514 GLU   B C    1 
ATOM   4306 O  O    . GLU   B 1 503 ? 6.754   17.025  -24.451 1.00 31.05  ? 514 GLU   B O    1 
ATOM   4307 C  CB   . GLU   B 1 503 ? 5.533   18.187  -21.582 1.00 34.17  ? 514 GLU   B CB   1 
ATOM   4308 C  CG   . GLU   B 1 503 ? 4.436   19.174  -21.159 1.00 41.31  ? 514 GLU   B CG   1 
ATOM   4309 C  CD   . GLU   B 1 503 ? 4.743   19.886  -19.842 1.00 38.05  ? 514 GLU   B CD   1 
ATOM   4310 O  OE1  . GLU   B 1 503 ? 5.730   19.531  -19.169 1.00 40.50  ? 514 GLU   B OE1  1 
ATOM   4311 O  OE2  . GLU   B 1 503 ? 4.000   20.815  -19.482 1.00 49.21  ? 514 GLU   B OE2  1 
ATOM   4312 N  N    . LEU   B 1 504 ? 6.944   15.615  -22.708 1.00 26.27  ? 515 LEU   B N    1 
ATOM   4313 C  CA   . LEU   B 1 504 ? 8.174   15.035  -23.240 1.00 25.11  ? 515 LEU   B CA   1 
ATOM   4314 C  C    . LEU   B 1 504 ? 7.946   14.256  -24.525 1.00 29.48  ? 515 LEU   B C    1 
ATOM   4315 O  O    . LEU   B 1 504 ? 8.883   14.106  -25.315 1.00 27.28  ? 515 LEU   B O    1 
ATOM   4316 C  CB   . LEU   B 1 504 ? 8.829   14.148  -22.188 1.00 25.80  ? 515 LEU   B CB   1 
ATOM   4317 C  CG   . LEU   B 1 504 ? 9.457   15.001  -21.085 1.00 33.41  ? 515 LEU   B CG   1 
ATOM   4318 C  CD1  . LEU   B 1 504 ? 9.865   14.153  -19.910 1.00 32.08  ? 515 LEU   B CD1  1 
ATOM   4319 C  CD2  . LEU   B 1 504 ? 10.665  15.711  -21.638 1.00 34.05  ? 515 LEU   B CD2  1 
ATOM   4320 N  N    . LEU   B 1 505 ? 6.725   13.782  -24.771 1.00 29.19  ? 516 LEU   B N    1 
ATOM   4321 C  CA   . LEU   B 1 505 ? 6.446   13.117  -26.038 1.00 31.53  ? 516 LEU   B CA   1 
ATOM   4322 C  C    . LEU   B 1 505 ? 6.586   14.064  -27.221 1.00 28.79  ? 516 LEU   B C    1 
ATOM   4323 O  O    . LEU   B 1 505 ? 6.717   13.596  -28.353 1.00 29.36  ? 516 LEU   B O    1 
ATOM   4324 C  CB   . LEU   B 1 505 ? 5.044   12.500  -26.027 1.00 31.02  ? 516 LEU   B CB   1 
ATOM   4325 C  CG   . LEU   B 1 505 ? 4.900   11.167  -25.285 1.00 31.45  ? 516 LEU   B CG   1 
ATOM   4326 C  CD1  . LEU   B 1 505 ? 3.442   10.863  -25.021 1.00 33.44  ? 516 LEU   B CD1  1 
ATOM   4327 C  CD2  . LEU   B 1 505 ? 5.548   10.036  -26.076 1.00 30.41  ? 516 LEU   B CD2  1 
ATOM   4328 N  N    . GLN   B 1 506 ? 6.604   15.374  -26.980 1.00 29.76  ? 517 GLN   B N    1 
ATOM   4329 C  CA   . GLN   B 1 506 ? 6.848   16.366  -28.024 1.00 31.39  ? 517 GLN   B CA   1 
ATOM   4330 C  C    . GLN   B 1 506 ? 8.318   16.758  -28.162 1.00 29.80  ? 517 GLN   B C    1 
ATOM   4331 O  O    . GLN   B 1 506 ? 8.650   17.550  -29.051 1.00 30.87  ? 517 GLN   B O    1 
ATOM   4332 C  CB   . GLN   B 1 506 ? 6.027   17.628  -27.746 1.00 33.68  ? 517 GLN   B CB   1 
ATOM   4333 C  CG   . GLN   B 1 506 ? 4.536   17.407  -27.649 1.00 42.93  ? 517 GLN   B CG   1 
ATOM   4334 C  CD   . GLN   B 1 506 ? 3.976   16.693  -28.858 1.00 52.51  ? 517 GLN   B CD   1 
ATOM   4335 O  OE1  . GLN   B 1 506 ? 4.320   17.012  -29.995 1.00 53.93  ? 517 GLN   B OE1  1 
ATOM   4336 N  NE2  . GLN   B 1 506 ? 3.093   15.731  -28.619 1.00 55.82  ? 517 GLN   B NE2  1 
ATOM   4337 N  N    . HIS   B 1 507 ? 9.211   16.222  -27.337 1.00 28.63  ? 518 HIS   B N    1 
ATOM   4338 C  CA   . HIS   B 1 507 ? 10.595  16.690  -27.333 1.00 29.14  ? 518 HIS   B CA   1 
ATOM   4339 C  C    . HIS   B 1 507 ? 11.320  16.296  -28.622 1.00 27.06  ? 518 HIS   B C    1 
ATOM   4340 O  O    . HIS   B 1 507 ? 11.101  15.211  -29.161 1.00 26.85  ? 518 HIS   B O    1 
ATOM   4341 C  CB   . HIS   B 1 507 ? 11.326  16.123  -26.120 1.00 26.91  ? 518 HIS   B CB   1 
ATOM   4342 C  CG   . HIS   B 1 507 ? 12.622  16.807  -25.827 1.00 30.81  ? 518 HIS   B CG   1 
ATOM   4343 N  ND1  . HIS   B 1 507 ? 13.785  16.525  -26.510 1.00 27.42  ? 518 HIS   B ND1  1 
ATOM   4344 C  CD2  . HIS   B 1 507 ? 12.937  17.768  -24.928 1.00 25.99  ? 518 HIS   B CD2  1 
ATOM   4345 C  CE1  . HIS   B 1 507 ? 14.764  17.276  -26.035 1.00 31.99  ? 518 HIS   B CE1  1 
ATOM   4346 N  NE2  . HIS   B 1 507 ? 14.273  18.043  -25.076 1.00 31.81  ? 518 HIS   B NE2  1 
ATOM   4347 N  N    . GLN   B 1 508 ? 12.179  17.201  -29.125 1.00 25.72  ? 519 GLN   B N    1 
ATOM   4348 C  CA   . GLN   B 1 508 ? 12.867  16.956  -30.396 1.00 27.57  ? 519 GLN   B CA   1 
ATOM   4349 C  C    . GLN   B 1 508 ? 13.733  15.703  -30.356 1.00 26.77  ? 519 GLN   B C    1 
ATOM   4350 O  O    . GLN   B 1 508 ? 13.926  15.053  -31.391 1.00 26.00  ? 519 GLN   B O    1 
ATOM   4351 C  CB   . GLN   B 1 508 ? 13.727  18.170  -30.778 1.00 27.17  ? 519 GLN   B CB   1 
ATOM   4352 C  CG   . GLN   B 1 508 ? 12.878  19.418  -31.007 1.00 31.49  ? 519 GLN   B CG   1 
ATOM   4353 C  CD   . GLN   B 1 508 ? 12.024  19.309  -32.249 1.00 40.14  ? 519 GLN   B CD   1 
ATOM   4354 O  OE1  . GLN   B 1 508 ? 10.816  19.099  -32.155 1.00 39.12  ? 519 GLN   B OE1  1 
ATOM   4355 N  NE2  . GLN   B 1 508 ? 12.623  19.555  -33.416 1.00 31.38  ? 519 GLN   B NE2  1 
ATOM   4356 N  N    . PHE   B 1 509 ? 14.291  15.366  -29.193 1.00 24.38  ? 520 PHE   B N    1 
ATOM   4357 C  CA   . PHE   B 1 509 ? 15.168  14.198  -29.119 1.00 25.43  ? 520 PHE   B CA   1 
ATOM   4358 C  C    . PHE   B 1 509 ? 14.460  12.943  -29.607 1.00 24.04  ? 520 PHE   B C    1 
ATOM   4359 O  O    . PHE   B 1 509 ? 15.078  12.076  -30.238 1.00 25.19  ? 520 PHE   B O    1 
ATOM   4360 C  CB   . PHE   B 1 509 ? 15.678  13.992  -27.694 1.00 24.00  ? 520 PHE   B CB   1 
ATOM   4361 C  CG   . PHE   B 1 509 ? 16.423  12.695  -27.495 1.00 24.60  ? 520 PHE   B CG   1 
ATOM   4362 C  CD1  . PHE   B 1 509 ? 17.613  12.444  -28.173 1.00 23.65  ? 520 PHE   B CD1  1 
ATOM   4363 C  CD2  . PHE   B 1 509 ? 15.943  11.733  -26.614 1.00 24.15  ? 520 PHE   B CD2  1 
ATOM   4364 C  CE1  . PHE   B 1 509 ? 18.313  11.240  -27.975 1.00 20.97  ? 520 PHE   B CE1  1 
ATOM   4365 C  CE2  . PHE   B 1 509 ? 16.627  10.533  -26.408 1.00 21.64  ? 520 PHE   B CE2  1 
ATOM   4366 C  CZ   . PHE   B 1 509 ? 17.807  10.281  -27.084 1.00 24.62  ? 520 PHE   B CZ   1 
ATOM   4367 N  N    . LEU   B 1 510 ? 13.164  12.823  -29.328 1.00 26.27  ? 521 LEU   B N    1 
ATOM   4368 C  CA   . LEU   B 1 510 ? 12.453  11.635  -29.757 1.00 26.99  ? 521 LEU   B CA   1 
ATOM   4369 C  C    . LEU   B 1 510 ? 12.352  11.551  -31.276 1.00 30.82  ? 521 LEU   B C    1 
ATOM   4370 O  O    . LEU   B 1 510 ? 12.174  10.456  -31.814 1.00 27.43  ? 521 LEU   B O    1 
ATOM   4371 C  CB   . LEU   B 1 510 ? 11.060  11.614  -29.124 1.00 31.71  ? 521 LEU   B CB   1 
ATOM   4372 C  CG   . LEU   B 1 510 ? 11.014  11.646  -27.595 1.00 25.33  ? 521 LEU   B CG   1 
ATOM   4373 C  CD1  . LEU   B 1 510 ? 9.572   11.477  -27.106 1.00 26.99  ? 521 LEU   B CD1  1 
ATOM   4374 C  CD2  . LEU   B 1 510 ? 11.914  10.559  -27.022 1.00 24.05  ? 521 LEU   B CD2  1 
ATOM   4375 N  N    . LYS   B 1 511 ? 12.499  12.672  -31.979 1.00 27.99  ? 522 LYS   B N    1 
ATOM   4376 C  CA   . LYS   B 1 511 ? 12.345  12.662  -33.423 1.00 30.21  ? 522 LYS   B CA   1 
ATOM   4377 C  C    . LYS   B 1 511 ? 13.552  12.074  -34.152 1.00 29.55  ? 522 LYS   B C    1 
ATOM   4378 O  O    . LYS   B 1 511 ? 13.472  11.880  -35.370 1.00 33.93  ? 522 LYS   B O    1 
ATOM   4379 C  CB   . LYS   B 1 511 ? 12.026  14.075  -33.914 1.00 35.43  ? 522 LYS   B CB   1 
ATOM   4380 C  CG   . LYS   B 1 511 ? 10.743  14.619  -33.285 1.00 30.96  ? 522 LYS   B CG   1 
ATOM   4381 C  CD   . LYS   B 1 511 ? 10.359  15.984  -33.808 1.00 29.90  ? 522 LYS   B CD   1 
ATOM   4382 C  CE   . LYS   B 1 511 ? 9.137   16.513  -33.062 1.00 37.70  ? 522 LYS   B CE   1 
ATOM   4383 N  NZ   . LYS   B 1 511 ? 8.680   17.805  -33.643 1.00 61.64  ? 522 LYS   B NZ   1 
ATOM   4384 N  N    . ILE   B 1 512 ? 14.656  11.787  -33.459 1.00 23.42  ? 523 ILE   B N    1 
ATOM   4385 C  CA   . ILE   B 1 512 ? 15.760  11.072  -34.099 1.00 28.49  ? 523 ILE   B CA   1 
ATOM   4386 C  C    . ILE   B 1 512 ? 15.597  9.571   -33.907 1.00 30.73  ? 523 ILE   B C    1 
ATOM   4387 O  O    . ILE   B 1 512 ? 16.491  8.796   -34.269 1.00 27.79  ? 523 ILE   B O    1 
ATOM   4388 C  CB   . ILE   B 1 512 ? 17.142  11.501  -33.569 1.00 25.29  ? 523 ILE   B CB   1 
ATOM   4389 C  CG1  . ILE   B 1 512 ? 17.369  10.992  -32.140 1.00 26.57  ? 523 ILE   B CG1  1 
ATOM   4390 C  CG2  . ILE   B 1 512 ? 17.335  12.997  -33.676 1.00 29.94  ? 523 ILE   B CG2  1 
ATOM   4391 C  CD1  . ILE   B 1 512 ? 18.793  11.157  -31.670 1.00 28.83  ? 523 ILE   B CD1  1 
ATOM   4392 N  N    . ALA   B 1 513 ? 14.465  9.145   -33.341 1.00 26.82  ? 524 ALA   B N    1 
ATOM   4393 C  CA   . ALA   B 1 513 ? 14.265  7.724   -33.078 1.00 24.08  ? 524 ALA   B CA   1 
ATOM   4394 C  C    . ALA   B 1 513 ? 14.394  6.909   -34.355 1.00 26.20  ? 524 ALA   B C    1 
ATOM   4395 O  O    . ALA   B 1 513 ? 13.833  7.265   -35.395 1.00 27.76  ? 524 ALA   B O    1 
ATOM   4396 C  CB   . ALA   B 1 513 ? 12.884  7.479   -32.473 1.00 23.81  ? 524 ALA   B CB   1 
ATOM   4397 N  N    . LYS   B 1 514 ? 15.145  5.824   -34.275 1.00 23.30  ? 525 LYS   B N    1 
ATOM   4398 C  CA   . LYS   B 1 514 ? 15.177  4.831   -35.342 1.00 25.33  ? 525 LYS   B CA   1 
ATOM   4399 C  C    . LYS   B 1 514 ? 13.928  3.957   -35.277 1.00 26.75  ? 525 LYS   B C    1 
ATOM   4400 O  O    . LYS   B 1 514 ? 13.268  3.882   -34.237 1.00 27.37  ? 525 LYS   B O    1 
ATOM   4401 C  CB   . LYS   B 1 514 ? 16.426  3.956   -35.209 1.00 24.83  ? 525 LYS   B CB   1 
ATOM   4402 C  CG   . LYS   B 1 514 ? 17.739  4.638   -35.583 1.00 33.61  ? 525 LYS   B CG   1 
ATOM   4403 C  CD   . LYS   B 1 514 ? 18.891  3.637   -35.488 1.00 30.78  ? 525 LYS   B CD   1 
ATOM   4404 C  CE   . LYS   B 1 514 ? 20.192  4.212   -36.005 1.00 32.13  ? 525 LYS   B CE   1 
ATOM   4405 N  NZ   . LYS   B 1 514 ? 21.272  3.176   -35.928 1.00 41.45  ? 525 LYS   B NZ   1 
ATOM   4406 N  N    . PRO   B 1 515 ? 13.586  3.263   -36.365 1.00 28.82  ? 526 PRO   B N    1 
ATOM   4407 C  CA   . PRO   B 1 515 ? 12.456  2.329   -36.300 1.00 28.75  ? 526 PRO   B CA   1 
ATOM   4408 C  C    . PRO   B 1 515 ? 12.730  1.238   -35.282 1.00 26.23  ? 526 PRO   B C    1 
ATOM   4409 O  O    . PRO   B 1 515 ? 13.881  0.892   -35.003 1.00 24.93  ? 526 PRO   B O    1 
ATOM   4410 C  CB   . PRO   B 1 515 ? 12.381  1.750   -37.716 1.00 35.01  ? 526 PRO   B CB   1 
ATOM   4411 C  CG   . PRO   B 1 515 ? 13.173  2.699   -38.563 1.00 36.37  ? 526 PRO   B CG   1 
ATOM   4412 C  CD   . PRO   B 1 515 ? 14.235  3.244   -37.688 1.00 34.43  ? 526 PRO   B CD   1 
ATOM   4413 N  N    . LEU   B 1 516 ? 11.655  0.694   -34.712 1.00 27.81  ? 527 LEU   B N    1 
ATOM   4414 C  CA   . LEU   B 1 516 ? 11.848  -0.292  -33.655 1.00 29.70  ? 527 LEU   B CA   1 
ATOM   4415 C  C    . LEU   B 1 516 ? 12.550  -1.540  -34.168 1.00 28.09  ? 527 LEU   B C    1 
ATOM   4416 O  O    . LEU   B 1 516 ? 13.194  -2.241  -33.379 1.00 27.01  ? 527 LEU   B O    1 
ATOM   4417 C  CB   . LEU   B 1 516 ? 10.512  -0.656  -33.014 1.00 31.21  ? 527 LEU   B CB   1 
ATOM   4418 C  CG   . LEU   B 1 516 ? 9.883   0.513   -32.240 1.00 29.91  ? 527 LEU   B CG   1 
ATOM   4419 C  CD1  . LEU   B 1 516 ? 8.499   0.137   -31.748 1.00 31.54  ? 527 LEU   B CD1  1 
ATOM   4420 C  CD2  . LEU   B 1 516 ? 10.767  0.948   -31.084 1.00 27.87  ? 527 LEU   B CD2  1 
ATOM   4421 N  N    . SER   B 1 517 ? 12.482  -1.803  -35.479 1.00 29.62  ? 528 SER   B N    1 
ATOM   4422 C  CA   . SER   B 1 517 ? 13.230  -2.920  -36.048 1.00 28.77  ? 528 SER   B CA   1 
ATOM   4423 C  C    . SER   B 1 517 ? 14.724  -2.784  -35.777 1.00 30.11  ? 528 SER   B C    1 
ATOM   4424 O  O    . SER   B 1 517 ? 15.438  -3.795  -35.730 1.00 28.40  ? 528 SER   B O    1 
ATOM   4425 C  CB   . SER   B 1 517 ? 12.980  -3.017  -37.555 1.00 32.37  ? 528 SER   B CB   1 
ATOM   4426 O  OG   . SER   B 1 517 ? 13.432  -1.843  -38.211 1.00 32.15  ? 528 SER   B OG   1 
ATOM   4427 N  N    . SER   B 1 518 ? 15.209  -1.546  -35.601 1.00 25.83  ? 529 SER   B N    1 
ATOM   4428 C  CA   . SER   B 1 518 ? 16.605  -1.308  -35.258 1.00 25.08  ? 529 SER   B CA   1 
ATOM   4429 C  C    . SER   B 1 518 ? 16.978  -1.917  -33.917 1.00 25.32  ? 529 SER   B C    1 
ATOM   4430 O  O    . SER   B 1 518 ? 18.170  -2.052  -33.622 1.00 25.20  ? 529 SER   B O    1 
ATOM   4431 C  CB   . SER   B 1 518 ? 16.930  0.190   -35.227 1.00 29.92  ? 529 SER   B CB   1 
ATOM   4432 O  OG   . SER   B 1 518 ? 16.366  0.799   -34.067 1.00 32.67  ? 529 SER   B OG   1 
ATOM   4433 N  N    . LEU   B 1 519 ? 16.002  -2.282  -33.089 1.00 26.37  ? 530 LEU   B N    1 
ATOM   4434 C  CA   . LEU   B 1 519 ? 16.359  -2.918  -31.834 1.00 22.51  ? 530 LEU   B CA   1 
ATOM   4435 C  C    . LEU   B 1 519 ? 16.618  -4.413  -31.972 1.00 26.87  ? 530 LEU   B C    1 
ATOM   4436 O  O    . LEU   B 1 519 ? 17.246  -4.993  -31.081 1.00 26.08  ? 530 LEU   B O    1 
ATOM   4437 C  CB   . LEU   B 1 519 ? 15.256  -2.701  -30.786 1.00 22.38  ? 530 LEU   B CB   1 
ATOM   4438 C  CG   . LEU   B 1 519 ? 14.909  -1.249  -30.455 1.00 25.16  ? 530 LEU   B CG   1 
ATOM   4439 C  CD1  . LEU   B 1 519 ? 13.856  -1.194  -29.316 1.00 24.44  ? 530 LEU   B CD1  1 
ATOM   4440 C  CD2  . LEU   B 1 519 ? 16.163  -0.440  -30.100 1.00 25.43  ? 530 LEU   B CD2  1 
ATOM   4441 N  N    . THR   B 1 520 ? 16.162  -5.059  -33.059 1.00 26.31  ? 531 THR   B N    1 
ATOM   4442 C  CA   . THR   B 1 520 ? 16.273  -6.517  -33.066 1.00 25.61  ? 531 THR   B CA   1 
ATOM   4443 C  C    . THR   B 1 520 ? 17.725  -6.989  -33.179 1.00 26.23  ? 531 THR   B C    1 
ATOM   4444 O  O    . THR   B 1 520 ? 18.057  -8.047  -32.621 1.00 25.78  ? 531 THR   B O    1 
ATOM   4445 C  CB   . THR   B 1 520 ? 15.406  -7.169  -34.163 1.00 28.61  ? 531 THR   B CB   1 
ATOM   4446 O  OG1  . THR   B 1 520 ? 15.936  -6.921  -35.473 1.00 26.76  ? 531 THR   B OG1  1 
ATOM   4447 C  CG2  . THR   B 1 520 ? 13.971  -6.651  -34.096 1.00 28.66  ? 531 THR   B CG2  1 
ATOM   4448 N  N    . PRO   B 1 521 ? 18.630  -6.261  -33.845 1.00 25.33  ? 532 PRO   B N    1 
ATOM   4449 C  CA   . PRO   B 1 521 ? 20.036  -6.677  -33.765 1.00 24.09  ? 532 PRO   B CA   1 
ATOM   4450 C  C    . PRO   B 1 521 ? 20.581  -6.573  -32.357 1.00 24.18  ? 532 PRO   B C    1 
ATOM   4451 O  O    . PRO   B 1 521 ? 21.403  -7.409  -31.960 1.00 24.13  ? 532 PRO   B O    1 
ATOM   4452 C  CB   . PRO   B 1 521 ? 20.748  -5.724  -34.741 1.00 24.83  ? 532 PRO   B CB   1 
ATOM   4453 C  CG   . PRO   B 1 521 ? 19.701  -5.352  -35.718 1.00 28.46  ? 532 PRO   B CG   1 
ATOM   4454 C  CD   . PRO   B 1 521 ? 18.462  -5.195  -34.854 1.00 24.14  ? 532 PRO   B CD   1 
ATOM   4455 N  N    . LEU   B 1 522 ? 20.103  -5.604  -31.563 1.00 19.69  ? 533 LEU   B N    1 
ATOM   4456 C  CA   . LEU   B 1 522 ? 20.549  -5.517  -30.177 1.00 21.38  ? 533 LEU   B CA   1 
ATOM   4457 C  C    . LEU   B 1 522 ? 20.123  -6.745  -29.397 1.00 22.76  ? 533 LEU   B C    1 
ATOM   4458 O  O    . LEU   B 1 522 ? 20.909  -7.297  -28.622 1.00 22.96  ? 533 LEU   B O    1 
ATOM   4459 C  CB   . LEU   B 1 522 ? 20.012  -4.249  -29.510 1.00 23.16  ? 533 LEU   B CB   1 
ATOM   4460 C  CG   . LEU   B 1 522 ? 20.450  -2.926  -30.157 1.00 28.36  ? 533 LEU   B CG   1 
ATOM   4461 C  CD1  . LEU   B 1 522 ? 19.838  -1.754  -29.378 1.00 24.67  ? 533 LEU   B CD1  1 
ATOM   4462 C  CD2  . LEU   B 1 522 ? 21.975  -2.814  -30.237 1.00 25.58  ? 533 LEU   B CD2  1 
ATOM   4463 N  N    . ILE   B 1 523 ? 18.887  -7.201  -29.615 1.00 23.85  ? 534 ILE   B N    1 
ATOM   4464 C  CA   . ILE   B 1 523 ? 18.406  -8.422  -28.980 1.00 23.97  ? 534 ILE   B CA   1 
ATOM   4465 C  C    . ILE   B 1 523 ? 19.268  -9.612  -29.381 1.00 24.56  ? 534 ILE   B C    1 
ATOM   4466 O  O    . ILE   B 1 523 ? 19.632  -10.451 -28.546 1.00 26.22  ? 534 ILE   B O    1 
ATOM   4467 C  CB   . ILE   B 1 523 ? 16.929  -8.647  -29.350 1.00 28.79  ? 534 ILE   B CB   1 
ATOM   4468 C  CG1  . ILE   B 1 523 ? 16.068  -7.517  -28.768 1.00 26.41  ? 534 ILE   B CG1  1 
ATOM   4469 C  CG2  . ILE   B 1 523 ? 16.468  -10.024 -28.860 1.00 33.13  ? 534 ILE   B CG2  1 
ATOM   4470 C  CD1  . ILE   B 1 523 ? 14.720  -7.411  -29.413 1.00 30.67  ? 534 ILE   B CD1  1 
ATOM   4471 N  N    . ALA   B 1 524 ? 19.615  -9.699  -30.662 1.00 27.46  ? 535 ALA   B N    1 
ATOM   4472 C  CA   . ALA   B 1 524 ? 20.429  -10.813 -31.128 1.00 26.94  ? 535 ALA   B CA   1 
ATOM   4473 C  C    . ALA   B 1 524 ? 21.784  -10.827 -30.434 1.00 27.05  ? 535 ALA   B C    1 
ATOM   4474 O  O    . ALA   B 1 524 ? 22.281  -11.894 -30.043 1.00 28.87  ? 535 ALA   B O    1 
ATOM   4475 C  CB   . ALA   B 1 524 ? 20.602  -10.728 -32.643 1.00 30.75  ? 535 ALA   B CB   1 
ATOM   4476 N  N    . ALA   B 1 525 ? 22.391  -9.646  -30.270 1.00 23.62  ? 536 ALA   B N    1 
ATOM   4477 C  CA   . ALA   B 1 525 ? 23.675  -9.540  -29.583 1.00 26.99  ? 536 ALA   B CA   1 
ATOM   4478 C  C    . ALA   B 1 525 ? 23.548  -9.957  -28.121 1.00 25.45  ? 536 ALA   B C    1 
ATOM   4479 O  O    . ALA   B 1 525 ? 24.364  -10.733 -27.607 1.00 29.52  ? 536 ALA   B O    1 
ATOM   4480 C  CB   . ALA   B 1 525 ? 24.194  -8.096  -29.675 1.00 22.54  ? 536 ALA   B CB   1 
ATOM   4481 N  N    . ALA   B 1 526 ? 22.512  -9.468  -27.445 1.00 28.15  ? 537 ALA   B N    1 
ATOM   4482 C  CA   . ALA   B 1 526 ? 22.345  -9.796  -26.029 1.00 32.18  ? 537 ALA   B CA   1 
ATOM   4483 C  C    . ALA   B 1 526 ? 22.159  -11.293 -25.821 1.00 31.25  ? 537 ALA   B C    1 
ATOM   4484 O  O    . ALA   B 1 526 ? 22.781  -11.880 -24.929 1.00 31.63  ? 537 ALA   B O    1 
ATOM   4485 C  CB   . ALA   B 1 526 ? 21.175  -9.010  -25.446 1.00 24.25  ? 537 ALA   B CB   1 
ATOM   4486 N  N    . LYS   B 1 527 ? 21.344  -11.939 -26.660 1.00 30.57  ? 538 LYS   B N    1 
ATOM   4487 C  CA   . LYS   B 1 527 ? 21.168  -13.386 -26.556 1.00 35.45  ? 538 LYS   B CA   1 
ATOM   4488 C  C    . LYS   B 1 527 ? 22.470  -14.137 -26.819 1.00 43.02  ? 538 LYS   B C    1 
ATOM   4489 O  O    . LYS   B 1 527 ? 22.785  -15.113 -26.126 1.00 35.48  ? 538 LYS   B O    1 
ATOM   4490 C  CB   . LYS   B 1 527 ? 20.069  -13.850 -27.511 1.00 36.11  ? 538 LYS   B CB   1 
ATOM   4491 C  CG   . LYS   B 1 527 ? 18.674  -13.363 -27.103 1.00 36.33  ? 538 LYS   B CG   1 
ATOM   4492 C  CD   . LYS   B 1 527 ? 17.613  -13.946 -28.022 1.00 53.65  ? 538 LYS   B CD   1 
ATOM   4493 C  CE   . LYS   B 1 527 ? 16.209  -13.786 -27.455 1.00 47.50  ? 538 LYS   B CE   1 
ATOM   4494 N  NZ   . LYS   B 1 527 ? 16.213  -13.182 -26.094 1.00 58.64  ? 538 LYS   B NZ   1 
ATOM   4495 N  N    . GLU   B 1 528 ? 23.233  -13.715 -27.831 1.00 32.28  ? 539 GLU   B N    1 
ATOM   4496 C  CA   . GLU   B 1 528 ? 24.523  -14.343 -28.077 1.00 33.52  ? 539 GLU   B CA   1 
ATOM   4497 C  C    . GLU   B 1 528 ? 25.462  -14.155 -26.889 1.00 32.15  ? 539 GLU   B C    1 
ATOM   4498 O  O    . GLU   B 1 528 ? 26.193  -15.078 -26.514 1.00 40.84  ? 539 GLU   B O    1 
ATOM   4499 C  CB   . GLU   B 1 528 ? 25.145  -13.771 -29.358 1.00 34.45  ? 539 GLU   B CB   1 
ATOM   4500 C  CG   . GLU   B 1 528 ? 26.603  -14.173 -29.576 1.00 36.68  ? 539 GLU   B CG   1 
ATOM   4501 C  CD   . GLU   B 1 528 ? 26.787  -15.646 -29.885 1.00 45.32  ? 539 GLU   B CD   1 
ATOM   4502 O  OE1  . GLU   B 1 528 ? 25.796  -16.326 -30.234 1.00 46.39  ? 539 GLU   B OE1  1 
ATOM   4503 O  OE2  . GLU   B 1 528 ? 27.938  -16.121 -29.781 1.00 45.68  ? 539 GLU   B OE2  1 
ATOM   4504 N  N    . ALA   B 1 529 ? 25.465  -12.955 -26.292 1.00 29.75  ? 540 ALA   B N    1 
ATOM   4505 C  CA   . ALA   B 1 529 ? 26.401  -12.678 -25.204 1.00 36.94  ? 540 ALA   B CA   1 
ATOM   4506 C  C    . ALA   B 1 529 ? 26.025  -13.412 -23.918 1.00 41.85  ? 540 ALA   B C    1 
ATOM   4507 O  O    . ALA   B 1 529 ? 26.913  -13.815 -23.159 1.00 41.16  ? 540 ALA   B O    1 
ATOM   4508 C  CB   . ALA   B 1 529 ? 26.483  -11.172 -24.946 1.00 32.26  ? 540 ALA   B CB   1 
ATOM   4509 N  N    . THR   B 1 530 ? 24.734  -13.574 -23.646 1.00 41.52  ? 541 THR   B N    1 
ATOM   4510 C  CA   . THR   B 1 530 ? 24.279  -14.237 -22.424 1.00 38.97  ? 541 THR   B CA   1 
ATOM   4511 C  C    . THR   B 1 530 ? 24.099  -15.741 -22.596 1.00 58.78  ? 541 THR   B C    1 
ATOM   4512 O  O    . THR   B 1 530 ? 23.759  -16.423 -21.624 1.00 65.38  ? 541 THR   B O    1 
ATOM   4513 C  CB   . THR   B 1 530 ? 22.965  -13.617 -21.943 1.00 38.92  ? 541 THR   B CB   1 
ATOM   4514 O  OG1  . THR   B 1 530 ? 21.981  -13.706 -22.980 1.00 41.78  ? 541 THR   B OG1  1 
ATOM   4515 C  CG2  . THR   B 1 530 ? 23.164  -12.155 -21.605 1.00 38.90  ? 541 THR   B CG2  1 
ATOM   4516 N  N    . LYS   B 1 531 ? 24.332  -16.271 -23.794 1.00 52.67  ? 542 LYS   B N    1 
ATOM   4517 C  CA   . LYS   B 1 531 ? 24.306  -17.714 -24.028 1.00 58.57  ? 542 LYS   B CA   1 
ATOM   4518 C  C    . LYS   B 1 531 ? 25.705  -18.268 -24.286 1.00 62.93  ? 542 LYS   B C    1 
ATOM   4519 O  O    . LYS   B 1 531 ? 26.649  -17.512 -24.536 1.00 67.84  ? 542 LYS   B O    1 
ATOM   4520 C  CB   . LYS   B 1 531 ? 23.388  -18.050 -25.208 1.00 53.47  ? 542 LYS   B CB   1 
HETATM 4521 N  N3   . A1BV1 C 2 .   ? 14.592  -16.091 17.676  0.96 25.78  ? 601 A1BV1 A N3   1 
HETATM 4522 C  C4   . A1BV1 C 2 .   ? 15.664  -16.212 16.810  0.96 24.85  ? 601 A1BV1 A C4   1 
HETATM 4523 C  C6   . A1BV1 C 2 .   ? 17.794  -17.001 16.366  0.96 24.04  ? 601 A1BV1 A C6   1 
HETATM 4524 C  C7   . A1BV1 C 2 .   ? 17.719  -16.424 15.089  0.96 21.04  ? 601 A1BV1 A C7   1 
HETATM 4525 C  C8   . A1BV1 C 2 .   ? 18.806  -16.526 14.177  0.96 24.11  ? 601 A1BV1 A C8   1 
HETATM 4526 C  C10  . A1BV1 C 2 .   ? 17.430  -15.246 12.609  0.96 27.43  ? 601 A1BV1 A C10  1 
HETATM 4527 N  N12  . A1BV1 C 2 .   ? 16.422  -15.145 13.506  0.96 26.47  ? 601 A1BV1 A N12  1 
HETATM 4528 C  C13  . A1BV1 C 2 .   ? 16.543  -15.722 14.735  0.96 25.40  ? 601 A1BV1 A C13  1 
HETATM 4529 C  C15  . A1BV1 C 2 .   ? 15.205  -14.418 13.143  0.96 32.94  ? 601 A1BV1 A C15  1 
HETATM 4530 C  C21  . A1BV1 C 2 .   ? 19.771  -15.996 11.960  0.96 23.26  ? 601 A1BV1 A C21  1 
HETATM 4531 C  C22  . A1BV1 C 2 .   ? 20.797  -15.070 12.004  0.96 25.48  ? 601 A1BV1 A C22  1 
HETATM 4532 C  C24  . A1BV1 C 2 .   ? 21.768  -16.070 10.037  0.96 28.80  ? 601 A1BV1 A C24  1 
HETATM 4533 C  C26  . A1BV1 C 2 .   ? 19.729  -16.941 10.946  0.96 28.08  ? 601 A1BV1 A C26  1 
HETATM 4534 C  C1   . A1BV1 C 2 .   ? 13.606  -13.847 17.457  0.96 34.36  ? 601 A1BV1 A C1   1 
HETATM 4535 C  C16  . A1BV1 C 2 .   ? 15.242  -13.024 13.779  0.96 38.80  ? 601 A1BV1 A C16  1 
HETATM 4536 C  C18  . A1BV1 C 2 .   ? 16.549  -10.994 13.816  0.96 31.47  ? 601 A1BV1 A C18  1 
HETATM 4537 C  C19  . A1BV1 C 2 .   ? 17.644  -10.264 13.029  0.96 32.40  ? 601 A1BV1 A C19  1 
HETATM 4538 C  C2   . A1BV1 C 2 .   ? 13.425  -15.340 17.183  0.96 29.05  ? 601 A1BV1 A C2   1 
HETATM 4539 C  C23  . A1BV1 C 2 .   ? 21.802  -15.121 11.053  0.96 32.86  ? 601 A1BV1 A C23  1 
HETATM 4540 C  C25  . A1BV1 C 2 .   ? 20.735  -16.996 9.996   0.96 33.05  ? 601 A1BV1 A C25  1 
HETATM 4541 C  C30  . A1BV1 C 2 .   ? 24.203  -16.394 9.424   0.96 25.75  ? 601 A1BV1 A C30  1 
HETATM 4542 C  C31  . A1BV1 C 2 .   ? 24.882  -16.742 8.064   0.96 32.42  ? 601 A1BV1 A C31  1 
HETATM 4543 C  C32  . A1BV1 C 2 .   ? 23.963  -16.028 7.051   0.96 24.18  ? 601 A1BV1 A C32  1 
HETATM 4544 C  C33  . A1BV1 C 2 .   ? 22.644  -15.907 7.776   0.96 29.36  ? 601 A1BV1 A C33  1 
HETATM 4545 C  C9   . A1BV1 C 2 .   ? 18.666  -15.956 12.948  0.96 25.40  ? 601 A1BV1 A C9   1 
HETATM 4546 F  F28  . A1BV1 C 2 .   ? 20.660  -17.952 9.044   0.96 33.89  ? 601 A1BV1 A F28  1 
HETATM 4547 N  N14  . A1BV1 C 2 .   ? 15.542  -15.659 15.620  0.96 27.35  ? 601 A1BV1 A N14  1 
HETATM 4548 N  N20  . A1BV1 C 2 .   ? 17.280  -10.218 11.606  0.96 30.26  ? 601 A1BV1 A N20  1 
HETATM 4549 N  N29  . A1BV1 C 2 .   ? 22.809  -16.104 9.090   0.96 33.68  ? 601 A1BV1 A N29  1 
HETATM 4550 N  N5   . A1BV1 C 2 .   ? 16.758  -16.871 17.188  0.96 27.95  ? 601 A1BV1 A N5   1 
HETATM 4551 O  O11  . A1BV1 C 2 .   ? 17.306  -14.737 11.515  0.96 29.52  ? 601 A1BV1 A O11  1 
HETATM 4552 O  O17  . A1BV1 C 2 .   ? 16.421  -12.340 13.358  0.96 31.88  ? 601 A1BV1 A O17  1 
HETATM 4553 O  O34  . A1BV1 C 2 .   ? 21.593  -15.638 7.243   0.96 35.59  ? 601 A1BV1 A O34  1 
HETATM 4554 CL CL27 . A1BV1 C 2 .   ? 18.448  -18.100 10.905  0.96 34.37  ? 601 A1BV1 A CL27 1 
HETATM 4555 N  N3   . A1BV1 D 2 .   ? 9.861   -12.080 -21.070 1.00 32.93  ? 601 A1BV1 B N3   1 
HETATM 4556 C  C4   . A1BV1 D 2 .   ? 8.741   -11.825 -20.308 1.00 31.54  ? 601 A1BV1 B C4   1 
HETATM 4557 C  C6   . A1BV1 D 2 .   ? 6.529   -11.211 -20.235 1.00 27.65  ? 601 A1BV1 B C6   1 
HETATM 4558 C  C7   . A1BV1 D 2 .   ? 6.561   -11.285 -18.838 1.00 30.21  ? 601 A1BV1 B C7   1 
HETATM 4559 C  C8   . A1BV1 D 2 .   ? 5.420   -10.984 -18.054 1.00 34.42  ? 601 A1BV1 B C8   1 
HETATM 4560 C  C10  . A1BV1 D 2 .   ? 6.789   -11.468 -16.094 1.00 38.13  ? 601 A1BV1 B C10  1 
HETATM 4561 N  N12  . A1BV1 D 2 .   ? 7.861   -11.733 -16.863 1.00 32.00  ? 601 A1BV1 B N12  1 
HETATM 4562 C  C13  . A1BV1 D 2 .   ? 7.777   -11.640 -18.227 1.00 34.30  ? 601 A1BV1 B C13  1 
HETATM 4563 C  C15  . A1BV1 D 2 .   ? 9.114   -12.149 -16.225 1.00 31.89  ? 601 A1BV1 B C15  1 
HETATM 4564 C  C21  . A1BV1 D 2 .   ? 4.382   -10.702 -15.820 1.00 33.35  ? 601 A1BV1 B C21  1 
HETATM 4565 C  C22  . A1BV1 D 2 .   ? 4.011   -9.356  -15.714 1.00 34.84  ? 601 A1BV1 B C22  1 
HETATM 4566 C  C24  . A1BV1 D 2 .   ? 2.209   -9.962  -14.236 1.00 41.07  ? 601 A1BV1 B C24  1 
HETATM 4567 C  C26  . A1BV1 D 2 .   ? 3.639   -11.674 -15.142 1.00 37.78  ? 601 A1BV1 B C26  1 
HETATM 4568 C  C1   . A1BV1 D 2 .   ? 11.845  -11.013 -20.148 1.00 42.76  ? 601 A1BV1 B C1   1 
HETATM 4569 C  C16  . A1BV1 D 2 .   ? 10.109  -10.981 -16.169 1.00 32.00  ? 601 A1BV1 B C16  1 
HETATM 4570 C  C18  . A1BV1 D 2 .   ? 10.477  -8.767  -15.349 1.00 40.21  ? 601 A1BV1 B C18  1 
HETATM 4571 C  C19  . A1BV1 D 2 .   ? 9.921   -7.778  -14.326 1.00 47.15  ? 601 A1BV1 B C19  1 
HETATM 4572 C  C2   . A1BV1 D 2 .   ? 11.128  -12.342 -20.388 1.00 35.23  ? 601 A1BV1 B C2   1 
HETATM 4573 C  C23  . A1BV1 D 2 .   ? 2.940   -8.984  -14.917 1.00 38.37  ? 601 A1BV1 B C23  1 
HETATM 4574 C  C25  . A1BV1 D 2 .   ? 2.568   -11.302 -14.342 1.00 37.14  ? 601 A1BV1 B C25  1 
HETATM 4575 C  C30  . A1BV1 D 2 .   ? 0.008   -8.773  -13.961 1.00 37.99  ? 601 A1BV1 B C30  1 
HETATM 4576 C  C31  . A1BV1 D 2 .   ? -1.091  -8.770  -12.866 1.00 43.46  ? 601 A1BV1 B C31  1 
HETATM 4577 C  C32  . A1BV1 D 2 .   ? -0.326  -9.273  -11.621 1.00 29.89  ? 601 A1BV1 B C32  1 
HETATM 4578 C  C33  . A1BV1 D 2 .   ? 0.967   -9.860  -12.128 1.00 42.59  ? 601 A1BV1 B C33  1 
HETATM 4579 C  C9   . A1BV1 D 2 .   ? 5.526   -11.051 -16.690 1.00 33.45  ? 601 A1BV1 B C9   1 
HETATM 4580 F  F28  . A1BV1 D 2 .   ? 1.862   -12.248 -13.673 1.00 34.85  ? 601 A1BV1 B F28  1 
HETATM 4581 N  N14  . A1BV1 D 2 .   ? 8.830   -11.898 -18.993 1.00 30.95  ? 601 A1BV1 B N14  1 
HETATM 4582 N  N20  . A1BV1 D 2 .   ? 9.742   -8.472  -13.033 1.00 41.87  ? 601 A1BV1 B N20  1 
HETATM 4583 N  N29  . A1BV1 D 2 .   ? 1.119   -9.586  -13.438 1.00 35.92  ? 601 A1BV1 B N29  1 
HETATM 4584 N  N5   . A1BV1 D 2 .   ? 7.621   -11.483 -20.919 1.00 26.94  ? 601 A1BV1 B N5   1 
HETATM 4585 O  O11  . A1BV1 D 2 .   ? 6.861   -11.572 -14.886 1.00 35.19  ? 601 A1BV1 B O11  1 
HETATM 4586 O  O17  . A1BV1 D 2 .   ? 9.542   -9.844  -15.499 1.00 36.72  ? 601 A1BV1 B O17  1 
HETATM 4587 O  O34  . A1BV1 D 2 .   ? 1.733   -10.509 -11.447 1.00 45.59  ? 601 A1BV1 B O34  1 
HETATM 4588 CL CL27 . A1BV1 D 2 .   ? 4.071   -13.349 -15.262 1.00 37.61  ? 601 A1BV1 B CL27 1 
HETATM 4589 O  O    . HOH   E 3 .   ? 24.450  -12.491 5.453   1.00 42.43  ? 701 HOH   A O    1 
HETATM 4590 O  O    . HOH   E 3 .   ? 31.503  -24.906 -5.955  1.00 39.48  ? 702 HOH   A O    1 
HETATM 4591 O  O    . HOH   E 3 .   ? 14.603  -23.143 23.116  1.00 46.45  ? 703 HOH   A O    1 
HETATM 4592 O  O    . HOH   E 3 .   ? 41.188  6.512   25.237  1.00 39.05  ? 704 HOH   A O    1 
HETATM 4593 O  O    . HOH   E 3 .   ? 40.361  -12.150 13.551  1.00 48.77  ? 705 HOH   A O    1 
HETATM 4594 O  O    . HOH   E 3 .   ? 10.279  2.127   27.844  1.00 28.61  ? 706 HOH   A O    1 
HETATM 4595 O  O    . HOH   E 3 .   ? 24.129  -27.618 -5.025  1.00 48.95  ? 707 HOH   A O    1 
HETATM 4596 O  O    . HOH   E 3 .   ? 27.204  -13.879 30.308  1.00 41.86  ? 708 HOH   A O    1 
HETATM 4597 O  O    . HOH   E 3 .   ? 24.012  -6.611  9.622   1.00 25.76  ? 709 HOH   A O    1 
HETATM 4598 O  O    . HOH   E 3 .   ? 40.838  -1.037  25.825  1.00 42.23  ? 710 HOH   A O    1 
HETATM 4599 O  O    . HOH   E 3 .   ? 33.277  -12.296 0.806   1.00 53.05  ? 711 HOH   A O    1 
HETATM 4600 O  O    . HOH   E 3 .   ? 10.845  -10.822 18.569  1.00 39.76  ? 712 HOH   A O    1 
HETATM 4601 O  O    . HOH   E 3 .   ? 30.852  -13.609 26.174  1.00 40.86  ? 713 HOH   A O    1 
HETATM 4602 O  O    . HOH   E 3 .   ? 27.840  1.396   11.712  1.00 32.74  ? 714 HOH   A O    1 
HETATM 4603 O  O    . HOH   E 3 .   ? 29.689  -26.082 9.132   1.00 44.77  ? 715 HOH   A O    1 
HETATM 4604 O  O    . HOH   E 3 .   ? 37.640  7.196   13.814  1.00 35.77  ? 716 HOH   A O    1 
HETATM 4605 O  O    . HOH   E 3 .   ? 14.311  8.707   21.809  1.00 37.63  ? 717 HOH   A O    1 
HETATM 4606 O  O    . HOH   E 3 .   ? 37.485  -13.958 11.477  1.00 52.63  ? 718 HOH   A O    1 
HETATM 4607 O  O    . HOH   E 3 .   ? 13.749  1.427   19.432  1.00 26.10  ? 719 HOH   A O    1 
HETATM 4608 O  O    . HOH   E 3 .   ? 41.155  0.629   14.266  1.00 43.30  ? 720 HOH   A O    1 
HETATM 4609 O  O    . HOH   E 3 .   ? 1.512   -2.201  22.619  1.00 44.90  ? 721 HOH   A O    1 
HETATM 4610 O  O    . HOH   E 3 .   ? 23.737  -32.977 17.134  1.00 40.89  ? 722 HOH   A O    1 
HETATM 4611 O  O    . HOH   E 3 .   ? 25.281  -13.987 12.070  1.00 39.07  ? 723 HOH   A O    1 
HETATM 4612 O  O    . HOH   E 3 .   ? 28.924  -9.983  5.339   1.00 46.49  ? 724 HOH   A O    1 
HETATM 4613 O  O    . HOH   E 3 .   ? 20.794  -34.767 15.110  1.00 50.33  ? 725 HOH   A O    1 
HETATM 4614 O  O    . HOH   E 3 .   ? 0.790   -13.284 26.350  1.00 43.78  ? 726 HOH   A O    1 
HETATM 4615 O  O    . HOH   E 3 .   ? 22.551  -30.217 20.140  1.00 39.24  ? 727 HOH   A O    1 
HETATM 4616 O  O    . HOH   E 3 .   ? 34.120  -11.070 26.259  1.00 38.32  ? 728 HOH   A O    1 
HETATM 4617 O  O    . HOH   E 3 .   ? 31.965  -8.786  32.226  1.00 33.10  ? 729 HOH   A O    1 
HETATM 4618 O  O    . HOH   E 3 .   ? 23.654  -9.691  35.414  1.00 36.92  ? 730 HOH   A O    1 
HETATM 4619 O  O    . HOH   E 3 .   ? 9.944   -7.812  16.450  1.00 41.45  ? 731 HOH   A O    1 
HETATM 4620 O  O    . HOH   E 3 .   ? 28.679  11.700  4.481   1.00 40.17  ? 732 HOH   A O    1 
HETATM 4621 O  O    . HOH   E 3 .   ? 12.493  6.740   30.381  1.00 41.90  ? 733 HOH   A O    1 
HETATM 4622 O  O    . HOH   E 3 .   ? 38.305  15.897  23.008  1.00 53.03  ? 734 HOH   A O    1 
HETATM 4623 O  O    . HOH   E 3 .   ? 23.166  12.736  17.092  1.00 32.10  ? 735 HOH   A O    1 
HETATM 4624 O  O    . HOH   E 3 .   ? 20.316  -2.095  40.415  1.00 38.85  ? 736 HOH   A O    1 
HETATM 4625 O  O    . HOH   E 3 .   ? 8.313   -22.508 16.616  1.00 42.91  ? 737 HOH   A O    1 
HETATM 4626 O  O    . HOH   E 3 .   ? 37.853  9.775   5.138   1.00 49.89  ? 738 HOH   A O    1 
HETATM 4627 O  O    . HOH   E 3 .   ? 28.466  -26.733 5.499   1.00 38.48  ? 739 HOH   A O    1 
HETATM 4628 O  O    . HOH   E 3 .   ? 16.657  11.647  22.730  1.00 43.72  ? 740 HOH   A O    1 
HETATM 4629 O  O    . HOH   E 3 .   ? 28.965  -11.607 33.034  1.00 47.00  ? 741 HOH   A O    1 
HETATM 4630 O  O    . HOH   E 3 .   ? 27.231  11.830  35.684  1.00 41.77  ? 742 HOH   A O    1 
HETATM 4631 O  O    . HOH   E 3 .   ? 25.444  -6.033  40.092  1.00 48.89  ? 743 HOH   A O    1 
HETATM 4632 O  O    . HOH   E 3 .   ? 37.225  -14.457 7.368   1.00 57.73  ? 744 HOH   A O    1 
HETATM 4633 O  O    . HOH   E 3 .   ? 40.176  -3.174  6.812   1.00 52.75  ? 745 HOH   A O    1 
HETATM 4634 O  O    . HOH   E 3 .   ? 16.046  -16.702 -0.610  1.00 55.36  ? 746 HOH   A O    1 
HETATM 4635 O  O    . HOH   E 3 .   ? 17.732  -6.783  12.146  1.00 34.39  ? 747 HOH   A O    1 
HETATM 4636 O  O    . HOH   E 3 .   ? 8.811   -4.519  18.536  1.00 42.52  ? 748 HOH   A O    1 
HETATM 4637 O  O    . HOH   E 3 .   ? 20.265  3.716   39.406  1.00 37.52  ? 749 HOH   A O    1 
HETATM 4638 O  O    . HOH   E 3 .   ? 19.322  -21.180 31.830  1.00 48.77  ? 750 HOH   A O    1 
HETATM 4639 O  O    . HOH   E 3 .   ? 7.981   14.314  13.301  1.00 50.65  ? 751 HOH   A O    1 
HETATM 4640 O  O    . HOH   E 3 .   ? 22.071  -37.508 21.661  1.00 36.94  ? 752 HOH   A O    1 
HETATM 4641 O  O    . HOH   E 3 .   ? 29.809  12.277  25.640  1.00 38.21  ? 753 HOH   A O    1 
HETATM 4642 O  O    . HOH   E 3 .   ? 18.742  -12.911 10.216  1.00 33.83  ? 754 HOH   A O    1 
HETATM 4643 O  O    . HOH   E 3 .   ? 12.032  1.560   26.464  1.00 30.44  ? 755 HOH   A O    1 
HETATM 4644 O  O    . HOH   E 3 .   ? 3.256   -2.648  26.242  1.00 36.40  ? 756 HOH   A O    1 
HETATM 4645 O  O    . HOH   E 3 .   ? 19.696  -23.264 20.152  1.00 37.54  ? 757 HOH   A O    1 
HETATM 4646 O  O    . HOH   E 3 .   ? 11.311  -2.834  34.662  1.00 31.86  ? 758 HOH   A O    1 
HETATM 4647 O  O    . HOH   E 3 .   ? 8.668   -10.645 21.776  1.00 37.75  ? 759 HOH   A O    1 
HETATM 4648 O  O    . HOH   E 3 .   ? 3.907   -0.270  20.575  1.00 44.44  ? 760 HOH   A O    1 
HETATM 4649 O  O    . HOH   E 3 .   ? 35.455  6.957   28.270  1.00 46.65  ? 761 HOH   A O    1 
HETATM 4650 O  O    . HOH   E 3 .   ? 11.421  -10.015 23.295  1.00 24.81  ? 762 HOH   A O    1 
HETATM 4651 O  O    . HOH   E 3 .   ? 15.075  10.701  28.575  1.00 31.82  ? 763 HOH   A O    1 
HETATM 4652 O  O    . HOH   E 3 .   ? 3.261   -13.173 27.766  1.00 29.67  ? 764 HOH   A O    1 
HETATM 4653 O  O    . HOH   E 3 .   ? 38.710  -6.218  22.911  1.00 38.69  ? 765 HOH   A O    1 
HETATM 4654 O  O    . HOH   E 3 .   ? 33.450  11.058  16.031  1.00 34.33  ? 766 HOH   A O    1 
HETATM 4655 O  O    . HOH   E 3 .   ? 16.776  5.936   35.354  1.00 35.75  ? 767 HOH   A O    1 
HETATM 4656 O  O    . HOH   E 3 .   ? 6.593   -3.318  19.461  1.00 45.65  ? 768 HOH   A O    1 
HETATM 4657 O  O    . HOH   E 3 .   ? 14.636  -8.251  15.245  1.00 26.57  ? 769 HOH   A O    1 
HETATM 4658 O  O    . HOH   E 3 .   ? 37.708  -5.148  31.204  1.00 44.58  ? 770 HOH   A O    1 
HETATM 4659 O  O    . HOH   E 3 .   ? 13.129  9.057   18.596  1.00 33.18  ? 771 HOH   A O    1 
HETATM 4660 O  O    . HOH   E 3 .   ? 17.974  -14.847 39.933  1.00 54.06  ? 772 HOH   A O    1 
HETATM 4661 O  O    . HOH   E 3 .   ? 3.478   -12.300 20.923  1.00 43.53  ? 773 HOH   A O    1 
HETATM 4662 O  O    . HOH   E 3 .   ? 39.244  -10.282 11.715  1.00 42.35  ? 774 HOH   A O    1 
HETATM 4663 O  O    . HOH   E 3 .   ? 34.273  -16.931 22.821  1.00 41.97  ? 775 HOH   A O    1 
HETATM 4664 O  O    . HOH   E 3 .   ? 24.140  -14.436 14.505  1.00 35.32  ? 776 HOH   A O    1 
HETATM 4665 O  O    . HOH   E 3 .   ? 22.241  -29.088 16.351  1.00 38.26  ? 777 HOH   A O    1 
HETATM 4666 O  O    . HOH   E 3 .   ? 8.935   1.768   25.813  1.00 30.62  ? 778 HOH   A O    1 
HETATM 4667 O  O    . HOH   E 3 .   ? 7.758   11.789  33.157  1.00 37.82  ? 779 HOH   A O    1 
HETATM 4668 O  O    . HOH   E 3 .   ? 20.081  8.829   16.222  1.00 27.94  ? 780 HOH   A O    1 
HETATM 4669 O  O    . HOH   E 3 .   ? 12.442  -7.251  16.334  1.00 31.37  ? 781 HOH   A O    1 
HETATM 4670 O  O    . HOH   E 3 .   ? 12.331  13.899  8.383   1.00 39.56  ? 782 HOH   A O    1 
HETATM 4671 O  O    . HOH   E 3 .   ? 12.395  -4.918  14.939  1.00 35.40  ? 783 HOH   A O    1 
HETATM 4672 O  O    . HOH   E 3 .   ? 9.779   -26.050 15.493  1.00 39.49  ? 784 HOH   A O    1 
HETATM 4673 O  O    . HOH   E 3 .   ? 38.974  5.618   25.944  1.00 48.46  ? 785 HOH   A O    1 
HETATM 4674 O  O    . HOH   E 3 .   ? 11.406  17.180  10.014  1.00 55.34  ? 786 HOH   A O    1 
HETATM 4675 O  O    . HOH   E 3 .   ? 20.098  15.232  19.773  1.00 43.11  ? 787 HOH   A O    1 
HETATM 4676 O  O    . HOH   E 3 .   ? 15.942  -12.743 10.153  1.00 38.43  ? 788 HOH   A O    1 
HETATM 4677 O  O    . HOH   E 3 .   ? 30.221  -7.496  5.525   1.00 45.48  ? 789 HOH   A O    1 
HETATM 4678 O  O    . HOH   E 3 .   ? 34.814  2.198   32.564  1.00 47.67  ? 790 HOH   A O    1 
HETATM 4679 O  O    . HOH   E 3 .   ? 4.777   -2.957  29.630  1.00 38.63  ? 791 HOH   A O    1 
HETATM 4680 O  O    . HOH   E 3 .   ? 13.429  3.521   33.558  1.00 48.08  ? 792 HOH   A O    1 
HETATM 4681 O  O    . HOH   E 3 .   ? 23.544  7.703   15.805  1.00 23.21  ? 793 HOH   A O    1 
HETATM 4682 O  O    . HOH   E 3 .   ? 9.123   2.729   21.163  1.00 38.27  ? 794 HOH   A O    1 
HETATM 4683 O  O    . HOH   E 3 .   ? 35.011  -22.160 6.541   1.00 43.57  ? 795 HOH   A O    1 
HETATM 4684 O  O    . HOH   E 3 .   ? 11.524  -2.424  37.244  1.00 37.16  ? 796 HOH   A O    1 
HETATM 4685 O  O    . HOH   E 3 .   ? 23.359  -9.812  8.813   1.00 28.94  ? 797 HOH   A O    1 
HETATM 4686 O  O    . HOH   E 3 .   ? 23.783  -13.923 28.322  1.00 27.92  ? 798 HOH   A O    1 
HETATM 4687 O  O    . HOH   E 3 .   ? 39.604  9.433   11.443  1.00 48.11  ? 799 HOH   A O    1 
HETATM 4688 O  O    . HOH   E 3 .   ? 22.994  17.325  20.504  1.00 51.32  ? 800 HOH   A O    1 
HETATM 4689 O  O    . HOH   E 3 .   ? 14.447  -4.402  12.005  1.00 39.76  ? 801 HOH   A O    1 
HETATM 4690 O  O    . HOH   E 3 .   ? 22.038  -12.503 8.711   1.00 33.03  ? 802 HOH   A O    1 
HETATM 4691 O  O    . HOH   E 3 .   ? 32.516  8.461   -0.628  1.00 40.37  ? 803 HOH   A O    1 
HETATM 4692 O  O    . HOH   E 3 .   ? 22.603  -0.361  13.604  1.00 20.85  ? 804 HOH   A O    1 
HETATM 4693 O  O    . HOH   E 3 .   ? 26.937  -6.807  10.921  1.00 25.66  ? 805 HOH   A O    1 
HETATM 4694 O  O    . HOH   E 3 .   ? 36.661  -1.977  21.987  1.00 28.55  ? 806 HOH   A O    1 
HETATM 4695 O  O    . HOH   E 3 .   ? 24.968  -15.998 26.959  1.00 36.77  ? 807 HOH   A O    1 
HETATM 4696 O  O    . HOH   E 3 .   ? 12.465  4.497   30.949  1.00 46.68  ? 808 HOH   A O    1 
HETATM 4697 O  O    . HOH   E 3 .   ? 35.943  5.377   15.097  1.00 33.15  ? 809 HOH   A O    1 
HETATM 4698 O  O    . HOH   E 3 .   ? 9.593   -20.871 20.779  1.00 49.59  ? 810 HOH   A O    1 
HETATM 4699 O  O    . HOH   E 3 .   ? 33.332  3.864   36.348  1.00 42.32  ? 811 HOH   A O    1 
HETATM 4700 O  O    . HOH   E 3 .   ? 19.294  -9.902  8.128   1.00 45.52  ? 812 HOH   A O    1 
HETATM 4701 O  O    . HOH   E 3 .   ? 12.368  1.952   29.694  1.00 31.79  ? 813 HOH   A O    1 
HETATM 4702 O  O    . HOH   E 3 .   ? 8.784   -13.140 20.793  1.00 50.51  ? 814 HOH   A O    1 
HETATM 4703 O  O    . HOH   E 3 .   ? 31.623  -6.283  33.570  1.00 36.07  ? 815 HOH   A O    1 
HETATM 4704 O  O    . HOH   E 3 .   ? 30.903  14.345  22.986  1.00 44.88  ? 816 HOH   A O    1 
HETATM 4705 O  O    . HOH   E 3 .   ? 15.963  2.341   37.538  1.00 28.87  ? 817 HOH   A O    1 
HETATM 4706 O  O    . HOH   E 3 .   ? 8.411   -2.921  33.509  1.00 31.52  ? 818 HOH   A O    1 
HETATM 4707 O  O    . HOH   E 3 .   ? 22.204  10.578  40.441  1.00 34.85  ? 819 HOH   A O    1 
HETATM 4708 O  O    . HOH   E 3 .   ? 9.434   -14.753 29.805  1.00 34.92  ? 820 HOH   A O    1 
HETATM 4709 O  O    . HOH   E 3 .   ? 12.521  -8.469  37.064  1.00 35.94  ? 821 HOH   A O    1 
HETATM 4710 O  O    . HOH   E 3 .   ? 17.764  -0.569  39.000  1.00 36.54  ? 822 HOH   A O    1 
HETATM 4711 O  O    . HOH   E 3 .   ? 31.899  -3.057  35.844  1.00 33.61  ? 823 HOH   A O    1 
HETATM 4712 O  O    . HOH   E 3 .   ? 27.448  -0.861  15.127  1.00 23.23  ? 824 HOH   A O    1 
HETATM 4713 O  O    . HOH   E 3 .   ? 3.880   0.340   24.239  1.00 46.73  ? 825 HOH   A O    1 
HETATM 4714 O  O    . HOH   E 3 .   ? 9.640   -30.594 9.256   1.00 45.44  ? 826 HOH   A O    1 
HETATM 4715 O  O    . HOH   E 3 .   ? 30.787  13.797  4.404   1.00 43.71  ? 827 HOH   A O    1 
HETATM 4716 O  O    . HOH   E 3 .   ? 25.761  19.569  19.927  1.00 56.97  ? 828 HOH   A O    1 
HETATM 4717 O  O    . HOH   E 3 .   ? 41.324  -12.806 15.510  1.00 53.60  ? 829 HOH   A O    1 
HETATM 4718 O  O    . HOH   E 3 .   ? 19.994  -14.929 36.197  1.00 35.67  ? 830 HOH   A O    1 
HETATM 4719 O  O    . HOH   E 3 .   ? 22.701  -13.399 35.847  1.00 36.93  ? 831 HOH   A O    1 
HETATM 4720 O  O    . HOH   E 3 .   ? 40.843  5.061   20.122  1.00 46.70  ? 832 HOH   A O    1 
HETATM 4721 O  O    . HOH   E 3 .   ? 5.417   1.833   21.611  1.00 50.86  ? 833 HOH   A O    1 
HETATM 4722 O  O    . HOH   E 3 .   ? 37.353  3.229   16.674  1.00 33.13  ? 834 HOH   A O    1 
HETATM 4723 O  O    . HOH   E 3 .   ? 38.397  -13.820 13.538  1.00 48.84  ? 835 HOH   A O    1 
HETATM 4724 O  O    . HOH   E 3 .   ? 35.732  -7.366  6.064   1.00 44.12  ? 836 HOH   A O    1 
HETATM 4725 O  O    . HOH   E 3 .   ? 15.074  12.442  18.945  1.00 39.08  ? 837 HOH   A O    1 
HETATM 4726 O  O    . HOH   E 3 .   ? 28.952  -18.358 15.744  1.00 41.36  ? 838 HOH   A O    1 
HETATM 4727 O  O    . HOH   E 3 .   ? 24.484  1.317   12.477  1.00 25.84  ? 839 HOH   A O    1 
HETATM 4728 O  O    . HOH   E 3 .   ? 27.941  -6.663  36.415  1.00 38.21  ? 840 HOH   A O    1 
HETATM 4729 O  O    . HOH   E 3 .   ? 10.708  4.450   27.568  1.00 39.34  ? 841 HOH   A O    1 
HETATM 4730 O  O    . HOH   E 3 .   ? 15.327  -11.785 39.015  1.00 41.15  ? 842 HOH   A O    1 
HETATM 4731 O  O    . HOH   E 3 .   ? 38.000  -3.485  23.794  1.00 34.36  ? 843 HOH   A O    1 
HETATM 4732 O  O    . HOH   E 3 .   ? 37.491  11.735  16.951  1.00 44.72  ? 844 HOH   A O    1 
HETATM 4733 O  O    . HOH   E 3 .   ? 28.531  16.762  20.030  1.00 43.49  ? 845 HOH   A O    1 
HETATM 4734 O  O    . HOH   E 3 .   ? 16.207  -19.628 24.096  1.00 51.69  ? 846 HOH   A O    1 
HETATM 4735 O  O    . HOH   E 3 .   ? 28.286  3.061   14.043  1.00 24.83  ? 847 HOH   A O    1 
HETATM 4736 O  O    . HOH   E 3 .   ? 15.540  9.590   30.620  1.00 40.82  ? 848 HOH   A O    1 
HETATM 4737 O  O    . HOH   E 3 .   ? 39.385  10.339  7.416   1.00 49.40  ? 849 HOH   A O    1 
HETATM 4738 O  O    . HOH   E 3 .   ? 26.890  -29.965 6.765   1.00 44.54  ? 850 HOH   A O    1 
HETATM 4739 O  O    . HOH   E 3 .   ? 36.315  -20.676 8.130   1.00 51.35  ? 851 HOH   A O    1 
HETATM 4740 O  O    . HOH   E 3 .   ? 36.964  5.070   28.991  1.00 50.91  ? 852 HOH   A O    1 
HETATM 4741 O  O    . HOH   E 3 .   ? 20.234  15.913  27.567  1.00 56.10  ? 853 HOH   A O    1 
HETATM 4742 O  O    . HOH   E 3 .   ? 21.580  14.194  27.442  1.00 51.54  ? 854 HOH   A O    1 
HETATM 4743 O  O    . HOH   E 3 .   ? 6.703   -2.267  31.638  1.00 34.28  ? 855 HOH   A O    1 
HETATM 4744 O  O    . HOH   E 3 .   ? 8.536   2.838   18.109  1.00 49.85  ? 856 HOH   A O    1 
HETATM 4745 O  O    . HOH   E 3 .   ? 30.444  5.591   1.712   1.00 45.00  ? 857 HOH   A O    1 
HETATM 4746 O  O    . HOH   E 3 .   ? 12.095  -13.555 36.920  1.00 40.90  ? 858 HOH   A O    1 
HETATM 4747 O  O    . HOH   E 3 .   ? 33.773  -13.716 26.310  1.00 52.28  ? 859 HOH   A O    1 
HETATM 4748 O  O    . HOH   E 3 .   ? 21.090  -16.363 31.867  1.00 41.92  ? 860 HOH   A O    1 
HETATM 4749 O  O    . HOH   E 3 .   ? 6.223   1.118   26.138  1.00 40.23  ? 861 HOH   A O    1 
HETATM 4750 O  O    . HOH   E 3 .   ? 8.027   7.835   34.299  1.00 33.82  ? 862 HOH   A O    1 
HETATM 4751 O  O    . HOH   E 3 .   ? 13.865  -7.773  39.196  1.00 45.65  ? 863 HOH   A O    1 
HETATM 4752 O  O    . HOH   E 3 .   ? 11.369  -26.572 17.575  1.00 43.50  ? 864 HOH   A O    1 
HETATM 4753 O  O    . HOH   E 3 .   ? 8.456   2.783   29.302  1.00 35.25  ? 865 HOH   A O    1 
HETATM 4754 O  O    . HOH   E 3 .   ? 42.920  -12.820 19.797  1.00 54.95  ? 866 HOH   A O    1 
HETATM 4755 O  O    . HOH   E 3 .   ? 40.606  -5.124  21.225  1.00 44.89  ? 867 HOH   A O    1 
HETATM 4756 O  O    . HOH   E 3 .   ? 32.485  5.806   36.538  1.00 51.98  ? 868 HOH   A O    1 
HETATM 4757 O  O    . HOH   E 3 .   ? 25.709  -32.483 5.304   1.00 52.90  ? 869 HOH   A O    1 
HETATM 4758 O  O    . HOH   E 3 .   ? 40.628  -2.562  24.197  1.00 44.04  ? 870 HOH   A O    1 
HETATM 4759 O  O    . HOH   E 3 .   ? 14.934  -7.545  12.660  1.00 42.89  ? 871 HOH   A O    1 
HETATM 4760 O  O    . HOH   E 3 .   ? 6.665   9.901   31.164  1.00 41.37  ? 872 HOH   A O    1 
HETATM 4761 O  O    . HOH   E 3 .   ? 14.454  -35.059 20.795  1.00 63.00  ? 873 HOH   A O    1 
HETATM 4762 O  O    . HOH   E 3 .   ? 7.531   -15.392 28.374  1.00 45.41  ? 874 HOH   A O    1 
HETATM 4763 O  O    . HOH   E 3 .   ? 28.829  -4.070  3.833   1.00 45.80  ? 875 HOH   A O    1 
HETATM 4764 O  O    . HOH   E 3 .   ? 12.510  -11.227 38.296  1.00 43.53  ? 876 HOH   A O    1 
HETATM 4765 O  O    . HOH   E 3 .   ? 7.912   15.558  31.661  1.00 40.35  ? 877 HOH   A O    1 
HETATM 4766 O  O    . HOH   E 3 .   ? 8.387   9.589   29.232  1.00 55.54  ? 878 HOH   A O    1 
HETATM 4767 O  O    . HOH   E 3 .   ? 34.313  -9.412  31.246  1.00 48.44  ? 879 HOH   A O    1 
HETATM 4768 O  O    . HOH   E 3 .   ? 27.716  14.307  5.591   1.00 55.16  ? 880 HOH   A O    1 
HETATM 4769 O  O    . HOH   E 3 .   ? 22.344  9.970   17.270  1.00 26.70  ? 881 HOH   A O    1 
HETATM 4770 O  O    . HOH   E 3 .   ? 13.021  -10.652 15.181  1.00 44.65  ? 882 HOH   A O    1 
HETATM 4771 O  O    . HOH   E 3 .   ? 28.072  -7.189  39.064  1.00 50.33  ? 883 HOH   A O    1 
HETATM 4772 O  O    . HOH   E 3 .   ? 21.455  -36.903 14.074  1.00 57.82  ? 884 HOH   A O    1 
HETATM 4773 O  O    . HOH   E 3 .   ? 8.955   -22.946 19.110  1.00 51.17  ? 885 HOH   A O    1 
HETATM 4774 O  O    . HOH   E 3 .   ? 18.102  2.317   39.695  1.00 45.58  ? 886 HOH   A O    1 
HETATM 4775 O  O    . HOH   E 3 .   ? 23.072  -16.023 30.272  1.00 39.34  ? 887 HOH   A O    1 
HETATM 4776 O  O    . HOH   E 3 .   ? 39.710  0.871   18.787  1.00 46.83  ? 888 HOH   A O    1 
HETATM 4777 O  O    . HOH   E 3 .   ? 12.772  6.992   34.458  1.00 54.13  ? 889 HOH   A O    1 
HETATM 4778 O  O    . HOH   E 3 .   ? 30.392  -6.399  35.730  1.00 46.58  ? 890 HOH   A O    1 
HETATM 4779 O  O    . HOH   E 3 .   ? 15.911  5.030   31.981  1.00 48.31  ? 891 HOH   A O    1 
HETATM 4780 O  O    . HOH   E 3 .   ? 14.836  4.441   35.421  1.00 45.31  ? 892 HOH   A O    1 
HETATM 4781 O  O    . HOH   E 3 .   ? 9.683   -13.466 18.706  1.00 44.05  ? 893 HOH   A O    1 
HETATM 4782 O  O    . HOH   E 3 .   ? 14.405  7.643   32.119  1.00 42.46  ? 894 HOH   A O    1 
HETATM 4783 O  O    . HOH   E 3 .   ? 16.059  -9.081  39.843  1.00 46.32  ? 895 HOH   A O    1 
HETATM 4784 O  O    . HOH   E 3 .   ? 38.722  -0.515  20.865  1.00 48.37  ? 896 HOH   A O    1 
HETATM 4785 O  O    . HOH   E 3 .   ? 24.185  -36.753 19.727  1.00 45.59  ? 897 HOH   A O    1 
HETATM 4786 O  O    . HOH   E 3 .   ? 39.622  3.325   17.941  1.00 46.02  ? 898 HOH   A O    1 
HETATM 4787 O  O    . HOH   E 3 .   ? 9.808   -14.887 16.550  1.00 50.73  ? 899 HOH   A O    1 
HETATM 4788 O  O    . HOH   E 3 .   ? 22.588  -8.132  5.296   1.00 49.04  ? 900 HOH   A O    1 
HETATM 4789 O  O    . HOH   E 3 .   ? 43.245  0.674   31.795  1.00 51.47  ? 901 HOH   A O    1 
HETATM 4790 O  O    . HOH   E 3 .   ? 16.654  4.413   3.403   1.00 52.84  ? 902 HOH   A O    1 
HETATM 4791 O  O    . HOH   F 3 .   ? 14.807  21.812  -11.574 1.00 46.57  ? 701 HOH   B O    1 
HETATM 4792 O  O    . HOH   F 3 .   ? 16.548  -13.451 -23.905 1.00 55.30  ? 702 HOH   B O    1 
HETATM 4793 O  O    . HOH   F 3 .   ? 29.457  -2.047  -15.634 1.00 62.48  ? 703 HOH   B O    1 
HETATM 4794 O  O    . HOH   F 3 .   ? 5.476   22.188  -15.460 1.00 51.48  ? 704 HOH   B O    1 
HETATM 4795 O  O    . HOH   F 3 .   ? 20.387  -6.678  10.424  1.00 26.95  ? 705 HOH   B O    1 
HETATM 4796 O  O    . HOH   F 3 .   ? -5.824  -19.050 -27.259 1.00 44.99  ? 706 HOH   B O    1 
HETATM 4797 O  O    . HOH   F 3 .   ? 2.288   14.948  -26.463 1.00 38.56  ? 707 HOH   B O    1 
HETATM 4798 O  O    . HOH   F 3 .   ? 17.156  1.666   -15.197 1.00 26.15  ? 708 HOH   B O    1 
HETATM 4799 O  O    . HOH   F 3 .   ? 26.917  -1.945  -22.841 1.00 25.85  ? 709 HOH   B O    1 
HETATM 4800 O  O    . HOH   F 3 .   ? 24.979  1.015   -6.207  1.00 48.65  ? 710 HOH   B O    1 
HETATM 4801 O  O    . HOH   F 3 .   ? 25.926  17.799  0.515   1.00 52.40  ? 711 HOH   B O    1 
HETATM 4802 O  O    . HOH   F 3 .   ? 7.753   -21.440 -27.727 1.00 46.62  ? 712 HOH   B O    1 
HETATM 4803 O  O    . HOH   F 3 .   ? 16.770  2.957   7.795   1.00 47.95  ? 713 HOH   B O    1 
HETATM 4804 O  O    . HOH   F 3 .   ? 10.605  4.364   -33.708 1.00 36.14  ? 714 HOH   B O    1 
HETATM 4805 O  O    . HOH   F 3 .   ? 13.948  10.133  -37.149 1.00 47.54  ? 715 HOH   B O    1 
HETATM 4806 O  O    . HOH   F 3 .   ? 8.293   -22.635 -22.072 1.00 49.92  ? 716 HOH   B O    1 
HETATM 4807 O  O    . HOH   F 3 .   ? -6.696  12.120  -16.675 1.00 57.73  ? 717 HOH   B O    1 
HETATM 4808 O  O    . HOH   F 3 .   ? 29.889  5.305   -1.273  1.00 46.14  ? 718 HOH   B O    1 
HETATM 4809 O  O    . HOH   F 3 .   ? 6.849   20.986  -17.387 1.00 45.04  ? 719 HOH   B O    1 
HETATM 4810 O  O    . HOH   F 3 .   ? -2.955  -17.668 -25.135 1.00 35.02  ? 720 HOH   B O    1 
HETATM 4811 O  O    . HOH   F 3 .   ? 19.209  -5.515  -13.194 1.00 50.60  ? 721 HOH   B O    1 
HETATM 4812 O  O    . HOH   F 3 .   ? 4.464   5.835   -31.660 1.00 49.67  ? 722 HOH   B O    1 
HETATM 4813 O  O    . HOH   F 3 .   ? 28.686  -8.202  -25.117 1.00 36.12  ? 723 HOH   B O    1 
HETATM 4814 O  O    . HOH   F 3 .   ? 7.605   -15.383 -28.504 1.00 48.11  ? 724 HOH   B O    1 
HETATM 4815 O  O    . HOH   F 3 .   ? 1.447   17.962  -19.432 1.00 41.10  ? 725 HOH   B O    1 
HETATM 4816 O  O    . HOH   F 3 .   ? 19.543  -12.886 -19.702 1.00 53.84  ? 726 HOH   B O    1 
HETATM 4817 O  O    . HOH   F 3 .   ? -6.043  -27.447 -14.156 1.00 54.88  ? 727 HOH   B O    1 
HETATM 4818 O  O    . HOH   F 3 .   ? 17.893  -3.098  0.460   1.00 57.50  ? 728 HOH   B O    1 
HETATM 4819 O  O    . HOH   F 3 .   ? 6.954   9.339   0.276   1.00 55.49  ? 729 HOH   B O    1 
HETATM 4820 O  O    . HOH   F 3 .   ? 26.773  8.387   -14.184 1.00 52.34  ? 730 HOH   B O    1 
HETATM 4821 O  O    . HOH   F 3 .   ? 12.474  16.919  -6.242  1.00 39.05  ? 731 HOH   B O    1 
HETATM 4822 O  O    . HOH   F 3 .   ? 28.306  9.560   -19.769 1.00 46.84  ? 732 HOH   B O    1 
HETATM 4823 O  O    . HOH   F 3 .   ? 6.731   -2.827  -14.914 1.00 30.19  ? 733 HOH   B O    1 
HETATM 4824 O  O    . HOH   F 3 .   ? -0.009  7.184   -24.411 1.00 43.05  ? 734 HOH   B O    1 
HETATM 4825 O  O    . HOH   F 3 .   ? 24.032  0.539   -24.156 1.00 35.67  ? 735 HOH   B O    1 
HETATM 4826 O  O    . HOH   F 3 .   ? 3.996   -13.612 -26.823 1.00 48.13  ? 736 HOH   B O    1 
HETATM 4827 O  O    . HOH   F 3 .   ? 2.142   1.211   -9.190  1.00 44.92  ? 737 HOH   B O    1 
HETATM 4828 O  O    . HOH   F 3 .   ? 24.858  2.285   2.711   1.00 40.92  ? 738 HOH   B O    1 
HETATM 4829 O  O    . HOH   F 3 .   ? -2.950  -16.659 -28.730 1.00 35.87  ? 739 HOH   B O    1 
HETATM 4830 O  O    . HOH   F 3 .   ? 23.945  12.602  -7.954  1.00 51.27  ? 740 HOH   B O    1 
HETATM 4831 O  O    . HOH   F 3 .   ? 25.789  9.736   -27.600 1.00 36.76  ? 741 HOH   B O    1 
HETATM 4832 O  O    . HOH   F 3 .   ? 13.058  25.916  -10.429 1.00 62.40  ? 742 HOH   B O    1 
HETATM 4833 O  O    . HOH   F 3 .   ? 8.995   18.501  -24.509 1.00 47.46  ? 743 HOH   B O    1 
HETATM 4834 O  O    . HOH   F 3 .   ? 23.951  0.212   -31.486 1.00 29.62  ? 744 HOH   B O    1 
HETATM 4835 O  O    . HOH   F 3 .   ? 6.548   11.225  -29.628 1.00 34.34  ? 745 HOH   B O    1 
HETATM 4836 O  O    . HOH   F 3 .   ? 15.963  -1.251  -38.932 1.00 35.75  ? 746 HOH   B O    1 
HETATM 4837 O  O    . HOH   F 3 .   ? 20.025  10.497  -9.223  1.00 35.69  ? 747 HOH   B O    1 
HETATM 4838 O  O    . HOH   F 3 .   ? 27.614  15.972  -4.189  1.00 49.74  ? 748 HOH   B O    1 
HETATM 4839 O  O    . HOH   F 3 .   ? 8.831   14.264  -30.297 1.00 30.63  ? 749 HOH   B O    1 
HETATM 4840 O  O    . HOH   F 3 .   ? 16.496  -4.979  -37.928 1.00 42.27  ? 750 HOH   B O    1 
HETATM 4841 O  O    . HOH   F 3 .   ? 17.389  -8.600  -23.988 1.00 29.62  ? 751 HOH   B O    1 
HETATM 4842 O  O    . HOH   F 3 .   ? 3.050   12.715  -16.778 1.00 29.39  ? 752 HOH   B O    1 
HETATM 4843 O  O    . HOH   F 3 .   ? 21.011  1.132   5.706   1.00 35.43  ? 753 HOH   B O    1 
HETATM 4844 O  O    . HOH   F 3 .   ? 4.015   -1.983  -28.497 1.00 34.10  ? 754 HOH   B O    1 
HETATM 4845 O  O    . HOH   F 3 .   ? 17.863  8.695   -8.940  1.00 24.81  ? 755 HOH   B O    1 
HETATM 4846 O  O    . HOH   F 3 .   ? -5.572  -9.625  -25.447 1.00 57.62  ? 756 HOH   B O    1 
HETATM 4847 O  O    . HOH   F 3 .   ? 21.557  -14.323 -31.088 1.00 30.96  ? 757 HOH   B O    1 
HETATM 4848 O  O    . HOH   F 3 .   ? 15.615  3.860   -14.123 1.00 20.70  ? 758 HOH   B O    1 
HETATM 4849 O  O    . HOH   F 3 .   ? 9.779   9.561   -32.813 1.00 33.70  ? 759 HOH   B O    1 
HETATM 4850 O  O    . HOH   F 3 .   ? 6.474   -0.943  -29.119 1.00 27.25  ? 760 HOH   B O    1 
HETATM 4851 O  O    . HOH   F 3 .   ? 30.123  3.929   -18.531 1.00 50.29  ? 761 HOH   B O    1 
HETATM 4852 O  O    . HOH   F 3 .   ? 24.222  -9.880  -19.584 1.00 51.99  ? 762 HOH   B O    1 
HETATM 4853 O  O    . HOH   F 3 .   ? 17.849  19.385  -15.104 1.00 44.10  ? 763 HOH   B O    1 
HETATM 4854 O  O    . HOH   F 3 .   ? -1.878  -3.884  -22.495 1.00 35.26  ? 764 HOH   B O    1 
HETATM 4855 O  O    . HOH   F 3 .   ? 21.805  20.694  -24.568 1.00 32.10  ? 765 HOH   B O    1 
HETATM 4856 O  O    . HOH   F 3 .   ? 1.090   3.453   -25.704 1.00 42.39  ? 766 HOH   B O    1 
HETATM 4857 O  O    . HOH   F 3 .   ? 24.526  1.475   -33.613 1.00 34.08  ? 767 HOH   B O    1 
HETATM 4858 O  O    . HOH   F 3 .   ? 14.021  -8.474  -15.988 1.00 33.26  ? 768 HOH   B O    1 
HETATM 4859 O  O    . HOH   F 3 .   ? 21.892  15.089  -16.263 1.00 48.43  ? 769 HOH   B O    1 
HETATM 4860 O  O    . HOH   F 3 .   ? 9.514   4.991   -11.581 1.00 23.95  ? 770 HOH   B O    1 
HETATM 4861 O  O    . HOH   F 3 .   ? 10.017  5.568   -7.614  1.00 33.83  ? 771 HOH   B O    1 
HETATM 4862 O  O    . HOH   F 3 .   ? -1.525  -19.005 -34.689 1.00 40.78  ? 772 HOH   B O    1 
HETATM 4863 O  O    . HOH   F 3 .   ? 22.107  12.726  -32.003 1.00 29.85  ? 773 HOH   B O    1 
HETATM 4864 O  O    . HOH   F 3 .   ? 4.512   2.316   -31.017 1.00 49.03  ? 774 HOH   B O    1 
HETATM 4865 O  O    . HOH   F 3 .   ? 9.824   20.630  -6.538  1.00 45.60  ? 775 HOH   B O    1 
HETATM 4866 O  O    . HOH   F 3 .   ? 27.703  3.869   -12.167 1.00 44.59  ? 776 HOH   B O    1 
HETATM 4867 O  O    . HOH   F 3 .   ? 8.318   -11.378 -29.125 1.00 33.90  ? 777 HOH   B O    1 
HETATM 4868 O  O    . HOH   F 3 .   ? 16.251  -8.076  -12.176 1.00 48.37  ? 778 HOH   B O    1 
HETATM 4869 O  O    . HOH   F 3 .   ? 22.485  -2.254  -16.953 1.00 36.41  ? 779 HOH   B O    1 
HETATM 4870 O  O    . HOH   F 3 .   ? 4.532   -15.664 -28.874 1.00 35.13  ? 780 HOH   B O    1 
HETATM 4871 O  O    . HOH   F 3 .   ? 11.545  -1.270  -40.218 1.00 52.73  ? 781 HOH   B O    1 
HETATM 4872 O  O    . HOH   F 3 .   ? 9.121   1.532   -35.605 1.00 42.29  ? 782 HOH   B O    1 
HETATM 4873 O  O    . HOH   F 3 .   ? 25.396  2.472   -24.936 1.00 43.85  ? 783 HOH   B O    1 
HETATM 4874 O  O    . HOH   F 3 .   ? 3.895   18.977  -11.599 1.00 44.84  ? 784 HOH   B O    1 
HETATM 4875 O  O    . HOH   F 3 .   ? -4.518  2.309   -24.242 1.00 43.73  ? 785 HOH   B O    1 
HETATM 4876 O  O    . HOH   F 3 .   ? -0.580  -29.371 -22.217 1.00 48.40  ? 786 HOH   B O    1 
HETATM 4877 O  O    . HOH   F 3 .   ? 26.963  11.267  2.350   1.00 36.87  ? 787 HOH   B O    1 
HETATM 4878 O  O    . HOH   F 3 .   ? 4.440   9.349   -29.675 1.00 31.51  ? 788 HOH   B O    1 
HETATM 4879 O  O    . HOH   F 3 .   ? 27.154  7.263   -10.823 1.00 43.76  ? 789 HOH   B O    1 
HETATM 4880 O  O    . HOH   F 3 .   ? 20.011  -1.710  -7.349  1.00 39.88  ? 790 HOH   B O    1 
HETATM 4881 O  O    . HOH   F 3 .   ? 17.571  20.253  -11.504 1.00 43.10  ? 791 HOH   B O    1 
HETATM 4882 O  O    . HOH   F 3 .   ? 25.727  18.003  -30.110 1.00 32.34  ? 792 HOH   B O    1 
HETATM 4883 O  O    . HOH   F 3 .   ? 16.668  -10.524 -32.641 1.00 34.47  ? 793 HOH   B O    1 
HETATM 4884 O  O    . HOH   F 3 .   ? 19.729  -1.804  -35.984 1.00 45.89  ? 794 HOH   B O    1 
HETATM 4885 O  O    . HOH   F 3 .   ? 4.827   14.436  -9.789  1.00 33.93  ? 795 HOH   B O    1 
HETATM 4886 O  O    . HOH   F 3 .   ? 16.814  -8.084  -16.349 1.00 40.84  ? 796 HOH   B O    1 
HETATM 4887 O  O    . HOH   F 3 .   ? -0.732  -10.849 -26.663 1.00 47.03  ? 797 HOH   B O    1 
HETATM 4888 O  O    . HOH   F 3 .   ? 23.430  1.469   -8.324  1.00 38.00  ? 798 HOH   B O    1 
HETATM 4889 O  O    . HOH   F 3 .   ? 8.838   -11.690 -12.822 1.00 47.02  ? 799 HOH   B O    1 
HETATM 4890 O  O    . HOH   F 3 .   ? -8.139  -17.728 -25.779 1.00 56.52  ? 800 HOH   B O    1 
HETATM 4891 O  O    . HOH   F 3 .   ? 17.099  -2.637  -13.537 1.00 38.14  ? 801 HOH   B O    1 
HETATM 4892 O  O    . HOH   F 3 .   ? 19.393  17.445  -11.479 1.00 52.93  ? 802 HOH   B O    1 
HETATM 4893 O  O    . HOH   F 3 .   ? -0.792  11.757  -19.218 1.00 34.28  ? 803 HOH   B O    1 
HETATM 4894 O  O    . HOH   F 3 .   ? 21.960  -2.386  -5.728  1.00 52.31  ? 804 HOH   B O    1 
HETATM 4895 O  O    . HOH   F 3 .   ? 4.843   -7.460  -28.995 1.00 46.45  ? 805 HOH   B O    1 
HETATM 4896 O  O    . HOH   F 3 .   ? 18.316  -11.141 -23.283 1.00 42.31  ? 806 HOH   B O    1 
HETATM 4897 O  O    . HOH   F 3 .   ? 15.893  -10.881 -20.050 1.00 37.08  ? 807 HOH   B O    1 
HETATM 4898 O  O    . HOH   F 3 .   ? 6.647   14.132  -7.574  1.00 32.81  ? 808 HOH   B O    1 
HETATM 4899 O  O    . HOH   F 3 .   ? 7.749   -10.462 -7.020  1.00 67.52  ? 809 HOH   B O    1 
HETATM 4900 O  O    . HOH   F 3 .   ? -7.499  0.903   -22.523 1.00 52.05  ? 810 HOH   B O    1 
HETATM 4901 O  O    . HOH   F 3 .   ? -2.174  -5.359  -20.248 1.00 39.52  ? 811 HOH   B O    1 
HETATM 4902 O  O    . HOH   F 3 .   ? 24.678  7.742   -31.161 1.00 30.34  ? 812 HOH   B O    1 
HETATM 4903 O  O    . HOH   F 3 .   ? 23.336  0.619   3.916   1.00 34.50  ? 813 HOH   B O    1 
HETATM 4904 O  O    . HOH   F 3 .   ? 12.286  19.799  -27.804 1.00 32.15  ? 814 HOH   B O    1 
HETATM 4905 O  O    . HOH   F 3 .   ? 26.741  4.972   -28.331 1.00 40.76  ? 815 HOH   B O    1 
HETATM 4906 O  O    . HOH   F 3 .   ? 10.728  -5.697  -36.657 1.00 44.16  ? 816 HOH   B O    1 
HETATM 4907 O  O    . HOH   F 3 .   ? 14.458  -10.531 -33.958 1.00 41.44  ? 817 HOH   B O    1 
HETATM 4908 O  O    . HOH   F 3 .   ? 2.202   -29.892 -21.060 1.00 53.12  ? 818 HOH   B O    1 
HETATM 4909 O  O    . HOH   F 3 .   ? 28.503  -5.749  -28.335 1.00 44.23  ? 819 HOH   B O    1 
HETATM 4910 O  O    . HOH   F 3 .   ? 4.511   -28.709 -19.800 1.00 43.63  ? 820 HOH   B O    1 
HETATM 4911 O  O    . HOH   F 3 .   ? 21.929  7.819   -33.497 1.00 38.77  ? 821 HOH   B O    1 
HETATM 4912 O  O    . HOH   F 3 .   ? 11.248  7.629   -8.790  1.00 26.50  ? 822 HOH   B O    1 
HETATM 4913 O  O    . HOH   F 3 .   ? 27.214  0.340   -23.514 1.00 36.68  ? 823 HOH   B O    1 
HETATM 4914 O  O    . HOH   F 3 .   ? 10.136  -1.050  -37.179 1.00 39.56  ? 824 HOH   B O    1 
HETATM 4915 O  O    . HOH   F 3 .   ? 20.131  0.692   -37.180 1.00 44.32  ? 825 HOH   B O    1 
HETATM 4916 O  O    . HOH   F 3 .   ? -8.113  9.058   -10.484 1.00 61.53  ? 826 HOH   B O    1 
HETATM 4917 O  O    . HOH   F 3 .   ? 28.095  -2.026  -20.542 1.00 44.28  ? 827 HOH   B O    1 
HETATM 4918 O  O    . HOH   F 3 .   ? 7.684   -5.634  -12.016 1.00 49.84  ? 828 HOH   B O    1 
HETATM 4919 O  O    . HOH   F 3 .   ? 1.422   13.292  -18.881 1.00 35.53  ? 829 HOH   B O    1 
HETATM 4920 O  O    . HOH   F 3 .   ? 9.897   1.281   16.356  1.00 29.27  ? 830 HOH   B O    1 
HETATM 4921 O  O    . HOH   F 3 .   ? 10.079  -2.661  11.882  1.00 55.36  ? 831 HOH   B O    1 
HETATM 4922 O  O    . HOH   F 3 .   ? 13.609  -13.538 -22.844 1.00 43.57  ? 832 HOH   B O    1 
HETATM 4923 O  O    . HOH   F 3 .   ? 6.060   -2.103  -31.810 1.00 38.99  ? 833 HOH   B O    1 
HETATM 4924 O  O    . HOH   F 3 .   ? 25.329  -3.332  0.551   1.00 48.73  ? 834 HOH   B O    1 
HETATM 4925 O  O    . HOH   F 3 .   ? 28.988  -8.331  -19.511 1.00 61.18  ? 835 HOH   B O    1 
HETATM 4926 O  O    . HOH   F 3 .   ? 37.203  9.773   -19.831 1.00 54.19  ? 836 HOH   B O    1 
HETATM 4927 O  O    . HOH   F 3 .   ? 18.749  2.248   6.008   1.00 48.50  ? 837 HOH   B O    1 
HETATM 4928 O  O    . HOH   F 3 .   ? 12.182  -3.645  10.678  1.00 50.12  ? 838 HOH   B O    1 
HETATM 4929 O  O    . HOH   F 3 .   ? 5.986   15.667  -5.617  1.00 38.80  ? 839 HOH   B O    1 
HETATM 4930 O  O    . HOH   F 3 .   ? 12.964  -0.482  3.408   1.00 53.45  ? 840 HOH   B O    1 
HETATM 4931 O  O    . HOH   F 3 .   ? 5.754   -30.034 -21.902 1.00 45.51  ? 841 HOH   B O    1 
HETATM 4932 O  O    . HOH   F 3 .   ? 29.980  -6.556  -22.445 1.00 49.31  ? 842 HOH   B O    1 
HETATM 4933 O  O    . HOH   F 3 .   ? 10.090  -28.764 -31.571 1.00 40.87  ? 843 HOH   B O    1 
HETATM 4934 O  O    . HOH   F 3 .   ? 15.157  -1.122  3.456   1.00 51.24  ? 844 HOH   B O    1 
HETATM 4935 O  O    . HOH   F 3 .   ? 28.774  8.448   -22.140 1.00 50.29  ? 845 HOH   B O    1 
HETATM 4936 O  O    . HOH   F 3 .   ? 7.297   -3.099  -33.723 1.00 50.57  ? 846 HOH   B O    1 
HETATM 4937 O  O    . HOH   F 3 .   ? -1.904  12.924  -17.018 1.00 49.23  ? 847 HOH   B O    1 
HETATM 4938 O  O    . HOH   F 3 .   ? 28.777  -3.244  -23.756 1.00 36.35  ? 848 HOH   B O    1 
HETATM 4939 O  O    . HOH   F 3 .   ? 12.027  -13.461 -14.911 1.00 53.17  ? 849 HOH   B O    1 
HETATM 4940 O  O    . HOH   F 3 .   ? 28.428  21.755  -25.000 1.00 52.54  ? 850 HOH   B O    1 
HETATM 4941 O  O    . HOH   F 3 .   ? 0.211   15.833  -18.525 1.00 46.35  ? 851 HOH   B O    1 
HETATM 4942 O  O    . HOH   F 3 .   ? 27.462  13.966  -30.090 1.00 44.92  ? 852 HOH   B O    1 
HETATM 4943 O  O    . HOH   F 3 .   ? 8.850   4.809   -5.287  1.00 42.10  ? 853 HOH   B O    1 
HETATM 4944 O  O    . HOH   F 3 .   ? 37.151  8.713   -23.159 1.00 50.25  ? 854 HOH   B O    1 
HETATM 4945 O  O    . HOH   F 3 .   ? 13.875  -9.179  -13.505 1.00 51.30  ? 855 HOH   B O    1 
HETATM 4946 O  O    . HOH   F 3 .   ? 22.379  -7.379  7.587   1.00 41.94  ? 856 HOH   B O    1 
HETATM 4947 O  O    . HOH   F 3 .   ? -14.097 -29.422 -20.413 1.00 47.68  ? 857 HOH   B O    1 
HETATM 4948 O  O    . HOH   F 3 .   ? 18.223  -3.056  -38.392 1.00 37.00  ? 858 HOH   B O    1 
HETATM 4949 O  O    . HOH   F 3 .   ? 11.945  27.114  -12.245 1.00 56.54  ? 859 HOH   B O    1 
HETATM 4950 O  O    . HOH   F 3 .   ? 1.358   2.656   -30.037 1.00 47.64  ? 860 HOH   B O    1 
HETATM 4951 O  O    . HOH   F 3 .   ? 0.279   3.852   -28.318 1.00 48.96  ? 861 HOH   B O    1 
HETATM 4952 O  O    . HOH   F 3 .   ? 17.709  -12.995 -32.134 1.00 45.05  ? 862 HOH   B O    1 
HETATM 4953 O  O    . HOH   F 3 .   ? -0.697  13.753  -14.934 1.00 50.81  ? 863 HOH   B O    1 
HETATM 4954 O  O    . HOH   F 3 .   ? 0.761   19.273  -21.624 1.00 48.28  ? 864 HOH   B O    1 
HETATM 4955 O  O    . HOH   F 3 .   ? 6.166   -9.946  -29.291 1.00 49.23  ? 865 HOH   B O    1 
HETATM 4956 O  O    . HOH   F 3 .   ? 9.503   19.034  -5.021  1.00 51.15  ? 866 HOH   B O    1 
HETATM 4957 O  O    . HOH   F 3 .   ? 25.604  14.143  5.790   1.00 50.41  ? 867 HOH   B O    1 
HETATM 4958 O  O    . HOH   F 3 .   ? -6.193  -27.167 -30.571 1.00 35.57  ? 868 HOH   B O    1 
HETATM 4959 O  O    . HOH   F 3 .   ? 9.860   -3.542  15.610  1.00 44.87  ? 869 HOH   B O    1 
HETATM 4960 O  O    . HOH   F 3 .   ? 0.846   16.759  -15.870 1.00 47.54  ? 870 HOH   B O    1 
HETATM 4961 O  O    . HOH   F 3 .   ? 8.865   -1.108  16.281  1.00 38.14  ? 871 HOH   B O    1 
HETATM 4962 O  O    . HOH   F 3 .   ? 2.238   10.214  -28.621 1.00 44.86  ? 872 HOH   B O    1 
HETATM 4963 O  O    . HOH   F 3 .   ? 12.810  -13.219 -17.265 1.00 45.94  ? 873 HOH   B O    1 
HETATM 4964 O  O    . HOH   F 3 .   ? 15.434  -13.580 -21.139 1.00 54.43  ? 874 HOH   B O    1 
HETATM 4965 O  O    . HOH   F 3 .   ? 4.700   0.049   -32.846 1.00 59.17  ? 875 HOH   B O    1 
HETATM 4966 O  O    . HOH   F 3 .   ? 3.366   16.650  -10.498 1.00 46.19  ? 876 HOH   B O    1 
HETATM 4967 O  O    . HOH   F 3 .   ? 22.510  10.449  -33.670 1.00 36.51  ? 877 HOH   B O    1 
HETATM 4968 O  O    . HOH   F 3 .   ? 22.847  -3.940  -14.812 1.00 38.84  ? 878 HOH   B O    1 
HETATM 4969 O  O    . HOH   F 3 .   ? 7.239   -0.684  -35.331 1.00 60.75  ? 879 HOH   B O    1 
HETATM 4970 O  O    . HOH   F 3 .   ? 2.191   15.780  -12.376 1.00 46.47  ? 880 HOH   B O    1 
HETATM 4971 O  O    . HOH   F 3 .   ? 2.220   14.679  -15.048 1.00 38.45  ? 881 HOH   B O    1 
HETATM 4972 O  O    . HOH   F 3 .   ? 27.050  -3.186  2.646   1.00 48.31  ? 882 HOH   B O    1 
HETATM 4973 O  O    . HOH   F 3 .   ? -7.498  -19.959 -32.095 1.00 40.85  ? 883 HOH   B O    1 
HETATM 4974 O  O    . HOH   F 3 .   ? -3.778  -17.156 -33.999 1.00 43.14  ? 884 HOH   B O    1 
HETATM 4975 O  O    . HOH   F 3 .   ? -6.061  -17.826 -33.273 1.00 49.64  ? 885 HOH   B O    1 
HETATM 4976 O  O    . HOH   F 3 .   ? 14.611  3.965   0.239   1.00 50.63  ? 886 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   . SER A 238 ? 1.1944 1.0614 0.5189 0.0362  0.1512  -0.0040 249 SER A N   
2    C CA  . SER A 238 ? 1.3145 1.1899 0.6690 0.0485  0.1390  0.0264  249 SER A CA  
3    C C   . SER A 238 ? 1.2465 1.1371 0.6371 0.0503  0.1136  0.0248  249 SER A C   
4    O O   . SER A 238 ? 1.1382 1.0201 0.5750 0.0527  0.1166  0.0142  249 SER A O   
5    C CB  . SER A 238 ? 1.3485 1.2355 0.6591 0.0521  0.1322  0.0544  249 SER A CB  
6    N N   . ASP A 239 ? 1.1583 1.0762 0.5283 0.0493  0.0885  0.0370  250 ASP A N   
7    C CA  . ASP A 239 ? 1.1447 1.0840 0.5474 0.0495  0.0643  0.0353  250 ASP A CA  
8    C C   . ASP A 239 ? 1.1771 1.1132 0.5814 0.0322  0.0619  -0.0002 250 ASP A C   
9    O O   . ASP A 239 ? 1.1400 1.0756 0.5869 0.0327  0.0556  -0.0087 250 ASP A O   
10   C CB  . ASP A 239 ? 1.1479 1.1263 0.5292 0.0528  0.0383  0.0592  250 ASP A CB  
11   N N   . GLU A 240 ? 1.2160 1.1461 0.5713 0.0163  0.0688  -0.0212 251 GLU A N   
12   C CA  . GLU A 240 ? 1.1571 1.0697 0.5098 0.0003  0.0746  -0.0568 251 GLU A CA  
13   C C   . GLU A 240 ? 1.1277 1.0061 0.5180 0.0102  0.1010  -0.0680 251 GLU A C   
14   O O   . GLU A 240 ? 0.9825 0.8473 0.3973 0.0057  0.1029  -0.0875 251 GLU A O   
15   C CB  . GLU A 240 ? 1.2465 1.1534 0.5322 -0.0193 0.0807  -0.0783 251 GLU A CB  
16   C CG  . GLU A 240 ? 1.4377 1.3858 0.6841 -0.0357 0.0509  -0.0730 251 GLU A CG  
17   C CD  . GLU A 240 ? 1.4981 1.4751 0.7254 -0.0226 0.0411  -0.0363 251 GLU A CD  
18   O OE1 . GLU A 240 ? 1.4377 1.3935 0.6530 -0.0105 0.0633  -0.0252 251 GLU A OE1 
19   O OE2 . GLU A 240 ? 1.5284 1.5505 0.7538 -0.0237 0.0122  -0.0167 251 GLU A OE2 
20   N N   . GLU A 241 ? 1.0118 0.8789 0.4078 0.0232  0.1213  -0.0541 252 GLU A N   
21   C CA  . GLU A 241 ? 1.0970 0.9432 0.5324 0.0327  0.1448  -0.0608 252 GLU A CA  
22   C C   . GLU A 241 ? 0.9374 0.7894 0.4314 0.0406  0.1333  -0.0533 252 GLU A C   
23   O O   . GLU A 241 ? 0.9035 0.7436 0.4272 0.0420  0.1410  -0.0681 252 GLU A O   
24   C CB  . GLU A 241 ? 1.1419 0.9836 0.5730 0.0413  0.1664  -0.0448 252 GLU A CB  
25   C CG  . GLU A 241 ? 1.2306 1.0643 0.7100 0.0509  0.1870  -0.0452 252 GLU A CG  
26   C CD  . GLU A 241 ? 1.3571 1.1790 0.8209 0.0525  0.2184  -0.0575 252 GLU A CD  
27   O OE1 . GLU A 241 ? 1.3925 1.2101 0.8055 0.0470  0.2274  -0.0600 252 GLU A OE1 
28   O OE2 . GLU A 241 ? 1.2190 1.0388 0.7217 0.0603  0.2346  -0.0633 252 GLU A OE2 
29   N N   . ILE A 242 ? 0.9169 0.7856 0.4268 0.0470  0.1167  -0.0292 253 ILE A N   
30   C CA  . ILE A 242 ? 0.7927 0.6653 0.3544 0.0540  0.1080  -0.0227 253 ILE A CA  
31   C C   . ILE A 242 ? 0.8043 0.6854 0.3768 0.0461  0.0899  -0.0375 253 ILE A C   
32   O O   . ILE A 242 ? 0.7322 0.6096 0.3448 0.0490  0.0891  -0.0423 253 ILE A O   
33   C CB  . ILE A 242 ? 0.8398 0.7210 0.4121 0.0641  0.0995  0.0061  253 ILE A CB  
34   C CG1 . ILE A 242 ? 0.9726 0.8503 0.5956 0.0709  0.0989  0.0109  253 ILE A CG1 
35   C CG2 . ILE A 242 ? 1.0358 0.9409 0.5871 0.0642  0.0757  0.0185  253 ILE A CG2 
36   C CD1 . ILE A 242 ? 1.0120 0.8754 0.6564 0.0718  0.1209  0.0090  253 ILE A CD1 
37   N N   . LEU A 243 ? 0.8078 0.7025 0.3440 0.0339  0.0752  -0.0447 254 LEU A N   
38   C CA  . LEU A 243 ? 0.9033 0.8056 0.4465 0.0208  0.0602  -0.0618 254 LEU A CA  
39   C C   . LEU A 243 ? 0.8244 0.6944 0.3715 0.0147  0.0792  -0.0889 254 LEU A C   
40   O O   . LEU A 243 ? 0.7818 0.6459 0.3628 0.0141  0.0768  -0.0962 254 LEU A O   
41   C CB  . LEU A 243 ? 0.8516 0.7793 0.3506 0.0041  0.0409  -0.0655 254 LEU A CB  
42   C CG  . LEU A 243 ? 0.8653 0.7954 0.3604 -0.0178 0.0301  -0.0905 254 LEU A CG  
43   C CD1 . LEU A 243 ? 0.8159 0.7645 0.3627 -0.0140 0.0146  -0.0822 254 LEU A CD1 
44   C CD2 . LEU A 243 ? 0.9212 0.8780 0.3646 -0.0402 0.0127  -0.0980 254 LEU A CD2 
45   N N   . GLU A 244 ? 0.8509 0.6983 0.3631 0.0120  0.1005  -0.1026 255 GLU A N   
46   C CA  . GLU A 244 ? 0.8626 0.6755 0.3786 0.0112  0.1232  -0.1258 255 GLU A CA  
47   C C   . GLU A 244 ? 0.8115 0.6187 0.3811 0.0298  0.1361  -0.1157 255 GLU A C   
48   O O   . GLU A 244 ? 0.8041 0.5918 0.3949 0.0322  0.1461  -0.1278 255 GLU A O   
49   C CB  . GLU A 244 ? 0.9200 0.7101 0.3878 0.0077  0.1472  -0.1410 255 GLU A CB  
50   C CG  . GLU A 244 ? 0.9847 0.7700 0.3923 -0.0164 0.1397  -0.1620 255 GLU A CG  
51   C CD  . GLU A 244 ? 1.0391 0.8124 0.4478 -0.0349 0.1297  -0.1836 255 GLU A CD  
52   O OE1 . GLU A 244 ? 0.9792 0.7291 0.4241 -0.0274 0.1409  -0.1901 255 GLU A OE1 
53   O OE2 . GLU A 244 ? 1.1026 0.8925 0.4750 -0.0584 0.1099  -0.1929 255 GLU A OE2 
54   N N   . LYS A 245 ? 0.7804 0.6042 0.3707 0.0420  0.1365  -0.0930 256 LYS A N   
55   C CA  . LYS A 245 ? 0.7322 0.5582 0.3729 0.0551  0.1444  -0.0831 256 LYS A CA  
56   C C   . LYS A 245 ? 0.7342 0.5675 0.4103 0.0543  0.1265  -0.0811 256 LYS A C   
57   O O   . LYS A 245 ? 0.6714 0.4971 0.3789 0.0602  0.1343  -0.0852 256 LYS A O   
58   C CB  . LYS A 245 ? 0.8098 0.6501 0.4600 0.0621  0.1473  -0.0611 256 LYS A CB  
59   C CG  . LYS A 245 ? 0.7779 0.6264 0.4772 0.0703  0.1518  -0.0505 256 LYS A CG  
60   C CD  . LYS A 245 ? 0.9316 0.7762 0.6494 0.0777  0.1747  -0.0582 256 LYS A CD  
61   C CE  . LYS A 245 ? 1.0244 0.8839 0.7921 0.0835  0.1737  -0.0489 256 LYS A CE  
62   N NZ  . LYS A 245 ? 1.0078 0.8814 0.7879 0.0798  0.1678  -0.0318 256 LYS A NZ  
63   N N   . LEU A 246 ? 0.6883 0.5387 0.3597 0.0481  0.1034  -0.0735 257 LEU A N   
64   C CA  . LEU A 246 ? 0.6563 0.5156 0.3593 0.0464  0.0876  -0.0725 257 LEU A CA  
65   C C   . LEU A 246 ? 0.6744 0.5159 0.3731 0.0358  0.0904  -0.0946 257 LEU A C   
66   O O   . LEU A 246 ? 0.6486 0.4834 0.3796 0.0390  0.0924  -0.0966 257 LEU A O   
67   C CB  . LEU A 246 ? 0.6532 0.5391 0.3518 0.0435  0.0642  -0.0589 257 LEU A CB  
68   C CG  . LEU A 246 ? 0.6336 0.5338 0.3653 0.0416  0.0485  -0.0568 257 LEU A CG  
69   C CD1 . LEU A 246 ? 0.6093 0.5033 0.3827 0.0531  0.0561  -0.0491 257 LEU A CD1 
70   C CD2 . LEU A 246 ? 0.6775 0.6095 0.4068 0.0432  0.0279  -0.0395 257 LEU A CD2 
71   N N   . ARG A 247 ? 0.7240 0.5556 0.3799 0.0215  0.0911  -0.1114 258 ARG A N   
72   C CA  . ARG A 247 ? 0.8330 0.6398 0.4788 0.0076  0.0962  -0.1348 258 ARG A CA  
73   C C   . ARG A 247 ? 0.8006 0.5734 0.4629 0.0202  0.1232  -0.1423 258 ARG A C   
74   O O   . ARG A 247 ? 0.7524 0.5061 0.4307 0.0172  0.1271  -0.1511 258 ARG A O   
75   C CB  . ARG A 247 ? 0.8158 0.6140 0.4050 -0.0130 0.0956  -0.1543 258 ARG A CB  
76   C CG  . ARG A 247 ? 0.8225 0.6616 0.3941 -0.0270 0.0667  -0.1461 258 ARG A CG  
77   C CD  . ARG A 247 ? 0.8905 0.7240 0.4038 -0.0530 0.0643  -0.1686 258 ARG A CD  
78   N NE  . ARG A 247 ? 0.9197 0.7265 0.4255 -0.0747 0.0681  -0.1948 258 ARG A NE  
79   C CZ  . ARG A 247 ? 0.9647 0.7188 0.4458 -0.0800 0.0954  -0.2198 258 ARG A CZ  
80   N NH1 . ARG A 247 ? 0.9846 0.7123 0.4468 -0.0647 0.1208  -0.2224 258 ARG A NH1 
81   N NH2 . ARG A 247 ? 0.9950 0.7206 0.4696 -0.1009 0.0993  -0.2422 258 ARG A NH2 
82   N N   . SER A 248 ? 0.7528 0.5213 0.4150 0.0355  0.1422  -0.1360 259 SER A N   
83   C CA  . SER A 248 ? 0.7585 0.5019 0.4375 0.0505  0.1692  -0.1404 259 SER A CA  
84   C C   . SER A 248 ? 0.7069 0.4612 0.4390 0.0632  0.1661  -0.1259 259 SER A C   
85   O O   . SER A 248 ? 0.7138 0.4470 0.4619 0.0742  0.1843  -0.1292 259 SER A O   
86   C CB  . SER A 248 ? 0.7680 0.5152 0.4387 0.0634  0.1893  -0.1343 259 SER A CB  
87   O OG  . SER A 248 ? 0.7857 0.5664 0.4882 0.0720  0.1805  -0.1114 259 SER A OG  
88   N N   . ILE A 249 ? 0.6593 0.4446 0.4170 0.0629  0.1449  -0.1093 260 ILE A N   
89   C CA  . ILE A 249 ? 0.6142 0.4116 0.4175 0.0732  0.1425  -0.0961 260 ILE A CA  
90   C C   . ILE A 249 ? 0.6063 0.3976 0.4212 0.0643  0.1295  -0.1009 260 ILE A C   
91   O O   . ILE A 249 ? 0.6341 0.4358 0.4837 0.0711  0.1257  -0.0899 260 ILE A O   
92   C CB  . ILE A 249 ? 0.6389 0.4678 0.4637 0.0777  0.1319  -0.0767 260 ILE A CB  
93   C CG1 . ILE A 249 ? 0.5636 0.4062 0.3792 0.0676  0.1092  -0.0723 260 ILE A CG1 
94   C CG2 . ILE A 249 ? 0.6379 0.4734 0.4529 0.0838  0.1466  -0.0713 260 ILE A CG2 
95   C CD1 . ILE A 249 ? 0.6292 0.4924 0.4650 0.0724  0.1017  -0.0542 260 ILE A CD1 
96   N N   . VAL A 250 ? 0.6388 0.4180 0.4250 0.0469  0.1213  -0.1161 261 VAL A N   
97   C CA  . VAL A 250 ? 0.6828 0.4585 0.4784 0.0341  0.1093  -0.1217 261 VAL A CA  
98   C C   . VAL A 250 ? 0.7451 0.4768 0.5165 0.0241  0.1262  -0.1434 261 VAL A C   
99   O O   . VAL A 250 ? 0.7381 0.4499 0.4695 0.0157  0.1359  -0.1596 261 VAL A O   
100  C CB  . VAL A 250 ? 0.6321 0.4379 0.4175 0.0184  0.0839  -0.1200 261 VAL A CB  
101  C CG1 . VAL A 250 ? 0.7238 0.5328 0.5243 0.0042  0.0723  -0.1244 261 VAL A CG1 
102  C CG2 . VAL A 250 ? 0.5910 0.4297 0.3948 0.0309  0.0727  -0.0985 261 VAL A CG2 
103  N N   A SER A 251 ? 0.6877 0.4009 0.4800 0.0244  0.1316  -0.1441 262 SER A N   
104  N N   B SER A 251 ? 0.6879 0.4010 0.4800 0.0243  0.1317  -0.1441 262 SER A N   
105  C CA  A SER A 251 ? 0.7616 0.4247 0.5300 0.0133  0.1498  -0.1646 262 SER A CA  
106  C CA  B SER A 251 ? 0.7620 0.4248 0.5296 0.0134  0.1501  -0.1648 262 SER A CA  
107  C C   A SER A 251 ? 0.7807 0.4428 0.5172 -0.0199 0.1347  -0.1840 262 SER A C   
108  C C   B SER A 251 ? 0.7808 0.4427 0.5173 -0.0198 0.1348  -0.1839 262 SER A C   
109  O O   A SER A 251 ? 0.7500 0.4527 0.5000 -0.0317 0.1090  -0.1766 262 SER A O   
110  O O   B SER A 251 ? 0.7498 0.4520 0.5004 -0.0315 0.1093  -0.1765 262 SER A O   
111  C CB  A SER A 251 ? 0.7842 0.4274 0.5838 0.0227  0.1597  -0.1564 262 SER A CB  
112  C CB  B SER A 251 ? 0.7856 0.4266 0.5836 0.0237  0.1615  -0.1570 262 SER A CB  
113  O OG  A SER A 251 ? 0.7449 0.3910 0.5715 0.0524  0.1750  -0.1389 262 SER A OG  
114  O OG  B SER A 251 ? 0.8035 0.3867 0.5751 0.0136  0.1833  -0.1767 262 SER A OG  
115  N N   . VAL A 252 ? 0.8495 0.4667 0.5429 -0.0354 0.1518  -0.2089 263 VAL A N   
116  C CA  . VAL A 252 ? 0.8943 0.5084 0.5528 -0.0725 0.1393  -0.2308 263 VAL A CA  
117  C C   . VAL A 252 ? 0.9584 0.5409 0.6281 -0.0876 0.1455  -0.2387 263 VAL A C   
118  O O   . VAL A 252 ? 1.0734 0.5974 0.7374 -0.0793 0.1746  -0.2464 263 VAL A O   
119  C CB  . VAL A 252 ? 0.9683 0.5465 0.5674 -0.0871 0.1556  -0.2571 263 VAL A CB  
120  C CG1 . VAL A 252 ? 1.0316 0.5886 0.5923 -0.1294 0.1511  -0.2852 263 VAL A CG1 
121  C CG2 . VAL A 252 ? 0.9527 0.5742 0.5353 -0.0825 0.1409  -0.2493 263 VAL A CG2 
122  N N   . GLY A 253 ? 0.8895 0.5109 0.5765 -0.1082 0.1199  -0.2347 264 GLY A N   
123  C CA  . GLY A 253 ? 1.0061 0.6013 0.7038 -0.1264 0.1251  -0.2415 264 GLY A CA  
124  C C   . GLY A 253 ? 0.9721 0.6238 0.6864 -0.1524 0.0943  -0.2378 264 GLY A C   
125  O O   . GLY A 253 ? 0.8468 0.5595 0.5699 -0.1502 0.0692  -0.2258 264 GLY A O   
126  N N   . ASP A 254 ? 0.9365 0.5676 0.6584 -0.1745 0.0985  -0.2454 265 ASP A N   
127  C CA  . ASP A 254 ? 0.8884 0.5729 0.6305 -0.2014 0.0728  -0.2421 265 ASP A CA  
128  C C   . ASP A 254 ? 0.8439 0.5573 0.6408 -0.1782 0.0669  -0.2144 265 ASP A C   
129  O O   . ASP A 254 ? 0.8612 0.5313 0.6721 -0.1690 0.0866  -0.2104 265 ASP A O   
130  C CB  . ASP A 254 ? 0.9598 0.6058 0.6749 -0.2456 0.0818  -0.2688 265 ASP A CB  
131  C CG  . ASP A 254 ? 0.9964 0.7059 0.7327 -0.2781 0.0548  -0.2665 265 ASP A CG  
132  O OD1 . ASP A 254 ? 0.8933 0.6733 0.6699 -0.2616 0.0318  -0.2418 265 ASP A OD1 
133  O OD2 . ASP A 254 ? 1.1030 0.7910 0.8153 -0.3214 0.0585  -0.2898 265 ASP A OD2 
134  N N   . PRO A 255 ? 0.7943 0.5772 0.6212 -0.1670 0.0421  -0.1943 266 PRO A N   
135  C CA  . PRO A 255 ? 0.7138 0.5217 0.5887 -0.1468 0.0385  -0.1702 266 PRO A CA  
136  C C   . PRO A 255 ? 0.7268 0.5314 0.6183 -0.1715 0.0401  -0.1735 266 PRO A C   
137  O O   . PRO A 255 ? 0.7185 0.5192 0.6410 -0.1558 0.0470  -0.1576 266 PRO A O   
138  C CB  . PRO A 255 ? 0.6721 0.5517 0.5669 -0.1355 0.0133  -0.1525 266 PRO A CB  
139  C CG  . PRO A 255 ? 0.6977 0.5863 0.5555 -0.1425 0.0052  -0.1631 266 PRO A CG  
140  C CD  . PRO A 255 ? 0.7897 0.6309 0.6060 -0.1738 0.0175  -0.1922 266 PRO A CD  
141  N N   . LYS A 256 ? 0.7669 0.5738 0.6367 -0.2120 0.0344  -0.1939 267 LYS A N   
142  C CA  . LYS A 256 ? 0.8241 0.6266 0.7066 -0.2421 0.0373  -0.1993 267 LYS A CA  
143  C C   . LYS A 256 ? 0.8374 0.5571 0.7093 -0.2415 0.0684  -0.2063 267 LYS A C   
144  O O   . LYS A 256 ? 0.9145 0.6263 0.8022 -0.2601 0.0740  -0.2050 267 LYS A O   
145  C CB  . LYS A 256 ? 0.8397 0.6668 0.6977 -0.2910 0.0234  -0.2217 267 LYS A CB  
146  C CG  . LYS A 256 ? 0.8032 0.7258 0.6813 -0.2960 -0.0093 -0.2096 267 LYS A CG  
147  C CD  . LYS A 256 ? 1.0366 0.9867 0.8885 -0.3483 -0.0234 -0.2323 267 LYS A CD  
148  C CE  . LYS A 256 ? 1.1837 1.2389 1.0604 -0.3521 -0.0568 -0.2158 267 LYS A CE  
149  N NZ  . LYS A 256 ? 1.0731 1.1657 0.9268 -0.4073 -0.0729 -0.2369 267 LYS A NZ  
150  N N   . LYS A 257 ? 0.9073 0.5662 0.7542 -0.2200 0.0902  -0.2118 268 LYS A N   
151  C CA  . LYS A 257 ? 1.1036 0.6872 0.9458 -0.2136 0.1209  -0.2125 268 LYS A CA  
152  C C   . LYS A 257 ? 1.0653 0.6618 0.9500 -0.1789 0.1239  -0.1822 268 LYS A C   
153  O O   . LYS A 257 ? 1.0760 0.6340 0.9688 -0.1810 0.1412  -0.1762 268 LYS A O   
154  C CB  . LYS A 257 ? 1.0216 0.5353 0.8253 -0.1997 0.1472  -0.2265 268 LYS A CB  
155  C CG  . LYS A 257 ? 1.3120 0.7832 1.0631 -0.2400 0.1561  -0.2618 268 LYS A CG  
156  C CD  . LYS A 257 ? 1.4618 0.8725 1.1865 -0.2145 0.1851  -0.2639 268 LYS A CD  
157  C CE  . LYS A 257 ? 1.4579 0.8509 1.1353 -0.2436 0.1884  -0.2897 268 LYS A CE  
158  N NZ  . LYS A 257 ? 1.5895 0.9343 1.2445 -0.2156 0.2154  -0.2901 268 LYS A NZ  
159  N N   . LYS A 258 ? 0.7671 0.4137 0.6757 -0.1482 0.1087  -0.1631 269 LYS A N   
160  C CA  . LYS A 258 ? 0.7164 0.3784 0.6609 -0.1189 0.1104  -0.1364 269 LYS A CA  
161  C C   . LYS A 258 ? 0.7978 0.5251 0.7760 -0.1256 0.0889  -0.1232 269 LYS A C   
162  O O   . LYS A 258 ? 0.6807 0.4134 0.6842 -0.1132 0.0932  -0.1053 269 LYS A O   
163  C CB  . LYS A 258 ? 0.7003 0.3694 0.6489 -0.0812 0.1119  -0.1237 269 LYS A CB  
164  C CG  . LYS A 258 ? 0.7357 0.4170 0.7150 -0.0524 0.1154  -0.0979 269 LYS A CG  
165  C CD  . LYS A 258 ? 0.7411 0.4280 0.7218 -0.0208 0.1187  -0.0880 269 LYS A CD  
166  C CE  . LYS A 258 ? 0.8222 0.5272 0.8309 0.0032  0.1201  -0.0633 269 LYS A CE  
167  N NZ  . LYS A 258 ? 0.8699 0.5893 0.8823 0.0296  0.1214  -0.0536 269 LYS A NZ  
168  N N   . TYR A 259 ? 0.6561 0.4343 0.6349 -0.1441 0.0672  -0.1304 270 TYR A N   
169  C CA  . TYR A 259 ? 0.6084 0.4532 0.6216 -0.1438 0.0485  -0.1154 270 TYR A CA  
170  C C   . TYR A 259 ? 0.6385 0.5174 0.6540 -0.1828 0.0358  -0.1267 270 TYR A C   
171  O O   . TYR A 259 ? 0.6761 0.5466 0.6627 -0.2092 0.0320  -0.1470 270 TYR A O   
172  C CB  . TYR A 259 ? 0.5616 0.4512 0.5828 -0.1186 0.0328  -0.1041 270 TYR A CB  
173  C CG  . TYR A 259 ? 0.5653 0.4306 0.5879 -0.0843 0.0437  -0.0924 270 TYR A CG  
174  C CD1 . TYR A 259 ? 0.5009 0.3748 0.5493 -0.0658 0.0479  -0.0743 270 TYR A CD1 
175  C CD2 . TYR A 259 ? 0.5508 0.3867 0.5480 -0.0725 0.0508  -0.0997 270 TYR A CD2 
176  C CE1 . TYR A 259 ? 0.4805 0.3392 0.5299 -0.0387 0.0562  -0.0639 270 TYR A CE1 
177  C CE2 . TYR A 259 ? 0.5309 0.3526 0.5329 -0.0434 0.0603  -0.0880 270 TYR A CE2 
178  C CZ  . TYR A 259 ? 0.5596 0.3945 0.5879 -0.0278 0.0619  -0.0702 270 TYR A CZ  
179  O OH  . TYR A 259 ? 0.5025 0.3306 0.5355 -0.0030 0.0694  -0.0586 270 TYR A OH  
180  N N   . THR A 260 ? 0.6054 0.5271 0.6552 -0.1872 0.0295  -0.1132 271 THR A N   
181  C CA  . THR A 260 ? 0.6213 0.5900 0.6832 -0.2233 0.0166  -0.1194 271 THR A CA  
182  C C   . THR A 260 ? 0.5669 0.6108 0.6711 -0.2076 0.0021  -0.0974 271 THR A C   
183  O O   . THR A 260 ? 0.5329 0.5840 0.6502 -0.1714 0.0029  -0.0810 271 THR A O   
184  C CB  . THR A 260 ? 0.6681 0.5939 0.7255 -0.2546 0.0336  -0.1292 271 THR A CB  
185  O OG1 . THR A 260 ? 0.6942 0.6665 0.7584 -0.2971 0.0204  -0.1396 271 THR A OG1 
186  C CG2 . THR A 260 ? 0.6391 0.5592 0.7257 -0.2358 0.0460  -0.1087 271 THR A CG2 
187  N N   . ARG A 261 ? 0.5737 0.6746 0.6987 -0.2359 -0.0101 -0.0976 272 ARG A N   
188  C CA  . ARG A 261 ? 0.5293 0.7049 0.6978 -0.2219 -0.0208 -0.0761 272 ARG A CA  
189  C C   . ARG A 261 ? 0.5258 0.7427 0.6991 -0.1901 -0.0355 -0.0634 272 ARG A C   
190  O O   . ARG A 261 ? 0.5319 0.7694 0.7291 -0.1579 -0.0331 -0.0443 272 ARG A O   
191  C CB  . ARG A 261 ? 0.5132 0.6707 0.7041 -0.2018 -0.0039 -0.0609 272 ARG A CB  
192  C CG  . ARG A 261 ? 0.6433 0.7895 0.8457 -0.2312 0.0083  -0.0636 272 ARG A CG  
193  C CD  . ARG A 261 ? 0.6740 0.8226 0.9011 -0.2047 0.0206  -0.0437 272 ARG A CD  
194  N NE  . ARG A 261 ? 0.6810 0.8234 0.9224 -0.2281 0.0340  -0.0411 272 ARG A NE  
195  C CZ  . ARG A 261 ? 0.8035 0.9645 1.0701 -0.2133 0.0434  -0.0238 272 ARG A CZ  
196  N NH1 . ARG A 261 ? 0.7365 0.9214 1.0156 -0.1768 0.0415  -0.0096 272 ARG A NH1 
197  N NH2 . ARG A 261 ? 0.9100 1.0624 1.1865 -0.2373 0.0567  -0.0214 272 ARG A NH2 
198  N N   . PHE A 262 ? 0.5341 0.7586 0.6812 -0.1993 -0.0487 -0.0740 273 PHE A N   
199  C CA  . PHE A 262 ? 0.4897 0.7514 0.6386 -0.1702 -0.0619 -0.0601 273 PHE A CA  
200  C C   . PHE A 262 ? 0.4678 0.8183 0.6580 -0.1657 -0.0765 -0.0399 273 PHE A C   
201  O O   . PHE A 262 ? 0.4881 0.8907 0.6906 -0.1980 -0.0891 -0.0437 273 PHE A O   
202  C CB  . PHE A 262 ? 0.5233 0.7763 0.6321 -0.1841 -0.0727 -0.0754 273 PHE A CB  
203  C CG  . PHE A 262 ? 0.5378 0.7099 0.6087 -0.1741 -0.0569 -0.0894 273 PHE A CG  
204  C CD1 . PHE A 262 ? 0.6218 0.7307 0.6706 -0.1966 -0.0406 -0.1096 273 PHE A CD1 
205  C CD2 . PHE A 262 ? 0.5188 0.6786 0.5765 -0.1424 -0.0566 -0.0813 273 PHE A CD2 
206  C CE1 . PHE A 262 ? 0.6412 0.6804 0.6586 -0.1841 -0.0244 -0.1200 273 PHE A CE1 
207  C CE2 . PHE A 262 ? 0.5322 0.6255 0.5588 -0.1334 -0.0417 -0.0928 273 PHE A CE2 
208  C CZ  . PHE A 262 ? 0.5699 0.6052 0.5779 -0.1526 -0.0256 -0.1115 273 PHE A CZ  
209  N N   . GLU A 263 ? 0.4304 0.7989 0.6421 -0.1262 -0.0737 -0.0183 274 GLU A N   
210  C CA  . GLU A 263 ? 0.4774 0.9269 0.7301 -0.1133 -0.0832 0.0044  274 GLU A CA  
211  C C   . GLU A 263 ? 0.4332 0.8899 0.6839 -0.0718 -0.0848 0.0226  274 GLU A C   
212  O O   . GLU A 263 ? 0.3765 0.7791 0.6159 -0.0458 -0.0696 0.0242  274 GLU A O   
213  C CB  . GLU A 263 ? 0.4188 0.8789 0.7080 -0.1094 -0.0688 0.0135  274 GLU A CB  
214  C CG  . GLU A 263 ? 0.5662 1.1148 0.9023 -0.0975 -0.0756 0.0369  274 GLU A CG  
215  C CD  . GLU A 263 ? 0.5542 1.1113 0.9238 -0.0949 -0.0587 0.0446  274 GLU A CD  
216  O OE1 . GLU A 263 ? 0.5925 1.0859 0.9494 -0.0834 -0.0402 0.0397  274 GLU A OE1 
217  O OE2 . GLU A 263 ? 0.6316 1.2634 1.0404 -0.1057 -0.0641 0.0560  274 GLU A OE2 
218  N N   . LYS A 264 ? 0.4222 0.9459 0.6828 -0.0669 -0.1028 0.0372  275 LYS A N   
219  C CA  . LYS A 264 ? 0.4309 0.9589 0.6858 -0.0283 -0.1038 0.0563  275 LYS A CA  
220  C C   . LYS A 264 ? 0.4456 0.9827 0.7337 0.0094  -0.0880 0.0783  275 LYS A C   
221  O O   . LYS A 264 ? 0.4360 1.0256 0.7638 0.0092  -0.0867 0.0898  275 LYS A O   
222  C CB  . LYS A 264 ? 0.4108 1.0129 0.6670 -0.0330 -0.1278 0.0692  275 LYS A CB  
223  C CG  . LYS A 264 ? 0.4215 1.0288 0.6705 0.0074  -0.1283 0.0925  275 LYS A CG  
224  C CD  . LYS A 264 ? 0.6360 1.3265 0.8881 0.0031  -0.1536 0.1094  275 LYS A CD  
225  C CE  . LYS A 264 ? 0.7254 1.4368 0.9864 0.0509  -0.1511 0.1431  275 LYS A CE  
226  N NZ  . LYS A 264 ? 0.7219 1.5196 0.9854 0.0497  -0.1769 0.1641  275 LYS A NZ  
227  N N   . ILE A 265 ? 0.4480 0.9320 0.7182 0.0404  -0.0741 0.0831  276 ILE A N   
228  C CA  . ILE A 265 ? 0.4939 0.9749 0.7864 0.0764  -0.0560 0.1015  276 ILE A CA  
229  C C   . ILE A 265 ? 0.6169 1.0959 0.8995 0.1115  -0.0539 0.1213  276 ILE A C   
230  O O   . ILE A 265 ? 0.6220 1.0911 0.9181 0.1432  -0.0361 0.1366  276 ILE A O   
231  C CB  . ILE A 265 ? 0.3306 0.7410 0.6114 0.0788  -0.0346 0.0877  276 ILE A CB  
232  C CG1 . ILE A 265 ? 0.3835 0.7264 0.6222 0.0807  -0.0311 0.0749  276 ILE A CG1 
233  C CG2 . ILE A 265 ? 0.4154 0.8253 0.7062 0.0475  -0.0339 0.0722  276 ILE A CG2 
234  C CD1 . ILE A 265 ? 0.3434 0.6262 0.5710 0.0910  -0.0106 0.0680  276 ILE A CD1 
235  N N   . GLY A 266 ? 0.5809 1.0655 0.8377 0.1068  -0.0695 0.1218  277 GLY A N   
236  C CA  . GLY A 266 ? 0.6713 1.1504 0.9163 0.1401  -0.0661 0.1428  277 GLY A CA  
237  C C   . GLY A 266 ? 0.6244 1.0983 0.8322 0.1304  -0.0818 0.1394  277 GLY A C   
238  O O   . GLY A 266 ? 0.6813 1.1293 0.8625 0.0998  -0.0891 0.1147  277 GLY A O   
239  N N   . GLN A 267 ? 0.7125 1.2087 0.9167 0.1582  -0.0847 0.1653  278 GLN A N   
240  C CA  . GLN A 267 ? 0.8325 1.3285 0.9999 0.1532  -0.0986 0.1671  278 GLN A CA  
241  C C   . GLN A 267 ? 1.0042 1.4570 1.1528 0.1892  -0.0826 0.1865  278 GLN A C   
242  O O   . GLN A 267 ? 0.8857 1.3560 1.0572 0.2239  -0.0723 0.2145  278 GLN A O   
243  C CB  . GLN A 267 ? 0.8900 1.4788 1.0696 0.1440  -0.1258 0.1834  278 GLN A CB  
244  C CG  . GLN A 267 ? 0.9710 1.5680 1.1121 0.1460  -0.1395 0.1930  278 GLN A CG  
245  C CD  . GLN A 267 ? 0.9816 1.5277 1.0756 0.1125  -0.1430 0.1600  278 GLN A CD  
246  O OE1 . GLN A 267 ? 1.0569 1.5936 1.1491 0.0780  -0.1466 0.1313  278 GLN A OE1 
247  N NE2 . GLN A 267 ? 0.9967 1.5071 1.0517 0.1236  -0.1396 0.1648  278 GLN A NE2 
248  N N   . GLY A 268 ? 1.0692 1.4633 1.1761 0.1807  -0.0781 0.1717  279 GLY A N   
249  C CA  . GLY A 268 ? 1.0723 1.4213 1.1556 0.2081  -0.0629 0.1876  279 GLY A CA  
250  C C   . GLY A 268 ? 1.0775 1.4268 1.1201 0.1974  -0.0760 0.1870  279 GLY A C   
251  O O   . GLY A 268 ? 1.0694 1.4493 1.0996 0.1678  -0.0957 0.1713  279 GLY A O   
252  N N   . ALA A 269 ? 1.1403 1.4517 1.1595 0.2209  -0.0627 0.2041  280 ALA A N   
253  C CA  . ALA A 269 ? 1.0996 1.4001 1.0756 0.2114  -0.0702 0.2027  280 ALA A CA  
254  C C   . ALA A 269 ? 1.0548 1.3071 1.0058 0.1805  -0.0663 0.1663  280 ALA A C   
255  O O   . ALA A 269 ? 1.0374 1.2921 0.9547 0.1628  -0.0761 0.1566  280 ALA A O   
256  C CB  . ALA A 269 ? 1.0051 1.2674 0.9614 0.2427  -0.0526 0.2290  280 ALA A CB  
257  N N   . SER A 270 ? 1.1097 1.3205 1.0760 0.1747  -0.0512 0.1472  281 SER A N   
258  C CA  . SER A 270 ? 1.0536 1.2250 1.0025 0.1487  -0.0469 0.1159  281 SER A CA  
259  C C   . SER A 270 ? 0.9514 1.1558 0.9042 0.1194  -0.0642 0.0953  281 SER A C   
260  O O   . SER A 270 ? 0.9317 1.1083 0.8632 0.0982  -0.0623 0.0713  281 SER A O   
261  C CB  . SER A 270 ? 0.9865 1.1101 0.9510 0.1521  -0.0267 0.1050  281 SER A CB  
262  O OG  . SER A 270 ? 1.0647 1.1660 1.0346 0.1786  -0.0105 0.1250  281 SER A OG  
263  N N   . GLY A 271 ? 0.8505 1.1126 0.8301 0.1173  -0.0793 0.1043  282 GLY A N   
264  C CA  . GLY A 271 ? 0.6965 0.9892 0.6786 0.0854  -0.0948 0.0844  282 GLY A CA  
265  C C   . GLY A 271 ? 0.7526 1.0820 0.7790 0.0845  -0.0980 0.0883  282 GLY A C   
266  O O   . GLY A 271 ? 0.7516 1.0961 0.8062 0.1114  -0.0913 0.1105  282 GLY A O   
267  N N   . THR A 272 ? 0.6655 1.0063 0.6959 0.0529  -0.1060 0.0665  283 THR A N   
268  C CA  . THR A 272 ? 0.5443 0.9203 0.6151 0.0451  -0.1087 0.0671  283 THR A CA  
269  C C   . THR A 272 ? 0.4595 0.7786 0.5383 0.0411  -0.0898 0.0496  283 THR A C   
270  O O   . THR A 272 ? 0.4531 0.7224 0.5058 0.0255  -0.0830 0.0277  283 THR A O   
271  C CB  . THR A 272 ? 0.5301 0.9570 0.5991 0.0085  -0.1294 0.0549  283 THR A CB  
272  O OG1 . THR A 272 ? 0.7208 1.1999 0.7734 0.0093  -0.1487 0.0697  283 THR A OG1 
273  C CG2 . THR A 272 ? 0.5002 0.9772 0.6152 0.0014  -0.1334 0.0611  283 THR A CG2 
274  N N   . VAL A 273 ? 0.4605 0.7885 0.5746 0.0563  -0.0805 0.0605  284 VAL A N   
275  C CA  . VAL A 273 ? 0.4711 0.7516 0.5932 0.0548  -0.0630 0.0480  284 VAL A CA  
276  C C   . VAL A 273 ? 0.3838 0.6947 0.5337 0.0336  -0.0668 0.0416  284 VAL A C   
277  O O   . VAL A 273 ? 0.3802 0.7494 0.5614 0.0381  -0.0738 0.0571  284 VAL A O   
278  C CB  . VAL A 273 ? 0.4731 0.7295 0.6064 0.0864  -0.0453 0.0624  284 VAL A CB  
279  C CG1 . VAL A 273 ? 0.4248 0.6429 0.5660 0.0812  -0.0301 0.0501  284 VAL A CG1 
280  C CG2 . VAL A 273 ? 0.4662 0.6839 0.5691 0.1022  -0.0389 0.0661  284 VAL A CG2 
281  N N   . TYR A 274 ? 0.3846 0.6564 0.5240 0.0113  -0.0607 0.0206  285 TYR A N   
282  C CA  . TYR A 274 ? 0.3947 0.6817 0.5549 -0.0122 -0.0608 0.0126  285 TYR A CA  
283  C C   . TYR A 274 ? 0.3651 0.6065 0.5323 -0.0056 -0.0419 0.0086  285 TYR A C   
284  O O   . TYR A 274 ? 0.3582 0.5515 0.5074 0.0086  -0.0309 0.0057  285 TYR A O   
285  C CB  . TYR A 274 ? 0.4351 0.7111 0.5716 -0.0487 -0.0686 -0.0096 285 TYR A CB  
286  C CG  . TYR A 274 ? 0.5197 0.8419 0.6423 -0.0635 -0.0890 -0.0099 285 TYR A CG  
287  C CD1 . TYR A 274 ? 0.5096 0.8101 0.5957 -0.0585 -0.0925 -0.0145 285 TYR A CD1 
288  C CD2 . TYR A 274 ? 0.5303 0.9217 0.6755 -0.0845 -0.1049 -0.0053 285 TYR A CD2 
289  C CE1 . TYR A 274 ? 0.5507 0.8952 0.6193 -0.0731 -0.1117 -0.0143 285 TYR A CE1 
290  C CE2 . TYR A 274 ? 0.5378 0.9788 0.6683 -0.1004 -0.1258 -0.0048 285 TYR A CE2 
291  C CZ  . TYR A 274 ? 0.5920 1.0079 0.6823 -0.0943 -0.1293 -0.0094 285 TYR A CZ  
292  O OH  . TYR A 274 ? 0.6503 1.1165 0.7216 -0.1107 -0.1504 -0.0083 285 TYR A OH  
293  N N   . THR A 275 ? 0.3596 0.6203 0.5528 -0.0178 -0.0386 0.0094  286 THR A N   
294  C CA  . THR A 275 ? 0.3876 0.6040 0.5800 -0.0238 -0.0234 0.0013  286 THR A CA  
295  C C   . THR A 275 ? 0.3818 0.5790 0.5606 -0.0575 -0.0253 -0.0166 286 THR A C   
296  O O   . THR A 275 ? 0.4023 0.6332 0.5813 -0.0810 -0.0385 -0.0226 286 THR A O   
297  C CB  . THR A 275 ? 0.3372 0.5782 0.5622 -0.0167 -0.0144 0.0133  286 THR A CB  
298  O OG1 . THR A 275 ? 0.3435 0.6457 0.5954 -0.0332 -0.0248 0.0183  286 THR A OG1 
299  C CG2 . THR A 275 ? 0.3189 0.5619 0.5502 0.0170  -0.0064 0.0278  286 THR A CG2 
300  N N   . ALA A 276 ? 0.3869 0.5291 0.5525 -0.0602 -0.0112 -0.0248 287 ALA A N   
301  C CA  . ALA A 276 ? 0.4207 0.5295 0.5704 -0.0889 -0.0067 -0.0413 287 ALA A CA  
302  C C   . ALA A 276 ? 0.4184 0.4809 0.5684 -0.0826 0.0115  -0.0391 287 ALA A C   
303  O O   . ALA A 276 ? 0.3905 0.4521 0.5505 -0.0590 0.0178  -0.0267 287 ALA A O   
304  C CB  . ALA A 276 ? 0.4484 0.5273 0.5624 -0.0965 -0.0102 -0.0569 287 ALA A CB  
305  N N   . MET A 277 ? 0.4533 0.4759 0.5896 -0.1044 0.0208  -0.0508 288 MET A N   
306  C CA  . MET A 277 ? 0.4583 0.4383 0.5948 -0.0986 0.0385  -0.0454 288 MET A CA  
307  C C   . MET A 277 ? 0.4954 0.4116 0.6023 -0.1017 0.0514  -0.0569 288 MET A C   
308  O O   . MET A 277 ? 0.5351 0.4324 0.6226 -0.1255 0.0513  -0.0741 288 MET A O   
309  C CB  . MET A 277 ? 0.4695 0.4632 0.6262 -0.1202 0.0437  -0.0417 288 MET A CB  
310  C CG  . MET A 277 ? 0.4777 0.4298 0.6336 -0.1130 0.0622  -0.0324 288 MET A CG  
311  S SD  . MET A 277 ? 0.6513 0.6178 0.8288 -0.1407 0.0703  -0.0272 288 MET A SD  
312  C CE  . MET A 277 ? 0.5646 0.5966 0.7739 -0.1186 0.0632  -0.0096 288 MET A CE  
313  N N   . ASP A 278 ? 0.4859 0.3710 0.5888 -0.0776 0.0632  -0.0472 289 ASP A N   
314  C CA  . ASP A 278 ? 0.5228 0.3477 0.6036 -0.0745 0.0800  -0.0524 289 ASP A CA  
315  C C   . ASP A 278 ? 0.6264 0.4170 0.7046 -0.0981 0.0938  -0.0562 289 ASP A C   
316  O O   . ASP A 278 ? 0.5594 0.3578 0.6552 -0.0989 0.0988  -0.0428 289 ASP A O   
317  C CB  . ASP A 278 ? 0.4997 0.3143 0.5844 -0.0431 0.0878  -0.0359 289 ASP A CB  
318  C CG  . ASP A 278 ? 0.5924 0.3524 0.6584 -0.0322 0.1056  -0.0371 289 ASP A CG  
319  O OD1 . ASP A 278 ? 0.6155 0.3318 0.6720 -0.0450 0.1210  -0.0410 289 ASP A OD1 
320  O OD2 . ASP A 278 ? 0.5657 0.3264 0.6273 -0.0102 0.1061  -0.0330 289 ASP A OD2 
321  N N   A VAL A 279 ? 0.6192 0.3689 0.6724 -0.1193 0.1016  -0.0753 290 VAL A N   
322  N N   B VAL A 279 ? 0.6194 0.3682 0.6723 -0.1188 0.1019  -0.0752 290 VAL A N   
323  C CA  A VAL A 279 ? 0.7038 0.4154 0.7502 -0.1481 0.1161  -0.0823 290 VAL A CA  
324  C CA  B VAL A 279 ? 0.7045 0.4159 0.7504 -0.1483 0.1159  -0.0827 290 VAL A CA  
325  C C   A VAL A 279 ? 0.6891 0.3532 0.7369 -0.1299 0.1385  -0.0649 290 VAL A C   
326  C C   B VAL A 279 ? 0.6964 0.3536 0.7403 -0.1318 0.1400  -0.0675 290 VAL A C   
327  O O   A VAL A 279 ? 0.7402 0.3917 0.7958 -0.1458 0.1482  -0.0585 290 VAL A O   
328  O O   B VAL A 279 ? 0.7502 0.3816 0.7952 -0.1518 0.1528  -0.0657 290 VAL A O   
329  C CB  A VAL A 279 ? 0.7332 0.4025 0.7451 -0.1755 0.1225  -0.1094 290 VAL A CB  
330  C CB  B VAL A 279 ? 0.7304 0.4065 0.7432 -0.1776 0.1198  -0.1103 290 VAL A CB  
331  C CG1 A VAL A 279 ? 0.8115 0.4273 0.8110 -0.2066 0.1424  -0.1180 290 VAL A CG1 
332  C CG1 B VAL A 279 ? 0.7684 0.3761 0.7523 -0.1582 0.1409  -0.1158 290 VAL A CG1 
333  C CG2 A VAL A 279 ? 0.7191 0.4458 0.7306 -0.1975 0.0977  -0.1237 290 VAL A CG2 
334  C CG2 B VAL A 279 ? 0.8020 0.4587 0.8103 -0.2197 0.1277  -0.1220 290 VAL A CG2 
335  N N   . ALA A 280 ? 0.6912 0.3336 0.7330 -0.0962 0.1467  -0.0545 291 ALA A N   
336  C CA  . ALA A 280 ? 0.7049 0.3028 0.7460 -0.0762 0.1686  -0.0356 291 ALA A CA  
337  C C   . ALA A 280 ? 0.6908 0.3293 0.7569 -0.0556 0.1623  -0.0094 291 ALA A C   
338  O O   . ALA A 280 ? 0.6995 0.3131 0.7685 -0.0500 0.1774  0.0081  291 ALA A O   
339  C CB  . ALA A 280 ? 0.7369 0.2948 0.7609 -0.0492 0.1827  -0.0350 291 ALA A CB  
340  N N   . THR A 281 ? 0.5981 0.2956 0.6792 -0.0449 0.1420  -0.0062 292 THR A N   
341  C CA  . THR A 281 ? 0.5589 0.2917 0.6575 -0.0267 0.1374  0.0155  292 THR A CA  
342  C C   . THR A 281 ? 0.5854 0.3683 0.7025 -0.0409 0.1242  0.0157  292 THR A C   
343  O O   . THR A 281 ? 0.5052 0.3105 0.6331 -0.0309 0.1244  0.0322  292 THR A O   
344  C CB  . THR A 281 ? 0.5223 0.2786 0.6217 0.0003  0.1291  0.0215  292 THR A CB  
345  O OG1 . THR A 281 ? 0.4910 0.2823 0.5925 -0.0059 0.1118  0.0070  292 THR A OG1 
346  C CG2 . THR A 281 ? 0.5859 0.2998 0.6707 0.0171  0.1431  0.0222  292 THR A CG2 
347  N N   . GLY A 282 ? 0.5231 0.3276 0.6437 -0.0626 0.1131  -0.0012 293 GLY A N   
348  C CA  . GLY A 282 ? 0.5061 0.3645 0.6480 -0.0714 0.1014  0.0009  293 GLY A CA  
349  C C   . GLY A 282 ? 0.4441 0.3449 0.5939 -0.0513 0.0878  0.0042  293 GLY A C   
350  O O   . GLY A 282 ? 0.4221 0.3659 0.5901 -0.0535 0.0811  0.0079  293 GLY A O   
351  N N   . GLN A 283 ? 0.4333 0.3225 0.5704 -0.0319 0.0855  0.0034  294 GLN A N   
352  C CA  . GLN A 283 ? 0.5079 0.4305 0.6491 -0.0156 0.0748  0.0054  294 GLN A CA  
353  C C   . GLN A 283 ? 0.4102 0.3646 0.5577 -0.0249 0.0615  -0.0047 294 GLN A C   
354  O O   . GLN A 283 ? 0.4061 0.3506 0.5433 -0.0376 0.0572  -0.0172 294 GLN A O   
355  C CB  . GLN A 283 ? 0.4145 0.3188 0.5408 0.0026  0.0757  0.0057  294 GLN A CB  
356  C CG  . GLN A 283 ? 0.4441 0.3766 0.5712 0.0157  0.0662  0.0060  294 GLN A CG  
357  C CD  . GLN A 283 ? 0.6420 0.5621 0.7566 0.0308  0.0675  0.0069  294 GLN A CD  
358  O OE1 . GLN A 283 ? 0.6213 0.5140 0.7269 0.0334  0.0743  0.0053  294 GLN A OE1 
359  N NE2 . GLN A 283 ? 0.5102 0.4498 0.6241 0.0404  0.0628  0.0094  294 GLN A NE2 
360  N N   . GLU A 284 ? 0.3597 0.3526 0.5224 -0.0176 0.0562  0.0018  295 GLU A N   
361  C CA  . GLU A 284 ? 0.3491 0.3776 0.5197 -0.0183 0.0440  -0.0020 295 GLU A CA  
362  C C   . GLU A 284 ? 0.3435 0.3637 0.4978 -0.0020 0.0389  -0.0047 295 GLU A C   
363  O O   . GLU A 284 ? 0.3452 0.3520 0.4921 0.0136  0.0443  0.0002  295 GLU A O   
364  C CB  . GLU A 284 ? 0.3300 0.3979 0.5229 -0.0110 0.0448  0.0084  295 GLU A CB  
365  C CG  . GLU A 284 ? 0.5281 0.6072 0.7384 -0.0257 0.0523  0.0132  295 GLU A CG  
366  C CD  . GLU A 284 ? 0.6008 0.7197 0.8333 -0.0161 0.0562  0.0235  295 GLU A CD  
367  O OE1 . GLU A 284 ? 0.4148 0.5468 0.6474 0.0035  0.0545  0.0268  295 GLU A OE1 
368  O OE2 . GLU A 284 ? 0.6360 0.7689 0.8843 -0.0273 0.0637  0.0287  295 GLU A OE2 
369  N N   . VAL A 285 ? 0.3474 0.3781 0.4948 -0.0077 0.0285  -0.0122 296 VAL A N   
370  C CA  . VAL A 285 ? 0.3436 0.3645 0.4731 0.0054  0.0247  -0.0148 296 VAL A CA  
371  C C   . VAL A 285 ? 0.3406 0.3984 0.4747 0.0079  0.0125  -0.0121 296 VAL A C   
372  O O   . VAL A 285 ? 0.3463 0.4381 0.4952 -0.0046 0.0046  -0.0112 296 VAL A O   
373  C CB  . VAL A 285 ? 0.3673 0.3520 0.4735 -0.0021 0.0274  -0.0268 296 VAL A CB  
374  C CG1 . VAL A 285 ? 0.3729 0.3226 0.4763 0.0015  0.0410  -0.0247 296 VAL A CG1 
375  C CG2 . VAL A 285 ? 0.3954 0.3858 0.4965 -0.0264 0.0208  -0.0385 296 VAL A CG2 
376  N N   . ALA A 286 ? 0.3344 0.3873 0.4558 0.0240  0.0112  -0.0091 297 ALA A N   
377  C CA  . ALA A 286 ? 0.3373 0.4191 0.4575 0.0305  0.0007  -0.0037 297 ALA A CA  
378  C C   . ALA A 286 ? 0.3563 0.4219 0.4492 0.0239  -0.0047 -0.0136 297 ALA A C   
379  O O   . ALA A 286 ? 0.4168 0.4478 0.4925 0.0294  0.0032  -0.0185 297 ALA A O   
380  C CB  . ALA A 286 ? 0.3245 0.4067 0.4468 0.0540  0.0067  0.0084  297 ALA A CB  
381  N N   . ILE A 287 ? 0.3735 0.4677 0.4623 0.0115  -0.0179 -0.0161 298 ILE A N   
382  C CA  . ILE A 287 ? 0.4134 0.4941 0.4719 0.0013  -0.0230 -0.0277 298 ILE A CA  
383  C C   . ILE A 287 ? 0.4055 0.5240 0.4587 0.0091  -0.0363 -0.0167 298 ILE A C   
384  O O   . ILE A 287 ? 0.4064 0.5738 0.4778 0.0045  -0.0484 -0.0081 298 ILE A O   
385  C CB  . ILE A 287 ? 0.4274 0.5013 0.4763 -0.0284 -0.0258 -0.0452 298 ILE A CB  
386  C CG1 . ILE A 287 ? 0.4255 0.4601 0.4809 -0.0327 -0.0105 -0.0516 298 ILE A CG1 
387  C CG2 . ILE A 287 ? 0.4602 0.5137 0.4719 -0.0386 -0.0276 -0.0595 298 ILE A CG2 
388  C CD1 . ILE A 287 ? 0.4634 0.4752 0.5047 -0.0618 -0.0074 -0.0699 298 ILE A CD1 
389  N N   . LYS A 288 ? 0.4356 0.5350 0.4651 0.0213  -0.0337 -0.0149 299 LYS A N   
390  C CA  . LYS A 288 ? 0.4251 0.5551 0.4435 0.0297  -0.0451 -0.0027 299 LYS A CA  
391  C C   . LYS A 288 ? 0.4588 0.5865 0.4430 0.0100  -0.0532 -0.0172 299 LYS A C   
392  O O   . LYS A 288 ? 0.4704 0.5550 0.4314 0.0039  -0.0426 -0.0327 299 LYS A O   
393  C CB  . LYS A 288 ? 0.4436 0.5531 0.4553 0.0556  -0.0353 0.0109  299 LYS A CB  
394  C CG  . LYS A 288 ? 0.4335 0.5748 0.4369 0.0690  -0.0451 0.0295  299 LYS A CG  
395  C CD  . LYS A 288 ? 0.5483 0.6590 0.5405 0.0919  -0.0319 0.0419  299 LYS A CD  
396  C CE  . LYS A 288 ? 0.5685 0.6681 0.5858 0.1094  -0.0189 0.0519  299 LYS A CE  
397  N NZ  . LYS A 288 ? 0.5176 0.5776 0.5192 0.1249  -0.0033 0.0588  299 LYS A NZ  
398  N N   . GLN A 289 ? 0.4873 0.6641 0.4684 -0.0001 -0.0711 -0.0118 300 GLN A N   
399  C CA  . GLN A 289 ? 0.5993 0.7821 0.5440 -0.0226 -0.0812 -0.0259 300 GLN A CA  
400  C C   . GLN A 289 ? 0.5733 0.7744 0.4968 -0.0059 -0.0882 -0.0091 300 GLN A C   
401  O O   . GLN A 289 ? 0.5221 0.7682 0.4649 0.0115  -0.0979 0.0155  300 GLN A O   
402  C CB  . GLN A 289 ? 0.5341 0.7654 0.4873 -0.0520 -0.0984 -0.0327 300 GLN A CB  
403  C CG  . GLN A 289 ? 0.6235 0.8756 0.5373 -0.0779 -0.1130 -0.0449 300 GLN A CG  
404  C CD  . GLN A 289 ? 0.7715 1.0941 0.7004 -0.1040 -0.1350 -0.0431 300 GLN A CD  
405  O OE1 . GLN A 289 ? 0.6242 0.9862 0.5970 -0.0974 -0.1393 -0.0282 300 GLN A OE1 
406  N NE2 . GLN A 289 ? 0.7619 1.1038 0.6539 -0.1354 -0.1485 -0.0585 300 GLN A NE2 
407  N N   . MET A 290 ? 0.5956 0.7615 0.4796 -0.0095 -0.0813 -0.0206 301 MET A N   
408  C CA  . MET A 290 ? 0.6597 0.8338 0.5187 0.0062  -0.0842 -0.0047 301 MET A CA  
409  C C   . MET A 290 ? 0.7988 0.9752 0.6103 -0.0168 -0.0916 -0.0206 301 MET A C   
410  O O   . MET A 290 ? 0.6363 0.7714 0.4250 -0.0349 -0.0804 -0.0470 301 MET A O   
411  C CB  . MET A 290 ? 0.7720 0.8955 0.6280 0.0287  -0.0633 0.0000  301 MET A CB  
412  C CG  . MET A 290 ? 0.8534 0.9625 0.7479 0.0467  -0.0522 0.0092  301 MET A CG  
413  S SD  . MET A 290 ? 0.9374 0.9959 0.8258 0.0676  -0.0299 0.0153  301 MET A SD  
414  C CE  . MET A 290 ? 0.9091 0.9846 0.7814 0.0883  -0.0336 0.0431  301 MET A CE  
415  N N   . ASN A 291 ? 0.8768 1.1012 0.6720 -0.0150 -0.1090 -0.0037 302 ASN A N   
416  C CA  . ASN A 291 ? 0.9208 1.1497 0.6639 -0.0338 -0.1158 -0.0149 302 ASN A CA  
417  C C   . ASN A 291 ? 0.9256 1.1148 0.6426 -0.0127 -0.0995 -0.0068 302 ASN A C   
418  O O   . ASN A 291 ? 0.9111 1.1167 0.6343 0.0131  -0.1014 0.0225  302 ASN A O   
419  C CB  . ASN A 291 ? 1.0736 1.3797 0.8105 -0.0421 -0.1436 0.0023  302 ASN A CB  
420  C CG  . ASN A 291 ? 1.1918 1.5332 0.9292 -0.0809 -0.1598 -0.0188 302 ASN A CG  
421  O OD1 . ASN A 291 ? 1.1846 1.4814 0.9093 -0.1058 -0.1485 -0.0508 302 ASN A OD1 
422  N ND2 . ASN A 291 ? 1.3391 1.7614 1.0914 -0.0866 -0.1855 0.0001  302 ASN A ND2 
423  N N   . LEU A 292 ? 0.7283 0.8641 0.4164 -0.0232 -0.0814 -0.0316 303 LEU A N   
424  C CA  . LEU A 292 ? 0.8325 0.9323 0.4989 -0.0055 -0.0636 -0.0250 303 LEU A CA  
425  C C   . LEU A 292 ? 0.8937 1.0215 0.5192 -0.0040 -0.0741 -0.0097 303 LEU A C   
426  O O   . LEU A 292 ? 0.9698 1.0866 0.5896 0.0182  -0.0652 0.0114  303 LEU A O   
427  C CB  . LEU A 292 ? 0.7401 0.7849 0.3853 -0.0170 -0.0416 -0.0543 303 LEU A CB  
428  C CG  . LEU A 292 ? 0.8229 0.8352 0.5017 -0.0185 -0.0286 -0.0697 303 LEU A CG  
429  C CD1 . LEU A 292 ? 0.8048 0.7661 0.4584 -0.0261 -0.0055 -0.0949 303 LEU A CD1 
430  C CD2 . LEU A 292 ? 0.7102 0.7173 0.4312 0.0074  -0.0218 -0.0492 303 LEU A CD2 
431  N N   . GLN A 293 ? 0.9041 1.0692 0.4993 -0.0290 -0.0929 -0.0191 304 GLN A N   
432  C CA  . GLN A 293 ? 1.0642 1.2660 0.6192 -0.0285 -0.1064 -0.0017 304 GLN A CA  
433  C C   . GLN A 293 ? 1.0255 1.2712 0.6072 0.0012  -0.1190 0.0409  304 GLN A C   
434  O O   . GLN A 293 ? 1.0391 1.3070 0.5904 0.0110  -0.1254 0.0632  304 GLN A O   
435  C CB  . GLN A 293 ? 0.9271 1.1688 0.4468 -0.0653 -0.1273 -0.0209 304 GLN A CB  
436  N N   . GLN A 294 ? 1.0458 1.3034 0.6815 0.0167  -0.1211 0.0536  305 GLN A N   
437  C CA  . GLN A 294 ? 1.0447 1.3402 0.7085 0.0475  -0.1293 0.0937  305 GLN A CA  
438  C C   . GLN A 294 ? 1.0983 1.3474 0.7958 0.0773  -0.1069 0.1067  305 GLN A C   
439  O O   . GLN A 294 ? 1.1309 1.4013 0.8545 0.1047  -0.1087 0.1382  305 GLN A O   
440  C CB  . GLN A 294 ? 1.0526 1.4179 0.7508 0.0402  -0.1534 0.1017  305 GLN A CB  
441  N N   . GLN A 295 ? 1.0590 1.2473 0.7567 0.0724  -0.0853 0.0837  306 GLN A N   
442  C CA  . GLN A 295 ? 1.0925 1.2363 0.8146 0.0955  -0.0638 0.0939  306 GLN A CA  
443  C C   . GLN A 295 ? 1.1575 1.2728 0.8500 0.1114  -0.0495 0.1120  306 GLN A C   
444  O O   . GLN A 295 ? 1.2157 1.3132 0.8699 0.0989  -0.0435 0.0997  306 GLN A O   
445  C CB  . GLN A 295 ? 1.0397 1.1394 0.7762 0.0831  -0.0483 0.0646  306 GLN A CB  
446  C CG  . GLN A 295 ? 0.9693 1.0881 0.7401 0.0717  -0.0577 0.0512  306 GLN A CG  
447  C CD  . GLN A 295 ? 1.0173 1.1666 0.8269 0.0913  -0.0643 0.0751  306 GLN A CD  
448  O OE1 . GLN A 295 ? 1.1137 1.2461 0.9326 0.1156  -0.0529 0.0960  306 GLN A OE1 
449  N NE2 . GLN A 295 ? 0.9823 1.1750 0.8144 0.0799  -0.0807 0.0717  306 GLN A NE2 
450  N N   . PRO A 296 ? 1.1599 1.2673 0.8675 0.1386  -0.0415 0.1414  307 PRO A N   
451  C CA  . PRO A 296 ? 1.1550 1.2334 0.8328 0.1532  -0.0267 0.1620  307 PRO A CA  
452  C C   . PRO A 296 ? 1.1238 1.1447 0.7913 0.1449  -0.0024 0.1442  307 PRO A C   
453  O O   . PRO A 296 ? 1.1944 1.2001 0.8250 0.1388  0.0057  0.1432  307 PRO A O   
454  C CB  . PRO A 296 ? 1.1616 1.2388 0.8641 0.1840  -0.0208 0.1948  307 PRO A CB  
455  C CG  . PRO A 296 ? 1.0958 1.1793 0.8439 0.1834  -0.0229 0.1826  307 PRO A CG  
456  C CD  . PRO A 296 ? 1.1596 1.2820 0.9106 0.1573  -0.0433 0.1572  307 PRO A CD  
457  N N   . LYS A 297 ? 1.0549 1.0482 0.7552 0.1443  0.0095  0.1312  308 LYS A N   
458  C CA  . LYS A 297 ? 0.9560 0.9012 0.6554 0.1394  0.0328  0.1205  308 LYS A CA  
459  C C   . LYS A 297 ? 0.8860 0.8271 0.6017 0.1207  0.0336  0.0888  308 LYS A C   
460  O O   . LYS A 297 ? 0.6942 0.6227 0.4413 0.1206  0.0393  0.0808  308 LYS A O   
461  C CB  . LYS A 297 ? 1.0289 0.9437 0.7491 0.1554  0.0481  0.1362  308 LYS A CB  
462  C CG  . LYS A 297 ? 0.9683 0.8782 0.6713 0.1777  0.0520  0.1704  308 LYS A CG  
463  C CD  . LYS A 297 ? 1.1771 1.0694 0.8385 0.1748  0.0622  0.1797  308 LYS A CD  
464  C CE  . LYS A 297 ? 1.2557 1.0988 0.9127 0.1640  0.0875  0.1699  308 LYS A CE  
465  N NZ  . LYS A 297 ? 1.3398 1.1429 1.0092 0.1766  0.1055  0.1845  308 LYS A NZ  
466  N N   . LYS A 298 ? 0.8684 0.8182 0.5601 0.1055  0.0294  0.0714  309 LYS A N   
467  C CA  . LYS A 298 ? 0.8284 0.7708 0.5326 0.0906  0.0326  0.0432  309 LYS A CA  
468  C C   . LYS A 298 ? 0.7205 0.6319 0.4404 0.0906  0.0535  0.0366  309 LYS A C   
469  O O   . LYS A 298 ? 0.6872 0.5940 0.4334 0.0857  0.0561  0.0217  309 LYS A O   
470  C CB  . LYS A 298 ? 0.7908 0.7395 0.4589 0.0755  0.0297  0.0262  309 LYS A CB  
471  C CG  . LYS A 298 ? 0.8471 0.8309 0.5065 0.0653  0.0069  0.0215  309 LYS A CG  
472  C CD  . LYS A 298 ? 0.9968 0.9819 0.6099 0.0478  0.0061  0.0041  309 LYS A CD  
473  C CE  . LYS A 298 ? 0.9828 0.9874 0.5570 0.0524  -0.0008 0.0244  309 LYS A CE  
474  N NZ  . LYS A 298 ? 0.9573 1.0089 0.5400 0.0578  -0.0256 0.0456  309 LYS A NZ  
475  N N   . GLU A 299 ? 0.7165 0.6094 0.4211 0.0951  0.0683  0.0488  310 GLU A N   
476  C CA  . GLU A 299 ? 0.7230 0.5942 0.4433 0.0918  0.0872  0.0439  310 GLU A CA  
477  C C   . GLU A 299 ? 0.6274 0.4943 0.3846 0.0947  0.0862  0.0444  310 GLU A C   
478  O O   . GLU A 299 ? 0.6113 0.4738 0.3902 0.0883  0.0943  0.0333  310 GLU A O   
479  C CB  . GLU A 299 ? 0.7941 0.6465 0.4922 0.0943  0.1024  0.0604  310 GLU A CB  
480  C CG  . GLU A 299 ? 1.0547 0.9125 0.7109 0.0942  0.1018  0.0664  310 GLU A CG  
481  C CD  . GLU A 299 ? 1.0728 0.9428 0.7130 0.1063  0.0868  0.0880  310 GLU A CD  
482  O OE1 . GLU A 299 ? 1.0832 0.9497 0.7453 0.1172  0.0830  0.1009  310 GLU A OE1 
483  O OE2 . GLU A 299 ? 1.1722 1.0578 0.7781 0.1056  0.0791  0.0925  310 GLU A OE2 
484  N N   . LEU A 300 ? 0.6878 0.5585 0.4519 0.1053  0.0771  0.0586  311 LEU A N   
485  C CA  . LEU A 300 ? 0.5677 0.4331 0.3628 0.1085  0.0775  0.0585  311 LEU A CA  
486  C C   . LEU A 300 ? 0.5718 0.4556 0.3913 0.1023  0.0668  0.0415  311 LEU A C   
487  O O   . LEU A 300 ? 0.5356 0.4138 0.3789 0.0988  0.0714  0.0345  311 LEU A O   
488  C CB  . LEU A 300 ? 0.5825 0.4478 0.3785 0.1248  0.0732  0.0792  311 LEU A CB  
489  C CG  . LEU A 300 ? 0.7318 0.5678 0.5053 0.1334  0.0884  0.0991  311 LEU A CG  
490  C CD1 . LEU A 300 ? 0.7747 0.6080 0.5533 0.1543  0.0873  0.1211  311 LEU A CD1 
491  C CD2 . LEU A 300 ? 0.6403 0.4432 0.4159 0.1215  0.1086  0.0919  311 LEU A CD2 
492  N N   . ILE A 301 ? 0.5446 0.4498 0.3564 0.0993  0.0528  0.0351  312 ILE A N   
493  C CA  . ILE A 301 ? 0.5161 0.4326 0.3477 0.0912  0.0452  0.0186  312 ILE A CA  
494  C C   . ILE A 301 ? 0.5623 0.4644 0.3992 0.0838  0.0580  0.0037  312 ILE A C   
495  O O   . ILE A 301 ? 0.5068 0.4085 0.3687 0.0817  0.0592  -0.0036 312 ILE A O   
496  C CB  . ILE A 301 ? 0.5820 0.5208 0.3986 0.0842  0.0296  0.0123  312 ILE A CB  
497  C CG1 . ILE A 301 ? 0.6337 0.5973 0.4443 0.0934  0.0162  0.0318  312 ILE A CG1 
498  C CG2 . ILE A 301 ? 0.5147 0.4596 0.3517 0.0741  0.0238  -0.0039 312 ILE A CG2 
499  C CD1 . ILE A 301 ? 0.7216 0.6933 0.5635 0.1052  0.0137  0.0443  312 ILE A CD1 
500  N N   . ILE A 302 ? 0.5461 0.4389 0.3600 0.0814  0.0684  0.0011  313 ILE A N   
501  C CA  . ILE A 302 ? 0.5236 0.4083 0.3443 0.0777  0.0827  -0.0099 313 ILE A CA  
502  C C   . ILE A 302 ? 0.5143 0.3973 0.3623 0.0786  0.0904  -0.0047 313 ILE A C   
503  O O   . ILE A 302 ? 0.5179 0.4054 0.3888 0.0775  0.0935  -0.0115 313 ILE A O   
504  C CB  . ILE A 302 ? 0.5510 0.4289 0.3420 0.0762  0.0948  -0.0105 313 ILE A CB  
505  C CG1 . ILE A 302 ? 0.5826 0.4620 0.3422 0.0715  0.0882  -0.0205 313 ILE A CG1 
506  C CG2 . ILE A 302 ? 0.5431 0.4186 0.3476 0.0756  0.1126  -0.0168 313 ILE A CG2 
507  C CD1 . ILE A 302 ? 0.6792 0.5519 0.4034 0.0699  0.1004  -0.0208 313 ILE A CD1 
508  N N   A ASN A 303 ? 0.5201 0.3957 0.3637 0.0798  0.0942  0.0079  314 ASN A N   
509  N N   B ASN A 303 ? 0.5203 0.3959 0.3639 0.0798  0.0942  0.0079  314 ASN A N   
510  C CA  A ASN A 303 ? 0.5366 0.4088 0.3997 0.0754  0.1022  0.0107  314 ASN A CA  
511  C CA  B ASN A 303 ? 0.5365 0.4088 0.3998 0.0754  0.1022  0.0107  314 ASN A CA  
512  C C   A ASN A 303 ? 0.5021 0.3807 0.3906 0.0764  0.0936  0.0075  314 ASN A C   
513  C C   B ASN A 303 ? 0.5024 0.3812 0.3910 0.0764  0.0935  0.0074  314 ASN A C   
514  O O   A ASN A 303 ? 0.4810 0.3678 0.3895 0.0713  0.0971  0.0031  314 ASN A O   
515  O O   B ASN A 303 ? 0.4814 0.3685 0.3902 0.0714  0.0970  0.0029  314 ASN A O   
516  C CB  A ASN A 303 ? 0.5868 0.4403 0.4343 0.0749  0.1101  0.0236  314 ASN A CB  
517  C CB  B ASN A 303 ? 0.5857 0.4394 0.4339 0.0749  0.1099  0.0235  314 ASN A CB  
518  C CG  A ASN A 303 ? 0.5653 0.4122 0.4258 0.0640  0.1208  0.0234  314 ASN A CG  
519  C CG  B ASN A 303 ? 0.5400 0.3872 0.3664 0.0704  0.1227  0.0274  314 ASN A CG  
520  O OD1 A ASN A 303 ? 0.6338 0.4654 0.4968 0.0638  0.1219  0.0275  314 ASN A OD1 
521  O OD1 B ASN A 303 ? 0.6392 0.4988 0.4691 0.0659  0.1292  0.0199  314 ASN A OD1 
522  N ND2 A ASN A 303 ? 0.4925 0.3527 0.3607 0.0541  0.1297  0.0186  314 ASN A ND2 
523  N ND2 B ASN A 303 ? 0.7099 0.5371 0.5136 0.0731  0.1282  0.0410  314 ASN A ND2 
524  N N   . GLU A 304 ? 0.4873 0.3669 0.3759 0.0829  0.0823  0.0110  315 GLU A N   
525  C CA  . GLU A 304 ? 0.4898 0.3754 0.4015 0.0837  0.0761  0.0090  315 GLU A CA  
526  C C   . GLU A 304 ? 0.4525 0.3500 0.3804 0.0802  0.0725  -0.0019 315 GLU A C   
527  O O   . GLU A 304 ? 0.4627 0.3649 0.4098 0.0775  0.0742  -0.0039 315 GLU A O   
528  C CB  . GLU A 304 ? 0.4895 0.3799 0.4013 0.0926  0.0660  0.0168  315 GLU A CB  
529  C CG  . GLU A 304 ? 0.4355 0.3339 0.3717 0.0936  0.0615  0.0149  315 GLU A CG  
530  C CD  . GLU A 304 ? 0.4722 0.3787 0.4133 0.1047  0.0552  0.0258  315 GLU A CD  
531  O OE1 . GLU A 304 ? 0.5293 0.4409 0.4562 0.1124  0.0509  0.0359  315 GLU A OE1 
532  O OE2 . GLU A 304 ? 0.5365 0.4471 0.4961 0.1068  0.0554  0.0258  315 GLU A OE2 
533  N N   . ILE A 305 ? 0.4685 0.3684 0.3860 0.0797  0.0694  -0.0090 316 ILE A N   
534  C CA  . ILE A 305 ? 0.4282 0.3301 0.3579 0.0775  0.0702  -0.0189 316 ILE A CA  
535  C C   . ILE A 305 ? 0.4339 0.3378 0.3752 0.0782  0.0825  -0.0189 316 ILE A C   
536  O O   . ILE A 305 ? 0.4258 0.3362 0.3881 0.0791  0.0835  -0.0189 316 ILE A O   
537  C CB  . ILE A 305 ? 0.4396 0.3360 0.3491 0.0744  0.0680  -0.0291 316 ILE A CB  
538  C CG1 . ILE A 305 ? 0.4459 0.3520 0.3499 0.0707  0.0525  -0.0288 316 ILE A CG1 
539  C CG2 . ILE A 305 ? 0.4423 0.3294 0.3597 0.0739  0.0761  -0.0393 316 ILE A CG2 
540  C CD1 . ILE A 305 ? 0.5337 0.4367 0.4123 0.0619  0.0488  -0.0408 316 ILE A CD1 
541  N N   . LEU A 306 ? 0.4575 0.3604 0.3865 0.0779  0.0921  -0.0167 317 LEU A N   
542  C CA  . LEU A 306 ? 0.4612 0.3758 0.4047 0.0781  0.1037  -0.0148 317 LEU A CA  
543  C C   . LEU A 306 ? 0.4844 0.4123 0.4483 0.0728  0.1017  -0.0085 317 LEU A C   
544  O O   . LEU A 306 ? 0.4726 0.4183 0.4576 0.0740  0.1044  -0.0064 317 LEU A O   
545  C CB  . LEU A 306 ? 0.4491 0.3628 0.3753 0.0764  0.1150  -0.0129 317 LEU A CB  
546  C CG  . LEU A 306 ? 0.4794 0.3828 0.3866 0.0816  0.1212  -0.0215 317 LEU A CG  
547  C CD1 . LEU A 306 ? 0.5373 0.4397 0.4238 0.0805  0.1341  -0.0198 317 LEU A CD1 
548  C CD2 . LEU A 306 ? 0.5550 0.4607 0.4798 0.0893  0.1283  -0.0268 317 LEU A CD2 
549  N N   . VAL A 307 ? 0.4479 0.3671 0.4039 0.0673  0.0981  -0.0048 318 VAL A N   
550  C CA  . VAL A 307 ? 0.4352 0.3616 0.4033 0.0588  0.0982  -0.0020 318 VAL A CA  
551  C C   . VAL A 307 ? 0.4450 0.3796 0.4308 0.0618  0.0901  -0.0034 318 VAL A C   
552  O O   . VAL A 307 ? 0.4310 0.3841 0.4322 0.0568  0.0905  -0.0015 318 VAL A O   
553  C CB  . VAL A 307 ? 0.5343 0.4391 0.4853 0.0540  0.1006  0.0012  318 VAL A CB  
554  C CG1 . VAL A 307 ? 0.4896 0.3946 0.4477 0.0438  0.1017  0.0004  318 VAL A CG1 
555  C CG2 . VAL A 307 ? 0.6067 0.5036 0.5411 0.0477  0.1114  0.0044  318 VAL A CG2 
556  N N   . MET A 308 ? 0.4368 0.3615 0.4204 0.0687  0.0824  -0.0057 319 MET A N   
557  C CA  . MET A 308 ? 0.5155 0.4466 0.5153 0.0702  0.0762  -0.0062 319 MET A CA  
558  C C   . MET A 308 ? 0.4877 0.4308 0.5022 0.0738  0.0789  -0.0060 319 MET A C   
559  O O   . MET A 308 ? 0.4458 0.4016 0.4754 0.0730  0.0775  -0.0021 319 MET A O   
560  C CB  . MET A 308 ? 0.4383 0.3613 0.4346 0.0745  0.0680  -0.0085 319 MET A CB  
561  C CG  . MET A 308 ? 0.3974 0.3129 0.3838 0.0764  0.0656  -0.0044 319 MET A CG  
562  S SD  . MET A 308 ? 0.5329 0.4419 0.5201 0.0716  0.0731  -0.0010 319 MET A SD  
563  C CE  . MET A 308 ? 0.4542 0.3748 0.4608 0.0712  0.0683  -0.0022 319 MET A CE  
564  N N   . ARG A 309 ? 0.3904 0.3287 0.3993 0.0792  0.0845  -0.0091 320 ARG A N   
565  C CA  . ARG A 309 ? 0.3958 0.3402 0.4183 0.0869  0.0912  -0.0072 320 ARG A CA  
566  C C   . ARG A 309 ? 0.4780 0.4514 0.5180 0.0869  0.0955  0.0025  320 ARG A C   
567  O O   . ARG A 309 ? 0.4678 0.4547 0.5255 0.0941  0.0976  0.0099  320 ARG A O   
568  C CB  . ARG A 309 ? 0.4369 0.3667 0.4455 0.0928  0.1005  -0.0137 320 ARG A CB  
569  C CG  . ARG A 309 ? 0.5260 0.4314 0.5169 0.0903  0.0961  -0.0244 320 ARG A CG  
570  C CD  . ARG A 309 ? 0.5119 0.4006 0.4851 0.0945  0.1083  -0.0327 320 ARG A CD  
571  N NE  . ARG A 309 ? 0.5519 0.4180 0.5050 0.0877  0.1042  -0.0454 320 ARG A NE  
572  C CZ  . ARG A 309 ? 0.5858 0.4329 0.5128 0.0859  0.1124  -0.0570 320 ARG A CZ  
573  N NH1 . ARG A 309 ? 0.5462 0.3936 0.4651 0.0930  0.1262  -0.0565 320 ARG A NH1 
574  N NH2 . ARG A 309 ? 0.5797 0.4096 0.4871 0.0747  0.1068  -0.0698 320 ARG A NH2 
575  N N   . GLU A 310 ? 0.3926 0.3773 0.4275 0.0782  0.0974  0.0038  321 GLU A N   
576  C CA  . GLU A 310 ? 0.4520 0.4713 0.5025 0.0733  0.1011  0.0120  321 GLU A CA  
577  C C   . GLU A 310 ? 0.5150 0.5496 0.5702 0.0599  0.0933  0.0146  321 GLU A C   
578  O O   . GLU A 310 ? 0.5253 0.5958 0.5943 0.0529  0.0936  0.0218  321 GLU A O   
579  C CB  . GLU A 310 ? 0.4404 0.4637 0.4813 0.0666  0.1094  0.0110  321 GLU A CB  
580  C CG  . GLU A 310 ? 0.5396 0.5522 0.5748 0.0799  0.1197  0.0085  321 GLU A CG  
581  C CD  . GLU A 310 ? 0.7359 0.7444 0.7545 0.0731  0.1280  0.0066  321 GLU A CD  
582  O OE1 . GLU A 310 ? 0.7561 0.7717 0.7710 0.0576  0.1273  0.0085  321 GLU A OE1 
583  O OE2 . GLU A 310 ? 0.7407 0.7355 0.7468 0.0821  0.1368  0.0025  321 GLU A OE2 
584  N N   . ASN A 311 ? 0.4328 0.4442 0.4763 0.0555  0.0871  0.0091  322 ASN A N   
585  C CA  . ASN A 311 ? 0.4038 0.4223 0.4446 0.0412  0.0832  0.0085  322 ASN A CA  
586  C C   . ASN A 311 ? 0.5172 0.5243 0.5596 0.0460  0.0771  0.0077  322 ASN A C   
587  O O   . ASN A 311 ? 0.5782 0.5628 0.6085 0.0433  0.0764  0.0024  322 ASN A O   
588  C CB  . ASN A 311 ? 0.4708 0.4682 0.4909 0.0280  0.0880  0.0023  322 ASN A CB  
589  C CG  . ASN A 311 ? 0.5393 0.5477 0.5571 0.0205  0.0955  0.0036  322 ASN A CG  
590  O OD1 . ASN A 311 ? 0.5372 0.5754 0.5622 0.0058  0.0970  0.0059  322 ASN A OD1 
591  N ND2 . ASN A 311 ? 0.4447 0.4326 0.4518 0.0288  0.1002  0.0025  322 ASN A ND2 
592  N N   . LYS A 312 ? 0.4051 0.4282 0.4633 0.0544  0.0742  0.0147  323 LYS A N   
593  C CA  . LYS A 312 ? 0.4125 0.4276 0.4730 0.0570  0.0698  0.0153  323 LYS A CA  
594  C C   . LYS A 312 ? 0.4504 0.4853 0.5091 0.0445  0.0671  0.0178  323 LYS A C   
595  O O   . LYS A 312 ? 0.4011 0.4677 0.4651 0.0373  0.0661  0.0239  323 LYS A O   
596  C CB  . LYS A 312 ? 0.5020 0.5173 0.5765 0.0710  0.0705  0.0221  323 LYS A CB  
597  C CG  . LYS A 312 ? 0.4936 0.4837 0.5628 0.0790  0.0741  0.0152  323 LYS A CG  
598  C CD  . LYS A 312 ? 0.4855 0.4638 0.5627 0.0901  0.0783  0.0185  323 LYS A CD  
599  C CE  . LYS A 312 ? 0.5122 0.4622 0.5769 0.0917  0.0808  0.0072  323 LYS A CE  
600  N NZ  . LYS A 312 ? 0.6412 0.5706 0.7087 0.0996  0.0886  0.0072  323 LYS A NZ  
601  N N   . ASN A 313 ? 0.3748 0.3943 0.4254 0.0411  0.0661  0.0134  324 ASN A N   
602  C CA  . ASN A 313 ? 0.4354 0.4662 0.4761 0.0268  0.0660  0.0119  324 ASN A CA  
603  C C   . ASN A 313 ? 0.3977 0.4125 0.4352 0.0300  0.0669  0.0098  324 ASN A C   
604  O O   . ASN A 313 ? 0.3909 0.3830 0.4295 0.0387  0.0686  0.0060  324 ASN A O   
605  C CB  . ASN A 313 ? 0.3997 0.4194 0.4214 0.0109  0.0715  0.0021  324 ASN A CB  
606  C CG  . ASN A 313 ? 0.4418 0.4695 0.4473 -0.0083 0.0731  -0.0030 324 ASN A CG  
607  O OD1 . ASN A 313 ? 0.4208 0.4239 0.4118 -0.0107 0.0791  -0.0103 324 ASN A OD1 
608  N ND2 . ASN A 313 ? 0.4499 0.5145 0.4568 -0.0229 0.0687  0.0008  324 ASN A ND2 
609  N N   . PRO A 314 ? 0.3401 0.3703 0.3739 0.0230  0.0659  0.0131  325 PRO A N   
610  C CA  . PRO A 314 ? 0.4369 0.4539 0.4686 0.0261  0.0690  0.0116  325 PRO A CA  
611  C C   . PRO A 314 ? 0.4025 0.3905 0.4204 0.0248  0.0775  0.0004  325 PRO A C   
612  O O   . PRO A 314 ? 0.3693 0.3478 0.3924 0.0325  0.0808  0.0006  325 PRO A O   
613  C CB  . PRO A 314 ? 0.4439 0.4852 0.4674 0.0154  0.0674  0.0167  325 PRO A CB  
614  C CG  . PRO A 314 ? 0.4012 0.4755 0.4341 0.0143  0.0601  0.0274  325 PRO A CG  
615  C CD  . PRO A 314 ? 0.4506 0.5172 0.4839 0.0126  0.0612  0.0206  325 PRO A CD  
616  N N   . ASN A 315 ? 0.3905 0.3646 0.3916 0.0155  0.0830  -0.0080 326 ASN A N   
617  C CA  . ASN A 315 ? 0.3769 0.3180 0.3637 0.0176  0.0947  -0.0162 326 ASN A CA  
618  C C   . ASN A 315 ? 0.3580 0.2820 0.3502 0.0300  0.0949  -0.0147 326 ASN A C   
619  O O   . ASN A 315 ? 0.3846 0.2801 0.3625 0.0320  0.1056  -0.0188 326 ASN A O   
620  C CB  . ASN A 315 ? 0.3932 0.3195 0.3515 -0.0022 0.1050  -0.0272 326 ASN A CB  
621  C CG  . ASN A 315 ? 0.4239 0.3619 0.3691 -0.0149 0.1075  -0.0308 326 ASN A CG  
622  O OD1 . ASN A 315 ? 0.4562 0.4178 0.3911 -0.0340 0.1024  -0.0325 326 ASN A OD1 
623  N ND2 . ASN A 315 ? 0.4122 0.3375 0.3570 -0.0050 0.1156  -0.0314 326 ASN A ND2 
624  N N   . ILE A 316 ? 0.3584 0.2971 0.3680 0.0384  0.0848  -0.0084 327 ILE A N   
625  C CA  . ILE A 316 ? 0.3465 0.2743 0.3595 0.0493  0.0830  -0.0066 327 ILE A CA  
626  C C   . ILE A 316 ? 0.3718 0.3101 0.4032 0.0603  0.0751  -0.0021 327 ILE A C   
627  O O   . ILE A 316 ? 0.4539 0.4072 0.4969 0.0587  0.0704  0.0005  327 ILE A O   
628  C CB  . ILE A 316 ? 0.3522 0.2856 0.3626 0.0444  0.0805  -0.0065 327 ILE A CB  
629  C CG1 . ILE A 316 ? 0.3686 0.2904 0.3599 0.0298  0.0893  -0.0117 327 ILE A CG1 
630  C CG2 . ILE A 316 ? 0.4548 0.3809 0.4671 0.0552  0.0773  -0.0043 327 ILE A CG2 
631  C CD1 . ILE A 316 ? 0.4923 0.4275 0.4842 0.0225  0.0878  -0.0106 327 ILE A CD1 
632  N N   . VAL A 317 ? 0.3223 0.2537 0.3559 0.0704  0.0744  -0.0002 328 VAL A N   
633  C CA  . VAL A 317 ? 0.3114 0.2562 0.3606 0.0756  0.0656  0.0024  328 VAL A CA  
634  C C   . VAL A 317 ? 0.3637 0.3099 0.4118 0.0730  0.0598  0.0004  328 VAL A C   
635  O O   . VAL A 317 ? 0.3990 0.3383 0.4368 0.0753  0.0592  -0.0004 328 VAL A O   
636  C CB  . VAL A 317 ? 0.3192 0.2657 0.3714 0.0860  0.0643  0.0068  328 VAL A CB  
637  C CG1 . VAL A 317 ? 0.3442 0.3100 0.4110 0.0853  0.0534  0.0077  328 VAL A CG1 
638  C CG2 . VAL A 317 ? 0.3419 0.2852 0.3966 0.0925  0.0744  0.0100  328 VAL A CG2 
639  N N   . ASN A 318 ? 0.3341 0.2870 0.3913 0.0696  0.0576  0.0004  329 ASN A N   
640  C CA  . ASN A 318 ? 0.3623 0.3128 0.4174 0.0695  0.0573  -0.0010 329 ASN A CA  
641  C C   . ASN A 318 ? 0.3573 0.3014 0.4105 0.0705  0.0531  -0.0056 329 ASN A C   
642  O O   . ASN A 318 ? 0.3812 0.3288 0.4402 0.0681  0.0483  -0.0069 329 ASN A O   
643  C CB  . ASN A 318 ? 0.4103 0.3684 0.4745 0.0686  0.0597  0.0038  329 ASN A CB  
644  C CG  . ASN A 318 ? 0.4930 0.4631 0.5538 0.0641  0.0624  0.0072  329 ASN A CG  
645  O OD1 . ASN A 318 ? 0.4087 0.3806 0.4616 0.0612  0.0645  0.0056  329 ASN A OD1 
646  N ND2 . ASN A 318 ? 0.5494 0.5285 0.6140 0.0607  0.0627  0.0112  329 ASN A ND2 
647  N N   . TYR A 319 ? 0.3719 0.3090 0.4154 0.0721  0.0556  -0.0086 330 TYR A N   
648  C CA  . TYR A 319 ? 0.3567 0.2838 0.3919 0.0707  0.0542  -0.0156 330 TYR A CA  
649  C C   . TYR A 319 ? 0.4238 0.3406 0.4661 0.0702  0.0595  -0.0171 330 TYR A C   
650  O O   . TYR A 319 ? 0.4804 0.3986 0.5303 0.0760  0.0663  -0.0109 330 TYR A O   
651  C CB  . TYR A 319 ? 0.4846 0.4057 0.5039 0.0736  0.0584  -0.0181 330 TYR A CB  
652  C CG  . TYR A 319 ? 0.5625 0.4690 0.5688 0.0723  0.0619  -0.0270 330 TYR A CG  
653  C CD1 . TYR A 319 ? 0.5168 0.4120 0.5272 0.0769  0.0726  -0.0282 330 TYR A CD1 
654  C CD2 . TYR A 319 ? 0.4750 0.3788 0.4628 0.0673  0.0561  -0.0336 330 TYR A CD2 
655  C CE1 . TYR A 319 ? 0.5810 0.4551 0.5756 0.0761  0.0801  -0.0384 330 TYR A CE1 
656  C CE2 . TYR A 319 ? 0.4797 0.3669 0.4495 0.0632  0.0608  -0.0447 330 TYR A CE2 
657  C CZ  . TYR A 319 ? 0.5934 0.4622 0.5658 0.0674  0.0743  -0.0483 330 TYR A CZ  
658  O OH  . TYR A 319 ? 0.5772 0.4222 0.5281 0.0636  0.0830  -0.0612 330 TYR A OH  
659  N N   . LEU A 320 ? 0.4060 0.3132 0.4456 0.0627  0.0569  -0.0241 331 LEU A N   
660  C CA  . LEU A 320 ? 0.3738 0.2614 0.4164 0.0605  0.0647  -0.0264 331 LEU A CA  
661  C C   . LEU A 320 ? 0.5480 0.4100 0.5715 0.0581  0.0721  -0.0382 331 LEU A C   
662  O O   . LEU A 320 ? 0.5402 0.3819 0.5631 0.0662  0.0856  -0.0369 331 LEU A O   
663  C CB  . LEU A 320 ? 0.3755 0.2659 0.4276 0.0491  0.0598  -0.0273 331 LEU A CB  
664  C CG  . LEU A 320 ? 0.4980 0.4109 0.5669 0.0521  0.0558  -0.0164 331 LEU A CG  
665  C CD1 . LEU A 320 ? 0.4008 0.3213 0.4806 0.0406  0.0520  -0.0170 331 LEU A CD1 
666  C CD2 . LEU A 320 ? 0.5255 0.4368 0.6017 0.0618  0.0637  -0.0058 331 LEU A CD2 
667  N N   . ASP A 321 ? 0.4689 0.3317 0.4758 0.0473  0.0646  -0.0490 332 ASP A N   
668  C CA  . ASP A 321 ? 0.5455 0.3815 0.5281 0.0403  0.0720  -0.0637 332 ASP A CA  
669  C C   . ASP A 321 ? 0.5249 0.3767 0.4883 0.0310  0.0597  -0.0709 332 ASP A C   
670  O O   . ASP A 321 ? 0.4439 0.3257 0.4163 0.0309  0.0461  -0.0630 332 ASP A O   
671  C CB  . ASP A 321 ? 0.5597 0.3691 0.5395 0.0266  0.0781  -0.0728 332 ASP A CB  
672  C CG  . ASP A 321 ? 0.7836 0.5492 0.7487 0.0323  0.0993  -0.0801 332 ASP A CG  
673  O OD1 . ASP A 321 ? 0.7202 0.4746 0.6654 0.0374  0.1067  -0.0875 332 ASP A OD1 
674  O OD2 . ASP A 321 ? 0.8642 0.6046 0.8370 0.0329  0.1107  -0.0773 332 ASP A OD2 
675  N N   . SER A 322 ? 0.5153 0.3461 0.4503 0.0246  0.0660  -0.0848 333 SER A N   
676  C CA  . SER A 322 ? 0.5780 0.4249 0.4896 0.0134  0.0537  -0.0916 333 SER A CA  
677  C C   . SER A 322 ? 0.6711 0.4868 0.5489 -0.0029 0.0622  -0.1128 333 SER A C   
678  O O   . SER A 322 ? 0.6551 0.4322 0.5257 0.0021  0.0822  -0.1202 333 SER A O   
679  C CB  . SER A 322 ? 0.5039 0.3656 0.4093 0.0275  0.0525  -0.0819 333 SER A CB  
680  O OG  . SER A 322 ? 0.5997 0.4381 0.4978 0.0390  0.0706  -0.0839 333 SER A OG  
681  N N   . TYR A 323 ? 0.5953 0.4287 0.4512 -0.0223 0.0479  -0.1219 334 TYR A N   
682  C CA  . TYR A 323 ? 0.6535 0.4594 0.4721 -0.0454 0.0537  -0.1455 334 TYR A CA  
683  C C   . TYR A 323 ? 0.6753 0.5061 0.4614 -0.0559 0.0402  -0.1503 334 TYR A C   
684  O O   . TYR A 323 ? 0.6501 0.5284 0.4475 -0.0547 0.0195  -0.1360 334 TYR A O   
685  C CB  . TYR A 323 ? 0.6729 0.4764 0.4962 -0.0716 0.0480  -0.1561 334 TYR A CB  
686  C CG  . TYR A 323 ? 0.6762 0.4561 0.5291 -0.0637 0.0604  -0.1498 334 TYR A CG  
687  C CD1 . TYR A 323 ? 0.6109 0.4244 0.5035 -0.0521 0.0501  -0.1298 334 TYR A CD1 
688  C CD2 . TYR A 323 ? 0.7826 0.5047 0.6216 -0.0671 0.0842  -0.1628 334 TYR A CD2 
689  C CE1 . TYR A 323 ? 0.5934 0.3877 0.5100 -0.0455 0.0611  -0.1226 334 TYR A CE1 
690  C CE2 . TYR A 323 ? 0.7062 0.4074 0.5711 -0.0582 0.0958  -0.1535 334 TYR A CE2 
691  C CZ  . TYR A 323 ? 0.6928 0.4323 0.5958 -0.0482 0.0831  -0.1333 334 TYR A CZ  
692  O OH  . TYR A 323 ? 0.7922 0.5130 0.7177 -0.0401 0.0944  -0.1228 334 TYR A OH  
693  N N   . LEU A 324 ? 0.7271 0.5246 0.4714 -0.0651 0.0536  -0.1696 335 LEU A N   
694  C CA  . LEU A 324 ? 0.8195 0.6357 0.5229 -0.0816 0.0422  -0.1788 335 LEU A CA  
695  C C   . LEU A 324 ? 0.8423 0.6529 0.5184 -0.1193 0.0357  -0.2024 335 LEU A C   
696  O O   . LEU A 324 ? 0.8629 0.6194 0.5171 -0.1322 0.0565  -0.2248 335 LEU A O   
697  C CB  . LEU A 324 ? 0.8536 0.6370 0.5218 -0.0716 0.0625  -0.1875 335 LEU A CB  
698  C CG  . LEU A 324 ? 0.8979 0.6974 0.5748 -0.0443 0.0651  -0.1673 335 LEU A CG  
699  C CD1 . LEU A 324 ? 0.8221 0.5921 0.4541 -0.0442 0.0846  -0.1816 335 LEU A CD1 
700  C CD2 . LEU A 324 ? 0.7874 0.6418 0.4735 -0.0421 0.0388  -0.1467 335 LEU A CD2 
701  N N   . VAL A 325 ? 0.8117 0.6782 0.4893 -0.1371 0.0082  -0.1969 336 VAL A N   
702  C CA  . VAL A 325 ? 0.9618 0.8372 0.6123 -0.1786 -0.0026 -0.2188 336 VAL A CA  
703  C C   . VAL A 325 ? 1.0205 0.9361 0.6310 -0.1917 -0.0207 -0.2203 336 VAL A C   
704  O O   . VAL A 325 ? 0.8698 0.8536 0.4967 -0.1912 -0.0475 -0.2004 336 VAL A O   
705  C CB  . VAL A 325 ? 0.8783 0.7954 0.5695 -0.1921 -0.0205 -0.2098 336 VAL A CB  
706  C CG1 . VAL A 325 ? 0.9633 0.8841 0.6251 -0.2404 -0.0282 -0.2360 336 VAL A CG1 
707  C CG2 . VAL A 325 ? 0.8566 0.7392 0.5883 -0.1734 -0.0034 -0.2023 336 VAL A CG2 
708  N N   . GLY A 326 ? 1.0606 0.9347 0.6173 -0.2028 -0.0049 -0.2430 337 GLY A N   
709  C CA  . GLY A 326 ? 1.0223 0.9311 0.5343 -0.2150 -0.0199 -0.2446 337 GLY A CA  
710  C C   . GLY A 326 ? 1.1278 1.0743 0.6610 -0.1783 -0.0291 -0.2109 337 GLY A C   
711  O O   . GLY A 326 ? 1.0152 0.9279 0.5575 -0.1482 -0.0089 -0.2026 337 GLY A O   
712  N N   . ASP A 327 ? 0.9971 1.0152 0.5391 -0.1805 -0.0588 -0.1898 338 ASP A N   
713  C CA  . ASP A 327 ? 0.8810 0.9331 0.4428 -0.1461 -0.0670 -0.1555 338 ASP A CA  
714  C C   . ASP A 327 ? 0.8696 0.9458 0.4956 -0.1223 -0.0735 -0.1300 338 ASP A C   
715  O O   . ASP A 327 ? 0.9096 1.0180 0.5552 -0.0960 -0.0822 -0.1002 338 ASP A O   
716  C CB  . ASP A 327 ? 0.9110 1.0265 0.4430 -0.1566 -0.0931 -0.1425 338 ASP A CB  
717  C CG  . ASP A 327 ? 1.1337 1.2255 0.5995 -0.1688 -0.0839 -0.1592 338 ASP A CG  
718  O OD1 . ASP A 327 ? 1.1360 1.1735 0.5898 -0.1507 -0.0576 -0.1643 338 ASP A OD1 
719  O OD2 . ASP A 327 ? 1.2623 1.3935 0.6875 -0.1973 -0.1030 -0.1667 338 ASP A OD2 
720  N N   . GLU A 328 ? 0.8473 0.9045 0.5035 -0.1306 -0.0674 -0.1410 339 GLU A N   
721  C CA  . GLU A 328 ? 0.7843 0.8592 0.4981 -0.1100 -0.0705 -0.1200 339 GLU A CA  
722  C C   . GLU A 328 ? 0.7048 0.7230 0.4392 -0.0879 -0.0451 -0.1215 339 GLU A C   
723  O O   . GLU A 328 ? 0.7368 0.7036 0.4556 -0.0980 -0.0262 -0.1438 339 GLU A O   
724  C CB  . GLU A 328 ? 0.8671 0.9720 0.6020 -0.1370 -0.0839 -0.1280 339 GLU A CB  
725  C CG  . GLU A 328 ? 0.9925 1.1765 0.7256 -0.1518 -0.1136 -0.1154 339 GLU A CG  
726  C CD  . GLU A 328 ? 0.9858 1.2089 0.7450 -0.1801 -0.1274 -0.1214 339 GLU A CD  
727  O OE1 . GLU A 328 ? 0.9147 1.0964 0.6888 -0.1903 -0.1125 -0.1370 339 GLU A OE1 
728  O OE2 . GLU A 328 ? 0.9973 1.2956 0.7623 -0.1925 -0.1528 -0.1090 339 GLU A OE2 
729  N N   . LEU A 329 ? 0.6564 0.6848 0.4248 -0.0581 -0.0439 -0.0970 340 LEU A N   
730  C CA  . LEU A 329 ? 0.6209 0.6116 0.4163 -0.0385 -0.0249 -0.0940 340 LEU A CA  
731  C C   . LEU A 329 ? 0.6456 0.6569 0.4859 -0.0354 -0.0313 -0.0839 340 LEU A C   
732  O O   . LEU A 329 ? 0.5636 0.6192 0.4244 -0.0271 -0.0460 -0.0648 340 LEU A O   
733  C CB  . LEU A 329 ? 0.6005 0.5848 0.3969 -0.0116 -0.0170 -0.0762 340 LEU A CB  
734  C CG  . LEU A 329 ? 0.5932 0.5517 0.4200 0.0074  -0.0011 -0.0695 340 LEU A CG  
735  C CD1 . LEU A 329 ? 0.5742 0.4898 0.3951 0.0025  0.0178  -0.0881 340 LEU A CD1 
736  C CD2 . LEU A 329 ? 0.6894 0.6462 0.5144 0.0280  0.0050  -0.0524 340 LEU A CD2 
737  N N   . TRP A 330 ? 0.5775 0.5570 0.4321 -0.0411 -0.0188 -0.0953 341 TRP A N   
738  C CA  . TRP A 330 ? 0.5432 0.5364 0.4385 -0.0375 -0.0211 -0.0860 341 TRP A CA  
739  C C   . TRP A 330 ? 0.5112 0.4744 0.4256 -0.0149 -0.0045 -0.0783 341 TRP A C   
740  O O   . TRP A 330 ? 0.5234 0.4460 0.4274 -0.0137 0.0120  -0.0888 341 TRP A O   
741  C CB  . TRP A 330 ? 0.5676 0.5517 0.4631 -0.0652 -0.0208 -0.1034 341 TRP A CB  
742  C CG  . TRP A 330 ? 0.6465 0.6682 0.5244 -0.0930 -0.0392 -0.1118 341 TRP A CG  
743  C CD1 . TRP A 330 ? 0.7113 0.7269 0.5456 -0.1106 -0.0424 -0.1277 341 TRP A CD1 
744  C CD2 . TRP A 330 ? 0.5935 0.6697 0.4962 -0.1080 -0.0573 -0.1048 341 TRP A CD2 
745  N NE1 . TRP A 330 ? 0.7388 0.8042 0.5681 -0.1376 -0.0632 -0.1310 341 TRP A NE1 
746  C CE2 . TRP A 330 ? 0.6361 0.7419 0.5096 -0.1360 -0.0729 -0.1163 341 TRP A CE2 
747  C CE3 . TRP A 330 ? 0.6217 0.7281 0.5683 -0.1009 -0.0612 -0.0895 341 TRP A CE3 
748  C CZ2 . TRP A 330 ? 0.6411 0.8110 0.5315 -0.1575 -0.0937 -0.1116 341 TRP A CZ2 
749  C CZ3 . TRP A 330 ? 0.5777 0.7446 0.5423 -0.1199 -0.0795 -0.0849 341 TRP A CZ3 
750  C CH2 . TRP A 330 ? 0.6034 0.8043 0.5417 -0.1483 -0.0963 -0.0952 341 TRP A CH2 
751  N N   . VAL A 331 ? 0.4745 0.4589 0.4160 0.0028  -0.0078 -0.0597 342 VAL A N   
752  C CA  . VAL A 331 ? 0.4464 0.4099 0.4041 0.0207  0.0055  -0.0521 342 VAL A CA  
753  C C   . VAL A 331 ? 0.4229 0.3950 0.4117 0.0205  0.0056  -0.0467 342 VAL A C   
754  O O   . VAL A 331 ? 0.4127 0.4179 0.4185 0.0198  -0.0049 -0.0381 342 VAL A O   
755  C CB  . VAL A 331 ? 0.4871 0.4588 0.4432 0.0391  0.0056  -0.0371 342 VAL A CB  
756  C CG1 . VAL A 331 ? 0.4352 0.3913 0.4083 0.0520  0.0175  -0.0305 342 VAL A CG1 
757  C CG2 . VAL A 331 ? 0.5239 0.4832 0.4475 0.0390  0.0087  -0.0421 342 VAL A CG2 
758  N N   . VAL A 332 ? 0.4164 0.3616 0.4132 0.0226  0.0181  -0.0499 343 VAL A N   
759  C CA  . VAL A 332 ? 0.4000 0.3490 0.4218 0.0209  0.0203  -0.0453 343 VAL A CA  
760  C C   . VAL A 332 ? 0.3730 0.3201 0.4082 0.0379  0.0273  -0.0337 343 VAL A C   
761  O O   . VAL A 332 ? 0.3727 0.3004 0.4016 0.0456  0.0368  -0.0338 343 VAL A O   
762  C CB  . VAL A 332 ? 0.4236 0.3426 0.4419 0.0088  0.0299  -0.0561 343 VAL A CB  
763  C CG1 . VAL A 332 ? 0.4087 0.3346 0.4517 0.0053  0.0315  -0.0493 343 VAL A CG1 
764  C CG2 . VAL A 332 ? 0.4602 0.3728 0.4570 -0.0123 0.0257  -0.0721 343 VAL A CG2 
765  N N   . MET A 333 ? 0.3526 0.3219 0.4061 0.0426  0.0235  -0.0239 344 MET A N   
766  C CA  . MET A 333 ? 0.4296 0.3979 0.4920 0.0545  0.0301  -0.0150 344 MET A CA  
767  C C   . MET A 333 ? 0.3795 0.3554 0.4613 0.0515  0.0327  -0.0109 344 MET A C   
768  O O   . MET A 333 ? 0.3444 0.3321 0.4364 0.0412  0.0285  -0.0127 344 MET A O   
769  C CB  . MET A 333 ? 0.4184 0.3992 0.4788 0.0654  0.0277  -0.0069 344 MET A CB  
770  C CG  . MET A 333 ? 0.4112 0.3887 0.4516 0.0677  0.0240  -0.0083 344 MET A CG  
771  S SD  . MET A 333 ? 0.4073 0.3582 0.4310 0.0698  0.0341  -0.0130 344 MET A SD  
772  C CE  . MET A 333 ? 0.4049 0.3513 0.4321 0.0782  0.0424  -0.0044 344 MET A CE  
773  N N   . GLU A 334 ? 0.3374 0.3081 0.4226 0.0580  0.0400  -0.0056 345 GLU A N   
774  C CA  . GLU A 334 ? 0.3562 0.3368 0.4563 0.0566  0.0434  -0.0003 345 GLU A CA  
775  C C   . GLU A 334 ? 0.2994 0.3032 0.4109 0.0595  0.0400  0.0038  345 GLU A C   
776  O O   . GLU A 334 ? 0.3589 0.3679 0.4651 0.0679  0.0376  0.0060  345 GLU A O   
777  C CB  . GLU A 334 ? 0.3686 0.3440 0.4647 0.0620  0.0508  0.0041  345 GLU A CB  
778  C CG  . GLU A 334 ? 0.4306 0.3946 0.5211 0.0617  0.0542  0.0050  345 GLU A CG  
779  C CD  . GLU A 334 ? 0.6628 0.6315 0.7480 0.0632  0.0587  0.0093  345 GLU A CD  
780  O OE1 . GLU A 334 ? 0.4093 0.3783 0.4868 0.0643  0.0606  0.0072  345 GLU A OE1 
781  O OE2 . GLU A 334 ? 0.7519 0.7235 0.8391 0.0626  0.0610  0.0151  345 GLU A OE2 
782  N N   . TYR A 335 ? 0.2973 0.3166 0.4259 0.0540  0.0412  0.0068  346 TYR A N   
783  C CA  . TYR A 335 ? 0.3146 0.3629 0.4598 0.0587  0.0399  0.0131  346 TYR A CA  
784  C C   . TYR A 335 ? 0.3137 0.3624 0.4641 0.0667  0.0518  0.0186  346 TYR A C   
785  O O   . TYR A 335 ? 0.3180 0.3599 0.4694 0.0602  0.0576  0.0186  346 TYR A O   
786  C CB  . TYR A 335 ? 0.3644 0.4375 0.5271 0.0439  0.0330  0.0122  346 TYR A CB  
787  C CG  . TYR A 335 ? 0.2965 0.4096 0.4832 0.0495  0.0328  0.0216  346 TYR A CG  
788  C CD1 . TYR A 335 ? 0.2983 0.4345 0.4892 0.0631  0.0275  0.0289  346 TYR A CD1 
789  C CD2 . TYR A 335 ? 0.3000 0.4300 0.5065 0.0425  0.0391  0.0255  346 TYR A CD2 
790  C CE1 . TYR A 335 ? 0.2971 0.4747 0.5141 0.0723  0.0290  0.0408  346 TYR A CE1 
791  C CE2 . TYR A 335 ? 0.3550 0.5265 0.5869 0.0492  0.0408  0.0353  346 TYR A CE2 
792  C CZ  . TYR A 335 ? 0.3258 0.5223 0.5644 0.0651  0.0358  0.0433  346 TYR A CZ  
793  O OH  . TYR A 335 ? 0.2926 0.5346 0.5601 0.0756  0.0391  0.0562  346 TYR A OH  
794  N N   . LEU A 336 ? 0.4802 0.2442 0.4500 -0.0039 0.1108  -0.0444 347 LEU A N   
795  C CA  . LEU A 336 ? 0.4846 0.2671 0.4582 0.0038  0.0998  -0.0288 347 LEU A CA  
796  C C   . LEU A 336 ? 0.4490 0.2442 0.4232 -0.0144 0.0962  -0.0344 347 LEU A C   
797  O O   . LEU A 336 ? 0.4731 0.2955 0.4491 -0.0244 0.0857  -0.0437 347 LEU A O   
798  C CB  . LEU A 336 ? 0.4482 0.2624 0.4259 0.0148  0.0843  -0.0234 347 LEU A CB  
799  C CG  . LEU A 336 ? 0.4728 0.2840 0.4541 0.0357  0.0853  -0.0115 347 LEU A CG  
800  C CD1 . LEU A 336 ? 0.5896 0.3900 0.5703 0.0474  0.0876  0.0055  347 LEU A CD1 
801  C CD2 . LEU A 336 ? 0.4614 0.2494 0.4424 0.0406  0.0994  -0.0187 347 LEU A CD2 
802  N N   . ALA A 337 ? 0.4618 0.2385 0.4346 -0.0182 0.1054  -0.0279 348 ALA A N   
803  C CA  . ALA A 337 ? 0.4583 0.2464 0.4337 -0.0378 0.1055  -0.0354 348 ALA A CA  
804  C C   . ALA A 337 ? 0.4577 0.2812 0.4386 -0.0348 0.0911  -0.0284 348 ALA A C   
805  O O   . ALA A 337 ? 0.5163 0.3587 0.5026 -0.0493 0.0890  -0.0351 348 ALA A O   
806  C CB  . ALA A 337 ? 0.5165 0.2699 0.4877 -0.0453 0.1231  -0.0314 348 ALA A CB  
807  N N   . GLY A 338 ? 0.3871 0.2212 0.3673 -0.0169 0.0816  -0.0161 349 GLY A N   
808  C CA  . GLY A 338 ? 0.4160 0.2793 0.3996 -0.0138 0.0696  -0.0109 349 GLY A CA  
809  C C   . GLY A 338 ? 0.4143 0.3080 0.4027 -0.0172 0.0561  -0.0196 349 GLY A C   
810  O O   . GLY A 338 ? 0.3882 0.3039 0.3797 -0.0142 0.0473  -0.0163 349 GLY A O   
811  N N   . GLY A 339 ? 0.4007 0.2948 0.3882 -0.0221 0.0548  -0.0299 350 GLY A N   
812  C CA  . GLY A 339 ? 0.3802 0.3016 0.3694 -0.0246 0.0421  -0.0361 350 GLY A CA  
813  C C   . GLY A 339 ? 0.3335 0.2614 0.3198 -0.0103 0.0329  -0.0287 350 GLY A C   
814  O O   . GLY A 339 ? 0.3565 0.2714 0.3407 0.0007  0.0356  -0.0205 350 GLY A O   
815  N N   . SER A 340 ? 0.3470 0.2964 0.3332 -0.0109 0.0218  -0.0313 351 SER A N   
816  C CA  . SER A 340 ? 0.2968 0.2516 0.2793 -0.0007 0.0137  -0.0255 351 SER A CA  
817  C C   . SER A 340 ? 0.2695 0.2309 0.2534 0.0083  0.0077  -0.0163 351 SER A C   
818  O O   . SER A 340 ? 0.2991 0.2685 0.2870 0.0070  0.0070  -0.0155 351 SER A O   
819  C CB  . SER A 340 ? 0.3377 0.3084 0.3163 -0.0051 0.0057  -0.0310 351 SER A CB  
820  O OG  . SER A 340 ? 0.3518 0.3415 0.3343 -0.0063 -0.0019 -0.0303 351 SER A OG  
821  N N   . LEU A 341 ? 0.2772 0.2369 0.2577 0.0166  0.0037  -0.0107 352 LEU A N   
822  C CA  . LEU A 341 ? 0.2861 0.2516 0.2652 0.0232  -0.0026 -0.0046 352 LEU A CA  
823  C C   . LEU A 341 ? 0.2767 0.2549 0.2555 0.0223  -0.0099 -0.0066 352 LEU A C   
824  O O   . LEU A 341 ? 0.2559 0.2382 0.2352 0.0266  -0.0123 -0.0040 352 LEU A O   
825  C CB  . LEU A 341 ? 0.2972 0.2603 0.2731 0.0291  -0.0053 -0.0002 352 LEU A CB  
826  C CG  . LEU A 341 ? 0.2535 0.2204 0.2256 0.0336  -0.0114 0.0039  352 LEU A CG  
827  C CD1 . LEU A 341 ? 0.3046 0.2700 0.2761 0.0369  -0.0086 0.0077  352 LEU A CD1 
828  C CD2 . LEU A 341 ? 0.3242 0.2926 0.2947 0.0357  -0.0141 0.0064  352 LEU A CD2 
829  N N   . THR A 342 ? 0.2826 0.2672 0.2597 0.0177  -0.0131 -0.0110 353 THR A N   
830  C CA  . THR A 342 ? 0.3175 0.3155 0.2943 0.0192  -0.0205 -0.0107 353 THR A CA  
831  C C   . THR A 342 ? 0.3127 0.3232 0.2984 0.0189  -0.0199 -0.0121 353 THR A C   
832  O O   . THR A 342 ? 0.2822 0.3001 0.2698 0.0260  -0.0241 -0.0089 353 THR A O   
833  C CB  . THR A 342 ? 0.3274 0.3333 0.2995 0.0133  -0.0238 -0.0148 353 THR A CB  
834  O OG1 . THR A 342 ? 0.3036 0.2992 0.2677 0.0129  -0.0225 -0.0139 353 THR A OG1 
835  C CG2 . THR A 342 ? 0.3325 0.3523 0.3027 0.0179  -0.0326 -0.0113 353 THR A CG2 
836  N N   . ASP A 343 ? 0.2821 0.2948 0.2738 0.0103  -0.0136 -0.0174 354 ASP A N   
837  C CA  . ASP A 343 ? 0.2886 0.3162 0.2907 0.0078  -0.0116 -0.0192 354 ASP A CA  
838  C C   . ASP A 343 ? 0.3377 0.3600 0.3402 0.0162  -0.0089 -0.0133 354 ASP A C   
839  O O   . ASP A 343 ? 0.2776 0.3150 0.2870 0.0203  -0.0102 -0.0129 354 ASP A O   
840  C CB  . ASP A 343 ? 0.2614 0.2866 0.2682 -0.0055 -0.0028 -0.0260 354 ASP A CB  
841  C CG  . ASP A 343 ? 0.4274 0.4613 0.4332 -0.0165 -0.0049 -0.0350 354 ASP A CG  
842  O OD1 . ASP A 343 ? 0.3802 0.4280 0.3825 -0.0136 -0.0144 -0.0351 354 ASP A OD1 
843  O OD2 . ASP A 343 ? 0.4449 0.4700 0.4516 -0.0285 0.0036  -0.0422 354 ASP A OD2 
844  N N   . VAL A 344 ? 0.2859 0.2892 0.2811 0.0193  -0.0051 -0.0091 355 VAL A N   
845  C CA  . VAL A 344 ? 0.2897 0.2886 0.2817 0.0264  -0.0031 -0.0041 355 VAL A CA  
846  C C   . VAL A 344 ? 0.2835 0.2851 0.2714 0.0352  -0.0102 -0.0026 355 VAL A C   
847  O O   . VAL A 344 ? 0.2677 0.2752 0.2571 0.0404  -0.0091 -0.0024 355 VAL A O   
848  C CB  . VAL A 344 ? 0.2800 0.2617 0.2644 0.0279  0.0010  0.0008  355 VAL A CB  
849  C CG1 . VAL A 344 ? 0.3182 0.2975 0.2951 0.0351  0.0000  0.0054  355 VAL A CG1 
850  C CG2 . VAL A 344 ? 0.3100 0.2836 0.2971 0.0211  0.0109  0.0011  355 VAL A CG2 
851  N N   . VAL A 345 ? 0.2949 0.2900 0.2768 0.0369  -0.0160 -0.0018 356 VAL A N   
852  C CA  . VAL A 345 ? 0.2765 0.2671 0.2521 0.0442  -0.0207 -0.0001 356 VAL A CA  
853  C C   . VAL A 345 ? 0.2904 0.2930 0.2717 0.0497  -0.0237 -0.0006 356 VAL A C   
854  O O   . VAL A 345 ? 0.2924 0.2905 0.2706 0.0578  -0.0243 0.0003  356 VAL A O   
855  C CB  . VAL A 345 ? 0.3098 0.2897 0.2772 0.0429  -0.0247 0.0014  356 VAL A CB  
856  C CG1 . VAL A 345 ? 0.3288 0.3023 0.2937 0.0398  -0.0221 0.0025  356 VAL A CG1 
857  C CG2 . VAL A 345 ? 0.3233 0.3086 0.2916 0.0397  -0.0280 0.0009  356 VAL A CG2 
858  N N   . THR A 346 ? 0.2564 0.2746 0.2456 0.0460  -0.0258 -0.0023 357 THR A N   
859  C CA  . THR A 346 ? 0.3014 0.3363 0.2973 0.0530  -0.0302 -0.0013 357 THR A CA  
860  C C   . THR A 346 ? 0.3256 0.3789 0.3348 0.0553  -0.0257 -0.0037 357 THR A C   
861  O O   . THR A 346 ? 0.2896 0.3595 0.3071 0.0643  -0.0287 -0.0024 357 THR A O   
862  C CB  . THR A 346 ? 0.4234 0.4731 0.4211 0.0479  -0.0362 -0.0021 357 THR A CB  
863  O OG1 . THR A 346 ? 0.3140 0.3738 0.3187 0.0355  -0.0323 -0.0084 357 THR A OG1 
864  C CG2 . THR A 346 ? 0.2775 0.3106 0.2611 0.0461  -0.0397 0.0007  357 THR A CG2 
865  N N   . GLU A 347 ? 0.2923 0.3448 0.3046 0.0477  -0.0181 -0.0065 358 GLU A N   
866  C CA  . GLU A 347 ? 0.3609 0.4327 0.3863 0.0468  -0.0121 -0.0090 358 GLU A CA  
867  C C   . GLU A 347 ? 0.3330 0.3939 0.3532 0.0493  -0.0037 -0.0082 358 GLU A C   
868  O O   . GLU A 347 ? 0.3228 0.3997 0.3528 0.0485  0.0031  -0.0100 358 GLU A O   
869  C CB  . GLU A 347 ? 0.3159 0.4006 0.3505 0.0318  -0.0086 -0.0136 358 GLU A CB  
870  C CG  . GLU A 347 ? 0.2575 0.3589 0.2969 0.0267  -0.0166 -0.0167 358 GLU A CG  
871  C CD  . GLU A 347 ? 0.3931 0.5258 0.4453 0.0355  -0.0236 -0.0160 358 GLU A CD  
872  O OE1 . GLU A 347 ? 0.3636 0.5079 0.4250 0.0444  -0.0202 -0.0148 358 GLU A OE1 
873  O OE2 . GLU A 347 ? 0.3959 0.5435 0.4488 0.0341  -0.0323 -0.0166 358 GLU A OE2 
874  N N   . THR A 348 ? 0.2761 0.3133 0.2809 0.0514  -0.0037 -0.0056 359 THR A N   
875  C CA  . THR A 348 ? 0.3349 0.3635 0.3315 0.0527  0.0034  -0.0047 359 THR A CA  
876  C C   . THR A 348 ? 0.3642 0.3761 0.3465 0.0603  0.0001  -0.0046 359 THR A C   
877  O O   . THR A 348 ? 0.3515 0.3541 0.3295 0.0624  -0.0067 -0.0041 359 THR A O   
878  C CB  . THR A 348 ? 0.3687 0.3866 0.3591 0.0441  0.0082  -0.0016 359 THR A CB  
879  O OG1 . THR A 348 ? 0.3144 0.3165 0.2949 0.0443  0.0027  0.0010  359 THR A OG1 
880  C CG2 . THR A 348 ? 0.3341 0.3608 0.3359 0.0337  0.0124  -0.0029 359 THR A CG2 
881  N N   . CYS A 349 ? 0.3343 0.3422 0.3079 0.0625  0.0059  -0.0055 360 CYS A N   
882  C CA  . CYS A 349 ? 0.3772 0.3688 0.3344 0.0656  0.0039  -0.0071 360 CYS A CA  
883  C C   . CYS A 349 ? 0.3910 0.3765 0.3371 0.0594  0.0039  -0.0032 360 CYS A C   
884  O O   . CYS A 349 ? 0.4384 0.4288 0.3828 0.0569  0.0103  -0.0002 360 CYS A O   
885  C CB  . CYS A 349 ? 0.5141 0.5066 0.4669 0.0728  0.0104  -0.0122 360 CYS A CB  
886  S SG  . CYS A 349 ? 0.5914 0.5682 0.5202 0.0717  0.0117  -0.0164 360 CYS A SG  
887  N N   . MET A 350 ? 0.3020 0.2783 0.2420 0.0570  -0.0030 -0.0020 361 MET A N   
888  C CA  . MET A 350 ? 0.3125 0.2868 0.2437 0.0536  -0.0045 0.0026  361 MET A CA  
889  C C   . MET A 350 ? 0.3658 0.3365 0.2807 0.0538  -0.0062 -0.0011 361 MET A C   
890  O O   . MET A 350 ? 0.3750 0.3379 0.2854 0.0542  -0.0088 -0.0075 361 MET A O   
891  C CB  . MET A 350 ? 0.3567 0.3284 0.2927 0.0507  -0.0105 0.0053  361 MET A CB  
892  C CG  . MET A 350 ? 0.3240 0.2980 0.2732 0.0489  -0.0091 0.0065  361 MET A CG  
893  S SD  . MET A 350 ? 0.3655 0.3364 0.3184 0.0459  -0.0141 0.0082  361 MET A SD  
894  C CE  . MET A 350 ? 0.3177 0.2888 0.2663 0.0474  -0.0125 0.0152  361 MET A CE  
895  N N   . ASP A 351 ? 0.2959 0.2710 0.2002 0.0531  -0.0045 0.0030  362 ASP A N   
896  C CA  . ASP A 351 ? 0.3394 0.3145 0.2263 0.0514  -0.0075 -0.0015 362 ASP A CA  
897  C C   . ASP A 351 ? 0.4017 0.3808 0.2874 0.0478  -0.0166 0.0009  362 ASP A C   
898  O O   . ASP A 351 ? 0.3247 0.3060 0.2222 0.0483  -0.0190 0.0072  362 ASP A O   
899  C CB  . ASP A 351 ? 0.3468 0.3281 0.2196 0.0525  -0.0019 0.0015  362 ASP A CB  
900  C CG  . ASP A 351 ? 0.4175 0.4047 0.2898 0.0536  -0.0019 0.0147  362 ASP A CG  
901  O OD1 . ASP A 351 ? 0.4392 0.4298 0.3144 0.0536  -0.0091 0.0200  362 ASP A OD1 
902  O OD2 . ASP A 351 ? 0.4513 0.4394 0.3193 0.0548  0.0064  0.0203  362 ASP A OD2 
903  N N   . GLU A 352 ? 0.3572 0.3388 0.2288 0.0433  -0.0212 -0.0051 363 GLU A N   
904  C CA  . GLU A 352 ? 0.3390 0.3291 0.2125 0.0383  -0.0300 -0.0045 363 GLU A CA  
905  C C   . GLU A 352 ? 0.3660 0.3716 0.2434 0.0424  -0.0334 0.0078  363 GLU A C   
906  O O   . GLU A 352 ? 0.3671 0.3803 0.2556 0.0419  -0.0383 0.0113  363 GLU A O   
907  C CB  . GLU A 352 ? 0.3363 0.3284 0.1936 0.0301  -0.0343 -0.0151 363 GLU A CB  
908  C CG  . GLU A 352 ? 0.4226 0.3940 0.2779 0.0256  -0.0313 -0.0270 363 GLU A CG  
909  C CD  . GLU A 352 ? 0.4875 0.4577 0.3285 0.0138  -0.0353 -0.0388 363 GLU A CD  
910  O OE1 . GLU A 352 ? 0.4072 0.3985 0.2430 0.0079  -0.0428 -0.0380 363 GLU A OE1 
911  O OE2 . GLU A 352 ? 0.4386 0.3865 0.2736 0.0104  -0.0307 -0.0491 363 GLU A OE2 
912  N N   . GLY A 353 ? 0.3660 0.3756 0.2345 0.0474  -0.0297 0.0153  364 GLY A N   
913  C CA  . GLY A 353 ? 0.4029 0.4226 0.2745 0.0538  -0.0315 0.0293  364 GLY A CA  
914  C C   . GLY A 353 ? 0.3444 0.3545 0.2343 0.0580  -0.0268 0.0354  364 GLY A C   
915  O O   . GLY A 353 ? 0.3491 0.3657 0.2476 0.0628  -0.0296 0.0433  364 GLY A O   
916  N N   . GLN A 354 ? 0.3409 0.3371 0.2374 0.0565  -0.0194 0.0313  365 GLN A N   
917  C CA  . GLN A 354 ? 0.3094 0.2971 0.2217 0.0578  -0.0152 0.0342  365 GLN A CA  
918  C C   . GLN A 354 ? 0.3428 0.3326 0.2658 0.0551  -0.0209 0.0290  365 GLN A C   
919  O O   . GLN A 354 ? 0.3295 0.3184 0.2629 0.0574  -0.0200 0.0329  365 GLN A O   
920  C CB  . GLN A 354 ? 0.2986 0.2772 0.2155 0.0553  -0.0073 0.0301  365 GLN A CB  
921  C CG  . GLN A 354 ? 0.3592 0.3358 0.2672 0.0565  0.0011  0.0360  365 GLN A CG  
922  C CD  . GLN A 354 ? 0.3431 0.3186 0.2558 0.0531  0.0083  0.0294  365 GLN A CD  
923  O OE1 . GLN A 354 ? 0.3285 0.3068 0.2430 0.0526  0.0058  0.0203  365 GLN A OE1 
924  N NE2 . GLN A 354 ? 0.3723 0.3439 0.2881 0.0510  0.0180  0.0344  365 GLN A NE2 
925  N N   . ILE A 355 ? 0.2951 0.2853 0.2147 0.0500  -0.0252 0.0199  366 ILE A N   
926  C CA  . ILE A 355 ? 0.3255 0.3166 0.2529 0.0459  -0.0297 0.0157  366 ILE A CA  
927  C C   . ILE A 355 ? 0.3778 0.3846 0.3083 0.0465  -0.0351 0.0199  366 ILE A C   
928  O O   . ILE A 355 ? 0.3035 0.3139 0.2455 0.0469  -0.0353 0.0216  366 ILE A O   
929  C CB  . ILE A 355 ? 0.3175 0.3014 0.2381 0.0402  -0.0317 0.0061  366 ILE A CB  
930  C CG1 . ILE A 355 ? 0.2873 0.2592 0.2093 0.0426  -0.0265 0.0032  366 ILE A CG1 
931  C CG2 . ILE A 355 ? 0.3463 0.3309 0.2722 0.0341  -0.0357 0.0031  366 ILE A CG2 
932  C CD1 . ILE A 355 ? 0.3682 0.3286 0.2826 0.0403  -0.0269 -0.0050 366 ILE A CD1 
933  N N   . ALA A 356 ? 0.2923 0.3116 0.2127 0.0467  -0.0397 0.0215  367 ALA A N   
934  C CA  . ALA A 356 ? 0.3439 0.3852 0.2687 0.0484  -0.0463 0.0264  367 ALA A CA  
935  C C   . ALA A 356 ? 0.3768 0.4203 0.3128 0.0594  -0.0427 0.0381  367 ALA A C   
936  O O   . ALA A 356 ? 0.3471 0.4041 0.2957 0.0619  -0.0451 0.0406  367 ALA A O   
937  C CB  . ALA A 356 ? 0.3276 0.3843 0.2370 0.0473  -0.0522 0.0269  367 ALA A CB  
938  N N   . ALA A 357 ? 0.3116 0.3408 0.2435 0.0658  -0.0356 0.0449  368 ALA A N   
939  C CA  . ALA A 357 ? 0.3161 0.3401 0.2568 0.0761  -0.0299 0.0555  368 ALA A CA  
940  C C   . ALA A 357 ? 0.3400 0.3554 0.2954 0.0743  -0.0255 0.0506  368 ALA A C   
941  O O   . ALA A 357 ? 0.3243 0.3457 0.2905 0.0813  -0.0243 0.0552  368 ALA A O   
942  C CB  . ALA A 357 ? 0.3111 0.3170 0.2431 0.0798  -0.0212 0.0625  368 ALA A CB  
943  N N   . VAL A 358 ? 0.3052 0.3079 0.2606 0.0658  -0.0229 0.0412  369 VAL A N   
944  C CA  . VAL A 358 ? 0.3181 0.3142 0.2839 0.0628  -0.0193 0.0359  369 VAL A CA  
945  C C   . VAL A 358 ? 0.3408 0.3530 0.3140 0.0607  -0.0246 0.0331  369 VAL A C   
946  O O   . VAL A 358 ? 0.3354 0.3497 0.3189 0.0638  -0.0210 0.0337  369 VAL A O   
947  C CB  . VAL A 358 ? 0.2933 0.2779 0.2563 0.0549  -0.0177 0.0277  369 VAL A CB  
948  C CG1 . VAL A 358 ? 0.2776 0.2591 0.2481 0.0507  -0.0160 0.0221  369 VAL A CG1 
949  C CG2 . VAL A 358 ? 0.3053 0.2778 0.2655 0.0557  -0.0108 0.0297  369 VAL A CG2 
950  N N   . CYS A 359 ? 0.2684 0.2918 0.2364 0.0543  -0.0321 0.0291  370 CYS A N   
951  C CA  . CYS A 359 ? 0.2791 0.3194 0.2545 0.0492  -0.0365 0.0257  370 CYS A CA  
952  C C   . CYS A 359 ? 0.2962 0.3583 0.2831 0.0584  -0.0377 0.0333  370 CYS A C   
953  O O   . CYS A 359 ? 0.2637 0.3369 0.2632 0.0583  -0.0359 0.0321  370 CYS A O   
954  C CB  . CYS A 359 ? 0.2803 0.3267 0.2463 0.0392  -0.0433 0.0194  370 CYS A CB  
955  S SG  . CYS A 359 ? 0.3352 0.3561 0.2908 0.0304  -0.0410 0.0107  370 CYS A SG  
956  N N   . ARG A 360 ? 0.2367 0.3065 0.2193 0.0672  -0.0403 0.0417  371 ARG A N   
957  C CA  . ARG A 360 ? 0.2632 0.3559 0.2573 0.0791  -0.0422 0.0511  371 ARG A CA  
958  C C   . ARG A 360 ? 0.2947 0.3748 0.3005 0.0897  -0.0321 0.0554  371 ARG A C   
959  O O   . ARG A 360 ? 0.2842 0.3827 0.3054 0.0962  -0.0312 0.0576  371 ARG A O   
960  C CB  . ARG A 360 ? 0.2964 0.3973 0.2802 0.0881  -0.0468 0.0617  371 ARG A CB  
961  C CG  . ARG A 360 ? 0.3055 0.4339 0.3020 0.1032  -0.0501 0.0735  371 ARG A CG  
962  C CD  . ARG A 360 ? 0.3845 0.5113 0.3693 0.1148  -0.0510 0.0871  371 ARG A CD  
963  N NE  . ARG A 360 ? 0.4382 0.5277 0.4167 0.1208  -0.0390 0.0923  371 ARG A NE  
964  C CZ  . ARG A 360 ? 0.6006 0.6711 0.5613 0.1185  -0.0361 0.0952  371 ARG A CZ  
965  N NH1 . ARG A 360 ? 0.5803 0.6644 0.5262 0.1130  -0.0439 0.0948  371 ARG A NH1 
966  N NH2 . ARG A 360 ? 0.5315 0.5693 0.4892 0.1206  -0.0242 0.0975  371 ARG A NH2 
967  N N   . GLU A 361 ? 0.3013 0.3514 0.3005 0.0911  -0.0235 0.0558  372 GLU A N   
968  C CA  . GLU A 361 ? 0.3119 0.3459 0.3197 0.0990  -0.0125 0.0574  372 GLU A CA  
969  C C   . GLU A 361 ? 0.3228 0.3606 0.3400 0.0916  -0.0098 0.0471  372 GLU A C   
970  O O   . GLU A 361 ? 0.2615 0.3032 0.2908 0.0997  -0.0033 0.0480  372 GLU A O   
971  C CB  . GLU A 361 ? 0.3182 0.3203 0.3164 0.0973  -0.0039 0.0573  372 GLU A CB  
972  C CG  . GLU A 361 ? 0.3347 0.3295 0.3222 0.1049  -0.0035 0.0692  372 GLU A CG  
973  C CD  . GLU A 361 ? 0.4288 0.4297 0.4219 0.1231  -0.0015 0.0835  372 GLU A CD  
974  O OE1 . GLU A 361 ? 0.3608 0.3447 0.3613 0.1317  0.0091  0.0859  372 GLU A OE1 
975  O OE2 . GLU A 361 ? 0.4578 0.4812 0.4473 0.1294  -0.0106 0.0923  372 GLU A OE2 
976  N N   . CYS A 362 ? 0.2276 0.2637 0.2385 0.0772  -0.0137 0.0379  373 CYS A N   
977  C CA  . CYS A 362 ? 0.3202 0.3596 0.3367 0.0694  -0.0112 0.0296  373 CYS A CA  
978  C C   . CYS A 362 ? 0.3207 0.3901 0.3499 0.0700  -0.0147 0.0303  373 CYS A C   
979  O O   . CYS A 362 ? 0.2410 0.3172 0.2803 0.0709  -0.0085 0.0273  373 CYS A O   
980  C CB  . CYS A 362 ? 0.2946 0.3238 0.2998 0.0557  -0.0148 0.0222  373 CYS A CB  
981  S SG  . CYS A 362 ? 0.3647 0.3663 0.3598 0.0536  -0.0099 0.0194  373 CYS A SG  
982  N N   . LEU A 363 ? 0.2459 0.3360 0.2749 0.0683  -0.0243 0.0332  374 LEU A N   
983  C CA  . LEU A 363 ? 0.2708 0.3956 0.3142 0.0674  -0.0284 0.0334  374 LEU A CA  
984  C C   . LEU A 363 ? 0.2866 0.4280 0.3469 0.0855  -0.0240 0.0417  374 LEU A C   
985  O O   . LEU A 363 ? 0.2832 0.4512 0.3603 0.0866  -0.0224 0.0405  374 LEU A O   
986  C CB  . LEU A 363 ? 0.3177 0.4619 0.3555 0.0604  -0.0401 0.0335  374 LEU A CB  
987  C CG  . LEU A 363 ? 0.2673 0.4010 0.2928 0.0413  -0.0434 0.0235  374 LEU A CG  
988  C CD1 . LEU A 363 ? 0.2816 0.4255 0.2963 0.0350  -0.0532 0.0220  374 LEU A CD1 
989  C CD2 . LEU A 363 ? 0.3127 0.4612 0.3485 0.0296  -0.0411 0.0173  374 LEU A CD2 
990  N N   . GLN A 364 ? 0.2505 0.3770 0.3070 0.1003  -0.0212 0.0508  375 GLN A N   
991  C CA  . GLN A 364 ? 0.2483 0.3832 0.3199 0.1202  -0.0147 0.0597  375 GLN A CA  
992  C C   . GLN A 364 ? 0.3554 0.4766 0.4353 0.1215  -0.0014 0.0527  375 GLN A C   
993  O O   . GLN A 364 ? 0.2827 0.4253 0.3808 0.1320  0.0033  0.0544  375 GLN A O   
994  C CB  . GLN A 364 ? 0.2871 0.4005 0.3492 0.1346  -0.0124 0.0717  375 GLN A CB  
995  C CG  . GLN A 364 ? 0.2969 0.4314 0.3516 0.1367  -0.0252 0.0805  375 GLN A CG  
996  C CD  . GLN A 364 ? 0.3866 0.4941 0.4251 0.1440  -0.0223 0.0905  375 GLN A CD  
997  O OE1 . GLN A 364 ? 0.4158 0.4882 0.4497 0.1481  -0.0105 0.0918  375 GLN A OE1 
998  N NE2 . GLN A 364 ? 0.3307 0.4534 0.3592 0.1418  -0.0320 0.0956  375 GLN A NE2 
999  N N   . ALA A 365 ? 0.2839 0.3724 0.3505 0.1110  0.0048  0.0443  376 ALA A N   
1000 C CA  . ALA A 365 ? 0.2944 0.3709 0.3650 0.1094  0.0169  0.0356  376 ALA A CA  
1001 C C   . ALA A 365 ? 0.2926 0.3969 0.3730 0.0998  0.0157  0.0289  376 ALA A C   
1002 O O   . ALA A 365 ? 0.2778 0.3922 0.3710 0.1060  0.0251  0.0261  376 ALA A O   
1003 C CB  . ALA A 365 ? 0.2947 0.3371 0.3481 0.0976  0.0211  0.0274  376 ALA A CB  
1004 N N   . LEU A 366 ? 0.3082 0.4239 0.3823 0.0844  0.0055  0.0261  377 LEU A N   
1005 C CA  . LEU A 366 ? 0.2715 0.4098 0.3525 0.0720  0.0053  0.0200  377 LEU A CA  
1006 C C   . LEU A 366 ? 0.2637 0.4443 0.3678 0.0800  0.0037  0.0242  377 LEU A C   
1007 O O   . LEU A 366 ? 0.2542 0.4544 0.3711 0.0771  0.0105  0.0199  377 LEU A O   
1008 C CB  . LEU A 366 ? 0.2387 0.3729 0.3057 0.0537  -0.0040 0.0164  377 LEU A CB  
1009 C CG  . LEU A 366 ? 0.2412 0.3403 0.2878 0.0452  -0.0027 0.0120  377 LEU A CG  
1010 C CD1 . LEU A 366 ? 0.2400 0.3363 0.2753 0.0302  -0.0106 0.0095  377 LEU A CD1 
1011 C CD2 . LEU A 366 ? 0.2454 0.3337 0.2892 0.0418  0.0077  0.0061  377 LEU A CD2 
1012 N N   . GLU A 367 ? 0.2335 0.4324 0.3432 0.0893  -0.0056 0.0328  378 GLU A N   
1013 C CA  . GLU A 367 ? 0.2167 0.4615 0.3504 0.0990  -0.0083 0.0379  378 GLU A CA  
1014 C C   . GLU A 367 ? 0.2575 0.5052 0.4081 0.1179  0.0051  0.0401  378 GLU A C   
1015 O O   . GLU A 367 ? 0.2474 0.5293 0.4189 0.1193  0.0095  0.0378  378 GLU A O   
1016 C CB  . GLU A 367 ? 0.2084 0.4706 0.3426 0.1093  -0.0205 0.0485  378 GLU A CB  
1017 C CG  . GLU A 367 ? 0.2742 0.5905 0.4345 0.1211  -0.0256 0.0552  378 GLU A CG  
1018 C CD  . GLU A 367 ? 0.5676 0.8885 0.7215 0.1334  -0.0353 0.0671  378 GLU A CD  
1019 O OE1 . GLU A 367 ? 0.6292 0.9123 0.7669 0.1434  -0.0320 0.0737  378 GLU A OE1 
1020 O OE2 . GLU A 367 ? 0.5538 0.9105 0.7150 0.1295  -0.0450 0.0684  378 GLU A OE2 
1021 N N   . PHE A 368 ? 0.2523 0.4632 0.3940 0.1317  0.0132  0.0438  379 PHE A N   
1022 C CA  . PHE A 368 ? 0.2997 0.5042 0.4542 0.1501  0.0283  0.0445  379 PHE A CA  
1023 C C   . PHE A 368 ? 0.2642 0.4661 0.4201 0.1385  0.0400  0.0313  379 PHE A C   
1024 O O   . PHE A 368 ? 0.3048 0.5324 0.4809 0.1472  0.0488  0.0295  379 PHE A O   
1025 C CB  . PHE A 368 ? 0.2732 0.4309 0.4131 0.1618  0.0356  0.0489  379 PHE A CB  
1026 C CG  . PHE A 368 ? 0.3433 0.4802 0.4895 0.1759  0.0541  0.0452  379 PHE A CG  
1027 C CD1 . PHE A 368 ? 0.3450 0.4928 0.5059 0.1921  0.0577  0.0511  379 PHE A CD1 
1028 C CD2 . PHE A 368 ? 0.4120 0.5129 0.5428 0.1642  0.0650  0.0324  379 PHE A CD2 
1029 C CE1 . PHE A 368 ? 0.4097 0.5333 0.5728 0.2008  0.0739  0.0450  379 PHE A CE1 
1030 C CE2 . PHE A 368 ? 0.3809 0.4611 0.5157 0.1758  0.0833  0.0266  379 PHE A CE2 
1031 C CZ  . PHE A 368 ? 0.4322 0.5220 0.5820 0.1924  0.0870  0.0323  379 PHE A CZ  
1032 N N   . LEU A 369 ? 0.2197 0.3929 0.3540 0.1192  0.0402  0.0223  380 LEU A N   
1033 C CA  . LEU A 369 ? 0.2750 0.4434 0.4056 0.1077  0.0510  0.0107  380 LEU A CA  
1034 C C   . LEU A 369 ? 0.2790 0.4895 0.4248 0.0976  0.0495  0.0083  380 LEU A C   
1035 O O   . LEU A 369 ? 0.2358 0.4615 0.3934 0.1000  0.0617  0.0029  380 LEU A O   
1036 C CB  . LEU A 369 ? 0.2929 0.4273 0.3967 0.0896  0.0484  0.0042  380 LEU A CB  
1037 C CG  . LEU A 369 ? 0.3058 0.3993 0.3943 0.0947  0.0527  0.0030  380 LEU A CG  
1038 C CD1 . LEU A 369 ? 0.2594 0.3311 0.3254 0.0766  0.0466  -0.0021 380 LEU A CD1 
1039 C CD2 . LEU A 369 ? 0.3058 0.3852 0.3971 0.1037  0.0700  -0.0043 380 LEU A CD2 
1040 N N   . HIS A 370 ? 0.2347 0.4641 0.3800 0.0849  0.0356  0.0112  381 HIS A N   
1041 C CA  . HIS A 370 ? 0.2810 0.5482 0.4393 0.0707  0.0346  0.0077  381 HIS A CA  
1042 C C   . HIS A 370 ? 0.2986 0.6127 0.4890 0.0863  0.0382  0.0115  381 HIS A C   
1043 O O   . HIS A 370 ? 0.2218 0.5637 0.4271 0.0808  0.0471  0.0064  381 HIS A O   
1044 C CB  . HIS A 370 ? 0.2148 0.4877 0.3641 0.0530  0.0197  0.0086  381 HIS A CB  
1045 C CG  . HIS A 370 ? 0.2453 0.4762 0.3657 0.0382  0.0172  0.0049  381 HIS A CG  
1046 N ND1 . HIS A 370 ? 0.1908 0.4152 0.2986 0.0242  0.0058  0.0049  381 HIS A ND1 
1047 C CD2 . HIS A 370 ? 0.2496 0.4448 0.3518 0.0361  0.0246  0.0011  381 HIS A CD2 
1048 C CE1 . HIS A 370 ? 0.2796 0.4660 0.3642 0.0161  0.0066  0.0024  381 HIS A CE1 
1049 N NE2 . HIS A 370 ? 0.2249 0.3952 0.3058 0.0228  0.0170  0.0003  381 HIS A NE2 
1050 N N   . SER A 371 ? 0.2507 0.5754 0.4521 0.1070  0.0321  0.0214  382 SER A N   
1051 C CA  . SER A 371 ? 0.2187 0.5880 0.4518 0.1271  0.0358  0.0270  382 SER A CA  
1052 C C   . SER A 371 ? 0.2576 0.6181 0.4999 0.1407  0.0558  0.0221  382 SER A C   
1053 O O   . SER A 371 ? 0.3173 0.7067 0.5817 0.1488  0.0606  0.0222  382 SER A O   
1054 C CB  . SER A 371 ? 0.3434 0.7111 0.5779 0.1468  0.0256  0.0400  382 SER A CB  
1055 O OG  . SER A 371 ? 0.4339 0.7536 0.6547 0.1630  0.0343  0.0433  382 SER A OG  
1056 N N   . ASN A 372 ? 0.2724 0.5818 0.4914 0.1380  0.0658  0.0156  383 ASN A N   
1057 C CA  . ASN A 372 ? 0.3282 0.6240 0.5500 0.1467  0.0858  0.0076  383 ASN A CA  
1058 C C   . ASN A 372 ? 0.3183 0.6102 0.5271 0.1228  0.0935  -0.0049 383 ASN A C   
1059 O O   . ASN A 372 ? 0.2929 0.5637 0.4937 0.1250  0.1096  -0.0139 383 ASN A O   
1060 C CB  . ASN A 372 ? 0.3890 0.6313 0.5931 0.1598  0.0935  0.0075  383 ASN A CB  
1061 C CG  . ASN A 372 ? 0.3458 0.5830 0.5610 0.1835  0.0913  0.0183  383 ASN A CG  
1062 O OD1 . ASN A 372 ? 0.4641 0.7255 0.6996 0.1943  0.0939  0.0200  383 ASN A OD1 
1063 N ND2 . ASN A 372 ? 0.5289 0.7309 0.7274 0.1881  0.0853  0.0253  383 ASN A ND2 
1064 N N   . GLN A 373 ? 0.2854 0.5949 0.4896 0.0997  0.0830  -0.0056 384 GLN A N   
1065 C CA  . GLN A 373 ? 0.2451 0.5530 0.4365 0.0766  0.0898  -0.0145 384 GLN A CA  
1066 C C   . GLN A 373 ? 0.2846 0.5415 0.4425 0.0679  0.0939  -0.0207 384 GLN A C   
1067 O O   . GLN A 373 ? 0.3434 0.5941 0.4897 0.0575  0.1055  -0.0287 384 GLN A O   
1068 C CB  . GLN A 373 ? 0.3010 0.6430 0.5136 0.0805  0.1067  -0.0203 384 GLN A CB  
1069 C CG  . GLN A 373 ? 0.3167 0.7188 0.5629 0.0808  0.1028  -0.0162 384 GLN A CG  
1070 C CD  . GLN A 373 ? 0.3969 0.8226 0.6704 0.1098  0.0997  -0.0078 384 GLN A CD  
1071 O OE1 . GLN A 373 ? 0.5175 0.9425 0.7908 0.1157  0.0839  0.0010  384 GLN A OE1 
1072 N NE2 . GLN A 373 ? 0.6860 1.1179 0.9758 0.1243  0.1126  -0.0105 384 GLN A NE2 
1073 N N   . VAL A 374 ? 0.2637 0.4865 0.4053 0.0716  0.0847  -0.0172 385 VAL A N   
1074 C CA  . VAL A 374 ? 0.2643 0.4446 0.3757 0.0616  0.0854  -0.0226 385 VAL A CA  
1075 C C   . VAL A 374 ? 0.2822 0.4526 0.3776 0.0453  0.0697  -0.0183 385 VAL A C   
1076 O O   . VAL A 374 ? 0.3487 0.5225 0.4494 0.0495  0.0577  -0.0113 385 VAL A O   
1077 C CB  . VAL A 374 ? 0.3325 0.4800 0.4378 0.0772  0.0894  -0.0234 385 VAL A CB  
1078 C CG1 . VAL A 374 ? 0.3793 0.4895 0.4550 0.0643  0.0873  -0.0292 385 VAL A CG1 
1079 C CG2 . VAL A 374 ? 0.3686 0.5192 0.4877 0.0942  0.1074  -0.0289 385 VAL A CG2 
1080 N N   . ILE A 375 ? 0.3177 0.4745 0.3920 0.0278  0.0704  -0.0221 386 ILE A N   
1081 C CA  . ILE A 375 ? 0.2708 0.4101 0.3265 0.0144  0.0577  -0.0184 386 ILE A CA  
1082 C C   . ILE A 375 ? 0.3058 0.4103 0.3383 0.0141  0.0571  -0.0214 386 ILE A C   
1083 O O   . ILE A 375 ? 0.3092 0.4052 0.3296 0.0106  0.0665  -0.0278 386 ILE A O   
1084 C CB  . ILE A 375 ? 0.2621 0.4110 0.3105 -0.0048 0.0582  -0.0180 386 ILE A CB  
1085 C CG1 . ILE A 375 ? 0.2803 0.4691 0.3542 -0.0070 0.0607  -0.0171 386 ILE A CG1 
1086 C CG2 . ILE A 375 ? 0.2811 0.4097 0.3124 -0.0154 0.0455  -0.0133 386 ILE A CG2 
1087 C CD1 . ILE A 375 ? 0.3417 0.5404 0.4099 -0.0276 0.0649  -0.0176 386 ILE A CD1 
1088 N N   . HIS A 376 ? 0.2846 0.3717 0.3108 0.0168  0.0463  -0.0175 387 HIS A N   
1089 C CA  . HIS A 376 ? 0.2512 0.3108 0.2592 0.0164  0.0455  -0.0209 387 HIS A CA  
1090 C C   . HIS A 376 ? 0.3343 0.3840 0.3202 0.0023  0.0425  -0.0213 387 HIS A C   
1091 O O   . HIS A 376 ? 0.3119 0.3509 0.2830 -0.0010 0.0471  -0.0270 387 HIS A O   
1092 C CB  . HIS A 376 ? 0.2439 0.2910 0.2533 0.0234  0.0362  -0.0164 387 HIS A CB  
1093 C CG  . HIS A 376 ? 0.3039 0.3274 0.2995 0.0230  0.0363  -0.0205 387 HIS A CG  
1094 N ND1 . HIS A 376 ? 0.2670 0.2803 0.2450 0.0133  0.0300  -0.0211 387 HIS A ND1 
1095 C CD2 . HIS A 376 ? 0.3093 0.3186 0.3067 0.0307  0.0420  -0.0242 387 HIS A CD2 
1096 C CE1 . HIS A 376 ? 0.3014 0.3001 0.2727 0.0140  0.0309  -0.0258 387 HIS A CE1 
1097 N NE2 . HIS A 376 ? 0.3245 0.3185 0.3067 0.0232  0.0388  -0.0283 387 HIS A NE2 
1098 N N   . ARG A 377 ? 0.2736 0.3252 0.2557 -0.0058 0.0344  -0.0151 388 ARG A N   
1099 C CA  . ARG A 377 ? 0.2584 0.2994 0.2198 -0.0177 0.0316  -0.0122 388 ARG A CA  
1100 C C   . ARG A 377 ? 0.2994 0.3203 0.2441 -0.0166 0.0238  -0.0109 388 ARG A C   
1101 O O   . ARG A 377 ? 0.3158 0.3270 0.2430 -0.0235 0.0203  -0.0064 388 ARG A O   
1102 C CB  . ARG A 377 ? 0.2671 0.3148 0.2191 -0.0255 0.0425  -0.0153 388 ARG A CB  
1103 C CG  . ARG A 377 ? 0.2962 0.3680 0.2656 -0.0287 0.0508  -0.0161 388 ARG A CG  
1104 C CD  . ARG A 377 ? 0.3133 0.3920 0.2714 -0.0394 0.0621  -0.0178 388 ARG A CD  
1105 N NE  . ARG A 377 ? 0.3544 0.4294 0.3015 -0.0362 0.0710  -0.0254 388 ARG A NE  
1106 C CZ  . ARG A 377 ? 0.5102 0.5927 0.4462 -0.0441 0.0826  -0.0285 388 ARG A CZ  
1107 N NH1 . ARG A 377 ? 0.4030 0.4962 0.3378 -0.0560 0.0872  -0.0234 388 ARG A NH1 
1108 N NH2 . ARG A 377 ? 0.4195 0.4981 0.3445 -0.0412 0.0909  -0.0376 388 ARG A NH2 
1109 N N   . ASN A 378 ? 0.2988 0.3137 0.2484 -0.0082 0.0217  -0.0141 389 ASN A N   
1110 C CA  . ASN A 378 ? 0.3068 0.3084 0.2438 -0.0081 0.0142  -0.0134 389 ASN A CA  
1111 C C   . ASN A 378 ? 0.2825 0.2793 0.2301 -0.0003 0.0086  -0.0122 389 ASN A C   
1112 O O   . ASN A 378 ? 0.3262 0.3165 0.2716 0.0019  0.0071  -0.0154 389 ASN A O   
1113 C CB  . ASN A 378 ? 0.3033 0.3030 0.2290 -0.0107 0.0191  -0.0211 389 ASN A CB  
1114 C CG  . ASN A 378 ? 0.3763 0.3702 0.2872 -0.0132 0.0104  -0.0196 389 ASN A CG  
1115 O OD1 . ASN A 378 ? 0.3600 0.3501 0.2650 -0.0131 0.0021  -0.0112 389 ASN A OD1 
1116 N ND2 . ASN A 378 ? 0.3356 0.3294 0.2408 -0.0153 0.0126  -0.0281 389 ASN A ND2 
1117 N N   . ILE A 379 ? 0.2945 0.2955 0.2522 0.0022  0.0052  -0.0076 390 ILE A N   
1118 C CA  . ILE A 379 ? 0.2551 0.2521 0.2194 0.0088  -0.0004 -0.0052 390 ILE A CA  
1119 C C   . ILE A 379 ? 0.3139 0.3000 0.2673 0.0074  -0.0080 -0.0027 390 ILE A C   
1120 O O   . ILE A 379 ? 0.3346 0.3162 0.2787 0.0027  -0.0113 0.0008  390 ILE A O   
1121 C CB  . ILE A 379 ? 0.2482 0.2560 0.2234 0.0104  -0.0028 -0.0018 390 ILE A CB  
1122 C CG1 . ILE A 379 ? 0.3117 0.3361 0.3014 0.0144  0.0043  -0.0032 390 ILE A CG1 
1123 C CG2 . ILE A 379 ? 0.3045 0.3082 0.2826 0.0167  -0.0085 0.0009  390 ILE A CG2 
1124 C CD1 . ILE A 379 ? 0.3600 0.3812 0.3574 0.0251  0.0093  -0.0043 390 ILE A CD1 
1125 N N   . LYS A 380 ? 0.2850 0.2664 0.2395 0.0116  -0.0096 -0.0042 391 LYS A N   
1126 C CA  . LYS A 380 ? 0.2672 0.2429 0.2161 0.0129  -0.0162 -0.0019 391 LYS A CA  
1127 C C   . LYS A 380 ? 0.3038 0.2788 0.2598 0.0170  -0.0151 -0.0042 391 LYS A C   
1128 O O   . LYS A 380 ? 0.2677 0.2423 0.2297 0.0180  -0.0089 -0.0074 391 LYS A O   
1129 C CB  . LYS A 380 ? 0.2653 0.2404 0.2020 0.0093  -0.0189 -0.0016 391 LYS A CB  
1130 C CG  . LYS A 380 ? 0.2896 0.2700 0.2235 0.0051  -0.0144 -0.0082 391 LYS A CG  
1131 C CD  . LYS A 380 ? 0.2910 0.2745 0.2094 0.0007  -0.0178 -0.0067 391 LYS A CD  
1132 C CE  . LYS A 380 ? 0.3382 0.3280 0.2515 -0.0052 -0.0132 -0.0157 391 LYS A CE  
1133 N NZ  . LYS A 380 ? 0.3528 0.3498 0.2494 -0.0094 -0.0181 -0.0142 391 LYS A NZ  
1134 N N   . SER A 381 ? 0.2748 0.2481 0.2300 0.0196  -0.0198 -0.0023 392 SER A N   
1135 C CA  . SER A 381 ? 0.2280 0.2011 0.1900 0.0220  -0.0174 -0.0039 392 SER A CA  
1136 C C   . SER A 381 ? 0.2894 0.2638 0.2524 0.0171  -0.0130 -0.0102 392 SER A C   
1137 O O   . SER A 381 ? 0.2909 0.2607 0.2595 0.0169  -0.0072 -0.0123 392 SER A O   
1138 C CB  . SER A 381 ? 0.2499 0.2241 0.2117 0.0253  -0.0220 -0.0017 392 SER A CB  
1139 O OG  . SER A 381 ? 0.2791 0.2593 0.2377 0.0241  -0.0261 -0.0026 392 SER A OG  
1140 N N   . ASP A 382 ? 0.2690 0.2486 0.2251 0.0121  -0.0152 -0.0133 393 ASP A N   
1141 C CA  . ASP A 382 ? 0.3175 0.3002 0.2721 0.0049  -0.0115 -0.0216 393 ASP A CA  
1142 C C   . ASP A 382 ? 0.3109 0.2836 0.2678 0.0034  -0.0012 -0.0268 393 ASP A C   
1143 O O   . ASP A 382 ? 0.2883 0.2569 0.2454 -0.0026 0.0048  -0.0351 393 ASP A O   
1144 C CB  . ASP A 382 ? 0.3048 0.2970 0.2481 0.0004  -0.0168 -0.0228 393 ASP A CB  
1145 C CG  . ASP A 382 ? 0.3183 0.3175 0.2585 0.0055  -0.0265 -0.0149 393 ASP A CG  
1146 O OD1 . ASP A 382 ? 0.3019 0.2933 0.2414 0.0113  -0.0283 -0.0078 393 ASP A OD1 
1147 O OD2 . ASP A 382 ? 0.3146 0.3275 0.2530 0.0037  -0.0322 -0.0162 393 ASP A OD2 
1148 N N   . ASN A 383 ? 0.2601 0.2294 0.2191 0.0088  0.0015  -0.0228 394 ASN A N   
1149 C CA  . ASN A 383 ? 0.2588 0.2209 0.2218 0.0109  0.0117  -0.0264 394 ASN A CA  
1150 C C   . ASN A 383 ? 0.2780 0.2338 0.2511 0.0201  0.0149  -0.0202 394 ASN A C   
1151 O O   . ASN A 383 ? 0.2868 0.2398 0.2657 0.0262  0.0220  -0.0196 394 ASN A O   
1152 C CB  . ASN A 383 ? 0.2900 0.2588 0.2494 0.0104  0.0132  -0.0264 394 ASN A CB  
1153 C CG  . ASN A 383 ? 0.3575 0.3304 0.3037 0.0014  0.0130  -0.0330 394 ASN A CG  
1154 O OD1 . ASN A 383 ? 0.3135 0.2842 0.2551 -0.0045 0.0139  -0.0404 394 ASN A OD1 
1155 N ND2 . ASN A 383 ? 0.3301 0.3100 0.2692 -0.0009 0.0119  -0.0306 394 ASN A ND2 
1156 N N   . ILE A 384 ? 0.2970 0.2525 0.2721 0.0223  0.0098  -0.0149 395 ILE A N   
1157 C CA  . ILE A 384 ? 0.2909 0.2401 0.2721 0.0302  0.0128  -0.0084 395 ILE A CA  
1158 C C   . ILE A 384 ? 0.2952 0.2327 0.2760 0.0261  0.0182  -0.0112 395 ILE A C   
1159 O O   . ILE A 384 ? 0.3053 0.2485 0.2843 0.0203  0.0135  -0.0131 395 ILE A O   
1160 C CB  . ILE A 384 ? 0.3224 0.2806 0.3036 0.0343  0.0042  -0.0008 395 ILE A CB  
1161 C CG1 . ILE A 384 ? 0.2862 0.2557 0.2676 0.0346  -0.0006 0.0006  395 ILE A CG1 
1162 C CG2 . ILE A 384 ? 0.3566 0.3098 0.3407 0.0422  0.0067  0.0066  395 ILE A CG2 
1163 C CD1 . ILE A 384 ? 0.3040 0.2779 0.2931 0.0403  0.0049  0.0018  395 ILE A CD1 
1164 N N   . LEU A 385 ? 0.2724 0.1937 0.2556 0.0290  0.0288  -0.0117 396 LEU A N   
1165 C CA  . LEU A 385 ? 0.3195 0.2257 0.3019 0.0230  0.0364  -0.0145 396 LEU A CA  
1166 C C   . LEU A 385 ? 0.3633 0.2593 0.3472 0.0323  0.0400  -0.0029 396 LEU A C   
1167 O O   . LEU A 385 ? 0.3547 0.2517 0.3410 0.0445  0.0396  0.0057  396 LEU A O   
1168 C CB  . LEU A 385 ? 0.3260 0.2147 0.3065 0.0171  0.0483  -0.0250 396 LEU A CB  
1169 C CG  . LEU A 385 ? 0.3786 0.2788 0.3543 0.0082  0.0450  -0.0364 396 LEU A CG  
1170 C CD1 . LEU A 385 ? 0.3636 0.2456 0.3348 0.0000  0.0576  -0.0494 396 LEU A CD1 
1171 C CD2 . LEU A 385 ? 0.4039 0.3237 0.3773 -0.0012 0.0339  -0.0390 396 LEU A CD2 
1172 N N   . LEU A 386 ? 0.3305 0.2198 0.3130 0.0261  0.0433  -0.0022 397 LEU A N   
1173 C CA  . LEU A 386 ? 0.3457 0.2265 0.3262 0.0332  0.0465  0.0097  397 LEU A CA  
1174 C C   . LEU A 386 ? 0.4048 0.2575 0.3833 0.0293  0.0615  0.0100  397 LEU A C   
1175 O O   . LEU A 386 ? 0.3906 0.2361 0.3696 0.0151  0.0675  -0.0012 397 LEU A O   
1176 C CB  . LEU A 386 ? 0.3264 0.2235 0.3057 0.0294  0.0392  0.0117  397 LEU A CB  
1177 C CG  . LEU A 386 ? 0.3612 0.2805 0.3411 0.0315  0.0261  0.0098  397 LEU A CG  
1178 C CD1 . LEU A 386 ? 0.3030 0.2357 0.2828 0.0272  0.0212  0.0084  397 LEU A CD1 
1179 C CD2 . LEU A 386 ? 0.3419 0.2663 0.3201 0.0433  0.0209  0.0185  397 LEU A CD2 
1180 N N   . GLY A 387 ? 0.3782 0.2149 0.3536 0.0414  0.0675  0.0229  398 GLY A N   
1181 C CA  . GLY A 387 ? 0.4475 0.2527 0.4185 0.0384  0.0829  0.0263  398 GLY A CA  
1182 C C   . GLY A 387 ? 0.5121 0.3179 0.4784 0.0313  0.0847  0.0319  398 GLY A C   
1183 O O   . GLY A 387 ? 0.4444 0.2742 0.4102 0.0332  0.0741  0.0357  398 GLY A O   
1184 N N   . MET A 388 ? 0.5291 0.3074 0.4918 0.0216  0.0996  0.0313  399 MET A N   
1185 C CA  . MET A 388 ? 0.5349 0.3133 0.4932 0.0134  0.1039  0.0371  399 MET A CA  
1186 C C   . MET A 388 ? 0.5349 0.3120 0.4836 0.0293  0.1023  0.0567  399 MET A C   
1187 O O   . MET A 388 ? 0.5705 0.3549 0.5142 0.0243  0.1035  0.0620  399 MET A O   
1188 C CB  . MET A 388 ? 0.6095 0.3560 0.5653 -0.0024 0.1222  0.0325  399 MET A CB  
1189 C CG  . MET A 388 ? 0.6340 0.3904 0.5985 -0.0242 0.1230  0.0116  399 MET A CG  
1190 S SD  . MET A 388 ? 0.6365 0.4450 0.6115 -0.0317 0.1058  0.0033  399 MET A SD  
1191 C CE  . MET A 388 ? 0.7652 0.5767 0.7374 -0.0365 0.1130  0.0141  399 MET A CE  
1192 N N   . ASP A 389 ? 0.5351 0.3061 0.4812 0.0480  0.0996  0.0674  400 ASP A N   
1193 C CA  . ASP A 389 ? 0.5094 0.2873 0.4461 0.0642  0.0944  0.0859  400 ASP A CA  
1194 C C   . ASP A 389 ? 0.5056 0.3213 0.4458 0.0707  0.0760  0.0839  400 ASP A C   
1195 O O   . ASP A 389 ? 0.5134 0.3405 0.4466 0.0840  0.0690  0.0969  400 ASP A O   
1196 C CB  . ASP A 389 ? 0.5935 0.3474 0.5267 0.0814  0.1017  0.0995  400 ASP A CB  
1197 C CG  . ASP A 389 ? 0.5853 0.3455 0.5307 0.0896  0.0976  0.0915  400 ASP A CG  
1198 O OD1 . ASP A 389 ? 0.5023 0.2751 0.4560 0.0812  0.0924  0.0766  400 ASP A OD1 
1199 O OD2 . ASP A 389 ? 0.6590 0.4172 0.6064 0.1030  0.0986  0.0986  400 ASP A OD2 
1200 N N   . GLY A 390 ? 0.3986 0.2334 0.3483 0.0613  0.0680  0.0682  401 GLY A N   
1201 C CA  . GLY A 390 ? 0.4342 0.2989 0.3863 0.0661  0.0525  0.0658  401 GLY A CA  
1202 C C   . GLY A 390 ? 0.4812 0.3534 0.4406 0.0765  0.0468  0.0657  401 GLY A C   
1203 O O   . GLY A 390 ? 0.3621 0.2584 0.3230 0.0798  0.0346  0.0648  401 GLY A O   
1204 N N   . SER A 391 ? 0.3968 0.2489 0.3607 0.0812  0.0562  0.0660  402 SER A N   
1205 C CA  . SER A 391 ? 0.3839 0.2466 0.3568 0.0909  0.0521  0.0646  402 SER A CA  
1206 C C   . SER A 391 ? 0.3524 0.2326 0.3315 0.0798  0.0446  0.0493  402 SER A C   
1207 O O   . SER A 391 ? 0.4033 0.2804 0.3812 0.0658  0.0458  0.0388  402 SER A O   
1208 C CB  . SER A 391 ? 0.4964 0.3311 0.4725 0.0988  0.0662  0.0664  402 SER A CB  
1209 O OG  . SER A 391 ? 0.5934 0.4058 0.5683 0.0837  0.0766  0.0536  402 SER A OG  
1210 N N   . VAL A 392 ? 0.3370 0.2376 0.3227 0.0862  0.0368  0.0489  403 VAL A N   
1211 C CA  . VAL A 392 ? 0.3499 0.2680 0.3391 0.0767  0.0289  0.0375  403 VAL A CA  
1212 C C   . VAL A 392 ? 0.3450 0.2656 0.3428 0.0814  0.0328  0.0332  403 VAL A C   
1213 O O   . VAL A 392 ? 0.3623 0.2937 0.3670 0.0942  0.0320  0.0410  403 VAL A O   
1214 C CB  . VAL A 392 ? 0.3079 0.2504 0.2950 0.0766  0.0157  0.0403  403 VAL A CB  
1215 C CG1 . VAL A 392 ? 0.3495 0.3049 0.3387 0.0673  0.0092  0.0300  403 VAL A CG1 
1216 C CG2 . VAL A 392 ? 0.2906 0.2310 0.2680 0.0731  0.0133  0.0438  403 VAL A CG2 
1217 N N   . LYS A 393 ? 0.3364 0.2506 0.3341 0.0713  0.0370  0.0208  404 LYS A N   
1218 C CA  . LYS A 393 ? 0.2944 0.2086 0.2984 0.0750  0.0434  0.0152  404 LYS A CA  
1219 C C   . LYS A 393 ? 0.3287 0.2542 0.3302 0.0627  0.0393  0.0038  404 LYS A C   
1220 O O   . LYS A 393 ? 0.3378 0.2606 0.3321 0.0507  0.0362  -0.0026 404 LYS A O   
1221 C CB  . LYS A 393 ? 0.3521 0.2370 0.3553 0.0775  0.0590  0.0115  404 LYS A CB  
1222 C CG  . LYS A 393 ? 0.4007 0.2677 0.4042 0.0908  0.0657  0.0244  404 LYS A CG  
1223 C CD  . LYS A 393 ? 0.4749 0.3088 0.4776 0.0940  0.0832  0.0198  404 LYS A CD  
1224 C CE  . LYS A 393 ? 0.5585 0.3702 0.5599 0.1090  0.0910  0.0354  404 LYS A CE  
1225 N NZ  . LYS A 393 ? 0.6362 0.4384 0.6436 0.1197  0.1011  0.0348  404 LYS A NZ  
1226 N N   . LEU A 394 ? 0.3157 0.2556 0.3234 0.0664  0.0396  0.0023  405 LEU A N   
1227 C CA  . LEU A 394 ? 0.2790 0.2296 0.2829 0.0559  0.0370  -0.0065 405 LEU A CA  
1228 C C   . LEU A 394 ? 0.3043 0.2412 0.3041 0.0516  0.0487  -0.0180 405 LEU A C   
1229 O O   . LEU A 394 ? 0.3260 0.2513 0.3314 0.0608  0.0602  -0.0190 405 LEU A O   
1230 C CB  . LEU A 394 ? 0.3439 0.3188 0.3564 0.0600  0.0326  -0.0024 405 LEU A CB  
1231 C CG  . LEU A 394 ? 0.4064 0.3938 0.4154 0.0504  0.0312  -0.0086 405 LEU A CG  
1232 C CD1 . LEU A 394 ? 0.3529 0.3378 0.3491 0.0386  0.0219  -0.0100 405 LEU A CD1 
1233 C CD2 . LEU A 394 ? 0.3610 0.3734 0.3821 0.0547  0.0282  -0.0033 405 LEU A CD2 
1234 N N   . THR A 395 ? 0.3194 0.2579 0.3085 0.0383  0.0459  -0.0267 406 THR A N   
1235 C CA  . THR A 395 ? 0.3491 0.2765 0.3305 0.0311  0.0558  -0.0396 406 THR A CA  
1236 C C   . THR A 395 ? 0.3555 0.2987 0.3280 0.0221  0.0518  -0.0446 406 THR A C   
1237 O O   . THR A 395 ? 0.3530 0.3124 0.3267 0.0221  0.0429  -0.0375 406 THR A O   
1238 C CB  . THR A 395 ? 0.3191 0.2299 0.2930 0.0215  0.0576  -0.0465 406 THR A CB  
1239 O OG1 . THR A 395 ? 0.4274 0.3246 0.3940 0.0148  0.0695  -0.0606 406 THR A OG1 
1240 C CG2 . THR A 395 ? 0.3412 0.2656 0.3079 0.0108  0.0448  -0.0466 406 THR A CG2 
1241 N N   . ASP A 396 ? 0.3593 0.2960 0.3213 0.0140  0.0596  -0.0572 407 ASP A N   
1242 C CA  . ASP A 396 ? 0.3598 0.3089 0.3080 0.0038  0.0574  -0.0629 407 ASP A CA  
1243 C C   . ASP A 396 ? 0.3865 0.3511 0.3394 0.0084  0.0591  -0.0579 407 ASP A C   
1244 O O   . ASP A 396 ? 0.3748 0.3526 0.3254 0.0056  0.0496  -0.0499 407 ASP A O   
1245 C CB  . ASP A 396 ? 0.3324 0.2904 0.2707 -0.0050 0.0431  -0.0595 407 ASP A CB  
1246 C CG  . ASP A 396 ? 0.4877 0.4402 0.4158 -0.0159 0.0432  -0.0705 407 ASP A CG  
1247 O OD1 . ASP A 396 ? 0.4814 0.4174 0.4116 -0.0172 0.0542  -0.0800 407 ASP A OD1 
1248 O OD2 . ASP A 396 ? 0.4626 0.4277 0.3806 -0.0234 0.0327  -0.0698 407 ASP A OD2 
1249 N N   . PHE A 397 ? 0.3294 0.2912 0.2889 0.0150  0.0729  -0.0635 408 PHE A N   
1250 C CA  . PHE A 397 ? 0.3833 0.3631 0.3511 0.0195  0.0775  -0.0603 408 PHE A CA  
1251 C C   . PHE A 397 ? 0.3413 0.3288 0.2932 0.0091  0.0834  -0.0686 408 PHE A C   
1252 O O   . PHE A 397 ? 0.3969 0.3990 0.3559 0.0120  0.0914  -0.0685 408 PHE A O   
1253 C CB  . PHE A 397 ? 0.4087 0.3857 0.3952 0.0354  0.0896  -0.0603 408 PHE A CB  
1254 C CG  . PHE A 397 ? 0.3279 0.3076 0.3310 0.0472  0.0820  -0.0475 408 PHE A CG  
1255 C CD1 . PHE A 397 ? 0.3775 0.3386 0.3774 0.0478  0.0769  -0.0446 408 PHE A CD1 
1256 C CD2 . PHE A 397 ? 0.3782 0.3817 0.3992 0.0564  0.0801  -0.0387 408 PHE A CD2 
1257 C CE1 . PHE A 397 ? 0.3984 0.3625 0.4103 0.0583  0.0704  -0.0324 408 PHE A CE1 
1258 C CE2 . PHE A 397 ? 0.3803 0.3892 0.4139 0.0665  0.0722  -0.0273 408 PHE A CE2 
1259 C CZ  . PHE A 397 ? 0.3391 0.3272 0.3668 0.0679  0.0675  -0.0237 408 PHE A CZ  
1260 N N   . GLY A 398 ? 0.3485 0.3298 0.2792 -0.0032 0.0797  -0.0753 409 GLY A N   
1261 C CA  . GLY A 398 ? 0.3464 0.3346 0.2593 -0.0124 0.0869  -0.0836 409 GLY A CA  
1262 C C   . GLY A 398 ? 0.3865 0.3923 0.2937 -0.0176 0.0816  -0.0737 409 GLY A C   
1263 O O   . GLY A 398 ? 0.3864 0.3999 0.2804 -0.0241 0.0900  -0.0787 409 GLY A O   
1264 N N   . PHE A 399 ? 0.3458 0.3566 0.2625 -0.0152 0.0700  -0.0604 410 PHE A N   
1265 C CA  . PHE A 399 ? 0.3963 0.4194 0.3086 -0.0210 0.0667  -0.0509 410 PHE A CA  
1266 C C   . PHE A 399 ? 0.3508 0.3886 0.2858 -0.0152 0.0726  -0.0470 410 PHE A C   
1267 O O   . PHE A 399 ? 0.3791 0.4278 0.3134 -0.0218 0.0716  -0.0401 410 PHE A O   
1268 C CB  . PHE A 399 ? 0.3490 0.3668 0.2545 -0.0239 0.0508  -0.0397 410 PHE A CB  
1269 C CG  . PHE A 399 ? 0.4060 0.4198 0.2855 -0.0321 0.0446  -0.0386 410 PHE A CG  
1270 C CD1 . PHE A 399 ? 0.4197 0.4334 0.2835 -0.0370 0.0499  -0.0497 410 PHE A CD1 
1271 C CD2 . PHE A 399 ? 0.5028 0.5132 0.3726 -0.0345 0.0335  -0.0266 410 PHE A CD2 
1272 C CE1 . PHE A 399 ? 0.5279 0.5431 0.3672 -0.0442 0.0425  -0.0480 410 PHE A CE1 
1273 C CE2 . PHE A 399 ? 0.5420 0.5512 0.3882 -0.0394 0.0270  -0.0234 410 PHE A CE2 
1274 C CZ  . PHE A 399 ? 0.4742 0.4883 0.3053 -0.0443 0.0305  -0.0337 410 PHE A CZ  
1275 N N   . CYS A 400 ? 0.3733 0.4125 0.3284 -0.0032 0.0792  -0.0510 411 CYS A N   
1276 C CA  . CYS A 400 ? 0.3550 0.4134 0.3351 0.0046  0.0817  -0.0458 411 CYS A CA  
1277 C C   . CYS A 400 ? 0.4584 0.5375 0.4424 0.0005  0.0945  -0.0492 411 CYS A C   
1278 O O   . CYS A 400 ? 0.4072 0.4831 0.3757 -0.0049 0.1049  -0.0576 411 CYS A O   
1279 C CB  . CYS A 400 ? 0.3659 0.4199 0.3651 0.0212  0.0856  -0.0473 411 CYS A CB  
1280 S SG  . CYS A 400 ? 0.4357 0.4849 0.4397 0.0313  0.1067  -0.0604 411 CYS A SG  
1281 N N   . ALA A 401 ? 0.4411 0.5442 0.4458 0.0020  0.0937  -0.0430 412 ALA A N   
1282 C CA  . ALA A 401 ? 0.5049 0.6341 0.5193 -0.0020 0.1062  -0.0455 412 ALA A CA  
1283 C C   . ALA A 401 ? 0.3555 0.5108 0.4035 0.0134  0.1112  -0.0448 412 ALA A C   
1284 O O   . ALA A 401 ? 0.3683 0.5289 0.4313 0.0211  0.1003  -0.0378 412 ALA A O   
1285 C CB  . ALA A 401 ? 0.4530 0.5922 0.4604 -0.0193 0.1011  -0.0383 412 ALA A CB  
1286 N N   . GLN A 402 ? 0.3838 0.5572 0.4431 0.0188  0.1277  -0.0516 413 GLN A N   
1287 C CA  . GLN A 402 ? 0.4278 0.6332 0.5215 0.0346  0.1332  -0.0499 413 GLN A CA  
1288 C C   . GLN A 402 ? 0.4946 0.7388 0.6022 0.0223  0.1374  -0.0482 413 GLN A C   
1289 O O   . GLN A 402 ? 0.5132 0.7612 0.6087 0.0108  0.1498  -0.0540 413 GLN A O   
1290 C CB  . GLN A 402 ? 0.5414 0.7404 0.6421 0.0526  0.1506  -0.0591 413 GLN A CB  
1291 C CG  . GLN A 402 ? 0.6382 0.7946 0.7219 0.0602  0.1486  -0.0626 413 GLN A CG  
1292 C CD  . GLN A 402 ? 0.7369 0.8848 0.8350 0.0829  0.1636  -0.0683 413 GLN A CD  
1293 O OE1 . GLN A 402 ? 0.6412 0.8064 0.7666 0.1018  0.1629  -0.0605 413 GLN A OE1 
1294 N NE2 . GLN A 402 ? 0.7129 0.8333 0.7915 0.0815  0.1776  -0.0818 413 GLN A NE2 
1295 N N   . ILE A 403 ? 0.3733 0.6467 0.5044 0.0228  0.1273  -0.0406 414 ILE A N   
1296 C CA  . ILE A 403 ? 0.4200 0.7324 0.5662 0.0081  0.1304  -0.0394 414 ILE A CA  
1297 C C   . ILE A 403 ? 0.3986 0.7571 0.5830 0.0247  0.1405  -0.0410 414 ILE A C   
1298 O O   . ILE A 403 ? 0.3994 0.7596 0.6001 0.0489  0.1404  -0.0394 414 ILE A O   
1299 C CB  . ILE A 403 ? 0.5104 0.8282 0.6564 -0.0073 0.1131  -0.0321 414 ILE A CB  
1300 C CG1 . ILE A 403 ? 0.4052 0.7328 0.5699 0.0089  0.0991  -0.0262 414 ILE A CG1 
1301 C CG2 . ILE A 403 ? 0.4658 0.7397 0.5750 -0.0231 0.1057  -0.0302 414 ILE A CG2 
1302 C CD1 . ILE A 403 ? 0.4167 0.7556 0.5834 -0.0064 0.0835  -0.0215 414 ILE A CD1 
1303 N N   . THR A 404 ? 0.3989 0.7958 0.5981 0.0121  0.1500  -0.0433 415 THR A N   
1304 C CA  . THR A 404 ? 0.5026 0.9478 0.7393 0.0262  0.1608  -0.0450 415 THR A CA  
1305 C C   . THR A 404 ? 0.5730 1.0563 0.8275 0.0070  0.1542  -0.0411 415 THR A C   
1306 O O   . THR A 404 ? 0.5472 1.0240 0.7847 -0.0184 0.1482  -0.0401 415 THR A O   
1307 C CB  . THR A 404 ? 0.4635 0.8965 0.6916 0.0308  0.1821  -0.0531 415 THR A CB  
1308 O OG1 . THR A 404 ? 0.7683 1.2290 1.0291 0.0495  0.1902  -0.0524 415 THR A OG1 
1309 C CG2 . THR A 404 ? 0.4383 0.8702 0.6456 0.0029  0.1895  -0.0558 415 THR A CG2 
1310 N N   . PRO A 405 ? 0.7717 1.2931 1.0596 0.0176  0.1546  -0.0388 416 PRO A N   
1311 C CA  . PRO A 405 ? 0.7643 1.3226 1.0679 -0.0035 0.1497  -0.0374 416 PRO A CA  
1312 C C   . PRO A 405 ? 0.7540 1.3050 1.0384 -0.0311 0.1614  -0.0415 416 PRO A C   
1313 O O   . PRO A 405 ? 0.7238 1.2758 0.9992 -0.0567 0.1538  -0.0402 416 PRO A O   
1314 C CB  . PRO A 405 ? 0.8792 1.4762 1.2200 0.0166  0.1534  -0.0361 416 PRO A CB  
1315 C CG  . PRO A 405 ? 0.9479 1.5298 1.2943 0.0469  0.1477  -0.0320 416 PRO A CG  
1316 C CD  . PRO A 405 ? 0.8103 1.3417 1.1233 0.0489  0.1537  -0.0356 416 PRO A CD  
1317 N N   . GLU A 406 ? 0.7374 1.2778 1.0130 -0.0270 0.1802  -0.0462 417 GLU A N   
1318 C CA  . GLU A 406 ? 0.8436 1.3762 1.0987 -0.0520 0.1916  -0.0484 417 GLU A CA  
1319 C C   . GLU A 406 ? 0.7910 1.2771 1.0028 -0.0685 0.1897  -0.0479 417 GLU A C   
1320 O O   . GLU A 406 ? 0.7001 1.1728 0.8892 -0.0890 0.1979  -0.0476 417 GLU A O   
1321 C CB  . GLU A 406 ? 0.8931 1.4324 1.1525 -0.0415 0.2124  -0.0534 417 GLU A CB  
1322 C CG  . GLU A 406 ? 0.9908 1.5034 1.2407 -0.0161 0.2205  -0.0578 417 GLU A CG  
1323 C CD  . GLU A 406 ? 1.0070 1.5401 1.2924 0.0135  0.2183  -0.0565 417 GLU A CD  
1324 O OE1 . GLU A 406 ? 1.0231 1.5979 1.3427 0.0175  0.2192  -0.0544 417 GLU A OE1 
1325 O OE2 . GLU A 406 ? 0.9807 1.4868 1.2591 0.0324  0.2153  -0.0573 417 GLU A OE2 
1326 N N   . GLN A 407 ? 0.7020 1.1632 0.9015 -0.0595 0.1791  -0.0469 418 GLN A N   
1327 C CA  . GLN A 407 ? 0.6076 1.0260 0.7679 -0.0732 0.1755  -0.0455 418 GLN A CA  
1328 C C   . GLN A 407 ? 0.4980 0.9017 0.6596 -0.0642 0.1562  -0.0413 418 GLN A C   
1329 O O   . GLN A 407 ? 0.4668 0.8384 0.6151 -0.0470 0.1511  -0.0417 418 GLN A O   
1330 C CB  . GLN A 407 ? 0.6582 1.0449 0.7899 -0.0658 0.1878  -0.0509 418 GLN A CB  
1331 C CG  . GLN A 407 ? 0.7410 1.1140 0.8451 -0.0851 0.1989  -0.0502 418 GLN A CG  
1332 C CD  . GLN A 407 ? 0.9055 1.2512 0.9799 -0.1090 0.1906  -0.0422 418 GLN A CD  
1333 O OE1 . GLN A 407 ? 0.9128 1.2621 0.9824 -0.1285 0.1938  -0.0376 418 GLN A OE1 
1334 N NE2 . GLN A 407 ? 0.7660 1.0778 0.8193 -0.1054 0.1782  -0.0394 418 GLN A NE2 
1335 N N   . SER A 408 ? 0.4783 0.9010 0.6543 -0.0761 0.1439  -0.0372 419 SER A N   
1336 C CA  . SER A 408 ? 0.4613 0.8711 0.6390 -0.0675 0.1237  -0.0327 419 SER A CA  
1337 C C   . SER A 408 ? 0.4063 0.7646 0.5476 -0.0808 0.1128  -0.0284 419 SER A C   
1338 O O   . SER A 408 ? 0.4567 0.7999 0.5955 -0.0742 0.0971  -0.0252 419 SER A O   
1339 C CB  . SER A 408 ? 0.4997 0.9591 0.7108 -0.0734 0.1152  -0.0318 419 SER A CB  
1340 O OG  . SER A 408 ? 0.5761 1.0427 0.7821 -0.1041 0.1172  -0.0326 419 SER A OG  
1341 N N   . LYS A 409 ? 0.4192 0.7509 0.5318 -0.0980 0.1210  -0.0275 420 LYS A N   
1342 C CA  . LYS A 409 ? 0.4548 0.7374 0.5327 -0.1077 0.1116  -0.0221 420 LYS A CA  
1343 C C   . LYS A 409 ? 0.5086 0.7579 0.5540 -0.1065 0.1198  -0.0213 420 LYS A C   
1344 O O   . LYS A 409 ? 0.5058 0.7696 0.5516 -0.1060 0.1351  -0.0255 420 LYS A O   
1345 C CB  . LYS A 409 ? 0.4858 0.7662 0.5576 -0.1345 0.1106  -0.0189 420 LYS A CB  
1346 C CG  . LYS A 409 ? 0.5751 0.8855 0.6740 -0.1395 0.1001  -0.0210 420 LYS A CG  
1347 C CD  . LYS A 409 ? 0.6717 0.9807 0.7651 -0.1696 0.1026  -0.0206 420 LYS A CD  
1348 C CE  . LYS A 409 ? 0.8462 1.1822 0.9621 -0.1766 0.0902  -0.0245 420 LYS A CE  
1349 N NZ  . LYS A 409 ? 0.8335 1.1550 0.9377 -0.2076 0.0917  -0.0255 420 LYS A NZ  
1350 N N   . ARG A 410 ? 0.4369 0.6444 0.4551 -0.1044 0.1089  -0.0166 421 ARG A N   
1351 C CA  . ARG A 410 ? 0.4733 0.6481 0.4570 -0.1049 0.1120  -0.0141 421 ARG A CA  
1352 C C   . ARG A 410 ? 0.5233 0.6674 0.4792 -0.1217 0.1081  -0.0046 421 ARG A C   
1353 O O   . ARG A 410 ? 0.5381 0.6788 0.5001 -0.1316 0.1017  -0.0012 421 ARG A O   
1354 C CB  . ARG A 410 ? 0.5362 0.6907 0.5131 -0.0859 0.1029  -0.0165 421 ARG A CB  
1355 C CG  . ARG A 410 ? 0.4999 0.6766 0.5005 -0.0684 0.1091  -0.0252 421 ARG A CG  
1356 C CD  . ARG A 410 ? 0.6068 0.8011 0.6057 -0.0720 0.1280  -0.0314 421 ARG A CD  
1357 N NE  . ARG A 410 ? 0.5885 0.7961 0.6047 -0.0539 0.1368  -0.0407 421 ARG A NE  
1358 C CZ  . ARG A 410 ? 0.7212 0.9068 0.7211 -0.0444 0.1394  -0.0471 421 ARG A CZ  
1359 N NH1 . ARG A 410 ? 0.6639 0.8191 0.6313 -0.0510 0.1325  -0.0451 421 ARG A NH1 
1360 N NH2 . ARG A 410 ? 0.6657 0.8605 0.6826 -0.0279 0.1495  -0.0559 421 ARG A NH2 
1361 N N   . SER A 411 ? 0.5141 0.6345 0.4376 -0.1248 0.1121  -0.0001 422 SER A N   
1362 C CA  . SER A 411 ? 0.5959 0.6846 0.4907 -0.1383 0.1099  0.0114  422 SER A CA  
1363 C C   . SER A 411 ? 0.7450 0.8012 0.6073 -0.1301 0.1018  0.0181  422 SER A C   
1364 O O   . SER A 411 ? 0.6649 0.6916 0.5052 -0.1363 0.0972  0.0292  422 SER A O   
1365 C CB  . SER A 411 ? 0.6819 0.7791 0.5666 -0.1579 0.1266  0.0149  422 SER A CB  
1366 O OG  . SER A 411 ? 0.7887 0.8591 0.6572 -0.1739 0.1258  0.0255  422 SER A OG  
1367 N N   . GLU A 412 ? 0.7182 0.7788 0.5772 -0.1165 0.1000  0.0116  423 GLU A N   
1368 C CA  . GLU A 412 ? 0.6948 0.7325 0.5246 -0.1098 0.0919  0.0164  423 GLU A CA  
1369 C C   . GLU A 412 ? 0.6381 0.6558 0.4695 -0.0994 0.0750  0.0204  423 GLU A C   
1370 O O   . GLU A 412 ? 0.5422 0.5665 0.3987 -0.0924 0.0690  0.0151  423 GLU A O   
1371 C CB  . GLU A 412 ? 0.6198 0.6711 0.4465 -0.1021 0.0972  0.0051  423 GLU A CB  
1372 C CG  . GLU A 412 ? 1.0697 1.1361 0.8843 -0.1125 0.1149  0.0022  423 GLU A CG  
1373 C CD  . GLU A 412 ? 1.1972 1.2931 1.0429 -0.1149 0.1284  -0.0064 423 GLU A CD  
1374 O OE1 . GLU A 412 ? 1.0407 1.1483 0.9177 -0.1051 0.1239  -0.0122 423 GLU A OE1 
1375 O OE2 . GLU A 412 ? 1.1103 1.2195 0.9489 -0.1265 0.1438  -0.0064 423 GLU A OE2 
1376 N N   . MET A 413 ? 0.5058 0.5008 0.3093 -0.0975 0.0675  0.0304  424 MET A N   
1377 C CA  . MET A 413 ? 0.4994 0.4762 0.3017 -0.0867 0.0524  0.0351  424 MET A CA  
1378 C C   . MET A 413 ? 0.5204 0.5079 0.3300 -0.0745 0.0458  0.0252  424 MET A C   
1379 O O   . MET A 413 ? 0.5870 0.5711 0.3777 -0.0702 0.0401  0.0270  424 MET A O   
1380 C CB  . MET A 413 ? 0.5311 0.4833 0.3020 -0.0871 0.0475  0.0505  424 MET A CB  
1381 C CG  . MET A 413 ? 0.6430 0.5735 0.4026 -0.0981 0.0531  0.0625  424 MET A CG  
1382 S SD  . MET A 413 ? 0.6988 0.5991 0.4201 -0.0921 0.0463  0.0825  424 MET A SD  
1383 C CE  . MET A 413 ? 0.5891 0.4739 0.3228 -0.0756 0.0308  0.0839  424 MET A CE  
1384 N N   . VAL A 414 ? 0.4743 0.4751 0.3117 -0.0693 0.0465  0.0149  425 VAL A N   
1385 C CA  . VAL A 414 ? 0.4104 0.4182 0.2577 -0.0589 0.0427  0.0048  425 VAL A CA  
1386 C C   . VAL A 414 ? 0.4272 0.4266 0.2889 -0.0501 0.0312  0.0064  425 VAL A C   
1387 O O   . VAL A 414 ? 0.3938 0.3935 0.2710 -0.0509 0.0303  0.0083  425 VAL A O   
1388 C CB  . VAL A 414 ? 0.4493 0.4764 0.3155 -0.0576 0.0544  -0.0070 425 VAL A CB  
1389 C CG1 . VAL A 414 ? 0.4304 0.4583 0.3081 -0.0468 0.0517  -0.0167 425 VAL A CG1 
1390 C CG2 . VAL A 414 ? 0.5209 0.5565 0.3703 -0.0660 0.0670  -0.0101 425 VAL A CG2 
1391 N N   . GLY A 415 ? 0.4354 0.4299 0.2922 -0.0428 0.0228  0.0048  426 GLY A N   
1392 C CA  . GLY A 415 ? 0.3649 0.3532 0.2350 -0.0344 0.0134  0.0055  426 GLY A CA  
1393 C C   . GLY A 415 ? 0.4234 0.4036 0.2798 -0.0298 0.0030  0.0105  426 GLY A C   
1394 O O   . GLY A 415 ? 0.4471 0.4297 0.2847 -0.0322 0.0019  0.0121  426 GLY A O   
1395 N N   . THR A 416 ? 0.3365 0.3109 0.2034 -0.0224 -0.0047 0.0122  427 THR A N   
1396 C CA  . THR A 416 ? 0.3769 0.3462 0.2354 -0.0162 -0.0145 0.0180  427 THR A CA  
1397 C C   . THR A 416 ? 0.4170 0.3687 0.2706 -0.0141 -0.0174 0.0286  427 THR A C   
1398 O O   . THR A 416 ? 0.3716 0.3174 0.2378 -0.0141 -0.0160 0.0270  427 THR A O   
1399 C CB  . THR A 416 ? 0.3664 0.3417 0.2402 -0.0096 -0.0192 0.0115  427 THR A CB  
1400 O OG1 . THR A 416 ? 0.3770 0.3633 0.2544 -0.0129 -0.0143 0.0006  427 THR A OG1 
1401 C CG2 . THR A 416 ? 0.3920 0.3685 0.2591 -0.0030 -0.0290 0.0173  427 THR A CG2 
1402 N N   . PRO A 417 ? 0.4123 0.3543 0.2466 -0.0121 -0.0211 0.0395  428 PRO A N   
1403 C CA  . PRO A 417 ? 0.3659 0.2842 0.1915 -0.0126 -0.0197 0.0499  428 PRO A CA  
1404 C C   . PRO A 417 ? 0.4019 0.3084 0.2416 -0.0083 -0.0214 0.0477  428 PRO A C   
1405 O O   . PRO A 417 ? 0.4163 0.3110 0.2580 -0.0161 -0.0159 0.0471  428 PRO A O   
1406 C CB  . PRO A 417 ? 0.4304 0.3420 0.2359 -0.0048 -0.0260 0.0625  428 PRO A CB  
1407 C CG  . PRO A 417 ? 0.4868 0.4195 0.2821 -0.0095 -0.0259 0.0593  428 PRO A CG  
1408 C CD  . PRO A 417 ? 0.4023 0.3544 0.2194 -0.0110 -0.0252 0.0431  428 PRO A CD  
1409 N N   . TYR A 418 ? 0.3994 0.3111 0.2488 0.0024  -0.0281 0.0453  429 TYR A N   
1410 C CA  . TYR A 418 ? 0.4231 0.3216 0.2813 0.0072  -0.0292 0.0440  429 TYR A CA  
1411 C C   . TYR A 418 ? 0.3972 0.3010 0.2696 -0.0006 -0.0249 0.0347  429 TYR A C   
1412 O O   . TYR A 418 ? 0.3809 0.2715 0.2556 -0.0019 -0.0240 0.0333  429 TYR A O   
1413 C CB  . TYR A 418 ? 0.4010 0.3088 0.2680 0.0198  -0.0360 0.0426  429 TYR A CB  
1414 C CG  . TYR A 418 ? 0.3963 0.3076 0.2519 0.0283  -0.0418 0.0519  429 TYR A CG  
1415 C CD1 . TYR A 418 ? 0.3947 0.2855 0.2393 0.0380  -0.0434 0.0631  429 TYR A CD1 
1416 C CD2 . TYR A 418 ? 0.3495 0.2841 0.2037 0.0265  -0.0454 0.0496  429 TYR A CD2 
1417 C CE1 . TYR A 418 ? 0.4308 0.3278 0.2648 0.0480  -0.0497 0.0738  429 TYR A CE1 
1418 C CE2 . TYR A 418 ? 0.4089 0.3517 0.2513 0.0338  -0.0522 0.0586  429 TYR A CE2 
1419 C CZ  . TYR A 418 ? 0.5555 0.4810 0.3885 0.0456  -0.0550 0.0717  429 TYR A CZ  
1420 O OH  . TYR A 418 ? 0.4929 0.4292 0.3144 0.0552  -0.0628 0.0829  429 TYR A OH  
1421 N N   . TRP A 419 ? 0.3538 0.2773 0.2354 -0.0055 -0.0222 0.0282  430 TRP A N   
1422 C CA  . TRP A 419 ? 0.3572 0.2906 0.2540 -0.0100 -0.0191 0.0210  430 TRP A CA  
1423 C C   . TRP A 419 ? 0.3331 0.2700 0.2295 -0.0219 -0.0123 0.0206  430 TRP A C   
1424 O O   . TRP A 419 ? 0.3203 0.2704 0.2308 -0.0254 -0.0103 0.0154  430 TRP A O   
1425 C CB  . TRP A 419 ? 0.3212 0.2726 0.2307 -0.0054 -0.0190 0.0146  430 TRP A CB  
1426 C CG  . TRP A 419 ? 0.3201 0.2711 0.2347 0.0038  -0.0244 0.0134  430 TRP A CG  
1427 C CD1 . TRP A 419 ? 0.3061 0.2584 0.2310 0.0078  -0.0257 0.0107  430 TRP A CD1 
1428 C CD2 . TRP A 419 ? 0.3099 0.2626 0.2196 0.0093  -0.0286 0.0150  430 TRP A CD2 
1429 N NE1 . TRP A 419 ? 0.3091 0.2621 0.2361 0.0150  -0.0292 0.0104  430 TRP A NE1 
1430 C CE2 . TRP A 419 ? 0.3085 0.2636 0.2280 0.0158  -0.0313 0.0126  430 TRP A CE2 
1431 C CE3 . TRP A 419 ? 0.3176 0.2732 0.2156 0.0088  -0.0307 0.0182  430 TRP A CE3 
1432 C CZ2 . TRP A 419 ? 0.3222 0.2841 0.2429 0.0213  -0.0355 0.0127  430 TRP A CZ2 
1433 C CZ3 . TRP A 419 ? 0.3577 0.3216 0.2563 0.0148  -0.0365 0.0185  430 TRP A CZ3 
1434 C CH2 . TRP A 419 ? 0.3076 0.2753 0.2190 0.0207  -0.0385 0.0154  430 TRP A CH2 
1435 N N   . MET A 420 ? 0.3374 0.2657 0.2185 -0.0282 -0.0086 0.0265  431 MET A N   
1436 C CA  . MET A 420 ? 0.4080 0.3438 0.2897 -0.0407 -0.0004 0.0257  431 MET A CA  
1437 C C   . MET A 420 ? 0.3707 0.2951 0.2531 -0.0510 0.0018  0.0261  431 MET A C   
1438 O O   . MET A 420 ? 0.3866 0.2852 0.2566 -0.0509 0.0000  0.0311  431 MET A O   
1439 C CB  . MET A 420 ? 0.4064 0.3366 0.2683 -0.0446 0.0037  0.0324  431 MET A CB  
1440 C CG  . MET A 420 ? 0.4480 0.3937 0.3092 -0.0381 0.0026  0.0286  431 MET A CG  
1441 S SD  . MET A 420 ? 0.4318 0.3746 0.2658 -0.0410 0.0048  0.0360  431 MET A SD  
1442 C CE  . MET A 420 ? 0.4301 0.3702 0.2575 -0.0568 0.0172  0.0395  431 MET A CE  
1443 N N   . ALA A 421 ? 0.3716 0.3160 0.2689 -0.0603 0.0063  0.0203  432 ALA A N   
1444 C CA  . ALA A 421 ? 0.3644 0.3034 0.2635 -0.0741 0.0088  0.0185  432 ALA A CA  
1445 C C   . ALA A 421 ? 0.4618 0.3788 0.3416 -0.0869 0.0166  0.0257  432 ALA A C   
1446 O O   . ALA A 421 ? 0.4075 0.3262 0.2774 -0.0873 0.0214  0.0309  432 ALA A O   
1447 C CB  . ALA A 421 ? 0.3593 0.3332 0.2813 -0.0805 0.0112  0.0111  432 ALA A CB  
1448 N N   . PRO A 422 ? 0.4502 0.3452 0.3229 -0.0988 0.0188  0.0259  433 PRO A N   
1449 C CA  . PRO A 422 ? 0.4366 0.3038 0.2882 -0.1112 0.0277  0.0345  433 PRO A CA  
1450 C C   . PRO A 422 ? 0.5040 0.3924 0.3588 -0.1254 0.0377  0.0350  433 PRO A C   
1451 O O   . PRO A 422 ? 0.4949 0.3667 0.3296 -0.1295 0.0447  0.0448  433 PRO A O   
1452 C CB  . PRO A 422 ? 0.4907 0.3334 0.3387 -0.1240 0.0295  0.0303  433 PRO A CB  
1453 C CG  . PRO A 422 ? 0.4655 0.3158 0.3259 -0.1120 0.0193  0.0220  433 PRO A CG  
1454 C CD  . PRO A 422 ? 0.4160 0.3088 0.2972 -0.1026 0.0145  0.0178  433 PRO A CD  
1455 N N   . GLU A 423 ? 0.4849 0.4111 0.3643 -0.1325 0.0391  0.0252  434 GLU A N   
1456 C CA  . GLU A 423 ? 0.4335 0.3836 0.3188 -0.1454 0.0500  0.0248  434 GLU A CA  
1457 C C   . GLU A 423 ? 0.4598 0.4195 0.3383 -0.1338 0.0525  0.0289  434 GLU A C   
1458 O O   . GLU A 423 ? 0.4516 0.4168 0.3219 -0.1438 0.0634  0.0324  434 GLU A O   
1459 C CB  . GLU A 423 ? 0.4248 0.4186 0.3412 -0.1525 0.0501  0.0138  434 GLU A CB  
1460 C CG  . GLU A 423 ? 0.4013 0.4241 0.3389 -0.1330 0.0415  0.0081  434 GLU A CG  
1461 C CD  . GLU A 423 ? 0.4342 0.4540 0.3791 -0.1274 0.0299  0.0034  434 GLU A CD  
1462 O OE1 . GLU A 423 ? 0.3647 0.3508 0.2931 -0.1318 0.0271  0.0051  434 GLU A OE1 
1463 O OE2 . GLU A 423 ? 0.3919 0.4426 0.3583 -0.1179 0.0245  -0.0017 434 GLU A OE2 
1464 N N   . VAL A 424 ? 0.3808 0.3424 0.2612 -0.1144 0.0435  0.0277  435 VAL A N   
1465 C CA  . VAL A 424 ? 0.4151 0.3820 0.2854 -0.1047 0.0452  0.0300  435 VAL A CA  
1466 C C   . VAL A 424 ? 0.4581 0.3931 0.2966 -0.1046 0.0453  0.0423  435 VAL A C   
1467 O O   . VAL A 424 ? 0.4613 0.3977 0.2833 -0.1091 0.0527  0.0471  435 VAL A O   
1468 C CB  . VAL A 424 ? 0.4163 0.3942 0.2987 -0.0866 0.0362  0.0240  435 VAL A CB  
1469 C CG1 . VAL A 424 ? 0.4054 0.3881 0.2758 -0.0798 0.0387  0.0240  435 VAL A CG1 
1470 C CG2 . VAL A 424 ? 0.4020 0.4098 0.3139 -0.0844 0.0363  0.0146  435 VAL A CG2 
1471 N N   . VAL A 425 ? 0.4294 0.3359 0.2583 -0.0985 0.0374  0.0480  436 VAL A N   
1472 C CA  . VAL A 425 ? 0.4899 0.3666 0.2900 -0.0939 0.0359  0.0616  436 VAL A CA  
1473 C C   . VAL A 425 ? 0.4763 0.3366 0.2570 -0.1105 0.0480  0.0709  436 VAL A C   
1474 O O   . VAL A 425 ? 0.5258 0.3763 0.2818 -0.1090 0.0505  0.0820  436 VAL A O   
1475 C CB  . VAL A 425 ? 0.4563 0.3047 0.2527 -0.0838 0.0274  0.0656  436 VAL A CB  
1476 C CG1 . VAL A 425 ? 0.4920 0.3070 0.2589 -0.0787 0.0275  0.0821  436 VAL A CG1 
1477 C CG2 . VAL A 425 ? 0.4062 0.2700 0.2185 -0.0668 0.0160  0.0583  436 VAL A CG2 
1478 N N   . THR A 426 ? 0.5001 0.3597 0.2911 -0.1277 0.0559  0.0664  437 THR A N   
1479 C CA  . THR A 426 ? 0.5114 0.3541 0.2854 -0.1469 0.0693  0.0746  437 THR A CA  
1480 C C   . THR A 426 ? 0.5067 0.3840 0.2898 -0.1603 0.0808  0.0693  437 THR A C   
1481 O O   . THR A 426 ? 0.5374 0.4070 0.3117 -0.1799 0.0937  0.0737  437 THR A O   
1482 C CB  . THR A 426 ? 0.5686 0.3867 0.3457 -0.1618 0.0730  0.0725  437 THR A CB  
1483 O OG1 . THR A 426 ? 0.5225 0.3734 0.3313 -0.1685 0.0707  0.0566  437 THR A OG1 
1484 C CG2 . THR A 426 ? 0.6173 0.3963 0.3817 -0.1479 0.0646  0.0784  437 THR A CG2 
1485 N N   . ARG A 427 ? 0.4784 0.3918 0.2782 -0.1503 0.0780  0.0600  438 ARG A N   
1486 C CA  . ARG A 427 ? 0.4714 0.4172 0.2779 -0.1585 0.0898  0.0549  438 ARG A CA  
1487 C C   . ARG A 427 ? 0.5227 0.4906 0.3517 -0.1779 0.1001  0.0479  438 ARG A C   
1488 O O   . ARG A 427 ? 0.5179 0.4973 0.3423 -0.1931 0.1144  0.0496  438 ARG A O   
1489 C CB  . ARG A 427 ? 0.5265 0.4567 0.2984 -0.1623 0.0976  0.0673  438 ARG A CB  
1490 C CG  . ARG A 427 ? 0.5615 0.4872 0.3176 -0.1431 0.0869  0.0701  438 ARG A CG  
1491 C CD  . ARG A 427 ? 0.5710 0.4806 0.2890 -0.1446 0.0911  0.0842  438 ARG A CD  
1492 N NE  . ARG A 427 ? 0.7127 0.5848 0.4104 -0.1530 0.0945  0.0999  438 ARG A NE  
1493 C CZ  . ARG A 427 ? 0.6546 0.5198 0.3417 -0.1630 0.1050  0.1071  438 ARG A CZ  
1494 N NH1 . ARG A 427 ? 0.7126 0.6031 0.3971 -0.1684 0.1147  0.1032  438 ARG A NH1 
1495 N NH2 . ARG A 427 ? 0.7298 0.5605 0.4082 -0.1672 0.1068  0.1182  438 ARG A NH2 
1496 N N   . LYS A 428 ? 0.4519 0.4277 0.3048 -0.1787 0.0929  0.0399  439 LYS A N   
1497 C CA  . LYS A 428 ? 0.6022 0.6111 0.4827 -0.1952 0.0998  0.0309  439 LYS A CA  
1498 C C   . LYS A 428 ? 0.5191 0.5758 0.4308 -0.1827 0.0983  0.0200  439 LYS A C   
1499 O O   . LYS A 428 ? 0.4883 0.5464 0.4009 -0.1621 0.0906  0.0182  439 LYS A O   
1500 C CB  . LYS A 428 ? 0.5385 0.5331 0.4262 -0.2048 0.0932  0.0275  439 LYS A CB  
1501 C CG  . LYS A 428 ? 0.6006 0.5408 0.4557 -0.2149 0.0966  0.0386  439 LYS A CG  
1502 C CD  . LYS A 428 ? 0.7072 0.6266 0.5655 -0.2259 0.0922  0.0336  439 LYS A CD  
1503 C CE  . LYS A 428 ? 0.7307 0.5895 0.5544 -0.2317 0.0971  0.0458  439 LYS A CE  
1504 N NZ  . LYS A 428 ? 0.8855 0.7156 0.7081 -0.2389 0.0930  0.0399  439 LYS A NZ  
1505 N N   . ALA A 429 ? 0.5060 0.6025 0.4436 -0.1953 0.1068  0.0129  440 ALA A N   
1506 C CA  . ALA A 429 ? 0.4486 0.5909 0.4189 -0.1813 0.1053  0.0035  440 ALA A CA  
1507 C C   . ALA A 429 ? 0.3521 0.4958 0.3372 -0.1671 0.0888  -0.0003 440 ALA A C   
1508 O O   . ALA A 429 ? 0.4330 0.5689 0.4204 -0.1777 0.0820  -0.0013 440 ALA A O   
1509 C CB  . ALA A 429 ? 0.4896 0.6786 0.4880 -0.1974 0.1166  -0.0025 440 ALA A CB  
1510 N N   . TYR A 430 ? 0.4337 0.5864 0.4274 -0.1442 0.0834  -0.0030 441 TYR A N   
1511 C CA  . TYR A 430 ? 0.4205 0.5703 0.4238 -0.1297 0.0685  -0.0049 441 TYR A CA  
1512 C C   . TYR A 430 ? 0.4404 0.6248 0.4707 -0.1106 0.0678  -0.0099 441 TYR A C   
1513 O O   . TYR A 430 ? 0.3327 0.5346 0.3700 -0.1046 0.0786  -0.0124 441 TYR A O   
1514 C CB  . TYR A 430 ? 0.3546 0.4602 0.3308 -0.1195 0.0600  0.0004  441 TYR A CB  
1515 C CG  . TYR A 430 ? 0.3472 0.4428 0.3099 -0.1062 0.0634  0.0016  441 TYR A CG  
1516 C CD1 . TYR A 430 ? 0.3851 0.4921 0.3609 -0.0873 0.0602  -0.0030 441 TYR A CD1 
1517 C CD2 . TYR A 430 ? 0.4127 0.4859 0.3478 -0.1130 0.0698  0.0074  441 TYR A CD2 
1518 C CE1 . TYR A 430 ? 0.4288 0.5255 0.3912 -0.0779 0.0638  -0.0043 441 TYR A CE1 
1519 C CE2 . TYR A 430 ? 0.4530 0.5198 0.3740 -0.1026 0.0720  0.0069  441 TYR A CE2 
1520 C CZ  . TYR A 430 ? 0.4479 0.5266 0.3831 -0.0860 0.0691  -0.0002 441 TYR A CZ  
1521 O OH  . TYR A 430 ? 0.4366 0.5082 0.3572 -0.0783 0.0718  -0.0029 441 TYR A OH  
1522 N N   . GLY A 431 ? 0.3466 0.5381 0.3902 -0.1002 0.0555  -0.0111 442 GLY A N   
1523 C CA  . GLY A 431 ? 0.3323 0.5532 0.4008 -0.0807 0.0538  -0.0136 442 GLY A CA  
1524 C C   . GLY A 431 ? 0.2948 0.4954 0.3581 -0.0633 0.0422  -0.0115 442 GLY A C   
1525 O O   . GLY A 431 ? 0.2736 0.4367 0.3132 -0.0632 0.0374  -0.0091 442 GLY A O   
1526 N N   . PRO A 432 ? 0.2633 0.4905 0.3494 -0.0478 0.0380  -0.0117 443 PRO A N   
1527 C CA  . PRO A 432 ? 0.2573 0.4663 0.3392 -0.0303 0.0292  -0.0089 443 PRO A CA  
1528 C C   . PRO A 432 ? 0.2557 0.4401 0.3209 -0.0367 0.0173  -0.0072 443 PRO A C   
1529 O O   . PRO A 432 ? 0.2618 0.4218 0.3161 -0.0255 0.0124  -0.0050 443 PRO A O   
1530 C CB  . PRO A 432 ? 0.2622 0.5099 0.3728 -0.0151 0.0270  -0.0074 443 PRO A CB  
1531 C CG  . PRO A 432 ? 0.2903 0.5744 0.4212 -0.0191 0.0381  -0.0105 443 PRO A CG  
1532 C CD  . PRO A 432 ? 0.2679 0.5448 0.3854 -0.0445 0.0420  -0.0134 443 PRO A CD  
1533 N N   . LYS A 433 ? 0.2275 0.4171 0.2905 -0.0548 0.0135  -0.0088 444 LYS A N   
1534 C CA  . LYS A 433 ? 0.2556 0.4213 0.3030 -0.0596 0.0034  -0.0086 444 LYS A CA  
1535 C C   . LYS A 433 ? 0.2811 0.4017 0.3018 -0.0608 0.0045  -0.0065 444 LYS A C   
1536 O O   . LYS A 433 ? 0.2752 0.3731 0.2829 -0.0615 -0.0026 -0.0062 444 LYS A O   
1537 C CB  . LYS A 433 ? 0.3056 0.4861 0.3565 -0.0803 0.0004  -0.0130 444 LYS A CB  
1538 C CG  . LYS A 433 ? 0.3660 0.5923 0.4410 -0.0772 -0.0070 -0.0149 444 LYS A CG  
1539 C CD  . LYS A 433 ? 0.3321 0.5784 0.4120 -0.1014 -0.0091 -0.0214 444 LYS A CD  
1540 C CE  . LYS A 433 ? 0.3182 0.6156 0.4214 -0.0987 -0.0188 -0.0234 444 LYS A CE  
1541 N NZ  . LYS A 433 ? 0.2725 0.5909 0.3797 -0.1260 -0.0214 -0.0322 444 LYS A NZ  
1542 N N   . VAL A 434 ? 0.2514 0.3603 0.2635 -0.0606 0.0131  -0.0049 445 VAL A N   
1543 C CA  . VAL A 434 ? 0.2712 0.3430 0.2594 -0.0580 0.0121  -0.0017 445 VAL A CA  
1544 C C   . VAL A 434 ? 0.2796 0.3420 0.2676 -0.0410 0.0058  -0.0011 445 VAL A C   
1545 O O   . VAL A 434 ? 0.2827 0.3191 0.2550 -0.0384 0.0012  0.0011  445 VAL A O   
1546 C CB  . VAL A 434 ? 0.3057 0.3709 0.2828 -0.0612 0.0218  -0.0002 445 VAL A CB  
1547 C CG1 . VAL A 434 ? 0.2910 0.3655 0.2678 -0.0797 0.0299  0.0000  445 VAL A CG1 
1548 C CG2 . VAL A 434 ? 0.2999 0.3814 0.2884 -0.0482 0.0273  -0.0034 445 VAL A CG2 
1549 N N   . ASP A 435 ? 0.2404 0.3235 0.2458 -0.0289 0.0065  -0.0024 446 ASP A N   
1550 C CA  . ASP A 435 ? 0.2586 0.3316 0.2638 -0.0144 0.0019  -0.0013 446 ASP A CA  
1551 C C   . ASP A 435 ? 0.2500 0.3198 0.2537 -0.0140 -0.0077 0.0000  446 ASP A C   
1552 O O   . ASP A 435 ? 0.2560 0.3083 0.2517 -0.0068 -0.0117 0.0013  446 ASP A O   
1553 C CB  . ASP A 435 ? 0.2322 0.3238 0.2551 -0.0009 0.0066  -0.0016 446 ASP A CB  
1554 C CG  . ASP A 435 ? 0.2325 0.3208 0.2537 0.0015  0.0174  -0.0050 446 ASP A CG  
1555 O OD1 . ASP A 435 ? 0.2780 0.3463 0.2813 -0.0043 0.0190  -0.0063 446 ASP A OD1 
1556 O OD2 . ASP A 435 ? 0.2556 0.3614 0.2929 0.0107  0.0243  -0.0062 446 ASP A OD2 
1557 N N   . ILE A 436 ? 0.2262 0.3147 0.2377 -0.0228 -0.0110 -0.0013 447 ILE A N   
1558 C CA  . ILE A 436 ? 0.2760 0.3623 0.2833 -0.0250 -0.0198 -0.0021 447 ILE A CA  
1559 C C   . ILE A 436 ? 0.3185 0.3712 0.3049 -0.0325 -0.0211 -0.0031 447 ILE A C   
1560 O O   . ILE A 436 ? 0.2838 0.3217 0.2616 -0.0272 -0.0259 -0.0031 447 ILE A O   
1561 C CB  . ILE A 436 ? 0.3267 0.4447 0.3470 -0.0354 -0.0229 -0.0052 447 ILE A CB  
1562 C CG1 . ILE A 436 ? 0.2619 0.4162 0.3048 -0.0230 -0.0229 -0.0023 447 ILE A CG1 
1563 C CG2 . ILE A 436 ? 0.2966 0.4089 0.3072 -0.0422 -0.0312 -0.0086 447 ILE A CG2 
1564 C CD1 . ILE A 436 ? 0.2665 0.4204 0.3104 -0.0052 -0.0283 0.0028  447 ILE A CD1 
1565 N N   . TRP A 437 ? 0.2637 0.3035 0.2413 -0.0438 -0.0158 -0.0032 448 TRP A N   
1566 C CA  . TRP A 437 ? 0.2694 0.2747 0.2268 -0.0473 -0.0158 -0.0018 448 TRP A CA  
1567 C C   . TRP A 437 ? 0.3087 0.2985 0.2594 -0.0328 -0.0176 0.0015  448 TRP A C   
1568 O O   . TRP A 437 ? 0.2932 0.2646 0.2346 -0.0285 -0.0214 0.0017  448 TRP A O   
1569 C CB  . TRP A 437 ? 0.2528 0.2471 0.2009 -0.0593 -0.0085 0.0006  448 TRP A CB  
1570 C CG  . TRP A 437 ? 0.3099 0.2673 0.2366 -0.0595 -0.0083 0.0048  448 TRP A CG  
1571 C CD1 . TRP A 437 ? 0.3347 0.2769 0.2513 -0.0481 -0.0094 0.0100  448 TRP A CD1 
1572 C CD2 . TRP A 437 ? 0.3214 0.2534 0.2350 -0.0706 -0.0068 0.0042  448 TRP A CD2 
1573 N NE1 . TRP A 437 ? 0.3476 0.2585 0.2466 -0.0489 -0.0093 0.0143  448 TRP A NE1 
1574 C CE2 . TRP A 437 ? 0.3596 0.2603 0.2557 -0.0624 -0.0069 0.0108  448 TRP A CE2 
1575 C CE3 . TRP A 437 ? 0.3416 0.2743 0.2563 -0.0872 -0.0052 -0.0018 448 TRP A CE3 
1576 C CZ2 . TRP A 437 ? 0.3748 0.2409 0.2542 -0.0679 -0.0041 0.0126  448 TRP A CZ2 
1577 C CZ3 . TRP A 437 ? 0.4479 0.3448 0.3451 -0.0955 -0.0020 -0.0019 448 TRP A CZ3 
1578 C CH2 . TRP A 437 ? 0.4898 0.3515 0.3692 -0.0848 -0.0009 0.0058  448 TRP A CH2 
1579 N N   . SER A 438 ? 0.2599 0.2577 0.2152 -0.0260 -0.0142 0.0031  449 SER A N   
1580 C CA  . SER A 438 ? 0.2519 0.2380 0.2015 -0.0153 -0.0158 0.0048  449 SER A CA  
1581 C C   . SER A 438 ? 0.2670 0.2555 0.2228 -0.0060 -0.0204 0.0038  449 SER A C   
1582 O O   . SER A 438 ? 0.2625 0.2379 0.2117 -0.0002 -0.0231 0.0048  449 SER A O   
1583 C CB  . SER A 438 ? 0.2343 0.2292 0.1873 -0.0124 -0.0102 0.0040  449 SER A CB  
1584 O OG  . SER A 438 ? 0.2981 0.2907 0.2422 -0.0215 -0.0052 0.0054  449 SER A OG  
1585 N N   . LEU A 439 ? 0.2620 0.2691 0.2304 -0.0040 -0.0213 0.0027  450 LEU A N   
1586 C CA  . LEU A 439 ? 0.2728 0.2817 0.2438 0.0041  -0.0255 0.0033  450 LEU A CA  
1587 C C   . LEU A 439 ? 0.2540 0.2492 0.2139 0.0004  -0.0300 0.0017  450 LEU A C   
1588 O O   . LEU A 439 ? 0.2932 0.2803 0.2490 0.0071  -0.0318 0.0021  450 LEU A O   
1589 C CB  . LEU A 439 ? 0.2946 0.3281 0.2794 0.0074  -0.0267 0.0043  450 LEU A CB  
1590 C CG  . LEU A 439 ? 0.3413 0.3783 0.3256 0.0149  -0.0315 0.0065  450 LEU A CG  
1591 C CD1 . LEU A 439 ? 0.3150 0.3399 0.2985 0.0256  -0.0283 0.0097  450 LEU A CD1 
1592 C CD2 . LEU A 439 ? 0.3291 0.3946 0.3257 0.0176  -0.0346 0.0089  450 LEU A CD2 
1593 N N   . GLY A 440 ? 0.2797 0.2719 0.2345 -0.0110 -0.0305 -0.0010 451 GLY A N   
1594 C CA  . GLY A 440 ? 0.3001 0.2733 0.2422 -0.0151 -0.0325 -0.0041 451 GLY A CA  
1595 C C   . GLY A 440 ? 0.3424 0.2914 0.2741 -0.0085 -0.0312 -0.0015 451 GLY A C   
1596 O O   . GLY A 440 ? 0.3245 0.2621 0.2501 -0.0033 -0.0325 -0.0031 451 GLY A O   
1597 N N   . ILE A 441 ? 0.2705 0.2140 0.2002 -0.0083 -0.0284 0.0025  452 ILE A N   
1598 C CA  . ILE A 441 ? 0.2885 0.2160 0.2102 -0.0005 -0.0287 0.0062  452 ILE A CA  
1599 C C   . ILE A 441 ? 0.3200 0.2564 0.2488 0.0100  -0.0306 0.0059  452 ILE A C   
1600 O O   . ILE A 441 ? 0.3089 0.2365 0.2341 0.0172  -0.0318 0.0066  452 ILE A O   
1601 C CB  . ILE A 441 ? 0.2898 0.2144 0.2062 -0.0030 -0.0263 0.0109  452 ILE A CB  
1602 C CG1 . ILE A 441 ? 0.3237 0.2368 0.2316 -0.0150 -0.0227 0.0121  452 ILE A CG1 
1603 C CG2 . ILE A 441 ? 0.3020 0.2154 0.2104 0.0061  -0.0284 0.0156  452 ILE A CG2 
1604 C CD1 . ILE A 441 ? 0.4196 0.3041 0.3139 -0.0154 -0.0222 0.0136  452 ILE A CD1 
1605 N N   . MET A 442 ? 0.2602 0.2136 0.1996 0.0114  -0.0297 0.0050  453 MET A N   
1606 C CA  . MET A 442 ? 0.2637 0.2224 0.2089 0.0193  -0.0298 0.0049  453 MET A CA  
1607 C C   . MET A 442 ? 0.3192 0.2760 0.2628 0.0226  -0.0315 0.0035  453 MET A C   
1608 O O   . MET A 442 ? 0.2901 0.2456 0.2345 0.0285  -0.0310 0.0036  453 MET A O   
1609 C CB  . MET A 442 ? 0.3089 0.2804 0.2640 0.0204  -0.0267 0.0048  453 MET A CB  
1610 C CG  . MET A 442 ? 0.4090 0.3811 0.3686 0.0257  -0.0243 0.0046  453 MET A CG  
1611 S SD  . MET A 442 ? 0.3787 0.3575 0.3470 0.0266  -0.0178 0.0036  453 MET A SD  
1612 C CE  . MET A 442 ? 0.4246 0.4140 0.4004 0.0312  -0.0183 0.0073  453 MET A CE  
1613 N N   . ALA A 443 ? 0.2697 0.2287 0.2110 0.0179  -0.0331 0.0015  454 ALA A N   
1614 C CA  . ALA A 443 ? 0.3394 0.2958 0.2751 0.0198  -0.0345 -0.0011 454 ALA A CA  
1615 C C   . ALA A 443 ? 0.3740 0.3113 0.3004 0.0220  -0.0334 -0.0033 454 ALA A C   
1616 O O   . ALA A 443 ? 0.3243 0.2590 0.2480 0.0279  -0.0324 -0.0048 454 ALA A O   
1617 C CB  . ALA A 443 ? 0.3322 0.2982 0.2662 0.0122  -0.0373 -0.0042 454 ALA A CB  
1618 N N   . ILE A 444 ? 0.3071 0.2303 0.2280 0.0186  -0.0328 -0.0026 455 ILE A N   
1619 C CA  . ILE A 444 ? 0.3066 0.2105 0.2198 0.0245  -0.0312 -0.0023 455 ILE A CA  
1620 C C   . ILE A 444 ? 0.3240 0.2357 0.2443 0.0350  -0.0314 0.0012  455 ILE A C   
1621 O O   . ILE A 444 ? 0.3448 0.2512 0.2640 0.0432  -0.0300 0.0003  455 ILE A O   
1622 C CB  . ILE A 444 ? 0.3245 0.2097 0.2290 0.0194  -0.0299 0.0004  455 ILE A CB  
1623 C CG1 . ILE A 444 ? 0.3315 0.2073 0.2287 0.0066  -0.0284 -0.0055 455 ILE A CG1 
1624 C CG2 . ILE A 444 ? 0.3568 0.2222 0.2543 0.0297  -0.0283 0.0037  455 ILE A CG2 
1625 C CD1 . ILE A 444 ? 0.4363 0.2886 0.3227 -0.0012 -0.0249 -0.0029 455 ILE A CD1 
1626 N N   . GLU A 445 ? 0.2998 0.2251 0.2277 0.0343  -0.0325 0.0043  456 GLU A N   
1627 C CA  . GLU A 445 ? 0.2977 0.2342 0.2334 0.0408  -0.0327 0.0056  456 GLU A CA  
1628 C C   . GLU A 445 ? 0.2933 0.2365 0.2337 0.0444  -0.0305 0.0028  456 GLU A C   
1629 O O   . GLU A 445 ? 0.3127 0.2607 0.2574 0.0507  -0.0294 0.0026  456 GLU A O   
1630 C CB  . GLU A 445 ? 0.2811 0.2298 0.2229 0.0368  -0.0328 0.0063  456 GLU A CB  
1631 C CG  . GLU A 445 ? 0.2942 0.2411 0.2308 0.0334  -0.0342 0.0091  456 GLU A CG  
1632 C CD  . GLU A 445 ? 0.2905 0.2500 0.2329 0.0298  -0.0328 0.0071  456 GLU A CD  
1633 O OE1 . GLU A 445 ? 0.2837 0.2522 0.2301 0.0319  -0.0339 0.0059  456 GLU A OE1 
1634 O OE2 . GLU A 445 ? 0.2888 0.2502 0.2329 0.0250  -0.0299 0.0056  456 GLU A OE2 
1635 N N   . MET A 446 ? 0.2591 0.2057 0.1992 0.0405  -0.0296 0.0015  457 MET A N   
1636 C CA  . MET A 446 ? 0.3301 0.2827 0.2717 0.0434  -0.0270 0.0006  457 MET A CA  
1637 C C   . MET A 446 ? 0.3537 0.2982 0.2877 0.0474  -0.0255 -0.0031 457 MET A C   
1638 O O   . MET A 446 ? 0.3738 0.3235 0.3095 0.0517  -0.0218 -0.0039 457 MET A O   
1639 C CB  . MET A 446 ? 0.2814 0.2406 0.2227 0.0402  -0.0273 0.0021  457 MET A CB  
1640 C CG  . MET A 446 ? 0.3363 0.3019 0.2865 0.0393  -0.0259 0.0054  457 MET A CG  
1641 S SD  . MET A 446 ? 0.3406 0.3148 0.2930 0.0406  -0.0253 0.0100  457 MET A SD  
1642 C CE  . MET A 446 ? 0.3823 0.3623 0.3376 0.0358  -0.0288 0.0091  457 MET A CE  
1643 N N   . ILE A 447 ? 0.3212 0.2517 0.2460 0.0451  -0.0267 -0.0060 458 ILE A N   
1644 C CA  . ILE A 447 ? 0.3972 0.3148 0.3127 0.0487  -0.0236 -0.0113 458 ILE A CA  
1645 C C   . ILE A 447 ? 0.4142 0.3259 0.3336 0.0590  -0.0213 -0.0098 458 ILE A C   
1646 O O   . ILE A 447 ? 0.4090 0.3219 0.3291 0.0666  -0.0169 -0.0127 458 ILE A O   
1647 C CB  . ILE A 447 ? 0.4008 0.3014 0.3043 0.0408  -0.0245 -0.0160 458 ILE A CB  
1648 C CG1 . ILE A 447 ? 0.4510 0.3629 0.3513 0.0309  -0.0277 -0.0185 458 ILE A CG1 
1649 C CG2 . ILE A 447 ? 0.4722 0.3519 0.3647 0.0453  -0.0194 -0.0226 458 ILE A CG2 
1650 C CD1 . ILE A 447 ? 0.5013 0.4017 0.3943 0.0196  -0.0291 -0.0225 458 ILE A CD1 
1651 N N   . GLU A 448 ? 0.3694 0.2755 0.2905 0.0602  -0.0241 -0.0050 459 GLU A N   
1652 C CA  . GLU A 448 ? 0.3599 0.2589 0.2825 0.0715  -0.0233 -0.0018 459 GLU A CA  
1653 C C   . GLU A 448 ? 0.3731 0.2940 0.3090 0.0767  -0.0265 0.0035  459 GLU A C   
1654 O O   . GLU A 448 ? 0.4233 0.3472 0.3640 0.0883  -0.0265 0.0065  459 GLU A O   
1655 C CB  . GLU A 448 ? 0.4143 0.2884 0.3255 0.0701  -0.0238 0.0012  459 GLU A CB  
1656 C CG  . GLU A 448 ? 0.5261 0.3762 0.4234 0.0633  -0.0197 -0.0060 459 GLU A CG  
1657 C CD  . GLU A 448 ? 0.5941 0.4135 0.4788 0.0616  -0.0175 -0.0031 459 GLU A CD  
1658 O OE1 . GLU A 448 ? 0.5124 0.3309 0.3975 0.0634  -0.0203 0.0059  459 GLU A OE1 
1659 O OE2 . GLU A 448 ? 0.6206 0.4155 0.4932 0.0575  -0.0124 -0.0102 459 GLU A OE2 
1660 N N   . GLY A 449 ? 0.3213 0.2581 0.2636 0.0686  -0.0289 0.0042  460 GLY A N   
1661 C CA  . GLY A 449 ? 0.3107 0.2684 0.2641 0.0696  -0.0317 0.0067  460 GLY A CA  
1662 C C   . GLY A 449 ? 0.3657 0.3234 0.3153 0.0668  -0.0367 0.0114  460 GLY A C   
1663 O O   . GLY A 449 ? 0.3079 0.2838 0.2645 0.0639  -0.0392 0.0115  460 GLY A O   
1664 N N   . GLU A 450 ? 0.3775 0.3152 0.3149 0.0653  -0.0372 0.0143  461 GLU A N   
1665 C CA  . GLU A 450 ? 0.3585 0.2942 0.2890 0.0629  -0.0408 0.0200  461 GLU A CA  
1666 C C   . GLU A 450 ? 0.3856 0.3008 0.3046 0.0545  -0.0385 0.0203  461 GLU A C   
1667 O O   . GLU A 450 ? 0.3549 0.2544 0.2696 0.0535  -0.0353 0.0171  461 GLU A O   
1668 C CB  . GLU A 450 ? 0.4202 0.3537 0.3473 0.0752  -0.0441 0.0277  461 GLU A CB  
1669 C CG  . GLU A 450 ? 0.4238 0.3856 0.3641 0.0831  -0.0482 0.0285  461 GLU A CG  
1670 C CD  . GLU A 450 ? 0.6027 0.5646 0.5400 0.0981  -0.0524 0.0382  461 GLU A CD  
1671 O OE1 . GLU A 450 ? 0.5004 0.4342 0.4238 0.1030  -0.0506 0.0446  461 GLU A OE1 
1672 O OE2 . GLU A 450 ? 0.5058 0.4961 0.4547 0.1050  -0.0574 0.0398  461 GLU A OE2 
1673 N N   . PRO A 451 ? 0.3032 0.2195 0.2167 0.0473  -0.0395 0.0232  462 PRO A N   
1674 C CA  . PRO A 451 ? 0.3565 0.2547 0.2592 0.0389  -0.0366 0.0247  462 PRO A CA  
1675 C C   . PRO A 451 ? 0.3483 0.2216 0.2382 0.0451  -0.0357 0.0317  462 PRO A C   
1676 O O   . PRO A 451 ? 0.3627 0.2374 0.2520 0.0574  -0.0387 0.0376  462 PRO A O   
1677 C CB  . PRO A 451 ? 0.3623 0.2719 0.2629 0.0312  -0.0368 0.0264  462 PRO A CB  
1678 C CG  . PRO A 451 ? 0.3344 0.2605 0.2377 0.0380  -0.0414 0.0286  462 PRO A CG  
1679 C CD  . PRO A 451 ? 0.3281 0.2632 0.2438 0.0457  -0.0427 0.0247  462 PRO A CD  
1680 N N   . PRO A 452 ? 0.3904 0.2405 0.2700 0.0372  -0.0313 0.0316  463 PRO A N   
1681 C CA  . PRO A 452 ? 0.4488 0.2688 0.3137 0.0429  -0.0287 0.0395  463 PRO A CA  
1682 C C   . PRO A 452 ? 0.4551 0.2778 0.3115 0.0480  -0.0317 0.0515  463 PRO A C   
1683 O O   . PRO A 452 ? 0.4214 0.2612 0.2777 0.0399  -0.0332 0.0522  463 PRO A O   
1684 C CB  . PRO A 452 ? 0.4835 0.2813 0.3390 0.0274  -0.0225 0.0359  463 PRO A CB  
1685 C CG  . PRO A 452 ? 0.4557 0.2753 0.3240 0.0174  -0.0233 0.0246  463 PRO A CG  
1686 C CD  . PRO A 452 ? 0.4034 0.2546 0.2846 0.0223  -0.0282 0.0247  463 PRO A CD  
1687 N N   . TYR A 453 ? 0.4261 0.2312 0.2742 0.0623  -0.0321 0.0610  464 TYR A N   
1688 C CA  . TYR A 453 ? 0.5261 0.3280 0.3615 0.0702  -0.0352 0.0756  464 TYR A CA  
1689 C C   . TYR A 453 ? 0.4257 0.2665 0.2699 0.0760  -0.0442 0.0773  464 TYR A C   
1690 O O   . TYR A 453 ? 0.4518 0.2974 0.2842 0.0789  -0.0480 0.0881  464 TYR A O   
1691 C CB  . TYR A 453 ? 0.4816 0.2663 0.2997 0.0557  -0.0304 0.0814  464 TYR A CB  
1692 C CG  . TYR A 453 ? 0.5458 0.3001 0.3582 0.0420  -0.0212 0.0754  464 TYR A CG  
1693 C CD1 . TYR A 453 ? 0.6212 0.3399 0.4268 0.0483  -0.0157 0.0759  464 TYR A CD1 
1694 C CD2 . TYR A 453 ? 0.5196 0.2825 0.3340 0.0221  -0.0175 0.0683  464 TYR A CD2 
1695 C CE1 . TYR A 453 ? 0.5998 0.2919 0.3994 0.0325  -0.0073 0.0681  464 TYR A CE1 
1696 C CE2 . TYR A 453 ? 0.5318 0.2733 0.3429 0.0075  -0.0101 0.0617  464 TYR A CE2 
1697 C CZ  . TYR A 453 ? 0.5653 0.2714 0.3683 0.0114  -0.0053 0.0610  464 TYR A CZ  
1698 O OH  . TYR A 453 ? 0.5956 0.2817 0.3945 -0.0063 0.0021  0.0523  464 TYR A OH  
1699 N N   . LEU A 454 ? 0.4259 0.2943 0.2890 0.0767  -0.0474 0.0670  465 LEU A N   
1700 C CA  . LEU A 454 ? 0.4278 0.3326 0.2991 0.0783  -0.0549 0.0662  465 LEU A CA  
1701 C C   . LEU A 454 ? 0.4749 0.3900 0.3426 0.0948  -0.0621 0.0784  465 LEU A C   
1702 O O   . LEU A 454 ? 0.5001 0.4412 0.3654 0.0935  -0.0691 0.0812  465 LEU A O   
1703 C CB  . LEU A 454 ? 0.4089 0.3364 0.3009 0.0766  -0.0553 0.0539  465 LEU A CB  
1704 C CG  . LEU A 454 ? 0.4058 0.3673 0.3055 0.0710  -0.0605 0.0492  465 LEU A CG  
1705 C CD1 . LEU A 454 ? 0.4714 0.4334 0.3607 0.0568  -0.0588 0.0470  465 LEU A CD1 
1706 C CD2 . LEU A 454 ? 0.4175 0.3962 0.3361 0.0686  -0.0590 0.0383  465 LEU A CD2 
1707 N N   . ASN A 455 ? 0.5158 0.4120 0.3826 0.1109  -0.0606 0.0857  466 ASN A N   
1708 C CA  . ASN A 455 ? 0.4699 0.3840 0.3427 0.1229  -0.0656 0.0955  466 ASN A CA  
1709 C C   . ASN A 455 ? 0.5229 0.4245 0.3765 0.1209  -0.0666 0.1090  466 ASN A C   
1710 O O   . ASN A 455 ? 0.5608 0.4808 0.4164 0.1292  -0.0731 0.1181  466 ASN A O   
1711 C CB  . ASN A 455 ? 0.5511 0.4514 0.4348 0.1375  -0.0606 0.0965  466 ASN A CB  
1712 C CG  . ASN A 455 ? 0.6134 0.4654 0.4823 0.1360  -0.0505 0.0986  466 ASN A CG  
1713 O OD1 . ASN A 455 ? 0.6743 0.5059 0.5363 0.1249  -0.0452 0.0903  466 ASN A OD1 
1714 N ND2 . ASN A 455 ? 0.5900 0.4235 0.4536 0.1461  -0.0480 0.1096  466 ASN A ND2 
1715 N N   . GLU A 456 ? 0.5496 0.4233 0.3844 0.1089  -0.0606 0.1103  467 GLU A N   
1716 C CA  . GLU A 456 ? 0.5073 0.3669 0.3220 0.1047  -0.0594 0.1231  467 GLU A CA  
1717 C C   . GLU A 456 ? 0.5724 0.4594 0.3777 0.0937  -0.0651 0.1219  467 GLU A C   
1718 O O   . GLU A 456 ? 0.5052 0.4119 0.3169 0.0867  -0.0676 0.1097  467 GLU A O   
1719 C CB  . GLU A 456 ? 0.5743 0.3895 0.3736 0.0949  -0.0480 0.1239  467 GLU A CB  
1720 C CG  . GLU A 456 ? 0.6357 0.4204 0.4416 0.1017  -0.0406 0.1206  467 GLU A CG  
1721 C CD  . GLU A 456 ? 0.6905 0.4630 0.4970 0.1172  -0.0398 0.1325  467 GLU A CD  
1722 O OE1 . GLU A 456 ? 0.6900 0.4756 0.4904 0.1222  -0.0456 0.1452  467 GLU A OE1 
1723 O OE2 . GLU A 456 ? 0.7639 0.5126 0.5756 0.1243  -0.0333 0.1288  467 GLU A OE2 
1724 N N   . ASN A 457 ? 0.5802 0.4674 0.3691 0.0921  -0.0669 0.1343  468 ASN A N   
1725 C CA  . ASN A 457 ? 0.7132 0.6220 0.4883 0.0798  -0.0701 0.1325  468 ASN A CA  
1726 C C   . ASN A 457 ? 0.5830 0.4721 0.3457 0.0641  -0.0606 0.1250  468 ASN A C   
1727 O O   . ASN A 457 ? 0.6385 0.4926 0.3973 0.0606  -0.0515 0.1264  468 ASN A O   
1728 C CB  . ASN A 457 ? 0.7202 0.6312 0.4773 0.0809  -0.0738 0.1481  468 ASN A CB  
1729 C CG  . ASN A 457 ? 0.8626 0.7361 0.6002 0.0751  -0.0629 0.1595  468 ASN A CG  
1730 O OD1 . ASN A 457 ? 0.8549 0.7193 0.5793 0.0604  -0.0548 0.1555  468 ASN A OD1 
1731 N ND2 . ASN A 457 ? 0.8725 0.7246 0.6077 0.0862  -0.0622 0.1736  468 ASN A ND2 
1732 N N   . PRO A 458 ? 0.6506 0.5637 0.4114 0.0515  -0.0614 0.1143  469 PRO A N   
1733 C CA  . PRO A 458 ? 0.5245 0.4289 0.2883 0.0335  -0.0505 0.1030  469 PRO A CA  
1734 C C   . PRO A 458 ? 0.5129 0.3871 0.2555 0.0255  -0.0411 0.1138  469 PRO A C   
1735 O O   . PRO A 458 ? 0.5905 0.4489 0.3402 0.0145  -0.0317 0.1071  469 PRO A O   
1736 C CB  . PRO A 458 ? 0.6376 0.5746 0.4022 0.0237  -0.0525 0.0914  469 PRO A CB  
1737 C CG  . PRO A 458 ? 0.6948 0.6591 0.4693 0.0343  -0.0643 0.0894  469 PRO A CG  
1738 C CD  . PRO A 458 ? 0.6330 0.5863 0.3971 0.0516  -0.0710 0.1081  469 PRO A CD  
1739 N N   . LEU A 459 ? 0.5403 0.4077 0.2568 0.0299  -0.0430 0.1306  470 LEU A N   
1740 C CA  . LEU A 459 ? 0.6132 0.4514 0.3118 0.0208  -0.0319 0.1411  470 LEU A CA  
1741 C C   . LEU A 459 ? 0.5671 0.3689 0.2723 0.0259  -0.0265 0.1464  470 LEU A C   
1742 O O   . LEU A 459 ? 0.6377 0.4129 0.3377 0.0123  -0.0154 0.1449  470 LEU A O   
1743 C CB  . LEU A 459 ? 0.7182 0.5673 0.3996 0.0237  -0.0338 0.1560  470 LEU A CB  
1744 C CG  . LEU A 459 ? 0.8479 0.7186 0.5136 0.0100  -0.0302 0.1507  470 LEU A CG  
1745 C CD1 . LEU A 459 ? 0.8482 0.6945 0.5067 -0.0078 -0.0148 0.1486  470 LEU A CD1 
1746 C CD2 . LEU A 459 ? 0.7302 0.6312 0.4048 0.0061  -0.0366 0.1325  470 LEU A CD2 
1747 N N   . ARG A 460 ? 0.7083 0.5100 0.4260 0.0439  -0.0335 0.1509  471 ARG A N   
1748 C CA  . ARG A 460 ? 0.6306 0.3971 0.3548 0.0491  -0.0275 0.1526  471 ARG A CA  
1749 C C   . ARG A 460 ? 0.6445 0.3988 0.3782 0.0397  -0.0228 0.1370  471 ARG A C   
1750 O O   . ARG A 460 ? 0.6400 0.3614 0.3707 0.0309  -0.0132 0.1352  471 ARG A O   
1751 C CB  . ARG A 460 ? 0.7022 0.4763 0.4401 0.0704  -0.0358 0.1583  471 ARG A CB  
1752 C CG  . ARG A 460 ? 0.7998 0.5386 0.5446 0.0775  -0.0290 0.1575  471 ARG A CG  
1753 C CD  . ARG A 460 ? 0.8872 0.5867 0.6151 0.0718  -0.0186 0.1687  471 ARG A CD  
1754 N NE  . ARG A 460 ? 1.1425 0.8074 0.8760 0.0779  -0.0115 0.1656  471 ARG A NE  
1755 C CZ  . ARG A 460 ? 1.0756 0.6999 0.7970 0.0723  -0.0007 0.1713  471 ARG A CZ  
1756 N NH1 . ARG A 460 ? 1.0645 0.6771 0.7681 0.0602  0.0048  0.1814  471 ARG A NH1 
1757 N NH2 . ARG A 460 ? 1.0290 0.6239 0.7558 0.0782  0.0055  0.1658  471 ARG A NH2 
1758 N N   . ALA A 461 ? 0.5848 0.3694 0.3336 0.0395  -0.0295 0.1241  472 ALA A N   
1759 C CA  . ALA A 461 ? 0.5663 0.3541 0.3356 0.0288  -0.0253 0.1067  472 ALA A CA  
1760 C C   . ALA A 461 ? 0.5961 0.3784 0.3615 0.0073  -0.0155 0.1018  472 ALA A C   
1761 O O   . ALA A 461 ? 0.5627 0.3302 0.3353 -0.0026 -0.0093 0.0939  472 ALA A O   
1762 C CB  . ALA A 461 ? 0.5180 0.3446 0.3091 0.0318  -0.0327 0.0938  472 ALA A CB  
1763 N N   . LEU A 462 ? 0.5776 0.3741 0.3314 -0.0008 -0.0137 0.1057  473 LEU A N   
1764 C CA  . LEU A 462 ? 0.5043 0.2975 0.2545 -0.0208 -0.0030 0.1022  473 LEU A CA  
1765 C C   . LEU A 462 ? 0.6143 0.3658 0.3492 -0.0283 0.0062  0.1113  473 LEU A C   
1766 O O   . LEU A 462 ? 0.5784 0.3231 0.3210 -0.0445 0.0143  0.1030  473 LEU A O   
1767 C CB  . LEU A 462 ? 0.5914 0.4038 0.3273 -0.0266 -0.0013 0.1065  473 LEU A CB  
1768 C CG  . LEU A 462 ? 0.5576 0.4092 0.3070 -0.0260 -0.0059 0.0939  473 LEU A CG  
1769 C CD1 . LEU A 462 ? 0.5642 0.4284 0.2928 -0.0326 -0.0024 0.0988  473 LEU A CD1 
1770 C CD2 . LEU A 462 ? 0.4964 0.3635 0.2715 -0.0350 -0.0015 0.0774  473 LEU A CD2 
1771 N N   . TYR A 463 ? 0.6578 0.3811 0.3706 -0.0169 0.0055  0.1286  474 TYR A N   
1772 C CA  . TYR A 463 ? 0.6614 0.3431 0.3630 -0.0225 0.0154  0.1361  474 TYR A CA  
1773 C C   . TYR A 463 ? 0.6772 0.3367 0.3905 -0.0242 0.0177  0.1252  474 TYR A C   
1774 O O   . TYR A 463 ? 0.6999 0.3373 0.4120 -0.0416 0.0279  0.1201  474 TYR A O   
1775 C CB  . TYR A 463 ? 0.7202 0.3917 0.4134 -0.0047 0.0126  0.1525  474 TYR A CB  
1776 C CG  . TYR A 463 ? 0.7457 0.3758 0.4334 -0.0077 0.0225  0.1579  474 TYR A CG  
1777 C CD1 . TYR A 463 ? 0.7646 0.3771 0.4382 -0.0235 0.0337  0.1649  474 TYR A CD1 
1778 C CD2 . TYR A 463 ? 0.8256 0.4341 0.5222 0.0047  0.0217  0.1546  474 TYR A CD2 
1779 C CE1 . TYR A 463 ? 0.8584 0.4311 0.5265 -0.0273 0.0432  0.1688  474 TYR A CE1 
1780 C CE2 . TYR A 463 ? 0.9130 0.4815 0.6035 0.0015  0.0316  0.1577  474 TYR A CE2 
1781 C CZ  . TYR A 463 ? 0.9157 0.4654 0.5916 -0.0148 0.0421  0.1648  474 TYR A CZ  
1782 O OH  . TYR A 463 ? 1.0074 0.5156 0.6766 -0.0187 0.0523  0.1671  474 TYR A OH  
1783 N N   . LEU A 464 ? 0.6419 0.3108 0.3684 -0.0073 0.0086  0.1200  475 LEU A N   
1784 C CA  . LEU A 464 ? 0.6565 0.3086 0.3949 -0.0077 0.0107  0.1080  475 LEU A CA  
1785 C C   . LEU A 464 ? 0.6623 0.3359 0.4186 -0.0281 0.0132  0.0899  475 LEU A C   
1786 O O   . LEU A 464 ? 0.6164 0.2689 0.3738 -0.0398 0.0195  0.0812  475 LEU A O   
1787 C CB  . LEU A 464 ? 0.6500 0.3154 0.4011 0.0151  0.0009  0.1058  475 LEU A CB  
1788 C CG  . LEU A 464 ? 0.7184 0.3741 0.4657 0.0361  -0.0011 0.1194  475 LEU A CG  
1789 C CD1 . LEU A 464 ? 0.6307 0.3128 0.3945 0.0572  -0.0112 0.1175  475 LEU A CD1 
1790 C CD2 . LEU A 464 ? 0.7191 0.3336 0.4614 0.0348  0.0092  0.1197  475 LEU A CD2 
1791 N N   . ILE A 465 ? 0.5717 0.2877 0.3419 -0.0322 0.0086  0.0837  476 ILE A N   
1792 C CA  . ILE A 465 ? 0.5875 0.3275 0.3760 -0.0487 0.0107  0.0687  476 ILE A CA  
1793 C C   . ILE A 465 ? 0.6111 0.3361 0.3910 -0.0714 0.0219  0.0692  476 ILE A C   
1794 O O   . ILE A 465 ? 0.6233 0.3471 0.4121 -0.0862 0.0256  0.0581  476 ILE A O   
1795 C CB  . ILE A 465 ? 0.5293 0.3135 0.3331 -0.0460 0.0052  0.0636  476 ILE A CB  
1796 C CG1 . ILE A 465 ? 0.5138 0.3128 0.3290 -0.0277 -0.0046 0.0603  476 ILE A CG1 
1797 C CG2 . ILE A 465 ? 0.5200 0.3298 0.3421 -0.0613 0.0084  0.0512  476 ILE A CG2 
1798 C CD1 . ILE A 465 ? 0.4634 0.2971 0.2880 -0.0241 -0.0089 0.0572  476 ILE A CD1 
1799 N N   . ALA A 466 ? 0.6031 0.3185 0.3649 -0.0756 0.0276  0.0819  477 ALA A N   
1800 C CA  . ALA A 466 ? 0.5860 0.2887 0.3394 -0.0989 0.0399  0.0831  477 ALA A CA  
1801 C C   . ALA A 466 ? 0.7387 0.3941 0.4799 -0.1079 0.0475  0.0836  477 ALA A C   
1802 O O   . ALA A 466 ? 0.7433 0.3949 0.4879 -0.1312 0.0562  0.0758  477 ALA A O   
1803 C CB  . ALA A 466 ? 0.6616 0.3601 0.3936 -0.1003 0.0453  0.0985  477 ALA A CB  
1804 N N   . THR A 467 ? 0.6831 0.3033 0.4110 -0.0901 0.0450  0.0917  478 THR A N   
1805 C CA  . THR A 467 ? 0.6955 0.2764 0.4167 -0.0931 0.0527  0.0906  478 THR A CA  
1806 C C   . THR A 467 ? 0.8126 0.3839 0.5438 -0.0930 0.0505  0.0751  478 THR A C   
1807 O O   . THR A 467 ? 0.8688 0.4186 0.5989 -0.1066 0.0583  0.0664  478 THR A O   
1808 C CB  . THR A 467 ? 0.7812 0.3393 0.4895 -0.0709 0.0522  0.1075  478 THR A CB  
1809 O OG1 . THR A 467 ? 0.9401 0.5117 0.6536 -0.0455 0.0406  0.1111  478 THR A OG1 
1810 C CG2 . THR A 467 ? 0.8146 0.3801 0.5107 -0.0743 0.0555  0.1221  478 THR A CG2 
1811 N N   . ASN A 468 ? 0.7128 0.3028 0.4544 -0.0780 0.0401  0.0702  479 ASN A N   
1812 C CA  . ASN A 468 ? 0.7769 0.3655 0.5294 -0.0776 0.0377  0.0541  479 ASN A CA  
1813 C C   . ASN A 468 ? 0.7521 0.3800 0.5247 -0.0971 0.0351  0.0368  479 ASN A C   
1814 O O   . ASN A 468 ? 0.7924 0.4116 0.5673 -0.1079 0.0369  0.0228  479 ASN A O   
1815 C CB  . ASN A 468 ? 0.7063 0.3096 0.4677 -0.0503 0.0274  0.0552  479 ASN A CB  
1816 C CG  . ASN A 468 ? 0.7655 0.3349 0.5129 -0.0285 0.0293  0.0689  479 ASN A CG  
1817 O OD1 . ASN A 468 ? 0.8096 0.3533 0.5472 -0.0317 0.0376  0.0754  479 ASN A OD1 
1818 N ND2 . ASN A 468 ? 0.7917 0.3763 0.5468 -0.0049 0.0208  0.0722  479 ASN A ND2 
1819 N N   . GLY A 469 ? 0.7052 0.3774 0.4923 -0.1005 0.0306  0.0373  480 GLY A N   
1820 C CA  . GLY A 469 ? 0.6593 0.3740 0.4682 -0.1135 0.0267  0.0230  480 GLY A CA  
1821 C C   . GLY A 469 ? 0.5943 0.3312 0.4175 -0.0984 0.0165  0.0146  480 GLY A C   
1822 O O   . GLY A 469 ? 0.6694 0.4167 0.4961 -0.0782 0.0102  0.0205  480 GLY A O   
1823 N N   . THR A 470 ? 0.6307 0.3749 0.4608 -0.1091 0.0151  0.0006  481 THR A N   
1824 C CA  . THR A 470 ? 0.5831 0.3482 0.4242 -0.0959 0.0062  -0.0067 481 THR A CA  
1825 C C   . THR A 470 ? 0.6199 0.3540 0.4494 -0.0753 0.0059  -0.0017 481 THR A C   
1826 O O   . THR A 470 ? 0.6152 0.3072 0.4283 -0.0776 0.0127  -0.0028 481 THR A O   
1827 C CB  . THR A 470 ? 0.6765 0.4512 0.5216 -0.1121 0.0050  -0.0224 481 THR A CB  
1828 O OG1 . THR A 470 ? 0.6277 0.4387 0.4873 -0.1298 0.0044  -0.0264 481 THR A OG1 
1829 C CG2 . THR A 470 ? 0.4999 0.2947 0.3529 -0.0982 -0.0034 -0.0286 481 THR A CG2 
1830 N N   . PRO A 471 ? 0.5659 0.3192 0.4042 -0.0555 -0.0009 0.0030  482 PRO A N   
1831 C CA  . PRO A 471 ? 0.5573 0.2876 0.3879 -0.0355 -0.0012 0.0081  482 PRO A CA  
1832 C C   . PRO A 471 ? 0.5666 0.2857 0.3951 -0.0330 -0.0006 -0.0035 482 PRO A C   
1833 O O   . PRO A 471 ? 0.5741 0.3130 0.4092 -0.0435 -0.0031 -0.0149 482 PRO A O   
1834 C CB  . PRO A 471 ? 0.5161 0.2789 0.3599 -0.0202 -0.0087 0.0141  482 PRO A CB  
1835 C CG  . PRO A 471 ? 0.4833 0.2830 0.3427 -0.0296 -0.0126 0.0066  482 PRO A CG  
1836 C CD  . PRO A 471 ? 0.5313 0.3285 0.3879 -0.0509 -0.0079 0.0028  482 PRO A CD  
1837 N N   . GLU A 472 ? 0.5686 0.2556 0.3866 -0.0183 0.0034  -0.0001 483 GLU A N   
1838 C CA  . GLU A 472 ? 0.6005 0.2730 0.4145 -0.0120 0.0060  -0.0107 483 GLU A CA  
1839 C C   . GLU A 472 ? 0.7119 0.4134 0.5394 0.0063  -0.0002 -0.0101 483 GLU A C   
1840 O O   . GLU A 472 ? 0.6173 0.3326 0.4524 0.0205  -0.0043 0.0010  483 GLU A O   
1841 C CB  . GLU A 472 ? 0.6379 0.2589 0.4345 -0.0034 0.0155  -0.0072 483 GLU A CB  
1842 C CG  . GLU A 472 ? 0.9463 0.5300 0.7267 -0.0215 0.0242  -0.0062 483 GLU A CG  
1843 C CD  . GLU A 472 ? 1.1058 0.6778 0.8791 -0.0449 0.0292  -0.0248 483 GLU A CD  
1844 O OE1 . GLU A 472 ? 1.2148 0.7999 0.9915 -0.0433 0.0269  -0.0378 483 GLU A OE1 
1845 O OE2 . GLU A 472 ? 1.2245 0.7781 0.9895 -0.0654 0.0355  -0.0264 483 GLU A OE2 
1846 N N   . LEU A 473 ? 0.6271 0.3405 0.4570 0.0039  -0.0011 -0.0223 484 LEU A N   
1847 C CA  . LEU A 473 ? 0.6025 0.3353 0.4417 0.0205  -0.0037 -0.0228 484 LEU A CA  
1848 C C   . LEU A 473 ? 0.6586 0.3609 0.4900 0.0371  0.0036  -0.0231 484 LEU A C   
1849 O O   . LEU A 473 ? 0.6166 0.2800 0.4325 0.0330  0.0117  -0.0283 484 LEU A O   
1850 C CB  . LEU A 473 ? 0.5521 0.3092 0.3944 0.0127  -0.0066 -0.0342 484 LEU A CB  
1851 C CG  . LEU A 473 ? 0.6672 0.4630 0.5222 0.0042  -0.0145 -0.0321 484 LEU A CG  
1852 C CD1 . LEU A 473 ? 0.6089 0.4247 0.4779 0.0168  -0.0184 -0.0207 484 LEU A CD1 
1853 C CD2 . LEU A 473 ? 0.7811 0.5782 0.6346 -0.0146 -0.0156 -0.0334 484 LEU A CD2 
1854 N N   . GLN A 474 ? 0.6274 0.3474 0.4703 0.0559  0.0015  -0.0174 485 GLN A N   
1855 C CA  . GLN A 474 ? 0.6483 0.3466 0.4880 0.0749  0.0086  -0.0173 485 GLN A CA  
1856 C C   . GLN A 474 ? 0.6907 0.3763 0.5214 0.0721  0.0159  -0.0333 485 GLN A C   
1857 O O   . GLN A 474 ? 0.6767 0.3254 0.4954 0.0793  0.0256  -0.0381 485 GLN A O   
1858 C CB  . GLN A 474 ? 0.7763 0.5055 0.6339 0.0937  0.0041  -0.0086 485 GLN A CB  
1859 C CG  . GLN A 474 ? 1.0164 0.7600 0.8808 0.0968  -0.0035 0.0061  485 GLN A CG  
1860 C CD  . GLN A 474 ? 1.1792 0.9537 1.0608 0.1143  -0.0080 0.0133  485 GLN A CD  
1861 O OE1 . GLN A 474 ? 1.3802 1.1481 1.2650 0.1329  -0.0039 0.0155  485 GLN A OE1 
1862 N NE2 . GLN A 474 ? 0.9593 0.7685 0.8527 0.1083  -0.0157 0.0162  485 GLN A NE2 
1863 N N   . ASN A 475 ? 0.6891 0.4031 0.5235 0.0622  0.0122  -0.0416 486 ASN A N   
1864 C CA  . ASN A 475 ? 0.7408 0.4485 0.5646 0.0589  0.0184  -0.0570 486 ASN A CA  
1865 C C   . ASN A 475 ? 0.6079 0.3350 0.4268 0.0377  0.0126  -0.0652 486 ASN A C   
1866 O O   . ASN A 475 ? 0.6069 0.3656 0.4316 0.0374  0.0084  -0.0664 486 ASN A O   
1867 C CB  . ASN A 475 ? 0.7656 0.4952 0.5999 0.0760  0.0208  -0.0570 486 ASN A CB  
1868 C CG  . ASN A 475 ? 0.7470 0.4619 0.5877 0.0988  0.0270  -0.0504 486 ASN A CG  
1869 O OD1 . ASN A 475 ? 0.8462 0.5814 0.7033 0.1100  0.0216  -0.0375 486 ASN A OD1 
1870 N ND2 . ASN A 475 ? 0.7371 0.4185 0.5655 0.1061  0.0384  -0.0595 486 ASN A ND2 
1871 N N   . PRO A 476 ? 0.5830 0.2927 0.3912 0.0195  0.0124  -0.0703 487 PRO A N   
1872 C CA  . PRO A 476 ? 0.6323 0.3674 0.4390 -0.0002 0.0053  -0.0770 487 PRO A CA  
1873 C C   . PRO A 476 ? 0.7029 0.4458 0.4977 -0.0047 0.0070  -0.0912 487 PRO A C   
1874 O O   . PRO A 476 ? 0.5817 0.3580 0.3787 -0.0135 -0.0008 -0.0926 487 PRO A O   
1875 C CB  . PRO A 476 ? 0.5960 0.3069 0.3936 -0.0188 0.0073  -0.0809 487 PRO A CB  
1876 C CG  . PRO A 476 ? 0.6636 0.3252 0.4489 -0.0103 0.0188  -0.0824 487 PRO A CG  
1877 C CD  . PRO A 476 ? 0.6868 0.3533 0.4838 0.0158  0.0193  -0.0700 487 PRO A CD  
1878 N N   . GLU A 477 ? 0.5405 0.2543 0.3222 0.0030  0.0175  -0.1009 488 GLU A N   
1879 C CA  . GLU A 477 ? 0.6720 0.3908 0.4388 -0.0015 0.0208  -0.1159 488 GLU A CA  
1880 C C   . GLU A 477 ? 0.6016 0.3594 0.3779 0.0088  0.0162  -0.1094 488 GLU A C   
1881 O O   . GLU A 477 ? 0.7006 0.4737 0.4645 0.0021  0.0156  -0.1187 488 GLU A O   
1882 C CB  . GLU A 477 ? 0.7091 0.3850 0.4605 0.0069  0.0355  -0.1277 488 GLU A CB  
1883 C CG  . GLU A 477 ? 0.7639 0.4357 0.5273 0.0339  0.0422  -0.1187 488 GLU A CG  
1884 C CD  . GLU A 477 ? 0.7978 0.4543 0.5749 0.0460  0.0416  -0.1029 488 GLU A CD  
1885 O OE1 . GLU A 477 ? 0.7555 0.3974 0.5297 0.0331  0.0382  -0.0996 488 GLU A OE1 
1886 O OE2 . GLU A 477 ? 0.8036 0.4641 0.5937 0.0680  0.0448  -0.0939 488 GLU A OE2 
1887 N N   . LYS A 478 ? 0.5051 0.2794 0.3016 0.0235  0.0132  -0.0937 489 LYS A N   
1888 C CA  . LYS A 478 ? 0.5319 0.3405 0.3378 0.0311  0.0101  -0.0870 489 LYS A CA  
1889 C C   . LYS A 478 ? 0.5616 0.4022 0.3719 0.0201  -0.0011 -0.0810 489 LYS A C   
1890 O O   . LYS A 478 ? 0.5504 0.4163 0.3655 0.0250  -0.0031 -0.0749 489 LYS A O   
1891 C CB  . LYS A 478 ? 0.5603 0.3763 0.3865 0.0484  0.0112  -0.0739 489 LYS A CB  
1892 C CG  . LYS A 478 ? 0.6623 0.4551 0.4895 0.0645  0.0213  -0.0762 489 LYS A CG  
1893 C CD  . LYS A 478 ? 0.6494 0.4652 0.4988 0.0794  0.0200  -0.0637 489 LYS A CD  
1894 C CE  . LYS A 478 ? 0.8077 0.6118 0.6633 0.0987  0.0292  -0.0641 489 LYS A CE  
1895 N NZ  . LYS A 478 ? 0.7566 0.5936 0.6346 0.1093  0.0272  -0.0541 489 LYS A NZ  
1896 N N   . LEU A 479 ? 0.5493 0.3896 0.3589 0.0059  -0.0074 -0.0820 490 LEU A N   
1897 C CA  . LEU A 479 ? 0.4982 0.3705 0.3155 -0.0021 -0.0178 -0.0753 490 LEU A CA  
1898 C C   . LEU A 479 ? 0.5273 0.4134 0.3285 -0.0167 -0.0222 -0.0862 490 LEU A C   
1899 O O   . LEU A 479 ? 0.5360 0.4024 0.3211 -0.0282 -0.0186 -0.1007 490 LEU A O   
1900 C CB  . LEU A 479 ? 0.4642 0.3343 0.2936 -0.0084 -0.0220 -0.0691 490 LEU A CB  
1901 C CG  . LEU A 479 ? 0.5102 0.3742 0.3552 0.0037  -0.0205 -0.0569 490 LEU A CG  
1902 C CD1 . LEU A 479 ? 0.5201 0.3975 0.3768 -0.0039 -0.0265 -0.0499 490 LEU A CD1 
1903 C CD2 . LEU A 479 ? 0.6382 0.5176 0.4928 0.0184  -0.0196 -0.0490 490 LEU A CD2 
1904 N N   . SER A 480 ? 0.4633 0.3832 0.2680 -0.0165 -0.0300 -0.0790 491 SER A N   
1905 C CA  . SER A 480 ? 0.4458 0.3860 0.2363 -0.0304 -0.0368 -0.0876 491 SER A CA  
1906 C C   . SER A 480 ? 0.4967 0.4394 0.2915 -0.0476 -0.0421 -0.0934 491 SER A C   
1907 O O   . SER A 480 ? 0.5087 0.4469 0.3201 -0.0469 -0.0425 -0.0860 491 SER A O   
1908 C CB  . SER A 480 ? 0.4268 0.4038 0.2218 -0.0243 -0.0448 -0.0752 491 SER A CB  
1909 O OG  . SER A 480 ? 0.4387 0.4320 0.2554 -0.0215 -0.0508 -0.0625 491 SER A OG  
1910 N N   . ALA A 481 ? 0.4810 0.4342 0.2600 -0.0644 -0.0462 -0.1071 492 ALA A N   
1911 C CA  . ALA A 481 ? 0.4968 0.4579 0.2804 -0.0841 -0.0513 -0.1141 492 ALA A CA  
1912 C C   . ALA A 481 ? 0.4953 0.4919 0.3032 -0.0807 -0.0604 -0.0990 492 ALA A C   
1913 O O   . ALA A 481 ? 0.4330 0.4257 0.2544 -0.0882 -0.0598 -0.0974 492 ALA A O   
1914 C CB  . ALA A 481 ? 0.5137 0.4896 0.2791 -0.1026 -0.0558 -0.1307 492 ALA A CB  
1915 N N   . ILE A 482 ? 0.4557 0.4853 0.2690 -0.0686 -0.0676 -0.0870 493 ILE A N   
1916 C CA  . ILE A 482 ? 0.4099 0.4734 0.2462 -0.0640 -0.0754 -0.0733 493 ILE A CA  
1917 C C   . ILE A 482 ? 0.3940 0.4389 0.2483 -0.0515 -0.0691 -0.0617 493 ILE A C   
1918 O O   . ILE A 482 ? 0.4063 0.4652 0.2789 -0.0537 -0.0714 -0.0561 493 ILE A O   
1919 C CB  . ILE A 482 ? 0.4551 0.5549 0.2906 -0.0526 -0.0839 -0.0622 493 ILE A CB  
1920 C CG1 . ILE A 482 ? 0.5287 0.6097 0.3558 -0.0351 -0.0771 -0.0540 493 ILE A CG1 
1921 C CG2 . ILE A 482 ? 0.5547 0.6815 0.3748 -0.0664 -0.0925 -0.0728 493 ILE A CG2 
1922 C CD1 . ILE A 482 ? 0.6125 0.7224 0.4398 -0.0217 -0.0831 -0.0389 493 ILE A CD1 
1923 N N   . PHE A 483 ? 0.3853 0.4018 0.2350 -0.0387 -0.0611 -0.0582 494 PHE A N   
1924 C CA  . PHE A 483 ? 0.4092 0.4095 0.2741 -0.0287 -0.0559 -0.0488 494 PHE A CA  
1925 C C   . PHE A 483 ? 0.4350 0.4130 0.3016 -0.0400 -0.0519 -0.0549 494 PHE A C   
1926 O O   . PHE A 483 ? 0.3554 0.3371 0.2367 -0.0396 -0.0517 -0.0480 494 PHE A O   
1927 C CB  . PHE A 483 ? 0.4187 0.3984 0.2789 -0.0142 -0.0488 -0.0451 494 PHE A CB  
1928 C CG  . PHE A 483 ? 0.4853 0.4558 0.3610 -0.0034 -0.0450 -0.0349 494 PHE A CG  
1929 C CD1 . PHE A 483 ? 0.4152 0.3977 0.3066 -0.0043 -0.0477 -0.0280 494 PHE A CD1 
1930 C CD2 . PHE A 483 ? 0.4385 0.3913 0.3129 0.0071  -0.0385 -0.0331 494 PHE A CD2 
1931 C CE1 . PHE A 483 ? 0.4046 0.3792 0.3074 0.0042  -0.0442 -0.0204 494 PHE A CE1 
1932 C CE2 . PHE A 483 ? 0.3855 0.3336 0.2731 0.0152  -0.0361 -0.0252 494 PHE A CE2 
1933 C CZ  . PHE A 483 ? 0.3581 0.3160 0.2585 0.0131  -0.0391 -0.0192 494 PHE A CZ  
1934 N N   . ARG A 484 ? 0.4332 0.3861 0.2833 -0.0504 -0.0475 -0.0679 495 ARG A N   
1935 C CA  . ARG A 484 ? 0.4447 0.3719 0.2939 -0.0618 -0.0424 -0.0725 495 ARG A CA  
1936 C C   . ARG A 484 ? 0.4276 0.3811 0.2884 -0.0774 -0.0477 -0.0730 495 ARG A C   
1937 O O   . ARG A 484 ? 0.3962 0.3403 0.2651 -0.0819 -0.0443 -0.0689 495 ARG A O   
1938 C CB  . ARG A 484 ? 0.4797 0.3732 0.3075 -0.0717 -0.0358 -0.0877 495 ARG A CB  
1939 C CG  . ARG A 484 ? 0.5909 0.4527 0.4095 -0.0555 -0.0275 -0.0875 495 ARG A CG  
1940 C CD  . ARG A 484 ? 0.5610 0.3805 0.3599 -0.0648 -0.0181 -0.1020 495 ARG A CD  
1941 N NE  . ARG A 484 ? 0.7550 0.5819 0.5378 -0.0820 -0.0199 -0.1187 495 ARG A NE  
1942 C CZ  . ARG A 484 ? 0.7981 0.6293 0.5669 -0.0781 -0.0189 -0.1271 495 ARG A CZ  
1943 N NH1 . ARG A 484 ? 0.7887 0.6177 0.5591 -0.0576 -0.0153 -0.1203 495 ARG A NH1 
1944 N NH2 . ARG A 484 ? 0.8160 0.6560 0.5684 -0.0966 -0.0214 -0.1434 495 ARG A NH2 
1945 N N   . ASP A 485 ? 0.4143 0.4032 0.2758 -0.0860 -0.0560 -0.0778 496 ASP A N   
1946 C CA  . ASP A 485 ? 0.4506 0.4718 0.3264 -0.1006 -0.0614 -0.0788 496 ASP A CA  
1947 C C   . ASP A 485 ? 0.4636 0.5059 0.3620 -0.0875 -0.0629 -0.0636 496 ASP A C   
1948 O O   . ASP A 485 ? 0.3982 0.4466 0.3090 -0.0962 -0.0607 -0.0620 496 ASP A O   
1949 C CB  . ASP A 485 ? 0.3886 0.4493 0.2609 -0.1103 -0.0716 -0.0863 496 ASP A CB  
1950 C CG  . ASP A 485 ? 0.5517 0.6504 0.4399 -0.1280 -0.0774 -0.0897 496 ASP A CG  
1951 O OD1 . ASP A 485 ? 0.5887 0.6753 0.4697 -0.1513 -0.0740 -0.1035 496 ASP A OD1 
1952 O OD2 . ASP A 485 ? 0.5106 0.6509 0.4188 -0.1187 -0.0844 -0.0789 496 ASP A OD2 
1953 N N   . PHE A 486 ? 0.3597 0.4113 0.2626 -0.0674 -0.0651 -0.0528 497 PHE A N   
1954 C CA  . PHE A 486 ? 0.3635 0.4281 0.2854 -0.0539 -0.0645 -0.0396 497 PHE A CA  
1955 C C   . PHE A 486 ? 0.3707 0.4053 0.2946 -0.0537 -0.0561 -0.0371 497 PHE A C   
1956 O O   . PHE A 486 ? 0.3563 0.4028 0.2944 -0.0555 -0.0545 -0.0327 497 PHE A O   
1957 C CB  . PHE A 486 ? 0.3437 0.4118 0.2654 -0.0341 -0.0657 -0.0299 497 PHE A CB  
1958 C CG  . PHE A 486 ? 0.2930 0.3684 0.2319 -0.0203 -0.0633 -0.0179 497 PHE A CG  
1959 C CD1 . PHE A 486 ? 0.3270 0.4374 0.2820 -0.0149 -0.0678 -0.0111 497 PHE A CD1 
1960 C CD2 . PHE A 486 ? 0.2867 0.3353 0.2256 -0.0127 -0.0564 -0.0142 497 PHE A CD2 
1961 C CE1 . PHE A 486 ? 0.2946 0.4076 0.2640 -0.0019 -0.0637 -0.0016 497 PHE A CE1 
1962 C CE2 . PHE A 486 ? 0.3269 0.3808 0.2795 -0.0020 -0.0535 -0.0056 497 PHE A CE2 
1963 C CZ  . PHE A 486 ? 0.3120 0.3956 0.2791 0.0033  -0.0563 0.0002  497 PHE A CZ  
1964 N N   . LEU A 487 ? 0.3801 0.3776 0.2898 -0.0505 -0.0507 -0.0394 498 LEU A N   
1965 C CA  . LEU A 487 ? 0.4325 0.4024 0.3415 -0.0497 -0.0438 -0.0359 498 LEU A CA  
1966 C C   . LEU A 487 ? 0.4312 0.3961 0.3398 -0.0684 -0.0408 -0.0407 498 LEU A C   
1967 O O   . LEU A 487 ? 0.4085 0.3726 0.3244 -0.0695 -0.0372 -0.0347 498 LEU A O   
1968 C CB  . LEU A 487 ? 0.4100 0.3438 0.3043 -0.0422 -0.0390 -0.0374 498 LEU A CB  
1969 C CG  . LEU A 487 ? 0.5361 0.4679 0.4322 -0.0238 -0.0387 -0.0312 498 LEU A CG  
1970 C CD1 . LEU A 487 ? 0.5897 0.4881 0.4730 -0.0183 -0.0332 -0.0341 498 LEU A CD1 
1971 C CD2 . LEU A 487 ? 0.4930 0.4330 0.4022 -0.0157 -0.0382 -0.0212 498 LEU A CD2 
1972 N N   . ASN A 488 ? 0.3966 0.3570 0.2951 -0.0847 -0.0413 -0.0521 499 ASN A N   
1973 C CA  . ASN A 488 ? 0.4463 0.3995 0.3435 -0.1058 -0.0369 -0.0576 499 ASN A CA  
1974 C C   . ASN A 488 ? 0.4571 0.4508 0.3754 -0.1117 -0.0396 -0.0535 499 ASN A C   
1975 O O   . ASN A 488 ? 0.4353 0.4224 0.3570 -0.1214 -0.0334 -0.0511 499 ASN A O   
1976 C CB  . ASN A 488 ? 0.4442 0.3915 0.3282 -0.1246 -0.0376 -0.0730 499 ASN A CB  
1977 C CG  . ASN A 488 ? 0.6026 0.5018 0.4642 -0.1211 -0.0311 -0.0789 499 ASN A CG  
1978 O OD1 . ASN A 488 ? 0.7973 0.6634 0.6535 -0.1085 -0.0249 -0.0712 499 ASN A OD1 
1979 N ND2 . ASN A 488 ? 0.5848 0.4810 0.4330 -0.1323 -0.0323 -0.0932 499 ASN A ND2 
1980 N N   . ARG A 489 ? 0.3711 0.4071 0.3033 -0.1050 -0.0479 -0.0518 500 ARG A N   
1981 C CA  . ARG A 489 ? 0.3501 0.4284 0.3050 -0.1073 -0.0501 -0.0478 500 ARG A CA  
1982 C C   . ARG A 489 ? 0.4018 0.4765 0.3666 -0.0926 -0.0448 -0.0364 500 ARG A C   
1983 O O   . ARG A 489 ? 0.3820 0.4781 0.3616 -0.0982 -0.0416 -0.0344 500 ARG A O   
1984 C CB  . ARG A 489 ? 0.2918 0.4151 0.2579 -0.1008 -0.0606 -0.0473 500 ARG A CB  
1985 C CG  . ARG A 489 ? 0.3861 0.5213 0.3425 -0.1190 -0.0667 -0.0602 500 ARG A CG  
1986 C CD  . ARG A 489 ? 0.6029 0.7901 0.5709 -0.1133 -0.0785 -0.0583 500 ARG A CD  
1987 N NE  . ARG A 489 ? 0.8628 1.0945 0.8478 -0.1316 -0.0828 -0.0644 500 ARG A NE  
1988 C CZ  . ARG A 489 ? 0.8147 1.0553 0.7923 -0.1532 -0.0858 -0.0777 500 ARG A CZ  
1989 N NH1 . ARG A 489 ? 0.8579 1.0658 0.8103 -0.1590 -0.0850 -0.0870 500 ARG A NH1 
1990 N NH2 . ARG A 489 ? 0.8807 1.1573 0.8769 -0.1647 -0.0860 -0.0800 500 ARG A NH2 
1991 N N   . CYS A 490 ? 0.3240 0.3747 0.2811 -0.0749 -0.0435 -0.0300 501 CYS A N   
1992 C CA  . CYS A 490 ? 0.3600 0.4046 0.3233 -0.0637 -0.0383 -0.0215 501 CYS A CA  
1993 C C   . CYS A 490 ? 0.3923 0.4070 0.3448 -0.0731 -0.0306 -0.0209 501 CYS A C   
1994 O O   . CYS A 490 ? 0.3411 0.3609 0.2999 -0.0724 -0.0256 -0.0162 501 CYS A O   
1995 C CB  . CYS A 490 ? 0.3262 0.3566 0.2851 -0.0444 -0.0393 -0.0159 501 CYS A CB  
1996 S SG  . CYS A 490 ? 0.3365 0.3947 0.3059 -0.0289 -0.0455 -0.0117 501 CYS A SG  
1997 N N   . LEU A 491 ? 0.3832 0.3652 0.3180 -0.0810 -0.0288 -0.0252 502 LEU A N   
1998 C CA  . LEU A 491 ? 0.4352 0.3821 0.3562 -0.0857 -0.0214 -0.0216 502 LEU A CA  
1999 C C   . LEU A 491 ? 0.4606 0.3985 0.3760 -0.1090 -0.0160 -0.0273 502 LEU A C   
2000 O O   . LEU A 491 ? 0.4448 0.3443 0.3433 -0.1147 -0.0094 -0.0253 502 LEU A O   
2001 C CB  . LEU A 491 ? 0.3812 0.2924 0.2860 -0.0741 -0.0213 -0.0201 502 LEU A CB  
2002 C CG  . LEU A 491 ? 0.4303 0.3496 0.3409 -0.0536 -0.0250 -0.0141 502 LEU A CG  
2003 C CD1 . LEU A 491 ? 0.4960 0.3888 0.3946 -0.0426 -0.0253 -0.0143 502 LEU A CD1 
2004 C CD2 . LEU A 491 ? 0.3657 0.2886 0.2801 -0.0481 -0.0221 -0.0057 502 LEU A CD2 
2005 N N   . GLU A 492 ? 0.4079 0.3815 0.3379 -0.1225 -0.0182 -0.0335 503 GLU A N   
2006 C CA  . GLU A 492 ? 0.4073 0.3789 0.3352 -0.1481 -0.0127 -0.0403 503 GLU A CA  
2007 C C   . GLU A 492 ? 0.4637 0.4259 0.3904 -0.1551 -0.0029 -0.0328 503 GLU A C   
2008 O O   . GLU A 492 ? 0.4431 0.4287 0.3823 -0.1453 -0.0021 -0.0260 503 GLU A O   
2009 C CB  . GLU A 492 ? 0.4560 0.4786 0.4036 -0.1590 -0.0193 -0.0485 503 GLU A CB  
2010 C CG  . GLU A 492 ? 0.5767 0.6119 0.5291 -0.1877 -0.0143 -0.0566 503 GLU A CG  
2011 C CD  . GLU A 492 ? 0.7078 0.6956 0.6367 -0.2068 -0.0078 -0.0647 503 GLU A CD  
2012 O OE1 . GLU A 492 ? 0.6685 0.6421 0.5855 -0.2071 -0.0125 -0.0734 503 GLU A OE1 
2013 O OE2 . GLU A 492 ? 0.6169 0.5800 0.5381 -0.2215 0.0032  -0.0622 503 GLU A OE2 
2014 N N   . MET A 493 ? 0.4674 0.3924 0.3769 -0.1720 0.0058  -0.0339 504 MET A N   
2015 C CA  . MET A 493 ? 0.4912 0.4044 0.3955 -0.1806 0.0163  -0.0257 504 MET A CA  
2016 C C   . MET A 493 ? 0.5806 0.5402 0.5065 -0.1976 0.0194  -0.0296 504 MET A C   
2017 O O   . MET A 493 ? 0.5504 0.5234 0.4819 -0.1956 0.0253  -0.0223 504 MET A O   
2018 C CB  . MET A 493 ? 0.6355 0.4943 0.5148 -0.1952 0.0259  -0.0250 504 MET A CB  
2019 C CG  . MET A 493 ? 0.6933 0.5045 0.5513 -0.1758 0.0255  -0.0175 504 MET A CG  
2020 S SD  . MET A 493 ? 0.7503 0.5617 0.6049 -0.1533 0.0254  -0.0003 504 MET A SD  
2021 C CE  . MET A 493 ? 0.5847 0.3884 0.4311 -0.1751 0.0390  0.0068  504 MET A CE  
2022 N N   . ASP A 494 ? 0.4902 0.4768 0.4282 -0.2146 0.0157  -0.0417 505 ASP A N   
2023 C CA  . ASP A 494 ? 0.5203 0.5587 0.4828 -0.2308 0.0177  -0.0464 505 ASP A CA  
2024 C C   . ASP A 494 ? 0.4713 0.5591 0.4584 -0.2088 0.0096  -0.0429 505 ASP A C   
2025 O O   . ASP A 494 ? 0.4531 0.5620 0.4485 -0.1977 -0.0017 -0.0467 505 ASP A O   
2026 C CB  . ASP A 494 ? 0.5275 0.5814 0.4946 -0.2561 0.0146  -0.0612 505 ASP A CB  
2027 C CG  . ASP A 494 ? 0.6053 0.7121 0.5976 -0.2744 0.0178  -0.0661 505 ASP A CG  
2028 O OD1 . ASP A 494 ? 0.5689 0.7204 0.5847 -0.2650 0.0172  -0.0610 505 ASP A OD1 
2029 O OD2 . ASP A 494 ? 0.6595 0.7619 0.6475 -0.2921 0.0215  -0.0742 505 ASP A OD2 
2030 N N   . VAL A 495 ? 0.4375 0.5420 0.4347 -0.2025 0.0166  -0.0356 506 VAL A N   
2031 C CA  . VAL A 495 ? 0.4321 0.5757 0.4506 -0.1798 0.0118  -0.0319 506 VAL A CA  
2032 C C   . VAL A 495 ? 0.4137 0.6146 0.4601 -0.1830 0.0037  -0.0389 506 VAL A C   
2033 O O   . VAL A 495 ? 0.3905 0.6151 0.4494 -0.1621 -0.0052 -0.0367 506 VAL A O   
2034 C CB  . VAL A 495 ? 0.3922 0.5426 0.4149 -0.1762 0.0232  -0.0254 506 VAL A CB  
2035 C CG1 . VAL A 495 ? 0.4151 0.6051 0.4612 -0.1540 0.0206  -0.0234 506 VAL A CG1 
2036 C CG2 . VAL A 495 ? 0.4345 0.5318 0.4280 -0.1690 0.0280  -0.0172 506 VAL A CG2 
2037 N N   . GLU A 496 ? 0.3794 0.6043 0.4357 -0.2095 0.0066  -0.0469 507 GLU A N   
2038 C CA  . GLU A 496 ? 0.3435 0.6284 0.4266 -0.2144 -0.0028 -0.0540 507 GLU A CA  
2039 C C   . GLU A 496 ? 0.4497 0.7296 0.5237 -0.2076 -0.0171 -0.0582 507 GLU A C   
2040 O O   . GLU A 496 ? 0.4618 0.7867 0.5544 -0.1948 -0.0280 -0.0578 507 GLU A O   
2041 C CB  . GLU A 496 ? 0.4714 0.7735 0.5608 -0.2440 0.0035  -0.0625 507 GLU A CB  
2042 C CG  . GLU A 496 ? 0.6372 0.9983 0.7516 -0.2420 -0.0051 -0.0674 507 GLU A CG  
2043 C CD  . GLU A 496 ? 0.8286 1.2425 0.9745 -0.2244 -0.0035 -0.0611 507 GLU A CD  
2044 O OE1 . GLU A 496 ? 0.6670 1.0732 0.8158 -0.2168 0.0067  -0.0545 507 GLU A OE1 
2045 O OE2 . GLU A 496 ? 0.7868 1.2489 0.9534 -0.2175 -0.0118 -0.0626 507 GLU A OE2 
2046 N N   . LYS A 497 ? 0.4169 0.6427 0.4617 -0.2149 -0.0166 -0.0616 508 LYS A N   
2047 C CA  . LYS A 497 ? 0.4946 0.7128 0.5278 -0.2099 -0.0283 -0.0669 508 LYS A CA  
2048 C C   . LYS A 497 ? 0.4021 0.6035 0.4286 -0.1782 -0.0335 -0.0572 508 LYS A C   
2049 O O   . LYS A 497 ? 0.3913 0.6038 0.4154 -0.1691 -0.0440 -0.0592 508 LYS A O   
2050 C CB  . LYS A 497 ? 0.4563 0.6232 0.4616 -0.2307 -0.0239 -0.0762 508 LYS A CB  
2051 C CG  . LYS A 497 ? 0.5673 0.7477 0.5757 -0.2560 -0.0201 -0.0865 508 LYS A CG  
2052 C CD  . LYS A 497 ? 0.6982 0.8197 0.6771 -0.2703 -0.0132 -0.0942 508 LYS A CD  
2053 C CE  . LYS A 497 ? 0.7743 0.9097 0.7557 -0.2929 -0.0094 -0.1047 508 LYS A CE  
2054 N NZ  . LYS A 497 ? 0.8959 0.9744 0.8492 -0.3054 -0.0021 -0.1129 508 LYS A NZ  
2055 N N   . ARG A 498 ? 0.3479 0.5229 0.3697 -0.1632 -0.0259 -0.0474 509 ARG A N   
2056 C CA  . ARG A 498 ? 0.3541 0.5132 0.3703 -0.1358 -0.0296 -0.0391 509 ARG A CA  
2057 C C   . ARG A 498 ? 0.3608 0.5680 0.3998 -0.1189 -0.0374 -0.0353 509 ARG A C   
2058 O O   . ARG A 498 ? 0.3557 0.6064 0.4179 -0.1219 -0.0364 -0.0351 509 ARG A O   
2059 C CB  . ARG A 498 ? 0.3171 0.4470 0.3261 -0.1264 -0.0201 -0.0308 509 ARG A CB  
2060 C CG  . ARG A 498 ? 0.3540 0.4568 0.3519 -0.1034 -0.0225 -0.0242 509 ARG A CG  
2061 C CD  . ARG A 498 ? 0.3587 0.4382 0.3490 -0.0966 -0.0140 -0.0173 509 ARG A CD  
2062 N NE  . ARG A 498 ? 0.3339 0.3815 0.3068 -0.1125 -0.0068 -0.0172 509 ARG A NE  
2063 C CZ  . ARG A 498 ? 0.4562 0.4928 0.4231 -0.1146 0.0018  -0.0118 509 ARG A CZ  
2064 N NH1 . ARG A 498 ? 0.3417 0.3954 0.3180 -0.1025 0.0046  -0.0081 509 ARG A NH1 
2065 N NH2 . ARG A 498 ? 0.3815 0.3875 0.3307 -0.1295 0.0085  -0.0102 509 ARG A NH2 
2066 N N   . GLY A 499 ? 0.2959 0.4958 0.3284 -0.1007 -0.0446 -0.0316 510 GLY A N   
2067 C CA  . GLY A 499 ? 0.2999 0.5402 0.3507 -0.0831 -0.0518 -0.0258 510 GLY A CA  
2068 C C   . GLY A 499 ? 0.2380 0.4874 0.3046 -0.0653 -0.0448 -0.0173 510 GLY A C   
2069 O O   . GLY A 499 ? 0.2992 0.5150 0.3563 -0.0597 -0.0369 -0.0144 510 GLY A O   
2070 N N   . SER A 500 ? 0.2420 0.5385 0.3330 -0.0557 -0.0479 -0.0135 511 SER A N   
2071 C CA  . SER A 500 ? 0.3068 0.6084 0.4113 -0.0336 -0.0415 -0.0053 511 SER A CA  
2072 C C   . SER A 500 ? 0.2851 0.5684 0.3806 -0.0121 -0.0459 0.0025  511 SER A C   
2073 O O   . SER A 500 ? 0.2768 0.5568 0.3603 -0.0129 -0.0552 0.0024  511 SER A O   
2074 C CB  . SER A 500 ? 0.2022 0.5606 0.3378 -0.0283 -0.0416 -0.0032 511 SER A CB  
2075 O OG  . SER A 500 ? 0.2476 0.6405 0.3915 -0.0202 -0.0544 0.0006  511 SER A OG  
2076 N N   . ALA A 501 ? 0.2801 0.5511 0.3804 0.0063  -0.0381 0.0086  512 ALA A N   
2077 C CA  . ALA A 501 ? 0.2805 0.5340 0.3734 0.0257  -0.0405 0.0165  512 ALA A CA  
2078 C C   . ALA A 501 ? 0.2570 0.5478 0.3612 0.0370  -0.0505 0.0236  512 ALA A C   
2079 O O   . ALA A 501 ? 0.2491 0.5299 0.3395 0.0426  -0.0575 0.0279  512 ALA A O   
2080 C CB  . ALA A 501 ? 0.2642 0.4988 0.3613 0.0416  -0.0290 0.0204  512 ALA A CB  
2081 N N   . LYS A 502 ? 0.2466 0.5832 0.3758 0.0412  -0.0512 0.0255  513 LYS A N   
2082 C CA  . LYS A 502 ? 0.3050 0.6838 0.4462 0.0534  -0.0622 0.0338  513 LYS A CA  
2083 C C   . LYS A 502 ? 0.3367 0.7269 0.4636 0.0362  -0.0755 0.0283  513 LYS A C   
2084 O O   . LYS A 502 ? 0.2662 0.6589 0.3830 0.0454  -0.0835 0.0350  513 LYS A O   
2085 C CB  . LYS A 502 ? 0.2536 0.6836 0.4264 0.0588  -0.0604 0.0352  513 LYS A CB  
2086 C CG  . LYS A 502 ? 0.2488 0.7020 0.4263 0.0709  -0.0678 0.0433  513 LYS A CG  
2087 C CD  . LYS A 502 ? 0.3919 0.8831 0.5971 0.0762  -0.0630 0.0438  513 LYS A CD  
2088 C CE  . LYS A 502 ? 0.4504 0.9702 0.6614 0.0879  -0.0718 0.0521  513 LYS A CE  
2089 N NZ  . LYS A 502 ? 0.6414 1.2027 0.8806 0.0917  -0.0683 0.0516  513 LYS A NZ  
2090 N N   . GLU A 503 ? 0.2816 0.6690 0.4030 0.0099  -0.0755 0.0154  514 GLU A N   
2091 C CA  . GLU A 503 ? 0.2985 0.6924 0.4046 -0.0089 -0.0862 0.0073  514 GLU A CA  
2092 C C   . GLU A 503 ? 0.2830 0.6304 0.3596 -0.0061 -0.0873 0.0077  514 GLU A C   
2093 O O   . GLU A 503 ? 0.2810 0.6388 0.3454 -0.0057 -0.0972 0.0084  514 GLU A O   
2094 C CB  . GLU A 503 ? 0.2317 0.6250 0.3374 -0.0382 -0.0829 -0.0068 514 GLU A CB  
2095 C CG  . GLU A 503 ? 0.3011 0.7469 0.4338 -0.0472 -0.0834 -0.0098 514 GLU A CG  
2096 C CD  . GLU A 503 ? 0.3829 0.8241 0.5163 -0.0765 -0.0766 -0.0222 514 GLU A CD  
2097 O OE1 . GLU A 503 ? 0.3426 0.7299 0.4529 -0.0857 -0.0695 -0.0264 514 GLU A OE1 
2098 O OE2 . GLU A 503 ? 0.4099 0.8830 0.5603 -0.0868 -0.0742 -0.0260 514 GLU A OE2 
2099 N N   . LEU A 504 ? 0.2694 0.5683 0.3343 -0.0041 -0.0770 0.0072  515 LEU A N   
2100 C CA  . LEU A 504 ? 0.2697 0.5270 0.3093 -0.0028 -0.0768 0.0065  515 LEU A CA  
2101 C C   . LEU A 504 ? 0.3110 0.5672 0.3464 0.0189  -0.0795 0.0185  515 LEU A C   
2102 O O   . LEU A 504 ? 0.2994 0.5351 0.3147 0.0189  -0.0820 0.0180  515 LEU A O   
2103 C CB  . LEU A 504 ? 0.2865 0.4990 0.3174 -0.0059 -0.0660 0.0035  515 LEU A CB  
2104 C CG  . LEU A 504 ? 0.3014 0.5038 0.3268 -0.0290 -0.0635 -0.0077 515 LEU A CG  
2105 C CD1 . LEU A 504 ? 0.2894 0.4552 0.3088 -0.0299 -0.0532 -0.0078 515 LEU A CD1 
2106 C CD2 . LEU A 504 ? 0.3323 0.5214 0.3376 -0.0421 -0.0690 -0.0162 515 LEU A CD2 
2107 N N   . LEU A 505 ? 0.2756 0.5520 0.3289 0.0376  -0.0780 0.0296  516 LEU A N   
2108 C CA  . LEU A 505 ? 0.2848 0.5601 0.3333 0.0583  -0.0801 0.0430  516 LEU A CA  
2109 C C   . LEU A 505 ? 0.3784 0.6811 0.4183 0.0565  -0.0922 0.0451  516 LEU A C   
2110 O O   . LEU A 505 ? 0.3256 0.6147 0.3533 0.0686  -0.0920 0.0544  516 LEU A O   
2111 C CB  . LEU A 505 ? 0.2795 0.5682 0.3494 0.0796  -0.0744 0.0544  516 LEU A CB  
2112 C CG  . LEU A 505 ? 0.2938 0.5419 0.3640 0.0859  -0.0600 0.0541  516 LEU A CG  
2113 C CD1 . LEU A 505 ? 0.3214 0.5864 0.4153 0.1028  -0.0528 0.0606  516 LEU A CD1 
2114 C CD2 . LEU A 505 ? 0.3326 0.5420 0.3838 0.0946  -0.0562 0.0605  516 LEU A CD2 
2115 N N   . GLN A 506 ? 0.2644 0.5962 0.3087 0.0390  -0.0992 0.0351  517 GLN A N   
2116 C CA  . GLN A 506 ? 0.3247 0.6730 0.3573 0.0323  -0.1078 0.0330  517 GLN A CA  
2117 C C   . GLN A 506 ? 0.3106 0.6386 0.3181 0.0137  -0.1109 0.0202  517 GLN A C   
2118 O O   . GLN A 506 ? 0.3511 0.6903 0.3462 0.0064  -0.1173 0.0162  517 GLN A O   
2119 C CB  . GLN A 506 ? 0.3517 0.7443 0.4034 0.0238  -0.1128 0.0288  517 GLN A CB  
2120 C CG  . GLN A 506 ? 0.3696 0.7842 0.4458 0.0440  -0.1095 0.0412  517 GLN A CG  
2121 C CD  . GLN A 506 ? 0.5803 0.9832 0.6491 0.0676  -0.1089 0.0572  517 GLN A CD  
2122 O OE1 . GLN A 506 ? 0.5896 0.9951 0.6418 0.0675  -0.1156 0.0599  517 GLN A OE1 
2123 N NE2 . GLN A 506 ? 0.5686 0.9554 0.6480 0.0868  -0.0997 0.0674  517 GLN A NE2 
2124 N N   . HIS A 507 ? 0.3194 0.6177 0.3181 0.0062  -0.1060 0.0133  518 HIS A N   
2125 C CA  . HIS A 507 ? 0.3288 0.6036 0.3043 -0.0123 -0.1066 -0.0010 518 HIS A CA  
2126 C C   . HIS A 507 ? 0.3904 0.6500 0.3425 -0.0045 -0.1082 0.0026  518 HIS A C   
2127 O O   . HIS A 507 ? 0.3572 0.6049 0.3076 0.0144  -0.1048 0.0158  518 HIS A O   
2128 C CB  . HIS A 507 ? 0.3576 0.5863 0.3302 -0.0186 -0.0947 -0.0073 518 HIS A CB  
2129 C CG  . HIS A 507 ? 0.4413 0.6448 0.3948 -0.0386 -0.0930 -0.0228 518 HIS A CG  
2130 N ND1 . HIS A 507 ? 0.3824 0.5594 0.3127 -0.0378 -0.0917 -0.0269 518 HIS A ND1 
2131 C CD2 . HIS A 507 ? 0.3844 0.5834 0.3383 -0.0597 -0.0911 -0.0352 518 HIS A CD2 
2132 C CE1 . HIS A 507 ? 0.4447 0.6006 0.3619 -0.0561 -0.0890 -0.0416 518 HIS A CE1 
2133 N NE2 . HIS A 507 ? 0.4474 0.6144 0.3779 -0.0702 -0.0885 -0.0466 518 HIS A NE2 
2134 N N   . GLN A 508 ? 0.3582 0.6147 0.2918 -0.0200 -0.1115 -0.0098 519 GLN A N   
2135 C CA  . GLN A 508 ? 0.3959 0.6395 0.3063 -0.0145 -0.1119 -0.0080 519 GLN A CA  
2136 C C   . GLN A 508 ? 0.4689 0.6775 0.3662 -0.0047 -0.1043 -0.0044 519 GLN A C   
2137 O O   . GLN A 508 ? 0.3870 0.5874 0.2715 0.0068  -0.1024 0.0040  519 GLN A O   
2138 C CB  . GLN A 508 ? 0.3954 0.6352 0.2863 -0.0343 -0.1143 -0.0254 519 GLN A CB  
2139 C CG  . GLN A 508 ? 0.5654 0.8399 0.4627 -0.0459 -0.1220 -0.0308 519 GLN A CG  
2140 C CD  . GLN A 508 ? 0.8018 1.1032 0.6986 -0.0317 -0.1285 -0.0173 519 GLN A CD  
2141 O OE1 . GLN A 508 ? 0.8667 1.2008 0.7840 -0.0241 -0.1332 -0.0076 519 GLN A OE1 
2142 N NE2 . GLN A 508 ? 0.7898 1.0759 0.6630 -0.0262 -0.1276 -0.0152 519 GLN A NE2 
2143 N N   . PHE A 509 ? 0.3673 0.5432 0.2708 -0.0095 -0.0951 -0.0106 520 PHE A N   
2144 C CA  . PHE A 509 ? 0.3544 0.4907 0.2509 -0.0007 -0.0847 -0.0081 520 PHE A CA  
2145 C C   . PHE A 509 ? 0.4390 0.5762 0.3436 0.0188  -0.0818 0.0089  520 PHE A C   
2146 O O   . PHE A 509 ? 0.3842 0.5020 0.2776 0.0266  -0.0761 0.0131  520 PHE A O   
2147 C CB  . PHE A 509 ? 0.3472 0.4551 0.2515 -0.0074 -0.0770 -0.0149 520 PHE A CB  
2148 C CG  . PHE A 509 ? 0.3646 0.4394 0.2668 0.0028  -0.0676 -0.0111 520 PHE A CG  
2149 C CD1 . PHE A 509 ? 0.4142 0.4694 0.2991 0.0041  -0.0635 -0.0156 520 PHE A CD1 
2150 C CD2 . PHE A 509 ? 0.2988 0.3646 0.2165 0.0099  -0.0627 -0.0043 520 PHE A CD2 
2151 C CE1 . PHE A 509 ? 0.3408 0.3717 0.2267 0.0128  -0.0552 -0.0124 520 PHE A CE1 
2152 C CE2 . PHE A 509 ? 0.3487 0.3892 0.2654 0.0173  -0.0552 -0.0018 520 PHE A CE2 
2153 C CZ  . PHE A 509 ? 0.4283 0.4531 0.3304 0.0189  -0.0518 -0.0055 520 PHE A CZ  
2154 N N   . LEU A 510 ? 0.3532 0.5117 0.2773 0.0268  -0.0843 0.0184  521 LEU A N   
2155 C CA  . LEU A 510 ? 0.3509 0.5046 0.2818 0.0453  -0.0798 0.0340  521 LEU A CA  
2156 C C   . LEU A 510 ? 0.3814 0.5474 0.2975 0.0552  -0.0839 0.0449  521 LEU A C   
2157 O O   . LEU A 510 ? 0.3878 0.5392 0.3027 0.0689  -0.0776 0.0574  521 LEU A O   
2158 C CB  . LEU A 510 ? 0.3532 0.5257 0.3081 0.0531  -0.0801 0.0410  521 LEU A CB  
2159 C CG  . LEU A 510 ? 0.2816 0.4413 0.2489 0.0434  -0.0746 0.0315  521 LEU A CG  
2160 C CD1 . LEU A 510 ? 0.3451 0.5208 0.3355 0.0529  -0.0720 0.0382  521 LEU A CD1 
2161 C CD2 . LEU A 510 ? 0.2943 0.4134 0.2535 0.0419  -0.0653 0.0275  521 LEU A CD2 
2162 N N   . LYS A 511 ? 0.4101 0.5982 0.3145 0.0466  -0.0926 0.0396  522 LYS A N   
2163 C CA  . LYS A 511 ? 0.3801 0.5731 0.2724 0.0539  -0.0938 0.0493  522 LYS A CA  
2164 C C   . LYS A 511 ? 0.4410 0.6081 0.3100 0.0547  -0.0870 0.0493  522 LYS A C   
2165 O O   . LYS A 511 ? 0.4642 0.6301 0.3226 0.0623  -0.0854 0.0599  522 LYS A O   
2166 C CB  . LYS A 511 ? 0.3690 0.5916 0.2560 0.0433  -0.1040 0.0425  522 LYS A CB  
2167 C CG  . LYS A 511 ? 0.5373 0.7926 0.4480 0.0416  -0.1107 0.0423  522 LYS A CG  
2168 C CD  . LYS A 511 ? 0.5590 0.8445 0.4630 0.0311  -0.1205 0.0360  522 LYS A CD  
2169 C CE  . LYS A 511 ? 0.6735 0.9948 0.6016 0.0265  -0.1266 0.0336  522 LYS A CE  
2170 N NZ  . LYS A 511 ? 0.6898 1.0141 0.6428 0.0413  -0.1220 0.0448  522 LYS A NZ  
2171 N N   . ILE A 512 ? 0.3816 0.5272 0.2431 0.0478  -0.0819 0.0380  523 ILE A N   
2172 C CA  . ILE A 512 ? 0.3742 0.4939 0.2188 0.0490  -0.0725 0.0370  523 ILE A CA  
2173 C C   . ILE A 512 ? 0.4139 0.5083 0.2705 0.0590  -0.0614 0.0464  523 ILE A C   
2174 O O   . ILE A 512 ? 0.4154 0.4886 0.2639 0.0589  -0.0521 0.0447  523 ILE A O   
2175 C CB  . ILE A 512 ? 0.4074 0.5099 0.2418 0.0351  -0.0691 0.0176  523 ILE A CB  
2176 C CG1 . ILE A 512 ? 0.4786 0.5595 0.3309 0.0315  -0.0637 0.0106  523 ILE A CG1 
2177 C CG2 . ILE A 512 ? 0.5768 0.7013 0.3982 0.0218  -0.0791 0.0054  523 ILE A CG2 
2178 C CD1 . ILE A 512 ? 0.5260 0.5839 0.3687 0.0227  -0.0580 -0.0050 523 ILE A CD1 
2179 N N   . ALA A 513 ? 0.3743 0.4719 0.2510 0.0666  -0.0616 0.0547  524 ALA A N   
2180 C CA  . ALA A 513 ? 0.4271 0.5000 0.3148 0.0736  -0.0508 0.0611  524 ALA A CA  
2181 C C   . ALA A 513 ? 0.4143 0.4757 0.2889 0.0820  -0.0435 0.0741  524 ALA A C   
2182 O O   . ALA A 513 ? 0.4438 0.5197 0.3080 0.0900  -0.0477 0.0864  524 ALA A O   
2183 C CB  . ALA A 513 ? 0.4117 0.4910 0.3205 0.0810  -0.0515 0.0674  524 ALA A CB  
2184 N N   . LYS A 514 ? 0.4451 0.4819 0.3199 0.0796  -0.0325 0.0715  525 LYS A N   
2185 C CA  . LYS A 514 ? 0.4217 0.4437 0.2876 0.0855  -0.0226 0.0838  525 LYS A CA  
2186 C C   . LYS A 514 ? 0.4589 0.4687 0.3382 0.0950  -0.0171 0.0956  525 LYS A C   
2187 O O   . LYS A 514 ? 0.4307 0.4417 0.3275 0.0957  -0.0192 0.0913  525 LYS A O   
2188 C CB  . LYS A 514 ? 0.4341 0.4389 0.2984 0.0775  -0.0126 0.0749  525 LYS A CB  
2189 C CG  . LYS A 514 ? 0.4633 0.4753 0.3116 0.0708  -0.0140 0.0648  525 LYS A CG  
2190 C CD  . LYS A 514 ? 0.4493 0.4473 0.3005 0.0659  -0.0028 0.0579  525 LYS A CD  
2191 C CE  . LYS A 514 ? 0.5175 0.5207 0.3521 0.0616  -0.0011 0.0485  525 LYS A CE  
2192 N NZ  . LYS A 514 ? 0.5183 0.5125 0.3597 0.0587  0.0105  0.0427  525 LYS A NZ  
2193 N N   . PRO A 515 ? 0.4309 0.4270 0.3010 0.1026  -0.0088 0.1108  526 PRO A N   
2194 C CA  . PRO A 515 ? 0.4190 0.3956 0.3006 0.1111  -0.0005 0.1206  526 PRO A CA  
2195 C C   . PRO A 515 ? 0.4776 0.4343 0.3738 0.1017  0.0082  0.1084  526 PRO A C   
2196 O O   . PRO A 515 ? 0.4266 0.3813 0.3220 0.0903  0.0105  0.0969  526 PRO A O   
2197 C CB  . PRO A 515 ? 0.5413 0.5033 0.4097 0.1141  0.0085  0.1339  526 PRO A CB  
2198 C CG  . PRO A 515 ? 0.5470 0.5145 0.3956 0.1069  0.0090  0.1315  526 PRO A CG  
2199 C CD  . PRO A 515 ? 0.4625 0.4574 0.3094 0.1032  -0.0050 0.1197  526 PRO A CD  
2200 N N   . LEU A 516 ? 0.3890 0.3329 0.2991 0.1071  0.0130  0.1105  527 LEU A N   
2201 C CA  . LEU A 516 ? 0.3904 0.3191 0.3133 0.0970  0.0199  0.0974  527 LEU A CA  
2202 C C   . LEU A 516 ? 0.4316 0.3391 0.3492 0.0877  0.0323  0.0964  527 LEU A C   
2203 O O   . LEU A 516 ? 0.3653 0.2695 0.2914 0.0762  0.0352  0.0834  527 LEU A O   
2204 C CB  . LEU A 516 ? 0.4467 0.3648 0.3829 0.1045  0.0241  0.0988  527 LEU A CB  
2205 C CG  . LEU A 516 ? 0.4736 0.4171 0.4202 0.1103  0.0127  0.0959  527 LEU A CG  
2206 C CD1 . LEU A 516 ? 0.4537 0.3874 0.4129 0.1203  0.0191  0.0987  527 LEU A CD1 
2207 C CD2 . LEU A 516 ? 0.3711 0.3277 0.3228 0.0972  0.0057  0.0796  527 LEU A CD2 
2208 N N   . SER A 517 ? 0.4290 0.3245 0.3327 0.0919  0.0397  0.1104  528 SER A N   
2209 C CA  . SER A 517 ? 0.4984 0.3774 0.3971 0.0807  0.0523  0.1091  528 SER A CA  
2210 C C   . SER A 517 ? 0.4825 0.3803 0.3816 0.0695  0.0482  0.0959  528 SER A C   
2211 O O   . SER A 517 ? 0.4198 0.3118 0.3242 0.0578  0.0568  0.0886  528 SER A O   
2212 C CB  . SER A 517 ? 0.5646 0.4294 0.4446 0.0873  0.0605  0.1281  528 SER A CB  
2213 O OG  . SER A 517 ? 0.5051 0.3927 0.3702 0.0938  0.0504  0.1346  528 SER A OG  
2214 N N   . SER A 518 ? 0.4081 0.3290 0.3029 0.0727  0.0357  0.0921  529 SER A N   
2215 C CA  . SER A 518 ? 0.4270 0.3624 0.3222 0.0645  0.0328  0.0792  529 SER A CA  
2216 C C   . SER A 518 ? 0.4220 0.3581 0.3352 0.0566  0.0324  0.0651  529 SER A C   
2217 O O   . SER A 518 ? 0.3823 0.3274 0.2987 0.0506  0.0330  0.0558  529 SER A O   
2218 C CB  . SER A 518 ? 0.3998 0.3550 0.2864 0.0685  0.0200  0.0758  529 SER A CB  
2219 O OG  . SER A 518 ? 0.4252 0.3875 0.3235 0.0700  0.0102  0.0695  529 SER A OG  
2220 N N   . LEU A 519 ? 0.3581 0.2860 0.2827 0.0572  0.0318  0.0634  530 LEU A N   
2221 C CA  . LEU A 519 ? 0.3383 0.2689 0.2772 0.0495  0.0306  0.0506  530 LEU A CA  
2222 C C   . LEU A 519 ? 0.3451 0.2660 0.2907 0.0392  0.0419  0.0471  530 LEU A C   
2223 O O   . LEU A 519 ? 0.3618 0.2912 0.3183 0.0318  0.0403  0.0362  530 LEU A O   
2224 C CB  . LEU A 519 ? 0.3478 0.2757 0.2946 0.0530  0.0257  0.0486  530 LEU A CB  
2225 C CG  . LEU A 519 ? 0.3523 0.2935 0.2967 0.0606  0.0145  0.0503  530 LEU A CG  
2226 C CD1 . LEU A 519 ? 0.3395 0.2791 0.2940 0.0626  0.0126  0.0474  530 LEU A CD1 
2227 C CD2 . LEU A 519 ? 0.3206 0.2767 0.2617 0.0575  0.0059  0.0425  530 LEU A CD2 
2228 N N   . THR A 520 ? 0.3801 0.2842 0.3193 0.0379  0.0533  0.0562  531 THR A N   
2229 C CA  . THR A 520 ? 0.3939 0.2876 0.3409 0.0250  0.0648  0.0509  531 THR A CA  
2230 C C   . THR A 520 ? 0.4062 0.3193 0.3593 0.0154  0.0666  0.0430  531 THR A C   
2231 O O   . THR A 520 ? 0.3608 0.2787 0.3264 0.0035  0.0703  0.0332  531 THR A O   
2232 C CB  . THR A 520 ? 0.4864 0.3514 0.4244 0.0244  0.0790  0.0628  531 THR A CB  
2233 O OG1 . THR A 520 ? 0.4767 0.3418 0.4011 0.0265  0.0842  0.0739  531 THR A OG1 
2234 C CG2 . THR A 520 ? 0.4809 0.3280 0.4150 0.0373  0.0778  0.0713  531 THR A CG2 
2235 N N   . PRO A 521 ? 0.3615 0.2887 0.3072 0.0200  0.0643  0.0458  532 PRO A N   
2236 C CA  . PRO A 521 ? 0.3241 0.2728 0.2794 0.0132  0.0659  0.0367  532 PRO A CA  
2237 C C   . PRO A 521 ? 0.2895 0.2552 0.2585 0.0138  0.0551  0.0252  532 PRO A C   
2238 O O   . PRO A 521 ? 0.2884 0.2709 0.2716 0.0063  0.0570  0.0170  532 PRO A O   
2239 C CB  . PRO A 521 ? 0.3536 0.3103 0.2949 0.0203  0.0660  0.0417  532 PRO A CB  
2240 C CG  . PRO A 521 ? 0.3634 0.3001 0.2867 0.0252  0.0702  0.0562  532 PRO A CG  
2241 C CD  . PRO A 521 ? 0.3715 0.2954 0.2990 0.0298  0.0633  0.0575  532 PRO A CD  
2242 N N   . LEU A 522 ? 0.3122 0.2758 0.2776 0.0224  0.0439  0.0249  533 LEU A N   
2243 C CA  . LEU A 522 ? 0.3299 0.3056 0.3055 0.0231  0.0342  0.0160  533 LEU A CA  
2244 C C   . LEU A 522 ? 0.2904 0.2648 0.2770 0.0134  0.0361  0.0102  533 LEU A C   
2245 O O   . LEU A 522 ? 0.2791 0.2707 0.2768 0.0096  0.0319  0.0024  533 LEU A O   
2246 C CB  . LEU A 522 ? 0.3062 0.2770 0.2742 0.0318  0.0240  0.0178  533 LEU A CB  
2247 C CG  . LEU A 522 ? 0.3185 0.2915 0.2741 0.0394  0.0202  0.0207  533 LEU A CG  
2248 C CD1 . LEU A 522 ? 0.3245 0.2941 0.2754 0.0442  0.0105  0.0212  533 LEU A CD1 
2249 C CD2 . LEU A 522 ? 0.3325 0.3185 0.2906 0.0412  0.0198  0.0143  533 LEU A CD2 
2250 N N   . ILE A 523 ? 0.2996 0.2537 0.2824 0.0102  0.0422  0.0138  534 ILE A N   
2251 C CA  . ILE A 523 ? 0.3476 0.2969 0.3382 -0.0009 0.0460  0.0063  534 ILE A CA  
2252 C C   . ILE A 523 ? 0.2765 0.2392 0.2774 -0.0144 0.0532  0.0001  534 ILE A C   
2253 O O   . ILE A 523 ? 0.2976 0.2757 0.3091 -0.0235 0.0501  -0.0100 534 ILE A O   
2254 C CB  . ILE A 523 ? 0.3560 0.2760 0.3395 -0.0003 0.0543  0.0116  534 ILE A CB  
2255 C CG1 . ILE A 523 ? 0.3624 0.2778 0.3406 0.0126  0.0461  0.0159  534 ILE A CG1 
2256 C CG2 . ILE A 523 ? 0.3974 0.3075 0.3868 -0.0147 0.0622  0.0019  534 ILE A CG2 
2257 C CD1 . ILE A 523 ? 0.4101 0.3006 0.3812 0.0199  0.0534  0.0254  534 ILE A CD1 
2258 N N   . ALA A 524 ? 0.3059 0.2661 0.3039 -0.0164 0.0625  0.0060  535 ALA A N   
2259 C CA  . ALA A 524 ? 0.3475 0.3240 0.3571 -0.0304 0.0707  0.0002  535 ALA A CA  
2260 C C   . ALA A 524 ? 0.3274 0.3404 0.3510 -0.0280 0.0614  -0.0072 535 ALA A C   
2261 O O   . ALA A 524 ? 0.2924 0.3277 0.3312 -0.0398 0.0621  -0.0162 535 ALA A O   
2262 C CB  . ALA A 524 ? 0.3155 0.2828 0.3173 -0.0321 0.0835  0.0094  535 ALA A CB  
2263 N N   . ALA A 525 ? 0.2695 0.2896 0.2882 -0.0128 0.0531  -0.0035 536 ALA A N   
2264 C CA  . ALA A 525 ? 0.2742 0.3242 0.3050 -0.0070 0.0451  -0.0090 536 ALA A CA  
2265 C C   . ALA A 525 ? 0.2467 0.3071 0.2850 -0.0084 0.0342  -0.0154 536 ALA A C   
2266 O O   . ALA A 525 ? 0.2709 0.3605 0.3244 -0.0115 0.0304  -0.0214 536 ALA A O   
2267 C CB  . ALA A 525 ? 0.2210 0.2682 0.2416 0.0090  0.0402  -0.0044 536 ALA A CB  
2268 N N   . ALA A 526 ? 0.2651 0.3046 0.2926 -0.0057 0.0291  -0.0138 537 ALA A N   
2269 C CA  . ALA A 526 ? 0.3437 0.3914 0.3745 -0.0076 0.0198  -0.0194 537 ALA A CA  
2270 C C   . ALA A 526 ? 0.3163 0.3763 0.3573 -0.0248 0.0235  -0.0284 537 ALA A C   
2271 O O   . ALA A 526 ? 0.2910 0.3767 0.3409 -0.0278 0.0155  -0.0344 537 ALA A O   
2272 C CB  . ALA A 526 ? 0.3007 0.3235 0.3183 -0.0029 0.0165  -0.0163 537 ALA A CB  
2273 N N   . LYS A 527 ? 0.3420 0.3836 0.3808 -0.0367 0.0358  -0.0294 538 LYS A N   
2274 C CA  . LYS A 527 ? 0.3236 0.3743 0.3712 -0.0564 0.0412  -0.0400 538 LYS A CA  
2275 C C   . LYS A 527 ? 0.3481 0.4387 0.4143 -0.0630 0.0403  -0.0449 538 LYS A C   
2276 O O   . LYS A 527 ? 0.3121 0.4302 0.3890 -0.0737 0.0348  -0.0546 538 LYS A O   
2277 C CB  . LYS A 527 ? 0.4236 0.4405 0.4639 -0.0673 0.0570  -0.0390 538 LYS A CB  
2278 C CG  . LYS A 527 ? 0.5365 0.5171 0.5617 -0.0608 0.0586  -0.0356 538 LYS A CG  
2279 C CD  . LYS A 527 ? 0.5679 0.5120 0.5857 -0.0697 0.0754  -0.0336 538 LYS A CD  
2280 C CE  . LYS A 527 ? 0.6684 0.5803 0.6749 -0.0637 0.0779  -0.0329 538 LYS A CE  
2281 N NZ  . LYS A 527 ? 0.6710 0.5906 0.6788 -0.0718 0.0725  -0.0469 538 LYS A NZ  
2282 N N   . GLU A 528 ? 0.2765 0.3742 0.3468 -0.0565 0.0456  -0.0385 539 GLU A N   
2283 C CA  . GLU A 528 ? 0.2825 0.4218 0.3729 -0.0602 0.0456  -0.0427 539 GLU A CA  
2284 C C   . GLU A 528 ? 0.2880 0.4594 0.3877 -0.0476 0.0299  -0.0441 539 GLU A C   
2285 O O   . GLU A 528 ? 0.2978 0.5091 0.4158 -0.0544 0.0255  -0.0510 539 GLU A O   
2286 C CB  . GLU A 528 ? 0.2615 0.3999 0.3517 -0.0530 0.0552  -0.0353 539 GLU A CB  
2287 C CG  . GLU A 528 ? 0.2790 0.4624 0.3909 -0.0510 0.0556  -0.0385 539 GLU A CG  
2288 C CD  . GLU A 528 ? 0.4646 0.6769 0.5961 -0.0739 0.0634  -0.0477 539 GLU A CD  
2289 O OE1 . GLU A 528 ? 0.3642 0.5540 0.4896 -0.0933 0.0723  -0.0512 539 GLU A OE1 
2290 O OE2 . GLU A 528 ? 0.3563 0.6142 0.5101 -0.0724 0.0614  -0.0516 539 GLU A OE2 
2291 N N   . ALA A 529 ? 0.2214 0.3769 0.3086 -0.0292 0.0215  -0.0372 540 ALA A N   
2292 C CA  . ALA A 529 ? 0.3273 0.5075 0.4208 -0.0153 0.0080  -0.0362 540 ALA A CA  
2293 C C   . ALA A 529 ? 0.3508 0.5451 0.4455 -0.0238 -0.0018 -0.0423 540 ALA A C   
2294 O O   . ALA A 529 ? 0.3085 0.5381 0.4150 -0.0187 -0.0119 -0.0433 540 ALA A O   
2295 C CB  . ALA A 529 ? 0.2999 0.4543 0.3774 0.0034  0.0031  -0.0280 540 ALA A CB  
2296 N N   . THR A 530 ? 0.2400 0.4082 0.3221 -0.0358 0.0011  -0.0462 541 THR A N   
2297 C CA  . THR A 530 ? 0.3915 0.5696 0.4703 -0.0446 -0.0072 -0.0532 541 THR A CA  
2298 C C   . THR A 530 ? 0.6041 0.8093 0.6962 -0.0669 -0.0042 -0.0656 541 THR A C   
2299 O O   . THR A 530 ? 0.6423 0.8568 0.7302 -0.0780 -0.0100 -0.0741 541 THR A O   
2300 C CB  . THR A 530 ? 0.3400 0.4783 0.3988 -0.0459 -0.0049 -0.0530 541 THR A CB  
2301 O OG1 . THR A 530 ? 0.5601 0.6684 0.6147 -0.0555 0.0095  -0.0545 541 THR A OG1 
2302 C CG2 . THR A 530 ? 0.5095 0.6298 0.5568 -0.0261 -0.0106 -0.0422 541 THR A CG2 
2332 N N   . GLU B 244 ? 1.4122 1.3692 1.4298 -0.0256 0.5875  0.0091  255 GLU B N   
2333 C CA  . GLU B 244 ? 1.2691 1.2515 1.3408 -0.0432 0.5594  0.0181  255 GLU B CA  
2334 C C   . GLU B 244 ? 1.1649 1.1615 1.2772 -0.0361 0.5350  0.0043  255 GLU B C   
2335 O O   . GLU B 244 ? 1.1714 1.2023 1.3494 -0.0463 0.5139  0.0109  255 GLU B O   
2336 C CB  . GLU B 244 ? 1.1229 1.1532 1.2691 -0.0552 0.5671  0.0387  255 GLU B CB  
2337 N N   . LYS B 245 ? 1.2691 1.2372 1.3395 -0.0190 0.5366  -0.0149 256 LYS B N   
2338 C CA  . LYS B 245 ? 1.1751 1.1480 1.2707 -0.0133 0.5119  -0.0284 256 LYS B CA  
2339 C C   . LYS B 245 ? 1.2843 1.2490 1.3698 -0.0306 0.4827  -0.0277 256 LYS B C   
2340 O O   . LYS B 245 ? 1.1956 1.1817 1.3272 -0.0328 0.4593  -0.0315 256 LYS B O   
2341 C CB  . LYS B 245 ? 1.2641 1.1979 1.3033 0.0055  0.5171  -0.0494 256 LYS B CB  
2342 N N   . LEU B 246 ? 1.2491 1.1818 1.2725 -0.0423 0.4836  -0.0223 257 LEU B N   
2343 C CA  . LEU B 246 ? 1.1542 1.0787 1.1679 -0.0595 0.4585  -0.0187 257 LEU B CA  
2344 C C   . LEU B 246 ? 1.1471 1.1177 1.2464 -0.0727 0.4426  -0.0063 257 LEU B C   
2345 O O   . LEU B 246 ? 1.1413 1.1194 1.2607 -0.0775 0.4053  -0.0107 257 LEU B O   
2346 C CB  . LEU B 246 ? 1.1328 1.0199 1.0754 -0.0698 0.4650  -0.0088 257 LEU B CB  
2347 C CG  . LEU B 246 ? 1.1540 1.0232 1.0730 -0.0842 0.4274  -0.0028 257 LEU B CG  
2348 C CD1 . LEU B 246 ? 1.1877 1.0371 1.0751 -0.0775 0.3895  -0.0194 257 LEU B CD1 
2349 C CD2 . LEU B 246 ? 1.3575 1.1908 1.2101 -0.0924 0.4420  0.0104  257 LEU B CD2 
2350 N N   . ARG B 247 ? 1.1649 1.1653 1.3111 -0.0764 0.4563  0.0085  258 ARG B N   
2351 C CA  . ARG B 247 ? 1.1440 1.1849 1.3665 -0.0903 0.4374  0.0201  258 ARG B CA  
2352 C C   . ARG B 247 ? 1.1106 1.1825 1.3912 -0.0833 0.4157  0.0112  258 ARG B C   
2353 O O   . ARG B 247 ? 1.0210 1.1131 1.3437 -0.0956 0.3880  0.0148  258 ARG B O   
2354 C CB  . ARG B 247 ? 1.1044 1.1733 1.3659 -0.0941 0.4574  0.0366  258 ARG B CB  
2355 N N   . SER B 248 ? 1.0897 1.1629 1.3706 -0.0636 0.4264  -0.0004 259 SER B N   
2356 C CA  . SER B 248 ? 1.0810 1.1820 1.4162 -0.0561 0.4056  -0.0068 259 SER B CA  
2357 C C   . SER B 248 ? 1.1278 1.2144 1.4452 -0.0613 0.3782  -0.0176 259 SER B C   
2358 O O   . SER B 248 ? 1.0090 1.1211 1.3737 -0.0633 0.3512  -0.0181 259 SER B O   
2359 C CB  . SER B 248 ? 1.0932 1.1929 1.4293 -0.0329 0.4246  -0.0162 259 SER B CB  
2360 O OG  . SER B 248 ? 1.0452 1.1005 1.3113 -0.0232 0.4310  -0.0328 259 SER B OG  
2361 N N   . ILE B 249 ? 1.0811 1.1230 1.3201 -0.0616 0.3711  -0.0253 260 ILE B N   
2362 C CA  . ILE B 249 ? 0.9917 1.0146 1.1998 -0.0632 0.3322  -0.0348 260 ILE B CA  
2363 C C   . ILE B 249 ? 1.0303 1.0470 1.2272 -0.0801 0.3089  -0.0275 260 ILE B C   
2364 O O   . ILE B 249 ? 1.1076 1.1118 1.2823 -0.0815 0.2779  -0.0339 260 ILE B O   
2365 C CB  . ILE B 249 ? 1.0745 1.0533 1.2072 -0.0525 0.3331  -0.0485 260 ILE B CB  
2366 C CG1 . ILE B 249 ? 1.2499 1.2163 1.3625 -0.0398 0.3741  -0.0517 260 ILE B CG1 
2367 C CG2 . ILE B 249 ? 1.1065 1.0838 1.2432 -0.0448 0.3056  -0.0603 260 ILE B CG2 
2368 C CD1 . ILE B 249 ? 1.2593 1.1762 1.2890 -0.0316 0.3754  -0.0653 260 ILE B CD1 
2369 N N   . VAL B 250 ? 0.8594 0.8841 1.0726 -0.0928 0.3234  -0.0137 261 VAL B N   
2370 C CA  . VAL B 250 ? 0.8315 0.8427 1.0293 -0.1081 0.3038  -0.0066 261 VAL B CA  
2371 C C   . VAL B 250 ? 0.7185 0.7646 0.9857 -0.1209 0.2894  0.0009  261 VAL B C   
2372 O O   . VAL B 250 ? 0.9788 1.0544 1.2988 -0.1264 0.3093  0.0110  261 VAL B O   
2373 C CB  . VAL B 250 ? 0.9454 0.9300 1.1004 -0.1152 0.3279  0.0046  261 VAL B CB  
2374 C CG1 . VAL B 250 ? 0.9561 0.9244 1.0996 -0.1303 0.3069  0.0130  261 VAL B CG1 
2375 C CG2 . VAL B 250 ? 0.9658 0.9115 1.0439 -0.1034 0.3365  -0.0038 261 VAL B CG2 
2376 N N   . SER B 251 ? 0.7394 0.7826 1.0064 -0.1255 0.2548  -0.0043 262 SER B N   
2377 C CA  . SER B 251 ? 0.8133 0.8777 1.1296 -0.1401 0.2368  0.0015  262 SER B CA  
2378 C C   . SER B 251 ? 0.8215 0.8700 1.1314 -0.1565 0.2460  0.0146  262 SER B C   
2379 O O   . SER B 251 ? 0.7987 0.8145 1.0557 -0.1559 0.2581  0.0182  262 SER B O   
2380 C CB  . SER B 251 ? 0.7110 0.7693 1.0161 -0.1389 0.2001  -0.0088 262 SER B CB  
2381 O OG  . SER B 251 ? 0.9360 1.0096 1.2814 -0.1527 0.1809  -0.0055 262 SER B OG  
2382 N N   . VAL B 252 ? 0.7422 0.8125 1.1058 -0.1725 0.2381  0.0225  263 VAL B N   
2383 C CA  . VAL B 252 ? 0.8918 0.9495 1.2592 -0.1907 0.2488  0.0372  263 VAL B CA  
2384 C C   . VAL B 252 ? 0.7880 0.8160 1.1339 -0.2015 0.2192  0.0350  263 VAL B C   
2385 O O   . VAL B 252 ? 1.0801 1.0857 1.4160 -0.2156 0.2257  0.0469  263 VAL B O   
2386 C CB  . VAL B 252 ? 0.9249 1.0211 1.3492 -0.1966 0.2509  0.0489  263 VAL B CB  
2387 C CG1 . VAL B 252 ? 0.8660 0.9836 1.2993 -0.1825 0.2831  0.0529  263 VAL B CG1 
2388 C CG2 . VAL B 252 ? 0.9906 1.1150 1.4589 -0.1982 0.2185  0.0424  263 VAL B CG2 
2389 N N   . GLY B 253 ? 0.8844 0.9094 1.2214 -0.1947 0.1886  0.0208  264 GLY B N   
2390 C CA  . GLY B 253 ? 0.8790 0.8746 1.1943 -0.2016 0.1622  0.0165  264 GLY B CA  
2391 C C   . GLY B 253 ? 0.8261 0.7774 1.0788 -0.1966 0.1647  0.0186  264 GLY B C   
2392 O O   . GLY B 253 ? 0.8197 0.7607 1.0400 -0.1891 0.1864  0.0238  264 GLY B O   
2393 N N   . ASP B 254 ? 0.6936 0.6159 0.9278 -0.2005 0.1423  0.0149  265 ASP B N   
2394 C CA  . ASP B 254 ? 0.5613 0.4420 0.7390 -0.1931 0.1394  0.0166  265 ASP B CA  
2395 C C   . ASP B 254 ? 0.5498 0.4284 0.7007 -0.1747 0.1194  0.0011  265 ASP B C   
2396 O O   . ASP B 254 ? 0.6210 0.4983 0.7807 -0.1740 0.0970  -0.0091 265 ASP B O   
2397 C CB  . ASP B 254 ? 0.6270 0.4741 0.8021 -0.2071 0.1288  0.0232  265 ASP B CB  
2398 C CG  . ASP B 254 ? 0.6722 0.4747 0.7915 -0.1987 0.1255  0.0277  265 ASP B CG  
2399 O OD1 . ASP B 254 ? 0.6877 0.4868 0.7703 -0.1822 0.1273  0.0243  265 ASP B OD1 
2400 O OD2 . ASP B 254 ? 0.7329 0.5019 0.8457 -0.2090 0.1194  0.0353  265 ASP B OD2 
2401 N N   . PRO B 255 ? 0.5691 0.4458 0.6861 -0.1604 0.1263  -0.0009 266 PRO B N   
2402 C CA  . PRO B 255 ? 0.5881 0.4663 0.6854 -0.1446 0.1071  -0.0137 266 PRO B CA  
2403 C C   . PRO B 255 ? 0.5127 0.3605 0.5843 -0.1399 0.0887  -0.0156 266 PRO B C   
2404 O O   . PRO B 255 ? 0.5198 0.3735 0.5879 -0.1290 0.0715  -0.0266 266 PRO B O   
2405 C CB  . PRO B 255 ? 0.6043 0.4816 0.6696 -0.1342 0.1194  -0.0128 266 PRO B CB  
2406 C CG  . PRO B 255 ? 0.5842 0.4410 0.6302 -0.1421 0.1408  0.0012  266 PRO B CG  
2407 C CD  . PRO B 255 ? 0.6553 0.5247 0.7461 -0.1585 0.1509  0.0085  266 PRO B CD  
2408 N N   . LYS B 256 ? 0.5628 0.3777 0.6166 -0.1470 0.0928  -0.0044 267 LYS B N   
2409 C CA  . LYS B 256 ? 0.6816 0.4642 0.7138 -0.1410 0.0754  -0.0058 267 LYS B CA  
2410 C C   . LYS B 256 ? 0.6015 0.3842 0.6603 -0.1461 0.0596  -0.0161 267 LYS B C   
2411 O O   . LYS B 256 ? 0.6885 0.4507 0.7323 -0.1362 0.0436  -0.0231 267 LYS B O   
2412 C CB  . LYS B 256 ? 0.6802 0.4246 0.6869 -0.1485 0.0841  0.0109  267 LYS B CB  
2413 C CG  . LYS B 256 ? 0.8211 0.5569 0.7882 -0.1417 0.0961  0.0206  267 LYS B CG  
2414 C CD  . LYS B 256 ? 0.7839 0.4806 0.7230 -0.1504 0.1055  0.0396  267 LYS B CD  
2415 C CE  . LYS B 256 ? 0.9578 0.6426 0.8490 -0.1434 0.1151  0.0487  267 LYS B CE  
2416 N NZ  . LYS B 256 ? 1.0969 0.7410 0.9542 -0.1511 0.1232  0.0691  267 LYS B NZ  
2417 N N   . LYS B 257 ? 0.5605 0.3649 0.6579 -0.1610 0.0634  -0.0170 268 LYS B N   
2418 C CA  . LYS B 257 ? 0.6083 0.4161 0.7303 -0.1677 0.0463  -0.0280 268 LYS B CA  
2419 C C   . LYS B 257 ? 0.5588 0.3998 0.6917 -0.1572 0.0363  -0.0422 268 LYS B C   
2420 O O   . LYS B 257 ? 0.5290 0.3643 0.6601 -0.1536 0.0189  -0.0546 268 LYS B O   
2421 C CB  . LYS B 257 ? 0.6061 0.4245 0.7687 -0.1907 0.0524  -0.0203 268 LYS B CB  
2422 C CG  . LYS B 257 ? 0.6357 0.4189 0.7948 -0.2063 0.0585  -0.0064 268 LYS B CG  
2423 C CD  . LYS B 257 ? 0.7395 0.5408 0.9484 -0.2302 0.0603  -0.0003 268 LYS B CD  
2424 C CE  . LYS B 257 ? 0.6840 0.4591 0.8970 -0.2489 0.0730  0.0184  268 LYS B CE  
2425 N NZ  . LYS B 257 ? 0.8869 0.6913 1.1575 -0.2727 0.0788  0.0273  268 LYS B NZ  
2426 N N   . LYS B 258 ? 0.5470 0.4191 0.6872 -0.1518 0.0474  -0.0404 269 LYS B N   
2427 C CA  . LYS B 258 ? 0.4939 0.3985 0.6487 -0.1445 0.0393  -0.0506 269 LYS B CA  
2428 C C   . LYS B 258 ? 0.4290 0.3319 0.5548 -0.1259 0.0309  -0.0585 269 LYS B C   
2429 O O   . LYS B 258 ? 0.4116 0.3343 0.5442 -0.1199 0.0207  -0.0676 269 LYS B O   
2430 C CB  . LYS B 258 ? 0.4879 0.4238 0.6664 -0.1468 0.0555  -0.0445 269 LYS B CB  
2431 C CG  . LYS B 258 ? 0.6118 0.5812 0.8094 -0.1405 0.0484  -0.0518 269 LYS B CG  
2432 C CD  . LYS B 258 ? 0.5846 0.5796 0.8078 -0.1419 0.0662  -0.0452 269 LYS B CD  
2433 C CE  . LYS B 258 ? 0.5499 0.5745 0.7913 -0.1346 0.0588  -0.0507 269 LYS B CE  
2434 N NZ  . LYS B 258 ? 0.5740 0.6169 0.8487 -0.1432 0.0423  -0.0533 269 LYS B NZ  
2435 N N   . TYR B 259 ? 0.4460 0.3270 0.5411 -0.1172 0.0346  -0.0539 270 TYR B N   
2436 C CA  . TYR B 259 ? 0.4419 0.3257 0.5151 -0.1002 0.0275  -0.0585 270 TYR B CA  
2437 C C   . TYR B 259 ? 0.4661 0.3168 0.5151 -0.0920 0.0195  -0.0582 270 TYR B C   
2438 O O   . TYR B 259 ? 0.4979 0.3194 0.5376 -0.0989 0.0234  -0.0501 270 TYR B O   
2439 C CB  . TYR B 259 ? 0.4379 0.3312 0.4983 -0.0957 0.0375  -0.0524 270 TYR B CB  
2440 C CG  . TYR B 259 ? 0.4310 0.3539 0.5148 -0.1005 0.0460  -0.0536 270 TYR B CG  
2441 C CD1 . TYR B 259 ? 0.3913 0.3403 0.4886 -0.0949 0.0379  -0.0610 270 TYR B CD1 
2442 C CD2 . TYR B 259 ? 0.4512 0.3755 0.5442 -0.1099 0.0634  -0.0463 270 TYR B CD2 
2443 C CE1 . TYR B 259 ? 0.4450 0.4184 0.5648 -0.0981 0.0442  -0.0613 270 TYR B CE1 
2444 C CE2 . TYR B 259 ? 0.4809 0.4319 0.5985 -0.1115 0.0716  -0.0476 270 TYR B CE2 
2445 C CZ  . TYR B 259 ? 0.4249 0.3990 0.5557 -0.1054 0.0607  -0.0551 270 TYR B CZ  
2446 O OH  . TYR B 259 ? 0.6405 0.6385 0.7963 -0.1057 0.0673  -0.0555 270 TYR B OH  
2447 N N   . THR B 260 ? 0.4595 0.3151 0.5000 -0.0767 0.0093  -0.0657 271 THR B N   
2448 C CA  . THR B 260 ? 0.5322 0.3592 0.5534 -0.0647 0.0019  -0.0657 271 THR B CA  
2449 C C   . THR B 260 ? 0.5985 0.4424 0.6118 -0.0472 -0.0030 -0.0661 271 THR B C   
2450 O O   . THR B 260 ? 0.4951 0.3703 0.5168 -0.0464 -0.0014 -0.0669 271 THR B O   
2451 C CB  . THR B 260 ? 0.5385 0.3479 0.5625 -0.0639 -0.0065 -0.0772 271 THR B CB  
2452 O OG1 . THR B 260 ? 0.5539 0.3282 0.5594 -0.0521 -0.0118 -0.0760 271 THR B OG1 
2453 C CG2 . THR B 260 ? 0.5222 0.3594 0.5535 -0.0550 -0.0118 -0.0899 271 THR B CG2 
2454 N N   A ARG B 261 ? 0.5679 0.3909 0.5678 -0.0331 -0.0097 -0.0646 272 ARG B N   
2455 N N   B ARG B 261 ? 0.5678 0.3906 0.5678 -0.0332 -0.0097 -0.0648 272 ARG B N   
2456 C CA  A ARG B 261 ? 0.5667 0.4066 0.5645 -0.0160 -0.0156 -0.0626 272 ARG B CA  
2457 C CA  B ARG B 261 ? 0.5677 0.4054 0.5645 -0.0159 -0.0157 -0.0622 272 ARG B CA  
2458 C C   A ARG B 261 ? 0.5576 0.4116 0.5489 -0.0204 -0.0144 -0.0525 272 ARG B C   
2459 C C   B ARG B 261 ? 0.5577 0.4114 0.5490 -0.0205 -0.0143 -0.0526 272 ARG B C   
2460 O O   A ARG B 261 ? 0.5876 0.4730 0.5884 -0.0174 -0.0164 -0.0540 272 ARG B O   
2461 O O   B ARG B 261 ? 0.5873 0.4728 0.5888 -0.0178 -0.0160 -0.0545 272 ARG B O   
2462 C CB  A ARG B 261 ? 0.5459 0.4173 0.5593 -0.0068 -0.0172 -0.0738 272 ARG B CB  
2463 C CB  B ARG B 261 ? 0.5521 0.4188 0.5636 -0.0048 -0.0180 -0.0734 272 ARG B CB  
2464 C CG  A ARG B 261 ? 0.6230 0.4784 0.6342 0.0063  -0.0200 -0.0845 272 ARG B CG  
2465 C CG  B ARG B 261 ? 0.6513 0.5011 0.6590 0.0139  -0.0223 -0.0795 272 ARG B CG  
2466 C CD  A ARG B 261 ? 0.5598 0.4472 0.5811 0.0232  -0.0202 -0.0897 272 ARG B CD  
2467 C CD  B ARG B 261 ? 0.6136 0.4582 0.6223 0.0127  -0.0208 -0.0947 272 ARG B CD  
2468 N NE  A ARG B 261 ? 0.6548 0.5241 0.6699 0.0397  -0.0204 -0.1005 272 ARG B NE  
2469 N NE  B ARG B 261 ? 0.5456 0.3552 0.5428 0.0265  -0.0238 -0.1024 272 ARG B NE  
2470 C CZ  A ARG B 261 ? 0.6162 0.5073 0.6387 0.0588  -0.0177 -0.1047 272 ARG B CZ  
2471 C CZ  B ARG B 261 ? 0.6271 0.4436 0.6246 0.0479  -0.0229 -0.1102 272 ARG B CZ  
2472 N NH1 A ARG B 261 ? 0.5506 0.4840 0.5902 0.0621  -0.0162 -0.0975 272 ARG B NH1 
2473 N NH1 B ARG B 261 ? 0.6033 0.4628 0.6143 0.0572  -0.0193 -0.1091 272 ARG B NH1 
2474 N NH2 A ARG B 261 ? 0.6594 0.5284 0.6722 0.0749  -0.0156 -0.1163 272 ARG B NH2 
2475 N NH2 B ARG B 261 ? 0.6258 0.4043 0.6104 0.0604  -0.0247 -0.1193 272 ARG B NH2 
2476 N N   . PHE B 262 ? 0.5033 0.3311 0.4754 -0.0282 -0.0112 -0.0420 273 PHE B N   
2477 C CA  . PHE B 262 ? 0.6451 0.4781 0.6014 -0.0317 -0.0106 -0.0335 273 PHE B CA  
2478 C C   . PHE B 262 ? 0.6769 0.5148 0.6266 -0.0169 -0.0251 -0.0280 273 PHE B C   
2479 O O   . PHE B 262 ? 0.5935 0.4106 0.5367 -0.0060 -0.0329 -0.0229 273 PHE B O   
2480 C CB  . PHE B 262 ? 0.6066 0.4079 0.5385 -0.0432 -0.0016 -0.0229 273 PHE B CB  
2481 C CG  . PHE B 262 ? 0.5699 0.3766 0.5128 -0.0592 0.0145  -0.0255 273 PHE B CG  
2482 C CD1 . PHE B 262 ? 0.6192 0.4194 0.5809 -0.0666 0.0185  -0.0297 273 PHE B CD1 
2483 C CD2 . PHE B 262 ? 0.6413 0.4590 0.5766 -0.0665 0.0250  -0.0240 273 PHE B CD2 
2484 C CE1 . PHE B 262 ? 0.6699 0.4799 0.6487 -0.0815 0.0319  -0.0304 273 PHE B CE1 
2485 C CE2 . PHE B 262 ? 0.5559 0.3820 0.5069 -0.0790 0.0412  -0.0255 273 PHE B CE2 
2486 C CZ  . PHE B 262 ? 0.5311 0.3560 0.5067 -0.0868 0.0443  -0.0277 273 PHE B CZ  
2487 N N   . GLU B 263 ? 0.6335 0.4979 0.5867 -0.0169 -0.0297 -0.0284 274 GLU B N   
2488 C CA  . GLU B 263 ? 0.6799 0.5561 0.6338 -0.0053 -0.0456 -0.0224 274 GLU B CA  
2489 C C   . GLU B 263 ? 0.6709 0.5500 0.6057 -0.0140 -0.0504 -0.0179 274 GLU B C   
2490 O O   . GLU B 263 ? 0.6464 0.5432 0.5881 -0.0228 -0.0441 -0.0244 274 GLU B O   
2491 C CB  . GLU B 263 ? 0.6617 0.5752 0.6491 0.0050  -0.0491 -0.0294 274 GLU B CB  
2492 C CG  . GLU B 263 ? 0.8974 0.8301 0.8959 0.0172  -0.0650 -0.0218 274 GLU B CG  
2493 C CD  . GLU B 263 ? 1.0500 1.0234 1.0836 0.0262  -0.0644 -0.0272 274 GLU B CD  
2494 O OE1 . GLU B 263 ? 1.0297 1.0210 1.0737 0.0182  -0.0548 -0.0354 274 GLU B OE1 
2495 O OE2 . GLU B 263 ? 1.1620 1.1506 1.2137 0.0417  -0.0730 -0.0219 274 GLU B OE2 
2496 N N   . LYS B 264 ? 0.7218 0.5811 0.6306 -0.0111 -0.0627 -0.0069 275 LYS B N   
2497 C CA  . LYS B 264 ? 0.7213 0.5773 0.6041 -0.0196 -0.0697 -0.0039 275 LYS B CA  
2498 C C   . LYS B 264 ? 0.7663 0.6585 0.6748 -0.0167 -0.0844 -0.0062 275 LYS B C   
2499 O O   . LYS B 264 ? 0.8284 0.7404 0.7628 -0.0046 -0.0967 -0.0021 275 LYS B O   
2500 C CB  . LYS B 264 ? 0.8168 0.6390 0.6597 -0.0179 -0.0811 0.0094  275 LYS B CB  
2501 C CG  . LYS B 264 ? 0.8817 0.6937 0.6877 -0.0269 -0.0901 0.0116  275 LYS B CG  
2502 C CD  . LYS B 264 ? 0.9775 0.7542 0.7391 -0.0249 -0.1035 0.0261  275 LYS B CD  
2503 C CE  . LYS B 264 ? 1.0676 0.8089 0.8045 -0.0278 -0.0847 0.0323  275 LYS B CE  
2504 N NZ  . LYS B 264 ? 1.1765 0.8803 0.8661 -0.0261 -0.0972 0.0489  275 LYS B NZ  
2505 N N   . ILE B 265 ? 0.7743 0.6754 0.6780 -0.0277 -0.0821 -0.0124 276 ILE B N   
2506 C CA  . ILE B 265 ? 0.7747 0.7078 0.7026 -0.0289 -0.0960 -0.0137 276 ILE B CA  
2507 C C   . ILE B 265 ? 0.9289 0.8479 0.8251 -0.0391 -0.1096 -0.0126 276 ILE B C   
2508 O O   . ILE B 265 ? 0.9067 0.8482 0.8209 -0.0435 -0.1227 -0.0135 276 ILE B O   
2509 C CB  . ILE B 265 ? 0.7333 0.6944 0.6938 -0.0323 -0.0829 -0.0233 276 ILE B CB  
2510 C CG1 . ILE B 265 ? 0.6648 0.6087 0.6055 -0.0437 -0.0670 -0.0312 276 ILE B CG1 
2511 C CG2 . ILE B 265 ? 0.6059 0.5798 0.5932 -0.0222 -0.0724 -0.0256 276 ILE B CG2 
2512 C CD1 . ILE B 265 ? 0.5663 0.5356 0.5352 -0.0485 -0.0600 -0.0384 276 ILE B CD1 
2513 N N   . GLY B 266 ? 0.7688 0.6494 0.6165 -0.0437 -0.1066 -0.0106 277 GLY B N   
2514 C CA  . GLY B 266 ? 0.9585 0.8191 0.7668 -0.0531 -0.1193 -0.0116 277 GLY B CA  
2515 C C   . GLY B 266 ? 1.0487 0.8650 0.7989 -0.0576 -0.1073 -0.0109 277 GLY B C   
2516 O O   . GLY B 266 ? 0.9921 0.7968 0.7385 -0.0568 -0.0834 -0.0118 277 GLY B O   
2517 N N   . GLN B 267 ? 1.2274 1.0185 0.9309 -0.0631 -0.1239 -0.0089 278 GLN B N   
2518 C CA  . GLN B 267 ? 1.2793 1.0258 0.9183 -0.0675 -0.1128 -0.0079 278 GLN B CA  
2519 C C   . GLN B 267 ? 1.3654 1.0946 0.9680 -0.0770 -0.1185 -0.0192 278 GLN B C   
2520 O O   . GLN B 267 ? 1.3280 1.0623 0.9286 -0.0809 -0.1479 -0.0189 278 GLN B O   
2521 C CB  . GLN B 267 ? 1.3685 1.0920 0.9736 -0.0629 -0.1312 0.0081  278 GLN B CB  
2522 C CG  . GLN B 267 ? 1.4788 1.1536 1.0085 -0.0681 -0.1223 0.0116  278 GLN B CG  
2523 C CD  . GLN B 267 ? 1.4331 1.0948 0.9574 -0.0683 -0.0854 0.0120  278 GLN B CD  
2524 O OE1 . GLN B 267 ? 1.4151 1.0941 0.9826 -0.0632 -0.0753 0.0164  278 GLN B OE1 
2525 N NE2 . GLN B 267 ? 1.4859 1.1164 0.9569 -0.0746 -0.0649 0.0075  278 GLN B NE2 
2526 N N   . GLY B 268 ? 1.2942 1.0025 0.8698 -0.0806 -0.0909 -0.0293 279 GLY B N   
2527 C CA  . GLY B 268 ? 1.2988 0.9851 0.8376 -0.0878 -0.0922 -0.0427 279 GLY B CA  
2528 C C   . GLY B 268 ? 1.3358 0.9756 0.8020 -0.0893 -0.0725 -0.0452 279 GLY B C   
2529 O O   . GLY B 268 ? 1.2108 0.8380 0.6590 -0.0861 -0.0559 -0.0349 279 GLY B O   
2530 N N   . ALA B 269 ? 1.4885 1.1011 0.9118 -0.0944 -0.0742 -0.0591 280 ALA B N   
2531 C CA  . ALA B 269 ? 1.4592 1.0266 0.8104 -0.0944 -0.0506 -0.0645 280 ALA B CA  
2532 C C   . ALA B 269 ? 1.4627 1.0389 0.8365 -0.0892 -0.0063 -0.0676 280 ALA B C   
2533 O O   . ALA B 269 ? 1.6056 1.1553 0.9342 -0.0876 0.0198  -0.0642 280 ALA B O   
2534 C CB  . ALA B 269 ? 1.4608 0.9947 0.7616 -0.0999 -0.0624 -0.0817 280 ALA B CB  
2535 N N   . SER B 270 ? 1.1892 0.8034 0.6333 -0.0870 0.0024  -0.0725 281 SER B N   
2536 C CA  . SER B 270 ? 1.2571 0.8867 0.7343 -0.0826 0.0401  -0.0738 281 SER B CA  
2537 C C   . SER B 270 ? 1.1743 0.8228 0.6819 -0.0815 0.0497  -0.0577 281 SER B C   
2538 O O   . SER B 270 ? 1.1884 0.8444 0.7147 -0.0801 0.0810  -0.0560 281 SER B O   
2539 C CB  . SER B 270 ? 1.1737 0.8347 0.7118 -0.0811 0.0422  -0.0843 281 SER B CB  
2540 O OG  . SER B 270 ? 1.0214 0.7116 0.6024 -0.0836 0.0117  -0.0806 281 SER B OG  
2541 N N   . GLY B 271 ? 1.1184 0.7746 0.6345 -0.0820 0.0236  -0.0460 282 GLY B N   
2542 C CA  . GLY B 271 ? 0.9857 0.6529 0.5267 -0.0805 0.0295  -0.0316 282 GLY B CA  
2543 C C   . GLY B 271 ? 1.0282 0.7251 0.6174 -0.0774 0.0021  -0.0267 282 GLY B C   
2544 O O   . GLY B 271 ? 1.0596 0.7679 0.6576 -0.0772 -0.0233 -0.0312 282 GLY B O   
2545 N N   . THR B 272 ? 0.8818 0.5910 0.5034 -0.0750 0.0084  -0.0175 283 THR B N   
2546 C CA  . THR B 272 ? 0.9610 0.6956 0.6264 -0.0694 -0.0126 -0.0129 283 THR B CA  
2547 C C   . THR B 272 ? 0.8204 0.5914 0.5464 -0.0685 -0.0031 -0.0217 283 THR B C   
2548 O O   . THR B 272 ? 0.7618 0.5361 0.5031 -0.0716 0.0209  -0.0242 283 THR B O   
2549 C CB  . THR B 272 ? 0.9606 0.6792 0.6189 -0.0663 -0.0140 0.0019  283 THR B CB  
2550 O OG1 . THR B 272 ? 1.0236 0.7046 0.6195 -0.0681 -0.0198 0.0120  283 THR B OG1 
2551 C CG2 . THR B 272 ? 0.9304 0.6705 0.6265 -0.0572 -0.0376 0.0058  283 THR B CG2 
2552 N N   . VAL B 273 ? 0.7257 0.5251 0.4864 -0.0646 -0.0222 -0.0252 284 VAL B N   
2553 C CA  . VAL B 273 ? 0.6933 0.5266 0.5058 -0.0637 -0.0162 -0.0329 284 VAL B CA  
2554 C C   . VAL B 273 ? 0.7243 0.5752 0.5703 -0.0562 -0.0245 -0.0282 284 VAL B C   
2555 O O   . VAL B 273 ? 0.6905 0.5455 0.5373 -0.0498 -0.0444 -0.0223 284 VAL B O   
2556 C CB  . VAL B 273 ? 0.6855 0.5372 0.5107 -0.0658 -0.0279 -0.0407 284 VAL B CB  
2557 C CG1 . VAL B 273 ? 0.6056 0.4918 0.4817 -0.0646 -0.0228 -0.0462 284 VAL B CG1 
2558 C CG2 . VAL B 273 ? 0.7579 0.5860 0.5467 -0.0719 -0.0186 -0.0480 284 VAL B CG2 
2559 N N   . TYR B 274 ? 0.6575 0.5183 0.5314 -0.0565 -0.0099 -0.0311 285 TYR B N   
2560 C CA  . TYR B 274 ? 0.5674 0.4413 0.4705 -0.0492 -0.0153 -0.0301 285 TYR B CA  
2561 C C   . TYR B 274 ? 0.5446 0.4510 0.4868 -0.0491 -0.0121 -0.0391 285 TYR B C   
2562 O O   . TYR B 274 ? 0.5605 0.4759 0.5106 -0.0557 -0.0022 -0.0447 285 TYR B O   
2563 C CB  . TYR B 274 ? 0.5781 0.4291 0.4757 -0.0510 -0.0041 -0.0255 285 TYR B CB  
2564 C CG  . TYR B 274 ? 0.7442 0.5606 0.6032 -0.0505 -0.0071 -0.0138 285 TYR B CG  
2565 C CD1 . TYR B 274 ? 0.7273 0.5214 0.5493 -0.0585 0.0039  -0.0096 285 TYR B CD1 
2566 C CD2 . TYR B 274 ? 0.8044 0.6083 0.6618 -0.0411 -0.0201 -0.0065 285 TYR B CD2 
2567 C CE1 . TYR B 274 ? 0.8273 0.5876 0.6085 -0.0586 0.0011  0.0028  285 TYR B CE1 
2568 C CE2 . TYR B 274 ? 0.8975 0.6674 0.7182 -0.0405 -0.0245 0.0065  285 TYR B CE2 
2569 C CZ  . TYR B 274 ? 0.9209 0.6691 0.7021 -0.0501 -0.0142 0.0116  285 TYR B CZ  
2570 O OH  . TYR B 274 ? 1.0642 0.7768 0.8038 -0.0499 -0.0186 0.0261  285 TYR B OH  
2571 N N   . THR B 275 ? 0.5826 0.5054 0.5478 -0.0404 -0.0203 -0.0400 286 THR B N   
2572 C CA  . THR B 275 ? 0.4701 0.4163 0.4658 -0.0400 -0.0151 -0.0476 286 THR B CA  
2573 C C   . THR B 275 ? 0.4762 0.4065 0.4748 -0.0398 -0.0082 -0.0494 286 THR B C   
2574 O O   . THR B 275 ? 0.5170 0.4225 0.5002 -0.0360 -0.0107 -0.0441 286 THR B O   
2575 C CB  . THR B 275 ? 0.5333 0.5082 0.5505 -0.0307 -0.0257 -0.0487 286 THR B CB  
2576 O OG1 . THR B 275 ? 0.5153 0.4826 0.5291 -0.0188 -0.0345 -0.0438 286 THR B OG1 
2577 C CG2 . THR B 275 ? 0.5519 0.5437 0.5714 -0.0345 -0.0334 -0.0466 286 THR B CG2 
2578 N N   . ALA B 276 ? 0.3834 0.3263 0.4016 -0.0448 -0.0014 -0.0562 287 ALA B N   
2579 C CA  . ALA B 276 ? 0.4295 0.3577 0.4529 -0.0476 0.0026  -0.0592 287 ALA B CA  
2580 C C   . ALA B 276 ? 0.4133 0.3647 0.4595 -0.0497 0.0028  -0.0677 287 ALA B C   
2581 O O   . ALA B 276 ? 0.3757 0.3525 0.4328 -0.0492 0.0016  -0.0693 287 ALA B O   
2582 C CB  . ALA B 276 ? 0.4131 0.3194 0.4274 -0.0594 0.0139  -0.0540 287 ALA B CB  
2583 N N   . MET B 277 ? 0.3769 0.3171 0.4288 -0.0532 0.0029  -0.0726 288 MET B N   
2584 C CA  . MET B 277 ? 0.3603 0.3188 0.4285 -0.0558 0.0002  -0.0807 288 MET B CA  
2585 C C   . MET B 277 ? 0.3816 0.3318 0.4621 -0.0701 0.0034  -0.0815 288 MET B C   
2586 O O   . MET B 277 ? 0.4232 0.3466 0.4975 -0.0751 0.0044  -0.0797 288 MET B O   
2587 C CB  . MET B 277 ? 0.3707 0.3258 0.4324 -0.0440 -0.0069 -0.0888 288 MET B CB  
2588 C CG  . MET B 277 ? 0.3603 0.3322 0.4307 -0.0464 -0.0106 -0.0971 288 MET B CG  
2589 S SD  . MET B 277 ? 0.3892 0.3507 0.4437 -0.0317 -0.0156 -0.1090 288 MET B SD  
2590 C CE  . MET B 277 ? 0.4217 0.3405 0.4676 -0.0405 -0.0199 -0.1148 288 MET B CE  
2591 N N   . ASP B 278 ? 0.3675 0.3411 0.4679 -0.0770 0.0038  -0.0829 289 ASP B N   
2592 C CA  . ASP B 278 ? 0.4211 0.3948 0.5415 -0.0906 0.0037  -0.0834 289 ASP B CA  
2593 C C   . ASP B 278 ? 0.3740 0.3312 0.4885 -0.0921 -0.0077 -0.0922 289 ASP B C   
2594 O O   . ASP B 278 ? 0.3682 0.3331 0.4745 -0.0845 -0.0160 -0.1003 289 ASP B O   
2595 C CB  . ASP B 278 ? 0.3443 0.3489 0.4882 -0.0942 0.0035  -0.0825 289 ASP B CB  
2596 C CG  . ASP B 278 ? 0.4169 0.4282 0.5895 -0.1082 0.0035  -0.0802 289 ASP B CG  
2597 O OD1 . ASP B 278 ? 0.4168 0.4170 0.5924 -0.1157 -0.0064 -0.0848 289 ASP B OD1 
2598 O OD2 . ASP B 278 ? 0.3622 0.3899 0.5561 -0.1116 0.0131  -0.0739 289 ASP B OD2 
2599 N N   . VAL B 279 ? 0.3959 0.3285 0.5126 -0.1025 -0.0077 -0.0907 290 VAL B N   
2600 C CA  . VAL B 279 ? 0.4257 0.3329 0.5322 -0.1046 -0.0195 -0.1002 290 VAL B CA  
2601 C C   . VAL B 279 ? 0.4233 0.3447 0.5431 -0.1130 -0.0321 -0.1081 290 VAL B C   
2602 O O   . VAL B 279 ? 0.4478 0.3516 0.5498 -0.1103 -0.0440 -0.1200 290 VAL B O   
2603 C CB  . VAL B 279 ? 0.4757 0.3507 0.5831 -0.1162 -0.0162 -0.0940 290 VAL B CB  
2604 C CG1 . VAL B 279 ? 0.5729 0.4263 0.6840 -0.1282 -0.0297 -0.1022 290 VAL B CG1 
2605 C CG2 . VAL B 279 ? 0.4759 0.3236 0.5566 -0.1035 -0.0116 -0.0905 290 VAL B CG2 
2606 N N   . ALA B 280 ? 0.3988 0.3500 0.5476 -0.1223 -0.0306 -0.1019 291 ALA B N   
2607 C CA  . ALA B 280 ? 0.3986 0.3647 0.5619 -0.1310 -0.0454 -0.1070 291 ALA B CA  
2608 C C   . ALA B 280 ? 0.3787 0.3692 0.5330 -0.1198 -0.0498 -0.1105 291 ALA B C   
2609 O O   . ALA B 280 ? 0.3912 0.3837 0.5383 -0.1223 -0.0648 -0.1181 291 ALA B O   
2610 C CB  . ALA B 280 ? 0.3862 0.3737 0.5924 -0.1470 -0.0431 -0.0967 291 ALA B CB  
2611 N N   . THR B 281 ? 0.3523 0.3599 0.5053 -0.1090 -0.0382 -0.1046 292 THR B N   
2612 C CA  . THR B 281 ? 0.3544 0.3857 0.5024 -0.1006 -0.0415 -0.1050 292 THR B CA  
2613 C C   . THR B 281 ? 0.3702 0.3988 0.4912 -0.0847 -0.0363 -0.1082 292 THR B C   
2614 O O   . THR B 281 ? 0.3904 0.4360 0.5034 -0.0784 -0.0394 -0.1090 292 THR B O   
2615 C CB  . THR B 281 ? 0.3155 0.3736 0.4906 -0.1024 -0.0344 -0.0944 292 THR B CB  
2616 O OG1 . THR B 281 ? 0.3190 0.3731 0.4891 -0.0960 -0.0199 -0.0895 292 THR B OG1 
2617 C CG2 . THR B 281 ? 0.3631 0.4294 0.5730 -0.1163 -0.0364 -0.0893 292 THR B CG2 
2618 N N   . GLY B 282 ? 0.3632 0.3732 0.4721 -0.0782 -0.0287 -0.1082 293 GLY B N   
2619 C CA  . GLY B 282 ? 0.3399 0.3527 0.4315 -0.0628 -0.0241 -0.1089 293 GLY B CA  
2620 C C   . GLY B 282 ? 0.3120 0.3469 0.4135 -0.0596 -0.0172 -0.0994 293 GLY B C   
2621 O O   . GLY B 282 ? 0.3502 0.3926 0.4432 -0.0486 -0.0148 -0.0981 293 GLY B O   
2622 N N   . GLN B 283 ? 0.3088 0.3542 0.4292 -0.0688 -0.0142 -0.0929 294 GLN B N   
2623 C CA  . GLN B 283 ? 0.3139 0.3731 0.4398 -0.0664 -0.0085 -0.0856 294 GLN B CA  
2624 C C   . GLN B 283 ? 0.3574 0.4006 0.4700 -0.0617 -0.0033 -0.0829 294 GLN B C   
2625 O O   . GLN B 283 ? 0.3259 0.3480 0.4337 -0.0656 0.0005  -0.0823 294 GLN B O   
2626 C CB  . GLN B 283 ? 0.2831 0.3514 0.4306 -0.0752 -0.0045 -0.0808 294 GLN B CB  
2627 C CG  . GLN B 283 ? 0.3622 0.4370 0.5105 -0.0727 0.0013  -0.0754 294 GLN B CG  
2628 C CD  . GLN B 283 ? 0.3381 0.4201 0.5073 -0.0779 0.0071  -0.0717 294 GLN B CD  
2629 O OE1 . GLN B 283 ? 0.4143 0.4974 0.6010 -0.0840 0.0093  -0.0714 294 GLN B OE1 
2630 N NE2 . GLN B 283 ? 0.4216 0.5087 0.5914 -0.0755 0.0093  -0.0687 294 GLN B NE2 
2631 N N   . GLU B 284 ? 0.2901 0.3437 0.3975 -0.0545 -0.0041 -0.0798 295 GLU B N   
2632 C CA  . GLU B 284 ? 0.3010 0.3422 0.3964 -0.0511 -0.0026 -0.0755 295 GLU B CA  
2633 C C   . GLU B 284 ? 0.3362 0.3731 0.4322 -0.0584 0.0032  -0.0715 295 GLU B C   
2634 O O   . GLU B 284 ? 0.3033 0.3545 0.4119 -0.0622 0.0044  -0.0708 295 GLU B O   
2635 C CB  . GLU B 284 ? 0.3179 0.3743 0.4118 -0.0418 -0.0079 -0.0730 295 GLU B CB  
2636 C CG  . GLU B 284 ? 0.3816 0.4411 0.4730 -0.0310 -0.0099 -0.0777 295 GLU B CG  
2637 C CD  . GLU B 284 ? 0.5028 0.5839 0.6000 -0.0207 -0.0124 -0.0737 295 GLU B CD  
2638 O OE1 . GLU B 284 ? 0.4637 0.5601 0.5691 -0.0242 -0.0152 -0.0668 295 GLU B OE1 
2639 O OE2 . GLU B 284 ? 0.8027 0.8848 0.8972 -0.0088 -0.0115 -0.0774 295 GLU B OE2 
2640 N N   . VAL B 285 ? 0.3359 0.3503 0.4158 -0.0596 0.0075  -0.0688 296 VAL B N   
2641 C CA  . VAL B 285 ? 0.3286 0.3338 0.4018 -0.0653 0.0160  -0.0663 296 VAL B CA  
2642 C C   . VAL B 285 ? 0.4136 0.4012 0.4597 -0.0622 0.0129  -0.0624 296 VAL B C   
2643 O O   . VAL B 285 ? 0.3779 0.3576 0.4135 -0.0564 0.0055  -0.0601 296 VAL B O   
2644 C CB  . VAL B 285 ? 0.3606 0.3545 0.4397 -0.0727 0.0282  -0.0655 296 VAL B CB  
2645 C CG1 . VAL B 285 ? 0.3050 0.3181 0.4137 -0.0770 0.0280  -0.0684 296 VAL B CG1 
2646 C CG2 . VAL B 285 ? 0.3745 0.3447 0.4386 -0.0732 0.0288  -0.0628 296 VAL B CG2 
2647 N N   . ALA B 286 ? 0.3655 0.3457 0.3993 -0.0656 0.0176  -0.0620 297 ALA B N   
2648 C CA  . ALA B 286 ? 0.4598 0.4179 0.4608 -0.0650 0.0148  -0.0588 297 ALA B CA  
2649 C C   . ALA B 286 ? 0.4149 0.3500 0.3974 -0.0697 0.0317  -0.0574 297 ALA B C   
2650 O O   . ALA B 286 ? 0.3917 0.3317 0.3865 -0.0730 0.0451  -0.0604 297 ALA B O   
2651 C CB  . ALA B 286 ? 0.4297 0.3924 0.4243 -0.0657 0.0060  -0.0605 297 ALA B CB  
2652 N N   . ILE B 287 ? 0.4285 0.3395 0.3829 -0.0694 0.0321  -0.0515 298 ILE B N   
2653 C CA  . ILE B 287 ? 0.4622 0.3512 0.3972 -0.0745 0.0505  -0.0476 298 ILE B CA  
2654 C C   . ILE B 287 ? 0.5888 0.4497 0.4754 -0.0738 0.0477  -0.0439 298 ILE B C   
2655 O O   . ILE B 287 ? 0.5642 0.4140 0.4323 -0.0702 0.0322  -0.0383 298 ILE B O   
2656 C CB  . ILE B 287 ? 0.4905 0.3718 0.4349 -0.0774 0.0553  -0.0417 298 ILE B CB  
2657 C CG1 . ILE B 287 ? 0.4440 0.3505 0.4318 -0.0790 0.0540  -0.0468 298 ILE B CG1 
2658 C CG2 . ILE B 287 ? 0.5345 0.3956 0.4614 -0.0845 0.0767  -0.0352 298 ILE B CG2 
2659 C CD1 . ILE B 287 ? 0.4511 0.3470 0.4493 -0.0843 0.0573  -0.0426 298 ILE B CD1 
2660 N N   . LYS B 288 ? 0.5242 0.3728 0.3891 -0.0763 0.0623  -0.0471 299 LYS B N   
2661 C CA  . LYS B 288 ? 0.6330 0.4500 0.4434 -0.0765 0.0614  -0.0447 299 LYS B CA  
2662 C C   . LYS B 288 ? 0.6950 0.4900 0.4819 -0.0804 0.0843  -0.0368 299 LYS B C   
2663 O O   . LYS B 288 ? 0.6311 0.4337 0.4362 -0.0830 0.1081  -0.0383 299 LYS B O   
2664 C CB  . LYS B 288 ? 0.6073 0.4185 0.4002 -0.0761 0.0628  -0.0550 299 LYS B CB  
2665 C CG  . LYS B 288 ? 0.7227 0.4974 0.4517 -0.0769 0.0572  -0.0547 299 LYS B CG  
2666 C CD  . LYS B 288 ? 0.8119 0.5740 0.5193 -0.0768 0.0592  -0.0674 299 LYS B CD  
2667 C CE  . LYS B 288 ? 0.7945 0.5757 0.5281 -0.0775 0.0337  -0.0729 299 LYS B CE  
2668 N NZ  . LYS B 288 ? 0.7309 0.4970 0.4483 -0.0782 0.0364  -0.0858 299 LYS B NZ  
2669 N N   . GLN B 289 ? 0.7344 0.5033 0.4829 -0.0807 0.0771  -0.0268 300 GLN B N   
2670 C CA  . GLN B 289 ? 0.7831 0.5279 0.5045 -0.0855 0.0978  -0.0161 300 GLN B CA  
2671 C C   . GLN B 289 ? 0.8771 0.5892 0.5329 -0.0855 0.1032  -0.0157 300 GLN B C   
2672 O O   . GLN B 289 ? 1.0083 0.7038 0.6283 -0.0829 0.0798  -0.0145 300 GLN B O   
2673 C CB  . GLN B 289 ? 0.9120 0.6453 0.6334 -0.0861 0.0861  -0.0031 300 GLN B CB  
2674 C CG  . GLN B 289 ? 0.8072 0.5672 0.5839 -0.0841 0.0749  -0.0062 300 GLN B CG  
2675 C CD  . GLN B 289 ? 0.9675 0.7101 0.7420 -0.0830 0.0641  0.0052  300 GLN B CD  
2676 O OE1 . GLN B 289 ? 1.0294 0.7427 0.7621 -0.0814 0.0570  0.0161  300 GLN B OE1 
2677 N NE2 . GLN B 289 ? 0.8909 0.6486 0.7082 -0.0833 0.0616  0.0025  300 GLN B NE2 
2678 N N   . MET B 290 ? 0.9135 0.6171 0.5541 -0.0879 0.1338  -0.0169 301 MET B N   
2679 C CA  . MET B 290 ? 1.1321 0.8009 0.7039 -0.0873 0.1442  -0.0182 301 MET B CA  
2680 C C   . MET B 290 ? 1.1657 0.8200 0.7189 -0.0921 0.1781  -0.0062 301 MET B C   
2681 O O   . MET B 290 ? 1.1353 0.8134 0.7352 -0.0946 0.2026  -0.0052 301 MET B O   
2682 C CB  . MET B 290 ? 1.0210 0.6927 0.5884 -0.0827 0.1501  -0.0360 301 MET B CB  
2683 C CG  . MET B 290 ? 1.0611 0.7691 0.6949 -0.0808 0.1657  -0.0436 301 MET B CG  
2684 S SD  . MET B 290 ? 1.3775 1.0835 1.0057 -0.0743 0.1627  -0.0638 301 MET B SD  
2685 C CE  . MET B 290 ? 1.1464 0.8914 0.8487 -0.0710 0.1886  -0.0673 301 MET B CE  
2686 N N   . ASN B 291 ? 1.3510 0.9676 0.8372 -0.0940 0.1793  0.0043  302 ASN B N   
2687 C CA  . ASN B 291 ? 1.5101 1.1109 0.9725 -0.0993 0.2144  0.0174  302 ASN B CA  
2688 C C   . ASN B 291 ? 1.6280 1.2219 1.0625 -0.0949 0.2458  0.0057  302 ASN B C   
2689 O O   . ASN B 291 ? 1.6869 1.2478 1.0521 -0.0909 0.2422  -0.0016 302 ASN B O   
2690 C CB  . ASN B 291 ? 1.6625 1.2232 1.0600 -0.1030 0.2050  0.0351  302 ASN B CB  
2691 C CG  . ASN B 291 ? 1.8011 1.3314 1.1309 -0.0981 0.1781  0.0286  302 ASN B CG  
2692 O OD1 . ASN B 291 ? 1.7880 1.3310 1.1318 -0.0933 0.1560  0.0125  302 ASN B OD1 
2693 N ND2 . ASN B 291 ? 1.8138 1.3030 1.0693 -0.1006 0.1785  0.0424  302 ASN B ND2 
2694 N N   . LEU B 292 ? 1.5489 1.1733 1.0384 -0.0949 0.2756  0.0032  303 LEU B N   
2695 C CA  . LEU B 292 ? 1.6379 1.2577 1.1076 -0.0884 0.3111  -0.0066 303 LEU B CA  
2696 C C   . LEU B 292 ? 1.7946 1.3788 1.1930 -0.0910 0.3402  0.0057  303 LEU B C   
2697 O O   . LEU B 292 ? 1.7790 1.3522 1.1465 -0.0841 0.3731  -0.0022 303 LEU B O   
2698 C CB  . LEU B 292 ? 1.4692 1.1339 1.0211 -0.0872 0.3358  -0.0090 303 LEU B CB  
2699 C CG  . LEU B 292 ? 1.4227 1.0938 0.9815 -0.0747 0.3451  -0.0300 303 LEU B CG  
2700 C CD1 . LEU B 292 ? 1.3754 1.0347 0.9164 -0.0710 0.3044  -0.0450 303 LEU B CD1 
2701 C CD2 . LEU B 292 ? 1.2579 0.9770 0.9055 -0.0726 0.3617  -0.0313 303 LEU B CD2 
2702 N N   . GLN B 293 ? 2.0542 1.6205 1.4284 -0.1001 0.3309  0.0258  304 GLN B N   
2703 C CA  . GLN B 293 ? 2.2368 1.7620 1.5299 -0.1033 0.3512  0.0397  304 GLN B CA  
2704 C C   . GLN B 293 ? 2.2648 1.7529 1.4766 -0.0945 0.3413  0.0228  304 GLN B C   
2705 O O   . GLN B 293 ? 2.2330 1.7042 1.4170 -0.0935 0.2996  0.0174  304 GLN B O   
2706 C CB  . GLN B 293 ? 2.1769 1.6826 1.4521 -0.1129 0.3290  0.0622  304 GLN B CB  
2707 N N   . GLN B 294 ? 2.1264 1.6088 1.3151 -0.0867 0.3740  0.0140  305 GLN B N   
2708 C CA  . GLN B 294 ? 2.1288 1.6027 1.2982 -0.0747 0.3706  -0.0118 305 GLN B CA  
2709 C C   . GLN B 294 ? 2.1897 1.6305 1.3023 -0.0743 0.3267  -0.0243 305 GLN B C   
2710 O O   . GLN B 294 ? 2.2711 1.6752 1.3126 -0.0740 0.3119  -0.0227 305 GLN B O   
2711 C CB  . GLN B 294 ? 2.1514 1.6144 1.2901 -0.0657 0.4027  -0.0151 305 GLN B CB  
2712 C CG  . GLN B 294 ? 2.0993 1.6046 1.3097 -0.0635 0.4447  -0.0074 305 GLN B CG  
2713 C CD  . GLN B 294 ? 2.2136 1.7141 1.4029 -0.0514 0.4781  -0.0144 305 GLN B CD  
2714 O OE1 . GLN B 294 ? 2.3040 1.7649 1.4167 -0.0459 0.4726  -0.0229 305 GLN B OE1 
2715 N NE2 . GLN B 294 ? 2.1257 1.6675 1.3845 -0.0470 0.5119  -0.0107 305 GLN B NE2 
2716 N N   . GLN B 295 ? 2.1933 1.6546 1.3514 -0.0742 0.3006  -0.0358 306 GLN B N   
2717 C CA  . GLN B 295 ? 2.2123 1.6500 1.3315 -0.0721 0.2632  -0.0529 306 GLN B CA  
2718 C C   . GLN B 295 ? 2.2365 1.6628 1.3405 -0.0614 0.2845  -0.0745 306 GLN B C   
2719 O O   . GLN B 295 ? 2.1522 1.6079 1.3148 -0.0550 0.3114  -0.0817 306 GLN B O   
2720 C CB  . GLN B 295 ? 2.0070 1.4818 1.2016 -0.0742 0.2246  -0.0563 306 GLN B CB  
2721 N N   . PRO B 296 ? 2.3259 1.7148 1.3643 -0.0583 0.2703  -0.0838 307 PRO B N   
2722 C CA  . PRO B 296 ? 2.3379 1.7159 1.3643 -0.0465 0.2952  -0.1004 307 PRO B CA  
2723 C C   . PRO B 296 ? 2.3304 1.7279 1.4113 -0.0399 0.2948  -0.1194 307 PRO B C   
2724 O O   . PRO B 296 ? 2.3063 1.7099 1.4078 -0.0453 0.2619  -0.1261 307 PRO B O   
2725 C CB  . PRO B 296 ? 2.4595 1.7911 1.4034 -0.0476 0.2686  -0.1074 307 PRO B CB  
2726 C CG  . PRO B 296 ? 2.5284 1.8550 1.4622 -0.0590 0.2202  -0.1008 307 PRO B CG  
2727 C CD  . PRO B 296 ? 2.4024 1.7587 1.3792 -0.0651 0.2275  -0.0806 307 PRO B CD  
2728 N N   . LYS B 297 ? 2.3435 1.7526 1.4508 -0.0277 0.3323  -0.1267 308 LYS B N   
2729 C CA  . LYS B 297 ? 2.2579 1.6926 1.4304 -0.0191 0.3414  -0.1403 308 LYS B CA  
2730 C C   . LYS B 297 ? 2.1322 1.6108 1.3797 -0.0255 0.3400  -0.1308 308 LYS B C   
2731 O O   . LYS B 297 ? 1.9796 1.4665 1.2546 -0.0294 0.3132  -0.1391 308 LYS B O   
2732 C CB  . LYS B 297 ? 2.2374 1.6445 1.3864 -0.0172 0.3094  -0.1614 308 LYS B CB  
2733 C CG  . LYS B 297 ? 2.1947 1.5599 1.2772 -0.0093 0.3147  -0.1739 308 LYS B CG  
2734 C CD  . LYS B 297 ? 2.1618 1.5389 1.2703 0.0074  0.3605  -0.1789 308 LYS B CD  
2735 C CE  . LYS B 297 ? 2.0654 1.4647 1.2414 0.0158  0.3617  -0.1911 308 LYS B CE  
2736 N NZ  . LYS B 297 ? 2.1230 1.4879 1.2692 0.0151  0.3279  -0.2105 308 LYS B NZ  
2737 N N   . LYS B 298 ? 2.0254 1.5321 1.3063 -0.0278 0.3689  -0.1126 309 LYS B N   
2738 C CA  . LYS B 298 ? 1.8500 1.4022 1.2096 -0.0339 0.3713  -0.1026 309 LYS B CA  
2739 C C   . LYS B 298 ? 1.7281 1.3145 1.1630 -0.0231 0.3870  -0.1127 309 LYS B C   
2740 O O   . LYS B 298 ? 1.6064 1.2310 1.1147 -0.0268 0.3645  -0.1097 309 LYS B O   
2741 C CB  . LYS B 298 ? 1.6565 1.2273 1.0320 -0.0416 0.3960  -0.0790 309 LYS B CB  
2742 N N   . GLU B 299 ? 1.7914 1.3726 1.2237 -0.0091 0.4142  -0.1204 310 GLU B N   
2743 C CA  . GLU B 299 ? 1.7421 1.3541 1.2455 0.0033  0.4287  -0.1285 310 GLU B CA  
2744 C C   . GLU B 299 ? 1.7202 1.3241 1.2349 0.0050  0.3989  -0.1457 310 GLU B C   
2745 O O   . GLU B 299 ? 1.6115 1.2512 1.2012 0.0090  0.3993  -0.1464 310 GLU B O   
2746 C CB  . GLU B 299 ? 1.8031 1.4061 1.2939 0.0195  0.4592  -0.1341 310 GLU B CB  
2747 C CG  . GLU B 299 ? 1.8960 1.5119 1.3840 0.0186  0.4921  -0.1167 310 GLU B CG  
2748 C CD  . GLU B 299 ? 2.0575 1.6287 1.4520 0.0132  0.4897  -0.1141 310 GLU B CD  
2749 O OE1 . GLU B 299 ? 2.1531 1.6807 1.4810 0.0128  0.4640  -0.1282 310 GLU B OE1 
2750 O OE2 . GLU B 299 ? 2.1581 1.7386 1.5477 0.0088  0.5123  -0.0970 310 GLU B OE2 
2751 N N   . LEU B 300 ? 1.8441 1.4036 1.2908 0.0011  0.3690  -0.1580 311 LEU B N   
2752 C CA  . LEU B 300 ? 1.7335 1.2897 1.1999 -0.0003 0.3355  -0.1707 311 LEU B CA  
2753 C C   . LEU B 300 ? 1.6013 1.2041 1.1353 -0.0129 0.3041  -0.1550 311 LEU B C   
2754 O O   . LEU B 300 ? 1.4535 1.0845 1.0505 -0.0114 0.2898  -0.1565 311 LEU B O   
2755 C CB  . LEU B 300 ? 1.8635 1.3668 1.2496 -0.0050 0.3049  -0.1845 311 LEU B CB  
2756 C CG  . LEU B 300 ? 1.9840 1.4486 1.3188 0.0061  0.3126  -0.1978 311 LEU B CG  
2757 C CD1 . LEU B 300 ? 2.0083 1.4312 1.2823 -0.0035 0.2705  -0.2083 311 LEU B CD1 
2758 C CD2 . LEU B 300 ? 1.9564 1.4317 1.3407 0.0221  0.3313  -0.2086 311 LEU B CD2 
2759 N N   . ILE B 301 ? 1.5520 1.1613 1.0720 -0.0244 0.2941  -0.1396 312 ILE B N   
2760 C CA  . ILE B 301 ? 1.4435 1.0939 1.0236 -0.0347 0.2676  -0.1255 312 ILE B CA  
2761 C C   . ILE B 301 ? 1.3127 1.0116 0.9765 -0.0314 0.2883  -0.1170 312 ILE B C   
2762 O O   . ILE B 301 ? 1.1628 0.8954 0.8878 -0.0341 0.2682  -0.1142 312 ILE B O   
2763 C CB  . ILE B 301 ? 1.4436 1.0845 0.9869 -0.0454 0.2562  -0.1110 312 ILE B CB  
2764 C CG1 . ILE B 301 ? 1.5624 1.1509 1.0140 -0.0471 0.2419  -0.1190 312 ILE B CG1 
2765 C CG2 . ILE B 301 ? 1.2645 0.9362 0.8549 -0.0542 0.2218  -0.1012 312 ILE B CG2 
2766 C CD1 . ILE B 301 ? 1.6367 1.2074 1.0392 -0.0546 0.2393  -0.1038 312 ILE B CD1 
2767 N N   . ILE B 302 ? 1.3351 1.0389 1.0023 -0.0261 0.3284  -0.1119 313 ILE B N   
2768 C CA  . ILE B 302 ? 1.2653 1.0169 1.0145 -0.0238 0.3486  -0.1027 313 ILE B CA  
2769 C C   . ILE B 302 ? 1.2434 1.0106 1.0403 -0.0121 0.3478  -0.1140 313 ILE B C   
2770 O O   . ILE B 302 ? 1.1731 0.9791 1.0390 -0.0146 0.3326  -0.1084 313 ILE B O   
2771 C CB  . ILE B 302 ? 1.2785 1.0318 1.0201 -0.0207 0.3941  -0.0940 313 ILE B CB  
2772 C CG1 . ILE B 302 ? 1.3286 1.0741 1.0399 -0.0350 0.3919  -0.0773 313 ILE B CG1 
2773 C CG2 . ILE B 302 ? 1.1663 0.9690 0.9957 -0.0159 0.4169  -0.0868 313 ILE B CG2 
2774 C CD1 . ILE B 302 ? 1.2805 1.0246 0.9774 -0.0345 0.4371  -0.0661 313 ILE B CD1 
2775 N N   . ASN B 303 ? 1.3173 1.0513 1.0751 0.0014  0.3639  -0.1302 314 ASN B N   
2776 C CA  . ASN B 303 ? 1.3260 1.0694 1.1270 0.0144  0.3648  -0.1406 314 ASN B CA  
2777 C C   . ASN B 303 ? 1.1914 0.9418 1.0148 0.0071  0.3208  -0.1427 314 ASN B C   
2778 O O   . ASN B 303 ? 1.0461 0.8290 0.9359 0.0106  0.3134  -0.1396 314 ASN B O   
2779 C CB  . ASN B 303 ? 1.3493 1.0450 1.0926 0.0302  0.3873  -0.1597 314 ASN B CB  
2780 C CG  . ASN B 303 ? 1.4732 1.1732 1.2117 0.0408  0.4312  -0.1549 314 ASN B CG  
2781 O OD1 . ASN B 303 ? 1.5053 1.2520 1.3107 0.0417  0.4501  -0.1401 314 ASN B OD1 
2782 N ND2 . ASN B 303 ? 1.5861 1.2428 1.2513 0.0469  0.4387  -0.1639 314 ASN B ND2 
2783 N N   . GLU B 304 ? 1.2637 0.9850 1.0330 -0.0031 0.2914  -0.1468 315 GLU B N   
2784 C CA  . GLU B 304 ? 1.1469 0.8790 0.9383 -0.0119 0.2509  -0.1460 315 GLU B CA  
2785 C C   . GLU B 304 ? 1.0777 0.8620 0.9408 -0.0185 0.2404  -0.1306 315 GLU B C   
2786 O O   . GLU B 304 ? 0.9613 0.7669 0.8690 -0.0190 0.2213  -0.1296 315 GLU B O   
2787 C CB  . GLU B 304 ? 1.2925 0.9947 1.0220 -0.0233 0.2232  -0.1479 315 GLU B CB  
2788 C CG  . GLU B 304 ? 1.2232 0.9418 0.9777 -0.0334 0.1831  -0.1442 315 GLU B CG  
2789 C CD  . GLU B 304 ? 1.3543 1.0613 1.1203 -0.0301 0.1692  -0.1550 315 GLU B CD  
2790 O OE1 . GLU B 304 ? 1.4722 1.1471 1.2126 -0.0199 0.1865  -0.1685 315 GLU B OE1 
2791 O OE2 . GLU B 304 ? 1.2641 0.9925 1.0636 -0.0375 0.1418  -0.1497 315 GLU B OE2 
2792 N N   . ILE B 305 ? 0.9812 0.7836 0.8528 -0.0246 0.2516  -0.1183 316 ILE B N   
2793 C CA  . ILE B 305 ? 0.8634 0.7109 0.7994 -0.0314 0.2422  -0.1054 316 ILE B CA  
2794 C C   . ILE B 305 ? 0.8025 0.6815 0.8038 -0.0225 0.2584  -0.1038 316 ILE B C   
2795 O O   . ILE B 305 ? 0.7642 0.6733 0.8166 -0.0248 0.2400  -0.0993 316 ILE B O   
2796 C CB  . ILE B 305 ? 0.8457 0.6991 0.7735 -0.0407 0.2508  -0.0929 316 ILE B CB  
2797 C CG1 . ILE B 305 ? 0.7296 0.5554 0.6007 -0.0486 0.2277  -0.0926 316 ILE B CG1 
2798 C CG2 . ILE B 305 ? 0.7284 0.6245 0.7224 -0.0477 0.2430  -0.0815 316 ILE B CG2 
2799 C CD1 . ILE B 305 ? 0.9384 0.7622 0.7946 -0.0569 0.2344  -0.0797 316 ILE B CD1 
2800 N N   . LEU B 306 ? 0.8749 0.7478 0.8749 -0.0116 0.2933  -0.1068 317 LEU B N   
2801 C CA  . LEU B 306 ? 0.9703 0.8741 1.0359 -0.0006 0.3096  -0.1048 317 LEU B CA  
2802 C C   . LEU B 306 ? 0.8337 0.7354 0.9186 0.0064  0.2882  -0.1124 317 LEU B C   
2803 O O   . LEU B 306 ? 0.7748 0.7118 0.9229 0.0079  0.2791  -0.1053 317 LEU B O   
2804 C CB  . LEU B 306 ? 0.8893 0.7807 0.9423 0.0137  0.3525  -0.1095 317 LEU B CB  
2805 C CG  . LEU B 306 ? 1.0252 0.9342 1.0884 0.0099  0.3847  -0.0975 317 LEU B CG  
2806 C CD1 . LEU B 306 ? 0.9366 0.8282 0.9790 0.0272  0.4284  -0.1049 317 LEU B CD1 
2807 C CD2 . LEU B 306 ? 1.0763 1.0412 1.2277 0.0039  0.3819  -0.0821 317 LEU B CD2 
2808 N N   . VAL B 307 ? 0.7849 0.6439 0.8145 0.0094  0.2783  -0.1258 318 VAL B N   
2809 C CA  . VAL B 307 ? 0.8615 0.7127 0.9059 0.0150  0.2589  -0.1325 318 VAL B CA  
2810 C C   . VAL B 307 ? 0.7067 0.5865 0.7848 0.0025  0.2239  -0.1226 318 VAL B C   
2811 O O   . VAL B 307 ? 0.7291 0.6297 0.8552 0.0066  0.2136  -0.1184 318 VAL B O   
2812 C CB  . VAL B 307 ? 0.9112 0.7067 0.8852 0.0174  0.2534  -0.1490 318 VAL B CB  
2813 C CG1 . VAL B 307 ? 0.9789 0.7641 0.9668 0.0186  0.2283  -0.1537 318 VAL B CG1 
2814 C CG2 . VAL B 307 ? 0.9934 0.7584 0.9339 0.0331  0.2906  -0.1608 318 VAL B CG2 
2815 N N   . MET B 308 ? 0.7030 0.5836 0.7557 -0.0116 0.2059  -0.1183 319 MET B N   
2816 C CA  . MET B 308 ? 0.6830 0.5884 0.7621 -0.0218 0.1752  -0.1103 319 MET B CA  
2817 C C   . MET B 308 ? 0.7395 0.6898 0.8827 -0.0225 0.1758  -0.0987 319 MET B C   
2818 O O   . MET B 308 ? 0.6385 0.6086 0.8137 -0.0246 0.1557  -0.0938 319 MET B O   
2819 C CB  . MET B 308 ? 0.6664 0.5636 0.7072 -0.0340 0.1580  -0.1083 319 MET B CB  
2820 C CG  . MET B 308 ? 0.8185 0.6749 0.8002 -0.0360 0.1472  -0.1183 319 MET B CG  
2821 S SD  . MET B 308 ? 0.8444 0.7016 0.8005 -0.0494 0.1161  -0.1132 319 MET B SD  
2822 C CE  . MET B 308 ? 0.6525 0.5411 0.6570 -0.0535 0.0909  -0.1070 319 MET B CE  
2823 N N   . ARG B 309 ? 0.6459 0.6128 0.8081 -0.0222 0.1975  -0.0932 320 ARG B N   
2824 C CA  . ARG B 309 ? 0.6469 0.6563 0.8719 -0.0250 0.1945  -0.0822 320 ARG B CA  
2825 C C   . ARG B 309 ? 0.6476 0.6732 0.9199 -0.0136 0.1956  -0.0810 320 ARG B C   
2826 O O   . ARG B 309 ? 0.6048 0.6601 0.9205 -0.0169 0.1779  -0.0729 320 ARG B O   
2827 C CB  . ARG B 309 ? 0.7635 0.7894 1.0079 -0.0282 0.2180  -0.0751 320 ARG B CB  
2828 C CG  . ARG B 309 ? 0.8190 0.8397 1.0366 -0.0417 0.2120  -0.0708 320 ARG B CG  
2829 C CD  . ARG B 309 ? 0.9445 0.9900 1.1989 -0.0488 0.2284  -0.0600 320 ARG B CD  
2830 N NE  . ARG B 309 ? 1.0884 1.1253 1.3181 -0.0623 0.2171  -0.0556 320 ARG B NE  
2831 C CZ  . ARG B 309 ? 0.9627 1.0102 1.2095 -0.0726 0.2267  -0.0460 320 ARG B CZ  
2832 N NH1 . ARG B 309 ? 1.0377 1.1102 1.3312 -0.0728 0.2488  -0.0384 320 ARG B NH1 
2833 N NH2 . ARG B 309 ? 0.7805 0.8131 0.9994 -0.0830 0.2136  -0.0433 320 ARG B NH2 
2834 N N   . GLU B 310 ? 0.5732 0.5774 0.8356 0.0006  0.2154  -0.0891 321 GLU B N   
2835 C CA  . GLU B 310 ? 0.6887 0.7069 0.9996 0.0143  0.2197  -0.0871 321 GLU B CA  
2836 C C   . GLU B 310 ? 0.7392 0.7400 1.0417 0.0167  0.1955  -0.0905 321 GLU B C   
2837 O O   . GLU B 310 ? 0.7735 0.7874 1.1190 0.0264  0.1915  -0.0858 321 GLU B O   
2838 C CB  . GLU B 310 ? 0.7778 0.7802 1.0850 0.0313  0.2562  -0.0946 321 GLU B CB  
2839 C CG  . GLU B 310 ? 0.8509 0.8739 1.1726 0.0294  0.2849  -0.0886 321 GLU B CG  
2840 C CD  . GLU B 310 ? 1.2127 1.2125 1.5123 0.0459  0.3245  -0.0978 321 GLU B CD  
2841 O OE1 . GLU B 310 ? 1.2775 1.2467 1.5582 0.0610  0.3292  -0.1097 321 GLU B OE1 
2842 O OE2 . GLU B 310 ? 1.1835 1.1929 1.4815 0.0438  0.3517  -0.0933 321 GLU B OE2 
2843 N N   . ASN B 311 ? 0.6075 0.5804 0.8584 0.0073  0.1781  -0.0967 322 ASN B N   
2844 C CA  . ASN B 311 ? 0.5682 0.5188 0.8057 0.0080  0.1580  -0.1002 322 ASN B CA  
2845 C C   . ASN B 311 ? 0.5346 0.4916 0.7548 -0.0084 0.1294  -0.0953 322 ASN B C   
2846 O O   . ASN B 311 ? 0.5818 0.5118 0.7575 -0.0152 0.1193  -0.1018 322 ASN B O   
2847 C CB  . ASN B 311 ? 0.5763 0.4771 0.7644 0.0156  0.1700  -0.1157 322 ASN B CB  
2848 C CG  . ASN B 311 ? 0.7684 0.6610 0.9702 0.0345  0.2025  -0.1219 322 ASN B CG  
2849 O OD1 . ASN B 311 ? 0.7957 0.6875 1.0309 0.0480  0.2057  -0.1214 322 ASN B OD1 
2850 N ND2 . ASN B 311 ? 0.8121 0.6993 0.9892 0.0363  0.2279  -0.1266 322 ASN B ND2 
2851 N N   . LYS B 312 ? 0.5000 0.4937 0.7570 -0.0143 0.1154  -0.0836 323 LYS B N   
2852 C CA  . LYS B 312 ? 0.5137 0.5172 0.7588 -0.0273 0.0912  -0.0785 323 LYS B CA  
2853 C C   . LYS B 312 ? 0.3883 0.3859 0.6390 -0.0282 0.0723  -0.0743 323 LYS B C   
2854 O O   . LYS B 312 ? 0.4457 0.4376 0.7192 -0.0188 0.0747  -0.0727 323 LYS B O   
2855 C CB  . LYS B 312 ? 0.5399 0.5803 0.8142 -0.0334 0.0851  -0.0694 323 LYS B CB  
2856 C CG  . LYS B 312 ? 0.5313 0.5747 0.7974 -0.0361 0.1011  -0.0719 323 LYS B CG  
2857 C CD  . LYS B 312 ? 0.6230 0.6966 0.9140 -0.0441 0.0916  -0.0643 323 LYS B CD  
2858 C CE  . LYS B 312 ? 0.5166 0.5875 0.7938 -0.0495 0.1046  -0.0657 323 LYS B CE  
2859 N NZ  . LYS B 312 ? 0.6097 0.7053 0.9103 -0.0583 0.0932  -0.0596 323 LYS B NZ  
2860 N N   . ASN B 313 ? 0.4438 0.4414 0.6734 -0.0392 0.0541  -0.0719 324 ASN B N   
2861 C CA  . ASN B 313 ? 0.3340 0.3251 0.5658 -0.0429 0.0370  -0.0663 324 ASN B CA  
2862 C C   . ASN B 313 ? 0.3589 0.3703 0.5838 -0.0546 0.0201  -0.0590 324 ASN B C   
2863 O O   . ASN B 313 ? 0.3251 0.3382 0.5280 -0.0596 0.0207  -0.0631 324 ASN B O   
2864 C CB  . ASN B 313 ? 0.4026 0.3521 0.6042 -0.0424 0.0376  -0.0759 324 ASN B CB  
2865 C CG  . ASN B 313 ? 0.4320 0.3725 0.6382 -0.0484 0.0195  -0.0687 324 ASN B CG  
2866 O OD1 . ASN B 313 ? 0.3835 0.3269 0.5754 -0.0606 0.0048  -0.0650 324 ASN B OD1 
2867 N ND2 . ASN B 313 ? 0.3913 0.3219 0.6204 -0.0398 0.0206  -0.0652 324 ASN B ND2 
2868 N N   . PRO B 314 ? 0.3474 0.3740 0.5898 -0.0582 0.0062  -0.0476 325 PRO B N   
2869 C CA  . PRO B 314 ? 0.3152 0.3638 0.5514 -0.0675 -0.0060 -0.0406 325 PRO B CA  
2870 C C   . PRO B 314 ? 0.3277 0.3643 0.5370 -0.0756 -0.0118 -0.0441 325 PRO B C   
2871 O O   . PRO B 314 ? 0.3193 0.3742 0.5215 -0.0801 -0.0161 -0.0420 325 PRO B O   
2872 C CB  . PRO B 314 ? 0.3691 0.4291 0.6249 -0.0693 -0.0177 -0.0269 325 PRO B CB  
2873 C CG  . PRO B 314 ? 0.4558 0.5113 0.7366 -0.0591 -0.0122 -0.0258 325 PRO B CG  
2874 C CD  . PRO B 314 ? 0.4015 0.4283 0.6713 -0.0525 0.0023  -0.0393 325 PRO B CD  
2875 N N   . ASN B 315 ? 0.3112 0.3168 0.5053 -0.0772 -0.0128 -0.0499 326 ASN B N   
2876 C CA  . ASN B 315 ? 0.3230 0.3180 0.4941 -0.0868 -0.0224 -0.0522 326 ASN B CA  
2877 C C   . ASN B 315 ? 0.3434 0.3163 0.4836 -0.0847 -0.0152 -0.0653 326 ASN B C   
2878 O O   . ASN B 315 ? 0.3655 0.3196 0.4826 -0.0919 -0.0246 -0.0694 326 ASN B O   
2879 C CB  . ASN B 315 ? 0.3463 0.3200 0.5179 -0.0940 -0.0337 -0.0487 326 ASN B CB  
2880 C CG  . ASN B 315 ? 0.3870 0.3853 0.5835 -0.0996 -0.0429 -0.0322 326 ASN B CG  
2881 O OD1 . ASN B 315 ? 0.3361 0.3265 0.5482 -0.0969 -0.0440 -0.0260 326 ASN B OD1 
2882 N ND2 . ASN B 315 ? 0.3065 0.3350 0.5063 -0.1062 -0.0486 -0.0242 326 ASN B ND2 
2883 N N   . ILE B 316 ? 0.3391 0.3144 0.4784 -0.0762 0.0002  -0.0707 327 ILE B N   
2884 C CA  . ILE B 316 ? 0.3727 0.3304 0.4811 -0.0744 0.0090  -0.0803 327 ILE B CA  
2885 C C   . ILE B 316 ? 0.3947 0.3787 0.5109 -0.0732 0.0135  -0.0765 327 ILE B C   
2886 O O   . ILE B 316 ? 0.3500 0.3559 0.4937 -0.0696 0.0187  -0.0719 327 ILE B O   
2887 C CB  . ILE B 316 ? 0.3901 0.3194 0.4871 -0.0651 0.0274  -0.0905 327 ILE B CB  
2888 C CG1 . ILE B 316 ? 0.4327 0.3276 0.5149 -0.0661 0.0213  -0.0967 327 ILE B CG1 
2889 C CG2 . ILE B 316 ? 0.4967 0.4104 0.5598 -0.0633 0.0396  -0.0981 327 ILE B CG2 
2890 C CD1 . ILE B 316 ? 0.5573 0.4233 0.6302 -0.0542 0.0409  -0.1075 327 ILE B CD1 
2891 N N   . VAL B 317 ? 0.3387 0.3175 0.4296 -0.0761 0.0104  -0.0786 328 VAL B N   
2892 C CA  . VAL B 317 ? 0.3377 0.3343 0.4318 -0.0749 0.0138  -0.0757 328 VAL B CA  
2893 C C   . VAL B 317 ? 0.3988 0.3961 0.5036 -0.0695 0.0323  -0.0778 328 VAL B C   
2894 O O   . VAL B 317 ? 0.4258 0.4012 0.5146 -0.0660 0.0465  -0.0837 328 VAL B O   
2895 C CB  . VAL B 317 ? 0.4090 0.3927 0.4712 -0.0773 0.0081  -0.0773 328 VAL B CB  
2896 C CG1 . VAL B 317 ? 0.3941 0.3882 0.4576 -0.0747 0.0140  -0.0749 328 VAL B CG1 
2897 C CG2 . VAL B 317 ? 0.3975 0.3921 0.4616 -0.0828 -0.0114 -0.0724 328 VAL B CG2 
2898 N N   . ASN B 318 ? 0.3773 0.4001 0.5098 -0.0691 0.0322  -0.0728 329 ASN B N   
2899 C CA  . ASN B 318 ? 0.4278 0.4574 0.5820 -0.0658 0.0465  -0.0727 329 ASN B CA  
2900 C C   . ASN B 318 ? 0.4171 0.4351 0.5539 -0.0664 0.0596  -0.0749 329 ASN B C   
2901 O O   . ASN B 318 ? 0.3276 0.3452 0.4498 -0.0694 0.0536  -0.0735 329 ASN B O   
2902 C CB  . ASN B 318 ? 0.4231 0.4814 0.6084 -0.0674 0.0381  -0.0668 329 ASN B CB  
2903 C CG  . ASN B 318 ? 0.5456 0.6159 0.7621 -0.0655 0.0484  -0.0649 329 ASN B CG  
2904 O OD1 . ASN B 318 ? 0.4799 0.5441 0.7078 -0.0603 0.0603  -0.0661 329 ASN B OD1 
2905 N ND2 . ASN B 318 ? 0.5074 0.5946 0.7390 -0.0695 0.0433  -0.0622 329 ASN B ND2 
2906 N N   . TYR B 319 ? 0.3797 0.3878 0.5187 -0.0627 0.0786  -0.0773 330 TYR B N   
2907 C CA  . TYR B 319 ? 0.3708 0.3701 0.4974 -0.0641 0.0946  -0.0767 330 TYR B CA  
2908 C C   . TYR B 319 ? 0.4569 0.4815 0.6225 -0.0676 0.0973  -0.0708 330 TYR B C   
2909 O O   . TYR B 319 ? 0.4156 0.4602 0.6192 -0.0653 0.0983  -0.0686 330 TYR B O   
2910 C CB  . TYR B 319 ? 0.4609 0.4392 0.5714 -0.0581 0.1167  -0.0816 330 TYR B CB  
2911 C CG  . TYR B 319 ? 0.5233 0.4966 0.6276 -0.0596 0.1383  -0.0786 330 TYR B CG  
2912 C CD1 . TYR B 319 ? 0.5840 0.5292 0.6392 -0.0615 0.1445  -0.0798 330 TYR B CD1 
2913 C CD2 . TYR B 319 ? 0.5462 0.5435 0.6942 -0.0602 0.1516  -0.0728 330 TYR B CD2 
2914 C CE1 . TYR B 319 ? 0.7163 0.6559 0.7641 -0.0638 0.1657  -0.0747 330 TYR B CE1 
2915 C CE2 . TYR B 319 ? 0.6221 0.6170 0.7681 -0.0636 0.1719  -0.0679 330 TYR B CE2 
2916 C CZ  . TYR B 319 ? 0.6514 0.6168 0.7467 -0.0653 0.1806  -0.0685 330 TYR B CZ  
2917 O OH  . TYR B 319 ? 0.6846 0.6478 0.7788 -0.0694 0.2030  -0.0613 330 TYR B OH  
2918 N N   . LEU B 320 ? 0.3922 0.4144 0.5490 -0.0734 0.0971  -0.0679 331 LEU B N   
2919 C CA  . LEU B 320 ? 0.3939 0.4365 0.5855 -0.0794 0.0960  -0.0630 331 LEU B CA  
2920 C C   . LEU B 320 ? 0.5413 0.5821 0.7439 -0.0831 0.1177  -0.0585 331 LEU B C   
2921 O O   . LEU B 320 ? 0.4873 0.5494 0.7316 -0.0840 0.1258  -0.0548 331 LEU B O   
2922 C CB  . LEU B 320 ? 0.3267 0.3675 0.5063 -0.0840 0.0787  -0.0629 331 LEU B CB  
2923 C CG  . LEU B 320 ? 0.4510 0.4987 0.6237 -0.0804 0.0597  -0.0657 331 LEU B CG  
2924 C CD1 . LEU B 320 ? 0.3789 0.4223 0.5367 -0.0819 0.0473  -0.0665 331 LEU B CD1 
2925 C CD2 . LEU B 320 ? 0.4578 0.5297 0.6645 -0.0800 0.0523  -0.0644 331 LEU B CD2 
2926 N N   . ASP B 321 ? 0.3888 0.4058 0.5563 -0.0854 0.1276  -0.0571 332 ASP B N   
2927 C CA  . ASP B 321 ? 0.5086 0.5250 0.6870 -0.0915 0.1483  -0.0501 332 ASP B CA  
2928 C C   . ASP B 321 ? 0.5361 0.5199 0.6625 -0.0910 0.1606  -0.0487 332 ASP B C   
2929 O O   . ASP B 321 ? 0.5600 0.5237 0.6459 -0.0871 0.1486  -0.0531 332 ASP B O   
2930 C CB  . ASP B 321 ? 0.5515 0.5797 0.7572 -0.1025 0.1372  -0.0449 332 ASP B CB  
2931 C CG  . ASP B 321 ? 0.6792 0.7332 0.9372 -0.1091 0.1494  -0.0380 332 ASP B CG  
2932 O OD1 . ASP B 321 ? 0.7805 0.8361 1.0453 -0.1075 0.1755  -0.0334 332 ASP B OD1 
2933 O OD2 . ASP B 321 ? 0.7405 0.8142 1.0334 -0.1156 0.1328  -0.0372 332 ASP B OD2 
2934 N N   . SER B 322 ? 0.5990 0.5787 0.7275 -0.0958 0.1841  -0.0412 333 SER B N   
2935 C CA  . SER B 322 ? 0.5496 0.4966 0.6255 -0.0970 0.1956  -0.0373 333 SER B CA  
2936 C C   . SER B 322 ? 0.6169 0.5645 0.7076 -0.1083 0.2118  -0.0246 333 SER B C   
2937 O O   . SER B 322 ? 0.5501 0.5253 0.6934 -0.1142 0.2208  -0.0196 333 SER B O   
2938 C CB  . SER B 322 ? 0.6205 0.5500 0.6608 -0.0875 0.2154  -0.0427 333 SER B CB  
2939 O OG  . SER B 322 ? 0.8367 0.7865 0.9135 -0.0840 0.2410  -0.0417 333 SER B OG  
2940 N N   . TYR B 323 ? 0.5789 0.4958 0.6244 -0.1124 0.2130  -0.0181 334 TYR B N   
2941 C CA  . TYR B 323 ? 0.6162 0.5264 0.6691 -0.1251 0.2245  -0.0041 334 TYR B CA  
2942 C C   . TYR B 323 ? 0.6245 0.5000 0.6177 -0.1247 0.2424  0.0036  334 TYR B C   
2943 O O   . TYR B 323 ? 0.6933 0.5435 0.6341 -0.1169 0.2314  -0.0017 334 TYR B O   
2944 C CB  . TYR B 323 ? 0.5370 0.4408 0.5985 -0.1323 0.1977  -0.0023 334 TYR B CB  
2945 C CG  . TYR B 323 ? 0.6809 0.6135 0.7894 -0.1323 0.1770  -0.0110 334 TYR B CG  
2946 C CD1 . TYR B 323 ? 0.5921 0.5292 0.6913 -0.1217 0.1562  -0.0227 334 TYR B CD1 
2947 C CD2 . TYR B 323 ? 0.7285 0.6836 0.8898 -0.1440 0.1774  -0.0065 334 TYR B CD2 
2948 C CE1 . TYR B 323 ? 0.6376 0.5993 0.7739 -0.1217 0.1386  -0.0294 334 TYR B CE1 
2949 C CE2 . TYR B 323 ? 0.6495 0.6282 0.8473 -0.1442 0.1566  -0.0143 334 TYR B CE2 
2950 C CZ  . TYR B 323 ? 0.7015 0.6826 0.8842 -0.1325 0.1383  -0.0256 334 TYR B CZ  
2951 O OH  . TYR B 323 ? 0.6908 0.6937 0.9039 -0.1327 0.1187  -0.0323 334 TYR B OH  
2952 N N   . LEU B 324 ? 0.6384 0.5132 0.6391 -0.1340 0.2696  0.0172  335 LEU B N   
2953 C CA  . LEU B 324 ? 0.6967 0.5357 0.6384 -0.1366 0.2858  0.0284  335 LEU B CA  
2954 C C   . LEU B 324 ? 0.7521 0.5730 0.6929 -0.1489 0.2704  0.0409  335 LEU B C   
2955 O O   . LEU B 324 ? 0.8248 0.6613 0.8132 -0.1621 0.2757  0.0501  335 LEU B O   
2956 C CB  . LEU B 324 ? 0.8033 0.6507 0.7504 -0.1391 0.3279  0.0375  335 LEU B CB  
2957 C CG  . LEU B 324 ? 1.0179 0.8270 0.8881 -0.1357 0.3490  0.0437  335 LEU B CG  
2958 C CD1 . LEU B 324 ? 1.0550 0.8459 0.8740 -0.1199 0.3390  0.0262  335 LEU B CD1 
2959 C CD2 . LEU B 324 ? 1.0851 0.9060 0.9669 -0.1393 0.3946  0.0551  335 LEU B CD2 
2960 N N   . VAL B 325 ? 0.7665 0.5539 0.6557 -0.1444 0.2497  0.0412  336 VAL B N   
2961 C CA  . VAL B 325 ? 0.8248 0.5876 0.7059 -0.1527 0.2336  0.0526  336 VAL B CA  
2962 C C   . VAL B 325 ? 0.8978 0.6202 0.7119 -0.1536 0.2453  0.0670  336 VAL B C   
2963 O O   . VAL B 325 ? 0.9401 0.6380 0.7029 -0.1438 0.2281  0.0641  336 VAL B O   
2964 C CB  . VAL B 325 ? 0.8463 0.6061 0.7296 -0.1445 0.1969  0.0418  336 VAL B CB  
2965 C CG1 . VAL B 325 ? 0.8723 0.6067 0.7557 -0.1519 0.1825  0.0524  336 VAL B CG1 
2966 C CG2 . VAL B 325 ? 0.6643 0.4629 0.6011 -0.1411 0.1862  0.0261  336 VAL B CG2 
2967 N N   . GLY B 326 ? 0.9994 0.7157 0.8140 -0.1659 0.2741  0.0839  337 GLY B N   
2968 C CA  . GLY B 326 ? 0.9566 0.6338 0.7051 -0.1684 0.2887  0.1004  337 GLY B CA  
2969 C C   . GLY B 326 ? 0.9581 0.6234 0.6468 -0.1556 0.2985  0.0921  337 GLY B C   
2970 O O   . GLY B 326 ? 0.9981 0.6308 0.6264 -0.1487 0.2799  0.0927  337 GLY B O   
2971 N N   . ASP B 327 ? 1.0331 0.7236 0.7384 -0.1521 0.3264  0.0838  338 ASP B N   
2972 C CA  . ASP B 327 ? 1.3108 0.9881 0.9604 -0.1395 0.3379  0.0726  338 ASP B CA  
2973 C C   . ASP B 327 ? 1.1433 0.8111 0.7671 -0.1276 0.3016  0.0553  338 ASP B C   
2974 O O   . ASP B 327 ? 1.2732 0.9188 0.8379 -0.1191 0.3024  0.0469  338 ASP B O   
2975 C CB  . ASP B 327 ? 1.3639 1.0019 0.9378 -0.1426 0.3615  0.0882  338 ASP B CB  
2976 C CG  . ASP B 327 ? 1.4240 1.0781 1.0167 -0.1488 0.4095  0.0989  338 ASP B CG  
2977 O OD1 . ASP B 327 ? 1.4627 1.1520 1.1019 -0.1429 0.4283  0.0869  338 ASP B OD1 
2978 O OD2 . ASP B 327 ? 1.5793 1.2131 1.1451 -0.1593 0.4280  0.1204  338 ASP B OD2 
2979 N N   . GLU B 328 ? 1.1365 0.8200 0.8027 -0.1276 0.2697  0.0503  339 GLU B N   
2980 C CA  . GLU B 328 ? 1.0207 0.7099 0.6845 -0.1170 0.2392  0.0332  339 GLU B CA  
2981 C C   . GLU B 328 ? 0.9290 0.6602 0.6589 -0.1143 0.2431  0.0195  339 GLU B C   
2982 O O   . GLU B 328 ? 0.8647 0.6214 0.6518 -0.1217 0.2522  0.0243  339 GLU B O   
2983 C CB  . GLU B 328 ? 1.1297 0.8103 0.7957 -0.1159 0.2023  0.0362  339 GLU B CB  
2984 C CG  . GLU B 328 ? 1.1822 0.8220 0.7805 -0.1141 0.1878  0.0469  339 GLU B CG  
2985 C CD  . GLU B 328 ? 1.1960 0.8343 0.8052 -0.1088 0.1504  0.0469  339 GLU B CD  
2986 O OE1 . GLU B 328 ? 1.1472 0.8148 0.8129 -0.1069 0.1387  0.0379  339 GLU B OE1 
2987 O OE2 . GLU B 328 ? 1.3049 0.9133 0.8661 -0.1056 0.1328  0.0561  339 GLU B OE2 
2988 N N   . LEU B 329 ? 0.8796 0.6161 0.6007 -0.1046 0.2359  0.0034  340 LEU B N   
2989 C CA  . LEU B 329 ? 0.7339 0.5072 0.5139 -0.1007 0.2346  -0.0090 340 LEU B CA  
2990 C C   . LEU B 329 ? 0.6984 0.4816 0.4957 -0.0977 0.1976  -0.0161 340 LEU B C   
2991 O O   . LEU B 329 ? 0.7810 0.5455 0.5381 -0.0929 0.1772  -0.0207 340 LEU B O   
2992 C CB  . LEU B 329 ? 0.8032 0.5743 0.5654 -0.0916 0.2521  -0.0218 340 LEU B CB  
2993 C CG  . LEU B 329 ? 0.7866 0.5920 0.6064 -0.0860 0.2487  -0.0338 340 LEU B CG  
2994 C CD1 . LEU B 329 ? 0.7631 0.6036 0.6505 -0.0919 0.2653  -0.0258 340 LEU B CD1 
2995 C CD2 . LEU B 329 ? 0.9256 0.7196 0.7203 -0.0755 0.2642  -0.0470 340 LEU B CD2 
2996 N N   . TRP B 330 ? 0.6375 0.4500 0.4934 -0.1010 0.1889  -0.0165 341 TRP B N   
2997 C CA  . TRP B 330 ? 0.5951 0.4215 0.4715 -0.0971 0.1584  -0.0238 341 TRP B CA  
2998 C C   . TRP B 330 ? 0.5555 0.4115 0.4712 -0.0928 0.1587  -0.0352 341 TRP B C   
2999 O O   . TRP B 330 ? 0.6059 0.4847 0.5648 -0.0959 0.1736  -0.0343 341 TRP B O   
3000 C CB  . TRP B 330 ? 0.5989 0.4323 0.5058 -0.1028 0.1459  -0.0176 341 TRP B CB  
3001 C CG  . TRP B 330 ? 0.7122 0.5150 0.5850 -0.1057 0.1404  -0.0061 341 TRP B CG  
3002 C CD1 . TRP B 330 ? 0.7142 0.4854 0.5331 -0.1059 0.1488  0.0024  341 TRP B CD1 
3003 C CD2 . TRP B 330 ? 0.6371 0.4342 0.5245 -0.1080 0.1244  -0.0014 341 TRP B CD2 
3004 N NE1 . TRP B 330 ? 0.7306 0.4779 0.5323 -0.1083 0.1381  0.0139  341 TRP B NE1 
3005 C CE2 . TRP B 330 ? 0.7499 0.5117 0.5940 -0.1090 0.1234  0.0111  341 TRP B CE2 
3006 C CE3 . TRP B 330 ? 0.7480 0.5633 0.6773 -0.1086 0.1106  -0.0071 341 TRP B CE3 
3007 C CZ2 . TRP B 330 ? 0.7705 0.5143 0.6160 -0.1098 0.1093  0.0183  341 TRP B CZ2 
3008 C CZ3 . TRP B 330 ? 0.6492 0.4454 0.5765 -0.1094 0.0975  -0.0019 341 TRP B CZ3 
3009 C CH2 . TRP B 330 ? 0.6975 0.4581 0.5852 -0.1096 0.0972  0.0107  341 TRP B CH2 
3010 N N   . VAL B 331 ? 0.5449 0.4007 0.4476 -0.0863 0.1414  -0.0444 342 VAL B N   
3011 C CA  . VAL B 331 ? 0.5117 0.3909 0.4472 -0.0820 0.1388  -0.0539 342 VAL B CA  
3012 C C   . VAL B 331 ? 0.4693 0.3688 0.4329 -0.0817 0.1132  -0.0556 342 VAL B C   
3013 O O   . VAL B 331 ? 0.5409 0.4310 0.4827 -0.0801 0.0942  -0.0548 342 VAL B O   
3014 C CB  . VAL B 331 ? 0.5400 0.4009 0.4393 -0.0763 0.1388  -0.0629 342 VAL B CB  
3015 C CG1 . VAL B 331 ? 0.5330 0.4149 0.4667 -0.0721 0.1331  -0.0713 342 VAL B CG1 
3016 C CG2 . VAL B 331 ? 0.5866 0.4247 0.4520 -0.0748 0.1673  -0.0627 342 VAL B CG2 
3017 N N   . VAL B 332 ? 0.4329 0.3607 0.4444 -0.0829 0.1128  -0.0571 343 VAL B N   
3018 C CA  . VAL B 332 ? 0.4074 0.3540 0.4430 -0.0827 0.0917  -0.0585 343 VAL B CA  
3019 C C   . VAL B 332 ? 0.4171 0.3822 0.4717 -0.0786 0.0839  -0.0645 343 VAL B C   
3020 O O   . VAL B 332 ? 0.3646 0.3422 0.4444 -0.0779 0.0947  -0.0660 343 VAL B O   
3021 C CB  . VAL B 332 ? 0.4170 0.3775 0.4867 -0.0888 0.0931  -0.0548 343 VAL B CB  
3022 C CG1 . VAL B 332 ? 0.3799 0.3535 0.4630 -0.0871 0.0719  -0.0580 343 VAL B CG1 
3023 C CG2 . VAL B 332 ? 0.4137 0.3524 0.4657 -0.0947 0.1028  -0.0471 343 VAL B CG2 
3024 N N   . MET B 333 ? 0.3628 0.3299 0.4072 -0.0757 0.0655  -0.0666 344 MET B N   
3025 C CA  . MET B 333 ? 0.3420 0.3245 0.4019 -0.0735 0.0560  -0.0701 344 MET B CA  
3026 C C   . MET B 333 ? 0.3329 0.3368 0.4124 -0.0729 0.0404  -0.0688 344 MET B C   
3027 O O   . MET B 333 ? 0.3662 0.3671 0.4382 -0.0723 0.0345  -0.0670 344 MET B O   
3028 C CB  . MET B 333 ? 0.3755 0.3414 0.4050 -0.0721 0.0483  -0.0729 344 MET B CB  
3029 C CG  . MET B 333 ? 0.4025 0.3387 0.3961 -0.0719 0.0620  -0.0756 344 MET B CG  
3030 S SD  . MET B 333 ? 0.4845 0.4202 0.4946 -0.0687 0.0841  -0.0805 344 MET B SD  
3031 C CE  . MET B 333 ? 0.3999 0.3376 0.4166 -0.0673 0.0688  -0.0859 344 MET B CE  
3032 N N   . GLU B 334 ? 0.3433 0.3666 0.4457 -0.0724 0.0345  -0.0694 345 GLU B N   
3033 C CA  . GLU B 334 ? 0.3082 0.3506 0.4216 -0.0711 0.0209  -0.0681 345 GLU B CA  
3034 C C   . GLU B 334 ? 0.3251 0.3637 0.4195 -0.0688 0.0103  -0.0667 345 GLU B C   
3035 O O   . GLU B 334 ? 0.3393 0.3647 0.4166 -0.0699 0.0086  -0.0670 345 GLU B O   
3036 C CB  . GLU B 334 ? 0.3594 0.4209 0.4963 -0.0716 0.0168  -0.0667 345 GLU B CB  
3037 C CG  . GLU B 334 ? 0.3160 0.3725 0.4478 -0.0719 0.0137  -0.0662 345 GLU B CG  
3038 C CD  . GLU B 334 ? 0.3924 0.4671 0.5459 -0.0727 0.0070  -0.0622 345 GLU B CD  
3039 O OE1 . GLU B 334 ? 0.5106 0.6041 0.6758 -0.0724 0.0017  -0.0594 345 GLU B OE1 
3040 O OE2 . GLU B 334 ? 0.3665 0.4337 0.5224 -0.0734 0.0069  -0.0617 345 GLU B OE2 
3041 N N   . TYR B 335 ? 0.3178 0.3682 0.4157 -0.0652 0.0027  -0.0654 346 TYR B N   
3042 C CA  . TYR B 335 ? 0.3256 0.3787 0.4138 -0.0615 -0.0074 -0.0626 346 TYR B CA  
3043 C C   . TYR B 335 ? 0.3170 0.3963 0.4233 -0.0613 -0.0146 -0.0594 346 TYR B C   
3044 O O   . TYR B 335 ? 0.3019 0.3972 0.4222 -0.0599 -0.0130 -0.0597 346 TYR B O   
3045 C CB  . TYR B 335 ? 0.3407 0.3884 0.4218 -0.0551 -0.0090 -0.0625 346 TYR B CB  
3046 C CG  . TYR B 335 ? 0.3950 0.4500 0.4730 -0.0488 -0.0196 -0.0582 346 TYR B CG  
3047 C CD1 . TYR B 335 ? 0.3667 0.4081 0.4275 -0.0504 -0.0266 -0.0547 346 TYR B CD1 
3048 C CD2 . TYR B 335 ? 0.4831 0.5589 0.5753 -0.0408 -0.0228 -0.0573 346 TYR B CD2 
3049 C CE1 . TYR B 335 ? 0.4089 0.4603 0.4723 -0.0451 -0.0389 -0.0492 346 TYR B CE1 
3050 C CE2 . TYR B 335 ? 0.3857 0.4728 0.4822 -0.0338 -0.0314 -0.0520 346 TYR B CE2 
3051 C CZ  . TYR B 335 ? 0.4495 0.5257 0.5343 -0.0364 -0.0407 -0.0473 346 TYR B CZ  
3052 O OH  . TYR B 335 ? 0.4540 0.5445 0.5480 -0.0298 -0.0520 -0.0405 346 TYR B OH  
3053 N N   . LEU B 336 ? 0.4857 0.3063 0.3449 -0.1640 0.0689  -0.0660 347 LEU B N   
3054 C CA  . LEU B 336 ? 0.4627 0.3009 0.3368 -0.1470 0.0581  -0.0630 347 LEU B CA  
3055 C C   . LEU B 336 ? 0.5252 0.3196 0.3759 -0.1305 0.0646  -0.0594 347 LEU B C   
3056 O O   . LEU B 336 ? 0.5287 0.3094 0.3778 -0.1121 0.0659  -0.0512 347 LEU B O   
3057 C CB  . LEU B 336 ? 0.4346 0.3121 0.3414 -0.1309 0.0465  -0.0560 347 LEU B CB  
3058 C CG  . LEU B 336 ? 0.5057 0.4329 0.4398 -0.1410 0.0367  -0.0592 347 LEU B CG  
3059 C CD1 . LEU B 336 ? 0.5199 0.4604 0.4554 -0.1621 0.0422  -0.0648 347 LEU B CD1 
3060 C CD2 . LEU B 336 ? 0.5553 0.5139 0.5185 -0.1221 0.0258  -0.0521 347 LEU B CD2 
3061 N N   . ALA B 337 ? 0.5102 0.2845 0.3423 -0.1370 0.0687  -0.0657 348 ALA B N   
3062 C CA  . ALA B 337 ? 0.5972 0.3250 0.4026 -0.1236 0.0781  -0.0641 348 ALA B CA  
3063 C C   . ALA B 337 ? 0.5849 0.3253 0.4040 -0.0980 0.0706  -0.0572 348 ALA B C   
3064 O O   . ALA B 337 ? 0.6153 0.3235 0.4163 -0.0827 0.0777  -0.0548 348 ALA B O   
3065 C CB  . ALA B 337 ? 0.6345 0.3411 0.4159 -0.1386 0.0862  -0.0732 348 ALA B CB  
3066 N N   . GLY B 338 ? 0.5139 0.2997 0.3636 -0.0930 0.0571  -0.0540 349 GLY B N   
3067 C CA  . GLY B 338 ? 0.4992 0.2968 0.3612 -0.0711 0.0507  -0.0474 349 GLY B CA  
3068 C C   . GLY B 338 ? 0.4943 0.2882 0.3618 -0.0515 0.0502  -0.0380 349 GLY B C   
3069 O O   . GLY B 338 ? 0.4684 0.2717 0.3446 -0.0338 0.0459  -0.0326 349 GLY B O   
3070 N N   . GLY B 339 ? 0.4988 0.2817 0.3610 -0.0553 0.0545  -0.0360 350 GLY B N   
3071 C CA  . GLY B 339 ? 0.4785 0.2595 0.3438 -0.0380 0.0536  -0.0271 350 GLY B CA  
3072 C C   . GLY B 339 ? 0.4607 0.2819 0.3554 -0.0347 0.0422  -0.0239 350 GLY B C   
3073 O O   . GLY B 339 ? 0.4391 0.2892 0.3528 -0.0449 0.0353  -0.0277 350 GLY B O   
3074 N N   . SER B 340 ? 0.4141 0.2364 0.3114 -0.0193 0.0404  -0.0167 351 SER B N   
3075 C CA  . SER B 340 ? 0.3829 0.2370 0.3038 -0.0153 0.0313  -0.0141 351 SER B CA  
3076 C C   . SER B 340 ? 0.3412 0.2189 0.2800 -0.0053 0.0222  -0.0123 351 SER B C   
3077 O O   . SER B 340 ? 0.3947 0.2647 0.3268 0.0035  0.0232  -0.0108 351 SER B O   
3078 C CB  . SER B 340 ? 0.3936 0.2396 0.3072 -0.0054 0.0334  -0.0079 351 SER B CB  
3079 O OG  . SER B 340 ? 0.5283 0.3670 0.4350 0.0126  0.0328  -0.0016 351 SER B OG  
3080 N N   . LEU B 341 ? 0.3106 0.2162 0.2713 -0.0064 0.0141  -0.0124 352 LEU B N   
3081 C CA  . LEU B 341 ? 0.3025 0.2281 0.2785 0.0022  0.0061  -0.0099 352 LEU B CA  
3082 C C   . LEU B 341 ? 0.2992 0.2217 0.2700 0.0169  0.0060  -0.0044 352 LEU B C   
3083 O O   . LEU B 341 ? 0.3230 0.2550 0.2988 0.0242  0.0027  -0.0024 352 LEU B O   
3084 C CB  . LEU B 341 ? 0.2458 0.1955 0.2430 -0.0016 -0.0009 -0.0110 352 LEU B CB  
3085 C CG  . LEU B 341 ? 0.2454 0.2134 0.2579 0.0043  -0.0088 -0.0087 352 LEU B CG  
3086 C CD1 . LEU B 341 ? 0.2286 0.1996 0.2414 0.0023  -0.0108 -0.0088 352 LEU B CD1 
3087 C CD2 . LEU B 341 ? 0.2655 0.2500 0.2955 0.0011  -0.0136 -0.0101 352 LEU B CD2 
3088 N N   . THR B 342 ? 0.3063 0.2172 0.2661 0.0212  0.0098  -0.0016 353 THR B N   
3089 C CA  . THR B 342 ? 0.3050 0.2173 0.2598 0.0358  0.0087  0.0046  353 THR B CA  
3090 C C   . THR B 342 ? 0.3546 0.2561 0.2993 0.0466  0.0123  0.0073  353 THR B C   
3091 O O   . THR B 342 ? 0.3796 0.2978 0.3314 0.0573  0.0081  0.0106  353 THR B O   
3092 C CB  . THR B 342 ? 0.3791 0.2764 0.3185 0.0386  0.0134  0.0082  353 THR B CB  
3093 O OG1 . THR B 342 ? 0.3920 0.2985 0.3397 0.0281  0.0120  0.0046  353 THR B OG1 
3094 C CG2 . THR B 342 ? 0.4245 0.3316 0.3615 0.0539  0.0098  0.0152  353 THR B CG2 
3095 N N   . ASP B 343 ? 0.3673 0.2408 0.2944 0.0436  0.0208  0.0054  354 ASP B N   
3096 C CA  . ASP B 343 ? 0.4146 0.2738 0.3299 0.0546  0.0261  0.0068  354 ASP B CA  
3097 C C   . ASP B 343 ? 0.3689 0.2504 0.2995 0.0541  0.0211  0.0039  354 ASP B C   
3098 O O   . ASP B 343 ? 0.3994 0.2874 0.3303 0.0673  0.0218  0.0067  354 ASP B O   
3099 C CB  . ASP B 343 ? 0.4345 0.2558 0.3262 0.0477  0.0371  0.0031  354 ASP B CB  
3100 C CG  . ASP B 343 ? 0.6261 0.4192 0.4975 0.0501  0.0441  0.0077  354 ASP B CG  
3101 O OD1 . ASP B 343 ? 0.6024 0.4055 0.4763 0.0605  0.0404  0.0147  354 ASP B OD1 
3102 O OD2 . ASP B 343 ? 0.6923 0.4529 0.5435 0.0401  0.0534  0.0041  354 ASP B OD2 
3103 N N   . VAL B 344 ? 0.3566 0.2508 0.2994 0.0392  0.0165  -0.0013 355 VAL B N   
3104 C CA  . VAL B 344 ? 0.3323 0.2472 0.2881 0.0377  0.0115  -0.0029 355 VAL B CA  
3105 C C   . VAL B 344 ? 0.3401 0.2824 0.3125 0.0458  0.0041  0.0016  355 VAL B C   
3106 O O   . VAL B 344 ? 0.3544 0.3097 0.3313 0.0526  0.0034  0.0031  355 VAL B O   
3107 C CB  . VAL B 344 ? 0.3418 0.2652 0.3063 0.0213  0.0073  -0.0077 355 VAL B CB  
3108 C CG1 . VAL B 344 ? 0.3379 0.2859 0.3182 0.0198  0.0000  -0.0069 355 VAL B CG1 
3109 C CG2 . VAL B 344 ? 0.3335 0.2343 0.2805 0.0116  0.0146  -0.0135 355 VAL B CG2 
3110 N N   . VAL B 345 ? 0.3055 0.2574 0.2865 0.0440  -0.0007 0.0032  356 VAL B N   
3111 C CA  . VAL B 345 ? 0.2955 0.2728 0.2913 0.0477  -0.0077 0.0058  356 VAL B CA  
3112 C C   . VAL B 345 ? 0.3476 0.3317 0.3390 0.0626  -0.0063 0.0106  356 VAL B C   
3113 O O   . VAL B 345 ? 0.3512 0.3585 0.3534 0.0657  -0.0102 0.0120  356 VAL B O   
3114 C CB  . VAL B 345 ? 0.3355 0.3175 0.3376 0.0423  -0.0116 0.0051  356 VAL B CB  
3115 C CG1 . VAL B 345 ? 0.3970 0.4007 0.4082 0.0465  -0.0173 0.0073  356 VAL B CG1 
3116 C CG2 . VAL B 345 ? 0.3797 0.3648 0.3925 0.0301  -0.0146 0.0011  356 VAL B CG2 
3117 N N   . THR B 346 ? 0.3155 0.2800 0.2905 0.0723  -0.0002 0.0137  357 THR B N   
3118 C CA  . THR B 346 ? 0.4061 0.3797 0.3775 0.0895  0.0005  0.0198  357 THR B CA  
3119 C C   . THR B 346 ? 0.4306 0.4014 0.3975 0.1000  0.0063  0.0202  357 THR B C   
3120 O O   . THR B 346 ? 0.4540 0.4433 0.4244 0.1145  0.0057  0.0249  357 THR B O   
3121 C CB  . THR B 346 ? 0.4308 0.3836 0.3845 0.0983  0.0047  0.0249  357 THR B CB  
3122 O OG1 . THR B 346 ? 0.5907 0.5064 0.5258 0.0962  0.0140  0.0230  357 THR B OG1 
3123 C CG2 . THR B 346 ? 0.3820 0.3411 0.3393 0.0895  -0.0004 0.0246  357 THR B CG2 
3124 N N   . GLU B 347 ? 0.4010 0.3528 0.3611 0.0927  0.0116  0.0150  358 GLU B N   
3125 C CA  . GLU B 347 ? 0.3882 0.3323 0.3401 0.1028  0.0191  0.0142  358 GLU B CA  
3126 C C   . GLU B 347 ? 0.3658 0.3278 0.3290 0.0937  0.0170  0.0095  358 GLU B C   
3127 O O   . GLU B 347 ? 0.3996 0.3589 0.3571 0.1012  0.0235  0.0079  358 GLU B O   
3128 C CB  . GLU B 347 ? 0.4420 0.3427 0.3693 0.1032  0.0299  0.0116  358 GLU B CB  
3129 C CG  . GLU B 347 ? 0.4215 0.2994 0.3332 0.1136  0.0338  0.0177  358 GLU B CG  
3130 C CD  . GLU B 347 ? 0.5467 0.4353 0.4574 0.1382  0.0350  0.0261  358 GLU B CD  
3131 O OE1 . GLU B 347 ? 0.5305 0.4397 0.4502 0.1482  0.0355  0.0261  358 GLU B OE1 
3132 O OE2 . GLU B 347 ? 0.6955 0.5737 0.5962 0.1478  0.0354  0.0332  358 GLU B OE2 
3133 N N   . THR B 348 ? 0.3193 0.2980 0.2970 0.0785  0.0088  0.0076  359 THR B N   
3134 C CA  . THR B 348 ? 0.3377 0.3325 0.3245 0.0693  0.0063  0.0049  359 THR B CA  
3135 C C   . THR B 348 ? 0.3401 0.3631 0.3459 0.0628  -0.0031 0.0072  359 THR B C   
3136 O O   . THR B 348 ? 0.3265 0.3531 0.3373 0.0622  -0.0077 0.0090  359 THR B O   
3137 C CB  . THR B 348 ? 0.3816 0.3597 0.3617 0.0544  0.0069  -0.0003 359 THR B CB  
3138 O OG1 . THR B 348 ? 0.3333 0.3150 0.3228 0.0438  -0.0003 -0.0001 359 THR B OG1 
3139 C CG2 . THR B 348 ? 0.4075 0.3522 0.3661 0.0563  0.0164  -0.0041 359 THR B CG2 
3140 N N   . CYS B 349 ? 0.3099 0.3510 0.3245 0.0565  -0.0055 0.0068  360 CYS B N   
3141 C CA  . CYS B 349 ? 0.4091 0.4671 0.4379 0.0457  -0.0136 0.0081  360 CYS B CA  
3142 C C   . CYS B 349 ? 0.3940 0.4419 0.4219 0.0330  -0.0160 0.0064  360 CYS B C   
3143 O O   . CYS B 349 ? 0.4033 0.4503 0.4259 0.0299  -0.0133 0.0052  360 CYS B O   
3144 C CB  . CYS B 349 ? 0.4896 0.5765 0.5293 0.0459  -0.0154 0.0103  360 CYS B CB  
3145 S SG  . CYS B 349 ? 0.5884 0.6865 0.6248 0.0501  -0.0086 0.0097  360 CYS B SG  
3146 N N   . MET B 350 ? 0.2924 0.3338 0.3247 0.0267  -0.0207 0.0062  361 MET B N   
3147 C CA  . MET B 350 ? 0.3281 0.3635 0.3612 0.0168  -0.0239 0.0056  361 MET B CA  
3148 C C   . MET B 350 ? 0.2592 0.3079 0.3017 0.0102  -0.0290 0.0090  361 MET B C   
3149 O O   . MET B 350 ? 0.2909 0.3497 0.3410 0.0103  -0.0312 0.0104  361 MET B O   
3150 C CB  . MET B 350 ? 0.2367 0.2625 0.2723 0.0143  -0.0260 0.0042  361 MET B CB  
3151 C CG  . MET B 350 ? 0.2573 0.2674 0.2819 0.0191  -0.0203 0.0015  361 MET B CG  
3152 S SD  . MET B 350 ? 0.3012 0.3044 0.3299 0.0144  -0.0220 -0.0004 361 MET B SD  
3153 C CE  . MET B 350 ? 0.2391 0.2463 0.2727 0.0041  -0.0258 -0.0013 361 MET B CE  
3154 N N   . ASP B 351 ? 0.2498 0.2983 0.2898 0.0037  -0.0305 0.0104  362 ASP B N   
3155 C CA  . ASP B 351 ? 0.3109 0.3669 0.3571 -0.0029 -0.0351 0.0149  362 ASP B CA  
3156 C C   . ASP B 351 ? 0.2839 0.3327 0.3367 -0.0057 -0.0405 0.0167  362 ASP B C   
3157 O O   . ASP B 351 ? 0.2564 0.2983 0.3095 -0.0037 -0.0407 0.0141  362 ASP B O   
3158 C CB  . ASP B 351 ? 0.2985 0.3592 0.3374 -0.0078 -0.0342 0.0171  362 ASP B CB  
3159 C CG  . ASP B 351 ? 0.3833 0.4367 0.4144 -0.0111 -0.0353 0.0161  362 ASP B CG  
3160 O OD1 . ASP B 351 ? 0.3107 0.3598 0.3463 -0.0127 -0.0400 0.0172  362 ASP B OD1 
3161 O OD2 . ASP B 351 ? 0.3564 0.4106 0.3766 -0.0127 -0.0314 0.0139  362 ASP B OD2 
3162 N N   . GLU B 352 ? 0.2781 0.3277 0.3355 -0.0102 -0.0441 0.0213  363 GLU B N   
3163 C CA  . GLU B 352 ? 0.2111 0.2524 0.2751 -0.0100 -0.0481 0.0230  363 GLU B CA  
3164 C C   . GLU B 352 ? 0.2584 0.2984 0.3218 -0.0096 -0.0511 0.0249  363 GLU B C   
3165 O O   . GLU B 352 ? 0.2688 0.3055 0.3387 -0.0064 -0.0528 0.0239  363 GLU B O   
3166 C CB  . GLU B 352 ? 0.2645 0.3017 0.3305 -0.0149 -0.0501 0.0279  363 GLU B CB  
3167 C CG  . GLU B 352 ? 0.3096 0.3491 0.3782 -0.0174 -0.0480 0.0246  363 GLU B CG  
3168 C CD  . GLU B 352 ? 0.3461 0.3753 0.4150 -0.0241 -0.0491 0.0279  363 GLU B CD  
3169 O OE1 . GLU B 352 ? 0.3433 0.3599 0.4111 -0.0236 -0.0515 0.0334  363 GLU B OE1 
3170 O OE2 . GLU B 352 ? 0.2940 0.3276 0.3634 -0.0300 -0.0474 0.0250  363 GLU B OE2 
3171 N N   . GLY B 353 ? 0.2311 0.2762 0.2867 -0.0130 -0.0516 0.0271  364 GLY B N   
3172 C CA  . GLY B 353 ? 0.2580 0.3066 0.3124 -0.0141 -0.0552 0.0283  364 GLY B CA  
3173 C C   . GLY B 353 ? 0.2413 0.2895 0.2954 -0.0133 -0.0525 0.0211  364 GLY B C   
3174 O O   . GLY B 353 ? 0.2515 0.3041 0.3110 -0.0134 -0.0555 0.0209  364 GLY B O   
3175 N N   . GLN B 354 ? 0.2672 0.3104 0.3146 -0.0122 -0.0463 0.0155  365 GLN B N   
3176 C CA  . GLN B 354 ? 0.2282 0.2657 0.2725 -0.0120 -0.0423 0.0092  365 GLN B CA  
3177 C C   . GLN B 354 ? 0.2629 0.2979 0.3174 -0.0079 -0.0427 0.0082  365 GLN B C   
3178 O O   . GLN B 354 ? 0.2279 0.2630 0.2845 -0.0097 -0.0421 0.0051  365 GLN B O   
3179 C CB  . GLN B 354 ? 0.2165 0.2455 0.2491 -0.0094 -0.0350 0.0049  365 GLN B CB  
3180 C CG  . GLN B 354 ? 0.2774 0.3074 0.2977 -0.0135 -0.0326 0.0039  365 GLN B CG  
3181 C CD  . GLN B 354 ? 0.3250 0.3484 0.3356 -0.0076 -0.0249 0.0009  365 GLN B CD  
3182 O OE1 . GLN B 354 ? 0.3082 0.3349 0.3244 -0.0004 -0.0236 0.0028  365 GLN B OE1 
3183 N NE2 . GLN B 354 ? 0.2838 0.2993 0.2793 -0.0106 -0.0194 -0.0038 365 GLN B NE2 
3184 N N   . ILE B 355 ? 0.2342 0.2680 0.2942 -0.0038 -0.0432 0.0100  366 ILE B N   
3185 C CA  . ILE B 355 ? 0.2369 0.2679 0.3050 -0.0005 -0.0431 0.0083  366 ILE B CA  
3186 C C   . ILE B 355 ? 0.2649 0.2999 0.3430 -0.0004 -0.0472 0.0104  366 ILE B C   
3187 O O   . ILE B 355 ? 0.2639 0.2996 0.3473 0.0009  -0.0459 0.0072  366 ILE B O   
3188 C CB  . ILE B 355 ? 0.2272 0.2573 0.2975 0.0015  -0.0431 0.0090  366 ILE B CB  
3189 C CG1 . ILE B 355 ? 0.2719 0.3031 0.3347 0.0042  -0.0391 0.0071  366 ILE B CG1 
3190 C CG2 . ILE B 355 ? 0.2687 0.2949 0.3464 0.0036  -0.0434 0.0068  366 ILE B CG2 
3191 C CD1 . ILE B 355 ? 0.2564 0.2938 0.3219 0.0045  -0.0398 0.0077  366 ILE B CD1 
3192 N N   . ALA B 356 ? 0.2196 0.2578 0.3001 -0.0011 -0.0519 0.0163  367 ALA B N   
3193 C CA  . ALA B 356 ? 0.2278 0.2707 0.3179 0.0019  -0.0562 0.0201  367 ALA B CA  
3194 C C   . ALA B 356 ? 0.2430 0.2983 0.3356 -0.0002 -0.0570 0.0177  367 ALA B C   
3195 O O   . ALA B 356 ? 0.2113 0.2738 0.3146 0.0035  -0.0578 0.0171  367 ALA B O   
3196 C CB  . ALA B 356 ? 0.2000 0.2429 0.2886 0.0019  -0.0611 0.0286  367 ALA B CB  
3197 N N   . ALA B 357 ? 0.2015 0.2602 0.2840 -0.0069 -0.0560 0.0155  368 ALA B N   
3198 C CA  . ALA B 357 ? 0.2406 0.3108 0.3230 -0.0127 -0.0563 0.0119  368 ALA B CA  
3199 C C   . ALA B 357 ? 0.2639 0.3310 0.3492 -0.0131 -0.0507 0.0052  368 ALA B C   
3200 O O   . ALA B 357 ? 0.2310 0.3116 0.3259 -0.0143 -0.0516 0.0037  368 ALA B O   
3201 C CB  . ALA B 357 ? 0.2414 0.3103 0.3084 -0.0211 -0.0548 0.0094  368 ALA B CB  
3202 N N   . VAL B 358 ? 0.1946 0.2459 0.2719 -0.0118 -0.0448 0.0018  369 VAL B N   
3203 C CA  . VAL B 358 ? 0.2114 0.2573 0.2885 -0.0121 -0.0391 -0.0034 369 VAL B CA  
3204 C C   . VAL B 358 ? 0.1923 0.2452 0.2843 -0.0062 -0.0403 -0.0029 369 VAL B C   
3205 O O   . VAL B 358 ? 0.2098 0.2707 0.3078 -0.0083 -0.0379 -0.0063 369 VAL B O   
3206 C CB  . VAL B 358 ? 0.2047 0.2336 0.2700 -0.0091 -0.0338 -0.0050 369 VAL B CB  
3207 C CG1 . VAL B 358 ? 0.2124 0.2351 0.2765 -0.0083 -0.0284 -0.0087 369 VAL B CG1 
3208 C CG2 . VAL B 358 ? 0.2326 0.2519 0.2818 -0.0133 -0.0301 -0.0067 369 VAL B CG2 
3209 N N   . CYS B 359 ? 0.2081 0.2572 0.3055 0.0005  -0.0432 0.0008  370 CYS B N   
3210 C CA  . CYS B 359 ? 0.2320 0.2831 0.3413 0.0070  -0.0432 0.0005  370 CYS B CA  
3211 C C   . CYS B 359 ? 0.2381 0.3071 0.3607 0.0091  -0.0463 0.0024  370 CYS B C   
3212 O O   . CYS B 359 ? 0.2114 0.2877 0.3436 0.0124  -0.0433 -0.0009 370 CYS B O   
3213 C CB  . CYS B 359 ? 0.2268 0.2675 0.3369 0.0118  -0.0454 0.0042  370 CYS B CB  
3214 S SG  . CYS B 359 ? 0.2706 0.2980 0.3698 0.0101  -0.0418 0.0008  370 CYS B SG  
3215 N N   . ARG B 360 ? 0.2133 0.2923 0.3367 0.0077  -0.0522 0.0078  371 ARG B N   
3216 C CA  . ARG B 360 ? 0.2397 0.3409 0.3763 0.0107  -0.0565 0.0107  371 ARG B CA  
3217 C C   . ARG B 360 ? 0.2413 0.3592 0.3814 0.0030  -0.0531 0.0042  371 ARG B C   
3218 O O   . ARG B 360 ? 0.1923 0.3279 0.3472 0.0074  -0.0524 0.0031  371 ARG B O   
3219 C CB  . ARG B 360 ? 0.2385 0.3489 0.3722 0.0092  -0.0641 0.0182  371 ARG B CB  
3220 C CG  . ARG B 360 ? 0.2184 0.3563 0.3667 0.0142  -0.0701 0.0230  371 ARG B CG  
3221 C CD  . ARG B 360 ? 0.2628 0.4158 0.4055 0.0089  -0.0779 0.0289  371 ARG B CD  
3222 N NE  . ARG B 360 ? 0.3640 0.5202 0.4944 -0.0067 -0.0756 0.0216  371 ARG B NE  
3223 C CZ  . ARG B 360 ? 0.4576 0.6048 0.5717 -0.0144 -0.0766 0.0222  371 ARG B CZ  
3224 N NH1 . ARG B 360 ? 0.3204 0.4607 0.4295 -0.0095 -0.0811 0.0306  371 ARG B NH1 
3225 N NH2 . ARG B 360 ? 0.3846 0.5285 0.4859 -0.0274 -0.0721 0.0140  371 ARG B NH2 
3226 N N   . GLU B 361 ? 0.1640 0.2760 0.2902 -0.0086 -0.0500 -0.0004 372 GLU B N   
3227 C CA  . GLU B 361 ? 0.2130 0.3374 0.3392 -0.0190 -0.0458 -0.0068 372 GLU B CA  
3228 C C   . GLU B 361 ? 0.2439 0.3645 0.3751 -0.0165 -0.0385 -0.0116 372 GLU B C   
3229 O O   . GLU B 361 ? 0.2229 0.3636 0.3646 -0.0200 -0.0362 -0.0150 372 GLU B O   
3230 C CB  . GLU B 361 ? 0.1774 0.2872 0.2834 -0.0315 -0.0422 -0.0109 372 GLU B CB  
3231 C CG  . GLU B 361 ? 0.2099 0.3254 0.3087 -0.0365 -0.0483 -0.0079 372 GLU B CG  
3232 C CD  . GLU B 361 ? 0.2884 0.4368 0.3986 -0.0416 -0.0550 -0.0065 372 GLU B CD  
3233 O OE1 . GLU B 361 ? 0.2941 0.4564 0.4050 -0.0534 -0.0521 -0.0127 372 GLU B OE1 
3234 O OE2 . GLU B 361 ? 0.2616 0.4230 0.3795 -0.0342 -0.0632 0.0011  372 GLU B OE2 
3235 N N   . CYS B 362 ? 0.1811 0.2787 0.3048 -0.0109 -0.0349 -0.0121 373 CYS B N   
3236 C CA  . CYS B 362 ? 0.2427 0.3360 0.3687 -0.0084 -0.0281 -0.0165 373 CYS B CA  
3237 C C   . CYS B 362 ? 0.2430 0.3517 0.3881 0.0018  -0.0292 -0.0159 373 CYS B C   
3238 O O   . CYS B 362 ? 0.1959 0.3155 0.3486 0.0015  -0.0237 -0.0205 373 CYS B O   
3239 C CB  . CYS B 362 ? 0.2547 0.3234 0.3679 -0.0048 -0.0254 -0.0167 373 CYS B CB  
3240 S SG  . CYS B 362 ? 0.2851 0.3339 0.3753 -0.0129 -0.0213 -0.0178 373 CYS B SG  
3241 N N   . LEU B 363 ? 0.1898 0.2983 0.3420 0.0113  -0.0354 -0.0100 374 LEU B N   
3242 C CA  . LEU B 363 ? 0.2005 0.3203 0.3699 0.0235  -0.0359 -0.0086 374 LEU B CA  
3243 C C   . LEU B 363 ? 0.2317 0.3852 0.4172 0.0232  -0.0374 -0.0084 374 LEU B C   
3244 O O   . LEU B 363 ? 0.2008 0.3687 0.4009 0.0312  -0.0338 -0.0107 374 LEU B O   
3245 C CB  . LEU B 363 ? 0.1735 0.2816 0.3436 0.0332  -0.0418 -0.0011 374 LEU B CB  
3246 C CG  . LEU B 363 ? 0.2106 0.2899 0.3700 0.0352  -0.0387 -0.0028 374 LEU B CG  
3247 C CD1 . LEU B 363 ? 0.1942 0.2594 0.3497 0.0395  -0.0442 0.0048  374 LEU B CD1 
3248 C CD2 . LEU B 363 ? 0.2325 0.3071 0.3984 0.0429  -0.0320 -0.0085 374 LEU B CD2 
3249 N N   . GLN B 364 ? 0.1661 0.3346 0.3491 0.0135  -0.0424 -0.0064 375 GLN B N   
3250 C CA  . GLN B 364 ? 0.2156 0.4212 0.4138 0.0102  -0.0443 -0.0071 375 GLN B CA  
3251 C C   . GLN B 364 ? 0.2405 0.4557 0.4410 0.0011  -0.0351 -0.0160 375 GLN B C   
3252 O O   . GLN B 364 ? 0.2129 0.4576 0.4318 0.0050  -0.0331 -0.0178 375 GLN B O   
3253 C CB  . GLN B 364 ? 0.1726 0.3903 0.3637 -0.0017 -0.0512 -0.0046 375 GLN B CB  
3254 C CG  . GLN B 364 ? 0.1713 0.3863 0.3621 0.0079  -0.0608 0.0055  375 GLN B CG  
3255 C CD  . GLN B 364 ? 0.2910 0.5099 0.4685 -0.0050 -0.0664 0.0070  375 GLN B CD  
3256 O OE1 . GLN B 364 ? 0.3302 0.5509 0.4975 -0.0214 -0.0628 -0.0002 375 GLN B OE1 
3257 N NE2 . GLN B 364 ? 0.1821 0.3992 0.3570 0.0017  -0.0743 0.0161  375 GLN B NE2 
3258 N N   . ALA B 365 ? 0.2169 0.4076 0.3982 -0.0104 -0.0289 -0.0210 376 ALA B N   
3259 C CA  . ALA B 365 ? 0.2111 0.4055 0.3906 -0.0196 -0.0192 -0.0284 376 ALA B CA  
3260 C C   . ALA B 365 ? 0.1768 0.3713 0.3668 -0.0071 -0.0136 -0.0307 376 ALA B C   
3261 O O   . ALA B 365 ? 0.2331 0.4499 0.4344 -0.0094 -0.0074 -0.0354 376 ALA B O   
3262 C CB  . ALA B 365 ? 0.2085 0.3711 0.3625 -0.0313 -0.0139 -0.0312 376 ALA B CB  
3263 N N   . LEU B 366 ? 0.2342 0.4043 0.4198 0.0051  -0.0148 -0.0282 377 LEU B N   
3264 C CA  . LEU B 366 ? 0.2545 0.4201 0.4463 0.0159  -0.0086 -0.0318 377 LEU B CA  
3265 C C   . LEU B 366 ? 0.2640 0.4575 0.4801 0.0293  -0.0095 -0.0307 377 LEU B C   
3266 O O   . LEU B 366 ? 0.2073 0.4125 0.4330 0.0338  -0.0016 -0.0362 377 LEU B O   
3267 C CB  . LEU B 366 ? 0.2228 0.3559 0.4026 0.0231  -0.0101 -0.0302 377 LEU B CB  
3268 C CG  . LEU B 366 ? 0.1909 0.2994 0.3482 0.0134  -0.0077 -0.0319 377 LEU B CG  
3269 C CD1 . LEU B 366 ? 0.2521 0.3361 0.4004 0.0197  -0.0096 -0.0307 377 LEU B CD1 
3270 C CD2 . LEU B 366 ? 0.2823 0.3927 0.4334 0.0060  0.0018  -0.0383 377 LEU B CD2 
3271 N N   . GLU B 367 ? 0.2023 0.4065 0.4280 0.0371  -0.0185 -0.0230 378 GLU B N   
3272 C CA  . GLU B 367 ? 0.2366 0.4700 0.4860 0.0522  -0.0199 -0.0203 378 GLU B CA  
3273 C C   . GLU B 367 ? 0.2896 0.5638 0.5540 0.0446  -0.0156 -0.0253 378 GLU B C   
3274 O O   . GLU B 367 ? 0.2132 0.5085 0.4952 0.0554  -0.0097 -0.0285 378 GLU B O   
3275 C CB  . GLU B 367 ? 0.1922 0.4331 0.4470 0.0601  -0.0314 -0.0096 378 GLU B CB  
3276 C CG  . GLU B 367 ? 0.2638 0.5361 0.5429 0.0787  -0.0339 -0.0043 378 GLU B CG  
3277 C CD  . GLU B 367 ? 0.4117 0.6986 0.6949 0.0837  -0.0463 0.0073  378 GLU B CD  
3278 O OE1 . GLU B 367 ? 0.4676 0.7595 0.7405 0.0675  -0.0524 0.0085  378 GLU B OE1 
3279 O OE2 . GLU B 367 ? 0.5786 0.8657 0.8715 0.1026  -0.0492 0.0153  378 GLU B OE2 
3280 N N   . PHE B 368 ? 0.2131 0.4984 0.4700 0.0251  -0.0176 -0.0269 379 PHE B N   
3281 C CA  . PHE B 368 ? 0.2160 0.5394 0.4844 0.0128  -0.0130 -0.0325 379 PHE B CA  
3282 C C   . PHE B 368 ? 0.2182 0.5355 0.4840 0.0095  0.0002  -0.0411 379 PHE B C   
3283 O O   . PHE B 368 ? 0.2283 0.5783 0.5135 0.0142  0.0060  -0.0449 379 PHE B O   
3284 C CB  . PHE B 368 ? 0.1845 0.5104 0.4389 -0.0102 -0.0162 -0.0336 379 PHE B CB  
3285 C CG  . PHE B 368 ? 0.2713 0.6260 0.5300 -0.0291 -0.0089 -0.0412 379 PHE B CG  
3286 C CD1 . PHE B 368 ? 0.1932 0.5876 0.4691 -0.0288 -0.0112 -0.0395 379 PHE B CD1 
3287 C CD2 . PHE B 368 ? 0.1936 0.5226 0.4310 -0.0461 0.0008  -0.0475 379 PHE B CD2 
3288 C CE1 . PHE B 368 ? 0.2948 0.7066 0.5685 -0.0467 -0.0040 -0.0455 379 PHE B CE1 
3289 C CE2 . PHE B 368 ? 0.2669 0.6194 0.5060 -0.0654 0.0087  -0.0543 379 PHE B CE2 
3290 C CZ  . PHE B 368 ? 0.3387 0.7305 0.5944 -0.0658 0.0062  -0.0532 379 PHE B CZ  
3291 N N   . LEU B 369 ? 0.1980 0.4751 0.4398 0.0026  0.0050  -0.0438 380 LEU B N   
3292 C CA  . LEU B 369 ? 0.1709 0.4405 0.4064 -0.0016 0.0172  -0.0513 380 LEU B CA  
3293 C C   . LEU B 369 ? 0.2610 0.5351 0.5108 0.0179  0.0221  -0.0538 380 LEU B C   
3294 O O   . LEU B 369 ? 0.2190 0.5143 0.4789 0.0178  0.0317  -0.0600 380 LEU B O   
3295 C CB  . LEU B 369 ? 0.2286 0.4548 0.4349 -0.0099 0.0197  -0.0519 380 LEU B CB  
3296 C CG  . LEU B 369 ? 0.1901 0.4050 0.3777 -0.0293 0.0187  -0.0510 380 LEU B CG  
3297 C CD1 . LEU B 369 ? 0.2323 0.4052 0.3933 -0.0311 0.0208  -0.0500 380 LEU B CD1 
3298 C CD2 . LEU B 369 ? 0.2871 0.5260 0.4771 -0.0466 0.0270  -0.0565 380 LEU B CD2 
3299 N N   . HIS B 370 ? 0.2085 0.4605 0.4577 0.0341  0.0168  -0.0495 381 HIS B N   
3300 C CA  . HIS B 370 ? 0.2968 0.5447 0.5554 0.0526  0.0226  -0.0526 381 HIS B CA  
3301 C C   . HIS B 370 ? 0.2938 0.5842 0.5817 0.0660  0.0238  -0.0521 381 HIS B C   
3302 O O   . HIS B 370 ? 0.2350 0.5363 0.5331 0.0753  0.0339  -0.0585 381 HIS B O   
3303 C CB  . HIS B 370 ? 0.2352 0.4471 0.4841 0.0639  0.0166  -0.0478 381 HIS B CB  
3304 C CG  . HIS B 370 ? 0.1879 0.3634 0.4106 0.0528  0.0167  -0.0494 381 HIS B CG  
3305 N ND1 . HIS B 370 ? 0.2044 0.3487 0.4153 0.0572  0.0112  -0.0456 381 HIS B ND1 
3306 C CD2 . HIS B 370 ? 0.2199 0.3869 0.4258 0.0376  0.0216  -0.0537 381 HIS B CD2 
3307 C CE1 . HIS B 370 ? 0.3308 0.4532 0.5210 0.0460  0.0123  -0.0479 381 HIS B CE1 
3308 N NE2 . HIS B 370 ? 0.2428 0.3770 0.4289 0.0351  0.0184  -0.0523 381 HIS B NE2 
3309 N N   . SER B 371 ? 0.2505 0.5681 0.5522 0.0672  0.0139  -0.0446 382 SER B N   
3310 C CA  . SER B 371 ? 0.1831 0.5427 0.5101 0.0789  0.0141  -0.0415 382 SER B CA  
3311 C C   . SER B 371 ? 0.2961 0.6845 0.6292 0.0666  0.0241  -0.0487 382 SER B C   
3312 O O   . SER B 371 ? 0.3448 0.7560 0.6937 0.0774  0.0285  -0.0474 382 SER B O   
3313 C CB  . SER B 371 ? 0.3743 0.7521 0.7060 0.0756  0.0010  -0.0305 382 SER B CB  
3314 O OG  . SER B 371 ? 0.3450 0.7405 0.6705 0.0508  -0.0004 -0.0338 382 SER B OG  
3315 N N   . ASN B 372 ? 0.2455 0.6316 0.5656 0.0440  0.0286  -0.0560 383 ASN B N   
3316 C CA  . ASN B 372 ? 0.3026 0.7098 0.6231 0.0289  0.0392  -0.0630 383 ASN B CA  
3317 C C   . ASN B 372 ? 0.3217 0.7093 0.6322 0.0284  0.0527  -0.0731 383 ASN B C   
3318 O O   . ASN B 372 ? 0.3034 0.7004 0.6074 0.0118  0.0623  -0.0790 383 ASN B O   
3319 C CB  . ASN B 372 ? 0.3295 0.7432 0.6379 0.0016  0.0365  -0.0634 383 ASN B CB  
3320 C CG  . ASN B 372 ? 0.3981 0.8398 0.7164 -0.0015 0.0261  -0.0561 383 ASN B CG  
3321 O OD1 . ASN B 372 ? 0.4499 0.9218 0.7861 0.0070  0.0265  -0.0540 383 ASN B OD1 
3322 N ND2 . ASN B 372 ? 0.3361 0.7674 0.6428 -0.0129 0.0168  -0.0524 383 ASN B ND2 
3323 N N   . GLN B 373 ? 0.2756 0.6264 0.5768 0.0441  0.0528  -0.0730 384 GLN B N   
3324 C CA  . GLN B 373 ? 0.2792 0.6034 0.5643 0.0444  0.0643  -0.0808 384 GLN B CA  
3325 C C   . GLN B 373 ? 0.3533 0.6517 0.6094 0.0219  0.0671  -0.0825 384 GLN B C   
3326 O O   . GLN B 373 ? 0.3525 0.6450 0.5971 0.0153  0.0782  -0.0893 384 GLN B O   
3327 C CB  . GLN B 373 ? 0.3308 0.6888 0.6349 0.0521  0.0773  -0.0890 384 GLN B CB  
3328 C CG  . GLN B 373 ? 0.5461 0.9045 0.8653 0.0793  0.0763  -0.0853 384 GLN B CG  
3329 C CD  . GLN B 373 ? 0.5908 0.9770 0.9291 0.0867  0.0656  -0.0736 384 GLN B CD  
3330 O OE1 . GLN B 373 ? 0.6422 1.0601 0.9877 0.0723  0.0630  -0.0711 384 GLN B OE1 
3331 N NE2 . GLN B 373 ? 0.6174 0.9891 0.9618 0.1080  0.0594  -0.0661 384 GLN B NE2 
3332 N N   . VAL B 374 ? 0.2750 0.5561 0.5176 0.0112  0.0575  -0.0760 385 VAL B N   
3333 C CA  . VAL B 374 ? 0.2923 0.5432 0.5057 -0.0062 0.0593  -0.0758 385 VAL B CA  
3334 C C   . VAL B 374 ? 0.2664 0.4765 0.4621 0.0017  0.0530  -0.0724 385 VAL B C   
3335 O O   . VAL B 374 ? 0.3594 0.5627 0.5604 0.0102  0.0429  -0.0667 385 VAL B O   
3336 C CB  . VAL B 374 ? 0.2617 0.5197 0.4700 -0.0243 0.0546  -0.0719 385 VAL B CB  
3337 C CG1 . VAL B 374 ? 0.3635 0.5833 0.5397 -0.0378 0.0563  -0.0702 385 VAL B CG1 
3338 C CG2 . VAL B 374 ? 0.3001 0.6000 0.5240 -0.0365 0.0615  -0.0762 385 VAL B CG2 
3339 N N   . ILE B 375 ? 0.2578 0.4426 0.4318 -0.0022 0.0589  -0.0756 386 ILE B N   
3340 C CA  . ILE B 375 ? 0.2804 0.4300 0.4355 0.0016  0.0531  -0.0727 386 ILE B CA  
3341 C C   . ILE B 375 ? 0.3770 0.5079 0.5088 -0.0126 0.0513  -0.0680 386 ILE B C   
3342 O O   . ILE B 375 ? 0.4021 0.5305 0.5197 -0.0236 0.0595  -0.0700 386 ILE B O   
3343 C CB  . ILE B 375 ? 0.3452 0.4808 0.4910 0.0079  0.0598  -0.0794 386 ILE B CB  
3344 C CG1 . ILE B 375 ? 0.3193 0.4714 0.4873 0.0231  0.0642  -0.0849 386 ILE B CG1 
3345 C CG2 . ILE B 375 ? 0.2997 0.4038 0.4267 0.0097  0.0529  -0.0765 386 ILE B CG2 
3346 C CD1 . ILE B 375 ? 0.4572 0.5968 0.6156 0.0280  0.0733  -0.0939 386 ILE B CD1 
3347 N N   . HIS B 376 ? 0.2932 0.4089 0.4196 -0.0117 0.0415  -0.0616 387 HIS B N   
3348 C CA  . HIS B 376 ? 0.2852 0.3829 0.3906 -0.0230 0.0405  -0.0570 387 HIS B CA  
3349 C C   . HIS B 376 ? 0.3508 0.4245 0.4321 -0.0236 0.0436  -0.0566 387 HIS B C   
3350 O O   . HIS B 376 ? 0.3304 0.3951 0.3938 -0.0335 0.0499  -0.0556 387 HIS B O   
3351 C CB  . HIS B 376 ? 0.2478 0.3375 0.3540 -0.0207 0.0301  -0.0509 387 HIS B CB  
3352 C CG  . HIS B 376 ? 0.3269 0.3985 0.4129 -0.0309 0.0302  -0.0468 387 HIS B CG  
3353 N ND1 . HIS B 376 ? 0.3249 0.3710 0.3884 -0.0303 0.0310  -0.0437 387 HIS B ND1 
3354 C CD2 . HIS B 376 ? 0.3548 0.4292 0.4388 -0.0414 0.0299  -0.0454 387 HIS B CD2 
3355 C CE1 . HIS B 376 ? 0.4062 0.4377 0.4546 -0.0381 0.0319  -0.0401 387 HIS B CE1 
3356 N NE2 . HIS B 376 ? 0.3576 0.4042 0.4171 -0.0460 0.0316  -0.0418 387 HIS B NE2 
3357 N N   . ARG B 377 ? 0.2978 0.3611 0.3772 -0.0139 0.0393  -0.0571 388 ARG B N   
3358 C CA  . ARG B 377 ? 0.3515 0.3977 0.4107 -0.0130 0.0402  -0.0573 388 ARG B CA  
3359 C C   . ARG B 377 ? 0.3681 0.3957 0.4087 -0.0144 0.0346  -0.0496 388 ARG B C   
3360 O O   . ARG B 377 ? 0.3855 0.4030 0.4117 -0.0118 0.0328  -0.0488 388 ARG B O   
3361 C CB  . ARG B 377 ? 0.3872 0.4352 0.4338 -0.0197 0.0509  -0.0613 388 ARG B CB  
3362 C CG  . ARG B 377 ? 0.3767 0.4441 0.4398 -0.0174 0.0584  -0.0698 388 ARG B CG  
3363 C CD  . ARG B 377 ? 0.4287 0.4973 0.4766 -0.0248 0.0695  -0.0739 388 ARG B CD  
3364 N NE  . ARG B 377 ? 0.5150 0.6026 0.5785 -0.0206 0.0778  -0.0834 388 ARG B NE  
3365 C CZ  . ARG B 377 ? 0.5619 0.6744 0.6456 -0.0221 0.0834  -0.0864 388 ARG B CZ  
3366 N NH1 . ARG B 377 ? 0.4734 0.5954 0.5638 -0.0300 0.0813  -0.0814 388 ARG B NH1 
3367 N NH2 . ARG B 377 ? 0.5098 0.6396 0.6075 -0.0155 0.0916  -0.0951 388 ARG B NH2 
3368 N N   . ASN B 378 ? 0.3086 0.3323 0.3487 -0.0178 0.0317  -0.0444 389 ASN B N   
3369 C CA  . ASN B 378 ? 0.3310 0.3363 0.3532 -0.0168 0.0278  -0.0373 389 ASN B CA  
3370 C C   . ASN B 378 ? 0.3639 0.3690 0.3952 -0.0146 0.0207  -0.0339 389 ASN B C   
3371 O O   . ASN B 378 ? 0.3621 0.3555 0.3827 -0.0178 0.0209  -0.0296 389 ASN B O   
3372 C CB  . ASN B 378 ? 0.3783 0.3692 0.3787 -0.0244 0.0353  -0.0339 389 ASN B CB  
3373 C CG  . ASN B 378 ? 0.5426 0.5317 0.5293 -0.0256 0.0413  -0.0356 389 ASN B CG  
3374 O OD1 . ASN B 378 ? 0.5090 0.4926 0.4846 -0.0194 0.0377  -0.0334 389 ASN B OD1 
3375 N ND2 . ASN B 378 ? 0.5327 0.5299 0.5207 -0.0342 0.0503  -0.0400 389 ASN B ND2 
3376 N N   . ILE B 379 ? 0.2654 0.2817 0.3149 -0.0091 0.0149  -0.0359 390 ILE B N   
3377 C CA  . ILE B 379 ? 0.2520 0.2680 0.3081 -0.0066 0.0077  -0.0320 390 ILE B CA  
3378 C C   . ILE B 379 ? 0.3093 0.3126 0.3521 -0.0020 0.0036  -0.0275 390 ILE B C   
3379 O O   . ILE B 379 ? 0.3072 0.3116 0.3514 0.0026  0.0000  -0.0283 390 ILE B O   
3380 C CB  . ILE B 379 ? 0.2489 0.2776 0.3255 -0.0013 0.0029  -0.0338 390 ILE B CB  
3381 C CG1 . ILE B 379 ? 0.2908 0.3372 0.3823 -0.0037 0.0070  -0.0376 390 ILE B CG1 
3382 C CG2 . ILE B 379 ? 0.2986 0.3262 0.3792 0.0006  -0.0046 -0.0288 390 ILE B CG2 
3383 C CD1 . ILE B 379 ? 0.2603 0.3140 0.3526 -0.0122 0.0073  -0.0360 390 ILE B CD1 
3384 N N   . LYS B 380 ? 0.2787 0.2708 0.3090 -0.0035 0.0042  -0.0231 391 LYS B N   
3385 C CA  . LYS B 380 ? 0.2587 0.2419 0.2776 0.0027  0.0009  -0.0181 391 LYS B CA  
3386 C C   . LYS B 380 ? 0.2754 0.2473 0.2860 0.0014  0.0022  -0.0147 391 LYS B C   
3387 O O   . LYS B 380 ? 0.2797 0.2479 0.2888 -0.0065 0.0066  -0.0167 391 LYS B O   
3388 C CB  . LYS B 380 ? 0.3320 0.3083 0.3344 0.0055  0.0038  -0.0162 391 LYS B CB  
3389 C CG  . LYS B 380 ? 0.4208 0.3843 0.4075 0.0002  0.0123  -0.0154 391 LYS B CG  
3390 C CD  . LYS B 380 ? 0.3932 0.3552 0.3663 0.0024  0.0144  -0.0143 391 LYS B CD  
3391 C CE  . LYS B 380 ? 0.5273 0.4727 0.4802 -0.0025 0.0231  -0.0113 391 LYS B CE  
3392 N NZ  . LYS B 380 ? 0.6320 0.5577 0.5656 0.0046  0.0235  -0.0026 391 LYS B NZ  
3393 N N   . SER B 381 ? 0.3063 0.2738 0.3111 0.0085  -0.0011 -0.0104 392 SER B N   
3394 C CA  . SER B 381 ? 0.2872 0.2449 0.2861 0.0083  0.0000  -0.0085 392 SER B CA  
3395 C C   . SER B 381 ? 0.3352 0.2708 0.3150 0.0039  0.0085  -0.0078 392 SER B C   
3396 O O   . SER B 381 ? 0.3128 0.2403 0.2888 -0.0019 0.0110  -0.0095 392 SER B O   
3397 C CB  . SER B 381 ? 0.2879 0.2479 0.2851 0.0182  -0.0041 -0.0042 392 SER B CB  
3398 O OG  . SER B 381 ? 0.3405 0.2936 0.3239 0.0265  -0.0023 0.0003  392 SER B OG  
3399 N N   A ASP B 382 ? 0.3222 0.2466 0.2877 0.0055  0.0133  -0.0054 393 ASP B N   
3400 N N   B ASP B 382 ? 0.3220 0.2463 0.2875 0.0052  0.0134  -0.0055 393 ASP B N   
3401 C CA  A ASP B 382 ? 0.3753 0.2742 0.3197 0.0001  0.0226  -0.0042 393 ASP B CA  
3402 C CA  B ASP B 382 ? 0.3735 0.2719 0.3180 0.0000  0.0226  -0.0043 393 ASP B CA  
3403 C C   A ASP B 382 ? 0.3734 0.2752 0.3229 -0.0159 0.0269  -0.0105 393 ASP B C   
3404 C C   B ASP B 382 ? 0.3757 0.2766 0.3237 -0.0159 0.0275  -0.0102 393 ASP B C   
3405 O O   A ASP B 382 ? 0.4308 0.3123 0.3649 -0.0245 0.0341  -0.0115 393 ASP B O   
3406 O O   B ASP B 382 ? 0.4062 0.2852 0.3363 -0.0243 0.0360  -0.0104 393 ASP B O   
3407 C CB  A ASP B 382 ? 0.4261 0.3140 0.3538 0.0040  0.0268  0.0005  393 ASP B CB  
3408 C CB  B ASP B 382 ? 0.4411 0.3232 0.3651 0.0079  0.0266  0.0023  393 ASP B CB  
3409 C CG  A ASP B 382 ? 0.4643 0.3468 0.3813 0.0201  0.0240  0.0084  393 ASP B CG  
3410 C CG  B ASP B 382 ? 0.4319 0.3230 0.3568 0.0029  0.0281  0.0009  393 ASP B CG  
3411 O OD1 A ASP B 382 ? 0.5101 0.3870 0.4254 0.0280  0.0227  0.0108  393 ASP B OD1 
3412 O OD1 B ASP B 382 ? 0.4253 0.3388 0.3700 -0.0024 0.0245  -0.0051 393 ASP B OD1 
3413 O OD2 A ASP B 382 ? 0.6285 0.5147 0.5385 0.0250  0.0230  0.0121  393 ASP B OD2 
3414 O OD2 B ASP B 382 ? 0.5742 0.4487 0.4785 0.0050  0.0334  0.0060  393 ASP B OD2 
3415 N N   . ASN B 383 ? 0.3442 0.2712 0.3145 -0.0201 0.0231  -0.0150 394 ASN B N   
3416 C CA  . ASN B 383 ? 0.3354 0.2736 0.3144 -0.0339 0.0266  -0.0207 394 ASN B CA  
3417 C C   . ASN B 383 ? 0.3469 0.3024 0.3429 -0.0380 0.0208  -0.0239 394 ASN B C   
3418 O O   . ASN B 383 ? 0.3755 0.3481 0.3828 -0.0482 0.0218  -0.0284 394 ASN B O   
3419 C CB  . ASN B 383 ? 0.3133 0.2699 0.3044 -0.0341 0.0271  -0.0235 394 ASN B CB  
3420 C CG  . ASN B 383 ? 0.3572 0.2981 0.3287 -0.0343 0.0343  -0.0210 394 ASN B CG  
3421 O OD1 . ASN B 383 ? 0.4637 0.3795 0.4126 -0.0378 0.0406  -0.0175 394 ASN B OD1 
3422 N ND2 . ASN B 383 ? 0.4620 0.4155 0.4400 -0.0304 0.0337  -0.0226 394 ASN B ND2 
3423 N N   . ILE B 384 ? 0.3066 0.2596 0.3037 -0.0307 0.0151  -0.0214 395 ILE B N   
3424 C CA  . ILE B 384 ? 0.2731 0.2391 0.2811 -0.0349 0.0100  -0.0233 395 ILE B CA  
3425 C C   . ILE B 384 ? 0.2927 0.2358 0.2804 -0.0407 0.0150  -0.0240 395 ILE B C   
3426 O O   . ILE B 384 ? 0.3379 0.2618 0.3120 -0.0316 0.0165  -0.0205 395 ILE B O   
3427 C CB  . ILE B 384 ? 0.3013 0.2790 0.3225 -0.0240 0.0012  -0.0202 395 ILE B CB  
3428 C CG1 . ILE B 384 ? 0.3786 0.3710 0.4152 -0.0175 -0.0023 -0.0200 395 ILE B CG1 
3429 C CG2 . ILE B 384 ? 0.2851 0.2759 0.3152 -0.0287 -0.0041 -0.0211 395 ILE B CG2 
3430 C CD1 . ILE B 384 ? 0.3747 0.3857 0.4262 -0.0229 -0.0018 -0.0236 395 ILE B CD1 
3431 N N   . LEU B 385 ? 0.2939 0.2398 0.2792 -0.0557 0.0178  -0.0290 396 LEU B N   
3432 C CA  . LEU B 385 ? 0.3485 0.2696 0.3120 -0.0637 0.0238  -0.0316 396 LEU B CA  
3433 C C   . LEU B 385 ? 0.3552 0.2912 0.3258 -0.0685 0.0177  -0.0343 396 LEU B C   
3434 O O   . LEU B 385 ? 0.3275 0.2947 0.3189 -0.0714 0.0101  -0.0349 396 LEU B O   
3435 C CB  . LEU B 385 ? 0.3743 0.2823 0.3233 -0.0813 0.0335  -0.0364 396 LEU B CB  
3436 C CG  . LEU B 385 ? 0.4445 0.3395 0.3855 -0.0785 0.0400  -0.0333 396 LEU B CG  
3437 C CD1 . LEU B 385 ? 0.4878 0.3654 0.4106 -0.0976 0.0510  -0.0376 396 LEU B CD1 
3438 C CD2 . LEU B 385 ? 0.4780 0.3466 0.4036 -0.0611 0.0417  -0.0263 396 LEU B CD2 
3439 N N   . LEU B 386 ? 0.3640 0.2772 0.3161 -0.0682 0.0213  -0.0354 397 LEU B N   
3440 C CA  . LEU B 386 ? 0.3193 0.2437 0.2738 -0.0724 0.0163  -0.0379 397 LEU B CA  
3441 C C   . LEU B 386 ? 0.3791 0.2878 0.3135 -0.0911 0.0232  -0.0460 397 LEU B C   
3442 O O   . LEU B 386 ? 0.4165 0.2897 0.3266 -0.0946 0.0341  -0.0486 397 LEU B O   
3443 C CB  . LEU B 386 ? 0.3329 0.2477 0.2833 -0.0568 0.0148  -0.0338 397 LEU B CB  
3444 C CG  . LEU B 386 ? 0.3599 0.2879 0.3271 -0.0406 0.0088  -0.0267 397 LEU B CG  
3445 C CD1 . LEU B 386 ? 0.3891 0.3067 0.3495 -0.0266 0.0095  -0.0231 397 LEU B CD1 
3446 C CD2 . LEU B 386 ? 0.3374 0.2986 0.3292 -0.0414 -0.0016 -0.0249 397 LEU B CD2 
3447 N N   . GLY B 387 ? 0.3755 0.3098 0.3184 -0.1033 0.0170  -0.0500 398 GLY B N   
3448 C CA  . GLY B 387 ? 0.4497 0.3725 0.3730 -0.1227 0.0225  -0.0588 398 GLY B CA  
3449 C C   . GLY B 387 ? 0.4539 0.3604 0.3620 -0.1182 0.0236  -0.0604 398 GLY B C   
3450 O O   . GLY B 387 ? 0.3889 0.3057 0.3077 -0.1025 0.0173  -0.0544 398 GLY B O   
3451 N N   . MET B 388 ? 0.4242 0.3050 0.3060 -0.1335 0.0325  -0.0694 399 MET B N   
3452 C CA  . MET B 388 ? 0.4812 0.3443 0.3456 -0.1301 0.0357  -0.0727 399 MET B CA  
3453 C C   . MET B 388 ? 0.5519 0.4520 0.4299 -0.1333 0.0240  -0.0723 399 MET B C   
3454 O O   . MET B 388 ? 0.5468 0.4392 0.4152 -0.1271 0.0250  -0.0731 399 MET B O   
3455 C CB  . MET B 388 ? 0.5779 0.4016 0.4084 -0.1473 0.0492  -0.0839 399 MET B CB  
3456 C CG  . MET B 388 ? 0.5878 0.3630 0.3971 -0.1394 0.0630  -0.0828 399 MET B CG  
3457 S SD  . MET B 388 ? 0.6384 0.3980 0.4516 -0.1048 0.0644  -0.0714 399 MET B SD  
3458 C CE  . MET B 388 ? 0.6492 0.3963 0.4468 -0.0986 0.0683  -0.0767 399 MET B CE  
3459 N N   . ASP B 389 ? 0.4351 0.3753 0.3348 -0.1416 0.0133  -0.0704 400 ASP B N   
3460 C CA  . ASP B 389 ? 0.3867 0.3635 0.3010 -0.1413 0.0009  -0.0668 400 ASP B CA  
3461 C C   . ASP B 389 ? 0.3865 0.3832 0.3265 -0.1206 -0.0083 -0.0549 400 ASP B C   
3462 O O   . ASP B 389 ? 0.4530 0.4795 0.4067 -0.1184 -0.0190 -0.0497 400 ASP B O   
3463 C CB  . ASP B 389 ? 0.5015 0.5134 0.4241 -0.1613 -0.0061 -0.0709 400 ASP B CB  
3464 C CG  . ASP B 389 ? 0.5167 0.5487 0.4608 -0.1614 -0.0085 -0.0679 400 ASP B CG  
3465 O OD1 . ASP B 389 ? 0.4309 0.4443 0.3791 -0.1487 -0.0034 -0.0640 400 ASP B OD1 
3466 O OD2 . ASP B 389 ? 0.5158 0.5848 0.4726 -0.1742 -0.0156 -0.0695 400 ASP B OD2 
3467 N N   . GLY B 390 ? 0.3698 0.3492 0.3143 -0.1056 -0.0040 -0.0504 401 GLY B N   
3468 C CA  . GLY B 390 ? 0.3549 0.3511 0.3221 -0.0886 -0.0117 -0.0406 401 GLY B CA  
3469 C C   . GLY B 390 ? 0.3834 0.4029 0.3726 -0.0884 -0.0170 -0.0376 401 GLY B C   
3470 O O   . GLY B 390 ? 0.3336 0.3665 0.3411 -0.0754 -0.0233 -0.0303 401 GLY B O   
3471 N N   A SER B 391 ? 0.3518 0.3765 0.3394 -0.1029 -0.0138 -0.0434 402 SER B N   
3472 N N   B SER B 391 ? 0.3515 0.3762 0.3389 -0.1030 -0.0138 -0.0435 402 SER B N   
3473 C CA  A SER B 391 ? 0.3597 0.4090 0.3690 -0.1019 -0.0175 -0.0411 402 SER B CA  
3474 C CA  B SER B 391 ? 0.3605 0.4086 0.3691 -0.1022 -0.0170 -0.0414 402 SER B CA  
3475 C C   A SER B 391 ? 0.3291 0.3612 0.3420 -0.0884 -0.0128 -0.0376 402 SER B C   
3476 C C   B SER B 391 ? 0.3288 0.3606 0.3418 -0.0876 -0.0130 -0.0373 402 SER B C   
3477 O O   A SER B 391 ? 0.3437 0.3438 0.3388 -0.0854 -0.0045 -0.0388 402 SER B O   
3478 O O   B SER B 391 ? 0.3426 0.3430 0.3387 -0.0831 -0.0054 -0.0379 402 SER B O   
3479 C CB  A SER B 391 ? 0.3466 0.4068 0.3525 -0.1223 -0.0137 -0.0489 402 SER B CB  
3480 C CB  B SER B 391 ? 0.3524 0.4067 0.3554 -0.1225 -0.0118 -0.0494 402 SER B CB  
3481 O OG  A SER B 391 ? 0.3594 0.3848 0.3443 -0.1296 -0.0013 -0.0543 402 SER B OG  
3482 O OG  B SER B 391 ? 0.3537 0.4343 0.3577 -0.1370 -0.0178 -0.0530 402 SER B OG  
3483 N N   . VAL B 392 ? 0.2822 0.3361 0.3175 -0.0796 -0.0180 -0.0332 403 VAL B N   
3484 C CA  . VAL B 392 ? 0.3154 0.3585 0.3559 -0.0668 -0.0153 -0.0300 403 VAL B CA  
3485 C C   . VAL B 392 ? 0.2688 0.3296 0.3227 -0.0710 -0.0132 -0.0323 403 VAL B C   
3486 O O   . VAL B 392 ? 0.2586 0.3505 0.3320 -0.0709 -0.0194 -0.0312 403 VAL B O   
3487 C CB  . VAL B 392 ? 0.2677 0.3173 0.3212 -0.0511 -0.0227 -0.0230 403 VAL B CB  
3488 C CG1 . VAL B 392 ? 0.2581 0.2984 0.3162 -0.0401 -0.0200 -0.0211 403 VAL B CG1 
3489 C CG2 . VAL B 392 ? 0.3112 0.3481 0.3528 -0.0481 -0.0244 -0.0208 403 VAL B CG2 
3490 N N   . LYS B 393 ? 0.2325 0.2748 0.2757 -0.0740 -0.0043 -0.0349 404 LYS B N   
3491 C CA  . LYS B 393 ? 0.2789 0.3381 0.3326 -0.0802 -0.0004 -0.0379 404 LYS B CA  
3492 C C   . LYS B 393 ? 0.3372 0.3777 0.3846 -0.0729 0.0062  -0.0368 404 LYS B C   
3493 O O   . LYS B 393 ? 0.3136 0.3235 0.3414 -0.0694 0.0107  -0.0350 404 LYS B O   
3494 C CB  . LYS B 393 ? 0.3524 0.4131 0.3952 -0.1017 0.0060  -0.0447 404 LYS B CB  
3495 C CG  . LYS B 393 ? 0.3186 0.4001 0.3645 -0.1127 -0.0003 -0.0472 404 LYS B CG  
3496 C CD  . LYS B 393 ? 0.3781 0.4620 0.4123 -0.1370 0.0066  -0.0553 404 LYS B CD  
3497 C CE  . LYS B 393 ? 0.3581 0.4628 0.3923 -0.1496 -0.0001 -0.0587 404 LYS B CE  
3498 N NZ  . LYS B 393 ? 0.4079 0.5285 0.4375 -0.1755 0.0047  -0.0673 404 LYS B NZ  
3499 N N   . LEU B 394 ? 0.2835 0.3442 0.3474 -0.0702 0.0071  -0.0377 405 LEU B N   
3500 C CA  . LEU B 394 ? 0.3047 0.3517 0.3618 -0.0663 0.0140  -0.0378 405 LEU B CA  
3501 C C   . LEU B 394 ? 0.3193 0.3554 0.3600 -0.0831 0.0244  -0.0417 405 LEU B C   
3502 O O   . LEU B 394 ? 0.3468 0.4017 0.3932 -0.0976 0.0259  -0.0462 405 LEU B O   
3503 C CB  . LEU B 394 ? 0.3271 0.3993 0.4063 -0.0583 0.0128  -0.0388 405 LEU B CB  
3504 C CG  . LEU B 394 ? 0.4214 0.5091 0.5206 -0.0436 0.0041  -0.0359 405 LEU B CG  
3505 C CD1 . LEU B 394 ? 0.3159 0.4193 0.4305 -0.0363 0.0072  -0.0385 405 LEU B CD1 
3506 C CD2 . LEU B 394 ? 0.3709 0.4361 0.4605 -0.0335 -0.0002 -0.0315 405 LEU B CD2 
3507 N N   . THR B 395 ? 0.3904 0.3971 0.4101 -0.0819 0.0316  -0.0398 406 THR B N   
3508 C CA  . THR B 395 ? 0.4894 0.4770 0.4877 -0.0988 0.0423  -0.0425 406 THR B CA  
3509 C C   . THR B 395 ? 0.5730 0.5835 0.5809 -0.1109 0.0488  -0.0471 406 THR B C   
3510 O O   . THR B 395 ? 0.5153 0.5248 0.5142 -0.1304 0.0558  -0.0514 406 THR B O   
3511 C CB  . THR B 395 ? 0.4515 0.3977 0.4211 -0.0933 0.0486  -0.0374 406 THR B CB  
3512 O OG1 . THR B 395 ? 0.5710 0.4996 0.5210 -0.1089 0.0604  -0.0391 406 THR B OG1 
3513 C CG2 . THR B 395 ? 0.6626 0.6094 0.6362 -0.0763 0.0454  -0.0328 406 THR B CG2 
3514 N N   . ASP B 396 ? 0.5189 0.5507 0.5445 -0.1010 0.0473  -0.0471 407 ASP B N   
3515 C CA  . ASP B 396 ? 0.4923 0.5514 0.5301 -0.1115 0.0540  -0.0522 407 ASP B CA  
3516 C C   . ASP B 396 ? 0.5804 0.6705 0.6461 -0.0962 0.0487  -0.0531 407 ASP B C   
3517 O O   . ASP B 396 ? 0.4621 0.5534 0.5379 -0.0808 0.0395  -0.0501 407 ASP B O   
3518 C CB  . ASP B 396 ? 0.6518 0.6866 0.6654 -0.1205 0.0662  -0.0518 407 ASP B CB  
3519 C CG  . ASP B 396 ? 0.7867 0.7942 0.7849 -0.1046 0.0657  -0.0459 407 ASP B CG  
3520 O OD1 . ASP B 396 ? 0.5638 0.5856 0.5775 -0.0894 0.0600  -0.0456 407 ASP B OD1 
3521 O OD2 . ASP B 396 ? 0.8418 0.8133 0.8111 -0.1077 0.0713  -0.0414 407 ASP B OD2 
3522 N N   . PHE B 397 ? 0.5694 0.6831 0.6462 -0.1006 0.0558  -0.0575 408 PHE B N   
3523 C CA  . PHE B 397 ? 0.5698 0.7092 0.6706 -0.0854 0.0535  -0.0594 408 PHE B CA  
3524 C C   . PHE B 397 ? 0.5783 0.6951 0.6669 -0.0739 0.0561  -0.0581 408 PHE B C   
3525 O O   . PHE B 397 ? 0.6205 0.7535 0.7237 -0.0638 0.0577  -0.0614 408 PHE B O   
3526 C CB  . PHE B 397 ? 0.5638 0.7420 0.6834 -0.0937 0.0610  -0.0655 408 PHE B CB  
3527 C CG  . PHE B 397 ? 0.5184 0.7348 0.6607 -0.0998 0.0558  -0.0673 408 PHE B CG  
3528 C CD1 . PHE B 397 ? 0.5866 0.7963 0.7236 -0.1061 0.0479  -0.0646 408 PHE B CD1 
3529 C CD2 . PHE B 397 ? 0.5132 0.7752 0.6825 -0.0987 0.0590  -0.0718 408 PHE B CD2 
3530 C CE1 . PHE B 397 ? 0.4845 0.7330 0.6415 -0.1126 0.0424  -0.0662 408 PHE B CE1 
3531 C CE2 . PHE B 397 ? 0.5269 0.8299 0.7185 -0.1036 0.0534  -0.0727 408 PHE B CE2 
3532 C CZ  . PHE B 397 ? 0.4686 0.7652 0.6535 -0.1111 0.0445  -0.0698 408 PHE B CZ  
3533 N N   . GLY B 398 ? 0.5009 0.5817 0.5626 -0.0748 0.0568  -0.0535 409 GLY B N   
3534 C CA  . GLY B 398 ? 0.5509 0.6147 0.5988 -0.0669 0.0597  -0.0524 409 GLY B CA  
3535 C C   . GLY B 398 ? 0.8172 0.8725 0.8460 -0.0788 0.0717  -0.0535 409 GLY B C   
3536 O O   . GLY B 398 ? 0.8540 0.9009 0.8720 -0.0734 0.0749  -0.0534 409 GLY B O   
3537 N N   . PHE B 399 ? 0.8540 0.9142 0.8790 -0.0962 0.0788  -0.0551 410 PHE B N   
3538 C CA  . PHE B 399 ? 0.9555 1.0062 0.9603 -0.1113 0.0916  -0.0557 410 PHE B CA  
3539 C C   . PHE B 399 ? 0.9831 1.0559 0.9974 -0.1081 0.0983  -0.0610 410 PHE B C   
3540 O O   . PHE B 399 ? 1.1334 1.2090 1.1372 -0.1216 0.1100  -0.0631 410 PHE B O   
3541 C CB  . PHE B 399 ? 0.9869 0.9924 0.9553 -0.1116 0.0940  -0.0475 410 PHE B CB  
3542 C CG  . PHE B 399 ? 0.9735 0.9668 0.9309 -0.0966 0.0915  -0.0439 410 PHE B CG  
3543 C CD1 . PHE B 399 ? 1.0145 1.0119 0.9627 -0.0995 0.0999  -0.0456 410 PHE B CD1 
3544 C CD2 . PHE B 399 ? 0.9939 0.9729 0.9486 -0.0812 0.0809  -0.0388 410 PHE B CD2 
3545 C CE1 . PHE B 399 ? 1.0149 1.0031 0.9515 -0.0874 0.0971  -0.0429 410 PHE B CE1 
3546 C CE2 . PHE B 399 ? 0.9661 0.9381 0.9109 -0.0695 0.0780  -0.0361 410 PHE B CE2 
3547 C CZ  . PHE B 399 ? 0.9815 0.9577 0.9166 -0.0728 0.0858  -0.0382 410 PHE B CZ  
3548 N N   . SER B 408 ? 0.6975 0.6826 0.4438 -0.0539 0.0839  -0.0358 419 SER B N   
3549 C CA  . SER B 408 ? 0.5503 0.5452 0.2744 -0.0600 0.0877  -0.0421 419 SER B CA  
3550 C C   . SER B 408 ? 0.4984 0.5065 0.2209 -0.0554 0.0749  -0.0464 419 SER B C   
3551 O O   . SER B 408 ? 0.5760 0.5838 0.2979 -0.0469 0.0622  -0.0361 419 SER B O   
3552 C CB  . SER B 408 ? 0.6237 0.6064 0.3101 -0.0637 0.0924  -0.0280 419 SER B CB  
3553 O OG  . SER B 408 ? 0.7084 0.7024 0.3706 -0.0694 0.0942  -0.0333 419 SER B OG  
3554 N N   . LYS B 409 ? 0.5143 0.5346 0.2363 -0.0617 0.0790  -0.0625 420 LYS B N   
3555 C CA  . LYS B 409 ? 0.6607 0.6936 0.3762 -0.0616 0.0682  -0.0685 420 LYS B CA  
3556 C C   . LYS B 409 ? 0.6356 0.6736 0.3187 -0.0602 0.0592  -0.0545 420 LYS B C   
3557 O O   . LYS B 409 ? 0.5889 0.6405 0.2691 -0.0581 0.0464  -0.0542 420 LYS B O   
3558 C CB  . LYS B 409 ? 0.6145 0.6549 0.3264 -0.0707 0.0771  -0.0886 420 LYS B CB  
3559 C CG  . LYS B 409 ? 0.7960 0.8336 0.5383 -0.0701 0.0861  -0.1039 420 LYS B CG  
3560 C CD  . LYS B 409 ? 0.7553 0.7972 0.4862 -0.0781 0.0976  -0.1224 420 LYS B CD  
3561 C CE  . LYS B 409 ? 0.8673 0.9061 0.6273 -0.0748 0.1064  -0.1383 420 LYS B CE  
3562 N NZ  . LYS B 409 ? 0.7610 0.8011 0.5074 -0.0814 0.1165  -0.1574 420 LYS B NZ  
3563 N N   . ARG B 410 ? 0.5796 0.6077 0.2380 -0.0613 0.0655  -0.0420 421 ARG B N   
3564 C CA  . ARG B 410 ? 0.6390 0.6706 0.2637 -0.0582 0.0577  -0.0265 421 ARG B CA  
3565 C C   . ARG B 410 ? 0.5678 0.5908 0.1938 -0.0440 0.0472  -0.0066 421 ARG B C   
3566 O O   . ARG B 410 ? 0.6681 0.6974 0.2701 -0.0373 0.0379  0.0076  421 ARG B O   
3567 C CB  . ARG B 410 ? 0.6069 0.6278 0.2008 -0.0657 0.0705  -0.0208 421 ARG B CB  
3568 C CG  . ARG B 410 ? 0.6169 0.6460 0.2064 -0.0793 0.0835  -0.0400 421 ARG B CG  
3569 C CD  . ARG B 410 ? 0.6543 0.6756 0.2109 -0.0861 0.0941  -0.0318 421 ARG B CD  
3570 N NE  . ARG B 410 ? 0.6819 0.7091 0.2103 -0.0807 0.0823  -0.0177 421 ARG B NE  
3571 C CZ  . ARG B 410 ? 0.7020 0.7439 0.2175 -0.0847 0.0796  -0.0246 421 ARG B CZ  
3572 N NH1 . ARG B 410 ? 0.7006 0.7499 0.2266 -0.0943 0.0888  -0.0451 421 ARG B NH1 
3573 N NH2 . ARG B 410 ? 0.7260 0.7751 0.2178 -0.0780 0.0673  -0.0107 421 ARG B NH2 
3574 N N   . SER B 411 ? 0.5418 0.5524 0.1948 -0.0385 0.0481  -0.0053 422 SER B N   
3575 C CA  . SER B 411 ? 0.6559 0.6545 0.3095 -0.0249 0.0407  0.0124  422 SER B CA  
3576 C C   . SER B 411 ? 0.5665 0.5834 0.2411 -0.0161 0.0259  0.0111  422 SER B C   
3577 O O   . SER B 411 ? 0.6823 0.7135 0.3789 -0.0218 0.0235  -0.0047 422 SER B O   
3578 C CB  . SER B 411 ? 0.6318 0.6061 0.3007 -0.0253 0.0505  0.0144  422 SER B CB  
3579 O OG  . SER B 411 ? 0.9064 0.8639 0.5549 -0.0347 0.0646  0.0170  422 SER B OG  
3580 N N   . GLU B 412 ? 0.6472 0.6625 0.3138 -0.0019 0.0168  0.0283  423 GLU B N   
3581 C CA  . GLU B 412 ? 0.6674 0.7018 0.3539 0.0074  0.0033  0.0292  423 GLU B CA  
3582 C C   . GLU B 412 ? 0.5556 0.5770 0.2728 0.0098  0.0060  0.0247  423 GLU B C   
3583 O O   . GLU B 412 ? 0.5941 0.5893 0.3115 0.0100  0.0156  0.0288  423 GLU B O   
3584 C CB  . GLU B 412 ? 0.5924 0.6302 0.2621 0.0248  -0.0061 0.0499  423 GLU B CB  
3585 C CG  . GLU B 412 ? 0.8245 0.8713 0.4603 0.0257  -0.0089 0.0594  423 GLU B CG  
3586 C CD  . GLU B 412 ? 0.5865 0.5986 0.1951 0.0258  0.0036  0.0709  423 GLU B CD  
3587 O OE1 . GLU B 412 ? 0.6724 0.6544 0.2879 0.0296  0.0118  0.0756  423 GLU B OE1 
3588 O OE2 . GLU B 412 ? 0.7069 0.7220 0.2868 0.0203  0.0059  0.0742  423 GLU B OE2 
3589 N N   . MET B 413 ? 0.5558 0.5960 0.2980 0.0100  -0.0023 0.0162  424 MET B N   
3590 C CA  . MET B 413 ? 0.5665 0.5975 0.3359 0.0143  -0.0022 0.0146  424 MET B CA  
3591 C C   . MET B 413 ? 0.6272 0.6592 0.3951 0.0308  -0.0101 0.0304  424 MET B C   
3592 O O   . MET B 413 ? 0.5427 0.6003 0.3084 0.0370  -0.0211 0.0348  424 MET B O   
3593 C CB  . MET B 413 ? 0.5196 0.5666 0.3153 0.0068  -0.0062 -0.0010 424 MET B CB  
3594 C CG  . MET B 413 ? 0.6192 0.6615 0.4209 -0.0063 0.0029  -0.0172 424 MET B CG  
3595 S SD  . MET B 413 ? 0.8721 0.9244 0.7046 -0.0107 -0.0019 -0.0312 424 MET B SD  
3596 C CE  . MET B 413 ? 0.5173 0.5511 0.3708 -0.0034 0.0017  -0.0252 424 MET B CE  
3597 N N   . VAL B 414 ? 0.6561 0.6620 0.4256 0.0376  -0.0040 0.0382  425 VAL B N   
3598 C CA  . VAL B 414 ? 0.5775 0.5790 0.3444 0.0550  -0.0090 0.0527  425 VAL B CA  
3599 C C   . VAL B 414 ? 0.6117 0.6165 0.4075 0.0577  -0.0118 0.0475  425 VAL B C   
3600 O O   . VAL B 414 ? 0.5875 0.6114 0.3919 0.0684  -0.0208 0.0524  425 VAL B O   
3601 C CB  . VAL B 414 ? 0.6995 0.6643 0.4416 0.0615  0.0006  0.0662  425 VAL B CB  
3602 C CG1 . VAL B 414 ? 0.7803 0.7356 0.5203 0.0811  -0.0028 0.0802  425 VAL B CG1 
3603 C CG2 . VAL B 414 ? 0.7270 0.6891 0.4372 0.0596  0.0028  0.0737  425 VAL B CG2 
3604 N N   . GLY B 415 ? 0.5319 0.5217 0.3433 0.0478  -0.0045 0.0377  426 GLY B N   
3605 C CA  . GLY B 415 ? 0.4726 0.4671 0.3104 0.0486  -0.0074 0.0321  426 GLY B CA  
3606 C C   . GLY B 415 ? 0.4562 0.4710 0.3148 0.0369  -0.0110 0.0172  426 GLY B C   
3607 O O   . GLY B 415 ? 0.4369 0.4583 0.2903 0.0273  -0.0092 0.0093  426 GLY B O   
3608 N N   . THR B 416 ? 0.4254 0.4466 0.3064 0.0375  -0.0147 0.0132  427 THR B N   
3609 C CA  . THR B 416 ? 0.4501 0.4850 0.3497 0.0273  -0.0174 0.0002  427 THR B CA  
3610 C C   . THR B 416 ? 0.4231 0.4430 0.3388 0.0212  -0.0108 -0.0071 427 THR B C   
3611 O O   . THR B 416 ? 0.3989 0.4105 0.3244 0.0254  -0.0104 -0.0035 427 THR B O   
3612 C CB  . THR B 416 ? 0.4147 0.4712 0.3275 0.0309  -0.0269 0.0010  427 THR B CB  
3613 O OG1 . THR B 416 ? 0.5076 0.5849 0.4072 0.0367  -0.0340 0.0078  427 THR B OG1 
3614 C CG2 . THR B 416 ? 0.3814 0.4466 0.3106 0.0193  -0.0288 -0.0119 427 THR B CG2 
3615 N N   . PRO B 417 ? 0.4501 0.4679 0.3689 0.0120  -0.0056 -0.0172 428 PRO B N   
3616 C CA  . PRO B 417 ? 0.4041 0.4131 0.3403 0.0075  0.0000  -0.0240 428 PRO B CA  
3617 C C   . PRO B 417 ? 0.3500 0.3665 0.3068 0.0063  -0.0053 -0.0296 428 PRO B C   
3618 O O   . PRO B 417 ? 0.3482 0.3656 0.3144 0.0012  -0.0032 -0.0393 428 PRO B O   
3619 C CB  . PRO B 417 ? 0.4633 0.4712 0.3932 0.0003  0.0077  -0.0324 428 PRO B CB  
3620 C CG  . PRO B 417 ? 0.4625 0.4823 0.3800 -0.0018 0.0031  -0.0352 428 PRO B CG  
3621 C CD  . PRO B 417 ? 0.5236 0.5490 0.4290 0.0059  -0.0043 -0.0231 428 PRO B CD  
3622 N N   . TYR B 418 ? 0.3005 0.3205 0.2629 0.0118  -0.0114 -0.0231 429 TYR B N   
3623 C CA  . TYR B 418 ? 0.3471 0.3757 0.3249 0.0100  -0.0171 -0.0267 429 TYR B CA  
3624 C C   . TYR B 418 ? 0.2905 0.3110 0.2852 0.0069  -0.0141 -0.0322 429 TYR B C   
3625 O O   . TYR B 418 ? 0.3110 0.3346 0.3164 0.0039  -0.0173 -0.0364 429 TYR B O   
3626 C CB  . TYR B 418 ? 0.2955 0.3309 0.2755 0.0170  -0.0228 -0.0180 429 TYR B CB  
3627 C CG  . TYR B 418 ? 0.2868 0.3086 0.2693 0.0221  -0.0193 -0.0124 429 TYR B CG  
3628 C CD1 . TYR B 418 ? 0.3532 0.3712 0.3512 0.0199  -0.0192 -0.0146 429 TYR B CD1 
3629 C CD2 . TYR B 418 ? 0.3994 0.4107 0.3667 0.0286  -0.0158 -0.0046 429 TYR B CD2 
3630 C CE1 . TYR B 418 ? 0.4682 0.4751 0.4669 0.0226  -0.0162 -0.0105 429 TYR B CE1 
3631 C CE2 . TYR B 418 ? 0.4796 0.4754 0.4467 0.0312  -0.0117 -0.0009 429 TYR B CE2 
3632 C CZ  . TYR B 418 ? 0.4424 0.4376 0.4255 0.0275  -0.0121 -0.0045 429 TYR B CZ  
3633 O OH  . TYR B 418 ? 0.5407 0.5223 0.5226 0.0280  -0.0083 -0.0021 429 TYR B OH  
3634 N N   . TRP B 419 ? 0.2717 0.2828 0.2688 0.0074  -0.0080 -0.0318 430 TRP B N   
3635 C CA  . TRP B 419 ? 0.2812 0.2892 0.2954 0.0062  -0.0059 -0.0355 430 TRP B CA  
3636 C C   . TRP B 419 ? 0.2918 0.2993 0.3108 0.0033  -0.0006 -0.0447 430 TRP B C   
3637 O O   . TRP B 419 ? 0.2936 0.3003 0.3277 0.0045  0.0009  -0.0475 430 TRP B O   
3638 C CB  . TRP B 419 ? 0.3040 0.3064 0.3195 0.0069  -0.0023 -0.0309 430 TRP B CB  
3639 C CG  . TRP B 419 ? 0.3461 0.3442 0.3497 0.0040  0.0054  -0.0317 430 TRP B CG  
3640 C CD1 . TRP B 419 ? 0.3655 0.3662 0.3752 0.0001  0.0121  -0.0375 430 TRP B CD1 
3641 C CD2 . TRP B 419 ? 0.3520 0.3429 0.3349 0.0049  0.0074  -0.0259 430 TRP B CD2 
3642 N NE1 . TRP B 419 ? 0.3515 0.3472 0.3451 -0.0035 0.0188  -0.0361 430 TRP B NE1 
3643 C CE2 . TRP B 419 ? 0.4525 0.4399 0.4282 -0.0004 0.0159  -0.0285 430 TRP B CE2 
3644 C CE3 . TRP B 419 ? 0.3842 0.3719 0.3538 0.0107  0.0033  -0.0180 430 TRP B CE3 
3645 C CZ2 . TRP B 419 ? 0.3992 0.3764 0.3525 -0.0013 0.0204  -0.0230 430 TRP B CZ2 
3646 C CZ3 . TRP B 419 ? 0.4281 0.4061 0.3762 0.0123  0.0072  -0.0121 430 TRP B CZ3 
3647 C CH2 . TRP B 419 ? 0.4077 0.3787 0.3467 0.0058  0.0158  -0.0143 430 TRP B CH2 
3648 N N   . MET B 420 ? 0.3147 0.3232 0.3208 0.0006  0.0024  -0.0493 431 MET B N   
3649 C CA  . MET B 420 ? 0.3232 0.3304 0.3323 -0.0014 0.0097  -0.0588 431 MET B CA  
3650 C C   . MET B 420 ? 0.3721 0.3755 0.3876 -0.0024 0.0084  -0.0667 431 MET B C   
3651 O O   . MET B 420 ? 0.3438 0.3479 0.3525 -0.0059 0.0029  -0.0675 431 MET B O   
3652 C CB  . MET B 420 ? 0.3468 0.3554 0.3372 -0.0050 0.0150  -0.0614 431 MET B CB  
3653 C CG  . MET B 420 ? 0.3879 0.3950 0.3710 -0.0052 0.0193  -0.0546 431 MET B CG  
3654 S SD  . MET B 420 ? 0.4608 0.4679 0.4191 -0.0100 0.0263  -0.0563 431 MET B SD  
3655 C CE  . MET B 420 ? 0.5068 0.5061 0.4572 -0.0111 0.0313  -0.0464 431 MET B CE  
3656 N N   . ALA B 421 ? 0.3396 0.3390 0.3678 0.0007  0.0141  -0.0724 432 ALA B N   
3657 C CA  . ALA B 421 ? 0.3906 0.3800 0.4235 0.0013  0.0153  -0.0801 432 ALA B CA  
3658 C C   . ALA B 421 ? 0.3685 0.3536 0.3848 -0.0049 0.0194  -0.0905 432 ALA B C   
3659 O O   . ALA B 421 ? 0.3603 0.3516 0.3648 -0.0075 0.0238  -0.0927 432 ALA B O   
3660 C CB  . ALA B 421 ? 0.3509 0.3382 0.4010 0.0092  0.0213  -0.0828 432 ALA B CB  
3661 N N   . PRO B 422 ? 0.3607 0.3340 0.3738 -0.0088 0.0187  -0.0973 433 PRO B N   
3662 C CA  . PRO B 422 ? 0.4646 0.4337 0.4594 -0.0170 0.0225  -0.1086 433 PRO B CA  
3663 C C   . PRO B 422 ? 0.4995 0.4659 0.4913 -0.0139 0.0341  -0.1176 433 PRO B C   
3664 O O   . PRO B 422 ? 0.4568 0.4287 0.4312 -0.0202 0.0372  -0.1230 433 PRO B O   
3665 C CB  . PRO B 422 ? 0.4310 0.3828 0.4251 -0.0219 0.0215  -0.1148 433 PRO B CB  
3666 C CG  . PRO B 422 ? 0.4176 0.3701 0.4265 -0.0181 0.0138  -0.1036 433 PRO B CG  
3667 C CD  . PRO B 422 ? 0.3854 0.3467 0.4089 -0.0071 0.0151  -0.0955 433 PRO B CD  
3668 N N   . GLU B 423 ? 0.3979 0.3589 0.4064 -0.0038 0.0406  -0.1188 434 GLU B N   
3669 C CA  . GLU B 423 ? 0.5831 0.5450 0.5910 0.0001  0.0527  -0.1279 434 GLU B CA  
3670 C C   . GLU B 423 ? 0.4710 0.4516 0.4741 -0.0021 0.0548  -0.1233 434 GLU B C   
3671 O O   . GLU B 423 ? 0.5145 0.4983 0.5088 -0.0037 0.0645  -0.1315 434 GLU B O   
3672 C CB  . GLU B 423 ? 0.4458 0.4025 0.4752 0.0135  0.0587  -0.1289 434 GLU B CB  
3673 C CG  . GLU B 423 ? 0.4988 0.4710 0.5486 0.0204  0.0535  -0.1164 434 GLU B CG  
3674 C CD  . GLU B 423 ? 0.4133 0.3766 0.4725 0.0234  0.0441  -0.1080 434 GLU B CD  
3675 O OE1 . GLU B 423 ? 0.3652 0.3147 0.4131 0.0164  0.0389  -0.1090 434 GLU B OE1 
3676 O OE2 . GLU B 423 ? 0.4138 0.3860 0.4916 0.0319  0.0420  -0.1006 434 GLU B OE2 
3677 N N   . VAL B 424 ? 0.4292 0.4198 0.4360 -0.0027 0.0469  -0.1107 435 VAL B N   
3678 C CA  . VAL B 424 ? 0.3901 0.3926 0.3877 -0.0063 0.0490  -0.1054 435 VAL B CA  
3679 C C   . VAL B 424 ? 0.5648 0.5676 0.5365 -0.0147 0.0469  -0.1066 435 VAL B C   
3680 O O   . VAL B 424 ? 0.5476 0.5548 0.5052 -0.0186 0.0541  -0.1099 435 VAL B O   
3681 C CB  . VAL B 424 ? 0.4392 0.4473 0.4458 -0.0045 0.0419  -0.0922 435 VAL B CB  
3682 C CG1 . VAL B 424 ? 0.4242 0.4381 0.4173 -0.0090 0.0448  -0.0864 435 VAL B CG1 
3683 C CG2 . VAL B 424 ? 0.3400 0.3522 0.3709 0.0027  0.0434  -0.0909 435 VAL B CG2 
3684 N N   . VAL B 425 ? 0.4892 0.4902 0.4542 -0.0178 0.0368  -0.1032 436 VAL B N   
3685 C CA  . VAL B 425 ? 0.5708 0.5780 0.5125 -0.0248 0.0324  -0.1021 436 VAL B CA  
3686 C C   . VAL B 425 ? 0.5559 0.5601 0.4819 -0.0316 0.0394  -0.1163 436 VAL B C   
3687 O O   . VAL B 425 ? 0.6037 0.6153 0.5080 -0.0375 0.0394  -0.1166 436 VAL B O   
3688 C CB  . VAL B 425 ? 0.5264 0.5380 0.4678 -0.0263 0.0200  -0.0957 436 VAL B CB  
3689 C CG1 . VAL B 425 ? 0.5383 0.5516 0.4933 -0.0191 0.0148  -0.0825 436 VAL B CG1 
3690 C CG2 . VAL B 425 ? 0.5046 0.5080 0.4520 -0.0304 0.0184  -0.1050 436 VAL B CG2 
3691 N N   . THR B 426 ? 0.5957 0.5879 0.5305 -0.0306 0.0457  -0.1280 437 THR B N   
3692 C CA  . THR B 426 ? 0.5431 0.5287 0.4627 -0.0366 0.0546  -0.1434 437 THR B CA  
3693 C C   . THR B 426 ? 0.7517 0.7393 0.6729 -0.0322 0.0681  -0.1486 437 THR B C   
3694 O O   . THR B 426 ? 0.7582 0.7380 0.6717 -0.0340 0.0785  -0.1629 437 THR B O   
3695 C CB  . THR B 426 ? 0.6282 0.5949 0.5537 -0.0373 0.0563  -0.1541 437 THR B CB  
3696 O OG1 . THR B 426 ? 0.7516 0.7102 0.7018 -0.0251 0.0597  -0.1511 437 THR B OG1 
3697 C CG2 . THR B 426 ? 0.6235 0.5910 0.5451 -0.0452 0.0438  -0.1503 437 THR B CG2 
3698 N N   . ARG B 427 ? 0.9458 0.9438 0.8768 -0.0273 0.0687  -0.1377 438 ARG B N   
3699 C CA  . ARG B 427 ? 0.9661 0.9719 0.8984 -0.0256 0.0810  -0.1403 438 ARG B CA  
3700 C C   . ARG B 427 ? 0.9765 0.9774 0.9239 -0.0183 0.0928  -0.1531 438 ARG B C   
3701 O O   . ARG B 427 ? 1.0210 1.0266 0.9625 -0.0190 0.1054  -0.1623 438 ARG B O   
3702 C CB  . ARG B 427 ? 1.0199 1.0316 0.9241 -0.0347 0.0855  -0.1425 438 ARG B CB  
3703 C CG  . ARG B 427 ? 1.0781 1.0958 0.9664 -0.0389 0.0766  -0.1276 438 ARG B CG  
3704 C CD  . ARG B 427 ? 1.1816 1.2043 1.0416 -0.0468 0.0834  -0.1301 438 ARG B CD  
3705 N NE  . ARG B 427 ? 1.2372 1.2571 1.0837 -0.0523 0.0880  -0.1461 438 ARG B NE  
3706 C CZ  . ARG B 427 ? 1.2378 1.2583 1.0765 -0.0551 0.1021  -0.1588 438 ARG B CZ  
3707 N NH1 . ARG B 427 ? 1.2761 1.3037 1.1177 -0.0544 0.1130  -0.1567 438 ARG B NH1 
3708 N NH2 . ARG B 427 ? 1.1238 1.1378 0.9505 -0.0599 0.1062  -0.1747 438 ARG B NH2 
3709 N N   . LYS B 428 ? 0.7485 0.7402 0.7154 -0.0102 0.0893  -0.1531 439 LYS B N   
3710 C CA  . LYS B 428 ? 0.7450 0.7320 0.7288 0.0007  0.1000  -0.1624 439 LYS B CA  
3711 C C   . LYS B 428 ? 0.8206 0.8267 0.8290 0.0091  0.1028  -0.1548 439 LYS B C   
3712 O O   . LYS B 428 ? 0.7789 0.7958 0.7922 0.0060  0.0951  -0.1424 439 LYS B O   
3713 C CB  . LYS B 428 ? 0.6760 0.6422 0.6680 0.0064  0.0954  -0.1646 439 LYS B CB  
3714 C CG  . LYS B 428 ? 0.8413 0.7905 0.8106 -0.0051 0.0902  -0.1706 439 LYS B CG  
3715 C CD  . LYS B 428 ? 0.7412 0.6666 0.7177 -0.0008 0.0877  -0.1730 439 LYS B CD  
3716 C CE  . LYS B 428 ? 0.8188 0.7300 0.7728 -0.0156 0.0823  -0.1795 439 LYS B CE  
3717 N NZ  . LYS B 428 ? 0.9032 0.7905 0.8628 -0.0142 0.0790  -0.1796 439 LYS B NZ  
3718 N N   . ALA B 429 ? 0.6681 0.6793 0.6916 0.0195  0.1146  -0.1630 440 ALA B N   
3719 C CA  . ALA B 429 ? 0.5810 0.6131 0.6325 0.0289  0.1157  -0.1561 440 ALA B CA  
3720 C C   . ALA B 429 ? 0.4394 0.4638 0.5063 0.0355  0.1032  -0.1461 440 ALA B C   
3721 O O   . ALA B 429 ? 0.5283 0.5301 0.5923 0.0398  0.1001  -0.1489 440 ALA B O   
3722 C CB  . ALA B 429 ? 0.6384 0.6798 0.7053 0.0417  0.1304  -0.1668 440 ALA B CB  
3723 N N   . TYR B 430 ? 0.4259 0.4679 0.5069 0.0347  0.0964  -0.1345 441 TYR B N   
3724 C CA  . TYR B 430 ? 0.4334 0.4692 0.5257 0.0389  0.0840  -0.1243 441 TYR B CA  
3725 C C   . TYR B 430 ? 0.4690 0.5300 0.5873 0.0458  0.0830  -0.1174 441 TYR B C   
3726 O O   . TYR B 430 ? 0.4182 0.5029 0.5445 0.0442  0.0909  -0.1197 441 TYR B O   
3727 C CB  . TYR B 430 ? 0.4334 0.4606 0.5090 0.0271  0.0728  -0.1162 441 TYR B CB  
3728 C CG  . TYR B 430 ? 0.4476 0.4894 0.5161 0.0172  0.0729  -0.1104 441 TYR B CG  
3729 C CD1 . TYR B 430 ? 0.4190 0.4755 0.5015 0.0167  0.0690  -0.1015 441 TYR B CD1 
3730 C CD2 . TYR B 430 ? 0.4903 0.5292 0.5355 0.0077  0.0772  -0.1135 441 TYR B CD2 
3731 C CE1 . TYR B 430 ? 0.5312 0.5954 0.6042 0.0063  0.0703  -0.0966 441 TYR B CE1 
3732 C CE2 . TYR B 430 ? 0.5239 0.5711 0.5596 -0.0011 0.0781  -0.1071 441 TYR B CE2 
3733 C CZ  . TYR B 430 ? 0.5755 0.6333 0.6248 -0.0020 0.0751  -0.0989 441 TYR B CZ  
3734 O OH  . TYR B 430 ? 0.6767 0.7375 0.7139 -0.0119 0.0773  -0.0929 441 TYR B OH  
3735 N N   . GLY B 431 ? 0.4199 0.4776 0.5511 0.0526  0.0734  -0.1092 442 GLY B N   
3736 C CA  . GLY B 431 ? 0.3618 0.4450 0.5173 0.0591  0.0708  -0.1024 442 GLY B CA  
3737 C C   . GLY B 431 ? 0.3382 0.4215 0.4951 0.0537  0.0577  -0.0907 442 GLY B C   
3738 O O   . GLY B 431 ? 0.3329 0.4008 0.4721 0.0435  0.0518  -0.0874 442 GLY B O   
3739 N N   . PRO B 432 ? 0.3403 0.4427 0.5185 0.0613  0.0532  -0.0842 443 PRO B N   
3740 C CA  . PRO B 432 ? 0.2901 0.3961 0.4695 0.0551  0.0417  -0.0739 443 PRO B CA  
3741 C C   . PRO B 432 ? 0.3163 0.3939 0.4823 0.0540  0.0330  -0.0692 443 PRO B C   
3742 O O   . PRO B 432 ? 0.2883 0.3644 0.4480 0.0456  0.0253  -0.0625 443 PRO B O   
3743 C CB  . PRO B 432 ? 0.2796 0.4114 0.4846 0.0667  0.0388  -0.0690 443 PRO B CB  
3744 C CG  . PRO B 432 ? 0.3576 0.5084 0.5767 0.0764  0.0502  -0.0770 443 PRO B CG  
3745 C CD  . PRO B 432 ? 0.3934 0.5168 0.5953 0.0771  0.0585  -0.0862 443 PRO B CD  
3746 N N   . LYS B 433 ? 0.3168 0.3716 0.4779 0.0616  0.0347  -0.0729 444 LYS B N   
3747 C CA  . LYS B 433 ? 0.3707 0.4022 0.5210 0.0590  0.0264  -0.0679 444 LYS B CA  
3748 C C   . LYS B 433 ? 0.3138 0.3346 0.4433 0.0453  0.0240  -0.0691 444 LYS B C   
3749 O O   . LYS B 433 ? 0.3152 0.3227 0.4369 0.0415  0.0168  -0.0645 444 LYS B O   
3750 C CB  . LYS B 433 ? 0.3854 0.3930 0.5345 0.0689  0.0295  -0.0717 444 LYS B CB  
3751 C CG  . LYS B 433 ? 0.3468 0.3593 0.5145 0.0847  0.0278  -0.0653 444 LYS B CG  
3752 C CD  . LYS B 433 ? 0.4909 0.4739 0.6545 0.0954  0.0331  -0.0693 444 LYS B CD  
3753 C CE  . LYS B 433 ? 0.4565 0.4416 0.6365 0.1132  0.0306  -0.0604 444 LYS B CE  
3754 N NZ  . LYS B 433 ? 0.4343 0.3828 0.6064 0.1237  0.0370  -0.0640 444 LYS B NZ  
3755 N N   . VAL B 434 ? 0.3036 0.3312 0.4238 0.0382  0.0298  -0.0742 445 VAL B N   
3756 C CA  . VAL B 434 ? 0.2532 0.2741 0.3543 0.0272  0.0264  -0.0725 445 VAL B CA  
3757 C C   . VAL B 434 ? 0.2629 0.2897 0.3655 0.0233  0.0184  -0.0627 445 VAL B C   
3758 O O   . VAL B 434 ? 0.2812 0.2998 0.3714 0.0183  0.0130  -0.0589 445 VAL B O   
3759 C CB  . VAL B 434 ? 0.3461 0.3726 0.4351 0.0210  0.0344  -0.0781 445 VAL B CB  
3760 C CG1 . VAL B 434 ? 0.3242 0.3457 0.4113 0.0249  0.0435  -0.0891 445 VAL B CG1 
3761 C CG2 . VAL B 434 ? 0.3296 0.3753 0.4266 0.0181  0.0381  -0.0753 445 VAL B CG2 
3762 N N   . ASP B 435 ? 0.2535 0.2962 0.3710 0.0255  0.0180  -0.0590 446 ASP B N   
3763 C CA  . ASP B 435 ? 0.2288 0.2760 0.3464 0.0208  0.0113  -0.0511 446 ASP B CA  
3764 C C   . ASP B 435 ? 0.2677 0.3061 0.3881 0.0246  0.0028  -0.0454 446 ASP B C   
3765 O O   . ASP B 435 ? 0.2557 0.2910 0.3694 0.0201  -0.0027 -0.0399 446 ASP B O   
3766 C CB  . ASP B 435 ? 0.2815 0.3509 0.4141 0.0201  0.0129  -0.0498 446 ASP B CB  
3767 C CG  . ASP B 435 ? 0.2646 0.3437 0.3922 0.0122  0.0216  -0.0543 446 ASP B CG  
3768 O OD1 . ASP B 435 ? 0.2525 0.3186 0.3613 0.0059  0.0245  -0.0552 446 ASP B OD1 
3769 O OD2 . ASP B 435 ? 0.2407 0.3423 0.3833 0.0119  0.0253  -0.0561 446 ASP B OD2 
3770 N N   . ILE B 436 ? 0.2664 0.2999 0.3961 0.0332  0.0024  -0.0464 447 ILE B N   
3771 C CA  . ILE B 436 ? 0.2165 0.2385 0.3466 0.0358  -0.0046 -0.0408 447 ILE B CA  
3772 C C   . ILE B 436 ? 0.2781 0.2841 0.3920 0.0293  -0.0064 -0.0422 447 ILE B C   
3773 O O   . ILE B 436 ? 0.2577 0.2603 0.3676 0.0259  -0.0126 -0.0365 447 ILE B O   
3774 C CB  . ILE B 436 ? 0.2283 0.2442 0.3696 0.0472  -0.0031 -0.0410 447 ILE B CB  
3775 C CG1 . ILE B 436 ? 0.2633 0.3015 0.4232 0.0553  -0.0036 -0.0373 447 ILE B CG1 
3776 C CG2 . ILE B 436 ? 0.2834 0.2802 0.4195 0.0476  -0.0086 -0.0360 447 ILE B CG2 
3777 C CD1 . ILE B 436 ? 0.3388 0.3892 0.5028 0.0524  -0.0121 -0.0282 447 ILE B CD1 
3778 N N   . TRP B 437 ? 0.2862 0.2853 0.3909 0.0270  -0.0011 -0.0499 448 TRP B N   
3779 C CA  . TRP B 437 ? 0.2846 0.2753 0.3739 0.0196  -0.0033 -0.0516 448 TRP B CA  
3780 C C   . TRP B 437 ? 0.2559 0.2551 0.3382 0.0150  -0.0074 -0.0457 448 TRP B C   
3781 O O   . TRP B 437 ? 0.2387 0.2364 0.3162 0.0120  -0.0130 -0.0415 448 TRP B O   
3782 C CB  . TRP B 437 ? 0.2724 0.2586 0.3513 0.0170  0.0032  -0.0611 448 TRP B CB  
3783 C CG  . TRP B 437 ? 0.2880 0.2712 0.3511 0.0088  -0.0001 -0.0627 448 TRP B CG  
3784 C CD1 . TRP B 437 ? 0.3334 0.3259 0.3861 0.0049  -0.0030 -0.0590 448 TRP B CD1 
3785 C CD2 . TRP B 437 ? 0.3070 0.2787 0.3628 0.0035  -0.0011 -0.0679 448 TRP B CD2 
3786 N NE1 . TRP B 437 ? 0.2756 0.2679 0.3171 -0.0013 -0.0065 -0.0612 448 TRP B NE1 
3787 C CE2 . TRP B 437 ? 0.2828 0.2630 0.3258 -0.0040 -0.0054 -0.0673 448 TRP B CE2 
3788 C CE3 . TRP B 437 ? 0.3215 0.2754 0.3791 0.0042  0.0017  -0.0730 448 TRP B CE3 
3789 C CZ2 . TRP B 437 ? 0.3674 0.3436 0.4009 -0.0128 -0.0076 -0.0725 448 TRP B CZ2 
3790 C CZ3 . TRP B 437 ? 0.4146 0.3587 0.4605 -0.0055 0.0006  -0.0786 448 TRP B CZ3 
3791 C CH2 . TRP B 437 ? 0.4128 0.3703 0.4474 -0.0149 -0.0043 -0.0787 448 TRP B CH2 
3792 N N   . SER B 438 ? 0.2332 0.2407 0.3140 0.0142  -0.0038 -0.0454 449 SER B N   
3793 C CA  . SER B 438 ? 0.2300 0.2399 0.3011 0.0109  -0.0060 -0.0400 449 SER B CA  
3794 C C   . SER B 438 ? 0.2624 0.2739 0.3393 0.0116  -0.0118 -0.0332 449 SER B C   
3795 O O   . SER B 438 ? 0.2357 0.2456 0.3043 0.0104  -0.0150 -0.0289 449 SER B O   
3796 C CB  . SER B 438 ? 0.2330 0.2475 0.3005 0.0085  0.0002  -0.0409 449 SER B CB  
3797 O OG  . SER B 438 ? 0.2708 0.2845 0.3309 0.0072  0.0063  -0.0471 449 SER B OG  
3798 N N   . LEU B 439 ? 0.2293 0.2453 0.3202 0.0143  -0.0130 -0.0320 450 LEU B N   
3799 C CA  . LEU B 439 ? 0.2404 0.2584 0.3354 0.0143  -0.0187 -0.0257 450 LEU B CA  
3800 C C   . LEU B 439 ? 0.2480 0.2591 0.3394 0.0141  -0.0234 -0.0232 450 LEU B C   
3801 O O   . LEU B 439 ? 0.2252 0.2373 0.3124 0.0123  -0.0269 -0.0186 450 LEU B O   
3802 C CB  . LEU B 439 ? 0.2168 0.2434 0.3270 0.0181  -0.0200 -0.0241 450 LEU B CB  
3803 C CG  . LEU B 439 ? 0.3539 0.3829 0.4667 0.0177  -0.0264 -0.0173 450 LEU B CG  
3804 C CD1 . LEU B 439 ? 0.3102 0.3433 0.4154 0.0117  -0.0265 -0.0157 450 LEU B CD1 
3805 C CD2 . LEU B 439 ? 0.4209 0.4586 0.5479 0.0235  -0.0291 -0.0142 450 LEU B CD2 
3806 N N   . GLY B 440 ? 0.2405 0.2443 0.3328 0.0150  -0.0228 -0.0268 451 GLY B N   
3807 C CA  . GLY B 440 ? 0.2652 0.2630 0.3528 0.0116  -0.0263 -0.0256 451 GLY B CA  
3808 C C   . GLY B 440 ? 0.3035 0.3070 0.3804 0.0078  -0.0277 -0.0253 451 GLY B C   
3809 O O   . GLY B 440 ? 0.2187 0.2261 0.2939 0.0056  -0.0315 -0.0212 451 GLY B O   
3810 N N   . ILE B 441 ? 0.2023 0.2080 0.2717 0.0077  -0.0244 -0.0289 452 ILE B N   
3811 C CA  . ILE B 441 ? 0.2200 0.2324 0.2785 0.0069  -0.0259 -0.0270 452 ILE B CA  
3812 C C   . ILE B 441 ? 0.2074 0.2226 0.2647 0.0100  -0.0271 -0.0204 452 ILE B C   
3813 O O   . ILE B 441 ? 0.1987 0.2203 0.2515 0.0111  -0.0298 -0.0168 452 ILE B O   
3814 C CB  . ILE B 441 ? 0.2252 0.2374 0.2740 0.0070  -0.0216 -0.0308 452 ILE B CB  
3815 C CG1 . ILE B 441 ? 0.2515 0.2602 0.2993 0.0034  -0.0195 -0.0390 452 ILE B CG1 
3816 C CG2 . ILE B 441 ? 0.2489 0.2680 0.2853 0.0089  -0.0235 -0.0265 452 ILE B CG2 
3817 C CD1 . ILE B 441 ? 0.3214 0.3345 0.3644 -0.0022 -0.0238 -0.0410 452 ILE B CD1 
3818 N N   . MET B 442 ? 0.2196 0.2314 0.2806 0.0111  -0.0246 -0.0193 453 MET B N   
3819 C CA  . MET B 442 ? 0.1845 0.1955 0.2416 0.0124  -0.0246 -0.0146 453 MET B CA  
3820 C C   . MET B 442 ? 0.2019 0.2165 0.2645 0.0121  -0.0291 -0.0110 453 MET B C   
3821 O O   . MET B 442 ? 0.2269 0.2425 0.2838 0.0140  -0.0294 -0.0077 453 MET B O   
3822 C CB  . MET B 442 ? 0.2574 0.2657 0.3168 0.0104  -0.0209 -0.0156 453 MET B CB  
3823 C CG  . MET B 442 ? 0.2369 0.2391 0.2866 0.0096  -0.0186 -0.0127 453 MET B CG  
3824 S SD  . MET B 442 ? 0.2839 0.2838 0.3328 0.0031  -0.0130 -0.0156 453 MET B SD  
3825 C CE  . MET B 442 ? 0.2957 0.3099 0.3635 0.0012  -0.0178 -0.0161 453 MET B CE  
3826 N N   . ALA B 443 ? 0.2128 0.2280 0.2851 0.0103  -0.0317 -0.0115 454 ALA B N   
3827 C CA  . ALA B 443 ? 0.2485 0.2662 0.3239 0.0088  -0.0355 -0.0075 454 ALA B CA  
3828 C C   . ALA B 443 ? 0.2873 0.3110 0.3587 0.0074  -0.0372 -0.0069 454 ALA B C   
3829 O O   . ALA B 443 ? 0.2274 0.2571 0.2975 0.0072  -0.0385 -0.0034 454 ALA B O   
3830 C CB  . ALA B 443 ? 0.2275 0.2412 0.3119 0.0080  -0.0375 -0.0069 454 ALA B CB  
3831 N N   . ILE B 444 ? 0.2073 0.2322 0.2764 0.0058  -0.0369 -0.0108 455 ILE B N   
3832 C CA  . ILE B 444 ? 0.1721 0.2088 0.2374 0.0038  -0.0389 -0.0106 455 ILE B CA  
3833 C C   . ILE B 444 ? 0.2411 0.2854 0.3000 0.0108  -0.0380 -0.0071 455 ILE B C   
3834 O O   . ILE B 444 ? 0.2358 0.2923 0.2947 0.0123  -0.0394 -0.0040 455 ILE B O   
3835 C CB  . ILE B 444 ? 0.2428 0.2803 0.3051 -0.0005 -0.0389 -0.0164 455 ILE B CB  
3836 C CG1 . ILE B 444 ? 0.2772 0.3034 0.3435 -0.0075 -0.0388 -0.0201 455 ILE B CG1 
3837 C CG2 . ILE B 444 ? 0.2619 0.3183 0.3198 -0.0019 -0.0417 -0.0159 455 ILE B CG2 
3838 C CD1 . ILE B 444 ? 0.3236 0.3477 0.3843 -0.0132 -0.0376 -0.0278 455 ILE B CD1 
3839 N N   . GLU B 445 ? 0.2244 0.2608 0.2769 0.0154  -0.0347 -0.0074 456 GLU B N   
3840 C CA  . GLU B 445 ? 0.2240 0.2605 0.2675 0.0230  -0.0325 -0.0033 456 GLU B CA  
3841 C C   . GLU B 445 ? 0.2394 0.2747 0.2841 0.0250  -0.0317 -0.0002 456 GLU B C   
3842 O O   . GLU B 445 ? 0.2458 0.2879 0.2865 0.0314  -0.0310 0.0030  456 GLU B O   
3843 C CB  . GLU B 445 ? 0.2397 0.2624 0.2743 0.0251  -0.0278 -0.0040 456 GLU B CB  
3844 C CG  . GLU B 445 ? 0.2912 0.3067 0.3127 0.0335  -0.0241 0.0008  456 GLU B CG  
3845 C CD  . GLU B 445 ? 0.4611 0.4602 0.4711 0.0332  -0.0186 0.0005  456 GLU B CD  
3846 O OE1 . GLU B 445 ? 0.4816 0.4810 0.4936 0.0281  -0.0181 -0.0033 456 GLU B OE1 
3847 O OE2 . GLU B 445 ? 0.4122 0.3970 0.4100 0.0378  -0.0138 0.0038  456 GLU B OE2 
3848 N N   . MET B 446 ? 0.2456 0.2740 0.2957 0.0201  -0.0317 -0.0012 457 MET B N   
3849 C CA  . MET B 446 ? 0.2436 0.2705 0.2922 0.0207  -0.0306 0.0010  457 MET B CA  
3850 C C   . MET B 446 ? 0.2409 0.2817 0.2938 0.0204  -0.0331 0.0032  457 MET B C   
3851 O O   . MET B 446 ? 0.2516 0.2956 0.2999 0.0251  -0.0307 0.0051  457 MET B O   
3852 C CB  . MET B 446 ? 0.2022 0.2232 0.2556 0.0149  -0.0314 0.0000  457 MET B CB  
3853 C CG  . MET B 446 ? 0.2418 0.2525 0.2905 0.0137  -0.0277 -0.0024 457 MET B CG  
3854 S SD  . MET B 446 ? 0.2477 0.2605 0.3037 0.0071  -0.0300 -0.0028 457 MET B SD  
3855 C CE  . MET B 446 ? 0.1999 0.2166 0.2682 0.0067  -0.0317 -0.0048 457 MET B CE  
3856 N N   . ILE B 447 ? 0.2063 0.2549 0.2670 0.0146  -0.0368 0.0026  458 ILE B N   
3857 C CA  . ILE B 447 ? 0.2222 0.2849 0.2867 0.0113  -0.0386 0.0046  458 ILE B CA  
3858 C C   . ILE B 447 ? 0.2516 0.3324 0.3153 0.0159  -0.0386 0.0050  458 ILE B C   
3859 O O   . ILE B 447 ? 0.2265 0.3228 0.2922 0.0171  -0.0381 0.0070  458 ILE B O   
3860 C CB  . ILE B 447 ? 0.2692 0.3297 0.3399 0.0016  -0.0416 0.0041  458 ILE B CB  
3861 C CG1 . ILE B 447 ? 0.2811 0.3531 0.3538 -0.0039 -0.0422 0.0071  458 ILE B CG1 
3862 C CG2 . ILE B 447 ? 0.2471 0.3088 0.3190 -0.0023 -0.0430 0.0002  458 ILE B CG2 
3863 C CD1 . ILE B 447 ? 0.2934 0.3627 0.3633 -0.0022 -0.0407 0.0103  458 ILE B CD1 
3864 N N   . GLU B 448 ? 0.2126 0.2947 0.2733 0.0191  -0.0393 0.0034  459 GLU B N   
3865 C CA  . GLU B 448 ? 0.2420 0.3457 0.3023 0.0240  -0.0407 0.0048  459 GLU B CA  
3866 C C   . GLU B 448 ? 0.2799 0.3819 0.3320 0.0386  -0.0372 0.0086  459 GLU B C   
3867 O O   . GLU B 448 ? 0.2639 0.3866 0.3163 0.0464  -0.0382 0.0115  459 GLU B O   
3868 C CB  . GLU B 448 ? 0.3327 0.4421 0.3922 0.0189  -0.0439 0.0013  459 GLU B CB  
3869 C CG  . GLU B 448 ? 0.3111 0.4206 0.3764 0.0044  -0.0463 -0.0032 459 GLU B CG  
3870 C CD  . GLU B 448 ? 0.5630 0.6807 0.6254 -0.0019 -0.0490 -0.0081 459 GLU B CD  
3871 O OE1 . GLU B 448 ? 0.5007 0.6196 0.5562 0.0050  -0.0491 -0.0079 459 GLU B OE1 
3872 O OE2 . GLU B 448 ? 0.6055 0.7274 0.6707 -0.0146 -0.0506 -0.0122 459 GLU B OE2 
3873 N N   . GLY B 449 ? 0.2537 0.3318 0.2977 0.0425  -0.0330 0.0089  460 GLY B N   
3874 C CA  . GLY B 449 ? 0.3026 0.3721 0.3354 0.0558  -0.0282 0.0125  460 GLY B CA  
3875 C C   . GLY B 449 ? 0.3309 0.3935 0.3535 0.0623  -0.0276 0.0147  460 GLY B C   
3876 O O   . GLY B 449 ? 0.4149 0.4660 0.4256 0.0744  -0.0229 0.0188  460 GLY B O   
3877 N N   . GLU B 450 ? 0.2993 0.3680 0.3245 0.0554  -0.0316 0.0122  461 GLU B N   
3878 C CA  . GLU B 450 ? 0.4064 0.4712 0.4206 0.0605  -0.0313 0.0144  461 GLU B CA  
3879 C C   . GLU B 450 ? 0.3536 0.4156 0.3703 0.0486  -0.0334 0.0086  461 GLU B C   
3880 O O   . GLU B 450 ? 0.3422 0.4113 0.3702 0.0386  -0.0363 0.0038  461 GLU B O   
3881 C CB  . GLU B 450 ? 0.4930 0.5839 0.5062 0.0703  -0.0353 0.0194  461 GLU B CB  
3882 C CG  . GLU B 450 ? 0.4522 0.5729 0.4785 0.0607  -0.0420 0.0157  461 GLU B CG  
3883 C CD  . GLU B 450 ? 0.6844 0.8382 0.7124 0.0700  -0.0464 0.0207  461 GLU B CD  
3884 O OE1 . GLU B 450 ? 0.6071 0.7613 0.6294 0.0868  -0.0437 0.0278  461 GLU B OE1 
3885 O OE2 . GLU B 450 ? 0.7847 0.9643 0.8192 0.0606  -0.0523 0.0173  461 GLU B OE2 
3886 N N   . PRO B 451 ? 0.4594 0.5098 0.4649 0.0497  -0.0310 0.0089  462 PRO B N   
3887 C CA  . PRO B 451 ? 0.3647 0.4145 0.3722 0.0395  -0.0320 0.0025  462 PRO B CA  
3888 C C   . PRO B 451 ? 0.3846 0.4577 0.3950 0.0355  -0.0380 0.0001  462 PRO B C   
3889 O O   . PRO B 451 ? 0.3952 0.4871 0.4022 0.0425  -0.0416 0.0050  462 PRO B O   
3890 C CB  . PRO B 451 ? 0.4199 0.4532 0.4121 0.0423  -0.0269 0.0044  462 PRO B CB  
3891 C CG  . PRO B 451 ? 0.5329 0.5636 0.5127 0.0555  -0.0256 0.0133  462 PRO B CG  
3892 C CD  . PRO B 451 ? 0.4411 0.4762 0.4298 0.0601  -0.0263 0.0152  462 PRO B CD  
3893 N N   . PRO B 452 ? 0.3671 0.4403 0.3832 0.0242  -0.0390 -0.0076 463 PRO B N   
3894 C CA  . PRO B 452 ? 0.5117 0.6037 0.5270 0.0170  -0.0438 -0.0120 463 PRO B CA  
3895 C C   . PRO B 452 ? 0.5275 0.6262 0.5280 0.0204  -0.0446 -0.0104 463 PRO B C   
3896 O O   . PRO B 452 ? 0.4476 0.5310 0.4379 0.0263  -0.0401 -0.0072 463 PRO B O   
3897 C CB  . PRO B 452 ? 0.4837 0.5629 0.5046 0.0055  -0.0418 -0.0212 463 PRO B CB  
3898 C CG  . PRO B 452 ? 0.6062 0.6677 0.6355 0.0078  -0.0382 -0.0197 463 PRO B CG  
3899 C CD  . PRO B 452 ? 0.4707 0.5261 0.4937 0.0179  -0.0354 -0.0129 463 PRO B CD  
3900 N N   . TYR B 453 ? 0.4161 0.5395 0.4143 0.0159  -0.0504 -0.0122 464 TYR B N   
3901 C CA  . TYR B 453 ? 0.3814 0.5164 0.3646 0.0170  -0.0528 -0.0113 464 TYR B CA  
3902 C C   . TYR B 453 ? 0.6300 0.7706 0.6034 0.0336  -0.0537 0.0011  464 TYR B C   
3903 O O   . TYR B 453 ? 0.5485 0.6927 0.5062 0.0370  -0.0546 0.0043  464 TYR B O   
3904 C CB  . TYR B 453 ? 0.4603 0.5749 0.4337 0.0107  -0.0472 -0.0181 464 TYR B CB  
3905 C CG  . TYR B 453 ? 0.3755 0.4790 0.3567 -0.0026 -0.0445 -0.0301 464 TYR B CG  
3906 C CD1 . TYR B 453 ? 0.4480 0.5662 0.4310 -0.0149 -0.0487 -0.0378 464 TYR B CD1 
3907 C CD2 . TYR B 453 ? 0.3930 0.4716 0.3794 -0.0028 -0.0376 -0.0336 464 TYR B CD2 
3908 C CE1 . TYR B 453 ? 0.4162 0.5186 0.4034 -0.0261 -0.0451 -0.0484 464 TYR B CE1 
3909 C CE2 . TYR B 453 ? 0.3979 0.4652 0.3911 -0.0120 -0.0348 -0.0433 464 TYR B CE2 
3910 C CZ  . TYR B 453 ? 0.4156 0.4920 0.4081 -0.0231 -0.0381 -0.0506 464 TYR B CZ  
3911 O OH  . TYR B 453 ? 0.5208 0.5804 0.5173 -0.0314 -0.0342 -0.0601 464 TYR B OH  
3912 N N   . LEU B 454 ? 0.5366 0.6769 0.5170 0.0445  -0.0531 0.0082  465 LEU B N   
3913 C CA  . LEU B 454 ? 0.5654 0.7023 0.5347 0.0623  -0.0518 0.0200  465 LEU B CA  
3914 C C   . LEU B 454 ? 0.6214 0.7893 0.5824 0.0697  -0.0590 0.0265  465 LEU B C   
3915 O O   . LEU B 454 ? 0.6555 0.8163 0.5998 0.0822  -0.0579 0.0358  465 LEU B O   
3916 C CB  . LEU B 454 ? 0.5667 0.7001 0.5459 0.0718  -0.0495 0.0245  465 LEU B CB  
3917 C CG  . LEU B 454 ? 0.7094 0.8208 0.6758 0.0889  -0.0437 0.0344  465 LEU B CG  
3918 C CD1 . LEU B 454 ? 0.6728 0.7485 0.6265 0.0837  -0.0364 0.0326  465 LEU B CD1 
3919 C CD2 . LEU B 454 ? 0.7095 0.8169 0.6864 0.0949  -0.0406 0.0355  465 LEU B CD2 
3920 N N   . ASN B 455 ? 0.4554 0.6588 0.4270 0.0619  -0.0665 0.0223  466 ASN B N   
3921 C CA  . ASN B 455 ? 0.6552 0.8959 0.6208 0.0671  -0.0748 0.0276  466 ASN B CA  
3922 C C   . ASN B 455 ? 0.5995 0.8463 0.5517 0.0540  -0.0779 0.0212  466 ASN B C   
3923 O O   . ASN B 455 ? 0.6755 0.9563 0.6213 0.0562  -0.0859 0.0250  466 ASN B O   
3924 C CB  . ASN B 455 ? 0.7470 1.0278 0.7308 0.0642  -0.0808 0.0263  466 ASN B CB  
3925 C CG  . ASN B 455 ? 0.8351 1.1208 0.8308 0.0411  -0.0820 0.0127  466 ASN B CG  
3926 O OD1 . ASN B 455 ? 0.8674 1.1284 0.8574 0.0273  -0.0786 0.0035  466 ASN B OD1 
3927 N ND2 . ASN B 455 ? 0.9320 1.2396 0.9436 0.0358  -0.0828 0.0111  466 ASN B ND2 
3928 N N   . GLU B 456 ? 0.5141 0.7320 0.4621 0.0405  -0.0721 0.0112  467 GLU B N   
3929 C CA  . GLU B 456 ? 0.5197 0.7418 0.4542 0.0274  -0.0736 0.0033  467 GLU B CA  
3930 C C   . GLU B 456 ? 0.4949 0.6976 0.4076 0.0354  -0.0694 0.0098  467 GLU B C   
3931 O O   . GLU B 456 ? 0.4736 0.6458 0.3827 0.0447  -0.0620 0.0156  467 GLU B O   
3932 C CB  . GLU B 456 ? 0.4875 0.6892 0.4287 0.0090  -0.0684 -0.0120 467 GLU B CB  
3933 C CG  . GLU B 456 ? 0.6171 0.8294 0.5769 -0.0014 -0.0707 -0.0188 467 GLU B CG  
3934 C CD  . GLU B 456 ? 0.5545 0.8056 0.5142 -0.0133 -0.0792 -0.0236 467 GLU B CD  
3935 O OE1 . GLU B 456 ? 0.6076 0.8781 0.5525 -0.0142 -0.0839 -0.0227 467 GLU B OE1 
3936 O OE2 . GLU B 456 ? 0.7438 1.0072 0.7174 -0.0231 -0.0813 -0.0283 467 GLU B OE2 
3937 N N   . ASN B 457 ? 0.4677 0.6875 0.3642 0.0292  -0.0737 0.0078  468 ASN B N   
3938 C CA  . ASN B 457 ? 0.4097 0.6094 0.2836 0.0325  -0.0686 0.0119  468 ASN B CA  
3939 C C   . ASN B 457 ? 0.3992 0.5657 0.2746 0.0204  -0.0581 -0.0003 468 ASN B C   
3940 O O   . ASN B 457 ? 0.4262 0.5917 0.3151 0.0073  -0.0570 -0.0134 468 ASN B O   
3941 C CB  . ASN B 457 ? 0.4821 0.7102 0.3371 0.0276  -0.0758 0.0120  468 ASN B CB  
3942 C CG  . ASN B 457 ? 0.6686 0.9325 0.5212 0.0428  -0.0864 0.0264  468 ASN B CG  
3943 O OD1 . ASN B 457 ? 0.6655 0.9603 0.5264 0.0345  -0.0930 0.0222  468 ASN B OD1 
3944 N ND2 . ASN B 457 ? 0.6453 0.8948 0.4921 0.0642  -0.0841 0.0427  468 ASN B ND2 
3945 N N   . PRO B 458 ? 0.4440 0.5830 0.3057 0.0250  -0.0498 0.0042  469 PRO B N   
3946 C CA  . PRO B 458 ? 0.3936 0.5055 0.2602 0.0152  -0.0394 -0.0068 469 PRO B CA  
3947 C C   . PRO B 458 ? 0.4107 0.5286 0.2748 -0.0011 -0.0382 -0.0225 469 PRO B C   
3948 O O   . PRO B 458 ? 0.4208 0.5253 0.2989 -0.0089 -0.0328 -0.0339 469 PRO B O   
3949 C CB  . PRO B 458 ? 0.5139 0.6028 0.3614 0.0215  -0.0315 0.0021  469 PRO B CB  
3950 C CG  . PRO B 458 ? 0.5719 0.6641 0.4121 0.0385  -0.0363 0.0191  469 PRO B CG  
3951 C CD  . PRO B 458 ? 0.5249 0.6545 0.3679 0.0403  -0.0485 0.0204  469 PRO B CD  
3952 N N   . LEU B 459 ? 0.3493 0.4868 0.1948 -0.0059 -0.0430 -0.0236 470 LEU B N   
3953 C CA  . LEU B 459 ? 0.3693 0.5096 0.2088 -0.0224 -0.0406 -0.0401 470 LEU B CA  
3954 C C   . LEU B 459 ? 0.4409 0.5920 0.2977 -0.0326 -0.0452 -0.0510 470 LEU B C   
3955 O O   . LEU B 459 ? 0.4097 0.5463 0.2712 -0.0437 -0.0390 -0.0656 470 LEU B O   
3956 C CB  . LEU B 459 ? 0.4715 0.6321 0.2845 -0.0262 -0.0452 -0.0384 470 LEU B CB  
3957 C CG  . LEU B 459 ? 0.3962 0.5395 0.1873 -0.0231 -0.0367 -0.0336 470 LEU B CG  
3958 C CD1 . LEU B 459 ? 0.4243 0.5899 0.1871 -0.0271 -0.0424 -0.0310 470 LEU B CD1 
3959 C CD2 . LEU B 459 ? 0.4801 0.5974 0.2753 -0.0315 -0.0232 -0.0472 470 LEU B CD2 
3960 N N   . ARG B 460 ? 0.3944 0.5706 0.2599 -0.0287 -0.0554 -0.0438 471 ARG B N   
3961 C CA  . ARG B 460 ? 0.4141 0.6000 0.2961 -0.0395 -0.0591 -0.0530 471 ARG B CA  
3962 C C   . ARG B 460 ? 0.3776 0.5351 0.2795 -0.0377 -0.0520 -0.0560 471 ARG B C   
3963 O O   . ARG B 460 ? 0.3866 0.5327 0.2953 -0.0497 -0.0487 -0.0686 471 ARG B O   
3964 C CB  . ARG B 460 ? 0.3799 0.6021 0.2690 -0.0343 -0.0707 -0.0433 471 ARG B CB  
3965 C CG  . ARG B 460 ? 0.4175 0.6521 0.3242 -0.0463 -0.0743 -0.0511 471 ARG B CG  
3966 C CD  . ARG B 460 ? 0.4273 0.6669 0.3249 -0.0693 -0.0744 -0.0683 471 ARG B CD  
3967 N NE  . ARG B 460 ? 0.3988 0.6483 0.3109 -0.0824 -0.0772 -0.0750 471 ARG B NE  
3968 C CZ  . ARG B 460 ? 0.4750 0.7197 0.3825 -0.1031 -0.0750 -0.0897 471 ARG B CZ  
3969 N NH1 . ARG B 460 ? 0.4184 0.6493 0.3077 -0.1129 -0.0700 -0.1007 471 ARG B NH1 
3970 N NH2 . ARG B 460 ? 0.4201 0.6689 0.3415 -0.1128 -0.0754 -0.0918 471 ARG B NH2 
3971 N N   . ALA B 461 ? 0.3649 0.5090 0.2743 -0.0230 -0.0492 -0.0447 472 ALA B N   
3972 C CA  . ALA B 461 ? 0.3159 0.4359 0.2431 -0.0212 -0.0432 -0.0469 472 ALA B CA  
3973 C C   . ALA B 461 ? 0.3930 0.4887 0.3184 -0.0279 -0.0335 -0.0584 472 ALA B C   
3974 O O   . ALA B 461 ? 0.3305 0.4118 0.2691 -0.0323 -0.0300 -0.0658 472 ALA B O   
3975 C CB  . ALA B 461 ? 0.3133 0.4242 0.2451 -0.0059 -0.0417 -0.0336 472 ALA B CB  
3976 N N   . LEU B 462 ? 0.3862 0.4772 0.2950 -0.0279 -0.0286 -0.0597 473 LEU B N   
3977 C CA  . LEU B 462 ? 0.3895 0.4612 0.2968 -0.0336 -0.0184 -0.0717 473 LEU B CA  
3978 C C   . LEU B 462 ? 0.3726 0.4429 0.2793 -0.0467 -0.0179 -0.0867 473 LEU B C   
3979 O O   . LEU B 462 ? 0.4338 0.4846 0.3504 -0.0486 -0.0109 -0.0955 473 LEU B O   
3980 C CB  . LEU B 462 ? 0.4949 0.5655 0.3818 -0.0332 -0.0130 -0.0709 473 LEU B CB  
3981 C CG  . LEU B 462 ? 0.6221 0.6795 0.5099 -0.0240 -0.0065 -0.0617 473 LEU B CG  
3982 C CD1 . LEU B 462 ? 0.6587 0.6997 0.5563 -0.0265 0.0046  -0.0719 473 LEU B CD1 
3983 C CD2 . LEU B 462 ? 0.7112 0.7667 0.6126 -0.0142 -0.0110 -0.0497 473 LEU B CD2 
3984 N N   . TYR B 463 ? 0.4197 0.5102 0.3139 -0.0559 -0.0250 -0.0898 474 TYR B N   
3985 C CA  . TYR B 463 ? 0.4019 0.4892 0.2927 -0.0712 -0.0242 -0.1051 474 TYR B CA  
3986 C C   . TYR B 463 ? 0.4939 0.5713 0.4041 -0.0731 -0.0254 -0.1062 474 TYR B C   
3987 O O   . TYR B 463 ? 0.4846 0.5395 0.3972 -0.0800 -0.0188 -0.1178 474 TYR B O   
3988 C CB  . TYR B 463 ? 0.3975 0.5143 0.2715 -0.0822 -0.0331 -0.1073 474 TYR B CB  
3989 C CG  . TYR B 463 ? 0.5175 0.6301 0.3835 -0.1015 -0.0315 -0.1247 474 TYR B CG  
3990 C CD1 . TYR B 463 ? 0.6592 0.7581 0.5065 -0.1106 -0.0232 -0.1391 474 TYR B CD1 
3991 C CD2 . TYR B 463 ? 0.5753 0.6954 0.4508 -0.1117 -0.0370 -0.1275 474 TYR B CD2 
3992 C CE1 . TYR B 463 ? 0.7037 0.7938 0.5408 -0.1291 -0.0204 -0.1565 474 TYR B CE1 
3993 C CE2 . TYR B 463 ? 0.5573 0.6690 0.4226 -0.1317 -0.0344 -0.1443 474 TYR B CE2 
3994 C CZ  . TYR B 463 ? 0.6830 0.7775 0.5297 -0.1393 -0.0257 -0.1580 474 TYR B CZ  
3995 O OH  . TYR B 463 ? 0.7582 0.8374 0.5985 -0.1540 -0.0207 -0.1692 474 TYR B OH  
3996 N N   . LEU B 464 ? 0.3542 0.4465 0.2771 -0.0663 -0.0331 -0.0938 475 LEU B N   
3997 C CA  . LEU B 464 ? 0.4331 0.5180 0.3730 -0.0686 -0.0343 -0.0936 475 LEU B CA  
3998 C C   . LEU B 464 ? 0.3755 0.4299 0.3278 -0.0607 -0.0259 -0.0942 475 LEU B C   
3999 O O   . LEU B 464 ? 0.4810 0.5173 0.4400 -0.0662 -0.0227 -0.1004 475 LEU B O   
4000 C CB  . LEU B 464 ? 0.3232 0.4319 0.2736 -0.0611 -0.0431 -0.0799 475 LEU B CB  
4001 C CG  . LEU B 464 ? 0.3682 0.5135 0.3107 -0.0681 -0.0526 -0.0785 475 LEU B CG  
4002 C CD1 . LEU B 464 ? 0.3910 0.5590 0.3441 -0.0549 -0.0594 -0.0634 475 LEU B CD1 
4003 C CD2 . LEU B 464 ? 0.3671 0.5175 0.3090 -0.0883 -0.0544 -0.0904 475 LEU B CD2 
4004 N N   . ILE B 465 ? 0.3866 0.4354 0.3413 -0.0482 -0.0221 -0.0875 476 ILE B N   
4005 C CA  . ILE B 465 ? 0.3596 0.3860 0.3273 -0.0409 -0.0147 -0.0880 476 ILE B CA  
4006 C C   . ILE B 465 ? 0.4316 0.4381 0.3943 -0.0464 -0.0060 -0.1021 476 ILE B C   
4007 O O   . ILE B 465 ? 0.4431 0.4306 0.4163 -0.0447 -0.0019 -0.1055 476 ILE B O   
4008 C CB  . ILE B 465 ? 0.3887 0.4156 0.3579 -0.0297 -0.0117 -0.0797 476 ILE B CB  
4009 C CG1 . ILE B 465 ? 0.3161 0.3550 0.2905 -0.0224 -0.0185 -0.0661 476 ILE B CG1 
4010 C CG2 . ILE B 465 ? 0.3905 0.3997 0.3729 -0.0238 -0.0037 -0.0823 476 ILE B CG2 
4011 C CD1 . ILE B 465 ? 0.3913 0.4288 0.3604 -0.0144 -0.0151 -0.0585 476 ILE B CD1 
4012 N N   . ALA B 466 ? 0.4296 0.4395 0.3749 -0.0523 -0.0026 -0.1104 477 ALA B N   
4013 C CA  . ALA B 466 ? 0.4747 0.4647 0.4132 -0.0565 0.0076  -0.1250 477 ALA B CA  
4014 C C   . ALA B 466 ? 0.6404 0.6153 0.5765 -0.0677 0.0077  -0.1348 477 ALA B C   
4015 O O   . ALA B 466 ? 0.6312 0.5801 0.5697 -0.0660 0.0166  -0.1435 477 ALA B O   
4016 C CB  . ALA B 466 ? 0.4283 0.4272 0.3456 -0.0621 0.0109  -0.1319 477 ALA B CB  
4017 N N   . THR B 467 ? 0.5634 0.5539 0.4942 -0.0791 -0.0013 -0.1336 478 THR B N   
4018 C CA  . THR B 467 ? 0.5808 0.5578 0.5041 -0.0947 -0.0004 -0.1449 478 THR B CA  
4019 C C   . THR B 467 ? 0.6985 0.6687 0.6362 -0.0956 -0.0044 -0.1382 478 THR B C   
4020 O O   . THR B 467 ? 0.7789 0.7210 0.7148 -0.1019 0.0012  -0.1458 478 THR B O   
4021 C CB  . THR B 467 ? 0.5728 0.5746 0.4780 -0.1115 -0.0070 -0.1508 478 THR B CB  
4022 O OG1 . THR B 467 ? 0.6606 0.6969 0.5731 -0.1084 -0.0188 -0.1370 478 THR B OG1 
4023 C CG2 . THR B 467 ? 0.5449 0.5510 0.4321 -0.1124 -0.0024 -0.1584 478 THR B CG2 
4024 N N   . ASN B 468 ? 0.7193 0.7126 0.6695 -0.0895 -0.0132 -0.1241 479 ASN B N   
4025 C CA  . ASN B 468 ? 0.5776 0.5654 0.5412 -0.0898 -0.0163 -0.1173 479 ASN B CA  
4026 C C   . ASN B 468 ? 0.7791 0.7470 0.7578 -0.0736 -0.0119 -0.1100 479 ASN B C   
4027 O O   . ASN B 468 ? 0.7561 0.7053 0.7418 -0.0741 -0.0105 -0.1081 479 ASN B O   
4028 C CB  . ASN B 468 ? 0.6850 0.7073 0.6555 -0.0902 -0.0269 -0.1062 479 ASN B CB  
4029 C CG  . ASN B 468 ? 0.7836 0.8306 0.7428 -0.1078 -0.0327 -0.1124 479 ASN B CG  
4030 O OD1 . ASN B 468 ? 0.9164 0.9532 0.8606 -0.1223 -0.0291 -0.1259 479 ASN B OD1 
4031 N ND2 . ASN B 468 ? 0.8447 0.9256 0.8110 -0.1070 -0.0416 -0.1030 479 ASN B ND2 
4032 N N   . GLY B 469 ? 0.7409 0.7133 0.7239 -0.0603 -0.0096 -0.1059 480 GLY B N   
4033 C CA  . GLY B 469 ? 0.6803 0.6431 0.6791 -0.0460 -0.0074 -0.0977 480 GLY B CA  
4034 C C   . GLY B 469 ? 0.8503 0.8310 0.8594 -0.0421 -0.0154 -0.0847 480 GLY B C   
4035 O O   . GLY B 469 ? 0.7372 0.7383 0.7444 -0.0385 -0.0195 -0.0787 480 GLY B O   
4036 N N   . THR B 470 ? 0.8728 0.8438 0.8911 -0.0420 -0.0170 -0.0800 481 THR B N   
4037 C CA  . THR B 470 ? 0.8051 0.7912 0.8329 -0.0383 -0.0235 -0.0685 481 THR B CA  
4038 C C   . THR B 470 ? 0.8415 0.8542 0.8638 -0.0453 -0.0300 -0.0666 481 THR B C   
4039 O O   . THR B 470 ? 0.8470 0.8645 0.8603 -0.0581 -0.0312 -0.0739 481 THR B O   
4040 C CB  . THR B 470 ? 0.7214 0.6929 0.7562 -0.0406 -0.0239 -0.0649 481 THR B CB  
4041 O OG1 . THR B 470 ? 0.7243 0.7116 0.7672 -0.0371 -0.0294 -0.0544 481 THR B OG1 
4042 C CG2 . THR B 470 ? 0.6218 0.5854 0.6472 -0.0567 -0.0236 -0.0722 481 THR B CG2 
4043 N N   . PRO B 471 ? 0.9186 0.9494 0.9450 -0.0369 -0.0340 -0.0574 482 PRO B N   
4044 C CA  . PRO B 471 ? 0.9826 1.0409 1.0063 -0.0404 -0.0403 -0.0539 482 PRO B CA  
4045 C C   . PRO B 471 ? 0.9111 0.9736 0.9415 -0.0489 -0.0430 -0.0526 482 PRO B C   
4046 O O   . PRO B 471 ? 0.8600 0.9042 0.8970 -0.0485 -0.0407 -0.0507 482 PRO B O   
4047 C CB  . PRO B 471 ? 0.8181 0.8858 0.8447 -0.0264 -0.0417 -0.0439 482 PRO B CB  
4048 C CG  . PRO B 471 ? 0.8484 0.8958 0.8837 -0.0200 -0.0378 -0.0410 482 PRO B CG  
4049 C CD  . PRO B 471 ? 0.7014 0.7280 0.7358 -0.0243 -0.0326 -0.0496 482 PRO B CD  
4050 N N   . GLU B 472 ? 0.8813 0.9701 0.9096 -0.0571 -0.0480 -0.0530 483 GLU B N   
4051 C CA  . GLU B 472 ? 0.9552 1.0511 0.9896 -0.0672 -0.0499 -0.0519 483 GLU B CA  
4052 C C   . GLU B 472 ? 0.9356 1.0423 0.9805 -0.0554 -0.0516 -0.0410 483 GLU B C   
4053 O O   . GLU B 472 ? 0.9198 1.0435 0.9654 -0.0433 -0.0538 -0.0351 483 GLU B O   
4054 C CB  . GLU B 472 ? 1.0890 1.2146 1.1190 -0.0818 -0.0545 -0.0570 483 GLU B CB  
4055 C CG  . GLU B 472 ? 1.2950 1.4115 1.3112 -0.0945 -0.0528 -0.0692 483 GLU B CG  
4056 C CD  . GLU B 472 ? 1.3822 1.4649 1.3934 -0.1088 -0.0468 -0.0778 483 GLU B CD  
4057 O OE1 . GLU B 472 ? 1.3031 1.3753 1.3209 -0.1120 -0.0454 -0.0737 483 GLU B OE1 
4058 O OE2 . GLU B 472 ? 1.2958 1.3602 1.2947 -0.1161 -0.0428 -0.0885 483 GLU B OE2 
4059 N N   . LEU B 473 ? 0.7450 0.8393 0.7960 -0.0585 -0.0499 -0.0381 484 LEU B N   
4060 C CA  . LEU B 473 ? 0.5997 0.7050 0.6590 -0.0492 -0.0509 -0.0290 484 LEU B CA  
4061 C C   . LEU B 473 ? 0.5922 0.7347 0.6550 -0.0529 -0.0549 -0.0271 484 LEU B C   
4062 O O   . LEU B 473 ? 0.5426 0.6984 0.6042 -0.0685 -0.0565 -0.0322 484 LEU B O   
4063 C CB  . LEU B 473 ? 0.6212 0.7059 0.6841 -0.0531 -0.0485 -0.0261 484 LEU B CB  
4064 C CG  . LEU B 473 ? 0.5918 0.6445 0.6543 -0.0463 -0.0452 -0.0257 484 LEU B CG  
4065 C CD1 . LEU B 473 ? 0.6223 0.6569 0.6864 -0.0515 -0.0437 -0.0221 484 LEU B CD1 
4066 C CD2 . LEU B 473 ? 0.5952 0.6491 0.6606 -0.0312 -0.0450 -0.0208 484 LEU B CD2 
4067 N N   . GLN B 474 ? 0.4301 0.5901 0.4970 -0.0387 -0.0560 -0.0200 485 GLN B N   
4068 C CA  . GLN B 474 ? 0.5728 0.7720 0.6452 -0.0386 -0.0594 -0.0173 485 GLN B CA  
4069 C C   . GLN B 474 ? 0.5480 0.7569 0.6277 -0.0499 -0.0583 -0.0166 485 GLN B C   
4070 O O   . GLN B 474 ? 0.5584 0.7988 0.6423 -0.0606 -0.0608 -0.0185 485 GLN B O   
4071 C CB  . GLN B 474 ? 0.4847 0.6953 0.5581 -0.0181 -0.0594 -0.0096 485 GLN B CB  
4072 C CG  . GLN B 474 ? 0.6984 0.9010 0.7623 -0.0077 -0.0601 -0.0090 485 GLN B CG  
4073 C CD  . GLN B 474 ? 0.7870 0.9992 0.8493 0.0124  -0.0595 -0.0007 485 GLN B CD  
4074 O OE1 . GLN B 474 ? 0.7962 1.0409 0.8638 0.0185  -0.0620 0.0033  485 GLN B OE1 
4075 N NE2 . GLN B 474 ? 0.7107 0.8944 0.7653 0.0227  -0.0556 0.0019  485 GLN B NE2 
4076 N N   . ASN B 475 ? 0.4813 0.6654 0.5620 -0.0486 -0.0547 -0.0135 486 ASN B N   
4077 C CA  . ASN B 475 ? 0.5177 0.7075 0.6030 -0.0589 -0.0529 -0.0115 486 ASN B CA  
4078 C C   . ASN B 475 ? 0.5258 0.6767 0.6062 -0.0652 -0.0501 -0.0115 486 ASN B C   
4079 O O   . ASN B 475 ? 0.4499 0.5873 0.5311 -0.0580 -0.0482 -0.0061 486 ASN B O   
4080 C CB  . ASN B 475 ? 0.5651 0.7732 0.6566 -0.0460 -0.0514 -0.0049 486 ASN B CB  
4081 C CG  . ASN B 475 ? 0.6660 0.9143 0.7630 -0.0373 -0.0538 -0.0037 486 ASN B CG  
4082 O OD1 . ASN B 475 ? 0.6098 0.8584 0.7044 -0.0205 -0.0544 -0.0011 486 ASN B OD1 
4083 N ND2 . ASN B 475 ? 0.5899 0.8731 0.6941 -0.0487 -0.0550 -0.0051 486 ASN B ND2 
4084 N N   . PRO B 476 ? 0.5385 0.6706 0.6130 -0.0783 -0.0496 -0.0174 487 PRO B N   
4085 C CA  . PRO B 476 ? 0.5594 0.6525 0.6288 -0.0809 -0.0466 -0.0164 487 PRO B CA  
4086 C C   . PRO B 476 ? 0.5610 0.6493 0.6307 -0.0881 -0.0447 -0.0104 487 PRO B C   
4087 O O   . PRO B 476 ? 0.5456 0.6065 0.6124 -0.0838 -0.0432 -0.0057 487 PRO B O   
4088 C CB  . PRO B 476 ? 0.5017 0.5782 0.5631 -0.0944 -0.0454 -0.0251 487 PRO B CB  
4089 C CG  . PRO B 476 ? 0.5527 0.6642 0.6151 -0.1071 -0.0478 -0.0300 487 PRO B CG  
4090 C CD  . PRO B 476 ? 0.4838 0.6296 0.5547 -0.0919 -0.0513 -0.0254 487 PRO B CD  
4091 N N   . GLU B 477 ? 0.5993 0.7159 0.6722 -0.0987 -0.0446 -0.0099 488 GLU B N   
4092 C CA  . GLU B 477 ? 0.6042 0.7178 0.6758 -0.1073 -0.0419 -0.0041 488 GLU B CA  
4093 C C   . GLU B 477 ? 0.4653 0.5792 0.5400 -0.0922 -0.0417 0.0035  488 GLU B C   
4094 O O   . GLU B 477 ? 0.5341 0.6351 0.6046 -0.0965 -0.0396 0.0094  488 GLU B O   
4095 C CB  . GLU B 477 ? 0.6268 0.7774 0.7027 -0.1225 -0.0413 -0.0061 488 GLU B CB  
4096 C CG  . GLU B 477 ? 0.5885 0.7821 0.6758 -0.1098 -0.0430 -0.0044 488 GLU B CG  
4097 C CD  . GLU B 477 ? 0.7467 0.9597 0.8378 -0.1007 -0.0471 -0.0091 488 GLU B CD  
4098 O OE1 . GLU B 477 ? 0.6382 0.8364 0.7234 -0.1078 -0.0487 -0.0151 488 GLU B OE1 
4099 O OE2 . GLU B 477 ? 0.6751 0.9161 0.7736 -0.0856 -0.0482 -0.0064 488 GLU B OE2 
4100 N N   . LYS B 478 ? 0.4355 0.5616 0.5151 -0.0754 -0.0433 0.0035  489 LYS B N   
4101 C CA  . LYS B 478 ? 0.4170 0.5429 0.4976 -0.0622 -0.0424 0.0089  489 LYS B CA  
4102 C C   . LYS B 478 ? 0.4102 0.5040 0.4863 -0.0552 -0.0430 0.0118  489 LYS B C   
4103 O O   . LYS B 478 ? 0.3877 0.4799 0.4628 -0.0470 -0.0424 0.0157  489 LYS B O   
4104 C CB  . LYS B 478 ? 0.4606 0.6087 0.5458 -0.0477 -0.0428 0.0076  489 LYS B CB  
4105 C CG  . LYS B 478 ? 0.5656 0.7522 0.6575 -0.0514 -0.0427 0.0059  489 LYS B CG  
4106 C CD  . LYS B 478 ? 0.6209 0.8279 0.7163 -0.0334 -0.0420 0.0072  489 LYS B CD  
4107 C CE  . LYS B 478 ? 0.7080 0.9585 0.8121 -0.0350 -0.0420 0.0067  489 LYS B CE  
4108 N NZ  . LYS B 478 ? 0.8421 1.1105 0.9490 -0.0148 -0.0398 0.0095  489 LYS B NZ  
4109 N N   . LEU B 479 ? 0.3294 0.3995 0.4027 -0.0580 -0.0439 0.0095  490 LEU B N   
4110 C CA  . LEU B 479 ? 0.3763 0.4210 0.4478 -0.0499 -0.0446 0.0123  490 LEU B CA  
4111 C C   . LEU B 479 ? 0.3026 0.3255 0.3684 -0.0575 -0.0440 0.0179  490 LEU B C   
4112 O O   . LEU B 479 ? 0.3498 0.3649 0.4112 -0.0702 -0.0422 0.0165  490 LEU B O   
4113 C CB  . LEU B 479 ? 0.3284 0.3610 0.4008 -0.0447 -0.0450 0.0065  490 LEU B CB  
4114 C CG  . LEU B 479 ? 0.3700 0.4157 0.4452 -0.0344 -0.0455 0.0029  490 LEU B CG  
4115 C CD1 . LEU B 479 ? 0.4466 0.5190 0.5230 -0.0360 -0.0458 0.0006  490 LEU B CD1 
4116 C CD2 . LEU B 479 ? 0.4415 0.4723 0.5160 -0.0317 -0.0449 -0.0025 490 LEU B CD2 
4117 N N   . SER B 480 ? 0.3208 0.3333 0.3854 -0.0501 -0.0454 0.0244  491 SER B N   
4118 C CA  . SER B 480 ? 0.3463 0.3367 0.4042 -0.0543 -0.0454 0.0319  491 SER B CA  
4119 C C   . SER B 480 ? 0.3775 0.3406 0.4336 -0.0532 -0.0443 0.0296  491 SER B C   
4120 O O   . SER B 480 ? 0.3483 0.3107 0.4092 -0.0474 -0.0441 0.0226  491 SER B O   
4121 C CB  . SER B 480 ? 0.3159 0.3054 0.3731 -0.0453 -0.0483 0.0395  491 SER B CB  
4122 O OG  . SER B 480 ? 0.3203 0.3051 0.3834 -0.0333 -0.0503 0.0375  491 SER B OG  
4123 N N   . ALA B 481 ? 0.3598 0.2983 0.4071 -0.0590 -0.0428 0.0358  492 ALA B N   
4124 C CA  . ALA B 481 ? 0.4239 0.3311 0.4675 -0.0561 -0.0405 0.0342  492 ALA B CA  
4125 C C   . ALA B 481 ? 0.4099 0.3139 0.4615 -0.0380 -0.0429 0.0350  492 ALA B C   
4126 O O   . ALA B 481 ? 0.3612 0.2543 0.4155 -0.0328 -0.0406 0.0280  492 ALA B O   
4127 C CB  . ALA B 481 ? 0.4252 0.3028 0.4557 -0.0629 -0.0382 0.0432  492 ALA B CB  
4128 N N   . ILE B 482 ? 0.3632 0.2788 0.4186 -0.0291 -0.0471 0.0429  493 ILE B N   
4129 C CA  . ILE B 482 ? 0.4184 0.3337 0.4821 -0.0134 -0.0495 0.0444  493 ILE B CA  
4130 C C   . ILE B 482 ? 0.3905 0.3247 0.4639 -0.0092 -0.0492 0.0344  493 ILE B C   
4131 O O   . ILE B 482 ? 0.3426 0.2723 0.4224 0.0002  -0.0481 0.0308  493 ILE B O   
4132 C CB  . ILE B 482 ? 0.3956 0.3202 0.4594 -0.0072 -0.0548 0.0556  493 ILE B CB  
4133 C CG1 . ILE B 482 ? 0.3834 0.3083 0.4562 0.0086  -0.0575 0.0585  493 ILE B CG1 
4134 C CG2 . ILE B 482 ? 0.3578 0.3098 0.4226 -0.0121 -0.0570 0.0541  493 ILE B CG2 
4135 C CD1 . ILE B 482 ? 0.5717 0.4667 0.6426 0.0164  -0.0542 0.0607  493 ILE B CD1 
4136 N N   . PHE B 483 ? 0.3020 0.2568 0.3756 -0.0157 -0.0494 0.0302  494 PHE B N   
4137 C CA  . PHE B 483 ? 0.3012 0.2706 0.3806 -0.0123 -0.0485 0.0218  494 PHE B CA  
4138 C C   . PHE B 483 ? 0.2998 0.2589 0.3780 -0.0152 -0.0449 0.0133  494 PHE B C   
4139 O O   . PHE B 483 ? 0.2898 0.2490 0.3725 -0.0087 -0.0434 0.0077  494 PHE B O   
4140 C CB  . PHE B 483 ? 0.2484 0.2389 0.3262 -0.0169 -0.0490 0.0206  494 PHE B CB  
4141 C CG  . PHE B 483 ? 0.2475 0.2507 0.3285 -0.0120 -0.0480 0.0144  494 PHE B CG  
4142 C CD1 . PHE B 483 ? 0.2497 0.2490 0.3351 -0.0050 -0.0472 0.0110  494 PHE B CD1 
4143 C CD2 . PHE B 483 ? 0.2369 0.2559 0.3155 -0.0140 -0.0471 0.0125  494 PHE B CD2 
4144 C CE1 . PHE B 483 ? 0.3022 0.3106 0.3879 -0.0018 -0.0456 0.0062  494 PHE B CE1 
4145 C CE2 . PHE B 483 ? 0.3045 0.3311 0.3832 -0.0086 -0.0457 0.0082  494 PHE B CE2 
4146 C CZ  . PHE B 483 ? 0.2636 0.2835 0.3449 -0.0034 -0.0449 0.0053  494 PHE B CZ  
4147 N N   . ARG B 484 ? 0.3431 0.2944 0.4145 -0.0266 -0.0431 0.0115  495 ARG B N   
4148 C CA  . ARG B 484 ? 0.3313 0.2723 0.3992 -0.0318 -0.0397 0.0024  495 ARG B CA  
4149 C C   . ARG B 484 ? 0.3655 0.2812 0.4335 -0.0235 -0.0366 0.0007  495 ARG B C   
4150 O O   . ARG B 484 ? 0.3661 0.2786 0.4343 -0.0215 -0.0336 -0.0079 495 ARG B O   
4151 C CB  . ARG B 484 ? 0.3830 0.3201 0.4425 -0.0483 -0.0382 0.0007  495 ARG B CB  
4152 C CG  . ARG B 484 ? 0.5021 0.4707 0.5637 -0.0553 -0.0401 -0.0023 495 ARG B CG  
4153 C CD  . ARG B 484 ? 0.5216 0.4950 0.5771 -0.0734 -0.0387 -0.0060 495 ARG B CD  
4154 N NE  . ARG B 484 ? 0.5581 0.5266 0.6098 -0.0816 -0.0381 0.0016  495 ARG B NE  
4155 C CZ  . ARG B 484 ? 0.6987 0.6361 0.7414 -0.0880 -0.0351 0.0051  495 ARG B CZ  
4156 N NH1 . ARG B 484 ? 0.7804 0.6868 0.8173 -0.0860 -0.0320 0.0011  495 ARG B NH1 
4157 N NH2 . ARG B 484 ? 0.7132 0.6493 0.7512 -0.0962 -0.0344 0.0129  495 ARG B NH2 
4158 N N   . ASP B 485 ? 0.3768 0.2755 0.4442 -0.0175 -0.0370 0.0093  496 ASP B N   
4159 C CA  . ASP B 485 ? 0.3934 0.2695 0.4623 -0.0062 -0.0336 0.0086  496 ASP B CA  
4160 C C   . ASP B 485 ? 0.3878 0.2813 0.4689 0.0067  -0.0343 0.0059  496 ASP B C   
4161 O O   . ASP B 485 ? 0.3731 0.2578 0.4562 0.0127  -0.0297 -0.0013 496 ASP B O   
4162 C CB  . ASP B 485 ? 0.3537 0.2103 0.4194 -0.0001 -0.0346 0.0206  496 ASP B CB  
4163 C CG  . ASP B 485 ? 0.5212 0.3528 0.5880 0.0139  -0.0303 0.0207  496 ASP B CG  
4164 O OD1 . ASP B 485 ? 0.5884 0.3889 0.6443 0.0092  -0.0241 0.0158  496 ASP B OD1 
4165 O OD2 . ASP B 485 ? 0.5069 0.3507 0.5855 0.0294  -0.0327 0.0249  496 ASP B OD2 
4166 N N   . PHE B 486 ? 0.3130 0.2307 0.4012 0.0101  -0.0393 0.0111  497 PHE B N   
4167 C CA  . PHE B 486 ? 0.3815 0.3176 0.4799 0.0187  -0.0396 0.0081  497 PHE B CA  
4168 C C   . PHE B 486 ? 0.3460 0.2871 0.4428 0.0149  -0.0357 -0.0029 497 PHE B C   
4169 O O   . PHE B 486 ? 0.3131 0.2542 0.4149 0.0216  -0.0320 -0.0084 497 PHE B O   
4170 C CB  . PHE B 486 ? 0.3292 0.2877 0.4309 0.0181  -0.0447 0.0138  497 PHE B CB  
4171 C CG  . PHE B 486 ? 0.3088 0.2859 0.4189 0.0233  -0.0446 0.0103  497 PHE B CG  
4172 C CD1 . PHE B 486 ? 0.2909 0.2755 0.4111 0.0329  -0.0459 0.0137  497 PHE B CD1 
4173 C CD2 . PHE B 486 ? 0.2797 0.2674 0.3868 0.0182  -0.0429 0.0043  497 PHE B CD2 
4174 C CE1 . PHE B 486 ? 0.2816 0.2853 0.4094 0.0348  -0.0450 0.0099  497 PHE B CE1 
4175 C CE2 . PHE B 486 ? 0.2796 0.2810 0.3919 0.0209  -0.0416 0.0013  497 PHE B CE2 
4176 C CZ  . PHE B 486 ? 0.2893 0.2990 0.4119 0.0278  -0.0425 0.0035  497 PHE B CZ  
4177 N N   . LEU B 487 ? 0.3056 0.2528 0.3953 0.0043  -0.0364 -0.0059 498 LEU B N   
4178 C CA  . LEU B 487 ? 0.2935 0.2465 0.3794 0.0004  -0.0337 -0.0150 498 LEU B CA  
4179 C C   . LEU B 487 ? 0.3527 0.2861 0.4344 -0.0002 -0.0283 -0.0230 498 LEU B C   
4180 O O   . LEU B 487 ? 0.3759 0.3117 0.4577 0.0027  -0.0247 -0.0302 498 LEU B O   
4181 C CB  . LEU B 487 ? 0.3181 0.2828 0.3976 -0.0099 -0.0360 -0.0155 498 LEU B CB  
4182 C CG  . LEU B 487 ? 0.3221 0.3063 0.4039 -0.0081 -0.0394 -0.0100 498 LEU B CG  
4183 C CD1 . LEU B 487 ? 0.3080 0.3059 0.3849 -0.0161 -0.0410 -0.0108 498 LEU B CD1 
4184 C CD2 . LEU B 487 ? 0.2991 0.2921 0.3836 -0.0009 -0.0382 -0.0118 498 LEU B CD2 
4185 N N   . ASN B 488 ? 0.3283 0.2401 0.4039 -0.0051 -0.0269 -0.0223 499 ASN B N   
4186 C CA  . ASN B 488 ? 0.3298 0.2172 0.3986 -0.0061 -0.0204 -0.0308 499 ASN B CA  
4187 C C   . ASN B 488 ? 0.4566 0.3376 0.5335 0.0094  -0.0162 -0.0321 499 ASN B C   
4188 O O   . ASN B 488 ? 0.4166 0.2892 0.4901 0.0107  -0.0101 -0.0419 499 ASN B O   
4189 C CB  . ASN B 488 ? 0.4514 0.3111 0.5106 -0.0136 -0.0186 -0.0285 499 ASN B CB  
4190 C CG  . ASN B 488 ? 0.5187 0.3856 0.5689 -0.0322 -0.0207 -0.0310 499 ASN B CG  
4191 O OD1 . ASN B 488 ? 0.5782 0.4657 0.6270 -0.0391 -0.0221 -0.0376 499 ASN B OD1 
4192 N ND2 . ASN B 488 ? 0.6073 0.4599 0.6515 -0.0402 -0.0211 -0.0251 499 ASN B ND2 
4193 N N   . ARG B 489 ? 0.3471 0.2344 0.4349 0.0210  -0.0192 -0.0225 500 ARG B N   
4194 C CA  . ARG B 489 ? 0.4301 0.3178 0.5285 0.0364  -0.0156 -0.0230 500 ARG B CA  
4195 C C   . ARG B 489 ? 0.4199 0.3320 0.5250 0.0380  -0.0141 -0.0292 500 ARG B C   
4196 O O   . ARG B 489 ? 0.3731 0.2838 0.4829 0.0463  -0.0079 -0.0353 500 ARG B O   
4197 C CB  . ARG B 489 ? 0.3860 0.2795 0.4943 0.0474  -0.0205 -0.0104 500 ARG B CB  
4198 C CG  . ARG B 489 ? 0.4668 0.3331 0.5672 0.0480  -0.0211 -0.0026 500 ARG B CG  
4199 C CD  . ARG B 489 ? 0.5159 0.3513 0.6130 0.0585  -0.0132 -0.0061 500 ARG B CD  
4200 N NE  . ARG B 489 ? 0.7166 0.5654 0.8295 0.0776  -0.0117 -0.0041 500 ARG B NE  
4201 C CZ  . ARG B 489 ? 0.7199 0.5702 0.8380 0.0850  -0.0044 -0.0142 500 ARG B CZ  
4202 N NH1 . ARG B 489 ? 0.5900 0.4267 0.6970 0.0751  0.0022  -0.0272 500 ARG B NH1 
4203 N NH2 . ARG B 489 ? 0.6778 0.5465 0.8126 0.1023  -0.0035 -0.0112 500 ARG B NH2 
4204 N N   . CYS B 490 ? 0.3360 0.2689 0.4403 0.0304  -0.0187 -0.0276 501 CYS B N   
4205 C CA  . CYS B 490 ? 0.2663 0.2178 0.3730 0.0301  -0.0166 -0.0328 501 CYS B CA  
4206 C C   . CYS B 490 ? 0.3258 0.2708 0.4212 0.0234  -0.0118 -0.0431 501 CYS B C   
4207 O O   . CYS B 490 ? 0.3259 0.2786 0.4221 0.0256  -0.0070 -0.0491 501 CYS B O   
4208 C CB  . CYS B 490 ? 0.2555 0.2255 0.3615 0.0248  -0.0220 -0.0275 501 CYS B CB  
4209 S SG  . CYS B 490 ? 0.3001 0.2831 0.4171 0.0300  -0.0276 -0.0172 501 CYS B SG  
4210 N N   . LEU B 491 ? 0.3694 0.3029 0.4537 0.0138  -0.0130 -0.0456 502 LEU B N   
4211 C CA  . LEU B 491 ? 0.4008 0.3346 0.4728 0.0048  -0.0105 -0.0547 502 LEU B CA  
4212 C C   . LEU B 491 ? 0.3719 0.2814 0.4354 0.0020  -0.0041 -0.0644 502 LEU B C   
4213 O O   . LEU B 491 ? 0.4141 0.3199 0.4649 -0.0099 -0.0038 -0.0713 502 LEU B O   
4214 C CB  . LEU B 491 ? 0.3692 0.3149 0.4346 -0.0055 -0.0168 -0.0516 502 LEU B CB  
4215 C CG  . LEU B 491 ? 0.3123 0.2788 0.3827 -0.0020 -0.0212 -0.0439 502 LEU B CG  
4216 C CD1 . LEU B 491 ? 0.3527 0.3305 0.4192 -0.0089 -0.0269 -0.0395 502 LEU B CD1 
4217 C CD2 . LEU B 491 ? 0.2851 0.2623 0.3521 0.0005  -0.0184 -0.0473 502 LEU B CD2 
4218 N N   . GLU B 492 ? 0.4199 0.3130 0.4897 0.0128  0.0012  -0.0649 503 GLU B N   
4219 C CA  . GLU B 492 ? 0.5303 0.3960 0.5907 0.0124  0.0095  -0.0751 503 GLU B CA  
4220 C C   . GLU B 492 ? 0.4198 0.2928 0.4739 0.0107  0.0156  -0.0866 503 GLU B C   
4221 O O   . GLU B 492 ? 0.4479 0.3395 0.5111 0.0186  0.0172  -0.0857 503 GLU B O   
4222 C CB  . GLU B 492 ? 0.5208 0.3686 0.5907 0.0287  0.0142  -0.0716 503 GLU B CB  
4223 C CG  . GLU B 492 ? 0.6556 0.4860 0.7259 0.0300  0.0102  -0.0612 503 GLU B CG  
4224 C CD  . GLU B 492 ? 0.7868 0.5807 0.8394 0.0198  0.0150  -0.0671 503 GLU B CD  
4225 O OE1 . GLU B 492 ? 0.6297 0.4119 0.6698 0.0117  0.0215  -0.0805 503 GLU B OE1 
4226 O OE2 . GLU B 492 ? 0.8062 0.5822 0.8557 0.0186  0.0126  -0.0585 503 GLU B OE2 
4227 N N   . MET B 493 ? 0.4766 0.3354 0.5137 -0.0014 0.0193  -0.0978 504 MET B N   
4228 C CA  . MET B 493 ? 0.5277 0.3917 0.5557 -0.0040 0.0257  -0.1094 504 MET B CA  
4229 C C   . MET B 493 ? 0.5652 0.4146 0.5984 0.0103  0.0367  -0.1158 504 MET B C   
4230 O O   . MET B 493 ? 0.5782 0.4421 0.6132 0.0147  0.0418  -0.1206 504 MET B O   
4231 C CB  . MET B 493 ? 0.5821 0.4360 0.5893 -0.0219 0.0264  -0.1204 504 MET B CB  
4232 C CG  . MET B 493 ? 0.6337 0.4964 0.6281 -0.0269 0.0316  -0.1320 504 MET B CG  
4233 S SD  . MET B 493 ? 1.0232 0.9194 1.0077 -0.0411 0.0211  -0.1291 504 MET B SD  
4234 C CE  . MET B 493 ? 0.5870 0.4770 0.5671 -0.0561 0.0138  -0.1271 504 MET B CE  
4235 N N   . ASP B 494 ? 0.5616 0.3826 0.5969 0.0182  0.0410  -0.1152 505 ASP B N   
4236 C CA  . ASP B 494 ? 0.5684 0.3749 0.6105 0.0354  0.0518  -0.1199 505 ASP B CA  
4237 C C   . ASP B 494 ? 0.5910 0.4259 0.6569 0.0514  0.0489  -0.1092 505 ASP B C   
4238 O O   . ASP B 494 ? 0.5171 0.3560 0.5947 0.0576  0.0416  -0.0963 505 ASP B O   
4239 C CB  . ASP B 494 ? 0.6085 0.3740 0.6444 0.0402  0.0566  -0.1201 505 ASP B CB  
4240 C CG  . ASP B 494 ? 0.6750 0.4212 0.7158 0.0602  0.0692  -0.1257 505 ASP B CG  
4241 O OD1 . ASP B 494 ? 0.6612 0.4332 0.7204 0.0755  0.0710  -0.1228 505 ASP B OD1 
4242 O OD2 . ASP B 494 ? 0.7654 0.4759 0.7891 0.0600  0.0749  -0.1304 505 ASP B OD2 
4243 N N   . VAL B 495 ? 0.4792 0.3347 0.5510 0.0565  0.0547  -0.1148 506 VAL B N   
4244 C CA  . VAL B 495 ? 0.4944 0.3816 0.5879 0.0675  0.0521  -0.1060 506 VAL B CA  
4245 C C   . VAL B 495 ? 0.5762 0.4576 0.6867 0.0867  0.0532  -0.0985 506 VAL B C   
4246 O O   . VAL B 495 ? 0.5152 0.4175 0.6417 0.0924  0.0453  -0.0864 506 VAL B O   
4247 C CB  . VAL B 495 ? 0.5349 0.4428 0.6301 0.0683  0.0606  -0.1147 506 VAL B CB  
4248 C CG1 . VAL B 495 ? 0.4828 0.4244 0.6010 0.0780  0.0591  -0.1067 506 VAL B CG1 
4249 C CG2 . VAL B 495 ? 0.5534 0.4690 0.6308 0.0504  0.0579  -0.1189 506 VAL B CG2 
4250 N N   . GLU B 496 ? 0.5070 0.3587 0.6128 0.0973  0.0629  -0.1054 507 GLU B N   
4251 C CA  . GLU B 496 ? 0.5375 0.3812 0.6581 0.1185  0.0642  -0.0971 507 GLU B CA  
4252 C C   . GLU B 496 ? 0.5658 0.3973 0.6854 0.1164  0.0533  -0.0831 507 GLU B C   
4253 O O   . GLU B 496 ? 0.5967 0.4403 0.7326 0.1309  0.0483  -0.0707 507 GLU B O   
4254 C CB  . GLU B 496 ? 0.6908 0.5015 0.7978 0.1289  0.0760  -0.1057 507 GLU B CB  
4255 C CG  . GLU B 496 ? 0.7523 0.5655 0.8708 0.1534  0.0763  -0.0960 507 GLU B CG  
4256 C CD  . GLU B 496 ? 1.0251 0.8833 1.1669 0.1659  0.0793  -0.0956 507 GLU B CD  
4257 O OE1 . GLU B 496 ? 0.9448 0.8260 1.0904 0.1549  0.0829  -0.1044 507 GLU B OE1 
4258 O OE2 . GLU B 496 ? 1.1642 1.0364 1.3197 0.1861  0.0775  -0.0869 507 GLU B OE2 
4259 N N   . LYS B 497 ? 0.5244 0.3348 0.6248 0.0979  0.0493  -0.0848 508 LYS B N   
4260 C CA  . LYS B 497 ? 0.5348 0.3326 0.6320 0.0937  0.0402  -0.0724 508 LYS B CA  
4261 C C   . LYS B 497 ? 0.5263 0.3601 0.6340 0.0868  0.0279  -0.0617 508 LYS B C   
4262 O O   . LYS B 497 ? 0.5034 0.3372 0.6156 0.0897  0.0202  -0.0489 508 LYS B O   
4263 C CB  . LYS B 497 ? 0.7012 0.4659 0.7744 0.0750  0.0418  -0.0795 508 LYS B CB  
4264 C CG  . LYS B 497 ? 0.8654 0.6049 0.9311 0.0714  0.0369  -0.0689 508 LYS B CG  
4265 C CD  . LYS B 497 ? 0.9131 0.6097 0.9542 0.0569  0.0442  -0.0794 508 LYS B CD  
4266 C CE  . LYS B 497 ? 1.0565 0.7254 1.0874 0.0501  0.0406  -0.0692 508 LYS B CE  
4267 N NZ  . LYS B 497 ? 0.9655 0.6600 0.9960 0.0310  0.0297  -0.0639 508 LYS B NZ  
4268 N N   . ARG B 498 ? 0.4833 0.3454 0.5931 0.0779  0.0264  -0.0666 509 ARG B N   
4269 C CA  . ARG B 498 ? 0.4060 0.2980 0.5230 0.0711  0.0163  -0.0579 509 ARG B CA  
4270 C C   . ARG B 498 ? 0.3677 0.2809 0.5045 0.0854  0.0124  -0.0473 509 ARG B C   
4271 O O   . ARG B 498 ? 0.4028 0.3233 0.5520 0.1002  0.0182  -0.0492 509 ARG B O   
4272 C CB  . ARG B 498 ? 0.3513 0.2652 0.4654 0.0614  0.0176  -0.0651 509 ARG B CB  
4273 C CG  . ARG B 498 ? 0.3298 0.2659 0.4444 0.0516  0.0087  -0.0580 509 ARG B CG  
4274 C CD  . ARG B 498 ? 0.4029 0.3550 0.5118 0.0442  0.0116  -0.0645 509 ARG B CD  
4275 N NE  . ARG B 498 ? 0.3824 0.3197 0.4746 0.0361  0.0162  -0.0748 509 ARG B NE  
4276 C CZ  . ARG B 498 ? 0.3760 0.3204 0.4611 0.0325  0.0220  -0.0830 509 ARG B CZ  
4277 N NH1 . ARG B 498 ? 0.3067 0.2716 0.3993 0.0355  0.0247  -0.0821 509 ARG B NH1 
4278 N NH2 . ARG B 498 ? 0.3749 0.3056 0.4435 0.0245  0.0256  -0.0926 509 ARG B NH2 
4279 N N   . GLY B 499 ? 0.3494 0.2748 0.4892 0.0810  0.0026  -0.0366 510 GLY B N   
4280 C CA  . GLY B 499 ? 0.3596 0.3073 0.5164 0.0924  -0.0025 -0.0264 510 GLY B CA  
4281 C C   . GLY B 499 ? 0.3390 0.3215 0.5094 0.0936  -0.0010 -0.0297 510 GLY B C   
4282 O O   . GLY B 499 ? 0.3056 0.2974 0.4702 0.0819  0.0007  -0.0361 510 GLY B O   
4283 N N   . SER B 500 ? 0.3205 0.3231 0.5089 0.1080  -0.0014 -0.0247 511 SER B N   
4284 C CA  . SER B 500 ? 0.2902 0.3312 0.4929 0.1065  -0.0018 -0.0257 511 SER B CA  
4285 C C   . SER B 500 ? 0.3473 0.4060 0.5503 0.0965  -0.0121 -0.0173 511 SER B C   
4286 O O   . SER B 500 ? 0.2664 0.3111 0.4618 0.0947  -0.0191 -0.0094 511 SER B O   
4287 C CB  . SER B 500 ? 0.3414 0.4037 0.5651 0.1253  0.0015  -0.0239 511 SER B CB  
4288 O OG  . SER B 500 ? 0.3402 0.4072 0.5715 0.1359  -0.0070 -0.0110 511 SER B OG  
4289 N N   . ALA B 501 ? 0.2823 0.3710 0.4924 0.0887  -0.0123 -0.0196 512 ALA B N   
4290 C CA  . ALA B 501 ? 0.2844 0.3895 0.4939 0.0790  -0.0210 -0.0130 512 ALA B CA  
4291 C C   . ALA B 501 ? 0.2153 0.3347 0.4369 0.0903  -0.0288 -0.0022 512 ALA B C   
4292 O O   . ALA B 501 ? 0.2787 0.3936 0.4931 0.0858  -0.0368 0.0055  512 ALA B O   
4293 C CB  . ALA B 501 ? 0.3044 0.4370 0.5184 0.0678  -0.0183 -0.0182 512 ALA B CB  
4294 N N   . LYS B 502 ? 0.2352 0.3734 0.4749 0.1058  -0.0265 -0.0011 513 LYS B N   
4295 C CA  . LYS B 502 ? 0.2720 0.4264 0.5237 0.1194  -0.0345 0.0107  513 LYS B CA  
4296 C C   . LYS B 502 ? 0.3139 0.4317 0.5526 0.1264  -0.0381 0.0192  513 LYS B C   
4297 O O   . LYS B 502 ? 0.3251 0.4477 0.5619 0.1272  -0.0474 0.0302  513 LYS B O   
4298 C CB  . LYS B 502 ? 0.3063 0.4857 0.5803 0.1384  -0.0298 0.0100  513 LYS B CB  
4299 C CG  . LYS B 502 ? 0.4436 0.6436 0.7246 0.1535  -0.0379 0.0216  513 LYS B CG  
4300 C CD  . LYS B 502 ? 0.5178 0.7363 0.8223 0.1664  -0.0333 0.0180  513 LYS B CD  
4301 C CE  . LYS B 502 ? 0.5198 0.7500 0.8307 0.1781  -0.0427 0.0283  513 LYS B CE  
4302 N NZ  . LYS B 502 ? 0.7957 1.0424 1.1261 0.1936  -0.0367 0.0267  513 LYS B NZ  
4303 N N   . GLU B 503 ? 0.3258 0.4066 0.5539 0.1298  -0.0305 0.0139  514 GLU B N   
4304 C CA  . GLU B 503 ? 0.3037 0.3469 0.5176 0.1336  -0.0325 0.0211  514 GLU B CA  
4305 C C   . GLU B 503 ? 0.3207 0.3542 0.5184 0.1152  -0.0386 0.0237  514 GLU B C   
4306 O O   . GLU B 503 ? 0.3214 0.3457 0.5125 0.1162  -0.0452 0.0345  514 GLU B O   
4307 C CB  . GLU B 503 ? 0.3625 0.3686 0.5671 0.1380  -0.0219 0.0125  514 GLU B CB  
4308 C CG  . GLU B 503 ? 0.4491 0.4538 0.6666 0.1611  -0.0149 0.0122  514 GLU B CG  
4309 C CD  . GLU B 503 ? 0.4223 0.3937 0.6297 0.1625  -0.0025 -0.0005 514 GLU B CD  
4310 O OE1 . GLU B 503 ? 0.4638 0.4193 0.6559 0.1447  0.0000  -0.0094 514 GLU B OE1 
4311 O OE2 . GLU B 503 ? 0.5670 0.5290 0.7738 0.1795  0.0047  -0.0017 514 GLU B OE2 
4312 N N   . LEU B 504 ? 0.2571 0.2932 0.4478 0.0991  -0.0362 0.0144  515 LEU B N   
4313 C CA  . LEU B 504 ? 0.2506 0.2774 0.4262 0.0837  -0.0407 0.0161  515 LEU B CA  
4314 C C   . LEU B 504 ? 0.2969 0.3479 0.4752 0.0791  -0.0494 0.0240  515 LEU B C   
4315 O O   . LEU B 504 ? 0.2760 0.3179 0.4425 0.0707  -0.0538 0.0287  515 LEU B O   
4316 C CB  . LEU B 504 ? 0.2629 0.2871 0.4304 0.0706  -0.0358 0.0053  515 LEU B CB  
4317 C CG  . LEU B 504 ? 0.3716 0.3676 0.5302 0.0710  -0.0287 -0.0020 515 LEU B CG  
4318 C CD1 . LEU B 504 ? 0.3562 0.3547 0.5082 0.0609  -0.0240 -0.0122 515 LEU B CD1 
4319 C CD2 . LEU B 504 ? 0.3925 0.3633 0.5378 0.0658  -0.0314 0.0027  515 LEU B CD2 
4320 N N   . LEU B 505 ? 0.2777 0.3609 0.4707 0.0835  -0.0518 0.0251  516 LEU B N   
4321 C CA  . LEU B 505 ? 0.2989 0.4060 0.4931 0.0781  -0.0604 0.0320  516 LEU B CA  
4322 C C   . LEU B 505 ? 0.2677 0.3674 0.4589 0.0868  -0.0675 0.0453  516 LEU B C   
4323 O O   . LEU B 505 ? 0.2724 0.3847 0.4583 0.0799  -0.0748 0.0514  516 LEU B O   
4324 C CB  . LEU B 505 ? 0.2733 0.4202 0.4850 0.0798  -0.0615 0.0299  516 LEU B CB  
4325 C CG  . LEU B 505 ? 0.2753 0.4340 0.4856 0.0650  -0.0563 0.0187  516 LEU B CG  
4326 C CD1 . LEU B 505 ? 0.2815 0.4779 0.5111 0.0680  -0.0550 0.0158  516 LEU B CD1 
4327 C CD2 . LEU B 505 ? 0.2668 0.4259 0.4629 0.0482  -0.0602 0.0185  516 LEU B CD2 
4328 N N   . GLN B 506 ? 0.2876 0.3640 0.4792 0.1010  -0.0649 0.0498  517 GLN B N   
4329 C CA  . GLN B 506 ? 0.3157 0.3766 0.5002 0.1092  -0.0703 0.0634  517 GLN B CA  
4330 C C   . GLN B 506 ? 0.3145 0.3389 0.4789 0.0988  -0.0684 0.0642  517 GLN B C   
4331 O O   . GLN B 506 ? 0.3365 0.3447 0.4916 0.1026  -0.0720 0.0758  517 GLN B O   
4332 C CB  . GLN B 506 ? 0.3449 0.3962 0.5386 0.1316  -0.0674 0.0689  517 GLN B CB  
4333 C CG  . GLN B 506 ? 0.4441 0.5336 0.6533 0.1425  -0.0680 0.0668  517 GLN B CG  
4334 C CD  . GLN B 506 ? 0.5526 0.6789 0.7636 0.1372  -0.0784 0.0724  517 GLN B CD  
4335 O OE1 . GLN B 506 ? 0.5770 0.6964 0.7757 0.1366  -0.0852 0.0826  517 GLN B OE1 
4336 N NE2 . GLN B 506 ? 0.5768 0.7417 0.8023 0.1319  -0.0794 0.0650  517 GLN B NE2 
4337 N N   . HIS B 507 ? 0.3058 0.3191 0.4629 0.0855  -0.0629 0.0531  518 HIS B N   
4338 C CA  . HIS B 507 ? 0.3281 0.3106 0.4684 0.0758  -0.0604 0.0528  518 HIS B CA  
4339 C C   . HIS B 507 ? 0.3035 0.2912 0.4333 0.0657  -0.0668 0.0607  518 HIS B C   
4340 O O   . HIS B 507 ? 0.2915 0.3050 0.4237 0.0598  -0.0711 0.0601  518 HIS B O   
4341 C CB  . HIS B 507 ? 0.3030 0.2799 0.4396 0.0649  -0.0541 0.0394  518 HIS B CB  
4342 C CG  . HIS B 507 ? 0.3669 0.3145 0.4892 0.0562  -0.0504 0.0373  518 HIS B CG  
4343 N ND1 . HIS B 507 ? 0.3283 0.2740 0.4396 0.0436  -0.0530 0.0402  518 HIS B ND1 
4344 C CD2 . HIS B 507 ? 0.3167 0.2373 0.4335 0.0570  -0.0439 0.0318  518 HIS B CD2 
4345 C CE1 . HIS B 507 ? 0.3975 0.3193 0.4986 0.0363  -0.0487 0.0369  518 HIS B CE1 
4346 N NE2 . HIS B 507 ? 0.4002 0.3050 0.5034 0.0435  -0.0432 0.0315  518 HIS B NE2 
4347 N N   . GLN B 508 ? 0.2998 0.2613 0.4163 0.0628  -0.0664 0.0675  519 GLN B N   
4348 C CA  . GLN B 508 ? 0.3254 0.2912 0.4308 0.0535  -0.0716 0.0757  519 GLN B CA  
4349 C C   . GLN B 508 ? 0.3117 0.2921 0.4133 0.0387  -0.0708 0.0673  519 GLN B C   
4350 O O   . GLN B 508 ? 0.2987 0.2941 0.3950 0.0326  -0.0752 0.0713  519 GLN B O   
4351 C CB  . GLN B 508 ? 0.3365 0.2691 0.4269 0.0506  -0.0693 0.0833  519 GLN B CB  
4352 C CG  . GLN B 508 ? 0.3974 0.3109 0.4881 0.0673  -0.0699 0.0942  519 GLN B CG  
4353 C CD  . GLN B 508 ? 0.4990 0.4337 0.5923 0.0765  -0.0789 0.1078  519 GLN B CD  
4354 O OE1 . GLN B 508 ? 0.4737 0.4308 0.5820 0.0898  -0.0823 0.1089  519 GLN B OE1 
4355 N NE2 . GLN B 508 ? 0.3952 0.3234 0.4736 0.0698  -0.0825 0.1188  519 GLN B NE2 
4356 N N   . PHE B 509 ? 0.2828 0.2581 0.3854 0.0333  -0.0651 0.0559  520 PHE B N   
4357 C CA  . PHE B 509 ? 0.2935 0.2809 0.3918 0.0219  -0.0640 0.0490  520 PHE B CA  
4358 C C   . PHE B 509 ? 0.2661 0.2786 0.3687 0.0216  -0.0673 0.0478  520 PHE B C   
4359 O O   . PHE B 509 ? 0.2801 0.3014 0.3756 0.0136  -0.0679 0.0470  520 PHE B O   
4360 C CB  . PHE B 509 ? 0.2769 0.2584 0.3765 0.0187  -0.0582 0.0379  520 PHE B CB  
4361 C CG  . PHE B 509 ? 0.2811 0.2762 0.3774 0.0110  -0.0569 0.0317  520 PHE B CG  
4362 C CD1 . PHE B 509 ? 0.2712 0.2685 0.3590 0.0028  -0.0571 0.0337  520 PHE B CD1 
4363 C CD2 . PHE B 509 ? 0.2706 0.2754 0.3717 0.0128  -0.0546 0.0241  520 PHE B CD2 
4364 C CE1 . PHE B 509 ? 0.2343 0.2434 0.3192 -0.0013 -0.0551 0.0283  520 PHE B CE1 
4365 C CE2 . PHE B 509 ? 0.2377 0.2507 0.3339 0.0077  -0.0527 0.0195  520 PHE B CE2 
4366 C CZ  . PHE B 509 ? 0.2773 0.2923 0.3657 0.0019  -0.0530 0.0216  520 PHE B CZ  
4367 N N   . LEU B 510 ? 0.2866 0.3111 0.4005 0.0297  -0.0687 0.0470  521 LEU B N   
4368 C CA  . LEU B 510 ? 0.2866 0.3352 0.4037 0.0265  -0.0714 0.0448  521 LEU B CA  
4369 C C   . LEU B 510 ? 0.3333 0.3933 0.4443 0.0237  -0.0780 0.0535  521 LEU B C   
4370 O O   . LEU B 510 ? 0.2864 0.3622 0.3937 0.0162  -0.0795 0.0503  521 LEU B O   
4371 C CB  . LEU B 510 ? 0.3365 0.3997 0.4686 0.0346  -0.0712 0.0421  521 LEU B CB  
4372 C CG  . LEU B 510 ? 0.2569 0.3111 0.3943 0.0371  -0.0641 0.0329  521 LEU B CG  
4373 C CD1 . LEU B 510 ? 0.2662 0.3406 0.4187 0.0438  -0.0633 0.0300  521 LEU B CD1 
4374 C CD2 . LEU B 510 ? 0.2454 0.2951 0.3735 0.0267  -0.0597 0.0247  521 LEU B CD2 
4375 N N   . LYS B 511 ? 0.3022 0.3520 0.4093 0.0286  -0.0815 0.0642  522 LYS B N   
4376 C CA  . LYS B 511 ? 0.3289 0.3904 0.4286 0.0264  -0.0883 0.0737  522 LYS B CA  
4377 C C   . LYS B 511 ? 0.3268 0.3848 0.4111 0.0137  -0.0867 0.0724  522 LYS B C   
4378 O O   . LYS B 511 ? 0.3813 0.4507 0.4570 0.0096  -0.0916 0.0784  522 LYS B O   
4379 C CB  . LYS B 511 ? 0.3991 0.4491 0.4982 0.0374  -0.0922 0.0872  522 LYS B CB  
4380 C CG  . LYS B 511 ? 0.3347 0.3915 0.4502 0.0528  -0.0935 0.0889  522 LYS B CG  
4381 C CD  . LYS B 511 ? 0.3261 0.3699 0.4402 0.0668  -0.0971 0.1035  522 LYS B CD  
4382 C CE  . LYS B 511 ? 0.4168 0.4672 0.5485 0.0845  -0.0965 0.1038  522 LYS B CE  
4383 N NZ  . LYS B 511 ? 0.7258 0.7626 0.8534 0.1006  -0.0991 0.1180  522 LYS B NZ  
4384 N N   . ILE B 512 ? 0.2547 0.3000 0.3352 0.0079  -0.0801 0.0647  523 ILE B N   
4385 C CA  . ILE B 512 ? 0.3224 0.3694 0.3906 -0.0024 -0.0776 0.0622  523 ILE B CA  
4386 C C   . ILE B 512 ? 0.3469 0.4061 0.4146 -0.0069 -0.0750 0.0520  523 ILE B C   
4387 O O   . ILE B 512 ? 0.3129 0.3724 0.3708 -0.0135 -0.0712 0.0479  523 ILE B O   
4388 C CB  . ILE B 512 ? 0.2885 0.3199 0.3527 -0.0064 -0.0719 0.0600  523 ILE B CB  
4389 C CG1 . ILE B 512 ? 0.3031 0.3319 0.3746 -0.0050 -0.0669 0.0495  523 ILE B CG1 
4390 C CG2 . ILE B 512 ? 0.3540 0.3676 0.4161 -0.0044 -0.0728 0.0689  523 ILE B CG2 
4391 C CD1 . ILE B 512 ? 0.3353 0.3573 0.4029 -0.0104 -0.0621 0.0462  523 ILE B CD1 
4392 N N   . ALA B 513 ? 0.2912 0.3596 0.3684 -0.0035 -0.0760 0.0479  524 ALA B N   
4393 C CA  . ALA B 513 ? 0.2550 0.3302 0.3295 -0.0092 -0.0724 0.0382  524 ALA B CA  
4394 C C   . ALA B 513 ? 0.2835 0.3673 0.3446 -0.0179 -0.0736 0.0376  524 ALA B C   
4395 O O   . ALA B 513 ? 0.2999 0.3959 0.3587 -0.0193 -0.0801 0.0443  524 ALA B O   
4396 C CB  . ALA B 513 ? 0.2437 0.3311 0.3300 -0.0065 -0.0738 0.0349  524 ALA B CB  
4397 N N   . LYS B 514 ? 0.2525 0.3294 0.3035 -0.0230 -0.0670 0.0299  525 LYS B N   
4398 C CA  . LYS B 514 ? 0.2813 0.3634 0.3177 -0.0319 -0.0658 0.0261  525 LYS B CA  
4399 C C   . LYS B 514 ? 0.2959 0.3878 0.3329 -0.0379 -0.0666 0.0199  525 LYS B C   
4400 O O   . LYS B 514 ? 0.3000 0.3922 0.3478 -0.0350 -0.0656 0.0170  525 LYS B O   
4401 C CB  . LYS B 514 ? 0.2831 0.3518 0.3084 -0.0329 -0.0570 0.0196  525 LYS B CB  
4402 C CG  . LYS B 514 ? 0.3963 0.4619 0.4187 -0.0306 -0.0556 0.0246  525 LYS B CG  
4403 C CD  . LYS B 514 ? 0.3664 0.4241 0.3791 -0.0299 -0.0465 0.0178  525 LYS B CD  
4404 C CE  . LYS B 514 ? 0.3834 0.4441 0.3935 -0.0295 -0.0445 0.0219  525 LYS B CE  
4405 N NZ  . LYS B 514 ? 0.5052 0.5623 0.5076 -0.0264 -0.0353 0.0153  525 LYS B NZ  
4406 N N   . PRO B 515 ? 0.3234 0.4240 0.3478 -0.0480 -0.0679 0.0170  526 PRO B N   
4407 C CA  . PRO B 515 ? 0.3199 0.4298 0.3428 -0.0573 -0.0676 0.0093  526 PRO B CA  
4408 C C   . PRO B 515 ? 0.2964 0.3862 0.3141 -0.0588 -0.0574 -0.0004 526 PRO B C   
4409 O O   . PRO B 515 ? 0.2892 0.3594 0.2988 -0.0542 -0.0504 -0.0025 526 PRO B O   
4410 C CB  . PRO B 515 ? 0.4025 0.5205 0.4074 -0.0695 -0.0692 0.0067  526 PRO B CB  
4411 C CG  . PRO B 515 ? 0.4202 0.5400 0.4219 -0.0644 -0.0733 0.0163  526 PRO B CG  
4412 C CD  . PRO B 515 ? 0.3990 0.5013 0.4080 -0.0532 -0.0686 0.0193  526 PRO B CD  
4413 N N   . LEU B 516 ? 0.3128 0.4088 0.3352 -0.0648 -0.0565 -0.0057 527 LEU B N   
4414 C CA  . LEU B 516 ? 0.3459 0.4205 0.3622 -0.0659 -0.0466 -0.0134 527 LEU B CA  
4415 C C   . LEU B 516 ? 0.3408 0.3932 0.3333 -0.0728 -0.0378 -0.0212 527 LEU B C   
4416 O O   . LEU B 516 ? 0.3378 0.3662 0.3223 -0.0683 -0.0290 -0.0247 527 LEU B O   
4417 C CB  . LEU B 516 ? 0.3583 0.4447 0.3826 -0.0736 -0.0464 -0.0177 527 LEU B CB  
4418 C CG  . LEU B 516 ? 0.3278 0.4323 0.3762 -0.0634 -0.0523 -0.0112 527 LEU B CG  
4419 C CD1 . LEU B 516 ? 0.3393 0.4621 0.3968 -0.0721 -0.0519 -0.0159 527 LEU B CD1 
4420 C CD2 . LEU B 516 ? 0.3068 0.3923 0.3599 -0.0504 -0.0482 -0.0088 527 LEU B CD2 
4421 N N   . SER B 517 ? 0.3622 0.4215 0.3419 -0.0825 -0.0398 -0.0235 528 SER B N   
4422 C CA  . SER B 517 ? 0.3672 0.4032 0.3227 -0.0876 -0.0303 -0.0314 528 SER B CA  
4423 C C   . SER B 517 ? 0.3905 0.4096 0.3440 -0.0729 -0.0248 -0.0282 528 SER B C   
4424 O O   . SER B 517 ? 0.3826 0.3771 0.3192 -0.0713 -0.0144 -0.0345 528 SER B O   
4425 C CB  . SER B 517 ? 0.4127 0.4621 0.3551 -0.0999 -0.0342 -0.0339 528 SER B CB  
4426 O OG  . SER B 517 ? 0.4013 0.4679 0.3522 -0.0925 -0.0424 -0.0238 528 SER B OG  
4427 N N   . SER B 518 ? 0.3265 0.3584 0.2965 -0.0622 -0.0314 -0.0186 529 SER B N   
4428 C CA  . SER B 518 ? 0.3198 0.3420 0.2910 -0.0497 -0.0271 -0.0154 529 SER B CA  
4429 C C   . SER B 518 ? 0.3288 0.3327 0.3007 -0.0414 -0.0200 -0.0179 529 SER B C   
4430 O O   . SER B 518 ? 0.3307 0.3263 0.3005 -0.0312 -0.0150 -0.0169 529 SER B O   
4431 C CB  . SER B 518 ? 0.3702 0.4084 0.3583 -0.0430 -0.0354 -0.0052 529 SER B CB  
4432 O OG  . SER B 518 ? 0.3984 0.4398 0.4031 -0.0381 -0.0391 -0.0021 529 SER B OG  
4433 N N   . LEU B 519 ? 0.3425 0.3422 0.3174 -0.0454 -0.0196 -0.0206 530 LEU B N   
4434 C CA  . LEU B 519 ? 0.3009 0.2816 0.2730 -0.0378 -0.0125 -0.0222 530 LEU B CA  
4435 C C   . LEU B 519 ? 0.3731 0.3262 0.3218 -0.0402 -0.0012 -0.0296 530 LEU B C   
4436 O O   . LEU B 519 ? 0.3712 0.3057 0.3141 -0.0303 0.0056  -0.0292 530 LEU B O   
4437 C CB  . LEU B 519 ? 0.2936 0.2794 0.2771 -0.0409 -0.0151 -0.0219 530 LEU B CB  
4438 C CG  . LEU B 519 ? 0.3140 0.3222 0.3199 -0.0366 -0.0246 -0.0152 530 LEU B CG  
4439 C CD1 . LEU B 519 ? 0.3005 0.3122 0.3160 -0.0385 -0.0245 -0.0165 530 LEU B CD1 
4440 C CD2 . LEU B 519 ? 0.3148 0.3237 0.3278 -0.0244 -0.0261 -0.0096 530 LEU B CD2 
4441 N N   . THR B 520 ? 0.3726 0.3211 0.3059 -0.0528 0.0014  -0.0363 531 THR B N   
4442 C CA  . THR B 520 ? 0.3829 0.2988 0.2915 -0.0562 0.0138  -0.0444 531 THR B CA  
4443 C C   . THR B 520 ? 0.4002 0.2985 0.2981 -0.0408 0.0221  -0.0440 531 THR B C   
4444 O O   . THR B 520 ? 0.4099 0.2778 0.2918 -0.0347 0.0326  -0.0468 531 THR B O   
4445 C CB  . THR B 520 ? 0.4275 0.3404 0.3192 -0.0759 0.0157  -0.0537 531 THR B CB  
4446 O OG1 . THR B 520 ? 0.4027 0.3255 0.2885 -0.0773 0.0140  -0.0549 531 THR B OG1 
4447 C CG2 . THR B 520 ? 0.4149 0.3536 0.3204 -0.0902 0.0064  -0.0534 531 THR B CG2 
4448 N N   . PRO B 521 ? 0.3802 0.2963 0.2861 -0.0334 0.0185  -0.0400 532 PRO B N   
4449 C CA  . PRO B 521 ? 0.3702 0.2752 0.2700 -0.0168 0.0266  -0.0390 532 PRO B CA  
4450 C C   . PRO B 521 ? 0.3686 0.2713 0.2789 -0.0016 0.0266  -0.0324 532 PRO B C   
4451 O O   . PRO B 521 ? 0.3779 0.2615 0.2776 0.0120  0.0357  -0.0326 532 PRO B O   
4452 C CB  . PRO B 521 ? 0.3676 0.2989 0.2769 -0.0155 0.0213  -0.0355 532 PRO B CB  
4453 C CG  . PRO B 521 ? 0.4104 0.3536 0.3175 -0.0331 0.0147  -0.0381 532 PRO B CG  
4454 C CD  . PRO B 521 ? 0.3522 0.2968 0.2684 -0.0404 0.0088  -0.0370 532 PRO B CD  
4455 N N   . LEU B 522 ? 0.2992 0.2201 0.2289 -0.0032 0.0171  -0.0268 533 LEU B N   
4456 C CA  . LEU B 522 ? 0.3185 0.2378 0.2562 0.0092  0.0169  -0.0213 533 LEU B CA  
4457 C C   . LEU B 522 ? 0.3522 0.2401 0.2724 0.0103  0.0255  -0.0240 533 LEU B C   
4458 O O   . LEU B 522 ? 0.3610 0.2362 0.2753 0.0250  0.0308  -0.0206 533 LEU B O   
4459 C CB  . LEU B 522 ? 0.3264 0.2680 0.2854 0.0055  0.0062  -0.0165 533 LEU B CB  
4460 C CG  . LEU B 522 ? 0.3781 0.3464 0.3531 0.0046  -0.0020 -0.0124 533 LEU B CG  
4461 C CD1 . LEU B 522 ? 0.3205 0.3034 0.3136 0.0021  -0.0107 -0.0084 533 LEU B CD1 
4462 C CD2 . LEU B 522 ? 0.3393 0.3161 0.3165 0.0166  0.0004  -0.0094 533 LEU B CD2 
4463 N N   . ILE B 523 ? 0.3731 0.2491 0.2841 -0.0056 0.0272  -0.0298 534 ILE B N   
4464 C CA  . ILE B 523 ? 0.3925 0.2349 0.2833 -0.0083 0.0368  -0.0330 534 ILE B CA  
4465 C C   . ILE B 523 ? 0.4185 0.2291 0.2856 0.0015  0.0492  -0.0360 534 ILE B C   
4466 O O   . ILE B 523 ? 0.4532 0.2366 0.3064 0.0126  0.0572  -0.0333 534 ILE B O   
4467 C CB  . ILE B 523 ? 0.4558 0.2964 0.3416 -0.0307 0.0363  -0.0400 534 ILE B CB  
4468 C CG1 . ILE B 523 ? 0.4073 0.2786 0.3175 -0.0364 0.0255  -0.0363 534 ILE B CG1 
4469 C CG2 . ILE B 523 ? 0.5326 0.3334 0.3927 -0.0370 0.0485  -0.0447 534 ILE B CG2 
4470 C CD1 . ILE B 523 ? 0.4557 0.3411 0.3686 -0.0566 0.0217  -0.0420 534 ILE B CD1 
4471 N N   . ALA B 524 ? 0.4565 0.2694 0.3173 -0.0013 0.0514  -0.0413 535 ALA B N   
4472 C CA  . ALA B 524 ? 0.4680 0.2501 0.3056 0.0090  0.0644  -0.0453 535 ALA B CA  
4473 C C   . ALA B 524 ? 0.4664 0.2511 0.3101 0.0348  0.0666  -0.0370 535 ALA B C   
4474 O O   . ALA B 524 ? 0.5067 0.2587 0.3315 0.0485  0.0778  -0.0364 535 ALA B O   
4475 C CB  . ALA B 524 ? 0.5153 0.3058 0.3474 0.0012  0.0656  -0.0526 535 ALA B CB  
4476 N N   . ALA B 525 ? 0.4015 0.2250 0.2709 0.0417  0.0562  -0.0303 536 ALA B N   
4477 C CA  . ALA B 525 ? 0.4373 0.2724 0.3157 0.0642  0.0564  -0.0224 536 ALA B CA  
4478 C C   . ALA B 525 ? 0.4242 0.2439 0.2988 0.0730  0.0572  -0.0161 536 ALA B C   
4479 O O   . ALA B 525 ? 0.4846 0.2883 0.3488 0.0924  0.0644  -0.0116 536 ALA B O   
4480 C CB  . ALA B 525 ? 0.3567 0.2368 0.2627 0.0639  0.0445  -0.0176 536 ALA B CB  
4481 N N   . ALA B 526 ? 0.4545 0.2786 0.3363 0.0595  0.0503  -0.0152 537 ALA B N   
4482 C CA  . ALA B 526 ? 0.5114 0.3227 0.3887 0.0661  0.0510  -0.0092 537 ALA B CA  
4483 C C   . ALA B 526 ? 0.5257 0.2890 0.3727 0.0703  0.0645  -0.0105 537 ALA B C   
4484 O O   . ALA B 526 ? 0.5386 0.2869 0.3762 0.0879  0.0688  -0.0031 537 ALA B O   
4485 C CB  . ALA B 526 ? 0.4023 0.2271 0.2921 0.0495  0.0427  -0.0097 537 ALA B CB  
4486 N N   . LYS B 527 ? 0.5313 0.2691 0.3612 0.0543  0.0716  -0.0197 538 LYS B N   
4487 C CA  . LYS B 527 ? 0.6212 0.3073 0.4185 0.0560  0.0862  -0.0222 538 LYS B CA  
4488 C C   . LYS B 527 ? 0.7275 0.3951 0.5118 0.0809  0.0957  -0.0194 538 LYS B C   
4489 O O   . LYS B 527 ? 0.6466 0.2871 0.4142 0.0931  0.1031  -0.0132 538 LYS B O   
4490 C CB  . LYS B 527 ? 0.6413 0.3077 0.4231 0.0309  0.0915  -0.0344 538 LYS B CB  
4491 C CG  . LYS B 527 ? 0.6362 0.3166 0.4276 0.0074  0.0845  -0.0366 538 LYS B CG  
4492 C CD  . LYS B 527 ? 0.8673 0.5298 0.6416 -0.0180 0.0902  -0.0488 538 LYS B CD  
4493 C CE  . LYS B 527 ? 0.7853 0.4554 0.5642 -0.0401 0.0868  -0.0509 538 LYS B CE  
4494 N NZ  . LYS B 527 ? 0.9153 0.6019 0.7109 -0.0306 0.0805  -0.0409 538 LYS B NZ  
4495 N N   . GLU B 528 ? 0.5799 0.2712 0.3754 0.0868  0.0941  -0.0226 539 GLU B N   
4496 C CA  . GLU B 528 ? 0.6018 0.2829 0.3889 0.1124  0.1031  -0.0199 539 GLU B CA  
4497 C C   . GLU B 528 ? 0.5725 0.2754 0.3737 0.1350  0.0974  -0.0062 539 GLU B C   
4498 O O   . GLU B 528 ? 0.6893 0.3812 0.4811 0.1505  0.1027  0.0005  539 GLU B O   
4499 C CB  . GLU B 528 ? 0.5994 0.3103 0.3993 0.1120  0.1013  -0.0257 539 GLU B CB  
4500 C CG  . GLU B 528 ? 0.6253 0.3424 0.4259 0.1393  0.1083  -0.0218 539 GLU B CG  
4501 C CD  . GLU B 528 ? 0.7553 0.4349 0.5317 0.1431  0.1205  -0.0234 539 GLU B CD  
4502 O OE1 . GLU B 528 ? 0.7876 0.4321 0.5427 0.1244  0.1265  -0.0309 539 GLU B OE1 
4503 O OE2 . GLU B 528 ? 0.7565 0.4436 0.5356 0.1645  0.1240  -0.0172 539 GLU B OE2 
4504 N N   . ALA B 529 ? 0.5203 0.2631 0.3470 0.1324  0.0840  -0.0013 540 ALA B N   
4505 C CA  . ALA B 529 ? 0.5992 0.3659 0.4385 0.1533  0.0782  0.0104  540 ALA B CA  
4506 C C   . ALA B 529 ? 0.6750 0.4164 0.4988 0.1560  0.0800  0.0180  540 ALA B C   
4507 O O   . ALA B 529 ? 0.6629 0.4141 0.4869 0.1731  0.0792  0.0275  540 ALA B O   
4508 C CB  . ALA B 529 ? 0.5122 0.3309 0.3827 0.1440  0.0627  0.0123  540 ALA B CB  
4509 N N   . THR B 530 ? 0.6843 0.3979 0.4954 0.1375  0.0820  0.0141  541 THR B N   
4510 C CA  . THR B 530 ? 0.6644 0.3560 0.4603 0.1366  0.0841  0.0210  541 THR B CA  
4511 C C   . THR B 530 ? 0.9394 0.5877 0.7063 0.1353  0.0972  0.0200  541 THR B C   
4512 O O   . THR B 530 ? 1.0356 0.6620 0.7863 0.1351  0.1008  0.0258  541 THR B O   
4513 C CB  . THR B 530 ? 0.6641 0.3521 0.4624 0.1158  0.0798  0.0176  541 THR B CB  
4514 O OG1 . THR B 530 ? 0.7061 0.3817 0.4998 0.0927  0.0835  0.0056  541 THR B OG1 
4515 C CG2 . THR B 530 ? 0.6351 0.3771 0.4659 0.1129  0.0646  0.0194  541 THR B CG2 
# 
