data_3RKI
# 
_entry.id   3RKI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3RKI         
RCSB  RCSB065044   
WWPDB D_1000065044 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3RKI 
_pdbx_database_status.recvd_initial_deposition_date   2011-04-18 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Swanson, K.A.'   1 
'Settembre, E.C.' 2 
'Shaw, C.A.'      3 
'Dey, A.K.'       4 
'Rappuoli, R.'    5 
'Mandl, C.W.'     6 
'Dormitzer, P.D.' 7 
'Carfi, A.'       8 
# 
_citation.id                        primary 
_citation.title                     
;Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers.
;
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            108 
_citation.page_first                9619 
_citation.page_last                 9624 
_citation.year                      2011 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   21586636 
_citation.pdbx_database_id_DOI      10.1073/pnas.1106536108 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Swanson, K.A.'   1 
primary 'Settembre, E.C.' 2 
primary 'Shaw, C.A.'      3 
primary 'Dey, A.K.'       4 
primary 'Rappuoli, R.'    5 
primary 'Mandl, C.W.'     6 
primary 'Dormitzer, P.R.' 7 
primary 'Carfi, A.'       8 
# 
_cell.entry_id           3RKI 
_cell.length_a           87.930 
_cell.length_b           113.160 
_cell.length_c           311.370 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3RKI 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Fusion glycoprotein F0' 58487.637 3  ? ? 'Respiratory Syncytial Virus F, residues 1-524' 
'Fusion Peptide deleted' 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE   221.208   13 ? ? ?                                               ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Protein F, Fusion glycoprotein F2, Fusion glycoprotein F1' 
# 
_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       
;MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIK
QELDKYKNAVTELQLLMQSTPATNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRSAIASGVAVSKVLHLEGEVNKIKS
ALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVST
YMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEG
SNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEVNLCNVDIFNPKYDCKIMTSKTDVSSSVITS
LGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFD
ASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNGGSAGSGHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIK
QELDKYKNAVTELQLLMQSTPATNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRSAIASGVAVSKVLHLEGEVNKIKS
ALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVST
YMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEG
SNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEVNLCNVDIFNPKYDCKIMTSKTDVSSSVITS
LGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFD
ASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNGGSAGSGHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   LEU n 
1 4   LEU n 
1 5   ILE n 
1 6   LEU n 
1 7   LYS n 
1 8   ALA n 
1 9   ASN n 
1 10  ALA n 
1 11  ILE n 
1 12  THR n 
1 13  THR n 
1 14  ILE n 
1 15  LEU n 
1 16  THR n 
1 17  ALA n 
1 18  VAL n 
1 19  THR n 
1 20  PHE n 
1 21  CYS n 
1 22  PHE n 
1 23  ALA n 
1 24  SER n 
1 25  GLY n 
1 26  GLN n 
1 27  ASN n 
1 28  ILE n 
1 29  THR n 
1 30  GLU n 
1 31  GLU n 
1 32  PHE n 
1 33  TYR n 
1 34  GLN n 
1 35  SER n 
1 36  THR n 
1 37  CYS n 
1 38  SER n 
1 39  ALA n 
1 40  VAL n 
1 41  SER n 
1 42  LYS n 
1 43  GLY n 
1 44  TYR n 
1 45  LEU n 
1 46  SER n 
1 47  ALA n 
1 48  LEU n 
1 49  ARG n 
1 50  THR n 
1 51  GLY n 
1 52  TRP n 
1 53  TYR n 
1 54  THR n 
1 55  SER n 
1 56  VAL n 
1 57  ILE n 
1 58  THR n 
1 59  ILE n 
1 60  GLU n 
1 61  LEU n 
1 62  SER n 
1 63  ASN n 
1 64  ILE n 
1 65  LYS n 
1 66  GLU n 
1 67  ASN n 
1 68  LYS n 
1 69  CYS n 
1 70  ASN n 
1 71  GLY n 
1 72  THR n 
1 73  ASP n 
1 74  ALA n 
1 75  LYS n 
1 76  VAL n 
1 77  LYS n 
1 78  LEU n 
1 79  ILE n 
1 80  LYS n 
1 81  GLN n 
1 82  GLU n 
1 83  LEU n 
1 84  ASP n 
1 85  LYS n 
1 86  TYR n 
1 87  LYS n 
1 88  ASN n 
1 89  ALA n 
1 90  VAL n 
1 91  THR n 
1 92  GLU n 
1 93  LEU n 
1 94  GLN n 
1 95  LEU n 
1 96  LEU n 
1 97  MET n 
1 98  GLN n 
1 99  SER n 
1 100 THR n 
1 101 PRO n 
1 102 ALA n 
1 103 THR n 
1 104 ASN n 
1 105 ASN n 
1 106 ARG n 
1 107 ALA n 
1 108 ARG n 
1 109 ARG n 
1 110 GLU n 
1 111 LEU n 
1 112 PRO n 
1 113 ARG n 
1 114 PHE n 
1 115 MET n 
1 116 ASN n 
1 117 TYR n 
1 118 THR n 
1 119 LEU n 
1 120 ASN n 
1 121 ASN n 
1 122 ALA n 
1 123 LYS n 
1 124 LYS n 
1 125 THR n 
1 126 ASN n 
1 127 VAL n 
1 128 THR n 
1 129 LEU n 
1 130 SER n 
1 131 LYS n 
1 132 LYS n 
1 133 ARG n 
1 134 LYS n 
1 135 ARG n 
1 136 ARG n 
1 137 SER n 
1 138 ALA n 
1 139 ILE n 
1 140 ALA n 
1 141 SER n 
1 142 GLY n 
1 143 VAL n 
1 144 ALA n 
1 145 VAL n 
1 146 SER n 
1 147 LYS n 
1 148 VAL n 
1 149 LEU n 
1 150 HIS n 
1 151 LEU n 
1 152 GLU n 
1 153 GLY n 
1 154 GLU n 
1 155 VAL n 
1 156 ASN n 
1 157 LYS n 
1 158 ILE n 
1 159 LYS n 
1 160 SER n 
1 161 ALA n 
1 162 LEU n 
1 163 LEU n 
1 164 SER n 
1 165 THR n 
1 166 ASN n 
1 167 LYS n 
1 168 ALA n 
1 169 VAL n 
1 170 VAL n 
1 171 SER n 
1 172 LEU n 
1 173 SER n 
1 174 ASN n 
1 175 GLY n 
1 176 VAL n 
1 177 SER n 
1 178 VAL n 
1 179 LEU n 
1 180 THR n 
1 181 SER n 
1 182 LYS n 
1 183 VAL n 
1 184 LEU n 
1 185 ASP n 
1 186 LEU n 
1 187 LYS n 
1 188 ASN n 
1 189 TYR n 
1 190 ILE n 
1 191 ASP n 
1 192 LYS n 
1 193 GLN n 
1 194 LEU n 
1 195 LEU n 
1 196 PRO n 
1 197 ILE n 
1 198 VAL n 
1 199 ASN n 
1 200 LYS n 
1 201 GLN n 
1 202 SER n 
1 203 CYS n 
1 204 SER n 
1 205 ILE n 
1 206 SER n 
1 207 ASN n 
1 208 ILE n 
1 209 GLU n 
1 210 THR n 
1 211 VAL n 
1 212 ILE n 
1 213 GLU n 
1 214 PHE n 
1 215 GLN n 
1 216 GLN n 
1 217 LYS n 
1 218 ASN n 
1 219 ASN n 
1 220 ARG n 
1 221 LEU n 
1 222 LEU n 
1 223 GLU n 
1 224 ILE n 
1 225 THR n 
1 226 ARG n 
1 227 GLU n 
1 228 PHE n 
1 229 SER n 
1 230 VAL n 
1 231 ASN n 
1 232 ALA n 
1 233 GLY n 
1 234 VAL n 
1 235 THR n 
1 236 THR n 
1 237 PRO n 
1 238 VAL n 
1 239 SER n 
1 240 THR n 
1 241 TYR n 
1 242 MET n 
1 243 LEU n 
1 244 THR n 
1 245 ASN n 
1 246 SER n 
1 247 GLU n 
1 248 LEU n 
1 249 LEU n 
1 250 SER n 
1 251 LEU n 
1 252 ILE n 
1 253 ASN n 
1 254 ASP n 
1 255 MET n 
1 256 PRO n 
1 257 ILE n 
1 258 THR n 
1 259 ASN n 
1 260 ASP n 
1 261 GLN n 
1 262 LYS n 
1 263 LYS n 
1 264 LEU n 
1 265 MET n 
1 266 SER n 
1 267 ASN n 
1 268 ASN n 
1 269 VAL n 
1 270 GLN n 
1 271 ILE n 
1 272 VAL n 
1 273 ARG n 
1 274 GLN n 
1 275 GLN n 
1 276 SER n 
1 277 TYR n 
1 278 SER n 
1 279 ILE n 
1 280 MET n 
1 281 SER n 
1 282 ILE n 
1 283 ILE n 
1 284 LYS n 
1 285 GLU n 
1 286 GLU n 
1 287 VAL n 
1 288 LEU n 
1 289 ALA n 
1 290 TYR n 
1 291 VAL n 
1 292 VAL n 
1 293 GLN n 
1 294 LEU n 
1 295 PRO n 
1 296 LEU n 
1 297 TYR n 
1 298 GLY n 
1 299 VAL n 
1 300 ILE n 
1 301 ASP n 
1 302 THR n 
1 303 PRO n 
1 304 CYS n 
1 305 TRP n 
1 306 LYS n 
1 307 LEU n 
1 308 HIS n 
1 309 THR n 
1 310 SER n 
1 311 PRO n 
1 312 LEU n 
1 313 CYS n 
1 314 THR n 
1 315 THR n 
1 316 ASN n 
1 317 THR n 
1 318 LYS n 
1 319 GLU n 
1 320 GLY n 
1 321 SER n 
1 322 ASN n 
1 323 ILE n 
1 324 CYS n 
1 325 LEU n 
1 326 THR n 
1 327 ARG n 
1 328 THR n 
1 329 ASP n 
1 330 ARG n 
1 331 GLY n 
1 332 TRP n 
1 333 TYR n 
1 334 CYS n 
1 335 ASP n 
1 336 ASN n 
1 337 ALA n 
1 338 GLY n 
1 339 SER n 
1 340 VAL n 
1 341 SER n 
1 342 PHE n 
1 343 PHE n 
1 344 PRO n 
1 345 GLN n 
1 346 ALA n 
1 347 GLU n 
1 348 THR n 
1 349 CYS n 
1 350 LYS n 
1 351 VAL n 
1 352 GLN n 
1 353 SER n 
1 354 ASN n 
1 355 ARG n 
1 356 VAL n 
1 357 PHE n 
1 358 CYS n 
1 359 ASP n 
1 360 THR n 
1 361 MET n 
1 362 ASN n 
1 363 SER n 
1 364 LEU n 
1 365 THR n 
1 366 LEU n 
1 367 PRO n 
1 368 SER n 
1 369 GLU n 
1 370 VAL n 
1 371 ASN n 
1 372 LEU n 
1 373 CYS n 
1 374 ASN n 
1 375 VAL n 
1 376 ASP n 
1 377 ILE n 
1 378 PHE n 
1 379 ASN n 
1 380 PRO n 
1 381 LYS n 
1 382 TYR n 
1 383 ASP n 
1 384 CYS n 
1 385 LYS n 
1 386 ILE n 
1 387 MET n 
1 388 THR n 
1 389 SER n 
1 390 LYS n 
1 391 THR n 
1 392 ASP n 
1 393 VAL n 
1 394 SER n 
1 395 SER n 
1 396 SER n 
1 397 VAL n 
1 398 ILE n 
1 399 THR n 
1 400 SER n 
1 401 LEU n 
1 402 GLY n 
1 403 ALA n 
1 404 ILE n 
1 405 VAL n 
1 406 SER n 
1 407 CYS n 
1 408 TYR n 
1 409 GLY n 
1 410 LYS n 
1 411 THR n 
1 412 LYS n 
1 413 CYS n 
1 414 THR n 
1 415 ALA n 
1 416 SER n 
1 417 ASN n 
1 418 LYS n 
1 419 ASN n 
1 420 ARG n 
1 421 GLY n 
1 422 ILE n 
1 423 ILE n 
1 424 LYS n 
1 425 THR n 
1 426 PHE n 
1 427 SER n 
1 428 ASN n 
1 429 GLY n 
1 430 CYS n 
1 431 ASP n 
1 432 TYR n 
1 433 VAL n 
1 434 SER n 
1 435 ASN n 
1 436 LYS n 
1 437 GLY n 
1 438 VAL n 
1 439 ASP n 
1 440 THR n 
1 441 VAL n 
1 442 SER n 
1 443 VAL n 
1 444 GLY n 
1 445 ASN n 
1 446 THR n 
1 447 LEU n 
1 448 TYR n 
1 449 TYR n 
1 450 VAL n 
1 451 ASN n 
1 452 LYS n 
1 453 GLN n 
1 454 GLU n 
1 455 GLY n 
1 456 LYS n 
1 457 SER n 
1 458 LEU n 
1 459 TYR n 
1 460 VAL n 
1 461 LYS n 
1 462 GLY n 
1 463 GLU n 
1 464 PRO n 
1 465 ILE n 
1 466 ILE n 
1 467 ASN n 
1 468 PHE n 
1 469 TYR n 
1 470 ASP n 
1 471 PRO n 
1 472 LEU n 
1 473 VAL n 
1 474 PHE n 
1 475 PRO n 
1 476 SER n 
1 477 ASP n 
1 478 GLU n 
1 479 PHE n 
1 480 ASP n 
1 481 ALA n 
1 482 SER n 
1 483 ILE n 
1 484 SER n 
1 485 GLN n 
1 486 VAL n 
1 487 ASN n 
1 488 GLU n 
1 489 LYS n 
1 490 ILE n 
1 491 ASN n 
1 492 GLN n 
1 493 SER n 
1 494 LEU n 
1 495 ALA n 
1 496 PHE n 
1 497 ILE n 
1 498 ARG n 
1 499 LYS n 
1 500 SER n 
1 501 ASP n 
1 502 GLU n 
1 503 LEU n 
1 504 LEU n 
1 505 HIS n 
1 506 ASN n 
1 507 VAL n 
1 508 ASN n 
1 509 ALA n 
1 510 GLY n 
1 511 LYS n 
1 512 SER n 
1 513 THR n 
1 514 THR n 
1 515 ASN n 
1 516 GLY n 
1 517 GLY n 
1 518 SER n 
1 519 ALA n 
1 520 GLY n 
1 521 SER n 
1 522 GLY n 
1 523 HIS n 
1 524 HIS n 
1 525 HIS n 
1 526 HIS n 
1 527 HIS n 
1 528 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 F 
_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      'Human respiratory syncytial virus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11250 
_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               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FUS_HRSVA 
_struct_ref.pdbx_db_accession          P03420 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIK
QELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHL
EGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVN
AGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSP
LCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEINLCNVDIFNPKYDCKIMTSKT
DVSSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGMDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDP
LVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTN
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
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 3RKI A 1 ? 515 ? P03420 1 ? 524 ? 1 524 
2 1 3RKI B 1 ? 515 ? P03420 1 ? 524 ? 1 524 
3 1 3RKI C 1 ? 515 ? P03420 1 ? 524 ? 1 524 
# 
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 3RKI ALA A 102 ? UNP P03420 PRO 102 VARIANT          111 1  
1 3RKI ?   A ?   ? UNP P03420 PHE 137 DELETION         ?   2  
1 3RKI ?   A ?   ? UNP P03420 LEU 138 DELETION         ?   3  
1 3RKI ?   A ?   ? UNP P03420 GLY 139 DELETION         ?   4  
1 3RKI ?   A ?   ? UNP P03420 PHE 140 DELETION         ?   5  
1 3RKI ?   A ?   ? UNP P03420 LEU 141 DELETION         ?   6  
1 3RKI ?   A ?   ? UNP P03420 LEU 142 DELETION         ?   7  
1 3RKI ?   A ?   ? UNP P03420 GLY 143 DELETION         ?   8  
1 3RKI ?   A ?   ? UNP P03420 VAL 144 DELETION         ?   9  
1 3RKI ?   A ?   ? UNP P03420 GLY 145 DELETION         ?   10 
1 3RKI VAL A 370 ? UNP P03420 ILE 379 VARIANT          379 11 
1 3RKI VAL A 438 ? UNP P03420 MET 447 VARIANT          447 12 
1 3RKI GLY A 516 ? UNP P03420 ?   ?   'EXPRESSION TAG' 525 13 
1 3RKI GLY A 517 ? UNP P03420 ?   ?   'EXPRESSION TAG' 526 14 
1 3RKI SER A 518 ? UNP P03420 ?   ?   'EXPRESSION TAG' 527 15 
1 3RKI ALA A 519 ? UNP P03420 ?   ?   'EXPRESSION TAG' 528 16 
1 3RKI GLY A 520 ? UNP P03420 ?   ?   'EXPRESSION TAG' 529 17 
1 3RKI SER A 521 ? UNP P03420 ?   ?   'EXPRESSION TAG' 530 18 
1 3RKI GLY A 522 ? UNP P03420 ?   ?   'EXPRESSION TAG' 531 19 
1 3RKI HIS A 523 ? UNP P03420 ?   ?   'EXPRESSION TAG' 532 20 
1 3RKI HIS A 524 ? UNP P03420 ?   ?   'EXPRESSION TAG' 533 21 
1 3RKI HIS A 525 ? UNP P03420 ?   ?   'EXPRESSION TAG' 534 22 
1 3RKI HIS A 526 ? UNP P03420 ?   ?   'EXPRESSION TAG' 535 23 
1 3RKI HIS A 527 ? UNP P03420 ?   ?   'EXPRESSION TAG' 536 24 
1 3RKI HIS A 528 ? UNP P03420 ?   ?   'EXPRESSION TAG' 537 25 
2 3RKI ALA B 102 ? UNP P03420 PRO 102 VARIANT          111 26 
2 3RKI ?   B ?   ? UNP P03420 PHE 137 DELETION         ?   27 
2 3RKI ?   B ?   ? UNP P03420 LEU 138 DELETION         ?   28 
2 3RKI ?   B ?   ? UNP P03420 GLY 139 DELETION         ?   29 
2 3RKI ?   B ?   ? UNP P03420 PHE 140 DELETION         ?   30 
2 3RKI ?   B ?   ? UNP P03420 LEU 141 DELETION         ?   31 
2 3RKI ?   B ?   ? UNP P03420 LEU 142 DELETION         ?   32 
2 3RKI ?   B ?   ? UNP P03420 GLY 143 DELETION         ?   33 
2 3RKI ?   B ?   ? UNP P03420 VAL 144 DELETION         ?   34 
2 3RKI ?   B ?   ? UNP P03420 GLY 145 DELETION         ?   35 
2 3RKI VAL B 370 ? UNP P03420 ILE 379 VARIANT          379 36 
2 3RKI VAL B 438 ? UNP P03420 MET 447 VARIANT          447 37 
2 3RKI GLY B 516 ? UNP P03420 ?   ?   'EXPRESSION TAG' 525 38 
2 3RKI GLY B 517 ? UNP P03420 ?   ?   'EXPRESSION TAG' 526 39 
2 3RKI SER B 518 ? UNP P03420 ?   ?   'EXPRESSION TAG' 527 40 
2 3RKI ALA B 519 ? UNP P03420 ?   ?   'EXPRESSION TAG' 528 41 
2 3RKI GLY B 520 ? UNP P03420 ?   ?   'EXPRESSION TAG' 529 42 
2 3RKI SER B 521 ? UNP P03420 ?   ?   'EXPRESSION TAG' 530 43 
2 3RKI GLY B 522 ? UNP P03420 ?   ?   'EXPRESSION TAG' 531 44 
2 3RKI HIS B 523 ? UNP P03420 ?   ?   'EXPRESSION TAG' 532 45 
2 3RKI HIS B 524 ? UNP P03420 ?   ?   'EXPRESSION TAG' 533 46 
2 3RKI HIS B 525 ? UNP P03420 ?   ?   'EXPRESSION TAG' 534 47 
2 3RKI HIS B 526 ? UNP P03420 ?   ?   'EXPRESSION TAG' 535 48 
2 3RKI HIS B 527 ? UNP P03420 ?   ?   'EXPRESSION TAG' 536 49 
2 3RKI HIS B 528 ? UNP P03420 ?   ?   'EXPRESSION TAG' 537 50 
3 3RKI ALA C 102 ? UNP P03420 PRO 102 VARIANT          111 51 
3 3RKI ?   C ?   ? UNP P03420 PHE 137 DELETION         ?   52 
3 3RKI ?   C ?   ? UNP P03420 LEU 138 DELETION         ?   53 
3 3RKI ?   C ?   ? UNP P03420 GLY 139 DELETION         ?   54 
3 3RKI ?   C ?   ? UNP P03420 PHE 140 DELETION         ?   55 
3 3RKI ?   C ?   ? UNP P03420 LEU 141 DELETION         ?   56 
3 3RKI ?   C ?   ? UNP P03420 LEU 142 DELETION         ?   57 
3 3RKI ?   C ?   ? UNP P03420 GLY 143 DELETION         ?   58 
3 3RKI ?   C ?   ? UNP P03420 VAL 144 DELETION         ?   59 
3 3RKI ?   C ?   ? UNP P03420 GLY 145 DELETION         ?   60 
3 3RKI VAL C 370 ? UNP P03420 ILE 379 VARIANT          379 61 
3 3RKI VAL C 438 ? UNP P03420 MET 447 VARIANT          447 62 
3 3RKI GLY C 516 ? UNP P03420 ?   ?   'EXPRESSION TAG' 525 63 
3 3RKI GLY C 517 ? UNP P03420 ?   ?   'EXPRESSION TAG' 526 64 
3 3RKI SER C 518 ? UNP P03420 ?   ?   'EXPRESSION TAG' 527 65 
3 3RKI ALA C 519 ? UNP P03420 ?   ?   'EXPRESSION TAG' 528 66 
3 3RKI GLY C 520 ? UNP P03420 ?   ?   'EXPRESSION TAG' 529 67 
3 3RKI SER C 521 ? UNP P03420 ?   ?   'EXPRESSION TAG' 530 68 
3 3RKI GLY C 522 ? UNP P03420 ?   ?   'EXPRESSION TAG' 531 69 
3 3RKI HIS C 523 ? UNP P03420 ?   ?   'EXPRESSION TAG' 532 70 
3 3RKI HIS C 524 ? UNP P03420 ?   ?   'EXPRESSION TAG' 533 71 
3 3RKI HIS C 525 ? UNP P03420 ?   ?   'EXPRESSION TAG' 534 72 
3 3RKI HIS C 526 ? UNP P03420 ?   ?   'EXPRESSION TAG' 535 73 
3 3RKI HIS C 527 ? UNP P03420 ?   ?   'EXPRESSION TAG' 536 74 
3 3RKI HIS C 528 ? UNP P03420 ?   ?   'EXPRESSION TAG' 537 75 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3RKI 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.41 
_exptl_crystal.density_percent_sol   72.14 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.1 
_exptl_crystal_grow.pdbx_details    
'4.2 M Sodium Formate, 100 mM Sodium Acetate, pH 5.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2010-06-10 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si (111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     3RKI 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            3.2 
_reflns.number_obs                   51911 
_reflns.number_all                   52224 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             3.2 
_reflns_shell.d_res_low              3.3 
_reflns_shell.percent_possible_all   ? 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3RKI 
_refine.ls_number_reflns_obs                     38122 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             30.00 
_refine.ls_d_res_high                            3.20 
_refine.ls_percent_reflns_obs                    77.04 
_refine.ls_R_factor_obs                          0.22984 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22798 
_refine.ls_R_factor_R_free                       0.26428 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2065 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.892 
_refine.correlation_coeff_Fo_to_Fc_free          0.856 
_refine.B_iso_mean                               16.264 
_refine.aniso_B[1][1]                            2.05 
_refine.aniso_B[2][2]                            -1.72 
_refine.aniso_B[3][3]                            -0.33 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      '3KPE and 1ZTM' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  0.491 
_refine.overall_SU_ML                            0.357 
_refine.overall_SU_B                             48.729 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        10256 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         182 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               10438 
_refine_hist.d_res_high                       3.20 
_refine_hist.d_res_low                        30.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.020  0.022  ? 10614 ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.963  1.984  ? 14410 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 9.368  5.000  ? 1311  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 41.694 26.276 ? 427   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 23.676 15.000 ? 1937  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 20.117 15.000 ? 27    ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.130  0.200  ? 1764  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.008  0.021  ? 7607  ? 'X-RAY DIFFRACTION' 
r_mcbond_it            0.518  1.500  ? 6569  ? 'X-RAY DIFFRACTION' 
r_mcangle_it           1.071  2.000  ? 10744 ? 'X-RAY DIFFRACTION' 
r_scbond_it            1.932  3.000  ? 4045  ? 'X-RAY DIFFRACTION' 
r_scangle_it           3.691  4.500  ? 3666  ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
'X-RAY DIFFRACTION' 1 1 'TIGHT POSITIONAL' A 1664 0.060 0.050  1  ? ? ? 
'X-RAY DIFFRACTION' 1 2 'TIGHT POSITIONAL' B 1664 0.060 0.050  2  ? ? ? 
'X-RAY DIFFRACTION' 1 3 'TIGHT POSITIONAL' C 1664 0.060 0.050  3  ? ? ? 
'X-RAY DIFFRACTION' 1 1 'LOOSE POSITIONAL' A 1585 0.070 5.000  4  ? ? ? 
'X-RAY DIFFRACTION' 1 2 'LOOSE POSITIONAL' B 1585 0.070 5.000  5  ? ? ? 
'X-RAY DIFFRACTION' 1 3 'LOOSE POSITIONAL' C 1585 0.070 5.000  6  ? ? ? 
'X-RAY DIFFRACTION' 1 1 'TIGHT THERMAL'    A 1664 0.100 0.500  7  ? ? ? 
'X-RAY DIFFRACTION' 1 2 'TIGHT THERMAL'    B 1664 0.090 0.500  8  ? ? ? 
'X-RAY DIFFRACTION' 1 3 'TIGHT THERMAL'    C 1664 0.090 0.500  9  ? ? ? 
'X-RAY DIFFRACTION' 1 1 'LOOSE THERMAL'    A 1585 0.110 10.000 10 ? ? ? 
'X-RAY DIFFRACTION' 1 2 'LOOSE THERMAL'    B 1585 0.100 10.000 11 ? ? ? 
'X-RAY DIFFRACTION' 1 3 'LOOSE THERMAL'    C 1585 0.100 10.000 12 ? ? ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       3.200 
_refine_ls_shell.d_res_low                        3.282 
_refine_ls_shell.number_reflns_R_work             682 
_refine_ls_shell.R_factor_R_work                  0.338 
_refine_ls_shell.percent_reflns_obs               19.24 
_refine_ls_shell.R_factor_R_free                  0.412 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             42 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 A 1 
2 B 1 
3 C 1 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1 A 27  A 98  1 3 ? ? ? ? ? ? ? ? 1 ? 
2 B 27  B 98  1 3 ? ? ? ? ? ? ? ? 1 ? 
3 C 27  C 98  1 3 ? ? ? ? ? ? ? ? 1 ? 
1 A 162 A 321 2 3 ? ? ? ? ? ? ? ? 1 ? 
2 B 162 B 321 2 3 ? ? ? ? ? ? ? ? 1 ? 
3 C 162 C 321 2 3 ? ? ? ? ? ? ? ? 1 ? 
1 A 334 A 517 3 3 ? ? ? ? ? ? ? ? 1 ? 
2 B 334 B 517 3 3 ? ? ? ? ? ? ? ? 1 ? 
3 C 334 C 517 3 3 ? ? ? ? ? ? ? ? 1 ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  3RKI 
_struct.title                     
'Structural basis for immunization with post-fusion RSV F to elicit high neutralizing antibody titers' 
_struct.pdbx_descriptor           'Fusion glycoprotein F0' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3RKI 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'Fusion Protein, VIRAL PROTEIN' 
# 
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 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLN A 34  ? THR A 36  ? GLN A 34  THR A 36  5 ? 3  
HELX_P HELX_P2  2  LYS A 77  ? LEU A 95  ? LYS A 77  LEU A 95  1 ? 19 
HELX_P HELX_P3  3  LEU A 96  ? GLN A 98  ? LEU A 96  GLN A 98  5 ? 3  
HELX_P HELX_P4  4  ALA A 144 ? GLN A 193 ? ALA A 153 GLN A 202 1 ? 50 
HELX_P HELX_P5  5  GLN A 193 ? ASN A 218 ? GLN A 202 ASN A 227 1 ? 26 
HELX_P HELX_P6  6  ASN A 218 ? ALA A 232 ? ASN A 227 ALA A 241 1 ? 15 
HELX_P HELX_P7  7  THR A 244 ? MET A 255 ? THR A 253 MET A 264 1 ? 12 
HELX_P HELX_P8  8  THR A 258 ? ASN A 267 ? THR A 267 ASN A 276 1 ? 10 
HELX_P HELX_P9  9  ASN A 268 ? SER A 276 ? ASN A 277 SER A 285 1 ? 9  
HELX_P HELX_P10 10 GLN A 345 ? GLU A 347 ? GLN A 354 GLU A 356 5 ? 3  
HELX_P HELX_P11 11 MET A 361 ? SER A 363 ? MET A 370 SER A 372 5 ? 3  
HELX_P HELX_P12 12 PRO A 367 ? VAL A 375 ? PRO A 376 VAL A 384 5 ? 9  
HELX_P HELX_P13 13 PRO A 475 ? HIS A 505 ? PRO A 484 HIS A 514 1 ? 31 
HELX_P HELX_P14 14 GLN B 34  ? THR B 36  ? GLN B 34  THR B 36  5 ? 3  
HELX_P HELX_P15 15 LYS B 77  ? LEU B 95  ? LYS B 77  LEU B 95  1 ? 19 
HELX_P HELX_P16 16 LEU B 96  ? GLN B 98  ? LEU B 96  GLN B 98  5 ? 3  
HELX_P HELX_P17 17 ALA B 144 ? GLN B 193 ? ALA B 153 GLN B 202 1 ? 50 
HELX_P HELX_P18 18 GLN B 193 ? ASN B 218 ? GLN B 202 ASN B 227 1 ? 26 
HELX_P HELX_P19 19 ASN B 218 ? ASN B 231 ? ASN B 227 ASN B 240 1 ? 14 
HELX_P HELX_P20 20 THR B 244 ? MET B 255 ? THR B 253 MET B 264 1 ? 12 
HELX_P HELX_P21 21 THR B 258 ? ASN B 267 ? THR B 267 ASN B 276 1 ? 10 
HELX_P HELX_P22 22 ASN B 268 ? GLN B 275 ? ASN B 277 GLN B 284 1 ? 8  
HELX_P HELX_P23 23 GLN B 345 ? CYS B 349 ? GLN B 354 CYS B 358 5 ? 5  
HELX_P HELX_P24 24 MET B 361 ? SER B 363 ? MET B 370 SER B 372 5 ? 3  
HELX_P HELX_P25 25 PRO B 367 ? VAL B 375 ? PRO B 376 VAL B 384 5 ? 9  
HELX_P HELX_P26 26 PRO B 475 ? HIS B 505 ? PRO B 484 HIS B 514 1 ? 31 
HELX_P HELX_P27 27 GLN C 34  ? THR C 36  ? GLN C 34  THR C 36  5 ? 3  
HELX_P HELX_P28 28 LYS C 77  ? LEU C 96  ? LYS C 77  LEU C 96  1 ? 20 
HELX_P HELX_P29 29 VAL C 148 ? GLN C 193 ? VAL C 157 GLN C 202 1 ? 46 
HELX_P HELX_P30 30 GLN C 193 ? ASN C 218 ? GLN C 202 ASN C 227 1 ? 26 
HELX_P HELX_P31 31 ASN C 218 ? ASN C 231 ? ASN C 227 ASN C 240 1 ? 14 
HELX_P HELX_P32 32 THR C 244 ? MET C 255 ? THR C 253 MET C 264 1 ? 12 
HELX_P HELX_P33 33 THR C 258 ? ASN C 267 ? THR C 267 ASN C 276 1 ? 10 
HELX_P HELX_P34 34 ASN C 268 ? SER C 276 ? ASN C 277 SER C 285 1 ? 9  
HELX_P HELX_P35 35 GLN C 345 ? GLU C 347 ? GLN C 354 GLU C 356 5 ? 3  
HELX_P HELX_P36 36 MET C 361 ? SER C 363 ? MET C 370 SER C 372 5 ? 3  
HELX_P HELX_P37 37 PRO C 367 ? VAL C 375 ? PRO C 376 VAL C 384 5 ? 9  
HELX_P HELX_P38 38 PRO C 475 ? HIS C 505 ? PRO C 484 HIS C 514 1 ? 31 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 37  SG  ? ? ? 1_555 A CYS 430 SG ? ? A CYS 37   A CYS 439  1_555 ? ? ? ? ? ? ? 2.075 ? 
disulf2  disulf ? ? A CYS 69  SG  ? ? ? 1_555 A CYS 203 SG ? ? A CYS 69   A CYS 212  1_555 ? ? ? ? ? ? ? 2.008 ? 
disulf3  disulf ? ? A CYS 304 SG  ? ? ? 1_555 A CYS 334 SG ? ? A CYS 313  A CYS 343  1_555 ? ? ? ? ? ? ? 2.080 ? 
disulf4  disulf ? ? A CYS 313 SG  ? ? ? 1_555 A CYS 324 SG ? ? A CYS 322  A CYS 333  1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf5  disulf ? ? A CYS 349 SG  ? ? ? 1_555 A CYS 358 SG ? ? A CYS 358  A CYS 367  1_555 ? ? ? ? ? ? ? 2.021 ? 
disulf6  disulf ? ? A CYS 373 SG  ? ? ? 1_555 A CYS 384 SG ? ? A CYS 382  A CYS 393  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf7  disulf ? ? A CYS 407 SG  ? ? ? 1_555 A CYS 413 SG ? ? A CYS 416  A CYS 422  1_555 ? ? ? ? ? ? ? 2.075 ? 
disulf8  disulf ? ? B CYS 37  SG  ? ? ? 1_555 B CYS 430 SG ? ? B CYS 37   B CYS 439  1_555 ? ? ? ? ? ? ? 2.077 ? 
disulf9  disulf ? ? B CYS 69  SG  ? ? ? 1_555 B CYS 203 SG ? ? B CYS 69   B CYS 212  1_555 ? ? ? ? ? ? ? 2.016 ? 
disulf10 disulf ? ? B CYS 304 SG  ? ? ? 1_555 B CYS 334 SG ? ? B CYS 313  B CYS 343  1_555 ? ? ? ? ? ? ? 2.072 ? 
disulf11 disulf ? ? B CYS 313 SG  ? ? ? 1_555 B CYS 324 SG ? ? B CYS 322  B CYS 333  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf12 disulf ? ? B CYS 349 SG  ? ? ? 1_555 B CYS 358 SG ? ? B CYS 358  B CYS 367  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf13 disulf ? ? B CYS 373 SG  ? ? ? 1_555 B CYS 384 SG ? ? B CYS 382  B CYS 393  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf14 disulf ? ? B CYS 407 SG  ? ? ? 1_555 B CYS 413 SG ? ? B CYS 416  B CYS 422  1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf15 disulf ? ? C CYS 37  SG  ? ? ? 1_555 C CYS 430 SG ? ? C CYS 37   C CYS 439  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf16 disulf ? ? C CYS 69  SG  ? ? ? 1_555 C CYS 203 SG ? ? C CYS 69   C CYS 212  1_555 ? ? ? ? ? ? ? 2.015 ? 
disulf17 disulf ? ? C CYS 304 SG  ? ? ? 1_555 C CYS 334 SG ? ? C CYS 313  C CYS 343  1_555 ? ? ? ? ? ? ? 2.108 ? 
disulf18 disulf ? ? C CYS 313 SG  ? ? ? 1_555 C CYS 324 SG ? ? C CYS 322  C CYS 333  1_555 ? ? ? ? ? ? ? 2.062 ? 
disulf19 disulf ? ? C CYS 349 SG  ? ? ? 1_555 C CYS 358 SG ? ? C CYS 358  C CYS 367  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf20 disulf ? ? C CYS 373 SG  ? ? ? 1_555 C CYS 384 SG ? ? C CYS 382  C CYS 393  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf21 disulf ? ? C CYS 407 SG  ? ? ? 1_555 C CYS 413 SG ? ? C CYS 416  C CYS 422  1_555 ? ? ? ? ? ? ? 2.044 ? 
covale1  covale ? ? B ASN 70  ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 70   B NAG 1535 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale2  covale ? ? C ASN 70  ND2 ? ? ? 1_555 O NAG .   C1 ? ? C ASN 70   C NAG 1535 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale3  covale ? ? B ASN 491 ND2 ? ? ? 1_555 K NAG .   C1 ? ? B ASN 500  B NAG 1545 1_555 ? ? ? ? ? ? ? 1.453 ? 
covale4  covale ? ? I NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? B NAG 1535 B NAG 1536 1_555 ? ? ? ? ? ? ? 1.459 ? 
covale5  covale ? ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? C NAG 1545 C NAG 1546 1_555 ? ? ? ? ? ? ? 1.461 ? 
covale6  covale ? ? G NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? A NAG 1535 A NAG 1536 1_555 ? ? ? ? ? ? ? 1.465 ? 
covale7  covale ? ? A ASN 70  ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 70   A NAG 1535 1_555 ? ? ? ? ? ? ? 1.468 ? 
covale8  covale ? ? K NAG .   O4  ? ? ? 1_555 L NAG .   C1 ? ? B NAG 1545 B NAG 1546 1_555 ? ? ? ? ? ? ? 1.469 ? 
covale9  covale ? ? O NAG .   O4  ? ? ? 1_555 P NAG .   C1 ? ? C NAG 1535 C NAG 1536 1_555 ? ? ? ? ? ? ? 1.470 ? 
covale10 covale ? ? A ASN 491 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 500  A NAG 1545 1_555 ? ? ? ? ? ? ? 1.473 ? 
covale11 covale ? ? D NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? A NAG 1545 A NAG 1546 1_555 ? ? ? ? ? ? ? 1.476 ? 
covale12 covale ? ? A ASN 27  ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 27   A NAG 1525 1_555 ? ? ? ? ? ? ? 1.493 ? 
covale13 covale ? ? C ASN 491 ND2 ? ? ? 1_555 M NAG .   C1 ? ? C ASN 500  C NAG 1545 1_555 ? ? ? ? ? ? ? 1.499 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 1535' 
AC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 1536' 
AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG C 1545' 
AC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 1546' 
AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG C 1535' 
AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 1536' 
AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1545' 
AC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1546' 
AC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1525' 
BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1535' 
BC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1536' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 1545' 
BC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 1546' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 3 LYS B 68  ? LYS B 68   . ? 1_555 ? 
2  AC1 3 ASN B 70  ? ASN B 70   . ? 1_555 ? 
3  AC1 3 NAG J .   ? NAG B 1536 . ? 1_555 ? 
4  AC2 1 NAG I .   ? NAG B 1535 . ? 1_555 ? 
5  AC3 3 ASN C 487 ? ASN C 496  . ? 1_555 ? 
6  AC3 3 ASN C 491 ? ASN C 500  . ? 1_555 ? 
7  AC3 3 NAG N .   ? NAG C 1546 . ? 1_555 ? 
8  AC4 1 NAG M .   ? NAG C 1545 . ? 1_555 ? 
9  AC5 3 LYS C 68  ? LYS C 68   . ? 1_555 ? 
10 AC5 3 ASN C 70  ? ASN C 70   . ? 1_555 ? 
11 AC5 3 NAG P .   ? NAG C 1536 . ? 1_555 ? 
12 AC6 1 NAG O .   ? NAG C 1535 . ? 1_555 ? 
13 AC7 3 ASN A 487 ? ASN A 496  . ? 1_555 ? 
14 AC7 3 ASN A 491 ? ASN A 500  . ? 1_555 ? 
15 AC7 3 NAG E .   ? NAG A 1546 . ? 1_555 ? 
16 AC8 1 NAG D .   ? NAG A 1545 . ? 1_555 ? 
17 AC9 1 ASN A 27  ? ASN A 27   . ? 1_555 ? 
18 BC1 2 ASN A 70  ? ASN A 70   . ? 1_555 ? 
19 BC1 2 NAG H .   ? NAG A 1536 . ? 1_555 ? 
20 BC2 1 NAG G .   ? NAG A 1535 . ? 1_555 ? 
21 BC3 4 SER B 484 ? SER B 493  . ? 1_555 ? 
22 BC3 4 ASN B 487 ? ASN B 496  . ? 1_555 ? 
23 BC3 4 ASN B 491 ? ASN B 500  . ? 1_555 ? 
24 BC3 4 NAG L .   ? NAG B 1546 . ? 1_555 ? 
25 BC4 1 NAG K .   ? NAG B 1545 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3RKI 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3RKI 
_atom_sites.fract_transf_matrix[1][1]   0.011373 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008837 
_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]   0.003212 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . GLN A 1 26  ? 16.074  32.019  -8.439  1.00 49.15  ? 26   GLN A N   1 
ATOM   2     C CA  . GLN A 1 26  ? 15.046  31.073  -8.953  1.00 48.61  ? 26   GLN A CA  1 
ATOM   3     C C   . GLN A 1 26  ? 14.035  31.878  -9.776  1.00 48.40  ? 26   GLN A C   1 
ATOM   4     O O   . GLN A 1 26  ? 13.683  32.986  -9.385  1.00 50.07  ? 26   GLN A O   1 
ATOM   5     C CB  . GLN A 1 26  ? 14.363  30.376  -7.776  1.00 47.61  ? 26   GLN A CB  1 
ATOM   6     C CG  . GLN A 1 26  ? 15.270  29.453  -6.980  1.00 51.61  ? 26   GLN A CG  1 
ATOM   7     C CD  . GLN A 1 26  ? 16.282  30.189  -6.055  1.00 60.25  ? 26   GLN A CD  1 
ATOM   8     O OE1 . GLN A 1 26  ? 16.983  31.123  -6.493  1.00 64.96  ? 26   GLN A OE1 1 
ATOM   9     N NE2 . GLN A 1 26  ? 16.373  29.751  -4.773  1.00 61.03  ? 26   GLN A NE2 1 
ATOM   10    N N   . ASN A 1 27  ? 13.569  31.353  -10.903 1.00 46.28  ? 27   ASN A N   1 
ATOM   11    C CA  . ASN A 1 27  ? 12.588  32.047  -11.728 1.00 45.50  ? 27   ASN A CA  1 
ATOM   12    C C   . ASN A 1 27  ? 11.595  31.021  -12.284 1.00 43.17  ? 27   ASN A C   1 
ATOM   13    O O   . ASN A 1 27  ? 11.617  30.696  -13.493 1.00 43.29  ? 27   ASN A O   1 
ATOM   14    C CB  . ASN A 1 27  ? 13.329  32.782  -12.866 1.00 47.70  ? 27   ASN A CB  1 
ATOM   15    C CG  . ASN A 1 27  ? 12.385  33.657  -13.748 1.00 51.72  ? 27   ASN A CG  1 
ATOM   16    O OD1 . ASN A 1 27  ? 11.756  34.612  -13.221 1.00 53.01  ? 27   ASN A OD1 1 
ATOM   17    N ND2 . ASN A 1 27  ? 12.292  33.321  -15.110 1.00 56.71  ? 27   ASN A ND2 1 
ATOM   18    N N   . ILE A 1 28  ? 10.748  30.464  -11.413 1.00 40.19  ? 28   ILE A N   1 
ATOM   19    C CA  . ILE A 1 28  ? 9.767   29.457  -11.886 1.00 37.56  ? 28   ILE A CA  1 
ATOM   20    C C   . ILE A 1 28  ? 8.517   30.134  -12.331 1.00 36.95  ? 28   ILE A C   1 
ATOM   21    O O   . ILE A 1 28  ? 8.117   31.117  -11.762 1.00 36.99  ? 28   ILE A O   1 
ATOM   22    C CB  . ILE A 1 28  ? 9.443   28.416  -10.882 1.00 36.06  ? 28   ILE A CB  1 
ATOM   23    C CG1 . ILE A 1 28  ? 9.541   29.038  -9.490  1.00 37.32  ? 28   ILE A CG1 1 
ATOM   24    C CG2 . ILE A 1 28  ? 10.423  27.309  -11.002 1.00 34.55  ? 28   ILE A CG2 1 
ATOM   25    C CD1 . ILE A 1 28  ? 8.193   29.696  -8.925  1.00 38.60  ? 28   ILE A CD1 1 
ATOM   26    N N   . THR A 1 29  ? 7.938   29.634  -13.402 1.00 36.16  ? 29   THR A N   1 
ATOM   27    C CA  . THR A 1 29  ? 6.771   30.245  -13.975 1.00 36.12  ? 29   THR A CA  1 
ATOM   28    C C   . THR A 1 29  ? 5.938   29.164  -14.565 1.00 35.64  ? 29   THR A C   1 
ATOM   29    O O   . THR A 1 29  ? 6.452   28.090  -14.870 1.00 35.17  ? 29   THR A O   1 
ATOM   30    C CB  . THR A 1 29  ? 7.112   31.113  -15.134 1.00 37.06  ? 29   THR A CB  1 
ATOM   31    O OG1 . THR A 1 29  ? 8.522   31.323  -15.162 1.00 37.24  ? 29   THR A OG1 1 
ATOM   32    C CG2 . THR A 1 29  ? 6.339   32.415  -15.017 1.00 38.11  ? 29   THR A CG2 1 
ATOM   33    N N   . GLU A 1 30  ? 4.654   29.446  -14.741 1.00 35.42  ? 30   GLU A N   1 
ATOM   34    C CA  . GLU A 1 30  ? 3.827   28.554  -15.488 1.00 35.22  ? 30   GLU A CA  1 
ATOM   35    C C   . GLU A 1 30  ? 3.235   29.392  -16.560 1.00 35.82  ? 30   GLU A C   1 
ATOM   36    O O   . GLU A 1 30  ? 2.925   30.556  -16.328 1.00 36.41  ? 30   GLU A O   1 
ATOM   37    C CB  . GLU A 1 30  ? 2.736   28.023  -14.612 1.00 35.34  ? 30   GLU A CB  1 
ATOM   38    C CG  . GLU A 1 30  ? 2.337   26.605  -14.901 1.00 36.47  ? 30   GLU A CG  1 
ATOM   39    C CD  . GLU A 1 30  ? 1.707   25.928  -13.688 1.00 38.38  ? 30   GLU A CD  1 
ATOM   40    O OE1 . GLU A 1 30  ? 0.786   26.506  -13.060 1.00 39.37  ? 30   GLU A OE1 1 
ATOM   41    O OE2 . GLU A 1 30  ? 2.149   24.810  -13.352 1.00 39.20  ? 30   GLU A OE2 1 
ATOM   42    N N   . GLU A 1 31  ? 3.122   28.814  -17.744 1.00 35.73  ? 31   GLU A N   1 
ATOM   43    C CA  . GLU A 1 31  ? 2.439   29.458  -18.831 1.00 36.69  ? 31   GLU A CA  1 
ATOM   44    C C   . GLU A 1 31  ? 1.403   28.498  -19.327 1.00 36.44  ? 31   GLU A C   1 
ATOM   45    O O   . GLU A 1 31  ? 1.704   27.335  -19.529 1.00 35.95  ? 31   GLU A O   1 
ATOM   46    C CB  . GLU A 1 31  ? 3.396   29.799  -19.949 1.00 37.36  ? 31   GLU A CB  1 
ATOM   47    C CG  . GLU A 1 31  ? 2.698   29.878  -21.295 1.00 40.44  ? 31   GLU A CG  1 
ATOM   48    C CD  . GLU A 1 31  ? 3.455   30.687  -22.328 1.00 44.33  ? 31   GLU A CD  1 
ATOM   49    O OE1 . GLU A 1 31  ? 2.846   31.006  -23.388 1.00 45.26  ? 31   GLU A OE1 1 
ATOM   50    O OE2 . GLU A 1 31  ? 4.655   30.999  -22.074 1.00 46.17  ? 31   GLU A OE2 1 
ATOM   51    N N   . PHE A 1 32  ? 0.185   29.003  -19.518 1.00 36.95  ? 32   PHE A N   1 
ATOM   52    C CA  . PHE A 1 32  ? -0.992  28.193  -19.839 1.00 37.02  ? 32   PHE A CA  1 
ATOM   53    C C   . PHE A 1 32  ? -1.310  28.281  -21.293 1.00 38.20  ? 32   PHE A C   1 
ATOM   54    O O   . PHE A 1 32  ? -1.285  29.371  -21.859 1.00 39.19  ? 32   PHE A O   1 
ATOM   55    C CB  . PHE A 1 32  ? -2.180  28.734  -19.074 1.00 37.37  ? 32   PHE A CB  1 
ATOM   56    C CG  . PHE A 1 32  ? -3.509  28.218  -19.532 1.00 37.82  ? 32   PHE A CG  1 
ATOM   57    C CD1 . PHE A 1 32  ? -3.844  26.879  -19.419 1.00 37.80  ? 32   PHE A CD1 1 
ATOM   58    C CD2 . PHE A 1 32  ? -4.451  29.093  -20.013 1.00 39.61  ? 32   PHE A CD2 1 
ATOM   59    C CE1 . PHE A 1 32  ? -5.083  26.418  -19.812 1.00 38.74  ? 32   PHE A CE1 1 
ATOM   60    C CE2 . PHE A 1 32  ? -5.682  28.639  -20.396 1.00 40.95  ? 32   PHE A CE2 1 
ATOM   61    C CZ  . PHE A 1 32  ? -5.997  27.293  -20.292 1.00 40.10  ? 32   PHE A CZ  1 
ATOM   62    N N   . TYR A 1 33  ? -1.639  27.147  -21.902 1.00 38.49  ? 33   TYR A N   1 
ATOM   63    C CA  . TYR A 1 33  ? -1.890  27.128  -23.331 1.00 39.47  ? 33   TYR A CA  1 
ATOM   64    C C   . TYR A 1 33  ? -3.315  26.780  -23.603 1.00 40.47  ? 33   TYR A C   1 
ATOM   65    O O   . TYR A 1 33  ? -3.655  25.608  -23.703 1.00 40.93  ? 33   TYR A O   1 
ATOM   66    C CB  . TYR A 1 33  ? -0.990  26.134  -23.995 1.00 39.09  ? 33   TYR A CB  1 
ATOM   67    C CG  . TYR A 1 33  ? 0.454   26.548  -23.954 1.00 39.64  ? 33   TYR A CG  1 
ATOM   68    C CD1 . TYR A 1 33  ? 1.340   25.982  -23.048 1.00 39.85  ? 33   TYR A CD1 1 
ATOM   69    C CD2 . TYR A 1 33  ? 0.945   27.493  -24.828 1.00 42.13  ? 33   TYR A CD2 1 
ATOM   70    C CE1 . TYR A 1 33  ? 2.676   26.336  -23.023 1.00 40.05  ? 33   TYR A CE1 1 
ATOM   71    C CE2 . TYR A 1 33  ? 2.278   27.856  -24.809 1.00 42.75  ? 33   TYR A CE2 1 
ATOM   72    C CZ  . TYR A 1 33  ? 3.135   27.274  -23.902 1.00 41.34  ? 33   TYR A CZ  1 
ATOM   73    O OH  . TYR A 1 33  ? 4.453   27.655  -23.878 1.00 41.94  ? 33   TYR A OH  1 
ATOM   74    N N   . GLN A 1 34  ? -4.138  27.816  -23.735 1.00 41.29  ? 34   GLN A N   1 
ATOM   75    C CA  . GLN A 1 34  ? -5.589  27.683  -23.830 1.00 42.22  ? 34   GLN A CA  1 
ATOM   76    C C   . GLN A 1 34  ? -6.012  26.802  -24.956 1.00 42.56  ? 34   GLN A C   1 
ATOM   77    O O   . GLN A 1 34  ? -7.029  26.172  -24.875 1.00 43.13  ? 34   GLN A O   1 
ATOM   78    C CB  . GLN A 1 34  ? -6.243  29.047  -24.004 1.00 43.52  ? 34   GLN A CB  1 
ATOM   79    C CG  . GLN A 1 34  ? -7.754  29.046  -23.929 1.00 45.83  ? 34   GLN A CG  1 
ATOM   80    C CD  . GLN A 1 34  ? -8.299  30.438  -23.709 1.00 48.96  ? 34   GLN A CD  1 
ATOM   81    O OE1 . GLN A 1 34  ? -8.306  31.262  -24.616 1.00 50.72  ? 34   GLN A OE1 1 
ATOM   82    N NE2 . GLN A 1 34  ? -8.756  30.711  -22.498 1.00 49.72  ? 34   GLN A NE2 1 
ATOM   83    N N   . SER A 1 35  ? -5.217  26.760  -26.010 1.00 42.55  ? 35   SER A N   1 
ATOM   84    C CA  . SER A 1 35  ? -5.589  26.036  -27.225 1.00 43.28  ? 35   SER A CA  1 
ATOM   85    C C   . SER A 1 35  ? -5.253  24.550  -27.149 1.00 42.51  ? 35   SER A C   1 
ATOM   86    O O   . SER A 1 35  ? -5.411  23.822  -28.124 1.00 43.11  ? 35   SER A O   1 
ATOM   87    C CB  . SER A 1 35  ? -4.910  26.673  -28.423 1.00 43.59  ? 35   SER A CB  1 
ATOM   88    O OG  . SER A 1 35  ? -3.556  26.868  -28.091 1.00 42.95  ? 35   SER A OG  1 
ATOM   89    N N   . THR A 1 36  ? -4.813  24.109  -25.978 1.00 41.05  ? 36   THR A N   1 
ATOM   90    C CA  . THR A 1 36  ? -4.393  22.739  -25.780 1.00 40.46  ? 36   THR A CA  1 
ATOM   91    C C   . THR A 1 36  ? -4.780  22.353  -24.391 1.00 39.52  ? 36   THR A C   1 
ATOM   92    O O   . THR A 1 36  ? -4.445  21.292  -23.900 1.00 38.93  ? 36   THR A O   1 
ATOM   93    C CB  . THR A 1 36  ? -2.893  22.629  -25.919 1.00 39.86  ? 36   THR A CB  1 
ATOM   94    O OG1 . THR A 1 36  ? -2.509  23.099  -27.223 1.00 42.08  ? 36   THR A OG1 1 
ATOM   95    C CG2 . THR A 1 36  ? -2.437  21.193  -25.739 1.00 39.65  ? 36   THR A CG2 1 
ATOM   96    N N   . CYS A 1 37  ? -5.522  23.236  -23.759 1.00 39.64  ? 37   CYS A N   1 
ATOM   97    C CA  . CYS A 1 37  ? -5.882  23.058  -22.377 1.00 39.38  ? 37   CYS A CA  1 
ATOM   98    C C   . CYS A 1 37  ? -4.768  22.365  -21.616 1.00 37.97  ? 37   CYS A C   1 
ATOM   99    O O   . CYS A 1 37  ? -4.968  21.305  -21.024 1.00 38.26  ? 37   CYS A O   1 
ATOM   100   C CB  . CYS A 1 37  ? -7.158  22.266  -22.259 1.00 40.54  ? 37   CYS A CB  1 
ATOM   101   S SG  . CYS A 1 37  ? -7.972  22.710  -20.774 1.00 42.40  ? 37   CYS A SG  1 
ATOM   102   N N   . SER A 1 38  ? -3.579  22.963  -21.663 1.00 36.75  ? 38   SER A N   1 
ATOM   103   C CA  . SER A 1 38  ? -2.421  22.423  -20.967 1.00 35.07  ? 38   SER A CA  1 
ATOM   104   C C   . SER A 1 38  ? -1.546  23.520  -20.393 1.00 33.58  ? 38   SER A C   1 
ATOM   105   O O   . SER A 1 38  ? -1.560  24.659  -20.850 1.00 33.63  ? 38   SER A O   1 
ATOM   106   C CB  . SER A 1 38  ? -1.624  21.500  -21.883 1.00 35.42  ? 38   SER A CB  1 
ATOM   107   O OG  . SER A 1 38  ? -1.383  22.099  -23.148 1.00 36.17  ? 38   SER A OG  1 
ATOM   108   N N   . ALA A 1 39  ? -0.807  23.166  -19.366 1.00 32.06  ? 39   ALA A N   1 
ATOM   109   C CA  . ALA A 1 39  ? -0.025  24.140  -18.701 1.00 31.32  ? 39   ALA A CA  1 
ATOM   110   C C   . ALA A 1 39  ? 1.387   23.617  -18.466 1.00 30.77  ? 39   ALA A C   1 
ATOM   111   O O   . ALA A 1 39  ? 1.578   22.441  -18.121 1.00 30.78  ? 39   ALA A O   1 
ATOM   112   C CB  . ALA A 1 39  ? -0.674  24.472  -17.423 1.00 31.05  ? 39   ALA A CB  1 
ATOM   113   N N   . VAL A 1 40  ? 2.377   24.493  -18.645 1.00 30.38  ? 40   VAL A N   1 
ATOM   114   C CA  . VAL A 1 40  ? 3.763   24.124  -18.399 1.00 29.65  ? 40   VAL A CA  1 
ATOM   115   C C   . VAL A 1 40  ? 4.460   24.977  -17.324 1.00 29.36  ? 40   VAL A C   1 
ATOM   116   O O   . VAL A 1 40  ? 4.360   26.214  -17.327 1.00 29.86  ? 40   VAL A O   1 
ATOM   117   C CB  . VAL A 1 40  ? 4.551   24.193  -19.657 1.00 29.69  ? 40   VAL A CB  1 
ATOM   118   C CG1 . VAL A 1 40  ? 5.975   23.979  -19.337 1.00 29.82  ? 40   VAL A CG1 1 
ATOM   119   C CG2 . VAL A 1 40  ? 4.092   23.136  -20.583 1.00 30.37  ? 40   VAL A CG2 1 
ATOM   120   N N   . SER A 1 41  ? 5.161   24.307  -16.414 1.00 28.70  ? 41   SER A N   1 
ATOM   121   C CA  . SER A 1 41  ? 5.936   24.980  -15.409 1.00 28.39  ? 41   SER A CA  1 
ATOM   122   C C   . SER A 1 41  ? 7.347   25.033  -15.918 1.00 28.59  ? 41   SER A C   1 
ATOM   123   O O   . SER A 1 41  ? 7.870   24.030  -16.349 1.00 28.51  ? 41   SER A O   1 
ATOM   124   C CB  . SER A 1 41  ? 5.886   24.191  -14.115 1.00 27.93  ? 41   SER A CB  1 
ATOM   125   O OG  . SER A 1 41  ? 4.582   23.683  -13.870 1.00 28.85  ? 41   SER A OG  1 
ATOM   126   N N   . LYS A 1 42  ? 7.960   26.206  -15.860 1.00 29.17  ? 42   LYS A N   1 
ATOM   127   C CA  . LYS A 1 42  ? 9.228   26.461  -16.531 1.00 30.23  ? 42   LYS A CA  1 
ATOM   128   C C   . LYS A 1 42  ? 10.274  27.082  -15.627 1.00 29.86  ? 42   LYS A C   1 
ATOM   129   O O   . LYS A 1 42  ? 9.956   27.762  -14.688 1.00 29.83  ? 42   LYS A O   1 
ATOM   130   C CB  . LYS A 1 42  ? 9.020   27.466  -17.649 1.00 31.64  ? 42   LYS A CB  1 
ATOM   131   C CG  . LYS A 1 42  ? 7.934   27.159  -18.652 1.00 33.85  ? 42   LYS A CG  1 
ATOM   132   C CD  . LYS A 1 42  ? 7.772   28.331  -19.644 1.00 38.19  ? 42   LYS A CD  1 
ATOM   133   C CE  . LYS A 1 42  ? 6.764   28.002  -20.762 1.00 40.06  ? 42   LYS A CE  1 
ATOM   134   N NZ  . LYS A 1 42  ? 6.948   28.823  -22.009 1.00 42.21  ? 42   LYS A NZ  1 
ATOM   135   N N   . GLY A 1 43  ? 11.538  26.903  -15.946 1.00 30.16  ? 43   GLY A N   1 
ATOM   136   C CA  . GLY A 1 43  ? 12.562  27.544  -15.144 1.00 30.01  ? 43   GLY A CA  1 
ATOM   137   C C   . GLY A 1 43  ? 13.331  26.644  -14.206 1.00 29.17  ? 43   GLY A C   1 
ATOM   138   O O   . GLY A 1 43  ? 14.016  27.112  -13.296 1.00 29.03  ? 43   GLY A O   1 
ATOM   139   N N   . TYR A 1 44  ? 13.239  25.348  -14.446 1.00 28.81  ? 44   TYR A N   1 
ATOM   140   C CA  . TYR A 1 44  ? 13.877  24.376  -13.595 1.00 28.04  ? 44   TYR A CA  1 
ATOM   141   C C   . TYR A 1 44  ? 15.193  23.958  -14.174 1.00 28.80  ? 44   TYR A C   1 
ATOM   142   O O   . TYR A 1 44  ? 15.381  24.057  -15.401 1.00 30.11  ? 44   TYR A O   1 
ATOM   143   C CB  . TYR A 1 44  ? 13.002  23.157  -13.489 1.00 27.44  ? 44   TYR A CB  1 
ATOM   144   C CG  . TYR A 1 44  ? 11.741  23.424  -12.736 1.00 26.73  ? 44   TYR A CG  1 
ATOM   145   C CD1 . TYR A 1 44  ? 10.545  23.563  -13.395 1.00 27.49  ? 44   TYR A CD1 1 
ATOM   146   C CD2 . TYR A 1 44  ? 11.746  23.542  -11.371 1.00 25.55  ? 44   TYR A CD2 1 
ATOM   147   C CE1 . TYR A 1 44  ? 9.391   23.795  -12.725 1.00 27.36  ? 44   TYR A CE1 1 
ATOM   148   C CE2 . TYR A 1 44  ? 10.603  23.771  -10.688 1.00 25.75  ? 44   TYR A CE2 1 
ATOM   149   C CZ  . TYR A 1 44  ? 9.415   23.902  -11.375 1.00 26.97  ? 44   TYR A CZ  1 
ATOM   150   O OH  . TYR A 1 44  ? 8.224   24.131  -10.705 1.00 28.06  ? 44   TYR A OH  1 
ATOM   151   N N   . LEU A 1 45  ? 16.087  23.477  -13.304 1.00 27.97  ? 45   LEU A N   1 
ATOM   152   C CA  . LEU A 1 45  ? 17.414  23.052  -13.722 1.00 28.17  ? 45   LEU A CA  1 
ATOM   153   C C   . LEU A 1 45  ? 17.742  21.597  -13.418 1.00 27.86  ? 45   LEU A C   1 
ATOM   154   O O   . LEU A 1 45  ? 17.830  21.167  -12.272 1.00 27.25  ? 45   LEU A O   1 
ATOM   155   C CB  . LEU A 1 45  ? 18.471  23.979  -13.152 1.00 28.46  ? 45   LEU A CB  1 
ATOM   156   C CG  . LEU A 1 45  ? 18.346  25.410  -13.635 1.00 28.66  ? 45   LEU A CG  1 
ATOM   157   C CD1 . LEU A 1 45  ? 19.110  26.347  -12.744 1.00 29.22  ? 45   LEU A CD1 1 
ATOM   158   C CD2 . LEU A 1 45  ? 18.851  25.485  -15.017 1.00 30.18  ? 45   LEU A CD2 1 
ATOM   159   N N   . SER A 1 46  ? 17.968  20.862  -14.490 1.00 28.12  ? 46   SER A N   1 
ATOM   160   C CA  . SER A 1 46  ? 18.212  19.448  -14.451 1.00 28.02  ? 46   SER A CA  1 
ATOM   161   C C   . SER A 1 46  ? 19.384  18.986  -13.648 1.00 28.45  ? 46   SER A C   1 
ATOM   162   O O   . SER A 1 46  ? 20.350  19.692  -13.398 1.00 28.98  ? 46   SER A O   1 
ATOM   163   C CB  . SER A 1 46  ? 18.524  19.003  -15.841 1.00 28.90  ? 46   SER A CB  1 
ATOM   164   O OG  . SER A 1 46  ? 19.697  19.637  -16.212 1.00 29.53  ? 46   SER A OG  1 
ATOM   165   N N   . ALA A 1 47  ? 19.296  17.722  -13.320 1.00 28.38  ? 47   ALA A N   1 
ATOM   166   C CA  . ALA A 1 47  ? 20.386  16.974  -12.781 1.00 28.62  ? 47   ALA A CA  1 
ATOM   167   C C   . ALA A 1 47  ? 19.930  15.551  -13.046 1.00 28.63  ? 47   ALA A C   1 
ATOM   168   O O   . ALA A 1 47  ? 18.905  15.155  -12.534 1.00 28.38  ? 47   ALA A O   1 
ATOM   169   C CB  . ALA A 1 47  ? 20.475  17.249  -11.320 1.00 27.78  ? 47   ALA A CB  1 
ATOM   170   N N   . LEU A 1 48  ? 20.630  14.790  -13.873 1.00 29.18  ? 48   LEU A N   1 
ATOM   171   C CA  . LEU A 1 48  ? 20.076  13.527  -14.328 1.00 29.07  ? 48   LEU A CA  1 
ATOM   172   C C   . LEU A 1 48  ? 20.984  12.365  -14.054 1.00 30.17  ? 48   LEU A C   1 
ATOM   173   O O   . LEU A 1 48  ? 22.057  12.302  -14.604 1.00 31.55  ? 48   LEU A O   1 
ATOM   174   C CB  . LEU A 1 48  ? 19.796  13.571  -15.824 1.00 29.64  ? 48   LEU A CB  1 
ATOM   175   C CG  . LEU A 1 48  ? 19.359  14.850  -16.501 1.00 28.04  ? 48   LEU A CG  1 
ATOM   176   C CD1 . LEU A 1 48  ? 18.924  14.435  -17.799 1.00 27.98  ? 48   LEU A CD1 1 
ATOM   177   C CD2 . LEU A 1 48  ? 18.236  15.456  -15.827 1.00 27.87  ? 48   LEU A CD2 1 
ATOM   178   N N   . ARG A 1 49  ? 20.538  11.420  -13.238 1.00 29.95  ? 49   ARG A N   1 
ATOM   179   C CA  . ARG A 1 49  ? 21.332  10.231  -12.902 1.00 31.28  ? 49   ARG A CA  1 
ATOM   180   C C   . ARG A 1 49  ? 21.732  9.472   -14.145 1.00 33.41  ? 49   ARG A C   1 
ATOM   181   O O   . ARG A 1 49  ? 20.917  9.204   -15.005 1.00 33.90  ? 49   ARG A O   1 
ATOM   182   C CB  . ARG A 1 49  ? 20.555  9.277   -12.012 1.00 30.72  ? 49   ARG A CB  1 
ATOM   183   C CG  . ARG A 1 49  ? 21.365  8.669   -10.942 1.00 30.15  ? 49   ARG A CG  1 
ATOM   184   C CD  . ARG A 1 49  ? 20.844  7.346   -10.616 1.00 30.27  ? 49   ARG A CD  1 
ATOM   185   N NE  . ARG A 1 49  ? 21.538  6.422   -11.450 1.00 36.36  ? 49   ARG A NE  1 
ATOM   186   C CZ  . ARG A 1 49  ? 20.962  5.594   -12.307 1.00 40.75  ? 49   ARG A CZ  1 
ATOM   187   N NH1 . ARG A 1 49  ? 19.642  5.559   -12.398 1.00 39.80  ? 49   ARG A NH1 1 
ATOM   188   N NH2 . ARG A 1 49  ? 21.724  4.774   -13.065 1.00 44.66  ? 49   ARG A NH2 1 
ATOM   189   N N   . THR A 1 50  ? 22.999  9.120   -14.255 1.00 34.91  ? 50   THR A N   1 
ATOM   190   C CA  . THR A 1 50  ? 23.389  8.229   -15.324 1.00 36.95  ? 50   THR A CA  1 
ATOM   191   C C   . THR A 1 50  ? 24.263  7.149   -14.776 1.00 38.76  ? 50   THR A C   1 
ATOM   192   O O   . THR A 1 50  ? 24.751  6.310   -15.520 1.00 40.97  ? 50   THR A O   1 
ATOM   193   C CB  . THR A 1 50  ? 24.118  8.942   -16.455 1.00 37.42  ? 50   THR A CB  1 
ATOM   194   O OG1 . THR A 1 50  ? 24.892  10.008  -15.929 1.00 36.35  ? 50   THR A OG1 1 
ATOM   195   C CG2 . THR A 1 50  ? 23.142  9.539   -17.365 1.00 37.18  ? 50   THR A CG2 1 
ATOM   196   N N   . GLY A 1 51  ? 24.454  7.154   -13.466 1.00 38.09  ? 51   GLY A N   1 
ATOM   197   C CA  . GLY A 1 51  ? 25.412  6.235   -12.897 1.00 40.07  ? 51   GLY A CA  1 
ATOM   198   C C   . GLY A 1 51  ? 25.387  6.200   -11.401 1.00 39.05  ? 51   GLY A C   1 
ATOM   199   O O   . GLY A 1 51  ? 24.625  6.904   -10.769 1.00 37.13  ? 51   GLY A O   1 
ATOM   200   N N   . TRP A 1 52  ? 26.247  5.360   -10.850 1.00 40.73  ? 52   TRP A N   1 
ATOM   201   C CA  . TRP A 1 52  ? 26.296  5.138   -9.424  1.00 40.09  ? 52   TRP A CA  1 
ATOM   202   C C   . TRP A 1 52  ? 27.736  5.187   -8.932  1.00 41.02  ? 52   TRP A C   1 
ATOM   203   O O   . TRP A 1 52  ? 28.661  4.736   -9.607  1.00 43.01  ? 52   TRP A O   1 
ATOM   204   C CB  . TRP A 1 52  ? 25.727  3.760   -9.066  1.00 41.18  ? 52   TRP A CB  1 
ATOM   205   C CG  . TRP A 1 52  ? 24.356  3.557   -9.406  1.00 41.12  ? 52   TRP A CG  1 
ATOM   206   C CD1 . TRP A 1 52  ? 23.871  2.785   -10.406 1.00 43.92  ? 52   TRP A CD1 1 
ATOM   207   C CD2 . TRP A 1 52  ? 23.249  4.115   -8.752  1.00 39.80  ? 52   TRP A CD2 1 
ATOM   208   N NE1 . TRP A 1 52  ? 22.509  2.833   -10.432 1.00 42.82  ? 52   TRP A NE1 1 
ATOM   209   C CE2 . TRP A 1 52  ? 22.094  3.648   -9.415  1.00 40.34  ? 52   TRP A CE2 1 
ATOM   210   C CE3 . TRP A 1 52  ? 23.105  4.970   -7.668  1.00 37.89  ? 52   TRP A CE3 1 
ATOM   211   C CZ2 . TRP A 1 52  ? 20.826  4.016   -9.037  1.00 38.21  ? 52   TRP A CZ2 1 
ATOM   212   C CZ3 . TRP A 1 52  ? 21.850  5.324   -7.293  1.00 36.19  ? 52   TRP A CZ3 1 
ATOM   213   C CH2 . TRP A 1 52  ? 20.725  4.850   -7.973  1.00 36.57  ? 52   TRP A CH2 1 
ATOM   214   N N   . TYR A 1 53  ? 27.893  5.680   -7.719  1.00 39.75  ? 53   TYR A N   1 
ATOM   215   C CA  . TYR A 1 53  ? 29.149  5.700   -7.043  1.00 40.98  ? 53   TYR A CA  1 
ATOM   216   C C   . TYR A 1 53  ? 29.101  4.801   -5.797  1.00 41.36  ? 53   TYR A C   1 
ATOM   217   O O   . TYR A 1 53  ? 28.336  5.021   -4.895  1.00 40.26  ? 53   TYR A O   1 
ATOM   218   C CB  . TYR A 1 53  ? 29.419  7.143   -6.712  1.00 39.49  ? 53   TYR A CB  1 
ATOM   219   C CG  . TYR A 1 53  ? 30.652  7.398   -5.933  1.00 40.84  ? 53   TYR A CG  1 
ATOM   220   C CD1 . TYR A 1 53  ? 31.844  7.687   -6.560  1.00 43.80  ? 53   TYR A CD1 1 
ATOM   221   C CD2 . TYR A 1 53  ? 30.633  7.385   -4.563  1.00 40.70  ? 53   TYR A CD2 1 
ATOM   222   C CE1 . TYR A 1 53  ? 32.992  7.938   -5.832  1.00 45.51  ? 53   TYR A CE1 1 
ATOM   223   C CE2 . TYR A 1 53  ? 31.776  7.642   -3.823  1.00 42.27  ? 53   TYR A CE2 1 
ATOM   224   C CZ  . TYR A 1 53  ? 32.945  7.920   -4.460  1.00 44.36  ? 53   TYR A CZ  1 
ATOM   225   O OH  . TYR A 1 53  ? 34.050  8.166   -3.701  1.00 45.41  ? 53   TYR A OH  1 
ATOM   226   N N   . THR A 1 54  ? 29.895  3.758   -5.778  1.00 43.72  ? 54   THR A N   1 
ATOM   227   C CA  . THR A 1 54  ? 29.919  2.801   -4.703  1.00 44.79  ? 54   THR A CA  1 
ATOM   228   C C   . THR A 1 54  ? 30.737  3.399   -3.607  1.00 44.26  ? 54   THR A C   1 
ATOM   229   O O   . THR A 1 54  ? 31.579  4.219   -3.886  1.00 44.78  ? 54   THR A O   1 
ATOM   230   C CB  . THR A 1 54  ? 30.669  1.596   -5.243  1.00 48.12  ? 54   THR A CB  1 
ATOM   231   O OG1 . THR A 1 54  ? 29.745  0.729   -5.882  1.00 49.87  ? 54   THR A OG1 1 
ATOM   232   C CG2 . THR A 1 54  ? 31.500  0.802   -4.175  1.00 50.63  ? 54   THR A CG2 1 
ATOM   233   N N   . SER A 1 55  ? 30.489  3.011   -2.361  1.00 43.84  ? 55   SER A N   1 
ATOM   234   C CA  . SER A 1 55  ? 31.497  3.149   -1.282  1.00 44.45  ? 55   SER A CA  1 
ATOM   235   C C   . SER A 1 55  ? 31.258  2.260   -0.084  1.00 44.89  ? 55   SER A C   1 
ATOM   236   O O   . SER A 1 55  ? 30.133  2.052   0.344   1.00 43.99  ? 55   SER A O   1 
ATOM   237   C CB  . SER A 1 55  ? 31.698  4.567   -0.777  1.00 42.62  ? 55   SER A CB  1 
ATOM   238   O OG  . SER A 1 55  ? 32.493  4.523   0.407   1.00 42.82  ? 55   SER A OG  1 
ATOM   239   N N   . VAL A 1 56  ? 32.352  1.785   0.483   1.00 46.67  ? 56   VAL A N   1 
ATOM   240   C CA  . VAL A 1 56  ? 32.307  0.639   1.347   1.00 47.81  ? 56   VAL A CA  1 
ATOM   241   C C   . VAL A 1 56  ? 32.628  1.046   2.743   1.00 46.67  ? 56   VAL A C   1 
ATOM   242   O O   . VAL A 1 56  ? 33.781  1.291   3.082   1.00 47.92  ? 56   VAL A O   1 
ATOM   243   C CB  . VAL A 1 56  ? 33.342  -0.387  0.939   1.00 50.96  ? 56   VAL A CB  1 
ATOM   244   C CG1 . VAL A 1 56  ? 32.962  -1.730  1.523   1.00 52.09  ? 56   VAL A CG1 1 
ATOM   245   C CG2 . VAL A 1 56  ? 33.503  -0.424  -0.611  1.00 53.05  ? 56   VAL A CG2 1 
ATOM   246   N N   . ILE A 1 57  ? 31.604  1.085   3.568   1.00 44.70  ? 57   ILE A N   1 
ATOM   247   C CA  . ILE A 1 57  ? 31.750  1.551   4.918   1.00 43.13  ? 57   ILE A CA  1 
ATOM   248   C C   . ILE A 1 57  ? 31.818  0.412   5.903   1.00 44.16  ? 57   ILE A C   1 
ATOM   249   O O   . ILE A 1 57  ? 31.019  -0.520  5.865   1.00 44.49  ? 57   ILE A O   1 
ATOM   250   C CB  . ILE A 1 57  ? 30.637  2.478   5.231   1.00 40.35  ? 57   ILE A CB  1 
ATOM   251   C CG1 . ILE A 1 57  ? 30.752  3.657   4.294   1.00 39.89  ? 57   ILE A CG1 1 
ATOM   252   C CG2 . ILE A 1 57  ? 30.739  2.950   6.630   1.00 39.23  ? 57   ILE A CG2 1 
ATOM   253   C CD1 . ILE A 1 57  ? 29.483  4.358   4.142   1.00 39.58  ? 57   ILE A CD1 1 
ATOM   254   N N   . THR A 1 58  ? 32.808  0.487   6.776   1.00 44.87  ? 58   THR A N   1 
ATOM   255   C CA  . THR A 1 58  ? 33.121  -0.617  7.668   1.00 46.64  ? 58   THR A CA  1 
ATOM   256   C C   . THR A 1 58  ? 33.138  -0.102  9.090   1.00 45.49  ? 58   THR A C   1 
ATOM   257   O O   . THR A 1 58  ? 33.737  0.939   9.374   1.00 44.89  ? 58   THR A O   1 
ATOM   258   C CB  . THR A 1 58  ? 34.500  -1.227  7.364   1.00 49.06  ? 58   THR A CB  1 
ATOM   259   O OG1 . THR A 1 58  ? 34.871  -0.970  6.006   1.00 50.66  ? 58   THR A OG1 1 
ATOM   260   C CG2 . THR A 1 58  ? 34.468  -2.701  7.584   1.00 50.97  ? 58   THR A CG2 1 
ATOM   261   N N   . ILE A 1 59  ? 32.477  -0.828  9.985   1.00 45.88  ? 59   ILE A N   1 
ATOM   262   C CA  . ILE A 1 59  ? 32.295  -0.361  11.353  1.00 44.86  ? 59   ILE A CA  1 
ATOM   263   C C   . ILE A 1 59  ? 32.601  -1.410  12.414  1.00 47.02  ? 59   ILE A C   1 
ATOM   264   O O   . ILE A 1 59  ? 31.982  -2.473  12.489  1.00 47.88  ? 59   ILE A O   1 
ATOM   265   C CB  . ILE A 1 59  ? 30.910  0.215   11.572  1.00 42.15  ? 59   ILE A CB  1 
ATOM   266   C CG1 . ILE A 1 59  ? 30.740  1.457   10.727  1.00 40.65  ? 59   ILE A CG1 1 
ATOM   267   C CG2 . ILE A 1 59  ? 30.743  0.637   12.986  1.00 40.39  ? 59   ILE A CG2 1 
ATOM   268   C CD1 . ILE A 1 59  ? 29.477  2.201   11.030  1.00 39.85  ? 59   ILE A CD1 1 
ATOM   269   N N   . GLU A 1 60  ? 33.580  -1.069  13.234  1.00 48.29  ? 60   GLU A N   1 
ATOM   270   C CA  . GLU A 1 60  ? 34.000  -1.874  14.342  1.00 50.69  ? 60   GLU A CA  1 
ATOM   271   C C   . GLU A 1 60  ? 33.010  -1.708  15.474  1.00 49.17  ? 60   GLU A C   1 
ATOM   272   O O   . GLU A 1 60  ? 32.616  -0.599  15.795  1.00 47.50  ? 60   GLU A O   1 
ATOM   273   C CB  . GLU A 1 60  ? 35.377  -1.409  14.816  1.00 51.74  ? 60   GLU A CB  1 
ATOM   274   C CG  . GLU A 1 60  ? 36.562  -1.829  13.933  1.00 57.20  ? 60   GLU A CG  1 
ATOM   275   C CD  . GLU A 1 60  ? 37.893  -1.905  14.708  1.00 63.33  ? 60   GLU A CD  1 
ATOM   276   O OE1 . GLU A 1 60  ? 38.069  -1.151  15.678  1.00 64.10  ? 60   GLU A OE1 1 
ATOM   277   O OE2 . GLU A 1 60  ? 38.779  -2.721  14.362  1.00 67.51  ? 60   GLU A OE2 1 
ATOM   278   N N   . LEU A 1 61  ? 32.612  -2.816  16.081  1.00 50.46  ? 61   LEU A N   1 
ATOM   279   C CA  . LEU A 1 61  ? 31.837  -2.797  17.319  1.00 49.34  ? 61   LEU A CA  1 
ATOM   280   C C   . LEU A 1 61  ? 32.752  -2.429  18.447  1.00 49.71  ? 61   LEU A C   1 
ATOM   281   O O   . LEU A 1 61  ? 33.926  -2.731  18.391  1.00 51.43  ? 61   LEU A O   1 
ATOM   282   C CB  . LEU A 1 61  ? 31.310  -4.195  17.604  1.00 50.82  ? 61   LEU A CB  1 
ATOM   283   C CG  . LEU A 1 61  ? 30.868  -4.537  19.029  1.00 50.00  ? 61   LEU A CG  1 
ATOM   284   C CD1 . LEU A 1 61  ? 29.464  -4.088  19.225  1.00 48.40  ? 61   LEU A CD1 1 
ATOM   285   C CD2 . LEU A 1 61  ? 30.929  -6.022  19.257  1.00 52.23  ? 61   LEU A CD2 1 
ATOM   286   N N   . SER A 1 62  ? 32.230  -1.803  19.486  1.00 48.69  ? 62   SER A N   1 
ATOM   287   C CA  . SER A 1 62  ? 33.050  -1.583  20.669  1.00 50.00  ? 62   SER A CA  1 
ATOM   288   C C   . SER A 1 62  ? 32.725  -2.629  21.698  1.00 51.76  ? 62   SER A C   1 
ATOM   289   O O   . SER A 1 62  ? 31.705  -2.540  22.362  1.00 50.65  ? 62   SER A O   1 
ATOM   290   C CB  . SER A 1 62  ? 32.830  -0.199  21.242  1.00 47.47  ? 62   SER A CB  1 
ATOM   291   O OG  . SER A 1 62  ? 33.383  0.746   20.370  1.00 47.53  ? 62   SER A OG  1 
ATOM   292   N N   . ASN A 1 63  ? 33.580  -3.631  21.834  1.00 55.36  ? 63   ASN A N   1 
ATOM   293   C CA  . ASN A 1 63  ? 33.133  -4.812  22.523  1.00 57.68  ? 63   ASN A CA  1 
ATOM   294   C C   . ASN A 1 63  ? 33.287  -4.704  24.008  1.00 58.06  ? 63   ASN A C   1 
ATOM   295   O O   . ASN A 1 63  ? 34.182  -4.025  24.480  1.00 58.24  ? 63   ASN A O   1 
ATOM   296   C CB  . ASN A 1 63  ? 33.835  -6.047  21.994  1.00 60.60  ? 63   ASN A CB  1 
ATOM   297   C CG  . ASN A 1 63  ? 32.923  -7.263  22.002  1.00 62.55  ? 63   ASN A CG  1 
ATOM   298   O OD1 . ASN A 1 63  ? 32.100  -7.449  22.919  1.00 61.77  ? 63   ASN A OD1 1 
ATOM   299   N ND2 . ASN A 1 63  ? 33.047  -8.091  20.967  1.00 64.93  ? 63   ASN A ND2 1 
ATOM   300   N N   . ILE A 1 64  ? 32.409  -5.361  24.748  1.00 59.20  ? 64   ILE A N   1 
ATOM   301   C CA  . ILE A 1 64  ? 32.569  -5.420  26.189  1.00 60.74  ? 64   ILE A CA  1 
ATOM   302   C C   . ILE A 1 64  ? 33.356  -6.643  26.601  1.00 65.14  ? 64   ILE A C   1 
ATOM   303   O O   . ILE A 1 64  ? 33.040  -7.756  26.159  1.00 67.44  ? 64   ILE A O   1 
ATOM   304   C CB  . ILE A 1 64  ? 31.238  -5.586  26.887  1.00 59.13  ? 64   ILE A CB  1 
ATOM   305   C CG1 . ILE A 1 64  ? 30.240  -4.570  26.373  1.00 56.35  ? 64   ILE A CG1 1 
ATOM   306   C CG2 . ILE A 1 64  ? 31.424  -5.479  28.404  1.00 59.15  ? 64   ILE A CG2 1 
ATOM   307   C CD1 . ILE A 1 64  ? 28.881  -4.702  27.019  1.00 55.00  ? 64   ILE A CD1 1 
ATOM   308   N N   . LYS A 1 65  ? 34.351  -6.459  27.466  1.00 67.63  ? 65   LYS A N   1 
ATOM   309   C CA  . LYS A 1 65  ? 34.882  -7.607  28.260  1.00 71.97  ? 65   LYS A CA  1 
ATOM   310   C C   . LYS A 1 65  ? 34.235  -7.699  29.695  1.00 72.08  ? 65   LYS A C   1 
ATOM   311   O O   . LYS A 1 65  ? 34.554  -6.910  30.639  1.00 70.72  ? 65   LYS A O   1 
ATOM   312   C CB  . LYS A 1 65  ? 36.437  -7.724  28.237  1.00 73.84  ? 65   LYS A CB  1 
ATOM   313   C CG  . LYS A 1 65  ? 37.202  -6.384  28.113  1.00 73.82  ? 65   LYS A CG  1 
ATOM   314   C CD  . LYS A 1 65  ? 36.658  -5.326  29.116  1.00 73.11  ? 65   LYS A CD  1 
ATOM   315   C CE  . LYS A 1 65  ? 37.655  -4.223  29.442  1.00 72.97  ? 65   LYS A CE  1 
ATOM   316   N NZ  . LYS A 1 65  ? 37.357  -3.664  30.800  1.00 71.11  ? 65   LYS A NZ  1 
ATOM   317   N N   . GLU A 1 66  ? 33.305  -8.668  29.795  1.00 73.93  ? 66   GLU A N   1 
ATOM   318   C CA  . GLU A 1 66  ? 32.365  -8.861  30.923  1.00 74.17  ? 66   GLU A CA  1 
ATOM   319   C C   . GLU A 1 66  ? 33.033  -9.320  32.231  1.00 75.74  ? 66   GLU A C   1 
ATOM   320   O O   . GLU A 1 66  ? 33.861  -10.264 32.237  1.00 78.40  ? 66   GLU A O   1 
ATOM   321   C CB  . GLU A 1 66  ? 31.274  -9.847  30.488  1.00 75.07  ? 66   GLU A CB  1 
ATOM   322   C CG  . GLU A 1 66  ? 30.547  -10.601 31.597  1.00 77.43  ? 66   GLU A CG  1 
ATOM   323   C CD  . GLU A 1 66  ? 29.803  -11.823 31.051  1.00 82.84  ? 66   GLU A CD  1 
ATOM   324   O OE1 . GLU A 1 66  ? 28.986  -12.405 31.809  1.00 85.45  ? 66   GLU A OE1 1 
ATOM   325   O OE2 . GLU A 1 66  ? 30.032  -12.195 29.865  1.00 84.15  ? 66   GLU A OE2 1 
ATOM   326   N N   . ASN A 1 67  ? 32.682  -8.664  33.340  1.00 74.52  ? 67   ASN A N   1 
ATOM   327   C CA  . ASN A 1 67  ? 33.423  -8.932  34.581  1.00 75.65  ? 67   ASN A CA  1 
ATOM   328   C C   . ASN A 1 67  ? 32.710  -9.681  35.663  1.00 76.10  ? 67   ASN A C   1 
ATOM   329   O O   . ASN A 1 67  ? 32.315  -9.133  36.709  1.00 74.71  ? 67   ASN A O   1 
ATOM   330   C CB  . ASN A 1 67  ? 34.233  -7.731  35.100  1.00 74.40  ? 67   ASN A CB  1 
ATOM   331   C CG  . ASN A 1 67  ? 35.672  -7.738  34.563  1.00 76.00  ? 67   ASN A CG  1 
ATOM   332   O OD1 . ASN A 1 67  ? 36.489  -8.613  34.926  1.00 77.99  ? 67   ASN A OD1 1 
ATOM   333   N ND2 . ASN A 1 67  ? 35.974  -6.788  33.660  1.00 74.34  ? 67   ASN A ND2 1 
ATOM   334   N N   . LYS A 1 68  ? 32.559  -10.959 35.331  1.00 78.20  ? 68   LYS A N   1 
ATOM   335   C CA  . LYS A 1 68  ? 32.323  -12.047 36.264  1.00 79.96  ? 68   LYS A CA  1 
ATOM   336   C C   . LYS A 1 68  ? 32.643  -11.640 37.722  1.00 79.06  ? 68   LYS A C   1 
ATOM   337   O O   . LYS A 1 68  ? 33.753  -11.817 38.237  1.00 80.28  ? 68   LYS A O   1 
ATOM   338   C CB  . LYS A 1 68  ? 33.142  -13.277 35.838  1.00 83.39  ? 68   LYS A CB  1 
ATOM   339   C CG  . LYS A 1 68  ? 33.334  -13.470 34.312  1.00 84.37  ? 68   LYS A CG  1 
ATOM   340   C CD  . LYS A 1 68  ? 34.759  -13.966 34.009  1.00 87.19  ? 68   LYS A CD  1 
ATOM   341   C CE  . LYS A 1 68  ? 35.430  -14.621 35.254  1.00 88.67  ? 68   LYS A CE  1 
ATOM   342   N NZ  . LYS A 1 68  ? 36.757  -15.235 34.964  1.00 91.58  ? 68   LYS A NZ  1 
ATOM   343   N N   . CYS A 1 69  ? 31.647  -11.036 38.348  1.00 76.61  ? 69   CYS A N   1 
ATOM   344   C CA  . CYS A 1 69  ? 31.630  -10.795 39.755  1.00 75.68  ? 69   CYS A CA  1 
ATOM   345   C C   . CYS A 1 69  ? 30.311  -11.509 40.169  1.00 76.56  ? 69   CYS A C   1 
ATOM   346   O O   . CYS A 1 69  ? 29.739  -12.302 39.398  1.00 77.61  ? 69   CYS A O   1 
ATOM   347   C CB  . CYS A 1 69  ? 31.501  -9.299  39.968  1.00 72.15  ? 69   CYS A CB  1 
ATOM   348   S SG  . CYS A 1 69  ? 29.738  -8.932  39.852  1.00 69.92  ? 69   CYS A SG  1 
ATOM   349   N N   . ASN A 1 70  ? 29.818  -11.205 41.370  1.00 76.30  ? 70   ASN A N   1 
ATOM   350   C CA  . ASN A 1 70  ? 28.442  -11.531 41.775  1.00 77.00  ? 70   ASN A CA  1 
ATOM   351   C C   . ASN A 1 70  ? 27.714  -10.207 42.069  1.00 72.22  ? 70   ASN A C   1 
ATOM   352   O O   . ASN A 1 70  ? 28.149  -9.424  42.922  1.00 70.73  ? 70   ASN A O   1 
ATOM   353   C CB  . ASN A 1 70  ? 28.493  -12.470 42.976  1.00 80.64  ? 70   ASN A CB  1 
ATOM   354   C CG  . ASN A 1 70  ? 29.710  -13.365 42.913  1.00 91.86  ? 70   ASN A CG  1 
ATOM   355   O OD1 . ASN A 1 70  ? 29.959  -13.955 41.863  1.00 97.39  ? 70   ASN A OD1 1 
ATOM   356   N ND2 . ASN A 1 70  ? 30.495  -13.452 44.004  1.00 106.32 ? 70   ASN A ND2 1 
ATOM   357   N N   . GLY A 1 71  ? 26.662  -9.919  41.300  1.00 69.49  ? 71   GLY A N   1 
ATOM   358   C CA  . GLY A 1 71  ? 25.845  -8.713  41.513  1.00 64.95  ? 71   GLY A CA  1 
ATOM   359   C C   . GLY A 1 71  ? 24.727  -8.987  42.511  1.00 63.83  ? 71   GLY A C   1 
ATOM   360   O O   . GLY A 1 71  ? 24.597  -10.108 43.023  1.00 65.84  ? 71   GLY A O   1 
ATOM   361   N N   . THR A 1 72  ? 23.925  -7.974  42.811  1.00 60.67  ? 72   THR A N   1 
ATOM   362   C CA  . THR A 1 72  ? 22.748  -8.157  43.659  1.00 60.01  ? 72   THR A CA  1 
ATOM   363   C C   . THR A 1 72  ? 21.691  -8.959  42.884  1.00 61.21  ? 72   THR A C   1 
ATOM   364   O O   . THR A 1 72  ? 21.223  -8.502  41.843  1.00 60.68  ? 72   THR A O   1 
ATOM   365   C CB  . THR A 1 72  ? 22.191  -6.789  44.103  1.00 57.67  ? 72   THR A CB  1 
ATOM   366   O OG1 . THR A 1 72  ? 21.402  -6.193  43.058  1.00 55.00  ? 72   THR A OG1 1 
ATOM   367   C CG2 . THR A 1 72  ? 23.343  -5.853  44.455  1.00 56.48  ? 72   THR A CG2 1 
ATOM   368   N N   . ASP A 1 73  ? 21.319  -10.145 43.369  1.00 63.09  ? 73   ASP A N   1 
ATOM   369   C CA  . ASP A 1 73  ? 20.606  -11.147 42.524  1.00 64.68  ? 73   ASP A CA  1 
ATOM   370   C C   . ASP A 1 73  ? 21.436  -11.585 41.290  1.00 64.94  ? 73   ASP A C   1 
ATOM   371   O O   . ASP A 1 73  ? 21.670  -10.780 40.360  1.00 62.95  ? 73   ASP A O   1 
ATOM   372   C CB  . ASP A 1 73  ? 19.180  -10.688 42.094  1.00 63.87  ? 73   ASP A CB  1 
ATOM   373   C CG  . ASP A 1 73  ? 18.417  -11.766 41.255  1.00 66.73  ? 73   ASP A CG  1 
ATOM   374   O OD1 . ASP A 1 73  ? 19.053  -12.714 40.717  1.00 68.84  ? 73   ASP A OD1 1 
ATOM   375   O OD2 . ASP A 1 73  ? 17.168  -11.679 41.141  1.00 67.47  ? 73   ASP A OD2 1 
ATOM   376   N N   . ALA A 1 74  ? 21.847  -12.858 41.278  1.00 66.91  ? 74   ALA A N   1 
ATOM   377   C CA  . ALA A 1 74  ? 22.620  -13.384 40.156  1.00 67.96  ? 74   ALA A CA  1 
ATOM   378   C C   . ALA A 1 74  ? 21.859  -14.347 39.231  1.00 69.66  ? 74   ALA A C   1 
ATOM   379   O O   . ALA A 1 74  ? 22.437  -15.274 38.689  1.00 71.80  ? 74   ALA A O   1 
ATOM   380   C CB  . ALA A 1 74  ? 23.988  -13.956 40.619  1.00 69.32  ? 74   ALA A CB  1 
ATOM   381   N N   . LYS A 1 75  ? 20.560  -14.122 39.059  1.00 69.14  ? 75   LYS A N   1 
ATOM   382   C CA  . LYS A 1 75  ? 19.835  -14.582 37.852  1.00 70.54  ? 75   LYS A CA  1 
ATOM   383   C C   . LYS A 1 75  ? 19.826  -13.439 36.803  1.00 67.97  ? 75   LYS A C   1 
ATOM   384   O O   . LYS A 1 75  ? 19.644  -13.644 35.583  1.00 68.62  ? 75   LYS A O   1 
ATOM   385   C CB  . LYS A 1 75  ? 18.405  -14.967 38.207  1.00 71.54  ? 75   LYS A CB  1 
ATOM   386   C CG  . LYS A 1 75  ? 18.300  -16.151 39.142  1.00 75.41  ? 75   LYS A CG  1 
ATOM   387   C CD  . LYS A 1 75  ? 17.257  -15.877 40.233  1.00 77.20  ? 75   LYS A CD  1 
ATOM   388   C CE  . LYS A 1 75  ? 17.523  -16.714 41.485  1.00 80.41  ? 75   LYS A CE  1 
ATOM   389   N NZ  . LYS A 1 75  ? 17.497  -15.887 42.725  1.00 79.19  ? 75   LYS A NZ  1 
ATOM   390   N N   . VAL A 1 76  ? 20.003  -12.233 37.330  1.00 64.98  ? 76   VAL A N   1 
ATOM   391   C CA  . VAL A 1 76  ? 20.280  -11.019 36.588  1.00 62.16  ? 76   VAL A CA  1 
ATOM   392   C C   . VAL A 1 76  ? 21.723  -11.037 36.011  1.00 62.21  ? 76   VAL A C   1 
ATOM   393   O O   . VAL A 1 76  ? 22.692  -11.196 36.759  1.00 62.66  ? 76   VAL A O   1 
ATOM   394   C CB  . VAL A 1 76  ? 20.110  -9.811  37.549  1.00 59.85  ? 76   VAL A CB  1 
ATOM   395   C CG1 . VAL A 1 76  ? 20.652  -8.540  36.935  1.00 58.06  ? 76   VAL A CG1 1 
ATOM   396   C CG2 . VAL A 1 76  ? 18.648  -9.648  37.967  1.00 59.48  ? 76   VAL A CG2 1 
ATOM   397   N N   . LYS A 1 77  ? 21.861  -10.873 34.693  1.00 61.70  ? 77   LYS A N   1 
ATOM   398   C CA  . LYS A 1 77  ? 23.162  -10.958 34.027  1.00 62.09  ? 77   LYS A CA  1 
ATOM   399   C C   . LYS A 1 77  ? 23.214  -10.063 32.828  1.00 59.69  ? 77   LYS A C   1 
ATOM   400   O O   . LYS A 1 77  ? 23.435  -10.521 31.705  1.00 60.59  ? 77   LYS A O   1 
ATOM   401   C CB  . LYS A 1 77  ? 23.438  -12.389 33.596  1.00 65.56  ? 77   LYS A CB  1 
ATOM   402   C CG  . LYS A 1 77  ? 24.386  -13.085 34.539  1.00 70.04  ? 77   LYS A CG  1 
ATOM   403   C CD  . LYS A 1 77  ? 23.939  -14.493 34.886  1.00 76.78  ? 77   LYS A CD  1 
ATOM   404   C CE  . LYS A 1 77  ? 24.676  -14.958 36.133  1.00 80.07  ? 77   LYS A CE  1 
ATOM   405   N NZ  . LYS A 1 77  ? 24.714  -16.445 36.239  1.00 85.64  ? 77   LYS A NZ  1 
ATOM   406   N N   . LEU A 1 78  ? 23.034  -8.774  33.087  1.00 56.50  ? 78   LEU A N   1 
ATOM   407   C CA  . LEU A 1 78  ? 22.779  -7.807  32.033  1.00 53.96  ? 78   LEU A CA  1 
ATOM   408   C C   . LEU A 1 78  ? 23.764  -7.944  30.896  1.00 54.38  ? 78   LEU A C   1 
ATOM   409   O O   . LEU A 1 78  ? 23.356  -8.159  29.748  1.00 54.78  ? 78   LEU A O   1 
ATOM   410   C CB  . LEU A 1 78  ? 22.759  -6.391  32.592  1.00 51.18  ? 78   LEU A CB  1 
ATOM   411   C CG  . LEU A 1 78  ? 21.696  -6.271  33.683  1.00 50.60  ? 78   LEU A CG  1 
ATOM   412   C CD1 . LEU A 1 78  ? 21.482  -4.807  34.118  1.00 47.85  ? 78   LEU A CD1 1 
ATOM   413   C CD2 . LEU A 1 78  ? 20.372  -6.951  33.263  1.00 51.68  ? 78   LEU A CD2 1 
ATOM   414   N N   . ILE A 1 79  ? 25.053  -7.869  31.217  1.00 54.32  ? 79   ILE A N   1 
ATOM   415   C CA  . ILE A 1 79  ? 26.057  -7.877  30.179  1.00 54.60  ? 79   ILE A CA  1 
ATOM   416   C C   . ILE A 1 79  ? 25.918  -9.129  29.325  1.00 56.80  ? 79   ILE A C   1 
ATOM   417   O O   . ILE A 1 79  ? 25.714  -9.027  28.110  1.00 56.92  ? 79   ILE A O   1 
ATOM   418   C CB  . ILE A 1 79  ? 27.466  -7.673  30.711  1.00 54.91  ? 79   ILE A CB  1 
ATOM   419   C CG1 . ILE A 1 79  ? 27.545  -6.369  31.502  1.00 52.87  ? 79   ILE A CG1 1 
ATOM   420   C CG2 . ILE A 1 79  ? 28.422  -7.551  29.553  1.00 55.65  ? 79   ILE A CG2 1 
ATOM   421   C CD1 . ILE A 1 79  ? 28.870  -6.148  32.213  1.00 53.99  ? 79   ILE A CD1 1 
ATOM   422   N N   . LYS A 1 80  ? 25.968  -10.304 29.945  1.00 58.65  ? 80   LYS A N   1 
ATOM   423   C CA  . LYS A 1 80  ? 25.716  -11.539 29.194  1.00 60.95  ? 80   LYS A CA  1 
ATOM   424   C C   . LYS A 1 80  ? 24.530  -11.358 28.238  1.00 59.60  ? 80   LYS A C   1 
ATOM   425   O O   . LYS A 1 80  ? 24.620  -11.644 27.043  1.00 60.05  ? 80   LYS A O   1 
ATOM   426   C CB  . LYS A 1 80  ? 25.433  -12.703 30.155  1.00 63.43  ? 80   LYS A CB  1 
ATOM   427   C CG  . LYS A 1 80  ? 24.830  -13.962 29.486  1.00 67.50  ? 80   LYS A CG  1 
ATOM   428   C CD  . LYS A 1 80  ? 25.879  -15.043 29.206  1.00 73.69  ? 80   LYS A CD  1 
ATOM   429   C CE  . LYS A 1 80  ? 25.632  -15.728 27.855  1.00 77.50  ? 80   LYS A CE  1 
ATOM   430   N NZ  . LYS A 1 80  ? 26.355  -15.041 26.726  1.00 79.21  ? 80   LYS A NZ  1 
ATOM   431   N N   . GLN A 1 81  ? 23.434  -10.846 28.791  1.00 57.70  ? 81   GLN A N   1 
ATOM   432   C CA  . GLN A 1 81  ? 22.166  -10.791 28.088  1.00 57.22  ? 81   GLN A CA  1 
ATOM   433   C C   . GLN A 1 81  ? 22.205  -9.814  26.930  1.00 54.89  ? 81   GLN A C   1 
ATOM   434   O O   . GLN A 1 81  ? 21.859  -10.209 25.822  1.00 55.90  ? 81   GLN A O   1 
ATOM   435   C CB  . GLN A 1 81  ? 21.012  -10.534 29.059  1.00 56.52  ? 81   GLN A CB  1 
ATOM   436   C CG  . GLN A 1 81  ? 20.869  -11.651 30.108  1.00 61.23  ? 81   GLN A CG  1 
ATOM   437   C CD  . GLN A 1 81  ? 19.723  -11.451 31.107  1.00 63.81  ? 81   GLN A CD  1 
ATOM   438   O OE1 . GLN A 1 81  ? 18.588  -11.137 30.715  1.00 64.90  ? 81   GLN A OE1 1 
ATOM   439   N NE2 . GLN A 1 81  ? 20.007  -11.681 32.405  1.00 64.00  ? 81   GLN A NE2 1 
ATOM   440   N N   . GLU A 1 82  ? 22.668  -8.578  27.162  1.00 51.90  ? 82   GLU A N   1 
ATOM   441   C CA  . GLU A 1 82  ? 22.805  -7.590  26.080  1.00 49.85  ? 82   GLU A CA  1 
ATOM   442   C C   . GLU A 1 82  ? 23.596  -8.152  24.946  1.00 50.89  ? 82   GLU A C   1 
ATOM   443   O O   . GLU A 1 82  ? 23.222  -7.992  23.794  1.00 50.69  ? 82   GLU A O   1 
ATOM   444   C CB  . GLU A 1 82  ? 23.496  -6.307  26.529  1.00 47.78  ? 82   GLU A CB  1 
ATOM   445   C CG  . GLU A 1 82  ? 22.556  -5.170  26.932  1.00 47.16  ? 82   GLU A CG  1 
ATOM   446   C CD  . GLU A 1 82  ? 21.812  -4.490  25.776  1.00 48.20  ? 82   GLU A CD  1 
ATOM   447   O OE1 . GLU A 1 82  ? 22.402  -4.370  24.682  1.00 48.87  ? 82   GLU A OE1 1 
ATOM   448   O OE2 . GLU A 1 82  ? 20.639  -4.056  25.980  1.00 47.58  ? 82   GLU A OE2 1 
ATOM   449   N N   . LEU A 1 83  ? 24.696  -8.813  25.274  1.00 52.34  ? 83   LEU A N   1 
ATOM   450   C CA  . LEU A 1 83  ? 25.545  -9.395  24.248  1.00 54.17  ? 83   LEU A CA  1 
ATOM   451   C C   . LEU A 1 83  ? 24.755  -10.368 23.414  1.00 55.80  ? 83   LEU A C   1 
ATOM   452   O O   . LEU A 1 83  ? 24.854  -10.345 22.193  1.00 56.15  ? 83   LEU A O   1 
ATOM   453   C CB  . LEU A 1 83  ? 26.782  -10.087 24.830  1.00 56.25  ? 83   LEU A CB  1 
ATOM   454   C CG  . LEU A 1 83  ? 28.017  -9.267  25.251  1.00 55.89  ? 83   LEU A CG  1 
ATOM   455   C CD1 . LEU A 1 83  ? 29.262  -9.770  24.504  1.00 59.03  ? 83   LEU A CD1 1 
ATOM   456   C CD2 . LEU A 1 83  ? 27.872  -7.781  25.026  1.00 53.51  ? 83   LEU A CD2 1 
ATOM   457   N N   . ASP A 1 84  ? 23.949  -11.197 24.072  1.00 56.86  ? 84   ASP A N   1 
ATOM   458   C CA  . ASP A 1 84  ? 23.169  -12.203 23.375  1.00 59.13  ? 84   ASP A CA  1 
ATOM   459   C C   . ASP A 1 84  ? 22.197  -11.581 22.421  1.00 57.08  ? 84   ASP A C   1 
ATOM   460   O O   . ASP A 1 84  ? 22.206  -11.886 21.233  1.00 57.96  ? 84   ASP A O   1 
ATOM   461   C CB  . ASP A 1 84  ? 22.448  -13.082 24.372  1.00 61.14  ? 84   ASP A CB  1 
ATOM   462   C CG  . ASP A 1 84  ? 23.394  -14.061 25.049  1.00 66.80  ? 84   ASP A CG  1 
ATOM   463   O OD1 . ASP A 1 84  ? 24.517  -14.256 24.506  1.00 71.47  ? 84   ASP A OD1 1 
ATOM   464   O OD2 . ASP A 1 84  ? 23.036  -14.637 26.112  1.00 70.83  ? 84   ASP A OD2 1 
ATOM   465   N N   . LYS A 1 85  ? 21.370  -10.695 22.957  1.00 54.40  ? 85   LYS A N   1 
ATOM   466   C CA  . LYS A 1 85  ? 20.494  -9.846  22.156  1.00 52.23  ? 85   LYS A CA  1 
ATOM   467   C C   . LYS A 1 85  ? 21.238  -9.419  20.897  1.00 51.60  ? 85   LYS A C   1 
ATOM   468   O O   . LYS A 1 85  ? 20.842  -9.788  19.781  1.00 52.38  ? 85   LYS A O   1 
ATOM   469   C CB  . LYS A 1 85  ? 20.088  -8.605  22.960  1.00 49.48  ? 85   LYS A CB  1 
ATOM   470   C CG  . LYS A 1 85  ? 18.802  -7.954  22.516  1.00 48.23  ? 85   LYS A CG  1 
ATOM   471   C CD  . LYS A 1 85  ? 18.668  -6.582  23.138  1.00 46.40  ? 85   LYS A CD  1 
ATOM   472   C CE  . LYS A 1 85  ? 19.668  -5.605  22.523  1.00 47.40  ? 85   LYS A CE  1 
ATOM   473   N NZ  . LYS A 1 85  ? 19.421  -4.223  23.066  1.00 47.33  ? 85   LYS A NZ  1 
ATOM   474   N N   . TYR A 1 86  ? 22.332  -8.679  21.095  1.00 50.05  ? 86   TYR A N   1 
ATOM   475   C CA  . TYR A 1 86  ? 23.155  -8.216  19.993  1.00 49.53  ? 86   TYR A CA  1 
ATOM   476   C C   . TYR A 1 86  ? 23.648  -9.333  19.067  1.00 51.78  ? 86   TYR A C   1 
ATOM   477   O O   . TYR A 1 86  ? 23.378  -9.328  17.857  1.00 51.80  ? 86   TYR A O   1 
ATOM   478   C CB  . TYR A 1 86  ? 24.353  -7.416  20.500  1.00 48.46  ? 86   TYR A CB  1 
ATOM   479   C CG  . TYR A 1 86  ? 25.286  -7.048  19.367  1.00 48.94  ? 86   TYR A CG  1 
ATOM   480   C CD1 . TYR A 1 86  ? 24.808  -6.351  18.246  1.00 48.76  ? 86   TYR A CD1 1 
ATOM   481   C CD2 . TYR A 1 86  ? 26.639  -7.419  19.396  1.00 50.20  ? 86   TYR A CD2 1 
ATOM   482   C CE1 . TYR A 1 86  ? 25.650  -6.024  17.195  1.00 49.34  ? 86   TYR A CE1 1 
ATOM   483   C CE2 . TYR A 1 86  ? 27.508  -7.088  18.351  1.00 50.71  ? 86   TYR A CE2 1 
ATOM   484   C CZ  . TYR A 1 86  ? 27.007  -6.389  17.252  1.00 50.90  ? 86   TYR A CZ  1 
ATOM   485   O OH  . TYR A 1 86  ? 27.853  -6.070  16.206  1.00 51.25  ? 86   TYR A OH  1 
ATOM   486   N N   . LYS A 1 87  ? 24.385  -10.273 19.642  1.00 53.72  ? 87   LYS A N   1 
ATOM   487   C CA  . LYS A 1 87  ? 24.970  -11.348 18.860  1.00 56.91  ? 87   LYS A CA  1 
ATOM   488   C C   . LYS A 1 87  ? 23.928  -11.967 17.968  1.00 57.72  ? 87   LYS A C   1 
ATOM   489   O O   . LYS A 1 87  ? 24.191  -12.326 16.820  1.00 59.39  ? 87   LYS A O   1 
ATOM   490   C CB  . LYS A 1 87  ? 25.533  -12.443 19.756  1.00 59.45  ? 87   LYS A CB  1 
ATOM   491   C CG  . LYS A 1 87  ? 26.821  -12.070 20.459  1.00 60.65  ? 87   LYS A CG  1 
ATOM   492   C CD  . LYS A 1 87  ? 27.336  -13.226 21.334  1.00 65.71  ? 87   LYS A CD  1 
ATOM   493   C CE  . LYS A 1 87  ? 28.212  -12.735 22.484  1.00 65.29  ? 87   LYS A CE  1 
ATOM   494   N NZ  . LYS A 1 87  ? 29.302  -13.705 22.745  1.00 69.10  ? 87   LYS A NZ  1 
ATOM   495   N N   . ASN A 1 88  ? 22.732  -12.092 18.512  1.00 56.70  ? 88   ASN A N   1 
ATOM   496   C CA  . ASN A 1 88  ? 21.679  -12.785 17.814  1.00 57.51  ? 88   ASN A CA  1 
ATOM   497   C C   . ASN A 1 88  ? 21.247  -11.994 16.582  1.00 55.24  ? 88   ASN A C   1 
ATOM   498   O O   . ASN A 1 88  ? 21.223  -12.527 15.457  1.00 56.49  ? 88   ASN A O   1 
ATOM   499   C CB  . ASN A 1 88  ? 20.526  -13.051 18.777  1.00 57.75  ? 88   ASN A CB  1 
ATOM   500   C CG  . ASN A 1 88  ? 19.255  -13.368 18.073  1.00 59.08  ? 88   ASN A CG  1 
ATOM   501   O OD1 . ASN A 1 88  ? 19.037  -14.480 17.599  1.00 62.63  ? 88   ASN A OD1 1 
ATOM   502   N ND2 . ASN A 1 88  ? 18.393  -12.378 17.994  1.00 58.32  ? 88   ASN A ND2 1 
ATOM   503   N N   . ALA A 1 89  ? 20.944  -10.715 16.809  1.00 51.55  ? 89   ALA A N   1 
ATOM   504   C CA  . ALA A 1 89  ? 20.572  -9.816  15.729  1.00 49.29  ? 89   ALA A CA  1 
ATOM   505   C C   . ALA A 1 89  ? 21.550  -10.103 14.599  1.00 50.05  ? 89   ALA A C   1 
ATOM   506   O O   . ALA A 1 89  ? 21.173  -10.259 13.422  1.00 50.61  ? 89   ALA A O   1 
ATOM   507   C CB  . ALA A 1 89  ? 20.639  -8.335  16.189  1.00 46.08  ? 89   ALA A CB  1 
ATOM   508   N N   . VAL A 1 90  ? 22.802  -10.257 14.997  1.00 49.89  ? 90   VAL A N   1 
ATOM   509   C CA  . VAL A 1 90  ? 23.862  -10.350 14.054  1.00 50.55  ? 90   VAL A CA  1 
ATOM   510   C C   . VAL A 1 90  ? 23.741  -11.627 13.252  1.00 53.54  ? 90   VAL A C   1 
ATOM   511   O O   . VAL A 1 90  ? 23.900  -11.627 12.018  1.00 54.15  ? 90   VAL A O   1 
ATOM   512   C CB  . VAL A 1 90  ? 25.182  -10.226 14.773  1.00 50.47  ? 90   VAL A CB  1 
ATOM   513   C CG1 . VAL A 1 90  ? 26.323  -10.629 13.859  1.00 52.48  ? 90   VAL A CG1 1 
ATOM   514   C CG2 . VAL A 1 90  ? 25.355  -8.804  15.256  1.00 47.28  ? 90   VAL A CG2 1 
ATOM   515   N N   . THR A 1 91  ? 23.428  -12.707 13.952  1.00 55.64  ? 91   THR A N   1 
ATOM   516   C CA  . THR A 1 91  ? 23.254  -13.975 13.285  1.00 59.11  ? 91   THR A CA  1 
ATOM   517   C C   . THR A 1 91  ? 22.084  -13.865 12.335  1.00 59.23  ? 91   THR A C   1 
ATOM   518   O O   . THR A 1 91  ? 22.182  -14.285 11.175  1.00 60.96  ? 91   THR A O   1 
ATOM   519   C CB  . THR A 1 91  ? 22.957  -15.083 14.240  1.00 60.84  ? 91   THR A CB  1 
ATOM   520   O OG1 . THR A 1 91  ? 23.717  -14.887 15.432  1.00 60.32  ? 91   THR A OG1 1 
ATOM   521   C CG2 . THR A 1 91  ? 23.334  -16.382 13.599  1.00 64.86  ? 91   THR A CG2 1 
ATOM   522   N N   . GLU A 1 92  ? 20.985  -13.281 12.816  1.00 57.59  ? 92   GLU A N   1 
ATOM   523   C CA  . GLU A 1 92  ? 19.810  -13.089 11.975  1.00 57.60  ? 92   GLU A CA  1 
ATOM   524   C C   . GLU A 1 92  ? 20.139  -12.463 10.632  1.00 56.61  ? 92   GLU A C   1 
ATOM   525   O O   . GLU A 1 92  ? 19.709  -12.968 9.579   1.00 57.84  ? 92   GLU A O   1 
ATOM   526   C CB  . GLU A 1 92  ? 18.745  -12.273 12.695  1.00 55.48  ? 92   GLU A CB  1 
ATOM   527   C CG  . GLU A 1 92  ? 17.708  -13.132 13.398  1.00 59.59  ? 92   GLU A CG  1 
ATOM   528   C CD  . GLU A 1 92  ? 17.097  -14.244 12.492  1.00 66.49  ? 92   GLU A CD  1 
ATOM   529   O OE1 . GLU A 1 92  ? 16.871  -14.048 11.253  1.00 67.95  ? 92   GLU A OE1 1 
ATOM   530   O OE2 . GLU A 1 92  ? 16.833  -15.337 13.044  1.00 69.62  ? 92   GLU A OE2 1 
ATOM   531   N N   . LEU A 1 93  ? 20.908  -11.377 10.683  1.00 54.43  ? 93   LEU A N   1 
ATOM   532   C CA  . LEU A 1 93  ? 21.314  -10.683 9.478   1.00 53.95  ? 93   LEU A CA  1 
ATOM   533   C C   . LEU A 1 93  ? 22.221  -11.571 8.650   1.00 57.31  ? 93   LEU A C   1 
ATOM   534   O O   . LEU A 1 93  ? 22.075  -11.661 7.418   1.00 58.50  ? 93   LEU A O   1 
ATOM   535   C CB  . LEU A 1 93  ? 22.029  -9.379  9.801   1.00 50.98  ? 93   LEU A CB  1 
ATOM   536   C CG  . LEU A 1 93  ? 21.191  -8.220  10.332  1.00 47.59  ? 93   LEU A CG  1 
ATOM   537   C CD1 . LEU A 1 93  ? 22.104  -7.168  10.886  1.00 45.99  ? 93   LEU A CD1 1 
ATOM   538   C CD2 . LEU A 1 93  ? 20.298  -7.604  9.276   1.00 45.89  ? 93   LEU A CD2 1 
ATOM   539   N N   . GLN A 1 94  ? 23.154  -12.240 9.316   1.00 59.23  ? 94   GLN A N   1 
ATOM   540   C CA  . GLN A 1 94  ? 24.041  -13.110 8.589   1.00 62.86  ? 94   GLN A CA  1 
ATOM   541   C C   . GLN A 1 94  ? 23.263  -14.001 7.655   1.00 65.18  ? 94   GLN A C   1 
ATOM   542   O O   . GLN A 1 94  ? 23.708  -14.295 6.551   1.00 67.10  ? 94   GLN A O   1 
ATOM   543   C CB  . GLN A 1 94  ? 24.818  -13.969 9.540   1.00 65.04  ? 94   GLN A CB  1 
ATOM   544   C CG  . GLN A 1 94  ? 26.247  -13.615 9.637   1.00 66.68  ? 94   GLN A CG  1 
ATOM   545   C CD  . GLN A 1 94  ? 26.790  -14.033 10.965  1.00 70.61  ? 94   GLN A CD  1 
ATOM   546   O OE1 . GLN A 1 94  ? 26.655  -15.198 11.383  1.00 74.49  ? 94   GLN A OE1 1 
ATOM   547   N NE2 . GLN A 1 94  ? 27.395  -13.081 11.664  1.00 70.04  ? 94   GLN A NE2 1 
ATOM   548   N N   . LEU A 1 95  ? 22.086  -14.412 8.092   1.00 65.55  ? 95   LEU A N   1 
ATOM   549   C CA  . LEU A 1 95  ? 21.366  -15.416 7.368   1.00 68.88  ? 95   LEU A CA  1 
ATOM   550   C C   . LEU A 1 95  ? 20.750  -14.855 6.111   1.00 69.23  ? 95   LEU A C   1 
ATOM   551   O O   . LEU A 1 95  ? 20.301  -15.587 5.240   1.00 71.90  ? 95   LEU A O   1 
ATOM   552   C CB  . LEU A 1 95  ? 20.339  -16.062 8.280   1.00 69.15  ? 95   LEU A CB  1 
ATOM   553   C CG  . LEU A 1 95  ? 21.010  -16.754 9.480   1.00 69.23  ? 95   LEU A CG  1 
ATOM   554   C CD1 . LEU A 1 95  ? 20.049  -16.954 10.631  1.00 67.30  ? 95   LEU A CD1 1 
ATOM   555   C CD2 . LEU A 1 95  ? 21.666  -18.090 9.098   1.00 71.69  ? 95   LEU A CD2 1 
ATOM   556   N N   . LEU A 1 96  ? 20.784  -13.545 5.992   1.00 67.56  ? 96   LEU A N   1 
ATOM   557   C CA  . LEU A 1 96  ? 20.177  -12.908 4.856   1.00 68.00  ? 96   LEU A CA  1 
ATOM   558   C C   . LEU A 1 96  ? 20.972  -13.075 3.588   1.00 71.05  ? 96   LEU A C   1 
ATOM   559   O O   . LEU A 1 96  ? 20.436  -12.903 2.495   1.00 71.48  ? 96   LEU A O   1 
ATOM   560   C CB  . LEU A 1 96  ? 19.933  -11.435 5.140   1.00 64.17  ? 96   LEU A CB  1 
ATOM   561   C CG  . LEU A 1 96  ? 18.731  -11.296 6.065   1.00 62.62  ? 96   LEU A CG  1 
ATOM   562   C CD1 . LEU A 1 96  ? 18.192  -9.901  5.996   1.00 59.12  ? 96   LEU A CD1 1 
ATOM   563   C CD2 . LEU A 1 96  ? 17.646  -12.309 5.660   1.00 64.75  ? 96   LEU A CD2 1 
ATOM   564   N N   . MET A 1 97  ? 22.234  -13.451 3.725   1.00 74.45  ? 97   MET A N   1 
ATOM   565   C CA  . MET A 1 97  ? 23.174  -13.341 2.614   1.00 77.89  ? 97   MET A CA  1 
ATOM   566   C C   . MET A 1 97  ? 23.048  -14.367 1.488   1.00 82.27  ? 97   MET A C   1 
ATOM   567   O O   . MET A 1 97  ? 23.357  -14.078 0.313   1.00 83.17  ? 97   MET A O   1 
ATOM   568   C CB  . MET A 1 97  ? 24.587  -13.245 3.158   1.00 78.37  ? 97   MET A CB  1 
ATOM   569   C CG  . MET A 1 97  ? 24.695  -12.110 4.199   1.00 78.44  ? 97   MET A CG  1 
ATOM   570   S SD  . MET A 1 97  ? 24.526  -10.341 3.685   1.00 81.20  ? 97   MET A SD  1 
ATOM   571   C CE  . MET A 1 97  ? 23.465  -10.378 2.207   1.00 77.95  ? 97   MET A CE  1 
ATOM   572   N N   . GLN A 1 98  ? 22.564  -15.557 1.844   1.00 86.02  ? 98   GLN A N   1 
ATOM   573   C CA  . GLN A 1 98  ? 22.426  -16.685 0.888   1.00 90.47  ? 98   GLN A CA  1 
ATOM   574   C C   . GLN A 1 98  ? 21.007  -17.330 0.915   1.00 91.35  ? 98   GLN A C   1 
ATOM   575   O O   . GLN A 1 98  ? 20.073  -16.872 1.607   1.00 88.90  ? 98   GLN A O   1 
ATOM   576   C CB  . GLN A 1 98  ? 23.533  -17.763 1.117   1.00 94.21  ? 98   GLN A CB  1 
ATOM   577   C CG  . GLN A 1 98  ? 24.939  -17.276 1.689   1.00 94.74  ? 98   GLN A CG  1 
ATOM   578   C CD  . GLN A 1 98  ? 24.985  -16.967 3.240   1.00 94.27  ? 98   GLN A CD  1 
ATOM   579   O OE1 . GLN A 1 98  ? 24.167  -16.197 3.784   1.00 90.31  ? 98   GLN A OE1 1 
ATOM   580   N NE2 . GLN A 1 98  ? 25.978  -17.557 3.928   1.00 95.89  ? 98   GLN A NE2 1 
ATOM   581   N N   . SER A 1 137 ? 45.077  -13.956 116.849 1.00 101.16 ? 146  SER A N   1 
ATOM   582   C CA  . SER A 1 137 ? 45.756  -12.985 117.705 1.00 101.40 ? 146  SER A CA  1 
ATOM   583   C C   . SER A 1 137 ? 45.664  -13.351 119.197 1.00 103.57 ? 146  SER A C   1 
ATOM   584   O O   . SER A 1 137 ? 45.019  -14.336 119.545 1.00 104.81 ? 146  SER A O   1 
ATOM   585   C CB  . SER A 1 137 ? 45.159  -11.603 117.451 1.00 98.81  ? 146  SER A CB  1 
ATOM   586   O OG  . SER A 1 137 ? 44.405  -11.188 118.576 1.00 99.03  ? 146  SER A OG  1 
ATOM   587   N N   . ALA A 1 138 ? 46.301  -12.553 120.062 1.00 104.10 ? 147  ALA A N   1 
ATOM   588   C CA  . ALA A 1 138 ? 46.354  -12.855 121.504 1.00 106.29 ? 147  ALA A CA  1 
ATOM   589   C C   . ALA A 1 138 ? 46.562  -11.716 122.492 1.00 106.27 ? 147  ALA A C   1 
ATOM   590   O O   . ALA A 1 138 ? 46.769  -11.962 123.654 1.00 108.22 ? 147  ALA A O   1 
ATOM   591   C CB  . ALA A 1 138 ? 47.348  -13.942 121.775 1.00 108.96 ? 147  ALA A CB  1 
ATOM   592   N N   . ILE A 1 139 ? 46.521  -10.479 122.028 1.00 104.21 ? 148  ILE A N   1 
ATOM   593   C CA  . ILE A 1 139 ? 46.264  -9.291  122.874 1.00 103.78 ? 148  ILE A CA  1 
ATOM   594   C C   . ILE A 1 139 ? 47.115  -9.038  124.106 1.00 105.86 ? 148  ILE A C   1 
ATOM   595   O O   . ILE A 1 139 ? 47.146  -9.831  125.040 1.00 107.92 ? 148  ILE A O   1 
ATOM   596   C CB  . ILE A 1 139 ? 44.767  -9.152  123.269 1.00 102.93 ? 148  ILE A CB  1 
ATOM   597   C CG1 . ILE A 1 139 ? 44.430  -7.699  123.581 1.00 101.67 ? 148  ILE A CG1 1 
ATOM   598   C CG2 . ILE A 1 139 ? 44.429  -10.025 124.467 1.00 105.17 ? 148  ILE A CG2 1 
ATOM   599   C CD1 . ILE A 1 139 ? 43.115  -7.315  123.061 1.00 99.69  ? 148  ILE A CD1 1 
ATOM   600   N N   . ALA A 1 140 ? 47.747  -7.871  124.108 1.00 105.31 ? 149  ALA A N   1 
ATOM   601   C CA  . ALA A 1 140 ? 48.756  -7.519  125.087 1.00 107.24 ? 149  ALA A CA  1 
ATOM   602   C C   . ALA A 1 140 ? 48.330  -8.015  126.397 1.00 109.01 ? 149  ALA A C   1 
ATOM   603   O O   . ALA A 1 140 ? 48.428  -9.186  126.678 1.00 110.59 ? 149  ALA A O   1 
ATOM   604   C CB  . ALA A 1 140 ? 48.934  -6.023  125.153 1.00 106.25 ? 149  ALA A CB  1 
ATOM   605   N N   . SER A 1 141 ? 47.790  -7.084  127.153 1.00 108.71 ? 150  SER A N   1 
ATOM   606   C CA  . SER A 1 141 ? 47.509  -7.194  128.556 1.00 110.48 ? 150  SER A CA  1 
ATOM   607   C C   . SER A 1 141 ? 47.845  -5.818  128.971 1.00 110.27 ? 150  SER A C   1 
ATOM   608   O O   . SER A 1 141 ? 48.431  -5.069  128.195 1.00 109.19 ? 150  SER A O   1 
ATOM   609   C CB  . SER A 1 141 ? 48.512  -8.077  129.259 1.00 113.13 ? 150  SER A CB  1 
ATOM   610   O OG  . SER A 1 141 ? 49.856  -7.630  129.065 1.00 113.77 ? 150  SER A OG  1 
ATOM   611   N N   . GLY A 1 142 ? 47.549  -5.503  130.220 1.00 111.55 ? 151  GLY A N   1 
ATOM   612   C CA  . GLY A 1 142 ? 47.926  -4.210  130.731 1.00 111.76 ? 151  GLY A CA  1 
ATOM   613   C C   . GLY A 1 142 ? 47.839  -3.251  129.564 1.00 109.44 ? 151  GLY A C   1 
ATOM   614   O O   . GLY A 1 142 ? 46.732  -2.850  129.180 1.00 107.71 ? 151  GLY A O   1 
ATOM   615   N N   . VAL A 1 143 ? 48.974  -2.897  128.966 1.00 109.46 ? 152  VAL A N   1 
ATOM   616   C CA  . VAL A 1 143 ? 48.886  -1.863  127.948 1.00 107.41 ? 152  VAL A CA  1 
ATOM   617   C C   . VAL A 1 143 ? 49.704  -1.951  126.647 1.00 106.46 ? 152  VAL A C   1 
ATOM   618   O O   . VAL A 1 143 ? 50.581  -2.802  126.470 1.00 107.59 ? 152  VAL A O   1 
ATOM   619   C CB  . VAL A 1 143 ? 48.907  -0.452  128.552 1.00 107.70 ? 152  VAL A CB  1 
ATOM   620   C CG1 . VAL A 1 143 ? 47.903  0.438   127.802 1.00 105.36 ? 152  VAL A CG1 1 
ATOM   621   C CG2 . VAL A 1 143 ? 48.540  -0.501  130.002 1.00 109.46 ? 152  VAL A CG2 1 
ATOM   622   N N   . ALA A 1 144 ? 49.421  -0.949  125.814 1.00 104.57 ? 153  ALA A N   1 
ATOM   623   C CA  . ALA A 1 144 ? 49.229  -1.068  124.407 1.00 102.51 ? 153  ALA A CA  1 
ATOM   624   C C   . ALA A 1 144 ? 47.780  -0.689  124.354 1.00 100.84 ? 153  ALA A C   1 
ATOM   625   O O   . ALA A 1 144 ? 47.421  0.327   123.774 1.00 99.31  ? 153  ALA A O   1 
ATOM   626   C CB  . ALA A 1 144 ? 49.385  -2.477  123.963 1.00 102.77 ? 153  ALA A CB  1 
ATOM   627   N N   . VAL A 1 145 ? 46.954  -1.523  124.997 1.00 101.33 ? 154  VAL A N   1 
ATOM   628   C CA  . VAL A 1 145 ? 45.498  -1.321  125.195 1.00 100.28 ? 154  VAL A CA  1 
ATOM   629   C C   . VAL A 1 145 ? 44.747  -0.640  124.034 1.00 97.76  ? 154  VAL A C   1 
ATOM   630   O O   . VAL A 1 145 ? 45.024  -0.880  122.862 1.00 96.48  ? 154  VAL A O   1 
ATOM   631   C CB  . VAL A 1 145 ? 45.240  -0.629  126.580 1.00 101.73 ? 154  VAL A CB  1 
ATOM   632   C CG1 . VAL A 1 145 ? 44.231  0.522   126.522 1.00 100.46 ? 154  VAL A CG1 1 
ATOM   633   C CG2 . VAL A 1 145 ? 44.855  -1.644  127.659 1.00 103.42 ? 154  VAL A CG2 1 
ATOM   634   N N   . SER A 1 146 ? 43.805  0.219   124.378 1.00 97.20  ? 155  SER A N   1 
ATOM   635   C CA  . SER A 1 146 ? 42.975  0.901   123.413 1.00 95.02  ? 155  SER A CA  1 
ATOM   636   C C   . SER A 1 146 ? 43.669  1.172   122.091 1.00 93.59  ? 155  SER A C   1 
ATOM   637   O O   . SER A 1 146 ? 43.066  0.993   121.033 1.00 91.76  ? 155  SER A O   1 
ATOM   638   C CB  . SER A 1 146 ? 42.414  2.188   124.003 1.00 95.12  ? 155  SER A CB  1 
ATOM   639   O OG  . SER A 1 146 ? 43.441  3.058   124.390 1.00 96.20  ? 155  SER A OG  1 
ATOM   640   N N   . LYS A 1 147 ? 44.925  1.594   122.126 1.00 94.48  ? 156  LYS A N   1 
ATOM   641   C CA  . LYS A 1 147 ? 45.594  1.932   120.869 1.00 93.24  ? 156  LYS A CA  1 
ATOM   642   C C   . LYS A 1 147 ? 45.626  0.753   119.915 1.00 92.37  ? 156  LYS A C   1 
ATOM   643   O O   . LYS A 1 147 ? 45.281  0.890   118.752 1.00 90.50  ? 156  LYS A O   1 
ATOM   644   C CB  . LYS A 1 147 ? 47.012  2.464   121.094 1.00 94.68  ? 156  LYS A CB  1 
ATOM   645   C CG  . LYS A 1 147 ? 47.174  3.998   121.122 1.00 94.60  ? 156  LYS A CG  1 
ATOM   646   C CD  . LYS A 1 147 ? 47.924  4.572   119.901 1.00 93.63  ? 156  LYS A CD  1 
ATOM   647   C CE  . LYS A 1 147 ? 48.230  6.070   120.107 1.00 94.16  ? 156  LYS A CE  1 
ATOM   648   N NZ  . LYS A 1 147 ? 48.057  6.934   118.886 1.00 92.39  ? 156  LYS A NZ  1 
ATOM   649   N N   . VAL A 1 148 ? 46.023  -0.409  120.408 1.00 93.83  ? 157  VAL A N   1 
ATOM   650   C CA  . VAL A 1 148 ? 46.094  -1.561  119.548 1.00 93.33  ? 157  VAL A CA  1 
ATOM   651   C C   . VAL A 1 148 ? 44.800  -1.629  118.793 1.00 91.28  ? 157  VAL A C   1 
ATOM   652   O O   . VAL A 1 148 ? 44.768  -1.701  117.574 1.00 89.74  ? 157  VAL A O   1 
ATOM   653   C CB  . VAL A 1 148 ? 46.205  -2.840  120.337 1.00 95.17  ? 157  VAL A CB  1 
ATOM   654   C CG1 . VAL A 1 148 ? 46.191  -4.027  119.391 1.00 94.72  ? 157  VAL A CG1 1 
ATOM   655   C CG2 . VAL A 1 148 ? 47.450  -2.836  121.204 1.00 97.43  ? 157  VAL A CG2 1 
ATOM   656   N N   . LEU A 1 149 ? 43.721  -1.552  119.547 1.00 91.36  ? 158  LEU A N   1 
ATOM   657   C CA  . LEU A 1 149 ? 42.406  -1.828  119.032 1.00 89.89  ? 158  LEU A CA  1 
ATOM   658   C C   . LEU A 1 149 ? 41.830  -0.667  118.244 1.00 87.87  ? 158  LEU A C   1 
ATOM   659   O O   . LEU A 1 149 ? 40.834  -0.834  117.543 1.00 86.40  ? 158  LEU A O   1 
ATOM   660   C CB  . LEU A 1 149 ? 41.492  -2.278  120.166 1.00 91.05  ? 158  LEU A CB  1 
ATOM   661   C CG  . LEU A 1 149 ? 42.153  -3.364  121.023 1.00 93.28  ? 158  LEU A CG  1 
ATOM   662   C CD1 . LEU A 1 149 ? 41.799  -3.155  122.456 1.00 94.86  ? 158  LEU A CD1 1 
ATOM   663   C CD2 . LEU A 1 149 ? 41.807  -4.769  120.571 1.00 93.44  ? 158  LEU A CD2 1 
ATOM   664   N N   . HIS A 1 150 ? 42.460  0.501   118.322 1.00 87.89  ? 159  HIS A N   1 
ATOM   665   C CA  . HIS A 1 150 ? 42.131  1.553   117.363 1.00 86.02  ? 159  HIS A CA  1 
ATOM   666   C C   . HIS A 1 150 ? 42.554  1.098   115.987 1.00 84.69  ? 159  HIS A C   1 
ATOM   667   O O   . HIS A 1 150 ? 41.771  1.168   115.031 1.00 82.90  ? 159  HIS A O   1 
ATOM   668   C CB  . HIS A 1 150 ? 42.805  2.889   117.674 1.00 86.52  ? 159  HIS A CB  1 
ATOM   669   C CG  . HIS A 1 150 ? 42.009  4.065   117.210 1.00 85.11  ? 159  HIS A CG  1 
ATOM   670   N ND1 . HIS A 1 150 ? 41.312  4.879   118.076 1.00 85.70  ? 159  HIS A ND1 1 
ATOM   671   C CD2 . HIS A 1 150 ? 41.739  4.522   115.963 1.00 83.21  ? 159  HIS A CD2 1 
ATOM   672   C CE1 . HIS A 1 150 ? 40.669  5.804   117.385 1.00 84.79  ? 159  HIS A CE1 1 
ATOM   673   N NE2 . HIS A 1 150 ? 40.914  5.613   116.100 1.00 82.85  ? 159  HIS A NE2 1 
ATOM   674   N N   . LEU A 1 151 ? 43.795  0.621   115.905 1.00 85.72  ? 160  LEU A N   1 
ATOM   675   C CA  . LEU A 1 151 ? 44.356  0.150   114.651 1.00 85.04  ? 160  LEU A CA  1 
ATOM   676   C C   . LEU A 1 151 ? 43.670  -1.084  114.124 1.00 85.07  ? 160  LEU A C   1 
ATOM   677   O O   . LEU A 1 151 ? 43.314  -1.141  112.944 1.00 83.91  ? 160  LEU A O   1 
ATOM   678   C CB  . LEU A 1 151 ? 45.851  -0.071  114.768 1.00 86.86  ? 160  LEU A CB  1 
ATOM   679   C CG  . LEU A 1 151 ? 46.555  1.238   114.438 1.00 87.64  ? 160  LEU A CG  1 
ATOM   680   C CD1 . LEU A 1 151 ? 46.892  2.000   115.743 1.00 89.48  ? 160  LEU A CD1 1 
ATOM   681   C CD2 . LEU A 1 151 ? 47.779  0.979   113.557 1.00 87.62  ? 160  LEU A CD2 1 
ATOM   682   N N   . GLU A 1 152 ? 43.491  -2.066  114.994 1.00 87.20  ? 161  GLU A N   1 
ATOM   683   C CA  . GLU A 1 152 ? 42.532  -3.117  114.757 1.00 88.01  ? 161  GLU A CA  1 
ATOM   684   C C   . GLU A 1 152 ? 41.332  -2.553  114.002 1.00 86.82  ? 161  GLU A C   1 
ATOM   685   O O   . GLU A 1 152 ? 40.931  -3.102  112.984 1.00 85.72  ? 161  GLU A O   1 
ATOM   686   C CB  . GLU A 1 152 ? 42.071  -3.668  116.099 1.00 89.92  ? 161  GLU A CB  1 
ATOM   687   C CG  . GLU A 1 152 ? 40.822  -4.545  116.086 1.00 89.96  ? 161  GLU A CG  1 
ATOM   688   C CD  . GLU A 1 152 ? 41.155  -6.007  115.899 1.00 91.08  ? 161  GLU A CD  1 
ATOM   689   O OE1 . GLU A 1 152 ? 41.177  -6.752  116.903 1.00 92.83  ? 161  GLU A OE1 1 
ATOM   690   O OE2 . GLU A 1 152 ? 41.419  -6.400  114.746 1.00 90.42  ? 161  GLU A OE2 1 
ATOM   691   N N   . GLY A 1 153 ? 40.779  -1.442  114.485 1.00 87.54  ? 162  GLY A N   1 
ATOM   692   C CA  . GLY A 1 153 ? 39.565  -0.909  113.897 1.00 87.49  ? 162  GLY A CA  1 
ATOM   693   C C   . GLY A 1 153 ? 39.812  -0.244  112.571 1.00 86.74  ? 162  GLY A C   1 
ATOM   694   O O   . GLY A 1 153 ? 39.030  -0.408  111.624 1.00 85.33  ? 162  GLY A O   1 
ATOM   695   N N   . GLU A 1 154 ? 40.903  0.510   112.518 1.00 88.07  ? 163  GLU A N   1 
ATOM   696   C CA  . GLU A 1 154 ? 41.280  1.223   111.317 1.00 88.06  ? 163  GLU A CA  1 
ATOM   697   C C   . GLU A 1 154 ? 41.594  0.240   110.190 1.00 87.23  ? 163  GLU A C   1 
ATOM   698   O O   . GLU A 1 154 ? 40.982  0.291   109.104 1.00 85.71  ? 163  GLU A O   1 
ATOM   699   C CB  . GLU A 1 154 ? 42.460  2.166   111.590 1.00 89.46  ? 163  GLU A CB  1 
ATOM   700   C CG  . GLU A 1 154 ? 42.250  3.596   111.002 1.00 91.97  ? 163  GLU A CG  1 
ATOM   701   C CD  . GLU A 1 154 ? 41.332  4.504   111.882 1.00 97.10  ? 163  GLU A CD  1 
ATOM   702   O OE1 . GLU A 1 154 ? 41.630  4.653   113.100 1.00 99.48  ? 163  GLU A OE1 1 
ATOM   703   O OE2 . GLU A 1 154 ? 40.325  5.070   111.359 1.00 96.80  ? 163  GLU A OE2 1 
ATOM   704   N N   . VAL A 1 155 ? 42.526  -0.665  110.465 1.00 88.69  ? 164  VAL A N   1 
ATOM   705   C CA  . VAL A 1 155 ? 42.851  -1.743  109.544 1.00 88.75  ? 164  VAL A CA  1 
ATOM   706   C C   . VAL A 1 155 ? 41.596  -2.371  108.998 1.00 88.07  ? 164  VAL A C   1 
ATOM   707   O O   . VAL A 1 155 ? 41.417  -2.511  107.781 1.00 86.78  ? 164  VAL A O   1 
ATOM   708   C CB  . VAL A 1 155 ? 43.658  -2.840  110.254 1.00 90.80  ? 164  VAL A CB  1 
ATOM   709   C CG1 . VAL A 1 155 ? 43.439  -4.231  109.618 1.00 90.65  ? 164  VAL A CG1 1 
ATOM   710   C CG2 . VAL A 1 155 ? 45.116  -2.463  110.252 1.00 91.71  ? 164  VAL A CG2 1 
ATOM   711   N N   . ASN A 1 156 ? 40.718  -2.719  109.923 1.00 89.29  ? 165  ASN A N   1 
ATOM   712   C CA  . ASN A 1 156 ? 39.529  -3.469  109.603 1.00 89.21  ? 165  ASN A CA  1 
ATOM   713   C C   . ASN A 1 156 ? 38.534  -2.763  108.698 1.00 86.64  ? 165  ASN A C   1 
ATOM   714   O O   . ASN A 1 156 ? 37.856  -3.407  107.897 1.00 85.65  ? 165  ASN A O   1 
ATOM   715   C CB  . ASN A 1 156 ? 38.862  -3.909  110.886 1.00 91.26  ? 165  ASN A CB  1 
ATOM   716   C CG  . ASN A 1 156 ? 38.751  -5.392  110.958 1.00 94.25  ? 165  ASN A CG  1 
ATOM   717   O OD1 . ASN A 1 156 ? 39.256  -6.033  111.892 1.00 97.07  ? 165  ASN A OD1 1 
ATOM   718   N ND2 . ASN A 1 156 ? 38.132  -5.972  109.924 1.00 95.06  ? 165  ASN A ND2 1 
ATOM   719   N N   . LYS A 1 157 ? 38.452  -1.445  108.841 1.00 85.62  ? 166  LYS A N   1 
ATOM   720   C CA  . LYS A 1 157 ? 37.767  -0.629  107.868 1.00 83.65  ? 166  LYS A CA  1 
ATOM   721   C C   . LYS A 1 157 ? 38.429  -0.849  106.527 1.00 82.18  ? 166  LYS A C   1 
ATOM   722   O O   . LYS A 1 157 ? 37.812  -1.369  105.607 1.00 81.26  ? 166  LYS A O   1 
ATOM   723   C CB  . LYS A 1 157 ? 37.781  0.854   108.263 1.00 83.59  ? 166  LYS A CB  1 
ATOM   724   C CG  . LYS A 1 157 ? 36.488  1.329   108.957 1.00 84.97  ? 166  LYS A CG  1 
ATOM   725   C CD  . LYS A 1 157 ? 36.746  2.446   109.985 1.00 88.23  ? 166  LYS A CD  1 
ATOM   726   C CE  . LYS A 1 157 ? 35.597  2.579   111.015 1.00 90.08  ? 166  LYS A CE  1 
ATOM   727   N NZ  . LYS A 1 157 ? 36.128  2.786   112.408 1.00 92.24  ? 166  LYS A NZ  1 
ATOM   728   N N   . ILE A 1 158 ? 39.702  -0.509  106.434 1.00 82.31  ? 167  ILE A N   1 
ATOM   729   C CA  . ILE A 1 158 ? 40.413  -0.585  105.168 1.00 81.22  ? 167  ILE A CA  1 
ATOM   730   C C   . ILE A 1 158 ? 40.190  -1.891  104.422 1.00 81.25  ? 167  ILE A C   1 
ATOM   731   O O   . ILE A 1 158 ? 39.857  -1.882  103.243 1.00 79.71  ? 167  ILE A O   1 
ATOM   732   C CB  . ILE A 1 158 ? 41.892  -0.268  105.359 1.00 82.21  ? 167  ILE A CB  1 
ATOM   733   C CG1 . ILE A 1 158 ? 42.035  1.234   105.555 1.00 81.72  ? 167  ILE A CG1 1 
ATOM   734   C CG2 . ILE A 1 158 ? 42.698  -0.703  104.168 1.00 81.13  ? 167  ILE A CG2 1 
ATOM   735   C CD1 . ILE A 1 158 ? 43.395  1.690   105.836 1.00 83.98  ? 167  ILE A CD1 1 
ATOM   736   N N   . LYS A 1 159 ? 40.339  -3.010  105.109 1.00 83.16  ? 168  LYS A N   1 
ATOM   737   C CA  . LYS A 1 159 ? 40.069  -4.273  104.478 1.00 83.84  ? 168  LYS A CA  1 
ATOM   738   C C   . LYS A 1 159 ? 38.727  -4.193  103.765 1.00 82.15  ? 168  LYS A C   1 
ATOM   739   O O   . LYS A 1 159 ? 38.656  -4.335  102.541 1.00 80.92  ? 168  LYS A O   1 
ATOM   740   C CB  . LYS A 1 159 ? 40.071  -5.403  105.495 1.00 86.38  ? 168  LYS A CB  1 
ATOM   741   C CG  . LYS A 1 159 ? 39.447  -6.694  104.955 1.00 88.77  ? 168  LYS A CG  1 
ATOM   742   C CD  . LYS A 1 159 ? 39.124  -7.745  106.047 1.00 94.11  ? 168  LYS A CD  1 
ATOM   743   C CE  . LYS A 1 159 ? 38.188  -8.846  105.502 1.00 94.97  ? 168  LYS A CE  1 
ATOM   744   N NZ  . LYS A 1 159 ? 38.333  -10.124 106.269 1.00 97.98  ? 168  LYS A NZ  1 
ATOM   745   N N   . SER A 1 160 ? 37.667  -3.932  104.523 1.00 82.28  ? 169  SER A N   1 
ATOM   746   C CA  . SER A 1 160 ? 36.325  -3.881  103.943 1.00 81.29  ? 169  SER A CA  1 
ATOM   747   C C   . SER A 1 160 ? 36.228  -2.946  102.741 1.00 78.99  ? 169  SER A C   1 
ATOM   748   O O   . SER A 1 160 ? 35.623  -3.296  101.733 1.00 78.05  ? 169  SER A O   1 
ATOM   749   C CB  . SER A 1 160 ? 35.286  -3.532  105.004 1.00 81.75  ? 169  SER A CB  1 
ATOM   750   O OG  . SER A 1 160 ? 35.324  -4.511  106.032 1.00 84.85  ? 169  SER A OG  1 
ATOM   751   N N   . ALA A 1 161 ? 36.862  -1.782  102.852 1.00 78.39  ? 170  ALA A N   1 
ATOM   752   C CA  . ALA A 1 161 ? 36.852  -0.774  101.796 1.00 76.49  ? 170  ALA A CA  1 
ATOM   753   C C   . ALA A 1 161 ? 37.513  -1.277  100.526 1.00 75.75  ? 170  ALA A C   1 
ATOM   754   O O   . ALA A 1 161 ? 37.043  -1.020  99.400  1.00 74.03  ? 170  ALA A O   1 
ATOM   755   C CB  . ALA A 1 161 ? 37.529  0.491   102.267 1.00 76.64  ? 170  ALA A CB  1 
ATOM   756   N N   . LEU A 1 162 ? 38.607  -2.003  100.712 1.00 77.00  ? 171  LEU A N   1 
ATOM   757   C CA  . LEU A 1 162 ? 39.314  -2.565  99.578  1.00 76.74  ? 171  LEU A CA  1 
ATOM   758   C C   . LEU A 1 162 ? 38.488  -3.635  98.878  1.00 76.57  ? 171  LEU A C   1 
ATOM   759   O O   . LEU A 1 162 ? 38.393  -3.640  97.649  1.00 75.55  ? 171  LEU A O   1 
ATOM   760   C CB  . LEU A 1 162 ? 40.648  -3.150  99.999  1.00 78.44  ? 171  LEU A CB  1 
ATOM   761   C CG  . LEU A 1 162 ? 41.431  -3.712  98.821  1.00 78.17  ? 171  LEU A CG  1 
ATOM   762   C CD1 . LEU A 1 162 ? 41.998  -2.589  98.062  1.00 77.46  ? 171  LEU A CD1 1 
ATOM   763   C CD2 . LEU A 1 162 ? 42.548  -4.585  99.270  1.00 80.64  ? 171  LEU A CD2 1 
ATOM   764   N N   . LEU A 1 163 ? 37.894  -4.542  99.656  1.00 77.78  ? 172  LEU A N   1 
ATOM   765   C CA  . LEU A 1 163 ? 37.026  -5.565  99.077  1.00 77.67  ? 172  LEU A CA  1 
ATOM   766   C C   . LEU A 1 163 ? 35.974  -4.918  98.163  1.00 75.52  ? 172  LEU A C   1 
ATOM   767   O O   . LEU A 1 163 ? 35.712  -5.392  97.048  1.00 74.69  ? 172  LEU A O   1 
ATOM   768   C CB  . LEU A 1 163 ? 36.345  -6.353  100.183 1.00 79.14  ? 172  LEU A CB  1 
ATOM   769   C CG  . LEU A 1 163 ? 37.248  -7.114  101.144 1.00 81.65  ? 172  LEU A CG  1 
ATOM   770   C CD1 . LEU A 1 163 ? 36.508  -7.400  102.457 1.00 84.69  ? 172  LEU A CD1 1 
ATOM   771   C CD2 . LEU A 1 163 ? 37.713  -8.404  100.521 1.00 82.75  ? 172  LEU A CD2 1 
ATOM   772   N N   . SER A 1 164 ? 35.402  -3.821  98.661  1.00 74.46  ? 173  SER A N   1 
ATOM   773   C CA  . SER A 1 164 ? 34.393  -3.074  97.966  1.00 72.39  ? 173  SER A CA  1 
ATOM   774   C C   . SER A 1 164 ? 35.027  -2.595  96.690  1.00 70.86  ? 173  SER A C   1 
ATOM   775   O O   . SER A 1 164 ? 34.420  -2.682  95.630  1.00 69.87  ? 173  SER A O   1 
ATOM   776   C CB  . SER A 1 164 ? 33.915  -1.893  98.812  0.82 72.21  ? 173  SER A CB  1 
ATOM   777   O OG  . SER A 1 164 ? 32.503  -1.741  98.747  0.82 71.66  ? 173  SER A OG  1 
ATOM   778   N N   . THR A 1 165 ? 36.264  -2.123  96.767  1.00 70.90  ? 174  THR A N   1 
ATOM   779   C CA  . THR A 1 165 ? 36.931  -1.663  95.551  1.00 69.80  ? 174  THR A CA  1 
ATOM   780   C C   . THR A 1 165 ? 37.116  -2.798  94.564  1.00 69.72  ? 174  THR A C   1 
ATOM   781   O O   . THR A 1 165 ? 36.810  -2.672  93.403  1.00 68.42  ? 174  THR A O   1 
ATOM   782   C CB  . THR A 1 165 ? 38.267  -0.995  95.855  1.00 70.55  ? 174  THR A CB  1 
ATOM   783   O OG1 . THR A 1 165 ? 38.029  0.224   96.568  1.00 70.52  ? 174  THR A OG1 1 
ATOM   784   C CG2 . THR A 1 165 ? 39.018  -0.692  94.582  1.00 69.06  ? 174  THR A CG2 1 
ATOM   785   N N   . ASN A 1 166 ? 37.593  -3.924  95.045  1.00 71.54  ? 175  ASN A N   1 
ATOM   786   C CA  . ASN A 1 166 ? 37.765  -5.072  94.193  1.00 72.22  ? 175  ASN A CA  1 
ATOM   787   C C   . ASN A 1 166 ? 36.520  -5.387  93.393  1.00 71.10  ? 175  ASN A C   1 
ATOM   788   O O   . ASN A 1 166 ? 36.573  -5.494  92.174  1.00 70.23  ? 175  ASN A O   1 
ATOM   789   C CB  . ASN A 1 166 ? 38.197  -6.265  95.030  1.00 74.68  ? 175  ASN A CB  1 
ATOM   790   C CG  . ASN A 1 166 ? 39.610  -6.119  95.523  1.00 76.87  ? 175  ASN A CG  1 
ATOM   791   O OD1 . ASN A 1 166 ? 40.271  -5.109  95.253  1.00 76.80  ? 175  ASN A OD1 1 
ATOM   792   N ND2 . ASN A 1 166 ? 40.097  -7.125  96.230  1.00 80.01  ? 175  ASN A ND2 1 
ATOM   793   N N   . LYS A 1 167 ? 35.395  -5.507  94.078  1.00 71.26  ? 176  LYS A N   1 
ATOM   794   C CA  . LYS A 1 167 ? 34.137  -5.807  93.423  1.00 70.60  ? 176  LYS A CA  1 
ATOM   795   C C   . LYS A 1 167 ? 33.741  -4.727  92.432  1.00 68.11  ? 176  LYS A C   1 
ATOM   796   O O   . LYS A 1 167 ? 32.971  -4.984  91.503  1.00 67.26  ? 176  LYS A O   1 
ATOM   797   C CB  . LYS A 1 167 ? 33.033  -5.945  94.458  1.00 71.67  ? 176  LYS A CB  1 
ATOM   798   C CG  . LYS A 1 167 ? 33.164  -7.136  95.364  1.00 75.23  ? 176  LYS A CG  1 
ATOM   799   C CD  . LYS A 1 167 ? 32.186  -6.997  96.509  1.00 78.18  ? 176  LYS A CD  1 
ATOM   800   C CE  . LYS A 1 167 ? 31.752  -8.357  96.999  1.00 81.71  ? 176  LYS A CE  1 
ATOM   801   N NZ  . LYS A 1 167 ? 31.028  -8.263  98.291  1.00 83.96  ? 176  LYS A NZ  1 
ATOM   802   N N   . ALA A 1 168 ? 34.246  -3.516  92.656  1.00 66.97  ? 177  ALA A N   1 
ATOM   803   C CA  . ALA A 1 168 ? 33.992  -2.416  91.745  1.00 64.78  ? 177  ALA A CA  1 
ATOM   804   C C   . ALA A 1 168 ? 34.754  -2.661  90.463  1.00 63.92  ? 177  ALA A C   1 
ATOM   805   O O   . ALA A 1 168 ? 34.233  -2.394  89.372  1.00 62.94  ? 177  ALA A O   1 
ATOM   806   C CB  . ALA A 1 168 ? 34.392  -1.085  92.352  1.00 64.54  ? 177  ALA A CB  1 
ATOM   807   N N   . VAL A 1 169 ? 35.974  -3.182  90.586  1.00 64.43  ? 178  VAL A N   1 
ATOM   808   C CA  . VAL A 1 169 ? 36.794  -3.427  89.415  1.00 63.46  ? 178  VAL A CA  1 
ATOM   809   C C   . VAL A 1 169 ? 36.281  -4.629  88.675  1.00 63.82  ? 178  VAL A C   1 
ATOM   810   O O   . VAL A 1 169 ? 36.330  -4.662  87.456  1.00 63.14  ? 178  VAL A O   1 
ATOM   811   C CB  . VAL A 1 169 ? 38.272  -3.549  89.743  1.00 64.61  ? 178  VAL A CB  1 
ATOM   812   C CG1 . VAL A 1 169 ? 39.008  -4.238  88.637  1.00 64.28  ? 178  VAL A CG1 1 
ATOM   813   C CG2 . VAL A 1 169 ? 38.849  -2.179  89.931  1.00 63.58  ? 178  VAL A CG2 1 
ATOM   814   N N   . VAL A 1 170 ? 35.749  -5.600  89.400  1.00 65.17  ? 179  VAL A N   1 
ATOM   815   C CA  . VAL A 1 170 ? 35.086  -6.711  88.745  1.00 65.82  ? 179  VAL A CA  1 
ATOM   816   C C   . VAL A 1 170 ? 33.929  -6.199  87.899  1.00 63.77  ? 179  VAL A C   1 
ATOM   817   O O   . VAL A 1 170 ? 33.867  -6.483  86.711  1.00 63.02  ? 179  VAL A O   1 
ATOM   818   C CB  . VAL A 1 170 ? 34.604  -7.756  89.743  1.00 67.99  ? 179  VAL A CB  1 
ATOM   819   C CG1 . VAL A 1 170 ? 33.453  -8.588  89.163  1.00 68.66  ? 179  VAL A CG1 1 
ATOM   820   C CG2 . VAL A 1 170 ? 35.766  -8.645  90.169  1.00 70.45  ? 179  VAL A CG2 1 
ATOM   821   N N   . SER A 1 171 ? 33.028  -5.428  88.497  1.00 62.95  ? 180  SER A N   1 
ATOM   822   C CA  . SER A 1 171 ? 31.953  -4.848  87.722  0.75 61.49  ? 180  SER A CA  1 
ATOM   823   C C   . SER A 1 171 ? 32.504  -4.243  86.440  1.00 60.33  ? 180  SER A C   1 
ATOM   824   O O   . SER A 1 171 ? 32.146  -4.678  85.346  1.00 60.28  ? 180  SER A O   1 
ATOM   825   C CB  . SER A 1 171 ? 31.163  -3.828  88.528  0.75 60.72  ? 180  SER A CB  1 
ATOM   826   O OG  . SER A 1 171 ? 29.959  -4.410  88.983  0.75 61.27  ? 180  SER A OG  1 
ATOM   827   N N   . LEU A 1 172 ? 33.406  -3.280  86.558  1.00 59.93  ? 181  LEU A N   1 
ATOM   828   C CA  . LEU A 1 172 ? 33.876  -2.597  85.370  1.00 58.80  ? 181  LEU A CA  1 
ATOM   829   C C   . LEU A 1 172 ? 34.473  -3.562  84.353  1.00 59.64  ? 181  LEU A C   1 
ATOM   830   O O   . LEU A 1 172 ? 34.276  -3.398  83.149  1.00 58.66  ? 181  LEU A O   1 
ATOM   831   C CB  . LEU A 1 172 ? 34.868  -1.488  85.709  1.00 58.59  ? 181  LEU A CB  1 
ATOM   832   C CG  . LEU A 1 172 ? 35.087  -0.438  84.609  1.00 56.37  ? 181  LEU A CG  1 
ATOM   833   C CD1 . LEU A 1 172 ? 33.855  0.380   84.465  1.00 55.77  ? 181  LEU A CD1 1 
ATOM   834   C CD2 . LEU A 1 172 ? 36.237  0.479   84.916  1.00 55.48  ? 181  LEU A CD2 1 
ATOM   835   N N   . SER A 1 173 ? 35.194  -4.566  84.833  1.00 61.69  ? 182  SER A N   1 
ATOM   836   C CA  . SER A 1 173 ? 35.802  -5.537  83.939  1.00 62.85  ? 182  SER A CA  1 
ATOM   837   C C   . SER A 1 173 ? 34.749  -6.241  83.145  1.00 62.87  ? 182  SER A C   1 
ATOM   838   O O   . SER A 1 173 ? 34.863  -6.362  81.951  1.00 62.56  ? 182  SER A O   1 
ATOM   839   C CB  . SER A 1 173 ? 36.605  -6.559  84.705  1.00 65.02  ? 182  SER A CB  1 
ATOM   840   O OG  . SER A 1 173 ? 37.735  -5.939  85.278  1.00 65.86  ? 182  SER A OG  1 
ATOM   841   N N   . ASN A 1 174 ? 33.700  -6.684  83.805  1.00 63.96  ? 183  ASN A N   1 
ATOM   842   C CA  . ASN A 1 174 ? 32.630  -7.353  83.107  1.00 64.54  ? 183  ASN A CA  1 
ATOM   843   C C   . ASN A 1 174 ? 31.919  -6.427  82.153  1.00 62.35  ? 183  ASN A C   1 
ATOM   844   O O   . ASN A 1 174 ? 31.551  -6.840  81.045  1.00 62.41  ? 183  ASN A O   1 
ATOM   845   C CB  . ASN A 1 174 ? 31.672  -7.962  84.107  1.00 66.20  ? 183  ASN A CB  1 
ATOM   846   C CG  . ASN A 1 174 ? 32.348  -9.015  84.935  1.00 70.40  ? 183  ASN A CG  1 
ATOM   847   O OD1 . ASN A 1 174 ? 33.207  -9.733  84.419  1.00 73.78  ? 183  ASN A OD1 1 
ATOM   848   N ND2 . ASN A 1 174 ? 32.005  -9.102  86.222  1.00 72.15  ? 183  ASN A ND2 1 
ATOM   849   N N   . GLY A 1 175 ? 31.753  -5.171  82.570  1.00 60.68  ? 184  GLY A N   1 
ATOM   850   C CA  . GLY A 1 175 ? 31.233  -4.135  81.684  1.00 58.13  ? 184  GLY A CA  1 
ATOM   851   C C   . GLY A 1 175 ? 32.005  -4.112  80.376  1.00 57.12  ? 184  GLY A C   1 
ATOM   852   O O   . GLY A 1 175 ? 31.428  -4.281  79.296  1.00 56.58  ? 184  GLY A O   1 
ATOM   853   N N   . VAL A 1 176 ? 33.319  -3.933  80.482  1.00 57.01  ? 185  VAL A N   1 
ATOM   854   C CA  . VAL A 1 176 ? 34.187  -3.905  79.317  1.00 56.09  ? 185  VAL A CA  1 
ATOM   855   C C   . VAL A 1 176 ? 34.155  -5.228  78.554  1.00 57.00  ? 185  VAL A C   1 
ATOM   856   O O   . VAL A 1 176 ? 34.098  -5.244  77.319  1.00 56.18  ? 185  VAL A O   1 
ATOM   857   C CB  . VAL A 1 176 ? 35.609  -3.554  79.717  1.00 56.58  ? 185  VAL A CB  1 
ATOM   858   C CG1 . VAL A 1 176 ? 36.547  -3.833  78.582  1.00 56.70  ? 185  VAL A CG1 1 
ATOM   859   C CG2 . VAL A 1 176 ? 35.684  -2.103  80.119  1.00 55.04  ? 185  VAL A CG2 1 
ATOM   860   N N   . SER A 1 177 ? 34.163  -6.328  79.299  1.00 58.65  ? 186  SER A N   1 
ATOM   861   C CA  . SER A 1 177 ? 34.122  -7.639  78.706  0.75 59.97  ? 186  SER A CA  1 
ATOM   862   C C   . SER A 1 177 ? 32.971  -7.708  77.764  1.00 58.64  ? 186  SER A C   1 
ATOM   863   O O   . SER A 1 177 ? 33.080  -8.325  76.717  1.00 59.28  ? 186  SER A O   1 
ATOM   864   C CB  . SER A 1 177 ? 33.937  -8.713  79.751  0.75 62.21  ? 186  SER A CB  1 
ATOM   865   O OG  . SER A 1 177 ? 33.737  -9.960  79.110  0.75 64.29  ? 186  SER A OG  1 
ATOM   866   N N   . VAL A 1 178 ? 31.872  -7.063  78.133  1.00 57.08  ? 187  VAL A N   1 
ATOM   867   C CA  . VAL A 1 178 ? 30.693  -7.018  77.272  1.00 55.79  ? 187  VAL A CA  1 
ATOM   868   C C   . VAL A 1 178 ? 30.762  -6.018  76.110  1.00 53.99  ? 187  VAL A C   1 
ATOM   869   O O   . VAL A 1 178 ? 30.458  -6.375  74.964  1.00 53.71  ? 187  VAL A O   1 
ATOM   870   C CB  . VAL A 1 178 ? 29.440  -6.809  78.082  1.00 55.25  ? 187  VAL A CB  1 
ATOM   871   C CG1 . VAL A 1 178 ? 28.328  -6.282  77.216  1.00 53.35  ? 187  VAL A CG1 1 
ATOM   872   C CG2 . VAL A 1 178 ? 29.049  -8.109  78.671  1.00 57.12  ? 187  VAL A CG2 1 
ATOM   873   N N   . LEU A 1 179 ? 31.156  -4.779  76.416  1.00 52.95  ? 188  LEU A N   1 
ATOM   874   C CA  . LEU A 1 179 ? 31.315  -3.735  75.411  1.00 51.17  ? 188  LEU A CA  1 
ATOM   875   C C   . LEU A 1 179 ? 32.279  -4.211  74.344  1.00 51.52  ? 188  LEU A C   1 
ATOM   876   O O   . LEU A 1 179 ? 32.063  -3.998  73.165  1.00 50.53  ? 188  LEU A O   1 
ATOM   877   C CB  . LEU A 1 179 ? 31.796  -2.424  76.037  1.00 50.38  ? 188  LEU A CB  1 
ATOM   878   C CG  . LEU A 1 179 ? 31.781  -1.205  75.101  1.00 48.58  ? 188  LEU A CG  1 
ATOM   879   C CD1 . LEU A 1 179 ? 30.398  -0.571  74.971  1.00 47.42  ? 188  LEU A CD1 1 
ATOM   880   C CD2 . LEU A 1 179 ? 32.783  -0.167  75.551  1.00 48.19  ? 188  LEU A CD2 1 
ATOM   881   N N   . THR A 1 180 ? 33.331  -4.882  74.766  1.00 53.22  ? 189  THR A N   1 
ATOM   882   C CA  . THR A 1 180 ? 34.166  -5.585  73.834  1.00 54.35  ? 189  THR A CA  1 
ATOM   883   C C   . THR A 1 180 ? 33.353  -6.604  73.055  1.00 55.01  ? 189  THR A C   1 
ATOM   884   O O   . THR A 1 180 ? 33.207  -6.460  71.848  1.00 54.11  ? 189  THR A O   1 
ATOM   885   C CB  . THR A 1 180 ? 35.286  -6.256  74.562  1.00 56.29  ? 189  THR A CB  1 
ATOM   886   O OG1 . THR A 1 180 ? 36.163  -5.243  75.062  1.00 55.96  ? 189  THR A OG1 1 
ATOM   887   C CG2 . THR A 1 180 ? 36.039  -7.176  73.634  1.00 57.91  ? 189  THR A CG2 1 
ATOM   888   N N   . SER A 1 181 ? 32.808  -7.607  73.745  1.00 56.73  ? 190  SER A N   1 
ATOM   889   C CA  . SER A 1 181 ? 31.974  -8.615  73.115  0.25 57.67  ? 190  SER A CA  1 
ATOM   890   C C   . SER A 1 181 ? 31.065  -8.016  72.055  1.00 56.18  ? 190  SER A C   1 
ATOM   891   O O   . SER A 1 181 ? 30.784  -8.684  71.068  1.00 56.94  ? 190  SER A O   1 
ATOM   892   C CB  . SER A 1 181 ? 31.133  -9.358  74.147  0.25 58.85  ? 190  SER A CB  1 
ATOM   893   O OG  . SER A 1 181 ? 30.304  -10.319 73.521  0.25 59.45  ? 190  SER A OG  1 
ATOM   894   N N   . LYS A 1 182 ? 30.624  -6.765  72.240  1.00 54.47  ? 191  LYS A N   1 
ATOM   895   C CA  . LYS A 1 182 ? 29.708  -6.100  71.298  1.00 52.71  ? 191  LYS A CA  1 
ATOM   896   C C   . LYS A 1 182 ? 30.367  -5.381  70.147  1.00 51.39  ? 191  LYS A C   1 
ATOM   897   O O   . LYS A 1 182 ? 29.826  -5.341  69.046  1.00 50.79  ? 191  LYS A O   1 
ATOM   898   C CB  . LYS A 1 182 ? 28.824  -5.107  72.017  1.00 51.50  ? 191  LYS A CB  1 
ATOM   899   C CG  . LYS A 1 182 ? 27.617  -5.739  72.629  1.00 53.94  ? 191  LYS A CG  1 
ATOM   900   C CD  . LYS A 1 182 ? 26.555  -6.083  71.600  1.00 56.21  ? 191  LYS A CD  1 
ATOM   901   C CE  . LYS A 1 182 ? 26.350  -7.581  71.479  1.00 60.44  ? 191  LYS A CE  1 
ATOM   902   N NZ  . LYS A 1 182 ? 25.073  -7.885  70.747  1.00 62.41  ? 191  LYS A NZ  1 
ATOM   903   N N   . VAL A 1 183 ? 31.518  -4.774  70.402  1.00 51.15  ? 192  VAL A N   1 
ATOM   904   C CA  . VAL A 1 183 ? 32.202  -4.030  69.360  1.00 49.76  ? 192  VAL A CA  1 
ATOM   905   C C   . VAL A 1 183 ? 32.639  -5.031  68.328  1.00 50.79  ? 192  VAL A C   1 
ATOM   906   O O   . VAL A 1 183 ? 32.647  -4.743  67.147  1.00 50.23  ? 192  VAL A O   1 
ATOM   907   C CB  . VAL A 1 183 ? 33.373  -3.161  69.896  1.00 49.54  ? 192  VAL A CB  1 
ATOM   908   C CG1 . VAL A 1 183 ? 34.440  -2.944  68.862  1.00 49.00  ? 192  VAL A CG1 1 
ATOM   909   C CG2 . VAL A 1 183 ? 32.856  -1.828  70.317  1.00 48.02  ? 192  VAL A CG2 1 
ATOM   910   N N   . LEU A 1 184 ? 32.955  -6.232  68.756  1.00 52.74  ? 193  LEU A N   1 
ATOM   911   C CA  . LEU A 1 184 ? 33.272  -7.227  67.780  1.00 54.33  ? 193  LEU A CA  1 
ATOM   912   C C   . LEU A 1 184 ? 32.100  -7.373  66.853  1.00 53.87  ? 193  LEU A C   1 
ATOM   913   O O   . LEU A 1 184 ? 32.250  -7.255  65.649  1.00 53.71  ? 193  LEU A O   1 
ATOM   914   C CB  . LEU A 1 184 ? 33.574  -8.563  68.426  1.00 56.90  ? 193  LEU A CB  1 
ATOM   915   C CG  . LEU A 1 184 ? 33.952  -9.685  67.453  1.00 58.65  ? 193  LEU A CG  1 
ATOM   916   C CD1 . LEU A 1 184 ? 35.433  -9.610  67.104  1.00 58.84  ? 193  LEU A CD1 1 
ATOM   917   C CD2 . LEU A 1 184 ? 33.593  -11.057 68.019  1.00 61.65  ? 193  LEU A CD2 1 
ATOM   918   N N   . ASP A 1 185 ? 30.927  -7.607  67.414  1.00 54.38  ? 194  ASP A N   1 
ATOM   919   C CA  . ASP A 1 185 ? 29.725  -7.796  66.607  1.00 54.47  ? 194  ASP A CA  1 
ATOM   920   C C   . ASP A 1 185 ? 29.462  -6.661  65.612  1.00 52.22  ? 194  ASP A C   1 
ATOM   921   O O   . ASP A 1 185 ? 29.101  -6.919  64.456  1.00 51.87  ? 194  ASP A O   1 
ATOM   922   C CB  . ASP A 1 185 ? 28.525  -8.028  67.520  1.00 55.19  ? 194  ASP A CB  1 
ATOM   923   C CG  . ASP A 1 185 ? 28.719  -9.233  68.430  1.00 58.91  ? 194  ASP A CG  1 
ATOM   924   O OD1 . ASP A 1 185 ? 29.737  -9.946  68.243  1.00 61.33  ? 194  ASP A OD1 1 
ATOM   925   O OD2 . ASP A 1 185 ? 27.867  -9.472  69.323  1.00 60.72  ? 194  ASP A OD2 1 
ATOM   926   N N   . LEU A 1 186 ? 29.672  -5.421  66.059  1.00 50.76  ? 195  LEU A N   1 
ATOM   927   C CA  . LEU A 1 186 ? 29.535  -4.267  65.189  1.00 48.84  ? 195  LEU A CA  1 
ATOM   928   C C   . LEU A 1 186 ? 30.464  -4.398  64.006  1.00 49.01  ? 195  LEU A C   1 
ATOM   929   O O   . LEU A 1 186 ? 30.032  -4.300  62.868  1.00 48.48  ? 195  LEU A O   1 
ATOM   930   C CB  . LEU A 1 186 ? 29.824  -2.956  65.912  1.00 47.82  ? 195  LEU A CB  1 
ATOM   931   C CG  . LEU A 1 186 ? 28.804  -1.826  65.665  1.00 45.96  ? 195  LEU A CG  1 
ATOM   932   C CD1 . LEU A 1 186 ? 29.464  -0.459  65.560  1.00 44.30  ? 195  LEU A CD1 1 
ATOM   933   C CD2 . LEU A 1 186 ? 27.950  -2.072  64.432  1.00 45.16  ? 195  LEU A CD2 1 
ATOM   934   N N   . LYS A 1 187 ? 31.740  -4.623  64.261  1.00 50.14  ? 196  LYS A N   1 
ATOM   935   C CA  . LYS A 1 187 ? 32.639  -4.928  63.168  1.00 50.96  ? 196  LYS A CA  1 
ATOM   936   C C   . LYS A 1 187 ? 32.054  -6.057  62.335  1.00 52.14  ? 196  LYS A C   1 
ATOM   937   O O   . LYS A 1 187 ? 31.884  -5.909  61.133  1.00 51.70  ? 196  LYS A O   1 
ATOM   938   C CB  . LYS A 1 187 ? 34.034  -5.285  63.673  1.00 52.47  ? 196  LYS A CB  1 
ATOM   939   C CG  . LYS A 1 187 ? 34.956  -5.941  62.655  1.00 52.97  ? 196  LYS A CG  1 
ATOM   940   C CD  . LYS A 1 187 ? 34.862  -7.440  62.711  1.00 55.01  ? 196  LYS A CD  1 
ATOM   941   C CE  . LYS A 1 187 ? 35.902  -8.070  61.843  1.00 57.48  ? 196  LYS A CE  1 
ATOM   942   N NZ  . LYS A 1 187 ? 35.691  -9.537  61.761  1.00 60.59  ? 196  LYS A NZ  1 
ATOM   943   N N   . ASN A 1 188 ? 31.700  -7.164  62.974  1.00 54.09  ? 197  ASN A N   1 
ATOM   944   C CA  . ASN A 1 188 ? 31.256  -8.329  62.230  1.00 55.93  ? 197  ASN A CA  1 
ATOM   945   C C   . ASN A 1 188 ? 30.030  -8.142  61.369  1.00 55.05  ? 197  ASN A C   1 
ATOM   946   O O   . ASN A 1 188 ? 29.942  -8.748  60.295  1.00 55.97  ? 197  ASN A O   1 
ATOM   947   C CB  . ASN A 1 188 ? 31.124  -9.540  63.122  1.00 58.12  ? 197  ASN A CB  1 
ATOM   948   C CG  . ASN A 1 188 ? 32.398  -10.353 63.145  1.00 61.11  ? 197  ASN A CG  1 
ATOM   949   O OD1 . ASN A 1 188 ? 33.000  -10.566 64.193  1.00 63.21  ? 197  ASN A OD1 1 
ATOM   950   N ND2 . ASN A 1 188 ? 32.839  -10.782 61.973  1.00 62.47  ? 197  ASN A ND2 1 
ATOM   951   N N   . TYR A 1 189 ? 29.098  -7.304  61.817  1.00 53.66  ? 198  TYR A N   1 
ATOM   952   C CA  . TYR A 1 189 ? 28.015  -6.860  60.935  1.00 52.32  ? 198  TYR A CA  1 
ATOM   953   C C   . TYR A 1 189 ? 28.583  -6.204  59.685  1.00 50.69  ? 198  TYR A C   1 
ATOM   954   O O   . TYR A 1 189 ? 28.426  -6.721  58.591  1.00 51.09  ? 198  TYR A O   1 
ATOM   955   C CB  . TYR A 1 189 ? 27.081  -5.875  61.618  1.00 51.30  ? 198  TYR A CB  1 
ATOM   956   C CG  . TYR A 1 189 ? 25.747  -5.795  60.913  1.00 52.48  ? 198  TYR A CG  1 
ATOM   957   C CD1 . TYR A 1 189 ? 24.794  -6.828  61.069  1.00 56.60  ? 198  TYR A CD1 1 
ATOM   958   C CD2 . TYR A 1 189 ? 25.428  -4.715  60.078  1.00 51.58  ? 198  TYR A CD2 1 
ATOM   959   C CE1 . TYR A 1 189 ? 23.533  -6.792  60.417  1.00 57.43  ? 198  TYR A CE1 1 
ATOM   960   C CE2 . TYR A 1 189 ? 24.167  -4.658  59.420  1.00 53.01  ? 198  TYR A CE2 1 
ATOM   961   C CZ  . TYR A 1 189 ? 23.224  -5.708  59.592  1.00 55.71  ? 198  TYR A CZ  1 
ATOM   962   O OH  . TYR A 1 189 ? 21.982  -5.684  58.958  1.00 55.32  ? 198  TYR A OH  1 
ATOM   963   N N   . ILE A 1 190 ? 29.258  -5.080  59.851  1.00 49.15  ? 199  ILE A N   1 
ATOM   964   C CA  . ILE A 1 190 ? 29.928  -4.463  58.738  1.00 48.23  ? 199  ILE A CA  1 
ATOM   965   C C   . ILE A 1 190 ? 30.639  -5.458  57.820  1.00 50.11  ? 199  ILE A C   1 
ATOM   966   O O   . ILE A 1 190 ? 30.275  -5.580  56.654  1.00 49.84  ? 199  ILE A O   1 
ATOM   967   C CB  . ILE A 1 190 ? 30.895  -3.431  59.219  1.00 47.30  ? 199  ILE A CB  1 
ATOM   968   C CG1 . ILE A 1 190 ? 30.130  -2.163  59.543  1.00 45.21  ? 199  ILE A CG1 1 
ATOM   969   C CG2 . ILE A 1 190 ? 31.899  -3.146  58.151  1.00 46.96  ? 199  ILE A CG2 1 
ATOM   970   C CD1 . ILE A 1 190 ? 30.850  -1.258  60.446  1.00 44.61  ? 199  ILE A CD1 1 
ATOM   971   N N   . ASP A 1 191 ? 31.628  -6.181  58.338  1.00 52.50  ? 200  ASP A N   1 
ATOM   972   C CA  . ASP A 1 191 ? 32.458  -7.048  57.480  1.00 54.85  ? 200  ASP A CA  1 
ATOM   973   C C   . ASP A 1 191 ? 31.656  -8.176  56.851  1.00 55.76  ? 200  ASP A C   1 
ATOM   974   O O   . ASP A 1 191 ? 31.852  -8.498  55.685  1.00 56.19  ? 200  ASP A O   1 
ATOM   975   C CB  . ASP A 1 191 ? 33.700  -7.622  58.219  1.00 57.26  ? 200  ASP A CB  1 
ATOM   976   C CG  . ASP A 1 191 ? 34.606  -8.518  57.310  1.00 60.87  ? 200  ASP A CG  1 
ATOM   977   O OD1 . ASP A 1 191 ? 34.794  -8.198  56.100  1.00 62.12  ? 200  ASP A OD1 1 
ATOM   978   O OD2 . ASP A 1 191 ? 35.139  -9.543  57.822  1.00 63.88  ? 200  ASP A OD2 1 
ATOM   979   N N   . LYS A 1 192 ? 30.760  -8.787  57.603  1.00 56.38  ? 201  LYS A N   1 
ATOM   980   C CA  . LYS A 1 192 ? 30.211  -10.021 57.111  1.00 58.37  ? 201  LYS A CA  1 
ATOM   981   C C   . LYS A 1 192 ? 28.742  -9.950  56.757  1.00 57.56  ? 201  LYS A C   1 
ATOM   982   O O   . LYS A 1 192 ? 28.147  -10.938 56.366  1.00 58.94  ? 201  LYS A O   1 
ATOM   983   C CB  . LYS A 1 192 ? 30.573  -11.155 58.062  1.00 60.91  ? 201  LYS A CB  1 
ATOM   984   C CG  . LYS A 1 192 ? 32.092  -11.359 58.120  1.00 63.14  ? 201  LYS A CG  1 
ATOM   985   C CD  . LYS A 1 192 ? 32.522  -12.618 58.858  1.00 69.03  ? 201  LYS A CD  1 
ATOM   986   C CE  . LYS A 1 192 ? 34.058  -12.624 59.049  1.00 72.38  ? 201  LYS A CE  1 
ATOM   987   N NZ  . LYS A 1 192 ? 34.568  -13.511 60.168  1.00 76.60  ? 201  LYS A NZ  1 
ATOM   988   N N   . GLN A 1 193 ? 28.173  -8.762  56.831  1.00 55.80  ? 202  GLN A N   1 
ATOM   989   C CA  . GLN A 1 193 ? 26.761  -8.585  56.530  1.00 55.35  ? 202  GLN A CA  1 
ATOM   990   C C   . GLN A 1 193 ? 26.564  -7.513  55.483  1.00 52.81  ? 202  GLN A C   1 
ATOM   991   O O   . GLN A 1 193 ? 26.141  -7.807  54.368  1.00 52.92  ? 202  GLN A O   1 
ATOM   992   C CB  . GLN A 1 193 ? 26.012  -8.199  57.800  1.00 55.46  ? 202  GLN A CB  1 
ATOM   993   C CG  . GLN A 1 193 ? 25.772  -9.356  58.741  1.00 60.57  ? 202  GLN A CG  1 
ATOM   994   C CD  . GLN A 1 193 ? 24.589  -10.204 58.282  1.00 65.94  ? 202  GLN A CD  1 
ATOM   995   O OE1 . GLN A 1 193 ? 23.572  -9.662  57.821  1.00 66.89  ? 202  GLN A OE1 1 
ATOM   996   N NE2 . GLN A 1 193 ? 24.715  -11.536 58.394  1.00 69.36  ? 202  GLN A NE2 1 
ATOM   997   N N   . LEU A 1 194 ? 26.889  -6.276  55.864  1.00 50.56  ? 203  LEU A N   1 
ATOM   998   C CA  . LEU A 1 194 ? 26.735  -5.103  55.019  1.00 47.96  ? 203  LEU A CA  1 
ATOM   999   C C   . LEU A 1 194 ? 27.720  -5.129  53.875  1.00 47.95  ? 203  LEU A C   1 
ATOM   1000  O O   . LEU A 1 194 ? 27.329  -5.095  52.711  1.00 47.36  ? 203  LEU A O   1 
ATOM   1001  C CB  . LEU A 1 194 ? 26.957  -3.832  55.842  1.00 46.33  ? 203  LEU A CB  1 
ATOM   1002  C CG  . LEU A 1 194 ? 26.982  -2.520  55.049  1.00 43.97  ? 203  LEU A CG  1 
ATOM   1003  C CD1 . LEU A 1 194 ? 25.616  -1.888  55.011  1.00 43.17  ? 203  LEU A CD1 1 
ATOM   1004  C CD2 . LEU A 1 194 ? 27.956  -1.547  55.649  1.00 43.21  ? 203  LEU A CD2 1 
ATOM   1005  N N   . LEU A 1 195 ? 28.998  -5.204  54.229  1.00 48.70  ? 204  LEU A N   1 
ATOM   1006  C CA  . LEU A 1 195 ? 30.066  -5.007  53.281  1.00 48.82  ? 204  LEU A CA  1 
ATOM   1007  C C   . LEU A 1 195 ? 29.919  -5.870  52.045  1.00 49.73  ? 204  LEU A C   1 
ATOM   1008  O O   . LEU A 1 195 ? 30.164  -5.377  50.959  1.00 49.54  ? 204  LEU A O   1 
ATOM   1009  C CB  . LEU A 1 195 ? 31.427  -5.204  53.922  1.00 50.03  ? 204  LEU A CB  1 
ATOM   1010  C CG  . LEU A 1 195 ? 32.600  -4.546  53.210  1.00 50.25  ? 204  LEU A CG  1 
ATOM   1011  C CD1 . LEU A 1 195 ? 32.614  -3.081  53.545  1.00 47.88  ? 204  LEU A CD1 1 
ATOM   1012  C CD2 . LEU A 1 195 ? 33.929  -5.212  53.604  1.00 53.79  ? 204  LEU A CD2 1 
ATOM   1013  N N   . PRO A 1 196 ? 29.500  -7.144  52.182  1.00 51.32  ? 205  PRO A N   1 
ATOM   1014  C CA  . PRO A 1 196 ? 29.259  -7.938  50.966  1.00 52.25  ? 205  PRO A CA  1 
ATOM   1015  C C   . PRO A 1 196 ? 28.214  -7.316  50.024  1.00 50.68  ? 205  PRO A C   1 
ATOM   1016  O O   . PRO A 1 196 ? 28.391  -7.291  48.794  1.00 50.70  ? 205  PRO A O   1 
ATOM   1017  C CB  . PRO A 1 196 ? 28.725  -9.258  51.510  1.00 54.02  ? 205  PRO A CB  1 
ATOM   1018  C CG  . PRO A 1 196 ? 29.320  -9.366  52.828  1.00 55.01  ? 205  PRO A CG  1 
ATOM   1019  C CD  . PRO A 1 196 ? 29.378  -7.973  53.387  1.00 52.88  ? 205  PRO A CD  1 
ATOM   1020  N N   . ILE A 1 197 ? 27.138  -6.797  50.591  1.00 49.38  ? 206  ILE A N   1 
ATOM   1021  C CA  . ILE A 1 197 ? 26.070  -6.309  49.738  1.00 48.03  ? 206  ILE A CA  1 
ATOM   1022  C C   . ILE A 1 197 ? 26.251  -4.849  49.382  1.00 45.55  ? 206  ILE A C   1 
ATOM   1023  O O   . ILE A 1 197 ? 25.474  -4.289  48.624  1.00 44.09  ? 206  ILE A O   1 
ATOM   1024  C CB  . ILE A 1 197 ? 24.640  -6.648  50.272  1.00 48.31  ? 206  ILE A CB  1 
ATOM   1025  C CG1 . ILE A 1 197 ? 23.992  -5.466  50.976  1.00 46.92  ? 206  ILE A CG1 1 
ATOM   1026  C CG2 . ILE A 1 197 ? 24.629  -7.961  51.113  1.00 51.16  ? 206  ILE A CG2 1 
ATOM   1027  C CD1 . ILE A 1 197 ? 22.460  -5.531  50.865  1.00 48.72  ? 206  ILE A CD1 1 
ATOM   1028  N N   . VAL A 1 198 ? 27.286  -4.233  49.921  1.00 45.39  ? 207  VAL A N   1 
ATOM   1029  C CA  . VAL A 1 198 ? 27.664  -2.967  49.389  1.00 44.42  ? 207  VAL A CA  1 
ATOM   1030  C C   . VAL A 1 198 ? 28.334  -3.337  48.112  1.00 45.38  ? 207  VAL A C   1 
ATOM   1031  O O   . VAL A 1 198 ? 27.831  -3.025  47.034  1.00 45.09  ? 207  VAL A O   1 
ATOM   1032  C CB  . VAL A 1 198 ? 28.641  -2.175  50.266  1.00 44.05  ? 207  VAL A CB  1 
ATOM   1033  C CG1 . VAL A 1 198 ? 29.254  -1.009  49.476  1.00 42.67  ? 207  VAL A CG1 1 
ATOM   1034  C CG2 . VAL A 1 198 ? 27.929  -1.641  51.471  1.00 44.02  ? 207  VAL A CG2 1 
ATOM   1035  N N   . ASN A 1 199 ? 29.456  -4.026  48.200  1.00 47.18  ? 208  ASN A N   1 
ATOM   1036  C CA  . ASN A 1 199 ? 30.172  -4.222  46.966  1.00 48.51  ? 208  ASN A CA  1 
ATOM   1037  C C   . ASN A 1 199 ? 29.567  -5.316  46.060  1.00 49.81  ? 208  ASN A C   1 
ATOM   1038  O O   . ASN A 1 199 ? 30.146  -5.722  45.046  1.00 50.89  ? 208  ASN A O   1 
ATOM   1039  C CB  . ASN A 1 199 ? 31.719  -4.168  47.117  1.00 49.58  ? 208  ASN A CB  1 
ATOM   1040  C CG  . ASN A 1 199 ? 32.284  -5.264  48.003  1.00 51.49  ? 208  ASN A CG  1 
ATOM   1041  O OD1 . ASN A 1 199 ? 31.562  -6.134  48.488  1.00 52.90  ? 208  ASN A OD1 1 
ATOM   1042  N ND2 . ASN A 1 199 ? 33.594  -5.227  48.211  1.00 51.95  ? 208  ASN A ND2 1 
ATOM   1043  N N   . LYS A 1 200 ? 28.360  -5.750  46.401  1.00 49.90  ? 209  LYS A N   1 
ATOM   1044  C CA  . LYS A 1 200 ? 27.581  -6.495  45.431  1.00 50.80  ? 209  LYS A CA  1 
ATOM   1045  C C   . LYS A 1 200 ? 26.921  -5.506  44.498  1.00 48.58  ? 209  LYS A C   1 
ATOM   1046  O O   . LYS A 1 200 ? 26.984  -5.647  43.282  1.00 48.38  ? 209  LYS A O   1 
ATOM   1047  C CB  . LYS A 1 200 ? 26.549  -7.379  46.114  1.00 52.02  ? 209  LYS A CB  1 
ATOM   1048  C CG  . LYS A 1 200 ? 26.581  -8.793  45.563  1.00 55.64  ? 209  LYS A CG  1 
ATOM   1049  C CD  . LYS A 1 200 ? 26.408  -9.841  46.637  1.00 59.33  ? 209  LYS A CD  1 
ATOM   1050  C CE  . LYS A 1 200 ? 24.986  -10.358 46.647  1.00 60.90  ? 209  LYS A CE  1 
ATOM   1051  N NZ  . LYS A 1 200 ? 24.542  -10.608 48.048  1.00 63.02  ? 209  LYS A NZ  1 
ATOM   1052  N N   . GLN A 1 201 ? 26.298  -4.501  45.103  1.00 46.85  ? 210  GLN A N   1 
ATOM   1053  C CA  . GLN A 1 201 ? 25.742  -3.375  44.389  1.00 45.06  ? 210  GLN A CA  1 
ATOM   1054  C C   . GLN A 1 201 ? 26.807  -2.772  43.518  1.00 45.00  ? 210  GLN A C   1 
ATOM   1055  O O   . GLN A 1 201 ? 26.550  -2.487  42.343  1.00 44.53  ? 210  GLN A O   1 
ATOM   1056  C CB  . GLN A 1 201 ? 25.284  -2.290  45.345  1.00 43.42  ? 210  GLN A CB  1 
ATOM   1057  C CG  . GLN A 1 201 ? 24.076  -2.598  46.195  1.00 44.09  ? 210  GLN A CG  1 
ATOM   1058  C CD  . GLN A 1 201 ? 23.791  -1.461  47.182  1.00 44.22  ? 210  GLN A CD  1 
ATOM   1059  O OE1 . GLN A 1 201 ? 24.667  -0.628  47.461  1.00 43.99  ? 210  GLN A OE1 1 
ATOM   1060  N NE2 . GLN A 1 201 ? 22.571  -1.422  47.711  1.00 43.88  ? 210  GLN A NE2 1 
ATOM   1061  N N   . SER A 1 202 ? 27.999  -2.567  44.085  1.00 45.76  ? 211  SER A N   1 
ATOM   1062  C CA  . SER A 1 202 ? 29.082  -1.953  43.331  1.00 46.11  ? 211  SER A CA  1 
ATOM   1063  C C   . SER A 1 202 ? 29.241  -2.695  42.041  1.00 47.41  ? 211  SER A C   1 
ATOM   1064  O O   . SER A 1 202 ? 29.479  -2.087  40.999  1.00 46.77  ? 211  SER A O   1 
ATOM   1065  C CB  . SER A 1 202 ? 30.390  -1.966  44.091  1.00 47.02  ? 211  SER A CB  1 
ATOM   1066  O OG  . SER A 1 202 ? 30.393  -0.947  45.059  1.00 46.67  ? 211  SER A OG  1 
ATOM   1067  N N   . CYS A 1 203 ? 29.062  -4.011  42.100  1.00 49.45  ? 212  CYS A N   1 
ATOM   1068  C CA  . CYS A 1 203 ? 29.158  -4.793  40.889  1.00 51.07  ? 212  CYS A CA  1 
ATOM   1069  C C   . CYS A 1 203 ? 28.050  -4.504  39.874  1.00 49.16  ? 212  CYS A C   1 
ATOM   1070  O O   . CYS A 1 203 ? 28.315  -4.126  38.721  1.00 48.08  ? 212  CYS A O   1 
ATOM   1071  C CB  . CYS A 1 203 ? 29.191  -6.276  41.180  1.00 53.84  ? 212  CYS A CB  1 
ATOM   1072  S SG  . CYS A 1 203 ? 29.566  -6.947  39.600  1.00 60.06  ? 212  CYS A SG  1 
ATOM   1073  N N   . SER A 1 204 ? 26.815  -4.719  40.327  1.00 48.46  ? 213  SER A N   1 
ATOM   1074  C CA  . SER A 1 204 ? 25.623  -4.516  39.510  1.00 47.26  ? 213  SER A CA  1 
ATOM   1075  C C   . SER A 1 204 ? 25.653  -3.173  38.837  1.00 44.86  ? 213  SER A C   1 
ATOM   1076  O O   . SER A 1 204 ? 25.360  -3.082  37.646  1.00 45.05  ? 213  SER A O   1 
ATOM   1077  C CB  . SER A 1 204 ? 24.355  -4.631  40.342  1.00 47.07  ? 213  SER A CB  1 
ATOM   1078  O OG  . SER A 1 204 ? 24.243  -5.935  40.887  1.00 50.35  ? 213  SER A OG  1 
ATOM   1079  N N   . ILE A 1 205 ? 26.020  -2.137  39.583  1.00 42.78  ? 214  ILE A N   1 
ATOM   1080  C CA  . ILE A 1 205 ? 26.223  -0.834  38.983  1.00 40.65  ? 214  ILE A CA  1 
ATOM   1081  C C   . ILE A 1 205 ? 27.256  -0.862  37.837  1.00 41.06  ? 214  ILE A C   1 
ATOM   1082  O O   . ILE A 1 205 ? 26.958  -0.392  36.725  1.00 40.37  ? 214  ILE A O   1 
ATOM   1083  C CB  . ILE A 1 205 ? 26.587  0.167   40.040  1.00 39.67  ? 214  ILE A CB  1 
ATOM   1084  C CG1 . ILE A 1 205 ? 25.394  0.350   40.945  1.00 38.91  ? 214  ILE A CG1 1 
ATOM   1085  C CG2 . ILE A 1 205 ? 26.992  1.500   39.428  1.00 38.05  ? 214  ILE A CG2 1 
ATOM   1086  C CD1 . ILE A 1 205 ? 25.779  0.897   42.238  1.00 40.05  ? 214  ILE A CD1 1 
ATOM   1087  N N   . SER A 1 206 ? 28.438  -1.435  38.089  1.00 41.98  ? 215  SER A N   1 
ATOM   1088  C CA  . SER A 1 206 ? 29.456  -1.567  37.053  1.00 42.44  ? 215  SER A CA  1 
ATOM   1089  C C   . SER A 1 206 ? 28.874  -2.191  35.795  1.00 42.47  ? 215  SER A C   1 
ATOM   1090  O O   . SER A 1 206 ? 29.185  -1.769  34.679  1.00 42.18  ? 215  SER A O   1 
ATOM   1091  C CB  . SER A 1 206 ? 30.626  -2.412  37.543  1.00 44.69  ? 215  SER A CB  1 
ATOM   1092  O OG  . SER A 1 206 ? 31.679  -2.482  36.576  1.00 46.26  ? 215  SER A OG  1 
ATOM   1093  N N   . ASN A 1 207 ? 28.019  -3.192  35.986  1.00 42.58  ? 216  ASN A N   1 
ATOM   1094  C CA  . ASN A 1 207 ? 27.306  -3.815  34.869  1.00 42.50  ? 216  ASN A CA  1 
ATOM   1095  C C   . ASN A 1 207 ? 26.380  -2.867  34.133  1.00 40.04  ? 216  ASN A C   1 
ATOM   1096  O O   . ASN A 1 207 ? 26.585  -2.590  32.945  1.00 39.98  ? 216  ASN A O   1 
ATOM   1097  C CB  . ASN A 1 207 ? 26.529  -5.020  35.349  1.00 43.83  ? 216  ASN A CB  1 
ATOM   1098  C CG  . ASN A 1 207 ? 27.409  -6.049  35.952  1.00 46.80  ? 216  ASN A CG  1 
ATOM   1099  O OD1 . ASN A 1 207 ? 28.648  -5.953  35.925  1.00 48.36  ? 216  ASN A OD1 1 
ATOM   1100  N ND2 . ASN A 1 207 ? 26.787  -7.059  36.501  1.00 49.40  ? 216  ASN A ND2 1 
ATOM   1101  N N   . ILE A 1 208 ? 25.371  -2.372  34.836  1.00 37.81  ? 217  ILE A N   1 
ATOM   1102  C CA  . ILE A 1 208 ? 24.492  -1.402  34.268  1.00 35.75  ? 217  ILE A CA  1 
ATOM   1103  C C   . ILE A 1 208 ? 25.269  -0.360  33.500  1.00 35.06  ? 217  ILE A C   1 
ATOM   1104  O O   . ILE A 1 208 ? 25.054  -0.182  32.306  1.00 34.71  ? 217  ILE A O   1 
ATOM   1105  C CB  . ILE A 1 208 ? 23.732  -0.737  35.337  1.00 34.53  ? 217  ILE A CB  1 
ATOM   1106  C CG1 . ILE A 1 208 ? 22.807  -1.769  35.952  1.00 35.74  ? 217  ILE A CG1 1 
ATOM   1107  C CG2 . ILE A 1 208 ? 22.929  0.429   34.762  1.00 33.29  ? 217  ILE A CG2 1 
ATOM   1108  C CD1 . ILE A 1 208 ? 22.250  -1.335  37.279  1.00 35.48  ? 217  ILE A CD1 1 
ATOM   1109  N N   . GLU A 1 209 ? 26.195  0.311   34.167  1.00 35.19  ? 218  GLU A N   1 
ATOM   1110  C CA  . GLU A 1 209 ? 26.979  1.313   33.489  1.00 35.50  ? 218  GLU A CA  1 
ATOM   1111  C C   . GLU A 1 209 ? 27.515  0.759   32.192  1.00 36.02  ? 218  GLU A C   1 
ATOM   1112  O O   . GLU A 1 209 ? 27.323  1.336   31.118  1.00 35.46  ? 218  GLU A O   1 
ATOM   1113  C CB  . GLU A 1 209 ? 28.105  1.791   34.379  1.00 36.17  ? 218  GLU A CB  1 
ATOM   1114  C CG  . GLU A 1 209 ? 27.608  2.785   35.414  1.00 39.21  ? 218  GLU A CG  1 
ATOM   1115  C CD  . GLU A 1 209 ? 28.631  3.110   36.533  1.00 45.29  ? 218  GLU A CD  1 
ATOM   1116  O OE1 . GLU A 1 209 ? 29.602  2.317   36.737  1.00 47.95  ? 218  GLU A OE1 1 
ATOM   1117  O OE2 . GLU A 1 209 ? 28.435  4.166   37.218  1.00 46.18  ? 218  GLU A OE2 1 
ATOM   1118  N N   . THR A 1 210 ? 28.158  -0.390  32.292  1.00 37.27  ? 219  THR A N   1 
ATOM   1119  C CA  . THR A 1 210 ? 28.758  -0.995  31.136  1.00 37.95  ? 219  THR A CA  1 
ATOM   1120  C C   . THR A 1 210 ? 27.710  -1.122  30.036  1.00 37.01  ? 219  THR A C   1 
ATOM   1121  O O   . THR A 1 210 ? 27.933  -0.638  28.924  1.00 37.12  ? 219  THR A O   1 
ATOM   1122  C CB  . THR A 1 210 ? 29.398  -2.332  31.486  1.00 40.23  ? 219  THR A CB  1 
ATOM   1123  O OG1 . THR A 1 210 ? 30.432  -2.120  32.466  1.00 40.73  ? 219  THR A OG1 1 
ATOM   1124  C CG2 . THR A 1 210 ? 29.992  -2.967  30.246  1.00 41.59  ? 219  THR A CG2 1 
ATOM   1125  N N   . VAL A 1 211 ? 26.563  -1.723  30.347  1.00 35.87  ? 220  VAL A N   1 
ATOM   1126  C CA  . VAL A 1 211 ? 25.508  -1.855  29.347  1.00 34.53  ? 220  VAL A CA  1 
ATOM   1127  C C   . VAL A 1 211 ? 25.154  -0.526  28.710  1.00 32.53  ? 220  VAL A C   1 
ATOM   1128  O O   . VAL A 1 211 ? 25.365  -0.331  27.521  1.00 32.61  ? 220  VAL A O   1 
ATOM   1129  C CB  . VAL A 1 211 ? 24.260  -2.492  29.897  1.00 34.47  ? 220  VAL A CB  1 
ATOM   1130  C CG1 . VAL A 1 211 ? 23.068  -2.179  29.011  1.00 32.96  ? 220  VAL A CG1 1 
ATOM   1131  C CG2 . VAL A 1 211 ? 24.473  -3.977  29.985  1.00 36.54  ? 220  VAL A CG2 1 
ATOM   1132  N N   . ILE A 1 212 ? 24.639  0.403   29.488  1.00 30.78  ? 221  ILE A N   1 
ATOM   1133  C CA  . ILE A 1 212 ? 24.348  1.708   28.940  1.00 29.28  ? 221  ILE A CA  1 
ATOM   1134  C C   . ILE A 1 212 ? 25.440  2.171   27.978  1.00 30.21  ? 221  ILE A C   1 
ATOM   1135  O O   . ILE A 1 212 ? 25.184  2.500   26.808  1.00 29.67  ? 221  ILE A O   1 
ATOM   1136  C CB  . ILE A 1 212 ? 24.259  2.750   30.049  1.00 27.74  ? 221  ILE A CB  1 
ATOM   1137  C CG1 . ILE A 1 212 ? 23.174  2.381   31.046  1.00 26.70  ? 221  ILE A CG1 1 
ATOM   1138  C CG2 . ILE A 1 212 ? 23.992  4.112   29.476  1.00 25.65  ? 221  ILE A CG2 1 
ATOM   1139  C CD1 . ILE A 1 212 ? 21.865  2.170   30.417  1.00 26.28  ? 221  ILE A CD1 1 
ATOM   1140  N N   . GLU A 1 213 ? 26.666  2.179   28.485  1.00 32.04  ? 222  GLU A N   1 
ATOM   1141  C CA  . GLU A 1 213 ? 27.784  2.723   27.737  1.00 33.96  ? 222  GLU A CA  1 
ATOM   1142  C C   . GLU A 1 213 ? 28.042  1.929   26.440  1.00 35.39  ? 222  GLU A C   1 
ATOM   1143  O O   . GLU A 1 213 ? 28.677  2.424   25.486  1.00 35.69  ? 222  GLU A O   1 
ATOM   1144  C CB  . GLU A 1 213 ? 29.026  2.814   28.621  1.00 34.79  ? 222  GLU A CB  1 
ATOM   1145  C CG  . GLU A 1 213 ? 29.878  4.072   28.348  1.00 37.91  ? 222  GLU A CG  1 
ATOM   1146  C CD  . GLU A 1 213 ? 31.075  4.224   29.307  1.00 44.13  ? 222  GLU A CD  1 
ATOM   1147  O OE1 . GLU A 1 213 ? 31.172  3.381   30.244  1.00 47.94  ? 222  GLU A OE1 1 
ATOM   1148  O OE2 . GLU A 1 213 ? 31.911  5.175   29.126  1.00 45.91  ? 222  GLU A OE2 1 
ATOM   1149  N N   . PHE A 1 214 ? 27.521  0.707   26.397  1.00 36.57  ? 223  PHE A N   1 
ATOM   1150  C CA  . PHE A 1 214 ? 27.664  -0.117  25.227  1.00 37.97  ? 223  PHE A CA  1 
ATOM   1151  C C   . PHE A 1 214 ? 26.720  0.403   24.160  1.00 37.29  ? 223  PHE A C   1 
ATOM   1152  O O   . PHE A 1 214 ? 27.092  0.574   22.993  1.00 37.88  ? 223  PHE A O   1 
ATOM   1153  C CB  . PHE A 1 214 ? 27.359  -1.553  25.593  1.00 39.17  ? 223  PHE A CB  1 
ATOM   1154  C CG  . PHE A 1 214 ? 27.250  -2.460  24.430  1.00 40.13  ? 223  PHE A CG  1 
ATOM   1155  C CD1 . PHE A 1 214 ? 28.378  -3.058  23.887  1.00 41.72  ? 223  PHE A CD1 1 
ATOM   1156  C CD2 . PHE A 1 214 ? 26.018  -2.726  23.876  1.00 39.60  ? 223  PHE A CD2 1 
ATOM   1157  C CE1 . PHE A 1 214 ? 28.284  -3.911  22.825  1.00 42.55  ? 223  PHE A CE1 1 
ATOM   1158  C CE2 . PHE A 1 214 ? 25.911  -3.579  22.803  1.00 41.09  ? 223  PHE A CE2 1 
ATOM   1159  C CZ  . PHE A 1 214 ? 27.048  -4.179  22.278  1.00 42.32  ? 223  PHE A CZ  1 
ATOM   1160  N N   . GLN A 1 215 ? 25.501  0.692   24.572  1.00 36.31  ? 224  GLN A N   1 
ATOM   1161  C CA  . GLN A 1 215 ? 24.519  1.186   23.644  1.00 36.01  ? 224  GLN A CA  1 
ATOM   1162  C C   . GLN A 1 215 ? 24.899  2.583   23.236  1.00 34.55  ? 224  GLN A C   1 
ATOM   1163  O O   . GLN A 1 215 ? 24.714  2.972   22.094  1.00 34.39  ? 224  GLN A O   1 
ATOM   1164  C CB  . GLN A 1 215 ? 23.147  1.198   24.284  1.00 35.57  ? 224  GLN A CB  1 
ATOM   1165  C CG  . GLN A 1 215 ? 22.908  -0.028  25.097  1.00 39.30  ? 224  GLN A CG  1 
ATOM   1166  C CD  . GLN A 1 215 ? 21.562  -0.048  25.760  1.00 41.90  ? 224  GLN A CD  1 
ATOM   1167  O OE1 . GLN A 1 215 ? 21.088  0.968   26.310  1.00 41.51  ? 224  GLN A OE1 1 
ATOM   1168  N NE2 . GLN A 1 215 ? 20.924  -1.222  25.725  1.00 43.92  ? 224  GLN A NE2 1 
ATOM   1169  N N   . GLN A 1 216 ? 25.434  3.345   24.168  1.00 33.69  ? 225  GLN A N   1 
ATOM   1170  C CA  . GLN A 1 216 ? 25.808  4.693   23.855  1.00 32.71  ? 225  GLN A CA  1 
ATOM   1171  C C   . GLN A 1 216 ? 26.837  4.745   22.717  1.00 33.48  ? 225  GLN A C   1 
ATOM   1172  O O   . GLN A 1 216 ? 26.639  5.364   21.664  1.00 32.31  ? 225  GLN A O   1 
ATOM   1173  C CB  . GLN A 1 216 ? 26.393  5.311   25.103  1.00 32.47  ? 225  GLN A CB  1 
ATOM   1174  C CG  . GLN A 1 216 ? 25.443  5.407   26.246  1.00 33.04  ? 225  GLN A CG  1 
ATOM   1175  C CD  . GLN A 1 216 ? 25.667  6.687   27.028  1.00 34.25  ? 225  GLN A CD  1 
ATOM   1176  O OE1 . GLN A 1 216 ? 26.760  6.945   27.546  1.00 35.57  ? 225  GLN A OE1 1 
ATOM   1177  N NE2 . GLN A 1 216 ? 24.636  7.514   27.096  1.00 33.56  ? 225  GLN A NE2 1 
ATOM   1178  N N   . LYS A 1 217 ? 27.945  4.068   22.956  1.00 35.21  ? 226  LYS A N   1 
ATOM   1179  C CA  . LYS A 1 217 ? 29.100  4.168   22.112  1.00 36.53  ? 226  LYS A CA  1 
ATOM   1180  C C   . LYS A 1 217 ? 28.926  3.330   20.856  1.00 37.10  ? 226  LYS A C   1 
ATOM   1181  O O   . LYS A 1 217 ? 29.558  3.603   19.829  1.00 37.80  ? 226  LYS A O   1 
ATOM   1182  C CB  . LYS A 1 217 ? 30.313  3.673   22.894  1.00 38.56  ? 226  LYS A CB  1 
ATOM   1183  C CG  . LYS A 1 217 ? 30.859  4.613   23.981  1.00 39.76  ? 226  LYS A CG  1 
ATOM   1184  C CD  . LYS A 1 217 ? 32.286  4.158   24.350  1.00 44.63  ? 226  LYS A CD  1 
ATOM   1185  C CE  . LYS A 1 217 ? 32.838  4.945   25.520  1.00 46.82  ? 226  LYS A CE  1 
ATOM   1186  N NZ  . LYS A 1 217 ? 34.002  4.221   26.112  1.00 50.36  ? 226  LYS A NZ  1 
ATOM   1187  N N   . ASN A 1 218 ? 28.097  2.294   20.943  1.00 36.84  ? 227  ASN A N   1 
ATOM   1188  C CA  . ASN A 1 218 ? 27.825  1.492   19.781  1.00 37.50  ? 227  ASN A CA  1 
ATOM   1189  C C   . ASN A 1 218 ? 26.592  1.937   19.014  1.00 36.64  ? 227  ASN A C   1 
ATOM   1190  O O   . ASN A 1 218 ? 26.108  1.250   18.119  1.00 37.67  ? 227  ASN A O   1 
ATOM   1191  C CB  . ASN A 1 218 ? 27.768  0.045   20.154  1.00 38.45  ? 227  ASN A CB  1 
ATOM   1192  C CG  . ASN A 1 218 ? 29.097  -0.600  20.023  1.00 40.24  ? 227  ASN A CG  1 
ATOM   1193  O OD1 . ASN A 1 218 ? 29.818  -0.389  19.035  1.00 41.34  ? 227  ASN A OD1 1 
ATOM   1194  N ND2 . ASN A 1 218 ? 29.461  -1.385  21.015  1.00 40.75  ? 227  ASN A ND2 1 
ATOM   1195  N N   . ASN A 1 219 ? 26.123  3.129   19.339  1.00 34.97  ? 228  ASN A N   1 
ATOM   1196  C CA  . ASN A 1 219 ? 24.860  3.632   18.847  1.00 33.33  ? 228  ASN A CA  1 
ATOM   1197  C C   . ASN A 1 219 ? 24.684  3.537   17.354  1.00 32.93  ? 228  ASN A C   1 
ATOM   1198  O O   . ASN A 1 219 ? 23.738  2.932   16.862  1.00 33.05  ? 228  ASN A O   1 
ATOM   1199  C CB  . ASN A 1 219 ? 24.718  5.079   19.278  1.00 32.25  ? 228  ASN A CB  1 
ATOM   1200  C CG  . ASN A 1 219 ? 23.491  5.724   18.710  1.00 32.64  ? 228  ASN A CG  1 
ATOM   1201  O OD1 . ASN A 1 219 ? 23.579  6.383   17.677  1.00 34.27  ? 228  ASN A OD1 1 
ATOM   1202  N ND2 . ASN A 1 219 ? 22.322  5.528   19.363  1.00 33.56  ? 228  ASN A ND2 1 
ATOM   1203  N N   . ARG A 1 220 ? 25.601  4.154   16.636  1.00 32.11  ? 229  ARG A N   1 
ATOM   1204  C CA  . ARG A 1 220 ? 25.466  4.207   15.218  1.00 31.39  ? 229  ARG A CA  1 
ATOM   1205  C C   . ARG A 1 220 ? 25.342  2.799   14.673  1.00 32.60  ? 229  ARG A C   1 
ATOM   1206  O O   . ARG A 1 220 ? 24.443  2.521   13.894  1.00 32.51  ? 229  ARG A O   1 
ATOM   1207  C CB  . ARG A 1 220 ? 26.656  4.908   14.634  1.00 31.77  ? 229  ARG A CB  1 
ATOM   1208  C CG  . ARG A 1 220 ? 26.345  5.686   13.428  1.00 30.02  ? 229  ARG A CG  1 
ATOM   1209  C CD  . ARG A 1 220 ? 27.614  6.219   12.863  1.00 30.28  ? 229  ARG A CD  1 
ATOM   1210  N NE  . ARG A 1 220 ? 27.558  6.186   11.423  1.00 31.43  ? 229  ARG A NE  1 
ATOM   1211  C CZ  . ARG A 1 220 ? 28.585  6.409   10.627  1.00 32.84  ? 229  ARG A CZ  1 
ATOM   1212  N NH1 . ARG A 1 220 ? 29.773  6.675   11.145  1.00 33.25  ? 229  ARG A NH1 1 
ATOM   1213  N NH2 . ARG A 1 220 ? 28.413  6.358   9.312   1.00 34.40  ? 229  ARG A NH2 1 
ATOM   1214  N N   . LEU A 1 221 ? 26.215  1.901   15.118  1.00 33.61  ? 230  LEU A N   1 
ATOM   1215  C CA  . LEU A 1 221 ? 26.162  0.525   14.649  1.00 35.02  ? 230  LEU A CA  1 
ATOM   1216  C C   . LEU A 1 221 ? 24.799  -0.092  14.878  1.00 34.66  ? 230  LEU A C   1 
ATOM   1217  O O   . LEU A 1 221 ? 24.228  -0.742  14.007  1.00 35.55  ? 230  LEU A O   1 
ATOM   1218  C CB  . LEU A 1 221 ? 27.229  -0.331  15.327  1.00 36.67  ? 230  LEU A CB  1 
ATOM   1219  C CG  . LEU A 1 221 ? 27.218  -1.816  14.932  1.00 38.40  ? 230  LEU A CG  1 
ATOM   1220  C CD1 . LEU A 1 221 ? 27.964  -2.046  13.653  1.00 40.50  ? 230  LEU A CD1 1 
ATOM   1221  C CD2 . LEU A 1 221 ? 27.843  -2.665  15.988  1.00 40.39  ? 230  LEU A CD2 1 
ATOM   1222  N N   . LEU A 1 222 ? 24.277  0.117   16.065  1.00 33.59  ? 231  LEU A N   1 
ATOM   1223  C CA  . LEU A 1 222 ? 23.028  -0.496  16.422  1.00 33.69  ? 231  LEU A CA  1 
ATOM   1224  C C   . LEU A 1 222 ? 21.964  0.015   15.508  1.00 32.78  ? 231  LEU A C   1 
ATOM   1225  O O   . LEU A 1 222 ? 21.227  -0.776  14.925  1.00 33.90  ? 231  LEU A O   1 
ATOM   1226  C CB  . LEU A 1 222 ? 22.682  -0.180  17.864  1.00 32.80  ? 231  LEU A CB  1 
ATOM   1227  C CG  . LEU A 1 222 ? 23.686  -0.831  18.788  1.00 34.33  ? 231  LEU A CG  1 
ATOM   1228  C CD1 . LEU A 1 222 ? 23.766  -0.068  20.087  1.00 34.94  ? 231  LEU A CD1 1 
ATOM   1229  C CD2 . LEU A 1 222 ? 23.321  -2.300  18.985  1.00 36.91  ? 231  LEU A CD2 1 
ATOM   1230  N N   . GLU A 1 223 ? 21.900  1.341   15.371  1.00 30.98  ? 232  GLU A N   1 
ATOM   1231  C CA  . GLU A 1 223 ? 20.910  1.953   14.517  1.00 29.90  ? 232  GLU A CA  1 
ATOM   1232  C C   . GLU A 1 223 ? 20.958  1.296   13.161  1.00 30.58  ? 232  GLU A C   1 
ATOM   1233  O O   . GLU A 1 223 ? 19.931  0.854   12.658  1.00 31.33  ? 232  GLU A O   1 
ATOM   1234  C CB  . GLU A 1 223 ? 21.143  3.444   14.389  1.00 28.47  ? 232  GLU A CB  1 
ATOM   1235  C CG  . GLU A 1 223 ? 20.668  4.197   15.584  1.00 29.53  ? 232  GLU A CG  1 
ATOM   1236  C CD  . GLU A 1 223 ? 19.147  4.022   15.906  1.00 32.40  ? 232  GLU A CD  1 
ATOM   1237  O OE1 . GLU A 1 223 ? 18.343  3.501   15.067  1.00 32.67  ? 232  GLU A OE1 1 
ATOM   1238  O OE2 . GLU A 1 223 ? 18.761  4.455   17.032  1.00 32.74  ? 232  GLU A OE2 1 
ATOM   1239  N N   . ILE A 1 224 ? 22.148  1.191   12.591  1.00 30.65  ? 233  ILE A N   1 
ATOM   1240  C CA  . ILE A 1 224 ? 22.284  0.552   11.310  1.00 31.72  ? 233  ILE A CA  1 
ATOM   1241  C C   . ILE A 1 224 ? 21.732  -0.856  11.357  1.00 33.30  ? 233  ILE A C   1 
ATOM   1242  O O   . ILE A 1 224 ? 20.889  -1.227  10.541  1.00 33.72  ? 233  ILE A O   1 
ATOM   1243  C CB  . ILE A 1 224 ? 23.734  0.497   10.868  1.00 32.77  ? 233  ILE A CB  1 
ATOM   1244  C CG1 . ILE A 1 224 ? 24.349  1.890   10.977  1.00 30.62  ? 233  ILE A CG1 1 
ATOM   1245  C CG2 . ILE A 1 224 ? 23.820  -0.063  9.451   1.00 34.09  ? 233  ILE A CG2 1 
ATOM   1246  C CD1 . ILE A 1 224 ? 25.522  2.114   10.103  1.00 31.74  ? 233  ILE A CD1 1 
ATOM   1247  N N   . THR A 1 225 ? 22.204  -1.631  12.321  1.00 34.29  ? 234  THR A N   1 
ATOM   1248  C CA  . THR A 1 225 ? 21.769  -3.006  12.485  1.00 36.33  ? 234  THR A CA  1 
ATOM   1249  C C   . THR A 1 225 ? 20.264  -3.178  12.378  1.00 36.37  ? 234  THR A C   1 
ATOM   1250  O O   . THR A 1 225 ? 19.785  -4.093  11.698  1.00 38.20  ? 234  THR A O   1 
ATOM   1251  C CB  . THR A 1 225 ? 22.249  -3.533  13.815  1.00 36.78  ? 234  THR A CB  1 
ATOM   1252  O OG1 . THR A 1 225 ? 23.673  -3.572  13.767  1.00 37.65  ? 234  THR A OG1 1 
ATOM   1253  C CG2 . THR A 1 225 ? 21.708  -4.937  14.095  1.00 38.59  ? 234  THR A CG2 1 
ATOM   1254  N N   . ARG A 1 226 ? 19.527  -2.294  13.042  1.00 34.85  ? 235  ARG A N   1 
ATOM   1255  C CA  . ARG A 1 226 ? 18.077  -2.317  12.994  1.00 34.82  ? 235  ARG A CA  1 
ATOM   1256  C C   . ARG A 1 226 ? 17.630  -2.045  11.580  1.00 34.65  ? 235  ARG A C   1 
ATOM   1257  O O   . ARG A 1 226 ? 17.057  -2.907  10.925  1.00 36.13  ? 235  ARG A O   1 
ATOM   1258  C CB  . ARG A 1 226 ? 17.538  -1.252  13.914  1.00 33.10  ? 235  ARG A CB  1 
ATOM   1259  C CG  . ARG A 1 226 ? 16.051  -1.073  13.870  1.00 34.01  ? 235  ARG A CG  1 
ATOM   1260  C CD  . ARG A 1 226 ? 15.693  0.321   14.392  1.00 34.31  ? 235  ARG A CD  1 
ATOM   1261  N NE  . ARG A 1 226 ? 16.477  0.691   15.582  1.00 33.78  ? 235  ARG A NE  1 
ATOM   1262  C CZ  . ARG A 1 226 ? 16.235  0.247   16.806  1.00 31.69  ? 235  ARG A CZ  1 
ATOM   1263  N NH1 . ARG A 1 226 ? 15.221  -0.576  16.998  1.00 31.13  ? 235  ARG A NH1 1 
ATOM   1264  N NH2 . ARG A 1 226 ? 17.007  0.630   17.818  1.00 29.88  ? 235  ARG A NH2 1 
ATOM   1265  N N   . GLU A 1 227 ? 17.925  -0.844  11.109  1.00 33.06  ? 236  GLU A N   1 
ATOM   1266  C CA  . GLU A 1 227 ? 17.621  -0.436  9.756   1.00 33.10  ? 236  GLU A CA  1 
ATOM   1267  C C   . GLU A 1 227 ? 17.703  -1.628  8.824   1.00 34.53  ? 236  GLU A C   1 
ATOM   1268  O O   . GLU A 1 227 ? 16.797  -1.894  8.053   1.00 35.09  ? 236  GLU A O   1 
ATOM   1269  C CB  . GLU A 1 227 ? 18.598  0.661   9.331   1.00 32.52  ? 236  GLU A CB  1 
ATOM   1270  C CG  . GLU A 1 227 ? 18.018  1.805   8.465   1.00 33.73  ? 236  GLU A CG  1 
ATOM   1271  C CD  . GLU A 1 227 ? 19.025  2.970   8.235   1.00 35.50  ? 236  GLU A CD  1 
ATOM   1272  O OE1 . GLU A 1 227 ? 19.200  3.410   7.051   1.00 38.18  ? 236  GLU A OE1 1 
ATOM   1273  O OE2 . GLU A 1 227 ? 19.634  3.438   9.236   1.00 32.86  ? 236  GLU A OE2 1 
ATOM   1274  N N   . PHE A 1 228 ? 18.780  -2.382  8.921   1.00 35.50  ? 237  PHE A N   1 
ATOM   1275  C CA  . PHE A 1 228 ? 18.961  -3.508  8.019   1.00 37.51  ? 237  PHE A CA  1 
ATOM   1276  C C   . PHE A 1 228 ? 18.022  -4.665  8.306   1.00 38.64  ? 237  PHE A C   1 
ATOM   1277  O O   . PHE A 1 228 ? 17.509  -5.290  7.383   1.00 39.95  ? 237  PHE A O   1 
ATOM   1278  C CB  . PHE A 1 228 ? 20.406  -3.985  8.011   1.00 38.98  ? 237  PHE A CB  1 
ATOM   1279  C CG  . PHE A 1 228 ? 21.298  -3.208  7.075   1.00 39.53  ? 237  PHE A CG  1 
ATOM   1280  C CD1 . PHE A 1 228 ? 22.476  -2.624  7.536   1.00 39.81  ? 237  PHE A CD1 1 
ATOM   1281  C CD2 . PHE A 1 228 ? 20.966  -3.064  5.733   1.00 40.82  ? 237  PHE A CD2 1 
ATOM   1282  C CE1 . PHE A 1 228 ? 23.304  -1.912  6.680   1.00 40.27  ? 237  PHE A CE1 1 
ATOM   1283  C CE2 . PHE A 1 228 ? 21.792  -2.345  4.861   1.00 40.79  ? 237  PHE A CE2 1 
ATOM   1284  C CZ  . PHE A 1 228 ? 22.962  -1.763  5.341   1.00 40.51  ? 237  PHE A CZ  1 
ATOM   1285  N N   . SER A 1 229 ? 17.801  -4.947  9.584   1.00 38.22  ? 238  SER A N   1 
ATOM   1286  C CA  . SER A 1 229 ? 16.877  -5.988  10.006  1.00 39.47  ? 238  SER A CA  1 
ATOM   1287  C C   . SER A 1 229 ? 15.472  -5.696  9.518   1.00 38.82  ? 238  SER A C   1 
ATOM   1288  O O   . SER A 1 229 ? 14.694  -6.608  9.253   1.00 40.60  ? 238  SER A O   1 
ATOM   1289  C CB  . SER A 1 229 ? 16.860  -6.076  11.528  1.00 39.00  ? 238  SER A CB  1 
ATOM   1290  O OG  . SER A 1 229 ? 18.099  -6.521  12.030  1.00 40.52  ? 238  SER A OG  1 
ATOM   1291  N N   . VAL A 1 230 ? 15.146  -4.419  9.401   1.00 36.34  ? 239  VAL A N   1 
ATOM   1292  C CA  . VAL A 1 230 ? 13.805  -4.061  9.064   1.00 35.67  ? 239  VAL A CA  1 
ATOM   1293  C C   . VAL A 1 230 ? 13.669  -3.965  7.590   1.00 36.36  ? 239  VAL A C   1 
ATOM   1294  O O   . VAL A 1 230 ? 12.562  -3.909  7.078   1.00 37.11  ? 239  VAL A O   1 
ATOM   1295  C CB  . VAL A 1 230 ? 13.443  -2.738  9.618   1.00 32.92  ? 239  VAL A CB  1 
ATOM   1296  C CG1 . VAL A 1 230 ? 11.946  -2.568  9.586   1.00 33.27  ? 239  VAL A CG1 1 
ATOM   1297  C CG2 . VAL A 1 230 ? 13.907  -2.662  11.001  1.00 32.75  ? 239  VAL A CG2 1 
ATOM   1298  N N   . ASN A 1 231 ? 14.785  -3.930  6.892   1.00 36.72  ? 240  ASN A N   1 
ATOM   1299  C CA  . ASN A 1 231 ? 14.704  -3.764  5.465   1.00 37.25  ? 240  ASN A CA  1 
ATOM   1300  C C   . ASN A 1 231 ? 15.273  -4.917  4.657   1.00 39.52  ? 240  ASN A C   1 
ATOM   1301  O O   . ASN A 1 231 ? 15.474  -4.806  3.441   1.00 39.83  ? 240  ASN A O   1 
ATOM   1302  C CB  . ASN A 1 231 ? 15.325  -2.442  5.080   1.00 35.66  ? 240  ASN A CB  1 
ATOM   1303  C CG  . ASN A 1 231 ? 14.436  -1.289  5.431   1.00 34.94  ? 240  ASN A CG  1 
ATOM   1304  O OD1 . ASN A 1 231 ? 13.514  -0.945  4.687   1.00 36.11  ? 240  ASN A OD1 1 
ATOM   1305  N ND2 . ASN A 1 231 ? 14.689  -0.687  6.587   1.00 35.93  ? 240  ASN A ND2 1 
ATOM   1306  N N   . ALA A 1 232 ? 15.519  -6.034  5.331   1.00 41.06  ? 241  ALA A N   1 
ATOM   1307  C CA  . ALA A 1 232 ? 16.110  -7.165  4.669   1.00 43.60  ? 241  ALA A CA  1 
ATOM   1308  C C   . ALA A 1 232 ? 17.402  -6.736  3.972   1.00 43.66  ? 241  ALA A C   1 
ATOM   1309  O O   . ALA A 1 232 ? 17.665  -7.129  2.844   1.00 45.34  ? 241  ALA A O   1 
ATOM   1310  C CB  . ALA A 1 232 ? 15.141  -7.705  3.676   1.00 45.05  ? 241  ALA A CB  1 
ATOM   1311  N N   . GLY A 1 233 ? 18.190  -5.898  4.639   1.00 42.10  ? 242  GLY A N   1 
ATOM   1312  C CA  . GLY A 1 233 ? 19.524  -5.533  4.172   1.00 42.16  ? 242  GLY A CA  1 
ATOM   1313  C C   . GLY A 1 233 ? 19.651  -4.581  2.998   1.00 41.20  ? 242  GLY A C   1 
ATOM   1314  O O   . GLY A 1 233 ? 20.652  -4.604  2.283   1.00 42.55  ? 242  GLY A O   1 
ATOM   1315  N N   . VAL A 1 234 ? 18.649  -3.746  2.774   1.00 39.28  ? 243  VAL A N   1 
ATOM   1316  C CA  . VAL A 1 234 ? 18.765  -2.714  1.756   1.00 38.19  ? 243  VAL A CA  1 
ATOM   1317  C C   . VAL A 1 234 ? 17.863  -1.554  2.105   1.00 36.19  ? 243  VAL A C   1 
ATOM   1318  O O   . VAL A 1 234 ? 16.697  -1.783  2.397   1.00 36.41  ? 243  VAL A O   1 
ATOM   1319  C CB  . VAL A 1 234 ? 18.331  -3.208  0.389   1.00 39.23  ? 243  VAL A CB  1 
ATOM   1320  C CG1 . VAL A 1 234 ? 19.177  -2.549  -0.620  1.00 39.03  ? 243  VAL A CG1 1 
ATOM   1321  C CG2 . VAL A 1 234 ? 18.503  -4.692  0.270   1.00 41.94  ? 243  VAL A CG2 1 
ATOM   1322  N N   . THR A 1 235 ? 18.368  -0.318  2.058   1.00 34.78  ? 244  THR A N   1 
ATOM   1323  C CA  . THR A 1 235 ? 17.520  0.840   2.381   1.00 33.35  ? 244  THR A CA  1 
ATOM   1324  C C   . THR A 1 235 ? 17.576  1.969   1.378   1.00 32.22  ? 244  THR A C   1 
ATOM   1325  O O   . THR A 1 235 ? 18.625  2.208   0.793   1.00 32.63  ? 244  THR A O   1 
ATOM   1326  C CB  . THR A 1 235 ? 17.964  1.513   3.663   1.00 32.41  ? 244  THR A CB  1 
ATOM   1327  O OG1 . THR A 1 235 ? 19.109  0.852   4.209   1.00 33.70  ? 244  THR A OG1 1 
ATOM   1328  C CG2 . THR A 1 235 ? 16.782  1.602   4.660   1.00 32.83  ? 244  THR A CG2 1 
ATOM   1329  N N   . THR A 1 236 ? 16.472  2.689   1.210   1.00 30.87  ? 245  THR A N   1 
ATOM   1330  C CA  . THR A 1 236 ? 16.562  3.989   0.589   1.00 29.97  ? 245  THR A CA  1 
ATOM   1331  C C   . THR A 1 236 ? 16.105  4.958   1.612   1.00 28.21  ? 245  THR A C   1 
ATOM   1332  O O   . THR A 1 236 ? 15.447  4.566   2.562   1.00 28.25  ? 245  THR A O   1 
ATOM   1333  C CB  . THR A 1 236 ? 15.856  4.058   -0.753  1.00 30.81  ? 245  THR A CB  1 
ATOM   1334  O OG1 . THR A 1 236 ? 16.702  3.410   -1.694  1.00 34.45  ? 245  THR A OG1 1 
ATOM   1335  C CG2 . THR A 1 236 ? 15.676  5.483   -1.288  1.00 29.79  ? 245  THR A CG2 1 
ATOM   1336  N N   . PRO A 1 237 ? 16.314  6.244   1.339   1.00 27.10  ? 246  PRO A N   1 
ATOM   1337  C CA  . PRO A 1 237 ? 17.117  7.195   2.020   1.00 25.46  ? 246  PRO A CA  1 
ATOM   1338  C C   . PRO A 1 237 ? 18.284  6.502   2.648   1.00 25.75  ? 246  PRO A C   1 
ATOM   1339  O O   . PRO A 1 237 ? 18.144  5.447   3.264   1.00 26.85  ? 246  PRO A O   1 
ATOM   1340  C CB  . PRO A 1 237 ? 16.167  7.740   3.072   1.00 24.39  ? 246  PRO A CB  1 
ATOM   1341  C CG  . PRO A 1 237 ? 14.802  7.628   2.461   1.00 25.40  ? 246  PRO A CG  1 
ATOM   1342  C CD  . PRO A 1 237 ? 14.970  6.829   1.183   1.00 27.03  ? 246  PRO A CD  1 
ATOM   1343  N N   . VAL A 1 238 ? 19.444  7.102   2.491   1.00 25.07  ? 247  VAL A N   1 
ATOM   1344  C CA  . VAL A 1 238 ? 20.614  6.630   3.164   1.00 25.13  ? 247  VAL A CA  1 
ATOM   1345  C C   . VAL A 1 238 ? 20.624  7.428   4.448   1.00 23.72  ? 247  VAL A C   1 
ATOM   1346  O O   . VAL A 1 238 ? 20.879  8.629   4.458   1.00 22.63  ? 247  VAL A O   1 
ATOM   1347  C CB  . VAL A 1 238 ? 21.818  6.870   2.286   1.00 25.62  ? 247  VAL A CB  1 
ATOM   1348  C CG1 . VAL A 1 238 ? 23.047  6.657   3.044   1.00 26.93  ? 247  VAL A CG1 1 
ATOM   1349  C CG2 . VAL A 1 238 ? 21.784  5.913   1.132   1.00 26.85  ? 247  VAL A CG2 1 
ATOM   1350  N N   . SER A 1 239 ? 20.273  6.771   5.536   1.00 23.78  ? 248  SER A N   1 
ATOM   1351  C CA  . SER A 1 239 ? 20.021  7.496   6.755   1.00 22.78  ? 248  SER A CA  1 
ATOM   1352  C C   . SER A 1 239 ? 21.262  8.213   7.164   1.00 22.99  ? 248  SER A C   1 
ATOM   1353  O O   . SER A 1 239 ? 22.357  7.898   6.701   1.00 24.12  ? 248  SER A O   1 
ATOM   1354  C CB  . SER A 1 239 ? 19.682  6.537   7.869   1.00 23.22  ? 248  SER A CB  1 
ATOM   1355  O OG  . SER A 1 239 ? 20.858  5.897   8.321   1.00 24.39  ? 248  SER A OG  1 
ATOM   1356  N N   . THR A 1 240 ? 21.108  9.141   8.094   1.00 22.22  ? 249  THR A N   1 
ATOM   1357  C CA  . THR A 1 240 ? 22.254  9.833   8.648   1.00 22.32  ? 249  THR A CA  1 
ATOM   1358  C C   . THR A 1 240 ? 23.022  8.880   9.534   1.00 23.06  ? 249  THR A C   1 
ATOM   1359  O O   . THR A 1 240 ? 24.076  9.219   10.009  1.00 23.62  ? 249  THR A O   1 
ATOM   1360  C CB  . THR A 1 240 ? 21.847  11.050  9.472   1.00 21.09  ? 249  THR A CB  1 
ATOM   1361  O OG1 . THR A 1 240 ? 21.298  10.611  10.717  1.00 21.59  ? 249  THR A OG1 1 
ATOM   1362  C CG2 . THR A 1 240 ? 20.814  11.875  8.754   1.00 20.31  ? 249  THR A CG2 1 
ATOM   1363  N N   . TYR A 1 241 ? 22.487  7.698   9.781   1.00 23.39  ? 250  TYR A N   1 
ATOM   1364  C CA  . TYR A 1 241 ? 23.264  6.720   10.480  1.00 24.51  ? 250  TYR A CA  1 
ATOM   1365  C C   . TYR A 1 241 ? 24.134  5.937   9.499   1.00 26.04  ? 250  TYR A C   1 
ATOM   1366  O O   . TYR A 1 241 ? 25.210  5.493   9.841   1.00 27.01  ? 250  TYR A O   1 
ATOM   1367  C CB  . TYR A 1 241 ? 22.372  5.751   11.239  1.00 25.09  ? 250  TYR A CB  1 
ATOM   1368  C CG  . TYR A 1 241 ? 21.395  6.337   12.225  1.00 25.23  ? 250  TYR A CG  1 
ATOM   1369  C CD1 . TYR A 1 241 ? 20.060  5.978   12.185  1.00 27.13  ? 250  TYR A CD1 1 
ATOM   1370  C CD2 . TYR A 1 241 ? 21.809  7.218   13.224  1.00 27.43  ? 250  TYR A CD2 1 
ATOM   1371  C CE1 . TYR A 1 241 ? 19.135  6.504   13.092  1.00 27.98  ? 250  TYR A CE1 1 
ATOM   1372  C CE2 . TYR A 1 241 ? 20.896  7.750   14.148  1.00 28.72  ? 250  TYR A CE2 1 
ATOM   1373  C CZ  . TYR A 1 241 ? 19.547  7.392   14.070  1.00 28.29  ? 250  TYR A CZ  1 
ATOM   1374  O OH  . TYR A 1 241 ? 18.632  7.916   14.970  1.00 27.69  ? 250  TYR A OH  1 
ATOM   1375  N N   . MET A 1 242 ? 23.670  5.737   8.281   1.00 26.38  ? 251  MET A N   1 
ATOM   1376  C CA  . MET A 1 242 ? 24.488  5.033   7.342   1.00 28.25  ? 251  MET A CA  1 
ATOM   1377  C C   . MET A 1 242 ? 25.617  5.939   6.920   1.00 28.65  ? 251  MET A C   1 
ATOM   1378  O O   . MET A 1 242 ? 26.756  5.520   6.823   1.00 30.21  ? 251  MET A O   1 
ATOM   1379  C CB  . MET A 1 242 ? 23.676  4.635   6.137   1.00 28.71  ? 251  MET A CB  1 
ATOM   1380  C CG  . MET A 1 242 ? 22.530  3.701   6.438   1.00 29.23  ? 251  MET A CG  1 
ATOM   1381  S SD  . MET A 1 242 ? 23.108  2.028   6.751   1.00 31.66  ? 251  MET A SD  1 
ATOM   1382  C CE  . MET A 1 242 ? 21.649  1.091   6.451   1.00 31.69  ? 251  MET A CE  1 
ATOM   1383  N N   . LEU A 1 243 ? 25.292  7.195   6.678   1.00 27.72  ? 252  LEU A N   1 
ATOM   1384  C CA  . LEU A 1 243 ? 26.271  8.167   6.266   1.00 27.95  ? 252  LEU A CA  1 
ATOM   1385  C C   . LEU A 1 243 ? 26.081  9.409   7.045   1.00 26.82  ? 252  LEU A C   1 
ATOM   1386  O O   . LEU A 1 243 ? 24.973  9.910   7.177   1.00 25.79  ? 252  LEU A O   1 
ATOM   1387  C CB  . LEU A 1 243 ? 26.060  8.537   4.826   1.00 28.11  ? 252  LEU A CB  1 
ATOM   1388  C CG  . LEU A 1 243 ? 27.029  7.932   3.869   1.00 29.87  ? 252  LEU A CG  1 
ATOM   1389  C CD1 . LEU A 1 243 ? 27.133  8.882   2.755   1.00 30.27  ? 252  LEU A CD1 1 
ATOM   1390  C CD2 . LEU A 1 243 ? 28.294  7.880   4.564   1.00 32.15  ? 252  LEU A CD2 1 
ATOM   1391  N N   . THR A 1 244 ? 27.171  9.926   7.554   1.00 27.26  ? 253  THR A N   1 
ATOM   1392  C CA  . THR A 1 244 ? 27.141  11.205  8.212   1.00 26.59  ? 253  THR A CA  1 
ATOM   1393  C C   . THR A 1 244 ? 27.253  12.246  7.182   1.00 26.66  ? 253  THR A C   1 
ATOM   1394  O O   . THR A 1 244 ? 27.763  11.986  6.107   1.00 28.29  ? 253  THR A O   1 
ATOM   1395  C CB  . THR A 1 244 ? 28.361  11.379  8.999   1.00 27.39  ? 253  THR A CB  1 
ATOM   1396  O OG1 . THR A 1 244 ? 28.451  10.283  9.903   1.00 28.60  ? 253  THR A OG1 1 
ATOM   1397  C CG2 . THR A 1 244 ? 28.323  12.707  9.738   1.00 26.79  ? 253  THR A CG2 1 
ATOM   1398  N N   . ASN A 1 245 ? 26.815  13.442  7.521   1.00 25.68  ? 254  ASN A N   1 
ATOM   1399  C CA  . ASN A 1 245 ? 26.986  14.554  6.630   1.00 26.27  ? 254  ASN A CA  1 
ATOM   1400  C C   . ASN A 1 245 ? 28.474  14.710  6.251   1.00 27.86  ? 254  ASN A C   1 
ATOM   1401  O O   . ASN A 1 245 ? 28.838  14.711  5.044   1.00 28.37  ? 254  ASN A O   1 
ATOM   1402  C CB  . ASN A 1 245 ? 26.425  15.807  7.279   1.00 25.40  ? 254  ASN A CB  1 
ATOM   1403  C CG  . ASN A 1 245 ? 26.437  17.002  6.365   1.00 25.98  ? 254  ASN A CG  1 
ATOM   1404  O OD1 . ASN A 1 245 ? 25.593  17.123  5.471   1.00 26.55  ? 254  ASN A OD1 1 
ATOM   1405  N ND2 . ASN A 1 245 ? 27.371  17.924  6.612   1.00 26.20  ? 254  ASN A ND2 1 
ATOM   1406  N N   . SER A 1 246 ? 29.326  14.801  7.276   1.00 28.55  ? 255  SER A N   1 
ATOM   1407  C CA  . SER A 1 246 ? 30.769  14.924  7.077   1.00 30.38  ? 255  SER A CA  1 
ATOM   1408  C C   . SER A 1 246 ? 31.177  13.863  6.100   1.00 31.10  ? 255  SER A C   1 
ATOM   1409  O O   . SER A 1 246 ? 31.861  14.176  5.140   1.00 32.72  ? 255  SER A O   1 
ATOM   1410  C CB  . SER A 1 246 ? 31.522  14.752  8.384   1.00 31.31  ? 255  SER A CB  1 
ATOM   1411  O OG  . SER A 1 246 ? 30.635  14.973  9.509   1.00 32.90  ? 255  SER A OG  1 
ATOM   1412  N N   . GLU A 1 247 ? 30.717  12.632  6.292   1.00 30.27  ? 256  GLU A N   1 
ATOM   1413  C CA  . GLU A 1 247 ? 31.119  11.574  5.403   1.00 31.55  ? 256  GLU A CA  1 
ATOM   1414  C C   . GLU A 1 247 ? 30.599  11.769  4.002   1.00 31.13  ? 256  GLU A C   1 
ATOM   1415  O O   . GLU A 1 247 ? 31.348  11.767  3.041   1.00 32.54  ? 256  GLU A O   1 
ATOM   1416  C CB  . GLU A 1 247 ? 30.690  10.248  5.955   1.00 31.73  ? 256  GLU A CB  1 
ATOM   1417  C CG  . GLU A 1 247 ? 31.348  9.947   7.267   1.00 34.12  ? 256  GLU A CG  1 
ATOM   1418  C CD  . GLU A 1 247 ? 30.710  8.789   8.020   1.00 36.10  ? 256  GLU A CD  1 
ATOM   1419  O OE1 . GLU A 1 247 ? 29.516  8.487   7.782   1.00 37.29  ? 256  GLU A OE1 1 
ATOM   1420  O OE2 . GLU A 1 247 ? 31.398  8.187   8.873   1.00 36.64  ? 256  GLU A OE2 1 
ATOM   1421  N N   . LEU A 1 248 ? 29.306  11.975  3.887   1.00 29.47  ? 257  LEU A N   1 
ATOM   1422  C CA  . LEU A 1 248 ? 28.703  12.127  2.591   1.00 28.95  ? 257  LEU A CA  1 
ATOM   1423  C C   . LEU A 1 248 ? 29.427  13.212  1.855   1.00 29.73  ? 257  LEU A C   1 
ATOM   1424  O O   . LEU A 1 248 ? 29.799  13.044  0.693   1.00 30.82  ? 257  LEU A O   1 
ATOM   1425  C CB  . LEU A 1 248 ? 27.200  12.436  2.697   1.00 26.85  ? 257  LEU A CB  1 
ATOM   1426  C CG  . LEU A 1 248 ? 26.489  12.865  1.407   1.00 24.35  ? 257  LEU A CG  1 
ATOM   1427  C CD1 . LEU A 1 248 ? 26.494  11.839  0.337   1.00 23.07  ? 257  LEU A CD1 1 
ATOM   1428  C CD2 . LEU A 1 248 ? 25.118  13.212  1.754   1.00 21.18  ? 257  LEU A CD2 1 
ATOM   1429  N N   . LEU A 1 249 ? 29.647  14.314  2.553   1.00 29.33  ? 258  LEU A N   1 
ATOM   1430  C CA  . LEU A 1 249 ? 30.247  15.471  1.940   1.00 30.45  ? 258  LEU A CA  1 
ATOM   1431  C C   . LEU A 1 249 ? 31.613  15.247  1.314   1.00 32.69  ? 258  LEU A C   1 
ATOM   1432  O O   . LEU A 1 249 ? 31.866  15.725  0.203   1.00 33.10  ? 258  LEU A O   1 
ATOM   1433  C CB  . LEU A 1 249 ? 30.288  16.596  2.931   1.00 29.72  ? 258  LEU A CB  1 
ATOM   1434  C CG  . LEU A 1 249 ? 29.063  17.421  2.661   1.00 28.72  ? 258  LEU A CG  1 
ATOM   1435  C CD1 . LEU A 1 249 ? 28.776  18.274  3.804   1.00 29.04  ? 258  LEU A CD1 1 
ATOM   1436  C CD2 . LEU A 1 249 ? 29.386  18.272  1.484   1.00 31.79  ? 258  LEU A CD2 1 
ATOM   1437  N N   . SER A 1 250 ? 32.478  14.521  2.027   1.00 34.15  ? 259  SER A N   1 
ATOM   1438  C CA  . SER A 1 250 ? 33.800  14.188  1.492   1.00 36.66  ? 259  SER A CA  1 
ATOM   1439  C C   . SER A 1 250 ? 33.714  13.094  0.439   1.00 37.35  ? 259  SER A C   1 
ATOM   1440  O O   . SER A 1 250 ? 34.526  13.072  -0.483  1.00 39.16  ? 259  SER A O   1 
ATOM   1441  C CB  . SER A 1 250 ? 34.835  13.855  2.592   1.00 37.86  ? 259  SER A CB  1 
ATOM   1442  O OG  . SER A 1 250 ? 34.942  12.468  2.837   1.00 38.62  ? 259  SER A OG  1 
ATOM   1443  N N   . LEU A 1 251 ? 32.734  12.209  0.588   1.00 35.99  ? 260  LEU A N   1 
ATOM   1444  C CA  . LEU A 1 251 ? 32.493  11.190  -0.373  1.00 36.53  ? 260  LEU A CA  1 
ATOM   1445  C C   . LEU A 1 251 ? 32.153  11.804  -1.685  1.00 36.61  ? 260  LEU A C   1 
ATOM   1446  O O   . LEU A 1 251 ? 32.661  11.383  -2.713  1.00 38.07  ? 260  LEU A O   1 
ATOM   1447  C CB  . LEU A 1 251 ? 31.347  10.348  0.074   1.00 35.38  ? 260  LEU A CB  1 
ATOM   1448  C CG  . LEU A 1 251 ? 31.800  9.031   0.641   1.00 36.74  ? 260  LEU A CG  1 
ATOM   1449  C CD1 . LEU A 1 251 ? 30.538  8.211   0.797   1.00 36.83  ? 260  LEU A CD1 1 
ATOM   1450  C CD2 . LEU A 1 251 ? 32.794  8.354   -0.296  1.00 38.53  ? 260  LEU A CD2 1 
ATOM   1451  N N   . ILE A 1 252 ? 31.284  12.800  -1.648  1.00 35.37  ? 261  ILE A N   1 
ATOM   1452  C CA  . ILE A 1 252 ? 30.944  13.545  -2.837  1.00 35.85  ? 261  ILE A CA  1 
ATOM   1453  C C   . ILE A 1 252 ? 32.221  14.095  -3.379  1.00 38.38  ? 261  ILE A C   1 
ATOM   1454  O O   . ILE A 1 252 ? 32.548  13.888  -4.538  1.00 39.98  ? 261  ILE A O   1 
ATOM   1455  C CB  . ILE A 1 252 ? 30.054  14.705  -2.523  1.00 33.89  ? 261  ILE A CB  1 
ATOM   1456  C CG1 . ILE A 1 252 ? 28.620  14.224  -2.422  1.00 32.85  ? 261  ILE A CG1 1 
ATOM   1457  C CG2 . ILE A 1 252 ? 30.135  15.742  -3.595  1.00 33.48  ? 261  ILE A CG2 1 
ATOM   1458  C CD1 . ILE A 1 252 ? 27.783  14.957  -1.377  1.00 31.37  ? 261  ILE A CD1 1 
ATOM   1459  N N   . ASN A 1 253 ? 32.966  14.773  -2.522  1.00 39.48  ? 262  ASN A N   1 
ATOM   1460  C CA  . ASN A 1 253 ? 34.245  15.314  -2.914  1.00 42.12  ? 262  ASN A CA  1 
ATOM   1461  C C   . ASN A 1 253 ? 35.040  14.375  -3.792  1.00 44.55  ? 262  ASN A C   1 
ATOM   1462  O O   . ASN A 1 253 ? 35.585  14.795  -4.800  1.00 46.12  ? 262  ASN A O   1 
ATOM   1463  C CB  . ASN A 1 253 ? 35.078  15.625  -1.701  1.00 42.41  ? 262  ASN A CB  1 
ATOM   1464  C CG  . ASN A 1 253 ? 35.907  16.811  -1.899  1.00 44.11  ? 262  ASN A CG  1 
ATOM   1465  O OD1 . ASN A 1 253 ? 35.951  17.378  -2.975  1.00 45.46  ? 262  ASN A OD1 1 
ATOM   1466  N ND2 . ASN A 1 253 ? 36.559  17.230  -0.856  1.00 46.99  ? 262  ASN A ND2 1 
ATOM   1467  N N   . ASP A 1 254 ? 35.072  13.101  -3.415  1.00 45.42  ? 263  ASP A N   1 
ATOM   1468  C CA  . ASP A 1 254 ? 35.887  12.094  -4.078  1.00 47.84  ? 263  ASP A CA  1 
ATOM   1469  C C   . ASP A 1 254 ? 35.303  11.616  -5.410  1.00 48.09  ? 263  ASP A C   1 
ATOM   1470  O O   . ASP A 1 254 ? 36.005  10.985  -6.191  1.00 50.13  ? 263  ASP A O   1 
ATOM   1471  C CB  . ASP A 1 254 ? 36.162  10.938  -3.104  1.00 48.68  ? 263  ASP A CB  1 
ATOM   1472  C CG  . ASP A 1 254 ? 36.872  9.780   -3.745  1.00 52.29  ? 263  ASP A CG  1 
ATOM   1473  O OD1 . ASP A 1 254 ? 37.955  9.975   -4.330  1.00 57.29  ? 263  ASP A OD1 1 
ATOM   1474  O OD2 . ASP A 1 254 ? 36.352  8.655   -3.656  1.00 53.20  ? 263  ASP A OD2 1 
ATOM   1475  N N   . MET A 1 255 ? 34.043  11.941  -5.689  1.00 46.35  ? 264  MET A N   1 
ATOM   1476  C CA  . MET A 1 255 ? 33.401  11.515  -6.931  1.00 46.67  ? 264  MET A CA  1 
ATOM   1477  C C   . MET A 1 255 ? 34.002  12.138  -8.208  1.00 48.06  ? 264  MET A C   1 
ATOM   1478  O O   . MET A 1 255 ? 34.347  13.301  -8.234  1.00 47.99  ? 264  MET A O   1 
ATOM   1479  C CB  . MET A 1 255 ? 31.919  11.786  -6.858  1.00 44.43  ? 264  MET A CB  1 
ATOM   1480  C CG  . MET A 1 255 ? 31.241  11.123  -5.691  1.00 43.67  ? 264  MET A CG  1 
ATOM   1481  S SD  . MET A 1 255 ? 29.443  11.398  -5.677  1.00 40.92  ? 264  MET A SD  1 
ATOM   1482  C CE  . MET A 1 255 ? 29.361  12.854  -6.656  1.00 42.31  ? 264  MET A CE  1 
ATOM   1483  N N   . PRO A 1 256 ? 34.136  11.351  -9.272  1.00 49.62  ? 265  PRO A N   1 
ATOM   1484  C CA  . PRO A 1 256 ? 34.740  11.798  -10.503 1.00 51.43  ? 265  PRO A CA  1 
ATOM   1485  C C   . PRO A 1 256 ? 33.896  12.719  -11.319 1.00 50.32  ? 265  PRO A C   1 
ATOM   1486  O O   . PRO A 1 256 ? 33.632  12.416  -12.480 1.00 51.10  ? 265  PRO A O   1 
ATOM   1487  C CB  . PRO A 1 256 ? 34.934  10.498  -11.281 1.00 53.58  ? 265  PRO A CB  1 
ATOM   1488  C CG  . PRO A 1 256 ? 33.992  9.557   -10.693 1.00 52.40  ? 265  PRO A CG  1 
ATOM   1489  C CD  . PRO A 1 256 ? 34.007  9.892   -9.254  1.00 50.83  ? 265  PRO A CD  1 
ATOM   1490  N N   . ILE A 1 257 ? 33.522  13.849  -10.739 1.00 49.18  ? 266  ILE A N   1 
ATOM   1491  C CA  . ILE A 1 257 ? 32.624  14.805  -11.404 1.00 48.67  ? 266  ILE A CA  1 
ATOM   1492  C C   . ILE A 1 257 ? 33.129  16.234  -11.386 1.00 48.94  ? 266  ILE A C   1 
ATOM   1493  O O   . ILE A 1 257 ? 34.076  16.564  -10.655 1.00 49.60  ? 266  ILE A O   1 
ATOM   1494  C CB  . ILE A 1 257 ? 31.221  14.806  -10.798 1.00 46.33  ? 266  ILE A CB  1 
ATOM   1495  C CG1 . ILE A 1 257 ? 31.316  14.907  -9.277  1.00 45.20  ? 266  ILE A CG1 1 
ATOM   1496  C CG2 . ILE A 1 257 ? 30.459  13.558  -11.217 1.00 46.76  ? 266  ILE A CG2 1 
ATOM   1497  C CD1 . ILE A 1 257 ? 30.115  15.479  -8.657  1.00 42.98  ? 266  ILE A CD1 1 
ATOM   1498  N N   . THR A 1 258 ? 32.471  17.079  -12.181 1.00 48.41  ? 267  THR A N   1 
ATOM   1499  C CA  . THR A 1 258 ? 32.909  18.453  -12.338 1.00 48.82  ? 267  THR A CA  1 
ATOM   1500  C C   . THR A 1 258 ? 32.780  19.146  -10.988 1.00 47.39  ? 267  THR A C   1 
ATOM   1501  O O   . THR A 1 258 ? 32.350  18.532  -10.029 1.00 46.14  ? 267  THR A O   1 
ATOM   1502  C CB  . THR A 1 258 ? 32.149  19.212  -13.439 1.00 48.42  ? 267  THR A CB  1 
ATOM   1503  O OG1 . THR A 1 258 ? 31.415  20.282  -12.853 1.00 47.56  ? 267  THR A OG1 1 
ATOM   1504  C CG2 . THR A 1 258 ? 31.216  18.296  -14.253 1.00 48.12  ? 267  THR A CG2 1 
ATOM   1505  N N   . ASN A 1 259 ? 33.168  20.411  -10.907 1.00 47.77  ? 268  ASN A N   1 
ATOM   1506  C CA  . ASN A 1 259 ? 33.171  21.100  -9.632  1.00 46.89  ? 268  ASN A CA  1 
ATOM   1507  C C   . ASN A 1 259 ? 31.874  21.706  -9.226  1.00 44.83  ? 268  ASN A C   1 
ATOM   1508  O O   . ASN A 1 259 ? 31.570  21.741  -8.037  1.00 43.62  ? 268  ASN A O   1 
ATOM   1509  C CB  . ASN A 1 259 ? 34.237  22.160  -9.592  1.00 48.64  ? 268  ASN A CB  1 
ATOM   1510  C CG  . ASN A 1 259 ? 35.440  21.692  -8.874  1.00 50.82  ? 268  ASN A CG  1 
ATOM   1511  O OD1 . ASN A 1 259 ? 35.588  20.505  -8.601  1.00 52.35  ? 268  ASN A OD1 1 
ATOM   1512  N ND2 . ASN A 1 259 ? 36.307  22.608  -8.533  1.00 53.01  ? 268  ASN A ND2 1 
ATOM   1513  N N   . ASP A 1 260 ? 31.124  22.199  -10.207 1.00 44.56  ? 269  ASP A N   1 
ATOM   1514  C CA  . ASP A 1 260 ? 29.764  22.697  -9.976  1.00 42.73  ? 269  ASP A CA  1 
ATOM   1515  C C   . ASP A 1 260 ? 28.855  21.574  -9.577  1.00 40.68  ? 269  ASP A C   1 
ATOM   1516  O O   . ASP A 1 260 ? 28.028  21.708  -8.681  1.00 39.34  ? 269  ASP A O   1 
ATOM   1517  C CB  . ASP A 1 260 ? 29.188  23.338  -11.220 1.00 43.32  ? 269  ASP A CB  1 
ATOM   1518  C CG  . ASP A 1 260 ? 29.922  24.582  -11.626 1.00 47.03  ? 269  ASP A CG  1 
ATOM   1519  O OD1 . ASP A 1 260 ? 30.591  25.205  -10.780 1.00 50.25  ? 269  ASP A OD1 1 
ATOM   1520  O OD2 . ASP A 1 260 ? 29.838  24.950  -12.812 1.00 50.94  ? 269  ASP A OD2 1 
ATOM   1521  N N   . GLN A 1 261 ? 29.006  20.464  -10.270 1.00 40.44  ? 270  GLN A N   1 
ATOM   1522  C CA  . GLN A 1 261 ? 28.322  19.269  -9.911  1.00 39.05  ? 270  GLN A CA  1 
ATOM   1523  C C   . GLN A 1 261 ? 28.526  18.967  -8.420  1.00 37.79  ? 270  GLN A C   1 
ATOM   1524  O O   . GLN A 1 261 ? 27.555  18.839  -7.672  1.00 36.25  ? 270  GLN A O   1 
ATOM   1525  C CB  . GLN A 1 261 ? 28.824  18.150  -10.770 1.00 40.61  ? 270  GLN A CB  1 
ATOM   1526  C CG  . GLN A 1 261 ? 27.756  17.250  -11.122 1.00 41.37  ? 270  GLN A CG  1 
ATOM   1527  C CD  . GLN A 1 261 ? 28.014  16.530  -12.390 1.00 45.84  ? 270  GLN A CD  1 
ATOM   1528  O OE1 . GLN A 1 261 ? 27.527  15.421  -12.534 1.00 48.07  ? 270  GLN A OE1 1 
ATOM   1529  N NE2 . GLN A 1 261 ? 28.771  17.137  -13.334 1.00 47.54  ? 270  GLN A NE2 1 
ATOM   1530  N N   . LYS A 1 262 ? 29.776  18.897  -7.972  1.00 38.17  ? 271  LYS A N   1 
ATOM   1531  C CA  . LYS A 1 262 ? 30.049  18.651  -6.571  1.00 37.00  ? 271  LYS A CA  1 
ATOM   1532  C C   . LYS A 1 262 ? 29.309  19.647  -5.703  1.00 35.26  ? 271  LYS A C   1 
ATOM   1533  O O   . LYS A 1 262 ? 28.669  19.277  -4.745  1.00 34.15  ? 271  LYS A O   1 
ATOM   1534  C CB  . LYS A 1 262 ? 31.546  18.673  -6.279  1.00 38.43  ? 271  LYS A CB  1 
ATOM   1535  C CG  . LYS A 1 262 ? 32.252  17.442  -6.774  1.00 40.05  ? 271  LYS A CG  1 
ATOM   1536  C CD  . LYS A 1 262 ? 33.693  17.328  -6.256  1.00 42.59  ? 271  LYS A CD  1 
ATOM   1537  C CE  . LYS A 1 262 ? 34.648  16.881  -7.394  1.00 44.99  ? 271  LYS A CE  1 
ATOM   1538  N NZ  . LYS A 1 262 ? 35.931  16.384  -6.905  1.00 45.78  ? 271  LYS A NZ  1 
ATOM   1539  N N   . LYS A 1 263 ? 29.372  20.915  -6.053  1.00 35.28  ? 272  LYS A N   1 
ATOM   1540  C CA  . LYS A 1 263 ? 28.709  21.925  -5.264  1.00 34.10  ? 272  LYS A CA  1 
ATOM   1541  C C   . LYS A 1 263 ? 27.213  21.736  -5.237  1.00 31.88  ? 272  LYS A C   1 
ATOM   1542  O O   . LYS A 1 263 ? 26.603  21.938  -4.203  1.00 30.81  ? 272  LYS A O   1 
ATOM   1543  C CB  . LYS A 1 263 ? 29.016  23.293  -5.821  1.00 35.63  ? 272  LYS A CB  1 
ATOM   1544  C CG  . LYS A 1 263 ? 28.136  24.409  -5.277  1.00 37.31  ? 272  LYS A CG  1 
ATOM   1545  C CD  . LYS A 1 263 ? 28.324  25.654  -6.131  1.00 43.43  ? 272  LYS A CD  1 
ATOM   1546  C CE  . LYS A 1 263 ? 27.931  26.949  -5.413  1.00 45.41  ? 272  LYS A CE  1 
ATOM   1547  N NZ  . LYS A 1 263 ? 28.584  28.120  -6.140  1.00 48.97  ? 272  LYS A NZ  1 
ATOM   1548  N N   . LEU A 1 264 ? 26.616  21.373  -6.371  1.00 31.00  ? 273  LEU A N   1 
ATOM   1549  C CA  . LEU A 1 264 ? 25.188  21.103  -6.408  1.00 28.60  ? 273  LEU A CA  1 
ATOM   1550  C C   . LEU A 1 264 ? 24.869  20.011  -5.454  1.00 27.45  ? 273  LEU A C   1 
ATOM   1551  O O   . LEU A 1 264 ? 24.023  20.180  -4.604  1.00 26.26  ? 273  LEU A O   1 
ATOM   1552  C CB  . LEU A 1 264 ? 24.741  20.629  -7.773  1.00 29.06  ? 273  LEU A CB  1 
ATOM   1553  C CG  . LEU A 1 264 ? 23.259  20.278  -7.985  1.00 25.88  ? 273  LEU A CG  1 
ATOM   1554  C CD1 . LEU A 1 264 ? 22.523  21.534  -8.134  1.00 24.74  ? 273  LEU A CD1 1 
ATOM   1555  C CD2 . LEU A 1 264 ? 23.057  19.489  -9.224  1.00 25.06  ? 273  LEU A CD2 1 
ATOM   1556  N N   . MET A 1 265 ? 25.537  18.883  -5.605  1.00 27.72  ? 274  MET A N   1 
ATOM   1557  C CA  . MET A 1 265 ? 25.306  17.799  -4.706  1.00 27.21  ? 274  MET A CA  1 
ATOM   1558  C C   . MET A 1 265 ? 25.464  18.196  -3.260  1.00 26.96  ? 274  MET A C   1 
ATOM   1559  O O   . MET A 1 265 ? 24.630  17.866  -2.453  1.00 26.60  ? 274  MET A O   1 
ATOM   1560  C CB  . MET A 1 265 ? 26.186  16.648  -5.049  1.00 28.05  ? 274  MET A CB  1 
ATOM   1561  C CG  . MET A 1 265 ? 25.706  16.014  -6.256  1.00 27.70  ? 274  MET A CG  1 
ATOM   1562  S SD  . MET A 1 265 ? 26.690  14.614  -6.672  1.00 28.76  ? 274  MET A SD  1 
ATOM   1563  C CE  . MET A 1 265 ? 26.302  13.348  -5.496  1.00 29.67  ? 274  MET A CE  1 
ATOM   1564  N N   . SER A 1 266 ? 26.488  18.960  -2.939  1.00 28.00  ? 275  SER A N   1 
ATOM   1565  C CA  . SER A 1 266 ? 26.693  19.400  -1.582  1.00 27.86  ? 275  SER A CA  1 
ATOM   1566  C C   . SER A 1 266 ? 25.574  20.276  -1.100  1.00 27.14  ? 275  SER A C   1 
ATOM   1567  O O   . SER A 1 266 ? 25.201  20.181  0.041   1.00 26.71  ? 275  SER A O   1 
ATOM   1568  C CB  . SER A 1 266 ? 27.998  20.155  -1.460  1.00 29.12  ? 275  SER A CB  1 
ATOM   1569  O OG  . SER A 1 266 ? 29.063  19.381  -1.963  1.00 30.29  ? 275  SER A OG  1 
ATOM   1570  N N   . ASN A 1 267 ? 25.011  21.129  -1.937  1.00 27.76  ? 276  ASN A N   1 
ATOM   1571  C CA  . ASN A 1 267 ? 23.913  21.940  -1.431  1.00 27.51  ? 276  ASN A CA  1 
ATOM   1572  C C   . ASN A 1 267 ? 22.578  21.269  -1.479  1.00 26.36  ? 276  ASN A C   1 
ATOM   1573  O O   . ASN A 1 267 ? 21.601  21.944  -1.383  1.00 26.20  ? 276  ASN A O   1 
ATOM   1574  C CB  . ASN A 1 267 ? 23.829  23.324  -2.078  1.00 28.22  ? 276  ASN A CB  1 
ATOM   1575  C CG  . ASN A 1 267 ? 24.920  24.271  -1.585  1.00 31.13  ? 276  ASN A CG  1 
ATOM   1576  O OD1 . ASN A 1 267 ? 25.101  24.490  -0.381  1.00 33.44  ? 276  ASN A OD1 1 
ATOM   1577  N ND2 . ASN A 1 267 ? 25.654  24.844  -2.522  1.00 34.15  ? 276  ASN A ND2 1 
ATOM   1578  N N   . ASN A 1 268 ? 22.529  19.950  -1.586  1.00 26.44  ? 277  ASN A N   1 
ATOM   1579  C CA  . ASN A 1 268 ? 21.258  19.237  -1.759  1.00 25.80  ? 277  ASN A CA  1 
ATOM   1580  C C   . ASN A 1 268 ? 21.177  17.842  -1.179  1.00 25.91  ? 277  ASN A C   1 
ATOM   1581  O O   . ASN A 1 268 ? 20.386  17.020  -1.646  1.00 25.90  ? 277  ASN A O   1 
ATOM   1582  C CB  . ASN A 1 268 ? 20.955  19.103  -3.220  1.00 26.08  ? 277  ASN A CB  1 
ATOM   1583  C CG  . ASN A 1 268 ? 20.334  20.292  -3.757  1.00 25.60  ? 277  ASN A CG  1 
ATOM   1584  O OD1 . ASN A 1 268 ? 19.172  20.505  -3.572  1.00 25.45  ? 277  ASN A OD1 1 
ATOM   1585  N ND2 . ASN A 1 268 ? 21.099  21.104  -4.417  1.00 27.17  ? 277  ASN A ND2 1 
ATOM   1586  N N   . VAL A 1 269 ? 22.002  17.590  -0.172  1.00 25.86  ? 278  VAL A N   1 
ATOM   1587  C CA  . VAL A 1 269 ? 22.088  16.319  0.540   1.00 25.72  ? 278  VAL A CA  1 
ATOM   1588  C C   . VAL A 1 269 ? 20.773  15.546  0.716   1.00 24.90  ? 278  VAL A C   1 
ATOM   1589  O O   . VAL A 1 269 ? 20.730  14.336  0.582   1.00 25.46  ? 278  VAL A O   1 
ATOM   1590  C CB  . VAL A 1 269 ? 22.619  16.582  1.915   1.00 25.50  ? 278  VAL A CB  1 
ATOM   1591  C CG1 . VAL A 1 269 ? 24.132  16.648  1.910   1.00 25.54  ? 278  VAL A CG1 1 
ATOM   1592  C CG2 . VAL A 1 269 ? 21.995  17.879  2.415   1.00 26.09  ? 278  VAL A CG2 1 
ATOM   1593  N N   . GLN A 1 270 ? 19.696  16.235  1.034   1.00 23.84  ? 279  GLN A N   1 
ATOM   1594  C CA  . GLN A 1 270 ? 18.422  15.552  1.201   1.00 23.31  ? 279  GLN A CA  1 
ATOM   1595  C C   . GLN A 1 270 ? 18.042  14.691  0.014   1.00 23.08  ? 279  GLN A C   1 
ATOM   1596  O O   . GLN A 1 270 ? 17.891  13.494  0.160   1.00 23.38  ? 279  GLN A O   1 
ATOM   1597  C CB  . GLN A 1 270 ? 17.315  16.550  1.460   1.00 23.10  ? 279  GLN A CB  1 
ATOM   1598  C CG  . GLN A 1 270 ? 16.202  15.960  2.310   1.00 25.32  ? 279  GLN A CG  1 
ATOM   1599  C CD  . GLN A 1 270 ? 15.050  16.937  2.560   1.00 28.83  ? 279  GLN A CD  1 
ATOM   1600  O OE1 . GLN A 1 270 ? 14.720  17.757  1.693   1.00 30.92  ? 279  GLN A OE1 1 
ATOM   1601  N NE2 . GLN A 1 270 ? 14.427  16.848  3.745   1.00 28.66  ? 279  GLN A NE2 1 
ATOM   1602  N N   . ILE A 1 271 ? 17.880  15.311  -1.151  1.00 22.44  ? 280  ILE A N   1 
ATOM   1603  C CA  . ILE A 1 271 ? 17.601  14.595  -2.406  1.00 22.35  ? 280  ILE A CA  1 
ATOM   1604  C C   . ILE A 1 271 ? 18.596  13.453  -2.661  1.00 23.08  ? 280  ILE A C   1 
ATOM   1605  O O   . ILE A 1 271 ? 18.242  12.293  -2.884  1.00 23.68  ? 280  ILE A O   1 
ATOM   1606  C CB  . ILE A 1 271 ? 17.694  15.573  -3.577  1.00 22.36  ? 280  ILE A CB  1 
ATOM   1607  C CG1 . ILE A 1 271 ? 16.824  16.785  -3.327  1.00 20.87  ? 280  ILE A CG1 1 
ATOM   1608  C CG2 . ILE A 1 271 ? 17.382  14.912  -4.896  1.00 22.60  ? 280  ILE A CG2 1 
ATOM   1609  C CD1 . ILE A 1 271 ? 15.531  16.694  -3.944  1.00 20.54  ? 280  ILE A CD1 1 
ATOM   1610  N N   . VAL A 1 272 ? 19.862  13.803  -2.618  1.00 23.00  ? 281  VAL A N   1 
ATOM   1611  C CA  . VAL A 1 272 ? 20.895  12.832  -2.814  1.00 23.94  ? 281  VAL A CA  1 
ATOM   1612  C C   . VAL A 1 272 ? 20.623  11.600  -1.975  1.00 24.28  ? 281  VAL A C   1 
ATOM   1613  O O   . VAL A 1 272 ? 20.547  10.510  -2.482  1.00 25.70  ? 281  VAL A O   1 
ATOM   1614  C CB  . VAL A 1 272 ? 22.251  13.388  -2.417  1.00 24.03  ? 281  VAL A CB  1 
ATOM   1615  C CG1 . VAL A 1 272 ? 23.301  12.397  -2.827  1.00 24.29  ? 281  VAL A CG1 1 
ATOM   1616  C CG2 . VAL A 1 272 ? 22.477  14.801  -3.012  1.00 23.07  ? 281  VAL A CG2 1 
ATOM   1617  N N   . ARG A 1 273 ? 20.470  11.784  -0.678  1.00 23.46  ? 282  ARG A N   1 
ATOM   1618  C CA  . ARG A 1 273 ? 20.207  10.666  0.187   1.00 23.64  ? 282  ARG A CA  1 
ATOM   1619  C C   . ARG A 1 273 ? 18.988  9.906   -0.334  1.00 24.74  ? 282  ARG A C   1 
ATOM   1620  O O   . ARG A 1 273 ? 19.059  8.709   -0.538  1.00 26.23  ? 282  ARG A O   1 
ATOM   1621  C CB  . ARG A 1 273 ? 19.983  11.136  1.609   1.00 22.12  ? 282  ARG A CB  1 
ATOM   1622  C CG  . ARG A 1 273 ? 21.128  11.849  2.195   1.00 20.61  ? 282  ARG A CG  1 
ATOM   1623  C CD  . ARG A 1 273 ? 21.117  11.673  3.655   1.00 19.20  ? 282  ARG A CD  1 
ATOM   1624  N NE  . ARG A 1 273 ? 22.116  12.498  4.297   1.00 18.92  ? 282  ARG A NE  1 
ATOM   1625  C CZ  . ARG A 1 273 ? 23.032  12.038  5.129   1.00 20.73  ? 282  ARG A CZ  1 
ATOM   1626  N NH1 . ARG A 1 273 ? 23.069  10.747  5.411   1.00 20.94  ? 282  ARG A NH1 1 
ATOM   1627  N NH2 . ARG A 1 273 ? 23.897  12.872  5.694   1.00 22.22  ? 282  ARG A NH2 1 
ATOM   1628  N N   . GLN A 1 274 ? 17.886  10.602  -0.593  1.00 24.36  ? 283  GLN A N   1 
ATOM   1629  C CA  . GLN A 1 274 ? 16.698  9.962   -1.085  1.00 25.09  ? 283  GLN A CA  1 
ATOM   1630  C C   . GLN A 1 274 ? 16.973  9.190   -2.348  1.00 26.10  ? 283  GLN A C   1 
ATOM   1631  O O   . GLN A 1 274 ? 16.321  8.194   -2.648  1.00 27.01  ? 283  GLN A O   1 
ATOM   1632  C CB  . GLN A 1 274 ? 15.662  11.012  -1.321  1.00 24.48  ? 283  GLN A CB  1 
ATOM   1633  C CG  . GLN A 1 274 ? 15.245  11.605  0.004   1.00 27.31  ? 283  GLN A CG  1 
ATOM   1634  C CD  . GLN A 1 274 ? 14.163  12.707  -0.103  1.00 31.31  ? 283  GLN A CD  1 
ATOM   1635  O OE1 . GLN A 1 274 ? 13.871  13.211  -1.213  1.00 34.53  ? 283  GLN A OE1 1 
ATOM   1636  N NE2 . GLN A 1 274 ? 13.581  13.097  1.054   1.00 29.94  ? 283  GLN A NE2 1 
ATOM   1637  N N   . GLN A 1 275 ? 17.981  9.624   -3.076  1.00 26.30  ? 284  GLN A N   1 
ATOM   1638  C CA  . GLN A 1 275 ? 18.303  8.962   -4.321  1.00 27.62  ? 284  GLN A CA  1 
ATOM   1639  C C   . GLN A 1 275 ? 19.292  7.808   -4.189  1.00 28.37  ? 284  GLN A C   1 
ATOM   1640  O O   . GLN A 1 275 ? 19.576  7.133   -5.155  1.00 29.17  ? 284  GLN A O   1 
ATOM   1641  C CB  . GLN A 1 275 ? 18.816  9.977   -5.310  1.00 27.76  ? 284  GLN A CB  1 
ATOM   1642  C CG  . GLN A 1 275 ? 17.732  10.750  -5.974  1.00 29.00  ? 284  GLN A CG  1 
ATOM   1643  C CD  . GLN A 1 275 ? 18.280  11.725  -7.013  1.00 32.17  ? 284  GLN A CD  1 
ATOM   1644  O OE1 . GLN A 1 275 ? 19.287  12.409  -6.759  1.00 32.75  ? 284  GLN A OE1 1 
ATOM   1645  N NE2 . GLN A 1 275 ? 17.625  11.791  -8.208  1.00 33.19  ? 284  GLN A NE2 1 
ATOM   1646  N N   . SER A 1 276 ? 19.789  7.578   -2.985  1.00 27.87  ? 285  SER A N   1 
ATOM   1647  C CA  . SER A 1 276 ? 20.857  6.631   -2.777  1.00 29.15  ? 285  SER A CA  1 
ATOM   1648  C C   . SER A 1 276 ? 20.372  5.416   -2.039  1.00 29.90  ? 285  SER A C   1 
ATOM   1649  O O   . SER A 1 276 ? 19.321  5.437   -1.433  1.00 29.61  ? 285  SER A O   1 
ATOM   1650  C CB  . SER A 1 276 ? 21.961  7.285   -1.968  1.00 28.72  ? 285  SER A CB  1 
ATOM   1651  O OG  . SER A 1 276 ? 22.312  8.569   -2.463  1.00 28.23  ? 285  SER A OG  1 
ATOM   1652  N N   . TYR A 1 277 ? 21.149  4.353   -2.082  1.00 31.61  ? 286  TYR A N   1 
ATOM   1653  C CA  . TYR A 1 277 ? 20.788  3.109   -1.433  1.00 32.97  ? 286  TYR A CA  1 
ATOM   1654  C C   . TYR A 1 277 ? 21.881  2.719   -0.449  1.00 33.83  ? 286  TYR A C   1 
ATOM   1655  O O   . TYR A 1 277 ? 23.009  3.178   -0.562  1.00 34.77  ? 286  TYR A O   1 
ATOM   1656  C CB  . TYR A 1 277 ? 20.635  2.002   -2.475  1.00 34.87  ? 286  TYR A CB  1 
ATOM   1657  C CG  . TYR A 1 277 ? 19.421  2.133   -3.339  1.00 35.33  ? 286  TYR A CG  1 
ATOM   1658  C CD1 . TYR A 1 277 ? 19.303  3.167   -4.237  1.00 36.59  ? 286  TYR A CD1 1 
ATOM   1659  C CD2 . TYR A 1 277 ? 18.396  1.216   -3.271  1.00 37.61  ? 286  TYR A CD2 1 
ATOM   1660  C CE1 . TYR A 1 277 ? 18.175  3.309   -5.041  1.00 38.27  ? 286  TYR A CE1 1 
ATOM   1661  C CE2 . TYR A 1 277 ? 17.256  1.337   -4.077  1.00 39.43  ? 286  TYR A CE2 1 
ATOM   1662  C CZ  . TYR A 1 277 ? 17.158  2.394   -4.962  1.00 39.01  ? 286  TYR A CZ  1 
ATOM   1663  O OH  . TYR A 1 277 ? 16.055  2.559   -5.774  1.00 40.61  ? 286  TYR A OH  1 
ATOM   1664  N N   . SER A 1 278 ? 21.567  1.863   0.511   1.00 34.12  ? 287  SER A N   1 
ATOM   1665  C CA  . SER A 1 278 ? 22.607  1.260   1.315   1.00 34.99  ? 287  SER A CA  1 
ATOM   1666  C C   . SER A 1 278 ? 22.407  -0.246  1.339   1.00 37.13  ? 287  SER A C   1 
ATOM   1667  O O   . SER A 1 278 ? 21.360  -0.739  1.706   1.00 37.19  ? 287  SER A O   1 
ATOM   1668  C CB  . SER A 1 278 ? 22.611  1.865   2.708   1.00 33.51  ? 287  SER A CB  1 
ATOM   1669  O OG  . SER A 1 278 ? 23.396  1.113   3.616   1.00 34.68  ? 287  SER A OG  1 
ATOM   1670  N N   . ILE A 1 279 ? 23.411  -0.973  0.900   1.00 39.46  ? 288  ILE A N   1 
ATOM   1671  C CA  . ILE A 1 279 ? 23.305  -2.401  0.818   1.00 42.49  ? 288  ILE A CA  1 
ATOM   1672  C C   . ILE A 1 279 ? 24.187  -2.979  1.859   1.00 44.34  ? 288  ILE A C   1 
ATOM   1673  O O   . ILE A 1 279 ? 25.340  -2.611  1.957   1.00 45.20  ? 288  ILE A O   1 
ATOM   1674  C CB  . ILE A 1 279 ? 23.888  -2.919  -0.463  1.00 44.20  ? 288  ILE A CB  1 
ATOM   1675  C CG1 . ILE A 1 279 ? 23.641  -1.925  -1.608  1.00 42.63  ? 288  ILE A CG1 1 
ATOM   1676  C CG2 . ILE A 1 279 ? 23.419  -4.358  -0.685  1.00 47.11  ? 288  ILE A CG2 1 
ATOM   1677  C CD1 . ILE A 1 279 ? 22.541  -2.295  -2.539  1.00 43.84  ? 288  ILE A CD1 1 
ATOM   1678  N N   . MET A 1 280 ? 23.663  -3.914  2.625   1.00 46.17  ? 289  MET A N   1 
ATOM   1679  C CA  . MET A 1 280 ? 24.455  -4.541  3.655   1.00 47.88  ? 289  MET A CA  1 
ATOM   1680  C C   . MET A 1 280 ? 25.415  -5.404  2.918   1.00 50.96  ? 289  MET A C   1 
ATOM   1681  O O   . MET A 1 280 ? 25.036  -6.022  1.934   1.00 52.51  ? 289  MET A O   1 
ATOM   1682  C CB  . MET A 1 280 ? 23.569  -5.403  4.499   1.00 48.47  ? 289  MET A CB  1 
ATOM   1683  C CG  . MET A 1 280 ? 24.143  -5.725  5.807   1.00 49.52  ? 289  MET A CG  1 
ATOM   1684  S SD  . MET A 1 280 ? 23.021  -6.846  6.650   1.00 52.57  ? 289  MET A SD  1 
ATOM   1685  C CE  . MET A 1 280 ? 22.783  -8.154  5.407   1.00 56.21  ? 289  MET A CE  1 
ATOM   1686  N N   . SER A 1 281 ? 26.663  -5.417  3.365   1.00 52.54  ? 290  SER A N   1 
ATOM   1687  C CA  . SER A 1 281 ? 27.696  -6.231  2.719   1.00 56.22  ? 290  SER A CA  1 
ATOM   1688  C C   . SER A 1 281 ? 28.128  -7.462  3.537   1.00 58.65  ? 290  SER A C   1 
ATOM   1689  O O   . SER A 1 281 ? 27.859  -8.589  3.112   1.00 61.20  ? 290  SER A O   1 
ATOM   1690  C CB  . SER A 1 281 ? 28.900  -5.388  2.322   1.00 56.31  ? 290  SER A CB  1 
ATOM   1691  O OG  . SER A 1 281 ? 29.909  -6.213  1.749   1.00 60.85  ? 290  SER A OG  1 
ATOM   1692  N N   . ILE A 1 282 ? 28.803  -7.263  4.676   1.00 58.37  ? 291  ILE A N   1 
ATOM   1693  C CA  . ILE A 1 282 ? 29.050  -8.380  5.603   1.00 60.52  ? 291  ILE A CA  1 
ATOM   1694  C C   . ILE A 1 282 ? 29.075  -8.073  7.085   1.00 58.88  ? 291  ILE A C   1 
ATOM   1695  O O   . ILE A 1 282 ? 29.626  -7.071  7.543   1.00 56.53  ? 291  ILE A O   1 
ATOM   1696  C CB  . ILE A 1 282 ? 30.300  -9.218  5.261   1.00 64.02  ? 291  ILE A CB  1 
ATOM   1697  C CG1 . ILE A 1 282 ? 31.365  -8.363  4.540   1.00 63.74  ? 291  ILE A CG1 1 
ATOM   1698  C CG2 . ILE A 1 282 ? 29.889  -10.517 4.507   1.00 67.55  ? 291  ILE A CG2 1 
ATOM   1699  C CD1 . ILE A 1 282 ? 32.373  -7.707  5.484   1.00 62.96  ? 291  ILE A CD1 1 
ATOM   1700  N N   . ILE A 1 283 ? 28.463  -8.990  7.820   1.00 60.17  ? 292  ILE A N   1 
ATOM   1701  C CA  . ILE A 1 283 ? 28.281  -8.860  9.255   1.00 59.49  ? 292  ILE A CA  1 
ATOM   1702  C C   . ILE A 1 283 ? 29.015  -9.957  9.967   1.00 62.03  ? 292  ILE A C   1 
ATOM   1703  O O   . ILE A 1 283 ? 28.876  -11.146 9.679   1.00 64.20  ? 292  ILE A O   1 
ATOM   1704  C CB  . ILE A 1 283 ? 26.797  -8.995  9.743   1.00 58.32  ? 292  ILE A CB  1 
ATOM   1705  C CG1 . ILE A 1 283 ? 25.824  -9.322  8.608   1.00 60.02  ? 292  ILE A CG1 1 
ATOM   1706  C CG2 . ILE A 1 283 ? 26.374  -7.804  10.628  1.00 54.58  ? 292  ILE A CG2 1 
ATOM   1707  C CD1 . ILE A 1 283 ? 25.933  -8.450  7.382   1.00 61.52  ? 292  ILE A CD1 1 
ATOM   1708  N N   . LYS A 1 284 ? 29.783  -9.512  10.932  1.00 61.71  ? 293  LYS A N   1 
ATOM   1709  C CA  . LYS A 1 284 ? 30.498  -10.369 11.793  1.00 64.44  ? 293  LYS A CA  1 
ATOM   1710  C C   . LYS A 1 284 ? 30.206  -9.769  13.126  1.00 62.72  ? 293  LYS A C   1 
ATOM   1711  O O   . LYS A 1 284 ? 29.889  -8.580  13.213  1.00 59.91  ? 293  LYS A O   1 
ATOM   1712  C CB  . LYS A 1 284 ? 31.988  -10.262 11.494  1.00 66.09  ? 293  LYS A CB  1 
ATOM   1713  C CG  . LYS A 1 284 ? 32.368  -10.506 10.035  1.00 68.61  ? 293  LYS A CG  1 
ATOM   1714  C CD  . LYS A 1 284 ? 33.741  -11.150 9.906   1.00 72.93  ? 293  LYS A CD  1 
ATOM   1715  C CE  . LYS A 1 284 ? 33.994  -11.555 8.474   1.00 76.26  ? 293  LYS A CE  1 
ATOM   1716  N NZ  . LYS A 1 284 ? 34.868  -12.734 8.453   1.00 81.67  ? 293  LYS A NZ  1 
ATOM   1717  N N   . GLU A 1 285 ? 30.333  -10.581 14.169  1.00 64.84  ? 294  GLU A N   1 
ATOM   1718  C CA  . GLU A 1 285 ? 29.986  -10.150 15.527  1.00 63.99  ? 294  GLU A CA  1 
ATOM   1719  C C   . GLU A 1 285 ? 30.554  -8.775  15.869  1.00 60.89  ? 294  GLU A C   1 
ATOM   1720  O O   . GLU A 1 285 ? 29.885  -7.963  16.503  1.00 58.34  ? 294  GLU A O   1 
ATOM   1721  C CB  . GLU A 1 285 ? 30.398  -11.201 16.577  1.00 66.85  ? 294  GLU A CB  1 
ATOM   1722  C CG  . GLU A 1 285 ? 29.402  -12.381 16.698  1.00 72.42  ? 294  GLU A CG  1 
ATOM   1723  C CD  . GLU A 1 285 ? 29.764  -13.408 17.789  1.00 78.61  ? 294  GLU A CD  1 
ATOM   1724  O OE1 . GLU A 1 285 ? 29.662  -13.064 18.999  1.00 77.45  ? 294  GLU A OE1 1 
ATOM   1725  O OE2 . GLU A 1 285 ? 30.131  -14.565 17.425  1.00 83.90  ? 294  GLU A OE2 1 
ATOM   1726  N N   . GLU A 1 286 ? 31.775  -8.514  15.421  1.00 61.13  ? 295  GLU A N   1 
ATOM   1727  C CA  . GLU A 1 286 ? 32.494  -7.315  15.825  1.00 59.18  ? 295  GLU A CA  1 
ATOM   1728  C C   . GLU A 1 286 ? 32.748  -6.345  14.695  1.00 57.13  ? 295  GLU A C   1 
ATOM   1729  O O   . GLU A 1 286 ? 33.369  -5.304  14.912  1.00 55.81  ? 295  GLU A O   1 
ATOM   1730  C CB  . GLU A 1 286 ? 33.819  -7.655  16.545  1.00 61.65  ? 295  GLU A CB  1 
ATOM   1731  C CG  . GLU A 1 286 ? 34.399  -9.079  16.338  1.00 68.41  ? 295  GLU A CG  1 
ATOM   1732  C CD  . GLU A 1 286 ? 34.594  -9.477  14.868  1.00 74.13  ? 295  GLU A CD  1 
ATOM   1733  O OE1 . GLU A 1 286 ? 33.697  -10.159 14.330  1.00 75.97  ? 295  GLU A OE1 1 
ATOM   1734  O OE2 . GLU A 1 286 ? 35.630  -9.122  14.258  1.00 75.96  ? 295  GLU A OE2 1 
ATOM   1735  N N   . VAL A 1 287 ? 32.297  -6.684  13.489  1.00 56.75  ? 296  VAL A N   1 
ATOM   1736  C CA  . VAL A 1 287 ? 32.389  -5.750  12.380  1.00 54.73  ? 296  VAL A CA  1 
ATOM   1737  C C   . VAL A 1 287 ? 31.237  -5.898  11.446  1.00 53.72  ? 296  VAL A C   1 
ATOM   1738  O O   . VAL A 1 287 ? 30.850  -7.013  11.078  1.00 55.61  ? 296  VAL A O   1 
ATOM   1739  C CB  . VAL A 1 287 ? 33.616  -5.919  11.505  1.00 56.69  ? 296  VAL A CB  1 
ATOM   1740  C CG1 . VAL A 1 287 ? 33.858  -4.631  10.773  1.00 55.13  ? 296  VAL A CG1 1 
ATOM   1741  C CG2 . VAL A 1 287 ? 34.834  -6.276  12.307  1.00 59.41  ? 296  VAL A CG2 1 
ATOM   1742  N N   . LEU A 1 288 ? 30.720  -4.740  11.046  1.00 50.71  ? 297  LEU A N   1 
ATOM   1743  C CA  . LEU A 1 288 ? 29.675  -4.628  10.040  1.00 49.04  ? 297  LEU A CA  1 
ATOM   1744  C C   . LEU A 1 288 ? 30.166  -3.759  8.887   1.00 47.94  ? 297  LEU A C   1 
ATOM   1745  O O   . LEU A 1 288 ? 30.664  -2.654  9.103   1.00 46.86  ? 297  LEU A O   1 
ATOM   1746  C CB  . LEU A 1 288 ? 28.430  -4.000  10.653  1.00 46.24  ? 297  LEU A CB  1 
ATOM   1747  C CG  . LEU A 1 288 ? 27.415  -3.586  9.600   1.00 45.30  ? 297  LEU A CG  1 
ATOM   1748  C CD1 . LEU A 1 288 ? 26.937  -4.799  8.831   1.00 48.40  ? 297  LEU A CD1 1 
ATOM   1749  C CD2 . LEU A 1 288 ? 26.246  -2.879  10.230  1.00 42.98  ? 297  LEU A CD2 1 
ATOM   1750  N N   . ALA A 1 289 ? 30.022  -4.250  7.665   1.00 48.08  ? 298  ALA A N   1 
ATOM   1751  C CA  . ALA A 1 289 ? 30.431  -3.465  6.521   1.00 46.80  ? 298  ALA A CA  1 
ATOM   1752  C C   . ALA A 1 289 ? 29.333  -3.509  5.522   1.00 45.75  ? 298  ALA A C   1 
ATOM   1753  O O   . ALA A 1 289 ? 28.749  -4.554  5.303   1.00 47.29  ? 298  ALA A O   1 
ATOM   1754  C CB  . ALA A 1 289 ? 31.680  -4.031  5.923   1.00 49.64  ? 298  ALA A CB  1 
ATOM   1755  N N   . TYR A 1 290 ? 29.072  -2.375  4.900   1.00 43.27  ? 299  TYR A N   1 
ATOM   1756  C CA  . TYR A 1 290 ? 28.021  -2.273  3.909   1.00 42.01  ? 299  TYR A CA  1 
ATOM   1757  C C   . TYR A 1 290 ? 28.414  -1.314  2.803   1.00 41.20  ? 299  TYR A C   1 
ATOM   1758  O O   . TYR A 1 290 ? 29.314  -0.520  2.948   1.00 41.16  ? 299  TYR A O   1 
ATOM   1759  C CB  . TYR A 1 290 ? 26.742  -1.809  4.575   1.00 39.58  ? 299  TYR A CB  1 
ATOM   1760  C CG  . TYR A 1 290 ? 26.924  -0.557  5.389   1.00 37.57  ? 299  TYR A CG  1 
ATOM   1761  C CD1 . TYR A 1 290 ? 26.630  0.676   4.856   1.00 36.31  ? 299  TYR A CD1 1 
ATOM   1762  C CD2 . TYR A 1 290 ? 27.388  -0.600  6.693   1.00 37.09  ? 299  TYR A CD2 1 
ATOM   1763  C CE1 . TYR A 1 290 ? 26.795  1.848   5.599   1.00 34.07  ? 299  TYR A CE1 1 
ATOM   1764  C CE2 . TYR A 1 290 ? 27.544  0.566   7.437   1.00 34.95  ? 299  TYR A CE2 1 
ATOM   1765  C CZ  . TYR A 1 290 ? 27.252  1.781   6.875   1.00 33.13  ? 299  TYR A CZ  1 
ATOM   1766  O OH  . TYR A 1 290 ? 27.407  2.945   7.569   1.00 30.61  ? 299  TYR A OH  1 
ATOM   1767  N N   . VAL A 1 291 ? 27.736  -1.388  1.685   1.00 40.99  ? 300  VAL A N   1 
ATOM   1768  C CA  . VAL A 1 291 ? 28.082  -0.540  0.586   1.00 40.41  ? 300  VAL A CA  1 
ATOM   1769  C C   . VAL A 1 291 ? 27.031  0.497   0.415   1.00 38.17  ? 300  VAL A C   1 
ATOM   1770  O O   . VAL A 1 291 ? 25.855  0.192   0.257   1.00 38.10  ? 300  VAL A O   1 
ATOM   1771  C CB  . VAL A 1 291 ? 28.191  -1.328  -0.694  1.00 42.32  ? 300  VAL A CB  1 
ATOM   1772  C CG1 . VAL A 1 291 ? 28.105  -0.409  -1.934  1.00 41.54  ? 300  VAL A CG1 1 
ATOM   1773  C CG2 . VAL A 1 291 ? 29.479  -2.095  -0.664  1.00 45.66  ? 300  VAL A CG2 1 
ATOM   1774  N N   . VAL A 1 292 ? 27.470  1.736   0.436   1.00 36.88  ? 301  VAL A N   1 
ATOM   1775  C CA  . VAL A 1 292 ? 26.628  2.841   0.064   1.00 34.93  ? 301  VAL A CA  1 
ATOM   1776  C C   . VAL A 1 292 ? 26.678  3.125   -1.443  1.00 35.64  ? 301  VAL A C   1 
ATOM   1777  O O   . VAL A 1 292 ? 27.719  2.929   -2.106  1.00 37.84  ? 301  VAL A O   1 
ATOM   1778  C CB  . VAL A 1 292 ? 27.079  4.034   0.807   1.00 33.27  ? 301  VAL A CB  1 
ATOM   1779  C CG1 . VAL A 1 292 ? 26.779  5.274   0.012   1.00 33.22  ? 301  VAL A CG1 1 
ATOM   1780  C CG2 . VAL A 1 292 ? 26.391  4.054   2.113   1.00 32.04  ? 301  VAL A CG2 1 
ATOM   1781  N N   . GLN A 1 293 ? 25.559  3.599   -1.977  1.00 34.04  ? 302  GLN A N   1 
ATOM   1782  C CA  . GLN A 1 293 ? 25.407  3.702   -3.411  1.00 34.53  ? 302  GLN A CA  1 
ATOM   1783  C C   . GLN A 1 293 ? 24.846  5.045   -3.786  1.00 32.05  ? 302  GLN A C   1 
ATOM   1784  O O   . GLN A 1 293 ? 23.691  5.302   -3.571  1.00 30.81  ? 302  GLN A O   1 
ATOM   1785  C CB  . GLN A 1 293 ? 24.492  2.582   -3.895  1.00 35.68  ? 302  GLN A CB  1 
ATOM   1786  C CG  . GLN A 1 293 ? 24.185  2.661   -5.353  1.00 38.43  ? 302  GLN A CG  1 
ATOM   1787  C CD  . GLN A 1 293 ? 23.700  1.347   -5.924  1.00 43.31  ? 302  GLN A CD  1 
ATOM   1788  O OE1 . GLN A 1 293 ? 24.098  0.260   -5.477  1.00 45.05  ? 302  GLN A OE1 1 
ATOM   1789  N NE2 . GLN A 1 293 ? 22.839  1.438   -6.944  1.00 44.73  ? 302  GLN A NE2 1 
ATOM   1790  N N   . LEU A 1 294 ? 25.664  5.907   -4.350  1.00 31.45  ? 303  LEU A N   1 
ATOM   1791  C CA  . LEU A 1 294 ? 25.255  7.274   -4.543  1.00 29.46  ? 303  LEU A CA  1 
ATOM   1792  C C   . LEU A 1 294 ? 25.002  7.522   -5.981  1.00 30.08  ? 303  LEU A C   1 
ATOM   1793  O O   . LEU A 1 294 ? 25.495  6.787   -6.809  1.00 32.36  ? 303  LEU A O   1 
ATOM   1794  C CB  . LEU A 1 294 ? 26.336  8.207   -4.055  1.00 28.98  ? 303  LEU A CB  1 
ATOM   1795  C CG  . LEU A 1 294 ? 26.712  7.939   -2.610  1.00 28.38  ? 303  LEU A CG  1 
ATOM   1796  C CD1 . LEU A 1 294 ? 27.543  9.054   -2.150  1.00 27.61  ? 303  LEU A CD1 1 
ATOM   1797  C CD2 . LEU A 1 294 ? 25.509  7.861   -1.730  1.00 27.49  ? 303  LEU A CD2 1 
ATOM   1798  N N   . PRO A 1 295 ? 24.227  8.560   -6.299  1.00 28.70  ? 304  PRO A N   1 
ATOM   1799  C CA  . PRO A 1 295 ? 23.938  8.861   -7.699  1.00 29.34  ? 304  PRO A CA  1 
ATOM   1800  C C   . PRO A 1 295 ? 25.038  9.683   -8.341  1.00 30.09  ? 304  PRO A C   1 
ATOM   1801  O O   . PRO A 1 295 ? 25.728  10.414  -7.645  1.00 29.74  ? 304  PRO A O   1 
ATOM   1802  C CB  . PRO A 1 295 ? 22.653  9.682   -7.626  1.00 27.33  ? 304  PRO A CB  1 
ATOM   1803  C CG  . PRO A 1 295 ? 22.685  10.309  -6.317  1.00 26.22  ? 304  PRO A CG  1 
ATOM   1804  C CD  . PRO A 1 295 ? 23.447  9.403   -5.388  1.00 26.73  ? 304  PRO A CD  1 
ATOM   1805  N N   . LEU A 1 296 ? 25.186  9.551   -9.654  1.00 31.42  ? 305  LEU A N   1 
ATOM   1806  C CA  . LEU A 1 296 ? 26.086  10.366  -10.428 1.00 31.99  ? 305  LEU A CA  1 
ATOM   1807  C C   . LEU A 1 296 ? 25.315  10.925  -11.591 1.00 31.97  ? 305  LEU A C   1 
ATOM   1808  O O   . LEU A 1 296 ? 24.662  10.172  -12.330 1.00 32.59  ? 305  LEU A O   1 
ATOM   1809  C CB  . LEU A 1 296 ? 27.198  9.496   -10.965 1.00 34.14  ? 305  LEU A CB  1 
ATOM   1810  C CG  . LEU A 1 296 ? 28.129  8.840   -9.961  1.00 35.08  ? 305  LEU A CG  1 
ATOM   1811  C CD1 . LEU A 1 296 ? 29.200  8.138   -10.688 1.00 37.56  ? 305  LEU A CD1 1 
ATOM   1812  C CD2 . LEU A 1 296 ? 28.760  9.891   -9.134  1.00 35.59  ? 305  LEU A CD2 1 
ATOM   1813  N N   . TYR A 1 297 ? 25.393  12.243  -11.759 1.00 31.34  ? 306  TYR A N   1 
ATOM   1814  C CA  . TYR A 1 297 ? 24.690  12.918  -12.861 1.00 31.31  ? 306  TYR A CA  1 
ATOM   1815  C C   . TYR A 1 297 ? 25.532  13.150  -14.110 1.00 32.82  ? 306  TYR A C   1 
ATOM   1816  O O   . TYR A 1 297 ? 26.606  13.710  -14.049 1.00 33.41  ? 306  TYR A O   1 
ATOM   1817  C CB  . TYR A 1 297 ? 24.076  14.239  -12.398 1.00 29.79  ? 306  TYR A CB  1 
ATOM   1818  C CG  . TYR A 1 297 ? 23.370  14.084  -11.102 1.00 28.97  ? 306  TYR A CG  1 
ATOM   1819  C CD1 . TYR A 1 297 ? 23.898  14.610  -9.930  1.00 29.32  ? 306  TYR A CD1 1 
ATOM   1820  C CD2 . TYR A 1 297 ? 22.199  13.353  -11.019 1.00 30.44  ? 306  TYR A CD2 1 
ATOM   1821  C CE1 . TYR A 1 297 ? 23.253  14.436  -8.673  1.00 28.49  ? 306  TYR A CE1 1 
ATOM   1822  C CE2 . TYR A 1 297 ? 21.540  13.162  -9.759  1.00 30.44  ? 306  TYR A CE2 1 
ATOM   1823  C CZ  . TYR A 1 297 ? 22.087  13.707  -8.600  1.00 28.37  ? 306  TYR A CZ  1 
ATOM   1824  O OH  . TYR A 1 297 ? 21.466  13.517  -7.404  1.00 24.78  ? 306  TYR A OH  1 
ATOM   1825  N N   . GLY A 1 298 ? 25.023  12.737  -15.256 1.00 33.58  ? 307  GLY A N   1 
ATOM   1826  C CA  . GLY A 1 298 ? 25.723  12.968  -16.483 1.00 34.95  ? 307  GLY A CA  1 
ATOM   1827  C C   . GLY A 1 298 ? 25.434  14.314  -17.105 1.00 34.59  ? 307  GLY A C   1 
ATOM   1828  O O   . GLY A 1 298 ? 25.985  14.587  -18.142 1.00 36.37  ? 307  GLY A O   1 
ATOM   1829  N N   . VAL A 1 299 ? 24.570  15.146  -16.515 1.00 32.87  ? 308  VAL A N   1 
ATOM   1830  C CA  . VAL A 1 299 ? 24.345  16.529  -16.990 1.00 32.57  ? 308  VAL A CA  1 
ATOM   1831  C C   . VAL A 1 299 ? 23.707  17.358  -15.936 1.00 31.55  ? 308  VAL A C   1 
ATOM   1832  O O   . VAL A 1 299 ? 22.866  16.893  -15.200 1.00 30.77  ? 308  VAL A O   1 
ATOM   1833  C CB  . VAL A 1 299 ? 23.374  16.607  -18.111 1.00 31.87  ? 308  VAL A CB  1 
ATOM   1834  C CG1 . VAL A 1 299 ? 24.064  16.613  -19.382 1.00 33.80  ? 308  VAL A CG1 1 
ATOM   1835  C CG2 . VAL A 1 299 ? 22.497  15.466  -18.054 1.00 31.94  ? 308  VAL A CG2 1 
ATOM   1836  N N   . ILE A 1 300 ? 24.076  18.618  -15.882 1.00 32.27  ? 309  ILE A N   1 
ATOM   1837  C CA  . ILE A 1 300 ? 23.536  19.518  -14.867 1.00 31.51  ? 309  ILE A CA  1 
ATOM   1838  C C   . ILE A 1 300 ? 23.038  20.742  -15.605 1.00 31.87  ? 309  ILE A C   1 
ATOM   1839  O O   . ILE A 1 300 ? 23.493  21.007  -16.715 1.00 33.82  ? 309  ILE A O   1 
ATOM   1840  C CB  . ILE A 1 300 ? 24.669  19.927  -13.919 1.00 31.71  ? 309  ILE A CB  1 
ATOM   1841  C CG1 . ILE A 1 300 ? 25.211  18.707  -13.236 1.00 33.02  ? 309  ILE A CG1 1 
ATOM   1842  C CG2 . ILE A 1 300 ? 24.229  20.847  -12.864 1.00 30.17  ? 309  ILE A CG2 1 
ATOM   1843  C CD1 . ILE A 1 300 ? 24.123  17.916  -12.581 1.00 33.79  ? 309  ILE A CD1 1 
ATOM   1844  N N   . ASP A 1 301 ? 22.107  21.475  -15.022 1.00 30.70  ? 310  ASP A N   1 
ATOM   1845  C CA  . ASP A 1 301 ? 21.818  22.836  -15.450 1.00 31.07  ? 310  ASP A CA  1 
ATOM   1846  C C   . ASP A 1 301 ? 21.142  22.993  -16.824 1.00 31.85  ? 310  ASP A C   1 
ATOM   1847  O O   . ASP A 1 301 ? 21.074  24.089  -17.359 1.00 32.56  ? 310  ASP A O   1 
ATOM   1848  C CB  . ASP A 1 301 ? 23.078  23.711  -15.359 1.00 32.24  ? 310  ASP A CB  1 
ATOM   1849  C CG  . ASP A 1 301 ? 23.678  23.778  -13.932 1.00 32.34  ? 310  ASP A CG  1 
ATOM   1850  O OD1 . ASP A 1 301 ? 24.883  23.582  -13.725 1.00 33.28  ? 310  ASP A OD1 1 
ATOM   1851  O OD2 . ASP A 1 301 ? 22.959  24.049  -12.979 1.00 31.79  ? 310  ASP A OD2 1 
ATOM   1852  N N   . THR A 1 302 ? 20.621  21.915  -17.391 1.00 32.02  ? 311  THR A N   1 
ATOM   1853  C CA  . THR A 1 302 ? 19.809  21.989  -18.588 1.00 32.49  ? 311  THR A CA  1 
ATOM   1854  C C   . THR A 1 302 ? 18.453  22.339  -18.126 1.00 31.94  ? 311  THR A C   1 
ATOM   1855  O O   . THR A 1 302 ? 18.098  21.905  -17.027 1.00 31.80  ? 311  THR A O   1 
ATOM   1856  C CB  . THR A 1 302 ? 19.538  20.644  -19.051 1.00 32.52  ? 311  THR A CB  1 
ATOM   1857  O OG1 . THR A 1 302 ? 20.668  19.841  -18.811 1.00 33.60  ? 311  THR A OG1 1 
ATOM   1858  C CG2 . THR A 1 302 ? 19.367  20.681  -20.436 1.00 35.81  ? 311  THR A CG2 1 
ATOM   1859  N N   . PRO A 1 303 ? 17.646  23.067  -18.942 1.00 32.23  ? 312  PRO A N   1 
ATOM   1860  C CA  . PRO A 1 303 ? 16.312  23.456  -18.490 1.00 31.51  ? 312  PRO A CA  1 
ATOM   1861  C C   . PRO A 1 303 ? 15.343  22.258  -18.493 1.00 31.53  ? 312  PRO A C   1 
ATOM   1862  O O   . PRO A 1 303 ? 15.463  21.387  -19.361 1.00 32.14  ? 312  PRO A O   1 
ATOM   1863  C CB  . PRO A 1 303 ? 15.913  24.503  -19.518 1.00 31.71  ? 312  PRO A CB  1 
ATOM   1864  C CG  . PRO A 1 303 ? 16.554  24.068  -20.710 1.00 32.34  ? 312  PRO A CG  1 
ATOM   1865  C CD  . PRO A 1 303 ? 17.895  23.619  -20.273 1.00 33.24  ? 312  PRO A CD  1 
ATOM   1866  N N   . CYS A 1 304 ? 14.454  22.179  -17.492 1.00 30.83  ? 313  CYS A N   1 
ATOM   1867  C CA  . CYS A 1 304 ? 13.332  21.247  -17.557 1.00 30.89  ? 313  CYS A CA  1 
ATOM   1868  C C   . CYS A 1 304 ? 12.054  21.989  -17.392 1.00 29.99  ? 313  CYS A C   1 
ATOM   1869  O O   . CYS A 1 304 ? 12.062  23.170  -17.054 1.00 29.58  ? 313  CYS A O   1 
ATOM   1870  C CB  . CYS A 1 304 ? 13.336  20.208  -16.466 1.00 30.72  ? 313  CYS A CB  1 
ATOM   1871  S SG  . CYS A 1 304 ? 14.819  19.537  -16.046 1.00 33.05  ? 313  CYS A SG  1 
ATOM   1872  N N   . TRP A 1 305 ? 10.961  21.256  -17.607 1.00 29.87  ? 314  TRP A N   1 
ATOM   1873  C CA  . TRP A 1 305 ? 9.613   21.762  -17.438 1.00 29.60  ? 314  TRP A CA  1 
ATOM   1874  C C   . TRP A 1 305 ? 8.622   20.668  -17.142 1.00 29.06  ? 314  TRP A C   1 
ATOM   1875  O O   . TRP A 1 305 ? 8.792   19.553  -17.581 1.00 29.62  ? 314  TRP A O   1 
ATOM   1876  C CB  . TRP A 1 305 ? 9.178   22.512  -18.678 1.00 30.51  ? 314  TRP A CB  1 
ATOM   1877  C CG  . TRP A 1 305 ? 9.279   21.744  -19.945 1.00 32.49  ? 314  TRP A CG  1 
ATOM   1878  C CD1 . TRP A 1 305 ? 8.284   21.091  -20.560 1.00 34.18  ? 314  TRP A CD1 1 
ATOM   1879  C CD2 . TRP A 1 305 ? 10.430  21.590  -20.777 1.00 34.35  ? 314  TRP A CD2 1 
ATOM   1880  N NE1 . TRP A 1 305 ? 8.724   20.520  -21.725 1.00 35.66  ? 314  TRP A NE1 1 
ATOM   1881  C CE2 . TRP A 1 305 ? 10.043  20.813  -21.882 1.00 35.34  ? 314  TRP A CE2 1 
ATOM   1882  C CE3 . TRP A 1 305 ? 11.755  22.025  -20.687 1.00 35.88  ? 314  TRP A CE3 1 
ATOM   1883  C CZ2 . TRP A 1 305 ? 10.917  20.448  -22.888 1.00 37.24  ? 314  TRP A CZ2 1 
ATOM   1884  C CZ3 . TRP A 1 305 ? 12.641  21.664  -21.693 1.00 38.23  ? 314  TRP A CZ3 1 
ATOM   1885  C CH2 . TRP A 1 305 ? 12.212  20.877  -22.789 1.00 38.95  ? 314  TRP A CH2 1 
ATOM   1886  N N   . LYS A 1 306 ? 7.583   20.992  -16.388 1.00 28.24  ? 315  LYS A N   1 
ATOM   1887  C CA  . LYS A 1 306 ? 6.560   20.006  -16.061 1.00 28.01  ? 315  LYS A CA  1 
ATOM   1888  C C   . LYS A 1 306 ? 5.326   20.339  -16.807 1.00 28.66  ? 315  LYS A C   1 
ATOM   1889  O O   . LYS A 1 306 ? 4.887   21.484  -16.814 1.00 28.83  ? 315  LYS A O   1 
ATOM   1890  C CB  . LYS A 1 306 ? 6.224   19.979  -14.583 1.00 27.03  ? 315  LYS A CB  1 
ATOM   1891  C CG  . LYS A 1 306 ? 5.547   18.728  -14.170 1.00 26.95  ? 315  LYS A CG  1 
ATOM   1892  C CD  . LYS A 1 306 ? 5.304   18.709  -12.689 1.00 28.02  ? 315  LYS A CD  1 
ATOM   1893  C CE  . LYS A 1 306 ? 4.933   17.302  -12.199 1.00 29.21  ? 315  LYS A CE  1 
ATOM   1894  N NZ  . LYS A 1 306 ? 4.061   17.329  -10.972 1.00 30.48  ? 315  LYS A NZ  1 
ATOM   1895  N N   . LEU A 1 307 ? 4.760   19.318  -17.428 1.00 29.47  ? 316  LEU A N   1 
ATOM   1896  C CA  . LEU A 1 307 ? 3.569   19.467  -18.232 1.00 30.68  ? 316  LEU A CA  1 
ATOM   1897  C C   . LEU A 1 307 ? 2.320   18.923  -17.541 1.00 31.77  ? 316  LEU A C   1 
ATOM   1898  O O   . LEU A 1 307 ? 2.292   17.739  -17.161 1.00 32.66  ? 316  LEU A O   1 
ATOM   1899  C CB  . LEU A 1 307 ? 3.759   18.696  -19.517 1.00 31.26  ? 316  LEU A CB  1 
ATOM   1900  C CG  . LEU A 1 307 ? 2.551   18.604  -20.429 1.00 31.83  ? 316  LEU A CG  1 
ATOM   1901  C CD1 . LEU A 1 307 ? 2.101   19.969  -20.849 1.00 31.66  ? 316  LEU A CD1 1 
ATOM   1902  C CD2 . LEU A 1 307 ? 2.879   17.762  -21.619 1.00 32.73  ? 316  LEU A CD2 1 
ATOM   1903  N N   . HIS A 1 308 ? 1.282   19.754  -17.391 1.00 32.27  ? 317  HIS A N   1 
ATOM   1904  C CA  . HIS A 1 308 ? 0.005   19.267  -16.867 1.00 32.97  ? 317  HIS A CA  1 
ATOM   1905  C C   . HIS A 1 308 ? -1.004  19.467  -17.933 1.00 33.39  ? 317  HIS A C   1 
ATOM   1906  O O   . HIS A 1 308 ? -0.826  20.279  -18.819 1.00 33.69  ? 317  HIS A O   1 
ATOM   1907  C CB  . HIS A 1 308 ? -0.426  20.010  -15.629 1.00 32.94  ? 317  HIS A CB  1 
ATOM   1908  C CG  . HIS A 1 308 ? 0.696   20.350  -14.709 1.00 34.32  ? 317  HIS A CG  1 
ATOM   1909  N ND1 . HIS A 1 308 ? 0.951   19.633  -13.562 1.00 36.34  ? 317  HIS A ND1 1 
ATOM   1910  C CD2 . HIS A 1 308 ? 1.628   21.334  -14.761 1.00 35.09  ? 317  HIS A CD2 1 
ATOM   1911  C CE1 . HIS A 1 308 ? 1.983   20.170  -12.937 1.00 36.59  ? 317  HIS A CE1 1 
ATOM   1912  N NE2 . HIS A 1 308 ? 2.418   21.198  -13.649 1.00 35.72  ? 317  HIS A NE2 1 
ATOM   1913  N N   . THR A 1 309 ? -2.096  18.751  -17.806 1.00 33.76  ? 318  THR A N   1 
ATOM   1914  C CA  . THR A 1 309 ? -2.940  18.488  -18.923 1.00 34.44  ? 318  THR A CA  1 
ATOM   1915  C C   . THR A 1 309 ? -4.388  18.318  -18.550 1.00 35.42  ? 318  THR A C   1 
ATOM   1916  O O   . THR A 1 309 ? -4.723  17.534  -17.688 1.00 35.60  ? 318  THR A O   1 
ATOM   1917  C CB  . THR A 1 309 ? -2.423  17.246  -19.509 1.00 34.71  ? 318  THR A CB  1 
ATOM   1918  O OG1 . THR A 1 309 ? -1.993  17.580  -20.801 1.00 35.31  ? 318  THR A OG1 1 
ATOM   1919  C CG2 . THR A 1 309 ? -3.447  16.191  -19.605 1.00 36.09  ? 318  THR A CG2 1 
ATOM   1920  N N   . SER A 1 310 ? -5.266  19.059  -19.195 1.00 36.46  ? 319  SER A N   1 
ATOM   1921  C CA  . SER A 1 310 ? -6.705  18.951  -18.890 1.00 37.98  ? 319  SER A CA  1 
ATOM   1922  C C   . SER A 1 310 ? -7.599  18.840  -20.131 1.00 40.12  ? 319  SER A C   1 
ATOM   1923  O O   . SER A 1 310 ? -7.275  19.417  -21.160 1.00 40.83  ? 319  SER A O   1 
ATOM   1924  C CB  . SER A 1 310 ? -7.183  20.141  -18.093 1.00 37.33  ? 319  SER A CB  1 
ATOM   1925  O OG  . SER A 1 310 ? -8.542  19.958  -17.780 1.00 38.02  ? 319  SER A OG  1 
ATOM   1926  N N   . PRO A 1 311 ? -8.729  18.111  -20.034 1.00 41.72  ? 320  PRO A N   1 
ATOM   1927  C CA  . PRO A 1 311 ? -9.580  17.881  -21.166 1.00 43.61  ? 320  PRO A CA  1 
ATOM   1928  C C   . PRO A 1 311 ? -10.047 19.139  -21.858 1.00 44.78  ? 320  PRO A C   1 
ATOM   1929  O O   . PRO A 1 311 ? -10.215 20.166  -21.229 1.00 43.92  ? 320  PRO A O   1 
ATOM   1930  C CB  . PRO A 1 311 ? -10.762 17.169  -20.546 1.00 44.46  ? 320  PRO A CB  1 
ATOM   1931  C CG  . PRO A 1 311 ? -10.626 17.357  -19.150 1.00 43.33  ? 320  PRO A CG  1 
ATOM   1932  C CD  . PRO A 1 311 ? -9.227  17.360  -18.880 1.00 41.96  ? 320  PRO A CD  1 
ATOM   1933  N N   . LEU A 1 312 ? -10.251 19.013  -23.162 1.00 47.05  ? 321  LEU A N   1 
ATOM   1934  C CA  . LEU A 1 312 ? -10.589 20.109  -24.036 1.00 49.00  ? 321  LEU A CA  1 
ATOM   1935  C C   . LEU A 1 312 ? -11.725 19.678  -24.983 1.00 52.22  ? 321  LEU A C   1 
ATOM   1936  O O   . LEU A 1 312 ? -11.592 18.698  -25.706 1.00 53.32  ? 321  LEU A O   1 
ATOM   1937  C CB  . LEU A 1 312 ? -9.362  20.450  -24.852 1.00 47.73  ? 321  LEU A CB  1 
ATOM   1938  C CG  . LEU A 1 312 ? -9.112  21.874  -25.322 1.00 47.23  ? 321  LEU A CG  1 
ATOM   1939  C CD1 . LEU A 1 312 ? -8.248  21.803  -26.540 1.00 46.38  ? 321  LEU A CD1 1 
ATOM   1940  C CD2 . LEU A 1 312 ? -10.368 22.632  -25.651 1.00 48.76  ? 321  LEU A CD2 1 
ATOM   1941  N N   . CYS A 1 313 ? -12.826 20.423  -24.984 1.00 53.56  ? 322  CYS A N   1 
ATOM   1942  C CA  . CYS A 1 313 ? -13.997 20.098  -25.764 1.00 56.51  ? 322  CYS A CA  1 
ATOM   1943  C C   . CYS A 1 313 ? -14.382 21.286  -26.595 1.00 59.05  ? 322  CYS A C   1 
ATOM   1944  O O   . CYS A 1 313 ? -14.221 22.398  -26.124 1.00 59.09  ? 322  CYS A O   1 
ATOM   1945  C CB  . CYS A 1 313 ? -15.143 19.868  -24.831 1.00 56.90  ? 322  CYS A CB  1 
ATOM   1946  S SG  . CYS A 1 313 ? -14.787 18.661  -23.674 1.00 54.48  ? 322  CYS A SG  1 
ATOM   1947  N N   . THR A 1 314 ? -14.907 21.056  -27.807 1.00 62.37  ? 323  THR A N   1 
ATOM   1948  C CA  . THR A 1 314 ? -15.493 22.103  -28.676 1.00 65.51  ? 323  THR A CA  1 
ATOM   1949  C C   . THR A 1 314 ? -16.802 22.634  -28.127 1.00 68.76  ? 323  THR A C   1 
ATOM   1950  O O   . THR A 1 314 ? -17.335 22.080  -27.152 1.00 69.76  ? 323  THR A O   1 
ATOM   1951  C CB  . THR A 1 314 ? -15.931 21.497  -29.970 1.00 66.85  ? 323  THR A CB  1 
ATOM   1952  O OG1 . THR A 1 314 ? -16.172 20.097  -29.757 1.00 66.77  ? 323  THR A OG1 1 
ATOM   1953  C CG2 . THR A 1 314 ? -14.876 21.709  -31.032 1.00 66.99  ? 323  THR A CG2 1 
ATOM   1954  N N   . THR A 1 315 ? -17.382 23.665  -28.743 1.00 71.51  ? 324  THR A N   1 
ATOM   1955  C CA  . THR A 1 315 ? -18.738 23.983  -28.282 1.00 74.80  ? 324  THR A CA  1 
ATOM   1956  C C   . THR A 1 315 ? -19.799 24.104  -29.339 1.00 78.18  ? 324  THR A C   1 
ATOM   1957  O O   . THR A 1 315 ? -20.959 24.439  -29.017 1.00 80.13  ? 324  THR A O   1 
ATOM   1958  C CB  . THR A 1 315 ? -18.841 25.130  -27.254 1.00 74.31  ? 324  THR A CB  1 
ATOM   1959  O OG1 . THR A 1 315 ? -17.545 25.459  -26.747 1.00 72.27  ? 324  THR A OG1 1 
ATOM   1960  C CG2 . THR A 1 315 ? -19.748 24.683  -26.105 1.00 74.68  ? 324  THR A CG2 1 
ATOM   1961  N N   . ASN A 1 316 ? -19.430 23.782  -30.578 1.00 79.56  ? 325  ASN A N   1 
ATOM   1962  C CA  . ASN A 1 316 ? -20.448 23.509  -31.594 1.00 82.90  ? 325  ASN A CA  1 
ATOM   1963  C C   . ASN A 1 316 ? -20.067 22.422  -32.597 1.00 83.37  ? 325  ASN A C   1 
ATOM   1964  O O   . ASN A 1 316 ? -19.265 22.663  -33.500 1.00 83.63  ? 325  ASN A O   1 
ATOM   1965  C CB  . ASN A 1 316 ? -20.931 24.804  -32.273 1.00 84.26  ? 325  ASN A CB  1 
ATOM   1966  C CG  . ASN A 1 316 ? -22.233 25.351  -31.647 1.00 87.20  ? 325  ASN A CG  1 
ATOM   1967  O OD1 . ASN A 1 316 ? -23.243 25.460  -32.336 1.00 91.58  ? 325  ASN A OD1 1 
ATOM   1968  N ND2 . ASN A 1 316 ? -22.211 25.684  -30.348 1.00 86.19  ? 325  ASN A ND2 1 
ATOM   1969  N N   . SER A 1 321 ? -19.827 20.646  -27.050 1.00 81.73  ? 330  SER A N   1 
ATOM   1970  C CA  . SER A 1 321 ? -20.423 19.574  -27.865 1.00 83.82  ? 330  SER A CA  1 
ATOM   1971  C C   . SER A 1 321 ? -19.378 18.705  -28.655 1.00 82.05  ? 330  SER A C   1 
ATOM   1972  O O   . SER A 1 321 ? -18.264 19.165  -28.981 1.00 80.23  ? 330  SER A O   1 
ATOM   1973  C CB  . SER A 1 321 ? -21.577 20.133  -28.803 1.00 86.78  ? 330  SER A CB  1 
ATOM   1974  O OG  . SER A 1 321 ? -21.192 20.449  -30.182 1.00 88.77  ? 330  SER A OG  1 
ATOM   1975  N N   . ASN A 1 322 ? -19.765 17.452  -28.935 1.00 82.08  ? 331  ASN A N   1 
ATOM   1976  C CA  . ASN A 1 322 ? -19.192 16.637  -30.035 1.00 81.02  ? 331  ASN A CA  1 
ATOM   1977  C C   . ASN A 1 322 ? -17.822 15.980  -29.778 1.00 77.55  ? 331  ASN A C   1 
ATOM   1978  O O   . ASN A 1 322 ? -17.701 14.776  -29.971 1.00 78.90  ? 331  ASN A O   1 
ATOM   1979  C CB  . ASN A 1 322 ? -19.266 17.346  -31.441 1.00 81.90  ? 331  ASN A CB  1 
ATOM   1980  C CG  . ASN A 1 322 ? -20.430 16.806  -32.351 1.00 86.13  ? 331  ASN A CG  1 
ATOM   1981  O OD1 . ASN A 1 322 ? -21.632 16.762  -31.960 1.00 89.78  ? 331  ASN A OD1 1 
ATOM   1982  N ND2 . ASN A 1 322 ? -20.063 16.407  -33.573 1.00 85.76  ? 331  ASN A ND2 1 
ATOM   1983  N N   . ILE A 1 323 ? -16.804 16.720  -29.336 1.00 72.63  ? 332  ILE A N   1 
ATOM   1984  C CA  . ILE A 1 323 ? -15.491 16.084  -29.157 1.00 68.34  ? 332  ILE A CA  1 
ATOM   1985  C C   . ILE A 1 323 ? -14.606 16.625  -28.018 1.00 64.64  ? 332  ILE A C   1 
ATOM   1986  O O   . ILE A 1 323 ? -14.521 17.842  -27.836 1.00 63.08  ? 332  ILE A O   1 
ATOM   1987  C CB  . ILE A 1 323 ? -14.724 16.160  -30.471 1.00 68.15  ? 332  ILE A CB  1 
ATOM   1988  C CG1 . ILE A 1 323 ? -13.485 15.261  -30.455 1.00 66.92  ? 332  ILE A CG1 1 
ATOM   1989  C CG2 . ILE A 1 323 ? -14.376 17.581  -30.781 1.00 67.11  ? 332  ILE A CG2 1 
ATOM   1990  C CD1 . ILE A 1 323 ? -13.703 13.897  -31.081 1.00 67.82  ? 332  ILE A CD1 1 
ATOM   1991  N N   . CYS A 1 324 ? -13.963 15.722  -27.258 1.00 62.10  ? 333  CYS A N   1 
ATOM   1992  C CA  . CYS A 1 324 ? -12.906 16.122  -26.333 1.00 58.54  ? 333  CYS A CA  1 
ATOM   1993  C C   . CYS A 1 324 ? -11.615 15.360  -26.468 1.00 57.37  ? 333  CYS A C   1 
ATOM   1994  O O   . CYS A 1 324 ? -11.584 14.199  -26.939 1.00 57.87  ? 333  CYS A O   1 
ATOM   1995  C CB  . CYS A 1 324 ? -13.342 16.157  -24.885 1.00 57.44  ? 333  CYS A CB  1 
ATOM   1996  S SG  . CYS A 1 324 ? -14.910 16.932  -24.723 1.00 59.31  ? 333  CYS A SG  1 
ATOM   1997  N N   . LEU A 1 325 ? -10.571 16.087  -26.029 1.00 55.50  ? 334  LEU A N   1 
ATOM   1998  C CA  . LEU A 1 325 ? -9.149  15.775  -26.116 1.00 53.32  ? 334  LEU A CA  1 
ATOM   1999  C C   . LEU A 1 325 ? -8.506  15.931  -24.792 1.00 51.30  ? 334  LEU A C   1 
ATOM   2000  O O   . LEU A 1 325 ? -8.672  16.967  -24.161 1.00 50.63  ? 334  LEU A O   1 
ATOM   2001  C CB  . LEU A 1 325 ? -8.476  16.815  -26.970 1.00 52.33  ? 334  LEU A CB  1 
ATOM   2002  C CG  . LEU A 1 325 ? -8.619  16.568  -28.452 1.00 54.28  ? 334  LEU A CG  1 
ATOM   2003  C CD1 . LEU A 1 325 ? -7.402  17.098  -29.154 1.00 53.22  ? 334  LEU A CD1 1 
ATOM   2004  C CD2 . LEU A 1 325 ? -8.760  15.076  -28.751 1.00 56.90  ? 334  LEU A CD2 1 
ATOM   2005  N N   . THR A 1 326 ? -7.755  14.928  -24.366 1.00 50.26  ? 335  THR A N   1 
ATOM   2006  C CA  . THR A 1 326 ? -6.872  15.135  -23.226 1.00 48.11  ? 335  THR A CA  1 
ATOM   2007  C C   . THR A 1 326 ? -5.515  14.661  -23.679 1.00 47.32  ? 335  THR A C   1 
ATOM   2008  O O   . THR A 1 326 ? -5.381  13.580  -24.246 1.00 48.33  ? 335  THR A O   1 
ATOM   2009  C CB  . THR A 1 326 ? -7.347  14.412  -21.936 1.00 48.03  ? 335  THR A CB  1 
ATOM   2010  O OG1 . THR A 1 326 ? -8.711  14.711  -21.690 1.00 48.87  ? 335  THR A OG1 1 
ATOM   2011  C CG2 . THR A 1 326 ? -6.649  14.930  -20.769 1.00 46.59  ? 335  THR A CG2 1 
ATOM   2012  N N   . ARG A 1 327 ? -4.517  15.493  -23.470 1.00 45.58  ? 336  ARG A N   1 
ATOM   2013  C CA  . ARG A 1 327 ? -3.201  15.167  -23.911 1.00 45.35  ? 336  ARG A CA  1 
ATOM   2014  C C   . ARG A 1 327 ? -2.573  14.168  -22.946 1.00 45.40  ? 336  ARG A C   1 
ATOM   2015  O O   . ARG A 1 327 ? -2.564  14.373  -21.742 1.00 44.43  ? 336  ARG A O   1 
ATOM   2016  C CB  . ARG A 1 327 ? -2.429  16.454  -23.985 1.00 44.04  ? 336  ARG A CB  1 
ATOM   2017  C CG  . ARG A 1 327 ? -1.306  16.416  -24.956 1.00 44.80  ? 336  ARG A CG  1 
ATOM   2018  C CD  . ARG A 1 327 ? -1.120  17.755  -25.644 1.00 44.39  ? 336  ARG A CD  1 
ATOM   2019  N NE  . ARG A 1 327 ? -0.229  18.700  -24.965 1.00 42.71  ? 336  ARG A NE  1 
ATOM   2020  C CZ  . ARG A 1 327 ? 1.100   18.626  -24.955 1.00 41.96  ? 336  ARG A CZ  1 
ATOM   2021  N NH1 . ARG A 1 327 ? 1.751   17.626  -25.553 1.00 42.18  ? 336  ARG A NH1 1 
ATOM   2022  N NH2 . ARG A 1 327 ? 1.775   19.561  -24.320 1.00 40.98  ? 336  ARG A NH2 1 
ATOM   2023  N N   . THR A 1 328 ? -2.057  13.073  -23.473 1.00 46.98  ? 337  THR A N   1 
ATOM   2024  C CA  . THR A 1 328 ? -1.714  11.942  -22.633 1.00 48.31  ? 337  THR A CA  1 
ATOM   2025  C C   . THR A 1 328 ? -0.445  12.122  -21.851 1.00 47.17  ? 337  THR A C   1 
ATOM   2026  O O   . THR A 1 328 ? -0.400  11.844  -20.648 1.00 46.98  ? 337  THR A O   1 
ATOM   2027  C CB  . THR A 1 328 ? -1.561  10.676  -23.461 1.00 50.30  ? 337  THR A CB  1 
ATOM   2028  O OG1 . THR A 1 328 ? -2.865  10.207  -23.838 1.00 53.41  ? 337  THR A OG1 1 
ATOM   2029  C CG2 . THR A 1 328 ? -0.843  9.582   -22.652 1.00 51.31  ? 337  THR A CG2 1 
ATOM   2030  N N   . ASP A 1 329 ? 0.572   12.585  -22.556 1.00 46.85  ? 338  ASP A N   1 
ATOM   2031  C CA  . ASP A 1 329 ? 1.954   12.601  -22.094 1.00 46.27  ? 338  ASP A CA  1 
ATOM   2032  C C   . ASP A 1 329 ? 2.304   13.632  -20.975 1.00 43.13  ? 338  ASP A C   1 
ATOM   2033  O O   . ASP A 1 329 ? 2.971   14.624  -21.223 1.00 42.31  ? 338  ASP A O   1 
ATOM   2034  C CB  . ASP A 1 329 ? 2.831   12.819  -23.355 1.00 48.13  ? 338  ASP A CB  1 
ATOM   2035  C CG  . ASP A 1 329 ? 2.149   13.797  -24.428 1.00 52.03  ? 338  ASP A CG  1 
ATOM   2036  O OD1 . ASP A 1 329 ? 2.530   13.766  -25.653 1.00 56.16  ? 338  ASP A OD1 1 
ATOM   2037  O OD2 . ASP A 1 329 ? 1.238   14.595  -24.038 1.00 52.97  ? 338  ASP A OD2 1 
ATOM   2038  N N   . ARG A 1 330 ? 1.885   13.417  -19.741 1.00 41.12  ? 339  ARG A N   1 
ATOM   2039  C CA  . ARG A 1 330 ? 2.180   14.439  -18.750 1.00 38.57  ? 339  ARG A CA  1 
ATOM   2040  C C   . ARG A 1 330 ? 3.387   14.032  -18.007 1.00 37.13  ? 339  ARG A C   1 
ATOM   2041  O O   . ARG A 1 330 ? 3.730   12.861  -17.970 1.00 37.64  ? 339  ARG A O   1 
ATOM   2042  C CB  . ARG A 1 330 ? 1.078   14.609  -17.730 1.00 38.46  ? 339  ARG A CB  1 
ATOM   2043  C CG  . ARG A 1 330 ? -0.355  14.481  -18.234 1.00 40.57  ? 339  ARG A CG  1 
ATOM   2044  C CD  . ARG A 1 330 ? -1.183  13.743  -17.154 1.00 41.99  ? 339  ARG A CD  1 
ATOM   2045  N NE  . ARG A 1 330 ? -2.608  13.639  -17.454 1.00 42.56  ? 339  ARG A NE  1 
ATOM   2046  C CZ  . ARG A 1 330 ? -3.516  14.456  -16.949 1.00 42.46  ? 339  ARG A CZ  1 
ATOM   2047  N NH1 . ARG A 1 330 ? -3.124  15.448  -16.120 1.00 42.61  ? 339  ARG A NH1 1 
ATOM   2048  N NH2 . ARG A 1 330 ? -4.793  14.276  -17.263 1.00 41.30  ? 339  ARG A NH2 1 
ATOM   2049  N N   . GLY A 1 331 ? 4.017   15.005  -17.384 1.00 35.15  ? 340  GLY A N   1 
ATOM   2050  C CA  . GLY A 1 331 ? 5.200   14.723  -16.614 1.00 33.97  ? 340  GLY A CA  1 
ATOM   2051  C C   . GLY A 1 331 ? 6.316   15.709  -16.873 1.00 32.85  ? 340  GLY A C   1 
ATOM   2052  O O   . GLY A 1 331 ? 6.089   16.818  -17.385 1.00 32.61  ? 340  GLY A O   1 
ATOM   2053  N N   . TRP A 1 332 ? 7.519   15.303  -16.494 1.00 32.04  ? 341  TRP A N   1 
ATOM   2054  C CA  . TRP A 1 332 ? 8.637   16.153  -16.634 1.00 31.36  ? 341  TRP A CA  1 
ATOM   2055  C C   . TRP A 1 332 ? 9.323   15.949  -17.954 1.00 32.72  ? 341  TRP A C   1 
ATOM   2056  O O   . TRP A 1 332 ? 9.697   14.837  -18.345 1.00 33.74  ? 341  TRP A O   1 
ATOM   2057  C CB  . TRP A 1 332 ? 9.608   15.862  -15.552 1.00 30.76  ? 341  TRP A CB  1 
ATOM   2058  C CG  . TRP A 1 332 ? 9.254   16.437  -14.309 1.00 29.39  ? 341  TRP A CG  1 
ATOM   2059  C CD1 . TRP A 1 332 ? 8.683   15.797  -13.280 1.00 29.44  ? 341  TRP A CD1 1 
ATOM   2060  C CD2 . TRP A 1 332 ? 9.465   17.796  -13.892 1.00 28.35  ? 341  TRP A CD2 1 
ATOM   2061  N NE1 . TRP A 1 332 ? 8.501   16.668  -12.241 1.00 29.21  ? 341  TRP A NE1 1 
ATOM   2062  C CE2 . TRP A 1 332 ? 8.988   17.902  -12.593 1.00 27.70  ? 341  TRP A CE2 1 
ATOM   2063  C CE3 . TRP A 1 332 ? 9.986   18.935  -14.504 1.00 28.21  ? 341  TRP A CE3 1 
ATOM   2064  C CZ2 . TRP A 1 332 ? 9.017   19.110  -11.881 1.00 26.34  ? 341  TRP A CZ2 1 
ATOM   2065  C CZ3 . TRP A 1 332 ? 10.024  20.126  -13.791 1.00 26.37  ? 341  TRP A CZ3 1 
ATOM   2066  C CH2 . TRP A 1 332 ? 9.548   20.204  -12.506 1.00 25.07  ? 341  TRP A CH2 1 
ATOM   2067  N N   . TYR A 1 333 ? 9.492   17.055  -18.650 1.00 32.88  ? 342  TYR A N   1 
ATOM   2068  C CA  . TYR A 1 333 ? 10.378  17.105  -19.776 1.00 33.53  ? 342  TYR A CA  1 
ATOM   2069  C C   . TYR A 1 333 ? 11.553  17.899  -19.298 1.00 33.16  ? 342  TYR A C   1 
ATOM   2070  O O   . TYR A 1 333 ? 11.493  18.559  -18.259 1.00 31.98  ? 342  TYR A O   1 
ATOM   2071  C CB  . TYR A 1 333 ? 9.695   17.794  -20.919 1.00 33.84  ? 342  TYR A CB  1 
ATOM   2072  C CG  . TYR A 1 333 ? 8.504   17.028  -21.372 1.00 34.80  ? 342  TYR A CG  1 
ATOM   2073  C CD1 . TYR A 1 333 ? 7.322   17.106  -20.704 1.00 35.14  ? 342  TYR A CD1 1 
ATOM   2074  C CD2 . TYR A 1 333 ? 8.574   16.195  -22.450 1.00 37.24  ? 342  TYR A CD2 1 
ATOM   2075  C CE1 . TYR A 1 333 ? 6.225   16.381  -21.115 1.00 36.75  ? 342  TYR A CE1 1 
ATOM   2076  C CE2 . TYR A 1 333 ? 7.496   15.481  -22.874 1.00 38.07  ? 342  TYR A CE2 1 
ATOM   2077  C CZ  . TYR A 1 333 ? 6.328   15.577  -22.210 1.00 38.18  ? 342  TYR A CZ  1 
ATOM   2078  O OH  . TYR A 1 333 ? 5.260   14.848  -22.642 1.00 41.10  ? 342  TYR A OH  1 
ATOM   2079  N N   . CYS A 1 334 ? 12.629  17.850  -20.055 1.00 34.25  ? 343  CYS A N   1 
ATOM   2080  C CA  . CYS A 1 334 ? 13.870  18.274  -19.514 1.00 34.28  ? 343  CYS A CA  1 
ATOM   2081  C C   . CYS A 1 334 ? 14.962  17.923  -20.540 1.00 35.57  ? 343  CYS A C   1 
ATOM   2082  O O   . CYS A 1 334 ? 15.077  16.775  -20.922 1.00 36.65  ? 343  CYS A O   1 
ATOM   2083  C CB  . CYS A 1 334 ? 13.950  17.516  -18.219 1.00 33.53  ? 343  CYS A CB  1 
ATOM   2084  S SG  . CYS A 1 334 ? 15.205  17.907  -17.279 1.00 35.49  ? 343  CYS A SG  1 
ATOM   2085  N N   . ASP A 1 335 ? 15.704  18.920  -21.039 1.00 36.09  ? 344  ASP A N   1 
ATOM   2086  C CA  . ASP A 1 335 ? 16.595  18.779  -22.217 1.00 37.40  ? 344  ASP A CA  1 
ATOM   2087  C C   . ASP A 1 335 ? 17.777  17.872  -21.987 1.00 38.14  ? 344  ASP A C   1 
ATOM   2088  O O   . ASP A 1 335 ? 18.468  17.988  -21.012 1.00 38.07  ? 344  ASP A O   1 
ATOM   2089  C CB  . ASP A 1 335 ? 17.157  20.138  -22.617 1.00 37.77  ? 344  ASP A CB  1 
ATOM   2090  C CG  . ASP A 1 335 ? 16.239  20.911  -23.490 1.00 39.53  ? 344  ASP A CG  1 
ATOM   2091  O OD1 . ASP A 1 335 ? 15.891  20.403  -24.563 1.00 43.20  ? 344  ASP A OD1 1 
ATOM   2092  O OD2 . ASP A 1 335 ? 15.876  22.045  -23.140 1.00 40.45  ? 344  ASP A OD2 1 
ATOM   2093  N N   . ASN A 1 336 ? 18.037  16.966  -22.891 1.00 39.70  ? 345  ASN A N   1 
ATOM   2094  C CA  . ASN A 1 336 ? 19.274  16.207  -22.839 1.00 41.17  ? 345  ASN A CA  1 
ATOM   2095  C C   . ASN A 1 336 ? 20.153  16.598  -24.043 1.00 43.34  ? 345  ASN A C   1 
ATOM   2096  O O   . ASN A 1 336 ? 19.939  17.662  -24.631 1.00 44.39  ? 345  ASN A O   1 
ATOM   2097  C CB  . ASN A 1 336 ? 18.962  14.738  -22.873 1.00 41.82  ? 345  ASN A CB  1 
ATOM   2098  C CG  . ASN A 1 336 ? 19.969  13.959  -22.188 1.00 41.68  ? 345  ASN A CG  1 
ATOM   2099  O OD1 . ASN A 1 336 ? 20.126  14.097  -21.020 1.00 37.95  ? 345  ASN A OD1 1 
ATOM   2100  N ND2 . ASN A 1 336 ? 20.694  13.139  -22.913 1.00 45.99  ? 345  ASN A ND2 1 
ATOM   2101  N N   . ALA A 1 337 ? 21.113  15.769  -24.443 1.00 44.51  ? 346  ALA A N   1 
ATOM   2102  C CA  . ALA A 1 337 ? 22.009  16.167  -25.502 1.00 45.68  ? 346  ALA A CA  1 
ATOM   2103  C C   . ALA A 1 337 ? 21.294  16.458  -26.829 1.00 46.37  ? 346  ALA A C   1 
ATOM   2104  O O   . ALA A 1 337 ? 21.151  15.600  -27.690 1.00 47.39  ? 346  ALA A O   1 
ATOM   2105  C CB  . ALA A 1 337 ? 23.063  15.156  -25.669 1.00 47.30  ? 346  ALA A CB  1 
ATOM   2106  N N   . GLY A 1 338 ? 20.846  17.697  -26.979 1.00 46.00  ? 347  GLY A N   1 
ATOM   2107  C CA  . GLY A 1 338 ? 20.248  18.175  -28.226 1.00 46.94  ? 347  GLY A CA  1 
ATOM   2108  C C   . GLY A 1 338 ? 18.841  17.660  -28.452 1.00 46.54  ? 347  GLY A C   1 
ATOM   2109  O O   . GLY A 1 338 ? 18.174  17.999  -29.468 1.00 47.59  ? 347  GLY A O   1 
ATOM   2110  N N   . SER A 1 339 ? 18.396  16.831  -27.511 1.00 44.96  ? 348  SER A N   1 
ATOM   2111  C CA  . SER A 1 339 ? 17.148  16.134  -27.650 1.00 44.03  ? 348  SER A CA  1 
ATOM   2112  C C   . SER A 1 339 ? 16.557  16.324  -26.316 1.00 42.11  ? 348  SER A C   1 
ATOM   2113  O O   . SER A 1 339 ? 17.174  17.010  -25.525 1.00 41.12  ? 348  SER A O   1 
ATOM   2114  C CB  . SER A 1 339 ? 17.370  14.660  -28.007 1.00 45.31  ? 348  SER A CB  1 
ATOM   2115  O OG  . SER A 1 339 ? 18.018  14.535  -29.292 1.00 46.82  ? 348  SER A OG  1 
ATOM   2116  N N   . VAL A 1 340 ? 15.355  15.780  -26.085 1.00 41.58  ? 349  VAL A N   1 
ATOM   2117  C CA  . VAL A 1 340 ? 14.623  16.006  -24.841 1.00 39.97  ? 349  VAL A CA  1 
ATOM   2118  C C   . VAL A 1 340 ? 14.261  14.718  -24.192 1.00 40.13  ? 349  VAL A C   1 
ATOM   2119  O O   . VAL A 1 340 ? 13.730  13.850  -24.832 1.00 41.21  ? 349  VAL A O   1 
ATOM   2120  C CB  . VAL A 1 340 ? 13.312  16.729  -25.056 1.00 39.08  ? 349  VAL A CB  1 
ATOM   2121  C CG1 . VAL A 1 340 ? 12.793  17.179  -23.712 1.00 37.46  ? 349  VAL A CG1 1 
ATOM   2122  C CG2 . VAL A 1 340 ? 13.460  17.917  -26.011 1.00 39.56  ? 349  VAL A CG2 1 
ATOM   2123  N N   . SER A 1 341 ? 14.538  14.607  -22.911 1.00 39.74  ? 350  SER A N   1 
ATOM   2124  C CA  . SER A 1 341 ? 14.201  13.407  -22.171 1.00 40.41  ? 350  SER A CA  1 
ATOM   2125  C C   . SER A 1 341 ? 12.910  13.605  -21.375 1.00 40.18  ? 350  SER A C   1 
ATOM   2126  O O   . SER A 1 341 ? 12.726  14.623  -20.678 1.00 38.92  ? 350  SER A O   1 
ATOM   2127  C CB  . SER A 1 341 ? 15.350  12.950  -21.259 1.00 40.01  ? 350  SER A CB  1 
ATOM   2128  O OG  . SER A 1 341 ? 16.338  12.258  -21.984 1.00 39.95  ? 350  SER A OG  1 
ATOM   2129  N N   . PHE A 1 342 ? 12.029  12.607  -21.485 1.00 41.82  ? 351  PHE A N   1 
ATOM   2130  C CA  . PHE A 1 342 ? 10.735  12.601  -20.813 1.00 42.20  ? 351  PHE A CA  1 
ATOM   2131  C C   . PHE A 1 342 ? 10.612  11.452  -19.794 1.00 43.38  ? 351  PHE A C   1 
ATOM   2132  O O   . PHE A 1 342 ? 10.910  10.295  -20.125 1.00 44.80  ? 351  PHE A O   1 
ATOM   2133  C CB  . PHE A 1 342 ? 9.634   12.529  -21.867 1.00 42.71  ? 351  PHE A CB  1 
ATOM   2134  C CG  . PHE A 1 342 ? 8.291   12.263  -21.305 1.00 42.83  ? 351  PHE A CG  1 
ATOM   2135  C CD1 . PHE A 1 342 ? 7.738   13.112  -20.376 1.00 42.24  ? 351  PHE A CD1 1 
ATOM   2136  C CD2 . PHE A 1 342 ? 7.583   11.149  -21.679 1.00 44.54  ? 351  PHE A CD2 1 
ATOM   2137  C CE1 . PHE A 1 342 ? 6.498   12.843  -19.838 1.00 42.75  ? 351  PHE A CE1 1 
ATOM   2138  C CE2 . PHE A 1 342 ? 6.348   10.891  -21.138 1.00 44.89  ? 351  PHE A CE2 1 
ATOM   2139  C CZ  . PHE A 1 342 ? 5.814   11.735  -20.221 1.00 43.92  ? 351  PHE A CZ  1 
ATOM   2140  N N   . PHE A 1 343 ? 10.185  11.790  -18.571 1.00 43.23  ? 352  PHE A N   1 
ATOM   2141  C CA  . PHE A 1 343 ? 10.088  10.845  -17.472 1.00 44.55  ? 352  PHE A CA  1 
ATOM   2142  C C   . PHE A 1 343 ? 8.637   10.740  -17.090 1.00 46.26  ? 352  PHE A C   1 
ATOM   2143  O O   . PHE A 1 343 ? 8.056   11.654  -16.468 1.00 45.50  ? 352  PHE A O   1 
ATOM   2144  C CB  . PHE A 1 343 ? 10.893  11.320  -16.281 1.00 42.98  ? 352  PHE A CB  1 
ATOM   2145  C CG  . PHE A 1 343 ? 12.186  11.959  -16.655 1.00 42.50  ? 352  PHE A CG  1 
ATOM   2146  C CD1 . PHE A 1 343 ? 12.235  13.278  -17.092 1.00 41.44  ? 352  PHE A CD1 1 
ATOM   2147  C CD2 . PHE A 1 343 ? 13.363  11.243  -16.607 1.00 42.54  ? 352  PHE A CD2 1 
ATOM   2148  C CE1 . PHE A 1 343 ? 13.448  13.877  -17.456 1.00 40.36  ? 352  PHE A CE1 1 
ATOM   2149  C CE2 . PHE A 1 343 ? 14.542  11.832  -16.963 1.00 41.16  ? 352  PHE A CE2 1 
ATOM   2150  C CZ  . PHE A 1 343 ? 14.578  13.159  -17.379 1.00 40.28  ? 352  PHE A CZ  1 
ATOM   2151  N N   . PRO A 1 344 ? 8.040   9.606   -17.422 1.00 49.19  ? 353  PRO A N   1 
ATOM   2152  C CA  . PRO A 1 344 ? 6.604   9.389   -17.413 1.00 51.27  ? 353  PRO A CA  1 
ATOM   2153  C C   . PRO A 1 344 ? 5.876   9.610   -16.054 1.00 52.28  ? 353  PRO A C   1 
ATOM   2154  O O   . PRO A 1 344 ? 4.719   10.098  -16.039 1.00 52.69  ? 353  PRO A O   1 
ATOM   2155  C CB  . PRO A 1 344 ? 6.490   7.933   -17.854 1.00 52.94  ? 353  PRO A CB  1 
ATOM   2156  C CG  . PRO A 1 344 ? 7.802   7.662   -18.535 1.00 52.77  ? 353  PRO A CG  1 
ATOM   2157  C CD  . PRO A 1 344 ? 8.772   8.367   -17.696 1.00 50.46  ? 353  PRO A CD  1 
ATOM   2158  N N   . GLN A 1 345 ? 6.519   9.263   -14.933 1.00 53.53  ? 354  GLN A N   1 
ATOM   2159  C CA  . GLN A 1 345 ? 5.823   9.280   -13.597 1.00 54.39  ? 354  GLN A CA  1 
ATOM   2160  C C   . GLN A 1 345 ? 6.658   9.901   -12.456 1.00 53.27  ? 354  GLN A C   1 
ATOM   2161  O O   . GLN A 1 345 ? 7.889   9.714   -12.388 1.00 52.83  ? 354  GLN A O   1 
ATOM   2162  C CB  . GLN A 1 345 ? 5.217   7.877   -13.197 1.00 55.92  ? 354  GLN A CB  1 
ATOM   2163  C CG  . GLN A 1 345 ? 5.898   6.618   -13.888 1.00 58.42  ? 354  GLN A CG  1 
ATOM   2164  C CD  . GLN A 1 345 ? 7.408   6.506   -13.592 1.00 57.94  ? 354  GLN A CD  1 
ATOM   2165  O OE1 . GLN A 1 345 ? 7.795   6.433   -12.415 1.00 57.72  ? 354  GLN A OE1 1 
ATOM   2166  N NE2 . GLN A 1 345 ? 8.255   6.523   -14.647 1.00 56.46  ? 354  GLN A NE2 1 
ATOM   2167  N N   . ALA A 1 346 ? 5.954   10.651  -11.591 1.00 52.85  ? 355  ALA A N   1 
ATOM   2168  C CA  . ALA A 1 346 ? 6.540   11.400  -10.427 1.00 51.66  ? 355  ALA A CA  1 
ATOM   2169  C C   . ALA A 1 346 ? 7.872   10.776  -9.923  1.00 51.25  ? 355  ALA A C   1 
ATOM   2170  O O   . ALA A 1 346 ? 8.973   11.315  -10.216 1.00 51.31  ? 355  ALA A O   1 
ATOM   2171  C CB  . ALA A 1 346 ? 5.467   11.578  -9.248  1.00 50.90  ? 355  ALA A CB  1 
ATOM   2172  N N   . GLU A 1 347 ? 7.721   9.664   -9.176  1.00 50.45  ? 356  GLU A N   1 
ATOM   2173  C CA  . GLU A 1 347 ? 8.685   8.562   -9.000  1.00 49.58  ? 356  GLU A CA  1 
ATOM   2174  C C   . GLU A 1 347 ? 10.111  8.833   -9.390  1.00 47.84  ? 356  GLU A C   1 
ATOM   2175  O O   . GLU A 1 347 ? 10.998  8.949   -8.533  1.00 47.09  ? 356  GLU A O   1 
ATOM   2176  C CB  . GLU A 1 347 ? 8.154   7.351   -9.772  1.00 51.69  ? 356  GLU A CB  1 
ATOM   2177  C CG  . GLU A 1 347 ? 6.900   6.883   -9.160  1.00 55.02  ? 356  GLU A CG  1 
ATOM   2178  C CD  . GLU A 1 347 ? 6.974   7.127   -7.612  1.00 59.42  ? 356  GLU A CD  1 
ATOM   2179  O OE1 . GLU A 1 347 ? 6.079   7.839   -7.043  1.00 60.49  ? 356  GLU A OE1 1 
ATOM   2180  O OE2 . GLU A 1 347 ? 7.968   6.652   -6.973  1.00 60.48  ? 356  GLU A OE2 1 
ATOM   2181  N N   . THR A 1 348 ? 10.306  8.946   -10.699 1.00 46.48  ? 357  THR A N   1 
ATOM   2182  C CA  . THR A 1 348 ? 11.589  9.180   -11.289 1.00 44.81  ? 357  THR A CA  1 
ATOM   2183  C C   . THR A 1 348 ? 12.166  10.529  -10.931 1.00 42.45  ? 357  THR A C   1 
ATOM   2184  O O   . THR A 1 348 ? 13.391  10.653  -10.962 1.00 43.19  ? 357  THR A O   1 
ATOM   2185  C CB  . THR A 1 348 ? 11.495  9.168   -12.772 1.00 45.64  ? 357  THR A CB  1 
ATOM   2186  O OG1 . THR A 1 348 ? 10.243  8.601   -13.153 1.00 46.96  ? 357  THR A OG1 1 
ATOM   2187  C CG2 . THR A 1 348 ? 12.581  8.348   -13.303 1.00 47.25  ? 357  THR A CG2 1 
ATOM   2188  N N   . CYS A 1 349 ? 11.333  11.534  -10.599 1.00 39.18  ? 358  CYS A N   1 
ATOM   2189  C CA  . CYS A 1 349 ? 11.836  12.903  -10.393 1.00 36.13  ? 358  CYS A CA  1 
ATOM   2190  C C   . CYS A 1 349 ? 11.599  13.462  -9.037  1.00 33.68  ? 358  CYS A C   1 
ATOM   2191  O O   . CYS A 1 349 ? 10.581  13.200  -8.480  1.00 33.46  ? 358  CYS A O   1 
ATOM   2192  C CB  . CYS A 1 349 ? 11.249  13.821  -11.441 1.00 35.76  ? 358  CYS A CB  1 
ATOM   2193  S SG  . CYS A 1 349 ? 11.791  13.314  -13.123 1.00 38.39  ? 358  CYS A SG  1 
ATOM   2194  N N   . LYS A 1 350 ? 12.552  14.197  -8.488  1.00 32.17  ? 359  LYS A N   1 
ATOM   2195  C CA  . LYS A 1 350 ? 12.276  15.012  -7.323  1.00 30.92  ? 359  LYS A CA  1 
ATOM   2196  C C   . LYS A 1 350 ? 12.839  16.345  -7.517  1.00 29.88  ? 359  LYS A C   1 
ATOM   2197  O O   . LYS A 1 350 ? 13.752  16.494  -8.283  1.00 30.64  ? 359  LYS A O   1 
ATOM   2198  C CB  . LYS A 1 350 ? 12.812  14.439  -6.036  1.00 30.96  ? 359  LYS A CB  1 
ATOM   2199  C CG  . LYS A 1 350 ? 13.808  13.384  -6.199  1.00 33.80  ? 359  LYS A CG  1 
ATOM   2200  C CD  . LYS A 1 350 ? 13.543  12.275  -5.206  1.00 36.50  ? 359  LYS A CD  1 
ATOM   2201  C CE  . LYS A 1 350 ? 14.159  11.003  -5.735  1.00 39.82  ? 359  LYS A CE  1 
ATOM   2202  N NZ  . LYS A 1 350 ? 13.622  9.861   -4.998  1.00 43.98  ? 359  LYS A NZ  1 
ATOM   2203  N N   . VAL A 1 351 ? 12.302  17.311  -6.790  1.00 28.57  ? 360  VAL A N   1 
ATOM   2204  C CA  . VAL A 1 351 ? 12.526  18.707  -7.084  1.00 27.92  ? 360  VAL A CA  1 
ATOM   2205  C C   . VAL A 1 351 ? 12.601  19.551  -5.807  1.00 27.25  ? 360  VAL A C   1 
ATOM   2206  O O   . VAL A 1 351 ? 11.878  19.283  -4.878  1.00 26.95  ? 360  VAL A O   1 
ATOM   2207  C CB  . VAL A 1 351 ? 11.419  19.166  -8.002  1.00 27.53  ? 360  VAL A CB  1 
ATOM   2208  C CG1 . VAL A 1 351 ? 10.155  18.693  -7.476  1.00 27.64  ? 360  VAL A CG1 1 
ATOM   2209  C CG2 . VAL A 1 351 ? 11.381  20.637  -8.105  1.00 27.89  ? 360  VAL A CG2 1 
ATOM   2210  N N   . GLN A 1 352 ? 13.458  20.563  -5.778  1.00 27.56  ? 361  GLN A N   1 
ATOM   2211  C CA  . GLN A 1 352 ? 13.741  21.318  -4.583  1.00 28.33  ? 361  GLN A CA  1 
ATOM   2212  C C   . GLN A 1 352 ? 13.987  22.729  -5.003  1.00 28.32  ? 361  GLN A C   1 
ATOM   2213  O O   . GLN A 1 352 ? 15.044  23.073  -5.453  1.00 29.85  ? 361  GLN A O   1 
ATOM   2214  C CB  . GLN A 1 352 ? 15.001  20.783  -3.922  1.00 28.97  ? 361  GLN A CB  1 
ATOM   2215  C CG  . GLN A 1 352 ? 15.487  21.533  -2.706  1.00 33.49  ? 361  GLN A CG  1 
ATOM   2216  C CD  . GLN A 1 352 ? 15.649  20.540  -1.504  1.00 42.56  ? 361  GLN A CD  1 
ATOM   2217  O OE1 . GLN A 1 352 ? 16.798  20.179  -1.075  1.00 45.98  ? 361  GLN A OE1 1 
ATOM   2218  N NE2 . GLN A 1 352 ? 14.482  20.056  -0.974  1.00 44.35  ? 361  GLN A NE2 1 
ATOM   2219  N N   . SER A 1 353 ? 13.027  23.585  -4.817  1.00 27.70  ? 362  SER A N   1 
ATOM   2220  C CA  . SER A 1 353 ? 13.136  24.908  -5.368  1.00 27.59  ? 362  SER A CA  1 
ATOM   2221  C C   . SER A 1 353 ? 13.172  24.717  -6.838  1.00 27.46  ? 362  SER A C   1 
ATOM   2222  O O   . SER A 1 353 ? 12.359  23.991  -7.344  1.00 27.66  ? 362  SER A O   1 
ATOM   2223  C CB  . SER A 1 353 ? 14.363  25.660  -4.886  1.00 28.14  ? 362  SER A CB  1 
ATOM   2224  O OG  . SER A 1 353 ? 14.214  27.015  -5.261  1.00 29.52  ? 362  SER A OG  1 
ATOM   2225  N N   . ASN A 1 354 ? 14.093  25.351  -7.533  1.00 27.59  ? 363  ASN A N   1 
ATOM   2226  C CA  . ASN A 1 354 ? 14.069  25.279  -8.975  1.00 27.81  ? 363  ASN A CA  1 
ATOM   2227  C C   . ASN A 1 354 ? 15.040  24.238  -9.437  1.00 27.44  ? 363  ASN A C   1 
ATOM   2228  O O   . ASN A 1 354 ? 15.490  24.256  -10.574 1.00 28.24  ? 363  ASN A O   1 
ATOM   2229  C CB  . ASN A 1 354 ? 14.413  26.616  -9.588  1.00 28.83  ? 363  ASN A CB  1 
ATOM   2230  C CG  . ASN A 1 354 ? 15.786  27.075  -9.212  1.00 29.50  ? 363  ASN A CG  1 
ATOM   2231  O OD1 . ASN A 1 354 ? 16.407  26.557  -8.280  1.00 28.76  ? 363  ASN A OD1 1 
ATOM   2232  N ND2 . ASN A 1 354 ? 16.268  28.061  -9.929  1.00 31.19  ? 363  ASN A ND2 1 
ATOM   2233  N N   . ARG A 1 355 ? 15.345  23.314  -8.553  1.00 26.05  ? 364  ARG A N   1 
ATOM   2234  C CA  . ARG A 1 355 ? 16.257  22.273  -8.883  1.00 26.25  ? 364  ARG A CA  1 
ATOM   2235  C C   . ARG A 1 355 ? 15.533  20.977  -9.038  1.00 25.85  ? 364  ARG A C   1 
ATOM   2236  O O   . ARG A 1 355 ? 14.774  20.638  -8.191  1.00 25.39  ? 364  ARG A O   1 
ATOM   2237  C CB  . ARG A 1 355 ? 17.228  22.140  -7.762  1.00 26.08  ? 364  ARG A CB  1 
ATOM   2238  C CG  . ARG A 1 355 ? 18.546  21.835  -8.219  1.00 27.67  ? 364  ARG A CG  1 
ATOM   2239  C CD  . ARG A 1 355 ? 19.047  22.924  -9.053  1.00 28.13  ? 364  ARG A CD  1 
ATOM   2240  N NE  . ARG A 1 355 ? 19.625  22.281  -10.206 1.00 30.45  ? 364  ARG A NE  1 
ATOM   2241  C CZ  . ARG A 1 355 ? 20.564  22.828  -10.942 1.00 31.81  ? 364  ARG A CZ  1 
ATOM   2242  N NH1 . ARG A 1 355 ? 21.013  24.041  -10.636 1.00 32.09  ? 364  ARG A NH1 1 
ATOM   2243  N NH2 . ARG A 1 355 ? 21.032  22.167  -11.983 1.00 33.96  ? 364  ARG A NH2 1 
ATOM   2244  N N   . VAL A 1 356 ? 15.766  20.259  -10.125 1.00 26.72  ? 365  VAL A N   1 
ATOM   2245  C CA  . VAL A 1 356 ? 15.089  18.987  -10.431 1.00 26.76  ? 365  VAL A CA  1 
ATOM   2246  C C   . VAL A 1 356 ? 16.090  17.889  -10.661 1.00 28.33  ? 365  VAL A C   1 
ATOM   2247  O O   . VAL A 1 356 ? 17.222  18.140  -11.145 1.00 30.04  ? 365  VAL A O   1 
ATOM   2248  C CB  . VAL A 1 356 ? 14.342  19.045  -11.728 1.00 26.72  ? 365  VAL A CB  1 
ATOM   2249  C CG1 . VAL A 1 356 ? 13.999  17.672  -12.175 1.00 26.67  ? 365  VAL A CG1 1 
ATOM   2250  C CG2 . VAL A 1 356 ? 13.140  19.851  -11.571 1.00 26.39  ? 365  VAL A CG2 1 
ATOM   2251  N N   . PHE A 1 357 ? 15.675  16.665  -10.349 1.00 28.32  ? 366  PHE A N   1 
ATOM   2252  C CA  . PHE A 1 357 ? 16.601  15.545  -10.315 1.00 29.17  ? 366  PHE A CA  1 
ATOM   2253  C C   . PHE A 1 357 ? 15.862  14.368  -10.798 1.00 29.84  ? 366  PHE A C   1 
ATOM   2254  O O   . PHE A 1 357 ? 15.001  13.868  -10.127 1.00 29.44  ? 366  PHE A O   1 
ATOM   2255  C CB  . PHE A 1 357 ? 17.094  15.245  -8.889  1.00 28.47  ? 366  PHE A CB  1 
ATOM   2256  C CG  . PHE A 1 357 ? 17.939  16.335  -8.264  1.00 27.46  ? 366  PHE A CG  1 
ATOM   2257  C CD1 . PHE A 1 357 ? 17.372  17.508  -7.782  1.00 26.68  ? 366  PHE A CD1 1 
ATOM   2258  C CD2 . PHE A 1 357 ? 19.288  16.161  -8.120  1.00 27.24  ? 366  PHE A CD2 1 
ATOM   2259  C CE1 . PHE A 1 357 ? 18.138  18.480  -7.197  1.00 25.47  ? 366  PHE A CE1 1 
ATOM   2260  C CE2 . PHE A 1 357 ? 20.053  17.128  -7.531  1.00 26.00  ? 366  PHE A CE2 1 
ATOM   2261  C CZ  . PHE A 1 357 ? 19.480  18.282  -7.062  1.00 24.96  ? 366  PHE A CZ  1 
ATOM   2262  N N   . CYS A 1 358 ? 16.197  13.909  -11.971 1.00 31.65  ? 367  CYS A N   1 
ATOM   2263  C CA  . CYS A 1 358 ? 15.485  12.774  -12.526 1.00 33.62  ? 367  CYS A CA  1 
ATOM   2264  C C   . CYS A 1 358 ? 16.397  11.619  -12.887 1.00 35.36  ? 367  CYS A C   1 
ATOM   2265  O O   . CYS A 1 358 ? 17.609  11.749  -12.900 1.00 36.38  ? 367  CYS A O   1 
ATOM   2266  C CB  . CYS A 1 358 ? 14.706  13.190  -13.767 1.00 34.17  ? 367  CYS A CB  1 
ATOM   2267  S SG  . CYS A 1 358 ? 13.432  14.428  -13.513 1.00 34.44  ? 367  CYS A SG  1 
ATOM   2268  N N   . ASP A 1 359 ? 15.806  10.494  -13.220 1.00 36.46  ? 368  ASP A N   1 
ATOM   2269  C CA  . ASP A 1 359 ? 16.571  9.321   -13.437 1.00 38.59  ? 368  ASP A CA  1 
ATOM   2270  C C   . ASP A 1 359 ? 16.415  8.859   -14.859 1.00 40.76  ? 368  ASP A C   1 
ATOM   2271  O O   . ASP A 1 359 ? 15.337  8.436   -15.276 1.00 41.40  ? 368  ASP A O   1 
ATOM   2272  C CB  . ASP A 1 359 ? 16.068  8.261   -12.493 1.00 38.86  ? 368  ASP A CB  1 
ATOM   2273  C CG  . ASP A 1 359 ? 17.019  7.145   -12.335 1.00 40.98  ? 368  ASP A CG  1 
ATOM   2274  O OD1 . ASP A 1 359 ? 17.525  6.640   -13.365 1.00 43.41  ? 368  ASP A OD1 1 
ATOM   2275  O OD2 . ASP A 1 359 ? 17.264  6.777   -11.170 1.00 41.11  ? 368  ASP A OD2 1 
ATOM   2276  N N   . THR A 1 360 ? 17.500  8.935   -15.610 1.00 42.63  ? 369  THR A N   1 
ATOM   2277  C CA  . THR A 1 360 ? 17.554  8.411   -16.954 1.00 44.92  ? 369  THR A CA  1 
ATOM   2278  C C   . THR A 1 360 ? 16.928  7.049   -17.033 1.00 47.48  ? 369  THR A C   1 
ATOM   2279  O O   . THR A 1 360 ? 16.010  6.860   -17.795 1.00 48.87  ? 369  THR A O   1 
ATOM   2280  C CB  . THR A 1 360 ? 18.960  8.262   -17.391 1.00 45.78  ? 369  THR A CB  1 
ATOM   2281  O OG1 . THR A 1 360 ? 19.565  9.540   -17.327 1.00 43.49  ? 369  THR A OG1 1 
ATOM   2282  C CG2 . THR A 1 360 ? 19.024  7.768   -18.799 1.00 48.44  ? 369  THR A CG2 1 
ATOM   2283  N N   . MET A 1 361 ? 17.405  6.103   -16.241 1.00 49.29  ? 370  MET A N   1 
ATOM   2284  C CA  . MET A 1 361 ? 16.959  4.713   -16.344 1.00 52.19  ? 370  MET A CA  1 
ATOM   2285  C C   . MET A 1 361 ? 15.826  4.427   -17.313 1.00 52.69  ? 370  MET A C   1 
ATOM   2286  O O   . MET A 1 361 ? 16.020  3.784   -18.351 1.00 54.46  ? 370  MET A O   1 
ATOM   2287  C CB  . MET A 1 361 ? 16.646  4.101   -14.973 1.00 52.71  ? 370  MET A CB  1 
ATOM   2288  C CG  . MET A 1 361 ? 17.678  3.035   -14.533 1.00 57.86  ? 370  MET A CG  1 
ATOM   2289  S SD  . MET A 1 361 ? 17.949  1.607   -15.681 1.00 68.20  ? 370  MET A SD  1 
ATOM   2290  C CE  . MET A 1 361 ? 18.727  2.286   -17.194 1.00 66.26  ? 370  MET A CE  1 
ATOM   2291  N N   . ASN A 1 362 ? 14.630  4.892   -16.997 1.00 51.23  ? 371  ASN A N   1 
ATOM   2292  C CA  . ASN A 1 362 ? 13.590  4.558   -17.930 1.00 51.91  ? 371  ASN A CA  1 
ATOM   2293  C C   . ASN A 1 362 ? 13.109  5.632   -18.921 1.00 50.76  ? 371  ASN A C   1 
ATOM   2294  O O   . ASN A 1 362 ? 12.291  5.344   -19.798 1.00 51.96  ? 371  ASN A O   1 
ATOM   2295  C CB  . ASN A 1 362 ? 12.497  3.729   -17.255 1.00 52.65  ? 371  ASN A CB  1 
ATOM   2296  C CG  . ASN A 1 362 ? 12.837  2.227   -17.258 1.00 55.11  ? 371  ASN A CG  1 
ATOM   2297  O OD1 . ASN A 1 362 ? 12.619  1.523   -18.249 1.00 56.61  ? 371  ASN A OD1 1 
ATOM   2298  N ND2 . ASN A 1 362 ? 13.380  1.745   -16.148 1.00 56.04  ? 371  ASN A ND2 1 
ATOM   2299  N N   . SER A 1 363 ? 13.677  6.833   -18.834 1.00 48.58  ? 372  SER A N   1 
ATOM   2300  C CA  . SER A 1 363 ? 13.354  7.943   -19.741 1.00 46.98  ? 372  SER A CA  1 
ATOM   2301  C C   . SER A 1 363 ? 13.047  7.561   -21.179 1.00 47.75  ? 372  SER A C   1 
ATOM   2302  O O   . SER A 1 363 ? 13.414  6.490   -21.665 1.00 49.37  ? 372  SER A O   1 
ATOM   2303  C CB  . SER A 1 363 ? 14.495  8.935   -19.766 1.00 46.29  ? 372  SER A CB  1 
ATOM   2304  O OG  . SER A 1 363 ? 15.677  8.237   -20.069 1.00 48.37  ? 372  SER A OG  1 
ATOM   2305  N N   . LEU A 1 364 ? 12.351  8.463   -21.850 1.00 46.36  ? 373  LEU A N   1 
ATOM   2306  C CA  . LEU A 1 364 ? 12.096  8.343   -23.270 1.00 46.71  ? 373  LEU A CA  1 
ATOM   2307  C C   . LEU A 1 364 ? 12.708  9.542   -23.937 1.00 45.67  ? 373  LEU A C   1 
ATOM   2308  O O   . LEU A 1 364 ? 12.507  10.667  -23.494 1.00 44.26  ? 373  LEU A O   1 
ATOM   2309  C CB  . LEU A 1 364 ? 10.601  8.341   -23.531 1.00 46.62  ? 373  LEU A CB  1 
ATOM   2310  C CG  . LEU A 1 364 ? 9.933   7.001   -23.802 1.00 47.88  ? 373  LEU A CG  1 
ATOM   2311  C CD1 . LEU A 1 364 ? 10.660  5.843   -23.129 1.00 49.50  ? 373  LEU A CD1 1 
ATOM   2312  C CD2 . LEU A 1 364 ? 8.469   7.084   -23.378 1.00 46.86  ? 373  LEU A CD2 1 
ATOM   2313  N N   . THR A 1 365 ? 13.451  9.300   -25.006 1.00 46.41  ? 374  THR A N   1 
ATOM   2314  C CA  . THR A 1 365 ? 14.148  10.378  -25.683 1.00 45.67  ? 374  THR A CA  1 
ATOM   2315  C C   . THR A 1 365 ? 13.377  10.851  -26.887 1.00 45.27  ? 374  THR A C   1 
ATOM   2316  O O   . THR A 1 365 ? 12.958  10.047  -27.695 1.00 46.72  ? 374  THR A O   1 
ATOM   2317  C CB  . THR A 1 365 ? 15.501  9.946   -26.124 1.00 46.92  ? 374  THR A CB  1 
ATOM   2318  O OG1 . THR A 1 365 ? 15.880  8.802   -25.355 1.00 48.97  ? 374  THR A OG1 1 
ATOM   2319  C CG2 . THR A 1 365 ? 16.487  11.093  -25.902 1.00 45.92  ? 374  THR A CG2 1 
ATOM   2320  N N   . LEU A 1 366 ? 13.196  12.160  -26.997 1.00 43.34  ? 375  LEU A N   1 
ATOM   2321  C CA  . LEU A 1 366 ? 12.254  12.731  -27.943 1.00 42.32  ? 375  LEU A CA  1 
ATOM   2322  C C   . LEU A 1 366 ? 12.863  14.000  -28.467 1.00 42.23  ? 375  LEU A C   1 
ATOM   2323  O O   . LEU A 1 366 ? 13.723  14.599  -27.798 1.00 41.70  ? 375  LEU A O   1 
ATOM   2324  C CB  . LEU A 1 366 ? 10.963  13.118  -27.224 1.00 40.53  ? 375  LEU A CB  1 
ATOM   2325  C CG  . LEU A 1 366 ? 10.217  12.150  -26.321 1.00 38.15  ? 375  LEU A CG  1 
ATOM   2326  C CD1 . LEU A 1 366 ? 9.127   12.879  -25.600 1.00 33.67  ? 375  LEU A CD1 1 
ATOM   2327  C CD2 . LEU A 1 366 ? 9.654   11.076  -27.157 1.00 39.09  ? 375  LEU A CD2 1 
ATOM   2328  N N   . PRO A 1 367 ? 12.404  14.440  -29.640 1.00 42.69  ? 376  PRO A N   1 
ATOM   2329  C CA  . PRO A 1 367 ? 12.833  15.667  -30.294 1.00 43.02  ? 376  PRO A CA  1 
ATOM   2330  C C   . PRO A 1 367 ? 12.203  16.930  -29.744 1.00 42.10  ? 376  PRO A C   1 
ATOM   2331  O O   . PRO A 1 367 ? 11.064  16.909  -29.330 1.00 41.55  ? 376  PRO A O   1 
ATOM   2332  C CB  . PRO A 1 367 ? 12.352  15.474  -31.714 1.00 44.11  ? 376  PRO A CB  1 
ATOM   2333  C CG  . PRO A 1 367 ? 11.196  14.642  -31.569 1.00 44.35  ? 376  PRO A CG  1 
ATOM   2334  C CD  . PRO A 1 367 ? 11.481  13.680  -30.477 1.00 43.67  ? 376  PRO A CD  1 
ATOM   2335  N N   . SER A 1 368 ? 12.940  18.031  -29.780 1.00 42.54  ? 377  SER A N   1 
ATOM   2336  C CA  . SER A 1 368 ? 12.439  19.358  -29.390 1.00 42.40  ? 377  SER A CA  1 
ATOM   2337  C C   . SER A 1 368 ? 11.102  19.686  -30.051 1.00 42.73  ? 377  SER A C   1 
ATOM   2338  O O   . SER A 1 368 ? 10.351  20.538  -29.591 1.00 41.75  ? 377  SER A O   1 
ATOM   2339  C CB  . SER A 1 368 ? 13.433  20.454  -29.785 1.00 42.99  ? 377  SER A CB  1 
ATOM   2340  O OG  . SER A 1 368 ? 14.771  19.976  -29.907 1.00 45.16  ? 377  SER A OG  1 
ATOM   2341  N N   . GLU A 1 369 ? 10.819  19.012  -31.148 1.00 44.45  ? 378  GLU A N   1 
ATOM   2342  C CA  . GLU A 1 369 ? 9.547   19.167  -31.836 1.00 45.57  ? 378  GLU A CA  1 
ATOM   2343  C C   . GLU A 1 369 ? 8.335   18.764  -30.973 1.00 44.78  ? 378  GLU A C   1 
ATOM   2344  O O   . GLU A 1 369 ? 7.217   19.188  -31.226 1.00 44.59  ? 378  GLU A O   1 
ATOM   2345  C CB  . GLU A 1 369 ? 9.566   18.370  -33.132 1.00 47.36  ? 378  GLU A CB  1 
ATOM   2346  C CG  . GLU A 1 369 ? 10.366  19.020  -34.254 1.00 50.54  ? 378  GLU A CG  1 
ATOM   2347  C CD  . GLU A 1 369 ? 11.892  19.176  -33.977 1.00 54.15  ? 378  GLU A CD  1 
ATOM   2348  O OE1 . GLU A 1 369 ? 12.444  18.633  -32.977 1.00 53.18  ? 378  GLU A OE1 1 
ATOM   2349  O OE2 . GLU A 1 369 ? 12.549  19.848  -34.812 1.00 57.08  ? 378  GLU A OE2 1 
ATOM   2350  N N   . VAL A 1 370 ? 8.560   17.967  -29.941 1.00 44.47  ? 379  VAL A N   1 
ATOM   2351  C CA  . VAL A 1 370 ? 7.542   17.724  -28.955 1.00 43.74  ? 379  VAL A CA  1 
ATOM   2352  C C   . VAL A 1 370 ? 6.909   19.000  -28.498 1.00 43.21  ? 379  VAL A C   1 
ATOM   2353  O O   . VAL A 1 370 ? 5.728   19.062  -28.377 1.00 43.35  ? 379  VAL A O   1 
ATOM   2354  C CB  . VAL A 1 370 ? 8.127   17.083  -27.759 1.00 42.96  ? 379  VAL A CB  1 
ATOM   2355  C CG1 . VAL A 1 370 ? 7.448   17.582  -26.541 1.00 42.18  ? 379  VAL A CG1 1 
ATOM   2356  C CG2 . VAL A 1 370 ? 7.956   15.624  -27.884 1.00 44.13  ? 379  VAL A CG2 1 
ATOM   2357  N N   . ASN A 1 371 ? 7.692   20.029  -28.249 1.00 43.56  ? 380  ASN A N   1 
ATOM   2358  C CA  . ASN A 1 371 ? 7.143   21.300  -27.792 1.00 43.97  ? 380  ASN A CA  1 
ATOM   2359  C C   . ASN A 1 371 ? 5.989   21.896  -28.590 1.00 44.36  ? 380  ASN A C   1 
ATOM   2360  O O   . ASN A 1 371 ? 5.124   22.530  -28.007 1.00 44.21  ? 380  ASN A O   1 
ATOM   2361  C CB  . ASN A 1 371 ? 8.237   22.343  -27.679 1.00 44.37  ? 380  ASN A CB  1 
ATOM   2362  C CG  . ASN A 1 371 ? 9.302   21.935  -26.694 1.00 46.54  ? 380  ASN A CG  1 
ATOM   2363  O OD1 . ASN A 1 371 ? 9.204   22.232  -25.485 1.00 48.89  ? 380  ASN A OD1 1 
ATOM   2364  N ND2 . ASN A 1 371 ? 10.327  21.225  -27.187 1.00 49.27  ? 380  ASN A ND2 1 
ATOM   2365  N N   . LEU A 1 372 ? 5.953   21.717  -29.902 1.00 45.03  ? 381  LEU A N   1 
ATOM   2366  C CA  . LEU A 1 372 ? 4.886   22.337  -30.672 1.00 45.71  ? 381  LEU A CA  1 
ATOM   2367  C C   . LEU A 1 372 ? 3.531   21.782  -30.234 1.00 45.69  ? 381  LEU A C   1 
ATOM   2368  O O   . LEU A 1 372 ? 2.468   22.408  -30.378 1.00 46.04  ? 381  LEU A O   1 
ATOM   2369  C CB  . LEU A 1 372 ? 5.091   22.079  -32.146 1.00 47.03  ? 381  LEU A CB  1 
ATOM   2370  C CG  . LEU A 1 372 ? 6.537   21.929  -32.582 1.00 48.25  ? 381  LEU A CG  1 
ATOM   2371  C CD1 . LEU A 1 372 ? 6.578   21.406  -34.030 1.00 50.06  ? 381  LEU A CD1 1 
ATOM   2372  C CD2 . LEU A 1 372 ? 7.328   23.243  -32.393 1.00 48.98  ? 381  LEU A CD2 1 
ATOM   2373  N N   . CYS A 1 373 ? 3.576   20.587  -29.678 1.00 45.44  ? 382  CYS A N   1 
ATOM   2374  C CA  . CYS A 1 373 ? 2.385   19.983  -29.177 1.00 45.39  ? 382  CYS A CA  1 
ATOM   2375  C C   . CYS A 1 373 ? 1.725   20.831  -28.096 1.00 44.34  ? 382  CYS A C   1 
ATOM   2376  O O   . CYS A 1 373 ? 0.542   20.717  -27.918 1.00 44.62  ? 382  CYS A O   1 
ATOM   2377  C CB  . CYS A 1 373 ? 2.680   18.562  -28.728 1.00 45.46  ? 382  CYS A CB  1 
ATOM   2378  S SG  . CYS A 1 373 ? 2.634   17.454  -30.142 1.00 48.62  ? 382  CYS A SG  1 
ATOM   2379  N N   . ASN A 1 374 ? 2.464   21.713  -27.413 1.00 43.42  ? 383  ASN A N   1 
ATOM   2380  C CA  . ASN A 1 374 ? 1.866   22.595  -26.395 1.00 42.79  ? 383  ASN A CA  1 
ATOM   2381  C C   . ASN A 1 374 ? 0.991   23.615  -27.041 1.00 43.49  ? 383  ASN A C   1 
ATOM   2382  O O   . ASN A 1 374 ? 0.102   24.145  -26.401 1.00 43.60  ? 383  ASN A O   1 
ATOM   2383  C CB  . ASN A 1 374 ? 2.908   23.350  -25.577 1.00 41.87  ? 383  ASN A CB  1 
ATOM   2384  C CG  . ASN A 1 374 ? 3.903   22.430  -24.921 1.00 42.07  ? 383  ASN A CG  1 
ATOM   2385  O OD1 . ASN A 1 374 ? 3.522   21.426  -24.340 1.00 42.65  ? 383  ASN A OD1 1 
ATOM   2386  N ND2 . ASN A 1 374 ? 5.198   22.755  -25.027 1.00 43.25  ? 383  ASN A ND2 1 
ATOM   2387  N N   . VAL A 1 375 ? 1.256   23.902  -28.306 1.00 44.32  ? 384  VAL A N   1 
ATOM   2388  C CA  . VAL A 1 375 ? 0.488   24.898  -29.008 1.00 45.17  ? 384  VAL A CA  1 
ATOM   2389  C C   . VAL A 1 375 ? -0.525  24.251  -29.928 1.00 46.54  ? 384  VAL A C   1 
ATOM   2390  O O   . VAL A 1 375 ? -1.656  24.738  -30.024 1.00 46.89  ? 384  VAL A O   1 
ATOM   2391  C CB  . VAL A 1 375 ? 1.387   25.842  -29.821 1.00 45.46  ? 384  VAL A CB  1 
ATOM   2392  C CG1 . VAL A 1 375 ? 0.550   26.652  -30.820 1.00 46.82  ? 384  VAL A CG1 1 
ATOM   2393  C CG2 . VAL A 1 375 ? 2.136   26.769  -28.917 1.00 44.10  ? 384  VAL A CG2 1 
ATOM   2394  N N   . ASP A 1 376 ? -0.132  23.167  -30.607 1.00 47.48  ? 385  ASP A N   1 
ATOM   2395  C CA  . ASP A 1 376 ? -0.985  22.663  -31.678 1.00 49.30  ? 385  ASP A CA  1 
ATOM   2396  C C   . ASP A 1 376 ? -1.612  21.260  -31.628 1.00 50.03  ? 385  ASP A C   1 
ATOM   2397  O O   . ASP A 1 376 ? -2.835  21.114  -31.894 1.00 50.94  ? 385  ASP A O   1 
ATOM   2398  C CB  . ASP A 1 376 ? -0.372  22.916  -33.014 1.00 50.08  ? 385  ASP A CB  1 
ATOM   2399  C CG  . ASP A 1 376 ? -1.394  23.359  -34.018 1.00 53.10  ? 385  ASP A CG  1 
ATOM   2400  O OD1 . ASP A 1 376 ? -2.618  23.246  -33.773 1.00 54.73  ? 385  ASP A OD1 1 
ATOM   2401  O OD2 . ASP A 1 376 ? -0.977  23.823  -35.089 1.00 56.59  ? 385  ASP A OD2 1 
ATOM   2402  N N   . ILE A 1 377 ? -0.834  20.232  -31.286 1.00 49.58  ? 386  ILE A N   1 
ATOM   2403  C CA  . ILE A 1 377 ? -1.436  18.888  -31.182 1.00 50.24  ? 386  ILE A CA  1 
ATOM   2404  C C   . ILE A 1 377 ? -1.411  18.313  -32.589 1.00 52.09  ? 386  ILE A C   1 
ATOM   2405  O O   . ILE A 1 377 ? -0.622  17.406  -32.899 1.00 52.44  ? 386  ILE A O   1 
ATOM   2406  C CB  . ILE A 1 377 ? -2.941  18.917  -30.670 1.00 49.92  ? 386  ILE A CB  1 
ATOM   2407  C CG1 . ILE A 1 377 ? -3.033  19.139  -29.185 1.00 47.90  ? 386  ILE A CG1 1 
ATOM   2408  C CG2 . ILE A 1 377 ? -3.612  17.637  -30.934 1.00 50.79  ? 386  ILE A CG2 1 
ATOM   2409  C CD1 . ILE A 1 377 ? -4.273  19.796  -28.789 1.00 47.03  ? 386  ILE A CD1 1 
ATOM   2410  N N   . PHE A 1 378 ? -2.303  18.854  -33.418 1.00 53.08  ? 387  PHE A N   1 
ATOM   2411  C CA  . PHE A 1 378 ? -2.307  18.605  -34.824 1.00 54.54  ? 387  PHE A CA  1 
ATOM   2412  C C   . PHE A 1 378 ? -1.338  19.584  -35.386 1.00 54.35  ? 387  PHE A C   1 
ATOM   2413  O O   . PHE A 1 378 ? -1.421  20.771  -35.111 1.00 53.78  ? 387  PHE A O   1 
ATOM   2414  C CB  . PHE A 1 378 ? -3.688  18.849  -35.365 1.00 55.31  ? 387  PHE A CB  1 
ATOM   2415  C CG  . PHE A 1 378 ? -4.722  18.176  -34.580 1.00 55.62  ? 387  PHE A CG  1 
ATOM   2416  C CD1 . PHE A 1 378 ? -5.643  18.909  -33.839 1.00 55.70  ? 387  PHE A CD1 1 
ATOM   2417  C CD2 . PHE A 1 378 ? -4.762  16.797  -34.532 1.00 55.85  ? 387  PHE A CD2 1 
ATOM   2418  C CE1 . PHE A 1 378 ? -6.627  18.272  -33.082 1.00 55.04  ? 387  PHE A CE1 1 
ATOM   2419  C CE2 . PHE A 1 378 ? -5.734  16.149  -33.779 1.00 56.36  ? 387  PHE A CE2 1 
ATOM   2420  C CZ  . PHE A 1 378 ? -6.670  16.889  -33.045 1.00 55.34  ? 387  PHE A CZ  1 
ATOM   2421  N N   . ASN A 1 379 ? -0.390  19.054  -36.132 1.00 55.05  ? 388  ASN A N   1 
ATOM   2422  C CA  . ASN A 1 379 ? 0.681   19.809  -36.741 1.00 55.46  ? 388  ASN A CA  1 
ATOM   2423  C C   . ASN A 1 379 ? 1.601   18.752  -37.233 1.00 56.92  ? 388  ASN A C   1 
ATOM   2424  O O   . ASN A 1 379 ? 1.884   17.799  -36.502 1.00 56.53  ? 388  ASN A O   1 
ATOM   2425  C CB  . ASN A 1 379 ? 1.468   20.685  -35.764 1.00 53.54  ? 388  ASN A CB  1 
ATOM   2426  C CG  . ASN A 1 379 ? 2.031   19.892  -34.584 1.00 52.63  ? 388  ASN A CG  1 
ATOM   2427  O OD1 . ASN A 1 379 ? 3.133   19.319  -34.647 1.00 50.27  ? 388  ASN A OD1 1 
ATOM   2428  N ND2 . ASN A 1 379 ? 1.261   19.868  -33.473 1.00 52.82  ? 388  ASN A ND2 1 
ATOM   2429  N N   . PRO A 1 380 ? 2.074   18.908  -38.479 1.00 58.80  ? 389  PRO A N   1 
ATOM   2430  C CA  . PRO A 1 380 ? 3.144   18.103  -39.092 1.00 60.12  ? 389  PRO A CA  1 
ATOM   2431  C C   . PRO A 1 380 ? 4.260   18.167  -38.097 1.00 59.47  ? 389  PRO A C   1 
ATOM   2432  O O   . PRO A 1 380 ? 4.179   19.002  -37.196 1.00 58.89  ? 389  PRO A O   1 
ATOM   2433  C CB  . PRO A 1 380 ? 3.545   18.941  -40.298 1.00 61.13  ? 389  PRO A CB  1 
ATOM   2434  C CG  . PRO A 1 380 ? 3.042   20.400  -39.934 1.00 59.79  ? 389  PRO A CG  1 
ATOM   2435  C CD  . PRO A 1 380 ? 1.753   20.113  -39.269 1.00 59.09  ? 389  PRO A CD  1 
ATOM   2436  N N   . LYS A 1 381 ? 5.292   17.345  -38.206 1.00 59.97  ? 390  LYS A N   1 
ATOM   2437  C CA  . LYS A 1 381 ? 6.399   17.481  -37.232 1.00 59.18  ? 390  LYS A CA  1 
ATOM   2438  C C   . LYS A 1 381 ? 6.223   16.614  -35.982 1.00 58.40  ? 390  LYS A C   1 
ATOM   2439  O O   . LYS A 1 381 ? 7.163   15.903  -35.602 1.00 59.12  ? 390  LYS A O   1 
ATOM   2440  C CB  . LYS A 1 381 ? 6.643   18.952  -36.800 1.00 57.89  ? 390  LYS A CB  1 
ATOM   2441  C CG  . LYS A 1 381 ? 7.375   19.876  -37.795 1.00 59.25  ? 390  LYS A CG  1 
ATOM   2442  C CD  . LYS A 1 381 ? 8.893   19.612  -37.783 1.00 62.52  ? 390  LYS A CD  1 
ATOM   2443  C CE  . LYS A 1 381 ? 9.723   20.867  -38.081 1.00 63.31  ? 390  LYS A CE  1 
ATOM   2444  N NZ  . LYS A 1 381 ? 9.807   21.195  -39.554 1.00 65.89  ? 390  LYS A NZ  1 
ATOM   2445  N N   . TYR A 1 382 ? 5.064   16.662  -35.327 1.00 57.21  ? 391  TYR A N   1 
ATOM   2446  C CA  . TYR A 1 382 ? 4.847   15.698  -34.276 1.00 56.43  ? 391  TYR A CA  1 
ATOM   2447  C C   . TYR A 1 382 ? 3.457   15.183  -34.136 1.00 57.02  ? 391  TYR A C   1 
ATOM   2448  O O   . TYR A 1 382 ? 2.537   15.939  -33.806 1.00 56.74  ? 391  TYR A O   1 
ATOM   2449  C CB  . TYR A 1 382 ? 5.257   16.271  -32.949 1.00 54.87  ? 391  TYR A CB  1 
ATOM   2450  C CG  . TYR A 1 382 ? 5.835   15.231  -32.021 1.00 54.32  ? 391  TYR A CG  1 
ATOM   2451  C CD1 . TYR A 1 382 ? 7.004   14.589  -32.337 1.00 55.20  ? 391  TYR A CD1 1 
ATOM   2452  C CD2 . TYR A 1 382 ? 5.226   14.911  -30.816 1.00 53.39  ? 391  TYR A CD2 1 
ATOM   2453  C CE1 . TYR A 1 382 ? 7.544   13.665  -31.501 1.00 54.81  ? 391  TYR A CE1 1 
ATOM   2454  C CE2 . TYR A 1 382 ? 5.768   13.973  -29.974 1.00 52.44  ? 391  TYR A CE2 1 
ATOM   2455  C CZ  . TYR A 1 382 ? 6.919   13.364  -30.335 1.00 53.17  ? 391  TYR A CZ  1 
ATOM   2456  O OH  . TYR A 1 382 ? 7.476   12.429  -29.539 1.00 53.26  ? 391  TYR A OH  1 
ATOM   2457  N N   . ASP A 1 383 ? 3.297   13.882  -34.349 1.00 58.18  ? 392  ASP A N   1 
ATOM   2458  C CA  . ASP A 1 383 ? 2.089   13.222  -33.845 1.00 58.58  ? 392  ASP A CA  1 
ATOM   2459  C C   . ASP A 1 383 ? 2.227   13.071  -32.335 1.00 56.85  ? 392  ASP A C   1 
ATOM   2460  O O   . ASP A 1 383 ? 3.302   12.822  -31.795 1.00 56.74  ? 392  ASP A O   1 
ATOM   2461  C CB  . ASP A 1 383 ? 1.715   11.912  -34.561 1.00 60.65  ? 392  ASP A CB  1 
ATOM   2462  C CG  . ASP A 1 383 ? 2.778   11.437  -35.528 1.00 62.56  ? 392  ASP A CG  1 
ATOM   2463  O OD1 . ASP A 1 383 ? 3.953   11.267  -35.109 1.00 63.53  ? 392  ASP A OD1 1 
ATOM   2464  O OD2 . ASP A 1 383 ? 2.424   11.210  -36.703 1.00 63.80  ? 392  ASP A OD2 1 
ATOM   2465  N N   . CYS A 1 384 ? 1.111   13.200  -31.674 1.00 55.51  ? 393  CYS A N   1 
ATOM   2466  C CA  . CYS A 1 384 ? 1.096   13.911  -30.495 1.00 53.50  ? 393  CYS A CA  1 
ATOM   2467  C C   . CYS A 1 384 ? 0.125   13.141  -29.611 1.00 53.12  ? 393  CYS A C   1 
ATOM   2468  O O   . CYS A 1 384 ? -1.042  13.124  -29.878 1.00 53.77  ? 393  CYS A O   1 
ATOM   2469  C CB  . CYS A 1 384 ? 0.613   15.258  -30.978 1.00 52.82  ? 393  CYS A CB  1 
ATOM   2470  S SG  . CYS A 1 384 ? 0.797   16.576  -29.906 1.00 54.60  ? 393  CYS A SG  1 
ATOM   2471  N N   . LYS A 1 385 ? 0.608   12.440  -28.591 1.00 52.42  ? 394  LYS A N   1 
ATOM   2472  C CA  . LYS A 1 385 ? -0.267  11.519  -27.821 1.00 52.62  ? 394  LYS A CA  1 
ATOM   2473  C C   . LYS A 1 385 ? -1.405  12.228  -27.048 1.00 51.25  ? 394  LYS A C   1 
ATOM   2474  O O   . LYS A 1 385 ? -1.208  13.269  -26.405 1.00 49.86  ? 394  LYS A O   1 
ATOM   2475  C CB  . LYS A 1 385 ? 0.552   10.574  -26.922 1.00 52.75  ? 394  LYS A CB  1 
ATOM   2476  C CG  . LYS A 1 385 ? 1.774   9.931   -27.611 1.00 55.30  ? 394  LYS A CG  1 
ATOM   2477  C CD  . LYS A 1 385 ? 2.619   9.005   -26.646 1.00 60.75  ? 394  LYS A CD  1 
ATOM   2478  C CE  . LYS A 1 385 ? 3.671   9.722   -25.592 1.00 61.20  ? 394  LYS A CE  1 
ATOM   2479  N NZ  . LYS A 1 385 ? 3.239   9.813   -24.102 1.00 60.39  ? 394  LYS A NZ  1 
ATOM   2480  N N   . ILE A 1 386 ? -2.584  11.629  -27.113 1.00 51.65  ? 395  ILE A N   1 
ATOM   2481  C CA  . ILE A 1 386 ? -3.854  12.311  -26.884 1.00 51.41  ? 395  ILE A CA  1 
ATOM   2482  C C   . ILE A 1 386 ? -4.810  11.254  -26.459 1.00 53.03  ? 395  ILE A C   1 
ATOM   2483  O O   . ILE A 1 386 ? -4.595  10.125  -26.851 1.00 54.74  ? 395  ILE A O   1 
ATOM   2484  C CB  . ILE A 1 386 ? -4.389  12.732  -28.241 1.00 52.19  ? 395  ILE A CB  1 
ATOM   2485  C CG1 . ILE A 1 386 ? -3.997  14.143  -28.526 1.00 51.85  ? 395  ILE A CG1 1 
ATOM   2486  C CG2 . ILE A 1 386 ? -5.897  12.676  -28.371 1.00 52.82  ? 395  ILE A CG2 1 
ATOM   2487  C CD1 . ILE A 1 386 ? -4.491  14.520  -29.879 1.00 54.90  ? 395  ILE A CD1 1 
ATOM   2488  N N   . MET A 1 387 ? -5.885  11.559  -25.720 1.00 53.12  ? 396  MET A N   1 
ATOM   2489  C CA  . MET A 1 387 ? -6.999  10.604  -25.696 1.00 54.96  ? 396  MET A CA  1 
ATOM   2490  C C   . MET A 1 387 ? -8.311  11.241  -26.017 1.00 55.69  ? 396  MET A C   1 
ATOM   2491  O O   . MET A 1 387 ? -8.492  12.437  -25.803 1.00 54.79  ? 396  MET A O   1 
ATOM   2492  C CB  . MET A 1 387 ? -7.077  9.846   -24.405 1.00 55.17  ? 396  MET A CB  1 
ATOM   2493  C CG  . MET A 1 387 ? -7.665  10.605  -23.265 1.00 55.81  ? 396  MET A CG  1 
ATOM   2494  S SD  . MET A 1 387 ? -7.941  9.400   -21.932 1.00 61.59  ? 396  MET A SD  1 
ATOM   2495  C CE  . MET A 1 387 ? -6.325  8.529   -21.935 1.00 60.22  ? 396  MET A CE  1 
ATOM   2496  N N   . THR A 1 388 ? -9.222  10.406  -26.503 1.00 57.50  ? 397  THR A N   1 
ATOM   2497  C CA  . THR A 1 388 ? -10.406 10.841  -27.208 1.00 58.47  ? 397  THR A CA  1 
ATOM   2498  C C   . THR A 1 388 ? -11.665 10.593  -26.450 1.00 59.64  ? 397  THR A C   1 
ATOM   2499  O O   . THR A 1 388 ? -11.822 9.520   -25.857 1.00 60.73  ? 397  THR A O   1 
ATOM   2500  C CB  . THR A 1 388 ? -10.497 10.042  -28.466 1.00 60.18  ? 397  THR A CB  1 
ATOM   2501  O OG1 . THR A 1 388 ? -9.641  10.663  -29.398 1.00 59.50  ? 397  THR A OG1 1 
ATOM   2502  C CG2 . THR A 1 388 ? -11.912 10.010  -29.062 1.00 62.61  ? 397  THR A CG2 1 
ATOM   2503  N N   . SER A 1 389 ? -12.572 11.572  -26.481 1.00 59.69  ? 398  SER A N   1 
ATOM   2504  C CA  . SER A 1 389 ? -13.969 11.324  -26.055 1.00 61.36  ? 398  SER A CA  1 
ATOM   2505  C C   . SER A 1 389 ? -15.041 11.884  -26.963 1.00 62.89  ? 398  SER A C   1 
ATOM   2506  O O   . SER A 1 389 ? -14.944 13.014  -27.442 1.00 62.26  ? 398  SER A O   1 
ATOM   2507  C CB  . SER A 1 389 ? -14.259 11.860  -24.669 1.00 60.27  ? 398  SER A CB  1 
ATOM   2508  O OG  . SER A 1 389 ? -15.646 11.717  -24.395 1.00 61.98  ? 398  SER A OG  1 
ATOM   2509  N N   . LYS A 1 390 ? -16.091 11.101  -27.148 1.00 65.09  ? 399  LYS A N   1 
ATOM   2510  C CA  . LYS A 1 390 ? -17.231 11.544  -27.927 1.00 66.92  ? 399  LYS A CA  1 
ATOM   2511  C C   . LYS A 1 390 ? -18.085 12.563  -27.123 1.00 66.36  ? 399  LYS A C   1 
ATOM   2512  O O   . LYS A 1 390 ? -18.636 13.536  -27.645 1.00 66.41  ? 399  LYS A O   1 
ATOM   2513  C CB  . LYS A 1 390 ? -18.059 10.308  -28.346 1.00 70.13  ? 399  LYS A CB  1 
ATOM   2514  C CG  . LYS A 1 390 ? -17.688 9.637   -29.687 1.00 71.58  ? 399  LYS A CG  1 
ATOM   2515  C CD  . LYS A 1 390 ? -18.526 10.236  -30.786 1.00 75.67  ? 399  LYS A CD  1 
ATOM   2516  C CE  . LYS A 1 390 ? -18.487 9.418   -32.067 1.00 78.99  ? 399  LYS A CE  1 
ATOM   2517  N NZ  . LYS A 1 390 ? -19.387 10.007  -33.125 1.00 79.82  ? 399  LYS A NZ  1 
ATOM   2518  N N   . THR A 1 391 ? -18.166 12.337  -25.832 1.00 65.65  ? 400  THR A N   1 
ATOM   2519  C CA  . THR A 1 391 ? -19.052 13.097  -24.984 1.00 65.91  ? 400  THR A CA  1 
ATOM   2520  C C   . THR A 1 391 ? -18.291 14.119  -24.135 1.00 63.06  ? 400  THR A C   1 
ATOM   2521  O O   . THR A 1 391 ? -17.151 13.881  -23.749 1.00 61.03  ? 400  THR A O   1 
ATOM   2522  C CB  . THR A 1 391 ? -19.760 12.145  -24.005 1.00 67.60  ? 400  THR A CB  1 
ATOM   2523  O OG1 . THR A 1 391 ? -19.668 10.796  -24.494 1.00 69.62  ? 400  THR A OG1 1 
ATOM   2524  C CG2 . THR A 1 391 ? -21.222 12.560  -23.789 1.00 69.91  ? 400  THR A CG2 1 
ATOM   2525  N N   . ASP A 1 392 ? -18.952 15.233  -23.824 1.00 62.74  ? 401  ASP A N   1 
ATOM   2526  C CA  . ASP A 1 392 ? -18.435 16.259  -22.930 1.00 60.46  ? 401  ASP A CA  1 
ATOM   2527  C C   . ASP A 1 392 ? -18.035 15.672  -21.583 1.00 59.22  ? 401  ASP A C   1 
ATOM   2528  O O   . ASP A 1 392 ? -18.809 14.955  -20.967 1.00 60.84  ? 401  ASP A O   1 
ATOM   2529  C CB  . ASP A 1 392 ? -19.498 17.328  -22.688 1.00 61.63  ? 401  ASP A CB  1 
ATOM   2530  C CG  . ASP A 1 392 ? -19.573 18.339  -23.794 1.00 63.26  ? 401  ASP A CG  1 
ATOM   2531  O OD1 . ASP A 1 392 ? -19.283 17.973  -24.949 1.00 66.78  ? 401  ASP A OD1 1 
ATOM   2532  O OD2 . ASP A 1 392 ? -19.926 19.503  -23.517 1.00 64.05  ? 401  ASP A OD2 1 
ATOM   2533  N N   . VAL A 1 393 ? -16.821 15.985  -21.133 1.00 56.50  ? 402  VAL A N   1 
ATOM   2534  C CA  . VAL A 1 393 ? -16.321 15.612  -19.818 1.00 54.43  ? 402  VAL A CA  1 
ATOM   2535  C C   . VAL A 1 393 ? -15.825 16.925  -19.229 1.00 52.11  ? 402  VAL A C   1 
ATOM   2536  O O   . VAL A 1 393 ? -15.226 17.706  -19.939 1.00 51.31  ? 402  VAL A O   1 
ATOM   2537  C CB  . VAL A 1 393 ? -15.150 14.645  -19.938 1.00 53.35  ? 402  VAL A CB  1 
ATOM   2538  C CG1 . VAL A 1 393 ? -14.587 14.357  -18.585 1.00 53.01  ? 402  VAL A CG1 1 
ATOM   2539  C CG2 . VAL A 1 393 ? -15.580 13.357  -20.575 1.00 55.52  ? 402  VAL A CG2 1 
ATOM   2540  N N   . SER A 1 394 ? -16.091 17.184  -17.956 1.00 50.98  ? 403  SER A N   1 
ATOM   2541  C CA  . SER A 1 394 ? -15.631 18.407  -17.319 1.00 48.86  ? 403  SER A CA  1 
ATOM   2542  C C   . SER A 1 394 ? -14.845 17.987  -16.127 1.00 46.82  ? 403  SER A C   1 
ATOM   2543  O O   . SER A 1 394 ? -15.205 17.039  -15.477 1.00 47.49  ? 403  SER A O   1 
ATOM   2544  C CB  . SER A 1 394 ? -16.792 19.258  -16.833 1.00 50.06  ? 403  SER A CB  1 
ATOM   2545  O OG  . SER A 1 394 ? -17.984 18.942  -17.531 1.00 53.60  ? 403  SER A OG  1 
ATOM   2546  N N   . SER A 1 395 ? -13.752 18.674  -15.846 1.00 44.55  ? 404  SER A N   1 
ATOM   2547  C CA  . SER A 1 395 ? -13.079 18.524  -14.547 1.00 43.11  ? 404  SER A CA  1 
ATOM   2548  C C   . SER A 1 395 ? -11.944 19.528  -14.292 1.00 40.70  ? 404  SER A C   1 
ATOM   2549  O O   . SER A 1 395 ? -11.812 20.516  -15.004 1.00 40.59  ? 404  SER A O   1 
ATOM   2550  C CB  . SER A 1 395 ? -12.592 17.098  -14.319 1.00 42.91  ? 404  SER A CB  1 
ATOM   2551  O OG  . SER A 1 395 ? -11.183 17.071  -14.341 1.00 42.03  ? 404  SER A OG  1 
ATOM   2552  N N   . SER A 1 396 ? -11.162 19.290  -13.252 1.00 38.79  ? 405  SER A N   1 
ATOM   2553  C CA  . SER A 1 396 ? -10.066 20.186  -12.911 1.00 37.09  ? 405  SER A CA  1 
ATOM   2554  C C   . SER A 1 396 ? -8.742  19.500  -12.524 1.00 35.76  ? 405  SER A C   1 
ATOM   2555  O O   . SER A 1 396 ? -8.706  18.331  -12.086 1.00 35.91  ? 405  SER A O   1 
ATOM   2556  C CB  . SER A 1 396 ? -10.481 21.159  -11.836 1.00 36.93  ? 405  SER A CB  1 
ATOM   2557  O OG  . SER A 1 396 ? -9.347  21.737  -11.261 1.00 34.37  ? 405  SER A OG  1 
ATOM   2558  N N   . VAL A 1 397 ? -7.659  20.250  -12.709 1.00 34.30  ? 406  VAL A N   1 
ATOM   2559  C CA  . VAL A 1 397 ? -6.321  19.704  -12.643 1.00 33.57  ? 406  VAL A CA  1 
ATOM   2560  C C   . VAL A 1 397 ? -5.428  20.693  -11.957 1.00 32.37  ? 406  VAL A C   1 
ATOM   2561  O O   . VAL A 1 397 ? -5.240  21.785  -12.468 1.00 32.60  ? 406  VAL A O   1 
ATOM   2562  C CB  . VAL A 1 397 ? -5.707  19.557  -14.041 1.00 33.51  ? 406  VAL A CB  1 
ATOM   2563  C CG1 . VAL A 1 397 ? -4.468  18.725  -13.975 1.00 33.86  ? 406  VAL A CG1 1 
ATOM   2564  C CG2 . VAL A 1 397 ? -6.652  18.914  -14.962 1.00 35.90  ? 406  VAL A CG2 1 
ATOM   2565  N N   . ILE A 1 398 ? -4.831  20.322  -10.835 1.00 31.56  ? 407  ILE A N   1 
ATOM   2566  C CA  . ILE A 1 398 ? -4.034  21.299  -10.115 1.00 30.60  ? 407  ILE A CA  1 
ATOM   2567  C C   . ILE A 1 398 ? -2.569  21.351  -10.491 1.00 30.24  ? 407  ILE A C   1 
ATOM   2568  O O   . ILE A 1 398 ? -1.857  20.338  -10.506 1.00 30.31  ? 407  ILE A O   1 
ATOM   2569  C CB  . ILE A 1 398 ? -4.115  21.081  -8.667  1.00 29.77  ? 407  ILE A CB  1 
ATOM   2570  C CG1 . ILE A 1 398 ? -5.492  21.448  -8.213  1.00 30.21  ? 407  ILE A CG1 1 
ATOM   2571  C CG2 . ILE A 1 398 ? -3.154  21.977  -8.014  1.00 28.23  ? 407  ILE A CG2 1 
ATOM   2572  C CD1 . ILE A 1 398 ? -5.611  21.263  -6.785  1.00 31.90  ? 407  ILE A CD1 1 
ATOM   2573  N N   . THR A 1 399 ? -2.103  22.558  -10.750 1.00 30.42  ? 408  THR A N   1 
ATOM   2574  C CA  . THR A 1 399 ? -0.732  22.726  -11.198 1.00 30.36  ? 408  THR A CA  1 
ATOM   2575  C C   . THR A 1 399 ? 0.217   23.251  -10.133 1.00 29.74  ? 408  THR A C   1 
ATOM   2576  O O   . THR A 1 399 ? -0.165  23.508  -8.983  1.00 30.15  ? 408  THR A O   1 
ATOM   2577  C CB  . THR A 1 399 ? -0.682  23.680  -12.352 1.00 30.74  ? 408  THR A CB  1 
ATOM   2578  O OG1 . THR A 1 399 ? -1.266  24.918  -11.951 1.00 31.57  ? 408  THR A OG1 1 
ATOM   2579  C CG2 . THR A 1 399 ? -1.454  23.133  -13.488 1.00 31.69  ? 408  THR A CG2 1 
ATOM   2580  N N   . SER A 1 400 ? 1.464   23.428  -10.526 1.00 29.46  ? 409  SER A N   1 
ATOM   2581  C CA  . SER A 1 400 ? 2.490   23.792  -9.590  1.00 29.06  ? 409  SER A CA  1 
ATOM   2582  C C   . SER A 1 400 ? 2.185   25.132  -9.040  1.00 29.01  ? 409  SER A C   1 
ATOM   2583  O O   . SER A 1 400 ? 2.467   25.409  -7.891  1.00 28.79  ? 409  SER A O   1 
ATOM   2584  C CB  . SER A 1 400 ? 3.821   23.854  -10.291 1.00 29.16  ? 409  SER A CB  1 
ATOM   2585  O OG  . SER A 1 400 ? 4.096   22.636  -10.986 1.00 30.63  ? 409  SER A OG  1 
ATOM   2586  N N   . LEU A 1 401 ? 1.551   25.946  -9.859  1.00 29.56  ? 410  LEU A N   1 
ATOM   2587  C CA  . LEU A 1 401 ? 1.553   27.356  -9.597  1.00 30.00  ? 410  LEU A CA  1 
ATOM   2588  C C   . LEU A 1 401 ? 0.185   27.992  -9.771  1.00 30.68  ? 410  LEU A C   1 
ATOM   2589  O O   . LEU A 1 401 ? 0.017   29.198  -9.617  1.00 31.11  ? 410  LEU A O   1 
ATOM   2590  C CB  . LEU A 1 401 ? 2.585   27.981  -10.523 1.00 30.24  ? 410  LEU A CB  1 
ATOM   2591  C CG  . LEU A 1 401 ? 3.634   28.826  -9.854  1.00 29.77  ? 410  LEU A CG  1 
ATOM   2592  C CD1 . LEU A 1 401 ? 4.359   28.012  -8.837  1.00 30.51  ? 410  LEU A CD1 1 
ATOM   2593  C CD2 . LEU A 1 401 ? 4.548   29.274  -10.879 1.00 29.34  ? 410  LEU A CD2 1 
ATOM   2594  N N   . GLY A 1 402 ? -0.780  27.143  -10.108 1.00 30.91  ? 411  GLY A N   1 
ATOM   2595  C CA  . GLY A 1 402 ? -2.216  27.463  -10.090 1.00 31.16  ? 411  GLY A CA  1 
ATOM   2596  C C   . GLY A 1 402 ? -3.047  26.217  -10.394 1.00 30.95  ? 411  GLY A C   1 
ATOM   2597  O O   . GLY A 1 402 ? -2.760  25.129  -9.906  1.00 30.31  ? 411  GLY A O   1 
ATOM   2598  N N   . ALA A 1 403 ? -4.070  26.364  -11.224 1.00 31.31  ? 412  ALA A N   1 
ATOM   2599  C CA  . ALA A 1 403 ? -4.907  25.259  -11.550 1.00 31.12  ? 412  ALA A CA  1 
ATOM   2600  C C   . ALA A 1 403 ? -5.567  25.527  -12.858 1.00 32.13  ? 412  ALA A C   1 
ATOM   2601  O O   . ALA A 1 403 ? -5.768  26.672  -13.224 1.00 32.55  ? 412  ALA A O   1 
ATOM   2602  C CB  . ALA A 1 403 ? -5.919  25.085  -10.511 1.00 31.37  ? 412  ALA A CB  1 
ATOM   2603  N N   . ILE A 1 404 ? -5.894  24.444  -13.555 1.00 32.73  ? 413  ILE A N   1 
ATOM   2604  C CA  . ILE A 1 404 ? -6.704  24.454  -14.760 1.00 34.00  ? 413  ILE A CA  1 
ATOM   2605  C C   . ILE A 1 404 ? -8.098  23.933  -14.474 1.00 35.64  ? 413  ILE A C   1 
ATOM   2606  O O   . ILE A 1 404 ? -8.296  23.079  -13.575 1.00 35.46  ? 413  ILE A O   1 
ATOM   2607  C CB  . ILE A 1 404 ? -6.129  23.518  -15.795 1.00 33.87  ? 413  ILE A CB  1 
ATOM   2608  C CG1 . ILE A 1 404 ? -4.704  23.919  -16.114 1.00 32.43  ? 413  ILE A CG1 1 
ATOM   2609  C CG2 . ILE A 1 404 ? -7.020  23.499  -17.054 1.00 35.13  ? 413  ILE A CG2 1 
ATOM   2610  C CD1 . ILE A 1 404 ? -4.126  23.239  -17.311 1.00 33.37  ? 413  ILE A CD1 1 
ATOM   2611  N N   . VAL A 1 405 ? -9.063  24.436  -15.245 1.00 37.36  ? 414  VAL A N   1 
ATOM   2612  C CA  . VAL A 1 405 ? -10.451 23.999  -15.103 1.00 39.44  ? 414  VAL A CA  1 
ATOM   2613  C C   . VAL A 1 405 ? -11.189 23.919  -16.443 1.00 41.08  ? 414  VAL A C   1 
ATOM   2614  O O   . VAL A 1 405 ? -11.235 24.883  -17.206 1.00 41.72  ? 414  VAL A O   1 
ATOM   2615  C CB  . VAL A 1 405 ? -11.211 24.820  -14.059 1.00 39.77  ? 414  VAL A CB  1 
ATOM   2616  C CG1 . VAL A 1 405 ? -10.868 26.259  -14.167 1.00 39.98  ? 414  VAL A CG1 1 
ATOM   2617  C CG2 . VAL A 1 405 ? -12.650 24.648  -14.255 1.00 41.89  ? 414  VAL A CG2 1 
ATOM   2618  N N   . SER A 1 406 ? -11.729 22.738  -16.719 1.00 41.97  ? 415  SER A N   1 
ATOM   2619  C CA  . SER A 1 406 ? -12.385 22.467  -17.947 1.00 43.59  ? 415  SER A CA  1 
ATOM   2620  C C   . SER A 1 406 ? -13.824 22.285  -17.574 1.00 45.86  ? 415  SER A C   1 
ATOM   2621  O O   . SER A 1 406 ? -14.190 21.245  -17.029 1.00 46.62  ? 415  SER A O   1 
ATOM   2622  C CB  . SER A 1 406 ? -11.862 21.171  -18.531 1.00 43.45  ? 415  SER A CB  1 
ATOM   2623  O OG  . SER A 1 406 ? -10.483 21.220  -18.848 1.00 42.34  ? 415  SER A OG  1 
ATOM   2624  N N   . CYS A 1 407 ? -14.640 23.305  -17.855 1.00 47.46  ? 416  CYS A N   1 
ATOM   2625  C CA  . CYS A 1 407 ? -16.056 23.330  -17.494 1.00 49.40  ? 416  CYS A CA  1 
ATOM   2626  C C   . CYS A 1 407 ? -16.880 23.213  -18.733 1.00 51.12  ? 416  CYS A C   1 
ATOM   2627  O O   . CYS A 1 407 ? -16.941 24.129  -19.537 1.00 51.77  ? 416  CYS A O   1 
ATOM   2628  C CB  . CYS A 1 407 ? -16.390 24.638  -16.841 1.00 49.65  ? 416  CYS A CB  1 
ATOM   2629  S SG  . CYS A 1 407 ? -17.674 24.483  -15.716 1.00 52.75  ? 416  CYS A SG  1 
ATOM   2630  N N   . TYR A 1 408 ? -17.520 22.070  -18.888 1.00 52.33  ? 417  TYR A N   1 
ATOM   2631  C CA  . TYR A 1 408 ? -18.205 21.753  -20.126 1.00 53.71  ? 417  TYR A CA  1 
ATOM   2632  C C   . TYR A 1 408 ? -19.629 21.188  -19.926 1.00 55.91  ? 417  TYR A C   1 
ATOM   2633  O O   . TYR A 1 408 ? -19.990 20.738  -18.849 1.00 56.05  ? 417  TYR A O   1 
ATOM   2634  C CB  . TYR A 1 408 ? -17.322 20.813  -20.953 1.00 52.75  ? 417  TYR A CB  1 
ATOM   2635  C CG  . TYR A 1 408 ? -16.132 21.478  -21.623 1.00 50.96  ? 417  TYR A CG  1 
ATOM   2636  C CD1 . TYR A 1 408 ? -14.905 20.899  -21.590 1.00 49.60  ? 417  TYR A CD1 1 
ATOM   2637  C CD2 . TYR A 1 408 ? -16.252 22.677  -22.300 1.00 51.95  ? 417  TYR A CD2 1 
ATOM   2638  C CE1 . TYR A 1 408 ? -13.819 21.492  -22.211 1.00 49.14  ? 417  TYR A CE1 1 
ATOM   2639  C CE2 . TYR A 1 408 ? -15.183 23.263  -22.934 1.00 50.92  ? 417  TYR A CE2 1 
ATOM   2640  C CZ  . TYR A 1 408 ? -13.968 22.672  -22.888 1.00 49.71  ? 417  TYR A CZ  1 
ATOM   2641  O OH  . TYR A 1 408 ? -12.872 23.259  -23.506 1.00 49.70  ? 417  TYR A OH  1 
ATOM   2642  N N   . GLY A 1 409 ? -20.427 21.216  -20.988 1.00 57.85  ? 418  GLY A N   1 
ATOM   2643  C CA  . GLY A 1 409 ? -21.815 20.748  -20.951 1.00 60.46  ? 418  GLY A CA  1 
ATOM   2644  C C   . GLY A 1 409 ? -22.633 21.477  -19.917 1.00 61.46  ? 418  GLY A C   1 
ATOM   2645  O O   . GLY A 1 409 ? -22.607 22.690  -19.812 1.00 61.29  ? 418  GLY A O   1 
ATOM   2646  N N   . LYS A 1 410 ? -23.342 20.718  -19.121 1.00 62.69  ? 419  LYS A N   1 
ATOM   2647  C CA  . LYS A 1 410 ? -24.166 21.298  -18.124 1.00 64.08  ? 419  LYS A CA  1 
ATOM   2648  C C   . LYS A 1 410 ? -23.454 21.727  -16.835 1.00 62.11  ? 419  LYS A C   1 
ATOM   2649  O O   . LYS A 1 410 ? -24.055 22.370  -15.995 1.00 62.92  ? 419  LYS A O   1 
ATOM   2650  C CB  . LYS A 1 410 ? -25.217 20.274  -17.789 1.00 66.87  ? 419  LYS A CB  1 
ATOM   2651  C CG  . LYS A 1 410 ? -26.460 20.338  -18.669 1.00 71.49  ? 419  LYS A CG  1 
ATOM   2652  C CD  . LYS A 1 410 ? -27.683 19.827  -17.854 1.00 77.18  ? 419  LYS A CD  1 
ATOM   2653  C CE  . LYS A 1 410 ? -29.036 20.245  -18.432 1.00 81.44  ? 419  LYS A CE  1 
ATOM   2654  N NZ  . LYS A 1 410 ? -29.058 19.877  -19.871 1.00 84.14  ? 419  LYS A NZ  1 
ATOM   2655  N N   . THR A 1 411 ? -22.183 21.384  -16.658 1.00 59.67  ? 420  THR A N   1 
ATOM   2656  C CA  . THR A 1 411 ? -21.540 21.514  -15.332 1.00 57.84  ? 420  THR A CA  1 
ATOM   2657  C C   . THR A 1 411 ? -21.243 22.963  -14.895 1.00 57.24  ? 420  THR A C   1 
ATOM   2658  O O   . THR A 1 411 ? -21.020 23.813  -15.736 1.00 57.29  ? 420  THR A O   1 
ATOM   2659  C CB  . THR A 1 411 ? -20.327 20.548  -15.174 1.00 55.56  ? 420  THR A CB  1 
ATOM   2660  O OG1 . THR A 1 411 ? -19.963 20.041  -16.453 1.00 55.05  ? 420  THR A OG1 1 
ATOM   2661  C CG2 . THR A 1 411 ? -20.729 19.339  -14.343 1.00 55.95  ? 420  THR A CG2 1 
ATOM   2662  N N   . LYS A 1 412 ? -21.323 23.249  -13.589 1.00 57.14  ? 421  LYS A N   1 
ATOM   2663  C CA  . LYS A 1 412 ? -20.999 24.573  -13.014 1.00 56.64  ? 421  LYS A CA  1 
ATOM   2664  C C   . LYS A 1 412 ? -19.640 24.606  -12.324 1.00 54.10  ? 421  LYS A C   1 
ATOM   2665  O O   . LYS A 1 412 ? -19.357 23.735  -11.491 1.00 53.67  ? 421  LYS A O   1 
ATOM   2666  C CB  . LYS A 1 412 ? -22.011 24.949  -11.966 1.00 58.23  ? 421  LYS A CB  1 
ATOM   2667  C CG  . LYS A 1 412 ? -23.031 25.893  -12.488 1.00 62.89  ? 421  LYS A CG  1 
ATOM   2668  C CD  . LYS A 1 412 ? -24.254 25.992  -11.526 1.00 68.30  ? 421  LYS A CD  1 
ATOM   2669  C CE  . LYS A 1 412 ? -25.589 26.187  -12.280 1.00 70.77  ? 421  LYS A CE  1 
ATOM   2670  N NZ  . LYS A 1 412 ? -26.642 25.942  -11.283 1.00 73.93  ? 421  LYS A NZ  1 
ATOM   2671  N N   . CYS A 1 413 ? -18.819 25.619  -12.626 1.00 52.54  ? 422  CYS A N   1 
ATOM   2672  C CA  . CYS A 1 413 ? -17.484 25.740  -12.036 1.00 49.82  ? 422  CYS A CA  1 
ATOM   2673  C C   . CYS A 1 413 ? -17.208 27.117  -11.457 1.00 49.25  ? 422  CYS A C   1 
ATOM   2674  O O   . CYS A 1 413 ? -17.681 28.133  -11.958 1.00 50.51  ? 422  CYS A O   1 
ATOM   2675  C CB  . CYS A 1 413 ? -16.439 25.382  -13.049 1.00 48.47  ? 422  CYS A CB  1 
ATOM   2676  S SG  . CYS A 1 413 ? -16.818 23.892  -13.920 1.00 51.18  ? 422  CYS A SG  1 
ATOM   2677  N N   . THR A 1 414 ? -16.414 27.133  -10.395 1.00 47.60  ? 423  THR A N   1 
ATOM   2678  C CA  . THR A 1 414 ? -16.299 28.278  -9.520  1.00 47.38  ? 423  THR A CA  1 
ATOM   2679  C C   . THR A 1 414 ? -14.902 28.375  -8.983  1.00 45.64  ? 423  THR A C   1 
ATOM   2680  O O   . THR A 1 414 ? -14.362 27.397  -8.452  1.00 45.09  ? 423  THR A O   1 
ATOM   2681  C CB  . THR A 1 414 ? -17.087 27.994  -8.306  1.00 47.94  ? 423  THR A CB  1 
ATOM   2682  O OG1 . THR A 1 414 ? -18.429 27.862  -8.680  1.00 50.10  ? 423  THR A OG1 1 
ATOM   2683  C CG2 . THR A 1 414 ? -17.009 29.093  -7.358  1.00 48.71  ? 423  THR A CG2 1 
ATOM   2684  N N   . ALA A 1 415 ? -14.311 29.553  -9.065  1.00 45.16  ? 424  ALA A N   1 
ATOM   2685  C CA  . ALA A 1 415 ? -13.079 29.764  -8.353  1.00 43.13  ? 424  ALA A CA  1 
ATOM   2686  C C   . ALA A 1 415 ? -13.358 30.672  -7.198  1.00 43.78  ? 424  ALA A C   1 
ATOM   2687  O O   . ALA A 1 415 ? -13.883 31.757  -7.390  1.00 45.54  ? 424  ALA A O   1 
ATOM   2688  C CB  . ALA A 1 415 ? -12.140 30.390  -9.222  1.00 42.35  ? 424  ALA A CB  1 
ATOM   2689  N N   . SER A 1 416 ? -12.995 30.249  -6.005  1.00 42.85  ? 425  SER A N   1 
ATOM   2690  C CA  . SER A 1 416 ? -13.179 31.090  -4.845  1.00 43.60  ? 425  SER A CA  1 
ATOM   2691  C C   . SER A 1 416 ? -11.834 31.477  -4.225  1.00 42.27  ? 425  SER A C   1 
ATOM   2692  O O   . SER A 1 416 ? -10.846 30.802  -4.416  1.00 40.30  ? 425  SER A O   1 
ATOM   2693  C CB  . SER A 1 416 ? -14.081 30.370  -3.860  1.00 44.47  ? 425  SER A CB  1 
ATOM   2694  O OG  . SER A 1 416 ? -14.884 29.430  -4.566  1.00 44.86  ? 425  SER A OG  1 
ATOM   2695  N N   . ASN A 1 417 ? -11.800 32.591  -3.509  1.00 43.60  ? 426  ASN A N   1 
ATOM   2696  C CA  . ASN A 1 417 ? -10.561 33.123  -2.972  1.00 43.13  ? 426  ASN A CA  1 
ATOM   2697  C C   . ASN A 1 417 ? -10.222 32.530  -1.628  1.00 43.47  ? 426  ASN A C   1 
ATOM   2698  O O   . ASN A 1 417 ? -10.875 31.593  -1.158  1.00 43.57  ? 426  ASN A O   1 
ATOM   2699  C CB  . ASN A 1 417 ? -10.582 34.664  -2.896  1.00 43.91  ? 426  ASN A CB  1 
ATOM   2700  C CG  . ASN A 1 417 ? -11.302 35.191  -1.687  1.00 44.74  ? 426  ASN A CG  1 
ATOM   2701  O OD1 . ASN A 1 417 ? -11.496 34.481  -0.718  1.00 43.39  ? 426  ASN A OD1 1 
ATOM   2702  N ND2 . ASN A 1 417 ? -11.691 36.449  -1.730  1.00 46.12  ? 426  ASN A ND2 1 
ATOM   2703  N N   . LYS A 1 418 ? -9.160  33.087  -1.044  1.00 44.34  ? 427  LYS A N   1 
ATOM   2704  C CA  . LYS A 1 418 ? -8.682  32.836  0.321   1.00 44.74  ? 427  LYS A CA  1 
ATOM   2705  C C   . LYS A 1 418 ? -9.767  32.514  1.331   1.00 45.73  ? 427  LYS A C   1 
ATOM   2706  O O   . LYS A 1 418 ? -9.704  31.469  1.955   1.00 44.46  ? 427  LYS A O   1 
ATOM   2707  C CB  . LYS A 1 418 ? -7.926  34.072  0.806   1.00 45.63  ? 427  LYS A CB  1 
ATOM   2708  C CG  . LYS A 1 418 ? -6.434  34.015  0.833   1.00 46.46  ? 427  LYS A CG  1 
ATOM   2709  C CD  . LYS A 1 418 ? -5.881  34.995  1.907   1.00 49.25  ? 427  LYS A CD  1 
ATOM   2710  C CE  . LYS A 1 418 ? -4.381  34.813  2.156   1.00 49.44  ? 427  LYS A CE  1 
ATOM   2711  N NZ  . LYS A 1 418 ? -3.937  33.383  2.461   1.00 49.09  ? 427  LYS A NZ  1 
ATOM   2712  N N   . ASN A 1 419 ? -10.720 33.443  1.490   1.00 48.10  ? 428  ASN A N   1 
ATOM   2713  C CA  . ASN A 1 419 ? -11.856 33.346  2.415   1.00 49.84  ? 428  ASN A CA  1 
ATOM   2714  C C   . ASN A 1 419 ? -13.188 32.735  1.847   1.00 51.33  ? 428  ASN A C   1 
ATOM   2715  O O   . ASN A 1 419 ? -14.194 32.678  2.516   1.00 53.08  ? 428  ASN A O   1 
ATOM   2716  C CB  . ASN A 1 419 ? -12.106 34.695  3.108   1.00 51.19  ? 428  ASN A CB  1 
ATOM   2717  C CG  . ASN A 1 419 ? -11.403 35.841  2.440   1.00 49.80  ? 428  ASN A CG  1 
ATOM   2718  O OD1 . ASN A 1 419 ? -10.312 36.163  2.828   1.00 45.15  ? 428  ASN A OD1 1 
ATOM   2719  N ND2 . ASN A 1 419 ? -12.061 36.504  1.466   1.00 50.97  ? 428  ASN A ND2 1 
ATOM   2720  N N   . ARG A 1 420 ? -13.172 32.255  0.625   1.00 50.80  ? 429  ARG A N   1 
ATOM   2721  C CA  . ARG A 1 420 ? -14.270 31.490  0.089   1.00 51.75  ? 429  ARG A CA  1 
ATOM   2722  C C   . ARG A 1 420 ? -15.278 32.308  -0.661  1.00 53.57  ? 429  ARG A C   1 
ATOM   2723  O O   . ARG A 1 420 ? -16.135 31.748  -1.327  1.00 55.00  ? 429  ARG A O   1 
ATOM   2724  C CB  . ARG A 1 420 ? -14.953 30.676  1.152   1.00 52.45  ? 429  ARG A CB  1 
ATOM   2725  C CG  . ARG A 1 420 ? -14.126 29.564  1.666   1.00 51.69  ? 429  ARG A CG  1 
ATOM   2726  C CD  . ARG A 1 420 ? -14.573 28.196  1.158   1.00 55.52  ? 429  ARG A CD  1 
ATOM   2727  N NE  . ARG A 1 420 ? -13.568 27.165  1.454   1.00 57.49  ? 429  ARG A NE  1 
ATOM   2728  C CZ  . ARG A 1 420 ? -13.322 26.613  2.655   1.00 58.50  ? 429  ARG A CZ  1 
ATOM   2729  N NH1 . ARG A 1 420 ? -14.018 26.970  3.748   1.00 59.26  ? 429  ARG A NH1 1 
ATOM   2730  N NH2 . ARG A 1 420 ? -12.350 25.693  2.768   1.00 57.13  ? 429  ARG A NH2 1 
ATOM   2731  N N   . GLY A 1 421 ? -15.184 33.624  -0.564  1.00 53.78  ? 430  GLY A N   1 
ATOM   2732  C CA  . GLY A 1 421 ? -15.815 34.490  -1.563  1.00 54.51  ? 430  GLY A CA  1 
ATOM   2733  C C   . GLY A 1 421 ? -15.506 34.038  -2.996  1.00 53.00  ? 430  GLY A C   1 
ATOM   2734  O O   . GLY A 1 421 ? -14.384 33.740  -3.327  1.00 51.30  ? 430  GLY A O   1 
ATOM   2735  N N   . ILE A 1 422 ? -16.515 33.989  -3.852  1.00 53.83  ? 431  ILE A N   1 
ATOM   2736  C CA  . ILE A 1 422 ? -16.389 33.439  -5.178  1.00 52.30  ? 431  ILE A CA  1 
ATOM   2737  C C   . ILE A 1 422 ? -15.932 34.539  -6.090  1.00 52.28  ? 431  ILE A C   1 
ATOM   2738  O O   . ILE A 1 422 ? -16.551 35.570  -6.110  1.00 53.72  ? 431  ILE A O   1 
ATOM   2739  C CB  . ILE A 1 422 ? -17.753 32.942  -5.634  1.00 53.94  ? 431  ILE A CB  1 
ATOM   2740  C CG1 . ILE A 1 422 ? -18.116 31.641  -4.922  1.00 54.26  ? 431  ILE A CG1 1 
ATOM   2741  C CG2 . ILE A 1 422 ? -17.769 32.691  -7.084  1.00 53.52  ? 431  ILE A CG2 1 
ATOM   2742  C CD1 . ILE A 1 422 ? -19.210 31.799  -3.832  1.00 57.66  ? 431  ILE A CD1 1 
ATOM   2743  N N   . ILE A 1 423 ? -14.845 34.341  -6.833  1.00 50.85  ? 432  ILE A N   1 
ATOM   2744  C CA  . ILE A 1 423 ? -14.364 35.402  -7.716  1.00 51.62  ? 432  ILE A CA  1 
ATOM   2745  C C   . ILE A 1 423 ? -14.689 35.194  -9.130  1.00 52.08  ? 432  ILE A C   1 
ATOM   2746  O O   . ILE A 1 423 ? -15.021 36.139  -9.802  1.00 53.82  ? 432  ILE A O   1 
ATOM   2747  C CB  . ILE A 1 423 ? -12.867 35.573  -7.815  1.00 49.77  ? 432  ILE A CB  1 
ATOM   2748  C CG1 . ILE A 1 423 ? -12.160 35.086  -6.583  1.00 49.05  ? 432  ILE A CG1 1 
ATOM   2749  C CG2 . ILE A 1 423 ? -12.528 37.045  -8.119  1.00 51.48  ? 432  ILE A CG2 1 
ATOM   2750  C CD1 . ILE A 1 423 ? -10.604 35.023  -6.807  1.00 48.64  ? 432  ILE A CD1 1 
ATOM   2751  N N   . LYS A 1 424 ? -14.504 33.988  -9.621  1.00 51.02  ? 433  LYS A N   1 
ATOM   2752  C CA  . LYS A 1 424 ? -14.771 33.760  -11.019 1.00 51.90  ? 433  LYS A CA  1 
ATOM   2753  C C   . LYS A 1 424 ? -15.830 32.690  -11.165 1.00 52.25  ? 433  LYS A C   1 
ATOM   2754  O O   . LYS A 1 424 ? -16.013 31.849  -10.272 1.00 51.68  ? 433  LYS A O   1 
ATOM   2755  C CB  . LYS A 1 424 ? -13.469 33.383  -11.743 1.00 50.50  ? 433  LYS A CB  1 
ATOM   2756  C CG  . LYS A 1 424 ? -13.600 33.328  -13.292 1.00 53.24  ? 433  LYS A CG  1 
ATOM   2757  C CD  . LYS A 1 424 ? -12.251 33.372  -14.090 1.00 54.34  ? 433  LYS A CD  1 
ATOM   2758  C CE  . LYS A 1 424 ? -12.543 33.240  -15.635 1.00 56.21  ? 433  LYS A CE  1 
ATOM   2759  N NZ  . LYS A 1 424 ? -11.779 34.169  -16.544 1.00 56.83  ? 433  LYS A NZ  1 
ATOM   2760  N N   . THR A 1 425 ? -16.535 32.716  -12.283 1.00 53.17  ? 434  THR A N   1 
ATOM   2761  C CA  . THR A 1 425 ? -17.467 31.641  -12.541 1.00 54.22  ? 434  THR A CA  1 
ATOM   2762  C C   . THR A 1 425 ? -17.427 31.273  -14.011 1.00 54.21  ? 434  THR A C   1 
ATOM   2763  O O   . THR A 1 425 ? -17.260 32.159  -14.831 1.00 54.84  ? 434  THR A O   1 
ATOM   2764  C CB  . THR A 1 425 ? -18.850 32.010  -12.027 1.00 56.60  ? 434  THR A CB  1 
ATOM   2765  O OG1 . THR A 1 425 ? -19.820 31.157  -12.627 1.00 57.99  ? 434  THR A OG1 1 
ATOM   2766  C CG2 . THR A 1 425 ? -19.173 33.467  -12.335 1.00 58.66  ? 434  THR A CG2 1 
ATOM   2767  N N   . PHE A 1 426 ? -17.563 29.983  -14.332 1.00 54.05  ? 435  PHE A N   1 
ATOM   2768  C CA  . PHE A 1 426 ? -16.936 29.447  -15.551 1.00 54.01  ? 435  PHE A CA  1 
ATOM   2769  C C   . PHE A 1 426 ? -17.701 29.258  -16.883 1.00 56.65  ? 435  PHE A C   1 
ATOM   2770  O O   . PHE A 1 426 ? -18.612 28.407  -17.055 1.00 57.86  ? 435  PHE A O   1 
ATOM   2771  C CB  . PHE A 1 426 ? -16.047 28.267  -15.241 1.00 51.95  ? 435  PHE A CB  1 
ATOM   2772  C CG  . PHE A 1 426 ? -14.725 28.664  -14.664 1.00 49.34  ? 435  PHE A CG  1 
ATOM   2773  C CD1 . PHE A 1 426 ? -14.363 28.268  -13.391 1.00 47.65  ? 435  PHE A CD1 1 
ATOM   2774  C CD2 . PHE A 1 426 ? -13.853 29.457  -15.367 1.00 48.28  ? 435  PHE A CD2 1 
ATOM   2775  C CE1 . PHE A 1 426 ? -13.146 28.641  -12.832 1.00 44.51  ? 435  PHE A CE1 1 
ATOM   2776  C CE2 . PHE A 1 426 ? -12.634 29.812  -14.808 1.00 46.21  ? 435  PHE A CE2 1 
ATOM   2777  C CZ  . PHE A 1 426 ? -12.294 29.408  -13.541 1.00 43.95  ? 435  PHE A CZ  1 
ATOM   2778  N N   . SER A 1 427 ? -17.237 30.025  -17.865 1.00 57.74  ? 436  SER A N   1 
ATOM   2779  C CA  . SER A 1 427 ? -17.910 30.169  -19.162 1.00 59.90  ? 436  SER A CA  1 
ATOM   2780  C C   . SER A 1 427 ? -17.701 28.943  -20.087 1.00 59.58  ? 436  SER A C   1 
ATOM   2781  O O   . SER A 1 427 ? -17.005 29.017  -21.154 1.00 58.85  ? 436  SER A O   1 
ATOM   2782  C CB  . SER A 1 427 ? -17.407 31.475  -19.835 1.00 60.40  ? 436  SER A CB  1 
ATOM   2783  O OG  . SER A 1 427 ? -18.235 31.879  -20.924 1.00 63.16  ? 436  SER A OG  1 
ATOM   2784  N N   . ASN A 1 428 ? -18.289 27.815  -19.675 1.00 59.75  ? 437  ASN A N   1 
ATOM   2785  C CA  . ASN A 1 428 ? -18.339 26.656  -20.556 1.00 59.88  ? 437  ASN A CA  1 
ATOM   2786  C C   . ASN A 1 428 ? -17.129 26.470  -21.519 1.00 57.61  ? 437  ASN A C   1 
ATOM   2787  O O   . ASN A 1 428 ? -17.316 26.373  -22.712 1.00 58.03  ? 437  ASN A O   1 
ATOM   2788  C CB  . ASN A 1 428 ? -19.631 26.773  -21.374 1.00 62.84  ? 437  ASN A CB  1 
ATOM   2789  C CG  . ASN A 1 428 ? -20.098 25.443  -21.942 1.00 64.58  ? 437  ASN A CG  1 
ATOM   2790  O OD1 . ASN A 1 428 ? -20.174 24.439  -21.221 1.00 66.31  ? 437  ASN A OD1 1 
ATOM   2791  N ND2 . ASN A 1 428 ? -20.430 25.432  -23.230 1.00 66.36  ? 437  ASN A ND2 1 
ATOM   2792  N N   . GLY A 1 429 ? -15.907 26.422  -20.986 1.00 55.35  ? 438  GLY A N   1 
ATOM   2793  C CA  . GLY A 1 429 ? -14.664 26.282  -21.777 1.00 53.44  ? 438  GLY A CA  1 
ATOM   2794  C C   . GLY A 1 429 ? -13.543 25.710  -20.918 1.00 51.35  ? 438  GLY A C   1 
ATOM   2795  O O   . GLY A 1 429 ? -13.791 24.792  -20.137 1.00 51.53  ? 438  GLY A O   1 
ATOM   2796  N N   . CYS A 1 430 ? -12.325 26.257  -21.033 1.00 49.43  ? 439  CYS A N   1 
ATOM   2797  C CA  . CYS A 1 430 ? -11.139 25.765  -20.293 1.00 46.78  ? 439  CYS A CA  1 
ATOM   2798  C C   . CYS A 1 430 ? -10.181 26.898  -19.937 1.00 45.19  ? 439  CYS A C   1 
ATOM   2799  O O   . CYS A 1 430 ? -9.550  27.481  -20.814 1.00 44.98  ? 439  CYS A O   1 
ATOM   2800  C CB  . CYS A 1 430 ? -10.437 24.658  -21.102 1.00 46.32  ? 439  CYS A CB  1 
ATOM   2801  S SG  . CYS A 1 430 ? -8.605  24.652  -21.138 1.00 45.63  ? 439  CYS A SG  1 
ATOM   2802  N N   . ASP A 1 431 ? -10.082 27.203  -18.647 1.00 43.99  ? 440  ASP A N   1 
ATOM   2803  C CA  . ASP A 1 431 ? -9.326  28.363  -18.160 1.00 42.89  ? 440  ASP A CA  1 
ATOM   2804  C C   . ASP A 1 431 ? -8.262  27.997  -17.141 1.00 40.24  ? 440  ASP A C   1 
ATOM   2805  O O   . ASP A 1 431 ? -8.274  26.880  -16.618 1.00 39.82  ? 440  ASP A O   1 
ATOM   2806  C CB  . ASP A 1 431 ? -10.298 29.327  -17.493 1.00 44.75  ? 440  ASP A CB  1 
ATOM   2807  C CG  . ASP A 1 431 ? -10.512 30.609  -18.295 1.00 48.45  ? 440  ASP A CG  1 
ATOM   2808  O OD1 . ASP A 1 431 ? -9.585  31.476  -18.254 1.00 49.92  ? 440  ASP A OD1 1 
ATOM   2809  O OD2 . ASP A 1 431 ? -11.607 30.754  -18.933 1.00 52.18  ? 440  ASP A OD2 1 
ATOM   2810  N N   . TYR A 1 432 ? -7.382  28.950  -16.821 1.00 38.27  ? 441  TYR A N   1 
ATOM   2811  C CA  . TYR A 1 432 ? -6.322  28.765  -15.827 1.00 35.77  ? 441  TYR A CA  1 
ATOM   2812  C C   . TYR A 1 432 ? -6.482  29.799  -14.753 1.00 35.40  ? 441  TYR A C   1 
ATOM   2813  O O   . TYR A 1 432 ? -6.907  30.868  -15.066 1.00 36.55  ? 441  TYR A O   1 
ATOM   2814  C CB  . TYR A 1 432 ? -4.985  28.987  -16.526 1.00 34.97  ? 441  TYR A CB  1 
ATOM   2815  C CG  . TYR A 1 432 ? -3.743  28.948  -15.654 1.00 33.39  ? 441  TYR A CG  1 
ATOM   2816  C CD1 . TYR A 1 432 ? -3.060  27.760  -15.412 1.00 32.87  ? 441  TYR A CD1 1 
ATOM   2817  C CD2 . TYR A 1 432 ? -3.232  30.092  -15.098 1.00 33.09  ? 441  TYR A CD2 1 
ATOM   2818  C CE1 . TYR A 1 432 ? -1.910  27.717  -14.608 1.00 31.21  ? 441  TYR A CE1 1 
ATOM   2819  C CE2 . TYR A 1 432 ? -2.091  30.053  -14.293 1.00 32.46  ? 441  TYR A CE2 1 
ATOM   2820  C CZ  . TYR A 1 432 ? -1.431  28.874  -14.060 1.00 31.05  ? 441  TYR A CZ  1 
ATOM   2821  O OH  . TYR A 1 432 ? -0.297  28.902  -13.273 1.00 29.12  ? 441  TYR A OH  1 
ATOM   2822  N N   . VAL A 1 433 ? -6.133  29.511  -13.503 1.00 34.40  ? 442  VAL A N   1 
ATOM   2823  C CA  . VAL A 1 433 ? -6.115  30.540  -12.424 1.00 34.68  ? 442  VAL A CA  1 
ATOM   2824  C C   . VAL A 1 433 ? -4.839  30.422  -11.623 1.00 33.69  ? 442  VAL A C   1 
ATOM   2825  O O   . VAL A 1 433 ? -4.131  29.464  -11.848 1.00 33.52  ? 442  VAL A O   1 
ATOM   2826  C CB  . VAL A 1 433 ? -7.253  30.330  -11.465 1.00 35.23  ? 442  VAL A CB  1 
ATOM   2827  C CG1 . VAL A 1 433 ? -8.527  30.801  -12.084 1.00 37.45  ? 442  VAL A CG1 1 
ATOM   2828  C CG2 . VAL A 1 433 ? -7.370  28.880  -11.084 1.00 34.20  ? 442  VAL A CG2 1 
ATOM   2829  N N   . SER A 1 434 ? -4.510  31.322  -10.690 1.00 33.79  ? 443  SER A N   1 
ATOM   2830  C CA  . SER A 1 434 ? -3.290  31.072  -9.866  1.00 32.80  ? 443  SER A CA  1 
ATOM   2831  C C   . SER A 1 434 ? -3.385  31.391  -8.390  1.00 33.32  ? 443  SER A C   1 
ATOM   2832  O O   . SER A 1 434 ? -4.350  31.982  -7.957  1.00 34.98  ? 443  SER A O   1 
ATOM   2833  C CB  . SER A 1 434 ? -2.110  31.810  -10.446 1.00 32.64  ? 443  SER A CB  1 
ATOM   2834  O OG  . SER A 1 434 ? -1.877  33.006  -9.749  1.00 32.56  ? 443  SER A OG  1 
ATOM   2835  N N   . ASN A 1 435 ? -2.375  31.032  -7.615  1.00 32.92  ? 444  ASN A N   1 
ATOM   2836  C CA  . ASN A 1 435 ? -2.377  31.292  -6.179  1.00 33.56  ? 444  ASN A CA  1 
ATOM   2837  C C   . ASN A 1 435 ? -2.208  32.766  -5.884  1.00 35.14  ? 444  ASN A C   1 
ATOM   2838  O O   . ASN A 1 435 ? -1.547  33.500  -6.624  1.00 34.85  ? 444  ASN A O   1 
ATOM   2839  C CB  . ASN A 1 435 ? -1.287  30.480  -5.501  1.00 32.45  ? 444  ASN A CB  1 
ATOM   2840  C CG  . ASN A 1 435 ? -0.760  29.378  -6.384  1.00 32.46  ? 444  ASN A CG  1 
ATOM   2841  O OD1 . ASN A 1 435 ? -1.468  28.923  -7.248  1.00 35.67  ? 444  ASN A OD1 1 
ATOM   2842  N ND2 . ASN A 1 435 ? 0.475   28.970  -6.198  1.00 31.93  ? 444  ASN A ND2 1 
ATOM   2843  N N   . LYS A 1 436 ? -2.747  33.173  -4.745  1.00 37.04  ? 445  LYS A N   1 
ATOM   2844  C CA  . LYS A 1 436 ? -3.324  34.523  -4.580  1.00 40.36  ? 445  LYS A CA  1 
ATOM   2845  C C   . LYS A 1 436 ? -4.138  34.869  -5.805  1.00 41.60  ? 445  LYS A C   1 
ATOM   2846  O O   . LYS A 1 436 ? -3.670  34.736  -6.916  1.00 41.65  ? 445  LYS A O   1 
ATOM   2847  C CB  . LYS A 1 436 ? -2.354  35.671  -4.222  1.00 41.34  ? 445  LYS A CB  1 
ATOM   2848  C CG  . LYS A 1 436 ? -3.040  37.113  -3.898  1.00 45.73  ? 445  LYS A CG  1 
ATOM   2849  C CD  . LYS A 1 436 ? -4.397  37.242  -2.965  1.00 50.01  ? 445  LYS A CD  1 
ATOM   2850  C CE  . LYS A 1 436 ? -4.905  36.002  -2.074  1.00 50.15  ? 445  LYS A CE  1 
ATOM   2851  N NZ  . LYS A 1 436 ? -3.801  35.215  -1.337  1.00 48.76  ? 445  LYS A NZ  1 
ATOM   2852  N N   . GLY A 1 437 ? -5.354  35.350  -5.574  1.00 43.13  ? 446  GLY A N   1 
ATOM   2853  C CA  . GLY A 1 437 ? -6.437  35.126  -6.502  1.00 43.40  ? 446  GLY A CA  1 
ATOM   2854  C C   . GLY A 1 437 ? -7.017  33.877  -5.896  1.00 42.09  ? 446  GLY A C   1 
ATOM   2855  O O   . GLY A 1 437 ? -7.655  33.952  -4.852  1.00 43.40  ? 446  GLY A O   1 
ATOM   2856  N N   . VAL A 1 438 ? -6.687  32.725  -6.461  1.00 39.71  ? 447  VAL A N   1 
ATOM   2857  C CA  . VAL A 1 438 ? -7.489  31.542  -6.232  1.00 38.91  ? 447  VAL A CA  1 
ATOM   2858  C C   . VAL A 1 438 ? -6.963  30.556  -5.220  1.00 37.09  ? 447  VAL A C   1 
ATOM   2859  O O   . VAL A 1 438 ? -5.804  30.294  -5.200  1.00 36.02  ? 447  VAL A O   1 
ATOM   2860  C CB  . VAL A 1 438 ? -7.734  30.827  -7.522  1.00 38.86  ? 447  VAL A CB  1 
ATOM   2861  C CG1 . VAL A 1 438 ? -8.878  29.886  -7.362  1.00 40.12  ? 447  VAL A CG1 1 
ATOM   2862  C CG2 . VAL A 1 438 ? -8.111  31.824  -8.556  1.00 40.56  ? 447  VAL A CG2 1 
ATOM   2863  N N   . ASP A 1 439 ? -7.860  29.992  -4.416  1.00 37.08  ? 448  ASP A N   1 
ATOM   2864  C CA  . ASP A 1 439 ? -7.556  29.104  -3.320  1.00 35.51  ? 448  ASP A CA  1 
ATOM   2865  C C   . ASP A 1 439 ? -8.310  27.796  -3.504  1.00 35.15  ? 448  ASP A C   1 
ATOM   2866  O O   . ASP A 1 439 ? -7.922  26.777  -2.984  1.00 34.00  ? 448  ASP A O   1 
ATOM   2867  C CB  . ASP A 1 439 ? -8.066  29.770  -2.066  1.00 36.74  ? 448  ASP A CB  1 
ATOM   2868  C CG  . ASP A 1 439 ? -7.299  29.373  -0.823  1.00 38.39  ? 448  ASP A CG  1 
ATOM   2869  O OD1 . ASP A 1 439 ? -6.870  28.217  -0.699  1.00 39.54  ? 448  ASP A OD1 1 
ATOM   2870  O OD2 . ASP A 1 439 ? -7.140  30.229  0.081   1.00 42.02  ? 448  ASP A OD2 1 
ATOM   2871  N N   . THR A 1 440 ? -9.403  27.847  -4.263  1.00 35.90  ? 449  THR A N   1 
ATOM   2872  C CA  . THR A 1 440 ? -10.368 26.776  -4.389  1.00 35.66  ? 449  THR A CA  1 
ATOM   2873  C C   . THR A 1 440 ? -11.000 26.852  -5.759  1.00 36.50  ? 449  THR A C   1 
ATOM   2874  O O   . THR A 1 440 ? -11.296 27.928  -6.262  1.00 37.69  ? 449  THR A O   1 
ATOM   2875  C CB  . THR A 1 440 ? -11.444 26.988  -3.349  1.00 37.00  ? 449  THR A CB  1 
ATOM   2876  O OG1 . THR A 1 440 ? -11.098 26.225  -2.217  1.00 35.28  ? 449  THR A OG1 1 
ATOM   2877  C CG2 . THR A 1 440 ? -12.888 26.610  -3.853  1.00 39.74  ? 449  THR A CG2 1 
ATOM   2878  N N   . VAL A 1 441 ? -11.197 25.714  -6.389  1.00 36.06  ? 450  VAL A N   1 
ATOM   2879  C CA  . VAL A 1 441 ? -12.164 25.665  -7.448  1.00 37.14  ? 450  VAL A CA  1 
ATOM   2880  C C   . VAL A 1 441 ? -13.095 24.505  -7.165  1.00 38.22  ? 450  VAL A C   1 
ATOM   2881  O O   . VAL A 1 441 ? -12.706 23.496  -6.581  1.00 37.49  ? 450  VAL A O   1 
ATOM   2882  C CB  . VAL A 1 441 ? -11.531 25.547  -8.817  1.00 36.27  ? 450  VAL A CB  1 
ATOM   2883  C CG1 . VAL A 1 441 ? -10.492 26.574  -8.979  1.00 34.54  ? 450  VAL A CG1 1 
ATOM   2884  C CG2 . VAL A 1 441 ? -10.931 24.184  -8.997  1.00 35.84  ? 450  VAL A CG2 1 
ATOM   2885  N N   . SER A 1 442 ? -14.344 24.667  -7.553  1.00 40.24  ? 451  SER A N   1 
ATOM   2886  C CA  . SER A 1 442 ? -15.276 23.576  -7.477  1.00 41.64  ? 451  SER A CA  1 
ATOM   2887  C C   . SER A 1 442 ? -15.744 23.325  -8.856  1.00 42.29  ? 451  SER A C   1 
ATOM   2888  O O   . SER A 1 442 ? -15.888 24.255  -9.651  1.00 42.68  ? 451  SER A O   1 
ATOM   2889  C CB  . SER A 1 442 ? -16.441 23.918  -6.586  1.00 43.48  ? 451  SER A CB  1 
ATOM   2890  O OG  . SER A 1 442 ? -16.458 25.306  -6.365  1.00 46.21  ? 451  SER A OG  1 
ATOM   2891  N N   . VAL A 1 443 ? -15.895 22.038  -9.145  1.00 42.71  ? 452  VAL A N   1 
ATOM   2892  C CA  . VAL A 1 443 ? -16.523 21.545  -10.363 1.00 43.68  ? 452  VAL A CA  1 
ATOM   2893  C C   . VAL A 1 443 ? -17.692 20.716  -9.853  1.00 45.68  ? 452  VAL A C   1 
ATOM   2894  O O   . VAL A 1 443 ? -17.501 19.745  -9.117  1.00 45.62  ? 452  VAL A O   1 
ATOM   2895  C CB  . VAL A 1 443 ? -15.595 20.682  -11.174 1.00 42.08  ? 452  VAL A CB  1 
ATOM   2896  C CG1 . VAL A 1 443 ? -16.238 20.343  -12.453 1.00 43.21  ? 452  VAL A CG1 1 
ATOM   2897  C CG2 . VAL A 1 443 ? -14.366 21.424  -11.434 1.00 40.13  ? 452  VAL A CG2 1 
ATOM   2898  N N   . GLY A 1 444 ? -18.902 21.153  -10.176 1.00 47.41  ? 453  GLY A N   1 
ATOM   2899  C CA  . GLY A 1 444 ? -20.072 20.471  -9.723  1.00 49.28  ? 453  GLY A CA  1 
ATOM   2900  C C   . GLY A 1 444 ? -19.897 20.318  -8.257  1.00 48.43  ? 453  GLY A C   1 
ATOM   2901  O O   . GLY A 1 444 ? -19.694 21.304  -7.570  1.00 47.67  ? 453  GLY A O   1 
ATOM   2902  N N   . ASN A 1 445 ? -19.928 19.081  -7.790  1.00 48.67  ? 454  ASN A N   1 
ATOM   2903  C CA  . ASN A 1 445 ? -19.910 18.870  -6.372  1.00 48.76  ? 454  ASN A CA  1 
ATOM   2904  C C   . ASN A 1 445 ? -18.604 18.562  -5.783  1.00 46.10  ? 454  ASN A C   1 
ATOM   2905  O O   . ASN A 1 445 ? -18.511 18.531  -4.563  1.00 46.04  ? 454  ASN A O   1 
ATOM   2906  C CB  . ASN A 1 445 ? -20.893 17.819  -5.949  1.00 51.30  ? 454  ASN A CB  1 
ATOM   2907  C CG  . ASN A 1 445 ? -22.168 18.429  -5.543  1.00 55.46  ? 454  ASN A CG  1 
ATOM   2908  O OD1 . ASN A 1 445 ? -22.449 18.538  -4.350  1.00 58.63  ? 454  ASN A OD1 1 
ATOM   2909  N ND2 . ASN A 1 445 ? -22.934 18.927  -6.528  1.00 58.17  ? 454  ASN A ND2 1 
ATOM   2910  N N   . THR A 1 446 ? -17.607 18.336  -6.637  1.00 43.98  ? 455  THR A N   1 
ATOM   2911  C CA  . THR A 1 446 ? -16.265 18.021  -6.216  1.00 40.96  ? 455  THR A CA  1 
ATOM   2912  C C   . THR A 1 446 ? -15.617 19.336  -5.990  1.00 39.01  ? 455  THR A C   1 
ATOM   2913  O O   . THR A 1 446 ? -15.868 20.281  -6.733  1.00 38.92  ? 455  THR A O   1 
ATOM   2914  C CB  . THR A 1 446 ? -15.507 17.311  -7.313  1.00 40.59  ? 455  THR A CB  1 
ATOM   2915  O OG1 . THR A 1 446 ? -16.236 16.175  -7.756  1.00 42.82  ? 455  THR A OG1 1 
ATOM   2916  C CG2 . THR A 1 446 ? -14.225 16.807  -6.817  1.00 39.31  ? 455  THR A CG2 1 
ATOM   2917  N N   . LEU A 1 447 ? -14.788 19.401  -4.955  1.00 37.41  ? 456  LEU A N   1 
ATOM   2918  C CA  . LEU A 1 447 ? -14.045 20.617  -4.627  1.00 36.25  ? 456  LEU A CA  1 
ATOM   2919  C C   . LEU A 1 447 ? -12.571 20.403  -4.709  1.00 34.56  ? 456  LEU A C   1 
ATOM   2920  O O   . LEU A 1 447 ? -12.071 19.470  -4.092  1.00 34.37  ? 456  LEU A O   1 
ATOM   2921  C CB  . LEU A 1 447 ? -14.311 20.998  -3.200  1.00 36.53  ? 456  LEU A CB  1 
ATOM   2922  C CG  . LEU A 1 447 ? -13.705 22.314  -2.751  1.00 35.29  ? 456  LEU A CG  1 
ATOM   2923  C CD1 . LEU A 1 447 ? -14.358 23.472  -3.511  1.00 38.02  ? 456  LEU A CD1 1 
ATOM   2924  C CD2 . LEU A 1 447 ? -13.861 22.467  -1.247  1.00 34.71  ? 456  LEU A CD2 1 
ATOM   2925  N N   . TYR A 1 448 ? -11.860 21.266  -5.436  1.00 34.00  ? 457  TYR A N   1 
ATOM   2926  C CA  . TYR A 1 448 ? -10.394 21.116  -5.612  1.00 32.40  ? 457  TYR A CA  1 
ATOM   2927  C C   . TYR A 1 448 ? -9.726  22.236  -4.847  1.00 31.30  ? 457  TYR A C   1 
ATOM   2928  O O   . TYR A 1 448 ? -10.242 23.362  -4.863  1.00 32.38  ? 457  TYR A O   1 
ATOM   2929  C CB  . TYR A 1 448 ? -10.019 21.161  -7.095  1.00 32.34  ? 457  TYR A CB  1 
ATOM   2930  C CG  . TYR A 1 448 ? -10.512 19.970  -7.887  1.00 34.62  ? 457  TYR A CG  1 
ATOM   2931  C CD1 . TYR A 1 448 ? -11.851 19.830  -8.212  1.00 38.11  ? 457  TYR A CD1 1 
ATOM   2932  C CD2 . TYR A 1 448 ? -9.654  18.976  -8.285  1.00 34.50  ? 457  TYR A CD2 1 
ATOM   2933  C CE1 . TYR A 1 448 ? -12.304 18.724  -8.914  1.00 39.85  ? 457  TYR A CE1 1 
ATOM   2934  C CE2 . TYR A 1 448 ? -10.089 17.881  -8.999  1.00 36.37  ? 457  TYR A CE2 1 
ATOM   2935  C CZ  . TYR A 1 448 ? -11.404 17.759  -9.306  1.00 39.13  ? 457  TYR A CZ  1 
ATOM   2936  O OH  . TYR A 1 448 ? -11.827 16.670  -10.018 1.00 40.83  ? 457  TYR A OH  1 
ATOM   2937  N N   . TYR A 1 449 ? -8.623  21.952  -4.142  1.00 29.46  ? 458  TYR A N   1 
ATOM   2938  C CA  . TYR A 1 449 ? -7.932  22.996  -3.370  1.00 28.04  ? 458  TYR A CA  1 
ATOM   2939  C C   . TYR A 1 449 ? -6.676  23.447  -4.052  1.00 26.71  ? 458  TYR A C   1 
ATOM   2940  O O   . TYR A 1 449 ? -5.754  22.680  -4.153  1.00 26.37  ? 458  TYR A O   1 
ATOM   2941  C CB  . TYR A 1 449 ? -7.533  22.463  -2.037  1.00 27.19  ? 458  TYR A CB  1 
ATOM   2942  C CG  . TYR A 1 449 ? -8.673  22.109  -1.189  1.00 28.27  ? 458  TYR A CG  1 
ATOM   2943  C CD1 . TYR A 1 449 ? -9.158  20.823  -1.163  1.00 29.30  ? 458  TYR A CD1 1 
ATOM   2944  C CD2 . TYR A 1 449 ? -9.245  23.051  -0.367  1.00 29.38  ? 458  TYR A CD2 1 
ATOM   2945  C CE1 . TYR A 1 449 ? -10.204 20.488  -0.335  1.00 32.23  ? 458  TYR A CE1 1 
ATOM   2946  C CE2 . TYR A 1 449 ? -10.305 22.738  0.467   1.00 31.81  ? 458  TYR A CE2 1 
ATOM   2947  C CZ  . TYR A 1 449 ? -10.797 21.459  0.485   1.00 33.20  ? 458  TYR A CZ  1 
ATOM   2948  O OH  . TYR A 1 449 ? -11.888 21.179  1.307   1.00 34.69  ? 458  TYR A OH  1 
ATOM   2949  N N   . VAL A 1 450 ? -6.614  24.692  -4.499  1.00 26.53  ? 459  VAL A N   1 
ATOM   2950  C CA  . VAL A 1 450 ? -5.449  25.176  -5.218  1.00 25.69  ? 459  VAL A CA  1 
ATOM   2951  C C   . VAL A 1 450 ? -4.209  25.396  -4.323  1.00 25.03  ? 459  VAL A C   1 
ATOM   2952  O O   . VAL A 1 450 ? -3.069  25.290  -4.772  1.00 24.39  ? 459  VAL A O   1 
ATOM   2953  C CB  . VAL A 1 450 ? -5.754  26.440  -5.949  1.00 25.93  ? 459  VAL A CB  1 
ATOM   2954  C CG1 . VAL A 1 450 ? -4.588  26.776  -6.824  1.00 25.89  ? 459  VAL A CG1 1 
ATOM   2955  C CG2 . VAL A 1 450 ? -6.871  26.216  -6.789  1.00 26.89  ? 459  VAL A CG2 1 
ATOM   2956  N N   . ASN A 1 451 ? -4.447  25.706  -3.060  1.00 25.44  ? 460  ASN A N   1 
ATOM   2957  C CA  . ASN A 1 451 ? -3.417  25.872  -2.092  1.00 24.70  ? 460  ASN A CA  1 
ATOM   2958  C C   . ASN A 1 451 ? -3.578  24.882  -0.965  1.00 24.83  ? 460  ASN A C   1 
ATOM   2959  O O   . ASN A 1 451 ? -4.533  24.143  -0.903  1.00 25.46  ? 460  ASN A O   1 
ATOM   2960  C CB  . ASN A 1 451 ? -3.405  27.308  -1.661  1.00 25.00  ? 460  ASN A CB  1 
ATOM   2961  C CG  . ASN A 1 451 ? -2.864  28.188  -2.744  1.00 26.31  ? 460  ASN A CG  1 
ATOM   2962  O OD1 . ASN A 1 451 ? -1.814  27.919  -3.305  1.00 27.56  ? 460  ASN A OD1 1 
ATOM   2963  N ND2 . ASN A 1 451 ? -3.568  29.230  -3.057  1.00 28.69  ? 460  ASN A ND2 1 
ATOM   2964  N N   . LYS A 1 452 ? -2.588  24.769  -0.117  1.00 24.78  ? 461  LYS A N   1 
ATOM   2965  C CA  . LYS A 1 452 ? -2.716  23.837  0.947   1.00 25.33  ? 461  LYS A CA  1 
ATOM   2966  C C   . LYS A 1 452 ? -3.439  24.605  2.004   1.00 26.45  ? 461  LYS A C   1 
ATOM   2967  O O   . LYS A 1 452 ? -3.268  25.800  2.127   1.00 26.50  ? 461  LYS A O   1 
ATOM   2968  C CB  . LYS A 1 452 ? -1.359  23.445  1.439   1.00 24.25  ? 461  LYS A CB  1 
ATOM   2969  C CG  . LYS A 1 452 ? -0.483  22.921  0.383   1.00 25.08  ? 461  LYS A CG  1 
ATOM   2970  C CD  . LYS A 1 452 ? 0.501   21.965  0.989   1.00 26.07  ? 461  LYS A CD  1 
ATOM   2971  C CE  . LYS A 1 452 ? 1.475   21.494  -0.034  1.00 28.00  ? 461  LYS A CE  1 
ATOM   2972  N NZ  . LYS A 1 452 ? 2.384   20.573  0.640   1.00 29.19  ? 461  LYS A NZ  1 
ATOM   2973  N N   . GLN A 1 453 ? -4.277  23.931  2.763   1.00 27.77  ? 462  GLN A N   1 
ATOM   2974  C CA  . GLN A 1 453 ? -5.006  24.623  3.765   1.00 29.48  ? 462  GLN A CA  1 
ATOM   2975  C C   . GLN A 1 453 ? -4.250  24.542  5.075   1.00 29.50  ? 462  GLN A C   1 
ATOM   2976  O O   . GLN A 1 453 ? -3.964  23.451  5.558   1.00 29.12  ? 462  GLN A O   1 
ATOM   2977  C CB  . GLN A 1 453 ? -6.395  24.024  3.834   1.00 30.69  ? 462  GLN A CB  1 
ATOM   2978  C CG  . GLN A 1 453 ? -7.116  24.111  2.509   1.00 32.55  ? 462  GLN A CG  1 
ATOM   2979  C CD  . GLN A 1 453 ? -7.214  25.551  1.983   1.00 35.39  ? 462  GLN A CD  1 
ATOM   2980  O OE1 . GLN A 1 453 ? -7.934  26.380  2.533   1.00 38.16  ? 462  GLN A OE1 1 
ATOM   2981  N NE2 . GLN A 1 453 ? -6.493  25.846  0.931   1.00 35.01  ? 462  GLN A NE2 1 
ATOM   2982  N N   . GLU A 1 454 ? -3.880  25.702  5.612   1.00 30.69  ? 463  GLU A N   1 
ATOM   2983  C CA  . GLU A 1 454 ? -3.200  25.805  6.905   1.00 31.63  ? 463  GLU A CA  1 
ATOM   2984  C C   . GLU A 1 454 ? -4.188  25.543  7.987   1.00 32.44  ? 463  GLU A C   1 
ATOM   2985  O O   . GLU A 1 454 ? -5.339  25.870  7.829   1.00 34.31  ? 463  GLU A O   1 
ATOM   2986  C CB  . GLU A 1 454 ? -2.719  27.234  7.116   1.00 32.43  ? 463  GLU A CB  1 
ATOM   2987  C CG  . GLU A 1 454 ? -1.193  27.431  7.076   1.00 35.96  ? 463  GLU A CG  1 
ATOM   2988  C CD  . GLU A 1 454 ? -0.767  28.936  6.965   1.00 41.27  ? 463  GLU A CD  1 
ATOM   2989  O OE1 . GLU A 1 454 ? -0.985  29.665  7.992   1.00 43.26  ? 463  GLU A OE1 1 
ATOM   2990  O OE2 . GLU A 1 454 ? -0.215  29.358  5.874   1.00 41.80  ? 463  GLU A OE2 1 
ATOM   2991  N N   . GLY A 1 455 ? -3.778  25.007  9.112   1.00 31.88  ? 464  GLY A N   1 
ATOM   2992  C CA  . GLY A 1 455 ? -4.713  24.952  10.225  1.00 33.03  ? 464  GLY A CA  1 
ATOM   2993  C C   . GLY A 1 455 ? -3.980  24.585  11.482  1.00 32.89  ? 464  GLY A C   1 
ATOM   2994  O O   . GLY A 1 455 ? -2.987  23.860  11.423  1.00 32.65  ? 464  GLY A O   1 
ATOM   2995  N N   . LYS A 1 456 ? -4.410  25.137  12.609  1.00 33.58  ? 465  LYS A N   1 
ATOM   2996  C CA  . LYS A 1 456 ? -4.096  24.596  13.929  1.00 33.17  ? 465  LYS A CA  1 
ATOM   2997  C C   . LYS A 1 456 ? -2.692  24.041  14.141  1.00 31.95  ? 465  LYS A C   1 
ATOM   2998  O O   . LYS A 1 456 ? -2.389  22.901  13.787  1.00 31.49  ? 465  LYS A O   1 
ATOM   2999  C CB  . LYS A 1 456 ? -5.101  23.503  14.262  1.00 33.58  ? 465  LYS A CB  1 
ATOM   3000  C CG  . LYS A 1 456 ? -5.177  23.233  15.693  1.00 34.36  ? 465  LYS A CG  1 
ATOM   3001  C CD  . LYS A 1 456 ? -6.329  22.352  16.060  1.00 37.53  ? 465  LYS A CD  1 
ATOM   3002  C CE  . LYS A 1 456 ? -6.503  22.429  17.592  1.00 40.83  ? 465  LYS A CE  1 
ATOM   3003  N NZ  . LYS A 1 456 ? -6.908  21.139  18.242  1.00 43.01  ? 465  LYS A NZ  1 
ATOM   3004  N N   . SER A 1 457 ? -1.836  24.828  14.753  1.00 31.85  ? 466  SER A N   1 
ATOM   3005  C CA  . SER A 1 457 ? -0.614  24.249  15.241  1.00 31.11  ? 466  SER A CA  1 
ATOM   3006  C C   . SER A 1 457 ? -0.933  23.419  16.481  1.00 30.89  ? 466  SER A C   1 
ATOM   3007  O O   . SER A 1 457 ? -1.824  23.748  17.246  1.00 31.23  ? 466  SER A O   1 
ATOM   3008  C CB  . SER A 1 457 ? 0.360   25.353  15.589  1.00 31.28  ? 466  SER A CB  1 
ATOM   3009  O OG  . SER A 1 457 ? -0.338  26.359  16.296  1.00 34.16  ? 466  SER A OG  1 
ATOM   3010  N N   . LEU A 1 458 ? -0.202  22.331  16.656  1.00 30.43  ? 467  LEU A N   1 
ATOM   3011  C CA  . LEU A 1 458 ? -0.279  21.545  17.867  1.00 30.66  ? 467  LEU A CA  1 
ATOM   3012  C C   . LEU A 1 458 ? 1.038   21.659  18.539  1.00 30.28  ? 467  LEU A C   1 
ATOM   3013  O O   . LEU A 1 458 ? 2.076   21.698  17.872  1.00 29.49  ? 467  LEU A O   1 
ATOM   3014  C CB  . LEU A 1 458 ? -0.567  20.100  17.551  1.00 30.48  ? 467  LEU A CB  1 
ATOM   3015  C CG  . LEU A 1 458 ? -2.020  19.958  17.112  1.00 31.43  ? 467  LEU A CG  1 
ATOM   3016  C CD1 . LEU A 1 458 ? -2.429  18.504  16.941  1.00 31.12  ? 467  LEU A CD1 1 
ATOM   3017  C CD2 . LEU A 1 458 ? -2.898  20.628  18.124  1.00 31.94  ? 467  LEU A CD2 1 
ATOM   3018  N N   . TYR A 1 459 ? 0.991   21.727  19.861  1.00 31.31  ? 468  TYR A N   1 
ATOM   3019  C CA  . TYR A 1 459 ? 2.171   22.023  20.643  1.00 31.62  ? 468  TYR A CA  1 
ATOM   3020  C C   . TYR A 1 459 ? 2.331   21.056  21.805  1.00 30.60  ? 468  TYR A C   1 
ATOM   3021  O O   . TYR A 1 459 ? 1.403   20.793  22.517  1.00 31.27  ? 468  TYR A O   1 
ATOM   3022  C CB  . TYR A 1 459 ? 2.139   23.486  21.101  1.00 33.09  ? 468  TYR A CB  1 
ATOM   3023  C CG  . TYR A 1 459 ? 3.394   23.889  21.850  1.00 37.75  ? 468  TYR A CG  1 
ATOM   3024  C CD1 . TYR A 1 459 ? 4.650   23.983  21.185  1.00 40.26  ? 468  TYR A CD1 1 
ATOM   3025  C CD2 . TYR A 1 459 ? 3.355   24.165  23.246  1.00 42.80  ? 468  TYR A CD2 1 
ATOM   3026  C CE1 . TYR A 1 459 ? 5.852   24.347  21.884  1.00 41.32  ? 468  TYR A CE1 1 
ATOM   3027  C CE2 . TYR A 1 459 ? 4.568   24.529  23.971  1.00 44.18  ? 468  TYR A CE2 1 
ATOM   3028  C CZ  . TYR A 1 459 ? 5.800   24.616  23.267  1.00 43.17  ? 468  TYR A CZ  1 
ATOM   3029  O OH  . TYR A 1 459 ? 6.937   24.982  23.952  1.00 43.15  ? 468  TYR A OH  1 
ATOM   3030  N N   . VAL A 1 460 ? 3.512   20.503  21.987  1.00 29.63  ? 469  VAL A N   1 
ATOM   3031  C CA  . VAL A 1 460 ? 3.710   19.560  23.070  1.00 29.79  ? 469  VAL A CA  1 
ATOM   3032  C C   . VAL A 1 460 ? 4.865   19.940  23.949  1.00 30.26  ? 469  VAL A C   1 
ATOM   3033  O O   . VAL A 1 460 ? 6.015   19.821  23.559  1.00 29.75  ? 469  VAL A O   1 
ATOM   3034  C CB  . VAL A 1 460 ? 3.960   18.184  22.551  1.00 29.09  ? 469  VAL A CB  1 
ATOM   3035  C CG1 . VAL A 1 460 ? 4.465   17.297  23.668  1.00 27.93  ? 469  VAL A CG1 1 
ATOM   3036  C CG2 . VAL A 1 460 ? 2.692   17.663  21.970  1.00 29.84  ? 469  VAL A CG2 1 
ATOM   3037  N N   . LYS A 1 461 ? 4.535   20.381  25.157  1.00 32.04  ? 470  LYS A N   1 
ATOM   3038  C CA  . LYS A 1 461 ? 5.492   20.974  26.086  1.00 32.80  ? 470  LYS A CA  1 
ATOM   3039  C C   . LYS A 1 461 ? 6.261   19.890  26.860  1.00 32.29  ? 470  LYS A C   1 
ATOM   3040  O O   . LYS A 1 461 ? 5.796   18.758  26.998  1.00 32.22  ? 470  LYS A O   1 
ATOM   3041  C CB  . LYS A 1 461 ? 4.748   22.019  26.967  1.00 34.14  ? 470  LYS A CB  1 
ATOM   3042  C CG  . LYS A 1 461 ? 5.086   22.081  28.498  1.00 37.64  ? 470  LYS A CG  1 
ATOM   3043  C CD  . LYS A 1 461 ? 5.933   23.364  28.992  1.00 41.71  ? 470  LYS A CD  1 
ATOM   3044  C CE  . LYS A 1 461 ? 6.400   23.282  30.526  1.00 42.06  ? 470  LYS A CE  1 
ATOM   3045  N NZ  . LYS A 1 461 ? 7.717   23.969  30.762  1.00 41.21  ? 470  LYS A NZ  1 
ATOM   3046  N N   . GLY A 1 462 ? 7.469   20.227  27.284  1.00 32.16  ? 471  GLY A N   1 
ATOM   3047  C CA  . GLY A 1 462 ? 8.223   19.388  28.177  1.00 33.00  ? 471  GLY A CA  1 
ATOM   3048  C C   . GLY A 1 462 ? 8.694   20.240  29.326  1.00 34.25  ? 471  GLY A C   1 
ATOM   3049  O O   . GLY A 1 462 ? 8.956   21.427  29.138  1.00 34.59  ? 471  GLY A O   1 
ATOM   3050  N N   . GLU A 1 463 ? 8.776   19.651  30.519  1.00 35.38  ? 472  GLU A N   1 
ATOM   3051  C CA  . GLU A 1 463 ? 9.444   20.285  31.678  1.00 36.80  ? 472  GLU A CA  1 
ATOM   3052  C C   . GLU A 1 463 ? 10.977  19.910  31.709  1.00 35.87  ? 472  GLU A C   1 
ATOM   3053  O O   . GLU A 1 463 ? 11.452  19.216  30.801  1.00 35.41  ? 472  GLU A O   1 
ATOM   3054  C CB  . GLU A 1 463 ? 8.665   19.963  32.988  1.00 37.79  ? 472  GLU A CB  1 
ATOM   3055  C CG  . GLU A 1 463 ? 9.261   18.842  33.932  1.00 41.76  ? 472  GLU A CG  1 
ATOM   3056  C CD  . GLU A 1 463 ? 9.812   17.527  33.202  1.00 46.57  ? 472  GLU A CD  1 
ATOM   3057  O OE1 . GLU A 1 463 ? 9.183   17.051  32.213  1.00 47.53  ? 472  GLU A OE1 1 
ATOM   3058  O OE2 . GLU A 1 463 ? 10.867  16.950  33.634  1.00 47.47  ? 472  GLU A OE2 1 
ATOM   3059  N N   . PRO A 1 464 ? 11.761  20.389  32.709  1.00 35.94  ? 473  PRO A N   1 
ATOM   3060  C CA  . PRO A 1 464 ? 13.103  19.815  32.763  1.00 35.39  ? 473  PRO A CA  1 
ATOM   3061  C C   . PRO A 1 464 ? 13.242  18.835  33.897  1.00 35.26  ? 473  PRO A C   1 
ATOM   3062  O O   . PRO A 1 464 ? 12.455  18.885  34.851  1.00 35.21  ? 473  PRO A O   1 
ATOM   3063  C CB  . PRO A 1 464 ? 14.008  21.030  33.001  1.00 35.66  ? 473  PRO A CB  1 
ATOM   3064  C CG  . PRO A 1 464 ? 13.161  21.985  33.758  1.00 36.59  ? 473  PRO A CG  1 
ATOM   3065  C CD  . PRO A 1 464 ? 11.679  21.604  33.538  1.00 36.67  ? 473  PRO A CD  1 
ATOM   3066  N N   . ILE A 1 465 ? 14.279  18.000  33.797  1.00 35.29  ? 474  ILE A N   1 
ATOM   3067  C CA  . ILE A 1 465 ? 14.421  16.780  34.586  1.00 35.79  ? 474  ILE A CA  1 
ATOM   3068  C C   . ILE A 1 465 ? 15.620  16.769  35.538  1.00 36.23  ? 474  ILE A C   1 
ATOM   3069  O O   . ILE A 1 465 ? 16.720  17.225  35.194  1.00 35.91  ? 474  ILE A O   1 
ATOM   3070  C CB  . ILE A 1 465 ? 14.372  15.563  33.648  1.00 35.67  ? 474  ILE A CB  1 
ATOM   3071  C CG1 . ILE A 1 465 ? 14.420  14.245  34.410  1.00 36.68  ? 474  ILE A CG1 1 
ATOM   3072  C CG2 . ILE A 1 465 ? 15.447  15.616  32.595  1.00 34.88  ? 474  ILE A CG2 1 
ATOM   3073  C CD1 . ILE A 1 465 ? 13.985  13.067  33.504  1.00 37.97  ? 474  ILE A CD1 1 
ATOM   3074  N N   . ILE A 1 466 ? 15.375  16.215  36.726  1.00 37.51  ? 475  ILE A N   1 
ATOM   3075  C CA  . ILE A 1 466 ? 16.142  16.516  37.983  1.00 38.87  ? 475  ILE A CA  1 
ATOM   3076  C C   . ILE A 1 466 ? 17.206  15.487  38.523  1.00 39.72  ? 475  ILE A C   1 
ATOM   3077  O O   . ILE A 1 466 ? 16.837  14.402  39.020  1.00 39.39  ? 475  ILE A O   1 
ATOM   3078  C CB  . ILE A 1 466 ? 15.149  16.910  39.157  1.00 39.45  ? 475  ILE A CB  1 
ATOM   3079  C CG1 . ILE A 1 466 ? 13.955  15.897  39.240  1.00 40.71  ? 475  ILE A CG1 1 
ATOM   3080  C CG2 . ILE A 1 466 ? 14.666  18.393  38.998  1.00 37.65  ? 475  ILE A CG2 1 
ATOM   3081  C CD1 . ILE A 1 466 ? 13.666  15.246  40.651  1.00 41.37  ? 475  ILE A CD1 1 
ATOM   3082  N N   . ASN A 1 467 ? 18.504  15.837  38.414  1.00 40.91  ? 476  ASN A N   1 
ATOM   3083  C CA  . ASN A 1 467 ? 19.604  15.020  38.994  1.00 42.51  ? 476  ASN A CA  1 
ATOM   3084  C C   . ASN A 1 467 ? 19.913  15.281  40.522  1.00 43.55  ? 476  ASN A C   1 
ATOM   3085  O O   . ASN A 1 467 ? 20.774  16.088  40.940  1.00 44.01  ? 476  ASN A O   1 
ATOM   3086  C CB  . ASN A 1 467 ? 20.872  14.982  38.097  1.00 42.57  ? 476  ASN A CB  1 
ATOM   3087  C CG  . ASN A 1 467 ? 21.789  13.762  38.443  1.00 44.10  ? 476  ASN A CG  1 
ATOM   3088  O OD1 . ASN A 1 467 ? 21.267  12.699  38.819  1.00 45.08  ? 476  ASN A OD1 1 
ATOM   3089  N ND2 . ASN A 1 467 ? 23.132  13.919  38.342  1.00 43.96  ? 476  ASN A ND2 1 
ATOM   3090  N N   . PHE A 1 468 ? 19.259  14.459  41.317  1.00 44.29  ? 477  PHE A N   1 
ATOM   3091  C CA  . PHE A 1 468 ? 18.615  14.798  42.597  1.00 45.26  ? 477  PHE A CA  1 
ATOM   3092  C C   . PHE A 1 468 ? 19.342  14.186  43.805  1.00 45.42  ? 477  PHE A C   1 
ATOM   3093  O O   . PHE A 1 468 ? 18.686  13.633  44.731  1.00 46.06  ? 477  PHE A O   1 
ATOM   3094  C CB  . PHE A 1 468 ? 17.302  14.039  42.482  1.00 45.81  ? 477  PHE A CB  1 
ATOM   3095  C CG  . PHE A 1 468 ? 17.499  12.686  41.745  1.00 47.53  ? 477  PHE A CG  1 
ATOM   3096  C CD1 . PHE A 1 468 ? 17.919  11.520  42.468  1.00 48.64  ? 477  PHE A CD1 1 
ATOM   3097  C CD2 . PHE A 1 468 ? 17.389  12.612  40.309  1.00 46.23  ? 477  PHE A CD2 1 
ATOM   3098  C CE1 . PHE A 1 468 ? 18.144  10.305  41.775  1.00 49.14  ? 477  PHE A CE1 1 
ATOM   3099  C CE2 . PHE A 1 468 ? 17.612  11.410  39.602  1.00 46.18  ? 477  PHE A CE2 1 
ATOM   3100  C CZ  . PHE A 1 468 ? 17.981  10.255  40.320  1.00 47.92  ? 477  PHE A CZ  1 
ATOM   3101  N N   . TYR A 1 469 ? 20.676  14.254  43.808  1.00 44.88  ? 478  TYR A N   1 
ATOM   3102  C CA  . TYR A 1 469 ? 21.459  13.406  44.735  1.00 44.52  ? 478  TYR A CA  1 
ATOM   3103  C C   . TYR A 1 469 ? 21.907  13.979  46.090  1.00 44.08  ? 478  TYR A C   1 
ATOM   3104  O O   . TYR A 1 469 ? 22.338  15.143  46.195  1.00 43.92  ? 478  TYR A O   1 
ATOM   3105  C CB  . TYR A 1 469 ? 22.618  12.759  43.976  1.00 44.91  ? 478  TYR A CB  1 
ATOM   3106  C CG  . TYR A 1 469 ? 23.952  12.729  44.679  1.00 45.27  ? 478  TYR A CG  1 
ATOM   3107  C CD1 . TYR A 1 469 ? 24.320  11.642  45.460  1.00 45.16  ? 478  TYR A CD1 1 
ATOM   3108  C CD2 . TYR A 1 469 ? 24.862  13.780  44.509  1.00 45.56  ? 478  TYR A CD2 1 
ATOM   3109  C CE1 . TYR A 1 469 ? 25.562  11.618  46.073  1.00 46.94  ? 478  TYR A CE1 1 
ATOM   3110  C CE2 . TYR A 1 469 ? 26.089  13.769  45.107  1.00 46.66  ? 478  TYR A CE2 1 
ATOM   3111  C CZ  . TYR A 1 469 ? 26.446  12.690  45.896  1.00 47.67  ? 478  TYR A CZ  1 
ATOM   3112  O OH  . TYR A 1 469 ? 27.690  12.678  46.507  1.00 48.96  ? 478  TYR A OH  1 
ATOM   3113  N N   . ASP A 1 470 ? 21.828  13.138  47.116  1.00 43.39  ? 479  ASP A N   1 
ATOM   3114  C CA  . ASP A 1 470 ? 22.087  13.630  48.457  1.00 43.36  ? 479  ASP A CA  1 
ATOM   3115  C C   . ASP A 1 470 ? 23.107  12.887  49.343  1.00 42.91  ? 479  ASP A C   1 
ATOM   3116  O O   . ASP A 1 470 ? 22.827  11.798  49.876  1.00 43.08  ? 479  ASP A O   1 
ATOM   3117  C CB  . ASP A 1 470 ? 20.781  13.879  49.205  1.00 43.91  ? 479  ASP A CB  1 
ATOM   3118  C CG  . ASP A 1 470 ? 20.959  14.885  50.356  1.00 46.19  ? 479  ASP A CG  1 
ATOM   3119  O OD1 . ASP A 1 470 ? 21.723  15.895  50.181  1.00 47.67  ? 479  ASP A OD1 1 
ATOM   3120  O OD2 . ASP A 1 470 ? 20.334  14.658  51.434  1.00 48.41  ? 479  ASP A OD2 1 
ATOM   3121  N N   . PRO A 1 471 ? 24.284  13.513  49.549  1.00 42.38  ? 480  PRO A N   1 
ATOM   3122  C CA  . PRO A 1 471 ? 25.390  12.739  50.086  1.00 41.99  ? 480  PRO A CA  1 
ATOM   3123  C C   . PRO A 1 471 ? 25.110  12.382  51.521  1.00 41.52  ? 480  PRO A C   1 
ATOM   3124  O O   . PRO A 1 471 ? 24.316  13.038  52.189  1.00 40.72  ? 480  PRO A O   1 
ATOM   3125  C CB  . PRO A 1 471 ? 26.575  13.710  49.993  1.00 42.30  ? 480  PRO A CB  1 
ATOM   3126  C CG  . PRO A 1 471 ? 25.941  15.080  50.179  1.00 42.68  ? 480  PRO A CG  1 
ATOM   3127  C CD  . PRO A 1 471 ? 24.600  14.964  49.482  1.00 42.49  ? 480  PRO A CD  1 
ATOM   3128  N N   . LEU A 1 472 ? 25.754  11.315  51.957  1.00 41.58  ? 481  LEU A N   1 
ATOM   3129  C CA  . LEU A 1 472 ? 25.790  10.941  53.358  1.00 41.66  ? 481  LEU A CA  1 
ATOM   3130  C C   . LEU A 1 472 ? 27.049  11.484  54.001  1.00 41.76  ? 481  LEU A C   1 
ATOM   3131  O O   . LEU A 1 472 ? 28.151  11.327  53.464  1.00 42.03  ? 481  LEU A O   1 
ATOM   3132  C CB  . LEU A 1 472 ? 25.783  9.418   53.485  1.00 42.05  ? 481  LEU A CB  1 
ATOM   3133  C CG  . LEU A 1 472 ? 25.142  8.912   54.763  1.00 42.30  ? 481  LEU A CG  1 
ATOM   3134  C CD1 . LEU A 1 472 ? 24.065  9.925   55.280  1.00 42.60  ? 481  LEU A CD1 1 
ATOM   3135  C CD2 . LEU A 1 472 ? 24.578  7.519   54.488  1.00 40.94  ? 481  LEU A CD2 1 
ATOM   3136  N N   . VAL A 1 473 ? 26.911  12.112  55.152  1.00 41.61  ? 482  VAL A N   1 
ATOM   3137  C CA  . VAL A 1 473 ? 28.117  12.612  55.772  1.00 42.49  ? 482  VAL A CA  1 
ATOM   3138  C C   . VAL A 1 473 ? 28.232  12.341  57.264  1.00 43.49  ? 482  VAL A C   1 
ATOM   3139  O O   . VAL A 1 473 ? 27.224  12.357  57.998  1.00 43.56  ? 482  VAL A O   1 
ATOM   3140  C CB  . VAL A 1 473 ? 28.464  14.077  55.328  1.00 42.42  ? 482  VAL A CB  1 
ATOM   3141  C CG1 . VAL A 1 473 ? 28.445  15.089  56.484  1.00 41.93  ? 482  VAL A CG1 1 
ATOM   3142  C CG2 . VAL A 1 473 ? 29.817  14.078  54.578  1.00 42.95  ? 482  VAL A CG2 1 
ATOM   3143  N N   . PHE A 1 474 ? 29.466  12.060  57.699  1.00 43.97  ? 483  PHE A N   1 
ATOM   3144  C CA  . PHE A 1 474 ? 29.674  11.623  59.071  1.00 44.32  ? 483  PHE A CA  1 
ATOM   3145  C C   . PHE A 1 474 ? 30.282  12.663  60.030  1.00 44.97  ? 483  PHE A C   1 
ATOM   3146  O O   . PHE A 1 474 ? 31.252  13.331  59.671  1.00 45.74  ? 483  PHE A O   1 
ATOM   3147  C CB  . PHE A 1 474 ? 30.517  10.357  59.084  1.00 44.85  ? 483  PHE A CB  1 
ATOM   3148  C CG  . PHE A 1 474 ? 30.592  9.732   60.429  1.00 45.20  ? 483  PHE A CG  1 
ATOM   3149  C CD1 . PHE A 1 474 ? 29.637  8.801   60.826  1.00 44.12  ? 483  PHE A CD1 1 
ATOM   3150  C CD2 . PHE A 1 474 ? 31.583  10.119  61.333  1.00 46.21  ? 483  PHE A CD2 1 
ATOM   3151  C CE1 . PHE A 1 474 ? 29.678  8.245   62.084  1.00 44.69  ? 483  PHE A CE1 1 
ATOM   3152  C CE2 . PHE A 1 474 ? 31.641  9.565   62.611  1.00 46.84  ? 483  PHE A CE2 1 
ATOM   3153  C CZ  . PHE A 1 474 ? 30.689  8.619   62.983  1.00 46.43  ? 483  PHE A CZ  1 
ATOM   3154  N N   . PRO A 1 475 ? 29.729  12.779  61.257  1.00 44.99  ? 484  PRO A N   1 
ATOM   3155  C CA  . PRO A 1 475 ? 30.188  13.671  62.336  1.00 45.88  ? 484  PRO A CA  1 
ATOM   3156  C C   . PRO A 1 475 ? 31.654  13.511  62.771  1.00 47.14  ? 484  PRO A C   1 
ATOM   3157  O O   . PRO A 1 475 ? 32.020  13.844  63.907  1.00 47.98  ? 484  PRO A O   1 
ATOM   3158  C CB  . PRO A 1 475 ? 29.255  13.307  63.509  1.00 46.05  ? 484  PRO A CB  1 
ATOM   3159  C CG  . PRO A 1 475 ? 28.575  12.042  63.111  1.00 45.36  ? 484  PRO A CG  1 
ATOM   3160  C CD  . PRO A 1 475 ? 28.469  12.117  61.628  1.00 44.62  ? 484  PRO A CD  1 
ATOM   3161  N N   . SER A 1 476 ? 32.488  13.042  61.854  1.00 47.54  ? 485  SER A N   1 
ATOM   3162  C CA  . SER A 1 476 ? 33.862  12.663  62.157  1.00 49.10  ? 485  SER A CA  1 
ATOM   3163  C C   . SER A 1 476 ? 34.472  13.462  63.289  1.00 50.22  ? 485  SER A C   1 
ATOM   3164  O O   . SER A 1 476 ? 34.890  12.888  64.285  1.00 51.03  ? 485  SER A O   1 
ATOM   3165  C CB  . SER A 1 476 ? 34.761  12.772  60.915  1.00 49.40  ? 485  SER A CB  1 
ATOM   3166  O OG  . SER A 1 476 ? 36.147  12.670  61.278  1.00 51.40  ? 485  SER A OG  1 
ATOM   3167  N N   . ASP A 1 477 ? 34.519  14.781  63.131  1.00 50.57  ? 486  ASP A N   1 
ATOM   3168  C CA  . ASP A 1 477 ? 35.236  15.619  64.078  1.00 52.20  ? 486  ASP A CA  1 
ATOM   3169  C C   . ASP A 1 477 ? 34.701  15.491  65.501  1.00 52.55  ? 486  ASP A C   1 
ATOM   3170  O O   . ASP A 1 477 ? 35.459  15.234  66.447  1.00 53.37  ? 486  ASP A O   1 
ATOM   3171  C CB  . ASP A 1 477 ? 35.230  17.066  63.604  1.00 52.52  ? 486  ASP A CB  1 
ATOM   3172  C CG  . ASP A 1 477 ? 36.342  17.334  62.623  1.00 54.02  ? 486  ASP A CG  1 
ATOM   3173  O OD1 . ASP A 1 477 ? 37.069  16.358  62.310  1.00 54.93  ? 486  ASP A OD1 1 
ATOM   3174  O OD2 . ASP A 1 477 ? 36.497  18.501  62.174  1.00 55.98  ? 486  ASP A OD2 1 
ATOM   3175  N N   . GLU A 1 478 ? 33.387  15.636  65.632  1.00 51.63  ? 487  GLU A N   1 
ATOM   3176  C CA  . GLU A 1 478 ? 32.751  15.586  66.934  1.00 52.05  ? 487  GLU A CA  1 
ATOM   3177  C C   . GLU A 1 478 ? 32.992  14.223  67.608  1.00 51.45  ? 487  GLU A C   1 
ATOM   3178  O O   . GLU A 1 478 ? 33.078  14.117  68.830  1.00 52.19  ? 487  GLU A O   1 
ATOM   3179  C CB  . GLU A 1 478 ? 31.254  15.869  66.767  1.00 51.74  ? 487  GLU A CB  1 
ATOM   3180  C CG  . GLU A 1 478 ? 30.493  16.153  68.082  1.00 55.15  ? 487  GLU A CG  1 
ATOM   3181  C CD  . GLU A 1 478 ? 29.083  15.493  68.130  1.00 58.08  ? 487  GLU A CD  1 
ATOM   3182  O OE1 . GLU A 1 478 ? 28.474  15.460  69.237  1.00 59.79  ? 487  GLU A OE1 1 
ATOM   3183  O OE2 . GLU A 1 478 ? 28.592  15.001  67.071  1.00 57.95  ? 487  GLU A OE2 1 
ATOM   3184  N N   . PHE A 1 479 ? 33.105  13.187  66.796  1.00 49.87  ? 488  PHE A N   1 
ATOM   3185  C CA  . PHE A 1 479 ? 33.325  11.867  67.313  1.00 49.47  ? 488  PHE A CA  1 
ATOM   3186  C C   . PHE A 1 479 ? 34.743  11.770  67.820  1.00 50.23  ? 488  PHE A C   1 
ATOM   3187  O O   . PHE A 1 479 ? 34.965  11.433  68.966  1.00 50.92  ? 488  PHE A O   1 
ATOM   3188  C CB  . PHE A 1 479 ? 33.086  10.863  66.206  1.00 48.88  ? 488  PHE A CB  1 
ATOM   3189  C CG  . PHE A 1 479 ? 33.211  9.436   66.635  1.00 49.16  ? 488  PHE A CG  1 
ATOM   3190  C CD1 . PHE A 1 479 ? 32.090  8.704   66.970  1.00 48.63  ? 488  PHE A CD1 1 
ATOM   3191  C CD2 . PHE A 1 479 ? 34.442  8.815   66.661  1.00 49.46  ? 488  PHE A CD2 1 
ATOM   3192  C CE1 . PHE A 1 479 ? 32.196  7.390   67.334  1.00 48.89  ? 488  PHE A CE1 1 
ATOM   3193  C CE2 . PHE A 1 479 ? 34.543  7.503   67.030  1.00 49.92  ? 488  PHE A CE2 1 
ATOM   3194  C CZ  . PHE A 1 479 ? 33.421  6.789   67.363  1.00 49.38  ? 488  PHE A CZ  1 
ATOM   3195  N N   . ASP A 1 480 ? 35.697  12.081  66.953  1.00 50.16  ? 489  ASP A N   1 
ATOM   3196  C CA  . ASP A 1 480 ? 37.129  12.090  67.295  1.00 51.57  ? 489  ASP A CA  1 
ATOM   3197  C C   . ASP A 1 480 ? 37.437  12.903  68.553  1.00 52.43  ? 489  ASP A C   1 
ATOM   3198  O O   . ASP A 1 480 ? 38.467  12.695  69.216  1.00 53.63  ? 489  ASP A O   1 
ATOM   3199  C CB  . ASP A 1 480 ? 37.960  12.677  66.143  1.00 51.85  ? 489  ASP A CB  1 
ATOM   3200  C CG  . ASP A 1 480 ? 38.059  11.747  64.937  1.00 52.38  ? 489  ASP A CG  1 
ATOM   3201  O OD1 . ASP A 1 480 ? 37.430  10.660  64.955  1.00 53.74  ? 489  ASP A OD1 1 
ATOM   3202  O OD2 . ASP A 1 480 ? 38.762  12.118  63.965  1.00 53.37  ? 489  ASP A OD2 1 
ATOM   3203  N N   . ALA A 1 481 ? 36.550  13.857  68.840  1.00 51.78  ? 490  ALA A N   1 
ATOM   3204  C CA  . ALA A 1 481 ? 36.613  14.686  70.041  1.00 52.20  ? 490  ALA A CA  1 
ATOM   3205  C C   . ALA A 1 481 ? 36.353  13.820  71.253  1.00 52.35  ? 490  ALA A C   1 
ATOM   3206  O O   . ALA A 1 481 ? 37.174  13.772  72.178  1.00 53.61  ? 490  ALA A O   1 
ATOM   3207  C CB  . ALA A 1 481 ? 35.576  15.791  69.966  1.00 51.64  ? 490  ALA A CB  1 
ATOM   3208  N N   . SER A 1 482 ? 35.213  13.131  71.226  1.00 50.89  ? 491  SER A N   1 
ATOM   3209  C CA  . SER A 1 482 ? 34.827  12.238  72.299  1.00 51.01  ? 491  SER A CA  1 
ATOM   3210  C C   . SER A 1 482 ? 35.944  11.265  72.626  1.00 51.86  ? 491  SER A C   1 
ATOM   3211  O O   . SER A 1 482 ? 36.244  11.000  73.798  1.00 53.02  ? 491  SER A O   1 
ATOM   3212  C CB  . SER A 1 482 ? 33.576  11.468  71.923  1.00 49.70  ? 491  SER A CB  1 
ATOM   3213  O OG  . SER A 1 482 ? 32.439  12.243  72.195  1.00 49.68  ? 491  SER A OG  1 
ATOM   3214  N N   . ILE A 1 483 ? 36.570  10.740  71.588  1.00 51.41  ? 492  ILE A N   1 
ATOM   3215  C CA  . ILE A 1 483 ? 37.578  9.736   71.805  1.00 52.50  ? 492  ILE A CA  1 
ATOM   3216  C C   . ILE A 1 483 ? 38.846  10.337  72.359  1.00 53.98  ? 492  ILE A C   1 
ATOM   3217  O O   . ILE A 1 483 ? 39.291  9.910   73.430  1.00 55.28  ? 492  ILE A O   1 
ATOM   3218  C CB  . ILE A 1 483 ? 37.852  8.916   70.556  1.00 52.12  ? 492  ILE A CB  1 
ATOM   3219  C CG1 . ILE A 1 483 ? 36.550  8.229   70.141  1.00 51.37  ? 492  ILE A CG1 1 
ATOM   3220  C CG2 . ILE A 1 483 ? 38.975  7.914   70.818  1.00 53.29  ? 492  ILE A CG2 1 
ATOM   3221  C CD1 . ILE A 1 483 ? 36.655  6.738   69.936  1.00 53.17  ? 492  ILE A CD1 1 
ATOM   3222  N N   . SER A 1 484 ? 39.420  11.318  71.653  1.00 54.07  ? 493  SER A N   1 
ATOM   3223  C CA  . SER A 1 484 ? 40.626  11.983  72.137  0.50 55.37  ? 493  SER A CA  1 
ATOM   3224  C C   . SER A 1 484 ? 40.365  12.390  73.578  1.00 56.19  ? 493  SER A C   1 
ATOM   3225  O O   . SER A 1 484 ? 41.285  12.708  74.334  1.00 58.16  ? 493  SER A O   1 
ATOM   3226  C CB  . SER A 1 484 ? 40.978  13.197  71.294  0.50 55.15  ? 493  SER A CB  1 
ATOM   3227  O OG  . SER A 1 484 ? 42.165  13.778  71.788  0.50 56.38  ? 493  SER A OG  1 
ATOM   3228  N N   . GLN A 1 485 ? 39.097  12.310  73.963  1.00 54.86  ? 494  GLN A N   1 
ATOM   3229  C CA  . GLN A 1 485 ? 38.676  12.638  75.306  1.00 55.35  ? 494  GLN A CA  1 
ATOM   3230  C C   . GLN A 1 485 ? 38.455  11.413  76.232  1.00 55.05  ? 494  GLN A C   1 
ATOM   3231  O O   . GLN A 1 485 ? 38.566  11.530  77.451  1.00 55.92  ? 494  GLN A O   1 
ATOM   3232  C CB  . GLN A 1 485 ? 37.437  13.528  75.204  1.00 54.62  ? 494  GLN A CB  1 
ATOM   3233  C CG  . GLN A 1 485 ? 37.288  14.545  76.313  1.00 57.66  ? 494  GLN A CG  1 
ATOM   3234  C CD  . GLN A 1 485 ? 36.261  14.105  77.344  1.00 60.54  ? 494  GLN A CD  1 
ATOM   3235  O OE1 . GLN A 1 485 ? 35.240  13.498  76.986  1.00 59.57  ? 494  GLN A OE1 1 
ATOM   3236  N NE2 . GLN A 1 485 ? 36.526  14.396  78.634  1.00 63.21  ? 494  GLN A NE2 1 
ATOM   3237  N N   . VAL A 1 486 ? 38.142  10.245  75.675  1.00 53.92  ? 495  VAL A N   1 
ATOM   3238  C CA  . VAL A 1 486 ? 38.143  9.028   76.488  1.00 54.00  ? 495  VAL A CA  1 
ATOM   3239  C C   . VAL A 1 486 ? 39.570  8.844   76.957  1.00 55.74  ? 495  VAL A C   1 
ATOM   3240  O O   . VAL A 1 486 ? 39.816  8.422   78.079  1.00 56.80  ? 495  VAL A O   1 
ATOM   3241  C CB  . VAL A 1 486 ? 37.627  7.779   75.723  1.00 53.16  ? 495  VAL A CB  1 
ATOM   3242  C CG1 . VAL A 1 486 ? 38.281  6.502   76.211  1.00 53.73  ? 495  VAL A CG1 1 
ATOM   3243  C CG2 . VAL A 1 486 ? 36.137  7.659   75.859  1.00 51.43  ? 495  VAL A CG2 1 
ATOM   3244  N N   . ASN A 1 487 ? 40.516  9.215   76.108  1.00 56.14  ? 496  ASN A N   1 
ATOM   3245  C CA  . ASN A 1 487 ? 41.912  9.086   76.469  1.00 58.39  ? 496  ASN A CA  1 
ATOM   3246  C C   . ASN A 1 487 ? 42.337  10.066  77.561  1.00 59.60  ? 496  ASN A C   1 
ATOM   3247  O O   . ASN A 1 487 ? 43.247  9.793   78.325  1.00 61.08  ? 496  ASN A O   1 
ATOM   3248  C CB  . ASN A 1 487 ? 42.781  9.177   75.226  1.00 58.67  ? 496  ASN A CB  1 
ATOM   3249  C CG  . ASN A 1 487 ? 42.401  8.126   74.171  1.00 58.73  ? 496  ASN A CG  1 
ATOM   3250  O OD1 . ASN A 1 487 ? 42.216  6.944   74.487  1.00 59.39  ? 496  ASN A OD1 1 
ATOM   3251  N ND2 . ASN A 1 487 ? 42.277  8.561   72.912  1.00 59.35  ? 496  ASN A ND2 1 
ATOM   3252  N N   . GLU A 1 488 ? 41.653  11.199  77.645  1.00 59.24  ? 497  GLU A N   1 
ATOM   3253  C CA  . GLU A 1 488 ? 41.746  12.039  78.833  0.50 60.23  ? 497  GLU A CA  1 
ATOM   3254  C C   . GLU A 1 488 ? 41.702  11.108  80.018  1.00 61.09  ? 497  GLU A C   1 
ATOM   3255  O O   . GLU A 1 488 ? 42.608  11.093  80.821  1.00 62.77  ? 497  GLU A O   1 
ATOM   3256  C CB  . GLU A 1 488 ? 40.559  13.005  78.943  0.50 59.29  ? 497  GLU A CB  1 
ATOM   3257  C CG  . GLU A 1 488 ? 40.647  14.215  78.054  0.50 58.57  ? 497  GLU A CG  1 
ATOM   3258  C CD  . GLU A 1 488 ? 42.045  14.745  78.006  0.50 59.63  ? 497  GLU A CD  1 
ATOM   3259  O OE1 . GLU A 1 488 ? 42.886  14.252  78.793  0.50 60.07  ? 497  GLU A OE1 1 
ATOM   3260  O OE2 . GLU A 1 488 ? 42.295  15.638  77.173  0.50 59.70  ? 497  GLU A OE2 1 
ATOM   3261  N N   . LYS A 1 489 ? 40.642  10.310  80.092  1.00 60.37  ? 498  LYS A N   1 
ATOM   3262  C CA  . LYS A 1 489 ? 40.313  9.567   81.301  1.00 61.43  ? 498  LYS A CA  1 
ATOM   3263  C C   . LYS A 1 489 ? 41.290  8.461   81.579  1.00 62.80  ? 498  LYS A C   1 
ATOM   3264  O O   . LYS A 1 489 ? 41.696  8.276   82.719  1.00 64.29  ? 498  LYS A O   1 
ATOM   3265  C CB  . LYS A 1 489 ? 38.915  8.975   81.226  1.00 60.27  ? 498  LYS A CB  1 
ATOM   3266  C CG  . LYS A 1 489 ? 37.877  9.936   80.766  1.00 59.96  ? 498  LYS A CG  1 
ATOM   3267  C CD  . LYS A 1 489 ? 37.463  10.800  81.896  1.00 62.46  ? 498  LYS A CD  1 
ATOM   3268  C CE  . LYS A 1 489 ? 36.519  11.855  81.377  1.00 63.15  ? 498  LYS A CE  1 
ATOM   3269  N NZ  . LYS A 1 489 ? 36.141  12.746  82.511  1.00 66.23  ? 498  LYS A NZ  1 
ATOM   3270  N N   . ILE A 1 490 ? 41.659  7.704   80.559  1.00 62.81  ? 499  ILE A N   1 
ATOM   3271  C CA  . ILE A 1 490 ? 42.623  6.650   80.798  1.00 64.82  ? 499  ILE A CA  1 
ATOM   3272  C C   . ILE A 1 490 ? 43.928  7.298   81.261  1.00 67.44  ? 499  ILE A C   1 
ATOM   3273  O O   . ILE A 1 490 ? 44.410  6.996   82.354  1.00 68.73  ? 499  ILE A O   1 
ATOM   3274  C CB  . ILE A 1 490 ? 42.841  5.776   79.577  1.00 64.26  ? 499  ILE A CB  1 
ATOM   3275  C CG1 . ILE A 1 490 ? 41.493  5.311   79.023  1.00 61.76  ? 499  ILE A CG1 1 
ATOM   3276  C CG2 . ILE A 1 490 ? 43.739  4.599   79.938  1.00 65.69  ? 499  ILE A CG2 1 
ATOM   3277  C CD1 . ILE A 1 490 ? 41.512  4.991   77.529  1.00 59.96  ? 499  ILE A CD1 1 
ATOM   3278  N N   . ASN A 1 491 ? 44.465  8.207   80.441  1.00 68.65  ? 500  ASN A N   1 
ATOM   3279  C CA  . ASN A 1 491 ? 45.645  9.009   80.791  1.00 71.88  ? 500  ASN A CA  1 
ATOM   3280  C C   . ASN A 1 491 ? 45.606  9.529   82.235  1.00 71.79  ? 500  ASN A C   1 
ATOM   3281  O O   . ASN A 1 491 ? 46.618  9.528   82.949  1.00 73.42  ? 500  ASN A O   1 
ATOM   3282  C CB  . ASN A 1 491 ? 45.847  10.156  79.776  1.00 72.82  ? 500  ASN A CB  1 
ATOM   3283  C CG  . ASN A 1 491 ? 46.962  9.854   78.770  1.00 81.65  ? 500  ASN A CG  1 
ATOM   3284  O OD1 . ASN A 1 491 ? 47.432  8.711   78.710  1.00 83.22  ? 500  ASN A OD1 1 
ATOM   3285  N ND2 . ASN A 1 491 ? 47.405  10.873  77.984  1.00 96.01  ? 500  ASN A ND2 1 
ATOM   3286  N N   . GLN A 1 492 ? 44.414  9.939   82.651  1.00 69.87  ? 501  GLN A N   1 
ATOM   3287  C CA  . GLN A 1 492 ? 44.149  10.455  83.985  1.00 70.24  ? 501  GLN A CA  1 
ATOM   3288  C C   . GLN A 1 492 ? 44.246  9.325   85.007  1.00 70.35  ? 501  GLN A C   1 
ATOM   3289  O O   . GLN A 1 492 ? 44.856  9.470   86.084  1.00 71.61  ? 501  GLN A O   1 
ATOM   3290  C CB  . GLN A 1 492 ? 42.725  10.996  83.976  1.00 69.14  ? 501  GLN A CB  1 
ATOM   3291  C CG  . GLN A 1 492 ? 42.331  12.040  85.018  1.00 71.74  ? 501  GLN A CG  1 
ATOM   3292  C CD  . GLN A 1 492 ? 41.170  12.919  84.492  1.00 73.22  ? 501  GLN A CD  1 
ATOM   3293  O OE1 . GLN A 1 492 ? 40.118  12.415  84.030  1.00 72.28  ? 501  GLN A OE1 1 
ATOM   3294  N NE2 . GLN A 1 492 ? 41.374  14.237  84.531  1.00 75.19  ? 501  GLN A NE2 1 
ATOM   3295  N N   . SER A 1 493 ? 43.624  8.205   84.639  1.00 68.56  ? 502  SER A N   1 
ATOM   3296  C CA  . SER A 1 493 ? 43.492  7.034   85.480  1.00 68.45  ? 502  SER A CA  1 
ATOM   3297  C C   . SER A 1 493 ? 44.871  6.478   85.814  1.00 70.05  ? 502  SER A C   1 
ATOM   3298  O O   . SER A 1 493 ? 45.235  6.320   86.985  1.00 71.30  ? 502  SER A O   1 
ATOM   3299  C CB  . SER A 1 493 ? 42.655  5.988   84.745  1.00 67.05  ? 502  SER A CB  1 
ATOM   3300  O OG  . SER A 1 493 ? 42.265  4.965   85.622  1.00 67.28  ? 502  SER A OG  1 
ATOM   3301  N N   . LEU A 1 494 ? 45.643  6.206   84.772  1.00 69.68  ? 503  LEU A N   1 
ATOM   3302  C CA  . LEU A 1 494 ? 46.974  5.683   84.942  1.00 71.29  ? 503  LEU A CA  1 
ATOM   3303  C C   . LEU A 1 494 ? 47.783  6.523   85.908  1.00 72.79  ? 503  LEU A C   1 
ATOM   3304  O O   . LEU A 1 494 ? 48.451  5.987   86.780  1.00 74.47  ? 503  LEU A O   1 
ATOM   3305  C CB  . LEU A 1 494 ? 47.668  5.643   83.604  1.00 71.11  ? 503  LEU A CB  1 
ATOM   3306  C CG  . LEU A 1 494 ? 47.101  4.642   82.620  1.00 70.14  ? 503  LEU A CG  1 
ATOM   3307  C CD1 . LEU A 1 494 ? 47.915  4.761   81.364  1.00 71.02  ? 503  LEU A CD1 1 
ATOM   3308  C CD2 . LEU A 1 494 ? 47.157  3.227   83.164  1.00 71.35  ? 503  LEU A CD2 1 
ATOM   3309  N N   . ALA A 1 495 ? 47.701  7.842   85.745  1.00 72.30  ? 504  ALA A N   1 
ATOM   3310  C CA  . ALA A 1 495 ? 48.412  8.794   86.594  1.00 73.46  ? 504  ALA A CA  1 
ATOM   3311  C C   . ALA A 1 495 ? 47.948  8.699   88.041  1.00 73.75  ? 504  ALA A C   1 
ATOM   3312  O O   . ALA A 1 495 ? 48.749  8.870   88.962  1.00 75.61  ? 504  ALA A O   1 
ATOM   3313  C CB  . ALA A 1 495 ? 48.243  10.213  86.072  1.00 72.87  ? 504  ALA A CB  1 
ATOM   3314  N N   . PHE A 1 496 ? 46.665  8.421   88.253  1.00 71.77  ? 505  PHE A N   1 
ATOM   3315  C CA  . PHE A 1 496 ? 46.214  8.203   89.608  1.00 72.07  ? 505  PHE A CA  1 
ATOM   3316  C C   . PHE A 1 496 ? 46.904  6.991   90.210  1.00 73.25  ? 505  PHE A C   1 
ATOM   3317  O O   . PHE A 1 496 ? 47.407  7.072   91.319  1.00 74.85  ? 505  PHE A O   1 
ATOM   3318  C CB  . PHE A 1 496 ? 44.706  8.055   89.672  1.00 70.71  ? 505  PHE A CB  1 
ATOM   3319  C CG  . PHE A 1 496 ? 43.962  9.354   89.863  1.00 71.00  ? 505  PHE A CG  1 
ATOM   3320  C CD1 . PHE A 1 496 ? 43.175  9.877   88.840  1.00 70.98  ? 505  PHE A CD1 1 
ATOM   3321  C CD2 . PHE A 1 496 ? 44.020  10.039  91.070  1.00 72.56  ? 505  PHE A CD2 1 
ATOM   3322  C CE1 . PHE A 1 496 ? 42.470  11.070  89.019  1.00 70.78  ? 505  PHE A CE1 1 
ATOM   3323  C CE2 . PHE A 1 496 ? 43.322  11.230  91.255  1.00 72.25  ? 505  PHE A CE2 1 
ATOM   3324  C CZ  . PHE A 1 496 ? 42.547  11.742  90.237  1.00 70.98  ? 505  PHE A CZ  1 
ATOM   3325  N N   . ILE A 1 497 ? 46.958  5.883   89.476  1.00 72.80  ? 506  ILE A N   1 
ATOM   3326  C CA  . ILE A 1 497 ? 47.612  4.667   89.976  1.00 74.48  ? 506  ILE A CA  1 
ATOM   3327  C C   . ILE A 1 497 ? 49.096  4.893   90.251  1.00 77.18  ? 506  ILE A C   1 
ATOM   3328  O O   . ILE A 1 497 ? 49.586  4.570   91.340  1.00 78.71  ? 506  ILE A O   1 
ATOM   3329  C CB  . ILE A 1 497 ? 47.427  3.481   89.019  1.00 73.74  ? 506  ILE A CB  1 
ATOM   3330  C CG1 . ILE A 1 497 ? 45.961  3.121   88.916  1.00 72.03  ? 506  ILE A CG1 1 
ATOM   3331  C CG2 . ILE A 1 497 ? 48.199  2.254   89.494  1.00 75.09  ? 506  ILE A CG2 1 
ATOM   3332  C CD1 . ILE A 1 497 ? 45.398  2.562   90.189  1.00 72.71  ? 506  ILE A CD1 1 
ATOM   3333  N N   . ARG A 1 498 ? 49.797  5.435   89.245  1.00 77.89  ? 507  ARG A N   1 
ATOM   3334  C CA  . ARG A 1 498 ? 51.189  5.904   89.353  1.00 80.50  ? 507  ARG A CA  1 
ATOM   3335  C C   . ARG A 1 498 ? 51.450  6.473   90.762  1.00 81.71  ? 507  ARG A C   1 
ATOM   3336  O O   . ARG A 1 498 ? 52.390  6.079   91.444  1.00 83.28  ? 507  ARG A O   1 
ATOM   3337  C CB  . ARG A 1 498 ? 51.439  7.021   88.330  1.00 80.31  ? 507  ARG A CB  1 
ATOM   3338  C CG  . ARG A 1 498 ? 51.560  6.679   86.795  1.00 82.38  ? 507  ARG A CG  1 
ATOM   3339  C CD  . ARG A 1 498 ? 52.484  7.742   86.170  1.00 87.27  ? 507  ARG A CD  1 
ATOM   3340  N NE  . ARG A 1 498 ? 53.450  8.075   87.242  1.00 94.44  ? 507  ARG A NE  1 
ATOM   3341  C CZ  . ARG A 1 498 ? 54.336  9.078   87.252  1.00 97.50  ? 507  ARG A CZ  1 
ATOM   3342  N NH1 . ARG A 1 498 ? 54.420  9.910   86.200  1.00 97.33  ? 507  ARG A NH1 1 
ATOM   3343  N NH2 . ARG A 1 498 ? 55.142  9.239   88.331  1.00 99.10  ? 507  ARG A NH2 1 
ATOM   3344  N N   . LYS A 1 499 ? 50.575  7.395   91.172  1.00 80.75  ? 508  LYS A N   1 
ATOM   3345  C CA  . LYS A 1 499 ? 50.629  8.084   92.459  1.00 81.95  ? 508  LYS A CA  1 
ATOM   3346  C C   . LYS A 1 499 ? 50.413  7.112   93.618  1.00 82.47  ? 508  LYS A C   1 
ATOM   3347  O O   . LYS A 1 499 ? 51.102  7.185   94.653  1.00 84.35  ? 508  LYS A O   1 
ATOM   3348  C CB  . LYS A 1 499 ? 49.573  9.219   92.490  1.00 80.64  ? 508  LYS A CB  1 
ATOM   3349  C CG  . LYS A 1 499 ? 49.567  10.116  93.768  1.00 83.51  ? 508  LYS A CG  1 
ATOM   3350  C CD  . LYS A 1 499 ? 50.464  11.400  93.643  1.00 87.38  ? 508  LYS A CD  1 
ATOM   3351  C CE  . LYS A 1 499 ? 52.009  11.201  93.999  1.00 90.40  ? 508  LYS A CE  1 
ATOM   3352  N NZ  . LYS A 1 499 ? 52.358  10.911  95.455  1.00 90.81  ? 508  LYS A NZ  1 
ATOM   3353  N N   . SER A 1 500 ? 49.444  6.218   93.438  1.00 80.88  ? 509  SER A N   1 
ATOM   3354  C CA  . SER A 1 500 ? 49.127  5.210   94.435  1.00 81.45  ? 509  SER A CA  1 
ATOM   3355  C C   . SER A 1 500 ? 50.333  4.321   94.689  1.00 83.85  ? 509  SER A C   1 
ATOM   3356  O O   . SER A 1 500 ? 50.730  4.119   95.833  1.00 85.28  ? 509  SER A O   1 
ATOM   3357  C CB  . SER A 1 500 ? 47.949  4.369   93.967  1.00 79.56  ? 509  SER A CB  1 
ATOM   3358  O OG  . SER A 1 500 ? 47.607  3.397   94.927  1.00 79.72  ? 509  SER A OG  1 
ATOM   3359  N N   . ASP A 1 501 ? 50.927  3.816   93.612  1.00 84.52  ? 510  ASP A N   1 
ATOM   3360  C CA  . ASP A 1 501 ? 52.074  2.918   93.720  1.00 87.15  ? 510  ASP A CA  1 
ATOM   3361  C C   . ASP A 1 501 ? 53.260  3.554   94.437  1.00 89.42  ? 510  ASP A C   1 
ATOM   3362  O O   . ASP A 1 501 ? 53.859  2.917   95.287  1.00 91.43  ? 510  ASP A O   1 
ATOM   3363  C CB  . ASP A 1 501 ? 52.492  2.388   92.343  1.00 87.21  ? 510  ASP A CB  1 
ATOM   3364  C CG  . ASP A 1 501 ? 51.620  1.217   91.868  1.00 87.01  ? 510  ASP A CG  1 
ATOM   3365  O OD1 . ASP A 1 501 ? 51.493  0.203   92.595  1.00 89.00  ? 510  ASP A OD1 1 
ATOM   3366  O OD2 . ASP A 1 501 ? 51.067  1.308   90.751  1.00 86.02  ? 510  ASP A OD2 1 
ATOM   3367  N N   . GLU A 1 502 ? 53.585  4.803   94.105  1.00 89.63  ? 511  GLU A N   1 
ATOM   3368  C CA  . GLU A 1 502 ? 54.682  5.515   94.764  1.00 92.24  ? 511  GLU A CA  1 
ATOM   3369  C C   . GLU A 1 502 ? 54.510  5.408   96.262  1.00 93.07  ? 511  GLU A C   1 
ATOM   3370  O O   . GLU A 1 502 ? 55.438  5.030   96.999  1.00 95.49  ? 511  GLU A O   1 
ATOM   3371  C CB  . GLU A 1 502 ? 54.736  6.994   94.356  1.00 92.06  ? 511  GLU A CB  1 
ATOM   3372  C CG  . GLU A 1 502 ? 55.548  7.283   93.056  1.00 94.95  ? 511  GLU A CG  1 
ATOM   3373  C CD  . GLU A 1 502 ? 55.302  8.703   92.457  1.00 96.85  ? 511  GLU A CD  1 
ATOM   3374  O OE1 . GLU A 1 502 ? 55.369  9.678   93.255  1.00 98.87  ? 511  GLU A OE1 1 
ATOM   3375  O OE2 . GLU A 1 502 ? 55.053  8.840   91.208  1.00 94.69  ? 511  GLU A OE2 1 
ATOM   3376  N N   . LEU A 1 503 ? 53.305  5.707   96.720  1.00 91.17  ? 512  LEU A N   1 
ATOM   3377  C CA  . LEU A 1 503 ? 53.050  5.662   98.146  1.00 91.92  ? 512  LEU A CA  1 
ATOM   3378  C C   . LEU A 1 503 ? 53.375  4.315   98.751  1.00 93.16  ? 512  LEU A C   1 
ATOM   3379  O O   . LEU A 1 503 ? 53.876  4.242   99.864  1.00 95.24  ? 512  LEU A O   1 
ATOM   3380  C CB  . LEU A 1 503 ? 51.619  6.082   98.454  1.00 90.03  ? 512  LEU A CB  1 
ATOM   3381  C CG  . LEU A 1 503 ? 51.388  7.571   98.154  1.00 89.70  ? 512  LEU A CG  1 
ATOM   3382  C CD1 . LEU A 1 503 ? 49.885  7.955   98.173  1.00 87.77  ? 512  LEU A CD1 1 
ATOM   3383  C CD2 . LEU A 1 503 ? 52.212  8.428   99.128  1.00 91.78  ? 512  LEU A CD2 1 
ATOM   3384  N N   . LEU A 1 504 ? 53.140  3.252   97.999  1.00 92.40  ? 513  LEU A N   1 
ATOM   3385  C CA  . LEU A 1 504 ? 53.306  1.904   98.523  1.00 93.78  ? 513  LEU A CA  1 
ATOM   3386  C C   . LEU A 1 504 ? 54.743  1.399   98.511  1.00 96.75  ? 513  LEU A C   1 
ATOM   3387  O O   . LEU A 1 504 ? 55.142  0.633   99.396  1.00 98.35  ? 513  LEU A O   1 
ATOM   3388  C CB  . LEU A 1 504 ? 52.399  0.940   97.776  1.00 92.03  ? 513  LEU A CB  1 
ATOM   3389  C CG  . LEU A 1 504 ? 50.925  1.287   97.906  1.00 89.10  ? 513  LEU A CG  1 
ATOM   3390  C CD1 . LEU A 1 504 ? 50.204  0.839   96.679  1.00 88.03  ? 513  LEU A CD1 1 
ATOM   3391  C CD2 . LEU A 1 504 ? 50.358  0.621   99.104  1.00 88.57  ? 513  LEU A CD2 1 
ATOM   3392  N N   . HIS A 1 505 ? 55.517  1.821   97.516  1.00 97.67  ? 514  HIS A N   1 
ATOM   3393  C CA  . HIS A 1 505 ? 56.937  1.500   97.490  1.00 101.26 ? 514  HIS A CA  1 
ATOM   3394  C C   . HIS A 1 505 ? 57.651  2.365   98.526  1.00 103.57 ? 514  HIS A C   1 
ATOM   3395  O O   . HIS A 1 505 ? 58.889  2.405   98.623  1.00 106.03 ? 514  HIS A O   1 
ATOM   3396  C CB  . HIS A 1 505 ? 57.505  1.665   96.082  1.00 101.05 ? 514  HIS A CB  1 
ATOM   3397  C CG  . HIS A 1 505 ? 56.844  0.782   95.068  1.00 100.66 ? 514  HIS A CG  1 
ATOM   3398  N ND1 . HIS A 1 505 ? 56.575  -0.552  95.306  1.00 101.71 ? 514  HIS A ND1 1 
ATOM   3399  C CD2 . HIS A 1 505 ? 56.397  1.041   93.815  1.00 99.46  ? 514  HIS A CD2 1 
ATOM   3400  C CE1 . HIS A 1 505 ? 55.995  -1.075  94.242  1.00 100.33 ? 514  HIS A CE1 1 
ATOM   3401  N NE2 . HIS A 1 505 ? 55.873  -0.130  93.324  1.00 98.89  ? 514  HIS A NE2 1 
ATOM   3402  N N   . ASN A 1 506 ? 56.827  3.048   99.310  1.00 103.28 ? 515  ASN A N   1 
ATOM   3403  C CA  . ASN A 1 506 ? 57.272  3.767   100.484 1.00 105.60 ? 515  ASN A CA  1 
ATOM   3404  C C   . ASN A 1 506 ? 56.789  3.104   101.779 1.00 106.40 ? 515  ASN A C   1 
ATOM   3405  O O   . ASN A 1 506 ? 56.776  3.732   102.845 1.00 107.29 ? 515  ASN A O   1 
ATOM   3406  C CB  . ASN A 1 506 ? 56.809  5.221   100.406 1.00 104.52 ? 515  ASN A CB  1 
ATOM   3407  C CG  . ASN A 1 506 ? 57.971  6.188   100.355 1.00 106.88 ? 515  ASN A CG  1 
ATOM   3408  O OD1 . ASN A 1 506 ? 58.261  6.765   99.303  1.00 106.70 ? 515  ASN A OD1 1 
ATOM   3409  N ND2 . ASN A 1 506 ? 58.664  6.354   101.495 1.00 108.65 ? 515  ASN A ND2 1 
ATOM   3410  N N   . VAL A 1 507 ? 56.403  1.831   101.671 1.00 106.39 ? 516  VAL A N   1 
ATOM   3411  C CA  . VAL A 1 507 ? 55.883  1.051   102.810 1.00 107.00 ? 516  VAL A CA  1 
ATOM   3412  C C   . VAL A 1 507 ? 56.642  -0.298  102.989 1.00 109.30 ? 516  VAL A C   1 
ATOM   3413  O O   . VAL A 1 507 ? 56.722  -1.099  102.045 1.00 109.27 ? 516  VAL A O   1 
ATOM   3414  C CB  . VAL A 1 507 ? 54.347  0.851   102.668 1.00 104.39 ? 516  VAL A CB  1 
ATOM   3415  C CG1 . VAL A 1 507 ? 53.839  -0.219  103.620 1.00 104.77 ? 516  VAL A CG1 1 
ATOM   3416  C CG2 . VAL A 1 507 ? 53.624  2.163   102.886 1.00 102.24 ? 516  VAL A CG2 1 
ATOM   3417  N N   . ASN A 1 508 ? 57.194  -0.542  104.184 1.00 111.15 ? 517  ASN A N   1 
ATOM   3418  C CA  . ASN A 1 508 ? 58.122  -1.665  104.383 1.00 113.53 ? 517  ASN A CA  1 
ATOM   3419  C C   . ASN A 1 508 ? 58.410  -1.911  105.872 1.00 115.17 ? 517  ASN A C   1 
ATOM   3420  O O   . ASN A 1 508 ? 57.542  -1.720  106.724 1.00 113.97 ? 517  ASN A O   1 
ATOM   3421  C CB  . ASN A 1 508 ? 59.432  -1.418  103.563 1.00 115.15 ? 517  ASN A CB  1 
ATOM   3422  C CG  . ASN A 1 508 ? 60.321  -2.686  103.385 1.00 118.15 ? 517  ASN A CG  1 
ATOM   3423  O OD1 . ASN A 1 508 ? 60.303  -3.621  104.209 1.00 120.68 ? 517  ASN A OD1 1 
ATOM   3424  N ND2 . ASN A 1 508 ? 61.126  -2.690  102.310 1.00 118.46 ? 517  ASN A ND2 1 
ATOM   3425  N N   . GLN B 1 26  ? 26.204  -20.279 -13.983 1.00 104.60 ? 26   GLN B N   1 
ATOM   3426  C CA  . GLN B 1 26  ? 25.544  -18.937 -14.156 1.00 100.82 ? 26   GLN B CA  1 
ATOM   3427  C C   . GLN B 1 26  ? 25.714  -18.395 -15.582 1.00 100.75 ? 26   GLN B C   1 
ATOM   3428  O O   . GLN B 1 26  ? 26.782  -17.878 -15.952 1.00 101.37 ? 26   GLN B O   1 
ATOM   3429  C CB  . GLN B 1 26  ? 26.045  -17.941 -13.097 1.00 98.04  ? 26   GLN B CB  1 
ATOM   3430  C CG  . GLN B 1 26  ? 25.163  -17.854 -11.839 1.00 95.92  ? 26   GLN B CG  1 
ATOM   3431  C CD  . GLN B 1 26  ? 25.038  -19.160 -11.028 1.00 97.58  ? 26   GLN B CD  1 
ATOM   3432  O OE1 . GLN B 1 26  ? 25.140  -20.276 -11.552 1.00 100.54 ? 26   GLN B OE1 1 
ATOM   3433  N NE2 . GLN B 1 26  ? 24.784  -19.006 -9.736  1.00 95.47  ? 26   GLN B NE2 1 
ATOM   3434  N N   . ASN B 1 27  ? 24.660  -18.522 -16.385 1.00 99.96  ? 27   ASN B N   1 
ATOM   3435  C CA  . ASN B 1 27  ? 24.825  -18.284 -17.806 1.00 99.77  ? 27   ASN B CA  1 
ATOM   3436  C C   . ASN B 1 27  ? 23.985  -17.118 -18.296 1.00 95.16  ? 27   ASN B C   1 
ATOM   3437  O O   . ASN B 1 27  ? 23.102  -17.296 -19.150 1.00 95.37  ? 27   ASN B O   1 
ATOM   3438  C CB  . ASN B 1 27  ? 24.540  -19.558 -18.614 1.00 104.01 ? 27   ASN B CB  1 
ATOM   3439  C CG  . ASN B 1 27  ? 25.100  -19.494 -20.023 1.00 108.40 ? 27   ASN B CG  1 
ATOM   3440  O OD1 . ASN B 1 27  ? 26.305  -19.338 -20.218 1.00 110.92 ? 27   ASN B OD1 1 
ATOM   3441  N ND2 . ASN B 1 27  ? 24.227  -19.625 -21.015 1.00 112.89 ? 27   ASN B ND2 1 
ATOM   3442  N N   . ILE B 1 28  ? 24.262  -15.930 -17.752 1.00 90.21  ? 28   ILE B N   1 
ATOM   3443  C CA  . ILE B 1 28  ? 23.606  -14.705 -18.217 1.00 85.34  ? 28   ILE B CA  1 
ATOM   3444  C C   . ILE B 1 28  ? 24.376  -14.071 -19.353 1.00 84.76  ? 28   ILE B C   1 
ATOM   3445  O O   . ILE B 1 28  ? 25.613  -14.059 -19.360 1.00 85.58  ? 28   ILE B O   1 
ATOM   3446  C CB  . ILE B 1 28  ? 23.404  -13.684 -17.110 1.00 81.79  ? 28   ILE B CB  1 
ATOM   3447  C CG1 . ILE B 1 28  ? 24.594  -13.706 -16.137 1.00 83.10  ? 28   ILE B CG1 1 
ATOM   3448  C CG2 . ILE B 1 28  ? 22.100  -13.966 -16.381 1.00 79.41  ? 28   ILE B CG2 1 
ATOM   3449  C CD1 . ILE B 1 28  ? 25.820  -12.864 -16.562 1.00 84.07  ? 28   ILE B CD1 1 
ATOM   3450  N N   . THR B 1 29  ? 23.623  -13.563 -20.319 1.00 82.85  ? 29   THR B N   1 
ATOM   3451  C CA  . THR B 1 29  ? 24.197  -13.018 -21.520 1.00 82.58  ? 29   THR B CA  1 
ATOM   3452  C C   . THR B 1 29  ? 23.299  -11.915 -21.965 1.00 79.58  ? 29   THR B C   1 
ATOM   3453  O O   . THR B 1 29  ? 22.140  -11.815 -21.537 1.00 77.72  ? 29   THR B O   1 
ATOM   3454  C CB  . THR B 1 29  ? 24.226  -14.038 -22.657 1.00 85.64  ? 29   THR B CB  1 
ATOM   3455  O OG1 . THR B 1 29  ? 23.963  -15.350 -22.144 1.00 87.56  ? 29   THR B OG1 1 
ATOM   3456  C CG2 . THR B 1 29  ? 25.572  -13.998 -23.355 1.00 87.70  ? 29   THR B CG2 1 
ATOM   3457  N N   . GLU B 1 30  ? 23.852  -11.081 -22.827 1.00 78.86  ? 30   GLU B N   1 
ATOM   3458  C CA  . GLU B 1 30  ? 23.076  -10.111 -23.548 1.00 76.71  ? 30   GLU B CA  1 
ATOM   3459  C C   . GLU B 1 30  ? 23.406  -10.302 -25.011 1.00 78.30  ? 30   GLU B C   1 
ATOM   3460  O O   . GLU B 1 30  ? 24.554  -10.533 -25.361 1.00 80.35  ? 30   GLU B O   1 
ATOM   3461  C CB  . GLU B 1 30  ? 23.461  -8.719  -23.108 1.00 74.31  ? 30   GLU B CB  1 
ATOM   3462  C CG  . GLU B 1 30  ? 22.312  -7.786  -23.017 1.00 72.84  ? 30   GLU B CG  1 
ATOM   3463  C CD  . GLU B 1 30  ? 22.611  -6.666  -22.060 1.00 72.79  ? 30   GLU B CD  1 
ATOM   3464  O OE1 . GLU B 1 30  ? 23.721  -6.096  -22.139 1.00 73.62  ? 30   GLU B OE1 1 
ATOM   3465  O OE2 . GLU B 1 30  ? 21.748  -6.361  -21.212 1.00 72.28  ? 30   GLU B OE2 1 
ATOM   3466  N N   . GLU B 1 31  ? 22.394  -10.247 -25.859 1.00 77.59  ? 31   GLU B N   1 
ATOM   3467  C CA  . GLU B 1 31  ? 22.602  -10.260 -27.284 1.00 79.07  ? 31   GLU B CA  1 
ATOM   3468  C C   . GLU B 1 31  ? 21.962  -8.996  -27.839 1.00 76.35  ? 31   GLU B C   1 
ATOM   3469  O O   . GLU B 1 31  ? 20.827  -8.656  -27.485 1.00 74.46  ? 31   GLU B O   1 
ATOM   3470  C CB  . GLU B 1 31  ? 21.993  -11.516 -27.879 1.00 81.52  ? 31   GLU B CB  1 
ATOM   3471  C CG  . GLU B 1 31  ? 21.548  -11.339 -29.312 1.00 84.47  ? 31   GLU B CG  1 
ATOM   3472  C CD  . GLU B 1 31  ? 21.399  -12.653 -30.078 1.00 90.65  ? 31   GLU B CD  1 
ATOM   3473  O OE1 . GLU B 1 31  ? 21.232  -12.615 -31.328 1.00 91.90  ? 31   GLU B OE1 1 
ATOM   3474  O OE2 . GLU B 1 31  ? 21.445  -13.724 -29.436 1.00 93.97  ? 31   GLU B OE2 1 
ATOM   3475  N N   . PHE B 1 32  ? 22.698  -8.285  -28.682 1.00 76.22  ? 32   PHE B N   1 
ATOM   3476  C CA  . PHE B 1 32  ? 22.260  -6.995  -29.175 1.00 73.73  ? 32   PHE B CA  1 
ATOM   3477  C C   . PHE B 1 32  ? 21.666  -7.156  -30.550 1.00 74.91  ? 32   PHE B C   1 
ATOM   3478  O O   . PHE B 1 32  ? 22.165  -7.898  -31.363 1.00 77.70  ? 32   PHE B O   1 
ATOM   3479  C CB  . PHE B 1 32  ? 23.451  -6.048  -29.188 1.00 73.25  ? 32   PHE B CB  1 
ATOM   3480  C CG  . PHE B 1 32  ? 23.254  -4.820  -30.003 1.00 71.67  ? 32   PHE B CG  1 
ATOM   3481  C CD1 . PHE B 1 32  ? 22.319  -3.885  -29.659 1.00 69.25  ? 32   PHE B CD1 1 
ATOM   3482  C CD2 . PHE B 1 32  ? 24.039  -4.580  -31.105 1.00 74.14  ? 32   PHE B CD2 1 
ATOM   3483  C CE1 . PHE B 1 32  ? 22.157  -2.736  -30.426 1.00 68.57  ? 32   PHE B CE1 1 
ATOM   3484  C CE2 . PHE B 1 32  ? 23.884  -3.430  -31.871 1.00 73.53  ? 32   PHE B CE2 1 
ATOM   3485  C CZ  . PHE B 1 32  ? 22.948  -2.512  -31.534 1.00 70.28  ? 32   PHE B CZ  1 
ATOM   3486  N N   . TYR B 1 33  ? 20.582  -6.458  -30.808 1.00 73.17  ? 33   TYR B N   1 
ATOM   3487  C CA  . TYR B 1 33  ? 19.937  -6.540  -32.096 1.00 74.29  ? 33   TYR B CA  1 
ATOM   3488  C C   . TYR B 1 33  ? 20.033  -5.206  -32.813 1.00 73.12  ? 33   TYR B C   1 
ATOM   3489  O O   . TYR B 1 33  ? 19.157  -4.347  -32.672 1.00 71.15  ? 33   TYR B O   1 
ATOM   3490  C CB  . TYR B 1 33  ? 18.481  -6.969  -31.933 1.00 73.48  ? 33   TYR B CB  1 
ATOM   3491  C CG  . TYR B 1 33  ? 18.338  -8.366  -31.396 1.00 76.10  ? 33   TYR B CG  1 
ATOM   3492  C CD1 . TYR B 1 33  ? 18.113  -8.598  -30.047 1.00 76.10  ? 33   TYR B CD1 1 
ATOM   3493  C CD2 . TYR B 1 33  ? 18.440  -9.461  -32.237 1.00 80.92  ? 33   TYR B CD2 1 
ATOM   3494  C CE1 . TYR B 1 33  ? 17.981  -9.893  -29.552 1.00 78.49  ? 33   TYR B CE1 1 
ATOM   3495  C CE2 . TYR B 1 33  ? 18.309  -10.760 -31.756 1.00 83.61  ? 33   TYR B CE2 1 
ATOM   3496  C CZ  . TYR B 1 33  ? 18.079  -10.968 -30.412 1.00 82.03  ? 33   TYR B CZ  1 
ATOM   3497  O OH  . TYR B 1 33  ? 17.952  -12.251 -29.933 1.00 84.68  ? 33   TYR B OH  1 
ATOM   3498  N N   . GLN B 1 34  ? 21.101  -5.050  -33.588 1.00 74.72  ? 34   GLN B N   1 
ATOM   3499  C CA  . GLN B 1 34  ? 21.376  -3.823  -34.319 1.00 73.98  ? 34   GLN B CA  1 
ATOM   3500  C C   . GLN B 1 34  ? 20.237  -3.323  -35.193 1.00 72.83  ? 34   GLN B C   1 
ATOM   3501  O O   . GLN B 1 34  ? 20.112  -2.121  -35.399 1.00 71.35  ? 34   GLN B O   1 
ATOM   3502  C CB  . GLN B 1 34  ? 22.587  -4.012  -35.196 1.00 76.76  ? 34   GLN B CB  1 
ATOM   3503  C CG  . GLN B 1 34  ? 23.045  -2.754  -35.862 1.00 77.45  ? 34   GLN B CG  1 
ATOM   3504  C CD  . GLN B 1 34  ? 24.441  -2.924  -36.397 1.00 82.43  ? 34   GLN B CD  1 
ATOM   3505  O OE1 . GLN B 1 34  ? 24.653  -3.503  -37.488 1.00 85.54  ? 34   GLN B OE1 1 
ATOM   3506  N NE2 . GLN B 1 34  ? 25.428  -2.447  -35.618 1.00 82.83  ? 34   GLN B NE2 1 
ATOM   3507  N N   . SER B 1 35  ? 19.420  -4.237  -35.711 1.00 73.68  ? 35   SER B N   1 
ATOM   3508  C CA  . SER B 1 35  ? 18.308  -3.883  -36.609 1.00 72.95  ? 35   SER B CA  1 
ATOM   3509  C C   . SER B 1 35  ? 17.037  -3.359  -35.898 1.00 69.94  ? 35   SER B C   1 
ATOM   3510  O O   . SER B 1 35  ? 16.027  -3.040  -36.532 1.00 69.27  ? 35   SER B O   1 
ATOM   3511  C CB  . SER B 1 35  ? 17.965  -5.091  -37.485 1.00 75.42  ? 35   SER B CB  1 
ATOM   3512  O OG  . SER B 1 35  ? 17.786  -6.240  -36.678 1.00 76.25  ? 35   SER B OG  1 
ATOM   3513  N N   . THR B 1 36  ? 17.101  -3.280  -34.580 1.00 68.07  ? 36   THR B N   1 
ATOM   3514  C CA  . THR B 1 36  ? 15.965  -2.926  -33.771 1.00 65.49  ? 36   THR B CA  1 
ATOM   3515  C C   . THR B 1 36  ? 16.532  -2.121  -32.645 1.00 63.41  ? 36   THR B C   1 
ATOM   3516  O O   . THR B 1 36  ? 15.891  -1.897  -31.650 1.00 61.54  ? 36   THR B O   1 
ATOM   3517  C CB  . THR B 1 36  ? 15.318  -4.177  -33.200 1.00 66.24  ? 36   THR B CB  1 
ATOM   3518  O OG1 . THR B 1 36  ? 14.945  -5.026  -34.275 1.00 69.89  ? 36   THR B OG1 1 
ATOM   3519  C CG2 . THR B 1 36  ? 14.074  -3.860  -32.436 1.00 64.22  ? 36   THR B CG2 1 
ATOM   3520  N N   . CYS B 1 37  ? 17.766  -1.688  -32.797 1.00 64.08  ? 37   CYS B N   1 
ATOM   3521  C CA  . CYS B 1 37  ? 18.429  -0.939  -31.753 1.00 62.75  ? 37   CYS B CA  1 
ATOM   3522  C C   . CYS B 1 37  ? 17.985  -1.351  -30.359 1.00 61.13  ? 37   CYS B C   1 
ATOM   3523  O O   . CYS B 1 37  ? 17.645  -0.502  -29.548 1.00 59.41  ? 37   CYS B O   1 
ATOM   3524  C CB  . CYS B 1 37  ? 18.208  0.550   -31.956 1.00 60.99  ? 37   CYS B CB  1 
ATOM   3525  S SG  . CYS B 1 37  ? 19.572  1.440   -31.317 1.00 62.64  ? 37   CYS B SG  1 
ATOM   3526  N N   . SER B 1 38  ? 17.990  -2.657  -30.098 1.00 62.18  ? 38   SER B N   1 
ATOM   3527  C CA  . SER B 1 38  ? 17.523  -3.207  -28.827 1.00 60.86  ? 38   SER B CA  1 
ATOM   3528  C C   . SER B 1 38  ? 18.383  -4.346  -28.311 1.00 62.15  ? 38   SER B C   1 
ATOM   3529  O O   . SER B 1 38  ? 19.026  -5.038  -29.071 1.00 64.44  ? 38   SER B O   1 
ATOM   3530  C CB  . SER B 1 38  ? 16.057  -3.658  -28.932 1.00 60.71  ? 38   SER B CB  1 
ATOM   3531  O OG  . SER B 1 38  ? 15.815  -4.487  -30.053 1.00 62.99  ? 38   SER B OG  1 
ATOM   3532  N N   . ALA B 1 39  ? 18.377  -4.552  -27.008 1.00 60.82  ? 39   ALA B N   1 
ATOM   3533  C CA  . ALA B 1 39  ? 19.221  -5.561  -26.413 1.00 62.26  ? 39   ALA B CA  1 
ATOM   3534  C C   . ALA B 1 39  ? 18.434  -6.419  -25.459 1.00 62.09  ? 39   ALA B C   1 
ATOM   3535  O O   . ALA B 1 39  ? 17.583  -5.914  -24.709 1.00 60.19  ? 39   ALA B O   1 
ATOM   3536  C CB  . ALA B 1 39  ? 20.329  -4.896  -25.676 1.00 61.50  ? 39   ALA B CB  1 
ATOM   3537  N N   . VAL B 1 40  ? 18.738  -7.708  -25.455 1.00 64.14  ? 40   VAL B N   1 
ATOM   3538  C CA  . VAL B 1 40  ? 18.089  -8.596  -24.515 1.00 64.26  ? 40   VAL B CA  1 
ATOM   3539  C C   . VAL B 1 40  ? 19.051  -9.325  -23.606 1.00 65.61  ? 40   VAL B C   1 
ATOM   3540  O O   . VAL B 1 40  ? 20.044  -9.852  -24.048 1.00 67.79  ? 40   VAL B O   1 
ATOM   3541  C CB  . VAL B 1 40  ? 17.236  -9.613  -25.224 1.00 65.89  ? 40   VAL B CB  1 
ATOM   3542  C CG1 . VAL B 1 40  ? 16.746  -10.639 -24.237 1.00 66.83  ? 40   VAL B CG1 1 
ATOM   3543  C CG2 . VAL B 1 40  ? 16.059  -8.933  -25.887 1.00 64.52  ? 40   VAL B CG2 1 
ATOM   3544  N N   . SER B 1 41  ? 18.730  -9.346  -22.322 1.00 64.63  ? 41   SER B N   1 
ATOM   3545  C CA  . SER B 1 41  ? 19.513  -10.081 -21.340 1.00 66.12  ? 41   SER B CA  1 
ATOM   3546  C C   . SER B 1 41  ? 18.852  -11.427 -21.163 1.00 68.03  ? 41   SER B C   1 
ATOM   3547  O O   . SER B 1 41  ? 17.663  -11.495 -20.874 1.00 66.96  ? 41   SER B O   1 
ATOM   3548  C CB  . SER B 1 41  ? 19.533  -9.365  -19.975 1.00 63.89  ? 41   SER B CB  1 
ATOM   3549  O OG  . SER B 1 41  ? 19.707  -7.960  -20.072 1.00 62.37  ? 41   SER B OG  1 
ATOM   3550  N N   . LYS B 1 42  ? 19.624  -12.493 -21.300 1.00 71.05  ? 42   LYS B N   1 
ATOM   3551  C CA  . LYS B 1 42  ? 19.047  -13.829 -21.344 1.00 73.96  ? 42   LYS B CA  1 
ATOM   3552  C C   . LYS B 1 42  ? 19.622  -14.729 -20.263 1.00 75.18  ? 42   LYS B C   1 
ATOM   3553  O O   . LYS B 1 42  ? 20.669  -14.415 -19.687 1.00 74.77  ? 42   LYS B O   1 
ATOM   3554  C CB  . LYS B 1 42  ? 19.299  -14.481 -22.713 1.00 77.11  ? 42   LYS B CB  1 
ATOM   3555  C CG  . LYS B 1 42  ? 18.852  -13.680 -23.930 1.00 77.97  ? 42   LYS B CG  1 
ATOM   3556  C CD  . LYS B 1 42  ? 19.349  -14.324 -25.223 1.00 84.18  ? 42   LYS B CD  1 
ATOM   3557  C CE  . LYS B 1 42  ? 18.876  -13.545 -26.448 1.00 84.51  ? 42   LYS B CE  1 
ATOM   3558  N NZ  . LYS B 1 42  ? 19.012  -14.338 -27.700 1.00 88.75  ? 42   LYS B NZ  1 
ATOM   3559  N N   . GLY B 1 43  ? 18.938  -15.853 -20.014 1.00 76.84  ? 43   GLY B N   1 
ATOM   3560  C CA  . GLY B 1 43  ? 19.439  -16.914 -19.121 1.00 78.60  ? 43   GLY B CA  1 
ATOM   3561  C C   . GLY B 1 43  ? 18.997  -16.807 -17.665 1.00 76.79  ? 43   GLY B C   1 
ATOM   3562  O O   . GLY B 1 43  ? 19.694  -17.265 -16.747 1.00 77.50  ? 43   GLY B O   1 
ATOM   3563  N N   . TYR B 1 44  ? 17.833  -16.199 -17.456 1.00 74.36  ? 44   TYR B N   1 
ATOM   3564  C CA  . TYR B 1 44  ? 17.296  -16.013 -16.133 1.00 72.15  ? 44   TYR B CA  1 
ATOM   3565  C C   . TYR B 1 44  ? 16.229  -17.029 -15.902 1.00 73.58  ? 44   TYR B C   1 
ATOM   3566  O O   . TYR B 1 44  ? 15.630  -17.552 -16.854 1.00 75.52  ? 44   TYR B O   1 
ATOM   3567  C CB  . TYR B 1 44  ? 16.683  -14.643 -16.020 1.00 68.72  ? 44   TYR B CB  1 
ATOM   3568  C CG  . TYR B 1 44  ? 17.702  -13.555 -16.029 1.00 66.94  ? 44   TYR B CG  1 
ATOM   3569  C CD1 . TYR B 1 44  ? 17.885  -12.770 -17.163 1.00 66.87  ? 44   TYR B CD1 1 
ATOM   3570  C CD2 . TYR B 1 44  ? 18.489  -13.305 -14.903 1.00 65.55  ? 44   TYR B CD2 1 
ATOM   3571  C CE1 . TYR B 1 44  ? 18.822  -11.743 -17.176 1.00 65.87  ? 44   TYR B CE1 1 
ATOM   3572  C CE2 . TYR B 1 44  ? 19.434  -12.288 -14.899 1.00 64.75  ? 44   TYR B CE2 1 
ATOM   3573  C CZ  . TYR B 1 44  ? 19.597  -11.505 -16.039 1.00 65.21  ? 44   TYR B CZ  1 
ATOM   3574  O OH  . TYR B 1 44  ? 20.530  -10.482 -16.045 1.00 65.00  ? 44   TYR B OH  1 
ATOM   3575  N N   . LEU B 1 45  ? 15.984  -17.292 -14.626 1.00 72.68  ? 45   LEU B N   1 
ATOM   3576  C CA  . LEU B 1 45  ? 15.005  -18.293 -14.242 1.00 73.75  ? 45   LEU B CA  1 
ATOM   3577  C C   . LEU B 1 45  ? 13.886  -17.760 -13.362 1.00 71.24  ? 45   LEU B C   1 
ATOM   3578  O O   . LEU B 1 45  ? 14.109  -17.174 -12.292 1.00 69.33  ? 45   LEU B O   1 
ATOM   3579  C CB  . LEU B 1 45  ? 15.689  -19.498 -13.604 1.00 76.43  ? 45   LEU B CB  1 
ATOM   3580  C CG  . LEU B 1 45  ? 16.669  -20.199 -14.541 1.00 79.05  ? 45   LEU B CG  1 
ATOM   3581  C CD1 . LEU B 1 45  ? 17.666  -21.063 -13.781 1.00 81.29  ? 45   LEU B CD1 1 
ATOM   3582  C CD2 . LEU B 1 45  ? 15.895  -21.009 -15.584 1.00 81.92  ? 45   LEU B CD2 1 
ATOM   3583  N N   . SER B 1 46  ? 12.676  -18.006 -13.845 1.00 71.26  ? 46   SER B N   1 
ATOM   3584  C CA  . SER B 1 46  ? 11.454  -17.475 -13.284 1.00 68.91  ? 46   SER B CA  1 
ATOM   3585  C C   . SER B 1 46  ? 11.091  -18.021 -11.932 1.00 69.27  ? 46   SER B C   1 
ATOM   3586  O O   . SER B 1 46  ? 11.434  -19.144 -11.556 1.00 71.73  ? 46   SER B O   1 
ATOM   3587  C CB  . SER B 1 46  ? 10.301  -17.857 -14.188 1.00 69.85  ? 46   SER B CB  1 
ATOM   3588  O OG  . SER B 1 46  ? 10.113  -19.259 -14.115 1.00 72.53  ? 46   SER B OG  1 
ATOM   3589  N N   . ALA B 1 47  ? 10.334  -17.188 -11.243 1.00 66.75  ? 47   ALA B N   1 
ATOM   3590  C CA  . ALA B 1 47  ? 9.554   -17.548 -10.083 1.00 66.52  ? 47   ALA B CA  1 
ATOM   3591  C C   . ALA B 1 47  ? 8.442   -16.485 -10.064 1.00 63.74  ? 47   ALA B C   1 
ATOM   3592  O O   . ALA B 1 47  ? 8.713   -15.277 -9.959  1.00 61.41  ? 47   ALA B O   1 
ATOM   3593  C CB  . ALA B 1 47  ? 10.406  -17.474 -8.848  1.00 65.88  ? 47   ALA B CB  1 
ATOM   3594  N N   . LEU B 1 48  ? 7.195   -16.907 -10.231 1.00 63.97  ? 48   LEU B N   1 
ATOM   3595  C CA  . LEU B 1 48  ? 6.141   -15.927 -10.421 1.00 61.19  ? 48   LEU B CA  1 
ATOM   3596  C C   . LEU B 1 48  ? 5.061   -16.057 -9.378  1.00 61.10  ? 48   LEU B C   1 
ATOM   3597  O O   . LEU B 1 48  ? 4.418   -17.097 -9.283  1.00 63.61  ? 48   LEU B O   1 
ATOM   3598  C CB  . LEU B 1 48  ? 5.523   -16.070 -11.796 1.00 61.83  ? 48   LEU B CB  1 
ATOM   3599  C CG  . LEU B 1 48  ? 6.389   -16.351 -13.008 1.00 62.19  ? 48   LEU B CG  1 
ATOM   3600  C CD1 . LEU B 1 48  ? 5.544   -16.074 -14.204 1.00 61.23  ? 48   LEU B CD1 1 
ATOM   3601  C CD2 . LEU B 1 48  ? 7.584   -15.466 -13.075 1.00 61.22  ? 48   LEU B CD2 1 
ATOM   3602  N N   . ARG B 1 49  ? 4.854   -14.994 -8.608  1.00 58.46  ? 49   ARG B N   1 
ATOM   3603  C CA  . ARG B 1 49  ? 3.819   -14.970 -7.583  1.00 58.23  ? 49   ARG B CA  1 
ATOM   3604  C C   . ARG B 1 49  ? 2.438   -15.178 -8.181  1.00 59.37  ? 49   ARG B C   1 
ATOM   3605  O O   . ARG B 1 49  ? 2.053   -14.509 -9.136  1.00 58.40  ? 49   ARG B O   1 
ATOM   3606  C CB  . ARG B 1 49  ? 3.834   -13.634 -6.837  1.00 55.20  ? 49   ARG B CB  1 
ATOM   3607  C CG  . ARG B 1 49  ? 3.588   -13.742 -5.328  1.00 54.12  ? 49   ARG B CG  1 
ATOM   3608  C CD  . ARG B 1 49  ? 2.733   -12.595 -4.803  1.00 51.53  ? 49   ARG B CD  1 
ATOM   3609  N NE  . ARG B 1 49  ? 1.326   -12.947 -4.950  1.00 56.54  ? 49   ARG B NE  1 
ATOM   3610  C CZ  . ARG B 1 49  ? 0.436   -12.275 -5.678  1.00 58.82  ? 49   ARG B CZ  1 
ATOM   3611  N NH1 . ARG B 1 49  ? 0.794   -11.150 -6.290  1.00 56.71  ? 49   ARG B NH1 1 
ATOM   3612  N NH2 . ARG B 1 49  ? -0.823  -12.726 -5.772  1.00 61.87  ? 49   ARG B NH2 1 
ATOM   3613  N N   . THR B 1 50  ? 1.697   -16.109 -7.604  1.00 61.53  ? 50   THR B N   1 
ATOM   3614  C CA  . THR B 1 50  ? 0.315   -16.276 -7.977  1.00 62.72  ? 50   THR B CA  1 
ATOM   3615  C C   . THR B 1 50  ? -0.584  -16.370 -6.758  1.00 63.37  ? 50   THR B C   1 
ATOM   3616  O O   . THR B 1 50  ? -1.784  -16.528 -6.904  1.00 64.79  ? 50   THR B O   1 
ATOM   3617  C CB  . THR B 1 50  ? 0.103   -17.510 -8.861  1.00 65.49  ? 50   THR B CB  1 
ATOM   3618  O OG1 . THR B 1 50  ? 0.971   -18.558 -8.430  1.00 66.94  ? 50   THR B OG1 1 
ATOM   3619  C CG2 . THR B 1 50  ? 0.420   -17.199 -10.283 1.00 65.37  ? 50   THR B CG2 1 
ATOM   3620  N N   . GLY B 1 51  ? -0.036  -16.280 -5.558  1.00 62.56  ? 51   GLY B N   1 
ATOM   3621  C CA  . GLY B 1 51  ? -0.891  -16.425 -4.414  1.00 63.34  ? 51   GLY B CA  1 
ATOM   3622  C C   . GLY B 1 51  ? -0.154  -16.080 -3.180  1.00 62.23  ? 51   GLY B C   1 
ATOM   3623  O O   . GLY B 1 51  ? 1.022   -15.756 -3.231  1.00 61.14  ? 51   GLY B O   1 
ATOM   3624  N N   . TRP B 1 52  ? -0.855  -16.155 -2.062  1.00 62.83  ? 52   TRP B N   1 
ATOM   3625  C CA  . TRP B 1 52  ? -0.281  -15.764 -0.792  1.00 61.64  ? 52   TRP B CA  1 
ATOM   3626  C C   . TRP B 1 52  ? -0.420  -16.840 0.224   1.00 63.86  ? 52   TRP B C   1 
ATOM   3627  O O   . TRP B 1 52  ? -1.370  -17.612 0.199   1.00 66.17  ? 52   TRP B O   1 
ATOM   3628  C CB  . TRP B 1 52  ? -0.975  -14.531 -0.246  1.00 59.68  ? 52   TRP B CB  1 
ATOM   3629  C CG  . TRP B 1 52  ? -0.798  -13.349 -1.108  1.00 58.39  ? 52   TRP B CG  1 
ATOM   3630  C CD1 . TRP B 1 52  ? -1.723  -12.808 -1.952  1.00 59.30  ? 52   TRP B CD1 1 
ATOM   3631  C CD2 . TRP B 1 52  ? 0.379   -12.553 -1.240  1.00 56.60  ? 52   TRP B CD2 1 
ATOM   3632  N NE1 . TRP B 1 52  ? -1.196  -11.713 -2.599  1.00 56.67  ? 52   TRP B NE1 1 
ATOM   3633  C CE2 . TRP B 1 52  ? 0.093   -11.539 -2.181  1.00 55.15  ? 52   TRP B CE2 1 
ATOM   3634  C CE3 . TRP B 1 52  ? 1.647   -12.597 -0.656  1.00 55.90  ? 52   TRP B CE3 1 
ATOM   3635  C CZ2 . TRP B 1 52  ? 1.023   -10.586 -2.553  1.00 52.91  ? 52   TRP B CZ2 1 
ATOM   3636  C CZ3 . TRP B 1 52  ? 2.575   -11.642 -1.020  1.00 53.72  ? 52   TRP B CZ3 1 
ATOM   3637  C CH2 . TRP B 1 52  ? 2.260   -10.647 -1.964  1.00 52.46  ? 52   TRP B CH2 1 
ATOM   3638  N N   . TYR B 1 53  ? 0.528   -16.859 1.145   1.00 63.45  ? 53   TYR B N   1 
ATOM   3639  C CA  . TYR B 1 53  ? 0.510   -17.792 2.251   1.00 65.84  ? 53   TYR B CA  1 
ATOM   3640  C C   . TYR B 1 53  ? 0.463   -17.012 3.574   1.00 64.26  ? 53   TYR B C   1 
ATOM   3641  O O   . TYR B 1 53  ? 1.389   -16.278 3.906   1.00 62.43  ? 53   TYR B O   1 
ATOM   3642  C CB  . TYR B 1 53  ? 1.733   -18.705 2.156   1.00 67.27  ? 53   TYR B CB  1 
ATOM   3643  C CG  . TYR B 1 53  ? 1.890   -19.686 3.285   1.00 69.83  ? 53   TYR B CG  1 
ATOM   3644  C CD1 . TYR B 1 53  ? 1.326   -20.946 3.218   1.00 74.27  ? 53   TYR B CD1 1 
ATOM   3645  C CD2 . TYR B 1 53  ? 2.628   -19.353 4.414   1.00 69.17  ? 53   TYR B CD2 1 
ATOM   3646  C CE1 . TYR B 1 53  ? 1.484   -21.847 4.255   1.00 77.29  ? 53   TYR B CE1 1 
ATOM   3647  C CE2 . TYR B 1 53  ? 2.791   -20.241 5.451   1.00 71.83  ? 53   TYR B CE2 1 
ATOM   3648  C CZ  . TYR B 1 53  ? 2.217   -21.482 5.369   1.00 75.69  ? 53   TYR B CZ  1 
ATOM   3649  O OH  . TYR B 1 53  ? 2.385   -22.351 6.416   1.00 78.10  ? 53   TYR B OH  1 
ATOM   3650  N N   . THR B 1 54  ? -0.642  -17.176 4.294   1.00 65.54  ? 54   THR B N   1 
ATOM   3651  C CA  . THR B 1 54  ? -0.925  -16.521 5.565   1.00 64.77  ? 54   THR B CA  1 
ATOM   3652  C C   . THR B 1 54  ? -0.236  -17.242 6.692   1.00 65.78  ? 54   THR B C   1 
ATOM   3653  O O   . THR B 1 54  ? -0.108  -18.456 6.632   1.00 68.84  ? 54   THR B O   1 
ATOM   3654  C CB  . THR B 1 54  ? -2.445  -16.626 5.804   1.00 66.41  ? 54   THR B CB  1 
ATOM   3655  O OG1 . THR B 1 54  ? -3.071  -15.489 5.202   1.00 65.71  ? 54   THR B OG1 1 
ATOM   3656  C CG2 . THR B 1 54  ? -2.848  -16.748 7.315   1.00 68.00  ? 54   THR B CG2 1 
ATOM   3657  N N   . SER B 1 55  ? 0.201   -16.516 7.718   1.00 63.94  ? 55   SER B N   1 
ATOM   3658  C CA  . SER B 1 55  ? 0.513   -17.141 9.014   1.00 65.40  ? 55   SER B CA  1 
ATOM   3659  C C   . SER B 1 55  ? 0.484   -16.207 10.204  1.00 63.81  ? 55   SER B C   1 
ATOM   3660  O O   . SER B 1 55  ? 0.953   -15.069 10.161  1.00 61.51  ? 55   SER B O   1 
ATOM   3661  C CB  . SER B 1 55  ? 1.846   -17.878 9.041   1.00 66.17  ? 55   SER B CB  1 
ATOM   3662  O OG  . SER B 1 55  ? 2.138   -18.274 10.385  1.00 66.84  ? 55   SER B OG  1 
ATOM   3663  N N   . VAL B 1 56  ? 0.003   -16.749 11.305  1.00 65.57  ? 56   VAL B N   1 
ATOM   3664  C CA  . VAL B 1 56  ? -0.450  -15.935 12.392  1.00 64.37  ? 56   VAL B CA  1 
ATOM   3665  C C   . VAL B 1 56  ? 0.473   -16.062 13.550  1.00 63.77  ? 56   VAL B C   1 
ATOM   3666  O O   . VAL B 1 56  ? 0.451   -17.049 14.288  1.00 66.08  ? 56   VAL B O   1 
ATOM   3667  C CB  . VAL B 1 56  ? -1.825  -16.379 12.848  1.00 66.71  ? 56   VAL B CB  1 
ATOM   3668  C CG1 . VAL B 1 56  ? -2.497  -15.238 13.582  1.00 64.95  ? 56   VAL B CG1 1 
ATOM   3669  C CG2 . VAL B 1 56  ? -2.670  -16.896 11.636  1.00 69.23  ? 56   VAL B CG2 1 
ATOM   3670  N N   . ILE B 1 57  ? 1.263   -15.027 13.729  1.00 60.80  ? 57   ILE B N   1 
ATOM   3671  C CA  . ILE B 1 57  ? 2.256   -15.055 14.755  1.00 60.00  ? 57   ILE B CA  1 
ATOM   3672  C C   . ILE B 1 57  ? 1.790   -14.313 15.996  1.00 59.03  ? 57   ILE B C   1 
ATOM   3673  O O   . ILE B 1 57  ? 1.325   -13.180 15.909  1.00 57.24  ? 57   ILE B O   1 
ATOM   3674  C CB  . ILE B 1 57  ? 3.533   -14.530 14.204  1.00 57.80  ? 57   ILE B CB  1 
ATOM   3675  C CG1 . ILE B 1 57  ? 3.970   -15.490 13.123  1.00 59.75  ? 57   ILE B CG1 1 
ATOM   3676  C CG2 . ILE B 1 57  ? 4.576   -14.520 15.249  1.00 57.34  ? 57   ILE B CG2 1 
ATOM   3677  C CD1 . ILE B 1 57  ? 4.798   -14.871 12.108  1.00 59.85  ? 57   ILE B CD1 1 
ATOM   3678  N N   . THR B 1 58  ? 1.910   -14.964 17.150  1.00 60.37  ? 58   THR B N   1 
ATOM   3679  C CA  . THR B 1 58  ? 1.382   -14.429 18.396  1.00 60.17  ? 58   THR B CA  1 
ATOM   3680  C C   . THR B 1 58  ? 2.487   -14.366 19.394  1.00 59.69  ? 58   THR B C   1 
ATOM   3681  O O   . THR B 1 58  ? 3.218   -15.347 19.558  1.00 61.42  ? 58   THR B O   1 
ATOM   3682  C CB  . THR B 1 58  ? 0.353   -15.358 18.969  1.00 62.66  ? 58   THR B CB  1 
ATOM   3683  O OG1 . THR B 1 58  ? -0.214  -16.120 17.904  1.00 65.47  ? 58   THR B OG1 1 
ATOM   3684  C CG2 . THR B 1 58  ? -0.724  -14.585 19.661  1.00 62.03  ? 58   THR B CG2 1 
ATOM   3685  N N   . ILE B 1 59  ? 2.612   -13.229 20.072  1.00 58.06  ? 59   ILE B N   1 
ATOM   3686  C CA  . ILE B 1 59  ? 3.753   -13.024 20.958  1.00 57.54  ? 59   ILE B CA  1 
ATOM   3687  C C   . ILE B 1 59  ? 3.352   -12.558 22.321  1.00 58.03  ? 59   ILE B C   1 
ATOM   3688  O O   . ILE B 1 59  ? 2.720   -11.528 22.454  1.00 56.93  ? 59   ILE B O   1 
ATOM   3689  C CB  . ILE B 1 59  ? 4.757   -12.054 20.361  1.00 54.62  ? 59   ILE B CB  1 
ATOM   3690  C CG1 . ILE B 1 59  ? 5.370   -12.689 19.123  1.00 55.04  ? 59   ILE B CG1 1 
ATOM   3691  C CG2 . ILE B 1 59  ? 5.838   -11.735 21.359  1.00 53.18  ? 59   ILE B CG2 1 
ATOM   3692  C CD1 . ILE B 1 59  ? 6.573   -12.008 18.630  1.00 54.51  ? 59   ILE B CD1 1 
ATOM   3693  N N   . GLU B 1 60  ? 3.727   -13.340 23.326  1.00 60.43  ? 60   GLU B N   1 
ATOM   3694  C CA  . GLU B 1 60  ? 3.485   -12.989 24.718  1.00 61.64  ? 60   GLU B CA  1 
ATOM   3695  C C   . GLU B 1 60  ? 4.501   -11.937 25.197  1.00 59.44  ? 60   GLU B C   1 
ATOM   3696  O O   . GLU B 1 60  ? 5.690   -12.019 24.870  1.00 59.07  ? 60   GLU B O   1 
ATOM   3697  C CB  . GLU B 1 60  ? 3.562   -14.235 25.605  1.00 64.31  ? 60   GLU B CB  1 
ATOM   3698  C CG  . GLU B 1 60  ? 2.352   -15.171 25.523  1.00 69.96  ? 60   GLU B CG  1 
ATOM   3699  C CD  . GLU B 1 60  ? 2.244   -16.145 26.719  1.00 77.00  ? 60   GLU B CD  1 
ATOM   3700  O OE1 . GLU B 1 60  ? 3.292   -16.462 27.340  1.00 79.09  ? 60   GLU B OE1 1 
ATOM   3701  O OE2 . GLU B 1 60  ? 1.110   -16.606 27.033  1.00 80.52  ? 60   GLU B OE2 1 
ATOM   3702  N N   . LEU B 1 61  ? 4.023   -10.947 25.952  1.00 58.47  ? 61   LEU B N   1 
ATOM   3703  C CA  . LEU B 1 61  ? 4.881   -9.976  26.609  1.00 56.54  ? 61   LEU B CA  1 
ATOM   3704  C C   . LEU B 1 61  ? 5.426   -10.653 27.838  1.00 58.02  ? 61   LEU B C   1 
ATOM   3705  O O   . LEU B 1 61  ? 4.750   -11.488 28.391  1.00 60.10  ? 61   LEU B O   1 
ATOM   3706  C CB  . LEU B 1 61  ? 4.032   -8.806  27.055  1.00 55.26  ? 61   LEU B CB  1 
ATOM   3707  C CG  . LEU B 1 61  ? 4.598   -7.946  28.176  1.00 53.58  ? 61   LEU B CG  1 
ATOM   3708  C CD1 . LEU B 1 61  ? 5.575   -6.918  27.619  1.00 51.70  ? 61   LEU B CD1 1 
ATOM   3709  C CD2 . LEU B 1 61  ? 3.478   -7.259  28.878  1.00 53.33  ? 61   LEU B CD2 1 
ATOM   3710  N N   . SER B 1 62  ? 6.628   -10.306 28.281  1.00 57.47  ? 62   SER B N   1 
ATOM   3711  C CA  . SER B 1 62  ? 7.113   -10.827 29.550  1.00 59.28  ? 62   SER B CA  1 
ATOM   3712  C C   . SER B 1 62  ? 6.939   -9.779  30.605  1.00 58.88  ? 62   SER B C   1 
ATOM   3713  O O   . SER B 1 62  ? 7.710   -8.857  30.691  1.00 57.17  ? 62   SER B O   1 
ATOM   3714  C CB  . SER B 1 62  ? 8.561   -11.264 29.453  1.00 58.96  ? 62   SER B CB  1 
ATOM   3715  O OG  . SER B 1 62  ? 8.649   -12.422 28.640  1.00 61.01  ? 62   SER B OG  1 
ATOM   3716  N N   . ASN B 1 63  ? 5.909   -9.919  31.417  1.00 61.51  ? 63   ASN B N   1 
ATOM   3717  C CA  . ASN B 1 63  ? 5.466   -8.799  32.224  1.00 61.59  ? 63   ASN B CA  1 
ATOM   3718  C C   . ASN B 1 63  ? 6.237   -8.640  33.497  1.00 62.01  ? 63   ASN B C   1 
ATOM   3719  O O   . ASN B 1 63  ? 6.689   -9.615  34.087  1.00 63.76  ? 63   ASN B O   1 
ATOM   3720  C CB  . ASN B 1 63  ? 3.970   -8.884  32.538  1.00 63.10  ? 63   ASN B CB  1 
ATOM   3721  C CG  . ASN B 1 63  ? 3.295   -7.501  32.546  1.00 62.38  ? 63   ASN B CG  1 
ATOM   3722  O OD1 . ASN B 1 63  ? 3.835   -6.528  33.078  1.00 60.71  ? 63   ASN B OD1 1 
ATOM   3723  N ND2 . ASN B 1 63  ? 2.110   -7.416  31.945  1.00 63.60  ? 63   ASN B ND2 1 
ATOM   3724  N N   . ILE B 1 64  ? 6.372   -7.396  33.920  1.00 61.45  ? 64   ILE B N   1 
ATOM   3725  C CA  . ILE B 1 64  ? 6.972   -7.100  35.193  1.00 62.67  ? 64   ILE B CA  1 
ATOM   3726  C C   . ILE B 1 64  ? 5.942   -7.003  36.308  1.00 65.53  ? 64   ILE B C   1 
ATOM   3727  O O   . ILE B 1 64  ? 4.989   -6.211  36.207  1.00 65.51  ? 64   ILE B O   1 
ATOM   3728  C CB  . ILE B 1 64  ? 7.619   -5.742  35.184  1.00 59.79  ? 64   ILE B CB  1 
ATOM   3729  C CG1 . ILE B 1 64  ? 8.535   -5.592  33.991  1.00 57.94  ? 64   ILE B CG1 1 
ATOM   3730  C CG2 . ILE B 1 64  ? 8.372   -5.548  36.489  1.00 60.12  ? 64   ILE B CG2 1 
ATOM   3731  C CD1 . ILE B 1 64  ? 9.222   -4.279  33.978  1.00 55.54  ? 64   ILE B CD1 1 
ATOM   3732  N N   . LYS B 1 65  ? 6.154   -7.762  37.388  1.00 68.92  ? 65   LYS B N   1 
ATOM   3733  C CA  . LYS B 1 65  ? 5.459   -7.474  38.666  1.00 71.59  ? 65   LYS B CA  1 
ATOM   3734  C C   . LYS B 1 65  ? 6.316   -6.570  39.612  1.00 70.98  ? 65   LYS B C   1 
ATOM   3735  O O   . LYS B 1 65  ? 7.257   -7.032  40.321  1.00 71.04  ? 65   LYS B O   1 
ATOM   3736  C CB  . LYS B 1 65  ? 4.870   -8.741  39.337  1.00 74.18  ? 65   LYS B CB  1 
ATOM   3737  C CG  . LYS B 1 65  ? 5.662   -10.026 39.093  1.00 76.67  ? 65   LYS B CG  1 
ATOM   3738  C CD  . LYS B 1 65  ? 7.193   -9.830  39.404  1.00 77.15  ? 65   LYS B CD  1 
ATOM   3739  C CE  . LYS B 1 65  ? 7.926   -11.139 39.802  1.00 79.38  ? 65   LYS B CE  1 
ATOM   3740  N NZ  . LYS B 1 65  ? 9.130   -10.886 40.675  1.00 77.91  ? 65   LYS B NZ  1 
ATOM   3741  N N   . GLU B 1 66  ? 5.961   -5.273  39.561  1.00 70.64  ? 66   GLU B N   1 
ATOM   3742  C CA  . GLU B 1 66  ? 6.698   -4.147  40.172  1.00 69.98  ? 66   GLU B CA  1 
ATOM   3743  C C   . GLU B 1 66  ? 6.729   -4.177  41.708  1.00 71.11  ? 66   GLU B C   1 
ATOM   3744  O O   . GLU B 1 66  ? 5.714   -4.478  42.360  1.00 72.78  ? 66   GLU B O   1 
ATOM   3745  C CB  . GLU B 1 66  ? 6.107   -2.835  39.664  1.00 68.69  ? 66   GLU B CB  1 
ATOM   3746  C CG  . GLU B 1 66  ? 6.195   -1.636  40.599  1.00 69.43  ? 66   GLU B CG  1 
ATOM   3747  C CD  . GLU B 1 66  ? 5.175   -0.555  40.216  1.00 72.65  ? 66   GLU B CD  1 
ATOM   3748  O OE1 . GLU B 1 66  ? 5.358   0.606   40.636  1.00 73.84  ? 66   GLU B OE1 1 
ATOM   3749  O OE2 . GLU B 1 66  ? 4.189   -0.847  39.481  1.00 73.70  ? 66   GLU B OE2 1 
ATOM   3750  N N   . ASN B 1 67  ? 7.894   -3.875  42.286  1.00 70.59  ? 67   ASN B N   1 
ATOM   3751  C CA  . ASN B 1 67  ? 8.043   -4.080  43.741  1.00 71.61  ? 67   ASN B CA  1 
ATOM   3752  C C   . ASN B 1 67  ? 8.222   -2.870  44.616  1.00 70.48  ? 67   ASN B C   1 
ATOM   3753  O O   . ASN B 1 67  ? 9.308   -2.613  45.187  1.00 69.68  ? 67   ASN B O   1 
ATOM   3754  C CB  . ASN B 1 67  ? 9.001   -5.232  44.101  1.00 72.43  ? 67   ASN B CB  1 
ATOM   3755  C CG  . ASN B 1 67  ? 8.265   -6.537  44.259  1.00 74.68  ? 67   ASN B CG  1 
ATOM   3756  O OD1 . ASN B 1 67  ? 7.491   -6.697  45.199  1.00 75.84  ? 67   ASN B OD1 1 
ATOM   3757  N ND2 . ASN B 1 67  ? 8.463   -7.459  43.314  1.00 74.79  ? 67   ASN B ND2 1 
ATOM   3758  N N   . LYS B 1 68  ? 7.122   -2.116  44.638  1.00 70.33  ? 68   LYS B N   1 
ATOM   3759  C CA  . LYS B 1 68  ? 6.768   -1.178  45.689  1.00 70.16  ? 68   LYS B CA  1 
ATOM   3760  C C   . LYS B 1 68  ? 7.685   -1.302  46.911  1.00 69.93  ? 68   LYS B C   1 
ATOM   3761  O O   . LYS B 1 68  ? 7.401   -2.016  47.884  1.00 71.48  ? 68   LYS B O   1 
ATOM   3762  C CB  . LYS B 1 68  ? 5.315   -1.409  46.122  1.00 72.30  ? 68   LYS B CB  1 
ATOM   3763  C CG  . LYS B 1 68  ? 4.289   -1.792  45.011  1.00 73.33  ? 68   LYS B CG  1 
ATOM   3764  C CD  . LYS B 1 68  ? 3.257   -2.840  45.542  1.00 76.05  ? 68   LYS B CD  1 
ATOM   3765  C CE  . LYS B 1 68  ? 3.196   -2.871  47.090  1.00 76.80  ? 68   LYS B CE  1 
ATOM   3766  N NZ  . LYS B 1 68  ? 2.129   -3.746  47.655  1.00 79.52  ? 68   LYS B NZ  1 
ATOM   3767  N N   . CYS B 1 69  ? 8.814   -0.624  46.804  1.00 67.81  ? 69   CYS B N   1 
ATOM   3768  C CA  . CYS B 1 69  ? 9.726   -0.428  47.886  1.00 67.14  ? 69   CYS B CA  1 
ATOM   3769  C C   . CYS B 1 69  ? 9.822   1.101   47.866  1.00 66.16  ? 69   CYS B C   1 
ATOM   3770  O O   . CYS B 1 69  ? 9.022   1.772   47.221  1.00 65.84  ? 69   CYS B O   1 
ATOM   3771  C CB  . CYS B 1 69  ? 11.080  -1.007  47.501  1.00 65.78  ? 69   CYS B CB  1 
ATOM   3772  S SG  . CYS B 1 69  ? 11.991  0.308   46.615  1.00 63.27  ? 69   CYS B SG  1 
ATOM   3773  N N   . ASN B 1 70  ? 10.828  1.643   48.537  1.00 66.02  ? 70   ASN B N   1 
ATOM   3774  C CA  . ASN B 1 70  ? 11.203  3.045   48.393  1.00 65.61  ? 70   ASN B CA  1 
ATOM   3775  C C   . ASN B 1 70  ? 12.629  3.111   47.810  1.00 62.30  ? 70   ASN B C   1 
ATOM   3776  O O   . ASN B 1 70  ? 13.577  2.579   48.417  1.00 62.13  ? 70   ASN B O   1 
ATOM   3777  C CB  . ASN B 1 70  ? 11.155  3.700   49.773  1.00 67.88  ? 70   ASN B CB  1 
ATOM   3778  C CG  . ASN B 1 70  ? 9.907   3.319   50.575  1.00 78.27  ? 70   ASN B CG  1 
ATOM   3779  O OD1 . ASN B 1 70  ? 8.831   3.070   50.001  1.00 83.21  ? 70   ASN B OD1 1 
ATOM   3780  N ND2 . ASN B 1 70  ? 10.046  3.273   51.914  1.00 92.63  ? 70   ASN B ND2 1 
ATOM   3781  N N   . GLY B 1 71  ? 12.786  3.700   46.624  1.00 59.39  ? 71   GLY B N   1 
ATOM   3782  C CA  . GLY B 1 71  ? 14.120  3.833   46.023  1.00 56.20  ? 71   GLY B CA  1 
ATOM   3783  C C   . GLY B 1 71  ? 14.827  5.085   46.520  1.00 54.02  ? 71   GLY B C   1 
ATOM   3784  O O   . GLY B 1 71  ? 14.277  5.820   47.328  1.00 54.37  ? 71   GLY B O   1 
ATOM   3785  N N   . THR B 1 72  ? 16.043  5.333   46.055  1.00 51.89  ? 72   THR B N   1 
ATOM   3786  C CA  . THR B 1 72  ? 16.728  6.589   46.341  1.00 50.29  ? 72   THR B CA  1 
ATOM   3787  C C   . THR B 1 72  ? 16.073  7.651   45.482  1.00 49.90  ? 72   THR B C   1 
ATOM   3788  O O   . THR B 1 72  ? 16.106  7.548   44.258  1.00 49.90  ? 72   THR B O   1 
ATOM   3789  C CB  . THR B 1 72  ? 18.233  6.498   45.986  1.00 49.68  ? 72   THR B CB  1 
ATOM   3790  O OG1 . THR B 1 72  ? 18.442  6.647   44.569  1.00 47.50  ? 72   THR B OG1 1 
ATOM   3791  C CG2 . THR B 1 72  ? 18.813  5.159   46.439  1.00 50.33  ? 72   THR B CG2 1 
ATOM   3792  N N   . ASP B 1 73  ? 15.475  8.671   46.097  1.00 50.04  ? 73   ASP B N   1 
ATOM   3793  C CA  . ASP B 1 73  ? 14.485  9.571   45.392  1.00 49.86  ? 73   ASP B CA  1 
ATOM   3794  C C   . ASP B 1 73  ? 13.230  8.831   44.863  1.00 49.81  ? 73   ASP B C   1 
ATOM   3795  O O   . ASP B 1 73  ? 13.300  8.076   43.874  1.00 48.99  ? 73   ASP B O   1 
ATOM   3796  C CB  . ASP B 1 73  ? 15.123  10.441  44.259  1.00 48.92  ? 73   ASP B CB  1 
ATOM   3797  C CG  . ASP B 1 73  ? 14.101  11.406  43.591  1.00 49.77  ? 73   ASP B CG  1 
ATOM   3798  O OD1 . ASP B 1 73  ? 12.864  11.181  43.708  1.00 50.73  ? 73   ASP B OD1 1 
ATOM   3799  O OD2 . ASP B 1 73  ? 14.537  12.399  42.953  1.00 50.00  ? 73   ASP B OD2 1 
ATOM   3800  N N   . ALA B 1 74  ? 12.087  9.073   45.509  1.00 50.24  ? 74   ALA B N   1 
ATOM   3801  C CA  . ALA B 1 74  ? 10.854  8.398   45.089  1.00 50.94  ? 74   ALA B CA  1 
ATOM   3802  C C   . ALA B 1 74  ? 9.885   9.288   44.303  1.00 50.68  ? 74   ALA B C   1 
ATOM   3803  O O   . ALA B 1 74  ? 8.691   9.117   44.379  1.00 51.62  ? 74   ALA B O   1 
ATOM   3804  C CB  . ALA B 1 74  ? 10.154  7.656   46.278  1.00 52.14  ? 74   ALA B CB  1 
ATOM   3805  N N   . LYS B 1 75  ? 10.417  10.238  43.549  1.00 49.80  ? 75   LYS B N   1 
ATOM   3806  C CA  . LYS B 1 75  ? 9.686   10.791  42.403  1.00 50.15  ? 75   LYS B CA  1 
ATOM   3807  C C   . LYS B 1 75  ? 10.039  9.922   41.177  1.00 49.39  ? 75   LYS B C   1 
ATOM   3808  O O   . LYS B 1 75  ? 9.271   9.817   40.189  1.00 49.69  ? 75   LYS B O   1 
ATOM   3809  C CB  . LYS B 1 75  ? 10.070  12.266  42.153  1.00 49.76  ? 75   LYS B CB  1 
ATOM   3810  C CG  . LYS B 1 75  ? 9.562   13.247  43.204  1.00 51.79  ? 75   LYS B CG  1 
ATOM   3811  C CD  . LYS B 1 75  ? 10.649  14.273  43.525  1.00 53.55  ? 75   LYS B CD  1 
ATOM   3812  C CE  . LYS B 1 75  ? 10.609  14.686  45.025  1.00 55.93  ? 75   LYS B CE  1 
ATOM   3813  N NZ  . LYS B 1 75  ? 11.992  14.546  45.709  1.00 55.83  ? 75   LYS B NZ  1 
ATOM   3814  N N   . VAL B 1 76  ? 11.228  9.324   41.272  1.00 48.20  ? 76   VAL B N   1 
ATOM   3815  C CA  . VAL B 1 76  ? 11.753  8.389   40.313  1.00 47.18  ? 76   VAL B CA  1 
ATOM   3816  C C   . VAL B 1 76  ? 10.994  7.084   40.465  1.00 47.99  ? 76   VAL B C   1 
ATOM   3817  O O   . VAL B 1 76  ? 10.900  6.554   41.568  1.00 48.81  ? 76   VAL B O   1 
ATOM   3818  C CB  . VAL B 1 76  ? 13.211  8.153   40.626  1.00 46.63  ? 76   VAL B CB  1 
ATOM   3819  C CG1 . VAL B 1 76  ? 13.721  6.953   39.882  1.00 47.05  ? 76   VAL B CG1 1 
ATOM   3820  C CG2 . VAL B 1 76  ? 14.027  9.389   40.297  1.00 45.87  ? 76   VAL B CG2 1 
ATOM   3821  N N   . LYS B 1 77  ? 10.452  6.574   39.362  1.00 47.87  ? 77   LYS B N   1 
ATOM   3822  C CA  . LYS B 1 77  ? 9.593   5.391   39.397  1.00 49.05  ? 77   LYS B CA  1 
ATOM   3823  C C   . LYS B 1 77  ? 9.705   4.555   38.142  1.00 48.07  ? 77   LYS B C   1 
ATOM   3824  O O   . LYS B 1 77  ? 8.731   4.327   37.436  1.00 48.62  ? 77   LYS B O   1 
ATOM   3825  C CB  . LYS B 1 77  ? 8.138   5.810   39.638  1.00 50.42  ? 77   LYS B CB  1 
ATOM   3826  C CG  . LYS B 1 77  ? 7.695   5.537   41.069  1.00 54.44  ? 77   LYS B CG  1 
ATOM   3827  C CD  . LYS B 1 77  ? 6.968   6.717   41.689  1.00 58.77  ? 77   LYS B CD  1 
ATOM   3828  C CE  . LYS B 1 77  ? 6.924   6.571   43.231  1.00 61.86  ? 77   LYS B CE  1 
ATOM   3829  N NZ  . LYS B 1 77  ? 5.795   7.377   43.855  1.00 65.05  ? 77   LYS B NZ  1 
ATOM   3830  N N   . LEU B 1 78  ? 10.901  4.066   37.886  1.00 46.76  ? 78   LEU B N   1 
ATOM   3831  C CA  . LEU B 1 78  ? 11.219  3.541   36.568  1.00 45.71  ? 78   LEU B CA  1 
ATOM   3832  C C   . LEU B 1 78  ? 10.203  2.532   36.110  1.00 46.56  ? 78   LEU B C   1 
ATOM   3833  O O   . LEU B 1 78  ? 9.564   2.717   35.075  1.00 46.58  ? 78   LEU B O   1 
ATOM   3834  C CB  . LEU B 1 78  ? 12.656  3.003   36.494  1.00 45.00  ? 78   LEU B CB  1 
ATOM   3835  C CG  . LEU B 1 78  ? 13.670  4.111   36.862  1.00 43.94  ? 78   LEU B CG  1 
ATOM   3836  C CD1 . LEU B 1 78  ? 15.152  3.697   36.698  1.00 43.11  ? 78   LEU B CD1 1 
ATOM   3837  C CD2 . LEU B 1 78  ? 13.376  5.482   36.151  1.00 43.23  ? 78   LEU B CD2 1 
ATOM   3838  N N   . ILE B 1 79  ? 10.002  1.496   36.905  1.00 47.30  ? 79   ILE B N   1 
ATOM   3839  C CA  . ILE B 1 79  ? 9.156   0.424   36.450  1.00 48.30  ? 79   ILE B CA  1 
ATOM   3840  C C   . ILE B 1 79  ? 7.769   0.931   36.103  1.00 48.47  ? 79   ILE B C   1 
ATOM   3841  O O   . ILE B 1 79  ? 7.297   0.696   34.988  1.00 48.71  ? 79   ILE B O   1 
ATOM   3842  C CB  . ILE B 1 79  ? 9.105   -0.737  37.430  1.00 49.93  ? 79   ILE B CB  1 
ATOM   3843  C CG1 . ILE B 1 79  ? 10.530  -1.275  37.685  1.00 49.79  ? 79   ILE B CG1 1 
ATOM   3844  C CG2 . ILE B 1 79  ? 8.191   -1.841  36.862  1.00 51.46  ? 79   ILE B CG2 1 
ATOM   3845  C CD1 . ILE B 1 79  ? 10.646  -2.292  38.838  1.00 51.84  ? 79   ILE B CD1 1 
ATOM   3846  N N   . LYS B 1 80  ? 7.133   1.640   37.032  1.00 48.38  ? 80   LYS B N   1 
ATOM   3847  C CA  . LYS B 1 80  ? 5.860   2.279   36.726  1.00 48.68  ? 80   LYS B CA  1 
ATOM   3848  C C   . LYS B 1 80  ? 5.946   2.975   35.361  1.00 47.08  ? 80   LYS B C   1 
ATOM   3849  O O   . LYS B 1 80  ? 5.089   2.766   34.488  1.00 47.34  ? 80   LYS B O   1 
ATOM   3850  C CB  . LYS B 1 80  ? 5.480   3.298   37.804  1.00 49.12  ? 80   LYS B CB  1 
ATOM   3851  C CG  . LYS B 1 80  ? 4.386   4.299   37.381  1.00 50.77  ? 80   LYS B CG  1 
ATOM   3852  C CD  . LYS B 1 80  ? 3.022   3.914   37.934  1.00 55.91  ? 80   LYS B CD  1 
ATOM   3853  C CE  . LYS B 1 80  ? 1.904   4.173   36.917  1.00 58.29  ? 80   LYS B CE  1 
ATOM   3854  N NZ  . LYS B 1 80  ? 1.666   2.962   36.050  1.00 61.61  ? 80   LYS B NZ  1 
ATOM   3855  N N   . GLN B 1 81  ? 7.005   3.766   35.178  1.00 45.19  ? 81   GLN B N   1 
ATOM   3856  C CA  . GLN B 1 81  ? 7.136   4.633   34.027  1.00 43.92  ? 81   GLN B CA  1 
ATOM   3857  C C   . GLN B 1 81  ? 7.317   3.834   32.760  1.00 43.19  ? 81   GLN B C   1 
ATOM   3858  O O   . GLN B 1 81  ? 6.569   4.027   31.813  1.00 43.49  ? 81   GLN B O   1 
ATOM   3859  C CB  . GLN B 1 81  ? 8.229   5.667   34.257  1.00 42.85  ? 81   GLN B CB  1 
ATOM   3860  C CG  . GLN B 1 81  ? 7.842   6.629   35.407  1.00 45.88  ? 81   GLN B CG  1 
ATOM   3861  C CD  . GLN B 1 81  ? 8.849   7.768   35.688  1.00 48.12  ? 81   GLN B CD  1 
ATOM   3862  O OE1 . GLN B 1 81  ? 9.264   8.502   34.767  1.00 49.03  ? 81   GLN B OE1 1 
ATOM   3863  N NE2 . GLN B 1 81  ? 9.204   7.947   36.976  1.00 48.08  ? 81   GLN B NE2 1 
ATOM   3864  N N   . GLU B 1 82  ? 8.249   2.896   32.752  1.00 42.52  ? 82   GLU B N   1 
ATOM   3865  C CA  . GLU B 1 82  ? 8.423   2.032   31.579  1.00 42.39  ? 82   GLU B CA  1 
ATOM   3866  C C   . GLU B 1 82  ? 7.130   1.359   31.201  1.00 43.13  ? 82   GLU B C   1 
ATOM   3867  O O   . GLU B 1 82  ? 6.763   1.301   30.036  1.00 43.14  ? 82   GLU B O   1 
ATOM   3868  C CB  . GLU B 1 82  ? 9.495   0.953   31.786  1.00 42.77  ? 82   GLU B CB  1 
ATOM   3869  C CG  . GLU B 1 82  ? 10.907  1.331   31.320  1.00 42.94  ? 82   GLU B CG  1 
ATOM   3870  C CD  . GLU B 1 82  ? 11.100  1.313   29.788  1.00 44.75  ? 82   GLU B CD  1 
ATOM   3871  O OE1 . GLU B 1 82  ? 10.458  0.462   29.108  1.00 46.28  ? 82   GLU B OE1 1 
ATOM   3872  O OE2 . GLU B 1 82  ? 11.914  2.140   29.272  1.00 43.80  ? 82   GLU B OE2 1 
ATOM   3873  N N   . LEU B 1 83  ? 6.431   0.840   32.184  1.00 44.06  ? 83   LEU B N   1 
ATOM   3874  C CA  . LEU B 1 83  ? 5.190   0.192   31.878  1.00 45.55  ? 83   LEU B CA  1 
ATOM   3875  C C   . LEU B 1 83  ? 4.250   1.120   31.147  1.00 45.09  ? 83   LEU B C   1 
ATOM   3876  O O   . LEU B 1 83  ? 3.646   0.692   30.180  1.00 45.71  ? 83   LEU B O   1 
ATOM   3877  C CB  . LEU B 1 83  ? 4.523   -0.336  33.135  1.00 47.36  ? 83   LEU B CB  1 
ATOM   3878  C CG  . LEU B 1 83  ? 5.014   -1.682  33.680  1.00 49.02  ? 83   LEU B CG  1 
ATOM   3879  C CD1 . LEU B 1 83  ? 3.804   -2.648  33.791  1.00 52.24  ? 83   LEU B CD1 1 
ATOM   3880  C CD2 . LEU B 1 83  ? 6.105   -2.303  32.819  1.00 48.79  ? 83   LEU B CD2 1 
ATOM   3881  N N   . ASP B 1 84  ? 4.144   2.378   31.587  1.00 44.30  ? 84   ASP B N   1 
ATOM   3882  C CA  . ASP B 1 84  ? 3.235   3.365   30.952  1.00 44.45  ? 84   ASP B CA  1 
ATOM   3883  C C   . ASP B 1 84  ? 3.587   3.656   29.520  1.00 42.74  ? 84   ASP B C   1 
ATOM   3884  O O   . ASP B 1 84  ? 2.749   3.526   28.639  1.00 43.00  ? 84   ASP B O   1 
ATOM   3885  C CB  . ASP B 1 84  ? 3.204   4.669   31.723  1.00 44.50  ? 84   ASP B CB  1 
ATOM   3886  C CG  . ASP B 1 84  ? 2.543   4.515   33.058  1.00 49.01  ? 84   ASP B CG  1 
ATOM   3887  O OD1 . ASP B 1 84  ? 1.783   3.522   33.230  1.00 54.13  ? 84   ASP B OD1 1 
ATOM   3888  O OD2 . ASP B 1 84  ? 2.780   5.375   33.939  1.00 51.85  ? 84   ASP B OD2 1 
ATOM   3889  N N   . LYS B 1 85  ? 4.838   4.049   29.308  1.00 40.80  ? 85   LYS B N   1 
ATOM   3890  C CA  . LYS B 1 85  ? 5.412   4.146   27.990  1.00 39.40  ? 85   LYS B CA  1 
ATOM   3891  C C   . LYS B 1 85  ? 4.862   2.995   27.167  1.00 40.03  ? 85   LYS B C   1 
ATOM   3892  O O   . LYS B 1 85  ? 4.135   3.209   26.206  1.00 39.97  ? 85   LYS B O   1 
ATOM   3893  C CB  . LYS B 1 85  ? 6.936   4.039   28.084  1.00 38.54  ? 85   LYS B CB  1 
ATOM   3894  C CG  . LYS B 1 85  ? 7.706   4.702   26.963  1.00 37.50  ? 85   LYS B CG  1 
ATOM   3895  C CD  . LYS B 1 85  ? 9.111   4.198   26.892  1.00 37.71  ? 85   LYS B CD  1 
ATOM   3896  C CE  . LYS B 1 85  ? 9.123   2.757   26.420  1.00 40.81  ? 85   LYS B CE  1 
ATOM   3897  N NZ  . LYS B 1 85  ? 10.525  2.297   26.332  1.00 43.38  ? 85   LYS B NZ  1 
ATOM   3898  N N   . TYR B 1 86  ? 5.187   1.771   27.578  1.00 40.63  ? 86   TYR B N   1 
ATOM   3899  C CA  . TYR B 1 86  ? 4.775   0.577   26.856  1.00 41.46  ? 86   TYR B CA  1 
ATOM   3900  C C   . TYR B 1 86  ? 3.291   0.491   26.687  1.00 42.23  ? 86   TYR B C   1 
ATOM   3901  O O   . TYR B 1 86  ? 2.811   0.393   25.587  1.00 42.41  ? 86   TYR B O   1 
ATOM   3902  C CB  . TYR B 1 86  ? 5.225   -0.694  27.545  1.00 42.53  ? 86   TYR B CB  1 
ATOM   3903  C CG  . TYR B 1 86  ? 4.643   -1.896  26.863  1.00 44.25  ? 86   TYR B CG  1 
ATOM   3904  C CD1 . TYR B 1 86  ? 4.851   -2.114  25.495  1.00 45.12  ? 86   TYR B CD1 1 
ATOM   3905  C CD2 . TYR B 1 86  ? 3.879   -2.807  27.568  1.00 45.70  ? 86   TYR B CD2 1 
ATOM   3906  C CE1 . TYR B 1 86  ? 4.315   -3.225  24.864  1.00 46.88  ? 86   TYR B CE1 1 
ATOM   3907  C CE2 . TYR B 1 86  ? 3.341   -3.924  26.957  1.00 47.45  ? 86   TYR B CE2 1 
ATOM   3908  C CZ  . TYR B 1 86  ? 3.558   -4.131  25.611  1.00 48.62  ? 86   TYR B CZ  1 
ATOM   3909  O OH  . TYR B 1 86  ? 3.020   -5.238  24.998  1.00 50.25  ? 86   TYR B OH  1 
ATOM   3910  N N   . LYS B 1 87  ? 2.573   0.502   27.789  1.00 43.10  ? 87   LYS B N   1 
ATOM   3911  C CA  . LYS B 1 87  ? 1.132   0.372   27.749  1.00 44.86  ? 87   LYS B CA  1 
ATOM   3912  C C   . LYS B 1 87  ? 0.533   1.334   26.770  1.00 43.83  ? 87   LYS B C   1 
ATOM   3913  O O   . LYS B 1 87  ? -0.420  1.012   26.069  1.00 45.17  ? 87   LYS B O   1 
ATOM   3914  C CB  . LYS B 1 87  ? 0.505   0.642   29.117  1.00 45.99  ? 87   LYS B CB  1 
ATOM   3915  C CG  . LYS B 1 87  ? 0.673   -0.465  30.135  1.00 48.54  ? 87   LYS B CG  1 
ATOM   3916  C CD  . LYS B 1 87  ? 0.025   -0.083  31.446  1.00 51.90  ? 87   LYS B CD  1 
ATOM   3917  C CE  . LYS B 1 87  ? 0.748   -0.712  32.613  1.00 52.86  ? 87   LYS B CE  1 
ATOM   3918  N NZ  . LYS B 1 87  ? -0.233  -1.141  33.619  1.00 55.89  ? 87   LYS B NZ  1 
ATOM   3919  N N   . ASN B 1 88  ? 1.084   2.525   26.730  1.00 41.62  ? 88   ASN B N   1 
ATOM   3920  C CA  . ASN B 1 88  ? 0.518   3.529   25.891  1.00 40.55  ? 88   ASN B CA  1 
ATOM   3921  C C   . ASN B 1 88  ? 0.740   3.234   24.418  1.00 39.36  ? 88   ASN B C   1 
ATOM   3922  O O   . ASN B 1 88  ? -0.210  3.210   23.660  1.00 39.89  ? 88   ASN B O   1 
ATOM   3923  C CB  . ASN B 1 88  ? 1.089   4.851   26.282  1.00 39.84  ? 88   ASN B CB  1 
ATOM   3924  C CG  . ASN B 1 88  ? 0.913   5.881   25.236  1.00 39.79  ? 88   ASN B CG  1 
ATOM   3925  O OD1 . ASN B 1 88  ? -0.124  6.506   25.169  1.00 41.32  ? 88   ASN B OD1 1 
ATOM   3926  N ND2 . ASN B 1 88  ? 1.948   6.099   24.420  1.00 40.18  ? 88   ASN B ND2 1 
ATOM   3927  N N   . ALA B 1 89  ? 1.982   2.992   24.011  1.00 37.55  ? 89   ALA B N   1 
ATOM   3928  C CA  . ALA B 1 89  ? 2.257   2.531   22.652  1.00 36.65  ? 89   ALA B CA  1 
ATOM   3929  C C   . ALA B 1 89  ? 1.156   1.578   22.205  1.00 37.76  ? 89   ALA B C   1 
ATOM   3930  O O   . ALA B 1 89  ? 0.644   1.671   21.093  1.00 37.77  ? 89   ALA B O   1 
ATOM   3931  C CB  . ALA B 1 89  ? 3.583   1.827   22.602  1.00 36.24  ? 89   ALA B CB  1 
ATOM   3932  N N   . VAL B 1 90  ? 0.785   0.685   23.115  1.00 38.50  ? 90   VAL B N   1 
ATOM   3933  C CA  . VAL B 1 90  ? -0.149  -0.390  22.857  1.00 39.72  ? 90   VAL B CA  1 
ATOM   3934  C C   . VAL B 1 90  ? -1.513  0.174   22.609  1.00 40.36  ? 90   VAL B C   1 
ATOM   3935  O O   . VAL B 1 90  ? -2.180  -0.226  21.677  1.00 41.33  ? 90   VAL B O   1 
ATOM   3936  C CB  . VAL B 1 90  ? -0.169  -1.384  24.020  1.00 40.85  ? 90   VAL B CB  1 
ATOM   3937  C CG1 . VAL B 1 90  ? -1.346  -2.308  23.937  1.00 42.83  ? 90   VAL B CG1 1 
ATOM   3938  C CG2 . VAL B 1 90  ? 1.113   -2.186  24.012  1.00 40.62  ? 90   VAL B CG2 1 
ATOM   3939  N N   . THR B 1 91  ? -1.925  1.131   23.414  1.00 40.28  ? 91   THR B N   1 
ATOM   3940  C CA  . THR B 1 91  ? -3.219  1.736   23.191  1.00 41.32  ? 91   THR B CA  1 
ATOM   3941  C C   . THR B 1 91  ? -3.251  2.400   21.844  1.00 40.73  ? 91   THR B C   1 
ATOM   3942  O O   . THR B 1 91  ? -4.167  2.203   21.065  1.00 41.66  ? 91   THR B O   1 
ATOM   3943  C CB  . THR B 1 91  ? -3.543  2.741   24.247  1.00 40.98  ? 91   THR B CB  1 
ATOM   3944  O OG1 . THR B 1 91  ? -3.131  2.223   25.517  1.00 41.57  ? 91   THR B OG1 1 
ATOM   3945  C CG2 . THR B 1 91  ? -5.026  2.957   24.289  1.00 43.12  ? 91   THR B CG2 1 
ATOM   3946  N N   . GLU B 1 92  ? -2.211  3.161   21.558  1.00 39.57  ? 92   GLU B N   1 
ATOM   3947  C CA  . GLU B 1 92  ? -2.101  3.833   20.273  1.00 39.14  ? 92   GLU B CA  1 
ATOM   3948  C C   . GLU B 1 92  ? -2.354  2.914   19.098  1.00 39.48  ? 92   GLU B C   1 
ATOM   3949  O O   . GLU B 1 92  ? -3.120  3.262   18.196  1.00 39.39  ? 92   GLU B O   1 
ATOM   3950  C CB  . GLU B 1 92  ? -0.730  4.498   20.115  1.00 37.77  ? 92   GLU B CB  1 
ATOM   3951  C CG  . GLU B 1 92  ? -0.688  5.953   20.573  1.00 39.45  ? 92   GLU B CG  1 
ATOM   3952  C CD  . GLU B 1 92  ? -1.782  6.786   19.952  1.00 43.71  ? 92   GLU B CD  1 
ATOM   3953  O OE1 . GLU B 1 92  ? -2.153  6.552   18.767  1.00 45.35  ? 92   GLU B OE1 1 
ATOM   3954  O OE2 . GLU B 1 92  ? -2.285  7.668   20.674  1.00 44.86  ? 92   GLU B OE2 1 
ATOM   3955  N N   . LEU B 1 93  ? -1.690  1.758   19.102  1.00 39.79  ? 93   LEU B N   1 
ATOM   3956  C CA  . LEU B 1 93  ? -1.834  0.816   18.014  1.00 40.67  ? 93   LEU B CA  1 
ATOM   3957  C C   . LEU B 1 93  ? -3.257  0.325   18.049  1.00 43.07  ? 93   LEU B C   1 
ATOM   3958  O O   . LEU B 1 93  ? -3.907  0.178   17.011  1.00 43.99  ? 93   LEU B O   1 
ATOM   3959  C CB  . LEU B 1 93  ? -0.862  -0.355  18.147  1.00 40.56  ? 93   LEU B CB  1 
ATOM   3960  C CG  . LEU B 1 93  ? 0.618   -0.114  17.864  1.00 38.49  ? 93   LEU B CG  1 
ATOM   3961  C CD1 . LEU B 1 93  ? 1.408   -1.275  18.342  1.00 39.53  ? 93   LEU B CD1 1 
ATOM   3962  C CD2 . LEU B 1 93  ? 0.900   0.060   16.422  1.00 37.20  ? 93   LEU B CD2 1 
ATOM   3963  N N   . GLN B 1 94  ? -3.765  0.107   19.252  1.00 44.49  ? 94   GLN B N   1 
ATOM   3964  C CA  . GLN B 1 94  ? -5.098  -0.414  19.374  1.00 47.31  ? 94   GLN B CA  1 
ATOM   3965  C C   . GLN B 1 94  ? -6.038  0.391   18.543  1.00 47.49  ? 94   GLN B C   1 
ATOM   3966  O O   . GLN B 1 94  ? -6.954  -0.144  17.939  1.00 49.25  ? 94   GLN B O   1 
ATOM   3967  C CB  . GLN B 1 94  ? -5.566  -0.379  20.807  1.00 48.35  ? 94   GLN B CB  1 
ATOM   3968  C CG  . GLN B 1 94  ? -5.786  -1.731  21.378  1.00 51.88  ? 94   GLN B CG  1 
ATOM   3969  C CD  . GLN B 1 94  ? -5.681  -1.689  22.855  1.00 55.57  ? 94   GLN B CD  1 
ATOM   3970  O OE1 . GLN B 1 94  ? -6.394  -0.912  23.519  1.00 57.38  ? 94   GLN B OE1 1 
ATOM   3971  N NE2 . GLN B 1 94  ? -4.765  -2.499  23.407  1.00 57.19  ? 94   GLN B NE2 1 
ATOM   3972  N N   . LEU B 1 95  ? -5.806  1.686   18.508  1.00 46.39  ? 95   LEU B N   1 
ATOM   3973  C CA  . LEU B 1 95  ? -6.781  2.573   17.918  1.00 47.25  ? 95   LEU B CA  1 
ATOM   3974  C C   . LEU B 1 95  ? -6.705  2.533   16.403  1.00 48.07  ? 95   LEU B C   1 
ATOM   3975  O O   . LEU B 1 95  ? -7.562  3.085   15.721  1.00 48.92  ? 95   LEU B O   1 
ATOM   3976  C CB  . LEU B 1 95  ? -6.616  3.987   18.464  1.00 45.69  ? 95   LEU B CB  1 
ATOM   3977  C CG  . LEU B 1 95  ? -6.661  4.067   19.986  1.00 44.73  ? 95   LEU B CG  1 
ATOM   3978  C CD1 . LEU B 1 95  ? -5.937  5.269   20.501  1.00 41.77  ? 95   LEU B CD1 1 
ATOM   3979  C CD2 . LEU B 1 95  ? -8.071  4.094   20.434  1.00 45.14  ? 95   LEU B CD2 1 
ATOM   3980  N N   . LEU B 1 96  ? -5.705  1.840   15.875  1.00 48.81  ? 96   LEU B N   1 
ATOM   3981  C CA  . LEU B 1 96  ? -5.516  1.786   14.439  1.00 49.79  ? 96   LEU B CA  1 
ATOM   3982  C C   . LEU B 1 96  ? -6.502  0.902   13.733  1.00 53.18  ? 96   LEU B C   1 
ATOM   3983  O O   . LEU B 1 96  ? -6.696  1.024   12.518  1.00 53.32  ? 96   LEU B O   1 
ATOM   3984  C CB  . LEU B 1 96  ? -4.105  1.331   14.120  1.00 48.58  ? 96   LEU B CB  1 
ATOM   3985  C CG  . LEU B 1 96  ? -3.096  2.458   14.353  1.00 46.32  ? 96   LEU B CG  1 
ATOM   3986  C CD1 . LEU B 1 96  ? -1.853  2.182   13.559  1.00 44.82  ? 96   LEU B CD1 1 
ATOM   3987  C CD2 . LEU B 1 96  ? -3.689  3.822   13.945  1.00 45.57  ? 96   LEU B CD2 1 
ATOM   3988  N N   . MET B 1 97  ? -7.143  0.032   14.511  1.00 57.09  ? 97   MET B N   1 
ATOM   3989  C CA  . MET B 1 97  ? -7.945  -1.088  13.998  1.00 61.39  ? 97   MET B CA  1 
ATOM   3990  C C   . MET B 1 97  ? -9.290  -0.717  13.384  1.00 63.59  ? 97   MET B C   1 
ATOM   3991  O O   . MET B 1 97  ? -9.792  -1.408  12.467  1.00 65.46  ? 97   MET B O   1 
ATOM   3992  C CB  . MET B 1 97  ? -8.093  -2.153  15.085  1.00 63.17  ? 97   MET B CB  1 
ATOM   3993  C CG  . MET B 1 97  ? -6.728  -2.588  15.613  1.00 65.39  ? 97   MET B CG  1 
ATOM   3994  S SD  . MET B 1 97  ? -5.593  -3.385  14.404  1.00 71.42  ? 97   MET B SD  1 
ATOM   3995  C CE  . MET B 1 97  ? -6.039  -2.808  12.754  1.00 66.95  ? 97   MET B CE  1 
ATOM   3996  N N   . GLN B 1 98  ? -9.862  0.383   13.868  1.00 64.49  ? 98   GLN B N   1 
ATOM   3997  C CA  . GLN B 1 98  ? -11.188 0.822   13.400  1.00 66.81  ? 98   GLN B CA  1 
ATOM   3998  C C   . GLN B 1 98  ? -11.177 2.327   13.016  1.00 65.16  ? 98   GLN B C   1 
ATOM   3999  O O   . GLN B 1 98  ? -10.135 3.001   13.018  1.00 62.73  ? 98   GLN B O   1 
ATOM   4000  C CB  . GLN B 1 98  ? -12.327 0.486   14.439  1.00 69.51  ? 98   GLN B CB  1 
ATOM   4001  C CG  . GLN B 1 98  ? -12.139 -0.788  15.404  1.00 72.13  ? 98   GLN B CG  1 
ATOM   4002  C CD  . GLN B 1 98  ? -11.143 -0.580  16.621  1.00 72.25  ? 98   GLN B CD  1 
ATOM   4003  O OE1 . GLN B 1 98  ? -10.007 -0.098  16.471  1.00 69.08  ? 98   GLN B OE1 1 
ATOM   4004  N NE2 . GLN B 1 98  ? -11.589 -0.982  17.812  1.00 73.58  ? 98   GLN B NE2 1 
ATOM   4005  N N   . ILE B 1 139 ? 55.677  -13.687 117.543 1.00 96.93  ? 148  ILE B N   1 
ATOM   4006  C CA  . ILE B 1 139 ? 56.360  -14.180 118.737 1.00 99.19  ? 148  ILE B CA  1 
ATOM   4007  C C   . ILE B 1 139 ? 55.725  -13.619 120.017 1.00 99.43  ? 148  ILE B C   1 
ATOM   4008  O O   . ILE B 1 139 ? 55.712  -14.307 121.049 1.00 101.56 ? 148  ILE B O   1 
ATOM   4009  C CB  . ILE B 1 139 ? 57.923  -13.883 118.763 1.00 99.51  ? 148  ILE B CB  1 
ATOM   4010  C CG1 . ILE B 1 139 ? 58.603  -14.212 117.425 1.00 99.04  ? 148  ILE B CG1 1 
ATOM   4011  C CG2 . ILE B 1 139 ? 58.627  -14.608 119.955 1.00 102.18 ? 148  ILE B CG2 1 
ATOM   4012  C CD1 . ILE B 1 139 ? 60.114  -13.925 117.419 1.00 99.51  ? 148  ILE B CD1 1 
ATOM   4013  N N   . ALA B 1 140 ? 55.222  -12.381 119.961 1.00 97.41  ? 149  ALA B N   1 
ATOM   4014  C CA  . ALA B 1 140 ? 54.670  -11.696 121.154 1.00 97.59  ? 149  ALA B CA  1 
ATOM   4015  C C   . ALA B 1 140 ? 55.704  -11.078 122.108 1.00 98.17  ? 149  ALA B C   1 
ATOM   4016  O O   . ALA B 1 140 ? 55.736  -11.468 123.277 1.00 100.01 ? 149  ALA B O   1 
ATOM   4017  C CB  . ALA B 1 140 ? 53.730  -12.650 121.962 1.00 99.54  ? 149  ALA B CB  1 
ATOM   4018  N N   . SER B 1 141 ? 56.531  -10.126 121.657 1.00 96.77  ? 150  SER B N   1 
ATOM   4019  C CA  . SER B 1 141 ? 57.440  -9.439  122.614 1.00 97.37  ? 150  SER B CA  1 
ATOM   4020  C C   . SER B 1 141 ? 58.403  -8.381  122.076 1.00 95.99  ? 150  SER B C   1 
ATOM   4021  O O   . SER B 1 141 ? 58.415  -8.076  120.886 1.00 94.38  ? 150  SER B O   1 
ATOM   4022  C CB  . SER B 1 141 ? 58.226  -10.454 123.456 1.00 99.89  ? 150  SER B CB  1 
ATOM   4023  O OG  . SER B 1 141 ? 59.073  -11.228 122.626 1.00 100.39 ? 150  SER B OG  1 
ATOM   4024  N N   . GLY B 1 142 ? 59.197  -7.841  123.006 1.00 96.80  ? 151  GLY B N   1 
ATOM   4025  C CA  . GLY B 1 142 ? 60.142  -6.745  122.785 1.00 95.91  ? 151  GLY B CA  1 
ATOM   4026  C C   . GLY B 1 142 ? 59.428  -5.439  122.502 1.00 93.94  ? 151  GLY B C   1 
ATOM   4027  O O   . GLY B 1 142 ? 58.965  -5.231  121.360 1.00 92.27  ? 151  GLY B O   1 
ATOM   4028  N N   . VAL B 1 143 ? 59.372  -4.547  123.510 1.00 94.20  ? 152  VAL B N   1 
ATOM   4029  C CA  . VAL B 1 143 ? 58.486  -3.340  123.463 1.00 92.70  ? 152  VAL B CA  1 
ATOM   4030  C C   . VAL B 1 143 ? 57.857  -3.056  122.070 1.00 90.62  ? 152  VAL B C   1 
ATOM   4031  O O   . VAL B 1 143 ? 58.527  -2.696  121.067 1.00 89.57  ? 152  VAL B O   1 
ATOM   4032  C CB  . VAL B 1 143 ? 59.056  -2.039  124.166 1.00 92.78  ? 152  VAL B CB  1 
ATOM   4033  C CG1 . VAL B 1 143 ? 59.469  -0.965  123.117 1.00 91.08  ? 152  VAL B CG1 1 
ATOM   4034  C CG2 . VAL B 1 143 ? 58.012  -1.441  125.132 1.00 92.99  ? 152  VAL B CG2 1 
ATOM   4035  N N   . ALA B 1 144 ? 56.544  -3.246  122.069 1.00 90.20  ? 153  ALA B N   1 
ATOM   4036  C CA  . ALA B 1 144 ? 55.776  -3.377  120.871 1.00 88.67  ? 153  ALA B CA  1 
ATOM   4037  C C   . ALA B 1 144 ? 54.931  -2.130  120.622 1.00 87.11  ? 153  ALA B C   1 
ATOM   4038  O O   . ALA B 1 144 ? 54.445  -1.918  119.527 1.00 85.56  ? 153  ALA B O   1 
ATOM   4039  C CB  . ALA B 1 144 ? 54.916  -4.602  121.008 1.00 89.56  ? 153  ALA B CB  1 
ATOM   4040  N N   . VAL B 1 145 ? 54.779  -1.296  121.643 1.00 87.64  ? 154  VAL B N   1 
ATOM   4041  C CA  . VAL B 1 145 ? 54.008  -0.076  121.532 1.00 86.50  ? 154  VAL B CA  1 
ATOM   4042  C C   . VAL B 1 145 ? 54.601  0.614   120.375 1.00 84.94  ? 154  VAL B C   1 
ATOM   4043  O O   . VAL B 1 145 ? 53.935  1.362   119.691 1.00 83.54  ? 154  VAL B O   1 
ATOM   4044  C CB  . VAL B 1 145 ? 54.250  0.893   122.675 1.00 87.36  ? 154  VAL B CB  1 
ATOM   4045  C CG1 . VAL B 1 145 ? 52.969  1.526   123.066 1.00 87.20  ? 154  VAL B CG1 1 
ATOM   4046  C CG2 . VAL B 1 145 ? 54.941  0.215   123.891 1.00 89.39  ? 154  VAL B CG2 1 
ATOM   4047  N N   . SER B 1 146 ? 55.891  0.356   120.175 1.00 85.33  ? 155  SER B N   1 
ATOM   4048  C CA  . SER B 1 146 ? 56.686  1.008   119.150 1.00 84.18  ? 155  SER B CA  1 
ATOM   4049  C C   . SER B 1 146 ? 56.032  0.680   117.824 1.00 82.63  ? 155  SER B C   1 
ATOM   4050  O O   . SER B 1 146 ? 55.353  1.531   117.251 1.00 81.26  ? 155  SER B O   1 
ATOM   4051  C CB  . SER B 1 146 ? 58.126  0.519   119.225 1.00 85.23  ? 155  SER B CB  1 
ATOM   4052  O OG  . SER B 1 146 ? 58.437  0.072   120.540 1.00 87.07  ? 155  SER B OG  1 
ATOM   4053  N N   . LYS B 1 147 ? 56.164  -0.571  117.388 1.00 82.98  ? 156  LYS B N   1 
ATOM   4054  C CA  . LYS B 1 147 ? 55.563  -1.070  116.137 1.00 81.73  ? 156  LYS B CA  1 
ATOM   4055  C C   . LYS B 1 147 ? 54.216  -0.435  115.813 1.00 80.41  ? 156  LYS B C   1 
ATOM   4056  O O   . LYS B 1 147 ? 53.972  -0.008  114.684 1.00 78.85  ? 156  LYS B O   1 
ATOM   4057  C CB  . LYS B 1 147 ? 55.410  -2.586  116.193 1.00 82.83  ? 156  LYS B CB  1 
ATOM   4058  C CG  . LYS B 1 147 ? 56.631  -3.269  116.779 1.00 84.55  ? 156  LYS B CG  1 
ATOM   4059  C CD  . LYS B 1 147 ? 56.367  -4.679  117.284 1.00 86.17  ? 156  LYS B CD  1 
ATOM   4060  C CE  . LYS B 1 147 ? 56.144  -5.655  116.142 1.00 85.81  ? 156  LYS B CE  1 
ATOM   4061  N NZ  . LYS B 1 147 ? 57.118  -5.444  115.047 1.00 84.99  ? 156  LYS B NZ  1 
ATOM   4062  N N   . VAL B 1 148 ? 53.355  -0.361  116.817 1.00 81.14  ? 157  VAL B N   1 
ATOM   4063  C CA  . VAL B 1 148 ? 52.040  0.240   116.662 1.00 80.22  ? 157  VAL B CA  1 
ATOM   4064  C C   . VAL B 1 148 ? 52.098  1.559   115.873 1.00 78.62  ? 157  VAL B C   1 
ATOM   4065  O O   . VAL B 1 148 ? 51.403  1.729   114.855 1.00 77.22  ? 157  VAL B O   1 
ATOM   4066  C CB  . VAL B 1 148 ? 51.339  0.413   118.040 1.00 81.51  ? 157  VAL B CB  1 
ATOM   4067  C CG1 . VAL B 1 148 ? 50.116  1.335   117.964 1.00 80.70  ? 157  VAL B CG1 1 
ATOM   4068  C CG2 . VAL B 1 148 ? 50.945  -0.940  118.583 1.00 82.91  ? 157  VAL B CG2 1 
ATOM   4069  N N   . LEU B 1 149 ? 52.949  2.474   116.319 1.00 78.91  ? 158  LEU B N   1 
ATOM   4070  C CA  . LEU B 1 149 ? 52.937  3.820   115.769 1.00 77.74  ? 158  LEU B CA  1 
ATOM   4071  C C   . LEU B 1 149 ? 53.542  3.854   114.382 1.00 76.44  ? 158  LEU B C   1 
ATOM   4072  O O   . LEU B 1 149 ? 53.168  4.696   113.552 1.00 75.12  ? 158  LEU B O   1 
ATOM   4073  C CB  . LEU B 1 149 ? 53.683  4.754   116.699 1.00 78.70  ? 158  LEU B CB  1 
ATOM   4074  C CG  . LEU B 1 149 ? 53.193  4.617   118.134 1.00 80.19  ? 158  LEU B CG  1 
ATOM   4075  C CD1 . LEU B 1 149 ? 54.353  4.270   119.034 1.00 81.70  ? 158  LEU B CD1 1 
ATOM   4076  C CD2 . LEU B 1 149 ? 52.448  5.870   118.583 1.00 80.16  ? 158  LEU B CD2 1 
ATOM   4077  N N   . HIS B 1 150 ? 54.473  2.933   114.132 1.00 77.01  ? 159  HIS B N   1 
ATOM   4078  C CA  . HIS B 1 150 ? 55.073  2.808   112.804 1.00 77.42  ? 159  HIS B CA  1 
ATOM   4079  C C   . HIS B 1 150 ? 54.048  2.242   111.833 1.00 76.30  ? 159  HIS B C   1 
ATOM   4080  O O   . HIS B 1 150 ? 54.093  2.566   110.627 1.00 75.18  ? 159  HIS B O   1 
ATOM   4081  C CB  . HIS B 1 150 ? 56.356  1.956   112.815 1.00 79.19  ? 159  HIS B CB  1 
ATOM   4082  C CG  . HIS B 1 150 ? 56.746  1.439   111.463 1.00 80.50  ? 159  HIS B CG  1 
ATOM   4083  N ND1 . HIS B 1 150 ? 56.668  0.102   111.126 1.00 83.13  ? 159  HIS B ND1 1 
ATOM   4084  C CD2 . HIS B 1 150 ? 57.177  2.083   110.353 1.00 80.97  ? 159  HIS B CD2 1 
ATOM   4085  C CE1 . HIS B 1 150 ? 57.059  -0.059  109.876 1.00 83.37  ? 159  HIS B CE1 1 
ATOM   4086  N NE2 . HIS B 1 150 ? 57.372  1.128   109.384 1.00 82.49  ? 159  HIS B NE2 1 
ATOM   4087  N N   . LEU B 1 151 ? 53.145  1.409   112.383 1.00 76.67  ? 160  LEU B N   1 
ATOM   4088  C CA  . LEU B 1 151 ? 51.984  0.849   111.678 1.00 75.14  ? 160  LEU B CA  1 
ATOM   4089  C C   . LEU B 1 151 ? 50.890  1.856   111.515 1.00 74.27  ? 160  LEU B C   1 
ATOM   4090  O O   . LEU B 1 151 ? 50.107  1.769   110.602 1.00 72.93  ? 160  LEU B O   1 
ATOM   4091  C CB  . LEU B 1 151 ? 51.421  -0.332  112.434 1.00 75.88  ? 160  LEU B CB  1 
ATOM   4092  C CG  . LEU B 1 151 ? 51.967  -1.666  111.984 1.00 76.46  ? 160  LEU B CG  1 
ATOM   4093  C CD1 . LEU B 1 151 ? 53.332  -1.901  112.581 1.00 77.74  ? 160  LEU B CD1 1 
ATOM   4094  C CD2 . LEU B 1 151 ? 51.014  -2.725  112.424 1.00 77.45  ? 160  LEU B CD2 1 
ATOM   4095  N N   . GLU B 1 152 ? 50.837  2.810   112.416 1.00 75.53  ? 161  GLU B N   1 
ATOM   4096  C CA  . GLU B 1 152 ? 49.859  3.857   112.341 1.00 76.31  ? 161  GLU B CA  1 
ATOM   4097  C C   . GLU B 1 152 ? 50.148  4.825   111.191 1.00 75.52  ? 161  GLU B C   1 
ATOM   4098  O O   . GLU B 1 152 ? 49.228  5.282   110.512 1.00 74.24  ? 161  GLU B O   1 
ATOM   4099  C CB  . GLU B 1 152 ? 49.875  4.590   113.660 1.00 77.91  ? 161  GLU B CB  1 
ATOM   4100  C CG  . GLU B 1 152 ? 48.648  5.418   113.981 1.00 79.32  ? 161  GLU B CG  1 
ATOM   4101  C CD  . GLU B 1 152 ? 48.717  5.967   115.412 1.00 83.57  ? 161  GLU B CD  1 
ATOM   4102  O OE1 . GLU B 1 152 ? 49.612  5.541   116.207 1.00 84.96  ? 161  GLU B OE1 1 
ATOM   4103  O OE2 . GLU B 1 152 ? 47.878  6.834   115.733 1.00 84.78  ? 161  GLU B OE2 1 
ATOM   4104  N N   . GLY B 1 153 ? 51.423  5.163   110.998 1.00 76.67  ? 162  GLY B N   1 
ATOM   4105  C CA  . GLY B 1 153 ? 51.843  5.920   109.818 1.00 77.01  ? 162  GLY B CA  1 
ATOM   4106  C C   . GLY B 1 153 ? 51.634  5.083   108.570 1.00 76.95  ? 162  GLY B C   1 
ATOM   4107  O O   . GLY B 1 153 ? 51.158  5.570   107.545 1.00 75.61  ? 162  GLY B O   1 
ATOM   4108  N N   . GLU B 1 154 ? 51.981  3.806   108.677 1.00 78.76  ? 163  GLU B N   1 
ATOM   4109  C CA  . GLU B 1 154 ? 51.812  2.870   107.587 1.00 79.32  ? 163  GLU B CA  1 
ATOM   4110  C C   . GLU B 1 154 ? 50.349  2.833   107.179 1.00 78.31  ? 163  GLU B C   1 
ATOM   4111  O O   . GLU B 1 154 ? 50.017  3.120   106.038 1.00 77.16  ? 163  GLU B O   1 
ATOM   4112  C CB  . GLU B 1 154 ? 52.288  1.482   108.000 1.00 81.26  ? 163  GLU B CB  1 
ATOM   4113  C CG  . GLU B 1 154 ? 53.185  0.804   106.972 1.00 84.75  ? 163  GLU B CG  1 
ATOM   4114  C CD  . GLU B 1 154 ? 54.659  1.247   107.058 1.00 90.26  ? 163  GLU B CD  1 
ATOM   4115  O OE1 . GLU B 1 154 ? 55.257  1.098   108.158 1.00 92.34  ? 163  GLU B OE1 1 
ATOM   4116  O OE2 . GLU B 1 154 ? 55.213  1.726   106.022 1.00 90.56  ? 163  GLU B OE2 1 
ATOM   4117  N N   . VAL B 1 155 ? 49.467  2.510   108.119 1.00 79.28  ? 164  VAL B N   1 
ATOM   4118  C CA  . VAL B 1 155 ? 48.040  2.529   107.845 1.00 78.80  ? 164  VAL B CA  1 
ATOM   4119  C C   . VAL B 1 155 ? 47.722  3.792   107.091 1.00 77.84  ? 164  VAL B C   1 
ATOM   4120  O O   . VAL B 1 155 ? 47.065  3.758   106.059 1.00 76.74  ? 164  VAL B O   1 
ATOM   4121  C CB  . VAL B 1 155 ? 47.220  2.528   109.134 1.00 79.94  ? 164  VAL B CB  1 
ATOM   4122  C CG1 . VAL B 1 155 ? 45.847  3.199   108.920 1.00 78.97  ? 164  VAL B CG1 1 
ATOM   4123  C CG2 . VAL B 1 155 ? 47.075  1.118   109.661 1.00 81.03  ? 164  VAL B CG2 1 
ATOM   4124  N N   . ASN B 1 156 ? 48.240  4.903   107.594 1.00 78.60  ? 165  ASN B N   1 
ATOM   4125  C CA  . ASN B 1 156 ? 47.832  6.201   107.109 1.00 78.19  ? 165  ASN B CA  1 
ATOM   4126  C C   . ASN B 1 156 ? 48.208  6.457   105.667 1.00 76.35  ? 165  ASN B C   1 
ATOM   4127  O O   . ASN B 1 156 ? 47.461  7.110   104.929 1.00 75.16  ? 165  ASN B O   1 
ATOM   4128  C CB  . ASN B 1 156 ? 48.344  7.302   108.028 1.00 79.57  ? 165  ASN B CB  1 
ATOM   4129  C CG  . ASN B 1 156 ? 47.215  8.194   108.516 1.00 81.60  ? 165  ASN B CG  1 
ATOM   4130  O OD1 . ASN B 1 156 ? 46.911  8.257   109.736 1.00 83.77  ? 165  ASN B OD1 1 
ATOM   4131  N ND2 . ASN B 1 156 ? 46.538  8.859   107.553 1.00 82.08  ? 165  ASN B ND2 1 
ATOM   4132  N N   . LYS B 1 157 ? 49.358  5.921   105.278 1.00 76.14  ? 166  LYS B N   1 
ATOM   4133  C CA  . LYS B 1 157 ? 49.745  5.872   103.884 1.00 74.85  ? 166  LYS B CA  1 
ATOM   4134  C C   . LYS B 1 157 ? 48.702  5.083   103.095 1.00 73.64  ? 166  LYS B C   1 
ATOM   4135  O O   . LYS B 1 157 ? 48.039  5.619   102.200 1.00 72.46  ? 166  LYS B O   1 
ATOM   4136  C CB  . LYS B 1 157 ? 51.144  5.259   103.731 1.00 75.65  ? 166  LYS B CB  1 
ATOM   4137  C CG  . LYS B 1 157 ? 52.277  6.294   103.678 1.00 77.08  ? 166  LYS B CG  1 
ATOM   4138  C CD  . LYS B 1 157 ? 53.618  5.727   104.126 1.00 80.73  ? 166  LYS B CD  1 
ATOM   4139  C CE  . LYS B 1 157 ? 54.626  6.845   104.431 1.00 82.31  ? 166  LYS B CE  1 
ATOM   4140  N NZ  . LYS B 1 157 ? 55.363  6.610   105.722 1.00 84.23  ? 166  LYS B NZ  1 
ATOM   4141  N N   . ILE B 1 158 ? 48.528  3.821   103.449 1.00 74.02  ? 167  ILE B N   1 
ATOM   4142  C CA  . ILE B 1 158 ? 47.603  2.971   102.724 1.00 73.29  ? 167  ILE B CA  1 
ATOM   4143  C C   . ILE B 1 158 ? 46.267  3.655   102.472 1.00 72.67  ? 167  ILE B C   1 
ATOM   4144  O O   . ILE B 1 158 ? 45.768  3.628   101.354 1.00 71.42  ? 167  ILE B O   1 
ATOM   4145  C CB  . ILE B 1 158 ? 47.444  1.623   103.415 1.00 74.53  ? 167  ILE B CB  1 
ATOM   4146  C CG1 . ILE B 1 158 ? 48.686  0.798   103.134 1.00 75.05  ? 167  ILE B CG1 1 
ATOM   4147  C CG2 . ILE B 1 158 ? 46.215  0.870   102.927 1.00 73.45  ? 167  ILE B CG2 1 
ATOM   4148  C CD1 . ILE B 1 158 ? 48.751  -0.485  103.893 1.00 77.76  ? 167  ILE B CD1 1 
ATOM   4149  N N   . LYS B 1 159 ? 45.708  4.289   103.496 1.00 73.65  ? 168  LYS B N   1 
ATOM   4150  C CA  . LYS B 1 159 ? 44.466  4.997   103.324 1.00 73.53  ? 168  LYS B CA  1 
ATOM   4151  C C   . LYS B 1 159 ? 44.620  5.874   102.112 1.00 72.01  ? 168  LYS B C   1 
ATOM   4152  O O   . LYS B 1 159 ? 43.916  5.696   101.128 1.00 71.10  ? 168  LYS B O   1 
ATOM   4153  C CB  . LYS B 1 159 ? 44.132  5.858   104.533 1.00 74.85  ? 168  LYS B CB  1 
ATOM   4154  C CG  . LYS B 1 159 ? 42.982  6.827   104.246 1.00 76.37  ? 168  LYS B CG  1 
ATOM   4155  C CD  . LYS B 1 159 ? 42.767  7.894   105.332 1.00 80.58  ? 168  LYS B CD  1 
ATOM   4156  C CE  . LYS B 1 159 ? 41.839  9.020   104.812 1.00 80.71  ? 168  LYS B CE  1 
ATOM   4157  N NZ  . LYS B 1 159 ? 41.105  9.732   105.907 1.00 82.72  ? 168  LYS B NZ  1 
ATOM   4158  N N   . SER B 1 160 ? 45.568  6.802   102.165 1.00 72.11  ? 169  SER B N   1 
ATOM   4159  C CA  . SER B 1 160 ? 45.745  7.768   101.077 1.00 71.19  ? 169  SER B CA  1 
ATOM   4160  C C   . SER B 1 160 ? 45.928  7.098   99.729  1.00 70.03  ? 169  SER B C   1 
ATOM   4161  O O   . SER B 1 160 ? 45.315  7.513   98.733  1.00 69.10  ? 169  SER B O   1 
ATOM   4162  C CB  . SER B 1 160 ? 46.920  8.688   101.352 1.00 71.49  ? 169  SER B CB  1 
ATOM   4163  O OG  . SER B 1 160 ? 46.649  9.461   102.497 1.00 73.66  ? 169  SER B OG  1 
ATOM   4164  N N   . ALA B 1 161 ? 46.756  6.057   99.710  1.00 70.23  ? 170  ALA B N   1 
ATOM   4165  C CA  . ALA B 1 161 ? 46.991  5.289   98.498  1.00 69.26  ? 170  ALA B CA  1 
ATOM   4166  C C   . ALA B 1 161 ? 45.708  4.674   97.919  1.00 68.51  ? 170  ALA B C   1 
ATOM   4167  O O   . ALA B 1 161 ? 45.480  4.721   96.713  1.00 67.27  ? 170  ALA B O   1 
ATOM   4168  C CB  . ALA B 1 161 ? 48.006  4.230   98.767  1.00 70.31  ? 170  ALA B CB  1 
ATOM   4169  N N   . LEU B 1 162 ? 44.875  4.106   98.778  1.00 69.16  ? 171  LEU B N   1 
ATOM   4170  C CA  . LEU B 1 162 ? 43.645  3.526   98.321  1.00 68.77  ? 171  LEU B CA  1 
ATOM   4171  C C   . LEU B 1 162 ? 42.697  4.571   97.761  1.00 67.84  ? 171  LEU B C   1 
ATOM   4172  O O   . LEU B 1 162 ? 42.024  4.309   96.775  1.00 67.35  ? 171  LEU B O   1 
ATOM   4173  C CB  . LEU B 1 162 ? 42.957  2.760   99.439  1.00 70.22  ? 171  LEU B CB  1 
ATOM   4174  C CG  . LEU B 1 162 ? 41.612  2.150   99.007  1.00 70.04  ? 171  LEU B CG  1 
ATOM   4175  C CD1 . LEU B 1 162 ? 41.869  0.970   98.133  1.00 70.33  ? 171  LEU B CD1 1 
ATOM   4176  C CD2 . LEU B 1 162 ? 40.723  1.723   100.171 1.00 71.68  ? 171  LEU B CD2 1 
ATOM   4177  N N   . LEU B 1 163 ? 42.621  5.741   98.388  1.00 68.03  ? 172  LEU B N   1 
ATOM   4178  C CA  . LEU B 1 163 ? 41.737  6.804   97.894  1.00 67.34  ? 172  LEU B CA  1 
ATOM   4179  C C   . LEU B 1 163 ? 42.111  7.161   96.456  1.00 65.88  ? 172  LEU B C   1 
ATOM   4180  O O   . LEU B 1 163 ? 41.241  7.338   95.584  1.00 64.80  ? 172  LEU B O   1 
ATOM   4181  C CB  . LEU B 1 163 ? 41.878  8.048   98.753  1.00 67.90  ? 172  LEU B CB  1 
ATOM   4182  C CG  . LEU B 1 163 ? 41.465  7.935   100.201 1.00 69.69  ? 172  LEU B CG  1 
ATOM   4183  C CD1 . LEU B 1 163 ? 42.174  9.011   101.010 1.00 71.92  ? 172  LEU B CD1 1 
ATOM   4184  C CD2 . LEU B 1 163 ? 39.955  8.036   100.307 1.00 69.93  ? 172  LEU B CD2 1 
ATOM   4185  N N   . SER B 1 164 ? 43.428  7.251   96.247  1.00 65.57  ? 173  SER B N   1 
ATOM   4186  C CA  . SER B 1 164 ? 44.031  7.531   94.963  1.00 64.10  ? 173  SER B CA  1 
ATOM   4187  C C   . SER B 1 164 ? 43.582  6.479   93.964  1.00 63.19  ? 173  SER B C   1 
ATOM   4188  O O   . SER B 1 164 ? 43.156  6.799   92.865  1.00 62.12  ? 173  SER B O   1 
ATOM   4189  C CB  . SER B 1 164 ? 45.545  7.515   95.110  0.82 64.57  ? 173  SER B CB  1 
ATOM   4190  O OG  . SER B 1 164 ? 46.125  8.626   94.462  0.82 64.04  ? 173  SER B OG  1 
ATOM   4191  N N   . THR B 1 165 ? 43.649  5.221   94.363  1.00 63.80  ? 174  THR B N   1 
ATOM   4192  C CA  . THR B 1 165 ? 43.136  4.141   93.535  1.00 63.41  ? 174  THR B CA  1 
ATOM   4193  C C   . THR B 1 165 ? 41.646  4.311   93.235  1.00 62.79  ? 174  THR B C   1 
ATOM   4194  O O   . THR B 1 165 ? 41.221  4.162   92.102  1.00 61.84  ? 174  THR B O   1 
ATOM   4195  C CB  . THR B 1 165 ? 43.391  2.762   94.185  1.00 64.89  ? 174  THR B CB  1 
ATOM   4196  O OG1 . THR B 1 165 ? 44.806  2.512   94.262  1.00 65.38  ? 174  THR B OG1 1 
ATOM   4197  C CG2 . THR B 1 165 ? 42.696  1.643   93.396  1.00 64.21  ? 174  THR B CG2 1 
ATOM   4198  N N   . ASN B 1 166 ? 40.854  4.625   94.249  1.00 63.58  ? 175  ASN B N   1 
ATOM   4199  C CA  . ASN B 1 166 ? 39.436  4.781   94.038  1.00 63.57  ? 175  ASN B CA  1 
ATOM   4200  C C   . ASN B 1 166 ? 39.166  5.769   92.930  1.00 62.21  ? 175  ASN B C   1 
ATOM   4201  O O   . ASN B 1 166 ? 38.429  5.463   91.990  1.00 61.44  ? 175  ASN B O   1 
ATOM   4202  C CB  . ASN B 1 166 ? 38.760  5.174   95.333  1.00 64.81  ? 175  ASN B CB  1 
ATOM   4203  C CG  . ASN B 1 166 ? 38.611  3.994   96.268  1.00 67.14  ? 175  ASN B CG  1 
ATOM   4204  O OD1 . ASN B 1 166 ? 39.064  2.890   95.958  1.00 67.91  ? 175  ASN B OD1 1 
ATOM   4205  N ND2 . ASN B 1 166 ? 37.961  4.209   97.413  1.00 69.45  ? 175  ASN B ND2 1 
ATOM   4206  N N   . LYS B 1 167 ? 39.822  6.923   93.023  1.00 61.99  ? 176  LYS B N   1 
ATOM   4207  C CA  . LYS B 1 167 ? 39.733  7.971   92.013  1.00 60.98  ? 176  LYS B CA  1 
ATOM   4208  C C   . LYS B 1 167 ? 40.225  7.524   90.657  1.00 59.60  ? 176  LYS B C   1 
ATOM   4209  O O   . LYS B 1 167 ? 39.773  8.041   89.631  1.00 58.74  ? 176  LYS B O   1 
ATOM   4210  C CB  . LYS B 1 167 ? 40.556  9.169   92.430  1.00 61.42  ? 176  LYS B CB  1 
ATOM   4211  C CG  . LYS B 1 167 ? 39.943  9.935   93.539  1.00 63.97  ? 176  LYS B CG  1 
ATOM   4212  C CD  . LYS B 1 167 ? 40.934  10.929  94.074  1.00 66.78  ? 176  LYS B CD  1 
ATOM   4213  C CE  . LYS B 1 167 ? 40.189  12.077  94.744  1.00 69.09  ? 176  LYS B CE  1 
ATOM   4214  N NZ  . LYS B 1 167 ? 41.140  12.890  95.541  1.00 71.28  ? 176  LYS B NZ  1 
ATOM   4215  N N   . ALA B 1 168 ? 41.165  6.587   90.649  1.00 59.44  ? 177  ALA B N   1 
ATOM   4216  C CA  . ALA B 1 168 ? 41.608  5.998   89.400  1.00 58.20  ? 177  ALA B CA  1 
ATOM   4217  C C   . ALA B 1 168 ? 40.498  5.186   88.784  1.00 57.60  ? 177  ALA B C   1 
ATOM   4218  O O   . ALA B 1 168 ? 40.308  5.249   87.587  1.00 56.89  ? 177  ALA B O   1 
ATOM   4219  C CB  . ALA B 1 168 ? 42.792  5.144   89.608  1.00 59.07  ? 177  ALA B CB  1 
ATOM   4220  N N   . VAL B 1 169 ? 39.758  4.435   89.598  1.00 57.94  ? 178  VAL B N   1 
ATOM   4221  C CA  . VAL B 1 169 ? 38.694  3.589   89.084  1.00 57.17  ? 178  VAL B CA  1 
ATOM   4222  C C   . VAL B 1 169 ? 37.532  4.438   88.628  1.00 56.55  ? 178  VAL B C   1 
ATOM   4223  O O   . VAL B 1 169 ? 36.846  4.097   87.670  1.00 56.16  ? 178  VAL B O   1 
ATOM   4224  C CB  . VAL B 1 169 ? 38.265  2.539   90.094  1.00 58.41  ? 178  VAL B CB  1 
ATOM   4225  C CG1 . VAL B 1 169 ? 36.932  1.958   89.727  1.00 58.01  ? 178  VAL B CG1 1 
ATOM   4226  C CG2 . VAL B 1 169 ? 39.274  1.437   90.113  1.00 58.76  ? 178  VAL B CG2 1 
ATOM   4227  N N   . VAL B 1 170 ? 37.327  5.563   89.294  1.00 56.81  ? 179  VAL B N   1 
ATOM   4228  C CA  . VAL B 1 170 ? 36.336  6.533   88.837  1.00 56.44  ? 179  VAL B CA  1 
ATOM   4229  C C   . VAL B 1 170 ? 36.702  7.034   87.448  1.00 54.69  ? 179  VAL B C   1 
ATOM   4230  O O   . VAL B 1 170 ? 35.910  6.917   86.529  1.00 53.82  ? 179  VAL B O   1 
ATOM   4231  C CB  . VAL B 1 170 ? 36.151  7.710   89.836  1.00 57.30  ? 179  VAL B CB  1 
ATOM   4232  C CG1 . VAL B 1 170 ? 35.600  8.942   89.140  1.00 57.09  ? 179  VAL B CG1 1 
ATOM   4233  C CG2 . VAL B 1 170 ? 35.237  7.291   90.990  1.00 59.05  ? 179  VAL B CG2 1 
ATOM   4234  N N   . SER B 1 171 ? 37.905  7.561   87.291  1.00 54.20  ? 180  SER B N   1 
ATOM   4235  C CA  . SER B 1 171 ? 38.317  7.982   85.987  0.75 53.37  ? 180  SER B CA  1 
ATOM   4236  C C   . SER B 1 171 ? 37.995  6.924   84.954  1.00 53.21  ? 180  SER B C   1 
ATOM   4237  O O   . SER B 1 171 ? 37.244  7.200   84.026  1.00 53.06  ? 180  SER B O   1 
ATOM   4238  C CB  . SER B 1 171 ? 39.780  8.345   85.950  0.75 53.26  ? 180  SER B CB  1 
ATOM   4239  O OG  . SER B 1 171 ? 39.915  9.745   85.976  0.75 52.92  ? 180  SER B OG  1 
ATOM   4240  N N   . LEU B 1 172 ? 38.510  5.710   85.115  1.00 53.88  ? 181  LEU B N   1 
ATOM   4241  C CA  . LEU B 1 172 ? 38.291  4.667   84.109  1.00 53.62  ? 181  LEU B CA  1 
ATOM   4242  C C   . LEU B 1 172 ? 36.802  4.403   83.855  1.00 53.89  ? 181  LEU B C   1 
ATOM   4243  O O   . LEU B 1 172 ? 36.363  4.260   82.707  1.00 53.23  ? 181  LEU B O   1 
ATOM   4244  C CB  . LEU B 1 172 ? 39.009  3.374   84.482  1.00 54.40  ? 181  LEU B CB  1 
ATOM   4245  C CG  . LEU B 1 172 ? 39.278  2.437   83.315  1.00 53.52  ? 181  LEU B CG  1 
ATOM   4246  C CD1 . LEU B 1 172 ? 40.301  3.072   82.438  1.00 53.60  ? 181  LEU B CD1 1 
ATOM   4247  C CD2 . LEU B 1 172 ? 39.751  1.072   83.743  1.00 53.69  ? 181  LEU B CD2 1 
ATOM   4248  N N   . SER B 1 173 ? 36.021  4.356   84.922  1.00 55.01  ? 182  SER B N   1 
ATOM   4249  C CA  . SER B 1 173 ? 34.604  4.138   84.776  1.00 55.64  ? 182  SER B CA  1 
ATOM   4250  C C   . SER B 1 173 ? 33.986  5.167   83.849  1.00 54.94  ? 182  SER B C   1 
ATOM   4251  O O   . SER B 1 173 ? 33.214  4.819   82.967  1.00 54.66  ? 182  SER B O   1 
ATOM   4252  C CB  . SER B 1 173 ? 33.931  4.187   86.131  1.00 56.83  ? 182  SER B CB  1 
ATOM   4253  O OG  . SER B 1 173 ? 34.371  3.098   86.906  1.00 58.25  ? 182  SER B OG  1 
ATOM   4254  N N   . ASN B 1 174 ? 34.350  6.432   84.045  1.00 55.29  ? 183  ASN B N   1 
ATOM   4255  C CA  . ASN B 1 174 ? 33.816  7.538   83.247  1.00 55.03  ? 183  ASN B CA  1 
ATOM   4256  C C   . ASN B 1 174 ? 34.307  7.493   81.824  1.00 53.68  ? 183  ASN B C   1 
ATOM   4257  O O   . ASN B 1 174 ? 33.574  7.852   80.892  1.00 53.35  ? 183  ASN B O   1 
ATOM   4258  C CB  . ASN B 1 174 ? 34.152  8.876   83.893  1.00 55.63  ? 183  ASN B CB  1 
ATOM   4259  C CG  . ASN B 1 174 ? 33.483  9.033   85.257  1.00 58.97  ? 183  ASN B CG  1 
ATOM   4260  O OD1 . ASN B 1 174 ? 32.335  8.604   85.462  1.00 61.74  ? 183  ASN B OD1 1 
ATOM   4261  N ND2 . ASN B 1 174 ? 34.205  9.629   86.204  1.00 60.42  ? 183  ASN B ND2 1 
ATOM   4262  N N   . GLY B 1 175 ? 35.545  7.033   81.668  1.00 53.14  ? 184  GLY B N   1 
ATOM   4263  C CA  . GLY B 1 175 ? 36.093  6.727   80.360  1.00 51.64  ? 184  GLY B CA  1 
ATOM   4264  C C   . GLY B 1 175 ? 35.208  5.747   79.625  1.00 51.04  ? 184  GLY B C   1 
ATOM   4265  O O   . GLY B 1 175 ? 34.730  6.037   78.533  1.00 50.46  ? 184  GLY B O   1 
ATOM   4266  N N   . VAL B 1 176 ? 34.966  4.598   80.237  1.00 51.29  ? 185  VAL B N   1 
ATOM   4267  C CA  . VAL B 1 176 ? 34.137  3.590   79.622  1.00 50.86  ? 185  VAL B CA  1 
ATOM   4268  C C   . VAL B 1 176 ? 32.705  4.098   79.405  1.00 50.68  ? 185  VAL B C   1 
ATOM   4269  O O   . VAL B 1 176 ? 32.121  3.949   78.326  1.00 49.91  ? 185  VAL B O   1 
ATOM   4270  C CB  . VAL B 1 176 ? 34.153  2.348   80.471  1.00 52.07  ? 185  VAL B CB  1 
ATOM   4271  C CG1 . VAL B 1 176 ? 33.022  1.424   80.081  1.00 52.60  ? 185  VAL B CG1 1 
ATOM   4272  C CG2 . VAL B 1 176 ? 35.487  1.661   80.326  1.00 51.88  ? 185  VAL B CG2 1 
ATOM   4273  N N   . SER B 1 177 ? 32.149  4.719   80.438  1.00 51.34  ? 186  SER B N   1 
ATOM   4274  C CA  . SER B 1 177 ? 30.826  5.317   80.354  0.75 51.32  ? 186  SER B CA  1 
ATOM   4275  C C   . SER B 1 177 ? 30.718  6.090   79.043  1.00 49.75  ? 186  SER B C   1 
ATOM   4276  O O   . SER B 1 177 ? 29.670  6.100   78.405  1.00 49.87  ? 186  SER B O   1 
ATOM   4277  C CB  . SER B 1 177 ? 30.561  6.235   81.561  0.75 52.14  ? 186  SER B CB  1 
ATOM   4278  O OG  . SER B 1 177 ? 29.309  6.886   81.456  0.75 52.94  ? 186  SER B OG  1 
ATOM   4279  N N   . VAL B 1 178 ? 31.815  6.712   78.635  1.00 48.46  ? 187  VAL B N   1 
ATOM   4280  C CA  . VAL B 1 178 ? 31.799  7.530   77.450  1.00 47.01  ? 187  VAL B CA  1 
ATOM   4281  C C   . VAL B 1 178 ? 32.002  6.705   76.188  1.00 46.42  ? 187  VAL B C   1 
ATOM   4282  O O   . VAL B 1 178 ? 31.241  6.832   75.239  1.00 46.05  ? 187  VAL B O   1 
ATOM   4283  C CB  . VAL B 1 178 ? 32.802  8.679   77.560  1.00 46.34  ? 187  VAL B CB  1 
ATOM   4284  C CG1 . VAL B 1 178 ? 33.203  9.168   76.200  1.00 44.87  ? 187  VAL B CG1 1 
ATOM   4285  C CG2 . VAL B 1 178 ? 32.189  9.800   78.344  1.00 46.57  ? 187  VAL B CG2 1 
ATOM   4286  N N   . LEU B 1 179 ? 33.021  5.861   76.180  1.00 46.66  ? 188  LEU B N   1 
ATOM   4287  C CA  . LEU B 1 179 ? 33.274  4.984   75.049  1.00 46.17  ? 188  LEU B CA  1 
ATOM   4288  C C   . LEU B 1 179 ? 32.037  4.145   74.754  1.00 46.60  ? 188  LEU B C   1 
ATOM   4289  O O   . LEU B 1 179 ? 31.706  3.904   73.598  1.00 45.91  ? 188  LEU B O   1 
ATOM   4290  C CB  . LEU B 1 179 ? 34.467  4.078   75.337  1.00 46.77  ? 188  LEU B CB  1 
ATOM   4291  C CG  . LEU B 1 179 ? 34.951  3.194   74.197  1.00 46.39  ? 188  LEU B CG  1 
ATOM   4292  C CD1 . LEU B 1 179 ? 35.871  3.984   73.319  1.00 45.91  ? 188  LEU B CD1 1 
ATOM   4293  C CD2 . LEU B 1 179 ? 35.671  1.961   74.686  1.00 47.27  ? 188  LEU B CD2 1 
ATOM   4294  N N   . THR B 1 180 ? 31.351  3.711   75.806  1.00 47.84  ? 189  THR B N   1 
ATOM   4295  C CA  . THR B 1 180 ? 30.058  3.095   75.645  1.00 48.65  ? 189  THR B CA  1 
ATOM   4296  C C   . THR B 1 180 ? 29.103  4.079   74.971  1.00 48.24  ? 189  THR B C   1 
ATOM   4297  O O   . THR B 1 180 ? 28.646  3.823   73.854  1.00 47.72  ? 189  THR B O   1 
ATOM   4298  C CB  . THR B 1 180 ? 29.515  2.672   76.973  1.00 49.94  ? 189  THR B CB  1 
ATOM   4299  O OG1 . THR B 1 180 ? 30.274  1.554   77.421  1.00 50.75  ? 189  THR B OG1 1 
ATOM   4300  C CG2 . THR B 1 180 ? 28.051  2.282   76.846  1.00 51.04  ? 189  THR B CG2 1 
ATOM   4301  N N   . SER B 1 181 ? 28.835  5.212   75.628  1.00 48.58  ? 190  SER B N   1 
ATOM   4302  C CA  . SER B 1 181 ? 27.994  6.262   75.062  0.25 48.12  ? 190  SER B CA  1 
ATOM   4303  C C   . SER B 1 181 ? 28.253  6.441   73.561  1.00 47.10  ? 190  SER B C   1 
ATOM   4304  O O   . SER B 1 181 ? 27.338  6.728   72.799  1.00 47.04  ? 190  SER B O   1 
ATOM   4305  C CB  . SER B 1 181 ? 28.213  7.580   75.806  0.25 48.07  ? 190  SER B CB  1 
ATOM   4306  O OG  . SER B 1 181 ? 27.389  8.600   75.283  0.25 47.52  ? 190  SER B OG  1 
ATOM   4307  N N   . LYS B 1 182 ? 29.488  6.222   73.129  1.00 46.67  ? 191  LYS B N   1 
ATOM   4308  C CA  . LYS B 1 182 ? 29.855  6.444   71.732  1.00 45.65  ? 191  LYS B CA  1 
ATOM   4309  C C   . LYS B 1 182 ? 29.666  5.265   70.821  1.00 45.41  ? 191  LYS B C   1 
ATOM   4310  O O   . LYS B 1 182 ? 29.346  5.446   69.657  1.00 44.89  ? 191  LYS B O   1 
ATOM   4311  C CB  . LYS B 1 182 ? 31.305  6.898   71.609  1.00 45.20  ? 191  LYS B CB  1 
ATOM   4312  C CG  . LYS B 1 182 ? 31.532  8.381   71.811  1.00 46.28  ? 191  LYS B CG  1 
ATOM   4313  C CD  . LYS B 1 182 ? 31.104  9.203   70.615  1.00 48.00  ? 191  LYS B CD  1 
ATOM   4314  C CE  . LYS B 1 182 ? 29.885  10.072  70.935  1.00 50.58  ? 191  LYS B CE  1 
ATOM   4315  N NZ  . LYS B 1 182 ? 29.669  11.152  69.916  1.00 51.87  ? 191  LYS B NZ  1 
ATOM   4316  N N   . VAL B 1 183 ? 29.913  4.065   71.323  1.00 46.03  ? 192  VAL B N   1 
ATOM   4317  C CA  . VAL B 1 183 ? 29.738  2.884   70.503  1.00 45.88  ? 192  VAL B CA  1 
ATOM   4318  C C   . VAL B 1 183 ? 28.277  2.720   70.163  1.00 46.23  ? 192  VAL B C   1 
ATOM   4319  O O   . VAL B 1 183 ? 27.942  2.204   69.104  1.00 46.16  ? 192  VAL B O   1 
ATOM   4320  C CB  . VAL B 1 183 ? 30.276  1.634   71.184  1.00 46.92  ? 192  VAL B CB  1 
ATOM   4321  C CG1 . VAL B 1 183 ? 29.601  0.364   70.663  1.00 47.16  ? 192  VAL B CG1 1 
ATOM   4322  C CG2 . VAL B 1 183 ? 31.729  1.556   70.944  1.00 46.77  ? 192  VAL B CG2 1 
ATOM   4323  N N   . LEU B 1 184 ? 27.405  3.174   71.050  1.00 46.90  ? 193  LEU B N   1 
ATOM   4324  C CA  . LEU B 1 184 ? 26.001  3.162   70.743  1.00 47.57  ? 193  LEU B CA  1 
ATOM   4325  C C   . LEU B 1 184 ? 25.802  3.997   69.500  1.00 46.73  ? 193  LEU B C   1 
ATOM   4326  O O   . LEU B 1 184 ? 25.282  3.525   68.505  1.00 46.83  ? 193  LEU B O   1 
ATOM   4327  C CB  . LEU B 1 184 ? 25.202  3.749   71.883  1.00 48.43  ? 193  LEU B CB  1 
ATOM   4328  C CG  . LEU B 1 184 ? 23.723  3.766   71.555  1.00 49.09  ? 193  LEU B CG  1 
ATOM   4329  C CD1 . LEU B 1 184 ? 23.149  2.408   71.855  1.00 50.00  ? 193  LEU B CD1 1 
ATOM   4330  C CD2 . LEU B 1 184 ? 23.006  4.869   72.324  1.00 50.43  ? 193  LEU B CD2 1 
ATOM   4331  N N   . ASP B 1 185 ? 26.260  5.235   69.548  1.00 46.60  ? 194  ASP B N   1 
ATOM   4332  C CA  . ASP B 1 185 ? 26.153  6.132   68.406  1.00 46.07  ? 194  ASP B CA  1 
ATOM   4333  C C   . ASP B 1 185 ? 26.674  5.556   67.105  1.00 45.11  ? 194  ASP B C   1 
ATOM   4334  O O   . ASP B 1 185 ? 26.040  5.703   66.070  1.00 44.60  ? 194  ASP B O   1 
ATOM   4335  C CB  . ASP B 1 185 ? 26.839  7.444   68.733  1.00 46.03  ? 194  ASP B CB  1 
ATOM   4336  C CG  . ASP B 1 185 ? 26.233  8.106   69.964  1.00 48.34  ? 194  ASP B CG  1 
ATOM   4337  O OD1 . ASP B 1 185 ? 25.190  7.608   70.481  1.00 50.05  ? 194  ASP B OD1 1 
ATOM   4338  O OD2 . ASP B 1 185 ? 26.802  9.127   70.408  1.00 49.65  ? 194  ASP B OD2 1 
ATOM   4339  N N   . LEU B 1 186 ? 27.815  4.890   67.161  1.00 45.14  ? 195  LEU B N   1 
ATOM   4340  C CA  . LEU B 1 186 ? 28.334  4.241   65.979  1.00 44.69  ? 195  LEU B CA  1 
ATOM   4341  C C   . LEU B 1 186 ? 27.305  3.273   65.455  1.00 45.24  ? 195  LEU B C   1 
ATOM   4342  O O   . LEU B 1 186 ? 26.963  3.326   64.276  1.00 44.65  ? 195  LEU B O   1 
ATOM   4343  C CB  . LEU B 1 186 ? 29.627  3.489   66.255  1.00 45.08  ? 195  LEU B CB  1 
ATOM   4344  C CG  . LEU B 1 186 ? 30.715  3.723   65.211  1.00 44.06  ? 195  LEU B CG  1 
ATOM   4345  C CD1 . LEU B 1 186 ? 31.536  2.479   64.950  1.00 44.35  ? 195  LEU B CD1 1 
ATOM   4346  C CD2 . LEU B 1 186 ? 30.110  4.186   63.937  1.00 43.10  ? 195  LEU B CD2 1 
ATOM   4347  N N   . LYS B 1 187 ? 26.810  2.391   66.322  1.00 46.54  ? 196  LYS B N   1 
ATOM   4348  C CA  . LYS B 1 187 ? 25.792  1.449   65.898  1.00 47.48  ? 196  LYS B CA  1 
ATOM   4349  C C   . LYS B 1 187 ? 24.662  2.253   65.318  1.00 47.25  ? 196  LYS B C   1 
ATOM   4350  O O   . LYS B 1 187 ? 24.216  1.982   64.215  1.00 47.22  ? 196  LYS B O   1 
ATOM   4351  C CB  . LYS B 1 187 ? 25.310  0.557   67.041  1.00 48.94  ? 196  LYS B CB  1 
ATOM   4352  C CG  . LYS B 1 187 ? 23.958  -0.122  66.812  1.00 49.23  ? 196  LYS B CG  1 
ATOM   4353  C CD  . LYS B 1 187 ? 22.816  0.704   67.401  1.00 49.53  ? 196  LYS B CD  1 
ATOM   4354  C CE  . LYS B 1 187 ? 21.471  0.008   67.280  1.00 51.58  ? 196  LYS B CE  1 
ATOM   4355  N NZ  . LYS B 1 187 ? 20.310  0.908   67.589  1.00 52.48  ? 196  LYS B NZ  1 
ATOM   4356  N N   . ASN B 1 188 ? 24.229  3.276   66.038  1.00 47.64  ? 197  ASN B N   1 
ATOM   4357  C CA  . ASN B 1 188 ? 23.069  4.024   65.596  1.00 48.01  ? 197  ASN B CA  1 
ATOM   4358  C C   . ASN B 1 188 ? 23.229  4.716   64.231  1.00 47.01  ? 197  ASN B C   1 
ATOM   4359  O O   . ASN B 1 188 ? 22.271  4.769   63.444  1.00 47.35  ? 197  ASN B O   1 
ATOM   4360  C CB  . ASN B 1 188 ? 22.547  4.950   66.693  1.00 48.52  ? 197  ASN B CB  1 
ATOM   4361  C CG  . ASN B 1 188 ? 21.474  4.286   67.529  1.00 50.93  ? 197  ASN B CG  1 
ATOM   4362  O OD1 . ASN B 1 188 ? 21.626  4.103   68.737  1.00 52.96  ? 197  ASN B OD1 1 
ATOM   4363  N ND2 . ASN B 1 188 ? 20.384  3.893   66.879  1.00 52.04  ? 197  ASN B ND2 1 
ATOM   4364  N N   . TYR B 1 189 ? 24.424  5.210   63.927  1.00 46.06  ? 198  TYR B N   1 
ATOM   4365  C CA  . TYR B 1 189 ? 24.659  5.718   62.594  1.00 44.95  ? 198  TYR B CA  1 
ATOM   4366  C C   . TYR B 1 189 ? 24.350  4.613   61.620  1.00 44.48  ? 198  TYR B C   1 
ATOM   4367  O O   . TYR B 1 189 ? 23.423  4.710   60.860  1.00 44.34  ? 198  TYR B O   1 
ATOM   4368  C CB  . TYR B 1 189 ? 26.094  6.173   62.410  1.00 44.86  ? 198  TYR B CB  1 
ATOM   4369  C CG  . TYR B 1 189 ? 26.280  7.078   61.218  1.00 45.61  ? 198  TYR B CG  1 
ATOM   4370  C CD1 . TYR B 1 189 ? 25.888  8.431   61.286  1.00 48.23  ? 198  TYR B CD1 1 
ATOM   4371  C CD2 . TYR B 1 189 ? 26.830  6.602   60.021  1.00 45.96  ? 198  TYR B CD2 1 
ATOM   4372  C CE1 . TYR B 1 189 ? 26.041  9.318   60.180  1.00 48.72  ? 198  TYR B CE1 1 
ATOM   4373  C CE2 . TYR B 1 189 ? 27.004  7.475   58.901  1.00 47.19  ? 198  TYR B CE2 1 
ATOM   4374  C CZ  . TYR B 1 189 ? 26.606  8.840   58.991  1.00 48.19  ? 198  TYR B CZ  1 
ATOM   4375  O OH  . TYR B 1 189 ? 26.750  9.722   57.922  1.00 47.15  ? 198  TYR B OH  1 
ATOM   4376  N N   . ILE B 1 190 ? 25.104  3.535   61.670  1.00 44.70  ? 199  ILE B N   1 
ATOM   4377  C CA  . ILE B 1 190 ? 24.812  2.410   60.811  1.00 45.02  ? 199  ILE B CA  1 
ATOM   4378  C C   . ILE B 1 190 ? 23.308  2.129   60.722  1.00 46.15  ? 199  ILE B C   1 
ATOM   4379  O O   . ILE B 1 190 ? 22.739  2.225   59.637  1.00 45.85  ? 199  ILE B O   1 
ATOM   4380  C CB  . ILE B 1 190 ? 25.583  1.160   61.226  1.00 45.61  ? 199  ILE B CB  1 
ATOM   4381  C CG1 . ILE B 1 190 ? 27.005  1.267   60.735  1.00 44.51  ? 199  ILE B CG1 1 
ATOM   4382  C CG2 . ILE B 1 190 ? 24.978  -0.081  60.620  1.00 46.00  ? 199  ILE B CG2 1 
ATOM   4383  C CD1 . ILE B 1 190 ? 27.924  0.438   61.512  1.00 45.28  ? 199  ILE B CD1 1 
ATOM   4384  N N   . ASP B 1 191 ? 22.658  1.807   61.843  1.00 47.91  ? 200  ASP B N   1 
ATOM   4385  C CA  . ASP B 1 191 ? 21.293  1.269   61.788  1.00 49.50  ? 200  ASP B CA  1 
ATOM   4386  C C   . ASP B 1 191 ? 20.348  2.306   61.271  1.00 48.77  ? 200  ASP B C   1 
ATOM   4387  O O   . ASP B 1 191 ? 19.485  1.997   60.464  1.00 48.92  ? 200  ASP B O   1 
ATOM   4388  C CB  . ASP B 1 191 ? 20.802  0.731   63.149  1.00 51.55  ? 200  ASP B CB  1 
ATOM   4389  C CG  . ASP B 1 191 ? 19.351  0.154   63.099  1.00 54.68  ? 200  ASP B CG  1 
ATOM   4390  O OD1 . ASP B 1 191 ? 18.993  -0.491  62.070  1.00 56.75  ? 200  ASP B OD1 1 
ATOM   4391  O OD2 . ASP B 1 191 ? 18.580  0.332   64.095  1.00 56.33  ? 200  ASP B OD2 1 
ATOM   4392  N N   . LYS B 1 192 ? 20.527  3.539   61.717  1.00 48.27  ? 201  LYS B N   1 
ATOM   4393  C CA  . LYS B 1 192 ? 19.508  4.546   61.479  1.00 48.63  ? 201  LYS B CA  1 
ATOM   4394  C C   . LYS B 1 192 ? 19.891  5.679   60.484  1.00 47.35  ? 201  LYS B C   1 
ATOM   4395  O O   . LYS B 1 192 ? 19.119  6.608   60.230  1.00 47.25  ? 201  LYS B O   1 
ATOM   4396  C CB  . LYS B 1 192 ? 18.949  5.038   62.821  1.00 49.52  ? 201  LYS B CB  1 
ATOM   4397  C CG  . LYS B 1 192 ? 18.320  3.907   63.583  1.00 51.95  ? 201  LYS B CG  1 
ATOM   4398  C CD  . LYS B 1 192 ? 17.651  4.357   64.837  1.00 56.29  ? 201  LYS B CD  1 
ATOM   4399  C CE  . LYS B 1 192 ? 17.246  3.126   65.650  1.00 60.26  ? 201  LYS B CE  1 
ATOM   4400  N NZ  . LYS B 1 192 ? 16.893  3.430   67.075  1.00 63.48  ? 201  LYS B NZ  1 
ATOM   4401  N N   . GLN B 1 193 ? 21.057  5.565   59.870  1.00 46.75  ? 202  GLN B N   1 
ATOM   4402  C CA  . GLN B 1 193 ? 21.509  6.577   58.928  1.00 45.91  ? 202  GLN B CA  1 
ATOM   4403  C C   . GLN B 1 193 ? 21.911  5.924   57.627  1.00 44.80  ? 202  GLN B C   1 
ATOM   4404  O O   . GLN B 1 193 ? 21.238  6.101   56.604  1.00 44.53  ? 202  GLN B O   1 
ATOM   4405  C CB  . GLN B 1 193 ? 22.695  7.328   59.512  1.00 46.12  ? 202  GLN B CB  1 
ATOM   4406  C CG  . GLN B 1 193 ? 22.308  8.305   60.590  1.00 49.60  ? 202  GLN B CG  1 
ATOM   4407  C CD  . GLN B 1 193 ? 21.741  9.538   59.970  1.00 53.48  ? 202  GLN B CD  1 
ATOM   4408  O OE1 . GLN B 1 193 ? 22.255  10.006  58.942  1.00 54.68  ? 202  GLN B OE1 1 
ATOM   4409  N NE2 . GLN B 1 193 ? 20.659  10.070  60.554  1.00 55.35  ? 202  GLN B NE2 1 
ATOM   4410  N N   . LEU B 1 194 ? 23.000  5.157   57.683  1.00 44.10  ? 203  LEU B N   1 
ATOM   4411  C CA  . LEU B 1 194 ? 23.554  4.478   56.526  1.00 43.08  ? 203  LEU B CA  1 
ATOM   4412  C C   . LEU B 1 194 ? 22.651  3.385   55.997  1.00 43.64  ? 203  LEU B C   1 
ATOM   4413  O O   . LEU B 1 194 ? 22.243  3.414   54.840  1.00 43.04  ? 203  LEU B O   1 
ATOM   4414  C CB  . LEU B 1 194 ? 24.899  3.868   56.883  1.00 43.09  ? 203  LEU B CB  1 
ATOM   4415  C CG  . LEU B 1 194 ? 25.514  2.982   55.794  1.00 42.54  ? 203  LEU B CG  1 
ATOM   4416  C CD1 . LEU B 1 194 ? 26.424  3.804   54.932  1.00 41.91  ? 203  LEU B CD1 1 
ATOM   4417  C CD2 . LEU B 1 194 ? 26.286  1.819   56.378  1.00 43.17  ? 203  LEU B CD2 1 
ATOM   4418  N N   . LEU B 1 195 ? 22.346  2.430   56.867  1.00 44.85  ? 204  LEU B N   1 
ATOM   4419  C CA  . LEU B 1 195 ? 21.620  1.226   56.502  1.00 45.90  ? 204  LEU B CA  1 
ATOM   4420  C C   . LEU B 1 195 ? 20.330  1.449   55.728  1.00 45.88  ? 204  LEU B C   1 
ATOM   4421  O O   . LEU B 1 195 ? 20.039  0.668   54.840  1.00 46.63  ? 204  LEU B O   1 
ATOM   4422  C CB  . LEU B 1 195 ? 21.303  0.383   57.725  1.00 47.39  ? 204  LEU B CB  1 
ATOM   4423  C CG  . LEU B 1 195 ? 21.050  -1.098  57.433  1.00 49.17  ? 204  LEU B CG  1 
ATOM   4424  C CD1 . LEU B 1 195 ? 22.363  -1.780  57.132  1.00 48.66  ? 204  LEU B CD1 1 
ATOM   4425  C CD2 . LEU B 1 195 ? 20.334  -1.802  58.607  1.00 52.24  ? 204  LEU B CD2 1 
ATOM   4426  N N   . PRO B 1 196 ? 19.535  2.487   56.063  1.00 45.62  ? 205  PRO B N   1 
ATOM   4427  C CA  . PRO B 1 196 ? 18.385  2.797   55.194  1.00 45.37  ? 205  PRO B CA  1 
ATOM   4428  C C   . PRO B 1 196 ? 18.813  3.061   53.748  1.00 44.27  ? 205  PRO B C   1 
ATOM   4429  O O   . PRO B 1 196 ? 18.241  2.485   52.805  1.00 44.45  ? 205  PRO B O   1 
ATOM   4430  C CB  . PRO B 1 196 ? 17.827  4.087   55.796  1.00 44.91  ? 205  PRO B CB  1 
ATOM   4431  C CG  . PRO B 1 196 ? 18.203  4.021   57.205  1.00 45.93  ? 205  PRO B CG  1 
ATOM   4432  C CD  . PRO B 1 196 ? 19.530  3.313   57.282  1.00 45.79  ? 205  PRO B CD  1 
ATOM   4433  N N   . ILE B 1 197 ? 19.833  3.900   53.579  1.00 43.04  ? 206  ILE B N   1 
ATOM   4434  C CA  . ILE B 1 197 ? 20.141  4.386   52.254  1.00 41.83  ? 206  ILE B CA  1 
ATOM   4435  C C   . ILE B 1 197 ? 21.054  3.440   51.537  1.00 41.43  ? 206  ILE B C   1 
ATOM   4436  O O   . ILE B 1 197 ? 21.386  3.652   50.392  1.00 40.42  ? 206  ILE B O   1 
ATOM   4437  C CB  . ILE B 1 197 ? 20.607  5.881   52.220  1.00 41.00  ? 206  ILE B CB  1 
ATOM   4438  C CG1 . ILE B 1 197 ? 22.108  6.030   52.113  1.00 40.91  ? 206  ILE B CG1 1 
ATOM   4439  C CG2 . ILE B 1 197 ? 20.041  6.697   53.398  1.00 42.10  ? 206  ILE B CG2 1 
ATOM   4440  C CD1 . ILE B 1 197 ? 22.484  7.350   51.436  1.00 41.84  ? 206  ILE B CD1 1 
ATOM   4441  N N   . VAL B 1 198 ? 21.461  2.378   52.206  1.00 42.70  ? 207  VAL B N   1 
ATOM   4442  C CA  . VAL B 1 198 ? 22.126  1.313   51.473  1.00 43.64  ? 207  VAL B CA  1 
ATOM   4443  C C   . VAL B 1 198 ? 21.019  0.560   50.831  1.00 44.57  ? 207  VAL B C   1 
ATOM   4444  O O   . VAL B 1 198 ? 20.959  0.456   49.619  1.00 44.57  ? 207  VAL B O   1 
ATOM   4445  C CB  . VAL B 1 198 ? 22.908  0.317   52.333  1.00 44.55  ? 207  VAL B CB  1 
ATOM   4446  C CG1 . VAL B 1 198 ? 23.239  -0.913  51.507  1.00 44.76  ? 207  VAL B CG1 1 
ATOM   4447  C CG2 . VAL B 1 198 ? 24.182  0.957   52.842  1.00 44.67  ? 207  VAL B CG2 1 
ATOM   4448  N N   . ASN B 1 199 ? 20.115  0.046   51.640  1.00 46.09  ? 208  ASN B N   1 
ATOM   4449  C CA  . ASN B 1 199 ? 19.066  -0.740  51.047  1.00 47.62  ? 208  ASN B CA  1 
ATOM   4450  C C   . ASN B 1 199 ? 17.918  0.126   50.466  1.00 47.25  ? 208  ASN B C   1 
ATOM   4451  O O   . ASN B 1 199 ? 16.863  -0.358  50.043  1.00 48.16  ? 208  ASN B O   1 
ATOM   4452  C CB  . ASN B 1 199 ? 18.691  -2.006  51.880  1.00 49.49  ? 208  ASN B CB  1 
ATOM   4453  C CG  . ASN B 1 199 ? 18.017  -1.698  53.205  1.00 49.84  ? 208  ASN B CG  1 
ATOM   4454  O OD1 . ASN B 1 199 ? 17.839  -0.543  53.603  1.00 49.59  ? 208  ASN B OD1 1 
ATOM   4455  N ND2 . ASN B 1 199 ? 17.632  -2.751  53.895  1.00 50.95  ? 208  ASN B ND2 1 
ATOM   4456  N N   . LYS B 1 200 ? 18.163  1.418   50.369  1.00 46.12  ? 209  LYS B N   1 
ATOM   4457  C CA  . LYS B 1 200 ? 17.364  2.173   49.430  1.00 45.81  ? 209  LYS B CA  1 
ATOM   4458  C C   . LYS B 1 200 ? 17.947  1.978   48.022  1.00 44.74  ? 209  LYS B C   1 
ATOM   4459  O O   . LYS B 1 200 ? 17.240  1.673   47.057  1.00 44.53  ? 209  LYS B O   1 
ATOM   4460  C CB  . LYS B 1 200 ? 17.317  3.639   49.825  1.00 45.22  ? 209  LYS B CB  1 
ATOM   4461  C CG  . LYS B 1 200 ? 15.887  4.154   49.872  1.00 47.02  ? 209  LYS B CG  1 
ATOM   4462  C CD  . LYS B 1 200 ? 15.624  5.077   51.058  1.00 49.12  ? 209  LYS B CD  1 
ATOM   4463  C CE  . LYS B 1 200 ? 15.796  6.519   50.632  1.00 49.23  ? 209  LYS B CE  1 
ATOM   4464  N NZ  . LYS B 1 200 ? 16.510  7.309   51.673  1.00 50.52  ? 209  LYS B NZ  1 
ATOM   4465  N N   . GLN B 1 201 ? 19.258  2.140   47.937  1.00 43.98  ? 210  GLN B N   1 
ATOM   4466  C CA  . GLN B 1 201 ? 19.992  1.877   46.722  1.00 43.60  ? 210  GLN B CA  1 
ATOM   4467  C C   . GLN B 1 201 ? 19.669  0.493   46.247  1.00 44.91  ? 210  GLN B C   1 
ATOM   4468  O O   . GLN B 1 201 ? 19.385  0.294   45.067  1.00 44.87  ? 210  GLN B O   1 
ATOM   4469  C CB  . GLN B 1 201 ? 21.494  1.948   46.964  1.00 43.02  ? 210  GLN B CB  1 
ATOM   4470  C CG  . GLN B 1 201 ? 22.041  3.322   47.268  1.00 42.45  ? 210  GLN B CG  1 
ATOM   4471  C CD  . GLN B 1 201 ? 23.519  3.255   47.565  1.00 43.79  ? 210  GLN B CD  1 
ATOM   4472  O OE1 . GLN B 1 201 ? 24.044  2.186   47.891  1.00 45.06  ? 210  GLN B OE1 1 
ATOM   4473  N NE2 . GLN B 1 201 ? 24.210  4.389   47.444  1.00 43.00  ? 210  GLN B NE2 1 
ATOM   4474  N N   . SER B 1 202 ? 19.714  -0.468  47.166  1.00 46.53  ? 211  SER B N   1 
ATOM   4475  C CA  . SER B 1 202 ? 19.461  -1.859  46.798  1.00 48.48  ? 211  SER B CA  1 
ATOM   4476  C C   . SER B 1 202 ? 18.153  -1.957  46.043  1.00 49.07  ? 211  SER B C   1 
ATOM   4477  O O   . SER B 1 202 ? 18.027  -2.766  45.113  1.00 49.67  ? 211  SER B O   1 
ATOM   4478  C CB  . SER B 1 202 ? 19.445  -2.792  48.012  1.00 49.93  ? 211  SER B CB  1 
ATOM   4479  O OG  . SER B 1 202 ? 20.759  -3.186  48.385  1.00 50.69  ? 211  SER B OG  1 
ATOM   4480  N N   . CYS B 1 203 ? 17.195  -1.110  46.419  1.00 49.04  ? 212  CYS B N   1 
ATOM   4481  C CA  . CYS B 1 203 ? 15.943  -1.091  45.711  1.00 49.71  ? 212  CYS B CA  1 
ATOM   4482  C C   . CYS B 1 203 ? 16.042  -0.527  44.294  1.00 47.76  ? 212  CYS B C   1 
ATOM   4483  O O   . CYS B 1 203 ? 15.701  -1.199  43.307  1.00 47.58  ? 212  CYS B O   1 
ATOM   4484  C CB  . CYS B 1 203 ? 14.905  -0.315  46.470  1.00 50.40  ? 212  CYS B CB  1 
ATOM   4485  S SG  . CYS B 1 203 ? 13.458  -0.567  45.544  1.00 55.68  ? 212  CYS B SG  1 
ATOM   4486  N N   . SER B 1 204 ? 16.491  0.722   44.214  1.00 45.99  ? 213  SER B N   1 
ATOM   4487  C CA  . SER B 1 204 ? 16.622  1.413   42.942  1.00 44.52  ? 213  SER B CA  1 
ATOM   4488  C C   . SER B 1 204 ? 17.334  0.547   41.938  1.00 44.10  ? 213  SER B C   1 
ATOM   4489  O O   . SER B 1 204 ? 16.920  0.488   40.800  1.00 44.40  ? 213  SER B O   1 
ATOM   4490  C CB  . SER B 1 204 ? 17.350  2.733   43.113  1.00 43.38  ? 213  SER B CB  1 
ATOM   4491  O OG  . SER B 1 204 ? 16.596  3.606   43.924  1.00 44.47  ? 213  SER B OG  1 
ATOM   4492  N N   . ILE B 1 205 ? 18.386  -0.142  42.361  1.00 43.75  ? 214  ILE B N   1 
ATOM   4493  C CA  . ILE B 1 205 ? 19.087  -1.081  41.490  1.00 43.61  ? 214  ILE B CA  1 
ATOM   4494  C C   . ILE B 1 205 ? 18.181  -2.213  41.019  1.00 44.66  ? 214  ILE B C   1 
ATOM   4495  O O   . ILE B 1 205 ? 18.099  -2.479  39.825  1.00 44.67  ? 214  ILE B O   1 
ATOM   4496  C CB  . ILE B 1 205 ? 20.348  -1.628  42.167  1.00 44.20  ? 214  ILE B CB  1 
ATOM   4497  C CG1 . ILE B 1 205 ? 21.376  -0.501  42.310  1.00 42.87  ? 214  ILE B CG1 1 
ATOM   4498  C CG2 . ILE B 1 205 ? 20.944  -2.811  41.384  1.00 44.60  ? 214  ILE B CG2 1 
ATOM   4499  C CD1 . ILE B 1 205 ? 22.375  -0.731  43.389  1.00 44.57  ? 214  ILE B CD1 1 
ATOM   4500  N N   . SER B 1 206 ? 17.485  -2.863  41.944  1.00 45.51  ? 215  SER B N   1 
ATOM   4501  C CA  . SER B 1 206 ? 16.531  -3.894  41.565  1.00 46.56  ? 215  SER B CA  1 
ATOM   4502  C C   . SER B 1 206 ? 15.627  -3.369  40.457  1.00 45.62  ? 215  SER B C   1 
ATOM   4503  O O   . SER B 1 206 ? 15.369  -4.073  39.476  1.00 46.40  ? 215  SER B O   1 
ATOM   4504  C CB  . SER B 1 206 ? 15.691  -4.359  42.756  1.00 48.14  ? 215  SER B CB  1 
ATOM   4505  O OG  . SER B 1 206 ? 14.822  -5.434  42.402  1.00 50.09  ? 215  SER B OG  1 
ATOM   4506  N N   . ASN B 1 207 ? 15.166  -2.128  40.592  1.00 43.70  ? 216  ASN B N   1 
ATOM   4507  C CA  . ASN B 1 207 ? 14.347  -1.522  39.547  1.00 42.39  ? 216  ASN B CA  1 
ATOM   4508  C C   . ASN B 1 207 ? 15.060  -1.375  38.210  1.00 40.66  ? 216  ASN B C   1 
ATOM   4509  O O   . ASN B 1 207 ? 14.620  -1.887  37.195  1.00 41.11  ? 216  ASN B O   1 
ATOM   4510  C CB  . ASN B 1 207 ? 13.814  -0.186  40.027  1.00 41.69  ? 216  ASN B CB  1 
ATOM   4511  C CG  . ASN B 1 207 ? 12.962  -0.318  41.275  1.00 43.58  ? 216  ASN B CG  1 
ATOM   4512  O OD1 . ASN B 1 207 ? 12.684  -1.412  41.760  1.00 45.68  ? 216  ASN B OD1 1 
ATOM   4513  N ND2 . ASN B 1 207 ? 12.540  0.812   41.798  1.00 44.54  ? 216  ASN B ND2 1 
ATOM   4514  N N   . ILE B 1 208 ? 16.171  -0.675  38.222  1.00 38.67  ? 217  ILE B N   1 
ATOM   4515  C CA  . ILE B 1 208 ? 16.927  -0.502  37.024  1.00 37.66  ? 217  ILE B CA  1 
ATOM   4516  C C   . ILE B 1 208 ? 17.098  -1.837  36.376  1.00 39.05  ? 217  ILE B C   1 
ATOM   4517  O O   . ILE B 1 208 ? 16.692  -2.013  35.247  1.00 39.14  ? 217  ILE B O   1 
ATOM   4518  C CB  . ILE B 1 208 ? 18.267  0.130   37.302  1.00 36.63  ? 217  ILE B CB  1 
ATOM   4519  C CG1 . ILE B 1 208 ? 18.029  1.580   37.696  1.00 35.70  ? 217  ILE B CG1 1 
ATOM   4520  C CG2 . ILE B 1 208 ? 19.143  0.089   36.072  1.00 36.39  ? 217  ILE B CG2 1 
ATOM   4521  C CD1 . ILE B 1 208 ? 19.135  2.211   38.447  1.00 35.58  ? 217  ILE B CD1 1 
ATOM   4522  N N   . GLU B 1 209 ? 17.664  -2.795  37.092  1.00 40.67  ? 218  GLU B N   1 
ATOM   4523  C CA  . GLU B 1 209 ? 17.842  -4.136  36.544  1.00 43.01  ? 218  GLU B CA  1 
ATOM   4524  C C   . GLU B 1 209 ? 16.559  -4.667  35.921  1.00 43.42  ? 218  GLU B C   1 
ATOM   4525  O O   . GLU B 1 209 ? 16.533  -5.079  34.761  1.00 43.86  ? 218  GLU B O   1 
ATOM   4526  C CB  . GLU B 1 209 ? 18.312  -5.089  37.621  1.00 44.70  ? 218  GLU B CB  1 
ATOM   4527  C CG  . GLU B 1 209 ? 19.774  -4.911  37.888  1.00 48.62  ? 218  GLU B CG  1 
ATOM   4528  C CD  . GLU B 1 209 ? 20.247  -5.578  39.170  1.00 55.33  ? 218  GLU B CD  1 
ATOM   4529  O OE1 . GLU B 1 209 ? 19.366  -5.898  40.011  1.00 57.61  ? 218  GLU B OE1 1 
ATOM   4530  O OE2 . GLU B 1 209 ? 21.499  -5.756  39.331  1.00 57.35  ? 218  GLU B OE2 1 
ATOM   4531  N N   . THR B 1 210 ? 15.486  -4.644  36.690  1.00 43.33  ? 219  THR B N   1 
ATOM   4532  C CA  . THR B 1 210 ? 14.208  -5.031  36.154  1.00 43.60  ? 219  THR B CA  1 
ATOM   4533  C C   . THR B 1 210 ? 13.938  -4.334  34.808  1.00 42.02  ? 219  THR B C   1 
ATOM   4534  O O   . THR B 1 210 ? 13.750  -5.014  33.796  1.00 43.12  ? 219  THR B O   1 
ATOM   4535  C CB  . THR B 1 210 ? 13.079  -4.727  37.143  1.00 44.06  ? 219  THR B CB  1 
ATOM   4536  O OG1 . THR B 1 210 ? 13.367  -5.362  38.393  1.00 45.27  ? 219  THR B OG1 1 
ATOM   4537  C CG2 . THR B 1 210 ? 11.776  -5.249  36.601  1.00 44.96  ? 219  THR B CG2 1 
ATOM   4538  N N   . VAL B 1 211 ? 13.940  -2.999  34.786  1.00 39.23  ? 220  VAL B N   1 
ATOM   4539  C CA  . VAL B 1 211 ? 13.680  -2.284  33.550  1.00 37.06  ? 220  VAL B CA  1 
ATOM   4540  C C   . VAL B 1 211 ? 14.537  -2.829  32.408  1.00 36.91  ? 220  VAL B C   1 
ATOM   4541  O O   . VAL B 1 211 ? 14.003  -3.307  31.418  1.00 37.30  ? 220  VAL B O   1 
ATOM   4542  C CB  . VAL B 1 211 ? 13.901  -0.797  33.702  1.00 35.18  ? 220  VAL B CB  1 
ATOM   4543  C CG1 . VAL B 1 211 ? 14.083  -0.198  32.363  1.00 33.67  ? 220  VAL B CG1 1 
ATOM   4544  C CG2 . VAL B 1 211 ? 12.727  -0.147  34.385  1.00 34.92  ? 220  VAL B CG2 1 
ATOM   4545  N N   . ILE B 1 212 ? 15.858  -2.781  32.561  1.00 36.32  ? 221  ILE B N   1 
ATOM   4546  C CA  . ILE B 1 212 ? 16.767  -3.228  31.518  1.00 36.36  ? 221  ILE B CA  1 
ATOM   4547  C C   . ILE B 1 212 ? 16.358  -4.581  31.035  1.00 38.74  ? 221  ILE B C   1 
ATOM   4548  O O   . ILE B 1 212 ? 16.222  -4.812  29.859  1.00 38.83  ? 221  ILE B O   1 
ATOM   4549  C CB  . ILE B 1 212 ? 18.191  -3.360  32.012  1.00 35.93  ? 221  ILE B CB  1 
ATOM   4550  C CG1 . ILE B 1 212 ? 18.727  -2.034  32.550  1.00 33.60  ? 221  ILE B CG1 1 
ATOM   4551  C CG2 . ILE B 1 212 ? 19.073  -3.901  30.903  1.00 35.80  ? 221  ILE B CG2 1 
ATOM   4552  C CD1 . ILE B 1 212 ? 18.751  -0.927  31.570  1.00 32.01  ? 221  ILE B CD1 1 
ATOM   4553  N N   . GLU B 1 213 ? 16.133  -5.474  31.972  1.00 41.36  ? 222  GLU B N   1 
ATOM   4554  C CA  . GLU B 1 213 ? 15.876  -6.856  31.639  1.00 44.94  ? 222  GLU B CA  1 
ATOM   4555  C C   . GLU B 1 213 ? 14.539  -7.005  30.953  1.00 45.54  ? 222  GLU B C   1 
ATOM   4556  O O   . GLU B 1 213 ? 14.268  -8.020  30.307  1.00 47.20  ? 222  GLU B O   1 
ATOM   4557  C CB  . GLU B 1 213 ? 15.917  -7.712  32.896  1.00 46.62  ? 222  GLU B CB  1 
ATOM   4558  C CG  . GLU B 1 213 ? 16.452  -9.112  32.646  1.00 52.09  ? 222  GLU B CG  1 
ATOM   4559  C CD  . GLU B 1 213 ? 16.616  -9.894  33.941  1.00 58.91  ? 222  GLU B CD  1 
ATOM   4560  O OE1 . GLU B 1 213 ? 16.350  -9.270  35.003  1.00 61.17  ? 222  GLU B OE1 1 
ATOM   4561  O OE2 . GLU B 1 213 ? 17.001  -11.109 33.908  1.00 62.80  ? 222  GLU B OE2 1 
ATOM   4562  N N   . PHE B 1 214 ? 13.708  -5.983  31.092  1.00 44.71  ? 223  PHE B N   1 
ATOM   4563  C CA  . PHE B 1 214 ? 12.400  -5.988  30.461  1.00 45.34  ? 223  PHE B CA  1 
ATOM   4564  C C   . PHE B 1 214 ? 12.568  -5.736  28.977  1.00 44.98  ? 223  PHE B C   1 
ATOM   4565  O O   . PHE B 1 214 ? 11.969  -6.425  28.140  1.00 46.10  ? 223  PHE B O   1 
ATOM   4566  C CB  . PHE B 1 214 ? 11.522  -4.914  31.101  1.00 44.21  ? 223  PHE B CB  1 
ATOM   4567  C CG  . PHE B 1 214 ? 10.238  -4.656  30.372  1.00 43.75  ? 223  PHE B CG  1 
ATOM   4568  C CD1 . PHE B 1 214 ? 9.091   -5.381  30.660  1.00 45.27  ? 223  PHE B CD1 1 
ATOM   4569  C CD2 . PHE B 1 214 ? 10.166  -3.666  29.422  1.00 42.17  ? 223  PHE B CD2 1 
ATOM   4570  C CE1 . PHE B 1 214 ? 7.883   -5.129  30.007  1.00 44.80  ? 223  PHE B CE1 1 
ATOM   4571  C CE2 . PHE B 1 214 ? 8.969   -3.416  28.761  1.00 42.44  ? 223  PHE B CE2 1 
ATOM   4572  C CZ  . PHE B 1 214 ? 7.821   -4.155  29.062  1.00 43.32  ? 223  PHE B CZ  1 
ATOM   4573  N N   . GLN B 1 215 ? 13.400  -4.744  28.679  1.00 43.64  ? 224  GLN B N   1 
ATOM   4574  C CA  . GLN B 1 215 ? 13.702  -4.350  27.311  1.00 43.45  ? 224  GLN B CA  1 
ATOM   4575  C C   . GLN B 1 215 ? 14.475  -5.436  26.624  1.00 44.33  ? 224  GLN B C   1 
ATOM   4576  O O   . GLN B 1 215 ? 14.323  -5.643  25.431  1.00 44.52  ? 224  GLN B O   1 
ATOM   4577  C CB  . GLN B 1 215 ? 14.521  -3.070  27.299  1.00 41.94  ? 224  GLN B CB  1 
ATOM   4578  C CG  . GLN B 1 215 ? 13.968  -2.057  28.256  1.00 43.46  ? 224  GLN B CG  1 
ATOM   4579  C CD  . GLN B 1 215 ? 14.680  -0.757  28.170  1.00 44.97  ? 224  GLN B CD  1 
ATOM   4580  O OE1 . GLN B 1 215 ? 15.904  -0.709  28.031  1.00 45.65  ? 224  GLN B OE1 1 
ATOM   4581  N NE2 . GLN B 1 215 ? 13.919  0.327   28.245  1.00 44.80  ? 224  GLN B NE2 1 
ATOM   4582  N N   . GLN B 1 216 ? 15.308  -6.124  27.397  1.00 45.19  ? 225  GLN B N   1 
ATOM   4583  C CA  . GLN B 1 216 ? 16.152  -7.199  26.888  1.00 46.47  ? 225  GLN B CA  1 
ATOM   4584  C C   . GLN B 1 216 ? 15.299  -8.367  26.436  1.00 48.10  ? 225  GLN B C   1 
ATOM   4585  O O   . GLN B 1 216 ? 15.357  -8.802  25.289  1.00 48.19  ? 225  GLN B O   1 
ATOM   4586  C CB  . GLN B 1 216 ? 17.109  -7.673  27.978  1.00 47.13  ? 225  GLN B CB  1 
ATOM   4587  C CG  . GLN B 1 216 ? 18.056  -6.617  28.467  1.00 46.94  ? 225  GLN B CG  1 
ATOM   4588  C CD  . GLN B 1 216 ? 19.388  -7.197  28.830  1.00 49.78  ? 225  GLN B CD  1 
ATOM   4589  O OE1 . GLN B 1 216 ? 19.485  -8.051  29.715  1.00 52.06  ? 225  GLN B OE1 1 
ATOM   4590  N NE2 . GLN B 1 216 ? 20.432  -6.746  28.150  1.00 49.42  ? 225  GLN B NE2 1 
ATOM   4591  N N   . LYS B 1 217 ? 14.488  -8.858  27.355  1.00 49.35  ? 226  LYS B N   1 
ATOM   4592  C CA  . LYS B 1 217 ? 13.744  -10.067 27.122  1.00 51.87  ? 226  LYS B CA  1 
ATOM   4593  C C   . LYS B 1 217 ? 12.531  -9.822  26.242  1.00 51.42  ? 226  LYS B C   1 
ATOM   4594  O O   . LYS B 1 217 ? 12.065  -10.733 25.546  1.00 53.07  ? 226  LYS B O   1 
ATOM   4595  C CB  . LYS B 1 217 ? 13.294  -10.653 28.449  1.00 53.65  ? 226  LYS B CB  1 
ATOM   4596  C CG  . LYS B 1 217 ? 14.390  -11.277 29.287  1.00 56.38  ? 226  LYS B CG  1 
ATOM   4597  C CD  . LYS B 1 217 ? 13.753  -12.161 30.346  1.00 61.50  ? 226  LYS B CD  1 
ATOM   4598  C CE  . LYS B 1 217 ? 14.775  -12.716 31.328  1.00 64.93  ? 226  LYS B CE  1 
ATOM   4599  N NZ  . LYS B 1 217 ? 14.111  -13.139 32.616  1.00 67.71  ? 226  LYS B NZ  1 
ATOM   4600  N N   . ASN B 1 218 ? 12.006  -8.600  26.285  1.00 49.15  ? 227  ASN B N   1 
ATOM   4601  C CA  . ASN B 1 218 ? 10.882  -8.259  25.431  1.00 48.51  ? 227  ASN B CA  1 
ATOM   4602  C C   . ASN B 1 218 ? 11.253  -7.644  24.110  1.00 47.50  ? 227  ASN B C   1 
ATOM   4603  O O   . ASN B 1 218 ? 10.397  -7.129  23.395  1.00 47.19  ? 227  ASN B O   1 
ATOM   4604  C CB  . ASN B 1 218 ? 9.932   -7.377  26.172  1.00 47.09  ? 227  ASN B CB  1 
ATOM   4605  C CG  . ASN B 1 218 ? 8.935   -8.160  26.867  1.00 48.46  ? 227  ASN B CG  1 
ATOM   4606  O OD1 . ASN B 1 218 ? 8.304   -9.041  26.286  1.00 50.26  ? 227  ASN B OD1 1 
ATOM   4607  N ND2 . ASN B 1 218 ? 8.785   -7.893  28.132  1.00 48.06  ? 227  ASN B ND2 1 
ATOM   4608  N N   . ASN B 1 219 ? 12.542  -7.730  23.795  1.00 47.23  ? 228  ASN B N   1 
ATOM   4609  C CA  . ASN B 1 219 ? 13.149  -7.036  22.663  1.00 45.69  ? 228  ASN B CA  1 
ATOM   4610  C C   . ASN B 1 219 ? 12.340  -7.182  21.384  1.00 45.30  ? 228  ASN B C   1 
ATOM   4611  O O   . ASN B 1 219 ? 11.938  -6.187  20.772  1.00 43.86  ? 228  ASN B O   1 
ATOM   4612  C CB  . ASN B 1 219 ? 14.596  -7.532  22.453  1.00 46.53  ? 228  ASN B CB  1 
ATOM   4613  C CG  . ASN B 1 219 ? 15.245  -6.963  21.187  1.00 47.01  ? 228  ASN B CG  1 
ATOM   4614  O OD1 . ASN B 1 219 ? 15.357  -7.668  20.190  1.00 49.83  ? 228  ASN B OD1 1 
ATOM   4615  N ND2 . ASN B 1 219 ? 15.664  -5.686  21.223  1.00 46.68  ? 228  ASN B ND2 1 
ATOM   4616  N N   . ARG B 1 220 ? 12.084  -8.431  21.013  1.00 46.22  ? 229  ARG B N   1 
ATOM   4617  C CA  . ARG B 1 220 ? 11.523  -8.724  19.735  1.00 45.70  ? 229  ARG B CA  1 
ATOM   4618  C C   . ARG B 1 220 ? 10.177  -8.083  19.662  1.00 44.72  ? 229  ARG B C   1 
ATOM   4619  O O   . ARG B 1 220 ? 9.846   -7.440  18.682  1.00 43.75  ? 229  ARG B O   1 
ATOM   4620  C CB  . ARG B 1 220 ? 11.413  -10.212 19.574  1.00 48.23  ? 229  ARG B CB  1 
ATOM   4621  C CG  . ARG B 1 220 ? 11.619  -10.646 18.168  1.00 48.06  ? 229  ARG B CG  1 
ATOM   4622  C CD  . ARG B 1 220 ? 11.357  -12.126 18.029  1.00 50.06  ? 229  ARG B CD  1 
ATOM   4623  N NE  . ARG B 1 220 ? 10.566  -12.353 16.827  1.00 51.35  ? 229  ARG B NE  1 
ATOM   4624  C CZ  . ARG B 1 220 ? 9.960   -13.485 16.525  1.00 53.93  ? 229  ARG B CZ  1 
ATOM   4625  N NH1 . ARG B 1 220 ? 10.064  -14.504 17.345  1.00 55.67  ? 229  ARG B NH1 1 
ATOM   4626  N NH2 . ARG B 1 220 ? 9.258   -13.594 15.405  1.00 55.38  ? 229  ARG B NH2 1 
ATOM   4627  N N   . LEU B 1 221 ? 9.407   -8.222  20.730  1.00 44.91  ? 230  LEU B N   1 
ATOM   4628  C CA  . LEU B 1 221 ? 8.104   -7.574  20.779  1.00 44.17  ? 230  LEU B CA  1 
ATOM   4629  C C   . LEU B 1 221 ? 8.190   -6.066  20.615  1.00 41.76  ? 230  LEU B C   1 
ATOM   4630  O O   . LEU B 1 221 ? 7.449   -5.482  19.851  1.00 41.28  ? 230  LEU B O   1 
ATOM   4631  C CB  . LEU B 1 221 ? 7.389   -7.878  22.080  1.00 45.11  ? 230  LEU B CB  1 
ATOM   4632  C CG  . LEU B 1 221 ? 6.010   -7.212  22.168  1.00 44.50  ? 230  LEU B CG  1 
ATOM   4633  C CD1 . LEU B 1 221 ? 4.948   -8.085  21.527  1.00 46.75  ? 230  LEU B CD1 1 
ATOM   4634  C CD2 . LEU B 1 221 ? 5.638   -6.977  23.600  1.00 45.39  ? 230  LEU B CD2 1 
ATOM   4635  N N   . LEU B 1 222 ? 9.090   -5.436  21.346  1.00 40.44  ? 231  LEU B N   1 
ATOM   4636  C CA  . LEU B 1 222 ? 9.239   -4.010  21.237  1.00 38.43  ? 231  LEU B CA  1 
ATOM   4637  C C   . LEU B 1 222 ? 9.611   -3.605  19.833  1.00 37.65  ? 231  LEU B C   1 
ATOM   4638  O O   . LEU B 1 222 ? 9.007   -2.697  19.293  1.00 37.13  ? 231  LEU B O   1 
ATOM   4639  C CB  . LEU B 1 222 ? 10.264  -3.524  22.221  1.00 37.64  ? 231  LEU B CB  1 
ATOM   4640  C CG  . LEU B 1 222 ? 9.804   -3.873  23.624  1.00 38.75  ? 231  LEU B CG  1 
ATOM   4641  C CD1 . LEU B 1 222 ? 10.977  -4.045  24.538  1.00 40.74  ? 231  LEU B CD1 1 
ATOM   4642  C CD2 . LEU B 1 222 ? 8.912   -2.784  24.132  1.00 38.78  ? 231  LEU B CD2 1 
ATOM   4643  N N   . GLU B 1 223 ? 10.577  -4.280  19.224  1.00 37.89  ? 232  GLU B N   1 
ATOM   4644  C CA  . GLU B 1 223 ? 10.956  -3.920  17.875  1.00 37.19  ? 232  GLU B CA  1 
ATOM   4645  C C   . GLU B 1 223 ? 9.729   -3.939  17.009  1.00 36.95  ? 232  GLU B C   1 
ATOM   4646  O O   . GLU B 1 223 ? 9.488   -3.006  16.281  1.00 36.21  ? 232  GLU B O   1 
ATOM   4647  C CB  . GLU B 1 223 ? 12.028  -4.841  17.308  1.00 38.37  ? 232  GLU B CB  1 
ATOM   4648  C CG  . GLU B 1 223 ? 13.403  -4.623  17.885  1.00 40.02  ? 232  GLU B CG  1 
ATOM   4649  C CD  . GLU B 1 223 ? 13.974  -3.273  17.564  1.00 41.46  ? 232  GLU B CD  1 
ATOM   4650  O OE1 . GLU B 1 223 ? 13.460  -2.585  16.647  1.00 40.81  ? 232  GLU B OE1 1 
ATOM   4651  O OE2 . GLU B 1 223 ? 14.961  -2.914  18.237  1.00 42.00  ? 232  GLU B OE2 1 
ATOM   4652  N N   . ILE B 1 224 ? 8.925   -4.980  17.126  1.00 37.94  ? 233  ILE B N   1 
ATOM   4653  C CA  . ILE B 1 224 ? 7.748   -5.104  16.287  1.00 38.27  ? 233  ILE B CA  1 
ATOM   4654  C C   . ILE B 1 224 ? 6.809   -3.953  16.516  1.00 37.00  ? 233  ILE B C   1 
ATOM   4655  O O   . ILE B 1 224 ? 6.321   -3.343  15.597  1.00 36.25  ? 233  ILE B O   1 
ATOM   4656  C CB  . ILE B 1 224 ? 6.979   -6.389  16.582  1.00 40.36  ? 233  ILE B CB  1 
ATOM   4657  C CG1 . ILE B 1 224 ? 7.918   -7.587  16.532  1.00 41.18  ? 233  ILE B CG1 1 
ATOM   4658  C CG2 . ILE B 1 224 ? 5.817   -6.537  15.619  1.00 40.99  ? 233  ILE B CG2 1 
ATOM   4659  C CD1 . ILE B 1 224 ? 7.238   -8.860  16.216  1.00 43.75  ? 233  ILE B CD1 1 
ATOM   4660  N N   . THR B 1 225 ? 6.562   -3.674  17.776  1.00 37.02  ? 234  THR B N   1 
ATOM   4661  C CA  . THR B 1 225 ? 5.621   -2.657  18.190  1.00 36.48  ? 234  THR B CA  1 
ATOM   4662  C C   . THR B 1 225 ? 5.965   -1.349  17.517  1.00 35.09  ? 234  THR B C   1 
ATOM   4663  O O   . THR B 1 225 ? 5.084   -0.640  17.050  1.00 35.04  ? 234  THR B O   1 
ATOM   4664  C CB  . THR B 1 225 ? 5.658   -2.503  19.715  1.00 36.34  ? 234  THR B CB  1 
ATOM   4665  O OG1 . THR B 1 225 ? 5.036   -3.636  20.328  1.00 37.85  ? 234  THR B OG1 1 
ATOM   4666  C CG2 . THR B 1 225 ? 4.953   -1.263  20.160  1.00 35.42  ? 234  THR B CG2 1 
ATOM   4667  N N   . ARG B 1 226 ? 7.252   -1.044  17.456  1.00 34.54  ? 235  ARG B N   1 
ATOM   4668  C CA  . ARG B 1 226 ? 7.722   0.175   16.829  1.00 33.45  ? 235  ARG B CA  1 
ATOM   4669  C C   . ARG B 1 226 ? 7.401   0.131   15.347  1.00 33.47  ? 235  ARG B C   1 
ATOM   4670  O O   . ARG B 1 226 ? 6.600   0.912   14.854  1.00 33.00  ? 235  ARG B O   1 
ATOM   4671  C CB  . ARG B 1 226 ? 9.216   0.298   17.039  1.00 32.99  ? 235  ARG B CB  1 
ATOM   4672  C CG  . ARG B 1 226 ? 9.868   1.322   16.165  1.00 33.37  ? 235  ARG B CG  1 
ATOM   4673  C CD  . ARG B 1 226 ? 11.335  0.997   15.981  1.00 35.34  ? 235  ARG B CD  1 
ATOM   4674  N NE  . ARG B 1 226 ? 11.925  0.569   17.252  1.00 35.70  ? 235  ARG B NE  1 
ATOM   4675  C CZ  . ARG B 1 226 ? 12.217  1.363   18.283  1.00 32.79  ? 235  ARG B CZ  1 
ATOM   4676  N NH1 . ARG B 1 226 ? 11.990  2.682   18.242  1.00 30.02  ? 235  ARG B NH1 1 
ATOM   4677  N NH2 . ARG B 1 226 ? 12.749  0.808   19.362  1.00 32.12  ? 235  ARG B NH2 1 
ATOM   4678  N N   . GLU B 1 227 ? 8.040   -0.805  14.653  1.00 34.31  ? 236  GLU B N   1 
ATOM   4679  C CA  . GLU B 1 227 ? 7.765   -1.112  13.250  1.00 34.89  ? 236  GLU B CA  1 
ATOM   4680  C C   . GLU B 1 227 ? 6.292   -0.833  12.924  1.00 34.47  ? 236  GLU B C   1 
ATOM   4681  O O   . GLU B 1 227 ? 5.998   -0.171  11.953  1.00 34.10  ? 236  GLU B O   1 
ATOM   4682  C CB  . GLU B 1 227 ? 8.120   -2.595  12.959  1.00 36.88  ? 236  GLU B CB  1 
ATOM   4683  C CG  . GLU B 1 227 ? 8.754   -2.919  11.579  1.00 39.60  ? 236  GLU B CG  1 
ATOM   4684  C CD  . GLU B 1 227 ? 9.285   -4.380  11.475  1.00 44.10  ? 236  GLU B CD  1 
ATOM   4685  O OE1 . GLU B 1 227 ? 9.069   -5.043  10.414  1.00 47.81  ? 236  GLU B OE1 1 
ATOM   4686  O OE2 . GLU B 1 227 ? 9.924   -4.861  12.449  1.00 42.67  ? 236  GLU B OE2 1 
ATOM   4687  N N   . PHE B 1 228 ? 5.370   -1.302  13.746  1.00 34.71  ? 237  PHE B N   1 
ATOM   4688  C CA  . PHE B 1 228 ? 3.974   -1.148  13.420  1.00 34.91  ? 237  PHE B CA  1 
ATOM   4689  C C   . PHE B 1 228 ? 3.483   0.247   13.636  1.00 33.25  ? 237  PHE B C   1 
ATOM   4690  O O   . PHE B 1 228 ? 2.671   0.721   12.877  1.00 33.13  ? 237  PHE B O   1 
ATOM   4691  C CB  . PHE B 1 228 ? 3.105   -2.109  14.227  1.00 36.99  ? 237  PHE B CB  1 
ATOM   4692  C CG  . PHE B 1 228 ? 2.926   -3.484  13.586  1.00 39.74  ? 237  PHE B CG  1 
ATOM   4693  C CD1 . PHE B 1 228 ? 3.183   -4.640  14.312  1.00 41.88  ? 237  PHE B CD1 1 
ATOM   4694  C CD2 . PHE B 1 228 ? 2.501   -3.614  12.264  1.00 40.98  ? 237  PHE B CD2 1 
ATOM   4695  C CE1 . PHE B 1 228 ? 3.015   -5.880  13.727  1.00 44.35  ? 237  PHE B CE1 1 
ATOM   4696  C CE2 . PHE B 1 228 ? 2.343   -4.854  11.678  1.00 42.74  ? 237  PHE B CE2 1 
ATOM   4697  C CZ  . PHE B 1 228 ? 2.600   -5.983  12.403  1.00 44.55  ? 237  PHE B CZ  1 
ATOM   4698  N N   . SER B 1 229 ? 3.956   0.902   14.680  1.00 32.20  ? 238  SER B N   1 
ATOM   4699  C CA  . SER B 1 229 ? 3.597   2.300   14.936  1.00 31.10  ? 238  SER B CA  1 
ATOM   4700  C C   . SER B 1 229 ? 4.052   3.269   13.833  1.00 29.97  ? 238  SER B C   1 
ATOM   4701  O O   . SER B 1 229 ? 3.450   4.317   13.581  1.00 29.46  ? 238  SER B O   1 
ATOM   4702  C CB  . SER B 1 229 ? 4.197   2.729   16.252  1.00 30.42  ? 238  SER B CB  1 
ATOM   4703  O OG  . SER B 1 229 ? 3.607   1.990   17.287  1.00 32.21  ? 238  SER B OG  1 
ATOM   4704  N N   . VAL B 1 230 ? 5.135   2.902   13.173  1.00 29.60  ? 239  VAL B N   1 
ATOM   4705  C CA  . VAL B 1 230 ? 5.730   3.748   12.185  1.00 28.31  ? 239  VAL B CA  1 
ATOM   4706  C C   . VAL B 1 230 ? 5.078   3.462   10.855  1.00 29.02  ? 239  VAL B C   1 
ATOM   4707  O O   . VAL B 1 230 ? 5.163   4.237   9.932   1.00 29.02  ? 239  VAL B O   1 
ATOM   4708  C CB  . VAL B 1 230 ? 7.214   3.452   12.102  1.00 27.52  ? 239  VAL B CB  1 
ATOM   4709  C CG1 . VAL B 1 230 ? 7.948   4.587   11.397  1.00 26.99  ? 239  VAL B CG1 1 
ATOM   4710  C CG2 . VAL B 1 230 ? 7.747   3.296   13.487  1.00 27.74  ? 239  VAL B CG2 1 
ATOM   4711  N N   . ASN B 1 231 ? 4.425   2.331   10.731  1.00 30.47  ? 240  ASN B N   1 
ATOM   4712  C CA  . ASN B 1 231 ? 3.932   1.931   9.427   1.00 31.17  ? 240  ASN B CA  1 
ATOM   4713  C C   . ASN B 1 231 ? 2.423   1.788   9.425   1.00 31.84  ? 240  ASN B C   1 
ATOM   4714  O O   . ASN B 1 231 ? 1.843   1.186   8.518   1.00 32.52  ? 240  ASN B O   1 
ATOM   4715  C CB  . ASN B 1 231 ? 4.594   0.617   9.009   1.00 32.49  ? 240  ASN B CB  1 
ATOM   4716  C CG  . ASN B 1 231 ? 6.037   0.795   8.547   1.00 32.95  ? 240  ASN B CG  1 
ATOM   4717  O OD1 . ASN B 1 231 ? 6.289   1.213   7.407   1.00 34.14  ? 240  ASN B OD1 1 
ATOM   4718  N ND2 . ASN B 1 231 ? 6.997   0.441   9.417   1.00 35.03  ? 240  ASN B ND2 1 
ATOM   4719  N N   . ALA B 1 232 ? 1.795   2.343   10.455  1.00 31.58  ? 241  ALA B N   1 
ATOM   4720  C CA  . ALA B 1 232 ? 0.374   2.244   10.593  1.00 32.69  ? 241  ALA B CA  1 
ATOM   4721  C C   . ALA B 1 232 ? -0.050  0.794   10.399  1.00 34.56  ? 241  ALA B C   1 
ATOM   4722  O O   . ALA B 1 232 ? -0.987  0.511   9.670   1.00 35.74  ? 241  ALA B O   1 
ATOM   4723  C CB  . ALA B 1 232 ? -0.290  3.121   9.582   1.00 32.35  ? 241  ALA B CB  1 
ATOM   4724  N N   . GLY B 1 233 ? 0.661   -0.128  11.032  1.00 35.12  ? 242  GLY B N   1 
ATOM   4725  C CA  . GLY B 1 233 ? 0.214   -1.517  11.094  1.00 37.02  ? 242  GLY B CA  1 
ATOM   4726  C C   . GLY B 1 233 ? 0.357   -2.393  9.853   1.00 37.93  ? 242  GLY B C   1 
ATOM   4727  O O   . GLY B 1 233 ? -0.369  -3.389  9.704   1.00 40.03  ? 242  GLY B O   1 
ATOM   4728  N N   . VAL B 1 234 ? 1.286   -2.048  8.963   1.00 36.63  ? 243  VAL B N   1 
ATOM   4729  C CA  . VAL B 1 234 ? 1.597   -2.922  7.843   1.00 37.41  ? 243  VAL B CA  1 
ATOM   4730  C C   . VAL B 1 234 ? 3.003   -2.675  7.369   1.00 36.52  ? 243  VAL B C   1 
ATOM   4731  O O   . VAL B 1 234 ? 3.354   -1.537  7.196   1.00 35.37  ? 243  VAL B O   1 
ATOM   4732  C CB  . VAL B 1 234 ? 0.707   -2.613  6.677   1.00 37.28  ? 243  VAL B CB  1 
ATOM   4733  C CG1 . VAL B 1 234 ? 0.387   -3.864  5.987   1.00 39.20  ? 243  VAL B CG1 1 
ATOM   4734  C CG2 . VAL B 1 234 ? -0.543  -1.976  7.141   1.00 37.36  ? 243  VAL B CG2 1 
ATOM   4735  N N   . THR B 1 235 ? 3.803   -3.706  7.131   1.00 37.57  ? 244  THR B N   1 
ATOM   4736  C CA  . THR B 1 235 ? 5.148   -3.443  6.675   1.00 37.52  ? 244  THR B CA  1 
ATOM   4737  C C   . THR B 1 235 ? 5.464   -4.262  5.481   1.00 38.72  ? 244  THR B C   1 
ATOM   4738  O O   . THR B 1 235 ? 4.915   -5.354  5.360   1.00 40.65  ? 244  THR B O   1 
ATOM   4739  C CB  . THR B 1 235 ? 6.168   -3.898  7.673   1.00 38.04  ? 244  THR B CB  1 
ATOM   4740  O OG1 . THR B 1 235 ? 5.505   -4.469  8.799   1.00 39.38  ? 244  THR B OG1 1 
ATOM   4741  C CG2 . THR B 1 235 ? 7.139   -2.736  8.060   1.00 37.50  ? 244  THR B CG2 1 
ATOM   4742  N N   . THR B 1 236 ? 6.346   -3.748  4.612   1.00 37.83  ? 245  THR B N   1 
ATOM   4743  C CA  . THR B 1 236 ? 7.078   -4.597  3.676   1.00 39.25  ? 245  THR B CA  1 
ATOM   4744  C C   . THR B 1 236 ? 8.557   -4.457  3.942   1.00 38.54  ? 245  THR B C   1 
ATOM   4745  O O   . THR B 1 236 ? 8.988   -3.435  4.475   1.00 37.10  ? 245  THR B O   1 
ATOM   4746  C CB  . THR B 1 236 ? 6.659   -4.401  2.215   1.00 39.69  ? 245  THR B CB  1 
ATOM   4747  O OG1 . THR B 1 236 ? 5.370   -4.974  2.050   1.00 42.78  ? 245  THR B OG1 1 
ATOM   4748  C CG2 . THR B 1 236 ? 7.551   -5.161  1.239   1.00 41.33  ? 245  THR B CG2 1 
ATOM   4749  N N   . PRO B 1 237 ? 9.342   -5.398  3.402   1.00 39.85  ? 246  PRO B N   1 
ATOM   4750  C CA  . PRO B 1 237 ? 10.132  -6.412  4.032   1.00 40.55  ? 246  PRO B CA  1 
ATOM   4751  C C   . PRO B 1 237 ? 9.475   -6.854  5.324   1.00 40.52  ? 246  PRO B C   1 
ATOM   4752  O O   . PRO B 1 237 ? 8.965   -6.059  6.112   1.00 39.40  ? 246  PRO B O   1 
ATOM   4753  C CB  . PRO B 1 237 ? 11.466  -5.718  4.272   1.00 39.48  ? 246  PRO B CB  1 
ATOM   4754  C CG  . PRO B 1 237 ? 11.521  -4.632  3.201   1.00 39.18  ? 246  PRO B CG  1 
ATOM   4755  C CD  . PRO B 1 237 ? 10.207  -4.676  2.460   1.00 39.57  ? 246  PRO B CD  1 
ATOM   4756  N N   . VAL B 1 238 ? 9.469   -8.148  5.517   1.00 41.85  ? 247  VAL B N   1 
ATOM   4757  C CA  . VAL B 1 238 ? 9.062   -8.704  6.770   1.00 41.95  ? 247  VAL B CA  1 
ATOM   4758  C C   . VAL B 1 238 ? 10.350  -8.809  7.556   1.00 41.69  ? 247  VAL B C   1 
ATOM   4759  O O   . VAL B 1 238 ? 11.218  -9.655  7.263   1.00 42.87  ? 247  VAL B O   1 
ATOM   4760  C CB  . VAL B 1 238 ? 8.418   -10.065 6.520   1.00 44.26  ? 247  VAL B CB  1 
ATOM   4761  C CG1 . VAL B 1 238 ? 8.167   -10.822 7.808   1.00 45.79  ? 247  VAL B CG1 1 
ATOM   4762  C CG2 . VAL B 1 238 ? 7.126   -9.872  5.757   1.00 44.06  ? 247  VAL B CG2 1 
ATOM   4763  N N   . SER B 1 239 ? 10.488  -7.934  8.540   1.00 40.08  ? 248  SER B N   1 
ATOM   4764  C CA  . SER B 1 239 ? 11.753  -7.835  9.224   1.00 39.93  ? 248  SER B CA  1 
ATOM   4765  C C   . SER B 1 239 ? 12.203  -9.162  9.803   1.00 42.10  ? 248  SER B C   1 
ATOM   4766  O O   . SER B 1 239 ? 11.458  -10.136 9.868   1.00 43.72  ? 248  SER B O   1 
ATOM   4767  C CB  . SER B 1 239 ? 11.654  -6.831  10.342  1.00 38.30  ? 248  SER B CB  1 
ATOM   4768  O OG  . SER B 1 239 ? 10.936  -7.387  11.403  1.00 38.95  ? 248  SER B OG  1 
ATOM   4769  N N   . THR B 1 240 ? 13.444  -9.201  10.238  1.00 42.34  ? 249  THR B N   1 
ATOM   4770  C CA  . THR B 1 240 ? 13.897  -10.363 10.959  1.00 44.44  ? 249  THR B CA  1 
ATOM   4771  C C   . THR B 1 240 ? 13.309  -10.309 12.353  1.00 44.14  ? 249  THR B C   1 
ATOM   4772  O O   . THR B 1 240 ? 13.438  -11.260 13.109  1.00 46.00  ? 249  THR B O   1 
ATOM   4773  C CB  . THR B 1 240 ? 15.418  -10.427 11.079  1.00 44.51  ? 249  THR B CB  1 
ATOM   4774  O OG1 . THR B 1 240 ? 15.840  -9.580  12.146  1.00 43.79  ? 249  THR B OG1 1 
ATOM   4775  C CG2 . THR B 1 240 ? 16.075  -9.966  9.802   1.00 44.33  ? 249  THR B CG2 1 
ATOM   4776  N N   . TYR B 1 241 ? 12.678  -9.202  12.714  1.00 42.06  ? 250  TYR B N   1 
ATOM   4777  C CA  . TYR B 1 241 ? 11.987  -9.219  13.968  1.00 42.13  ? 250  TYR B CA  1 
ATOM   4778  C C   . TYR B 1 241 ? 10.589  -9.801  13.822  1.00 43.30  ? 250  TYR B C   1 
ATOM   4779  O O   . TYR B 1 241 ? 10.092  -10.415 14.737  1.00 44.44  ? 250  TYR B O   1 
ATOM   4780  C CB  . TYR B 1 241 ? 11.885  -7.845  14.566  1.00 40.26  ? 250  TYR B CB  1 
ATOM   4781  C CG  . TYR B 1 241 ? 13.166  -7.108  14.718  1.00 40.52  ? 250  TYR B CG  1 
ATOM   4782  C CD1 . TYR B 1 241 ? 13.294  -5.822  14.195  1.00 40.97  ? 250  TYR B CD1 1 
ATOM   4783  C CD2 . TYR B 1 241 ? 14.240  -7.654  15.408  1.00 44.11  ? 250  TYR B CD2 1 
ATOM   4784  C CE1 . TYR B 1 241 ? 14.475  -5.079  14.331  1.00 41.72  ? 250  TYR B CE1 1 
ATOM   4785  C CE2 . TYR B 1 241 ? 15.449  -6.916  15.558  1.00 45.47  ? 250  TYR B CE2 1 
ATOM   4786  C CZ  . TYR B 1 241 ? 15.548  -5.622  14.998  1.00 43.58  ? 250  TYR B CZ  1 
ATOM   4787  O OH  . TYR B 1 241 ? 16.689  -4.856  15.101  1.00 43.21  ? 250  TYR B OH  1 
ATOM   4788  N N   . MET B 1 242 ? 9.930   -9.603  12.693  1.00 43.34  ? 251  MET B N   1 
ATOM   4789  C CA  . MET B 1 242 ? 8.594   -10.175 12.521  1.00 44.79  ? 251  MET B CA  1 
ATOM   4790  C C   . MET B 1 242 ? 8.750   -11.658 12.338  1.00 47.47  ? 251  MET B C   1 
ATOM   4791  O O   . MET B 1 242 ? 8.025   -12.429 12.907  1.00 49.09  ? 251  MET B O   1 
ATOM   4792  C CB  . MET B 1 242 ? 7.914   -9.605  11.285  1.00 44.32  ? 251  MET B CB  1 
ATOM   4793  C CG  . MET B 1 242 ? 7.700   -8.115  11.285  1.00 42.11  ? 251  MET B CG  1 
ATOM   4794  S SD  . MET B 1 242 ? 6.301   -7.737  12.351  1.00 41.75  ? 251  MET B SD  1 
ATOM   4795  C CE  . MET B 1 242 ? 5.984   -6.078  11.772  1.00 39.21  ? 251  MET B CE  1 
ATOM   4796  N N   . LEU B 1 243 ? 9.728   -12.032 11.534  1.00 48.40  ? 252  LEU B N   1 
ATOM   4797  C CA  . LEU B 1 243 ? 10.014  -13.408 11.249  1.00 51.30  ? 252  LEU B CA  1 
ATOM   4798  C C   . LEU B 1 243 ? 11.488  -13.711 11.379  1.00 51.90  ? 252  LEU B C   1 
ATOM   4799  O O   . LEU B 1 243 ? 12.331  -13.007 10.802  1.00 50.67  ? 252  LEU B O   1 
ATOM   4800  C CB  . LEU B 1 243 ? 9.589   -13.748 9.834   1.00 52.27  ? 252  LEU B CB  1 
ATOM   4801  C CG  . LEU B 1 243 ? 8.417   -14.704 9.698   1.00 54.45  ? 252  LEU B CG  1 
ATOM   4802  C CD1 . LEU B 1 243 ? 8.640   -15.577 8.503   1.00 56.58  ? 252  LEU B CD1 1 
ATOM   4803  C CD2 . LEU B 1 243 ? 8.335   -15.590 10.875  1.00 57.25  ? 252  LEU B CD2 1 
ATOM   4804  N N   . THR B 1 244 ? 11.778  -14.780 12.115  1.00 53.89  ? 253  THR B N   1 
ATOM   4805  C CA  . THR B 1 244 ? 13.115  -15.289 12.231  1.00 55.08  ? 253  THR B CA  1 
ATOM   4806  C C   . THR B 1 244 ? 13.355  -16.149 11.048  1.00 57.16  ? 253  THR B C   1 
ATOM   4807  O O   . THR B 1 244 ? 12.407  -16.691 10.468  1.00 58.70  ? 253  THR B O   1 
ATOM   4808  C CB  . THR B 1 244 ? 13.236  -16.166 13.446  1.00 56.77  ? 253  THR B CB  1 
ATOM   4809  O OG1 . THR B 1 244 ? 12.854  -15.395 14.589  1.00 55.78  ? 253  THR B OG1 1 
ATOM   4810  C CG2 . THR B 1 244 ? 14.675  -16.705 13.620  1.00 58.14  ? 253  THR B CG2 1 
ATOM   4811  N N   . ASN B 1 245 ? 14.628  -16.262 10.695  1.00 57.59  ? 254  ASN B N   1 
ATOM   4812  C CA  . ASN B 1 245 ? 15.037  -17.199 9.695   1.00 60.21  ? 254  ASN B CA  1 
ATOM   4813  C C   . ASN B 1 245 ? 14.542  -18.599 10.042  1.00 63.11  ? 254  ASN B C   1 
ATOM   4814  O O   . ASN B 1 245 ? 13.908  -19.241 9.214   1.00 64.36  ? 254  ASN B O   1 
ATOM   4815  C CB  . ASN B 1 245 ? 16.547  -17.177 9.566   1.00 60.74  ? 254  ASN B CB  1 
ATOM   4816  C CG  . ASN B 1 245 ? 17.044  -18.054 8.429   1.00 63.54  ? 254  ASN B CG  1 
ATOM   4817  O OD1 . ASN B 1 245 ? 16.915  -17.698 7.253   1.00 64.06  ? 254  ASN B OD1 1 
ATOM   4818  N ND2 . ASN B 1 245 ? 17.625  -19.202 8.775   1.00 65.76  ? 254  ASN B ND2 1 
ATOM   4819  N N   . SER B 1 246 ? 14.809  -19.043 11.272  1.00 64.17  ? 255  SER B N   1 
ATOM   4820  C CA  . SER B 1 246 ? 14.312  -20.326 11.786  1.00 67.53  ? 255  SER B CA  1 
ATOM   4821  C C   . SER B 1 246 ? 12.856  -20.470 11.421  1.00 67.58  ? 255  SER B C   1 
ATOM   4822  O O   . SER B 1 246 ? 12.433  -21.422 10.765  1.00 70.29  ? 255  SER B O   1 
ATOM   4823  C CB  . SER B 1 246 ? 14.410  -20.406 13.319  1.00 67.73  ? 255  SER B CB  1 
ATOM   4824  O OG  . SER B 1 246 ? 15.450  -19.609 13.871  1.00 68.34  ? 255  SER B OG  1 
ATOM   4825  N N   . GLU B 1 247 ? 12.089  -19.487 11.847  1.00 64.87  ? 256  GLU B N   1 
ATOM   4826  C CA  . GLU B 1 247 ? 10.666  -19.483 11.606  1.00 64.95  ? 256  GLU B CA  1 
ATOM   4827  C C   . GLU B 1 247 ? 10.327  -19.496 10.121  1.00 64.83  ? 256  GLU B C   1 
ATOM   4828  O O   . GLU B 1 247 ? 9.707   -20.457 9.631   1.00 67.05  ? 256  GLU B O   1 
ATOM   4829  C CB  . GLU B 1 247 ? 10.061  -18.283 12.304  1.00 62.26  ? 256  GLU B CB  1 
ATOM   4830  C CG  . GLU B 1 247 ? 10.179  -18.413 13.806  1.00 64.11  ? 256  GLU B CG  1 
ATOM   4831  C CD  . GLU B 1 247 ? 9.885   -17.131 14.544  1.00 63.47  ? 256  GLU B CD  1 
ATOM   4832  O OE1 . GLU B 1 247 ? 9.950   -16.043 13.920  1.00 63.25  ? 256  GLU B OE1 1 
ATOM   4833  O OE2 . GLU B 1 247 ? 9.601   -17.218 15.759  1.00 63.25  ? 256  GLU B OE2 1 
ATOM   4834  N N   . LEU B 1 248 ? 10.751  -18.440 9.418   1.00 62.12  ? 257  LEU B N   1 
ATOM   4835  C CA  . LEU B 1 248 ? 10.537  -18.343 7.985   1.00 61.66  ? 257  LEU B CA  1 
ATOM   4836  C C   . LEU B 1 248 ? 10.849  -19.678 7.323   1.00 65.03  ? 257  LEU B C   1 
ATOM   4837  O O   . LEU B 1 248 ? 10.090  -20.167 6.495   1.00 66.44  ? 257  LEU B O   1 
ATOM   4838  C CB  . LEU B 1 248 ? 11.397  -17.235 7.379   1.00 58.76  ? 257  LEU B CB  1 
ATOM   4839  C CG  . LEU B 1 248 ? 11.400  -17.199 5.851   1.00 57.04  ? 257  LEU B CG  1 
ATOM   4840  C CD1 . LEU B 1 248 ? 9.986   -17.025 5.281   1.00 54.46  ? 257  LEU B CD1 1 
ATOM   4841  C CD2 . LEU B 1 248 ? 12.354  -16.114 5.382   1.00 53.09  ? 257  LEU B CD2 1 
ATOM   4842  N N   . LEU B 1 249 ? 11.964  -20.274 7.710   1.00 66.47  ? 258  LEU B N   1 
ATOM   4843  C CA  . LEU B 1 249 ? 12.375  -21.484 7.067   1.00 70.12  ? 258  LEU B CA  1 
ATOM   4844  C C   . LEU B 1 249 ? 11.373  -22.595 7.244   1.00 73.30  ? 258  LEU B C   1 
ATOM   4845  O O   . LEU B 1 249 ? 11.001  -23.249 6.261   1.00 75.33  ? 258  LEU B O   1 
ATOM   4846  C CB  . LEU B 1 249 ? 13.763  -21.911 7.515   1.00 71.11  ? 258  LEU B CB  1 
ATOM   4847  C CG  . LEU B 1 249 ? 14.789  -21.457 6.469   1.00 71.02  ? 258  LEU B CG  1 
ATOM   4848  C CD1 . LEU B 1 249 ? 16.204  -21.308 7.042   1.00 71.52  ? 258  LEU B CD1 1 
ATOM   4849  C CD2 . LEU B 1 249 ? 14.792  -22.401 5.257   1.00 75.51  ? 258  LEU B CD2 1 
ATOM   4850  N N   . SER B 1 250 ? 10.909  -22.810 8.474   1.00 74.04  ? 259  SER B N   1 
ATOM   4851  C CA  . SER B 1 250 ? 9.957   -23.911 8.711   1.00 77.28  ? 259  SER B CA  1 
ATOM   4852  C C   . SER B 1 250 ? 8.567   -23.566 8.162   1.00 76.58  ? 259  SER B C   1 
ATOM   4853  O O   . SER B 1 250 ? 7.788   -24.450 7.789   1.00 79.13  ? 259  SER B O   1 
ATOM   4854  C CB  . SER B 1 250 ? 9.885   -24.291 10.192  1.00 78.13  ? 259  SER B CB  1 
ATOM   4855  O OG  . SER B 1 250 ? 8.991   -23.438 10.881  1.00 75.96  ? 259  SER B OG  1 
ATOM   4856  N N   . LEU B 1 251 ? 8.271   -22.271 8.122   1.00 73.05  ? 260  LEU B N   1 
ATOM   4857  C CA  . LEU B 1 251 ? 7.060   -21.803 7.491   1.00 72.09  ? 260  LEU B CA  1 
ATOM   4858  C C   . LEU B 1 251 ? 7.034   -22.140 6.022   1.00 73.27  ? 260  LEU B C   1 
ATOM   4859  O O   . LEU B 1 251 ? 6.026   -22.596 5.504   1.00 74.69  ? 260  LEU B O   1 
ATOM   4860  C CB  . LEU B 1 251 ? 6.943   -20.309 7.638   1.00 68.39  ? 260  LEU B CB  1 
ATOM   4861  C CG  . LEU B 1 251 ? 5.992   -19.860 8.721   1.00 67.56  ? 260  LEU B CG  1 
ATOM   4862  C CD1 . LEU B 1 251 ? 5.792   -18.364 8.550   1.00 65.22  ? 260  LEU B CD1 1 
ATOM   4863  C CD2 . LEU B 1 251 ? 4.688   -20.593 8.575   1.00 69.27  ? 260  LEU B CD2 1 
ATOM   4864  N N   . ILE B 1 252 ? 8.149   -21.890 5.350   1.00 72.92  ? 261  ILE B N   1 
ATOM   4865  C CA  . ILE B 1 252 ? 8.282   -22.239 3.955   1.00 74.65  ? 261  ILE B CA  1 
ATOM   4866  C C   . ILE B 1 252 ? 7.992   -23.715 3.860   1.00 79.34  ? 261  ILE B C   1 
ATOM   4867  O O   . ILE B 1 252 ? 7.124   -24.152 3.106   1.00 81.10  ? 261  ILE B O   1 
ATOM   4868  C CB  . ILE B 1 252 ? 9.698   -21.988 3.469   1.00 73.61  ? 261  ILE B CB  1 
ATOM   4869  C CG1 . ILE B 1 252 ? 9.861   -20.528 3.092   1.00 70.27  ? 261  ILE B CG1 1 
ATOM   4870  C CG2 . ILE B 1 252 ? 10.000  -22.850 2.267   1.00 75.63  ? 261  ILE B CG2 1 
ATOM   4871  C CD1 . ILE B 1 252 ? 11.228  -20.011 3.364   1.00 69.18  ? 261  ILE B CD1 1 
ATOM   4872  N N   . ASN B 1 253 ? 8.713   -24.476 4.668   1.00 81.92  ? 262  ASN B N   1 
ATOM   4873  C CA  . ASN B 1 253 ? 8.538   -25.905 4.723   1.00 86.72  ? 262  ASN B CA  1 
ATOM   4874  C C   . ASN B 1 253 ? 7.070   -26.319 4.695   1.00 88.55  ? 262  ASN B C   1 
ATOM   4875  O O   . ASN B 1 253 ? 6.714   -27.292 4.040   1.00 91.80  ? 262  ASN B O   1 
ATOM   4876  C CB  . ASN B 1 253 ? 9.205   -26.444 5.981   1.00 87.90  ? 262  ASN B CB  1 
ATOM   4877  C CG  . ASN B 1 253 ? 9.718   -27.858 5.812   1.00 92.72  ? 262  ASN B CG  1 
ATOM   4878  O OD1 . ASN B 1 253 ? 9.597   -28.470 4.748   1.00 95.31  ? 262  ASN B OD1 1 
ATOM   4879  N ND2 . ASN B 1 253 ? 10.309  -28.383 6.870   1.00 96.25  ? 262  ASN B ND2 1 
ATOM   4880  N N   . ASP B 1 254 ? 6.226   -25.562 5.390   1.00 86.98  ? 263  ASP B N   1 
ATOM   4881  C CA  . ASP B 1 254 ? 4.812   -25.903 5.543   1.00 88.76  ? 263  ASP B CA  1 
ATOM   4882  C C   . ASP B 1 254 ? 3.931   -25.503 4.346   1.00 88.14  ? 263  ASP B C   1 
ATOM   4883  O O   . ASP B 1 254 ? 2.762   -25.884 4.262   1.00 89.64  ? 263  ASP B O   1 
ATOM   4884  C CB  . ASP B 1 254 ? 4.272   -25.295 6.850   1.00 87.48  ? 263  ASP B CB  1 
ATOM   4885  C CG  . ASP B 1 254 ? 2.782   -25.519 7.030   1.00 90.00  ? 263  ASP B CG  1 
ATOM   4886  O OD1 . ASP B 1 254 ? 2.324   -26.669 6.882   1.00 96.41  ? 263  ASP B OD1 1 
ATOM   4887  O OD2 . ASP B 1 254 ? 2.060   -24.549 7.308   1.00 88.44  ? 263  ASP B OD2 1 
ATOM   4888  N N   . MET B 1 255 ? 4.488   -24.745 3.414   1.00 86.09  ? 264  MET B N   1 
ATOM   4889  C CA  . MET B 1 255 ? 3.697   -24.244 2.298   1.00 85.42  ? 264  MET B CA  1 
ATOM   4890  C C   . MET B 1 255 ? 3.419   -25.321 1.280   1.00 88.73  ? 264  MET B C   1 
ATOM   4891  O O   . MET B 1 255 ? 4.303   -26.106 0.981   1.00 90.77  ? 264  MET B O   1 
ATOM   4892  C CB  . MET B 1 255 ? 4.408   -23.092 1.625   1.00 82.35  ? 264  MET B CB  1 
ATOM   4893  C CG  . MET B 1 255 ? 4.781   -21.980 2.591   1.00 79.45  ? 264  MET B CG  1 
ATOM   4894  S SD  . MET B 1 255 ? 5.589   -20.606 1.781   1.00 75.73  ? 264  MET B SD  1 
ATOM   4895  C CE  . MET B 1 255 ? 6.295   -21.450 0.365   1.00 79.70  ? 264  MET B CE  1 
ATOM   4896  N N   . PRO B 1 256 ? 2.186   -25.361 0.746   1.00 89.69  ? 265  PRO B N   1 
ATOM   4897  C CA  . PRO B 1 256 ? 1.714   -26.347 -0.231  1.00 93.14  ? 265  PRO B CA  1 
ATOM   4898  C C   . PRO B 1 256 ? 2.330   -26.216 -1.622  1.00 93.08  ? 265  PRO B C   1 
ATOM   4899  O O   . PRO B 1 256 ? 1.617   -25.978 -2.610  1.00 92.84  ? 265  PRO B O   1 
ATOM   4900  C CB  . PRO B 1 256 ? 0.210   -26.072 -0.302  1.00 93.21  ? 265  PRO B CB  1 
ATOM   4901  C CG  . PRO B 1 256 ? 0.067   -24.696 0.101   1.00 89.36  ? 265  PRO B CG  1 
ATOM   4902  C CD  . PRO B 1 256 ? 1.074   -24.518 1.199   1.00 88.02  ? 265  PRO B CD  1 
ATOM   4903  N N   . ILE B 1 257 ? 3.645   -26.405 -1.688  1.00 93.64  ? 266  ILE B N   1 
ATOM   4904  C CA  . ILE B 1 257 ? 4.404   -26.302 -2.939  1.00 94.00  ? 266  ILE B CA  1 
ATOM   4905  C C   . ILE B 1 257 ? 5.361   -27.484 -3.177  1.00 97.35  ? 266  ILE B C   1 
ATOM   4906  O O   . ILE B 1 257 ? 5.625   -28.310 -2.280  1.00 99.41  ? 266  ILE B O   1 
ATOM   4907  C CB  . ILE B 1 257 ? 5.198   -24.959 -3.014  1.00 90.15  ? 266  ILE B CB  1 
ATOM   4908  C CG1 . ILE B 1 257 ? 6.019   -24.718 -1.731  1.00 88.59  ? 266  ILE B CG1 1 
ATOM   4909  C CG2 . ILE B 1 257 ? 4.248   -23.790 -3.265  1.00 87.69  ? 266  ILE B CG2 1 
ATOM   4910  C CD1 . ILE B 1 257 ? 7.219   -23.809 -1.929  1.00 85.71  ? 266  ILE B CD1 1 
ATOM   4911  N N   . THR B 1 258 ? 5.888   -27.541 -4.395  1.00 97.92  ? 267  THR B N   1 
ATOM   4912  C CA  . THR B 1 258 ? 6.841   -28.577 -4.759  1.00 100.99 ? 267  THR B CA  1 
ATOM   4913  C C   . THR B 1 258 ? 8.108   -28.479 -3.893  1.00 100.08 ? 267  THR B C   1 
ATOM   4914  O O   . THR B 1 258 ? 8.305   -27.518 -3.150  1.00 96.78  ? 267  THR B O   1 
ATOM   4915  C CB  . THR B 1 258 ? 7.188   -28.532 -6.280  1.00 101.51 ? 267  THR B CB  1 
ATOM   4916  O OG1 . THR B 1 258 ? 8.545   -28.119 -6.468  1.00 100.82 ? 267  THR B OG1 1 
ATOM   4917  C CG2 . THR B 1 258 ? 6.241   -27.600 -7.055  1.00 99.17  ? 267  THR B CG2 1 
ATOM   4918  N N   . ASN B 1 259 ? 8.968   -29.477 -3.989  1.00 103.04 ? 268  ASN B N   1 
ATOM   4919  C CA  . ASN B 1 259 ? 10.171  -29.473 -3.181  1.00 102.72 ? 268  ASN B CA  1 
ATOM   4920  C C   . ASN B 1 259 ? 11.291  -28.567 -3.639  1.00 100.15 ? 268  ASN B C   1 
ATOM   4921  O O   . ASN B 1 259 ? 11.976  -27.980 -2.813  1.00 97.92  ? 268  ASN B O   1 
ATOM   4922  C CB  . ASN B 1 259 ? 10.686  -30.883 -3.025  1.00 107.25 ? 268  ASN B CB  1 
ATOM   4923  C CG  . ASN B 1 259 ? 10.231  -31.502 -1.742  1.00 109.49 ? 268  ASN B CG  1 
ATOM   4924  O OD1 . ASN B 1 259 ? 9.386   -30.945 -1.039  1.00 108.80 ? 268  ASN B OD1 1 
ATOM   4925  N ND2 . ASN B 1 259 ? 10.791  -32.651 -1.411  1.00 113.91 ? 268  ASN B ND2 1 
ATOM   4926  N N   . ASP B 1 260 ? 11.487  -28.483 -4.952  1.00 100.65 ? 269  ASP B N   1 
ATOM   4927  C CA  . ASP B 1 260 ? 12.455  -27.556 -5.547  1.00 98.36  ? 269  ASP B CA  1 
ATOM   4928  C C   . ASP B 1 260 ? 12.036  -26.149 -5.212  1.00 93.38  ? 269  ASP B C   1 
ATOM   4929  O O   . ASP B 1 260 ? 12.849  -25.292 -4.866  1.00 90.91  ? 269  ASP B O   1 
ATOM   4930  C CB  . ASP B 1 260 ? 12.484  -27.715 -7.069  1.00 100.11 ? 269  ASP B CB  1 
ATOM   4931  C CG  . ASP B 1 260 ? 13.004  -29.071 -7.508  1.00 106.46 ? 269  ASP B CG  1 
ATOM   4932  O OD1 . ASP B 1 260 ? 13.720  -29.719 -6.720  1.00 110.69 ? 269  ASP B OD1 1 
ATOM   4933  O OD2 . ASP B 1 260 ? 12.706  -29.484 -8.647  1.00 111.16 ? 269  ASP B OD2 1 
ATOM   4934  N N   . GLN B 1 261 ? 10.738  -25.936 -5.319  1.00 91.82  ? 270  GLN B N   1 
ATOM   4935  C CA  . GLN B 1 261 ? 10.164  -24.695 -4.959  1.00 87.75  ? 270  GLN B CA  1 
ATOM   4936  C C   . GLN B 1 261 ? 10.623  -24.326 -3.552  1.00 85.44  ? 270  GLN B C   1 
ATOM   4937  O O   . GLN B 1 261 ? 11.244  -23.277 -3.340  1.00 82.53  ? 270  GLN B O   1 
ATOM   4938  C CB  . GLN B 1 261 ? 8.659   -24.801 -5.061  1.00 88.30  ? 270  GLN B CB  1 
ATOM   4939  C CG  . GLN B 1 261 ? 8.070   -23.546 -5.598  1.00 86.83  ? 270  GLN B CG  1 
ATOM   4940  C CD  . GLN B 1 261 ? 6.732   -23.747 -6.238  1.00 90.43  ? 270  GLN B CD  1 
ATOM   4941  O OE1 . GLN B 1 261 ? 5.867   -22.893 -6.107  1.00 90.40  ? 270  GLN B OE1 1 
ATOM   4942  N NE2 . GLN B 1 261 ? 6.546   -24.866 -6.941  1.00 94.05  ? 270  GLN B NE2 1 
ATOM   4943  N N   . LYS B 1 262 ? 10.371  -25.203 -2.593  1.00 86.60  ? 271  LYS B N   1 
ATOM   4944  C CA  . LYS B 1 262 ? 10.786  -24.898 -1.231  1.00 84.68  ? 271  LYS B CA  1 
ATOM   4945  C C   . LYS B 1 262 ? 12.267  -24.549 -1.177  1.00 83.52  ? 271  LYS B C   1 
ATOM   4946  O O   . LYS B 1 262 ? 12.652  -23.557 -0.574  1.00 80.68  ? 271  LYS B O   1 
ATOM   4947  C CB  . LYS B 1 262 ? 10.458  -26.039 -0.274  1.00 87.22  ? 271  LYS B CB  1 
ATOM   4948  C CG  . LYS B 1 262 ? 8.969   -26.225 -0.076  1.00 87.97  ? 271  LYS B CG  1 
ATOM   4949  C CD  . LYS B 1 262 ? 8.624   -27.227 1.017   1.00 91.15  ? 271  LYS B CD  1 
ATOM   4950  C CE  . LYS B 1 262 ? 7.394   -28.060 0.620   1.00 94.02  ? 271  LYS B CE  1 
ATOM   4951  N NZ  . LYS B 1 262 ? 6.845   -28.857 1.751   1.00 95.45  ? 271  LYS B NZ  1 
ATOM   4952  N N   . LYS B 1 263 ? 13.085  -25.340 -1.853  1.00 85.89  ? 272  LYS B N   1 
ATOM   4953  C CA  . LYS B 1 263 ? 14.523  -25.130 -1.844  1.00 85.50  ? 272  LYS B CA  1 
ATOM   4954  C C   . LYS B 1 263 ? 14.892  -23.771 -2.413  1.00 81.43  ? 272  LYS B C   1 
ATOM   4955  O O   . LYS B 1 263 ? 15.802  -23.119 -1.903  1.00 79.76  ? 272  LYS B O   1 
ATOM   4956  C CB  . LYS B 1 263 ? 15.222  -26.239 -2.630  1.00 89.77  ? 272  LYS B CB  1 
ATOM   4957  C CG  . LYS B 1 263 ? 16.716  -26.031 -2.866  1.00 92.35  ? 272  LYS B CG  1 
ATOM   4958  C CD  . LYS B 1 263 ? 17.217  -27.000 -3.925  1.00 100.72 ? 272  LYS B CD  1 
ATOM   4959  C CE  . LYS B 1 263 ? 18.732  -27.114 -3.922  1.00 103.86 ? 272  LYS B CE  1 
ATOM   4960  N NZ  . LYS B 1 263 ? 19.172  -28.282 -4.749  1.00 109.72 ? 272  LYS B NZ  1 
ATOM   4961  N N   . LEU B 1 264 ? 14.197  -23.356 -3.470  1.00 79.74  ? 273  LEU B N   1 
ATOM   4962  C CA  . LEU B 1 264 ? 14.440  -22.052 -4.075  1.00 75.71  ? 273  LEU B CA  1 
ATOM   4963  C C   . LEU B 1 264 ? 14.180  -20.963 -3.066  1.00 72.22  ? 273  LEU B C   1 
ATOM   4964  O O   . LEU B 1 264 ? 15.020  -20.082 -2.843  1.00 69.95  ? 273  LEU B O   1 
ATOM   4965  C CB  . LEU B 1 264 ? 13.510  -21.834 -5.244  1.00 75.38  ? 273  LEU B CB  1 
ATOM   4966  C CG  . LEU B 1 264 ? 13.644  -20.498 -5.946  1.00 70.72  ? 273  LEU B CG  1 
ATOM   4967  C CD1 . LEU B 1 264 ? 14.907  -20.463 -6.743  1.00 70.80  ? 273  LEU B CD1 1 
ATOM   4968  C CD2 . LEU B 1 264 ? 12.488  -20.359 -6.865  1.00 69.46  ? 273  LEU B CD2 1 
ATOM   4969  N N   . MET B 1 265 ? 13.003  -21.040 -2.457  1.00 71.53  ? 274  MET B N   1 
ATOM   4970  C CA  . MET B 1 265 ? 12.627  -20.105 -1.422  1.00 68.66  ? 274  MET B CA  1 
ATOM   4971  C C   . MET B 1 265 ? 13.639  -20.063 -0.300  1.00 68.54  ? 274  MET B C   1 
ATOM   4972  O O   . MET B 1 265 ? 14.076  -18.994 0.104   1.00 66.40  ? 274  MET B O   1 
ATOM   4973  C CB  . MET B 1 265 ? 11.245  -20.424 -0.897  1.00 68.59  ? 274  MET B CB  1 
ATOM   4974  C CG  . MET B 1 265 ? 10.205  -20.103 -1.929  1.00 67.74  ? 274  MET B CG  1 
ATOM   4975  S SD  . MET B 1 265 ? 8.493   -20.212 -1.374  1.00 67.47  ? 274  MET B SD  1 
ATOM   4976  C CE  . MET B 1 265 ? 8.426   -18.873 -0.177  1.00 64.55  ? 274  MET B CE  1 
ATOM   4977  N N   . SER B 1 266 ? 14.045  -21.223 0.177   1.00 71.52  ? 275  SER B N   1 
ATOM   4978  C CA  . SER B 1 266 ? 15.014  -21.269 1.248   1.00 71.81  ? 275  SER B CA  1 
ATOM   4979  C C   . SER B 1 266 ? 16.330  -20.629 0.886   1.00 71.26  ? 275  SER B C   1 
ATOM   4980  O O   . SER B 1 266 ? 16.941  -19.992 1.734   1.00 69.64  ? 275  SER B O   1 
ATOM   4981  C CB  . SER B 1 266 ? 15.265  -22.695 1.658   1.00 75.26  ? 275  SER B CB  1 
ATOM   4982  O OG  . SER B 1 266 ? 14.032  -23.324 1.886   1.00 76.73  ? 275  SER B OG  1 
ATOM   4983  N N   . ASN B 1 267 ? 16.773  -20.784 -0.361  1.00 73.10  ? 276  ASN B N   1 
ATOM   4984  C CA  . ASN B 1 267 ? 18.062  -20.203 -0.770  1.00 73.16  ? 276  ASN B CA  1 
ATOM   4985  C C   . ASN B 1 267 ? 17.993  -18.734 -1.199  1.00 69.84  ? 276  ASN B C   1 
ATOM   4986  O O   . ASN B 1 267 ? 18.938  -18.233 -1.820  1.00 69.53  ? 276  ASN B O   1 
ATOM   4987  C CB  . ASN B 1 267 ? 18.751  -21.049 -1.856  1.00 76.37  ? 276  ASN B CB  1 
ATOM   4988  C CG  . ASN B 1 267 ? 19.408  -22.310 -1.302  1.00 81.17  ? 276  ASN B CG  1 
ATOM   4989  O OD1 . ASN B 1 267 ? 20.089  -22.288 -0.274  1.00 83.27  ? 276  ASN B OD1 1 
ATOM   4990  N ND2 . ASN B 1 267 ? 19.219  -23.416 -2.007  1.00 85.96  ? 276  ASN B ND2 1 
ATOM   4991  N N   . ASN B 1 268 ? 16.894  -18.056 -0.845  1.00 67.82  ? 277  ASN B N   1 
ATOM   4992  C CA  . ASN B 1 268 ? 16.607  -16.683 -1.301  1.00 64.80  ? 277  ASN B CA  1 
ATOM   4993  C C   . ASN B 1 268 ? 15.832  -15.797 -0.351  1.00 62.20  ? 277  ASN B C   1 
ATOM   4994  O O   . ASN B 1 268 ? 15.257  -14.795 -0.763  1.00 60.15  ? 277  ASN B O   1 
ATOM   4995  C CB  . ASN B 1 268 ? 15.839  -16.735 -2.603  1.00 65.13  ? 277  ASN B CB  1 
ATOM   4996  C CG  . ASN B 1 268 ? 16.729  -16.956 -3.759  1.00 66.41  ? 277  ASN B CG  1 
ATOM   4997  O OD1 . ASN B 1 268 ? 17.316  -16.015 -4.295  1.00 65.29  ? 277  ASN B OD1 1 
ATOM   4998  N ND2 . ASN B 1 268 ? 16.867  -18.212 -4.152  1.00 70.14  ? 277  ASN B ND2 1 
ATOM   4999  N N   . VAL B 1 269 ? 15.813  -16.189 0.910   1.00 62.33  ? 278  VAL B N   1 
ATOM   5000  C CA  . VAL B 1 269 ? 15.136  -15.460 1.964   1.00 60.24  ? 278  VAL B CA  1 
ATOM   5001  C C   . VAL B 1 269 ? 14.988  -13.945 1.725   1.00 57.16  ? 278  VAL B C   1 
ATOM   5002  O O   . VAL B 1 269 ? 13.917  -13.371 1.948   1.00 55.92  ? 278  VAL B O   1 
ATOM   5003  C CB  . VAL B 1 269 ? 15.872  -15.663 3.295   1.00 60.36  ? 278  VAL B CB  1 
ATOM   5004  C CG1 . VAL B 1 269 ? 15.381  -16.909 3.971   1.00 61.85  ? 278  VAL B CG1 1 
ATOM   5005  C CG2 . VAL B 1 269 ? 17.385  -15.717 3.053   1.00 62.11  ? 278  VAL B CG2 1 
ATOM   5006  N N   . GLN B 1 270 ? 16.056  -13.289 1.288   1.00 56.03  ? 279  GLN B N   1 
ATOM   5007  C CA  . GLN B 1 270 ? 16.011  -11.846 1.149   1.00 53.21  ? 279  GLN B CA  1 
ATOM   5008  C C   . GLN B 1 270 ? 14.814  -11.405 0.277   1.00 51.66  ? 279  GLN B C   1 
ATOM   5009  O O   . GLN B 1 270 ? 13.885  -10.741 0.746   1.00 49.91  ? 279  GLN B O   1 
ATOM   5010  C CB  . GLN B 1 270 ? 17.336  -11.344 0.585   1.00 53.45  ? 279  GLN B CB  1 
ATOM   5011  C CG  . GLN B 1 270 ? 17.682  -9.953  1.053   1.00 53.45  ? 279  GLN B CG  1 
ATOM   5012  C CD  . GLN B 1 270 ? 18.923  -9.405  0.397   1.00 57.39  ? 279  GLN B CD  1 
ATOM   5013  O OE1 . GLN B 1 270 ? 19.224  -9.710  -0.777  1.00 60.65  ? 279  GLN B OE1 1 
ATOM   5014  N NE2 . GLN B 1 270 ? 19.665  -8.587  1.149   1.00 56.52  ? 279  GLN B NE2 1 
ATOM   5015  N N   . ILE B 1 271 ? 14.835  -11.808 -0.986  1.00 52.05  ? 280  ILE B N   1 
ATOM   5016  C CA  . ILE B 1 271 ? 13.763  -11.510 -1.916  1.00 50.75  ? 280  ILE B CA  1 
ATOM   5017  C C   . ILE B 1 271 ? 12.420  -11.835 -1.273  1.00 50.53  ? 280  ILE B C   1 
ATOM   5018  O O   . ILE B 1 271 ? 11.551  -10.988 -1.142  1.00 48.94  ? 280  ILE B O   1 
ATOM   5019  C CB  . ILE B 1 271 ? 13.935  -12.331 -3.200  1.00 52.76  ? 280  ILE B CB  1 
ATOM   5020  C CG1 . ILE B 1 271 ? 15.320  -12.100 -3.817  1.00 52.55  ? 280  ILE B CG1 1 
ATOM   5021  C CG2 . ILE B 1 271 ? 12.819  -12.049 -4.188  1.00 51.96  ? 280  ILE B CG2 1 
ATOM   5022  C CD1 . ILE B 1 271 ? 15.360  -11.113 -4.954  1.00 50.92  ? 280  ILE B CD1 1 
ATOM   5023  N N   . VAL B 1 272 ? 12.267  -13.073 -0.850  1.00 52.26  ? 281  VAL B N   1 
ATOM   5024  C CA  . VAL B 1 272 ? 11.039  -13.506 -0.220  1.00 52.53  ? 281  VAL B CA  1 
ATOM   5025  C C   . VAL B 1 272 ? 10.566  -12.461 0.751   1.00 50.42  ? 281  VAL B C   1 
ATOM   5026  O O   . VAL B 1 272 ? 9.432   -12.009 0.679   1.00 50.05  ? 281  VAL B O   1 
ATOM   5027  C CB  . VAL B 1 272 ? 11.253  -14.794 0.568   1.00 54.65  ? 281  VAL B CB  1 
ATOM   5028  C CG1 . VAL B 1 272 ? 9.930   -15.318 1.082   1.00 54.52  ? 281  VAL B CG1 1 
ATOM   5029  C CG2 . VAL B 1 272 ? 11.970  -15.829 -0.297  1.00 56.68  ? 281  VAL B CG2 1 
ATOM   5030  N N   . ARG B 1 273 ? 11.447  -12.067 1.657   1.00 49.41  ? 282  ARG B N   1 
ATOM   5031  C CA  . ARG B 1 273 ? 11.063  -11.104 2.667   1.00 47.44  ? 282  ARG B CA  1 
ATOM   5032  C C   . ARG B 1 273 ? 10.613  -9.792  2.019   1.00 46.06  ? 282  ARG B C   1 
ATOM   5033  O O   . ARG B 1 273 ? 9.566   -9.245  2.355   1.00 45.43  ? 282  ARG B O   1 
ATOM   5034  C CB  . ARG B 1 273 ? 12.195  -10.878 3.650   1.00 46.30  ? 282  ARG B CB  1 
ATOM   5035  C CG  . ARG B 1 273 ? 12.562  -12.089 4.453   1.00 46.78  ? 282  ARG B CG  1 
ATOM   5036  C CD  . ARG B 1 273 ? 13.222  -11.641 5.693   1.00 44.85  ? 282  ARG B CD  1 
ATOM   5037  N NE  . ARG B 1 273 ? 13.860  -12.725 6.416   1.00 46.64  ? 282  ARG B NE  1 
ATOM   5038  C CZ  . ARG B 1 273 ? 13.581  -13.042 7.674   1.00 48.09  ? 282  ARG B CZ  1 
ATOM   5039  N NH1 . ARG B 1 273 ? 12.653  -12.348 8.352   1.00 45.82  ? 282  ARG B NH1 1 
ATOM   5040  N NH2 . ARG B 1 273 ? 14.246  -14.046 8.253   1.00 51.31  ? 282  ARG B NH2 1 
ATOM   5041  N N   . GLN B 1 274 ? 11.374  -9.311  1.052   1.00 46.01  ? 283  GLN B N   1 
ATOM   5042  C CA  . GLN B 1 274 ? 10.970  -8.105  0.355   1.00 44.92  ? 283  GLN B CA  1 
ATOM   5043  C C   . GLN B 1 274 ? 9.628   -8.279  -0.333  1.00 45.07  ? 283  GLN B C   1 
ATOM   5044  O O   . GLN B 1 274 ? 8.902   -7.322  -0.587  1.00 43.85  ? 283  GLN B O   1 
ATOM   5045  C CB  . GLN B 1 274 ? 12.039  -7.711  -0.636  1.00 45.01  ? 283  GLN B CB  1 
ATOM   5046  C CG  . GLN B 1 274 ? 13.326  -7.490  0.082   1.00 48.03  ? 283  GLN B CG  1 
ATOM   5047  C CD  . GLN B 1 274 ? 14.470  -7.273  -0.839  1.00 52.90  ? 283  GLN B CD  1 
ATOM   5048  O OE1 . GLN B 1 274 ? 14.388  -7.571  -2.034  1.00 57.03  ? 283  GLN B OE1 1 
ATOM   5049  N NE2 . GLN B 1 274 ? 15.566  -6.748  -0.297  1.00 52.14  ? 283  GLN B NE2 1 
ATOM   5050  N N   . GLN B 1 275 ? 9.276   -9.516  -0.608  1.00 46.90  ? 284  GLN B N   1 
ATOM   5051  C CA  . GLN B 1 275 ? 8.056   -9.741  -1.312  1.00 47.65  ? 284  GLN B CA  1 
ATOM   5052  C C   . GLN B 1 275 ? 6.896   -9.975  -0.386  1.00 47.43  ? 284  GLN B C   1 
ATOM   5053  O O   . GLN B 1 275 ? 5.766   -10.149 -0.845  1.00 47.91  ? 284  GLN B O   1 
ATOM   5054  C CB  . GLN B 1 275 ? 8.224   -10.905 -2.262  1.00 50.27  ? 284  GLN B CB  1 
ATOM   5055  C CG  . GLN B 1 275 ? 8.849   -10.496 -3.566  1.00 51.78  ? 284  GLN B CG  1 
ATOM   5056  C CD  . GLN B 1 275 ? 8.955   -11.653 -4.507  1.00 57.10  ? 284  GLN B CD  1 
ATOM   5057  O OE1 . GLN B 1 275 ? 9.241   -12.778 -4.080  1.00 59.92  ? 284  GLN B OE1 1 
ATOM   5058  N NE2 . GLN B 1 275 ? 8.709   -11.405 -5.799  1.00 57.72  ? 284  GLN B NE2 1 
ATOM   5059  N N   . SER B 1 276 ? 7.163   -9.976  0.911   1.00 46.68  ? 285  SER B N   1 
ATOM   5060  C CA  . SER B 1 276 ? 6.128   -10.326 1.882   1.00 47.38  ? 285  SER B CA  1 
ATOM   5061  C C   . SER B 1 276 ? 5.670   -9.124  2.694   1.00 45.40  ? 285  SER B C   1 
ATOM   5062  O O   . SER B 1 276 ? 6.348   -8.092  2.741   1.00 43.79  ? 285  SER B O   1 
ATOM   5063  C CB  . SER B 1 276 ? 6.620   -11.424 2.814   1.00 48.78  ? 285  SER B CB  1 
ATOM   5064  O OG  . SER B 1 276 ? 7.317   -12.414 2.091   1.00 50.73  ? 285  SER B OG  1 
ATOM   5065  N N   . TYR B 1 277 ? 4.515   -9.267  3.328   1.00 45.87  ? 286  TYR B N   1 
ATOM   5066  C CA  . TYR B 1 277 ? 3.942   -8.204  4.119   1.00 44.51  ? 286  TYR B CA  1 
ATOM   5067  C C   . TYR B 1 277 ? 3.732   -8.708  5.513   1.00 45.50  ? 286  TYR B C   1 
ATOM   5068  O O   . TYR B 1 277 ? 3.666   -9.913  5.730   1.00 48.28  ? 286  TYR B O   1 
ATOM   5069  C CB  . TYR B 1 277 ? 2.588   -7.830  3.569   1.00 44.59  ? 286  TYR B CB  1 
ATOM   5070  C CG  . TYR B 1 277 ? 2.628   -7.102  2.267   1.00 44.55  ? 286  TYR B CG  1 
ATOM   5071  C CD1 . TYR B 1 277 ? 2.934   -7.758  1.095   1.00 47.62  ? 286  TYR B CD1 1 
ATOM   5072  C CD2 . TYR B 1 277 ? 2.334   -5.750  2.197   1.00 44.23  ? 286  TYR B CD2 1 
ATOM   5073  C CE1 . TYR B 1 277 ? 2.960   -7.074  -0.132  1.00 48.63  ? 286  TYR B CE1 1 
ATOM   5074  C CE2 . TYR B 1 277 ? 2.367   -5.049  0.975   1.00 45.13  ? 286  TYR B CE2 1 
ATOM   5075  C CZ  . TYR B 1 277 ? 2.674   -5.719  -0.179  1.00 46.61  ? 286  TYR B CZ  1 
ATOM   5076  O OH  . TYR B 1 277 ? 2.691   -5.041  -1.375  1.00 47.46  ? 286  TYR B OH  1 
ATOM   5077  N N   . SER B 1 278 ? 3.617   -7.801  6.470   1.00 43.93  ? 287  SER B N   1 
ATOM   5078  C CA  . SER B 1 278 ? 3.201   -8.201  7.796   1.00 44.69  ? 287  SER B CA  1 
ATOM   5079  C C   . SER B 1 278 ? 2.091   -7.281  8.205   1.00 44.02  ? 287  SER B C   1 
ATOM   5080  O O   . SER B 1 278 ? 2.236   -6.074  8.189   1.00 42.45  ? 287  SER B O   1 
ATOM   5081  C CB  . SER B 1 278 ? 4.353   -8.133  8.794   1.00 44.08  ? 287  SER B CB  1 
ATOM   5082  O OG  . SER B 1 278 ? 3.898   -8.424  10.113  1.00 44.91  ? 287  SER B OG  1 
ATOM   5083  N N   . ILE B 1 279 ? 0.963   -7.851  8.550   1.00 45.89  ? 288  ILE B N   1 
ATOM   5084  C CA  . ILE B 1 279 ? -0.162  -7.051  8.942   1.00 46.26  ? 288  ILE B CA  1 
ATOM   5085  C C   . ILE B 1 279 ? -0.461  -7.248  10.400  1.00 47.81  ? 288  ILE B C   1 
ATOM   5086  O O   . ILE B 1 279 ? -0.542  -8.380  10.894  1.00 50.31  ? 288  ILE B O   1 
ATOM   5087  C CB  . ILE B 1 279 ? -1.399  -7.531  8.299   1.00 47.64  ? 288  ILE B CB  1 
ATOM   5088  C CG1 . ILE B 1 279 ? -1.119  -8.040  6.885   1.00 47.74  ? 288  ILE B CG1 1 
ATOM   5089  C CG2 . ILE B 1 279 ? -2.437  -6.449  8.412   1.00 47.49  ? 288  ILE B CG2 1 
ATOM   5090  C CD1 . ILE B 1 279 ? -1.656  -7.168  5.789   1.00 47.31  ? 288  ILE B CD1 1 
ATOM   5091  N N   . MET B 1 280 ? -0.685  -6.150  11.091  1.00 47.33  ? 289  MET B N   1 
ATOM   5092  C CA  . MET B 1 280 ? -0.898  -6.239  12.509  1.00 48.57  ? 289  MET B CA  1 
ATOM   5093  C C   . MET B 1 280 ? -2.275  -6.800  12.659  1.00 50.82  ? 289  MET B C   1 
ATOM   5094  O O   . MET B 1 280 ? -3.160  -6.372  11.949  1.00 50.94  ? 289  MET B O   1 
ATOM   5095  C CB  . MET B 1 280 ? -0.822  -4.849  13.102  1.00 46.83  ? 289  MET B CB  1 
ATOM   5096  C CG  . MET B 1 280 ? -0.694  -4.815  14.591  1.00 47.74  ? 289  MET B CG  1 
ATOM   5097  S SD  . MET B 1 280 ? -0.902  -3.137  15.241  1.00 47.85  ? 289  MET B SD  1 
ATOM   5098  C CE  . MET B 1 280 ? -2.405  -2.575  14.443  1.00 48.57  ? 289  MET B CE  1 
ATOM   5099  N N   . SER B 1 281 ? -2.453  -7.761  13.555  1.00 53.27  ? 290  SER B N   1 
ATOM   5100  C CA  . SER B 1 281 ? -3.765  -8.362  13.754  1.00 56.40  ? 290  SER B CA  1 
ATOM   5101  C C   . SER B 1 281 ? -4.478  -7.872  15.016  1.00 56.80  ? 290  SER B C   1 
ATOM   5102  O O   . SER B 1 281 ? -5.470  -7.169  14.900  1.00 56.93  ? 290  SER B O   1 
ATOM   5103  C CB  . SER B 1 281 ? -3.687  -9.888  13.721  1.00 59.13  ? 290  SER B CB  1 
ATOM   5104  O OG  . SER B 1 281 ? -4.941  -10.464 14.052  1.00 62.75  ? 290  SER B OG  1 
ATOM   5105  N N   . ILE B 1 282 ? -4.006  -8.258  16.207  1.00 57.48  ? 291  ILE B N   1 
ATOM   5106  C CA  . ILE B 1 282 ? -4.539  -7.696  17.465  1.00 57.66  ? 291  ILE B CA  1 
ATOM   5107  C C   . ILE B 1 282 ? -3.521  -7.516  18.558  1.00 56.47  ? 291  ILE B C   1 
ATOM   5108  O O   . ILE B 1 282 ? -2.634  -8.362  18.760  1.00 56.31  ? 291  ILE B O   1 
ATOM   5109  C CB  . ILE B 1 282 ? -5.769  -8.448  18.062  1.00 60.66  ? 291  ILE B CB  1 
ATOM   5110  C CG1 . ILE B 1 282 ? -5.809  -9.924  17.647  1.00 62.81  ? 291  ILE B CG1 1 
ATOM   5111  C CG2 . ILE B 1 282 ? -7.053  -7.712  17.717  1.00 61.77  ? 291  ILE B CG2 1 
ATOM   5112  C CD1 . ILE B 1 282 ? -5.166  -10.812 18.656  1.00 63.89  ? 291  ILE B CD1 1 
ATOM   5113  N N   . ILE B 1 283 ? -3.679  -6.389  19.253  1.00 55.54  ? 292  ILE B N   1 
ATOM   5114  C CA  . ILE B 1 283 ? -2.768  -5.973  20.325  1.00 54.83  ? 292  ILE B CA  1 
ATOM   5115  C C   . ILE B 1 283 ? -3.501  -5.875  21.622  1.00 55.91  ? 292  ILE B C   1 
ATOM   5116  O O   . ILE B 1 283 ? -4.523  -5.215  21.709  1.00 56.06  ? 292  ILE B O   1 
ATOM   5117  C CB  . ILE B 1 283 ? -2.152  -4.557  20.151  1.00 52.25  ? 292  ILE B CB  1 
ATOM   5118  C CG1 . ILE B 1 283 ? -2.638  -3.847  18.898  1.00 52.67  ? 292  ILE B CG1 1 
ATOM   5119  C CG2 . ILE B 1 283 ? -0.636  -4.606  20.271  1.00 50.39  ? 292  ILE B CG2 1 
ATOM   5120  C CD1 . ILE B 1 283 ? -2.444  -4.620  17.648  1.00 55.90  ? 292  ILE B CD1 1 
ATOM   5121  N N   . LYS B 1 284 ? -2.947  -6.519  22.631  1.00 56.95  ? 293  LYS B N   1 
ATOM   5122  C CA  . LYS B 1 284 ? -3.465  -6.460  23.961  1.00 58.59  ? 293  LYS B CA  1 
ATOM   5123  C C   . LYS B 1 284 ? -2.241  -6.196  24.751  1.00 57.63  ? 293  LYS B C   1 
ATOM   5124  O O   . LYS B 1 284 ? -1.143  -6.499  24.285  1.00 56.73  ? 293  LYS B O   1 
ATOM   5125  C CB  . LYS B 1 284 ? -4.040  -7.803  24.357  1.00 61.47  ? 293  LYS B CB  1 
ATOM   5126  C CG  . LYS B 1 284 ? -5.070  -8.332  23.395  1.00 63.93  ? 293  LYS B CG  1 
ATOM   5127  C CD  . LYS B 1 284 ? -6.119  -9.148  24.112  1.00 68.20  ? 293  LYS B CD  1 
ATOM   5128  C CE  . LYS B 1 284 ? -7.235  -9.512  23.153  1.00 71.14  ? 293  LYS B CE  1 
ATOM   5129  N NZ  . LYS B 1 284 ? -8.509  -9.644  23.878  1.00 75.02  ? 293  LYS B NZ  1 
ATOM   5130  N N   . GLU B 1 285 ? -2.424  -5.643  25.943  1.00 58.26  ? 294  GLU B N   1 
ATOM   5131  C CA  . GLU B 1 285 ? -1.299  -5.228  26.762  1.00 57.76  ? 294  GLU B CA  1 
ATOM   5132  C C   . GLU B 1 285 ? -0.241  -6.312  26.895  1.00 57.50  ? 294  GLU B C   1 
ATOM   5133  O O   . GLU B 1 285 ? 0.958   -6.009  26.936  1.00 55.96  ? 294  GLU B O   1 
ATOM   5134  C CB  . GLU B 1 285 ? -1.756  -4.766  28.148  1.00 59.09  ? 294  GLU B CB  1 
ATOM   5135  C CG  . GLU B 1 285 ? -2.243  -3.298  28.208  1.00 61.73  ? 294  GLU B CG  1 
ATOM   5136  C CD  . GLU B 1 285 ? -2.595  -2.828  29.638  1.00 66.26  ? 294  GLU B CD  1 
ATOM   5137  O OE1 . GLU B 1 285 ? -1.680  -2.657  30.483  1.00 65.47  ? 294  GLU B OE1 1 
ATOM   5138  O OE2 . GLU B 1 285 ? -3.803  -2.623  29.910  1.00 69.86  ? 294  GLU B OE2 1 
ATOM   5139  N N   . GLU B 1 286 ? -0.672  -7.566  26.940  1.00 58.96  ? 295  GLU B N   1 
ATOM   5140  C CA  . GLU B 1 286 ? 0.260   -8.648  27.179  1.00 59.56  ? 295  GLU B CA  1 
ATOM   5141  C C   . GLU B 1 286 ? 0.404   -9.612  26.017  1.00 59.42  ? 295  GLU B C   1 
ATOM   5142  O O   . GLU B 1 286 ? 1.182   -10.557 26.094  1.00 60.19  ? 295  GLU B O   1 
ATOM   5143  C CB  . GLU B 1 286 ? -0.041  -9.381  28.502  1.00 62.25  ? 295  GLU B CB  1 
ATOM   5144  C CG  . GLU B 1 286 ? -1.461  -9.224  29.082  1.00 67.05  ? 295  GLU B CG  1 
ATOM   5145  C CD  . GLU B 1 286 ? -2.582  -9.606  28.083  1.00 72.82  ? 295  GLU B CD  1 
ATOM   5146  O OE1 . GLU B 1 286 ? -3.100  -8.653  27.433  1.00 73.05  ? 295  GLU B OE1 1 
ATOM   5147  O OE2 . GLU B 1 286 ? -2.934  -10.826 27.943  1.00 75.96  ? 295  GLU B OE2 1 
ATOM   5148  N N   . VAL B 1 287 ? -0.336  -9.379  24.941  1.00 58.30  ? 296  VAL B N   1 
ATOM   5149  C CA  . VAL B 1 287 ? -0.132  -10.174 23.742  1.00 58.21  ? 296  VAL B CA  1 
ATOM   5150  C C   . VAL B 1 287 ? -0.303  -9.372  22.493  1.00 56.20  ? 296  VAL B C   1 
ATOM   5151  O O   . VAL B 1 287 ? -1.186  -8.533  22.404  1.00 55.85  ? 296  VAL B O   1 
ATOM   5152  C CB  . VAL B 1 287 ? -1.101  -11.320 23.581  1.00 60.97  ? 296  VAL B CB  1 
ATOM   5153  C CG1 . VAL B 1 287 ? -0.503  -12.309 22.594  1.00 61.81  ? 296  VAL B CG1 1 
ATOM   5154  C CG2 . VAL B 1 287 ? -1.420  -11.991 24.923  1.00 63.89  ? 296  VAL B CG2 1 
ATOM   5155  N N   . LEU B 1 288 ? 0.543   -9.678  21.519  1.00 54.95  ? 297  LEU B N   1 
ATOM   5156  C CA  . LEU B 1 288 ? 0.498   -9.082  20.204  1.00 52.79  ? 297  LEU B CA  1 
ATOM   5157  C C   . LEU B 1 288 ? 0.460   -10.209 19.179  1.00 53.70  ? 297  LEU B C   1 
ATOM   5158  O O   . LEU B 1 288 ? 1.238   -11.164 19.243  1.00 54.91  ? 297  LEU B O   1 
ATOM   5159  C CB  . LEU B 1 288 ? 1.718   -8.170  19.975  1.00 50.14  ? 297  LEU B CB  1 
ATOM   5160  C CG  . LEU B 1 288 ? 1.888   -7.751  18.509  1.00 49.23  ? 297  LEU B CG  1 
ATOM   5161  C CD1 . LEU B 1 288 ? 0.719   -6.872  18.097  1.00 49.85  ? 297  LEU B CD1 1 
ATOM   5162  C CD2 . LEU B 1 288 ? 3.193   -7.069  18.217  1.00 46.95  ? 297  LEU B CD2 1 
ATOM   5163  N N   . ALA B 1 289 ? -0.454  -10.099 18.235  1.00 52.91  ? 298  ALA B N   1 
ATOM   5164  C CA  . ALA B 1 289 ? -0.537  -11.098 17.216  1.00 53.56  ? 298  ALA B CA  1 
ATOM   5165  C C   . ALA B 1 289 ? -0.718  -10.397 15.933  1.00 51.85  ? 298  ALA B C   1 
ATOM   5166  O O   . ALA B 1 289 ? -1.485  -9.456  15.866  1.00 51.18  ? 298  ALA B O   1 
ATOM   5167  C CB  . ALA B 1 289 ? -1.709  -11.959 17.456  1.00 56.53  ? 298  ALA B CB  1 
ATOM   5168  N N   . TYR B 1 290 ? -0.035  -10.881 14.907  1.00 51.33  ? 299  TYR B N   1 
ATOM   5169  C CA  . TYR B 1 290 ? -0.087  -10.296 13.572  1.00 49.43  ? 299  TYR B CA  1 
ATOM   5170  C C   . TYR B 1 290 ? 0.041   -11.370 12.503  1.00 50.85  ? 299  TYR B C   1 
ATOM   5171  O O   . TYR B 1 290 ? 0.517   -12.489 12.755  1.00 52.75  ? 299  TYR B O   1 
ATOM   5172  C CB  . TYR B 1 290 ? 1.042   -9.309  13.414  1.00 46.68  ? 299  TYR B CB  1 
ATOM   5173  C CG  . TYR B 1 290 ? 2.389   -9.909  13.742  1.00 47.07  ? 299  TYR B CG  1 
ATOM   5174  C CD1 . TYR B 1 290 ? 3.242   -10.357 12.718  1.00 47.58  ? 299  TYR B CD1 1 
ATOM   5175  C CD2 . TYR B 1 290 ? 2.827   -10.036 15.073  1.00 46.78  ? 299  TYR B CD2 1 
ATOM   5176  C CE1 . TYR B 1 290 ? 4.505   -10.916 13.006  1.00 47.40  ? 299  TYR B CE1 1 
ATOM   5177  C CE2 . TYR B 1 290 ? 4.086   -10.594 15.366  1.00 46.75  ? 299  TYR B CE2 1 
ATOM   5178  C CZ  . TYR B 1 290 ? 4.914   -11.032 14.326  1.00 46.82  ? 299  TYR B CZ  1 
ATOM   5179  O OH  . TYR B 1 290 ? 6.151   -11.576 14.585  1.00 46.18  ? 299  TYR B OH  1 
ATOM   5180  N N   . VAL B 1 291 ? -0.380  -11.026 11.298  1.00 50.07  ? 300  VAL B N   1 
ATOM   5181  C CA  . VAL B 1 291 ? -0.374  -11.988 10.226  1.00 51.43  ? 300  VAL B CA  1 
ATOM   5182  C C   . VAL B 1 291 ? 0.711   -11.678 9.263   1.00 50.18  ? 300  VAL B C   1 
ATOM   5183  O O   . VAL B 1 291 ? 0.791   -10.578 8.737   1.00 48.54  ? 300  VAL B O   1 
ATOM   5184  C CB  . VAL B 1 291 ? -1.690  -12.011 9.487   1.00 52.27  ? 300  VAL B CB  1 
ATOM   5185  C CG1 . VAL B 1 291 ? -1.545  -12.680 8.130   1.00 53.31  ? 300  VAL B CG1 1 
ATOM   5186  C CG2 . VAL B 1 291 ? -2.675  -12.767 10.311  1.00 55.38  ? 300  VAL B CG2 1 
ATOM   5187  N N   . VAL B 1 292 ? 1.555   -12.666 9.042   1.00 51.51  ? 301  VAL B N   1 
ATOM   5188  C CA  . VAL B 1 292 ? 2.568   -12.590 8.022   1.00 50.75  ? 301  VAL B CA  1 
ATOM   5189  C C   . VAL B 1 292 ? 2.037   -13.092 6.689   1.00 52.05  ? 301  VAL B C   1 
ATOM   5190  O O   . VAL B 1 292 ? 1.224   -14.004 6.633   1.00 54.92  ? 301  VAL B O   1 
ATOM   5191  C CB  . VAL B 1 292 ? 3.752   -13.385 8.458   1.00 51.39  ? 301  VAL B CB  1 
ATOM   5192  C CG1 . VAL B 1 292 ? 4.432   -13.978 7.266   1.00 53.36  ? 301  VAL B CG1 1 
ATOM   5193  C CG2 . VAL B 1 292 ? 4.673   -12.473 9.230   1.00 49.39  ? 301  VAL B CG2 1 
ATOM   5194  N N   . GLN B 1 293 ? 2.502   -12.497 5.615   1.00 50.38  ? 302  GLN B N   1 
ATOM   5195  C CA  . GLN B 1 293 ? 1.938   -12.797 4.342   1.00 51.29  ? 302  GLN B CA  1 
ATOM   5196  C C   . GLN B 1 293 ? 3.016   -13.087 3.328   1.00 50.94  ? 302  GLN B C   1 
ATOM   5197  O O   . GLN B 1 293 ? 3.744   -12.192 2.911   1.00 48.93  ? 302  GLN B O   1 
ATOM   5198  C CB  . GLN B 1 293 ? 1.087   -11.634 3.902   1.00 49.89  ? 302  GLN B CB  1 
ATOM   5199  C CG  . GLN B 1 293 ? 0.618   -11.747 2.477   1.00 52.80  ? 302  GLN B CG  1 
ATOM   5200  C CD  . GLN B 1 293 ? -0.548  -10.832 2.183   1.00 54.83  ? 302  GLN B CD  1 
ATOM   5201  O OE1 . GLN B 1 293 ? -1.327  -10.505 3.077   1.00 55.09  ? 302  GLN B OE1 1 
ATOM   5202  N NE2 . GLN B 1 293 ? -0.683  -10.418 0.923   1.00 55.50  ? 302  GLN B NE2 1 
ATOM   5203  N N   . LEU B 1 294 ? 3.095   -14.346 2.922   1.00 52.86  ? 303  LEU B N   1 
ATOM   5204  C CA  . LEU B 1 294 ? 4.215   -14.818 2.139   1.00 53.20  ? 303  LEU B CA  1 
ATOM   5205  C C   . LEU B 1 294 ? 3.776   -15.094 0.732   1.00 54.40  ? 303  LEU B C   1 
ATOM   5206  O O   . LEU B 1 294 ? 2.604   -15.424 0.524   1.00 55.92  ? 303  LEU B O   1 
ATOM   5207  C CB  . LEU B 1 294 ? 4.802   -16.081 2.757   1.00 55.18  ? 303  LEU B CB  1 
ATOM   5208  C CG  . LEU B 1 294 ? 5.293   -15.892 4.193   1.00 53.97  ? 303  LEU B CG  1 
ATOM   5209  C CD1 . LEU B 1 294 ? 6.182   -17.009 4.635   1.00 55.53  ? 303  LEU B CD1 1 
ATOM   5210  C CD2 . LEU B 1 294 ? 6.056   -14.623 4.308   1.00 51.69  ? 303  LEU B CD2 1 
ATOM   5211  N N   . PRO B 1 295 ? 4.707   -14.952 -0.243  1.00 53.95  ? 304  PRO B N   1 
ATOM   5212  C CA  . PRO B 1 295 ? 4.369   -15.194 -1.642  1.00 55.04  ? 304  PRO B CA  1 
ATOM   5213  C C   . PRO B 1 295 ? 4.341   -16.681 -1.973  1.00 58.47  ? 304  PRO B C   1 
ATOM   5214  O O   . PRO B 1 295 ? 5.028   -17.476 -1.327  1.00 59.97  ? 304  PRO B O   1 
ATOM   5215  C CB  . PRO B 1 295 ? 5.500   -14.500 -2.400  1.00 53.30  ? 304  PRO B CB  1 
ATOM   5216  C CG  . PRO B 1 295 ? 6.645   -14.533 -1.482  1.00 52.95  ? 304  PRO B CG  1 
ATOM   5217  C CD  . PRO B 1 295 ? 6.094   -14.474 -0.092  1.00 52.33  ? 304  PRO B CD  1 
ATOM   5218  N N   . LEU B 1 296 ? 3.534   -17.043 -2.964  1.00 60.01  ? 305  LEU B N   1 
ATOM   5219  C CA  . LEU B 1 296 ? 3.508   -18.400 -3.490  1.00 63.20  ? 305  LEU B CA  1 
ATOM   5220  C C   . LEU B 1 296 ? 3.624   -18.332 -4.992  1.00 63.70  ? 305  LEU B C   1 
ATOM   5221  O O   . LEU B 1 296 ? 2.836   -17.629 -5.643  1.00 62.62  ? 305  LEU B O   1 
ATOM   5222  C CB  . LEU B 1 296 ? 2.202   -19.099 -3.124  1.00 65.05  ? 305  LEU B CB  1 
ATOM   5223  C CG  . LEU B 1 296 ? 1.874   -19.315 -1.647  1.00 65.36  ? 305  LEU B CG  1 
ATOM   5224  C CD1 . LEU B 1 296 ? 0.555   -20.036 -1.549  1.00 67.70  ? 305  LEU B CD1 1 
ATOM   5225  C CD2 . LEU B 1 296 ? 2.954   -20.114 -0.950  1.00 67.76  ? 305  LEU B CD2 1 
ATOM   5226  N N   . TYR B 1 297 ? 4.596   -19.066 -5.534  1.00 65.43  ? 306  TYR B N   1 
ATOM   5227  C CA  . TYR B 1 297 ? 4.834   -19.092 -6.980  1.00 66.14  ? 306  TYR B CA  1 
ATOM   5228  C C   . TYR B 1 297 ? 4.137   -20.228 -7.682  1.00 69.28  ? 306  TYR B C   1 
ATOM   5229  O O   . TYR B 1 297 ? 4.222   -21.370 -7.267  1.00 71.81  ? 306  TYR B O   1 
ATOM   5230  C CB  . TYR B 1 297 ? 6.319   -19.150 -7.289  1.00 66.23  ? 306  TYR B CB  1 
ATOM   5231  C CG  . TYR B 1 297 ? 7.069   -18.174 -6.471  1.00 64.22  ? 306  TYR B CG  1 
ATOM   5232  C CD1 . TYR B 1 297 ? 7.792   -18.593 -5.366  1.00 65.53  ? 306  TYR B CD1 1 
ATOM   5233  C CD2 . TYR B 1 297 ? 7.008   -16.810 -6.758  1.00 63.06  ? 306  TYR B CD2 1 
ATOM   5234  C CE1 . TYR B 1 297 ? 8.477   -17.673 -4.575  1.00 63.75  ? 306  TYR B CE1 1 
ATOM   5235  C CE2 . TYR B 1 297 ? 7.686   -15.873 -5.976  1.00 61.73  ? 306  TYR B CE2 1 
ATOM   5236  C CZ  . TYR B 1 297 ? 8.423   -16.313 -4.880  1.00 61.23  ? 306  TYR B CZ  1 
ATOM   5237  O OH  . TYR B 1 297 ? 9.096   -15.412 -4.080  1.00 56.71  ? 306  TYR B OH  1 
ATOM   5238  N N   . GLY B 1 298 ? 3.449   -19.909 -8.763  1.00 69.19  ? 307  GLY B N   1 
ATOM   5239  C CA  . GLY B 1 298 ? 2.757   -20.922 -9.498  1.00 72.08  ? 307  GLY B CA  1 
ATOM   5240  C C   . GLY B 1 298 ? 3.630   -21.511 -10.566 1.00 73.97  ? 307  GLY B C   1 
ATOM   5241  O O   . GLY B 1 298 ? 3.192   -22.423 -11.260 1.00 77.10  ? 307  GLY B O   1 
ATOM   5242  N N   . VAL B 1 299 ? 4.842   -20.980 -10.723 1.00 72.56  ? 308  VAL B N   1 
ATOM   5243  C CA  . VAL B 1 299 ? 5.809   -21.513 -11.700 1.00 74.66  ? 308  VAL B CA  1 
ATOM   5244  C C   . VAL B 1 299 ? 7.230   -21.147 -11.381 1.00 74.10  ? 308  VAL B C   1 
ATOM   5245  O O   . VAL B 1 299 ? 7.516   -20.008 -11.022 1.00 71.31  ? 308  VAL B O   1 
ATOM   5246  C CB  . VAL B 1 299 ? 5.608   -20.978 -13.125 1.00 73.60  ? 308  VAL B CB  1 
ATOM   5247  C CG1 . VAL B 1 299 ? 4.781   -21.934 -13.954 1.00 76.56  ? 308  VAL B CG1 1 
ATOM   5248  C CG2 . VAL B 1 299 ? 5.033   -19.599 -13.086 1.00 70.10  ? 308  VAL B CG2 1 
ATOM   5249  N N   . ILE B 1 300 ? 8.121   -22.109 -11.584 1.00 77.32  ? 309  ILE B N   1 
ATOM   5250  C CA  . ILE B 1 300 ? 9.533   -21.942 -11.301 1.00 77.51  ? 309  ILE B CA  1 
ATOM   5251  C C   . ILE B 1 300 ? 10.313  -22.322 -12.540 1.00 79.78  ? 309  ILE B C   1 
ATOM   5252  O O   . ILE B 1 300 ? 9.825   -23.130 -13.334 1.00 82.87  ? 309  ILE B O   1 
ATOM   5253  C CB  . ILE B 1 300 ? 9.937   -22.887 -10.160 1.00 79.34  ? 309  ILE B CB  1 
ATOM   5254  C CG1 . ILE B 1 300 ? 9.057   -22.634 -8.948  1.00 78.92  ? 309  ILE B CG1 1 
ATOM   5255  C CG2 . ILE B 1 300 ? 11.365  -22.674 -9.748  1.00 78.49  ? 309  ILE B CG2 1 
ATOM   5256  C CD1 . ILE B 1 300 ? 9.071   -21.173 -8.506  1.00 77.04  ? 309  ILE B CD1 1 
ATOM   5257  N N   . ASP B 1 301 ? 11.506  -21.749 -12.716 1.00 78.88  ? 310  ASP B N   1 
ATOM   5258  C CA  . ASP B 1 301 ? 12.491  -22.302 -13.662 1.00 81.44  ? 310  ASP B CA  1 
ATOM   5259  C C   . ASP B 1 301 ? 12.114  -22.156 -15.155 1.00 82.23  ? 310  ASP B C   1 
ATOM   5260  O O   . ASP B 1 301 ? 12.601  -22.915 -16.024 1.00 85.04  ? 310  ASP B O   1 
ATOM   5261  C CB  . ASP B 1 301 ? 12.777  -23.786 -13.335 1.00 85.19  ? 310  ASP B CB  1 
ATOM   5262  C CG  . ASP B 1 301 ? 13.318  -23.991 -11.931 1.00 85.35  ? 310  ASP B CG  1 
ATOM   5263  O OD1 . ASP B 1 301 ? 12.849  -24.919 -11.240 1.00 87.32  ? 310  ASP B OD1 1 
ATOM   5264  O OD2 . ASP B 1 301 ? 14.211  -23.228 -11.516 1.00 83.81  ? 310  ASP B OD2 1 
ATOM   5265  N N   . THR B 1 302 ? 11.240  -21.195 -15.443 1.00 79.85  ? 311  THR B N   1 
ATOM   5266  C CA  . THR B 1 302 ? 10.958  -20.806 -16.812 1.00 80.12  ? 311  THR B CA  1 
ATOM   5267  C C   . THR B 1 302 ? 11.982  -19.773 -17.200 1.00 78.44  ? 311  THR B C   1 
ATOM   5268  O O   . THR B 1 302 ? 12.384  -18.980 -16.360 1.00 76.50  ? 311  THR B O   1 
ATOM   5269  C CB  . THR B 1 302 ? 9.645   -20.084 -16.909 1.00 77.85  ? 311  THR B CB  1 
ATOM   5270  O OG1 . THR B 1 302 ? 8.780   -20.547 -15.872 1.00 78.42  ? 311  THR B OG1 1 
ATOM   5271  C CG2 . THR B 1 302 ? 9.027   -20.336 -18.246 1.00 81.04  ? 311  THR B CG2 1 
ATOM   5272  N N   . PRO B 1 303 ? 12.402  -19.760 -18.474 1.00 79.63  ? 312  PRO B N   1 
ATOM   5273  C CA  . PRO B 1 303 ? 13.351  -18.717 -18.800 1.00 77.92  ? 312  PRO B CA  1 
ATOM   5274  C C   . PRO B 1 303 ? 12.674  -17.350 -18.744 1.00 74.88  ? 312  PRO B C   1 
ATOM   5275  O O   . PRO B 1 303 ? 11.484  -17.246 -19.048 1.00 74.54  ? 312  PRO B O   1 
ATOM   5276  C CB  . PRO B 1 303 ? 13.740  -19.056 -20.233 1.00 79.81  ? 312  PRO B CB  1 
ATOM   5277  C CG  . PRO B 1 303 ? 12.567  -19.806 -20.777 1.00 81.11  ? 312  PRO B CG  1 
ATOM   5278  C CD  . PRO B 1 303 ? 12.067  -20.601 -19.641 1.00 82.26  ? 312  PRO B CD  1 
ATOM   5279  N N   . CYS B 1 304 ? 13.410  -16.329 -18.311 1.00 72.89  ? 313  CYS B N   1 
ATOM   5280  C CA  . CYS B 1 304 ? 13.002  -14.937 -18.540 1.00 70.34  ? 313  CYS B CA  1 
ATOM   5281  C C   . CYS B 1 304 ? 14.095  -14.157 -19.219 1.00 69.33  ? 313  CYS B C   1 
ATOM   5282  O O   . CYS B 1 304 ? 15.247  -14.587 -19.278 1.00 70.78  ? 313  CYS B O   1 
ATOM   5283  C CB  . CYS B 1 304 ? 12.701  -14.179 -17.254 1.00 68.22  ? 313  CYS B CB  1 
ATOM   5284  S SG  . CYS B 1 304 ? 11.853  -15.024 -15.909 1.00 71.25  ? 313  CYS B SG  1 
ATOM   5285  N N   . TRP B 1 305 ? 13.735  -12.974 -19.687 1.00 66.94  ? 314  TRP B N   1 
ATOM   5286  C CA  . TRP B 1 305 ? 14.704  -12.088 -20.289 1.00 66.18  ? 314  TRP B CA  1 
ATOM   5287  C C   . TRP B 1 305 ? 14.335  -10.631 -20.074 1.00 62.77  ? 314  TRP B C   1 
ATOM   5288  O O   . TRP B 1 305 ? 13.155  -10.307 -19.949 1.00 61.79  ? 314  TRP B O   1 
ATOM   5289  C CB  . TRP B 1 305 ? 14.825  -12.387 -21.776 1.00 68.20  ? 314  TRP B CB  1 
ATOM   5290  C CG  . TRP B 1 305 ? 13.542  -12.383 -22.534 1.00 69.17  ? 314  TRP B CG  1 
ATOM   5291  C CD1 . TRP B 1 305 ? 13.050  -11.367 -23.302 1.00 68.81  ? 314  TRP B CD1 1 
ATOM   5292  C CD2 . TRP B 1 305 ? 12.601  -13.458 -22.638 1.00 72.27  ? 314  TRP B CD2 1 
ATOM   5293  N NE1 . TRP B 1 305 ? 11.853  -11.733 -23.871 1.00 70.05  ? 314  TRP B NE1 1 
ATOM   5294  C CE2 . TRP B 1 305 ? 11.555  -13.015 -23.484 1.00 72.02  ? 314  TRP B CE2 1 
ATOM   5295  C CE3 . TRP B 1 305 ? 12.544  -14.762 -22.110 1.00 75.70  ? 314  TRP B CE3 1 
ATOM   5296  C CZ2 . TRP B 1 305 ? 10.449  -13.831 -23.806 1.00 74.38  ? 314  TRP B CZ2 1 
ATOM   5297  C CZ3 . TRP B 1 305 ? 11.447  -15.576 -22.432 1.00 78.44  ? 314  TRP B CZ3 1 
ATOM   5298  C CH2 . TRP B 1 305 ? 10.415  -15.104 -23.271 1.00 77.72  ? 314  TRP B CH2 1 
ATOM   5299  N N   . LYS B 1 306 ? 15.333  -9.753  -20.022 1.00 61.10  ? 315  LYS B N   1 
ATOM   5300  C CA  . LYS B 1 306 ? 15.054  -8.336  -19.906 1.00 58.15  ? 315  LYS B CA  1 
ATOM   5301  C C   . LYS B 1 306 ? 15.393  -7.617  -21.181 1.00 58.20  ? 315  LYS B C   1 
ATOM   5302  O O   . LYS B 1 306 ? 16.462  -7.796  -21.745 1.00 59.69  ? 315  LYS B O   1 
ATOM   5303  C CB  . LYS B 1 306 ? 15.817  -7.714  -18.752 1.00 56.66  ? 315  LYS B CB  1 
ATOM   5304  C CG  . LYS B 1 306 ? 15.270  -6.356  -18.327 1.00 53.96  ? 315  LYS B CG  1 
ATOM   5305  C CD  . LYS B 1 306 ? 16.123  -5.721  -17.243 1.00 53.86  ? 315  LYS B CD  1 
ATOM   5306  C CE  . LYS B 1 306 ? 15.389  -4.589  -16.568 1.00 52.09  ? 315  LYS B CE  1 
ATOM   5307  N NZ  . LYS B 1 306 ? 16.366  -3.665  -15.966 1.00 52.34  ? 315  LYS B NZ  1 
ATOM   5308  N N   . LEU B 1 307 ? 14.464  -6.787  -21.617 1.00 56.89  ? 316  LEU B N   1 
ATOM   5309  C CA  . LEU B 1 307 ? 14.587  -6.066  -22.859 1.00 57.26  ? 316  LEU B CA  1 
ATOM   5310  C C   . LEU B 1 307 ? 14.943  -4.617  -22.591 1.00 55.77  ? 316  LEU B C   1 
ATOM   5311  O O   . LEU B 1 307 ? 14.303  -3.937  -21.763 1.00 54.45  ? 316  LEU B O   1 
ATOM   5312  C CB  . LEU B 1 307 ? 13.264  -6.154  -23.633 1.00 57.12  ? 316  LEU B CB  1 
ATOM   5313  C CG  . LEU B 1 307 ? 13.050  -5.334  -24.915 1.00 56.43  ? 316  LEU B CG  1 
ATOM   5314  C CD1 . LEU B 1 307 ? 14.087  -5.682  -25.955 1.00 58.15  ? 316  LEU B CD1 1 
ATOM   5315  C CD2 . LEU B 1 307 ? 11.634  -5.532  -25.479 1.00 56.47  ? 316  LEU B CD2 1 
ATOM   5316  N N   . HIS B 1 308 ? 15.965  -4.138  -23.284 1.00 56.61  ? 317  HIS B N   1 
ATOM   5317  C CA  . HIS B 1 308 ? 16.262  -2.705  -23.256 1.00 55.44  ? 317  HIS B CA  1 
ATOM   5318  C C   . HIS B 1 308 ? 16.182  -2.206  -24.670 1.00 55.33  ? 317  HIS B C   1 
ATOM   5319  O O   . HIS B 1 308 ? 16.206  -2.992  -25.592 1.00 57.20  ? 317  HIS B O   1 
ATOM   5320  C CB  . HIS B 1 308 ? 17.637  -2.402  -22.665 1.00 56.07  ? 317  HIS B CB  1 
ATOM   5321  C CG  . HIS B 1 308 ? 18.003  -3.268  -21.497 1.00 58.92  ? 317  HIS B CG  1 
ATOM   5322  N ND1 . HIS B 1 308 ? 17.853  -2.857  -20.188 1.00 59.79  ? 317  HIS B ND1 1 
ATOM   5323  C CD2 . HIS B 1 308 ? 18.509  -4.524  -21.443 1.00 62.21  ? 317  HIS B CD2 1 
ATOM   5324  C CE1 . HIS B 1 308 ? 18.249  -3.826  -19.379 1.00 61.59  ? 317  HIS B CE1 1 
ATOM   5325  N NE2 . HIS B 1 308 ? 18.656  -4.845  -20.117 1.00 63.03  ? 317  HIS B NE2 1 
ATOM   5326  N N   . THR B 1 309 ? 16.126  -0.898  -24.844 1.00 53.37  ? 318  THR B N   1 
ATOM   5327  C CA  . THR B 1 309 ? 15.568  -0.368  -26.051 1.00 52.84  ? 318  THR B CA  1 
ATOM   5328  C C   . THR B 1 309 ? 16.121  1.014   -26.271 1.00 51.89  ? 318  THR B C   1 
ATOM   5329  O O   . THR B 1 309 ? 16.141  1.815   -25.347 1.00 50.59  ? 318  THR B O   1 
ATOM   5330  C CB  . THR B 1 309 ? 14.054  -0.344  -25.859 1.00 51.56  ? 318  THR B CB  1 
ATOM   5331  O OG1 . THR B 1 309 ? 13.456  -1.294  -26.736 1.00 53.05  ? 318  THR B OG1 1 
ATOM   5332  C CG2 . THR B 1 309 ? 13.472  1.026   -26.104 1.00 50.20  ? 318  THR B CG2 1 
ATOM   5333  N N   . SER B 1 310 ? 16.583  1.306   -27.475 1.00 53.01  ? 319  SER B N   1 
ATOM   5334  C CA  . SER B 1 310 ? 17.086  2.643   -27.759 1.00 52.63  ? 319  SER B CA  1 
ATOM   5335  C C   . SER B 1 310 ? 16.666  3.105   -29.127 1.00 53.80  ? 319  SER B C   1 
ATOM   5336  O O   . SER B 1 310 ? 16.459  2.281   -29.993 1.00 56.03  ? 319  SER B O   1 
ATOM   5337  C CB  . SER B 1 310 ? 18.587  2.673   -27.683 1.00 53.42  ? 319  SER B CB  1 
ATOM   5338  O OG  . SER B 1 310 ? 19.024  3.995   -27.875 1.00 52.27  ? 319  SER B OG  1 
ATOM   5339  N N   . PRO B 1 311 ? 16.558  4.423   -29.344 1.00 53.03  ? 320  PRO B N   1 
ATOM   5340  C CA  . PRO B 1 311 ? 16.128  4.976   -30.614 1.00 53.95  ? 320  PRO B CA  1 
ATOM   5341  C C   . PRO B 1 311 ? 16.981  4.513   -31.812 1.00 57.06  ? 320  PRO B C   1 
ATOM   5342  O O   . PRO B 1 311 ? 18.153  4.184   -31.662 1.00 57.67  ? 320  PRO B O   1 
ATOM   5343  C CB  . PRO B 1 311 ? 16.248  6.489   -30.404 1.00 52.09  ? 320  PRO B CB  1 
ATOM   5344  C CG  . PRO B 1 311 ? 17.196  6.610   -29.342 1.00 51.75  ? 320  PRO B CG  1 
ATOM   5345  C CD  . PRO B 1 311 ? 16.866  5.499   -28.411 1.00 51.69  ? 320  PRO B CD  1 
ATOM   5346  N N   . LEU B 1 312 ? 16.348  4.514   -32.988 1.00 59.11  ? 321  LEU B N   1 
ATOM   5347  C CA  . LEU B 1 312 ? 16.874  3.973   -34.225 1.00 62.68  ? 321  LEU B CA  1 
ATOM   5348  C C   . LEU B 1 312 ? 16.428  4.873   -35.369 1.00 64.16  ? 321  LEU B C   1 
ATOM   5349  O O   . LEU B 1 312 ? 15.251  4.922   -35.690 1.00 63.73  ? 321  LEU B O   1 
ATOM   5350  C CB  . LEU B 1 312 ? 16.251  2.605   -34.425 1.00 63.18  ? 321  LEU B CB  1 
ATOM   5351  C CG  . LEU B 1 312 ? 17.067  1.547   -35.126 1.00 65.46  ? 321  LEU B CG  1 
ATOM   5352  C CD1 . LEU B 1 312 ? 16.113  0.539   -35.708 1.00 65.50  ? 321  LEU B CD1 1 
ATOM   5353  C CD2 . LEU B 1 312 ? 17.918  2.165   -36.193 1.00 66.81  ? 321  LEU B CD2 1 
ATOM   5354  N N   . CYS B 1 313 ? 17.345  5.605   -35.973 1.00 67.36  ? 322  CYS B N   1 
ATOM   5355  C CA  . CYS B 1 313 ? 16.932  6.511   -37.026 1.00 70.48  ? 322  CYS B CA  1 
ATOM   5356  C C   . CYS B 1 313 ? 17.474  6.018   -38.346 1.00 74.93  ? 322  CYS B C   1 
ATOM   5357  O O   . CYS B 1 313 ? 18.345  5.150   -38.367 1.00 76.83  ? 322  CYS B O   1 
ATOM   5358  C CB  . CYS B 1 313 ? 17.372  7.953   -36.763 1.00 69.60  ? 322  CYS B CB  1 
ATOM   5359  S SG  . CYS B 1 313 ? 16.876  8.660   -35.150 1.00 68.72  ? 322  CYS B SG  1 
ATOM   5360  N N   . THR B 1 314 ? 16.950  6.583   -39.438 1.00 77.86  ? 323  THR B N   1 
ATOM   5361  C CA  . THR B 1 314 ? 17.221  6.132   -40.808 1.00 82.31  ? 323  THR B CA  1 
ATOM   5362  C C   . THR B 1 314 ? 17.753  7.292   -41.685 1.00 85.13  ? 323  THR B C   1 
ATOM   5363  O O   . THR B 1 314 ? 18.000  8.392   -41.154 1.00 84.43  ? 323  THR B O   1 
ATOM   5364  C CB  . THR B 1 314 ? 15.956  5.554   -41.451 1.00 82.01  ? 323  THR B CB  1 
ATOM   5365  O OG1 . THR B 1 314 ? 14.992  6.604   -41.549 1.00 80.77  ? 323  THR B OG1 1 
ATOM   5366  C CG2 . THR B 1 314 ? 15.387  4.376   -40.629 1.00 80.70  ? 323  THR B CG2 1 
ATOM   5367  N N   . THR B 1 315 ? 17.881  7.046   -43.011 1.00 89.47  ? 324  THR B N   1 
ATOM   5368  C CA  . THR B 1 315 ? 18.735  7.853   -43.964 1.00 92.82  ? 324  THR B CA  1 
ATOM   5369  C C   . THR B 1 315 ? 18.134  8.419   -45.306 1.00 94.60  ? 324  THR B C   1 
ATOM   5370  O O   . THR B 1 315 ? 18.043  9.651   -45.446 1.00 94.28  ? 324  THR B O   1 
ATOM   5371  C CB  . THR B 1 315 ? 20.125  7.140   -44.254 1.00 95.29  ? 324  THR B CB  1 
ATOM   5372  O OG1 . THR B 1 315 ? 20.805  6.896   -43.012 1.00 95.27  ? 324  THR B OG1 1 
ATOM   5373  C CG2 . THR B 1 315 ? 21.045  7.974   -45.207 1.00 96.32  ? 324  THR B CG2 1 
ATOM   5374  N N   . ASN B 1 316 ? 17.750  7.540   -46.258 1.00 97.14  ? 325  ASN B N   1 
ATOM   5375  C CA  . ASN B 1 316 ? 17.466  7.899   -47.705 1.00 99.11  ? 325  ASN B CA  1 
ATOM   5376  C C   . ASN B 1 316 ? 16.122  8.577   -48.080 1.00 97.57  ? 325  ASN B C   1 
ATOM   5377  O O   . ASN B 1 316 ? 15.208  7.953   -48.643 1.00 97.54  ? 325  ASN B O   1 
ATOM   5378  C CB  . ASN B 1 316 ? 17.717  6.699   -48.660 1.00 101.80 ? 325  ASN B CB  1 
ATOM   5379  C CG  . ASN B 1 316 ? 19.198  6.266   -48.727 1.00 105.05 ? 325  ASN B CG  1 
ATOM   5380  O OD1 . ASN B 1 316 ? 19.596  5.585   -49.678 1.00 108.71 ? 325  ASN B OD1 1 
ATOM   5381  N ND2 . ASN B 1 316 ? 20.009  6.647   -47.719 1.00 104.33 ? 325  ASN B ND2 1 
ATOM   5382  N N   . SER B 1 321 ? 14.823  8.670   -45.438 1.00 90.73  ? 330  SER B N   1 
ATOM   5383  C CA  . SER B 1 321 ? 14.950  10.051  -44.938 1.00 89.41  ? 330  SER B CA  1 
ATOM   5384  C C   . SER B 1 321 ? 13.855  10.479  -43.925 1.00 87.09  ? 330  SER B C   1 
ATOM   5385  O O   . SER B 1 321 ? 12.672  10.703  -44.304 1.00 86.12  ? 330  SER B O   1 
ATOM   5386  C CB  . SER B 1 321 ? 15.105  11.082  -46.094 1.00 90.47  ? 330  SER B CB  1 
ATOM   5387  O OG  . SER B 1 321 ? 14.523  10.667  -47.337 1.00 91.31  ? 330  SER B OG  1 
ATOM   5388  N N   . ASN B 1 322 ? 14.272  10.537  -42.644 1.00 85.67  ? 331  ASN B N   1 
ATOM   5389  C CA  . ASN B 1 322 ? 13.546  11.205  -41.504 1.00 83.06  ? 331  ASN B CA  1 
ATOM   5390  C C   . ASN B 1 322 ? 12.492  10.443  -40.676 1.00 80.08  ? 331  ASN B C   1 
ATOM   5391  O O   . ASN B 1 322 ? 11.356  10.936  -40.468 1.00 78.69  ? 331  ASN B O   1 
ATOM   5392  C CB  . ASN B 1 322 ? 12.973  12.603  -41.888 1.00 83.51  ? 331  ASN B CB  1 
ATOM   5393  C CG  . ASN B 1 322 ? 13.988  13.754  -41.695 1.00 85.92  ? 331  ASN B CG  1 
ATOM   5394  O OD1 . ASN B 1 322 ? 14.584  13.927  -40.607 1.00 86.92  ? 331  ASN B OD1 1 
ATOM   5395  N ND2 . ASN B 1 322 ? 14.172  14.556  -42.763 1.00 89.35  ? 331  ASN B ND2 1 
ATOM   5396  N N   . ILE B 1 323 ? 12.877  9.268   -40.181 1.00 78.10  ? 332  ILE B N   1 
ATOM   5397  C CA  . ILE B 1 323 ? 12.041  8.570   -39.215 1.00 74.53  ? 332  ILE B CA  1 
ATOM   5398  C C   . ILE B 1 323 ? 12.889  7.955   -38.099 1.00 72.92  ? 332  ILE B C   1 
ATOM   5399  O O   . ILE B 1 323 ? 13.927  7.341   -38.379 1.00 74.09  ? 332  ILE B O   1 
ATOM   5400  C CB  . ILE B 1 323 ? 11.096  7.540   -39.895 1.00 75.18  ? 332  ILE B CB  1 
ATOM   5401  C CG1 . ILE B 1 323 ? 9.659   7.690   -39.360 1.00 73.40  ? 332  ILE B CG1 1 
ATOM   5402  C CG2 . ILE B 1 323 ? 11.638  6.124   -39.777 1.00 75.78  ? 332  ILE B CG2 1 
ATOM   5403  C CD1 . ILE B 1 323 ? 8.814   8.774   -40.069 1.00 72.09  ? 332  ILE B CD1 1 
ATOM   5404  N N   . CYS B 1 324 ? 12.457  8.170   -36.846 1.00 69.20  ? 333  CYS B N   1 
ATOM   5405  C CA  . CYS B 1 324 ? 13.097  7.583   -35.657 1.00 66.83  ? 333  CYS B CA  1 
ATOM   5406  C C   . CYS B 1 324 ? 12.130  6.732   -34.871 1.00 63.83  ? 333  CYS B C   1 
ATOM   5407  O O   . CYS B 1 324 ? 11.001  7.155   -34.579 1.00 62.29  ? 333  CYS B O   1 
ATOM   5408  C CB  . CYS B 1 324 ? 13.731  8.639   -34.737 1.00 65.90  ? 333  CYS B CB  1 
ATOM   5409  S SG  . CYS B 1 324 ? 15.125  9.675   -35.455 1.00 70.76  ? 333  CYS B SG  1 
ATOM   5410  N N   . LEU B 1 325 ? 12.613  5.535   -34.533 1.00 62.31  ? 334  LEU B N   1 
ATOM   5411  C CA  . LEU B 1 325 ? 11.858  4.470   -33.858 1.00 61.03  ? 334  LEU B CA  1 
ATOM   5412  C C   . LEU B 1 325 ? 12.384  4.141   -32.466 1.00 59.81  ? 334  LEU B C   1 
ATOM   5413  O O   . LEU B 1 325 ? 13.578  3.847   -32.325 1.00 60.77  ? 334  LEU B O   1 
ATOM   5414  C CB  . LEU B 1 325 ? 11.989  3.177   -34.658 1.00 62.58  ? 334  LEU B CB  1 
ATOM   5415  C CG  . LEU B 1 325 ? 11.128  3.028   -35.890 1.00 63.73  ? 334  LEU B CG  1 
ATOM   5416  C CD1 . LEU B 1 325 ? 10.837  1.556   -36.056 1.00 64.91  ? 334  LEU B CD1 1 
ATOM   5417  C CD2 . LEU B 1 325 ? 9.828   3.821   -35.718 1.00 63.59  ? 334  LEU B CD2 1 
ATOM   5418  N N   . THR B 1 326 ? 11.531  4.135   -31.445 1.00 57.43  ? 335  THR B N   1 
ATOM   5419  C CA  . THR B 1 326 ? 11.986  3.575   -30.197 1.00 56.39  ? 335  THR B CA  1 
ATOM   5420  C C   . THR B 1 326 ? 10.973  2.553   -29.852 1.00 56.29  ? 335  THR B C   1 
ATOM   5421  O O   . THR B 1 326 ? 9.781   2.796   -29.958 1.00 55.68  ? 335  THR B O   1 
ATOM   5422  C CB  . THR B 1 326 ? 12.141  4.629   -29.104 1.00 54.54  ? 335  THR B CB  1 
ATOM   5423  O OG1 . THR B 1 326 ? 12.825  5.760   -29.640 1.00 54.38  ? 335  THR B OG1 1 
ATOM   5424  C CG2 . THR B 1 326 ? 12.981  4.103   -27.969 1.00 54.70  ? 335  THR B CG2 1 
ATOM   5425  N N   . ARG B 1 327 ? 11.452  1.381   -29.499 1.00 57.19  ? 336  ARG B N   1 
ATOM   5426  C CA  . ARG B 1 327 ? 10.561  0.324   -29.137 1.00 58.05  ? 336  ARG B CA  1 
ATOM   5427  C C   . ARG B 1 327 ? 9.999   0.568   -27.710 1.00 56.82  ? 336  ARG B C   1 
ATOM   5428  O O   . ARG B 1 327 ? 10.752  0.731   -26.779 1.00 56.13  ? 336  ARG B O   1 
ATOM   5429  C CB  . ARG B 1 327 ? 11.322  -0.979  -29.269 1.00 59.71  ? 336  ARG B CB  1 
ATOM   5430  C CG  . ARG B 1 327 ? 10.431  -2.112  -29.602 1.00 61.73  ? 336  ARG B CG  1 
ATOM   5431  C CD  . ARG B 1 327 ? 11.091  -3.065  -30.556 1.00 63.90  ? 336  ARG B CD  1 
ATOM   5432  N NE  . ARG B 1 327 ? 11.903  -4.088  -29.905 1.00 64.74  ? 336  ARG B NE  1 
ATOM   5433  C CZ  . ARG B 1 327 ? 11.424  -5.186  -29.319 1.00 65.58  ? 336  ARG B CZ  1 
ATOM   5434  N NH1 . ARG B 1 327 ? 10.112  -5.429  -29.248 1.00 65.16  ? 336  ARG B NH1 1 
ATOM   5435  N NH2 . ARG B 1 327 ? 12.273  -6.044  -28.784 1.00 66.71  ? 336  ARG B NH2 1 
ATOM   5436  N N   . THR B 1 328 ? 8.683   0.620   -27.542 1.00 56.79  ? 337  THR B N   1 
ATOM   5437  C CA  . THR B 1 328 ? 8.094   1.079   -26.289 1.00 56.12  ? 337  THR B CA  1 
ATOM   5438  C C   . THR B 1 328 ? 8.216   0.098   -25.154 1.00 56.66  ? 337  THR B C   1 
ATOM   5439  O O   . THR B 1 328 ? 8.550   0.482   -24.045 1.00 55.93  ? 337  THR B O   1 
ATOM   5440  C CB  . THR B 1 328 ? 6.603   1.389   -26.499 1.00 56.17  ? 337  THR B CB  1 
ATOM   5441  O OG1 . THR B 1 328 ? 6.503   2.607   -27.246 1.00 57.21  ? 337  THR B OG1 1 
ATOM   5442  C CG2 . THR B 1 328 ? 5.769   1.484   -25.145 1.00 55.81  ? 337  THR B CG2 1 
ATOM   5443  N N   . ASP B 1 329 ? 7.942   -1.163  -25.457 1.00 58.63  ? 338  ASP B N   1 
ATOM   5444  C CA  . ASP B 1 329 ? 7.623   -2.233  -24.503 1.00 59.38  ? 338  ASP B CA  1 
ATOM   5445  C C   . ASP B 1 329 ? 8.853   -2.809  -23.748 1.00 58.37  ? 338  ASP B C   1 
ATOM   5446  O O   . ASP B 1 329 ? 9.243   -3.935  -23.958 1.00 60.02  ? 338  ASP B O   1 
ATOM   5447  C CB  . ASP B 1 329 ? 6.849   -3.337  -25.295 1.00 62.70  ? 338  ASP B CB  1 
ATOM   5448  C CG  . ASP B 1 329 ? 7.365   -3.522  -26.846 1.00 67.75  ? 338  ASP B CG  1 
ATOM   5449  O OD1 . ASP B 1 329 ? 6.577   -3.943  -27.757 1.00 72.27  ? 338  ASP B OD1 1 
ATOM   5450  O OD2 . ASP B 1 329 ? 8.556   -3.251  -27.161 1.00 69.31  ? 338  ASP B OD2 1 
ATOM   5451  N N   . ARG B 1 330 ? 9.477   -2.046  -22.867 1.00 55.52  ? 339  ARG B N   1 
ATOM   5452  C CA  . ARG B 1 330 ? 10.688  -2.554  -22.210 1.00 54.93  ? 339  ARG B CA  1 
ATOM   5453  C C   . ARG B 1 330 ? 10.350  -3.181  -20.897 1.00 53.97  ? 339  ARG B C   1 
ATOM   5454  O O   . ARG B 1 330 ? 9.304   -2.911  -20.306 1.00 52.78  ? 339  ARG B O   1 
ATOM   5455  C CB  . ARG B 1 330 ? 11.729  -1.475  -21.891 1.00 53.79  ? 339  ARG B CB  1 
ATOM   5456  C CG  . ARG B 1 330 ? 11.935  -0.351  -22.886 1.00 54.23  ? 339  ARG B CG  1 
ATOM   5457  C CD  . ARG B 1 330 ? 12.117  0.962   -22.117 1.00 53.30  ? 339  ARG B CD  1 
ATOM   5458  N NE  . ARG B 1 330 ? 12.354  2.137   -22.962 1.00 52.50  ? 339  ARG B NE  1 
ATOM   5459  C CZ  . ARG B 1 330 ? 13.558  2.601   -23.292 1.00 52.79  ? 339  ARG B CZ  1 
ATOM   5460  N NH1 . ARG B 1 330 ? 14.658  1.973   -22.864 1.00 54.87  ? 339  ARG B NH1 1 
ATOM   5461  N NH2 . ARG B 1 330 ? 13.659  3.687   -24.052 1.00 50.16  ? 339  ARG B NH2 1 
ATOM   5462  N N   . GLY B 1 331 ? 11.292  -3.973  -20.409 1.00 54.23  ? 340  GLY B N   1 
ATOM   5463  C CA  . GLY B 1 331 ? 11.138  -4.661  -19.140 1.00 53.64  ? 340  GLY B CA  1 
ATOM   5464  C C   . GLY B 1 331 ? 11.335  -6.163  -19.214 1.00 55.39  ? 340  GLY B C   1 
ATOM   5465  O O   . GLY B 1 331 ? 11.954  -6.684  -20.129 1.00 57.13  ? 340  GLY B O   1 
ATOM   5466  N N   . TRP B 1 332 ? 10.782  -6.868  -18.246 1.00 55.23  ? 341  TRP B N   1 
ATOM   5467  C CA  . TRP B 1 332 ? 10.955  -8.295  -18.176 1.00 57.29  ? 341  TRP B CA  1 
ATOM   5468  C C   . TRP B 1 332 ? 9.911   -9.089  -18.912 1.00 59.16  ? 341  TRP B C   1 
ATOM   5469  O O   . TRP B 1 332 ? 8.708   -8.997  -18.663 1.00 58.94  ? 341  TRP B O   1 
ATOM   5470  C CB  . TRP B 1 332 ? 10.949  -8.740  -16.745 1.00 56.90  ? 341  TRP B CB  1 
ATOM   5471  C CG  . TRP B 1 332 ? 12.176  -8.364  -16.074 1.00 55.86  ? 341  TRP B CG  1 
ATOM   5472  C CD1 . TRP B 1 332 ? 12.387  -7.256  -15.328 1.00 54.03  ? 341  TRP B CD1 1 
ATOM   5473  C CD2 . TRP B 1 332 ? 13.401  -9.090  -16.070 1.00 57.26  ? 341  TRP B CD2 1 
ATOM   5474  N NE1 . TRP B 1 332 ? 13.678  -7.238  -14.855 1.00 54.47  ? 341  TRP B NE1 1 
ATOM   5475  C CE2 . TRP B 1 332 ? 14.321  -8.360  -15.290 1.00 55.65  ? 341  TRP B CE2 1 
ATOM   5476  C CE3 . TRP B 1 332 ? 13.810  -10.288 -16.644 1.00 59.82  ? 341  TRP B CE3 1 
ATOM   5477  C CZ2 . TRP B 1 332 ? 15.618  -8.786  -15.066 1.00 55.87  ? 341  TRP B CZ2 1 
ATOM   5478  C CZ3 . TRP B 1 332 ? 15.105  -10.706 -16.422 1.00 59.95  ? 341  TRP B CZ3 1 
ATOM   5479  C CH2 . TRP B 1 332 ? 15.994  -9.952  -15.637 1.00 57.55  ? 341  TRP B CH2 1 
ATOM   5480  N N   . TYR B 1 333 ? 10.390  -9.904  -19.818 1.00 61.34  ? 342  TYR B N   1 
ATOM   5481  C CA  . TYR B 1 333 ? 9.560   -10.917 -20.356 1.00 63.25  ? 342  TYR B CA  1 
ATOM   5482  C C   . TYR B 1 333 ? 10.018  -12.163 -19.670 1.00 65.31  ? 342  TYR B C   1 
ATOM   5483  O O   . TYR B 1 333 ? 11.066  -12.176 -19.015 1.00 64.84  ? 342  TYR B O   1 
ATOM   5484  C CB  . TYR B 1 333 ? 9.773   -10.973 -21.835 1.00 64.37  ? 342  TYR B CB  1 
ATOM   5485  C CG  . TYR B 1 333 ? 9.349   -9.698  -22.475 1.00 62.93  ? 342  TYR B CG  1 
ATOM   5486  C CD1 . TYR B 1 333 ? 10.126  -8.555  -22.388 1.00 61.57  ? 342  TYR B CD1 1 
ATOM   5487  C CD2 . TYR B 1 333 ? 8.141   -9.623  -23.146 1.00 64.29  ? 342  TYR B CD2 1 
ATOM   5488  C CE1 . TYR B 1 333 ? 9.719   -7.390  -22.974 1.00 60.83  ? 342  TYR B CE1 1 
ATOM   5489  C CE2 . TYR B 1 333 ? 7.729   -8.454  -23.743 1.00 62.72  ? 342  TYR B CE2 1 
ATOM   5490  C CZ  . TYR B 1 333 ? 8.523   -7.353  -23.651 1.00 61.33  ? 342  TYR B CZ  1 
ATOM   5491  O OH  . TYR B 1 333 ? 8.094   -6.217  -24.242 1.00 61.91  ? 342  TYR B OH  1 
ATOM   5492  N N   . CYS B 1 334 ? 9.220   -13.210 -19.810 1.00 67.61  ? 343  CYS B N   1 
ATOM   5493  C CA  . CYS B 1 334 ? 9.390   -14.381 -18.994 1.00 69.74  ? 343  CYS B CA  1 
ATOM   5494  C C   . CYS B 1 334 ? 8.254   -15.383 -19.250 1.00 71.64  ? 343  CYS B C   1 
ATOM   5495  O O   . CYS B 1 334 ? 7.087   -15.053 -19.114 1.00 70.77  ? 343  CYS B O   1 
ATOM   5496  C CB  . CYS B 1 334 ? 9.450   -13.906 -17.552 1.00 67.78  ? 343  CYS B CB  1 
ATOM   5497  S SG  . CYS B 1 334 ? 9.854   -15.193 -16.429 1.00 72.14  ? 343  CYS B SG  1 
ATOM   5498  N N   . ASP B 1 335 ? 8.608   -16.597 -19.651 1.00 74.79  ? 344  ASP B N   1 
ATOM   5499  C CA  . ASP B 1 335 ? 7.645   -17.545 -20.215 1.00 77.43  ? 344  ASP B CA  1 
ATOM   5500  C C   . ASP B 1 335 ? 6.639   -18.058 -19.202 1.00 77.75  ? 344  ASP B C   1 
ATOM   5501  O O   . ASP B 1 335 ? 7.026   -18.463 -18.114 1.00 77.97  ? 344  ASP B O   1 
ATOM   5502  C CB  . ASP B 1 335 ? 8.378   -18.772 -20.771 1.00 81.01  ? 344  ASP B CB  1 
ATOM   5503  C CG  . ASP B 1 335 ? 8.776   -18.627 -22.222 1.00 83.35  ? 344  ASP B CG  1 
ATOM   5504  O OD1 . ASP B 1 335 ? 7.894   -18.425 -23.101 1.00 85.95  ? 344  ASP B OD1 1 
ATOM   5505  O OD2 . ASP B 1 335 ? 9.989   -18.763 -22.482 1.00 85.68  ? 344  ASP B OD2 1 
ATOM   5506  N N   . ASN B 1 336 ? 5.360   -18.077 -19.575 1.00 78.21  ? 345  ASN B N   1 
ATOM   5507  C CA  . ASN B 1 336 ? 4.322   -18.733 -18.772 1.00 79.54  ? 345  ASN B CA  1 
ATOM   5508  C C   . ASN B 1 336 ? 3.767   -19.881 -19.569 1.00 83.20  ? 345  ASN B C   1 
ATOM   5509  O O   . ASN B 1 336 ? 4.350   -20.262 -20.583 1.00 85.63  ? 345  ASN B O   1 
ATOM   5510  C CB  . ASN B 1 336 ? 3.192   -17.764 -18.415 1.00 77.38  ? 345  ASN B CB  1 
ATOM   5511  C CG  . ASN B 1 336 ? 2.508   -18.105 -17.087 1.00 76.83  ? 345  ASN B CG  1 
ATOM   5512  O OD1 . ASN B 1 336 ? 3.121   -18.072 -16.024 1.00 73.37  ? 345  ASN B OD1 1 
ATOM   5513  N ND2 . ASN B 1 336 ? 1.223   -18.410 -17.153 1.00 79.95  ? 345  ASN B ND2 1 
ATOM   5514  N N   . ALA B 1 337 ? 2.632   -20.416 -19.138 1.00 84.22  ? 346  ALA B N   1 
ATOM   5515  C CA  . ALA B 1 337 ? 2.110   -21.629 -19.730 1.00 87.65  ? 346  ALA B CA  1 
ATOM   5516  C C   . ALA B 1 337 ? 1.913   -21.503 -21.257 1.00 88.57  ? 346  ALA B C   1 
ATOM   5517  O O   . ALA B 1 337 ? 0.830   -21.178 -21.736 1.00 88.22  ? 346  ALA B O   1 
ATOM   5518  C CB  . ALA B 1 337 ? 0.846   -22.042 -19.024 1.00 88.32  ? 346  ALA B CB  1 
ATOM   5519  N N   . GLY B 1 338 ? 2.986   -21.740 -22.012 1.00 89.89  ? 347  GLY B N   1 
ATOM   5520  C CA  . GLY B 1 338 ? 2.939   -21.751 -23.485 1.00 91.26  ? 347  GLY B CA  1 
ATOM   5521  C C   . GLY B 1 338 ? 2.878   -20.379 -24.126 1.00 88.27  ? 347  GLY B C   1 
ATOM   5522  O O   . GLY B 1 338 ? 2.918   -20.237 -25.356 1.00 89.37  ? 347  GLY B O   1 
ATOM   5523  N N   . SER B 1 339 ? 2.761   -19.372 -23.277 1.00 84.60  ? 348  SER B N   1 
ATOM   5524  C CA  . SER B 1 339 ? 2.610   -18.014 -23.713 1.00 81.07  ? 348  SER B CA  1 
ATOM   5525  C C   . SER B 1 339 ? 3.622   -17.296 -22.857 1.00 78.66  ? 348  SER B C   1 
ATOM   5526  O O   . SER B 1 339 ? 4.342   -17.959 -22.111 1.00 79.47  ? 348  SER B O   1 
ATOM   5527  C CB  . SER B 1 339 ? 1.188   -17.525 -23.450 1.00 79.74  ? 348  SER B CB  1 
ATOM   5528  O OG  . SER B 1 339 ? 0.237   -18.256 -24.203 1.00 81.56  ? 348  SER B OG  1 
ATOM   5529  N N   . VAL B 1 340 ? 3.696   -15.966 -22.973 1.00 75.67  ? 349  VAL B N   1 
ATOM   5530  C CA  . VAL B 1 340 ? 4.747   -15.166 -22.323 1.00 73.38  ? 349  VAL B CA  1 
ATOM   5531  C C   . VAL B 1 340 ? 4.144   -14.046 -21.532 1.00 70.75  ? 349  VAL B C   1 
ATOM   5532  O O   . VAL B 1 340 ? 3.319   -13.295 -22.064 1.00 69.71  ? 349  VAL B O   1 
ATOM   5533  C CB  . VAL B 1 340 ? 5.669   -14.472 -23.330 1.00 72.47  ? 349  VAL B CB  1 
ATOM   5534  C CG1 . VAL B 1 340 ? 6.851   -13.881 -22.616 1.00 70.56  ? 349  VAL B CG1 1 
ATOM   5535  C CG2 . VAL B 1 340 ? 6.131   -15.446 -24.414 1.00 75.87  ? 349  VAL B CG2 1 
ATOM   5536  N N   . SER B 1 341 ? 4.589   -13.926 -20.276 1.00 70.22  ? 350  SER B N   1 
ATOM   5537  C CA  . SER B 1 341 ? 4.166   -12.860 -19.336 1.00 67.87  ? 350  SER B CA  1 
ATOM   5538  C C   . SER B 1 341 ? 5.122   -11.650 -19.288 1.00 66.35  ? 350  SER B C   1 
ATOM   5539  O O   . SER B 1 341 ? 6.344   -11.759 -19.084 1.00 66.35  ? 350  SER B O   1 
ATOM   5540  C CB  . SER B 1 341 ? 3.946   -13.413 -17.925 1.00 67.60  ? 350  SER B CB  1 
ATOM   5541  O OG  . SER B 1 341 ? 2.696   -14.045 -17.821 1.00 67.43  ? 350  SER B OG  1 
ATOM   5542  N N   . PHE B 1 342 ? 4.538   -10.483 -19.482 1.00 65.35  ? 351  PHE B N   1 
ATOM   5543  C CA  . PHE B 1 342 ? 5.312   -9.271  -19.515 1.00 64.41  ? 351  PHE B CA  1 
ATOM   5544  C C   . PHE B 1 342 ? 4.928   -8.350  -18.345 1.00 63.30  ? 351  PHE B C   1 
ATOM   5545  O O   . PHE B 1 342 ? 3.742   -8.119  -18.072 1.00 63.07  ? 351  PHE B O   1 
ATOM   5546  C CB  . PHE B 1 342 ? 5.126   -8.587  -20.866 1.00 63.85  ? 351  PHE B CB  1 
ATOM   5547  C CG  . PHE B 1 342 ? 5.668   -7.193  -20.921 1.00 61.93  ? 351  PHE B CG  1 
ATOM   5548  C CD1 . PHE B 1 342 ? 7.008   -6.944  -20.689 1.00 62.08  ? 351  PHE B CD1 1 
ATOM   5549  C CD2 . PHE B 1 342 ? 4.829   -6.128  -21.209 1.00 61.02  ? 351  PHE B CD2 1 
ATOM   5550  C CE1 . PHE B 1 342 ? 7.489   -5.660  -20.731 1.00 60.97  ? 351  PHE B CE1 1 
ATOM   5551  C CE2 . PHE B 1 342 ? 5.306   -4.834  -21.270 1.00 59.60  ? 351  PHE B CE2 1 
ATOM   5552  C CZ  . PHE B 1 342 ? 6.632   -4.599  -21.028 1.00 59.66  ? 351  PHE B CZ  1 
ATOM   5553  N N   . PHE B 1 343 ? 5.953   -7.839  -17.665 1.00 63.29  ? 352  PHE B N   1 
ATOM   5554  C CA  . PHE B 1 343 ? 5.811   -7.000  -16.488 1.00 62.44  ? 352  PHE B CA  1 
ATOM   5555  C C   . PHE B 1 343 ? 6.410   -5.669  -16.853 1.00 62.26  ? 352  PHE B C   1 
ATOM   5556  O O   . PHE B 1 343 ? 7.631   -5.553  -16.999 1.00 62.34  ? 352  PHE B O   1 
ATOM   5557  C CB  . PHE B 1 343 ? 6.566   -7.613  -15.314 1.00 62.35  ? 352  PHE B CB  1 
ATOM   5558  C CG  . PHE B 1 343 ? 6.460   -9.097  -15.258 1.00 64.19  ? 352  PHE B CG  1 
ATOM   5559  C CD1 . PHE B 1 343 ? 7.219   -9.898  -16.116 1.00 65.57  ? 352  PHE B CD1 1 
ATOM   5560  C CD2 . PHE B 1 343 ? 5.582   -9.699  -14.381 1.00 64.13  ? 352  PHE B CD2 1 
ATOM   5561  C CE1 . PHE B 1 343 ? 7.118   -11.277 -16.097 1.00 67.07  ? 352  PHE B CE1 1 
ATOM   5562  C CE2 . PHE B 1 343 ? 5.470   -11.080 -14.351 1.00 65.42  ? 352  PHE B CE2 1 
ATOM   5563  C CZ  . PHE B 1 343 ? 6.249   -11.876 -15.213 1.00 67.10  ? 352  PHE B CZ  1 
ATOM   5564  N N   . PRO B 1 344 ? 5.551   -4.657  -16.996 1.00 62.58  ? 353  PRO B N   1 
ATOM   5565  C CA  . PRO B 1 344 ? 5.846   -3.329  -17.546 1.00 62.77  ? 353  PRO B CA  1 
ATOM   5566  C C   . PRO B 1 344 ? 6.908   -2.514  -16.779 1.00 63.25  ? 353  PRO B C   1 
ATOM   5567  O O   . PRO B 1 344 ? 7.782   -1.886  -17.400 1.00 63.42  ? 353  PRO B O   1 
ATOM   5568  C CB  . PRO B 1 344 ? 4.498   -2.618  -17.473 1.00 61.70  ? 353  PRO B CB  1 
ATOM   5569  C CG  . PRO B 1 344 ? 3.493   -3.738  -17.327 1.00 62.57  ? 353  PRO B CG  1 
ATOM   5570  C CD  . PRO B 1 344 ? 4.181   -4.727  -16.477 1.00 62.44  ? 353  PRO B CD  1 
ATOM   5571  N N   . GLN B 1 345 ? 6.855   -2.530  -15.448 1.00 64.30  ? 354  GLN B N   1 
ATOM   5572  C CA  . GLN B 1 345 ? 7.800   -1.716  -14.631 1.00 64.46  ? 354  GLN B CA  1 
ATOM   5573  C C   . GLN B 1 345 ? 8.588   -2.427  -13.471 1.00 65.25  ? 354  GLN B C   1 
ATOM   5574  O O   . GLN B 1 345 ? 7.966   -3.102  -12.609 1.00 65.24  ? 354  GLN B O   1 
ATOM   5575  C CB  . GLN B 1 345 ? 7.098   -0.429  -14.120 1.00 62.93  ? 354  GLN B CB  1 
ATOM   5576  C CG  . GLN B 1 345 ? 5.593   -0.565  -13.922 1.00 63.66  ? 354  GLN B CG  1 
ATOM   5577  C CD  . GLN B 1 345 ? 5.247   -1.678  -12.961 1.00 64.56  ? 354  GLN B CD  1 
ATOM   5578  O OE1 . GLN B 1 345 ? 5.675   -1.665  -11.797 1.00 64.13  ? 354  GLN B OE1 1 
ATOM   5579  N NE2 . GLN B 1 345 ? 4.491   -2.672  -13.454 1.00 64.57  ? 354  GLN B NE2 1 
ATOM   5580  N N   . ALA B 1 346 ? 9.938   -2.251  -13.483 1.00 65.73  ? 355  ALA B N   1 
ATOM   5581  C CA  . ALA B 1 346 ? 10.913  -2.709  -12.419 1.00 65.91  ? 355  ALA B CA  1 
ATOM   5582  C C   . ALA B 1 346 ? 10.232  -3.340  -11.171 1.00 65.68  ? 355  ALA B C   1 
ATOM   5583  O O   . ALA B 1 346 ? 10.153  -4.590  -11.069 1.00 67.71  ? 355  ALA B O   1 
ATOM   5584  C CB  . ALA B 1 346 ? 11.927  -1.545  -11.999 1.00 64.19  ? 355  ALA B CB  1 
ATOM   5585  N N   . GLU B 1 347 ? 9.785   -2.463  -10.248 1.00 62.65  ? 356  GLU B N   1 
ATOM   5586  C CA  . GLU B 1 347 ? 8.680   -2.690  -9.306  1.00 60.86  ? 356  GLU B CA  1 
ATOM   5587  C C   . GLU B 1 347 ? 8.240   -4.110  -9.105  1.00 60.94  ? 356  GLU B C   1 
ATOM   5588  O O   . GLU B 1 347 ? 8.501   -4.716  -8.064  1.00 61.04  ? 356  GLU B O   1 
ATOM   5589  C CB  . GLU B 1 347 ? 7.482   -1.846  -9.757  1.00 60.46  ? 356  GLU B CB  1 
ATOM   5590  C CG  . GLU B 1 347 ? 7.791   -0.410  -9.568  1.00 61.74  ? 356  GLU B CG  1 
ATOM   5591  C CD  . GLU B 1 347 ? 8.736   -0.223  -8.344  1.00 66.16  ? 356  GLU B CD  1 
ATOM   5592  O OE1 . GLU B 1 347 ? 9.898   0.196   -8.539  1.00 67.68  ? 356  GLU B OE1 1 
ATOM   5593  O OE2 . GLU B 1 347 ? 8.335   -0.543  -7.192  1.00 67.21  ? 356  GLU B OE2 1 
ATOM   5594  N N   . THR B 1 348 ? 7.573   -4.624  -10.133 1.00 60.15  ? 357  THR B N   1 
ATOM   5595  C CA  . THR B 1 348 ? 7.032   -5.960  -10.145 1.00 60.29  ? 357  THR B CA  1 
ATOM   5596  C C   . THR B 1 348 ? 8.099   -7.050  -10.039 1.00 60.66  ? 357  THR B C   1 
ATOM   5597  O O   . THR B 1 348 ? 7.781   -8.140  -9.582  1.00 62.63  ? 357  THR B O   1 
ATOM   5598  C CB  . THR B 1 348 ? 6.257   -6.201  -11.430 1.00 61.29  ? 357  THR B CB  1 
ATOM   5599  O OG1 . THR B 1 348 ? 6.045   -4.952  -12.096 1.00 60.16  ? 357  THR B OG1 1 
ATOM   5600  C CG2 . THR B 1 348 ? 4.934   -6.828  -11.124 1.00 62.44  ? 357  THR B CG2 1 
ATOM   5601  N N   . CYS B 1 349 ? 9.343   -6.776  -10.446 1.00 58.39  ? 358  CYS B N   1 
ATOM   5602  C CA  . CYS B 1 349 ? 10.376  -7.821  -10.508 1.00 58.27  ? 358  CYS B CA  1 
ATOM   5603  C C   . CYS B 1 349 ? 11.627  -7.547  -9.722  1.00 56.42  ? 358  CYS B C   1 
ATOM   5604  O O   . CYS B 1 349 ? 12.141  -6.443  -9.755  1.00 54.58  ? 358  CYS B O   1 
ATOM   5605  C CB  . CYS B 1 349 ? 10.771  -8.058  -11.950 1.00 59.11  ? 358  CYS B CB  1 
ATOM   5606  S SG  . CYS B 1 349 ? 9.381   -8.658  -12.880 1.00 61.67  ? 358  CYS B SG  1 
ATOM   5607  N N   . LYS B 1 350 ? 12.131  -8.557  -9.027  1.00 56.88  ? 359  LYS B N   1 
ATOM   5608  C CA  . LYS B 1 350 ? 13.479  -8.481  -8.451  1.00 56.52  ? 359  LYS B CA  1 
ATOM   5609  C C   . LYS B 1 350 ? 14.260  -9.721  -8.725  1.00 58.46  ? 359  LYS B C   1 
ATOM   5610  O O   . LYS B 1 350 ? 13.702  -10.791 -8.964  1.00 60.55  ? 359  LYS B O   1 
ATOM   5611  C CB  . LYS B 1 350 ? 13.491  -8.227  -6.958  1.00 55.48  ? 359  LYS B CB  1 
ATOM   5612  C CG  . LYS B 1 350 ? 12.246  -8.616  -6.290  1.00 57.67  ? 359  LYS B CG  1 
ATOM   5613  C CD  . LYS B 1 350 ? 11.848  -7.554  -5.318  1.00 57.81  ? 359  LYS B CD  1 
ATOM   5614  C CE  . LYS B 1 350 ? 10.372  -7.662  -5.085  1.00 59.82  ? 359  LYS B CE  1 
ATOM   5615  N NZ  . LYS B 1 350 ? 10.009  -6.528  -4.255  1.00 61.63  ? 359  LYS B NZ  1 
ATOM   5616  N N   . VAL B 1 351 ? 15.571  -9.568  -8.647  1.00 57.94  ? 360  VAL B N   1 
ATOM   5617  C CA  . VAL B 1 351 ? 16.462  -10.487 -9.295  1.00 59.71  ? 360  VAL B CA  1 
ATOM   5618  C C   . VAL B 1 351 ? 17.730  -10.653 -8.485  1.00 60.06  ? 360  VAL B C   1 
ATOM   5619  O O   . VAL B 1 351 ? 18.249  -9.702  -7.947  1.00 58.16  ? 360  VAL B O   1 
ATOM   5620  C CB  . VAL B 1 351 ? 16.752  -9.987  -10.723 1.00 59.46  ? 360  VAL B CB  1 
ATOM   5621  C CG1 . VAL B 1 351 ? 17.116  -8.491  -10.718 1.00 57.04  ? 360  VAL B CG1 1 
ATOM   5622  C CG2 . VAL B 1 351 ? 17.816  -10.820 -11.379 1.00 62.21  ? 360  VAL B CG2 1 
ATOM   5623  N N   . GLN B 1 352 ? 18.214  -11.883 -8.407  1.00 63.06  ? 361  GLN B N   1 
ATOM   5624  C CA  . GLN B 1 352 ? 19.361  -12.247 -7.580  1.00 64.97  ? 361  GLN B CA  1 
ATOM   5625  C C   . GLN B 1 352 ? 20.211  -13.280 -8.293  1.00 67.44  ? 361  GLN B C   1 
ATOM   5626  O O   . GLN B 1 352 ? 19.866  -14.463 -8.326  1.00 70.02  ? 361  GLN B O   1 
ATOM   5627  C CB  . GLN B 1 352 ? 18.876  -12.844 -6.277  1.00 65.61  ? 361  GLN B CB  1 
ATOM   5628  C CG  . GLN B 1 352 ? 19.962  -13.237 -5.293  1.00 71.14  ? 361  GLN B CG  1 
ATOM   5629  C CD  . GLN B 1 352 ? 19.639  -12.664 -3.906  1.00 78.06  ? 361  GLN B CD  1 
ATOM   5630  O OE1 . GLN B 1 352 ? 19.156  -13.367 -2.999  1.00 81.75  ? 361  GLN B OE1 1 
ATOM   5631  N NE2 . GLN B 1 352 ? 19.855  -11.355 -3.756  1.00 78.15  ? 361  GLN B NE2 1 
ATOM   5632  N N   . SER B 1 353 ? 21.335  -12.830 -8.836  1.00 67.13  ? 362  SER B N   1 
ATOM   5633  C CA  . SER B 1 353 ? 22.106  -13.627 -9.761  1.00 69.20  ? 362  SER B CA  1 
ATOM   5634  C C   . SER B 1 353 ? 21.227  -13.883 -10.980 1.00 69.45  ? 362  SER B C   1 
ATOM   5635  O O   . SER B 1 353 ? 20.718  -12.932 -11.574 1.00 67.67  ? 362  SER B O   1 
ATOM   5636  C CB  . SER B 1 353 ? 22.562  -14.925 -9.110  1.00 71.83  ? 362  SER B CB  1 
ATOM   5637  O OG  . SER B 1 353 ? 23.477  -15.599 -9.947  1.00 75.18  ? 362  SER B OG  1 
ATOM   5638  N N   . ASN B 1 354 ? 21.027  -15.148 -11.345 1.00 71.61  ? 363  ASN B N   1 
ATOM   5639  C CA  . ASN B 1 354 ? 20.227  -15.485 -12.533 1.00 72.21  ? 363  ASN B CA  1 
ATOM   5640  C C   . ASN B 1 354 ? 18.813  -15.894 -12.162 1.00 71.27  ? 363  ASN B C   1 
ATOM   5641  O O   . ASN B 1 354 ? 18.091  -16.534 -12.935 1.00 72.65  ? 363  ASN B O   1 
ATOM   5642  C CB  . ASN B 1 354 ? 20.887  -16.613 -13.303 1.00 75.82  ? 363  ASN B CB  1 
ATOM   5643  C CG  . ASN B 1 354 ? 20.921  -17.892 -12.515 1.00 78.39  ? 363  ASN B CG  1 
ATOM   5644  O OD1 . ASN B 1 354 ? 20.739  -17.891 -11.293 1.00 77.13  ? 363  ASN B OD1 1 
ATOM   5645  N ND2 . ASN B 1 354 ? 21.149  -18.998 -13.206 1.00 82.50  ? 363  ASN B ND2 1 
ATOM   5646  N N   . ARG B 1 355 ? 18.442  -15.513 -10.956 1.00 68.61  ? 364  ARG B N   1 
ATOM   5647  C CA  . ARG B 1 355 ? 17.157  -15.822 -10.445 1.00 67.96  ? 364  ARG B CA  1 
ATOM   5648  C C   . ARG B 1 355 ? 16.280  -14.593 -10.471 1.00 64.88  ? 364  ARG B C   1 
ATOM   5649  O O   . ARG B 1 355 ? 16.689  -13.526 -10.029 1.00 62.66  ? 364  ARG B O   1 
ATOM   5650  C CB  . ARG B 1 355 ? 17.324  -16.286 -9.028  1.00 68.10  ? 364  ARG B CB  1 
ATOM   5651  C CG  . ARG B 1 355 ? 16.371  -17.338 -8.711  1.00 70.55  ? 364  ARG B CG  1 
ATOM   5652  C CD  . ARG B 1 355 ? 16.628  -18.515 -9.582  1.00 73.60  ? 364  ARG B CD  1 
ATOM   5653  N NE  . ARG B 1 355 ? 15.352  -18.984 -10.070 1.00 75.70  ? 364  ARG B NE  1 
ATOM   5654  C CZ  . ARG B 1 355 ? 15.115  -20.237 -10.408 1.00 79.08  ? 364  ARG B CZ  1 
ATOM   5655  N NH1 . ARG B 1 355 ? 16.082  -21.140 -10.301 1.00 81.54  ? 364  ARG B NH1 1 
ATOM   5656  N NH2 . ARG B 1 355 ? 13.916  -20.577 -10.864 1.00 81.04  ? 364  ARG B NH2 1 
ATOM   5657  N N   . VAL B 1 356 ? 15.070  -14.738 -10.989 1.00 65.00  ? 365  VAL B N   1 
ATOM   5658  C CA  . VAL B 1 356 ? 14.161  -13.607 -11.102 1.00 62.40  ? 365  VAL B CA  1 
ATOM   5659  C C   . VAL B 1 356 ? 12.858  -13.956 -10.434 1.00 62.87  ? 365  VAL B C   1 
ATOM   5660  O O   . VAL B 1 356 ? 12.461  -15.127 -10.388 1.00 65.82  ? 365  VAL B O   1 
ATOM   5661  C CB  . VAL B 1 356 ? 13.881  -13.251 -12.568 1.00 62.21  ? 365  VAL B CB  1 
ATOM   5662  C CG1 . VAL B 1 356 ? 12.625  -12.427 -12.687 1.00 59.98  ? 365  VAL B CG1 1 
ATOM   5663  C CG2 . VAL B 1 356 ? 15.025  -12.476 -13.144 1.00 61.55  ? 365  VAL B CG2 1 
ATOM   5664  N N   . PHE B 1 357 ? 12.196  -12.929 -9.920  1.00 60.44  ? 366  PHE B N   1 
ATOM   5665  C CA  . PHE B 1 357 ? 10.973  -13.102 -9.188  1.00 60.17  ? 366  PHE B CA  1 
ATOM   5666  C C   . PHE B 1 357 ? 10.070  -12.010 -9.616  1.00 58.57  ? 366  PHE B C   1 
ATOM   5667  O O   . PHE B 1 357 ? 10.380  -10.840 -9.401  1.00 56.31  ? 366  PHE B O   1 
ATOM   5668  C CB  . PHE B 1 357 ? 11.250  -12.977 -7.705  1.00 58.97  ? 366  PHE B CB  1 
ATOM   5669  C CG  . PHE B 1 357 ? 12.122  -14.062 -7.177  1.00 60.53  ? 366  PHE B CG  1 
ATOM   5670  C CD1 . PHE B 1 357 ? 13.495  -14.033 -7.376  1.00 61.13  ? 366  PHE B CD1 1 
ATOM   5671  C CD2 . PHE B 1 357 ? 11.579  -15.128 -6.489  1.00 61.39  ? 366  PHE B CD2 1 
ATOM   5672  C CE1 . PHE B 1 357 ? 14.316  -15.064 -6.888  1.00 62.12  ? 366  PHE B CE1 1 
ATOM   5673  C CE2 . PHE B 1 357 ? 12.390  -16.144 -5.998  1.00 62.40  ? 366  PHE B CE2 1 
ATOM   5674  C CZ  . PHE B 1 357 ? 13.763  -16.109 -6.198  1.00 62.52  ? 366  PHE B CZ  1 
ATOM   5675  N N   . CYS B 1 358 ? 8.967   -12.381 -10.249 1.00 60.15  ? 367  CYS B N   1 
ATOM   5676  C CA  . CYS B 1 358 ? 7.995   -11.380 -10.651 1.00 59.53  ? 367  CYS B CA  1 
ATOM   5677  C C   . CYS B 1 358 ? 6.614   -11.627 -10.069 1.00 60.07  ? 367  CYS B C   1 
ATOM   5678  O O   . CYS B 1 358 ? 6.342   -12.680 -9.486  1.00 62.13  ? 367  CYS B O   1 
ATOM   5679  C CB  . CYS B 1 358 ? 7.956   -11.236 -12.168 1.00 60.11  ? 367  CYS B CB  1 
ATOM   5680  S SG  . CYS B 1 358 ? 9.521   -10.701 -12.788 1.00 61.16  ? 367  CYS B SG  1 
ATOM   5681  N N   . ASP B 1 359 ? 5.755   -10.631 -10.227 1.00 58.78  ? 368  ASP B N   1 
ATOM   5682  C CA  . ASP B 1 359 ? 4.412   -10.703 -9.719  1.00 59.57  ? 368  ASP B CA  1 
ATOM   5683  C C   . ASP B 1 359 ? 3.396   -10.668 -10.854 1.00 60.96  ? 368  ASP B C   1 
ATOM   5684  O O   . ASP B 1 359 ? 3.245   -9.645  -11.561 1.00 59.60  ? 368  ASP B O   1 
ATOM   5685  C CB  . ASP B 1 359 ? 4.167   -9.543  -8.775  1.00 57.27  ? 368  ASP B CB  1 
ATOM   5686  C CG  . ASP B 1 359 ? 3.026   -9.798  -7.848  1.00 58.15  ? 368  ASP B CG  1 
ATOM   5687  O OD1 . ASP B 1 359 ? 1.944   -10.173 -8.338  1.00 60.13  ? 368  ASP B OD1 1 
ATOM   5688  O OD2 . ASP B 1 359 ? 3.209   -9.640  -6.625  1.00 57.74  ? 368  ASP B OD2 1 
ATOM   5689  N N   . THR B 1 360 ? 2.702   -11.797 -11.022 1.00 64.26  ? 369  THR B N   1 
ATOM   5690  C CA  . THR B 1 360 ? 1.603   -11.903 -11.979 1.00 65.92  ? 369  THR B CA  1 
ATOM   5691  C C   . THR B 1 360 ? 0.721   -10.666 -11.882 1.00 65.19  ? 369  THR B C   1 
ATOM   5692  O O   . THR B 1 360 ? 0.621   -9.906  -12.840 1.00 64.90  ? 369  THR B O   1 
ATOM   5693  C CB  . THR B 1 360 ? 0.756   -13.116 -11.705 1.00 67.86  ? 369  THR B CB  1 
ATOM   5694  O OG1 . THR B 1 360 ? 1.607   -14.260 -11.711 1.00 68.43  ? 369  THR B OG1 1 
ATOM   5695  C CG2 . THR B 1 360 ? -0.332  -13.239 -12.760 1.00 69.47  ? 369  THR B CG2 1 
ATOM   5696  N N   . MET B 1 361 ? 0.141   -10.446 -10.702 1.00 65.72  ? 370  MET B N   1 
ATOM   5697  C CA  . MET B 1 361 ? -0.832  -9.378  -10.478 1.00 65.37  ? 370  MET B CA  1 
ATOM   5698  C C   . MET B 1 361 ? -1.155  -8.470  -11.638 1.00 64.17  ? 370  MET B C   1 
ATOM   5699  O O   . MET B 1 361 ? -2.305  -8.513  -12.124 1.00 65.19  ? 370  MET B O   1 
ATOM   5700  C CB  . MET B 1 361 ? -0.540  -8.546  -9.232  1.00 64.29  ? 370  MET B CB  1 
ATOM   5701  C CG  . MET B 1 361 ? -1.530  -8.861  -8.091  1.00 68.42  ? 370  MET B CG  1 
ATOM   5702  S SD  . MET B 1 361 ? -3.320  -8.697  -8.475  1.00 76.43  ? 370  MET B SD  1 
ATOM   5703  C CE  . MET B 1 361 ? -3.734  -10.032 -9.655  1.00 76.75  ? 370  MET B CE  1 
ATOM   5704  N N   . ASN B 1 362 ? -0.200  -7.649  -12.084 1.00 62.11  ? 371  ASN B N   1 
ATOM   5705  C CA  . ASN B 1 362 ? -0.545  -6.830  -13.234 1.00 61.18  ? 371  ASN B CA  1 
ATOM   5706  C C   . ASN B 1 362 ? 0.003   -7.203  -14.614 1.00 61.62  ? 371  ASN B C   1 
ATOM   5707  O O   . ASN B 1 362 ? -0.330  -6.551  -15.596 1.00 61.42  ? 371  ASN B O   1 
ATOM   5708  C CB  . ASN B 1 362 ? -0.556  -5.348  -12.903 1.00 59.09  ? 371  ASN B CB  1 
ATOM   5709  C CG  . ASN B 1 362 ? -1.858  -4.936  -12.243 1.00 59.27  ? 371  ASN B CG  1 
ATOM   5710  O OD1 . ASN B 1 362 ? -2.870  -4.700  -12.905 1.00 59.51  ? 371  ASN B OD1 1 
ATOM   5711  N ND2 . ASN B 1 362 ? -1.848  -4.891  -10.929 1.00 59.81  ? 371  ASN B ND2 1 
ATOM   5712  N N   . SER B 1 363 ? 0.771   -8.283  -14.683 1.00 62.40  ? 372  SER B N   1 
ATOM   5713  C CA  . SER B 1 363 ? 1.312   -8.821  -15.943 1.00 62.94  ? 372  SER B CA  1 
ATOM   5714  C C   . SER B 1 363 ? 0.397   -8.739  -17.164 1.00 63.06  ? 372  SER B C   1 
ATOM   5715  O O   . SER B 1 363 ? -0.844  -8.714  -17.038 1.00 63.48  ? 372  SER B O   1 
ATOM   5716  C CB  . SER B 1 363 ? 1.699   -10.286 -15.755 1.00 65.38  ? 372  SER B CB  1 
ATOM   5717  O OG  . SER B 1 363 ? 0.585   -11.055 -15.300 1.00 67.66  ? 372  SER B OG  1 
ATOM   5718  N N   . LEU B 1 364 ? 1.024   -8.724  -18.341 1.00 62.54  ? 373  LEU B N   1 
ATOM   5719  C CA  . LEU B 1 364 ? 0.320   -8.814  -19.614 1.00 62.71  ? 373  LEU B CA  1 
ATOM   5720  C C   . LEU B 1 364 ? 0.712   -10.103 -20.287 1.00 64.74  ? 373  LEU B C   1 
ATOM   5721  O O   . LEU B 1 364 ? 1.899   -10.417 -20.367 1.00 65.13  ? 373  LEU B O   1 
ATOM   5722  C CB  . LEU B 1 364 ? 0.680   -7.620  -20.495 1.00 60.98  ? 373  LEU B CB  1 
ATOM   5723  C CG  . LEU B 1 364 ? -0.264  -6.413  -20.548 1.00 58.98  ? 373  LEU B CG  1 
ATOM   5724  C CD1 . LEU B 1 364 ? -1.048  -6.198  -19.255 1.00 58.96  ? 373  LEU B CD1 1 
ATOM   5725  C CD2 . LEU B 1 364 ? 0.502   -5.165  -20.891 1.00 56.39  ? 373  LEU B CD2 1 
ATOM   5726  N N   . THR B 1 365 ? -0.272  -10.856 -20.754 1.00 65.84  ? 374  THR B N   1 
ATOM   5727  C CA  . THR B 1 365 ? 0.044   -12.139 -21.328 1.00 67.86  ? 374  THR B CA  1 
ATOM   5728  C C   . THR B 1 365 ? 0.134   -11.956 -22.824 1.00 67.68  ? 374  THR B C   1 
ATOM   5729  O O   . THR B 1 365 ? -0.686  -11.264 -23.418 1.00 67.11  ? 374  THR B O   1 
ATOM   5730  C CB  . THR B 1 365 ? -0.963  -13.182 -20.912 1.00 69.91  ? 374  THR B CB  1 
ATOM   5731  O OG1 . THR B 1 365 ? -1.561  -12.763 -19.677 1.00 70.12  ? 374  THR B OG1 1 
ATOM   5732  C CG2 . THR B 1 365 ? -0.265  -14.513 -20.710 1.00 71.96  ? 374  THR B CG2 1 
ATOM   5733  N N   . LEU B 1 366 ? 1.174   -12.532 -23.417 1.00 68.15  ? 375  LEU B N   1 
ATOM   5734  C CA  . LEU B 1 366 ? 1.508   -12.284 -24.808 1.00 67.52  ? 375  LEU B CA  1 
ATOM   5735  C C   . LEU B 1 366 ? 1.991   -13.554 -25.460 1.00 70.60  ? 375  LEU B C   1 
ATOM   5736  O O   . LEU B 1 366 ? 2.429   -14.474 -24.783 1.00 72.10  ? 375  LEU B O   1 
ATOM   5737  C CB  . LEU B 1 366 ? 2.627   -11.259 -24.892 1.00 64.97  ? 375  LEU B CB  1 
ATOM   5738  C CG  . LEU B 1 366 ? 2.468   -9.931  -24.177 1.00 59.80  ? 375  LEU B CG  1 
ATOM   5739  C CD1 . LEU B 1 366 ? 3.749   -9.191  -24.283 1.00 55.23  ? 375  LEU B CD1 1 
ATOM   5740  C CD2 . LEU B 1 366 ? 1.344   -9.156  -24.815 1.00 58.48  ? 375  LEU B CD2 1 
ATOM   5741  N N   . PRO B 1 367 ? 1.932   -13.601 -26.789 1.00 71.73  ? 376  PRO B N   1 
ATOM   5742  C CA  . PRO B 1 367 ? 2.380   -14.793 -27.513 1.00 75.13  ? 376  PRO B CA  1 
ATOM   5743  C C   . PRO B 1 367 ? 3.888   -14.781 -27.735 1.00 75.74  ? 376  PRO B C   1 
ATOM   5744  O O   . PRO B 1 367 ? 4.499   -13.703 -27.824 1.00 73.58  ? 376  PRO B O   1 
ATOM   5745  C CB  . PRO B 1 367 ? 1.650   -14.675 -28.858 1.00 75.85  ? 376  PRO B CB  1 
ATOM   5746  C CG  . PRO B 1 367 ? 1.534   -13.157 -29.061 1.00 72.89  ? 376  PRO B CG  1 
ATOM   5747  C CD  . PRO B 1 367 ? 1.370   -12.562 -27.677 1.00 70.25  ? 376  PRO B CD  1 
ATOM   5748  N N   . SER B 1 368 ? 4.467   -15.975 -27.837 1.00 79.04  ? 377  SER B N   1 
ATOM   5749  C CA  . SER B 1 368 ? 5.870   -16.144 -28.192 1.00 80.65  ? 377  SER B CA  1 
ATOM   5750  C C   . SER B 1 368 ? 6.242   -15.312 -29.416 1.00 80.24  ? 377  SER B C   1 
ATOM   5751  O O   . SER B 1 368 ? 7.380   -14.895 -29.563 1.00 79.71  ? 377  SER B O   1 
ATOM   5752  C CB  . SER B 1 368 ? 6.148   -17.613 -28.468 1.00 84.46  ? 377  SER B CB  1 
ATOM   5753  O OG  . SER B 1 368 ? 5.293   -18.432 -27.687 1.00 86.66  ? 377  SER B OG  1 
ATOM   5754  N N   . GLU B 1 369 ? 5.269   -15.069 -30.288 1.00 80.88  ? 378  GLU B N   1 
ATOM   5755  C CA  . GLU B 1 369 ? 5.449   -14.230 -31.481 1.00 80.92  ? 378  GLU B CA  1 
ATOM   5756  C C   . GLU B 1 369 ? 5.980   -12.826 -31.158 1.00 77.89  ? 378  GLU B C   1 
ATOM   5757  O O   . GLU B 1 369 ? 6.520   -12.147 -32.033 1.00 77.44  ? 378  GLU B O   1 
ATOM   5758  C CB  . GLU B 1 369 ? 4.136   -14.136 -32.275 1.00 81.45  ? 378  GLU B CB  1 
ATOM   5759  C CG  . GLU B 1 369 ? 3.798   -15.376 -33.126 1.00 86.98  ? 378  GLU B CG  1 
ATOM   5760  C CD  . GLU B 1 369 ? 3.566   -16.685 -32.327 1.00 92.50  ? 378  GLU B CD  1 
ATOM   5761  O OE1 . GLU B 1 369 ? 3.481   -16.652 -31.074 1.00 91.12  ? 378  GLU B OE1 1 
ATOM   5762  O OE2 . GLU B 1 369 ? 3.464   -17.761 -32.978 1.00 97.54  ? 378  GLU B OE2 1 
ATOM   5763  N N   . VAL B 1 370 ? 5.828   -12.397 -29.908 1.00 76.12  ? 379  VAL B N   1 
ATOM   5764  C CA  . VAL B 1 370 ? 6.461   -11.175 -29.442 1.00 73.79  ? 379  VAL B CA  1 
ATOM   5765  C C   . VAL B 1 370 ? 7.943   -11.103 -29.812 1.00 74.73  ? 379  VAL B C   1 
ATOM   5766  O O   . VAL B 1 370 ? 8.445   -10.039 -30.183 1.00 73.23  ? 379  VAL B O   1 
ATOM   5767  C CB  . VAL B 1 370 ? 6.320   -11.047 -27.938 1.00 72.13  ? 379  VAL B CB  1 
ATOM   5768  C CG1 . VAL B 1 370 ? 7.491   -10.283 -27.354 1.00 70.69  ? 379  VAL B CG1 1 
ATOM   5769  C CG2 . VAL B 1 370 ? 5.022   -10.359 -27.628 1.00 70.67  ? 379  VAL B CG2 1 
ATOM   5770  N N   . ASN B 1 371 ? 8.619   -12.248 -29.723 1.00 77.91  ? 380  ASN B N   1 
ATOM   5771  C CA  . ASN B 1 371 ? 10.069  -12.359 -29.977 1.00 79.84  ? 380  ASN B CA  1 
ATOM   5772  C C   . ASN B 1 371 ? 10.556  -11.875 -31.329 1.00 80.08  ? 380  ASN B C   1 
ATOM   5773  O O   . ASN B 1 371 ? 11.639  -11.307 -31.436 1.00 79.76  ? 380  ASN B O   1 
ATOM   5774  C CB  . ASN B 1 371 ? 10.574  -13.784 -29.741 1.00 83.17  ? 380  ASN B CB  1 
ATOM   5775  C CG  . ASN B 1 371 ? 10.415  -14.221 -28.297 1.00 85.29  ? 380  ASN B CG  1 
ATOM   5776  O OD1 . ASN B 1 371 ? 11.351  -14.126 -27.506 1.00 87.85  ? 380  ASN B OD1 1 
ATOM   5777  N ND2 . ASN B 1 371 ? 9.216   -14.680 -27.937 1.00 87.70  ? 380  ASN B ND2 1 
ATOM   5778  N N   . LEU B 1 372 ? 9.764   -12.090 -32.365 1.00 80.93  ? 381  LEU B N   1 
ATOM   5779  C CA  . LEU B 1 372 ? 10.171  -11.631 -33.690 1.00 81.58  ? 381  LEU B CA  1 
ATOM   5780  C C   . LEU B 1 372 ? 10.329  -10.116 -33.711 1.00 78.73  ? 381  LEU B C   1 
ATOM   5781  O O   . LEU B 1 372 ? 10.997  -9.566  -34.593 1.00 79.19  ? 381  LEU B O   1 
ATOM   5782  C CB  . LEU B 1 372 ? 9.181   -12.062 -34.769 1.00 82.93  ? 381  LEU B CB  1 
ATOM   5783  C CG  . LEU B 1 372 ? 8.372   -13.306 -34.443 1.00 85.52  ? 381  LEU B CG  1 
ATOM   5784  C CD1 . LEU B 1 372 ? 7.222   -13.401 -35.435 1.00 86.74  ? 381  LEU B CD1 1 
ATOM   5785  C CD2 . LEU B 1 372 ? 9.241   -14.561 -34.409 1.00 89.29  ? 381  LEU B CD2 1 
ATOM   5786  N N   . CYS B 1 373 ? 9.720   -9.446  -32.742 1.00 76.06  ? 382  CYS B N   1 
ATOM   5787  C CA  . CYS B 1 373 ? 9.866   -8.025  -32.653 1.00 73.59  ? 382  CYS B CA  1 
ATOM   5788  C C   . CYS B 1 373 ? 11.280  -7.599  -32.322 1.00 73.04  ? 382  CYS B C   1 
ATOM   5789  O O   . CYS B 1 373 ? 11.647  -6.469  -32.593 1.00 71.72  ? 382  CYS B O   1 
ATOM   5790  C CB  . CYS B 1 373 ? 8.871   -7.458  -31.679 1.00 71.44  ? 382  CYS B CB  1 
ATOM   5791  S SG  . CYS B 1 373 ? 7.394   -7.058  -32.562 1.00 73.17  ? 382  CYS B SG  1 
ATOM   5792  N N   . ASN B 1 374 ? 12.089  -8.502  -31.775 1.00 74.40  ? 383  ASN B N   1 
ATOM   5793  C CA  . ASN B 1 374 ? 13.487  -8.179  -31.487 1.00 74.50  ? 383  ASN B CA  1 
ATOM   5794  C C   . ASN B 1 374 ? 14.291  -8.059  -32.751 1.00 76.13  ? 383  ASN B C   1 
ATOM   5795  O O   . ASN B 1 374 ? 15.332  -7.394  -32.773 1.00 75.83  ? 383  ASN B O   1 
ATOM   5796  C CB  . ASN B 1 374 ? 14.142  -9.253  -30.639 1.00 75.99  ? 383  ASN B CB  1 
ATOM   5797  C CG  . ASN B 1 374 ? 13.460  -9.449  -29.333 1.00 75.35  ? 383  ASN B CG  1 
ATOM   5798  O OD1 . ASN B 1 374 ? 13.086  -8.495  -28.657 1.00 73.66  ? 383  ASN B OD1 1 
ATOM   5799  N ND2 . ASN B 1 374 ? 13.292  -10.699 -28.956 1.00 78.47  ? 383  ASN B ND2 1 
ATOM   5800  N N   . VAL B 1 375 ? 13.808  -8.744  -33.789 1.00 78.20  ? 384  VAL B N   1 
ATOM   5801  C CA  . VAL B 1 375 ? 14.459  -8.807  -35.095 1.00 80.06  ? 384  VAL B CA  1 
ATOM   5802  C C   . VAL B 1 375 ? 13.843  -7.832  -36.105 1.00 79.20  ? 384  VAL B C   1 
ATOM   5803  O O   . VAL B 1 375 ? 14.557  -7.162  -36.844 1.00 79.17  ? 384  VAL B O   1 
ATOM   5804  C CB  . VAL B 1 375 ? 14.420  -10.240 -35.653 1.00 83.06  ? 384  VAL B CB  1 
ATOM   5805  C CG1 . VAL B 1 375 ? 14.745  -10.248 -37.146 1.00 85.19  ? 384  VAL B CG1 1 
ATOM   5806  C CG2 . VAL B 1 375 ? 15.366  -11.145 -34.862 1.00 84.06  ? 384  VAL B CG2 1 
ATOM   5807  N N   . ASP B 1 376 ? 12.522  -7.727  -36.122 1.00 78.67  ? 385  ASP B N   1 
ATOM   5808  C CA  . ASP B 1 376 ? 11.907  -7.014  -37.215 1.00 78.84  ? 385  ASP B CA  1 
ATOM   5809  C C   . ASP B 1 376 ? 11.019  -5.788  -36.961 1.00 76.03  ? 385  ASP B C   1 
ATOM   5810  O O   . ASP B 1 376 ? 11.157  -4.798  -37.684 1.00 75.33  ? 385  ASP B O   1 
ATOM   5811  C CB  . ASP B 1 376 ? 11.229  -8.000  -38.155 1.00 81.47  ? 385  ASP B CB  1 
ATOM   5812  C CG  . ASP B 1 376 ? 11.520  -7.687  -39.626 1.00 84.36  ? 385  ASP B CG  1 
ATOM   5813  O OD1 . ASP B 1 376 ? 12.008  -6.563  -39.914 1.00 84.42  ? 385  ASP B OD1 1 
ATOM   5814  O OD2 . ASP B 1 376 ? 11.263  -8.556  -40.500 1.00 89.09  ? 385  ASP B OD2 1 
ATOM   5815  N N   . ILE B 1 377 ? 10.118  -5.838  -35.978 1.00 74.61  ? 386  ILE B N   1 
ATOM   5816  C CA  . ILE B 1 377 ? 9.220   -4.692  -35.695 1.00 72.23  ? 386  ILE B CA  1 
ATOM   5817  C C   . ILE B 1 377 ? 8.015   -4.706  -36.650 1.00 73.20  ? 386  ILE B C   1 
ATOM   5818  O O   . ILE B 1 377 ? 6.829   -4.826  -36.243 1.00 72.44  ? 386  ILE B O   1 
ATOM   5819  C CB  . ILE B 1 377 ? 9.963   -3.322  -35.867 1.00 70.37  ? 386  ILE B CB  1 
ATOM   5820  C CG1 . ILE B 1 377 ? 10.937  -3.054  -34.721 1.00 68.51  ? 386  ILE B CG1 1 
ATOM   5821  C CG2 . ILE B 1 377 ? 8.984   -2.168  -36.002 1.00 67.96  ? 386  ILE B CG2 1 
ATOM   5822  C CD1 . ILE B 1 377 ? 12.097  -2.188  -35.128 1.00 67.19  ? 386  ILE B CD1 1 
ATOM   5823  N N   . PHE B 1 378 ? 8.353   -4.544  -37.932 1.00 74.62  ? 387  PHE B N   1 
ATOM   5824  C CA  . PHE B 1 378 ? 7.435   -4.753  -39.031 1.00 75.67  ? 387  PHE B CA  1 
ATOM   5825  C C   . PHE B 1 378 ? 7.643   -6.165  -39.430 1.00 78.46  ? 387  PHE B C   1 
ATOM   5826  O O   . PHE B 1 378 ? 8.754   -6.600  -39.710 1.00 79.87  ? 387  PHE B O   1 
ATOM   5827  C CB  . PHE B 1 378 ? 7.766   -3.829  -40.181 1.00 75.39  ? 387  PHE B CB  1 
ATOM   5828  C CG  . PHE B 1 378 ? 7.957   -2.419  -39.746 1.00 73.24  ? 387  PHE B CG  1 
ATOM   5829  C CD1 . PHE B 1 378 ? 9.230   -1.826  -39.805 1.00 73.49  ? 387  PHE B CD1 1 
ATOM   5830  C CD2 . PHE B 1 378 ? 6.876   -1.696  -39.201 1.00 70.43  ? 387  PHE B CD2 1 
ATOM   5831  C CE1 . PHE B 1 378 ? 9.409   -0.502  -39.368 1.00 70.50  ? 387  PHE B CE1 1 
ATOM   5832  C CE2 . PHE B 1 378 ? 7.035   -0.388  -38.773 1.00 68.17  ? 387  PHE B CE2 1 
ATOM   5833  C CZ  . PHE B 1 378 ? 8.299   0.217   -38.851 1.00 67.86  ? 387  PHE B CZ  1 
ATOM   5834  N N   . ASN B 1 379 ? 6.548   -6.887  -39.383 1.00 79.43  ? 388  ASN B N   1 
ATOM   5835  C CA  . ASN B 1 379 ? 6.503   -8.273  -39.732 1.00 82.64  ? 388  ASN B CA  1 
ATOM   5836  C C   . ASN B 1 379 ? 5.092   -8.633  -39.407 1.00 83.26  ? 388  ASN B C   1 
ATOM   5837  O O   . ASN B 1 379 ? 4.562   -8.194  -38.367 1.00 81.21  ? 388  ASN B O   1 
ATOM   5838  C CB  . ASN B 1 379 ? 7.462   -9.125  -38.894 1.00 83.23  ? 388  ASN B CB  1 
ATOM   5839  C CG  . ASN B 1 379 ? 7.256   -8.946  -37.411 1.00 81.17  ? 388  ASN B CG  1 
ATOM   5840  O OD1 . ASN B 1 379 ? 6.345   -9.531  -36.817 1.00 79.39  ? 388  ASN B OD1 1 
ATOM   5841  N ND2 . ASN B 1 379 ? 8.113   -8.138  -36.795 1.00 80.21  ? 388  ASN B ND2 1 
ATOM   5842  N N   . PRO B 1 380 ? 4.470   -9.418  -40.301 1.00 86.18  ? 389  PRO B N   1 
ATOM   5843  C CA  . PRO B 1 380 ? 3.196   -10.105 -40.038 1.00 87.44  ? 389  PRO B CA  1 
ATOM   5844  C C   . PRO B 1 380 ? 3.377   -10.878 -38.740 1.00 88.16  ? 389  PRO B C   1 
ATOM   5845  O O   . PRO B 1 380 ? 4.535   -11.139 -38.357 1.00 88.99  ? 389  PRO B O   1 
ATOM   5846  C CB  . PRO B 1 380 ? 3.124   -11.114 -41.173 1.00 90.64  ? 389  PRO B CB  1 
ATOM   5847  C CG  . PRO B 1 380 ? 4.628   -11.313 -41.571 1.00 91.39  ? 389  PRO B CG  1 
ATOM   5848  C CD  . PRO B 1 380 ? 5.151   -9.938  -41.502 1.00 88.35  ? 389  PRO B CD  1 
ATOM   5849  N N   . LYS B 1 381 ? 2.290   -11.265 -38.072 1.00 88.14  ? 390  LYS B N   1 
ATOM   5850  C CA  . LYS B 1 381 ? 2.447   -12.035 -36.833 1.00 88.78  ? 390  LYS B CA  1 
ATOM   5851  C C   . LYS B 1 381 ? 2.436   -11.153 -35.584 1.00 85.93  ? 390  LYS B C   1 
ATOM   5852  O O   . LYS B 1 381 ? 1.747   -11.492 -34.611 1.00 86.23  ? 390  LYS B O   1 
ATOM   5853  C CB  . LYS B 1 381 ? 3.752   -12.871 -36.835 1.00 90.64  ? 390  LYS B CB  1 
ATOM   5854  C CG  . LYS B 1 381 ? 3.733   -14.185 -37.623 1.00 94.82  ? 390  LYS B CG  1 
ATOM   5855  C CD  . LYS B 1 381 ? 3.069   -15.316 -36.807 1.00 99.03  ? 390  LYS B CD  1 
ATOM   5856  C CE  . LYS B 1 381 ? 3.632   -16.716 -37.133 1.00 103.34 ? 390  LYS B CE  1 
ATOM   5857  N NZ  . LYS B 1 381 ? 3.187   -17.305 -38.457 1.00 107.02 ? 390  LYS B NZ  1 
ATOM   5858  N N   . TYR B 1 382 ? 3.214   -10.057 -35.579 1.00 83.53  ? 391  TYR B N   1 
ATOM   5859  C CA  . TYR B 1 382 ? 3.148   -9.103  -34.458 1.00 80.35  ? 391  TYR B CA  1 
ATOM   5860  C C   . TYR B 1 382 ? 3.254   -7.625  -34.786 1.00 78.01  ? 391  TYR B C   1 
ATOM   5861  O O   . TYR B 1 382 ? 4.302   -7.127  -35.187 1.00 77.79  ? 391  TYR B O   1 
ATOM   5862  C CB  . TYR B 1 382 ? 4.123   -9.474  -33.348 1.00 79.98  ? 391  TYR B CB  1 
ATOM   5863  C CG  . TYR B 1 382 ? 3.543   -9.229  -31.985 1.00 78.00  ? 391  TYR B CG  1 
ATOM   5864  C CD1 . TYR B 1 382 ? 2.471   -9.990  -31.525 1.00 79.00  ? 391  TYR B CD1 1 
ATOM   5865  C CD2 . TYR B 1 382 ? 4.057   -8.233  -31.149 1.00 75.52  ? 391  TYR B CD2 1 
ATOM   5866  C CE1 . TYR B 1 382 ? 1.922   -9.772  -30.273 1.00 77.47  ? 391  TYR B CE1 1 
ATOM   5867  C CE2 . TYR B 1 382 ? 3.515   -7.999  -29.880 1.00 73.40  ? 391  TYR B CE2 1 
ATOM   5868  C CZ  . TYR B 1 382 ? 2.447   -8.780  -29.456 1.00 74.50  ? 391  TYR B CZ  1 
ATOM   5869  O OH  . TYR B 1 382 ? 1.884   -8.581  -28.220 1.00 73.17  ? 391  TYR B OH  1 
ATOM   5870  N N   . ASP B 1 383 ? 2.142   -6.924  -34.618 1.00 76.57  ? 392  ASP B N   1 
ATOM   5871  C CA  . ASP B 1 383 ? 2.224   -5.488  -34.491 1.00 74.29  ? 392  ASP B CA  1 
ATOM   5872  C C   . ASP B 1 383 ? 2.797   -5.178  -33.112 1.00 72.39  ? 392  ASP B C   1 
ATOM   5873  O O   . ASP B 1 383 ? 2.470   -5.800  -32.093 1.00 72.74  ? 392  ASP B O   1 
ATOM   5874  C CB  . ASP B 1 383 ? 0.917   -4.723  -34.796 1.00 73.52  ? 392  ASP B CB  1 
ATOM   5875  C CG  . ASP B 1 383 ? -0.272  -5.628  -35.031 1.00 75.82  ? 392  ASP B CG  1 
ATOM   5876  O OD1 . ASP B 1 383 ? -0.667  -6.369  -34.093 1.00 77.53  ? 392  ASP B OD1 1 
ATOM   5877  O OD2 . ASP B 1 383 ? -0.824  -5.563  -36.157 1.00 76.58  ? 392  ASP B OD2 1 
ATOM   5878  N N   . CYS B 1 384 ? 3.634   -4.166  -33.109 1.00 70.19  ? 393  CYS B N   1 
ATOM   5879  C CA  . CYS B 1 384 ? 4.802   -4.188  -32.307 1.00 69.23  ? 393  CYS B CA  1 
ATOM   5880  C C   . CYS B 1 384 ? 4.974   -2.791  -31.719 1.00 66.20  ? 393  CYS B C   1 
ATOM   5881  O O   . CYS B 1 384 ? 5.092   -1.814  -32.472 1.00 65.37  ? 393  CYS B O   1 
ATOM   5882  C CB  . CYS B 1 384 ? 5.905   -4.547  -33.286 1.00 70.65  ? 393  CYS B CB  1 
ATOM   5883  S SG  . CYS B 1 384 ? 7.430   -5.023  -32.567 1.00 73.75  ? 393  CYS B SG  1 
ATOM   5884  N N   . LYS B 1 385 ? 4.951   -2.677  -30.386 1.00 64.54  ? 394  LYS B N   1 
ATOM   5885  C CA  . LYS B 1 385 ? 4.845   -1.347  -29.759 1.00 61.86  ? 394  LYS B CA  1 
ATOM   5886  C C   . LYS B 1 385 ? 6.119   -0.543  -29.947 1.00 60.45  ? 394  LYS B C   1 
ATOM   5887  O O   . LYS B 1 385 ? 7.218   -1.053  -29.768 1.00 60.81  ? 394  LYS B O   1 
ATOM   5888  C CB  . LYS B 1 385 ? 4.354   -1.404  -28.304 1.00 60.91  ? 394  LYS B CB  1 
ATOM   5889  C CG  . LYS B 1 385 ? 3.034   -2.172  -28.162 1.00 63.98  ? 394  LYS B CG  1 
ATOM   5890  C CD  . LYS B 1 385 ? 2.382   -2.052  -26.773 1.00 68.00  ? 394  LYS B CD  1 
ATOM   5891  C CE  . LYS B 1 385 ? 3.108   -2.903  -25.675 1.00 70.79  ? 394  LYS B CE  1 
ATOM   5892  N NZ  . LYS B 1 385 ? 4.089   -2.145  -24.777 1.00 69.55  ? 394  LYS B NZ  1 
ATOM   5893  N N   . ILE B 1 386 ? 5.915   0.719   -30.320 1.00 58.62  ? 395  ILE B N   1 
ATOM   5894  C CA  . ILE B 1 386 ? 6.891   1.585   -30.934 1.00 58.01  ? 395  ILE B CA  1 
ATOM   5895  C C   . ILE B 1 386 ? 6.512   3.018   -30.644 1.00 56.21  ? 395  ILE B C   1 
ATOM   5896  O O   . ILE B 1 386 ? 5.349   3.331   -30.480 1.00 55.67  ? 395  ILE B O   1 
ATOM   5897  C CB  . ILE B 1 386 ? 6.737   1.466   -32.447 1.00 59.36  ? 395  ILE B CB  1 
ATOM   5898  C CG1 . ILE B 1 386 ? 7.452   0.235   -32.967 1.00 62.05  ? 395  ILE B CG1 1 
ATOM   5899  C CG2 . ILE B 1 386 ? 7.256   2.712   -33.195 1.00 58.46  ? 395  ILE B CG2 1 
ATOM   5900  C CD1 . ILE B 1 386 ? 7.222   0.046   -34.423 1.00 65.18  ? 395  ILE B CD1 1 
ATOM   5901  N N   . MET B 1 387 ? 7.476   3.915   -30.631 1.00 55.81  ? 396  MET B N   1 
ATOM   5902  C CA  . MET B 1 387 ? 7.111   5.309   -30.808 1.00 54.97  ? 396  MET B CA  1 
ATOM   5903  C C   . MET B 1 387 ? 7.885   6.023   -31.922 1.00 55.64  ? 396  MET B C   1 
ATOM   5904  O O   . MET B 1 387 ? 8.978   5.592   -32.358 1.00 56.85  ? 396  MET B O   1 
ATOM   5905  C CB  . MET B 1 387 ? 7.193   6.069   -29.511 1.00 53.64  ? 396  MET B CB  1 
ATOM   5906  C CG  . MET B 1 387 ? 8.576   6.373   -29.068 1.00 54.97  ? 396  MET B CG  1 
ATOM   5907  S SD  . MET B 1 387 ? 8.469   7.460   -27.664 1.00 58.23  ? 396  MET B SD  1 
ATOM   5908  C CE  . MET B 1 387 ? 6.993   6.846   -26.736 1.00 56.99  ? 396  MET B CE  1 
ATOM   5909  N N   . THR B 1 388 ? 7.298   7.128   -32.369 1.00 54.78  ? 397  THR B N   1 
ATOM   5910  C CA  . THR B 1 388 ? 7.681   7.732   -33.633 1.00 55.39  ? 397  THR B CA  1 
ATOM   5911  C C   . THR B 1 388 ? 8.305   9.088   -33.486 1.00 54.65  ? 397  THR B C   1 
ATOM   5912  O O   . THR B 1 388 ? 7.807   9.922   -32.710 1.00 53.61  ? 397  THR B O   1 
ATOM   5913  C CB  . THR B 1 388 ? 6.446   7.869   -34.511 1.00 55.45  ? 397  THR B CB  1 
ATOM   5914  O OG1 . THR B 1 388 ? 6.207   6.594   -35.087 1.00 56.85  ? 397  THR B OG1 1 
ATOM   5915  C CG2 . THR B 1 388 ? 6.655   8.870   -35.651 1.00 56.13  ? 397  THR B CG2 1 
ATOM   5916  N N   . SER B 1 389 ? 9.373   9.318   -34.245 1.00 55.35  ? 398  SER B N   1 
ATOM   5917  C CA  . SER B 1 389 ? 9.842   10.671  -34.405 1.00 54.99  ? 398  SER B CA  1 
ATOM   5918  C C   . SER B 1 389 ? 10.159  11.042  -35.847 1.00 56.44  ? 398  SER B C   1 
ATOM   5919  O O   . SER B 1 389 ? 10.762  10.269  -36.593 1.00 57.90  ? 398  SER B O   1 
ATOM   5920  C CB  . SER B 1 389 ? 11.036  10.947  -33.517 1.00 54.47  ? 398  SER B CB  1 
ATOM   5921  O OG  . SER B 1 389 ? 11.521  12.235  -33.822 1.00 54.63  ? 398  SER B OG  1 
ATOM   5922  N N   . LYS B 1 390 ? 9.749   12.253  -36.214 1.00 56.15  ? 399  LYS B N   1 
ATOM   5923  C CA  . LYS B 1 390 ? 10.118  12.867  -37.489 1.00 57.30  ? 399  LYS B CA  1 
ATOM   5924  C C   . LYS B 1 390 ? 11.622  13.238  -37.588 1.00 57.73  ? 399  LYS B C   1 
ATOM   5925  O O   . LYS B 1 390 ? 12.235  13.078  -38.636 1.00 58.93  ? 399  LYS B O   1 
ATOM   5926  C CB  . LYS B 1 390 ? 9.213   14.094  -37.716 1.00 57.01  ? 399  LYS B CB  1 
ATOM   5927  C CG  . LYS B 1 390 ? 7.887   13.788  -38.445 1.00 57.72  ? 399  LYS B CG  1 
ATOM   5928  C CD  . LYS B 1 390 ? 8.188   13.895  -39.983 1.00 62.37  ? 399  LYS B CD  1 
ATOM   5929  C CE  . LYS B 1 390 ? 6.928   13.825  -40.905 1.00 63.98  ? 399  LYS B CE  1 
ATOM   5930  N NZ  . LYS B 1 390 ? 7.342   13.980  -42.352 1.00 64.35  ? 399  LYS B NZ  1 
ATOM   5931  N N   . THR B 1 391 ? 12.195  13.698  -36.478 1.00 56.63  ? 400  THR B N   1 
ATOM   5932  C CA  . THR B 1 391 ? 13.539  14.285  -36.430 1.00 57.33  ? 400  THR B CA  1 
ATOM   5933  C C   . THR B 1 391 ? 14.532  13.349  -35.740 1.00 57.20  ? 400  THR B C   1 
ATOM   5934  O O   . THR B 1 391 ? 14.141  12.550  -34.899 1.00 56.12  ? 400  THR B O   1 
ATOM   5935  C CB  . THR B 1 391 ? 13.510  15.604  -35.615 1.00 56.55  ? 400  THR B CB  1 
ATOM   5936  O OG1 . THR B 1 391 ? 12.149  16.046  -35.475 1.00 56.38  ? 400  THR B OG1 1 
ATOM   5937  C CG2 . THR B 1 391 ? 14.387  16.701  -36.265 1.00 57.94  ? 400  THR B CG2 1 
ATOM   5938  N N   . ASP B 1 392 ? 15.812  13.464  -36.087 1.00 58.06  ? 401  ASP B N   1 
ATOM   5939  C CA  . ASP B 1 392 ? 16.860  12.687  -35.454 1.00 58.08  ? 401  ASP B CA  1 
ATOM   5940  C C   . ASP B 1 392 ? 16.907  12.964  -33.982 1.00 56.25  ? 401  ASP B C   1 
ATOM   5941  O O   . ASP B 1 392 ? 16.869  14.113  -33.561 1.00 55.72  ? 401  ASP B O   1 
ATOM   5942  C CB  . ASP B 1 392 ? 18.191  13.067  -36.043 1.00 60.09  ? 401  ASP B CB  1 
ATOM   5943  C CG  . ASP B 1 392 ? 18.429  12.439  -37.402 1.00 63.60  ? 401  ASP B CG  1 
ATOM   5944  O OD1 . ASP B 1 392 ? 17.435  12.176  -38.114 1.00 66.58  ? 401  ASP B OD1 1 
ATOM   5945  O OD2 . ASP B 1 392 ? 19.615  12.216  -37.773 1.00 66.27  ? 401  ASP B OD2 1 
ATOM   5946  N N   . VAL B 1 393 ? 16.981  11.899  -33.199 1.00 55.41  ? 402  VAL B N   1 
ATOM   5947  C CA  . VAL B 1 393 ? 17.131  11.989  -31.754 1.00 53.43  ? 402  VAL B CA  1 
ATOM   5948  C C   . VAL B 1 393 ? 18.273  11.083  -31.391 1.00 53.92  ? 402  VAL B C   1 
ATOM   5949  O O   . VAL B 1 393 ? 18.233  9.924   -31.775 1.00 54.96  ? 402  VAL B O   1 
ATOM   5950  C CB  . VAL B 1 393 ? 15.916  11.407  -31.055 1.00 51.91  ? 402  VAL B CB  1 
ATOM   5951  C CG1 . VAL B 1 393 ? 16.152  11.334  -29.563 1.00 51.79  ? 402  VAL B CG1 1 
ATOM   5952  C CG2 . VAL B 1 393 ? 14.728  12.271  -31.297 1.00 51.47  ? 402  VAL B CG2 1 
ATOM   5953  N N   . SER B 1 394 ? 19.265  11.567  -30.642 1.00 52.98  ? 403  SER B N   1 
ATOM   5954  C CA  . SER B 1 394 ? 20.412  10.730  -30.315 1.00 53.37  ? 403  SER B CA  1 
ATOM   5955  C C   . SER B 1 394 ? 20.403  10.513  -28.849 1.00 51.33  ? 403  SER B C   1 
ATOM   5956  O O   . SER B 1 394 ? 20.109  11.443  -28.151 1.00 50.12  ? 403  SER B O   1 
ATOM   5957  C CB  . SER B 1 394 ? 21.688  11.460  -30.695 1.00 54.71  ? 403  SER B CB  1 
ATOM   5958  O OG  . SER B 1 394 ? 21.419  12.449  -31.679 1.00 55.90  ? 403  SER B OG  1 
ATOM   5959  N N   . SER B 1 395 ? 20.687  9.305   -28.370 1.00 51.33  ? 404  SER B N   1 
ATOM   5960  C CA  . SER B 1 395 ? 21.019  9.118   -26.930 1.00 50.50  ? 404  SER B CA  1 
ATOM   5961  C C   . SER B 1 395 ? 21.620  7.752   -26.548 1.00 51.13  ? 404  SER B C   1 
ATOM   5962  O O   . SER B 1 395 ? 22.008  6.974   -27.432 1.00 52.73  ? 404  SER B O   1 
ATOM   5963  C CB  . SER B 1 395 ? 19.843  9.469   -25.994 1.00 48.35  ? 404  SER B CB  1 
ATOM   5964  O OG  . SER B 1 395 ? 19.235  8.295   -25.501 1.00 48.72  ? 404  SER B OG  1 
ATOM   5965  N N   . SER B 1 396 ? 21.696  7.470   -25.240 1.00 49.51  ? 405  SER B N   1 
ATOM   5966  C CA  . SER B 1 396 ? 22.280  6.224   -24.777 1.00 50.15  ? 405  SER B CA  1 
ATOM   5967  C C   . SER B 1 396 ? 21.487  5.561   -23.685 1.00 48.91  ? 405  SER B C   1 
ATOM   5968  O O   . SER B 1 396 ? 20.832  6.237   -22.923 1.00 47.62  ? 405  SER B O   1 
ATOM   5969  C CB  . SER B 1 396 ? 23.690  6.462   -24.298 1.00 50.76  ? 405  SER B CB  1 
ATOM   5970  O OG  . SER B 1 396 ? 24.054  5.430   -23.420 1.00 50.51  ? 405  SER B OG  1 
ATOM   5971  N N   . VAL B 1 397 ? 21.579  4.235   -23.605 1.00 49.93  ? 406  VAL B N   1 
ATOM   5972  C CA  . VAL B 1 397 ? 20.774  3.426   -22.697 1.00 49.49  ? 406  VAL B CA  1 
ATOM   5973  C C   . VAL B 1 397 ? 21.611  2.336   -22.080 1.00 50.61  ? 406  VAL B C   1 
ATOM   5974  O O   . VAL B 1 397 ? 22.164  1.522   -22.781 1.00 52.65  ? 406  VAL B O   1 
ATOM   5975  C CB  . VAL B 1 397 ? 19.669  2.711   -23.449 1.00 49.96  ? 406  VAL B CB  1 
ATOM   5976  C CG1 . VAL B 1 397 ? 18.605  2.186   -22.477 1.00 49.89  ? 406  VAL B CG1 1 
ATOM   5977  C CG2 . VAL B 1 397 ? 19.052  3.632   -24.481 1.00 50.33  ? 406  VAL B CG2 1 
ATOM   5978  N N   . ILE B 1 398 ? 21.672  2.281   -20.763 1.00 49.82  ? 407  ILE B N   1 
ATOM   5979  C CA  . ILE B 1 398 ? 22.547  1.314   -20.124 1.00 51.05  ? 407  ILE B CA  1 
ATOM   5980  C C   . ILE B 1 398 ? 21.898  0.001   -19.772 1.00 52.30  ? 407  ILE B C   1 
ATOM   5981  O O   . ILE B 1 398 ? 20.878  -0.034  -19.078 1.00 51.44  ? 407  ILE B O   1 
ATOM   5982  C CB  . ILE B 1 398 ? 23.120  1.865   -18.882 1.00 49.59  ? 407  ILE B CB  1 
ATOM   5983  C CG1 . ILE B 1 398 ? 24.059  2.997   -19.275 1.00 49.32  ? 407  ILE B CG1 1 
ATOM   5984  C CG2 . ILE B 1 398 ? 23.811  0.744   -18.116 1.00 50.32  ? 407  ILE B CG2 1 
ATOM   5985  C CD1 . ILE B 1 398 ? 24.707  3.690   -18.130 1.00 50.15  ? 407  ILE B CD1 1 
ATOM   5986  N N   . THR B 1 399 ? 22.529  -1.079  -20.211 1.00 54.87  ? 408  THR B N   1 
ATOM   5987  C CA  . THR B 1 399 ? 21.973  -2.401  -20.030 1.00 56.42  ? 408  THR B CA  1 
ATOM   5988  C C   . THR B 1 399 ? 22.607  -3.160  -18.872 1.00 57.38  ? 408  THR B C   1 
ATOM   5989  O O   . THR B 1 399 ? 23.507  -2.653  -18.188 1.00 57.39  ? 408  THR B O   1 
ATOM   5990  C CB  . THR B 1 399 ? 22.138  -3.205  -21.283 1.00 58.62  ? 408  THR B CB  1 
ATOM   5991  O OG1 . THR B 1 399 ? 23.513  -3.224  -21.631 1.00 60.80  ? 408  THR B OG1 1 
ATOM   5992  C CG2 . THR B 1 399 ? 21.416  -2.561  -22.399 1.00 58.41  ? 408  THR B CG2 1 
ATOM   5993  N N   . SER B 1 400 ? 22.120  -4.383  -18.666 1.00 58.76  ? 409  SER B N   1 
ATOM   5994  C CA  . SER B 1 400 ? 22.559  -5.246  -17.576 1.00 59.86  ? 409  SER B CA  1 
ATOM   5995  C C   . SER B 1 400 ? 24.043  -5.489  -17.701 1.00 61.48  ? 409  SER B C   1 
ATOM   5996  O O   . SER B 1 400 ? 24.764  -5.531  -16.708 1.00 61.54  ? 409  SER B O   1 
ATOM   5997  C CB  . SER B 1 400 ? 21.851  -6.610  -17.637 1.00 61.54  ? 409  SER B CB  1 
ATOM   5998  O OG  . SER B 1 400 ? 20.436  -6.512  -17.604 1.00 61.39  ? 409  SER B OG  1 
ATOM   5999  N N   . LEU B 1 401 ? 24.487  -5.621  -18.943 1.00 62.94  ? 410  LEU B N   1 
ATOM   6000  C CA  . LEU B 1 401 ? 25.766  -6.228  -19.221 1.00 65.45  ? 410  LEU B CA  1 
ATOM   6001  C C   . LEU B 1 401 ? 26.626  -5.424  -20.209 1.00 65.95  ? 410  LEU B C   1 
ATOM   6002  O O   . LEU B 1 401 ? 27.734  -5.844  -20.589 1.00 68.09  ? 410  LEU B O   1 
ATOM   6003  C CB  . LEU B 1 401 ? 25.517  -7.639  -19.733 1.00 67.99  ? 410  LEU B CB  1 
ATOM   6004  C CG  . LEU B 1 401 ? 26.171  -8.771  -18.944 1.00 69.79  ? 410  LEU B CG  1 
ATOM   6005  C CD1 . LEU B 1 401 ? 25.774  -8.731  -17.464 1.00 69.16  ? 410  LEU B CD1 1 
ATOM   6006  C CD2 . LEU B 1 401 ? 25.784  -10.095 -19.573 1.00 71.73  ? 410  LEU B CD2 1 
ATOM   6007  N N   . GLY B 1 402 ? 26.107  -4.262  -20.602 1.00 63.90  ? 411  GLY B N   1 
ATOM   6008  C CA  . GLY B 1 402 ? 26.839  -3.274  -21.402 1.00 63.33  ? 411  GLY B CA  1 
ATOM   6009  C C   . GLY B 1 402 ? 26.023  -2.000  -21.550 1.00 60.41  ? 411  GLY B C   1 
ATOM   6010  O O   . GLY B 1 402 ? 25.352  -1.557  -20.603 1.00 58.28  ? 411  GLY B O   1 
ATOM   6011  N N   . ALA B 1 403 ? 26.057  -1.429  -22.749 1.00 60.16  ? 412  ALA B N   1 
ATOM   6012  C CA  . ALA B 1 403 ? 25.284  -0.240  -23.048 1.00 57.60  ? 412  ALA B CA  1 
ATOM   6013  C C   . ALA B 1 403 ? 24.991  -0.139  -24.525 1.00 58.34  ? 412  ALA B C   1 
ATOM   6014  O O   . ALA B 1 403 ? 25.670  -0.729  -25.344 1.00 60.41  ? 412  ALA B O   1 
ATOM   6015  C CB  . ALA B 1 403 ? 26.016  0.989   -22.581 1.00 56.37  ? 412  ALA B CB  1 
ATOM   6016  N N   . ILE B 1 404 ? 23.947  0.607   -24.841 1.00 56.89  ? 413  ILE B N   1 
ATOM   6017  C CA  . ILE B 1 404 ? 23.588  0.925   -26.202 1.00 57.56  ? 413  ILE B CA  1 
ATOM   6018  C C   . ILE B 1 404 ? 23.797  2.407   -26.389 1.00 56.80  ? 413  ILE B C   1 
ATOM   6019  O O   . ILE B 1 404 ? 23.738  3.188   -25.447 1.00 54.97  ? 413  ILE B O   1 
ATOM   6020  C CB  . ILE B 1 404 ? 22.122  0.626   -26.510 1.00 56.45  ? 413  ILE B CB  1 
ATOM   6021  C CG1 . ILE B 1 404 ? 21.828  -0.859  -26.335 1.00 57.47  ? 413  ILE B CG1 1 
ATOM   6022  C CG2 . ILE B 1 404 ? 21.791  1.066   -27.908 1.00 56.98  ? 413  ILE B CG2 1 
ATOM   6023  C CD1 . ILE B 1 404 ? 20.456  -1.296  -26.832 1.00 57.97  ? 413  ILE B CD1 1 
ATOM   6024  N N   . VAL B 1 405 ? 24.050  2.782   -27.628 1.00 58.47  ? 414  VAL B N   1 
ATOM   6025  C CA  . VAL B 1 405 ? 24.243  4.167   -27.974 1.00 58.32  ? 414  VAL B CA  1 
ATOM   6026  C C   . VAL B 1 405 ? 23.765  4.446   -29.400 1.00 59.37  ? 414  VAL B C   1 
ATOM   6027  O O   . VAL B 1 405 ? 24.228  3.843   -30.387 1.00 61.60  ? 414  VAL B O   1 
ATOM   6028  C CB  . VAL B 1 405 ? 25.704  4.618   -27.741 1.00 59.22  ? 414  VAL B CB  1 
ATOM   6029  C CG1 . VAL B 1 405 ? 26.681  3.523   -28.121 1.00 62.08  ? 414  VAL B CG1 1 
ATOM   6030  C CG2 . VAL B 1 405 ? 26.002  5.912   -28.489 1.00 59.54  ? 414  VAL B CG2 1 
ATOM   6031  N N   . SER B 1 406 ? 22.807  5.360   -29.474 1.00 57.93  ? 415  SER B N   1 
ATOM   6032  C CA  . SER B 1 406 ? 22.236  5.790   -30.723 1.00 58.54  ? 415  SER B CA  1 
ATOM   6033  C C   . SER B 1 406 ? 22.782  7.162   -31.040 1.00 58.80  ? 415  SER B C   1 
ATOM   6034  O O   . SER B 1 406 ? 22.307  8.160   -30.498 1.00 57.34  ? 415  SER B O   1 
ATOM   6035  C CB  . SER B 1 406 ? 20.728  5.864   -30.581 1.00 56.67  ? 415  SER B CB  1 
ATOM   6036  O OG  . SER B 1 406 ? 20.206  4.644   -30.101 1.00 56.81  ? 415  SER B OG  1 
ATOM   6037  N N   . CYS B 1 407 ? 23.788  7.207   -31.903 1.00 61.12  ? 416  CYS B N   1 
ATOM   6038  C CA  . CYS B 1 407 ? 24.395  8.470   -32.284 1.00 61.83  ? 416  CYS B CA  1 
ATOM   6039  C C   . CYS B 1 407 ? 23.939  8.918   -33.660 1.00 62.39  ? 416  CYS B C   1 
ATOM   6040  O O   . CYS B 1 407 ? 24.261  8.305   -34.658 1.00 64.36  ? 416  CYS B O   1 
ATOM   6041  C CB  . CYS B 1 407 ? 25.910  8.373   -32.262 1.00 63.85  ? 416  CYS B CB  1 
ATOM   6042  S SG  . CYS B 1 407 ? 26.645  9.921   -31.756 1.00 65.24  ? 416  CYS B SG  1 
ATOM   6043  N N   . TYR B 1 408 ? 23.195  10.009  -33.705 1.00 61.02  ? 417  TYR B N   1 
ATOM   6044  C CA  . TYR B 1 408 ? 22.568  10.442  -34.929 1.00 61.08  ? 417  TYR B CA  1 
ATOM   6045  C C   . TYR B 1 408 ? 22.638  11.942  -35.148 1.00 60.79  ? 417  TYR B C   1 
ATOM   6046  O O   . TYR B 1 408 ? 22.902  12.709  -34.226 1.00 60.02  ? 417  TYR B O   1 
ATOM   6047  C CB  . TYR B 1 408 ? 21.135  10.020  -34.883 1.00 59.57  ? 417  TYR B CB  1 
ATOM   6048  C CG  . TYR B 1 408 ? 20.914  8.560   -35.116 1.00 60.36  ? 417  TYR B CG  1 
ATOM   6049  C CD1 . TYR B 1 408 ? 20.094  7.821   -34.277 1.00 59.29  ? 417  TYR B CD1 1 
ATOM   6050  C CD2 . TYR B 1 408 ? 21.488  7.918   -36.188 1.00 63.27  ? 417  TYR B CD2 1 
ATOM   6051  C CE1 . TYR B 1 408 ? 19.839  6.475   -34.507 1.00 60.85  ? 417  TYR B CE1 1 
ATOM   6052  C CE2 . TYR B 1 408 ? 21.250  6.568   -36.423 1.00 64.67  ? 417  TYR B CE2 1 
ATOM   6053  C CZ  . TYR B 1 408 ? 20.416  5.855   -35.582 1.00 63.47  ? 417  TYR B CZ  1 
ATOM   6054  O OH  . TYR B 1 408 ? 20.161  4.522   -35.804 1.00 65.54  ? 417  TYR B OH  1 
ATOM   6055  N N   . GLY B 1 409 ? 22.392  12.363  -36.378 1.00 61.75  ? 418  GLY B N   1 
ATOM   6056  C CA  . GLY B 1 409 ? 22.581  13.759  -36.747 1.00 62.23  ? 418  GLY B CA  1 
ATOM   6057  C C   . GLY B 1 409 ? 23.971  14.320  -36.433 1.00 63.62  ? 418  GLY B C   1 
ATOM   6058  O O   . GLY B 1 409 ? 25.014  13.699  -36.692 1.00 65.38  ? 418  GLY B O   1 
ATOM   6059  N N   . LYS B 1 410 ? 23.979  15.506  -35.849 1.00 63.00  ? 419  LYS B N   1 
ATOM   6060  C CA  . LYS B 1 410 ? 25.220  16.210  -35.563 1.00 64.55  ? 419  LYS B CA  1 
ATOM   6061  C C   . LYS B 1 410 ? 25.949  15.760  -34.290 1.00 63.79  ? 419  LYS B C   1 
ATOM   6062  O O   . LYS B 1 410 ? 27.032  16.259  -33.997 1.00 64.75  ? 419  LYS B O   1 
ATOM   6063  C CB  . LYS B 1 410 ? 24.914  17.704  -35.429 1.00 64.44  ? 419  LYS B CB  1 
ATOM   6064  C CG  . LYS B 1 410 ? 24.947  18.474  -36.732 1.00 67.53  ? 419  LYS B CG  1 
ATOM   6065  C CD  . LYS B 1 410 ? 25.271  19.942  -36.434 1.00 70.89  ? 419  LYS B CD  1 
ATOM   6066  C CE  . LYS B 1 410 ? 25.773  20.653  -37.677 1.00 74.57  ? 419  LYS B CE  1 
ATOM   6067  N NZ  . LYS B 1 410 ? 24.745  20.559  -38.767 1.00 76.29  ? 419  LYS B NZ  1 
ATOM   6068  N N   . THR B 1 411 ? 25.361  14.853  -33.520 1.00 62.01  ? 420  THR B N   1 
ATOM   6069  C CA  . THR B 1 411 ? 25.882  14.592  -32.180 1.00 61.07  ? 420  THR B CA  1 
ATOM   6070  C C   . THR B 1 411 ? 27.116  13.701  -32.148 1.00 62.95  ? 420  THR B C   1 
ATOM   6071  O O   . THR B 1 411 ? 27.250  12.816  -32.995 1.00 64.69  ? 420  THR B O   1 
ATOM   6072  C CB  . THR B 1 411 ? 24.781  14.071  -31.245 1.00 58.70  ? 420  THR B CB  1 
ATOM   6073  O OG1 . THR B 1 411 ? 23.661  13.666  -32.028 1.00 57.72  ? 420  THR B OG1 1 
ATOM   6074  C CG2 . THR B 1 411 ? 24.316  15.198  -30.309 1.00 56.46  ? 420  THR B CG2 1 
ATOM   6075  N N   . LYS B 1 412 ? 28.010  13.958  -31.189 1.00 62.91  ? 421  LYS B N   1 
ATOM   6076  C CA  . LYS B 1 412 ? 29.246  13.189  -31.033 1.00 65.01  ? 421  LYS B CA  1 
ATOM   6077  C C   . LYS B 1 412 ? 29.182  12.192  -29.894 1.00 63.83  ? 421  LYS B C   1 
ATOM   6078  O O   . LYS B 1 412 ? 28.770  12.549  -28.792 1.00 62.12  ? 421  LYS B O   1 
ATOM   6079  C CB  . LYS B 1 412 ? 30.417  14.123  -30.762 1.00 66.41  ? 421  LYS B CB  1 
ATOM   6080  C CG  . LYS B 1 412 ? 31.266  14.409  -31.970 1.00 71.22  ? 421  LYS B CG  1 
ATOM   6081  C CD  . LYS B 1 412 ? 32.220  15.544  -31.684 1.00 75.13  ? 421  LYS B CD  1 
ATOM   6082  C CE  . LYS B 1 412 ? 32.541  16.268  -32.994 1.00 77.48  ? 421  LYS B CE  1 
ATOM   6083  N NZ  . LYS B 1 412 ? 33.294  17.531  -32.711 1.00 79.67  ? 421  LYS B NZ  1 
ATOM   6084  N N   . CYS B 1 413 ? 29.626  10.958  -30.147 1.00 64.90  ? 422  CYS B N   1 
ATOM   6085  C CA  . CYS B 1 413 ? 29.571  9.891   -29.140 1.00 63.98  ? 422  CYS B CA  1 
ATOM   6086  C C   . CYS B 1 413 ? 30.883  9.118   -28.973 1.00 65.71  ? 422  CYS B C   1 
ATOM   6087  O O   . CYS B 1 413 ? 31.601  8.894   -29.920 1.00 68.16  ? 422  CYS B O   1 
ATOM   6088  C CB  . CYS B 1 413 ? 28.410  8.938   -29.422 1.00 63.39  ? 422  CYS B CB  1 
ATOM   6089  S SG  . CYS B 1 413 ? 26.788  9.751   -29.704 1.00 62.66  ? 422  CYS B SG  1 
ATOM   6090  N N   . THR B 1 414 ? 31.149  8.675   -27.754 1.00 64.79  ? 423  THR B N   1 
ATOM   6091  C CA  . THR B 1 414 ? 32.471  8.313   -27.298 1.00 66.17  ? 423  THR B CA  1 
ATOM   6092  C C   . THR B 1 414 ? 32.383  7.231   -26.257 1.00 65.70  ? 423  THR B C   1 
ATOM   6093  O O   . THR B 1 414 ? 31.806  7.439   -25.211 1.00 64.10  ? 423  THR B O   1 
ATOM   6094  C CB  . THR B 1 414 ? 33.058  9.500   -26.538 1.00 65.28  ? 423  THR B CB  1 
ATOM   6095  O OG1 . THR B 1 414 ? 33.280  10.579  -27.441 1.00 65.75  ? 423  THR B OG1 1 
ATOM   6096  C CG2 . THR B 1 414 ? 34.333  9.129   -25.867 1.00 67.18  ? 423  THR B CG2 1 
ATOM   6097  N N   . ALA B 1 415 ? 32.990  6.091   -26.495 1.00 67.59  ? 424  ALA B N   1 
ATOM   6098  C CA  . ALA B 1 415 ? 33.135  5.141   -25.410 1.00 67.23  ? 424  ALA B CA  1 
ATOM   6099  C C   . ALA B 1 415 ? 34.551  5.223   -24.862 1.00 68.81  ? 424  ALA B C   1 
ATOM   6100  O O   . ALA B 1 415 ? 35.497  5.118   -25.623 1.00 71.67  ? 424  ALA B O   1 
ATOM   6101  C CB  . ALA B 1 415 ? 32.824  3.753   -25.889 1.00 68.43  ? 424  ALA B CB  1 
ATOM   6102  N N   . SER B 1 416 ? 34.715  5.430   -23.559 1.00 67.54  ? 425  SER B N   1 
ATOM   6103  C CA  . SER B 1 416 ? 36.059  5.454   -22.963 1.00 69.01  ? 425  SER B CA  1 
ATOM   6104  C C   . SER B 1 416 ? 36.232  4.284   -22.000 1.00 69.59  ? 425  SER B C   1 
ATOM   6105  O O   . SER B 1 416 ? 35.235  3.788   -21.425 1.00 67.54  ? 425  SER B O   1 
ATOM   6106  C CB  . SER B 1 416 ? 36.328  6.780   -22.266 1.00 67.56  ? 425  SER B CB  1 
ATOM   6107  O OG  . SER B 1 416 ? 35.675  7.829   -22.944 1.00 66.33  ? 425  SER B OG  1 
ATOM   6108  N N   . ASN B 1 417 ? 37.487  3.835   -21.843 1.00 72.46  ? 426  ASN B N   1 
ATOM   6109  C CA  . ASN B 1 417 ? 37.790  2.660   -21.021 1.00 73.93  ? 426  ASN B CA  1 
ATOM   6110  C C   . ASN B 1 417 ? 37.889  3.008   -19.555 1.00 73.38  ? 426  ASN B C   1 
ATOM   6111  O O   . ASN B 1 417 ? 37.677  4.166   -19.150 1.00 71.50  ? 426  ASN B O   1 
ATOM   6112  C CB  . ASN B 1 417 ? 39.067  1.943   -21.455 1.00 76.72  ? 426  ASN B CB  1 
ATOM   6113  C CG  . ASN B 1 417 ? 40.336  2.578   -20.855 1.00 77.52  ? 426  ASN B CG  1 
ATOM   6114  O OD1 . ASN B 1 417 ? 40.261  3.258   -19.852 1.00 74.43  ? 426  ASN B OD1 1 
ATOM   6115  N ND2 . ASN B 1 417 ? 41.505  2.361   -21.487 1.00 80.30  ? 426  ASN B ND2 1 
ATOM   6116  N N   . LYS B 1 418 ? 38.199  1.970   -18.778 1.00 75.70  ? 427  LYS B N   1 
ATOM   6117  C CA  . LYS B 1 418 ? 38.480  2.045   -17.338 1.00 76.04  ? 427  LYS B CA  1 
ATOM   6118  C C   . LYS B 1 418 ? 39.123  3.371   -16.851 1.00 75.38  ? 427  LYS B C   1 
ATOM   6119  O O   . LYS B 1 418 ? 38.612  4.031   -15.930 1.00 72.42  ? 427  LYS B O   1 
ATOM   6120  C CB  . LYS B 1 418 ? 39.413  0.874   -16.976 1.00 79.23  ? 427  LYS B CB  1 
ATOM   6121  C CG  . LYS B 1 418 ? 38.797  -0.290  -16.137 1.00 80.99  ? 427  LYS B CG  1 
ATOM   6122  C CD  . LYS B 1 418 ? 39.957  -1.070  -15.360 1.00 85.57  ? 427  LYS B CD  1 
ATOM   6123  C CE  . LYS B 1 418 ? 39.446  -2.138  -14.360 1.00 86.25  ? 427  LYS B CE  1 
ATOM   6124  N NZ  . LYS B 1 418 ? 38.297  -1.657  -13.514 1.00 83.92  ? 427  LYS B NZ  1 
ATOM   6125  N N   . ASN B 1 419 ? 40.263  3.712   -17.474 1.00 78.16  ? 428  ASN B N   1 
ATOM   6126  C CA  . ASN B 1 419 ? 41.081  4.915   -17.156 1.00 78.58  ? 428  ASN B CA  1 
ATOM   6127  C C   . ASN B 1 419 ? 40.698  6.204   -17.909 1.00 78.19  ? 428  ASN B C   1 
ATOM   6128  O O   . ASN B 1 419 ? 41.369  7.254   -17.716 1.00 78.83  ? 428  ASN B O   1 
ATOM   6129  C CB  . ASN B 1 419 ? 42.593  4.652   -17.372 1.00 81.37  ? 428  ASN B CB  1 
ATOM   6130  C CG  . ASN B 1 419 ? 42.851  3.349   -18.066 1.00 82.33  ? 428  ASN B CG  1 
ATOM   6131  O OD1 . ASN B 1 419 ? 42.755  2.288   -17.438 1.00 79.43  ? 428  ASN B OD1 1 
ATOM   6132  N ND2 . ASN B 1 419 ? 43.154  3.406   -19.369 1.00 83.36  ? 428  ASN B ND2 1 
ATOM   6133  N N   . ARG B 1 420 ? 39.650  6.122   -18.755 1.00 77.23  ? 429  ARG B N   1 
ATOM   6134  C CA  . ARG B 1 420 ? 39.139  7.268   -19.541 1.00 76.22  ? 429  ARG B CA  1 
ATOM   6135  C C   . ARG B 1 420 ? 39.806  7.451   -20.931 1.00 78.43  ? 429  ARG B C   1 
ATOM   6136  O O   . ARG B 1 420 ? 39.274  8.224   -21.748 1.00 78.48  ? 429  ARG B O   1 
ATOM   6137  C CB  . ARG B 1 420 ? 39.172  8.589   -18.735 1.00 74.74  ? 429  ARG B CB  1 
ATOM   6138  C CG  . ARG B 1 420 ? 38.367  8.571   -17.475 1.00 73.00  ? 429  ARG B CG  1 
ATOM   6139  C CD  . ARG B 1 420 ? 37.129  9.379   -17.674 1.00 74.59  ? 429  ARG B CD  1 
ATOM   6140  N NE  . ARG B 1 420 ? 36.151  9.167   -16.596 1.00 75.96  ? 429  ARG B NE  1 
ATOM   6141  C CZ  . ARG B 1 420 ? 36.276  9.544   -15.306 1.00 76.09  ? 429  ARG B CZ  1 
ATOM   6142  N NH1 . ARG B 1 420 ? 37.372  10.172  -14.846 1.00 76.47  ? 429  ARG B NH1 1 
ATOM   6143  N NH2 . ARG B 1 420 ? 35.273  9.282   -14.459 1.00 74.43  ? 429  ARG B NH2 1 
ATOM   6144  N N   . GLY B 1 421 ? 40.937  6.770   -21.211 1.00 80.45  ? 430  GLY B N   1 
ATOM   6145  C CA  . GLY B 1 421 ? 41.379  6.609   -22.609 1.00 81.85  ? 430  GLY B CA  1 
ATOM   6146  C C   . GLY B 1 421 ? 40.119  6.310   -23.460 1.00 80.13  ? 430  GLY B C   1 
ATOM   6147  O O   . GLY B 1 421 ? 39.330  5.411   -23.136 1.00 79.15  ? 430  GLY B O   1 
ATOM   6148  N N   . ILE B 1 422 ? 39.888  7.083   -24.517 1.00 79.56  ? 431  ILE B N   1 
ATOM   6149  C CA  . ILE B 1 422 ? 38.730  6.881   -25.412 1.00 77.84  ? 431  ILE B CA  1 
ATOM   6150  C C   . ILE B 1 422 ? 38.961  5.719   -26.361 1.00 79.96  ? 431  ILE B C   1 
ATOM   6151  O O   . ILE B 1 422 ? 39.935  5.743   -27.091 1.00 82.66  ? 431  ILE B O   1 
ATOM   6152  C CB  . ILE B 1 422 ? 38.511  8.151   -26.270 1.00 77.48  ? 431  ILE B CB  1 
ATOM   6153  C CG1 . ILE B 1 422 ? 37.985  9.294   -25.397 1.00 75.39  ? 431  ILE B CG1 1 
ATOM   6154  C CG2 . ILE B 1 422 ? 37.620  7.882   -27.472 1.00 76.67  ? 431  ILE B CG2 1 
ATOM   6155  C CD1 . ILE B 1 422 ? 39.020  10.358  -25.074 1.00 77.41  ? 431  ILE B CD1 1 
ATOM   6156  N N   . ILE B 1 423 ? 38.099  4.707   -26.374 1.00 79.32  ? 432  ILE B N   1 
ATOM   6157  C CA  . ILE B 1 423 ? 38.317  3.572   -27.296 1.00 82.43  ? 432  ILE B CA  1 
ATOM   6158  C C   . ILE B 1 423 ? 37.595  3.673   -28.644 1.00 82.76  ? 432  ILE B C   1 
ATOM   6159  O O   . ILE B 1 423 ? 38.190  3.457   -29.727 1.00 85.71  ? 432  ILE B O   1 
ATOM   6160  C CB  . ILE B 1 423 ? 37.986  2.154   -26.710 1.00 82.52  ? 432  ILE B CB  1 
ATOM   6161  C CG1 . ILE B 1 423 ? 38.004  2.113   -25.180 1.00 81.16  ? 432  ILE B CG1 1 
ATOM   6162  C CG2 . ILE B 1 423 ? 38.940  1.072   -27.354 1.00 87.03  ? 432  ILE B CG2 1 
ATOM   6163  C CD1 . ILE B 1 423 ? 37.438  0.807   -24.620 1.00 82.12  ? 432  ILE B CD1 1 
ATOM   6164  N N   . LYS B 1 424 ? 36.302  3.929   -28.578 1.00 80.18  ? 433  LYS B N   1 
ATOM   6165  C CA  . LYS B 1 424 ? 35.513  3.918   -29.776 1.00 80.67  ? 433  LYS B CA  1 
ATOM   6166  C C   . LYS B 1 424 ? 35.042  5.335   -29.992 1.00 78.56  ? 433  LYS B C   1 
ATOM   6167  O O   . LYS B 1 424 ? 35.068  6.145   -29.078 1.00 76.74  ? 433  LYS B O   1 
ATOM   6168  C CB  . LYS B 1 424 ? 34.368  2.883   -29.670 1.00 79.85  ? 433  LYS B CB  1 
ATOM   6169  C CG  . LYS B 1 424 ? 33.647  2.594   -30.989 1.00 82.45  ? 433  LYS B CG  1 
ATOM   6170  C CD  . LYS B 1 424 ? 32.977  1.228   -31.048 1.00 85.40  ? 433  LYS B CD  1 
ATOM   6171  C CE  . LYS B 1 424 ? 32.126  1.138   -32.337 1.00 87.37  ? 433  LYS B CE  1 
ATOM   6172  N NZ  . LYS B 1 424 ? 32.309  -0.107  -33.190 1.00 90.90  ? 433  LYS B NZ  1 
ATOM   6173  N N   . THR B 1 425 ? 34.666  5.647   -31.219 1.00 79.02  ? 434  THR B N   1 
ATOM   6174  C CA  . THR B 1 425 ? 34.039  6.918   -31.515 1.00 77.37  ? 434  THR B CA  1 
ATOM   6175  C C   . THR B 1 425 ? 33.009  6.649   -32.620 1.00 77.26  ? 434  THR B C   1 
ATOM   6176  O O   . THR B 1 425 ? 33.262  5.844   -33.513 1.00 79.63  ? 434  THR B O   1 
ATOM   6177  C CB  . THR B 1 425 ? 35.099  8.016   -31.779 1.00 78.59  ? 434  THR B CB  1 
ATOM   6178  O OG1 . THR B 1 425 ? 34.486  9.130   -32.423 1.00 77.44  ? 434  THR B OG1 1 
ATOM   6179  C CG2 . THR B 1 425 ? 36.270  7.477   -32.596 1.00 82.65  ? 434  THR B CG2 1 
ATOM   6180  N N   . PHE B 1 426 ? 31.843  7.283   -32.539 1.00 75.07  ? 435  PHE B N   1 
ATOM   6181  C CA  . PHE B 1 426 ? 30.626  6.638   -33.040 1.00 74.95  ? 435  PHE B CA  1 
ATOM   6182  C C   . PHE B 1 426 ? 30.050  7.002   -34.385 1.00 76.32  ? 435  PHE B C   1 
ATOM   6183  O O   . PHE B 1 426 ? 29.581  8.120   -34.626 1.00 75.37  ? 435  PHE B O   1 
ATOM   6184  C CB  . PHE B 1 426 ? 29.528  6.650   -31.980 1.00 71.93  ? 435  PHE B CB  1 
ATOM   6185  C CG  . PHE B 1 426 ? 29.637  5.516   -31.008 1.00 71.14  ? 435  PHE B CG  1 
ATOM   6186  C CD1 . PHE B 1 426 ? 29.903  5.752   -29.658 1.00 68.71  ? 435  PHE B CD1 1 
ATOM   6187  C CD2 . PHE B 1 426 ? 29.518  4.203   -31.451 1.00 72.21  ? 435  PHE B CD2 1 
ATOM   6188  C CE1 . PHE B 1 426 ? 30.029  4.706   -28.760 1.00 67.27  ? 435  PHE B CE1 1 
ATOM   6189  C CE2 . PHE B 1 426 ? 29.632  3.157   -30.552 1.00 71.82  ? 435  PHE B CE2 1 
ATOM   6190  C CZ  . PHE B 1 426 ? 29.889  3.414   -29.197 1.00 68.99  ? 435  PHE B CZ  1 
ATOM   6191  N N   . SER B 1 427 ? 30.014  5.988   -35.230 1.00 79.01  ? 436  SER B N   1 
ATOM   6192  C CA  . SER B 1 427 ? 29.694  6.173   -36.622 1.00 81.04  ? 436  SER B CA  1 
ATOM   6193  C C   . SER B 1 427 ? 28.202  6.367   -36.873 1.00 79.20  ? 436  SER B C   1 
ATOM   6194  O O   . SER B 1 427 ? 27.538  5.463   -37.399 1.00 79.77  ? 436  SER B O   1 
ATOM   6195  C CB  . SER B 1 427 ? 30.235  4.993   -37.432 1.00 84.12  ? 436  SER B CB  1 
ATOM   6196  O OG  . SER B 1 427 ? 30.294  5.318   -38.805 1.00 86.55  ? 436  SER B OG  1 
ATOM   6197  N N   . ASN B 1 428 ? 27.678  7.529   -36.479 1.00 77.08  ? 437  ASN B N   1 
ATOM   6198  C CA  . ASN B 1 428 ? 26.332  7.981   -36.903 1.00 75.38  ? 437  ASN B CA  1 
ATOM   6199  C C   . ASN B 1 428 ? 25.239  6.876   -37.088 1.00 74.17  ? 437  ASN B C   1 
ATOM   6200  O O   . ASN B 1 428 ? 24.516  6.862   -38.074 1.00 73.98  ? 437  ASN B O   1 
ATOM   6201  C CB  . ASN B 1 428 ? 26.466  8.860   -38.166 1.00 76.89  ? 437  ASN B CB  1 
ATOM   6202  C CG  . ASN B 1 428 ? 25.259  9.753   -38.397 1.00 75.89  ? 437  ASN B CG  1 
ATOM   6203  O OD1 . ASN B 1 428 ? 24.831  10.480  -37.511 1.00 75.66  ? 437  ASN B OD1 1 
ATOM   6204  N ND2 . ASN B 1 428 ? 24.713  9.706   -39.598 1.00 77.61  ? 437  ASN B ND2 1 
ATOM   6205  N N   . GLY B 1 429 ? 25.135  5.961   -36.126 1.00 73.18  ? 438  GLY B N   1 
ATOM   6206  C CA  . GLY B 1 429 ? 24.153  4.870   -36.167 1.00 72.30  ? 438  GLY B CA  1 
ATOM   6207  C C   . GLY B 1 429 ? 23.746  4.426   -34.767 1.00 70.38  ? 438  GLY B C   1 
ATOM   6208  O O   . GLY B 1 429 ? 23.450  5.255   -33.902 1.00 68.54  ? 438  GLY B O   1 
ATOM   6209  N N   . CYS B 1 430 ? 23.750  3.117   -34.528 1.00 70.79  ? 439  CYS B N   1 
ATOM   6210  C CA  . CYS B 1 430 ? 23.363  2.556   -33.232 1.00 68.64  ? 439  CYS B CA  1 
ATOM   6211  C C   . CYS B 1 430 ? 24.151  1.291   -32.875 1.00 69.94  ? 439  CYS B C   1 
ATOM   6212  O O   . CYS B 1 430 ? 23.962  0.230   -33.481 1.00 71.57  ? 439  CYS B O   1 
ATOM   6213  C CB  . CYS B 1 430 ? 21.851  2.312   -33.239 1.00 67.27  ? 439  CYS B CB  1 
ATOM   6214  S SG  . CYS B 1 430 ? 21.185  0.802   -32.460 1.00 68.31  ? 439  CYS B SG  1 
ATOM   6215  N N   . ASP B 1 431 ? 25.035  1.412   -31.892 1.00 69.06  ? 440  ASP B N   1 
ATOM   6216  C CA  . ASP B 1 431 ? 25.925  0.316   -31.522 1.00 70.59  ? 440  ASP B CA  1 
ATOM   6217  C C   . ASP B 1 431 ? 25.731  -0.160  -30.090 1.00 68.24  ? 440  ASP B C   1 
ATOM   6218  O O   . ASP B 1 431 ? 25.010  0.464   -29.332 1.00 65.95  ? 440  ASP B O   1 
ATOM   6219  C CB  . ASP B 1 431 ? 27.370  0.763   -31.701 1.00 72.83  ? 440  ASP B CB  1 
ATOM   6220  C CG  . ASP B 1 431 ? 28.053  0.102   -32.895 1.00 78.27  ? 440  ASP B CG  1 
ATOM   6221  O OD1 . ASP B 1 431 ? 28.528  -1.058  -32.776 1.00 82.02  ? 440  ASP B OD1 1 
ATOM   6222  O OD2 . ASP B 1 431 ? 28.138  0.762   -33.953 1.00 81.38  ? 440  ASP B OD2 1 
ATOM   6223  N N   . TYR B 1 432 ? 26.400  -1.252  -29.728 1.00 68.71  ? 441  TYR B N   1 
ATOM   6224  C CA  . TYR B 1 432 ? 26.401  -1.810  -28.368 1.00 67.00  ? 441  TYR B CA  1 
ATOM   6225  C C   . TYR B 1 432 ? 27.831  -1.933  -27.858 1.00 67.86  ? 441  TYR B C   1 
ATOM   6226  O O   . TYR B 1 432 ? 28.725  -2.098  -28.639 1.00 70.32  ? 441  TYR B O   1 
ATOM   6227  C CB  . TYR B 1 432 ? 25.770  -3.193  -28.413 1.00 67.98  ? 441  TYR B CB  1 
ATOM   6228  C CG  . TYR B 1 432 ? 25.792  -3.983  -27.125 1.00 67.35  ? 441  TYR B CG  1 
ATOM   6229  C CD1 . TYR B 1 432 ? 24.754  -3.880  -26.221 1.00 65.45  ? 441  TYR B CD1 1 
ATOM   6230  C CD2 . TYR B 1 432 ? 26.828  -4.859  -26.828 1.00 69.26  ? 441  TYR B CD2 1 
ATOM   6231  C CE1 . TYR B 1 432 ? 24.737  -4.613  -25.044 1.00 64.88  ? 441  TYR B CE1 1 
ATOM   6232  C CE2 . TYR B 1 432 ? 26.816  -5.600  -25.640 1.00 69.54  ? 441  TYR B CE2 1 
ATOM   6233  C CZ  . TYR B 1 432 ? 25.755  -5.470  -24.758 1.00 66.78  ? 441  TYR B CZ  1 
ATOM   6234  O OH  . TYR B 1 432 ? 25.700  -6.178  -23.584 1.00 65.63  ? 441  TYR B OH  1 
ATOM   6235  N N   . VAL B 1 433 ? 28.058  -1.873  -26.555 1.00 66.48  ? 442  VAL B N   1 
ATOM   6236  C CA  . VAL B 1 433 ? 29.401  -2.089  -25.988 1.00 67.96  ? 442  VAL B CA  1 
ATOM   6237  C C   . VAL B 1 433 ? 29.273  -2.887  -24.701 1.00 67.73  ? 442  VAL B C   1 
ATOM   6238  O O   . VAL B 1 433 ? 28.162  -3.055  -24.231 1.00 66.54  ? 442  VAL B O   1 
ATOM   6239  C CB  . VAL B 1 433 ? 30.109  -0.765  -25.684 1.00 66.75  ? 442  VAL B CB  1 
ATOM   6240  C CG1 . VAL B 1 433 ? 30.542  -0.091  -26.947 1.00 68.47  ? 442  VAL B CG1 1 
ATOM   6241  C CG2 . VAL B 1 433 ? 29.223  0.157   -24.923 1.00 63.38  ? 442  VAL B CG2 1 
ATOM   6242  N N   . SER B 1 434 ? 30.364  -3.375  -24.111 1.00 69.39  ? 443  SER B N   1 
ATOM   6243  C CA  . SER B 1 434 ? 30.204  -4.117  -22.852 1.00 69.32  ? 443  SER B CA  1 
ATOM   6244  C C   . SER B 1 434 ? 31.236  -3.814  -21.761 1.00 69.79  ? 443  SER B C   1 
ATOM   6245  O O   . SER B 1 434 ? 32.226  -3.159  -22.033 1.00 71.02  ? 443  SER B O   1 
ATOM   6246  C CB  . SER B 1 434 ? 30.105  -5.610  -23.138 1.00 71.49  ? 443  SER B CB  1 
ATOM   6247  O OG  . SER B 1 434 ? 31.278  -6.275  -22.788 1.00 73.13  ? 443  SER B OG  1 
ATOM   6248  N N   . ASN B 1 435 ? 30.998  -4.272  -20.532 1.00 69.57  ? 444  ASN B N   1 
ATOM   6249  C CA  . ASN B 1 435 ? 31.949  -4.074  -19.415 1.00 70.41  ? 444  ASN B CA  1 
ATOM   6250  C C   . ASN B 1 435 ? 33.237  -4.853  -19.600 1.00 74.37  ? 444  ASN B C   1 
ATOM   6251  O O   . ASN B 1 435 ? 33.255  -5.937  -20.202 1.00 76.20  ? 444  ASN B O   1 
ATOM   6252  C CB  . ASN B 1 435 ? 31.325  -4.483  -18.113 1.00 68.75  ? 444  ASN B CB  1 
ATOM   6253  C CG  . ASN B 1 435 ? 29.871  -4.522  -18.221 1.00 68.08  ? 444  ASN B CG  1 
ATOM   6254  O OD1 . ASN B 1 435 ? 29.311  -3.867  -19.097 1.00 69.71  ? 444  ASN B OD1 1 
ATOM   6255  N ND2 . ASN B 1 435 ? 29.224  -5.305  -17.378 1.00 68.25  ? 444  ASN B ND2 1 
ATOM   6256  N N   . LYS B 1 436 ? 34.301  -4.320  -19.004 1.00 75.92  ? 445  LYS B N   1 
ATOM   6257  C CA  . LYS B 1 436 ? 35.652  -4.412  -19.561 1.00 79.98  ? 445  LYS B CA  1 
ATOM   6258  C C   . LYS B 1 436 ? 35.540  -4.141  -21.022 1.00 80.91  ? 445  LYS B C   1 
ATOM   6259  O O   . LYS B 1 436 ? 34.650  -4.626  -21.696 1.00 81.16  ? 445  LYS B O   1 
ATOM   6260  C CB  . LYS B 1 436 ? 36.412  -5.724  -19.282 1.00 83.54  ? 445  LYS B CB  1 
ATOM   6261  C CG  . LYS B 1 436 ? 37.950  -5.810  -19.798 1.00 89.14  ? 445  LYS B CG  1 
ATOM   6262  C CD  . LYS B 1 436 ? 38.968  -4.589  -19.525 1.00 91.91  ? 445  LYS B CD  1 
ATOM   6263  C CE  . LYS B 1 436 ? 38.480  -3.343  -18.644 1.00 89.51  ? 445  LYS B CE  1 
ATOM   6264  N NZ  . LYS B 1 436 ? 37.801  -3.585  -17.313 1.00 87.33  ? 445  LYS B NZ  1 
ATOM   6265  N N   . GLY B 1 437 ? 36.491  -3.373  -21.504 1.00 82.10  ? 446  GLY B N   1 
ATOM   6266  C CA  . GLY B 1 437 ? 36.269  -2.580  -22.668 1.00 81.56  ? 446  GLY B CA  1 
ATOM   6267  C C   . GLY B 1 437 ? 35.775  -1.313  -22.015 1.00 77.75  ? 446  GLY B C   1 
ATOM   6268  O O   . GLY B 1 437 ? 36.578  -0.537  -21.467 1.00 77.92  ? 446  GLY B O   1 
ATOM   6269  N N   . VAL B 1 438 ? 34.456  -1.159  -21.989 1.00 74.39  ? 447  VAL B N   1 
ATOM   6270  C CA  . VAL B 1 438 ? 33.869  0.150   -21.779 1.00 70.88  ? 447  VAL B CA  1 
ATOM   6271  C C   . VAL B 1 438 ? 33.396  0.410   -20.378 1.00 67.87  ? 447  VAL B C   1 
ATOM   6272  O O   . VAL B 1 438 ? 32.828  -0.453  -19.705 1.00 67.29  ? 447  VAL B O   1 
ATOM   6273  C CB  . VAL B 1 438 ? 32.735  0.427   -22.752 1.00 69.93  ? 447  VAL B CB  1 
ATOM   6274  C CG1 . VAL B 1 438 ? 32.476  1.899   -22.821 1.00 68.28  ? 447  VAL B CG1 1 
ATOM   6275  C CG2 . VAL B 1 438 ? 33.100  -0.082  -24.129 1.00 72.88  ? 447  VAL B CG2 1 
ATOM   6276  N N   . ASP B 1 439 ? 33.625  1.650   -19.984 1.00 65.89  ? 448  ASP B N   1 
ATOM   6277  C CA  . ASP B 1 439 ? 33.371  2.116   -18.653 1.00 63.51  ? 448  ASP B CA  1 
ATOM   6278  C C   . ASP B 1 439 ? 32.443  3.351   -18.661 1.00 60.38  ? 448  ASP B C   1 
ATOM   6279  O O   . ASP B 1 439 ? 31.708  3.643   -17.709 1.00 57.79  ? 448  ASP B O   1 
ATOM   6280  C CB  . ASP B 1 439 ? 34.712  2.494   -18.073 1.00 64.87  ? 448  ASP B CB  1 
ATOM   6281  C CG  . ASP B 1 439 ? 34.819  2.180   -16.600 1.00 66.74  ? 448  ASP B CG  1 
ATOM   6282  O OD1 . ASP B 1 439 ? 33.837  2.433   -15.819 1.00 66.68  ? 448  ASP B OD1 1 
ATOM   6283  O OD2 . ASP B 1 439 ? 35.917  1.679   -16.226 1.00 71.51  ? 448  ASP B OD2 1 
ATOM   6284  N N   . THR B 1 440 ? 32.472  4.050   -19.782 1.00 60.28  ? 449  THR B N   1 
ATOM   6285  C CA  . THR B 1 440 ? 31.846  5.342   -19.936 1.00 57.59  ? 449  THR B CA  1 
ATOM   6286  C C   . THR B 1 440 ? 31.457  5.521   -21.392 1.00 58.04  ? 449  THR B C   1 
ATOM   6287  O O   . THR B 1 440 ? 32.225  5.184   -22.288 1.00 60.54  ? 449  THR B O   1 
ATOM   6288  C CB  . THR B 1 440 ? 32.884  6.409   -19.577 1.00 57.94  ? 449  THR B CB  1 
ATOM   6289  O OG1 . THR B 1 440 ? 32.684  6.785   -18.227 1.00 55.12  ? 449  THR B OG1 1 
ATOM   6290  C CG2 . THR B 1 440 ? 32.833  7.657   -20.504 1.00 58.47  ? 449  THR B CG2 1 
ATOM   6291  N N   . VAL B 1 441 ? 30.268  6.036   -21.646 1.00 55.73  ? 450  VAL B N   1 
ATOM   6292  C CA  . VAL B 1 441 ? 29.991  6.590   -22.969 1.00 55.90  ? 450  VAL B CA  1 
ATOM   6293  C C   . VAL B 1 441 ? 29.496  7.998   -22.782 1.00 54.19  ? 450  VAL B C   1 
ATOM   6294  O O   . VAL B 1 441 ? 28.879  8.311   -21.775 1.00 52.51  ? 450  VAL B O   1 
ATOM   6295  C CB  . VAL B 1 441 ? 28.979  5.784   -23.803 1.00 55.58  ? 450  VAL B CB  1 
ATOM   6296  C CG1 . VAL B 1 441 ? 29.271  4.316   -23.743 1.00 56.60  ? 450  VAL B CG1 1 
ATOM   6297  C CG2 . VAL B 1 441 ? 27.617  6.007   -23.311 1.00 53.80  ? 450  VAL B CG2 1 
ATOM   6298  N N   . SER B 1 442 ? 29.789  8.857   -23.733 1.00 55.03  ? 451  SER B N   1 
ATOM   6299  C CA  . SER B 1 442 ? 29.354  10.221  -23.643 1.00 53.96  ? 451  SER B CA  1 
ATOM   6300  C C   . SER B 1 442 ? 28.630  10.495  -24.905 1.00 53.97  ? 451  SER B C   1 
ATOM   6301  O O   . SER B 1 442 ? 29.051  10.057  -25.944 1.00 55.99  ? 451  SER B O   1 
ATOM   6302  C CB  . SER B 1 442 ? 30.515  11.190  -23.469 1.00 55.19  ? 451  SER B CB  1 
ATOM   6303  O OG  . SER B 1 442 ? 31.780  10.586  -23.786 1.00 60.35  ? 451  SER B OG  1 
ATOM   6304  N N   . VAL B 1 443 ? 27.490  11.167  -24.788 1.00 52.32  ? 452  VAL B N   1 
ATOM   6305  C CA  . VAL B 1 443 ? 26.668  11.622  -25.904 1.00 51.78  ? 452  VAL B CA  1 
ATOM   6306  C C   . VAL B 1 443 ? 26.579  13.114  -25.740 1.00 51.06  ? 452  VAL B C   1 
ATOM   6307  O O   . VAL B 1 443 ? 26.100  13.614  -24.740 1.00 49.46  ? 452  VAL B O   1 
ATOM   6308  C CB  . VAL B 1 443 ? 25.251  11.067  -25.853 1.00 49.97  ? 452  VAL B CB  1 
ATOM   6309  C CG1 . VAL B 1 443 ? 24.481  11.508  -27.052 1.00 49.72  ? 452  VAL B CG1 1 
ATOM   6310  C CG2 . VAL B 1 443 ? 25.271  9.567   -25.785 1.00 50.52  ? 452  VAL B CG2 1 
ATOM   6311  N N   . GLY B 1 444 ? 27.082  13.833  -26.720 1.00 52.60  ? 453  GLY B N   1 
ATOM   6312  C CA  . GLY B 1 444 ? 27.180  15.269  -26.591 1.00 52.24  ? 453  GLY B CA  1 
ATOM   6313  C C   . GLY B 1 444 ? 27.792  15.576  -25.255 1.00 51.41  ? 453  GLY B C   1 
ATOM   6314  O O   . GLY B 1 444 ? 28.888  15.101  -24.936 1.00 52.55  ? 453  GLY B O   1 
ATOM   6315  N N   . ASN B 1 445 ? 27.060  16.333  -24.463 1.00 49.42  ? 454  ASN B N   1 
ATOM   6316  C CA  . ASN B 1 445 ? 27.567  16.732  -23.183 1.00 49.17  ? 454  ASN B CA  1 
ATOM   6317  C C   . ASN B 1 445 ? 27.159  15.899  -21.996 1.00 47.09  ? 454  ASN B C   1 
ATOM   6318  O O   . ASN B 1 445 ? 27.612  16.122  -20.886 1.00 46.83  ? 454  ASN B O   1 
ATOM   6319  C CB  . ASN B 1 445 ? 27.271  18.198  -22.952 1.00 49.15  ? 454  ASN B CB  1 
ATOM   6320  C CG  . ASN B 1 445 ? 28.394  19.065  -23.439 1.00 53.15  ? 454  ASN B CG  1 
ATOM   6321  O OD1 . ASN B 1 445 ? 29.200  19.574  -22.630 1.00 56.44  ? 454  ASN B OD1 1 
ATOM   6322  N ND2 . ASN B 1 445 ? 28.523  19.178  -24.772 1.00 55.71  ? 454  ASN B ND2 1 
ATOM   6323  N N   . THR B 1 446 ? 26.333  14.909  -22.250 1.00 45.80  ? 455  THR B N   1 
ATOM   6324  C CA  . THR B 1 446 ? 25.819  14.064  -21.210 1.00 43.89  ? 455  THR B CA  1 
ATOM   6325  C C   . THR B 1 446 ? 26.714  12.879  -21.114 1.00 44.37  ? 455  THR B C   1 
ATOM   6326  O O   . THR B 1 446 ? 27.044  12.319  -22.099 1.00 45.67  ? 455  THR B O   1 
ATOM   6327  C CB  . THR B 1 446 ? 24.393  13.587  -21.552 1.00 43.07  ? 455  THR B CB  1 
ATOM   6328  O OG1 . THR B 1 446 ? 23.572  14.723  -21.869 1.00 42.40  ? 455  THR B OG1 1 
ATOM   6329  C CG2 . THR B 1 446 ? 23.781  12.813  -20.400 1.00 41.85  ? 455  THR B CG2 1 
ATOM   6330  N N   . LEU B 1 447 ? 27.084  12.485  -19.919 1.00 43.63  ? 456  LEU B N   1 
ATOM   6331  C CA  . LEU B 1 447 ? 27.972  11.380  -19.748 1.00 45.10  ? 456  LEU B CA  1 
ATOM   6332  C C   . LEU B 1 447 ? 27.244  10.220  -19.129 1.00 44.44  ? 456  LEU B C   1 
ATOM   6333  O O   . LEU B 1 447 ? 26.571  10.386  -18.131 1.00 43.35  ? 456  LEU B O   1 
ATOM   6334  C CB  . LEU B 1 447 ? 29.124  11.813  -18.839 1.00 45.70  ? 456  LEU B CB  1 
ATOM   6335  C CG  . LEU B 1 447 ? 30.208  10.775  -18.579 1.00 46.97  ? 456  LEU B CG  1 
ATOM   6336  C CD1 . LEU B 1 447 ? 31.012  10.588  -19.844 1.00 50.94  ? 456  LEU B CD1 1 
ATOM   6337  C CD2 . LEU B 1 447 ? 31.086  11.202  -17.453 1.00 46.42  ? 456  LEU B CD2 1 
ATOM   6338  N N   . TYR B 1 448 ? 27.385  9.036   -19.693 1.00 45.81  ? 457  TYR B N   1 
ATOM   6339  C CA  . TYR B 1 448 ? 26.756  7.863   -19.103 1.00 45.75  ? 457  TYR B CA  1 
ATOM   6340  C C   . TYR B 1 448 ? 27.807  6.908   -18.551 1.00 46.93  ? 457  TYR B C   1 
ATOM   6341  O O   . TYR B 1 448 ? 28.844  6.712   -19.173 1.00 49.22  ? 457  TYR B O   1 
ATOM   6342  C CB  . TYR B 1 448 ? 25.885  7.158   -20.142 1.00 46.45  ? 457  TYR B CB  1 
ATOM   6343  C CG  . TYR B 1 448 ? 24.708  7.987   -20.644 1.00 46.53  ? 457  TYR B CG  1 
ATOM   6344  C CD1 . TYR B 1 448 ? 24.896  9.165   -21.402 1.00 48.29  ? 457  TYR B CD1 1 
ATOM   6345  C CD2 . TYR B 1 448 ? 23.399  7.588   -20.382 1.00 45.90  ? 457  TYR B CD2 1 
ATOM   6346  C CE1 . TYR B 1 448 ? 23.791  9.926   -21.861 1.00 47.77  ? 457  TYR B CE1 1 
ATOM   6347  C CE2 . TYR B 1 448 ? 22.290  8.342   -20.836 1.00 45.55  ? 457  TYR B CE2 1 
ATOM   6348  C CZ  . TYR B 1 448 ? 22.498  9.501   -21.569 1.00 46.45  ? 457  TYR B CZ  1 
ATOM   6349  O OH  . TYR B 1 448 ? 21.403  10.206  -21.998 1.00 45.80  ? 457  TYR B OH  1 
ATOM   6350  N N   . TYR B 1 449 ? 27.547  6.314   -17.388 1.00 45.72  ? 458  TYR B N   1 
ATOM   6351  C CA  . TYR B 1 449 ? 28.494  5.376   -16.769 1.00 46.55  ? 458  TYR B CA  1 
ATOM   6352  C C   . TYR B 1 449 ? 28.117  3.916   -16.910 1.00 47.19  ? 458  TYR B C   1 
ATOM   6353  O O   . TYR B 1 449 ? 27.216  3.458   -16.223 1.00 46.49  ? 458  TYR B O   1 
ATOM   6354  C CB  . TYR B 1 449 ? 28.608  5.656   -15.286 1.00 44.98  ? 458  TYR B CB  1 
ATOM   6355  C CG  . TYR B 1 449 ? 29.141  6.994   -14.991 1.00 44.30  ? 458  TYR B CG  1 
ATOM   6356  C CD1 . TYR B 1 449 ? 28.285  8.048   -14.845 1.00 43.08  ? 458  TYR B CD1 1 
ATOM   6357  C CD2 . TYR B 1 449 ? 30.510  7.213   -14.843 1.00 46.11  ? 458  TYR B CD2 1 
ATOM   6358  C CE1 . TYR B 1 449 ? 28.747  9.304   -14.551 1.00 44.22  ? 458  TYR B CE1 1 
ATOM   6359  C CE2 . TYR B 1 449 ? 31.006  8.484   -14.555 1.00 46.87  ? 458  TYR B CE2 1 
ATOM   6360  C CZ  . TYR B 1 449 ? 30.091  9.533   -14.406 1.00 45.92  ? 458  TYR B CZ  1 
ATOM   6361  O OH  . TYR B 1 449 ? 30.438  10.837  -14.116 1.00 45.94  ? 458  TYR B OH  1 
ATOM   6362  N N   . VAL B 1 450 ? 28.840  3.166   -17.723 1.00 48.87  ? 459  VAL B N   1 
ATOM   6363  C CA  . VAL B 1 450 ? 28.473  1.787   -17.933 1.00 49.87  ? 459  VAL B CA  1 
ATOM   6364  C C   . VAL B 1 450 ? 28.763  0.884   -16.754 1.00 50.52  ? 459  VAL B C   1 
ATOM   6365  O O   . VAL B 1 450 ? 28.119  -0.142  -16.598 1.00 50.90  ? 459  VAL B O   1 
ATOM   6366  C CB  . VAL B 1 450 ? 29.162  1.228   -19.139 1.00 52.28  ? 459  VAL B CB  1 
ATOM   6367  C CG1 . VAL B 1 450 ? 28.598  -0.148  -19.477 1.00 53.70  ? 459  VAL B CG1 1 
ATOM   6368  C CG2 . VAL B 1 450 ? 28.971  2.170   -20.299 1.00 51.97  ? 459  VAL B CG2 1 
ATOM   6369  N N   . ASN B 1 451 ? 29.741  1.250   -15.939 1.00 51.10  ? 460  ASN B N   1 
ATOM   6370  C CA  . ASN B 1 451 ? 30.021  0.513   -14.711 1.00 51.68  ? 460  ASN B CA  1 
ATOM   6371  C C   . ASN B 1 451 ? 29.904  1.404   -13.501 1.00 50.03  ? 460  ASN B C   1 
ATOM   6372  O O   . ASN B 1 451 ? 29.913  2.626   -13.626 1.00 48.98  ? 460  ASN B O   1 
ATOM   6373  C CB  . ASN B 1 451 ? 31.390  -0.128  -14.790 1.00 54.13  ? 460  ASN B CB  1 
ATOM   6374  C CG  . ASN B 1 451 ? 31.398  -1.320  -15.713 1.00 57.45  ? 460  ASN B CG  1 
ATOM   6375  O OD1 . ASN B 1 451 ? 30.551  -2.201  -15.574 1.00 59.21  ? 460  ASN B OD1 1 
ATOM   6376  N ND2 . ASN B 1 451 ? 32.332  -1.353  -16.679 1.00 60.61  ? 460  ASN B ND2 1 
ATOM   6377  N N   . LYS B 1 452 ? 29.749  0.820   -12.326 1.00 50.19  ? 461  LYS B N   1 
ATOM   6378  C CA  . LYS B 1 452 ? 29.607  1.672   -11.165 1.00 49.19  ? 461  LYS B CA  1 
ATOM   6379  C C   . LYS B 1 452 ? 30.998  2.123   -10.797 1.00 50.43  ? 461  LYS B C   1 
ATOM   6380  O O   . LYS B 1 452 ? 31.945  1.351   -10.894 1.00 52.39  ? 461  LYS B O   1 
ATOM   6381  C CB  . LYS B 1 452 ? 28.980  0.927   -10.008 1.00 48.48  ? 461  LYS B CB  1 
ATOM   6382  C CG  . LYS B 1 452 ? 27.723  0.212   -10.366 1.00 49.41  ? 461  LYS B CG  1 
ATOM   6383  C CD  . LYS B 1 452 ? 26.990  -0.182  -9.123  1.00 50.02  ? 461  LYS B CD  1 
ATOM   6384  C CE  . LYS B 1 452 ? 25.809  -1.060  -9.432  1.00 52.31  ? 461  LYS B CE  1 
ATOM   6385  N NZ  . LYS B 1 452 ? 24.952  -1.104  -8.220  1.00 52.77  ? 461  LYS B NZ  1 
ATOM   6386  N N   . GLN B 1 453 ? 31.132  3.368   -10.385 1.00 49.77  ? 462  GLN B N   1 
ATOM   6387  C CA  . GLN B 1 453 ? 32.432  3.862   -10.059 1.00 51.64  ? 462  GLN B CA  1 
ATOM   6388  C C   . GLN B 1 453 ? 32.753  3.586   -8.617  1.00 52.10  ? 462  GLN B C   1 
ATOM   6389  O O   . GLN B 1 453 ? 32.062  4.045   -7.727  1.00 50.39  ? 462  GLN B O   1 
ATOM   6390  C CB  . GLN B 1 453 ? 32.531  5.330   -10.395 1.00 50.64  ? 462  GLN B CB  1 
ATOM   6391  C CG  . GLN B 1 453 ? 32.183  5.601   -11.844 1.00 52.54  ? 462  GLN B CG  1 
ATOM   6392  C CD  . GLN B 1 453 ? 32.997  4.753   -12.849 1.00 57.59  ? 462  GLN B CD  1 
ATOM   6393  O OE1 . GLN B 1 453 ? 34.193  5.001   -13.087 1.00 60.51  ? 462  GLN B OE1 1 
ATOM   6394  N NE2 . GLN B 1 453 ? 32.337  3.759   -13.461 1.00 58.29  ? 462  GLN B NE2 1 
ATOM   6395  N N   . GLU B 1 454 ? 33.791  2.786   -8.397  1.00 55.35  ? 463  GLU B N   1 
ATOM   6396  C CA  . GLU B 1 454 ? 34.305  2.513   -7.057  1.00 56.53  ? 463  GLU B CA  1 
ATOM   6397  C C   . GLU B 1 454 ? 34.903  3.788   -6.508  1.00 55.60  ? 463  GLU B C   1 
ATOM   6398  O O   . GLU B 1 454 ? 35.352  4.641   -7.254  1.00 56.47  ? 463  GLU B O   1 
ATOM   6399  C CB  . GLU B 1 454 ? 35.375  1.421   -7.099  1.00 59.48  ? 463  GLU B CB  1 
ATOM   6400  C CG  . GLU B 1 454 ? 34.940  0.055   -6.577  1.00 64.02  ? 463  GLU B CG  1 
ATOM   6401  C CD  . GLU B 1 454 ? 35.943  -1.060  -6.922  1.00 71.80  ? 463  GLU B CD  1 
ATOM   6402  O OE1 . GLU B 1 454 ? 37.094  -1.029  -6.408  1.00 74.72  ? 463  GLU B OE1 1 
ATOM   6403  O OE2 . GLU B 1 454 ? 35.582  -1.978  -7.702  1.00 73.95  ? 463  GLU B OE2 1 
ATOM   6404  N N   . GLY B 1 455 ? 34.903  3.929   -5.201  1.00 54.49  ? 464  GLY B N   1 
ATOM   6405  C CA  . GLY B 1 455 ? 35.600  5.037   -4.599  1.00 54.43  ? 464  GLY B CA  1 
ATOM   6406  C C   . GLY B 1 455 ? 35.730  4.858   -3.109  1.00 53.91  ? 464  GLY B C   1 
ATOM   6407  O O   . GLY B 1 455 ? 34.894  4.275   -2.480  1.00 53.46  ? 464  GLY B O   1 
ATOM   6408  N N   . LYS B 1 456 ? 36.831  5.312   -2.561  1.00 54.84  ? 465  LYS B N   1 
ATOM   6409  C CA  . LYS B 1 456 ? 36.968  5.599   -1.152  1.00 53.82  ? 465  LYS B CA  1 
ATOM   6410  C C   . LYS B 1 456 ? 36.195  4.753   -0.180  1.00 52.92  ? 465  LYS B C   1 
ATOM   6411  O O   . LYS B 1 456 ? 35.040  4.996   0.039   1.00 51.31  ? 465  LYS B O   1 
ATOM   6412  C CB  . LYS B 1 456 ? 36.592  7.048   -0.926  1.00 51.80  ? 465  LYS B CB  1 
ATOM   6413  C CG  . LYS B 1 456 ? 37.200  7.564   0.297   1.00 52.16  ? 465  LYS B CG  1 
ATOM   6414  C CD  . LYS B 1 456 ? 37.120  9.053   0.376   1.00 53.36  ? 465  LYS B CD  1 
ATOM   6415  C CE  . LYS B 1 456 ? 37.917  9.519   1.611   1.00 56.03  ? 465  LYS B CE  1 
ATOM   6416  N NZ  . LYS B 1 456 ? 37.393  10.741  2.310   1.00 55.91  ? 465  LYS B NZ  1 
ATOM   6417  N N   . SER B 1 457 ? 36.843  3.774   0.432   1.00 54.66  ? 466  SER B N   1 
ATOM   6418  C CA  . SER B 1 457 ? 36.250  3.084   1.570   1.00 53.96  ? 466  SER B CA  1 
ATOM   6419  C C   . SER B 1 457 ? 36.317  4.014   2.719   1.00 52.17  ? 466  SER B C   1 
ATOM   6420  O O   . SER B 1 457 ? 37.231  4.800   2.831   1.00 52.38  ? 466  SER B O   1 
ATOM   6421  C CB  . SER B 1 457 ? 37.044  1.852   1.947   1.00 56.20  ? 466  SER B CB  1 
ATOM   6422  O OG  . SER B 1 457 ? 38.416  2.186   2.069   1.00 59.56  ? 466  SER B OG  1 
ATOM   6423  N N   . LEU B 1 458 ? 35.333  3.915   3.579   1.00 50.86  ? 467  LEU B N   1 
ATOM   6424  C CA  . LEU B 1 458 ? 35.323  4.695   4.781   1.00 49.95  ? 467  LEU B CA  1 
ATOM   6425  C C   . LEU B 1 458 ? 35.267  3.762   5.938   1.00 50.42  ? 467  LEU B C   1 
ATOM   6426  O O   . LEU B 1 458 ? 34.565  2.760   5.910   1.00 50.30  ? 467  LEU B O   1 
ATOM   6427  C CB  . LEU B 1 458 ? 34.133  5.630   4.818   1.00 47.85  ? 467  LEU B CB  1 
ATOM   6428  C CG  . LEU B 1 458 ? 34.245  6.855   3.923   1.00 47.49  ? 467  LEU B CG  1 
ATOM   6429  C CD1 . LEU B 1 458 ? 33.053  7.763   4.217   1.00 44.75  ? 467  LEU B CD1 1 
ATOM   6430  C CD2 . LEU B 1 458 ? 35.600  7.580   4.090   1.00 47.81  ? 467  LEU B CD2 1 
ATOM   6431  N N   . TYR B 1 459 ? 36.011  4.109   6.970   1.00 51.33  ? 468  TYR B N   1 
ATOM   6432  C CA  . TYR B 1 459 ? 36.286  3.167   8.019   1.00 52.96  ? 468  TYR B CA  1 
ATOM   6433  C C   . TYR B 1 459 ? 36.032  3.810   9.349   1.00 50.52  ? 468  TYR B C   1 
ATOM   6434  O O   . TYR B 1 459 ? 36.439  4.927   9.573   1.00 50.01  ? 468  TYR B O   1 
ATOM   6435  C CB  . TYR B 1 459 ? 37.741  2.636   7.908   1.00 56.27  ? 468  TYR B CB  1 
ATOM   6436  C CG  . TYR B 1 459 ? 38.027  1.568   8.950   1.00 61.99  ? 468  TYR B CG  1 
ATOM   6437  C CD1 . TYR B 1 459 ? 37.381  0.313   8.887   1.00 65.84  ? 468  TYR B CD1 1 
ATOM   6438  C CD2 . TYR B 1 459 ? 38.903  1.813   10.033  1.00 66.73  ? 468  TYR B CD2 1 
ATOM   6439  C CE1 . TYR B 1 459 ? 37.601  -0.690  9.867   1.00 68.11  ? 468  TYR B CE1 1 
ATOM   6440  C CE2 . TYR B 1 459 ? 39.137  0.806   11.029  1.00 69.32  ? 468  TYR B CE2 1 
ATOM   6441  C CZ  . TYR B 1 459 ? 38.470  -0.442  10.926  1.00 69.65  ? 468  TYR B CZ  1 
ATOM   6442  O OH  . TYR B 1 459 ? 38.658  -1.444  11.852  1.00 70.66  ? 468  TYR B OH  1 
ATOM   6443  N N   . VAL B 1 460 ? 35.344  3.117   10.231  1.00 49.64  ? 469  VAL B N   1 
ATOM   6444  C CA  . VAL B 1 460 ? 35.052  3.711   11.513  1.00 48.55  ? 469  VAL B CA  1 
ATOM   6445  C C   . VAL B 1 460 ? 35.376  2.810   12.673  1.00 50.11  ? 469  VAL B C   1 
ATOM   6446  O O   . VAL B 1 460 ? 34.616  1.887   12.985  1.00 50.24  ? 469  VAL B O   1 
ATOM   6447  C CB  . VAL B 1 460 ? 33.620  4.126   11.612  1.00 46.30  ? 469  VAL B CB  1 
ATOM   6448  C CG1 . VAL B 1 460 ? 33.287  4.358   13.047  1.00 44.45  ? 469  VAL B CG1 1 
ATOM   6449  C CG2 . VAL B 1 460 ? 33.426  5.393   10.823  1.00 45.33  ? 469  VAL B CG2 1 
ATOM   6450  N N   . LYS B 1 461 ? 36.491  3.119   13.328  1.00 51.96  ? 470  LYS B N   1 
ATOM   6451  C CA  . LYS B 1 461 ? 37.109  2.268   14.353  1.00 53.97  ? 470  LYS B CA  1 
ATOM   6452  C C   . LYS B 1 461 ? 36.350  2.341   15.684  1.00 52.59  ? 470  LYS B C   1 
ATOM   6453  O O   . LYS B 1 461 ? 35.695  3.337   15.988  1.00 50.96  ? 470  LYS B O   1 
ATOM   6454  C CB  . LYS B 1 461 ? 38.622  2.628   14.463  1.00 55.76  ? 470  LYS B CB  1 
ATOM   6455  C CG  . LYS B 1 461 ? 39.287  2.711   15.883  1.00 58.83  ? 470  LYS B CG  1 
ATOM   6456  C CD  . LYS B 1 461 ? 40.353  1.577   16.177  1.00 64.96  ? 470  LYS B CD  1 
ATOM   6457  C CE  . LYS B 1 461 ? 40.807  1.556   17.682  1.00 65.15  ? 470  LYS B CE  1 
ATOM   6458  N NZ  . LYS B 1 461 ? 41.014  0.167   18.248  1.00 66.05  ? 470  LYS B NZ  1 
ATOM   6459  N N   . GLY B 1 462 ? 36.383  1.249   16.435  1.00 53.73  ? 471  GLY B N   1 
ATOM   6460  C CA  . GLY B 1 462 ? 35.934  1.243   17.832  1.00 53.83  ? 471  GLY B CA  1 
ATOM   6461  C C   . GLY B 1 462 ? 37.031  0.678   18.752  1.00 56.31  ? 471  GLY B C   1 
ATOM   6462  O O   . GLY B 1 462 ? 37.821  -0.220  18.350  1.00 58.40  ? 471  GLY B O   1 
ATOM   6463  N N   . GLU B 1 463 ? 37.118  1.199   19.980  1.00 56.27  ? 472  GLU B N   1 
ATOM   6464  C CA  . GLU B 1 463 ? 38.021  0.614   20.983  1.00 58.46  ? 472  GLU B CA  1 
ATOM   6465  C C   . GLU B 1 463 ? 37.197  -0.455  21.790  1.00 58.09  ? 472  GLU B C   1 
ATOM   6466  O O   . GLU B 1 463 ? 36.010  -0.703  21.489  1.00 57.03  ? 472  GLU B O   1 
ATOM   6467  C CB  . GLU B 1 463 ? 38.708  1.736   21.829  1.00 58.16  ? 472  GLU B CB  1 
ATOM   6468  C CG  . GLU B 1 463 ? 38.102  2.089   23.246  1.00 60.89  ? 472  GLU B CG  1 
ATOM   6469  C CD  . GLU B 1 463 ? 36.505  2.160   23.340  1.00 64.71  ? 472  GLU B CD  1 
ATOM   6470  O OE1 . GLU B 1 463 ? 35.819  2.662   22.388  1.00 64.90  ? 472  GLU B OE1 1 
ATOM   6471  O OE2 . GLU B 1 463 ? 35.942  1.718   24.399  1.00 65.62  ? 472  GLU B OE2 1 
ATOM   6472  N N   . PRO B 1 464 ? 37.815  -1.114  22.788  1.00 59.02  ? 473  PRO B N   1 
ATOM   6473  C CA  . PRO B 1 464 ? 36.926  -1.918  23.616  1.00 58.57  ? 473  PRO B CA  1 
ATOM   6474  C C   . PRO B 1 464 ? 36.670  -1.270  24.974  1.00 56.96  ? 473  PRO B C   1 
ATOM   6475  O O   . PRO B 1 464 ? 37.451  -0.422  25.418  1.00 56.11  ? 473  PRO B O   1 
ATOM   6476  C CB  . PRO B 1 464 ? 37.683  -3.249  23.749  1.00 60.88  ? 473  PRO B CB  1 
ATOM   6477  C CG  . PRO B 1 464 ? 39.159  -2.875  23.584  1.00 62.25  ? 473  PRO B CG  1 
ATOM   6478  C CD  . PRO B 1 464 ? 39.231  -1.460  23.009  1.00 60.81  ? 473  PRO B CD  1 
ATOM   6479  N N   . ILE B 1 465 ? 35.603  -1.724  25.623  1.00 56.56  ? 474  ILE B N   1 
ATOM   6480  C CA  . ILE B 1 465 ? 35.004  -1.042  26.754  1.00 55.54  ? 474  ILE B CA  1 
ATOM   6481  C C   . ILE B 1 465 ? 35.047  -1.806  28.119  1.00 56.54  ? 474  ILE B C   1 
ATOM   6482  O O   . ILE B 1 465 ? 34.841  -3.037  28.180  1.00 57.30  ? 474  ILE B O   1 
ATOM   6483  C CB  . ILE B 1 465 ? 33.604  -0.571  26.335  1.00 54.09  ? 474  ILE B CB  1 
ATOM   6484  C CG1 . ILE B 1 465 ? 32.956  0.297   27.410  1.00 53.26  ? 474  ILE B CG1 1 
ATOM   6485  C CG2 . ILE B 1 465 ? 32.725  -1.746  25.883  1.00 54.37  ? 474  ILE B CG2 1 
ATOM   6486  C CD1 . ILE B 1 465 ? 31.724  1.010   26.879  1.00 52.99  ? 474  ILE B CD1 1 
ATOM   6487  N N   . ILE B 1 466 ? 35.284  -1.035  29.193  1.00 56.65  ? 475  ILE B N   1 
ATOM   6488  C CA  . ILE B 1 466 ? 35.912  -1.510  30.462  1.00 58.36  ? 475  ILE B CA  1 
ATOM   6489  C C   . ILE B 1 466 ? 34.980  -1.754  31.682  1.00 58.53  ? 475  ILE B C   1 
ATOM   6490  O O   . ILE B 1 466 ? 34.444  -0.782  32.263  1.00 56.58  ? 475  ILE B O   1 
ATOM   6491  C CB  . ILE B 1 466 ? 37.114  -0.559  30.909  1.00 58.36  ? 475  ILE B CB  1 
ATOM   6492  C CG1 . ILE B 1 466 ? 36.709  0.936   30.770  1.00 57.84  ? 475  ILE B CG1 1 
ATOM   6493  C CG2 . ILE B 1 466 ? 38.407  -0.872  30.130  1.00 57.96  ? 475  ILE B CG2 1 
ATOM   6494  C CD1 . ILE B 1 466 ? 37.047  1.850   31.989  1.00 57.34  ? 475  ILE B CD1 1 
ATOM   6495  N N   . ASN B 1 467 ? 34.803  -3.040  32.061  1.00 61.01  ? 476  ASN B N   1 
ATOM   6496  C CA  . ASN B 1 467 ? 34.049  -3.432  33.300  1.00 62.11  ? 476  ASN B CA  1 
ATOM   6497  C C   . ASN B 1 467 ? 34.902  -3.443  34.614  1.00 63.22  ? 476  ASN B C   1 
ATOM   6498  O O   . ASN B 1 467 ? 35.495  -4.466  35.035  1.00 64.99  ? 476  ASN B O   1 
ATOM   6499  C CB  . ASN B 1 467 ? 33.191  -4.712  33.131  1.00 63.08  ? 476  ASN B CB  1 
ATOM   6500  C CG  . ASN B 1 467 ? 32.020  -4.761  34.142  1.00 63.39  ? 476  ASN B CG  1 
ATOM   6501  O OD1 . ASN B 1 467 ? 31.493  -3.710  34.538  1.00 62.43  ? 476  ASN B OD1 1 
ATOM   6502  N ND2 . ASN B 1 467 ? 31.618  -5.973  34.561  1.00 64.38  ? 476  ASN B ND2 1 
ATOM   6503  N N   . PHE B 1 468 ? 34.828  -2.294  35.287  1.00 62.39  ? 477  PHE B N   1 
ATOM   6504  C CA  . PHE B 1 468 ? 35.934  -1.581  35.970  1.00 62.87  ? 477  PHE B CA  1 
ATOM   6505  C C   . PHE B 1 468 ? 35.830  -1.608  37.498  1.00 62.39  ? 477  PHE B C   1 
ATOM   6506  O O   . PHE B 1 468 ? 36.092  -0.590  38.161  1.00 61.77  ? 477  PHE B O   1 
ATOM   6507  C CB  . PHE B 1 468 ? 35.749  -0.129  35.529  1.00 61.71  ? 477  PHE B CB  1 
ATOM   6508  C CG  . PHE B 1 468 ? 34.281  0.243   35.425  1.00 61.98  ? 477  PHE B CG  1 
ATOM   6509  C CD1 . PHE B 1 468 ? 33.569  0.671   36.581  1.00 62.02  ? 477  PHE B CD1 1 
ATOM   6510  C CD2 . PHE B 1 468 ? 33.575  0.057   34.205  1.00 61.01  ? 477  PHE B CD2 1 
ATOM   6511  C CE1 . PHE B 1 468 ? 32.181  0.969   36.508  1.00 61.28  ? 477  PHE B CE1 1 
ATOM   6512  C CE2 . PHE B 1 468 ? 32.198  0.337   34.103  1.00 60.00  ? 477  PHE B CE2 1 
ATOM   6513  C CZ  . PHE B 1 468 ? 31.493  0.803   35.251  1.00 60.34  ? 477  PHE B CZ  1 
ATOM   6514  N N   . TYR B 1 469 ? 35.434  -2.748  38.058  1.00 62.71  ? 478  TYR B N   1 
ATOM   6515  C CA  . TYR B 1 469 ? 34.947  -2.780  39.447  1.00 61.51  ? 478  TYR B CA  1 
ATOM   6516  C C   . TYR B 1 469 ? 35.972  -3.105  40.562  1.00 61.68  ? 478  TYR B C   1 
ATOM   6517  O O   . TYR B 1 469 ? 36.883  -3.948  40.396  1.00 62.97  ? 478  TYR B O   1 
ATOM   6518  C CB  . TYR B 1 469 ? 33.675  -3.640  39.511  1.00 61.93  ? 478  TYR B CB  1 
ATOM   6519  C CG  . TYR B 1 469 ? 33.550  -4.566  40.699  1.00 62.89  ? 478  TYR B CG  1 
ATOM   6520  C CD1 . TYR B 1 469 ? 33.001  -4.126  41.908  1.00 61.49  ? 478  TYR B CD1 1 
ATOM   6521  C CD2 . TYR B 1 469 ? 33.956  -5.898  40.595  1.00 65.03  ? 478  TYR B CD2 1 
ATOM   6522  C CE1 . TYR B 1 469 ? 32.872  -4.988  42.991  1.00 63.59  ? 478  TYR B CE1 1 
ATOM   6523  C CE2 . TYR B 1 469 ? 33.841  -6.771  41.668  1.00 66.63  ? 478  TYR B CE2 1 
ATOM   6524  C CZ  . TYR B 1 469 ? 33.296  -6.315  42.869  1.00 66.25  ? 478  TYR B CZ  1 
ATOM   6525  O OH  . TYR B 1 469 ? 33.187  -7.189  43.943  1.00 67.88  ? 478  TYR B OH  1 
ATOM   6526  N N   . ASP B 1 470 ? 35.807  -2.424  41.696  1.00 59.77  ? 479  ASP B N   1 
ATOM   6527  C CA  . ASP B 1 470 ? 36.795  -2.531  42.759  1.00 60.02  ? 479  ASP B CA  1 
ATOM   6528  C C   . ASP B 1 470 ? 36.271  -2.810  44.176  1.00 59.00  ? 479  ASP B C   1 
ATOM   6529  O O   . ASP B 1 470 ? 35.753  -1.907  44.852  1.00 57.84  ? 479  ASP B O   1 
ATOM   6530  C CB  . ASP B 1 470 ? 37.739  -1.328  42.754  1.00 59.74  ? 479  ASP B CB  1 
ATOM   6531  C CG  . ASP B 1 470 ? 39.069  -1.660  43.384  1.00 62.80  ? 479  ASP B CG  1 
ATOM   6532  O OD1 . ASP B 1 470 ? 39.570  -2.795  43.156  1.00 66.00  ? 479  ASP B OD1 1 
ATOM   6533  O OD2 . ASP B 1 470 ? 39.605  -0.797  44.115  1.00 64.34  ? 479  ASP B OD2 1 
ATOM   6534  N N   . PRO B 1 471 ? 36.465  -4.058  44.652  1.00 59.51  ? 480  PRO B N   1 
ATOM   6535  C CA  . PRO B 1 471 ? 35.785  -4.451  45.865  1.00 58.64  ? 480  PRO B CA  1 
ATOM   6536  C C   . PRO B 1 471 ? 36.291  -3.682  47.064  1.00 57.28  ? 480  PRO B C   1 
ATOM   6537  O O   . PRO B 1 471 ? 37.423  -3.191  47.081  1.00 56.80  ? 480  PRO B O   1 
ATOM   6538  C CB  . PRO B 1 471 ? 36.134  -5.934  45.989  1.00 60.69  ? 480  PRO B CB  1 
ATOM   6539  C CG  . PRO B 1 471 ? 37.472  -6.046  45.366  1.00 62.18  ? 480  PRO B CG  1 
ATOM   6540  C CD  . PRO B 1 471 ? 37.454  -5.070  44.224  1.00 61.31  ? 480  PRO B CD  1 
ATOM   6541  N N   . LEU B 1 472 ? 35.418  -3.559  48.044  1.00 56.22  ? 481  LEU B N   1 
ATOM   6542  C CA  . LEU B 1 472 ? 35.797  -3.071  49.346  1.00 55.59  ? 481  LEU B CA  1 
ATOM   6543  C C   . LEU B 1 472 ? 36.129  -4.238  50.253  1.00 56.82  ? 481  LEU B C   1 
ATOM   6544  O O   . LEU B 1 472 ? 35.366  -5.207  50.327  1.00 57.48  ? 481  LEU B O   1 
ATOM   6545  C CB  . LEU B 1 472 ? 34.644  -2.292  49.955  1.00 54.20  ? 481  LEU B CB  1 
ATOM   6546  C CG  . LEU B 1 472 ? 35.109  -1.226  50.936  1.00 53.42  ? 481  LEU B CG  1 
ATOM   6547  C CD1 . LEU B 1 472 ? 36.572  -0.775  50.627  1.00 54.36  ? 481  LEU B CD1 1 
ATOM   6548  C CD2 . LEU B 1 472 ? 34.111  -0.059  50.915  1.00 50.30  ? 481  LEU B CD2 1 
ATOM   6549  N N   . VAL B 1 473 ? 37.251  -4.150  50.959  1.00 57.06  ? 482  VAL B N   1 
ATOM   6550  C CA  . VAL B 1 473 ? 37.590  -5.247  51.847  1.00 58.57  ? 482  VAL B CA  1 
ATOM   6551  C C   . VAL B 1 473 ? 38.140  -4.871  53.220  1.00 58.81  ? 482  VAL B C   1 
ATOM   6552  O O   . VAL B 1 473 ? 38.915  -3.910  53.361  1.00 58.41  ? 482  VAL B O   1 
ATOM   6553  C CB  . VAL B 1 473 ? 38.407  -6.328  51.114  1.00 60.22  ? 482  VAL B CB  1 
ATOM   6554  C CG1 . VAL B 1 473 ? 39.794  -6.539  51.749  1.00 60.54  ? 482  VAL B CG1 1 
ATOM   6555  C CG2 . VAL B 1 473 ? 37.563  -7.611  51.023  1.00 61.51  ? 482  VAL B CG2 1 
ATOM   6556  N N   . PHE B 1 474 ? 37.712  -5.634  54.226  1.00 59.33  ? 483  PHE B N   1 
ATOM   6557  C CA  . PHE B 1 474 ? 37.968  -5.288  55.620  1.00 59.03  ? 483  PHE B CA  1 
ATOM   6558  C C   . PHE B 1 474 ? 39.077  -6.072  56.347  1.00 60.70  ? 483  PHE B C   1 
ATOM   6559  O O   . PHE B 1 474 ? 39.089  -7.309  56.305  1.00 62.53  ? 483  PHE B O   1 
ATOM   6560  C CB  . PHE B 1 474 ? 36.675  -5.384  56.436  1.00 58.66  ? 483  PHE B CB  1 
ATOM   6561  C CG  . PHE B 1 474 ? 36.817  -4.811  57.793  1.00 57.84  ? 483  PHE B CG  1 
ATOM   6562  C CD1 . PHE B 1 474 ? 36.576  -3.453  58.009  1.00 55.33  ? 483  PHE B CD1 1 
ATOM   6563  C CD2 . PHE B 1 474 ? 37.271  -5.602  58.835  1.00 59.18  ? 483  PHE B CD2 1 
ATOM   6564  C CE1 . PHE B 1 474 ? 36.752  -2.894  59.245  1.00 54.98  ? 483  PHE B CE1 1 
ATOM   6565  C CE2 . PHE B 1 474 ? 37.456  -5.064  60.077  1.00 59.04  ? 483  PHE B CE2 1 
ATOM   6566  C CZ  . PHE B 1 474 ? 37.187  -3.694  60.290  1.00 57.27  ? 483  PHE B CZ  1 
ATOM   6567  N N   . PRO B 1 475 ? 39.972  -5.353  57.067  1.00 60.29  ? 484  PRO B N   1 
ATOM   6568  C CA  . PRO B 1 475 ? 41.085  -5.918  57.855  1.00 61.83  ? 484  PRO B CA  1 
ATOM   6569  C C   . PRO B 1 475 ? 40.704  -6.960  58.906  1.00 63.35  ? 484  PRO B C   1 
ATOM   6570  O O   . PRO B 1 475 ? 41.442  -7.123  59.883  1.00 64.27  ? 484  PRO B O   1 
ATOM   6571  C CB  . PRO B 1 475 ? 41.667  -4.685  58.568  1.00 60.86  ? 484  PRO B CB  1 
ATOM   6572  C CG  . PRO B 1 475 ? 40.659  -3.587  58.385  1.00 58.73  ? 484  PRO B CG  1 
ATOM   6573  C CD  . PRO B 1 475 ? 40.017  -3.880  57.077  1.00 58.48  ? 484  PRO B CD  1 
ATOM   6574  N N   . SER B 1 476 ? 39.592  -7.671  58.682  1.00 63.95  ? 485  SER B N   1 
ATOM   6575  C CA  . SER B 1 476 ? 38.970  -8.581  59.668  1.00 65.53  ? 485  SER B CA  1 
ATOM   6576  C C   . SER B 1 476 ? 39.937  -9.280  60.611  1.00 67.26  ? 485  SER B C   1 
ATOM   6577  O O   . SER B 1 476 ? 39.776  -9.237  61.829  1.00 67.46  ? 485  SER B O   1 
ATOM   6578  C CB  . SER B 1 476 ? 38.100  -9.645  58.985  1.00 66.61  ? 485  SER B CB  1 
ATOM   6579  O OG  . SER B 1 476 ? 37.780  -10.702 59.894  1.00 68.71  ? 485  SER B OG  1 
ATOM   6580  N N   . ASP B 1 477 ? 40.932  -9.938  60.047  1.00 68.81  ? 486  ASP B N   1 
ATOM   6581  C CA  . ASP B 1 477 ? 41.837  -10.705 60.871  1.00 71.19  ? 486  ASP B CA  1 
ATOM   6582  C C   . ASP B 1 477 ? 42.598  -9.833  61.862  1.00 70.58  ? 486  ASP B C   1 
ATOM   6583  O O   . ASP B 1 477 ? 42.563  -10.092 63.073  1.00 71.21  ? 486  ASP B O   1 
ATOM   6584  C CB  . ASP B 1 477 ? 42.773  -11.557 60.004  1.00 73.22  ? 486  ASP B CB  1 
ATOM   6585  C CG  . ASP B 1 477 ? 42.135  -12.888 59.589  1.00 75.80  ? 486  ASP B CG  1 
ATOM   6586  O OD1 . ASP B 1 477 ? 40.970  -13.147 59.971  1.00 76.34  ? 486  ASP B OD1 1 
ATOM   6587  O OD2 . ASP B 1 477 ? 42.795  -13.679 58.882  1.00 78.84  ? 486  ASP B OD2 1 
ATOM   6588  N N   . GLU B 1 478 ? 43.242  -8.786  61.346  1.00 69.34  ? 487  GLU B N   1 
ATOM   6589  C CA  . GLU B 1 478 ? 44.059  -7.877  62.153  1.00 68.91  ? 487  GLU B CA  1 
ATOM   6590  C C   . GLU B 1 478 ? 43.250  -7.180  63.274  1.00 66.94  ? 487  GLU B C   1 
ATOM   6591  O O   . GLU B 1 478 ? 43.767  -6.892  64.367  1.00 67.14  ? 487  GLU B O   1 
ATOM   6592  C CB  . GLU B 1 478 ? 44.716  -6.850  61.238  1.00 68.38  ? 487  GLU B CB  1 
ATOM   6593  C CG  . GLU B 1 478 ? 45.848  -6.070  61.895  1.00 71.36  ? 487  GLU B CG  1 
ATOM   6594  C CD  . GLU B 1 478 ? 45.696  -4.547  61.716  1.00 73.17  ? 487  GLU B CD  1 
ATOM   6595  O OE1 . GLU B 1 478 ? 46.379  -3.778  62.451  1.00 74.25  ? 487  GLU B OE1 1 
ATOM   6596  O OE2 . GLU B 1 478 ? 44.881  -4.119  60.856  1.00 72.75  ? 487  GLU B OE2 1 
ATOM   6597  N N   . PHE B 1 479 ? 41.980  -6.916  62.988  1.00 64.73  ? 488  PHE B N   1 
ATOM   6598  C CA  . PHE B 1 479 ? 41.057  -6.412  63.979  1.00 62.96  ? 488  PHE B CA  1 
ATOM   6599  C C   . PHE B 1 479 ? 40.779  -7.479  65.056  1.00 64.15  ? 488  PHE B C   1 
ATOM   6600  O O   . PHE B 1 479 ? 41.040  -7.247  66.242  1.00 64.35  ? 488  PHE B O   1 
ATOM   6601  C CB  . PHE B 1 479 ? 39.783  -5.990  63.274  1.00 61.54  ? 488  PHE B CB  1 
ATOM   6602  C CG  . PHE B 1 479 ? 38.803  -5.286  64.150  1.00 60.47  ? 488  PHE B CG  1 
ATOM   6603  C CD1 . PHE B 1 479 ? 38.794  -3.885  64.226  1.00 58.98  ? 488  PHE B CD1 1 
ATOM   6604  C CD2 . PHE B 1 479 ? 37.860  -6.004  64.874  1.00 60.61  ? 488  PHE B CD2 1 
ATOM   6605  C CE1 . PHE B 1 479 ? 37.854  -3.196  65.029  1.00 57.76  ? 488  PHE B CE1 1 
ATOM   6606  C CE2 . PHE B 1 479 ? 36.931  -5.339  65.682  1.00 59.79  ? 488  PHE B CE2 1 
ATOM   6607  C CZ  . PHE B 1 479 ? 36.926  -3.927  65.757  1.00 58.05  ? 488  PHE B CZ  1 
ATOM   6608  N N   . ASP B 1 480 ? 40.282  -8.648  64.641  1.00 64.91  ? 489  ASP B N   1 
ATOM   6609  C CA  . ASP B 1 480 ? 39.981  -9.756  65.555  1.00 66.56  ? 489  ASP B CA  1 
ATOM   6610  C C   . ASP B 1 480 ? 41.148  -10.081 66.475  1.00 67.69  ? 489  ASP B C   1 
ATOM   6611  O O   . ASP B 1 480 ? 40.977  -10.630 67.576  1.00 68.76  ? 489  ASP B O   1 
ATOM   6612  C CB  . ASP B 1 480 ? 39.616  -11.003 64.758  1.00 68.07  ? 489  ASP B CB  1 
ATOM   6613  C CG  . ASP B 1 480 ? 38.222  -10.949 64.189  1.00 68.26  ? 489  ASP B CG  1 
ATOM   6614  O OD1 . ASP B 1 480 ? 37.571  -9.886  64.250  1.00 68.37  ? 489  ASP B OD1 1 
ATOM   6615  O OD2 . ASP B 1 480 ? 37.771  -11.985 63.674  1.00 70.38  ? 489  ASP B OD2 1 
ATOM   6616  N N   . ALA B 1 481 ? 42.335  -9.752  65.984  1.00 67.37  ? 490  ALA B N   1 
ATOM   6617  C CA  . ALA B 1 481 ? 43.562  -9.906  66.724  1.00 68.26  ? 490  ALA B CA  1 
ATOM   6618  C C   . ALA B 1 481 ? 43.585  -8.952  67.917  1.00 67.21  ? 490  ALA B C   1 
ATOM   6619  O O   . ALA B 1 481 ? 43.716  -9.395  69.077  1.00 68.41  ? 490  ALA B O   1 
ATOM   6620  C CB  . ALA B 1 481 ? 44.719  -9.637  65.823  1.00 68.35  ? 490  ALA B CB  1 
ATOM   6621  N N   . SER B 1 482 ? 43.447  -7.655  67.632  1.00 64.76  ? 491  SER B N   1 
ATOM   6622  C CA  . SER B 1 482 ? 43.368  -6.640  68.673  1.00 63.50  ? 491  SER B CA  1 
ATOM   6623  C C   . SER B 1 482 ? 42.375  -7.000  69.761  1.00 63.69  ? 491  SER B C   1 
ATOM   6624  O O   . SER B 1 482 ? 42.664  -6.840  70.948  1.00 64.28  ? 491  SER B O   1 
ATOM   6625  C CB  . SER B 1 482 ? 42.973  -5.313  68.078  1.00 61.26  ? 491  SER B CB  1 
ATOM   6626  O OG  . SER B 1 482 ? 44.092  -4.731  67.472  1.00 61.51  ? 491  SER B OG  1 
ATOM   6627  N N   . ILE B 1 483 ? 41.214  -7.500  69.356  1.00 63.32  ? 492  ILE B N   1 
ATOM   6628  C CA  . ILE B 1 483 ? 40.184  -7.852  70.318  1.00 63.78  ? 492  ILE B CA  1 
ATOM   6629  C C   . ILE B 1 483 ? 40.501  -9.098  71.143  1.00 66.10  ? 492  ILE B C   1 
ATOM   6630  O O   . ILE B 1 483 ? 40.480  -9.043  72.394  1.00 66.74  ? 492  ILE B O   1 
ATOM   6631  C CB  . ILE B 1 483 ? 38.838  -8.009  69.659  1.00 63.07  ? 492  ILE B CB  1 
ATOM   6632  C CG1 . ILE B 1 483 ? 38.494  -6.709  68.951  1.00 61.44  ? 492  ILE B CG1 1 
ATOM   6633  C CG2 . ILE B 1 483 ? 37.800  -8.389  70.700  1.00 63.65  ? 492  ILE B CG2 1 
ATOM   6634  C CD1 . ILE B 1 483 ? 37.116  -6.170  69.289  1.00 62.11  ? 492  ILE B CD1 1 
ATOM   6635  N N   . SER B 1 484 ? 40.778  -10.214 70.460  1.00 67.42  ? 493  SER B N   1 
ATOM   6636  C CA  . SER B 1 484 ? 41.140  -11.421 71.161  0.50 69.48  ? 493  SER B CA  1 
ATOM   6637  C C   . SER B 1 484 ? 42.265  -11.040 72.105  1.00 69.88  ? 493  SER B C   1 
ATOM   6638  O O   . SER B 1 484 ? 42.589  -11.794 73.024  1.00 72.12  ? 493  SER B O   1 
ATOM   6639  C CB  . SER B 1 484 ? 41.578  -12.515 70.201  0.50 70.83  ? 493  SER B CB  1 
ATOM   6640  O OG  . SER B 1 484 ? 41.881  -13.689 70.930  0.50 72.83  ? 493  SER B OG  1 
ATOM   6641  N N   . GLN B 1 485 ? 42.808  -9.840  71.901  1.00 67.82  ? 494  GLN B N   1 
ATOM   6642  C CA  . GLN B 1 485 ? 43.874  -9.316  72.717  1.00 67.90  ? 494  GLN B CA  1 
ATOM   6643  C C   . GLN B 1 485 ? 43.446  -8.293  73.777  1.00 66.19  ? 494  GLN B C   1 
ATOM   6644  O O   . GLN B 1 485 ? 44.164  -8.059  74.734  1.00 66.73  ? 494  GLN B O   1 
ATOM   6645  C CB  . GLN B 1 485 ? 44.936  -8.748  71.811  1.00 67.70  ? 494  GLN B CB  1 
ATOM   6646  C CG  . GLN B 1 485 ? 46.343  -8.917  72.325  1.00 71.28  ? 494  GLN B CG  1 
ATOM   6647  C CD  . GLN B 1 485 ? 46.931  -7.608  72.814  1.00 73.11  ? 494  GLN B CD  1 
ATOM   6648  O OE1 . GLN B 1 485 ? 46.645  -6.539  72.262  1.00 71.50  ? 494  GLN B OE1 1 
ATOM   6649  N NE2 . GLN B 1 485 ? 47.769  -7.685  73.851  1.00 75.74  ? 494  GLN B NE2 1 
ATOM   6650  N N   . VAL B 1 486 ? 42.280  -7.683  73.624  1.00 64.37  ? 495  VAL B N   1 
ATOM   6651  C CA  . VAL B 1 486 ? 41.713  -6.872  74.709  1.00 63.05  ? 495  VAL B CA  1 
ATOM   6652  C C   . VAL B 1 486 ? 41.302  -7.830  75.791  1.00 64.69  ? 495  VAL B C   1 
ATOM   6653  O O   . VAL B 1 486 ? 41.440  -7.553  76.971  1.00 64.98  ? 495  VAL B O   1 
ATOM   6654  C CB  . VAL B 1 486 ? 40.518  -6.005  74.242  1.00 61.19  ? 495  VAL B CB  1 
ATOM   6655  C CG1 . VAL B 1 486 ? 39.489  -5.836  75.321  1.00 60.64  ? 495  VAL B CG1 1 
ATOM   6656  C CG2 . VAL B 1 486 ? 41.011  -4.639  73.788  1.00 59.03  ? 495  VAL B CG2 1 
ATOM   6657  N N   . ASN B 1 487 ? 40.830  -8.988  75.374  1.00 66.04  ? 496  ASN B N   1 
ATOM   6658  C CA  . ASN B 1 487 ? 40.484  -10.018 76.326  1.00 68.49  ? 496  ASN B CA  1 
ATOM   6659  C C   . ASN B 1 487 ? 41.686  -10.577 77.100  1.00 70.30  ? 496  ASN B C   1 
ATOM   6660  O O   . ASN B 1 487 ? 41.515  -11.032 78.240  1.00 71.55  ? 496  ASN B O   1 
ATOM   6661  C CB  . ASN B 1 487 ? 39.666  -11.107 75.648  1.00 69.57  ? 496  ASN B CB  1 
ATOM   6662  C CG  . ASN B 1 487 ? 38.434  -10.553 74.970  1.00 68.90  ? 496  ASN B CG  1 
ATOM   6663  O OD1 . ASN B 1 487 ? 37.652  -9.825  75.568  1.00 68.38  ? 496  ASN B OD1 1 
ATOM   6664  N ND2 . ASN B 1 487 ? 38.261  -10.887 73.712  1.00 70.39  ? 496  ASN B ND2 1 
ATOM   6665  N N   . GLU B 1 488 ? 42.883  -10.526 76.495  1.00 70.53  ? 497  GLU B N   1 
ATOM   6666  C CA  . GLU B 1 488 ? 44.139  -10.705 77.238  0.50 71.78  ? 497  GLU B CA  1 
ATOM   6667  C C   . GLU B 1 488 ? 44.047  -9.906  78.520  1.00 71.43  ? 497  GLU B C   1 
ATOM   6668  O O   . GLU B 1 488 ? 44.140  -10.463 79.605  1.00 73.18  ? 497  GLU B O   1 
ATOM   6669  C CB  . GLU B 1 488 ? 45.363  -10.191 76.469  0.50 71.24  ? 497  GLU B CB  1 
ATOM   6670  C CG  . GLU B 1 488 ? 45.882  -11.098 75.392  0.50 72.02  ? 497  GLU B CG  1 
ATOM   6671  C CD  . GLU B 1 488 ? 45.784  -12.539 75.785  0.50 73.92  ? 497  GLU B CD  1 
ATOM   6672  O OE1 . GLU B 1 488 ? 45.469  -12.807 76.959  0.50 73.97  ? 497  GLU B OE1 1 
ATOM   6673  O OE2 . GLU B 1 488 ? 46.011  -13.403 74.921  0.50 75.23  ? 497  GLU B OE2 1 
ATOM   6674  N N   . LYS B 1 489 ? 43.822  -8.606  78.386  1.00 69.58  ? 498  LYS B N   1 
ATOM   6675  C CA  . LYS B 1 489 ? 43.874  -7.697  79.514  1.00 69.44  ? 498  LYS B CA  1 
ATOM   6676  C C   . LYS B 1 489 ? 42.789  -7.895  80.532  1.00 70.05  ? 498  LYS B C   1 
ATOM   6677  O O   . LYS B 1 489 ? 43.060  -7.843  81.722  1.00 71.07  ? 498  LYS B O   1 
ATOM   6678  C CB  . LYS B 1 489 ? 43.801  -6.268  79.042  1.00 67.57  ? 498  LYS B CB  1 
ATOM   6679  C CG  . LYS B 1 489 ? 44.681  -5.987  77.879  1.00 68.14  ? 498  LYS B CG  1 
ATOM   6680  C CD  . LYS B 1 489 ? 46.080  -5.769  78.341  1.00 70.79  ? 498  LYS B CD  1 
ATOM   6681  C CE  . LYS B 1 489 ? 46.973  -5.563  77.154  1.00 72.11  ? 498  LYS B CE  1 
ATOM   6682  N NZ  . LYS B 1 489 ? 48.359  -5.524  77.638  1.00 75.39  ? 498  LYS B NZ  1 
ATOM   6683  N N   . ILE B 1 490 ? 41.558  -8.097  80.091  1.00 69.96  ? 499  ILE B N   1 
ATOM   6684  C CA  . ILE B 1 490 ? 40.511  -8.368  81.049  1.00 71.20  ? 499  ILE B CA  1 
ATOM   6685  C C   . ILE B 1 490 ? 40.823  -9.672  81.776  1.00 74.50  ? 499  ILE B C   1 
ATOM   6686  O O   . ILE B 1 490 ? 40.994  -9.670  82.995  1.00 75.30  ? 499  ILE B O   1 
ATOM   6687  C CB  . ILE B 1 490 ? 39.153  -8.439  80.401  1.00 70.43  ? 499  ILE B CB  1 
ATOM   6688  C CG1 . ILE B 1 490 ? 38.942  -7.219  79.510  1.00 67.39  ? 499  ILE B CG1 1 
ATOM   6689  C CG2 . ILE B 1 490 ? 38.073  -8.537  81.479  1.00 71.03  ? 499  ILE B CG2 1 
ATOM   6690  C CD1 . ILE B 1 490 ? 37.863  -7.421  78.478  1.00 65.83  ? 499  ILE B CD1 1 
ATOM   6691  N N   . ASN B 1 491 ? 40.926  -10.771 81.029  1.00 76.88  ? 500  ASN B N   1 
ATOM   6692  C CA  . ASN B 1 491 ? 41.364  -12.051 81.589  1.00 80.98  ? 500  ASN B CA  1 
ATOM   6693  C C   . ASN B 1 491 ? 42.511  -11.905 82.596  1.00 80.61  ? 500  ASN B C   1 
ATOM   6694  O O   . ASN B 1 491 ? 42.538  -12.567 83.621  1.00 82.17  ? 500  ASN B O   1 
ATOM   6695  C CB  . ASN B 1 491 ? 41.756  -13.022 80.468  1.00 83.44  ? 500  ASN B CB  1 
ATOM   6696  C CG  . ASN B 1 491 ? 40.646  -14.001 80.118  1.00 92.50  ? 500  ASN B CG  1 
ATOM   6697  O OD1 . ASN B 1 491 ? 39.525  -13.872 80.606  1.00 93.10  ? 500  ASN B OD1 1 
ATOM   6698  N ND2 . ASN B 1 491 ? 40.965  -14.996 79.267  1.00 108.18 ? 500  ASN B ND2 1 
ATOM   6699  N N   . GLN B 1 492 ? 43.434  -11.009 82.287  1.00 78.63  ? 501  GLN B N   1 
ATOM   6700  C CA  . GLN B 1 492 ? 44.594  -10.709 83.104  1.00 78.74  ? 501  GLN B CA  1 
ATOM   6701  C C   . GLN B 1 492 ? 44.179  -9.969  84.358  1.00 77.47  ? 501  GLN B C   1 
ATOM   6702  O O   . GLN B 1 492 ? 44.642  -10.276 85.457  1.00 78.65  ? 501  GLN B O   1 
ATOM   6703  C CB  . GLN B 1 492 ? 45.507  -9.805  82.285  1.00 77.85  ? 501  GLN B CB  1 
ATOM   6704  C CG  . GLN B 1 492 ? 46.990  -9.777  82.620  1.00 80.78  ? 501  GLN B CG  1 
ATOM   6705  C CD  . GLN B 1 492 ? 47.827  -9.379  81.400  1.00 82.79  ? 501  GLN B CD  1 
ATOM   6706  O OE1 . GLN B 1 492 ? 47.562  -8.372  80.719  1.00 81.35  ? 501  GLN B OE1 1 
ATOM   6707  N NE2 . GLN B 1 492 ? 48.832  -10.189 81.108  1.00 85.95  ? 501  GLN B NE2 1 
ATOM   6708  N N   . SER B 1 493 ? 43.308  -8.985  84.169  1.00 74.79  ? 502  SER B N   1 
ATOM   6709  C CA  . SER B 1 493 ? 42.838  -8.104  85.232  1.00 73.49  ? 502  SER B CA  1 
ATOM   6710  C C   . SER B 1 493 ? 42.079  -8.876  86.318  1.00 74.75  ? 502  SER B C   1 
ATOM   6711  O O   . SER B 1 493 ? 42.401  -8.774  87.507  1.00 75.43  ? 502  SER B O   1 
ATOM   6712  C CB  . SER B 1 493 ? 41.943  -7.021  84.631  1.00 71.37  ? 502  SER B CB  1 
ATOM   6713  O OG  . SER B 1 493 ? 41.704  -5.971  85.544  1.00 70.15  ? 502  SER B OG  1 
ATOM   6714  N N   . LEU B 1 494 ? 41.078  -9.647  85.896  1.00 74.73  ? 503  LEU B N   1 
ATOM   6715  C CA  . LEU B 1 494 ? 40.309  -10.508 86.783  1.00 76.11  ? 503  LEU B CA  1 
ATOM   6716  C C   . LEU B 1 494 ? 41.164  -11.396 87.671  1.00 78.20  ? 503  LEU B C   1 
ATOM   6717  O O   . LEU B 1 494 ? 40.888  -11.548 88.860  1.00 79.38  ? 503  LEU B O   1 
ATOM   6718  C CB  . LEU B 1 494 ? 39.413  -11.402 85.959  1.00 76.59  ? 503  LEU B CB  1 
ATOM   6719  C CG  . LEU B 1 494 ? 38.306  -10.693 85.205  1.00 75.19  ? 503  LEU B CG  1 
ATOM   6720  C CD1 . LEU B 1 494 ? 37.504  -11.747 84.471  1.00 76.66  ? 503  LEU B CD1 1 
ATOM   6721  C CD2 . LEU B 1 494 ? 37.415  -9.874  86.150  1.00 74.91  ? 503  LEU B CD2 1 
ATOM   6722  N N   . ALA B 1 495 ? 42.189  -11.993 87.070  1.00 78.79  ? 504  ALA B N   1 
ATOM   6723  C CA  . ALA B 1 495 ? 43.156  -12.823 87.769  1.00 80.44  ? 504  ALA B CA  1 
ATOM   6724  C C   . ALA B 1 495 ? 43.981  -12.042 88.808  1.00 79.87  ? 504  ALA B C   1 
ATOM   6725  O O   . ALA B 1 495 ? 44.304  -12.579 89.868  1.00 81.60  ? 504  ALA B O   1 
ATOM   6726  C CB  . ALA B 1 495 ? 44.058  -13.504 86.764  1.00 81.16  ? 504  ALA B CB  1 
ATOM   6727  N N   . PHE B 1 496 ? 44.316  -10.788 88.512  1.00 77.36  ? 505  PHE B N   1 
ATOM   6728  C CA  . PHE B 1 496 ? 44.952  -9.940  89.498  1.00 76.83  ? 505  PHE B CA  1 
ATOM   6729  C C   . PHE B 1 496 ? 44.053  -9.716  90.696  1.00 76.97  ? 505  PHE B C   1 
ATOM   6730  O O   . PHE B 1 496 ? 44.517  -9.795  91.820  1.00 78.21  ? 505  PHE B O   1 
ATOM   6731  C CB  . PHE B 1 496 ? 45.347  -8.601  88.912  1.00 74.99  ? 505  PHE B CB  1 
ATOM   6732  C CG  . PHE B 1 496 ? 46.709  -8.585  88.299  1.00 76.14  ? 505  PHE B CG  1 
ATOM   6733  C CD1 . PHE B 1 496 ? 46.873  -8.434  86.928  1.00 76.82  ? 505  PHE B CD1 1 
ATOM   6734  C CD2 . PHE B 1 496 ? 47.842  -8.709  89.088  1.00 77.84  ? 505  PHE B CD2 1 
ATOM   6735  C CE1 . PHE B 1 496 ? 48.159  -8.422  86.356  1.00 77.37  ? 505  PHE B CE1 1 
ATOM   6736  C CE2 . PHE B 1 496 ? 49.122  -8.694  88.526  1.00 78.16  ? 505  PHE B CE2 1 
ATOM   6737  C CZ  . PHE B 1 496 ? 49.277  -8.550  87.163  1.00 77.56  ? 505  PHE B CZ  1 
ATOM   6738  N N   . ILE B 1 497 ? 42.772  -9.447  90.466  1.00 76.04  ? 506  ILE B N   1 
ATOM   6739  C CA  . ILE B 1 497 ? 41.805  -9.303  91.560  1.00 76.62  ? 506  ILE B CA  1 
ATOM   6740  C C   . ILE B 1 497 ? 41.628  -10.600 92.337  1.00 79.49  ? 506  ILE B C   1 
ATOM   6741  O O   . ILE B 1 497 ? 41.757  -10.607 93.556  1.00 80.55  ? 506  ILE B O   1 
ATOM   6742  C CB  . ILE B 1 497 ? 40.452  -8.793  91.055  1.00 75.18  ? 506  ILE B CB  1 
ATOM   6743  C CG1 . ILE B 1 497 ? 40.615  -7.382  90.494  1.00 72.93  ? 506  ILE B CG1 1 
ATOM   6744  C CG2 . ILE B 1 497 ? 39.385  -8.832  92.149  1.00 75.63  ? 506  ILE B CG2 1 
ATOM   6745  C CD1 . ILE B 1 497 ? 41.118  -6.333  91.471  1.00 72.51  ? 506  ILE B CD1 1 
ATOM   6746  N N   . ARG B 1 498 ? 41.330  -11.681 91.619  1.00 81.05  ? 507  ARG B N   1 
ATOM   6747  C CA  . ARG B 1 498 ? 41.356  -13.044 92.145  1.00 84.26  ? 507  ARG B CA  1 
ATOM   6748  C C   . ARG B 1 498 ? 42.414  -13.218 93.238  1.00 85.34  ? 507  ARG B C   1 
ATOM   6749  O O   . ARG B 1 498 ? 42.116  -13.659 94.351  1.00 86.69  ? 507  ARG B O   1 
ATOM   6750  C CB  . ARG B 1 498 ? 41.692  -14.006 91.007  1.00 85.39  ? 507  ARG B CB  1 
ATOM   6751  C CG  . ARG B 1 498 ? 40.580  -14.347 89.992  1.00 87.88  ? 507  ARG B CG  1 
ATOM   6752  C CD  . ARG B 1 498 ? 40.788  -15.804 89.590  1.00 94.41  ? 507  ARG B CD  1 
ATOM   6753  N NE  . ARG B 1 498 ? 41.251  -16.538 90.789  1.00 101.33 ? 507  ARG B NE  1 
ATOM   6754  C CZ  . ARG B 1 498 ? 41.797  -17.762 90.833  1.00 105.27 ? 507  ARG B CZ  1 
ATOM   6755  N NH1 . ARG B 1 498 ? 41.972  -18.477 89.724  1.00 106.45 ? 507  ARG B NH1 1 
ATOM   6756  N NH2 . ARG B 1 498 ? 42.172  -18.282 92.008  1.00 106.68 ? 507  ARG B NH2 1 
ATOM   6757  N N   . LYS B 1 499 ? 43.648  -12.867 92.888  1.00 84.75  ? 508  LYS B N   1 
ATOM   6758  C CA  . LYS B 1 499 ? 44.796  -12.909 93.779  1.00 85.92  ? 508  LYS B CA  1 
ATOM   6759  C C   . LYS B 1 499 ? 44.637  -11.970 94.978  1.00 85.17  ? 508  LYS B C   1 
ATOM   6760  O O   . LYS B 1 499 ? 44.865  -12.376 96.119  1.00 86.92  ? 508  LYS B O   1 
ATOM   6761  C CB  . LYS B 1 499 ? 46.073  -12.585 92.986  1.00 85.27  ? 508  LYS B CB  1 
ATOM   6762  C CG  . LYS B 1 499 ? 47.400  -12.756 93.745  1.00 88.33  ? 508  LYS B CG  1 
ATOM   6763  C CD  . LYS B 1 499 ? 48.084  -14.178 93.606  1.00 93.32  ? 508  LYS B CD  1 
ATOM   6764  C CE  . LYS B 1 499 ? 47.591  -15.316 94.600  1.00 96.18  ? 508  LYS B CE  1 
ATOM   6765  N NZ  . LYS B 1 499 ? 47.946  -15.210 96.055  1.00 95.91  ? 508  LYS B NZ  1 
ATOM   6766  N N   . SER B 1 500 ? 44.242  -10.728 94.720  1.00 82.84  ? 509  SER B N   1 
ATOM   6767  C CA  . SER B 1 500 ? 43.982  -9.755  95.776  1.00 82.25  ? 509  SER B CA  1 
ATOM   6768  C C   . SER B 1 500 ? 42.973  -10.283 96.820  1.00 84.06  ? 509  SER B C   1 
ATOM   6769  O O   . SER B 1 500 ? 43.229  -10.258 98.026  1.00 84.94  ? 509  SER B O   1 
ATOM   6770  C CB  . SER B 1 500 ? 43.488  -8.456  95.153  1.00 79.74  ? 509  SER B CB  1 
ATOM   6771  O OG  . SER B 1 500 ? 43.362  -7.437  96.110  1.00 78.62  ? 509  SER B OG  1 
ATOM   6772  N N   . ASP B 1 501 ? 41.839  -10.788 96.345  1.00 84.82  ? 510  ASP B N   1 
ATOM   6773  C CA  . ASP B 1 501 ? 40.776  -11.273 97.222  1.00 86.82  ? 510  ASP B CA  1 
ATOM   6774  C C   . ASP B 1 501 ? 41.249  -12.389 98.129  1.00 89.49  ? 510  ASP B C   1 
ATOM   6775  O O   . ASP B 1 501 ? 40.945  -12.367 99.318  1.00 90.78  ? 510  ASP B O   1 
ATOM   6776  C CB  . ASP B 1 501 ? 39.540  -11.724 96.424  1.00 87.08  ? 510  ASP B CB  1 
ATOM   6777  C CG  . ASP B 1 501 ? 38.610  -10.550 96.028  1.00 86.10  ? 510  ASP B CG  1 
ATOM   6778  O OD1 . ASP B 1 501 ? 38.168  -9.769  96.901  1.00 87.18  ? 510  ASP B OD1 1 
ATOM   6779  O OD2 . ASP B 1 501 ? 38.295  -10.413 94.830  1.00 85.48  ? 510  ASP B OD2 1 
ATOM   6780  N N   . GLU B 1 502 ? 41.987  -13.354 97.578  1.00 90.82  ? 511  GLU B N   1 
ATOM   6781  C CA  . GLU B 1 502 ? 42.521  -14.468 98.372  1.00 93.86  ? 511  GLU B CA  1 
ATOM   6782  C C   . GLU B 1 502 ? 43.258  -13.946 99.582  1.00 93.94  ? 511  GLU B C   1 
ATOM   6783  O O   . GLU B 1 502 ? 43.048  -14.428 100.705 1.00 95.92  ? 511  GLU B O   1 
ATOM   6784  C CB  . GLU B 1 502 ? 43.480  -15.328 97.560  1.00 94.95  ? 511  GLU B CB  1 
ATOM   6785  C CG  . GLU B 1 502 ? 42.816  -16.436 96.771  1.00 98.61  ? 511  GLU B CG  1 
ATOM   6786  C CD  . GLU B 1 502 ? 43.758  -17.062 95.746  1.00 101.84 ? 511  GLU B CD  1 
ATOM   6787  O OE1 . GLU B 1 502 ? 44.911  -17.409 96.121  1.00 104.13 ? 511  GLU B OE1 1 
ATOM   6788  O OE2 . GLU B 1 502 ? 43.339  -17.203 94.567  1.00 100.62 ? 511  GLU B OE2 1 
ATOM   6789  N N   . LEU B 1 503 ? 44.109  -12.950 99.347  1.00 91.88  ? 512  LEU B N   1 
ATOM   6790  C CA  . LEU B 1 503 ? 44.885  -12.358 100.416 1.00 91.86  ? 512  LEU B CA  1 
ATOM   6791  C C   . LEU B 1 503 ? 44.011  -11.767 101.504 1.00 91.90  ? 512  LEU B C   1 
ATOM   6792  O O   . LEU B 1 503 ? 44.371  -11.810 102.677 1.00 93.37  ? 512  LEU B O   1 
ATOM   6793  C CB  . LEU B 1 503 ? 45.841  -11.313 99.874  1.00 89.95  ? 512  LEU B CB  1 
ATOM   6794  C CG  . LEU B 1 503 ? 46.962  -11.921 99.032  1.00 90.58  ? 512  LEU B CG  1 
ATOM   6795  C CD1 . LEU B 1 503 ? 47.844  -10.853 98.412  1.00 88.96  ? 512  LEU B CD1 1 
ATOM   6796  C CD2 . LEU B 1 503 ? 47.793  -12.844 99.873  1.00 93.18  ? 512  LEU B CD2 1 
ATOM   6797  N N   . LEU B 1 504 ? 42.848  -11.256 101.125 1.00 90.67  ? 513  LEU B N   1 
ATOM   6798  C CA  . LEU B 1 504 ? 41.955  -10.637 102.094 1.00 90.85  ? 513  LEU B CA  1 
ATOM   6799  C C   . LEU B 1 504 ? 41.070  -11.599 102.895 1.00 93.58  ? 513  LEU B C   1 
ATOM   6800  O O   . LEU B 1 504 ? 40.775  -11.335 104.066 1.00 94.24  ? 513  LEU B O   1 
ATOM   6801  C CB  . LEU B 1 504 ? 41.118  -9.583  101.407 1.00 88.57  ? 513  LEU B CB  1 
ATOM   6802  C CG  . LEU B 1 504 ? 42.009  -8.541  100.746 1.00 85.87  ? 513  LEU B CG  1 
ATOM   6803  C CD1 . LEU B 1 504 ? 41.279  -7.989  99.543  1.00 84.80  ? 513  LEU B CD1 1 
ATOM   6804  C CD2 . LEU B 1 504 ? 42.383  -7.447  101.718 1.00 84.26  ? 513  LEU B CD2 1 
ATOM   6805  N N   . HIS B 1 505 ? 40.649  -12.705 102.279 1.00 95.36  ? 514  HIS B N   1 
ATOM   6806  C CA  . HIS B 1 505 ? 39.922  -13.749 103.008 1.00 98.74  ? 514  HIS B CA  1 
ATOM   6807  C C   . HIS B 1 505 ? 40.909  -14.548 103.847 1.00 101.27 ? 514  HIS B C   1 
ATOM   6808  O O   . HIS B 1 505 ? 40.602  -15.617 104.374 1.00 103.86 ? 514  HIS B O   1 
ATOM   6809  C CB  . HIS B 1 505 ? 39.100  -14.620 102.058 1.00 99.30  ? 514  HIS B CB  1 
ATOM   6810  C CG  . HIS B 1 505 ? 38.145  -13.829 101.214 1.00 98.64  ? 514  HIS B CG  1 
ATOM   6811  N ND1 . HIS B 1 505 ? 37.245  -12.928 101.749 1.00 98.64  ? 514  HIS B ND1 1 
ATOM   6812  C CD2 . HIS B 1 505 ? 37.965  -13.783 99.870  1.00 97.97  ? 514  HIS B CD2 1 
ATOM   6813  C CE1 . HIS B 1 505 ? 36.542  -12.374 100.775 1.00 97.00  ? 514  HIS B CE1 1 
ATOM   6814  N NE2 . HIS B 1 505 ? 36.959  -12.875 99.624  1.00 96.49  ? 514  HIS B NE2 1 
ATOM   6815  N N   . ASN B 1 506 ? 42.104  -13.983 103.974 1.00 101.10 ? 515  ASN B N   1 
ATOM   6816  C CA  . ASN B 1 506 ? 43.116  -14.449 104.914 1.00 103.56 ? 515  ASN B CA  1 
ATOM   6817  C C   . ASN B 1 506 ? 43.375  -13.416 106.043 1.00 103.38 ? 515  ASN B C   1 
ATOM   6818  O O   . ASN B 1 506 ? 44.396  -13.479 106.751 1.00 104.30 ? 515  ASN B O   1 
ATOM   6819  C CB  . ASN B 1 506 ? 44.412  -14.747 104.153 1.00 103.44 ? 515  ASN B CB  1 
ATOM   6820  C CG  . ASN B 1 506 ? 44.848  -16.196 104.287 1.00 106.59 ? 515  ASN B CG  1 
ATOM   6821  O OD1 . ASN B 1 506 ? 44.716  -16.965 103.330 1.00 107.43 ? 515  ASN B OD1 1 
ATOM   6822  N ND2 . ASN B 1 506 ? 45.353  -16.584 105.473 1.00 107.91 ? 515  ASN B ND2 1 
ATOM   6823  N N   . VAL B 1 507 ? 42.437  -12.472 106.191 1.00 102.52 ? 516  VAL B N   1 
ATOM   6824  C CA  . VAL B 1 507 ? 42.513  -11.340 107.158 1.00 101.95 ? 516  VAL B CA  1 
ATOM   6825  C C   . VAL B 1 507 ? 41.253  -11.242 108.082 1.00 103.16 ? 516  VAL B C   1 
ATOM   6826  O O   . VAL B 1 507 ? 40.100  -11.033 107.616 1.00 102.64 ? 516  VAL B O   1 
ATOM   6827  C CB  . VAL B 1 507 ? 42.834  -9.968  106.426 1.00 99.23  ? 516  VAL B CB  1 
ATOM   6828  C CG1 . VAL B 1 507 ? 42.564  -8.740  107.332 1.00 98.28  ? 516  VAL B CG1 1 
ATOM   6829  C CG2 . VAL B 1 507 ? 44.281  -9.964  105.899 1.00 97.98  ? 516  VAL B CG2 1 
ATOM   6830  N N   . ASN B 1 508 ? 41.487  -11.384 109.391 1.00 104.48 ? 517  ASN B N   1 
ATOM   6831  C CA  . ASN B 1 508 ? 40.396  -11.519 110.348 1.00 105.83 ? 517  ASN B CA  1 
ATOM   6832  C C   . ASN B 1 508 ? 40.889  -11.342 111.786 1.00 106.74 ? 517  ASN B C   1 
ATOM   6833  O O   . ASN B 1 508 ? 41.782  -10.540 112.050 1.00 105.41 ? 517  ASN B O   1 
ATOM   6834  C CB  . ASN B 1 508 ? 39.741  -12.899 110.157 1.00 107.92 ? 517  ASN B CB  1 
ATOM   6835  C CG  . ASN B 1 508 ? 38.348  -13.008 110.788 1.00 109.96 ? 517  ASN B CG  1 
ATOM   6836  O OD1 . ASN B 1 508 ? 37.999  -12.282 111.730 1.00 111.43 ? 517  ASN B OD1 1 
ATOM   6837  N ND2 . ASN B 1 508 ? 37.553  -13.955 110.280 1.00 110.89 ? 517  ASN B ND2 1 
ATOM   6838  N N   . GLN C 1 26  ? -22.457 -2.733  3.837   1.00 81.72  ? 26   GLN C N   1 
ATOM   6839  C CA  . GLN C 1 26  ? -21.597 -2.997  2.641   1.00 81.04  ? 26   GLN C CA  1 
ATOM   6840  C C   . GLN C 1 26  ? -22.480 -3.429  1.481   1.00 83.08  ? 26   GLN C C   1 
ATOM   6841  O O   . GLN C 1 26  ? -23.693 -3.179  1.490   1.00 85.20  ? 26   GLN C O   1 
ATOM   6842  C CB  . GLN C 1 26  ? -20.582 -4.112  2.924   1.00 81.37  ? 26   GLN C CB  1 
ATOM   6843  C CG  . GLN C 1 26  ? -19.715 -3.905  4.147   1.00 81.30  ? 26   GLN C CG  1 
ATOM   6844  C CD  . GLN C 1 26  ? -20.504 -3.950  5.456   1.00 85.46  ? 26   GLN C CD  1 
ATOM   6845  O OE1 . GLN C 1 26  ? -21.560 -4.603  5.550   1.00 89.15  ? 26   GLN C OE1 1 
ATOM   6846  N NE2 . GLN C 1 26  ? -19.994 -3.248  6.477   1.00 84.45  ? 26   GLN C NE2 1 
ATOM   6847  N N   . ASN C 1 27  ? -21.861 -4.070  0.487   1.00 82.67  ? 27   ASN C N   1 
ATOM   6848  C CA  . ASN C 1 27  ? -22.537 -4.725  -0.638  1.00 83.93  ? 27   ASN C CA  1 
ATOM   6849  C C   . ASN C 1 27  ? -21.582 -4.738  -1.813  1.00 80.89  ? 27   ASN C C   1 
ATOM   6850  O O   . ASN C 1 27  ? -21.854 -4.132  -2.848  1.00 80.18  ? 27   ASN C O   1 
ATOM   6851  C CB  . ASN C 1 27  ? -23.862 -4.032  -1.026  1.00 85.62  ? 27   ASN C CB  1 
ATOM   6852  C CG  . ASN C 1 27  ? -24.711 -4.863  -1.980  1.00 91.33  ? 27   ASN C CG  1 
ATOM   6853  O OD1 . ASN C 1 27  ? -25.059 -6.013  -1.688  1.00 95.62  ? 27   ASN C OD1 1 
ATOM   6854  N ND2 . ASN C 1 27  ? -25.063 -4.275  -3.123  1.00 94.97  ? 27   ASN C ND2 1 
ATOM   6855  N N   . ILE C 1 28  ? -20.450 -5.412  -1.645  1.00 78.33  ? 28   ILE C N   1 
ATOM   6856  C CA  . ILE C 1 28  ? -19.500 -5.560  -2.743  1.00 75.36  ? 28   ILE C CA  1 
ATOM   6857  C C   . ILE C 1 28  ? -19.821 -6.775  -3.585  1.00 77.35  ? 28   ILE C C   1 
ATOM   6858  O O   . ILE C 1 28  ? -20.219 -7.820  -3.071  1.00 79.60  ? 28   ILE C O   1 
ATOM   6859  C CB  . ILE C 1 28  ? -18.059 -5.625  -2.269  1.00 73.00  ? 28   ILE C CB  1 
ATOM   6860  C CG1 . ILE C 1 28  ? -17.955 -6.437  -0.979  1.00 75.17  ? 28   ILE C CG1 1 
ATOM   6861  C CG2 . ILE C 1 28  ? -17.539 -4.227  -2.062  1.00 68.39  ? 28   ILE C CG2 1 
ATOM   6862  C CD1 . ILE C 1 28  ? -17.865 -7.969  -1.157  1.00 79.13  ? 28   ILE C CD1 1 
ATOM   6863  N N   . THR C 1 29  ? -19.659 -6.620  -4.889  1.00 76.06  ? 29   THR C N   1 
ATOM   6864  C CA  . THR C 1 29  ? -19.992 -7.673  -5.822  1.00 78.12  ? 29   THR C CA  1 
ATOM   6865  C C   . THR C 1 29  ? -19.069 -7.568  -6.991  1.00 76.55  ? 29   THR C C   1 
ATOM   6866  O O   . THR C 1 29  ? -18.456 -6.529  -7.221  1.00 73.55  ? 29   THR C O   1 
ATOM   6867  C CB  . THR C 1 29  ? -21.381 -7.492  -6.399  1.00 79.77  ? 29   THR C CB  1 
ATOM   6868  O OG1 . THR C 1 29  ? -22.059 -6.452  -5.691  1.00 78.45  ? 29   THR C OG1 1 
ATOM   6869  C CG2 . THR C 1 29  ? -22.153 -8.804  -6.327  1.00 83.66  ? 29   THR C CG2 1 
ATOM   6870  N N   . GLU C 1 30  ? -18.988 -8.654  -7.738  1.00 78.43  ? 30   GLU C N   1 
ATOM   6871  C CA  . GLU C 1 30  ? -18.291 -8.649  -8.985  1.00 77.63  ? 30   GLU C CA  1 
ATOM   6872  C C   . GLU C 1 30  ? -19.263 -9.174  -9.978  1.00 79.89  ? 30   GLU C C   1 
ATOM   6873  O O   . GLU C 1 30  ? -20.008 -10.093 -9.684  1.00 82.93  ? 30   GLU C O   1 
ATOM   6874  C CB  . GLU C 1 30  ? -17.104 -9.581  -8.914  1.00 78.41  ? 30   GLU C CB  1 
ATOM   6875  C CG  . GLU C 1 30  ? -15.910 -9.111  -9.684  1.00 77.65  ? 30   GLU C CG  1 
ATOM   6876  C CD  . GLU C 1 30  ? -14.636 -9.665  -9.102  1.00 79.49  ? 30   GLU C CD  1 
ATOM   6877  O OE1 . GLU C 1 30  ? -14.539 -10.908 -8.990  1.00 82.61  ? 30   GLU C OE1 1 
ATOM   6878  O OE2 . GLU C 1 30  ? -13.741 -8.860  -8.745  1.00 78.04  ? 30   GLU C OE2 1 
ATOM   6879  N N   . GLU C 1 31  ? -19.285 -8.563  -11.144 1.00 78.59  ? 31   GLU C N   1 
ATOM   6880  C CA  . GLU C 1 31  ? -20.059 -9.089  -12.236 1.00 81.20  ? 31   GLU C CA  1 
ATOM   6881  C C   . GLU C 1 31  ? -19.093 -9.279  -13.392 1.00 80.49  ? 31   GLU C C   1 
ATOM   6882  O O   . GLU C 1 31  ? -18.307 -8.387  -13.702 1.00 77.67  ? 31   GLU C O   1 
ATOM   6883  C CB  . GLU C 1 31  ? -21.215 -8.155  -12.593 1.00 80.98  ? 31   GLU C CB  1 
ATOM   6884  C CG  . GLU C 1 31  ? -21.687 -8.293  -14.028 1.00 84.59  ? 31   GLU C CG  1 
ATOM   6885  C CD  . GLU C 1 31  ? -23.020 -7.648  -14.289 1.00 87.97  ? 31   GLU C CD  1 
ATOM   6886  O OE1 . GLU C 1 31  ? -23.545 -7.812  -15.412 1.00 89.72  ? 31   GLU C OE1 1 
ATOM   6887  O OE2 . GLU C 1 31  ? -23.540 -6.980  -13.376 1.00 88.72  ? 31   GLU C OE2 1 
ATOM   6888  N N   . PHE C 1 32  ? -19.149 -10.454 -14.010 1.00 83.21  ? 32   PHE C N   1 
ATOM   6889  C CA  . PHE C 1 32  ? -18.217 -10.849 -15.058 1.00 83.14  ? 32   PHE C CA  1 
ATOM   6890  C C   . PHE C 1 32  ? -18.836 -10.610 -16.410 1.00 84.20  ? 32   PHE C C   1 
ATOM   6891  O O   . PHE C 1 32  ? -20.017 -10.874 -16.605 1.00 86.67  ? 32   PHE C O   1 
ATOM   6892  C CB  . PHE C 1 32  ? -17.867 -12.320 -14.885 1.00 85.96  ? 32   PHE C CB  1 
ATOM   6893  C CG  . PHE C 1 32  ? -17.246 -12.949 -16.080 1.00 87.15  ? 32   PHE C CG  1 
ATOM   6894  C CD1 . PHE C 1 32  ? -16.025 -12.549 -16.530 1.00 85.32  ? 32   PHE C CD1 1 
ATOM   6895  C CD2 . PHE C 1 32  ? -17.876 -13.979 -16.739 1.00 91.87  ? 32   PHE C CD2 1 
ATOM   6896  C CE1 . PHE C 1 32  ? -15.448 -13.149 -17.627 1.00 87.20  ? 32   PHE C CE1 1 
ATOM   6897  C CE2 . PHE C 1 32  ? -17.294 -14.593 -17.839 1.00 93.84  ? 32   PHE C CE2 1 
ATOM   6898  C CZ  . PHE C 1 32  ? -16.082 -14.174 -18.277 1.00 91.09  ? 32   PHE C CZ  1 
ATOM   6899  N N   . TYR C 1 33  ? -18.044 -10.100 -17.342 1.00 82.72  ? 33   TYR C N   1 
ATOM   6900  C CA  . TYR C 1 33  ? -18.543 -9.816  -18.671 1.00 83.70  ? 33   TYR C CA  1 
ATOM   6901  C C   . TYR C 1 33  ? -17.891 -10.738 -19.697 1.00 85.97  ? 33   TYR C C   1 
ATOM   6902  O O   . TYR C 1 33  ? -16.835 -10.425 -20.232 1.00 84.81  ? 33   TYR C O   1 
ATOM   6903  C CB  . TYR C 1 33  ? -18.328 -8.346  -19.014 1.00 80.11  ? 33   TYR C CB  1 
ATOM   6904  C CG  . TYR C 1 33  ? -19.156 -7.414  -18.172 1.00 79.40  ? 33   TYR C CG  1 
ATOM   6905  C CD1 . TYR C 1 33  ? -18.618 -6.786  -17.069 1.00 77.95  ? 33   TYR C CD1 1 
ATOM   6906  C CD2 . TYR C 1 33  ? -20.486 -7.165  -18.472 1.00 82.58  ? 33   TYR C CD2 1 
ATOM   6907  C CE1 . TYR C 1 33  ? -19.381 -5.914  -16.284 1.00 77.25  ? 33   TYR C CE1 1 
ATOM   6908  C CE2 . TYR C 1 33  ? -21.260 -6.299  -17.691 1.00 82.13  ? 33   TYR C CE2 1 
ATOM   6909  C CZ  . TYR C 1 33  ? -20.696 -5.679  -16.604 1.00 79.13  ? 33   TYR C CZ  1 
ATOM   6910  O OH  . TYR C 1 33  ? -21.454 -4.834  -15.835 1.00 78.79  ? 33   TYR C OH  1 
ATOM   6911  N N   . GLN C 1 34  ? -18.539 -11.870 -19.968 1.00 89.61  ? 34   GLN C N   1 
ATOM   6912  C CA  . GLN C 1 34  ? -18.004 -12.912 -20.836 1.00 92.22  ? 34   GLN C CA  1 
ATOM   6913  C C   . GLN C 1 34  ? -17.613 -12.420 -22.215 1.00 91.20  ? 34   GLN C C   1 
ATOM   6914  O O   . GLN C 1 34  ? -16.677 -12.928 -22.810 1.00 91.93  ? 34   GLN C O   1 
ATOM   6915  C CB  . GLN C 1 34  ? -19.030 -14.038 -20.968 1.00 96.78  ? 34   GLN C CB  1 
ATOM   6916  C CG  . GLN C 1 34  ? -18.522 -15.269 -21.705 1.00 101.39 ? 34   GLN C CG  1 
ATOM   6917  C CD  . GLN C 1 34  ? -19.401 -16.488 -21.482 1.00 107.73 ? 34   GLN C CD  1 
ATOM   6918  O OE1 . GLN C 1 34  ? -20.452 -16.628 -22.104 1.00 110.73 ? 34   GLN C OE1 1 
ATOM   6919  N NE2 . GLN C 1 34  ? -18.966 -17.382 -20.595 1.00 109.84 ? 34   GLN C NE2 1 
ATOM   6920  N N   . SER C 1 35  ? -18.337 -11.427 -22.710 1.00 89.63  ? 35   SER C N   1 
ATOM   6921  C CA  . SER C 1 35  ? -18.177 -10.937 -24.071 1.00 89.13  ? 35   SER C CA  1 
ATOM   6922  C C   . SER C 1 35  ? -17.054 -9.911  -24.186 1.00 85.28  ? 35   SER C C   1 
ATOM   6923  O O   . SER C 1 35  ? -16.864 -9.293  -25.236 1.00 84.43  ? 35   SER C O   1 
ATOM   6924  C CB  . SER C 1 35  ? -19.476 -10.287 -24.511 1.00 89.29  ? 35   SER C CB  1 
ATOM   6925  O OG  . SER C 1 35  ? -19.812 -9.281  -23.570 1.00 86.70  ? 35   SER C OG  1 
ATOM   6926  N N   . THR C 1 36  ? -16.317 -9.725  -23.100 1.00 82.93  ? 36   THR C N   1 
ATOM   6927  C CA  . THR C 1 36  ? -15.241 -8.745  -23.033 1.00 79.27  ? 36   THR C CA  1 
ATOM   6928  C C   . THR C 1 36  ? -14.191 -9.335  -22.126 1.00 78.66  ? 36   THR C C   1 
ATOM   6929  O O   . THR C 1 36  ? -13.299 -8.656  -21.665 1.00 75.82  ? 36   THR C O   1 
ATOM   6930  C CB  . THR C 1 36  ? -15.756 -7.420  -22.431 1.00 76.32  ? 36   THR C CB  1 
ATOM   6931  O OG1 . THR C 1 36  ? -16.840 -6.933  -23.224 1.00 78.44  ? 36   THR C OG1 1 
ATOM   6932  C CG2 . THR C 1 36  ? -14.702 -6.359  -22.414 1.00 72.97  ? 36   THR C CG2 1 
ATOM   6933  N N   . CYS C 1 37  ? -14.315 -10.619 -21.853 1.00 81.65  ? 37   CYS C N   1 
ATOM   6934  C CA  . CYS C 1 37  ? -13.446 -11.273 -20.899 1.00 81.89  ? 37   CYS C CA  1 
ATOM   6935  C C   . CYS C 1 37  ? -12.917 -10.323 -19.824 1.00 78.06  ? 37   CYS C C   1 
ATOM   6936  O O   . CYS C 1 37  ? -11.712 -10.230 -19.611 1.00 77.06  ? 37   CYS C O   1 
ATOM   6937  C CB  . CYS C 1 37  ? -12.290 -11.943 -21.618 1.00 83.30  ? 37   CYS C CB  1 
ATOM   6938  S SG  . CYS C 1 37  ? -11.700 -13.373 -20.712 1.00 87.42  ? 37   CYS C SG  1 
ATOM   6939  N N   . SER C 1 38  ? -13.821 -9.610  -19.159 1.00 76.25  ? 38   SER C N   1 
ATOM   6940  C CA  . SER C 1 38  ? -13.442 -8.656  -18.116 1.00 72.40  ? 38   SER C CA  1 
ATOM   6941  C C   . SER C 1 38  ? -14.423 -8.689  -16.949 1.00 72.11  ? 38   SER C C   1 
ATOM   6942  O O   . SER C 1 38  ? -15.591 -9.046  -17.116 1.00 74.14  ? 38   SER C O   1 
ATOM   6943  C CB  . SER C 1 38  ? -13.331 -7.240  -18.695 1.00 69.63  ? 38   SER C CB  1 
ATOM   6944  O OG  . SER C 1 38  ? -14.448 -6.915  -19.499 1.00 70.72  ? 38   SER C OG  1 
ATOM   6945  N N   . ALA C 1 39  ? -13.943 -8.309  -15.772 1.00 69.57  ? 39   ALA C N   1 
ATOM   6946  C CA  . ALA C 1 39  ? -14.727 -8.394  -14.551 1.00 69.62  ? 39   ALA C CA  1 
ATOM   6947  C C   . ALA C 1 39  ? -14.687 -7.097  -13.783 1.00 66.33  ? 39   ALA C C   1 
ATOM   6948  O O   . ALA C 1 39  ? -13.640 -6.505  -13.636 1.00 64.26  ? 39   ALA C O   1 
ATOM   6949  C CB  . ALA C 1 39  ? -14.195 -9.511  -13.679 1.00 71.10  ? 39   ALA C CB  1 
ATOM   6950  N N   . VAL C 1 40  ? -15.824 -6.668  -13.264 1.00 66.19  ? 40   VAL C N   1 
ATOM   6951  C CA  . VAL C 1 40  ? -15.875 -5.453  -12.469 1.00 63.30  ? 40   VAL C CA  1 
ATOM   6952  C C   . VAL C 1 40  ? -16.344 -5.698  -11.055 1.00 63.89  ? 40   VAL C C   1 
ATOM   6953  O O   . VAL C 1 40  ? -17.385 -6.301  -10.828 1.00 66.40  ? 40   VAL C O   1 
ATOM   6954  C CB  . VAL C 1 40  ? -16.803 -4.419  -13.099 1.00 62.27  ? 40   VAL C CB  1 
ATOM   6955  C CG1 . VAL C 1 40  ? -17.023 -3.277  -12.167 1.00 60.19  ? 40   VAL C CG1 1 
ATOM   6956  C CG2 . VAL C 1 40  ? -16.205 -3.900  -14.353 1.00 61.31  ? 40   VAL C CG2 1 
ATOM   6957  N N   . SER C 1 41  ? -15.580 -5.208  -10.100 1.00 61.93  ? 41   SER C N   1 
ATOM   6958  C CA  . SER C 1 41  ? -16.013 -5.233  -8.713  1.00 62.38  ? 41   SER C CA  1 
ATOM   6959  C C   . SER C 1 41  ? -16.774 -3.942  -8.412  1.00 60.84  ? 41   SER C C   1 
ATOM   6960  O O   . SER C 1 41  ? -16.296 -2.856  -8.724  1.00 58.35  ? 41   SER C O   1 
ATOM   6961  C CB  . SER C 1 41  ? -14.804 -5.369  -7.796  1.00 61.15  ? 41   SER C CB  1 
ATOM   6962  O OG  . SER C 1 41  ? -13.845 -6.234  -8.376  1.00 62.80  ? 41   SER C OG  1 
ATOM   6963  N N   . LYS C 1 42  ? -17.952 -4.053  -7.808  1.00 62.60  ? 42   LYS C N   1 
ATOM   6964  C CA  . LYS C 1 42  ? -18.837 -2.896  -7.659  1.00 62.07  ? 42   LYS C CA  1 
ATOM   6965  C C   . LYS C 1 42  ? -19.229 -2.659  -6.206  1.00 61.68  ? 42   LYS C C   1 
ATOM   6966  O O   . LYS C 1 42  ? -19.117 -3.564  -5.370  1.00 63.03  ? 42   LYS C O   1 
ATOM   6967  C CB  . LYS C 1 42  ? -20.113 -3.104  -8.468  1.00 64.72  ? 42   LYS C CB  1 
ATOM   6968  C CG  . LYS C 1 42  ? -19.940 -3.464  -9.925  1.00 67.44  ? 42   LYS C CG  1 
ATOM   6969  C CD  . LYS C 1 42  ? -21.289 -3.900  -10.548 1.00 73.63  ? 42   LYS C CD  1 
ATOM   6970  C CE  . LYS C 1 42  ? -21.167 -4.190  -12.056 1.00 75.62  ? 42   LYS C CE  1 
ATOM   6971  N NZ  . LYS C 1 42  ? -22.482 -4.157  -12.750 1.00 78.61  ? 42   LYS C NZ  1 
ATOM   6972  N N   . GLY C 1 43  ? -19.701 -1.444  -5.917  1.00 59.97  ? 43   GLY C N   1 
ATOM   6973  C CA  . GLY C 1 43  ? -20.318 -1.148  -4.631  1.00 59.92  ? 43   GLY C CA  1 
ATOM   6974  C C   . GLY C 1 43  ? -19.369 -0.558  -3.628  1.00 57.48  ? 43   GLY C C   1 
ATOM   6975  O O   . GLY C 1 43  ? -19.516 -0.739  -2.423  1.00 57.96  ? 43   GLY C O   1 
ATOM   6976  N N   . TYR C 1 44  ? -18.382 0.156   -4.138  1.00 55.08  ? 44   TYR C N   1 
ATOM   6977  C CA  . TYR C 1 44  ? -17.395 0.812   -3.307  1.00 52.28  ? 44   TYR C CA  1 
ATOM   6978  C C   . TYR C 1 44  ? -17.736 2.273   -3.229  1.00 50.56  ? 44   TYR C C   1 
ATOM   6979  O O   . TYR C 1 44  ? -18.416 2.798   -4.112  1.00 51.40  ? 44   TYR C O   1 
ATOM   6980  C CB  . TYR C 1 44  ? -16.037 0.686   -3.949  1.00 50.87  ? 44   TYR C CB  1 
ATOM   6981  C CG  . TYR C 1 44  ? -15.469 -0.695  -3.886  1.00 52.17  ? 44   TYR C CG  1 
ATOM   6982  C CD1 . TYR C 1 44  ? -15.477 -1.506  -5.006  1.00 54.25  ? 44   TYR C CD1 1 
ATOM   6983  C CD2 . TYR C 1 44  ? -14.919 -1.196  -2.705  1.00 51.51  ? 44   TYR C CD2 1 
ATOM   6984  C CE1 . TYR C 1 44  ? -14.953 -2.787  -4.963  1.00 56.16  ? 44   TYR C CE1 1 
ATOM   6985  C CE2 . TYR C 1 44  ? -14.383 -2.471  -2.646  1.00 53.47  ? 44   TYR C CE2 1 
ATOM   6986  C CZ  . TYR C 1 44  ? -14.405 -3.265  -3.786  1.00 56.14  ? 44   TYR C CZ  1 
ATOM   6987  O OH  . TYR C 1 44  ? -13.882 -4.539  -3.777  1.00 58.69  ? 44   TYR C OH  1 
ATOM   6988  N N   . LEU C 1 45  ? -17.253 2.938   -2.189  1.00 48.39  ? 45   LEU C N   1 
ATOM   6989  C CA  . LEU C 1 45  ? -17.561 4.344   -2.017  1.00 46.43  ? 45   LEU C CA  1 
ATOM   6990  C C   . LEU C 1 45  ? -16.336 5.219   -1.928  1.00 43.64  ? 45   LEU C C   1 
ATOM   6991  O O   . LEU C 1 45  ? -15.446 5.030   -1.079  1.00 42.89  ? 45   LEU C O   1 
ATOM   6992  C CB  . LEU C 1 45  ? -18.463 4.551   -0.814  1.00 47.49  ? 45   LEU C CB  1 
ATOM   6993  C CG  . LEU C 1 45  ? -19.819 3.865   -0.946  1.00 49.90  ? 45   LEU C CG  1 
ATOM   6994  C CD1 . LEU C 1 45  ? -20.473 3.609   0.396   1.00 51.37  ? 45   LEU C CD1 1 
ATOM   6995  C CD2 . LEU C 1 45  ? -20.682 4.708   -1.835  1.00 50.41  ? 45   LEU C CD2 1 
ATOM   6996  N N   . SER C 1 46  ? -16.333 6.199   -2.814  1.00 41.98  ? 46   SER C N   1 
ATOM   6997  C CA  . SER C 1 46  ? -15.215 7.061   -3.030  1.00 39.39  ? 46   SER C CA  1 
ATOM   6998  C C   . SER C 1 46  ? -14.874 7.991   -1.875  1.00 38.26  ? 46   SER C C   1 
ATOM   6999  O O   . SER C 1 46  ? -15.696 8.363   -1.022  1.00 38.74  ? 46   SER C O   1 
ATOM   7000  C CB  . SER C 1 46  ? -15.550 7.950   -4.169  1.00 38.53  ? 46   SER C CB  1 
ATOM   7001  O OG  . SER C 1 46  ? -16.539 8.800   -3.691  1.00 38.55  ? 46   SER C OG  1 
ATOM   7002  N N   . ALA C 1 47  ? -13.623 8.400   -1.910  1.00 36.25  ? 47   ALA C N   1 
ATOM   7003  C CA  . ALA C 1 47  ? -13.176 9.491   -1.139  1.00 34.40  ? 47   ALA C CA  1 
ATOM   7004  C C   . ALA C 1 47  ? -11.994 9.871   -1.973  1.00 32.54  ? 47   ALA C C   1 
ATOM   7005  O O   . ALA C 1 47  ? -11.173 9.008   -2.243  1.00 32.99  ? 47   ALA C O   1 
ATOM   7006  C CB  . ALA C 1 47  ? -12.784 8.998   0.206   1.00 34.63  ? 47   ALA C CB  1 
ATOM   7007  N N   . LEU C 1 48  ? -11.930 11.119  -2.443  1.00 30.84  ? 48   LEU C N   1 
ATOM   7008  C CA  . LEU C 1 48  ? -10.892 11.511  -3.411  1.00 29.13  ? 48   LEU C CA  1 
ATOM   7009  C C   . LEU C 1 48  ? -10.087 12.722  -3.010  1.00 27.35  ? 48   LEU C C   1 
ATOM   7010  O O   . LEU C 1 48  ? -10.616 13.810  -2.999  1.00 27.15  ? 48   LEU C O   1 
ATOM   7011  C CB  . LEU C 1 48  ? -11.514 11.773  -4.788  1.00 29.25  ? 48   LEU C CB  1 
ATOM   7012  C CG  . LEU C 1 48  ? -12.606 10.863  -5.382  1.00 30.11  ? 48   LEU C CG  1 
ATOM   7013  C CD1 . LEU C 1 48  ? -12.849 11.188  -6.807  1.00 28.94  ? 48   LEU C CD1 1 
ATOM   7014  C CD2 . LEU C 1 48  ? -12.290 9.389   -5.308  1.00 31.99  ? 48   LEU C CD2 1 
ATOM   7015  N N   . ARG C 1 49  ? -8.804  12.532  -2.726  1.00 26.40  ? 49   ARG C N   1 
ATOM   7016  C CA  . ARG C 1 49  ? -7.884  13.659  -2.413  1.00 25.27  ? 49   ARG C CA  1 
ATOM   7017  C C   . ARG C 1 49  ? -7.921  14.777  -3.441  1.00 24.91  ? 49   ARG C C   1 
ATOM   7018  O O   . ARG C 1 49  ? -7.785  14.527  -4.634  1.00 25.17  ? 49   ARG C O   1 
ATOM   7019  C CB  . ARG C 1 49  ? -6.422  13.195  -2.326  1.00 24.46  ? 49   ARG C CB  1 
ATOM   7020  C CG  . ARG C 1 49  ? -5.630  13.812  -1.227  1.00 22.58  ? 49   ARG C CG  1 
ATOM   7021  C CD  . ARG C 1 49  ? -4.210  13.947  -1.606  1.00 21.01  ? 49   ARG C CD  1 
ATOM   7022  N NE  . ARG C 1 49  ? -4.105  15.280  -2.123  1.00 24.18  ? 49   ARG C NE  1 
ATOM   7023  C CZ  . ARG C 1 49  ? -3.662  15.567  -3.335  1.00 27.32  ? 49   ARG C CZ  1 
ATOM   7024  N NH1 . ARG C 1 49  ? -3.229  14.581  -4.100  1.00 27.77  ? 49   ARG C NH1 1 
ATOM   7025  N NH2 . ARG C 1 49  ? -3.634  16.833  -3.787  1.00 28.47  ? 49   ARG C NH2 1 
ATOM   7026  N N   . THR C 1 50  ? -8.098  16.004  -2.977  1.00 24.54  ? 50   THR C N   1 
ATOM   7027  C CA  . THR C 1 50  ? -7.988  17.147  -3.851  1.00 24.12  ? 50   THR C CA  1 
ATOM   7028  C C   . THR C 1 50  ? -7.269  18.243  -3.137  1.00 23.79  ? 50   THR C C   1 
ATOM   7029  O O   . THR C 1 50  ? -7.186  19.344  -3.668  1.00 23.91  ? 50   THR C O   1 
ATOM   7030  C CB  . THR C 1 50  ? -9.323  17.711  -4.323  1.00 24.43  ? 50   THR C CB  1 
ATOM   7031  O OG1 . THR C 1 50  ? -10.256 17.641  -3.266  1.00 24.73  ? 50   THR C OG1 1 
ATOM   7032  C CG2 . THR C 1 50  ? -9.859  16.927  -5.422  1.00 25.46  ? 50   THR C CG2 1 
ATOM   7033  N N   . GLY C 1 51  ? -6.751  17.981  -1.940  1.00 23.55  ? 51   GLY C N   1 
ATOM   7034  C CA  . GLY C 1 51  ? -5.942  19.014  -1.303  1.00 23.26  ? 51   GLY C CA  1 
ATOM   7035  C C   . GLY C 1 51  ? -5.212  18.547  -0.087  1.00 23.17  ? 51   GLY C C   1 
ATOM   7036  O O   . GLY C 1 51  ? -5.322  17.379  0.290   1.00 23.69  ? 51   GLY C O   1 
ATOM   7037  N N   . TRP C 1 52  ? -4.483  19.457  0.548   1.00 22.74  ? 52   TRP C N   1 
ATOM   7038  C CA  . TRP C 1 52  ? -3.773  19.079  1.734   1.00 22.45  ? 52   TRP C CA  1 
ATOM   7039  C C   . TRP C 1 52  ? -4.052  19.969  2.898   1.00 22.52  ? 52   TRP C C   1 
ATOM   7040  O O   . TRP C 1 52  ? -4.392  21.128  2.752   1.00 22.74  ? 52   TRP C O   1 
ATOM   7041  C CB  . TRP C 1 52  ? -2.318  19.156  1.447   1.00 22.28  ? 52   TRP C CB  1 
ATOM   7042  C CG  . TRP C 1 52  ? -1.850  18.216  0.395   1.00 23.39  ? 52   TRP C CG  1 
ATOM   7043  C CD1 . TRP C 1 52  ? -1.484  18.533  -0.874  1.00 24.48  ? 52   TRP C CD1 1 
ATOM   7044  C CD2 . TRP C 1 52  ? -1.662  16.805  0.525   1.00 23.87  ? 52   TRP C CD2 1 
ATOM   7045  N NE1 . TRP C 1 52  ? -1.085  17.409  -1.542  1.00 24.30  ? 52   TRP C NE1 1 
ATOM   7046  C CE2 . TRP C 1 52  ? -1.192  16.334  -0.706  1.00 24.00  ? 52   TRP C CE2 1 
ATOM   7047  C CE3 . TRP C 1 52  ? -1.846  15.898  1.563   1.00 24.02  ? 52   TRP C CE3 1 
ATOM   7048  C CZ2 . TRP C 1 52  ? -0.919  15.004  -0.933  1.00 24.23  ? 52   TRP C CZ2 1 
ATOM   7049  C CZ3 . TRP C 1 52  ? -1.545  14.583  1.343   1.00 24.16  ? 52   TRP C CZ3 1 
ATOM   7050  C CH2 . TRP C 1 52  ? -1.095  14.144  0.106   1.00 24.51  ? 52   TRP C CH2 1 
ATOM   7051  N N   . TYR C 1 53  ? -3.872  19.419  4.073   1.00 22.63  ? 53   TYR C N   1 
ATOM   7052  C CA  . TYR C 1 53  ? -4.061  20.165  5.270   1.00 23.37  ? 53   TYR C CA  1 
ATOM   7053  C C   . TYR C 1 53  ? -2.769  20.113  6.061   1.00 23.36  ? 53   TYR C C   1 
ATOM   7054  O O   . TYR C 1 53  ? -2.343  19.049  6.508   1.00 23.70  ? 53   TYR C O   1 
ATOM   7055  C CB  . TYR C 1 53  ? -5.197  19.540  6.045   1.00 24.35  ? 53   TYR C CB  1 
ATOM   7056  C CG  . TYR C 1 53  ? -5.480  20.162  7.371   1.00 25.32  ? 53   TYR C CG  1 
ATOM   7057  C CD1 . TYR C 1 53  ? -6.347  21.217  7.485   1.00 27.29  ? 53   TYR C CD1 1 
ATOM   7058  C CD2 . TYR C 1 53  ? -4.904  19.665  8.522   1.00 25.90  ? 53   TYR C CD2 1 
ATOM   7059  C CE1 . TYR C 1 53  ? -6.602  21.790  8.717   1.00 29.13  ? 53   TYR C CE1 1 
ATOM   7060  C CE2 . TYR C 1 53  ? -5.152  20.227  9.752   1.00 27.24  ? 53   TYR C CE2 1 
ATOM   7061  C CZ  . TYR C 1 53  ? -5.996  21.290  9.848   1.00 28.60  ? 53   TYR C CZ  1 
ATOM   7062  O OH  . TYR C 1 53  ? -6.255  21.857  11.070  1.00 29.61  ? 53   TYR C OH  1 
ATOM   7063  N N   . THR C 1 54  ? -2.144  21.275  6.198   1.00 23.39  ? 54   THR C N   1 
ATOM   7064  C CA  . THR C 1 54  ? -0.923  21.512  6.930   1.00 23.38  ? 54   THR C CA  1 
ATOM   7065  C C   . THR C 1 54  ? -1.225  21.583  8.407   1.00 23.92  ? 54   THR C C   1 
ATOM   7066  O O   . THR C 1 54  ? -2.252  22.150  8.773   1.00 24.90  ? 54   THR C O   1 
ATOM   7067  C CB  . THR C 1 54  ? -0.492  22.917  6.524   1.00 23.66  ? 54   THR C CB  1 
ATOM   7068  O OG1 . THR C 1 54  ? 0.268   22.827  5.343   1.00 24.20  ? 54   THR C OG1 1 
ATOM   7069  C CG2 . THR C 1 54  ? 0.316   23.696  7.586   1.00 25.01  ? 54   THR C CG2 1 
ATOM   7070  N N   . SER C 1 55  ? -0.348  21.051  9.260   1.00 23.69  ? 55   SER C N   1 
ATOM   7071  C CA  . SER C 1 55  ? -0.330  21.445  10.665  1.00 24.17  ? 55   SER C CA  1 
ATOM   7072  C C   . SER C 1 55  ? 1.032   21.310  11.260  1.00 24.23  ? 55   SER C C   1 
ATOM   7073  O O   . SER C 1 55  ? 1.752   20.369  10.958  1.00 24.28  ? 55   SER C O   1 
ATOM   7074  C CB  . SER C 1 55  ? -1.254  20.604  11.496  1.00 24.64  ? 55   SER C CB  1 
ATOM   7075  O OG  . SER C 1 55  ? -1.062  20.954  12.845  1.00 25.14  ? 55   SER C OG  1 
ATOM   7076  N N   . VAL C 1 56  ? 1.354   22.214  12.169  1.00 24.77  ? 56   VAL C N   1 
ATOM   7077  C CA  . VAL C 1 56  ? 2.721   22.383  12.622  1.00 24.52  ? 56   VAL C CA  1 
ATOM   7078  C C   . VAL C 1 56  ? 2.888   21.992  14.054  1.00 24.60  ? 56   VAL C C   1 
ATOM   7079  O O   . VAL C 1 56  ? 2.466   22.706  14.987  1.00 25.41  ? 56   VAL C O   1 
ATOM   7080  C CB  . VAL C 1 56  ? 3.086   23.818  12.572  1.00 25.10  ? 56   VAL C CB  1 
ATOM   7081  C CG1 . VAL C 1 56  ? 4.554   23.941  12.488  1.00 24.59  ? 56   VAL C CG1 1 
ATOM   7082  C CG2 . VAL C 1 56  ? 2.350   24.508  11.400  1.00 26.28  ? 56   VAL C CG2 1 
ATOM   7083  N N   . ILE C 1 57  ? 3.552   20.874  14.241  1.00 23.85  ? 57   ILE C N   1 
ATOM   7084  C CA  . ILE C 1 57  ? 3.667   20.333  15.568  1.00 23.73  ? 57   ILE C CA  1 
ATOM   7085  C C   . ILE C 1 57  ? 5.009   20.684  16.127  1.00 23.56  ? 57   ILE C C   1 
ATOM   7086  O O   . ILE C 1 57  ? 5.990   20.647  15.393  1.00 23.21  ? 57   ILE C O   1 
ATOM   7087  C CB  . ILE C 1 57  ? 3.432   18.877  15.508  1.00 23.28  ? 57   ILE C CB  1 
ATOM   7088  C CG1 . ILE C 1 57  ? 1.990   18.706  15.073  1.00 24.10  ? 57   ILE C CG1 1 
ATOM   7089  C CG2 . ILE C 1 57  ? 3.630   18.276  16.846  1.00 23.42  ? 57   ILE C CG2 1 
ATOM   7090  C CD1 . ILE C 1 57  ? 1.713   17.434  14.411  1.00 25.80  ? 57   ILE C CD1 1 
ATOM   7091  N N   . THR C 1 58  ? 5.050   21.065  17.405  1.00 23.96  ? 58   THR C N   1 
ATOM   7092  C CA  . THR C 1 58  ? 6.284   21.547  18.028  1.00 24.17  ? 58   THR C CA  1 
ATOM   7093  C C   . THR C 1 58  ? 6.468   20.821  19.307  1.00 24.34  ? 58   THR C C   1 
ATOM   7094  O O   . THR C 1 58  ? 5.559   20.712  20.068  1.00 25.11  ? 58   THR C O   1 
ATOM   7095  C CB  . THR C 1 58  ? 6.211   23.027  18.300  1.00 24.58  ? 58   THR C CB  1 
ATOM   7096  O OG1 . THR C 1 58  ? 5.316   23.612  17.367  1.00 25.87  ? 58   THR C OG1 1 
ATOM   7097  C CG2 . THR C 1 58  ? 7.502   23.666  18.078  1.00 24.45  ? 58   THR C CG2 1 
ATOM   7098  N N   . ILE C 1 59  ? 7.650   20.292  19.528  1.00 24.63  ? 59   ILE C N   1 
ATOM   7099  C CA  . ILE C 1 59  ? 7.910   19.466  20.699  1.00 25.46  ? 59   ILE C CA  1 
ATOM   7100  C C   . ILE C 1 59  ? 9.114   19.926  21.530  1.00 26.64  ? 59   ILE C C   1 
ATOM   7101  O O   . ILE C 1 59  ? 10.251  19.997  21.029  1.00 26.76  ? 59   ILE C O   1 
ATOM   7102  C CB  . ILE C 1 59  ? 8.113   18.032  20.308  1.00 24.51  ? 59   ILE C CB  1 
ATOM   7103  C CG1 . ILE C 1 59  ? 6.851   17.522  19.688  1.00 24.53  ? 59   ILE C CG1 1 
ATOM   7104  C CG2 . ILE C 1 59  ? 8.440   17.221  21.504  1.00 24.23  ? 59   ILE C CG2 1 
ATOM   7105  C CD1 . ILE C 1 59  ? 6.779   16.063  19.690  1.00 25.98  ? 59   ILE C CD1 1 
ATOM   7106  N N   . GLU C 1 60  ? 8.855   20.259  22.791  1.00 28.01  ? 60   GLU C N   1 
ATOM   7107  C CA  . GLU C 1 60  ? 9.895   20.669  23.697  1.00 29.60  ? 60   GLU C CA  1 
ATOM   7108  C C   . GLU C 1 60  ? 10.655  19.407  24.135  1.00 29.71  ? 60   GLU C C   1 
ATOM   7109  O O   . GLU C 1 60  ? 10.044  18.348  24.297  1.00 30.10  ? 60   GLU C O   1 
ATOM   7110  C CB  . GLU C 1 60  ? 9.266   21.372  24.892  1.00 30.59  ? 60   GLU C CB  1 
ATOM   7111  C CG  . GLU C 1 60  ? 8.865   22.827  24.652  1.00 34.17  ? 60   GLU C CG  1 
ATOM   7112  C CD  . GLU C 1 60  ? 8.752   23.685  25.963  1.00 40.06  ? 60   GLU C CD  1 
ATOM   7113  O OE1 . GLU C 1 60  ? 8.436   23.147  27.054  1.00 42.54  ? 60   GLU C OE1 1 
ATOM   7114  O OE2 . GLU C 1 60  ? 8.984   24.920  25.923  1.00 42.25  ? 60   GLU C OE2 1 
ATOM   7115  N N   . LEU C 1 61  ? 11.978  19.489  24.281  1.00 29.86  ? 61   LEU C N   1 
ATOM   7116  C CA  . LEU C 1 61  ? 12.746  18.391  24.863  1.00 29.90  ? 61   LEU C CA  1 
ATOM   7117  C C   . LEU C 1 61  ? 12.647  18.576  26.359  1.00 30.93  ? 61   LEU C C   1 
ATOM   7118  O O   . LEU C 1 61  ? 12.479  19.707  26.809  1.00 31.34  ? 61   LEU C O   1 
ATOM   7119  C CB  . LEU C 1 61  ? 14.199  18.509  24.444  1.00 29.78  ? 61   LEU C CB  1 
ATOM   7120  C CG  . LEU C 1 61  ? 15.263  17.901  25.340  1.00 29.49  ? 61   LEU C CG  1 
ATOM   7121  C CD1 . LEU C 1 61  ? 15.439  16.487  24.950  1.00 29.57  ? 61   LEU C CD1 1 
ATOM   7122  C CD2 . LEU C 1 61  ? 16.550  18.669  25.193  1.00 29.67  ? 61   LEU C CD2 1 
ATOM   7123  N N   . SER C 1 62  ? 12.749  17.493  27.132  1.00 31.69  ? 62   SER C N   1 
ATOM   7124  C CA  . SER C 1 62  ? 12.823  17.621  28.576  1.00 33.12  ? 62   SER C CA  1 
ATOM   7125  C C   . SER C 1 62  ? 14.262  17.499  28.986  1.00 34.23  ? 62   SER C C   1 
ATOM   7126  O O   . SER C 1 62  ? 14.797  16.387  28.987  1.00 34.12  ? 62   SER C O   1 
ATOM   7127  C CB  . SER C 1 62  ? 12.004  16.549  29.232  1.00 33.00  ? 62   SER C CB  1 
ATOM   7128  O OG  . SER C 1 62  ? 10.655  16.785  28.935  1.00 33.52  ? 62   SER C OG  1 
ATOM   7129  N N   . ASN C 1 63  ? 14.894  18.634  29.320  1.00 35.91  ? 63   ASN C N   1 
ATOM   7130  C CA  . ASN C 1 63  ? 16.348  18.657  29.418  1.00 37.16  ? 63   ASN C CA  1 
ATOM   7131  C C   . ASN C 1 63  ? 16.884  18.255  30.763  1.00 38.39  ? 63   ASN C C   1 
ATOM   7132  O O   . ASN C 1 63  ? 16.272  18.516  31.781  1.00 39.15  ? 63   ASN C O   1 
ATOM   7133  C CB  . ASN C 1 63  ? 16.907  20.015  29.030  1.00 37.71  ? 63   ASN C CB  1 
ATOM   7134  C CG  . ASN C 1 63  ? 18.246  19.901  28.259  1.00 38.57  ? 63   ASN C CG  1 
ATOM   7135  O OD1 . ASN C 1 63  ? 19.140  19.110  28.617  1.00 38.50  ? 63   ASN C OD1 1 
ATOM   7136  N ND2 . ASN C 1 63  ? 18.377  20.697  27.185  1.00 39.03  ? 63   ASN C ND2 1 
ATOM   7137  N N   . ILE C 1 64  ? 18.041  17.615  30.766  1.00 39.66  ? 64   ILE C N   1 
ATOM   7138  C CA  . ILE C 1 64  ? 18.692  17.254  32.010  1.00 41.60  ? 64   ILE C CA  1 
ATOM   7139  C C   . ILE C 1 64  ? 19.666  18.312  32.459  1.00 44.11  ? 64   ILE C C   1 
ATOM   7140  O O   . ILE C 1 64  ? 20.581  18.637  31.706  1.00 44.71  ? 64   ILE C O   1 
ATOM   7141  C CB  . ILE C 1 64  ? 19.573  16.072  31.825  1.00 40.75  ? 64   ILE C CB  1 
ATOM   7142  C CG1 . ILE C 1 64  ? 18.805  14.956  31.159  1.00 39.71  ? 64   ILE C CG1 1 
ATOM   7143  C CG2 . ILE C 1 64  ? 20.077  15.675  33.165  1.00 41.78  ? 64   ILE C CG2 1 
ATOM   7144  C CD1 . ILE C 1 64  ? 19.573  13.735  30.964  1.00 39.27  ? 64   ILE C CD1 1 
ATOM   7145  N N   . LYS C 1 65  ? 19.516  18.826  33.682  1.00 46.84  ? 65   LYS C N   1 
ATOM   7146  C CA  . LYS C 1 65  ? 20.628  19.604  34.329  1.00 49.61  ? 65   LYS C CA  1 
ATOM   7147  C C   . LYS C 1 65  ? 21.560  18.676  35.175  1.00 50.76  ? 65   LYS C C   1 
ATOM   7148  O O   . LYS C 1 65  ? 21.260  18.289  36.349  1.00 51.06  ? 65   LYS C O   1 
ATOM   7149  C CB  . LYS C 1 65  ? 20.145  20.875  35.089  1.00 50.36  ? 65   LYS C CB  1 
ATOM   7150  C CG  . LYS C 1 65  ? 18.690  20.811  35.651  1.00 51.63  ? 65   LYS C CG  1 
ATOM   7151  C CD  . LYS C 1 65  ? 18.430  19.539  36.528  1.00 53.20  ? 65   LYS C CD  1 
ATOM   7152  C CE  . LYS C 1 65  ? 17.282  19.694  37.554  1.00 54.12  ? 65   LYS C CE  1 
ATOM   7153  N NZ  . LYS C 1 65  ? 17.517  18.846  38.776  1.00 54.00  ? 65   LYS C NZ  1 
ATOM   7154  N N   . GLU C 1 66  ? 22.671  18.307  34.526  1.00 51.63  ? 66   GLU C N   1 
ATOM   7155  C CA  . GLU C 1 66  ? 23.627  17.288  34.998  1.00 52.82  ? 66   GLU C CA  1 
ATOM   7156  C C   . GLU C 1 66  ? 24.335  17.605  36.341  1.00 53.99  ? 66   GLU C C   1 
ATOM   7157  O O   . GLU C 1 66  ? 24.767  18.739  36.576  1.00 54.97  ? 66   GLU C O   1 
ATOM   7158  C CB  . GLU C 1 66  ? 24.626  17.042  33.870  1.00 52.79  ? 66   GLU C CB  1 
ATOM   7159  C CG  . GLU C 1 66  ? 25.998  16.541  34.262  1.00 55.15  ? 66   GLU C CG  1 
ATOM   7160  C CD  . GLU C 1 66  ? 27.008  16.758  33.112  1.00 59.13  ? 66   GLU C CD  1 
ATOM   7161  O OE1 . GLU C 1 66  ? 28.125  16.152  33.185  1.00 61.89  ? 66   GLU C OE1 1 
ATOM   7162  O OE2 . GLU C 1 66  ? 26.684  17.525  32.139  1.00 58.91  ? 66   GLU C OE2 1 
ATOM   7163  N N   . ASN C 1 67  ? 24.450  16.612  37.224  1.00 54.49  ? 67   ASN C N   1 
ATOM   7164  C CA  . ASN C 1 67  ? 24.959  16.916  38.575  1.00 55.50  ? 67   ASN C CA  1 
ATOM   7165  C C   . ASN C 1 67  ? 26.315  16.380  38.968  1.00 56.02  ? 67   ASN C C   1 
ATOM   7166  O O   . ASN C 1 67  ? 26.446  15.495  39.864  1.00 56.14  ? 67   ASN C O   1 
ATOM   7167  C CB  . ASN C 1 67  ? 23.904  16.774  39.685  1.00 55.53  ? 67   ASN C CB  1 
ATOM   7168  C CG  . ASN C 1 67  ? 23.215  18.096  39.962  1.00 56.12  ? 67   ASN C CG  1 
ATOM   7169  O OD1 . ASN C 1 67  ? 23.832  19.021  40.516  1.00 56.94  ? 67   ASN C OD1 1 
ATOM   7170  N ND2 . ASN C 1 67  ? 21.950  18.221  39.529  1.00 55.16  ? 67   ASN C ND2 1 
ATOM   7171  N N   . LYS C 1 68  ? 27.294  16.931  38.238  1.00 56.19  ? 68   LYS C N   1 
ATOM   7172  C CA  . LYS C 1 68  ? 28.696  17.009  38.623  1.00 56.96  ? 68   LYS C CA  1 
ATOM   7173  C C   . LYS C 1 68  ? 28.888  16.595  40.087  1.00 57.18  ? 68   LYS C C   1 
ATOM   7174  O O   . LYS C 1 68  ? 28.870  17.420  41.014  1.00 57.97  ? 68   LYS C O   1 
ATOM   7175  C CB  . LYS C 1 68  ? 29.201  18.441  38.419  1.00 58.10  ? 68   LYS C CB  1 
ATOM   7176  C CG  . LYS C 1 68  ? 28.605  19.226  37.197  1.00 57.97  ? 68   LYS C CG  1 
ATOM   7177  C CD  . LYS C 1 68  ? 28.409  20.755  37.524  1.00 59.17  ? 68   LYS C CD  1 
ATOM   7178  C CE  . LYS C 1 68  ? 29.232  21.200  38.792  1.00 60.22  ? 68   LYS C CE  1 
ATOM   7179  N NZ  . LYS C 1 68  ? 29.273  22.675  39.030  1.00 61.44  ? 68   LYS C NZ  1 
ATOM   7180  N N   . CYS C 1 69  ? 28.999  15.289  40.273  1.00 56.38  ? 69   CYS C N   1 
ATOM   7181  C CA  . CYS C 1 69  ? 29.361  14.691  41.523  1.00 56.47  ? 69   CYS C CA  1 
ATOM   7182  C C   . CYS C 1 69  ? 30.571  13.839  41.081  1.00 57.29  ? 69   CYS C C   1 
ATOM   7183  O O   . CYS C 1 69  ? 31.105  14.042  39.970  1.00 57.31  ? 69   CYS C O   1 
ATOM   7184  C CB  . CYS C 1 69  ? 28.227  13.785  41.962  1.00 55.02  ? 69   CYS C CB  1 
ATOM   7185  S SG  . CYS C 1 69  ? 28.570  12.218  41.160  1.00 54.41  ? 69   CYS C SG  1 
ATOM   7186  N N   . ASN C 1 70  ? 30.999  12.891  41.922  1.00 58.20  ? 70   ASN C N   1 
ATOM   7187  C CA  . ASN C 1 70  ? 31.921  11.839  41.487  1.00 59.48  ? 70   ASN C CA  1 
ATOM   7188  C C   . ASN C 1 70  ? 31.192  10.504  41.661  1.00 56.90  ? 70   ASN C C   1 
ATOM   7189  O O   . ASN C 1 70  ? 30.751  10.184  42.763  1.00 56.47  ? 70   ASN C O   1 
ATOM   7190  C CB  . ASN C 1 70  ? 33.221  11.895  42.294  1.00 62.38  ? 70   ASN C CB  1 
ATOM   7191  C CG  . ASN C 1 70  ? 33.683  13.318  42.549  1.00 71.75  ? 70   ASN C CG  1 
ATOM   7192  O OD1 . ASN C 1 70  ? 33.699  14.137  41.621  1.00 75.92  ? 70   ASN C OD1 1 
ATOM   7193  N ND2 . ASN C 1 70  ? 34.051  13.631  43.809  1.00 86.07  ? 70   ASN C ND2 1 
ATOM   7194  N N   . GLY C 1 71  ? 30.999  9.771   40.565  1.00 54.79  ? 71   GLY C N   1 
ATOM   7195  C CA  . GLY C 1 71  ? 30.389  8.444   40.620  1.00 52.46  ? 71   GLY C CA  1 
ATOM   7196  C C   . GLY C 1 71  ? 31.441  7.372   40.848  1.00 52.05  ? 71   GLY C C   1 
ATOM   7197  O O   . GLY C 1 71  ? 32.612  7.675   41.022  1.00 52.83  ? 71   GLY C O   1 
ATOM   7198  N N   . THR C 1 72  ? 31.030  6.112   40.857  1.00 50.96  ? 72   THR C N   1 
ATOM   7199  C CA  . THR C 1 72  ? 31.960  4.982   40.947  1.00 51.13  ? 72   THR C CA  1 
ATOM   7200  C C   . THR C 1 72  ? 32.623  4.798   39.593  1.00 51.70  ? 72   THR C C   1 
ATOM   7201  O O   . THR C 1 72  ? 31.913  4.539   38.615  1.00 51.84  ? 72   THR C O   1 
ATOM   7202  C CB  . THR C 1 72  ? 31.203  3.687   41.297  1.00 51.14  ? 72   THR C CB  1 
ATOM   7203  O OG1 . THR C 1 72  ? 30.533  3.150   40.144  1.00 49.25  ? 72   THR C OG1 1 
ATOM   7204  C CG2 . THR C 1 72  ? 30.175  3.963   42.368  1.00 50.83  ? 72   THR C CG2 1 
ATOM   7205  N N   . ASP C 1 73  ? 33.954  4.921   39.506  1.00 52.42  ? 73   ASP C N   1 
ATOM   7206  C CA  . ASP C 1 73  ? 34.645  5.169   38.183  1.00 52.70  ? 73   ASP C CA  1 
ATOM   7207  C C   . ASP C 1 73  ? 34.179  6.454   37.437  1.00 51.23  ? 73   ASP C C   1 
ATOM   7208  O O   . ASP C 1 73  ? 33.044  6.518   36.922  1.00 49.68  ? 73   ASP C O   1 
ATOM   7209  C CB  . ASP C 1 73  ? 34.566  3.959   37.207  1.00 53.24  ? 73   ASP C CB  1 
ATOM   7210  C CG  . ASP C 1 73  ? 35.301  4.218   35.844  1.00 54.59  ? 73   ASP C CG  1 
ATOM   7211  O OD1 . ASP C 1 73  ? 35.581  5.393   35.475  1.00 54.50  ? 73   ASP C OD1 1 
ATOM   7212  O OD2 . ASP C 1 73  ? 35.616  3.229   35.134  1.00 56.34  ? 73   ASP C OD2 1 
ATOM   7213  N N   . ALA C 1 74  ? 35.067  7.448   37.353  1.00 51.13  ? 74   ALA C N   1 
ATOM   7214  C CA  . ALA C 1 74  ? 34.694  8.694   36.708  1.00 50.38  ? 74   ALA C CA  1 
ATOM   7215  C C   . ALA C 1 74  ? 35.336  8.863   35.346  1.00 50.81  ? 74   ALA C C   1 
ATOM   7216  O O   . ALA C 1 74  ? 35.639  9.976   34.951  1.00 51.08  ? 74   ALA C O   1 
ATOM   7217  C CB  . ALA C 1 74  ? 34.942  9.916   37.624  1.00 50.39  ? 74   ALA C CB  1 
ATOM   7218  N N   . LYS C 1 75  ? 35.551  7.760   34.632  1.00 51.32  ? 75   LYS C N   1 
ATOM   7219  C CA  . LYS C 1 75  ? 35.693  7.813   33.162  1.00 51.98  ? 75   LYS C CA  1 
ATOM   7220  C C   . LYS C 1 75  ? 34.302  7.614   32.542  1.00 50.62  ? 75   LYS C C   1 
ATOM   7221  O O   . LYS C 1 75  ? 34.021  7.995   31.380  1.00 50.64  ? 75   LYS C O   1 
ATOM   7222  C CB  . LYS C 1 75  ? 36.631  6.717   32.663  1.00 53.50  ? 75   LYS C CB  1 
ATOM   7223  C CG  . LYS C 1 75  ? 38.091  6.943   33.015  1.00 56.20  ? 75   LYS C CG  1 
ATOM   7224  C CD  . LYS C 1 75  ? 38.742  5.630   33.425  1.00 59.59  ? 75   LYS C CD  1 
ATOM   7225  C CE  . LYS C 1 75  ? 39.912  5.875   34.402  1.00 62.06  ? 75   LYS C CE  1 
ATOM   7226  N NZ  . LYS C 1 75  ? 39.807  5.014   35.640  1.00 62.74  ? 75   LYS C NZ  1 
ATOM   7227  N N   . VAL C 1 76  ? 33.451  6.991   33.348  1.00 49.43  ? 76   VAL C N   1 
ATOM   7228  C CA  . VAL C 1 76  ? 32.037  6.840   33.098  1.00 47.81  ? 76   VAL C CA  1 
ATOM   7229  C C   . VAL C 1 76  ? 31.339  8.193   33.339  1.00 46.57  ? 76   VAL C C   1 
ATOM   7230  O O   . VAL C 1 76  ? 31.529  8.828   34.384  1.00 46.49  ? 76   VAL C O   1 
ATOM   7231  C CB  . VAL C 1 76  ? 31.500  5.760   34.059  1.00 47.93  ? 76   VAL C CB  1 
ATOM   7232  C CG1 . VAL C 1 76  ? 29.982  5.772   34.126  1.00 47.24  ? 76   VAL C CG1 1 
ATOM   7233  C CG2 . VAL C 1 76  ? 32.053  4.375   33.689  1.00 48.90  ? 76   VAL C CG2 1 
ATOM   7234  N N   . LYS C 1 77  ? 30.555  8.637   32.359  1.00 45.64  ? 77   LYS C N   1 
ATOM   7235  C CA  . LYS C 1 77  ? 29.887  9.939   32.424  1.00 44.87  ? 77   LYS C CA  1 
ATOM   7236  C C   . LYS C 1 77  ? 28.568  9.934   31.697  1.00 43.04  ? 77   LYS C C   1 
ATOM   7237  O O   . LYS C 1 77  ? 28.387  10.654  30.739  1.00 42.71  ? 77   LYS C O   1 
ATOM   7238  C CB  . LYS C 1 77  ? 30.794  11.028  31.853  1.00 45.87  ? 77   LYS C CB  1 
ATOM   7239  C CG  . LYS C 1 77  ? 31.448  11.850  32.941  1.00 49.28  ? 77   LYS C CG  1 
ATOM   7240  C CD  . LYS C 1 77  ? 32.935  12.062  32.681  1.00 54.54  ? 77   LYS C CD  1 
ATOM   7241  C CE  . LYS C 1 77  ? 33.657  12.424  34.004  1.00 57.45  ? 77   LYS C CE  1 
ATOM   7242  N NZ  . LYS C 1 77  ? 34.995  13.106  33.738  1.00 60.97  ? 77   LYS C NZ  1 
ATOM   7243  N N   . LEU C 1 78  ? 27.631  9.143   32.193  1.00 41.96  ? 78   LEU C N   1 
ATOM   7244  C CA  . LEU C 1 78  ? 26.460  8.762   31.414  1.00 40.53  ? 78   LEU C CA  1 
ATOM   7245  C C   . LEU C 1 78  ? 25.687  9.936   30.904  1.00 39.57  ? 78   LEU C C   1 
ATOM   7246  O O   . LEU C 1 78  ? 25.476  10.055  29.698  1.00 39.44  ? 78   LEU C O   1 
ATOM   7247  C CB  . LEU C 1 78  ? 25.559  7.821   32.201  1.00 40.07  ? 78   LEU C CB  1 
ATOM   7248  C CG  . LEU C 1 78  ? 26.259  6.489   32.542  1.00 40.89  ? 78   LEU C CG  1 
ATOM   7249  C CD1 . LEU C 1 78  ? 25.345  5.416   33.105  1.00 40.58  ? 78   LEU C CD1 1 
ATOM   7250  C CD2 . LEU C 1 78  ? 26.999  5.905   31.342  1.00 41.88  ? 78   LEU C CD2 1 
ATOM   7251  N N   . ILE C 1 79  ? 25.307  10.822  31.816  1.00 39.00  ? 79   ILE C N   1 
ATOM   7252  C CA  . ILE C 1 79  ? 24.577  12.027  31.440  1.00 38.12  ? 79   ILE C CA  1 
ATOM   7253  C C   . ILE C 1 79  ? 25.322  12.833  30.363  1.00 38.20  ? 79   ILE C C   1 
ATOM   7254  O O   . ILE C 1 79  ? 24.786  13.025  29.266  1.00 37.94  ? 79   ILE C O   1 
ATOM   7255  C CB  . ILE C 1 79  ? 24.215  12.893  32.642  1.00 38.10  ? 79   ILE C CB  1 
ATOM   7256  C CG1 . ILE C 1 79  ? 23.345  12.101  33.617  1.00 38.22  ? 79   ILE C CG1 1 
ATOM   7257  C CG2 . ILE C 1 79  ? 23.403  14.038  32.193  1.00 37.82  ? 79   ILE C CG2 1 
ATOM   7258  C CD1 . ILE C 1 79  ? 23.078  12.824  34.946  1.00 39.05  ? 79   ILE C CD1 1 
ATOM   7259  N N   . LYS C 1 80  ? 26.556  13.263  30.636  1.00 38.64  ? 80   LYS C N   1 
ATOM   7260  C CA  . LYS C 1 80  ? 27.371  13.910  29.588  1.00 38.80  ? 80   LYS C CA  1 
ATOM   7261  C C   . LYS C 1 80  ? 27.276  13.169  28.267  1.00 37.92  ? 80   LYS C C   1 
ATOM   7262  O O   . LYS C 1 80  ? 27.085  13.767  27.231  1.00 37.55  ? 80   LYS C O   1 
ATOM   7263  C CB  . LYS C 1 80  ? 28.841  13.999  29.998  1.00 40.27  ? 80   LYS C CB  1 
ATOM   7264  C CG  . LYS C 1 80  ? 29.793  14.333  28.831  1.00 42.61  ? 80   LYS C CG  1 
ATOM   7265  C CD  . LYS C 1 80  ? 30.252  15.797  28.860  1.00 46.50  ? 80   LYS C CD  1 
ATOM   7266  C CE  . LYS C 1 80  ? 30.259  16.434  27.459  1.00 48.64  ? 80   LYS C CE  1 
ATOM   7267  N NZ  . LYS C 1 80  ? 28.874  16.991  27.132  1.00 50.36  ? 80   LYS C NZ  1 
ATOM   7268  N N   . GLN C 1 81  ? 27.396  11.857  28.333  1.00 37.69  ? 81   GLN C N   1 
ATOM   7269  C CA  . GLN C 1 81  ? 27.456  11.031  27.154  1.00 37.93  ? 81   GLN C CA  1 
ATOM   7270  C C   . GLN C 1 81  ? 26.118  10.954  26.422  1.00 36.63  ? 81   GLN C C   1 
ATOM   7271  O O   . GLN C 1 81  ? 26.088  11.196  25.208  1.00 36.87  ? 81   GLN C O   1 
ATOM   7272  C CB  . GLN C 1 81  ? 28.030  9.656   27.495  1.00 38.85  ? 81   GLN C CB  1 
ATOM   7273  C CG  . GLN C 1 81  ? 29.502  9.755   27.964  1.00 42.67  ? 81   GLN C CG  1 
ATOM   7274  C CD  . GLN C 1 81  ? 30.198  8.411   28.273  1.00 46.78  ? 81   GLN C CD  1 
ATOM   7275  O OE1 . GLN C 1 81  ? 30.151  7.471   27.463  1.00 48.90  ? 81   GLN C OE1 1 
ATOM   7276  N NE2 . GLN C 1 81  ? 30.894  8.340   29.427  1.00 47.02  ? 81   GLN C NE2 1 
ATOM   7277  N N   . GLU C 1 82  ? 25.021  10.653  27.133  1.00 35.22  ? 82   GLU C N   1 
ATOM   7278  C CA  . GLU C 1 82  ? 23.687  10.646  26.511  1.00 33.88  ? 82   GLU C CA  1 
ATOM   7279  C C   . GLU C 1 82  ? 23.386  11.952  25.843  1.00 33.04  ? 82   GLU C C   1 
ATOM   7280  O O   . GLU C 1 82  ? 22.947  11.954  24.706  1.00 32.90  ? 82   GLU C O   1 
ATOM   7281  C CB  . GLU C 1 82  ? 22.589  10.384  27.508  1.00 33.46  ? 82   GLU C CB  1 
ATOM   7282  C CG  . GLU C 1 82  ? 22.188  8.946   27.625  1.00 35.29  ? 82   GLU C CG  1 
ATOM   7283  C CD  . GLU C 1 82  ? 21.309  8.426   26.482  1.00 37.47  ? 82   GLU C CD  1 
ATOM   7284  O OE1 . GLU C 1 82  ? 20.518  9.210   25.897  1.00 37.51  ? 82   GLU C OE1 1 
ATOM   7285  O OE2 . GLU C 1 82  ? 21.393  7.200   26.187  1.00 38.50  ? 82   GLU C OE2 1 
ATOM   7286  N N   . LEU C 1 83  ? 23.633  13.061  26.534  1.00 32.70  ? 83   LEU C N   1 
ATOM   7287  C CA  . LEU C 1 83  ? 23.401  14.365  25.944  1.00 32.57  ? 83   LEU C CA  1 
ATOM   7288  C C   . LEU C 1 83  ? 24.135  14.521  24.641  1.00 32.83  ? 83   LEU C C   1 
ATOM   7289  O O   . LEU C 1 83  ? 23.589  15.060  23.701  1.00 32.54  ? 83   LEU C O   1 
ATOM   7290  C CB  . LEU C 1 83  ? 23.812  15.492  26.869  1.00 33.25  ? 83   LEU C CB  1 
ATOM   7291  C CG  . LEU C 1 83  ? 22.927  15.912  28.037  1.00 33.52  ? 83   LEU C CG  1 
ATOM   7292  C CD1 . LEU C 1 83  ? 22.638  17.401  27.947  1.00 34.94  ? 83   LEU C CD1 1 
ATOM   7293  C CD2 . LEU C 1 83  ? 21.635  15.183  28.052  1.00 33.45  ? 83   LEU C CD2 1 
ATOM   7294  N N   . ASP C 1 84  ? 25.369  14.040  24.588  1.00 33.54  ? 84   ASP C N   1 
ATOM   7295  C CA  . ASP C 1 84  ? 26.172  14.170  23.393  1.00 34.63  ? 84   ASP C CA  1 
ATOM   7296  C C   . ASP C 1 84  ? 25.566  13.415  22.262  1.00 33.79  ? 84   ASP C C   1 
ATOM   7297  O O   . ASP C 1 84  ? 25.372  13.985  21.183  1.00 33.77  ? 84   ASP C O   1 
ATOM   7298  C CB  . ASP C 1 84  ? 27.602  13.720  23.627  1.00 36.35  ? 84   ASP C CB  1 
ATOM   7299  C CG  . ASP C 1 84  ? 28.404  14.743  24.419  1.00 40.15  ? 84   ASP C CG  1 
ATOM   7300  O OD1 . ASP C 1 84  ? 27.981  15.928  24.467  1.00 43.53  ? 84   ASP C OD1 1 
ATOM   7301  O OD2 . ASP C 1 84  ? 29.454  14.370  25.000  1.00 44.16  ? 84   ASP C OD2 1 
ATOM   7302  N N   . LYS C 1 85  ? 25.254  12.144  22.525  1.00 33.13  ? 85   LYS C N   1 
ATOM   7303  C CA  . LYS C 1 85  ? 24.511  11.293  21.600  1.00 32.32  ? 85   LYS C CA  1 
ATOM   7304  C C   . LYS C 1 85  ? 23.345  12.063  21.026  1.00 31.05  ? 85   LYS C C   1 
ATOM   7305  O O   . LYS C 1 85  ? 23.267  12.285  19.829  1.00 31.03  ? 85   LYS C O   1 
ATOM   7306  C CB  . LYS C 1 85  ? 23.987  10.073  22.326  1.00 32.15  ? 85   LYS C CB  1 
ATOM   7307  C CG  . LYS C 1 85  ? 23.699  8.907   21.409  1.00 32.78  ? 85   LYS C CG  1 
ATOM   7308  C CD  . LYS C 1 85  ? 22.880  7.823   22.097  1.00 33.36  ? 85   LYS C CD  1 
ATOM   7309  C CE  . LYS C 1 85  ? 21.491  8.338   22.366  1.00 34.93  ? 85   LYS C CE  1 
ATOM   7310  N NZ  . LYS C 1 85  ? 20.676  7.301   23.038  1.00 37.52  ? 85   LYS C NZ  1 
ATOM   7311  N N   . TYR C 1 86  ? 22.467  12.508  21.903  1.00 30.00  ? 86   TYR C N   1 
ATOM   7312  C CA  . TYR C 1 86  ? 21.324  13.261  21.491  1.00 29.04  ? 86   TYR C CA  1 
ATOM   7313  C C   . TYR C 1 86  ? 21.711  14.485  20.720  1.00 28.93  ? 86   TYR C C   1 
ATOM   7314  O O   . TYR C 1 86  ? 21.321  14.612  19.570  1.00 28.67  ? 86   TYR C O   1 
ATOM   7315  C CB  . TYR C 1 86  ? 20.474  13.675  22.682  1.00 28.75  ? 86   TYR C CB  1 
ATOM   7316  C CG  . TYR C 1 86  ? 19.348  14.614  22.299  1.00 28.50  ? 86   TYR C CG  1 
ATOM   7317  C CD1 . TYR C 1 86  ? 18.449  14.270  21.295  1.00 29.39  ? 86   TYR C CD1 1 
ATOM   7318  C CD2 . TYR C 1 86  ? 19.190  15.839  22.912  1.00 28.23  ? 86   TYR C CD2 1 
ATOM   7319  C CE1 . TYR C 1 86  ? 17.424  15.117  20.900  1.00 29.03  ? 86   TYR C CE1 1 
ATOM   7320  C CE2 . TYR C 1 86  ? 18.161  16.699  22.541  1.00 28.22  ? 86   TYR C CE2 1 
ATOM   7321  C CZ  . TYR C 1 86  ? 17.276  16.326  21.526  1.00 29.15  ? 86   TYR C CZ  1 
ATOM   7322  O OH  . TYR C 1 86  ? 16.256  17.159  21.092  1.00 28.82  ? 86   TYR C OH  1 
ATOM   7323  N N   . LYS C 1 87  ? 22.458  15.389  21.352  1.00 29.38  ? 87   LYS C N   1 
ATOM   7324  C CA  . LYS C 1 87  ? 22.827  16.675  20.725  1.00 30.06  ? 87   LYS C CA  1 
ATOM   7325  C C   . LYS C 1 87  ? 23.325  16.471  19.303  1.00 30.17  ? 87   LYS C C   1 
ATOM   7326  O O   . LYS C 1 87  ? 23.105  17.313  18.421  1.00 30.39  ? 87   LYS C O   1 
ATOM   7327  C CB  . LYS C 1 87  ? 23.924  17.399  21.496  1.00 30.94  ? 87   LYS C CB  1 
ATOM   7328  C CG  . LYS C 1 87  ? 23.508  17.994  22.786  1.00 32.15  ? 87   LYS C CG  1 
ATOM   7329  C CD  . LYS C 1 87  ? 24.682  18.702  23.444  1.00 35.77  ? 87   LYS C CD  1 
ATOM   7330  C CE  . LYS C 1 87  ? 24.542  18.713  24.960  1.00 36.38  ? 87   LYS C CE  1 
ATOM   7331  N NZ  . LYS C 1 87  ? 24.986  20.023  25.501  1.00 38.34  ? 87   LYS C NZ  1 
ATOM   7332  N N   . ASN C 1 88  ? 24.009  15.349  19.097  1.00 29.93  ? 88   ASN C N   1 
ATOM   7333  C CA  . ASN C 1 88  ? 24.626  15.055  17.828  1.00 29.90  ? 88   ASN C CA  1 
ATOM   7334  C C   . ASN C 1 88  ? 23.612  14.711  16.757  1.00 28.46  ? 88   ASN C C   1 
ATOM   7335  O O   . ASN C 1 88  ? 23.602  15.310  15.674  1.00 28.44  ? 88   ASN C O   1 
ATOM   7336  C CB  . ASN C 1 88  ? 25.657  13.958  18.016  1.00 31.09  ? 88   ASN C CB  1 
ATOM   7337  C CG  . ASN C 1 88  ? 26.080  13.331  16.731  1.00 32.47  ? 88   ASN C CG  1 
ATOM   7338  O OD1 . ASN C 1 88  ? 26.875  13.881  15.953  1.00 34.39  ? 88   ASN C OD1 1 
ATOM   7339  N ND2 . ASN C 1 88  ? 25.573  12.151  16.505  1.00 33.71  ? 88   ASN C ND2 1 
ATOM   7340  N N   . ALA C 1 89  ? 22.752  13.756  17.070  1.00 27.15  ? 89   ALA C N   1 
ATOM   7341  C CA  . ALA C 1 89  ? 21.607  13.434  16.219  1.00 25.92  ? 89   ALA C CA  1 
ATOM   7342  C C   . ALA C 1 89  ? 20.944  14.699  15.702  1.00 24.93  ? 89   ALA C C   1 
ATOM   7343  O O   . ALA C 1 89  ? 20.591  14.792  14.519  1.00 24.79  ? 89   ALA C O   1 
ATOM   7344  C CB  . ALA C 1 89  ? 20.627  12.626  16.972  1.00 25.31  ? 89   ALA C CB  1 
ATOM   7345  N N   . VAL C 1 90  ? 20.812  15.665  16.608  1.00 23.98  ? 90   VAL C N   1 
ATOM   7346  C CA  . VAL C 1 90  ? 20.213  16.965  16.345  1.00 23.14  ? 90   VAL C CA  1 
ATOM   7347  C C   . VAL C 1 90  ? 21.009  17.761  15.343  1.00 23.82  ? 90   VAL C C   1 
ATOM   7348  O O   . VAL C 1 90  ? 20.457  18.294  14.404  1.00 23.78  ? 90   VAL C O   1 
ATOM   7349  C CB  . VAL C 1 90  ? 20.038  17.741  17.642  1.00 22.67  ? 90   VAL C CB  1 
ATOM   7350  C CG1 . VAL C 1 90  ? 19.575  19.124  17.406  1.00 22.42  ? 90   VAL C CG1 1 
ATOM   7351  C CG2 . VAL C 1 90  ? 19.035  17.064  18.447  1.00 22.31  ? 90   VAL C CG2 1 
ATOM   7352  N N   . THR C 1 91  ? 22.319  17.820  15.522  1.00 25.12  ? 91   THR C N   1 
ATOM   7353  C CA  . THR C 1 91  ? 23.183  18.501  14.561  1.00 26.17  ? 91   THR C CA  1 
ATOM   7354  C C   . THR C 1 91  ? 23.043  17.825  13.201  1.00 26.41  ? 91   THR C C   1 
ATOM   7355  O O   . THR C 1 91  ? 22.768  18.494  12.210  1.00 26.56  ? 91   THR C O   1 
ATOM   7356  C CB  . THR C 1 91  ? 24.675  18.571  15.008  1.00 26.86  ? 91   THR C CB  1 
ATOM   7357  O OG1 . THR C 1 91  ? 24.764  18.706  16.425  1.00 26.48  ? 91   THR C OG1 1 
ATOM   7358  C CG2 . THR C 1 91  ? 25.316  19.783  14.422  1.00 28.21  ? 91   THR C CG2 1 
ATOM   7359  N N   . GLU C 1 92  ? 23.176  16.505  13.166  1.00 26.63  ? 92   GLU C N   1 
ATOM   7360  C CA  . GLU C 1 92  ? 22.998  15.779  11.925  1.00 27.42  ? 92   GLU C CA  1 
ATOM   7361  C C   . GLU C 1 92  ? 21.772  16.204  11.145  1.00 26.55  ? 92   GLU C C   1 
ATOM   7362  O O   . GLU C 1 92  ? 21.831  16.438  9.932   1.00 26.35  ? 92   GLU C O   1 
ATOM   7363  C CB  . GLU C 1 92  ? 22.939  14.292  12.177  1.00 27.84  ? 92   GLU C CB  1 
ATOM   7364  C CG  . GLU C 1 92  ? 24.297  13.613  12.154  1.00 31.89  ? 92   GLU C CG  1 
ATOM   7365  C CD  . GLU C 1 92  ? 25.079  13.868  10.869  1.00 37.00  ? 92   GLU C CD  1 
ATOM   7366  O OE1 . GLU C 1 92  ? 24.415  14.001  9.799   1.00 38.40  ? 92   GLU C OE1 1 
ATOM   7367  O OE2 . GLU C 1 92  ? 26.344  13.923  10.937  1.00 38.74  ? 92   GLU C OE2 1 
ATOM   7368  N N   . LEU C 1 93  ? 20.652  16.298  11.854  1.00 25.89  ? 93   LEU C N   1 
ATOM   7369  C CA  . LEU C 1 93  ? 19.399  16.656  11.227  1.00 25.29  ? 93   LEU C CA  1 
ATOM   7370  C C   . LEU C 1 93  ? 19.409  18.086  10.787  1.00 25.88  ? 93   LEU C C   1 
ATOM   7371  O O   . LEU C 1 93  ? 18.973  18.394  9.682   1.00 26.41  ? 93   LEU C O   1 
ATOM   7372  C CB  . LEU C 1 93  ? 18.229  16.391  12.133  1.00 24.06  ? 93   LEU C CB  1 
ATOM   7373  C CG  . LEU C 1 93  ? 17.798  14.947  12.361  1.00 23.46  ? 93   LEU C CG  1 
ATOM   7374  C CD1 . LEU C 1 93  ? 16.848  14.963  13.506  1.00 23.40  ? 93   LEU C CD1 1 
ATOM   7375  C CD2 . LEU C 1 93  ? 17.105  14.302  11.204  1.00 22.54  ? 93   LEU C CD2 1 
ATOM   7376  N N   . GLN C 1 94  ? 19.921  18.962  11.630  1.00 26.48  ? 94   GLN C N   1 
ATOM   7377  C CA  . GLN C 1 94  ? 20.066  20.355  11.250  1.00 27.78  ? 94   GLN C CA  1 
ATOM   7378  C C   . GLN C 1 94  ? 20.724  20.532  9.891   1.00 28.76  ? 94   GLN C C   1 
ATOM   7379  O O   . GLN C 1 94  ? 20.470  21.517  9.174   1.00 29.09  ? 94   GLN C O   1 
ATOM   7380  C CB  . GLN C 1 94  ? 20.948  21.061  12.240  1.00 28.68  ? 94   GLN C CB  1 
ATOM   7381  C CG  . GLN C 1 94  ? 20.308  22.106  13.070  1.00 29.99  ? 94   GLN C CG  1 
ATOM   7382  C CD  . GLN C 1 94  ? 21.090  22.275  14.352  1.00 33.78  ? 94   GLN C CD  1 
ATOM   7383  O OE1 . GLN C 1 94  ? 22.312  22.485  14.361  1.00 36.18  ? 94   GLN C OE1 1 
ATOM   7384  N NE2 . GLN C 1 94  ? 20.404  22.128  15.450  1.00 35.02  ? 94   GLN C NE2 1 
ATOM   7385  N N   . LEU C 1 95  ? 21.599  19.602  9.542   1.00 29.47  ? 95   LEU C N   1 
ATOM   7386  C CA  . LEU C 1 95  ? 22.380  19.823  8.372   1.00 31.11  ? 95   LEU C CA  1 
ATOM   7387  C C   . LEU C 1 95  ? 21.570  19.448  7.154   1.00 32.42  ? 95   LEU C C   1 
ATOM   7388  O O   . LEU C 1 95  ? 21.835  19.919  6.037   1.00 33.86  ? 95   LEU C O   1 
ATOM   7389  C CB  . LEU C 1 95  ? 23.714  19.104  8.459   1.00 31.68  ? 95   LEU C CB  1 
ATOM   7390  C CG  . LEU C 1 95  ? 24.575  19.529  9.661   1.00 30.47  ? 95   LEU C CG  1 
ATOM   7391  C CD1 . LEU C 1 95  ? 25.606  18.498  9.982   1.00 29.55  ? 95   LEU C CD1 1 
ATOM   7392  C CD2 . LEU C 1 95  ? 25.209  20.829  9.443   1.00 29.73  ? 95   LEU C CD2 1 
ATOM   7393  N N   . LEU C 1 96  ? 20.522  18.664  7.359   1.00 32.93  ? 96   LEU C N   1 
ATOM   7394  C CA  . LEU C 1 96  ? 19.653  18.320  6.263   1.00 33.83  ? 96   LEU C CA  1 
ATOM   7395  C C   . LEU C 1 96  ? 18.983  19.477  5.600   1.00 35.25  ? 96   LEU C C   1 
ATOM   7396  O O   . LEU C 1 96  ? 18.645  19.353  4.453   1.00 35.86  ? 96   LEU C O   1 
ATOM   7397  C CB  . LEU C 1 96  ? 18.610  17.385  6.749   1.00 32.83  ? 96   LEU C CB  1 
ATOM   7398  C CG  . LEU C 1 96  ? 19.364  16.090  6.828   1.00 33.02  ? 96   LEU C CG  1 
ATOM   7399  C CD1 . LEU C 1 96  ? 18.372  14.975  6.810   1.00 32.41  ? 96   LEU C CD1 1 
ATOM   7400  C CD2 . LEU C 1 96  ? 20.277  16.008  5.654   1.00 33.54  ? 96   LEU C CD2 1 
ATOM   7401  N N   . MET C 1 97  ? 18.833  20.594  6.303   1.00 37.09  ? 97   MET C N   1 
ATOM   7402  C CA  . MET C 1 97  ? 17.986  21.709  5.887   1.00 39.46  ? 97   MET C CA  1 
ATOM   7403  C C   . MET C 1 97  ? 18.414  22.540  4.678   1.00 41.68  ? 97   MET C C   1 
ATOM   7404  O O   . MET C 1 97  ? 17.551  23.076  3.899   1.00 42.37  ? 97   MET C O   1 
ATOM   7405  C CB  . MET C 1 97  ? 17.745  22.614  7.071   1.00 39.53  ? 97   MET C CB  1 
ATOM   7406  C CG  . MET C 1 97  ? 17.177  21.821  8.258   1.00 42.13  ? 97   MET C CG  1 
ATOM   7407  S SD  . MET C 1 97  ? 15.501  21.038  8.079   1.00 48.23  ? 97   MET C SD  1 
ATOM   7408  C CE  . MET C 1 97  ? 15.301  20.682  6.291   1.00 43.94  ? 97   MET C CE  1 
ATOM   7409  N N   . GLN C 1 98  ? 19.728  22.645  4.484   1.00 43.69  ? 98   GLN C N   1 
ATOM   7410  C CA  . GLN C 1 98  ? 20.217  23.397  3.322   1.00 45.77  ? 98   GLN C CA  1 
ATOM   7411  C C   . GLN C 1 98  ? 21.218  22.530  2.538   1.00 46.69  ? 98   GLN C C   1 
ATOM   7412  O O   . GLN C 1 98  ? 21.460  21.354  2.896   1.00 46.15  ? 98   GLN C O   1 
ATOM   7413  C CB  . GLN C 1 98  ? 20.803  24.761  3.756   1.00 46.97  ? 98   GLN C CB  1 
ATOM   7414  C CG  . GLN C 1 98  ? 20.185  25.373  5.074   1.00 47.66  ? 98   GLN C CG  1 
ATOM   7415  C CD  . GLN C 1 98  ? 20.652  24.677  6.410   1.00 48.79  ? 98   GLN C CD  1 
ATOM   7416  O OE1 . GLN C 1 98  ? 20.554  23.449  6.575   1.00 47.07  ? 98   GLN C OE1 1 
ATOM   7417  N NE2 . GLN C 1 98  ? 21.145  25.487  7.362   1.00 49.15  ? 98   GLN C NE2 1 
ATOM   7418  N N   . VAL C 1 143 ? 54.887  -22.010 119.017 1.00 112.51 ? 152  VAL C N   1 
ATOM   7419  C CA  . VAL C 1 143 ? 53.600  -22.498 119.557 1.00 113.32 ? 152  VAL C CA  1 
ATOM   7420  C C   . VAL C 1 143 ? 52.345  -21.723 118.979 1.00 111.43 ? 152  VAL C C   1 
ATOM   7421  O O   . VAL C 1 143 ? 51.220  -22.219 119.141 1.00 111.94 ? 152  VAL C O   1 
ATOM   7422  C CB  . VAL C 1 143 ? 53.617  -22.690 121.193 1.00 115.74 ? 152  VAL C CB  1 
ATOM   7423  C CG1 . VAL C 1 143 ? 52.277  -23.269 121.772 1.00 116.87 ? 152  VAL C CG1 1 
ATOM   7424  C CG2 . VAL C 1 143 ? 54.845  -23.532 121.685 1.00 117.63 ? 152  VAL C CG2 1 
ATOM   7425  N N   . ALA C 1 144 ? 52.564  -20.549 118.322 1.00 109.47 ? 153  ALA C N   1 
ATOM   7426  C CA  . ALA C 1 144 ? 51.578  -19.637 117.550 1.00 107.36 ? 153  ALA C CA  1 
ATOM   7427  C C   . ALA C 1 144 ? 51.679  -18.085 117.813 1.00 106.46 ? 153  ALA C C   1 
ATOM   7428  O O   . ALA C 1 144 ? 52.744  -17.589 118.144 1.00 106.82 ? 153  ALA C O   1 
ATOM   7429  C CB  . ALA C 1 144 ? 50.090  -20.143 117.521 1.00 107.50 ? 153  ALA C CB  1 
ATOM   7430  N N   . VAL C 1 145 ? 50.603  -17.310 117.684 1.00 105.47 ? 154  VAL C N   1 
ATOM   7431  C CA  . VAL C 1 145 ? 50.782  -15.866 117.402 1.00 104.11 ? 154  VAL C CA  1 
ATOM   7432  C C   . VAL C 1 145 ? 50.141  -14.761 118.268 1.00 104.58 ? 154  VAL C C   1 
ATOM   7433  O O   . VAL C 1 145 ? 48.960  -14.830 118.601 1.00 104.95 ? 154  VAL C O   1 
ATOM   7434  C CB  . VAL C 1 145 ? 50.298  -15.630 116.019 1.00 101.91 ? 154  VAL C CB  1 
ATOM   7435  C CG1 . VAL C 1 145 ? 50.708  -14.252 115.568 1.00 100.55 ? 154  VAL C CG1 1 
ATOM   7436  C CG2 . VAL C 1 145 ? 50.861  -16.733 115.128 1.00 101.57 ? 154  VAL C CG2 1 
ATOM   7437  N N   . SER C 1 146 ? 50.906  -13.711 118.580 1.00 104.63 ? 155  SER C N   1 
ATOM   7438  C CA  . SER C 1 146 ? 50.344  -12.570 119.316 1.00 105.12 ? 155  SER C CA  1 
ATOM   7439  C C   . SER C 1 146 ? 49.554  -11.695 118.385 1.00 103.24 ? 155  SER C C   1 
ATOM   7440  O O   . SER C 1 146 ? 49.750  -11.740 117.161 1.00 101.46 ? 155  SER C O   1 
ATOM   7441  C CB  . SER C 1 146 ? 51.451  -11.673 119.895 1.00 105.89 ? 155  SER C CB  1 
ATOM   7442  O OG  . SER C 1 146 ? 50.896  -10.477 120.501 1.00 106.36 ? 155  SER C OG  1 
ATOM   7443  N N   . LYS C 1 147 ? 48.695  -10.864 118.983 1.00 103.77 ? 156  LYS C N   1 
ATOM   7444  C CA  . LYS C 1 147 ? 48.126  -9.694  118.296 1.00 102.33 ? 156  LYS C CA  1 
ATOM   7445  C C   . LYS C 1 147 ? 49.199  -8.620  118.229 1.00 102.14 ? 156  LYS C C   1 
ATOM   7446  O O   . LYS C 1 147 ? 50.196  -8.717  118.947 1.00 103.45 ? 156  LYS C O   1 
ATOM   7447  C CB  . LYS C 1 147 ? 46.945  -9.154  119.082 1.00 103.38 ? 156  LYS C CB  1 
ATOM   7448  C CG  . LYS C 1 147 ? 46.371  -7.858  118.547 1.00 102.29 ? 156  LYS C CG  1 
ATOM   7449  C CD  . LYS C 1 147 ? 45.253  -8.105  117.543 1.00 100.72 ? 156  LYS C CD  1 
ATOM   7450  C CE  . LYS C 1 147 ? 43.871  -8.089  118.195 1.00 101.88 ? 156  LYS C CE  1 
ATOM   7451  N NZ  . LYS C 1 147 ? 42.881  -8.778  117.331 1.00 100.73 ? 156  LYS C NZ  1 
ATOM   7452  N N   . VAL C 1 148 ? 48.991  -7.583  117.411 1.00 100.70 ? 157  VAL C N   1 
ATOM   7453  C CA  . VAL C 1 148 ? 50.047  -6.571  117.116 1.00 100.38 ? 157  VAL C CA  1 
ATOM   7454  C C   . VAL C 1 148 ? 51.068  -7.175  116.159 1.00 99.23  ? 157  VAL C C   1 
ATOM   7455  O O   . VAL C 1 148 ? 51.318  -6.624  115.086 1.00 97.69  ? 157  VAL C O   1 
ATOM   7456  C CB  . VAL C 1 148 ? 50.786  -5.945  118.401 1.00 102.55 ? 157  VAL C CB  1 
ATOM   7457  C CG1 . VAL C 1 148 ? 52.131  -5.312  117.985 1.00 102.33 ? 157  VAL C CG1 1 
ATOM   7458  C CG2 . VAL C 1 148 ? 49.910  -4.879  118.907 1.00 103.21 ? 157  VAL C CG2 1 
ATOM   7459  N N   . LEU C 1 149 ? 51.654  -8.307  116.527 1.00 100.09 ? 158  LEU C N   1 
ATOM   7460  C CA  . LEU C 1 149 ? 52.373  -9.080  115.544 1.00 99.04  ? 158  LEU C CA  1 
ATOM   7461  C C   . LEU C 1 149 ? 51.403  -9.580  114.497 1.00 97.33  ? 158  LEU C C   1 
ATOM   7462  O O   . LEU C 1 149 ? 51.740  -9.672  113.316 1.00 95.82  ? 158  LEU C O   1 
ATOM   7463  C CB  . LEU C 1 149 ? 53.102  -10.233 116.178 1.00 100.50 ? 158  LEU C CB  1 
ATOM   7464  C CG  . LEU C 1 149 ? 54.415  -9.774  116.789 1.00 101.79 ? 158  LEU C CG  1 
ATOM   7465  C CD1 . LEU C 1 149 ? 54.877  -10.809 117.813 1.00 103.71 ? 158  LEU C CD1 1 
ATOM   7466  C CD2 . LEU C 1 149 ? 55.459  -9.521  115.711 1.00 100.73 ? 158  LEU C CD2 1 
ATOM   7467  N N   . HIS C 1 150 ? 50.182  -9.875  114.922 1.00 97.66  ? 159  HIS C N   1 
ATOM   7468  C CA  . HIS C 1 150 ? 49.157  -10.274 113.974 1.00 96.18  ? 159  HIS C CA  1 
ATOM   7469  C C   . HIS C 1 150 ? 48.615  -9.102  113.143 1.00 94.53  ? 159  HIS C C   1 
ATOM   7470  O O   . HIS C 1 150 ? 48.360  -9.246  111.942 1.00 92.80  ? 159  HIS C O   1 
ATOM   7471  C CB  . HIS C 1 150 ? 48.015  -10.974 114.680 1.00 97.24  ? 159  HIS C CB  1 
ATOM   7472  C CG  . HIS C 1 150 ? 46.959  -11.441 113.742 1.00 96.69  ? 159  HIS C CG  1 
ATOM   7473  N ND1 . HIS C 1 150 ? 45.798  -10.728 113.515 1.00 97.89  ? 159  HIS C ND1 1 
ATOM   7474  C CD2 . HIS C 1 150 ? 46.914  -12.516 112.921 1.00 97.22  ? 159  HIS C CD2 1 
ATOM   7475  C CE1 . HIS C 1 150 ? 45.063  -11.367 112.622 1.00 97.02  ? 159  HIS C CE1 1 
ATOM   7476  N NE2 . HIS C 1 150 ? 45.723  -12.448 112.238 1.00 97.78  ? 159  HIS C NE2 1 
ATOM   7477  N N   . LEU C 1 151 ? 48.409  -7.962  113.803 1.00 95.19  ? 160  LEU C N   1 
ATOM   7478  C CA  . LEU C 1 151 ? 48.122  -6.709  113.124 1.00 93.96  ? 160  LEU C CA  1 
ATOM   7479  C C   . LEU C 1 151 ? 49.265  -6.345  112.194 1.00 93.61  ? 160  LEU C C   1 
ATOM   7480  O O   . LEU C 1 151 ? 49.022  -5.922  111.081 1.00 92.35  ? 160  LEU C O   1 
ATOM   7481  C CB  . LEU C 1 151 ? 47.955  -5.563  114.124 1.00 95.35  ? 160  LEU C CB  1 
ATOM   7482  C CG  . LEU C 1 151 ? 46.594  -5.146  114.716 1.00 96.06  ? 160  LEU C CG  1 
ATOM   7483  C CD1 . LEU C 1 151 ? 46.675  -3.656  114.973 1.00 96.60  ? 160  LEU C CD1 1 
ATOM   7484  C CD2 . LEU C 1 151 ? 45.454  -5.435  113.744 1.00 95.38  ? 160  LEU C CD2 1 
ATOM   7485  N N   . GLU C 1 152 ? 50.513  -6.488  112.638 1.00 95.55  ? 161  GLU C N   1 
ATOM   7486  C CA  . GLU C 1 152 ? 51.641  -6.124  111.786 1.00 95.75  ? 161  GLU C CA  1 
ATOM   7487  C C   . GLU C 1 152 ? 51.517  -6.837  110.468 1.00 94.73  ? 161  GLU C C   1 
ATOM   7488  O O   . GLU C 1 152 ? 51.421  -6.222  109.415 1.00 93.21  ? 161  GLU C O   1 
ATOM   7489  C CB  . GLU C 1 152 ? 52.959  -6.500  112.431 1.00 97.24  ? 161  GLU C CB  1 
ATOM   7490  C CG  . GLU C 1 152 ? 54.172  -6.033  111.658 1.00 97.31  ? 161  GLU C CG  1 
ATOM   7491  C CD  . GLU C 1 152 ? 55.350  -5.826  112.567 1.00 100.02 ? 161  GLU C CD  1 
ATOM   7492  O OE1 . GLU C 1 152 ? 55.848  -6.825  113.126 1.00 100.93 ? 161  GLU C OE1 1 
ATOM   7493  O OE2 . GLU C 1 152 ? 55.767  -4.662  112.739 1.00 101.58 ? 161  GLU C OE2 1 
ATOM   7494  N N   . GLY C 1 153 ? 51.491  -8.153  110.547 1.00 96.34  ? 162  GLY C N   1 
ATOM   7495  C CA  . GLY C 1 153 ? 51.292  -8.995  109.382 1.00 96.64  ? 162  GLY C CA  1 
ATOM   7496  C C   . GLY C 1 153 ? 50.070  -8.623  108.559 1.00 96.15  ? 162  GLY C C   1 
ATOM   7497  O O   . GLY C 1 153 ? 50.089  -8.697  107.330 1.00 94.56  ? 162  GLY C O   1 
ATOM   7498  N N   . GLU C 1 154 ? 49.003  -8.217  109.238 1.00 97.74  ? 163  GLU C N   1 
ATOM   7499  C CA  . GLU C 1 154 ? 47.765  -7.868  108.557 1.00 97.67  ? 163  GLU C CA  1 
ATOM   7500  C C   . GLU C 1 154 ? 48.020  -6.736  107.612 1.00 95.99  ? 163  GLU C C   1 
ATOM   7501  O O   . GLU C 1 154 ? 47.795  -6.891  106.438 1.00 94.59  ? 163  GLU C O   1 
ATOM   7502  C CB  . GLU C 1 154 ? 46.678  -7.458  109.542 1.00 99.48  ? 163  GLU C CB  1 
ATOM   7503  C CG  . GLU C 1 154 ? 45.316  -8.111  109.285 1.00 102.63 ? 163  GLU C CG  1 
ATOM   7504  C CD  . GLU C 1 154 ? 45.229  -9.537  109.877 1.00 108.94 ? 163  GLU C CD  1 
ATOM   7505  O OE1 . GLU C 1 154 ? 45.460  -9.718  111.123 1.00 111.48 ? 163  GLU C OE1 1 
ATOM   7506  O OE2 . GLU C 1 154 ? 44.927  -10.467 109.080 1.00 109.29 ? 163  GLU C OE2 1 
ATOM   7507  N N   . VAL C 1 155 ? 48.496  -5.606  108.124 1.00 96.73  ? 164  VAL C N   1 
ATOM   7508  C CA  . VAL C 1 155 ? 48.858  -4.480  107.283 1.00 95.91  ? 164  VAL C CA  1 
ATOM   7509  C C   . VAL C 1 155 ? 49.635  -4.991  106.084 1.00 95.17  ? 164  VAL C C   1 
ATOM   7510  O O   . VAL C 1 155 ? 49.363  -4.627  104.936 1.00 93.52  ? 164  VAL C O   1 
ATOM   7511  C CB  . VAL C 1 155 ? 49.752  -3.476  108.029 1.00 97.19  ? 164  VAL C CB  1 
ATOM   7512  C CG1 . VAL C 1 155 ? 50.641  -2.683  107.046 1.00 96.17  ? 164  VAL C CG1 1 
ATOM   7513  C CG2 . VAL C 1 155 ? 48.919  -2.541  108.844 1.00 97.87  ? 164  VAL C CG2 1 
ATOM   7514  N N   . ASN C 1 156 ? 50.600  -5.857  106.363 1.00 96.59  ? 165  ASN C N   1 
ATOM   7515  C CA  . ASN C 1 156 ? 51.535  -6.270  105.345 1.00 96.27  ? 165  ASN C CA  1 
ATOM   7516  C C   . ASN C 1 156 ? 50.861  -7.070  104.253 1.00 94.39  ? 165  ASN C C   1 
ATOM   7517  O O   . ASN C 1 156 ? 51.216  -6.937  103.099 1.00 93.10  ? 165  ASN C O   1 
ATOM   7518  C CB  . ASN C 1 156 ? 52.706  -7.023  105.958 1.00 98.24  ? 165  ASN C CB  1 
ATOM   7519  C CG  . ASN C 1 156 ? 54.020  -6.410  105.583 1.00 100.14 ? 165  ASN C CG  1 
ATOM   7520  O OD1 . ASN C 1 156 ? 54.784  -5.986  106.453 1.00 102.69 ? 165  ASN C OD1 1 
ATOM   7521  N ND2 . ASN C 1 156 ? 54.282  -6.312  104.274 1.00 100.42 ? 165  ASN C ND2 1 
ATOM   7522  N N   . LYS C 1 157 ? 49.887  -7.895  104.622 1.00 94.35  ? 166  LYS C N   1 
ATOM   7523  C CA  . LYS C 1 157 ? 49.046  -8.540  103.643 1.00 92.86  ? 166  LYS C CA  1 
ATOM   7524  C C   . LYS C 1 157 ? 48.376  -7.468  102.802 1.00 90.86  ? 166  LYS C C   1 
ATOM   7525  O O   . LYS C 1 157 ? 48.551  -7.429  101.600 1.00 89.53  ? 166  LYS C O   1 
ATOM   7526  C CB  . LYS C 1 157 ? 48.011  -9.418  104.326 1.00 93.94  ? 166  LYS C CB  1 
ATOM   7527  C CG  . LYS C 1 157 ? 48.431  -10.857 104.463 1.00 96.11  ? 166  LYS C CG  1 
ATOM   7528  C CD  . LYS C 1 157 ? 47.726  -11.549 105.642 1.00 100.05 ? 166  LYS C CD  1 
ATOM   7529  C CE  . LYS C 1 157 ? 48.399  -12.898 105.963 1.00 102.52 ? 166  LYS C CE  1 
ATOM   7530  N NZ  . LYS C 1 157 ? 48.704  -13.112 107.415 1.00 104.81 ? 166  LYS C NZ  1 
ATOM   7531  N N   . ILE C 1 158 ? 47.647  -6.567  103.443 1.00 90.92  ? 167  ILE C N   1 
ATOM   7532  C CA  . ILE C 1 158 ? 46.898  -5.541  102.718 1.00 89.46  ? 167  ILE C CA  1 
ATOM   7533  C C   . ILE C 1 158 ? 47.738  -4.797  101.695 1.00 88.58  ? 167  ILE C C   1 
ATOM   7534  O O   . ILE C 1 158 ? 47.287  -4.585  100.572 1.00 87.04  ? 167  ILE C O   1 
ATOM   7535  C CB  . ILE C 1 158 ? 46.182  -4.558  103.662 1.00 90.26  ? 167  ILE C CB  1 
ATOM   7536  C CG1 . ILE C 1 158 ? 45.000  -5.283  104.301 1.00 90.84  ? 167  ILE C CG1 1 
ATOM   7537  C CG2 . ILE C 1 158 ? 45.747  -3.258  102.920 1.00 88.11  ? 167  ILE C CG2 1 
ATOM   7538  C CD1 . ILE C 1 158 ? 44.300  -4.514  105.388 1.00 93.15  ? 167  ILE C CD1 1 
ATOM   7539  N N   . LYS C 1 159 ? 48.956  -4.414  102.062 1.00 89.80  ? 168  LYS C N   1 
ATOM   7540  C CA  . LYS C 1 159 ? 49.827  -3.747  101.099 1.00 89.40  ? 168  LYS C CA  1 
ATOM   7541  C C   . LYS C 1 159 ? 49.908  -4.581  99.840  1.00 87.82  ? 168  LYS C C   1 
ATOM   7542  O O   . LYS C 1 159 ? 49.592  -4.108  98.768  1.00 86.37  ? 168  LYS C O   1 
ATOM   7543  C CB  . LYS C 1 159 ? 51.223  -3.533  101.663 1.00 91.16  ? 168  LYS C CB  1 
ATOM   7544  C CG  . LYS C 1 159 ? 52.216  -3.098  100.617 1.00 92.40  ? 168  LYS C CG  1 
ATOM   7545  C CD  . LYS C 1 159 ? 53.650  -3.266  101.084 1.00 97.18  ? 168  LYS C CD  1 
ATOM   7546  C CE  . LYS C 1 159 ? 54.593  -3.216  99.892  1.00 97.38  ? 168  LYS C CE  1 
ATOM   7547  N NZ  . LYS C 1 159 ? 55.942  -2.712  100.237 1.00 99.69  ? 168  LYS C NZ  1 
ATOM   7548  N N   . SER C 1 160 ? 50.295  -5.839  99.991  1.00 88.51  ? 169  SER C N   1 
ATOM   7549  C CA  . SER C 1 160 ? 50.472  -6.728  98.862  1.00 87.87  ? 169  SER C CA  1 
ATOM   7550  C C   . SER C 1 160 ? 49.211  -6.856  98.051  1.00 86.34  ? 169  SER C C   1 
ATOM   7551  O O   . SER C 1 160 ? 49.256  -6.813  96.827  1.00 85.37  ? 169  SER C O   1 
ATOM   7552  C CB  . SER C 1 160 ? 50.924  -8.105  99.320  1.00 89.10  ? 169  SER C CB  1 
ATOM   7553  O OG  . SER C 1 160 ? 52.195  -8.037  99.955  1.00 91.79  ? 169  SER C OG  1 
ATOM   7554  N N   . ALA C 1 161 ? 48.082  -6.998  98.730  1.00 86.45  ? 170  ALA C N   1 
ATOM   7555  C CA  . ALA C 1 161 ? 46.791  -7.146  98.062  1.00 85.04  ? 170  ALA C CA  1 
ATOM   7556  C C   . ALA C 1 161 ? 46.411  -5.939  97.232  1.00 83.43  ? 170  ALA C C   1 
ATOM   7557  O O   . ALA C 1 161 ? 45.848  -6.086  96.157  1.00 81.99  ? 170  ALA C O   1 
ATOM   7558  C CB  . ALA C 1 161 ? 45.712  -7.429  99.077  1.00 86.17  ? 170  ALA C CB  1 
ATOM   7559  N N   . LEU C 1 162 ? 46.709  -4.753  97.751  1.00 83.75  ? 171  LEU C N   1 
ATOM   7560  C CA  . LEU C 1 162 ? 46.432  -3.518  97.046  1.00 82.64  ? 171  LEU C CA  1 
ATOM   7561  C C   . LEU C 1 162 ? 47.297  -3.403  95.823  1.00 81.71  ? 171  LEU C C   1 
ATOM   7562  O O   . LEU C 1 162 ? 46.817  -3.018  94.777  1.00 80.70  ? 171  LEU C O   1 
ATOM   7563  C CB  . LEU C 1 162 ? 46.659  -2.295  97.926  1.00 83.68  ? 171  LEU C CB  1 
ATOM   7564  C CG  . LEU C 1 162 ? 46.359  -0.963  97.238  1.00 82.59  ? 171  LEU C CG  1 
ATOM   7565  C CD1 . LEU C 1 162 ? 44.895  -0.809  97.134  1.00 82.48  ? 171  LEU C CD1 1 
ATOM   7566  C CD2 . LEU C 1 162 ? 46.890  0.217   97.978  1.00 84.08  ? 171  LEU C CD2 1 
ATOM   7567  N N   . LEU C 1 163 ? 48.575  -3.728  95.948  1.00 82.57  ? 172  LEU C N   1 
ATOM   7568  C CA  . LEU C 1 163 ? 49.473  -3.693  94.801  1.00 81.88  ? 172  LEU C CA  1 
ATOM   7569  C C   . LEU C 1 163 ? 48.891  -4.523  93.682  1.00 80.44  ? 172  LEU C C   1 
ATOM   7570  O O   . LEU C 1 163 ? 48.817  -4.069  92.540  1.00 79.21  ? 172  LEU C O   1 
ATOM   7571  C CB  . LEU C 1 163 ? 50.849  -4.230  95.166  1.00 83.20  ? 172  LEU C CB  1 
ATOM   7572  C CG  . LEU C 1 163 ? 51.630  -3.466  96.226  1.00 85.05  ? 172  LEU C CG  1 
ATOM   7573  C CD1 . LEU C 1 163 ? 52.685  -4.376  96.806  1.00 88.04  ? 172  LEU C CD1 1 
ATOM   7574  C CD2 . LEU C 1 163 ? 52.248  -2.204  95.669  1.00 84.85  ? 172  LEU C CD2 1 
ATOM   7575  N N   . SER C 1 164 ? 48.456  -5.728  94.041  1.00 80.59  ? 173  SER C N   1 
ATOM   7576  C CA  . SER C 1 164 ? 47.804  -6.658  93.133  1.00 79.39  ? 173  SER C CA  1 
ATOM   7577  C C   . SER C 1 164 ? 46.587  -6.002  92.474  1.00 77.73  ? 173  SER C C   1 
ATOM   7578  O O   . SER C 1 164 ? 46.339  -6.166  91.282  1.00 76.50  ? 173  SER C O   1 
ATOM   7579  C CB  . SER C 1 164 ? 47.380  -7.912  93.901  0.82 80.53  ? 173  SER C CB  1 
ATOM   7580  O OG  . SER C 1 164 ? 47.779  -9.098  93.236  0.82 80.59  ? 173  SER C OG  1 
ATOM   7581  N N   . THR C 1 165 ? 45.834  -5.245  93.254  1.00 77.84  ? 174  THR C N   1 
ATOM   7582  C CA  . THR C 1 165 ? 44.695  -4.526  92.712  1.00 76.62  ? 174  THR C CA  1 
ATOM   7583  C C   . THR C 1 165 ? 45.168  -3.467  91.748  1.00 75.46  ? 174  THR C C   1 
ATOM   7584  O O   . THR C 1 165 ? 44.616  -3.329  90.681  1.00 74.27  ? 174  THR C O   1 
ATOM   7585  C CB  . THR C 1 165 ? 43.829  -3.869  93.811  1.00 77.54  ? 174  THR C CB  1 
ATOM   7586  O OG1 . THR C 1 165 ? 43.248  -4.879  94.661  1.00 78.72  ? 174  THR C OG1 1 
ATOM   7587  C CG2 . THR C 1 165 ? 42.729  -3.025  93.183  1.00 75.76  ? 174  THR C CG2 1 
ATOM   7588  N N   . ASN C 1 166 ? 46.197  -2.725  92.112  1.00 76.14  ? 175  ASN C N   1 
ATOM   7589  C CA  . ASN C 1 166 ? 46.692  -1.690  91.238  1.00 75.66  ? 175  ASN C CA  1 
ATOM   7590  C C   . ASN C 1 166 ? 47.038  -2.202  89.855  1.00 74.49  ? 175  ASN C C   1 
ATOM   7591  O O   . ASN C 1 166 ? 46.577  -1.670  88.851  1.00 73.03  ? 175  ASN C O   1 
ATOM   7592  C CB  . ASN C 1 166 ? 47.880  -1.014  91.882  1.00 77.19  ? 175  ASN C CB  1 
ATOM   7593  C CG  . ASN C 1 166 ? 47.463  -0.086  92.989  1.00 79.07  ? 175  ASN C CG  1 
ATOM   7594  O OD1 . ASN C 1 166 ? 46.275  0.019   93.313  1.00 79.43  ? 175  ASN C OD1 1 
ATOM   7595  N ND2 . ASN C 1 166 ? 48.431  0.609   93.573  1.00 81.40  ? 175  ASN C ND2 1 
ATOM   7596  N N   . LYS C 1 167 ? 47.827  -3.265  89.820  1.00 75.11  ? 176  LYS C N   1 
ATOM   7597  C CA  . LYS C 1 167 ? 48.172  -3.928  88.581  1.00 74.42  ? 176  LYS C CA  1 
ATOM   7598  C C   . LYS C 1 167 ? 46.957  -4.464  87.860  1.00 72.95  ? 176  LYS C C   1 
ATOM   7599  O O   . LYS C 1 167 ? 46.986  -4.643  86.655  1.00 72.15  ? 176  LYS C O   1 
ATOM   7600  C CB  . LYS C 1 167 ? 49.094  -5.090  88.845  1.00 75.77  ? 176  LYS C CB  1 
ATOM   7601  C CG  . LYS C 1 167 ? 50.446  -4.682  89.282  1.00 78.55  ? 176  LYS C CG  1 
ATOM   7602  C CD  . LYS C 1 167 ? 51.186  -5.884  89.791  1.00 82.30  ? 176  LYS C CD  1 
ATOM   7603  C CE  . LYS C 1 167 ? 52.678  -5.686  89.693  1.00 84.80  ? 176  LYS C CE  1 
ATOM   7604  N NZ  . LYS C 1 167 ? 53.340  -6.773  90.452  1.00 87.81  ? 176  LYS C NZ  1 
ATOM   7605  N N   . ALA C 1 168 ? 45.894  -4.760  88.587  1.00 72.78  ? 177  ALA C N   1 
ATOM   7606  C CA  . ALA C 1 168 ? 44.666  -5.175  87.933  1.00 71.34  ? 177  ALA C CA  1 
ATOM   7607  C C   . ALA C 1 168 ? 44.055  -3.999  87.178  1.00 69.60  ? 177  ALA C C   1 
ATOM   7608  O O   . ALA C 1 168 ? 43.515  -4.167  86.087  1.00 68.53  ? 177  ALA C O   1 
ATOM   7609  C CB  . ALA C 1 168 ? 43.680  -5.738  88.949  1.00 72.30  ? 177  ALA C CB  1 
ATOM   7610  N N   . VAL C 1 169 ? 44.155  -2.806  87.757  1.00 69.27  ? 178  VAL C N   1 
ATOM   7611  C CA  . VAL C 1 169 ? 43.514  -1.648  87.165  1.00 67.64  ? 178  VAL C CA  1 
ATOM   7612  C C   . VAL C 1 169 ? 44.336  -1.212  86.010  1.00 66.97  ? 178  VAL C C   1 
ATOM   7613  O O   . VAL C 1 169 ? 43.807  -0.696  85.039  1.00 66.04  ? 178  VAL C O   1 
ATOM   7614  C CB  . VAL C 1 169 ? 43.298  -0.491  88.160  1.00 68.32  ? 178  VAL C CB  1 
ATOM   7615  C CG1 . VAL C 1 169 ? 43.152  0.843   87.452  1.00 66.74  ? 178  VAL C CG1 1 
ATOM   7616  C CG2 . VAL C 1 169 ? 42.049  -0.750  88.976  1.00 68.48  ? 178  VAL C CG2 1 
ATOM   7617  N N   . VAL C 1 170 ? 45.635  -1.436  86.099  1.00 67.85  ? 179  VAL C N   1 
ATOM   7618  C CA  . VAL C 1 170 ? 46.501  -1.148  84.971  1.00 67.50  ? 179  VAL C CA  1 
ATOM   7619  C C   . VAL C 1 170 ? 46.103  -2.016  83.786  1.00 66.04  ? 179  VAL C C   1 
ATOM   7620  O O   . VAL C 1 170 ? 45.848  -1.498  82.714  1.00 64.70  ? 179  VAL C O   1 
ATOM   7621  C CB  . VAL C 1 170 ? 47.976  -1.334  85.339  1.00 69.15  ? 179  VAL C CB  1 
ATOM   7622  C CG1 . VAL C 1 170 ? 48.820  -1.627  84.113  1.00 69.44  ? 179  VAL C CG1 1 
ATOM   7623  C CG2 . VAL C 1 170 ? 48.493  -0.106  86.060  1.00 70.56  ? 179  VAL C CG2 1 
ATOM   7624  N N   . SER C 1 171 ? 46.017  -3.325  83.996  1.00 66.38  ? 180  SER C N   1 
ATOM   7625  C CA  . SER C 1 171 ? 45.599  -4.228  82.947  0.75 65.76  ? 180  SER C CA  1 
ATOM   7626  C C   . SER C 1 171 ? 44.350  -3.718  82.275  1.00 64.72  ? 180  SER C C   1 
ATOM   7627  O O   . SER C 1 171 ? 44.341  -3.547  81.070  1.00 64.17  ? 180  SER C O   1 
ATOM   7628  C CB  . SER C 1 171 ? 45.362  -5.625  83.486  0.75 66.54  ? 180  SER C CB  1 
ATOM   7629  O OG  . SER C 1 171 ? 46.420  -6.461  83.094  0.75 67.24  ? 180  SER C OG  1 
ATOM   7630  N N   . LEU C 1 172 ? 43.301  -3.450  83.052  1.00 65.08  ? 181  LEU C N   1 
ATOM   7631  C CA  . LEU C 1 172 ? 42.025  -2.988  82.483  1.00 63.96  ? 181  LEU C CA  1 
ATOM   7632  C C   . LEU C 1 172 ? 42.166  -1.672  81.751  1.00 63.32  ? 181  LEU C C   1 
ATOM   7633  O O   . LEU C 1 172 ? 41.564  -1.485  80.704  1.00 62.35  ? 181  LEU C O   1 
ATOM   7634  C CB  . LEU C 1 172 ? 40.916  -2.873  83.541  1.00 64.44  ? 181  LEU C CB  1 
ATOM   7635  C CG  . LEU C 1 172 ? 39.472  -2.897  83.004  1.00 62.84  ? 181  LEU C CG  1 
ATOM   7636  C CD1 . LEU C 1 172 ? 39.155  -4.269  82.447  1.00 63.50  ? 181  LEU C CD1 1 
ATOM   7637  C CD2 . LEU C 1 172 ? 38.426  -2.530  84.047  1.00 62.34  ? 181  LEU C CD2 1 
ATOM   7638  N N   . SER C 1 173 ? 42.960  -0.766  82.296  1.00 64.24  ? 182  SER C N   1 
ATOM   7639  C CA  . SER C 1 173 ? 43.208  0.487   81.630  1.00 64.16  ? 182  SER C CA  1 
ATOM   7640  C C   . SER C 1 173 ? 43.778  0.274   80.245  1.00 63.68  ? 182  SER C C   1 
ATOM   7641  O O   . SER C 1 173 ? 43.325  0.873   79.293  1.00 62.85  ? 182  SER C O   1 
ATOM   7642  C CB  . SER C 1 173 ? 44.148  1.336   82.450  1.00 65.29  ? 182  SER C CB  1 
ATOM   7643  O OG  . SER C 1 173 ? 43.490  1.759   83.615  1.00 66.29  ? 182  SER C OG  1 
ATOM   7644  N N   . ASN C 1 174 ? 44.761  -0.601  80.135  1.00 64.91  ? 183  ASN C N   1 
ATOM   7645  C CA  . ASN C 1 174 ? 45.395  -0.886  78.857  1.00 65.02  ? 183  ASN C CA  1 
ATOM   7646  C C   . ASN C 1 174 ? 44.480  -1.605  77.921  1.00 63.71  ? 183  ASN C C   1 
ATOM   7647  O O   . ASN C 1 174 ? 44.527  -1.380  76.721  1.00 63.32  ? 183  ASN C O   1 
ATOM   7648  C CB  . ASN C 1 174 ? 46.663  -1.704  79.060  1.00 66.81  ? 183  ASN C CB  1 
ATOM   7649  C CG  . ASN C 1 174 ? 47.736  -0.918  79.800  1.00 70.08  ? 183  ASN C CG  1 
ATOM   7650  O OD1 . ASN C 1 174 ? 47.839  0.301   79.605  1.00 72.39  ? 183  ASN C OD1 1 
ATOM   7651  N ND2 . ASN C 1 174 ? 48.528  -1.593  80.658  1.00 72.03  ? 183  ASN C ND2 1 
ATOM   7652  N N   . GLY C 1 175 ? 43.647  -2.473  78.474  1.00 63.46  ? 184  GLY C N   1 
ATOM   7653  C CA  . GLY C 1 175 ? 42.587  -3.113  77.706  1.00 61.96  ? 184  GLY C CA  1 
ATOM   7654  C C   . GLY C 1 175 ? 41.669  -2.111  77.050  1.00 60.24  ? 184  GLY C C   1 
ATOM   7655  O O   . GLY C 1 175 ? 41.448  -2.176  75.848  1.00 59.46  ? 184  GLY C O   1 
ATOM   7656  N N   . VAL C 1 176 ? 41.149  -1.182  77.847  1.00 59.81  ? 185  VAL C N   1 
ATOM   7657  C CA  . VAL C 1 176 ? 40.319  -0.098  77.352  1.00 58.28  ? 185  VAL C CA  1 
ATOM   7658  C C   . VAL C 1 176 ? 41.092  0.801   76.394  1.00 57.76  ? 185  VAL C C   1 
ATOM   7659  O O   . VAL C 1 176 ? 40.601  1.143   75.320  1.00 56.73  ? 185  VAL C O   1 
ATOM   7660  C CB  . VAL C 1 176 ? 39.763  0.724   78.504  1.00 58.74  ? 185  VAL C CB  1 
ATOM   7661  C CG1 . VAL C 1 176 ? 39.260  2.040   78.006  1.00 57.98  ? 185  VAL C CG1 1 
ATOM   7662  C CG2 . VAL C 1 176 ? 38.650  -0.040  79.207  1.00 58.62  ? 185  VAL C CG2 1 
ATOM   7663  N N   . SER C 1 177 ? 42.310  1.159   76.773  1.00 58.56  ? 186  SER C N   1 
ATOM   7664  C CA  . SER C 1 177 ? 43.155  1.965   75.930  0.75 58.37  ? 186  SER C CA  1 
ATOM   7665  C C   . SER C 1 177 ? 43.177  1.399   74.523  1.00 57.22  ? 186  SER C C   1 
ATOM   7666  O O   . SER C 1 177 ? 43.164  2.150   73.547  1.00 56.77  ? 186  SER C O   1 
ATOM   7667  C CB  . SER C 1 177 ? 44.560  2.007   76.496  0.75 59.92  ? 186  SER C CB  1 
ATOM   7668  O OG  . SER C 1 177 ? 45.410  2.704   75.613  0.75 60.84  ? 186  SER C OG  1 
ATOM   7669  N N   . VAL C 1 178 ? 43.190  0.073   74.422  1.00 56.91  ? 187  VAL C N   1 
ATOM   7670  C CA  . VAL C 1 178 ? 43.188  -0.597  73.125  1.00 55.83  ? 187  VAL C CA  1 
ATOM   7671  C C   . VAL C 1 178 ? 41.813  -0.626  72.465  1.00 54.76  ? 187  VAL C C   1 
ATOM   7672  O O   . VAL C 1 178 ? 41.696  -0.254  71.305  1.00 54.13  ? 187  VAL C O   1 
ATOM   7673  C CB  . VAL C 1 178 ? 43.809  -1.974  73.210  1.00 56.31  ? 187  VAL C CB  1 
ATOM   7674  C CG1 . VAL C 1 178 ? 43.355  -2.854  72.073  1.00 55.08  ? 187  VAL C CG1 1 
ATOM   7675  C CG2 . VAL C 1 178 ? 45.290  -1.814  73.189  1.00 57.09  ? 187  VAL C CG2 1 
ATOM   7676  N N   . LEU C 1 179 ? 40.783  -1.060  73.193  1.00 54.87  ? 188  LEU C N   1 
ATOM   7677  C CA  . LEU C 1 179 ? 39.410  -1.097  72.666  1.00 53.75  ? 188  LEU C CA  1 
ATOM   7678  C C   . LEU C 1 179 ? 38.998  0.253   72.164  1.00 52.88  ? 188  LEU C C   1 
ATOM   7679  O O   . LEU C 1 179 ? 38.322  0.350   71.161  1.00 51.89  ? 188  LEU C O   1 
ATOM   7680  C CB  . LEU C 1 179 ? 38.404  -1.545  73.722  1.00 54.26  ? 188  LEU C CB  1 
ATOM   7681  C CG  . LEU C 1 179 ? 36.983  -1.793  73.212  1.00 53.25  ? 188  LEU C CG  1 
ATOM   7682  C CD1 . LEU C 1 179 ? 36.890  -3.150  72.551  1.00 53.54  ? 188  LEU C CD1 1 
ATOM   7683  C CD2 . LEU C 1 179 ? 35.975  -1.699  74.335  1.00 53.54  ? 188  LEU C CD2 1 
ATOM   7684  N N   . THR C 1 180 ? 39.396  1.292   72.880  1.00 53.55  ? 189  THR C N   1 
ATOM   7685  C CA  . THR C 1 180 ? 39.276  2.635   72.375  1.00 53.38  ? 189  THR C CA  1 
ATOM   7686  C C   . THR C 1 180 ? 40.075  2.765   71.083  1.00 53.25  ? 189  THR C C   1 
ATOM   7687  O O   . THR C 1 180 ? 39.498  3.024   70.034  1.00 52.20  ? 189  THR C O   1 
ATOM   7688  C CB  . THR C 1 180 ? 39.766  3.639   73.392  1.00 54.32  ? 189  THR C CB  1 
ATOM   7689  O OG1 . THR C 1 180 ? 38.827  3.690   74.456  1.00 54.81  ? 189  THR C OG1 1 
ATOM   7690  C CG2 . THR C 1 180 ? 39.857  5.015   72.796  1.00 54.42  ? 189  THR C CG2 1 
ATOM   7691  N N   . SER C 1 181 ? 41.392  2.562   71.149  1.00 54.39  ? 190  SER C N   1 
ATOM   7692  C CA  . SER C 1 181 ? 42.230  2.631   69.965  0.25 54.25  ? 190  SER C CA  1 
ATOM   7693  C C   . SER C 1 181 ? 41.524  1.998   68.774  1.00 53.29  ? 190  SER C C   1 
ATOM   7694  O O   . SER C 1 181 ? 41.633  2.505   67.682  1.00 53.00  ? 190  SER C O   1 
ATOM   7695  C CB  . SER C 1 181 ? 43.580  1.963   70.208  0.25 55.32  ? 190  SER C CB  1 
ATOM   7696  O OG  . SER C 1 181 ? 44.393  2.040   69.056  0.25 55.04  ? 190  SER C OG  1 
ATOM   7697  N N   . LYS C 1 182 ? 40.758  0.928   68.995  1.00 53.25  ? 191  LYS C N   1 
ATOM   7698  C CA  . LYS C 1 182 ? 40.101  0.165   67.916  1.00 52.49  ? 191  LYS C CA  1 
ATOM   7699  C C   . LYS C 1 182 ? 38.735  0.641   67.444  1.00 51.28  ? 191  LYS C C   1 
ATOM   7700  O O   . LYS C 1 182 ? 38.370  0.472   66.279  1.00 50.64  ? 191  LYS C O   1 
ATOM   7701  C CB  . LYS C 1 182 ? 39.947  -1.284  68.325  1.00 53.05  ? 191  LYS C CB  1 
ATOM   7702  C CG  . LYS C 1 182 ? 41.173  -2.109  68.085  1.00 55.47  ? 191  LYS C CG  1 
ATOM   7703  C CD  . LYS C 1 182 ? 41.350  -2.433  66.623  1.00 57.72  ? 191  LYS C CD  1 
ATOM   7704  C CE  . LYS C 1 182 ? 42.603  -1.792  66.064  1.00 60.28  ? 191  LYS C CE  1 
ATOM   7705  N NZ  . LYS C 1 182 ? 42.986  -2.388  64.744  1.00 62.35  ? 191  LYS C NZ  1 
ATOM   7706  N N   . VAL C 1 183 ? 37.950  1.177   68.362  1.00 51.14  ? 192  VAL C N   1 
ATOM   7707  C CA  . VAL C 1 183 ? 36.660  1.718   68.011  1.00 49.85  ? 192  VAL C CA  1 
ATOM   7708  C C   . VAL C 1 183 ? 36.866  2.923   67.123  1.00 49.32  ? 192  VAL C C   1 
ATOM   7709  O O   . VAL C 1 183 ? 36.089  3.167   66.219  1.00 48.51  ? 192  VAL C O   1 
ATOM   7710  C CB  . VAL C 1 183 ? 35.855  2.066   69.265  1.00 50.28  ? 192  VAL C CB  1 
ATOM   7711  C CG1 . VAL C 1 183 ? 34.882  3.191   69.013  1.00 49.18  ? 192  VAL C CG1 1 
ATOM   7712  C CG2 . VAL C 1 183 ? 35.120  0.841   69.728  1.00 50.71  ? 192  VAL C CG2 1 
ATOM   7713  N N   . LEU C 1 184 ? 37.936  3.667   67.356  1.00 50.18  ? 193  LEU C N   1 
ATOM   7714  C CA  . LEU C 1 184 ? 38.253  4.770   66.479  1.00 50.11  ? 193  LEU C CA  1 
ATOM   7715  C C   . LEU C 1 184 ? 38.393  4.246   65.072  1.00 49.77  ? 193  LEU C C   1 
ATOM   7716  O O   . LEU C 1 184 ? 37.741  4.738   64.171  1.00 49.22  ? 193  LEU C O   1 
ATOM   7717  C CB  . LEU C 1 184 ? 39.538  5.460   66.884  1.00 51.16  ? 193  LEU C CB  1 
ATOM   7718  C CG  . LEU C 1 184 ? 39.898  6.621   65.952  1.00 51.25  ? 193  LEU C CG  1 
ATOM   7719  C CD1 . LEU C 1 184 ? 39.187  7.881   66.399  1.00 50.86  ? 193  LEU C CD1 1 
ATOM   7720  C CD2 . LEU C 1 184 ? 41.421  6.848   65.886  1.00 53.28  ? 193  LEU C CD2 1 
ATOM   7721  N N   . ASP C 1 185 ? 39.237  3.238   64.890  1.00 50.83  ? 194  ASP C N   1 
ATOM   7722  C CA  . ASP C 1 185 ? 39.429  2.611   63.583  1.00 50.88  ? 194  ASP C CA  1 
ATOM   7723  C C   . ASP C 1 185 ? 38.110  2.157   62.940  1.00 49.77  ? 194  ASP C C   1 
ATOM   7724  O O   . ASP C 1 185 ? 37.894  2.376   61.748  1.00 49.09  ? 194  ASP C O   1 
ATOM   7725  C CB  . ASP C 1 185 ? 40.413  1.445   63.698  1.00 52.20  ? 194  ASP C CB  1 
ATOM   7726  C CG  . ASP C 1 185 ? 41.758  1.886   64.216  1.00 54.70  ? 194  ASP C CG  1 
ATOM   7727  O OD1 . ASP C 1 185 ? 41.953  3.116   64.332  1.00 55.90  ? 194  ASP C OD1 1 
ATOM   7728  O OD2 . ASP C 1 185 ? 42.618  1.024   64.499  1.00 56.84  ? 194  ASP C OD2 1 
ATOM   7729  N N   . LEU C 1 186 ? 37.219  1.541   63.712  1.00 49.73  ? 195  LEU C N   1 
ATOM   7730  C CA  . LEU C 1 186 ? 35.943  1.133   63.148  1.00 48.85  ? 195  LEU C CA  1 
ATOM   7731  C C   . LEU C 1 186 ? 35.228  2.330   62.580  1.00 48.01  ? 195  LEU C C   1 
ATOM   7732  O O   . LEU C 1 186 ? 34.854  2.321   61.418  1.00 47.23  ? 195  LEU C O   1 
ATOM   7733  C CB  . LEU C 1 186 ? 35.052  0.482   64.185  1.00 49.39  ? 195  LEU C CB  1 
ATOM   7734  C CG  . LEU C 1 186 ? 34.376  -0.809  63.733  1.00 49.07  ? 195  LEU C CG  1 
ATOM   7735  C CD1 . LEU C 1 186 ? 32.967  -0.932  64.292  1.00 48.56  ? 195  LEU C CD1 1 
ATOM   7736  C CD2 . LEU C 1 186 ? 34.355  -0.886  62.244  1.00 48.12  ? 195  LEU C CD2 1 
ATOM   7737  N N   . LYS C 1 187 ? 35.044  3.364   63.396  1.00 48.44  ? 196  LYS C N   1 
ATOM   7738  C CA  . LYS C 1 187 ? 34.512  4.630   62.889  1.00 48.11  ? 196  LYS C CA  1 
ATOM   7739  C C   . LYS C 1 187 ? 35.260  5.055   61.634  1.00 47.91  ? 196  LYS C C   1 
ATOM   7740  O O   . LYS C 1 187 ? 34.655  5.295   60.609  1.00 47.32  ? 196  LYS C O   1 
ATOM   7741  C CB  . LYS C 1 187 ? 34.569  5.745   63.946  1.00 48.75  ? 196  LYS C CB  1 
ATOM   7742  C CG  . LYS C 1 187 ? 34.390  7.182   63.408  1.00 47.81  ? 196  LYS C CG  1 
ATOM   7743  C CD  . LYS C 1 187 ? 35.726  7.859   63.109  1.00 48.19  ? 196  LYS C CD  1 
ATOM   7744  C CE  . LYS C 1 187 ? 35.514  9.288   62.661  1.00 49.08  ? 196  LYS C CE  1 
ATOM   7745  N NZ  . LYS C 1 187 ? 36.757  9.906   62.114  1.00 50.39  ? 196  LYS C NZ  1 
ATOM   7746  N N   . ASN C 1 188 ? 36.576  5.133   61.711  1.00 48.98  ? 197  ASN C N   1 
ATOM   7747  C CA  . ASN C 1 188 ? 37.335  5.622   60.586  1.00 49.42  ? 197  ASN C CA  1 
ATOM   7748  C C   . ASN C 1 188 ? 37.205  4.805   59.303  1.00 49.04  ? 197  ASN C C   1 
ATOM   7749  O O   . ASN C 1 188 ? 37.249  5.386   58.210  1.00 48.99  ? 197  ASN C O   1 
ATOM   7750  C CB  . ASN C 1 188 ? 38.787  5.855   60.967  1.00 50.73  ? 197  ASN C CB  1 
ATOM   7751  C CG  . ASN C 1 188 ? 39.015  7.251   61.478  1.00 52.08  ? 197  ASN C CG  1 
ATOM   7752  O OD1 . ASN C 1 188 ? 39.432  7.446   62.630  1.00 54.08  ? 197  ASN C OD1 1 
ATOM   7753  N ND2 . ASN C 1 188 ? 38.727  8.242   60.630  1.00 52.11  ? 197  ASN C ND2 1 
ATOM   7754  N N   . TYR C 1 189 ? 37.018  3.487   59.421  1.00 49.07  ? 198  TYR C N   1 
ATOM   7755  C CA  . TYR C 1 189 ? 36.717  2.692   58.248  1.00 48.44  ? 198  TYR C CA  1 
ATOM   7756  C C   . TYR C 1 189 ? 35.467  3.263   57.669  1.00 46.93  ? 198  TYR C C   1 
ATOM   7757  O O   . TYR C 1 189 ? 35.488  3.822   56.607  1.00 46.41  ? 198  TYR C O   1 
ATOM   7758  C CB  . TYR C 1 189 ? 36.488  1.232   58.570  1.00 49.41  ? 198  TYR C CB  1 
ATOM   7759  C CG  . TYR C 1 189 ? 36.553  0.374   57.335  1.00 51.03  ? 198  TYR C CG  1 
ATOM   7760  C CD1 . TYR C 1 189 ? 37.779  0.106   56.729  1.00 54.67  ? 198  TYR C CD1 1 
ATOM   7761  C CD2 . TYR C 1 189 ? 35.406  -0.164  56.762  1.00 51.33  ? 198  TYR C CD2 1 
ATOM   7762  C CE1 . TYR C 1 189 ? 37.872  -0.683  55.562  1.00 56.11  ? 198  TYR C CE1 1 
ATOM   7763  C CE2 . TYR C 1 189 ? 35.477  -0.963  55.597  1.00 53.34  ? 198  TYR C CE2 1 
ATOM   7764  C CZ  . TYR C 1 189 ? 36.716  -1.213  54.995  1.00 55.42  ? 198  TYR C CZ  1 
ATOM   7765  O OH  . TYR C 1 189 ? 36.823  -1.983  53.843  1.00 55.37  ? 198  TYR C OH  1 
ATOM   7766  N N   . ILE C 1 190 ? 34.377  3.175   58.401  1.00 46.64  ? 199  ILE C N   1 
ATOM   7767  C CA  . ILE C 1 190 ? 33.138  3.794   57.963  1.00 45.74  ? 199  ILE C CA  1 
ATOM   7768  C C   . ILE C 1 190 ? 33.309  5.187   57.358  1.00 45.71  ? 199  ILE C C   1 
ATOM   7769  O O   . ILE C 1 190 ? 32.978  5.369   56.200  1.00 45.11  ? 199  ILE C O   1 
ATOM   7770  C CB  . ILE C 1 190 ? 32.129  3.845   59.093  1.00 45.72  ? 199  ILE C CB  1 
ATOM   7771  C CG1 . ILE C 1 190 ? 31.468  2.483   59.228  1.00 45.40  ? 199  ILE C CG1 1 
ATOM   7772  C CG2 . ILE C 1 190 ? 31.101  4.929   58.843  1.00 44.72  ? 199  ILE C CG2 1 
ATOM   7773  C CD1 . ILE C 1 190 ? 30.900  2.275   60.567  1.00 45.86  ? 199  ILE C CD1 1 
ATOM   7774  N N   . ASP C 1 191 ? 33.824  6.156   58.112  1.00 46.84  ? 200  ASP C N   1 
ATOM   7775  C CA  . ASP C 1 191 ? 33.859  7.528   57.612  1.00 47.42  ? 200  ASP C CA  1 
ATOM   7776  C C   . ASP C 1 191 ? 34.770  7.687   56.421  1.00 47.21  ? 200  ASP C C   1 
ATOM   7777  O O   . ASP C 1 191 ? 34.425  8.398   55.468  1.00 46.56  ? 200  ASP C O   1 
ATOM   7778  C CB  . ASP C 1 191 ? 34.247  8.560   58.679  1.00 48.81  ? 200  ASP C CB  1 
ATOM   7779  C CG  . ASP C 1 191 ? 34.302  10.029  58.118  1.00 50.68  ? 200  ASP C CG  1 
ATOM   7780  O OD1 . ASP C 1 191 ? 33.454  10.449  57.274  1.00 51.66  ? 200  ASP C OD1 1 
ATOM   7781  O OD2 . ASP C 1 191 ? 35.214  10.780  58.531  1.00 52.54  ? 200  ASP C OD2 1 
ATOM   7782  N N   . LYS C 1 192 ? 35.924  7.038   56.458  1.00 47.84  ? 201  LYS C N   1 
ATOM   7783  C CA  . LYS C 1 192 ? 36.920  7.347   55.448  1.00 48.49  ? 201  LYS C CA  1 
ATOM   7784  C C   . LYS C 1 192 ? 37.177  6.282   54.374  1.00 48.35  ? 201  LYS C C   1 
ATOM   7785  O O   . LYS C 1 192 ? 37.960  6.483   53.458  1.00 48.50  ? 201  LYS C O   1 
ATOM   7786  C CB  . LYS C 1 192 ? 38.180  7.865   56.125  1.00 49.76  ? 201  LYS C CB  1 
ATOM   7787  C CG  . LYS C 1 192 ? 37.868  9.122   56.923  1.00 51.22  ? 201  LYS C CG  1 
ATOM   7788  C CD  . LYS C 1 192 ? 39.090  9.862   57.444  1.00 55.66  ? 201  LYS C CD  1 
ATOM   7789  C CE  . LYS C 1 192 ? 38.642  10.984  58.408  1.00 58.37  ? 201  LYS C CE  1 
ATOM   7790  N NZ  . LYS C 1 192 ? 39.709  11.400  59.392  1.00 61.90  ? 201  LYS C NZ  1 
ATOM   7791  N N   . GLN C 1 193 ? 36.450  5.177   54.454  1.00 48.45  ? 202  GLN C N   1 
ATOM   7792  C CA  . GLN C 1 193 ? 36.634  4.045   53.538  1.00 48.74  ? 202  GLN C CA  1 
ATOM   7793  C C   . GLN C 1 193 ? 35.345  3.664   52.821  1.00 47.21  ? 202  GLN C C   1 
ATOM   7794  O O   . GLN C 1 193 ? 35.265  3.764   51.594  1.00 46.85  ? 202  GLN C O   1 
ATOM   7795  C CB  . GLN C 1 193 ? 37.137  2.824   54.312  1.00 50.21  ? 202  GLN C CB  1 
ATOM   7796  C CG  . GLN C 1 193 ? 38.603  2.886   54.728  1.00 54.45  ? 202  GLN C CG  1 
ATOM   7797  C CD  . GLN C 1 193 ? 39.532  2.550   53.568  1.00 59.27  ? 202  GLN C CD  1 
ATOM   7798  O OE1 . GLN C 1 193 ? 39.297  1.589   52.818  1.00 61.34  ? 202  GLN C OE1 1 
ATOM   7799  N NE2 . GLN C 1 193 ? 40.587  3.346   53.403  1.00 61.07  ? 202  GLN C NE2 1 
ATOM   7800  N N   . LEU C 1 194 ? 34.357  3.220   53.601  1.00 46.29  ? 203  LEU C N   1 
ATOM   7801  C CA  . LEU C 1 194 ? 33.063  2.780   53.112  1.00 44.93  ? 203  LEU C CA  1 
ATOM   7802  C C   . LEU C 1 194 ? 32.200  3.951   52.627  1.00 44.16  ? 203  LEU C C   1 
ATOM   7803  O O   . LEU C 1 194 ? 31.798  4.029   51.448  1.00 43.34  ? 203  LEU C O   1 
ATOM   7804  C CB  . LEU C 1 194 ? 32.347  2.066   54.244  1.00 44.95  ? 203  LEU C CB  1 
ATOM   7805  C CG  . LEU C 1 194 ? 30.920  1.682   53.933  1.00 44.06  ? 203  LEU C CG  1 
ATOM   7806  C CD1 . LEU C 1 194 ? 30.873  0.295   53.342  1.00 44.87  ? 203  LEU C CD1 1 
ATOM   7807  C CD2 . LEU C 1 194 ? 30.111  1.742   55.192  1.00 44.22  ? 203  LEU C CD2 1 
ATOM   7808  N N   . LEU C 1 195 ? 31.938  4.873   53.554  1.00 44.34  ? 204  LEU C N   1 
ATOM   7809  C CA  . LEU C 1 195 ? 31.038  6.004   53.338  1.00 43.60  ? 204  LEU C CA  1 
ATOM   7810  C C   . LEU C 1 195 ? 31.264  6.758   52.052  1.00 42.87  ? 204  LEU C C   1 
ATOM   7811  O O   . LEU C 1 195 ? 30.297  7.150   51.459  1.00 42.48  ? 204  LEU C O   1 
ATOM   7812  C CB  . LEU C 1 195 ? 31.091  6.980   54.511  1.00 44.18  ? 204  LEU C CB  1 
ATOM   7813  C CG  . LEU C 1 195 ? 29.853  7.854   54.685  1.00 44.42  ? 204  LEU C CG  1 
ATOM   7814  C CD1 . LEU C 1 195 ? 28.712  7.044   55.306  1.00 43.78  ? 204  LEU C CD1 1 
ATOM   7815  C CD2 . LEU C 1 195 ? 30.171  9.124   55.520  1.00 46.46  ? 204  LEU C CD2 1 
ATOM   7816  N N   . PRO C 1 196 ? 32.533  6.993   51.643  1.00 43.26  ? 205  PRO C N   1 
ATOM   7817  C CA  . PRO C 1 196 ? 32.775  7.603   50.347  1.00 42.82  ? 205  PRO C CA  1 
ATOM   7818  C C   . PRO C 1 196 ? 32.238  6.788   49.210  1.00 42.30  ? 205  PRO C C   1 
ATOM   7819  O O   . PRO C 1 196 ? 31.708  7.373   48.255  1.00 41.93  ? 205  PRO C O   1 
ATOM   7820  C CB  . PRO C 1 196 ? 34.292  7.613   50.226  1.00 43.49  ? 205  PRO C CB  1 
ATOM   7821  C CG  . PRO C 1 196 ? 34.776  7.670   51.573  1.00 44.67  ? 205  PRO C CG  1 
ATOM   7822  C CD  . PRO C 1 196 ? 33.774  6.956   52.439  1.00 44.43  ? 205  PRO C CD  1 
ATOM   7823  N N   . ILE C 1 197 ? 32.369  5.465   49.284  1.00 42.29  ? 206  ILE C N   1 
ATOM   7824  C CA  . ILE C 1 197 ? 31.994  4.680   48.126  1.00 41.87  ? 206  ILE C CA  1 
ATOM   7825  C C   . ILE C 1 197 ? 30.590  4.240   48.214  1.00 40.97  ? 206  ILE C C   1 
ATOM   7826  O O   . ILE C 1 197 ? 30.079  3.663   47.282  1.00 40.37  ? 206  ILE C O   1 
ATOM   7827  C CB  . ILE C 1 197 ? 32.958  3.531   47.744  1.00 42.91  ? 206  ILE C CB  1 
ATOM   7828  C CG1 . ILE C 1 197 ? 32.461  2.166   48.248  1.00 43.86  ? 206  ILE C CG1 1 
ATOM   7829  C CG2 . ILE C 1 197 ? 34.449  3.871   48.098  1.00 44.55  ? 206  ILE C CG2 1 
ATOM   7830  C CD1 . ILE C 1 197 ? 33.067  0.953   47.431  1.00 46.37  ? 206  ILE C CD1 1 
ATOM   7831  N N   . VAL C 1 198 ? 29.949  4.522   49.329  1.00 41.38  ? 207  VAL C N   1 
ATOM   7832  C CA  . VAL C 1 198 ? 28.517  4.344   49.353  1.00 41.57  ? 207  VAL C CA  1 
ATOM   7833  C C   . VAL C 1 198 ? 27.976  5.483   48.568  1.00 41.05  ? 207  VAL C C   1 
ATOM   7834  O O   . VAL C 1 198 ? 27.360  5.290   47.536  1.00 40.84  ? 207  VAL C O   1 
ATOM   7835  C CB  . VAL C 1 198 ? 27.901  4.390   50.747  1.00 42.00  ? 207  VAL C CB  1 
ATOM   7836  C CG1 . VAL C 1 198 ? 26.379  4.493   50.634  1.00 41.34  ? 207  VAL C CG1 1 
ATOM   7837  C CG2 . VAL C 1 198 ? 28.281  3.155   51.534  1.00 43.39  ? 207  VAL C CG2 1 
ATOM   7838  N N   . ASN C 1 199 ? 28.220  6.689   49.047  1.00 41.64  ? 208  ASN C N   1 
ATOM   7839  C CA  . ASN C 1 199 ? 27.610  7.817   48.378  1.00 41.84  ? 208  ASN C CA  1 
ATOM   7840  C C   . ASN C 1 199 ? 28.362  8.224   47.095  1.00 41.66  ? 208  ASN C C   1 
ATOM   7841  O O   . ASN C 1 199 ? 28.079  9.245   46.462  1.00 41.40  ? 208  ASN C O   1 
ATOM   7842  C CB  . ASN C 1 199 ? 27.126  8.946   49.343  1.00 42.09  ? 208  ASN C CB  1 
ATOM   7843  C CG  . ASN C 1 199 ? 28.243  9.669   50.031  1.00 42.55  ? 208  ASN C CG  1 
ATOM   7844  O OD1 . ASN C 1 199 ? 29.413  9.350   49.874  1.00 43.58  ? 208  ASN C OD1 1 
ATOM   7845  N ND2 . ASN C 1 199 ? 27.884  10.667  50.795  1.00 42.47  ? 208  ASN C ND2 1 
ATOM   7846  N N   . LYS C 1 200 ? 29.276  7.365   46.676  1.00 42.12  ? 209  LYS C N   1 
ATOM   7847  C CA  . LYS C 1 200 ? 29.699  7.414   45.289  1.00 42.11  ? 209  LYS C CA  1 
ATOM   7848  C C   . LYS C 1 200 ? 28.680  6.645   44.442  1.00 41.29  ? 209  LYS C C   1 
ATOM   7849  O O   . LYS C 1 200 ? 28.234  7.152   43.402  1.00 40.60  ? 209  LYS C O   1 
ATOM   7850  C CB  . LYS C 1 200 ? 31.089  6.843   45.117  1.00 43.04  ? 209  LYS C CB  1 
ATOM   7851  C CG  . LYS C 1 200 ? 32.002  7.756   44.358  1.00 44.57  ? 209  LYS C CG  1 
ATOM   7852  C CD  . LYS C 1 200 ? 33.434  7.702   44.927  1.00 47.57  ? 209  LYS C CD  1 
ATOM   7853  C CE  . LYS C 1 200 ? 34.340  6.809   44.072  1.00 49.11  ? 209  LYS C CE  1 
ATOM   7854  N NZ  . LYS C 1 200 ? 35.299  6.097   44.954  1.00 51.70  ? 209  LYS C NZ  1 
ATOM   7855  N N   . GLN C 1 201 ? 28.310  5.439   44.891  1.00 41.31  ? 210  GLN C N   1 
ATOM   7856  C CA  . GLN C 1 201 ? 27.252  4.676   44.249  1.00 40.98  ? 210  GLN C CA  1 
ATOM   7857  C C   . GLN C 1 201 ? 25.989  5.510   44.204  1.00 40.73  ? 210  GLN C C   1 
ATOM   7858  O O   . GLN C 1 201 ? 25.293  5.547   43.183  1.00 40.30  ? 210  GLN C O   1 
ATOM   7859  C CB  . GLN C 1 201 ? 26.932  3.421   45.020  1.00 41.42  ? 210  GLN C CB  1 
ATOM   7860  C CG  . GLN C 1 201 ? 27.987  2.353   45.050  1.00 42.71  ? 210  GLN C CG  1 
ATOM   7861  C CD  . GLN C 1 201 ? 27.596  1.191   45.999  1.00 44.88  ? 210  GLN C CD  1 
ATOM   7862  O OE1 . GLN C 1 201 ? 26.718  1.330   46.870  1.00 45.15  ? 210  GLN C OE1 1 
ATOM   7863  N NE2 . GLN C 1 201 ? 28.250  0.048   45.830  1.00 45.49  ? 210  GLN C NE2 1 
ATOM   7864  N N   . SER C 1 202 ? 25.683  6.192   45.307  1.00 41.29  ? 211  SER C N   1 
ATOM   7865  C CA  . SER C 1 202 ? 24.483  7.027   45.336  1.00 41.50  ? 211  SER C CA  1 
ATOM   7866  C C   . SER C 1 202 ? 24.497  7.980   44.166  1.00 41.17  ? 211  SER C C   1 
ATOM   7867  O O   . SER C 1 202 ? 23.481  8.223   43.558  1.00 40.79  ? 211  SER C O   1 
ATOM   7868  C CB  . SER C 1 202 ? 24.349  7.808   46.636  1.00 41.94  ? 211  SER C CB  1 
ATOM   7869  O OG  . SER C 1 202 ? 23.832  6.996   47.680  1.00 43.15  ? 211  SER C OG  1 
ATOM   7870  N N   . CYS C 1 203 ? 25.662  8.499   43.823  1.00 41.67  ? 212  CYS C N   1 
ATOM   7871  C CA  . CYS C 1 203 ? 25.738  9.341   42.657  1.00 41.62  ? 212  CYS C CA  1 
ATOM   7872  C C   . CYS C 1 203 ? 25.484  8.616   41.344  1.00 40.40  ? 212  CYS C C   1 
ATOM   7873  O O   . CYS C 1 203 ? 24.534  8.937   40.627  1.00 39.49  ? 212  CYS C O   1 
ATOM   7874  C CB  . CYS C 1 203 ? 27.066  10.026  42.560  1.00 42.63  ? 212  CYS C CB  1 
ATOM   7875  S SG  . CYS C 1 203 ? 26.876  11.129  41.239  1.00 46.83  ? 212  CYS C SG  1 
ATOM   7876  N N   . SER C 1 204 ? 26.348  7.664   41.019  1.00 40.18  ? 213  SER C N   1 
ATOM   7877  C CA  . SER C 1 204 ? 26.162  6.835   39.831  1.00 39.80  ? 213  SER C CA  1 
ATOM   7878  C C   . SER C 1 204 ? 24.712  6.425   39.603  1.00 38.85  ? 213  SER C C   1 
ATOM   7879  O O   . SER C 1 204 ? 24.204  6.509   38.487  1.00 38.81  ? 213  SER C O   1 
ATOM   7880  C CB  . SER C 1 204 ? 27.039  5.587   39.883  1.00 40.62  ? 213  SER C CB  1 
ATOM   7881  O OG  . SER C 1 204 ? 28.410  5.939   39.856  1.00 42.35  ? 213  SER C OG  1 
ATOM   7882  N N   . ILE C 1 205 ? 24.035  5.986   40.652  1.00 38.34  ? 214  ILE C N   1 
ATOM   7883  C CA  . ILE C 1 205 ? 22.617  5.670   40.515  1.00 37.63  ? 214  ILE C CA  1 
ATOM   7884  C C   . ILE C 1 205 ? 21.786  6.890   40.068  1.00 36.83  ? 214  ILE C C   1 
ATOM   7885  O O   . ILE C 1 205 ? 21.001  6.786   39.115  1.00 36.52  ? 214  ILE C O   1 
ATOM   7886  C CB  . ILE C 1 205 ? 22.063  5.049   41.794  1.00 38.18  ? 214  ILE C CB  1 
ATOM   7887  C CG1 . ILE C 1 205 ? 22.727  3.706   42.016  1.00 38.84  ? 214  ILE C CG1 1 
ATOM   7888  C CG2 . ILE C 1 205 ? 20.552  4.854   41.720  1.00 37.50  ? 214  ILE C CG2 1 
ATOM   7889  C CD1 . ILE C 1 205 ? 22.774  3.320   43.446  1.00 40.86  ? 214  ILE C CD1 1 
ATOM   7890  N N   . SER C 1 206 ? 21.985  8.040   40.721  1.00 36.32  ? 215  SER C N   1 
ATOM   7891  C CA  . SER C 1 206 ? 21.267  9.254   40.348  1.00 35.51  ? 215  SER C CA  1 
ATOM   7892  C C   . SER C 1 206 ? 21.425  9.473   38.857  1.00 34.43  ? 215  SER C C   1 
ATOM   7893  O O   . SER C 1 206 ? 20.461  9.782   38.162  1.00 34.00  ? 215  SER C O   1 
ATOM   7894  C CB  . SER C 1 206 ? 21.763  10.477  41.130  1.00 36.07  ? 215  SER C CB  1 
ATOM   7895  O OG  . SER C 1 206 ? 20.908  11.614  40.941  1.00 36.38  ? 215  SER C OG  1 
ATOM   7896  N N   . ASN C 1 207 ? 22.638  9.277   38.367  1.00 33.60  ? 216  ASN C N   1 
ATOM   7897  C CA  . ASN C 1 207 ? 22.874  9.394   36.962  1.00 32.70  ? 216  ASN C CA  1 
ATOM   7898  C C   . ASN C 1 207 ? 22.096  8.410   36.146  1.00 31.95  ? 216  ASN C C   1 
ATOM   7899  O O   . ASN C 1 207 ? 21.321  8.808   35.303  1.00 31.87  ? 216  ASN C O   1 
ATOM   7900  C CB  . ASN C 1 207 ? 24.339  9.266   36.657  1.00 33.36  ? 216  ASN C CB  1 
ATOM   7901  C CG  . ASN C 1 207 ? 25.154  10.303  37.367  1.00 34.80  ? 216  ASN C CG  1 
ATOM   7902  O OD1 . ASN C 1 207 ? 24.613  11.209  38.037  1.00 35.50  ? 216  ASN C OD1 1 
ATOM   7903  N ND2 . ASN C 1 207 ? 26.473  10.190  37.230  1.00 36.62  ? 216  ASN C ND2 1 
ATOM   7904  N N   . ILE C 1 208 ? 22.285  7.124   36.382  1.00 31.55  ? 217  ILE C N   1 
ATOM   7905  C CA  . ILE C 1 208 ? 21.564  6.112   35.621  1.00 31.17  ? 217  ILE C CA  1 
ATOM   7906  C C   . ILE C 1 208 ? 20.081  6.390   35.593  1.00 30.88  ? 217  ILE C C   1 
ATOM   7907  O O   . ILE C 1 208 ? 19.457  6.411   34.560  1.00 30.21  ? 217  ILE C O   1 
ATOM   7908  C CB  . ILE C 1 208 ? 21.769  4.772   36.233  1.00 31.74  ? 217  ILE C CB  1 
ATOM   7909  C CG1 . ILE C 1 208 ? 23.192  4.342   35.997  1.00 32.26  ? 217  ILE C CG1 1 
ATOM   7910  C CG2 . ILE C 1 208 ? 20.873  3.771   35.598  1.00 32.27  ? 217  ILE C CG2 1 
ATOM   7911  C CD1 . ILE C 1 208 ? 23.603  3.270   36.900  1.00 33.58  ? 217  ILE C CD1 1 
ATOM   7912  N N   . GLU C 1 209 ? 19.519  6.609   36.755  1.00 31.67  ? 218  GLU C N   1 
ATOM   7913  C CA  . GLU C 1 209 ? 18.136  6.994   36.826  1.00 32.73  ? 218  GLU C CA  1 
ATOM   7914  C C   . GLU C 1 209 ? 17.849  8.171   35.905  1.00 31.61  ? 218  GLU C C   1 
ATOM   7915  O O   . GLU C 1 209 ? 16.926  8.119   35.085  1.00 31.61  ? 218  GLU C O   1 
ATOM   7916  C CB  . GLU C 1 209 ? 17.751  7.364   38.264  1.00 33.71  ? 218  GLU C CB  1 
ATOM   7917  C CG  . GLU C 1 209 ? 17.568  6.147   39.150  1.00 38.58  ? 218  GLU C CG  1 
ATOM   7918  C CD  . GLU C 1 209 ? 17.378  6.491   40.631  1.00 44.52  ? 218  GLU C CD  1 
ATOM   7919  O OE1 . GLU C 1 209 ? 17.747  7.614   41.038  1.00 45.60  ? 218  GLU C OE1 1 
ATOM   7920  O OE2 . GLU C 1 209 ? 16.866  5.614   41.387  1.00 47.39  ? 218  GLU C OE2 1 
ATOM   7921  N N   . THR C 1 210 ? 18.627  9.239   36.046  1.00 30.87  ? 219  THR C N   1 
ATOM   7922  C CA  . THR C 1 210 ? 18.424  10.411  35.211  1.00 29.71  ? 219  THR C CA  1 
ATOM   7923  C C   . THR C 1 210 ? 18.458  10.042  33.728  1.00 28.73  ? 219  THR C C   1 
ATOM   7924  O O   . THR C 1 210 ? 17.517  10.310  33.012  1.00 28.99  ? 219  THR C O   1 
ATOM   7925  C CB  . THR C 1 210 ? 19.430  11.474  35.509  1.00 29.81  ? 219  THR C CB  1 
ATOM   7926  O OG1 . THR C 1 210 ? 19.317  11.837  36.895  1.00 30.52  ? 219  THR C OG1 1 
ATOM   7927  C CG2 . THR C 1 210 ? 19.156  12.657  34.640  1.00 29.31  ? 219  THR C CG2 1 
ATOM   7928  N N   . VAL C 1 211 ? 19.502  9.376   33.273  1.00 27.71  ? 220  VAL C N   1 
ATOM   7929  C CA  . VAL C 1 211 ? 19.497  8.874   31.904  1.00 26.50  ? 220  VAL C CA  1 
ATOM   7930  C C   . VAL C 1 211 ? 18.199  8.161   31.513  1.00 26.18  ? 220  VAL C C   1 
ATOM   7931  O O   . VAL C 1 211 ? 17.498  8.604   30.625  1.00 25.57  ? 220  VAL C O   1 
ATOM   7932  C CB  . VAL C 1 211 ? 20.709  7.980   31.612  1.00 26.68  ? 220  VAL C CB  1 
ATOM   7933  C CG1 . VAL C 1 211 ? 20.459  7.172   30.353  1.00 26.04  ? 220  VAL C CG1 1 
ATOM   7934  C CG2 . VAL C 1 211 ? 21.970  8.835   31.475  1.00 26.32  ? 220  VAL C CG2 1 
ATOM   7935  N N   . ILE C 1 212 ? 17.887  7.058   32.182  1.00 26.66  ? 221  ILE C N   1 
ATOM   7936  C CA  . ILE C 1 212 ? 16.677  6.306   31.879  1.00 26.86  ? 221  ILE C CA  1 
ATOM   7937  C C   . ILE C 1 212 ? 15.505  7.245   31.770  1.00 27.24  ? 221  ILE C C   1 
ATOM   7938  O O   . ILE C 1 212 ? 14.818  7.270   30.761  1.00 27.15  ? 221  ILE C O   1 
ATOM   7939  C CB  . ILE C 1 212 ? 16.317  5.308   32.970  1.00 27.14  ? 221  ILE C CB  1 
ATOM   7940  C CG1 . ILE C 1 212 ? 17.430  4.319   33.195  1.00 26.73  ? 221  ILE C CG1 1 
ATOM   7941  C CG2 . ILE C 1 212 ? 15.073  4.580   32.590  1.00 26.78  ? 221  ILE C CG2 1 
ATOM   7942  C CD1 . ILE C 1 212 ? 17.702  3.539   31.987  1.00 26.94  ? 221  ILE C CD1 1 
ATOM   7943  N N   . GLU C 1 213 ? 15.298  8.037   32.806  1.00 28.23  ? 222  GLU C N   1 
ATOM   7944  C CA  . GLU C 1 213 ? 14.153  8.894   32.864  1.00 29.84  ? 222  GLU C CA  1 
ATOM   7945  C C   . GLU C 1 213 ? 14.160  9.956   31.731  1.00 29.52  ? 222  GLU C C   1 
ATOM   7946  O O   . GLU C 1 213 ? 13.132  10.548  31.374  1.00 29.69  ? 222  GLU C O   1 
ATOM   7947  C CB  . GLU C 1 213 ? 14.071  9.523   34.244  1.00 30.41  ? 222  GLU C CB  1 
ATOM   7948  C CG  . GLU C 1 213 ? 12.642  9.735   34.746  1.00 34.43  ? 222  GLU C CG  1 
ATOM   7949  C CD  . GLU C 1 213 ? 12.586  10.411  36.129  1.00 40.34  ? 222  GLU C CD  1 
ATOM   7950  O OE1 . GLU C 1 213 ? 13.674  10.706  36.674  1.00 43.36  ? 222  GLU C OE1 1 
ATOM   7951  O OE2 . GLU C 1 213 ? 11.473  10.655  36.688  1.00 42.91  ? 222  GLU C OE2 1 
ATOM   7952  N N   . PHE C 1 214 ? 15.319  10.176  31.138  1.00 29.52  ? 223  PHE C N   1 
ATOM   7953  C CA  . PHE C 1 214 ? 15.416  11.093  30.014  1.00 29.13  ? 223  PHE C CA  1 
ATOM   7954  C C   . PHE C 1 214 ? 14.888  10.415  28.766  1.00 29.38  ? 223  PHE C C   1 
ATOM   7955  O O   . PHE C 1 214 ? 14.220  11.041  27.954  1.00 29.44  ? 223  PHE C O   1 
ATOM   7956  C CB  . PHE C 1 214 ? 16.863  11.467  29.809  1.00 28.79  ? 223  PHE C CB  1 
ATOM   7957  C CG  . PHE C 1 214 ? 17.135  12.187  28.539  1.00 27.98  ? 223  PHE C CG  1 
ATOM   7958  C CD1 . PHE C 1 214 ? 17.081  13.555  28.496  1.00 28.03  ? 223  PHE C CD1 1 
ATOM   7959  C CD2 . PHE C 1 214 ? 17.492  11.512  27.391  1.00 27.55  ? 223  PHE C CD2 1 
ATOM   7960  C CE1 . PHE C 1 214 ? 17.391  14.245  27.315  1.00 27.08  ? 223  PHE C CE1 1 
ATOM   7961  C CE2 . PHE C 1 214 ? 17.780  12.193  26.231  1.00 27.13  ? 223  PHE C CE2 1 
ATOM   7962  C CZ  . PHE C 1 214 ? 17.736  13.558  26.197  1.00 26.43  ? 223  PHE C CZ  1 
ATOM   7963  N N   . GLN C 1 215 ? 15.191  9.134   28.607  1.00 29.81  ? 224  GLN C N   1 
ATOM   7964  C CA  . GLN C 1 215 ? 14.722  8.413   27.452  1.00 30.40  ? 224  GLN C CA  1 
ATOM   7965  C C   . GLN C 1 215 ? 13.265  8.170   27.602  1.00 30.42  ? 224  GLN C C   1 
ATOM   7966  O O   . GLN C 1 215 ? 12.541  8.131   26.630  1.00 30.44  ? 224  GLN C O   1 
ATOM   7967  C CB  . GLN C 1 215 ? 15.447  7.098   27.324  1.00 31.25  ? 224  GLN C CB  1 
ATOM   7968  C CG  . GLN C 1 215 ? 16.919  7.296   27.526  1.00 33.97  ? 224  GLN C CG  1 
ATOM   7969  C CD  . GLN C 1 215 ? 17.717  6.034   27.353  1.00 37.88  ? 224  GLN C CD  1 
ATOM   7970  O OE1 . GLN C 1 215 ? 17.288  4.942   27.807  1.00 39.72  ? 224  GLN C OE1 1 
ATOM   7971  N NE2 . GLN C 1 215 ? 18.899  6.158   26.702  1.00 38.19  ? 224  GLN C NE2 1 
ATOM   7972  N N   . GLN C 1 216 ? 12.833  8.017   28.837  1.00 30.69  ? 225  GLN C N   1 
ATOM   7973  C CA  . GLN C 1 216 ? 11.469  7.674   29.101  1.00 31.25  ? 225  GLN C CA  1 
ATOM   7974  C C   . GLN C 1 216 ? 10.574  8.831   28.747  1.00 30.85  ? 225  GLN C C   1 
ATOM   7975  O O   . GLN C 1 216 ? 9.632   8.708   27.970  1.00 30.46  ? 225  GLN C O   1 
ATOM   7976  C CB  . GLN C 1 216 ? 11.324  7.381   30.571  1.00 32.03  ? 225  GLN C CB  1 
ATOM   7977  C CG  . GLN C 1 216 ? 12.047  6.145   31.033  1.00 33.97  ? 225  GLN C CG  1 
ATOM   7978  C CD  . GLN C 1 216 ? 11.278  5.411   32.106  1.00 36.88  ? 225  GLN C CD  1 
ATOM   7979  O OE1 . GLN C 1 216 ? 10.920  5.984   33.136  1.00 37.97  ? 225  GLN C OE1 1 
ATOM   7980  N NE2 . GLN C 1 216 ? 11.001  4.138   31.862  1.00 37.94  ? 225  GLN C NE2 1 
ATOM   7981  N N   . LYS C 1 217 ? 10.889  9.972   29.329  1.00 30.85  ? 226  LYS C N   1 
ATOM   7982  C CA  . LYS C 1 217 ? 10.051  11.142  29.196  1.00 31.20  ? 226  LYS C CA  1 
ATOM   7983  C C   . LYS C 1 217 ? 10.237  11.806  27.849  1.00 30.15  ? 226  LYS C C   1 
ATOM   7984  O O   . LYS C 1 217 ? 9.358   12.487  27.376  1.00 30.36  ? 226  LYS C O   1 
ATOM   7985  C CB  . LYS C 1 217 ? 10.390  12.151  30.287  1.00 31.81  ? 226  LYS C CB  1 
ATOM   7986  C CG  . LYS C 1 217 ? 9.938   11.773  31.676  1.00 34.57  ? 226  LYS C CG  1 
ATOM   7987  C CD  . LYS C 1 217 ? 9.953   13.011  32.572  1.00 38.10  ? 226  LYS C CD  1 
ATOM   7988  C CE  . LYS C 1 217 ? 9.608   12.672  34.032  1.00 41.50  ? 226  LYS C CE  1 
ATOM   7989  N NZ  . LYS C 1 217 ? 10.145  13.751  34.942  1.00 43.35  ? 226  LYS C NZ  1 
ATOM   7990  N N   . ASN C 1 218 ? 11.398  11.640  27.241  1.00 29.18  ? 227  ASN C N   1 
ATOM   7991  C CA  . ASN C 1 218 ? 11.628  12.243  25.946  1.00 28.39  ? 227  ASN C CA  1 
ATOM   7992  C C   . ASN C 1 218 ? 11.347  11.287  24.800  1.00 28.66  ? 227  ASN C C   1 
ATOM   7993  O O   . ASN C 1 218 ? 11.751  11.524  23.653  1.00 28.47  ? 227  ASN C O   1 
ATOM   7994  C CB  . ASN C 1 218 ? 13.035  12.811  25.872  1.00 27.65  ? 227  ASN C CB  1 
ATOM   7995  C CG  . ASN C 1 218 ? 13.079  14.249  26.295  1.00 27.37  ? 227  ASN C CG  1 
ATOM   7996  O OD1 . ASN C 1 218 ? 12.247  15.049  25.855  1.00 27.78  ? 227  ASN C OD1 1 
ATOM   7997  N ND2 . ASN C 1 218 ? 14.028  14.596  27.155  1.00 26.72  ? 227  ASN C ND2 1 
ATOM   7998  N N   . ASN C 1 219 ? 10.609  10.224  25.117  1.00 29.19  ? 228  ASN C N   1 
ATOM   7999  C CA  . ASN C 1 219 ? 10.419  9.101   24.218  1.00 29.01  ? 228  ASN C CA  1 
ATOM   8000  C C   . ASN C 1 219 ? 9.924   9.502   22.849  1.00 28.06  ? 228  ASN C C   1 
ATOM   8001  O O   . ASN C 1 219 ? 10.565  9.229   21.817  1.00 27.78  ? 228  ASN C O   1 
ATOM   8002  C CB  . ASN C 1 219 ? 9.437   8.133   24.822  1.00 30.08  ? 228  ASN C CB  1 
ATOM   8003  C CG  . ASN C 1 219 ? 9.109   7.035   23.892  1.00 32.03  ? 228  ASN C CG  1 
ATOM   8004  O OD1 . ASN C 1 219 ? 8.052   7.056   23.288  1.00 34.13  ? 228  ASN C OD1 1 
ATOM   8005  N ND2 . ASN C 1 219 ? 10.029  6.075   23.721  1.00 33.86  ? 228  ASN C ND2 1 
ATOM   8006  N N   . ARG C 1 220 ? 8.778   10.168  22.849  1.00 27.15  ? 229  ARG C N   1 
ATOM   8007  C CA  . ARG C 1 220 ? 8.168   10.550  21.600  1.00 25.86  ? 229  ARG C CA  1 
ATOM   8008  C C   . ARG C 1 220 ? 9.150   11.323  20.756  1.00 24.77  ? 229  ARG C C   1 
ATOM   8009  O O   . ARG C 1 220 ? 9.369   10.978  19.616  1.00 24.80  ? 229  ARG C O   1 
ATOM   8010  C CB  . ARG C 1 220 ? 6.934   11.369  21.849  1.00 26.05  ? 229  ARG C CB  1 
ATOM   8011  C CG  . ARG C 1 220 ? 5.861   11.091  20.866  1.00 25.15  ? 229  ARG C CG  1 
ATOM   8012  C CD  . ARG C 1 220 ? 4.709   11.952  21.171  1.00 24.85  ? 229  ARG C CD  1 
ATOM   8013  N NE  . ARG C 1 220 ? 4.122   12.433  19.937  1.00 25.47  ? 229  ARG C NE  1 
ATOM   8014  C CZ  . ARG C 1 220 ? 3.273   13.462  19.840  1.00 26.05  ? 229  ARG C CZ  1 
ATOM   8015  N NH1 . ARG C 1 220 ? 2.921   14.158  20.911  1.00 25.88  ? 229  ARG C NH1 1 
ATOM   8016  N NH2 . ARG C 1 220 ? 2.773   13.811  18.653  1.00 27.00  ? 229  ARG C NH2 1 
ATOM   8017  N N   . LEU C 1 221 ? 9.782   12.335  21.325  1.00 23.95  ? 230  LEU C N   1 
ATOM   8018  C CA  . LEU C 1 221 ? 10.760  13.103  20.576  1.00 23.10  ? 230  LEU C CA  1 
ATOM   8019  C C   . LEU C 1 221 ? 11.822  12.223  20.019  1.00 23.00  ? 230  LEU C C   1 
ATOM   8020  O O   . LEU C 1 221 ? 12.223  12.375  18.893  1.00 22.98  ? 230  LEU C O   1 
ATOM   8021  C CB  . LEU C 1 221 ? 11.439  14.138  21.436  1.00 23.11  ? 230  LEU C CB  1 
ATOM   8022  C CG  . LEU C 1 221 ? 12.449  15.016  20.722  1.00 22.20  ? 230  LEU C CG  1 
ATOM   8023  C CD1 . LEU C 1 221 ? 11.748  16.148  20.070  1.00 22.66  ? 230  LEU C CD1 1 
ATOM   8024  C CD2 . LEU C 1 221 ? 13.368  15.578  21.725  1.00 23.37  ? 230  LEU C CD2 1 
ATOM   8025  N N   . LEU C 1 222 ? 12.287  11.284  20.805  1.00 23.22  ? 231  LEU C N   1 
ATOM   8026  C CA  . LEU C 1 222 ? 13.360  10.473  20.313  1.00 23.56  ? 231  LEU C CA  1 
ATOM   8027  C C   . LEU C 1 222 ? 12.877  9.648   19.155  1.00 23.66  ? 231  LEU C C   1 
ATOM   8028  O O   . LEU C 1 222 ? 13.526  9.576   18.116  1.00 24.12  ? 231  LEU C O   1 
ATOM   8029  C CB  . LEU C 1 222 ? 13.946  9.624   21.421  1.00 24.11  ? 231  LEU C CB  1 
ATOM   8030  C CG  . LEU C 1 222 ? 14.571  10.506  22.502  1.00 24.12  ? 231  LEU C CG  1 
ATOM   8031  C CD1 . LEU C 1 222 ? 14.598  9.802   23.807  1.00 26.62  ? 231  LEU C CD1 1 
ATOM   8032  C CD2 . LEU C 1 222 ? 15.941  10.889  22.133  1.00 24.88  ? 231  LEU C CD2 1 
ATOM   8033  N N   . GLU C 1 223 ? 11.712  9.060   19.303  1.00 23.66  ? 232  GLU C N   1 
ATOM   8034  C CA  . GLU C 1 223 ? 11.203  8.261   18.224  1.00 24.08  ? 232  GLU C CA  1 
ATOM   8035  C C   . GLU C 1 223 ? 11.125  9.038   16.948  1.00 23.07  ? 232  GLU C C   1 
ATOM   8036  O O   . GLU C 1 223 ? 11.527  8.561   15.908  1.00 23.78  ? 232  GLU C O   1 
ATOM   8037  C CB  . GLU C 1 223 ? 9.861   7.683   18.574  1.00 24.74  ? 232  GLU C CB  1 
ATOM   8038  C CG  . GLU C 1 223 ? 9.970   6.510   19.547  1.00 27.76  ? 232  GLU C CG  1 
ATOM   8039  C CD  . GLU C 1 223 ? 10.666  5.228   18.980  1.00 31.74  ? 232  GLU C CD  1 
ATOM   8040  O OE1 . GLU C 1 223 ? 10.999  5.120   17.746  1.00 31.57  ? 232  GLU C OE1 1 
ATOM   8041  O OE2 . GLU C 1 223 ? 10.866  4.308   19.812  1.00 33.24  ? 232  GLU C OE2 1 
ATOM   8042  N N   . ILE C 1 224 ? 10.634  10.255  17.036  1.00 21.97  ? 233  ILE C N   1 
ATOM   8043  C CA  . ILE C 1 224 ? 10.582  11.134  15.881  1.00 21.30  ? 233  ILE C CA  1 
ATOM   8044  C C   . ILE C 1 224 ? 11.978  11.378  15.276  1.00 21.09  ? 233  ILE C C   1 
ATOM   8045  O O   . ILE C 1 224 ? 12.231  11.101  14.108  1.00 20.99  ? 233  ILE C O   1 
ATOM   8046  C CB  . ILE C 1 224 ? 9.962   12.487  16.269  1.00 20.68  ? 233  ILE C CB  1 
ATOM   8047  C CG1 . ILE C 1 224 ? 8.674   12.275  17.022  1.00 20.19  ? 233  ILE C CG1 1 
ATOM   8048  C CG2 . ILE C 1 224 ? 9.721   13.316  15.053  1.00 20.54  ? 233  ILE C CG2 1 
ATOM   8049  C CD1 . ILE C 1 224 ? 7.748   13.396  16.934  1.00 20.46  ? 233  ILE C CD1 1 
ATOM   8050  N N   . THR C 1 225 ? 12.872  11.898  16.099  1.00 20.89  ? 234  THR C N   1 
ATOM   8051  C CA  . THR C 1 225 ? 14.228  12.172  15.719  1.00 21.13  ? 234  THR C CA  1 
ATOM   8052  C C   . THR C 1 225 ? 14.808  11.046  14.913  1.00 22.11  ? 234  THR C C   1 
ATOM   8053  O O   . THR C 1 225 ? 15.475  11.286  13.931  1.00 22.54  ? 234  THR C O   1 
ATOM   8054  C CB  . THR C 1 225 ? 15.039  12.343  16.956  1.00 21.19  ? 234  THR C CB  1 
ATOM   8055  O OG1 . THR C 1 225 ? 14.769  13.629  17.479  1.00 20.93  ? 234  THR C OG1 1 
ATOM   8056  C CG2 . THR C 1 225 ? 16.468  12.253  16.691  1.00 21.64  ? 234  THR C CG2 1 
ATOM   8057  N N   . ARG C 1 226 ? 14.556  9.812   15.323  1.00 22.93  ? 235  ARG C N   1 
ATOM   8058  C CA  . ARG C 1 226 ? 15.045  8.673   14.576  1.00 24.11  ? 235  ARG C CA  1 
ATOM   8059  C C   . ARG C 1 226 ? 14.417  8.632   13.222  1.00 24.06  ? 235  ARG C C   1 
ATOM   8060  O O   . ARG C 1 226 ? 15.094  8.786   12.229  1.00 24.49  ? 235  ARG C O   1 
ATOM   8061  C CB  . ARG C 1 226 ? 14.705  7.382   15.291  1.00 24.92  ? 235  ARG C CB  1 
ATOM   8062  C CG  . ARG C 1 226 ? 15.007  6.122   14.459  1.00 27.39  ? 235  ARG C CG  1 
ATOM   8063  C CD  . ARG C 1 226 ? 14.309  4.939   15.043  1.00 30.31  ? 235  ARG C CD  1 
ATOM   8064  N NE  . ARG C 1 226 ? 14.334  5.030   16.500  1.00 30.21  ? 235  ARG C NE  1 
ATOM   8065  C CZ  . ARG C 1 226 ? 15.344  4.616   17.247  1.00 28.31  ? 235  ARG C CZ  1 
ATOM   8066  N NH1 . ARG C 1 226 ? 16.390  4.061   16.659  1.00 27.24  ? 235  ARG C NH1 1 
ATOM   8067  N NH2 . ARG C 1 226 ? 15.283  4.756   18.565  1.00 27.00  ? 235  ARG C NH2 1 
ATOM   8068  N N   . GLU C 1 227 ? 13.113  8.402   13.217  1.00 23.98  ? 236  GLU C N   1 
ATOM   8069  C CA  . GLU C 1 227 ? 12.290  8.389   12.042  1.00 24.20  ? 236  GLU C CA  1 
ATOM   8070  C C   . GLU C 1 227 ? 12.816  9.418   11.013  1.00 23.13  ? 236  GLU C C   1 
ATOM   8071  O O   . GLU C 1 227 ? 13.005  9.106   9.844   1.00 23.45  ? 236  GLU C O   1 
ATOM   8072  C CB  . GLU C 1 227 ? 10.852  8.674   12.503  1.00 24.39  ? 236  GLU C CB  1 
ATOM   8073  C CG  . GLU C 1 227 ? 9.702   7.935   11.771  1.00 27.49  ? 236  GLU C CG  1 
ATOM   8074  C CD  . GLU C 1 227 ? 8.280   8.304   12.343  1.00 30.11  ? 236  GLU C CD  1 
ATOM   8075  O OE1 . GLU C 1 227 ? 7.316   8.591   11.557  1.00 32.85  ? 236  GLU C OE1 1 
ATOM   8076  O OE2 . GLU C 1 227 ? 8.125   8.318   13.580  1.00 27.97  ? 236  GLU C OE2 1 
ATOM   8077  N N   . PHE C 1 228 ? 13.108  10.630  11.455  1.00 21.83  ? 237  PHE C N   1 
ATOM   8078  C CA  . PHE C 1 228 ? 13.561  11.635  10.528  1.00 21.33  ? 237  PHE C CA  1 
ATOM   8079  C C   . PHE C 1 228 ? 14.948  11.391  10.014  1.00 21.64  ? 237  PHE C C   1 
ATOM   8080  O O   . PHE C 1 228 ? 15.192  11.600  8.860   1.00 21.87  ? 237  PHE C O   1 
ATOM   8081  C CB  . PHE C 1 228 ? 13.510  12.998  11.150  1.00 20.99  ? 237  PHE C CB  1 
ATOM   8082  C CG  . PHE C 1 228 ? 12.204  13.659  11.010  1.00 21.57  ? 237  PHE C CG  1 
ATOM   8083  C CD1 . PHE C 1 228 ? 11.568  14.193  12.101  1.00 22.26  ? 237  PHE C CD1 1 
ATOM   8084  C CD2 . PHE C 1 228 ? 11.591  13.741  9.786   1.00 22.89  ? 237  PHE C CD2 1 
ATOM   8085  C CE1 . PHE C 1 228 ? 10.343  14.814  11.971  1.00 22.86  ? 237  PHE C CE1 1 
ATOM   8086  C CE2 . PHE C 1 228 ? 10.370  14.348  9.650   1.00 22.93  ? 237  PHE C CE2 1 
ATOM   8087  C CZ  . PHE C 1 228 ? 9.746   14.890  10.746  1.00 22.89  ? 237  PHE C CZ  1 
ATOM   8088  N N   . SER C 1 229 ? 15.853  10.976  10.888  1.00 21.70  ? 238  SER C N   1 
ATOM   8089  C CA  . SER C 1 229 ? 17.181  10.531  10.526  1.00 22.24  ? 238  SER C CA  1 
ATOM   8090  C C   . SER C 1 229 ? 17.202  9.388   9.516   1.00 23.00  ? 238  SER C C   1 
ATOM   8091  O O   . SER C 1 229 ? 18.111  9.253   8.703   1.00 24.04  ? 238  SER C O   1 
ATOM   8092  C CB  . SER C 1 229 ? 17.888  10.062  11.781  1.00 22.56  ? 238  SER C CB  1 
ATOM   8093  O OG  . SER C 1 229 ? 18.226  11.162  12.605  1.00 23.16  ? 238  SER C OG  1 
ATOM   8094  N N   . VAL C 1 230 ? 16.200  8.546   9.556   1.00 22.95  ? 239  VAL C N   1 
ATOM   8095  C CA  . VAL C 1 230 ? 16.190  7.415   8.667   1.00 23.87  ? 239  VAL C CA  1 
ATOM   8096  C C   . VAL C 1 230 ? 15.593  7.762   7.336   1.00 24.20  ? 239  VAL C C   1 
ATOM   8097  O O   . VAL C 1 230 ? 15.771  7.029   6.355   1.00 25.63  ? 239  VAL C O   1 
ATOM   8098  C CB  . VAL C 1 230 ? 15.359  6.319   9.243   1.00 23.74  ? 239  VAL C CB  1 
ATOM   8099  C CG1 . VAL C 1 230 ? 15.657  4.992   8.537   1.00 25.62  ? 239  VAL C CG1 1 
ATOM   8100  C CG2 . VAL C 1 230 ? 15.672  6.222   10.686  1.00 24.09  ? 239  VAL C CG2 1 
ATOM   8101  N N   . ASN C 1 231 ? 14.871  8.867   7.288   1.00 23.31  ? 240  ASN C N   1 
ATOM   8102  C CA  . ASN C 1 231 ? 14.154  9.179   6.088   1.00 23.18  ? 240  ASN C CA  1 
ATOM   8103  C C   . ASN C 1 231 ? 14.507  10.498  5.519   1.00 22.34  ? 240  ASN C C   1 
ATOM   8104  O O   . ASN C 1 231 ? 13.768  11.072  4.745   1.00 21.93  ? 240  ASN C O   1 
ATOM   8105  C CB  . ASN C 1 231 ? 12.704  9.134   6.405   1.00 23.14  ? 240  ASN C CB  1 
ATOM   8106  C CG  . ASN C 1 231 ? 12.238  7.755   6.640   1.00 25.10  ? 240  ASN C CG  1 
ATOM   8107  O OD1 . ASN C 1 231 ? 12.057  7.008   5.699   1.00 27.50  ? 240  ASN C OD1 1 
ATOM   8108  N ND2 . ASN C 1 231 ? 12.041  7.390   7.897   1.00 27.42  ? 240  ASN C ND2 1 
ATOM   8109  N N   . ALA C 1 232 ? 15.643  11.002  5.926   1.00 22.14  ? 241  ALA C N   1 
ATOM   8110  C CA  . ALA C 1 232 ? 16.047  12.259  5.423   1.00 22.20  ? 241  ALA C CA  1 
ATOM   8111  C C   . ALA C 1 232 ? 14.946  13.297  5.582   1.00 21.63  ? 241  ALA C C   1 
ATOM   8112  O O   . ALA C 1 232 ? 14.622  14.032  4.651   1.00 21.82  ? 241  ALA C O   1 
ATOM   8113  C CB  . ALA C 1 232 ? 16.348  12.090  4.013   1.00 23.21  ? 241  ALA C CB  1 
ATOM   8114  N N   . GLY C 1 233 ? 14.350  13.328  6.760   1.00 21.23  ? 242  GLY C N   1 
ATOM   8115  C CA  . GLY C 1 233 ? 13.417  14.371  7.117   1.00 20.54  ? 242  GLY C CA  1 
ATOM   8116  C C   . GLY C 1 233 ? 12.058  14.393  6.461   1.00 20.22  ? 242  GLY C C   1 
ATOM   8117  O O   . GLY C 1 233 ? 11.477  15.459  6.382   1.00 20.39  ? 242  GLY C O   1 
ATOM   8118  N N   . VAL C 1 234 ? 11.546  13.261  5.986   1.00 20.24  ? 243  VAL C N   1 
ATOM   8119  C CA  . VAL C 1 234 ? 10.178  13.212  5.475   1.00 20.23  ? 243  VAL C CA  1 
ATOM   8120  C C   . VAL C 1 234 ? 9.671   11.831  5.525   1.00 21.14  ? 243  VAL C C   1 
ATOM   8121  O O   . VAL C 1 234 ? 10.335  10.969  5.004   1.00 22.35  ? 243  VAL C O   1 
ATOM   8122  C CB  . VAL C 1 234 ? 10.104  13.496  4.012   1.00 20.09  ? 243  VAL C CB  1 
ATOM   8123  C CG1 . VAL C 1 234 ? 8.870   14.195  3.755   1.00 19.73  ? 243  VAL C CG1 1 
ATOM   8124  C CG2 . VAL C 1 234 ? 11.248  14.338  3.577   1.00 20.73  ? 243  VAL C CG2 1 
ATOM   8125  N N   . THR C 1 235 ? 8.485   11.593  6.069   1.00 21.31  ? 244  THR C N   1 
ATOM   8126  C CA  . THR C 1 235 ? 8.003   10.224  6.151   1.00 22.72  ? 244  THR C CA  1 
ATOM   8127  C C   . THR C 1 235 ? 6.619   10.089  5.610   1.00 22.95  ? 244  THR C C   1 
ATOM   8128  O O   . THR C 1 235 ? 5.858   11.044  5.671   1.00 22.49  ? 244  THR C O   1 
ATOM   8129  C CB  . THR C 1 235 ? 7.843   9.797   7.583   1.00 23.31  ? 244  THR C CB  1 
ATOM   8130  O OG1 . THR C 1 235 ? 8.144   10.905  8.432   1.00 23.25  ? 244  THR C OG1 1 
ATOM   8131  C CG2 . THR C 1 235 ? 8.702   8.495   7.911   1.00 25.22  ? 244  THR C CG2 1 
ATOM   8132  N N   . THR C 1 236 ? 6.303   8.891   5.100   1.00 23.87  ? 245  THR C N   1 
ATOM   8133  C CA  . THR C 1 236 ? 4.929   8.430   4.931   1.00 24.67  ? 245  THR C CA  1 
ATOM   8134  C C   . THR C 1 236 ? 4.729   7.180   5.723   1.00 25.39  ? 245  THR C C   1 
ATOM   8135  O O   . THR C 1 236 ? 5.669   6.404   5.911   1.00 25.85  ? 245  THR C O   1 
ATOM   8136  C CB  . THR C 1 236 ? 4.507   8.328   3.491   1.00 25.53  ? 245  THR C CB  1 
ATOM   8137  O OG1 . THR C 1 236 ? 4.347   9.669   3.033   1.00 26.91  ? 245  THR C OG1 1 
ATOM   8138  C CG2 . THR C 1 236 ? 3.148   7.647   3.317   1.00 26.71  ? 245  THR C CG2 1 
ATOM   8139  N N   . PRO C 1 237 ? 3.457   6.910   6.028   1.00 25.97  ? 246  PRO C N   1 
ATOM   8140  C CA  . PRO C 1 237 ? 2.676   6.848   7.213   1.00 25.35  ? 246  PRO C CA  1 
ATOM   8141  C C   . PRO C 1 237 ? 3.138   7.902   8.119   1.00 23.69  ? 246  PRO C C   1 
ATOM   8142  O O   . PRO C 1 237 ? 4.333   8.104   8.317   1.00 23.52  ? 246  PRO C O   1 
ATOM   8143  C CB  . PRO C 1 237 ? 2.984   5.469   7.762   1.00 26.51  ? 246  PRO C CB  1 
ATOM   8144  C CG  . PRO C 1 237 ? 3.159   4.635   6.567   1.00 28.62  ? 246  PRO C CG  1 
ATOM   8145  C CD  . PRO C 1 237 ? 3.293   5.612   5.362   1.00 28.24  ? 246  PRO C CD  1 
ATOM   8146  N N   . VAL C 1 238 ? 2.182   8.605   8.660   1.00 22.69  ? 247  VAL C N   1 
ATOM   8147  C CA  . VAL C 1 238 ? 2.480   9.492   9.713   1.00 21.54  ? 247  VAL C CA  1 
ATOM   8148  C C   . VAL C 1 238 ? 2.371   8.650   10.967  1.00 22.10  ? 247  VAL C C   1 
ATOM   8149  O O   . VAL C 1 238 ? 1.297   8.283   11.376  1.00 22.64  ? 247  VAL C O   1 
ATOM   8150  C CB  . VAL C 1 238 ? 1.514   10.624  9.684   1.00 21.01  ? 247  VAL C CB  1 
ATOM   8151  C CG1 . VAL C 1 238 ? 1.704   11.522  10.874  1.00 21.10  ? 247  VAL C CG1 1 
ATOM   8152  C CG2 . VAL C 1 238 ? 1.702   11.391  8.416   1.00 20.31  ? 247  VAL C CG2 1 
ATOM   8153  N N   . SER C 1 239 ? 3.508   8.308   11.557  1.00 22.13  ? 248  SER C N   1 
ATOM   8154  C CA  . SER C 1 239 ? 3.534   7.396   12.683  1.00 22.88  ? 248  SER C CA  1 
ATOM   8155  C C   . SER C 1 239 ? 2.684   7.887   13.850  1.00 23.02  ? 248  SER C C   1 
ATOM   8156  O O   . SER C 1 239 ? 2.369   9.053   13.995  1.00 22.17  ? 248  SER C O   1 
ATOM   8157  C CB  . SER C 1 239 ? 4.967   7.193   13.156  1.00 22.58  ? 248  SER C CB  1 
ATOM   8158  O OG  . SER C 1 239 ? 5.416   8.327   13.880  1.00 21.93  ? 248  SER C OG  1 
ATOM   8159  N N   . THR C 1 240 ? 2.338   6.967   14.710  1.00 24.10  ? 249  THR C N   1 
ATOM   8160  C CA  . THR C 1 240 ? 1.661   7.351   15.886  1.00 24.53  ? 249  THR C CA  1 
ATOM   8161  C C   . THR C 1 240 ? 2.590   8.197   16.741  1.00 23.72  ? 249  THR C C   1 
ATOM   8162  O O   . THR C 1 240 ? 2.164   8.772   17.715  1.00 24.11  ? 249  THR C O   1 
ATOM   8163  C CB  . THR C 1 240 ? 1.152   6.123   16.646  1.00 25.78  ? 249  THR C CB  1 
ATOM   8164  O OG1 . THR C 1 240 ? 2.196   5.527   17.412  1.00 26.84  ? 249  THR C OG1 1 
ATOM   8165  C CG2 . THR C 1 240 ? 0.711   5.119   15.689  1.00 27.03  ? 249  THR C CG2 1 
ATOM   8166  N N   . TYR C 1 241 ? 3.865   8.288   16.407  1.00 23.01  ? 250  TYR C N   1 
ATOM   8167  C CA  . TYR C 1 241 ? 4.729   9.113   17.222  1.00 22.21  ? 250  TYR C CA  1 
ATOM   8168  C C   . TYR C 1 241 ? 4.710   10.523  16.692  1.00 21.42  ? 250  TYR C C   1 
ATOM   8169  O O   . TYR C 1 241 ? 4.895   11.472  17.445  1.00 20.82  ? 250  TYR C O   1 
ATOM   8170  C CB  . TYR C 1 241 ? 6.147   8.624   17.211  1.00 22.24  ? 250  TYR C CB  1 
ATOM   8171  C CG  . TYR C 1 241 ? 6.383   7.229   17.652  1.00 24.45  ? 250  TYR C CG  1 
ATOM   8172  C CD1 . TYR C 1 241 ? 7.031   6.345   16.820  1.00 27.30  ? 250  TYR C CD1 1 
ATOM   8173  C CD2 . TYR C 1 241 ? 6.011   6.794   18.899  1.00 28.05  ? 250  TYR C CD2 1 
ATOM   8174  C CE1 . TYR C 1 241 ? 7.299   5.040   17.198  1.00 30.09  ? 250  TYR C CE1 1 
ATOM   8175  C CE2 . TYR C 1 241 ? 6.274   5.481   19.311  1.00 31.30  ? 250  TYR C CE2 1 
ATOM   8176  C CZ  . TYR C 1 241 ? 6.926   4.611   18.443  1.00 31.68  ? 250  TYR C CZ  1 
ATOM   8177  O OH  . TYR C 1 241 ? 7.222   3.309   18.791  1.00 33.43  ? 250  TYR C OH  1 
ATOM   8178  N N   . MET C 1 242 ? 4.518   10.670  15.388  1.00 21.37  ? 251  MET C N   1 
ATOM   8179  C CA  . MET C 1 242 ? 4.395   11.995  14.831  1.00 21.06  ? 251  MET C CA  1 
ATOM   8180  C C   . MET C 1 242 ? 3.045   12.567  15.251  1.00 21.80  ? 251  MET C C   1 
ATOM   8181  O O   . MET C 1 242 ? 2.962   13.701  15.690  1.00 21.77  ? 251  MET C O   1 
ATOM   8182  C CB  . MET C 1 242 ? 4.468   11.963  13.320  1.00 21.01  ? 251  MET C CB  1 
ATOM   8183  C CG  . MET C 1 242 ? 5.724   11.399  12.734  1.00 21.08  ? 251  MET C CG  1 
ATOM   8184  S SD  . MET C 1 242 ? 7.024   12.595  12.818  1.00 20.27  ? 251  MET C SD  1 
ATOM   8185  C CE  . MET C 1 242 ? 8.167   11.941  11.633  1.00 19.78  ? 251  MET C CE  1 
ATOM   8186  N N   . LEU C 1 243 ? 1.990   11.768  15.134  1.00 22.92  ? 252  LEU C N   1 
ATOM   8187  C CA  . LEU C 1 243 ? 0.632   12.192  15.511  1.00 23.74  ? 252  LEU C CA  1 
ATOM   8188  C C   . LEU C 1 243 ? -0.048  11.162  16.325  1.00 24.98  ? 252  LEU C C   1 
ATOM   8189  O O   . LEU C 1 243 ? -0.158  10.023  15.882  1.00 25.91  ? 252  LEU C O   1 
ATOM   8190  C CB  . LEU C 1 243 ? -0.273  12.304  14.295  1.00 24.07  ? 252  LEU C CB  1 
ATOM   8191  C CG  . LEU C 1 243 ? -0.634  13.703  13.892  1.00 23.78  ? 252  LEU C CG  1 
ATOM   8192  C CD1 . LEU C 1 243 ? -1.954  13.640  13.245  1.00 24.45  ? 252  LEU C CD1 1 
ATOM   8193  C CD2 . LEU C 1 243 ? -0.723  14.522  15.122  1.00 25.00  ? 252  LEU C CD2 1 
ATOM   8194  N N   . THR C 1 244 ? -0.569  11.571  17.470  1.00 25.44  ? 253  THR C N   1 
ATOM   8195  C CA  . THR C 1 244 ? -1.356  10.700  18.313  1.00 26.73  ? 253  THR C CA  1 
ATOM   8196  C C   . THR C 1 244 ? -2.694  10.639  17.725  1.00 27.80  ? 253  THR C C   1 
ATOM   8197  O O   . THR C 1 244 ? -3.057  11.524  16.989  1.00 28.19  ? 253  THR C O   1 
ATOM   8198  C CB  . THR C 1 244 ? -1.552  11.339  19.605  1.00 26.96  ? 253  THR C CB  1 
ATOM   8199  O OG1 . THR C 1 244 ? -0.264  11.567  20.146  1.00 27.00  ? 253  THR C OG1 1 
ATOM   8200  C CG2 . THR C 1 244 ? -2.363  10.455  20.538  1.00 28.77  ? 253  THR C CG2 1 
ATOM   8201  N N   . ASN C 1 245 ? -3.440  9.601   18.051  1.00 29.24  ? 254  ASN C N   1 
ATOM   8202  C CA  . ASN C 1 245 ? -4.817  9.497   17.622  1.00 30.60  ? 254  ASN C CA  1 
ATOM   8203  C C   . ASN C 1 245 ? -5.595  10.677  18.156  1.00 30.57  ? 254  ASN C C   1 
ATOM   8204  O O   . ASN C 1 245 ? -6.265  11.350  17.424  1.00 30.11  ? 254  ASN C O   1 
ATOM   8205  C CB  . ASN C 1 245 ? -5.376  8.183   18.118  1.00 32.49  ? 254  ASN C CB  1 
ATOM   8206  C CG  . ASN C 1 245 ? -6.815  7.966   17.728  1.00 34.35  ? 254  ASN C CG  1 
ATOM   8207  O OD1 . ASN C 1 245 ? -7.128  7.609   16.592  1.00 35.64  ? 254  ASN C OD1 1 
ATOM   8208  N ND2 . ASN C 1 245 ? -7.697  8.118   18.691  1.00 35.22  ? 254  ASN C ND2 1 
ATOM   8209  N N   . SER C 1 246 ? -5.427  10.958  19.434  1.00 31.30  ? 255  SER C N   1 
ATOM   8210  C CA  . SER C 1 246 ? -6.017  12.146  20.053  1.00 32.30  ? 255  SER C CA  1 
ATOM   8211  C C   . SER C 1 246 ? -5.787  13.315  19.126  1.00 30.79  ? 255  SER C C   1 
ATOM   8212  O O   . SER C 1 246 ? -6.716  13.968  18.685  1.00 31.75  ? 255  SER C O   1 
ATOM   8213  C CB  . SER C 1 246 ? -5.404  12.490  21.439  1.00 32.48  ? 255  SER C CB  1 
ATOM   8214  O OG  . SER C 1 246 ? -4.859  11.366  22.134  1.00 35.45  ? 255  SER C OG  1 
ATOM   8215  N N   . GLU C 1 247 ? -4.533  13.565  18.806  1.00 29.01  ? 256  GLU C N   1 
ATOM   8216  C CA  . GLU C 1 247 ? -4.190  14.723  18.004  1.00 27.87  ? 256  GLU C CA  1 
ATOM   8217  C C   . GLU C 1 247 ? -4.835  14.645  16.625  1.00 27.52  ? 256  GLU C C   1 
ATOM   8218  O O   . GLU C 1 247 ? -5.572  15.535  16.226  1.00 27.84  ? 256  GLU C O   1 
ATOM   8219  C CB  . GLU C 1 247 ? -2.690  14.888  17.936  1.00 26.37  ? 256  GLU C CB  1 
ATOM   8220  C CG  . GLU C 1 247 ? -2.094  15.096  19.296  1.00 28.30  ? 256  GLU C CG  1 
ATOM   8221  C CD  . GLU C 1 247 ? -0.578  14.899  19.375  1.00 29.59  ? 256  GLU C CD  1 
ATOM   8222  O OE1 . GLU C 1 247 ? 0.023   14.220  18.500  1.00 31.07  ? 256  GLU C OE1 1 
ATOM   8223  O OE2 . GLU C 1 247 ? 0.013   15.434  20.343  1.00 28.97  ? 256  GLU C OE2 1 
ATOM   8224  N N   . LEU C 1 248 ? -4.614  13.539  15.936  1.00 27.10  ? 257  LEU C N   1 
ATOM   8225  C CA  . LEU C 1 248 ? -5.128  13.357  14.601  1.00 26.54  ? 257  LEU C CA  1 
ATOM   8226  C C   . LEU C 1 248 ? -6.565  13.632  14.632  1.00 27.99  ? 257  LEU C C   1 
ATOM   8227  O O   . LEU C 1 248 ? -7.080  14.319  13.766  1.00 28.07  ? 257  LEU C O   1 
ATOM   8228  C CB  . LEU C 1 248 ? -4.922  11.931  14.101  1.00 26.34  ? 257  LEU C CB  1 
ATOM   8229  C CG  . LEU C 1 248 ? -5.589  11.567  12.776  1.00 24.44  ? 257  LEU C CG  1 
ATOM   8230  C CD1 . LEU C 1 248 ? -5.152  12.412  11.658  1.00 21.41  ? 257  LEU C CD1 1 
ATOM   8231  C CD2 . LEU C 1 248 ? -5.276  10.196  12.414  1.00 23.20  ? 257  LEU C CD2 1 
ATOM   8232  N N   . LEU C 1 249 ? -7.219  13.098  15.650  1.00 29.54  ? 258  LEU C N   1 
ATOM   8233  C CA  . LEU C 1 249 ? -8.663  13.191  15.714  1.00 31.42  ? 258  LEU C CA  1 
ATOM   8234  C C   . LEU C 1 249 ? -9.092  14.625  15.782  1.00 31.75  ? 258  LEU C C   1 
ATOM   8235  O O   . LEU C 1 249 ? -9.927  15.054  15.000  1.00 32.23  ? 258  LEU C O   1 
ATOM   8236  C CB  . LEU C 1 249 ? -9.255  12.359  16.847  1.00 32.70  ? 258  LEU C CB  1 
ATOM   8237  C CG  . LEU C 1 249 ? -9.670  11.017  16.234  1.00 34.14  ? 258  LEU C CG  1 
ATOM   8238  C CD1 . LEU C 1 249 ? -9.701  9.890   17.212  1.00 36.23  ? 258  LEU C CD1 1 
ATOM   8239  C CD2 . LEU C 1 249 ? -11.031 11.128  15.573  1.00 37.55  ? 258  LEU C CD2 1 
ATOM   8240  N N   . SER C 1 250 ? -8.473  15.394  16.664  1.00 31.72  ? 259  SER C N   1 
ATOM   8241  C CA  . SER C 1 250 ? -8.893  16.772  16.807  1.00 32.35  ? 259  SER C CA  1 
ATOM   8242  C C   . SER C 1 250 ? -8.445  17.595  15.608  1.00 31.05  ? 259  SER C C   1 
ATOM   8243  O O   . SER C 1 250 ? -9.083  18.559  15.216  1.00 31.63  ? 259  SER C O   1 
ATOM   8244  C CB  . SER C 1 250 ? -8.392  17.360  18.112  1.00 32.48  ? 259  SER C CB  1 
ATOM   8245  O OG  . SER C 1 250 ? -7.080  17.802  17.952  1.00 30.54  ? 259  SER C OG  1 
ATOM   8246  N N   . LEU C 1 251 ? -7.343  17.198  15.016  1.00 29.52  ? 260  LEU C N   1 
ATOM   8247  C CA  . LEU C 1 251 ? -6.895  17.853  13.820  1.00 28.35  ? 260  LEU C CA  1 
ATOM   8248  C C   . LEU C 1 251 ? -7.904  17.718  12.738  1.00 28.96  ? 260  LEU C C   1 
ATOM   8249  O O   . LEU C 1 251 ? -8.207  18.670  12.045  1.00 28.78  ? 260  LEU C O   1 
ATOM   8250  C CB  . LEU C 1 251 ? -5.621  17.227  13.335  1.00 27.01  ? 260  LEU C CB  1 
ATOM   8251  C CG  . LEU C 1 251 ? -4.427  18.073  13.673  1.00 26.38  ? 260  LEU C CG  1 
ATOM   8252  C CD1 . LEU C 1 251 ? -3.256  17.458  12.946  1.00 26.28  ? 260  LEU C CD1 1 
ATOM   8253  C CD2 . LEU C 1 251 ? -4.648  19.520  13.256  1.00 25.68  ? 260  LEU C CD2 1 
ATOM   8254  N N   . ILE C 1 252 ? -8.405  16.506  12.578  1.00 30.02  ? 261  ILE C N   1 
ATOM   8255  C CA  . ILE C 1 252 ? -9.392  16.238  11.564  1.00 31.21  ? 261  ILE C CA  1 
ATOM   8256  C C   . ILE C 1 252 ? -10.505 17.176  11.844  1.00 33.06  ? 261  ILE C C   1 
ATOM   8257  O O   . ILE C 1 252 ? -10.900 17.944  10.997  1.00 33.30  ? 261  ILE C O   1 
ATOM   8258  C CB  . ILE C 1 252 ? -9.894  14.831  11.667  1.00 31.79  ? 261  ILE C CB  1 
ATOM   8259  C CG1 . ILE C 1 252 ? -8.960  13.930  10.893  1.00 31.08  ? 261  ILE C CG1 1 
ATOM   8260  C CG2 . ILE C 1 252 ? -11.276 14.707  11.098  1.00 32.42  ? 261  ILE C CG2 1 
ATOM   8261  C CD1 . ILE C 1 252 ? -8.833  12.608  11.494  1.00 32.15  ? 261  ILE C CD1 1 
ATOM   8262  N N   . ASN C 1 253 ? -10.968 17.146  13.077  1.00 35.06  ? 262  ASN C N   1 
ATOM   8263  C CA  . ASN C 1 253 ? -12.041 17.997  13.514  1.00 37.14  ? 262  ASN C CA  1 
ATOM   8264  C C   . ASN C 1 253 ? -11.899 19.435  13.038  1.00 37.04  ? 262  ASN C C   1 
ATOM   8265  O O   . ASN C 1 253 ? -12.871 20.060  12.687  1.00 38.39  ? 262  ASN C O   1 
ATOM   8266  C CB  . ASN C 1 253 ? -12.057 17.980  15.012  1.00 38.03  ? 262  ASN C CB  1 
ATOM   8267  C CG  . ASN C 1 253 ? -13.407 18.121  15.555  1.00 40.93  ? 262  ASN C CG  1 
ATOM   8268  O OD1 . ASN C 1 253 ? -14.393 18.177  14.803  1.00 42.30  ? 262  ASN C OD1 1 
ATOM   8269  N ND2 . ASN C 1 253 ? -13.495 18.162  16.903  1.00 44.35  ? 262  ASN C ND2 1 
ATOM   8270  N N   . ASP C 1 254 ? -10.681 19.949  13.007  1.00 36.17  ? 263  ASP C N   1 
ATOM   8271  C CA  . ASP C 1 254 ? -10.458 21.331  12.640  1.00 36.21  ? 263  ASP C CA  1 
ATOM   8272  C C   . ASP C 1 254 ? -10.427 21.546  11.137  1.00 35.52  ? 263  ASP C C   1 
ATOM   8273  O O   . ASP C 1 254 ? -10.396 22.669  10.663  1.00 35.53  ? 263  ASP C O   1 
ATOM   8274  C CB  . ASP C 1 254 ? -9.150  21.819  13.246  1.00 35.79  ? 263  ASP C CB  1 
ATOM   8275  C CG  . ASP C 1 254 ? -8.748  23.204  12.742  1.00 36.74  ? 263  ASP C CG  1 
ATOM   8276  O OD1 . ASP C 1 254 ? -9.552  24.134  12.918  1.00 40.85  ? 263  ASP C OD1 1 
ATOM   8277  O OD2 . ASP C 1 254 ? -7.648  23.381  12.168  1.00 36.21  ? 263  ASP C OD2 1 
ATOM   8278  N N   . MET C 1 255 ? -10.431 20.476  10.370  1.00 35.23  ? 264  MET C N   1 
ATOM   8279  C CA  . MET C 1 255 ? -10.352 20.629  8.923   1.00 34.88  ? 264  MET C CA  1 
ATOM   8280  C C   . MET C 1 255 ? -11.629 21.236  8.343   1.00 36.07  ? 264  MET C C   1 
ATOM   8281  O O   . MET C 1 255 ? -12.716 20.932  8.813   1.00 37.51  ? 264  MET C O   1 
ATOM   8282  C CB  . MET C 1 255 ? -10.019 19.293  8.253   1.00 34.41  ? 264  MET C CB  1 
ATOM   8283  C CG  . MET C 1 255 ? -8.797  18.599  8.842   1.00 33.68  ? 264  MET C CG  1 
ATOM   8284  S SD  . MET C 1 255 ? -8.396  17.106  7.952   1.00 32.64  ? 264  MET C SD  1 
ATOM   8285  C CE  . MET C 1 255 ? -9.992  16.661  7.357   1.00 35.94  ? 264  MET C CE  1 
ATOM   8286  N N   . PRO C 1 256 ? -11.501 22.097  7.325   1.00 35.81  ? 265  PRO C N   1 
ATOM   8287  C CA  . PRO C 1 256 ? -12.625 22.746  6.670   1.00 37.12  ? 265  PRO C CA  1 
ATOM   8288  C C   . PRO C 1 256 ? -13.414 21.832  5.751   1.00 37.70  ? 265  PRO C C   1 
ATOM   8289  O O   . PRO C 1 256 ? -13.479 22.090  4.558   1.00 37.53  ? 265  PRO C O   1 
ATOM   8290  C CB  . PRO C 1 256 ? -11.949 23.834  5.838   1.00 36.35  ? 265  PRO C CB  1 
ATOM   8291  C CG  . PRO C 1 256 ? -10.660 23.285  5.571   1.00 34.88  ? 265  PRO C CG  1 
ATOM   8292  C CD  . PRO C 1 256 ? -10.244 22.667  6.854   1.00 34.75  ? 265  PRO C CD  1 
ATOM   8293  N N   . ILE C 1 257 ? -14.036 20.800  6.308   1.00 38.88  ? 266  ILE C N   1 
ATOM   8294  C CA  . ILE C 1 257 ? -14.821 19.852  5.521   1.00 40.14  ? 266  ILE C CA  1 
ATOM   8295  C C   . ILE C 1 257 ? -16.206 19.611  6.116   1.00 42.38  ? 266  ILE C C   1 
ATOM   8296  O O   . ILE C 1 257 ? -16.491 20.020  7.266   1.00 43.35  ? 266  ILE C O   1 
ATOM   8297  C CB  . ILE C 1 257 ? -14.103 18.490  5.377   1.00 39.45  ? 266  ILE C CB  1 
ATOM   8298  C CG1 . ILE C 1 257 ? -13.621 17.980  6.731   1.00 39.11  ? 266  ILE C CG1 1 
ATOM   8299  C CG2 . ILE C 1 257 ? -12.936 18.590  4.399   1.00 38.45  ? 266  ILE C CG2 1 
ATOM   8300  C CD1 . ILE C 1 257 ? -13.387 16.506  6.759   1.00 39.04  ? 266  ILE C CD1 1 
ATOM   8301  N N   . THR C 1 258 ? -17.060 18.932  5.344   1.00 43.31  ? 267  THR C N   1 
ATOM   8302  C CA  . THR C 1 258 ? -18.381 18.542  5.827   1.00 45.22  ? 267  THR C CA  1 
ATOM   8303  C C   . THR C 1 258 ? -18.287 17.582  7.029   1.00 45.61  ? 267  THR C C   1 
ATOM   8304  O O   . THR C 1 258 ? -17.244 17.008  7.322   1.00 44.31  ? 267  THR C O   1 
ATOM   8305  C CB  . THR C 1 258 ? -19.237 17.882  4.729   1.00 46.20  ? 267  THR C CB  1 
ATOM   8306  O OG1 . THR C 1 258 ? -19.423 16.491  5.036   1.00 47.69  ? 267  THR C OG1 1 
ATOM   8307  C CG2 . THR C 1 258 ? -18.611 18.037  3.352   1.00 45.03  ? 267  THR C CG2 1 
ATOM   8308  N N   . ASN C 1 259 ? -19.393 17.397  7.716   1.00 47.41  ? 268  ASN C N   1 
ATOM   8309  C CA  . ASN C 1 259 ? -19.366 16.548  8.869   1.00 48.16  ? 268  ASN C CA  1 
ATOM   8310  C C   . ASN C 1 259 ? -19.213 15.071  8.625   1.00 48.30  ? 268  ASN C C   1 
ATOM   8311  O O   . ASN C 1 259 ? -18.553 14.383  9.408   1.00 47.80  ? 268  ASN C O   1 
ATOM   8312  C CB  . ASN C 1 259 ? -20.588 16.804  9.707   1.00 50.72  ? 268  ASN C CB  1 
ATOM   8313  C CG  . ASN C 1 259 ? -20.324 17.818  10.759  1.00 51.51  ? 268  ASN C CG  1 
ATOM   8314  O OD1 . ASN C 1 259 ? -19.279 18.481  10.732  1.00 51.15  ? 268  ASN C OD1 1 
ATOM   8315  N ND2 . ASN C 1 259 ? -21.250 17.954  11.706  1.00 54.25  ? 268  ASN C ND2 1 
ATOM   8316  N N   . ASP C 1 260 ? -19.848 14.583  7.560   1.00 49.17  ? 269  ASP C N   1 
ATOM   8317  C CA  . ASP C 1 260 ? -19.782 13.172  7.187   1.00 49.63  ? 269  ASP C CA  1 
ATOM   8318  C C   . ASP C 1 260 ? -18.345 12.899  6.843   1.00 46.94  ? 269  ASP C C   1 
ATOM   8319  O O   . ASP C 1 260 ? -17.755 11.884  7.245   1.00 47.08  ? 269  ASP C O   1 
ATOM   8320  C CB  . ASP C 1 260 ? -20.680 12.873  5.984   1.00 51.07  ? 269  ASP C CB  1 
ATOM   8321  C CG  . ASP C 1 260 ? -22.156 12.950  6.324   1.00 55.78  ? 269  ASP C CG  1 
ATOM   8322  O OD1 . ASP C 1 260 ? -22.510 12.768  7.516   1.00 59.65  ? 269  ASP C OD1 1 
ATOM   8323  O OD2 . ASP C 1 260 ? -22.980 13.187  5.410   1.00 59.56  ? 269  ASP C OD2 1 
ATOM   8324  N N   . GLN C 1 261 ? -17.777 13.843  6.119   1.00 44.37  ? 270  GLN C N   1 
ATOM   8325  C CA  . GLN C 1 261 ? -16.421 13.753  5.767   1.00 42.05  ? 270  GLN C CA  1 
ATOM   8326  C C   . GLN C 1 261 ? -15.588 13.518  7.009   1.00 40.74  ? 270  GLN C C   1 
ATOM   8327  O O   . GLN C 1 261 ? -14.846 12.544  7.085   1.00 40.14  ? 270  GLN C O   1 
ATOM   8328  C CB  . GLN C 1 261 ? -16.044 15.040  5.102   1.00 41.18  ? 270  GLN C CB  1 
ATOM   8329  C CG  . GLN C 1 261 ? -15.135 14.790  3.950   1.00 41.69  ? 270  GLN C CG  1 
ATOM   8330  C CD  . GLN C 1 261 ? -15.146 15.881  2.892   1.00 43.62  ? 270  GLN C CD  1 
ATOM   8331  O OE1 . GLN C 1 261 ? -14.089 16.203  2.342   1.00 44.38  ? 270  GLN C OE1 1 
ATOM   8332  N NE2 . GLN C 1 261 ? -16.324 16.437  2.585   1.00 44.81  ? 270  GLN C NE2 1 
ATOM   8333  N N   . LYS C 1 262 ? -15.757 14.379  8.005   1.00 40.09  ? 271  LYS C N   1 
ATOM   8334  C CA  . LYS C 1 262 ? -15.004 14.239  9.228   1.00 38.91  ? 271  LYS C CA  1 
ATOM   8335  C C   . LYS C 1 262 ? -15.192 12.867  9.799   1.00 39.76  ? 271  LYS C C   1 
ATOM   8336  O O   . LYS C 1 262 ? -14.226 12.223  10.181  1.00 39.14  ? 271  LYS C O   1 
ATOM   8337  C CB  . LYS C 1 262 ? -15.376 15.301  10.243  1.00 39.04  ? 271  LYS C CB  1 
ATOM   8338  C CG  . LYS C 1 262 ? -14.916 16.668  9.843   1.00 38.06  ? 271  LYS C CG  1 
ATOM   8339  C CD  . LYS C 1 262 ? -15.021 17.674  10.944  1.00 39.11  ? 271  LYS C CD  1 
ATOM   8340  C CE  . LYS C 1 262 ? -15.366 19.026  10.365  1.00 39.46  ? 271  LYS C CE  1 
ATOM   8341  N NZ  . LYS C 1 262 ? -15.245 20.112  11.365  1.00 39.12  ? 271  LYS C NZ  1 
ATOM   8342  N N   . LYS C 1 263 ? -16.431 12.401  9.818   1.00 41.47  ? 272  LYS C N   1 
ATOM   8343  C CA  . LYS C 1 263 ? -16.745 11.097  10.386  1.00 42.90  ? 272  LYS C CA  1 
ATOM   8344  C C   . LYS C 1 263 ? -16.031 9.975   9.667   1.00 41.65  ? 272  LYS C C   1 
ATOM   8345  O O   . LYS C 1 263 ? -15.553 9.027   10.297  1.00 41.94  ? 272  LYS C O   1 
ATOM   8346  C CB  . LYS C 1 263 ? -18.239 10.856  10.334  1.00 45.68  ? 272  LYS C CB  1 
ATOM   8347  C CG  . LYS C 1 263 ? -18.658 9.453   10.725  1.00 50.24  ? 272  LYS C CG  1 
ATOM   8348  C CD  . LYS C 1 263 ? -20.154 9.243   10.436  1.00 57.66  ? 272  LYS C CD  1 
ATOM   8349  C CE  . LYS C 1 263 ? -20.778 8.037   11.183  1.00 62.07  ? 272  LYS C CE  1 
ATOM   8350  N NZ  . LYS C 1 263 ? -22.273 7.999   11.008  1.00 66.10  ? 272  LYS C NZ  1 
ATOM   8351  N N   . LEU C 1 264 ? -15.970 10.094  8.348   1.00 40.21  ? 273  LEU C N   1 
ATOM   8352  C CA  . LEU C 1 264 ? -15.261 9.141   7.511   1.00 38.80  ? 273  LEU C CA  1 
ATOM   8353  C C   . LEU C 1 264 ? -13.811 9.036   7.889   1.00 36.79  ? 273  LEU C C   1 
ATOM   8354  O O   . LEU C 1 264 ? -13.288 7.959   8.156   1.00 36.98  ? 273  LEU C O   1 
ATOM   8355  C CB  . LEU C 1 264 ? -15.315 9.577   6.064   1.00 38.01  ? 273  LEU C CB  1 
ATOM   8356  C CG  . LEU C 1 264 ? -14.635 8.628   5.101   1.00 35.98  ? 273  LEU C CG  1 
ATOM   8357  C CD1 . LEU C 1 264 ? -15.366 7.314   5.011   1.00 37.60  ? 273  LEU C CD1 1 
ATOM   8358  C CD2 . LEU C 1 264 ? -14.668 9.292   3.795   1.00 34.16  ? 273  LEU C CD2 1 
ATOM   8359  N N   . MET C 1 265 ? -13.150 10.173  7.890   1.00 34.81  ? 274  MET C N   1 
ATOM   8360  C CA  . MET C 1 265 ? -11.754 10.201  8.247   1.00 33.11  ? 274  MET C CA  1 
ATOM   8361  C C   . MET C 1 265 ? -11.527 9.592   9.612   1.00 33.93  ? 274  MET C C   1 
ATOM   8362  O O   . MET C 1 265 ? -10.644 8.761   9.785   1.00 33.83  ? 274  MET C O   1 
ATOM   8363  C CB  . MET C 1 265 ? -11.243 11.616  8.176   1.00 31.11  ? 274  MET C CB  1 
ATOM   8364  C CG  . MET C 1 265 ? -11.151 12.019  6.770   1.00 29.96  ? 274  MET C CG  1 
ATOM   8365  S SD  . MET C 1 265 ? -10.580 13.659  6.579   1.00 27.70  ? 274  MET C SD  1 
ATOM   8366  C CE  . MET C 1 265 ? -8.894  13.456  7.129   1.00 27.73  ? 274  MET C CE  1 
ATOM   8367  N N   . SER C 1 266 ? -12.361 9.961   10.573  1.00 35.36  ? 275  SER C N   1 
ATOM   8368  C CA  . SER C 1 266 ? -12.225 9.446   11.927  1.00 36.28  ? 275  SER C CA  1 
ATOM   8369  C C   . SER C 1 266 ? -12.380 7.941   12.010  1.00 38.16  ? 275  SER C C   1 
ATOM   8370  O O   . SER C 1 266 ? -11.706 7.279   12.788  1.00 38.09  ? 275  SER C O   1 
ATOM   8371  C CB  . SER C 1 266 ? -13.228 10.119  12.824  1.00 37.25  ? 275  SER C CB  1 
ATOM   8372  O OG  . SER C 1 266 ? -13.116 11.510  12.629  1.00 36.05  ? 275  SER C OG  1 
ATOM   8373  N N   . ASN C 1 267 ? -13.258 7.379   11.196  1.00 40.25  ? 276  ASN C N   1 
ATOM   8374  C CA  . ASN C 1 267 ? -13.406 5.936   11.225  1.00 42.48  ? 276  ASN C CA  1 
ATOM   8375  C C   . ASN C 1 267 ? -12.412 5.197   10.375  1.00 41.75  ? 276  ASN C C   1 
ATOM   8376  O O   . ASN C 1 267 ? -12.639 4.036   10.079  1.00 43.42  ? 276  ASN C O   1 
ATOM   8377  C CB  . ASN C 1 267 ? -14.832 5.516   10.864  1.00 44.91  ? 276  ASN C CB  1 
ATOM   8378  C CG  . ASN C 1 267 ? -15.800 5.755   12.000  1.00 48.25  ? 276  ASN C CG  1 
ATOM   8379  O OD1 . ASN C 1 267 ? -15.487 5.503   13.177  1.00 51.02  ? 276  ASN C OD1 1 
ATOM   8380  N ND2 . ASN C 1 267 ? -16.980 6.251   11.667  1.00 50.97  ? 276  ASN C ND2 1 
ATOM   8381  N N   . ASN C 1 268 ? -11.311 5.848   9.997   1.00 39.84  ? 277  ASN C N   1 
ATOM   8382  C CA  . ASN C 1 268 ? -10.398 5.263   9.033   1.00 39.07  ? 277  ASN C CA  1 
ATOM   8383  C C   . ASN C 1 268 ? -8.977  5.664   9.182   1.00 37.36  ? 277  ASN C C   1 
ATOM   8384  O O   . ASN C 1 268 ? -8.202  5.504   8.240   1.00 37.07  ? 277  ASN C O   1 
ATOM   8385  C CB  . ASN C 1 268 ? -10.835 5.633   7.637   1.00 38.90  ? 277  ASN C CB  1 
ATOM   8386  C CG  . ASN C 1 268 ? -11.891 4.728   7.127   1.00 40.79  ? 277  ASN C CG  1 
ATOM   8387  O OD1 . ASN C 1 268 ? -11.603 3.623   6.696   1.00 42.14  ? 277  ASN C OD1 1 
ATOM   8388  N ND2 . ASN C 1 268 ? -13.131 5.174   7.181   1.00 42.23  ? 277  ASN C ND2 1 
ATOM   8389  N N   . VAL C 1 269 ? -8.638  6.199   10.348  1.00 36.44  ? 278  VAL C N   1 
ATOM   8390  C CA  . VAL C 1 269 ? -7.278  6.654   10.667  1.00 34.65  ? 278  VAL C CA  1 
ATOM   8391  C C   . VAL C 1 269 ? -6.147  5.985   9.909   1.00 33.85  ? 278  VAL C C   1 
ATOM   8392  O O   . VAL C 1 269 ? -5.260  6.649   9.435   1.00 32.69  ? 278  VAL C O   1 
ATOM   8393  C CB  . VAL C 1 269 ? -6.997  6.466   12.145  1.00 34.92  ? 278  VAL C CB  1 
ATOM   8394  C CG1 . VAL C 1 269 ? -7.541  7.616   12.926  1.00 33.88  ? 278  VAL C CG1 1 
ATOM   8395  C CG2 . VAL C 1 269 ? -7.638  5.168   12.636  1.00 38.18  ? 278  VAL C CG2 1 
ATOM   8396  N N   . GLN C 1 270 ? -6.187  4.672   9.787   1.00 34.90  ? 279  GLN C N   1 
ATOM   8397  C CA  . GLN C 1 270 ? -5.114  3.966   9.139   1.00 34.74  ? 279  GLN C CA  1 
ATOM   8398  C C   . GLN C 1 270 ? -4.811  4.495   7.750   1.00 33.26  ? 279  GLN C C   1 
ATOM   8399  O O   . GLN C 1 270 ? -3.724  5.007   7.501   1.00 32.19  ? 279  GLN C O   1 
ATOM   8400  C CB  . GLN C 1 270 ? -5.416  2.498   9.071   1.00 37.20  ? 279  GLN C CB  1 
ATOM   8401  C CG  . GLN C 1 270 ? -4.164  1.675   9.053   1.00 39.76  ? 279  GLN C CG  1 
ATOM   8402  C CD  . GLN C 1 270 ? -4.484  0.213   8.937   1.00 46.19  ? 279  GLN C CD  1 
ATOM   8403  O OE1 . GLN C 1 270 ? -5.415  -0.180  8.193   1.00 49.70  ? 279  GLN C OE1 1 
ATOM   8404  N NE2 . GLN C 1 270 ? -3.733  -0.621  9.675   1.00 47.19  ? 279  GLN C NE2 1 
ATOM   8405  N N   . ILE C 1 271 ? -5.762  4.374   6.843   1.00 33.23  ? 280  ILE C N   1 
ATOM   8406  C CA  . ILE C 1 271 ? -5.625  4.955   5.514   1.00 31.72  ? 280  ILE C CA  1 
ATOM   8407  C C   . ILE C 1 271 ? -5.113  6.403   5.561   1.00 29.58  ? 280  ILE C C   1 
ATOM   8408  O O   . ILE C 1 271 ? -4.078  6.729   4.982   1.00 28.76  ? 280  ILE C O   1 
ATOM   8409  C CB  . ILE C 1 271 ? -6.977  4.940   4.804   1.00 32.86  ? 280  ILE C CB  1 
ATOM   8410  C CG1 . ILE C 1 271 ? -7.582  3.530   4.824   1.00 34.44  ? 280  ILE C CG1 1 
ATOM   8411  C CG2 . ILE C 1 271 ? -6.857  5.514   3.394   1.00 31.76  ? 280  ILE C CG2 1 
ATOM   8412  C CD1 . ILE C 1 271 ? -7.317  2.722   3.558   1.00 34.87  ? 280  ILE C CD1 1 
ATOM   8413  N N   . VAL C 1 272 ? -5.838  7.260   6.267   1.00 28.82  ? 281  VAL C N   1 
ATOM   8414  C CA  . VAL C 1 272 ? -5.455  8.642   6.421   1.00 27.03  ? 281  VAL C CA  1 
ATOM   8415  C C   . VAL C 1 272 ? -3.972  8.726   6.696   1.00 26.33  ? 281  VAL C C   1 
ATOM   8416  O O   . VAL C 1 272 ? -3.239  9.414   5.991   1.00 26.03  ? 281  VAL C O   1 
ATOM   8417  C CB  . VAL C 1 272 ? -6.176  9.259   7.569   1.00 26.68  ? 281  VAL C CB  1 
ATOM   8418  C CG1 . VAL C 1 272 ? -5.904  10.702  7.622   1.00 24.56  ? 281  VAL C CG1 1 
ATOM   8419  C CG2 . VAL C 1 272 ? -7.597  9.053   7.379   1.00 27.70  ? 281  VAL C CG2 1 
ATOM   8420  N N   . ARG C 1 273 ? -3.514  8.007   7.705   1.00 26.39  ? 282  ARG C N   1 
ATOM   8421  C CA  . ARG C 1 273 ? -2.137  8.068   8.033   1.00 25.34  ? 282  ARG C CA  1 
ATOM   8422  C C   . ARG C 1 273 ? -1.360  7.685   6.811   1.00 26.07  ? 282  ARG C C   1 
ATOM   8423  O O   . ARG C 1 273 ? -0.529  8.435   6.369   1.00 25.75  ? 282  ARG C O   1 
ATOM   8424  C CB  . ARG C 1 273 ? -1.832  7.165   9.189   1.00 25.51  ? 282  ARG C CB  1 
ATOM   8425  C CG  . ARG C 1 273 ? -2.493  7.576   10.459  1.00 24.36  ? 282  ARG C CG  1 
ATOM   8426  C CD  . ARG C 1 273 ? -1.740  7.046   11.637  1.00 23.59  ? 282  ARG C CD  1 
ATOM   8427  N NE  . ARG C 1 273 ? -2.406  7.296   12.897  1.00 23.78  ? 282  ARG C NE  1 
ATOM   8428  C CZ  . ARG C 1 273 ? -1.983  8.145   13.839  1.00 24.25  ? 282  ARG C CZ  1 
ATOM   8429  N NH1 . ARG C 1 273 ? -0.862  8.850   13.702  1.00 22.04  ? 282  ARG C NH1 1 
ATOM   8430  N NH2 . ARG C 1 273 ? -2.710  8.269   14.951  1.00 26.51  ? 282  ARG C NH2 1 
ATOM   8431  N N   . GLN C 1 274 ? -1.672  6.561   6.204   1.00 27.67  ? 283  GLN C N   1 
ATOM   8432  C CA  . GLN C 1 274 ? -0.914  6.135   5.051   1.00 28.62  ? 283  GLN C CA  1 
ATOM   8433  C C   . GLN C 1 274 ? -0.929  7.138   3.930   1.00 27.53  ? 283  GLN C C   1 
ATOM   8434  O O   . GLN C 1 274 ? -0.045  7.151   3.080   1.00 27.68  ? 283  GLN C O   1 
ATOM   8435  C CB  . GLN C 1 274 ? -1.419  4.808   4.569   1.00 30.65  ? 283  GLN C CB  1 
ATOM   8436  C CG  . GLN C 1 274 ? -1.221  3.764   5.634   1.00 35.13  ? 283  GLN C CG  1 
ATOM   8437  C CD  . GLN C 1 274 ? -1.900  2.453   5.327   1.00 41.59  ? 283  GLN C CD  1 
ATOM   8438  O OE1 . GLN C 1 274 ? -2.762  2.364   4.450   1.00 45.54  ? 283  GLN C OE1 1 
ATOM   8439  N NE2 . GLN C 1 274 ? -1.517  1.421   6.057   1.00 42.41  ? 283  GLN C NE2 1 
ATOM   8440  N N   . GLN C 1 275 ? -1.902  8.013   3.949   1.00 26.87  ? 284  GLN C N   1 
ATOM   8441  C CA  . GLN C 1 275 ? -1.979  8.991   2.912   1.00 26.28  ? 284  GLN C CA  1 
ATOM   8442  C C   . GLN C 1 275 ? -1.318  10.300  3.281   1.00 24.46  ? 284  GLN C C   1 
ATOM   8443  O O   . GLN C 1 275 ? -1.291  11.217  2.482   1.00 23.64  ? 284  GLN C O   1 
ATOM   8444  C CB  . GLN C 1 275 ? -3.426  9.232   2.580   1.00 27.28  ? 284  GLN C CB  1 
ATOM   8445  C CG  . GLN C 1 275 ? -3.996  8.181   1.675   1.00 30.54  ? 284  GLN C CG  1 
ATOM   8446  C CD  . GLN C 1 275 ? -5.428  8.478   1.307   1.00 33.95  ? 284  GLN C CD  1 
ATOM   8447  O OE1 . GLN C 1 275 ? -6.250  8.827   2.183   1.00 34.75  ? 284  GLN C OE1 1 
ATOM   8448  N NE2 . GLN C 1 275 ? -5.746  8.352   0.002   1.00 34.91  ? 284  GLN C NE2 1 
ATOM   8449  N N   . SER C 1 276 ? -0.776  10.401  4.478   1.00 23.62  ? 285  SER C N   1 
ATOM   8450  C CA  . SER C 1 276 ? -0.236  11.668  4.921   1.00 22.66  ? 285  SER C CA  1 
ATOM   8451  C C   . SER C 1 276 ? 1.275   11.655  4.961   1.00 22.35  ? 285  SER C C   1 
ATOM   8452  O O   . SER C 1 276 ? 1.892   10.593  4.852   1.00 23.11  ? 285  SER C O   1 
ATOM   8453  C CB  . SER C 1 276 ? -0.790  12.005  6.281   1.00 22.57  ? 285  SER C CB  1 
ATOM   8454  O OG  . SER C 1 276 ? -2.191  11.859  6.259   1.00 23.60  ? 285  SER C OG  1 
ATOM   8455  N N   . TYR C 1 277 ? 1.875   12.837  5.089   1.00 21.68  ? 286  TYR C N   1 
ATOM   8456  C CA  . TYR C 1 277 ? 3.335   12.968  5.146   1.00 21.42  ? 286  TYR C CA  1 
ATOM   8457  C C   . TYR C 1 277 ? 3.727   13.739  6.389   1.00 21.13  ? 286  TYR C C   1 
ATOM   8458  O O   . TYR C 1 277 ? 2.935   14.510  6.924   1.00 21.65  ? 286  TYR C O   1 
ATOM   8459  C CB  . TYR C 1 277 ? 3.867   13.725  3.943   1.00 21.04  ? 286  TYR C CB  1 
ATOM   8460  C CG  . TYR C 1 277 ? 3.783   12.992  2.660   1.00 22.31  ? 286  TYR C CG  1 
ATOM   8461  C CD1 . TYR C 1 277 ? 2.580   12.752  2.077   1.00 24.96  ? 286  TYR C CD1 1 
ATOM   8462  C CD2 . TYR C 1 277 ? 4.900   12.581  2.007   1.00 23.91  ? 286  TYR C CD2 1 
ATOM   8463  C CE1 . TYR C 1 277 ? 2.475   12.076  0.883   1.00 27.31  ? 286  TYR C CE1 1 
ATOM   8464  C CE2 . TYR C 1 277 ? 4.812   11.921  0.805   1.00 26.52  ? 286  TYR C CE2 1 
ATOM   8465  C CZ  . TYR C 1 277 ? 3.583   11.661  0.250   1.00 27.39  ? 286  TYR C CZ  1 
ATOM   8466  O OH  . TYR C 1 277 ? 3.407   10.991  -0.946  1.00 30.01  ? 286  TYR C OH  1 
ATOM   8467  N N   . SER C 1 278 ? 4.951   13.548  6.856   1.00 20.83  ? 287  SER C N   1 
ATOM   8468  C CA  . SER C 1 278 ? 5.436   14.378  7.917   1.00 20.34  ? 287  SER C CA  1 
ATOM   8469  C C   . SER C 1 278 ? 6.749   14.956  7.455   1.00 20.30  ? 287  SER C C   1 
ATOM   8470  O O   . SER C 1 278 ? 7.629   14.220  7.060   1.00 20.76  ? 287  SER C O   1 
ATOM   8471  C CB  . SER C 1 278 ? 5.606   13.541  9.156   1.00 20.53  ? 287  SER C CB  1 
ATOM   8472  O OG  . SER C 1 278 ? 6.048   14.350  10.210  1.00 20.59  ? 287  SER C OG  1 
ATOM   8473  N N   . ILE C 1 279 ? 6.860   16.273  7.445   1.00 20.34  ? 288  ILE C N   1 
ATOM   8474  C CA  . ILE C 1 279 ? 8.042   16.928  6.955   1.00 20.97  ? 288  ILE C CA  1 
ATOM   8475  C C   . ILE C 1 279 ? 8.690   17.606  8.120   1.00 21.92  ? 288  ILE C C   1 
ATOM   8476  O O   . ILE C 1 279 ? 8.028   18.314  8.848   1.00 22.79  ? 288  ILE C O   1 
ATOM   8477  C CB  . ILE C 1 279 ? 7.691   18.072  6.095   1.00 20.54  ? 288  ILE C CB  1 
ATOM   8478  C CG1 . ILE C 1 279 ? 6.492   17.749  5.236   1.00 20.21  ? 288  ILE C CG1 1 
ATOM   8479  C CG2 . ILE C 1 279 ? 8.906   18.527  5.363   1.00 21.69  ? 288  ILE C CG2 1 
ATOM   8480  C CD1 . ILE C 1 279 ? 6.781   17.154  3.993   1.00 21.14  ? 288  ILE C CD1 1 
ATOM   8481  N N   . MET C 1 280 ? 9.988   17.439  8.286   1.00 22.93  ? 289  MET C N   1 
ATOM   8482  C CA  . MET C 1 280 ? 10.678  18.005  9.409   1.00 23.54  ? 289  MET C CA  1 
ATOM   8483  C C   . MET C 1 280 ? 10.760  19.457  9.118   1.00 23.99  ? 289  MET C C   1 
ATOM   8484  O O   . MET C 1 280 ? 11.006  19.814  8.002   1.00 24.34  ? 289  MET C O   1 
ATOM   8485  C CB  . MET C 1 280 ? 12.060  17.432  9.413   1.00 24.07  ? 289  MET C CB  1 
ATOM   8486  C CG  . MET C 1 280 ? 12.820  17.680  10.656  1.00 25.22  ? 289  MET C CG  1 
ATOM   8487  S SD  . MET C 1 280 ? 14.506  17.054  10.522  1.00 27.09  ? 289  MET C SD  1 
ATOM   8488  C CE  . MET C 1 280 ? 15.093  17.899  9.055   1.00 28.22  ? 289  MET C CE  1 
ATOM   8489  N N   . SER C 1 281 ? 10.541  20.299  10.103  1.00 24.86  ? 290  SER C N   1 
ATOM   8490  C CA  . SER C 1 281 ? 10.530  21.737  9.850   1.00 26.25  ? 290  SER C CA  1 
ATOM   8491  C C   . SER C 1 281 ? 11.704  22.456  10.473  1.00 26.82  ? 290  SER C C   1 
ATOM   8492  O O   . SER C 1 281 ? 12.494  22.973  9.724   1.00 27.63  ? 290  SER C O   1 
ATOM   8493  C CB  . SER C 1 281 ? 9.208   22.387  10.267  1.00 26.85  ? 290  SER C CB  1 
ATOM   8494  O OG  . SER C 1 281 ? 9.208   23.783  10.013  1.00 28.85  ? 290  SER C OG  1 
ATOM   8495  N N   . ILE C 1 282 ? 11.826  22.520  11.804  1.00 27.05  ? 291  ILE C N   1 
ATOM   8496  C CA  . ILE C 1 282 ? 13.106  22.945  12.383  1.00 27.93  ? 291  ILE C CA  1 
ATOM   8497  C C   . ILE C 1 282 ? 13.502  22.309  13.670  1.00 27.60  ? 291  ILE C C   1 
ATOM   8498  O O   . ILE C 1 282 ? 12.648  22.093  14.525  1.00 26.77  ? 291  ILE C O   1 
ATOM   8499  C CB  . ILE C 1 282 ? 13.232  24.460  12.552  1.00 29.07  ? 291  ILE C CB  1 
ATOM   8500  C CG1 . ILE C 1 282 ? 11.854  25.100  12.678  1.00 28.72  ? 291  ILE C CG1 1 
ATOM   8501  C CG2 . ILE C 1 282 ? 14.171  25.070  11.448  1.00 30.59  ? 291  ILE C CG2 1 
ATOM   8502  C CD1 . ILE C 1 282 ? 11.506  25.315  14.144  1.00 29.30  ? 291  ILE C CD1 1 
ATOM   8503  N N   . ILE C 1 283 ? 14.818  22.039  13.777  1.00 28.28  ? 292  ILE C N   1 
ATOM   8504  C CA  . ILE C 1 283 ? 15.438  21.348  14.938  1.00 28.83  ? 292  ILE C CA  1 
ATOM   8505  C C   . ILE C 1 283 ? 16.403  22.245  15.635  1.00 29.57  ? 292  ILE C C   1 
ATOM   8506  O O   . ILE C 1 283 ? 17.242  22.898  15.013  1.00 29.80  ? 292  ILE C O   1 
ATOM   8507  C CB  . ILE C 1 283 ? 16.276  20.084  14.615  1.00 28.57  ? 292  ILE C CB  1 
ATOM   8508  C CG1 . ILE C 1 283 ? 16.351  19.811  13.128  1.00 30.08  ? 292  ILE C CG1 1 
ATOM   8509  C CG2 . ILE C 1 283 ? 15.806  18.886  15.401  1.00 27.56  ? 292  ILE C CG2 1 
ATOM   8510  C CD1 . ILE C 1 283 ? 15.009  19.797  12.395  1.00 32.20  ? 292  ILE C CD1 1 
ATOM   8511  N N   . LYS C 1 284 ? 16.252  22.257  16.944  1.00 29.92  ? 293  LYS C N   1 
ATOM   8512  C CA  . LYS C 1 284 ? 17.099  22.989  17.808  1.00 31.44  ? 293  LYS C CA  1 
ATOM   8513  C C   . LYS C 1 284 ? 17.303  21.977  18.889  1.00 31.72  ? 293  LYS C C   1 
ATOM   8514  O O   . LYS C 1 284 ? 16.510  21.046  18.998  1.00 31.23  ? 293  LYS C O   1 
ATOM   8515  C CB  . LYS C 1 284 ? 16.373  24.215  18.335  1.00 32.03  ? 293  LYS C CB  1 
ATOM   8516  C CG  . LYS C 1 284 ? 15.857  25.121  17.256  1.00 32.99  ? 293  LYS C CG  1 
ATOM   8517  C CD  . LYS C 1 284 ? 15.758  26.541  17.726  1.00 35.45  ? 293  LYS C CD  1 
ATOM   8518  C CE  . LYS C 1 284 ? 15.373  27.418  16.558  1.00 37.28  ? 293  LYS C CE  1 
ATOM   8519  N NZ  . LYS C 1 284 ? 16.089  28.728  16.639  1.00 40.57  ? 293  LYS C NZ  1 
ATOM   8520  N N   . GLU C 1 285 ? 18.353  22.144  19.686  1.00 33.04  ? 294  GLU C N   1 
ATOM   8521  C CA  . GLU C 1 285 ? 18.677  21.167  20.736  1.00 33.76  ? 294  GLU C CA  1 
ATOM   8522  C C   . GLU C 1 285 ? 17.504  20.843  21.634  1.00 32.41  ? 294  GLU C C   1 
ATOM   8523  O O   . GLU C 1 285 ? 17.351  19.719  22.074  1.00 31.85  ? 294  GLU C O   1 
ATOM   8524  C CB  . GLU C 1 285 ? 19.879  21.626  21.595  1.00 35.59  ? 294  GLU C CB  1 
ATOM   8525  C CG  . GLU C 1 285 ? 21.287  21.526  20.880  1.00 40.26  ? 294  GLU C CG  1 
ATOM   8526  C CD  . GLU C 1 285 ? 22.480  21.961  21.755  1.00 45.03  ? 294  GLU C CD  1 
ATOM   8527  O OE1 . GLU C 1 285 ? 22.690  21.361  22.854  1.00 45.16  ? 294  GLU C OE1 1 
ATOM   8528  O OE2 . GLU C 1 285 ? 23.194  22.907  21.313  1.00 48.05  ? 294  GLU C OE2 1 
ATOM   8529  N N   . GLU C 1 286 ? 16.675  21.839  21.888  1.00 31.97  ? 295  GLU C N   1 
ATOM   8530  C CA  . GLU C 1 286 ? 15.630  21.700  22.882  1.00 31.80  ? 295  GLU C CA  1 
ATOM   8531  C C   . GLU C 1 286 ? 14.232  21.829  22.334  1.00 30.40  ? 295  GLU C C   1 
ATOM   8532  O O   . GLU C 1 286 ? 13.268  21.741  23.084  1.00 30.30  ? 295  GLU C O   1 
ATOM   8533  C CB  . GLU C 1 286 ? 15.833  22.645  24.095  1.00 33.45  ? 295  GLU C CB  1 
ATOM   8534  C CG  . GLU C 1 286 ? 16.688  23.910  23.893  1.00 37.63  ? 295  GLU C CG  1 
ATOM   8535  C CD  . GLU C 1 286 ? 16.255  24.699  22.653  1.00 41.98  ? 295  GLU C CD  1 
ATOM   8536  O OE1 . GLU C 1 286 ? 16.910  24.521  21.582  1.00 42.96  ? 295  GLU C OE1 1 
ATOM   8537  O OE2 . GLU C 1 286 ? 15.247  25.464  22.746  1.00 43.27  ? 295  GLU C OE2 1 
ATOM   8538  N N   . VAL C 1 287 ? 14.114  22.025  21.028  1.00 29.20  ? 296  VAL C N   1 
ATOM   8539  C CA  . VAL C 1 287 ? 12.811  21.993  20.376  1.00 27.87  ? 296  VAL C CA  1 
ATOM   8540  C C   . VAL C 1 287 ? 12.873  21.416  19.004  1.00 26.80  ? 296  VAL C C   1 
ATOM   8541  O O   . VAL C 1 287 ? 13.757  21.770  18.226  1.00 27.19  ? 296  VAL C O   1 
ATOM   8542  C CB  . VAL C 1 287 ? 12.240  23.356  20.135  1.00 28.33  ? 296  VAL C CB  1 
ATOM   8543  C CG1 . VAL C 1 287 ? 10.763  23.198  19.922  1.00 28.25  ? 296  VAL C CG1 1 
ATOM   8544  C CG2 . VAL C 1 287 ? 12.518  24.289  21.302  1.00 30.31  ? 296  VAL C CG2 1 
ATOM   8545  N N   . LEU C 1 288 ? 11.911  20.560  18.695  1.00 25.37  ? 297  LEU C N   1 
ATOM   8546  C CA  . LEU C 1 288 ? 11.789  20.028  17.357  1.00 24.24  ? 297  LEU C CA  1 
ATOM   8547  C C   . LEU C 1 288 ? 10.434  20.396  16.808  1.00 23.53  ? 297  LEU C C   1 
ATOM   8548  O O   . LEU C 1 288 ? 9.466   20.219  17.498  1.00 24.19  ? 297  LEU C O   1 
ATOM   8549  C CB  . LEU C 1 288 ? 11.962  18.511  17.354  1.00 23.68  ? 297  LEU C CB  1 
ATOM   8550  C CG  . LEU C 1 288 ? 11.533  17.835  16.047  1.00 23.54  ? 297  LEU C CG  1 
ATOM   8551  C CD1 . LEU C 1 288 ? 12.345  18.296  14.877  1.00 24.74  ? 297  LEU C CD1 1 
ATOM   8552  C CD2 . LEU C 1 288 ? 11.643  16.370  16.132  1.00 23.26  ? 297  LEU C CD2 1 
ATOM   8553  N N   . ALA C 1 289 ? 10.352  20.906  15.587  1.00 22.25  ? 298  ALA C N   1 
ATOM   8554  C CA  . ALA C 1 289 ? 9.073   21.266  15.043  1.00 21.28  ? 298  ALA C CA  1 
ATOM   8555  C C   . ALA C 1 289 ? 9.048   20.747  13.675  1.00 20.63  ? 298  ALA C C   1 
ATOM   8556  O O   . ALA C 1 289 ? 10.038  20.884  12.988  1.00 21.09  ? 298  ALA C O   1 
ATOM   8557  C CB  . ALA C 1 289 ? 8.933   22.733  14.995  1.00 21.99  ? 298  ALA C CB  1 
ATOM   8558  N N   . TYR C 1 290 ? 7.913   20.186  13.269  1.00 19.82  ? 299  TYR C N   1 
ATOM   8559  C CA  . TYR C 1 290 ? 7.705   19.628  11.935  1.00 18.75  ? 299  TYR C CA  1 
ATOM   8560  C C   . TYR C 1 290 ? 6.282   19.839  11.457  1.00 18.61  ? 299  TYR C C   1 
ATOM   8561  O O   . TYR C 1 290 ? 5.393   20.144  12.241  1.00 19.26  ? 299  TYR C O   1 
ATOM   8562  C CB  . TYR C 1 290 ? 7.999   18.148  11.950  1.00 18.45  ? 299  TYR C CB  1 
ATOM   8563  C CG  . TYR C 1 290 ? 7.245   17.396  13.005  1.00 18.70  ? 299  TYR C CG  1 
ATOM   8564  C CD1 . TYR C 1 290 ? 6.107   16.679  12.687  1.00 18.96  ? 299  TYR C CD1 1 
ATOM   8565  C CD2 . TYR C 1 290 ? 7.680   17.391  14.332  1.00 18.70  ? 299  TYR C CD2 1 
ATOM   8566  C CE1 . TYR C 1 290 ? 5.402   15.969  13.655  1.00 19.03  ? 299  TYR C CE1 1 
ATOM   8567  C CE2 . TYR C 1 290 ? 6.978   16.683  15.319  1.00 18.78  ? 299  TYR C CE2 1 
ATOM   8568  C CZ  . TYR C 1 290 ? 5.828   15.972  14.971  1.00 18.73  ? 299  TYR C CZ  1 
ATOM   8569  O OH  . TYR C 1 290 ? 5.126   15.260  15.933  1.00 17.97  ? 299  TYR C OH  1 
ATOM   8570  N N   . VAL C 1 291 ? 6.060   19.677  10.163  1.00 18.12  ? 300  VAL C N   1 
ATOM   8571  C CA  . VAL C 1 291 ? 4.754   19.892  9.594   1.00 17.94  ? 300  VAL C CA  1 
ATOM   8572  C C   . VAL C 1 291 ? 4.143   18.601  9.143   1.00 18.08  ? 300  VAL C C   1 
ATOM   8573  O O   . VAL C 1 291 ? 4.721   17.856  8.383   1.00 18.25  ? 300  VAL C O   1 
ATOM   8574  C CB  . VAL C 1 291 ? 4.798   20.818  8.432   1.00 17.68  ? 300  VAL C CB  1 
ATOM   8575  C CG1 . VAL C 1 291 ? 3.553   20.699  7.672   1.00 17.97  ? 300  VAL C CG1 1 
ATOM   8576  C CG2 . VAL C 1 291 ? 4.889   22.197  8.916   1.00 18.95  ? 300  VAL C CG2 1 
ATOM   8577  N N   . VAL C 1 292 ? 2.954   18.341  9.644   1.00 18.36  ? 301  VAL C N   1 
ATOM   8578  C CA  . VAL C 1 292 ? 2.211   17.213  9.248   1.00 18.54  ? 301  VAL C CA  1 
ATOM   8579  C C   . VAL C 1 292 ? 1.313   17.661  8.109   1.00 19.26  ? 301  VAL C C   1 
ATOM   8580  O O   . VAL C 1 292 ? 0.821   18.805  8.080   1.00 20.00  ? 301  VAL C O   1 
ATOM   8581  C CB  . VAL C 1 292 ? 1.410   16.765  10.380  1.00 18.58  ? 301  VAL C CB  1 
ATOM   8582  C CG1 . VAL C 1 292 ? 0.169   16.238  9.909   1.00 20.46  ? 301  VAL C CG1 1 
ATOM   8583  C CG2 . VAL C 1 292 ? 2.129   15.705  11.051  1.00 18.97  ? 301  VAL C CG2 1 
ATOM   8584  N N   . GLN C 1 293 ? 1.093   16.753  7.159   1.00 19.25  ? 302  GLN C N   1 
ATOM   8585  C CA  . GLN C 1 293 ? 0.383   17.060  5.935   1.00 18.84  ? 302  GLN C CA  1 
ATOM   8586  C C   . GLN C 1 293 ? -0.645  16.003  5.650   1.00 18.87  ? 302  GLN C C   1 
ATOM   8587  O O   . GLN C 1 293 ? -0.304  14.890  5.277   1.00 18.83  ? 302  GLN C O   1 
ATOM   8588  C CB  . GLN C 1 293 ? 1.376   17.087  4.843   1.00 18.63  ? 302  GLN C CB  1 
ATOM   8589  C CG  . GLN C 1 293 ? 0.799   17.113  3.540   1.00 21.04  ? 302  GLN C CG  1 
ATOM   8590  C CD  . GLN C 1 293 ? 1.810   17.542  2.512   1.00 23.97  ? 302  GLN C CD  1 
ATOM   8591  O OE1 . GLN C 1 293 ? 2.753   18.301  2.819   1.00 23.99  ? 302  GLN C OE1 1 
ATOM   8592  N NE2 . GLN C 1 293 ? 1.623   17.079  1.272   1.00 25.36  ? 302  GLN C NE2 1 
ATOM   8593  N N   . LEU C 1 294 ? -1.905  16.386  5.824   1.00 18.80  ? 303  LEU C N   1 
ATOM   8594  C CA  . LEU C 1 294 ? -3.019  15.483  5.816   1.00 19.08  ? 303  LEU C CA  1 
ATOM   8595  C C   . LEU C 1 294 ? -3.810  15.648  4.562   1.00 19.60  ? 303  LEU C C   1 
ATOM   8596  O O   . LEU C 1 294 ? -3.792  16.732  3.981   1.00 19.78  ? 303  LEU C O   1 
ATOM   8597  C CB  . LEU C 1 294 ? -3.894  15.841  6.980   1.00 19.47  ? 303  LEU C CB  1 
ATOM   8598  C CG  . LEU C 1 294 ? -3.211  15.735  8.320   1.00 18.77  ? 303  LEU C CG  1 
ATOM   8599  C CD1 . LEU C 1 294 ? -4.216  15.743  9.401   1.00 19.06  ? 303  LEU C CD1 1 
ATOM   8600  C CD2 . LEU C 1 294 ? -2.472  14.446  8.365   1.00 19.53  ? 303  LEU C CD2 1 
ATOM   8601  N N   . PRO C 1 295 ? -4.505  14.586  4.121   1.00 20.27  ? 304  PRO C N   1 
ATOM   8602  C CA  . PRO C 1 295 ? -5.267  14.654  2.878   1.00 20.87  ? 304  PRO C CA  1 
ATOM   8603  C C   . PRO C 1 295 ? -6.568  15.351  3.084   1.00 21.73  ? 304  PRO C C   1 
ATOM   8604  O O   . PRO C 1 295 ? -7.066  15.328  4.189   1.00 22.28  ? 304  PRO C O   1 
ATOM   8605  C CB  . PRO C 1 295 ? -5.542  13.200  2.544   1.00 21.43  ? 304  PRO C CB  1 
ATOM   8606  C CG  . PRO C 1 295 ? -5.380  12.500  3.761   1.00 21.96  ? 304  PRO C CG  1 
ATOM   8607  C CD  . PRO C 1 295 ? -4.431  13.219  4.631   1.00 20.61  ? 304  PRO C CD  1 
ATOM   8608  N N   . LEU C 1 296 ? -7.079  15.995  2.034   1.00 22.15  ? 305  LEU C N   1 
ATOM   8609  C CA  . LEU C 1 296 ? -8.437  16.555  1.984   1.00 22.85  ? 305  LEU C CA  1 
ATOM   8610  C C   . LEU C 1 296 ? -9.152  16.059  0.728   1.00 23.85  ? 305  LEU C C   1 
ATOM   8611  O O   . LEU C 1 296 ? -8.669  16.264  -0.391  1.00 23.37  ? 305  LEU C O   1 
ATOM   8612  C CB  . LEU C 1 296 ? -8.441  18.076  1.953   1.00 22.03  ? 305  LEU C CB  1 
ATOM   8613  C CG  . LEU C 1 296 ? -7.786  18.821  3.072   1.00 21.54  ? 305  LEU C CG  1 
ATOM   8614  C CD1 . LEU C 1 296 ? -7.946  20.274  2.815   1.00 21.63  ? 305  LEU C CD1 1 
ATOM   8615  C CD2 . LEU C 1 296 ? -8.402  18.457  4.362   1.00 23.81  ? 305  LEU C CD2 1 
ATOM   8616  N N   . TYR C 1 297 ? -10.308 15.431  0.938   1.00 25.20  ? 306  TYR C N   1 
ATOM   8617  C CA  . TYR C 1 297 ? -11.171 14.985  -0.110  1.00 26.05  ? 306  TYR C CA  1 
ATOM   8618  C C   . TYR C 1 297 ? -12.210 16.053  -0.527  1.00 26.58  ? 306  TYR C C   1 
ATOM   8619  O O   . TYR C 1 297 ? -12.871 16.680  0.275   1.00 26.59  ? 306  TYR C O   1 
ATOM   8620  C CB  . TYR C 1 297 ? -11.856 13.716  0.346   1.00 27.50  ? 306  TYR C CB  1 
ATOM   8621  C CG  . TYR C 1 297 ? -10.933 12.805  1.026   1.00 27.73  ? 306  TYR C CG  1 
ATOM   8622  C CD1 . TYR C 1 297 ? -11.008 12.613  2.404   1.00 28.89  ? 306  TYR C CD1 1 
ATOM   8623  C CD2 . TYR C 1 297 ? -9.944  12.158  0.307   1.00 29.16  ? 306  TYR C CD2 1 
ATOM   8624  C CE1 . TYR C 1 297 ? -10.116 11.762  3.064   1.00 29.36  ? 306  TYR C CE1 1 
ATOM   8625  C CE2 . TYR C 1 297 ? -9.030  11.306  0.939   1.00 30.21  ? 306  TYR C CE2 1 
ATOM   8626  C CZ  . TYR C 1 297 ? -9.114  11.106  2.322   1.00 29.45  ? 306  TYR C CZ  1 
ATOM   8627  O OH  . TYR C 1 297 ? -8.198  10.254  2.924   1.00 26.90  ? 306  TYR C OH  1 
ATOM   8628  N N   . GLY C 1 298 ? -12.345 16.255  -1.821  1.00 26.91  ? 307  GLY C N   1 
ATOM   8629  C CA  . GLY C 1 298 ? -13.354 17.139  -2.312  1.00 27.14  ? 307  GLY C CA  1 
ATOM   8630  C C   . GLY C 1 298 ? -14.535 16.394  -2.835  1.00 28.63  ? 307  GLY C C   1 
ATOM   8631  O O   . GLY C 1 298 ? -15.308 17.000  -3.520  1.00 29.44  ? 307  GLY C O   1 
ATOM   8632  N N   . VAL C 1 299 ? -14.635 15.084  -2.572  1.00 29.51  ? 308  VAL C N   1 
ATOM   8633  C CA  . VAL C 1 299 ? -15.867 14.281  -2.791  1.00 31.73  ? 308  VAL C CA  1 
ATOM   8634  C C   . VAL C 1 299 ? -15.903 12.996  -2.010  1.00 33.18  ? 308  VAL C C   1 
ATOM   8635  O O   . VAL C 1 299 ? -14.908 12.306  -1.912  1.00 32.94  ? 308  VAL C O   1 
ATOM   8636  C CB  . VAL C 1 299 ? -16.058 13.820  -4.219  1.00 31.53  ? 308  VAL C CB  1 
ATOM   8637  C CG1 . VAL C 1 299 ? -16.803 14.803  -4.950  1.00 31.93  ? 308  VAL C CG1 1 
ATOM   8638  C CG2 . VAL C 1 299 ? -14.766 13.540  -4.861  1.00 30.38  ? 308  VAL C CG2 1 
ATOM   8639  N N   . ILE C 1 300 ? -17.067 12.637  -1.511  1.00 35.30  ? 309  ILE C N   1 
ATOM   8640  C CA  . ILE C 1 300 ? -17.199 11.424  -0.749  1.00 37.13  ? 309  ILE C CA  1 
ATOM   8641  C C   . ILE C 1 300 ? -18.378 10.666  -1.297  1.00 39.73  ? 309  ILE C C   1 
ATOM   8642  O O   . ILE C 1 300 ? -19.275 11.242  -1.906  1.00 40.95  ? 309  ILE C O   1 
ATOM   8643  C CB  . ILE C 1 300 ? -17.495 11.790  0.707   1.00 37.55  ? 309  ILE C CB  1 
ATOM   8644  C CG1 . ILE C 1 300 ? -16.372 12.645  1.241   1.00 36.71  ? 309  ILE C CG1 1 
ATOM   8645  C CG2 . ILE C 1 300 ? -17.614 10.585  1.598   1.00 38.33  ? 309  ILE C CG2 1 
ATOM   8646  C CD1 . ILE C 1 300 ? -15.024 11.987  1.061   1.00 37.38  ? 309  ILE C CD1 1 
ATOM   8647  N N   . ASP C 1 301 ? -18.401 9.364   -1.087  1.00 41.25  ? 310  ASP C N   1 
ATOM   8648  C CA  . ASP C 1 301 ? -19.646 8.609   -1.257  1.00 43.83  ? 310  ASP C CA  1 
ATOM   8649  C C   . ASP C 1 301 ? -20.147 8.502   -2.694  1.00 44.67  ? 310  ASP C C   1 
ATOM   8650  O O   . ASP C 1 301 ? -21.283 8.190   -2.906  1.00 47.02  ? 310  ASP C O   1 
ATOM   8651  C CB  . ASP C 1 301 ? -20.761 9.179   -0.353  1.00 44.88  ? 310  ASP C CB  1 
ATOM   8652  C CG  . ASP C 1 301 ? -20.415 9.116   1.147   1.00 45.18  ? 310  ASP C CG  1 
ATOM   8653  O OD1 . ASP C 1 301 ? -20.826 10.031  1.905   1.00 45.10  ? 310  ASP C OD1 1 
ATOM   8654  O OD2 . ASP C 1 301 ? -19.736 8.154   1.576   1.00 45.48  ? 310  ASP C OD2 1 
ATOM   8655  N N   . THR C 1 302 ? -19.310 8.758   -3.675  1.00 43.40  ? 311  THR C N   1 
ATOM   8656  C CA  . THR C 1 302 ? -19.619 8.425   -5.043  1.00 44.54  ? 311  THR C CA  1 
ATOM   8657  C C   . THR C 1 302 ? -19.336 6.956   -5.196  1.00 46.20  ? 311  THR C C   1 
ATOM   8658  O O   . THR C 1 302 ? -18.453 6.454   -4.497  1.00 46.27  ? 311  THR C O   1 
ATOM   8659  C CB  . THR C 1 302 ? -18.605 9.055   -5.924  1.00 42.55  ? 311  THR C CB  1 
ATOM   8660  O OG1 . THR C 1 302 ? -18.242 10.302  -5.369  1.00 41.39  ? 311  THR C OG1 1 
ATOM   8661  C CG2 . THR C 1 302 ? -19.169 9.329   -7.213  1.00 45.21  ? 311  THR C CG2 1 
ATOM   8662  N N   . PRO C 1 303 ? -20.040 6.255   -6.117  1.00 48.15  ? 312  PRO C N   1 
ATOM   8663  C CA  . PRO C 1 303 ? -19.642 4.855   -6.365  1.00 49.59  ? 312  PRO C CA  1 
ATOM   8664  C C   . PRO C 1 303 ? -18.274 4.708   -7.104  1.00 48.58  ? 312  PRO C C   1 
ATOM   8665  O O   . PRO C 1 303 ? -17.934 5.546   -7.953  1.00 47.32  ? 312  PRO C O   1 
ATOM   8666  C CB  . PRO C 1 303 ? -20.778 4.338   -7.224  1.00 51.53  ? 312  PRO C CB  1 
ATOM   8667  C CG  . PRO C 1 303 ? -21.284 5.568   -7.939  1.00 50.31  ? 312  PRO C CG  1 
ATOM   8668  C CD  . PRO C 1 303 ? -21.190 6.661   -6.952  1.00 48.95  ? 312  PRO C CD  1 
ATOM   8669  N N   . CYS C 1 304 ? -17.486 3.687   -6.753  1.00 49.09  ? 313  CYS C N   1 
ATOM   8670  C CA  . CYS C 1 304 ? -16.350 3.314   -7.575  1.00 48.92  ? 313  CYS C CA  1 
ATOM   8671  C C   . CYS C 1 304 ? -16.447 1.869   -7.899  1.00 50.79  ? 313  CYS C C   1 
ATOM   8672  O O   . CYS C 1 304 ? -17.198 1.144   -7.273  1.00 52.51  ? 313  CYS C O   1 
ATOM   8673  C CB  . CYS C 1 304 ? -15.011 3.482   -6.882  1.00 47.64  ? 313  CYS C CB  1 
ATOM   8674  S SG  . CYS C 1 304 ? -14.673 4.930   -5.853  1.00 48.05  ? 313  CYS C SG  1 
ATOM   8675  N N   . TRP C 1 305 ? -15.633 1.452   -8.859  1.00 50.74  ? 314  TRP C N   1 
ATOM   8676  C CA  . TRP C 1 305 ? -15.540 0.058   -9.265  1.00 52.93  ? 314  TRP C CA  1 
ATOM   8677  C C   . TRP C 1 305 ? -14.152 -0.331  -9.775  1.00 51.98  ? 314  TRP C C   1 
ATOM   8678  O O   . TRP C 1 305 ? -13.475 0.489   -10.392 1.00 50.53  ? 314  TRP C O   1 
ATOM   8679  C CB  . TRP C 1 305 ? -16.576 -0.221  -10.333 1.00 55.08  ? 314  TRP C CB  1 
ATOM   8680  C CG  . TRP C 1 305 ? -16.529 0.664   -11.528 1.00 54.94  ? 314  TRP C CG  1 
ATOM   8681  C CD1 . TRP C 1 305 ? -15.978 0.366   -12.720 1.00 56.64  ? 314  TRP C CD1 1 
ATOM   8682  C CD2 . TRP C 1 305 ? -17.103 1.961   -11.666 1.00 54.55  ? 314  TRP C CD2 1 
ATOM   8683  N NE1 . TRP C 1 305 ? -16.159 1.398   -13.599 1.00 56.09  ? 314  TRP C NE1 1 
ATOM   8684  C CE2 . TRP C 1 305 ? -16.847 2.393   -12.970 1.00 54.47  ? 314  TRP C CE2 1 
ATOM   8685  C CE3 . TRP C 1 305 ? -17.804 2.796   -10.814 1.00 55.08  ? 314  TRP C CE3 1 
ATOM   8686  C CZ2 . TRP C 1 305 ? -17.256 3.618   -13.442 1.00 54.12  ? 314  TRP C CZ2 1 
ATOM   8687  C CZ3 . TRP C 1 305 ? -18.211 4.005   -11.281 1.00 55.29  ? 314  TRP C CZ3 1 
ATOM   8688  C CH2 . TRP C 1 305 ? -17.937 4.410   -12.588 1.00 54.77  ? 314  TRP C CH2 1 
ATOM   8689  N N   . LYS C 1 306 ? -13.726 -1.566  -9.517  1.00 52.95  ? 315  LYS C N   1 
ATOM   8690  C CA  . LYS C 1 306 ? -12.438 -2.021  -10.012 1.00 52.53  ? 315  LYS C CA  1 
ATOM   8691  C C   . LYS C 1 306 ? -12.612 -2.923  -11.211 1.00 54.96  ? 315  LYS C C   1 
ATOM   8692  O O   . LYS C 1 306 ? -13.398 -3.873  -11.164 1.00 57.59  ? 315  LYS C O   1 
ATOM   8693  C CB  . LYS C 1 306 ? -11.639 -2.745  -8.940  1.00 52.46  ? 315  LYS C CB  1 
ATOM   8694  C CG  . LYS C 1 306 ? -10.157 -2.841  -9.279  1.00 51.57  ? 315  LYS C CG  1 
ATOM   8695  C CD  . LYS C 1 306 ? -9.365  -3.546  -8.210  1.00 52.90  ? 315  LYS C CD  1 
ATOM   8696  C CE  . LYS C 1 306 ? -7.906  -3.296  -8.424  1.00 52.28  ? 315  LYS C CE  1 
ATOM   8697  N NZ  . LYS C 1 306 ? -7.104  -4.351  -7.802  1.00 55.09  ? 315  LYS C NZ  1 
ATOM   8698  N N   . LEU C 1 307 ? -11.855 -2.628  -12.267 1.00 54.43  ? 316  LEU C N   1 
ATOM   8699  C CA  . LEU C 1 307 ? -11.881 -3.379  -13.518 1.00 56.82  ? 316  LEU C CA  1 
ATOM   8700  C C   . LEU C 1 307 ? -10.702 -4.344  -13.640 1.00 58.37  ? 316  LEU C C   1 
ATOM   8701  O O   . LEU C 1 307 ? -9.555  -3.957  -13.473 1.00 57.36  ? 316  LEU C O   1 
ATOM   8702  C CB  . LEU C 1 307 ? -11.880 -2.397  -14.685 1.00 55.29  ? 316  LEU C CB  1 
ATOM   8703  C CG  . LEU C 1 307 ? -11.794 -2.955  -16.093 1.00 56.66  ? 316  LEU C CG  1 
ATOM   8704  C CD1 . LEU C 1 307 ? -12.954 -3.879  -16.371 1.00 59.42  ? 316  LEU C CD1 1 
ATOM   8705  C CD2 . LEU C 1 307 ? -11.775 -1.807  -17.080 1.00 55.14  ? 316  LEU C CD2 1 
ATOM   8706  N N   . HIS C 1 308 ? -10.975 -5.608  -13.906 1.00 61.58  ? 317  HIS C N   1 
ATOM   8707  C CA  . HIS C 1 308 ? -9.900  -6.526  -14.187 1.00 63.33  ? 317  HIS C CA  1 
ATOM   8708  C C   . HIS C 1 308 ? -10.160 -7.012  -15.575 1.00 64.97  ? 317  HIS C C   1 
ATOM   8709  O O   . HIS C 1 308 ? -11.263 -6.871  -16.089 1.00 65.99  ? 317  HIS C O   1 
ATOM   8710  C CB  . HIS C 1 308 ? -9.862  -7.702  -13.224 1.00 65.82  ? 317  HIS C CB  1 
ATOM   8711  C CG  . HIS C 1 308 ? -10.078 -7.334  -11.789 1.00 66.85  ? 317  HIS C CG  1 
ATOM   8712  N ND1 . HIS C 1 308 ? -9.040  -7.166  -10.895 1.00 67.61  ? 317  HIS C ND1 1 
ATOM   8713  C CD2 . HIS C 1 308 ? -11.221 -7.143  -11.083 1.00 68.32  ? 317  HIS C CD2 1 
ATOM   8714  C CE1 . HIS C 1 308 ? -9.535  -6.873  -9.703  1.00 67.76  ? 317  HIS C CE1 1 
ATOM   8715  N NE2 . HIS C 1 308 ? -10.855 -6.852  -9.791  1.00 68.03  ? 317  HIS C NE2 1 
ATOM   8716  N N   . THR C 1 309 ? -9.154  -7.622  -16.172 1.00 65.54  ? 318  THR C N   1 
ATOM   8717  C CA  . THR C 1 309 ? -9.132  -7.750  -17.594 1.00 66.32  ? 318  THR C CA  1 
ATOM   8718  C C   . THR C 1 309 ? -8.367  -8.989  -18.002 1.00 68.94  ? 318  THR C C   1 
ATOM   8719  O O   . THR C 1 309 ? -7.292  -9.225  -17.495 1.00 68.57  ? 318  THR C O   1 
ATOM   8720  C CB  . THR C 1 309 ? -8.502  -6.472  -18.127 1.00 63.30  ? 318  THR C CB  1 
ATOM   8721  O OG1 . THR C 1 309 ? -9.508  -5.707  -18.784 1.00 62.91  ? 318  THR C OG1 1 
ATOM   8722  C CG2 . THR C 1 309 ? -7.389  -6.741  -19.072 1.00 64.11  ? 318  THR C CG2 1 
ATOM   8723  N N   . SER C 1 310 ? -8.916  -9.797  -18.897 1.00 71.99  ? 319  SER C N   1 
ATOM   8724  C CA  . SER C 1 310 ? -8.175  -10.953 -19.362 1.00 75.03  ? 319  SER C CA  1 
ATOM   8725  C C   . SER C 1 310 ? -8.334  -11.120 -20.851 1.00 77.41  ? 319  SER C C   1 
ATOM   8726  O O   . SER C 1 310 ? -9.344  -10.687 -21.388 1.00 77.92  ? 319  SER C O   1 
ATOM   8727  C CB  . SER C 1 310 ? -8.651  -12.203 -18.659 1.00 77.64  ? 319  SER C CB  1 
ATOM   8728  O OG  . SER C 1 310 ? -7.848  -13.295 -19.051 1.00 79.89  ? 319  SER C OG  1 
ATOM   8729  N N   . PRO C 1 311 ? -7.341  -11.751 -21.520 1.00 79.46  ? 320  PRO C N   1 
ATOM   8730  C CA  . PRO C 1 311 ? -7.369  -11.976 -22.968 1.00 81.86  ? 320  PRO C CA  1 
ATOM   8731  C C   . PRO C 1 311 ? -8.594  -12.710 -23.495 1.00 85.66  ? 320  PRO C C   1 
ATOM   8732  O O   . PRO C 1 311 ? -9.189  -13.534 -22.799 1.00 87.20  ? 320  PRO C O   1 
ATOM   8733  C CB  . PRO C 1 311 ? -6.115  -12.811 -23.218 1.00 83.31  ? 320  PRO C CB  1 
ATOM   8734  C CG  . PRO C 1 311 ? -5.718  -13.319 -21.883 1.00 82.93  ? 320  PRO C CG  1 
ATOM   8735  C CD  . PRO C 1 311 ? -6.075  -12.237 -20.951 1.00 79.49  ? 320  PRO C CD  1 
ATOM   8736  N N   . LEU C 1 312 ? -8.933  -12.410 -24.740 1.00 87.53  ? 321  LEU C N   1 
ATOM   8737  C CA  . LEU C 1 312 ? -10.146 -12.875 -25.342 1.00 91.66  ? 321  LEU C CA  1 
ATOM   8738  C C   . LEU C 1 312 ? -9.884  -13.257 -26.816 1.00 95.64  ? 321  LEU C C   1 
ATOM   8739  O O   . LEU C 1 312 ? -9.461  -12.419 -27.608 1.00 94.15  ? 321  LEU C O   1 
ATOM   8740  C CB  . LEU C 1 312 ? -11.162 -11.747 -25.255 1.00 88.64  ? 321  LEU C CB  1 
ATOM   8741  C CG  . LEU C 1 312 ? -12.642 -12.081 -25.154 1.00 90.52  ? 321  LEU C CG  1 
ATOM   8742  C CD1 . LEU C 1 312 ? -13.378 -10.877 -25.694 1.00 87.70  ? 321  LEU C CD1 1 
ATOM   8743  C CD2 . LEU C 1 312 ? -13.099 -13.397 -25.890 1.00 95.19  ? 321  LEU C CD2 1 
ATOM   8744  N N   . CYS C 1 313 ? -10.137 -14.511 -27.192 1.00 102.06 ? 322  CYS C N   1 
ATOM   8745  C CA  . CYS C 1 313 ? -9.944  -14.924 -28.583 1.00 107.08 ? 322  CYS C CA  1 
ATOM   8746  C C   . CYS C 1 313 ? -11.257 -15.139 -29.307 1.00 109.99 ? 322  CYS C C   1 
ATOM   8747  O O   . CYS C 1 313 ? -11.283 -15.248 -30.550 1.00 111.89 ? 322  CYS C O   1 
ATOM   8748  C CB  . CYS C 1 313 ? -9.046  -16.160 -28.692 1.00 110.55 ? 322  CYS C CB  1 
ATOM   8749  S SG  . CYS C 1 313 ? -7.262  -15.783 -28.485 1.00 112.72 ? 322  CYS C SG  1 
ATOM   8750  N N   . THR C 1 314 ? -12.333 -15.239 -28.521 1.00 111.29 ? 323  THR C N   1 
ATOM   8751  C CA  . THR C 1 314 ? -13.696 -15.225 -29.075 1.00 113.75 ? 323  THR C CA  1 
ATOM   8752  C C   . THR C 1 314 ? -14.109 -13.744 -29.292 1.00 110.58 ? 323  THR C C   1 
ATOM   8753  O O   . THR C 1 314 ? -14.365 -12.992 -28.320 1.00 107.59 ? 323  THR C O   1 
ATOM   8754  C CB  . THR C 1 314 ? -14.767 -16.121 -28.265 1.00 116.54 ? 323  THR C CB  1 
ATOM   8755  O OG1 . THR C 1 314 ? -14.367 -16.302 -26.887 1.00 115.07 ? 323  THR C OG1 1 
ATOM   8756  C CG2 . THR C 1 314 ? -15.019 -17.508 -28.971 1.00 120.37 ? 323  THR C CG2 1 
ATOM   8757  N N   . THR C 1 315 ? -14.113 -13.335 -30.575 1.00 110.93 ? 324  THR C N   1 
ATOM   8758  C CA  . THR C 1 315 ? -14.402 -11.948 -30.978 1.00 107.77 ? 324  THR C CA  1 
ATOM   8759  C C   . THR C 1 315 ? -14.546 -11.749 -32.516 1.00 109.19 ? 324  THR C C   1 
ATOM   8760  O O   . THR C 1 315 ? -14.256 -12.666 -33.291 1.00 112.30 ? 324  THR C O   1 
ATOM   8761  C CB  . THR C 1 315 ? -13.358 -10.955 -30.377 1.00 103.78 ? 324  THR C CB  1 
ATOM   8762  O OG1 . THR C 1 315 ? -12.388 -11.661 -29.581 1.00 103.07 ? 324  THR C OG1 1 
ATOM   8763  C CG2 . THR C 1 315 ? -14.071 -9.934  -29.514 1.00 100.64 ? 324  THR C CG2 1 
ATOM   8764  N N   . ASN C 1 316 ? -15.036 -10.568 -32.925 1.00 107.15 ? 325  ASN C N   1 
ATOM   8765  C CA  . ASN C 1 316 ? -15.096 -10.116 -34.339 1.00 107.72 ? 325  ASN C CA  1 
ATOM   8766  C C   . ASN C 1 316 ? -15.670 -8.694  -34.518 1.00 104.75 ? 325  ASN C C   1 
ATOM   8767  O O   . ASN C 1 316 ? -16.579 -8.291  -33.790 1.00 103.71 ? 325  ASN C O   1 
ATOM   8768  C CB  . ASN C 1 316 ? -15.910 -11.085 -35.215 1.00 111.80 ? 325  ASN C CB  1 
ATOM   8769  C CG  . ASN C 1 316 ? -17.315 -10.562 -35.535 1.00 112.19 ? 325  ASN C CG  1 
ATOM   8770  O OD1 . ASN C 1 316 ? -18.196 -10.559 -34.675 1.00 112.50 ? 325  ASN C OD1 1 
ATOM   8771  N ND2 . ASN C 1 316 ? -17.520 -10.112 -36.775 1.00 112.54 ? 325  ASN C ND2 1 
ATOM   8772  N N   . THR C 1 317 ? -15.156 -7.953  -35.500 1.00 103.69 ? 326  THR C N   1 
ATOM   8773  C CA  . THR C 1 317 ? -15.798 -6.713  -35.946 1.00 101.90 ? 326  THR C CA  1 
ATOM   8774  C C   . THR C 1 317 ? -16.117 -6.801  -37.423 1.00 104.15 ? 326  THR C C   1 
ATOM   8775  O O   . THR C 1 317 ? -15.206 -7.004  -38.235 1.00 105.29 ? 326  THR C O   1 
ATOM   8776  C CB  . THR C 1 317 ? -14.878 -5.477  -35.806 1.00 98.25  ? 326  THR C CB  1 
ATOM   8777  O OG1 . THR C 1 317 ? -14.286 -5.446  -34.507 1.00 96.70  ? 326  THR C OG1 1 
ATOM   8778  C CG2 . THR C 1 317 ? -15.660 -4.172  -36.052 1.00 96.21  ? 326  THR C CG2 1 
ATOM   8779  N N   . LYS C 1 318 ? -17.396 -6.656  -37.774 1.00 105.05 ? 327  LYS C N   1 
ATOM   8780  C CA  . LYS C 1 318 ? -17.762 -6.221  -39.121 1.00 105.59 ? 327  LYS C CA  1 
ATOM   8781  C C   . LYS C 1 318 ? -16.834 -6.840  -40.193 1.00 107.13 ? 327  LYS C C   1 
ATOM   8782  O O   . LYS C 1 318 ? -15.981 -6.147  -40.782 1.00 105.75 ? 327  LYS C O   1 
ATOM   8783  C CB  . LYS C 1 318 ? -17.678 -4.683  -39.146 1.00 102.23 ? 327  LYS C CB  1 
ATOM   8784  C CG  . LYS C 1 318 ? -18.564 -3.971  -40.142 1.00 103.57 ? 327  LYS C CG  1 
ATOM   8785  C CD  . LYS C 1 318 ? -18.245 -2.474  -40.149 1.00 102.27 ? 327  LYS C CD  1 
ATOM   8786  C CE  . LYS C 1 318 ? -18.739 -1.817  -41.446 1.00 104.65 ? 327  LYS C CE  1 
ATOM   8787  N NZ  . LYS C 1 318 ? -18.001 -0.552  -41.793 1.00 103.01 ? 327  LYS C NZ  1 
ATOM   8788  N N   . GLU C 1 319 ? -16.983 -8.152  -40.401 1.00 109.87 ? 328  GLU C N   1 
ATOM   8789  C CA  . GLU C 1 319 ? -16.204 -8.923  -41.386 1.00 111.69 ? 328  GLU C CA  1 
ATOM   8790  C C   . GLU C 1 319 ? -14.725 -9.052  -41.031 1.00 110.08 ? 328  GLU C C   1 
ATOM   8791  O O   . GLU C 1 319 ? -13.843 -8.899  -41.873 1.00 109.97 ? 328  GLU C O   1 
ATOM   8792  C CB  . GLU C 1 319 ? -16.380 -8.354  -42.801 1.00 112.08 ? 328  GLU C CB  1 
ATOM   8793  C CG  . GLU C 1 319 ? -17.688 -8.747  -43.474 1.00 114.76 ? 328  GLU C CG  1 
ATOM   8794  C CD  . GLU C 1 319 ? -17.519 -9.010  -44.962 1.00 118.05 ? 328  GLU C CD  1 
ATOM   8795  O OE1 . GLU C 1 319 ? -18.468 -9.533  -45.596 1.00 121.43 ? 328  GLU C OE1 1 
ATOM   8796  O OE2 . GLU C 1 319 ? -16.429 -8.704  -45.502 1.00 117.67 ? 328  GLU C OE2 1 
ATOM   8797  N N   . GLY C 1 320 ? -14.463 -9.351  -39.774 1.00 108.67 ? 329  GLY C N   1 
ATOM   8798  C CA  . GLY C 1 320 ? -13.110 -9.277  -39.263 1.00 106.92 ? 329  GLY C CA  1 
ATOM   8799  C C   . GLY C 1 320 ? -12.833 -10.430 -38.336 1.00 108.53 ? 329  GLY C C   1 
ATOM   8800  O O   . GLY C 1 320 ? -12.309 -10.242 -37.232 1.00 106.28 ? 329  GLY C O   1 
ATOM   8801  N N   . SER C 1 321 ? -13.227 -11.616 -38.800 1.00 112.24 ? 330  SER C N   1 
ATOM   8802  C CA  . SER C 1 321 ? -12.906 -12.924 -38.191 1.00 114.71 ? 330  SER C CA  1 
ATOM   8803  C C   . SER C 1 321 ? -12.299 -12.916 -36.757 1.00 112.20 ? 330  SER C C   1 
ATOM   8804  O O   . SER C 1 321 ? -12.968 -12.519 -35.801 1.00 110.04 ? 330  SER C O   1 
ATOM   8805  C CB  . SER C 1 321 ? -12.046 -13.756 -39.176 1.00 118.04 ? 330  SER C CB  1 
ATOM   8806  O OG  . SER C 1 321 ? -12.629 -15.020 -39.481 1.00 122.24 ? 330  SER C OG  1 
ATOM   8807  N N   . ASN C 1 322 ? -11.040 -13.346 -36.638 1.00 112.36 ? 331  ASN C N   1 
ATOM   8808  C CA  . ASN C 1 322 ? -10.352 -13.589 -35.350 1.00 110.90 ? 331  ASN C CA  1 
ATOM   8809  C C   . ASN C 1 322 ? -9.989  -12.337 -34.511 1.00 105.80 ? 331  ASN C C   1 
ATOM   8810  O O   . ASN C 1 322 ? -10.841 -11.490 -34.220 1.00 103.33 ? 331  ASN C O   1 
ATOM   8811  C CB  . ASN C 1 322 ? -9.098  -14.471 -35.601 1.00 113.31 ? 331  ASN C CB  1 
ATOM   8812  C CG  . ASN C 1 322 ? -8.629  -15.243 -34.353 1.00 113.93 ? 331  ASN C CG  1 
ATOM   8813  O OD1 . ASN C 1 322 ? -8.654  -14.739 -33.223 1.00 110.46 ? 331  ASN C OD1 1 
ATOM   8814  N ND2 . ASN C 1 322 ? -8.172  -16.473 -34.575 1.00 117.95 ? 331  ASN C ND2 1 
ATOM   8815  N N   . ILE C 1 323 ? -8.708  -12.258 -34.150 1.00 104.17 ? 332  ILE C N   1 
ATOM   8816  C CA  . ILE C 1 323 ? -8.113  -11.302 -33.191 1.00 99.87  ? 332  ILE C CA  1 
ATOM   8817  C C   . ILE C 1 323 ? -8.381  -11.564 -31.702 1.00 98.79  ? 332  ILE C C   1 
ATOM   8818  O O   . ILE C 1 323 ? -9.508  -11.825 -31.271 1.00 99.18  ? 332  ILE C O   1 
ATOM   8819  C CB  . ILE C 1 323 ? -8.269  -9.780  -33.577 1.00 96.38  ? 332  ILE C CB  1 
ATOM   8820  C CG1 . ILE C 1 323 ? -6.920  -9.063  -33.459 1.00 93.30  ? 332  ILE C CG1 1 
ATOM   8821  C CG2 . ILE C 1 323 ? -9.324  -9.080  -32.732 1.00 93.23  ? 332  ILE C CG2 1 
ATOM   8822  C CD1 . ILE C 1 323 ? -5.928  -9.364  -34.600 1.00 94.64  ? 332  ILE C CD1 1 
ATOM   8823  N N   . CYS C 1 324 ? -7.292  -11.540 -30.945 1.00 97.39  ? 333  CYS C N   1 
ATOM   8824  C CA  . CYS C 1 324 ? -7.342  -11.699 -29.508 1.00 96.45  ? 333  CYS C CA  1 
ATOM   8825  C C   . CYS C 1 324 ? -7.003  -10.388 -28.867 1.00 91.44  ? 333  CYS C C   1 
ATOM   8826  O O   . CYS C 1 324 ? -6.170  -9.608  -29.336 1.00 89.40  ? 333  CYS C O   1 
ATOM   8827  C CB  . CYS C 1 324 ? -6.453  -12.837 -29.008 1.00 98.97  ? 333  CYS C CB  1 
ATOM   8828  S SG  . CYS C 1 324 ? -6.824  -14.373 -29.925 1.00 108.60 ? 333  CYS C SG  1 
ATOM   8829  N N   . LEU C 1 325 ? -7.721  -10.148 -27.795 1.00 89.34  ? 334  LEU C N   1 
ATOM   8830  C CA  . LEU C 1 325 ? -7.907  -8.830  -27.286 1.00 84.61  ? 334  LEU C CA  1 
ATOM   8831  C C   . LEU C 1 325 ? -7.655  -8.937  -25.858 1.00 82.88  ? 334  LEU C C   1 
ATOM   8832  O O   . LEU C 1 325 ? -8.149  -9.854  -25.210 1.00 84.79  ? 334  LEU C O   1 
ATOM   8833  C CB  . LEU C 1 325 ? -9.364  -8.416  -27.410 1.00 84.30  ? 334  LEU C CB  1 
ATOM   8834  C CG  . LEU C 1 325 ? -9.838  -7.976  -28.780 1.00 85.45  ? 334  LEU C CG  1 
ATOM   8835  C CD1 . LEU C 1 325 ? -11.068 -7.091  -28.649 1.00 83.51  ? 334  LEU C CD1 1 
ATOM   8836  C CD2 . LEU C 1 325 ? -8.691  -7.248  -29.446 1.00 85.09  ? 334  LEU C CD2 1 
ATOM   8837  N N   . THR C 1 326 ? -6.887  -7.986  -25.359 1.00 79.20  ? 335  THR C N   1 
ATOM   8838  C CA  . THR C 1 326 ? -6.832  -7.720  -23.939 1.00 76.57  ? 335  THR C CA  1 
ATOM   8839  C C   . THR C 1 326 ? -7.077  -6.249  -23.714 1.00 72.90  ? 335  THR C C   1 
ATOM   8840  O O   . THR C 1 326 ? -6.450  -5.400  -24.322 1.00 71.14  ? 335  THR C O   1 
ATOM   8841  C CB  . THR C 1 326 ? -5.527  -8.146  -23.340 1.00 76.31  ? 335  THR C CB  1 
ATOM   8842  O OG1 . THR C 1 326 ? -5.186  -9.424  -23.866 1.00 79.55  ? 335  THR C OG1 1 
ATOM   8843  C CG2 . THR C 1 326 ? -5.683  -8.295  -21.872 1.00 75.64  ? 335  THR C CG2 1 
ATOM   8844  N N   . ARG C 1 327 ? -8.036  -5.965  -22.853 1.00 71.87  ? 336  ARG C N   1 
ATOM   8845  C CA  . ARG C 1 327 ? -8.465  -4.612  -22.622 1.00 69.36  ? 336  ARG C CA  1 
ATOM   8846  C C   . ARG C 1 327 ? -7.432  -3.948  -21.732 1.00 67.16  ? 336  ARG C C   1 
ATOM   8847  O O   . ARG C 1 327 ? -7.099  -4.459  -20.674 1.00 67.03  ? 336  ARG C O   1 
ATOM   8848  C CB  . ARG C 1 327 ? -9.855  -4.608  -21.988 1.00 69.39  ? 336  ARG C CB  1 
ATOM   8849  C CG  . ARG C 1 327 ? -10.619 -3.330  -22.231 1.00 67.93  ? 336  ARG C CG  1 
ATOM   8850  C CD  . ARG C 1 327 ? -12.084 -3.584  -22.449 1.00 69.56  ? 336  ARG C CD  1 
ATOM   8851  N NE  . ARG C 1 327 ? -12.875 -3.663  -21.216 1.00 69.17  ? 336  ARG C NE  1 
ATOM   8852  C CZ  . ARG C 1 327 ? -13.281 -2.619  -20.500 1.00 66.60  ? 336  ARG C CZ  1 
ATOM   8853  N NH1 . ARG C 1 327 ? -12.948 -1.372  -20.831 1.00 63.84  ? 336  ARG C NH1 1 
ATOM   8854  N NH2 . ARG C 1 327 ? -14.011 -2.840  -19.428 1.00 66.80  ? 336  ARG C NH2 1 
ATOM   8855  N N   . THR C 1 328 ? -6.924  -2.807  -22.175 1.00 65.81  ? 337  THR C N   1 
ATOM   8856  C CA  . THR C 1 328 ? -5.746  -2.194  -21.569 1.00 64.76  ? 337  THR C CA  1 
ATOM   8857  C C   . THR C 1 328 ? -5.997  -1.550  -20.231 1.00 62.85  ? 337  THR C C   1 
ATOM   8858  O O   . THR C 1 328 ? -5.250  -1.736  -19.280 1.00 62.43  ? 337  THR C O   1 
ATOM   8859  C CB  . THR C 1 328 ? -5.183  -1.108  -22.473 1.00 63.53  ? 337  THR C CB  1 
ATOM   8860  O OG1 . THR C 1 328 ? -4.576  -1.735  -23.594 1.00 67.45  ? 337  THR C OG1 1 
ATOM   8861  C CG2 . THR C 1 328 ? -4.114  -0.299  -21.762 1.00 62.10  ? 337  THR C CG2 1 
ATOM   8862  N N   . ASP C 1 329 ? -7.066  -0.775  -20.183 1.00 62.25  ? 338  ASP C N   1 
ATOM   8863  C CA  . ASP C 1 329 ? -7.350  0.200   -19.122 1.00 60.00  ? 338  ASP C CA  1 
ATOM   8864  C C   . ASP C 1 329 ? -7.814  -0.408  -17.792 1.00 58.94  ? 338  ASP C C   1 
ATOM   8865  O O   . ASP C 1 329 ? -8.956  -0.205  -17.405 1.00 58.88  ? 338  ASP C O   1 
ATOM   8866  C CB  . ASP C 1 329 ? -8.430  1.172   -19.654 1.00 60.47  ? 338  ASP C CB  1 
ATOM   8867  C CG  . ASP C 1 329 ? -9.481  0.468   -20.618 1.00 66.53  ? 338  ASP C CG  1 
ATOM   8868  O OD1 . ASP C 1 329 ? -9.993  1.140   -21.564 1.00 70.03  ? 338  ASP C OD1 1 
ATOM   8869  O OD2 . ASP C 1 329 ? -9.801  -0.747  -20.441 1.00 70.21  ? 338  ASP C OD2 1 
ATOM   8870  N N   . ARG C 1 330 ? -6.962  -1.149  -17.083 1.00 57.81  ? 339  ARG C N   1 
ATOM   8871  C CA  . ARG C 1 330 ? -7.414  -1.778  -15.838 1.00 57.03  ? 339  ARG C CA  1 
ATOM   8872  C C   . ARG C 1 330 ? -7.169  -0.865  -14.688 1.00 53.89  ? 339  ARG C C   1 
ATOM   8873  O O   . ARG C 1 330 ? -6.315  0.007   -14.757 1.00 52.02  ? 339  ARG C O   1 
ATOM   8874  C CB  . ARG C 1 330 ? -6.684  -3.066  -15.505 1.00 58.70  ? 339  ARG C CB  1 
ATOM   8875  C CG  . ARG C 1 330 ? -6.352  -3.968  -16.619 1.00 61.93  ? 339  ARG C CG  1 
ATOM   8876  C CD  . ARG C 1 330 ? -5.037  -4.587  -16.268 1.00 63.37  ? 339  ARG C CD  1 
ATOM   8877  N NE  . ARG C 1 330 ? -4.577  -5.548  -17.254 1.00 65.64  ? 339  ARG C NE  1 
ATOM   8878  C CZ  . ARG C 1 330 ? -4.731  -6.861  -17.126 1.00 68.47  ? 339  ARG C CZ  1 
ATOM   8879  N NH1 . ARG C 1 330 ? -5.343  -7.357  -16.043 1.00 70.21  ? 339  ARG C NH1 1 
ATOM   8880  N NH2 . ARG C 1 330 ? -4.282  -7.679  -18.078 1.00 68.59  ? 339  ARG C NH2 1 
ATOM   8881  N N   . GLY C 1 331 ? -7.884  -1.111  -13.600 1.00 53.38  ? 340  GLY C N   1 
ATOM   8882  C CA  . GLY C 1 331 ? -7.760  -0.315  -12.388 1.00 50.59  ? 340  GLY C CA  1 
ATOM   8883  C C   . GLY C 1 331 ? -9.081  0.224   -11.869 1.00 49.69  ? 340  GLY C C   1 
ATOM   8884  O O   . GLY C 1 331 ? -10.144 -0.299  -12.171 1.00 51.48  ? 340  GLY C O   1 
ATOM   8885  N N   . TRP C 1 332 ? -9.003  1.289   -11.090 1.00 47.19  ? 341  TRP C N   1 
ATOM   8886  C CA  . TRP C 1 332 ? -10.149 1.832   -10.397 1.00 46.59  ? 341  TRP C CA  1 
ATOM   8887  C C   . TRP C 1 332 ? -10.833 2.929   -11.165 1.00 46.04  ? 341  TRP C C   1 
ATOM   8888  O O   . TRP C 1 332 ? -10.240 3.937   -11.523 1.00 44.71  ? 341  TRP C O   1 
ATOM   8889  C CB  . TRP C 1 332 ? -9.714  2.407   -9.061  1.00 44.86  ? 341  TRP C CB  1 
ATOM   8890  C CG  . TRP C 1 332 ? -9.502  1.407   -8.042  1.00 45.22  ? 341  TRP C CG  1 
ATOM   8891  C CD1 . TRP C 1 332 ? -8.318  0.940   -7.614  1.00 45.07  ? 341  TRP C CD1 1 
ATOM   8892  C CD2 . TRP C 1 332 ? -10.510 0.724   -7.297  1.00 46.55  ? 341  TRP C CD2 1 
ATOM   8893  N NE1 . TRP C 1 332 ? -8.509  -0.009  -6.653  1.00 46.76  ? 341  TRP C NE1 1 
ATOM   8894  C CE2 . TRP C 1 332 ? -9.852  -0.157  -6.431  1.00 47.05  ? 341  TRP C CE2 1 
ATOM   8895  C CE3 . TRP C 1 332 ? -11.912 0.768   -7.282  1.00 47.48  ? 341  TRP C CE3 1 
ATOM   8896  C CZ2 . TRP C 1 332 ? -10.543 -0.998  -5.549  1.00 47.92  ? 341  TRP C CZ2 1 
ATOM   8897  C CZ3 . TRP C 1 332 ? -12.599 -0.061  -6.403  1.00 48.00  ? 341  TRP C CZ3 1 
ATOM   8898  C CH2 . TRP C 1 332 ? -11.917 -0.931  -5.555  1.00 47.87  ? 341  TRP C CH2 1 
ATOM   8899  N N   . TYR C 1 333 ? -12.104 2.742   -11.407 1.00 47.41  ? 342  TYR C N   1 
ATOM   8900  C CA  . TYR C 1 333 ? -12.867 3.809   -11.929 1.00 46.71  ? 342  TYR C CA  1 
ATOM   8901  C C   . TYR C 1 333 ? -13.650 4.229   -10.734 1.00 46.49  ? 342  TYR C C   1 
ATOM   8902  O O   . TYR C 1 333 ? -13.661 3.537   -9.724  1.00 46.74  ? 342  TYR C O   1 
ATOM   8903  C CB  . TYR C 1 333 ? -13.723 3.309   -13.079 1.00 48.61  ? 342  TYR C CB  1 
ATOM   8904  C CG  . TYR C 1 333 ? -12.892 2.884   -14.260 1.00 49.47  ? 342  TYR C CG  1 
ATOM   8905  C CD1 . TYR C 1 333 ? -12.195 1.680   -14.245 1.00 51.34  ? 342  TYR C CD1 1 
ATOM   8906  C CD2 . TYR C 1 333 ? -12.775 3.702   -15.380 1.00 49.79  ? 342  TYR C CD2 1 
ATOM   8907  C CE1 . TYR C 1 333 ? -11.426 1.303   -15.306 1.00 52.62  ? 342  TYR C CE1 1 
ATOM   8908  C CE2 . TYR C 1 333 ? -12.004 3.341   -16.440 1.00 50.34  ? 342  TYR C CE2 1 
ATOM   8909  C CZ  . TYR C 1 333 ? -11.339 2.140   -16.395 1.00 52.30  ? 342  TYR C CZ  1 
ATOM   8910  O OH  . TYR C 1 333 ? -10.568 1.765   -17.453 1.00 55.29  ? 342  TYR C OH  1 
ATOM   8911  N N   . CYS C 1 334 ? -14.310 5.367   -10.831 1.00 46.01  ? 343  CYS C N   1 
ATOM   8912  C CA  . CYS C 1 334 ? -14.933 5.910   -9.674  1.00 45.77  ? 343  CYS C CA  1 
ATOM   8913  C C   . CYS C 1 334 ? -15.482 7.279   -10.065 1.00 44.72  ? 343  CYS C C   1 
ATOM   8914  O O   . CYS C 1 334 ? -14.762 8.057   -10.626 1.00 43.52  ? 343  CYS C O   1 
ATOM   8915  C CB  . CYS C 1 334 ? -13.809 5.933   -8.682  1.00 44.40  ? 343  CYS C CB  1 
ATOM   8916  S SG  . CYS C 1 334 ? -14.100 6.517   -7.117  1.00 46.33  ? 343  CYS C SG  1 
ATOM   8917  N N   . ASP C 1 335 ? -16.772 7.535   -9.845  1.00 45.89  ? 344  ASP C N   1 
ATOM   8918  C CA  . ASP C 1 335 ? -17.467 8.700   -10.422 1.00 45.72  ? 344  ASP C CA  1 
ATOM   8919  C C   . ASP C 1 335 ? -17.072 10.044  -9.833  1.00 43.78  ? 344  ASP C C   1 
ATOM   8920  O O   . ASP C 1 335 ? -17.021 10.195  -8.624  1.00 43.27  ? 344  ASP C O   1 
ATOM   8921  C CB  . ASP C 1 335 ? -18.958 8.591   -10.160 1.00 47.74  ? 344  ASP C CB  1 
ATOM   8922  C CG  . ASP C 1 335 ? -19.708 7.882   -11.234 1.00 51.29  ? 344  ASP C CG  1 
ATOM   8923  O OD1 . ASP C 1 335 ? -19.666 8.297   -12.426 1.00 53.60  ? 344  ASP C OD1 1 
ATOM   8924  O OD2 . ASP C 1 335 ? -20.405 6.922   -10.853 1.00 54.81  ? 344  ASP C OD2 1 
ATOM   8925  N N   . ASN C 1 336 ? -16.852 11.040  -10.680 1.00 43.02  ? 345  ASN C N   1 
ATOM   8926  C CA  . ASN C 1 336 ? -16.589 12.399  -10.210 1.00 41.83  ? 345  ASN C CA  1 
ATOM   8927  C C   . ASN C 1 336 ? -17.650 13.261  -10.761 1.00 42.84  ? 345  ASN C C   1 
ATOM   8928  O O   . ASN C 1 336 ? -18.642 12.727  -11.204 1.00 45.75  ? 345  ASN C O   1 
ATOM   8929  C CB  . ASN C 1 336 ? -15.275 12.915  -10.732 1.00 40.69  ? 345  ASN C CB  1 
ATOM   8930  C CG  . ASN C 1 336 ? -14.645 13.903  -9.800  1.00 38.42  ? 345  ASN C CG  1 
ATOM   8931  O OD1 . ASN C 1 336 ? -14.245 13.545  -8.723  1.00 35.40  ? 345  ASN C OD1 1 
ATOM   8932  N ND2 . ASN C 1 336 ? -14.552 15.150  -10.213 1.00 39.86  ? 345  ASN C ND2 1 
ATOM   8933  N N   . ALA C 1 337 ? -17.465 14.572  -10.796 1.00 41.40  ? 346  ALA C N   1 
ATOM   8934  C CA  . ALA C 1 337 ? -18.584 15.452  -11.137 1.00 42.25  ? 346  ALA C CA  1 
ATOM   8935  C C   . ALA C 1 337 ? -19.279 15.190  -12.512 1.00 43.69  ? 346  ALA C C   1 
ATOM   8936  O O   . ALA C 1 337 ? -19.048 15.859  -13.509 1.00 43.09  ? 346  ALA C O   1 
ATOM   8937  C CB  . ALA C 1 337 ? -18.191 16.861  -10.983 1.00 40.80  ? 346  ALA C CB  1 
ATOM   8938  N N   . GLY C 1 338 ? -20.156 14.194  -12.547 1.00 45.81  ? 347  GLY C N   1 
ATOM   8939  C CA  . GLY C 1 338 ? -20.886 13.870  -13.763 1.00 47.48  ? 347  GLY C CA  1 
ATOM   8940  C C   . GLY C 1 338 ? -20.066 13.209  -14.844 1.00 47.32  ? 347  GLY C C   1 
ATOM   8941  O O   . GLY C 1 338 ? -20.584 12.913  -15.952 1.00 49.25  ? 347  GLY C O   1 
ATOM   8942  N N   . SER C 1 339 ? -18.793 13.002  -14.522 1.00 45.30  ? 348  SER C N   1 
ATOM   8943  C CA  . SER C 1 339 ? -17.844 12.336  -15.382 1.00 44.38  ? 348  SER C CA  1 
ATOM   8944  C C   . SER C 1 339 ? -17.177 11.297  -14.517 1.00 44.18  ? 348  SER C C   1 
ATOM   8945  O O   . SER C 1 339 ? -17.527 11.167  -13.352 1.00 44.32  ? 348  SER C O   1 
ATOM   8946  C CB  . SER C 1 339 ? -16.873 13.344  -15.932 1.00 42.43  ? 348  SER C CB  1 
ATOM   8947  O OG  . SER C 1 339 ? -17.600 14.372  -16.561 1.00 42.17  ? 348  SER C OG  1 
ATOM   8948  N N   . VAL C 1 340 ? -16.263 10.521  -15.076 1.00 43.98  ? 349  VAL C N   1 
ATOM   8949  C CA  . VAL C 1 340 ? -15.664 9.430   -14.318 1.00 44.41  ? 349  VAL C CA  1 
ATOM   8950  C C   . VAL C 1 340 ? -14.161 9.559   -14.243 1.00 43.18  ? 349  VAL C C   1 
ATOM   8951  O O   . VAL C 1 340 ? -13.516 9.767   -15.260 1.00 43.09  ? 349  VAL C O   1 
ATOM   8952  C CB  . VAL C 1 340 ? -15.933 8.082   -14.953 1.00 46.04  ? 349  VAL C CB  1 
ATOM   8953  C CG1 . VAL C 1 340 ? -15.559 6.979   -13.994 1.00 46.47  ? 349  VAL C CG1 1 
ATOM   8954  C CG2 . VAL C 1 340 ? -17.352 7.962   -15.313 1.00 48.11  ? 349  VAL C CG2 1 
ATOM   8955  N N   . SER C 1 341 ? -13.603 9.400   -13.046 1.00 42.94  ? 350  SER C N   1 
ATOM   8956  C CA  . SER C 1 341 ? -12.156 9.487   -12.833 1.00 42.05  ? 350  SER C CA  1 
ATOM   8957  C C   . SER C 1 341 ? -11.504 8.103   -12.809 1.00 43.78  ? 350  SER C C   1 
ATOM   8958  O O   . SER C 1 341 ? -11.960 7.192   -12.118 1.00 44.86  ? 350  SER C O   1 
ATOM   8959  C CB  . SER C 1 341 ? -11.833 10.289  -11.562 1.00 40.10  ? 350  SER C CB  1 
ATOM   8960  O OG  . SER C 1 341 ? -12.085 11.669  -11.751 1.00 37.49  ? 350  SER C OG  1 
ATOM   8961  N N   . PHE C 1 342 ? -10.442 7.956   -13.582 1.00 44.41  ? 351  PHE C N   1 
ATOM   8962  C CA  . PHE C 1 342 ? -9.750  6.710   -13.672 1.00 46.52  ? 351  PHE C CA  1 
ATOM   8963  C C   . PHE C 1 342 ? -8.335  6.874   -13.139 1.00 46.54  ? 351  PHE C C   1 
ATOM   8964  O O   . PHE C 1 342 ? -7.650  7.860   -13.426 1.00 45.61  ? 351  PHE C O   1 
ATOM   8965  C CB  . PHE C 1 342 ? -9.763  6.276   -15.109 1.00 47.50  ? 351  PHE C CB  1 
ATOM   8966  C CG  . PHE C 1 342 ? -8.894  5.127   -15.398 1.00 48.99  ? 351  PHE C CG  1 
ATOM   8967  C CD1 . PHE C 1 342 ? -9.010  3.959   -14.699 1.00 51.03  ? 351  PHE C CD1 1 
ATOM   8968  C CD2 . PHE C 1 342 ? -7.963  5.203   -16.405 1.00 49.68  ? 351  PHE C CD2 1 
ATOM   8969  C CE1 . PHE C 1 342 ? -8.191  2.880   -14.993 1.00 53.10  ? 351  PHE C CE1 1 
ATOM   8970  C CE2 . PHE C 1 342 ? -7.154  4.131   -16.712 1.00 51.51  ? 351  PHE C CE2 1 
ATOM   8971  C CZ  . PHE C 1 342 ? -7.263  2.969   -16.003 1.00 53.10  ? 351  PHE C CZ  1 
ATOM   8972  N N   . PHE C 1 343 ? -7.907  5.907   -12.341 1.00 48.30  ? 352  PHE C N   1 
ATOM   8973  C CA  . PHE C 1 343 ? -6.603  5.940   -11.699 1.00 48.56  ? 352  PHE C CA  1 
ATOM   8974  C C   . PHE C 1 343 ? -5.846  4.715   -12.128 1.00 51.62  ? 352  PHE C C   1 
ATOM   8975  O O   . PHE C 1 343 ? -6.148  3.605   -11.676 1.00 53.12  ? 352  PHE C O   1 
ATOM   8976  C CB  . PHE C 1 343 ? -6.782  5.906   -10.202 1.00 47.75  ? 352  PHE C CB  1 
ATOM   8977  C CG  . PHE C 1 343 ? -7.907  6.765   -9.717  1.00 46.52  ? 352  PHE C CG  1 
ATOM   8978  C CD1 . PHE C 1 343 ? -9.193  6.319   -9.777  1.00 47.23  ? 352  PHE C CD1 1 
ATOM   8979  C CD2 . PHE C 1 343 ? -7.670  8.032   -9.208  1.00 44.27  ? 352  PHE C CD2 1 
ATOM   8980  C CE1 . PHE C 1 343 ? -10.205 7.112   -9.355  1.00 46.00  ? 352  PHE C CE1 1 
ATOM   8981  C CE2 . PHE C 1 343 ? -8.688  8.819   -8.776  1.00 42.34  ? 352  PHE C CE2 1 
ATOM   8982  C CZ  . PHE C 1 343 ? -9.950  8.360   -8.852  1.00 43.59  ? 352  PHE C CZ  1 
ATOM   8983  N N   . PRO C 1 344 ? -4.850  4.913   -12.996 1.00 53.08  ? 353  PRO C N   1 
ATOM   8984  C CA  . PRO C 1 344 ? -4.179  3.868   -13.770 1.00 56.28  ? 353  PRO C CA  1 
ATOM   8985  C C   . PRO C 1 344 ? -3.463  2.734   -12.967 1.00 59.05  ? 353  PRO C C   1 
ATOM   8986  O O   . PRO C 1 344 ? -3.505  1.566   -13.397 1.00 61.44  ? 353  PRO C O   1 
ATOM   8987  C CB  . PRO C 1 344 ? -3.201  4.669   -14.625 1.00 55.35  ? 353  PRO C CB  1 
ATOM   8988  C CG  . PRO C 1 344 ? -3.796  6.069   -14.634 1.00 52.82  ? 353  PRO C CG  1 
ATOM   8989  C CD  . PRO C 1 344 ? -4.280  6.239   -13.268 1.00 51.25  ? 353  PRO C CD  1 
ATOM   8990  N N   . GLN C 1 345 ? -2.850  3.051   -11.817 1.00 59.52  ? 354  GLN C N   1 
ATOM   8991  C CA  . GLN C 1 345 ? -2.082  2.032   -11.037 1.00 61.76  ? 354  GLN C CA  1 
ATOM   8992  C C   . GLN C 1 345 ? -2.310  2.009   -9.502  1.00 61.47  ? 354  GLN C C   1 
ATOM   8993  O O   . GLN C 1 345 ? -2.357  3.089   -8.869  1.00 59.47  ? 354  GLN C O   1 
ATOM   8994  C CB  . GLN C 1 345 ? -0.577  2.109   -11.381 1.00 61.86  ? 354  GLN C CB  1 
ATOM   8995  C CG  . GLN C 1 345 ? -0.096  3.501   -11.857 1.00 60.96  ? 354  GLN C CG  1 
ATOM   8996  C CD  . GLN C 1 345 ? -0.430  4.589   -10.835 1.00 59.05  ? 354  GLN C CD  1 
ATOM   8997  O OE1 . GLN C 1 345 ? 0.005   4.514   -9.678  1.00 58.85  ? 354  GLN C OE1 1 
ATOM   8998  N NE2 . GLN C 1 345 ? -1.234  5.581   -11.250 1.00 56.50  ? 354  GLN C NE2 1 
ATOM   8999  N N   . ALA C 1 346 ? -2.448  0.777   -8.949  1.00 63.50  ? 355  ALA C N   1 
ATOM   9000  C CA  . ALA C 1 346 ? -2.742  0.469   -7.492  1.00 63.39  ? 355  ALA C CA  1 
ATOM   9001  C C   . ALA C 1 346 ? -2.437  1.641   -6.525  1.00 60.78  ? 355  ALA C C   1 
ATOM   9002  O O   . ALA C 1 346 ? -3.352  2.347   -6.052  1.00 60.37  ? 355  ALA C O   1 
ATOM   9003  C CB  . ALA C 1 346 ? -2.005  -0.847  -7.021  1.00 64.57  ? 355  ALA C CB  1 
ATOM   9004  N N   . GLU C 1 347 ? -1.145  1.788   -6.229  1.00 58.60  ? 356  GLU C N   1 
ATOM   9005  C CA  . GLU C 1 347 ? -0.512  3.045   -5.855  1.00 55.07  ? 356  GLU C CA  1 
ATOM   9006  C C   . GLU C 1 347 ? -1.435  4.139   -5.427  1.00 52.07  ? 356  GLU C C   1 
ATOM   9007  O O   . GLU C 1 347 ? -1.543  4.461   -4.246  1.00 51.08  ? 356  GLU C O   1 
ATOM   9008  C CB  . GLU C 1 347 ? 0.330   3.524   -7.054  1.00 55.47  ? 356  GLU C CB  1 
ATOM   9009  C CG  . GLU C 1 347 ? 1.529   2.625   -7.302  1.00 59.40  ? 356  GLU C CG  1 
ATOM   9010  C CD  . GLU C 1 347 ? 2.033   2.037   -5.953  1.00 64.65  ? 356  GLU C CD  1 
ATOM   9011  O OE1 . GLU C 1 347 ? 1.820   0.808   -5.737  1.00 68.32  ? 356  GLU C OE1 1 
ATOM   9012  O OE2 . GLU C 1 347 ? 2.573   2.806   -5.092  1.00 64.06  ? 356  GLU C OE2 1 
ATOM   9013  N N   . THR C 1 348 ? -2.105  4.693   -6.421  1.00 50.11  ? 357  THR C N   1 
ATOM   9014  C CA  . THR C 1 348 ? -2.971  5.818   -6.240  1.00 47.45  ? 357  THR C CA  1 
ATOM   9015  C C   . THR C 1 348 ? -4.141  5.533   -5.317  1.00 46.70  ? 357  THR C C   1 
ATOM   9016  O O   . THR C 1 348 ? -4.657  6.468   -4.705  1.00 46.23  ? 357  THR C O   1 
ATOM   9017  C CB  . THR C 1 348 ? -3.547  6.271   -7.578  1.00 47.79  ? 357  THR C CB  1 
ATOM   9018  O OG1 . THR C 1 348 ? -2.874  5.606   -8.667  1.00 48.82  ? 357  THR C OG1 1 
ATOM   9019  C CG2 . THR C 1 348 ? -3.433  7.800   -7.695  1.00 46.46  ? 357  THR C CG2 1 
ATOM   9020  N N   . CYS C 1 349 ? -4.561  4.268   -5.216  1.00 46.26  ? 358  CYS C N   1 
ATOM   9021  C CA  . CYS C 1 349 ? -5.772  3.908   -4.460  1.00 45.15  ? 358  CYS C CA  1 
ATOM   9022  C C   . CYS C 1 349 ? -5.538  2.933   -3.329  1.00 44.58  ? 358  CYS C C   1 
ATOM   9023  O O   . CYS C 1 349 ? -4.791  1.984   -3.487  1.00 45.11  ? 358  CYS C O   1 
ATOM   9024  C CB  . CYS C 1 349 ? -6.817  3.311   -5.398  1.00 46.58  ? 358  CYS C CB  1 
ATOM   9025  S SG  . CYS C 1 349 ? -7.482  4.442   -6.643  1.00 46.74  ? 358  CYS C SG  1 
ATOM   9026  N N   . LYS C 1 350 ? -6.177  3.173   -2.190  1.00 43.53  ? 359  LYS C N   1 
ATOM   9027  C CA  . LYS C 1 350 ? -6.273  2.151   -1.126  1.00 44.47  ? 359  LYS C CA  1 
ATOM   9028  C C   . LYS C 1 350 ? -7.678  2.030   -0.627  1.00 45.10  ? 359  LYS C C   1 
ATOM   9029  O O   . LYS C 1 350 ? -8.442  3.013   -0.658  1.00 44.73  ? 359  LYS C O   1 
ATOM   9030  C CB  . LYS C 1 350 ? -5.366  2.399   0.074   1.00 43.48  ? 359  LYS C CB  1 
ATOM   9031  C CG  . LYS C 1 350 ? -4.955  3.810   0.269   1.00 43.38  ? 359  LYS C CG  1 
ATOM   9032  C CD  . LYS C 1 350 ? -3.482  3.831   0.487   1.00 44.75  ? 359  LYS C CD  1 
ATOM   9033  C CE  . LYS C 1 350 ? -2.952  5.139   0.024   1.00 45.28  ? 359  LYS C CE  1 
ATOM   9034  N NZ  . LYS C 1 350 ? -1.502  5.008   -0.021  1.00 48.71  ? 359  LYS C NZ  1 
ATOM   9035  N N   . VAL C 1 351 ? -7.994  0.833   -0.126  1.00 46.20  ? 360  VAL C N   1 
ATOM   9036  C CA  . VAL C 1 351 ? -9.369  0.423   0.052   1.00 47.13  ? 360  VAL C CA  1 
ATOM   9037  C C   . VAL C 1 351 ? -9.538  -0.394  1.334   1.00 48.27  ? 360  VAL C C   1 
ATOM   9038  O O   . VAL C 1 351 ? -8.709  -1.228  1.632   1.00 48.48  ? 360  VAL C O   1 
ATOM   9039  C CB  . VAL C 1 351 ? -9.768  -0.346  -1.153  1.00 48.19  ? 360  VAL C CB  1 
ATOM   9040  C CG1 . VAL C 1 351 ? -8.735  -1.392  -1.432  1.00 49.20  ? 360  VAL C CG1 1 
ATOM   9041  C CG2 . VAL C 1 351 ? -11.048 -0.952  -0.916  1.00 50.94  ? 360  VAL C CG2 1 
ATOM   9042  N N   . GLN C 1 352 ? -10.607 -0.118  2.084   1.00 49.32  ? 361  GLN C N   1 
ATOM   9043  C CA  . GLN C 1 352 ? -10.867 -0.693  3.415   1.00 51.39  ? 361  GLN C CA  1 
ATOM   9044  C C   . GLN C 1 352 ? -12.321 -1.072  3.535   1.00 53.23  ? 361  GLN C C   1 
ATOM   9045  O O   . GLN C 1 352 ? -13.169 -0.214  3.802   1.00 53.40  ? 361  GLN C O   1 
ATOM   9046  C CB  . GLN C 1 352 ? -10.593 0.331   4.495   1.00 50.08  ? 361  GLN C CB  1 
ATOM   9047  C CG  . GLN C 1 352 ? -10.708 -0.150  5.942   1.00 55.71  ? 361  GLN C CG  1 
ATOM   9048  C CD  . GLN C 1 352 ? -9.371  0.171   6.728   1.00 63.00  ? 361  GLN C CD  1 
ATOM   9049  O OE1 . GLN C 1 352 ? -9.263  1.175   7.479   1.00 64.64  ? 361  GLN C OE1 1 
ATOM   9050  N NE2 . GLN C 1 352 ? -8.337  -0.671  6.508   1.00 65.36  ? 361  GLN C NE2 1 
ATOM   9051  N N   . SER C 1 353 ? -12.605 -2.365  3.371   1.00 55.21  ? 362  SER C N   1 
ATOM   9052  C CA  . SER C 1 353 ? -13.970 -2.860  3.261   1.00 56.76  ? 362  SER C CA  1 
ATOM   9053  C C   . SER C 1 353 ? -14.463 -2.288  1.956   1.00 55.87  ? 362  SER C C   1 
ATOM   9054  O O   . SER C 1 353 ? -13.797 -2.462  0.935   1.00 55.35  ? 362  SER C O   1 
ATOM   9055  C CB  . SER C 1 353 ? -14.826 -2.416  4.454   1.00 57.10  ? 362  SER C CB  1 
ATOM   9056  O OG  . SER C 1 353 ? -16.075 -3.065  4.452   1.00 60.34  ? 362  SER C OG  1 
ATOM   9057  N N   . ASN C 1 354 ? -15.589 -1.585  1.989   1.00 55.57  ? 363  ASN C N   1 
ATOM   9058  C CA  . ASN C 1 354 ? -16.183 -1.038  0.769   1.00 55.17  ? 363  ASN C CA  1 
ATOM   9059  C C   . ASN C 1 354 ? -15.869 0.425   0.623   1.00 51.94  ? 363  ASN C C   1 
ATOM   9060  O O   . ASN C 1 354 ? -16.528 1.149   -0.141  1.00 51.59  ? 363  ASN C O   1 
ATOM   9061  C CB  . ASN C 1 354 ? -17.689 -1.211  0.764   1.00 57.57  ? 363  ASN C CB  1 
ATOM   9062  C CG  . ASN C 1 354 ? -18.358 -0.420  1.858   1.00 57.61  ? 363  ASN C CG  1 
ATOM   9063  O OD1 . ASN C 1 354 ? -17.708 0.001   2.827   1.00 56.05  ? 363  ASN C OD1 1 
ATOM   9064  N ND2 . ASN C 1 354 ? -19.665 -0.216  1.722   1.00 59.99  ? 363  ASN C ND2 1 
ATOM   9065  N N   . ARG C 1 355 ? -14.855 0.843   1.365   1.00 49.21  ? 364  ARG C N   1 
ATOM   9066  C CA  . ARG C 1 355 ? -14.386 2.192   1.292   1.00 46.58  ? 364  ARG C CA  1 
ATOM   9067  C C   . ARG C 1 355 ? -13.088 2.376   0.486   1.00 44.81  ? 364  ARG C C   1 
ATOM   9068  O O   . ARG C 1 355 ? -12.093 1.677   0.701   1.00 44.57  ? 364  ARG C O   1 
ATOM   9069  C CB  . ARG C 1 355 ? -14.188 2.657   2.689   1.00 45.69  ? 364  ARG C CB  1 
ATOM   9070  C CG  . ARG C 1 355 ? -14.535 4.058   2.821   1.00 45.18  ? 364  ARG C CG  1 
ATOM   9071  C CD  . ARG C 1 355 ? -15.996 4.219   2.671   1.00 46.43  ? 364  ARG C CD  1 
ATOM   9072  N NE  . ARG C 1 355 ? -16.219 5.401   1.863   1.00 46.68  ? 364  ARG C NE  1 
ATOM   9073  C CZ  . ARG C 1 355 ? -17.323 6.121   1.909   1.00 47.28  ? 364  ARG C CZ  1 
ATOM   9074  N NH1 . ARG C 1 355 ? -18.289 5.771   2.719   1.00 48.89  ? 364  ARG C NH1 1 
ATOM   9075  N NH2 . ARG C 1 355 ? -17.461 7.182   1.144   1.00 47.63  ? 364  ARG C NH2 1 
ATOM   9076  N N   . VAL C 1 356 ? -13.104 3.310   -0.455  1.00 43.67  ? 365  VAL C N   1 
ATOM   9077  C CA  . VAL C 1 356 ? -11.975 3.474   -1.355  1.00 42.32  ? 365  VAL C CA  1 
ATOM   9078  C C   . VAL C 1 356 ? -11.477 4.886   -1.258  1.00 40.85  ? 365  VAL C C   1 
ATOM   9079  O O   . VAL C 1 356 ? -12.257 5.821   -1.013  1.00 41.45  ? 365  VAL C O   1 
ATOM   9080  C CB  . VAL C 1 356 ? -12.368 3.231   -2.774  1.00 42.69  ? 365  VAL C CB  1 
ATOM   9081  C CG1 . VAL C 1 356 ? -11.360 3.794   -3.664  1.00 40.94  ? 365  VAL C CG1 1 
ATOM   9082  C CG2 . VAL C 1 356 ? -12.383 1.815   -3.004  1.00 45.02  ? 365  VAL C CG2 1 
ATOM   9083  N N   . PHE C 1 357 ? -10.174 5.040   -1.446  1.00 39.44  ? 366  PHE C N   1 
ATOM   9084  C CA  . PHE C 1 357 ? -9.537  6.304   -1.283  1.00 37.42  ? 366  PHE C CA  1 
ATOM   9085  C C   . PHE C 1 357 ? -8.536  6.457   -2.398  1.00 37.09  ? 366  PHE C C   1 
ATOM   9086  O O   . PHE C 1 357 ? -7.534  5.746   -2.433  1.00 36.99  ? 366  PHE C O   1 
ATOM   9087  C CB  . PHE C 1 357 ? -8.814  6.305   0.042   1.00 36.49  ? 366  PHE C CB  1 
ATOM   9088  C CG  . PHE C 1 357 ? -9.716  6.267   1.232   1.00 36.67  ? 366  PHE C CG  1 
ATOM   9089  C CD1 . PHE C 1 357 ? -10.236 5.072   1.681   1.00 38.56  ? 366  PHE C CD1 1 
ATOM   9090  C CD2 . PHE C 1 357 ? -10.015 7.422   1.937   1.00 34.96  ? 366  PHE C CD2 1 
ATOM   9091  C CE1 . PHE C 1 357 ? -11.069 5.028   2.785   1.00 38.17  ? 366  PHE C CE1 1 
ATOM   9092  C CE2 . PHE C 1 357 ? -10.841 7.376   3.043   1.00 34.69  ? 366  PHE C CE2 1 
ATOM   9093  C CZ  . PHE C 1 357 ? -11.362 6.170   3.463   1.00 36.09  ? 366  PHE C CZ  1 
ATOM   9094  N N   . CYS C 1 358 ? -8.808  7.370   -3.319  1.00 37.17  ? 367  CYS C N   1 
ATOM   9095  C CA  . CYS C 1 358 ? -7.897  7.581   -4.414  1.00 37.59  ? 367  CYS C CA  1 
ATOM   9096  C C   . CYS C 1 358 ? -7.375  8.989   -4.472  1.00 36.37  ? 367  CYS C C   1 
ATOM   9097  O O   . CYS C 1 358 ? -7.903  9.869   -3.784  1.00 36.18  ? 367  CYS C O   1 
ATOM   9098  C CB  . CYS C 1 358 ? -8.550  7.191   -5.718  1.00 38.84  ? 367  CYS C CB  1 
ATOM   9099  S SG  . CYS C 1 358 ? -8.967  5.483   -5.688  1.00 42.28  ? 367  CYS C SG  1 
ATOM   9100  N N   . ASP C 1 359 ? -6.340  9.186   -5.294  1.00 36.02  ? 368  ASP C N   1 
ATOM   9101  C CA  . ASP C 1 359 ? -5.691  10.465  -5.422  1.00 35.26  ? 368  ASP C CA  1 
ATOM   9102  C C   . ASP C 1 359 ? -5.951  11.046  -6.777  1.00 36.04  ? 368  ASP C C   1 
ATOM   9103  O O   . ASP C 1 359 ? -5.503  10.487  -7.773  1.00 36.87  ? 368  ASP C O   1 
ATOM   9104  C CB  . ASP C 1 359 ? -4.185  10.311  -5.223  1.00 34.76  ? 368  ASP C CB  1 
ATOM   9105  C CG  . ASP C 1 359 ? -3.533  11.601  -4.795  1.00 33.93  ? 368  ASP C CG  1 
ATOM   9106  O OD1 . ASP C 1 359 ? -3.698  12.599  -5.515  1.00 34.25  ? 368  ASP C OD1 1 
ATOM   9107  O OD2 . ASP C 1 359 ? -2.898  11.639  -3.717  1.00 33.77  ? 368  ASP C OD2 1 
ATOM   9108  N N   . THR C 1 360 ? -6.664  12.168  -6.819  1.00 36.49  ? 369  THR C N   1 
ATOM   9109  C CA  . THR C 1 360 ? -6.859  12.892  -8.062  1.00 37.33  ? 369  THR C CA  1 
ATOM   9110  C C   . THR C 1 360 ? -5.549  13.053  -8.799  1.00 38.14  ? 369  THR C C   1 
ATOM   9111  O O   . THR C 1 360 ? -5.388  12.496  -9.868  1.00 39.68  ? 369  THR C O   1 
ATOM   9112  C CB  . THR C 1 360 ? -7.385  14.253  -7.817  1.00 36.25  ? 369  THR C CB  1 
ATOM   9113  O OG1 . THR C 1 360 ? -8.611  14.116  -7.129  1.00 35.48  ? 369  THR C OG1 1 
ATOM   9114  C CG2 . THR C 1 360 ? -7.636  14.948  -9.130  1.00 37.21  ? 369  THR C CG2 1 
ATOM   9115  N N   . MET C 1 361 ? -4.608  13.784  -8.213  1.00 38.32  ? 370  MET C N   1 
ATOM   9116  C CA  . MET C 1 361 ? -3.302  14.080  -8.839  1.00 39.07  ? 370  MET C CA  1 
ATOM   9117  C C   . MET C 1 361 ? -3.039  13.620  -10.257 1.00 39.43  ? 370  MET C C   1 
ATOM   9118  O O   . MET C 1 361 ? -2.932  14.443  -11.183 1.00 39.36  ? 370  MET C O   1 
ATOM   9119  C CB  . MET C 1 361 ? -2.113  13.713  -7.941  1.00 39.60  ? 370  MET C CB  1 
ATOM   9120  C CG  . MET C 1 361 ? -1.450  14.981  -7.277  1.00 42.10  ? 370  MET C CG  1 
ATOM   9121  S SD  . MET C 1 361 ? -0.902  16.327  -8.437  1.00 49.06  ? 370  MET C SD  1 
ATOM   9122  C CE  . MET C 1 361 ? -2.406  16.997  -9.207  1.00 46.61  ? 370  MET C CE  1 
ATOM   9123  N N   . ASN C 1 362 ? -2.926  12.324  -10.464 1.00 39.89  ? 371  ASN C N   1 
ATOM   9124  C CA  . ASN C 1 362 ? -2.733  11.983  -11.838 1.00 40.56  ? 371  ASN C CA  1 
ATOM   9125  C C   . ASN C 1 362 ? -3.882  11.363  -12.608 1.00 41.28  ? 371  ASN C C   1 
ATOM   9126  O O   . ASN C 1 362 ? -3.714  11.001  -13.757 1.00 42.56  ? 371  ASN C O   1 
ATOM   9127  C CB  . ASN C 1 362 ? -1.391  11.296  -12.055 1.00 41.51  ? 371  ASN C CB  1 
ATOM   9128  C CG  . ASN C 1 362 ? -0.257  12.293  -12.274 1.00 40.94  ? 371  ASN C CG  1 
ATOM   9129  O OD1 . ASN C 1 362 ? -0.054  12.805  -13.383 1.00 40.91  ? 371  ASN C OD1 1 
ATOM   9130  N ND2 . ASN C 1 362 ? 0.495   12.556  -11.220 1.00 41.16  ? 371  ASN C ND2 1 
ATOM   9131  N N   . SER C 1 363 ? -5.045  11.246  -11.991 1.00 40.77  ? 372  SER C N   1 
ATOM   9132  C CA  . SER C 1 363 ? -6.266  10.756  -12.652 1.00 41.07  ? 372  SER C CA  1 
ATOM   9133  C C   . SER C 1 363 ? -6.556  11.259  -14.072 1.00 40.67  ? 372  SER C C   1 
ATOM   9134  O O   . SER C 1 363 ? -6.185  12.378  -14.477 1.00 39.58  ? 372  SER C O   1 
ATOM   9135  C CB  . SER C 1 363 ? -7.474  11.117  -11.801 1.00 41.12  ? 372  SER C CB  1 
ATOM   9136  O OG  . SER C 1 363 ? -7.505  12.525  -11.579 1.00 40.73  ? 372  SER C OG  1 
ATOM   9137  N N   . LEU C 1 364 ? -7.275  10.414  -14.799 1.00 41.20  ? 373  LEU C N   1 
ATOM   9138  C CA  . LEU C 1 364 ? -7.758  10.714  -16.132 1.00 40.96  ? 373  LEU C CA  1 
ATOM   9139  C C   . LEU C 1 364 ? -9.244  10.815  -16.056 1.00 41.28  ? 373  LEU C C   1 
ATOM   9140  O O   . LEU C 1 364 ? -9.890  9.914   -15.510 1.00 42.48  ? 373  LEU C O   1 
ATOM   9141  C CB  . LEU C 1 364 ? -7.415  9.574   -17.086 1.00 42.25  ? 373  LEU C CB  1 
ATOM   9142  C CG  . LEU C 1 364 ? -6.250  9.780   -18.051 1.00 41.90  ? 373  LEU C CG  1 
ATOM   9143  C CD1 . LEU C 1 364 ? -5.170  10.742  -17.454 1.00 41.32  ? 373  LEU C CD1 1 
ATOM   9144  C CD2 . LEU C 1 364 ? -5.656  8.436   -18.426 1.00 42.66  ? 373  LEU C CD2 1 
ATOM   9145  N N   . THR C 1 365 ? -9.803  11.887  -16.616 1.00 40.27  ? 374  THR C N   1 
ATOM   9146  C CA  . THR C 1 365 ? -11.257 12.127  -16.523 1.00 40.07  ? 374  THR C CA  1 
ATOM   9147  C C   . THR C 1 365 ? -11.902 11.645  -17.760 1.00 40.59  ? 374  THR C C   1 
ATOM   9148  O O   . THR C 1 365 ? -11.465 11.976  -18.831 1.00 40.96  ? 374  THR C O   1 
ATOM   9149  C CB  . THR C 1 365 ? -11.555 13.584  -16.368 1.00 38.93  ? 374  THR C CB  1 
ATOM   9150  O OG1 . THR C 1 365 ? -10.433 14.187  -15.702 1.00 39.64  ? 374  THR C OG1 1 
ATOM   9151  C CG2 . THR C 1 365 ? -12.766 13.770  -15.535 1.00 38.90  ? 374  THR C CG2 1 
ATOM   9152  N N   . LEU C 1 366 ? -12.931 10.839  -17.612 1.00 41.15  ? 375  LEU C N   1 
ATOM   9153  C CA  . LEU C 1 366 ? -13.526 10.129  -18.731 1.00 41.90  ? 375  LEU C CA  1 
ATOM   9154  C C   . LEU C 1 366 ? -15.036 10.183  -18.664 1.00 43.17  ? 375  LEU C C   1 
ATOM   9155  O O   . LEU C 1 366 ? -15.592 10.392  -17.583 1.00 43.19  ? 375  LEU C O   1 
ATOM   9156  C CB  . LEU C 1 366 ? -13.134 8.670   -18.664 1.00 42.53  ? 375  LEU C CB  1 
ATOM   9157  C CG  . LEU C 1 366 ? -11.689 8.305   -18.550 1.00 39.59  ? 375  LEU C CG  1 
ATOM   9158  C CD1 . LEU C 1 366 ? -11.636 6.837   -18.272 1.00 37.94  ? 375  LEU C CD1 1 
ATOM   9159  C CD2 . LEU C 1 366 ? -11.043 8.680   -19.874 1.00 39.21  ? 375  LEU C CD2 1 
ATOM   9160  N N   . PRO C 1 367 ? -15.711 9.960   -19.801 1.00 44.41  ? 376  PRO C N   1 
ATOM   9161  C CA  . PRO C 1 367 ? -17.144 9.986   -19.840 1.00 46.11  ? 376  PRO C CA  1 
ATOM   9162  C C   . PRO C 1 367 ? -17.740 8.675   -19.382 1.00 48.44  ? 376  PRO C C   1 
ATOM   9163  O O   . PRO C 1 367 ? -17.137 7.632   -19.590 1.00 49.33  ? 376  PRO C O   1 
ATOM   9164  C CB  . PRO C 1 367 ? -17.434 10.189  -21.322 1.00 46.65  ? 376  PRO C CB  1 
ATOM   9165  C CG  . PRO C 1 367 ? -16.362 9.552   -21.977 1.00 46.71  ? 376  PRO C CG  1 
ATOM   9166  C CD  . PRO C 1 367 ? -15.159 9.763   -21.142 1.00 44.88  ? 376  PRO C CD  1 
ATOM   9167  N N   . SER C 1 368 ? -18.926 8.743   -18.779 1.00 49.85  ? 377  SER C N   1 
ATOM   9168  C CA  . SER C 1 368 ? -19.696 7.569   -18.407 1.00 52.74  ? 377  SER C CA  1 
ATOM   9169  C C   . SER C 1 368 ? -19.679 6.533   -19.560 1.00 54.89  ? 377  SER C C   1 
ATOM   9170  O O   . SER C 1 368 ? -19.709 5.332   -19.354 1.00 56.48  ? 377  SER C O   1 
ATOM   9171  C CB  . SER C 1 368 ? -21.145 7.984   -18.045 1.00 54.01  ? 377  SER C CB  1 
ATOM   9172  O OG  . SER C 1 368 ? -21.260 9.317   -17.537 1.00 53.33  ? 377  SER C OG  1 
ATOM   9173  N N   . GLU C 1 369 ? -19.588 7.017   -20.786 1.00 55.28  ? 378  GLU C N   1 
ATOM   9174  C CA  . GLU C 1 369 ? -19.650 6.170   -21.952 1.00 57.65  ? 378  GLU C CA  1 
ATOM   9175  C C   . GLU C 1 369 ? -18.602 5.110   -21.882 1.00 57.93  ? 378  GLU C C   1 
ATOM   9176  O O   . GLU C 1 369 ? -18.713 4.118   -22.531 1.00 59.93  ? 378  GLU C O   1 
ATOM   9177  C CB  . GLU C 1 369 ? -19.502 7.007   -23.223 1.00 57.35  ? 378  GLU C CB  1 
ATOM   9178  C CG  . GLU C 1 369 ? -20.793 7.703   -23.710 1.00 60.22  ? 378  GLU C CG  1 
ATOM   9179  C CD  . GLU C 1 369 ? -21.383 8.755   -22.735 1.00 62.70  ? 378  GLU C CD  1 
ATOM   9180  O OE1 . GLU C 1 369 ? -20.673 9.229   -21.801 1.00 60.79  ? 378  GLU C OE1 1 
ATOM   9181  O OE2 . GLU C 1 369 ? -22.581 9.117   -22.924 1.00 65.72  ? 378  GLU C OE2 1 
ATOM   9182  N N   . VAL C 1 370 ? -17.588 5.315   -21.068 1.00 56.57  ? 379  VAL C N   1 
ATOM   9183  C CA  . VAL C 1 370 ? -16.547 4.322   -20.891 1.00 57.32  ? 379  VAL C CA  1 
ATOM   9184  C C   . VAL C 1 370 ? -17.121 2.987   -20.533 1.00 60.16  ? 379  VAL C C   1 
ATOM   9185  O O   . VAL C 1 370 ? -16.576 1.964   -20.917 1.00 61.62  ? 379  VAL C O   1 
ATOM   9186  C CB  . VAL C 1 370 ? -15.628 4.689   -19.750 1.00 55.23  ? 379  VAL C CB  1 
ATOM   9187  C CG1 . VAL C 1 370 ? -15.100 3.446   -19.068 1.00 56.45  ? 379  VAL C CG1 1 
ATOM   9188  C CG2 . VAL C 1 370 ? -14.517 5.512   -20.243 1.00 53.66  ? 379  VAL C CG2 1 
ATOM   9189  N N   . ASN C 1 371 ? -18.206 2.998   -19.777 1.00 61.52  ? 380  ASN C N   1 
ATOM   9190  C CA  . ASN C 1 371 ? -18.784 1.770   -19.284 1.00 64.83  ? 380  ASN C CA  1 
ATOM   9191  C C   . ASN C 1 371 ? -19.231 0.812   -20.382 1.00 67.36  ? 380  ASN C C   1 
ATOM   9192  O O   . ASN C 1 371 ? -19.108 -0.388  -20.230 1.00 69.51  ? 380  ASN C O   1 
ATOM   9193  C CB  . ASN C 1 371 ? -19.935 2.079   -18.339 1.00 65.89  ? 380  ASN C CB  1 
ATOM   9194  C CG  . ASN C 1 371 ? -19.468 2.804   -17.086 1.00 66.12  ? 380  ASN C CG  1 
ATOM   9195  O OD1 . ASN C 1 371 ? -19.212 2.177   -16.068 1.00 69.48  ? 380  ASN C OD1 1 
ATOM   9196  N ND2 . ASN C 1 371 ? -19.335 4.128   -17.162 1.00 66.12  ? 380  ASN C ND2 1 
ATOM   9197  N N   . LEU C 1 372 ? -19.715 1.325   -21.502 1.00 67.35  ? 381  LEU C N   1 
ATOM   9198  C CA  . LEU C 1 372 ? -20.182 0.452   -22.559 1.00 69.83  ? 381  LEU C CA  1 
ATOM   9199  C C   . LEU C 1 372 ? -19.059 -0.428  -22.991 1.00 70.33  ? 381  LEU C C   1 
ATOM   9200  O O   . LEU C 1 372 ? -19.249 -1.455  -23.578 1.00 73.15  ? 381  LEU C O   1 
ATOM   9201  C CB  . LEU C 1 372 ? -20.659 1.256   -23.743 1.00 69.70  ? 381  LEU C CB  1 
ATOM   9202  C CG  . LEU C 1 372 ? -21.304 2.590   -23.398 1.00 68.90  ? 381  LEU C CG  1 
ATOM   9203  C CD1 . LEU C 1 372 ? -21.465 3.392   -24.672 1.00 68.95  ? 381  LEU C CD1 1 
ATOM   9204  C CD2 . LEU C 1 372 ? -22.643 2.464   -22.583 1.00 71.14  ? 381  LEU C CD2 1 
ATOM   9205  N N   . CYS C 1 373 ? -17.858 -0.029  -22.678 1.00 68.19  ? 382  CYS C N   1 
ATOM   9206  C CA  . CYS C 1 373 ? -16.731 -0.834  -23.037 1.00 68.99  ? 382  CYS C CA  1 
ATOM   9207  C C   . CYS C 1 373 ? -16.707 -2.186  -22.308 1.00 70.78  ? 382  CYS C C   1 
ATOM   9208  O O   . CYS C 1 373 ? -16.070 -3.132  -22.756 1.00 72.31  ? 382  CYS C O   1 
ATOM   9209  C CB  . CYS C 1 373 ? -15.454 -0.023  -22.841 1.00 66.41  ? 382  CYS C CB  1 
ATOM   9210  S SG  . CYS C 1 373 ? -14.987 0.960   -24.327 1.00 67.09  ? 382  CYS C SG  1 
ATOM   9211  N N   . ASN C 1 374 ? -17.435 -2.293  -21.209 1.00 70.90  ? 383  ASN C N   1 
ATOM   9212  C CA  . ASN C 1 374 ? -17.481 -3.544  -20.465 1.00 73.04  ? 383  ASN C CA  1 
ATOM   9213  C C   . ASN C 1 374 ? -18.283 -4.578  -21.187 1.00 76.42  ? 383  ASN C C   1 
ATOM   9214  O O   . ASN C 1 374 ? -18.134 -5.768  -20.956 1.00 78.73  ? 383  ASN C O   1 
ATOM   9215  C CB  . ASN C 1 374 ? -18.139 -3.335  -19.113 1.00 72.63  ? 383  ASN C CB  1 
ATOM   9216  C CG  . ASN C 1 374 ? -17.447 -2.284  -18.292 1.00 70.15  ? 383  ASN C CG  1 
ATOM   9217  O OD1 . ASN C 1 374 ? -16.218 -2.271  -18.192 1.00 69.79  ? 383  ASN C OD1 1 
ATOM   9218  N ND2 . ASN C 1 374 ? -18.227 -1.389  -17.692 1.00 70.24  ? 383  ASN C ND2 1 
ATOM   9219  N N   . VAL C 1 375 ? -19.168 -4.098  -22.040 1.00 77.06  ? 384  VAL C N   1 
ATOM   9220  C CA  . VAL C 1 375 ? -20.082 -4.937  -22.781 1.00 80.33  ? 384  VAL C CA  1 
ATOM   9221  C C   . VAL C 1 375 ? -19.569 -5.146  -24.207 1.00 81.47  ? 384  VAL C C   1 
ATOM   9222  O O   . VAL C 1 375 ? -19.611 -6.262  -24.713 1.00 84.14  ? 384  VAL C O   1 
ATOM   9223  C CB  . VAL C 1 375 ? -21.514 -4.311  -22.785 1.00 80.56  ? 384  VAL C CB  1 
ATOM   9224  C CG1 . VAL C 1 375 ? -22.385 -4.880  -23.893 1.00 83.75  ? 384  VAL C CG1 1 
ATOM   9225  C CG2 . VAL C 1 375 ? -22.179 -4.463  -21.417 1.00 80.36  ? 384  VAL C CG2 1 
ATOM   9226  N N   . ASP C 1 376 ? -19.051 -4.097  -24.846 1.00 79.72  ? 385  ASP C N   1 
ATOM   9227  C CA  . ASP C 1 376 ? -18.868 -4.162  -26.295 1.00 81.29  ? 385  ASP C CA  1 
ATOM   9228  C C   . ASP C 1 376 ? -17.488 -3.972  -26.906 1.00 80.02  ? 385  ASP C C   1 
ATOM   9229  O O   . ASP C 1 376 ? -17.125 -4.705  -27.809 1.00 82.05  ? 385  ASP C O   1 
ATOM   9230  C CB  . ASP C 1 376 ? -19.903 -3.313  -27.026 1.00 81.43  ? 385  ASP C CB  1 
ATOM   9231  C CG  . ASP C 1 376 ? -20.455 -4.012  -28.245 1.00 85.87  ? 385  ASP C CG  1 
ATOM   9232  O OD1 . ASP C 1 376 ? -19.846 -5.004  -28.692 1.00 89.09  ? 385  ASP C OD1 1 
ATOM   9233  O OD2 . ASP C 1 376 ? -21.496 -3.572  -28.762 1.00 88.93  ? 385  ASP C OD2 1 
ATOM   9234  N N   . ILE C 1 377 ? -16.730 -2.980  -26.460 1.00 77.04  ? 386  ILE C N   1 
ATOM   9235  C CA  . ILE C 1 377 ? -15.377 -2.749  -27.023 1.00 75.95  ? 386  ILE C CA  1 
ATOM   9236  C C   . ILE C 1 377 ? -15.485 -1.990  -28.336 1.00 76.05  ? 386  ILE C C   1 
ATOM   9237  O O   . ILE C 1 377 ? -14.967 -0.858  -28.502 1.00 73.75  ? 386  ILE C O   1 
ATOM   9238  C CB  . ILE C 1 377 ? -14.646 -4.080  -27.325 1.00 77.85  ? 386  ILE C CB  1 
ATOM   9239  C CG1 . ILE C 1 377 ? -14.181 -4.750  -26.045 1.00 77.14  ? 386  ILE C CG1 1 
ATOM   9240  C CG2 . ILE C 1 377 ? -13.471 -3.858  -28.210 1.00 76.82  ? 386  ILE C CG2 1 
ATOM   9241  C CD1 . ILE C 1 377 ? -14.140 -6.251  -26.180 1.00 79.29  ? 386  ILE C CD1 1 
ATOM   9242  N N   . PHE C 1 378 ? -16.136 -2.656  -29.277 1.00 78.75  ? 387  PHE C N   1 
ATOM   9243  C CA  . PHE C 1 378 ? -16.527 -2.033  -30.500 1.00 79.10  ? 387  PHE C CA  1 
ATOM   9244  C C   . PHE C 1 378 ? -17.917 -1.548  -30.251 1.00 79.23  ? 387  PHE C C   1 
ATOM   9245  O O   . PHE C 1 378 ? -18.760 -2.286  -29.773 1.00 81.06  ? 387  PHE C O   1 
ATOM   9246  C CB  . PHE C 1 378 ? -16.485 -3.037  -31.630 1.00 81.87  ? 387  PHE C CB  1 
ATOM   9247  C CG  . PHE C 1 378 ? -15.207 -3.787  -31.683 1.00 82.63  ? 387  PHE C CG  1 
ATOM   9248  C CD1 . PHE C 1 378 ? -15.155 -5.125  -31.309 1.00 85.49  ? 387  PHE C CD1 1 
ATOM   9249  C CD2 . PHE C 1 378 ? -14.038 -3.152  -32.059 1.00 80.29  ? 387  PHE C CD2 1 
ATOM   9250  C CE1 . PHE C 1 378 ? -13.955 -5.844  -31.341 1.00 85.30  ? 387  PHE C CE1 1 
ATOM   9251  C CE2 . PHE C 1 378 ? -12.842 -3.858  -32.087 1.00 81.01  ? 387  PHE C CE2 1 
ATOM   9252  C CZ  . PHE C 1 378 ? -12.805 -5.215  -31.726 1.00 83.03  ? 387  PHE C CZ  1 
ATOM   9253  N N   . ASN C 1 379 ? -18.111 -0.274  -30.532 1.00 77.44  ? 388  ASN C N   1 
ATOM   9254  C CA  . ASN C 1 379 ? -19.349 0.405   -30.369 1.00 77.45  ? 388  ASN C CA  1 
ATOM   9255  C C   . ASN C 1 379 ? -18.980 1.838   -30.597 1.00 75.54  ? 388  ASN C C   1 
ATOM   9256  O O   . ASN C 1 379 ? -17.944 2.323   -30.077 1.00 73.36  ? 388  ASN C O   1 
ATOM   9257  C CB  . ASN C 1 379 ? -19.899 0.236   -28.959 1.00 76.84  ? 388  ASN C CB  1 
ATOM   9258  C CG  . ASN C 1 379 ? -18.894 0.616   -27.893 1.00 74.21  ? 388  ASN C CG  1 
ATOM   9259  O OD1 . ASN C 1 379 ? -18.689 1.799   -27.591 1.00 69.88  ? 388  ASN C OD1 1 
ATOM   9260  N ND2 . ASN C 1 379 ? -18.265 -0.387  -27.308 1.00 75.61  ? 388  ASN C ND2 1 
ATOM   9261  N N   . PRO C 1 380 ? -19.813 2.530   -31.380 1.00 76.48  ? 389  PRO C N   1 
ATOM   9262  C CA  . PRO C 1 380 ? -19.792 3.996   -31.475 1.00 74.66  ? 389  PRO C CA  1 
ATOM   9263  C C   . PRO C 1 380 ? -19.805 4.542   -30.053 1.00 73.28  ? 389  PRO C C   1 
ATOM   9264  O O   . PRO C 1 380 ? -20.196 3.816   -29.127 1.00 74.61  ? 389  PRO C O   1 
ATOM   9265  C CB  . PRO C 1 380 ? -21.145 4.312   -32.120 1.00 76.20  ? 389  PRO C CB  1 
ATOM   9266  C CG  . PRO C 1 380 ? -22.034 3.048   -31.846 1.00 78.55  ? 389  PRO C CG  1 
ATOM   9267  C CD  . PRO C 1 380 ? -21.041 1.935   -31.947 1.00 79.06  ? 389  PRO C CD  1 
ATOM   9268  N N   . LYS C 1 381 ? -19.421 5.792   -29.845 1.00 70.96  ? 390  LYS C N   1 
ATOM   9269  C CA  . LYS C 1 381 ? -19.529 6.341   -28.479 1.00 69.52  ? 390  LYS C CA  1 
ATOM   9270  C C   . LYS C 1 381 ? -18.200 6.214   -27.732 1.00 68.00  ? 390  LYS C C   1 
ATOM   9271  O O   . LYS C 1 381 ? -17.750 7.183   -27.090 1.00 66.40  ? 390  LYS C O   1 
ATOM   9272  C CB  . LYS C 1 381 ? -20.666 5.670   -27.668 1.00 70.94  ? 390  LYS C CB  1 
ATOM   9273  C CG  . LYS C 1 381 ? -22.113 6.173   -27.936 1.00 72.72  ? 390  LYS C CG  1 
ATOM   9274  C CD  . LYS C 1 381 ? -22.411 7.476   -27.096 1.00 73.57  ? 390  LYS C CD  1 
ATOM   9275  C CE  . LYS C 1 381 ? -23.885 7.591   -26.563 1.00 75.31  ? 390  LYS C CE  1 
ATOM   9276  N NZ  . LYS C 1 381 ? -24.855 7.835   -27.669 1.00 77.91  ? 390  LYS C NZ  1 
ATOM   9277  N N   . TYR C 1 382 ? -17.560 5.041   -27.796 1.00 68.78  ? 391  TYR C N   1 
ATOM   9278  C CA  . TYR C 1 382 ? -16.217 4.933   -27.200 1.00 67.13  ? 391  TYR C CA  1 
ATOM   9279  C C   . TYR C 1 382 ? -15.236 4.033   -27.911 1.00 68.34  ? 391  TYR C C   1 
ATOM   9280  O O   . TYR C 1 382 ? -15.445 2.812   -28.041 1.00 70.65  ? 391  TYR C O   1 
ATOM   9281  C CB  . TYR C 1 382 ? -16.265 4.520   -25.735 1.00 66.64  ? 391  TYR C CB  1 
ATOM   9282  C CG  . TYR C 1 382 ? -15.210 5.193   -24.921 1.00 63.75  ? 391  TYR C CG  1 
ATOM   9283  C CD1 . TYR C 1 382 ? -15.217 6.578   -24.785 1.00 61.87  ? 391  TYR C CD1 1 
ATOM   9284  C CD2 . TYR C 1 382 ? -14.220 4.458   -24.272 1.00 63.40  ? 391  TYR C CD2 1 
ATOM   9285  C CE1 . TYR C 1 382 ? -14.263 7.226   -24.023 1.00 59.67  ? 391  TYR C CE1 1 
ATOM   9286  C CE2 . TYR C 1 382 ? -13.246 5.097   -23.505 1.00 60.69  ? 391  TYR C CE2 1 
ATOM   9287  C CZ  . TYR C 1 382 ? -13.281 6.490   -23.388 1.00 58.77  ? 391  TYR C CZ  1 
ATOM   9288  O OH  . TYR C 1 382 ? -12.359 7.187   -22.651 1.00 56.53  ? 391  TYR C OH  1 
ATOM   9289  N N   . ASP C 1 383 ? -14.153 4.656   -28.372 1.00 67.00  ? 392  ASP C N   1 
ATOM   9290  C CA  . ASP C 1 383 ? -12.967 3.881   -28.748 1.00 67.74  ? 392  ASP C CA  1 
ATOM   9291  C C   . ASP C 1 383 ? -12.200 3.612   -27.481 1.00 66.26  ? 392  ASP C C   1 
ATOM   9292  O O   . ASP C 1 383 ? -12.042 4.465   -26.604 1.00 64.28  ? 392  ASP C O   1 
ATOM   9293  C CB  . ASP C 1 383 ? -12.081 4.455   -29.881 1.00 67.35  ? 392  ASP C CB  1 
ATOM   9294  C CG  . ASP C 1 383 ? -12.438 5.879   -30.272 1.00 66.60  ? 392  ASP C CG  1 
ATOM   9295  O OD1 . ASP C 1 383 ? -12.530 6.787   -29.369 1.00 65.71  ? 392  ASP C OD1 1 
ATOM   9296  O OD2 . ASP C 1 383 ? -12.595 6.056   -31.516 1.00 67.32  ? 392  ASP C OD2 1 
ATOM   9297  N N   . CYS C 1 384 ? -11.690 2.401   -27.448 1.00 67.17  ? 393  CYS C N   1 
ATOM   9298  C CA  . CYS C 1 384 ? -11.768 1.607   -26.276 1.00 67.07  ? 393  CYS C CA  1 
ATOM   9299  C C   . CYS C 1 384 ? -10.428 0.926   -26.162 1.00 66.53  ? 393  CYS C C   1 
ATOM   9300  O O   . CYS C 1 384 ? -10.076 0.136   -27.004 1.00 68.30  ? 393  CYS C O   1 
ATOM   9301  C CB  . CYS C 1 384 ? -12.923 0.633   -26.558 1.00 69.50  ? 393  CYS C CB  1 
ATOM   9302  S SG  . CYS C 1 384 ? -13.588 -0.261  -25.195 1.00 72.90  ? 393  CYS C SG  1 
ATOM   9303  N N   . LYS C 1 385 ? -9.656  1.261   -25.146 1.00 64.32  ? 394  LYS C N   1 
ATOM   9304  C CA  . LYS C 1 385 ? -8.270  0.805   -25.096 1.00 64.12  ? 394  LYS C CA  1 
ATOM   9305  C C   . LYS C 1 385 ? -8.138  -0.705  -24.925 1.00 65.92  ? 394  LYS C C   1 
ATOM   9306  O O   . LYS C 1 385 ? -8.770  -1.292  -24.065 1.00 66.47  ? 394  LYS C O   1 
ATOM   9307  C CB  . LYS C 1 385 ? -7.487  1.582   -24.053 1.00 61.74  ? 394  LYS C CB  1 
ATOM   9308  C CG  . LYS C 1 385 ? -7.745  3.096   -24.175 1.00 61.64  ? 394  LYS C CG  1 
ATOM   9309  C CD  . LYS C 1 385 ? -6.737  3.982   -23.412 1.00 64.64  ? 394  LYS C CD  1 
ATOM   9310  C CE  . LYS C 1 385 ? -7.027  4.164   -21.897 1.00 65.77  ? 394  LYS C CE  1 
ATOM   9311  N NZ  . LYS C 1 385 ? -6.205  3.314   -20.939 1.00 66.58  ? 394  LYS C NZ  1 
ATOM   9312  N N   . ILE C 1 386 ? -7.282  -1.294  -25.760 1.00 66.79  ? 395  ILE C N   1 
ATOM   9313  C CA  . ILE C 1 386 ? -7.221  -2.720  -26.114 1.00 69.35  ? 395  ILE C CA  1 
ATOM   9314  C C   . ILE C 1 386 ? -5.774  -3.086  -26.474 1.00 70.01  ? 395  ILE C C   1 
ATOM   9315  O O   . ILE C 1 386 ? -5.037  -2.253  -26.954 1.00 68.83  ? 395  ILE C O   1 
ATOM   9316  C CB  . ILE C 1 386 ? -7.998  -2.892  -27.434 1.00 71.13  ? 395  ILE C CB  1 
ATOM   9317  C CG1 . ILE C 1 386 ? -9.489  -2.973  -27.206 1.00 72.58  ? 395  ILE C CG1 1 
ATOM   9318  C CG2 . ILE C 1 386 ? -7.545  -4.095  -28.281 1.00 73.76  ? 395  ILE C CG2 1 
ATOM   9319  C CD1 . ILE C 1 386 ? -10.255 -3.019  -28.548 1.00 75.94  ? 395  ILE C CD1 1 
ATOM   9320  N N   . MET C 1 387 ? -5.345  -4.325  -26.315 1.00 72.32  ? 396  MET C N   1 
ATOM   9321  C CA  . MET C 1 387 ? -4.174  -4.721  -27.112 1.00 73.96  ? 396  MET C CA  1 
ATOM   9322  C C   . MET C 1 387 ? -4.370  -5.967  -27.979 1.00 77.68  ? 396  MET C C   1 
ATOM   9323  O O   . MET C 1 387 ? -5.290  -6.780  -27.746 1.00 79.89  ? 396  MET C O   1 
ATOM   9324  C CB  . MET C 1 387 ? -2.948  -4.859  -26.268 1.00 73.39  ? 396  MET C CB  1 
ATOM   9325  C CG  . MET C 1 387 ? -2.931  -6.088  -25.432 1.00 76.75  ? 396  MET C CG  1 
ATOM   9326  S SD  . MET C 1 387 ? -1.336  -6.179  -24.591 1.00 81.07  ? 396  MET C SD  1 
ATOM   9327  C CE  . MET C 1 387 ? -1.019  -4.444  -24.168 1.00 76.10  ? 396  MET C CE  1 
ATOM   9328  N N   . THR C 1 388 ? -3.492  -6.127  -28.965 1.00 78.58  ? 397  THR C N   1 
ATOM   9329  C CA  . THR C 1 388 ? -3.753  -7.039  -30.065 1.00 81.65  ? 397  THR C CA  1 
ATOM   9330  C C   . THR C 1 388 ? -2.813  -8.228  -30.137 1.00 84.32  ? 397  THR C C   1 
ATOM   9331  O O   . THR C 1 388 ? -1.614  -8.078  -29.955 1.00 83.83  ? 397  THR C O   1 
ATOM   9332  C CB  . THR C 1 388 ? -3.667  -6.262  -31.361 1.00 81.19  ? 397  THR C CB  1 
ATOM   9333  O OG1 . THR C 1 388 ? -4.852  -5.484  -31.478 1.00 79.83  ? 397  THR C OG1 1 
ATOM   9334  C CG2 . THR C 1 388 ? -3.545  -7.190  -32.565 1.00 85.13  ? 397  THR C CG2 1 
ATOM   9335  N N   . SER C 1 389 ? -3.362  -9.408  -30.409 1.00 87.40  ? 398  SER C N   1 
ATOM   9336  C CA  . SER C 1 389 ? -2.530  -10.540 -30.788 1.00 90.50  ? 398  SER C CA  1 
ATOM   9337  C C   . SER C 1 389 ? -3.053  -11.310 -31.982 1.00 94.06  ? 398  SER C C   1 
ATOM   9338  O O   . SER C 1 389 ? -4.241  -11.612 -32.094 1.00 95.37  ? 398  SER C O   1 
ATOM   9339  C CB  . SER C 1 389 ? -2.336  -11.510 -29.638 1.00 91.43  ? 398  SER C CB  1 
ATOM   9340  O OG  . SER C 1 389 ? -1.789  -12.715 -30.149 1.00 95.20  ? 398  SER C OG  1 
ATOM   9341  N N   . LYS C 1 390 ? -2.138  -11.653 -32.862 1.00 95.93  ? 399  LYS C N   1 
ATOM   9342  C CA  . LYS C 1 390 ? -2.471  -12.499 -33.965 1.00 99.76  ? 399  LYS C CA  1 
ATOM   9343  C C   . LYS C 1 390 ? -2.707  -13.938 -33.462 1.00 102.78 ? 399  LYS C C   1 
ATOM   9344  O O   . LYS C 1 390 ? -3.565  -14.667 -34.010 1.00 105.40 ? 399  LYS C O   1 
ATOM   9345  C CB  . LYS C 1 390 ? -1.342  -12.413 -34.992 1.00 101.29 ? 399  LYS C CB  1 
ATOM   9346  C CG  . LYS C 1 390 ? -1.508  -11.330 -36.076 1.00 100.51 ? 399  LYS C CG  1 
ATOM   9347  C CD  . LYS C 1 390 ? -2.241  -11.962 -37.272 1.00 106.75 ? 399  LYS C CD  1 
ATOM   9348  C CE  . LYS C 1 390 ? -2.180  -11.148 -38.573 1.00 107.74 ? 399  LYS C CE  1 
ATOM   9349  N NZ  . LYS C 1 390 ? -2.859  -11.872 -39.729 1.00 110.47 ? 399  LYS C NZ  1 
ATOM   9350  N N   . THR C 1 391 ? -1.978  -14.306 -32.395 1.00 102.09 ? 400  THR C N   1 
ATOM   9351  C CA  . THR C 1 391 ? -1.901  -15.693 -31.894 1.00 105.32 ? 400  THR C CA  1 
ATOM   9352  C C   . THR C 1 391 ? -2.640  -15.932 -30.581 1.00 103.86 ? 400  THR C C   1 
ATOM   9353  O O   . THR C 1 391 ? -2.656  -15.071 -29.719 1.00 99.97  ? 400  THR C O   1 
ATOM   9354  C CB  . THR C 1 391 ? -0.437  -16.145 -31.670 1.00 106.41 ? 400  THR C CB  1 
ATOM   9355  O OG1 . THR C 1 391 ? 0.460   -15.178 -32.224 1.00 105.03 ? 400  THR C OG1 1 
ATOM   9356  C CG2 . THR C 1 391 ? -0.182  -17.569 -32.290 1.00 111.97 ? 400  THR C CG2 1 
ATOM   9357  N N   . ASP C 1 392 ? -3.237  -17.122 -30.451 1.00 106.96 ? 401  ASP C N   1 
ATOM   9358  C CA  . ASP C 1 392 ? -3.876  -17.579 -29.222 1.00 106.46 ? 401  ASP C CA  1 
ATOM   9359  C C   . ASP C 1 392 ? -2.915  -17.414 -28.074 1.00 103.85 ? 401  ASP C C   1 
ATOM   9360  O O   . ASP C 1 392 ? -1.759  -17.827 -28.129 1.00 105.06 ? 401  ASP C O   1 
ATOM   9361  C CB  . ASP C 1 392 ? -4.295  -19.053 -29.313 1.00 111.35 ? 401  ASP C CB  1 
ATOM   9362  C CG  . ASP C 1 392 ? -5.564  -19.263 -30.110 1.00 114.74 ? 401  ASP C CG  1 
ATOM   9363  O OD1 . ASP C 1 392 ? -5.821  -18.520 -31.082 1.00 116.69 ? 401  ASP C OD1 1 
ATOM   9364  O OD2 . ASP C 1 392 ? -6.302  -20.204 -29.766 1.00 118.51 ? 401  ASP C OD2 1 
ATOM   9365  N N   . VAL C 1 393 ? -3.413  -16.775 -27.038 1.00 100.37 ? 402  VAL C N   1 
ATOM   9366  C CA  . VAL C 1 393 ? -2.695  -16.613 -25.789 1.00 97.67  ? 402  VAL C CA  1 
ATOM   9367  C C   . VAL C 1 393 ? -3.642  -17.079 -24.719 1.00 97.37  ? 402  VAL C C   1 
ATOM   9368  O O   . VAL C 1 393 ? -4.801  -16.680 -24.720 1.00 96.69  ? 402  VAL C O   1 
ATOM   9369  C CB  . VAL C 1 393 ? -2.396  -15.137 -25.507 1.00 93.12  ? 402  VAL C CB  1 
ATOM   9370  C CG1 . VAL C 1 393 ? -1.785  -14.982 -24.143 1.00 91.58  ? 402  VAL C CG1 1 
ATOM   9371  C CG2 . VAL C 1 393 ? -1.481  -14.566 -26.570 1.00 93.11  ? 402  VAL C CG2 1 
ATOM   9372  N N   . SER C 1 394 ? -3.169  -17.911 -23.806 1.00 97.76  ? 403  SER C N   1 
ATOM   9373  C CA  . SER C 1 394 ? -4.036  -18.385 -22.745 1.00 97.62  ? 403  SER C CA  1 
ATOM   9374  C C   . SER C 1 394 ? -3.452  -17.894 -21.441 1.00 93.95  ? 403  SER C C   1 
ATOM   9375  O O   . SER C 1 394 ? -2.248  -17.942 -21.290 1.00 93.60  ? 403  SER C O   1 
ATOM   9376  C CB  . SER C 1 394 ? -4.105  -19.923 -22.737 1.00 102.20 ? 403  SER C CB  1 
ATOM   9377  O OG  . SER C 1 394 ? -3.857  -20.486 -24.016 1.00 106.16 ? 403  SER C OG  1 
ATOM   9378  N N   . SER C 1 395 ? -4.278  -17.405 -20.514 1.00 91.39  ? 404  SER C N   1 
ATOM   9379  C CA  . SER C 1 395 ? -3.848  -17.293 -19.107 1.00 89.32  ? 404  SER C CA  1 
ATOM   9380  C C   . SER C 1 395 ? -4.975  -17.012 -18.095 1.00 87.60  ? 404  SER C C   1 
ATOM   9381  O O   . SER C 1 395 ? -6.158  -17.120 -18.411 1.00 88.71  ? 404  SER C O   1 
ATOM   9382  C CB  . SER C 1 395 ? -2.672  -16.316 -18.946 1.00 86.09  ? 404  SER C CB  1 
ATOM   9383  O OG  . SER C 1 395 ? -3.074  -15.088 -18.380 1.00 83.26  ? 404  SER C OG  1 
ATOM   9384  N N   . SER C 1 396 ? -4.593  -16.672 -16.871 1.00 84.86  ? 405  SER C N   1 
ATOM   9385  C CA  . SER C 1 396 ? -5.558  -16.393 -15.825 1.00 83.34  ? 405  SER C CA  1 
ATOM   9386  C C   . SER C 1 396 ? -5.248  -15.124 -15.006 1.00 79.28  ? 405  SER C C   1 
ATOM   9387  O O   . SER C 1 396 ? -4.077  -14.708 -14.868 1.00 77.65  ? 405  SER C O   1 
ATOM   9388  C CB  . SER C 1 396 ? -5.674  -17.597 -14.915 1.00 85.77  ? 405  SER C CB  1 
ATOM   9389  O OG  . SER C 1 396 ? -6.160  -17.192 -13.662 1.00 83.33  ? 405  SER C OG  1 
ATOM   9390  N N   . VAL C 1 397 ? -6.318  -14.529 -14.464 1.00 77.82  ? 406  VAL C N   1 
ATOM   9391  C CA  . VAL C 1 397 ? -6.280  -13.221 -13.791 1.00 74.23  ? 406  VAL C CA  1 
ATOM   9392  C C   . VAL C 1 397 ? -7.117  -13.244 -12.528 1.00 73.75  ? 406  VAL C C   1 
ATOM   9393  O O   . VAL C 1 397 ? -8.317  -13.483 -12.584 1.00 75.29  ? 406  VAL C O   1 
ATOM   9394  C CB  . VAL C 1 397 ? -6.901  -12.117 -14.670 1.00 72.54  ? 406  VAL C CB  1 
ATOM   9395  C CG1 . VAL C 1 397 ? -6.506  -10.728 -14.147 1.00 69.53  ? 406  VAL C CG1 1 
ATOM   9396  C CG2 . VAL C 1 397 ? -6.512  -12.288 -16.134 1.00 74.58  ? 406  VAL C CG2 1 
ATOM   9397  N N   . ILE C 1 398 ? -6.508  -12.948 -11.391 1.00 71.95  ? 407  ILE C N   1 
ATOM   9398  C CA  . ILE C 1 398 ? -7.246  -13.063 -10.152 1.00 71.94  ? 407  ILE C CA  1 
ATOM   9399  C C   . ILE C 1 398 ? -7.907  -11.784 -9.741  1.00 69.72  ? 407  ILE C C   1 
ATOM   9400  O O   . ILE C 1 398 ? -7.264  -10.726 -9.681  1.00 67.19  ? 407  ILE C O   1 
ATOM   9401  C CB  . ILE C 1 398 ? -6.377  -13.551 -9.025  1.00 71.55  ? 407  ILE C CB  1 
ATOM   9402  C CG1 . ILE C 1 398 ? -6.054  -15.013 -9.272  1.00 74.68  ? 407  ILE C CG1 1 
ATOM   9403  C CG2 . ILE C 1 398 ? -7.104  -13.412 -7.691  1.00 70.41  ? 407  ILE C CG2 1 
ATOM   9404  C CD1 . ILE C 1 398 ? -5.153  -15.581 -8.259  1.00 76.48  ? 407  ILE C CD1 1 
ATOM   9405  N N   . THR C 1 399 ? -9.188  -11.903 -9.415  1.00 71.15  ? 408  THR C N   1 
ATOM   9406  C CA  . THR C 1 399 ? -9.988  -10.753 -9.068  1.00 69.56  ? 408  THR C CA  1 
ATOM   9407  C C   . THR C 1 399 ? -10.273 -10.671 -7.589  1.00 69.10  ? 408  THR C C   1 
ATOM   9408  O O   . THR C 1 399 ? -9.941  -11.576 -6.819  1.00 70.72  ? 408  THR C O   1 
ATOM   9409  C CB  . THR C 1 399 ? -11.309 -10.788 -9.791  1.00 71.19  ? 408  THR C CB  1 
ATOM   9410  O OG1 . THR C 1 399 ? -11.999 -11.987 -9.434  1.00 75.06  ? 408  THR C OG1 1 
ATOM   9411  C CG2 . THR C 1 399 ? -11.102 -10.767 -11.297 1.00 72.06  ? 408  THR C CG2 1 
ATOM   9412  N N   . SER C 1 400 ? -10.917 -9.573  -7.217  1.00 67.39  ? 409  SER C N   1 
ATOM   9413  C CA  . SER C 1 400 ? -11.228 -9.276  -5.830  1.00 66.90  ? 409  SER C CA  1 
ATOM   9414  C C   . SER C 1 400 ? -11.996 -10.407 -5.193  1.00 69.70  ? 409  SER C C   1 
ATOM   9415  O O   . SER C 1 400 ? -11.825 -10.703 -4.010  1.00 69.83  ? 409  SER C O   1 
ATOM   9416  C CB  . SER C 1 400 ? -12.100 -8.025  -5.739  1.00 65.28  ? 409  SER C CB  1 
ATOM   9417  O OG  . SER C 1 400 ? -11.502 -6.922  -6.383  1.00 64.02  ? 409  SER C OG  1 
ATOM   9418  N N   . LEU C 1 401 ? -12.846 -11.033 -5.993  1.00 72.13  ? 410  LEU C N   1 
ATOM   9419  C CA  . LEU C 1 401 ? -13.910 -11.858 -5.456  1.00 74.94  ? 410  LEU C CA  1 
ATOM   9420  C C   . LEU C 1 401 ? -14.050 -13.225 -6.160  1.00 78.49  ? 410  LEU C C   1 
ATOM   9421  O O   . LEU C 1 401 ? -14.958 -14.023 -5.860  1.00 81.21  ? 410  LEU C O   1 
ATOM   9422  C CB  . LEU C 1 401 ? -15.207 -11.052 -5.526  1.00 74.72  ? 410  LEU C CB  1 
ATOM   9423  C CG  . LEU C 1 401 ? -15.958 -10.816 -4.214  1.00 74.61  ? 410  LEU C CG  1 
ATOM   9424  C CD1 . LEU C 1 401 ? -15.047 -10.188 -3.153  1.00 72.95  ? 410  LEU C CD1 1 
ATOM   9425  C CD2 . LEU C 1 401 ? -17.185 -9.946  -4.452  1.00 73.71  ? 410  LEU C CD2 1 
ATOM   9426  N N   . GLY C 1 402 ? -13.130 -13.475 -7.090  1.00 78.33  ? 411  GLY C N   1 
ATOM   9427  C CA  . GLY C 1 402 ? -12.993 -14.753 -7.781  1.00 80.93  ? 411  GLY C CA  1 
ATOM   9428  C C   . GLY C 1 402 ? -11.783 -14.698 -8.695  1.00 79.61  ? 411  GLY C C   1 
ATOM   9429  O O   . GLY C 1 402 ? -10.759 -14.078 -8.356  1.00 77.02  ? 411  GLY C O   1 
ATOM   9430  N N   . ALA C 1 403 ? -11.907 -15.313 -9.866  1.00 81.23  ? 412  ALA C N   1 
ATOM   9431  C CA  . ALA C 1 403 ? -10.837 -15.297 -10.849 1.00 80.27  ? 412  ALA C CA  1 
ATOM   9432  C C   . ALA C 1 403 ? -11.373 -15.460 -12.262 1.00 81.95  ? 412  ALA C C   1 
ATOM   9433  O O   . ALA C 1 403 ? -12.433 -16.052 -12.451 1.00 84.63  ? 412  ALA C O   1 
ATOM   9434  C CB  . ALA C 1 403 ? -9.857  -16.383 -10.539 1.00 81.85  ? 412  ALA C CB  1 
ATOM   9435  N N   . ILE C 1 404 ? -10.639 -14.930 -13.242 1.00 80.70  ? 413  ILE C N   1 
ATOM   9436  C CA  . ILE C 1 404 ? -10.922 -15.147 -14.664 1.00 82.61  ? 413  ILE C CA  1 
ATOM   9437  C C   . ILE C 1 404 ? -9.910  -16.103 -15.252 1.00 85.19  ? 413  ILE C C   1 
ATOM   9438  O O   . ILE C 1 404 ? -8.768  -16.165 -14.813 1.00 84.22  ? 413  ILE C O   1 
ATOM   9439  C CB  . ILE C 1 404 ? -10.845 -13.854 -15.488 1.00 79.60  ? 413  ILE C CB  1 
ATOM   9440  C CG1 . ILE C 1 404 ? -11.828 -12.817 -14.956 1.00 77.17  ? 413  ILE C CG1 1 
ATOM   9441  C CG2 . ILE C 1 404 ? -11.109 -14.144 -16.961 1.00 81.53  ? 413  ILE C CG2 1 
ATOM   9442  C CD1 . ILE C 1 404 ? -11.980 -11.605 -15.844 1.00 75.61  ? 413  ILE C CD1 1 
ATOM   9443  N N   . VAL C 1 405 ? -10.326 -16.842 -16.262 1.00 88.79  ? 414  VAL C N   1 
ATOM   9444  C CA  . VAL C 1 405 ? -9.425  -17.756 -16.917 1.00 91.82  ? 414  VAL C CA  1 
ATOM   9445  C C   . VAL C 1 405 ? -9.749  -17.819 -18.396 1.00 93.84  ? 414  VAL C C   1 
ATOM   9446  O O   . VAL C 1 405 ? -10.881 -18.094 -18.804 1.00 96.07  ? 414  VAL C O   1 
ATOM   9447  C CB  . VAL C 1 405 ? -9.417  -19.150 -16.240 1.00 95.17  ? 414  VAL C CB  1 
ATOM   9448  C CG1 . VAL C 1 405 ? -10.808 -19.522 -15.762 1.00 97.32  ? 414  VAL C CG1 1 
ATOM   9449  C CG2 . VAL C 1 405 ? -8.851  -20.213 -17.174 1.00 98.97  ? 414  VAL C CG2 1 
ATOM   9450  N N   . SER C 1 406 ? -8.732  -17.531 -19.189 1.00 93.30  ? 415  SER C N   1 
ATOM   9451  C CA  . SER C 1 406 ? -8.838  -17.575 -20.624 1.00 95.22  ? 415  SER C CA  1 
ATOM   9452  C C   . SER C 1 406 ? -8.074  -18.799 -21.118 1.00 99.21  ? 415  SER C C   1 
ATOM   9453  O O   . SER C 1 406 ? -6.854  -18.776 -21.184 1.00 98.88  ? 415  SER C O   1 
ATOM   9454  C CB  . SER C 1 406 ? -8.240  -16.298 -21.203 1.00 91.65  ? 415  SER C CB  1 
ATOM   9455  O OG  . SER C 1 406 ? -8.868  -15.158 -20.653 1.00 88.41  ? 415  SER C OG  1 
ATOM   9456  N N   . CYS C 1 407 ? -8.783  -19.874 -21.445 1.00 103.49 ? 416  CYS C N   1 
ATOM   9457  C CA  . CYS C 1 407 ? -8.127  -21.096 -21.880 1.00 107.58 ? 416  CYS C CA  1 
ATOM   9458  C C   . CYS C 1 407 ? -8.289  -21.252 -23.367 1.00 109.66 ? 416  CYS C C   1 
ATOM   9459  O O   . CYS C 1 407 ? -9.398  -21.506 -23.846 1.00 111.79 ? 416  CYS C O   1 
ATOM   9460  C CB  . CYS C 1 407 ? -8.729  -22.304 -21.185 1.00 111.21 ? 416  CYS C CB  1 
ATOM   9461  S SG  . CYS C 1 407 ? -7.528  -23.614 -20.941 1.00 116.06 ? 416  CYS C SG  1 
ATOM   9462  N N   . TYR C 1 408 ? -7.180  -21.117 -24.089 1.00 109.42 ? 417  TYR C N   1 
ATOM   9463  C CA  . TYR C 1 408 ? -7.210  -21.100 -25.548 1.00 110.87 ? 417  TYR C CA  1 
ATOM   9464  C C   . TYR C 1 408 ? -6.183  -22.025 -26.206 1.00 114.10 ? 417  TYR C C   1 
ATOM   9465  O O   . TYR C 1 408 ? -5.220  -22.452 -25.573 1.00 114.32 ? 417  TYR C O   1 
ATOM   9466  C CB  . TYR C 1 408 ? -7.072  -19.661 -26.060 1.00 106.80 ? 417  TYR C CB  1 
ATOM   9467  C CG  . TYR C 1 408 ? -8.321  -18.812 -25.869 1.00 104.54 ? 417  TYR C CG  1 
ATOM   9468  C CD1 . TYR C 1 408 ? -8.254  -17.572 -25.252 1.00 100.09 ? 417  TYR C CD1 1 
ATOM   9469  C CD2 . TYR C 1 408 ? -9.577  -19.254 -26.314 1.00 107.89 ? 417  TYR C CD2 1 
ATOM   9470  C CE1 . TYR C 1 408 ? -9.400  -16.781 -25.078 1.00 98.88  ? 417  TYR C CE1 1 
ATOM   9471  C CE2 . TYR C 1 408 ? -10.735 -18.465 -26.141 1.00 106.33 ? 417  TYR C CE2 1 
ATOM   9472  C CZ  . TYR C 1 408 ? -10.634 -17.227 -25.522 1.00 101.83 ? 417  TYR C CZ  1 
ATOM   9473  O OH  . TYR C 1 408 ? -11.770 -16.457 -25.350 1.00 101.01 ? 417  TYR C OH  1 
ATOM   9474  N N   . GLY C 1 409 ? -6.409  -22.325 -27.482 1.00 116.80 ? 418  GLY C N   1 
ATOM   9475  C CA  . GLY C 1 409 ? -5.554  -23.226 -28.236 1.00 120.54 ? 418  GLY C CA  1 
ATOM   9476  C C   . GLY C 1 409 ? -5.424  -24.575 -27.568 1.00 124.36 ? 418  GLY C C   1 
ATOM   9477  O O   . GLY C 1 409 ? -6.411  -25.181 -27.158 1.00 126.36 ? 418  GLY C O   1 
ATOM   9478  N N   . LYS C 1 410 ? -4.187  -25.026 -27.435 1.00 125.53 ? 419  LYS C N   1 
ATOM   9479  C CA  . LYS C 1 410 ? -3.894  -26.344 -26.907 1.00 129.66 ? 419  LYS C CA  1 
ATOM   9480  C C   . LYS C 1 410 ? -3.911  -26.438 -25.385 1.00 127.76 ? 419  LYS C C   1 
ATOM   9481  O O   . LYS C 1 410 ? -3.803  -27.523 -24.837 1.00 130.81 ? 419  LYS C O   1 
ATOM   9482  C CB  . LYS C 1 410 ? -2.534  -26.815 -27.424 1.00 132.01 ? 419  LYS C CB  1 
ATOM   9483  C CG  . LYS C 1 410 ? -2.586  -27.542 -28.755 1.00 138.21 ? 419  LYS C CG  1 
ATOM   9484  C CD  . LYS C 1 410 ? -1.400  -28.498 -28.868 1.00 144.79 ? 419  LYS C CD  1 
ATOM   9485  C CE  . LYS C 1 410 ? -1.628  -29.606 -29.890 1.00 151.74 ? 419  LYS C CE  1 
ATOM   9486  N NZ  . LYS C 1 410 ? -1.906  -29.040 -31.226 1.00 153.56 ? 419  LYS C NZ  1 
ATOM   9487  N N   . THR C 1 411 ? -4.046  -25.319 -24.693 1.00 122.87 ? 420  THR C N   1 
ATOM   9488  C CA  . THR C 1 411 ? -3.771  -25.318 -23.259 1.00 120.81 ? 420  THR C CA  1 
ATOM   9489  C C   . THR C 1 411 ? -4.891  -25.920 -22.397 1.00 122.43 ? 420  THR C C   1 
ATOM   9490  O O   . THR C 1 411 ? -6.058  -25.861 -22.760 1.00 123.34 ? 420  THR C O   1 
ATOM   9491  C CB  . THR C 1 411 ? -3.318  -23.922 -22.778 1.00 115.26 ? 420  THR C CB  1 
ATOM   9492  O OG1 . THR C 1 411 ? -3.619  -22.954 -23.785 1.00 112.87 ? 420  THR C OG1 1 
ATOM   9493  C CG2 . THR C 1 411 ? -1.821  -23.904 -22.580 1.00 114.04 ? 420  THR C CG2 1 
ATOM   9494  N N   . LYS C 1 412 ? -4.506  -26.537 -21.280 1.00 123.12 ? 421  LYS C N   1 
ATOM   9495  C CA  . LYS C 1 412 ? -5.439  -27.178 -20.350 1.00 125.01 ? 421  LYS C CA  1 
ATOM   9496  C C   . LYS C 1 412 ? -5.644  -26.350 -19.104 1.00 120.73 ? 421  LYS C C   1 
ATOM   9497  O O   . LYS C 1 412 ? -4.675  -25.915 -18.495 1.00 118.38 ? 421  LYS C O   1 
ATOM   9498  C CB  . LYS C 1 412 ? -4.913  -28.545 -19.923 1.00 129.26 ? 421  LYS C CB  1 
ATOM   9499  C CG  . LYS C 1 412 ? -5.554  -29.700 -20.661 1.00 136.82 ? 421  LYS C CG  1 
ATOM   9500  C CD  . LYS C 1 412 ? -4.838  -31.015 -20.396 1.00 143.97 ? 421  LYS C CD  1 
ATOM   9501  C CE  . LYS C 1 412 ? -5.009  -31.980 -21.571 1.00 149.27 ? 421  LYS C CE  1 
ATOM   9502  N NZ  . LYS C 1 412 ? -4.101  -33.147 -21.435 1.00 154.28 ? 421  LYS C NZ  1 
ATOM   9503  N N   . CYS C 1 413 ? -6.897  -26.157 -18.704 1.00 120.04 ? 422  CYS C N   1 
ATOM   9504  C CA  . CYS C 1 413 ? -7.197  -25.350 -17.522 1.00 116.08 ? 422  CYS C CA  1 
ATOM   9505  C C   . CYS C 1 413 ? -8.176  -26.009 -16.554 1.00 117.59 ? 422  CYS C C   1 
ATOM   9506  O O   . CYS C 1 413 ? -9.085  -26.711 -16.956 1.00 121.13 ? 422  CYS C O   1 
ATOM   9507  C CB  . CYS C 1 413 ? -7.681  -23.957 -17.928 1.00 112.38 ? 422  CYS C CB  1 
ATOM   9508  S SG  . CYS C 1 413 ? -6.644  -23.095 -19.173 1.00 111.65 ? 422  CYS C SG  1 
ATOM   9509  N N   . THR C 1 414 ? -7.988  -25.746 -15.272 1.00 115.14 ? 423  THR C N   1 
ATOM   9510  C CA  . THR C 1 414 ? -8.561  -26.553 -14.217 1.00 117.09 ? 423  THR C CA  1 
ATOM   9511  C C   . THR C 1 414 ? -8.891  -25.678 -13.044 1.00 113.56 ? 423  THR C C   1 
ATOM   9512  O O   . THR C 1 414 ? -8.025  -24.968 -12.546 1.00 110.66 ? 423  THR C O   1 
ATOM   9513  C CB  . THR C 1 414 ? -7.500  -27.517 -13.694 1.00 118.87 ? 423  THR C CB  1 
ATOM   9514  O OG1 . THR C 1 414 ? -7.145  -28.429 -14.725 1.00 122.44 ? 423  THR C OG1 1 
ATOM   9515  C CG2 . THR C 1 414 ? -7.991  -28.285 -12.499 1.00 121.09 ? 423  THR C CG2 1 
ATOM   9516  N N   . ALA C 1 415 ? -10.117 -25.757 -12.561 1.00 114.29 ? 424  ALA C N   1 
ATOM   9517  C CA  . ALA C 1 415 ? -10.413 -25.162 -11.274 1.00 111.48 ? 424  ALA C CA  1 
ATOM   9518  C C   . ALA C 1 415 ? -10.540 -26.253 -10.208 1.00 114.32 ? 424  ALA C C   1 
ATOM   9519  O O   . ALA C 1 415 ? -11.305 -27.189 -10.375 1.00 118.56 ? 424  ALA C O   1 
ATOM   9520  C CB  . ALA C 1 415 ? -11.666 -24.337 -11.367 1.00 110.04 ? 424  ALA C CB  1 
ATOM   9521  N N   . SER C 1 416 ? -9.778  -26.144 -9.125  1.00 112.43 ? 425  SER C N   1 
ATOM   9522  C CA  . SER C 1 416 ? -9.859  -27.113 -8.034  1.00 114.96 ? 425  SER C CA  1 
ATOM   9523  C C   . SER C 1 416 ? -10.382 -26.446 -6.767  1.00 112.71 ? 425  SER C C   1 
ATOM   9524  O O   . SER C 1 416 ? -10.173 -25.255 -6.564  1.00 108.49 ? 425  SER C O   1 
ATOM   9525  C CB  . SER C 1 416 ? -8.493  -27.728 -7.780  1.00 115.51 ? 425  SER C CB  1 
ATOM   9526  O OG  . SER C 1 416 ? -7.772  -27.818 -8.991  1.00 115.85 ? 425  SER C OG  1 
ATOM   9527  N N   . ASN C 1 417 ? -11.060 -27.210 -5.918  1.00 115.91 ? 426  ASN C N   1 
ATOM   9528  C CA  . ASN C 1 417 ? -11.697 -26.655 -4.727  1.00 114.81 ? 426  ASN C CA  1 
ATOM   9529  C C   . ASN C 1 417 ? -10.742 -26.586 -3.580  1.00 113.98 ? 426  ASN C C   1 
ATOM   9530  O O   . ASN C 1 417 ? -9.555  -26.877 -3.733  1.00 113.80 ? 426  ASN C O   1 
ATOM   9531  C CB  . ASN C 1 417 ? -12.936 -27.458 -4.291  1.00 118.26 ? 426  ASN C CB  1 
ATOM   9532  C CG  . ASN C 1 417 ? -12.587 -28.696 -3.435  1.00 121.19 ? 426  ASN C CG  1 
ATOM   9533  O OD1 . ASN C 1 417 ? -11.538 -28.739 -2.802  1.00 118.58 ? 426  ASN C OD1 1 
ATOM   9534  N ND2 . ASN C 1 417 ? -13.476 -29.704 -3.426  1.00 125.29 ? 426  ASN C ND2 1 
ATOM   9535  N N   . LYS C 1 418 ? -11.308 -26.211 -2.432  1.00 114.34 ? 427  LYS C N   1 
ATOM   9536  C CA  . LYS C 1 418 ? -10.640 -26.140 -1.119  1.00 114.21 ? 427  LYS C CA  1 
ATOM   9537  C C   . LYS C 1 418 ? -9.521  -27.178 -0.904  1.00 116.26 ? 427  LYS C C   1 
ATOM   9538  O O   . LYS C 1 418 ? -8.353  -26.827 -0.608  1.00 113.26 ? 427  LYS C O   1 
ATOM   9539  C CB  . LYS C 1 418 ? -11.701 -26.297 0.002   1.00 116.03 ? 427  LYS C CB  1 
ATOM   9540  C CG  . LYS C 1 418 ? -12.064 -25.027 0.819   1.00 114.45 ? 427  LYS C CG  1 
ATOM   9541  C CD  . LYS C 1 418 ? -12.632 -25.401 2.223   1.00 118.12 ? 427  LYS C CD  1 
ATOM   9542  C CE  . LYS C 1 418 ? -12.864 -24.173 3.125   1.00 115.80 ? 427  LYS C CE  1 
ATOM   9543  N NZ  . LYS C 1 418 ? -11.694 -23.231 3.210   1.00 112.62 ? 427  LYS C NZ  1 
ATOM   9544  N N   . ASN C 1 419 ? -9.927  -28.448 -1.047  1.00 121.38 ? 428  ASN C N   1 
ATOM   9545  C CA  . ASN C 1 419 ? -9.084  -29.635 -0.818  1.00 124.59 ? 428  ASN C CA  1 
ATOM   9546  C C   . ASN C 1 419 ? -8.305  -30.128 -2.053  1.00 126.64 ? 428  ASN C C   1 
ATOM   9547  O O   . ASN C 1 419 ? -7.568  -31.122 -1.953  1.00 129.67 ? 428  ASN C O   1 
ATOM   9548  C CB  . ASN C 1 419 ? -9.888  -30.814 -0.198  1.00 128.84 ? 428  ASN C CB  1 
ATOM   9549  C CG  . ASN C 1 419 ? -11.395 -30.589 -0.206  1.00 128.34 ? 428  ASN C CG  1 
ATOM   9550  O OD1 . ASN C 1 419 ? -11.929 -29.895 0.656   1.00 123.04 ? 428  ASN C OD1 1 
ATOM   9551  N ND2 . ASN C 1 419 ? -12.086 -31.202 -1.163  1.00 131.06 ? 428  ASN C ND2 1 
ATOM   9552  N N   . ARG C 1 420 ? -8.467  -29.439 -3.193  1.00 125.14 ? 429  ARG C N   1 
ATOM   9553  C CA  . ARG C 1 420 ? -7.755  -29.757 -4.454  1.00 126.34 ? 429  ARG C CA  1 
ATOM   9554  C C   . ARG C 1 420 ? -8.482  -30.740 -5.398  1.00 130.84 ? 429  ARG C C   1 
ATOM   9555  O O   . ARG C 1 420 ? -8.058  -30.883 -6.554  1.00 132.34 ? 429  ARG C O   1 
ATOM   9556  C CB  . ARG C 1 420 ? -6.308  -30.229 -4.205  1.00 126.70 ? 429  ARG C CB  1 
ATOM   9557  C CG  . ARG C 1 420 ? -5.406  -29.200 -3.553  1.00 123.06 ? 429  ARG C CG  1 
ATOM   9558  C CD  . ARG C 1 420 ? -4.380  -28.663 -4.528  1.00 124.77 ? 429  ARG C CD  1 
ATOM   9559  N NE  . ARG C 1 420 ? -3.709  -27.473 -3.997  1.00 123.64 ? 429  ARG C NE  1 
ATOM   9560  C CZ  . ARG C 1 420 ? -2.827  -27.452 -2.988  1.00 123.74 ? 429  ARG C CZ  1 
ATOM   9561  N NH1 . ARG C 1 420 ? -2.480  -28.576 -2.354  1.00 126.41 ? 429  ARG C NH1 1 
ATOM   9562  N NH2 . ARG C 1 420 ? -2.286  -26.288 -2.604  1.00 119.79 ? 429  ARG C NH2 1 
ATOM   9563  N N   . GLY C 1 421 ? -9.540  -31.429 -4.930  1.00 133.24 ? 430  GLY C N   1 
ATOM   9564  C CA  . GLY C 1 421 ? -10.473 -32.114 -5.845  1.00 136.14 ? 430  GLY C CA  1 
ATOM   9565  C C   . GLY C 1 421 ? -10.854 -31.168 -6.985  1.00 133.37 ? 430  GLY C C   1 
ATOM   9566  O O   . GLY C 1 421 ? -11.261 -30.035 -6.747  1.00 129.90 ? 430  GLY C O   1 
ATOM   9567  N N   . ILE C 1 422 ? -10.694 -31.605 -8.226  1.00 134.89 ? 431  ILE C N   1 
ATOM   9568  C CA  . ILE C 1 422 ? -10.914 -30.738 -9.388  1.00 132.19 ? 431  ILE C CA  1 
ATOM   9569  C C   . ILE C 1 422 ? -12.400 -30.569 -9.691  1.00 133.12 ? 431  ILE C C   1 
ATOM   9570  O O   . ILE C 1 422 ? -13.068 -31.560 -9.902  1.00 137.43 ? 431  ILE C O   1 
ATOM   9571  C CB  . ILE C 1 422 ? -10.226 -31.358 -10.612 1.00 134.62 ? 431  ILE C CB  1 
ATOM   9572  C CG1 . ILE C 1 422 ? -8.707  -31.280 -10.451 1.00 133.32 ? 431  ILE C CG1 1 
ATOM   9573  C CG2 . ILE C 1 422 ? -10.699 -30.711 -11.912 1.00 133.22 ? 431  ILE C CG2 1 
ATOM   9574  C CD1 . ILE C 1 422 ? -8.043  -32.599 -10.071 1.00 138.26 ? 431  ILE C CD1 1 
ATOM   9575  N N   . ILE C 1 423 ? -12.928 -29.344 -9.732  1.00 129.50 ? 432  ILE C N   1 
ATOM   9576  C CA  . ILE C 1 423 ? -14.374 -29.176 -10.022 1.00 131.23 ? 432  ILE C CA  1 
ATOM   9577  C C   . ILE C 1 423 ? -14.717 -28.927 -11.489 1.00 131.91 ? 432  ILE C C   1 
ATOM   9578  O O   . ILE C 1 423 ? -15.603 -29.574 -12.050 1.00 135.88 ? 432  ILE C O   1 
ATOM   9579  C CB  . ILE C 1 423 ? -15.090 -28.036 -9.233  1.00 127.59 ? 432  ILE C CB  1 
ATOM   9580  C CG1 . ILE C 1 423 ? -14.339 -27.610 -7.964  1.00 124.89 ? 432  ILE C CG1 1 
ATOM   9581  C CG2 . ILE C 1 423 ? -16.563 -28.431 -8.974  1.00 131.18 ? 432  ILE C CG2 1 
ATOM   9582  C CD1 . ILE C 1 423 ? -14.871 -26.297 -7.336  1.00 121.85 ? 432  ILE C CD1 1 
ATOM   9583  N N   . LYS C 1 424 ? -14.056 -27.947 -12.086 1.00 128.31 ? 433  LYS C N   1 
ATOM   9584  C CA  . LYS C 1 424 ? -14.369 -27.561 -13.440 1.00 128.65 ? 433  LYS C CA  1 
ATOM   9585  C C   . LYS C 1 424 ? -13.160 -27.868 -14.305 1.00 128.79 ? 433  LYS C C   1 
ATOM   9586  O O   . LYS C 1 424 ? -12.043 -28.035 -13.809 1.00 127.75 ? 433  LYS C O   1 
ATOM   9587  C CB  . LYS C 1 424 ? -14.775 -26.075 -13.490 1.00 124.40 ? 433  LYS C CB  1 
ATOM   9588  C CG  . LYS C 1 424 ? -15.386 -25.612 -14.817 1.00 126.54 ? 433  LYS C CG  1 
ATOM   9589  C CD  . LYS C 1 424 ? -16.250 -24.344 -14.703 1.00 125.73 ? 433  LYS C CD  1 
ATOM   9590  C CE  . LYS C 1 424 ? -16.679 -23.886 -16.098 1.00 127.20 ? 433  LYS C CE  1 
ATOM   9591  N NZ  . LYS C 1 424 ? -18.119 -23.517 -16.199 1.00 128.53 ? 433  LYS C NZ  1 
ATOM   9592  N N   . THR C 1 425 ? -13.398 -27.984 -15.599 1.00 130.33 ? 434  THR C N   1 
ATOM   9593  C CA  . THR C 1 425 ? -12.319 -28.134 -16.547 1.00 130.72 ? 434  THR C CA  1 
ATOM   9594  C C   . THR C 1 425 ? -12.718 -27.403 -17.833 1.00 129.73 ? 434  THR C C   1 
ATOM   9595  O O   . THR C 1 425 ? -13.874 -27.442 -18.230 1.00 131.46 ? 434  THR C O   1 
ATOM   9596  C CB  . THR C 1 425 ? -11.945 -29.603 -16.723 1.00 135.74 ? 434  THR C CB  1 
ATOM   9597  O OG1 . THR C 1 425 ? -11.216 -29.761 -17.936 1.00 136.85 ? 434  THR C OG1 1 
ATOM   9598  C CG2 . THR C 1 425 ? -13.186 -30.491 -16.737 1.00 140.73 ? 434  THR C CG2 1 
ATOM   9599  N N   . PHE C 1 426 ? -11.770 -26.723 -18.468 1.00 127.40 ? 435  PHE C N   1 
ATOM   9600  C CA  . PHE C 1 426 ? -12.119 -25.517 -19.225 1.00 124.95 ? 435  PHE C CA  1 
ATOM   9601  C C   . PHE C 1 426 ? -12.263 -25.544 -20.706 1.00 127.47 ? 435  PHE C C   1 
ATOM   9602  O O   . PHE C 1 426 ? -11.310 -25.751 -21.445 1.00 128.26 ? 435  PHE C O   1 
ATOM   9603  C CB  . PHE C 1 426 ? -11.248 -24.343 -18.828 1.00 119.73 ? 435  PHE C CB  1 
ATOM   9604  C CG  . PHE C 1 426 ? -11.713 -23.681 -17.584 1.00 116.10 ? 435  PHE C CG  1 
ATOM   9605  C CD1 . PHE C 1 426 ? -10.936 -23.709 -16.425 1.00 113.55 ? 435  PHE C CD1 1 
ATOM   9606  C CD2 . PHE C 1 426 ? -12.963 -23.079 -17.547 1.00 114.79 ? 435  PHE C CD2 1 
ATOM   9607  C CE1 . PHE C 1 426 ? -11.383 -23.118 -15.253 1.00 109.65 ? 435  PHE C CE1 1 
ATOM   9608  C CE2 . PHE C 1 426 ? -13.420 -22.482 -16.384 1.00 111.87 ? 435  PHE C CE2 1 
ATOM   9609  C CZ  . PHE C 1 426 ? -12.627 -22.500 -15.232 1.00 109.03 ? 435  PHE C CZ  1 
ATOM   9610  N N   . SER C 1 427 ? -13.477 -25.211 -21.110 1.00 128.85 ? 436  SER C N   1 
ATOM   9611  C CA  . SER C 1 427 ? -13.919 -25.372 -22.472 1.00 132.06 ? 436  SER C CA  1 
ATOM   9612  C C   . SER C 1 427 ? -13.420 -24.236 -23.366 1.00 128.83 ? 436  SER C C   1 
ATOM   9613  O O   . SER C 1 427 ? -14.183 -23.344 -23.746 1.00 126.98 ? 436  SER C O   1 
ATOM   9614  C CB  . SER C 1 427 ? -15.448 -25.485 -22.504 1.00 134.21 ? 436  SER C CB  1 
ATOM   9615  O OG  . SER C 1 427 ? -15.894 -26.126 -23.683 1.00 138.85 ? 436  SER C OG  1 
ATOM   9616  N N   . ASN C 1 428 ? -12.123 -24.263 -23.667 1.00 128.14 ? 437  ASN C N   1 
ATOM   9617  C CA  . ASN C 1 428 ? -11.540 -23.499 -24.787 1.00 126.22 ? 437  ASN C CA  1 
ATOM   9618  C C   . ASN C 1 428 ? -12.172 -22.103 -25.021 1.00 121.61 ? 437  ASN C C   1 
ATOM   9619  O O   . ASN C 1 428 ? -12.448 -21.688 -26.155 1.00 121.30 ? 437  ASN C O   1 
ATOM   9620  C CB  . ASN C 1 428 ? -11.550 -24.379 -26.069 1.00 131.05 ? 437  ASN C CB  1 
ATOM   9621  C CG  . ASN C 1 428 ? -10.530 -23.928 -27.121 1.00 130.98 ? 437  ASN C CG  1 
ATOM   9622  O OD1 . ASN C 1 428 ? -9.356  -23.687 -26.824 1.00 130.82 ? 437  ASN C OD1 1 
ATOM   9623  N ND2 . ASN C 1 428 ? -10.982 -23.835 -28.364 1.00 133.25 ? 437  ASN C ND2 1 
ATOM   9624  N N   . GLY C 1 429 ? -12.393 -21.385 -23.928 1.00 117.83 ? 438  GLY C N   1 
ATOM   9625  C CA  . GLY C 1 429 ? -13.004 -20.061 -23.994 1.00 113.77 ? 438  GLY C CA  1 
ATOM   9626  C C   . GLY C 1 429 ? -12.516 -19.126 -22.892 1.00 109.18 ? 438  GLY C C   1 
ATOM   9627  O O   . GLY C 1 429 ? -11.325 -19.079 -22.586 1.00 108.05 ? 438  GLY C O   1 
ATOM   9628  N N   . CYS C 1 430 ? -13.435 -18.380 -22.290 1.00 106.45 ? 439  CYS C N   1 
ATOM   9629  C CA  . CYS C 1 430 ? -13.084 -17.483 -21.206 1.00 101.81 ? 439  CYS C CA  1 
ATOM   9630  C C   . CYS C 1 430 ? -14.197 -17.414 -20.149 1.00 101.15 ? 439  CYS C C   1 
ATOM   9631  O O   . CYS C 1 430 ? -15.292 -16.933 -20.426 1.00 100.94 ? 439  CYS C O   1 
ATOM   9632  C CB  . CYS C 1 430 ? -12.730 -16.112 -21.785 1.00 98.18  ? 439  CYS C CB  1 
ATOM   9633  S SG  . CYS C 1 430 ? -13.284 -14.670 -20.825 1.00 95.15  ? 439  CYS C SG  1 
ATOM   9634  N N   . ASP C 1 431 ? -13.904 -17.906 -18.944 1.00 100.66 ? 440  ASP C N   1 
ATOM   9635  C CA  . ASP C 1 431 ? -14.898 -18.067 -17.866 1.00 100.82 ? 440  ASP C CA  1 
ATOM   9636  C C   . ASP C 1 431 ? -14.470 -17.350 -16.594 1.00 96.23  ? 440  ASP C C   1 
ATOM   9637  O O   . ASP C 1 431 ? -13.341 -16.925 -16.479 1.00 93.94  ? 440  ASP C O   1 
ATOM   9638  C CB  . ASP C 1 431 ? -15.096 -19.563 -17.540 1.00 105.93 ? 440  ASP C CB  1 
ATOM   9639  C CG  . ASP C 1 431 ? -16.464 -20.119 -17.984 1.00 111.69 ? 440  ASP C CG  1 
ATOM   9640  O OD1 . ASP C 1 431 ? -17.469 -19.888 -17.270 1.00 113.43 ? 440  ASP C OD1 1 
ATOM   9641  O OD2 . ASP C 1 431 ? -16.523 -20.832 -19.018 1.00 117.12 ? 440  ASP C OD2 1 
ATOM   9642  N N   . TYR C 1 432 ? -15.377 -17.262 -15.630 1.00 94.96  ? 441  TYR C N   1 
ATOM   9643  C CA  . TYR C 1 432 ? -15.138 -16.659 -14.324 1.00 91.06  ? 441  TYR C CA  1 
ATOM   9644  C C   . TYR C 1 432 ? -15.431 -17.709 -13.262 1.00 93.23  ? 441  TYR C C   1 
ATOM   9645  O O   . TYR C 1 432 ? -16.240 -18.583 -13.501 1.00 97.08  ? 441  TYR C O   1 
ATOM   9646  C CB  . TYR C 1 432 ? -16.105 -15.494 -14.165 1.00 88.63  ? 441  TYR C CB  1 
ATOM   9647  C CG  . TYR C 1 432 ? -16.094 -14.817 -12.823 1.00 85.70  ? 441  TYR C CG  1 
ATOM   9648  C CD1 . TYR C 1 432 ? -15.226 -13.754 -12.577 1.00 82.62  ? 441  TYR C CD1 1 
ATOM   9649  C CD2 . TYR C 1 432 ? -16.952 -15.210 -11.803 1.00 86.89  ? 441  TYR C CD2 1 
ATOM   9650  C CE1 . TYR C 1 432 ? -15.183 -13.093 -11.327 1.00 79.73  ? 441  TYR C CE1 1 
ATOM   9651  C CE2 . TYR C 1 432 ? -16.938 -14.565 -10.551 1.00 84.99  ? 441  TYR C CE2 1 
ATOM   9652  C CZ  . TYR C 1 432 ? -16.039 -13.502 -10.319 1.00 81.00  ? 441  TYR C CZ  1 
ATOM   9653  O OH  . TYR C 1 432 ? -15.974 -12.831 -9.107  1.00 77.56  ? 441  TYR C OH  1 
ATOM   9654  N N   . VAL C 1 433 ? -14.806 -17.638 -12.095 1.00 91.28  ? 442  VAL C N   1 
ATOM   9655  C CA  . VAL C 1 433 ? -15.180 -18.518 -10.971 1.00 93.63  ? 442  VAL C CA  1 
ATOM   9656  C C   . VAL C 1 433 ? -15.158 -17.700 -9.693  1.00 90.87  ? 442  VAL C C   1 
ATOM   9657  O O   . VAL C 1 433 ? -14.746 -16.556 -9.745  1.00 87.78  ? 442  VAL C O   1 
ATOM   9658  C CB  . VAL C 1 433 ? -14.231 -19.713 -10.826 1.00 95.74  ? 442  VAL C CB  1 
ATOM   9659  C CG1 . VAL C 1 433 ? -14.501 -20.748 -11.880 1.00 100.24 ? 442  VAL C CG1 1 
ATOM   9660  C CG2 . VAL C 1 433 ? -12.810 -19.266 -10.912 1.00 92.86  ? 442  VAL C CG2 1 
ATOM   9661  N N   . SER C 1 434 ? -15.574 -18.255 -8.550  1.00 92.53  ? 443  SER C N   1 
ATOM   9662  C CA  . SER C 1 434 ? -15.527 -17.482 -7.285  1.00 90.12  ? 443  SER C CA  1 
ATOM   9663  C C   . SER C 1 434 ? -15.096 -18.235 -6.021  1.00 91.62  ? 443  SER C C   1 
ATOM   9664  O O   . SER C 1 434 ? -15.045 -19.460 -6.030  1.00 95.21  ? 443  SER C O   1 
ATOM   9665  C CB  . SER C 1 434 ? -16.851 -16.755 -7.053  1.00 89.53  ? 443  SER C CB  1 
ATOM   9666  O OG  . SER C 1 434 ? -17.437 -17.168 -5.840  1.00 90.26  ? 443  SER C OG  1 
ATOM   9667  N N   . ASN C 1 435 ? -14.791 -17.494 -4.950  1.00 89.47  ? 444  ASN C N   1 
ATOM   9668  C CA  . ASN C 1 435 ? -14.383 -18.076 -3.660  1.00 90.86  ? 444  ASN C CA  1 
ATOM   9669  C C   . ASN C 1 435 ? -15.527 -18.793 -2.962  1.00 94.75  ? 444  ASN C C   1 
ATOM   9670  O O   . ASN C 1 435 ? -16.698 -18.411 -3.095  1.00 94.83  ? 444  ASN C O   1 
ATOM   9671  C CB  . ASN C 1 435 ? -13.813 -17.016 -2.747  1.00 86.91  ? 444  ASN C CB  1 
ATOM   9672  C CG  . ASN C 1 435 ? -13.377 -15.810 -3.504  1.00 84.55  ? 444  ASN C CG  1 
ATOM   9673  O OD1 . ASN C 1 435 ? -13.088 -15.887 -4.695  1.00 87.22  ? 444  ASN C OD1 1 
ATOM   9674  N ND2 . ASN C 1 435 ? -13.343 -14.675 -2.834  1.00 82.09  ? 444  ASN C ND2 1 
ATOM   9675  N N   . LYS C 1 436 ? -15.155 -19.792 -2.162  1.00 98.09  ? 445  LYS C N   1 
ATOM   9676  C CA  . LYS C 1 436 ? -15.928 -21.032 -2.010  1.00 103.98 ? 445  LYS C CA  1 
ATOM   9677  C C   . LYS C 1 436 ? -16.431 -21.444 -3.381  1.00 106.44 ? 445  LYS C C   1 
ATOM   9678  O O   . LYS C 1 436 ? -16.854 -20.606 -4.176  1.00 105.19 ? 445  LYS C O   1 
ATOM   9679  C CB  . LYS C 1 436 ? -17.041 -20.974 -0.947  1.00 105.59 ? 445  LYS C CB  1 
ATOM   9680  C CG  . LYS C 1 436 ? -17.891 -22.326 -0.711  1.00 113.18 ? 445  LYS C CG  1 
ATOM   9681  C CD  . LYS C 1 436 ? -17.166 -23.744 -0.571  1.00 119.38 ? 445  LYS C CD  1 
ATOM   9682  C CE  . LYS C 1 436 ? -15.611 -23.760 -0.399  1.00 118.37 ? 445  LYS C CE  1 
ATOM   9683  N NZ  . LYS C 1 436 ? -14.981 -22.738 0.525   1.00 114.31 ? 445  LYS C NZ  1 
ATOM   9684  N N   . GLY C 1 437 ? -16.380 -22.744 -3.641  1.00 110.46 ? 446  GLY C N   1 
ATOM   9685  C CA  . GLY C 1 437 ? -16.273 -23.237 -4.997  1.00 112.02 ? 446  GLY C CA  1 
ATOM   9686  C C   . GLY C 1 437 ? -14.768 -23.297 -5.175  1.00 109.81 ? 446  GLY C C   1 
ATOM   9687  O O   . GLY C 1 437 ? -14.127 -24.238 -4.686  1.00 112.14 ? 446  GLY C O   1 
ATOM   9688  N N   . VAL C 1 438 ? -14.195 -22.253 -5.781  1.00 105.20 ? 447  VAL C N   1 
ATOM   9689  C CA  . VAL C 1 438 ? -12.827 -22.328 -6.288  1.00 103.23 ? 447  VAL C CA  1 
ATOM   9690  C C   . VAL C 1 438 ? -11.753 -21.765 -5.372  1.00 99.31  ? 447  VAL C C   1 
ATOM   9691  O O   . VAL C 1 438 ? -11.925 -20.722 -4.741  1.00 96.12  ? 447  VAL C O   1 
ATOM   9692  C CB  . VAL C 1 438 ? -12.709 -21.700 -7.668  1.00 101.92 ? 447  VAL C CB  1 
ATOM   9693  C CG1 . VAL C 1 438 ? -11.466 -22.206 -8.352  1.00 102.85 ? 447  VAL C CG1 1 
ATOM   9694  C CG2 . VAL C 1 438 ? -13.912 -22.054 -8.487  1.00 105.16 ? 447  VAL C CG2 1 
ATOM   9695  N N   . ASP C 1 439 ? -10.636 -22.478 -5.343  1.00 99.66  ? 448  ASP C N   1 
ATOM   9696  C CA  . ASP C 1 439 ? -9.532  -22.181 -4.479  1.00 96.83  ? 448  ASP C CA  1 
ATOM   9697  C C   . ASP C 1 439 ? -8.268  -22.031 -5.318  1.00 95.10  ? 448  ASP C C   1 
ATOM   9698  O O   . ASP C 1 439 ? -7.323  -21.316 -4.945  1.00 91.76  ? 448  ASP C O   1 
ATOM   9699  C CB  . ASP C 1 439 ? -9.374  -23.332 -3.513  1.00 99.89  ? 448  ASP C CB  1 
ATOM   9700  C CG  . ASP C 1 439 ? -8.919  -22.887 -2.164  1.00 99.98  ? 448  ASP C CG  1 
ATOM   9701  O OD1 . ASP C 1 439 ? -8.083  -21.960 -2.092  1.00 99.01  ? 448  ASP C OD1 1 
ATOM   9702  O OD2 . ASP C 1 439 ? -9.385  -23.460 -1.162  1.00 104.58 ? 448  ASP C OD2 1 
ATOM   9703  N N   . THR C 1 440 ? -8.289  -22.683 -6.476  1.00 97.08  ? 449  THR C N   1 
ATOM   9704  C CA  . THR C 1 440 ? -7.125  -22.856 -7.320  1.00 96.45  ? 449  THR C CA  1 
ATOM   9705  C C   . THR C 1 440 ? -7.557  -22.905 -8.755  1.00 97.61  ? 449  THR C C   1 
ATOM   9706  O O   . THR C 1 440 ? -8.544  -23.542 -9.068  1.00 100.86 ? 449  THR C O   1 
ATOM   9707  C CB  . THR C 1 440 ? -6.461  -24.205 -6.978  1.00 99.81  ? 449  THR C CB  1 
ATOM   9708  O OG1 . THR C 1 440 ? -5.410  -23.980 -6.047  1.00 97.05  ? 449  THR C OG1 1 
ATOM   9709  C CG2 . THR C 1 440 ? -5.887  -24.911 -8.208  1.00 103.07 ? 449  THR C CG2 1 
ATOM   9710  N N   . VAL C 1 441 ? -6.843  -22.226 -9.635  1.00 95.11  ? 450  VAL C N   1 
ATOM   9711  C CA  . VAL C 1 441 ? -6.941  -22.579 -11.035 1.00 97.02  ? 450  VAL C CA  1 
ATOM   9712  C C   . VAL C 1 441 ? -5.550  -22.858 -11.544 1.00 97.50  ? 450  VAL C C   1 
ATOM   9713  O O   . VAL C 1 441 ? -4.598  -22.233 -11.102 1.00 94.81  ? 450  VAL C O   1 
ATOM   9714  C CB  . VAL C 1 441 ? -7.670  -21.530 -11.911 1.00 94.75  ? 450  VAL C CB  1 
ATOM   9715  C CG1 . VAL C 1 441 ? -8.929  -21.057 -11.242 1.00 93.18  ? 450  VAL C CG1 1 
ATOM   9716  C CG2 . VAL C 1 441 ? -6.792  -20.378 -12.231 1.00 91.33  ? 450  VAL C CG2 1 
ATOM   9717  N N   . SER C 1 442 ? -5.425  -23.818 -12.444 1.00 101.33 ? 451  SER C N   1 
ATOM   9718  C CA  . SER C 1 442 ? -4.158  -24.064 -13.100 1.00 102.22 ? 451  SER C CA  1 
ATOM   9719  C C   . SER C 1 442 ? -4.329  -23.842 -14.574 1.00 102.68 ? 451  SER C C   1 
ATOM   9720  O O   . SER C 1 442 ? -5.331  -24.228 -15.151 1.00 105.08 ? 451  SER C O   1 
ATOM   9721  C CB  . SER C 1 442 ? -3.637  -25.467 -12.812 1.00 106.26 ? 451  SER C CB  1 
ATOM   9722  O OG  . SER C 1 442 ? -4.649  -26.256 -12.232 1.00 111.16 ? 451  SER C OG  1 
ATOM   9723  N N   . VAL C 1 443 ? -3.360  -23.164 -15.161 1.00 100.63 ? 452  VAL C N   1 
ATOM   9724  C CA  . VAL C 1 443 ? -3.286  -23.012 -16.590 1.00 101.27 ? 452  VAL C CA  1 
ATOM   9725  C C   . VAL C 1 443 ? -1.981  -23.657 -16.985 1.00 103.35 ? 452  VAL C C   1 
ATOM   9726  O O   . VAL C 1 443 ? -0.904  -23.216 -16.563 1.00 101.29 ? 452  VAL C O   1 
ATOM   9727  C CB  . VAL C 1 443 ? -3.256  -21.551 -17.004 1.00 96.87  ? 452  VAL C CB  1 
ATOM   9728  C CG1 . VAL C 1 443 ? -3.334  -21.454 -18.507 1.00 97.79  ? 452  VAL C CG1 1 
ATOM   9729  C CG2 . VAL C 1 443 ? -4.402  -20.809 -16.371 1.00 94.33  ? 452  VAL C CG2 1 
ATOM   9730  N N   . GLY C 1 444 ? -2.085  -24.713 -17.784 1.00 107.56 ? 453  GLY C N   1 
ATOM   9731  C CA  . GLY C 1 444 ? -0.929  -25.515 -18.129 1.00 110.07 ? 453  GLY C CA  1 
ATOM   9732  C C   . GLY C 1 444 ? -0.208  -25.850 -16.849 1.00 109.35 ? 453  GLY C C   1 
ATOM   9733  O O   . GLY C 1 444 ? -0.783  -26.438 -15.935 1.00 110.26 ? 453  GLY C O   1 
ATOM   9734  N N   . ASN C 1 445 ? 1.040   -25.423 -16.763 1.00 107.54 ? 454  ASN C N   1 
ATOM   9735  C CA  . ASN C 1 445 ? 1.846   -25.746 -15.605 1.00 107.42 ? 454  ASN C CA  1 
ATOM   9736  C C   . ASN C 1 445 ? 1.905   -24.691 -14.530 1.00 102.37 ? 454  ASN C C   1 
ATOM   9737  O O   . ASN C 1 445 ? 2.406   -24.938 -13.430 1.00 102.03 ? 454  ASN C O   1 
ATOM   9738  C CB  . ASN C 1 445 ? 3.239   -26.141 -16.034 1.00 109.43 ? 454  ASN C CB  1 
ATOM   9739  C CG  . ASN C 1 445 ? 3.345   -27.598 -16.245 1.00 116.32 ? 454  ASN C CG  1 
ATOM   9740  O OD1 . ASN C 1 445 ? 3.889   -28.302 -15.413 1.00 120.48 ? 454  ASN C OD1 1 
ATOM   9741  N ND2 . ASN C 1 445 ? 2.766   -28.083 -17.328 1.00 120.59 ? 454  ASN C ND2 1 
ATOM   9742  N N   . THR C 1 446 ? 1.385   -23.516 -14.860 1.00 98.44  ? 455  THR C N   1 
ATOM   9743  C CA  . THR C 1 446 ? 1.331   -22.415 -13.934 1.00 93.41  ? 455  THR C CA  1 
ATOM   9744  C C   . THR C 1 446 ? 0.116   -22.615 -13.064 1.00 92.91  ? 455  THR C C   1 
ATOM   9745  O O   . THR C 1 446 ? -0.950  -22.946 -13.560 1.00 94.55  ? 455  THR C O   1 
ATOM   9746  C CB  . THR C 1 446 ? 1.219   -21.077 -14.684 1.00 90.38  ? 455  THR C CB  1 
ATOM   9747  O OG1 . THR C 1 446 ? 2.215   -21.017 -15.710 1.00 91.40  ? 455  THR C OG1 1 
ATOM   9748  C CG2 . THR C 1 446 ? 1.430   -19.913 -13.743 1.00 86.33  ? 455  THR C CG2 1 
ATOM   9749  N N   . LEU C 1 447 ? 0.282   -22.409 -11.770 1.00 90.71  ? 456  LEU C N   1 
ATOM   9750  C CA  . LEU C 1 447 ? -0.812  -22.535 -10.839 1.00 90.81  ? 456  LEU C CA  1 
ATOM   9751  C C   . LEU C 1 447 ? -1.177  -21.194 -10.230 1.00 86.71  ? 456  LEU C C   1 
ATOM   9752  O O   . LEU C 1 447 ? -0.316  -20.508 -9.702  1.00 84.37  ? 456  LEU C O   1 
ATOM   9753  C CB  . LEU C 1 447 ? -0.409  -23.490 -9.730  1.00 92.66  ? 456  LEU C CB  1 
ATOM   9754  C CG  . LEU C 1 447 ? -1.499  -23.811 -8.716  1.00 93.13  ? 456  LEU C CG  1 
ATOM   9755  C CD1 . LEU C 1 447 ? -2.542  -24.720 -9.364  1.00 98.57  ? 456  LEU C CD1 1 
ATOM   9756  C CD2 . LEU C 1 447 ? -0.888  -24.467 -7.501  1.00 93.31  ? 456  LEU C CD2 1 
ATOM   9757  N N   . TYR C 1 448 ? -2.453  -20.830 -10.275 1.00 86.46  ? 457  TYR C N   1 
ATOM   9758  C CA  . TYR C 1 448 ? -2.914  -19.571 -9.681  1.00 82.91  ? 457  TYR C CA  1 
ATOM   9759  C C   . TYR C 1 448 ? -3.758  -19.856 -8.440  1.00 82.98  ? 457  TYR C C   1 
ATOM   9760  O O   . TYR C 1 448 ? -4.532  -20.811 -8.420  1.00 86.51  ? 457  TYR C O   1 
ATOM   9761  C CB  . TYR C 1 448 ? -3.713  -18.762 -10.711 1.00 82.07  ? 457  TYR C CB  1 
ATOM   9762  C CG  . TYR C 1 448 ? -2.918  -18.299 -11.921 1.00 82.56  ? 457  TYR C CG  1 
ATOM   9763  C CD1 . TYR C 1 448 ? -2.441  -19.196 -12.863 1.00 87.30  ? 457  TYR C CD1 1 
ATOM   9764  C CD2 . TYR C 1 448 ? -2.663  -16.957 -12.130 1.00 79.71  ? 457  TYR C CD2 1 
ATOM   9765  C CE1 . TYR C 1 448 ? -1.716  -18.757 -13.971 1.00 87.51  ? 457  TYR C CE1 1 
ATOM   9766  C CE2 . TYR C 1 448 ? -1.943  -16.512 -13.230 1.00 79.89  ? 457  TYR C CE2 1 
ATOM   9767  C CZ  . TYR C 1 448 ? -1.470  -17.411 -14.143 1.00 83.71  ? 457  TYR C CZ  1 
ATOM   9768  O OH  . TYR C 1 448 ? -0.764  -16.954 -15.235 1.00 83.65  ? 457  TYR C OH  1 
ATOM   9769  N N   . TYR C 1 449 ? -3.609  -19.039 -7.404  1.00 79.43  ? 458  TYR C N   1 
ATOM   9770  C CA  . TYR C 1 449 ? -4.353  -19.257 -6.160  1.00 79.33  ? 458  TYR C CA  1 
ATOM   9771  C C   . TYR C 1 449 ? -5.449  -18.232 -5.943  1.00 77.03  ? 458  TYR C C   1 
ATOM   9772  O O   . TYR C 1 449 ? -5.154  -17.061 -5.652  1.00 73.91  ? 458  TYR C O   1 
ATOM   9773  C CB  . TYR C 1 449 ? -3.426  -19.166 -4.964  1.00 77.64  ? 458  TYR C CB  1 
ATOM   9774  C CG  . TYR C 1 449 ? -2.361  -20.210 -4.920  1.00 79.83  ? 458  TYR C CG  1 
ATOM   9775  C CD1 . TYR C 1 449 ? -1.115  -19.968 -5.471  1.00 79.39  ? 458  TYR C CD1 1 
ATOM   9776  C CD2 . TYR C 1 449 ? -2.586  -21.432 -4.303  1.00 83.30  ? 458  TYR C CD2 1 
ATOM   9777  C CE1 . TYR C 1 449 ? -0.123  -20.913 -5.422  1.00 82.92  ? 458  TYR C CE1 1 
ATOM   9778  C CE2 . TYR C 1 449 ? -1.601  -22.387 -4.245  1.00 86.57  ? 458  TYR C CE2 1 
ATOM   9779  C CZ  . TYR C 1 449 ? -0.369  -22.121 -4.809  1.00 86.38  ? 458  TYR C CZ  1 
ATOM   9780  O OH  . TYR C 1 449 ? 0.626   -23.071 -4.763  1.00 89.30  ? 458  TYR C OH  1 
ATOM   9781  N N   . VAL C 1 450 ? -6.707  -18.664 -6.024  1.00 78.77  ? 459  VAL C N   1 
ATOM   9782  C CA  . VAL C 1 450 ? -7.821  -17.718 -5.928  1.00 76.88  ? 459  VAL C CA  1 
ATOM   9783  C C   . VAL C 1 450 ? -8.046  -17.218 -4.514  1.00 75.35  ? 459  VAL C C   1 
ATOM   9784  O O   . VAL C 1 450 ? -8.552  -16.114 -4.327  1.00 73.01  ? 459  VAL C O   1 
ATOM   9785  C CB  . VAL C 1 450 ? -9.103  -18.288 -6.478  1.00 79.45  ? 459  VAL C CB  1 
ATOM   9786  C CG1 . VAL C 1 450 ? -10.166 -17.215 -6.548  1.00 77.77  ? 459  VAL C CG1 1 
ATOM   9787  C CG2 . VAL C 1 450 ? -8.847  -18.832 -7.842  1.00 81.33  ? 459  VAL C CG2 1 
ATOM   9788  N N   . ASN C 1 451 ? -7.664  -18.025 -3.530  1.00 77.05  ? 460  ASN C N   1 
ATOM   9789  C CA  . ASN C 1 451 ? -7.713  -17.609 -2.137  1.00 75.77  ? 460  ASN C CA  1 
ATOM   9790  C C   . ASN C 1 451 ? -6.338  -17.647 -1.483  1.00 74.79  ? 460  ASN C C   1 
ATOM   9791  O O   . ASN C 1 451 ? -5.401  -18.233 -2.014  1.00 75.89  ? 460  ASN C O   1 
ATOM   9792  C CB  . ASN C 1 451 ? -8.745  -18.438 -1.378  1.00 78.45  ? 460  ASN C CB  1 
ATOM   9793  C CG  . ASN C 1 451 ? -10.171 -18.078 -1.770  1.00 80.00  ? 460  ASN C CG  1 
ATOM   9794  O OD1 . ASN C 1 451 ? -10.561 -16.918 -1.731  1.00 79.16  ? 460  ASN C OD1 1 
ATOM   9795  N ND2 . ASN C 1 451 ? -10.947 -19.069 -2.157  1.00 84.78  ? 460  ASN C ND2 1 
ATOM   9796  N N   . LYS C 1 452 ? -6.190  -16.983 -0.353  1.00 73.10  ? 461  LYS C N   1 
ATOM   9797  C CA  . LYS C 1 452 ? -4.897  -16.987 0.280   1.00 72.72  ? 461  LYS C CA  1 
ATOM   9798  C C   . LYS C 1 452 ? -4.812  -18.274 1.017   1.00 76.01  ? 461  LYS C C   1 
ATOM   9799  O O   . LYS C 1 452 ? -5.792  -18.696 1.587   1.00 77.64  ? 461  LYS C O   1 
ATOM   9800  C CB  . LYS C 1 452 ? -4.780  -15.842 1.254   1.00 69.48  ? 461  LYS C CB  1 
ATOM   9801  C CG  . LYS C 1 452 ? -5.100  -14.515 0.638   1.00 68.03  ? 461  LYS C CG  1 
ATOM   9802  C CD  . LYS C 1 452 ? -4.490  -13.414 1.443   1.00 66.54  ? 461  LYS C CD  1 
ATOM   9803  C CE  . LYS C 1 452 ? -4.995  -12.083 0.949   1.00 66.18  ? 461  LYS C CE  1 
ATOM   9804  N NZ  . LYS C 1 452 ? -4.275  -10.996 1.638   1.00 65.02  ? 461  LYS C NZ  1 
ATOM   9805  N N   . GLN C 1 453 ? -3.653  -18.909 1.005   1.00 77.68  ? 462  GLN C N   1 
ATOM   9806  C CA  . GLN C 1 453 ? -3.510  -20.183 1.700   1.00 81.67  ? 462  GLN C CA  1 
ATOM   9807  C C   . GLN C 1 453 ? -3.095  -19.974 3.135   1.00 80.96  ? 462  GLN C C   1 
ATOM   9808  O O   . GLN C 1 453 ? -2.016  -19.452 3.417   1.00 78.73  ? 462  GLN C O   1 
ATOM   9809  C CB  . GLN C 1 453 ? -2.545  -21.108 0.973   1.00 83.73  ? 462  GLN C CB  1 
ATOM   9810  C CG  . GLN C 1 453 ? -2.942  -21.308 -0.478  1.00 86.67  ? 462  GLN C CG  1 
ATOM   9811  C CD  . GLN C 1 453 ? -4.366  -21.827 -0.633  1.00 91.26  ? 462  GLN C CD  1 
ATOM   9812  O OE1 . GLN C 1 453 ? -4.638  -22.993 -0.352  1.00 95.98  ? 462  GLN C OE1 1 
ATOM   9813  N NE2 . GLN C 1 453 ? -5.278  -20.960 -1.089  1.00 89.95  ? 462  GLN C NE2 1 
ATOM   9814  N N   . GLU C 1 454 ? -3.994  -20.355 4.038   1.00 83.63  ? 463  GLU C N   1 
ATOM   9815  C CA  . GLU C 1 454 ? -3.739  -20.343 5.478   1.00 84.19  ? 463  GLU C CA  1 
ATOM   9816  C C   . GLU C 1 454 ? -2.739  -21.424 5.816   1.00 86.07  ? 463  GLU C C   1 
ATOM   9817  O O   . GLU C 1 454 ? -2.725  -22.498 5.189   1.00 89.67  ? 463  GLU C O   1 
ATOM   9818  C CB  . GLU C 1 454 ? -5.018  -20.680 6.243   1.00 86.47  ? 463  GLU C CB  1 
ATOM   9819  C CG  . GLU C 1 454 ? -5.681  -19.529 7.024   1.00 87.77  ? 463  GLU C CG  1 
ATOM   9820  C CD  . GLU C 1 454 ? -7.086  -19.930 7.544   1.00 94.83  ? 463  GLU C CD  1 
ATOM   9821  O OE1 . GLU C 1 454 ? -7.189  -20.824 8.428   1.00 98.63  ? 463  GLU C OE1 1 
ATOM   9822  O OE2 . GLU C 1 454 ? -8.092  -19.356 7.056   1.00 95.48  ? 463  GLU C OE2 1 
ATOM   9823  N N   . GLY C 1 455 ? -1.936  -21.161 6.832   1.00 84.22  ? 464  GLY C N   1 
ATOM   9824  C CA  . GLY C 1 455 ? -1.014  -22.160 7.286   1.00 86.38  ? 464  GLY C CA  1 
ATOM   9825  C C   . GLY C 1 455 ? -0.437  -21.799 8.621   1.00 84.74  ? 464  GLY C C   1 
ATOM   9826  O O   . GLY C 1 455 ? -0.257  -20.623 8.939   1.00 81.68  ? 464  GLY C O   1 
ATOM   9827  N N   . LYS C 1 456 ? -0.211  -22.842 9.413   1.00 87.31  ? 465  LYS C N   1 
ATOM   9828  C CA  . LYS C 1 456 ? 0.675   -22.824 10.566  1.00 86.25  ? 465  LYS C CA  1 
ATOM   9829  C C   . LYS C 1 456 ? 0.766   -21.493 11.314  1.00 82.50  ? 465  LYS C C   1 
ATOM   9830  O O   . LYS C 1 456 ? 1.431   -20.553 10.871  1.00 79.86  ? 465  LYS C O   1 
ATOM   9831  C CB  . LYS C 1 456 ? 2.062   -23.289 10.117  1.00 86.60  ? 465  LYS C CB  1 
ATOM   9832  C CG  . LYS C 1 456 ? 2.921   -23.793 11.231  1.00 87.52  ? 465  LYS C CG  1 
ATOM   9833  C CD  . LYS C 1 456 ? 4.245   -24.353 10.728  1.00 90.63  ? 465  LYS C CD  1 
ATOM   9834  C CE  . LYS C 1 456 ? 5.029   -24.900 11.923  1.00 93.71  ? 465  LYS C CE  1 
ATOM   9835  N NZ  . LYS C 1 456 ? 6.517   -24.825 11.823  1.00 94.41  ? 465  LYS C NZ  1 
ATOM   9836  N N   . SER C 1 457 ? 0.096   -21.415 12.454  1.00 82.72  ? 466  SER C N   1 
ATOM   9837  C CA  . SER C 1 457 ? 0.330   -20.310 13.366  1.00 79.83  ? 466  SER C CA  1 
ATOM   9838  C C   . SER C 1 457 ? 1.644   -20.553 14.056  1.00 79.03  ? 466  SER C C   1 
ATOM   9839  O O   . SER C 1 457 ? 2.014   -21.685 14.348  1.00 81.20  ? 466  SER C O   1 
ATOM   9840  C CB  . SER C 1 457 ? -0.754  -20.224 14.423  1.00 80.44  ? 466  SER C CB  1 
ATOM   9841  O OG  . SER C 1 457 ? -0.860  -21.467 15.084  1.00 85.25  ? 466  SER C OG  1 
ATOM   9842  N N   . LEU C 1 458 ? 2.357   -19.478 14.305  1.00 76.09  ? 467  LEU C N   1 
ATOM   9843  C CA  . LEU C 1 458 ? 3.568   -19.581 15.053  1.00 75.73  ? 467  LEU C CA  1 
ATOM   9844  C C   . LEU C 1 458 ? 3.319   -18.837 16.319  1.00 74.25  ? 467  LEU C C   1 
ATOM   9845  O O   . LEU C 1 458 ? 2.622   -17.824 16.334  1.00 72.27  ? 467  LEU C O   1 
ATOM   9846  C CB  . LEU C 1 458 ? 4.742   -19.000 14.270  1.00 73.77  ? 467  LEU C CB  1 
ATOM   9847  C CG  . LEU C 1 458 ? 5.204   -19.944 13.155  1.00 75.98  ? 467  LEU C CG  1 
ATOM   9848  C CD1 . LEU C 1 458 ? 6.452   -19.393 12.490  1.00 73.72  ? 467  LEU C CD1 1 
ATOM   9849  C CD2 . LEU C 1 458 ? 5.452   -21.372 13.697  1.00 78.66  ? 467  LEU C CD2 1 
ATOM   9850  N N   . TYR C 1 459 ? 3.875   -19.359 17.394  1.00 75.70  ? 468  TYR C N   1 
ATOM   9851  C CA  . TYR C 1 459 ? 3.605   -18.804 18.692  1.00 75.31  ? 468  TYR C CA  1 
ATOM   9852  C C   . TYR C 1 459 ? 4.888   -18.571 19.493  1.00 73.03  ? 468  TYR C C   1 
ATOM   9853  O O   . TYR C 1 459 ? 5.769   -19.423 19.532  1.00 74.47  ? 468  TYR C O   1 
ATOM   9854  C CB  . TYR C 1 459 ? 2.645   -19.736 19.427  1.00 79.02  ? 468  TYR C CB  1 
ATOM   9855  C CG  . TYR C 1 459 ? 2.220   -19.203 20.785  1.00 82.93  ? 468  TYR C CG  1 
ATOM   9856  C CD1 . TYR C 1 459 ? 1.474   -18.016 20.885  1.00 84.15  ? 468  TYR C CD1 1 
ATOM   9857  C CD2 . TYR C 1 459 ? 2.564   -19.876 21.984  1.00 88.57  ? 468  TYR C CD2 1 
ATOM   9858  C CE1 . TYR C 1 459 ? 1.070   -17.500 22.143  1.00 84.74  ? 468  TYR C CE1 1 
ATOM   9859  C CE2 . TYR C 1 459 ? 2.164   -19.369 23.254  1.00 89.39  ? 468  TYR C CE2 1 
ATOM   9860  C CZ  . TYR C 1 459 ? 1.415   -18.178 23.318  1.00 87.17  ? 468  TYR C CZ  1 
ATOM   9861  O OH  . TYR C 1 459 ? 0.999   -17.665 24.532  1.00 86.49  ? 468  TYR C OH  1 
ATOM   9862  N N   . VAL C 1 460 ? 5.007   -17.419 20.130  1.00 69.91  ? 469  VAL C N   1 
ATOM   9863  C CA  . VAL C 1 460 ? 6.204   -17.176 20.902  1.00 68.81  ? 469  VAL C CA  1 
ATOM   9864  C C   . VAL C 1 460 ? 5.903   -16.722 22.311  1.00 68.78  ? 469  VAL C C   1 
ATOM   9865  O O   . VAL C 1 460 ? 5.477   -15.587 22.550  1.00 66.64  ? 469  VAL C O   1 
ATOM   9866  C CB  . VAL C 1 460 ? 7.131   -16.204 20.227  1.00 65.97  ? 469  VAL C CB  1 
ATOM   9867  C CG1 . VAL C 1 460 ? 8.196   -15.768 21.200  1.00 63.57  ? 469  VAL C CG1 1 
ATOM   9868  C CG2 . VAL C 1 460 ? 7.759   -16.861 19.020  1.00 67.14  ? 469  VAL C CG2 1 
ATOM   9869  N N   . LYS C 1 461 ? 6.167   -17.639 23.237  1.00 71.79  ? 470  LYS C N   1 
ATOM   9870  C CA  . LYS C 1 461 ? 5.804   -17.517 24.645  1.00 72.64  ? 470  LYS C CA  1 
ATOM   9871  C C   . LYS C 1 461 ? 6.803   -16.603 25.380  1.00 70.09  ? 470  LYS C C   1 
ATOM   9872  O O   . LYS C 1 461 ? 7.957   -16.456 24.964  1.00 69.03  ? 470  LYS C O   1 
ATOM   9873  C CB  . LYS C 1 461 ? 5.618   -18.949 25.249  1.00 76.22  ? 470  LYS C CB  1 
ATOM   9874  C CG  . LYS C 1 461 ? 6.100   -19.229 26.692  1.00 79.53  ? 470  LYS C CG  1 
ATOM   9875  C CD  . LYS C 1 461 ? 4.973   -19.470 27.742  1.00 84.69  ? 470  LYS C CD  1 
ATOM   9876  C CE  . LYS C 1 461 ? 5.547   -19.575 29.189  1.00 85.02  ? 470  LYS C CE  1 
ATOM   9877  N NZ  . LYS C 1 461 ? 4.705   -18.927 30.250  1.00 83.79  ? 470  LYS C NZ  1 
ATOM   9878  N N   . GLY C 1 462 ? 6.311   -15.931 26.417  1.00 69.38  ? 471  GLY C N   1 
ATOM   9879  C CA  . GLY C 1 462 ? 7.138   -15.210 27.375  1.00 68.41  ? 471  GLY C CA  1 
ATOM   9880  C C   . GLY C 1 462 ? 6.759   -15.657 28.780  1.00 70.57  ? 471  GLY C C   1 
ATOM   9881  O O   . GLY C 1 462 ? 5.607   -15.977 29.046  1.00 72.13  ? 471  GLY C O   1 
ATOM   9882  N N   . GLU C 1 463 ? 7.731   -15.713 29.682  1.00 71.10  ? 472  GLU C N   1 
ATOM   9883  C CA  . GLU C 1 463 ? 7.464   -15.911 31.118  1.00 72.85  ? 472  GLU C CA  1 
ATOM   9884  C C   . GLU C 1 463 ? 7.252   -14.501 31.789  1.00 69.99  ? 472  GLU C C   1 
ATOM   9885  O O   . GLU C 1 463 ? 7.242   -13.483 31.094  1.00 67.99  ? 472  GLU C O   1 
ATOM   9886  C CB  . GLU C 1 463 ? 8.585   -16.802 31.740  1.00 74.39  ? 472  GLU C CB  1 
ATOM   9887  C CG  . GLU C 1 463 ? 9.782   -16.123 32.535  1.00 76.52  ? 472  GLU C CG  1 
ATOM   9888  C CD  . GLU C 1 463 ? 10.457  -14.825 31.894  1.00 78.97  ? 472  GLU C CD  1 
ATOM   9889  O OE1 . GLU C 1 463 ? 10.614  -14.729 30.641  1.00 79.71  ? 472  GLU C OE1 1 
ATOM   9890  O OE2 . GLU C 1 463 ? 10.864  -13.899 32.671  1.00 78.41  ? 472  GLU C OE2 1 
ATOM   9891  N N   . PRO C 1 464 ? 7.041   -14.424 33.117  1.00 70.09  ? 473  PRO C N   1 
ATOM   9892  C CA  . PRO C 1 464 ? 7.109   -13.075 33.708  1.00 67.57  ? 473  PRO C CA  1 
ATOM   9893  C C   . PRO C 1 464 ? 8.375   -12.819 34.562  1.00 66.39  ? 473  PRO C C   1 
ATOM   9894  O O   . PRO C 1 464 ? 9.053   -13.753 35.021  1.00 67.29  ? 473  PRO C O   1 
ATOM   9895  C CB  . PRO C 1 464 ? 5.852   -13.007 34.566  1.00 68.54  ? 473  PRO C CB  1 
ATOM   9896  C CG  . PRO C 1 464 ? 5.631   -14.463 34.993  1.00 71.83  ? 473  PRO C CG  1 
ATOM   9897  C CD  . PRO C 1 464 ? 6.411   -15.379 34.041  1.00 72.64  ? 473  PRO C CD  1 
ATOM   9898  N N   . ILE C 1 465 ? 8.665   -11.546 34.793  1.00 64.37  ? 474  ILE C N   1 
ATOM   9899  C CA  . ILE C 1 465 ? 10.003  -11.135 35.191  1.00 63.41  ? 474  ILE C CA  1 
ATOM   9900  C C   . ILE C 1 465 ? 10.049  -10.496 36.597  1.00 63.09  ? 474  ILE C C   1 
ATOM   9901  O O   . ILE C 1 465 ? 9.162   -9.699  36.982  1.00 62.06  ? 474  ILE C O   1 
ATOM   9902  C CB  . ILE C 1 465 ? 10.636  -10.268 34.054  1.00 61.47  ? 474  ILE C CB  1 
ATOM   9903  C CG1 . ILE C 1 465 ? 12.073  -9.869  34.367  1.00 60.89  ? 474  ILE C CG1 1 
ATOM   9904  C CG2 . ILE C 1 465 ? 9.766   -9.062  33.710  1.00 59.51  ? 474  ILE C CG2 1 
ATOM   9905  C CD1 . ILE C 1 465 ? 12.791  -9.309  33.143  1.00 60.76  ? 474  ILE C CD1 1 
ATOM   9906  N N   . ILE C 1 466 ? 11.122  -10.843 37.321  1.00 64.15  ? 475  ILE C N   1 
ATOM   9907  C CA  . ILE C 1 466 ? 11.191  -10.799 38.804  1.00 65.25  ? 475  ILE C CA  1 
ATOM   9908  C C   . ILE C 1 466 ? 11.893  -9.602  39.500  1.00 63.92  ? 475  ILE C C   1 
ATOM   9909  O O   . ILE C 1 466 ? 13.118  -9.467  39.426  1.00 62.59  ? 475  ILE C O   1 
ATOM   9910  C CB  . ILE C 1 466 ? 11.773  -12.163 39.354  1.00 67.34  ? 475  ILE C CB  1 
ATOM   9911  C CG1 . ILE C 1 466 ? 13.035  -12.586 38.557  1.00 68.20  ? 475  ILE C CG1 1 
ATOM   9912  C CG2 . ILE C 1 466 ? 10.689  -13.276 39.321  1.00 67.95  ? 475  ILE C CG2 1 
ATOM   9913  C CD1 . ILE C 1 466 ? 14.248  -13.045 39.413  1.00 68.80  ? 475  ILE C CD1 1 
ATOM   9914  N N   . ASN C 1 467 ? 11.108  -8.747  40.170  1.00 64.54  ? 476  ASN C N   1 
ATOM   9915  C CA  . ASN C 1 467 ? 11.675  -7.652  40.996  1.00 64.46  ? 476  ASN C CA  1 
ATOM   9916  C C   . ASN C 1 467 ? 12.008  -8.075  42.452  1.00 65.95  ? 476  ASN C C   1 
ATOM   9917  O O   . ASN C 1 467 ? 11.194  -7.999  43.385  1.00 66.85  ? 476  ASN C O   1 
ATOM   9918  C CB  . ASN C 1 467 ? 10.867  -6.329  40.917  1.00 63.27  ? 476  ASN C CB  1 
ATOM   9919  C CG  . ASN C 1 467 ? 11.724  -5.087  41.297  1.00 62.42  ? 476  ASN C CG  1 
ATOM   9920  O OD1 . ASN C 1 467 ? 12.951  -5.076  41.089  1.00 62.18  ? 476  ASN C OD1 1 
ATOM   9921  N ND2 . ASN C 1 467 ? 11.072  -4.046  41.853  1.00 61.55  ? 476  ASN C ND2 1 
ATOM   9922  N N   . PHE C 1 468 ? 13.280  -8.411  42.607  1.00 66.41  ? 477  PHE C N   1 
ATOM   9923  C CA  . PHE C 1 468 ? 13.817  -9.502  43.432  1.00 68.47  ? 477  PHE C CA  1 
ATOM   9924  C C   . PHE C 1 468 ? 14.579  -9.037  44.682  1.00 67.61  ? 477  PHE C C   1 
ATOM   9925  O O   . PHE C 1 468 ? 15.637  -9.619  45.006  1.00 68.34  ? 477  PHE C O   1 
ATOM   9926  C CB  . PHE C 1 468 ? 14.858  -10.139 42.508  1.00 69.07  ? 477  PHE C CB  1 
ATOM   9927  C CG  . PHE C 1 468 ? 15.592  -9.089  41.658  1.00 68.59  ? 477  PHE C CG  1 
ATOM   9928  C CD1 . PHE C 1 468 ? 16.738  -8.438  42.159  1.00 68.27  ? 477  PHE C CD1 1 
ATOM   9929  C CD2 . PHE C 1 468 ? 15.077  -8.691  40.405  1.00 67.13  ? 477  PHE C CD2 1 
ATOM   9930  C CE1 . PHE C 1 468 ? 17.375  -7.457  41.410  1.00 66.86  ? 477  PHE C CE1 1 
ATOM   9931  C CE2 . PHE C 1 468 ? 15.704  -7.712  39.645  1.00 65.45  ? 477  PHE C CE2 1 
ATOM   9932  C CZ  . PHE C 1 468 ? 16.856  -7.093  40.142  1.00 65.58  ? 477  PHE C CZ  1 
ATOM   9933  N N   . TYR C 1 469 ? 14.079  -8.007  45.370  1.00 66.09  ? 478  TYR C N   1 
ATOM   9934  C CA  . TYR C 1 469 ? 14.918  -7.257  46.337  1.00 64.32  ? 478  TYR C CA  1 
ATOM   9935  C C   . TYR C 1 469 ? 14.846  -7.681  47.838  1.00 64.69  ? 478  TYR C C   1 
ATOM   9936  O O   . TYR C 1 469 ? 13.775  -8.040  48.383  1.00 65.52  ? 478  TYR C O   1 
ATOM   9937  C CB  . TYR C 1 469 ? 14.772  -5.727  46.101  1.00 62.76  ? 478  TYR C CB  1 
ATOM   9938  C CG  . TYR C 1 469 ? 14.640  -4.880  47.347  1.00 62.38  ? 478  TYR C CG  1 
ATOM   9939  C CD1 . TYR C 1 469 ? 15.767  -4.332  47.970  1.00 60.84  ? 478  TYR C CD1 1 
ATOM   9940  C CD2 . TYR C 1 469 ? 13.373  -4.628  47.901  1.00 63.18  ? 478  TYR C CD2 1 
ATOM   9941  C CE1 . TYR C 1 469 ? 15.633  -3.565  49.118  1.00 61.77  ? 478  TYR C CE1 1 
ATOM   9942  C CE2 . TYR C 1 469 ? 13.228  -3.871  49.050  1.00 63.55  ? 478  TYR C CE2 1 
ATOM   9943  C CZ  . TYR C 1 469 ? 14.352  -3.338  49.658  1.00 63.25  ? 478  TYR C CZ  1 
ATOM   9944  O OH  . TYR C 1 469 ? 14.169  -2.582  50.802  1.00 63.83  ? 478  TYR C OH  1 
ATOM   9945  N N   . ASP C 1 470 ? 16.010  -7.645  48.488  1.00 63.38  ? 479  ASP C N   1 
ATOM   9946  C CA  . ASP C 1 470 ? 16.124  -8.146  49.854  1.00 63.87  ? 479  ASP C CA  1 
ATOM   9947  C C   . ASP C 1 470 ? 16.804  -7.227  50.880  1.00 61.97  ? 479  ASP C C   1 
ATOM   9948  O O   . ASP C 1 470 ? 18.027  -7.069  50.891  1.00 61.43  ? 479  ASP C O   1 
ATOM   9949  C CB  . ASP C 1 470 ? 16.778  -9.518  49.866  1.00 65.61  ? 479  ASP C CB  1 
ATOM   9950  C CG  . ASP C 1 470 ? 16.412  -10.290 51.094  1.00 69.12  ? 479  ASP C CG  1 
ATOM   9951  O OD1 . ASP C 1 470 ? 15.266  -10.101 51.568  1.00 71.31  ? 479  ASP C OD1 1 
ATOM   9952  O OD2 . ASP C 1 470 ? 17.253  -11.070 51.598  1.00 71.94  ? 479  ASP C OD2 1 
ATOM   9953  N N   . PRO C 1 471 ? 16.008  -6.639  51.777  1.00 61.12  ? 480  PRO C N   1 
ATOM   9954  C CA  . PRO C 1 471 ? 16.517  -5.549  52.579  1.00 59.22  ? 480  PRO C CA  1 
ATOM   9955  C C   . PRO C 1 471 ? 17.525  -6.061  53.568  1.00 59.07  ? 480  PRO C C   1 
ATOM   9956  O O   . PRO C 1 471 ? 17.494  -7.241  53.935  1.00 59.92  ? 480  PRO C O   1 
ATOM   9957  C CB  . PRO C 1 471 ? 15.283  -5.068  53.323  1.00 59.84  ? 480  PRO C CB  1 
ATOM   9958  C CG  . PRO C 1 471 ? 14.476  -6.319  53.509  1.00 62.30  ? 480  PRO C CG  1 
ATOM   9959  C CD  . PRO C 1 471 ? 14.690  -7.105  52.243  1.00 62.71  ? 480  PRO C CD  1 
ATOM   9960  N N   . LEU C 1 472 ? 18.427  -5.171  53.966  1.00 57.57  ? 481  LEU C N   1 
ATOM   9961  C CA  . LEU C 1 472 ? 19.356  -5.428  55.058  1.00 57.48  ? 481  LEU C CA  1 
ATOM   9962  C C   . LEU C 1 472 ? 18.755  -4.931  56.354  1.00 57.57  ? 481  LEU C C   1 
ATOM   9963  O O   . LEU C 1 472 ? 18.223  -3.828  56.412  1.00 56.81  ? 481  LEU C O   1 
ATOM   9964  C CB  . LEU C 1 472 ? 20.681  -4.726  54.796  1.00 56.01  ? 481  LEU C CB  1 
ATOM   9965  C CG  . LEU C 1 472 ? 21.867  -5.444  55.426  1.00 56.65  ? 481  LEU C CG  1 
ATOM   9966  C CD1 . LEU C 1 472 ? 21.604  -6.957  55.638  1.00 59.00  ? 481  LEU C CD1 1 
ATOM   9967  C CD2 . LEU C 1 472 ? 23.117  -5.218  54.593  1.00 54.13  ? 481  LEU C CD2 1 
ATOM   9968  N N   . VAL C 1 473 ? 18.812  -5.738  57.399  1.00 58.61  ? 482  VAL C N   1 
ATOM   9969  C CA  . VAL C 1 473 ? 18.257  -5.262  58.664  1.00 59.23  ? 482  VAL C CA  1 
ATOM   9970  C C   . VAL C 1 473 ? 19.070  -5.549  59.927  1.00 60.13  ? 482  VAL C C   1 
ATOM   9971  O O   . VAL C 1 473 ? 19.684  -6.629  60.073  1.00 61.19  ? 482  VAL C O   1 
ATOM   9972  C CB  . VAL C 1 473 ? 16.755  -5.585  58.806  1.00 60.35  ? 482  VAL C CB  1 
ATOM   9973  C CG1 . VAL C 1 473 ? 16.457  -6.443  60.050  1.00 61.12  ? 482  VAL C CG1 1 
ATOM   9974  C CG2 . VAL C 1 473 ? 15.939  -4.266  58.757  1.00 59.77  ? 482  VAL C CG2 1 
ATOM   9975  N N   . PHE C 1 474 ? 19.080  -4.570  60.830  1.00 59.55  ? 483  PHE C N   1 
ATOM   9976  C CA  . PHE C 1 474 ? 19.985  -4.638  61.955  1.00 59.68  ? 483  PHE C CA  1 
ATOM   9977  C C   . PHE C 1 474 ? 19.328  -5.021  63.281  1.00 61.30  ? 483  PHE C C   1 
ATOM   9978  O O   . PHE C 1 474 ? 18.274  -4.471  63.612  1.00 61.93  ? 483  PHE C O   1 
ATOM   9979  C CB  . PHE C 1 474 ? 20.739  -3.327  62.111  1.00 58.32  ? 483  PHE C CB  1 
ATOM   9980  C CG  . PHE C 1 474 ? 21.823  -3.412  63.116  1.00 58.23  ? 483  PHE C CG  1 
ATOM   9981  C CD1 . PHE C 1 474 ? 23.076  -3.835  62.749  1.00 56.94  ? 483  PHE C CD1 1 
ATOM   9982  C CD2 . PHE C 1 474 ? 21.567  -3.147  64.449  1.00 59.28  ? 483  PHE C CD2 1 
ATOM   9983  C CE1 . PHE C 1 474 ? 24.063  -3.950  63.680  1.00 57.39  ? 483  PHE C CE1 1 
ATOM   9984  C CE2 . PHE C 1 474 ? 22.545  -3.262  65.396  1.00 59.60  ? 483  PHE C CE2 1 
ATOM   9985  C CZ  . PHE C 1 474 ? 23.800  -3.657  65.013  1.00 59.08  ? 483  PHE C CZ  1 
ATOM   9986  N N   . PRO C 1 475 ? 19.968  -5.939  64.053  1.00 62.11  ? 484  PRO C N   1 
ATOM   9987  C CA  . PRO C 1 475 ? 19.540  -6.403  65.378  1.00 63.74  ? 484  PRO C CA  1 
ATOM   9988  C C   . PRO C 1 475 ? 19.382  -5.314  66.445  1.00 64.02  ? 484  PRO C C   1 
ATOM   9989  O O   . PRO C 1 475 ? 19.506  -5.600  67.630  1.00 65.44  ? 484  PRO C O   1 
ATOM   9990  C CB  . PRO C 1 475 ? 20.666  -7.367  65.787  1.00 64.32  ? 484  PRO C CB  1 
ATOM   9991  C CG  . PRO C 1 475 ? 21.790  -7.095  64.860  1.00 62.70  ? 484  PRO C CG  1 
ATOM   9992  C CD  . PRO C 1 475 ? 21.138  -6.703  63.588  1.00 61.82  ? 484  PRO C CD  1 
ATOM   9993  N N   . SER C 1 476 ? 19.063  -4.096  66.026  1.00 63.24  ? 485  SER C N   1 
ATOM   9994  C CA  . SER C 1 476 ? 19.051  -2.912  66.886  1.00 63.58  ? 485  SER C CA  1 
ATOM   9995  C C   . SER C 1 476 ? 18.627  -3.164  68.304  1.00 65.26  ? 485  SER C C   1 
ATOM   9996  O O   . SER C 1 476 ? 19.341  -2.831  69.236  1.00 65.54  ? 485  SER C O   1 
ATOM   9997  C CB  . SER C 1 476 ? 18.157  -1.820  66.292  1.00 63.18  ? 485  SER C CB  1 
ATOM   9998  O OG  . SER C 1 476 ? 17.927  -0.773  67.228  1.00 64.21  ? 485  SER C OG  1 
ATOM   9999  N N   . ASP C 1 477 ? 17.461  -3.754  68.475  1.00 66.70  ? 486  ASP C N   1 
ATOM   10000 C CA  . ASP C 1 477 ? 16.978  -3.949  69.815  1.00 69.01  ? 486  ASP C CA  1 
ATOM   10001 C C   . ASP C 1 477 ? 17.923  -4.782  70.687  1.00 69.83  ? 486  ASP C C   1 
ATOM   10002 O O   . ASP C 1 477 ? 18.329  -4.353  71.769  1.00 70.28  ? 486  ASP C O   1 
ATOM   10003 C CB  . ASP C 1 477 ? 15.567  -4.515  69.781  1.00 70.67  ? 486  ASP C CB  1 
ATOM   10004 C CG  . ASP C 1 477 ? 14.526  -3.428  69.604  1.00 71.56  ? 486  ASP C CG  1 
ATOM   10005 O OD1 . ASP C 1 477 ? 14.912  -2.242  69.535  1.00 71.23  ? 486  ASP C OD1 1 
ATOM   10006 O OD2 . ASP C 1 477 ? 13.321  -3.739  69.540  1.00 74.26  ? 486  ASP C OD2 1 
ATOM   10007 N N   . GLU C 1 478 ? 18.292  -5.955  70.189  1.00 69.95  ? 487  GLU C N   1 
ATOM   10008 C CA  . GLU C 1 478 ? 19.151  -6.872  70.911  1.00 70.85  ? 487  GLU C CA  1 
ATOM   10009 C C   . GLU C 1 478 ? 20.501  -6.232  71.283  1.00 69.05  ? 487  GLU C C   1 
ATOM   10010 O O   . GLU C 1 478 ? 21.071  -6.506  72.346  1.00 69.93  ? 487  GLU C O   1 
ATOM   10011 C CB  . GLU C 1 478 ? 19.361  -8.122  70.063  1.00 71.56  ? 487  GLU C CB  1 
ATOM   10012 C CG  . GLU C 1 478 ? 19.836  -9.348  70.853  1.00 76.15  ? 487  GLU C CG  1 
ATOM   10013 C CD  . GLU C 1 478 ? 20.960  -10.084 70.143  1.00 79.27  ? 487  GLU C CD  1 
ATOM   10014 O OE1 . GLU C 1 478 ? 21.587  -10.964 70.788  1.00 81.55  ? 487  GLU C OE1 1 
ATOM   10015 O OE2 . GLU C 1 478 ? 21.217  -9.757  68.951  1.00 78.68  ? 487  GLU C OE2 1 
ATOM   10016 N N   . PHE C 1 479 ? 21.000  -5.377  70.406  1.00 66.23  ? 488  PHE C N   1 
ATOM   10017 C CA  . PHE C 1 479 ? 22.216  -4.642  70.661  1.00 64.51  ? 488  PHE C CA  1 
ATOM   10018 C C   . PHE C 1 479 ? 22.015  -3.622  71.783  1.00 64.58  ? 488  PHE C C   1 
ATOM   10019 O O   . PHE C 1 479 ? 22.714  -3.658  72.784  1.00 65.14  ? 488  PHE C O   1 
ATOM   10020 C CB  . PHE C 1 479 ? 22.619  -3.949  69.376  1.00 62.85  ? 488  PHE C CB  1 
ATOM   10021 C CG  . PHE C 1 479 ? 23.950  -3.251  69.430  1.00 61.89  ? 488  PHE C CG  1 
ATOM   10022 C CD1 . PHE C 1 479 ? 25.109  -3.904  69.000  1.00 61.44  ? 488  PHE C CD1 1 
ATOM   10023 C CD2 . PHE C 1 479 ? 24.047  -1.920  69.859  1.00 60.88  ? 488  PHE C CD2 1 
ATOM   10024 C CE1 . PHE C 1 479 ? 26.363  -3.248  69.021  1.00 60.39  ? 488  PHE C CE1 1 
ATOM   10025 C CE2 . PHE C 1 479 ? 25.292  -1.260  69.885  1.00 60.05  ? 488  PHE C CE2 1 
ATOM   10026 C CZ  . PHE C 1 479 ? 26.454  -1.927  69.460  1.00 59.50  ? 488  PHE C CZ  1 
ATOM   10027 N N   . ASP C 1 480 ? 21.054  -2.722  71.621  1.00 64.00  ? 489  ASP C N   1 
ATOM   10028 C CA  . ASP C 1 480 ? 20.736  -1.715  72.644  1.00 64.68  ? 489  ASP C CA  1 
ATOM   10029 C C   . ASP C 1 480 ? 20.532  -2.296  74.027  1.00 66.39  ? 489  ASP C C   1 
ATOM   10030 O O   . ASP C 1 480 ? 20.665  -1.585  75.036  1.00 66.98  ? 489  ASP C O   1 
ATOM   10031 C CB  . ASP C 1 480 ? 19.451  -0.985  72.278  1.00 64.83  ? 489  ASP C CB  1 
ATOM   10032 C CG  . ASP C 1 480 ? 19.641  -0.016  71.149  1.00 64.40  ? 489  ASP C CG  1 
ATOM   10033 O OD1 . ASP C 1 480 ? 20.745  -0.026  70.552  1.00 65.36  ? 489  ASP C OD1 1 
ATOM   10034 O OD2 . ASP C 1 480 ? 18.697  0.757   70.847  1.00 65.18  ? 489  ASP C OD2 1 
ATOM   10035 N N   . ALA C 1 481 ? 20.148  -3.577  74.044  1.00 67.13  ? 490  ALA C N   1 
ATOM   10036 C CA  . ALA C 1 481 ? 19.951  -4.371  75.252  1.00 68.51  ? 490  ALA C CA  1 
ATOM   10037 C C   . ALA C 1 481 ? 21.284  -4.592  75.950  1.00 68.36  ? 490  ALA C C   1 
ATOM   10038 O O   . ALA C 1 481 ? 21.442  -4.279  77.133  1.00 69.26  ? 490  ALA C O   1 
ATOM   10039 C CB  . ALA C 1 481 ? 19.332  -5.696  74.890  1.00 69.36  ? 490  ALA C CB  1 
ATOM   10040 N N   . SER C 1 482 ? 22.241  -5.121  75.193  1.00 66.93  ? 491  SER C N   1 
ATOM   10041 C CA  . SER C 1 482 ? 23.597  -5.318  75.675  1.00 66.61  ? 491  SER C CA  1 
ATOM   10042 C C   . SER C 1 482 ? 24.167  -4.060  76.290  1.00 66.00  ? 491  SER C C   1 
ATOM   10043 O O   . SER C 1 482 ? 24.773  -4.110  77.361  1.00 67.09  ? 491  SER C O   1 
ATOM   10044 C CB  . SER C 1 482 ? 24.502  -5.754  74.529  1.00 65.26  ? 491  SER C CB  1 
ATOM   10045 O OG  . SER C 1 482 ? 24.392  -7.143  74.296  1.00 66.68  ? 491  SER C OG  1 
ATOM   10046 N N   . ILE C 1 483 ? 23.971  -2.937  75.613  1.00 64.47  ? 492  ILE C N   1 
ATOM   10047 C CA  . ILE C 1 483 ? 24.545  -1.699  76.073  1.00 64.13  ? 492  ILE C CA  1 
ATOM   10048 C C   . ILE C 1 483 ? 23.851  -1.115  77.272  1.00 65.63  ? 492  ILE C C   1 
ATOM   10049 O O   . ILE C 1 483 ? 24.520  -0.800  78.258  1.00 66.55  ? 492  ILE C O   1 
ATOM   10050 C CB  . ILE C 1 483 ? 24.560  -0.671  75.012  1.00 62.67  ? 492  ILE C CB  1 
ATOM   10051 C CG1 . ILE C 1 483 ? 25.374  -1.202  73.850  1.00 61.94  ? 492  ILE C CG1 1 
ATOM   10052 C CG2 . ILE C 1 483 ? 25.160  0.607   75.568  1.00 62.57  ? 492  ILE C CG2 1 
ATOM   10053 C CD1 . ILE C 1 483 ? 26.449  -0.256  73.376  1.00 62.35  ? 492  ILE C CD1 1 
ATOM   10054 N N   . SER C 1 484 ? 22.526  -0.953  77.202  1.00 66.18  ? 493  SER C N   1 
ATOM   10055 C CA  . SER C 1 484 ? 21.773  -0.528  78.382  0.50 67.64  ? 493  SER C CA  1 
ATOM   10056 C C   . SER C 1 484 ? 22.186  -1.416  79.554  1.00 69.14  ? 493  SER C C   1 
ATOM   10057 O O   . SER C 1 484 ? 21.930  -1.095  80.709  1.00 71.02  ? 493  SER C O   1 
ATOM   10058 C CB  . SER C 1 484 ? 20.262  -0.591  78.154  0.50 68.18  ? 493  SER C CB  1 
ATOM   10059 O OG  . SER C 1 484 ? 19.572  -0.110  79.294  0.50 69.38  ? 493  SER C OG  1 
ATOM   10060 N N   . GLN C 1 485 ? 22.878  -2.508  79.227  1.00 68.54  ? 494  GLN C N   1 
ATOM   10061 C CA  . GLN C 1 485 ? 23.328  -3.495  80.191  1.00 69.61  ? 494  GLN C CA  1 
ATOM   10062 C C   . GLN C 1 485 ? 24.806  -3.384  80.545  1.00 68.55  ? 494  GLN C C   1 
ATOM   10063 O O   . GLN C 1 485 ? 25.213  -3.814  81.614  1.00 69.89  ? 494  GLN C O   1 
ATOM   10064 C CB  . GLN C 1 485 ? 22.999  -4.882  79.667  1.00 70.20  ? 494  GLN C CB  1 
ATOM   10065 C CG  . GLN C 1 485 ? 22.651  -5.874  80.737  1.00 74.41  ? 494  GLN C CG  1 
ATOM   10066 C CD  . GLN C 1 485 ? 23.774  -6.869  80.936  1.00 77.78  ? 494  GLN C CD  1 
ATOM   10067 O OE1 . GLN C 1 485 ? 24.466  -7.242  79.967  1.00 76.57  ? 494  GLN C OE1 1 
ATOM   10068 N NE2 . GLN C 1 485 ? 23.975  -7.312  82.199  1.00 80.93  ? 494  GLN C NE2 1 
ATOM   10069 N N   . VAL C 1 486 ? 25.617  -2.809  79.668  1.00 66.50  ? 495  VAL C N   1 
ATOM   10070 C CA  . VAL C 1 486 ? 26.980  -2.449  80.042  1.00 65.63  ? 495  VAL C CA  1 
ATOM   10071 C C   . VAL C 1 486 ? 26.905  -1.366  81.109  1.00 66.58  ? 495  VAL C C   1 
ATOM   10072 O O   . VAL C 1 486 ? 27.689  -1.334  82.043  1.00 67.29  ? 495  VAL C O   1 
ATOM   10073 C CB  . VAL C 1 486 ? 27.801  -1.988  78.833  1.00 63.71  ? 495  VAL C CB  1 
ATOM   10074 C CG1 . VAL C 1 486 ? 28.843  -0.987  79.239  1.00 63.18  ? 495  VAL C CG1 1 
ATOM   10075 C CG2 . VAL C 1 486 ? 28.453  -3.158  78.167  1.00 62.68  ? 495  VAL C CG2 1 
ATOM   10076 N N   . ASN C 1 487 ? 25.917  -0.503  80.989  1.00 66.78  ? 496  ASN C N   1 
ATOM   10077 C CA  . ASN C 1 487 ? 25.730  0.529   81.971  1.00 68.34  ? 496  ASN C CA  1 
ATOM   10078 C C   . ASN C 1 487 ? 25.273  -0.004  83.325  1.00 70.53  ? 496  ASN C C   1 
ATOM   10079 O O   . ASN C 1 487 ? 25.569  0.600   84.360  1.00 71.43  ? 496  ASN C O   1 
ATOM   10080 C CB  . ASN C 1 487 ? 24.796  1.567   81.404  1.00 68.05  ? 496  ASN C CB  1 
ATOM   10081 C CG  . ASN C 1 487 ? 25.303  2.103   80.083  1.00 67.23  ? 496  ASN C CG  1 
ATOM   10082 O OD1 . ASN C 1 487 ? 26.466  2.496   79.954  1.00 66.93  ? 496  ASN C OD1 1 
ATOM   10083 N ND2 . ASN C 1 487 ? 24.445  2.095   79.081  1.00 68.21  ? 496  ASN C ND2 1 
ATOM   10084 N N   . GLU C 1 488 ? 24.574  -1.148  83.310  1.00 71.44  ? 497  GLU C N   1 
ATOM   10085 C CA  . GLU C 1 488 ? 24.335  -1.933  84.523  0.50 73.23  ? 497  GLU C CA  1 
ATOM   10086 C C   . GLU C 1 488 ? 25.639  -1.920  85.263  1.00 73.64  ? 497  GLU C C   1 
ATOM   10087 O O   . GLU C 1 488 ? 25.702  -1.453  86.390  1.00 75.23  ? 497  GLU C O   1 
ATOM   10088 C CB  . GLU C 1 488 ? 23.978  -3.399  84.230  0.50 73.53  ? 497  GLU C CB  1 
ATOM   10089 C CG  . GLU C 1 488 ? 22.544  -3.655  83.861  0.50 73.68  ? 497  GLU C CG  1 
ATOM   10090 C CD  . GLU C 1 488 ? 21.625  -2.758  84.618  0.50 74.49  ? 497  GLU C CD  1 
ATOM   10091 O OE1 . GLU C 1 488 ? 22.106  -2.124  85.584  0.50 74.41  ? 497  GLU C OE1 1 
ATOM   10092 O OE2 . GLU C 1 488 ? 20.437  -2.676  84.238  0.50 74.96  ? 497  GLU C OE2 1 
ATOM   10093 N N   . LYS C 1 489 ? 26.686  -2.399  84.597  1.00 72.58  ? 498  LYS C N   1 
ATOM   10094 C CA  . LYS C 1 489 ? 27.967  -2.650  85.242  1.00 73.36  ? 498  LYS C CA  1 
ATOM   10095 C C   . LYS C 1 489 ? 28.693  -1.414  85.705  1.00 73.44  ? 498  LYS C C   1 
ATOM   10096 O O   . LYS C 1 489 ? 29.233  -1.387  86.793  1.00 74.79  ? 498  LYS C O   1 
ATOM   10097 C CB  . LYS C 1 489 ? 28.874  -3.424  84.317  1.00 72.33  ? 498  LYS C CB  1 
ATOM   10098 C CG  . LYS C 1 489 ? 28.192  -4.580  83.669  1.00 73.37  ? 498  LYS C CG  1 
ATOM   10099 C CD  . LYS C 1 489 ? 28.215  -5.771  84.565  1.00 76.88  ? 498  LYS C CD  1 
ATOM   10100 C CE  . LYS C 1 489 ? 27.470  -6.901  83.916  1.00 78.67  ? 498  LYS C CE  1 
ATOM   10101 N NZ  . LYS C 1 489 ? 27.403  -7.986  84.923  1.00 82.79  ? 498  LYS C NZ  1 
ATOM   10102 N N   . ILE C 1 490 ? 28.731  -0.387  84.882  1.00 72.60  ? 499  ILE C N   1 
ATOM   10103 C CA  . ILE C 1 490 ? 29.359  0.836   85.323  1.00 73.33  ? 499  ILE C CA  1 
ATOM   10104 C C   . ILE C 1 490 ? 28.556  1.378   86.512  1.00 76.09  ? 499  ILE C C   1 
ATOM   10105 O O   . ILE C 1 490 ? 29.101  1.535   87.615  1.00 77.10  ? 499  ILE C O   1 
ATOM   10106 C CB  . ILE C 1 490 ? 29.447  1.868   84.189  1.00 71.75  ? 499  ILE C CB  1 
ATOM   10107 C CG1 . ILE C 1 490 ? 30.016  1.233   82.918  1.00 69.28  ? 499  ILE C CG1 1 
ATOM   10108 C CG2 . ILE C 1 490 ? 30.311  3.038   84.615  1.00 71.90  ? 499  ILE C CG2 1 
ATOM   10109 C CD1 . ILE C 1 490 ? 29.709  1.987   81.649  1.00 66.68  ? 499  ILE C CD1 1 
ATOM   10110 N N   . ASN C 1 491 ? 27.257  1.629   86.287  1.00 77.61  ? 500  ASN C N   1 
ATOM   10111 C CA  . ASN C 1 491 ? 26.354  2.066   87.351  1.00 81.05  ? 500  ASN C CA  1 
ATOM   10112 C C   . ASN C 1 491 ? 26.620  1.285   88.637  1.00 81.63  ? 500  ASN C C   1 
ATOM   10113 O O   . ASN C 1 491 ? 26.623  1.855   89.720  1.00 83.07  ? 500  ASN C O   1 
ATOM   10114 C CB  . ASN C 1 491 ? 24.876  1.977   86.918  1.00 82.60  ? 500  ASN C CB  1 
ATOM   10115 C CG  . ASN C 1 491 ? 24.309  3.332   86.508  1.00 90.43  ? 500  ASN C CG  1 
ATOM   10116 O OD1 . ASN C 1 491 ? 25.059  4.307   86.471  1.00 90.71  ? 500  ASN C OD1 1 
ATOM   10117 N ND2 . ASN C 1 491 ? 22.970  3.402   86.203  1.00 105.40 ? 500  ASN C ND2 1 
ATOM   10118 N N   . GLN C 1 492 ? 26.883  -0.009  88.483  1.00 80.58  ? 501  GLN C N   1 
ATOM   10119 C CA  . GLN C 1 492 ? 27.126  -0.940  89.573  1.00 81.69  ? 501  GLN C CA  1 
ATOM   10120 C C   . GLN C 1 492 ? 28.474  -0.663  90.239  1.00 81.12  ? 501  GLN C C   1 
ATOM   10121 O O   . GLN C 1 492 ? 28.606  -0.699  91.481  1.00 82.51  ? 501  GLN C O   1 
ATOM   10122 C CB  . GLN C 1 492 ? 27.120  -2.351  88.983  1.00 81.55  ? 501  GLN C CB  1 
ATOM   10123 C CG  . GLN C 1 492 ? 26.845  -3.522  89.927  1.00 85.45  ? 501  GLN C CG  1 
ATOM   10124 C CD  . GLN C 1 492 ? 26.271  -4.725  89.162  1.00 87.95  ? 501  GLN C CD  1 
ATOM   10125 O OE1 . GLN C 1 492 ? 26.825  -5.156  88.142  1.00 86.97  ? 501  GLN C OE1 1 
ATOM   10126 N NE2 . GLN C 1 492 ? 25.146  -5.255  89.644  1.00 90.99  ? 501  GLN C NE2 1 
ATOM   10127 N N   . SER C 1 493 ? 29.456  -0.387  89.381  1.00 78.72  ? 502  SER C N   1 
ATOM   10128 C CA  . SER C 1 493 ? 30.860  -0.246  89.748  1.00 77.88  ? 502  SER C CA  1 
ATOM   10129 C C   . SER C 1 493 ? 31.064  1.016   90.540  1.00 78.46  ? 502  SER C C   1 
ATOM   10130 O O   . SER C 1 493 ? 31.680  0.988   91.600  1.00 79.67  ? 502  SER C O   1 
ATOM   10131 C CB  . SER C 1 493 ? 31.718  -0.198  88.490  1.00 75.91  ? 502  SER C CB  1 
ATOM   10132 O OG  . SER C 1 493 ? 33.081  -0.228  88.809  1.00 75.38  ? 502  SER C OG  1 
ATOM   10133 N N   . LEU C 1 494 ? 30.533  2.119   90.025  1.00 77.43  ? 503  LEU C N   1 
ATOM   10134 C CA  . LEU C 1 494 ? 30.573  3.388   90.726  1.00 78.24  ? 503  LEU C CA  1 
ATOM   10135 C C   . LEU C 1 494 ? 30.029  3.288   92.133  1.00 80.36  ? 503  LEU C C   1 
ATOM   10136 O O   . LEU C 1 494 ? 30.631  3.820   93.068  1.00 81.67  ? 503  LEU C O   1 
ATOM   10137 C CB  . LEU C 1 494 ? 29.744  4.402   89.984  1.00 77.64  ? 503  LEU C CB  1 
ATOM   10138 C CG  . LEU C 1 494 ? 30.290  4.768   88.619  1.00 76.00  ? 503  LEU C CG  1 
ATOM   10139 C CD1 . LEU C 1 494 ? 29.343  5.802   87.980  1.00 76.18  ? 503  LEU C CD1 1 
ATOM   10140 C CD2 . LEU C 1 494 ? 31.712  5.312   88.757  1.00 76.09  ? 503  LEU C CD2 1 
ATOM   10141 N N   . ALA C 1 495 ? 28.887  2.604   92.264  1.00 80.85  ? 504  ALA C N   1 
ATOM   10142 C CA  . ALA C 1 495 ? 28.218  2.363   93.551  1.00 82.63  ? 504  ALA C CA  1 
ATOM   10143 C C   . ALA C 1 495 ? 29.089  1.562   94.520  1.00 83.22  ? 504  ALA C C   1 
ATOM   10144 O O   . ALA C 1 495 ? 29.054  1.800   95.729  1.00 85.12  ? 504  ALA C O   1 
ATOM   10145 C CB  . ALA C 1 495 ? 26.848  1.681   93.350  1.00 82.95  ? 504  ALA C CB  1 
ATOM   10146 N N   . PHE C 1 496 ? 29.868  0.623   93.995  1.00 81.59  ? 505  PHE C N   1 
ATOM   10147 C CA  . PHE C 1 496 ? 30.827  -0.089  94.820  1.00 82.15  ? 505  PHE C CA  1 
ATOM   10148 C C   . PHE C 1 496 ? 31.915  0.831   95.374  1.00 82.30  ? 505  PHE C C   1 
ATOM   10149 O O   . PHE C 1 496 ? 32.281  0.718   96.540  1.00 83.83  ? 505  PHE C O   1 
ATOM   10150 C CB  . PHE C 1 496 ? 31.452  -1.231  94.044  1.00 81.05  ? 505  PHE C CB  1 
ATOM   10151 C CG  . PHE C 1 496 ? 30.699  -2.523  94.142  1.00 82.58  ? 505  PHE C CG  1 
ATOM   10152 C CD1 . PHE C 1 496 ? 30.057  -3.050  93.041  1.00 83.23  ? 505  PHE C CD1 1 
ATOM   10153 C CD2 . PHE C 1 496 ? 30.649  -3.231  95.330  1.00 84.89  ? 505  PHE C CD2 1 
ATOM   10154 C CE1 . PHE C 1 496 ? 29.362  -4.266  93.129  1.00 84.37  ? 505  PHE C CE1 1 
ATOM   10155 C CE2 . PHE C 1 496 ? 29.965  -4.446  95.420  1.00 85.79  ? 505  PHE C CE2 1 
ATOM   10156 C CZ  . PHE C 1 496 ? 29.328  -4.964  94.320  1.00 85.07  ? 505  PHE C CZ  1 
ATOM   10157 N N   . ILE C 1 497 ? 32.412  1.746   94.547  1.00 80.95  ? 506  ILE C N   1 
ATOM   10158 C CA  . ILE C 1 497 ? 33.408  2.732   94.980  1.00 81.56  ? 506  ILE C CA  1 
ATOM   10159 C C   . ILE C 1 497 ? 32.819  3.717   95.976  1.00 83.85  ? 506  ILE C C   1 
ATOM   10160 O O   . ILE C 1 497 ? 33.384  3.921   97.044  1.00 85.40  ? 506  ILE C O   1 
ATOM   10161 C CB  . ILE C 1 497 ? 34.021  3.506   93.788  1.00 79.82  ? 506  ILE C CB  1 
ATOM   10162 C CG1 . ILE C 1 497 ? 34.812  2.562   92.881  1.00 78.21  ? 506  ILE C CG1 1 
ATOM   10163 C CG2 . ILE C 1 497 ? 34.917  4.655   94.256  1.00 80.02  ? 506  ILE C CG2 1 
ATOM   10164 C CD1 . ILE C 1 497 ? 36.025  1.926   93.534  1.00 78.90  ? 506  ILE C CD1 1 
ATOM   10165 N N   . ARG C 1 498 ? 31.694  4.329   95.613  1.00 84.36  ? 507  ARG C N   1 
ATOM   10166 C CA  . ARG C 1 498 ? 30.885  5.124   96.538  1.00 87.06  ? 507  ARG C CA  1 
ATOM   10167 C C   . ARG C 1 498 ? 30.961  4.572   97.987  1.00 88.88  ? 507  ARG C C   1 
ATOM   10168 O O   . ARG C 1 498 ? 31.296  5.295   98.935  1.00 90.09  ? 507  ARG C O   1 
ATOM   10169 C CB  . ARG C 1 498 ? 29.419  5.103   96.078  1.00 87.42  ? 507  ARG C CB  1 
ATOM   10170 C CG  . ARG C 1 498 ? 28.987  5.972   94.836  1.00 88.97  ? 507  ARG C CG  1 
ATOM   10171 C CD  . ARG C 1 498 ? 27.527  6.425   95.044  1.00 94.31  ? 507  ARG C CD  1 
ATOM   10172 N NE  . ARG C 1 498 ? 27.376  6.626   96.505  1.00 101.56 ? 507  ARG C NE  1 
ATOM   10173 C CZ  . ARG C 1 498 ? 26.238  6.792   97.194  1.00 105.02 ? 507  ARG C CZ  1 
ATOM   10174 N NH1 . ARG C 1 498 ? 25.055  6.811   96.565  1.00 105.23 ? 507  ARG C NH1 1 
ATOM   10175 N NH2 . ARG C 1 498 ? 26.292  6.950   98.533  1.00 106.66 ? 507  ARG C NH2 1 
ATOM   10176 N N   . LYS C 1 499 ? 30.648  3.280   98.121  1.00 88.91  ? 508  LYS C N   1 
ATOM   10177 C CA  . LYS C 1 499 ? 30.641  2.550   99.387  1.00 90.82  ? 508  LYS C CA  1 
ATOM   10178 C C   . LYS C 1 499 ? 32.038  2.437   99.989  1.00 90.96  ? 508  LYS C C   1 
ATOM   10179 O O   . LYS C 1 499 ? 32.217  2.539   101.208 1.00 93.00  ? 508  LYS C O   1 
ATOM   10180 C CB  . LYS C 1 499 ? 30.032  1.147   99.198  1.00 90.71  ? 508  LYS C CB  1 
ATOM   10181 C CG  . LYS C 1 499 ? 29.873  0.306   100.502 1.00 94.48  ? 508  LYS C CG  1 
ATOM   10182 C CD  . LYS C 1 499 ? 28.437  0.348   101.137 1.00 98.76  ? 508  LYS C CD  1 
ATOM   10183 C CE  . LYS C 1 499 ? 28.185  1.493   102.165 1.00 101.16 ? 508  LYS C CE  1 
ATOM   10184 N NZ  . LYS C 1 499 ? 28.984  1.453   103.439 1.00 101.44 ? 508  LYS C NZ  1 
ATOM   10185 N N   . SER C 1 500 ? 33.025  2.210   99.137  1.00 89.04  ? 509  SER C N   1 
ATOM   10186 C CA  . SER C 1 500 ? 34.405  2.152   99.575  1.00 89.19  ? 509  SER C CA  1 
ATOM   10187 C C   . SER C 1 500 ? 34.856  3.473   100.174 1.00 90.61  ? 509  SER C C   1 
ATOM   10188 O O   . SER C 1 500 ? 35.422  3.501   101.254 1.00 92.05  ? 509  SER C O   1 
ATOM   10189 C CB  . SER C 1 500 ? 35.300  1.801   98.403  1.00 87.06  ? 509  SER C CB  1 
ATOM   10190 O OG  . SER C 1 500 ? 36.639  1.725   98.824  1.00 86.91  ? 509  SER C OG  1 
ATOM   10191 N N   . ASP C 1 501 ? 34.588  4.564   99.472  1.00 90.52  ? 510  ASP C N   1 
ATOM   10192 C CA  . ASP C 1 501 ? 34.979  5.889   99.923  1.00 92.29  ? 510  ASP C CA  1 
ATOM   10193 C C   . ASP C 1 501 ? 34.377  6.274   101.259 1.00 94.94  ? 510  ASP C C   1 
ATOM   10194 O O   . ASP C 1 501 ? 35.092  6.761   102.133 1.00 96.58  ? 510  ASP C O   1 
ATOM   10195 C CB  . ASP C 1 501 ? 34.613  6.935   98.880  1.00 91.62  ? 510  ASP C CB  1 
ATOM   10196 C CG  . ASP C 1 501 ? 35.646  7.040   97.774  1.00 90.79  ? 510  ASP C CG  1 
ATOM   10197 O OD1 . ASP C 1 501 ? 36.830  7.216   98.113  1.00 92.51  ? 510  ASP C OD1 1 
ATOM   10198 O OD2 . ASP C 1 501 ? 35.285  6.959   96.571  1.00 89.71  ? 510  ASP C OD2 1 
ATOM   10199 N N   . GLU C 1 502 ? 33.071  6.060   101.424 1.00 95.80  ? 511  GLU C N   1 
ATOM   10200 C CA  . GLU C 1 502 ? 32.417  6.321   102.713 1.00 98.78  ? 511  GLU C CA  1 
ATOM   10201 C C   . GLU C 1 502 ? 33.245  5.723   103.838 1.00 99.80  ? 511  GLU C C   1 
ATOM   10202 O O   . GLU C 1 502 ? 33.594  6.402   104.805 1.00 101.84 ? 511  GLU C O   1 
ATOM   10203 C CB  . GLU C 1 502 ? 30.986  5.758   102.762 1.00 99.49  ? 511  GLU C CB  1 
ATOM   10204 C CG  . GLU C 1 502 ? 29.924  6.653   102.070 1.00 101.89 ? 511  GLU C CG  1 
ATOM   10205 C CD  . GLU C 1 502 ? 28.533  5.990   101.899 1.00 104.77 ? 511  GLU C CD  1 
ATOM   10206 O OE1 . GLU C 1 502 ? 28.066  5.320   102.876 1.00 107.58 ? 511  GLU C OE1 1 
ATOM   10207 O OE2 . GLU C 1 502 ? 27.919  6.167   100.797 1.00 102.63 ? 511  GLU C OE2 1 
ATOM   10208 N N   . LEU C 1 503 ? 33.590  4.455   103.688 1.00 98.50  ? 512  LEU C N   1 
ATOM   10209 C CA  . LEU C 1 503 ? 34.334  3.773   104.710 1.00 99.48  ? 512  LEU C CA  1 
ATOM   10210 C C   . LEU C 1 503 ? 35.636  4.477   105.031 1.00 99.90  ? 512  LEU C C   1 
ATOM   10211 O O   . LEU C 1 503 ? 36.122  4.390   106.154 1.00 101.94 ? 512  LEU C O   1 
ATOM   10212 C CB  . LEU C 1 503 ? 34.575  2.320   104.316 1.00 98.19  ? 512  LEU C CB  1 
ATOM   10213 C CG  . LEU C 1 503 ? 33.296  1.481   104.319 1.00 98.76  ? 512  LEU C CG  1 
ATOM   10214 C CD1 . LEU C 1 503 ? 33.558  0.093   103.759 1.00 97.60  ? 512  LEU C CD1 1 
ATOM   10215 C CD2 . LEU C 1 503 ? 32.680  1.406   105.738 1.00 101.58 ? 512  LEU C CD2 1 
ATOM   10216 N N   . LEU C 1 504 ? 36.181  5.208   104.069 1.00 98.45  ? 513  LEU C N   1 
ATOM   10217 C CA  . LEU C 1 504 ? 37.490  5.825   104.258 1.00 98.99  ? 513  LEU C CA  1 
ATOM   10218 C C   . LEU C 1 504 ? 37.447  7.222   104.829 1.00 101.20 ? 513  LEU C C   1 
ATOM   10219 O O   . LEU C 1 504 ? 38.347  7.622   105.561 1.00 102.36 ? 513  LEU C O   1 
ATOM   10220 C CB  . LEU C 1 504 ? 38.255  5.833   102.955 1.00 96.66  ? 513  LEU C CB  1 
ATOM   10221 C CG  . LEU C 1 504 ? 38.505  4.433   102.413 1.00 94.51  ? 513  LEU C CG  1 
ATOM   10222 C CD1 . LEU C 1 504 ? 38.544  4.472   100.901 1.00 92.89  ? 513  LEU C CD1 1 
ATOM   10223 C CD2 . LEU C 1 504 ? 39.785  3.864   102.984 1.00 93.88  ? 513  LEU C CD2 1 
ATOM   10224 N N   . HIS C 1 505 ? 36.405  7.967   104.492 1.00 102.02 ? 514  HIS C N   1 
ATOM   10225 C CA  . HIS C 1 505 ? 36.161  9.242   105.148 1.00 105.18 ? 514  HIS C CA  1 
ATOM   10226 C C   . HIS C 1 505 ? 35.618  9.014   106.575 1.00 108.21 ? 514  HIS C C   1 
ATOM   10227 O O   . HIS C 1 505 ? 35.123  9.931   107.250 1.00 110.45 ? 514  HIS C O   1 
ATOM   10228 C CB  . HIS C 1 505 ? 35.234  10.104  104.305 1.00 104.56 ? 514  HIS C CB  1 
ATOM   10229 C CG  . HIS C 1 505 ? 35.739  10.340  102.913 1.00 103.66 ? 514  HIS C CG  1 
ATOM   10230 N ND1 . HIS C 1 505 ? 37.044  10.701  102.648 1.00 103.95 ? 514  HIS C ND1 1 
ATOM   10231 C CD2 . HIS C 1 505 ? 35.114  10.278  101.708 1.00 102.46 ? 514  HIS C CD2 1 
ATOM   10232 C CE1 . HIS C 1 505 ? 37.200  10.851  101.341 1.00 101.95 ? 514  HIS C CE1 1 
ATOM   10233 N NE2 . HIS C 1 505 ? 36.045  10.601  100.748 1.00 100.85 ? 514  HIS C NE2 1 
ATOM   10234 N N   . ASN C 1 506 ? 35.730  7.769   107.024 1.00 108.75 ? 515  ASN C N   1 
ATOM   10235 C CA  . ASN C 1 506 ? 35.459  7.400   108.396 1.00 111.58 ? 515  ASN C CA  1 
ATOM   10236 C C   . ASN C 1 506 ? 36.749  6.934   109.077 1.00 112.37 ? 515  ASN C C   1 
ATOM   10237 O O   . ASN C 1 506 ? 36.700  6.274   110.123 1.00 113.89 ? 515  ASN C O   1 
ATOM   10238 C CB  . ASN C 1 506 ? 34.419  6.286   108.422 1.00 111.38 ? 515  ASN C CB  1 
ATOM   10239 C CG  . ASN C 1 506 ? 33.189  6.666   109.197 1.00 114.10 ? 515  ASN C CG  1 
ATOM   10240 O OD1 . ASN C 1 506 ? 32.167  6.998   108.593 1.00 114.11 ? 515  ASN C OD1 1 
ATOM   10241 N ND2 . ASN C 1 506 ? 33.271  6.639   110.539 1.00 115.98 ? 515  ASN C ND2 1 
ATOM   10242 N N   . VAL C 1 507 ? 37.892  7.278   108.469 1.00 111.63 ? 516  VAL C N   1 
ATOM   10243 C CA  . VAL C 1 507 ? 39.234  6.863   108.939 1.00 112.08 ? 516  VAL C CA  1 
ATOM   10244 C C   . VAL C 1 507 ? 40.174  8.074   109.126 1.00 113.38 ? 516  VAL C C   1 
ATOM   10245 O O   . VAL C 1 507 ? 40.379  8.858   108.185 1.00 112.47 ? 516  VAL C O   1 
ATOM   10246 C CB  . VAL C 1 507 ? 39.877  5.778   108.000 1.00 109.68 ? 516  VAL C CB  1 
ATOM   10247 C CG1 . VAL C 1 507 ? 41.372  5.586   108.293 1.00 109.64 ? 516  VAL C CG1 1 
ATOM   10248 C CG2 . VAL C 1 507 ? 39.137  4.447   108.118 1.00 108.62 ? 516  VAL C CG2 1 
ATOM   10249 N N   . ASN C 1 508 ? 40.745  8.210   110.332 1.00 115.32 ? 517  ASN C N   1 
ATOM   10250 C CA  . ASN C 1 508 ? 41.444  9.440   110.715 1.00 116.87 ? 517  ASN C CA  1 
ATOM   10251 C C   . ASN C 1 508 ? 42.192  9.323   112.047 1.00 118.67 ? 517  ASN C C   1 
ATOM   10252 O O   . ASN C 1 508 ? 42.683  8.263   112.412 1.00 118.07 ? 517  ASN C O   1 
ATOM   10253 C CB  . ASN C 1 508 ? 40.425  10.612  110.738 1.00 118.21 ? 517  ASN C CB  1 
ATOM   10254 C CG  . ASN C 1 508 ? 41.081  11.987  110.656 1.00 120.06 ? 517  ASN C CG  1 
ATOM   10255 O OD1 . ASN C 1 508 ? 42.252  12.155  111.030 1.00 122.26 ? 517  ASN C OD1 1 
ATOM   10256 N ND2 . ASN C 1 508 ? 40.319  12.985  110.184 1.00 119.96 ? 517  ASN C ND2 1 
HETATM 10257 C C1  . NAG D 2 .   ? 48.507  10.728  77.017  1.00 63.84  ? 1545 NAG A C1  1 
HETATM 10258 C C2  . NAG D 2 .   ? 48.510  11.358  75.606  1.00 73.49  ? 1545 NAG A C2  1 
HETATM 10259 C C3  . NAG D 2 .   ? 49.711  10.867  74.762  1.00 76.93  ? 1545 NAG A C3  1 
HETATM 10260 C C4  . NAG D 2 .   ? 51.059  11.075  75.519  1.00 79.45  ? 1545 NAG A C4  1 
HETATM 10261 C C5  . NAG D 2 .   ? 50.950  10.432  76.959  1.00 75.16  ? 1545 NAG A C5  1 
HETATM 10262 C C6  . NAG D 2 .   ? 52.238  10.255  77.861  1.00 74.26  ? 1545 NAG A C6  1 
HETATM 10263 C C7  . NAG D 2 .   ? 46.116  11.945  75.209  1.00 75.96  ? 1545 NAG A C7  1 
HETATM 10264 C C8  . NAG D 2 .   ? 44.918  11.704  74.333  1.00 76.36  ? 1545 NAG A C8  1 
HETATM 10265 N N2  . NAG D 2 .   ? 47.229  11.253  74.890  1.00 74.56  ? 1545 NAG A N2  1 
HETATM 10266 O O3  . NAG D 2 .   ? 49.704  11.498  73.483  1.00 79.34  ? 1545 NAG A O3  1 
HETATM 10267 O O4  . NAG D 2 .   ? 52.213  10.762  74.686  1.00 85.38  ? 1545 NAG A O4  1 
HETATM 10268 O O5  . NAG D 2 .   ? 49.794  10.974  77.636  1.00 69.03  ? 1545 NAG A O5  1 
HETATM 10269 O O6  . NAG D 2 .   ? 52.548  11.232  78.861  1.00 71.24  ? 1545 NAG A O6  1 
HETATM 10270 O O7  . NAG D 2 .   ? 46.018  12.737  76.156  1.00 75.75  ? 1545 NAG A O7  1 
HETATM 10271 C C1  . NAG E 2 .   ? 53.170  11.885  74.639  1.00 90.76  ? 1546 NAG A C1  1 
HETATM 10272 C C2  . NAG E 2 .   ? 54.020  11.990  73.340  1.00 93.22  ? 1546 NAG A C2  1 
HETATM 10273 C C3  . NAG E 2 .   ? 54.794  13.327  73.332  1.00 94.25  ? 1546 NAG A C3  1 
HETATM 10274 C C4  . NAG E 2 .   ? 53.815  14.505  73.281  1.00 95.16  ? 1546 NAG A C4  1 
HETATM 10275 C C5  . NAG E 2 .   ? 52.628  14.373  74.277  1.00 94.52  ? 1546 NAG A C5  1 
HETATM 10276 C C6  . NAG E 2 .   ? 51.267  14.692  73.619  1.00 93.93  ? 1546 NAG A C6  1 
HETATM 10277 C C7  . NAG E 2 .   ? 54.716  9.602   72.722  1.00 94.44  ? 1546 NAG A C7  1 
HETATM 10278 C C8  . NAG E 2 .   ? 55.920  8.748   72.383  1.00 93.50  ? 1546 NAG A C8  1 
HETATM 10279 N N2  . NAG E 2 .   ? 54.961  10.896  73.014  1.00 94.54  ? 1546 NAG A N2  1 
HETATM 10280 O O3  . NAG E 2 .   ? 55.702  13.460  72.247  1.00 93.80  ? 1546 NAG A O3  1 
HETATM 10281 O O4  . NAG E 2 .   ? 54.534  15.720  73.473  1.00 96.33  ? 1546 NAG A O4  1 
HETATM 10282 O O5  . NAG E 2 .   ? 52.548  13.137  75.020  1.00 92.96  ? 1546 NAG A O5  1 
HETATM 10283 O O6  . NAG E 2 .   ? 50.261  14.897  74.604  1.00 93.18  ? 1546 NAG A O6  1 
HETATM 10284 O O7  . NAG E 2 .   ? 53.585  9.103   72.741  1.00 94.38  ? 1546 NAG A O7  1 
HETATM 10285 C C1  . NAG F 2 .   ? 11.485  33.887  -16.231 1.00 51.83  ? 1525 NAG A C1  1 
HETATM 10286 C C2  . NAG F 2 .   ? 11.046  33.628  -17.755 1.00 59.92  ? 1525 NAG A C2  1 
HETATM 10287 C C3  . NAG F 2 .   ? 10.919  34.946  -18.638 1.00 61.34  ? 1525 NAG A C3  1 
HETATM 10288 C C4  . NAG F 2 .   ? 10.918  36.324  -17.889 1.00 63.38  ? 1525 NAG A C4  1 
HETATM 10289 C C5  . NAG F 2 .   ? 11.707  36.242  -16.543 1.00 62.49  ? 1525 NAG A C5  1 
HETATM 10290 C C6  . NAG F 2 .   ? 11.981  37.516  -15.681 1.00 62.75  ? 1525 NAG A C6  1 
HETATM 10291 C C7  . NAG F 2 .   ? 12.028  31.969  -19.667 1.00 62.71  ? 1525 NAG A C7  1 
HETATM 10292 C C8  . NAG F 2 .   ? 13.014  30.817  -19.793 1.00 61.05  ? 1525 NAG A C8  1 
HETATM 10293 N N2  . NAG F 2 .   ? 11.856  32.509  -18.400 1.00 62.41  ? 1525 NAG A N2  1 
HETATM 10294 O O3  . NAG F 2 .   ? 9.830   34.949  -19.557 1.00 59.59  ? 1525 NAG A O3  1 
HETATM 10295 O O4  . NAG F 2 .   ? 11.390  37.382  -18.733 1.00 66.17  ? 1525 NAG A O4  1 
HETATM 10296 O O5  . NAG F 2 .   ? 11.063  35.193  -15.812 1.00 57.13  ? 1525 NAG A O5  1 
HETATM 10297 O O6  . NAG F 2 .   ? 11.424  38.720  -16.191 1.00 64.48  ? 1525 NAG A O6  1 
HETATM 10298 O O7  . NAG F 2 .   ? 11.463  32.337  -20.709 1.00 61.89  ? 1525 NAG A O7  1 
HETATM 10299 C C1  . NAG G 2 .   ? 31.745  -14.221 44.042  1.00 80.33  ? 1535 NAG A C1  1 
HETATM 10300 C C2  . NAG G 2 .   ? 32.870  -14.504 45.048  1.00 89.82  ? 1535 NAG A C2  1 
HETATM 10301 C C3  . NAG G 2 .   ? 32.410  -15.817 45.731  1.00 92.14  ? 1535 NAG A C3  1 
HETATM 10302 C C4  . NAG G 2 .   ? 31.550  -16.697 44.774  1.00 94.68  ? 1535 NAG A C4  1 
HETATM 10303 C C5  . NAG G 2 .   ? 32.095  -16.517 43.333  1.00 91.23  ? 1535 NAG A C5  1 
HETATM 10304 C C6  . NAG G 2 .   ? 31.589  -17.484 42.243  1.00 90.16  ? 1535 NAG A C6  1 
HETATM 10305 C C7  . NAG G 2 .   ? 35.456  -14.250 44.729  1.00 93.90  ? 1535 NAG A C7  1 
HETATM 10306 C C8  . NAG G 2 .   ? 36.551  -14.419 43.698  1.00 93.53  ? 1535 NAG A C8  1 
HETATM 10307 N N2  . NAG G 2 .   ? 34.180  -14.547 44.334  1.00 91.69  ? 1535 NAG A N2  1 
HETATM 10308 O O3  . NAG G 2 .   ? 31.662  -15.489 46.889  1.00 91.12  ? 1535 NAG A O3  1 
HETATM 10309 O O4  . NAG G 2 .   ? 31.514  -18.072 45.141  1.00 101.58 ? 1535 NAG A O4  1 
HETATM 10310 O O5  . NAG G 2 .   ? 31.933  -15.138 42.949  1.00 86.48  ? 1535 NAG A O5  1 
HETATM 10311 O O6  . NAG G 2 .   ? 30.181  -17.612 42.217  1.00 89.44  ? 1535 NAG A O6  1 
HETATM 10312 O O7  . NAG G 2 .   ? 35.806  -13.861 45.856  1.00 95.07  ? 1535 NAG A O7  1 
HETATM 10313 C C1  . NAG H 2 .   ? 30.195  -18.598 45.500  1.00 106.51 ? 1536 NAG A C1  1 
HETATM 10314 C C2  . NAG H 2 .   ? 29.945  -19.928 44.746  1.00 108.87 ? 1536 NAG A C2  1 
HETATM 10315 C C3  . NAG H 2 .   ? 30.574  -21.183 45.406  1.00 109.64 ? 1536 NAG A C3  1 
HETATM 10316 C C4  . NAG H 2 .   ? 31.237  -21.009 46.791  1.00 110.01 ? 1536 NAG A C4  1 
HETATM 10317 C C5  . NAG H 2 .   ? 30.972  -19.673 47.552  1.00 109.95 ? 1536 NAG A C5  1 
HETATM 10318 C C6  . NAG H 2 .   ? 32.324  -18.997 47.887  1.00 110.47 ? 1536 NAG A C6  1 
HETATM 10319 C C7  . NAG H 2 .   ? 28.086  -21.047 43.541  1.00 109.86 ? 1536 NAG A C7  1 
HETATM 10320 C C8  . NAG H 2 .   ? 26.589  -21.199 43.428  1.00 109.16 ? 1536 NAG A C8  1 
HETATM 10321 N N2  . NAG H 2 .   ? 28.522  -20.193 44.490  1.00 109.76 ? 1536 NAG A N2  1 
HETATM 10322 O O3  . NAG H 2 .   ? 31.482  -21.807 44.503  1.00 109.04 ? 1536 NAG A O3  1 
HETATM 10323 O O4  . NAG H 2 .   ? 30.879  -22.126 47.589  1.00 109.89 ? 1536 NAG A O4  1 
HETATM 10324 O O5  . NAG H 2 .   ? 30.031  -18.789 46.905  1.00 108.30 ? 1536 NAG A O5  1 
HETATM 10325 O O6  . NAG H 2 .   ? 32.195  -17.888 48.757  1.00 110.69 ? 1536 NAG A O6  1 
HETATM 10326 O O7  . NAG H 2 .   ? 28.841  -21.682 42.786  1.00 109.27 ? 1536 NAG A O7  1 
HETATM 10327 C C1  . NAG I 2 .   ? 8.903   3.028   52.760  1.00 78.16  ? 1535 NAG B C1  1 
HETATM 10328 C C2  . NAG I 2 .   ? 8.058   1.897   53.414  1.00 87.05  ? 1535 NAG B C2  1 
HETATM 10329 C C3  . NAG I 2 .   ? 6.927   2.386   54.357  1.00 90.17  ? 1535 NAG B C3  1 
HETATM 10330 C C4  . NAG I 2 .   ? 6.270   3.686   53.802  1.00 92.97  ? 1535 NAG B C4  1 
HETATM 10331 C C5  . NAG I 2 .   ? 6.697   3.948   52.336  1.00 89.25  ? 1535 NAG B C5  1 
HETATM 10332 C C6  . NAG I 2 .   ? 5.865   4.979   51.524  1.00 88.72  ? 1535 NAG B C6  1 
HETATM 10333 C C7  . NAG I 2 .   ? 7.984   0.037   51.773  1.00 87.77  ? 1535 NAG B C7  1 
HETATM 10334 C C8  . NAG I 2 .   ? 7.146   -0.545  50.669  1.00 87.37  ? 1535 NAG B C8  1 
HETATM 10335 N N2  . NAG I 2 .   ? 7.452   1.117   52.336  1.00 87.03  ? 1535 NAG B N2  1 
HETATM 10336 O O3  . NAG I 2 .   ? 7.391   2.553   55.700  1.00 89.53  ? 1535 NAG B O3  1 
HETATM 10337 O O4  . NAG I 2 .   ? 4.868   3.846   54.030  1.00 99.21  ? 1535 NAG B O4  1 
HETATM 10338 O O5  . NAG I 2 .   ? 8.098   4.198   52.482  1.00 84.20  ? 1535 NAG B O5  1 
HETATM 10339 O O6  . NAG I 2 .   ? 6.597   6.007   50.874  1.00 88.14  ? 1535 NAG B O6  1 
HETATM 10340 O O7  . NAG I 2 .   ? 9.067   -0.462  52.114  1.00 87.85  ? 1535 NAG B O7  1 
HETATM 10341 C C1  . NAG J 2 .   ? 4.730   4.778   55.144  1.00 104.86 ? 1536 NAG B C1  1 
HETATM 10342 C C2  . NAG J 2 .   ? 4.929   6.297   54.756  1.00 106.75 ? 1536 NAG B C2  1 
HETATM 10343 C C3  . NAG J 2 .   ? 3.840   7.273   55.255  1.00 107.37 ? 1536 NAG B C3  1 
HETATM 10344 C C4  . NAG J 2 .   ? 2.673   6.619   56.005  1.00 108.37 ? 1536 NAG B C4  1 
HETATM 10345 C C5  . NAG J 2 .   ? 3.128   5.381   56.795  1.00 108.72 ? 1536 NAG B C5  1 
HETATM 10346 C C6  . NAG J 2 .   ? 2.057   4.758   57.700  1.00 109.31 ? 1536 NAG B C6  1 
HETATM 10347 C C7  . NAG J 2 .   ? 7.127   7.533   54.303  1.00 106.58 ? 1536 NAG B C7  1 
HETATM 10348 C C8  . NAG J 2 .   ? 8.478   7.855   54.887  1.00 105.62 ? 1536 NAG B C8  1 
HETATM 10349 N N2  . NAG J 2 .   ? 6.300   6.785   55.082  1.00 107.08 ? 1536 NAG B N2  1 
HETATM 10350 O O3  . NAG J 2 .   ? 3.299   7.955   54.144  1.00 106.72 ? 1536 NAG B O3  1 
HETATM 10351 O O4  . NAG J 2 .   ? 2.062   7.582   56.835  1.00 108.94 ? 1536 NAG B O4  1 
HETATM 10352 O O5  . NAG J 2 .   ? 3.548   4.421   55.848  1.00 106.77 ? 1536 NAG B O5  1 
HETATM 10353 O O6  . NAG J 2 .   ? 2.596   3.612   58.333  1.00 110.21 ? 1536 NAG B O6  1 
HETATM 10354 O O7  . NAG J 2 .   ? 6.856   7.968   53.172  1.00 105.85 ? 1536 NAG B O7  1 
HETATM 10355 C C1  . NAG K 2 .   ? 40.090  -16.052 78.788  1.00 66.25  ? 1545 NAG B C1  1 
HETATM 10356 C C2  . NAG K 2 .   ? 40.383  -16.870 77.501  1.00 76.40  ? 1545 NAG B C2  1 
HETATM 10357 C C3  . NAG K 2 .   ? 39.472  -18.097 77.274  1.00 78.61  ? 1545 NAG B C3  1 
HETATM 10358 C C4  . NAG K 2 .   ? 39.103  -18.809 78.592  1.00 81.00  ? 1545 NAG B C4  1 
HETATM 10359 C C5  . NAG K 2 .   ? 38.526  -17.760 79.564  1.00 77.83  ? 1545 NAG B C5  1 
HETATM 10360 C C6  . NAG K 2 .   ? 37.866  -18.360 80.827  1.00 78.24  ? 1545 NAG B C6  1 
HETATM 10361 C C7  . NAG K 2 .   ? 41.134  -15.193 75.796  1.00 82.55  ? 1545 NAG B C7  1 
HETATM 10362 C C8  . NAG K 2 .   ? 40.703  -14.460 74.547  1.00 82.87  ? 1545 NAG B C8  1 
HETATM 10363 N N2  . NAG K 2 .   ? 40.226  -16.040 76.310  1.00 79.42  ? 1545 NAG B N2  1 
HETATM 10364 O O3  . NAG K 2 .   ? 40.082  -18.962 76.334  1.00 78.40  ? 1545 NAG B O3  1 
HETATM 10365 O O4  . NAG K 2 .   ? 38.252  -19.945 78.448  1.00 86.58  ? 1545 NAG B O4  1 
HETATM 10366 O O5  . NAG K 2 .   ? 39.576  -16.836 79.873  1.00 72.43  ? 1545 NAG B O5  1 
HETATM 10367 O O6  . NAG K 2 .   ? 38.716  -18.473 81.967  1.00 78.35  ? 1545 NAG B O6  1 
HETATM 10368 O O7  . NAG K 2 .   ? 42.258  -14.993 76.282  1.00 83.81  ? 1545 NAG B O7  1 
HETATM 10369 C C1  . NAG L 2 .   ? 39.042  -21.184 78.449  1.00 93.31  ? 1546 NAG B C1  1 
HETATM 10370 C C2  . NAG L 2 .   ? 39.565  -21.650 79.864  1.00 96.27  ? 1546 NAG B C2  1 
HETATM 10371 C C3  . NAG L 2 .   ? 39.641  -23.209 80.043  1.00 98.24  ? 1546 NAG B C3  1 
HETATM 10372 C C4  . NAG L 2 .   ? 38.962  -24.136 78.989  1.00 98.09  ? 1546 NAG B C4  1 
HETATM 10373 C C5  . NAG L 2 .   ? 38.764  -23.514 77.593  1.00 96.79  ? 1546 NAG B C5  1 
HETATM 10374 C C6  . NAG L 2 .   ? 37.755  -24.322 76.754  1.00 95.65  ? 1546 NAG B C6  1 
HETATM 10375 C C7  . NAG L 2 .   ? 41.215  -20.512 81.537  1.00 94.65  ? 1546 NAG B C7  1 
HETATM 10376 C C8  . NAG L 2 .   ? 42.608  -19.951 81.645  1.00 93.37  ? 1546 NAG B C8  1 
HETATM 10377 N N2  . NAG L 2 .   ? 40.852  -21.013 80.313  1.00 95.68  ? 1546 NAG B N2  1 
HETATM 10378 O O3  . NAG L 2 .   ? 39.123  -23.579 81.320  1.00 99.15  ? 1546 NAG B O3  1 
HETATM 10379 O O4  . NAG L 2 .   ? 39.650  -25.385 78.890  1.00 98.22  ? 1546 NAG B O4  1 
HETATM 10380 O O5  . NAG L 2 .   ? 38.291  -22.169 77.716  1.00 95.57  ? 1546 NAG B O5  1 
HETATM 10381 O O6  . NAG L 2 .   ? 38.255  -25.593 76.399  1.00 94.99  ? 1546 NAG B O6  1 
HETATM 10382 O O7  . NAG L 2 .   ? 40.513  -20.467 82.561  1.00 93.84  ? 1546 NAG B O7  1 
HETATM 10383 C C1  . NAG M 2 .   ? 22.111  4.552   85.771  1.00 67.80  ? 1545 NAG C C1  1 
HETATM 10384 C C2  . NAG M 2 .   ? 20.592  4.492   85.367  1.00 78.94  ? 1545 NAG C C2  1 
HETATM 10385 C C3  . NAG M 2 .   ? 20.055  5.831   84.823  1.00 80.89  ? 1545 NAG C C3  1 
HETATM 10386 C C4  . NAG M 2 .   ? 20.051  6.780   86.026  1.00 82.30  ? 1545 NAG C C4  1 
HETATM 10387 C C5  . NAG M 2 .   ? 21.554  6.958   86.413  1.00 79.30  ? 1545 NAG C C5  1 
HETATM 10388 C C6  . NAG M 2 .   ? 21.849  7.964   87.564  1.00 79.27  ? 1545 NAG C C6  1 
HETATM 10389 C C7  . NAG M 2 .   ? 20.720  2.762   83.502  1.00 84.59  ? 1545 NAG C C7  1 
HETATM 10390 C C8  . NAG M 2 .   ? 19.807  1.766   82.812  1.00 84.56  ? 1545 NAG C C8  1 
HETATM 10391 N N2  . NAG M 2 .   ? 20.098  3.438   84.474  1.00 82.16  ? 1545 NAG C N2  1 
HETATM 10392 O O3  . NAG M 2 .   ? 18.802  5.716   84.138  1.00 81.20  ? 1545 NAG C O3  1 
HETATM 10393 O O4  . NAG M 2 .   ? 19.361  7.978   85.676  1.00 87.05  ? 1545 NAG C O4  1 
HETATM 10394 O O5  . NAG M 2 .   ? 22.239  5.698   86.650  1.00 73.99  ? 1545 NAG C O5  1 
HETATM 10395 O O6  . NAG M 2 .   ? 21.614  7.475   88.882  1.00 79.48  ? 1545 NAG C O6  1 
HETATM 10396 O O7  . NAG M 2 .   ? 21.923  2.911   83.196  1.00 84.88  ? 1545 NAG C O7  1 
HETATM 10397 C C1  . NAG N 2 .   ? 18.328  8.384   86.626  1.00 91.28  ? 1546 NAG C C1  1 
HETATM 10398 C C2  . NAG N 2 .   ? 18.010  9.891   86.399  1.00 93.21  ? 1546 NAG C C2  1 
HETATM 10399 C C3  . NAG N 2 .   ? 16.753  10.387  87.173  1.00 95.43  ? 1546 NAG C C3  1 
HETATM 10400 C C4  . NAG N 2 .   ? 15.555  9.436   87.035  1.00 95.87  ? 1546 NAG C C4  1 
HETATM 10401 C C5  . NAG N 2 .   ? 15.976  7.976   87.324  1.00 95.60  ? 1546 NAG C C5  1 
HETATM 10402 C C6  . NAG N 2 .   ? 14.791  7.049   87.012  1.00 96.10  ? 1546 NAG C C6  1 
HETATM 10403 C C7  . NAG N 2 .   ? 20.312  10.867  86.043  1.00 89.64  ? 1546 NAG C C7  1 
HETATM 10404 C C8  . NAG N 2 .   ? 21.244  11.893  86.600  1.00 88.87  ? 1546 NAG C C8  1 
HETATM 10405 N N2  . NAG N 2 .   ? 19.146  10.781  86.691  1.00 91.39  ? 1546 NAG C N2  1 
HETATM 10406 O O3  . NAG N 2 .   ? 16.336  11.692  86.779  1.00 96.42  ? 1546 NAG C O3  1 
HETATM 10407 O O4  . NAG N 2 .   ? 14.465  9.886   87.841  1.00 95.49  ? 1546 NAG C O4  1 
HETATM 10408 O O5  . NAG N 2 .   ? 17.157  7.551   86.605  1.00 93.34  ? 1546 NAG C O5  1 
HETATM 10409 O O6  . NAG N 2 .   ? 15.049  5.736   87.461  1.00 97.21  ? 1546 NAG C O6  1 
HETATM 10410 O O7  . NAG N 2 .   ? 20.650  10.179  85.075  1.00 88.85  ? 1546 NAG C O7  1 
HETATM 10411 C C1  . NAG O 2 .   ? 34.531  14.960  44.107  1.00 76.80  ? 1535 NAG C C1  1 
HETATM 10412 C C2  . NAG O 2 .   ? 33.939  16.419  44.195  1.00 86.07  ? 1535 NAG C C2  1 
HETATM 10413 C C3  . NAG O 2 .   ? 35.024  17.480  44.514  1.00 87.88  ? 1535 NAG C C3  1 
HETATM 10414 C C4  . NAG O 2 .   ? 36.404  17.035  43.967  1.00 89.81  ? 1535 NAG C C4  1 
HETATM 10415 C C5  . NAG O 2 .   ? 36.157  16.067  42.775  1.00 85.88  ? 1535 NAG C C5  1 
HETATM 10416 C C6  . NAG O 2 .   ? 37.128  15.730  41.619  1.00 84.62  ? 1535 NAG C C6  1 
HETATM 10417 C C7  . NAG O 2 .   ? 33.135  17.924  42.212  1.00 90.23  ? 1535 NAG C C7  1 
HETATM 10418 C C8  . NAG O 2 .   ? 32.283  17.885  40.956  1.00 89.10  ? 1535 NAG C C8  1 
HETATM 10419 N N2  . NAG O 2 .   ? 33.189  16.773  42.954  1.00 88.57  ? 1535 NAG C N2  1 
HETATM 10420 O O3  . NAG O 2 .   ? 35.071  17.797  45.895  1.00 87.92  ? 1535 NAG C O3  1 
HETATM 10421 O O4  . NAG O 2 .   ? 37.299  18.128  43.808  1.00 96.14  ? 1535 NAG C O4  1 
HETATM 10422 O O5  . NAG O 2 .   ? 35.824  14.893  43.489  1.00 80.73  ? 1535 NAG C O5  1 
HETATM 10423 O O6  . NAG O 2 .   ? 38.400  16.313  41.733  1.00 84.71  ? 1535 NAG C O6  1 
HETATM 10424 O O7  . NAG O 2 .   ? 33.722  18.988  42.490  1.00 91.37  ? 1535 NAG C O7  1 
HETATM 10425 C C1  . NAG P 2 .   ? 37.997  18.294  45.091  1.00 101.00 ? 1536 NAG C C1  1 
HETATM 10426 C C2  . NAG P 2 .   ? 39.054  17.183  45.378  1.00 102.39 ? 1536 NAG C C2  1 
HETATM 10427 C C3  . NAG P 2 .   ? 40.304  17.392  44.484  1.00 103.08 ? 1536 NAG C C3  1 
HETATM 10428 C C4  . NAG P 2 .   ? 40.308  18.785  43.832  1.00 103.45 ? 1536 NAG C C4  1 
HETATM 10429 C C5  . NAG P 2 .   ? 39.851  19.838  44.871  1.00 103.71 ? 1536 NAG C C5  1 
HETATM 10430 C C6  . NAG P 2 .   ? 39.986  21.293  44.428  1.00 104.06 ? 1536 NAG C C6  1 
HETATM 10431 C C7  . NAG P 2 .   ? 38.629  16.727  47.871  1.00 103.32 ? 1536 NAG C C7  1 
HETATM 10432 C C8  . NAG P 2 .   ? 39.296  16.712  49.227  1.00 102.66 ? 1536 NAG C C8  1 
HETATM 10433 N N2  . NAG P 2 .   ? 39.409  17.075  46.815  1.00 103.08 ? 1536 NAG C N2  1 
HETATM 10434 O O3  . NAG P 2 .   ? 40.412  16.419  43.460  1.00 102.83 ? 1536 NAG C O3  1 
HETATM 10435 O O4  . NAG P 2 .   ? 41.580  19.049  43.270  1.00 102.90 ? 1536 NAG C O4  1 
HETATM 10436 O O5  . NAG P 2 .   ? 38.498  19.617  45.289  1.00 102.87 ? 1536 NAG C O5  1 
HETATM 10437 O O6  . NAG P 2 .   ? 39.628  22.112  45.523  1.00 104.48 ? 1536 NAG C O6  1 
HETATM 10438 O O7  . NAG P 2 .   ? 37.427  16.424  47.799  1.00 103.57 ? 1536 NAG C O7  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   . GLN A 26  ? 0.5346 0.8191 0.5137 -0.1329 -0.0615 0.0613  26  GLN A N   
2     C CA  . GLN A 26  ? 0.5134 0.8211 0.5126 -0.1166 -0.0507 0.0457  26  GLN A CA  
3     C C   . GLN A 26  ? 0.5177 0.8185 0.5027 -0.1108 -0.0542 0.0491  26  GLN A C   
4     O O   . GLN A 26  ? 0.5612 0.8216 0.5195 -0.1101 -0.0628 0.0580  26  GLN A O   
5     C CB  . GLN A 26  ? 0.5052 0.7921 0.5117 -0.1035 -0.0447 0.0335  26  GLN A CB  
6     C CG  . GLN A 26  ? 0.5482 0.8429 0.5698 -0.1067 -0.0402 0.0288  26  GLN A CG  
7     C CD  . GLN A 26  ? 0.6716 0.9404 0.6770 -0.1193 -0.0490 0.0414  26  GLN A CD  
8     O OE1 . GLN A 26  ? 0.7367 1.0048 0.7268 -0.1339 -0.0579 0.0555  26  GLN A OE1 
9     N NE2 . GLN A 26  ? 0.6874 0.9358 0.6955 -0.1152 -0.0468 0.0367  26  GLN A NE2 
10    N N   . ASN A 27  ? 0.4735 0.8114 0.4737 -0.1058 -0.0481 0.0421  27  ASN A N   
11    C CA  . ASN A 27  ? 0.4679 0.8046 0.4563 -0.0990 -0.0506 0.0451  27  ASN A CA  
12    C C   . ASN A 27  ? 0.4207 0.7890 0.4306 -0.0866 -0.0403 0.0294  27  ASN A C   
13    O O   . ASN A 27  ? 0.4057 0.8124 0.4267 -0.0888 -0.0372 0.0271  27  ASN A O   
14    C CB  . ASN A 27  ? 0.4926 0.8476 0.4720 -0.1132 -0.0574 0.0590  27  ASN A CB  
15    C CG  . ASN A 27  ? 0.5507 0.9008 0.5136 -0.1067 -0.0616 0.0648  27  ASN A CG  
16    O OD1 . ASN A 27  ? 0.5903 0.8964 0.5273 -0.0996 -0.0685 0.0709  27  ASN A OD1 
17    N ND2 . ASN A 27  ? 0.5940 0.9899 0.5707 -0.1077 -0.0576 0.0626  27  ASN A ND2 
18    N N   . ILE A 28  ? 0.3856 0.7403 0.4012 -0.0749 -0.0350 0.0187  28  ILE A N   
19    C CA  . ILE A 28  ? 0.3363 0.7203 0.3706 -0.0661 -0.0260 0.0042  28  ILE A CA  
20    C C   . ILE A 28  ? 0.3325 0.7158 0.3555 -0.0554 -0.0278 0.0064  28  ILE A C   
21    O O   . ILE A 28  ? 0.3510 0.7016 0.3528 -0.0486 -0.0338 0.0144  28  ILE A O   
22    C CB  . ILE A 28  ? 0.3151 0.6925 0.3624 -0.0610 -0.0193 -0.0079 28  ILE A CB  
23    C CG1 . ILE A 28  ? 0.3505 0.6848 0.3825 -0.0583 -0.0240 -0.0017 28  ILE A CG1 
24    C CG2 . ILE A 28  ? 0.2835 0.6807 0.3486 -0.0681 -0.0142 -0.0153 28  ILE A CG2 
25    C CD1 . ILE A 28  ? 0.3792 0.6915 0.3961 -0.0436 -0.0258 -0.0008 28  ILE A CD1 
26    N N   . THR A 29  ? 0.3061 0.7264 0.3415 -0.0535 -0.0230 -0.0005 29  THR A N   
27    C CA  . THR A 29  ? 0.3062 0.7340 0.3322 -0.0432 -0.0244 0.0020  29  THR A CA  
28    C C   . THR A 29  ? 0.2808 0.7468 0.3266 -0.0406 -0.0162 -0.0118 29  THR A C   
29    O O   . THR A 29  ? 0.2621 0.7488 0.3254 -0.0485 -0.0109 -0.0216 29  THR A O   
30    C CB  . THR A 29  ? 0.3181 0.7567 0.3332 -0.0479 -0.0301 0.0132  29  THR A CB  
31    O OG1 . THR A 29  ? 0.3236 0.7551 0.3361 -0.0621 -0.0344 0.0212  29  THR A OG1 
32    C CG2 . THR A 29  ? 0.3495 0.7606 0.3378 -0.0361 -0.0373 0.0242  29  THR A CG2 
33    N N   . GLU A 30  ? 0.2763 0.7519 0.3174 -0.0294 -0.0155 -0.0125 30  GLU A N   
34    C CA  . GLU A 30  ? 0.2550 0.7709 0.3122 -0.0294 -0.0092 -0.0237 30  GLU A CA  
35    C C   . GLU A 30  ? 0.2593 0.7947 0.3069 -0.0233 -0.0124 -0.0162 30  GLU A C   
36    O O   . GLU A 30  ? 0.2810 0.7941 0.3082 -0.0130 -0.0183 -0.0048 30  GLU A O   
37    C CB  . GLU A 30  ? 0.2549 0.7708 0.3169 -0.0221 -0.0049 -0.0312 30  GLU A CB  
38    C CG  . GLU A 30  ? 0.2528 0.7983 0.3345 -0.0301 0.0021  -0.0461 30  GLU A CG  
39    C CD  . GLU A 30  ? 0.2789 0.8140 0.3655 -0.0283 0.0058  -0.0526 30  GLU A CD  
40    O OE1 . GLU A 30  ? 0.2956 0.8266 0.3737 -0.0167 0.0047  -0.0477 30  GLU A OE1 
41    O OE2 . GLU A 30  ? 0.2868 0.8179 0.3848 -0.0378 0.0096  -0.0624 30  GLU A OE2 
42    N N   . GLU A 31  ? 0.2410 0.8157 0.3011 -0.0292 -0.0091 -0.0226 31  GLU A N   
43    C CA  . GLU A 31  ? 0.2468 0.8470 0.3003 -0.0235 -0.0111 -0.0169 31  GLU A CA  
44    C C   . GLU A 31  ? 0.2251 0.8656 0.2940 -0.0238 -0.0049 -0.0295 31  GLU A C   
45    O O   . GLU A 31  ? 0.2088 0.8643 0.2931 -0.0343 -0.0001 -0.0420 31  GLU A O   
46    C CB  . GLU A 31  ? 0.2515 0.8645 0.3036 -0.0324 -0.0142 -0.0106 31  GLU A CB  
47    C CG  . GLU A 31  ? 0.2757 0.9304 0.3305 -0.0302 -0.0134 -0.0110 31  GLU A CG  
48    C CD  . GLU A 31  ? 0.3256 0.9875 0.3712 -0.0353 -0.0187 0.0011  31  GLU A CD  
49    O OE1 . GLU A 31  ? 0.3282 1.0199 0.3717 -0.0315 -0.0193 0.0040  31  GLU A OE1 
50    O OE2 . GLU A 31  ? 0.3580 0.9979 0.3983 -0.0439 -0.0225 0.0084  31  GLU A OE2 
51    N N   . PHE A 32  ? 0.2282 0.8854 0.2904 -0.0120 -0.0055 -0.0259 32  PHE A N   
52    C CA  . PHE A 32  ? 0.2117 0.9088 0.2861 -0.0123 -0.0004 -0.0361 32  PHE A CA  
53    C C   . PHE A 32  ? 0.2122 0.9500 0.2892 -0.0141 -0.0004 -0.0359 32  PHE A C   
54    O O   . PHE A 32  ? 0.2296 0.9664 0.2931 -0.0057 -0.0052 -0.0237 32  PHE A O   
55    C CB  . PHE A 32  ? 0.2196 0.9155 0.2846 0.0038  -0.0009 -0.0310 32  PHE A CB  
56    C CG  . PHE A 32  ? 0.2062 0.9506 0.2802 0.0051  0.0029  -0.0370 32  PHE A CG  
57    C CD1 . PHE A 32  ? 0.1933 0.9587 0.2842 -0.0092 0.0080  -0.0506 32  PHE A CD1 
58    C CD2 . PHE A 32  ? 0.2247 0.9922 0.2879 0.0208  0.0007  -0.0282 32  PHE A CD2 
59    C CE1 . PHE A 32  ? 0.1876 0.9989 0.2853 -0.0108 0.0107  -0.0551 32  PHE A CE1 
60    C CE2 . PHE A 32  ? 0.2226 1.0392 0.2942 0.0216  0.0040  -0.0326 32  PHE A CE2 
61    C CZ  . PHE A 32  ? 0.1983 1.0379 0.2876 0.0044  0.0089  -0.0460 32  PHE A CZ  
62    N N   . TYR A 33  ? 0.1995 0.9713 0.2917 -0.0253 0.0042  -0.0491 33  TYR A N   
63    C CA  . TYR A 33  ? 0.1972 1.0098 0.2926 -0.0285 0.0043  -0.0504 33  TYR A CA  
64    C C   . TYR A 33  ? 0.1950 1.0478 0.2951 -0.0266 0.0067  -0.0551 33  TYR A C   
65    O O   . TYR A 33  ? 0.1907 1.0623 0.3020 -0.0392 0.0104  -0.0686 33  TYR A O   
66    C CB  . TYR A 33  ? 0.1862 1.0070 0.2922 -0.0434 0.0068  -0.0621 33  TYR A CB  
67    C CG  . TYR A 33  ? 0.2037 0.9969 0.3055 -0.0454 0.0042  -0.0557 33  TYR A CG  
68    C CD1 . TYR A 33  ? 0.2158 0.9773 0.3211 -0.0505 0.0056  -0.0607 33  TYR A CD1 
69    C CD2 . TYR A 33  ? 0.2353 1.0364 0.3291 -0.0430 0.0001  -0.0439 33  TYR A CD2 
70    C CE1 . TYR A 33  ? 0.2257 0.9681 0.3278 -0.0533 0.0031  -0.0542 33  TYR A CE1 
71    C CE2 . TYR A 33  ? 0.2512 1.0320 0.3411 -0.0475 -0.0027 -0.0368 33  TYR A CE2 
72    C CZ  . TYR A 33  ? 0.2409 0.9943 0.3355 -0.0526 -0.0011 -0.0421 33  TYR A CZ  
73    O OH  . TYR A 33  ? 0.2548 0.9934 0.3455 -0.0576 -0.0041 -0.0340 33  TYR A OH  
74    N N   . GLN A 34  ? 0.2047 1.0701 0.2941 -0.0109 0.0041  -0.0434 34  GLN A N   
75    C CA  . GLN A 34  ? 0.2018 1.1085 0.2938 -0.0053 0.0060  -0.0446 34  GLN A CA  
76    C C   . GLN A 34  ? 0.1864 1.1404 0.2903 -0.0194 0.0085  -0.0552 34  GLN A C   
77    O O   . GLN A 34  ? 0.1806 1.1668 0.2913 -0.0244 0.0110  -0.0613 34  GLN A O   
78    C CB  . GLN A 34  ? 0.2217 1.1349 0.2971 0.0170  0.0022  -0.0292 34  GLN A CB  
79    C CG  . GLN A 34  ? 0.2360 1.1930 0.3124 0.0272  0.0041  -0.0282 34  GLN A CG  
80    C CD  . GLN A 34  ? 0.2853 1.2342 0.3406 0.0547  0.0001  -0.0127 34  GLN A CD  
81    O OE1 . GLN A 34  ? 0.3083 1.2659 0.3528 0.0642  -0.0033 -0.0037 34  GLN A OE1 
82    N NE2 . GLN A 34  ? 0.3036 1.2344 0.3512 0.0686  0.0003  -0.0095 34  GLN A NE2 
83    N N   . SER A 35  ? 0.1840 1.1432 0.2894 -0.0267 0.0076  -0.0571 35  SER A N   
84    C CA  . SER A 35  ? 0.1753 1.1799 0.2891 -0.0386 0.0093  -0.0668 35  SER A CA  
85    C C   . SER A 35  ? 0.1636 1.1641 0.2874 -0.0583 0.0125  -0.0849 35  SER A C   
86    O O   . SER A 35  ? 0.1598 1.1901 0.2880 -0.0701 0.0134  -0.0953 35  SER A O   
87    C CB  . SER A 35  ? 0.1774 1.1918 0.2868 -0.0363 0.0068  -0.0604 35  SER A CB  
88    O OG  . SER A 35  ? 0.1842 1.1572 0.2906 -0.0379 0.0055  -0.0577 35  SER A OG  
89    N N   . THR A 36  ? 0.1578 1.1192 0.2829 -0.0613 0.0137  -0.0887 36  THR A N   
90    C CA  . THR A 36  ? 0.1530 1.1005 0.2838 -0.0778 0.0160  -0.1050 36  THR A CA  
91    C C   . THR A 36  ? 0.1485 1.0725 0.2806 -0.0793 0.0173  -0.1063 36  THR A C   
92    O O   . THR A 36  ? 0.1474 1.0497 0.2819 -0.0912 0.0189  -0.1176 36  THR A O   
93    C CB  . THR A 36  ? 0.1558 1.0727 0.2858 -0.0789 0.0159  -0.1076 36  THR A CB  
94    O OG1 . THR A 36  ? 0.1761 1.1182 0.3046 -0.0767 0.0146  -0.1043 36  THR A OG1 
95    C CG2 . THR A 36  ? 0.1580 1.0580 0.2907 -0.0928 0.0182  -0.1249 36  THR A CG2 
96    N N   . CYS A 37  ? 0.1496 1.0784 0.2784 -0.0659 0.0165  -0.0942 37  CYS A N   
97    C CA  . CYS A 37  ? 0.1531 1.0610 0.2822 -0.0642 0.0176  -0.0930 37  CYS A CA  
98    C C   . CYS A 37  ? 0.1503 1.0113 0.2810 -0.0719 0.0186  -0.1002 37  CYS A C   
99    O O   . CYS A 37  ? 0.1556 1.0081 0.2900 -0.0846 0.0204  -0.1098 37  CYS A O   
100   C CB  . CYS A 37  ? 0.1543 1.0979 0.2884 -0.0754 0.0191  -0.0990 37  CYS A CB  
101   S SG  . CYS A 37  ? 0.1801 1.1186 0.3121 -0.0634 0.0198  -0.0895 37  CYS A SG  
102   N N   . SER A 38  ? 0.1458 0.9776 0.2727 -0.0649 0.0172  -0.0950 38  SER A N   
103   C CA  . SER A 38  ? 0.1381 0.9282 0.2661 -0.0697 0.0181  -0.1002 38  SER A CA  
104   C C   . SER A 38  ? 0.1325 0.8896 0.2536 -0.0575 0.0154  -0.0875 38  SER A C   
105   O O   . SER A 38  ? 0.1334 0.8970 0.2473 -0.0473 0.0123  -0.0757 38  SER A O   
106   C CB  . SER A 38  ? 0.1403 0.9340 0.2715 -0.0810 0.0192  -0.1128 38  SER A CB  
107   O OG  . SER A 38  ? 0.1417 0.9611 0.2714 -0.0777 0.0176  -0.1087 38  SER A OG  
108   N N   . ALA A 39  ? 0.1253 0.8457 0.2471 -0.0594 0.0162  -0.0895 39  ALA A N   
109   C CA  . ALA A 39  ? 0.1294 0.8172 0.2435 -0.0503 0.0132  -0.0779 39  ALA A CA  
110   C C   . ALA A 39  ? 0.1301 0.7919 0.2472 -0.0569 0.0138  -0.0822 39  ALA A C   
111   O O   . ALA A 39  ? 0.1306 0.7846 0.2541 -0.0649 0.0171  -0.0941 39  ALA A O   
112   C CB  . ALA A 39  ? 0.1335 0.8029 0.2432 -0.0423 0.0130  -0.0728 39  ALA A CB  
113   N N   . VAL A 40  ? 0.1317 0.7802 0.2424 -0.0535 0.0102  -0.0719 40  VAL A N   
114   C CA  . VAL A 40  ? 0.1282 0.7573 0.2413 -0.0586 0.0105  -0.0736 40  VAL A CA  
115   C C   . VAL A 40  ? 0.1396 0.7318 0.2441 -0.0545 0.0066  -0.0616 40  VAL A C   
116   O O   . VAL A 40  ? 0.1530 0.7362 0.2454 -0.0487 0.0016  -0.0482 40  VAL A O   
117   C CB  . VAL A 40  ? 0.1203 0.7729 0.2348 -0.0623 0.0097  -0.0730 40  VAL A CB  
118   C CG1 . VAL A 40  ? 0.1270 0.7636 0.2427 -0.0655 0.0095  -0.0721 40  VAL A CG1 
119   C CG2 . VAL A 40  ? 0.1165 0.7990 0.2384 -0.0673 0.0136  -0.0876 40  VAL A CG2 
120   N N   . SER A 41  ? 0.1376 0.7068 0.2463 -0.0576 0.0086  -0.0665 41  SER A N   
121   C CA  . SER A 41  ? 0.1472 0.6831 0.2482 -0.0559 0.0050  -0.0565 41  SER A CA  
122   C C   . SER A 41  ? 0.1477 0.6887 0.2498 -0.0619 0.0034  -0.0527 41  SER A C   
123   O O   . SER A 41  ? 0.1385 0.6949 0.2500 -0.0655 0.0074  -0.0629 41  SER A O   
124   C CB  . SER A 41  ? 0.1480 0.6597 0.2535 -0.0558 0.0081  -0.0634 41  SER A CB  
125   O OG  . SER A 41  ? 0.1557 0.6755 0.2648 -0.0537 0.0113  -0.0708 41  SER A OG  
126   N N   . LYS A 42  ? 0.1633 0.6913 0.2538 -0.0630 -0.0029 -0.0378 42  LYS A N   
127   C CA  . LYS A 42  ? 0.1722 0.7140 0.2624 -0.0703 -0.0055 -0.0308 42  LYS A CA  
128   C C   . LYS A 42  ? 0.1798 0.6936 0.2613 -0.0752 -0.0106 -0.0193 42  LYS A C   
129   O O   . LYS A 42  ? 0.1944 0.6750 0.2642 -0.0724 -0.0145 -0.0128 42  LYS A O   
130   C CB  . LYS A 42  ? 0.1872 0.7468 0.2683 -0.0715 -0.0102 -0.0202 42  LYS A CB  
131   C CG  . LYS A 42  ? 0.2033 0.7929 0.2898 -0.0671 -0.0068 -0.0280 42  LYS A CG  
132   C CD  . LYS A 42  ? 0.2582 0.8603 0.3327 -0.0674 -0.0126 -0.0146 42  LYS A CD  
133   C CE  . LYS A 42  ? 0.2675 0.9061 0.3484 -0.0635 -0.0092 -0.0222 42  LYS A CE  
134   N NZ  . LYS A 42  ? 0.2893 0.9515 0.3631 -0.0662 -0.0134 -0.0112 42  LYS A NZ  
135   N N   . GLY A 43  ? 0.1769 0.7064 0.2625 -0.0825 -0.0110 -0.0161 43  GLY A N   
136   C CA  . GLY A 43  ? 0.1854 0.6927 0.2621 -0.0897 -0.0167 -0.0037 43  GLY A CA  
137   C C   . GLY A 43  ? 0.1741 0.6740 0.2602 -0.0895 -0.0128 -0.0104 43  GLY A C   
138   O O   . GLY A 43  ? 0.1825 0.6596 0.2611 -0.0946 -0.0172 -0.0014 43  GLY A O   
139   N N   . TYR A 44  ? 0.1588 0.6768 0.2592 -0.0836 -0.0050 -0.0260 44  TYR A N   
140   C CA  . TYR A 44  ? 0.1492 0.6588 0.2573 -0.0809 -0.0008 -0.0337 44  TYR A CA  
141   C C   . TYR A 44  ? 0.1463 0.6877 0.2602 -0.0830 0.0005  -0.0328 44  TYR A C   
142   O O   . TYR A 44  ? 0.1510 0.7264 0.2667 -0.0846 0.0005  -0.0317 44  TYR A O   
143   C CB  . TYR A 44  ? 0.1401 0.6460 0.2564 -0.0731 0.0062  -0.0514 44  TYR A CB  
144   C CG  . TYR A 44  ? 0.1416 0.6202 0.2536 -0.0705 0.0057  -0.0525 44  TYR A CG  
145   C CD1 . TYR A 44  ? 0.1481 0.6371 0.2594 -0.0684 0.0063  -0.0561 44  TYR A CD1 
146   C CD2 . TYR A 44  ? 0.1388 0.5848 0.2473 -0.0694 0.0046  -0.0496 44  TYR A CD2 
147   C CE1 . TYR A 44  ? 0.1538 0.6243 0.2613 -0.0646 0.0062  -0.0566 44  TYR A CE1 
148   C CE2 . TYR A 44  ? 0.1496 0.5750 0.2539 -0.0655 0.0044  -0.0505 44  TYR A CE2 
149   C CZ  . TYR A 44  ? 0.1606 0.5998 0.2645 -0.0627 0.0053  -0.0538 44  TYR A CZ  
150   O OH  . TYR A 44  ? 0.1806 0.6054 0.2803 -0.0574 0.0054  -0.0543 44  TYR A OH  
151   N N   . LEU A 45  ? 0.1373 0.6710 0.2543 -0.0818 0.0017  -0.0331 45  LEU A N   
152   C CA  . LEU A 45  ? 0.1270 0.6940 0.2491 -0.0815 0.0032  -0.0315 45  LEU A CA  
153   C C   . LEU A 45  ? 0.1202 0.6887 0.2497 -0.0693 0.0104  -0.0470 45  LEU A C   
154   O O   . LEU A 45  ? 0.1213 0.6627 0.2512 -0.0660 0.0118  -0.0499 45  LEU A O   
155   C CB  . LEU A 45  ? 0.1329 0.6995 0.2491 -0.0925 -0.0035 -0.0136 45  LEU A CB  
156   C CG  . LEU A 45  ? 0.1393 0.7058 0.2439 -0.1056 -0.0118 0.0029  45  LEU A CG  
157   C CD1 . LEU A 45  ? 0.1562 0.7042 0.2500 -0.1184 -0.0198 0.0195  45  LEU A CD1 
158   C CD2 . LEU A 45  ? 0.1417 0.7554 0.2496 -0.1088 -0.0118 0.0065  45  LEU A CD2 
159   N N   . SER A 46  ? 0.1118 0.7118 0.2451 -0.0622 0.0146  -0.0566 46  SER A N   
160   C CA  . SER A 46  ? 0.1095 0.7098 0.2452 -0.0487 0.0210  -0.0729 46  SER A CA  
161   C C   . SER A 46  ? 0.1142 0.7156 0.2510 -0.0424 0.0223  -0.0707 46  SER A C   
162   O O   . SER A 46  ? 0.1148 0.7338 0.2524 -0.0487 0.0186  -0.0559 46  SER A O   
163   C CB  . SER A 46  ? 0.1072 0.7474 0.2436 -0.0424 0.0236  -0.0800 46  SER A CB  
164   O OG  . SER A 46  ? 0.1020 0.7799 0.2400 -0.0460 0.0209  -0.0660 46  SER A OG  
165   N N   . ALA A 47  ? 0.1197 0.7037 0.2550 -0.0298 0.0274  -0.0861 47  ALA A N   
166   C CA  . ALA A 47  ? 0.1212 0.7100 0.2561 -0.0181 0.0301  -0.0882 47  ALA A CA  
167   C C   . ALA A 47  ? 0.1296 0.7004 0.2580 -0.0040 0.0353  -0.1090 47  ALA A C   
168   O O   . ALA A 47  ? 0.1400 0.6725 0.2657 -0.0067 0.0360  -0.1172 47  ALA A O   
169   C CB  . ALA A 47  ? 0.1209 0.6782 0.2566 -0.0229 0.0282  -0.0804 47  ALA A CB  
170   N N   . LEU A 48  ? 0.1290 0.7266 0.2531 0.0106  0.0385  -0.1178 48  LEU A N   
171   C CA  . LEU A 48  ? 0.1380 0.7152 0.2514 0.0221  0.0421  -0.1383 48  LEU A CA  
172   C C   . LEU A 48  ? 0.1568 0.7289 0.2604 0.0431  0.0456  -0.1478 48  LEU A C   
173   O O   . LEU A 48  ? 0.1613 0.7732 0.2642 0.0553  0.0470  -0.1454 48  LEU A O   
174   C CB  . LEU A 48  ? 0.1356 0.7438 0.2469 0.0226  0.0424  -0.1446 48  LEU A CB  
175   C CG  . LEU A 48  ? 0.1033 0.7382 0.2237 0.0063  0.0389  -0.1322 48  LEU A CG  
176   C CD1 . LEU A 48  ? 0.0985 0.7510 0.2135 0.0102  0.0404  -0.1443 48  LEU A CD1 
177   C CD2 . LEU A 48  ? 0.1106 0.7134 0.2348 -0.0086 0.0363  -0.1273 48  LEU A CD2 
178   N N   . ARG A 49  ? 0.1732 0.6971 0.2676 0.0481  0.0470  -0.1585 49  ARG A N   
179   C CA  . ARG A 49  ? 0.1992 0.7091 0.2802 0.0700  0.0500  -0.1683 49  ARG A CA  
180   C C   . ARG A 49  ? 0.2235 0.7547 0.2911 0.0880  0.0522  -0.1821 49  ARG A C   
181   O O   . ARG A 49  ? 0.2345 0.7584 0.2952 0.0839  0.0518  -0.1934 49  ARG A O   
182   C CB  . ARG A 49  ? 0.2163 0.6654 0.2857 0.0699  0.0502  -0.1793 49  ARG A CB  
183   C CG  . ARG A 49  ? 0.2173 0.6473 0.2811 0.0841  0.0517  -0.1780 49  ARG A CG  
184   C CD  . ARG A 49  ? 0.2436 0.6194 0.2870 0.0919  0.0523  -0.1942 49  ARG A CD  
185   N NE  . ARG A 49  ? 0.3245 0.7077 0.3492 0.1157  0.0543  -0.2073 49  ARG A NE  
186   C CZ  . ARG A 49  ? 0.3938 0.7554 0.3992 0.1198  0.0537  -0.2246 49  ARG A CZ  
187   N NH1 . ARG A 49  ? 0.3919 0.7245 0.3959 0.0994  0.0513  -0.2301 49  ARG A NH1 
188   N NH2 . ARG A 49  ? 0.4471 0.8168 0.4329 0.1452  0.0554  -0.2367 49  ARG A NH2 
189   N N   . THR A 50  ? 0.2345 0.7944 0.2976 0.1090  0.0545  -0.1812 50  THR A N   
190   C CA  . THR A 50  ? 0.2615 0.8350 0.3072 0.1309  0.0568  -0.1967 50  THR A CA  
191   C C   . THR A 50  ? 0.2958 0.8523 0.3246 0.1579  0.0594  -0.2042 50  THR A C   
192   O O   . THR A 50  ? 0.3273 0.8919 0.3375 0.1819  0.0614  -0.2174 50  THR A O   
193   C CB  . THR A 50  ? 0.2413 0.8844 0.2961 0.1338  0.0574  -0.1887 50  THR A CB  
194   O OG1 . THR A 50  ? 0.2085 0.8903 0.2823 0.1242  0.0562  -0.1669 50  THR A OG1 
195   C CG2 . THR A 50  ? 0.2336 0.8848 0.2944 0.1152  0.0554  -0.1898 50  THR A CG2 
196   N N   . GLY A 51  ? 0.2940 0.8259 0.3275 0.1556  0.0591  -0.1961 51  GLY A N   
197   C CA  . GLY A 51  ? 0.3271 0.8495 0.3460 0.1826  0.0616  -0.2003 51  GLY A CA  
198   C C   . GLY A 51  ? 0.3247 0.8111 0.3481 0.1768  0.0609  -0.1925 51  GLY A C   
199   O O   . GLY A 51  ? 0.3013 0.7702 0.3391 0.1518  0.0585  -0.1839 51  GLY A O   
200   N N   . TRP A 52  ? 0.3538 0.8307 0.3633 0.2020  0.0630  -0.1957 52  TRP A N   
201   C CA  . TRP A 52  ? 0.3576 0.7980 0.3677 0.2006  0.0627  -0.1899 52  TRP A CA  
202   C C   . TRP A 52  ? 0.3539 0.8364 0.3681 0.2206  0.0649  -0.1788 52  TRP A C   
203   O O   . TRP A 52  ? 0.3710 0.8888 0.3745 0.2471  0.0674  -0.1833 52  TRP A O   
204   C CB  . TRP A 52  ? 0.4050 0.7729 0.3868 0.2127  0.0624  -0.2076 52  TRP A CB  
205   C CG  . TRP A 52  ? 0.4209 0.7457 0.3959 0.1933  0.0598  -0.2183 52  TRP A CG  
206   C CD1 . TRP A 52  ? 0.4712 0.7739 0.4239 0.2001  0.0590  -0.2363 52  TRP A CD1 
207   C CD2 . TRP A 52  ? 0.4079 0.7071 0.3971 0.1635  0.0574  -0.2120 52  TRP A CD2 
208   N NE1 . TRP A 52  ? 0.4690 0.7360 0.4221 0.1743  0.0561  -0.2410 52  TRP A NE1 
209   C CE2 . TRP A 52  ? 0.4304 0.6960 0.4063 0.1523  0.0553  -0.2261 52  TRP A CE2 
210   C CE3 . TRP A 52  ? 0.3757 0.6778 0.3862 0.1456  0.0566  -0.1960 52  TRP A CE3 
211   C CZ2 . TRP A 52  ? 0.4087 0.6494 0.3937 0.1245  0.0529  -0.2237 52  TRP A CZ2 
212   C CZ3 . TRP A 52  ? 0.3610 0.6350 0.3789 0.1201  0.0543  -0.1946 52  TRP A CZ3 
213   C CH2 . TRP A 52  ? 0.3792 0.6252 0.3852 0.1100  0.0526  -0.2079 52  TRP A CH2 
214   N N   . TYR A 53  ? 0.3350 0.8124 0.3630 0.2088  0.0638  -0.1648 53  TYR A N   
215   C CA  . TYR A 53  ? 0.3379 0.8492 0.3699 0.2245  0.0654  -0.1534 53  TYR A CA  
216   C C   . TYR A 53  ? 0.3658 0.8214 0.3844 0.2358  0.0659  -0.1574 53  TYR A C   
217   O O   . TYR A 53  ? 0.3632 0.7785 0.3881 0.2159  0.0639  -0.1539 53  TYR A O   
218   C CB  . TYR A 53  ? 0.2952 0.8511 0.3540 0.1986  0.0628  -0.1323 53  TYR A CB  
219   C CG  . TYR A 53  ? 0.2963 0.8922 0.3630 0.2065  0.0632  -0.1171 53  TYR A CG  
220   C CD1 . TYR A 53  ? 0.3078 0.9768 0.3795 0.2185  0.0644  -0.1084 53  TYR A CD1 
221   C CD2 . TYR A 53  ? 0.3038 0.8690 0.3737 0.2009  0.0622  -0.1104 53  TYR A CD2 
222   C CE1 . TYR A 53  ? 0.3129 1.0241 0.3922 0.2241  0.0644  -0.0933 53  TYR A CE1 
223   C CE2 . TYR A 53  ? 0.3082 0.9126 0.3854 0.2069  0.0622  -0.0959 53  TYR A CE2 
224   C CZ  . TYR A 53  ? 0.3086 0.9863 0.3906 0.2179  0.0631  -0.0872 53  TYR A CZ  
225   O OH  . TYR A 53  ? 0.3057 1.0247 0.3949 0.2222  0.0628  -0.0721 53  TYR A OH  
226   N N   . THR A 54  ? 0.4035 0.8560 0.4016 0.2693  0.0686  -0.1652 54  THR A N   
227   C CA  . THR A 54  ? 0.4407 0.8395 0.4217 0.2838  0.0691  -0.1696 54  THR A CA  
228   C C   . THR A 54  ? 0.4172 0.8483 0.4163 0.2806  0.0693  -0.1510 54  THR A C   
229   O O   . THR A 54  ? 0.3953 0.8946 0.4115 0.2785  0.0697  -0.1379 54  THR A O   
230   C CB  . THR A 54  ? 0.4937 0.8895 0.4450 0.3249  0.0717  -0.1832 54  THR A CB  
231   O OG1 . THR A 54  ? 0.5441 0.8809 0.4698 0.3278  0.0703  -0.2032 54  THR A OG1 
232   C CG2 . THR A 54  ? 0.5358 0.9152 0.4727 0.3522  0.0734  -0.1806 54  THR A CG2 
233   N N   . SER A 55  ? 0.4291 0.8129 0.4239 0.2785  0.0686  -0.1490 55  SER A N   
234   C CA  . SER A 55  ? 0.4255 0.8353 0.4282 0.2877  0.0694  -0.1347 55  SER A CA  
235   C C   . SER A 55  ? 0.4569 0.8043 0.4442 0.2964  0.0694  -0.1381 55  SER A C   
236   O O   . SER A 55  ? 0.4669 0.7546 0.4498 0.2788  0.0674  -0.1438 55  SER A O   
237   C CB  . SER A 55  ? 0.3776 0.8317 0.4102 0.2587  0.0671  -0.1148 55  SER A CB  
238   O OG  . SER A 55  ? 0.3753 0.8400 0.4116 0.2663  0.0674  -0.1032 55  SER A OG  
239   N N   . VAL A 56  ? 0.4756 0.8422 0.4556 0.3231  0.0715  -0.1329 56  VAL A N   
240   C CA  . VAL A 56  ? 0.5176 0.8250 0.4740 0.3426  0.0720  -0.1394 56  VAL A CA  
241   C C   . VAL A 56  ? 0.4962 0.8091 0.4678 0.3329  0.0713  -0.1238 56  VAL A C   
242   O O   . VAL A 56  ? 0.4913 0.8584 0.4712 0.3468  0.0729  -0.1119 56  VAL A O   
243   C CB  . VAL A 56  ? 0.5620 0.8818 0.4924 0.3876  0.0749  -0.1471 56  VAL A CB  
244   C CG1 . VAL A 56  ? 0.6152 0.8523 0.5117 0.4065  0.0742  -0.1592 56  VAL A CG1 
245   C CG2 . VAL A 56  ? 0.5799 0.9328 0.5029 0.4002  0.0762  -0.1577 56  VAL A CG2 
246   N N   . ILE A 57  ? 0.4887 0.7468 0.4629 0.3094  0.0690  -0.1236 57  ILE A N   
247   C CA  . ILE A 57  ? 0.4634 0.7229 0.4525 0.2962  0.0680  -0.1092 57  ILE A CA  
248   C C   . ILE A 57  ? 0.5014 0.7078 0.4685 0.3159  0.0686  -0.1125 57  ILE A C   
249   O O   . ILE A 57  ? 0.5354 0.6754 0.4795 0.3193  0.0677  -0.1254 57  ILE A O   
250   C CB  . ILE A 57  ? 0.4275 0.6700 0.4356 0.2577  0.0650  -0.1049 57  ILE A CB  
251   C CG1 . ILE A 57  ? 0.3961 0.6951 0.4244 0.2409  0.0641  -0.0993 57  ILE A CG1 
252   C CG2 . ILE A 57  ? 0.4096 0.6502 0.4308 0.2446  0.0637  -0.0911 57  ILE A CG2 
253   C CD1 . ILE A 57  ? 0.3966 0.6718 0.4356 0.2093  0.0614  -0.1009 57  ILE A CD1 
254   N N   . THR A 58  ? 0.4982 0.7354 0.4711 0.3285  0.0697  -0.1002 58  THR A N   
255   C CA  . THR A 58  ? 0.5418 0.7380 0.4925 0.3533  0.0707  -0.1019 58  THR A CA  
256   C C   . THR A 58  ? 0.5213 0.7183 0.4890 0.3359  0.0694  -0.0871 58  THR A C   
257   O O   . THR A 58  ? 0.4858 0.7418 0.4780 0.3232  0.0690  -0.0729 58  THR A O   
258   C CB  . THR A 58  ? 0.5636 0.8007 0.4998 0.3954  0.0738  -0.1015 58  THR A CB  
259   O OG1 . THR A 58  ? 0.5675 0.8519 0.5054 0.4042  0.0752  -0.1069 58  THR A OG1 
260   C CG2 . THR A 58  ? 0.6224 0.7937 0.5207 0.4269  0.0742  -0.1134 58  THR A CG2 
261   N N   . ILE A 59  ? 0.5532 0.6839 0.5062 0.3341  0.0683  -0.0902 59  ILE A N   
262   C CA  . ILE A 59  ? 0.5375 0.6617 0.5055 0.3150  0.0670  -0.0775 59  ILE A CA  
263   C C   . ILE A 59  ? 0.5849 0.6691 0.5325 0.3367  0.0676  -0.0759 59  ILE A C   
264   O O   . ILE A 59  ? 0.6270 0.6438 0.5482 0.3448  0.0667  -0.0862 59  ILE A O   
265   C CB  . ILE A 59  ? 0.5105 0.6005 0.4905 0.2780  0.0643  -0.0788 59  ILE A CB  
266   C CG1 . ILE A 59  ? 0.4683 0.6050 0.4713 0.2559  0.0633  -0.0763 59  ILE A CG1 
267   C CG2 . ILE A 59  ? 0.4865 0.5691 0.4790 0.2617  0.0630  -0.0666 59  ILE A CG2 
268   C CD1 . ILE A 59  ? 0.4615 0.5745 0.4782 0.2211  0.0607  -0.0751 59  ILE A CD1 
269   N N   . GLU A 60  ? 0.5825 0.7103 0.5419 0.3447  0.0685  -0.0621 60  GLU A N   
270   C CA  . GLU A 60  ? 0.6264 0.7285 0.5710 0.3644  0.0691  -0.0572 60  GLU A CA  
271   C C   . GLU A 60  ? 0.6202 0.6767 0.5712 0.3365  0.0668  -0.0528 60  GLU A C   
272   O O   . GLU A 60  ? 0.5830 0.6622 0.5594 0.3060  0.0652  -0.0452 60  GLU A O   
273   C CB  . GLU A 60  ? 0.6108 0.7854 0.5696 0.3786  0.0706  -0.0426 60  GLU A CB  
274   C CG  . GLU A 60  ? 0.6675 0.8906 0.6151 0.4156  0.0736  -0.0450 60  GLU A CG  
275   C CD  . GLU A 60  ? 0.7267 1.0025 0.6770 0.4394  0.0753  -0.0312 60  GLU A CD  
276   O OE1 . GLU A 60  ? 0.7207 1.0226 0.6920 0.4187  0.0738  -0.0172 60  GLU A OE1 
277   O OE2 . GLU A 60  ? 0.7808 1.0732 0.7110 0.4798  0.0781  -0.0341 60  GLU A OE2 
278   N N   . LEU A 61  ? 0.6666 0.6579 0.5926 0.3474  0.0662  -0.0571 61  LEU A N   
279   C CA  . LEU A 61  ? 0.6642 0.6164 0.5941 0.3258  0.0643  -0.0508 61  LEU A CA  
280   C C   . LEU A 61  ? 0.6513 0.6429 0.5945 0.3321  0.0652  -0.0355 61  LEU A C   
281   O O   . LEU A 61  ? 0.6636 0.6899 0.6007 0.3614  0.0672  -0.0319 61  LEU A O   
282   C CB  . LEU A 61  ? 0.7209 0.5939 0.6161 0.3387  0.0630  -0.0587 61  LEU A CB  
283   C CG  . LEU A 61  ? 0.7253 0.5581 0.6165 0.3287  0.0616  -0.0504 61  LEU A CG  
284   C CD1 . LEU A 61  ? 0.7103 0.5156 0.6130 0.2905  0.0592  -0.0516 61  LEU A CD1 
285   C CD2 . LEU A 61  ? 0.7887 0.5557 0.6401 0.3542  0.0604  -0.0558 61  LEU A CD2 
286   N N   . SER A 62  ? 0.6341 0.6219 0.5940 0.3060  0.0636  -0.0266 62  SER A N   
287   C CA  . SER A 62  ? 0.6378 0.6553 0.6066 0.3121  0.0639  -0.0125 62  SER A CA  
288   C C   . SER A 62  ? 0.6866 0.6453 0.6347 0.3213  0.0636  -0.0112 62  SER A C   
289   O O   . SER A 62  ? 0.6840 0.6056 0.6350 0.2975  0.0618  -0.0102 62  SER A O   
290   C CB  . SER A 62  ? 0.5840 0.6374 0.5821 0.2800  0.0619  -0.0025 62  SER A CB  
291   O OG  . SER A 62  ? 0.5597 0.6720 0.5743 0.2745  0.0616  -0.0009 62  SER A OG  
292   N N   . ASN A 63  ? 0.7423 0.6929 0.6682 0.3565  0.0652  -0.0109 63  ASN A N   
293   C CA  . ASN A 63  ? 0.8044 0.6846 0.7025 0.3665  0.0641  -0.0128 63  ASN A CA  
294   C C   . ASN A 63  ? 0.8058 0.6884 0.7117 0.3610  0.0637  0.0009  63  ASN A C   
295   O O   . ASN A 63  ? 0.7819 0.7241 0.7069 0.3644  0.0648  0.0118  63  ASN A O   
296   C CB  . ASN A 63  ? 0.8610 0.7167 0.7247 0.4081  0.0652  -0.0200 63  ASN A CB  
297   C CG  . ASN A 63  ? 0.9282 0.6922 0.7562 0.4099  0.0624  -0.0295 63  ASN A CG  
298   O OD1 . ASN A 63  ? 0.9334 0.6544 0.7593 0.3890  0.0601  -0.0250 63  ASN A OD1 
299   N ND2 . ASN A 63  ? 0.9784 0.7119 0.7768 0.4338  0.0619  -0.0426 63  ASN A ND2 
300   N N   . ILE A 64  ? 0.8464 0.6658 0.7373 0.3509  0.0618  0.0010  64  ILE A N   
301   C CA  . ILE A 64  ? 0.8656 0.6824 0.7599 0.3491  0.0615  0.0139  64  ILE A CA  
302   C C   . ILE A 64  ? 0.9405 0.7301 0.8044 0.3864  0.0621  0.0164  64  ILE A C   
303   O O   . ILE A 64  ? 1.0012 0.7291 0.8319 0.4013  0.0607  0.0073  64  ILE A O   
304   C CB  . ILE A 64  ? 0.8641 0.6270 0.7555 0.3203  0.0591  0.0144  64  ILE A CB  
305   C CG1 . ILE A 64  ? 0.8170 0.5930 0.7313 0.2856  0.0582  0.0096  64  ILE A CG1 
306   C CG2 . ILE A 64  ? 0.8596 0.6293 0.7585 0.3164  0.0589  0.0286  64  ILE A CG2 
307   C CD1 . ILE A 64  ? 0.8158 0.5459 0.7281 0.2572  0.0560  0.0104  64  ILE A CD1 
308   N N   . LYS A 65  ? 0.9549 0.7872 0.8277 0.4013  0.0636  0.0289  65  LYS A N   
309   C CA  . LYS A 65  ? 1.0307 0.8287 0.8751 0.4318  0.0636  0.0346  65  LYS A CA  
310   C C   . LYS A 65  ? 1.0422 0.8079 0.8887 0.4116  0.0618  0.0449  65  LYS A C   
311   O O   . LYS A 65  ? 1.0011 0.8131 0.8727 0.3997  0.0624  0.0569  65  LYS A O   
312   C CB  . LYS A 65  ? 1.0358 0.8917 0.8782 0.4707  0.0664  0.0410  65  LYS A CB  
313   C CG  . LYS A 65  ? 0.9914 0.9419 0.8713 0.4599  0.0681  0.0484  65  LYS A CG  
314   C CD  . LYS A 65  ? 0.9665 0.9352 0.8761 0.4204  0.0664  0.0579  65  LYS A CD  
315   C CE  . LYS A 65  ? 0.9263 0.9818 0.8645 0.4151  0.0668  0.0697  65  LYS A CE  
316   N NZ  . LYS A 65  ? 0.8966 0.9553 0.8501 0.3909  0.0649  0.0807  65  LYS A NZ  
317   N N   . GLU A 66  ? 1.1016 0.7874 0.9201 0.4066  0.0590  0.0398  66  GLU A N   
318   C CA  . GLU A 66  ? 1.1193 0.7629 0.9359 0.3819  0.0567  0.0471  66  GLU A CA  
319   C C   . GLU A 66  ? 1.1419 0.7854 0.9504 0.3998  0.0570  0.0610  66  GLU A C   
320   O O   . GLU A 66  ? 1.1911 0.8162 0.9715 0.4369  0.0572  0.0621  66  GLU A O   
321   C CB  . GLU A 66  ? 1.1692 0.7290 0.9541 0.3725  0.0529  0.0377  66  GLU A CB  
322   C CG  . GLU A 66  ? 1.2252 0.7254 0.9912 0.3601  0.0497  0.0457  66  GLU A CG  
323   C CD  . GLU A 66  ? 1.3369 0.7502 1.0606 0.3601  0.0450  0.0366  66  GLU A CD  
324   O OE1 . GLU A 66  ? 1.3927 0.7536 1.1004 0.3418  0.0413  0.0426  66  GLU A OE1 
325   O OE2 . GLU A 66  ? 1.3648 0.7624 1.0701 0.3772  0.0445  0.0238  66  GLU A OE2 
326   N N   . ASN A 67  ? 1.1120 0.7760 0.9433 0.3754  0.0569  0.0717  67  ASN A N   
327   C CA  . ASN A 67  ? 1.1229 0.8001 0.9514 0.3920  0.0575  0.0857  67  ASN A CA  
328   C C   . ASN A 67  ? 1.1538 0.7732 0.9644 0.3824  0.0550  0.0933  67  ASN A C   
329   O O   . ASN A 67  ? 1.1244 0.7601 0.9540 0.3598  0.0548  0.1027  67  ASN A O   
330   C CB  . ASN A 67  ? 1.0673 0.8286 0.9310 0.3876  0.0597  0.0949  67  ASN A CB  
331   C CG  . ASN A 67  ? 1.0702 0.8843 0.9332 0.4225  0.0621  0.0957  67  ASN A CG  
332   O OD1 . ASN A 67  ? 1.1054 0.9115 0.9464 0.4567  0.0629  0.1012  67  ASN A OD1 
333   N ND2 . ASN A 67  ? 1.0237 0.8919 0.9090 0.4147  0.0632  0.0904  67  ASN A ND2 
334   N N   . LYS A 68  ? 1.2169 0.7666 0.9878 0.4005  0.0526  0.0885  68  LYS A N   
335   C CA  . LYS A 68  ? 1.2700 0.7578 1.0102 0.4071  0.0497  0.0969  68  LYS A CA  
336   C C   . LYS A 68  ? 1.2401 0.7644 0.9993 0.4025  0.0511  0.1131  68  LYS A C   
337   O O   . LYS A 68  ? 1.2471 0.8000 1.0033 0.4320  0.0528  0.1214  68  LYS A O   
338   C CB  . LYS A 68  ? 1.3419 0.7871 1.0393 0.4514  0.0486  0.0935  68  LYS A CB  
339   C CG  . LYS A 68  ? 1.3620 0.7984 1.0453 0.4679  0.0488  0.0772  68  LYS A CG  
340   C CD  . LYS A 68  ? 1.3969 0.8544 1.0614 0.5193  0.0511  0.0771  68  LYS A CD  
341   C CE  . LYS A 68  ? 1.4249 0.8720 1.0723 0.5442  0.0508  0.0919  68  LYS A CE  
342   N NZ  . LYS A 68  ? 1.4647 0.9265 1.0882 0.5977  0.0527  0.0919  68  LYS A NZ  
343   N N   . CYS A 69  ? 1.2010 0.7289 0.9809 0.3650  0.0502  0.1172  69  CYS A N   
344   C CA  . CYS A 69  ? 1.1792 0.7250 0.9714 0.3552  0.0505  0.1315  69  CYS A CA  
345   C C   . CYS A 69  ? 1.2202 0.6964 0.9924 0.3299  0.0466  0.1336  69  CYS A C   
346   O O   . CYS A 69  ? 1.2626 0.6788 1.0073 0.3281  0.0435  0.1253  69  CYS A O   
347   C CB  . CYS A 69  ? 1.0970 0.7122 0.9321 0.3301  0.0526  0.1323  69  CYS A CB  
348   S SG  . CYS A 69  ? 1.0758 0.6611 0.9198 0.2849  0.0505  0.1269  69  CYS A SG  
349   N N   . ASN A 70  ? 1.2090 0.6955 0.9946 0.3090  0.0463  0.1450  70  ASN A N   
350   C CA  . ASN A 70  ? 1.2356 0.6771 1.0130 0.2765  0.0431  0.1479  70  ASN A CA  
351   C C   . ASN A 70  ? 1.1445 0.6386 0.9608 0.2441  0.0450  0.1478  70  ASN A C   
352   O O   . ASN A 70  ? 1.1008 0.6462 0.9406 0.2438  0.0472  0.1553  70  ASN A O   
353   C CB  . ASN A 70  ? 1.3024 0.7056 1.0560 0.2833  0.0408  0.1625  70  ASN A CB  
354   C CG  . ASN A 70  ? 1.4610 0.8430 1.1861 0.3258  0.0406  0.1648  70  ASN A CG  
355   O OD1 . ASN A 70  ? 1.5505 0.8982 1.2518 0.3440  0.0393  0.1544  70  ASN A OD1 
356   N ND2 . ASN A 70  ? 1.6361 1.0408 1.3627 0.3436  0.0420  0.1780  70  ASN A ND2 
357   N N   . GLY A 71  ? 1.1119 0.5948 0.9338 0.2187  0.0439  0.1384  71  GLY A N   
358   C CA  . GLY A 71  ? 1.0291 0.5555 0.8833 0.1892  0.0453  0.1375  71  GLY A CA  
359   C C   . GLY A 71  ? 1.0233 0.5285 0.8735 0.1633  0.0433  0.1474  71  GLY A C   
360   O O   . GLY A 71  ? 1.0744 0.5302 0.8970 0.1663  0.0406  0.1555  71  GLY A O   
361   N N   . THR A 72  ? 0.9623 0.5046 0.8382 0.1387  0.0445  0.1474  72  THR A N   
362   C CA  . THR A 72  ? 0.9588 0.4885 0.8329 0.1125  0.0429  0.1562  72  THR A CA  
363   C C   . THR A 72  ? 0.9977 0.4771 0.8510 0.0939  0.0394  0.1514  72  THR A C   
364   O O   . THR A 72  ? 0.9853 0.4730 0.8474 0.0840  0.0397  0.1399  72  THR A O   
365   C CB  . THR A 72  ? 0.8998 0.4858 0.8056 0.0946  0.0451  0.1560  72  THR A CB  
366   O OG1 . THR A 72  ? 0.8592 0.4547 0.7759 0.0786  0.0452  0.1443  72  THR A OG1 
367   C CG2 . THR A 72  ? 0.8617 0.4971 0.7871 0.1126  0.0475  0.1562  72  THR A CG2 
368   N N   . ASP A 73  ? 1.0487 0.4755 0.8731 0.0880  0.0356  0.1606  73  ASP A N   
369   C CA  . ASP A 73  ? 1.0988 0.4650 0.8937 0.0752  0.0308  0.1558  73  ASP A CA  
370   C C   . ASP A 73  ? 1.1177 0.4549 0.8949 0.1003  0.0302  0.1428  73  ASP A C   
371   O O   . ASP A 73  ? 1.0746 0.4457 0.8716 0.1056  0.0331  0.1305  73  ASP A O   
372   C CB  . ASP A 73  ? 1.0798 0.4598 0.8873 0.0402  0.0299  0.1518  73  ASP A CB  
373   C CG  . ASP A 73  ? 1.1480 0.4646 0.9227 0.0235  0.0240  0.1477  73  ASP A CG  
374   O OD1 . ASP A 73  ? 1.2033 0.4656 0.9466 0.0420  0.0208  0.1434  73  ASP A OD1 
375   O OD2 . ASP A 73  ? 1.1548 0.4757 0.9331 -0.0083 0.0219  0.1489  73  ASP A OD2 
376   N N   . ALA A 74  ? 1.1768 0.4503 0.9151 0.1156  0.0261  0.1457  74  ALA A N   
377   C CA  . ALA A 74  ? 1.2082 0.4495 0.9244 0.1422  0.0251  0.1336  74  ALA A CA  
378   C C   . ALA A 74  ? 1.2647 0.4369 0.9453 0.1281  0.0188  0.1259  74  ALA A C   
379   O O   . ALA A 74  ? 1.3216 0.4401 0.9666 0.1510  0.0156  0.1207  74  ALA A O   
380   C CB  . ALA A 74  ? 1.2357 0.4642 0.9340 0.1819  0.0260  0.1389  74  ALA A CB  
381   N N   . LYS A 75  ? 1.2547 0.4290 0.9434 0.0908  0.0168  0.1254  75  LYS A N   
382   C CA  . LYS A 75  ? 1.2930 0.4262 0.9610 0.0747  0.0121  0.1137  75  LYS A CA  
383   C C   . LYS A 75  ? 1.2303 0.4198 0.9323 0.0749  0.0170  0.0994  75  LYS A C   
384   O O   . LYS A 75  ? 1.2502 0.4174 0.9396 0.0739  0.0150  0.0861  75  LYS A O   
385   C CB  . LYS A 75  ? 1.3169 0.4264 0.9750 0.0324  0.0068  0.1219  75  LYS A CB  
386   C CG  . LYS A 75  ? 1.3990 0.4469 1.0195 0.0272  0.0006  0.1365  75  LYS A CG  
387   C CD  . LYS A 75  ? 1.4062 0.4831 1.0439 -0.0075 0.0003  0.1520  75  LYS A CD  
388   C CE  . LYS A 75  ? 1.4672 0.5075 1.0805 -0.0035 -0.0030 0.1694  75  LYS A CE  
389   N NZ  . LYS A 75  ? 1.4180 0.5237 1.0673 -0.0069 0.0027  0.1817  75  LYS A NZ  
390   N N   . VAL A 76  ? 1.1550 0.4158 0.8982 0.0752  0.0231  0.1028  76  VAL A N   
391   C CA  . VAL A 76  ? 1.0881 0.4084 0.8652 0.0811  0.0282  0.0923  76  VAL A CA  
392   C C   . VAL A 76  ? 1.0880 0.4144 0.8612 0.1198  0.0307  0.0848  76  VAL A C   
393   O O   . VAL A 76  ? 1.0924 0.4252 0.8631 0.1434  0.0323  0.0924  76  VAL A O   
394   C CB  . VAL A 76  ? 1.0239 0.4105 0.8396 0.0711  0.0326  0.1004  76  VAL A CB  
395   C CG1 . VAL A 76  ? 0.9710 0.4166 0.8184 0.0815  0.0372  0.0915  76  VAL A CG1 
396   C CG2 . VAL A 76  ? 1.0150 0.4072 0.8378 0.0347  0.0308  0.1063  76  VAL A CG2 
397   N N   . LYS A 77  ? 1.0812 0.4093 0.8539 0.1265  0.0311  0.0705  77  LYS A N   
398   C CA  . LYS A 77  ? 1.0859 0.4209 0.8525 0.1627  0.0333  0.0630  77  LYS A CA  
399   C C   . LYS A 77  ? 1.0344 0.4104 0.8231 0.1620  0.0360  0.0503  77  LYS A C   
400   O O   . LYS A 77  ? 1.0603 0.4115 0.8303 0.1745  0.0347  0.0386  77  LYS A O   
401   C CB  . LYS A 77  ? 1.1708 0.4307 0.8896 0.1809  0.0285  0.0588  77  LYS A CB  
402   C CG  . LYS A 77  ? 1.2406 0.4804 0.9400 0.2088  0.0284  0.0692  77  LYS A CG  
403   C CD  . LYS A 77  ? 1.3703 0.5245 1.0225 0.2050  0.0215  0.0739  77  LYS A CD  
404   C CE  . LYS A 77  ? 1.4185 0.5640 1.0599 0.2253  0.0218  0.0883  77  LYS A CE  
405   N NZ  . LYS A 77  ? 1.5373 0.5932 1.1236 0.2374  0.0149  0.0906  77  LYS A NZ  
406   N N   . LEU A 78  ? 0.9607 0.3986 0.7876 0.1484  0.0395  0.0528  78  LEU A N   
407   C CA  . LEU A 78  ? 0.9082 0.3843 0.7578 0.1392  0.0414  0.0423  78  LEU A CA  
408   C C   . LEU A 78  ? 0.9148 0.3951 0.7564 0.1663  0.0425  0.0317  78  LEU A C   
409   O O   . LEU A 78  ? 0.9293 0.3910 0.7610 0.1619  0.0411  0.0201  78  LEU A O   
410   C CB  . LEU A 78  ? 0.8390 0.3795 0.7263 0.1284  0.0446  0.0476  78  LEU A CB  
411   C CG  . LEU A 78  ? 0.8304 0.3679 0.7241 0.1025  0.0435  0.0574  78  LEU A CG  
412   C CD1 . LEU A 78  ? 0.7645 0.3613 0.6923 0.0902  0.0460  0.0603  78  LEU A CD1 
413   C CD2 . LEU A 78  ? 0.8639 0.3591 0.7406 0.0779  0.0400  0.0539  78  LEU A CD2 
414   N N   . ILE A 79  ? 0.9046 0.4103 0.7491 0.1947  0.0450  0.0359  79  ILE A N   
415   C CA  . ILE A 79  ? 0.9039 0.4264 0.7443 0.2216  0.0467  0.0272  79  ILE A CA  
416   C C   . ILE A 79  ? 0.9661 0.4246 0.7675 0.2339  0.0435  0.0170  79  ILE A C   
417   O O   . ILE A 79  ? 0.9684 0.4265 0.7678 0.2323  0.0433  0.0049  79  ILE A O   
418   C CB  . ILE A 79  ? 0.8919 0.4548 0.7398 0.2502  0.0496  0.0348  79  ILE A CB  
419   C CG1 . ILE A 79  ? 0.8336 0.4573 0.7181 0.2344  0.0517  0.0438  79  ILE A CG1 
420   C CG2 . ILE A 79  ? 0.8921 0.4831 0.7394 0.2751  0.0516  0.0260  79  ILE A CG2 
421   C CD1 . ILE A 79  ? 0.8312 0.4967 0.7235 0.2577  0.0537  0.0535  79  ILE A CD1 
422   N N   . LYS A 80  ? 1.0198 0.4206 0.7880 0.2446  0.0405  0.0218  80  LYS A N   
423   C CA  . LYS A 80  ? 1.0875 0.4161 0.8124 0.2532  0.0359  0.0121  80  LYS A CA  
424   C C   . LYS A 80  ? 1.0744 0.3888 0.8012 0.2229  0.0335  0.0016  80  LYS A C   
425   O O   . LYS A 80  ? 1.0908 0.3890 0.8020 0.2328  0.0324  -0.0116 80  LYS A O   
426   C CB  . LYS A 80  ? 1.1531 0.4138 0.8433 0.2525  0.0312  0.0209  80  LYS A CB  
427   C CG  . LYS A 80  ? 1.2495 0.4239 0.8914 0.2494  0.0243  0.0119  80  LYS A CG  
428   C CD  . LYS A 80  ? 1.3578 0.4855 0.9567 0.2927  0.0224  0.0074  80  LYS A CD  
429   C CE  . LYS A 80  ? 1.4351 0.5108 0.9989 0.2983  0.0180  -0.0096 80  LYS A CE  
430   N NZ  . LYS A 80  ? 1.4313 0.5632 1.0150 0.3195  0.0232  -0.0213 80  LYS A NZ  
431   N N   . GLN A 81  ? 1.0401 0.3654 0.7869 0.1871  0.0328  0.0078  81  GLN A N   
432   C CA  . GLN A 81  ? 1.0397 0.3485 0.7857 0.1554  0.0298  0.0005  81  GLN A CA  
433   C C   . GLN A 81  ? 0.9852 0.3435 0.7569 0.1541  0.0330  -0.0103 81  GLN A C   
434   O O   . GLN A 81  ? 1.0128 0.3442 0.7670 0.1514  0.0305  -0.0224 81  GLN A O   
435   C CB  . GLN A 81  ? 1.0253 0.3373 0.7848 0.1201  0.0285  0.0115  81  GLN A CB  
436   C CG  . GLN A 81  ? 1.1144 0.3691 0.8430 0.1183  0.0241  0.0223  81  GLN A CG  
437   C CD  . GLN A 81  ? 1.1409 0.4019 0.8818 0.0833  0.0227  0.0343  81  GLN A CD  
438   O OE1 . GLN A 81  ? 1.1487 0.4182 0.8989 0.0531  0.0213  0.0316  81  GLN A OE1 
439   N NE2 . GLN A 81  ? 1.1451 0.4023 0.8842 0.0878  0.0230  0.0481  81  GLN A NE2 
440   N N   . GLU A 82  ? 0.9116 0.3389 0.7214 0.1565  0.0380  -0.0061 82  GLU A N   
441   C CA  . GLU A 82  ? 0.8614 0.3375 0.6952 0.1562  0.0408  -0.0150 82  GLU A CA  
442   C C   . GLU A 82  ? 0.8865 0.3480 0.6992 0.1835  0.0407  -0.0266 82  GLU A C   
443   O O   . GLU A 82  ? 0.8832 0.3469 0.6958 0.1770  0.0402  -0.0377 82  GLU A O   
444   C CB  . GLU A 82  ? 0.7999 0.3457 0.6699 0.1608  0.0452  -0.0079 82  GLU A CB  
445   C CG  . GLU A 82  ? 0.7703 0.3513 0.6704 0.1307  0.0459  -0.0033 82  GLU A CG  
446   C CD  . GLU A 82  ? 0.7730 0.3725 0.6860 0.1137  0.0458  -0.0131 82  GLU A CD  
447   O OE1 . GLU A 82  ? 0.7771 0.3905 0.6895 0.1279  0.0468  -0.0219 82  GLU A OE1 
448   O OE2 . GLU A 82  ? 0.7601 0.3637 0.6841 0.0870  0.0449  -0.0114 82  GLU A OE2 
449   N N   . LEU A 83  ? 0.9155 0.3638 0.7095 0.2154  0.0413  -0.0239 83  LEU A N   
450   C CA  . LEU A 83  ? 0.9502 0.3865 0.7214 0.2469  0.0415  -0.0347 83  LEU A CA  
451   C C   . LEU A 83  ? 1.0050 0.3743 0.7407 0.2394  0.0364  -0.0468 83  LEU A C   
452   O O   . LEU A 83  ? 1.0098 0.3837 0.7401 0.2469  0.0365  -0.0593 83  LEU A O   
453   C CB  . LEU A 83  ? 0.9862 0.4133 0.7377 0.2845  0.0425  -0.0292 83  LEU A CB  
454   C CG  . LEU A 83  ? 0.9481 0.4478 0.7276 0.3047  0.0476  -0.0205 83  LEU A CG  
455   C CD1 . LEU A 83  ? 0.9912 0.5001 0.7514 0.3472  0.0493  -0.0269 83  LEU A CD1 
456   C CD2 . LEU A 83  ? 0.8798 0.4500 0.7033 0.2829  0.0505  -0.0186 83  LEU A CD2 
457   N N   . ASP A 84  ? 1.0467 0.3554 0.7582 0.2223  0.0315  -0.0426 84  ASP A N   
458   C CA  . ASP A 84  ? 1.1119 0.3501 0.7848 0.2118  0.0252  -0.0529 84  ASP A CA  
459   C C   . ASP A 84  ? 1.0734 0.3318 0.7637 0.1830  0.0248  -0.0615 84  ASP A C   
460   O O   . ASP A 84  ? 1.0960 0.3373 0.7688 0.1904  0.0231  -0.0752 84  ASP A O   
461   C CB  . ASP A 84  ? 1.1666 0.3429 0.8136 0.1933  0.0196  -0.0438 84  ASP A CB  
462   C CG  . ASP A 84  ? 1.2639 0.3969 0.8773 0.2264  0.0181  -0.0386 84  ASP A CG  
463   O OD1 . ASP A 84  ? 1.3245 0.4645 0.9263 0.2651  0.0204  -0.0455 84  ASP A OD1 
464   O OD2 . ASP A 84  ? 1.3330 0.4271 0.9311 0.2152  0.0147  -0.0274 84  ASP A OD2 
465   N N   . LYS A 85  ? 1.0153 0.3119 0.7397 0.1517  0.0264  -0.0533 85  LYS A N   
466   C CA  . LYS A 85  ? 0.9678 0.2996 0.7169 0.1258  0.0272  -0.0593 85  LYS A CA  
467   C C   . LYS A 85  ? 0.9468 0.3110 0.7029 0.1474  0.0302  -0.0712 85  LYS A C   
468   O O   . LYS A 85  ? 0.9703 0.3109 0.7088 0.1434  0.0274  -0.0838 85  LYS A O   
469   C CB  . LYS A 85  ? 0.8986 0.2905 0.6909 0.1060  0.0311  -0.0480 85  LYS A CB  
470   C CG  . LYS A 85  ? 0.8696 0.2825 0.6804 0.0724  0.0304  -0.0504 85  LYS A CG  
471   C CD  . LYS A 85  ? 0.8111 0.2884 0.6634 0.0624  0.0348  -0.0416 85  LYS A CD  
472   C CE  . LYS A 85  ? 0.7984 0.3286 0.6738 0.0826  0.0392  -0.0454 85  LYS A CE  
473   N NZ  . LYS A 85  ? 0.7666 0.3532 0.6784 0.0696  0.0422  -0.0376 85  LYS A NZ  
474   N N   . TYR A 86  ? 0.9012 0.3193 0.6811 0.1699  0.0355  -0.0667 86  TYR A N   
475   C CA  . TYR A 86  ? 0.8785 0.3360 0.6673 0.1911  0.0387  -0.0756 86  TYR A CA  
476   C C   . TYR A 86  ? 0.9361 0.3470 0.6844 0.2177  0.0362  -0.0886 86  TYR A C   
477   O O   . TYR A 86  ? 0.9388 0.3483 0.6810 0.2155  0.0352  -0.1010 86  TYR A O   
478   C CB  . TYR A 86  ? 0.8359 0.3542 0.6510 0.2114  0.0437  -0.0665 86  TYR A CB  
479   C CG  . TYR A 86  ? 0.8264 0.3859 0.6472 0.2346  0.0466  -0.0744 86  TYR A CG  
480   C CD1 . TYR A 86  ? 0.8097 0.3967 0.6460 0.2200  0.0470  -0.0827 86  TYR A CD1 
481   C CD2 . TYR A 86  ? 0.8414 0.4147 0.6512 0.2719  0.0488  -0.0732 86  TYR A CD2 
482   C CE1 . TYR A 86  ? 0.8023 0.4288 0.6435 0.2402  0.0495  -0.0893 86  TYR A CE1 
483   C CE2 . TYR A 86  ? 0.8316 0.4485 0.6467 0.2933  0.0515  -0.0796 86  TYR A CE2 
484   C CZ  . TYR A 86  ? 0.8201 0.4631 0.6510 0.2766  0.0518  -0.0875 86  TYR A CZ  
485   O OH  . TYR A 86  ? 0.8079 0.4956 0.6437 0.2969  0.0543  -0.0932 86  TYR A OH  
486   N N   . LYS A 87  ? 0.9829 0.3559 0.7023 0.2444  0.0350  -0.0858 87  LYS A N   
487   C CA  . LYS A 87  ? 1.0529 0.3797 0.7298 0.2756  0.0326  -0.0978 87  LYS A CA  
488   C C   . LYS A 87  ? 1.0908 0.3622 0.7401 0.2559  0.0268  -0.1107 87  LYS A C   
489   O O   . LYS A 87  ? 1.1233 0.3817 0.7517 0.2729  0.0257  -0.1247 87  LYS A O   
490   C CB  . LYS A 87  ? 1.1147 0.3879 0.7563 0.2999  0.0301  -0.0922 87  LYS A CB  
491   C CG  . LYS A 87  ? 1.1070 0.4313 0.7662 0.3300  0.0355  -0.0817 87  LYS A CG  
492   C CD  . LYS A 87  ? 1.2030 0.4698 0.8237 0.3555  0.0328  -0.0762 87  LYS A CD  
493   C CE  . LYS A 87  ? 1.1724 0.4900 0.8184 0.3693  0.0374  -0.0605 87  LYS A CE  
494   N NZ  . LYS A 87  ? 1.2418 0.5315 0.8522 0.4144  0.0371  -0.0595 87  LYS A NZ  
495   N N   . ASN A 88  ? 1.0883 0.3290 0.7370 0.2193  0.0227  -0.1056 88  ASN A N   
496   C CA  . ASN A 88  ? 1.1276 0.3108 0.7466 0.1965  0.0160  -0.1159 88  ASN A CA  
497   C C   . ASN A 88  ? 1.0769 0.3035 0.7186 0.1830  0.0179  -0.1261 88  ASN A C   
498   O O   . ASN A 88  ? 1.1118 0.3086 0.7259 0.1913  0.0147  -0.1409 88  ASN A O   
499   C CB  . ASN A 88  ? 1.1427 0.2928 0.7587 0.1590  0.0114  -0.1054 88  ASN A CB  
500   C CG  . ASN A 88  ? 1.1759 0.2924 0.7763 0.1247  0.0053  -0.1132 88  ASN A CG  
501   O OD1 . ASN A 88  ? 1.2608 0.3051 0.8138 0.1254  -0.0020 -0.1223 88  ASN A OD1 
502   N ND2 . ASN A 88  ? 1.1360 0.3049 0.7749 0.0942  0.0078  -0.1097 88  ASN A ND2 
503   N N   . ALA A 89  ? 0.9908 0.2869 0.6809 0.1641  0.0228  -0.1183 89  ALA A N   
504   C CA  . ALA A 89  ? 0.9377 0.2819 0.6534 0.1518  0.0251  -0.1257 89  ALA A CA  
505   C C   . ALA A 89  ? 0.9522 0.2988 0.6507 0.1858  0.0263  -0.1387 89  ALA A C   
506   O O   . ALA A 89  ? 0.9667 0.3033 0.6529 0.1814  0.0241  -0.1518 89  ALA A O   
507   C CB  . ALA A 89  ? 0.8534 0.2765 0.6209 0.1417  0.0311  -0.1147 89  ALA A CB  
508   N N   . VAL A 90  ? 0.9476 0.3057 0.6422 0.2206  0.0295  -0.1349 90  VAL A N   
509   C CA  . VAL A 90  ? 0.9525 0.3304 0.6376 0.2559  0.0320  -0.1445 90  VAL A CA  
510   C C   . VAL A 90  ? 1.0324 0.3370 0.6650 0.2697  0.0263  -0.1600 90  VAL A C   
511   O O   . VAL A 90  ? 1.0395 0.3538 0.6641 0.2806  0.0264  -0.1732 90  VAL A O   
512   C CB  . VAL A 90  ? 0.9378 0.3486 0.6311 0.2885  0.0366  -0.1349 90  VAL A CB  
513   C CG1 . VAL A 90  ? 0.9667 0.3878 0.6396 0.3305  0.0384  -0.1450 90  VAL A CG1 
514   C CG2 . VAL A 90  ? 0.8536 0.3440 0.5988 0.2741  0.0418  -0.1222 90  VAL A CG2 
515   N N   . THR A 91  ? 1.0964 0.3260 0.6918 0.2678  0.0206  -0.1585 91  THR A N   
516   C CA  . THR A 91  ? 1.1861 0.3345 0.7253 0.2785  0.0135  -0.1729 91  THR A CA  
517   C C   . THR A 91  ? 1.1919 0.3289 0.7298 0.2445  0.0094  -0.1831 91  THR A C   
518   O O   . THR A 91  ? 1.2295 0.3457 0.7410 0.2576  0.0070  -0.1988 91  THR A O   
519   C CB  . THR A 91  ? 1.2485 0.3152 0.7479 0.2745  0.0068  -0.1677 91  THR A CB  
520   O OG1 . THR A 91  ? 1.2282 0.3195 0.7441 0.2913  0.0112  -0.1528 91  THR A OG1 
521   C CG2 . THR A 91  ? 1.3467 0.3342 0.7834 0.3036  0.0005  -0.1823 91  THR A CG2 
522   N N   . GLU A 92  ? 1.1557 0.3101 0.7223 0.2021  0.0088  -0.1740 92  GLU A N   
523   C CA  . GLU A 92  ? 1.1555 0.3080 0.7251 0.1675  0.0053  -0.1818 92  GLU A CA  
524   C C   . GLU A 92  ? 1.1214 0.3231 0.7065 0.1798  0.0091  -0.1936 92  GLU A C   
525   O O   . GLU A 92  ? 1.1572 0.3258 0.7147 0.1749  0.0043  -0.2081 92  GLU A O   
526   C CB  . GLU A 92  ? 1.1039 0.2919 0.7121 0.1262  0.0064  -0.1686 92  GLU A CB  
527   C CG  . GLU A 92  ? 1.1870 0.3099 0.7673 0.0951  -0.0014 -0.1635 92  GLU A CG  
528   C CD  . GLU A 92  ? 1.3162 0.3648 0.8452 0.0839  -0.0109 -0.1781 92  GLU A CD  
529   O OE1 . GLU A 92  ? 1.3303 0.3928 0.8587 0.0813  -0.0114 -0.1912 92  GLU A OE1 
530   O OE2 . GLU A 92  ? 1.3951 0.3682 0.8820 0.0766  -0.0185 -0.1760 92  GLU A OE2 
531   N N   . LEU A 93  ? 1.0537 0.3334 0.6811 0.1948  0.0172  -0.1870 93  LEU A N   
532   C CA  . LEU A 93  ? 1.0233 0.3576 0.6689 0.2068  0.0213  -0.1957 93  LEU A CA  
533   C C   . LEU A 93  ? 1.0899 0.3927 0.6949 0.2462  0.0199  -0.2100 93  LEU A C   
534   O O   . LEU A 93  ? 1.1091 0.4117 0.7021 0.2488  0.0186  -0.2240 93  LEU A O   
535   C CB  . LEU A 93  ? 0.9405 0.3607 0.6357 0.2141  0.0292  -0.1839 93  LEU A CB  
536   C CG  . LEU A 93  ? 0.8678 0.3334 0.6070 0.1786  0.0312  -0.1719 93  LEU A CG  
537   C CD1 . LEU A 93  ? 0.8125 0.3458 0.5891 0.1909  0.0375  -0.1595 93  LEU A CD1 
538   C CD2 . LEU A 93  ? 0.8328 0.3237 0.5873 0.1542  0.0306  -0.1789 93  LEU A CD2 
539   N N   . GLN A 94  ? 1.1306 0.4069 0.7129 0.2783  0.0203  -0.2068 94  GLN A N   
540   C CA  . GLN A 94  ? 1.2007 0.4463 0.7414 0.3200  0.0190  -0.2202 94  GLN A CA  
541   C C   . GLN A 94  ? 1.2682 0.4440 0.7642 0.3099  0.0111  -0.2374 94  GLN A C   
542   O O   . GLN A 94  ? 1.3006 0.4742 0.7747 0.3345  0.0109  -0.2520 94  GLN A O   
543   C CB  . GLN A 94  ? 1.2527 0.4549 0.7634 0.3501  0.0179  -0.2149 94  GLN A CB  
544   C CG  . GLN A 94  ? 1.2486 0.5105 0.7744 0.3917  0.0251  -0.2099 94  GLN A CG  
545   C CD  . GLN A 94  ? 1.3080 0.5493 0.8256 0.4073  0.0254  -0.1972 94  GLN A CD  
546   O OE1 . GLN A 94  ? 1.4009 0.5585 0.8709 0.4165  0.0193  -0.2003 94  GLN A OE1 
547   N NE2 . GLN A 94  ? 1.2610 0.5767 0.8235 0.4089  0.0320  -0.1821 94  GLN A NE2 
548   N N   . LEU A 95  ? 1.2956 0.4169 0.7780 0.2724  0.0045  -0.2353 95  LEU A N   
549   C CA  . LEU A 95  ? 1.3805 0.4238 0.8129 0.2612  -0.0048 -0.2504 95  LEU A CA  
550   C C   . LEU A 95  ? 1.3679 0.4464 0.8161 0.2420  -0.0045 -0.2610 95  LEU A C   
551   O O   . LEU A 95  ? 1.4329 0.4581 0.8408 0.2375  -0.0115 -0.2763 95  LEU A O   
552   C CB  . LEU A 95  ? 1.4132 0.3894 0.8246 0.2256  -0.0126 -0.2430 95  LEU A CB  
553   C CG  . LEU A 95  ? 1.4364 0.3692 0.8248 0.2483  -0.0136 -0.2333 95  LEU A CG  
554   C CD1 . LEU A 95  ? 1.4225 0.3221 0.8124 0.2090  -0.0182 -0.2192 95  LEU A CD1 
555   C CD2 . LEU A 95  ? 1.5185 0.3667 0.8385 0.2861  -0.0200 -0.2471 95  LEU A CD2 
556   N N   . LEU A 96  ? 1.2979 0.4660 0.8030 0.2325  0.0033  -0.2531 96  LEU A N   
557   C CA  . LEU A 96  ? 1.2841 0.4913 0.8084 0.2132  0.0040  -0.2611 96  LEU A CA  
558   C C   . LEU A 96  ? 1.3246 0.5442 0.8310 0.2475  0.0055  -0.2768 96  LEU A C   
559   O O   . LEU A 96  ? 1.3267 0.5567 0.8324 0.2342  0.0038  -0.2877 96  LEU A O   
560   C CB  . LEU A 96  ? 1.1852 0.4799 0.7728 0.1921  0.0111  -0.2471 96  LEU A CB  
561   C CG  . LEU A 96  ? 1.1662 0.4458 0.7672 0.1496  0.0080  -0.2356 96  LEU A CG  
562   C CD1 . LEU A 96  ? 1.0783 0.4350 0.7331 0.1251  0.0131  -0.2267 96  LEU A CD1 
563   C CD2 . LEU A 96  ? 1.2321 0.4378 0.7903 0.1238  -0.0018 -0.2460 96  LEU A CD2 
564   N N   . MET A 97  ? 1.3733 0.5921 0.8633 0.2922  0.0085  -0.2782 97  MET A N   
565   C CA  . MET A 97  ? 1.4059 0.6625 0.8911 0.3287  0.0124  -0.2895 97  MET A CA  
566   C C   . MET A 97  ? 1.5007 0.6948 0.9304 0.3433  0.0057  -0.3113 97  MET A C   
567   O O   . MET A 97  ? 1.4983 0.7309 0.9310 0.3578  0.0082  -0.3220 97  MET A O   
568   C CB  . MET A 97  ? 1.3973 0.6904 0.8901 0.3712  0.0188  -0.2814 97  MET A CB  
569   C CG  . MET A 97  ? 1.3570 0.7170 0.9065 0.3536  0.0250  -0.2603 97  MET A CG  
570   S SD  . MET A 97  ? 1.3325 0.8024 0.9502 0.3283  0.0320  -0.2511 97  MET A SD  
571   C CE  . MET A 97  ? 1.2999 0.7558 0.9061 0.3050  0.0277  -0.2681 97  MET A CE  
572   N N   . GLN A 98  ? 1.5983 0.6945 0.9757 0.3378  -0.0034 -0.3176 98  GLN A N   
573   C CA  . GLN A 98  ? 1.7015 0.7205 1.0155 0.3515  -0.0118 -0.3390 98  GLN A CA  
574   C C   . GLN A 98  ? 1.7488 0.6896 1.0324 0.3051  -0.0228 -0.3436 98  GLN A C   
575   O O   . GLN A 98  ? 1.7036 0.6562 1.0178 0.2616  -0.0235 -0.3304 98  GLN A O   
576   C CB  . GLN A 98  ? 1.7856 0.7477 1.0462 0.4044  -0.0137 -0.3459 98  GLN A CB  
577   C CG  . GLN A 98  ? 1.7597 0.7906 1.0492 0.4473  -0.0035 -0.3341 98  GLN A CG  
578   C CD  . GLN A 98  ? 1.7402 0.7822 1.0595 0.4342  -0.0007 -0.3123 98  GLN A CD  
579   O OE1 . GLN A 98  ? 1.6655 0.7380 1.0279 0.3906  0.0007  -0.2995 98  GLN A OE1 
580   N NE2 . GLN A 98  ? 1.7759 0.7961 1.0712 0.4747  0.0004  -0.3083 98  GLN A NE2 
581   N N   . SER A 137 ? 0.8876 2.3159 0.6402 0.4746  0.0194  1.0047  146 SER A N   
582   C CA  . SER A 137 ? 0.8602 2.3716 0.6209 0.4693  0.0155  0.9962  146 SER A CA  
583   C C   . SER A 137 ? 0.8766 2.4301 0.6283 0.4721  0.0154  1.0189  146 SER A C   
584   O O   . SER A 137 ? 0.9087 2.4253 0.6483 0.4764  0.0184  1.0411  146 SER A O   
585   C CB  . SER A 137 ? 0.8195 2.3428 0.5919 0.4396  0.0132  0.9634  146 SER A CB  
586   O OG  . SER A 137 ? 0.8131 2.3671 0.5825 0.4228  0.0127  0.9634  146 SER A OG  
587   N N   . ALA A 138 ? 0.8564 2.4860 0.6129 0.4682  0.0114  1.0134  147 ALA A N   
588   C CA  . ALA A 138 ? 0.8708 2.5486 0.6191 0.4725  0.0110  1.0347  147 ALA A CA  
589   C C   . ALA A 138 ? 0.8439 2.5975 0.5964 0.4567  0.0064  1.0211  147 ALA A C   
590   O O   . ALA A 138 ? 0.8555 2.6545 0.6017 0.4626  0.0057  1.0388  147 ALA A O   
591   C CB  . ALA A 138 ? 0.9042 2.5923 0.6434 0.5046  0.0117  1.0643  147 ALA A CB  
592   N N   . ILE A 139 ? 0.8111 2.5763 0.5722 0.4370  0.0027  0.9898  148 ILE A N   
593   C CA  . ILE A 139 ? 0.7890 2.6048 0.5493 0.4154  -0.0019 0.9711  148 ILE A CA  
594   C C   . ILE A 139 ? 0.7905 2.6853 0.5463 0.4200  -0.0064 0.9805  148 ILE A C   
595   O O   . ILE A 139 ? 0.8118 2.7275 0.5611 0.4328  -0.0041 1.0068  148 ILE A O   
596   C CB  . ILE A 139 ? 0.7883 2.5786 0.5441 0.3980  0.0012  0.9659  148 ILE A CB  
597   C CG1 . ILE A 139 ? 0.7626 2.5833 0.5171 0.3753  -0.0040 0.9353  148 ILE A CG1 
598   C CG2 . ILE A 139 ? 0.8130 2.6229 0.5599 0.4064  0.0043  0.9955  148 ILE A CG2 
599   C CD1 . ILE A 139 ? 0.7531 2.5267 0.5080 0.3589  -0.0013 0.9175  148 ILE A CD1 
600   N N   . ALA A 140 ? 0.7687 2.7060 0.5266 0.4068  -0.0134 0.9578  149 ALA A N   
601   C CA  . ALA A 140 ? 0.7685 2.7834 0.5226 0.4093  -0.0192 0.9636  149 ALA A CA  
602   C C   . ALA A 140 ? 0.7847 2.8268 0.5304 0.4143  -0.0169 0.9840  149 ALA A C   
603   O O   . ALA A 140 ? 0.8077 2.8427 0.5517 0.4350  -0.0120 1.0132  149 ALA A O   
604   C CB  . ALA A 140 ? 0.7467 2.7926 0.4978 0.3842  -0.0277 0.9323  149 ALA A CB  
605   N N   . SER A 141 ? 0.7745 2.8430 0.5130 0.3947  -0.0206 0.9670  150 SER A N   
606   C CA  . SER A 141 ? 0.7852 2.8983 0.5143 0.3949  -0.0207 0.9803  150 SER A CA  
607   C C   . SER A 141 ? 0.7698 2.9281 0.4919 0.3756  -0.0296 0.9535  150 SER A C   
608   O O   . SER A 141 ? 0.7561 2.9115 0.4811 0.3661  -0.0351 0.9330  150 SER A O   
609   C CB  . SER A 141 ? 0.8033 2.9632 0.5319 0.4172  -0.0202 1.0116  150 SER A CB  
610   O OG  . SER A 141 ? 0.7950 3.0008 0.5271 0.4201  -0.0265 1.0063  150 SER A OG  
611   N N   . GLY A 142 ? 0.7751 2.9772 0.4860 0.3700  -0.0318 0.9549  151 GLY A N   
612   C CA  . GLY A 142 ? 0.7670 3.0132 0.4663 0.3520  -0.0415 0.9303  151 GLY A CA  
613   C C   . GLY A 142 ? 0.7512 2.9555 0.4515 0.3353  -0.0458 0.8984  151 GLY A C   
614   O O   . GLY A 142 ? 0.7459 2.9037 0.4429 0.3254  -0.0436 0.8804  151 GLY A O   
615   N N   . VAL A 143 ? 0.7444 2.9652 0.4491 0.3322  -0.0519 0.8921  152 VAL A N   
616   C CA  . VAL A 143 ? 0.7315 2.9157 0.4340 0.3131  -0.0573 0.8606  152 VAL A CA  
617   C C   . VAL A 143 ? 0.7214 2.8863 0.4374 0.3151  -0.0582 0.8584  152 VAL A C   
618   O O   . VAL A 143 ? 0.7245 2.9113 0.4520 0.3332  -0.0554 0.8815  152 VAL A O   
619   C CB  . VAL A 143 ? 0.7333 2.9440 0.4147 0.2897  -0.0686 0.8327  152 VAL A CB  
620   C CG1 . VAL A 143 ? 0.7269 2.8762 0.4003 0.2738  -0.0700 0.8013  152 VAL A CG1 
621   C CG2 . VAL A 143 ? 0.7459 2.9987 0.4143 0.2925  -0.0686 0.8413  152 VAL A CG2 
622   N N   . ALA A 144 ? 0.7112 2.8391 0.4228 0.2956  -0.0632 0.8287  153 ALA A N   
623   C CA  . ALA A 144 ? 0.7002 2.7707 0.4239 0.2961  -0.0596 0.8205  153 ALA A CA  
624   C C   . ALA A 144 ? 0.6987 2.7179 0.4148 0.2873  -0.0565 0.8030  153 ALA A C   
625   O O   . ALA A 144 ? 0.6924 2.6807 0.4004 0.2695  -0.0616 0.7748  153 ALA A O   
626   C CB  . ALA A 144 ? 0.7035 2.7572 0.4441 0.3219  -0.0497 0.8487  153 ALA A CB  
627   N N   . VAL A 145 ? 0.7066 2.7195 0.4242 0.3003  -0.0482 0.8211  154 VAL A N   
628   C CA  . VAL A 145 ? 0.7074 2.6848 0.4178 0.2948  -0.0440 0.8102  154 VAL A CA  
629   C C   . VAL A 145 ? 0.6960 2.6120 0.4066 0.2824  -0.0441 0.7831  154 VAL A C   
630   O O   . VAL A 145 ? 0.6874 2.5678 0.4106 0.2842  -0.0423 0.7817  154 VAL A O   
631   C CB  . VAL A 145 ? 0.7169 2.7406 0.4076 0.2871  -0.0492 0.8027  154 VAL A CB  
632   C CG1 . VAL A 145 ? 0.7158 2.7114 0.3898 0.2716  -0.0529 0.7708  154 VAL A CG1 
633   C CG2 . VAL A 145 ? 0.7283 2.7803 0.4209 0.3021  -0.0421 0.8319  154 VAL A CG2 
634   N N   . SER A 146 ? 0.6975 2.6028 0.3928 0.2711  -0.0465 0.7614  155 SER A N   
635   C CA  . SER A 146 ? 0.6894 2.5391 0.3820 0.2607  -0.0466 0.7358  155 SER A CA  
636   C C   . SER A 146 ? 0.6783 2.4976 0.3801 0.2544  -0.0499 0.7247  155 SER A C   
637   O O   . SER A 146 ? 0.6694 2.4362 0.3810 0.2547  -0.0449 0.7188  155 SER A O   
638   C CB  . SER A 146 ? 0.6970 2.5529 0.3644 0.2479  -0.0540 0.7078  155 SER A CB  
639   O OG  . SER A 146 ? 0.7043 2.5944 0.3564 0.2364  -0.0657 0.6955  155 SER A OG  
640   N N   . LYS A 147 ? 0.6791 2.5329 0.3778 0.2481  -0.0583 0.7223  156 LYS A N   
641   C CA  . LYS A 147 ? 0.6689 2.4982 0.3754 0.2403  -0.0621 0.7111  156 LYS A CA  
642   C C   . LYS A 147 ? 0.6604 2.4589 0.3902 0.2566  -0.0524 0.7302  156 LYS A C   
643   O O   . LYS A 147 ? 0.6509 2.4000 0.3876 0.2527  -0.0505 0.7179  156 LYS A O   
644   C CB  . LYS A 147 ? 0.6722 2.5523 0.3728 0.2306  -0.0727 0.7098  156 LYS A CB  
645   C CG  . LYS A 147 ? 0.6796 2.5589 0.3558 0.2050  -0.0862 0.6787  156 LYS A CG  
646   C CD  . LYS A 147 ? 0.6721 2.5336 0.3519 0.1904  -0.0928 0.6653  156 LYS A CD  
647   C CE  . LYS A 147 ? 0.6870 2.5530 0.3377 0.1629  -0.1082 0.6377  156 LYS A CE  
648   N NZ  . LYS A 147 ? 0.6845 2.4968 0.3290 0.1460  -0.1136 0.6130  156 LYS A NZ  
649   N N   . VAL A 148 ? 0.6666 2.4918 0.4065 0.2755  -0.0464 0.7601  157 VAL A N   
650   C CA  . VAL A 148 ? 0.6653 2.4580 0.4227 0.2927  -0.0380 0.7787  157 VAL A CA  
651   C C   . VAL A 148 ? 0.6602 2.3875 0.4206 0.2891  -0.0320 0.7679  157 VAL A C   
652   O O   . VAL A 148 ? 0.6519 2.3362 0.4216 0.2887  -0.0300 0.7606  157 VAL A O   
653   C CB  . VAL A 148 ? 0.6799 2.4945 0.4415 0.3139  -0.0313 0.8118  157 VAL A CB  
654   C CG1 . VAL A 148 ? 0.6848 2.4546 0.4595 0.3320  -0.0233 0.8293  157 VAL A CG1 
655   C CG2 . VAL A 148 ? 0.6859 2.5716 0.4444 0.3195  -0.0368 0.8249  157 VAL A CG2 
656   N N   . LEU A 149 ? 0.6652 2.3891 0.4171 0.2857  -0.0293 0.7664  158 LEU A N   
657   C CA  . LEU A 149 ? 0.6631 2.3340 0.4183 0.2844  -0.0224 0.7627  158 LEU A CA  
658   C C   . LEU A 149 ? 0.6511 2.2870 0.4006 0.2680  -0.0263 0.7299  158 LEU A C   
659   O O   . LEU A 149 ? 0.6466 2.2353 0.4010 0.2663  -0.0209 0.7244  158 LEU A O   
660   C CB  . LEU A 149 ? 0.6744 2.3620 0.4232 0.2882  -0.0177 0.7770  158 LEU A CB  
661   C CG  . LEU A 149 ? 0.6892 2.4141 0.4409 0.3043  -0.0150 0.8098  158 LEU A CG  
662   C CD1 . LEU A 149 ? 0.6974 2.4697 0.4370 0.3026  -0.0162 0.8148  158 LEU A CD1 
663   C CD2 . LEU A 149 ? 0.7010 2.3865 0.4626 0.3177  -0.0064 0.8356  158 LEU A CD2 
664   N N   . HIS A 150 ? 0.6480 2.3053 0.3861 0.2552  -0.0361 0.7087  159 HIS A N   
665   C CA  . HIS A 150 ? 0.6394 2.2571 0.3717 0.2406  -0.0408 0.6788  159 HIS A CA  
666   C C   . HIS A 150 ? 0.6288 2.2108 0.3785 0.2438  -0.0379 0.6815  159 HIS A C   
667   O O   . HIS A 150 ? 0.6213 2.1526 0.3758 0.2407  -0.0342 0.6701  159 HIS A O   
668   C CB  . HIS A 150 ? 0.6439 2.2867 0.3569 0.2243  -0.0534 0.6563  159 HIS A CB  
669   C CG  . HIS A 150 ? 0.6446 2.2478 0.3414 0.2104  -0.0582 0.6249  159 HIS A CG  
670   N ND1 . HIS A 150 ? 0.6574 2.2682 0.3307 0.2054  -0.0624 0.6090  159 HIS A ND1 
671   C CD2 . HIS A 150 ? 0.6361 2.1898 0.3356 0.2027  -0.0590 0.6071  159 HIS A CD2 
672   C CE1 . HIS A 150 ? 0.6646 2.2314 0.3256 0.1961  -0.0659 0.5825  159 HIS A CE1 
673   N NE2 . HIS A 150 ? 0.6463 2.1782 0.3235 0.1935  -0.0639 0.5810  159 HIS A NE2 
674   N N   . LEU A 151 ? 0.6290 2.2405 0.3875 0.2512  -0.0394 0.6969  160 LEU A N   
675   C CA  . LEU A 151 ? 0.6239 2.2094 0.3978 0.2572  -0.0369 0.7010  160 LEU A CA  
676   C C   . LEU A 151 ? 0.6344 2.1768 0.4211 0.2726  -0.0261 0.7182  160 LEU A C   
677   O O   . LEU A 151 ? 0.6332 2.1272 0.4277 0.2710  -0.0232 0.7092  160 LEU A O   
678   C CB  . LEU A 151 ? 0.6289 2.2637 0.4077 0.2637  -0.0411 0.7145  160 LEU A CB  
679   C CG  . LEU A 151 ? 0.6361 2.2878 0.4060 0.2425  -0.0524 0.6912  160 LEU A CG  
680   C CD1 . LEU A 151 ? 0.6481 2.3523 0.3997 0.2310  -0.0612 0.6866  160 LEU A CD1 
681   C CD2 . LEU A 151 ? 0.6262 2.2941 0.4089 0.2476  -0.0540 0.6985  160 LEU A CD2 
682   N N   . GLU A 152 ? 0.6558 2.2145 0.4430 0.2866  -0.0206 0.7430  161 GLU A N   
683   C CA  . GLU A 152 ? 0.6787 2.1940 0.4714 0.2959  -0.0115 0.7579  161 GLU A CA  
684   C C   . GLU A 152 ? 0.6801 2.1462 0.4725 0.2821  -0.0099 0.7359  161 GLU A C   
685   O O   . GLU A 152 ? 0.6797 2.0966 0.4805 0.2853  -0.0050 0.7376  161 GLU A O   
686   C CB  . GLU A 152 ? 0.6956 2.2393 0.4815 0.3015  -0.0086 0.7776  161 GLU A CB  
687   C CG  . GLU A 152 ? 0.7091 2.2130 0.4962 0.3040  -0.0005 0.7909  161 GLU A CG  
688   C CD  . GLU A 152 ? 0.7286 2.2119 0.5203 0.3224  0.0049  0.8207  161 GLU A CD  
689   O OE1 . GLU A 152 ? 0.7444 2.2517 0.5309 0.3316  0.0069  0.8449  161 GLU A OE1 
690   O OE2 . GLU A 152 ? 0.7317 2.1736 0.5302 0.3284  0.0066  0.8197  161 GLU A OE2 
691   N N   . GLY A 153 ? 0.6887 2.1677 0.4697 0.2678  -0.0144 0.7149  162 GLY A N   
692   C CA  . GLY A 153 ? 0.7027 2.1400 0.4815 0.2572  -0.0126 0.6952  162 GLY A CA  
693   C C   . GLY A 153 ? 0.7036 2.1057 0.4865 0.2489  -0.0159 0.6734  162 GLY A C   
694   O O   . GLY A 153 ? 0.6994 2.0539 0.4889 0.2468  -0.0114 0.6671  162 GLY A O   
695   N N   . GLU A 154 ? 0.7134 2.1410 0.4920 0.2430  -0.0242 0.6627  163 GLU A N   
696   C CA  . GLU A 154 ? 0.7214 2.1222 0.5024 0.2332  -0.0287 0.6427  163 GLU A CA  
697   C C   . GLU A 154 ? 0.7151 2.0850 0.5141 0.2443  -0.0226 0.6555  163 GLU A C   
698   O O   . GLU A 154 ? 0.7100 2.0316 0.5148 0.2407  -0.0197 0.6444  163 GLU A O   
699   C CB  . GLU A 154 ? 0.7291 2.1698 0.5002 0.2226  -0.0397 0.6322  163 GLU A CB  
700   C CG  . GLU A 154 ? 0.7738 2.1899 0.5308 0.2027  -0.0483 0.6002  163 GLU A CG  
701   C CD  . GLU A 154 ? 0.8462 2.2626 0.5804 0.1945  -0.0522 0.5828  163 GLU A CD  
702   O OE1 . GLU A 154 ? 0.8658 2.3260 0.5880 0.1947  -0.0561 0.5882  163 GLU A OE1 
703   O OE2 . GLU A 154 ? 0.8587 2.2330 0.5861 0.1892  -0.0516 0.5637  163 GLU A OE2 
704   N N   . VAL A 155 ? 0.7220 2.1195 0.5282 0.2593  -0.0207 0.6789  164 VAL A N   
705   C CA  . VAL A 155 ? 0.7277 2.0972 0.5472 0.2746  -0.0147 0.6941  164 VAL A CA  
706   C C   . VAL A 155 ? 0.7369 2.0493 0.5602 0.2764  -0.0070 0.6960  164 VAL A C   
707   O O   . VAL A 155 ? 0.7326 2.0013 0.5633 0.2763  -0.0046 0.6887  164 VAL A O   
708   C CB  . VAL A 155 ? 0.7416 2.1450 0.5633 0.2950  -0.0120 0.7235  164 VAL A CB  
709   C CG1 . VAL A 155 ? 0.7522 2.1113 0.5807 0.3139  -0.0037 0.7433  164 VAL A CG1 
710   C CG2 . VAL A 155 ? 0.7361 2.1889 0.5594 0.2972  -0.0185 0.7240  164 VAL A CG2 
711   N N   . ASN A 156 ? 0.7530 2.0692 0.5705 0.2767  -0.0034 0.7059  165 ASN A N   
712   C CA  . ASN A 156 ? 0.7664 2.0367 0.5864 0.2776  0.0038  0.7133  165 ASN A CA  
713   C C   . ASN A 156 ? 0.7471 1.9765 0.5684 0.2634  0.0043  0.6895  165 ASN A C   
714   O O   . ASN A 156 ? 0.7481 1.9310 0.5750 0.2643  0.0096  0.6933  165 ASN A O   
715   C CB  . ASN A 156 ? 0.7872 2.0804 0.6000 0.2790  0.0066  0.7298  165 ASN A CB  
716   C CG  . ASN A 156 ? 0.8317 2.1031 0.6462 0.2925  0.0127  0.7591  165 ASN A CG  
717   O OD1 . ASN A 156 ? 0.8584 2.1608 0.6688 0.3038  0.0131  0.7811  165 ASN A OD1 
718   N ND2 . ASN A 156 ? 0.8594 2.0742 0.6783 0.2918  0.0170  0.7600  165 ASN A ND2 
719   N N   . LYS A 157 ? 0.7310 1.9770 0.5451 0.2504  -0.0018 0.6652  166 LYS A N   
720   C CA  . LYS A 157 ? 0.7184 1.9275 0.5324 0.2385  -0.0028 0.6403  166 LYS A CA  
721   C C   . LYS A 157 ? 0.7063 1.8848 0.5314 0.2413  -0.0027 0.6372  166 LYS A C   
722   O O   . LYS A 157 ? 0.7071 1.8408 0.5397 0.2423  0.0024  0.6379  166 LYS A O   
723   C CB  . LYS A 157 ? 0.7153 1.9458 0.5150 0.2258  -0.0111 0.6150  166 LYS A CB  
724   C CG  . LYS A 157 ? 0.7360 1.9685 0.5240 0.2209  -0.0097 0.6059  166 LYS A CG  
725   C CD  . LYS A 157 ? 0.7710 2.0420 0.5394 0.2150  -0.0180 0.5916  166 LYS A CD  
726   C CE  . LYS A 157 ? 0.7926 2.0807 0.5495 0.2167  -0.0152 0.5915  166 LYS A CE  
727   N NZ  . LYS A 157 ? 0.8067 2.1472 0.5508 0.2190  -0.0197 0.5977  166 LYS A NZ  
728   N N   . ILE A 158 ? 0.6987 1.9042 0.5245 0.2426  -0.0084 0.6353  167 ILE A N   
729   C CA  . ILE A 158 ? 0.6888 1.8730 0.5243 0.2450  -0.0090 0.6308  167 ILE A CA  
730   C C   . ILE A 158 ? 0.6991 1.8433 0.5448 0.2592  -0.0010 0.6474  167 ILE A C   
731   O O   . ILE A 158 ? 0.6917 1.7937 0.5434 0.2563  0.0009  0.6372  167 ILE A O   
732   C CB  . ILE A 158 ? 0.6859 1.9166 0.5212 0.2468  -0.0156 0.6334  167 ILE A CB  
733   C CG1 . ILE A 158 ? 0.6775 1.9267 0.5008 0.2267  -0.0253 0.6091  167 ILE A CG1 
734   C CG2 . ILE A 158 ? 0.6730 1.8896 0.5200 0.2555  -0.0144 0.6367  167 ILE A CG2 
735   C CD1 . ILE A 158 ? 0.6906 1.9890 0.5111 0.2229  -0.0332 0.6103  167 ILE A CD1 
736   N N   . LYS A 159 ? 0.7200 1.8746 0.5653 0.2742  0.0032  0.6729  168 LYS A N   
737   C CA  . LYS A 159 ? 0.7419 1.8524 0.5913 0.2872  0.0098  0.6892  168 LYS A CA  
738   C C   . LYS A 159 ? 0.7369 1.7966 0.5879 0.2752  0.0134  0.6773  168 LYS A C   
739   O O   . LYS A 159 ? 0.7330 1.7521 0.5897 0.2755  0.0150  0.6696  168 LYS A O   
740   C CB  . LYS A 159 ? 0.7720 1.8942 0.6158 0.3010  0.0134  0.7175  168 LYS A CB  
741   C CG  . LYS A 159 ? 0.8217 1.8874 0.6639 0.3098  0.0196  0.7339  168 LYS A CG  
742   C CD  . LYS A 159 ? 0.8908 1.9610 0.7238 0.3179  0.0227  0.7616  168 LYS A CD  
743   C CE  . LYS A 159 ? 0.9246 1.9313 0.7524 0.3181  0.0275  0.7742  168 LYS A CE  
744   N NZ  . LYS A 159 ? 0.9686 1.9696 0.7846 0.3326  0.0295  0.8052  168 LYS A NZ  
745   N N   . SER A 160 ? 0.7384 1.8038 0.5839 0.2647  0.0145  0.6755  169 SER A N   
746   C CA  . SER A 160 ? 0.7392 1.7637 0.5859 0.2533  0.0181  0.6662  169 SER A CA  
747   C C   . SER A 160 ? 0.7167 1.7164 0.5682 0.2436  0.0157  0.6396  169 SER A C   
748   O O   . SER A 160 ? 0.7182 1.6728 0.5746 0.2411  0.0192  0.6362  169 SER A O   
749   C CB  . SER A 160 ? 0.7398 1.7870 0.5794 0.2441  0.0189  0.6658  169 SER A CB  
750   O OG  . SER A 160 ? 0.7743 1.8401 0.6096 0.2524  0.0216  0.6926  169 SER A OG  
751   N N   . ALA A 161 ? 0.7002 1.7291 0.5490 0.2377  0.0092  0.6218  170 ALA A N   
752   C CA  . ALA A 161 ? 0.6824 1.6908 0.5331 0.2272  0.0055  0.5964  170 ALA A CA  
753   C C   . ALA A 161 ? 0.6792 1.6588 0.5401 0.2341  0.0069  0.5981  170 ALA A C   
754   O O   . ALA A 161 ? 0.6685 1.6102 0.5340 0.2278  0.0079  0.5839  170 ALA A O   
755   C CB  . ALA A 161 ? 0.6750 1.7202 0.5167 0.2187  -0.0031 0.5802  170 ALA A CB  
756   N N   . LEU A 162 ? 0.6874 1.6869 0.5512 0.2484  0.0070  0.6156  171 LEU A N   
757   C CA  . LEU A 162 ? 0.6891 1.6658 0.5608 0.2590  0.0086  0.6190  171 LEU A CA  
758   C C   . LEU A 162 ? 0.7045 1.6262 0.5786 0.2650  0.0155  0.6279  171 LEU A C   
759   O O   . LEU A 162 ? 0.7019 1.5874 0.5814 0.2639  0.0166  0.6179  171 LEU A O   
760   C CB  . LEU A 162 ? 0.6981 1.7118 0.5704 0.2763  0.0075  0.6371  171 LEU A CB  
761   C CG  . LEU A 162 ? 0.6988 1.6934 0.5779 0.2904  0.0090  0.6403  171 LEU A CG  
762   C CD1 . LEU A 162 ? 0.6834 1.6923 0.5675 0.2784  0.0034  0.6196  171 LEU A CD1 
763   C CD2 . LEU A 162 ? 0.7205 1.7453 0.5982 0.3131  0.0098  0.6626  171 LEU A CD2 
764   N N   . LEU A 163 ? 0.7238 1.6388 0.5925 0.2700  0.0195  0.6471  172 LEU A N   
765   C CA  . LEU A 163 ? 0.7410 1.6018 0.6084 0.2719  0.0250  0.6567  172 LEU A CA  
766   C C   . LEU A 163 ? 0.7233 1.5509 0.5951 0.2550  0.0258  0.6355  172 LEU A C   
767   O O   . LEU A 163 ? 0.7273 1.5089 0.6018 0.2562  0.0282  0.6332  172 LEU A O   
768   C CB  . LEU A 163 ? 0.7612 1.6252 0.6204 0.2723  0.0279  0.6777  172 LEU A CB  
769   C CG  . LEU A 163 ? 0.7855 1.6782 0.6385 0.2897  0.0276  0.7014  172 LEU A CG  
770   C CD1 . LEU A 163 ? 0.8196 1.7327 0.6654 0.2839  0.0289  0.7165  172 LEU A CD1 
771   C CD2 . LEU A 163 ? 0.8150 1.6665 0.6627 0.3083  0.0301  0.7186  172 LEU A CD2 
772   N N   . SER A 164 ? 0.7020 1.5543 0.5729 0.2408  0.0233  0.6200  173 SER A N   
773   C CA  . SER A 164 ? 0.6828 1.5117 0.5560 0.2262  0.0236  0.5995  173 SER A CA  
774   C C   . SER A 164 ? 0.6676 1.4776 0.5473 0.2262  0.0212  0.5832  173 SER A C   
775   O O   . SER A 164 ? 0.6669 1.4369 0.5508 0.2213  0.0235  0.5748  173 SER A O   
776   C CB  . SER A 164 ? 0.6711 1.5346 0.5381 0.2156  0.0202  0.5851  173 SER A CB  
777   O OG  . SER A 164 ? 0.6701 1.5171 0.5355 0.2056  0.0233  0.5790  173 SER A OG  
778   N N   . THR A 165 ? 0.6575 1.4982 0.5381 0.2312  0.0164  0.5798  174 THR A N   
779   C CA  . THR A 165 ? 0.6458 1.4735 0.5326 0.2304  0.0138  0.5656  174 THR A CA  
780   C C   . THR A 165 ? 0.6559 1.4449 0.5481 0.2431  0.0185  0.5762  174 THR A C   
781   O O   . THR A 165 ? 0.6493 1.4039 0.5462 0.2389  0.0196  0.5643  174 THR A O   
782   C CB  . THR A 165 ? 0.6403 1.5137 0.5265 0.2317  0.0074  0.5625  174 THR A CB  
783   O OG1 . THR A 165 ? 0.6341 1.5333 0.5118 0.2170  0.0016  0.5476  174 THR A OG1 
784   C CG2 . THR A 165 ? 0.6226 1.4857 0.5158 0.2319  0.0051  0.5519  174 THR A CG2 
785   N N   . ASN A 166 ? 0.6788 1.4714 0.5680 0.2595  0.0212  0.5988  175 ASN A N   
786   C CA  . ASN A 166 ? 0.7012 1.4526 0.5902 0.2741  0.0251  0.6097  175 ASN A CA  
787   C C   . ASN A 166 ? 0.7053 1.4019 0.5943 0.2643  0.0288  0.6040  175 ASN A C   
788   O O   . ASN A 166 ? 0.7041 1.3675 0.5968 0.2661  0.0297  0.5954  175 ASN A O   
789   C CB  . ASN A 166 ? 0.7332 1.4905 0.6138 0.2924  0.0273  0.6363  175 ASN A CB  
790   C CG  . ASN A 166 ? 0.7434 1.5523 0.6251 0.3066  0.0241  0.6430  175 ASN A CG  
791   O OD1 . ASN A 166 ? 0.7293 1.5708 0.6179 0.3004  0.0198  0.6280  175 ASN A OD1 
792   N ND2 . ASN A 166 ? 0.7830 1.6000 0.6568 0.3253  0.0257  0.6661  175 ASN A ND2 
793   N N   . LYS A 167 ? 0.7107 1.4016 0.5955 0.2531  0.0307  0.6088  176 LYS A N   
794   C CA  . LYS A 167 ? 0.7177 1.3629 0.6020 0.2415  0.0339  0.6050  176 LYS A CA  
795   C C   . LYS A 167 ? 0.6865 1.3224 0.5789 0.2286  0.0326  0.5792  176 LYS A C   
796   O O   . LYS A 167 ? 0.6890 1.2836 0.5830 0.2219  0.0349  0.5737  176 LYS A O   
797   C CB  . LYS A 167 ? 0.7295 1.3849 0.6087 0.2303  0.0357  0.6143  176 LYS A CB  
798   C CG  . LYS A 167 ? 0.7781 1.4328 0.6473 0.2398  0.0373  0.6417  176 LYS A CG  
799   C CD  . LYS A 167 ? 0.8081 1.4886 0.6738 0.2275  0.0383  0.6487  176 LYS A CD  
800   C CE  . LYS A 167 ? 0.8645 1.5209 0.7190 0.2289  0.0407  0.6756  176 LYS A CE  
801   N NZ  . LYS A 167 ? 0.8820 1.5750 0.7330 0.2195  0.0414  0.6859  176 LYS A NZ  
802   N N   . ALA A 168 ? 0.6585 1.3318 0.5543 0.2243  0.0282  0.5638  177 ALA A N   
803   C CA  . ALA A 168 ? 0.6320 1.2965 0.5328 0.2128  0.0258  0.5394  177 ALA A CA  
804   C C   . ALA A 168 ? 0.6271 1.2679 0.5338 0.2205  0.0258  0.5350  177 ALA A C   
805   O O   . ALA A 168 ? 0.6237 1.2331 0.5346 0.2132  0.0266  0.5213  177 ALA A O   
806   C CB  . ALA A 168 ? 0.6160 1.3221 0.5140 0.2056  0.0199  0.5251  177 ALA A CB  
807   N N   . VAL A 169 ? 0.6278 1.2856 0.5345 0.2362  0.0249  0.5471  178 VAL A N   
808   C CA  . VAL A 169 ? 0.6191 1.2614 0.5307 0.2464  0.0249  0.5439  178 VAL A CA  
809   C C   . VAL A 169 ? 0.6426 1.2313 0.5511 0.2545  0.0299  0.5528  178 VAL A C   
810   O O   . VAL A 169 ? 0.6422 1.2022 0.5545 0.2558  0.0307  0.5432  178 VAL A O   
811   C CB  . VAL A 169 ? 0.6199 1.3029 0.5319 0.2619  0.0224  0.5534  178 VAL A CB  
812   C CG1 . VAL A 169 ? 0.6218 1.2845 0.5361 0.2789  0.0242  0.5566  178 VAL A CG1 
813   C CG2 . VAL A 169 ? 0.5913 1.3179 0.5066 0.2493  0.0159  0.5384  178 VAL A CG2 
814   N N   . VAL A 170 ? 0.6675 1.2409 0.5675 0.2584  0.0328  0.5709  179 VAL A N   
815   C CA  . VAL A 170 ? 0.6971 1.2136 0.5903 0.2613  0.0364  0.5790  179 VAL A CA  
816   C C   . VAL A 170 ? 0.6791 1.1666 0.5775 0.2421  0.0374  0.5619  179 VAL A C   
817   O O   . VAL A 170 ? 0.6819 1.1315 0.5811 0.2441  0.0385  0.5551  179 VAL A O   
818   C CB  . VAL A 170 ? 0.7324 1.2374 0.6134 0.2640  0.0384  0.6018  179 VAL A CB  
819   C CG1 . VAL A 170 ? 0.7630 1.2096 0.6361 0.2545  0.0409  0.6063  179 VAL A CG1 
820   C CG2 . VAL A 170 ? 0.7641 1.2765 0.6361 0.2888  0.0381  0.6208  179 VAL A CG2 
821   N N   . SER A 171 ? 0.6611 1.1682 0.5624 0.2250  0.0370  0.5545  180 SER A N   
822   C CA  . SER A 171 ? 0.6480 1.1339 0.5543 0.2084  0.0378  0.5378  180 SER A CA  
823   C C   . SER A 171 ? 0.6344 1.1095 0.5483 0.2100  0.0362  0.5195  180 SER A C   
824   O O   . SER A 171 ? 0.6472 1.0812 0.5618 0.2089  0.0381  0.5156  180 SER A O   
825   C CB  . SER A 171 ? 0.6269 1.1456 0.5345 0.1943  0.0367  0.5286  180 SER A CB  
826   O OG  . SER A 171 ? 0.6394 1.1463 0.5423 0.1850  0.0398  0.5394  180 SER A OG  
827   N N   . LEU A 172 ? 0.6157 1.1274 0.5341 0.2120  0.0323  0.5093  181 LEU A N   
828   C CA  . LEU A 172 ? 0.6013 1.1064 0.5266 0.2104  0.0302  0.4920  181 LEU A CA  
829   C C   . LEU A 172 ? 0.6221 1.0962 0.5478 0.2251  0.0324  0.4981  181 LEU A C   
830   O O   . LEU A 172 ? 0.6172 1.0644 0.5473 0.2216  0.0329  0.4858  181 LEU A O   
831   C CB  . LEU A 172 ? 0.5826 1.1331 0.5102 0.2087  0.0245  0.4829  181 LEU A CB  
832   C CG  . LEU A 172 ? 0.5539 1.1008 0.4869 0.1995  0.0210  0.4620  181 LEU A CG  
833   C CD1 . LEU A 172 ? 0.5521 1.0834 0.4836 0.1833  0.0205  0.4464  181 LEU A CD1 
834   C CD2 . LEU A 172 ? 0.5282 1.1186 0.4610 0.1974  0.0145  0.4569  181 LEU A CD2 
835   N N   . SER A 173 ? 0.6490 1.1264 0.5686 0.2429  0.0336  0.5168  182 SER A N   
836   C CA  . SER A 173 ? 0.6751 1.1220 0.5908 0.2610  0.0355  0.5233  182 SER A CA  
837   C C   . SER A 173 ? 0.6965 1.0850 0.6071 0.2553  0.0386  0.5223  182 SER A C   
838   O O   . SER A 173 ? 0.7013 1.0623 0.6134 0.2590  0.0392  0.5135  182 SER A O   
839   C CB  . SER A 173 ? 0.7029 1.1588 0.6089 0.2825  0.0363  0.5450  182 SER A CB  
840   O OG  . SER A 173 ? 0.6927 1.2057 0.6040 0.2892  0.0333  0.5458  182 SER A OG  
841   N N   . ASN A 174 ? 0.7181 1.0898 0.6222 0.2449  0.0402  0.5314  183 ASN A N   
842   C CA  . ASN A 174 ? 0.7453 1.0636 0.6432 0.2357  0.0423  0.5316  183 ASN A CA  
843   C C   . ASN A 174 ? 0.7163 1.0277 0.6250 0.2190  0.0423  0.5101  183 ASN A C   
844   O O   . ASN A 174 ? 0.7320 1.0009 0.6385 0.2172  0.0434  0.5047  183 ASN A O   
845   C CB  . ASN A 174 ? 0.7720 1.0823 0.6609 0.2255  0.0435  0.5475  183 ASN A CB  
846   C CG  . ASN A 174 ? 0.8307 1.1383 0.7059 0.2430  0.0434  0.5702  183 ASN A CG  
847   O OD1 . ASN A 174 ? 0.8840 1.1685 0.7507 0.2631  0.0432  0.5756  183 ASN A OD1 
848   N ND2 . ASN A 174 ? 0.8455 1.1783 0.7174 0.2373  0.0434  0.5835  183 ASN A ND2 
849   N N   . GLY A 175 ? 0.6786 1.0300 0.5970 0.2076  0.0405  0.4976  184 GLY A N   
850   C CA  . GLY A 175 ? 0.6441 0.9929 0.5716 0.1943  0.0397  0.4761  184 GLY A CA  
851   C C   . GLY A 175 ? 0.6356 0.9674 0.5674 0.2030  0.0391  0.4664  184 GLY A C   
852   O O   . GLY A 175 ? 0.6403 0.9363 0.5732 0.1976  0.0406  0.4582  184 GLY A O   
853   N N   . VAL A 176 ? 0.6240 0.9843 0.5578 0.2166  0.0370  0.4681  185 VAL A N   
854   C CA  . VAL A 176 ? 0.6132 0.9668 0.5511 0.2268  0.0364  0.4605  185 VAL A CA  
855   C C   . VAL A 176 ? 0.6440 0.9488 0.5731 0.2404  0.0395  0.4690  185 VAL A C   
856   O O   . VAL A 176 ? 0.6415 0.9200 0.5730 0.2408  0.0402  0.4585  185 VAL A O   
857   C CB  . VAL A 176 ? 0.6029 1.0034 0.5436 0.2389  0.0334  0.4641  185 VAL A CB  
858   C CG1 . VAL A 176 ? 0.6054 1.0004 0.5484 0.2539  0.0336  0.4613  185 VAL A CG1 
859   C CG2 . VAL A 176 ? 0.5680 1.0083 0.5151 0.2227  0.0287  0.4511  185 VAL A CG2 
860   N N   . SER A 177 ? 0.6737 0.9642 0.5906 0.2512  0.0410  0.4879  186 SER A N   
861   C CA  . SER A 177 ? 0.7125 0.9508 0.6152 0.2645  0.0430  0.4973  186 SER A CA  
862   C C   . SER A 177 ? 0.7107 0.9046 0.6129 0.2482  0.0441  0.4870  186 SER A C   
863   O O   . SER A 177 ? 0.7345 0.8885 0.6295 0.2569  0.0448  0.4842  186 SER A O   
864   C CB  . SER A 177 ? 0.7513 0.9739 0.6383 0.2711  0.0436  0.5190  186 SER A CB  
865   O OG  . SER A 177 ? 0.8042 0.9658 0.6729 0.2807  0.0445  0.5267  186 SER A OG  
866   N N   . VAL A 178 ? 0.6857 0.8885 0.5948 0.2254  0.0442  0.4812  187 VAL A N   
867   C CA  . VAL A 178 ? 0.6805 0.8486 0.5907 0.2078  0.0452  0.4711  187 VAL A CA  
868   C C   . VAL A 178 ? 0.6513 0.8255 0.5746 0.2025  0.0447  0.4495  187 VAL A C   
869   O O   . VAL A 178 ? 0.6613 0.7973 0.5821 0.2013  0.0455  0.4427  187 VAL A O   
870   C CB  . VAL A 178 ? 0.6706 0.8471 0.5815 0.1874  0.0459  0.4748  187 VAL A CB  
871   C CG1 . VAL A 178 ? 0.6492 0.8109 0.5669 0.1688  0.0466  0.4598  187 VAL A CG1 
872   C CG2 . VAL A 178 ? 0.7101 0.8558 0.6043 0.1879  0.0465  0.4956  187 VAL A CG2 
873   N N   . LEU A 179 ? 0.6189 0.8388 0.5540 0.1986  0.0427  0.4391  188 LEU A N   
874   C CA  . LEU A 179 ? 0.5900 0.8185 0.5359 0.1929  0.0412  0.4196  188 LEU A CA  
875   C C   . LEU A 179 ? 0.5999 0.8127 0.5449 0.2093  0.0415  0.4179  188 LEU A C   
876   O O   . LEU A 179 ? 0.5928 0.7854 0.5418 0.2053  0.0418  0.4054  188 LEU A O   
877   C CB  . LEU A 179 ? 0.5610 0.8389 0.5143 0.1876  0.0376  0.4115  188 LEU A CB  
878   C CG  . LEU A 179 ? 0.5332 0.8178 0.4949 0.1773  0.0350  0.3912  188 LEU A CG  
879   C CD1 . LEU A 179 ? 0.5222 0.7946 0.4850 0.1598  0.0355  0.3800  188 LEU A CD1 
880   C CD2 . LEU A 179 ? 0.5126 0.8415 0.4771 0.1770  0.0301  0.3864  188 LEU A CD2 
881   N N   . THR A 180 ? 0.6199 0.8432 0.5589 0.2290  0.0414  0.4309  189 THR A N   
882   C CA  . THR A 180 ? 0.6422 0.8467 0.5762 0.2489  0.0423  0.4322  189 THR A CA  
883   C C   . THR A 180 ? 0.6751 0.8178 0.5973 0.2488  0.0445  0.4333  189 THR A C   
884   O O   . THR A 180 ? 0.6695 0.7917 0.5947 0.2466  0.0449  0.4207  189 THR A O   
885   C CB  . THR A 180 ? 0.6627 0.8871 0.5890 0.2720  0.0422  0.4483  189 THR A CB  
886   O OG1 . THR A 180 ? 0.6347 0.9189 0.5724 0.2710  0.0395  0.4454  189 THR A OG1 
887   C CG2 . THR A 180 ? 0.6952 0.8936 0.6116 0.2966  0.0435  0.4512  189 THR A CG2 
888   N N   . SER A 181 ? 0.7116 0.8246 0.6193 0.2493  0.0454  0.4483  190 SER A N   
889   C CA  . SER A 181 ? 0.7491 0.8003 0.6418 0.2455  0.0463  0.4510  190 SER A CA  
890   C C   . SER A 181 ? 0.7323 0.7680 0.6342 0.2261  0.0466  0.4336  190 SER A C   
891   O O   . SER A 181 ? 0.7608 0.7499 0.6526 0.2279  0.0469  0.4304  190 SER A O   
892   C CB  . SER A 181 ? 0.7749 0.8063 0.6548 0.2354  0.0462  0.4675  190 SER A CB  
893   O OG  . SER A 181 ? 0.8084 0.7786 0.6717 0.2281  0.0460  0.4705  190 SER A OG  
894   N N   . LYS A 182 ? 0.6924 0.7656 0.6117 0.2088  0.0463  0.4223  191 LYS A N   
895   C CA  . LYS A 182 ? 0.6706 0.7331 0.5989 0.1906  0.0466  0.4059  191 LYS A CA  
896   C C   . LYS A 182 ? 0.6472 0.7198 0.5857 0.1960  0.0460  0.3898  191 LYS A C   
897   O O   . LYS A 182 ? 0.6479 0.6941 0.5878 0.1887  0.0465  0.3789  191 LYS A O   
898   C CB  . LYS A 182 ? 0.6417 0.7353 0.5800 0.1710  0.0463  0.4011  191 LYS A CB  
899   C CG  . LYS A 182 ? 0.6814 0.7565 0.6116 0.1569  0.0474  0.4120  191 LYS A CG  
900   C CD  . LYS A 182 ? 0.7242 0.7600 0.6514 0.1428  0.0483  0.4058  191 LYS A CD  
901   C CE  . LYS A 182 ? 0.8014 0.7860 0.7091 0.1448  0.0482  0.4204  191 LYS A CE  
902   N NZ  . LYS A 182 ? 0.8385 0.7907 0.7423 0.1245  0.0483  0.4168  191 LYS A NZ  
903   N N   . VAL A 183 ? 0.6282 0.7416 0.5738 0.2071  0.0445  0.3885  192 VAL A N   
904   C CA  . VAL A 183 ? 0.6021 0.7311 0.5576 0.2103  0.0433  0.3746  192 VAL A CA  
905   C C   . VAL A 183 ? 0.6301 0.7235 0.5763 0.2276  0.0449  0.3757  192 VAL A C   
906   O O   . VAL A 183 ? 0.6248 0.7082 0.5757 0.2262  0.0450  0.3633  192 VAL A O   
907   C CB  . VAL A 183 ? 0.5782 0.7623 0.5418 0.2158  0.0404  0.3745  192 VAL A CB  
908   C CG1 . VAL A 183 ? 0.5650 0.7632 0.5336 0.2274  0.0395  0.3678  192 VAL A CG1 
909   C CG2 . VAL A 183 ? 0.5473 0.7578 0.5195 0.1953  0.0377  0.3642  192 VAL A CG2 
910   N N   . LEU A 184 ? 0.6674 0.7383 0.5982 0.2445  0.0459  0.3905  193 LEU A N   
911   C CA  . LEU A 184 ? 0.7059 0.7354 0.6231 0.2621  0.0470  0.3909  193 LEU A CA  
912   C C   . LEU A 184 ? 0.7158 0.7005 0.6303 0.2453  0.0475  0.3810  193 LEU A C   
913   O O   . LEU A 184 ? 0.7171 0.6898 0.6338 0.2487  0.0478  0.3693  193 LEU A O   
914   C CB  . LEU A 184 ? 0.7553 0.7557 0.6509 0.2813  0.0474  0.4088  193 LEU A CB  
915   C CG  . LEU A 184 ? 0.8008 0.7517 0.6760 0.3035  0.0478  0.4094  193 LEU A CG  
916   C CD1 . LEU A 184 ? 0.7908 0.7767 0.6683 0.3322  0.0482  0.4090  193 LEU A CD1 
917   C CD2 . LEU A 184 ? 0.8659 0.7628 0.7136 0.3110  0.0470  0.4256  193 LEU A CD2 
918   N N   . ASP A 185 ? 0.7309 0.6945 0.6409 0.2265  0.0476  0.3861  194 ASP A N   
919   C CA  . ASP A 185 ? 0.7465 0.6700 0.6532 0.2082  0.0478  0.3784  194 ASP A CA  
920   C C   . ASP A 185 ? 0.7059 0.6477 0.6305 0.1963  0.0480  0.3592  194 ASP A C   
921   O O   . ASP A 185 ? 0.7137 0.6227 0.6344 0.1936  0.0483  0.3503  194 ASP A O   
922   C CB  . ASP A 185 ? 0.7599 0.6744 0.6625 0.1875  0.0477  0.3879  194 ASP A CB  
923   C CG  . ASP A 185 ? 0.8223 0.7118 0.7043 0.1975  0.0470  0.4079  194 ASP A CG  
924   O OD1 . ASP A 185 ? 0.8629 0.7356 0.7318 0.2223  0.0466  0.4132  194 ASP A OD1 
925   O OD2 . ASP A 185 ? 0.8472 0.7348 0.7251 0.1817  0.0467  0.4186  194 ASP A OD2 
926   N N   . LEU A 186 ? 0.6651 0.6567 0.6067 0.1897  0.0474  0.3532  195 LEU A N   
927   C CA  . LEU A 186 ? 0.6299 0.6397 0.5863 0.1795  0.0467  0.3359  195 LEU A CA  
928   C C   . LEU A 186 ? 0.6339 0.6378 0.5904 0.1950  0.0468  0.3288  195 LEU A C   
929   O O   . LEU A 186 ? 0.6335 0.6164 0.5919 0.1892  0.0472  0.3175  195 LEU A O   
930   C CB  . LEU A 186 ? 0.5957 0.6563 0.5649 0.1726  0.0447  0.3316  195 LEU A CB  
931   C CG  . LEU A 186 ? 0.5663 0.6353 0.5447 0.1520  0.0439  0.3181  195 LEU A CG  
932   C CD1 . LEU A 186 ? 0.5295 0.6362 0.5175 0.1492  0.0405  0.3073  195 LEU A CD1 
933   C CD2 . LEU A 186 ? 0.5680 0.6017 0.5462 0.1439  0.0454  0.3089  195 LEU A CD2 
934   N N   . LYS A 187 ? 0.6418 0.6672 0.5963 0.2155  0.0464  0.3356  196 LYS A N   
935   C CA  . LYS A 187 ? 0.6545 0.6749 0.6066 0.2338  0.0468  0.3309  196 LYS A CA  
936   C C   . LYS A 187 ? 0.6950 0.6554 0.6308 0.2384  0.0483  0.3301  196 LYS A C   
937   O O   . LYS A 187 ? 0.6936 0.6391 0.6318 0.2361  0.0486  0.3180  196 LYS A O   
938   C CB  . LYS A 187 ? 0.6653 0.7150 0.6134 0.2585  0.0466  0.3418  196 LYS A CB  
939   C CG  . LYS A 187 ? 0.6776 0.7175 0.6175 0.2839  0.0477  0.3404  196 LYS A CG  
940   C CD  . LYS A 187 ? 0.7292 0.7162 0.6447 0.3028  0.0490  0.3504  196 LYS A CD  
941   C CE  . LYS A 187 ? 0.7656 0.7480 0.6703 0.3330  0.0500  0.3497  196 LYS A CE  
942   N NZ  . LYS A 187 ? 0.8362 0.7544 0.7117 0.3508  0.0503  0.3573  196 LYS A NZ  
943   N N   . ASN A 188 ? 0.7377 0.6620 0.6557 0.2430  0.0486  0.3428  197 ASN A N   
944   C CA  . ASN A 188 ? 0.7886 0.6507 0.6856 0.2482  0.0487  0.3433  197 ASN A CA  
945   C C   . ASN A 188 ? 0.7862 0.6195 0.6858 0.2251  0.0486  0.3318  197 ASN A C   
946   O O   . ASN A 188 ? 0.8154 0.6084 0.7026 0.2309  0.0484  0.3255  197 ASN A O   
947   C CB  . ASN A 188 ? 0.8362 0.6620 0.7102 0.2558  0.0480  0.3605  197 ASN A CB  
948   C CG  . ASN A 188 ? 0.8816 0.7011 0.7392 0.2902  0.0480  0.3686  197 ASN A CG  
949   O OD1 . ASN A 188 ? 0.9023 0.7428 0.7566 0.3025  0.0479  0.3818  197 ASN A OD1 
950   N ND2 . ASN A 188 ? 0.9109 0.7049 0.7579 0.3074  0.0482  0.3605  197 ASN A ND2 
951   N N   . TYR A 189 ? 0.7565 0.6115 0.6708 0.2002  0.0486  0.3288  198 TYR A N   
952   C CA  . TYR A 189 ? 0.7416 0.5833 0.6630 0.1791  0.0487  0.3161  198 TYR A CA  
953   C C   . TYR A 189 ? 0.7131 0.5680 0.6451 0.1858  0.0490  0.3008  198 TYR A C   
954   O O   . TYR A 189 ? 0.7327 0.5525 0.6558 0.1887  0.0491  0.2940  198 TYR A O   
955   C CB  . TYR A 189 ? 0.7131 0.5864 0.6497 0.1562  0.0488  0.3141  198 TYR A CB  
956   C CG  . TYR A 189 ? 0.7349 0.5865 0.6726 0.1345  0.0490  0.3062  198 TYR A CG  
957   C CD1 . TYR A 189 ? 0.8058 0.6172 0.7276 0.1224  0.0484  0.3153  198 TYR A CD1 
958   C CD2 . TYR A 189 ? 0.7119 0.5827 0.6651 0.1253  0.0492  0.2905  198 TYR A CD2 
959   C CE1 . TYR A 189 ? 0.8216 0.6165 0.7440 0.1008  0.0483  0.3091  198 TYR A CE1 
960   C CE2 . TYR A 189 ? 0.7355 0.5891 0.6896 0.1060  0.0495  0.2837  198 TYR A CE2 
961   C CZ  . TYR A 189 ? 0.7866 0.6042 0.7259 0.0936  0.0491  0.2932  198 TYR A CZ  
962   O OH  . TYR A 189 ? 0.7857 0.5905 0.7257 0.0732  0.0490  0.2877  198 TYR A OH  
963   N N   . ILE A 190 ? 0.6711 0.5760 0.6203 0.1877  0.0487  0.2957  199 ILE A N   
964   C CA  . ILE A 190 ? 0.6508 0.5726 0.6093 0.1942  0.0486  0.2835  199 ILE A CA  
965   C C   . ILE A 190 ? 0.6889 0.5817 0.6333 0.2167  0.0494  0.2832  199 ILE A C   
966   O O   . ILE A 190 ? 0.6946 0.5624 0.6368 0.2139  0.0497  0.2729  199 ILE A O   
967   C CB  . ILE A 190 ? 0.6160 0.5930 0.5884 0.1978  0.0471  0.2833  199 ILE A CB  
968   C CG1 . ILE A 190 ? 0.5773 0.5775 0.5628 0.1748  0.0456  0.2759  199 ILE A CG1 
969   C CG2 . ILE A 190 ? 0.6042 0.5987 0.5815 0.2105  0.0468  0.2758  199 ILE A CG2 
970   C CD1 . ILE A 190 ? 0.5515 0.5985 0.5448 0.1741  0.0431  0.2789  199 ILE A CD1 
971   N N   . ASP A 191 ? 0.7219 0.6175 0.6554 0.2401  0.0496  0.2943  200 ASP A N   
972   C CA  . ASP A 191 ? 0.7638 0.6377 0.6823 0.2667  0.0503  0.2935  200 ASP A CA  
973   C C   . ASP A 191 ? 0.8059 0.6110 0.7019 0.2662  0.0501  0.2920  200 ASP A C   
974   O O   . ASP A 191 ? 0.8212 0.6045 0.7094 0.2768  0.0504  0.2830  200 ASP A O   
975   C CB  . ASP A 191 ? 0.7913 0.6840 0.7004 0.2951  0.0506  0.3068  200 ASP A CB  
976   C CG  . ASP A 191 ? 0.8495 0.7224 0.7408 0.3274  0.0515  0.3056  200 ASP A CG  
977   O OD1 . ASP A 191 ? 0.8619 0.7397 0.7586 0.3300  0.0520  0.2932  200 ASP A OD1 
978   O OD2 . ASP A 191 ? 0.9014 0.7540 0.7718 0.3516  0.0515  0.3173  200 ASP A OD2 
979   N N   . LYS A 192 ? 0.8291 0.6000 0.7131 0.2533  0.0492  0.3009  201 LYS A N   
980   C CA  . LYS A 192 ? 0.8864 0.5887 0.7428 0.2556  0.0478  0.3024  201 LYS A CA  
981   C C   . LYS A 192 ? 0.8853 0.5592 0.7425 0.2244  0.0467  0.2967  201 LYS A C   
982   O O   . LYS A 192 ? 0.9300 0.5458 0.7635 0.2202  0.0446  0.2981  201 LYS A O   
983   C CB  . LYS A 192 ? 0.9367 0.6093 0.7682 0.2723  0.0465  0.3192  201 LYS A CB  
984   C CG  . LYS A 192 ? 0.9583 0.6554 0.7853 0.3085  0.0476  0.3232  201 LYS A CG  
985   C CD  . LYS A 192 ? 1.0558 0.7146 0.8525 0.3311  0.0461  0.3390  201 LYS A CD  
986   C CE  . LYS A 192 ? 1.0842 0.7843 0.8816 0.3671  0.0478  0.3438  201 LYS A CE  
987   N NZ  . LYS A 192 ? 1.1491 0.8357 0.9255 0.3876  0.0468  0.3620  201 LYS A NZ  
988   N N   . GLN A 193 ? 0.8407 0.5558 0.7237 0.2028  0.0478  0.2899  202 GLN A N   
989   C CA  . GLN A 193 ? 0.8395 0.5378 0.7258 0.1738  0.0471  0.2848  202 GLN A CA  
990   C C   . GLN A 193 ? 0.7921 0.5159 0.6985 0.1650  0.0482  0.2681  202 GLN A C   
991   O O   . GLN A 193 ? 0.8060 0.4992 0.7055 0.1605  0.0477  0.2589  202 GLN A O   
992   C CB  . GLN A 193 ? 0.8298 0.5522 0.7252 0.1548  0.0473  0.2944  202 GLN A CB  
993   C CG  . GLN A 193 ? 0.9135 0.6013 0.7867 0.1545  0.0456  0.3115  202 GLN A CG  
994   C CD  . GLN A 193 ? 1.0054 0.6402 0.8600 0.1341  0.0432  0.3131  202 GLN A CD  
995   O OE1 . GLN A 193 ? 1.0105 0.6544 0.8766 0.1115  0.0435  0.3051  202 GLN A OE1 
996   N NE2 . GLN A 193 ? 1.0776 0.6563 0.9014 0.1418  0.0403  0.3236  202 GLN A NE2 
997   N N   . LEU A 194 ? 0.7378 0.5162 0.6670 0.1624  0.0492  0.2646  203 LEU A N   
998   C CA  . LEU A 194 ? 0.6893 0.4956 0.6374 0.1532  0.0496  0.2500  203 LEU A CA  
999   C C   . LEU A 194 ? 0.6893 0.4958 0.6368 0.1715  0.0498  0.2414  203 LEU A C   
1000  O O   . LEU A 194 ? 0.6876 0.4769 0.6351 0.1664  0.0499  0.2304  203 LEU A O   
1001  C CB  . LEU A 194 ? 0.6447 0.5040 0.6114 0.1474  0.0493  0.2499  203 LEU A CB  
1002  C CG  . LEU A 194 ? 0.5994 0.4882 0.5830 0.1397  0.0486  0.2357  203 LEU A CG  
1003  C CD1 . LEU A 194 ? 0.5870 0.4759 0.5772 0.1173  0.0486  0.2296  203 LEU A CD1 
1004  C CD2 . LEU A 194 ? 0.5707 0.5061 0.5650 0.1451  0.0471  0.2367  203 LEU A CD2 
1005  N N   . LEU A 195 ? 0.6914 0.5208 0.6383 0.1930  0.0500  0.2471  204 LEU A N   
1006  C CA  . LEU A 195 ? 0.6859 0.5329 0.6362 0.2108  0.0504  0.2401  204 LEU A CA  
1007  C C   . LEU A 195 ? 0.7175 0.5196 0.6523 0.2197  0.0508  0.2328  204 LEU A C   
1008  O O   . LEU A 195 ? 0.7082 0.5230 0.6510 0.2211  0.0511  0.2217  204 LEU A O   
1009  C CB  . LEU A 195 ? 0.6921 0.5686 0.6403 0.2346  0.0505  0.2499  204 LEU A CB  
1010  C CG  . LEU A 195 ? 0.6765 0.5970 0.6359 0.2475  0.0505  0.2443  204 LEU A CG  
1011  C CD1 . LEU A 195 ? 0.6230 0.5923 0.6039 0.2281  0.0487  0.2408  204 LEU A CD1 
1012  C CD2 . LEU A 195 ? 0.7186 0.6566 0.6685 0.2778  0.0512  0.2548  204 LEU A CD2 
1013  N N   . PRO A 196 ? 0.7638 0.5116 0.6744 0.2245  0.0503  0.2389  205 PRO A N   
1014  C CA  . PRO A 196 ? 0.7977 0.4973 0.6903 0.2305  0.0498  0.2305  205 PRO A CA  
1015  C C   . PRO A 196 ? 0.7753 0.4708 0.6793 0.2061  0.0496  0.2175  205 PRO A C   
1016  O O   . PRO A 196 ? 0.7785 0.4667 0.6812 0.2122  0.0499  0.2061  205 PRO A O   
1017  C CB  . PRO A 196 ? 0.8495 0.4895 0.7135 0.2306  0.0478  0.2407  205 PRO A CB  
1018  C CG  . PRO A 196 ? 0.8550 0.5160 0.7190 0.2410  0.0482  0.2550  205 PRO A CG  
1019  C CD  . PRO A 196 ? 0.7961 0.5218 0.6914 0.2275  0.0495  0.2539  205 PRO A CD  
1020  N N   . ILE A 197 ? 0.7527 0.4559 0.6677 0.1797  0.0493  0.2191  206 ILE A N   
1021  C CA  . ILE A 197 ? 0.7347 0.4323 0.6580 0.1576  0.0491  0.2080  206 ILE A CA  
1022  C C   . ILE A 197 ? 0.6774 0.4266 0.6268 0.1514  0.0500  0.1987  206 ILE A C   
1023  O O   . ILE A 197 ? 0.6554 0.4064 0.6135 0.1356  0.0500  0.1889  206 ILE A O   
1024  C CB  . ILE A 197 ? 0.7482 0.4215 0.6657 0.1318  0.0479  0.2135  206 ILE A CB  
1025  C CG1 . ILE A 197 ? 0.7083 0.4263 0.6483 0.1133  0.0488  0.2139  206 ILE A CG1 
1026  C CG2 . ILE A 197 ? 0.8068 0.4380 0.6990 0.1369  0.0462  0.2279  206 ILE A CG2 
1027  C CD1 . ILE A 197 ? 0.7363 0.4397 0.6753 0.0866  0.0481  0.2129  206 ILE A CD1 
1028  N N   . VAL A 198 ? 0.6580 0.4484 0.6182 0.1634  0.0503  0.2023  207 VAL A N   
1029  C CA  . VAL A 198 ? 0.6255 0.4577 0.6047 0.1598  0.0501  0.1934  207 VAL A CA  
1030  C C   . VAL A 198 ? 0.6425 0.4653 0.6163 0.1755  0.0507  0.1857  207 VAL A C   
1031  O O   . VAL A 198 ? 0.6399 0.4555 0.6178 0.1666  0.0507  0.1747  207 VAL A O   
1032  C CB  . VAL A 198 ? 0.6011 0.4812 0.5915 0.1659  0.0492  0.1994  207 VAL A CB  
1033  C CG1 . VAL A 198 ? 0.5659 0.4842 0.5712 0.1641  0.0480  0.1903  207 VAL A CG1 
1034  C CG2 . VAL A 198 ? 0.5947 0.4871 0.5908 0.1497  0.0484  0.2048  207 VAL A CG2 
1035  N N   . ASN A 199 ? 0.6686 0.4920 0.6321 0.2004  0.0512  0.1914  208 ASN A N   
1036  C CA  . ASN A 199 ? 0.6864 0.5105 0.6462 0.2172  0.0519  0.1835  208 ASN A CA  
1037  C C   . ASN A 199 ? 0.7292 0.4952 0.6680 0.2210  0.0521  0.1773  208 ASN A C   
1038  O O   . ASN A 199 ? 0.7487 0.5064 0.6786 0.2389  0.0527  0.1708  208 ASN A O   
1039  C CB  . ASN A 199 ? 0.6857 0.5506 0.6476 0.2423  0.0524  0.1892  208 ASN A CB  
1040  C CG  . ASN A 199 ? 0.7217 0.5692 0.6654 0.2644  0.0530  0.2015  208 ASN A CG  
1041  O OD1 . ASN A 199 ? 0.7609 0.5610 0.6880 0.2613  0.0526  0.2062  208 ASN A OD1 
1042  N ND2 . ASN A 199 ? 0.7136 0.6009 0.6592 0.2867  0.0535  0.2075  208 ASN A ND2 
1043  N N   . LYS A 200 ? 0.7460 0.4734 0.6765 0.2025  0.0511  0.1790  209 LYS A N   
1044  C CA  . LYS A 200 ? 0.7797 0.4568 0.6935 0.1968  0.0502  0.1712  209 LYS A CA  
1045  C C   . LYS A 200 ? 0.7390 0.4356 0.6713 0.1776  0.0505  0.1589  209 LYS A C   
1046  O O   . LYS A 200 ? 0.7421 0.4265 0.6697 0.1827  0.0506  0.1486  209 LYS A O   
1047  C CB  . LYS A 200 ? 0.8169 0.4467 0.7130 0.1821  0.0484  0.1789  209 LYS A CB  
1048  C CG  . LYS A 200 ? 0.8952 0.4611 0.7576 0.1954  0.0463  0.1781  209 LYS A CG  
1049  C CD  . LYS A 200 ? 0.9630 0.4890 0.8021 0.1969  0.0442  0.1922  209 LYS A CD  
1050  C CE  . LYS A 200 ? 1.0017 0.4842 0.8279 0.1676  0.0411  0.1937  209 LYS A CE  
1051  N NZ  . LYS A 200 ? 1.0302 0.5106 0.8538 0.1552  0.0402  0.2092  209 LYS A NZ  
1052  N N   . GLN A 201 ? 0.7005 0.4276 0.6521 0.1569  0.0506  0.1604  210 GLN A N   
1053  C CA  . GLN A 201 ? 0.6634 0.4154 0.6334 0.1402  0.0506  0.1502  210 GLN A CA  
1054  C C   . GLN A 201 ? 0.6490 0.4322 0.6284 0.1541  0.0511  0.1433  210 GLN A C   
1055  O O   . GLN A 201 ? 0.6425 0.4241 0.6255 0.1496  0.0511  0.1326  210 GLN A O   
1056  C CB  . GLN A 201 ? 0.6255 0.4119 0.6125 0.1240  0.0503  0.1539  210 GLN A CB  
1057  C CG  . GLN A 201 ? 0.6413 0.4100 0.6240 0.1063  0.0500  0.1603  210 GLN A CG  
1058  C CD  . GLN A 201 ? 0.6251 0.4322 0.6231 0.0955  0.0497  0.1635  210 GLN A CD  
1059  O OE1 . GLN A 201 ? 0.6074 0.4485 0.6154 0.1028  0.0491  0.1635  210 GLN A OE1 
1060  N NE2 . GLN A 201 ? 0.6221 0.4246 0.6204 0.0779  0.0498  0.1663  210 GLN A NE2 
1061  N N   . SER A 202 ? 0.6468 0.4615 0.6303 0.1701  0.0512  0.1500  211 SER A N   
1062  C CA  . SER A 202 ? 0.6356 0.4879 0.6286 0.1819  0.0513  0.1455  211 SER A CA  
1063  C C   . SER A 202 ? 0.6645 0.4915 0.6452 0.1954  0.0523  0.1371  211 SER A C   
1064  O O   . SER A 202 ? 0.6464 0.4944 0.6363 0.1944  0.0523  0.1286  211 SER A O   
1065  C CB  . SER A 202 ? 0.6356 0.5212 0.6296 0.2002  0.0513  0.1554  211 SER A CB  
1066  O OG  . SER A 202 ? 0.6152 0.5348 0.6233 0.1860  0.0495  0.1605  211 SER A OG  
1067  N N   . CYS A 203 ? 0.7139 0.4930 0.6720 0.2070  0.0527  0.1393  212 CYS A N   
1068  C CA  . CYS A 203 ? 0.7503 0.4981 0.6920 0.2207  0.0531  0.1304  212 CYS A CA  
1069  C C   . CYS A 203 ? 0.7309 0.4608 0.6761 0.1997  0.0525  0.1187  212 CYS A C   
1070  O O   . CYS A 203 ? 0.7103 0.4554 0.6612 0.2034  0.0530  0.1091  212 CYS A O   
1071  C CB  . CYS A 203 ? 0.8138 0.5066 0.7251 0.2375  0.0524  0.1351  212 CYS A CB  
1072  S SG  . CYS A 203 ? 0.9074 0.5745 0.8001 0.2578  0.0526  0.1223  212 CYS A SG  
1073  N N   . SER A 204 ? 0.7334 0.4331 0.6748 0.1780  0.0513  0.1204  213 SER A N   
1074  C CA  . SER A 204 ? 0.7231 0.4059 0.6669 0.1560  0.0506  0.1111  213 SER A CA  
1075  C C   . SER A 204 ? 0.6695 0.3976 0.6373 0.1471  0.0512  0.1035  213 SER A C   
1076  O O   . SER A 204 ? 0.6740 0.3961 0.6418 0.1436  0.0512  0.0930  213 SER A O   
1077  C CB  . SER A 204 ? 0.7271 0.3915 0.6699 0.1318  0.0494  0.1169  213 SER A CB  
1078  O OG  . SER A 204 ? 0.7930 0.4095 0.7104 0.1371  0.0480  0.1244  213 SER A OG  
1079  N N   . ILE A 205 ? 0.6226 0.3941 0.6088 0.1431  0.0513  0.1088  214 ILE A N   
1080  C CA  . ILE A 205 ? 0.5755 0.3881 0.5809 0.1361  0.0509  0.1027  214 ILE A CA  
1081  C C   . ILE A 205 ? 0.5757 0.4039 0.5806 0.1536  0.0516  0.0966  214 ILE A C   
1082  O O   . ILE A 205 ? 0.5631 0.3970 0.5738 0.1466  0.0514  0.0872  214 ILE A O   
1083  C CB  . ILE A 205 ? 0.5458 0.3964 0.5650 0.1307  0.0498  0.1101  214 ILE A CB  
1084  C CG1 . ILE A 205 ? 0.5395 0.3786 0.5603 0.1121  0.0494  0.1135  214 ILE A CG1 
1085  C CG2 . ILE A 205 ? 0.5068 0.3974 0.5415 0.1245  0.0482  0.1049  214 ILE A CG2 
1086  C CD1 . ILE A 205 ? 0.5436 0.4077 0.5704 0.1114  0.0484  0.1225  214 ILE A CD1 
1087  N N   . SER A 206 ? 0.5872 0.4236 0.5843 0.1771  0.0523  0.1023  215 SER A N   
1088  C CA  . SER A 206 ? 0.5878 0.4423 0.5826 0.1969  0.0533  0.0976  215 SER A CA  
1089  C C   . SER A 206 ? 0.6041 0.4227 0.5867 0.1982  0.0538  0.0860  215 SER A C   
1090  O O   . SER A 206 ? 0.5915 0.4308 0.5802 0.2010  0.0541  0.0783  215 SER A O   
1091  C CB  . SER A 206 ? 0.6192 0.4776 0.6013 0.2255  0.0544  0.1055  215 SER A CB  
1092  O OG  . SER A 206 ? 0.6307 0.5156 0.6113 0.2467  0.0555  0.1017  215 SER A OG  
1093  N N   . ASN A 207 ? 0.6296 0.3944 0.5938 0.1947  0.0534  0.0852  216 ASN A N   
1094  C CA  . ASN A 207 ? 0.6466 0.3715 0.5965 0.1915  0.0529  0.0742  216 ASN A CA  
1095  C C   . ASN A 207 ? 0.6052 0.3443 0.5719 0.1671  0.0525  0.0661  216 ASN A C   
1096  O O   . ASN A 207 ? 0.5991 0.3507 0.5691 0.1708  0.0529  0.0570  216 ASN A O   
1097  C CB  . ASN A 207 ? 0.6917 0.3563 0.6174 0.1877  0.0514  0.0768  216 ASN A CB  
1098  C CG  . ASN A 207 ? 0.7438 0.3864 0.6480 0.2140  0.0514  0.0840  216 ASN A CG  
1099  O OD1 . ASN A 207 ? 0.7522 0.4263 0.6589 0.2385  0.0530  0.0864  216 ASN A OD1 
1100  N ND2 . ASN A 207 ? 0.8020 0.3914 0.6836 0.2096  0.0493  0.0884  216 ASN A ND2 
1101  N N   . ILE A 208 ? 0.5737 0.3126 0.5503 0.1436  0.0517  0.0697  217 ILE A N   
1102  C CA  . ILE A 208 ? 0.5370 0.2924 0.5291 0.1224  0.0512  0.0632  217 ILE A CA  
1103  C C   . ILE A 208 ? 0.5082 0.3079 0.5162 0.1273  0.0515  0.0589  217 ILE A C   
1104  O O   . ILE A 208 ? 0.5029 0.3036 0.5123 0.1247  0.0515  0.0495  217 ILE A O   
1105  C CB  . ILE A 208 ? 0.5138 0.2810 0.5172 0.1039  0.0507  0.0699  217 ILE A CB  
1106  C CG1 . ILE A 208 ? 0.5484 0.2734 0.5362 0.0950  0.0501  0.0742  217 ILE A CG1 
1107  C CG2 . ILE A 208 ? 0.4853 0.2750 0.5046 0.0856  0.0501  0.0634  217 ILE A CG2 
1108  C CD1 . ILE A 208 ? 0.5383 0.2757 0.5342 0.0821  0.0499  0.0835  217 ILE A CD1 
1109  N N   . GLU A 209 ? 0.4939 0.3304 0.5125 0.1335  0.0512  0.0662  218 GLU A N   
1110  C CA  . GLU A 209 ? 0.4790 0.3587 0.5111 0.1355  0.0506  0.0639  218 GLU A CA  
1111  C C   . GLU A 209 ? 0.4890 0.3661 0.5134 0.1513  0.0519  0.0561  218 GLU A C   
1112  O O   . GLU A 209 ? 0.4753 0.3655 0.5067 0.1444  0.0515  0.0485  218 GLU A O   
1113  C CB  . GLU A 209 ? 0.4729 0.3893 0.5120 0.1432  0.0497  0.0739  218 GLU A CB  
1114  C CG  . GLU A 209 ? 0.5038 0.4328 0.5532 0.1245  0.0474  0.0791  218 GLU A CG  
1115  C CD  . GLU A 209 ? 0.5696 0.5288 0.6226 0.1306  0.0460  0.0901  218 GLU A CD  
1116  O OE1 . GLU A 209 ? 0.6036 0.5684 0.6498 0.1509  0.0475  0.0953  218 GLU A OE1 
1117  O OE2 . GLU A 209 ? 0.5724 0.5489 0.6334 0.1154  0.0431  0.0933  218 GLU A OE2 
1118  N N   . THR A 210 ? 0.5167 0.3749 0.5245 0.1738  0.0533  0.0579  219 THR A N   
1119  C CA  . THR A 210 ? 0.5299 0.3852 0.5269 0.1935  0.0545  0.0505  219 THR A CA  
1120  C C   . THR A 210 ? 0.5289 0.3559 0.5214 0.1810  0.0542  0.0387  219 THR A C   
1121  O O   . THR A 210 ? 0.5203 0.3705 0.5197 0.1817  0.0544  0.0318  219 THR A O   
1122  C CB  . THR A 210 ? 0.5760 0.4028 0.5499 0.2207  0.0556  0.0535  219 THR A CB  
1123  O OG1 . THR A 210 ? 0.5686 0.4302 0.5488 0.2326  0.0560  0.0651  219 THR A OG1 
1124  C CG2 . THR A 210 ? 0.5996 0.4217 0.5590 0.2438  0.0568  0.0446  219 THR A CG2 
1125  N N   . VAL A 211 ? 0.5334 0.3144 0.5151 0.1678  0.0534  0.0370  220 VAL A N   
1126  C CA  . VAL A 211 ? 0.5263 0.2823 0.5034 0.1536  0.0527  0.0264  220 VAL A CA  
1127  C C   . VAL A 211 ? 0.4809 0.2749 0.4804 0.1365  0.0524  0.0225  220 VAL A C   
1128  O O   . VAL A 211 ? 0.4772 0.2836 0.4783 0.1407  0.0528  0.0144  220 VAL A O   
1129  C CB  . VAL A 211 ? 0.5443 0.2554 0.5101 0.1361  0.0512  0.0276  220 VAL A CB  
1130  C CG1 . VAL A 211 ? 0.5262 0.2301 0.4962 0.1145  0.0503  0.0188  220 VAL A CG1 
1131  C CG2 . VAL A 211 ? 0.5977 0.2573 0.5334 0.1522  0.0503  0.0273  220 VAL A CG2 
1132  N N   . ILE A 212 ? 0.4473 0.2597 0.4625 0.1186  0.0516  0.0282  221 ILE A N   
1133  C CA  . ILE A 212 ? 0.4113 0.2566 0.4444 0.1042  0.0507  0.0252  221 ILE A CA  
1134  C C   . ILE A 212 ? 0.4096 0.2894 0.4487 0.1163  0.0509  0.0223  221 ILE A C   
1135  O O   . ILE A 212 ? 0.3993 0.2863 0.4417 0.1118  0.0507  0.0142  221 ILE A O   
1136  C CB  . ILE A 212 ? 0.3795 0.2486 0.4260 0.0927  0.0493  0.0336  221 ILE A CB  
1137  C CG1 . ILE A 212 ? 0.3766 0.2190 0.4187 0.0807  0.0493  0.0374  221 ILE A CG1 
1138  C CG2 . ILE A 212 ? 0.3388 0.2363 0.3993 0.0792  0.0474  0.0305  221 ILE A CG2 
1139  C CD1 . ILE A 212 ? 0.3796 0.2004 0.4185 0.0661  0.0493  0.0304  221 ILE A CD1 
1140  N N   . GLU A 213 ? 0.4244 0.3285 0.4647 0.1315  0.0511  0.0296  222 GLU A N   
1141  C CA  . GLU A 213 ? 0.4320 0.3787 0.4797 0.1411  0.0509  0.0297  222 GLU A CA  
1142  C C   . GLU A 213 ? 0.4570 0.3943 0.4934 0.1574  0.0528  0.0202  222 GLU A C   
1143  O O   . GLU A 213 ? 0.4471 0.4190 0.4901 0.1618  0.0527  0.0177  222 GLU A O   
1144  C CB  . GLU A 213 ? 0.4313 0.4088 0.4817 0.1537  0.0506  0.0406  222 GLU A CB  
1145  C CG  . GLU A 213 ? 0.4476 0.4798 0.5130 0.1470  0.0480  0.0455  222 GLU A CG  
1146  C CD  . GLU A 213 ? 0.5139 0.5806 0.5823 0.1559  0.0470  0.0574  222 GLU A CD  
1147  O OE1 . GLU A 213 ? 0.5717 0.6183 0.6314 0.1678  0.0487  0.0618  222 GLU A OE1 
1148  O OE2 . GLU A 213 ? 0.5173 0.6313 0.5957 0.1499  0.0442  0.0630  222 GLU A OE2 
1149  N N   . PHE A 214 ? 0.4941 0.3834 0.5119 0.1653  0.0540  0.0149  223 PHE A N   
1150  C CA  . PHE A 214 ? 0.5229 0.3946 0.5253 0.1808  0.0551  0.0047  223 PHE A CA  
1151  C C   . PHE A 214 ? 0.5127 0.3824 0.5216 0.1623  0.0543  -0.0046 223 PHE A C   
1152  O O   . PHE A 214 ? 0.5132 0.4028 0.5233 0.1692  0.0549  -0.0112 223 PHE A O   
1153  C CB  . PHE A 214 ? 0.5658 0.3805 0.5422 0.1924  0.0553  0.0025  223 PHE A CB  
1154  C CG  . PHE A 214 ? 0.5954 0.3786 0.5506 0.2050  0.0553  -0.0095 223 PHE A CG  
1155  C CD1 . PHE A 214 ? 0.6174 0.4090 0.5587 0.2360  0.0568  -0.0124 223 PHE A CD1 
1156  C CD2 . PHE A 214 ? 0.6036 0.3498 0.5511 0.1867  0.0538  -0.0181 223 PHE A CD2 
1157  C CE1 . PHE A 214 ? 0.6462 0.4058 0.5646 0.2495  0.0565  -0.0245 223 PHE A CE1 
1158  C CE2 . PHE A 214 ? 0.6405 0.3548 0.5658 0.1975  0.0531  -0.0299 223 PHE A CE2 
1159  C CZ  . PHE A 214 ? 0.6599 0.3785 0.5696 0.2295  0.0544  -0.0336 223 PHE A CZ  
1160  N N   . GLN A 215 ? 0.5054 0.3553 0.5191 0.1392  0.0531  -0.0045 224 GLN A N   
1161  C CA  . GLN A 215 ? 0.4999 0.3488 0.5197 0.1214  0.0523  -0.0125 224 GLN A CA  
1162  C C   . GLN A 215 ? 0.4581 0.3562 0.4983 0.1140  0.0516  -0.0103 224 GLN A C   
1163  O O   . GLN A 215 ? 0.4506 0.3613 0.4948 0.1099  0.0514  -0.0172 224 GLN A O   
1164  C CB  . GLN A 215 ? 0.5028 0.3256 0.5232 0.0996  0.0512  -0.0113 224 GLN A CB  
1165  C CG  . GLN A 215 ? 0.5709 0.3497 0.5726 0.1040  0.0511  -0.0086 224 GLN A CG  
1166  C CD  . GLN A 215 ? 0.6105 0.3687 0.6127 0.0814  0.0500  -0.0060 224 GLN A CD  
1167  O OE1 . GLN A 215 ? 0.5917 0.3746 0.6109 0.0673  0.0498  -0.0010 224 GLN A OE1 
1168  N NE2 . GLN A 215 ? 0.6583 0.3704 0.6399 0.0777  0.0488  -0.0090 224 GLN A NE2 
1169  N N   . GLN A 216 ? 0.4348 0.3593 0.4861 0.1114  0.0506  -0.0003 225 GLN A N   
1170  C CA  . GLN A 216 ? 0.4032 0.3696 0.4701 0.1021  0.0485  0.0029  225 GLN A CA  
1171  C C   . GLN A 216 ? 0.4021 0.4001 0.4700 0.1153  0.0491  0.0002  225 GLN A C   
1172  O O   . GLN A 216 ? 0.3799 0.3940 0.4538 0.1076  0.0482  -0.0046 225 GLN A O   
1173  C CB  . GLN A 216 ? 0.3914 0.3773 0.4650 0.0995  0.0467  0.0143  225 GLN A CB  
1174  C CG  . GLN A 216 ? 0.4066 0.3685 0.4802 0.0869  0.0460  0.0176  225 GLN A CG  
1175  C CD  . GLN A 216 ? 0.4103 0.3974 0.4935 0.0751  0.0425  0.0256  225 GLN A CD  
1176  O OE1 . GLN A 216 ? 0.4178 0.4302 0.5033 0.0810  0.0411  0.0333  225 GLN A OE1 
1177  N NE2 . GLN A 216 ? 0.4025 0.3831 0.4895 0.0585  0.0406  0.0237  225 GLN A NE2 
1178  N N   . LYS A 217 ? 0.4226 0.4312 0.4839 0.1364  0.0506  0.0039  226 LYS A N   
1179  C CA  . LYS A 217 ? 0.4252 0.4743 0.4885 0.1509  0.0512  0.0043  226 LYS A CA  
1180  C C   . LYS A 217 ? 0.4421 0.4743 0.4933 0.1642  0.0535  -0.0077 226 LYS A C   
1181  O O   . LYS A 217 ? 0.4384 0.5049 0.4929 0.1712  0.0539  -0.0100 226 LYS A O   
1182  C CB  . LYS A 217 ? 0.4460 0.5140 0.5051 0.1713  0.0523  0.0129  226 LYS A CB  
1183  C CG  . LYS A 217 ? 0.4464 0.5464 0.5179 0.1600  0.0495  0.0259  226 LYS A CG  
1184  C CD  . LYS A 217 ? 0.4976 0.6323 0.5660 0.1832  0.0507  0.0340  226 LYS A CD  
1185  C CE  . LYS A 217 ? 0.5125 0.6760 0.5906 0.1723  0.0476  0.0470  226 LYS A CE  
1186  N NZ  . LYS A 217 ? 0.5516 0.7378 0.6240 0.1969  0.0495  0.0547  226 LYS A NZ  
1187  N N   . ASN A 218 ? 0.4616 0.4412 0.4971 0.1673  0.0547  -0.0151 227 ASN A N   
1188  C CA  . ASN A 218 ? 0.4824 0.4392 0.5031 0.1775  0.0559  -0.0275 227 ASN A CA  
1189  C C   . ASN A 218 ? 0.4744 0.4177 0.5002 0.1553  0.0547  -0.0354 227 ASN A C   
1190  O O   . ASN A 218 ? 0.5007 0.4176 0.5130 0.1588  0.0551  -0.0464 227 ASN A O   
1191  C CB  . ASN A 218 ? 0.5195 0.4260 0.5152 0.1952  0.0568  -0.0314 227 ASN A CB  
1192  C CG  . ASN A 218 ? 0.5407 0.4639 0.5245 0.2274  0.0587  -0.0302 227 ASN A CG  
1193  O OD1 . ASN A 218 ? 0.5415 0.5013 0.5278 0.2402  0.0598  -0.0335 227 ASN A OD1 
1194  N ND2 . ASN A 218 ? 0.5593 0.4592 0.5299 0.2422  0.0591  -0.0248 227 ASN A ND2 
1195  N N   . ASN A 219 ? 0.4403 0.4038 0.4844 0.1332  0.0529  -0.0298 228 ASN A N   
1196  C CA  . ASN A 219 ? 0.4216 0.3735 0.4713 0.1117  0.0517  -0.0352 228 ASN A CA  
1197  C C   . ASN A 219 ? 0.4160 0.3728 0.4624 0.1136  0.0522  -0.0458 228 ASN A C   
1198  O O   . ASN A 219 ? 0.4318 0.3560 0.4681 0.1079  0.0522  -0.0548 228 ASN A O   
1199  C CB  . ASN A 219 ? 0.3920 0.3735 0.4599 0.0937  0.0493  -0.0271 228 ASN A CB  
1200  C CG  . ASN A 219 ? 0.3969 0.3728 0.4706 0.0744  0.0480  -0.0321 228 ASN A CG  
1201  O OD1 . ASN A 219 ? 0.4075 0.4074 0.4874 0.0707  0.0472  -0.0350 228 ASN A OD1 
1202  N ND2 . ASN A 219 ? 0.4191 0.3658 0.4904 0.0622  0.0479  -0.0326 228 ASN A ND2 
1203  N N   . ARG A 220 ? 0.3885 0.3884 0.4432 0.1204  0.0522  -0.0441 229 ARG A N   
1204  C CA  . ARG A 220 ? 0.3762 0.3869 0.4297 0.1213  0.0526  -0.0531 229 ARG A CA  
1205  C C   . ARG A 220 ? 0.4112 0.3849 0.4426 0.1378  0.0543  -0.0646 229 ARG A C   
1206  O O   . ARG A 220 ? 0.4196 0.3713 0.4444 0.1297  0.0538  -0.0744 229 ARG A O   
1207  C CB  . ARG A 220 ? 0.3598 0.4244 0.4230 0.1291  0.0524  -0.0480 229 ARG A CB  
1208  C CG  . ARG A 220 ? 0.3270 0.4150 0.3985 0.1180  0.0514  -0.0518 229 ARG A CG  
1209  C CD  . ARG A 220 ? 0.3100 0.4521 0.3886 0.1268  0.0511  -0.0458 229 ARG A CD  
1210  N NE  . ARG A 220 ? 0.3201 0.4772 0.3967 0.1304  0.0520  -0.0543 229 ARG A NE  
1211  C CZ  . ARG A 220 ? 0.3214 0.5255 0.4010 0.1410  0.0525  -0.0519 229 ARG A CZ  
1212  N NH1 . ARG A 220 ? 0.3119 0.5545 0.3968 0.1487  0.0521  -0.0406 229 ARG A NH1 
1213  N NH2 . ARG A 220 ? 0.3382 0.5533 0.4154 0.1436  0.0533  -0.0603 229 ARG A NH2 
1214  N N   . LEU A 221 ? 0.4317 0.3958 0.4494 0.1609  0.0557  -0.0634 230 LEU A N   
1215  C CA  . LEU A 221 ? 0.4725 0.3946 0.4636 0.1791  0.0564  -0.0745 230 LEU A CA  
1216  C C   . LEU A 221 ? 0.4908 0.3566 0.4695 0.1622  0.0546  -0.0805 230 LEU A C   
1217  O O   . LEU A 221 ? 0.5173 0.3538 0.4796 0.1618  0.0537  -0.0921 230 LEU A O   
1218  C CB  . LEU A 221 ? 0.5008 0.4156 0.4770 0.2068  0.0578  -0.0707 230 LEU A CB  
1219  C CG  . LEU A 221 ? 0.5514 0.4138 0.4936 0.2285  0.0577  -0.0821 230 LEU A CG  
1220  C CD1 . LEU A 221 ? 0.5733 0.4591 0.5063 0.2514  0.0592  -0.0909 230 LEU A CD1 
1221  C CD2 . LEU A 221 ? 0.5902 0.4283 0.5162 0.2489  0.0581  -0.0764 230 LEU A CD2 
1222  N N   . LEU A 222 ? 0.4793 0.3319 0.4650 0.1473  0.0538  -0.0721 231 LEU A N   
1223  C CA  . LEU A 222 ? 0.5007 0.3047 0.4748 0.1304  0.0519  -0.0754 231 LEU A CA  
1224  C C   . LEU A 222 ? 0.4847 0.2940 0.4666 0.1096  0.0508  -0.0822 231 LEU A C   
1225  O O   . LEU A 222 ? 0.5169 0.2900 0.4809 0.1042  0.0492  -0.0916 231 LEU A O   
1226  C CB  . LEU A 222 ? 0.4875 0.2875 0.4715 0.1178  0.0515  -0.0638 231 LEU A CB  
1227  C CG  . LEU A 222 ? 0.5136 0.3038 0.4871 0.1389  0.0524  -0.0573 231 LEU A CG  
1228  C CD1 . LEU A 222 ? 0.5083 0.3195 0.4998 0.1297  0.0525  -0.0443 231 LEU A CD1 
1229  C CD2 . LEU A 222 ? 0.5773 0.3052 0.5200 0.1452  0.0508  -0.0623 231 LEU A CD2 
1230  N N   . GLU A 223 ? 0.4390 0.2926 0.4455 0.0979  0.0512  -0.0771 232 GLU A N   
1231  C CA  . GLU A 223 ? 0.4190 0.2828 0.4343 0.0793  0.0503  -0.0823 232 GLU A CA  
1232  C C   . GLU A 223 ? 0.4360 0.2897 0.4364 0.0881  0.0502  -0.0951 232 GLU A C   
1233  O O   . GLU A 223 ? 0.4571 0.2852 0.4479 0.0752  0.0487  -0.1029 232 GLU A O   
1234  C CB  . GLU A 223 ? 0.3768 0.2892 0.4158 0.0719  0.0502  -0.0756 232 GLU A CB  
1235  C CG  . GLU A 223 ? 0.3847 0.3013 0.4361 0.0578  0.0493  -0.0655 232 GLU A CG  
1236  C CD  . GLU A 223 ? 0.4303 0.3214 0.4795 0.0384  0.0484  -0.0672 232 GLU A CD  
1237  O OE1 . GLU A 223 ? 0.4419 0.3167 0.4826 0.0313  0.0479  -0.0762 232 GLU A OE1 
1238  O OE2 . GLU A 223 ? 0.4323 0.3234 0.4884 0.0298  0.0479  -0.0590 232 GLU A OE2 
1239  N N   . ILE A 224 ? 0.4309 0.3056 0.4281 0.1101  0.0517  -0.0972 233 ILE A N   
1240  C CA  . ILE A 224 ? 0.4525 0.3190 0.4337 0.1217  0.0518  -0.1098 233 ILE A CA  
1241  C C   . ILE A 224 ? 0.5032 0.3078 0.4543 0.1242  0.0499  -0.1188 233 ILE A C   
1242  O O   . ILE A 224 ? 0.5195 0.3025 0.4593 0.1135  0.0480  -0.1289 233 ILE A O   
1243  C CB  . ILE A 224 ? 0.4560 0.3540 0.4351 0.1491  0.0539  -0.1097 233 ILE A CB  
1244  C CG1 . ILE A 224 ? 0.3995 0.3575 0.4066 0.1435  0.0547  -0.0983 233 ILE A CG1 
1245  C CG2 . ILE A 224 ? 0.4796 0.3733 0.4424 0.1613  0.0540  -0.1235 233 ILE A CG2 
1246  C CD1 . ILE A 224 ? 0.3978 0.4009 0.4074 0.1623  0.0564  -0.0987 233 ILE A CD1 
1247  N N   . THR A 225 ? 0.5302 0.3057 0.4668 0.1373  0.0498  -0.1148 234 THR A N   
1248  C CA  . THR A 225 ? 0.5888 0.2993 0.4925 0.1401  0.0470  -0.1218 234 THR A CA  
1249  C C   . THR A 225 ? 0.6008 0.2812 0.5000 0.1100  0.0438  -0.1255 234 THR A C   
1250  O O   . THR A 225 ? 0.6468 0.2853 0.5194 0.1080  0.0406  -0.1367 234 THR A O   
1251  C CB  . THR A 225 ? 0.6048 0.2924 0.5002 0.1506  0.0471  -0.1126 234 THR A CB  
1252  O OG1 . THR A 225 ? 0.6076 0.3212 0.5016 0.1816  0.0498  -0.1108 234 THR A OG1 
1253  C CG2 . THR A 225 ? 0.6642 0.2787 0.5232 0.1497  0.0432  -0.1181 234 THR A CG2 
1254  N N   . ARG A 226 ? 0.5658 0.2688 0.4896 0.0869  0.0442  -0.1162 235 ARG A N   
1255  C CA  . ARG A 226 ? 0.5708 0.2575 0.4945 0.0578  0.0415  -0.1177 235 ARG A CA  
1256  C C   . ARG A 226 ? 0.5630 0.2653 0.4883 0.0511  0.0409  -0.1283 235 ARG A C   
1257  O O   . ARG A 226 ? 0.6017 0.2676 0.5036 0.0446  0.0377  -0.1383 235 ARG A O   
1258  C CB  . ARG A 226 ? 0.5292 0.2478 0.4807 0.0405  0.0428  -0.1056 235 ARG A CB  
1259  C CG  . ARG A 226 ? 0.5400 0.2561 0.4960 0.0119  0.0408  -0.1056 235 ARG A CG  
1260  C CD  . ARG A 226 ? 0.5185 0.2806 0.5046 0.0014  0.0428  -0.0959 235 ARG A CD  
1261  N NE  . ARG A 226 ? 0.5052 0.2774 0.5010 0.0120  0.0445  -0.0853 235 ARG A NE  
1262  C CZ  . ARG A 226 ? 0.4877 0.2382 0.4783 0.0071  0.0439  -0.0777 235 ARG A CZ  
1263  N NH1 . ARG A 226 ? 0.4963 0.2143 0.4721 -0.0095 0.0414  -0.0788 235 ARG A NH1 
1264  N NH2 . ARG A 226 ? 0.4576 0.2205 0.4572 0.0176  0.0455  -0.0685 235 ARG A NH2 
1265  N N   . GLU A 227 ? 0.5166 0.2718 0.4678 0.0525  0.0436  -0.1258 236 GLU A N   
1266  C CA  . GLU A 227 ? 0.5079 0.2857 0.4638 0.0479  0.0435  -0.1344 236 GLU A CA  
1267  C C   . GLU A 227 ? 0.5492 0.2887 0.4743 0.0577  0.0413  -0.1486 236 GLU A C   
1268  O O   . GLU A 227 ? 0.5637 0.2900 0.4797 0.0425  0.0387  -0.1568 236 GLU A O   
1269  C CB  . GLU A 227 ? 0.4754 0.3072 0.4530 0.0610  0.0464  -0.1304 236 GLU A CB  
1270  C CG  . GLU A 227 ? 0.4705 0.3428 0.4684 0.0465  0.0466  -0.1307 236 GLU A CG  
1271  C CD  . GLU A 227 ? 0.4688 0.3927 0.4873 0.0563  0.0485  -0.1236 236 GLU A CD  
1272  O OE1 . GLU A 227 ? 0.4917 0.4438 0.5150 0.0586  0.0489  -0.1284 236 GLU A OE1 
1273  O OE2 . GLU A 227 ? 0.4279 0.3642 0.4566 0.0603  0.0493  -0.1129 236 GLU A OE2 
1274  N N   . PHE A 228 ? 0.5743 0.2939 0.4806 0.0838  0.0418  -0.1514 237 PHE A N   
1275  C CA  . PHE A 228 ? 0.6240 0.3044 0.4968 0.0975  0.0394  -0.1658 237 PHE A CA  
1276  C C   . PHE A 228 ? 0.6706 0.2848 0.5127 0.0820  0.0342  -0.1708 237 PHE A C   
1277  O O   . PHE A 228 ? 0.7042 0.2900 0.5236 0.0761  0.0306  -0.1831 237 PHE A O   
1278  C CB  . PHE A 228 ? 0.6474 0.3272 0.5064 0.1335  0.0415  -0.1676 237 PHE A CB  
1279  C CG  . PHE A 228 ? 0.6292 0.3674 0.5052 0.1502  0.0452  -0.1692 237 PHE A CG  
1280  C CD1 . PHE A 228 ? 0.6124 0.3942 0.5060 0.1686  0.0489  -0.1592 237 PHE A CD1 
1281  C CD2 . PHE A 228 ? 0.6418 0.3934 0.5158 0.1464  0.0446  -0.1800 237 PHE A CD2 
1282  C CE1 . PHE A 228 ? 0.5944 0.4327 0.5029 0.1816  0.0517  -0.1593 237 PHE A CE1 
1283  C CE2 . PHE A 228 ? 0.6176 0.4252 0.5070 0.1609  0.0478  -0.1805 237 PHE A CE2 
1284  C CZ  . PHE A 228 ? 0.5936 0.4452 0.5004 0.1778  0.0512  -0.1696 237 PHE A CZ  
1285  N N   . SER A 229 ? 0.6741 0.2640 0.5143 0.0742  0.0332  -0.1610 238 SER A N   
1286  C CA  . SER A 229 ? 0.7195 0.2486 0.5317 0.0553  0.0276  -0.1627 238 SER A CA  
1287  C C   . SER A 229 ? 0.7062 0.2431 0.5259 0.0215  0.0249  -0.1648 238 SER A C   
1288  O O   . SER A 229 ? 0.7539 0.2436 0.5452 0.0050  0.0192  -0.1714 238 SER A O   
1289  C CB  . SER A 229 ? 0.7161 0.2327 0.5332 0.0505  0.0279  -0.1488 238 SER A CB  
1290  O OG  . SER A 229 ? 0.7438 0.2466 0.5490 0.0812  0.0296  -0.1467 238 SER A OG  
1291  N N   . VAL A 230 ? 0.6426 0.2391 0.4991 0.0111  0.0286  -0.1590 239 VAL A N   
1292  C CA  . VAL A 230 ? 0.6262 0.2367 0.4923 -0.0193 0.0266  -0.1590 239 VAL A CA  
1293  C C   . VAL A 230 ? 0.6320 0.2554 0.4942 -0.0188 0.0259  -0.1716 239 VAL A C   
1294  O O   . VAL A 230 ? 0.6398 0.2679 0.5023 -0.0429 0.0232  -0.1746 239 VAL A O   
1295  C CB  . VAL A 230 ? 0.5607 0.2256 0.4644 -0.0294 0.0304  -0.1472 239 VAL A CB  
1296  C CG1 . VAL A 230 ? 0.5605 0.2337 0.4699 -0.0609 0.0279  -0.1450 239 VAL A CG1 
1297  C CG2 . VAL A 230 ? 0.5575 0.2186 0.4682 -0.0225 0.0322  -0.1354 239 VAL A CG2 
1298  N N   . ASN A 231 ? 0.6343 0.2677 0.4931 0.0084  0.0283  -0.1785 240 ASN A N   
1299  C CA  . ASN A 231 ? 0.6358 0.2869 0.4925 0.0101  0.0280  -0.1901 240 ASN A CA  
1300  C C   . ASN A 231 ? 0.6922 0.2985 0.5107 0.0292  0.0250  -0.2051 240 ASN A C   
1301  O O   . ASN A 231 ? 0.6917 0.3149 0.5070 0.0375  0.0254  -0.2155 240 ASN A O   
1302  C CB  . ASN A 231 ? 0.5826 0.2993 0.4731 0.0213  0.0333  -0.1852 240 ASN A CB  
1303  C CG  . ASN A 231 ? 0.5494 0.3068 0.4713 -0.0013 0.0346  -0.1748 240 ASN A CG  
1304  O OD1 . ASN A 231 ? 0.5566 0.3309 0.4846 -0.0189 0.0334  -0.1784 240 ASN A OD1 
1305  N ND2 . ASN A 231 ? 0.5505 0.3234 0.4911 -0.0002 0.0370  -0.1618 240 ASN A ND2 
1306  N N   . ALA A 232 ? 0.7418 0.2892 0.5291 0.0367  0.0217  -0.2062 241 ALA A N   
1307  C CA  . ALA A 232 ? 0.8042 0.3023 0.5502 0.0585  0.0184  -0.2204 241 ALA A CA  
1308  C C   . ALA A 232 ? 0.7885 0.3271 0.5435 0.0932  0.0237  -0.2247 241 ALA A C   
1309  O O   . ALA A 232 ? 0.8191 0.3497 0.5539 0.1069  0.0224  -0.2385 241 ALA A O   
1310  C CB  . ALA A 232 ? 0.8400 0.3093 0.5625 0.0380  0.0125  -0.2331 241 ALA A CB  
1311  N N   . GLY A 233 ? 0.7429 0.3282 0.5284 0.1061  0.0293  -0.2124 242 GLY A N   
1312  C CA  . GLY A 233 ? 0.7272 0.3537 0.5210 0.1388  0.0341  -0.2135 242 GLY A CA  
1313  C C   . GLY A 233 ? 0.6872 0.3740 0.5041 0.1391  0.0371  -0.2167 242 GLY A C   
1314  O O   . GLY A 233 ? 0.6981 0.4086 0.5100 0.1664  0.0395  -0.2222 242 GLY A O   
1315  N N   . VAL A 234 ? 0.6459 0.3596 0.4871 0.1098  0.0368  -0.2131 243 VAL A N   
1316  C CA  . VAL A 234 ? 0.6040 0.3775 0.4697 0.1087  0.0396  -0.2136 243 VAL A CA  
1317  C C   . VAL A 234 ? 0.5560 0.3639 0.4551 0.0800  0.0403  -0.2024 243 VAL A C   
1318  O O   . VAL A 234 ? 0.5689 0.3507 0.4639 0.0556  0.0372  -0.2026 243 VAL A O   
1319  C CB  . VAL A 234 ? 0.6284 0.3887 0.4733 0.1072  0.0369  -0.2296 243 VAL A CB  
1320  C CG1 . VAL A 234 ? 0.6030 0.4184 0.4614 0.1253  0.0405  -0.2316 243 VAL A CG1 
1321  C CG2 . VAL A 234 ? 0.7004 0.3935 0.4996 0.1225  0.0329  -0.2429 243 VAL A CG2 
1322  N N   . THR A 235 ? 0.5086 0.3743 0.4384 0.0824  0.0438  -0.1926 244 THR A N   
1323  C CA  . THR A 235 ? 0.4709 0.3668 0.4293 0.0578  0.0440  -0.1822 244 THR A CA  
1324  C C   . THR A 235 ? 0.4318 0.3812 0.4111 0.0546  0.0454  -0.1807 244 THR A C   
1325  O O   . THR A 235 ? 0.4261 0.4055 0.4083 0.0729  0.0474  -0.1811 244 THR A O   
1326  C CB  . THR A 235 ? 0.4477 0.3586 0.4251 0.0585  0.0458  -0.1672 244 THR A CB  
1327  O OG1 . THR A 235 ? 0.4731 0.3693 0.4380 0.0821  0.0471  -0.1663 244 THR A OG1 
1328  C CG2 . THR A 235 ? 0.4581 0.3484 0.4409 0.0348  0.0441  -0.1608 244 THR A CG2 
1329  N N   . THR A 236 ? 0.4050 0.3690 0.3988 0.0320  0.0443  -0.1777 245 THR A N   
1330  C CA  . THR A 236 ? 0.3691 0.3842 0.3856 0.0281  0.0454  -0.1715 245 THR A CA  
1331  C C   . THR A 236 ? 0.3364 0.3630 0.3724 0.0145  0.0453  -0.1581 245 THR A C   
1332  O O   . THR A 236 ? 0.3478 0.3458 0.3798 0.0049  0.0444  -0.1558 245 THR A O   
1333  C CB  . THR A 236 ? 0.3762 0.4042 0.3901 0.0195  0.0443  -0.1808 245 THR A CB  
1334  O OG1 . THR A 236 ? 0.4272 0.4561 0.4257 0.0387  0.0450  -0.1913 245 THR A OG1 
1335  C CG2 . THR A 236 ? 0.3393 0.4160 0.3766 0.0112  0.0447  -0.1727 245 THR A CG2 
1336  N N   . PRO A 237 ? 0.3023 0.3699 0.3574 0.0118  0.0456  -0.1496 246 PRO A N   
1337  C CA  . PRO A 237 ? 0.2690 0.3598 0.3385 0.0160  0.0460  -0.1367 246 PRO A CA  
1338  C C   . PRO A 237 ? 0.2792 0.3586 0.3408 0.0336  0.0475  -0.1358 246 PRO A C   
1339  O O   . PRO A 237 ? 0.3103 0.3520 0.3578 0.0375  0.0477  -0.1404 246 PRO A O   
1340  C CB  . PRO A 237 ? 0.2563 0.3365 0.3341 0.0007  0.0448  -0.1287 246 PRO A CB  
1341  C CG  . PRO A 237 ? 0.2714 0.3468 0.3470 -0.0138 0.0439  -0.1353 246 PRO A CG  
1342  C CD  . PRO A 237 ? 0.2968 0.3704 0.3599 -0.0077 0.0442  -0.1482 246 PRO A CD  
1343  N N   . VAL A 238 ? 0.2565 0.3698 0.3261 0.0439  0.0480  -0.1289 247 VAL A N   
1344  C CA  . VAL A 238 ? 0.2593 0.3713 0.3243 0.0609  0.0494  -0.1253 247 VAL A CA  
1345  C C   . VAL A 238 ? 0.2369 0.3503 0.3142 0.0514  0.0482  -0.1120 247 VAL A C   
1346  O O   . VAL A 238 ? 0.2084 0.3523 0.2993 0.0435  0.0464  -0.1020 247 VAL A O   
1347  C CB  . VAL A 238 ? 0.2507 0.4047 0.3181 0.0755  0.0504  -0.1243 247 VAL A CB  
1348  C CG1 . VAL A 238 ? 0.2642 0.4284 0.3307 0.0913  0.0516  -0.1172 247 VAL A CG1 
1349  C CG2 . VAL A 238 ? 0.2745 0.4203 0.3255 0.0879  0.0518  -0.1391 247 VAL A CG2 
1350  N N   . SER A 239 ? 0.2518 0.3294 0.3225 0.0509  0.0485  -0.1119 248 SER A N   
1351  C CA  . SER A 239 ? 0.2367 0.3115 0.3175 0.0400  0.0471  -0.1008 248 SER A CA  
1352  C C   . SER A 239 ? 0.2262 0.3318 0.3157 0.0466  0.0465  -0.0897 248 SER A C   
1353  O O   . SER A 239 ? 0.2346 0.3607 0.3211 0.0618  0.0478  -0.0904 248 SER A O   
1354  C CB  . SER A 239 ? 0.2590 0.2934 0.3298 0.0415  0.0479  -0.1019 248 SER A CB  
1355  O OG  . SER A 239 ? 0.2769 0.3089 0.3407 0.0600  0.0493  -0.1001 248 SER A OG  
1356  N N   . THR A 240 ? 0.2123 0.3212 0.3109 0.0355  0.0444  -0.0793 249 THR A N   
1357  C CA  . THR A 240 ? 0.2027 0.3376 0.3077 0.0383  0.0427  -0.0677 249 THR A CA  
1358  C C   . THR A 240 ? 0.2184 0.3408 0.3169 0.0533  0.0449  -0.0666 249 THR A C   
1359  O O   . THR A 240 ? 0.2166 0.3620 0.3190 0.0582  0.0440  -0.0576 249 THR A O   
1360  C CB  . THR A 240 ? 0.1846 0.3197 0.2968 0.0226  0.0390  -0.0577 249 THR A CB  
1361  O OG1 . THR A 240 ? 0.2025 0.3062 0.3117 0.0213  0.0398  -0.0570 249 THR A OG1 
1362  C CG2 . THR A 240 ? 0.1731 0.3103 0.2884 0.0094  0.0370  -0.0596 249 THR A CG2 
1363  N N   . TYR A 241 ? 0.2386 0.3242 0.3260 0.0596  0.0472  -0.0750 250 TYR A N   
1364  C CA  . TYR A 241 ? 0.2604 0.3324 0.3384 0.0766  0.0491  -0.0746 250 TYR A CA  
1365  C C   . TYR A 241 ? 0.2790 0.3634 0.3470 0.0975  0.0512  -0.0819 250 TYR A C   
1366  O O   . TYR A 241 ? 0.2892 0.3845 0.3526 0.1155  0.0526  -0.0786 250 TYR A O   
1367  C CB  . TYR A 241 ? 0.2879 0.3110 0.3546 0.0743  0.0498  -0.0793 250 TYR A CB  
1368  C CG  . TYR A 241 ? 0.2916 0.3011 0.3659 0.0559  0.0482  -0.0733 250 TYR A CG  
1369  C CD1 . TYR A 241 ? 0.3267 0.3080 0.3962 0.0432  0.0479  -0.0791 250 TYR A CD1 
1370  C CD2 . TYR A 241 ? 0.3107 0.3363 0.3953 0.0515  0.0467  -0.0616 250 TYR A CD2 
1371  C CE1 . TYR A 241 ? 0.3380 0.3113 0.4140 0.0281  0.0468  -0.0734 250 TYR A CE1 
1372  C CE2 . TYR A 241 ? 0.3297 0.3424 0.4190 0.0369  0.0452  -0.0568 250 TYR A CE2 
1373  C CZ  . TYR A 241 ? 0.3337 0.3219 0.4192 0.0262  0.0456  -0.0627 250 TYR A CZ  
1374  O OH  . TYR A 241 ? 0.3272 0.3078 0.4171 0.0137  0.0445  -0.0577 250 TYR A OH  
1375  N N   . MET A 242 ? 0.2852 0.3689 0.3483 0.0969  0.0516  -0.0921 251 MET A N   
1376  C CA  . MET A 242 ? 0.3082 0.4048 0.3602 0.1183  0.0536  -0.0996 251 MET A CA  
1377  C C   . MET A 242 ? 0.2895 0.4445 0.3548 0.1224  0.0534  -0.0905 251 MET A C   
1378  O O   . MET A 242 ? 0.3033 0.4812 0.3635 0.1433  0.0551  -0.0891 251 MET A O   
1379  C CB  . MET A 242 ? 0.3221 0.4039 0.3650 0.1151  0.0536  -0.1129 251 MET A CB  
1380  C CG  . MET A 242 ? 0.3525 0.3780 0.3801 0.1079  0.0529  -0.1219 251 MET A CG  
1381  S SD  . MET A 242 ? 0.4081 0.3891 0.4059 0.1341  0.0539  -0.1303 251 MET A SD  
1382  C CE  . MET A 242 ? 0.4348 0.3571 0.4123 0.1194  0.0515  -0.1431 251 MET A CE  
1383  N N   . LEU A 243 ? 0.2641 0.4440 0.3450 0.1023  0.0509  -0.0836 252 LEU A N   
1384  C CA  . LEU A 243 ? 0.2451 0.4791 0.3376 0.1006  0.0494  -0.0734 252 LEU A CA  
1385  C C   . LEU A 243 ? 0.2243 0.4654 0.3292 0.0793  0.0455  -0.0608 252 LEU A C   
1386  O O   . LEU A 243 ? 0.2181 0.4361 0.3259 0.0627  0.0437  -0.0619 252 LEU A O   
1387  C CB  . LEU A 243 ? 0.2385 0.4962 0.3333 0.0967  0.0492  -0.0786 252 LEU A CB  
1388  C CG  . LEU A 243 ? 0.2527 0.5418 0.3406 0.1186  0.0518  -0.0835 252 LEU A CG  
1389  C CD1 . LEU A 243 ? 0.2405 0.5716 0.3379 0.1080  0.0501  -0.0799 252 LEU A CD1 
1390  C CD2 . LEU A 243 ? 0.2714 0.5888 0.3612 0.1314  0.0524  -0.0735 252 LEU A CD2 
1391  N N   . THR A 244 ? 0.2170 0.4910 0.3278 0.0802  0.0438  -0.0486 253 THR A N   
1392  C CA  . THR A 244 ? 0.2028 0.4854 0.3221 0.0594  0.0388  -0.0361 253 THR A CA  
1393  C C   . THR A 244 ? 0.1908 0.5066 0.3158 0.0464  0.0354  -0.0314 253 THR A C   
1394  O O   . THR A 244 ? 0.2014 0.5475 0.3262 0.0558  0.0372  -0.0346 253 THR A O   
1395  C CB  . THR A 244 ? 0.2027 0.5134 0.3247 0.0634  0.0374  -0.0243 253 THR A CB  
1396  O OG1 . THR A 244 ? 0.2289 0.5132 0.3444 0.0796  0.0410  -0.0281 253 THR A OG1 
1397  C CG2 . THR A 244 ? 0.1924 0.5061 0.3193 0.0405  0.0311  -0.0117 253 THR A CG2 
1398  N N   . ASN A 245 ? 0.1791 0.4892 0.3073 0.0256  0.0302  -0.0235 254 ASN A N   
1399  C CA  . ASN A 245 ? 0.1759 0.5153 0.3071 0.0112  0.0256  -0.0166 254 ASN A CA  
1400  C C   . ASN A 245 ? 0.1767 0.5709 0.3110 0.0148  0.0244  -0.0067 254 ASN A C   
1401  O O   . ASN A 245 ? 0.1712 0.5996 0.3073 0.0183  0.0254  -0.0079 254 ASN A O   
1402  C CB  . ASN A 245 ? 0.1721 0.4915 0.3015 -0.0097 0.0192  -0.0083 254 ASN A CB  
1403  C CG  . ASN A 245 ? 0.1729 0.5127 0.3016 -0.0259 0.0135  -0.0013 254 ASN A CG  
1404  O OD1 . ASN A 245 ? 0.1827 0.5149 0.3111 -0.0278 0.0144  -0.0081 254 ASN A OD1 
1405  N ND2 . ASN A 245 ? 0.1680 0.5326 0.2949 -0.0393 0.0071  0.0130  254 ASN A ND2 
1406  N N   . SER A 246 ? 0.1815 0.5871 0.3163 0.0144  0.0225  0.0031  255 SER A N   
1407  C CA  . SER A 246 ? 0.1847 0.6470 0.3227 0.0173  0.0212  0.0141  255 SER A CA  
1408  C C   . SER A 246 ? 0.1853 0.6729 0.3234 0.0414  0.0277  0.0049  255 SER A C   
1409  O O   . SER A 246 ? 0.1888 0.7245 0.3298 0.0404  0.0268  0.0099  255 SER A O   
1410  C CB  . SER A 246 ? 0.1952 0.6615 0.3331 0.0204  0.0204  0.0222  255 SER A CB  
1411  O OG  . SER A 246 ? 0.2336 0.6482 0.3681 0.0114  0.0185  0.0206  255 SER A OG  
1412  N N   . GLU A 247 ? 0.1878 0.6416 0.3207 0.0622  0.0338  -0.0087 256 GLU A N   
1413  C CA  . GLU A 247 ? 0.1997 0.6714 0.3278 0.0874  0.0395  -0.0186 256 GLU A CA  
1414  C C   . GLU A 247 ? 0.1915 0.6715 0.3198 0.0838  0.0399  -0.0259 256 GLU A C   
1415  O O   . GLU A 247 ? 0.1930 0.7208 0.3226 0.0919  0.0408  -0.0242 256 GLU A O   
1416  C CB  . GLU A 247 ? 0.2208 0.6460 0.3389 0.1081  0.0445  -0.0312 256 GLU A CB  
1417  C CG  . GLU A 247 ? 0.2520 0.6750 0.3693 0.1156  0.0446  -0.0236 256 GLU A CG  
1418  C CD  . GLU A 247 ? 0.2999 0.6656 0.4063 0.1297  0.0482  -0.0343 256 GLU A CD  
1419  O OE1 . GLU A 247 ? 0.3316 0.6521 0.4330 0.1243  0.0490  -0.0453 256 GLU A OE1 
1420  O OE2 . GLU A 247 ? 0.3078 0.6744 0.4098 0.1452  0.0498  -0.0306 256 GLU A OE2 
1421  N N   . LEU A 248 ? 0.1851 0.6221 0.3124 0.0713  0.0390  -0.0333 257 LEU A N   
1422  C CA  . LEU A 248 ? 0.1770 0.6189 0.3041 0.0678  0.0395  -0.0409 257 LEU A CA  
1423  C C   . LEU A 248 ? 0.1665 0.6623 0.3008 0.0547  0.0354  -0.0282 257 LEU A C   
1424  O O   . LEU A 248 ? 0.1687 0.6995 0.3027 0.0631  0.0372  -0.0313 257 LEU A O   
1425  C CB  . LEU A 248 ? 0.1666 0.5604 0.2931 0.0523  0.0381  -0.0472 257 LEU A CB  
1426  C CG  . LEU A 248 ? 0.1321 0.5331 0.2598 0.0438  0.0373  -0.0524 257 LEU A CG  
1427  C CD1 . LEU A 248 ? 0.1160 0.5233 0.2372 0.0621  0.0420  -0.0663 257 LEU A CD1 
1428  C CD2 . LEU A 248 ? 0.1063 0.4649 0.2337 0.0297  0.0357  -0.0560 257 LEU A CD2 
1429  N N   . LEU A 249 ? 0.1580 0.6596 0.2966 0.0339  0.0294  -0.0136 258 LEU A N   
1430  C CA  . LEU A 249 ? 0.1561 0.7021 0.2988 0.0159  0.0237  0.0003  258 LEU A CA  
1431  C C   . LEU A 249 ? 0.1615 0.7735 0.3071 0.0269  0.0251  0.0071  258 LEU A C   
1432  O O   . LEU A 249 ? 0.1532 0.8034 0.3011 0.0206  0.0235  0.0111  258 LEU A O   
1433  C CB  . LEU A 249 ? 0.1512 0.6847 0.2933 -0.0075 0.0163  0.0143  258 LEU A CB  
1434  C CG  . LEU A 249 ? 0.1520 0.6487 0.2908 -0.0244 0.0125  0.0121  258 LEU A CG  
1435  C CD1 . LEU A 249 ? 0.1682 0.6330 0.3021 -0.0414 0.0064  0.0203  258 LEU A CD1 
1436  C CD2 . LEU A 249 ? 0.1779 0.7127 0.3173 -0.0376 0.0083  0.0203  258 LEU A CD2 
1437  N N   . SER A 250 ? 0.1750 0.8024 0.3203 0.0439  0.0281  0.0087  259 SER A N   
1438  C CA  . SER A 250 ? 0.1837 0.8782 0.3311 0.0590  0.0302  0.0147  259 SER A CA  
1439  C C   . SER A 250 ? 0.1919 0.8931 0.3341 0.0870  0.0373  -0.0012 259 SER A C   
1440  O O   . SER A 250 ? 0.1948 0.9544 0.3387 0.0957  0.0385  0.0024  259 SER A O   
1441  C CB  . SER A 250 ? 0.1915 0.9075 0.3396 0.0686  0.0306  0.0236  259 SER A CB  
1442  O OG  . SER A 250 ? 0.2087 0.9086 0.3502 0.1016  0.0379  0.0108  259 SER A OG  
1443  N N   . LEU A 251 ? 0.1969 0.8390 0.3315 0.1000  0.0414  -0.0182 260 LEU A N   
1444  C CA  . LEU A 251 ? 0.2086 0.8448 0.3344 0.1237  0.0469  -0.0348 260 LEU A CA  
1445  C C   . LEU A 251 ? 0.2008 0.8602 0.3301 0.1120  0.0454  -0.0357 260 LEU A C   
1446  O O   . LEU A 251 ? 0.2076 0.9054 0.3334 0.1291  0.0485  -0.0405 260 LEU A O   
1447  C CB  . LEU A 251 ? 0.2215 0.7850 0.3377 0.1301  0.0494  -0.0506 260 LEU A CB  
1448  C CG  . LEU A 251 ? 0.2491 0.7944 0.3526 0.1600  0.0540  -0.0588 260 LEU A CG  
1449  C CD1 . LEU A 251 ? 0.2781 0.7513 0.3698 0.1625  0.0557  -0.0753 260 LEU A CD1 
1450  C CD2 . LEU A 251 ? 0.2586 0.8511 0.3542 0.1890  0.0579  -0.0633 260 LEU A CD2 
1451  N N   . ILE A 252 ? 0.1909 0.8271 0.3259 0.0843  0.0407  -0.0311 261 ILE A N   
1452  C CA  . ILE A 252 ? 0.1885 0.8467 0.3271 0.0701  0.0383  -0.0295 261 ILE A CA  
1453  C C   . ILE A 252 ? 0.1941 0.9260 0.3382 0.0676  0.0363  -0.0147 261 ILE A C   
1454  O O   . ILE A 252 ? 0.2014 0.9729 0.3447 0.0779  0.0386  -0.0181 261 ILE A O   
1455  C CB  . ILE A 252 ? 0.1723 0.8004 0.3148 0.0408  0.0323  -0.0223 261 ILE A CB  
1456  C CG1 . ILE A 252 ? 0.1814 0.7477 0.3191 0.0422  0.0346  -0.0378 261 ILE A CG1 
1457  C CG2 . ILE A 252 ? 0.1536 0.8187 0.2998 0.0233  0.0280  -0.0130 261 ILE A CG2 
1458  C CD1 . ILE A 252 ? 0.1772 0.6987 0.3159 0.0226  0.0303  -0.0326 261 ILE A CD1 
1459  N N   . ASN A 253 ? 0.1995 0.9521 0.3484 0.0537  0.0317  0.0021  262 ASN A N   
1460  C CA  . ASN A 253 ? 0.2064 1.0335 0.3604 0.0482  0.0289  0.0187  262 ASN A CA  
1461  C C   . ASN A 253 ? 0.2207 1.0991 0.3727 0.0783  0.0354  0.0120  262 ASN A C   
1462  O O   . ASN A 253 ? 0.2203 1.1562 0.3757 0.0741  0.0342  0.0195  262 ASN A O   
1463  C CB  . ASN A 253 ? 0.2046 1.0458 0.3611 0.0402  0.0254  0.0332  262 ASN A CB  
1464  C CG  . ASN A 253 ? 0.2065 1.1023 0.3674 0.0136  0.0178  0.0548  262 ASN A CG  
1465  O OD1 . ASN A 253 ? 0.2124 1.1402 0.3747 0.0024  0.0154  0.0597  262 ASN A OD1 
1466  N ND2 . ASN A 253 ? 0.2392 1.1451 0.4011 0.0010  0.0132  0.0684  262 ASN A ND2 
1467  N N   . ASP A 254 ? 0.2420 1.0971 0.3865 0.1091  0.0419  -0.0022 263 ASP A N   
1468  C CA  . ASP A 254 ? 0.2605 1.1586 0.3986 0.1435  0.0480  -0.0096 263 ASP A CA  
1469  C C   . ASP A 254 ? 0.2680 1.1604 0.3990 0.1565  0.0516  -0.0258 263 ASP A C   
1470  O O   . ASP A 254 ? 0.2808 1.2180 0.4059 0.1827  0.0559  -0.0307 263 ASP A O   
1471  C CB  . ASP A 254 ? 0.2839 1.1534 0.4126 0.1720  0.0526  -0.0179 263 ASP A CB  
1472  C CG  . ASP A 254 ? 0.3234 1.2235 0.4399 0.2125  0.0591  -0.0286 263 ASP A CG  
1473  O OD1 . ASP A 254 ? 0.3594 1.3376 0.4800 0.2209  0.0597  -0.0186 263 ASP A OD1 
1474  O OD2 . ASP A 254 ? 0.3582 1.2040 0.4590 0.2365  0.0632  -0.0469 263 ASP A OD2 
1475  N N   . MET A 255 ? 0.2628 1.1044 0.3938 0.1388  0.0498  -0.0336 264 MET A N   
1476  C CA  . MET A 255 ? 0.2718 1.1055 0.3958 0.1485  0.0526  -0.0491 264 MET A CA  
1477  C C   . MET A 255 ? 0.2634 1.1694 0.3934 0.1437  0.0516  -0.0406 264 MET A C   
1478  O O   . MET A 255 ? 0.2466 1.1890 0.3878 0.1175  0.0462  -0.0220 264 MET A O   
1479  C CB  . MET A 255 ? 0.2654 1.0333 0.3893 0.1288  0.0505  -0.0574 264 MET A CB  
1480  C CG  . MET A 255 ? 0.2812 0.9797 0.3985 0.1330  0.0516  -0.0663 264 MET A CG  
1481  S SD  . MET A 255 ? 0.2696 0.8988 0.3866 0.1110  0.0494  -0.0760 264 MET A SD  
1482  C CE  . MET A 255 ? 0.2688 0.9413 0.3975 0.0848  0.0445  -0.0627 264 MET A CE  
1483  N N   . PRO A 256 ? 0.2796 1.2055 0.4000 0.1690  0.0563  -0.0541 265 PRO A N   
1484  C CA  . PRO A 256 ? 0.2772 1.2748 0.4021 0.1686  0.0562  -0.0472 265 PRO A CA  
1485  C C   . PRO A 256 ? 0.2626 1.2554 0.3941 0.1411  0.0522  -0.0445 265 PRO A C   
1486  O O   . PRO A 256 ? 0.2698 1.2758 0.3959 0.1514  0.0547  -0.0552 265 PRO A O   
1487  C CB  . PRO A 256 ? 0.3084 1.3111 0.4163 0.2081  0.0627  -0.0671 265 PRO A CB  
1488  C CG  . PRO A 256 ? 0.3263 1.2439 0.4205 0.2191  0.0647  -0.0861 265 PRO A CG  
1489  C CD  . PRO A 256 ? 0.3135 1.2025 0.4155 0.2042  0.0620  -0.0751 265 PRO A CD  
1490  N N   . ILE A 257 ? 0.2505 1.2263 0.3919 0.1076  0.0460  -0.0298 266 ILE A N   
1491  C CA  . ILE A 257 ? 0.2468 1.2099 0.3926 0.0808  0.0415  -0.0263 266 ILE A CA  
1492  C C   . ILE A 257 ? 0.2338 1.2366 0.3889 0.0490  0.0339  -0.0015 266 ILE A C   
1493  O O   . ILE A 257 ? 0.2311 1.2634 0.3900 0.0425  0.0311  0.0138  266 ILE A O   
1494  C CB  . ILE A 257 ? 0.2451 1.1269 0.3883 0.0700  0.0404  -0.0365 266 ILE A CB  
1495  C CG1 . ILE A 257 ? 0.2418 1.0888 0.3867 0.0632  0.0383  -0.0299 266 ILE A CG1 
1496  C CG2 . ILE A 257 ? 0.2675 1.1097 0.3996 0.0937  0.0463  -0.0611 266 ILE A CG2 
1497  C CD1 . ILE A 257 ? 0.2339 1.0195 0.3795 0.0424  0.0345  -0.0304 266 ILE A CD1 
1498  N N   . THR A 258 ? 0.2273 1.2282 0.3840 0.0284  0.0299  0.0026  267 THR A N   
1499  C CA  . THR A 258 ? 0.2193 1.2550 0.3805 -0.0029 0.0216  0.0261  267 THR A CA  
1500  C C   . THR A 258 ? 0.2155 1.2089 0.3762 -0.0240 0.0154  0.0371  267 THR A C   
1501  O O   . THR A 258 ? 0.2170 1.1604 0.3758 -0.0130 0.0184  0.0262  267 THR A O   
1502  C CB  . THR A 258 ? 0.2148 1.2497 0.3753 -0.0195 0.0183  0.0279  267 THR A CB  
1503  O OG1 . THR A 258 ? 0.2209 1.2072 0.3789 -0.0472 0.0107  0.0373  267 THR A OG1 
1504  C CG2 . THR A 258 ? 0.2201 1.2308 0.3773 0.0020  0.0251  0.0044  267 THR A CG2 
1505  N N   . ASN A 259 ? 0.2140 1.2264 0.3745 -0.0544 0.0064  0.0587  268 ASN A N   
1506  C CA  . ASN A 259 ? 0.2164 1.1918 0.3735 -0.0746 -0.0003 0.0698  268 ASN A CA  
1507  C C   . ASN A 259 ? 0.2169 1.1188 0.3676 -0.0886 -0.0044 0.0657  268 ASN A C   
1508  O O   . ASN A 259 ? 0.2183 1.0730 0.3659 -0.0915 -0.0060 0.0645  268 ASN A O   
1509  C CB  . ASN A 259 ? 0.2226 1.2473 0.3783 -0.1021 -0.0094 0.0953  268 ASN A CB  
1510  C CG  . ASN A 259 ? 0.2345 1.3016 0.3947 -0.0936 -0.0078 0.1022  268 ASN A CG  
1511  O OD1 . ASN A 259 ? 0.2520 1.3207 0.4163 -0.0631 0.0010  0.0876  268 ASN A OD1 
1512  N ND2 . ASN A 259 ? 0.2521 1.3524 0.4097 -0.1207 -0.0166 0.1246  268 ASN A ND2 
1513  N N   . ASP A 260 ? 0.2168 1.1115 0.3648 -0.0965 -0.0061 0.0643  269 ASP A N   
1514  C CA  . ASP A 260 ? 0.2181 1.0460 0.3595 -0.1051 -0.0089 0.0584  269 ASP A CA  
1515  C C   . ASP A 260 ? 0.2059 0.9896 0.3501 -0.0816 -0.0006 0.0360  269 ASP A C   
1516  O O   . ASP A 260 ? 0.2091 0.9364 0.3493 -0.0847 -0.0018 0.0316  269 ASP A O   
1517  C CB  . ASP A 260 ? 0.2236 1.0604 0.3619 -0.1147 -0.0116 0.0608  269 ASP A CB  
1518  C CG  . ASP A 260 ? 0.2614 1.1324 0.3933 -0.1422 -0.0215 0.0844  269 ASP A CG  
1519  O OD1 . ASP A 260 ? 0.3046 1.1738 0.4308 -0.1598 -0.0286 0.0995  269 ASP A OD1 
1520  O OD2 . ASP A 260 ? 0.3013 1.2015 0.4327 -0.1478 -0.0228 0.0885  269 ASP A OD2 
1521  N N   . GLN A 261 ? 0.1925 1.0022 0.3418 -0.0583 0.0076  0.0219  270 GLN A N   
1522  C CA  . GLN A 261 ? 0.1877 0.9589 0.3371 -0.0362 0.0150  0.0012  270 GLN A CA  
1523  C C   . GLN A 261 ? 0.1827 0.9216 0.3316 -0.0332 0.0152  0.0017  270 GLN A C   
1524  O O   . GLN A 261 ? 0.1826 0.8658 0.3289 -0.0338 0.0156  -0.0061 270 GLN A O   
1525  C CB  . GLN A 261 ? 0.1943 1.0036 0.3451 -0.0113 0.0224  -0.0111 270 GLN A CB  
1526  C CG  . GLN A 261 ? 0.2178 0.9894 0.3648 0.0035  0.0278  -0.0323 270 GLN A CG  
1527  C CD  . GLN A 261 ? 0.2625 1.0718 0.4075 0.0216  0.0327  -0.0431 270 GLN A CD  
1528  O OE1 . GLN A 261 ? 0.3016 1.0847 0.4403 0.0406  0.0379  -0.0622 270 GLN A OE1 
1529  N NE2 . GLN A 261 ? 0.2625 1.1329 0.4111 0.0155  0.0306  -0.0311 270 GLN A NE2 
1530  N N   . LYS A 262 ? 0.1742 0.9506 0.3254 -0.0310 0.0146  0.0120  271 LYS A N   
1531  C CA  . LYS A 262 ? 0.1682 0.9187 0.3189 -0.0287 0.0144  0.0139  271 LYS A CA  
1532  C C   . LYS A 262 ? 0.1641 0.8650 0.3105 -0.0511 0.0075  0.0213  271 LYS A C   
1533  O O   . LYS A 262 ? 0.1669 0.8192 0.3115 -0.0461 0.0093  0.0133  271 LYS A O   
1534  C CB  . LYS A 262 ? 0.1666 0.9732 0.3205 -0.0276 0.0132  0.0277  271 LYS A CB  
1535  C CG  . LYS A 262 ? 0.1735 1.0192 0.3292 0.0027  0.0213  0.0175  271 LYS A CG  
1536  C CD  . LYS A 262 ? 0.1867 1.0859 0.3455 0.0079  0.0209  0.0304  271 LYS A CD  
1537  C CE  . LYS A 262 ? 0.1915 1.1655 0.3525 0.0256  0.0250  0.0311  271 LYS A CE  
1538  N NZ  . LYS A 262 ? 0.1843 1.2081 0.3471 0.0416  0.0273  0.0381  271 LYS A NZ  
1539  N N   . LYS A 263 ? 0.1622 0.8737 0.3047 -0.0753 -0.0006 0.0365  272 LYS A N   
1540  C CA  . LYS A 263 ? 0.1662 0.8290 0.3003 -0.0950 -0.0080 0.0437  272 LYS A CA  
1541  C C   . LYS A 263 ? 0.1569 0.7657 0.2887 -0.0886 -0.0051 0.0291  272 LYS A C   
1542  O O   . LYS A 263 ? 0.1606 0.7226 0.2875 -0.0918 -0.0070 0.0277  272 LYS A O   
1543  C CB  . LYS A 263 ? 0.1821 0.8634 0.3084 -0.1211 -0.0178 0.0621  272 LYS A CB  
1544  C CG  . LYS A 263 ? 0.2267 0.8517 0.3391 -0.1390 -0.0260 0.0677  272 LYS A CG  
1545  C CD  . LYS A 263 ? 0.3022 0.9437 0.4042 -0.1622 -0.0353 0.0838  272 LYS A CD  
1546  C CE  . LYS A 263 ? 0.3509 0.9417 0.4329 -0.1838 -0.0466 0.0953  272 LYS A CE  
1547  N NZ  . LYS A 263 ? 0.3916 1.0079 0.4610 -0.2102 -0.0574 0.1156  272 LYS A NZ  
1548  N N   . LEU A 264 ? 0.1418 0.7598 0.2765 -0.0801 -0.0009 0.0188  273 LEU A N   
1549  C CA  . LEU A 264 ? 0.1266 0.7002 0.2599 -0.0740 0.0022  0.0048  273 LEU A CA  
1550  C C   . LEU A 264 ? 0.1217 0.6639 0.2575 -0.0583 0.0082  -0.0083 273 LEU A C   
1551  O O   . LEU A 264 ? 0.1225 0.6204 0.2547 -0.0614 0.0071  -0.0108 273 LEU A O   
1552  C CB  . LEU A 264 ? 0.1244 0.7188 0.2610 -0.0649 0.0068  -0.0059 273 LEU A CB  
1553  C CG  . LEU A 264 ? 0.0969 0.6541 0.2324 -0.0594 0.0100  -0.0206 273 LEU A CG  
1554  C CD1 . LEU A 264 ? 0.0903 0.6301 0.2195 -0.0755 0.0034  -0.0113 273 LEU A CD1 
1555  C CD2 . LEU A 264 ? 0.0774 0.6587 0.2161 -0.0474 0.0155  -0.0334 273 LEU A CD2 
1556  N N   . MET A 265 ? 0.1160 0.6809 0.2562 -0.0406 0.0144  -0.0165 274 MET A N   
1557  C CA  . MET A 265 ? 0.1201 0.6536 0.2602 -0.0256 0.0196  -0.0281 274 MET A CA  
1558  C C   . MET A 265 ? 0.1263 0.6333 0.2648 -0.0334 0.0162  -0.0195 274 MET A C   
1559  O O   . MET A 265 ? 0.1367 0.6007 0.2734 -0.0310 0.0177  -0.0267 274 MET A O   
1560  C CB  . MET A 265 ? 0.1206 0.6832 0.2619 -0.0046 0.0255  -0.0358 274 MET A CB  
1561  C CG  . MET A 265 ? 0.1142 0.6844 0.2538 0.0061  0.0297  -0.0495 274 MET A CG  
1562  S SD  . MET A 265 ? 0.1197 0.7179 0.2553 0.0349  0.0363  -0.0604 274 MET A SD  
1563  C CE  . MET A 265 ? 0.1522 0.6949 0.2803 0.0507  0.0405  -0.0736 274 MET A CE  
1564  N N   . SER A 266 ? 0.1307 0.6641 0.2691 -0.0447 0.0109  -0.0035 275 SER A N   
1565  C CA  . SER A 266 ? 0.1379 0.6475 0.2731 -0.0535 0.0067  0.0052  275 SER A CA  
1566  C C   . SER A 266 ? 0.1465 0.6099 0.2748 -0.0670 0.0019  0.0068  275 SER A C   
1567  O O   . SER A 266 ? 0.1538 0.5818 0.2794 -0.0661 0.0018  0.0051  275 SER A O   
1568  C CB  . SER A 266 ? 0.1407 0.6907 0.2752 -0.0669 0.0006  0.0232  275 SER A CB  
1569  O OG  . SER A 266 ? 0.1365 0.7371 0.2774 -0.0527 0.0053  0.0226  275 SER A OG  
1570  N N   . ASN A 267 ? 0.1559 0.6190 0.2798 -0.0780 -0.0021 0.0101  276 ASN A N   
1571  C CA  . ASN A 267 ? 0.1709 0.5888 0.2858 -0.0870 -0.0066 0.0111  276 ASN A CA  
1572  C C   . ASN A 267 ? 0.1651 0.5538 0.2826 -0.0755 -0.0007 -0.0044 276 ASN A C   
1573  O O   . ASN A 267 ? 0.1744 0.5358 0.2851 -0.0808 -0.0038 -0.0040 276 ASN A O   
1574  C CB  . ASN A 267 ? 0.1824 0.6033 0.2867 -0.1048 -0.0153 0.0235  276 ASN A CB  
1575  C CG  . ASN A 267 ? 0.2189 0.6497 0.3141 -0.1229 -0.0243 0.0413  276 ASN A CG  
1576  O OD1 . ASN A 267 ? 0.2585 0.6645 0.3476 -0.1271 -0.0275 0.0454  276 ASN A OD1 
1577  N ND2 . ASN A 267 ? 0.2453 0.7138 0.3385 -0.1351 -0.0288 0.0525  276 ASN A ND2 
1578  N N   . ASN A 268 ? 0.1619 0.5552 0.2874 -0.0598 0.0072  -0.0175 277 ASN A N   
1579  C CA  . ASN A 268 ? 0.1615 0.5304 0.2885 -0.0515 0.0123  -0.0321 277 ASN A CA  
1580  C C   . ASN A 268 ? 0.1671 0.5203 0.2971 -0.0374 0.0190  -0.0443 277 ASN A C   
1581  O O   . ASN A 268 ? 0.1701 0.5135 0.3007 -0.0305 0.0234  -0.0572 277 ASN A O   
1582  C CB  . ASN A 268 ? 0.1563 0.5492 0.2856 -0.0495 0.0143  -0.0382 277 ASN A CB  
1583  C CG  . ASN A 268 ? 0.1522 0.5437 0.2766 -0.0614 0.0089  -0.0310 277 ASN A CG  
1584  O OD1 . ASN A 268 ? 0.1599 0.5257 0.2814 -0.0625 0.0087  -0.0350 277 ASN A OD1 
1585  N ND2 . ASN A 268 ? 0.1632 0.5833 0.2857 -0.0703 0.0042  -0.0196 277 ASN A ND2 
1586  N N   . VAL A 269 ? 0.1674 0.5176 0.2977 -0.0341 0.0190  -0.0396 278 VAL A N   
1587  C CA  . VAL A 269 ? 0.1712 0.5040 0.3020 -0.0205 0.0243  -0.0487 278 VAL A CA  
1588  C C   . VAL A 269 ? 0.1733 0.4709 0.3020 -0.0169 0.0281  -0.0616 278 VAL A C   
1589  O O   . VAL A 269 ? 0.1840 0.4729 0.3105 -0.0054 0.0327  -0.0727 278 VAL A O   
1590  C CB  . VAL A 269 ? 0.1728 0.4932 0.3027 -0.0232 0.0220  -0.0396 278 VAL A CB  
1591  C CG1 . VAL A 269 ? 0.1603 0.5177 0.2924 -0.0205 0.0207  -0.0304 278 VAL A CG1 
1592  C CG2 . VAL A 269 ? 0.1879 0.4897 0.3137 -0.0387 0.0158  -0.0307 278 VAL A CG2 
1593  N N   . GLN A 270 ? 0.1671 0.4441 0.2946 -0.0268 0.0256  -0.0598 279 GLN A N   
1594  C CA  . GLN A 270 ? 0.1698 0.4199 0.2959 -0.0256 0.0287  -0.0704 279 GLN A CA  
1595  C C   . GLN A 270 ? 0.1645 0.4227 0.2898 -0.0206 0.0322  -0.0829 279 GLN A C   
1596  O O   . GLN A 270 ? 0.1753 0.4165 0.2966 -0.0134 0.0358  -0.0930 279 GLN A O   
1597  C CB  . GLN A 270 ? 0.1718 0.4092 0.2965 -0.0354 0.0254  -0.0660 279 GLN A CB  
1598  C CG  . GLN A 270 ? 0.2099 0.4188 0.3333 -0.0353 0.0278  -0.0719 279 GLN A CG  
1599  C CD  . GLN A 270 ? 0.2580 0.4585 0.3790 -0.0419 0.0249  -0.0678 279 GLN A CD  
1600  O OE1 . GLN A 270 ? 0.2801 0.4948 0.4000 -0.0454 0.0224  -0.0653 279 GLN A OE1 
1601  N NE2 . GLN A 270 ? 0.2638 0.4423 0.3830 -0.0421 0.0253  -0.0667 279 GLN A NE2 
1602  N N   . ILE A 271 ? 0.1480 0.4297 0.2748 -0.0250 0.0307  -0.0822 280 ILE A N   
1603  C CA  . ILE A 271 ? 0.1433 0.4372 0.2686 -0.0206 0.0335  -0.0939 280 ILE A CA  
1604  C C   . ILE A 271 ? 0.1518 0.4519 0.2731 -0.0063 0.0370  -0.1015 280 ILE A C   
1605  O O   . ILE A 271 ? 0.1677 0.4503 0.2819 0.0004  0.0400  -0.1144 280 ILE A O   
1606  C CB  . ILE A 271 ? 0.1318 0.4578 0.2599 -0.0262 0.0308  -0.0885 280 ILE A CB  
1607  C CG1 . ILE A 271 ? 0.1154 0.4339 0.2439 -0.0374 0.0267  -0.0800 280 ILE A CG1 
1608  C CG2 . ILE A 271 ? 0.1306 0.4713 0.2569 -0.0221 0.0334  -0.1004 280 ILE A CG2 
1609  C CD1 . ILE A 271 ? 0.1123 0.4276 0.2403 -0.0408 0.0276  -0.0875 280 ILE A CD1 
1610  N N   . VAL A 272 ? 0.1415 0.4668 0.2656 -0.0016 0.0360  -0.0928 281 VAL A N   
1611  C CA  . VAL A 272 ? 0.1511 0.4876 0.2708 0.0148  0.0392  -0.0983 281 VAL A CA  
1612  C C   . VAL A 272 ? 0.1713 0.4683 0.2828 0.0238  0.0422  -0.1078 281 VAL A C   
1613  O O   . VAL A 272 ? 0.1965 0.4820 0.2981 0.0348  0.0449  -0.1207 281 VAL A O   
1614  C CB  . VAL A 272 ? 0.1409 0.5069 0.2653 0.0171  0.0375  -0.0850 281 VAL A CB  
1615  C CG1 . VAL A 272 ? 0.1392 0.5253 0.2586 0.0371  0.0412  -0.0911 281 VAL A CG1 
1616  C CG2 . VAL A 272 ? 0.1156 0.5147 0.2463 0.0026  0.0328  -0.0719 281 VAL A CG2 
1617  N N   . ARG A 273 ? 0.1679 0.4418 0.2815 0.0188  0.0411  -0.1013 282 ARG A N   
1618  C CA  . ARG A 273 ? 0.1856 0.4215 0.2910 0.0257  0.0434  -0.1084 282 ARG A CA  
1619  C C   . ARG A 273 ? 0.2110 0.4208 0.3082 0.0217  0.0445  -0.1218 282 ARG A C   
1620  O O   . ARG A 273 ? 0.2409 0.4305 0.3252 0.0323  0.0465  -0.1329 282 ARG A O   
1621  C CB  . ARG A 273 ? 0.1713 0.3880 0.2812 0.0175  0.0418  -0.0989 282 ARG A CB  
1622  C CG  . ARG A 273 ? 0.1428 0.3819 0.2586 0.0190  0.0399  -0.0859 282 ARG A CG  
1623  C CD  . ARG A 273 ? 0.1339 0.3469 0.2489 0.0186  0.0398  -0.0812 282 ARG A CD  
1624  N NE  . ARG A 273 ? 0.1217 0.3554 0.2420 0.0163  0.0370  -0.0678 282 ARG A NE  
1625  C CZ  . ARG A 273 ? 0.1447 0.3792 0.2637 0.0260  0.0380  -0.0638 282 ARG A CZ  
1626  N NH1 . ARG A 273 ? 0.1574 0.3697 0.2687 0.0403  0.0418  -0.0724 282 ARG A NH1 
1627  N NH2 . ARG A 273 ? 0.1550 0.4107 0.2784 0.0208  0.0346  -0.0509 282 ARG A NH2 
1628  N N   . GLN A 274 ? 0.2040 0.4148 0.3068 0.0067  0.0427  -0.1205 283 GLN A N   
1629  C CA  . GLN A 274 ? 0.2218 0.4137 0.3178 0.0003  0.0432  -0.1317 283 GLN A CA  
1630  C C   . GLN A 274 ? 0.2353 0.4349 0.3216 0.0093  0.0446  -0.1440 283 GLN A C   
1631  O O   . GLN A 274 ? 0.2593 0.4338 0.3331 0.0083  0.0449  -0.1560 283 GLN A O   
1632  C CB  . GLN A 274 ? 0.2071 0.4114 0.3119 -0.0143 0.0412  -0.1267 283 GLN A CB  
1633  C CG  . GLN A 274 ? 0.2459 0.4358 0.3559 -0.0213 0.0399  -0.1168 283 GLN A CG  
1634  C CD  . GLN A 274 ? 0.2912 0.4913 0.4073 -0.0329 0.0376  -0.1112 283 GLN A CD  
1635  O OE1 . GLN A 274 ? 0.3238 0.5462 0.4421 -0.0358 0.0367  -0.1125 283 GLN A OE1 
1636  N NE2 . GLN A 274 ? 0.2783 0.4632 0.3962 -0.0377 0.0367  -0.1048 283 GLN A NE2 
1637  N N   . GLN A 275 ? 0.2249 0.4592 0.3152 0.0182  0.0449  -0.1408 284 GLN A N   
1638  C CA  . GLN A 275 ? 0.2407 0.4872 0.3214 0.0289  0.0463  -0.1523 284 GLN A CA  
1639  C C   . GLN A 275 ? 0.2595 0.4929 0.3257 0.0499  0.0485  -0.1597 284 GLN A C   
1640  O O   . GLN A 275 ? 0.2720 0.5102 0.3261 0.0620  0.0495  -0.1709 284 GLN A O   
1641  C CB  . GLN A 275 ? 0.2231 0.5176 0.3142 0.0279  0.0455  -0.1455 284 GLN A CB  
1642  C CG  . GLN A 275 ? 0.2331 0.5379 0.3308 0.0121  0.0436  -0.1445 284 GLN A CG  
1643  C CD  . GLN A 275 ? 0.2550 0.6063 0.3609 0.0111  0.0425  -0.1373 284 GLN A CD  
1644  O OE1 . GLN A 275 ? 0.2521 0.6276 0.3647 0.0131  0.0414  -0.1252 284 GLN A OE1 
1645  N NE2 . GLN A 275 ? 0.2636 0.6292 0.3682 0.0067  0.0422  -0.1441 284 GLN A NE2 
1646  N N   . SER A 276 ? 0.2591 0.4750 0.3248 0.0555  0.0490  -0.1539 285 SER A N   
1647  C CA  . SER A 276 ? 0.2821 0.4908 0.3348 0.0780  0.0510  -0.1582 285 SER A CA  
1648  C C   . SER A 276 ? 0.3162 0.4691 0.3508 0.0813  0.0510  -0.1670 285 SER A C   
1649  O O   . SER A 276 ? 0.3212 0.4463 0.3575 0.0644  0.0495  -0.1662 285 SER A O   
1650  C CB  . SER A 276 ? 0.2635 0.4992 0.3284 0.0832  0.0513  -0.1434 285 SER A CB  
1651  O OG  . SER A 276 ? 0.2360 0.5191 0.3174 0.0739  0.0499  -0.1321 285 SER A OG  
1652  N N   . TYR A 277 ? 0.3494 0.4864 0.3651 0.1038  0.0524  -0.1749 286 TYR A N   
1653  C CA  . TYR A 277 ? 0.3935 0.4726 0.3868 0.1087  0.0516  -0.1835 286 TYR A CA  
1654  C C   . TYR A 277 ? 0.4076 0.4814 0.3965 0.1282  0.0533  -0.1773 286 TYR A C   
1655  O O   . TYR A 277 ? 0.4020 0.5190 0.4003 0.1424  0.0552  -0.1702 286 TYR A O   
1656  C CB  . TYR A 277 ? 0.4353 0.4885 0.4013 0.1203  0.0509  -0.2014 286 TYR A CB  
1657  C CG  . TYR A 277 ? 0.4429 0.4911 0.4084 0.0998  0.0487  -0.2091 286 TYR A CG  
1658  C CD1 . TYR A 277 ? 0.4362 0.5330 0.4208 0.0914  0.0493  -0.2055 286 TYR A CD1 
1659  C CD2 . TYR A 277 ? 0.4960 0.4921 0.4408 0.0881  0.0456  -0.2193 286 TYR A CD2 
1660  C CE1 . TYR A 277 ? 0.4579 0.5537 0.4426 0.0731  0.0473  -0.2120 286 TYR A CE1 
1661  C CE2 . TYR A 277 ? 0.5192 0.5151 0.4638 0.0680  0.0433  -0.2259 286 TYR A CE2 
1662  C CZ  . TYR A 277 ? 0.4899 0.5371 0.4551 0.0616  0.0445  -0.2223 286 TYR A CZ  
1663  O OH  . TYR A 277 ? 0.5083 0.5603 0.4744 0.0428  0.0424  -0.2280 286 TYR A OH  
1664  N N   . SER A 278 ? 0.4330 0.4563 0.4070 0.1288  0.0523  -0.1793 287 SER A N   
1665  C CA  . SER A 278 ? 0.4510 0.4638 0.4148 0.1515  0.0537  -0.1760 287 SER A CA  
1666  C C   . SER A 278 ? 0.5107 0.4610 0.4390 0.1645  0.0521  -0.1896 287 SER A C   
1667  O O   . SER A 278 ? 0.5306 0.4341 0.4481 0.1473  0.0493  -0.1935 287 SER A O   
1668  C CB  . SER A 278 ? 0.4253 0.4408 0.4071 0.1400  0.0538  -0.1610 287 SER A CB  
1669  O OG  . SER A 278 ? 0.4513 0.4459 0.4203 0.1596  0.0547  -0.1585 287 SER A OG  
1670  N N   . ILE A 279 ? 0.5470 0.4973 0.4552 0.1951  0.0534  -0.1967 288 ILE A N   
1671  C CA  . ILE A 279 ? 0.6193 0.5067 0.4884 0.2106  0.0511  -0.2106 288 ILE A CA  
1672  C C   . ILE A 279 ? 0.6523 0.5223 0.5101 0.2332  0.0523  -0.2049 288 ILE A C   
1673  O O   . ILE A 279 ? 0.6440 0.5604 0.5130 0.2537  0.0556  -0.1975 288 ILE A O   
1674  C CB  . ILE A 279 ? 0.6451 0.5412 0.4930 0.2359  0.0517  -0.2244 288 ILE A CB  
1675  C CG1 . ILE A 279 ? 0.5994 0.5502 0.4701 0.2225  0.0528  -0.2248 288 ILE A CG1 
1676  C CG2 . ILE A 279 ? 0.7228 0.5415 0.5255 0.2442  0.0474  -0.2411 288 ILE A CG2 
1677  C CD1 . ILE A 279 ? 0.6300 0.5505 0.4854 0.2066  0.0494  -0.2388 288 ILE A CD1 
1678  N N   . MET A 280 ? 0.7053 0.5094 0.5395 0.2295  0.0491  -0.2080 289 MET A N   
1679  C CA  . MET A 280 ? 0.7389 0.5208 0.5594 0.2516  0.0499  -0.2026 289 MET A CA  
1680  C C   . MET A 280 ? 0.7909 0.5651 0.5804 0.2902  0.0505  -0.2141 289 MET A C   
1681  O O   . MET A 280 ? 0.8291 0.5732 0.5926 0.2941  0.0479  -0.2294 289 MET A O   
1682  C CB  . MET A 280 ? 0.7783 0.4868 0.5765 0.2368  0.0455  -0.2041 289 MET A CB  
1683  C CG  . MET A 280 ? 0.7980 0.4906 0.5930 0.2490  0.0463  -0.1937 289 MET A CG  
1684  S SD  . MET A 280 ? 0.8775 0.4791 0.6410 0.2296  0.0402  -0.1964 289 MET A SD  
1685  C CE  . MET A 280 ? 0.9620 0.4999 0.6736 0.2432  0.0350  -0.2185 289 MET A CE  
1686  N N   . SER A 281 ? 0.8000 0.6046 0.5916 0.3194  0.0539  -0.2068 290 SER A N   
1687  C CA  . SER A 281 ? 0.8570 0.6609 0.6183 0.3619  0.0552  -0.2168 290 SER A CA  
1688  C C   . SER A 281 ? 0.9206 0.6635 0.6445 0.3893  0.0534  -0.2192 290 SER A C   
1689  O O   . SER A 281 ? 0.9895 0.6661 0.6698 0.4030  0.0495  -0.2343 290 SER A O   
1690  C CB  . SER A 281 ? 0.8197 0.7129 0.6071 0.3804  0.0604  -0.2082 290 SER A CB  
1691  O OG  . SER A 281 ? 0.8865 0.7823 0.6434 0.4246  0.0619  -0.2175 290 SER A OG  
1692  N N   . ILE A 282 ? 0.9057 0.6686 0.6435 0.3976  0.0558  -0.2046 291 ILE A N   
1693  C CA  . ILE A 282 ? 0.9651 0.6652 0.6691 0.4184  0.0537  -0.2048 291 ILE A CA  
1694  C C   . ILE A 282 ? 0.9372 0.6389 0.6612 0.4053  0.0544  -0.1879 291 ILE A C   
1695  O O   . ILE A 282 ? 0.8725 0.6418 0.6338 0.4000  0.0582  -0.1736 291 ILE A O   
1696  C CB  . ILE A 282 ? 1.0198 0.7216 0.6910 0.4707  0.0554  -0.2114 291 ILE A CB  
1697  C CG1 . ILE A 282 ? 0.9745 0.7742 0.6731 0.4887  0.0612  -0.2067 291 ILE A CG1 
1698  C CG2 . ILE A 282 ? 1.1106 0.7295 0.7264 0.4874  0.0502  -0.2321 291 ILE A CG2 
1699  C CD1 . ILE A 282 ? 0.9328 0.7979 0.6614 0.4972  0.0654  -0.1876 291 ILE A CD1 
1700  N N   . ILE A 283 ? 0.9891 0.6124 0.6846 0.3996  0.0500  -0.1900 292 ILE A N   
1701  C CA  . ILE A 283 ? 0.9801 0.5913 0.6890 0.3845  0.0498  -0.1754 292 ILE A CA  
1702  C C   . ILE A 283 ? 1.0387 0.6058 0.7122 0.4190  0.0488  -0.1746 292 ILE A C   
1703  O O   . ILE A 283 ? 1.1060 0.6012 0.7322 0.4362  0.0445  -0.1867 292 ILE A O   
1704  C CB  . ILE A 283 ? 0.9847 0.5395 0.6918 0.3429  0.0449  -0.1752 292 ILE A CB  
1705  C CG1 . ILE A 283 ? 1.0244 0.5432 0.7129 0.3261  0.0408  -0.1908 292 ILE A CG1 
1706  C CG2 . ILE A 283 ? 0.9068 0.5069 0.6602 0.3103  0.0472  -0.1593 292 ILE A CG2 
1707  C CD1 . ILE A 283 ? 1.0146 0.5958 0.7269 0.3237  0.0439  -0.1962 292 ILE A CD1 
1708  N N   . LYS A 284 ? 1.0130 0.6230 0.7088 0.4277  0.0524  -0.1595 293 LYS A N   
1709  C CA  . LYS A 284 ? 1.0666 0.6457 0.7363 0.4580  0.0521  -0.1549 293 LYS A CA  
1710  C C   . LYS A 284 ? 1.0303 0.6228 0.7300 0.4315  0.0527  -0.1382 293 LYS A C   
1711  O O   . LYS A 284 ? 0.9628 0.6089 0.7046 0.4021  0.0548  -0.1303 293 LYS A O   
1712  C CB  . LYS A 284 ? 1.0652 0.7084 0.7374 0.5007  0.0570  -0.1523 293 LYS A CB  
1713  C CG  . LYS A 284 ? 1.0984 0.7558 0.7524 0.5256  0.0579  -0.1675 293 LYS A CG  
1714  C CD  . LYS A 284 ? 1.1548 0.8324 0.7836 0.5804  0.0606  -0.1688 293 LYS A CD  
1715  C CE  . LYS A 284 ? 1.2053 0.8839 0.8082 0.6066  0.0607  -0.1860 293 LYS A CE  
1716  N NZ  . LYS A 284 ? 1.3013 0.9459 0.8558 0.6605  0.0603  -0.1930 293 LYS A NZ  
1717  N N   . GLU A 285 ? 1.0813 0.6248 0.7577 0.4432  0.0507  -0.1326 294 GLU A N   
1718  C CA  . GLU A 285 ? 1.0614 0.6086 0.7614 0.4184  0.0508  -0.1171 294 GLU A CA  
1719  C C   . GLU A 285 ? 0.9749 0.6141 0.7247 0.4088  0.0557  -0.1038 294 GLU A C   
1720  O O   . GLU A 285 ? 0.9274 0.5824 0.7070 0.3745  0.0556  -0.0951 294 GLU A O   
1721  C CB  . GLU A 285 ? 1.1257 0.6207 0.7936 0.4419  0.0489  -0.1114 294 GLU A CB  
1722  C CG  . GLU A 285 ? 1.2451 0.6373 0.8691 0.4311  0.0420  -0.1193 294 GLU A CG  
1723  C CD  . GLU A 285 ? 1.3535 0.6895 0.9440 0.4522  0.0394  -0.1122 294 GLU A CD  
1724  O OE1 . GLU A 285 ? 1.3272 0.6765 0.9391 0.4366  0.0404  -0.0974 294 GLU A OE1 
1725  O OE2 . GLU A 285 ? 1.4571 0.7332 0.9977 0.4848  0.0360  -0.1218 294 GLU A OE2 
1726  N N   . GLU A 286 ? 0.9554 0.6551 0.7120 0.4389  0.0596  -0.1024 295 GLU A N   
1727  C CA  . GLU A 286 ? 0.8884 0.6736 0.6865 0.4325  0.0633  -0.0883 295 GLU A CA  
1728  C C   . GLU A 286 ? 0.8319 0.6840 0.6549 0.4260  0.0655  -0.0911 295 GLU A C   
1729  O O   . GLU A 286 ? 0.7804 0.7045 0.6358 0.4188  0.0677  -0.0794 295 GLU A O   
1730  C CB  . GLU A 286 ? 0.9118 0.7268 0.7036 0.4686  0.0658  -0.0783 295 GLU A CB  
1731  C CG  . GLU A 286 ? 1.0296 0.7963 0.7735 0.5144  0.0653  -0.0869 295 GLU A CG  
1732  C CD  . GLU A 286 ? 1.1098 0.8749 0.8319 0.5371  0.0656  -0.1030 295 GLU A CD  
1733  O OE1 . GLU A 286 ? 1.1663 0.8600 0.8603 0.5299  0.0618  -0.1167 295 GLU A OE1 
1734  O OE2 . GLU A 286 ? 1.1062 0.9418 0.8381 0.5613  0.0694  -0.1016 295 GLU A OE2 
1735  N N   . VAL A 287 ? 0.8403 0.6690 0.6468 0.4281  0.0644  -0.1062 296 VAL A N   
1736  C CA  . VAL A 287 ? 0.7871 0.6753 0.6170 0.4181  0.0661  -0.1090 296 VAL A CA  
1737  C C   . VAL A 287 ? 0.7916 0.6378 0.6118 0.3982  0.0635  -0.1231 296 VAL A C   
1738  O O   . VAL A 287 ? 0.8499 0.6301 0.6328 0.4111  0.0609  -0.1362 296 VAL A O   
1739  C CB  . VAL A 287 ? 0.7977 0.7368 0.6193 0.4559  0.0692  -0.1123 296 VAL A CB  
1740  C CG1 . VAL A 287 ? 0.7398 0.7581 0.5969 0.4383  0.0710  -0.1073 296 VAL A CG1 
1741  C CG2 . VAL A 287 ? 0.8253 0.7911 0.6407 0.4887  0.0715  -0.1021 296 VAL A CG2 
1742  N N   . LEU A 288 ? 0.7293 0.6153 0.5820 0.3667  0.0637  -0.1201 297 LEU A N   
1743  C CA  . LEU A 288 ? 0.7159 0.5806 0.5667 0.3456  0.0617  -0.1320 297 LEU A CA  
1744  C C   . LEU A 288 ? 0.6723 0.6063 0.5430 0.3472  0.0640  -0.1330 297 LEU A C   
1745  O O   . LEU A 288 ? 0.6268 0.6246 0.5291 0.3369  0.0656  -0.1204 297 LEU A O   
1746  C CB  . LEU A 288 ? 0.6801 0.5259 0.5508 0.3040  0.0594  -0.1267 297 LEU A CB  
1747  C CG  . LEU A 288 ? 0.6669 0.5104 0.5441 0.2798  0.0579  -0.1360 297 LEU A CG  
1748  C CD1 . LEU A 288 ? 0.7393 0.5212 0.5783 0.2903  0.0552  -0.1529 297 LEU A CD1 
1749  C CD2 . LEU A 288 ? 0.6333 0.4678 0.5318 0.2417  0.0561  -0.1295 297 LEU A CD2 
1750  N N   . ALA A 289 ? 0.6851 0.6058 0.5360 0.3589  0.0636  -0.1478 298 ALA A N   
1751  C CA  . ALA A 289 ? 0.6414 0.6267 0.5099 0.3596  0.0656  -0.1489 298 ALA A CA  
1752  C C   . ALA A 289 ? 0.6401 0.5963 0.5020 0.3407  0.0633  -0.1621 298 ALA A C   
1753  O O   . ALA A 289 ? 0.6923 0.5825 0.5219 0.3464  0.0607  -0.1753 298 ALA A O   
1754  C CB  . ALA A 289 ? 0.6735 0.6890 0.5236 0.4022  0.0683  -0.1532 298 ALA A CB  
1755  N N   . TYR A 290 ? 0.5826 0.5880 0.4734 0.3181  0.0638  -0.1582 299 TYR A N   
1756  C CA  . TYR A 290 ? 0.5735 0.5607 0.4620 0.2984  0.0618  -0.1694 299 TYR A CA  
1757  C C   . TYR A 290 ? 0.5332 0.5897 0.4427 0.2958  0.0636  -0.1677 299 TYR A C   
1758  O O   . TYR A 290 ? 0.5048 0.6232 0.4360 0.2994  0.0657  -0.1551 299 TYR A O   
1759  C CB  . TYR A 290 ? 0.5476 0.5054 0.4509 0.2607  0.0592  -0.1649 299 TYR A CB  
1760  C CG  . TYR A 290 ? 0.4951 0.4988 0.4334 0.2420  0.0601  -0.1474 299 TYR A CG  
1761  C CD1 . TYR A 290 ? 0.4553 0.5040 0.4203 0.2200  0.0600  -0.1420 299 TYR A CD1 
1762  C CD2 . TYR A 290 ? 0.4891 0.4888 0.4315 0.2463  0.0606  -0.1362 299 TYR A CD2 
1763  C CE1 . TYR A 290 ? 0.4055 0.4908 0.3983 0.2026  0.0597  -0.1264 299 TYR A CE1 
1764  C CE2 . TYR A 290 ? 0.4391 0.4780 0.4109 0.2283  0.0607  -0.1208 299 TYR A CE2 
1765  C CZ  . TYR A 290 ? 0.3945 0.4743 0.3901 0.2066  0.0600  -0.1163 299 TYR A CZ  
1766  O OH  . TYR A 290 ? 0.3432 0.4565 0.3632 0.1889  0.0590  -0.1018 299 TYR A OH  
1767  N N   . VAL A 291 ? 0.5361 0.5829 0.4384 0.2881  0.0625  -0.1798 300 VAL A N   
1768  C CA  . VAL A 291 ? 0.5017 0.6119 0.4217 0.2860  0.0640  -0.1784 300 VAL A CA  
1769  C C   . VAL A 291 ? 0.4622 0.5812 0.4068 0.2487  0.0621  -0.1739 300 VAL A C   
1770  O O   . VAL A 291 ? 0.4797 0.5527 0.4154 0.2312  0.0597  -0.1827 300 VAL A O   
1771  C CB  . VAL A 291 ? 0.5378 0.6391 0.4312 0.3081  0.0642  -0.1955 300 VAL A CB  
1772  C CG1 . VAL A 291 ? 0.5030 0.6601 0.4154 0.2962  0.0649  -0.1956 300 VAL A CG1 
1773  C CG2 . VAL A 291 ? 0.5825 0.6968 0.4554 0.3499  0.0668  -0.1976 300 VAL A CG2 
1774  N N   . VAL A 292 ? 0.4161 0.5952 0.3898 0.2366  0.0628  -0.1596 301 VAL A N   
1775  C CA  . VAL A 292 ? 0.3783 0.5748 0.3739 0.2055  0.0610  -0.1550 301 VAL A CA  
1776  C C   . VAL A 292 ? 0.3748 0.6078 0.3714 0.2078  0.0615  -0.1617 301 VAL A C   
1777  O O   . VAL A 292 ? 0.3914 0.6640 0.3824 0.2315  0.0637  -0.1631 301 VAL A O   
1778  C CB  . VAL A 292 ? 0.3349 0.5723 0.3568 0.1910  0.0604  -0.1366 301 VAL A CB  
1779  C CG1 . VAL A 292 ? 0.3141 0.5924 0.3558 0.1695  0.0588  -0.1307 301 VAL A CG1 
1780  C CG2 . VAL A 292 ? 0.3322 0.5276 0.3574 0.1753  0.0589  -0.1315 301 VAL A CG2 
1781  N N   . GLN A 293 ? 0.3555 0.5787 0.3592 0.1839  0.0596  -0.1653 302 GLN A N   
1782  C CA  . GLN A 293 ? 0.3546 0.6017 0.3555 0.1852  0.0598  -0.1740 302 GLN A CA  
1783  C C   . GLN A 293 ? 0.3041 0.5841 0.3296 0.1578  0.0581  -0.1645 302 GLN A C   
1784  O O   . GLN A 293 ? 0.2964 0.5480 0.3264 0.1361  0.0561  -0.1654 302 GLN A O   
1785  C CB  . GLN A 293 ? 0.3968 0.5872 0.3715 0.1878  0.0586  -0.1928 302 GLN A CB  
1786  C CG  . GLN A 293 ? 0.4264 0.6368 0.3972 0.1869  0.0584  -0.2029 302 GLN A CG  
1787  C CD  . GLN A 293 ? 0.5168 0.6748 0.4540 0.1985  0.0571  -0.2230 302 GLN A CD  
1788  O OE1 . GLN A 293 ? 0.5606 0.6786 0.4724 0.2196  0.0571  -0.2304 302 GLN A OE1 
1789  N NE2 . GLN A 293 ? 0.5360 0.6927 0.4707 0.1847  0.0554  -0.2322 302 GLN A NE2 
1790  N N   . LEU A 294 ? 0.2715 0.6121 0.3115 0.1590  0.0585  -0.1547 303 LEU A N   
1791  C CA  . LEU A 294 ? 0.2295 0.5988 0.2911 0.1331  0.0560  -0.1429 303 LEU A CA  
1792  C C   . LEU A 294 ? 0.2282 0.6247 0.2899 0.1308  0.0560  -0.1490 303 LEU A C   
1793  O O   . LEU A 294 ? 0.2576 0.6663 0.3057 0.1516  0.0582  -0.1593 303 LEU A O   
1794  C CB  . LEU A 294 ? 0.2022 0.6190 0.2797 0.1304  0.0552  -0.1245 303 LEU A CB  
1795  C CG  . LEU A 294 ? 0.2024 0.5967 0.2794 0.1346  0.0553  -0.1181 303 LEU A CG  
1796  C CD1 . LEU A 294 ? 0.1724 0.6110 0.2658 0.1240  0.0530  -0.0993 303 LEU A CD1 
1797  C CD2 . LEU A 294 ? 0.2099 0.5482 0.2862 0.1186  0.0538  -0.1207 303 LEU A CD2 
1798  N N   . PRO A 295 ? 0.2030 0.6090 0.2785 0.1069  0.0534  -0.1428 304 PRO A N   
1799  C CA  . PRO A 295 ? 0.2016 0.6354 0.2779 0.1033  0.0532  -0.1477 304 PRO A CA  
1800  C C   . PRO A 295 ? 0.1857 0.6849 0.2728 0.1057  0.0529  -0.1354 304 PRO A C   
1801  O O   . PRO A 295 ? 0.1702 0.6916 0.2684 0.0993  0.0513  -0.1197 304 PRO A O   
1802  C CB  . PRO A 295 ? 0.1787 0.5948 0.2649 0.0773  0.0502  -0.1441 304 PRO A CB  
1803  C CG  . PRO A 295 ? 0.1657 0.5690 0.2616 0.0662  0.0483  -0.1309 304 PRO A CG  
1804  C CD  . PRO A 295 ? 0.1809 0.5663 0.2685 0.0836  0.0505  -0.1328 304 PRO A CD  
1805  N N   . LEU A 296 ? 0.1937 0.7237 0.2765 0.1136  0.0541  -0.1423 305 LEU A N   
1806  C CA  . LEU A 296 ? 0.1757 0.7712 0.2686 0.1127  0.0535  -0.1305 305 LEU A CA  
1807  C C   . LEU A 296 ? 0.1697 0.7787 0.2662 0.0991  0.0520  -0.1329 305 LEU A C   
1808  O O   . LEU A 296 ? 0.1881 0.7775 0.2727 0.1065  0.0536  -0.1496 305 LEU A O   
1809  C CB  . LEU A 296 ? 0.1960 0.8238 0.2775 0.1424  0.0573  -0.1373 305 LEU A CB  
1810  C CG  . LEU A 296 ? 0.2115 0.8345 0.2871 0.1620  0.0594  -0.1353 305 LEU A CG  
1811  C CD1 . LEU A 296 ? 0.2328 0.8973 0.2970 0.1922  0.0629  -0.1412 305 LEU A CD1 
1812  C CD2 . LEU A 296 ? 0.2023 0.8546 0.2954 0.1459  0.0566  -0.1139 305 LEU A CD2 
1813  N N   . TYR A 297 ? 0.1462 0.7873 0.2572 0.0787  0.0483  -0.1161 306 TYR A N   
1814  C CA  . TYR A 297 ? 0.1391 0.7963 0.2541 0.0648  0.0464  -0.1157 306 TYR A CA  
1815  C C   . TYR A 297 ? 0.1367 0.8572 0.2532 0.0718  0.0471  -0.1120 306 TYR A C   
1816  O O   . TYR A 297 ? 0.1267 0.8925 0.2500 0.0704  0.0458  -0.0970 306 TYR A O   
1817  C CB  . TYR A 297 ? 0.1197 0.7666 0.2454 0.0383  0.0412  -0.1006 306 TYR A CB  
1818  C CG  . TYR A 297 ? 0.1278 0.7201 0.2528 0.0325  0.0406  -0.1023 306 TYR A CG  
1819  C CD1 . TYR A 297 ? 0.1325 0.7190 0.2625 0.0258  0.0381  -0.0887 306 TYR A CD1 
1820  C CD2 . TYR A 297 ? 0.1635 0.7112 0.2817 0.0337  0.0423  -0.1175 306 TYR A CD2 
1821  C CE1 . TYR A 297 ? 0.1390 0.6757 0.2678 0.0216  0.0377  -0.0904 306 TYR A CE1 
1822  C CE2 . TYR A 297 ? 0.1799 0.6792 0.2973 0.0283  0.0419  -0.1184 306 TYR A CE2 
1823  C CZ  . TYR A 297 ? 0.1534 0.6483 0.2763 0.0233  0.0398  -0.1050 306 TYR A CZ  
1824  O OH  . TYR A 297 ? 0.1228 0.5739 0.2448 0.0190  0.0396  -0.1059 306 TYR A OH  
1825  N N   . GLY A 298 ? 0.1467 0.8727 0.2566 0.0778  0.0488  -0.1251 307 GLY A N   
1826  C CA  . GLY A 298 ? 0.1435 0.9301 0.2545 0.0840  0.0495  -0.1220 307 GLY A CA  
1827  C C   . GLY A 298 ? 0.1253 0.9411 0.2478 0.0600  0.0451  -0.1067 307 GLY A C   
1828  O O   . GLY A 298 ? 0.1297 0.9983 0.2540 0.0625  0.0452  -0.1023 307 GLY A O   
1829  N N   . VAL A 299 ? 0.1126 0.8949 0.2412 0.0380  0.0410  -0.0985 308 VAL A N   
1830  C CA  . VAL A 299 ? 0.0988 0.9035 0.2352 0.0153  0.0357  -0.0817 308 VAL A CA  
1831  C C   . VAL A 299 ? 0.0986 0.8619 0.2383 -0.0034 0.0311  -0.0715 308 VAL A C   
1832  O O   . VAL A 299 ? 0.1060 0.8202 0.2430 -0.0018 0.0324  -0.0814 308 VAL A O   
1833  C CB  . VAL A 299 ? 0.0901 0.8961 0.2246 0.0115  0.0358  -0.0900 308 VAL A CB  
1834  C CG1 . VAL A 299 ? 0.0952 0.9595 0.2296 0.0184  0.0370  -0.0889 308 VAL A CG1 
1835  C CG2 . VAL A 299 ? 0.1076 0.8720 0.2339 0.0232  0.0397  -0.1117 308 VAL A CG2 
1836  N N   . ILE A 300 ? 0.1000 0.8826 0.2436 -0.0218 0.0252  -0.0514 309 ILE A N   
1837  C CA  . ILE A 300 ? 0.1039 0.8462 0.2472 -0.0389 0.0198  -0.0407 309 ILE A CA  
1838  C C   . ILE A 300 ? 0.1060 0.8571 0.2478 -0.0566 0.0140  -0.0288 309 ILE A C   
1839  O O   . ILE A 300 ? 0.1151 0.9118 0.2580 -0.0586 0.0134  -0.0236 309 ILE A O   
1840  C CB  . ILE A 300 ? 0.1024 0.8552 0.2470 -0.0451 0.0165  -0.0254 309 ILE A CB  
1841  C CG1 . ILE A 300 ? 0.1207 0.8679 0.2660 -0.0254 0.0223  -0.0366 309 ILE A CG1 
1842  C CG2 . ILE A 300 ? 0.0978 0.8093 0.2392 -0.0616 0.0105  -0.0147 309 ILE A CG2 
1843  C CD1 . ILE A 300 ? 0.1503 0.8409 0.2926 -0.0172 0.0259  -0.0531 309 ILE A CD1 
1844  N N   . ASP A 301 ? 0.1065 0.8155 0.2445 -0.0681 0.0099  -0.0244 310 ASP A N   
1845  C CA  . ASP A 301 ? 0.1123 0.8234 0.2449 -0.0858 0.0025  -0.0087 310 ASP A CA  
1846  C C   . ASP A 301 ? 0.1152 0.8471 0.2477 -0.0857 0.0031  -0.0126 310 ASP A C   
1847  O O   . ASP A 301 ? 0.1229 0.8643 0.2499 -0.0993 -0.0030 0.0016  310 ASP A O   
1848  C CB  . ASP A 301 ? 0.1182 0.8587 0.2481 -0.1006 -0.0041 0.0123  310 ASP A CB  
1849  C CG  . ASP A 301 ? 0.1279 0.8450 0.2560 -0.1044 -0.0064 0.0187  310 ASP A CG  
1850  O OD1 . ASP A 301 ? 0.1277 0.8777 0.2592 -0.1047 -0.0064 0.0256  310 ASP A OD1 
1851  O OD2 . ASP A 301 ? 0.1391 0.8068 0.2621 -0.1070 -0.0085 0.0175  310 ASP A OD2 
1852  N N   . THR A 302 ? 0.1145 0.8511 0.2511 -0.0710 0.0100  -0.0315 311 THR A N   
1853  C CA  . THR A 302 ? 0.1158 0.8669 0.2519 -0.0706 0.0109  -0.0373 311 THR A CA  
1854  C C   . THR A 302 ? 0.1244 0.8320 0.2571 -0.0745 0.0093  -0.0401 311 THR A C   
1855  O O   . THR A 302 ? 0.1351 0.8054 0.2678 -0.0707 0.0110  -0.0465 311 THR A O   
1856  C CB  . THR A 302 ? 0.1137 0.8699 0.2521 -0.0545 0.0181  -0.0585 311 THR A CB  
1857  O OG1 . THR A 302 ? 0.1208 0.8949 0.2608 -0.0431 0.0216  -0.0625 311 THR A OG1 
1858  C CG2 . THR A 302 ? 0.1433 0.9354 0.2818 -0.0536 0.0189  -0.0614 311 THR A CG2 
1859  N N   . PRO A 303 ? 0.1273 0.8407 0.2568 -0.0806 0.0064  -0.0358 312 PRO A N   
1860  C CA  . PRO A 303 ? 0.1321 0.8079 0.2574 -0.0824 0.0048  -0.0376 312 PRO A CA  
1861  C C   . PRO A 303 ? 0.1350 0.7984 0.2646 -0.0722 0.0114  -0.0585 312 PRO A C   
1862  O O   . PRO A 303 ? 0.1332 0.8219 0.2660 -0.0655 0.0157  -0.0709 312 PRO A O   
1863  C CB  . PRO A 303 ? 0.1302 0.8243 0.2502 -0.0899 0.0001  -0.0266 312 PRO A CB  
1864  C CG  . PRO A 303 ? 0.1209 0.8621 0.2459 -0.0876 0.0028  -0.0300 312 PRO A CG  
1865  C CD  . PRO A 303 ? 0.1263 0.8817 0.2549 -0.0858 0.0042  -0.0281 312 PRO A CD  
1866  N N   . CYS A 304 ? 0.1395 0.7643 0.2676 -0.0714 0.0116  -0.0623 313 CYS A N   
1867  C CA  . CYS A 304 ? 0.1432 0.7573 0.2733 -0.0663 0.0162  -0.0791 313 CYS A CA  
1868  C C   . CYS A 304 ? 0.1379 0.7370 0.2645 -0.0696 0.0136  -0.0746 313 CYS A C   
1869  O O   . CYS A 304 ? 0.1382 0.7266 0.2590 -0.0737 0.0083  -0.0596 313 CYS A O   
1870  C CB  . CYS A 304 ? 0.1504 0.7347 0.2819 -0.0613 0.0199  -0.0899 313 CYS A CB  
1871  S SG  . CYS A 304 ? 0.1784 0.7661 0.3114 -0.0552 0.0220  -0.0912 313 CYS A SG  
1872  N N   . TRP A 305 ? 0.1362 0.7340 0.2648 -0.0676 0.0169  -0.0879 314 TRP A N   
1873  C CA  . TRP A 305 ? 0.1365 0.7255 0.2627 -0.0687 0.0155  -0.0858 314 TRP A CA  
1874  C C   . TRP A 305 ? 0.1319 0.7116 0.2606 -0.0685 0.0196  -0.1009 314 TRP A C   
1875  O O   . TRP A 305 ? 0.1362 0.7227 0.2665 -0.0684 0.0230  -0.1145 314 TRP A O   
1876  C CB  . TRP A 305 ? 0.1388 0.7575 0.2629 -0.0702 0.0132  -0.0802 314 TRP A CB  
1877  C CG  . TRP A 305 ? 0.1517 0.8032 0.2796 -0.0703 0.0162  -0.0915 314 TRP A CG  
1878  C CD1 . TRP A 305 ? 0.1681 0.8330 0.2974 -0.0710 0.0188  -0.1037 314 TRP A CD1 
1879  C CD2 . TRP A 305 ? 0.1662 0.8434 0.2955 -0.0698 0.0167  -0.0913 314 TRP A CD2 
1880  N NE1 . TRP A 305 ? 0.1770 0.8706 0.3073 -0.0705 0.0206  -0.1122 314 TRP A NE1 
1881  C CE2 . TRP A 305 ? 0.1697 0.8726 0.3003 -0.0686 0.0197  -0.1049 314 TRP A CE2 
1882  C CE3 . TRP A 305 ? 0.1836 0.8671 0.3125 -0.0705 0.0146  -0.0807 314 TRP A CE3 
1883  C CZ2 . TRP A 305 ? 0.1835 0.9170 0.3146 -0.0659 0.0211  -0.1090 314 TRP A CZ2 
1884  C CZ3 . TRP A 305 ? 0.2012 0.9195 0.3320 -0.0686 0.0162  -0.0836 314 TRP A CZ3 
1885  C CH2 . TRP A 305 ? 0.2019 0.9446 0.3336 -0.0651 0.0196  -0.0982 314 TRP A CH2 
1886  N N   . LYS A 306 ? 0.1272 0.6911 0.2545 -0.0686 0.0188  -0.0980 315 LYS A N   
1887  C CA  . LYS A 306 ? 0.1256 0.6835 0.2549 -0.0711 0.0220  -0.1103 315 LYS A CA  
1888  C C   . LYS A 306 ? 0.1257 0.7086 0.2548 -0.0728 0.0213  -0.1103 315 LYS A C   
1889  O O   . LYS A 306 ? 0.1272 0.7152 0.2530 -0.0688 0.0184  -0.0984 315 LYS A O   
1890  C CB  . LYS A 306 ? 0.1238 0.6508 0.2524 -0.0702 0.0221  -0.1076 315 LYS A CB  
1891  C CG  . LYS A 306 ? 0.1254 0.6432 0.2554 -0.0753 0.0253  -0.1205 315 LYS A CG  
1892  C CD  . LYS A 306 ? 0.1485 0.6379 0.2781 -0.0743 0.0255  -0.1168 315 LYS A CD  
1893  C CE  . LYS A 306 ? 0.1687 0.6431 0.2980 -0.0812 0.0283  -0.1293 315 LYS A CE  
1894  N NZ  . LYS A 306 ? 0.1892 0.6498 0.3189 -0.0829 0.0286  -0.1255 315 LYS A NZ  
1895  N N   . LEU A 307 ? 0.1308 0.7278 0.2612 -0.0783 0.0238  -0.1239 316 LEU A N   
1896  C CA  . LEU A 307 ? 0.1362 0.7627 0.2670 -0.0815 0.0234  -0.1255 316 LEU A CA  
1897  C C   . LEU A 307 ? 0.1509 0.7739 0.2823 -0.0872 0.0245  -0.1302 316 LEU A C   
1898  O O   . LEU A 307 ? 0.1679 0.7750 0.2982 -0.0946 0.0263  -0.1416 316 LEU A O   
1899  C CB  . LEU A 307 ? 0.1361 0.7851 0.2663 -0.0861 0.0246  -0.1376 316 LEU A CB  
1900  C CG  . LEU A 307 ? 0.1324 0.8142 0.2627 -0.0918 0.0243  -0.1420 316 LEU A CG  
1901  C CD1 . LEU A 307 ? 0.1222 0.8272 0.2534 -0.0855 0.0219  -0.1275 316 LEU A CD1 
1902  C CD2 . LEU A 307 ? 0.1393 0.8375 0.2667 -0.0961 0.0252  -0.1554 316 LEU A CD2 
1903  N N   . HIS A 308 ? 0.1520 0.7906 0.2834 -0.0837 0.0232  -0.1211 317 HIS A N   
1904  C CA  . HIS A 308 ? 0.1578 0.8046 0.2905 -0.0897 0.0242  -0.1245 317 HIS A CA  
1905  C C   . HIS A 308 ? 0.1489 0.8376 0.2822 -0.0923 0.0236  -0.1250 317 HIS A C   
1906  O O   . HIS A 308 ? 0.1469 0.8541 0.2793 -0.0857 0.0221  -0.1190 317 HIS A O   
1907  C CB  . HIS A 308 ? 0.1624 0.7954 0.2939 -0.0812 0.0236  -0.1136 317 HIS A CB  
1908  C CG  . HIS A 308 ? 0.1933 0.7881 0.3226 -0.0748 0.0230  -0.1082 317 HIS A CG  
1909  N ND1 . HIS A 308 ? 0.2281 0.7943 0.3585 -0.0784 0.0246  -0.1121 317 HIS A ND1 
1910  C CD2 . HIS A 308 ? 0.2088 0.7905 0.3342 -0.0664 0.0205  -0.0987 317 HIS A CD2 
1911  C CE1 . HIS A 308 ? 0.2413 0.7799 0.3692 -0.0716 0.0233  -0.1054 317 HIS A CE1 
1912  N NE2 . HIS A 308 ? 0.2284 0.7757 0.3530 -0.0652 0.0206  -0.0972 317 HIS A NE2 
1913  N N   . THR A 309 ? 0.1477 0.8527 0.2822 -0.1026 0.0244  -0.1309 318 THR A N   
1914  C CA  . THR A 309 ? 0.1428 0.8877 0.2779 -0.1106 0.0239  -0.1360 318 THR A CA  
1915  C C   . THR A 309 ? 0.1455 0.9181 0.2821 -0.1173 0.0240  -0.1341 318 THR A C   
1916  O O   . THR A 309 ? 0.1525 0.9114 0.2889 -0.1274 0.0246  -0.1381 318 THR A O   
1917  C CB  . THR A 309 ? 0.1509 0.8851 0.2827 -0.1237 0.0243  -0.1515 318 THR A CB  
1918  O OG1 . THR A 309 ? 0.1518 0.9066 0.2831 -0.1200 0.0236  -0.1529 318 THR A OG1 
1919  C CG2 . THR A 309 ? 0.1647 0.9130 0.2936 -0.1418 0.0237  -0.1611 318 THR A CG2 
1920  N N   . SER A 310 ? 0.1444 0.9587 0.2823 -0.1116 0.0232  -0.1271 319 SER A N   
1921  C CA  . SER A 310 ? 0.1509 1.0014 0.2907 -0.1169 0.0233  -0.1240 319 SER A CA  
1922  C C   . SER A 310 ? 0.1605 1.0626 0.3014 -0.1248 0.0223  -0.1267 319 SER A C   
1923  O O   . SER A 310 ? 0.1652 1.0808 0.3054 -0.1172 0.0216  -0.1251 319 SER A O   
1924  C CB  . SER A 310 ? 0.1409 0.9975 0.2801 -0.0968 0.0235  -0.1092 319 SER A CB  
1925  O OG  . SER A 310 ? 0.1356 1.0320 0.2770 -0.1014 0.0240  -0.1063 319 SER A OG  
1926  N N   . PRO A 311 ? 0.1699 1.1031 0.3120 -0.1412 0.0219  -0.1301 320 PRO A N   
1927  C CA  . PRO A 311 ? 0.1774 1.1601 0.3197 -0.1522 0.0205  -0.1334 320 PRO A CA  
1928  C C   . PRO A 311 ? 0.1780 1.2011 0.3223 -0.1328 0.0205  -0.1219 320 PRO A C   
1929  O O   . PRO A 311 ? 0.1672 1.1902 0.3113 -0.1121 0.0213  -0.1094 320 PRO A O   
1930  C CB  . PRO A 311 ? 0.1789 1.1880 0.3223 -0.1697 0.0200  -0.1335 320 PRO A CB  
1931  C CG  . PRO A 311 ? 0.1735 1.1547 0.3182 -0.1613 0.0216  -0.1271 320 PRO A CG  
1932  C CD  . PRO A 311 ? 0.1762 1.0996 0.3185 -0.1538 0.0223  -0.1313 320 PRO A CD  
1933  N N   . LEU A 312 ? 0.1962 1.2514 0.3400 -0.1397 0.0193  -0.1267 321 LEU A N   
1934  C CA  . LEU A 312 ? 0.2084 1.3008 0.3526 -0.1229 0.0189  -0.1170 321 LEU A CA  
1935  C C   . LEU A 312 ? 0.2284 1.3814 0.3743 -0.1375 0.0176  -0.1204 321 LEU A C   
1936  O O   . LEU A 312 ? 0.2423 1.3973 0.3863 -0.1585 0.0162  -0.1337 321 LEU A O   
1937  C CB  . LEU A 312 ? 0.2017 1.2685 0.3434 -0.1159 0.0184  -0.1196 321 LEU A CB  
1938  C CG  . LEU A 312 ? 0.1940 1.2674 0.3329 -0.0923 0.0177  -0.1060 321 LEU A CG  
1939  C CD1 . LEU A 312 ? 0.1841 1.2562 0.3221 -0.0960 0.0169  -0.1117 321 LEU A CD1 
1940  C CD2 . LEU A 312 ? 0.1960 1.3222 0.3344 -0.0808 0.0171  -0.0952 321 LEU A CD2 
1941  N N   . CYS A 313 ? 0.2283 1.4307 0.3761 -0.1255 0.0177  -0.1085 322 CYS A N   
1942  C CA  . CYS A 313 ? 0.2435 1.5102 0.3935 -0.1384 0.0165  -0.1094 322 CYS A CA  
1943  C C   . CYS A 313 ? 0.2626 1.5691 0.4118 -0.1160 0.0164  -0.0979 322 CYS A C   
1944  O O   . CYS A 313 ? 0.2690 1.5614 0.4149 -0.0892 0.0172  -0.0858 322 CYS A O   
1945  C CB  . CYS A 313 ? 0.2366 1.5357 0.3895 -0.1438 0.0170  -0.1036 322 CYS A CB  
1946  S SG  . CYS A 313 ? 0.2219 1.4740 0.3742 -0.1666 0.0169  -0.1131 322 CYS A SG  
1947  N N   . THR A 314 ? 0.2884 1.6428 0.4386 -0.1267 0.0149  -0.1015 323 THR A N   
1948  C CA  . THR A 314 ? 0.3120 1.7156 0.4614 -0.1070 0.0146  -0.0901 323 THR A CA  
1949  C C   . THR A 314 ? 0.3356 1.7911 0.4861 -0.0935 0.0154  -0.0772 323 THR A C   
1950  O O   . THR A 314 ? 0.3453 1.8063 0.4989 -0.1037 0.0161  -0.0778 323 THR A O   
1951  C CB  . THR A 314 ? 0.3131 1.7629 0.4640 -0.1267 0.0128  -0.0983 323 THR A CB  
1952  O OG1 . THR A 314 ? 0.3122 1.7607 0.4640 -0.1596 0.0114  -0.1121 323 THR A OG1 
1953  C CG2 . THR A 314 ? 0.3236 1.7500 0.4716 -0.1234 0.0121  -0.1033 323 THR A CG2 
1954  N N   . THR A 315 ? 0.3572 1.8551 0.5048 -0.0707 0.0152  -0.0651 324 THR A N   
1955  C CA  . THR A 315 ? 0.3785 1.9364 0.5272 -0.0597 0.0160  -0.0542 324 THR A CA  
1956  C C   . THR A 315 ? 0.3941 2.0314 0.5450 -0.0608 0.0151  -0.0498 324 THR A C   
1957  O O   . THR A 315 ? 0.3993 2.0945 0.5508 -0.0489 0.0159  -0.0394 324 THR A O   
1958  C CB  . THR A 315 ? 0.3813 1.9204 0.5219 -0.0240 0.0174  -0.0401 324 THR A CB  
1959  O OG1 . THR A 315 ? 0.3840 1.8431 0.5188 -0.0158 0.0172  -0.0420 324 THR A OG1 
1960  C CG2 . THR A 315 ? 0.3751 1.9424 0.5201 -0.0288 0.0190  -0.0376 324 THR A CG2 
1961  N N   . ASN A 316 ? 0.4090 2.0528 0.5611 -0.0755 0.0134  -0.0578 325 ASN A N   
1962  C CA  . ASN A 316 ? 0.4243 2.1456 0.5800 -0.0878 0.0120  -0.0577 325 ASN A CA  
1963  C C   . ASN A 316 ? 0.4300 2.1500 0.5878 -0.1218 0.0097  -0.0743 325 ASN A C   
1964  O O   . ASN A 316 ? 0.4415 2.1396 0.5965 -0.1179 0.0090  -0.0782 325 ASN A O   
1965  C CB  . ASN A 316 ? 0.4294 2.1920 0.5800 -0.0546 0.0122  -0.0424 325 ASN A CB  
1966  C CG  . ASN A 316 ? 0.4468 2.2696 0.5969 -0.0341 0.0135  -0.0280 325 ASN A CG  
1967  O OD1 . ASN A 316 ? 0.4764 2.3746 0.6287 -0.0329 0.0130  -0.0222 325 ASN A OD1 
1968  N ND2 . ASN A 316 ? 0.4452 2.2377 0.5919 -0.0174 0.0153  -0.0223 325 ASN A ND2 
1969  N N   . SER A 321 ? 0.4522 2.0384 0.6147 -0.1462 0.0143  -0.0780 330 SER A N   
1970  C CA  . SER A 321 ? 0.4644 2.0925 0.6281 -0.1818 0.0110  -0.0875 330 SER A CA  
1971  C C   . SER A 321 ? 0.4605 2.0379 0.6192 -0.2045 0.0086  -0.1055 330 SER A C   
1972  O O   . SER A 321 ? 0.4543 1.9832 0.6107 -0.1883 0.0098  -0.1085 330 SER A O   
1973  C CB  . SER A 321 ? 0.4715 2.1880 0.6379 -0.1739 0.0104  -0.0778 330 SER A CB  
1974  O OG  . SER A 321 ? 0.4952 2.2181 0.6594 -0.1694 0.0093  -0.0817 330 SER A OG  
1975  N N   . ASN A 322 ? 0.4579 2.0478 0.6131 -0.2420 0.0048  -0.1169 331 ASN A N   
1976  C CA  . ASN A 322 ? 0.4541 2.0228 0.6014 -0.2641 0.0014  -0.1337 331 ASN A CA  
1977  C C   . ASN A 322 ? 0.4414 1.9238 0.5812 -0.2700 0.0012  -0.1481 331 ASN A C   
1978  O O   . ASN A 322 ? 0.4697 1.9291 0.5992 -0.3000 -0.0027 -0.1627 331 ASN A O   
1979  C CB  . ASN A 322 ? 0.4510 2.0611 0.5997 -0.2505 0.0014  -0.1314 331 ASN A CB  
1980  C CG  . ASN A 322 ? 0.4805 2.1643 0.6276 -0.2765 -0.0027 -0.1337 331 ASN A CG  
1981  O OD1 . ASN A 322 ? 0.5055 2.2490 0.6568 -0.2853 -0.0036 -0.1243 331 ASN A OD1 
1982  N ND2 . ASN A 322 ? 0.4786 2.1609 0.6191 -0.2886 -0.0054 -0.1459 331 ASN A ND2 
1983  N N   . ILE A 323 ? 0.3942 1.8284 0.5370 -0.2427 0.0049  -0.1441 332 ILE A N   
1984  C CA  . ILE A 323 ? 0.3673 1.7263 0.5031 -0.2476 0.0049  -0.1575 332 ILE A CA  
1985  C C   . ILE A 323 ? 0.3375 1.6417 0.4767 -0.2256 0.0084  -0.1514 332 ILE A C   
1986  O O   . ILE A 323 ? 0.3133 1.6253 0.4583 -0.1974 0.0111  -0.1379 332 ILE A O   
1987  C CB  . ILE A 323 ? 0.3686 1.7209 0.5001 -0.2434 0.0043  -0.1662 332 ILE A CB  
1988  C CG1 . ILE A 323 ? 0.3790 1.6631 0.5006 -0.2523 0.0035  -0.1827 332 ILE A CG1 
1989  C CG2 . ILE A 323 ? 0.3490 1.7128 0.4878 -0.2107 0.0074  -0.1527 332 ILE A CG2 
1990  C CD1 . ILE A 323 ? 0.3965 1.6767 0.5037 -0.2841 -0.0014 -0.2005 332 ILE A CD1 
1991  N N   . CYS A 324 ? 0.3262 1.5738 0.4597 -0.2387 0.0078  -0.1611 333 CYS A N   
1992  C CA  . CYS A 324 ? 0.2994 1.4900 0.4348 -0.2199 0.0108  -0.1579 333 CYS A CA  
1993  C C   . CYS A 324 ? 0.3077 1.4373 0.4349 -0.2258 0.0103  -0.1725 333 CYS A C   
1994  O O   . CYS A 324 ? 0.3216 1.4390 0.4380 -0.2490 0.0072  -0.1875 333 CYS A O   
1995  C CB  . CYS A 324 ? 0.2872 1.4691 0.4263 -0.2184 0.0121  -0.1494 333 CYS A CB  
1996  S SG  . CYS A 324 ? 0.2825 1.5418 0.4292 -0.2108 0.0127  -0.1332 333 CYS A SG  
1997  N N   . LEU A 325 ? 0.2952 1.3875 0.4260 -0.2030 0.0132  -0.1670 334 LEU A N   
1998  C CA  . LEU A 325 ? 0.2870 1.3261 0.4129 -0.1983 0.0139  -0.1761 334 LEU A CA  
1999  C C   . LEU A 325 ? 0.2762 1.2690 0.4042 -0.1883 0.0159  -0.1711 334 LEU A C   
2000  O O   . LEU A 325 ? 0.2632 1.2625 0.3980 -0.1708 0.0176  -0.1569 334 LEU A O   
2001  C CB  . LEU A 325 ? 0.2698 1.3192 0.3993 -0.1780 0.0151  -0.1699 334 LEU A CB  
2002  C CG  . LEU A 325 ? 0.2847 1.3675 0.4103 -0.1857 0.0134  -0.1781 334 LEU A CG  
2003  C CD1 . LEU A 325 ? 0.2760 1.3445 0.4016 -0.1705 0.0145  -0.1778 334 LEU A CD1 
2004  C CD2 . LEU A 325 ? 0.3258 1.3961 0.4399 -0.2113 0.0106  -0.1967 334 LEU A CD2 
2005  N N   . THR A 326 ? 0.2815 1.2261 0.4020 -0.1980 0.0155  -0.1828 335 THR A N   
2006  C CA  . THR A 326 ? 0.2691 1.1671 0.3917 -0.1858 0.0176  -0.1784 335 THR A CA  
2007  C C   . THR A 326 ? 0.2738 1.1343 0.3898 -0.1824 0.0179  -0.1894 335 THR A C   
2008  O O   . THR A 326 ? 0.2940 1.1431 0.3990 -0.1965 0.0160  -0.2044 335 THR A O   
2009  C CB  . THR A 326 ? 0.2760 1.1523 0.3966 -0.1986 0.0173  -0.1789 335 THR A CB  
2010  O OG1 . THR A 326 ? 0.2698 1.1916 0.3956 -0.2043 0.0167  -0.1699 335 THR A OG1 
2011  C CG2 . THR A 326 ? 0.2680 1.1091 0.3931 -0.1829 0.0196  -0.1707 335 THR A CG2 
2012  N N   . ARG A 327 ? 0.2558 1.0990 0.3768 -0.1634 0.0199  -0.1817 336 ARG A N   
2013  C CA  . ARG A 327 ? 0.2636 1.0798 0.3797 -0.1578 0.0205  -0.1899 336 ARG A CA  
2014  C C   . ARG A 327 ? 0.2835 1.0491 0.3925 -0.1625 0.0209  -0.1984 336 ARG A C   
2015  O O   . ARG A 327 ? 0.2769 1.0212 0.3901 -0.1591 0.0219  -0.1909 336 ARG A O   
2016  C CB  . ARG A 327 ? 0.2434 1.0630 0.3668 -0.1385 0.0217  -0.1764 336 ARG A CB  
2017  C CG  . ARG A 327 ? 0.2542 1.0733 0.3747 -0.1325 0.0220  -0.1818 336 ARG A CG  
2018  C CD  . ARG A 327 ? 0.2375 1.0855 0.3636 -0.1201 0.0216  -0.1679 336 ARG A CD  
2019  N NE  . ARG A 327 ? 0.2224 1.0486 0.3517 -0.1072 0.0218  -0.1544 336 ARG A NE  
2020  C CZ  . ARG A 327 ? 0.2200 1.0262 0.3482 -0.1019 0.0225  -0.1554 336 ARG A CZ  
2021  N NH1 . ARG A 327 ? 0.2255 1.0283 0.3489 -0.1053 0.0235  -0.1700 336 ARG A NH1 
2022  N NH2 . ARG A 327 ? 0.2124 1.0019 0.3426 -0.0929 0.0217  -0.1417 336 ARG A NH2 
2023  N N   . THR A 328 ? 0.3143 1.0598 0.4110 -0.1695 0.0199  -0.2144 337 THR A N   
2024  C CA  . THR A 328 ? 0.3507 1.0485 0.4364 -0.1767 0.0193  -0.2241 337 THR A CA  
2025  C C   . THR A 328 ? 0.3473 1.0096 0.4354 -0.1611 0.0218  -0.2204 337 THR A C   
2026  O O   . THR A 328 ? 0.3552 0.9867 0.4431 -0.1626 0.0222  -0.2177 337 THR A O   
2027  C CB  . THR A 328 ? 0.3876 1.0695 0.4540 -0.1874 0.0167  -0.2433 337 THR A CB  
2028  O OG1 . THR A 328 ? 0.4217 1.1258 0.4820 -0.2088 0.0132  -0.2478 337 THR A OG1 
2029  C CG2 . THR A 328 ? 0.4246 1.0488 0.4763 -0.1883 0.0161  -0.2532 337 THR A CG2 
2030  N N   . ASP A 329 ? 0.3399 1.0101 0.4302 -0.1468 0.0232  -0.2198 338 ASP A N   
2031  C CA  . ASP A 329 ? 0.3420 0.9839 0.4322 -0.1325 0.0252  -0.2187 338 ASP A CA  
2032  C C   . ASP A 329 ? 0.3008 0.9344 0.4037 -0.1228 0.0267  -0.2018 338 ASP A C   
2033  O O   . ASP A 329 ? 0.2829 0.9312 0.3933 -0.1117 0.0273  -0.1913 338 ASP A O   
2034  C CB  . ASP A 329 ? 0.3586 1.0229 0.4473 -0.1222 0.0258  -0.2224 338 ASP A CB  
2035  C CG  . ASP A 329 ? 0.3884 1.1032 0.4855 -0.1236 0.0250  -0.2146 338 ASP A CG  
2036  O OD1 . ASP A 329 ? 0.4339 1.1726 0.5273 -0.1200 0.0249  -0.2204 338 ASP A OD1 
2037  O OD2 . ASP A 329 ? 0.3917 1.1228 0.4979 -0.1268 0.0245  -0.2026 338 ASP A OD2 
2038  N N   . ARG A 330 ? 0.2832 0.8923 0.3870 -0.1277 0.0267  -0.1985 339 ARG A N   
2039  C CA  . ARG A 330 ? 0.2499 0.8521 0.3636 -0.1181 0.0276  -0.1831 339 ARG A CA  
2040  C C   . ARG A 330 ? 0.2446 0.8108 0.3554 -0.1106 0.0289  -0.1849 339 ARG A C   
2041  O O   . ARG A 330 ? 0.2627 0.8043 0.3632 -0.1137 0.0291  -0.1978 339 ARG A O   
2042  C CB  . ARG A 330 ? 0.2480 0.8479 0.3654 -0.1247 0.0273  -0.1763 339 ARG A CB  
2043  C CG  . ARG A 330 ? 0.2641 0.8962 0.3813 -0.1370 0.0260  -0.1783 339 ARG A CG  
2044  C CD  . ARG A 330 ? 0.2883 0.9043 0.4029 -0.1497 0.0256  -0.1799 339 ARG A CD  
2045  N NE  . ARG A 330 ? 0.2837 0.9346 0.3988 -0.1630 0.0241  -0.1795 339 ARG A NE  
2046  C CZ  . ARG A 330 ? 0.2711 0.9480 0.3940 -0.1596 0.0245  -0.1673 339 ARG A CZ  
2047  N NH1 . ARG A 330 ? 0.2747 0.9407 0.4034 -0.1431 0.0258  -0.1553 339 ARG A NH1 
2048  N NH2 . ARG A 330 ? 0.2441 0.9579 0.3673 -0.1722 0.0232  -0.1672 339 ARG A NH2 
2049  N N   . GLY A 331 ? 0.2185 0.7803 0.3366 -0.1008 0.0293  -0.1717 340 GLY A N   
2050  C CA  . GLY A 331 ? 0.2141 0.7459 0.3307 -0.0934 0.0304  -0.1715 340 GLY A CA  
2051  C C   . GLY A 331 ? 0.1944 0.7380 0.3159 -0.0829 0.0301  -0.1608 340 GLY A C   
2052  O O   . GLY A 331 ? 0.1815 0.7499 0.3075 -0.0815 0.0285  -0.1503 340 GLY A O   
2053  N N   . TRP A 332 ? 0.1908 0.7165 0.3102 -0.0760 0.0312  -0.1626 341 TRP A N   
2054  C CA  . TRP A 332 ? 0.1769 0.7145 0.3003 -0.0686 0.0305  -0.1518 341 TRP A CA  
2055  C C   . TRP A 332 ? 0.1855 0.7511 0.3067 -0.0643 0.0312  -0.1574 341 TRP A C   
2056  O O   . TRP A 332 ? 0.2026 0.7630 0.3163 -0.0604 0.0330  -0.1715 341 TRP A O   
2057  C CB  . TRP A 332 ? 0.1783 0.6893 0.3012 -0.0631 0.0314  -0.1496 341 TRP A CB  
2058  C CG  . TRP A 332 ? 0.1669 0.6568 0.2929 -0.0653 0.0303  -0.1397 341 TRP A CG  
2059  C CD1 . TRP A 332 ? 0.1775 0.6394 0.3017 -0.0684 0.0313  -0.1440 341 TRP A CD1 
2060  C CD2 . TRP A 332 ? 0.1517 0.6444 0.2811 -0.0646 0.0273  -0.1231 341 TRP A CD2 
2061  N NE1 . TRP A 332 ? 0.1776 0.6273 0.3051 -0.0684 0.0297  -0.1317 341 TRP A NE1 
2062  C CE2 . TRP A 332 ? 0.1524 0.6181 0.2818 -0.0658 0.0270  -0.1192 341 TRP A CE2 
2063  C CE3 . TRP A 332 ? 0.1427 0.6563 0.2728 -0.0640 0.0243  -0.1110 341 TRP A CE3 
2064  C CZ2 . TRP A 332 ? 0.1384 0.5953 0.2671 -0.0647 0.0237  -0.1047 341 TRP A CZ2 
2065  C CZ3 . TRP A 332 ? 0.1240 0.6258 0.2523 -0.0646 0.0204  -0.0960 341 TRP A CZ3 
2066  C CH2 . TRP A 332 ? 0.1176 0.5906 0.2446 -0.0643 0.0201  -0.0936 341 TRP A CH2 
2067  N N   . TYR A 333 ? 0.1764 0.7709 0.3020 -0.0642 0.0292  -0.1459 342 TYR A N   
2068  C CA  . TYR A 333 ? 0.1746 0.7998 0.2997 -0.0595 0.0295  -0.1467 342 TYR A CA  
2069  C C   . TYR A 333 ? 0.1680 0.7955 0.2966 -0.0563 0.0280  -0.1319 342 TYR A C   
2070  O O   . TYR A 333 ? 0.1595 0.7658 0.2899 -0.0590 0.0259  -0.1209 342 TYR A O   
2071  C CB  . TYR A 333 ? 0.1671 0.8247 0.2938 -0.0638 0.0278  -0.1430 342 TYR A CB  
2072  C CG  . TYR A 333 ? 0.1802 0.8386 0.3033 -0.0688 0.0288  -0.1569 342 TYR A CG  
2073  C CD1 . TYR A 333 ? 0.1892 0.8325 0.3134 -0.0753 0.0282  -0.1560 342 TYR A CD1 
2074  C CD2 . TYR A 333 ? 0.2075 0.8827 0.3247 -0.0675 0.0302  -0.1711 342 TYR A CD2 
2075  C CE1 . TYR A 333 ? 0.2094 0.8570 0.3298 -0.0825 0.0286  -0.1679 342 TYR A CE1 
2076  C CE2 . TYR A 333 ? 0.2198 0.8950 0.3317 -0.0745 0.0303  -0.1838 342 TYR A CE2 
2077  C CZ  . TYR A 333 ? 0.2247 0.8873 0.3386 -0.0831 0.0293  -0.1817 342 TYR A CZ  
2078  O OH  . TYR A 333 ? 0.2624 0.9286 0.3706 -0.0926 0.0288  -0.1936 342 TYR A OH  
2079  N N   . CYS A 334 ? 0.1727 0.8275 0.3011 -0.0510 0.0286  -0.1311 343 CYS A N   
2080  C CA  . CYS A 334 ? 0.1715 0.8289 0.3021 -0.0484 0.0275  -0.1196 343 CYS A CA  
2081  C C   . CYS A 334 ? 0.1754 0.8710 0.3050 -0.0407 0.0292  -0.1227 343 CYS A C   
2082  O O   . CYS A 334 ? 0.1908 0.8866 0.3150 -0.0314 0.0328  -0.1391 343 CYS A O   
2083  C CB  . CYS A 334 ? 0.1754 0.7941 0.3044 -0.0447 0.0294  -0.1257 343 CYS A CB  
2084  S SG  . CYS A 334 ? 0.2010 0.8150 0.3324 -0.0426 0.0282  -0.1132 343 CYS A SG  
2085  N N   . ASP A 335 ? 0.1701 0.8983 0.3029 -0.0448 0.0263  -0.1069 344 ASP A N   
2086  C CA  . ASP A 335 ? 0.1710 0.9464 0.3037 -0.0390 0.0275  -0.1075 344 ASP A CA  
2087  C C   . ASP A 335 ? 0.1781 0.9621 0.3088 -0.0255 0.0311  -0.1142 344 ASP A C   
2088  O O   . ASP A 335 ? 0.1806 0.9528 0.3132 -0.0251 0.0304  -0.1065 344 ASP A O   
2089  C CB  . ASP A 335 ? 0.1644 0.9704 0.3001 -0.0496 0.0226  -0.0857 344 ASP A CB  
2090  C CG  . ASP A 335 ? 0.1831 1.0008 0.3182 -0.0578 0.0198  -0.0808 344 ASP A CG  
2091  O OD1 . ASP A 335 ? 0.2220 1.0631 0.3562 -0.0530 0.0224  -0.0921 344 ASP A OD1 
2092  O OD2 . ASP A 335 ? 0.1999 1.0036 0.3335 -0.0685 0.0146  -0.0655 344 ASP A OD2 
2093  N N   . ASN A 336 ? 0.1925 0.9982 0.3179 -0.0130 0.0346  -0.1287 345 ASN A N   
2094  C CA  . ASN A 336 ? 0.2066 1.0295 0.3283 0.0031  0.0378  -0.1336 345 ASN A CA  
2095  C C   . ASN A 336 ? 0.2126 1.0979 0.3363 0.0066  0.0378  -0.1263 345 ASN A C   
2096  O O   . ASN A 336 ? 0.2159 1.1257 0.3452 -0.0072 0.0343  -0.1125 345 ASN A O   
2097  C CB  . ASN A 336 ? 0.2282 1.0232 0.3375 0.0183  0.0418  -0.1574 345 ASN A CB  
2098  C CG  . ASN A 336 ? 0.2310 1.0179 0.3347 0.0346  0.0444  -0.1617 345 ASN A CG  
2099  O OD1 . ASN A 336 ? 0.1912 0.9521 0.2988 0.0312  0.0437  -0.1546 345 ASN A OD1 
2100  N ND2 . ASN A 336 ? 0.2809 1.0919 0.3745 0.0540  0.0475  -0.1731 345 ASN A ND2 
2101  N N   . ALA A 337 ? 0.2204 1.1325 0.3381 0.0255  0.0415  -0.1350 346 ALA A N   
2102  C CA  . ALA A 337 ? 0.2130 1.1894 0.3333 0.0289  0.0416  -0.1264 346 ALA A CA  
2103  C C   . ALA A 337 ? 0.2140 1.2143 0.3335 0.0232  0.0408  -0.1298 346 ALA A C   
2104  O O   . ALA A 337 ? 0.2268 1.2372 0.3368 0.0372  0.0439  -0.1475 346 ALA A O   
2105  C CB  . ALA A 337 ? 0.2285 1.2282 0.3407 0.0534  0.0461  -0.1368 346 ALA A CB  
2106  N N   . GLY A 338 ? 0.2042 1.2118 0.3319 0.0027  0.0362  -0.1125 347 GLY A N   
2107  C CA  . GLY A 338 ? 0.2065 1.2424 0.3347 -0.0044 0.0347  -0.1113 347 GLY A CA  
2108  C C   . GLY A 338 ? 0.2151 1.2152 0.3381 -0.0050 0.0357  -0.1287 347 GLY A C   
2109  O O   . GLY A 338 ? 0.2217 1.2418 0.3446 -0.0108 0.0346  -0.1293 347 GLY A O   
2110  N N   . SER A 339 ? 0.2136 1.1630 0.3318 0.0002  0.0375  -0.1421 348 SER A N   
2111  C CA  . SER A 339 ? 0.2153 1.1311 0.3265 -0.0004 0.0384  -0.1601 348 SER A CA  
2112  C C   . SER A 339 ? 0.2062 1.0728 0.3209 -0.0094 0.0368  -0.1557 348 SER A C   
2113  O O   . SER A 339 ? 0.1921 1.0568 0.3136 -0.0137 0.0351  -0.1398 348 SER A O   
2114  C CB  . SER A 339 ? 0.2394 1.1465 0.3355 0.0181  0.0422  -0.1841 348 SER A CB  
2115  O OG  . SER A 339 ? 0.2427 1.2014 0.3347 0.0288  0.0438  -0.1876 348 SER A OG  
2116  N N   . VAL A 340 ? 0.2133 1.0434 0.3232 -0.0136 0.0370  -0.1686 349 VAL A N   
2117  C CA  . VAL A 340 ? 0.2063 0.9926 0.3198 -0.0229 0.0355  -0.1641 349 VAL A CA  
2118  C C   . VAL A 340 ? 0.2260 0.9692 0.3295 -0.0175 0.0376  -0.1822 349 VAL A C   
2119  O O   . VAL A 340 ? 0.2449 0.9829 0.3379 -0.0151 0.0385  -0.1991 349 VAL A O   
2120  C CB  . VAL A 340 ? 0.1943 0.9785 0.3121 -0.0364 0.0329  -0.1590 349 VAL A CB  
2121  C CG1 . VAL A 340 ? 0.1849 0.9314 0.3070 -0.0437 0.0312  -0.1503 349 VAL A CG1 
2122  C CG2 . VAL A 340 ? 0.1841 1.0111 0.3077 -0.0419 0.0302  -0.1436 349 VAL A CG2 
2123  N N   . SER A 341 ? 0.2314 0.9421 0.3365 -0.0166 0.0378  -0.1782 350 SER A N   
2124  C CA  . SER A 341 ? 0.2585 0.9240 0.3529 -0.0126 0.0393  -0.1935 350 SER A CA  
2125  C C   . SER A 341 ? 0.2650 0.8988 0.3630 -0.0270 0.0375  -0.1915 350 SER A C   
2126  O O   . SER A 341 ? 0.2462 0.8779 0.3549 -0.0346 0.0358  -0.1757 350 SER A O   
2127  C CB  . SER A 341 ? 0.2596 0.9093 0.3514 -0.0001 0.0411  -0.1924 350 SER A CB  
2128  O OG  . SER A 341 ? 0.2549 0.9257 0.3372 0.0171  0.0434  -0.2017 350 SER A OG  
2129  N N   . PHE A 342 ? 0.2977 0.9068 0.3844 -0.0306 0.0376  -0.2078 351 PHE A N   
2130  C CA  . PHE A 342 ? 0.3105 0.8942 0.3989 -0.0446 0.0361  -0.2077 351 PHE A CA  
2131  C C   . PHE A 342 ? 0.3453 0.8804 0.4224 -0.0442 0.0366  -0.2182 351 PHE A C   
2132  O O   . PHE A 342 ? 0.3749 0.8921 0.4352 -0.0371 0.0371  -0.2342 351 PHE A O   
2133  C CB  . PHE A 342 ? 0.3118 0.9141 0.3970 -0.0542 0.0347  -0.2152 351 PHE A CB  
2134  C CG  . PHE A 342 ? 0.3209 0.9016 0.4048 -0.0685 0.0332  -0.2180 351 PHE A CG  
2135  C CD1 . PHE A 342 ? 0.3110 0.8873 0.4066 -0.0747 0.0325  -0.2039 351 PHE A CD1 
2136  C CD2 . PHE A 342 ? 0.3528 0.9175 0.4219 -0.0759 0.0320  -0.2347 351 PHE A CD2 
2137  C CE1 . PHE A 342 ? 0.3227 0.8846 0.4172 -0.0871 0.0314  -0.2059 351 PHE A CE1 
2138  C CE2 . PHE A 342 ? 0.3629 0.9120 0.4308 -0.0912 0.0303  -0.2359 351 PHE A CE2 
2139  C CZ  . PHE A 342 ? 0.3456 0.8960 0.4272 -0.0962 0.0303  -0.2213 351 PHE A CZ  
2140  N N   . PHE A 343 ? 0.3484 0.8613 0.4328 -0.0511 0.0361  -0.2090 352 PHE A N   
2141  C CA  . PHE A 343 ? 0.3832 0.8511 0.4586 -0.0519 0.0363  -0.2154 352 PHE A CA  
2142  C C   . PHE A 343 ? 0.4089 0.8641 0.4845 -0.0687 0.0345  -0.2164 352 PHE A C   
2143  O O   . PHE A 343 ? 0.3926 0.8552 0.4809 -0.0752 0.0340  -0.2033 352 PHE A O   
2144  C CB  . PHE A 343 ? 0.3644 0.8203 0.4484 -0.0454 0.0373  -0.2029 352 PHE A CB  
2145  C CG  . PHE A 343 ? 0.3466 0.8312 0.4370 -0.0334 0.0383  -0.1946 352 PHE A CG  
2146  C CD1 . PHE A 343 ? 0.3174 0.8369 0.4204 -0.0372 0.0370  -0.1802 352 PHE A CD1 
2147  C CD2 . PHE A 343 ? 0.3519 0.8304 0.4340 -0.0183 0.0402  -0.2004 352 PHE A CD2 
2148  C CE1 . PHE A 343 ? 0.2923 0.8410 0.4002 -0.0292 0.0372  -0.1711 352 PHE A CE1 
2149  C CE2 . PHE A 343 ? 0.3212 0.8330 0.4097 -0.0085 0.0410  -0.1916 352 PHE A CE2 
2150  C CZ  . PHE A 343 ? 0.2938 0.8411 0.3956 -0.0156 0.0393  -0.1765 352 PHE A CZ  
2151  N N   . PRO A 344 ? 0.4582 0.8934 0.5176 -0.0759 0.0331  -0.2317 353 PRO A N   
2152  C CA  . PRO A 344 ? 0.4858 0.9192 0.5430 -0.0944 0.0308  -0.2345 353 PRO A CA  
2153  C C   . PRO A 344 ? 0.5018 0.9181 0.5667 -0.1041 0.0305  -0.2246 353 PRO A C   
2154  O O   . PRO A 344 ? 0.4976 0.9340 0.5702 -0.1164 0.0294  -0.2188 353 PRO A O   
2155  C CB  . PRO A 344 ? 0.5254 0.9282 0.5579 -0.0986 0.0287  -0.2536 353 PRO A CB  
2156  C CG  . PRO A 344 ? 0.5253 0.9302 0.5496 -0.0789 0.0304  -0.2608 353 PRO A CG  
2157  C CD  . PRO A 344 ? 0.4902 0.8979 0.5290 -0.0660 0.0332  -0.2474 353 PRO A CD  
2158  N N   . GLN A 345 ? 0.5295 0.9125 0.5921 -0.0979 0.0315  -0.2224 354 GLN A N   
2159  C CA  . GLN A 345 ? 0.5453 0.9087 0.6124 -0.1074 0.0312  -0.2148 354 GLN A CA  
2160  C C   . GLN A 345 ? 0.5313 0.8840 0.6087 -0.0961 0.0332  -0.2026 354 GLN A C   
2161  O O   . GLN A 345 ? 0.5304 0.8721 0.6048 -0.0823 0.0345  -0.2040 354 GLN A O   
2162  C CB  . GLN A 345 ? 0.5840 0.9087 0.6321 -0.1211 0.0287  -0.2262 354 GLN A CB  
2163  C CG  . GLN A 345 ? 0.6337 0.9285 0.6577 -0.1154 0.0273  -0.2437 354 GLN A CG  
2164  C CD  . GLN A 345 ? 0.6339 0.9122 0.6554 -0.0932 0.0299  -0.2440 354 GLN A CD  
2165  O OE1 . GLN A 345 ? 0.6382 0.8927 0.6622 -0.0889 0.0310  -0.2376 354 GLN A OE1 
2166  N NE2 . GLN A 345 ? 0.6109 0.9062 0.6283 -0.0787 0.0310  -0.2505 354 GLN A NE2 
2167  N N   . ALA A 346 ? 0.5201 0.8791 0.6089 -0.1017 0.0331  -0.1907 355 ALA A N   
2168  C CA  . ALA A 346 ? 0.5049 0.8548 0.6031 -0.0933 0.0342  -0.1778 355 ALA A CA  
2169  C C   . ALA A 346 ? 0.5112 0.8329 0.6032 -0.0819 0.0355  -0.1810 355 ALA A C   
2170  O O   . ALA A 346 ? 0.5061 0.8406 0.6027 -0.0700 0.0363  -0.1766 355 ALA A O   
2171  C CB  . ALA A 346 ? 0.4964 0.8386 0.5989 -0.1027 0.0338  -0.1704 355 ALA A CB  
2172  N N   . GLU A 347 ? 0.5166 0.8026 0.5977 -0.0863 0.0353  -0.1876 356 GLU A N   
2173  C CA  . GLU A 347 ? 0.5211 0.7746 0.5879 -0.0770 0.0359  -0.1968 356 GLU A CA  
2174  C C   . GLU A 347 ? 0.4946 0.7597 0.5634 -0.0590 0.0376  -0.1957 356 GLU A C   
2175  O O   . GLU A 347 ? 0.4877 0.7420 0.5596 -0.0493 0.0389  -0.1892 356 GLU A O   
2176  C CB  . GLU A 347 ? 0.5602 0.7963 0.6076 -0.0851 0.0339  -0.2126 356 GLU A CB  
2177  C CG  . GLU A 347 ? 0.6094 0.8290 0.6522 -0.1043 0.0317  -0.2128 356 GLU A CG  
2178  C CD  . GLU A 347 ? 0.6680 0.8708 0.7189 -0.1037 0.0329  -0.2013 356 GLU A CD  
2179  O OE1 . GLU A 347 ? 0.6715 0.8918 0.7351 -0.1131 0.0328  -0.1912 356 GLU A OE1 
2180  O OE2 . GLU A 347 ? 0.6930 0.8676 0.7375 -0.0918 0.0339  -0.2021 356 GLU A OE2 
2181  N N   . THR A 348 ? 0.4694 0.7602 0.5365 -0.0553 0.0376  -0.2015 357 THR A N   
2182  C CA  . THR A 348 ? 0.4413 0.7519 0.5096 -0.0393 0.0391  -0.2009 357 THR A CA  
2183  C C   . THR A 348 ? 0.3965 0.7338 0.4825 -0.0363 0.0395  -0.1841 357 THR A C   
2184  O O   . THR A 348 ? 0.4018 0.7502 0.4891 -0.0237 0.0406  -0.1806 357 THR A O   
2185  C CB  . THR A 348 ? 0.4439 0.7818 0.5084 -0.0384 0.0388  -0.2090 357 THR A CB  
2186  O OG1 . THR A 348 ? 0.4673 0.7941 0.5229 -0.0528 0.0369  -0.2185 357 THR A OG1 
2187  C CG2 . THR A 348 ? 0.4704 0.8038 0.5210 -0.0213 0.0401  -0.2194 357 THR A CG2 
2188  N N   . CYS A 349 ? 0.3479 0.6956 0.4453 -0.0472 0.0381  -0.1734 358 CYS A N   
2189  C CA  . CYS A 349 ? 0.2978 0.6675 0.4075 -0.0455 0.0371  -0.1575 358 CYS A CA  
2190  C C   . CYS A 349 ? 0.2711 0.6226 0.3862 -0.0492 0.0361  -0.1468 358 CYS A C   
2191  O O   . CYS A 349 ? 0.2741 0.6091 0.3880 -0.0566 0.0361  -0.1488 358 CYS A O   
2192  C CB  . CYS A 349 ? 0.2804 0.6826 0.3956 -0.0512 0.0355  -0.1534 358 CYS A CB  
2193  S SG  . CYS A 349 ? 0.3061 0.7370 0.4155 -0.0449 0.0365  -0.1646 358 CYS A SG  
2194  N N   . LYS A 350 ? 0.2491 0.6043 0.3689 -0.0444 0.0352  -0.1353 359 LYS A N   
2195  C CA  . LYS A 350 ? 0.2365 0.5780 0.3604 -0.0483 0.0334  -0.1238 359 LYS A CA  
2196  C C   . LYS A 350 ? 0.2157 0.5762 0.3433 -0.0488 0.0301  -0.1102 359 LYS A C   
2197  O O   . LYS A 350 ? 0.2176 0.6005 0.3461 -0.0455 0.0298  -0.1085 359 LYS A O   
2198  C CB  . LYS A 350 ? 0.2468 0.5606 0.3689 -0.0442 0.0345  -0.1231 359 LYS A CB  
2199  C CG  . LYS A 350 ? 0.2860 0.5952 0.4031 -0.0347 0.0369  -0.1312 359 LYS A CG  
2200  C CD  . LYS A 350 ? 0.3342 0.6076 0.4448 -0.0337 0.0387  -0.1379 359 LYS A CD  
2201  C CE  . LYS A 350 ? 0.3829 0.6477 0.4824 -0.0235 0.0408  -0.1507 359 LYS A CE  
2202  N NZ  . LYS A 350 ? 0.4519 0.6781 0.5410 -0.0257 0.0414  -0.1587 359 LYS A NZ  
2203  N N   . VAL A 351 ? 0.2023 0.5530 0.3304 -0.0529 0.0273  -0.1003 360 VAL A N   
2204  C CA  . VAL A 351 ? 0.1900 0.5537 0.3170 -0.0556 0.0228  -0.0873 360 VAL A CA  
2205  C C   . VAL A 351 ? 0.1906 0.5311 0.3137 -0.0567 0.0193  -0.0762 360 VAL A C   
2206  O O   . VAL A 351 ? 0.1938 0.5138 0.3164 -0.0559 0.0206  -0.0785 360 VAL A O   
2207  C CB  . VAL A 351 ? 0.1802 0.5594 0.3065 -0.0584 0.0220  -0.0885 360 VAL A CB  
2208  C CG1 . VAL A 351 ? 0.1859 0.5519 0.3123 -0.0595 0.0240  -0.0948 360 VAL A CG1 
2209  C CG2 . VAL A 351 ? 0.1853 0.5679 0.3064 -0.0604 0.0166  -0.0748 360 VAL A CG2 
2210  N N   . GLN A 352 ? 0.1945 0.5388 0.3137 -0.0594 0.0146  -0.0639 361 GLN A N   
2211  C CA  . GLN A 352 ? 0.2144 0.5349 0.3272 -0.0610 0.0105  -0.0538 361 GLN A CA  
2212  C C   . GLN A 352 ? 0.2162 0.5405 0.3194 -0.0667 0.0034  -0.0407 361 GLN A C   
2213  O O   . GLN A 352 ? 0.2306 0.5707 0.3329 -0.0718 0.0006  -0.0335 361 GLN A O   
2214  C CB  . GLN A 352 ? 0.2221 0.5404 0.3381 -0.0602 0.0114  -0.0525 361 GLN A CB  
2215  C CG  . GLN A 352 ? 0.2891 0.5853 0.3980 -0.0635 0.0067  -0.0417 361 GLN A CG  
2216  C CD  . GLN A 352 ? 0.4087 0.6865 0.5220 -0.0583 0.0108  -0.0474 361 GLN A CD  
2217  O OE1 . GLN A 352 ? 0.4497 0.7320 0.5654 -0.0574 0.0112  -0.0447 361 GLN A OE1 
2218  N NE2 . GLN A 352 ? 0.4370 0.6967 0.5511 -0.0548 0.0140  -0.0548 361 GLN A NE2 
2219  N N   . SER A 353 ? 0.2166 0.5255 0.3104 -0.0657 0.0001  -0.0366 362 SER A N   
2220  C CA  . SER A 353 ? 0.2195 0.5283 0.3005 -0.0704 -0.0071 -0.0248 362 SER A CA  
2221  C C   . SER A 353 ? 0.2044 0.5470 0.2919 -0.0722 -0.0053 -0.0275 362 SER A C   
2222  O O   . SER A 353 ? 0.1998 0.5555 0.2955 -0.0675 0.0000  -0.0382 362 SER A O   
2223  C CB  . SER A 353 ? 0.2332 0.5313 0.3047 -0.0790 -0.0138 -0.0121 362 SER A CB  
2224  O OG  . SER A 353 ? 0.2603 0.5474 0.3139 -0.0838 -0.0220 -0.0005 362 SER A OG  
2225  N N   . ASN A 354 ? 0.2023 0.5604 0.2856 -0.0800 -0.0100 -0.0178 363 ASN A N   
2226  C CA  . ASN A 354 ? 0.1922 0.5841 0.2804 -0.0813 -0.0087 -0.0195 363 ASN A CA  
2227  C C   . ASN A 354 ? 0.1733 0.5945 0.2746 -0.0811 -0.0037 -0.0260 363 ASN A C   
2228  O O   . ASN A 354 ? 0.1718 0.6251 0.2761 -0.0838 -0.0036 -0.0246 363 ASN A O   
2229  C CB  . ASN A 354 ? 0.2089 0.6033 0.2831 -0.0900 -0.0170 -0.0042 363 ASN A CB  
2230  C CG  . ASN A 354 ? 0.2194 0.6134 0.2882 -0.1010 -0.0225 0.0080  363 ASN A CG  
2231  O OD1 . ASN A 354 ? 0.2111 0.5970 0.2846 -0.1008 -0.0207 0.0061  363 ASN A OD1 
2232  N ND2 . ASN A 354 ? 0.2412 0.6449 0.2990 -0.1117 -0.0296 0.0214  363 ASN A ND2 
2233  N N   . ARG A 355 ? 0.1572 0.5675 0.2650 -0.0765 0.0006  -0.0334 364 ARG A N   
2234  C CA  . ARG A 355 ? 0.1488 0.5827 0.2660 -0.0727 0.0054  -0.0403 364 ARG A CA  
2235  C C   . ARG A 355 ? 0.1422 0.5739 0.2662 -0.0639 0.0125  -0.0576 364 ARG A C   
2236  O O   . ARG A 355 ? 0.1453 0.5505 0.2689 -0.0615 0.0142  -0.0628 364 ARG A O   
2237  C CB  . ARG A 355 ? 0.1505 0.5726 0.2677 -0.0733 0.0045  -0.0353 364 ARG A CB  
2238  C CG  . ARG A 355 ? 0.1582 0.6132 0.2798 -0.0732 0.0052  -0.0322 364 ARG A CG  
2239  C CD  . ARG A 355 ? 0.1575 0.6370 0.2742 -0.0841 -0.0008 -0.0185 364 ARG A CD  
2240  N NE  . ARG A 355 ? 0.1704 0.6923 0.2943 -0.0788 0.0032  -0.0237 364 ARG A NE  
2241  C CZ  . ARG A 355 ? 0.1756 0.7342 0.2989 -0.0863 -0.0003 -0.0124 364 ARG A CZ  
2242  N NH1 . ARG A 355 ? 0.1835 0.7378 0.2980 -0.1016 -0.0085 0.0053  364 ARG A NH1 
2243  N NH2 . ARG A 355 ? 0.1873 0.7861 0.3169 -0.0789 0.0041  -0.0186 364 ARG A NH2 
2244  N N   . VAL A 356 ? 0.1425 0.6018 0.2709 -0.0597 0.0161  -0.0663 365 VAL A N   
2245  C CA  . VAL A 356 ? 0.1435 0.5990 0.2743 -0.0530 0.0218  -0.0837 365 VAL A CA  
2246  C C   . VAL A 356 ? 0.1589 0.6266 0.2910 -0.0439 0.0258  -0.0922 365 VAL A C   
2247  O O   . VAL A 356 ? 0.1705 0.6671 0.3038 -0.0422 0.0248  -0.0857 365 VAL A O   
2248  C CB  . VAL A 356 ? 0.1357 0.6128 0.2668 -0.0545 0.0223  -0.0890 365 VAL A CB  
2249  C CG1 . VAL A 356 ? 0.1354 0.6120 0.2662 -0.0486 0.0272  -0.1067 365 VAL A CG1 
2250  C CG2 . VAL A 356 ? 0.1361 0.6016 0.2649 -0.0598 0.0196  -0.0843 365 VAL A CG2 
2251  N N   . PHE A 357 ? 0.1665 0.6133 0.2965 -0.0377 0.0298  -0.1064 366 PHE A N   
2252  C CA  . PHE A 357 ? 0.1779 0.6255 0.3049 -0.0259 0.0333  -0.1151 366 PHE A CA  
2253  C C   . PHE A 357 ? 0.1931 0.6271 0.3135 -0.0219 0.0364  -0.1325 366 PHE A C   
2254  O O   . PHE A 357 ? 0.1994 0.6023 0.3168 -0.0255 0.0370  -0.1383 366 PHE A O   
2255  C CB  . PHE A 357 ? 0.1781 0.5990 0.3047 -0.0225 0.0338  -0.1117 366 PHE A CB  
2256  C CG  . PHE A 357 ? 0.1604 0.5916 0.2913 -0.0274 0.0301  -0.0945 366 PHE A CG  
2257  C CD1 . PHE A 357 ? 0.1539 0.5742 0.2858 -0.0389 0.0257  -0.0832 366 PHE A CD1 
2258  C CD2 . PHE A 357 ? 0.1509 0.6013 0.2826 -0.0203 0.0306  -0.0898 366 PHE A CD2 
2259  C CE1 . PHE A 357 ? 0.1372 0.5614 0.2690 -0.0451 0.0212  -0.0680 366 PHE A CE1 
2260  C CE2 . PHE A 357 ? 0.1313 0.5912 0.2655 -0.0276 0.0265  -0.0738 366 PHE A CE2 
2261  C CZ  . PHE A 357 ? 0.1237 0.5678 0.2570 -0.0409 0.0215  -0.0632 366 PHE A CZ  
2262  N N   . CYS A 358 ? 0.2095 0.6671 0.3261 -0.0151 0.0380  -0.1409 367 CYS A N   
2263  C CA  . CYS A 358 ? 0.2429 0.6851 0.3494 -0.0125 0.0399  -0.1585 367 CYS A CA  
2264  C C   . CYS A 358 ? 0.2691 0.7104 0.3640 0.0044  0.0426  -0.1706 367 CYS A C   
2265  O O   . CYS A 358 ? 0.2741 0.7374 0.3709 0.0151  0.0435  -0.1649 367 CYS A O   
2266  C CB  . CYS A 358 ? 0.2411 0.7080 0.3491 -0.0198 0.0388  -0.1611 367 CYS A CB  
2267  S SG  . CYS A 358 ? 0.2413 0.7086 0.3585 -0.0361 0.0357  -0.1495 367 CYS A SG  
2268  N N   . ASP A 359 ? 0.2959 0.7125 0.3768 0.0067  0.0434  -0.1872 368 ASP A N   
2269  C CA  . ASP A 359 ? 0.3322 0.7371 0.3969 0.0245  0.0454  -0.1999 368 ASP A CA  
2270  C C   . ASP A 359 ? 0.3578 0.7793 0.4117 0.0293  0.0456  -0.2133 368 ASP A C   
2271  O O   . ASP A 359 ? 0.3744 0.7783 0.4202 0.0191  0.0441  -0.2235 368 ASP A O   
2272  C CB  . ASP A 359 ? 0.3580 0.7090 0.4093 0.0237  0.0451  -0.2089 368 ASP A CB  
2273  C CG  . ASP A 359 ? 0.3976 0.7286 0.4310 0.0447  0.0468  -0.2185 368 ASP A CG  
2274  O OD1 . ASP A 359 ? 0.4276 0.7733 0.4486 0.0590  0.0477  -0.2290 368 ASP A OD1 
2275  O OD2 . ASP A 359 ? 0.4101 0.7111 0.4408 0.0481  0.0471  -0.2155 368 ASP A OD2 
2276  N N   . THR A 360 ? 0.3696 0.8277 0.4226 0.0447  0.0472  -0.2129 369 THR A N   
2277  C CA  . THR A 360 ? 0.3969 0.8725 0.4372 0.0538  0.0478  -0.2265 369 THR A CA  
2278  C C   . THR A 360 ? 0.4540 0.8808 0.4694 0.0570  0.0469  -0.2466 369 THR A C   
2279  O O   . THR A 360 ? 0.4749 0.8980 0.4838 0.0467  0.0451  -0.2559 369 THR A O   
2280  C CB  . THR A 360 ? 0.3977 0.9074 0.4345 0.0760  0.0502  -0.2259 369 THR A CB  
2281  O OG1 . THR A 360 ? 0.3462 0.9018 0.4045 0.0698  0.0501  -0.2060 369 THR A OG1 
2282  C CG2 . THR A 360 ? 0.4289 0.9595 0.4519 0.0868  0.0509  -0.2400 369 THR A CG2 
2283  N N   . MET A 361 ? 0.4950 0.8831 0.4949 0.0704  0.0475  -0.2529 370 MET A N   
2284  C CA  . MET A 361 ? 0.5590 0.8949 0.5289 0.0754  0.0457  -0.2726 370 MET A CA  
2285  C C   . MET A 361 ? 0.5714 0.8998 0.5307 0.0607  0.0429  -0.2850 370 MET A C   
2286  O O   . MET A 361 ? 0.6000 0.9301 0.5393 0.0726  0.0423  -0.2998 370 MET A O   
2287  C CB  . MET A 361 ? 0.5867 0.8672 0.5489 0.0704  0.0445  -0.2722 370 MET A CB  
2288  C CG  . MET A 361 ? 0.6699 0.9195 0.6088 0.0969  0.0456  -0.2803 370 MET A CG  
2289  S SD  . MET A 361 ? 0.8245 1.0458 0.7211 0.1197  0.0440  -0.3058 370 MET A SD  
2290  C CE  . MET A 361 ? 0.7715 1.0678 0.6782 0.1348  0.0470  -0.3058 370 MET A CE  
2291  N N   . ASN A 362 ? 0.5510 0.8728 0.5225 0.0354  0.0408  -0.2792 371 ASN A N   
2292  C CA  . ASN A 362 ? 0.5648 0.8824 0.5250 0.0216  0.0379  -0.2911 371 ASN A CA  
2293  C C   . ASN A 362 ? 0.5260 0.8971 0.5057 0.0105  0.0381  -0.2843 371 ASN A C   
2294  O O   . ASN A 362 ? 0.5439 0.9166 0.5139 0.0002  0.0357  -0.2946 371 ASN A O   
2295  C CB  . ASN A 362 ? 0.5975 0.8608 0.5421 0.0035  0.0340  -0.2982 371 ASN A CB  
2296  C CG  . ASN A 362 ? 0.6598 0.8675 0.5667 0.0165  0.0316  -0.3166 371 ASN A CG  
2297  O OD1 . ASN A 362 ? 0.6905 0.8868 0.5734 0.0182  0.0289  -0.3328 371 ASN A OD1 
2298  N ND2 . ASN A 362 ? 0.6860 0.8576 0.5857 0.0262  0.0322  -0.3140 371 ASN A ND2 
2299  N N   . SER A 363 ? 0.4756 0.8900 0.4802 0.0133  0.0405  -0.2673 372 SER A N   
2300  C CA  . SER A 363 ? 0.4326 0.8975 0.4548 0.0047  0.0405  -0.2585 372 SER A CA  
2301  C C   . SER A 363 ? 0.4405 0.9237 0.4502 0.0057  0.0395  -0.2723 372 SER A C   
2302  O O   . SER A 363 ? 0.4751 0.9395 0.4611 0.0187  0.0393  -0.2891 372 SER A O   
2303  C CB  . SER A 363 ? 0.4040 0.9112 0.4435 0.0150  0.0428  -0.2430 372 SER A CB  
2304  O OG  . SER A 363 ? 0.4333 0.9449 0.4596 0.0374  0.0448  -0.2510 372 SER A OG  
2305  N N   . LEU A 364 ? 0.4061 0.9250 0.4302 -0.0075 0.0387  -0.2650 373 LEU A N   
2306  C CA  . LEU A 364 ? 0.4038 0.9506 0.4203 -0.0074 0.0379  -0.2749 373 LEU A CA  
2307  C C   . LEU A 364 ? 0.3655 0.9689 0.4009 -0.0030 0.0395  -0.2603 373 LEU A C   
2308  O O   . LEU A 364 ? 0.3357 0.9553 0.3907 -0.0125 0.0392  -0.2426 373 LEU A O   
2309  C CB  . LEU A 364 ? 0.4046 0.9460 0.4206 -0.0289 0.0349  -0.2786 373 LEU A CB  
2310  C CG  . LEU A 364 ? 0.4427 0.9450 0.4316 -0.0350 0.0319  -0.2994 373 LEU A CG  
2311  C CD1 . LEU A 364 ? 0.4874 0.9393 0.4540 -0.0212 0.0318  -0.3106 373 LEU A CD1 
2312  C CD2 . LEU A 364 ? 0.4322 0.9226 0.4256 -0.0598 0.0290  -0.2966 373 LEU A CD2 
2313  N N   . THR A 365 ? 0.3680 1.0004 0.3950 0.0113  0.0408  -0.2677 374 THR A N   
2314  C CA  . THR A 365 ? 0.3345 1.0232 0.3775 0.0153  0.0420  -0.2532 374 THR A CA  
2315  C C   . THR A 365 ? 0.3170 1.0396 0.3635 0.0051  0.0406  -0.2539 374 THR A C   
2316  O O   . THR A 365 ? 0.3425 1.0602 0.3725 0.0067  0.0399  -0.2713 374 THR A O   
2317  C CB  . THR A 365 ? 0.3460 1.0565 0.3804 0.0379  0.0446  -0.2579 374 THR A CB  
2318  O OG1 . THR A 365 ? 0.3933 1.0574 0.4099 0.0510  0.0455  -0.2703 374 THR A OG1 
2319  C CG2 . THR A 365 ? 0.3128 1.0649 0.3671 0.0396  0.0457  -0.2358 374 THR A CG2 
2320  N N   . LEU A 366 ? 0.2752 1.0302 0.3411 -0.0053 0.0397  -0.2350 375 LEU A N   
2321  C CA  . LEU A 366 ? 0.2515 1.0340 0.3223 -0.0173 0.0379  -0.2330 375 LEU A CA  
2322  C C   . LEU A 366 ? 0.2295 1.0603 0.3149 -0.0175 0.0377  -0.2137 375 LEU A C   
2323  O O   . LEU A 366 ? 0.2187 1.0531 0.3128 -0.0147 0.0379  -0.1990 375 LEU A O   
2324  C CB  . LEU A 366 ? 0.2344 0.9931 0.3124 -0.0344 0.0358  -0.2273 375 LEU A CB  
2325  C CG  . LEU A 366 ? 0.2245 0.9327 0.2925 -0.0405 0.0352  -0.2392 375 LEU A CG  
2326  C CD1 . LEU A 366 ? 0.1665 0.8664 0.2463 -0.0554 0.0335  -0.2276 375 LEU A CD1 
2327  C CD2 . LEU A 366 ? 0.2449 0.9458 0.2946 -0.0426 0.0341  -0.2598 375 LEU A CD2 
2328  N N   . PRO A 367 ? 0.2224 1.0897 0.3097 -0.0223 0.0366  -0.2126 376 PRO A N   
2329  C CA  . PRO A 367 ? 0.2073 1.1211 0.3061 -0.0251 0.0355  -0.1940 376 PRO A CA  
2330  C C   . PRO A 367 ? 0.1934 1.1022 0.3042 -0.0386 0.0324  -0.1742 376 PRO A C   
2331  O O   . PRO A 367 ? 0.1944 1.0789 0.3056 -0.0468 0.0313  -0.1770 376 PRO A O   
2332  C CB  . PRO A 367 ? 0.2119 1.1590 0.3052 -0.0253 0.0354  -0.2036 376 PRO A CB  
2333  C CG  . PRO A 367 ? 0.2289 1.1432 0.3131 -0.0314 0.0349  -0.2202 376 PRO A CG  
2334  C CD  . PRO A 367 ? 0.2391 1.1052 0.3147 -0.0257 0.0361  -0.2306 376 PRO A CD  
2335  N N   . SER A 368 ? 0.1882 1.1212 0.3069 -0.0407 0.0306  -0.1541 377 SER A N   
2336  C CA  . SER A 368 ? 0.1857 1.1139 0.3113 -0.0520 0.0265  -0.1340 377 SER A CA  
2337  C C   . SER A 368 ? 0.1871 1.1238 0.3126 -0.0588 0.0251  -0.1354 377 SER A C   
2338  O O   . SER A 368 ? 0.1786 1.1011 0.3066 -0.0655 0.0222  -0.1237 377 SER A O   
2339  C CB  . SER A 368 ? 0.1807 1.1424 0.3101 -0.0550 0.0237  -0.1132 377 SER A CB  
2340  O OG  . SER A 368 ? 0.2013 1.1844 0.3302 -0.0465 0.0260  -0.1150 377 SER A OG  
2341  N N   . GLU A 369 ? 0.2021 1.1636 0.3233 -0.0559 0.0269  -0.1497 378 GLU A N   
2342  C CA  . GLU A 369 ? 0.2123 1.1862 0.3329 -0.0622 0.0257  -0.1531 378 GLU A CA  
2343  C C   . GLU A 369 ? 0.2149 1.1521 0.3346 -0.0679 0.0256  -0.1606 378 GLU A C   
2344  O O   . GLU A 369 ? 0.2091 1.1548 0.3304 -0.0739 0.0240  -0.1575 378 GLU A O   
2345  C CB  . GLU A 369 ? 0.2267 1.2319 0.3408 -0.0581 0.0275  -0.1693 378 GLU A CB  
2346  C CG  . GLU A 369 ? 0.2498 1.3043 0.3661 -0.0551 0.0270  -0.1589 378 GLU A CG  
2347  C CD  . GLU A 369 ? 0.2917 1.3556 0.4100 -0.0481 0.0278  -0.1500 378 GLU A CD  
2348  O OE1 . GLU A 369 ? 0.2903 1.3232 0.4072 -0.0430 0.0294  -0.1546 378 GLU A OE1 
2349  O OE2 . GLU A 369 ? 0.3137 1.4204 0.4346 -0.0482 0.0267  -0.1378 378 GLU A OE2 
2350  N N   . VAL A 370 ? 0.2246 1.1236 0.3414 -0.0657 0.0273  -0.1695 379 VAL A N   
2351  C CA  . VAL A 370 ? 0.2266 1.0917 0.3436 -0.0719 0.0269  -0.1726 379 VAL A CA  
2352  C C   . VAL A 370 ? 0.2177 1.0827 0.3415 -0.0760 0.0242  -0.1539 379 VAL A C   
2353  O O   . VAL A 370 ? 0.2198 1.0832 0.3441 -0.0814 0.0235  -0.1549 379 VAL A O   
2354  C CB  . VAL A 370 ? 0.2308 1.0559 0.3456 -0.0683 0.0284  -0.1771 379 VAL A CB  
2355  C CG1 . VAL A 370 ? 0.2287 1.0256 0.3484 -0.0735 0.0271  -0.1676 379 VAL A CG1 
2356  C CG2 . VAL A 370 ? 0.2554 1.0625 0.3589 -0.0678 0.0300  -0.1992 379 VAL A CG2 
2357  N N   . ASN A 371 ? 0.2203 1.0874 0.3475 -0.0735 0.0223  -0.1364 380 ASN A N   
2358  C CA  . ASN A 371 ? 0.2271 1.0875 0.3560 -0.0756 0.0189  -0.1183 380 ASN A CA  
2359  C C   . ASN A 371 ? 0.2237 1.1098 0.3521 -0.0778 0.0171  -0.1140 380 ASN A C   
2360  O O   . ASN A 371 ? 0.2263 1.0996 0.3539 -0.0777 0.0152  -0.1058 380 ASN A O   
2361  C CB  . ASN A 371 ? 0.2318 1.0938 0.3603 -0.0748 0.0158  -0.0999 380 ASN A CB  
2362  C CG  . ASN A 371 ? 0.2675 1.1039 0.3969 -0.0727 0.0169  -0.1007 380 ASN A CG  
2363  O OD1 . ASN A 371 ? 0.3090 1.1108 0.4378 -0.0733 0.0157  -0.0948 380 ASN A OD1 
2364  N ND2 . ASN A 371 ? 0.2959 1.1502 0.4259 -0.0690 0.0195  -0.1086 380 ASN A ND2 
2365  N N   . LEU A 372 ? 0.2198 1.1433 0.3478 -0.0785 0.0176  -0.1192 381 LEU A N   
2366  C CA  . LEU A 372 ? 0.2195 1.1701 0.3470 -0.0800 0.0158  -0.1138 381 LEU A CA  
2367  C C   . LEU A 372 ? 0.2218 1.1643 0.3498 -0.0833 0.0169  -0.1237 381 LEU A C   
2368  O O   . LEU A 372 ? 0.2218 1.1781 0.3496 -0.0829 0.0153  -0.1165 381 LEU A O   
2369  C CB  . LEU A 372 ? 0.2222 1.2153 0.3492 -0.0807 0.0165  -0.1199 381 LEU A CB  
2370  C CG  . LEU A 372 ? 0.2340 1.2387 0.3607 -0.0779 0.0173  -0.1196 381 LEU A CG  
2371  C CD1 . LEU A 372 ? 0.2434 1.2903 0.3683 -0.0775 0.0188  -0.1305 381 LEU A CD1 
2372  C CD2 . LEU A 372 ? 0.2435 1.2474 0.3700 -0.0778 0.0135  -0.0963 381 LEU A CD2 
2373  N N   . CYS A 373 ? 0.2263 1.1467 0.3537 -0.0866 0.0195  -0.1397 382 CYS A N   
2374  C CA  . CYS A 373 ? 0.2287 1.1403 0.3558 -0.0926 0.0202  -0.1484 382 CYS A CA  
2375  C C   . CYS A 373 ? 0.2203 1.1146 0.3497 -0.0896 0.0187  -0.1346 382 CYS A C   
2376  O O   . CYS A 373 ? 0.2207 1.1238 0.3507 -0.0933 0.0187  -0.1364 382 CYS A O   
2377  C CB  . CYS A 373 ? 0.2399 1.1245 0.3628 -0.0973 0.0223  -0.1668 382 CYS A CB  
2378  S SG  . CYS A 373 ? 0.2741 1.1843 0.3891 -0.1025 0.0229  -0.1868 382 CYS A SG  
2379  N N   . ASN A 374 ? 0.2162 1.0884 0.3453 -0.0830 0.0172  -0.1204 383 ASN A N   
2380  C CA  . ASN A 374 ? 0.2150 1.0680 0.3427 -0.0779 0.0153  -0.1073 383 ASN A CA  
2381  C C   . ASN A 374 ? 0.2157 1.0963 0.3405 -0.0729 0.0128  -0.0959 383 ASN A C   
2382  O O   . ASN A 374 ? 0.2199 1.0946 0.3421 -0.0674 0.0117  -0.0888 383 ASN A O   
2383  C CB  . ASN A 374 ? 0.2151 1.0359 0.3398 -0.0729 0.0132  -0.0947 383 ASN A CB  
2384  C CG  . ASN A 374 ? 0.2253 1.0205 0.3527 -0.0758 0.0156  -0.1041 383 ASN A CG  
2385  O OD1 . ASN A 374 ? 0.2366 1.0178 0.3660 -0.0794 0.0183  -0.1165 383 ASN A OD1 
2386  N ND2 . ASN A 374 ? 0.2420 1.0327 0.3685 -0.0746 0.0145  -0.0976 383 ASN A ND2 
2387  N N   . VAL A 375 ? 0.2161 1.1276 0.3402 -0.0733 0.0118  -0.0937 384 VAL A N   
2388  C CA  . VAL A 375 ? 0.2193 1.1576 0.3393 -0.0675 0.0091  -0.0820 384 VAL A CA  
2389  C C   . VAL A 375 ? 0.2216 1.2010 0.3455 -0.0726 0.0110  -0.0930 384 VAL A C   
2390  O O   . VAL A 375 ? 0.2201 1.2192 0.3422 -0.0678 0.0100  -0.0872 384 VAL A O   
2391  C CB  . VAL A 375 ? 0.2218 1.1690 0.3366 -0.0651 0.0057  -0.0685 384 VAL A CB  
2392  C CG1 . VAL A 375 ? 0.2291 1.2107 0.3393 -0.0600 0.0033  -0.0592 384 VAL A CG1 
2393  C CG2 . VAL A 375 ? 0.2203 1.1282 0.3273 -0.0609 0.0020  -0.0535 384 VAL A CG2 
2394  N N   . ASP A 376 ? 0.2280 1.2209 0.3553 -0.0814 0.0133  -0.1088 385 ASP A N   
2395  C CA  . ASP A 376 ? 0.2368 1.2711 0.3653 -0.0874 0.0140  -0.1183 385 ASP A CA  
2396  C C   . ASP A 376 ? 0.2448 1.2821 0.3742 -0.0996 0.0160  -0.1381 385 ASP A C   
2397  O O   . ASP A 376 ? 0.2467 1.3120 0.3767 -0.1047 0.0156  -0.1405 385 ASP A O   
2398  C CB  . ASP A 376 ? 0.2370 1.3012 0.3644 -0.0866 0.0133  -0.1168 385 ASP A CB  
2399  C CG  . ASP A 376 ? 0.2606 1.3695 0.3876 -0.0859 0.0120  -0.1127 385 ASP A CG  
2400  O OD1 . ASP A 376 ? 0.2766 1.3983 0.4046 -0.0876 0.0120  -0.1142 385 ASP A OD1 
2401  O OD2 . ASP A 376 ? 0.2965 1.4317 0.4221 -0.0838 0.0108  -0.1073 385 ASP A OD2 
2402  N N   . ILE A 377 ? 0.2491 1.2582 0.3766 -0.1047 0.0177  -0.1517 386 ILE A N   
2403  C CA  . ILE A 377 ? 0.2604 1.2643 0.3842 -0.1178 0.0184  -0.1702 386 ILE A CA  
2404  C C   . ILE A 377 ? 0.2752 1.3099 0.3940 -0.1233 0.0180  -0.1826 386 ILE A C   
2405  O O   . ILE A 377 ? 0.2870 1.3068 0.3988 -0.1252 0.0188  -0.1971 386 ILE A O   
2406  C CB  . ILE A 377 ? 0.2509 1.2686 0.3770 -0.1245 0.0176  -0.1673 386 ILE A CB  
2407  C CG1 . ILE A 377 ? 0.2357 1.2196 0.3645 -0.1209 0.0182  -0.1598 386 ILE A CG1 
2408  C CG2 . ILE A 377 ? 0.2621 1.2855 0.3823 -0.1415 0.0169  -0.1847 386 ILE A CG2 
2409  C CD1 . ILE A 377 ? 0.2161 1.2224 0.3483 -0.1184 0.0175  -0.1488 386 ILE A CD1 
2410  N N   . PHE A 378 ? 0.2726 1.3506 0.3936 -0.1246 0.0167  -0.1770 387 PHE A N   
2411  C CA  . PHE A 378 ? 0.2803 1.3942 0.3976 -0.1279 0.0161  -0.1849 387 PHE A CA  
2412  C C   . PHE A 378 ? 0.2731 1.3984 0.3934 -0.1153 0.0163  -0.1722 387 PHE A C   
2413  O O   . PHE A 378 ? 0.2631 1.3921 0.3880 -0.1067 0.0154  -0.1536 387 PHE A O   
2414  C CB  . PHE A 378 ? 0.2752 1.4320 0.3942 -0.1342 0.0145  -0.1819 387 PHE A CB  
2415  C CG  . PHE A 378 ? 0.2822 1.4309 0.4001 -0.1467 0.0138  -0.1880 387 PHE A CG  
2416  C CD1 . PHE A 378 ? 0.2776 1.4365 0.4020 -0.1428 0.0137  -0.1738 387 PHE A CD1 
2417  C CD2 . PHE A 378 ? 0.2951 1.4238 0.4033 -0.1621 0.0130  -0.2075 387 PHE A CD2 
2418  C CE1 . PHE A 378 ? 0.2702 1.4270 0.3941 -0.1554 0.0131  -0.1783 387 PHE A CE1 
2419  C CE2 . PHE A 378 ? 0.3047 1.4260 0.4106 -0.1767 0.0117  -0.2120 387 PHE A CE2 
2420  C CZ  . PHE A 378 ? 0.2831 1.4214 0.3983 -0.1739 0.0119  -0.1969 387 PHE A CZ  
2421  N N   . ASN A 379 ? 0.2825 1.4110 0.3981 -0.1142 0.0171  -0.1825 388 ASN A N   
2422  C CA  . ASN A 379 ? 0.2824 1.4250 0.4000 -0.1045 0.0173  -0.1719 388 ASN A CA  
2423  C C   . ASN A 379 ? 0.3050 1.4425 0.4152 -0.1041 0.0189  -0.1896 388 ASN A C   
2424  O O   . ASN A 379 ? 0.3141 1.4149 0.4190 -0.1060 0.0200  -0.2025 388 ASN A O   
2425  C CB  . ASN A 379 ? 0.2661 1.3798 0.3882 -0.0966 0.0172  -0.1550 388 ASN A CB  
2426  C CG  . ASN A 379 ? 0.2706 1.3377 0.3913 -0.0970 0.0189  -0.1639 388 ASN A CG  
2427  O OD1 . ASN A 379 ? 0.2455 1.3015 0.3630 -0.0935 0.0204  -0.1718 388 ASN A OD1 
2428  N ND2 . ASN A 379 ? 0.2810 1.3224 0.4036 -0.1001 0.0186  -0.1620 388 ASN A ND2 
2429  N N   . PRO A 380 ? 0.3172 1.4915 0.4256 -0.1005 0.0190  -0.1902 389 PRO A N   
2430  C CA  . PRO A 380 ? 0.3356 1.5127 0.4360 -0.0953 0.0206  -0.2044 389 PRO A CA  
2431  C C   . PRO A 380 ? 0.3377 1.4811 0.4406 -0.0879 0.0221  -0.1989 389 PRO A C   
2432  O O   . PRO A 380 ? 0.3336 1.4596 0.4443 -0.0879 0.0213  -0.1824 389 PRO A O   
2433  C CB  . PRO A 380 ? 0.3310 1.5567 0.4349 -0.0905 0.0202  -0.1930 389 PRO A CB  
2434  C CG  . PRO A 380 ? 0.3086 1.5407 0.4224 -0.0911 0.0180  -0.1676 389 PRO A CG  
2435  C CD  . PRO A 380 ? 0.3055 1.5202 0.4195 -0.0983 0.0173  -0.1726 389 PRO A CD  
2436  N N   . LYS A 381 ? 0.3498 1.4836 0.4451 -0.0806 0.0241  -0.2115 390 LYS A N   
2437  C CA  . LYS A 381 ? 0.3478 1.4542 0.4465 -0.0732 0.0255  -0.2041 390 LYS A CA  
2438  C C   . LYS A 381 ? 0.3571 1.4107 0.4510 -0.0751 0.0262  -0.2149 390 LYS A C   
2439  O O   . LYS A 381 ? 0.3757 1.4077 0.4631 -0.0667 0.0280  -0.2237 390 LYS A O   
2440  C CB  . LYS A 381 ? 0.3253 1.4382 0.4360 -0.0736 0.0239  -0.1774 390 LYS A CB  
2441  C CG  . LYS A 381 ? 0.3263 1.4841 0.4407 -0.0704 0.0229  -0.1622 390 LYS A CG  
2442  C CD  . LYS A 381 ? 0.3663 1.5299 0.4794 -0.0617 0.0248  -0.1623 390 LYS A CD  
2443  C CE  . LYS A 381 ? 0.3647 1.5572 0.4838 -0.0627 0.0226  -0.1379 390 LYS A CE  
2444  N NZ  . LYS A 381 ? 0.3795 1.6262 0.4978 -0.0625 0.0221  -0.1346 390 LYS A NZ  
2445  N N   . TYR A 382 ? 0.3476 1.3821 0.4439 -0.0851 0.0248  -0.2138 391 TYR A N   
2446  C CA  . TYR A 382 ? 0.3555 1.3432 0.4453 -0.0886 0.0252  -0.2258 391 TYR A CA  
2447  C C   . TYR A 382 ? 0.3674 1.3465 0.4527 -0.1023 0.0233  -0.2346 391 TYR A C   
2448  O O   . TYR A 382 ? 0.3574 1.3464 0.4522 -0.1085 0.0222  -0.2221 391 TYR A O   
2449  C CB  . TYR A 382 ? 0.3426 1.3009 0.4412 -0.0856 0.0257  -0.2115 391 TYR A CB  
2450  C CG  . TYR A 382 ? 0.3534 1.2667 0.4439 -0.0820 0.0271  -0.2236 391 TYR A CG  
2451  C CD1 . TYR A 382 ? 0.3682 1.2789 0.4502 -0.0706 0.0289  -0.2331 391 TYR A CD1 
2452  C CD2 . TYR A 382 ? 0.3543 1.2293 0.4448 -0.0888 0.0267  -0.2245 391 TYR A CD2 
2453  C CE1 . TYR A 382 ? 0.3801 1.2495 0.4531 -0.0652 0.0301  -0.2434 391 TYR A CE1 
2454  C CE2 . TYR A 382 ? 0.3591 1.1922 0.4412 -0.0853 0.0278  -0.2346 391 TYR A CE2 
2455  C CZ  . TYR A 382 ? 0.3725 1.2023 0.4455 -0.0731 0.0294  -0.2439 391 TYR A CZ  
2456  O OH  . TYR A 382 ? 0.3909 1.1792 0.4535 -0.0674 0.0303  -0.2539 391 TYR A OH  
2457  N N   . ASP A 383 ? 0.3939 1.3536 0.4630 -0.1071 0.0225  -0.2559 392 ASP A N   
2458  C CA  . ASP A 383 ? 0.4078 1.3470 0.4708 -0.1231 0.0202  -0.2640 392 ASP A CA  
2459  C C   . ASP A 383 ? 0.3999 1.2941 0.4658 -0.1233 0.0210  -0.2595 392 ASP A C   
2460  O O   . ASP A 383 ? 0.4087 1.2752 0.4721 -0.1124 0.0228  -0.2608 392 ASP A O   
2461  C CB  . ASP A 383 ? 0.4444 1.3743 0.4856 -0.1324 0.0175  -0.2873 392 ASP A CB  
2462  C CG  . ASP A 383 ? 0.4709 1.4069 0.4991 -0.1190 0.0185  -0.2999 392 ASP A CG  
2463  O OD1 . ASP A 383 ? 0.4912 1.4053 0.5172 -0.1041 0.0209  -0.3006 392 ASP A OD1 
2464  O OD2 . ASP A 383 ? 0.4800 1.4446 0.4996 -0.1230 0.0168  -0.3093 392 ASP A OD2 
2465  N N   . CYS A 384 ? 0.3826 1.2730 0.4535 -0.1356 0.0196  -0.2542 393 CYS A N   
2466  C CA  . CYS A 384 ? 0.3580 1.2335 0.4414 -0.1323 0.0208  -0.2388 393 CYS A CA  
2467  C C   . CYS A 384 ? 0.3638 1.2130 0.4416 -0.1475 0.0191  -0.2449 393 CYS A C   
2468  O O   . CYS A 384 ? 0.3641 1.2366 0.4422 -0.1602 0.0172  -0.2451 393 CYS A O   
2469  C CB  . CYS A 384 ? 0.3303 1.2494 0.4273 -0.1290 0.0207  -0.2214 393 CYS A CB  
2470  S SG  . CYS A 384 ? 0.3512 1.2615 0.4618 -0.1195 0.0216  -0.1989 393 CYS A SG  
2471  N N   . LYS A 385 ? 0.3726 1.1753 0.4440 -0.1470 0.0196  -0.2502 394 LYS A N   
2472  C CA  . LYS A 385 ? 0.3874 1.1624 0.4496 -0.1639 0.0173  -0.2577 394 LYS A CA  
2473  C C   . LYS A 385 ? 0.3596 1.1522 0.4355 -0.1717 0.0171  -0.2429 394 LYS A C   
2474  O O   . LYS A 385 ? 0.3358 1.1329 0.4259 -0.1603 0.0193  -0.2270 394 LYS A O   
2475  C CB  . LYS A 385 ? 0.4117 1.1307 0.4619 -0.1606 0.0176  -0.2666 394 LYS A CB  
2476  C CG  . LYS A 385 ? 0.4543 1.1568 0.4899 -0.1476 0.0183  -0.2803 394 LYS A CG  
2477  C CD  . LYS A 385 ? 0.5468 1.1924 0.5691 -0.1411 0.0187  -0.2882 394 LYS A CD  
2478  C CE  . LYS A 385 ? 0.5514 1.1846 0.5891 -0.1243 0.0226  -0.2737 394 LYS A CE  
2479  N NZ  . LYS A 385 ? 0.5479 1.1538 0.5929 -0.1312 0.0228  -0.2642 394 LYS A NZ  
2480  N N   . ILE A 386 ? 0.3637 1.1658 0.4331 -0.1911 0.0141  -0.2486 395 ILE A N   
2481  C CA  . ILE A 386 ? 0.3440 1.1842 0.4252 -0.1985 0.0137  -0.2360 395 ILE A CA  
2482  C C   . ILE A 386 ? 0.3720 1.2010 0.4420 -0.2221 0.0102  -0.2442 395 ILE A C   
2483  O O   . ILE A 386 ? 0.4086 1.2112 0.4600 -0.2333 0.0072  -0.2606 395 ILE A O   
2484  C CB  . ILE A 386 ? 0.3361 1.2276 0.4192 -0.2003 0.0126  -0.2361 395 ILE A CB  
2485  C CG1 . ILE A 386 ? 0.3181 1.2361 0.4158 -0.1803 0.0152  -0.2205 395 ILE A CG1 
2486  C CG2 . ILE A 386 ? 0.3305 1.2612 0.4151 -0.2178 0.0100  -0.2334 395 ILE A CG2 
2487  C CD1 . ILE A 386 ? 0.3398 1.3076 0.4386 -0.1817 0.0141  -0.2205 395 ILE A CD1 
2488  N N   . MET A 387 ? 0.3635 1.2127 0.4420 -0.2306 0.0099  -0.2334 396 MET A N   
2489  C CA  . MET A 387 ? 0.3879 1.2448 0.4554 -0.2580 0.0054  -0.2404 396 MET A CA  
2490  C C   . MET A 387 ? 0.3728 1.2924 0.4509 -0.2649 0.0048  -0.2298 396 MET A C   
2491  O O   . MET A 387 ? 0.3461 1.2952 0.4405 -0.2473 0.0080  -0.2145 396 MET A O   
2492  C CB  . MET A 387 ? 0.4068 1.2216 0.4677 -0.2694 0.0043  -0.2413 396 MET A CB  
2493  C CG  . MET A 387 ? 0.4040 1.2357 0.4810 -0.2642 0.0069  -0.2243 396 MET A CG  
2494  S SD  . MET A 387 ? 0.4966 1.2826 0.5611 -0.2859 0.0040  -0.2280 396 MET A SD  
2495  C CE  . MET A 387 ? 0.5099 1.2213 0.5571 -0.2769 0.0039  -0.2439 396 MET A CE  
2496  N N   . THR A 388 ? 0.3934 1.3313 0.4599 -0.2908 0.0000  -0.2381 397 THR A N   
2497  C CA  . THR A 388 ? 0.3814 1.3856 0.4546 -0.2993 -0.0014 -0.2318 397 THR A CA  
2498  C C   . THR A 388 ? 0.3865 1.4176 0.4618 -0.3192 -0.0036 -0.2240 397 THR A C   
2499  O O   . THR A 388 ? 0.4161 1.4137 0.4776 -0.3416 -0.0073 -0.2312 397 THR A O   
2500  C CB  . THR A 388 ? 0.4065 1.4168 0.4630 -0.3164 -0.0060 -0.2477 397 THR A CB  
2501  O OG1 . THR A 388 ? 0.3947 1.4106 0.4554 -0.2948 -0.0032 -0.2496 397 THR A OG1 
2502  C CG2 . THR A 388 ? 0.4160 1.4897 0.4732 -0.3373 -0.0097 -0.2444 397 THR A CG2 
2503  N N   . SER A 389 ? 0.3616 1.4539 0.4525 -0.3110 -0.0016 -0.2089 398 SER A N   
2504  C CA  . SER A 389 ? 0.3668 1.5049 0.4596 -0.3323 -0.0043 -0.2014 398 SER A CA  
2505  C C   . SER A 389 ? 0.3580 1.5736 0.4579 -0.3344 -0.0051 -0.1943 398 SER A C   
2506  O O   . SER A 389 ? 0.3364 1.5814 0.4478 -0.3085 -0.0015 -0.1855 398 SER A O   
2507  C CB  . SER A 389 ? 0.3486 1.4884 0.4532 -0.3209 -0.0009 -0.1866 398 SER A CB  
2508  O OG  . SER A 389 ? 0.3503 1.5468 0.4578 -0.3395 -0.0031 -0.1781 398 SER A OG  
2509  N N   . LYS A 390 ? 0.3774 1.6265 0.4694 -0.3659 -0.0103 -0.1970 399 LYS A N   
2510  C CA  . LYS A 390 ? 0.3715 1.7009 0.4702 -0.3709 -0.0115 -0.1894 399 LYS A CA  
2511  C C   . LYS A 390 ? 0.3407 1.7237 0.4569 -0.3528 -0.0073 -0.1688 399 LYS A C   
2512  O O   . LYS A 390 ? 0.3183 1.7599 0.4451 -0.3344 -0.0050 -0.1581 399 LYS A O   
2513  C CB  . LYS A 390 ? 0.4118 1.7587 0.4941 -0.4140 -0.0193 -0.1989 399 LYS A CB  
2514  C CG  . LYS A 390 ? 0.4408 1.7729 0.5060 -0.4288 -0.0240 -0.2168 399 LYS A CG  
2515  C CD  . LYS A 390 ? 0.4636 1.8749 0.5366 -0.4277 -0.0245 -0.2110 399 LYS A CD  
2516  C CE  . LYS A 390 ? 0.5130 1.9216 0.5668 -0.4508 -0.0307 -0.2283 399 LYS A CE  
2517  N NZ  . LYS A 390 ? 0.4927 1.9850 0.5549 -0.4509 -0.0313 -0.2216 399 LYS A NZ  
2518  N N   . THR A 391 ? 0.3385 1.6994 0.4563 -0.3560 -0.0064 -0.1635 400 THR A N   
2519  C CA  . THR A 391 ? 0.3208 1.7320 0.4516 -0.3425 -0.0033 -0.1456 400 THR A CA  
2520  C C   . THR A 391 ? 0.2934 1.6693 0.4331 -0.3048 0.0027  -0.1371 400 THR A C   
2521  O O   . THR A 391 ? 0.2927 1.5982 0.4280 -0.2995 0.0037  -0.1449 400 THR A O   
2522  C CB  . THR A 391 ? 0.3423 1.7579 0.4682 -0.3734 -0.0067 -0.1437 400 THR A CB  
2523  O OG1 . THR A 391 ? 0.3838 1.7697 0.4918 -0.4120 -0.0135 -0.1592 400 THR A OG1 
2524  C CG2 . THR A 391 ? 0.3380 1.8446 0.4736 -0.3764 -0.0065 -0.1276 400 THR A CG2 
2525  N N   . ASP A 392 ? 0.2694 1.6948 0.4195 -0.2789 0.0062  -0.1212 401 ASP A N   
2526  C CA  . ASP A 392 ? 0.2481 1.6456 0.4036 -0.2439 0.0109  -0.1115 401 ASP A CA  
2527  C C   . ASP A 392 ? 0.2499 1.5967 0.4035 -0.2522 0.0115  -0.1132 401 ASP A C   
2528  O O   . ASP A 392 ? 0.2630 1.6327 0.4160 -0.2752 0.0096  -0.1111 401 ASP A O   
2529  C CB  . ASP A 392 ? 0.2380 1.7033 0.4004 -0.2197 0.0134  -0.0944 401 ASP A CB  
2530  C CG  . ASP A 392 ? 0.2475 1.7451 0.4111 -0.1961 0.0143  -0.0895 401 ASP A CG  
2531  O OD1 . ASP A 392 ? 0.2929 1.7904 0.4539 -0.2096 0.0120  -0.0991 401 ASP A OD1 
2532  O OD2 . ASP A 392 ? 0.2488 1.7709 0.4141 -0.1632 0.0169  -0.0761 401 ASP A OD2 
2533  N N   . VAL A 393 ? 0.2381 1.5181 0.3904 -0.2341 0.0138  -0.1161 402 VAL A N   
2534  C CA  . VAL A 393 ? 0.2293 1.4585 0.3804 -0.2357 0.0149  -0.1164 402 VAL A CA  
2535  C C   . VAL A 393 ? 0.2046 1.4156 0.3597 -0.1975 0.0188  -0.1061 402 VAL A C   
2536  O O   . VAL A 393 ? 0.1983 1.3984 0.3528 -0.1778 0.0196  -0.1057 402 VAL A O   
2537  C CB  . VAL A 393 ? 0.2418 1.4006 0.3846 -0.2517 0.0131  -0.1319 402 VAL A CB  
2538  C CG1 . VAL A 393 ? 0.2552 1.3621 0.3969 -0.2500 0.0145  -0.1311 402 VAL A CG1 
2539  C CG2 . VAL A 393 ? 0.2695 1.4371 0.4030 -0.2888 0.0081  -0.1434 402 VAL A CG2 
2540  N N   . SER A 394 ? 0.1907 1.3985 0.3479 -0.1874 0.0208  -0.0974 403 SER A N   
2541  C CA  . SER A 394 ? 0.1715 1.3565 0.3285 -0.1520 0.0237  -0.0881 403 SER A CA  
2542  C C   . SER A 394 ? 0.1660 1.2913 0.3216 -0.1549 0.0245  -0.0911 403 SER A C   
2543  O O   . SER A 394 ? 0.1740 1.3001 0.3302 -0.1774 0.0238  -0.0935 403 SER A O   
2544  C CB  . SER A 394 ? 0.1668 1.4097 0.3256 -0.1314 0.0253  -0.0737 403 SER A CB  
2545  O OG  . SER A 394 ? 0.1861 1.5019 0.3484 -0.1462 0.0240  -0.0715 403 SER A OG  
2546  N N   . SER A 395 ? 0.1556 1.2287 0.3084 -0.1336 0.0257  -0.0905 404 SER A N   
2547  C CA  . SER A 395 ? 0.1550 1.1766 0.3064 -0.1301 0.0269  -0.0902 404 SER A CA  
2548  C C   . SER A 395 ? 0.1426 1.1142 0.2896 -0.1039 0.0275  -0.0871 404 SER A C   
2549  O O   . SER A 395 ? 0.1397 1.1192 0.2835 -0.0851 0.0270  -0.0824 404 SER A O   
2550  C CB  . SER A 395 ? 0.1646 1.1505 0.3153 -0.1600 0.0257  -0.1020 404 SER A CB  
2551  O OG  . SER A 395 ? 0.1750 1.0994 0.3227 -0.1546 0.0258  -0.1088 404 SER A OG  
2552  N N   . SER A 396 ? 0.1356 1.0569 0.2813 -0.1036 0.0283  -0.0887 405 SER A N   
2553  C CA  . SER A 396 ? 0.1318 1.0051 0.2724 -0.0823 0.0282  -0.0853 405 SER A CA  
2554  C C   . SER A 396 ? 0.1347 0.9486 0.2753 -0.0926 0.0282  -0.0936 405 SER A C   
2555  O O   . SER A 396 ? 0.1401 0.9411 0.2831 -0.1131 0.0286  -0.1009 405 SER A O   
2556  C CB  . SER A 396 ? 0.1312 1.0057 0.2665 -0.0582 0.0289  -0.0739 405 SER A CB  
2557  O OG  . SER A 396 ? 0.1192 0.9384 0.2483 -0.0449 0.0281  -0.0721 405 SER A OG  
2558  N N   . VAL A 397 ? 0.1292 0.9083 0.2657 -0.0783 0.0273  -0.0918 406 VAL A N   
2559  C CA  . VAL A 397 ? 0.1359 0.8672 0.2724 -0.0859 0.0272  -0.0993 406 VAL A CA  
2560  C C   . VAL A 397 ? 0.1353 0.8284 0.2662 -0.0672 0.0263  -0.0917 406 VAL A C   
2561  O O   . VAL A 397 ? 0.1394 0.8347 0.2647 -0.0522 0.0244  -0.0847 406 VAL A O   
2562  C CB  . VAL A 397 ? 0.1338 0.8685 0.2707 -0.0915 0.0262  -0.1061 406 VAL A CB  
2563  C CG1 . VAL A 397 ? 0.1521 0.8454 0.2890 -0.1010 0.0266  -0.1155 406 VAL A CG1 
2564  C CG2 . VAL A 397 ? 0.1489 0.9267 0.2886 -0.1064 0.0261  -0.1120 406 VAL A CG2 
2565  N N   . ILE A 398 ? 0.1374 0.7935 0.2682 -0.0691 0.0271  -0.0927 407 ILE A N   
2566  C CA  . ILE A 398 ? 0.1394 0.7600 0.2632 -0.0525 0.0255  -0.0849 407 ILE A CA  
2567  C C   . ILE A 398 ? 0.1464 0.7335 0.2691 -0.0540 0.0242  -0.0874 407 ILE A C   
2568  O O   . ILE A 398 ? 0.1514 0.7214 0.2789 -0.0668 0.0256  -0.0962 407 ILE A O   
2569  C CB  . ILE A 398 ? 0.1361 0.7360 0.2592 -0.0509 0.0267  -0.0829 407 ILE A CB  
2570  C CG1 . ILE A 398 ? 0.1305 0.7653 0.2519 -0.0424 0.0274  -0.0766 407 ILE A CG1 
2571  C CG2 . ILE A 398 ? 0.1326 0.6926 0.2474 -0.0371 0.0245  -0.0764 407 ILE A CG2 
2572  C CD1 . ILE A 398 ? 0.1578 0.7759 0.2782 -0.0400 0.0286  -0.0741 407 ILE A CD1 
2573  N N   . THR A 399 ? 0.1548 0.7316 0.2693 -0.0403 0.0212  -0.0787 408 THR A N   
2574  C CA  . THR A 399 ? 0.1626 0.7153 0.2757 -0.0424 0.0194  -0.0789 408 THR A CA  
2575  C C   . THR A 399 ? 0.1710 0.6818 0.2773 -0.0361 0.0173  -0.0727 408 THR A C   
2576  O O   . THR A 399 ? 0.1826 0.6787 0.2842 -0.0289 0.0171  -0.0688 408 THR A O   
2577  C CB  . THR A 399 ? 0.1639 0.7328 0.2712 -0.0357 0.0164  -0.0728 408 THR A CB  
2578  O OG1 . THR A 399 ? 0.1800 0.7452 0.2745 -0.0190 0.0133  -0.0615 408 THR A OG1 
2579  C CG2 . THR A 399 ? 0.1598 0.7702 0.2741 -0.0431 0.0183  -0.0794 408 THR A CG2 
2580  N N   . SER A 400 ? 0.1733 0.6675 0.2784 -0.0390 0.0154  -0.0715 409 SER A N   
2581  C CA  . SER A 400 ? 0.1825 0.6397 0.2820 -0.0367 0.0131  -0.0663 409 SER A CA  
2582  C C   . SER A 400 ? 0.1926 0.6331 0.2764 -0.0233 0.0085  -0.0546 409 SER A C   
2583  O O   . SER A 400 ? 0.2018 0.6130 0.2790 -0.0190 0.0070  -0.0509 409 SER A O   
2584  C CB  . SER A 400 ? 0.1852 0.6373 0.2856 -0.0425 0.0114  -0.0653 409 SER A CB  
2585  O OG  . SER A 400 ? 0.1942 0.6634 0.3062 -0.0521 0.0154  -0.0770 409 SER A OG  
2586  N N   . LEU A 401 ? 0.1962 0.6548 0.2723 -0.0157 0.0060  -0.0493 410 LEU A N   
2587  C CA  . LEU A 401 ? 0.2162 0.6518 0.2718 -0.0027 -0.0001 -0.0373 410 LEU A CA  
2588  C C   . LEU A 401 ? 0.2215 0.6767 0.2677 0.0127  -0.0007 -0.0335 410 LEU A C   
2589  O O   . LEU A 401 ? 0.2405 0.6759 0.2656 0.0269  -0.0062 -0.0239 410 LEU A O   
2590  C CB  . LEU A 401 ? 0.2237 0.6525 0.2729 -0.0084 -0.0049 -0.0308 410 LEU A CB  
2591  C CG  . LEU A 401 ? 0.2371 0.6236 0.2703 -0.0087 -0.0112 -0.0214 410 LEU A CG  
2592  C CD1 . LEU A 401 ? 0.2488 0.6183 0.2920 -0.0164 -0.0084 -0.0268 410 LEU A CD1 
2593  C CD2 . LEU A 401 ? 0.2316 0.6218 0.2614 -0.0174 -0.0153 -0.0152 410 LEU A CD2 
2594  N N   . GLY A 402 ? 0.2065 0.7009 0.2672 0.0095  0.0046  -0.0412 411 GLY A N   
2595  C CA  . GLY A 402 ? 0.2015 0.7248 0.2577 0.0233  0.0057  -0.0390 411 GLY A CA  
2596  C C   . GLY A 402 ? 0.1780 0.7444 0.2534 0.0113  0.0116  -0.0488 411 GLY A C   
2597  O O   . GLY A 402 ? 0.1676 0.7289 0.2553 -0.0027 0.0150  -0.0568 411 GLY A O   
2598  N N   . ALA A 403 ? 0.1683 0.7765 0.2447 0.0159  0.0124  -0.0479 412 ALA A N   
2599  C CA  . ALA A 403 ? 0.1468 0.7970 0.2387 0.0028  0.0168  -0.0561 412 ALA A CA  
2600  C C   . ALA A 403 ? 0.1455 0.8373 0.2380 0.0048  0.0164  -0.0549 412 ALA A C   
2601  O O   . ALA A 403 ? 0.1549 0.8479 0.2340 0.0221  0.0131  -0.0458 412 ALA A O   
2602  C CB  . ALA A 403 ? 0.1450 0.8101 0.2370 0.0089  0.0190  -0.0547 412 ALA A CB  
2603  N N   . ILE A 404 ? 0.1380 0.8617 0.2441 -0.0136 0.0192  -0.0642 413 ILE A N   
2604  C CA  . ILE A 404 ? 0.1369 0.9089 0.2461 -0.0153 0.0194  -0.0648 413 ILE A CA  
2605  C C   . ILE A 404 ? 0.1405 0.9581 0.2556 -0.0189 0.0219  -0.0658 413 ILE A C   
2606  O O   . ILE A 404 ? 0.1377 0.9507 0.2589 -0.0303 0.0240  -0.0704 413 ILE A O   
2607  C CB  . ILE A 404 ? 0.1299 0.9081 0.2487 -0.0357 0.0203  -0.0755 413 ILE A CB  
2608  C CG1 . ILE A 404 ? 0.1257 0.8660 0.2403 -0.0341 0.0182  -0.0745 413 ILE A CG1 
2609  C CG2 . ILE A 404 ? 0.1273 0.9583 0.2490 -0.0387 0.0203  -0.0765 413 ILE A CG2 
2610  C CD1 . ILE A 404 ? 0.1318 0.8832 0.2529 -0.0484 0.0187  -0.0836 413 ILE A CD1 
2611  N N   . VAL A 405 ? 0.1476 1.0114 0.2606 -0.0101 0.0215  -0.0609 414 VAL A N   
2612  C CA  . VAL A 405 ? 0.1539 1.0718 0.2727 -0.0139 0.0235  -0.0604 414 VAL A CA  
2613  C C   . VAL A 405 ? 0.1553 1.1275 0.2781 -0.0195 0.0233  -0.0613 414 VAL A C   
2614  O O   . VAL A 405 ? 0.1625 1.1449 0.2778 -0.0027 0.0214  -0.0546 414 VAL A O   
2615  C CB  . VAL A 405 ? 0.1585 1.0845 0.2681 0.0102  0.0238  -0.0500 414 VAL A CB  
2616  C CG1 . VAL A 405 ? 0.1754 1.0760 0.2677 0.0384  0.0206  -0.0404 414 VAL A CG1 
2617  C CG2 . VAL A 405 ? 0.1614 1.1549 0.2754 0.0108  0.0254  -0.0469 414 VAL A CG2 
2618  N N   . SER A 406 ? 0.1526 1.1565 0.2858 -0.0445 0.0246  -0.0697 415 SER A N   
2619  C CA  . SER A 406 ? 0.1549 1.2090 0.2923 -0.0548 0.0241  -0.0724 415 SER A CA  
2620  C C   . SER A 406 ? 0.1630 1.2757 0.3038 -0.0564 0.0252  -0.0674 415 SER A C   
2621  O O   . SER A 406 ? 0.1679 1.2889 0.3145 -0.0785 0.0259  -0.0725 415 SER A O   
2622  C CB  . SER A 406 ? 0.1551 1.1972 0.2986 -0.0849 0.0238  -0.0868 415 SER A CB  
2623  O OG  . SER A 406 ? 0.1586 1.1503 0.2997 -0.0840 0.0231  -0.0921 415 SER A OG  
2624  N N   . CYS A 407 ? 0.1712 1.3251 0.3069 -0.0327 0.0251  -0.0565 416 CYS A N   
2625  C CA  . CYS A 407 ? 0.1736 1.3918 0.3114 -0.0281 0.0264  -0.0491 416 CYS A CA  
2626  C C   . CYS A 407 ? 0.1729 1.4547 0.3148 -0.0360 0.0256  -0.0489 416 CYS A C   
2627  O O   . CYS A 407 ? 0.1785 1.4741 0.3143 -0.0159 0.0247  -0.0431 416 CYS A O   
2628  C CB  . CYS A 407 ? 0.1808 1.3992 0.3065 0.0099  0.0267  -0.0365 416 CYS A CB  
2629  S SG  . CYS A 407 ? 0.2020 1.4723 0.3299 0.0158  0.0291  -0.0292 416 CYS A SG  
2630  N N   . TYR A 408 ? 0.1724 1.4926 0.3233 -0.0667 0.0255  -0.0549 417 TYR A N   
2631  C CA  . TYR A 408 ? 0.1694 1.5469 0.3244 -0.0813 0.0241  -0.0570 417 TYR A CA  
2632  C C   . TYR A 408 ? 0.1699 1.6236 0.3307 -0.0972 0.0242  -0.0526 417 TYR A C   
2633  O O   . TYR A 408 ? 0.1698 1.6270 0.3329 -0.1054 0.0251  -0.0504 417 TYR A O   
2634  C CB  . TYR A 408 ? 0.1685 1.5105 0.3253 -0.1096 0.0222  -0.0719 417 TYR A CB  
2635  C CG  . TYR A 408 ? 0.1633 1.4575 0.3154 -0.0940 0.0218  -0.0743 417 TYR A CG  
2636  C CD1 . TYR A 408 ? 0.1670 1.3994 0.3183 -0.1065 0.0213  -0.0852 417 TYR A CD1 
2637  C CD2 . TYR A 408 ? 0.1711 1.4844 0.3183 -0.0671 0.0215  -0.0649 417 TYR A CD2 
2638  C CE1 . TYR A 408 ? 0.1748 1.3700 0.3223 -0.0939 0.0208  -0.0862 417 TYR A CE1 
2639  C CE2 . TYR A 408 ? 0.1734 1.4459 0.3156 -0.0561 0.0205  -0.0659 417 TYR A CE2 
2640  C CZ  . TYR A 408 ? 0.1766 1.3925 0.3197 -0.0701 0.0202  -0.0763 417 TYR A CZ  
2641  O OH  . TYR A 408 ? 0.1900 1.3698 0.3284 -0.0602 0.0191  -0.0761 417 TYR A OH  
2642  N N   . GLY A 409 ? 0.1725 1.6897 0.3357 -0.1025 0.0230  -0.0507 418 GLY A N   
2643  C CA  . GLY A 409 ? 0.1764 1.7759 0.3450 -0.1183 0.0225  -0.0451 418 GLY A CA  
2644  C C   . GLY A 409 ? 0.1768 1.8139 0.3444 -0.0908 0.0253  -0.0308 418 GLY A C   
2645  O O   . GLY A 409 ? 0.1781 1.8120 0.3387 -0.0513 0.0270  -0.0221 418 GLY A O   
2646  N N   . LYS A 410 ? 0.1798 1.8499 0.3524 -0.1118 0.0253  -0.0286 419 LYS A N   
2647  C CA  . LYS A 410 ? 0.1833 1.8960 0.3553 -0.0875 0.0280  -0.0154 419 LYS A CA  
2648  C C   . LYS A 410 ? 0.1818 1.8297 0.3483 -0.0654 0.0303  -0.0141 419 LYS A C   
2649  O O   . LYS A 410 ? 0.1836 1.8605 0.3465 -0.0383 0.0327  -0.0034 419 LYS A O   
2650  C CB  . LYS A 410 ? 0.1942 1.9729 0.3737 -0.1220 0.0267  -0.0125 419 LYS A CB  
2651  C CG  . LYS A 410 ? 0.2180 2.0966 0.4016 -0.1269 0.0257  -0.0050 419 LYS A CG  
2652  C CD  . LYS A 410 ? 0.2620 2.2192 0.4513 -0.1431 0.0259  0.0055  419 LYS A CD  
2653  C CE  . LYS A 410 ? 0.2775 2.3466 0.4703 -0.1332 0.0262  0.0180  419 LYS A CE  
2654  N NZ  . LYS A 410 ? 0.3055 2.3918 0.4998 -0.1566 0.0225  0.0108  419 LYS A NZ  
2655  N N   . THR A 411 ? 0.1801 1.7423 0.3448 -0.0755 0.0295  -0.0247 420 THR A N   
2656  C CA  . THR A 411 ? 0.1778 1.6813 0.3387 -0.0639 0.0312  -0.0244 420 THR A CA  
2657  C C   . THR A 411 ? 0.1831 1.6596 0.3322 -0.0159 0.0329  -0.0164 420 THR A C   
2658  O O   . THR A 411 ? 0.1880 1.6586 0.3302 0.0053  0.0321  -0.0147 420 THR A O   
2659  C CB  . THR A 411 ? 0.1742 1.5996 0.3370 -0.0925 0.0298  -0.0379 420 THR A CB  
2660  O OG1 . THR A 411 ? 0.1692 1.5885 0.3338 -0.1140 0.0273  -0.0477 420 THR A OG1 
2661  C CG2 . THR A 411 ? 0.1738 1.6100 0.3420 -0.1259 0.0292  -0.0397 420 THR A CG2 
2662  N N   . LYS A 412 ? 0.1877 1.6510 0.3324 0.0011  0.0348  -0.0110 421 LYS A N   
2663  C CA  . LYS A 412 ? 0.1984 1.6261 0.3274 0.0455  0.0355  -0.0044 421 LYS A CA  
2664  C C   . LYS A 412 ? 0.1990 1.5335 0.3230 0.0457  0.0348  -0.0109 421 LYS A C   
2665  O O   . LYS A 412 ? 0.1986 1.5111 0.3297 0.0235  0.0356  -0.0155 421 LYS A O   
2666  C CB  . LYS A 412 ? 0.2039 1.6802 0.3285 0.0683  0.0379  0.0061  421 LYS A CB  
2667  C CG  . LYS A 412 ? 0.2439 1.7858 0.3601 0.1009  0.0384  0.0165  421 LYS A CG  
2668  C CD  . LYS A 412 ? 0.2888 1.9021 0.4042 0.1173  0.0413  0.0270  421 LYS A CD  
2669  C CE  . LYS A 412 ? 0.2850 2.0006 0.4033 0.1261  0.0421  0.0362  421 LYS A CE  
2670  N NZ  . LYS A 412 ? 0.3007 2.0857 0.4228 0.1300  0.0449  0.0449  421 LYS A NZ  
2671  N N   . CYS A 413 ? 0.2017 1.4827 0.3120 0.0705  0.0330  -0.0104 422 CYS A N   
2672  C CA  . CYS A 413 ? 0.1978 1.3928 0.3023 0.0710  0.0317  -0.0155 422 CYS A CA  
2673  C C   . CYS A 413 ? 0.2111 1.3665 0.2936 0.1114  0.0301  -0.0082 422 CYS A C   
2674  O O   . CYS A 413 ? 0.2252 1.4002 0.2937 0.1401  0.0287  -0.0007 422 CYS A O   
2675  C CB  . CYS A 413 ? 0.1921 1.3480 0.3017 0.0504  0.0298  -0.0244 422 CYS A CB  
2676  S SG  . CYS A 413 ? 0.2053 1.4052 0.3340 0.0069  0.0304  -0.0337 422 CYS A SG  
2677  N N   . THR A 414 ? 0.2117 1.3079 0.2891 0.1131  0.0298  -0.0104 423 THR A N   
2678  C CA  . THR A 414 ? 0.2281 1.2888 0.2831 0.1489  0.0282  -0.0038 423 THR A CA  
2679  C C   . THR A 414 ? 0.2360 1.2133 0.2850 0.1435  0.0258  -0.0084 423 THR A C   
2680  O O   . THR A 414 ? 0.2310 1.1882 0.2942 0.1175  0.0275  -0.0152 423 THR A O   
2681  C CB  . THR A 414 ? 0.2242 1.3164 0.2811 0.1552  0.0313  -0.0007 423 THR A CB  
2682  O OG1 . THR A 414 ? 0.2212 1.3980 0.2844 0.1594  0.0336  0.0047  423 THR A OG1 
2683  C CG2 . THR A 414 ? 0.2539 1.3103 0.2864 0.1919  0.0295  0.0049  423 THR A CG2 
2684  N N   . ALA A 415 ? 0.2541 1.1816 0.2803 0.1679  0.0214  -0.0042 424 ALA A N   
2685  C CA  . ALA A 415 ? 0.2565 1.1085 0.2739 0.1657  0.0187  -0.0067 424 ALA A CA  
2686  C C   . ALA A 415 ? 0.2802 1.1095 0.2737 0.1980  0.0170  -0.0009 424 ALA A C   
2687  O O   . ALA A 415 ? 0.3088 1.1424 0.2793 0.2297  0.0141  0.0062  424 ALA A O   
2688  C CB  . ALA A 415 ? 0.2643 1.0732 0.2715 0.1657  0.0140  -0.0060 424 ALA A CB  
2689  N N   . SER A 416 ? 0.2761 1.0794 0.2728 0.1915  0.0183  -0.0039 425 SER A N   
2690  C CA  . SER A 416 ? 0.3023 1.0795 0.2748 0.2219  0.0164  0.0006  425 SER A CA  
2691  C C   . SER A 416 ? 0.3176 1.0120 0.2764 0.2193  0.0118  -0.0013 425 SER A C   
2692  O O   . SER A 416 ? 0.2963 0.9640 0.2708 0.1909  0.0120  -0.0068 425 SER A O   
2693  C CB  . SER A 416 ? 0.2928 1.1188 0.2781 0.2206  0.0218  0.0005  425 SER A CB  
2694  O OG  . SER A 416 ? 0.2658 1.1628 0.2759 0.1996  0.0262  -0.0007 425 SER A OG  
2695  N N   . ASN A 417 ? 0.3585 1.0125 0.2856 0.2499  0.0072  0.0032  426 ASN A N   
2696  C CA  . ASN A 417 ? 0.3850 0.9597 0.2940 0.2487  0.0014  0.0027  426 ASN A CA  
2697  C C   . ASN A 417 ? 0.3927 0.9495 0.3093 0.2399  0.0038  -0.0014 426 ASN A C   
2698  O O   . ASN A 417 ? 0.3707 0.9755 0.3092 0.2305  0.0102  -0.0039 426 ASN A O   
2699  C CB  . ASN A 417 ? 0.4248 0.9534 0.2903 0.2840  -0.0065 0.0094  426 ASN A CB  
2700  C CG  . ASN A 417 ? 0.4436 0.9704 0.2861 0.3164  -0.0067 0.0113  426 ASN A CG  
2701  O OD1 . ASN A 417 ? 0.4152 0.9605 0.2728 0.3099  -0.0018 0.0078  426 ASN A OD1 
2702  N ND2 . ASN A 417 ? 0.4819 0.9847 0.2857 0.3523  -0.0126 0.0169  426 ASN A ND2 
2703  N N   . LYS A 418 ? 0.4334 0.9203 0.3309 0.2410  -0.0019 -0.0013 427 LYS A N   
2704  C CA  . LYS A 418 ? 0.4498 0.9047 0.3456 0.2380  -0.0016 -0.0040 427 LYS A CA  
2705  C C   . LYS A 418 ? 0.4469 0.9446 0.3460 0.2533  0.0037  -0.0040 427 LYS A C   
2706  O O   . LYS A 418 ? 0.4169 0.9326 0.3399 0.2334  0.0088  -0.0077 427 LYS A O   
2707  C CB  . LYS A 418 ? 0.4987 0.8787 0.3563 0.2554  -0.0107 -0.0007 427 LYS A CB  
2708  C CG  . LYS A 418 ? 0.5279 0.8511 0.3864 0.2312  -0.0152 -0.0021 427 LYS A CG  
2709  C CD  . LYS A 418 ? 0.5980 0.8534 0.4199 0.2475  -0.0231 0.0001  427 LYS A CD  
2710  C CE  . LYS A 418 ? 0.6159 0.8211 0.4416 0.2209  -0.0270 -0.0010 427 LYS A CE  
2711  N NZ  . LYS A 418 ? 0.5894 0.8209 0.4550 0.1920  -0.0193 -0.0070 427 LYS A NZ  
2712  N N   . ASN A 419 ? 0.4808 0.9928 0.3539 0.2895  0.0020  0.0008  428 ASN A N   
2713  C CA  . ASN A 419 ? 0.4883 1.0464 0.3591 0.3111  0.0065  0.0023  428 ASN A CA  
2714  C C   . ASN A 419 ? 0.4691 1.1192 0.3621 0.3112  0.0133  0.0046  428 ASN A C   
2715  O O   . ASN A 419 ? 0.4758 1.1735 0.3674 0.3293  0.0171  0.0072  428 ASN A O   
2716  C CB  . ASN A 419 ? 0.5332 1.0526 0.3591 0.3538  0.0006  0.0056  428 ASN A CB  
2717  C CG  . ASN A 419 ? 0.5482 1.0019 0.3419 0.3647  -0.0087 0.0079  428 ASN A CG  
2718  O OD1 . ASN A 419 ? 0.5168 0.9023 0.2964 0.3557  -0.0145 0.0064  428 ASN A OD1 
2719  N ND2 . ASN A 419 ? 0.5610 1.0354 0.3404 0.3851  -0.0106 0.0125  428 ASN A ND2 
2720  N N   . ARG A 420 ? 0.4466 1.1234 0.3600 0.2895  0.0148  0.0038  429 ARG A N   
2721  C CA  . ARG A 420 ? 0.4225 1.1835 0.3603 0.2802  0.0208  0.0052  429 ARG A CA  
2722  C C   . ARG A 420 ? 0.4368 1.2396 0.3589 0.3102  0.0199  0.0112  429 ARG A C   
2723  O O   . ARG A 420 ? 0.4249 1.2983 0.3666 0.3008  0.0241  0.0129  429 ARG A O   
2724  C CB  . ARG A 420 ? 0.4109 1.2178 0.3641 0.2744  0.0264  0.0054  429 ARG A CB  
2725  C CG  . ARG A 420 ? 0.4019 1.1844 0.3778 0.2382  0.0284  -0.0003 429 ARG A CG  
2726  C CD  . ARG A 420 ? 0.4201 1.2601 0.4292 0.2023  0.0334  -0.0023 429 ARG A CD  
2727  N NE  . ARG A 420 ? 0.4517 1.2539 0.4786 0.1675  0.0341  -0.0087 429 ARG A NE  
2728  C CZ  . ARG A 420 ? 0.4679 1.2552 0.4997 0.1589  0.0358  -0.0097 429 ARG A CZ  
2729  N NH1 . ARG A 420 ? 0.4739 1.2827 0.4949 0.1815  0.0373  -0.0047 429 ARG A NH1 
2730  N NH2 . ARG A 420 ? 0.4578 1.2084 0.5043 0.1284  0.0361  -0.0155 429 ARG A NH2 
2731  N N   . GLY A 421 ? 0.4665 1.2254 0.3517 0.3459  0.0141  0.0147  430 GLY A N   
2732  C CA  . GLY A 421 ? 0.4748 1.2545 0.3418 0.3718  0.0116  0.0202  430 GLY A CA  
2733  C C   . GLY A 421 ? 0.4434 1.2383 0.3322 0.3433  0.0118  0.0189  430 GLY A C   
2734  O O   . GLY A 421 ? 0.4345 1.1824 0.3323 0.3161  0.0096  0.0146  430 GLY A O   
2735  N N   . ILE A 422 ? 0.4281 1.2923 0.3247 0.3504  0.0146  0.0228  431 ILE A N   
2736  C CA  . ILE A 422 ? 0.3923 1.2832 0.3117 0.3229  0.0156  0.0211  431 ILE A CA  
2737  C C   . ILE A 422 ? 0.4154 1.2618 0.3091 0.3398  0.0090  0.0249  431 ILE A C   
2738  O O   . ILE A 422 ? 0.4425 1.2914 0.3071 0.3779  0.0062  0.0313  431 ILE A O   
2739  C CB  . ILE A 422 ? 0.3744 1.3635 0.3114 0.3239  0.0210  0.0245  431 ILE A CB  
2740  C CG1 . ILE A 422 ? 0.3534 1.3882 0.3201 0.2954  0.0270  0.0210  431 ILE A CG1 
2741  C CG2 . ILE A 422 ? 0.3553 1.3717 0.3066 0.3057  0.0209  0.0241  431 ILE A CG2 
2742  C CD1 . ILE A 422 ? 0.3824 1.4670 0.3413 0.3222  0.0303  0.0265  431 ILE A CD1 
2743  N N   . ILE A 423 ? 0.4081 1.2134 0.3105 0.3127  0.0063  0.0214  432 ILE A N   
2744  C CA  . ILE A 423 ? 0.4408 1.2028 0.3178 0.3262  -0.0006 0.0263  432 ILE A CA  
2745  C C   . ILE A 423 ? 0.4262 1.2346 0.3179 0.3155  0.0006  0.0277  432 ILE A C   
2746  O O   . ILE A 423 ? 0.4563 1.2635 0.3251 0.3401  -0.0034 0.0346  432 ILE A O   
2747  C CB  . ILE A 423 ? 0.4452 1.1294 0.3165 0.3061  -0.0061 0.0240  432 ILE A CB  
2748  C CG1 . ILE A 423 ? 0.4469 1.0925 0.3242 0.2923  -0.0052 0.0185  432 ILE A CG1 
2749  C CG2 . ILE A 423 ? 0.5009 1.1254 0.3296 0.3332  -0.0154 0.0319  432 ILE A CG2 
2750  C CD1 . ILE A 423 ? 0.4626 1.0436 0.3420 0.2651  -0.0097 0.0159  432 ILE A CD1 
2751  N N   . LYS A 424 ? 0.3897 1.2321 0.3169 0.2785  0.0054  0.0211  433 LYS A N   
2752  C CA  . LYS A 424 ? 0.3818 1.2676 0.3226 0.2666  0.0063  0.0216  433 LYS A CA  
2753  C C   . LYS A 424 ? 0.3483 1.3191 0.3176 0.2516  0.0130  0.0186  433 LYS A C   
2754  O O   . LYS A 424 ? 0.3308 1.3171 0.3158 0.2376  0.0171  0.0141  433 LYS A O   
2755  C CB  . LYS A 424 ? 0.3739 1.2182 0.3265 0.2352  0.0041  0.0164  433 LYS A CB  
2756  C CG  . LYS A 424 ? 0.3937 1.2738 0.3554 0.2253  0.0039  0.0174  433 LYS A CG  
2757  C CD  . LYS A 424 ? 0.4232 1.2551 0.3863 0.2041  0.0000  0.0154  433 LYS A CD  
2758  C CE  . LYS A 424 ? 0.4278 1.3063 0.4016 0.1952  0.0005  0.0160  433 LYS A CE  
2759  N NZ  . LYS A 424 ? 0.4545 1.2947 0.4099 0.2002  -0.0057 0.0227  433 LYS A NZ  
2760  N N   . THR A 425 ? 0.3395 1.3660 0.3146 0.2532  0.0139  0.0215  434 THR A N   
2761  C CA  . THR A 425 ? 0.3170 1.4239 0.3191 0.2327  0.0194  0.0186  434 THR A CA  
2762  C C   . THR A 425 ? 0.3022 1.4392 0.3185 0.2120  0.0192  0.0161  434 THR A C   
2763  O O   . THR A 425 ? 0.3202 1.4429 0.3206 0.2290  0.0155  0.0213  434 THR A O   
2764  C CB  . THR A 425 ? 0.3290 1.4988 0.3228 0.2625  0.0218  0.0263  434 THR A CB  
2765  O OG1 . THR A 425 ? 0.3101 1.5660 0.3271 0.2434  0.0257  0.0259  434 THR A OG1 
2766  C CG2 . THR A 425 ? 0.3700 1.5280 0.3310 0.3073  0.0177  0.0359  434 THR A CG2 
2767  N N   . PHE A 426 ? 0.2784 1.4535 0.3220 0.1755  0.0225  0.0084  435 PHE A N   
2768  C CA  . PHE A 426 ? 0.2749 1.4456 0.3316 0.1477  0.0216  0.0017  435 PHE A CA  
2769  C C   . PHE A 426 ? 0.2828 1.5212 0.3485 0.1404  0.0222  0.0027  435 PHE A C   
2770  O O   . PHE A 426 ? 0.2705 1.5754 0.3524 0.1224  0.0249  0.0006  435 PHE A O   
2771  C CB  . PHE A 426 ? 0.2544 1.3910 0.3284 0.1115  0.0229  -0.0098 435 PHE A CB  
2772  C CG  . PHE A 426 ? 0.2523 1.3062 0.3160 0.1152  0.0204  -0.0115 435 PHE A CG  
2773  C CD1 . PHE A 426 ? 0.2415 1.2619 0.3070 0.1101  0.0217  -0.0145 435 PHE A CD1 
2774  C CD2 . PHE A 426 ? 0.2573 1.2688 0.3085 0.1233  0.0165  -0.0091 435 PHE A CD2 
2775  C CE1 . PHE A 426 ? 0.2295 1.1765 0.2851 0.1130  0.0192  -0.0156 435 PHE A CE1 
2776  C CE2 . PHE A 426 ? 0.2585 1.1974 0.2998 0.1243  0.0136  -0.0097 435 PHE A CE2 
2777  C CZ  . PHE A 426 ? 0.2395 1.1472 0.2831 0.1195  0.0150  -0.0131 435 PHE A CZ  
2778  N N   . SER A 427 ? 0.3069 1.5251 0.3616 0.1513  0.0189  0.0059  436 SER A N   
2779  C CA  . SER A 427 ? 0.3140 1.5902 0.3717 0.1528  0.0186  0.0092  436 SER A CA  
2780  C C   . SER A 427 ? 0.2939 1.5953 0.3744 0.1123  0.0199  -0.0019 436 SER A C   
2781  O O   . SER A 427 ? 0.2902 1.5743 0.3713 0.1031  0.0179  -0.0048 436 SER A O   
2782  C CB  . SER A 427 ? 0.3406 1.5788 0.3754 0.1792  0.0140  0.0174  436 SER A CB  
2783  O OG  . SER A 427 ? 0.3570 1.6535 0.3892 0.1912  0.0135  0.0238  436 SER A OG  
2784  N N   . ASN A 428 ? 0.2775 1.6180 0.3748 0.0879  0.0228  -0.0079 437 ASN A N   
2785  C CA  . ASN A 428 ? 0.2631 1.6346 0.3776 0.0512  0.0233  -0.0180 437 ASN A CA  
2786  C C   . ASN A 428 ? 0.2487 1.5751 0.3650 0.0356  0.0213  -0.0264 437 ASN A C   
2787  O O   . ASN A 428 ? 0.2417 1.6015 0.3616 0.0275  0.0205  -0.0281 437 ASN A O   
2788  C CB  . ASN A 428 ? 0.2707 1.7286 0.3882 0.0558  0.0237  -0.0118 437 ASN A CB  
2789  C CG  . ASN A 428 ? 0.2714 1.7768 0.4055 0.0160  0.0240  -0.0211 437 ASN A CG  
2790  O OD1 . ASN A 428 ? 0.2915 1.7940 0.4341 -0.0091 0.0249  -0.0273 437 ASN A OD1 
2791  N ND2 . ASN A 428 ? 0.2788 1.8269 0.4157 0.0095  0.0228  -0.0217 437 ASN A ND2 
2792  N N   . GLY A 429 ? 0.2450 1.4994 0.3585 0.0319  0.0207  -0.0311 438 GLY A N   
2793  C CA  . GLY A 429 ? 0.2350 1.4460 0.3494 0.0193  0.0190  -0.0382 438 GLY A CA  
2794  C C   . GLY A 429 ? 0.2290 1.3759 0.3461 0.0060  0.0195  -0.0460 438 GLY A C   
2795  O O   . GLY A 429 ? 0.2280 1.3769 0.3530 -0.0103 0.0214  -0.0520 438 GLY A O   
2796  N N   . CYS A 430 ? 0.2256 1.3175 0.3352 0.0127  0.0175  -0.0450 439 CYS A N   
2797  C CA  . CYS A 430 ? 0.2113 1.2432 0.3231 0.0012  0.0178  -0.0519 439 CYS A CA  
2798  C C   . CYS A 430 ? 0.2141 1.1915 0.3114 0.0208  0.0148  -0.0433 439 CYS A C   
2799  O O   . CYS A 430 ? 0.2171 1.1833 0.3084 0.0245  0.0122  -0.0399 439 CYS A O   
2800  C CB  . CYS A 430 ? 0.2032 1.2310 0.3256 -0.0260 0.0184  -0.0653 439 CYS A CB  
2801  S SG  . CYS A 430 ? 0.2172 1.1791 0.3374 -0.0308 0.0171  -0.0697 439 CYS A SG  
2802  N N   . ASP A 431 ? 0.2123 1.1562 0.3027 0.0319  0.0147  -0.0394 440 ASP A N   
2803  C CA  . ASP A 431 ? 0.2220 1.1132 0.2943 0.0514  0.0108  -0.0302 440 ASP A CA  
2804  C C   . ASP A 431 ? 0.2062 1.0430 0.2799 0.0424  0.0109  -0.0345 440 ASP A C   
2805  O O   . ASP A 431 ? 0.1950 1.0351 0.2826 0.0251  0.0144  -0.0438 440 ASP A O   
2806  C CB  . ASP A 431 ? 0.2479 1.1484 0.3041 0.0802  0.0097  -0.0197 440 ASP A CB  
2807  C CG  . ASP A 431 ? 0.3001 1.2039 0.3371 0.1031  0.0053  -0.0084 440 ASP A CG  
2808  O OD1 . ASP A 431 ? 0.3422 1.1928 0.3619 0.1111  0.0004  -0.0021 440 ASP A OD1 
2809  O OD2 . ASP A 431 ? 0.3288 1.2876 0.3664 0.1126  0.0064  -0.0051 440 ASP A OD2 
2810  N N   . TYR A 432 ? 0.2033 0.9898 0.2609 0.0540  0.0066  -0.0271 441 TYR A N   
2811  C CA  . TYR A 432 ? 0.1894 0.9236 0.2461 0.0474  0.0059  -0.0293 441 TYR A CA  
2812  C C   . TYR A 432 ? 0.2030 0.9033 0.2388 0.0702  0.0026  -0.0201 441 TYR A C   
2813  O O   . TYR A 432 ? 0.2236 0.9242 0.2409 0.0901  -0.0011 -0.0108 441 TYR A O   
2814  C CB  . TYR A 432 ? 0.1896 0.8950 0.2442 0.0376  0.0028  -0.0283 441 TYR A CB  
2815  C CG  . TYR A 432 ? 0.1879 0.8410 0.2397 0.0311  0.0011  -0.0287 441 TYR A CG  
2816  C CD1 . TYR A 432 ? 0.1775 0.8251 0.2463 0.0119  0.0048  -0.0395 441 TYR A CD1 
2817  C CD2 . TYR A 432 ? 0.2061 0.8148 0.2365 0.0439  -0.0047 -0.0181 441 TYR A CD2 
2818  C CE1 . TYR A 432 ? 0.1718 0.7754 0.2384 0.0068  0.0035  -0.0392 441 TYR A CE1 
2819  C CE2 . TYR A 432 ? 0.2138 0.7779 0.2417 0.0364  -0.0065 -0.0180 441 TYR A CE2 
2820  C CZ  . TYR A 432 ? 0.1895 0.7536 0.2366 0.0183  -0.0022 -0.0282 441 TYR A CZ  
2821  O OH  . TYR A 432 ? 0.1798 0.7028 0.2236 0.0125  -0.0042 -0.0269 441 TYR A OH  
2822  N N   . VAL A 433 ? 0.2006 0.8695 0.2367 0.0684  0.0035  -0.0226 442 VAL A N   
2823  C CA  . VAL A 433 ? 0.2257 0.8535 0.2385 0.0900  -0.0006 -0.0144 442 VAL A CA  
2824  C C   . VAL A 433 ? 0.2314 0.8060 0.2426 0.0794  -0.0025 -0.0159 442 VAL A C   
2825  O O   . VAL A 433 ? 0.2224 0.7989 0.2522 0.0578  0.0004  -0.0236 442 VAL A O   
2826  C CB  . VAL A 433 ? 0.2244 0.8761 0.2380 0.1026  0.0029  -0.0152 442 VAL A CB  
2827  C CG1 . VAL A 433 ? 0.2384 0.9384 0.2460 0.1207  0.0034  -0.0102 442 VAL A CG1 
2828  C CG2 . VAL A 433 ? 0.1951 0.8703 0.2342 0.0801  0.0090  -0.0256 442 VAL A CG2 
2829  N N   . SER A 434 ? 0.2559 0.7835 0.2446 0.0939  -0.0073 -0.0093 443 SER A N   
2830  C CA  . SER A 434 ? 0.2580 0.7402 0.2481 0.0811  -0.0087 -0.0114 443 SER A CA  
2831  C C   . SER A 434 ? 0.2802 0.7293 0.2566 0.0937  -0.0100 -0.0097 443 SER A C   
2832  O O   . SER A 434 ? 0.3042 0.7593 0.2654 0.1159  -0.0108 -0.0060 443 SER A O   
2833  C CB  . SER A 434 ? 0.2722 0.7188 0.2490 0.0746  -0.0154 -0.0047 443 SER A CB  
2834  O OG  . SER A 434 ? 0.2979 0.6952 0.2440 0.0898  -0.0229 0.0044  443 SER A OG  
2835  N N   . ASN A 435 ? 0.2851 0.7003 0.2655 0.0813  -0.0105 -0.0122 444 ASN A N   
2836  C CA  . ASN A 435 ? 0.3083 0.6909 0.2760 0.0917  -0.0118 -0.0111 444 ASN A CA  
2837  C C   . ASN A 435 ? 0.3559 0.6918 0.2875 0.1107  -0.0207 -0.0014 444 ASN A C   
2838  O O   . ASN A 435 ? 0.3646 0.6778 0.2818 0.1072  -0.0270 0.0050  444 ASN A O   
2839  C CB  . ASN A 435 ? 0.2967 0.6574 0.2788 0.0723  -0.0100 -0.0161 444 ASN A CB  
2840  C CG  . ASN A 435 ? 0.2794 0.6663 0.2878 0.0497  -0.0055 -0.0232 444 ASN A CG  
2841  O OD1 . ASN A 435 ? 0.3022 0.7303 0.3229 0.0471  -0.0018 -0.0269 444 ASN A OD1 
2842  N ND2 . ASN A 435 ? 0.2779 0.6420 0.2933 0.0343  -0.0060 -0.0250 444 ASN A ND2 
2843  N N   . LYS A 436 ? 0.3913 0.7098 0.3062 0.1296  -0.0217 -0.0002 445 LYS A N   
2844  C CA  . LYS A 436 ? 0.4544 0.7470 0.3322 0.1582  -0.0285 0.0075  445 LYS A CA  
2845  C C   . LYS A 436 ? 0.4587 0.7876 0.3343 0.1687  -0.0282 0.0108  445 LYS A C   
2846  O O   . LYS A 436 ? 0.4521 0.7922 0.3381 0.1531  -0.0288 0.0119  445 LYS A O   
2847  C CB  . LYS A 436 ? 0.5019 0.7241 0.3447 0.1610  -0.0393 0.0148  445 LYS A CB  
2848  C CG  . LYS A 436 ? 0.5853 0.7707 0.3814 0.1950  -0.0475 0.0221  445 LYS A CG  
2849  C CD  . LYS A 436 ? 0.6369 0.8415 0.4219 0.2277  -0.0437 0.0195  445 LYS A CD  
2850  C CE  . LYS A 436 ? 0.6125 0.8623 0.4306 0.2223  -0.0332 0.0110  445 LYS A CE  
2851  N NZ  . LYS A 436 ? 0.5957 0.8240 0.4329 0.1956  -0.0316 0.0063  445 LYS A NZ  
2852  N N   . GLY A 437 ? 0.4768 0.8248 0.3373 0.1968  -0.0275 0.0130  446 GLY A N   
2853  C CA  . GLY A 437 ? 0.4557 0.8646 0.3286 0.2044  -0.0229 0.0129  446 GLY A CA  
2854  C C   . GLY A 437 ? 0.4131 0.8694 0.3169 0.1946  -0.0137 0.0049  446 GLY A C   
2855  O O   . GLY A 437 ? 0.4310 0.8910 0.3269 0.2118  -0.0121 0.0046  446 GLY A O   
2856  N N   . VAL A 438 ? 0.3621 0.8481 0.2986 0.1659  -0.0084 -0.0016 447 VAL A N   
2857  C CA  . VAL A 438 ? 0.3245 0.8654 0.2885 0.1558  -0.0004 -0.0081 447 VAL A CA  
2858  C C   . VAL A 438 ? 0.3002 0.8279 0.2811 0.1374  0.0032  -0.0146 447 VAL A C   
2859  O O   . VAL A 438 ? 0.2969 0.7890 0.2827 0.1202  0.0017  -0.0171 447 VAL A O   
2860  C CB  . VAL A 438 ? 0.3007 0.8888 0.2870 0.1379  0.0031  -0.0117 447 VAL A CB  
2861  C CG1 . VAL A 438 ? 0.2896 0.9389 0.2958 0.1327  0.0097  -0.0158 447 VAL A CG1 
2862  C CG2 . VAL A 438 ? 0.3247 0.9221 0.2941 0.1550  -0.0009 -0.0047 447 VAL A CG2 
2863  N N   . ASP A 439 ? 0.2860 0.8470 0.2759 0.1411  0.0081  -0.0165 448 ASP A N   
2864  C CA  . ASP A 439 ? 0.2651 0.8162 0.2681 0.1271  0.0115  -0.0213 448 ASP A CA  
2865  C C   . ASP A 439 ? 0.2328 0.8400 0.2626 0.1074  0.0179  -0.0265 448 ASP A C   
2866  O O   . ASP A 439 ? 0.2152 0.8162 0.2606 0.0869  0.0208  -0.0319 448 ASP A O   
2867  C CB  . ASP A 439 ? 0.2910 0.8305 0.2746 0.1526  0.0104  -0.0170 448 ASP A CB  
2868  C CG  . ASP A 439 ? 0.3241 0.8248 0.3096 0.1439  0.0107  -0.0198 448 ASP A CG  
2869  O OD1 . ASP A 439 ? 0.3295 0.8350 0.3379 0.1182  0.0144  -0.0254 448 ASP A OD1 
2870  O OD2 . ASP A 439 ? 0.3905 0.8540 0.3523 0.1640  0.0068  -0.0163 448 ASP A OD2 
2871  N N   . THR A 440 ? 0.2231 0.8847 0.2562 0.1134  0.0196  -0.0244 449 THR A N   
2872  C CA  . THR A 440 ? 0.1933 0.9148 0.2466 0.0973  0.0246  -0.0273 449 THR A CA  
2873  C C   . THR A 440 ? 0.1874 0.9543 0.2452 0.0959  0.0247  -0.0266 449 THR A C   
2874  O O   . THR A 440 ? 0.2065 0.9774 0.2482 0.1195  0.0220  -0.0206 449 THR A O   
2875  C CB  . THR A 440 ? 0.2018 0.9552 0.2489 0.1161  0.0268  -0.0220 449 THR A CB  
2876  O OG1 . THR A 440 ? 0.1835 0.9183 0.2389 0.1025  0.0288  -0.0250 449 THR A OG1 
2877  C CG2 . THR A 440 ? 0.2061 1.0404 0.2636 0.1148  0.0301  -0.0193 449 THR A CG2 
2878  N N   . VAL A 441 ? 0.1644 0.9636 0.2422 0.0683  0.0274  -0.0326 450 VAL A N   
2879  C CA  . VAL A 441 ? 0.1565 1.0150 0.2397 0.0670  0.0283  -0.0312 450 VAL A CA  
2880  C C   . VAL A 441 ? 0.1473 1.0581 0.2467 0.0456  0.0319  -0.0334 450 VAL A C   
2881  O O   . VAL A 441 ? 0.1409 1.0335 0.2502 0.0228  0.0332  -0.0389 450 VAL A O   
2882  C CB  . VAL A 441 ? 0.1465 0.9970 0.2346 0.0535  0.0266  -0.0360 450 VAL A CB  
2883  C CG1 . VAL A 441 ? 0.1481 0.9437 0.2206 0.0690  0.0226  -0.0331 450 VAL A CG1 
2884  C CG2 . VAL A 441 ? 0.1394 0.9785 0.2440 0.0198  0.0281  -0.0463 450 VAL A CG2 
2885  N N   . SER A 442 ? 0.1506 1.1272 0.2512 0.0532  0.0330  -0.0281 451 SER A N   
2886  C CA  . SER A 442 ? 0.1447 1.1776 0.2599 0.0290  0.0354  -0.0292 451 SER A CA  
2887  C C   . SER A 442 ? 0.1361 1.2125 0.2581 0.0162  0.0348  -0.0312 451 SER A C   
2888  O O   . SER A 442 ? 0.1399 1.2279 0.2537 0.0371  0.0335  -0.0273 451 SER A O   
2889  C CB  . SER A 442 ? 0.1525 1.2357 0.2638 0.0477  0.0375  -0.0199 451 SER A CB  
2890  O OG  . SER A 442 ? 0.1983 1.2668 0.2907 0.0878  0.0363  -0.0133 451 SER A OG  
2891  N N   . VAL A 443 ? 0.1313 1.2253 0.2664 -0.0196 0.0351  -0.0378 452 VAL A N   
2892  C CA  . VAL A 443 ? 0.1244 1.2687 0.2667 -0.0385 0.0343  -0.0405 452 VAL A CA  
2893  C C   . VAL A 443 ? 0.1270 1.3314 0.2770 -0.0584 0.0353  -0.0367 452 VAL A C   
2894  O O   . VAL A 443 ? 0.1315 1.3161 0.2858 -0.0822 0.0354  -0.0404 452 VAL A O   
2895  C CB  . VAL A 443 ? 0.1154 1.2210 0.2624 -0.0661 0.0325  -0.0526 452 VAL A CB  
2896  C CG1 . VAL A 443 ? 0.1115 1.2674 0.2630 -0.0815 0.0313  -0.0551 452 VAL A CG1 
2897  C CG2 . VAL A 443 ? 0.1129 1.1588 0.2531 -0.0487 0.0316  -0.0550 452 VAL A CG2 
2898  N N   . GLY A 444 ? 0.1241 1.4026 0.2745 -0.0470 0.0360  -0.0282 453 GLY A N   
2899  C CA  . GLY A 444 ? 0.1234 1.4685 0.2807 -0.0650 0.0368  -0.0225 453 GLY A CA  
2900  C C   . GLY A 444 ? 0.1217 1.4408 0.2777 -0.0615 0.0384  -0.0196 453 GLY A C   
2901  O O   . GLY A 444 ? 0.1218 1.4203 0.2690 -0.0269 0.0400  -0.0147 453 GLY A O   
2902  N N   . ASN A 445 ? 0.1240 1.4389 0.2864 -0.0975 0.0375  -0.0230 454 ASN A N   
2903  C CA  . ASN A 445 ? 0.1300 1.4306 0.2920 -0.0962 0.0391  -0.0189 454 ASN A CA  
2904  C C   . ASN A 445 ? 0.1261 1.3402 0.2854 -0.1007 0.0388  -0.0268 454 ASN A C   
2905  O O   . ASN A 445 ? 0.1311 1.3291 0.2889 -0.0949 0.0403  -0.0231 454 ASN A O   
2906  C CB  . ASN A 445 ? 0.1413 1.4977 0.3100 -0.1293 0.0384  -0.0139 454 ASN A CB  
2907  C CG  . ASN A 445 ? 0.1657 1.6063 0.3353 -0.1091 0.0407  -0.0004 454 ASN A CG  
2908  O OD1 . ASN A 445 ? 0.2024 1.6542 0.3710 -0.0986 0.0429  0.0067  454 ASN A OD1 
2909  N ND2 . ASN A 445 ? 0.1792 1.6811 0.3498 -0.0990 0.0406  0.0035  454 ASN A ND2 
2910  N N   . THR A 446 ? 0.1170 1.2788 0.2754 -0.1102 0.0370  -0.0375 455 THR A N   
2911  C CA  . THR A 446 ? 0.1067 1.1870 0.2625 -0.1144 0.0365  -0.0456 455 THR A CA  
2912  C C   . THR A 446 ? 0.0958 1.1422 0.2442 -0.0763 0.0377  -0.0429 455 THR A C   
2913  O O   . THR A 446 ? 0.0887 1.1569 0.2331 -0.0545 0.0375  -0.0397 455 THR A O   
2914  C CB  . THR A 446 ? 0.1131 1.1593 0.2697 -0.1370 0.0340  -0.0577 455 THR A CB  
2915  O OG1 . THR A 446 ? 0.1285 1.2103 0.2881 -0.1724 0.0318  -0.0605 455 THR A OG1 
2916  C CG2 . THR A 446 ? 0.1230 1.0938 0.2770 -0.1438 0.0337  -0.0655 455 THR A CG2 
2917  N N   . LEU A 447 ? 0.0950 1.0867 0.2398 -0.0689 0.0383  -0.0437 456 LEU A N   
2918  C CA  . LEU A 447 ? 0.0978 1.0471 0.2325 -0.0357 0.0383  -0.0414 456 LEU A CA  
2919  C C   . LEU A 447 ? 0.1009 0.9779 0.2344 -0.0425 0.0370  -0.0496 456 LEU A C   
2920  O O   . LEU A 447 ? 0.1071 0.9540 0.2448 -0.0620 0.0373  -0.0542 456 LEU A O   
2921  C CB  . LEU A 447 ? 0.1035 1.0515 0.2329 -0.0181 0.0399  -0.0344 456 LEU A CB  
2922  C CG  . LEU A 447 ? 0.1066 1.0130 0.2211 0.0171  0.0390  -0.0311 456 LEU A CG  
2923  C CD1 . LEU A 447 ? 0.1333 1.0735 0.2377 0.0452  0.0381  -0.0254 456 LEU A CD1 
2924  C CD2 . LEU A 447 ? 0.1036 1.0025 0.2128 0.0299  0.0405  -0.0262 456 LEU A CD2 
2925  N N   . TYR A 448 ? 0.1051 0.9548 0.2320 -0.0262 0.0353  -0.0507 457 TYR A N   
2926  C CA  . TYR A 448 ? 0.1063 0.8924 0.2322 -0.0323 0.0339  -0.0578 457 TYR A CA  
2927  C C   . TYR A 448 ? 0.1106 0.8545 0.2242 -0.0060 0.0326  -0.0525 457 TYR A C   
2928  O O   . TYR A 448 ? 0.1228 0.8821 0.2253 0.0197  0.0316  -0.0451 457 TYR A O   
2929  C CB  . TYR A 448 ? 0.1041 0.8928 0.2318 -0.0384 0.0323  -0.0628 457 TYR A CB  
2930  C CG  . TYR A 448 ? 0.1192 0.9398 0.2563 -0.0670 0.0327  -0.0701 457 TYR A CG  
2931  C CD1 . TYR A 448 ? 0.1412 1.0251 0.2819 -0.0720 0.0332  -0.0664 457 TYR A CD1 
2932  C CD2 . TYR A 448 ? 0.1275 0.9154 0.2681 -0.0887 0.0321  -0.0805 457 TYR A CD2 
2933  C CE1 . TYR A 448 ? 0.1521 1.0630 0.2990 -0.1010 0.0326  -0.0730 457 TYR A CE1 
2934  C CE2 . TYR A 448 ? 0.1421 0.9528 0.2870 -0.1149 0.0315  -0.0879 457 TYR A CE2 
2935  C CZ  . TYR A 448 ? 0.1562 1.0267 0.3039 -0.1224 0.0314  -0.0842 457 TYR A CZ  
2936  O OH  . TYR A 448 ? 0.1704 1.0610 0.3198 -0.1508 0.0298  -0.0916 457 TYR A OH  
2937  N N   . TYR A 449 ? 0.1051 0.7961 0.2183 -0.0113 0.0323  -0.0558 458 TYR A N   
2938  C CA  . TYR A 449 ? 0.1059 0.7539 0.2056 0.0110  0.0302  -0.0509 458 TYR A CA  
2939  C C   . TYR A 449 ? 0.1047 0.7107 0.1996 0.0118  0.0272  -0.0531 458 TYR A C   
2940  O O   . TYR A 449 ? 0.1064 0.6866 0.2090 -0.0054 0.0276  -0.0594 458 TYR A O   
2941  C CB  . TYR A 449 ? 0.1040 0.7237 0.2055 0.0054  0.0315  -0.0517 458 TYR A CB  
2942  C CG  . TYR A 449 ? 0.1039 0.7617 0.2085 0.0058  0.0341  -0.0480 458 TYR A CG  
2943  C CD1 . TYR A 449 ? 0.1040 0.7877 0.2215 -0.0200 0.0364  -0.0516 458 TYR A CD1 
2944  C CD2 . TYR A 449 ? 0.1192 0.7857 0.2115 0.0316  0.0339  -0.0405 458 TYR A CD2 
2945  C CE1 . TYR A 449 ? 0.1275 0.8495 0.2477 -0.0219 0.0385  -0.0467 458 TYR A CE1 
2946  C CE2 . TYR A 449 ? 0.1354 0.8425 0.2306 0.0332  0.0366  -0.0362 458 TYR A CE2 
2947  C CZ  . TYR A 449 ? 0.1379 0.8755 0.2481 0.0055  0.0390  -0.0386 458 TYR A CZ  
2948  O OH  . TYR A 449 ? 0.1405 0.9242 0.2533 0.0057  0.0413  -0.0327 458 TYR A OH  
2949  N N   . VAL A 450 ? 0.1094 0.7083 0.1902 0.0320  0.0239  -0.0472 459 VAL A N   
2950  C CA  . VAL A 450 ? 0.1123 0.6761 0.1878 0.0309  0.0204  -0.0475 459 VAL A CA  
2951  C C   . VAL A 450 ? 0.1249 0.6328 0.1935 0.0314  0.0180  -0.0467 459 VAL A C   
2952  O O   . VAL A 450 ? 0.1246 0.6066 0.1954 0.0214  0.0164  -0.0490 459 VAL A O   
2953  C CB  . VAL A 450 ? 0.1186 0.6883 0.1783 0.0506  0.0166  -0.0404 459 VAL A CB  
2954  C CG1 . VAL A 450 ? 0.1285 0.6699 0.1852 0.0441  0.0131  -0.0405 459 VAL A CG1 
2955  C CG2 . VAL A 450 ? 0.1100 0.7345 0.1769 0.0500  0.0189  -0.0409 459 VAL A CG2 
2956  N N   . ASN A 451 ? 0.1379 0.6310 0.1978 0.0434  0.0179  -0.0432 460 ASN A N   
2957  C CA  . ASN A 451 ? 0.1467 0.5917 0.2000 0.0437  0.0157  -0.0423 460 ASN A CA  
2958  C C   . ASN A 451 ? 0.1442 0.5908 0.2083 0.0346  0.0198  -0.0459 460 ASN A C   
2959  O O   . ASN A 451 ? 0.1361 0.6204 0.2110 0.0283  0.0237  -0.0481 460 ASN A O   
2960  C CB  . ASN A 451 ? 0.1685 0.5854 0.1960 0.0673  0.0103  -0.0343 460 ASN A CB  
2961  C CG  . ASN A 451 ? 0.1939 0.5960 0.2097 0.0705  0.0051  -0.0304 460 ASN A CG  
2962  O OD1 . ASN A 451 ? 0.2126 0.5993 0.2354 0.0549  0.0040  -0.0324 460 ASN A OD1 
2963  N ND2 . ASN A 451 ? 0.2284 0.6363 0.2255 0.0910  0.0019  -0.0244 460 ASN A ND2 
2964  N N   . LYS A 452 ? 0.1575 0.5643 0.2197 0.0309  0.0187  -0.0463 461 LYS A N   
2965  C CA  . LYS A 452 ? 0.1614 0.5683 0.2329 0.0224  0.0223  -0.0490 461 LYS A CA  
2966  C C   . LYS A 452 ? 0.1799 0.5875 0.2374 0.0429  0.0215  -0.0431 461 LYS A C   
2967  O O   . LYS A 452 ? 0.1947 0.5796 0.2327 0.0611  0.0169  -0.0382 461 LYS A O   
2968  C CB  . LYS A 452 ? 0.1604 0.5264 0.2347 0.0123  0.0215  -0.0513 461 LYS A CB  
2969  C CG  . LYS A 452 ? 0.1693 0.5307 0.2528 -0.0025 0.0215  -0.0563 461 LYS A CG  
2970  C CD  . LYS A 452 ? 0.1874 0.5241 0.2792 -0.0152 0.0232  -0.0606 461 LYS A CD  
2971  C CE  . LYS A 452 ? 0.2112 0.5428 0.3098 -0.0265 0.0231  -0.0656 461 LYS A CE  
2972  N NZ  . LYS A 452 ? 0.2321 0.5403 0.3367 -0.0355 0.0248  -0.0693 461 LYS A NZ  
2973  N N   . GLN A 453 ? 0.1853 0.6192 0.2505 0.0402  0.0254  -0.0434 462 GLN A N   
2974  C CA  . GLN A 453 ? 0.2094 0.6494 0.2612 0.0613  0.0250  -0.0381 462 GLN A CA  
2975  C C   . GLN A 453 ? 0.2243 0.6251 0.2716 0.0615  0.0243  -0.0377 462 GLN A C   
2976  O O   . GLN A 453 ? 0.2152 0.6143 0.2768 0.0436  0.0274  -0.0408 462 GLN A O   
2977  C CB  . GLN A 453 ? 0.2021 0.6998 0.2640 0.0589  0.0294  -0.0371 462 GLN A CB  
2978  C CG  . GLN A 453 ? 0.2108 0.7492 0.2770 0.0579  0.0298  -0.0373 462 GLN A CG  
2979  C CD  . GLN A 453 ? 0.2564 0.7862 0.3022 0.0841  0.0256  -0.0328 462 GLN A CD  
2980  O OE1 . GLN A 453 ? 0.2932 0.8336 0.3231 0.1092  0.0248  -0.0277 462 GLN A OE1 
2981  N NE2 . GLN A 453 ? 0.2587 0.7686 0.3031 0.0792  0.0228  -0.0346 462 GLN A NE2 
2982  N N   . GLU A 454 ? 0.2581 0.6244 0.2834 0.0814  0.0196  -0.0339 463 GLU A N   
2983  C CA  . GLU A 454 ? 0.2853 0.6139 0.3026 0.0844  0.0181  -0.0330 463 GLU A CA  
2984  C C   . GLU A 454 ? 0.2863 0.6421 0.3040 0.0934  0.0217  -0.0311 463 GLU A C   
2985  O O   . GLU A 454 ? 0.2988 0.6927 0.3121 0.1078  0.0231  -0.0286 463 GLU A O   
2986  C CB  . GLU A 454 ? 0.3193 0.6051 0.3078 0.1043  0.0109  -0.0292 463 GLU A CB  
2987  C CG  . GLU A 454 ? 0.3819 0.6182 0.3661 0.0924  0.0062  -0.0295 463 GLU A CG  
2988  C CD  . GLU A 454 ? 0.4740 0.6679 0.4261 0.1086  -0.0027 -0.0248 463 GLU A CD  
2989  O OE1 . GLU A 454 ? 0.5146 0.6854 0.4437 0.1269  -0.0060 -0.0226 463 GLU A OE1 
2990  O OE2 . GLU A 454 ? 0.4856 0.6685 0.4340 0.1023  -0.0065 -0.0232 463 GLU A OE2 
2991  N N   . GLY A 455 ? 0.2832 0.6229 0.3052 0.0868  0.0231  -0.0315 464 GLY A N   
2992  C CA  . GLY A 455 ? 0.2905 0.6553 0.3091 0.0989  0.0259  -0.0285 464 GLY A CA  
2993  C C   . GLY A 455 ? 0.2990 0.6330 0.3178 0.0934  0.0260  -0.0286 464 GLY A C   
2994  O O   . GLY A 455 ? 0.2999 0.6099 0.3308 0.0734  0.0263  -0.0315 464 GLY A O   
2995  N N   . LYS A 456 ? 0.3132 0.6461 0.3167 0.1131  0.0254  -0.0256 465 LYS A N   
2996  C CA  . LYS A 456 ? 0.3107 0.6320 0.3178 0.1079  0.0271  -0.0248 465 LYS A CA  
2997  C C   . LYS A 456 ? 0.3068 0.5852 0.3220 0.0885  0.0258  -0.0273 465 LYS A C   
2998  O O   . LYS A 456 ? 0.2916 0.5773 0.3274 0.0654  0.0291  -0.0295 465 LYS A O   
2999  C CB  . LYS A 456 ? 0.2921 0.6658 0.3180 0.0962  0.0333  -0.0227 465 LYS A CB  
3000  C CG  . LYS A 456 ? 0.3027 0.6759 0.3268 0.0994  0.0350  -0.0199 465 LYS A CG  
3001  C CD  . LYS A 456 ? 0.3192 0.7492 0.3574 0.0906  0.0403  -0.0158 465 LYS A CD  
3002  C CE  . LYS A 456 ? 0.3632 0.7945 0.3935 0.1021  0.0414  -0.0120 465 LYS A CE  
3003  N NZ  . LYS A 456 ? 0.3748 0.8365 0.4231 0.0799  0.0458  -0.0079 465 LYS A NZ  
3004  N N   . SER A 457 ? 0.3265 0.5600 0.3237 0.0982  0.0209  -0.0270 466 SER A N   
3005  C CA  . SER A 457 ? 0.3252 0.5264 0.3303 0.0819  0.0203  -0.0281 466 SER A CA  
3006  C C   . SER A 457 ? 0.3147 0.5302 0.3288 0.0778  0.0247  -0.0264 466 SER A C   
3007  O O   . SER A 457 ? 0.3155 0.5508 0.3204 0.0935  0.0258  -0.0238 466 SER A O   
3008  C CB  . SER A 457 ? 0.3515 0.5034 0.3334 0.0918  0.0130  -0.0273 466 SER A CB  
3009  O OG  . SER A 457 ? 0.3975 0.5457 0.3547 0.1168  0.0102  -0.0254 466 SER A OG  
3010  N N   . LEU A 458 ? 0.3064 0.5126 0.3373 0.0573  0.0271  -0.0275 467 LEU A N   
3011  C CA  . LEU A 458 ? 0.3054 0.5165 0.3432 0.0516  0.0303  -0.0252 467 LEU A CA  
3012  C C   . LEU A 458 ? 0.3166 0.4848 0.3491 0.0493  0.0272  -0.0253 467 LEU A C   
3013  O O   . LEU A 458 ? 0.3141 0.4577 0.3485 0.0411  0.0247  -0.0275 467 LEU A O   
3014  C CB  . LEU A 458 ? 0.2881 0.5225 0.3474 0.0293  0.0353  -0.0258 467 LEU A CB  
3015  C CG  . LEU A 458 ? 0.2820 0.5663 0.3459 0.0303  0.0383  -0.0242 467 LEU A CG  
3016  C CD1 . LEU A 458 ? 0.2647 0.5717 0.3461 0.0058  0.0422  -0.0240 467 LEU A CD1 
3017  C CD2 . LEU A 458 ? 0.2853 0.5911 0.3372 0.0503  0.0387  -0.0197 467 LEU A CD2 
3018  N N   . TYR A 459 ? 0.3339 0.4965 0.3593 0.0567  0.0274  -0.0224 468 TYR A N   
3019  C CA  . TYR A 459 ? 0.3537 0.4771 0.3704 0.0573  0.0236  -0.0219 468 TYR A CA  
3020  C C   . TYR A 459 ? 0.3367 0.4625 0.3632 0.0490  0.0272  -0.0192 468 TYR A C   
3021  O O   . TYR A 459 ? 0.3363 0.4880 0.3639 0.0536  0.0304  -0.0165 468 TYR A O   
3022  C CB  . TYR A 459 ? 0.3890 0.4906 0.3776 0.0790  0.0175  -0.0214 468 TYR A CB  
3023  C CG  . TYR A 459 ? 0.4659 0.5256 0.4427 0.0776  0.0123  -0.0206 468 TYR A CG  
3024  C CD1 . TYR A 459 ? 0.5060 0.5391 0.4846 0.0651  0.0085  -0.0212 468 TYR A CD1 
3025  C CD2 . TYR A 459 ? 0.5376 0.5873 0.5012 0.0882  0.0111  -0.0189 468 TYR A CD2 
3026  C CE1 . TYR A 459 ? 0.5345 0.5331 0.5023 0.0616  0.0032  -0.0195 468 TYR A CE1 
3027  C CE2 . TYR A 459 ? 0.5719 0.5831 0.5238 0.0851  0.0057  -0.0180 468 TYR A CE2 
3028  C CZ  . TYR A 459 ? 0.5662 0.5534 0.5206 0.0711  0.0017  -0.0180 468 TYR A CZ  
3029  O OH  . TYR A 459 ? 0.5804 0.5358 0.5234 0.0668  -0.0039 -0.0162 468 TYR A OH  
3030  N N   . VAL A 460 ? 0.3304 0.4314 0.3639 0.0368  0.0266  -0.0194 469 VAL A N   
3031  C CA  . VAL A 460 ? 0.3297 0.4307 0.3716 0.0292  0.0298  -0.0164 469 VAL A CA  
3032  C C   . VAL A 460 ? 0.3496 0.4182 0.3821 0.0322  0.0260  -0.0149 469 VAL A C   
3033  O O   . VAL A 460 ? 0.3491 0.3965 0.3849 0.0242  0.0239  -0.0159 469 VAL A O   
3034  C CB  . VAL A 460 ? 0.3130 0.4188 0.3736 0.0101  0.0337  -0.0173 469 VAL A CB  
3035  C CG1 . VAL A 460 ? 0.3001 0.3952 0.3658 0.0030  0.0356  -0.0138 469 VAL A CG1 
3036  C CG2 . VAL A 460 ? 0.3081 0.4487 0.3769 0.0043  0.0374  -0.0176 469 VAL A CG2 
3037  N N   . LYS A 461 ? 0.3761 0.4443 0.3968 0.0438  0.0251  -0.0123 470 LYS A N   
3038  C CA  . LYS A 461 ? 0.4005 0.4386 0.4073 0.0490  0.0204  -0.0110 470 LYS A CA  
3039  C C   . LYS A 461 ? 0.3916 0.4238 0.4115 0.0369  0.0232  -0.0079 470 LYS A C   
3040  O O   . LYS A 461 ? 0.3793 0.4306 0.4144 0.0280  0.0287  -0.0060 470 LYS A O   
3041  C CB  . LYS A 461 ? 0.4248 0.4633 0.4091 0.0694  0.0176  -0.0106 470 LYS A CB  
3042  C CG  . LYS A 461 ? 0.4763 0.5030 0.4510 0.0749  0.0164  -0.0078 470 LYS A CG  
3043  C CD  . LYS A 461 ? 0.5507 0.5367 0.4974 0.0845  0.0075  -0.0093 470 LYS A CD  
3044  C CE  . LYS A 461 ? 0.5615 0.5361 0.5006 0.0870  0.0064  -0.0066 470 LYS A CE  
3045  N NZ  . LYS A 461 ? 0.5690 0.5045 0.4922 0.0824  -0.0017 -0.0067 470 LYS A NZ  
3046  N N   . GLY A 462 ? 0.4013 0.4064 0.4141 0.0355  0.0188  -0.0069 471 GLY A N   
3047  C CA  . GLY A 462 ? 0.4114 0.4101 0.4324 0.0281  0.0207  -0.0034 471 GLY A CA  
3048  C C   . GLY A 462 ? 0.4396 0.4196 0.4422 0.0369  0.0156  -0.0016 471 GLY A C   
3049  O O   . GLY A 462 ? 0.4564 0.4178 0.4402 0.0436  0.0090  -0.0035 471 GLY A O   
3050  N N   . GLU A 463 ? 0.4518 0.4350 0.4577 0.0365  0.0180  0.0022  472 GLU A N   
3051  C CA  . GLU A 463 ? 0.4813 0.4455 0.4713 0.0422  0.0131  0.0042  472 GLU A CA  
3052  C C   . GLU A 463 ? 0.4727 0.4209 0.4692 0.0307  0.0109  0.0068  472 GLU A C   
3053  O O   . GLU A 463 ? 0.4605 0.4124 0.4724 0.0211  0.0134  0.0064  472 GLU A O   
3054  C CB  . GLU A 463 ? 0.4894 0.4690 0.4774 0.0497  0.0166  0.0073  472 GLU A CB  
3055  C CG  . GLU A 463 ? 0.5345 0.5167 0.5357 0.0410  0.0201  0.0130  472 GLU A CG  
3056  C CD  . GLU A 463 ? 0.5872 0.5718 0.6105 0.0258  0.0245  0.0146  472 GLU A CD  
3057  O OE1 . GLU A 463 ? 0.5918 0.5887 0.6254 0.0207  0.0279  0.0125  472 GLU A OE1 
3058  O OE2 . GLU A 463 ? 0.6002 0.5743 0.6290 0.0200  0.0245  0.0180  472 GLU A OE2 
3059  N N   . PRO A 464 ? 0.4833 0.4154 0.4669 0.0323  0.0061  0.0092  473 PRO A N   
3060  C CA  . PRO A 464 ? 0.4748 0.4017 0.4683 0.0217  0.0056  0.0128  473 PRO A CA  
3061  C C   . PRO A 464 ? 0.4673 0.4021 0.4702 0.0210  0.0100  0.0176  473 PRO A C   
3062  O O   . PRO A 464 ? 0.4667 0.4074 0.4636 0.0285  0.0115  0.0185  473 PRO A O   
3063  C CB  . PRO A 464 ? 0.4927 0.3972 0.4650 0.0208  -0.0039 0.0132  473 PRO A CB  
3064  C CG  . PRO A 464 ? 0.5155 0.4097 0.4649 0.0334  -0.0075 0.0107  473 PRO A CG  
3065  C CD  . PRO A 464 ? 0.5072 0.4218 0.4642 0.0426  -0.0007 0.0081  473 PRO A CD  
3066  N N   . ILE A 465 ? 0.4631 0.3987 0.4791 0.0132  0.0117  0.0209  474 ILE A N   
3067  C CA  . ILE A 465 ? 0.4630 0.4058 0.4909 0.0116  0.0170  0.0258  474 ILE A CA  
3068  C C   . ILE A 465 ? 0.4716 0.4088 0.4960 0.0107  0.0141  0.0310  474 ILE A C   
3069  O O   . ILE A 465 ? 0.4704 0.4023 0.4916 0.0066  0.0093  0.0317  474 ILE A O   
3070  C CB  . ILE A 465 ? 0.4537 0.4026 0.4988 0.0059  0.0228  0.0250  474 ILE A CB  
3071  C CG1 . ILE A 465 ? 0.4629 0.4139 0.5168 0.0042  0.0278  0.0303  474 ILE A CG1 
3072  C CG2 . ILE A 465 ? 0.4436 0.3890 0.4929 0.0018  0.0207  0.0234  474 ILE A CG2 
3073  C CD1 . ILE A 465 ? 0.4751 0.4274 0.5403 -0.0015 0.0328  0.0285  474 ILE A CD1 
3074  N N   . ILE A 466 ? 0.4861 0.4275 0.5115 0.0136  0.0169  0.0354  475 ILE A N   
3075  C CA  . ILE A 466 ? 0.5077 0.4451 0.5241 0.0154  0.0132  0.0401  475 ILE A CA  
3076  C C   . ILE A 466 ? 0.5138 0.4549 0.5405 0.0128  0.0156  0.0469  475 ILE A C   
3077  O O   . ILE A 466 ? 0.5051 0.4510 0.5405 0.0138  0.0212  0.0509  475 ILE A O   
3078  C CB  . ILE A 466 ? 0.5180 0.4582 0.5229 0.0232  0.0133  0.0404  475 ILE A CB  
3079  C CG1 . ILE A 466 ? 0.5249 0.4800 0.5417 0.0239  0.0210  0.0421  475 ILE A CG1 
3080  C CG2 . ILE A 466 ? 0.5058 0.4352 0.4896 0.0293  0.0070  0.0342  475 ILE A CG2 
3081  C CD1 . ILE A 466 ? 0.5298 0.4944 0.5475 0.0262  0.0242  0.0490  475 ILE A CD1 
3082  N N   . ASN A 467 ? 0.5301 0.4699 0.5545 0.0094  0.0109  0.0489  476 ASN A N   
3083  C CA  . ASN A 467 ? 0.5457 0.4921 0.5773 0.0094  0.0123  0.0559  476 ASN A CA  
3084  C C   . ASN A 467 ? 0.5616 0.5092 0.5838 0.0115  0.0096  0.0612  476 ASN A C   
3085  O O   . ASN A 467 ? 0.5710 0.5185 0.5827 0.0082  0.0029  0.0630  476 ASN A O   
3086  C CB  . ASN A 467 ? 0.5424 0.4956 0.5796 0.0056  0.0102  0.0571  476 ASN A CB  
3087  C CG  . ASN A 467 ? 0.5551 0.5176 0.6028 0.0098  0.0143  0.0637  476 ASN A CG  
3088  O OD1 . ASN A 467 ? 0.5671 0.5253 0.6205 0.0145  0.0201  0.0655  476 ASN A OD1 
3089  N ND2 . ASN A 467 ? 0.5488 0.5244 0.5971 0.0083  0.0109  0.0680  476 ASN A ND2 
3090  N N   . PHE A 468 ? 0.5688 0.5187 0.5955 0.0158  0.0148  0.0645  477 PHE A N   
3091  C CA  . PHE A 468 ? 0.5841 0.5347 0.6008 0.0197  0.0141  0.0661  477 PHE A CA  
3092  C C   . PHE A 468 ? 0.5835 0.5405 0.6018 0.0215  0.0149  0.0744  477 PHE A C   
3093  O O   . PHE A 468 ? 0.5898 0.5511 0.6090 0.0249  0.0186  0.0785  477 PHE A O   
3094  C CB  . PHE A 468 ? 0.5874 0.5415 0.6117 0.0214  0.0207  0.0656  477 PHE A CB  
3095  C CG  . PHE A 468 ? 0.6044 0.5573 0.6440 0.0182  0.0262  0.0681  477 PHE A CG  
3096  C CD1 . PHE A 468 ? 0.6167 0.5698 0.6618 0.0193  0.0297  0.0761  477 PHE A CD1 
3097  C CD2 . PHE A 468 ? 0.5873 0.5362 0.6329 0.0150  0.0271  0.0623  477 PHE A CD2 
3098  C CE1 . PHE A 468 ? 0.6225 0.5681 0.6764 0.0181  0.0337  0.0777  477 PHE A CE1 
3099  C CE2 . PHE A 468 ? 0.5849 0.5290 0.6406 0.0133  0.0313  0.0633  477 PHE A CE2 
3100  C CZ  . PHE A 468 ? 0.6072 0.5476 0.6658 0.0152  0.0344  0.0707  477 PHE A CZ  
3101  N N   . TYR A 469 ? 0.5753 0.5360 0.5941 0.0191  0.0114  0.0779  478 TYR A N   
3102  C CA  . TYR A 469 ? 0.5661 0.5356 0.5900 0.0220  0.0134  0.0867  478 TYR A CA  
3103  C C   . TYR A 469 ? 0.5626 0.5374 0.5749 0.0224  0.0087  0.0908  478 TYR A C   
3104  O O   . TYR A 469 ? 0.5659 0.5382 0.5646 0.0178  0.0012  0.0879  478 TYR A O   
3105  C CB  . TYR A 469 ? 0.5653 0.5417 0.5994 0.0222  0.0145  0.0898  478 TYR A CB  
3106  C CG  . TYR A 469 ? 0.5655 0.5563 0.5984 0.0231  0.0114  0.0972  478 TYR A CG  
3107  C CD1 . TYR A 469 ? 0.5604 0.5569 0.5987 0.0302  0.0156  0.1054  478 TYR A CD1 
3108  C CD2 . TYR A 469 ? 0.5688 0.5682 0.5941 0.0159  0.0039  0.0968  478 TYR A CD2 
3109  C CE1 . TYR A 469 ? 0.5775 0.5912 0.6150 0.0319  0.0128  0.1127  478 TYR A CE1 
3110  C CE2 . TYR A 469 ? 0.5769 0.5945 0.6014 0.0150  0.0007  0.1043  478 TYR A CE2 
3111  C CZ  . TYR A 469 ? 0.5845 0.6110 0.6158 0.0239  0.0054  0.1121  478 TYR A CZ  
3112  O OH  . TYR A 469 ? 0.5937 0.6423 0.6242 0.0240  0.0023  0.1201  478 TYR A OH  
3113  N N   . ASP A 470 ? 0.5507 0.5313 0.5666 0.0271  0.0127  0.0978  479 ASP A N   
3114  C CA  . ASP A 470 ? 0.5522 0.5385 0.5569 0.0281  0.0088  0.1014  479 ASP A CA  
3115  C C   . ASP A 470 ? 0.5406 0.5399 0.5499 0.0308  0.0098  0.1114  479 ASP A C   
3116  O O   . ASP A 470 ? 0.5396 0.5411 0.5562 0.0358  0.0156  0.1180  479 ASP A O   
3117  C CB  . ASP A 470 ? 0.5627 0.5460 0.5595 0.0319  0.0104  0.0990  479 ASP A CB  
3118  C CG  . ASP A 470 ? 0.5975 0.5817 0.5757 0.0329  0.0039  0.0982  479 ASP A CG  
3119  O OD1 . ASP A 470 ? 0.6224 0.6005 0.5882 0.0277  -0.0040 0.0947  479 ASP A OD1 
3120  O OD2 . ASP A 470 ? 0.6246 0.6153 0.5993 0.0382  0.0064  0.1013  479 ASP A OD2 
3121  N N   . PRO A 471 ? 0.5329 0.5414 0.5361 0.0266  0.0034  0.1134  480 PRO A N   
3122  C CA  . PRO A 471 ? 0.5200 0.5453 0.5301 0.0301  0.0046  0.1232  480 PRO A CA  
3123  C C   . PRO A 471 ? 0.5139 0.5436 0.5202 0.0348  0.0063  0.1293  480 PRO A C   
3124  O O   . PRO A 471 ? 0.5094 0.5330 0.5045 0.0338  0.0042  0.1255  480 PRO A O   
3125  C CB  . PRO A 471 ? 0.5226 0.5600 0.5247 0.0216  -0.0039 0.1235  480 PRO A CB  
3126  C CG  . PRO A 471 ? 0.5390 0.5604 0.5222 0.0142  -0.0109 0.1152  480 PRO A CG  
3127  C CD  . PRO A 471 ? 0.5413 0.5452 0.5279 0.0182  -0.0059 0.1078  480 PRO A CD  
3128  N N   . LEU A 472 ? 0.5082 0.5488 0.5229 0.0413  0.0102  0.1389  481 LEU A N   
3129  C CA  . LEU A 472 ? 0.5074 0.5567 0.5188 0.0455  0.0111  0.1469  481 LEU A CA  
3130  C C   . LEU A 472 ? 0.5040 0.5733 0.5094 0.0428  0.0048  0.1515  481 LEU A C   
3131  O O   . LEU A 472 ? 0.5008 0.5841 0.5118 0.0429  0.0035  0.1549  481 LEU A O   
3132  C CB  . LEU A 472 ? 0.5097 0.5567 0.5312 0.0546  0.0184  0.1558  481 LEU A CB  
3133  C CG  . LEU A 472 ? 0.5137 0.5613 0.5322 0.0577  0.0213  0.1627  481 LEU A CG  
3134  C CD1 . LEU A 472 ? 0.5216 0.5670 0.5302 0.0524  0.0188  0.1558  481 LEU A CD1 
3135  C CD2 . LEU A 472 ? 0.4994 0.5316 0.5246 0.0623  0.0282  0.1680  481 LEU A CD2 
3136  N N   . VAL A 473 ? 0.5048 0.5782 0.4982 0.0403  0.0008  0.1520  482 VAL A N   
3137  C CA  . VAL A 473 ? 0.5115 0.6049 0.4981 0.0357  -0.0058 0.1567  482 VAL A CA  
3138  C C   . VAL A 473 ? 0.5215 0.6274 0.5034 0.0400  -0.0057 0.1644  482 VAL A C   
3139  O O   . VAL A 473 ? 0.5274 0.6241 0.5035 0.0430  -0.0036 0.1627  482 VAL A O   
3140  C CB  . VAL A 473 ? 0.5172 0.6059 0.4889 0.0222  -0.0158 0.1486  482 VAL A CB  
3141  C CG1 . VAL A 473 ? 0.5187 0.6053 0.4691 0.0162  -0.0237 0.1463  482 VAL A CG1 
3142  C CG2 . VAL A 473 ? 0.5146 0.6242 0.4931 0.0166  -0.0189 0.1531  482 VAL A CG2 
3143  N N   . PHE A 474 ? 0.5185 0.6489 0.5031 0.0408  -0.0076 0.1736  483 PHE A N   
3144  C CA  . PHE A 474 ? 0.5188 0.6640 0.5012 0.0463  -0.0067 0.1826  483 PHE A CA  
3145  C C   . PHE A 474 ? 0.5277 0.6870 0.4938 0.0369  -0.0159 0.1825  483 PHE A C   
3146  O O   . PHE A 474 ? 0.5347 0.7068 0.4962 0.0269  -0.0229 0.1820  483 PHE A O   
3147  C CB  . PHE A 474 ? 0.5151 0.6781 0.5111 0.0575  -0.0012 0.1947  483 PHE A CB  
3148  C CG  . PHE A 474 ? 0.5158 0.6908 0.5106 0.0650  0.0011  0.2050  483 PHE A CG  
3149  C CD1 . PHE A 474 ? 0.5062 0.6658 0.5045 0.0731  0.0081  0.2088  483 PHE A CD1 
3150  C CD2 . PHE A 474 ? 0.5216 0.7242 0.5102 0.0621  -0.0045 0.2111  483 PHE A CD2 
3151  C CE1 . PHE A 474 ? 0.5104 0.6810 0.5066 0.0792  0.0100  0.2190  483 PHE A CE1 
3152  C CE2 . PHE A 474 ? 0.5260 0.7409 0.5129 0.0692  -0.0025 0.2208  483 PHE A CE2 
3153  C CZ  . PHE A 474 ? 0.5249 0.7234 0.5159 0.0782  0.0049  0.2249  483 PHE A CZ  
3154  N N   . PRO A 475 ? 0.5316 0.6898 0.4880 0.0394  -0.0161 0.1833  484 PRO A N   
3155  C CA  . PRO A 475 ? 0.5454 0.7142 0.4836 0.0320  -0.0246 0.1830  484 PRO A CA  
3156  C C   . PRO A 475 ? 0.5495 0.7513 0.4902 0.0285  -0.0286 0.1935  484 PRO A C   
3157  O O   . PRO A 475 ? 0.5593 0.7752 0.4885 0.0254  -0.0334 0.1968  484 PRO A O   
3158  C CB  . PRO A 475 ? 0.5497 0.7160 0.4841 0.0410  -0.0202 0.1851  484 PRO A CB  
3159  C CG  . PRO A 475 ? 0.5367 0.6972 0.4896 0.0517  -0.0095 0.1903  484 PRO A CG  
3160  C CD  . PRO A 475 ? 0.5301 0.6749 0.4905 0.0487  -0.0085 0.1836  484 PRO A CD  
3161  N N   . SER A 476 ? 0.5451 0.7614 0.4998 0.0291  -0.0268 0.1984  485 SER A N   
3162  C CA  . SER A 476 ? 0.5502 0.8043 0.5111 0.0298  -0.0286 0.2101  485 SER A CA  
3163  C C   . SER A 476 ? 0.5638 0.8363 0.5081 0.0187  -0.0377 0.2124  485 SER A C   
3164  O O   . SER A 476 ? 0.5655 0.8609 0.5126 0.0260  -0.0358 0.2223  485 SER A O   
3165  C CB  . SER A 476 ? 0.5464 0.8155 0.5152 0.0244  -0.0306 0.2108  485 SER A CB  
3166  O OG  . SER A 476 ? 0.5565 0.8687 0.5277 0.0223  -0.0344 0.2219  485 SER A OG  
3167  N N   . ASP A 477 ? 0.5787 0.8391 0.5038 0.0008  -0.0481 0.2033  486 ASP A N   
3168  C CA  . ASP A 477 ? 0.6003 0.8768 0.5064 -0.0133 -0.0587 0.2051  486 ASP A CA  
3169  C C   . ASP A 477 ? 0.6086 0.8824 0.5054 -0.0059 -0.0575 0.2060  486 ASP A C   
3170  O O   . ASP A 477 ? 0.6089 0.9135 0.5054 -0.0057 -0.0593 0.2156  486 ASP A O   
3171  C CB  . ASP A 477 ? 0.6201 0.8730 0.5024 -0.0342 -0.0708 0.1940  486 ASP A CB  
3172  C CG  . ASP A 477 ? 0.6299 0.9056 0.5172 -0.0484 -0.0761 0.1985  486 ASP A CG  
3173  O OD1 . ASP A 477 ? 0.6218 0.9331 0.5321 -0.0389 -0.0694 0.2094  486 ASP A OD1 
3174  O OD2 . ASP A 477 ? 0.6671 0.9257 0.5341 -0.0684 -0.0871 0.1916  486 ASP A OD2 
3175  N N   . GLU A 478 ? 0.6104 0.8509 0.5005 0.0011  -0.0541 0.1966  487 GLU A N   
3176  C CA  . GLU A 478 ? 0.6199 0.8578 0.4999 0.0086  -0.0529 0.1965  487 GLU A CA  
3177  C C   . GLU A 478 ? 0.5963 0.8622 0.4964 0.0233  -0.0436 0.2111  487 GLU A C   
3178  O O   . GLU A 478 ? 0.6029 0.8838 0.4963 0.0264  -0.0444 0.2163  487 GLU A O   
3179  C CB  . GLU A 478 ? 0.6303 0.8327 0.5027 0.0157  -0.0495 0.1849  487 GLU A CB  
3180  C CG  . GLU A 478 ? 0.6809 0.8785 0.5361 0.0221  -0.0503 0.1817  487 GLU A CG  
3181  C CD  . GLU A 478 ? 0.7185 0.9049 0.5836 0.0372  -0.0398 0.1804  487 GLU A CD  
3182  O OE1 . GLU A 478 ? 0.7415 0.9328 0.5977 0.0448  -0.0383 0.1810  487 GLU A OE1 
3183  O OE2 . GLU A 478 ? 0.7152 0.8903 0.5964 0.0408  -0.0333 0.1794  487 GLU A OE2 
3184  N N   . PHE A 479 ? 0.5672 0.8379 0.4897 0.0328  -0.0351 0.2176  488 PHE A N   
3185  C CA  . PHE A 479 ? 0.5503 0.8404 0.4888 0.0476  -0.0267 0.2314  488 PHE A CA  
3186  C C   . PHE A 479 ? 0.5464 0.8761 0.4860 0.0453  -0.0310 0.2423  488 PHE A C   
3187  O O   . PHE A 479 ? 0.5495 0.8984 0.4868 0.0504  -0.0305 0.2507  488 PHE A O   
3188  C CB  . PHE A 479 ? 0.5406 0.8190 0.4977 0.0580  -0.0180 0.2338  488 PHE A CB  
3189  C CG  . PHE A 479 ? 0.5365 0.8249 0.5063 0.0745  -0.0095 0.2476  488 PHE A CG  
3190  C CD1 . PHE A 479 ? 0.5357 0.8037 0.5083 0.0826  -0.0024 0.2494  488 PHE A CD1 
3191  C CD2 . PHE A 479 ? 0.5278 0.8459 0.5054 0.0820  -0.0089 0.2592  488 PHE A CD2 
3192  C CE1 . PHE A 479 ? 0.5350 0.8065 0.5159 0.0964  0.0044  0.2626  488 PHE A CE1 
3193  C CE2 . PHE A 479 ? 0.5297 0.8516 0.5155 0.0988  -0.0017 0.2717  488 PHE A CE2 
3194  C CZ  . PHE A 479 ? 0.5312 0.8271 0.5178 0.1054  0.0047  0.2734  488 PHE A CZ  
3195  N N   . ASP A 480 ? 0.5392 0.8843 0.4824 0.0373  -0.0354 0.2427  489 ASP A N   
3196  C CA  . ASP A 480 ? 0.5418 0.9316 0.4861 0.0330  -0.0404 0.2534  489 ASP A CA  
3197  C C   . ASP A 480 ? 0.5541 0.9583 0.4795 0.0207  -0.0494 0.2536  489 ASP A C   
3198  O O   . ASP A 480 ? 0.5555 1.0000 0.4822 0.0204  -0.0521 0.2648  489 ASP A O   
3199  C CB  . ASP A 480 ? 0.5405 0.9432 0.4863 0.0200  -0.0462 0.2511  489 ASP A CB  
3200  C CG  . ASP A 480 ? 0.5407 0.9432 0.5062 0.0342  -0.0376 0.2540  489 ASP A CG  
3201  O OD1 . ASP A 480 ? 0.5599 0.9461 0.5360 0.0532  -0.0276 0.2569  489 ASP A OD1 
3202  O OD2 . ASP A 480 ? 0.5470 0.9649 0.5157 0.0256  -0.0413 0.2533  489 ASP A OD2 
3203  N N   . ALA A 481 ? 0.5633 0.9347 0.4694 0.0110  -0.0546 0.2408  490 ALA A N   
3204  C CA  . ALA A 481 ? 0.5752 0.9498 0.4584 0.0006  -0.0634 0.2379  490 ALA A CA  
3205  C C   . ALA A 481 ? 0.5702 0.9596 0.4591 0.0162  -0.0567 0.2471  490 ALA A C   
3206  O O   . ALA A 481 ? 0.5764 0.9991 0.4615 0.0137  -0.0605 0.2560  490 ALA A O   
3207  C CB  . ALA A 481 ? 0.5906 0.9208 0.4505 -0.0076 -0.0691 0.2212  490 ALA A CB  
3208  N N   . SER A 482 ? 0.5565 0.9226 0.4544 0.0312  -0.0469 0.2456  491 SER A N   
3209  C CA  . SER A 482 ? 0.5526 0.9293 0.4562 0.0457  -0.0398 0.2551  491 SER A CA  
3210  C C   . SER A 482 ? 0.5456 0.9613 0.4637 0.0544  -0.0366 0.2721  491 SER A C   
3211  O O   . SER A 482 ? 0.5535 0.9929 0.4682 0.0586  -0.0370 0.2809  491 SER A O   
3212  C CB  . SER A 482 ? 0.5415 0.8907 0.4562 0.0585  -0.0295 0.2537  491 SER A CB  
3213  O OG  . SER A 482 ? 0.5549 0.8787 0.4540 0.0553  -0.0316 0.2412  491 SER A OG  
3214  N N   . ILE A 483 ? 0.5321 0.9558 0.4655 0.0586  -0.0335 0.2767  492 ILE A N   
3215  C CA  . ILE A 483 ? 0.5298 0.9889 0.4761 0.0714  -0.0296 0.2928  492 ILE A CA  
3216  C C   . ILE A 483 ? 0.5364 1.0391 0.4755 0.0602  -0.0387 0.2983  492 ILE A C   
3217  O O   . ILE A 483 ? 0.5436 1.0746 0.4822 0.0670  -0.0382 0.3094  492 ILE A O   
3218  C CB  . ILE A 483 ? 0.5208 0.9759 0.4836 0.0828  -0.0231 0.2962  492 ILE A CB  
3219  C CG1 . ILE A 483 ? 0.5239 0.9356 0.4923 0.0928  -0.0145 0.2920  492 ILE A CG1 
3220  C CG2 . ILE A 483 ? 0.5194 1.0130 0.4922 0.0991  -0.0197 0.3129  492 ILE A CG2 
3221  C CD1 . ILE A 483 ? 0.5436 0.9524 0.5242 0.1141  -0.0052 0.3040  492 ILE A CD1 
3222  N N   . SER A 484 ? 0.5376 1.0468 0.4701 0.0419  -0.0473 0.2914  493 SER A N   
3223  C CA  . SER A 484 ? 0.5430 1.0947 0.4663 0.0265  -0.0574 0.2967  493 SER A CA  
3224  C C   . SER A 484 ? 0.5583 1.1119 0.4648 0.0215  -0.0620 0.2960  493 SER A C   
3225  O O   . SER A 484 ? 0.5732 1.1647 0.4719 0.0121  -0.0692 0.3029  493 SER A O   
3226  C CB  . SER A 484 ? 0.5458 1.0920 0.4575 0.0021  -0.0679 0.2869  493 SER A CB  
3227  O OG  . SER A 484 ? 0.5501 1.1399 0.4523 -0.0149 -0.0782 0.2936  493 SER A OG  
3228  N N   . GLN A 485 ? 0.5558 1.0713 0.4573 0.0288  -0.0574 0.2885  494 GLN A N   
3229  C CA  . GLN A 485 ? 0.5678 1.0821 0.4532 0.0273  -0.0605 0.2870  494 GLN A CA  
3230  C C   . GLN A 485 ? 0.5549 1.0845 0.4524 0.0482  -0.0507 0.3005  494 GLN A C   
3231  O O   . GLN A 485 ? 0.5632 1.1109 0.4506 0.0475  -0.0537 0.3045  494 GLN A O   
3232  C CB  . GLN A 485 ? 0.5804 1.0469 0.4479 0.0206  -0.0633 0.2694  494 GLN A CB  
3233  C CG  . GLN A 485 ? 0.6297 1.0921 0.4689 0.0092  -0.0731 0.2616  494 GLN A CG  
3234  C CD  . GLN A 485 ? 0.6697 1.1238 0.5067 0.0243  -0.0665 0.2621  494 GLN A CD  
3235  O OE1 . GLN A 485 ? 0.6607 1.0930 0.5095 0.0376  -0.0569 0.2609  494 GLN A OE1 
3236  N NE2 . GLN A 485 ? 0.7022 1.1760 0.5236 0.0215  -0.0718 0.2646  494 GLN A NE2 
3237  N N   . VAL A 486 ? 0.5370 1.0576 0.4540 0.0661  -0.0398 0.3076  495 VAL A N   
3238  C CA  . VAL A 486 ? 0.5296 1.0658 0.4564 0.0850  -0.0318 0.3230  495 VAL A CA  
3239  C C   . VAL A 486 ? 0.5338 1.1210 0.4632 0.0863  -0.0355 0.3362  495 VAL A C   
3240  O O   . VAL A 486 ? 0.5397 1.1510 0.4673 0.0935  -0.0346 0.3470  495 VAL A O   
3241  C CB  . VAL A 486 ? 0.5213 1.0337 0.4646 0.1029  -0.0206 0.3286  495 VAL A CB  
3242  C CG1 . VAL A 486 ? 0.5172 1.0540 0.4701 0.1223  -0.0147 0.3475  495 VAL A CG1 
3243  C CG2 . VAL A 486 ? 0.5132 0.9871 0.4537 0.1046  -0.0157 0.3219  495 VAL A CG2 
3244  N N   . ASN A 487 ? 0.5312 1.1380 0.4641 0.0782  -0.0402 0.3355  496 ASN A N   
3245  C CA  . ASN A 487 ? 0.5403 1.2022 0.4762 0.0786  -0.0441 0.3484  496 ASN A CA  
3246  C C   . ASN A 487 ? 0.5531 1.2403 0.4711 0.0597  -0.0549 0.3469  496 ASN A C   
3247  O O   . ASN A 487 ? 0.5561 1.2894 0.4751 0.0630  -0.0568 0.3597  496 ASN A O   
3248  C CB  . ASN A 487 ? 0.5345 1.2149 0.4796 0.0753  -0.0458 0.3491  496 ASN A CB  
3249  C CG  . ASN A 487 ? 0.5385 1.1936 0.4995 0.0963  -0.0351 0.3507  496 ASN A CG  
3250  O OD1 . ASN A 487 ? 0.5459 1.1963 0.5144 0.1192  -0.0264 0.3610  496 ASN A OD1 
3251  N ND2 . ASN A 487 ? 0.5517 1.1879 0.5156 0.0879  -0.0363 0.3406  496 ASN A ND2 
3252  N N   . GLU A 488 ? 0.5652 1.2207 0.4648 0.0409  -0.0622 0.3310  497 GLU A N   
3253  C CA  . GLU A 488 ? 0.5815 1.2477 0.4594 0.0263  -0.0716 0.3277  497 GLU A CA  
3254  C C   . GLU A 488 ? 0.5830 1.2713 0.4669 0.0444  -0.0650 0.3409  497 GLU A C   
3255  O O   . GLU A 488 ? 0.5905 1.3228 0.4715 0.0416  -0.0694 0.3511  497 GLU A O   
3256  C CB  . GLU A 488 ? 0.5934 1.2090 0.4503 0.0160  -0.0759 0.3090  497 GLU A CB  
3257  C CG  . GLU A 488 ? 0.5974 1.1894 0.4387 -0.0064 -0.0861 0.2949  497 GLU A CG  
3258  C CD  . GLU A 488 ? 0.5989 1.2325 0.4343 -0.0262 -0.0968 0.3010  497 GLU A CD  
3259  O OE1 . GLU A 488 ? 0.5864 1.2680 0.4280 -0.0221 -0.0967 0.3151  497 GLU A OE1 
3260  O OE2 . GLU A 488 ? 0.6080 1.2277 0.4325 -0.0461 -0.1054 0.2926  497 GLU A OE2 
3261  N N   . LYS A 489 ? 0.5809 1.2394 0.4733 0.0622  -0.0546 0.3417  498 LYS A N   
3262  C CA  . LYS A 489 ? 0.5903 1.2600 0.4838 0.0767  -0.0491 0.3522  498 LYS A CA  
3263  C C   . LYS A 489 ? 0.5888 1.3000 0.4972 0.0933  -0.0441 0.3722  498 LYS A C   
3264  O O   . LYS A 489 ? 0.5985 1.3417 0.5026 0.0966  -0.0456 0.3821  498 LYS A O   
3265  C CB  . LYS A 489 ? 0.5879 1.2159 0.4862 0.0891  -0.0396 0.3491  498 LYS A CB  
3266  C CG  . LYS A 489 ? 0.6020 1.1884 0.4879 0.0775  -0.0428 0.3298  498 LYS A CG  
3267  C CD  . LYS A 489 ? 0.6409 1.2275 0.5046 0.0691  -0.0494 0.3219  498 LYS A CD  
3268  C CE  . LYS A 489 ? 0.6690 1.2138 0.5167 0.0591  -0.0536 0.3019  498 LYS A CE  
3269  N NZ  . LYS A 489 ? 0.7171 1.2606 0.5387 0.0529  -0.0609 0.2931  498 LYS A NZ  
3270  N N   . ILE A 490 ? 0.5838 1.2945 0.5083 0.1055  -0.0382 0.3783  499 ILE A N   
3271  C CA  . ILE A 490 ? 0.5925 1.3420 0.5283 0.1246  -0.0337 0.3973  499 ILE A CA  
3272  C C   . ILE A 490 ? 0.6084 1.4153 0.5389 0.1121  -0.0432 0.4024  499 ILE A C   
3273  O O   . ILE A 490 ? 0.6137 1.4560 0.5417 0.1181  -0.0440 0.4144  499 ILE A O   
3274  C CB  . ILE A 490 ? 0.5842 1.3226 0.5348 0.1414  -0.0265 0.4016  499 ILE A CB  
3275  C CG1 . ILE A 490 ? 0.5714 1.2503 0.5249 0.1477  -0.0190 0.3941  499 ILE A CG1 
3276  C CG2 . ILE A 490 ? 0.5879 1.3618 0.5464 0.1662  -0.0214 0.4217  499 ILE A CG2 
3277  C CD1 . ILE A 490 ? 0.5529 1.2093 0.5162 0.1537  -0.0151 0.3894  499 ILE A CD1 
3278  N N   . ASN A 491 ? 0.6216 1.4374 0.5492 0.0932  -0.0509 0.3937  500 ASN A N   
3279  C CA  . ASN A 491 ? 0.6479 1.5159 0.5674 0.0743  -0.0620 0.3970  500 ASN A CA  
3280  C C   . ASN A 491 ? 0.6473 1.5303 0.5501 0.0633  -0.0686 0.3972  500 ASN A C   
3281  O O   . ASN A 491 ? 0.6505 1.5877 0.5515 0.0605  -0.0734 0.4088  500 ASN A O   
3282  C CB  . ASN A 491 ? 0.6655 1.5237 0.5777 0.0484  -0.0711 0.3836  500 ASN A CB  
3283  C CG  . ASN A 491 ? 0.7588 1.6580 0.6856 0.0522  -0.0706 0.3926  500 ASN A CG  
3284  O OD1 . ASN A 491 ? 0.7646 1.6902 0.7071 0.0784  -0.0620 0.4070  500 ASN A OD1 
3285  N ND2 . ASN A 491 ? 0.9409 1.8463 0.8609 0.0266  -0.0801 0.3848  500 ASN A ND2 
3286  N N   . GLN A 492 ? 0.6427 1.4791 0.5331 0.0585  -0.0686 0.3846  501 GLN A N   
3287  C CA  . GLN A 492 ? 0.6519 1.4929 0.5239 0.0500  -0.0742 0.3819  501 GLN A CA  
3288  C C   . GLN A 492 ? 0.6410 1.5092 0.5226 0.0726  -0.0663 0.3993  501 GLN A C   
3289  O O   . GLN A 492 ? 0.6464 1.5546 0.5199 0.0685  -0.0714 0.4069  501 GLN A O   
3290  C CB  . GLN A 492 ? 0.6619 1.4441 0.5210 0.0459  -0.0736 0.3644  501 GLN A CB  
3291  C CG  . GLN A 492 ? 0.7072 1.4799 0.5387 0.0305  -0.0831 0.3530  501 GLN A CG  
3292  C CD  . GLN A 492 ? 0.7509 1.4648 0.5665 0.0219  -0.0857 0.3321  501 GLN A CD  
3293  O OE1 . GLN A 492 ? 0.7469 1.4264 0.5729 0.0360  -0.0761 0.3287  501 GLN A OE1 
3294  N NE2 . GLN A 492 ? 0.7888 1.4906 0.5774 -0.0015 -0.0992 0.3184  501 GLN A NE2 
3295  N N   . SER A 493 ? 0.6213 1.4651 0.5186 0.0957  -0.0542 0.4056  502 SER A N   
3296  C CA  . SER A 493 ? 0.6134 1.4689 0.5184 0.1184  -0.0457 0.4218  502 SER A CA  
3297  C C   . SER A 493 ? 0.6113 1.5265 0.5238 0.1286  -0.0464 0.4401  502 SER A C   
3298  O O   . SER A 493 ? 0.6173 1.5668 0.5248 0.1319  -0.0480 0.4505  502 SER A O   
3299  C CB  . SER A 493 ? 0.6057 1.4182 0.5236 0.1375  -0.0342 0.4243  502 SER A CB  
3300  O OG  . SER A 493 ? 0.6080 1.4199 0.5283 0.1556  -0.0270 0.4382  502 SER A OG  
3301  N N   . LEU A 494 ? 0.5977 1.5281 0.5217 0.1343  -0.0452 0.4441  503 LEU A N   
3302  C CA  . LEU A 494 ? 0.5955 1.5861 0.5270 0.1463  -0.0455 0.4614  503 LEU A CA  
3303  C C   . LEU A 494 ? 0.6008 1.6438 0.5210 0.1270  -0.0563 0.4637  503 LEU A C   
3304  O O   . LEU A 494 ? 0.6066 1.6946 0.5285 0.1391  -0.0554 0.4796  503 LEU A O   
3305  C CB  . LEU A 494 ? 0.5858 1.5881 0.5279 0.1486  -0.0453 0.4609  503 LEU A CB  
3306  C CG  . LEU A 494 ? 0.5846 1.5428 0.5377 0.1717  -0.0345 0.4614  503 LEU A CG  
3307  C CD1 . LEU A 494 ? 0.5859 1.5650 0.5476 0.1718  -0.0358 0.4604  503 LEU A CD1 
3308  C CD2 . LEU A 494 ? 0.5975 1.5583 0.5551 0.2039  -0.0254 0.4793  503 LEU A CD2 
3309  N N   . ALA A 495 ? 0.6021 1.6363 0.5086 0.0965  -0.0669 0.4478  504 ALA A N   
3310  C CA  . ALA A 495 ? 0.6081 1.6842 0.4989 0.0726  -0.0792 0.4473  504 ALA A CA  
3311  C C   . ALA A 495 ? 0.6150 1.6921 0.4950 0.0762  -0.0791 0.4501  504 ALA A C   
3312  O O   . ALA A 495 ? 0.6238 1.7517 0.4972 0.0699  -0.0852 0.4590  504 ALA A O   
3313  C CB  . ALA A 495 ? 0.6149 1.6656 0.4883 0.0395  -0.0909 0.4281  504 ALA A CB  
3314  N N   . PHE A 496 ? 0.6081 1.6328 0.4861 0.0860  -0.0723 0.4430  505 PHE A N   
3315  C CA  . PHE A 496 ? 0.6131 1.6425 0.4828 0.0923  -0.0708 0.4477  505 PHE A CA  
3316  C C   . PHE A 496 ? 0.6086 1.6827 0.4918 0.1169  -0.0639 0.4710  505 PHE A C   
3317  O O   . PHE A 496 ? 0.6175 1.7329 0.4934 0.1145  -0.0681 0.4792  505 PHE A O   
3318  C CB  . PHE A 496 ? 0.6165 1.5870 0.4831 0.0991  -0.0641 0.4378  505 PHE A CB  
3319  C CG  . PHE A 496 ? 0.6388 1.5763 0.4826 0.0770  -0.0727 0.4164  505 PHE A CG  
3320  C CD1 . PHE A 496 ? 0.6564 1.5431 0.4975 0.0695  -0.0727 0.3997  505 PHE A CD1 
3321  C CD2 . PHE A 496 ? 0.6595 1.6149 0.4827 0.0654  -0.0808 0.4128  505 PHE A CD2 
3322  C CE1 . PHE A 496 ? 0.6729 1.5264 0.4900 0.0523  -0.0808 0.3799  505 PHE A CE1 
3323  C CE2 . PHE A 496 ? 0.6754 1.5962 0.4734 0.0480  -0.0891 0.3924  505 PHE A CE2 
3324  C CZ  . PHE A 496 ? 0.6777 1.5471 0.4721 0.0422  -0.0891 0.3761  505 PHE A CZ  
3325  N N   . ILE A 497 ? 0.6001 1.6653 0.5008 0.1408  -0.0539 0.4815  506 ILE A N   
3326  C CA  . ILE A 497 ? 0.6057 1.7076 0.5165 0.1677  -0.0472 0.5040  506 ILE A CA  
3327  C C   . ILE A 497 ? 0.6151 1.7907 0.5267 0.1637  -0.0541 0.5150  506 ILE A C   
3328  O O   . ILE A 497 ? 0.6212 1.8392 0.5302 0.1713  -0.0548 0.5288  506 ILE A O   
3329  C CB  . ILE A 497 ? 0.6015 1.6738 0.5263 0.1943  -0.0364 0.5116  506 ILE A CB  
3330  C CG1 . ILE A 497 ? 0.6026 1.6081 0.5261 0.1983  -0.0294 0.5043  506 ILE A CG1 
3331  C CG2 . ILE A 497 ? 0.6044 1.7130 0.5356 0.2241  -0.0305 0.5350  506 ILE A CG2 
3332  C CD1 . ILE A 497 ? 0.6138 1.6172 0.5318 0.2075  -0.0258 0.5146  506 ILE A CD1 
3333  N N   . ARG A 498 ? 0.6170 1.8101 0.5325 0.1515  -0.0592 0.5097  507 ARG A N   
3334  C CA  . ARG A 498 ? 0.6260 1.8917 0.5410 0.1396  -0.0679 0.5176  507 ARG A CA  
3335  C C   . ARG A 498 ? 0.6342 1.9359 0.5346 0.1236  -0.0762 0.5201  507 ARG A C   
3336  O O   . ARG A 498 ? 0.6324 1.9961 0.5357 0.1329  -0.0772 0.5369  507 ARG A O   
3337  C CB  . ARG A 498 ? 0.6264 1.8878 0.5374 0.1107  -0.0768 0.5027  507 ARG A CB  
3338  C CG  . ARG A 498 ? 0.6529 1.8986 0.5784 0.1209  -0.0714 0.5007  507 ARG A CG  
3339  C CD  . ARG A 498 ? 0.7031 1.9884 0.6245 0.0912  -0.0831 0.4961  507 ARG A CD  
3340  N NE  . ARG A 498 ? 0.7736 2.1273 0.6872 0.0790  -0.0917 0.5072  507 ARG A NE  
3341  C CZ  . ARG A 498 ? 0.8001 2.2006 0.7040 0.0473  -0.1049 0.5064  507 ARG A CZ  
3342  N NH1 . ARG A 498 ? 0.8038 2.1902 0.7041 0.0230  -0.1116 0.4951  507 ARG A NH1 
3343  N NH2 . ARG A 498 ? 0.8021 2.2643 0.6990 0.0389  -0.1117 0.5177  507 ARG A NH2 
3344  N N   . LYS A 499 ? 0.6413 1.9022 0.5247 0.1011  -0.0822 0.5027  508 LYS A N   
3345  C CA  . LYS A 499 ? 0.6557 1.9376 0.5204 0.0834  -0.0911 0.5003  508 LYS A CA  
3346  C C   . LYS A 499 ? 0.6563 1.9526 0.5248 0.1080  -0.0833 0.5155  508 LYS A C   
3347  O O   . LYS A 499 ? 0.6646 2.0137 0.5268 0.1046  -0.0883 0.5255  508 LYS A O   
3348  C CB  . LYS A 499 ? 0.6658 1.8885 0.5094 0.0594  -0.0978 0.4764  508 LYS A CB  
3349  C CG  . LYS A 499 ? 0.7063 1.9424 0.5243 0.0386  -0.1089 0.4697  508 LYS A CG  
3350  C CD  . LYS A 499 ? 0.7531 2.0154 0.5516 0.0022  -0.1257 0.4616  508 LYS A CD  
3351  C CE  . LYS A 499 ? 0.7601 2.1095 0.5653 -0.0026 -0.1310 0.4809  508 LYS A CE  
3352  N NZ  . LYS A 499 ? 0.7517 2.1474 0.5511 0.0033  -0.1323 0.4930  508 LYS A NZ  
3353  N N   . SER A 500 ? 0.6488 1.8980 0.5264 0.1312  -0.0715 0.5174  509 SER A N   
3354  C CA  . SER A 500 ? 0.6530 1.9076 0.5339 0.1548  -0.0635 0.5326  509 SER A CA  
3355  C C   . SER A 500 ? 0.6592 1.9756 0.5510 0.1761  -0.0607 0.5559  509 SER A C   
3356  O O   . SER A 500 ? 0.6650 2.0230 0.5522 0.1808  -0.0622 0.5680  509 SER A O   
3357  C CB  . SER A 500 ? 0.6475 1.8393 0.5361 0.1736  -0.0520 0.5316  509 SER A CB  
3358  O OG  . SER A 500 ? 0.6484 1.8426 0.5382 0.1942  -0.0449 0.5472  509 SER A OG  
3359  N N   . ASP A 501 ? 0.6606 1.9849 0.5657 0.1899  -0.0567 0.5618  510 ASP A N   
3360  C CA  . ASP A 501 ? 0.6715 2.0536 0.5863 0.2149  -0.0533 0.5839  510 ASP A CA  
3361  C C   . ASP A 501 ? 0.6754 2.1370 0.5852 0.1993  -0.0635 0.5909  510 ASP A C   
3362  O O   . ASP A 501 ? 0.6848 2.1932 0.5960 0.2170  -0.0615 0.6091  510 ASP A O   
3363  C CB  . ASP A 501 ? 0.6699 2.0460 0.5975 0.2318  -0.0481 0.5864  510 ASP A CB  
3364  C CG  . ASP A 501 ? 0.6869 1.9994 0.6197 0.2604  -0.0361 0.5899  510 ASP A CG  
3365  O OD1 . ASP A 501 ? 0.7134 2.0233 0.6448 0.2851  -0.0297 0.6056  510 ASP A OD1 
3366  O OD2 . ASP A 501 ? 0.6892 1.9532 0.6259 0.2572  -0.0335 0.5773  510 ASP A OD2 
3367  N N   . GLU A 502 ? 0.6759 2.1516 0.5782 0.1654  -0.0747 0.5768  511 GLU A N   
3368  C CA  . GLU A 502 ? 0.6869 2.2362 0.5815 0.1444  -0.0861 0.5822  511 GLU A CA  
3369  C C   . GLU A 502 ? 0.6951 2.2616 0.5796 0.1462  -0.0873 0.5890  511 GLU A C   
3370  O O   . GLU A 502 ? 0.7025 2.3366 0.5893 0.1559  -0.0885 0.6068  511 GLU A O   
3371  C CB  . GLU A 502 ? 0.6921 2.2335 0.5725 0.1019  -0.0996 0.5628  511 GLU A CB  
3372  C CG  . GLU A 502 ? 0.7170 2.2838 0.6066 0.0927  -0.1029 0.5625  511 GLU A CG  
3373  C CD  . GLU A 502 ? 0.7572 2.2918 0.6308 0.0513  -0.1152 0.5409  511 GLU A CD  
3374  O OE1 . GLU A 502 ? 0.7872 2.3300 0.6395 0.0215  -0.1274 0.5332  511 GLU A OE1 
3375  O OE2 . GLU A 502 ? 0.7392 2.2392 0.6195 0.0490  -0.1131 0.5318  511 GLU A OE2 
3376  N N   . LEU A 503 ? 0.6944 2.2020 0.5678 0.1387  -0.0866 0.5753  512 LEU A N   
3377  C CA  . LEU A 503 ? 0.7029 2.2244 0.5654 0.1395  -0.0878 0.5802  512 LEU A CA  
3378  C C   . LEU A 503 ? 0.7042 2.2569 0.5785 0.1750  -0.0780 0.6047  512 LEU A C   
3379  O O   . LEU A 503 ? 0.7158 2.3183 0.5847 0.1762  -0.0811 0.6162  512 LEU A O   
3380  C CB  . LEU A 503 ? 0.7061 2.1586 0.5559 0.1308  -0.0869 0.5624  512 LEU A CB  
3381  C CG  . LEU A 503 ? 0.7167 2.1442 0.5471 0.0942  -0.0993 0.5383  512 LEU A CG  
3382  C CD1 . LEU A 503 ? 0.7211 2.0739 0.5401 0.0902  -0.0969 0.5192  512 LEU A CD1 
3383  C CD2 . LEU A 503 ? 0.7312 2.2128 0.5430 0.0697  -0.1129 0.5384  512 LEU A CD2 
3384  N N   . LEU A 504 ? 0.6996 2.2231 0.5882 0.2038  -0.0667 0.6129  513 LEU A N   
3385  C CA  . LEU A 504 ? 0.7098 2.2478 0.6056 0.2397  -0.0571 0.6357  513 LEU A CA  
3386  C C   . LEU A 504 ? 0.7194 2.3335 0.6233 0.2577  -0.0576 0.6557  513 LEU A C   
3387  O O   . LEU A 504 ? 0.7276 2.3776 0.6315 0.2795  -0.0542 0.6751  513 LEU A O   
3388  C CB  . LEU A 504 ? 0.7085 2.1769 0.6114 0.2631  -0.0457 0.6363  513 LEU A CB  
3389  C CG  . LEU A 504 ? 0.6968 2.0961 0.5925 0.2491  -0.0441 0.6199  513 LEU A CG  
3390  C CD1 . LEU A 504 ? 0.7023 2.0371 0.6053 0.2584  -0.0368 0.6126  513 LEU A CD1 
3391  C CD2 . LEU A 504 ? 0.6937 2.0875 0.5839 0.2621  -0.0394 0.6321  513 LEU A CD2 
3392  N N   . HIS A 505 ? 0.7199 2.3610 0.6302 0.2493  -0.0616 0.6517  514 HIS A N   
3393  C CA  . HIS A 505 ? 0.7354 2.4592 0.6528 0.2632  -0.0632 0.6698  514 HIS A CA  
3394  C C   . HIS A 505 ? 0.7447 2.5373 0.6530 0.2364  -0.0749 0.6720  514 HIS A C   
3395  O O   . HIS A 505 ? 0.7475 2.6213 0.6598 0.2375  -0.0794 0.6852  514 HIS A O   
3396  C CB  . HIS A 505 ? 0.7262 2.4599 0.6534 0.2625  -0.0637 0.6654  514 HIS A CB  
3397  C CG  . HIS A 505 ? 0.7411 2.4081 0.6755 0.2897  -0.0526 0.6634  514 HIS A CG  
3398  N ND1 . HIS A 505 ? 0.7624 2.4040 0.6980 0.3291  -0.0420 0.6784  514 HIS A ND1 
3399  C CD2 . HIS A 505 ? 0.7405 2.3592 0.6794 0.2824  -0.0512 0.6483  514 HIS A CD2 
3400  C CE1 . HIS A 505 ? 0.7643 2.3440 0.7038 0.3440  -0.0348 0.6722  514 HIS A CE1 
3401  N NE2 . HIS A 505 ? 0.7494 2.3158 0.6920 0.3167  -0.0398 0.6539  514 HIS A NE2 
3402  N N   . ASN A 506 ? 0.7567 2.5162 0.6515 0.2128  -0.0797 0.6588  515 ASN A N   
3403  C CA  . ASN A 506 ? 0.7732 2.5841 0.6552 0.1897  -0.0901 0.6600  515 ASN A CA  
3404  C C   . ASN A 506 ? 0.7859 2.5934 0.6632 0.2079  -0.0848 0.6709  515 ASN A C   
3405  O O   . ASN A 506 ? 0.7944 2.6241 0.6579 0.1881  -0.0925 0.6675  515 ASN A O   
3406  C CB  . ASN A 506 ? 0.7753 2.5555 0.6404 0.1459  -0.1020 0.6350  515 ASN A CB  
3407  C CG  . ASN A 506 ? 0.7851 2.6324 0.6432 0.1143  -0.1160 0.6344  515 ASN A CG  
3408  O OD1 . ASN A 506 ? 0.7837 2.6271 0.6435 0.0964  -0.1209 0.6255  515 ASN A OD1 
3409  N ND2 . ASN A 506 ? 0.7889 2.7008 0.6386 0.1063  -0.1228 0.6450  515 ASN A ND2 
3410  N N   . VAL A 507 ? 0.7923 2.5708 0.6792 0.2453  -0.0721 0.6842  516 VAL A N   
3411  C CA  . VAL A 507 ? 0.8044 2.5737 0.6873 0.2652  -0.0659 0.6969  516 VAL A CA  
3412  C C   . VAL A 507 ? 0.8177 2.6259 0.7094 0.3068  -0.0577 0.7246  516 VAL A C   
3413  O O   . VAL A 507 ? 0.8224 2.6066 0.7228 0.3326  -0.0501 0.7306  516 VAL A O   
3414  C CB  . VAL A 507 ? 0.8025 2.4816 0.6822 0.2665  -0.0591 0.6847  516 VAL A CB  
3415  C CG1 . VAL A 507 ? 0.8122 2.4787 0.6901 0.2923  -0.0508 0.7019  516 VAL A CG1 
3416  C CG2 . VAL A 507 ? 0.7890 2.4404 0.6553 0.2295  -0.0677 0.6601  516 VAL A CG2 
3417  N N   . ASN A 508 ? 0.8232 2.6894 0.7107 0.3144  -0.0596 0.7410  517 ASN A N   
3418  C CA  . ASN A 508 ? 0.8347 2.7509 0.7282 0.3525  -0.0539 0.7676  517 ASN A CA  
3419  C C   . ASN A 508 ? 0.8410 2.8074 0.7276 0.3587  -0.0555 0.7840  517 ASN A C   
3420  O O   . ASN A 508 ? 0.8388 2.7750 0.7166 0.3468  -0.0560 0.7785  517 ASN A O   
3421  C CB  . ASN A 508 ? 0.8300 2.8129 0.7324 0.3534  -0.0581 0.7717  517 ASN A CB  
3422  C CG  . ASN A 508 ? 0.8527 2.8750 0.7615 0.4007  -0.0503 0.7973  517 ASN A CG  
3423  O OD1 . ASN A 508 ? 0.8848 2.9114 0.7892 0.4294  -0.0448 0.8159  517 ASN A OD1 
3424  N ND2 . ASN A 508 ? 0.8434 2.8965 0.7609 0.4091  -0.0504 0.7983  517 ASN A ND2 
3425  N N   . GLN B 26  ? 1.6147 1.1059 1.2536 0.5344  -0.0779 -0.6344 26  GLN B N   
3426  C CA  . GLN B 26  ? 1.5309 1.0865 1.2133 0.4923  -0.0571 -0.6125 26  GLN B CA  
3427  C C   . GLN B 26  ? 1.5021 1.1300 1.1959 0.4995  -0.0467 -0.6258 26  GLN B C   
3428  O O   . GLN B 26  ? 1.4781 1.1845 1.1888 0.5248  -0.0358 -0.6316 26  GLN B O   
3429  C CB  . GLN B 26  ? 1.4657 1.0733 1.1860 0.4819  -0.0410 -0.5882 26  GLN B CB  
3430  C CG  . GLN B 26  ? 1.4540 1.0093 1.1811 0.4450  -0.0427 -0.5631 26  GLN B CG  
3431  C CD  . GLN B 26  ? 1.5210 0.9771 1.2095 0.4555  -0.0645 -0.5679 26  GLN B CD  
3432  O OE1 . GLN B 26  ? 1.5899 0.9914 1.2387 0.4804  -0.0824 -0.5906 26  GLN B OE1 
3433  N NE2 . GLN B 26  ? 1.4993 0.9300 1.1981 0.4352  -0.0636 -0.5459 26  GLN B NE2 
3434  N N   . ASN B 27  ? 1.5035 1.1070 1.1876 0.4763  -0.0506 -0.6302 27  ASN B N   
3435  C CA  . ASN B 27  ? 1.4825 1.1406 1.1678 0.4885  -0.0452 -0.6475 27  ASN B CA  
3436  C C   . ASN B 27  ? 1.3954 1.1058 1.1143 0.4476  -0.0286 -0.6302 27  ASN B C   
3437  O O   . ASN B 27  ? 1.4079 1.1000 1.1158 0.4313  -0.0327 -0.6373 27  ASN B O   
3438  C CB  . ASN B 27  ? 1.5745 1.1648 1.2126 0.5084  -0.0660 -0.6753 27  ASN B CB  
3439  C CG  . ASN B 27  ? 1.6115 1.2616 1.2456 0.5365  -0.0624 -0.6988 27  ASN B CG  
3440  O OD1 . ASN B 27  ? 1.6212 1.3315 1.2616 0.5728  -0.0565 -0.7089 27  ASN B OD1 
3441  N ND2 . ASN B 27  ? 1.6767 1.3130 1.2996 0.5197  -0.0660 -0.7074 27  ASN B ND2 
3442  N N   . ILE B 28  ? 1.2985 1.0723 1.0567 0.4316  -0.0107 -0.6077 28  ILE B N   
3443  C CA  . ILE B 28  ? 1.2071 1.0376 0.9979 0.3966  0.0057  -0.5910 28  ILE B CA  
3444  C C   . ILE B 28  ? 1.1656 1.0845 0.9704 0.4139  0.0171  -0.6011 28  ILE B C   
3445  O O   . ILE B 28  ? 1.1600 1.1242 0.9674 0.4463  0.0199  -0.6093 28  ILE B O   
3446  C CB  . ILE B 28  ? 1.1446 0.9950 0.9679 0.3675  0.0182  -0.5611 28  ILE B CB  
3447  C CG1 . ILE B 28  ? 1.1548 1.0191 0.9836 0.3922  0.0196  -0.5575 28  ILE B CG1 
3448  C CG2 . ILE B 28  ? 1.1405 0.9196 0.9570 0.3334  0.0112  -0.5469 28  ILE B CG2 
3449  C CD1 . ILE B 28  ? 1.1277 1.0875 0.9792 0.4114  0.0333  -0.5584 28  ILE B CD1 
3450  N N   . THR B 29  ? 1.1300 1.0747 0.9433 0.3920  0.0231  -0.6001 29  THR B N   
3451  C CA  . THR B 29  ? 1.0964 1.1211 0.9201 0.4050  0.0325  -0.6101 29  THR B CA  
3452  C C   . THR B 29  ? 1.0380 1.0984 0.8871 0.3660  0.0449  -0.5924 29  THR B C   
3453  O O   . THR B 29  ? 1.0287 1.0441 0.8801 0.3335  0.0433  -0.5784 29  THR B O   
3454  C CB  . THR B 29  ? 1.1530 1.1570 0.9438 0.4316  0.0201  -0.6405 29  THR B CB  
3455  O OG1 . THR B 29  ? 1.2208 1.1303 0.9756 0.4446  0.0007  -0.6532 29  THR B OG1 
3456  C CG2 . THR B 29  ? 1.1548 1.2315 0.9458 0.4712  0.0243  -0.6574 29  THR B CG2 
3457  N N   . GLU B 30  ? 0.9951 1.1388 0.8623 0.3698  0.0569  -0.5925 30  GLU B N   
3458  C CA  . GLU B 30  ? 0.9490 1.1307 0.8351 0.3387  0.0672  -0.5806 30  GLU B CA  
3459  C C   . GLU B 30  ? 0.9576 1.1838 0.8337 0.3579  0.0670  -0.6021 30  GLU B C   
3460  O O   . GLU B 30  ? 0.9710 1.2398 0.8421 0.3910  0.0671  -0.6165 30  GLU B O   
3461  C CB  . GLU B 30  ? 0.8863 1.1311 0.8062 0.3205  0.0827  -0.5556 30  GLU B CB  
3462  C CG  . GLU B 30  ? 0.8625 1.1050 0.8003 0.2797  0.0900  -0.5338 30  GLU B CG  
3463  C CD  . GLU B 30  ? 0.8435 1.1149 0.8073 0.2628  0.1005  -0.5079 30  GLU B CD  
3464  O OE1 . GLU B 30  ? 0.8291 1.1627 0.8054 0.2749  0.1077  -0.5050 30  GLU B OE1 
3465  O OE2 . GLU B 30  ? 0.8475 1.0802 0.8185 0.2373  0.1010  -0.4905 30  GLU B OE2 
3466  N N   . GLU B 31  ? 0.9530 1.1702 0.8249 0.3382  0.0662  -0.6048 31  GLU B N   
3467  C CA  . GLU B 31  ? 0.9576 1.2233 0.8234 0.3513  0.0677  -0.6223 31  GLU B CA  
3468  C C   . GLU B 31  ? 0.8974 1.2142 0.7892 0.3171  0.0809  -0.6033 31  GLU B C   
3469  O O   . GLU B 31  ? 0.8826 1.1652 0.7816 0.2845  0.0819  -0.5875 31  GLU B O   
3470  C CB  . GLU B 31  ? 1.0217 1.2231 0.8526 0.3627  0.0519  -0.6469 31  GLU B CB  
3471  C CG  . GLU B 31  ? 1.0482 1.2851 0.8762 0.3572  0.0542  -0.6577 31  GLU B CG  
3472  C CD  . GLU B 31  ? 1.1554 1.3441 0.9447 0.3815  0.0379  -0.6887 31  GLU B CD  
3473  O OE1 . GLU B 31  ? 1.1618 1.3845 0.9456 0.3845  0.0390  -0.7019 31  GLU B OE1 
3474  O OE2 . GLU B 31  ? 1.2310 1.3460 0.9935 0.3976  0.0233  -0.6999 31  GLU B OE2 
3475  N N   . PHE B 32  ? 0.8635 1.2636 0.7689 0.3248  0.0907  -0.6041 32  PHE B N   
3476  C CA  . PHE B 32  ? 0.8061 1.2595 0.7358 0.2942  0.1032  -0.5845 32  PHE B CA  
3477  C C   . PHE B 32  ? 0.8195 1.2874 0.7392 0.2914  0.1016  -0.5986 32  PHE B C   
3478  O O   . PHE B 32  ? 0.8567 1.3375 0.7580 0.3197  0.0960  -0.6230 32  PHE B O   
3479  C CB  . PHE B 32  ? 0.7653 1.3020 0.7159 0.3002  0.1144  -0.5735 32  PHE B CB  
3480  C CG  . PHE B 32  ? 0.7171 1.3191 0.6869 0.2761  0.1254  -0.5586 32  PHE B CG  
3481  C CD1 . PHE B 32  ? 0.6856 1.2748 0.6709 0.2400  0.1308  -0.5349 32  PHE B CD1 
3482  C CD2 . PHE B 32  ? 0.7225 1.4008 0.6938 0.2904  0.1300  -0.5679 32  PHE B CD2 
3483  C CE1 . PHE B 32  ? 0.6526 1.2997 0.6531 0.2187  0.1399  -0.5209 32  PHE B CE1 
3484  C CE2 . PHE B 32  ? 0.6891 1.4279 0.6767 0.2670  0.1394  -0.5530 32  PHE B CE2 
3485  C CZ  . PHE B 32  ? 0.6493 1.3702 0.6507 0.2315  0.1439  -0.5296 32  PHE B CZ  
3486  N N   . TYR B 33  ? 0.7944 1.2603 0.7253 0.2581  0.1063  -0.5836 33  TYR B N   
3487  C CA  . TYR B 33  ? 0.8065 1.2869 0.7293 0.2523  0.1052  -0.5949 33  TYR B CA  
3488  C C   . TYR B 33  ? 0.7579 1.3167 0.7037 0.2344  0.1183  -0.5788 33  TYR B C   
3489  O O   . TYR B 33  ? 0.7288 1.2855 0.6892 0.2029  0.1238  -0.5581 33  TYR B O   
3490  C CB  . TYR B 33  ? 0.8231 1.2333 0.7356 0.2289  0.0978  -0.5931 33  TYR B CB  
3491  C CG  . TYR B 33  ? 0.8922 1.2225 0.7768 0.2450  0.0827  -0.6106 33  TYR B CG  
3492  C CD1 . TYR B 33  ? 0.9107 1.1848 0.7958 0.2369  0.0787  -0.5986 33  TYR B CD1 
3493  C CD2 . TYR B 33  ? 0.9697 1.2793 0.8256 0.2686  0.0714  -0.6391 33  TYR B CD2 
3494  C CE1 . TYR B 33  ? 0.9758 1.1735 0.8331 0.2504  0.0635  -0.6136 33  TYR B CE1 
3495  C CE2 . TYR B 33  ? 1.0402 1.2703 0.8664 0.2831  0.0555  -0.6552 33  TYR B CE2 
3496  C CZ  . TYR B 33  ? 1.0385 1.2126 0.8656 0.2732  0.0515  -0.6418 33  TYR B CZ  
3497  O OH  . TYR B 33  ? 1.1095 1.2028 0.9053 0.2862  0.0346  -0.6565 33  TYR B OH  
3498  N N   . GLN B 34  ? 0.7545 1.3826 0.7019 0.2551  0.1225  -0.5883 34  GLN B N   
3499  C CA  . GLN B 34  ? 0.7121 1.4201 0.6788 0.2401  0.1338  -0.5736 34  GLN B CA  
3500  C C   . GLN B 34  ? 0.6950 1.4075 0.6646 0.2139  0.1363  -0.5678 34  GLN B C   
3501  O O   . GLN B 34  ? 0.6559 1.4115 0.6435 0.1906  0.1450  -0.5466 34  GLN B O   
3502  C CB  . GLN B 34  ? 0.7251 1.5040 0.6873 0.2691  0.1356  -0.5902 34  GLN B CB  
3503  C CG  . GLN B 34  ? 0.6986 1.5641 0.6801 0.2537  0.1467  -0.5734 34  GLN B CG  
3504  C CD  . GLN B 34  ? 0.7376 1.6772 0.7170 0.2833  0.1488  -0.5864 34  GLN B CD  
3505  O OE1 . GLN B 34  ? 0.7717 1.7410 0.7374 0.3045  0.1461  -0.6089 34  GLN B OE1 
3506  N NE2 . GLN B 34  ? 0.7276 1.6998 0.7198 0.2862  0.1533  -0.5728 34  GLN B NE2 
3507  N N   . SER B 35  ? 0.7271 1.3947 0.6775 0.2176  0.1277  -0.5862 35  SER B N   
3508  C CA  . SER B 35  ? 0.7163 1.3881 0.6673 0.1946  0.1291  -0.5832 35  SER B CA  
3509  C C   . SER B 35  ? 0.6901 1.3164 0.6510 0.1609  0.1301  -0.5614 35  SER B C   
3510  O O   . SER B 35  ? 0.6810 1.3080 0.6431 0.1406  0.1311  -0.5570 35  SER B O   
3511  C CB  . SER B 35  ? 0.7656 1.4096 0.6904 0.2120  0.1187  -0.6126 35  SER B CB  
3512  O OG  . SER B 35  ? 0.8085 1.3746 0.7140 0.2241  0.1070  -0.6250 35  SER B OG  
3513  N N   . THR B 36  ? 0.6765 1.2658 0.6441 0.1562  0.1299  -0.5480 36  THR B N   
3514  C CA  . THR B 36  ? 0.6567 1.2003 0.6314 0.1288  0.1298  -0.5293 36  THR B CA  
3515  C C   . THR B 36  ? 0.6217 1.1740 0.6136 0.1235  0.1361  -0.5080 36  THR B C   
3516  O O   . THR B 36  ? 0.6094 1.1219 0.6072 0.1072  0.1358  -0.4927 36  THR B O   
3517  C CB  . THR B 36  ? 0.6988 1.1638 0.6541 0.1324  0.1180  -0.5420 36  THR B CB  
3518  O OG1 . THR B 36  ? 0.7549 1.2104 0.6903 0.1406  0.1105  -0.5647 36  THR B OG1 
3519  C CG2 . THR B 36  ? 0.6849 1.1083 0.6469 0.1035  0.1177  -0.5233 36  THR B CG2 
3520  N N   . CYS B 37  ? 0.6093 1.2164 0.6090 0.1373  0.1415  -0.5070 37  CYS B N   
3521  C CA  . CYS B 37  ? 0.5838 1.2022 0.5984 0.1331  0.1467  -0.4876 37  CYS B CA  
3522  C C   . CYS B 37  ? 0.5865 1.1366 0.5996 0.1287  0.1421  -0.4809 37  CYS B C   
3523  O O   . CYS B 37  ? 0.5632 1.1048 0.5893 0.1091  0.1463  -0.4587 37  CYS B O   
3524  C CB  . CYS B 37  ? 0.5417 1.2025 0.5734 0.1073  0.1554  -0.4630 37  CYS B CB  
3525  S SG  . CYS B 37  ? 0.5421 1.2500 0.5878 0.1098  0.1616  -0.4466 37  CYS B SG  
3526  N N   . SER B 38  ? 0.6221 1.1229 0.6176 0.1472  0.1328  -0.5002 38  SER B N   
3527  C CA  . SER B 38  ? 0.6298 1.0620 0.6207 0.1431  0.1268  -0.4955 38  SER B CA  
3528  C C   . SER B 38  ? 0.6612 1.0633 0.6369 0.1725  0.1187  -0.5129 38  SER B C   
3529  O O   . SER B 38  ? 0.6895 1.1074 0.6514 0.1975  0.1147  -0.5346 38  SER B O   
3530  C CB  . SER B 38  ? 0.6482 1.0291 0.6294 0.1243  0.1207  -0.4969 38  SER B CB  
3531  O OG  . SER B 38  ? 0.6847 1.0611 0.6476 0.1343  0.1141  -0.5194 38  SER B OG  
3532  N N   . ALA B 39  ? 0.6587 1.0165 0.6356 0.1706  0.1160  -0.5037 39  ALA B N   
3533  C CA  . ALA B 39  ? 0.6915 1.0197 0.6543 0.1985  0.1082  -0.5178 39  ALA B CA  
3534  C C   . ALA B 39  ? 0.7211 0.9677 0.6702 0.1916  0.0981  -0.5175 39  ALA B C   
3535  O O   . ALA B 39  ? 0.7010 0.9249 0.6610 0.1653  0.1007  -0.4978 39  ALA B O   
3536  C CB  . ALA B 39  ? 0.6640 1.0298 0.6430 0.2061  0.1154  -0.5054 39  ALA B CB  
3537  N N   . VAL B 40  ? 0.7700 0.9727 0.6941 0.2156  0.0860  -0.5389 40  VAL B N   
3538  C CA  . VAL B 40  ? 0.8037 0.9263 0.7118 0.2095  0.0746  -0.5385 40  VAL B CA  
3539  C C   . VAL B 40  ? 0.8341 0.9273 0.7313 0.2359  0.0679  -0.5452 40  VAL B C   
3540  O O   . VAL B 40  ? 0.8605 0.9699 0.7455 0.2680  0.0643  -0.5641 40  VAL B O   
3541  C CB  . VAL B 40  ? 0.8493 0.9233 0.7308 0.2072  0.0621  -0.5561 40  VAL B CB  
3542  C CG1 . VAL B 40  ? 0.8961 0.8862 0.7570 0.2033  0.0483  -0.5567 40  VAL B CG1 
3543  C CG2 . VAL B 40  ? 0.8221 0.9147 0.7145 0.1760  0.0678  -0.5458 40  VAL B CG2 
3544  N N   . SER B 41  ? 0.8344 0.8855 0.7357 0.2226  0.0660  -0.5293 41  SER B N   
3545  C CA  . SER B 41  ? 0.8694 0.8839 0.7591 0.2450  0.0585  -0.5338 41  SER B CA  
3546  C C   . SER B 41  ? 0.9324 0.8623 0.7899 0.2463  0.0410  -0.5466 41  SER B C   
3547  O O   . SER B 41  ? 0.9327 0.8234 0.7881 0.2170  0.0375  -0.5360 41  SER B O   
3548  C CB  . SER B 41  ? 0.8342 0.8480 0.7454 0.2289  0.0656  -0.5086 41  SER B CB  
3549  O OG  . SER B 41  ? 0.7828 0.8636 0.7234 0.2145  0.0810  -0.4910 41  SER B OG  
3550  N N   . LYS B 42  ? 0.9889 0.8905 0.8201 0.2801  0.0292  -0.5687 42  LYS B N   
3551  C CA  . LYS B 42  ? 1.0657 0.8846 0.8600 0.2834  0.0102  -0.5842 42  LYS B CA  
3552  C C   . LYS B 42  ? 1.1071 0.8677 0.8819 0.3036  -0.0019 -0.5877 42  LYS B C   
3553  O O   . LYS B 42  ? 1.0869 0.8793 0.8747 0.3236  0.0045  -0.5839 42  LYS B O   
3554  C CB  . LYS B 42  ? 1.1118 0.9362 0.8820 0.3077  0.0026  -0.6126 42  LYS B CB  
3555  C CG  . LYS B 42  ? 1.0970 0.9820 0.8834 0.2926  0.0136  -0.6125 42  LYS B CG  
3556  C CD  . LYS B 42  ? 1.1792 1.0772 0.9421 0.3232  0.0067  -0.6421 42  LYS B CD  
3557  C CE  . LYS B 42  ? 1.1582 1.1163 0.9366 0.3073  0.0172  -0.6417 42  LYS B CE  
3558  N NZ  . LYS B 42  ? 1.2230 1.1764 0.9729 0.3307  0.0074  -0.6709 42  LYS B NZ  
3559  N N   . GLY B 43  ? 1.1674 0.8428 0.9095 0.2977  -0.0200 -0.5947 43  GLY B N   
3560  C CA  . GLY B 43  ? 1.2214 0.8290 0.9361 0.3192  -0.0356 -0.6017 43  GLY B CA  
3561  C C   . GLY B 43  ? 1.2076 0.7782 0.9318 0.2948  -0.0359 -0.5772 43  GLY B C   
3562  O O   . GLY B 43  ? 1.2293 0.7708 0.9445 0.3139  -0.0420 -0.5767 43  GLY B O   
3563  N N   . TYR B 44  ? 1.1697 0.7439 0.9118 0.2534  -0.0294 -0.5568 44  TYR B N   
3564  C CA  . TYR B 44  ? 1.1473 0.6938 0.9002 0.2275  -0.0286 -0.5327 44  TYR B CA  
3565  C C   . TYR B 44  ? 1.2030 0.6674 0.9251 0.2054  -0.0468 -0.5325 44  TYR B C   
3566  O O   . TYR B 44  ? 1.2423 0.6839 0.9431 0.1992  -0.0560 -0.5462 44  TYR B O   
3567  C CB  . TYR B 44  ? 1.0707 0.6776 0.8626 0.1969  -0.0098 -0.5097 44  TYR B CB  
3568  C CG  . TYR B 44  ? 1.0124 0.6962 0.8350 0.2128  0.0075  -0.5047 44  TYR B CG  
3569  C CD1 . TYR B 44  ? 0.9837 0.7346 0.8224 0.2158  0.0191  -0.5102 44  TYR B CD1 
3570  C CD2 . TYR B 44  ? 0.9886 0.6788 0.8233 0.2235  0.0117  -0.4938 44  TYR B CD2 
3571  C CE1 . TYR B 44  ? 0.9382 0.7606 0.8039 0.2273  0.0341  -0.5039 44  TYR B CE1 
3572  C CE2 . TYR B 44  ? 0.9456 0.7072 0.8075 0.2356  0.0268  -0.4881 44  TYR B CE2 
3573  C CZ  . TYR B 44  ? 0.9245 0.7518 0.8014 0.2366  0.0377  -0.4929 44  TYR B CZ  
3574  O OH  . TYR B 44  ? 0.8897 0.7879 0.7920 0.2456  0.0517  -0.4858 44  TYR B OH  
3575  N N   . LEU B 45  ? 1.2068 0.6282 0.9263 0.1918  -0.0522 -0.5162 45  LEU B N   
3576  C CA  . LEU B 45  ? 1.2576 0.5982 0.9464 0.1682  -0.0708 -0.5131 45  LEU B CA  
3577  C C   . LEU B 45  ? 1.2186 0.5612 0.9272 0.1255  -0.0650 -0.4848 45  LEU B C   
3578  O O   . LEU B 45  ? 1.1803 0.5423 0.9118 0.1212  -0.0556 -0.4664 45  LEU B O   
3579  C CB  . LEU B 45  ? 1.3280 0.5949 0.9810 0.1933  -0.0899 -0.5238 45  LEU B CB  
3580  C CG  . LEU B 45  ? 1.3739 0.6299 0.9997 0.2369  -0.0993 -0.5545 45  LEU B CG  
3581  C CD1 . LEU B 45  ? 1.4276 0.6331 1.0280 0.2707  -0.1126 -0.5633 45  LEU B CD1 
3582  C CD2 . LEU B 45  ? 1.4372 0.6467 1.0287 0.2275  -0.1151 -0.5713 45  LEU B CD2 
3583  N N   . SER B 46  ? 1.2292 0.5515 0.9268 0.0946  -0.0716 -0.4824 46  SER B N   
3584  C CA  . SER B 46  ? 1.1895 0.5237 0.9052 0.0528  -0.0658 -0.4577 46  SER B CA  
3585  C C   . SER B 46  ? 1.2156 0.4962 0.9200 0.0350  -0.0761 -0.4407 46  SER B C   
3586  O O   . SER B 46  ? 1.2814 0.4919 0.9519 0.0462  -0.0945 -0.4491 46  SER B O   
3587  C CB  . SER B 46  ? 1.2126 0.5298 0.9116 0.0264  -0.0743 -0.4623 46  SER B CB  
3588  O OG  . SER B 46  ? 1.2902 0.5212 0.9443 0.0243  -0.0987 -0.4726 46  SER B OG  
3589  N N   . ALA B 47  ? 1.1627 0.4784 0.8951 0.0064  -0.0643 -0.4165 47  ALA B N   
3590  C CA  . ALA B 47  ? 1.1744 0.4526 0.9003 -0.0228 -0.0722 -0.3960 47  ALA B CA  
3591  C C   . ALA B 47  ? 1.1093 0.4462 0.8662 -0.0550 -0.0573 -0.3763 47  ALA B C   
3592  O O   . ALA B 47  ? 1.0467 0.4483 0.8383 -0.0484 -0.0380 -0.3682 47  ALA B O   
3593  C CB  . ALA B 47  ? 1.1665 0.4364 0.9003 -0.0064 -0.0696 -0.3871 47  ALA B CB  
3594  N N   . LEU B 48  ? 1.1237 0.4399 0.8669 -0.0892 -0.0666 -0.3693 48  LEU B N   
3595  C CA  . LEU B 48  ? 1.0596 0.4355 0.8299 -0.1159 -0.0530 -0.3540 48  LEU B CA  
3596  C C   . LEU B 48  ? 1.0623 0.4266 0.8326 -0.1517 -0.0574 -0.3302 48  LEU B C   
3597  O O   . LEU B 48  ? 1.1222 0.4322 0.8626 -0.1739 -0.0755 -0.3289 48  LEU B O   
3598  C CB  . LEU B 48  ? 1.0679 0.4529 0.8283 -0.1253 -0.0562 -0.3670 48  LEU B CB  
3599  C CG  . LEU B 48  ? 1.0783 0.4585 0.8259 -0.0946 -0.0587 -0.3940 48  LEU B CG  
3600  C CD1 . LEU B 48  ? 1.0548 0.4666 0.8050 -0.1108 -0.0558 -0.3992 48  LEU B CD1 
3601  C CD2 . LEU B 48  ? 1.0413 0.4701 0.8145 -0.0610 -0.0423 -0.3995 48  LEU B CD2 
3602  N N   . ARG B 49  ? 1.0010 0.4169 0.8035 -0.1578 -0.0414 -0.3113 49  ARG B N   
3603  C CA  . ARG B 49  ? 0.9960 0.4138 0.8026 -0.1903 -0.0431 -0.2875 49  ARG B CA  
3604  C C   . ARG B 49  ? 1.0104 0.4366 0.8089 -0.2248 -0.0488 -0.2823 49  ARG B C   
3605  O O   . ARG B 49  ? 0.9778 0.4507 0.7905 -0.2260 -0.0391 -0.2870 49  ARG B O   
3606  C CB  . ARG B 49  ? 0.9244 0.4050 0.7681 -0.1870 -0.0233 -0.2708 49  ARG B CB  
3607  C CG  . ARG B 49  ? 0.9143 0.3818 0.7603 -0.2009 -0.0255 -0.2500 49  ARG B CG  
3608  C CD  . ARG B 49  ? 0.8506 0.3816 0.7257 -0.2170 -0.0106 -0.2298 49  ARG B CD  
3609  N NE  . ARG B 49  ? 0.9155 0.4511 0.7815 -0.2528 -0.0178 -0.2195 49  ARG B NE  
3610  C CZ  . ARG B 49  ? 0.9232 0.5093 0.8025 -0.2655 -0.0097 -0.2169 49  ARG B CZ  
3611  N NH1 . ARG B 49  ? 0.8722 0.5077 0.7748 -0.2454 0.0062  -0.2230 49  ARG B NH1 
3612  N NH2 . ARG B 49  ? 0.9648 0.5528 0.8332 -0.2993 -0.0180 -0.2073 49  ARG B NH2 
3613  N N   . THR B 50  ? 1.0603 0.4422 0.8353 -0.2538 -0.0649 -0.2717 50  THR B N   
3614  C CA  . THR B 50  ? 1.0729 0.4684 0.8417 -0.2909 -0.0703 -0.2625 50  THR B CA  
3615  C C   . THR B 50  ? 1.0791 0.4788 0.8500 -0.3229 -0.0735 -0.2367 50  THR B C   
3616  O O   . THR B 50  ? 1.0936 0.5085 0.8595 -0.3568 -0.0784 -0.2258 50  THR B O   
3617  C CB  . THR B 50  ? 1.1415 0.4759 0.8709 -0.3018 -0.0913 -0.2781 50  THR B CB  
3618  O OG1 . THR B 50  ? 1.1955 0.4531 0.8947 -0.2870 -0.1076 -0.2872 50  THR B OG1 
3619  C CG2 . THR B 50  ? 1.1316 0.4878 0.8644 -0.2823 -0.0854 -0.2995 50  THR B CG2 
3620  N N   . GLY B 51  ? 1.0698 0.4594 0.8476 -0.3134 -0.0710 -0.2263 51  GLY B N   
3621  C CA  . GLY B 51  ? 1.0781 0.4722 0.8561 -0.3442 -0.0749 -0.2019 51  GLY B CA  
3622  C C   . GLY B 51  ? 1.0593 0.4539 0.8512 -0.3270 -0.0679 -0.1925 51  GLY B C   
3623  O O   . GLY B 51  ? 1.0441 0.4344 0.8446 -0.2922 -0.0607 -0.2049 51  GLY B O   
3624  N N   . TRP B 52  ? 1.0636 0.4662 0.8574 -0.3524 -0.0703 -0.1700 52  TRP B N   
3625  C CA  . TRP B 52  ? 1.0415 0.4506 0.8500 -0.3392 -0.0630 -0.1585 52  TRP B CA  
3626  C C   . TRP B 52  ? 1.0969 0.4500 0.8796 -0.3599 -0.0807 -0.1457 52  TRP B C   
3627  O O   . TRP B 52  ? 1.1405 0.4725 0.9013 -0.3950 -0.0954 -0.1366 52  TRP B O   
3628  C CB  . TRP B 52  ? 0.9792 0.4670 0.8212 -0.3462 -0.0449 -0.1412 52  TRP B CB  
3629  C CG  . TRP B 52  ? 0.9356 0.4793 0.8038 -0.3247 -0.0270 -0.1514 52  TRP B CG  
3630  C CD1 . TRP B 52  ? 0.9276 0.5198 0.8059 -0.3374 -0.0206 -0.1511 52  TRP B CD1 
3631  C CD2 . TRP B 52  ? 0.9022 0.4597 0.7885 -0.2876 -0.0139 -0.1630 52  TRP B CD2 
3632  N NE1 . TRP B 52  ? 0.8731 0.5060 0.7741 -0.3102 -0.0045 -0.1617 52  TRP B NE1 
3633  C CE2 . TRP B 52  ? 0.8589 0.4717 0.7649 -0.2805 -0.0003 -0.1688 52  TRP B CE2 
3634  C CE3 . TRP B 52  ? 0.9023 0.4322 0.7894 -0.2605 -0.0127 -0.1685 52  TRP B CE3 
3635  C CZ2 . TRP B 52  ? 0.8154 0.4544 0.7405 -0.2494 0.0135  -0.1791 52  TRP B CZ2 
3636  C CZ3 . TRP B 52  ? 0.8580 0.4177 0.7655 -0.2294 0.0016  -0.1789 52  TRP B CZ3 
3637  C CH2 . TRP B 52  ? 0.8181 0.4311 0.7439 -0.2249 0.0143  -0.1838 52  TRP B CH2 
3638  N N   . TYR B 53  ? 1.0982 0.4291 0.8834 -0.3389 -0.0795 -0.1440 53  TYR B N   
3639  C CA  . TYR B 53  ? 1.1533 0.4323 0.9159 -0.3553 -0.0951 -0.1303 53  TYR B CA  
3640  C C   . TYR B 53  ? 1.1096 0.4334 0.8984 -0.3552 -0.0821 -0.1105 53  TYR B C   
3641  O O   . TYR B 53  ? 1.0730 0.4164 0.8827 -0.3239 -0.0687 -0.1153 53  TYR B O   
3642  C CB  . TYR B 53  ? 1.2063 0.4080 0.9418 -0.3292 -0.1088 -0.1475 53  TYR B CB  
3643  C CG  . TYR B 53  ? 1.2676 0.4082 0.9773 -0.3410 -0.1260 -0.1352 53  TYR B CG  
3644  C CD1 . TYR B 53  ? 1.3590 0.4343 1.0285 -0.3704 -0.1502 -0.1315 53  TYR B CD1 
3645  C CD2 . TYR B 53  ? 1.2527 0.3987 0.9766 -0.3227 -0.1188 -0.1271 53  TYR B CD2 
3646  C CE1 . TYR B 53  ? 1.4256 0.4418 1.0693 -0.3817 -0.1671 -0.1193 53  TYR B CE1 
3647  C CE2 . TYR B 53  ? 1.3130 0.4033 1.0131 -0.3328 -0.1345 -0.1155 53  TYR B CE2 
3648  C CZ  . TYR B 53  ? 1.3969 0.4222 1.0568 -0.3623 -0.1587 -0.1113 53  TYR B CZ  
3649  O OH  . TYR B 53  ? 1.4547 0.4230 1.0896 -0.3729 -0.1751 -0.0986 53  TYR B OH  
3650  N N   . THR B 54  ? 1.1205 0.4624 0.9071 -0.3912 -0.0865 -0.0882 54  THR B N   
3651  C CA  . THR B 54  ? 1.0885 0.4757 0.8967 -0.3969 -0.0761 -0.0674 54  THR B CA  
3652  C C   . THR B 54  ? 1.1247 0.4579 0.9168 -0.3934 -0.0869 -0.0601 54  THR B C   
3653  O O   . THR B 54  ? 1.1986 0.4606 0.9564 -0.4049 -0.1075 -0.0627 54  THR B O   
3654  C CB  . THR B 54  ? 1.0975 0.5219 0.9038 -0.4403 -0.0800 -0.0467 54  THR B CB  
3655  O OG1 . THR B 54  ? 1.0538 0.5546 0.8882 -0.4372 -0.0626 -0.0478 54  THR B OG1 
3656  C CG2 . THR B 54  ? 1.1135 0.5494 0.9210 -0.4603 -0.0825 -0.0214 54  THR B CG2 
3657  N N   . SER B 55  ? 1.0836 0.4477 0.8981 -0.3775 -0.0743 -0.0512 55  SER B N   
3658  C CA  . SER B 55  ? 1.1190 0.4457 0.9204 -0.3837 -0.0841 -0.0370 55  SER B CA  
3659  C C   . SER B 55  ? 1.0712 0.4529 0.9004 -0.3782 -0.0690 -0.0211 55  SER B C   
3660  O O   . SER B 55  ? 1.0173 0.4450 0.8747 -0.3513 -0.0506 -0.0276 55  SER B O   
3661  C CB  . SER B 55  ? 1.1596 0.4134 0.9410 -0.3562 -0.0946 -0.0518 55  SER B CB  
3662  O OG  . SER B 55  ? 1.1788 0.4078 0.9529 -0.3601 -0.1009 -0.0364 55  SER B OG  
3663  N N   . VAL B 56  ? 1.1008 0.4718 0.9188 -0.4037 -0.0783 -0.0004 56  VAL B N   
3664  C CA  . VAL B 56  ? 1.0573 0.4896 0.8987 -0.4091 -0.0658 0.0182  56  VAL B CA  
3665  C C   . VAL B 56  ? 1.0587 0.4645 0.8997 -0.3925 -0.0667 0.0235  56  VAL B C   
3666  O O   . VAL B 56  ? 1.1114 0.4705 0.9289 -0.4108 -0.0827 0.0355  56  VAL B O   
3667  C CB  . VAL B 56  ? 1.0829 0.5374 0.9144 -0.4537 -0.0745 0.0408  56  VAL B CB  
3668  C CG1 . VAL B 56  ? 1.0220 0.5623 0.8835 -0.4554 -0.0571 0.0555  56  VAL B CG1 
3669  C CG2 . VAL B 56  ? 1.1229 0.5694 0.9382 -0.4787 -0.0842 0.0354  56  VAL B CG2 
3670  N N   . ILE B 57  ? 1.0021 0.4394 0.8687 -0.3590 -0.0497 0.0155  57  ILE B N   
3671  C CA  . ILE B 57  ? 0.9987 0.4138 0.8670 -0.3393 -0.0492 0.0182  57  ILE B CA  
3672  C C   . ILE B 57  ? 0.9614 0.4321 0.8492 -0.3462 -0.0387 0.0378  57  ILE B C   
3673  O O   . ILE B 57  ? 0.9087 0.4450 0.8210 -0.3411 -0.0228 0.0391  57  ILE B O   
3674  C CB  . ILE B 57  ? 0.9698 0.3769 0.8495 -0.2990 -0.0399 -0.0029 57  ILE B CB  
3675  C CG1 . ILE B 57  ? 1.0233 0.3689 0.8780 -0.2940 -0.0537 -0.0207 57  ILE B CG1 
3676  C CG2 . ILE B 57  ? 0.9693 0.3577 0.8517 -0.2782 -0.0389 -0.0002 57  ILE B CG2 
3677  C CD1 . ILE B 57  ? 1.0166 0.3733 0.8842 -0.2620 -0.0433 -0.0427 57  ILE B CD1 
3678  N N   . THR B 58  ? 0.9919 0.4350 0.8670 -0.3573 -0.0483 0.0528  58  THR B N   
3679  C CA  . THR B 58  ? 0.9678 0.4609 0.8573 -0.3677 -0.0409 0.0731  58  THR B CA  
3680  C C   . THR B 58  ? 0.9678 0.4395 0.8606 -0.3446 -0.0391 0.0740  58  THR B C   
3681  O O   . THR B 58  ? 1.0192 0.4244 0.8902 -0.3410 -0.0531 0.0712  58  THR B O   
3682  C CB  . THR B 58  ? 1.0091 0.4931 0.8784 -0.4095 -0.0559 0.0946  58  THR B CB  
3683  O OG1 . THR B 58  ? 1.0613 0.5160 0.9104 -0.4312 -0.0683 0.0894  58  THR B OG1 
3684  C CG2 . THR B 58  ? 0.9684 0.5318 0.8566 -0.4259 -0.0451 0.1126  58  THR B CG2 
3685  N N   . ILE B 59  ? 0.9206 0.4468 0.8388 -0.3284 -0.0228 0.0779  59  ILE B N   
3686  C CA  . ILE B 59  ? 0.9171 0.4279 0.8411 -0.3031 -0.0193 0.0768  59  ILE B CA  
3687  C C   . ILE B 59  ? 0.9056 0.4588 0.8406 -0.3108 -0.0134 0.0960  59  ILE B C   
3688  O O   . ILE B 59  ? 0.8640 0.4808 0.8183 -0.3100 -0.0002 0.1001  59  ILE B O   
3689  C CB  . ILE B 59  ? 0.8695 0.3934 0.8123 -0.2663 -0.0055 0.0571  59  ILE B CB  
3690  C CG1 . ILE B 59  ? 0.8961 0.3704 0.8249 -0.2557 -0.0132 0.0377  59  ILE B CG1 
3691  C CG2 . ILE B 59  ? 0.8506 0.3687 0.8012 -0.2429 -0.0009 0.0582  59  ILE B CG2 
3692  C CD1 . ILE B 59  ? 0.8842 0.3604 0.8265 -0.2200 -0.0032 0.0192  59  ILE B CD1 
3693  N N   . GLU B 60  ? 0.9531 0.4693 0.8738 -0.3172 -0.0241 0.1075  60  GLU B N   
3694  C CA  . GLU B 60  ? 0.9537 0.5052 0.8830 -0.3228 -0.0196 0.1258  60  GLU B CA  
3695  C C   . GLU B 60  ? 0.9118 0.4844 0.8620 -0.2875 -0.0051 0.1174  60  GLU B C   
3696  O O   . GLU B 60  ? 0.9203 0.4550 0.8692 -0.2621 -0.0055 0.1025  60  GLU B O   
3697  C CB  . GLU B 60  ? 1.0124 0.5137 0.9173 -0.3429 -0.0372 0.1416  60  GLU B CB  
3698  C CG  . GLU B 60  ? 1.0935 0.5868 0.9777 -0.3858 -0.0518 0.1576  60  GLU B CG  
3699  C CD  . GLU B 60  ? 1.1999 0.6624 1.0635 -0.4094 -0.0669 0.1794  60  GLU B CD  
3700  O OE1 . GLU B 60  ? 1.2425 0.6627 1.0998 -0.3910 -0.0712 0.1777  60  GLU B OE1 
3701  O OE2 . GLU B 60  ? 1.2415 0.7231 1.0946 -0.4472 -0.0750 0.1989  60  GLU B OE2 
3702  N N   . LEU B 61  ? 0.8731 0.5073 0.8412 -0.2858 0.0071  0.1267  61  LEU B N   
3703  C CA  . LEU B 61  ? 0.8364 0.4908 0.8213 -0.2569 0.0191  0.1222  61  LEU B CA  
3704  C C   . LEU B 61  ? 0.8684 0.4928 0.8434 -0.2593 0.0108  0.1345  61  LEU B C   
3705  O O   . LEU B 61  ? 0.9025 0.5179 0.8633 -0.2866 0.0001  0.1512  61  LEU B O   
3706  C CB  . LEU B 61  ? 0.7901 0.5172 0.7924 -0.2571 0.0322  0.1294  61  LEU B CB  
3707  C CG  . LEU B 61  ? 0.7564 0.5084 0.7710 -0.2370 0.0414  0.1327  61  LEU B CG  
3708  C CD1 . LEU B 61  ? 0.7276 0.4814 0.7555 -0.2048 0.0522  0.1140  61  LEU B CD1 
3709  C CD2 . LEU B 61  ? 0.7288 0.5458 0.7515 -0.2470 0.0484  0.1461  61  LEU B CD2 
3710  N N   . SER B 62  ? 0.8640 0.4742 0.8455 -0.2324 0.0151  0.1273  62  SER B N   
3711  C CA  . SER B 62  ? 0.8965 0.4856 0.8704 -0.2334 0.0086  0.1400  62  SER B CA  
3712  C C   . SER B 62  ? 0.8673 0.5119 0.8580 -0.2264 0.0206  0.1487  62  SER B C   
3713  O O   . SER B 62  ? 0.8361 0.4957 0.8406 -0.2005 0.0310  0.1387  62  SER B O   
3714  C CB  . SER B 62  ? 0.9123 0.4479 0.8799 -0.2093 0.0037  0.1279  62  SER B CB  
3715  O OG  . SER B 62  ? 0.9645 0.4427 0.9109 -0.2176 -0.0106 0.1220  62  SER B OG  
3716  N N   . ASN B 63  ? 0.8908 0.5673 0.8789 -0.2500 0.0186  0.1677  63  ASN B N   
3717  C CA  . ASN B 63  ? 0.8653 0.6054 0.8693 -0.2438 0.0311  0.1743  63  ASN B CA  
3718  C C   . ASN B 63  ? 0.8706 0.6084 0.8772 -0.2308 0.0324  0.1808  63  ASN B C   
3719  O O   . ASN B 63  ? 0.9109 0.6074 0.9043 -0.2384 0.0214  0.1894  63  ASN B O   
3720  C CB  . ASN B 63  ? 0.8691 0.6573 0.8712 -0.2726 0.0301  0.1913  63  ASN B CB  
3721  C CG  . ASN B 63  ? 0.8307 0.6895 0.8501 -0.2610 0.0450  0.1883  63  ASN B CG  
3722  O OD1 . ASN B 63  ? 0.7992 0.6779 0.8295 -0.2366 0.0546  0.1829  63  ASN B OD1 
3723  N ND2 . ASN B 63  ? 0.8337 0.7292 0.8537 -0.2781 0.0461  0.1914  63  ASN B ND2 
3724  N N   . ILE B 64  ? 0.8439 0.6251 0.8659 -0.2111 0.0453  0.1767  64  ILE B N   
3725  C CA  . ILE B 64  ? 0.8558 0.6444 0.8811 -0.1995 0.0477  0.1835  64  ILE B CA  
3726  C C   . ILE B 64  ? 0.8758 0.7130 0.9009 -0.2166 0.0485  0.2029  64  ILE B C   
3727  O O   . ILE B 64  ? 0.8549 0.7464 0.8876 -0.2184 0.0565  0.2038  64  ILE B O   
3728  C CB  . ILE B 64  ? 0.8067 0.6187 0.8464 -0.1701 0.0604  0.1700  64  ILE B CB  
3729  C CG1 . ILE B 64  ? 0.7933 0.5721 0.8359 -0.1526 0.0619  0.1504  64  ILE B CG1 
3730  C CG2 . ILE B 64  ? 0.8103 0.6225 0.8515 -0.1584 0.0613  0.1764  64  ILE B CG2 
3731  C CD1 . ILE B 64  ? 0.7523 0.5511 0.8069 -0.1265 0.0728  0.1383  64  ILE B CD1 
3732  N N   . LYS B 65  ? 0.9274 0.7479 0.9435 -0.2273 0.0405  0.2180  65  LYS B N   
3733  C CA  . LYS B 65  ? 0.9435 0.8148 0.9617 -0.2364 0.0432  0.2353  65  LYS B CA  
3734  C C   . LYS B 65  ? 0.9281 0.8133 0.9555 -0.2094 0.0515  0.2312  65  LYS B C   
3735  O O   . LYS B 65  ? 0.9418 0.7928 0.9647 -0.2035 0.0464  0.2348  65  LYS B O   
3736  C CB  . LYS B 65  ? 0.9855 0.8451 0.9880 -0.2695 0.0298  0.2577  65  LYS B CB  
3737  C CG  . LYS B 65  ? 1.0482 0.8306 1.0342 -0.2770 0.0153  0.2582  65  LYS B CG  
3738  C CD  . LYS B 65  ? 1.0658 0.8103 1.0554 -0.2465 0.0172  0.2467  65  LYS B CD  
3739  C CE  . LYS B 65  ? 1.1223 0.8008 1.0930 -0.2538 0.0015  0.2545  65  LYS B CE  
3740  N NZ  . LYS B 65  ? 1.1064 0.7721 1.0817 -0.2295 0.0041  0.2521  65  LYS B NZ  
3741  N N   . GLU B 66  ? 0.9036 0.8379 0.9425 -0.1930 0.0636  0.2232  66  GLU B N   
3742  C CA  . GLU B 66  ? 0.8874 0.8369 0.9346 -0.1650 0.0725  0.2149  66  GLU B CA  
3743  C C   . GLU B 66  ? 0.8953 0.8660 0.9404 -0.1665 0.0716  0.2297  66  GLU B C   
3744  O O   . GLU B 66  ? 0.9051 0.9134 0.9466 -0.1856 0.0696  0.2461  66  GLU B O   
3745  C CB  . GLU B 66  ? 0.8534 0.8477 0.9087 -0.1504 0.0832  0.2039  66  GLU B CB  
3746  C CG  . GLU B 66  ? 0.8489 0.8810 0.9081 -0.1296 0.0911  0.2021  66  GLU B CG  
3747  C CD  . GLU B 66  ? 0.8715 0.9552 0.9337 -0.1214 0.0990  0.1964  66  GLU B CD  
3748  O OE1 . GLU B 66  ? 0.8792 0.9840 0.9425 -0.0990 0.1054  0.1891  66  GLU B OE1 
3749  O OE2 . GLU B 66  ? 0.8786 0.9810 0.9406 -0.1366 0.0983  0.1989  66  GLU B OE2 
3750  N N   . ASN B 67  ? 0.8952 0.8446 0.9424 -0.1472 0.0730  0.2246  67  ASN B N   
3751  C CA  . ASN B 67  ? 0.9050 0.8667 0.9490 -0.1499 0.0706  0.2392  67  ASN B CA  
3752  C C   . ASN B 67  ? 0.8765 0.8756 0.9258 -0.1288 0.0792  0.2357  67  ASN B C   
3753  O O   . ASN B 67  ? 0.8724 0.8520 0.9229 -0.1126 0.0798  0.2316  67  ASN B O   
3754  C CB  . ASN B 67  ? 0.9362 0.8430 0.9726 -0.1557 0.0603  0.2457  67  ASN B CB  
3755  C CG  . ASN B 67  ? 0.9726 0.8675 0.9972 -0.1869 0.0491  0.2639  67  ASN B CG  
3756  O OD1 . ASN B 67  ? 0.9763 0.9075 0.9976 -0.2027 0.0476  0.2811  67  ASN B OD1 
3757  N ND2 . ASN B 67  ? 0.9933 0.8385 1.0100 -0.1968 0.0405  0.2603  67  ASN B ND2 
3758  N N   . LYS B 68  ? 0.8560 0.9090 0.9074 -0.1285 0.0854  0.2365  68  LYS B N   
3759  C CA  . LYS B 68  ? 0.8371 0.9396 0.8890 -0.1159 0.0914  0.2394  68  LYS B CA  
3760  C C   . LYS B 68  ? 0.8395 0.9282 0.8894 -0.1088 0.0892  0.2455  68  LYS B C   
3761  O O   . LYS B 68  ? 0.8563 0.9575 0.9020 -0.1244 0.0844  0.2630  68  LYS B O   
3762  C CB  . LYS B 68  ? 0.8461 1.0056 0.8954 -0.1346 0.0912  0.2549  68  LYS B CB  
3763  C CG  . LYS B 68  ? 0.8551 1.0266 0.9047 -0.1529 0.0901  0.2558  68  LYS B CG  
3764  C CD  . LYS B 68  ? 0.8816 1.0823 0.9257 -0.1857 0.0834  0.2788  68  LYS B CD  
3765  C CE  . LYS B 68  ? 0.8813 1.1144 0.9225 -0.1872 0.0828  0.2940  68  LYS B CE  
3766  N NZ  . LYS B 68  ? 0.9049 1.1761 0.9403 -0.2192 0.0768  0.3172  68  LYS B NZ  
3767  N N   . CYS B 69  ? 0.8207 0.8827 0.8732 -0.0866 0.0921  0.2312  69  CYS B N   
3768  C CA  . CYS B 69  ? 0.8151 0.8693 0.8665 -0.0748 0.0916  0.2333  69  CYS B CA  
3769  C C   . CYS B 69  ? 0.7952 0.8716 0.8471 -0.0500 0.0994  0.2184  69  CYS B C   
3770  O O   . CYS B 69  ? 0.7827 0.8842 0.8346 -0.0457 0.1038  0.2112  69  CYS B O   
3771  C CB  . CYS B 69  ? 0.8168 0.8131 0.8696 -0.0709 0.0870  0.2275  69  CYS B CB  
3772  S SG  . CYS B 69  ? 0.7882 0.7699 0.8457 -0.0445 0.0937  0.2037  69  CYS B SG  
3773  N N   . ASN B 70  ? 0.7978 0.8622 0.8486 -0.0338 0.1001  0.2135  70  ASN B N   
3774  C CA  . ASN B 70  ? 0.7917 0.8610 0.8402 -0.0108 0.1052  0.1978  70  ASN B CA  
3775  C C   . ASN B 70  ? 0.7644 0.7865 0.8162 -0.0022 0.1038  0.1866  70  ASN B C   
3776  O O   . ASN B 70  ? 0.7692 0.7692 0.8222 -0.0027 0.1002  0.1915  70  ASN B O   
3777  C CB  . ASN B 70  ? 0.8126 0.9120 0.8546 0.0003  0.1065  0.2021  70  ASN B CB  
3778  C CG  . ASN B 70  ? 0.9288 1.0767 0.9684 -0.0113 0.1066  0.2174  70  ASN B CG  
3779  O OD1 . ASN B 70  ? 0.9831 1.1544 1.0240 -0.0222 0.1076  0.2208  70  ASN B OD1 
3780  N ND2 . ASN B 70  ? 1.1059 1.2721 1.1417 -0.0095 0.1054  0.2270  70  ASN B ND2 
3781  N N   . GLY B 71  ? 0.7316 0.7400 0.7849 0.0050  0.1063  0.1724  71  GLY B N   
3782  C CA  . GLY B 71  ? 0.7028 0.6732 0.7592 0.0130  0.1053  0.1617  71  GLY B CA  
3783  C C   . GLY B 71  ? 0.6765 0.6492 0.7269 0.0307  0.1069  0.1533  71  GLY B C   
3784  O O   . GLY B 71  ? 0.6743 0.6745 0.7172 0.0380  0.1084  0.1549  71  GLY B O   
3785  N N   . THR B 72  ? 0.6580 0.6030 0.7105 0.0374  0.1060  0.1444  72  THR B N   
3786  C CA  . THR B 72  ? 0.6406 0.5845 0.6856 0.0516  0.1065  0.1356  72  THR B CA  
3787  C C   . THR B 72  ? 0.6353 0.5870 0.6737 0.0581  0.1090  0.1248  72  THR B C   
3788  O O   . THR B 72  ? 0.6381 0.5767 0.6813 0.0548  0.1100  0.1181  72  THR B O   
3789  C CB  . THR B 72  ? 0.6409 0.5562 0.6904 0.0545  0.1043  0.1300  72  THR B CB  
3790  O OG1 . THR B 72  ? 0.6170 0.5175 0.6701 0.0540  0.1055  0.1197  72  THR B OG1 
3791  C CG2 . THR B 72  ? 0.6510 0.5530 0.7084 0.0475  0.1012  0.1397  72  THR B CG2 
3792  N N   . ASP B 73  ? 0.6342 0.6066 0.6603 0.0685  0.1096  0.1228  73  ASP B N   
3793  C CA  . ASP B 73  ? 0.6303 0.6164 0.6480 0.0755  0.1117  0.1146  73  ASP B CA  
3794  C C   . ASP B 73  ? 0.6200 0.6276 0.6450 0.0653  0.1145  0.1200  73  ASP B C   
3795  O O   . ASP B 73  ? 0.6110 0.6041 0.6462 0.0543  0.1150  0.1196  73  ASP B O   
3796  C CB  . ASP B 73  ? 0.6283 0.5892 0.6414 0.0810  0.1108  0.1014  73  ASP B CB  
3797  C CG  . ASP B 73  ? 0.6387 0.6117 0.6407 0.0898  0.1119  0.0933  73  ASP B CG  
3798  O OD1 . ASP B 73  ? 0.6410 0.6432 0.6433 0.0894  0.1144  0.0976  73  ASP B OD1 
3799  O OD2 . ASP B 73  ? 0.6512 0.6054 0.6431 0.0970  0.1098  0.0831  73  ASP B OD2 
3800  N N   . ALA B 74  ? 0.6155 0.6592 0.6341 0.0692  0.1159  0.1248  74  ALA B N   
3801  C CA  . ALA B 74  ? 0.6135 0.6837 0.6383 0.0580  0.1182  0.1312  74  ALA B CA  
3802  C C   . ALA B 74  ? 0.6064 0.6954 0.6237 0.0677  0.1205  0.1223  74  ALA B C   
3803  O O   . ALA B 74  ? 0.6061 0.7320 0.6233 0.0647  0.1224  0.1277  74  ALA B O   
3804  C CB  . ALA B 74  ? 0.6167 0.7210 0.6432 0.0493  0.1180  0.1468  74  ALA B CB  
3805  N N   . LYS B 75  ? 0.6058 0.6702 0.6162 0.0789  0.1198  0.1092  75  LYS B N   
3806  C CA  . LYS B 75  ? 0.6094 0.6798 0.6162 0.0834  0.1214  0.1007  75  LYS B CA  
3807  C C   . LYS B 75  ? 0.6027 0.6499 0.6240 0.0674  0.1222  0.0999  75  LYS B C   
3808  O O   . LYS B 75  ? 0.6021 0.6593 0.6266 0.0629  0.1242  0.0973  75  LYS B O   
3809  C CB  . LYS B 75  ? 0.6163 0.6687 0.6057 0.1026  0.1189  0.0875  75  LYS B CB  
3810  C CG  . LYS B 75  ? 0.6410 0.7149 0.6117 0.1219  0.1170  0.0856  75  LYS B CG  
3811  C CD  . LYS B 75  ? 0.6800 0.7196 0.6349 0.1338  0.1119  0.0773  75  LYS B CD  
3812  C CE  . LYS B 75  ? 0.7095 0.7644 0.6513 0.1463  0.1095  0.0800  75  LYS B CE  
3813  N NZ  . LYS B 75  ? 0.7170 0.7439 0.6606 0.1411  0.1065  0.0823  75  LYS B NZ  
3814  N N   . VAL B 76  ? 0.5952 0.6121 0.6240 0.0603  0.1204  0.1015  76  VAL B N   
3815  C CA  . VAL B 76  ? 0.5864 0.5788 0.6275 0.0471  0.1202  0.1009  76  VAL B CA  
3816  C C   . VAL B 76  ? 0.5889 0.5957 0.6387 0.0301  0.1202  0.1127  76  VAL B C   
3817  O O   . VAL B 76  ? 0.5954 0.6135 0.6455 0.0254  0.1188  0.1236  76  VAL B O   
3818  C CB  . VAL B 76  ? 0.5883 0.5508 0.6328 0.0476  0.1177  0.1002  76  VAL B CB  
3819  C CG1 . VAL B 76  ? 0.5972 0.5371 0.6535 0.0351  0.1167  0.1014  76  VAL B CG1 
3820  C CG2 . VAL B 76  ? 0.5871 0.5332 0.6227 0.0601  0.1168  0.0890  76  VAL B CG2 
3821  N N   . LYS B 77  ? 0.5859 0.5916 0.6414 0.0199  0.1210  0.1110  77  LYS B N   
3822  C CA  . LYS B 77  ? 0.5945 0.6139 0.6553 0.0013  0.1198  0.1223  77  LYS B CA  
3823  C C   . LYS B 77  ? 0.5881 0.5829 0.6555 -0.0111 0.1183  0.1187  77  LYS B C   
3824  O O   . LYS B 77  ? 0.5893 0.6001 0.6580 -0.0202 0.1191  0.1194  77  LYS B O   
3825  C CB  . LYS B 77  ? 0.5976 0.6642 0.6539 0.0016  0.1224  0.1268  77  LYS B CB  
3826  C CG  . LYS B 77  ? 0.6397 0.7357 0.6933 -0.0016 0.1215  0.1403  77  LYS B CG  
3827  C CD  . LYS B 77  ? 0.6844 0.8203 0.7283 0.0160  0.1245  0.1378  77  LYS B CD  
3828  C CE  . LYS B 77  ? 0.7172 0.8755 0.7576 0.0170  0.1235  0.1491  77  LYS B CE  
3829  N NZ  . LYS B 77  ? 0.7430 0.9545 0.7743 0.0298  0.1261  0.1503  77  LYS B NZ  
3830  N N   . LEU B 78  ? 0.5827 0.5401 0.6538 -0.0109 0.1157  0.1150  78  LEU B N   
3831  C CA  . LEU B 78  ? 0.5765 0.5082 0.6522 -0.0164 0.1145  0.1072  78  LEU B CA  
3832  C C   . LEU B 78  ? 0.5850 0.5222 0.6617 -0.0352 0.1121  0.1139  78  LEU B C   
3833  O O   . LEU B 78  ? 0.5822 0.5278 0.6600 -0.0382 0.1141  0.1080  78  LEU B O   
3834  C CB  . LEU B 78  ? 0.5790 0.4732 0.6577 -0.0127 0.1113  0.1034  78  LEU B CB  
3835  C CG  . LEU B 78  ? 0.5668 0.4587 0.6439 0.0042  0.1135  0.0965  78  LEU B CG  
3836  C CD1 . LEU B 78  ? 0.5652 0.4267 0.6460 0.0094  0.1109  0.0918  78  LEU B CD1 
3837  C CD2 . LEU B 78  ? 0.5545 0.4603 0.6278 0.0141  0.1177  0.0861  78  LEU B CD2 
3838  N N   . ILE B 79  ? 0.5959 0.5299 0.6712 -0.0488 0.1074  0.1270  79  ILE B N   
3839  C CA  . ILE B 79  ? 0.6096 0.5419 0.6837 -0.0697 0.1031  0.1342  79  ILE B CA  
3840  C C   . ILE B 79  ? 0.5976 0.5725 0.6714 -0.0752 0.1070  0.1358  79  ILE B C   
3841  O O   . ILE B 79  ? 0.6013 0.5733 0.6762 -0.0831 0.1067  0.1308  79  ILE B O   
3842  C CB  . ILE B 79  ? 0.6351 0.5570 0.7048 -0.0854 0.0960  0.1500  79  ILE B CB  
3843  C CG1 . ILE B 79  ? 0.6483 0.5259 0.7175 -0.0775 0.0916  0.1472  79  ILE B CG1 
3844  C CG2 . ILE B 79  ? 0.6576 0.5745 0.7232 -0.1099 0.0900  0.1576  79  ILE B CG2 
3845  C CD1 . ILE B 79  ? 0.6804 0.5454 0.7438 -0.0892 0.0843  0.1631  79  ILE B CD1 
3846  N N   . LYS B 80  ? 0.5835 0.5993 0.6555 -0.0697 0.1105  0.1420  80  LYS B N   
3847  C CA  . LYS B 80  ? 0.5723 0.6338 0.6436 -0.0698 0.1148  0.1420  80  LYS B CA  
3848  C C   . LYS B 80  ? 0.5545 0.6068 0.6276 -0.0596 0.1183  0.1263  80  LYS B C   
3849  O O   . LYS B 80  ? 0.5526 0.6191 0.6268 -0.0698 0.1186  0.1256  80  LYS B O   
3850  C CB  . LYS B 80  ? 0.5658 0.6673 0.6331 -0.0546 0.1189  0.1447  80  LYS B CB  
3851  C CG  . LYS B 80  ? 0.5730 0.7183 0.6375 -0.0445 0.1238  0.1395  80  LYS B CG  
3852  C CD  . LYS B 80  ? 0.6208 0.8193 0.6842 -0.0583 0.1237  0.1536  80  LYS B CD  
3853  C CE  . LYS B 80  ? 0.6402 0.8702 0.7042 -0.0614 0.1262  0.1500  80  LYS B CE  
3854  N NZ  . LYS B 80  ? 0.6869 0.8988 0.7554 -0.0881 0.1220  0.1549  80  LYS B NZ  
3855  N N   . GLN B 81  ? 0.5384 0.5671 0.6114 -0.0411 0.1203  0.1146  81  GLN B N   
3856  C CA  . GLN B 81  ? 0.5241 0.5473 0.5972 -0.0295 0.1236  0.1005  81  GLN B CA  
3857  C C   . GLN B 81  ? 0.5221 0.5190 0.5999 -0.0411 0.1215  0.0952  81  GLN B C   
3858  O O   . GLN B 81  ? 0.5210 0.5321 0.5992 -0.0442 0.1233  0.0908  81  GLN B O   
3859  C CB  . GLN B 81  ? 0.5175 0.5232 0.5873 -0.0096 0.1251  0.0915  81  GLN B CB  
3860  C CG  . GLN B 81  ? 0.5489 0.5837 0.6107 0.0039  0.1268  0.0948  81  GLN B CG  
3861  C CD  . GLN B 81  ? 0.5855 0.6026 0.6403 0.0228  0.1270  0.0862  81  GLN B CD  
3862  O OE1 . GLN B 81  ? 0.6031 0.6047 0.6552 0.0308  0.1276  0.0752  81  GLN B OE1 
3863  N NE2 . GLN B 81  ? 0.5851 0.6061 0.6357 0.0289  0.1258  0.0917  81  GLN B NE2 
3864  N N   . GLU B 82  ? 0.5252 0.4851 0.6054 -0.0472 0.1172  0.0958  82  GLU B N   
3865  C CA  . GLU B 82  ? 0.5319 0.4645 0.6142 -0.0574 0.1141  0.0903  82  GLU B CA  
3866  C C   . GLU B 82  ? 0.5355 0.4866 0.6165 -0.0769 0.1120  0.0973  82  GLU B C   
3867  O O   . GLU B 82  ? 0.5358 0.4856 0.6179 -0.0813 0.1125  0.0903  82  GLU B O   
3868  C CB  . GLU B 82  ? 0.5506 0.4415 0.6327 -0.0609 0.1081  0.0915  82  GLU B CB  
3869  C CG  . GLU B 82  ? 0.5607 0.4252 0.6457 -0.0446 0.1093  0.0791  82  GLU B CG  
3870  C CD  . GLU B 82  ? 0.5874 0.4384 0.6746 -0.0433 0.1100  0.0660  82  GLU B CD  
3871  O OE1 . GLU B 82  ? 0.6098 0.4533 0.6952 -0.0572 0.1065  0.0667  82  GLU B OE1 
3872  O OE2 . GLU B 82  ? 0.5756 0.4234 0.6653 -0.0294 0.1135  0.0555  82  GLU B OE2 
3873  N N   . LEU B 83  ? 0.5418 0.5121 0.6201 -0.0898 0.1094  0.1119  83  LEU B N   
3874  C CA  . LEU B 83  ? 0.5542 0.5458 0.6305 -0.1110 0.1067  0.1203  83  LEU B CA  
3875  C C   . LEU B 83  ? 0.5349 0.5652 0.6132 -0.1055 0.1127  0.1144  83  LEU B C   
3876  O O   . LEU B 83  ? 0.5422 0.5740 0.6205 -0.1183 0.1111  0.1126  83  LEU B O   
3877  C CB  . LEU B 83  ? 0.5702 0.5863 0.6430 -0.1256 0.1035  0.1382  83  LEU B CB  
3878  C CG  . LEU B 83  ? 0.6057 0.5837 0.6731 -0.1420 0.0943  0.1485  83  LEU B CG  
3879  C CD1 . LEU B 83  ? 0.6422 0.6390 0.7037 -0.1721 0.0880  0.1641  83  LEU B CD1 
3880  C CD2 . LEU B 83  ? 0.6224 0.5431 0.6884 -0.1386 0.0897  0.1373  83  LEU B CD2 
3881  N N   . ASP B 84  ? 0.5152 0.5743 0.5936 -0.0859 0.1188  0.1109  84  ASP B N   
3882  C CA  . ASP B 84  ? 0.5049 0.6013 0.5829 -0.0770 0.1240  0.1050  84  ASP B CA  
3883  C C   . ASP B 84  ? 0.4899 0.5641 0.5700 -0.0717 0.1254  0.0909  84  ASP B C   
3884  O O   . ASP B 84  ? 0.4873 0.5785 0.5682 -0.0806 0.1259  0.0895  84  ASP B O   
3885  C CB  . ASP B 84  ? 0.4984 0.6202 0.5722 -0.0540 0.1285  0.1026  84  ASP B CB  
3886  C CG  . ASP B 84  ? 0.5442 0.7027 0.6154 -0.0581 0.1281  0.1164  84  ASP B CG  
3887  O OD1 . ASP B 84  ? 0.6024 0.7791 0.6753 -0.0807 0.1251  0.1288  84  ASP B OD1 
3888  O OD2 . ASP B 84  ? 0.5780 0.7476 0.6445 -0.0398 0.1303  0.1153  84  ASP B OD2 
3889  N N   . LYS B 85  ? 0.4769 0.5157 0.5577 -0.0579 0.1260  0.0809  85  LYS B N   
3890  C CA  . LYS B 85  ? 0.4671 0.4797 0.5502 -0.0546 0.1265  0.0682  85  LYS B CA  
3891  C C   . LYS B 85  ? 0.4767 0.4827 0.5617 -0.0754 0.1228  0.0701  85  LYS B C   
3892  O O   . LYS B 85  ? 0.4702 0.4928 0.5557 -0.0786 0.1246  0.0657  85  LYS B O   
3893  C CB  . LYS B 85  ? 0.4693 0.4411 0.5540 -0.0462 0.1249  0.0622  85  LYS B CB  
3894  C CG  . LYS B 85  ? 0.4616 0.4159 0.5474 -0.0349 0.1271  0.0483  85  LYS B CG  
3895  C CD  . LYS B 85  ? 0.4756 0.3930 0.5641 -0.0319 0.1245  0.0435  85  LYS B CD  
3896  C CE  . LYS B 85  ? 0.5219 0.4166 0.6121 -0.0468 0.1196  0.0445  85  LYS B CE  
3897  N NZ  . LYS B 85  ? 0.5652 0.4261 0.6570 -0.0401 0.1169  0.0387  85  LYS B NZ  
3898  N N   . TYR B 86  ? 0.4929 0.4736 0.5772 -0.0897 0.1169  0.0771  86  TYR B N   
3899  C CA  . TYR B 86  ? 0.5093 0.4743 0.5917 -0.1105 0.1111  0.0790  86  TYR B CA  
3900  C C   . TYR B 86  ? 0.5059 0.5117 0.5871 -0.1262 0.1114  0.0869  86  TYR B C   
3901  O O   . TYR B 86  ? 0.5069 0.5161 0.5885 -0.1327 0.1113  0.0811  86  TYR B O   
3902  C CB  . TYR B 86  ? 0.5354 0.4675 0.6132 -0.1237 0.1030  0.0878  86  TYR B CB  
3903  C CG  . TYR B 86  ? 0.5647 0.4802 0.6365 -0.1470 0.0954  0.0909  86  TYR B CG  
3904  C CD1 . TYR B 86  ? 0.5832 0.4767 0.6545 -0.1468 0.0943  0.0781  86  TYR B CD1 
3905  C CD2 . TYR B 86  ? 0.5832 0.5051 0.6484 -0.1702 0.0887  0.1069  86  TYR B CD2 
3906  C CE1 . TYR B 86  ? 0.6141 0.4894 0.6776 -0.1685 0.0862  0.0804  86  TYR B CE1 
3907  C CE2 . TYR B 86  ? 0.6143 0.5174 0.6711 -0.1939 0.0800  0.1105  86  TYR B CE2 
3908  C CZ  . TYR B 86  ? 0.6377 0.5162 0.6932 -0.1927 0.0786  0.0968  86  TYR B CZ  
3909  O OH  . TYR B 86  ? 0.6691 0.5262 0.7140 -0.2164 0.0690  0.0998  86  TYR B OH  
3910  N N   . LYS B 87  ? 0.5062 0.5453 0.5860 -0.1325 0.1114  0.1004  87  LYS B N   
3911  C CA  . LYS B 87  ? 0.5135 0.5989 0.5922 -0.1487 0.1113  0.1099  87  LYS B CA  
3912  C C   . LYS B 87  ? 0.4898 0.6043 0.5712 -0.1377 0.1174  0.1001  87  LYS B C   
3913  O O   . LYS B 87  ? 0.4996 0.6359 0.5807 -0.1528 0.1162  0.1023  87  LYS B O   
3914  C CB  . LYS B 87  ? 0.5137 0.6423 0.5913 -0.1491 0.1129  0.1237  87  LYS B CB  
3915  C CG  . LYS B 87  ? 0.5527 0.6654 0.6262 -0.1677 0.1058  0.1384  87  LYS B CG  
3916  C CD  . LYS B 87  ? 0.5790 0.7412 0.6519 -0.1664 0.1083  0.1514  87  LYS B CD  
3917  C CE  . LYS B 87  ? 0.6006 0.7372 0.6705 -0.1710 0.1035  0.1611  87  LYS B CE  
3918  N NZ  . LYS B 87  ? 0.6251 0.8064 0.6919 -0.1897 0.1010  0.1802  87  LYS B NZ  
3919  N N   . ASN B 88  ? 0.4613 0.5758 0.5442 -0.1120 0.1232  0.0898  88  ASN B N   
3920  C CA  . ASN B 88  ? 0.4388 0.5800 0.5220 -0.0995 0.1283  0.0812  88  ASN B CA  
3921  C C   . ASN B 88  ? 0.4315 0.5473 0.5168 -0.1050 0.1273  0.0705  88  ASN B C   
3922  O O   . ASN B 88  ? 0.4293 0.5713 0.5150 -0.1134 0.1279  0.0703  88  ASN B O   
3923  C CB  . ASN B 88  ? 0.4304 0.5721 0.5112 -0.0721 0.1328  0.0739  88  ASN B CB  
3924  C CG  . ASN B 88  ? 0.4278 0.5771 0.5068 -0.0572 0.1365  0.0622  88  ASN B CG  
3925  O OD1 . ASN B 88  ? 0.4343 0.6254 0.5102 -0.0511 0.1390  0.0634  88  ASN B OD1 
3926  N ND2 . ASN B 88  ? 0.4454 0.5558 0.5255 -0.0502 0.1366  0.0508  88  ASN B ND2 
3927  N N   . ALA B 89  ? 0.4241 0.4920 0.5107 -0.1002 0.1257  0.0616  89  ALA B N   
3928  C CA  . ALA B 89  ? 0.4208 0.4629 0.5087 -0.1065 0.1239  0.0517  89  ALA B CA  
3929  C C   . ALA B 89  ? 0.4304 0.4874 0.5167 -0.1312 0.1197  0.0584  89  ALA B C   
3930  O O   . ALA B 89  ? 0.4271 0.4941 0.5140 -0.1351 0.1206  0.0522  89  ALA B O   
3931  C CB  . ALA B 89  ? 0.4326 0.4238 0.5206 -0.1056 0.1199  0.0465  89  ALA B CB  
3932  N N   . VAL B 90  ? 0.4400 0.4996 0.5232 -0.1488 0.1145  0.0719  90  VAL B N   
3933  C CA  . VAL B 90  ? 0.4544 0.5215 0.5333 -0.1769 0.1081  0.0808  90  VAL B CA  
3934  C C   . VAL B 90  ? 0.4422 0.5683 0.5231 -0.1811 0.1122  0.0852  90  VAL B C   
3935  O O   . VAL B 90  ? 0.4523 0.5862 0.5319 -0.1960 0.1099  0.0839  90  VAL B O   
3936  C CB  . VAL B 90  ? 0.4741 0.5304 0.5476 -0.1946 0.1011  0.0960  90  VAL B CB  
3937  C CG1 . VAL B 90  ? 0.4944 0.5709 0.5621 -0.2257 0.0944  0.1087  90  VAL B CG1 
3938  C CG2 . VAL B 90  ? 0.4938 0.4866 0.5631 -0.1930 0.0949  0.0907  90  VAL B CG2 
3939  N N   . THR B 91  ? 0.4264 0.5947 0.5094 -0.1665 0.1181  0.0897  91  THR B N   
3940  C CA  . THR B 91  ? 0.4193 0.6476 0.5033 -0.1665 0.1220  0.0931  91  THR B CA  
3941  C C   . THR B 91  ? 0.4115 0.6387 0.4975 -0.1549 0.1258  0.0790  91  THR B C   
3942  O O   . THR B 91  ? 0.4144 0.6679 0.5006 -0.1675 0.1252  0.0798  91  THR B O   
3943  C CB  . THR B 91  ? 0.4011 0.6710 0.4850 -0.1471 0.1274  0.0976  91  THR B CB  
3944  O OG1 . THR B 91  ? 0.4128 0.6716 0.4952 -0.1530 0.1243  0.1081  91  THR B OG1 
3945  C CG2 . THR B 91  ? 0.4056 0.7436 0.4891 -0.1538 0.1292  0.1061  91  THR B CG2 
3946  N N   . GLU B 92  ? 0.4068 0.6030 0.4938 -0.1321 0.1291  0.0664  92  GLU B N   
3947  C CA  . GLU B 92  ? 0.4027 0.5937 0.4907 -0.1205 0.1323  0.0530  92  GLU B CA  
3948  C C   . GLU B 92  ? 0.4114 0.5885 0.5001 -0.1410 0.1285  0.0497  92  GLU B C   
3949  O O   . GLU B 92  ? 0.4011 0.6053 0.4904 -0.1417 0.1305  0.0460  92  GLU B O   
3950  C CB  . GLU B 92  ? 0.3990 0.5488 0.4871 -0.0996 0.1344  0.0414  92  GLU B CB  
3951  C CG  . GLU B 92  ? 0.4154 0.5840 0.4997 -0.0734 0.1392  0.0383  92  GLU B CG  
3952  C CD  . GLU B 92  ? 0.4562 0.6670 0.5377 -0.0652 0.1423  0.0361  92  GLU B CD  
3953  O OE1 . GLU B 92  ? 0.4752 0.6889 0.5589 -0.0738 0.1422  0.0312  92  GLU B OE1 
3954  O OE2 . GLU B 92  ? 0.4622 0.7040 0.5383 -0.0491 0.1445  0.0391  92  GLU B OE2 
3955  N N   . LEU B 93  ? 0.4304 0.5637 0.5177 -0.1562 0.1223  0.0504  93  LEU B N   
3956  C CA  . LEU B 93  ? 0.4493 0.5618 0.5344 -0.1750 0.1170  0.0461  93  LEU B CA  
3957  C C   . LEU B 93  ? 0.4663 0.6210 0.5492 -0.1985 0.1142  0.0580  93  LEU B C   
3958  O O   . LEU B 93  ? 0.4736 0.6417 0.5560 -0.2087 0.1134  0.0543  93  LEU B O   
3959  C CB  . LEU B 93  ? 0.4684 0.5238 0.5489 -0.1848 0.1094  0.0449  93  LEU B CB  
3960  C CG  . LEU B 93  ? 0.4562 0.4677 0.5386 -0.1647 0.1109  0.0319  93  LEU B CG  
3961  C CD1 . LEU B 93  ? 0.4872 0.4512 0.5636 -0.1732 0.1029  0.0342  93  LEU B CD1 
3962  C CD2 . LEU B 93  ? 0.4436 0.4428 0.5271 -0.1591 0.1123  0.0173  93  LEU B CD2 
3963  N N   . GLN B 94  ? 0.4763 0.6563 0.5579 -0.2075 0.1127  0.0727  94  GLN B N   
3964  C CA  . GLN B 94  ? 0.4981 0.7223 0.5772 -0.2324 0.1093  0.0860  94  GLN B CA  
3965  C C   . GLN B 94  ? 0.4828 0.7560 0.5655 -0.2258 0.1150  0.0817  94  GLN B C   
3966  O O   . GLN B 94  ? 0.4982 0.7942 0.5789 -0.2477 0.1114  0.0861  94  GLN B O   
3967  C CB  . GLN B 94  ? 0.4995 0.7595 0.5782 -0.2362 0.1096  0.1017  94  GLN B CB  
3968  C CG  . GLN B 94  ? 0.5516 0.7966 0.6231 -0.2683 0.0997  0.1163  94  GLN B CG  
3969  C CD  . GLN B 94  ? 0.5938 0.8527 0.6651 -0.2658 0.1000  0.1287  94  GLN B CD  
3970  O OE1 . GLN B 94  ? 0.5956 0.9138 0.6708 -0.2560 0.1060  0.1352  94  GLN B OE1 
3971  N NE2 . GLN B 94  ? 0.6339 0.8390 0.7000 -0.2725 0.0934  0.1315  94  GLN B NE2 
3972  N N   . LEU B 95  ? 0.4625 0.7508 0.5492 -0.1958 0.1230  0.0731  95  LEU B N   
3973  C CA  . LEU B 95  ? 0.4555 0.7960 0.5439 -0.1858 0.1282  0.0706  95  LEU B CA  
3974  C C   . LEU B 95  ? 0.4716 0.7940 0.5607 -0.1880 0.1280  0.0584  95  LEU B C   
3975  O O   . LEU B 95  ? 0.4685 0.8316 0.5586 -0.1841 0.1311  0.0563  95  LEU B O   
3976  C CB  . LEU B 95  ? 0.4290 0.7895 0.5175 -0.1523 0.1352  0.0663  95  LEU B CB  
3977  C CG  . LEU B 95  ? 0.4111 0.7902 0.4982 -0.1481 0.1355  0.0773  95  LEU B CG  
3978  C CD1 . LEU B 95  ? 0.3784 0.7457 0.4630 -0.1156 0.1400  0.0697  95  LEU B CD1 
3979  C CD2 . LEU B 95  ? 0.3928 0.8430 0.4794 -0.1563 0.1363  0.0896  95  LEU B CD2 
3980  N N   . LEU B 96  ? 0.5010 0.7645 0.5891 -0.1944 0.1239  0.0505  96  LEU B N   
3981  C CA  . LEU B 96  ? 0.5199 0.7637 0.6082 -0.1951 0.1237  0.0379  96  LEU B CA  
3982  C C   . LEU B 96  ? 0.5579 0.8191 0.6434 -0.2233 0.1183  0.0424  96  LEU B C   
3983  O O   . LEU B 96  ? 0.5590 0.8218 0.6451 -0.2238 0.1191  0.0332  96  LEU B O   
3984  C CB  . LEU B 96  ? 0.5266 0.7053 0.6139 -0.1906 0.1209  0.0274  96  LEU B CB  
3985  C CG  . LEU B 96  ? 0.5017 0.6661 0.5921 -0.1606 0.1271  0.0192  96  LEU B CG  
3986  C CD1 . LEU B 96  ? 0.4998 0.6130 0.5902 -0.1550 0.1256  0.0060  96  LEU B CD1 
3987  C CD2 . LEU B 96  ? 0.4780 0.6836 0.5699 -0.1416 0.1339  0.0156  96  LEU B CD2 
3988  N N   . MET B 97  ? 0.6038 0.8798 0.6857 -0.2479 0.1126  0.0572  97  MET B N   
3989  C CA  . MET B 97  ? 0.6587 0.9393 0.7344 -0.2817 0.1043  0.0637  97  MET B CA  
3990  C C   . MET B 97  ? 0.6645 1.0091 0.7426 -0.2896 0.1069  0.0673  97  MET B C   
3991  O O   . MET B 97  ? 0.6903 1.0329 0.7639 -0.3120 0.1013  0.0663  97  MET B O   
3992  C CB  . MET B 97  ? 0.6869 0.9576 0.7557 -0.3071 0.0959  0.0796  97  MET B CB  
3993  C CG  . MET B 97  ? 0.7382 0.9426 0.8036 -0.2988 0.0925  0.0752  97  MET B CG  
3994  S SD  . MET B 97  ? 0.8435 0.9686 0.9016 -0.2993 0.0858  0.0576  97  MET B SD  
3995  C CE  . MET B 97  ? 0.7784 0.9247 0.8407 -0.2932 0.0906  0.0435  97  MET B CE  
3996  N N   . GLN B 98  ? 0.6553 1.0559 0.7391 -0.2699 0.1149  0.0709  98  GLN B N   
3997  C CA  . GLN B 98  ? 0.6610 1.1306 0.7471 -0.2737 0.1179  0.0751  98  GLN B CA  
3998  C C   . GLN B 98  ? 0.6303 1.1246 0.7209 -0.2368 0.1273  0.0643  98  GLN B C   
3999  O O   . GLN B 98  ? 0.6122 1.0677 0.7036 -0.2114 0.1310  0.0535  98  GLN B O   
4000  C CB  . GLN B 98  ? 0.6746 1.2065 0.7598 -0.2930 0.1158  0.0948  98  GLN B CB  
4001  C CG  . GLN B 98  ? 0.7189 1.2239 0.7978 -0.3235 0.1065  0.1091  98  GLN B CG  
4002  C CD  . GLN B 98  ? 0.7309 1.2036 0.8106 -0.3058 0.1084  0.1103  98  GLN B CD  
4003  O OE1 . GLN B 98  ? 0.7062 1.1307 0.7878 -0.2810 0.1119  0.0969  98  GLN B OE1 
4004  N NE2 . GLN B 98  ? 0.7389 1.2405 0.8165 -0.3206 0.1055  0.1271  98  GLN B NE2 
4005  N N   . ILE B 139 ? 1.0104 1.8276 0.8449 0.2779  -0.1824 0.8851  148 ILE B N   
4006  C CA  . ILE B 139 ? 1.0332 1.8761 0.8594 0.2862  -0.1913 0.9047  148 ILE B CA  
4007  C C   . ILE B 139 ? 1.0217 1.9128 0.8435 0.2660  -0.1869 0.9130  148 ILE B C   
4008  O O   . ILE B 139 ? 1.0500 1.9491 0.8598 0.2642  -0.1953 0.9376  148 ILE B O   
4009  C CB  . ILE B 139 ? 1.0234 1.8987 0.8586 0.3100  -0.1927 0.8936  148 ILE B CB  
4010  C CG1 . ILE B 139 ? 1.0273 1.8665 0.8693 0.3311  -0.1948 0.8803  148 ILE B CG1 
4011  C CG2 . ILE B 139 ? 1.0542 1.9491 0.8789 0.3212  -0.2039 0.9170  148 ILE B CG2 
4012  C CD1 . ILE B 139 ? 1.0176 1.8946 0.8689 0.3538  -0.1962 0.8699  148 ILE B CD1 
4013  N N   . ALA B 140 ? 0.9827 1.9058 0.8126 0.2522  -0.1744 0.8927  149 ALA B N   
4014  C CA  . ALA B 140 ? 0.9695 1.9436 0.7949 0.2359  -0.1696 0.8962  149 ALA B CA  
4015  C C   . ALA B 140 ? 0.9578 1.9871 0.7852 0.2437  -0.1697 0.8918  149 ALA B C   
4016  O O   . ALA B 140 ? 0.9757 2.0302 0.7940 0.2410  -0.1752 0.9118  149 ALA B O   
4017  C CB  . ALA B 140 ? 1.0023 1.9669 0.8130 0.2218  -0.1764 0.9268  149 ALA B CB  
4018  N N   . SER B 141 ? 0.9298 1.9793 0.7678 0.2516  -0.1643 0.8671  150 SER B N   
4019  C CA  . SER B 141 ? 0.9186 2.0239 0.7570 0.2554  -0.1645 0.8624  150 SER B CA  
4020  C C   . SER B 141 ? 0.8904 2.0177 0.7391 0.2616  -0.1598 0.8357  150 SER B C   
4021  O O   . SER B 141 ? 0.8760 1.9771 0.7329 0.2636  -0.1555 0.8184  150 SER B O   
4022  C CB  . SER B 141 ? 0.9494 2.0638 0.7820 0.2684  -0.1756 0.8871  150 SER B CB  
4023  O OG  . SER B 141 ? 0.9651 2.0466 0.8026 0.2887  -0.1821 0.8890  150 SER B OG  
4024  N N   . GLY B 142 ? 0.8846 2.0617 0.7316 0.2631  -0.1613 0.8340  151 GLY B N   
4025  C CA  . GLY B 142 ? 0.8609 2.0693 0.7141 0.2646  -0.1583 0.8112  151 GLY B CA  
4026  C C   . GLY B 142 ? 0.8352 2.0479 0.6861 0.2482  -0.1495 0.7873  151 GLY B C   
4027  O O   . GLY B 142 ? 0.8239 2.0016 0.6802 0.2457  -0.1446 0.7737  151 GLY B O   
4028  N N   . VAL B 143 ? 0.8278 2.0819 0.6695 0.2383  -0.1482 0.7812  152 VAL B N   
4029  C CA  . VAL B 143 ? 0.8104 2.0675 0.6441 0.2234  -0.1411 0.7604  152 VAL B CA  
4030  C C   . VAL B 143 ? 0.7968 2.0100 0.6364 0.2202  -0.1349 0.7439  152 VAL B C   
4031  O O   . VAL B 143 ? 0.7852 1.9849 0.6332 0.2237  -0.1341 0.7286  152 VAL B O   
4032  C CB  . VAL B 143 ? 0.8003 2.1004 0.6245 0.2165  -0.1415 0.7429  152 VAL B CB  
4033  C CG1 . VAL B 143 ? 0.7821 2.0697 0.6089 0.2120  -0.1388 0.7154  152 VAL B CG1 
4034  C CG2 . VAL B 143 ? 0.8016 2.1217 0.6100 0.2060  -0.1386 0.7405  152 VAL B CG2 
4035  N N   . ALA B 144 ? 0.7992 1.9942 0.6339 0.2129  -0.1308 0.7485  153 ALA B N   
4036  C CA  . ALA B 144 ? 0.7925 1.9435 0.6329 0.2108  -0.1259 0.7413  153 ALA B CA  
4037  C C   . ALA B 144 ? 0.7754 1.9266 0.6079 0.2001  -0.1189 0.7179  153 ALA B C   
4038  O O   . ALA B 144 ? 0.7652 1.8834 0.6023 0.1981  -0.1143 0.7054  153 ALA B O   
4039  C CB  . ALA B 144 ? 0.8113 1.9403 0.6512 0.2099  -0.1275 0.7657  153 ALA B CB  
4040  N N   . VAL B 145 ? 0.7742 1.9623 0.5935 0.1945  -0.1187 0.7114  154 VAL B N   
4041  C CA  . VAL B 145 ? 0.7631 1.9527 0.5708 0.1870  -0.1136 0.6886  154 VAL B CA  
4042  C C   . VAL B 145 ? 0.7497 1.9149 0.5627 0.1873  -0.1126 0.6669  154 VAL B C   
4043  O O   . VAL B 145 ? 0.7404 1.8852 0.5487 0.1828  -0.1081 0.6485  154 VAL B O   
4044  C CB  . VAL B 145 ? 0.7657 1.9967 0.5570 0.1839  -0.1160 0.6792  154 VAL B CB  
4045  C CG1 . VAL B 145 ? 0.7657 2.0051 0.5422 0.1792  -0.1114 0.6704  154 VAL B CG1 
4046  C CG2 . VAL B 145 ? 0.7791 2.0470 0.5703 0.1875  -0.1218 0.7010  154 VAL B CG2 
4047  N N   . SER B 146 ? 0.7499 1.9201 0.5722 0.1928  -0.1172 0.6698  155 SER B N   
4048  C CA  . SER B 146 ? 0.7382 1.8942 0.5659 0.1922  -0.1175 0.6509  155 SER B CA  
4049  C C   . SER B 146 ? 0.7303 1.8413 0.5680 0.1933  -0.1123 0.6464  155 SER B C   
4050  O O   . SER B 146 ? 0.7213 1.8140 0.5524 0.1867  -0.1081 0.6278  155 SER B O   
4051  C CB  . SER B 146 ? 0.7417 1.9170 0.5797 0.2000  -0.1233 0.6599  155 SER B CB  
4052  O OG  . SER B 146 ? 0.7546 1.9657 0.5879 0.2031  -0.1278 0.6775  155 SER B OG  
4053  N N   . LYS B 147 ? 0.7367 1.8284 0.5878 0.2021  -0.1133 0.6639  156 LYS B N   
4054  C CA  . LYS B 147 ? 0.7325 1.7796 0.5932 0.2041  -0.1093 0.6623  156 LYS B CA  
4055  C C   . LYS B 147 ? 0.7243 1.7535 0.5773 0.1946  -0.1028 0.6500  156 LYS B C   
4056  O O   . LYS B 147 ? 0.7127 1.7137 0.5696 0.1925  -0.0989 0.6342  156 LYS B O   
4057  C CB  . LYS B 147 ? 0.7499 1.7795 0.6177 0.2125  -0.1124 0.6878  156 LYS B CB  
4058  C CG  . LYS B 147 ? 0.7629 1.8147 0.6347 0.2240  -0.1197 0.7028  156 LYS B CG  
4059  C CD  . LYS B 147 ? 0.7875 1.8276 0.6587 0.2305  -0.1248 0.7307  156 LYS B CD  
4060  C CE  . LYS B 147 ? 0.7970 1.7873 0.6759 0.2381  -0.1258 0.7364  156 LYS B CE  
4061  N NZ  . LYS B 147 ? 0.7863 1.7669 0.6761 0.2483  -0.1256 0.7211  156 LYS B NZ  
4062  N N   . VAL B 148 ? 0.7308 1.7797 0.5725 0.1895  -0.1017 0.6571  157 VAL B N   
4063  C CA  . VAL B 148 ? 0.7249 1.7652 0.5577 0.1824  -0.0958 0.6463  157 VAL B CA  
4064  C C   . VAL B 148 ? 0.7109 1.7380 0.5381 0.1789  -0.0931 0.6173  157 VAL B C   
4065  O O   . VAL B 148 ? 0.7026 1.6987 0.5328 0.1770  -0.0884 0.6072  157 VAL B O   
4066  C CB  . VAL B 148 ? 0.7337 1.8112 0.5522 0.1786  -0.0958 0.6543  157 VAL B CB  
4067  C CG1 . VAL B 148 ? 0.7276 1.8052 0.5334 0.1737  -0.0902 0.6376  157 VAL B CG1 
4068  C CG2 . VAL B 148 ? 0.7486 1.8298 0.5719 0.1787  -0.0977 0.6837  157 VAL B CG2 
4069  N N   . LEU B 149 ? 0.7104 1.7593 0.5285 0.1775  -0.0970 0.6047  158 LEU B N   
4070  C CA  . LEU B 149 ? 0.7033 1.7404 0.5101 0.1722  -0.0964 0.5779  158 LEU B CA  
4071  C C   . LEU B 149 ? 0.6928 1.6994 0.5122 0.1720  -0.0957 0.5685  158 LEU B C   
4072  O O   . LEU B 149 ? 0.6861 1.6686 0.4997 0.1675  -0.0934 0.5491  158 LEU B O   
4073  C CB  . LEU B 149 ? 0.7105 1.7784 0.5012 0.1687  -0.1023 0.5686  158 LEU B CB  
4074  C CG  . LEU B 149 ? 0.7217 1.8244 0.5008 0.1702  -0.1033 0.5797  158 LEU B CG  
4075  C CD1 . LEU B 149 ? 0.7286 1.8652 0.5103 0.1716  -0.1094 0.5925  158 LEU B CD1 
4076  C CD2 . LEU B 149 ? 0.7278 1.8358 0.4821 0.1674  -0.1034 0.5594  158 LEU B CD2 
4077  N N   . HIS B 150 ? 0.6938 1.7024 0.5298 0.1778  -0.0981 0.5824  159 HIS B N   
4078  C CA  . HIS B 150 ? 0.7028 1.6864 0.5525 0.1798  -0.0973 0.5755  159 HIS B CA  
4079  C C   . HIS B 150 ? 0.6987 1.6437 0.5568 0.1818  -0.0915 0.5771  159 HIS B C   
4080  O O   . HIS B 150 ? 0.6914 1.6100 0.5551 0.1802  -0.0890 0.5636  159 HIS B O   
4081  C CB  . HIS B 150 ? 0.7151 1.7145 0.5790 0.1886  -0.1019 0.5894  159 HIS B CB  
4082  C CG  . HIS B 150 ? 0.7354 1.7079 0.6153 0.1949  -0.1004 0.5875  159 HIS B CG  
4083  N ND1 . HIS B 150 ? 0.7708 1.7248 0.6631 0.2067  -0.1004 0.6045  159 HIS B ND1 
4084  C CD2 . HIS B 150 ? 0.7444 1.7040 0.6283 0.1911  -0.0993 0.5705  159 HIS B CD2 
4085  C CE1 . HIS B 150 ? 0.7772 1.7096 0.6808 0.2114  -0.0991 0.5972  159 HIS B CE1 
4086  N NE2 . HIS B 150 ? 0.7657 1.7031 0.6654 0.2017  -0.0980 0.5770  159 HIS B NE2 
4087  N N   . LEU B 151 ? 0.7037 1.6477 0.5618 0.1839  -0.0897 0.5941  160 LEU B N   
4088  C CA  . LEU B 151 ? 0.6933 1.6052 0.5563 0.1833  -0.0846 0.5981  160 LEU B CA  
4089  C C   . LEU B 151 ? 0.6885 1.5940 0.5393 0.1762  -0.0797 0.5809  160 LEU B C   
4090  O O   . LEU B 151 ? 0.6798 1.5565 0.5347 0.1746  -0.0751 0.5759  160 LEU B O   
4091  C CB  . LEU B 151 ? 0.7005 1.6179 0.5648 0.1850  -0.0859 0.6235  160 LEU B CB  
4092  C CG  . LEU B 151 ? 0.7106 1.6068 0.5879 0.1935  -0.0897 0.6411  160 LEU B CG  
4093  C CD1 . LEU B 151 ? 0.7173 1.6389 0.5974 0.2018  -0.0960 0.6483  160 LEU B CD1 
4094  C CD2 . LEU B 151 ? 0.7267 1.6142 0.6020 0.1908  -0.0904 0.6635  160 LEU B CD2 
4095  N N   . GLU B 152 ? 0.7010 1.6334 0.5356 0.1729  -0.0811 0.5716  161 GLU B N   
4096  C CA  . GLU B 152 ? 0.7174 1.6452 0.5367 0.1691  -0.0777 0.5534  161 GLU B CA  
4097  C C   . GLU B 152 ? 0.7175 1.6174 0.5345 0.1662  -0.0773 0.5298  161 GLU B C   
4098  O O   . GLU B 152 ? 0.7102 1.5880 0.5225 0.1649  -0.0730 0.5175  161 GLU B O   
4099  C CB  . GLU B 152 ? 0.7322 1.6957 0.5325 0.1684  -0.0810 0.5495  161 GLU B CB  
4100  C CG  . GLU B 152 ? 0.7545 1.7232 0.5362 0.1683  -0.0780 0.5365  161 GLU B CG  
4101  C CD  . GLU B 152 ? 0.8016 1.8092 0.5643 0.1695  -0.0820 0.5355  161 GLU B CD  
4102  O OE1 . GLU B 152 ? 0.8098 1.8420 0.5762 0.1695  -0.0864 0.5486  161 GLU B OE1 
4103  O OE2 . GLU B 152 ? 0.8213 1.8353 0.5646 0.1717  -0.0810 0.5209  161 GLU B OE2 
4104  N N   . GLY B 153 ? 0.7301 1.6335 0.5494 0.1646  -0.0821 0.5240  162 GLY B N   
4105  C CA  . GLY B 153 ? 0.7430 1.6205 0.5625 0.1601  -0.0824 0.5052  162 GLY B CA  
4106  C C   . GLY B 153 ? 0.7457 1.5931 0.5849 0.1634  -0.0776 0.5102  162 GLY B C   
4107  O O   . GLY B 153 ? 0.7386 1.5574 0.5769 0.1606  -0.0745 0.4960  162 GLY B O   
4108  N N   . GLU B 154 ? 0.7616 1.6139 0.6169 0.1700  -0.0778 0.5306  163 GLU B N   
4109  C CA  . GLU B 154 ? 0.7730 1.5957 0.6453 0.1747  -0.0746 0.5372  163 GLU B CA  
4110  C C   . GLU B 154 ? 0.7689 1.5682 0.6384 0.1721  -0.0687 0.5347  163 GLU B C   
4111  O O   . GLU B 154 ? 0.7625 1.5335 0.6356 0.1703  -0.0653 0.5225  163 GLU B O   
4112  C CB  . GLU B 154 ? 0.7909 1.6213 0.6752 0.1834  -0.0775 0.5608  163 GLU B CB  
4113  C CG  . GLU B 154 ? 0.8354 1.6490 0.7356 0.1915  -0.0790 0.5630  163 GLU B CG  
4114  C CD  . GLU B 154 ? 0.8955 1.7360 0.7980 0.1935  -0.0837 0.5573  163 GLU B CD  
4115  O OE1 . GLU B 154 ? 0.9122 1.7850 0.8111 0.1958  -0.0882 0.5676  163 GLU B OE1 
4116  O OE2 . GLU B 154 ? 0.9004 1.7321 0.8083 0.1920  -0.0830 0.5434  163 GLU B OE2 
4117  N N   . VAL B 155 ? 0.7785 1.5928 0.6412 0.1713  -0.0676 0.5464  164 VAL B N   
4118  C CA  . VAL B 155 ? 0.7782 1.5788 0.6369 0.1681  -0.0621 0.5446  164 VAL B CA  
4119  C C   . VAL B 155 ? 0.7744 1.5592 0.6240 0.1652  -0.0595 0.5192  164 VAL B C   
4120  O O   . VAL B 155 ? 0.7681 1.5251 0.6226 0.1641  -0.0552 0.5129  164 VAL B O   
4121  C CB  . VAL B 155 ? 0.7863 1.6182 0.6329 0.1664  -0.0618 0.5542  164 VAL B CB  
4122  C CG1 . VAL B 155 ? 0.7786 1.6071 0.6146 0.1638  -0.0563 0.5420  164 VAL B CG1 
4123  C CG2 . VAL B 155 ? 0.7951 1.6333 0.6504 0.1667  -0.0634 0.5818  164 VAL B CG2 
4124  N N   . ASN B 156 ? 0.7837 1.5842 0.6184 0.1637  -0.0631 0.5049  165 ASN B N   
4125  C CA  . ASN B 156 ? 0.7886 1.5743 0.6079 0.1610  -0.0625 0.4810  165 ASN B CA  
4126  C C   . ASN B 156 ? 0.7737 1.5258 0.6014 0.1584  -0.0614 0.4687  165 ASN B C   
4127  O O   . ASN B 156 ? 0.7686 1.4979 0.5892 0.1571  -0.0586 0.4537  165 ASN B O   
4128  C CB  . ASN B 156 ? 0.8062 1.6127 0.6042 0.1591  -0.0685 0.4692  165 ASN B CB  
4129  C CG  . ASN B 156 ? 0.8382 1.6489 0.6134 0.1616  -0.0675 0.4561  165 ASN B CG  
4130  O OD1 . ASN B 156 ? 0.8593 1.7008 0.6228 0.1647  -0.0690 0.4613  165 ASN B OD1 
4131  N ND2 . ASN B 156 ? 0.8562 1.6374 0.6248 0.1616  -0.0650 0.4392  165 ASN B ND2 
4132  N N   . LYS B 157 ? 0.7663 1.5178 0.6089 0.1585  -0.0639 0.4754  166 LYS B N   
4133  C CA  . LYS B 157 ? 0.7551 1.4789 0.6099 0.1574  -0.0623 0.4680  166 LYS B CA  
4134  C C   . LYS B 157 ? 0.7445 1.4427 0.6107 0.1603  -0.0560 0.4738  166 LYS B C   
4135  O O   . LYS B 157 ? 0.7388 1.4125 0.6018 0.1578  -0.0526 0.4601  166 LYS B O   
4136  C CB  . LYS B 157 ? 0.7565 1.4919 0.6260 0.1600  -0.0660 0.4770  166 LYS B CB  
4137  C CG  . LYS B 157 ? 0.7733 1.5211 0.6345 0.1529  -0.0717 0.4637  166 LYS B CG  
4138  C CD  . LYS B 157 ? 0.8062 1.5837 0.6776 0.1564  -0.0763 0.4758  166 LYS B CD  
4139  C CE  . LYS B 157 ? 0.8237 1.6217 0.6819 0.1462  -0.0831 0.4644  166 LYS B CE  
4140  N NZ  . LYS B 157 ? 0.8361 1.6728 0.6916 0.1481  -0.0881 0.4763  166 LYS B NZ  
4141  N N   . ILE B 158 ? 0.7440 1.4469 0.6216 0.1649  -0.0552 0.4944  167 ILE B N   
4142  C CA  . ILE B 158 ? 0.7398 1.4174 0.6273 0.1659  -0.0506 0.5020  167 ILE B CA  
4143  C C   . ILE B 158 ? 0.7387 1.4068 0.6158 0.1618  -0.0456 0.4905  167 ILE B C   
4144  O O   . ILE B 158 ? 0.7301 1.3705 0.6130 0.1607  -0.0419 0.4834  167 ILE B O   
4145  C CB  . ILE B 158 ? 0.7508 1.4360 0.6449 0.1691  -0.0522 0.5270  167 ILE B CB  
4146  C CG1 . ILE B 158 ? 0.7548 1.4352 0.6617 0.1765  -0.0567 0.5361  167 ILE B CG1 
4147  C CG2 . ILE B 158 ? 0.7431 1.4061 0.6415 0.1663  -0.0483 0.5357  167 ILE B CG2 
4148  C CD1 . ILE B 158 ? 0.7860 1.4723 0.6964 0.1809  -0.0606 0.5607  167 ILE B CD1 
4149  N N   . LYS B 159 ? 0.7482 1.4407 0.6094 0.1608  -0.0458 0.4878  168 LYS B N   
4150  C CA  . LYS B 159 ? 0.7522 1.4403 0.6015 0.1597  -0.0417 0.4757  168 LYS B CA  
4151  C C   . LYS B 159 ? 0.7434 1.4020 0.5906 0.1584  -0.0408 0.4545  168 LYS B C   
4152  O O   . LYS B 159 ? 0.7375 1.3727 0.5912 0.1576  -0.0364 0.4511  168 LYS B O   
4153  C CB  . LYS B 159 ? 0.7657 1.4840 0.5942 0.1614  -0.0436 0.4695  168 LYS B CB  
4154  C CG  . LYS B 159 ? 0.7924 1.5043 0.6051 0.1635  -0.0404 0.4518  168 LYS B CG  
4155  C CD  . LYS B 159 ? 0.8458 1.5826 0.6333 0.1679  -0.0438 0.4401  168 LYS B CD  
4156  C CE  . LYS B 159 ? 0.8587 1.5799 0.6278 0.1727  -0.0423 0.4177  168 LYS B CE  
4157  N NZ  . LYS B 159 ? 0.8826 1.6328 0.6277 0.1807  -0.0437 0.4105  168 LYS B NZ  
4158  N N   . SER B 160 ? 0.7475 1.4071 0.5851 0.1569  -0.0457 0.4410  169 SER B N   
4159  C CA  . SER B 160 ? 0.7470 1.3791 0.5787 0.1537  -0.0464 0.4206  169 SER B CA  
4160  C C   . SER B 160 ? 0.7344 1.3401 0.5864 0.1527  -0.0429 0.4228  169 SER B C   
4161  O O   . SER B 160 ? 0.7316 1.3120 0.5821 0.1515  -0.0397 0.4108  169 SER B O   
4162  C CB  . SER B 160 ? 0.7526 1.3912 0.5724 0.1491  -0.0537 0.4099  169 SER B CB  
4163  O OG  . SER B 160 ? 0.7815 1.4387 0.5786 0.1503  -0.0575 0.4041  169 SER B OG  
4164  N N   . ALA B 161 ? 0.7292 1.3407 0.5987 0.1547  -0.0439 0.4380  170 ALA B N   
4165  C CA  . ALA B 161 ? 0.7185 1.3064 0.6066 0.1562  -0.0413 0.4413  170 ALA B CA  
4166  C C   . ALA B 161 ? 0.7140 1.2811 0.6080 0.1570  -0.0355 0.4457  170 ALA B C   
4167  O O   . ALA B 161 ? 0.7048 1.2458 0.6053 0.1560  -0.0325 0.4373  170 ALA B O   
4168  C CB  . ALA B 161 ? 0.7231 1.3229 0.6253 0.1614  -0.0444 0.4576  170 ALA B CB  
4169  N N   . LEU B 162 ? 0.7185 1.2994 0.6100 0.1576  -0.0342 0.4594  171 LEU B N   
4170  C CA  . LEU B 162 ? 0.7170 1.2832 0.6128 0.1560  -0.0294 0.4652  171 LEU B CA  
4171  C C   . LEU B 162 ? 0.7120 1.2682 0.5972 0.1540  -0.0254 0.4467  171 LEU B C   
4172  O O   . LEU B 162 ? 0.7111 1.2447 0.6031 0.1525  -0.0214 0.4443  171 LEU B O   
4173  C CB  . LEU B 162 ? 0.7287 1.3173 0.6222 0.1548  -0.0296 0.4848  171 LEU B CB  
4174  C CG  . LEU B 162 ? 0.7291 1.3063 0.6259 0.1503  -0.0252 0.4925  171 LEU B CG  
4175  C CD1 . LEU B 162 ? 0.7379 1.2845 0.6497 0.1498  -0.0263 0.5035  171 LEU B CD1 
4176  C CD2 . LEU B 162 ? 0.7421 1.3493 0.6321 0.1465  -0.0249 0.5090  171 LEU B CD2 
4177  N N   . LEU B 163 ? 0.7154 1.2871 0.5824 0.1549  -0.0270 0.4335  172 LEU B N   
4178  C CA  . LEU B 163 ? 0.7150 1.2755 0.5682 0.1555  -0.0245 0.4146  172 LEU B CA  
4179  C C   . LEU B 163 ? 0.7057 1.2324 0.5650 0.1532  -0.0238 0.4011  172 LEU B C   
4180  O O   . LEU B 163 ? 0.6982 1.2062 0.5578 0.1531  -0.0197 0.3933  172 LEU B O   
4181  C CB  . LEU B 163 ? 0.7247 1.3008 0.5543 0.1581  -0.0290 0.4008  172 LEU B CB  
4182  C CG  . LEU B 163 ? 0.7386 1.3510 0.5582 0.1615  -0.0298 0.4104  172 LEU B CG  
4183  C CD1 . LEU B 163 ? 0.7701 1.3937 0.5689 0.1631  -0.0366 0.3982  172 LEU B CD1 
4184  C CD2 . LEU B 163 ? 0.7407 1.3634 0.5527 0.1654  -0.0249 0.4090  172 LEU B CD2 
4185  N N   . SER B 164 ? 0.7015 1.2243 0.5657 0.1512  -0.0281 0.3991  173 SER B N   
4186  C CA  . SER B 164 ? 0.6891 1.1863 0.5602 0.1482  -0.0283 0.3884  173 SER B CA  
4187  C C   . SER B 164 ? 0.6776 1.1553 0.5679 0.1493  -0.0231 0.3963  173 SER B C   
4188  O O   . SER B 164 ? 0.6715 1.1256 0.5632 0.1477  -0.0202 0.3855  173 SER B O   
4189  C CB  . SER B 164 ? 0.6897 1.1977 0.5659 0.1462  -0.0336 0.3906  173 SER B CB  
4190  O OG  . SER B 164 ? 0.6905 1.1860 0.5567 0.1401  -0.0371 0.3735  173 SER B OG  
4191  N N   . THR B 165 ? 0.6785 1.1641 0.5816 0.1518  -0.0227 0.4155  174 THR B N   
4192  C CA  . THR B 165 ? 0.6756 1.1402 0.5936 0.1525  -0.0192 0.4246  174 THR B CA  
4193  C C   . THR B 165 ? 0.6722 1.1286 0.5850 0.1497  -0.0141 0.4210  174 THR B C   
4194  O O   . THR B 165 ? 0.6660 1.0980 0.5857 0.1484  -0.0108 0.4158  174 THR B O   
4195  C CB  . THR B 165 ? 0.6887 1.1609 0.6161 0.1553  -0.0216 0.4472  174 THR B CB  
4196  O OG1 . THR B 165 ? 0.6905 1.1689 0.6246 0.1602  -0.0262 0.4500  174 THR B OG1 
4197  C CG2 . THR B 165 ? 0.6851 1.1313 0.6232 0.1545  -0.0194 0.4571  174 THR B CG2 
4198  N N   . ASN B 166 ? 0.6785 1.1580 0.5790 0.1494  -0.0134 0.4238  175 ASN B N   
4199  C CA  . ASN B 166 ? 0.6802 1.1595 0.5756 0.1478  -0.0087 0.4212  175 ASN B CA  
4200  C C   . ASN B 166 ? 0.6722 1.1290 0.5624 0.1484  -0.0064 0.4001  175 ASN B C   
4201  O O   . ASN B 166 ? 0.6661 1.1051 0.5633 0.1463  -0.0023 0.3990  175 ASN B O   
4202  C CB  . ASN B 166 ? 0.6895 1.2029 0.5701 0.1495  -0.0088 0.4243  175 ASN B CB  
4203  C CG  . ASN B 166 ? 0.7100 1.2441 0.5969 0.1463  -0.0098 0.4485  175 ASN B CG  
4204  O OD1 . ASN B 166 ? 0.7202 1.2391 0.6211 0.1436  -0.0114 0.4627  175 ASN B OD1 
4205  N ND2 . ASN B 166 ? 0.7317 1.3001 0.6070 0.1472  -0.0095 0.4536  175 ASN B ND2 
4206  N N   . LYS B 167 ? 0.6740 1.1301 0.5512 0.1503  -0.0099 0.3842  176 LYS B N   
4207  C CA  . LYS B 167 ? 0.6719 1.1041 0.5409 0.1501  -0.0096 0.3638  176 LYS B CA  
4208  C C   . LYS B 167 ? 0.6579 1.0628 0.5437 0.1468  -0.0080 0.3624  176 LYS B C   
4209  O O   . LYS B 167 ? 0.6550 1.0384 0.5384 0.1460  -0.0058 0.3497  176 LYS B O   
4210  C CB  . LYS B 167 ? 0.6830 1.1170 0.5337 0.1501  -0.0160 0.3501  176 LYS B CB  
4211  C CG  . LYS B 167 ? 0.7162 1.1699 0.5446 0.1553  -0.0181 0.3446  176 LYS B CG  
4212  C CD  . LYS B 167 ? 0.7573 1.2121 0.5678 0.1536  -0.0261 0.3342  176 LYS B CD  
4213  C CE  . LYS B 167 ? 0.7950 1.2540 0.5759 0.1606  -0.0294 0.3198  176 LYS B CE  
4214  N NZ  . LYS B 167 ? 0.8274 1.2914 0.5893 0.1584  -0.0383 0.3130  176 LYS B NZ  
4215  N N   . ALA B 168 ? 0.6503 1.0566 0.5516 0.1462  -0.0096 0.3747  177 ALA B N   
4216  C CA  . ALA B 168 ? 0.6369 1.0200 0.5546 0.1454  -0.0081 0.3746  177 ALA B CA  
4217  C C   . ALA B 168 ? 0.6311 0.9995 0.5578 0.1448  -0.0031 0.3812  177 ALA B C   
4218  O O   . ALA B 168 ? 0.6279 0.9734 0.5602 0.1435  -0.0006 0.3728  177 ALA B O   
4219  C CB  . ALA B 168 ? 0.6413 1.0315 0.5715 0.1479  -0.0114 0.3864  177 ALA B CB  
4220  N N   . VAL B 169 ? 0.6307 1.0130 0.5577 0.1443  -0.0022 0.3965  178 VAL B N   
4221  C CA  . VAL B 169 ? 0.6226 0.9926 0.5569 0.1410  0.0014  0.4051  178 VAL B CA  
4222  C C   . VAL B 169 ? 0.6183 0.9865 0.5437 0.1397  0.0059  0.3920  178 VAL B C   
4223  O O   . VAL B 169 ? 0.6173 0.9674 0.5492 0.1368  0.0093  0.3909  178 VAL B O   
4224  C CB  . VAL B 169 ? 0.6324 1.0188 0.5680 0.1384  0.0000  0.4269  178 VAL B CB  
4225  C CG1 . VAL B 169 ? 0.6285 1.0093 0.5663 0.1319  0.0034  0.4345  178 VAL B CG1 
4226  C CG2 . VAL B 169 ? 0.6371 1.0122 0.5835 0.1407  -0.0046 0.4403  178 VAL B CG2 
4227  N N   . VAL B 170 ? 0.6212 1.0073 0.5302 0.1428  0.0054  0.3813  179 VAL B N   
4228  C CA  . VAL B 170 ? 0.6216 1.0043 0.5187 0.1448  0.0085  0.3658  179 VAL B CA  
4229  C C   . VAL B 170 ? 0.6088 0.9599 0.5093 0.1440  0.0090  0.3506  179 VAL B C   
4230  O O   . VAL B 170 ? 0.6010 0.9379 0.5061 0.1426  0.0130  0.3470  179 VAL B O   
4231  C CB  . VAL B 170 ? 0.6328 1.0369 0.5076 0.1508  0.0060  0.3553  179 VAL B CB  
4232  C CG1 . VAL B 170 ? 0.6403 1.0291 0.4997 0.1553  0.0065  0.3341  179 VAL B CG1 
4233  C CG2 . VAL B 170 ? 0.6446 1.0838 0.5150 0.1522  0.0077  0.3684  179 VAL B CG2 
4234  N N   . SER B 171 ? 0.6062 0.9485 0.5047 0.1440  0.0049  0.3425  180 SER B N   
4235  C CA  . SER B 171 ? 0.6034 0.9188 0.5055 0.1418  0.0050  0.3298  180 SER B CA  
4236  C C   . SER B 171 ? 0.6007 0.8991 0.5218 0.1397  0.0093  0.3369  180 SER B C   
4237  O O   . SER B 171 ? 0.6043 0.8868 0.5250 0.1389  0.0127  0.3283  180 SER B O   
4238  C CB  . SER B 171 ? 0.6025 0.9162 0.5049 0.1396  -0.0001 0.3257  180 SER B CB  
4239  O OG  . SER B 171 ? 0.6071 0.9151 0.4888 0.1384  -0.0042 0.3092  180 SER B OG  
4240  N N   . LEU B 172 ? 0.6037 0.9038 0.5395 0.1394  0.0086  0.3524  181 LEU B N   
4241  C CA  . LEU B 172 ? 0.6023 0.8812 0.5536 0.1381  0.0111  0.3585  181 LEU B CA  
4242  C C   . LEU B 172 ? 0.6072 0.8828 0.5575 0.1346  0.0155  0.3614  181 LEU B C   
4243  O O   . LEU B 172 ? 0.6038 0.8586 0.5602 0.1327  0.0184  0.3560  181 LEU B O   
4244  C CB  . LEU B 172 ? 0.6084 0.8877 0.5710 0.1401  0.0079  0.3756  181 LEU B CB  
4245  C CG  . LEU B 172 ? 0.6016 0.8540 0.5780 0.1416  0.0080  0.3778  181 LEU B CG  
4246  C CD1 . LEU B 172 ? 0.6037 0.8493 0.5837 0.1444  0.0076  0.3634  181 LEU B CD1 
4247  C CD2 . LEU B 172 ? 0.6027 0.8511 0.5861 0.1452  0.0037  0.3957  181 LEU B CD2 
4248  N N   . SER B 173 ? 0.6162 0.9154 0.5586 0.1337  0.0160  0.3701  182 SER B N   
4249  C CA  . SER B 173 ? 0.6229 0.9271 0.5639 0.1297  0.0200  0.3738  182 SER B CA  
4250  C C   . SER B 173 ? 0.6197 0.9136 0.5542 0.1317  0.0235  0.3551  182 SER B C   
4251  O O   . SER B 173 ? 0.6184 0.8997 0.5589 0.1280  0.0268  0.3549  182 SER B O   
4252  C CB  . SER B 173 ? 0.6297 0.9687 0.5607 0.1295  0.0199  0.3834  182 SER B CB  
4253  O OG  . SER B 173 ? 0.6433 0.9893 0.5805 0.1262  0.0165  0.4030  182 SER B OG  
4254  N N   . ASN B 174 ? 0.6276 0.9248 0.5484 0.1372  0.0219  0.3395  183 ASN B N   
4255  C CA  . ASN B 174 ? 0.6319 0.9169 0.5421 0.1403  0.0236  0.3208  183 ASN B CA  
4256  C C   . ASN B 174 ? 0.6217 0.8756 0.5422 0.1374  0.0244  0.3129  183 ASN B C   
4257  O O   . ASN B 174 ? 0.6224 0.8632 0.5415 0.1374  0.0274  0.3035  183 ASN B O   
4258  C CB  . ASN B 174 ? 0.6443 0.9359 0.5333 0.1465  0.0194  0.3070  183 ASN B CB  
4259  C CG  . ASN B 174 ? 0.6799 1.0045 0.5560 0.1517  0.0190  0.3124  183 ASN B CG  
4260  O OD1 . ASN B 174 ? 0.7082 1.0515 0.5860 0.1521  0.0231  0.3198  183 ASN B OD1 
4261  N ND2 . ASN B 174 ? 0.6993 1.0340 0.5625 0.1550  0.0139  0.3092  183 ASN B ND2 
4262  N N   . GLY B 175 ? 0.6144 0.8593 0.5453 0.1355  0.0216  0.3170  184 GLY B N   
4263  C CA  . GLY B 175 ? 0.5995 0.8197 0.5431 0.1332  0.0224  0.3125  184 GLY B CA  
4264  C C   . GLY B 175 ? 0.5917 0.8003 0.5472 0.1303  0.0265  0.3197  184 GLY B C   
4265  O O   . GLY B 175 ? 0.5894 0.7815 0.5463 0.1291  0.0293  0.3100  184 GLY B O   
4266  N N   . VAL B 176 ? 0.5901 0.8064 0.5524 0.1283  0.0261  0.3371  185 VAL B N   
4267  C CA  . VAL B 176 ? 0.5858 0.7894 0.5571 0.1232  0.0283  0.3459  185 VAL B CA  
4268  C C   . VAL B 176 ? 0.5831 0.7951 0.5474 0.1205  0.0328  0.3408  185 VAL B C   
4269  O O   . VAL B 176 ? 0.5772 0.7727 0.5465 0.1174  0.0357  0.3362  185 VAL B O   
4270  C CB  . VAL B 176 ? 0.5976 0.8076 0.5731 0.1201  0.0252  0.3666  185 VAL B CB  
4271  C CG1 . VAL B 176 ? 0.6059 0.8074 0.5852 0.1116  0.0266  0.3774  185 VAL B CG1 
4272  C CG2 . VAL B 176 ? 0.5973 0.7923 0.5814 0.1247  0.0208  0.3709  185 VAL B CG2 
4273  N N   . SER B 177 ? 0.5863 0.8262 0.5383 0.1228  0.0333  0.3410  186 SER B N   
4274  C CA  . SER B 177 ? 0.5841 0.8386 0.5272 0.1235  0.0372  0.3350  186 SER B CA  
4275  C C   . SER B 177 ? 0.5723 0.8037 0.5142 0.1260  0.0393  0.3170  186 SER B C   
4276  O O   . SER B 177 ? 0.5737 0.8051 0.5161 0.1241  0.0430  0.3143  186 SER B O   
4277  C CB  . SER B 177 ? 0.5900 0.8749 0.5162 0.1306  0.0363  0.3310  186 SER B CB  
4278  O OG  . SER B 177 ? 0.5982 0.8991 0.5141 0.1346  0.0397  0.3233  186 SER B OG  
4279  N N   . VAL B 178 ? 0.5625 0.7758 0.5029 0.1293  0.0367  0.3055  187 VAL B N   
4280  C CA  . VAL B 178 ? 0.5524 0.7442 0.4897 0.1308  0.0378  0.2887  187 VAL B CA  
4281  C C   . VAL B 178 ? 0.5473 0.7150 0.5014 0.1256  0.0397  0.2906  187 VAL B C   
4282  O O   . VAL B 178 ? 0.5456 0.7029 0.5011 0.1242  0.0430  0.2842  187 VAL B O   
4283  C CB  . VAL B 178 ? 0.5506 0.7350 0.4754 0.1345  0.0333  0.2755  187 VAL B CB  
4284  C CG1 . VAL B 178 ? 0.5401 0.6979 0.4670 0.1325  0.0333  0.2626  187 VAL B CG1 
4285  C CG2 . VAL B 178 ? 0.5562 0.7548 0.4587 0.1416  0.0316  0.2667  187 VAL B CG2 
4286  N N   . LEU B 179 ? 0.5492 0.7086 0.5150 0.1239  0.0374  0.2989  188 LEU B N   
4287  C CA  . LEU B 179 ? 0.5458 0.6823 0.5263 0.1210  0.0382  0.3008  188 LEU B CA  
4288  C C   . LEU B 179 ? 0.5506 0.6843 0.5357 0.1153  0.0411  0.3096  188 LEU B C   
4289  O O   . LEU B 179 ? 0.5460 0.6610 0.5375 0.1128  0.0432  0.3049  188 LEU B O   
4290  C CB  . LEU B 179 ? 0.5517 0.6840 0.5415 0.1229  0.0343  0.3106  188 LEU B CB  
4291  C CG  . LEU B 179 ? 0.5507 0.6586 0.5534 0.1236  0.0339  0.3108  188 LEU B CG  
4292  C CD1 . LEU B 179 ? 0.5462 0.6475 0.5505 0.1265  0.0339  0.2959  188 LEU B CD1 
4293  C CD2 . LEU B 179 ? 0.5608 0.6649 0.5702 0.1267  0.0294  0.3252  188 LEU B CD2 
4294  N N   . THR B 180 ? 0.5607 0.7149 0.5421 0.1123  0.0408  0.3229  189 THR B N   
4295  C CA  . THR B 180 ? 0.5689 0.7278 0.5517 0.1046  0.0431  0.3316  189 THR B CA  
4296  C C   . THR B 180 ? 0.5641 0.7280 0.5408 0.1063  0.0478  0.3175  189 THR B C   
4297  O O   . THR B 180 ? 0.5612 0.7081 0.5439 0.1023  0.0499  0.3137  189 THR B O   
4298  C CB  . THR B 180 ? 0.5774 0.7646 0.5553 0.1007  0.0419  0.3476  189 THR B CB  
4299  O OG1 . THR B 180 ? 0.5893 0.7659 0.5732 0.0979  0.0370  0.3626  189 THR B OG1 
4300  C CG2 . THR B 180 ? 0.5870 0.7881 0.5641 0.0915  0.0447  0.3554  189 THR B CG2 
4301  N N   . SER B 181 ? 0.5658 0.7511 0.5290 0.1133  0.0486  0.3089  190 SER B N   
4302  C CA  . SER B 181 ? 0.5618 0.7508 0.5156 0.1182  0.0518  0.2941  190 SER B CA  
4303  C C   . SER B 181 ? 0.5571 0.7150 0.5173 0.1172  0.0530  0.2822  190 SER B C   
4304  O O   . SER B 181 ? 0.5574 0.7140 0.5160 0.1170  0.0563  0.2756  190 SER B O   
4305  C CB  . SER B 181 ? 0.5632 0.7645 0.4989 0.1288  0.0497  0.2822  190 SER B CB  
4306  O OG  . SER B 181 ? 0.5600 0.7620 0.4835 0.1357  0.0516  0.2676  190 SER B OG  
4307  N N   . LYS B 182 ? 0.5566 0.6924 0.5244 0.1167  0.0505  0.2802  191 LYS B N   
4308  C CA  . LYS B 182 ? 0.5506 0.6600 0.5241 0.1162  0.0515  0.2687  191 LYS B CA  
4309  C C   . LYS B 182 ? 0.5482 0.6405 0.5365 0.1097  0.0529  0.2755  191 LYS B C   
4310  O O   . LYS B 182 ? 0.5456 0.6231 0.5370 0.1084  0.0553  0.2666  191 LYS B O   
4311  C CB  . LYS B 182 ? 0.5487 0.6466 0.5222 0.1189  0.0479  0.2616  191 LYS B CB  
4312  C CG  . LYS B 182 ? 0.5675 0.6673 0.5236 0.1235  0.0456  0.2476  191 LYS B CG  
4313  C CD  . LYS B 182 ? 0.5969 0.6797 0.5473 0.1238  0.0471  0.2331  191 LYS B CD  
4314  C CE  . LYS B 182 ? 0.6319 0.7248 0.5651 0.1297  0.0481  0.2262  191 LYS B CE  
4315  N NZ  . LYS B 182 ? 0.6583 0.7321 0.5803 0.1318  0.0473  0.2102  191 LYS B NZ  
4316  N N   . VAL B 183 ? 0.5538 0.6455 0.5498 0.1058  0.0506  0.2909  192 VAL B N   
4317  C CA  . VAL B 183 ? 0.5553 0.6259 0.5619 0.0999  0.0502  0.2977  192 VAL B CA  
4318  C C   . VAL B 183 ? 0.5580 0.6351 0.5632 0.0923  0.0534  0.3005  192 VAL B C   
4319  O O   . VAL B 183 ? 0.5616 0.6194 0.5729 0.0876  0.0543  0.2990  192 VAL B O   
4320  C CB  . VAL B 183 ? 0.5689 0.6338 0.5799 0.0978  0.0453  0.3143  192 VAL B CB  
4321  C CG1 . VAL B 183 ? 0.5768 0.6227 0.5923 0.0887  0.0435  0.3252  192 VAL B CG1 
4322  C CG2 . VAL B 183 ? 0.5698 0.6212 0.5860 0.1058  0.0424  0.3095  192 VAL B CG2 
4323  N N   . LEU B 184 ? 0.5595 0.6661 0.5562 0.0916  0.0552  0.3043  193 LEU B N   
4324  C CA  . LEU B 184 ? 0.5641 0.6845 0.5588 0.0854  0.0586  0.3059  193 LEU B CA  
4325  C C   . LEU B 184 ? 0.5580 0.6653 0.5524 0.0898  0.0620  0.2883  193 LEU B C   
4326  O O   . LEU B 184 ? 0.5617 0.6556 0.5622 0.0834  0.0635  0.2879  193 LEU B O   
4327  C CB  . LEU B 184 ? 0.5655 0.7250 0.5495 0.0880  0.0602  0.3094  193 LEU B CB  
4328  C CG  . LEU B 184 ? 0.5676 0.7480 0.5496 0.0825  0.0639  0.3110  193 LEU B CG  
4329  C CD1 . LEU B 184 ? 0.5751 0.7620 0.5629 0.0665  0.0618  0.3319  193 LEU B CD1 
4330  C CD2 . LEU B 184 ? 0.5767 0.7944 0.5451 0.0927  0.0664  0.3045  193 LEU B CD2 
4331  N N   . ASP B 185 ? 0.5586 0.6676 0.5444 0.1001  0.0624  0.2739  194 ASP B N   
4332  C CA  . ASP B 185 ? 0.5577 0.6523 0.5406 0.1044  0.0646  0.2570  194 ASP B CA  
4333  C C   . ASP B 185 ? 0.5514 0.6160 0.5466 0.1000  0.0647  0.2537  194 ASP B C   
4334  O O   . ASP B 185 ? 0.5471 0.6037 0.5440 0.0981  0.0675  0.2468  194 ASP B O   
4335  C CB  . ASP B 185 ? 0.5618 0.6556 0.5315 0.1141  0.0624  0.2440  194 ASP B CB  
4336  C CG  . ASP B 185 ? 0.5865 0.7090 0.5410 0.1209  0.0619  0.2448  194 ASP B CG  
4337  O OD1 . ASP B 185 ? 0.5995 0.7472 0.5548 0.1183  0.0642  0.2549  194 ASP B OD1 
4338  O OD2 . ASP B 185 ? 0.6083 0.7290 0.5491 0.1285  0.0587  0.2353  194 ASP B OD2 
4339  N N   . LEU B 186 ? 0.5541 0.6040 0.5571 0.0994  0.0616  0.2585  195 LEU B N   
4340  C CA  . LEU B 186 ? 0.5534 0.5771 0.5675 0.0972  0.0612  0.2557  195 LEU B CA  
4341  C C   . LEU B 186 ? 0.5608 0.5781 0.5802 0.0884  0.0624  0.2635  195 LEU B C   
4342  O O   . LEU B 186 ? 0.5566 0.5604 0.5796 0.0865  0.0646  0.2554  195 LEU B O   
4343  C CB  . LEU B 186 ? 0.5598 0.5726 0.5806 0.0997  0.0571  0.2618  195 LEU B CB  
4344  C CG  . LEU B 186 ? 0.5505 0.5465 0.5772 0.1043  0.0566  0.2503  195 LEU B CG  
4345  C CD1 . LEU B 186 ? 0.5566 0.5358 0.5927 0.1066  0.0531  0.2570  195 LEU B CD1 
4346  C CD2 . LEU B 186 ? 0.5415 0.5272 0.5689 0.1021  0.0601  0.2388  195 LEU B CD2 
4347  N N   . LYS B 187 ? 0.5741 0.6011 0.5931 0.0819  0.0604  0.2796  196 LYS B N   
4348  C CA  . LYS B 187 ? 0.5868 0.6084 0.6087 0.0704  0.0602  0.2888  196 LYS B CA  
4349  C C   . LYS B 187 ? 0.5800 0.6166 0.5986 0.0692  0.0654  0.2799  196 LYS B C   
4350  O O   . LYS B 187 ? 0.5831 0.6051 0.6060 0.0644  0.0667  0.2757  196 LYS B O   
4351  C CB  . LYS B 187 ? 0.6016 0.6373 0.6206 0.0614  0.0568  0.3086  196 LYS B CB  
4352  C CG  . LYS B 187 ? 0.6033 0.6460 0.6214 0.0465  0.0569  0.3191  196 LYS B CG  
4353  C CD  . LYS B 187 ? 0.5948 0.6803 0.6067 0.0457  0.0617  0.3192  196 LYS B CD  
4354  C CE  . LYS B 187 ? 0.6160 0.7165 0.6272 0.0292  0.0615  0.3317  196 LYS B CE  
4355  N NZ  . LYS B 187 ? 0.6144 0.7596 0.6201 0.0314  0.0670  0.3284  196 LYS B NZ  
4356  N N   . ASN B 188 ? 0.5783 0.6436 0.5882 0.0751  0.0679  0.2759  197 ASN B N   
4357  C CA  . ASN B 188 ? 0.5789 0.6618 0.5836 0.0762  0.0723  0.2682  197 ASN B CA  
4358  C C   . ASN B 188 ? 0.5727 0.6348 0.5787 0.0810  0.0746  0.2511  197 ASN B C   
4359  O O   . ASN B 188 ? 0.5756 0.6413 0.5824 0.0774  0.0775  0.2478  197 ASN B O   
4360  C CB  . ASN B 188 ? 0.5778 0.6958 0.5701 0.0842  0.0737  0.2670  197 ASN B CB  
4361  C CG  . ASN B 188 ? 0.5976 0.7488 0.5890 0.0752  0.0741  0.2833  197 ASN B CG  
4362  O OD1 . ASN B 188 ? 0.6181 0.7883 0.6059 0.0753  0.0722  0.2935  197 ASN B OD1 
4363  N ND2 . ASN B 188 ? 0.6075 0.7676 0.6021 0.0661  0.0763  0.2869  197 ASN B ND2 
4364  N N   . TYR B 189 ? 0.5672 0.6093 0.5735 0.0880  0.0730  0.2412  198 TYR B N   
4365  C CA  . TYR B 189 ? 0.5593 0.5809 0.5678 0.0903  0.0745  0.2271  198 TYR B CA  
4366  C C   . TYR B 189 ? 0.5551 0.5600 0.5749 0.0812  0.0751  0.2316  198 TYR B C   
4367  O O   . TYR B 189 ? 0.5526 0.5596 0.5726 0.0778  0.0779  0.2278  198 TYR B O   
4368  C CB  . TYR B 189 ? 0.5636 0.5683 0.5725 0.0958  0.0720  0.2190  198 TYR B CB  
4369  C CG  . TYR B 189 ? 0.5788 0.5691 0.5850 0.0987  0.0732  0.2035  198 TYR B CG  
4370  C CD1 . TYR B 189 ? 0.6150 0.6116 0.6060 0.1049  0.0732  0.1929  198 TYR B CD1 
4371  C CD2 . TYR B 189 ? 0.5865 0.5562 0.6034 0.0958  0.0735  0.1993  198 TYR B CD2 
4372  C CE1 . TYR B 189 ? 0.6280 0.6089 0.6140 0.1066  0.0732  0.1792  198 TYR B CE1 
4373  C CE2 . TYR B 189 ? 0.6069 0.5651 0.6208 0.0973  0.0745  0.1856  198 TYR B CE2 
4374  C CZ  . TYR B 189 ? 0.6231 0.5863 0.6214 0.1019  0.0741  0.1761  198 TYR B CZ  
4375  O OH  . TYR B 189 ? 0.6163 0.5661 0.6092 0.1025  0.0739  0.1636  198 TYR B OH  
4376  N N   . ILE B 190 ? 0.5610 0.5489 0.5886 0.0777  0.0717  0.2398  199 ILE B N   
4377  C CA  . ILE B 190 ? 0.5692 0.5370 0.6043 0.0694  0.0706  0.2443  199 ILE B CA  
4378  C C   . ILE B 190 ? 0.5793 0.5618 0.6125 0.0590  0.0725  0.2509  199 ILE B C   
4379  O O   . ILE B 190 ? 0.5769 0.5528 0.6124 0.0560  0.0750  0.2438  199 ILE B O   
4380  C CB  . ILE B 190 ? 0.5813 0.5312 0.6204 0.0674  0.0649  0.2560  199 ILE B CB  
4381  C CG1 . ILE B 190 ? 0.5717 0.5040 0.6156 0.0775  0.0634  0.2467  199 ILE B CG1 
4382  C CG2 . ILE B 190 ? 0.5922 0.5219 0.6337 0.0566  0.0619  0.2640  199 ILE B CG2 
4383  C CD1 . ILE B 190 ? 0.5837 0.5081 0.6285 0.0808  0.0581  0.2567  199 ILE B CD1 
4384  N N   . ASP B 191 ? 0.5952 0.6009 0.6241 0.0531  0.0715  0.2647  200 ASP B N   
4385  C CA  . ASP B 191 ? 0.6104 0.6320 0.6383 0.0398  0.0721  0.2746  200 ASP B CA  
4386  C C   . ASP B 191 ? 0.5949 0.6386 0.6195 0.0438  0.0778  0.2637  200 ASP B C   
4387  O O   . ASP B 191 ? 0.5959 0.6400 0.6228 0.0351  0.0791  0.2640  200 ASP B O   
4388  C CB  . ASP B 191 ? 0.6293 0.6765 0.6527 0.0316  0.0697  0.2929  200 ASP B CB  
4389  C CG  . ASP B 191 ? 0.6622 0.7313 0.6840 0.0149  0.0698  0.3050  200 ASP B CG  
4390  O OD1 . ASP B 191 ? 0.6943 0.7424 0.7196 0.0047  0.0684  0.3052  200 ASP B OD1 
4391  O OD2 . ASP B 191 ? 0.6715 0.7807 0.6883 0.0115  0.0711  0.3146  200 ASP B OD2 
4392  N N   . LYS B 192 ? 0.5855 0.6456 0.6031 0.0573  0.0803  0.2537  201 LYS B N   
4393  C CA  . LYS B 192 ? 0.5839 0.6692 0.5945 0.0633  0.0846  0.2448  201 LYS B CA  
4394  C C   . LYS B 192 ? 0.5747 0.6424 0.5819 0.0749  0.0865  0.2253  201 LYS B C   
4395  O O   . LYS B 192 ? 0.5709 0.6546 0.5697 0.0824  0.0892  0.2163  201 LYS B O   
4396  C CB  . LYS B 192 ? 0.5854 0.7101 0.5861 0.0689  0.0853  0.2503  201 LYS B CB  
4397  C CG  . LYS B 192 ? 0.6078 0.7539 0.6120 0.0541  0.0837  0.2705  201 LYS B CG  
4398  C CD  . LYS B 192 ? 0.6508 0.8422 0.6457 0.0591  0.0849  0.2763  201 LYS B CD  
4399  C CE  . LYS B 192 ? 0.6940 0.9032 0.6925 0.0416  0.0821  0.2987  201 LYS B CE  
4400  N NZ  . LYS B 192 ? 0.7231 0.9756 0.7134 0.0463  0.0824  0.3066  201 LYS B NZ  
4401  N N   . GLN B 193 ? 0.5760 0.6113 0.5889 0.0760  0.0847  0.2193  202 GLN B N   
4402  C CA  . GLN B 193 ? 0.5723 0.5905 0.5816 0.0842  0.0856  0.2027  202 GLN B CA  
4403  C C   . GLN B 193 ? 0.5635 0.5544 0.5841 0.0779  0.0857  0.1994  202 GLN B C   
4404  O O   . GLN B 193 ? 0.5606 0.5489 0.5823 0.0760  0.0882  0.1929  202 GLN B O   
4405  C CB  . GLN B 193 ? 0.5797 0.5902 0.5823 0.0928  0.0827  0.1970  202 GLN B CB  
4406  C CG  . GLN B 193 ? 0.6215 0.6544 0.6085 0.1022  0.0821  0.1950  202 GLN B CG  
4407  C CD  . GLN B 193 ? 0.6752 0.7076 0.6493 0.1109  0.0829  0.1808  202 GLN B CD  
4408  O OE1 . GLN B 193 ? 0.6983 0.7072 0.6722 0.1114  0.0822  0.1704  202 GLN B OE1 
4409  N NE2 . GLN B 193 ? 0.6939 0.7529 0.6561 0.1185  0.0840  0.1801  202 GLN B NE2 
4410  N N   . LEU B 194 ? 0.5584 0.5305 0.5867 0.0758  0.0828  0.2037  203 LEU B N   
4411  C CA  . LEU B 194 ? 0.5511 0.4969 0.5890 0.0725  0.0821  0.2000  203 LEU B CA  
4412  C C   . LEU B 194 ? 0.5582 0.4984 0.6015 0.0616  0.0820  0.2074  203 LEU B C   
4413  O O   . LEU B 194 ? 0.5526 0.4840 0.5988 0.0590  0.0840  0.2001  203 LEU B O   
4414  C CB  . LEU B 194 ? 0.5543 0.4857 0.5973 0.0755  0.0782  0.2038  203 LEU B CB  
4415  C CG  . LEU B 194 ? 0.5530 0.4583 0.6049 0.0744  0.0765  0.2009  203 LEU B CG  
4416  C CD1 . LEU B 194 ? 0.5466 0.4458 0.6001 0.0812  0.0777  0.1869  203 LEU B CD1 
4417  C CD2 . LEU B 194 ? 0.5641 0.4568 0.6194 0.0752  0.0714  0.2113  203 LEU B CD2 
4418  N N   . LEU B 195 ? 0.5718 0.5170 0.6152 0.0541  0.0791  0.2225  204 LEU B N   
4419  C CA  . LEU B 195 ? 0.5876 0.5227 0.6337 0.0408  0.0767  0.2324  204 LEU B CA  
4420  C C   . LEU B 195 ? 0.5834 0.5311 0.6289 0.0336  0.0802  0.2293  204 LEU B C   
4421  O O   . LEU B 195 ? 0.5981 0.5270 0.6468 0.0249  0.0785  0.2301  204 LEU B O   
4422  C CB  . LEU B 195 ? 0.6042 0.5492 0.6470 0.0320  0.0726  0.2507  204 LEU B CB  
4423  C CG  . LEU B 195 ? 0.6351 0.5551 0.6781 0.0180  0.0664  0.2625  204 LEU B CG  
4424  C CD1 . LEU B 195 ? 0.6401 0.5233 0.6855 0.0253  0.0613  0.2598  204 LEU B CD1 
4425  C CD2 . LEU B 195 ? 0.6700 0.6075 0.7074 0.0045  0.0627  0.2824  204 LEU B CD2 
4426  N N   . PRO B 196 ? 0.5712 0.5507 0.6115 0.0377  0.0847  0.2258  205 PRO B N   
4427  C CA  . PRO B 196 ? 0.5638 0.5562 0.6037 0.0336  0.0883  0.2208  205 PRO B CA  
4428  C C   . PRO B 196 ? 0.5570 0.5236 0.6014 0.0374  0.0897  0.2063  205 PRO B C   
4429  O O   . PRO B 196 ? 0.5610 0.5187 0.6091 0.0282  0.0897  0.2063  205 PRO B O   
4430  C CB  . PRO B 196 ? 0.5499 0.5756 0.5810 0.0446  0.0921  0.2154  205 PRO B CB  
4431  C CG  . PRO B 196 ? 0.5597 0.5986 0.5870 0.0472  0.0900  0.2246  205 PRO B CG  
4432  C CD  . PRO B 196 ? 0.5667 0.5733 0.5997 0.0463  0.0859  0.2273  205 PRO B CD  
4433  N N   . ILE B 197 ? 0.5456 0.5009 0.5889 0.0497  0.0903  0.1948  206 ILE B N   
4434  C CA  . ILE B 197 ? 0.5350 0.4734 0.5808 0.0537  0.0922  0.1808  206 ILE B CA  
4435  C C   . ILE B 197 ? 0.5372 0.4455 0.5913 0.0509  0.0893  0.1799  206 ILE B C   
4436  O O   . ILE B 197 ? 0.5280 0.4223 0.5855 0.0532  0.0905  0.1692  206 ILE B O   
4437  C CB  . ILE B 197 ? 0.5259 0.4682 0.5638 0.0662  0.0937  0.1681  206 ILE B CB  
4438  C CG1 . ILE B 197 ? 0.5303 0.4533 0.5708 0.0714  0.0914  0.1628  206 ILE B CG1 
4439  C CG2 . ILE B 197 ? 0.5347 0.5036 0.5612 0.0727  0.0942  0.1706  206 ILE B CG2 
4440  C CD1 . ILE B 197 ? 0.5461 0.4642 0.5794 0.0784  0.0921  0.1489  206 ILE B CD1 
4441  N N   . VAL B 198 ? 0.5558 0.4543 0.6121 0.0468  0.0851  0.1910  207 VAL B N   
4442  C CA  . VAL B 198 ? 0.5760 0.4443 0.6377 0.0450  0.0813  0.1905  207 VAL B CA  
4443  C C   . VAL B 198 ? 0.5897 0.4524 0.6514 0.0323  0.0804  0.1948  207 VAL B C   
4444  O O   . VAL B 198 ? 0.5933 0.4419 0.6580 0.0315  0.0812  0.1859  207 VAL B O   
4445  C CB  . VAL B 198 ? 0.5924 0.4465 0.6539 0.0456  0.0754  0.2012  207 VAL B CB  
4446  C CG1 . VAL B 198 ? 0.6055 0.4264 0.6688 0.0432  0.0703  0.2012  207 VAL B CG1 
4447  C CG2 . VAL B 198 ? 0.5922 0.4503 0.6547 0.0582  0.0757  0.1964  207 VAL B CG2 
4448  N N   . ASN B 199 ? 0.6058 0.4818 0.6636 0.0211  0.0786  0.2087  208 ASN B N   
4449  C CA  . ASN B 199 ? 0.6272 0.4983 0.6840 0.0061  0.0767  0.2143  208 ASN B CA  
4450  C C   . ASN B 199 ? 0.6132 0.5118 0.6702 0.0036  0.0828  0.2081  208 ASN B C   
4451  O O   . ASN B 199 ? 0.6230 0.5276 0.6790 -0.0100 0.0821  0.2132  208 ASN B O   
4452  C CB  . ASN B 199 ? 0.6550 0.5187 0.7065 -0.0087 0.0695  0.2331  208 ASN B CB  
4453  C CG  . ASN B 199 ? 0.6483 0.5492 0.6963 -0.0136 0.0710  0.2456  208 ASN B CG  
4454  O OD1 . ASN B 199 ? 0.6347 0.5665 0.6831 -0.0041 0.0771  0.2400  208 ASN B OD1 
4455  N ND2 . ASN B 199 ? 0.6654 0.5625 0.7081 -0.0286 0.0646  0.2629  208 ASN B ND2 
4456  N N   . LYS B 200 ? 0.5940 0.5072 0.6512 0.0170  0.0881  0.1964  209 LYS B N   
4457  C CA  . LYS B 200 ? 0.5857 0.5121 0.6428 0.0180  0.0928  0.1866  209 LYS B CA  
4458  C C   . LYS B 200 ? 0.5803 0.4772 0.6425 0.0197  0.0926  0.1750  209 LYS B C   
4459  O O   . LYS B 200 ? 0.5782 0.4718 0.6421 0.0118  0.0932  0.1725  209 LYS B O   
4460  C CB  . LYS B 200 ? 0.5725 0.5219 0.6240 0.0316  0.0971  0.1786  209 LYS B CB  
4461  C CG  . LYS B 200 ? 0.5853 0.5691 0.6321 0.0297  0.1005  0.1799  209 LYS B CG  
4462  C CD  . LYS B 200 ? 0.6050 0.6185 0.6427 0.0402  0.1019  0.1814  209 LYS B CD  
4463  C CE  . LYS B 200 ? 0.6092 0.6223 0.6390 0.0561  0.1042  0.1658  209 LYS B CE  
4464  N NZ  . LYS B 200 ? 0.6279 0.6427 0.6488 0.0683  0.1026  0.1637  209 LYS B NZ  
4465  N N   . GLN B 201 ? 0.5761 0.4542 0.6406 0.0298  0.0915  0.1683  210 GLN B N   
4466  C CA  . GLN B 201 ? 0.5781 0.4310 0.6475 0.0329  0.0908  0.1579  210 GLN B CA  
4467  C C   . GLN B 201 ? 0.6017 0.4327 0.6721 0.0220  0.0861  0.1637  210 GLN B C   
4468  O O   . GLN B 201 ? 0.6041 0.4242 0.6765 0.0188  0.0866  0.1564  210 GLN B O   
4469  C CB  . GLN B 201 ? 0.5743 0.4143 0.6459 0.0438  0.0889  0.1541  210 GLN B CB  
4470  C CG  . GLN B 201 ? 0.5630 0.4180 0.6320 0.0535  0.0919  0.1469  210 GLN B CG  
4471  C CD  . GLN B 201 ? 0.5822 0.4280 0.6537 0.0618  0.0894  0.1452  210 GLN B CD  
4472  O OE1 . GLN B 201 ? 0.6019 0.4340 0.6761 0.0621  0.0854  0.1516  210 GLN B OE1 
4473  N NE2 . GLN B 201 ? 0.5706 0.4236 0.6398 0.0684  0.0910  0.1369  210 GLN B NE2 
4474  N N   . SER B 202 ? 0.6259 0.4485 0.6933 0.0160  0.0807  0.1768  211 SER B N   
4475  C CA  . SER B 202 ? 0.6610 0.4557 0.7253 0.0048  0.0739  0.1834  211 SER B CA  
4476  C C   . SER B 202 ? 0.6660 0.4691 0.7292 -0.0090 0.0752  0.1838  211 SER B C   
4477  O O   . SER B 202 ? 0.6828 0.4603 0.7443 -0.0154 0.0711  0.1811  211 SER B O   
4478  C CB  . SER B 202 ? 0.6837 0.4714 0.7420 -0.0029 0.0672  0.2002  211 SER B CB  
4479  O OG  . SER B 202 ? 0.7007 0.4668 0.7587 0.0091  0.0631  0.1995  211 SER B OG  
4480  N N   . CYS B 203 ? 0.6534 0.4932 0.7168 -0.0122 0.0807  0.1863  212 CYS B N   
4481  C CA  . CYS B 203 ? 0.6571 0.5116 0.7201 -0.0240 0.0827  0.1864  212 CYS B CA  
4482  C C   . CYS B 203 ? 0.6332 0.4809 0.7005 -0.0172 0.0867  0.1701  212 CYS B C   
4483  O O   . CYS B 203 ? 0.6369 0.4670 0.7038 -0.0261 0.0841  0.1676  212 CYS B O   
4484  C CB  . CYS B 203 ? 0.6515 0.5507 0.7128 -0.0263 0.0874  0.1925  212 CYS B CB  
4485  S SG  . CYS B 203 ? 0.7133 0.6282 0.7742 -0.0423 0.0882  0.1940  212 CYS B SG  
4486  N N   . SER B 204 ? 0.6055 0.4667 0.6751 -0.0024 0.0924  0.1594  213 SER B N   
4487  C CA  . SER B 204 ? 0.5871 0.4446 0.6598 0.0043  0.0963  0.1446  213 SER B CA  
4488  C C   . SER B 204 ? 0.5921 0.4157 0.6677 0.0037  0.0926  0.1383  213 SER B C   
4489  O O   . SER B 204 ? 0.5971 0.4159 0.6742 0.0000  0.0937  0.1312  213 SER B O   
4490  C CB  . SER B 204 ? 0.5698 0.4365 0.6420 0.0197  0.1002  0.1354  213 SER B CB  
4491  O OG  . SER B 204 ? 0.5754 0.4721 0.6421 0.0224  0.1030  0.1390  213 SER B OG  
4492  N N   . ILE B 205 ? 0.5953 0.3963 0.6709 0.0084  0.0879  0.1408  214 ILE B N   
4493  C CA  . ILE B 205 ? 0.6044 0.3722 0.6805 0.0103  0.0832  0.1349  214 ILE B CA  
4494  C C   . ILE B 205 ? 0.6252 0.3755 0.6962 -0.0053 0.0778  0.1405  214 ILE B C   
4495  O O   . ILE B 205 ? 0.6300 0.3659 0.7013 -0.0064 0.0772  0.1314  214 ILE B O   
4496  C CB  . ILE B 205 ? 0.6183 0.3677 0.6935 0.0201  0.0785  0.1375  214 ILE B CB  
4497  C CG1 . ILE B 205 ? 0.5945 0.3595 0.6748 0.0347  0.0834  0.1293  214 ILE B CG1 
4498  C CG2 . ILE B 205 ? 0.6366 0.3494 0.7088 0.0231  0.0717  0.1328  214 ILE B CG2 
4499  C CD1 . ILE B 205 ? 0.6174 0.3789 0.6971 0.0426  0.0803  0.1353  214 ILE B CD1 
4500  N N   . SER B 206 ? 0.6372 0.3894 0.7025 -0.0185 0.0735  0.1557  215 SER B N   
4501  C CA  . SER B 206 ? 0.6578 0.3952 0.7161 -0.0372 0.0673  0.1629  215 SER B CA  
4502  C C   . SER B 206 ? 0.6390 0.3934 0.7008 -0.0428 0.0725  0.1549  215 SER B C   
4503  O O   . SER B 206 ? 0.6578 0.3895 0.7158 -0.0504 0.0682  0.1509  215 SER B O   
4504  C CB  . SER B 206 ? 0.6752 0.4265 0.7275 -0.0536 0.0636  0.1819  215 SER B CB  
4505  O OG  . SER B 206 ? 0.7086 0.4427 0.7520 -0.0746 0.0559  0.1904  215 SER B OG  
4506  N N   . ASN B 207 ? 0.6001 0.3926 0.6675 -0.0379 0.0810  0.1520  216 ASN B N   
4507  C CA  . ASN B 207 ? 0.5767 0.3870 0.6470 -0.0406 0.0861  0.1438  216 ASN B CA  
4508  C C   . ASN B 207 ? 0.5605 0.3500 0.6344 -0.0308 0.0874  0.1276  216 ASN B C   
4509  O O   . ASN B 207 ? 0.5708 0.3480 0.6433 -0.0389 0.0853  0.1234  216 ASN B O   
4510  C CB  . ASN B 207 ? 0.5532 0.4050 0.6259 -0.0337 0.0937  0.1432  216 ASN B CB  
4511  C CG  . ASN B 207 ? 0.5691 0.4488 0.6381 -0.0433 0.0929  0.1588  216 ASN B CG  
4512  O OD1 . ASN B 207 ? 0.6004 0.4700 0.6652 -0.0584 0.0866  0.1716  216 ASN B OD1 
4513  N ND2 . ASN B 207 ? 0.5694 0.4845 0.6384 -0.0345 0.0987  0.1579  216 ASN B ND2 
4514  N N   . ILE B 208 ? 0.5347 0.3220 0.6126 -0.0141 0.0905  0.1189  217 ILE B N   
4515  C CA  . ILE B 208 ? 0.5257 0.2983 0.6071 -0.0047 0.0918  0.1044  217 ILE B CA  
4516  C C   . ILE B 208 ? 0.5560 0.2944 0.6334 -0.0101 0.0846  0.1031  217 ILE B C   
4517  O O   . ILE B 208 ? 0.5592 0.2915 0.6365 -0.0145 0.0847  0.0958  217 ILE B O   
4518  C CB  . ILE B 208 ? 0.5117 0.2836 0.5965 0.0114  0.0937  0.0984  217 ILE B CB  
4519  C CG1 . ILE B 208 ? 0.4897 0.2914 0.5753 0.0164  0.0999  0.0971  217 ILE B CG1 
4520  C CG2 . ILE B 208 ? 0.5123 0.2698 0.6005 0.0201  0.0939  0.0847  217 ILE B CG2 
4521  C CD1 . ILE B 208 ? 0.4870 0.2919 0.5731 0.0279  0.1006  0.0964  217 ILE B CD1 
4522  N N   . GLU B 209 ? 0.5861 0.3006 0.6586 -0.0097 0.0776  0.1102  218 GLU B N   
4523  C CA  . GLU B 209 ? 0.6315 0.3068 0.6958 -0.0135 0.0686  0.1091  218 GLU B CA  
4524  C C   . GLU B 209 ? 0.6400 0.3111 0.6987 -0.0326 0.0657  0.1124  218 GLU B C   
4525  O O   . GLU B 209 ? 0.6527 0.3051 0.7088 -0.0331 0.0633  0.1027  218 GLU B O   
4526  C CB  . GLU B 209 ? 0.6635 0.3149 0.7199 -0.0138 0.0603  0.1202  218 GLU B CB  
4527  C CG  . GLU B 209 ? 0.7138 0.3595 0.7739 0.0068  0.0608  0.1139  218 GLU B CG  
4528  C CD  . GLU B 209 ? 0.8057 0.4369 0.8596 0.0083  0.0543  0.1261  218 GLU B CD  
4529  O OE1 . GLU B 209 ? 0.8352 0.4700 0.8839 -0.0078 0.0514  0.1409  218 GLU B OE1 
4530  O OE2 . GLU B 209 ? 0.8351 0.4545 0.8894 0.0255  0.0521  0.1213  218 GLU B OE2 
4531  N N   . THR B 210 ? 0.6328 0.3241 0.6896 -0.0486 0.0658  0.1261  219 THR B N   
4532  C CA  . THR B 210 ? 0.6361 0.3322 0.6884 -0.0684 0.0636  0.1305  219 THR B CA  
4533  C C   . THR B 210 ? 0.6095 0.3187 0.6683 -0.0642 0.0701  0.1161  219 THR B C   
4534  O O   . THR B 210 ? 0.6329 0.3188 0.6865 -0.0705 0.0654  0.1102  219 THR B O   
4535  C CB  . THR B 210 ? 0.6294 0.3626 0.6820 -0.0832 0.0659  0.1459  219 THR B CB  
4536  O OG1 . THR B 210 ? 0.6506 0.3725 0.6971 -0.0874 0.0598  0.1597  219 THR B OG1 
4537  C CG2 . THR B 210 ? 0.6405 0.3801 0.6877 -0.1058 0.0625  0.1519  219 THR B CG2 
4538  N N   . VAL B 211 ? 0.5596 0.3032 0.6279 -0.0534 0.0800  0.1103  220 VAL B N   
4539  C CA  . VAL B 211 ? 0.5262 0.2825 0.5996 -0.0494 0.0858  0.0977  220 VAL B CA  
4540  C C   . VAL B 211 ? 0.5355 0.2589 0.6078 -0.0418 0.0825  0.0845  220 VAL B C   
4541  O O   . VAL B 211 ? 0.5450 0.2582 0.6142 -0.0505 0.0800  0.0799  220 VAL B O   
4542  C CB  . VAL B 211 ? 0.4898 0.2766 0.5702 -0.0354 0.0947  0.0921  220 VAL B CB  
4543  C CG1 . VAL B 211 ? 0.4689 0.2572 0.5533 -0.0283 0.0988  0.0777  220 VAL B CG1 
4544  C CG2 . VAL B 211 ? 0.4741 0.2986 0.5542 -0.0421 0.0986  0.1012  220 VAL B CG2 
4545  N N   . ILE B 212 ? 0.5321 0.2412 0.6065 -0.0254 0.0821  0.0785  221 ILE B N   
4546  C CA  . ILE B 212 ? 0.5414 0.2253 0.6150 -0.0147 0.0795  0.0652  221 ILE B CA  
4547  C C   . ILE B 212 ? 0.5867 0.2361 0.6492 -0.0256 0.0700  0.0661  221 ILE B C   
4548  O O   . ILE B 212 ? 0.5917 0.2313 0.6524 -0.0262 0.0690  0.0560  221 ILE B O   
4549  C CB  . ILE B 212 ? 0.5398 0.2110 0.6143 0.0022  0.0776  0.0625  221 ILE B CB  
4550  C CG1 . ILE B 212 ? 0.4970 0.1991 0.5804 0.0122  0.0856  0.0619  221 ILE B CG1 
4551  C CG2 . ILE B 212 ? 0.5462 0.1951 0.6188 0.0144  0.0744  0.0485  221 ILE B CG2 
4552  C CD1 . ILE B 212 ? 0.4675 0.1914 0.5574 0.0168  0.0929  0.0512  221 ILE B CD1 
4553  N N   . GLU B 213 ? 0.6294 0.2595 0.6828 -0.0352 0.0621  0.0788  222 GLU B N   
4554  C CA  . GLU B 213 ? 0.6935 0.2819 0.7320 -0.0457 0.0503  0.0807  222 GLU B CA  
4555  C C   . GLU B 213 ? 0.6998 0.2955 0.7350 -0.0665 0.0495  0.0830  222 GLU B C   
4556  O O   . GLU B 213 ? 0.7365 0.2981 0.7587 -0.0758 0.0401  0.0808  222 GLU B O   
4557  C CB  . GLU B 213 ? 0.7256 0.2923 0.7536 -0.0531 0.0414  0.0960  222 GLU B CB  
4558  C CG  . GLU B 213 ? 0.8194 0.3300 0.8296 -0.0506 0.0275  0.0936  222 GLU B CG  
4559  C CD  . GLU B 213 ? 0.9173 0.4049 0.9162 -0.0560 0.0183  0.1091  222 GLU B CD  
4560  O OE1 . GLU B 213 ? 0.9320 0.4526 0.9396 -0.0610 0.0243  0.1209  222 GLU B OE1 
4561  O OE2 . GLU B 213 ? 0.9897 0.4263 0.9701 -0.0548 0.0048  0.1096  222 GLU B OE2 
4562  N N   . PHE B 214 ? 0.6711 0.3112 0.7165 -0.0730 0.0588  0.0869  223 PHE B N   
4563  C CA  . PHE B 214 ? 0.6742 0.3304 0.7182 -0.0918 0.0593  0.0893  223 PHE B CA  
4564  C C   . PHE B 214 ? 0.6698 0.3224 0.7170 -0.0841 0.0624  0.0724  223 PHE B C   
4565  O O   . PHE B 214 ? 0.6922 0.3281 0.7314 -0.0970 0.0567  0.0699  223 PHE B O   
4566  C CB  . PHE B 214 ? 0.6396 0.3473 0.6929 -0.0968 0.0684  0.0978  223 PHE B CB  
4567  C CG  . PHE B 214 ? 0.6243 0.3590 0.6789 -0.1114 0.0712  0.0982  223 PHE B CG  
4568  C CD1 . PHE B 214 ? 0.6443 0.3848 0.6910 -0.1363 0.0651  0.1119  223 PHE B CD1 
4569  C CD2 . PHE B 214 ? 0.5942 0.3508 0.6574 -0.1011 0.0797  0.0858  223 PHE B CD2 
4570  C CE1 . PHE B 214 ? 0.6278 0.3985 0.6760 -0.1500 0.0679  0.1129  223 PHE B CE1 
4571  C CE2 . PHE B 214 ? 0.5882 0.3718 0.6525 -0.1135 0.0822  0.0864  223 PHE B CE2 
4572  C CZ  . PHE B 214 ? 0.5989 0.3911 0.6562 -0.1378 0.0765  0.0999  223 PHE B CZ  
4573  N N   . GLN B 215 ? 0.6439 0.3124 0.7019 -0.0641 0.0709  0.0615  224 GLN B N   
4574  C CA  . GLN B 215 ? 0.6395 0.3096 0.7019 -0.0547 0.0748  0.0455  224 GLN B CA  
4575  C C   . GLN B 215 ? 0.6680 0.2954 0.7210 -0.0481 0.0663  0.0359  224 GLN B C   
4576  O O   . GLN B 215 ? 0.6739 0.2932 0.7245 -0.0488 0.0653  0.0253  224 GLN B O   
4577  C CB  . GLN B 215 ? 0.6080 0.3034 0.6820 -0.0363 0.0843  0.0382  224 GLN B CB  
4578  C CG  . GLN B 215 ? 0.6139 0.3440 0.6934 -0.0387 0.0907  0.0480  224 GLN B CG  
4579  C CD  . GLN B 215 ? 0.6233 0.3745 0.7107 -0.0230 0.0984  0.0409  224 GLN B CD  
4580  O OE1 . GLN B 215 ? 0.6350 0.3749 0.7245 -0.0095 0.0983  0.0337  224 GLN B OE1 
4581  N NE2 . GLN B 215 ? 0.6098 0.3922 0.7001 -0.0246 0.1046  0.0429  224 GLN B NE2 
4582  N N   . GLN B 216 ? 0.6900 0.2903 0.7366 -0.0404 0.0598  0.0395  225 GLN B N   
4583  C CA  . GLN B 216 ? 0.7246 0.2816 0.7595 -0.0299 0.0504  0.0302  225 GLN B CA  
4584  C C   . GLN B 216 ? 0.7625 0.2847 0.7805 -0.0480 0.0391  0.0326  225 GLN B C   
4585  O O   . GLN B 216 ? 0.7722 0.2753 0.7836 -0.0451 0.0354  0.0202  225 GLN B O   
4586  C CB  . GLN B 216 ? 0.7411 0.2781 0.7714 -0.0185 0.0452  0.0359  225 GLN B CB  
4587  C CG  . GLN B 216 ? 0.7236 0.2915 0.7684 -0.0012 0.0546  0.0338  225 GLN B CG  
4588  C CD  . GLN B 216 ? 0.7689 0.3136 0.8088 0.0184  0.0491  0.0298  225 GLN B CD  
4589  O OE1 . GLN B 216 ? 0.8107 0.3277 0.8397 0.0161  0.0404  0.0393  225 GLN B OE1 
4590  N NE2 . GLN B 216 ? 0.7578 0.3150 0.8049 0.0380  0.0537  0.0163  225 GLN B NE2 
4591  N N   . LYS B 217 ? 0.7830 0.2985 0.7934 -0.0679 0.0334  0.0491  226 LYS B N   
4592  C CA  . LYS B 217 ? 0.8342 0.3117 0.8250 -0.0880 0.0202  0.0543  226 LYS B CA  
4593  C C   . LYS B 217 ? 0.8206 0.3193 0.8136 -0.1068 0.0231  0.0534  226 LYS B C   
4594  O O   . LYS B 217 ? 0.8578 0.3239 0.8349 -0.1199 0.0128  0.0509  226 LYS B O   
4595  C CB  . LYS B 217 ? 0.8634 0.3302 0.8449 -0.1053 0.0127  0.0743  226 LYS B CB  
4596  C CG  . LYS B 217 ? 0.9124 0.3446 0.8850 -0.0904 0.0052  0.0767  226 LYS B CG  
4597  C CD  . LYS B 217 ? 0.9900 0.3999 0.9468 -0.1135 -0.0064 0.0968  226 LYS B CD  
4598  C CE  . LYS B 217 ? 1.0466 0.4256 0.9948 -0.0994 -0.0136 0.1016  226 LYS B CE  
4599  N NZ  . LYS B 217 ? 1.0845 0.4632 1.0248 -0.1222 -0.0199 0.1243  226 LYS B NZ  
4600  N N   . ASN B 218 ? 0.7682 0.3201 0.7791 -0.1081 0.0362  0.0553  227 ASN B N   
4601  C CA  . ASN B 218 ? 0.7505 0.3278 0.7648 -0.1231 0.0400  0.0538  227 ASN B CA  
4602  C C   . ASN B 218 ? 0.7315 0.3190 0.7541 -0.1082 0.0470  0.0356  227 ASN B C   
4603  O O   . ASN B 218 ? 0.7164 0.3319 0.7446 -0.1171 0.0523  0.0335  227 ASN B O   
4604  C CB  . ASN B 218 ? 0.7118 0.3402 0.7372 -0.1340 0.0485  0.0667  227 ASN B CB  
4605  C CG  . ASN B 218 ? 0.7339 0.3591 0.7483 -0.1606 0.0401  0.0841  227 ASN B CG  
4606  O OD1 . ASN B 218 ? 0.7686 0.3712 0.7698 -0.1797 0.0307  0.0857  227 ASN B OD1 
4607  N ND2 . ASN B 218 ? 0.7204 0.3670 0.7385 -0.1637 0.0423  0.0980  227 ASN B ND2 
4608  N N   . ASN B 219 ? 0.7353 0.3013 0.7579 -0.0855 0.0466  0.0230  228 ASN B N   
4609  C CA  . ASN B 219 ? 0.7079 0.2881 0.7399 -0.0680 0.0542  0.0061  228 ASN B CA  
4610  C C   . ASN B 219 ? 0.7037 0.2854 0.7323 -0.0791 0.0533  -0.0015 228 ASN B C   
4611  O O   . ASN B 219 ? 0.6692 0.2876 0.7096 -0.0786 0.0629  -0.0056 228 ASN B O   
4612  C CB  . ASN B 219 ? 0.7303 0.2801 0.7574 -0.0449 0.0498  -0.0057 228 ASN B CB  
4613  C CG  . ASN B 219 ? 0.7290 0.2934 0.7639 -0.0282 0.0563  -0.0233 228 ASN B CG  
4614  O OD1 . ASN B 219 ? 0.7763 0.3161 0.8011 -0.0252 0.0502  -0.0349 228 ASN B OD1 
4615  N ND2 . ASN B 219 ? 0.7061 0.3100 0.7573 -0.0180 0.0678  -0.0251 228 ASN B ND2 
4616  N N   . ARG B 220 ? 0.7354 0.2751 0.7459 -0.0896 0.0408  -0.0029 229 ARG B N   
4617  C CA  . ARG B 220 ? 0.7329 0.2661 0.7374 -0.0977 0.0381  -0.0125 229 ARG B CA  
4618  C C   . ARG B 220 ? 0.7041 0.2781 0.7168 -0.1181 0.0444  -0.0035 229 ARG B C   
4619  O O   . ARG B 220 ? 0.6806 0.2802 0.7014 -0.1167 0.0513  -0.0119 229 ARG B O   
4620  C CB  . ARG B 220 ? 0.7920 0.2687 0.7720 -0.1080 0.0215  -0.0130 229 ARG B CB  
4621  C CG  . ARG B 220 ? 0.8001 0.2550 0.7710 -0.1011 0.0172  -0.0307 229 ARG B CG  
4622  C CD  . ARG B 220 ? 0.8549 0.2498 0.7975 -0.1141 -0.0011 -0.0304 229 ARG B CD  
4623  N NE  . ARG B 220 ? 0.8743 0.2668 0.8098 -0.1278 -0.0041 -0.0381 229 ARG B NE  
4624  C CZ  . ARG B 220 ? 0.9300 0.2782 0.8409 -0.1472 -0.0196 -0.0366 229 ARG B CZ  
4625  N NH1 . ARG B 220 ? 0.9752 0.2751 0.8649 -0.1551 -0.0340 -0.0273 229 ARG B NH1 
4626  N NH2 . ARG B 220 ? 0.9492 0.2998 0.8551 -0.1592 -0.0213 -0.0441 229 ARG B NH2 
4627  N N   . LEU B 221 ? 0.7040 0.2876 0.7149 -0.1361 0.0421  0.0141  230 LEU B N   
4628  C CA  . LEU B 221 ? 0.6766 0.3061 0.6955 -0.1538 0.0484  0.0238  230 LEU B CA  
4629  C C   . LEU B 221 ? 0.6235 0.3015 0.6617 -0.1380 0.0633  0.0190  230 LEU B C   
4630  O O   . LEU B 221 ? 0.6055 0.3133 0.6495 -0.1428 0.0689  0.0157  230 LEU B O   
4631  C CB  . LEU B 221 ? 0.6868 0.3254 0.7018 -0.1727 0.0446  0.0439  230 LEU B CB  
4632  C CG  . LEU B 221 ? 0.6584 0.3510 0.6814 -0.1896 0.0510  0.0541  230 LEU B CG  
4633  C CD1 . LEU B 221 ? 0.6941 0.3778 0.7043 -0.2172 0.0418  0.0582  230 LEU B CD1 
4634  C CD2 . LEU B 221 ? 0.6599 0.3785 0.6863 -0.1962 0.0529  0.0715  230 LEU B CD2 
4635  N N   . LEU B 222 ? 0.6018 0.2863 0.6483 -0.1197 0.0689  0.0190  231 LEU B N   
4636  C CA  . LEU B 222 ? 0.5584 0.2825 0.6195 -0.1052 0.0811  0.0148  231 LEU B CA  
4637  C C   . LEU B 222 ? 0.5465 0.2725 0.6115 -0.0945 0.0851  -0.0015 231 LEU B C   
4638  O O   . LEU B 222 ? 0.5267 0.2857 0.5986 -0.0949 0.0922  -0.0036 231 LEU B O   
4639  C CB  . LEU B 222 ? 0.5465 0.2706 0.6130 -0.0885 0.0845  0.0169  231 LEU B CB  
4640  C CG  . LEU B 222 ? 0.5610 0.2876 0.6239 -0.0998 0.0811  0.0337  231 LEU B CG  
4641  C CD1 . LEU B 222 ? 0.5931 0.2993 0.6556 -0.0862 0.0792  0.0352  231 LEU B CD1 
4642  C CD2 . LEU B 222 ? 0.5429 0.3170 0.6136 -0.1025 0.0892  0.0417  231 LEU B CD2 
4643  N N   . GLU B 223 ? 0.5628 0.2548 0.6222 -0.0845 0.0801  -0.0130 232 GLU B N   
4644  C CA  . GLU B 223 ? 0.5511 0.2479 0.6141 -0.0744 0.0838  -0.0284 232 GLU B CA  
4645  C C   . GLU B 223 ? 0.5438 0.2552 0.6050 -0.0907 0.0839  -0.0289 232 GLU B C   
4646  O O   . GLU B 223 ? 0.5219 0.2625 0.5913 -0.0867 0.0915  -0.0342 232 GLU B O   
4647  C CB  . GLU B 223 ? 0.5818 0.2401 0.6362 -0.0623 0.0768  -0.0408 232 GLU B CB  
4648  C CG  . GLU B 223 ? 0.6029 0.2560 0.6616 -0.0418 0.0785  -0.0436 232 GLU B CG  
4649  C CD  . GLU B 223 ? 0.6046 0.2933 0.6772 -0.0285 0.0894  -0.0487 232 GLU B CD  
4650  O OE1 . GLU B 223 ? 0.5869 0.2991 0.6645 -0.0318 0.0949  -0.0536 232 GLU B OE1 
4651  O OE2 . GLU B 223 ? 0.6089 0.3009 0.6861 -0.0153 0.0916  -0.0476 232 GLU B OE2 
4652  N N   . ILE B 224 ? 0.5667 0.2585 0.6164 -0.1103 0.0749  -0.0223 233 ILE B N   
4653  C CA  . ILE B 224 ? 0.5673 0.2727 0.6140 -0.1279 0.0738  -0.0224 233 ILE B CA  
4654  C C   . ILE B 224 ? 0.5303 0.2871 0.5885 -0.1323 0.0834  -0.0144 233 ILE B C   
4655  O O   . ILE B 224 ? 0.5109 0.2926 0.5741 -0.1323 0.0886  -0.0203 233 ILE B O   
4656  C CB  . ILE B 224 ? 0.6083 0.2861 0.6392 -0.1521 0.0615  -0.0132 233 ILE B CB  
4657  C CG1 . ILE B 224 ? 0.6431 0.2632 0.6584 -0.1461 0.0499  -0.0201 233 ILE B CG1 
4658  C CG2 . ILE B 224 ? 0.6124 0.3051 0.6398 -0.1709 0.0599  -0.0142 233 ILE B CG2 
4659  C CD1 . ILE B 224 ? 0.6943 0.2784 0.6895 -0.1686 0.0360  -0.0175 233 ILE B CD1 
4660  N N   . THR B 225 ? 0.5243 0.2968 0.5855 -0.1350 0.0851  -0.0010 234 THR B N   
4661  C CA  . THR B 225 ? 0.4986 0.3196 0.5679 -0.1379 0.0928  0.0078  234 THR B CA  
4662  C C   . THR B 225 ? 0.4699 0.3147 0.5488 -0.1191 0.1025  -0.0024 234 THR B C   
4663  O O   . THR B 225 ? 0.4567 0.3356 0.5392 -0.1217 0.1074  -0.0021 234 THR B O   
4664  C CB  . THR B 225 ? 0.4935 0.3233 0.5640 -0.1372 0.0934  0.0213  234 THR B CB  
4665  O OG1 . THR B 225 ? 0.5202 0.3368 0.5811 -0.1593 0.0843  0.0337  234 THR B OG1 
4666  C CG2 . THR B 225 ? 0.4629 0.3417 0.5412 -0.1318 0.1022  0.0270  234 THR B CG2 
4667  N N   . ARG B 226 ? 0.4679 0.2947 0.5498 -0.1008 0.1046  -0.0110 235 ARG B N   
4668  C CA  . ARG B 226 ? 0.4456 0.2907 0.5346 -0.0845 0.1124  -0.0199 235 ARG B CA  
4669  C C   . ARG B 226 ? 0.4449 0.2934 0.5335 -0.0878 0.1129  -0.0305 235 ARG B C   
4670  O O   . ARG B 226 ? 0.4280 0.3065 0.5194 -0.0893 0.1176  -0.0305 235 ARG B O   
4671  C CB  . ARG B 226 ? 0.4460 0.2704 0.5370 -0.0678 0.1128  -0.0262 235 ARG B CB  
4672  C CG  . ARG B 226 ? 0.4451 0.2816 0.5411 -0.0540 0.1187  -0.0365 235 ARG B CG  
4673  C CD  . ARG B 226 ? 0.4774 0.2913 0.5741 -0.0413 0.1170  -0.0451 235 ARG B CD  
4674  N NE  . ARG B 226 ? 0.4879 0.2855 0.5833 -0.0380 0.1139  -0.0379 235 ARG B NE  
4675  C CZ  . ARG B 226 ? 0.4460 0.2553 0.5444 -0.0317 0.1172  -0.0306 235 ARG B CZ  
4676  N NH1 . ARG B 226 ? 0.4015 0.2366 0.5027 -0.0273 0.1230  -0.0296 235 ARG B NH1 
4677  N NH2 . ARG B 226 ? 0.4437 0.2363 0.5404 -0.0296 0.1136  -0.0245 235 ARG B NH2 
4678  N N   . GLU B 227 ? 0.4674 0.2846 0.5514 -0.0876 0.1075  -0.0400 236 GLU B N   
4679  C CA  . GLU B 227 ? 0.4766 0.2912 0.5580 -0.0921 0.1061  -0.0507 236 GLU B CA  
4680  C C   . GLU B 227 ? 0.4609 0.3061 0.5429 -0.1073 0.1079  -0.0448 236 GLU B C   
4681  O O   . GLU B 227 ? 0.4481 0.3140 0.5336 -0.1044 0.1125  -0.0513 236 GLU B O   
4682  C CB  . GLU B 227 ? 0.5197 0.2915 0.5900 -0.0979 0.0959  -0.0563 236 GLU B CB  
4683  C CG  . GLU B 227 ? 0.5603 0.3169 0.6274 -0.0894 0.0943  -0.0732 236 GLU B CG  
4684  C CD  . GLU B 227 ? 0.6382 0.3464 0.6910 -0.0899 0.0828  -0.0796 236 GLU B CD  
4685  O OE1 . GLU B 227 ? 0.6934 0.3858 0.7373 -0.0947 0.0775  -0.0896 236 GLU B OE1 
4686  O OE2 . GLU B 227 ? 0.6293 0.3139 0.6781 -0.0846 0.0785  -0.0749 236 GLU B OE2 
4687  N N   . PHE B 228 ? 0.4632 0.3143 0.5415 -0.1233 0.1043  -0.0320 237 PHE B N   
4688  C CA  . PHE B 228 ? 0.4550 0.3383 0.5332 -0.1385 0.1053  -0.0263 237 PHE B CA  
4689  C C   . PHE B 228 ? 0.4169 0.3436 0.5029 -0.1286 0.1143  -0.0225 237 PHE B C   
4690  O O   . PHE B 228 ? 0.4056 0.3601 0.4933 -0.1317 0.1173  -0.0244 237 PHE B O   
4691  C CB  . PHE B 228 ? 0.4845 0.3653 0.5555 -0.1610 0.0980  -0.0125 237 PHE B CB  
4692  C CG  . PHE B 228 ? 0.5351 0.3810 0.5938 -0.1792 0.0873  -0.0158 237 PHE B CG  
4693  C CD1 . PHE B 228 ? 0.5787 0.3863 0.6262 -0.1902 0.0772  -0.0094 237 PHE B CD1 
4694  C CD2 . PHE B 228 ? 0.5505 0.3997 0.6069 -0.1853 0.0864  -0.0252 237 PHE B CD2 
4695  C CE1 . PHE B 228 ? 0.6273 0.3979 0.6599 -0.2066 0.0656  -0.0126 237 PHE B CE1 
4696  C CE2 . PHE B 228 ? 0.5890 0.4033 0.6316 -0.2016 0.0755  -0.0289 237 PHE B CE2 
4697  C CZ  . PHE B 228 ? 0.6298 0.4033 0.6596 -0.2122 0.0647  -0.0228 237 PHE B CZ  
4698  N N   . SER B 229 ? 0.4008 0.3325 0.4900 -0.1163 0.1177  -0.0172 238 SER B N   
4699  C CA  . SER B 229 ? 0.3737 0.3408 0.4670 -0.1035 0.1250  -0.0148 238 SER B CA  
4700  C C   . SER B 229 ? 0.3572 0.3285 0.4528 -0.0893 0.1298  -0.0265 238 SER B C   
4701  O O   . SER B 229 ? 0.3410 0.3415 0.4369 -0.0824 0.1342  -0.0262 238 SER B O   
4702  C CB  . SER B 229 ? 0.3661 0.3296 0.4601 -0.0926 0.1264  -0.0084 238 SER B CB  
4703  O OG  . SER B 229 ? 0.3882 0.3559 0.4798 -0.1060 0.1226  0.0040  238 SER B OG  
4704  N N   . VAL B 230 ? 0.3620 0.3044 0.4582 -0.0846 0.1283  -0.0367 239 VAL B N   
4705  C CA  . VAL B 230 ? 0.3441 0.2893 0.4423 -0.0725 0.1322  -0.0469 239 VAL B CA  
4706  C C   . VAL B 230 ? 0.3504 0.3041 0.4480 -0.0811 0.1317  -0.0537 239 VAL B C   
4707  O O   . VAL B 230 ? 0.3461 0.3117 0.4448 -0.0742 0.1352  -0.0603 239 VAL B O   
4708  C CB  . VAL B 230 ? 0.3434 0.2595 0.4427 -0.0633 0.1308  -0.0543 239 VAL B CB  
4709  C CG1 . VAL B 230 ? 0.3334 0.2577 0.4346 -0.0501 0.1352  -0.0615 239 VAL B CG1 
4710  C CG2 . VAL B 230 ? 0.3504 0.2540 0.4497 -0.0595 0.1294  -0.0466 239 VAL B CG2 
4711  N N   . ASN B 231 ? 0.3721 0.3188 0.4669 -0.0975 0.1267  -0.0518 240 ASN B N   
4712  C CA  . ASN B 231 ? 0.3804 0.3303 0.4735 -0.1064 0.1252  -0.0595 240 ASN B CA  
4713  C C   . ASN B 231 ? 0.3798 0.3585 0.4713 -0.1224 0.1244  -0.0513 240 ASN B C   
4714  O O   . ASN B 231 ? 0.3891 0.3690 0.4777 -0.1352 0.1213  -0.0553 240 ASN B O   
4715  C CB  . ASN B 231 ? 0.4119 0.3229 0.4997 -0.1120 0.1182  -0.0674 240 ASN B CB  
4716  C CG  . ASN B 231 ? 0.4236 0.3153 0.5133 -0.0949 0.1197  -0.0790 240 ASN B CG  
4717  O OD1 . ASN B 231 ? 0.4351 0.3353 0.5268 -0.0889 0.1226  -0.0889 240 ASN B OD1 
4718  N ND2 . ASN B 231 ? 0.4580 0.3259 0.5471 -0.0874 0.1174  -0.0775 240 ASN B ND2 
4719  N N   . ALA B 232 ? 0.3676 0.3718 0.4605 -0.1215 0.1269  -0.0398 241 ALA B N   
4720  C CA  . ALA B 232 ? 0.3704 0.4092 0.4623 -0.1357 0.1264  -0.0306 241 ALA B CA  
4721  C C   . ALA B 232 ? 0.4019 0.4231 0.4882 -0.1597 0.1183  -0.0283 241 ALA B C   
4722  O O   . ALA B 232 ? 0.4112 0.4511 0.4956 -0.1738 0.1166  -0.0281 241 ALA B O   
4723  C CB  . ALA B 232 ? 0.3550 0.4257 0.4486 -0.1305 0.1310  -0.0353 241 ALA B CB  
4724  N N   . GLY B 233 ? 0.4231 0.4062 0.5051 -0.1643 0.1124  -0.0267 242 GLY B N   
4725  C CA  . GLY B 233 ? 0.4574 0.4193 0.5301 -0.1884 0.1026  -0.0218 242 GLY B CA  
4726  C C   . GLY B 233 ? 0.4812 0.4136 0.5463 -0.1975 0.0962  -0.0333 242 GLY B C   
4727  O O   . GLY B 233 ? 0.5139 0.4377 0.5694 -0.2210 0.0877  -0.0287 242 GLY B O   
4728  N N   . VAL B 234 ? 0.4691 0.3859 0.5369 -0.1800 0.0994  -0.0481 243 VAL B N   
4729  C CA  . VAL B 234 ? 0.4924 0.3773 0.5516 -0.1850 0.0928  -0.0607 243 VAL B CA  
4730  C C   . VAL B 234 ? 0.4880 0.3497 0.5499 -0.1621 0.0956  -0.0747 243 VAL B C   
4731  O O   . VAL B 234 ? 0.4621 0.3477 0.5340 -0.1460 0.1044  -0.0775 243 VAL B O   
4732  C CB  . VAL B 234 ? 0.4805 0.3947 0.5412 -0.1927 0.0952  -0.0651 243 VAL B CB  
4733  C CG1 . VAL B 234 ? 0.5190 0.4044 0.5661 -0.2116 0.0846  -0.0699 243 VAL B CG1 
4734  C CG2 . VAL B 234 ? 0.4633 0.4266 0.5296 -0.2021 0.0996  -0.0519 243 VAL B CG2 
4735  N N   . THR B 235 ? 0.5197 0.3364 0.5714 -0.1601 0.0876  -0.0835 244 THR B N   
4736  C CA  . THR B 235 ? 0.5228 0.3251 0.5777 -0.1373 0.0906  -0.0967 244 THR B CA  
4737  C C   . THR B 235 ? 0.5502 0.3262 0.5948 -0.1367 0.0843  -0.1119 244 THR B C   
4738  O O   . THR B 235 ? 0.5880 0.3376 0.6187 -0.1534 0.0741  -0.1115 244 THR B O   
4739  C CB  . THR B 235 ? 0.5408 0.3119 0.5926 -0.1271 0.0870  -0.0949 244 THR B CB  
4740  O OG1 . THR B 235 ? 0.5628 0.3245 0.6089 -0.1436 0.0813  -0.0802 244 THR B OG1 
4741  C CG2 . THR B 235 ? 0.5232 0.3136 0.5880 -0.1057 0.0967  -0.0954 244 THR B CG2 
4742  N N   . THR B 236 ? 0.5347 0.3179 0.5848 -0.1182 0.0895  -0.1250 245 THR B N   
4743  C CA  . THR B 236 ? 0.5664 0.3191 0.6059 -0.1098 0.0831  -0.1414 245 THR B CA  
4744  C C   . THR B 236 ? 0.5598 0.3020 0.6026 -0.0862 0.0852  -0.1482 245 THR B C   
4745  O O   . THR B 236 ? 0.5289 0.2960 0.5846 -0.0768 0.0938  -0.1422 245 THR B O   
4746  C CB  . THR B 236 ? 0.5659 0.3367 0.6053 -0.1125 0.0851  -0.1522 245 THR B CB  
4747  O OG1 . THR B 236 ? 0.6088 0.3768 0.6398 -0.1363 0.0790  -0.1468 245 THR B OG1 
4748  C CG2 . THR B 236 ? 0.5993 0.3429 0.6280 -0.0994 0.0794  -0.1707 245 THR B CG2 
4749  N N   . PRO B 237 ? 0.5914 0.3006 0.6220 -0.0755 0.0777  -0.1622 246 PRO B N   
4750  C CA  . PRO B 237 ? 0.6189 0.2849 0.6370 -0.0664 0.0685  -0.1651 246 PRO B CA  
4751  C C   . PRO B 237 ? 0.6265 0.2734 0.6396 -0.0831 0.0630  -0.1488 246 PRO B C   
4752  O O   . PRO B 237 ? 0.5990 0.2738 0.6243 -0.0911 0.0700  -0.1345 246 PRO B O   
4753  C CB  . PRO B 237 ? 0.5958 0.2790 0.6255 -0.0427 0.0760  -0.1687 246 PRO B CB  
4754  C CG  . PRO B 237 ? 0.5731 0.2999 0.6156 -0.0378 0.0862  -0.1748 246 PRO B CG  
4755  C CD  . PRO B 237 ? 0.5763 0.3113 0.6158 -0.0572 0.0853  -0.1741 246 PRO B CD  
4756  N N   . VAL B 238 ? 0.6664 0.2644 0.6594 -0.0884 0.0495  -0.1510 247 VAL B N   
4757  C CA  . VAL B 238 ? 0.6781 0.2523 0.6635 -0.1026 0.0426  -0.1360 247 VAL B CA  
4758  C C   . VAL B 238 ? 0.6803 0.2373 0.6665 -0.0804 0.0422  -0.1375 247 VAL B C   
4759  O O   . VAL B 238 ? 0.7126 0.2321 0.6841 -0.0645 0.0336  -0.1501 247 VAL B O   
4760  C CB  . VAL B 238 ? 0.7318 0.2579 0.6919 -0.1209 0.0265  -0.1374 247 VAL B CB  
4761  C CG1 . VAL B 238 ? 0.7663 0.2593 0.7143 -0.1349 0.0166  -0.1224 247 VAL B CG1 
4762  C CG2 . VAL B 238 ? 0.7208 0.2712 0.6821 -0.1439 0.0277  -0.1349 247 VAL B CG2 
4763  N N   . SER B 239 ? 0.6449 0.2305 0.6473 -0.0780 0.0513  -0.1254 248 SER B N   
4764  C CA  . SER B 239 ? 0.6440 0.2228 0.6502 -0.0563 0.0529  -0.1269 248 SER B CA  
4765  C C   . SER B 239 ? 0.6968 0.2202 0.6825 -0.0529 0.0388  -0.1277 248 SER B C   
4766  O O   . SER B 239 ? 0.7353 0.2231 0.7029 -0.0708 0.0270  -0.1239 248 SER B O   
4767  C CB  . SER B 239 ? 0.6071 0.2182 0.6299 -0.0587 0.0623  -0.1117 248 SER B CB  
4768  O OG  . SER B 239 ? 0.6240 0.2169 0.6393 -0.0765 0.0558  -0.0968 248 SER B OG  
4769  N N   . THR B 240 ? 0.7021 0.2175 0.6892 -0.0301 0.0391  -0.1321 249 THR B N   
4770  C CA  . THR B 240 ? 0.7522 0.2162 0.7200 -0.0251 0.0259  -0.1309 249 THR B CA  
4771  C C   . THR B 240 ? 0.7479 0.2108 0.7184 -0.0427 0.0253  -0.1104 249 THR B C   
4772  O O   . THR B 240 ? 0.7913 0.2115 0.7452 -0.0451 0.0137  -0.1048 249 THR B O   
4773  C CB  . THR B 240 ? 0.7544 0.2139 0.7230 0.0060  0.0264  -0.1412 249 THR B CB  
4774  O OG1 . THR B 240 ? 0.7295 0.2185 0.7158 0.0101  0.0357  -0.1294 249 THR B OG1 
4775  C CG2 . THR B 240 ? 0.7406 0.2274 0.7164 0.0245  0.0331  -0.1587 249 THR B CG2 
4776  N N   . TYR B 241 ? 0.6996 0.2089 0.6895 -0.0541 0.0372  -0.0990 250 TYR B N   
4777  C CA  . TYR B 241 ? 0.6999 0.2102 0.6905 -0.0721 0.0359  -0.0800 250 TYR B CA  
4778  C C   . TYR B 241 ? 0.7221 0.2218 0.7012 -0.1018 0.0284  -0.0715 250 TYR B C   
4779  O O   . TYR B 241 ? 0.7466 0.2263 0.7157 -0.1184 0.0205  -0.0577 250 TYR B O   
4780  C CB  . TYR B 241 ? 0.6515 0.2135 0.6647 -0.0706 0.0501  -0.0707 250 TYR B CB  
4781  C CG  . TYR B 241 ? 0.6449 0.2241 0.6704 -0.0457 0.0581  -0.0770 250 TYR B CG  
4782  C CD1 . TYR B 241 ? 0.6303 0.2537 0.6726 -0.0385 0.0705  -0.0810 250 TYR B CD1 
4783  C CD2 . TYR B 241 ? 0.7012 0.2540 0.7208 -0.0301 0.0528  -0.0780 250 TYR B CD2 
4784  C CE1 . TYR B 241 ? 0.6301 0.2720 0.6830 -0.0184 0.0773  -0.0854 250 TYR B CE1 
4785  C CE2 . TYR B 241 ? 0.7071 0.2817 0.7389 -0.0081 0.0605  -0.0830 250 TYR B CE2 
4786  C CZ  . TYR B 241 ? 0.6626 0.2822 0.7109 -0.0037 0.0726  -0.0865 250 TYR B CZ  
4787  O OH  . TYR B 241 ? 0.6467 0.2894 0.7058 0.0143  0.0794  -0.0903 250 TYR B OH  
4788  N N   . MET B 242 ? 0.7169 0.2325 0.6973 -0.1099 0.0307  -0.0788 251 MET B N   
4789  C CA  . MET B 242 ? 0.7416 0.2498 0.7105 -0.1397 0.0231  -0.0705 251 MET B CA  
4790  C C   . MET B 242 ? 0.8066 0.2501 0.7471 -0.1451 0.0050  -0.0755 251 MET B C   
4791  O O   . MET B 242 ? 0.8403 0.2592 0.7656 -0.1686 -0.0058 -0.0629 251 MET B O   
4792  C CB  . MET B 242 ? 0.7222 0.2631 0.6988 -0.1454 0.0297  -0.0784 251 MET B CB  
4793  C CG  . MET B 242 ? 0.6658 0.2672 0.6670 -0.1394 0.0462  -0.0750 251 MET B CG  
4794  S SD  . MET B 242 ? 0.6474 0.2842 0.6548 -0.1654 0.0489  -0.0522 251 MET B SD  
4795  C CE  . MET B 242 ? 0.5867 0.2867 0.6165 -0.1553 0.0657  -0.0552 251 MET B CE  
4796  N N   . LEU B 243 ? 0.8301 0.2467 0.7623 -0.1223 0.0014  -0.0941 252 LEU B N   
4797  C CA  . LEU B 243 ? 0.8985 0.2496 0.8009 -0.1213 -0.0165 -0.1024 252 LEU B CA  
4798  C C   . LEU B 243 ? 0.9168 0.2412 0.8138 -0.0882 -0.0191 -0.1146 252 LEU B C   
4799  O O   . LEU B 243 ? 0.8863 0.2404 0.7985 -0.0636 -0.0084 -0.1275 252 LEU B O   
4800  C CB  . LEU B 243 ? 0.9177 0.2591 0.8090 -0.1263 -0.0211 -0.1168 252 LEU B CB  
4801  C CG  . LEU B 243 ? 0.9647 0.2719 0.8324 -0.1592 -0.0360 -0.1094 252 LEU B CG  
4802  C CD1 . LEU B 243 ? 1.0147 0.2771 0.8581 -0.1523 -0.0483 -0.1287 252 LEU B CD1 
4803  C CD2 . LEU B 243 ? 1.0213 0.2840 0.8701 -0.1726 -0.0496 -0.0947 252 LEU B CD2 
4804  N N   . THR B 244 ? 0.9682 0.2373 0.8422 -0.0885 -0.0341 -0.1102 253 THR B N   
4805  C CA  . THR B 244 ? 0.9979 0.2339 0.8610 -0.0572 -0.0400 -0.1221 253 THR B CA  
4806  C C   . THR B 244 ? 1.0462 0.2405 0.8850 -0.0461 -0.0519 -0.1420 253 THR B C   
4807  O O   . THR B 244 ? 1.0789 0.2501 0.9012 -0.0688 -0.0611 -0.1422 253 THR B O   
4808  C CB  . THR B 244 ? 1.0416 0.2297 0.8857 -0.0628 -0.0534 -0.1094 253 THR B CB  
4809  O OG1 . THR B 244 ? 1.0086 0.2365 0.8741 -0.0767 -0.0429 -0.0894 253 THR B OG1 
4810  C CG2 . THR B 244 ? 1.0742 0.2286 0.9062 -0.0272 -0.0600 -0.1218 253 THR B CG2 
4811  N N   . ASN B 245 ? 1.0549 0.2420 0.8911 -0.0110 -0.0518 -0.1588 254 ASN B N   
4812  C CA  . ASN B 245 ? 1.1124 0.2539 0.9215 0.0059  -0.0651 -0.1793 254 ASN B CA  
4813  C C   . ASN B 245 ? 1.1885 0.2508 0.9586 -0.0100 -0.0884 -0.1747 254 ASN B C   
4814  O O   . ASN B 245 ? 1.2226 0.2519 0.9708 -0.0230 -0.0997 -0.1822 254 ASN B O   
4815  C CB  . ASN B 245 ? 1.1168 0.2632 0.9277 0.0476  -0.0627 -0.1950 254 ASN B CB  
4816  C CG  . ASN B 245 ? 1.1745 0.2816 0.9582 0.0705  -0.0751 -0.2189 254 ASN B CG  
4817  O OD1 . ASN B 245 ? 1.1698 0.3040 0.9600 0.0736  -0.0690 -0.2320 254 ASN B OD1 
4818  N ND2 . ASN B 245 ? 1.2347 0.2774 0.9865 0.0878  -0.0931 -0.2250 254 ASN B ND2 
4819  N N   . SER B 246 ? 1.2149 0.2472 0.9760 -0.0106 -0.0960 -0.1617 255 SER B N   
4820  C CA  . SER B 246 ? 1.2954 0.2516 1.0188 -0.0295 -0.1188 -0.1532 255 SER B CA  
4821  C C   . SER B 246 ? 1.2994 0.2525 1.0161 -0.0707 -0.1234 -0.1434 255 SER B C   
4822  O O   . SER B 246 ? 1.3627 0.2611 1.0469 -0.0812 -0.1409 -0.1509 255 SER B O   
4823  C CB  . SER B 246 ? 1.3000 0.2477 1.0256 -0.0373 -0.1207 -0.1323 255 SER B CB  
4824  O OG  . SER B 246 ? 1.2843 0.2757 1.0366 -0.0098 -0.1058 -0.1332 255 SER B OG  
4825  N N   . GLU B 247 ? 1.2344 0.2487 0.9816 -0.0937 -0.1077 -0.1268 256 GLU B N   
4826  C CA  . GLU B 247 ? 1.2323 0.2576 0.9780 -0.1335 -0.1096 -0.1151 256 GLU B CA  
4827  C C   . GLU B 247 ? 1.2313 0.2602 0.9719 -0.1338 -0.1098 -0.1326 256 GLU B C   
4828  O O   . GLU B 247 ? 1.2867 0.2647 0.9961 -0.1531 -0.1275 -0.1350 256 GLU B O   
4829  C CB  . GLU B 247 ? 1.1615 0.2605 0.9435 -0.1495 -0.0904 -0.0969 256 GLU B CB  
4830  C CG  . GLU B 247 ? 1.1876 0.2783 0.9700 -0.1560 -0.0929 -0.0775 256 GLU B CG  
4831  C CD  . GLU B 247 ? 1.1426 0.3072 0.9617 -0.1612 -0.0727 -0.0632 256 GLU B CD  
4832  O OE1 . GLU B 247 ? 1.1123 0.3329 0.9580 -0.1498 -0.0556 -0.0713 256 GLU B OE1 
4833  O OE2 . GLU B 247 ? 1.1396 0.3046 0.9590 -0.1762 -0.0748 -0.0439 256 GLU B OE2 
4834  N N   . LEU B 248 ? 1.1676 0.2552 0.9375 -0.1131 -0.0911 -0.1445 257 LEU B N   
4835  C CA  . LEU B 248 ? 1.1588 0.2569 0.9270 -0.1099 -0.0893 -0.1619 257 LEU B CA  
4836  C C   . LEU B 248 ? 1.2411 0.2620 0.9678 -0.1007 -0.1113 -0.1785 257 LEU B C   
4837  O O   . LEU B 248 ? 1.2724 0.2713 0.9807 -0.1193 -0.1209 -0.1838 257 LEU B O   
4838  C CB  . LEU B 248 ? 1.0926 0.2493 0.8908 -0.0791 -0.0698 -0.1754 257 LEU B CB  
4839  C CG  . LEU B 248 ? 1.0692 0.2342 0.8639 -0.0698 -0.0687 -0.1960 257 LEU B CG  
4840  C CD1 . LEU B 248 ? 1.0295 0.2135 0.8263 -0.1046 -0.0679 -0.1890 257 LEU B CD1 
4841  C CD2 . LEU B 248 ? 0.9901 0.2133 0.8137 -0.0399 -0.0502 -0.2071 257 LEU B CD2 
4842  N N   . LEU B 249 ? 1.2788 0.2576 0.9891 -0.0715 -0.1200 -0.1869 258 LEU B N   
4843  C CA  . LEU B 249 ? 1.3631 0.2687 1.0326 -0.0563 -0.1408 -0.2051 258 LEU B CA  
4844  C C   . LEU B 249 ? 1.4382 0.2764 1.0705 -0.0915 -0.1634 -0.1951 258 LEU B C   
4845  O O   . LEU B 249 ? 1.4854 0.2859 1.0911 -0.0976 -0.1764 -0.2080 258 LEU B O   
4846  C CB  . LEU B 249 ? 1.3897 0.2644 1.0477 -0.0164 -0.1464 -0.2153 258 LEU B CB  
4847  C CG  . LEU B 249 ? 1.3730 0.2823 1.0432 0.0235  -0.1358 -0.2400 258 LEU B CG  
4848  C CD1 . LEU B 249 ? 1.3731 0.2928 1.0515 0.0631  -0.1309 -0.2457 258 LEU B CD1 
4849  C CD2 . LEU B 249 ? 1.4595 0.3161 1.0935 0.0340  -0.1527 -0.2625 258 LEU B CD2 
4850  N N   . SER B 250 ? 1.4535 0.2771 1.0826 -0.1163 -0.1687 -0.1717 259 SER B N   
4851  C CA  . SER B 250 ? 1.5292 0.2870 1.1202 -0.1534 -0.1921 -0.1598 259 SER B CA  
4852  C C   . SER B 250 ? 1.5051 0.2991 1.1056 -0.1937 -0.1877 -0.1506 259 SER B C   
4853  O O   . SER B 250 ? 1.5652 0.3088 1.1324 -0.2217 -0.2069 -0.1487 259 SER B O   
4854  C CB  . SER B 250 ? 1.5513 0.2830 1.1342 -0.1690 -0.2001 -0.1366 259 SER B CB  
4855  O OG  . SER B 250 ? 1.4912 0.2886 1.1063 -0.1996 -0.1850 -0.1135 259 SER B OG  
4856  N N   . LEU B 251 ? 1.4165 0.2978 1.0613 -0.1961 -0.1631 -0.1448 260 LEU B N   
4857  C CA  . LEU B 251 ? 1.3852 0.3109 1.0430 -0.2273 -0.1563 -0.1389 260 LEU B CA  
4858  C C   . LEU B 251 ? 1.4123 0.3182 1.0535 -0.2198 -0.1625 -0.1614 260 LEU B C   
4859  O O   . LEU B 251 ? 1.4415 0.3315 1.0650 -0.2513 -0.1731 -0.1581 260 LEU B O   
4860  C CB  . LEU B 251 ? 1.2911 0.3102 0.9973 -0.2222 -0.1289 -0.1324 260 LEU B CB  
4861  C CG  . LEU B 251 ? 1.2615 0.3209 0.9848 -0.2544 -0.1226 -0.1051 260 LEU B CG  
4862  C CD1 . LEU B 251 ? 1.1873 0.3364 0.9542 -0.2476 -0.0970 -0.1033 260 LEU B CD1 
4863  C CD2 . LEU B 251 ? 1.2984 0.3354 0.9982 -0.2987 -0.1380 -0.0929 260 LEU B CD2 
4864  N N   . ILE B 252 ? 1.4041 0.3152 1.0516 -0.1781 -0.1555 -0.1840 261 ILE B N   
4865  C CA  . ILE B 252 ? 1.4382 0.3296 1.0687 -0.1653 -0.1616 -0.2076 261 ILE B CA  
4866  C C   . ILE B 252 ? 1.5464 0.3436 1.1246 -0.1805 -0.1910 -0.2106 261 ILE B C   
4867  O O   . ILE B 252 ? 1.5815 0.3594 1.1405 -0.2060 -0.2015 -0.2131 261 ILE B O   
4868  C CB  . ILE B 252 ? 1.4199 0.3193 1.0577 -0.1155 -0.1540 -0.2304 261 ILE B CB  
4869  C CG1 . ILE B 252 ? 1.3313 0.3228 1.0160 -0.1039 -0.1267 -0.2318 261 ILE B CG1 
4870  C CG2 . ILE B 252 ? 1.4742 0.3216 1.0776 -0.0988 -0.1696 -0.2557 261 ILE B CG2 
4871  C CD1 . ILE B 252 ? 1.3031 0.3194 1.0061 -0.0633 -0.1151 -0.2405 261 ILE B CD1 
4872  N N   . ASN B 253 ? 1.6069 0.3445 1.1611 -0.1657 -0.2050 -0.2094 262 ASN B N   
4873  C CA  . ASN B 253 ? 1.7184 0.3578 1.2189 -0.1781 -0.2351 -0.2111 262 ASN B CA  
4874  C C   . ASN B 253 ? 1.7521 0.3763 1.2360 -0.2322 -0.2471 -0.1938 262 ASN B C   
4875  O O   . ASN B 253 ? 1.8291 0.3876 1.2714 -0.2450 -0.2691 -0.2027 262 ASN B O   
4876  C CB  . ASN B 253 ? 1.7540 0.3469 1.2391 -0.1672 -0.2454 -0.2010 262 ASN B CB  
4877  C CG  . ASN B 253 ? 1.8696 0.3558 1.2977 -0.1522 -0.2751 -0.2150 262 ASN B CG  
4878  O OD1 . ASN B 253 ? 1.9266 0.3702 1.3244 -0.1491 -0.2890 -0.2334 262 ASN B OD1 
4879  N ND2 . ASN B 253 ? 1.9349 0.3758 1.3463 -0.1415 -0.2857 -0.2068 262 ASN B ND2 
4880  N N   . ASP B 254 ? 1.7005 0.3879 1.2164 -0.2633 -0.2328 -0.1695 263 ASP B N   
4881  C CA  . ASP B 254 ? 1.7285 0.4121 1.2318 -0.3168 -0.2431 -0.1491 263 ASP B CA  
4882  C C   . ASP B 254 ? 1.7032 0.4290 1.2167 -0.3350 -0.2364 -0.1559 263 ASP B C   
4883  O O   . ASP B 254 ? 1.7293 0.4488 1.2279 -0.3790 -0.2471 -0.1422 263 ASP B O   
4884  C CB  . ASP B 254 ? 1.6853 0.4216 1.2171 -0.3412 -0.2313 -0.1198 263 ASP B CB  
4885  C CG  . ASP B 254 ? 1.7155 0.4646 1.2396 -0.3966 -0.2391 -0.0972 263 ASP B CG  
4886  O OD1 . ASP B 254 ? 1.8357 0.5123 1.3152 -0.4235 -0.2650 -0.0944 263 ASP B OD1 
4887  O OD2 . ASP B 254 ? 1.6558 0.4876 1.2169 -0.4134 -0.2201 -0.0823 263 ASP B OD2 
4888  N N   . MET B 255 ? 1.6543 0.4243 1.1923 -0.3023 -0.2193 -0.1764 264 MET B N   
4889  C CA  . MET B 255 ? 1.6255 0.4429 1.1772 -0.3169 -0.2105 -0.1825 264 MET B CA  
4890  C C   . MET B 255 ? 1.7054 0.4537 1.2123 -0.3271 -0.2337 -0.1979 264 MET B C   
4891  O O   . MET B 255 ? 1.7645 0.4444 1.2397 -0.2991 -0.2485 -0.2169 264 MET B O   
4892  C CB  . MET B 255 ? 1.5510 0.4362 1.1416 -0.2794 -0.1857 -0.1988 264 MET B CB  
4893  C CG  . MET B 255 ? 1.4784 0.4289 1.1115 -0.2664 -0.1633 -0.1854 264 MET B CG  
4894  S SD  . MET B 255 ? 1.3912 0.4193 1.0668 -0.2265 -0.1358 -0.2028 264 MET B SD  
4895  C CE  . MET B 255 ? 1.4711 0.4435 1.1136 -0.1993 -0.1500 -0.2350 264 MET B CE  
4896  N N   . PRO B 256 ? 1.7126 0.4793 1.2157 -0.3666 -0.2373 -0.1901 265 PRO B N   
4897  C CA  . PRO B 256 ? 1.7911 0.4966 1.2514 -0.3844 -0.2599 -0.2022 265 PRO B CA  
4898  C C   . PRO B 256 ? 1.7905 0.4969 1.2493 -0.3496 -0.2556 -0.2330 265 PRO B C   
4899  O O   . PRO B 256 ? 1.7755 0.5129 1.2391 -0.3653 -0.2522 -0.2386 265 PRO B O   
4900  C CB  . PRO B 256 ? 1.7719 0.5264 1.2431 -0.4354 -0.2574 -0.1818 265 PRO B CB  
4901  C CG  . PRO B 256 ? 1.6715 0.5262 1.1974 -0.4292 -0.2280 -0.1702 265 PRO B CG  
4902  C CD  . PRO B 256 ? 1.6536 0.4999 1.1907 -0.4009 -0.2219 -0.1659 265 PRO B CD  
4903  N N   . ILE B 257 ? 1.8112 0.4846 1.2621 -0.3028 -0.2566 -0.2527 266 ILE B N   
4904  C CA  . ILE B 257 ? 1.8158 0.4913 1.2646 -0.2640 -0.2525 -0.2830 266 ILE B CA  
4905  C C   . ILE B 257 ? 1.9067 0.4859 1.3062 -0.2329 -0.2763 -0.3052 266 ILE B C   
4906  O O   . ILE B 257 ? 1.9657 0.4762 1.3351 -0.2349 -0.2944 -0.2976 266 ILE B O   
4907  C CB  . ILE B 257 ? 1.7203 0.4836 1.2215 -0.2278 -0.2219 -0.2886 266 ILE B CB  
4908  C CG1 . ILE B 257 ? 1.6943 0.4608 1.2108 -0.2083 -0.2150 -0.2776 266 ILE B CG1 
4909  C CG2 . ILE B 257 ? 1.6441 0.4996 1.1881 -0.2524 -0.1999 -0.2751 266 ILE B CG2 
4910  C CD1 . ILE B 257 ? 1.6289 0.4492 1.1787 -0.1618 -0.1937 -0.2914 266 ILE B CD1 
4911  N N   . THR B 258 ? 1.9177 0.4940 1.3087 -0.2025 -0.2762 -0.3330 267 THR B N   
4912  C CA  . THR B 258 ? 1.9998 0.4926 1.3449 -0.1665 -0.2972 -0.3577 267 THR B CA  
4913  C C   . THR B 258 ? 1.9865 0.4752 1.3407 -0.1256 -0.2917 -0.3597 267 THR B C   
4914  O O   . THR B 258 ? 1.9075 0.4637 1.3062 -0.1229 -0.2696 -0.3444 267 THR B O   
4915  C CB  . THR B 258 ? 2.0045 0.5088 1.3435 -0.1388 -0.2952 -0.3880 267 THR B CB  
4916  O OG1 . THR B 258 ? 1.9805 0.5137 1.3365 -0.0842 -0.2820 -0.4068 267 THR B OG1 
4917  C CG2 . THR B 258 ? 1.9360 0.5217 1.3104 -0.1655 -0.2765 -0.3825 267 THR B CG2 
4918  N N   . ASN B 259 ? 2.0652 0.4741 1.3756 -0.0929 -0.3125 -0.3789 268 ASN B N   
4919  C CA  . ASN B 259 ? 2.0620 0.4637 1.3772 -0.0535 -0.3093 -0.3814 268 ASN B CA  
4920  C C   . ASN B 259 ? 1.9922 0.4683 1.3450 -0.0057 -0.2854 -0.3983 268 ASN B C   
4921  O O   . ASN B 259 ? 1.9408 0.4564 1.3232 0.0120  -0.2706 -0.3894 268 ASN B O   
4922  C CB  . ASN B 259 ? 2.1781 0.4661 1.4310 -0.0347 -0.3413 -0.3944 268 ASN B CB  
4923  C CG  . ASN B 259 ? 2.2331 0.4627 1.4644 -0.0667 -0.3578 -0.3690 268 ASN B CG  
4924  O OD1 . ASN B 259 ? 2.2001 0.4732 1.4606 -0.1076 -0.3466 -0.3416 268 ASN B OD1 
4925  N ND2 . ASN B 259 ? 2.3391 0.4707 1.5183 -0.0475 -0.3847 -0.3777 268 ASN B ND2 
4926  N N   . ASP B 260 ? 1.9936 0.4875 1.3431 0.0144  -0.2827 -0.4225 269 ASP B N   
4927  C CA  . ASP B 260 ? 1.9258 0.4995 1.3121 0.0552  -0.2592 -0.4381 269 ASP B CA  
4928  C C   . ASP B 260 ? 1.8097 0.4826 1.2556 0.0335  -0.2299 -0.4170 269 ASP B C   
4929  O O   . ASP B 260 ? 1.7458 0.4805 1.2280 0.0577  -0.2101 -0.4149 269 ASP B O   
4930  C CB  . ASP B 260 ? 1.9516 0.5290 1.3231 0.0711  -0.2622 -0.4650 269 ASP B CB  
4931  C CG  . ASP B 260 ? 2.0845 0.5654 1.3951 0.0997  -0.2913 -0.4901 269 ASP B CG  
4932  O OD1 . ASP B 260 ? 2.1643 0.5907 1.4508 0.1225  -0.3044 -0.4913 269 ASP B OD1 
4933  O OD2 . ASP B 260 ? 2.1598 0.6186 1.4453 0.1009  -0.3013 -0.5092 269 ASP B OD2 
4934  N N   . GLN B 261 ? 1.7833 0.4691 1.2366 -0.0129 -0.2287 -0.4012 270 GLN B N   
4935  C CA  . GLN B 261 ? 1.6867 0.4572 1.1902 -0.0370 -0.2043 -0.3800 270 GLN B CA  
4936  C C   . GLN B 261 ? 1.6458 0.4303 1.1702 -0.0328 -0.1960 -0.3610 270 GLN B C   
4937  O O   . GLN B 261 ? 1.5720 0.4268 1.1368 -0.0138 -0.1737 -0.3582 270 GLN B O   
4938  C CB  . GLN B 261 ? 1.6971 0.4625 1.1954 -0.0890 -0.2101 -0.3639 270 GLN B CB  
4939  C CG  . GLN B 261 ? 1.6328 0.4908 1.1758 -0.1032 -0.1858 -0.3572 270 GLN B CG  
4940  C CD  . GLN B 261 ? 1.6830 0.5378 1.2150 -0.1442 -0.1930 -0.3521 270 GLN B CD  
4941  O OE1 . GLN B 261 ? 1.6513 0.5682 1.2152 -0.1718 -0.1779 -0.3345 270 GLN B OE1 
4942  N NE2 . GLN B 261 ? 1.7681 0.5513 1.2541 -0.1479 -0.2163 -0.3677 270 GLN B NE2 
4943  N N   . LYS B 262 ? 1.6931 0.4089 1.1883 -0.0498 -0.2148 -0.3482 271 LYS B N   
4944  C CA  . LYS B 262 ? 1.6588 0.3861 1.1724 -0.0467 -0.2079 -0.3298 271 LYS B CA  
4945  C C   . LYS B 262 ? 1.6311 0.3832 1.1590 0.0043  -0.1974 -0.3446 271 LYS B C   
4946  O O   . LYS B 262 ? 1.5606 0.3765 1.1283 0.0114  -0.1770 -0.3337 271 LYS B O   
4947  C CB  . LYS B 262 ? 1.7332 0.3739 1.2067 -0.0672 -0.2327 -0.3168 271 LYS B CB  
4948  C CG  . LYS B 262 ? 1.7482 0.3794 1.2147 -0.1229 -0.2402 -0.2957 271 LYS B CG  
4949  C CD  . LYS B 262 ? 1.8257 0.3806 1.2569 -0.1477 -0.2629 -0.2780 271 LYS B CD  
4950  C CE  . LYS B 262 ? 1.8915 0.3945 1.2862 -0.1930 -0.2844 -0.2718 271 LYS B CE  
4951  N NZ  . LYS B 262 ? 1.9388 0.3827 1.3053 -0.2278 -0.3041 -0.2482 271 LYS B NZ  
4952  N N   . LYS B 263 ? 1.6880 0.3925 1.1829 0.0398  -0.2115 -0.3701 272 LYS B N   
4953  C CA  . LYS B 263 ? 1.6726 0.3992 1.1768 0.0900  -0.2038 -0.3855 272 LYS B CA  
4954  C C   . LYS B 263 ? 1.5706 0.3993 1.1239 0.1029  -0.1755 -0.3889 272 LYS B C   
4955  O O   . LYS B 263 ? 1.5252 0.4000 1.1054 0.1266  -0.1611 -0.3863 272 LYS B O   
4956  C CB  . LYS B 263 ? 1.7645 0.4246 1.2217 0.1260  -0.2248 -0.4143 272 LYS B CB  
4957  C CG  . LYS B 263 ? 1.7838 0.4758 1.2494 0.1813  -0.2167 -0.4341 272 LYS B CG  
4958  C CD  . LYS B 263 ? 1.9221 0.5613 1.3435 0.2152  -0.2354 -0.4651 272 LYS B CD  
4959  C CE  . LYS B 263 ? 1.9588 0.6107 1.3769 0.2722  -0.2340 -0.4838 272 LYS B CE  
4960  N NZ  . LYS B 263 ? 2.0741 0.6557 1.4390 0.3064  -0.2578 -0.5133 272 LYS B NZ  
4961  N N   . LEU B 264 ? 1.5346 0.3973 1.0979 0.0867  -0.1685 -0.3943 273 LEU B N   
4962  C CA  . LEU B 264 ? 1.4373 0.3945 1.0450 0.0950  -0.1429 -0.3963 273 LEU B CA  
4963  C C   . LEU B 264 ? 1.3602 0.3744 1.0094 0.0750  -0.1239 -0.3705 273 LEU B C   
4964  O O   . LEU B 264 ? 1.3016 0.3742 0.9818 0.0962  -0.1067 -0.3694 273 LEU B O   
4965  C CB  . LEU B 264 ? 1.4257 0.4032 1.0351 0.0732  -0.1404 -0.4020 273 LEU B CB  
4966  C CG  . LEU B 264 ? 1.3210 0.3925 0.9733 0.0782  -0.1155 -0.4032 273 LEU B CG  
4967  C CD1 . LEU B 264 ? 1.3148 0.4092 0.9659 0.1235  -0.1118 -0.4274 273 LEU B CD1 
4968  C CD2 . LEU B 264 ? 1.3013 0.3846 0.9533 0.0485  -0.1152 -0.4033 273 LEU B CD2 
4969  N N   . MET B 265 ? 1.3575 0.3547 1.0058 0.0336  -0.1280 -0.3497 274 MET B N   
4970  C CA  . MET B 265 ? 1.2937 0.3382 0.9767 0.0128  -0.1125 -0.3246 274 MET B CA  
4971  C C   . MET B 265 ? 1.2913 0.3319 0.9809 0.0355  -0.1102 -0.3187 274 MET B C   
4972  O O   . MET B 265 ? 1.2316 0.3345 0.9568 0.0435  -0.0912 -0.3107 274 MET B O   
4973  C CB  . MET B 265 ? 1.3045 0.3233 0.9782 -0.0332 -0.1210 -0.3043 274 MET B CB  
4974  C CG  . MET B 265 ? 1.2824 0.3296 0.9619 -0.0577 -0.1170 -0.3061 274 MET B CG  
4975  S SD  . MET B 265 ? 1.2814 0.3235 0.9587 -0.1141 -0.1225 -0.2800 274 MET B SD  
4976  C CE  . MET B 265 ? 1.2044 0.3199 0.9283 -0.1206 -0.0994 -0.2556 274 MET B CE  
4977  N N   . SER B 266 ? 1.3658 0.3322 1.0195 0.0470  -0.1303 -0.3233 275 SER B N   
4978  C CA  . SER B 266 ? 1.3707 0.3298 1.0279 0.0695  -0.1297 -0.3181 275 SER B CA  
4979  C C   . SER B 266 ? 1.3393 0.3506 1.0176 0.1110  -0.1155 -0.3328 275 SER B C   
4980  O O   . SER B 266 ? 1.2987 0.3459 1.0014 0.1207  -0.1037 -0.3225 275 SER B O   
4981  C CB  . SER B 266 ? 1.4613 0.3269 1.0713 0.0784  -0.1557 -0.3236 275 SER B CB  
4982  O OG  . SER B 266 ? 1.5038 0.3204 1.0913 0.0373  -0.1704 -0.3102 275 SER B OG  
4983  N N   . ASN B 267 ? 1.3636 0.3817 1.0323 0.1349  -0.1167 -0.3565 276 ASN B N   
4984  C CA  . ASN B 267 ? 1.3398 0.4125 1.0274 0.1745  -0.1038 -0.3708 276 ASN B CA  
4985  C C   . ASN B 267 ? 1.2521 0.4170 0.9845 0.1665  -0.0790 -0.3648 276 ASN B C   
4986  O O   . ASN B 267 ? 1.2269 0.4414 0.9735 0.1950  -0.0687 -0.3780 276 ASN B O   
4987  C CB  . ASN B 267 ? 1.4011 0.4435 1.0571 0.2099  -0.1166 -0.4000 276 ASN B CB  
4988  C CG  . ASN B 267 ? 1.5014 0.4658 1.1170 0.2357  -0.1384 -0.4089 276 ASN B CG  
4989  O OD1 . ASN B 267 ? 1.5262 0.4899 1.1477 0.2492  -0.1372 -0.4003 276 ASN B OD1 
4990  N ND2 . ASN B 267 ? 1.5988 0.4959 1.1713 0.2437  -0.1591 -0.4268 276 ASN B ND2 
4991  N N   . ASN B 268 ? 1.2120 0.3996 0.9651 0.1284  -0.0701 -0.3445 277 ASN B N   
4992  C CA  . ASN B 268 ? 1.1348 0.4016 0.9258 0.1165  -0.0488 -0.3378 277 ASN B CA  
4993  C C   . ASN B 268 ? 1.0828 0.3800 0.9006 0.0857  -0.0373 -0.3121 277 ASN B C   
4994  O O   . ASN B 268 ? 1.0312 0.3807 0.8735 0.0693  -0.0234 -0.3055 277 ASN B O   
4995  C CB  . ASN B 268 ? 1.1396 0.4112 0.9237 0.1040  -0.0502 -0.3486 277 ASN B CB  
4996  C CG  . ASN B 268 ? 1.1552 0.4381 0.9298 0.1373  -0.0514 -0.3738 277 ASN B CG  
4997  O OD1 . ASN B 268 ? 1.1106 0.4594 0.9107 0.1510  -0.0357 -0.3781 277 ASN B OD1 
4998  N ND2 . ASN B 268 ? 1.2369 0.4552 0.9729 0.1513  -0.0709 -0.3908 277 ASN B ND2 
4999  N N   . VAL B 269 ? 1.0980 0.3611 0.9092 0.0789  -0.0439 -0.2981 278 VAL B N   
5000  C CA  . VAL B 269 ? 1.0560 0.3434 0.8893 0.0524  -0.0347 -0.2737 278 VAL B CA  
5001  C C   . VAL B 269 ? 0.9785 0.3441 0.8493 0.0460  -0.0132 -0.2663 278 VAL B C   
5002  O O   . VAL B 269 ? 0.9511 0.3383 0.8351 0.0175  -0.0070 -0.2512 278 VAL B O   
5003  C CB  . VAL B 269 ? 1.0639 0.3329 0.8967 0.0644  -0.0373 -0.2641 278 VAL B CB  
5004  C CG1 . VAL B 269 ? 1.1183 0.3126 0.9190 0.0504  -0.0572 -0.2579 278 VAL B CG1 
5005  C CG2 . VAL B 269 ? 1.0826 0.3622 0.9150 0.1056  -0.0357 -0.2807 278 VAL B CG2 
5006  N N   . GLN B 270 ? 0.9445 0.3532 0.8311 0.0724  -0.0026 -0.2763 279 GLN B N   
5007  C CA  . GLN B 270 ? 0.8750 0.3526 0.7941 0.0667  0.0161  -0.2682 279 GLN B CA  
5008  C C   . GLN B 270 ? 0.8465 0.3452 0.7714 0.0423  0.0205  -0.2665 279 GLN B C   
5009  O O   . GLN B 270 ? 0.8128 0.3318 0.7518 0.0180  0.0272  -0.2498 279 GLN B O   
5010  C CB  . GLN B 270 ? 0.8609 0.3790 0.7911 0.0971  0.0244  -0.2812 279 GLN B CB  
5011  C CG  . GLN B 270 ? 0.8312 0.4079 0.7916 0.0953  0.0407  -0.2684 279 GLN B CG  
5012  C CD  . GLN B 270 ? 0.8624 0.4847 0.8336 0.1208  0.0487  -0.2800 279 GLN B CD  
5013  O OE1 . GLN B 270 ? 0.9039 0.5334 0.8669 0.1344  0.0466  -0.2974 279 GLN B OE1 
5014  N NE2 . GLN B 270 ? 0.8342 0.4899 0.8234 0.1270  0.0576  -0.2702 279 GLN B NE2 
5015  N N   . ILE B 271 ? 0.8570 0.3510 0.7697 0.0500  0.0163  -0.2842 280 ILE B N   
5016  C CA  . ILE B 271 ? 0.8337 0.3452 0.7492 0.0292  0.0190  -0.2848 280 ILE B CA  
5017  C C   . ILE B 271 ? 0.8420 0.3272 0.7509 -0.0039 0.0127  -0.2687 280 ILE B C   
5018  O O   . ILE B 271 ? 0.8040 0.3249 0.7306 -0.0247 0.0221  -0.2550 280 ILE B O   
5019  C CB  . ILE B 271 ? 0.8741 0.3630 0.7677 0.0417  0.0095  -0.3072 280 ILE B CB  
5020  C CG1 . ILE B 271 ? 0.8601 0.3779 0.7588 0.0764  0.0149  -0.3237 280 ILE B CG1 
5021  C CG2 . ILE B 271 ? 0.8570 0.3644 0.7529 0.0197  0.0120  -0.3081 280 ILE B CG2 
5022  C CD1 . ILE B 271 ? 0.8130 0.3913 0.7304 0.0783  0.0280  -0.3295 280 ILE B CD1 
5023  N N   . VAL B 272 ? 0.8939 0.3165 0.7754 -0.0083 -0.0039 -0.2699 281 VAL B N   
5024  C CA  . VAL B 272 ? 0.9095 0.3051 0.7815 -0.0412 -0.0119 -0.2541 281 VAL B CA  
5025  C C   . VAL B 272 ? 0.8594 0.2983 0.7581 -0.0564 0.0011  -0.2326 281 VAL B C   
5026  O O   . VAL B 272 ? 0.8433 0.3075 0.7510 -0.0816 0.0056  -0.2215 281 VAL B O   
5027  C CB  . VAL B 272 ? 0.9697 0.2946 0.8123 -0.0406 -0.0302 -0.2531 281 VAL B CB  
5028  C CG1 . VAL B 272 ? 0.9814 0.2788 0.8111 -0.0781 -0.0402 -0.2368 281 VAL B CG1 
5029  C CG2 . VAL B 272 ? 1.0208 0.2986 0.8341 -0.0171 -0.0441 -0.2767 281 VAL B CG2 
5030  N N   . ARG B 273 ? 0.8393 0.2880 0.7499 -0.0399 0.0071  -0.2271 282 ARG B N   
5031  C CA  . ARG B 273 ? 0.7946 0.2801 0.7279 -0.0521 0.0183  -0.2073 282 ARG B CA  
5032  C C   . ARG B 273 ? 0.7483 0.2959 0.7058 -0.0573 0.0339  -0.2051 282 ARG B C   
5033  O O   . ARG B 273 ? 0.7288 0.3009 0.6965 -0.0790 0.0389  -0.1907 282 ARG B O   
5034  C CB  . ARG B 273 ? 0.7772 0.2636 0.7185 -0.0313 0.0220  -0.2039 282 ARG B CB  
5035  C CG  . ARG B 273 ? 0.8108 0.2375 0.7291 -0.0273 0.0069  -0.2030 282 ARG B CG  
5036  C CD  . ARG B 273 ? 0.7781 0.2164 0.7094 -0.0179 0.0127  -0.1916 282 ARG B CD  
5037  N NE  . ARG B 273 ? 0.8258 0.2101 0.7361 -0.0068 -0.0008 -0.1928 282 ARG B NE  
5038  C CZ  . ARG B 273 ? 0.8531 0.2153 0.7590 -0.0195 -0.0060 -0.1765 282 ARG B CZ  
5039  N NH1 . ARG B 273 ? 0.8089 0.2015 0.7306 -0.0435 0.0017  -0.1580 282 ARG B NH1 
5040  N NH2 . ARG B 273 ? 0.9180 0.2287 0.8027 -0.0067 -0.0191 -0.1789 282 ARG B NH2 
5041  N N   . GLN B 274 ? 0.7366 0.3099 0.7017 -0.0373 0.0407  -0.2193 283 GLN B N   
5042  C CA  . GLN B 274 ? 0.6981 0.3258 0.6830 -0.0421 0.0539  -0.2176 283 GLN B CA  
5043  C C   . GLN B 274 ? 0.7012 0.3311 0.6803 -0.0662 0.0508  -0.2162 283 GLN B C   
5044  O O   . GLN B 274 ? 0.6667 0.3383 0.6610 -0.0773 0.0603  -0.2087 283 GLN B O   
5045  C CB  . GLN B 274 ? 0.6892 0.3411 0.6798 -0.0181 0.0597  -0.2336 283 GLN B CB  
5046  C CG  . GLN B 274 ? 0.7238 0.3798 0.7211 0.0037  0.0629  -0.2334 283 GLN B CG  
5047  C CD  . GLN B 274 ? 0.7769 0.4559 0.7772 0.0279  0.0668  -0.2492 283 GLN B CD  
5048  O OE1 . GLN B 274 ? 0.8310 0.5121 0.8237 0.0315  0.0645  -0.2633 283 GLN B OE1 
5049  N NE2 . GLN B 274 ? 0.7567 0.4562 0.7681 0.0446  0.0727  -0.2469 283 GLN B NE2 
5050  N N   . GLN B 275 ? 0.7477 0.3311 0.7033 -0.0745 0.0366  -0.2229 284 GLN B N   
5051  C CA  . GLN B 275 ? 0.7589 0.3441 0.7074 -0.0979 0.0328  -0.2222 284 GLN B CA  
5052  C C   . GLN B 275 ? 0.7598 0.3369 0.7052 -0.1267 0.0282  -0.2033 284 GLN B C   
5053  O O   . GLN B 275 ? 0.7657 0.3487 0.7059 -0.1499 0.0249  -0.1998 284 GLN B O   
5054  C CB  . GLN B 275 ? 0.8153 0.3566 0.7380 -0.0936 0.0192  -0.2405 284 GLN B CB  
5055  C CG  . GLN B 275 ? 0.8238 0.3917 0.7519 -0.0736 0.0256  -0.2585 284 GLN B CG  
5056  C CD  . GLN B 275 ? 0.9149 0.4392 0.8155 -0.0687 0.0115  -0.2774 284 GLN B CD  
5057  O OE1 . GLN B 275 ? 0.9778 0.4446 0.8541 -0.0651 -0.0032 -0.2816 284 GLN B OE1 
5058  N NE2 . GLN B 275 ? 0.9141 0.4628 0.8162 -0.0683 0.0148  -0.2890 284 GLN B NE2 
5059  N N   . SER B 276 ? 0.7526 0.3197 0.7014 -0.1260 0.0281  -0.1908 285 SER B N   
5060  C CA  . SER B 276 ? 0.7663 0.3239 0.7099 -0.1533 0.0224  -0.1722 285 SER B CA  
5061  C C   . SER B 276 ? 0.7160 0.3254 0.6838 -0.1586 0.0360  -0.1553 285 SER B C   
5062  O O   . SER B 276 ? 0.6786 0.3205 0.6649 -0.1392 0.0483  -0.1570 285 SER B O   
5063  C CB  . SER B 276 ? 0.8099 0.3100 0.7337 -0.1522 0.0089  -0.1693 285 SER B CB  
5064  O OG  . SER B 276 ? 0.8583 0.3097 0.7593 -0.1382 -0.0031 -0.1877 285 SER B OG  
5065  N N   . TYR B 277 ? 0.7199 0.3371 0.6858 -0.1850 0.0329  -0.1389 286 TYR B N   
5066  C CA  . TYR B 277 ? 0.6797 0.3459 0.6655 -0.1904 0.0443  -0.1229 286 TYR B CA  
5067  C C   . TYR B 277 ? 0.7005 0.3480 0.6802 -0.2029 0.0381  -0.1068 286 TYR B C   
5068  O O   . TYR B 277 ? 0.7587 0.3585 0.7173 -0.2157 0.0238  -0.1057 286 TYR B O   
5069  C CB  . TYR B 277 ? 0.6662 0.3716 0.6565 -0.2115 0.0473  -0.1169 286 TYR B CB  
5070  C CG  . TYR B 277 ? 0.6528 0.3876 0.6522 -0.2007 0.0555  -0.1296 286 TYR B CG  
5071  C CD1 . TYR B 277 ? 0.7047 0.4133 0.6914 -0.1975 0.0489  -0.1463 286 TYR B CD1 
5072  C CD2 . TYR B 277 ? 0.6244 0.4127 0.6435 -0.1936 0.0691  -0.1250 286 TYR B CD2 
5073  C CE1 . TYR B 277 ? 0.7046 0.4431 0.6999 -0.1882 0.0566  -0.1576 286 TYR B CE1 
5074  C CE2 . TYR B 277 ? 0.6243 0.4396 0.6509 -0.1842 0.0762  -0.1358 286 TYR B CE2 
5075  C CZ  . TYR B 277 ? 0.6545 0.4464 0.6700 -0.1823 0.0702  -0.1517 286 TYR B CZ  
5076  O OH  . TYR B 277 ? 0.6535 0.4737 0.6762 -0.1741 0.0771  -0.1617 286 TYR B OH  
5077  N N   . SER B 278 ? 0.6632 0.3463 0.6595 -0.1997 0.0479  -0.0940 287 SER B N   
5078  C CA  . SER B 278 ? 0.6769 0.3524 0.6689 -0.2150 0.0429  -0.0766 287 SER B CA  
5079  C C   . SER B 278 ? 0.6443 0.3775 0.6507 -0.2269 0.0520  -0.0623 287 SER B C   
5080  O O   . SER B 278 ? 0.6056 0.3780 0.6292 -0.2110 0.0645  -0.0632 287 SER B O   
5081  C CB  . SER B 278 ? 0.6747 0.3305 0.6698 -0.1953 0.0443  -0.0752 287 SER B CB  
5082  O OG  . SER B 278 ? 0.6867 0.3408 0.6790 -0.2104 0.0404  -0.0572 287 SER B OG  
5083  N N   . ILE B 279 ? 0.6689 0.4080 0.6668 -0.2551 0.0449  -0.0492 288 ILE B N   
5084  C CA  . ILE B 279 ? 0.6498 0.4477 0.6600 -0.2663 0.0527  -0.0355 288 ILE B CA  
5085  C C   . ILE B 279 ? 0.6680 0.4714 0.6773 -0.2775 0.0502  -0.0173 288 ILE B C   
5086  O O   . ILE B 279 ? 0.7177 0.4834 0.7105 -0.2962 0.0375  -0.0099 288 ILE B O   
5087  C CB  . ILE B 279 ? 0.6649 0.4781 0.6669 -0.2940 0.0466  -0.0314 288 ILE B CB  
5088  C CG1 . ILE B 279 ? 0.6797 0.4626 0.6715 -0.2926 0.0412  -0.0490 288 ILE B CG1 
5089  C CG2 . ILE B 279 ? 0.6346 0.5176 0.6523 -0.2966 0.0576  -0.0220 288 ILE B CG2 
5090  C CD1 . ILE B 279 ? 0.6554 0.4833 0.6588 -0.2880 0.0506  -0.0562 288 ILE B CD1 
5091  N N   . MET B 280 ? 0.6409 0.4914 0.6660 -0.2670 0.0616  -0.0094 289 MET B N   
5092  C CA  . MET B 280 ? 0.6534 0.5131 0.6789 -0.2745 0.0604  0.0072  289 MET B CA  
5093  C C   . MET B 280 ? 0.6761 0.5609 0.6941 -0.3072 0.0538  0.0218  289 MET B C   
5094  O O   . MET B 280 ? 0.6625 0.5877 0.6854 -0.3140 0.0578  0.0212  289 MET B O   
5095  C CB  . MET B 280 ? 0.6104 0.5157 0.6532 -0.2530 0.0740  0.0100  289 MET B CB  
5096  C CG  . MET B 280 ? 0.6198 0.5298 0.6641 -0.2525 0.0742  0.0237  289 MET B CG  
5097  S SD  . MET B 280 ? 0.5959 0.5652 0.6571 -0.2298 0.0889  0.0275  289 MET B SD  
5098  C CE  . MET B 280 ? 0.5836 0.6131 0.6489 -0.2405 0.0933  0.0299  289 MET B CE  
5099  N N   . SER B 281 ? 0.7189 0.5808 0.7243 -0.3281 0.0432  0.0354  290 SER B N   
5100  C CA  . SER B 281 ? 0.7531 0.6401 0.7498 -0.3632 0.0355  0.0515  290 SER B CA  
5101  C C   . SER B 281 ? 0.7370 0.6785 0.7425 -0.3698 0.0408  0.0705  290 SER B C   
5102  O O   . SER B 281 ? 0.7144 0.7189 0.7298 -0.3736 0.0482  0.0760  290 SER B O   
5103  C CB  . SER B 281 ? 0.8168 0.6414 0.7886 -0.3892 0.0171  0.0549  290 SER B CB  
5104  O OG  . SER B 281 ? 0.8571 0.7077 0.8195 -0.4264 0.0089  0.0733  290 SER B OG  
5105  N N   . ILE B 282 ? 0.7544 0.6739 0.7555 -0.3709 0.0367  0.0805  291 ILE B N   
5106  C CA  . ILE B 282 ? 0.7361 0.7082 0.7465 -0.3720 0.0429  0.0971  291 ILE B CA  
5107  C C   . ILE B 282 ? 0.7276 0.6766 0.7413 -0.3524 0.0454  0.0986  291 ILE B C   
5108  O O   . ILE B 282 ? 0.7502 0.6372 0.7522 -0.3528 0.0362  0.0961  291 ILE B O   
5109  C CB  . ILE B 282 ? 0.7676 0.7691 0.7680 -0.4110 0.0337  0.1190  291 ILE B CB  
5110  C CG1 . ILE B 282 ? 0.8226 0.7646 0.7993 -0.4421 0.0156  0.1219  291 ILE B CG1 
5111  C CG2 . ILE B 282 ? 0.7519 0.8323 0.7628 -0.4177 0.0416  0.1241  291 ILE B CG2 
5112  C CD1 . ILE B 282 ? 0.8584 0.7484 0.8209 -0.4503 0.0047  0.1313  291 ILE B CD1 
5113  N N   . ILE B 283 ? 0.6936 0.6941 0.7224 -0.3343 0.0574  0.1023  292 ILE B N   
5114  C CA  . ILE B 283 ? 0.6866 0.6759 0.7209 -0.3128 0.0619  0.1034  292 ILE B CA  
5115  C C   . ILE B 283 ? 0.6846 0.7194 0.7205 -0.3243 0.0627  0.1228  292 ILE B C   
5116  O O   . ILE B 283 ? 0.6629 0.7614 0.7058 -0.3267 0.0691  0.1291  292 ILE B O   
5117  C CB  . ILE B 283 ? 0.6426 0.6507 0.6919 -0.2764 0.0757  0.0899  292 ILE B CB  
5118  C CG1 . ILE B 283 ? 0.6367 0.6723 0.6924 -0.2692 0.0821  0.0785  292 ILE B CG1 
5119  C CG2 . ILE B 283 ? 0.6373 0.5909 0.6865 -0.2550 0.0754  0.0790  292 ILE B CG2 
5120  C CD1 . ILE B 283 ? 0.6936 0.6889 0.7414 -0.2794 0.0752  0.0678  292 ILE B CD1 
5121  N N   . LYS B 284 ? 0.7107 0.7136 0.7394 -0.3296 0.0562  0.1318  293 LYS B N   
5122  C CA  . LYS B 284 ? 0.7182 0.7598 0.7481 -0.3387 0.0567  0.1501  293 LYS B CA  
5123  C C   . LYS B 284 ? 0.7156 0.7253 0.7487 -0.3146 0.0595  0.1459  293 LYS B C   
5124  O O   . LYS B 284 ? 0.7246 0.6766 0.7543 -0.3021 0.0566  0.1331  293 LYS B O   
5125  C CB  . LYS B 284 ? 0.7656 0.7912 0.7790 -0.3774 0.0422  0.1679  293 LYS B CB  
5126  C CG  . LYS B 284 ? 0.7947 0.8339 0.8006 -0.4056 0.0358  0.1706  293 LYS B CG  
5127  C CD  . LYS B 284 ? 0.8433 0.9100 0.8381 -0.4447 0.0259  0.1945  293 LYS B CD  
5128  C CE  . LYS B 284 ? 0.8739 0.9660 0.8629 -0.4726 0.0209  0.1976  293 LYS B CE  
5129  N NZ  . LYS B 284 ? 0.9005 1.0614 0.8885 -0.5017 0.0190  0.2203  293 LYS B NZ  
5130  N N   . GLU B 285 ? 0.7085 0.7575 0.7475 -0.3077 0.0650  0.1564  294 GLU B N   
5131  C CA  . GLU B 285 ? 0.7082 0.7349 0.7516 -0.2832 0.0689  0.1525  294 GLU B CA  
5132  C C   . GLU B 285 ? 0.7328 0.6870 0.7651 -0.2879 0.0583  0.1514  294 GLU B C   
5133  O O   . GLU B 285 ? 0.7232 0.6438 0.7592 -0.2635 0.0613  0.1400  294 GLU B O   
5134  C CB  . GLU B 285 ? 0.7072 0.7835 0.7545 -0.2820 0.0731  0.1672  294 GLU B CB  
5135  C CG  . GLU B 285 ? 0.7162 0.8539 0.7752 -0.2583 0.0861  0.1617  294 GLU B CG  
5136  C CD  . GLU B 285 ? 0.7573 0.9418 0.8186 -0.2531 0.0900  0.1747  294 GLU B CD  
5137  O OE1 . GLU B 285 ? 0.7546 0.9162 0.8166 -0.2382 0.0909  0.1741  294 GLU B OE1 
5138  O OE2 . GLU B 285 ? 0.7815 1.0290 0.8437 -0.2636 0.0920  0.1853  294 GLU B OE2 
5139  N N   . GLU B 286 ? 0.7643 0.6940 0.7817 -0.3188 0.0452  0.1632  295 GLU B N   
5140  C CA  . GLU B 286 ? 0.8000 0.6596 0.8033 -0.3232 0.0333  0.1638  295 GLU B CA  
5141  C C   . GLU B 286 ? 0.8213 0.6262 0.8100 -0.3353 0.0223  0.1549  295 GLU B C   
5142  O O   . GLU B 286 ? 0.8572 0.5988 0.8311 -0.3370 0.0110  0.1534  295 GLU B O   
5143  C CB  . GLU B 286 ? 0.8371 0.6977 0.8303 -0.3454 0.0247  0.1859  295 GLU B CB  
5144  C CG  . GLU B 286 ? 0.8739 0.8043 0.8694 -0.3699 0.0263  0.2050  295 GLU B CG  
5145  C CD  . GLU B 286 ? 0.9429 0.8916 0.9324 -0.3966 0.0215  0.2073  295 GLU B CD  
5146  O OE1 . GLU B 286 ? 0.9253 0.9220 0.9282 -0.3845 0.0327  0.1984  295 GLU B OE1 
5147  O OE2 . GLU B 286 ? 1.0005 0.9148 0.9708 -0.4292 0.0062  0.2178  295 GLU B OE2 
5148  N N   . VAL B 287 ? 0.7986 0.6267 0.7901 -0.3426 0.0249  0.1484  296 VAL B N   
5149  C CA  . VAL B 287 ? 0.8189 0.5958 0.7971 -0.3499 0.0155  0.1369  296 VAL B CA  
5150  C C   . VAL B 287 ? 0.7814 0.5825 0.7714 -0.3359 0.0252  0.1204  296 VAL B C   
5151  O O   . VAL B 287 ? 0.7522 0.6153 0.7545 -0.3372 0.0347  0.1237  296 VAL B O   
5152  C CB  . VAL B 287 ? 0.8646 0.6286 0.8232 -0.3898 0.0005  0.1504  296 VAL B CB  
5153  C CG1 . VAL B 287 ? 0.9066 0.5960 0.8459 -0.3920 -0.0124 0.1373  296 VAL B CG1 
5154  C CG2 . VAL B 287 ? 0.9054 0.6691 0.8531 -0.4133 -0.0086 0.1734  296 VAL B CG2 
5155  N N   . LEU B 288 ? 0.7840 0.5353 0.7685 -0.3224 0.0220  0.1027  297 LEU B N   
5156  C CA  . LEU B 288 ? 0.7496 0.5138 0.7424 -0.3102 0.0291  0.0859  297 LEU B CA  
5157  C C   . LEU B 288 ? 0.7846 0.4977 0.7580 -0.3262 0.0157  0.0786  297 LEU B C   
5158  O O   . LEU B 288 ? 0.8263 0.4767 0.7832 -0.3252 0.0041  0.0750  297 LEU B O   
5159  C CB  . LEU B 288 ? 0.7135 0.4718 0.7199 -0.2729 0.0400  0.0692  297 LEU B CB  
5160  C CG  . LEU B 288 ? 0.7003 0.4587 0.7116 -0.2604 0.0449  0.0505  297 LEU B CG  
5161  C CD1 . LEU B 288 ? 0.6835 0.5045 0.7061 -0.2669 0.0539  0.0536  297 LEU B CD1 
5162  C CD2 . LEU B 288 ? 0.6727 0.4175 0.6937 -0.2275 0.0527  0.0347  297 LEU B CD2 
5163  N N   . ALA B 289 ? 0.7655 0.5050 0.7396 -0.3401 0.0166  0.0761  298 ALA B N   
5164  C CA  . ALA B 289 ? 0.7955 0.4888 0.7507 -0.3551 0.0039  0.0682  298 ALA B CA  
5165  C C   . ALA B 289 ? 0.7618 0.4806 0.7278 -0.3437 0.0128  0.0529  298 ALA B C   
5166  O O   . ALA B 289 ? 0.7272 0.5083 0.7091 -0.3435 0.0239  0.0567  298 ALA B O   
5167  C CB  . ALA B 289 ? 0.8369 0.5346 0.7762 -0.3953 -0.0084 0.0858  298 ALA B CB  
5168  N N   . TYR B 290 ? 0.7745 0.4455 0.7304 -0.3340 0.0072  0.0354  299 TYR B N   
5169  C CA  . TYR B 290 ? 0.7415 0.4307 0.7060 -0.3223 0.0147  0.0191  299 TYR B CA  
5170  C C   . TYR B 290 ? 0.7848 0.4197 0.7276 -0.3318 0.0010  0.0072  299 TYR B C   
5171  O O   . TYR B 290 ? 0.8367 0.4099 0.7576 -0.3379 -0.0136 0.0071  299 TYR B O   
5172  C CB  . TYR B 290 ? 0.6987 0.3948 0.6802 -0.2852 0.0275  0.0051  299 TYR B CB  
5173  C CG  . TYR B 290 ? 0.7260 0.3645 0.6981 -0.2672 0.0212  -0.0026 299 TYR B CG  
5174  C CD1 . TYR B 290 ? 0.7495 0.3458 0.7124 -0.2520 0.0166  -0.0217 299 TYR B CD1 
5175  C CD2 . TYR B 290 ? 0.7259 0.3537 0.6978 -0.2640 0.0198  0.0088  299 TYR B CD2 
5176  C CE1 . TYR B 290 ? 0.7671 0.3134 0.7206 -0.2326 0.0106  -0.0296 299 TYR B CE1 
5177  C CE2 . TYR B 290 ? 0.7457 0.3219 0.7086 -0.2459 0.0138  0.0015  299 TYR B CE2 
5178  C CZ  . TYR B 290 ? 0.7629 0.2993 0.7166 -0.2298 0.0091  -0.0178 299 TYR B CZ  
5179  O OH  . TYR B 290 ? 0.7736 0.2632 0.7179 -0.2097 0.0031  -0.0257 299 TYR B OH  
5180  N N   . VAL B 291 ? 0.7663 0.4225 0.7135 -0.3320 0.0052  -0.0035 300 VAL B N   
5181  C CA  . VAL B 291 ? 0.8061 0.4157 0.7324 -0.3418 -0.0075 -0.0153 300 VAL B CA  
5182  C C   . VAL B 291 ? 0.7949 0.3861 0.7257 -0.3102 -0.0022 -0.0379 300 VAL B C   
5183  O O   . VAL B 291 ? 0.7526 0.3880 0.7038 -0.2928 0.0122  -0.0452 300 VAL B O   
5184  C CB  . VAL B 291 ? 0.8061 0.4497 0.7304 -0.3690 -0.0091 -0.0109 300 VAL B CB  
5185  C CG1 . VAL B 291 ? 0.8383 0.4418 0.7456 -0.3706 -0.0183 -0.0284 300 VAL B CG1 
5186  C CG2 . VAL B 291 ? 0.8500 0.4939 0.7602 -0.4060 -0.0207 0.0105  300 VAL B CG2 
5187  N N   . VAL B 292 ? 0.8407 0.3660 0.7506 -0.3025 -0.0147 -0.0487 301 VAL B N   
5188  C CA  . VAL B 292 ? 0.8382 0.3425 0.7477 -0.2743 -0.0125 -0.0712 301 VAL B CA  
5189  C C   . VAL B 292 ? 0.8637 0.3547 0.7590 -0.2866 -0.0199 -0.0827 301 VAL B C   
5190  O O   . VAL B 292 ? 0.9157 0.3809 0.7899 -0.3160 -0.0341 -0.0758 301 VAL B O   
5191  C CB  . VAL B 292 ? 0.8719 0.3154 0.7652 -0.2565 -0.0223 -0.0779 301 VAL B CB  
5192  C CG1 . VAL B 292 ? 0.9160 0.3182 0.7932 -0.2404 -0.0298 -0.1003 301 VAL B CG1 
5193  C CG2 . VAL B 292 ? 0.8307 0.2999 0.7460 -0.2298 -0.0088 -0.0766 301 VAL B CG2 
5194  N N   . GLN B 293 ? 0.8332 0.3420 0.7392 -0.2652 -0.0110 -0.0999 302 GLN B N   
5195  C CA  . GLN B 293 ? 0.8488 0.3553 0.7449 -0.2762 -0.0157 -0.1104 302 GLN B CA  
5196  C C   . GLN B 293 ? 0.8583 0.3316 0.7455 -0.2492 -0.0182 -0.1340 302 GLN B C   
5197  O O   . GLN B 293 ? 0.8163 0.3200 0.7226 -0.2229 -0.0049 -0.1441 302 GLN B O   
5198  C CB  . GLN B 293 ? 0.7993 0.3771 0.7192 -0.2818 -0.0007 -0.1058 302 GLN B CB  
5199  C CG  . GLN B 293 ? 0.8361 0.4198 0.7501 -0.2883 -0.0027 -0.1185 302 GLN B CG  
5200  C CD  . GLN B 293 ? 0.8336 0.4843 0.7656 -0.3028 0.0080  -0.1093 302 GLN B CD  
5201  O OE1 . GLN B 293 ? 0.8229 0.5070 0.7634 -0.3186 0.0113  -0.0910 302 GLN B OE1 
5202  N NE2 . GLN B 293 ? 0.8330 0.5057 0.7702 -0.2967 0.0132  -0.1221 302 GLN B NE2 
5203  N N   . LEU B 294 ? 0.9137 0.3249 0.7701 -0.2565 -0.0363 -0.1427 303 LEU B N   
5204  C CA  . LEU B 294 ? 0.9358 0.3069 0.7786 -0.2283 -0.0416 -0.1653 303 LEU B CA  
5205  C C   . LEU B 294 ? 0.9560 0.3235 0.7873 -0.2346 -0.0462 -0.1798 303 LEU B C   
5206  O O   . LEU B 294 ? 0.9778 0.3473 0.7997 -0.2666 -0.0531 -0.1713 303 LEU B O   
5207  C CB  . LEU B 294 ? 0.9964 0.2917 0.8085 -0.2253 -0.0602 -0.1667 303 LEU B CB  
5208  C CG  . LEU B 294 ? 0.9780 0.2731 0.7996 -0.2186 -0.0568 -0.1523 303 LEU B CG  
5209  C CD1 . LEU B 294 ? 1.0313 0.2538 0.8246 -0.2046 -0.0732 -0.1586 303 LEU B CD1 
5210  C CD2 . LEU B 294 ? 0.9199 0.2698 0.7744 -0.1911 -0.0365 -0.1552 303 LEU B CD2 
5211  N N   . PRO B 295 ? 0.9507 0.3164 0.7829 -0.2047 -0.0425 -0.2014 304 PRO B N   
5212  C CA  . PRO B 295 ? 0.9687 0.3323 0.7901 -0.2079 -0.0465 -0.2171 304 PRO B CA  
5213  C C   . PRO B 295 ? 1.0519 0.3378 0.8320 -0.2159 -0.0699 -0.2271 304 PRO B C   
5214  O O   . PRO B 295 ? 1.0960 0.3266 0.8559 -0.2052 -0.0818 -0.2289 304 PRO B O   
5215  C CB  . PRO B 295 ? 0.9323 0.3232 0.7696 -0.1710 -0.0340 -0.2352 304 PRO B CB  
5216  C CG  . PRO B 295 ? 0.9329 0.3063 0.7727 -0.1467 -0.0329 -0.2347 304 PRO B CG  
5217  C CD  . PRO B 295 ? 0.9230 0.2968 0.7684 -0.1674 -0.0332 -0.2114 304 PRO B CD  
5218  N N   . LEU B 296 ? 1.0778 0.3584 0.8438 -0.2350 -0.0771 -0.2334 305 LEU B N   
5219  C CA  . LEU B 296 ? 1.1570 0.3632 0.8812 -0.2414 -0.1000 -0.2460 305 LEU B CA  
5220  C C   . LEU B 296 ? 1.1612 0.3776 0.8816 -0.2285 -0.0984 -0.2680 305 LEU B C   
5221  O O   . LEU B 296 ? 1.1234 0.3937 0.8623 -0.2430 -0.0879 -0.2650 305 LEU B O   
5222  C CB  . LEU B 296 ? 1.1953 0.3771 0.8993 -0.2870 -0.1148 -0.2288 305 LEU B CB  
5223  C CG  . LEU B 296 ? 1.2035 0.3731 0.9065 -0.3077 -0.1193 -0.2047 305 LEU B CG  
5224  C CD1 . LEU B 296 ? 1.2473 0.3971 0.9280 -0.3546 -0.1349 -0.1898 305 LEU B CD1 
5225  C CD2 . LEU B 296 ? 1.2640 0.3661 0.9445 -0.2859 -0.1317 -0.2101 305 LEU B CD2 
5226  N N   . TYR B 297 ? 1.2081 0.3741 0.9039 -0.2003 -0.1092 -0.2902 306 TYR B N   
5227  C CA  . TYR B 297 ? 1.2173 0.3894 0.9063 -0.1840 -0.1090 -0.3135 306 TYR B CA  
5228  C C   . TYR B 297 ? 1.2899 0.4037 0.9389 -0.2056 -0.1309 -0.3221 306 TYR B C   
5229  O O   . TYR B 297 ? 1.3594 0.3974 0.9717 -0.2111 -0.1521 -0.3235 306 TYR B O   
5230  C CB  . TYR B 297 ? 1.2231 0.3839 0.9094 -0.1375 -0.1069 -0.3346 306 TYR B CB  
5231  C CG  . TYR B 297 ? 1.1705 0.3786 0.8909 -0.1182 -0.0887 -0.3252 306 TYR B CG  
5232  C CD1 . TYR B 297 ? 1.2021 0.3734 0.9143 -0.1050 -0.0946 -0.3200 306 TYR B CD1 
5233  C CD2 . TYR B 297 ? 1.1159 0.4045 0.8757 -0.1151 -0.0662 -0.3199 306 TYR B CD2 
5234  C CE1 . TYR B 297 ? 1.1542 0.3700 0.8978 -0.0886 -0.0780 -0.3107 306 TYR B CE1 
5235  C CE2 . TYR B 297 ? 1.0752 0.4056 0.8648 -0.0991 -0.0502 -0.3104 306 TYR B CE2 
5236  C CZ  . TYR B 297 ? 1.0835 0.3779 0.8652 -0.0862 -0.0561 -0.3059 306 TYR B CZ  
5237  O OH  . TYR B 297 ? 1.0036 0.3378 0.8133 -0.0715 -0.0412 -0.2964 306 TYR B OH  
5238  N N   . GLY B 298 ? 1.2755 0.4234 0.9302 -0.2182 -0.1265 -0.3279 307 GLY B N   
5239  C CA  . GLY B 298 ? 1.3416 0.4383 0.9589 -0.2401 -0.1468 -0.3365 307 GLY B CA  
5240  C C   . GLY B 298 ? 1.3867 0.4453 0.9786 -0.2073 -0.1559 -0.3664 307 GLY B C   
5241  O O   . GLY B 298 ? 1.4552 0.4631 1.0111 -0.2205 -0.1747 -0.3774 307 GLY B O   
5242  N N   . VAL B 299 ? 1.3539 0.4393 0.9638 -0.1651 -0.1430 -0.3795 308 VAL B N   
5243  C CA  . VAL B 299 ? 1.3982 0.4537 0.9850 -0.1282 -0.1506 -0.4091 308 VAL B CA  
5244  C C   . VAL B 299 ? 1.3806 0.4528 0.9822 -0.0840 -0.1404 -0.4180 308 VAL B C   
5245  O O   . VAL B 299 ? 1.3090 0.4492 0.9513 -0.0769 -0.1188 -0.4071 308 VAL B O   
5246  C CB  . VAL B 299 ? 1.3641 0.4697 0.9626 -0.1233 -0.1408 -0.4238 308 VAL B CB  
5247  C CG1 . VAL B 299 ? 1.4312 0.4864 0.9915 -0.1460 -0.1611 -0.4339 308 VAL B CG1 
5248  C CG2 . VAL B 299 ? 1.2745 0.4688 0.9200 -0.1391 -0.1169 -0.4060 308 VAL B CG2 
5249  N N   . ILE B 300 ? 1.4532 0.4645 1.0200 -0.0536 -0.1564 -0.4388 309 ILE B N   
5250  C CA  . ILE B 300 ? 1.4497 0.4710 1.0245 -0.0093 -0.1498 -0.4493 309 ILE B CA  
5251  C C   . ILE B 300 ? 1.4871 0.5017 1.0424 0.0270  -0.1548 -0.4800 309 ILE B C   
5252  O O   . ILE B 300 ? 1.5532 0.5212 1.0741 0.0188  -0.1716 -0.4938 309 ILE B O   
5253  C CB  . ILE B 300 ? 1.5074 0.4536 1.0536 -0.0035 -0.1673 -0.4445 309 ILE B CB  
5254  C CG1 . ILE B 300 ? 1.4963 0.4448 1.0573 -0.0429 -0.1648 -0.4139 309 ILE B CG1 
5255  C CG2 . ILE B 300 ? 1.4879 0.4495 1.0448 0.0407  -0.1598 -0.4528 309 ILE B CG2 
5256  C CD1 . ILE B 300 ? 1.4243 0.4638 1.0392 -0.0461 -0.1371 -0.3965 309 ILE B CD1 
5257  N N   . ASP B 301 ? 1.4530 0.5152 1.0288 0.0661  -0.1409 -0.4906 310 ASP B N   
5258  C CA  . ASP B 301 ? 1.4984 0.5459 1.0501 0.1086  -0.1486 -0.5209 310 ASP B CA  
5259  C C   . ASP B 301 ? 1.4996 0.5758 1.0487 0.1074  -0.1463 -0.5377 310 ASP B C   
5260  O O   . ASP B 301 ? 1.5570 0.6007 1.0735 0.1350  -0.1593 -0.5642 310 ASP B O   
5261  C CB  . ASP B 301 ? 1.5983 0.5426 1.0959 0.1229  -0.1769 -0.5339 310 ASP B CB  
5262  C CG  . ASP B 301 ? 1.6101 0.5254 1.1076 0.1307  -0.1800 -0.5203 310 ASP B CG  
5263  O OD1 . ASP B 301 ? 1.6725 0.5084 1.1370 0.1126  -0.2003 -0.5129 310 ASP B OD1 
5264  O OD2 . ASP B 301 ? 1.5612 0.5328 1.0906 0.1538  -0.1628 -0.5165 310 ASP B OD2 
5265  N N   . THR B 302 ? 1.4387 0.5746 1.0205 0.0765  -0.1304 -0.5227 311 THR B N   
5266  C CA  . THR B 302 ? 1.4252 0.6053 1.0137 0.0763  -0.1235 -0.5357 311 THR B CA  
5267  C C   . THR B 302 ? 1.3650 0.6271 0.9882 0.1067  -0.1021 -0.5410 311 THR B C   
5268  O O   . THR B 302 ? 1.3170 0.6185 0.9712 0.1087  -0.0877 -0.5246 311 THR B O   
5269  C CB  . THR B 302 ? 1.3759 0.5937 0.9884 0.0323  -0.1136 -0.5157 311 THR B CB  
5270  O OG1 . THR B 302 ? 1.4033 0.5720 1.0045 -0.0016 -0.1245 -0.4959 311 THR B OG1 
5271  C CG2 . THR B 302 ? 1.4213 0.6398 1.0179 0.0234  -0.1194 -0.5309 311 THR B CG2 
5272  N N   . PRO B 303 ? 1.3728 0.6625 0.9903 0.1293  -0.1004 -0.5633 312 PRO B N   
5273  C CA  . PRO B 303 ? 1.3120 0.6848 0.9638 0.1542  -0.0798 -0.5652 312 PRO B CA  
5274  C C   . PRO B 303 ? 1.2352 0.6793 0.9307 0.1243  -0.0588 -0.5421 312 PRO B C   
5275  O O   . PRO B 303 ? 1.2315 0.6729 0.9278 0.0910  -0.0598 -0.5337 312 PRO B O   
5276  C CB  . PRO B 303 ? 1.3379 0.7230 0.9714 0.1792  -0.0840 -0.5932 312 PRO B CB  
5277  C CG  . PRO B 303 ? 1.3822 0.7134 0.9862 0.1522  -0.0999 -0.5984 312 PRO B CG  
5278  C CD  . PRO B 303 ? 1.4303 0.6831 1.0121 0.1328  -0.1159 -0.5863 312 PRO B CD  
5279  N N   . CYS B 304 ? 1.1784 0.6831 0.9079 0.1357  -0.0410 -0.5312 313 CYS B N   
5280  C CA  . CYS B 304 ? 1.1078 0.6882 0.8766 0.1163  -0.0207 -0.5144 313 CYS B CA  
5281  C C   . CYS B 304 ? 1.0648 0.7158 0.8535 0.1438  -0.0066 -0.5230 313 CYS B C   
5282  O O   . CYS B 304 ? 1.0876 0.7365 0.8653 0.1784  -0.0103 -0.5386 313 CYS B O   
5283  C CB  . CYS B 304 ? 1.0679 0.6611 0.8631 0.0957  -0.0109 -0.4869 313 CYS B CB  
5284  S SG  . CYS B 304 ? 1.1382 0.6539 0.9150 0.0699  -0.0257 -0.4715 313 CYS B SG  
5285  N N   . TRP B 305 ? 1.0032 0.7190 0.8213 0.1280  0.0093  -0.5116 314 TRP B N   
5286  C CA  . TRP B 305 ? 0.9622 0.7506 0.8016 0.1481  0.0234  -0.5154 314 TRP B CA  
5287  C C   . TRP B 305 ? 0.8876 0.7345 0.7627 0.1257  0.0409  -0.4919 314 TRP B C   
5288  O O   . TRP B 305 ? 0.8751 0.7159 0.7569 0.0954  0.0425  -0.4779 314 TRP B O   
5289  C CB  . TRP B 305 ? 0.9859 0.7937 0.8115 0.1620  0.0206  -0.5379 314 TRP B CB  
5290  C CG  . TRP B 305 ? 1.0018 0.8034 0.8228 0.1342  0.0183  -0.5371 314 TRP B CG  
5291  C CD1 . TRP B 305 ? 0.9705 0.8305 0.8134 0.1179  0.0309  -0.5293 314 TRP B CD1 
5292  C CD2 . TRP B 305 ? 1.0735 0.8077 0.8647 0.1195  0.0016  -0.5447 314 TRP B CD2 
5293  N NE1 . TRP B 305 ? 0.9985 0.8345 0.8286 0.0947  0.0239  -0.5315 314 TRP B NE1 
5294  C CE2 . TRP B 305 ? 1.0595 0.8190 0.8578 0.0941  0.0058  -0.5408 314 TRP B CE2 
5295  C CE3 . TRP B 305 ? 1.1552 0.8085 0.9124 0.1245  -0.0175 -0.5540 314 TRP B CE3 
5296  C CZ2 . TRP B 305 ? 1.1142 0.8239 0.8880 0.0725  -0.0081 -0.5457 314 TRP B CZ2 
5297  C CZ3 . TRP B 305 ? 1.2165 0.8164 0.9475 0.1020  -0.0322 -0.5586 314 TRP B CZ3 
5298  C CH2 . TRP B 305 ? 1.1943 0.8243 0.9344 0.0758  -0.0272 -0.5544 314 TRP B CH2 
5299  N N   . LYS B 306 ? 0.8405 0.7439 0.7370 0.1404  0.0533  -0.4872 315 LYS B N   
5300  C CA  . LYS B 306 ? 0.7751 0.7325 0.7020 0.1208  0.0686  -0.4662 315 LYS B CA  
5301  C C   . LYS B 306 ? 0.7508 0.7724 0.6880 0.1266  0.0776  -0.4727 315 LYS B C   
5302  O O   . LYS B 306 ? 0.7619 0.8112 0.6950 0.1528  0.0780  -0.4876 315 LYS B O   
5303  C CB  . LYS B 306 ? 0.7454 0.7177 0.6898 0.1260  0.0757  -0.4508 315 LYS B CB  
5304  C CG  . LYS B 306 ? 0.6910 0.6979 0.6615 0.1012  0.0881  -0.4264 315 LYS B CG  
5305  C CD  . LYS B 306 ? 0.6790 0.7022 0.6652 0.1075  0.0946  -0.4125 315 LYS B CD  
5306  C CE  . LYS B 306 ? 0.6457 0.6825 0.6511 0.0821  0.1031  -0.3884 315 LYS B CE  
5307  N NZ  . LYS B 306 ? 0.6313 0.7038 0.6534 0.0888  0.1116  -0.3769 315 LYS B NZ  
5308  N N   . LEU B 307 ? 0.7212 0.7687 0.6717 0.1019  0.0846  -0.4608 316 LEU B N   
5309  C CA  . LEU B 307 ? 0.7033 0.8095 0.6629 0.1025  0.0927  -0.4647 316 LEU B CA  
5310  C C   . LEU B 307 ? 0.6576 0.8179 0.6435 0.0942  0.1063  -0.4447 316 LEU B C   
5311  O O   . LEU B 307 ? 0.6391 0.7922 0.6375 0.0741  0.1104  -0.4244 316 LEU B O   
5312  C CB  . LEU B 307 ? 0.7065 0.8034 0.6602 0.0807  0.0900  -0.4660 316 LEU B CB  
5313  C CG  . LEU B 307 ? 0.6755 0.8296 0.6390 0.0742  0.0981  -0.4667 316 LEU B CG  
5314  C CD1 . LEU B 307 ? 0.6899 0.8750 0.6447 0.1007  0.0974  -0.4878 316 LEU B CD1 
5315  C CD2 . LEU B 307 ? 0.6841 0.8210 0.6404 0.0512  0.0941  -0.4666 316 LEU B CD2 
5316  N N   . HIS B 308 ? 0.6478 0.8625 0.6405 0.1096  0.1125  -0.4501 317 HIS B N   
5317  C CA  . HIS B 308 ? 0.6077 0.8764 0.6224 0.0988  0.1242  -0.4313 317 HIS B CA  
5318  C C   . HIS B 308 ? 0.5889 0.9074 0.6060 0.0959  0.1288  -0.4366 317 HIS B C   
5319  O O   . HIS B 308 ? 0.6176 0.9351 0.6207 0.1081  0.1237  -0.4565 317 HIS B O   
5320  C CB  . HIS B 308 ? 0.6041 0.8996 0.6269 0.1155  0.1281  -0.4278 317 HIS B CB  
5321  C CG  . HIS B 308 ? 0.6590 0.9061 0.6736 0.1285  0.1213  -0.4309 317 HIS B CG  
5322  N ND1 . HIS B 308 ? 0.6743 0.8991 0.6984 0.1171  0.1231  -0.4126 317 HIS B ND1 
5323  C CD2 . HIS B 308 ? 0.7173 0.9327 0.7137 0.1525  0.1120  -0.4504 317 HIS B CD2 
5324  C CE1 . HIS B 308 ? 0.7148 0.8975 0.7279 0.1325  0.1156  -0.4199 317 HIS B CE1 
5325  N NE2 . HIS B 308 ? 0.7415 0.9165 0.7371 0.1544  0.1084  -0.4428 317 HIS B NE2 
5326  N N   . THR B 309 ? 0.5444 0.9057 0.5776 0.0806  0.1378  -0.4191 318 THR B N   
5327  C CA  . THR B 309 ? 0.5257 0.9211 0.5608 0.0693  0.1412  -0.4194 318 THR B CA  
5328  C C   . THR B 309 ? 0.4901 0.9415 0.5402 0.0613  0.1501  -0.4029 318 THR B C   
5329  O O   . THR B 309 ? 0.4716 0.9188 0.5317 0.0505  0.1534  -0.3840 318 THR B O   
5330  C CB  . THR B 309 ? 0.5221 0.8812 0.5558 0.0472  0.1390  -0.4114 318 THR B CB  
5331  O OG1 . THR B 309 ? 0.5517 0.8936 0.5705 0.0497  0.1325  -0.4297 318 THR B OG1 
5332  C CG2 . THR B 309 ? 0.4898 0.8809 0.5365 0.0267  0.1464  -0.3918 318 THR B CG2 
5333  N N   . SER B 310 ? 0.4869 0.9901 0.5373 0.0659  0.1532  -0.4096 319 SER B N   
5334  C CA  . SER B 310 ? 0.4602 1.0168 0.5225 0.0552  0.1605  -0.3927 319 SER B CA  
5335  C C   . SER B 310 ? 0.4623 1.0576 0.5240 0.0463  0.1630  -0.3944 319 SER B C   
5336  O O   . SER B 310 ? 0.4936 1.0895 0.5457 0.0561  0.1598  -0.4134 319 SER B O   
5337  C CB  . SER B 310 ? 0.4559 1.0525 0.5213 0.0719  0.1625  -0.3957 319 SER B CB  
5338  O OG  . SER B 310 ? 0.4222 1.0661 0.4975 0.0575  0.1682  -0.3769 319 SER B OG  
5339  N N   . PRO B 311 ? 0.4394 1.0661 0.5094 0.0281  0.1679  -0.3748 320 PRO B N   
5340  C CA  . PRO B 311 ? 0.4390 1.1027 0.5083 0.0177  0.1702  -0.3737 320 PRO B CA  
5341  C C   . PRO B 311 ? 0.4630 1.1772 0.5279 0.0336  0.1709  -0.3914 320 PRO B C   
5342  O O   . PRO B 311 ? 0.4628 1.2003 0.5281 0.0503  0.1712  -0.3985 320 PRO B O   
5343  C CB  . PRO B 311 ? 0.4049 1.0924 0.4820 -0.0012 0.1741  -0.3482 320 PRO B CB  
5344  C CG  . PRO B 311 ? 0.4006 1.0837 0.4821 0.0044  0.1745  -0.3411 320 PRO B CG  
5345  C CD  . PRO B 311 ? 0.4192 1.0472 0.4978 0.0161  0.1707  -0.3522 320 PRO B CD  
5346  N N   . LEU B 312 ? 0.4841 1.2169 0.5448 0.0284  0.1711  -0.3981 321 LEU B N   
5347  C CA  . LEU B 312 ? 0.5171 1.2928 0.5715 0.0432  0.1710  -0.4173 321 LEU B CA  
5348  C C   . LEU B 312 ? 0.5211 1.3391 0.5776 0.0265  0.1744  -0.4084 321 LEU B C   
5349  O O   . LEU B 312 ? 0.5240 1.3196 0.5779 0.0144  0.1731  -0.4071 321 LEU B O   
5350  C CB  . LEU B 312 ? 0.5422 1.2748 0.5837 0.0564  0.1647  -0.4409 321 LEU B CB  
5351  C CG  . LEU B 312 ? 0.5680 1.3207 0.5983 0.0836  0.1615  -0.4672 321 LEU B CG  
5352  C CD1 . LEU B 312 ? 0.5858 1.3014 0.6014 0.0870  0.1549  -0.4866 321 LEU B CD1 
5353  C CD2 . LEU B 312 ? 0.5579 1.3884 0.5924 0.0868  0.1668  -0.4667 321 LEU B CD2 
5354  N N   . CYS B 313 ? 0.5396 1.4197 0.6003 0.0248  0.1783  -0.4012 322 CYS B N   
5355  C CA  . CYS B 313 ? 0.5658 1.4846 0.6275 0.0075  0.1809  -0.3908 322 CYS B CA  
5356  C C   . CYS B 313 ? 0.6059 1.5788 0.6624 0.0213  0.1817  -0.4092 322 CYS B C   
5357  O O   . CYS B 313 ? 0.6265 1.6132 0.6794 0.0444  0.1807  -0.4273 322 CYS B O   
5358  C CB  . CYS B 313 ? 0.5431 1.4898 0.6116 -0.0120 0.1838  -0.3633 322 CYS B CB  
5359  S SG  . CYS B 313 ? 0.5504 1.4371 0.6235 -0.0266 0.1825  -0.3408 322 CYS B SG  
5360  N N   . THR B 314 ? 0.6331 1.6368 0.6883 0.0081  0.1833  -0.4047 323 THR B N   
5361  C CA  . THR B 314 ? 0.6749 1.7284 0.7242 0.0191  0.1839  -0.4225 323 THR B CA  
5362  C C   . THR B 314 ? 0.6857 1.8100 0.7390 0.0041  0.1879  -0.4058 323 THR B C   
5363  O O   . THR B 314 ? 0.6727 1.8031 0.7320 -0.0139 0.1893  -0.3811 323 THR B O   
5364  C CB  . THR B 314 ? 0.6837 1.7071 0.7253 0.0173  0.1809  -0.4357 323 THR B CB  
5365  O OG1 . THR B 314 ? 0.6690 1.6851 0.7147 -0.0082 0.1822  -0.4144 323 THR B OG1 
5366  C CG2 . THR B 314 ? 0.6930 1.6453 0.7280 0.0291  0.1755  -0.4514 323 THR B CG2 
5367  N N   . THR B 315 ? 0.7256 1.8998 0.7741 0.0104  0.1889  -0.4190 324 THR B N   
5368  C CA  . THR B 315 ? 0.7400 1.9962 0.7907 0.0028  0.1924  -0.4090 324 THR B CA  
5369  C C   . THR B 315 ? 0.7510 2.0449 0.7985 -0.0122 0.1935  -0.4044 324 THR B C   
5370  O O   . THR B 315 ? 0.7397 2.0525 0.7899 -0.0365 0.1944  -0.3791 324 THR B O   
5371  C CB  . THR B 315 ? 0.7531 2.0649 0.8025 0.0287  0.1938  -0.4270 324 THR B CB  
5372  O OG1 . THR B 315 ? 0.7598 2.0467 0.8132 0.0386  0.1932  -0.4251 324 THR B OG1 
5373  C CG2 . THR B 315 ? 0.7349 2.1379 0.7869 0.0192  0.1974  -0.4151 324 THR B CG2 
5374  N N   . ASN B 316 ? 0.7827 2.0853 0.8229 0.0022  0.1926  -0.4283 325 ASN B N   
5375  C CA  . ASN B 316 ? 0.7915 2.1464 0.8280 -0.0063 0.1941  -0.4289 325 ASN B CA  
5376  C C   . ASN B 316 ? 0.7806 2.1105 0.8162 -0.0293 0.1931  -0.4152 325 ASN B C   
5377  O O   . ASN B 316 ? 0.7889 2.0985 0.8185 -0.0251 0.1912  -0.4308 325 ASN B O   
5378  C CB  . ASN B 316 ? 0.8193 2.2018 0.8468 0.0202  0.1932  -0.4612 325 ASN B CB  
5379  C CG  . ASN B 316 ? 0.8421 2.2800 0.8694 0.0431  0.1949  -0.4730 325 ASN B CG  
5380  O OD1 . ASN B 316 ? 0.8765 2.3577 0.8963 0.0630  0.1949  -0.4951 325 ASN B OD1 
5381  N ND2 . ASN B 316 ? 0.8303 2.2686 0.8652 0.0415  0.1962  -0.4590 325 ASN B ND2 
5382  N N   . SER B 321 ? 0.7402 1.9250 0.7821 -0.0409 0.1889  -0.3969 330 SER B N   
5383  C CA  . SER B 321 ? 0.7207 1.9091 0.7672 -0.0625 0.1897  -0.3664 330 SER B CA  
5384  C C   . SER B 321 ? 0.7132 1.8350 0.7610 -0.0749 0.1874  -0.3519 330 SER B C   
5385  O O   . SER B 321 ? 0.7078 1.8115 0.7528 -0.0847 0.1862  -0.3486 330 SER B O   
5386  C CB  . SER B 321 ? 0.7149 1.9634 0.7592 -0.0792 0.1910  -0.3515 330 SER B CB  
5387  O OG  . SER B 321 ? 0.7191 1.9915 0.7587 -0.0760 0.1913  -0.3661 330 SER B OG  
5388  N N   . ASN B 322 ? 0.7047 1.7935 0.7567 -0.0728 0.1869  -0.3445 331 ASN B N   
5389  C CA  . ASN B 322 ? 0.6894 1.7236 0.7429 -0.0852 0.1849  -0.3256 331 ASN B CA  
5390  C C   . ASN B 322 ? 0.6729 1.6430 0.7269 -0.0796 0.1830  -0.3346 331 ASN B C   
5391  O O   . ASN B 322 ? 0.6657 1.6060 0.7183 -0.0911 0.1815  -0.3236 331 ASN B O   
5392  C CB  . ASN B 322 ? 0.6935 1.7364 0.7430 -0.1071 0.1837  -0.3012 331 ASN B CB  
5393  C CG  . ASN B 322 ? 0.7151 1.7862 0.7633 -0.1201 0.1830  -0.2788 331 ASN B CG  
5394  O OD1 . ASN B 322 ? 0.7337 1.7842 0.7845 -0.1195 0.1823  -0.2709 331 ASN B OD1 
5395  N ND2 . ASN B 322 ? 0.7446 1.8626 0.7876 -0.1333 0.1825  -0.2678 331 ASN B ND2 
5396  N N   . ILE B 323 ? 0.6543 1.6041 0.7092 -0.0619 0.1824  -0.3536 332 ILE B N   
5397  C CA  . ILE B 323 ? 0.6297 1.5176 0.6845 -0.0585 0.1798  -0.3593 332 ILE B CA  
5398  C C   . ILE B 323 ? 0.6166 1.4802 0.6740 -0.0448 0.1791  -0.3650 332 ILE B C   
5399  O O   . ILE B 323 ? 0.6229 1.5130 0.6792 -0.0289 0.1797  -0.3792 332 ILE B O   
5400  C CB  . ILE B 323 ? 0.6450 1.5178 0.6935 -0.0536 0.1773  -0.3796 332 ILE B CB  
5401  C CG1 . ILE B 323 ? 0.6374 1.4654 0.6860 -0.0663 0.1752  -0.3708 332 ILE B CG1 
5402  C CG2 . ILE B 323 ? 0.6595 1.5168 0.7029 -0.0328 0.1746  -0.4049 332 ILE B CG2 
5403  C CD1 . ILE B 323 ? 0.6136 1.4633 0.6621 -0.0829 0.1764  -0.3549 332 ILE B CD1 
5404  N N   . CYS B 324 ? 0.5840 1.4006 0.6446 -0.0503 0.1780  -0.3531 333 CYS B N   
5405  C CA  . CYS B 324 ? 0.5634 1.3493 0.6263 -0.0386 0.1769  -0.3571 333 CYS B CA  
5406  C C   . CYS B 324 ? 0.5460 1.2727 0.6065 -0.0367 0.1733  -0.3643 333 CYS B C   
5407  O O   . CYS B 324 ? 0.5345 1.2365 0.5957 -0.0502 0.1726  -0.3532 333 CYS B O   
5408  C CB  . CYS B 324 ? 0.5493 1.3367 0.6178 -0.0467 0.1784  -0.3350 333 CYS B CB  
5409  S SG  . CYS B 324 ? 0.5865 1.4451 0.6568 -0.0519 0.1814  -0.3230 333 CYS B SG  
5410  N N   . LEU B 325 ? 0.5349 1.2409 0.5915 -0.0196 0.1705  -0.3827 334 LEU B N   
5411  C CA  . LEU B 325 ? 0.5395 1.1888 0.5905 -0.0161 0.1654  -0.3932 334 LEU B CA  
5412  C C   . LEU B 325 ? 0.5352 1.1485 0.5887 -0.0085 0.1639  -0.3901 334 LEU B C   
5413  O O   . LEU B 325 ? 0.5422 1.1709 0.5957 0.0072  0.1643  -0.3972 334 LEU B O   
5414  C CB  . LEU B 325 ? 0.5638 1.2109 0.6031 -0.0005 0.1608  -0.4200 334 LEU B CB  
5415  C CG  . LEU B 325 ? 0.5755 1.2375 0.6086 -0.0075 0.1596  -0.4287 334 LEU B CG  
5416  C CD1 . LEU B 325 ? 0.6079 1.2324 0.6261 0.0038  0.1518  -0.4528 334 LEU B CD1 
5417  C CD2 . LEU B 325 ? 0.5758 1.2262 0.6142 -0.0300 0.1610  -0.4103 334 LEU B CD2 
5418  N N   . THR B 326 ? 0.5196 1.0878 0.5747 -0.0181 0.1620  -0.3803 335 THR B N   
5419  C CA  . THR B 326 ? 0.5189 1.0497 0.5741 -0.0092 0.1595  -0.3812 335 THR B CA  
5420  C C   . THR B 326 ? 0.5370 1.0180 0.5839 -0.0122 0.1533  -0.3900 335 THR B C   
5421  O O   . THR B 326 ? 0.5325 1.0036 0.5796 -0.0278 0.1529  -0.3830 335 THR B O   
5422  C CB  . THR B 326 ? 0.4938 1.0199 0.5587 -0.0181 0.1630  -0.3584 335 THR B CB  
5423  O OG1 . THR B 326 ? 0.4738 1.0482 0.5441 -0.0222 0.1678  -0.3473 335 THR B OG1 
5424  C CG2 . THR B 326 ? 0.5039 1.0050 0.5697 -0.0057 0.1613  -0.3605 335 THR B CG2 
5425  N N   . ARG B 327 ? 0.5614 1.0124 0.5992 0.0030  0.1477  -0.4060 336 ARG B N   
5426  C CA  . ARG B 327 ? 0.5931 0.9925 0.6201 -0.0009 0.1400  -0.4144 336 ARG B CA  
5427  C C   . ARG B 327 ? 0.5876 0.9505 0.6207 -0.0127 0.1399  -0.3969 336 ARG B C   
5428  O O   . ARG B 327 ? 0.5797 0.9350 0.6180 -0.0053 0.1414  -0.3903 336 ARG B O   
5429  C CB  . ARG B 327 ? 0.6264 1.0038 0.6384 0.0207  0.1328  -0.4375 336 ARG B CB  
5430  C CG  . ARG B 327 ? 0.6714 1.0080 0.6662 0.0167  0.1234  -0.4522 336 ARG B CG  
5431  C CD  . ARG B 327 ? 0.7033 1.0431 0.6815 0.0378  0.1176  -0.4780 336 ARG B CD  
5432  N NE  . ARG B 327 ? 0.7309 1.0327 0.6961 0.0589  0.1101  -0.4913 336 ARG B NE  
5433  C CZ  . ARG B 327 ? 0.7684 1.0068 0.7164 0.0578  0.0990  -0.4988 336 ARG B CZ  
5434  N NH1 . ARG B 327 ? 0.7754 0.9824 0.7180 0.0346  0.0942  -0.4937 336 ARG B NH1 
5435  N NH2 . ARG B 327 ? 0.7975 1.0045 0.7328 0.0797  0.0922  -0.5108 336 ARG B NH2 
5436  N N   . THR B 328 ? 0.5935 0.9381 0.6263 -0.0309 0.1382  -0.3889 337 THR B N   
5437  C CA  . THR B 328 ? 0.5899 0.9122 0.6301 -0.0426 0.1394  -0.3702 337 THR B CA  
5438  C C   . THR B 328 ? 0.6155 0.8881 0.6491 -0.0383 0.1330  -0.3735 337 THR B C   
5439  O O   . THR B 328 ? 0.6074 0.8694 0.6483 -0.0371 0.1353  -0.3613 337 THR B O   
5440  C CB  . THR B 328 ? 0.5899 0.9132 0.6310 -0.0625 0.1393  -0.3612 337 THR B CB  
5441  O OG1 . THR B 328 ? 0.5853 0.9536 0.6347 -0.0670 0.1461  -0.3517 337 THR B OG1 
5442  C CG2 . THR B 328 ? 0.5942 0.8873 0.6390 -0.0746 0.1381  -0.3453 337 THR B CG2 
5443  N N   . ASP B 329 ? 0.6563 0.8971 0.6743 -0.0364 0.1242  -0.3901 338 ASP B N   
5444  C CA  . ASP B 329 ? 0.6879 0.8735 0.6949 -0.0392 0.1153  -0.3927 338 ASP B CA  
5445  C C   . ASP B 329 ? 0.6847 0.8460 0.6872 -0.0189 0.1123  -0.3995 338 ASP B C   
5446  O O   . ASP B 329 ? 0.7211 0.8527 0.7067 -0.0066 0.1036  -0.4173 338 ASP B O   
5447  C CB  . ASP B 329 ? 0.7444 0.9051 0.7326 -0.0463 0.1054  -0.4085 338 ASP B CB  
5448  C CG  . ASP B 329 ? 0.8010 0.9914 0.7816 -0.0329 0.1054  -0.4285 338 ASP B CG  
5449  O OD1 . ASP B 329 ? 0.8621 1.0515 0.8323 -0.0426 0.1007  -0.4376 338 ASP B OD1 
5450  O OD2 . ASP B 329 ? 0.8105 1.0279 0.7952 -0.0131 0.1098  -0.4350 338 ASP B OD2 
5451  N N   . ARG B 330 ? 0.6401 0.8131 0.6562 -0.0146 0.1187  -0.3858 339 ARG B N   
5452  C CA  . ARG B 330 ? 0.6395 0.7955 0.6521 0.0055  0.1163  -0.3924 339 ARG B CA  
5453  C C   . ARG B 330 ? 0.6460 0.7511 0.6534 0.0002  0.1101  -0.3858 339 ARG B C   
5454  O O   . ARG B 330 ? 0.6335 0.7265 0.6453 -0.0195 0.1105  -0.3714 339 ARG B O   
5455  C CB  . ARG B 330 ? 0.6066 0.8017 0.6353 0.0142  0.1256  -0.3817 339 ARG B CB  
5456  C CG  . ARG B 330 ? 0.5896 0.8419 0.6288 0.0116  0.1340  -0.3773 339 ARG B CG  
5457  C CD  . ARG B 330 ? 0.5660 0.8385 0.6207 0.0036  0.1416  -0.3553 339 ARG B CD  
5458  N NE  . ARG B 330 ? 0.5361 0.8597 0.5991 -0.0009 0.1485  -0.3481 339 ARG B NE  
5459  C CZ  . ARG B 330 ? 0.5256 0.8870 0.5931 0.0096  0.1524  -0.3489 339 ARG B CZ  
5460  N NH1 . ARG B 330 ? 0.5544 0.9109 0.6196 0.0274  0.1504  -0.3577 339 ARG B NH1 
5461  N NH2 . ARG B 330 ? 0.4758 0.8809 0.5491 0.0019  0.1576  -0.3403 339 ARG B NH2 
5462  N N   . GLY B 331 ? 0.6611 0.7400 0.6595 0.0188  0.1047  -0.3956 340 GLY B N   
5463  C CA  . GLY B 331 ? 0.6728 0.7009 0.6642 0.0162  0.0978  -0.3904 340 GLY B CA  
5464  C C   . GLY B 331 ? 0.7206 0.6972 0.6869 0.0280  0.0841  -0.4092 340 GLY B C   
5465  O O   . GLY B 331 ? 0.7447 0.7265 0.6993 0.0462  0.0805  -0.4286 340 GLY B O   
5466  N N   . TRP B 332 ? 0.7389 0.6645 0.6952 0.0174  0.0757  -0.4035 341 TRP B N   
5467  C CA  . TRP B 332 ? 0.7931 0.6613 0.7224 0.0273  0.0608  -0.4194 341 TRP B CA  
5468  C C   . TRP B 332 ? 0.8333 0.6720 0.7427 0.0116  0.0503  -0.4286 341 TRP B C   
5469  O O   . TRP B 332 ? 0.8328 0.6628 0.7439 -0.0157 0.0491  -0.4159 341 TRP B O   
5470  C CB  . TRP B 332 ? 0.8042 0.6281 0.7295 0.0234  0.0551  -0.4085 341 TRP B CB  
5471  C CG  . TRP B 332 ? 0.7823 0.6218 0.7186 0.0446  0.0610  -0.4059 341 TRP B CG  
5472  C CD1 . TRP B 332 ? 0.7397 0.6131 0.6999 0.0402  0.0727  -0.3877 341 TRP B CD1 
5473  C CD2 . TRP B 332 ? 0.8099 0.6329 0.7328 0.0747  0.0550  -0.4221 341 TRP B CD2 
5474  N NE1 . TRP B 332 ? 0.7420 0.6223 0.7055 0.0637  0.0747  -0.3908 341 TRP B NE1 
5475  C CE2 . TRP B 332 ? 0.7738 0.6253 0.7152 0.0859  0.0642  -0.4118 341 TRP B CE2 
5476  C CE3 . TRP B 332 ? 0.8637 0.6500 0.7591 0.0943  0.0422  -0.4448 341 TRP B CE3 
5477  C CZ2 . TRP B 332 ? 0.7795 0.6285 0.7147 0.1153  0.0616  -0.4226 341 TRP B CZ2 
5478  C CZ3 . TRP B 332 ? 0.8690 0.6514 0.7572 0.1258  0.0394  -0.4563 341 TRP B CZ3 
5479  C CH2 . TRP B 332 ? 0.8206 0.6365 0.7296 0.1358  0.0494  -0.4448 341 TRP B CH2 
5480  N N   . TYR B 333 ? 0.8728 0.6962 0.7615 0.0297  0.0420  -0.4513 342 TYR B N   
5481  C CA  . TYR B 333 ? 0.9204 0.6999 0.7831 0.0176  0.0281  -0.4624 342 TYR B CA  
5482  C C   . TYR B 333 ? 0.9783 0.6894 0.8138 0.0304  0.0125  -0.4718 342 TYR B C   
5483  O O   . TYR B 333 ? 0.9722 0.6807 0.8109 0.0528  0.0142  -0.4727 342 TYR B O   
5484  C CB  . TYR B 333 ? 0.9279 0.7343 0.7834 0.0299  0.0284  -0.4820 342 TYR B CB  
5485  C CG  . TYR B 333 ? 0.8784 0.7520 0.7605 0.0172  0.0436  -0.4711 342 TYR B CG  
5486  C CD1 . TYR B 333 ? 0.8340 0.7636 0.7419 0.0283  0.0584  -0.4624 342 TYR B CD1 
5487  C CD2 . TYR B 333 ? 0.8942 0.7742 0.7744 -0.0073 0.0423  -0.4686 342 TYR B CD2 
5488  C CE1 . TYR B 333 ? 0.7988 0.7847 0.7277 0.0162  0.0706  -0.4520 342 TYR B CE1 
5489  C CE2 . TYR B 333 ? 0.8468 0.7867 0.7496 -0.0179 0.0554  -0.4586 342 TYR B CE2 
5490  C CZ  . TYR B 333 ? 0.8047 0.7948 0.7308 -0.0058 0.0691  -0.4504 342 TYR B CZ  
5491  O OH  . TYR B 333 ? 0.7878 0.8315 0.7329 -0.0168 0.0804  -0.4402 342 TYR B OH  
5492  N N   . CYS B 334 ? 1.0356 0.6904 0.8430 0.0153  -0.0035 -0.4782 343 CYS B N   
5493  C CA  . CYS B 334 ? 1.0964 0.6775 0.8759 0.0194  -0.0203 -0.4821 343 CYS B CA  
5494  C C   . CYS B 334 ? 1.1495 0.6738 0.8987 -0.0067 -0.0378 -0.4855 343 CYS B C   
5495  O O   . CYS B 334 ? 1.1316 0.6671 0.8903 -0.0400 -0.0354 -0.4693 343 CYS B O   
5496  C CB  . CYS B 334 ? 1.0647 0.6472 0.8634 0.0113  -0.0137 -0.4595 343 CYS B CB  
5497  S SG  . CYS B 334 ? 1.1580 0.6568 0.9263 0.0197  -0.0323 -0.4619 343 CYS B SG  
5498  N N   . ASP B 335 ? 1.2218 0.6866 0.9334 0.0091  -0.0560 -0.5070 344 ASP B N   
5499  C CA  . ASP B 335 ? 1.2831 0.6970 0.9620 -0.0127 -0.0737 -0.5150 344 ASP B CA  
5500  C C   . ASP B 335 ? 1.3076 0.6719 0.9747 -0.0484 -0.0850 -0.4960 344 ASP B C   
5501  O O   . ASP B 335 ? 1.3262 0.6508 0.9856 -0.0436 -0.0913 -0.4889 344 ASP B O   
5502  C CB  . ASP B 335 ? 1.3628 0.7159 0.9994 0.0164  -0.0926 -0.5434 344 ASP B CB  
5503  C CG  . ASP B 335 ? 1.3810 0.7708 1.0152 0.0383  -0.0887 -0.5662 344 ASP B CG  
5504  O OD1 . ASP B 335 ? 1.4062 0.8175 1.0420 0.0167  -0.0873 -0.5671 344 ASP B OD1 
5505  O OD2 . ASP B 335 ? 1.4097 0.8069 1.0387 0.0780  -0.0878 -0.5838 344 ASP B OD2 
5506  N N   . ASN B 336 ? 1.3134 0.6805 0.9775 -0.0842 -0.0884 -0.4879 345 ASN B N   
5507  C CA  . ASN B 336 ? 1.3526 0.6702 0.9991 -0.1213 -0.1025 -0.4716 345 ASN B CA  
5508  C C   . ASN B 336 ? 1.4330 0.6913 1.0368 -0.1346 -0.1245 -0.4873 345 ASN B C   
5509  O O   . ASN B 336 ? 1.4739 0.7205 1.0592 -0.1093 -0.1299 -0.5122 345 ASN B O   
5510  C CB  . ASN B 336 ? 1.2952 0.6703 0.9745 -0.1558 -0.0885 -0.4457 345 ASN B CB  
5511  C CG  . ASN B 336 ? 1.3005 0.6433 0.9752 -0.1855 -0.0961 -0.4227 345 ASN B CG  
5512  O OD1 . ASN B 336 ? 1.2593 0.5882 0.9402 -0.1738 -0.0941 -0.4144 345 ASN B OD1 
5513  N ND2 . ASN B 336 ? 1.3459 0.6813 1.0105 -0.2247 -0.1045 -0.4116 345 ASN B ND2 
5514  N N   . ALA B 337 ? 1.4631 0.6864 1.0504 -0.1748 -0.1374 -0.4727 346 ALA B N   
5515  C CA  . ALA B 337 ? 1.5451 0.6993 1.0859 -0.1910 -0.1619 -0.4858 346 ALA B CA  
5516  C C   . ALA B 337 ? 1.5485 0.7311 1.0856 -0.1859 -0.1600 -0.5052 346 ALA B C   
5517  O O   . ALA B 337 ? 1.5296 0.7465 1.0760 -0.2173 -0.1567 -0.4962 346 ALA B O   
5518  C CB  . ALA B 337 ? 1.5661 0.6938 1.0958 -0.2399 -0.1735 -0.4632 346 ALA B CB  
5519  N N   . GLY B 338 ? 1.5729 0.7454 1.0971 -0.1450 -0.1617 -0.5316 347 GLY B N   
5520  C CA  . GLY B 338 ? 1.5864 0.7792 1.1019 -0.1355 -0.1620 -0.5532 347 GLY B CA  
5521  C C   . GLY B 338 ? 1.4998 0.7926 1.0615 -0.1314 -0.1359 -0.5480 347 GLY B C   
5522  O O   . GLY B 338 ? 1.5050 0.8258 1.0649 -0.1212 -0.1331 -0.5649 347 GLY B O   
5523  N N   . SER B 339 ? 1.4227 0.7674 1.0242 -0.1400 -0.1176 -0.5242 348 SER B N   
5524  C CA  . SER B 339 ? 1.3335 0.7687 0.9781 -0.1400 -0.0939 -0.5150 348 SER B CA  
5525  C C   . SER B 339 ? 1.2844 0.7476 0.9566 -0.1146 -0.0791 -0.5068 348 SER B C   
5526  O O   . SER B 339 ? 1.3175 0.7294 0.9725 -0.0982 -0.0886 -0.5110 348 SER B O   
5527  C CB  . SER B 339 ? 1.3006 0.7669 0.9622 -0.1833 -0.0891 -0.4909 348 SER B CB  
5528  O OG  . SER B 339 ? 1.3422 0.7807 0.9762 -0.2094 -0.1043 -0.4978 348 SER B OG  
5529  N N   . VAL B 340 ? 1.2069 0.7486 0.9196 -0.1110 -0.0569 -0.4956 349 VAL B N   
5530  C CA  . VAL B 340 ? 1.1576 0.7333 0.8973 -0.0854 -0.0418 -0.4894 349 VAL B CA  
5531  C C   . VAL B 340 ? 1.0965 0.7204 0.8713 -0.1059 -0.0263 -0.4621 349 VAL B C   
5532  O O   . VAL B 340 ? 1.0613 0.7338 0.8537 -0.1240 -0.0170 -0.4535 349 VAL B O   
5533  C CB  . VAL B 340 ? 1.1222 0.7538 0.8774 -0.0552 -0.0289 -0.5039 349 VAL B CB  
5534  C CG1 . VAL B 340 ? 1.0835 0.7386 0.8590 -0.0288 -0.0175 -0.4994 349 VAL B CG1 
5535  C CG2 . VAL B 340 ? 1.1873 0.7861 0.9093 -0.0345 -0.0425 -0.5332 349 VAL B CG2 
5536  N N   . SER B 341 ? 1.0912 0.7020 0.8750 -0.1008 -0.0238 -0.4493 350 SER B N   
5537  C CA  . SER B 341 ? 1.0367 0.6893 0.8526 -0.1156 -0.0094 -0.4236 350 SER B CA  
5538  C C   . SER B 341 ? 0.9882 0.6982 0.8348 -0.0914 0.0093  -0.4203 350 SER B C   
5539  O O   . SER B 341 ? 0.9911 0.6933 0.8365 -0.0629 0.0102  -0.4295 350 SER B O   
5540  C CB  . SER B 341 ? 1.0518 0.6575 0.8591 -0.1290 -0.0180 -0.4090 350 SER B CB  
5541  O OG  . SER B 341 ? 1.0646 0.6422 0.8553 -0.1633 -0.0300 -0.4010 350 SER B OG  
5542  N N   . PHE B 342 ? 0.9472 0.7156 0.8202 -0.1037 0.0234  -0.4065 351 PHE B N   
5543  C CA  . PHE B 342 ? 0.9082 0.7308 0.8082 -0.0857 0.0399  -0.4017 351 PHE B CA  
5544  C C   . PHE B 342 ? 0.8791 0.7237 0.8021 -0.0980 0.0497  -0.3771 351 PHE B C   
5545  O O   . PHE B 342 ? 0.8717 0.7251 0.7997 -0.1233 0.0502  -0.3627 351 PHE B O   
5546  C CB  . PHE B 342 ? 0.8811 0.7547 0.7904 -0.0845 0.0480  -0.4086 351 PHE B CB  
5547  C CG  . PHE B 342 ? 0.8278 0.7605 0.7648 -0.0737 0.0647  -0.3993 351 PHE B CG  
5548  C CD1 . PHE B 342 ? 0.8244 0.7665 0.7678 -0.0481 0.0696  -0.4040 351 PHE B CD1 
5549  C CD2 . PHE B 342 ? 0.7949 0.7736 0.7499 -0.0896 0.0745  -0.3854 351 PHE B CD2 
5550  C CE1 . PHE B 342 ? 0.7852 0.7795 0.7518 -0.0414 0.0834  -0.3942 351 PHE B CE1 
5551  C CE2 . PHE B 342 ? 0.7532 0.7811 0.7302 -0.0809 0.0880  -0.3763 351 PHE B CE2 
5552  C CZ  . PHE B 342 ? 0.7499 0.7847 0.7323 -0.0582 0.0922  -0.3803 351 PHE B CZ  
5553  N N   . PHE B 343 ? 0.8713 0.7261 0.8074 -0.0790 0.0571  -0.3729 352 PHE B N   
5554  C CA  . PHE B 343 ? 0.8487 0.7197 0.8042 -0.0856 0.0656  -0.3517 352 PHE B CA  
5555  C C   . PHE B 343 ? 0.8203 0.7471 0.7982 -0.0730 0.0802  -0.3477 352 PHE B C   
5556  O O   . PHE B 343 ? 0.8178 0.7530 0.7980 -0.0502 0.0832  -0.3564 352 PHE B O   
5557  C CB  . PHE B 343 ? 0.8637 0.6930 0.8121 -0.0748 0.0598  -0.3502 352 PHE B CB  
5558  C CG  . PHE B 343 ? 0.9175 0.6844 0.8369 -0.0775 0.0428  -0.3617 352 PHE B CG  
5559  C CD1 . PHE B 343 ? 0.9488 0.6935 0.8488 -0.0573 0.0348  -0.3846 352 PHE B CD1 
5560  C CD2 . PHE B 343 ? 0.9324 0.6628 0.8417 -0.1004 0.0338  -0.3499 352 PHE B CD2 
5561  C CE1 . PHE B 343 ? 0.9993 0.6806 0.8683 -0.0587 0.0172  -0.3961 352 PHE B CE1 
5562  C CE2 . PHE B 343 ? 0.9796 0.6477 0.8586 -0.1049 0.0162  -0.3598 352 PHE B CE2 
5563  C CZ  . PHE B 343 ? 1.0172 0.6576 0.8748 -0.0834 0.0074  -0.3835 352 PHE B CZ  
5564  N N   . PRO B 344 ? 0.8064 0.7719 0.7993 -0.0878 0.0886  -0.3342 353 PRO B N   
5565  C CA  . PRO B 344 ? 0.7851 0.8037 0.7960 -0.0810 0.1010  -0.3293 353 PRO B CA  
5566  C C   . PRO B 344 ? 0.7819 0.8148 0.8064 -0.0660 0.1087  -0.3211 353 PRO B C   
5567  O O   . PRO B 344 ? 0.7713 0.8355 0.8027 -0.0521 0.1149  -0.3258 353 PRO B O   
5568  C CB  . PRO B 344 ? 0.7609 0.8031 0.7804 -0.1021 0.1050  -0.3138 353 PRO B CB  
5569  C CG  . PRO B 344 ? 0.7885 0.7962 0.7927 -0.1208 0.0941  -0.3156 353 PRO B CG  
5570  C CD  . PRO B 344 ? 0.8070 0.7660 0.7994 -0.1131 0.0858  -0.3203 353 PRO B CD  
5571  N N   . GLN B 345 ? 0.8013 0.8129 0.8289 -0.0694 0.1080  -0.3088 354 GLN B N   
5572  C CA  . GLN B 345 ? 0.7949 0.8193 0.8351 -0.0572 0.1149  -0.2996 354 GLN B CA  
5573  C C   . GLN B 345 ? 0.8190 0.8060 0.8542 -0.0469 0.1100  -0.2998 354 GLN B C   
5574  O O   . GLN B 345 ? 0.8328 0.7852 0.8610 -0.0578 0.1035  -0.2940 354 GLN B O   
5575  C CB  . GLN B 345 ? 0.7616 0.8136 0.8158 -0.0683 0.1229  -0.2801 354 GLN B CB  
5576  C CG  . GLN B 345 ? 0.7731 0.8207 0.8250 -0.0889 0.1203  -0.2714 354 GLN B CG  
5577  C CD  . GLN B 345 ? 0.8020 0.8067 0.8441 -0.0970 0.1117  -0.2697 354 GLN B CD  
5578  O OE1 . GLN B 345 ? 0.8010 0.7894 0.8461 -0.0926 0.1118  -0.2618 354 GLN B OE1 
5579  N NE2 . GLN B 345 ? 0.8132 0.7981 0.8420 -0.1098 0.1032  -0.2771 354 GLN B NE2 
5580  N N   . ALA B 346 ? 0.8204 0.8178 0.8591 -0.0268 0.1129  -0.3059 355 ALA B N   
5581  C CA  . ALA B 346 ? 0.8320 0.8037 0.8686 -0.0131 0.1099  -0.3057 355 ALA B CA  
5582  C C   . ALA B 346 ? 0.8452 0.7745 0.8759 -0.0249 0.1035  -0.2959 355 ALA B C   
5583  O O   . ALA B 346 ? 0.8908 0.7773 0.9045 -0.0240 0.0928  -0.3051 355 ALA B O   
5584  C CB  . ALA B 346 ? 0.7934 0.7997 0.8457 -0.0029 0.1193  -0.2965 355 ALA B CB  
5585  N N   . GLU B 347 ? 0.7986 0.7401 0.8417 -0.0353 0.1094  -0.2775 356 GLU B N   
5586  C CA  . GLU B 347 ? 0.7836 0.7039 0.8249 -0.0537 0.1060  -0.2644 356 GLU B CA  
5587  C C   . GLU B 347 ? 0.8063 0.6794 0.8295 -0.0613 0.0938  -0.2704 356 GLU B C   
5588  O O   . GLU B 347 ? 0.8206 0.6606 0.8380 -0.0598 0.0883  -0.2664 356 GLU B O   
5589  C CB  . GLU B 347 ? 0.7654 0.7175 0.8143 -0.0702 0.1114  -0.2553 356 GLU B CB  
5590  C CG  . GLU B 347 ? 0.7646 0.7531 0.8284 -0.0651 0.1216  -0.2448 356 GLU B CG  
5591  C CD  . GLU B 347 ? 0.8228 0.7996 0.8914 -0.0543 0.1230  -0.2379 356 GLU B CD  
5592  O OE1 . GLU B 347 ? 0.8359 0.8267 0.9089 -0.0396 0.1266  -0.2422 356 GLU B OE1 
5593  O OE2 . GLU B 347 ? 0.8440 0.7986 0.9112 -0.0611 0.1200  -0.2283 356 GLU B OE2 
5594  N N   . THR B 348 ? 0.8009 0.6705 0.8140 -0.0702 0.0890  -0.2800 357 THR B N   
5595  C CA  . THR B 348 ? 0.8248 0.6486 0.8172 -0.0810 0.0757  -0.2863 357 THR B CA  
5596  C C   . THR B 348 ? 0.8497 0.6299 0.8250 -0.0622 0.0661  -0.3009 357 THR B C   
5597  O O   . THR B 348 ? 0.8970 0.6291 0.8537 -0.0705 0.0538  -0.3018 357 THR B O   
5598  C CB  . THR B 348 ? 0.8372 0.6699 0.8217 -0.0919 0.0728  -0.2958 357 THR B CB  
5599  O OG1 . THR B 348 ? 0.7991 0.6856 0.8013 -0.0919 0.0848  -0.2916 357 THR B OG1 
5600  C CG2 . THR B 348 ? 0.8623 0.6737 0.8363 -0.1190 0.0644  -0.2875 357 THR B CG2 
5601  N N   . CYS B 349 ? 0.8139 0.6107 0.7939 -0.0373 0.0708  -0.3117 358 CYS B N   
5602  C CA  . CYS B 349 ? 0.8305 0.5906 0.7927 -0.0154 0.0614  -0.3282 358 CYS B CA  
5603  C C   . CYS B 349 ? 0.8024 0.5683 0.7730 0.0058  0.0656  -0.3262 358 CYS B C   
5604  O O   . CYS B 349 ? 0.7572 0.5690 0.7475 0.0123  0.0775  -0.3204 358 CYS B O   
5605  C CB  . CYS B 349 ? 0.8396 0.6128 0.7935 -0.0016 0.0601  -0.3485 358 CYS B CB  
5606  S SG  . CYS B 349 ? 0.8830 0.6391 0.8212 -0.0253 0.0517  -0.3539 358 CYS B SG  
5607  N N   . LYS B 350 ? 0.8294 0.5479 0.7838 0.0163  0.0552  -0.3308 359 LYS B N   
5608  C CA  . LYS B 350 ? 0.8218 0.5450 0.7807 0.0413  0.0576  -0.3332 359 LYS B CA  
5609  C C   . LYS B 350 ? 0.8681 0.5506 0.8025 0.0645  0.0450  -0.3526 359 LYS B C   
5610  O O   . LYS B 350 ? 0.9189 0.5525 0.8292 0.0584  0.0316  -0.3609 359 LYS B O   
5611  C CB  . LYS B 350 ? 0.8093 0.5217 0.7771 0.0346  0.0595  -0.3150 359 LYS B CB  
5612  C CG  . LYS B 350 ? 0.8501 0.5302 0.8110 0.0081  0.0532  -0.3022 359 LYS B CG  
5613  C CD  . LYS B 350 ? 0.8352 0.5437 0.8175 -0.0056 0.0635  -0.2810 359 LYS B CD  
5614  C CE  . LYS B 350 ? 0.8650 0.5635 0.8445 -0.0349 0.0605  -0.2690 359 LYS B CE  
5615  N NZ  . LYS B 350 ? 0.8698 0.6020 0.8699 -0.0445 0.0712  -0.2503 359 LYS B NZ  
5616  N N   . VAL B 351 ? 0.8532 0.5557 0.7926 0.0914  0.0487  -0.3595 360 VAL B N   
5617  C CA  . VAL B 351 ? 0.8882 0.5730 0.8074 0.1200  0.0399  -0.3818 360 VAL B CA  
5618  C C   . VAL B 351 ? 0.8929 0.5762 0.8127 0.1457  0.0393  -0.3830 360 VAL B C   
5619  O O   . VAL B 351 ? 0.8477 0.5722 0.7901 0.1466  0.0507  -0.3709 360 VAL B O   
5620  C CB  . VAL B 351 ? 0.8659 0.6015 0.7917 0.1295  0.0471  -0.3950 360 VAL B CB  
5621  C CG1 . VAL B 351 ? 0.8019 0.6067 0.7587 0.1252  0.0642  -0.3818 360 VAL B CG1 
5622  C CG2 . VAL B 351 ? 0.9096 0.6377 0.8164 0.1635  0.0395  -0.4186 360 VAL B CG2 
5623  N N   . GLN B 352 ? 0.9565 0.5900 0.8494 0.1666  0.0251  -0.3978 361 GLN B N   
5624  C CA  . GLN B 352 ? 0.9856 0.6085 0.8743 0.1925  0.0218  -0.3999 361 GLN B CA  
5625  C C   . GLN B 352 ? 1.0327 0.6346 0.8951 0.2274  0.0105  -0.4254 361 GLN B C   
5626  O O   . GLN B 352 ? 1.0979 0.6335 0.9291 0.2309  -0.0061 -0.4357 361 GLN B O   
5627  C CB  . GLN B 352 ? 1.0170 0.5810 0.8950 0.1790  0.0125  -0.3866 361 GLN B CB  
5628  C CG  . GLN B 352 ? 1.0939 0.6422 0.9670 0.2034  0.0084  -0.3865 361 GLN B CG  
5629  C CD  . GLN B 352 ? 1.1755 0.7242 1.0664 0.1827  0.0143  -0.3619 361 GLN B CD  
5630  O OE1 . GLN B 352 ? 1.2456 0.7389 1.1216 0.1717  0.0038  -0.3536 361 GLN B OE1 
5631  N NE2 . GLN B 352 ? 1.1456 0.7567 1.0672 0.1757  0.0308  -0.3497 361 GLN B NE2 
5632  N N   . SER B 353 ? 1.0063 0.6648 0.8797 0.2532  0.0187  -0.4351 362 SER B N   
5633  C CA  . SER B 353 ? 1.0410 0.6962 0.8922 0.2875  0.0104  -0.4609 362 SER B CA  
5634  C C   . SER B 353 ? 1.0519 0.6965 0.8905 0.2758  0.0063  -0.4726 362 SER B C   
5635  O O   . SER B 353 ? 1.0063 0.6984 0.8665 0.2553  0.0184  -0.4650 362 SER B O   
5636  C CB  . SER B 353 ? 1.1074 0.6945 0.9272 0.3115  -0.0070 -0.4712 362 SER B CB  
5637  O OG  . SER B 353 ? 1.1550 0.7471 0.9544 0.3504  -0.0141 -0.4967 362 SER B OG  
5638  N N   . ASN B 354 ? 1.1123 0.6933 0.9151 0.2881  -0.0113 -0.4906 363 ASN B N   
5639  C CA  . ASN B 354 ? 1.1297 0.6970 0.9170 0.2784  -0.0169 -0.5035 363 ASN B CA  
5640  C C   . ASN B 354 ? 1.1418 0.6490 0.9170 0.2418  -0.0261 -0.4921 363 ASN B C   
5641  O O   . ASN B 354 ? 1.1788 0.6505 0.9311 0.2334  -0.0367 -0.5035 363 ASN B O   
5642  C CB  . ASN B 354 ? 1.1975 0.7338 0.9496 0.3154  -0.0317 -0.5325 363 ASN B CB  
5643  C CG  . ASN B 354 ? 1.2714 0.7192 0.9877 0.3265  -0.0521 -0.5379 363 ASN B CG  
5644  O OD1 . ASN B 354 ? 1.2631 0.6829 0.9845 0.3122  -0.0533 -0.5197 363 ASN B OD1 
5645  N ND2 . ASN B 354 ? 1.3517 0.7531 1.0297 0.3522  -0.0690 -0.5629 363 ASN B ND2 
5646  N N   . ARG B 355 ? 1.1060 0.6046 0.8964 0.2201  -0.0220 -0.4692 364 ARG B N   
5647  C CA  . ARG B 355 ? 1.1166 0.5670 0.8987 0.1847  -0.0294 -0.4552 364 ARG B CA  
5648  C C   . ARG B 355 ? 1.0491 0.5519 0.8641 0.1519  -0.0132 -0.4356 364 ARG B C   
5649  O O   . ARG B 355 ? 0.9932 0.5494 0.8383 0.1518  0.0021  -0.4225 364 ARG B O   
5650  C CB  . ARG B 355 ? 1.1362 0.5405 0.9108 0.1837  -0.0369 -0.4428 364 ARG B CB  
5651  C CG  . ARG B 355 ? 1.2035 0.5297 0.9473 0.1627  -0.0553 -0.4405 364 ARG B CG  
5652  C CD  . ARG B 355 ? 1.2725 0.5474 0.9767 0.1847  -0.0733 -0.4663 364 ARG B CD  
5653  N NE  . ARG B 355 ? 1.3180 0.5547 1.0037 0.1533  -0.0837 -0.4656 364 ARG B NE  
5654  C CZ  . ARG B 355 ? 1.4002 0.5620 1.0427 0.1565  -0.1057 -0.4802 364 ARG B CZ  
5655  N NH1 . ARG B 355 ? 1.4564 0.5723 1.0693 0.1924  -0.1196 -0.4974 364 ARG B NH1 
5656  N NH2 . ARG B 355 ? 1.4394 0.5726 1.0671 0.1242  -0.1143 -0.4779 364 ARG B NH2 
5657  N N   . VAL B 356 ? 1.0583 0.5452 0.8660 0.1243  -0.0173 -0.4335 365 VAL B N   
5658  C CA  . VAL B 356 ? 0.9995 0.5356 0.8358 0.0947  -0.0030 -0.4163 365 VAL B CA  
5659  C C   . VAL B 356 ? 1.0216 0.5171 0.8500 0.0596  -0.0106 -0.4004 365 VAL B C   
5660  O O   . VAL B 356 ? 1.0911 0.5217 0.8880 0.0537  -0.0284 -0.4069 365 VAL B O   
5661  C CB  . VAL B 356 ? 0.9833 0.5576 0.8229 0.0938  0.0021  -0.4286 365 VAL B CB  
5662  C CG1 . VAL B 356 ? 0.9389 0.5427 0.7974 0.0592  0.0109  -0.4117 365 VAL B CG1 
5663  C CG2 . VAL B 356 ? 0.9478 0.5847 0.8059 0.1203  0.0149  -0.4367 365 VAL B CG2 
5664  N N   . PHE B 357 ? 0.9687 0.5032 0.8244 0.0363  0.0021  -0.3793 366 PHE B N   
5665  C CA  . PHE B 357 ? 0.9746 0.4840 0.8275 0.0028  -0.0027 -0.3615 366 PHE B CA  
5666  C C   . PHE B 357 ? 0.9280 0.4924 0.8050 -0.0188 0.0106  -0.3502 366 PHE B C   
5667  O O   . PHE B 357 ? 0.8727 0.4895 0.7773 -0.0144 0.0260  -0.3407 366 PHE B O   
5668  C CB  . PHE B 357 ? 0.9605 0.4585 0.8218 0.0017  -0.0012 -0.3446 366 PHE B CB  
5669  C CG  . PHE B 357 ? 1.0073 0.4487 0.8440 0.0231  -0.0150 -0.3541 366 PHE B CG  
5670  C CD1 . PHE B 357 ? 1.0101 0.4643 0.8481 0.0590  -0.0121 -0.3682 366 PHE B CD1 
5671  C CD2 . PHE B 357 ? 1.0488 0.4243 0.8594 0.0076  -0.0317 -0.3488 366 PHE B CD2 
5672  C CE1 . PHE B 357 ? 1.0485 0.4499 0.8619 0.0818  -0.0256 -0.3777 366 PHE B CE1 
5673  C CE2 . PHE B 357 ? 1.0889 0.4078 0.8740 0.0286  -0.0458 -0.3576 366 PHE B CE2 
5674  C CZ  . PHE B 357 ? 1.0857 0.4176 0.8723 0.0671  -0.0426 -0.3725 366 PHE B CZ  
5675  N N   . CYS B 358 ? 0.9560 0.5084 0.8212 -0.0417 0.0040  -0.3514 367 CYS B N   
5676  C CA  . CYS B 358 ? 0.9237 0.5280 0.8103 -0.0630 0.0157  -0.3401 367 CYS B CA  
5677  C C   . CYS B 358 ? 0.9373 0.5259 0.8193 -0.0980 0.0099  -0.3233 367 CYS B C   
5678  O O   . CYS B 358 ? 0.9895 0.5226 0.8485 -0.1091 -0.0049 -0.3212 367 CYS B O   
5679  C CB  . CYS B 358 ? 0.9231 0.5531 0.8077 -0.0571 0.0180  -0.3565 367 CYS B CB  
5680  S SG  . CYS B 358 ? 0.9206 0.5868 0.8163 -0.0189 0.0277  -0.3720 367 CYS B SG  
5681  N N   . ASP B 359 ? 0.8970 0.5363 0.8002 -0.1150 0.0214  -0.3107 368 ASP B N   
5682  C CA  . ASP B 359 ? 0.9072 0.5463 0.8098 -0.1475 0.0182  -0.2937 368 ASP B CA  
5683  C C   . ASP B 359 ? 0.9191 0.5789 0.8184 -0.1657 0.0172  -0.2978 368 ASP B C   
5684  O O   . ASP B 359 ? 0.8775 0.5909 0.7962 -0.1619 0.0300  -0.2979 368 ASP B O   
5685  C CB  . ASP B 359 ? 0.8544 0.5375 0.7841 -0.1519 0.0320  -0.2735 368 ASP B CB  
5686  C CG  . ASP B 359 ? 0.8690 0.5445 0.7959 -0.1810 0.0270  -0.2547 368 ASP B CG  
5687  O OD1 . ASP B 359 ? 0.8972 0.5731 0.8145 -0.2050 0.0208  -0.2528 368 ASP B OD1 
5688  O OD2 . ASP B 359 ? 0.8631 0.5339 0.7968 -0.1806 0.0290  -0.2415 368 ASP B OD2 
5689  N N   . THR B 360 ? 0.9843 0.6001 0.8574 -0.1863 0.0012  -0.3007 369 THR B N   
5690  C CA  . THR B 360 ? 1.0021 0.6332 0.8692 -0.2088 -0.0021 -0.3026 369 THR B CA  
5691  C C   . THR B 360 ? 0.9611 0.6595 0.8563 -0.2221 0.0130  -0.2856 369 THR B C   
5692  O O   . THR B 360 ? 0.9385 0.6806 0.8468 -0.2159 0.0226  -0.2911 369 THR B O   
5693  C CB  . THR B 360 ? 1.0533 0.6333 0.8919 -0.2380 -0.0207 -0.2984 369 THR B CB  
5694  O OG1 . THR B 360 ? 1.0930 0.6046 0.9024 -0.2233 -0.0360 -0.3140 369 THR B OG1 
5695  C CG2 . THR B 360 ? 1.0702 0.6676 0.9017 -0.2611 -0.0245 -0.3014 369 THR B CG2 
5696  N N   . MET B 361 ? 0.9622 0.6688 0.8659 -0.2381 0.0148  -0.2652 370 MET B N   
5697  C CA  . MET B 361 ? 0.9301 0.6970 0.8566 -0.2517 0.0267  -0.2481 370 MET B CA  
5698  C C   . MET B 361 ? 0.8928 0.7118 0.8334 -0.2473 0.0373  -0.2535 370 MET B C   
5699  O O   . MET B 361 ? 0.8992 0.7402 0.8375 -0.2699 0.0350  -0.2488 370 MET B O   
5700  C CB  . MET B 361 ? 0.9027 0.6909 0.8491 -0.2426 0.0371  -0.2326 370 MET B CB  
5701  C CG  . MET B 361 ? 0.9567 0.7427 0.9002 -0.2693 0.0319  -0.2125 370 MET B CG  
5702  S SD  . MET B 361 ? 1.0420 0.8742 0.9876 -0.3034 0.0313  -0.1998 370 MET B SD  
5703  C CE  . MET B 361 ? 1.0700 0.8604 0.9857 -0.3236 0.0139  -0.2145 370 MET B CE  
5704  N N   . ASN B 362 ? 0.8547 0.6957 0.8094 -0.2202 0.0483  -0.2620 371 ASN B N   
5705  C CA  . ASN B 362 ? 0.8236 0.7117 0.7893 -0.2178 0.0570  -0.2666 371 ASN B CA  
5706  C C   . ASN B 362 ? 0.8355 0.7150 0.7907 -0.2059 0.0539  -0.2881 371 ASN B C   
5707  O O   . ASN B 362 ? 0.8170 0.7362 0.7806 -0.2055 0.0606  -0.2914 371 ASN B O   
5708  C CB  . ASN B 362 ? 0.7713 0.7115 0.7622 -0.2080 0.0725  -0.2542 371 ASN B CB  
5709  C CG  . ASN B 362 ? 0.7612 0.7311 0.7598 -0.2290 0.0748  -0.2350 371 ASN B CG  
5710  O OD1 . ASN B 362 ? 0.7531 0.7549 0.7533 -0.2431 0.0758  -0.2324 371 ASN B OD1 
5711  N ND2 . ASN B 362 ? 0.7696 0.7307 0.7722 -0.2310 0.0751  -0.2217 371 ASN B ND2 
5712  N N   . SER B 363 ? 0.8694 0.6970 0.8045 -0.1967 0.0428  -0.3025 372 SER B N   
5713  C CA  . SER B 363 ? 0.8860 0.6991 0.8064 -0.1840 0.0375  -0.3249 372 SER B CA  
5714  C C   . SER B 363 ? 0.8795 0.7192 0.7971 -0.1988 0.0371  -0.3300 372 SER B C   
5715  O O   . SER B 363 ? 0.8799 0.7338 0.7982 -0.2254 0.0352  -0.3176 372 SER B O   
5716  C CB  . SER B 363 ? 0.9502 0.6935 0.8405 -0.1830 0.0200  -0.3370 372 SER B CB  
5717  O OG  . SER B 363 ? 0.9939 0.7083 0.8684 -0.2141 0.0079  -0.3270 372 SER B OG  
5718  N N   . LEU B 364 ? 0.8713 0.7198 0.7853 -0.1814 0.0385  -0.3483 373 LEU B N   
5719  C CA  . LEU B 364 ? 0.8695 0.7365 0.7768 -0.1924 0.0363  -0.3572 373 LEU B CA  
5720  C C   . LEU B 364 ? 0.9223 0.7377 0.7996 -0.1868 0.0210  -0.3790 373 LEU B C   
5721  O O   . LEU B 364 ? 0.9369 0.7307 0.8070 -0.1605 0.0193  -0.3932 373 LEU B O   
5722  C CB  . LEU B 364 ? 0.8211 0.7466 0.7492 -0.1768 0.0510  -0.3599 373 LEU B CB  
5723  C CG  . LEU B 364 ? 0.7694 0.7519 0.7195 -0.1901 0.0627  -0.3426 373 LEU B CG  
5724  C CD1 . LEU B 364 ? 0.7665 0.7494 0.7245 -0.2074 0.0636  -0.3212 373 LEU B CD1 
5725  C CD2 . LEU B 364 ? 0.7150 0.7422 0.6854 -0.1692 0.0770  -0.3415 373 LEU B CD2 
5726  N N   . THR B 365 ? 0.9494 0.7448 0.8074 -0.2110 0.0093  -0.3819 374 THR B N   
5727  C CA  . THR B 365 ? 1.0052 0.7434 0.8299 -0.2068 -0.0076 -0.4026 374 THR B CA  
5728  C C   . THR B 365 ? 0.9940 0.7606 0.8169 -0.1972 -0.0048 -0.4200 374 THR B C   
5729  O O   . THR B 365 ? 0.9658 0.7811 0.8031 -0.2116 0.0030  -0.4130 374 THR B O   
5730  C CB  . THR B 365 ? 1.0554 0.7459 0.8552 -0.2391 -0.0249 -0.3964 374 THR B CB  
5731  O OG1 . THR B 365 ? 1.0480 0.7524 0.8639 -0.2574 -0.0200 -0.3717 374 THR B OG1 
5732  C CG2 . THR B 365 ? 1.1193 0.7306 0.8841 -0.2286 -0.0434 -0.4119 374 THR B CG2 
5733  N N   . LEU B 366 ? 1.0145 0.7543 0.8204 -0.1705 -0.0106 -0.4425 375 LEU B N   
5734  C CA  . LEU B 366 ? 0.9959 0.7677 0.8020 -0.1549 -0.0062 -0.4602 375 LEU B CA  
5735  C C   . LEU B 366 ? 1.0658 0.7814 0.8354 -0.1415 -0.0234 -0.4859 375 LEU B C   
5736  O O   . LEU B 366 ? 1.1126 0.7672 0.8598 -0.1345 -0.0363 -0.4912 375 LEU B O   
5737  C CB  . LEU B 366 ? 0.9389 0.7591 0.7706 -0.1256 0.0104  -0.4609 375 LEU B CB  
5738  C CG  . LEU B 366 ? 0.8450 0.7161 0.7110 -0.1309 0.0272  -0.4375 375 LEU B CG  
5739  C CD1 . LEU B 366 ? 0.7705 0.6748 0.6530 -0.1012 0.0390  -0.4417 375 LEU B CD1 
5740  C CD2 . LEU B 366 ? 0.8072 0.7272 0.6875 -0.1523 0.0347  -0.4273 375 LEU B CD2 
5741  N N   . PRO B 367 ? 1.0762 0.8113 0.8381 -0.1362 -0.0242 -0.5025 376 PRO B N   
5742  C CA  . PRO B 367 ? 1.1491 0.8318 0.8737 -0.1211 -0.0411 -0.5292 376 PRO B CA  
5743  C C   . PRO B 367 ? 1.1552 0.8435 0.8793 -0.0784 -0.0371 -0.5468 376 PRO B C   
5744  O O   . PRO B 367 ? 1.0970 0.8468 0.8517 -0.0628 -0.0193 -0.5411 376 PRO B O   
5745  C CB  . PRO B 367 ? 1.1492 0.8626 0.8703 -0.1336 -0.0410 -0.5379 376 PRO B CB  
5746  C CG  . PRO B 367 ? 1.0694 0.8679 0.8323 -0.1346 -0.0184 -0.5221 376 PRO B CG  
5747  C CD  . PRO B 367 ? 1.0261 0.8314 0.8117 -0.1451 -0.0103 -0.4968 376 PRO B CD  
5748  N N   . SER B 368 ? 1.2301 0.8549 0.9182 -0.0599 -0.0545 -0.5679 377 SER B N   
5749  C CA  . SER B 368 ? 1.2516 0.8799 0.9330 -0.0171 -0.0534 -0.5887 377 SER B CA  
5750  C C   . SER B 368 ? 1.2151 0.9178 0.9157 -0.0018 -0.0390 -0.5978 377 SER B C   
5751  O O   . SER B 368 ? 1.1923 0.9310 0.9053 0.0291  -0.0295 -0.6050 377 SER B O   
5752  C CB  . SER B 368 ? 1.3424 0.8913 0.9755 -0.0024 -0.0769 -0.6135 377 SER B CB  
5753  O OG  . SER B 368 ? 1.4012 0.8804 1.0111 -0.0315 -0.0935 -0.6039 377 SER B OG  
5754  N N   . GLU B 369 ? 1.2142 0.9417 0.9171 -0.0246 -0.0376 -0.5967 378 GLU B N   
5755  C CA  . GLU B 369 ? 1.1844 0.9843 0.9059 -0.0155 -0.0240 -0.6028 378 GLU B CA  
5756  C C   . GLU B 369 ? 1.1082 0.9799 0.8712 -0.0085 -0.0022 -0.5849 378 GLU B C   
5757  O O   . GLU B 369 ? 1.0782 1.0088 0.8555 0.0071  0.0089  -0.5910 378 GLU B O   
5758  C CB  . GLU B 369 ? 1.1871 1.0008 0.9067 -0.0470 -0.0259 -0.5993 378 GLU B CB  
5759  C CG  . GLU B 369 ? 1.2887 1.0495 0.9666 -0.0482 -0.0459 -0.6233 378 GLU B CG  
5760  C CD  . GLU B 369 ? 1.4021 1.0693 1.0432 -0.0568 -0.0680 -0.6275 378 GLU B CD  
5761  O OE1 . GLU B 369 ? 1.3897 1.0336 1.0388 -0.0673 -0.0678 -0.6094 378 GLU B OE1 
5762  O OE2 . GLU B 369 ? 1.4962 1.1116 1.0982 -0.0533 -0.0864 -0.6494 378 GLU B OE2 
5763  N N   . VAL B 370 ? 1.0819 0.9479 0.8626 -0.0206 0.0032  -0.5627 379 VAL B N   
5764  C CA  . VAL B 370 ? 1.0224 0.9440 0.8373 -0.0117 0.0211  -0.5467 379 VAL B CA  
5765  C C   . VAL B 370 ? 1.0255 0.9726 0.8414 0.0258  0.0257  -0.5623 379 VAL B C   
5766  O O   . VAL B 370 ? 0.9767 0.9885 0.8173 0.0335  0.0405  -0.5560 379 VAL B O   
5767  C CB  . VAL B 370 ? 1.0067 0.9023 0.8316 -0.0228 0.0221  -0.5262 379 VAL B CB  
5768  C CG1 . VAL B 370 ? 0.9701 0.8988 0.8169 -0.0007 0.0343  -0.5194 379 VAL B CG1 
5769  C CG2 . VAL B 370 ? 0.9759 0.8910 0.8182 -0.0569 0.0280  -0.5034 379 VAL B CG2 
5770  N N   . ASN B 371 ? 1.0924 0.9883 0.8797 0.0486  0.0119  -0.5823 380 ASN B N   
5771  C CA  . ASN B 371 ? 1.1113 1.0268 0.8954 0.0875  0.0140  -0.5988 380 ASN B CA  
5772  C C   . ASN B 371 ? 1.0907 1.0707 0.8814 0.1034  0.0223  -0.6120 380 ASN B C   
5773  O O   . ASN B 371 ? 1.0649 1.0947 0.8709 0.1259  0.0325  -0.6132 380 ASN B O   
5774  C CB  . ASN B 371 ? 1.1901 1.0335 0.9366 0.1101  -0.0048 -0.6204 380 ASN B CB  
5775  C CG  . ASN B 371 ? 1.2384 1.0227 0.9795 0.1005  -0.0121 -0.6070 380 ASN B CG  
5776  O OD1 . ASN B 371 ? 1.2680 1.0536 1.0164 0.1203  -0.0087 -0.6038 380 ASN B OD1 
5777  N ND2 . ASN B 371 ? 1.2893 1.0248 1.0180 0.0688  -0.0221 -0.5981 380 ASN B ND2 
5778  N N   . LEU B 372 ? 1.1046 1.0865 0.8839 0.0908  0.0179  -0.6212 381 LEU B N   
5779  C CA  . LEU B 372 ? 1.0899 1.1349 0.8751 0.1044  0.0256  -0.6334 381 LEU B CA  
5780  C C   . LEU B 372 ? 1.0153 1.1372 0.8390 0.0953  0.0454  -0.6116 381 LEU B C   
5781  O O   . LEU B 372 ? 0.9974 1.1806 0.8308 0.1102  0.0541  -0.6178 381 LEU B O   
5782  C CB  . LEU B 372 ? 1.1164 1.1508 0.8838 0.0888  0.0177  -0.6449 381 LEU B CB  
5783  C CG  . LEU B 372 ? 1.1888 1.1379 0.9228 0.0753  -0.0019 -0.6531 381 LEU B CG  
5784  C CD1 . LEU B 372 ? 1.2059 1.1588 0.9312 0.0510  -0.0061 -0.6568 381 LEU B CD1 
5785  C CD2 . LEU B 372 ? 1.2671 1.1602 0.9652 0.1082  -0.0180 -0.6792 381 LEU B CD2 
5786  N N   . CYS B 373 ? 0.9759 1.0942 0.8198 0.0709  0.0517  -0.5860 382 CYS B N   
5787  C CA  . CYS B 373 ? 0.9127 1.0944 0.7892 0.0625  0.0684  -0.5649 382 CYS B CA  
5788  C C   . CYS B 373 ? 0.8903 1.1061 0.7787 0.0877  0.0760  -0.5644 382 CYS B C   
5789  O O   . CYS B 373 ? 0.8459 1.1225 0.7567 0.0858  0.0888  -0.5523 382 CYS B O   
5790  C CB  . CYS B 373 ? 0.8851 1.0521 0.7770 0.0330  0.0720  -0.5394 382 CYS B CB  
5791  S SG  . CYS B 373 ? 0.8994 1.0861 0.7946 0.0031  0.0735  -0.5328 382 CYS B SG  
5792  N N   . ASN B 374 ? 0.9256 1.1034 0.7977 0.1114  0.0676  -0.5777 383 ASN B N   
5793  C CA  . ASN B 374 ? 0.9118 1.1250 0.7938 0.1373  0.0741  -0.5788 383 ASN B CA  
5794  C C   . ASN B 374 ? 0.9137 1.1853 0.7937 0.1591  0.0779  -0.5956 383 ASN B C   
5795  O O   . ASN B 374 ? 0.8862 1.2131 0.7817 0.1731  0.0873  -0.5912 383 ASN B O   
5796  C CB  . ASN B 374 ? 0.9557 1.1133 0.8181 0.1598  0.0630  -0.5905 383 ASN B CB  
5797  C CG  . ASN B 374 ? 0.9667 1.0666 0.8296 0.1401  0.0584  -0.5744 383 ASN B CG  
5798  O OD1 . ASN B 374 ? 0.9314 1.0492 0.8183 0.1190  0.0681  -0.5503 383 ASN B OD1 
5799  N ND2 . ASN B 374 ? 1.0394 1.0681 0.8740 0.1470  0.0428  -0.5876 383 ASN B ND2 
5800  N N   . VAL B 375 ? 0.9510 1.2100 0.8103 0.1615  0.0699  -0.6149 384 VAL B N   
5801  C CA  . VAL B 375 ? 0.9598 1.2697 0.8124 0.1832  0.0715  -0.6345 384 VAL B CA  
5802  C C   . VAL B 375 ? 0.9244 1.2913 0.7935 0.1619  0.0814  -0.6248 384 VAL B C   
5803  O O   . VAL B 375 ? 0.8968 1.3333 0.7779 0.1718  0.0906  -0.6254 384 VAL B O   
5804  C CB  . VAL B 375 ? 1.0273 1.2860 0.8425 0.2038  0.0549  -0.6649 384 VAL B CB  
5805  C CG1 . VAL B 375 ? 1.0391 1.3506 0.8470 0.2196  0.0565  -0.6842 384 VAL B CG1 
5806  C CG2 . VAL B 375 ? 1.0599 1.2767 0.8571 0.2345  0.0456  -0.6779 384 VAL B CG2 
5807  N N   . ASP B 376 ? 0.9264 1.2665 0.7962 0.1321  0.0794  -0.6149 385 ASP B N   
5808  C CA  . ASP B 376 ? 0.9093 1.2976 0.7887 0.1157  0.0862  -0.6106 385 ASP B CA  
5809  C C   . ASP B 376 ? 0.8573 1.2694 0.7620 0.0833  0.0965  -0.5821 385 ASP B C   
5810  O O   . ASP B 376 ? 0.8225 1.2969 0.7429 0.0783  0.1066  -0.5736 385 ASP B O   
5811  C CB  . ASP B 376 ? 0.9615 1.3198 0.8142 0.1161  0.0744  -0.6329 385 ASP B CB  
5812  C CG  . ASP B 376 ? 0.9768 1.3989 0.8297 0.1256  0.0793  -0.6451 385 ASP B CG  
5813  O OD1 . ASP B 376 ? 0.9470 1.4372 0.8234 0.1239  0.0926  -0.6314 385 ASP B OD1 
5814  O OD2 . ASP B 376 ? 1.0510 1.4548 0.8794 0.1339  0.0694  -0.6682 385 ASP B OD2 
5815  N N   . ILE B 377 ? 0.8543 1.2192 0.7614 0.0622  0.0935  -0.5675 386 ILE B N   
5816  C CA  . ILE B 377 ? 0.8099 1.1957 0.7389 0.0338  0.1024  -0.5411 386 ILE B CA  
5817  C C   . ILE B 377 ? 0.8219 1.2139 0.7454 0.0144  0.1002  -0.5434 386 ILE B C   
5818  O O   . ILE B 377 ? 0.8233 1.1837 0.7454 -0.0085 0.0963  -0.5339 386 ILE B O   
5819  C CB  . ILE B 377 ? 0.7560 1.2092 0.7086 0.0360  0.1161  -0.5254 386 ILE B CB  
5820  C CG1 . ILE B 377 ? 0.7306 1.1794 0.6931 0.0471  0.1197  -0.5157 386 ILE B CG1 
5821  C CG2 . ILE B 377 ? 0.7112 1.1905 0.6803 0.0098  0.1236  -0.5032 386 ILE B CG2 
5822  C CD1 . ILE B 377 ? 0.6881 1.2011 0.6637 0.0590  0.1290  -0.5113 386 ILE B CD1 
5823  N N   . PHE B 378 ? 0.8252 1.2636 0.7465 0.0237  0.1030  -0.5555 387 PHE B N   
5824  C CA  . PHE B 378 ? 0.8390 1.2855 0.7508 0.0116  0.0994  -0.5640 387 PHE B CA  
5825  C C   . PHE B 378 ? 0.8978 1.3029 0.7806 0.0281  0.0861  -0.5922 387 PHE B C   
5826  O O   . PHE B 378 ? 0.9158 1.3297 0.7892 0.0558  0.0843  -0.6095 387 PHE B O   
5827  C CB  . PHE B 378 ? 0.8074 1.3261 0.7310 0.0141  0.1092  -0.5620 387 PHE B CB  
5828  C CG  . PHE B 378 ? 0.7581 1.3173 0.7073 0.0045  0.1214  -0.5357 387 PHE B CG  
5829  C CD1 . PHE B 378 ? 0.7432 1.3467 0.7025 0.0207  0.1287  -0.5330 387 PHE B CD1 
5830  C CD2 . PHE B 378 ? 0.7212 1.2723 0.6827 -0.0204 0.1246  -0.5133 387 PHE B CD2 
5831  C CE1 . PHE B 378 ? 0.6876 1.3235 0.6677 0.0099  0.1384  -0.5078 387 PHE B CE1 
5832  C CE2 . PHE B 378 ? 0.6754 1.2579 0.6569 -0.0283 0.1343  -0.4895 387 PHE B CE2 
5833  C CZ  . PHE B 378 ? 0.6553 1.2775 0.6454 -0.0141 0.1408  -0.4864 387 PHE B CZ  
5834  N N   . ASN B 379 ? 0.9311 1.2887 0.7983 0.0106  0.0759  -0.5960 388 ASN B N   
5835  C CA  . ASN B 379 ? 0.9996 1.3058 0.8345 0.0206  0.0604  -0.6216 388 ASN B CA  
5836  C C   . ASN B 379 ? 1.0242 1.2878 0.8515 -0.0103 0.0525  -0.6132 388 ASN B C   
5837  O O   . ASN B 379 ? 0.9974 1.2486 0.8397 -0.0288 0.0561  -0.5910 388 ASN B O   
5838  C CB  . ASN B 379 ? 1.0279 1.2867 0.8477 0.0449  0.0524  -0.6331 388 ASN B CB  
5839  C CG  . ASN B 379 ? 1.0095 1.2339 0.8408 0.0322  0.0535  -0.6123 388 ASN B CG  
5840  O OD1 . ASN B 379 ? 1.0088 1.1792 0.8286 0.0122  0.0440  -0.6077 388 ASN B OD1 
5841  N ND2 . ASN B 379 ? 0.9791 1.2361 0.8326 0.0428  0.0648  -0.5991 388 ASN B ND2 
5842  N N   . PRO B 380 ? 1.0756 1.3195 0.8793 -0.0164 0.0416  -0.6305 389 PRO B N   
5843  C CA  . PRO B 380 ? 1.1141 1.3068 0.9016 -0.0447 0.0295  -0.6278 389 PRO B CA  
5844  C C   . PRO B 380 ? 1.1502 1.2746 0.9250 -0.0434 0.0196  -0.6258 389 PRO B C   
5845  O O   . PRO B 380 ? 1.1663 1.2783 0.9368 -0.0154 0.0191  -0.6350 389 PRO B O   
5846  C CB  . PRO B 380 ? 1.1724 1.3437 0.9278 -0.0368 0.0162  -0.6558 389 PRO B CB  
5847  C CG  . PRO B 380 ? 1.1790 1.3658 0.9275 0.0040  0.0177  -0.6765 389 PRO B CG  
5848  C CD  . PRO B 380 ? 1.1043 1.3633 0.8892 0.0083  0.0371  -0.6578 389 PRO B CD  
5849  N N   . LYS B 381 ? 1.1663 1.2485 0.9341 -0.0723 0.0114  -0.6142 390 LYS B N   
5850  C CA  . LYS B 381 ? 1.2012 1.2167 0.9551 -0.0725 0.0010  -0.6116 390 LYS B CA  
5851  C C   . LYS B 381 ? 1.1498 1.1817 0.9335 -0.0809 0.0129  -0.5844 390 LYS B C   
5852  O O   . LYS B 381 ? 1.1683 1.1601 0.9480 -0.1021 0.0064  -0.5713 390 LYS B O   
5853  C CB  . LYS B 381 ? 1.2442 1.2241 0.9754 -0.0361 -0.0075 -0.6353 390 LYS B CB  
5854  C CG  . LYS B 381 ? 1.3289 1.2562 1.0177 -0.0273 -0.0269 -0.6640 390 LYS B CG  
5855  C CD  . LYS B 381 ? 1.4212 1.2615 1.0799 -0.0470 -0.0466 -0.6634 390 LYS B CD  
5856  C CE  . LYS B 381 ? 1.5149 1.2844 1.1271 -0.0239 -0.0677 -0.6934 390 LYS B CE  
5857  N NZ  . LYS B 381 ? 1.5735 1.3347 1.1579 -0.0265 -0.0789 -0.7153 390 LYS B NZ  
5858  N N   . TYR B 382 ? 1.0913 1.1799 0.9028 -0.0647 0.0293  -0.5760 391 TYR B N   
5859  C CA  . TYR B 382 ? 1.0353 1.1427 0.8750 -0.0735 0.0409  -0.5497 391 TYR B CA  
5860  C C   . TYR B 382 ? 0.9708 1.1513 0.8418 -0.0735 0.0587  -0.5341 391 TYR B C   
5861  O O   . TYR B 382 ? 0.9526 1.1700 0.8329 -0.0513 0.0668  -0.5394 391 TYR B O   
5862  C CB  . TYR B 382 ? 1.0438 1.1147 0.8804 -0.0549 0.0384  -0.5501 391 TYR B CB  
5863  C CG  . TYR B 382 ? 1.0218 1.0716 0.8702 -0.0745 0.0398  -0.5269 391 TYR B CG  
5864  C CD1 . TYR B 382 ? 1.0557 1.0579 0.8881 -0.1001 0.0277  -0.5224 391 TYR B CD1 
5865  C CD2 . TYR B 382 ? 0.9721 1.0507 0.8468 -0.0686 0.0527  -0.5089 391 TYR B CD2 
5866  C CE1 . TYR B 382 ? 1.0377 1.0249 0.8808 -0.1182 0.0290  -0.5007 391 TYR B CE1 
5867  C CE2 . TYR B 382 ? 0.9478 1.0083 0.8327 -0.0855 0.0539  -0.4880 391 TYR B CE2 
5868  C CZ  . TYR B 382 ? 0.9817 0.9981 0.8510 -0.1098 0.0423  -0.4842 391 TYR B CZ  
5869  O OH  . TYR B 382 ? 0.9664 0.9686 0.8452 -0.1268 0.0433  -0.4636 391 TYR B OH  
5870  N N   . ASP B 383 ? 0.9404 1.1423 0.8264 -0.0990 0.0640  -0.5145 392 ASP B N   
5871  C CA  . ASP B 383 ? 0.8837 1.1408 0.7983 -0.0999 0.0795  -0.4948 392 ASP B CA  
5872  C C   . ASP B 383 ? 0.8612 1.1016 0.7875 -0.0935 0.0835  -0.4809 392 ASP B C   
5873  O O   . ASP B 383 ? 0.8837 1.0774 0.8026 -0.1020 0.0763  -0.4762 392 ASP B O   
5874  C CB  . ASP B 383 ? 0.8588 1.1493 0.7855 -0.1247 0.0845  -0.4785 392 ASP B CB  
5875  C CG  . ASP B 383 ? 0.9036 1.1646 0.8125 -0.1469 0.0728  -0.4837 392 ASP B CG  
5876  O OD1 . ASP B 383 ? 0.9448 1.1577 0.8433 -0.1583 0.0639  -0.4802 392 ASP B OD1 
5877  O OD2 . ASP B 383 ? 0.9055 1.1937 0.8106 -0.1544 0.0724  -0.4902 392 ASP B OD2 
5878  N N   . CYS B 384 ? 0.8136 1.0951 0.7581 -0.0799 0.0949  -0.4733 393 CYS B N   
5879  C CA  . CYS B 384 ? 0.8044 1.0735 0.7524 -0.0609 0.0968  -0.4734 393 CYS B CA  
5880  C C   . CYS B 384 ? 0.7458 1.0513 0.7183 -0.0640 0.1092  -0.4504 393 CYS B C   
5881  O O   . CYS B 384 ? 0.7146 1.0703 0.6987 -0.0636 0.1176  -0.4450 393 CYS B O   
5882  C CB  . CYS B 384 ? 0.8194 1.1068 0.7581 -0.0365 0.0959  -0.4950 393 CYS B CB  
5883  S SG  . CYS B 384 ? 0.8666 1.1345 0.8010 -0.0078 0.0942  -0.5043 393 CYS B SG  
5884  N N   . LYS B 385 ? 0.7313 1.0107 0.7104 -0.0678 0.1097  -0.4365 394 LYS B N   
5885  C CA  . LYS B 385 ? 0.6812 0.9887 0.6807 -0.0743 0.1198  -0.4133 394 LYS B CA  
5886  C C   . LYS B 385 ? 0.6477 0.9915 0.6577 -0.0575 0.1278  -0.4116 394 LYS B C   
5887  O O   . LYS B 385 ? 0.6572 0.9910 0.6624 -0.0394 0.1259  -0.4225 394 LYS B O   
5888  C CB  . LYS B 385 ? 0.6794 0.9522 0.6826 -0.0844 0.1180  -0.3983 394 LYS B CB  
5889  C CG  . LYS B 385 ? 0.7317 0.9749 0.7243 -0.1045 0.1098  -0.3982 394 LYS B CG  
5890  C CD  . LYS B 385 ? 0.7883 1.0087 0.7867 -0.1175 0.1093  -0.3802 394 LYS B CD  
5891  C CE  . LYS B 385 ? 0.8423 1.0143 0.8329 -0.1083 0.1031  -0.3839 394 LYS B CE  
5892  N NZ  . LYS B 385 ? 0.8194 0.9993 0.8239 -0.0944 0.1107  -0.3736 394 LYS B NZ  
5893  N N   . ILE B 386 ? 0.6062 0.9923 0.6290 -0.0644 0.1360  -0.3973 395 ILE B N   
5894  C CA  . ILE B 386 ? 0.5807 1.0122 0.6112 -0.0545 0.1429  -0.3953 395 ILE B CA  
5895  C C   . ILE B 386 ? 0.5456 1.0012 0.5890 -0.0659 0.1498  -0.3722 395 ILE B C   
5896  O O   . ILE B 386 ? 0.5400 0.9901 0.5851 -0.0802 0.1496  -0.3620 395 ILE B O   
5897  C CB  . ILE B 386 ? 0.5890 1.0529 0.6136 -0.0541 0.1427  -0.4083 395 ILE B CB  
5898  C CG1 . ILE B 386 ? 0.6319 1.0833 0.6423 -0.0369 0.1366  -0.4332 395 ILE B CG1 
5899  C CG2 . ILE B 386 ? 0.5559 1.0750 0.5901 -0.0536 0.1506  -0.3987 395 ILE B CG2 
5900  C CD1 . ILE B 386 ? 0.6644 1.1449 0.6674 -0.0366 0.1356  -0.4470 395 ILE B CD1 
5901  N N   . MET B 387 ? 0.5285 1.0127 0.5794 -0.0596 0.1552  -0.3638 396 MET B N   
5902  C CA  . MET B 387 ? 0.5060 1.0185 0.5641 -0.0702 0.1602  -0.3448 396 MET B CA  
5903  C C   . MET B 387 ? 0.4976 1.0594 0.5571 -0.0671 0.1641  -0.3449 396 MET B C   
5904  O O   . MET B 387 ? 0.5075 1.0873 0.5652 -0.0545 0.1644  -0.3573 396 MET B O   
5905  C CB  . MET B 387 ? 0.4927 0.9879 0.5573 -0.0731 0.1621  -0.3263 396 MET B CB  
5906  C CG  . MET B 387 ? 0.5055 1.0093 0.5738 -0.0631 0.1643  -0.3235 396 MET B CG  
5907  S SD  . MET B 387 ? 0.5512 1.0362 0.6252 -0.0694 0.1659  -0.3000 396 MET B SD  
5908  C CE  . MET B 387 ? 0.5504 0.9917 0.6232 -0.0771 0.1625  -0.2978 396 MET B CE  
5909  N N   . THR B 388 ? 0.4783 1.0631 0.5400 -0.0783 0.1667  -0.3305 397 THR B N   
5910  C CA  . THR B 388 ? 0.4707 1.1023 0.5315 -0.0796 0.1692  -0.3307 397 THR B CA  
5911  C C   . THR B 388 ? 0.4529 1.1066 0.5169 -0.0842 0.1721  -0.3114 397 THR B C   
5912  O O   . THR B 388 ? 0.4454 1.0811 0.5104 -0.0916 0.1719  -0.2940 397 THR B O   
5913  C CB  . THR B 388 ? 0.4689 1.1115 0.5266 -0.0898 0.1685  -0.3308 397 THR B CB  
5914  O OG1 . THR B 388 ? 0.4909 1.1263 0.5428 -0.0850 0.1654  -0.3522 397 THR B OG1 
5915  C CG2 . THR B 388 ? 0.4622 1.1514 0.5192 -0.0948 0.1712  -0.3233 397 THR B CG2 
5916  N N   . SER B 389 ? 0.4486 1.1420 0.5125 -0.0802 0.1740  -0.3143 398 SER B N   
5917  C CA  . SER B 389 ? 0.4352 1.1550 0.4990 -0.0890 0.1754  -0.2952 398 SER B CA  
5918  C C   . SER B 389 ? 0.4374 1.2085 0.4983 -0.0926 0.1768  -0.2971 398 SER B C   
5919  O O   . SER B 389 ? 0.4471 1.2449 0.5079 -0.0831 0.1778  -0.3142 398 SER B O   
5920  C CB  . SER B 389 ? 0.4283 1.1461 0.4953 -0.0851 0.1759  -0.2879 398 SER B CB  
5921  O OG  . SER B 389 ? 0.4220 1.1676 0.4861 -0.0961 0.1760  -0.2696 398 SER B OG  
5922  N N   . LYS B 390 ? 0.4307 1.2147 0.4879 -0.1057 0.1762  -0.2791 399 LYS B N   
5923  C CA  . LYS B 390 ? 0.4302 1.2636 0.4835 -0.1124 0.1769  -0.2753 399 LYS B CA  
5924  C C   . LYS B 390 ? 0.4232 1.2928 0.4774 -0.1124 0.1780  -0.2703 399 LYS B C   
5925  O O   . LYS B 390 ? 0.4228 1.3397 0.4766 -0.1107 0.1796  -0.2779 399 LYS B O   
5926  C CB  . LYS B 390 ? 0.4301 1.2593 0.4767 -0.1262 0.1746  -0.2558 399 LYS B CB  
5927  C CG  . LYS B 390 ? 0.4400 1.2682 0.4848 -0.1277 0.1744  -0.2631 399 LYS B CG  
5928  C CD  . LYS B 390 ? 0.4824 1.3633 0.5242 -0.1311 0.1756  -0.2680 399 LYS B CD  
5929  C CE  . LYS B 390 ? 0.5012 1.3900 0.5399 -0.1352 0.1750  -0.2723 399 LYS B CE  
5930  N NZ  . LYS B 390 ? 0.4892 1.4311 0.5248 -0.1386 0.1762  -0.2761 399 LYS B NZ  
5931  N N   . THR B 391 ? 0.4159 1.2649 0.4711 -0.1142 0.1769  -0.2580 400 THR B N   
5932  C CA  . THR B 391 ? 0.4140 1.2954 0.4688 -0.1188 0.1768  -0.2478 400 THR B CA  
5933  C C   . THR B 391 ? 0.4101 1.2910 0.4721 -0.1038 0.1788  -0.2608 400 THR B C   
5934  O O   . THR B 391 ? 0.4090 1.2485 0.4747 -0.0932 0.1789  -0.2707 400 THR B O   
5935  C CB  . THR B 391 ? 0.4147 1.2711 0.4627 -0.1334 0.1727  -0.2222 400 THR B CB  
5936  O OG1 . THR B 391 ? 0.4264 1.2469 0.4690 -0.1381 0.1703  -0.2152 400 THR B OG1 
5937  C CG2 . THR B 391 ? 0.4205 1.3199 0.4610 -0.1491 0.1703  -0.2050 400 THR B CG2 
5938  N N   . ASP B 392 ? 0.4048 1.3330 0.4681 -0.1031 0.1800  -0.2600 401 ASP B N   
5939  C CA  . ASP B 392 ? 0.4011 1.3352 0.4704 -0.0880 0.1816  -0.2708 401 ASP B CA  
5940  C C   . ASP B 392 ? 0.3928 1.2805 0.4638 -0.0901 0.1798  -0.2594 401 ASP B C   
5941  O O   . ASP B 392 ? 0.3912 1.2684 0.4576 -0.1065 0.1771  -0.2378 401 ASP B O   
5942  C CB  . ASP B 392 ? 0.4049 1.4037 0.4746 -0.0912 0.1828  -0.2660 401 ASP B CB  
5943  C CG  . ASP B 392 ? 0.4319 1.4832 0.5015 -0.0815 0.1854  -0.2836 401 ASP B CG  
5944  O OD1 . ASP B 392 ? 0.4739 1.5152 0.5406 -0.0811 0.1855  -0.2921 401 ASP B OD1 
5945  O OD2 . ASP B 392 ? 0.4468 1.5523 0.5187 -0.0739 0.1873  -0.2890 401 ASP B OD2 
5946  N N   . VAL B 393 ? 0.3905 1.2484 0.4663 -0.0733 0.1805  -0.2742 402 VAL B N   
5947  C CA  . VAL B 393 ? 0.3785 1.1948 0.4568 -0.0725 0.1791  -0.2660 402 VAL B CA  
5948  C C   . VAL B 393 ? 0.3778 1.2097 0.4610 -0.0545 0.1805  -0.2796 402 VAL B C   
5949  O O   . VAL B 393 ? 0.3907 1.2232 0.4744 -0.0371 0.1812  -0.3013 402 VAL B O   
5950  C CB  . VAL B 393 ? 0.3789 1.1358 0.4575 -0.0679 0.1780  -0.2720 402 VAL B CB  
5951  C CG1 . VAL B 393 ? 0.3897 1.1068 0.4713 -0.0645 0.1768  -0.2660 402 VAL B CG1 
5952  C CG2 . VAL B 393 ? 0.3806 1.1209 0.4542 -0.0830 0.1765  -0.2589 402 VAL B CG2 
5953  N N   . SER B 394 ? 0.3617 1.2042 0.4473 -0.0577 0.1802  -0.2677 403 SER B N   
5954  C CA  . SER B 394 ? 0.3582 1.2213 0.4484 -0.0392 0.1814  -0.2804 403 SER B CA  
5955  C C   . SER B 394 ? 0.3481 1.1613 0.4409 -0.0348 0.1800  -0.2767 403 SER B C   
5956  O O   . SER B 394 ? 0.3415 1.1301 0.4329 -0.0506 0.1783  -0.2577 403 SER B O   
5957  C CB  . SER B 394 ? 0.3537 1.2802 0.4447 -0.0473 0.1823  -0.2691 403 SER B CB  
5958  O OG  . SER B 394 ? 0.3604 1.3171 0.4465 -0.0670 0.1818  -0.2561 403 SER B OG  
5959  N N   . SER B 395 ? 0.3533 1.1487 0.4484 -0.0132 0.1799  -0.2946 404 SER B N   
5960  C CA  . SER B 395 ? 0.3539 1.1129 0.4521 -0.0080 0.1786  -0.2900 404 SER B CA  
5961  C C   . SER B 395 ? 0.3644 1.1149 0.4634 0.0185  0.1779  -0.3106 404 SER B C   
5962  O O   . SER B 395 ? 0.3756 1.1562 0.4719 0.0351  0.1783  -0.3292 404 SER B O   
5963  C CB  . SER B 395 ? 0.3478 1.0445 0.4449 -0.0196 0.1767  -0.2787 404 SER B CB  
5964  O OG  . SER B 395 ? 0.3680 1.0187 0.4645 -0.0056 0.1752  -0.2940 404 SER B OG  
5965  N N   . SER B 396 ? 0.3572 1.0659 0.4581 0.0234  0.1763  -0.3076 405 SER B N   
5966  C CA  . SER B 396 ? 0.3700 1.0657 0.4697 0.0485  0.1745  -0.3254 405 SER B CA  
5967  C C   . SER B 396 ? 0.3783 1.0041 0.4760 0.0520  0.1712  -0.3279 405 SER B C   
5968  O O   . SER B 396 ? 0.3715 0.9660 0.4717 0.0355  0.1712  -0.3117 405 SER B O   
5969  C CB  . SER B 396 ? 0.3632 1.0977 0.4677 0.0551  0.1757  -0.3199 405 SER B CB  
5970  O OG  . SER B 396 ? 0.3708 1.0745 0.4740 0.0761  0.1731  -0.3315 405 SER B OG  
5971  N N   . VAL B 397 ? 0.4011 1.0033 0.4927 0.0741  0.1677  -0.3483 406 VAL B N   
5972  C CA  . VAL B 397 ? 0.4196 0.9544 0.5066 0.0773  0.1633  -0.3527 406 VAL B CA  
5973  C C   . VAL B 397 ? 0.4404 0.9598 0.5226 0.1022  0.1594  -0.3666 406 VAL B C   
5974  O O   . VAL B 397 ? 0.4627 1.0004 0.5375 0.1231  0.1573  -0.3858 406 VAL B O   
5975  C CB  . VAL B 397 ? 0.4374 0.9452 0.5155 0.0770  0.1601  -0.3664 406 VAL B CB  
5976  C CG1 . VAL B 397 ? 0.4602 0.9008 0.5346 0.0705  0.1557  -0.3640 406 VAL B CG1 
5977  C CG2 . VAL B 397 ? 0.4308 0.9698 0.5118 0.0588  0.1638  -0.3586 406 VAL B CG2 
5978  N N   . ILE B 398 ? 0.4415 0.9250 0.5264 0.1015  0.1580  -0.3577 407 ILE B N   
5979  C CA  . ILE B 398 ? 0.4630 0.9335 0.5431 0.1257  0.1541  -0.3693 407 ILE B CA  
5980  C C   . ILE B 398 ? 0.5044 0.9115 0.5714 0.1371  0.1464  -0.3840 407 ILE B C   
5981  O O   . ILE B 398 ? 0.5100 0.8680 0.5763 0.1223  0.1443  -0.3756 407 ILE B O   
5982  C CB  . ILE B 398 ? 0.4425 0.9105 0.5311 0.1212  0.1558  -0.3529 407 ILE B CB  
5983  C CG1 . ILE B 398 ? 0.4136 0.9488 0.5117 0.1136  0.1616  -0.3410 407 ILE B CG1 
5984  C CG2 . ILE B 398 ? 0.4624 0.9050 0.5444 0.1463  0.1507  -0.3651 407 ILE B CG2 
5985  C CD1 . ILE B 398 ? 0.4200 0.9596 0.5260 0.1065  0.1632  -0.3235 407 ILE B CD1 
5986  N N   . THR B 399 ? 0.5403 0.9489 0.5955 0.1638  0.1414  -0.4055 408 THR B N   
5987  C CA  . THR B 399 ? 0.5864 0.9330 0.6243 0.1757  0.1320  -0.4215 408 THR B CA  
5988  C C   . THR B 399 ? 0.6122 0.9238 0.6442 0.1938  0.1264  -0.4245 408 THR B C   
5989  O O   . THR B 399 ? 0.5998 0.9383 0.6425 0.1978  0.1306  -0.4143 408 THR B O   
5990  C CB  . THR B 399 ? 0.6147 0.9744 0.6382 0.1950  0.1277  -0.4455 408 THR B CB  
5991  O OG1 . THR B 399 ? 0.6236 1.0379 0.6484 0.2191  0.1300  -0.4542 408 THR B OG1 
5992  C CG2 . THR B 399 ? 0.6010 0.9893 0.6289 0.1768  0.1323  -0.4430 408 THR B CG2 
5993  N N   . SER B 400 ? 0.6563 0.9066 0.6697 0.2037  0.1163  -0.4383 409 SER B N   
5994  C CA  . SER B 400 ? 0.6886 0.8939 0.6921 0.2204  0.1088  -0.4419 409 SER B CA  
5995  C C   . SER B 400 ? 0.6957 0.9426 0.6977 0.2518  0.1091  -0.4532 409 SER B C   
5996  O O   . SER B 400 ? 0.6963 0.9400 0.7020 0.2615  0.1089  -0.4472 409 SER B O   
5997  C CB  . SER B 400 ? 0.7417 0.8765 0.7201 0.2278  0.0957  -0.4583 409 SER B CB  
5998  O OG  . SER B 400 ? 0.7521 0.8505 0.7300 0.1990  0.0943  -0.4494 409 SER B OG  
5999  N N   . LEU B 401 ? 0.7015 0.9916 0.6983 0.2673  0.1099  -0.4693 410 LEU B N   
6000  C CA  . LEU B 401 ? 0.7260 1.0469 0.7137 0.3035  0.1070  -0.4869 410 LEU B CA  
6001  C C   . LEU B 401 ? 0.6977 1.1098 0.6982 0.3085  0.1163  -0.4875 410 LEU B C   
6002  O O   . LEU B 401 ? 0.7134 1.1659 0.7078 0.3393  0.1150  -0.5025 410 LEU B O   
6003  C CB  . LEU B 401 ? 0.7848 1.0550 0.7435 0.3272  0.0941  -0.5130 410 LEU B CB  
6004  C CG  . LEU B 401 ? 0.8289 1.0545 0.7684 0.3580  0.0832  -0.5255 410 LEU B CG  
6005  C CD1 . LEU B 401 ? 0.8367 1.0094 0.7816 0.3411  0.0814  -0.5069 410 LEU B CD1 
6006  C CD2 . LEU B 401 ? 0.8826 1.0528 0.7899 0.3779  0.0690  -0.5510 410 LEU B CD2 
6007  N N   . GLY B 402 ? 0.6552 1.1000 0.6727 0.2782  0.1252  -0.4707 411 GLY B N   
6008  C CA  . GLY B 402 ? 0.6146 1.1454 0.6463 0.2741  0.1344  -0.4645 411 GLY B CA  
6009  C C   . GLY B 402 ? 0.5682 1.1116 0.6156 0.2362  0.1419  -0.4424 411 GLY B C   
6010  O O   . GLY B 402 ? 0.5523 1.0556 0.6065 0.2146  0.1427  -0.4250 411 GLY B O   
6011  N N   . ALA B 403 ? 0.5455 1.1436 0.5969 0.2294  0.1468  -0.4434 412 ALA B N   
6012  C CA  . ALA B 403 ? 0.5048 1.1159 0.5678 0.1958  0.1528  -0.4241 412 ALA B CA  
6013  C C   . ALA B 403 ? 0.5031 1.1510 0.5626 0.1939  0.1546  -0.4338 412 ALA B C   
6014  O O   . ALA B 403 ? 0.5199 1.2038 0.5716 0.2177  0.1532  -0.4525 412 ALA B O   
6015  C CB  . ALA B 403 ? 0.4683 1.1264 0.5471 0.1803  0.1594  -0.4017 412 ALA B CB  
6016  N N   . ILE B 404 ? 0.4864 1.1244 0.5508 0.1665  0.1573  -0.4212 413 ILE B N   
6017  C CA  . ILE B 404 ? 0.4829 1.1580 0.5462 0.1592  0.1599  -0.4258 413 ILE B CA  
6018  C C   . ILE B 404 ? 0.4520 1.1773 0.5289 0.1343  0.1669  -0.4024 413 ILE B C   
6019  O O   . ILE B 404 ? 0.4308 1.1418 0.5161 0.1172  0.1687  -0.3821 413 ILE B O   
6020  C CB  . ILE B 404 ? 0.4882 1.1120 0.5445 0.1461  0.1566  -0.4295 413 ILE B CB  
6021  C CG1 . ILE B 404 ? 0.5259 1.0927 0.5651 0.1671  0.1478  -0.4518 413 ILE B CG1 
6022  C CG2 . ILE B 404 ? 0.4806 1.1475 0.5368 0.1373  0.1598  -0.4323 413 ILE B CG2 
6023  C CD1 . ILE B 404 ? 0.5499 1.0731 0.5794 0.1554  0.1434  -0.4586 413 ILE B CD1 
6024  N N   . VAL B 405 ? 0.4537 1.2371 0.5310 0.1324  0.1700  -0.4055 414 VAL B N   
6025  C CA  . VAL B 405 ? 0.4323 1.2645 0.5193 0.1079  0.1753  -0.3839 414 VAL B CA  
6026  C C   . VAL B 405 ? 0.4352 1.3014 0.5193 0.0997  0.1771  -0.3880 414 VAL B C   
6027  O O   . VAL B 405 ? 0.4520 1.3579 0.5306 0.1182  0.1770  -0.4065 414 VAL B O   
6028  C CB  . VAL B 405 ? 0.4212 1.3142 0.5149 0.1128  0.1780  -0.3759 414 VAL B CB  
6029  C CG1 . VAL B 405 ? 0.4484 1.3742 0.5363 0.1471  0.1765  -0.3997 414 VAL B CG1 
6030  C CG2 . VAL B 405 ? 0.4027 1.3576 0.5020 0.0890  0.1820  -0.3575 414 VAL B CG2 
6031  N N   . SER B 406 ? 0.4217 1.2708 0.5088 0.0730  0.1783  -0.3710 415 SER B N   
6032  C CA  . SER B 406 ? 0.4207 1.2977 0.5057 0.0611  0.1800  -0.3708 415 SER B CA  
6033  C C   . SER B 406 ? 0.4041 1.3351 0.4950 0.0397  0.1833  -0.3484 415 SER B C   
6034  O O   . SER B 406 ? 0.3921 1.3009 0.4856 0.0170  0.1832  -0.3270 415 SER B O   
6035  C CB  . SER B 406 ? 0.4172 1.2363 0.4997 0.0464  0.1782  -0.3667 415 SER B CB  
6036  O OG  . SER B 406 ? 0.4397 1.2029 0.5159 0.0618  0.1739  -0.3838 415 SER B OG  
6037  N N   . CYS B 407 ? 0.4097 1.4115 0.5010 0.0471  0.1855  -0.3534 416 CYS B N   
6038  C CA  . CYS B 407 ? 0.3985 1.4571 0.4936 0.0252  0.1877  -0.3319 416 CYS B CA  
6039  C C   . CYS B 407 ? 0.3947 1.4894 0.4864 0.0133  0.1890  -0.3309 416 CYS B C   
6040  O O   . CYS B 407 ? 0.4063 1.5437 0.4954 0.0290  0.1903  -0.3485 416 CYS B O   
6041  C CB  . CYS B 407 ? 0.4015 1.5243 0.5001 0.0372  0.1892  -0.3335 416 CYS B CB  
6042  S SG  . CYS B 407 ? 0.4067 1.5625 0.5096 0.0060  0.1892  -0.3002 416 CYS B SG  
6043  N N   . TYR B 408 ? 0.3834 1.4611 0.4740 -0.0136 0.1882  -0.3103 417 TYR B N   
6044  C CA  . TYR B 408 ? 0.3777 1.4788 0.4643 -0.0258 0.1888  -0.3084 417 TYR B CA  
6045  C C   . TYR B 408 ? 0.3670 1.4915 0.4514 -0.0561 0.1876  -0.2804 417 TYR B C   
6046  O O   . TYR B 408 ? 0.3633 1.4694 0.4478 -0.0703 0.1855  -0.2612 417 TYR B O   
6047  C CB  . TYR B 408 ? 0.3804 1.4193 0.4639 -0.0247 0.1874  -0.3165 417 TYR B CB  
6048  C CG  . TYR B 408 ? 0.3970 1.4184 0.4780 0.0016  0.1870  -0.3453 417 TYR B CG  
6049  C CD1 . TYR B 408 ? 0.4071 1.3590 0.4867 0.0092  0.1845  -0.3537 417 TYR B CD1 
6050  C CD2 . TYR B 408 ? 0.4176 1.4907 0.4957 0.0183  0.1883  -0.3640 417 TYR B CD2 
6051  C CE1 . TYR B 408 ? 0.4363 1.3658 0.5100 0.0312  0.1823  -0.3796 417 TYR B CE1 
6052  C CE2 . TYR B 408 ? 0.4447 1.4957 0.5167 0.0431  0.1863  -0.3914 417 TYR B CE2 
6053  C CZ  . TYR B 408 ? 0.4552 1.4320 0.5243 0.0485  0.1828  -0.3988 417 TYR B CZ  
6054  O OH  . TYR B 408 ? 0.4938 1.4430 0.5536 0.0708  0.1791  -0.4250 417 TYR B OH  
6055  N N   . GLY B 409 ? 0.3675 1.5306 0.4480 -0.0664 0.1882  -0.2780 418 GLY B N   
6056  C CA  . GLY B 409 ? 0.3657 1.5577 0.4412 -0.0952 0.1859  -0.2517 418 GLY B CA  
6057  C C   . GLY B 409 ? 0.3663 1.6077 0.4432 -0.1045 0.1852  -0.2371 418 GLY B C   
6058  O O   . GLY B 409 ? 0.3686 1.6651 0.4505 -0.0890 0.1881  -0.2491 418 GLY B O   
6059  N N   . LYS B 410 ? 0.3672 1.5884 0.4382 -0.1297 0.1806  -0.2111 419 LYS B N   
6060  C CA  . LYS B 410 ? 0.3725 1.6381 0.4422 -0.1451 0.1784  -0.1932 419 LYS B CA  
6061  C C   . LYS B 410 ? 0.3658 1.6154 0.4424 -0.1328 0.1790  -0.1963 419 LYS B C   
6062  O O   . LYS B 410 ? 0.3650 1.6541 0.4413 -0.1445 0.1772  -0.1825 419 LYS B O   
6063  C CB  . LYS B 410 ? 0.3828 1.6261 0.4396 -0.1785 0.1713  -0.1634 419 LYS B CB  
6064  C CG  . LYS B 410 ? 0.4082 1.7014 0.4563 -0.1991 0.1690  -0.1512 419 LYS B CG  
6065  C CD  . LYS B 410 ? 0.4577 1.7449 0.4909 -0.2332 0.1602  -0.1192 419 LYS B CD  
6066  C CE  . LYS B 410 ? 0.4842 1.8401 0.5091 -0.2556 0.1575  -0.1051 419 LYS B CE  
6067  N NZ  . LYS B 410 ? 0.5078 1.8608 0.5301 -0.2522 0.1592  -0.1131 419 LYS B NZ  
6068  N N   . THR B 411 ? 0.3606 1.5531 0.4425 -0.1112 0.1808  -0.2129 420 THR B N   
6069  C CA  . THR B 411 ? 0.3563 1.5211 0.4429 -0.1031 0.1803  -0.2120 420 THR B CA  
6070  C C   . THR B 411 ? 0.3597 1.5780 0.4542 -0.0809 0.1838  -0.2270 420 THR B C   
6071  O O   . THR B 411 ? 0.3690 1.6225 0.4662 -0.0602 0.1873  -0.2479 420 THR B O   
6072  C CB  . THR B 411 ? 0.3540 1.4348 0.4417 -0.0917 0.1800  -0.2204 420 THR B CB  
6073  O OG1 . THR B 411 ? 0.3486 1.4100 0.4346 -0.0859 0.1813  -0.2328 420 THR B OG1 
6074  C CG2 . THR B 411 ? 0.3450 1.3743 0.4258 -0.1143 0.1749  -0.1967 420 THR B CG2 
6075  N N   . LYS B 412 ? 0.3560 1.5812 0.4530 -0.0848 0.1823  -0.2163 421 LYS B N   
6076  C CA  . LYS B 412 ? 0.3627 1.6404 0.4670 -0.0635 0.1851  -0.2285 421 LYS B CA  
6077  C C   . LYS B 412 ? 0.3634 1.5892 0.4727 -0.0381 0.1858  -0.2436 421 LYS B C   
6078  O O   . LYS B 412 ? 0.3620 1.5279 0.4704 -0.0474 0.1832  -0.2325 421 LYS B O   
6079  C CB  . LYS B 412 ? 0.3631 1.6936 0.4667 -0.0855 0.1827  -0.2059 421 LYS B CB  
6080  C CG  . LYS B 412 ? 0.3926 1.8178 0.4957 -0.0933 0.1841  -0.2024 421 LYS B CG  
6081  C CD  . LYS B 412 ? 0.4292 1.8968 0.5285 -0.1241 0.1798  -0.1747 421 LYS B CD  
6082  C CE  . LYS B 412 ? 0.4367 1.9768 0.5304 -0.1464 0.1788  -0.1625 421 LYS B CE  
6083  N NZ  . LYS B 412 ? 0.4574 2.0264 0.5433 -0.1838 0.1723  -0.1314 421 LYS B NZ  
6084  N N   . CYS B 413 ? 0.3680 1.6171 0.4809 -0.0056 0.1887  -0.2686 422 CYS B N   
6085  C CA  . CYS B 413 ? 0.3724 1.5709 0.4878 0.0209  0.1884  -0.2848 422 CYS B CA  
6086  C C   . CYS B 413 ? 0.3753 1.6265 0.4947 0.0476  0.1898  -0.2978 422 CYS B C   
6087  O O   . CYS B 413 ? 0.3824 1.7058 0.5018 0.0584  0.1919  -0.3067 422 CYS B O   
6088  C CB  . CYS B 413 ? 0.3851 1.5268 0.4966 0.0381  0.1882  -0.3058 422 CYS B CB  
6089  S SG  . CYS B 413 ? 0.3962 1.4814 0.5032 0.0103  0.1868  -0.2928 422 CYS B SG  
6090  N N   . THR B 414 ? 0.3754 1.5892 0.4973 0.0599  0.1884  -0.2998 423 THR B N   
6091  C CA  . THR B 414 ? 0.3752 1.6377 0.5013 0.0773  0.1890  -0.3032 423 THR B CA  
6092  C C   . THR B 414 ? 0.3889 1.5928 0.5145 0.1048  0.1872  -0.3187 423 THR B C   
6093  O O   . THR B 414 ? 0.3904 1.5283 0.5167 0.0941  0.1852  -0.3089 423 THR B O   
6094  C CB  . THR B 414 ? 0.3570 1.6362 0.4870 0.0477  0.1878  -0.2748 423 THR B CB  
6095  O OG1 . THR B 414 ? 0.3444 1.6808 0.4729 0.0193  0.1881  -0.2573 423 THR B OG1 
6096  C CG2 . THR B 414 ? 0.3656 1.6864 0.5005 0.0644  0.1881  -0.2768 423 THR B CG2 
6097  N N   . ALA B 415 ? 0.4056 1.6337 0.5286 0.1407  0.1871  -0.3423 424 ALA B N   
6098  C CA  . ALA B 415 ? 0.4180 1.5971 0.5394 0.1660  0.1843  -0.3541 424 ALA B CA  
6099  C C   . ALA B 415 ? 0.4162 1.6549 0.5433 0.1755  0.1851  -0.3486 424 ALA B C   
6100  O O   . ALA B 415 ? 0.4250 1.7454 0.5528 0.1886  0.1871  -0.3552 424 ALA B O   
6101  C CB  . ALA B 415 ? 0.4453 1.5982 0.5564 0.2016  0.1817  -0.3844 424 ALA B CB  
6102  N N   . SER B 416 ? 0.4107 1.6137 0.5419 0.1687  0.1837  -0.3361 425 SER B N   
6103  C CA  . SER B 416 ? 0.4091 1.6674 0.5457 0.1786  0.1841  -0.3311 425 SER B CA  
6104  C C   . SER B 416 ? 0.4334 1.6446 0.5663 0.2122  0.1808  -0.3477 425 SER B C   
6105  O O   . SER B 416 ? 0.4381 1.5619 0.5662 0.2153  0.1779  -0.3534 425 SER B O   
6106  C CB  . SER B 416 ? 0.3848 1.6539 0.5283 0.1408  0.1844  -0.3006 425 SER B CB  
6107  O OG  . SER B 416 ? 0.3689 1.6400 0.5115 0.1068  0.1851  -0.2848 425 SER B OG  
6108  N N   . ASN B 417 ? 0.4492 1.7201 0.5837 0.2375  0.1810  -0.3551 426 ASN B N   
6109  C CA  . ASN B 417 ? 0.4821 1.7159 0.6110 0.2740  0.1771  -0.3724 426 ASN B CA  
6110  C C   . ASN B 417 ? 0.4866 1.6800 0.6214 0.2607  0.1758  -0.3552 426 ASN B C   
6111  O O   . ASN B 417 ? 0.4616 1.6511 0.6039 0.2232  0.1775  -0.3303 426 ASN B O   
6112  C CB  . ASN B 417 ? 0.4921 1.8046 0.6183 0.3119  0.1771  -0.3898 426 ASN B CB  
6113  C CG  . ASN B 417 ? 0.4744 1.8596 0.6113 0.3043  0.1794  -0.3725 426 ASN B CG  
6114  O OD1 . ASN B 417 ? 0.4425 1.7992 0.5863 0.2787  0.1793  -0.3517 426 ASN B OD1 
6115  N ND2 . ASN B 417 ? 0.4770 1.9594 0.6147 0.3265  0.1811  -0.3811 426 ASN B ND2 
6116  N N   . LYS B 418 ? 0.5286 1.6895 0.6581 0.2930  0.1719  -0.3694 427 LYS B N   
6117  C CA  . LYS B 418 ? 0.5424 1.6703 0.6764 0.2898  0.1702  -0.3574 427 LYS B CA  
6118  C C   . LYS B 418 ? 0.5134 1.6909 0.6597 0.2556  0.1735  -0.3291 427 LYS B C   
6119  O O   . LYS B 418 ? 0.4914 1.6188 0.6415 0.2287  0.1729  -0.3107 427 LYS B O   
6120  C CB  . LYS B 418 ? 0.5799 1.7233 0.7074 0.3350  0.1666  -0.3770 427 LYS B CB  
6121  C CG  . LYS B 418 ? 0.6382 1.6851 0.7539 0.3592  0.1600  -0.3917 427 LYS B CG  
6122  C CD  . LYS B 418 ? 0.6902 1.7585 0.8026 0.3957  0.1565  -0.4008 427 LYS B CD  
6123  C CE  . LYS B 418 ? 0.7350 1.7072 0.8351 0.4165  0.1489  -0.4113 427 LYS B CE  
6124  N NZ  . LYS B 418 ? 0.7309 1.6222 0.8353 0.3822  0.1488  -0.3940 427 LYS B NZ  
6125  N N   . ASN B 419 ? 0.5139 1.7910 0.6650 0.2580  0.1762  -0.3264 428 ASN B N   
6126  C CA  . ASN B 419 ? 0.4951 1.8347 0.6558 0.2267  0.1782  -0.3003 428 ASN B CA  
6127  C C   . ASN B 419 ? 0.4812 1.8454 0.6443 0.1838  0.1803  -0.2804 428 ASN B C   
6128  O O   . ASN B 419 ? 0.4706 1.8857 0.6388 0.1544  0.1805  -0.2577 428 ASN B O   
6129  C CB  . ASN B 419 ? 0.4950 1.9373 0.6595 0.2491  0.1795  -0.3052 428 ASN B CB  
6130  C CG  . ASN B 419 ? 0.5033 1.9647 0.6600 0.2974  0.1789  -0.3358 428 ASN B CG  
6131  O OD1 . ASN B 419 ? 0.4866 1.8948 0.6366 0.3304  0.1752  -0.3527 428 ASN B OD1 
6132  N ND2 . ASN B 419 ? 0.4925 2.0266 0.6482 0.3022  0.1816  -0.3433 428 ASN B ND2 
6133  N N   . ARG B 420 ? 0.4826 1.8111 0.6406 0.1799  0.1809  -0.2886 429 ARG B N   
6134  C CA  . ARG B 420 ? 0.4651 1.8078 0.6230 0.1419  0.1822  -0.2716 429 ARG B CA  
6135  C C   . ARG B 420 ? 0.4603 1.9007 0.6189 0.1426  0.1850  -0.2749 429 ARG B C   
6136  O O   . ARG B 420 ? 0.4591 1.9072 0.6158 0.1157  0.1857  -0.2648 429 ARG B O   
6137  C CB  . ARG B 420 ? 0.4496 1.7802 0.6101 0.1003  0.1803  -0.2413 429 ARG B CB  
6138  C CG  . ARG B 420 ? 0.4598 1.6950 0.6189 0.0952  0.1777  -0.2363 429 ARG B CG  
6139  C CD  . ARG B 420 ? 0.5004 1.6787 0.6547 0.0656  0.1766  -0.2246 429 ARG B CD  
6140  N NE  . ARG B 420 ? 0.5500 1.6336 0.7024 0.0663  0.1746  -0.2245 429 ARG B NE  
6141  C CZ  . ARG B 420 ? 0.5627 1.6122 0.7161 0.0559  0.1721  -0.2109 429 ARG B CZ  
6142  N NH1 . ARG B 420 ? 0.5501 1.6492 0.7062 0.0428  0.1709  -0.1955 429 ARG B NH1 
6143  N NH2 . ARG B 420 ? 0.5704 1.5359 0.7217 0.0580  0.1707  -0.2126 429 ARG B NH2 
6144  N N   . GLY B 421 ? 0.4602 1.9758 0.6207 0.1731  0.1864  -0.2885 430 GLY B N   
6145  C CA  . GLY B 421 ? 0.4506 2.0495 0.6099 0.1844  0.1892  -0.2994 430 GLY B CA  
6146  C C   . GLY B 421 ? 0.4494 1.9936 0.6018 0.1863  0.1894  -0.3128 430 GLY B C   
6147  O O   . GLY B 421 ? 0.4653 1.9303 0.6119 0.2085  0.1874  -0.3305 430 GLY B O   
6148  N N   . ILE B 422 ? 0.4291 2.0125 0.5813 0.1609  0.1913  -0.3031 431 ILE B N   
6149  C CA  . ILE B 422 ? 0.4236 1.9646 0.5696 0.1605  0.1917  -0.3143 431 ILE B CA  
6150  C C   . ILE B 422 ? 0.4406 2.0166 0.5809 0.2020  0.1927  -0.3447 431 ILE B C   
6151  O O   . ILE B 422 ? 0.4423 2.1140 0.5844 0.2112  0.1950  -0.3475 431 ILE B O   
6152  C CB  . ILE B 422 ? 0.4059 1.9853 0.5527 0.1192  0.1928  -0.2926 431 ILE B CB  
6153  C CG1 . ILE B 422 ? 0.3979 1.9213 0.5454 0.0786  0.1901  -0.2647 431 ILE B CG1 
6154  C CG2 . ILE B 422 ? 0.4014 1.9693 0.5425 0.1237  0.1941  -0.3065 431 ILE B CG2 
6155  C CD1 . ILE B 422 ? 0.4011 1.9879 0.5520 0.0491  0.1888  -0.2383 431 ILE B CD1 
6156  N N   . ILE B 423 ? 0.4598 1.9621 0.5918 0.2271  0.1905  -0.3672 432 ILE B N   
6157  C CA  . ILE B 423 ? 0.4927 2.0236 0.6157 0.2682  0.1900  -0.3977 432 ILE B CA  
6158  C C   . ILE B 423 ? 0.4949 2.0365 0.6130 0.2608  0.1915  -0.4050 432 ILE B C   
6159  O O   . ILE B 423 ? 0.5068 2.1276 0.6223 0.2773  0.1935  -0.4171 432 ILE B O   
6160  C CB  . ILE B 423 ? 0.5232 1.9771 0.6349 0.3085  0.1848  -0.4241 432 ILE B CB  
6161  C CG1 . ILE B 423 ? 0.5251 1.9184 0.6404 0.3054  0.1823  -0.4137 432 ILE B CG1 
6162  C CG2 . ILE B 423 ? 0.5630 2.0782 0.6653 0.3577  0.1834  -0.4524 432 ILE B CG2 
6163  C CD1 . ILE B 423 ? 0.5714 1.8751 0.6737 0.3374  0.1761  -0.4364 432 ILE B CD1 
6164  N N   . LYS B 424 ? 0.4894 1.9518 0.6054 0.2390  0.1904  -0.3994 433 LYS B N   
6165  C CA  . LYS B 424 ? 0.4976 1.9596 0.6081 0.2340  0.1912  -0.4080 433 LYS B CA  
6166  C C   . LYS B 424 ? 0.4658 1.9357 0.5834 0.1867  0.1936  -0.3791 433 LYS B C   
6167  O O   . LYS B 424 ? 0.4476 1.8965 0.5716 0.1608  0.1933  -0.3560 433 LYS B O   
6168  C CB  . LYS B 424 ? 0.5229 1.8890 0.6221 0.2524  0.1867  -0.4293 433 LYS B CB  
6169  C CG  . LYS B 424 ? 0.5575 1.9269 0.6484 0.2561  0.1867  -0.4447 433 LYS B CG  
6170  C CD  . LYS B 424 ? 0.6235 1.9224 0.6988 0.2876  0.1808  -0.4737 433 LYS B CD  
6171  C CE  . LYS B 424 ? 0.6509 1.9498 0.7189 0.2830  0.1809  -0.4847 433 LYS B CE  
6172  N NZ  . LYS B 424 ? 0.6980 2.0067 0.7489 0.3239  0.1766  -0.5184 433 LYS B NZ  
6173  N N   . THR B 425 ? 0.4615 1.9643 0.5767 0.1762  0.1955  -0.3804 434 THR B N   
6174  C CA  . THR B 425 ? 0.4409 1.9396 0.5593 0.1333  0.1965  -0.3550 434 THR B CA  
6175  C C   . THR B 425 ? 0.4483 1.9272 0.5600 0.1347  0.1967  -0.3683 434 THR B C   
6176  O O   . THR B 425 ? 0.4675 1.9843 0.5738 0.1621  0.1974  -0.3912 434 THR B O   
6177  C CB  . THR B 425 ? 0.4238 2.0140 0.5483 0.1081  0.1984  -0.3314 434 THR B CB  
6178  O OG1 . THR B 425 ? 0.4084 2.0022 0.5317 0.0707  0.1984  -0.3112 434 THR B OG1 
6179  C CG2 . THR B 425 ? 0.4415 2.1325 0.5664 0.1346  0.2010  -0.3466 434 THR B CG2 
6180  N N   . PHE B 426 ? 0.4409 1.8597 0.5518 0.1072  0.1957  -0.3549 435 PHE B N   
6181  C CA  . PHE B 426 ? 0.4609 1.8223 0.5647 0.1160  0.1944  -0.3722 435 PHE B CA  
6182  C C   . PHE B 426 ? 0.4698 1.8598 0.5703 0.1034  0.1959  -0.3728 435 PHE B C   
6183  O O   . PHE B 426 ? 0.4567 1.8479 0.5590 0.0701  0.1964  -0.3506 435 PHE B O   
6184  C CB  . PHE B 426 ? 0.4559 1.7178 0.5593 0.1053  0.1916  -0.3657 435 PHE B CB  
6185  C CG  . PHE B 426 ? 0.4638 1.6746 0.5646 0.1340  0.1888  -0.3827 435 PHE B CG  
6186  C CD1 . PHE B 426 ? 0.4423 1.6201 0.5482 0.1282  0.1877  -0.3694 435 PHE B CD1 
6187  C CD2 . PHE B 426 ? 0.4854 1.6814 0.5766 0.1673  0.1863  -0.4122 435 PHE B CD2 
6188  C CE1 . PHE B 426 ? 0.4406 1.5721 0.5433 0.1544  0.1846  -0.3842 435 PHE B CE1 
6189  C CE2 . PHE B 426 ? 0.4991 1.6445 0.5851 0.1934  0.1823  -0.4271 435 PHE B CE2 
6190  C CZ  . PHE B 426 ? 0.4717 1.5855 0.5640 0.1866  0.1817  -0.4126 435 PHE B CZ  
6191  N N   . SER B 427 ? 0.5013 1.9062 0.5946 0.1318  0.1957  -0.3997 436 SER B N   
6192  C CA  . SER B 427 ? 0.5140 1.9615 0.6038 0.1261  0.1974  -0.4045 436 SER B CA  
6193  C C   . SER B 427 ? 0.5138 1.8954 0.5999 0.1082  0.1960  -0.4018 436 SER B C   
6194  O O   . SER B 427 ? 0.5338 1.8856 0.6116 0.1262  0.1941  -0.4245 436 SER B O   
6195  C CB  . SER B 427 ? 0.5420 2.0306 0.6236 0.1654  0.1972  -0.4358 436 SER B CB  
6196  O OG  . SER B 427 ? 0.5508 2.1070 0.6307 0.1595  0.1998  -0.4374 436 SER B OG  
6197  N N   . ASN B 428 ? 0.4934 1.8511 0.5842 0.0735  0.1961  -0.3746 437 ASN B N   
6198  C CA  . ASN B 428 ? 0.4873 1.8017 0.5751 0.0526  0.1953  -0.3678 437 ASN B CA  
6199  C C   . ASN B 428 ? 0.4951 1.7474 0.5757 0.0706  0.1930  -0.3919 437 ASN B C   
6200  O O   . ASN B 428 ? 0.4927 1.7495 0.5688 0.0660  0.1931  -0.3979 437 ASN B O   
6201  C CB  . ASN B 428 ? 0.4836 1.8671 0.5708 0.0328  0.1974  -0.3562 437 ASN B CB  
6202  C CG  . ASN B 428 ? 0.4845 1.8295 0.5695 0.0038  0.1962  -0.3390 437 ASN B CG  
6203  O OD1 . ASN B 428 ? 0.4969 1.7946 0.5833 -0.0157 0.1942  -0.3195 437 ASN B OD1 
6204  N ND2 . ASN B 428 ? 0.5005 1.8672 0.5812 0.0021  0.1970  -0.3466 437 ASN B ND2 
6205  N N   . GLY B 429 ? 0.5025 1.6971 0.5810 0.0898  0.1902  -0.4047 438 GLY B N   
6206  C CA  . GLY B 429 ? 0.5155 1.6465 0.5850 0.1051  0.1863  -0.4262 438 GLY B CA  
6207  C C   . GLY B 429 ? 0.5174 1.5699 0.5869 0.1083  0.1829  -0.4251 438 GLY B C   
6208  O O   . GLY B 429 ? 0.5007 1.5261 0.5774 0.0866  0.1838  -0.4028 438 GLY B O   
6209  N N   . CYS B 430 ? 0.5382 1.5535 0.5982 0.1358  0.1784  -0.4491 439 CYS B N   
6210  C CA  . CYS B 430 ? 0.5367 1.4766 0.5948 0.1403  0.1742  -0.4497 439 CYS B CA  
6211  C C   . CYS B 430 ? 0.5602 1.4887 0.6086 0.1757  0.1696  -0.4728 439 CYS B C   
6212  O O   . CYS B 430 ? 0.5908 1.5038 0.6248 0.1972  0.1646  -0.4975 439 CYS B O   
6213  C CB  . CYS B 430 ? 0.5430 1.4172 0.5957 0.1269  0.1709  -0.4513 439 CYS B CB  
6214  S SG  . CYS B 430 ? 0.5909 1.3752 0.6292 0.1448  0.1620  -0.4714 439 CYS B SG  
6215  N N   . ASP B 431 ? 0.5447 1.4797 0.5994 0.1822  0.1704  -0.4647 440 ASP B N   
6216  C CA  . ASP B 431 ? 0.5682 1.4999 0.6139 0.2173  0.1661  -0.4847 440 ASP B CA  
6217  C C   . ASP B 431 ? 0.5629 1.4227 0.6072 0.2208  0.1617  -0.4816 440 ASP B C   
6218  O O   . ASP B 431 ? 0.5443 1.3649 0.5966 0.1953  0.1630  -0.4622 440 ASP B O   
6219  C CB  . ASP B 431 ? 0.5655 1.5825 0.6191 0.2273  0.1709  -0.4803 440 ASP B CB  
6220  C CG  . ASP B 431 ? 0.6182 1.6940 0.6619 0.2564  0.1701  -0.5044 440 ASP B CG  
6221  O OD1 . ASP B 431 ? 0.6752 1.7360 0.7053 0.2919  0.1645  -0.5281 440 ASP B OD1 
6222  O OD2 . ASP B 431 ? 0.6353 1.7735 0.6834 0.2444  0.1748  -0.4995 440 ASP B OD2 
6223  N N   . TYR B 432 ? 0.5777 1.4224 0.6107 0.2536  0.1562  -0.5009 441 TYR B N   
6224  C CA  . TYR B 432 ? 0.5782 1.3593 0.6080 0.2613  0.1512  -0.4996 441 TYR B CA  
6225  C C   . TYR B 432 ? 0.5736 1.3979 0.6067 0.2847  0.1522  -0.5014 441 TYR B C   
6226  O O   . TYR B 432 ? 0.5845 1.4728 0.6147 0.3056  0.1536  -0.5136 441 TYR B O   
6227  C CB  . TYR B 432 ? 0.6216 1.3319 0.6295 0.2811  0.1409  -0.5235 441 TYR B CB  
6228  C CG  . TYR B 432 ? 0.6391 1.2810 0.6389 0.2931  0.1338  -0.5260 441 TYR B CG  
6229  C CD1 . TYR B 432 ? 0.6367 1.2112 0.6391 0.2693  0.1318  -0.5120 441 TYR B CD1 
6230  C CD2 . TYR B 432 ? 0.6661 1.3112 0.6543 0.3292  0.1284  -0.5427 441 TYR B CD2 
6231  C CE1 . TYR B 432 ? 0.6531 1.1647 0.6475 0.2786  0.1248  -0.5134 441 TYR B CE1 
6232  C CE2 . TYR B 432 ? 0.6947 1.2734 0.6740 0.3397  0.1210  -0.5444 441 TYR B CE2 
6233  C CZ  . TYR B 432 ? 0.6811 1.1927 0.6636 0.3131  0.1193  -0.5293 441 TYR B CZ  
6234  O OH  . TYR B 432 ? 0.6911 1.1377 0.6647 0.3210  0.1119  -0.5295 441 TYR B OH  
6235  N N   . VAL B 433 ? 0.5650 1.3574 0.6037 0.2822  0.1514  -0.4895 442 VAL B N   
6236  C CA  . VAL B 433 ? 0.5708 1.4000 0.6114 0.3062  0.1516  -0.4920 442 VAL B CA  
6237  C C   . VAL B 433 ? 0.5955 1.3497 0.6284 0.3182  0.1447  -0.4950 442 VAL B C   
6238  O O   . VAL B 433 ? 0.6055 1.2879 0.6347 0.3020  0.1412  -0.4906 442 VAL B O   
6239  C CB  . VAL B 433 ? 0.5274 1.4206 0.5882 0.2838  0.1599  -0.4663 442 VAL B CB  
6240  C CG1 . VAL B 433 ? 0.5190 1.4972 0.5853 0.2773  0.1657  -0.4647 442 VAL B CG1 
6241  C CG2 . VAL B 433 ? 0.4954 1.3460 0.5669 0.2468  0.1624  -0.4413 442 VAL B CG2 
6242  N N   . SER B 434 ? 0.6120 1.3825 0.6421 0.3456  0.1424  -0.5017 443 SER B N   
6243  C CA  . SER B 434 ? 0.6387 1.3344 0.6607 0.3554  0.1353  -0.5031 443 SER B CA  
6244  C C   . SER B 434 ? 0.6329 1.3531 0.6658 0.3613  0.1378  -0.4905 443 SER B C   
6245  O O   . SER B 434 ? 0.6178 1.4182 0.6623 0.3627  0.1441  -0.4838 443 SER B O   
6246  C CB  . SER B 434 ? 0.6914 1.3379 0.6869 0.3904  0.1239  -0.5323 443 SER B CB  
6247  O OG  . SER B 434 ? 0.7083 1.3748 0.6956 0.4272  0.1200  -0.5450 443 SER B OG  
6248  N N   . ASN B 435 ? 0.6537 1.3071 0.6826 0.3630  0.1326  -0.4865 444 ASN B N   
6249  C CA  . ASN B 435 ? 0.6557 1.3261 0.6934 0.3698  0.1340  -0.4754 444 ASN B CA  
6250  C C   . ASN B 435 ? 0.6947 1.4082 0.7227 0.4126  0.1305  -0.4946 444 ASN B C   
6251  O O   . ASN B 435 ? 0.7312 1.4255 0.7385 0.4436  0.1229  -0.5199 444 ASN B O   
6252  C CB  . ASN B 435 ? 0.6643 1.2500 0.6979 0.3632  0.1285  -0.4684 444 ASN B CB  
6253  C CG  . ASN B 435 ? 0.6787 1.2003 0.7078 0.3393  0.1262  -0.4655 444 ASN B CG  
6254  O OD1 . ASN B 435 ? 0.6892 1.2349 0.7246 0.3189  0.1312  -0.4611 444 ASN B OD1 
6255  N ND2 . ASN B 435 ? 0.7117 1.1526 0.7290 0.3411  0.1182  -0.4679 444 ASN B ND2 
6256  N N   . LYS B 436 ? 0.6918 1.4598 0.7331 0.4147  0.1352  -0.4823 445 LYS B N   
6257  C CA  . LYS B 436 ? 0.7135 1.5702 0.7554 0.4432  0.1374  -0.4926 445 LYS B CA  
6258  C C   . LYS B 436 ? 0.7075 1.6177 0.7490 0.4404  0.1412  -0.5008 445 LYS B C   
6259  O O   . LYS B 436 ? 0.7292 1.5962 0.7582 0.4414  0.1373  -0.5141 445 LYS B O   
6260  C CB  . LYS B 436 ? 0.7696 1.6123 0.7923 0.4924  0.1285  -0.5163 445 LYS B CB  
6261  C CG  . LYS B 436 ? 0.8053 1.7524 0.8292 0.5263  0.1310  -0.5269 445 LYS B CG  
6262  C CD  . LYS B 436 ? 0.7999 1.8435 0.8487 0.5062  0.1411  -0.5029 445 LYS B CD  
6263  C CE  . LYS B 436 ? 0.7689 1.7937 0.8383 0.4558  0.1473  -0.4699 445 LYS B CE  
6264  N NZ  . LYS B 436 ? 0.7734 1.7037 0.8409 0.4459  0.1428  -0.4612 445 LYS B NZ  
6265  N N   . GLY B 437 ? 0.6857 1.6932 0.7404 0.4367  0.1484  -0.4926 446 GLY B N   
6266  C CA  . GLY B 437 ? 0.6582 1.7205 0.7204 0.4150  0.1547  -0.4870 446 GLY B CA  
6267  C C   . GLY B 437 ? 0.6084 1.6575 0.6882 0.3681  0.1602  -0.4559 446 GLY B C   
6268  O O   . GLY B 437 ? 0.5898 1.6879 0.6829 0.3552  0.1643  -0.4374 446 GLY B O   
6269  N N   . VAL B 438 ? 0.5899 1.5686 0.6679 0.3443  0.1591  -0.4508 447 VAL B N   
6270  C CA  . VAL B 438 ? 0.5415 1.5177 0.6337 0.2999  0.1644  -0.4236 447 VAL B CA  
6271  C C   . VAL B 438 ? 0.5238 1.4339 0.6209 0.2823  0.1631  -0.4070 447 VAL B C   
6272  O O   . VAL B 438 ? 0.5444 1.3798 0.6324 0.2947  0.1574  -0.4163 447 VAL B O   
6273  C CB  . VAL B 438 ? 0.5366 1.4941 0.6262 0.2806  0.1656  -0.4247 447 VAL B CB  
6274  C CG1 . VAL B 438 ? 0.5027 1.4860 0.6055 0.2393  0.1713  -0.3975 447 VAL B CG1 
6275  C CG2 . VAL B 438 ? 0.5589 1.5703 0.6401 0.3034  0.1656  -0.4458 447 VAL B CG2 
6276  N N   . ASP B 439 ? 0.4845 1.4241 0.5949 0.2518  0.1677  -0.3818 448 ASP B N   
6277  C CA  . ASP B 439 ? 0.4680 1.3607 0.5844 0.2333  0.1672  -0.3633 448 ASP B CA  
6278  C C   . ASP B 439 ? 0.4327 1.3060 0.5553 0.1924  0.1701  -0.3412 448 ASP B C   
6279  O O   . ASP B 439 ? 0.4196 1.2326 0.5438 0.1761  0.1688  -0.3290 448 ASP B O   
6280  C CB  . ASP B 439 ? 0.4629 1.4144 0.5873 0.2370  0.1689  -0.3533 448 ASP B CB  
6281  C CG  . ASP B 439 ? 0.5031 1.4042 0.6283 0.2428  0.1659  -0.3481 448 ASP B CG  
6282  O OD1 . ASP B 439 ? 0.5256 1.3567 0.6513 0.2235  0.1647  -0.3374 448 ASP B OD1 
6283  O OD2 . ASP B 439 ? 0.5521 1.4878 0.6773 0.2676  0.1648  -0.3548 448 ASP B OD2 
6284  N N   . THR B 440 ? 0.4133 1.3390 0.5381 0.1777  0.1734  -0.3367 449 THR B N   
6285  C CA  . THR B 440 ? 0.3786 1.3020 0.5076 0.1404  0.1756  -0.3149 449 THR B CA  
6286  C C   . THR B 440 ? 0.3742 1.3306 0.5003 0.1349  0.1776  -0.3210 449 THR B C   
6287  O O   . THR B 440 ? 0.3850 1.4048 0.5102 0.1513  0.1790  -0.3330 449 THR B O   
6288  C CB  . THR B 440 ? 0.3617 1.3417 0.4979 0.1217  0.1773  -0.2936 449 THR B CB  
6289  O OG1 . THR B 440 ? 0.3418 1.2720 0.4804 0.1092  0.1755  -0.2789 449 THR B OG1 
6290  C CG2 . THR B 440 ? 0.3527 1.3792 0.4899 0.0907  0.1793  -0.2769 449 THR B CG2 
6291  N N   . VAL B 441 ? 0.3589 1.2754 0.4833 0.1131  0.1776  -0.3135 450 VAL B N   
6292  C CA  . VAL B 441 ? 0.3481 1.3047 0.4711 0.0995  0.1799  -0.3118 450 VAL B CA  
6293  C C   . VAL B 441 ? 0.3292 1.2758 0.4540 0.0631  0.1801  -0.2858 450 VAL B C   
6294  O O   . VAL B 441 ? 0.3272 1.2160 0.4521 0.0516  0.1783  -0.2749 450 VAL B O   
6295  C CB  . VAL B 441 ? 0.3569 1.2819 0.4729 0.1112  0.1790  -0.3313 450 VAL B CB  
6296  C CG1 . VAL B 441 ? 0.3769 1.2869 0.4867 0.1476  0.1762  -0.3573 450 VAL B CG1 
6297  C CG2 . VAL B 441 ? 0.3593 1.2112 0.4736 0.0944  0.1774  -0.3238 450 VAL B CG2 
6298  N N   . SER B 442 ? 0.3210 1.3241 0.4458 0.0452  0.1816  -0.2755 451 SER B N   
6299  C CA  . SER B 442 ? 0.3115 1.3045 0.4343 0.0111  0.1803  -0.2509 451 SER B CA  
6300  C C   . SER B 442 ? 0.3087 1.3144 0.4275 0.0017  0.1813  -0.2530 451 SER B C   
6301  O O   . SER B 442 ? 0.3168 1.3748 0.4358 0.0138  0.1834  -0.2658 451 SER B O   
6302  C CB  . SER B 442 ? 0.3078 1.3572 0.4321 -0.0074 0.1794  -0.2311 451 SER B CB  
6303  O OG  . SER B 442 ? 0.3483 1.4675 0.4773 0.0122  0.1816  -0.2418 451 SER B OG  
6304  N N   . VAL B 443 ? 0.3060 1.2617 0.4204 -0.0176 0.1795  -0.2417 452 VAL B N   
6305  C CA  . VAL B 443 ? 0.2988 1.2602 0.4084 -0.0307 0.1798  -0.2397 452 VAL B CA  
6306  C C   . VAL B 443 ? 0.2924 1.2517 0.3961 -0.0626 0.1764  -0.2126 452 VAL B C   
6307  O O   . VAL B 443 ? 0.2905 1.1973 0.3913 -0.0728 0.1735  -0.2005 452 VAL B O   
6308  C CB  . VAL B 443 ? 0.2980 1.1951 0.4055 -0.0240 0.1796  -0.2506 452 VAL B CB  
6309  C CG1 . VAL B 443 ? 0.2921 1.2019 0.3950 -0.0361 0.1800  -0.2492 452 VAL B CG1 
6310  C CG2 . VAL B 443 ? 0.3091 1.1917 0.4189 0.0063  0.1807  -0.2763 452 VAL B CG2 
6311  N N   . GLY B 444 ? 0.2936 1.3111 0.3939 -0.0785 0.1760  -0.2029 453 GLY B N   
6312  C CA  . GLY B 444 ? 0.2916 1.3104 0.3830 -0.1100 0.1710  -0.1761 453 GLY B CA  
6313  C C   . GLY B 444 ? 0.2877 1.2861 0.3794 -0.1149 0.1682  -0.1644 453 GLY B C   
6314  O O   . GLY B 444 ? 0.2869 1.3241 0.3856 -0.1039 0.1700  -0.1692 453 GLY B O   
6315  N N   . ASN B 445 ? 0.2855 1.2231 0.3693 -0.1293 0.1636  -0.1502 454 ASN B N   
6316  C CA  . ASN B 445 ? 0.2908 1.2048 0.3728 -0.1361 0.1601  -0.1379 454 ASN B CA  
6317  C C   . ASN B 445 ? 0.2803 1.1395 0.3693 -0.1157 0.1621  -0.1493 454 ASN B C   
6318  O O   . ASN B 445 ? 0.2832 1.1241 0.3718 -0.1188 0.1597  -0.1408 454 ASN B O   
6319  C CB  . ASN B 445 ? 0.3051 1.1917 0.3708 -0.1660 0.1522  -0.1129 454 ASN B CB  
6320  C CG  . ASN B 445 ? 0.3382 1.2844 0.3968 -0.1900 0.1479  -0.0954 454 ASN B CG  
6321  O OD1 . ASN B 445 ? 0.3800 1.3299 0.4345 -0.2026 0.1434  -0.0816 454 ASN B OD1 
6322  N ND2 . ASN B 445 ? 0.3537 1.3521 0.4111 -0.1965 0.1491  -0.0961 454 ASN B ND2 
6323  N N   . THR B 446 ? 0.2702 1.1052 0.3648 -0.0955 0.1662  -0.1685 455 THR B N   
6324  C CA  . THR B 446 ? 0.2622 1.0432 0.3621 -0.0774 0.1674  -0.1793 455 THR B CA  
6325  C C   . THR B 446 ? 0.2554 1.0658 0.3647 -0.0530 0.1709  -0.1968 455 THR B C   
6326  O O   . THR B 446 ? 0.2566 1.1101 0.3687 -0.0418 0.1736  -0.2100 455 THR B O   
6327  C CB  . THR B 446 ? 0.2665 1.0042 0.3656 -0.0702 0.1688  -0.1905 455 THR B CB  
6328  O OG1 . THR B 446 ? 0.2674 0.9870 0.3565 -0.0912 0.1656  -0.1750 455 THR B OG1 
6329  C CG2 . THR B 446 ? 0.2695 0.9485 0.3722 -0.0559 0.1691  -0.1984 455 THR B CG2 
6330  N N   . LEU B 447 ? 0.2529 1.0387 0.3661 -0.0433 0.1704  -0.1976 456 LEU B N   
6331  C CA  . LEU B 447 ? 0.2607 1.0720 0.3810 -0.0184 0.1727  -0.2136 456 LEU B CA  
6332  C C   . LEU B 447 ? 0.2707 1.0248 0.3929 0.0029  0.1730  -0.2300 456 LEU B C   
6333  O O   . LEU B 447 ? 0.2757 0.9745 0.3967 -0.0026 0.1712  -0.2228 456 LEU B O   
6334  C CB  . LEU B 447 ? 0.2601 1.0936 0.3827 -0.0240 0.1711  -0.2008 456 LEU B CB  
6335  C CG  . LEU B 447 ? 0.2628 1.1295 0.3923 0.0023  0.1729  -0.2153 456 LEU B CG  
6336  C CD1 . LEU B 447 ? 0.2867 1.2309 0.4178 0.0092  0.1754  -0.2236 456 LEU B CD1 
6337  C CD2 . LEU B 447 ? 0.2531 1.1260 0.3846 -0.0044 0.1710  -0.2016 456 LEU B CD2 
6338  N N   . TYR B 448 ? 0.2834 1.0500 0.4071 0.0274  0.1745  -0.2519 457 TYR B N   
6339  C CA  . TYR B 448 ? 0.3018 1.0121 0.4246 0.0470  0.1733  -0.2674 457 TYR B CA  
6340  C C   . TYR B 448 ? 0.3118 1.0346 0.4368 0.0726  0.1726  -0.2794 457 TYR B C   
6341  O O   . TYR B 448 ? 0.3204 1.1030 0.4468 0.0845  0.1740  -0.2865 457 TYR B O   
6342  C CB  . TYR B 448 ? 0.3158 1.0149 0.4341 0.0554  0.1735  -0.2845 457 TYR B CB  
6343  C CG  . TYR B 448 ? 0.3236 1.0049 0.4394 0.0326  0.1739  -0.2740 457 TYR B CG  
6344  C CD1 . TYR B 448 ? 0.3318 1.0561 0.4471 0.0122  0.1751  -0.2597 457 TYR B CD1 
6345  C CD2 . TYR B 448 ? 0.3361 0.9590 0.4488 0.0313  0.1723  -0.2781 457 TYR B CD2 
6346  C CE1 . TYR B 448 ? 0.3327 1.0384 0.4439 -0.0068 0.1748  -0.2502 457 TYR B CE1 
6347  C CE2 . TYR B 448 ? 0.3373 0.9462 0.4474 0.0122  0.1726  -0.2687 457 TYR B CE2 
6348  C CZ  . TYR B 448 ? 0.3355 0.9847 0.4447 -0.0055 0.1738  -0.2553 457 TYR B CZ  
6349  O OH  . TYR B 448 ? 0.3339 0.9671 0.4390 -0.0218 0.1734  -0.2467 457 TYR B OH  
6350  N N   . TYR B 449 ? 0.3146 0.9835 0.4392 0.0816  0.1703  -0.2816 458 TYR B N   
6351  C CA  . TYR B 449 ? 0.3232 0.9970 0.4484 0.1072  0.1687  -0.2927 458 TYR B CA  
6352  C C   . TYR B 449 ? 0.3463 0.9830 0.4639 0.1337  0.1654  -0.3161 458 TYR B C   
6353  O O   . TYR B 449 ? 0.3599 0.9325 0.4739 0.1327  0.1625  -0.3172 458 TYR B O   
6354  C CB  . TYR B 449 ? 0.3137 0.9531 0.4421 0.1008  0.1674  -0.2789 458 TYR B CB  
6355  C CG  . TYR B 449 ? 0.2927 0.9646 0.4258 0.0773  0.1689  -0.2568 458 TYR B CG  
6356  C CD1 . TYR B 449 ? 0.2863 0.9325 0.4179 0.0508  0.1687  -0.2401 458 TYR B CD1 
6357  C CD2 . TYR B 449 ? 0.2955 1.0236 0.4327 0.0815  0.1696  -0.2524 458 TYR B CD2 
6358  C CE1 . TYR B 449 ? 0.2932 0.9619 0.4252 0.0282  0.1683  -0.2195 458 TYR B CE1 
6359  C CE2 . TYR B 449 ? 0.2952 1.0511 0.4344 0.0564  0.1696  -0.2307 458 TYR B CE2 
6360  C CZ  . TYR B 449 ? 0.2959 1.0177 0.4313 0.0294  0.1684  -0.2143 458 TYR B CZ  
6361  O OH  . TYR B 449 ? 0.2917 1.0291 0.4247 0.0029  0.1665  -0.1924 458 TYR B OH  
6362  N N   . VAL B 450 ? 0.3559 1.0315 0.4694 0.1577  0.1649  -0.3344 459 VAL B N   
6363  C CA  . VAL B 450 ? 0.3854 1.0218 0.4877 0.1829  0.1600  -0.3575 459 VAL B CA  
6364  C C   . VAL B 450 ? 0.4100 1.0018 0.5076 0.2022  0.1551  -0.3632 459 VAL B C   
6365  O O   . VAL B 450 ? 0.4376 0.9724 0.5241 0.2144  0.1494  -0.3765 459 VAL B O   
6366  C CB  . VAL B 450 ? 0.4003 1.0891 0.4969 0.2059  0.1600  -0.3769 459 VAL B CB  
6367  C CG1 . VAL B 450 ? 0.4399 1.0794 0.5208 0.2291  0.1534  -0.4012 459 VAL B CG1 
6368  C CG2 . VAL B 450 ? 0.3781 1.1169 0.4796 0.1858  0.1650  -0.3697 459 VAL B CG2 
6369  N N   . ASN B 451 ? 0.4062 1.0241 0.5112 0.2044  0.1566  -0.3528 460 ASN B N   
6370  C CA  . ASN B 451 ? 0.4287 1.0046 0.5303 0.2204  0.1522  -0.3551 460 ASN B CA  
6371  C C   . ASN B 451 ? 0.4105 0.9685 0.5218 0.1972  0.1543  -0.3319 460 ASN B C   
6372  O O   . ASN B 451 ? 0.3839 0.9730 0.5039 0.1722  0.1589  -0.3145 460 ASN B O   
6373  C CB  . ASN B 451 ? 0.4455 1.0670 0.5443 0.2522  0.1507  -0.3683 460 ASN B CB  
6374  C CG  . ASN B 451 ? 0.4941 1.1107 0.5779 0.2822  0.1458  -0.3950 460 ASN B CG  
6375  O OD1 . ASN B 451 ? 0.5432 1.0919 0.6144 0.2889  0.1396  -0.4059 460 ASN B OD1 
6376  N ND2 . ASN B 451 ? 0.5102 1.1989 0.5938 0.2996  0.1480  -0.4057 460 ASN B ND2 
6377  N N   . LYS B 452 ? 0.4313 0.9363 0.5395 0.2045  0.1502  -0.3312 461 LYS B N   
6378  C CA  . LYS B 452 ? 0.4215 0.9092 0.5381 0.1830  0.1521  -0.3097 461 LYS B CA  
6379  C C   . LYS B 452 ? 0.4159 0.9603 0.5399 0.1884  0.1543  -0.3024 461 LYS B C   
6380  O O   . LYS B 452 ? 0.4332 1.0035 0.5540 0.2157  0.1524  -0.3157 461 LYS B O   
6381  C CB  . LYS B 452 ? 0.4384 0.8542 0.5496 0.1876  0.1471  -0.3101 461 LYS B CB  
6382  C CG  . LYS B 452 ? 0.4715 0.8328 0.5729 0.1862  0.1433  -0.3200 461 LYS B CG  
6383  C CD  . LYS B 452 ? 0.5023 0.7977 0.6005 0.1806  0.1393  -0.3133 461 LYS B CD  
6384  C CE  . LYS B 452 ? 0.5534 0.7944 0.6398 0.1801  0.1339  -0.3239 461 LYS B CE  
6385  N NZ  . LYS B 452 ? 0.5775 0.7636 0.6638 0.1659  0.1315  -0.3116 461 LYS B NZ  
6386  N N   . GLN B 453 ? 0.3982 0.9623 0.5306 0.1629  0.1577  -0.2815 462 GLN B N   
6387  C CA  . GLN B 453 ? 0.4011 1.0212 0.5398 0.1639  0.1593  -0.2730 462 GLN B CA  
6388  C C   . GLN B 453 ? 0.4169 1.0057 0.5570 0.1704  0.1568  -0.2672 462 GLN B C   
6389  O O   . GLN B 453 ? 0.4101 0.9534 0.5512 0.1528  0.1562  -0.2541 462 GLN B O   
6390  C CB  . GLN B 453 ? 0.3737 1.0328 0.5177 0.1327  0.1625  -0.2535 462 GLN B CB  
6391  C CG  . GLN B 453 ? 0.3881 1.0779 0.5303 0.1258  0.1648  -0.2587 462 GLN B CG  
6392  C CD  . GLN B 453 ? 0.4347 1.1779 0.5754 0.1533  0.1654  -0.2785 462 GLN B CD  
6393  O OE1 . GLN B 453 ? 0.4475 1.2595 0.5922 0.1578  0.1669  -0.2761 462 GLN B OE1 
6394  N NE2 . GLN B 453 ? 0.4561 1.1691 0.5895 0.1714  0.1637  -0.2980 462 GLN B NE2 
6395  N N   . GLU B 454 ? 0.4501 1.0638 0.5893 0.1979  0.1550  -0.2779 463 GLU B N   
6396  C CA  . GLU B 454 ? 0.4710 1.0653 0.6117 0.2065  0.1526  -0.2726 463 GLU B CA  
6397  C C   . GLU B 454 ? 0.4440 1.0752 0.5935 0.1817  0.1553  -0.2506 463 GLU B C   
6398  O O   . GLU B 454 ? 0.4347 1.1229 0.5880 0.1667  0.1582  -0.2433 463 GLU B O   
6399  C CB  . GLU B 454 ? 0.5003 1.1226 0.6370 0.2436  0.1498  -0.2897 463 GLU B CB  
6400  C CG  . GLU B 454 ? 0.5842 1.1391 0.7093 0.2693  0.1434  -0.3050 463 GLU B CG  
6401  C CD  . GLU B 454 ? 0.6759 1.2594 0.7928 0.3099  0.1396  -0.3256 463 GLU B CD  
6402  O OE1 . GLU B 454 ? 0.6969 1.3238 0.8184 0.3229  0.1399  -0.3226 463 GLU B OE1 
6403  O OE2 . GLU B 454 ? 0.7144 1.2766 0.8188 0.3299  0.1357  -0.3453 463 GLU B OE2 
6404  N N   . GLY B 455 ? 0.4404 1.0382 0.5917 0.1761  0.1536  -0.2397 464 GLY B N   
6405  C CA  . GLY B 455 ? 0.4262 1.0582 0.5836 0.1553  0.1548  -0.2202 464 GLY B CA  
6406  C C   . GLY B 455 ? 0.4318 1.0267 0.5900 0.1583  0.1523  -0.2129 464 GLY B C   
6407  O O   . GLY B 455 ? 0.4484 0.9798 0.6029 0.1637  0.1502  -0.2165 464 GLY B O   
6408  N N   . LYS B 456 ? 0.4274 1.0661 0.5903 0.1551  0.1523  -0.2029 465 LYS B N   
6409  C CA  . LYS B 456 ? 0.4230 1.0346 0.5873 0.1474  0.1504  -0.1900 465 LYS B CA  
6410  C C   . LYS B 456 ? 0.4371 0.9755 0.5980 0.1600  0.1478  -0.1950 465 LYS B C   
6411  O O   . LYS B 456 ? 0.4354 0.9210 0.5933 0.1456  0.1476  -0.1905 465 LYS B O   
6412  C CB  . LYS B 456 ? 0.3994 1.0057 0.5632 0.1109  0.1506  -0.1695 465 LYS B CB  
6413  C CG  . LYS B 456 ? 0.4028 1.0109 0.5681 0.1012  0.1485  -0.1551 465 LYS B CG  
6414  C CD  . LYS B 456 ? 0.4167 1.0321 0.5785 0.0660  0.1473  -0.1354 465 LYS B CD  
6415  C CE  . LYS B 456 ? 0.4476 1.0713 0.6100 0.0576  0.1444  -0.1217 465 LYS B CE  
6416  N NZ  . LYS B 456 ? 0.4608 1.0483 0.6152 0.0278  0.1411  -0.1037 465 LYS B NZ  
6417  N N   . SER B 457 ? 0.4599 0.9965 0.6204 0.1865  0.1454  -0.2035 466 SER B N   
6418  C CA  . SER B 457 ? 0.4747 0.9441 0.6313 0.1948  0.1420  -0.2041 466 SER B CA  
6419  C C   . SER B 457 ? 0.4536 0.9145 0.6141 0.1729  0.1421  -0.1848 466 SER B C   
6420  O O   . SER B 457 ? 0.4380 0.9491 0.6030 0.1623  0.1433  -0.1745 466 SER B O   
6421  C CB  . SER B 457 ? 0.5033 0.9755 0.6567 0.2293  0.1384  -0.2172 466 SER B CB  
6422  O OG  . SER B 457 ? 0.5211 1.0611 0.6807 0.2350  0.1396  -0.2128 466 SER B OG  
6423  N N   . LEU B 458 ? 0.4592 0.8565 0.6166 0.1656  0.1405  -0.1799 467 LEU B N   
6424  C CA  . LEU B 458 ? 0.4522 0.8342 0.6114 0.1478  0.1400  -0.1630 467 LEU B CA  
6425  C C   . LEU B 458 ? 0.4728 0.8128 0.6300 0.1646  0.1367  -0.1654 467 LEU B C   
6426  O O   . LEU B 458 ? 0.4878 0.7836 0.6398 0.1783  0.1344  -0.1758 467 LEU B O   
6427  C CB  . LEU B 458 ? 0.4382 0.7853 0.5947 0.1210  0.1410  -0.1524 467 LEU B CB  
6428  C CG  . LEU B 458 ? 0.4208 0.8065 0.5773 0.0986  0.1431  -0.1445 467 LEU B CG  
6429  C CD1 . LEU B 458 ? 0.4019 0.7450 0.5533 0.0752  0.1428  -0.1335 467 LEU B CD1 
6430  C CD2 . LEU B 458 ? 0.4043 0.8484 0.5638 0.0908  0.1426  -0.1346 467 LEU B CD2 
6431  N N   . TYR B 459 ? 0.4789 0.8323 0.6392 0.1620  0.1357  -0.1548 468 TYR B N   
6432  C CA  . TYR B 459 ? 0.5088 0.8359 0.6676 0.1817  0.1323  -0.1576 468 TYR B CA  
6433  C C   . TYR B 459 ? 0.4866 0.7868 0.6461 0.1647  0.1316  -0.1417 468 TYR B C   
6434  O O   . TYR B 459 ? 0.4698 0.7981 0.6320 0.1453  0.1328  -0.1291 468 TYR B O   
6435  C CB  . TYR B 459 ? 0.5317 0.9129 0.6933 0.2059  0.1313  -0.1648 468 TYR B CB  
6436  C CG  . TYR B 459 ? 0.6155 0.9663 0.7735 0.2295  0.1268  -0.1688 468 TYR B CG  
6437  C CD1 . TYR B 459 ? 0.6848 0.9831 0.8337 0.2496  0.1226  -0.1819 468 TYR B CD1 
6438  C CD2 . TYR B 459 ? 0.6674 1.0385 0.8294 0.2303  0.1259  -0.1586 468 TYR B CD2 
6439  C CE1 . TYR B 459 ? 0.7268 0.9912 0.8698 0.2705  0.1171  -0.1848 468 TYR B CE1 
6440  C CE2 . TYR B 459 ? 0.7119 1.0522 0.8698 0.2525  0.1212  -0.1618 468 TYR B CE2 
6441  C CZ  . TYR B 459 ? 0.7375 1.0233 0.8854 0.2725  0.1166  -0.1748 468 TYR B CZ  
6442  O OH  . TYR B 459 ? 0.7641 1.0153 0.9052 0.2935  0.1108  -0.1775 468 TYR B OH  
6443  N N   . VAL B 460 ? 0.4951 0.7403 0.6508 0.1711  0.1289  -0.1420 469 VAL B N   
6444  C CA  . VAL B 460 ? 0.4896 0.7097 0.6455 0.1558  0.1282  -0.1273 469 VAL B CA  
6445  C C   . VAL B 460 ? 0.5178 0.7140 0.6723 0.1731  0.1245  -0.1274 469 VAL B C   
6446  O O   . VAL B 460 ? 0.5375 0.6847 0.6866 0.1820  0.1216  -0.1323 469 VAL B O   
6447  C CB  . VAL B 460 ? 0.4775 0.6521 0.6298 0.1376  0.1290  -0.1222 469 VAL B CB  
6448  C CG1 . VAL B 460 ? 0.4651 0.6077 0.6160 0.1298  0.1274  -0.1103 469 VAL B CG1 
6449  C CG2 . VAL B 460 ? 0.4567 0.6562 0.6094 0.1157  0.1320  -0.1163 469 VAL B CG2 
6450  N N   . LYS B 461 ? 0.5283 0.7591 0.6868 0.1757  0.1240  -0.1207 470 LYS B N   
6451  C CA  . LYS B 461 ? 0.5571 0.7784 0.7149 0.1954  0.1203  -0.1213 470 LYS B CA  
6452  C C   . LYS B 461 ? 0.5572 0.7285 0.7124 0.1849  0.1186  -0.1104 470 LYS B C   
6453  O O   . LYS B 461 ? 0.5404 0.7000 0.6957 0.1613  0.1206  -0.0997 470 LYS B O   
6454  C CB  . LYS B 461 ? 0.5564 0.8421 0.7200 0.2013  0.1208  -0.1181 470 LYS B CB  
6455  C CG  . LYS B 461 ? 0.5938 0.8821 0.7592 0.2027  0.1186  -0.1074 470 LYS B CG  
6456  C CD  . LYS B 461 ? 0.6651 0.9728 0.8302 0.2356  0.1151  -0.1160 470 LYS B CD  
6457  C CE  . LYS B 461 ? 0.6701 0.9693 0.8361 0.2370  0.1125  -0.1051 470 LYS B CE  
6458  N NZ  . LYS B 461 ? 0.6931 0.9633 0.8532 0.2677  0.1072  -0.1131 470 LYS B NZ  
6459  N N   . GLY B 462 ? 0.5835 0.7234 0.7346 0.2035  0.1143  -0.1136 471 GLY B N   
6460  C CA  . GLY B 462 ? 0.5980 0.7002 0.7473 0.1964  0.1123  -0.1024 471 GLY B CA  
6461  C C   . GLY B 462 ? 0.6248 0.7402 0.7746 0.2152  0.1088  -0.1009 471 GLY B C   
6462  O O   . GLY B 462 ? 0.6466 0.7782 0.7943 0.2408  0.1060  -0.1119 471 GLY B O   
6463  N N   . GLU B 463 ? 0.6254 0.7357 0.7771 0.2043  0.1086  -0.0877 472 GLU B N   
6464  C CA  . GLU B 463 ? 0.6511 0.7674 0.8027 0.2214  0.1049  -0.0852 472 GLU B CA  
6465  C C   . GLU B 463 ? 0.6701 0.7237 0.8134 0.2297  0.0999  -0.0849 472 GLU B C   
6466  O O   . GLU B 463 ? 0.6719 0.6846 0.8104 0.2214  0.0996  -0.0869 472 GLU B O   
6467  C CB  . GLU B 463 ? 0.6341 0.7843 0.7915 0.2056  0.1068  -0.0715 472 GLU B CB  
6468  C CG  . GLU B 463 ? 0.6813 0.7957 0.8365 0.1914  0.1057  -0.0582 472 GLU B CG  
6469  C CD  . GLU B 463 ? 0.7492 0.8101 0.8995 0.1766  0.1064  -0.0557 472 GLU B CD  
6470  O OE1 . GLU B 463 ? 0.7522 0.8118 0.9021 0.1644  0.1094  -0.0590 472 GLU B OE1 
6471  O OE2 . GLU B 463 ? 0.7746 0.7974 0.9212 0.1769  0.1039  -0.0497 472 GLU B OE2 
6472  N N   . PRO B 464 ? 0.6850 0.7317 0.8259 0.2454  0.0955  -0.0820 473 PRO B N   
6473  C CA  . PRO B 464 ? 0.7019 0.6891 0.8344 0.2462  0.0906  -0.0783 473 PRO B CA  
6474  C C   . PRO B 464 ? 0.6835 0.6618 0.8190 0.2291  0.0917  -0.0626 473 PRO B C   
6475  O O   . PRO B 464 ? 0.6576 0.6743 0.7998 0.2231  0.0944  -0.0556 473 PRO B O   
6476  C CB  . PRO B 464 ? 0.7374 0.7142 0.8615 0.2775  0.0833  -0.0868 473 PRO B CB  
6477  C CG  . PRO B 464 ? 0.7308 0.7717 0.8626 0.2909  0.0855  -0.0892 473 PRO B CG  
6478  C CD  . PRO B 464 ? 0.6936 0.7802 0.8366 0.2674  0.0933  -0.0848 473 PRO B CD  
6479  N N   . ILE B 465 ? 0.6972 0.6256 0.8263 0.2219  0.0889  -0.0572 474 ILE B N   
6480  C CA  . ILE B 465 ? 0.6879 0.6037 0.8186 0.2026  0.0907  -0.0431 474 ILE B CA  
6481  C C   . ILE B 465 ? 0.7119 0.5990 0.8374 0.2101  0.0851  -0.0349 474 ILE B C   
6482  O O   . ILE B 465 ? 0.7368 0.5876 0.8529 0.2236  0.0786  -0.0388 474 ILE B O   
6483  C CB  . ILE B 465 ? 0.6774 0.5709 0.8070 0.1821  0.0939  -0.0415 474 ILE B CB  
6484  C CG1 . ILE B 465 ? 0.6688 0.5553 0.7996 0.1630  0.0962  -0.0281 474 ILE B CG1 
6485  C CG2 . ILE B 465 ? 0.6984 0.5481 0.8192 0.1875  0.0892  -0.0480 474 ILE B CG2 
6486  C CD1 . ILE B 465 ? 0.6686 0.5458 0.7989 0.1442  0.1001  -0.0272 474 ILE B CD1 
6487  N N   . ILE B 466 ? 0.7071 0.6086 0.8368 0.2000  0.0871  -0.0234 475 ILE B N   
6488  C CA  . ILE B 466 ? 0.7308 0.6279 0.8586 0.2103  0.0828  -0.0158 475 ILE B CA  
6489  C C   . ILE B 466 ? 0.7475 0.6062 0.8701 0.1998  0.0803  -0.0041 475 ILE B C   
6490  O O   . ILE B 466 ? 0.7203 0.5838 0.8458 0.1812  0.0842  0.0047  475 ILE B O   
6491  C CB  . ILE B 466 ? 0.7115 0.6588 0.8473 0.2091  0.0857  -0.0110 475 ILE B CB  
6492  C CG1 . ILE B 466 ? 0.6972 0.6632 0.8371 0.1842  0.0915  -0.0058 475 ILE B CG1 
6493  C CG2 . ILE B 466 ? 0.6921 0.6789 0.8312 0.2292  0.0850  -0.0209 475 ILE B CG2 
6494  C CD1 . ILE B 466 ? 0.6856 0.6663 0.8267 0.1724  0.0920  0.0063  475 ILE B CD1 
6495  N N   . ASN B 467 ? 0.7945 0.6156 0.9079 0.2122  0.0732  -0.0040 476 ASN B N   
6496  C CA  . ASN B 467 ? 0.8219 0.6087 0.9294 0.2036  0.0695  0.0084  476 ASN B CA  
6497  C C   . ASN B 467 ? 0.8316 0.6302 0.9402 0.2110  0.0673  0.0177  476 ASN B C   
6498  O O   . ASN B 467 ? 0.8616 0.6445 0.9632 0.2292  0.0602  0.0176  476 ASN B O   
6499  C CB  . ASN B 467 ? 0.8556 0.5909 0.9501 0.2059  0.0620  0.0070  476 ASN B CB  
6500  C CG  . ASN B 467 ? 0.8701 0.5779 0.9605 0.1869  0.0608  0.0208  476 ASN B CG  
6501  O OD1 . ASN B 467 ? 0.8494 0.5755 0.9470 0.1698  0.0673  0.0277  476 ASN B OD1 
6502  N ND2 . ASN B 467 ? 0.9014 0.5659 0.9787 0.1900  0.0517  0.0250  476 ASN B ND2 
6503  N N   . PHE B 468 ? 0.8112 0.6329 0.9265 0.1955  0.0726  0.0261  477 PHE B N   
6504  C CA  . PHE B 468 ? 0.8026 0.6622 0.9241 0.1983  0.0745  0.0306  477 PHE B CA  
6505  C C   . PHE B 468 ? 0.8006 0.6500 0.9197 0.1940  0.0722  0.0438  477 PHE B C   
6506  O O   . PHE B 468 ? 0.7835 0.6571 0.9065 0.1839  0.0754  0.0501  477 PHE B O   
6507  C CB  . PHE B 468 ? 0.7766 0.6641 0.9041 0.1803  0.0813  0.0302  477 PHE B CB  
6508  C CG  . PHE B 468 ? 0.7892 0.6519 0.9138 0.1624  0.0839  0.0329  477 PHE B CG  
6509  C CD1 . PHE B 468 ? 0.7944 0.6458 0.9162 0.1499  0.0844  0.0440  477 PHE B CD1 
6510  C CD2 . PHE B 468 ? 0.7812 0.6318 0.9050 0.1597  0.0855  0.0243  477 PHE B CD2 
6511  C CE1 . PHE B 468 ? 0.7925 0.6250 0.9111 0.1352  0.0866  0.0465  477 PHE B CE1 
6512  C CE2 . PHE B 468 ? 0.7762 0.6063 0.8972 0.1442  0.0876  0.0269  477 PHE B CE2 
6513  C CZ  . PHE B 468 ? 0.7839 0.6063 0.9023 0.1322  0.0883  0.0381  477 PHE B CZ  
6514  N N   . TYR B 469 ? 0.8197 0.6323 0.9307 0.2006  0.0660  0.0481  478 TYR B N   
6515  C CA  . TYR B 469 ? 0.8107 0.6082 0.9183 0.1917  0.0642  0.0617  478 TYR B CA  
6516  C C   . TYR B 469 ? 0.8096 0.6173 0.9166 0.2044  0.0601  0.0686  478 TYR B C   
6517  O O   . TYR B 469 ? 0.8271 0.6342 0.9313 0.2253  0.0550  0.0638  478 TYR B O   
6518  C CB  . TYR B 469 ? 0.8339 0.5867 0.9324 0.1839  0.0601  0.0658  478 TYR B CB  
6519  C CG  . TYR B 469 ? 0.8581 0.5833 0.9480 0.1868  0.0528  0.0773  478 TYR B CG  
6520  C CD1 . TYR B 469 ? 0.8395 0.5672 0.9297 0.1728  0.0543  0.0903  478 TYR B CD1 
6521  C CD2 . TYR B 469 ? 0.8989 0.5936 0.9782 0.2040  0.0436  0.0749  478 TYR B CD2 
6522  C CE1 . TYR B 469 ? 0.8769 0.5805 0.9587 0.1742  0.0474  0.1018  478 TYR B CE1 
6523  C CE2 . TYR B 469 ? 0.9321 0.5982 1.0013 0.2059  0.0357  0.0862  478 TYR B CE2 
6524  C CZ  . TYR B 469 ? 0.9248 0.5965 0.9960 0.1901  0.0379  0.1002  478 TYR B CZ  
6525  O OH  . TYR B 469 ? 0.9578 0.6026 1.0186 0.1909  0.0298  0.1124  478 TYR B OH  
6526  N N   . ASP B 470 ? 0.7815 0.5992 0.8903 0.1926  0.0622  0.0793  479 ASP B N   
6527  C CA  . ASP B 470 ? 0.7791 0.6127 0.8886 0.2024  0.0593  0.0860  479 ASP B CA  
6528  C C   . ASP B 470 ? 0.7743 0.5889 0.8784 0.1957  0.0563  0.0999  479 ASP B C   
6529  O O   . ASP B 470 ? 0.7559 0.5804 0.8615 0.1800  0.0602  0.1066  479 ASP B O   
6530  C CB  . ASP B 470 ? 0.7573 0.6376 0.8749 0.1994  0.0641  0.0842  479 ASP B CB  
6531  C CG  . ASP B 470 ? 0.7877 0.6912 0.9071 0.2157  0.0605  0.0866  479 ASP B CG  
6532  O OD1 . ASP B 470 ? 0.8333 0.7252 0.9491 0.2363  0.0552  0.0827  479 ASP B OD1 
6533  O OD2 . ASP B 470 ? 0.7966 0.7287 0.9193 0.2086  0.0624  0.0922  479 ASP B OD2 
6534  N N   . PRO B 471 ? 0.7923 0.5802 0.8886 0.2089  0.0485  0.1042  480 PRO B N   
6535  C CA  . PRO B 471 ? 0.7911 0.5564 0.8808 0.2004  0.0449  0.1180  480 PRO B CA  
6536  C C   . PRO B 471 ? 0.7627 0.5570 0.8569 0.1966  0.0473  0.1265  480 PRO B C   
6537  O O   . PRO B 471 ? 0.7436 0.5707 0.8438 0.2055  0.0490  0.1229  480 PRO B O   
6538  C CB  . PRO B 471 ? 0.8321 0.5633 0.9106 0.2179  0.0347  0.1195  480 PRO B CB  
6539  C CG  . PRO B 471 ? 0.8422 0.5962 0.9244 0.2403  0.0339  0.1086  480 PRO B CG  
6540  C CD  . PRO B 471 ? 0.8185 0.6004 0.9107 0.2335  0.0421  0.0974  480 PRO B CD  
6541  N N   . LEU B 472 ? 0.7538 0.5378 0.8444 0.1826  0.0474  0.1379  481 LEU B N   
6542  C CA  . LEU B 472 ? 0.7388 0.5427 0.8306 0.1800  0.0479  0.1476  481 LEU B CA  
6543  C C   . LEU B 472 ? 0.7637 0.5472 0.8481 0.1907  0.0397  0.1574  481 LEU B C   
6544  O O   . LEU B 472 ? 0.7870 0.5344 0.8625 0.1879  0.0342  0.1630  481 LEU B O   
6545  C CB  . LEU B 472 ? 0.7207 0.5271 0.8114 0.1604  0.0522  0.1544  481 LEU B CB  
6546  C CG  . LEU B 472 ? 0.6999 0.5370 0.7930 0.1563  0.0552  0.1587  481 LEU B CG  
6547  C CD1 . LEU B 472 ? 0.7000 0.5663 0.7992 0.1673  0.0557  0.1515  481 LEU B CD1 
6548  C CD2 . LEU B 472 ? 0.6576 0.5035 0.7500 0.1401  0.0610  0.1575  481 LEU B CD2 
6549  N N   . VAL B 473 ? 0.7585 0.5642 0.8453 0.2019  0.0381  0.1601  482 VAL B N   
6550  C CA  . VAL B 473 ? 0.7869 0.5728 0.8657 0.2131  0.0297  0.1699  482 VAL B CA  
6551  C C   . VAL B 473 ? 0.7816 0.5909 0.8619 0.2129  0.0295  0.1802  482 VAL B C   
6552  O O   . VAL B 473 ? 0.7612 0.6087 0.8494 0.2133  0.0341  0.1768  482 VAL B O   
6553  C CB  . VAL B 473 ? 0.8151 0.5843 0.8888 0.2366  0.0228  0.1622  482 VAL B CB  
6554  C CG1 . VAL B 473 ? 0.8109 0.6034 0.8859 0.2564  0.0192  0.1640  482 VAL B CG1 
6555  C CG2 . VAL B 473 ? 0.8542 0.5695 0.9134 0.2362  0.0141  0.1670  482 VAL B CG2 
6556  N N   . PHE B 474 ? 0.7989 0.5846 0.8706 0.2106  0.0236  0.1934  483 PHE B N   
6557  C CA  . PHE B 474 ? 0.7886 0.5935 0.8606 0.2070  0.0235  0.2048  483 PHE B CA  
6558  C C   . PHE B 474 ? 0.8109 0.6166 0.8790 0.2260  0.0161  0.2106  483 PHE B C   
6559  O O   . PHE B 474 ? 0.8492 0.6197 0.9068 0.2370  0.0074  0.2142  483 PHE B O   
6560  C CB  . PHE B 474 ? 0.7916 0.5798 0.8574 0.1884  0.0231  0.2175  483 PHE B CB  
6561  C CG  . PHE B 474 ? 0.7728 0.5855 0.8396 0.1828  0.0246  0.2275  483 PHE B CG  
6562  C CD1 . PHE B 474 ? 0.7289 0.5721 0.8014 0.1712  0.0324  0.2243  483 PHE B CD1 
6563  C CD2 . PHE B 474 ? 0.7944 0.5994 0.8550 0.1905  0.0176  0.2394  483 PHE B CD2 
6564  C CE1 . PHE B 474 ? 0.7172 0.5828 0.7891 0.1671  0.0333  0.2323  483 PHE B CE1 
6565  C CE2 . PHE B 474 ? 0.7840 0.6137 0.8456 0.1860  0.0190  0.2482  483 PHE B CE2 
6566  C CZ  . PHE B 474 ? 0.7494 0.6100 0.8166 0.1741  0.0270  0.2443  483 PHE B CZ  
6567  N N   . PRO B 475 ? 0.7908 0.6348 0.8653 0.2291  0.0187  0.2123  484 PRO B N   
6568  C CA  . PRO B 475 ? 0.8077 0.6616 0.8799 0.2467  0.0127  0.2182  484 PRO B CA  
6569  C C   . PRO B 475 ? 0.8414 0.6637 0.9018 0.2480  0.0043  0.2333  484 PRO B C   
6570  O O   . PRO B 475 ? 0.8487 0.6854 0.9079 0.2566  0.0008  0.2411  484 PRO B O   
6571  C CB  . PRO B 475 ? 0.7772 0.6774 0.8577 0.2393  0.0184  0.2194  484 PRO B CB  
6572  C CG  . PRO B 475 ? 0.7477 0.6529 0.8310 0.2171  0.0259  0.2168  484 PRO B CG  
6573  C CD  . PRO B 475 ? 0.7526 0.6336 0.8358 0.2159  0.0272  0.2076  484 PRO B CD  
6574  N N   . SER B 476 ? 0.8661 0.6464 0.9171 0.2389  0.0006  0.2378  485 SER B N   
6575  C CA  . SER B 476 ? 0.9011 0.6495 0.9393 0.2329  -0.0074 0.2543  485 SER B CA  
6576  C C   . SER B 476 ? 0.9255 0.6730 0.9572 0.2501  -0.0156 0.2631  485 SER B C   
6577  O O   . SER B 476 ? 0.9264 0.6812 0.9556 0.2421  -0.0169 0.2767  485 SER B O   
6578  C CB  . SER B 476 ? 0.9364 0.6329 0.9616 0.2293  -0.0147 0.2554  485 SER B CB  
6579  O OG  . SER B 476 ? 0.9796 0.6420 0.9892 0.2269  -0.0254 0.2718  485 SER B OG  
6580  N N   . ASP B 477 ? 0.9490 0.6885 0.9771 0.2748  -0.0214 0.2554  486 ASP B N   
6581  C CA  . ASP B 477 ? 0.9833 0.7185 1.0031 0.2940  -0.0304 0.2633  486 ASP B CA  
6582  C C   . ASP B 477 ? 0.9548 0.7410 0.9859 0.2938  -0.0249 0.2676  486 ASP B C   
6583  O O   . ASP B 477 ? 0.9653 0.7495 0.9908 0.2903  -0.0290 0.2820  486 ASP B O   
6584  C CB  . ASP B 477 ? 1.0168 0.7360 1.0294 0.3240  -0.0379 0.2523  486 ASP B CB  
6585  C CG  . ASP B 477 ? 1.0787 0.7314 1.0700 0.3284  -0.0502 0.2550  486 ASP B CG  
6586  O OD1 . ASP B 477 ? 1.0986 0.7200 1.0818 0.3058  -0.0527 0.2665  486 ASP B OD1 
6587  O OD2 . ASP B 477 ? 1.1274 0.7592 1.1088 0.3542  -0.0580 0.2457  486 ASP B OD2 
6588  N N   . GLU B 478 ? 0.9192 0.7504 0.9650 0.2953  -0.0160 0.2557  487 GLU B N   
6589  C CA  . GLU B 478 ? 0.8936 0.7752 0.9494 0.2943  -0.0112 0.2579  487 GLU B CA  
6590  C C   . GLU B 478 ? 0.8655 0.7556 0.9222 0.2705  -0.0071 0.2694  487 GLU B C   
6591  O O   . GLU B 478 ? 0.8591 0.7747 0.9171 0.2707  -0.0076 0.2774  487 GLU B O   
6592  C CB  . GLU B 478 ? 0.8686 0.7918 0.9377 0.2951  -0.0032 0.2432  487 GLU B CB  
6593  C CG  . GLU B 478 ? 0.8860 0.8619 0.9634 0.2981  -0.0006 0.2442  487 GLU B CG  
6594  C CD  . GLU B 478 ? 0.8945 0.9042 0.9814 0.2767  0.0087  0.2384  487 GLU B CD  
6595  O OE1 . GLU B 478 ? 0.8941 0.9421 0.9851 0.2720  0.0103  0.2414  487 GLU B OE1 
6596  O OE2 . GLU B 478 ? 0.8933 0.8892 0.9818 0.2642  0.0135  0.2310  487 GLU B OE2 
6597  N N   . PHE B 479 ? 0.8445 0.7150 0.8999 0.2510  -0.0033 0.2696  488 PHE B N   
6598  C CA  . PHE B 479 ? 0.8212 0.6961 0.8750 0.2305  -0.0002 0.2803  488 PHE B CA  
6599  C C   . PHE B 479 ? 0.8488 0.6980 0.8907 0.2314  -0.0090 0.2976  488 PHE B C   
6600  O O   . PHE B 479 ? 0.8445 0.7143 0.8861 0.2292  -0.0095 0.3074  488 PHE B O   
6601  C CB  . PHE B 479 ? 0.8076 0.6686 0.8622 0.2126  0.0053  0.2756  488 PHE B CB  
6602  C CG  . PHE B 479 ? 0.7903 0.6632 0.8439 0.1927  0.0098  0.2836  488 PHE B CG  
6603  C CD1 . PHE B 479 ? 0.7582 0.6646 0.8183 0.1839  0.0178  0.2763  488 PHE B CD1 
6604  C CD2 . PHE B 479 ? 0.8025 0.6533 0.8470 0.1827  0.0054  0.2982  488 PHE B CD2 
6605  C CE1 . PHE B 479 ? 0.7398 0.6578 0.7971 0.1681  0.0216  0.2822  488 PHE B CE1 
6606  C CE2 . PHE B 479 ? 0.7870 0.6544 0.8306 0.1656  0.0098  0.3052  488 PHE B CE2 
6607  C CZ  . PHE B 479 ? 0.7515 0.6527 0.8014 0.1598  0.0181  0.2964  488 PHE B CZ  
6608  N N   . ASP B 480 ? 0.8774 0.6807 0.9081 0.2344  -0.0168 0.3015  489 ASP B N   
6609  C CA  . ASP B 480 ? 0.9136 0.6855 0.9298 0.2337  -0.0271 0.3188  489 ASP B CA  
6610  C C   . ASP B 480 ? 0.9238 0.7102 0.9378 0.2514  -0.0327 0.3254  489 ASP B C   
6611  O O   . ASP B 480 ? 0.9440 0.7199 0.9487 0.2478  -0.0391 0.3416  489 ASP B O   
6612  C CB  . ASP B 480 ? 0.9558 0.6729 0.9578 0.2394  -0.0369 0.3188  489 ASP B CB  
6613  C CG  . ASP B 480 ? 0.9658 0.6623 0.9656 0.2171  -0.0342 0.3191  489 ASP B CG  
6614  O OD1 . ASP B 480 ? 0.9535 0.6801 0.9641 0.2001  -0.0238 0.3167  489 ASP B OD1 
6615  O OD2 . ASP B 480 ? 1.0131 0.6621 0.9988 0.2170  -0.0433 0.3217  489 ASP B OD2 
6616  N N   . ALA B 481 ? 0.9082 0.7208 0.9308 0.2705  -0.0304 0.3131  490 ALA B N   
6617  C CA  . ALA B 481 ? 0.9114 0.7477 0.9345 0.2888  -0.0343 0.3168  490 ALA B CA  
6618  C C   . ALA B 481 ? 0.8823 0.7591 0.9125 0.2749  -0.0284 0.3246  490 ALA B C   
6619  O O   . ALA B 481 ? 0.9002 0.7756 0.9235 0.2763  -0.0340 0.3389  490 ALA B O   
6620  C CB  . ALA B 481 ? 0.9008 0.7635 0.9327 0.3090  -0.0319 0.3012  490 ALA B CB  
6621  N N   . SER B 482 ? 0.8358 0.7464 0.8781 0.2618  -0.0179 0.3151  491 SER B N   
6622  C CA  . SER B 482 ? 0.8067 0.7526 0.8535 0.2477  -0.0125 0.3202  491 SER B CA  
6623  C C   . SER B 482 ? 0.8175 0.7470 0.8554 0.2336  -0.0152 0.3365  491 SER B C   
6624  O O   . SER B 482 ? 0.8186 0.7687 0.8551 0.2322  -0.0165 0.3464  491 SER B O   
6625  C CB  . SER B 482 ? 0.7682 0.7359 0.8236 0.2327  -0.0026 0.3081  491 SER B CB  
6626  O OG  . SER B 482 ? 0.7584 0.7564 0.8223 0.2424  0.0000  0.2963  491 SER B OG  
6627  N N   . ILE B 483 ? 0.8265 0.7212 0.8582 0.2226  -0.0165 0.3399  492 ILE B N   
6628  C CA  . ILE B 483 ? 0.8394 0.7216 0.8624 0.2068  -0.0191 0.3561  492 ILE B CA  
6629  C C   . ILE B 483 ? 0.8807 0.7391 0.8915 0.2154  -0.0306 0.3724  492 ILE B C   
6630  O O   . ILE B 483 ? 0.8843 0.7593 0.8920 0.2100  -0.0320 0.3855  492 ILE B O   
6631  C CB  . ILE B 483 ? 0.8401 0.6966 0.8597 0.1904  -0.0174 0.3560  492 ILE B CB  
6632  C CG1 . ILE B 483 ? 0.8076 0.6889 0.8379 0.1821  -0.0063 0.3408  492 ILE B CG1 
6633  C CG2 . ILE B 483 ? 0.8527 0.7028 0.8631 0.1731  -0.0205 0.3743  492 ILE B CG2 
6634  C CD1 . ILE B 483 ? 0.8140 0.7032 0.8428 0.1610  -0.0011 0.3455  492 ILE B CD1 
6635  N N   . SER B 484 ? 0.9139 0.7320 0.9159 0.2292  -0.0395 0.3718  493 SER B N   
6636  C CA  . SER B 484 ? 0.9543 0.7439 0.9416 0.2397  -0.0521 0.3864  493 SER B CA  
6637  C C   . SER B 484 ? 0.9444 0.7731 0.9375 0.2524  -0.0513 0.3889  493 SER B C   
6638  O O   . SER B 484 ? 0.9800 0.7978 0.9625 0.2590  -0.0603 0.4032  493 SER B O   
6639  C CB  . SER B 484 ? 0.9901 0.7348 0.9665 0.2594  -0.0619 0.3806  493 SER B CB  
6640  O OG  . SER B 484 ? 1.0321 0.7444 0.9908 0.2696  -0.0756 0.3956  493 SER B OG  
6641  N N   . GLN B 485 ? 0.8980 0.7721 0.9065 0.2536  -0.0411 0.3759  494 GLN B N   
6642  C CA  . GLN B 485 ? 0.8828 0.7992 0.8978 0.2628  -0.0395 0.3767  494 GLN B CA  
6643  C C   . GLN B 485 ? 0.8477 0.7997 0.8673 0.2441  -0.0326 0.3824  494 GLN B C   
6644  O O   . GLN B 485 ? 0.8446 0.8254 0.8655 0.2490  -0.0336 0.3880  494 GLN B O   
6645  C CB  . GLN B 485 ? 0.8675 0.8109 0.8938 0.2777  -0.0350 0.3594  494 GLN B CB  
6646  C CG  . GLN B 485 ? 0.9029 0.8744 0.9310 0.2986  -0.0391 0.3608  494 GLN B CG  
6647  C CD  . GLN B 485 ? 0.9039 0.9305 0.9436 0.2910  -0.0313 0.3562  494 GLN B CD  
6648  O OE1 . GLN B 485 ? 0.8747 0.9192 0.9226 0.2774  -0.0229 0.3453  494 GLN B OE1 
6649  N NE2 . GLN B 485 ? 0.9288 0.9814 0.9678 0.2995  -0.0350 0.3647  494 GLN B NE2 
6650  N N   . VAL B 486 ? 0.8246 0.7757 0.8457 0.2238  -0.0261 0.3807  495 VAL B N   
6651  C CA  . VAL B 486 ? 0.7982 0.7777 0.8196 0.2075  -0.0212 0.3875  495 VAL B CA  
6652  C C   . VAL B 486 ? 0.8281 0.7916 0.8383 0.2035  -0.0291 0.4079  495 VAL B C   
6653  O O   . VAL B 486 ? 0.8239 0.8127 0.8325 0.2000  -0.0291 0.4170  495 VAL B O   
6654  C CB  . VAL B 486 ? 0.7725 0.7556 0.7967 0.1891  -0.0128 0.3801  495 VAL B CB  
6655  C CG1 . VAL B 486 ? 0.7641 0.7575 0.7823 0.1728  -0.0117 0.3928  495 VAL B CG1 
6656  C CG2 . VAL B 486 ? 0.7317 0.7462 0.7651 0.1893  -0.0048 0.3631  495 VAL B CG2 
6657  N N   . ASN B 487 ? 0.8630 0.7826 0.8637 0.2038  -0.0366 0.4152  496 ASN B N   
6658  C CA  . ASN B 487 ? 0.9056 0.8039 0.8927 0.1993  -0.0462 0.4360  496 ASN B CA  
6659  C C   . ASN B 487 ? 0.9286 0.8311 0.9114 0.2180  -0.0540 0.4438  496 ASN B C   
6660  O O   . ASN B 487 ? 0.9472 0.8500 0.9213 0.2125  -0.0597 0.4614  496 ASN B O   
6661  C CB  . ASN B 487 ? 0.9407 0.7869 0.9158 0.1928  -0.0539 0.4421  496 ASN B CB  
6662  C CG  . ASN B 487 ? 0.9306 0.7774 0.9101 0.1733  -0.0460 0.4359  496 ASN B CG  
6663  O OD1 . ASN B 487 ? 0.9130 0.7892 0.8960 0.1568  -0.0392 0.4397  496 ASN B OD1 
6664  N ND2 . ASN B 487 ? 0.9600 0.7758 0.9387 0.1765  -0.0471 0.4256  496 ASN B ND2 
6665  N N   . GLU B 488 ? 0.9273 0.8364 0.9161 0.2399  -0.0544 0.4311  497 GLU B N   
6666  C CA  . GLU B 488 ? 0.9362 0.8663 0.9250 0.2585  -0.0590 0.4352  497 GLU B CA  
6667  C C   . GLU B 488 ? 0.9166 0.8883 0.9093 0.2460  -0.0541 0.4431  497 GLU B C   
6668  O O   . GLU B 488 ? 0.9419 0.9125 0.9261 0.2465  -0.0607 0.4594  497 GLU B O   
6669  C CB  . GLU B 488 ? 0.9166 0.8730 0.9171 0.2777  -0.0551 0.4176  497 GLU B CB  
6670  C CG  . GLU B 488 ? 0.9393 0.8625 0.9347 0.2993  -0.0619 0.4100  497 GLU B CG  
6671  C CD  . GLU B 488 ? 0.9858 0.8609 0.9620 0.3089  -0.0759 0.4251  497 GLU B CD  
6672  O OE1 . GLU B 488 ? 0.9893 0.8633 0.9579 0.2995  -0.0801 0.4423  497 GLU B OE1 
6673  O OE2 . GLU B 488 ? 1.0180 0.8552 0.9851 0.3258  -0.0835 0.4199  497 GLU B OE2 
6674  N N   . LYS B 489 ? 0.8780 0.8840 0.8818 0.2345  -0.0431 0.4316  498 LYS B N   
6675  C CA  . LYS B 489 ? 0.8613 0.9092 0.8681 0.2253  -0.0384 0.4352  498 LYS B CA  
6676  C C   . LYS B 489 ? 0.8727 0.9179 0.8710 0.2081  -0.0396 0.4515  498 LYS B C   
6677  O O   . LYS B 489 ? 0.8791 0.9469 0.8744 0.2075  -0.0416 0.4622  498 LYS B O   
6678  C CB  . LYS B 489 ? 0.8245 0.9017 0.8411 0.2168  -0.0280 0.4182  498 LYS B CB  
6679  C CG  . LYS B 489 ? 0.8276 0.9086 0.8528 0.2292  -0.0259 0.4019  498 LYS B CG  
6680  C CD  . LYS B 489 ? 0.8486 0.9631 0.8780 0.2428  -0.0280 0.4006  498 LYS B CD  
6681  C CE  . LYS B 489 ? 0.8599 0.9823 0.8977 0.2551  -0.0263 0.3854  498 LYS B CE  
6682  N NZ  . LYS B 489 ? 0.8886 1.0458 0.9299 0.2694  -0.0295 0.3864  498 LYS B NZ  
6683  N N   . ILE B 490 ? 0.8806 0.9024 0.8752 0.1936  -0.0382 0.4537  499 ILE B N   
6684  C CA  . ILE B 490 ? 0.8987 0.9216 0.8848 0.1766  -0.0399 0.4707  499 ILE B CA  
6685  C C   . ILE B 490 ? 0.9526 0.9515 0.9267 0.1822  -0.0520 0.4905  499 ILE B C   
6686  O O   . ILE B 490 ? 0.9563 0.9777 0.9268 0.1802  -0.0541 0.5029  499 ILE B O   
6687  C CB  . ILE B 490 ? 0.8962 0.8999 0.8800 0.1598  -0.0371 0.4706  499 ILE B CB  
6688  C CG1 . ILE B 490 ? 0.8484 0.8693 0.8428 0.1576  -0.0263 0.4497  499 ILE B CG1 
6689  C CG2 . ILE B 490 ? 0.9015 0.9196 0.8776 0.1410  -0.0376 0.4879  499 ILE B CG2 
6690  C CD1 . ILE B 490 ? 0.8376 0.8325 0.8312 0.1467  -0.0244 0.4458  499 ILE B CD1 
6691  N N   . ASN B 491 ? 1.0008 0.9529 0.9673 0.1900  -0.0606 0.4931  500 ASN B N   
6692  C CA  . ASN B 491 ? 1.0678 0.9893 1.0199 0.1992  -0.0742 0.5102  500 ASN B CA  
6693  C C   . ASN B 491 ? 1.0521 1.0045 1.0063 0.2139  -0.0760 0.5144  500 ASN B C   
6694  O O   . ASN B 491 ? 1.0771 1.0245 1.0204 0.2123  -0.0841 0.5329  500 ASN B O   
6695  C CB  . ASN B 491 ? 1.1184 0.9890 1.0629 0.2150  -0.0828 0.5046  500 ASN B CB  
6696  C CG  . ASN B 491 ? 1.2553 1.0751 1.1841 0.1994  -0.0912 0.5163  500 ASN B CG  
6697  O OD1 . ASN B 491 ? 1.2612 1.0889 1.1874 0.1751  -0.0889 0.5276  500 ASN B OD1 
6698  N ND2 . ASN B 491 ? 1.4751 1.2433 1.3921 0.2135  -0.1015 0.5137  500 ASN B ND2 
6699  N N   . GLN B 492 ? 1.0114 0.9972 0.9792 0.2267  -0.0687 0.4975  501 GLN B N   
6700  C CA  . GLN B 492 ? 0.9995 1.0210 0.9714 0.2403  -0.0693 0.4984  501 GLN B CA  
6701  C C   . GLN B 492 ? 0.9698 1.0305 0.9430 0.2245  -0.0643 0.5067  501 GLN B C   
6702  O O   . GLN B 492 ? 0.9819 1.0566 0.9500 0.2288  -0.0695 0.5198  501 GLN B O   
6703  C CB  . GLN B 492 ? 0.9742 1.0231 0.9605 0.2523  -0.0618 0.4771  501 GLN B CB  
6704  C CG  . GLN B 492 ? 1.0006 1.0778 0.9910 0.2733  -0.0647 0.4746  501 GLN B CG  
6705  C CD  . GLN B 492 ? 1.0191 1.1064 1.0201 0.2876  -0.0609 0.4551  501 GLN B CD  
6706  O OE1 . GLN B 492 ? 0.9926 1.0954 1.0031 0.2771  -0.0517 0.4406  501 GLN B OE1 
6707  N NE2 . GLN B 492 ? 1.0630 1.1415 1.0612 0.3123  -0.0684 0.4548  501 GLN B NE2 
6708  N N   . SER B 493 ? 0.9280 1.0064 0.9071 0.2076  -0.0545 0.4982  502 SER B N   
6709  C CA  . SER B 493 ? 0.8982 1.0160 0.8780 0.1938  -0.0487 0.5019  502 SER B CA  
6710  C C   . SER B 493 ? 0.9202 1.0318 0.8882 0.1820  -0.0548 0.5249  502 SER B C   
6711  O O   . SER B 493 ? 0.9207 1.0596 0.8858 0.1821  -0.0565 0.5350  502 SER B O   
6712  C CB  . SER B 493 ? 0.8656 0.9950 0.8511 0.1804  -0.0384 0.4874  502 SER B CB  
6713  O OG  . SER B 493 ? 0.8366 1.0066 0.8222 0.1720  -0.0327 0.4857  502 SER B OG  
6714  N N   . LEU B 494 ? 0.9341 1.0107 0.8947 0.1707  -0.0585 0.5337  503 LEU B N   
6715  C CA  . LEU B 494 ? 0.9594 1.0253 0.9071 0.1568  -0.0658 0.5573  503 LEU B CA  
6716  C C   . LEU B 494 ? 0.9917 1.0493 0.9302 0.1679  -0.0767 0.5736  503 LEU B C   
6717  O O   . LEU B 494 ? 1.0024 1.0794 0.9344 0.1587  -0.0795 0.5905  503 LEU B O   
6718  C CB  . LEU B 494 ? 0.9838 1.0030 0.9232 0.1462  -0.0712 0.5635  503 LEU B CB  
6719  C CG  . LEU B 494 ? 0.9614 0.9882 0.9072 0.1313  -0.0616 0.5523  503 LEU B CG  
6720  C CD1 . LEU B 494 ? 0.9998 0.9778 0.9351 0.1202  -0.0692 0.5612  503 LEU B CD1 
6721  C CD2 . LEU B 494 ? 0.9417 1.0158 0.8888 0.1149  -0.0541 0.5573  503 LEU B CD2 
6722  N N   . ALA B 495 ? 1.0088 1.0385 0.9464 0.1888  -0.0833 0.5685  504 ALA B N   
6723  C CA  . ALA B 495 ? 1.0358 1.0560 0.9645 0.2047  -0.0941 0.5811  504 ALA B CA  
6724  C C   . ALA B 495 ? 1.0083 1.0815 0.9449 0.2115  -0.0896 0.5800  504 ALA B C   
6725  O O   . ALA B 495 ? 1.0315 1.1097 0.9594 0.2142  -0.0970 0.5969  504 ALA B O   
6726  C CB  . ALA B 495 ? 1.0581 1.0412 0.9845 0.2284  -0.1009 0.5720  504 ALA B CB  
6727  N N   . PHE B 496 ? 0.9591 1.0701 0.9103 0.2135  -0.0783 0.5606  505 PHE B N   
6728  C CA  . PHE B 496 ? 0.9336 1.0948 0.8906 0.2157  -0.0740 0.5590  505 PHE B CA  
6729  C C   . PHE B 496 ? 0.9296 1.1142 0.8806 0.1970  -0.0724 0.5732  505 PHE B C   
6730  O O   . PHE B 496 ? 0.9387 1.1469 0.8861 0.1998  -0.0758 0.5843  505 PHE B O   
6731  C CB  . PHE B 496 ? 0.8956 1.0878 0.8660 0.2174  -0.0634 0.5360  505 PHE B CB  
6732  C CG  . PHE B 496 ? 0.9061 1.1031 0.8838 0.2382  -0.0650 0.5244  505 PHE B CG  
6733  C CD1 . PHE B 496 ? 0.9180 1.0982 0.9026 0.2445  -0.0618 0.5080  505 PHE B CD1 
6734  C CD2 . PHE B 496 ? 0.9192 1.1414 0.8968 0.2517  -0.0695 0.5299  505 PHE B CD2 
6735  C CE1 . PHE B 496 ? 0.9191 1.1100 0.9106 0.2642  -0.0632 0.4975  505 PHE B CE1 
6736  C CE2 . PHE B 496 ? 0.9173 1.1506 0.9019 0.2715  -0.0710 0.5196  505 PHE B CE2 
6737  C CZ  . PHE B 496 ? 0.9122 1.1311 0.9038 0.2776  -0.0677 0.5035  505 PHE B CZ  
6738  N N   . ILE B 497 ? 0.9195 1.1005 0.8693 0.1785  -0.0673 0.5730  506 ILE B N   
6739  C CA  . ILE B 497 ? 0.9207 1.1264 0.8641 0.1606  -0.0659 0.5872  506 ILE B CA  
6740  C C   . ILE B 497 ? 0.9687 1.1532 0.8984 0.1560  -0.0775 0.6136  506 ILE B C   
6741  O O   . ILE B 497 ? 0.9743 1.1866 0.8995 0.1534  -0.0797 0.6266  506 ILE B O   
6742  C CB  . ILE B 497 ? 0.9013 1.1092 0.8460 0.1432  -0.0583 0.5813  506 ILE B CB  
6743  C CG1 . ILE B 497 ? 0.8610 1.0935 0.8163 0.1472  -0.0474 0.5562  506 ILE B CG1 
6744  C CG2 . ILE B 497 ? 0.9010 1.1349 0.8377 0.1251  -0.0580 0.5983  506 ILE B CG2 
6745  C CD1 . ILE B 497 ? 0.8396 1.1188 0.7964 0.1504  -0.0431 0.5502  506 ILE B CD1 
6746  N N   . ARG B 498 ? 1.0080 1.1418 0.9298 0.1546  -0.0857 0.6214  507 ARG B N   
6747  C CA  . ARG B 498 ? 1.0656 1.1651 0.9710 0.1532  -0.0999 0.6454  507 ARG B CA  
6748  C C   . ARG B 498 ? 1.0734 1.1931 0.9759 0.1670  -0.1052 0.6548  507 ARG B C   
6749  O O   . ARG B 498 ? 1.0905 1.2203 0.9829 0.1568  -0.1109 0.6757  507 ARG B O   
6750  C CB  . ARG B 498 ? 1.1022 1.1415 1.0009 0.1652  -0.1088 0.6424  507 ARG B CB  
6751  C CG  . ARG B 498 ? 1.1474 1.1499 1.0418 0.1495  -0.1092 0.6412  507 ARG B CG  
6752  C CD  . ARG B 498 ? 1.2585 1.1949 1.1339 0.1561  -0.1256 0.6535  507 ARG B CD  
6753  N NE  . ARG B 498 ? 1.3515 1.2854 1.2132 0.1595  -0.1369 0.6752  507 ARG B NE  
6754  C CZ  . ARG B 498 ? 1.4246 1.3079 1.2673 0.1720  -0.1532 0.6878  507 ARG B CZ  
6755  N NH1 . ARG B 498 ? 1.4615 1.2884 1.2949 0.1836  -0.1613 0.6808  507 ARG B NH1 
6756  N NH2 . ARG B 498 ? 1.4448 1.3328 1.2759 0.1737  -0.1623 0.7076  507 ARG B NH2 
6757  N N   . LYS B 499 ? 1.0601 1.1881 0.9718 0.1897  -0.1034 0.6393  508 LYS B N   
6758  C CA  . LYS B 499 ? 1.0671 1.2190 0.9786 0.2056  -0.1074 0.6443  508 LYS B CA  
6759  C C   . LYS B 499 ? 1.0369 1.2462 0.9531 0.1950  -0.1001 0.6468  508 LYS B C   
6760  O O   . LYS B 499 ? 1.0572 1.2801 0.9655 0.1947  -0.1062 0.6642  508 LYS B O   
6761  C CB  . LYS B 499 ? 1.0541 1.2096 0.9763 0.2301  -0.1054 0.6245  508 LYS B CB  
6762  C CG  . LYS B 499 ? 1.0854 1.2634 1.0073 0.2501  -0.1108 0.6290  508 LYS B CG  
6763  C CD  . LYS B 499 ? 1.1686 1.3008 1.0764 0.2711  -0.1260 0.6409  508 LYS B CD  
6764  C CE  . LYS B 499 ? 1.2211 1.3248 1.1084 0.2628  -0.1390 0.6694  508 LYS B CE  
6765  N NZ  . LYS B 499 ? 1.2055 1.3481 1.0904 0.2611  -0.1409 0.6842  508 LYS B NZ  
6766  N N   . SER B 500 ? 0.9931 1.2341 0.9203 0.1869  -0.0877 0.6293  509 SER B N   
6767  C CA  . SER B 500 ? 0.9676 1.2604 0.8969 0.1773  -0.0808 0.6290  509 SER B CA  
6768  C C   . SER B 500 ? 0.9921 1.2921 0.9098 0.1593  -0.0846 0.6523  509 SER B C   
6769  O O   . SER B 500 ? 0.9945 1.3249 0.9079 0.1586  -0.0869 0.6640  509 SER B O   
6770  C CB  . SER B 500 ? 0.9261 1.2390 0.8647 0.1707  -0.0687 0.6067  509 SER B CB  
6771  O OG  . SER B 500 ? 0.8961 1.2564 0.8347 0.1650  -0.0629 0.6030  509 SER B OG  
6772  N N   . ASP B 501 ? 1.0124 1.2859 0.9247 0.1441  -0.0858 0.6598  510 ASP B N   
6773  C CA  . ASP B 501 ? 1.0381 1.3212 0.9394 0.1238  -0.0892 0.6823  510 ASP B CA  
6774  C C   . ASP B 501 ? 1.0808 1.3500 0.9694 0.1259  -0.1021 0.7070  510 ASP B C   
6775  O O   . ASP B 501 ? 1.0878 1.3905 0.9708 0.1161  -0.1030 0.7223  510 ASP B O   
6776  C CB  . ASP B 501 ? 1.0528 1.3063 0.9498 0.1063  -0.0896 0.6868  510 ASP B CB  
6777  C CG  . ASP B 501 ? 1.0267 1.3120 0.9327 0.0968  -0.0763 0.6695  510 ASP B CG  
6778  O OD1 . ASP B 501 ? 1.0238 1.3584 0.9303 0.0904  -0.0699 0.6694  510 ASP B OD1 
6779  O OD2 . ASP B 501 ? 1.0255 1.2857 0.9367 0.0967  -0.0728 0.6558  510 ASP B OD2 
6780  N N   . GLU B 502 ? 1.1158 1.3362 0.9988 0.1398  -0.1124 0.7108  511 GLU B N   
6781  C CA  . GLU B 502 ? 1.1659 1.3660 1.0344 0.1450  -0.1264 0.7338  511 GLU B CA  
6782  C C   . GLU B 502 ? 1.1491 1.3990 1.0213 0.1528  -0.1241 0.7364  511 GLU B C   
6783  O O   . GLU B 502 ? 1.1736 1.4359 1.0349 0.1434  -0.1306 0.7586  511 GLU B O   
6784  C CB  . GLU B 502 ? 1.1991 1.3462 1.0624 0.1672  -0.1365 0.7304  511 GLU B CB  
6785  C CG  . GLU B 502 ? 1.2719 1.3547 1.1202 0.1587  -0.1470 0.7405  511 GLU B CG  
6786  C CD  . GLU B 502 ? 1.3304 1.3637 1.1753 0.1845  -0.1547 0.7298  511 GLU B CD  
6787  O OE1 . GLU B 502 ? 1.3610 1.3929 1.2026 0.2074  -0.1615 0.7319  511 GLU B OE1 
6788  O OE2 . GLU B 502 ? 1.3267 1.3246 1.1719 0.1827  -0.1540 0.7191  511 GLU B OE2 
6789  N N   . LEU B 503 ? 1.1085 1.3875 0.9952 0.1684  -0.1154 0.7140  512 LEU B N   
6790  C CA  . LEU B 503 ? 1.0908 1.4180 0.9814 0.1762  -0.1130 0.7137  512 LEU B CA  
6791  C C   . LEU B 503 ? 1.0767 1.4500 0.9651 0.1572  -0.1074 0.7218  512 LEU B C   
6792  O O   . LEU B 503 ? 1.0869 1.4899 0.9708 0.1581  -0.1105 0.7341  512 LEU B O   
6793  C CB  . LEU B 503 ? 1.0540 1.4041 0.9596 0.1920  -0.1047 0.6876  512 LEU B CB  
6794  C CG  . LEU B 503 ? 1.0723 1.3894 0.9799 0.2149  -0.1112 0.6814  512 LEU B CG  
6795  C CD1 . LEU B 503 ? 1.0381 1.3813 0.9607 0.2272  -0.1027 0.6560  512 LEU B CD1 
6796  C CD2 . LEU B 503 ? 1.1101 1.4224 1.0079 0.2281  -0.1229 0.6999  512 LEU B CD2 
6797  N N   . LEU B 504 ? 1.0580 1.4384 0.9487 0.1409  -0.0996 0.7155  513 LEU B N   
6798  C CA  . LEU B 504 ? 1.0453 1.4733 0.9334 0.1249  -0.0936 0.7210  513 LEU B CA  
6799  C C   . LEU B 504 ? 1.0850 1.5112 0.9594 0.1061  -0.1013 0.7505  513 LEU B C   
6800  O O   . LEU B 504 ? 1.0801 1.5504 0.9502 0.0981  -0.1000 0.7609  513 LEU B O   
6801  C CB  . LEU B 504 ? 1.0089 1.4519 0.9046 0.1178  -0.0818 0.7006  513 LEU B CB  
6802  C CG  . LEU B 504 ? 0.9689 1.4178 0.8760 0.1340  -0.0749 0.6728  513 LEU B CG  
6803  C CD1 . LEU B 504 ? 0.9583 1.3921 0.8715 0.1293  -0.0672 0.6548  513 LEU B CD1 
6804  C CD2 . LEU B 504 ? 0.9310 1.4317 0.8389 0.1376  -0.0696 0.6639  513 LEU B CD2 
6805  N N   . HIS B 505 ? 1.1271 1.5028 0.9932 0.0981  -0.1100 0.7641  514 HIS B N   
6806  C CA  . HIS B 505 ? 1.1782 1.5452 1.0283 0.0788  -0.1202 0.7947  514 HIS B CA  
6807  C C   . HIS B 505 ? 1.2172 1.5730 1.0577 0.0895  -0.1321 0.8123  514 HIS B C   
6808  O O   . HIS B 505 ? 1.2627 1.5968 1.0869 0.0772  -0.1443 0.8392  514 HIS B O   
6809  C CB  . HIS B 505 ? 1.2054 1.5203 1.0473 0.0643  -0.1266 0.8031  514 HIS B CB  
6810  C CG  . HIS B 505 ? 1.1894 1.5172 1.0413 0.0548  -0.1148 0.7856  514 HIS B CG  
6811  N ND1 . HIS B 505 ? 1.1686 1.5540 1.0252 0.0424  -0.1041 0.7823  514 HIS B ND1 
6812  C CD2 . HIS B 505 ? 1.1911 1.4827 1.0485 0.0576  -0.1121 0.7697  514 HIS B CD2 
6813  C CE1 . HIS B 505 ? 1.1460 1.5293 1.0102 0.0381  -0.0957 0.7656  514 HIS B CE1 
6814  N NE2 . HIS B 505 ? 1.1580 1.4849 1.0234 0.0463  -0.1001 0.7580  514 HIS B NE2 
6815  N N   . ASN B 506 ? 1.2063 1.5788 1.0561 0.1120  -0.1288 0.7969  515 ASN B N   
6816  C CA  . ASN B 506 ? 1.2375 1.6162 1.0811 0.1247  -0.1374 0.8101  515 ASN B CA  
6817  C C   . ASN B 506 ? 1.2102 1.6569 1.0607 0.1260  -0.1290 0.8049  515 ASN B C   
6818  O O   . ASN B 506 ? 1.2170 1.6789 1.0668 0.1401  -0.1331 0.8086  515 ASN B O   
6819  C CB  . ASN B 506 ? 1.2466 1.5898 1.0939 0.1515  -0.1422 0.7979  515 ASN B CB  
6820  C CG  . ASN B 506 ? 1.3096 1.6013 1.1391 0.1587  -0.1596 0.8201  515 ASN B CG  
6821  O OD1 . ASN B 506 ? 1.3419 1.5763 1.1638 0.1613  -0.1669 0.8208  515 ASN B OD1 
6822  N ND2 . ASN B 506 ? 1.3232 1.6328 1.1441 0.1622  -0.1670 0.8383  515 ASN B ND2 
6823  N N   . VAL B 507 ? 1.1843 1.6710 1.0401 0.1122  -0.1177 0.7958  516 VAL B N   
6824  C CA  . VAL B 507 ? 1.1543 1.7047 1.0148 0.1130  -0.1089 0.7868  516 VAL B CA  
6825  C C   . VAL B 507 ? 1.1585 1.7497 1.0112 0.0913  -0.1064 0.8022  516 VAL B C   
6826  O O   . VAL B 507 ? 1.1509 1.7450 1.0039 0.0769  -0.1009 0.7994  516 VAL B O   
6827  C CB  . VAL B 507 ? 1.1099 1.6762 0.9840 0.1240  -0.0969 0.7533  516 VAL B CB  
6828  C CG1 . VAL B 507 ? 1.0776 1.7045 0.9521 0.1211  -0.0882 0.7429  516 VAL B CG1 
6829  C CG2 . VAL B 507 ? 1.0984 1.6444 0.9798 0.1458  -0.0997 0.7407  516 VAL B CG2 
6830  N N   . ASN B 508 ? 1.1659 1.7921 1.0117 0.0894  -0.1102 0.8184  517 ASN B N   
6831  C CA  . ASN B 508 ? 1.1732 1.8380 1.0099 0.0691  -0.1101 0.8378  517 ASN B CA  
6832  C C   . ASN B 508 ? 1.1706 1.8826 1.0025 0.0724  -0.1119 0.8480  517 ASN B C   
6833  O O   . ASN B 508 ? 1.1444 1.8782 0.9825 0.0888  -0.1077 0.8308  517 ASN B O   
6834  C CB  . ASN B 508 ? 1.2173 1.8409 1.0422 0.0510  -0.1213 0.8659  517 ASN B CB  
6835  C CG  . ASN B 508 ? 1.2331 1.8948 1.0500 0.0252  -0.1198 0.8842  517 ASN B CG  
6836  O OD1 . ASN B 508 ? 1.2311 1.9546 1.0482 0.0222  -0.1131 0.8829  517 ASN B OD1 
6837  N ND2 . ASN B 508 ? 1.2599 1.8854 1.0682 0.0061  -0.1271 0.9021  517 ASN B ND2 
6838  N N   . GLN C 26  ? 0.8028 1.3543 0.9479 -0.6268 -0.0509 0.0967  26  GLN C N   
6839  C CA  . GLN C 26  ? 0.8236 1.3041 0.9513 -0.6214 -0.0570 0.0680  26  GLN C CA  
6840  C C   . GLN C 26  ? 0.8460 1.3404 0.9701 -0.6517 -0.0708 0.0671  26  GLN C C   
6841  O O   . GLN C 26  ? 0.8438 1.4120 0.9816 -0.6679 -0.0714 0.0856  26  GLN C O   
6842  C CB  . GLN C 26  ? 0.8635 1.2549 0.9730 -0.6298 -0.0669 0.0604  26  GLN C CB  
6843  C CG  . GLN C 26  ? 0.8680 1.2411 0.9800 -0.6058 -0.0560 0.0636  26  GLN C CG  
6844  C CD  . GLN C 26  ? 0.8971 1.3261 1.0239 -0.6186 -0.0533 0.0938  26  GLN C CD  
6845  O OE1 . GLN C 26  ? 0.9319 1.3926 1.0628 -0.6551 -0.0647 0.1145  26  GLN C OE1 
6846  N NE2 . GLN C 26  ? 0.8770 1.3203 1.0115 -0.5888 -0.0385 0.0970  26  GLN C NE2 
6847  N N   . ASN C 27  ? 0.8705 1.2954 0.9751 -0.6580 -0.0819 0.0456  27  ASN C N   
6848  C CA  . ASN C 27  ? 0.8920 1.3101 0.9868 -0.6899 -0.0989 0.0419  27  ASN C CA  
6849  C C   . ASN C 27  ? 0.8803 1.2361 0.9568 -0.6716 -0.1009 0.0103  27  ASN C C   
6850  O O   . ASN C 27  ? 0.8618 1.2441 0.9406 -0.6635 -0.0981 -0.0014 27  ASN C O   
6851  C CB  . ASN C 27  ? 0.8769 1.3868 0.9897 -0.6995 -0.0958 0.0556  27  ASN C CB  
6852  C CG  . ASN C 27  ? 0.9528 1.4609 1.0564 -0.7406 -0.1161 0.0581  27  ASN C CG  
6853  O OD1 . ASN C 27  ? 1.0190 1.5006 1.1134 -0.7788 -0.1340 0.0717  27  ASN C OD1 
6854  N ND2 . ASN C 27  ? 0.9889 1.5253 1.0942 -0.7339 -0.1142 0.0457  27  ASN C ND2 
6855  N N   . ILE C 28  ? 0.8808 1.1564 0.9389 -0.6635 -0.1053 -0.0032 28  ILE C N   
6856  C CA  . ILE C 28  ? 0.8703 1.0846 0.9083 -0.6464 -0.1085 -0.0326 28  ILE C CA  
6857  C C   . ILE C 28  ? 0.9198 1.0848 0.9342 -0.6801 -0.1321 -0.0392 28  ILE C C   
6858  O O   . ILE C 28  ? 0.9600 1.0993 0.9652 -0.7131 -0.1480 -0.0246 28  ILE C O   
6859  C CB  . ILE C 28  ? 0.8638 1.0182 0.8919 -0.6165 -0.1012 -0.0461 28  ILE C CB  
6860  C CG1 . ILE C 28  ? 0.9009 1.0284 0.9266 -0.6318 -0.1066 -0.0284 28  ILE C CG1 
6861  C CG2 . ILE C 28  ? 0.7864 0.9803 0.8319 -0.5767 -0.0792 -0.0511 28  ILE C CG2 
6862  C CD1 . ILE C 28  ? 0.9856 1.0372 0.9839 -0.6620 -0.1300 -0.0307 28  ILE C CD1 
6863  N N   . THR C 29  ? 0.9116 1.0634 0.9149 -0.6719 -0.1351 -0.0610 29  THR C N   
6864  C CA  . THR C 29  ? 0.9609 1.0675 0.9396 -0.7014 -0.1579 -0.0699 29  THR C CA  
6865  C C   . THR C 29  ? 0.9622 1.0244 0.9221 -0.6746 -0.1571 -0.1010 29  THR C C   
6866  O O   . THR C 29  ? 0.9123 0.9984 0.8837 -0.6386 -0.1387 -0.1120 29  THR C O   
6867  C CB  . THR C 29  ? 0.9568 1.1275 0.9466 -0.7306 -0.1648 -0.0577 29  THR C CB  
6868  O OG1 . THR C 29  ? 0.9001 1.1591 0.9217 -0.7235 -0.1476 -0.0369 29  THR C OG1 
6869  C CG2 . THR C 29  ? 1.0212 1.1625 0.9948 -0.7800 -0.1908 -0.0439 29  THR C CG2 
6870  N N   . GLU C 30  ? 1.0176 1.0153 0.9471 -0.6928 -0.1783 -0.1145 30  GLU C N   
6871  C CA  . GLU C 30  ? 1.0267 0.9870 0.9357 -0.6714 -0.1804 -0.1435 30  GLU C CA  
6872  C C   . GLU C 30  ? 1.0591 1.0214 0.9549 -0.7042 -0.1998 -0.1459 30  GLU C C   
6873  O O   . GLU C 30  ? 1.1068 1.0514 0.9928 -0.7437 -0.2192 -0.1317 30  GLU C O   
6874  C CB  . GLU C 30  ? 1.0778 0.9456 0.9556 -0.6574 -0.1892 -0.1606 30  GLU C CB  
6875  C CG  . GLU C 30  ? 1.0785 0.9248 0.9469 -0.6145 -0.1780 -0.1873 30  GLU C CG  
6876  C CD  . GLU C 30  ? 1.1304 0.9092 0.9808 -0.5916 -0.1772 -0.1962 30  GLU C CD  
6877  O OE1 . GLU C 30  ? 1.2033 0.9113 1.0241 -0.6089 -0.1973 -0.1993 30  GLU C OE1 
6878  O OE2 . GLU C 30  ? 1.1014 0.8974 0.9664 -0.5569 -0.1574 -0.1994 30  GLU C OE2 
6879  N N   . GLU C 31  ? 1.0344 1.0213 0.9306 -0.6893 -0.1951 -0.1625 31  GLU C N   
6880  C CA  . GLU C 31  ? 1.0750 1.0558 0.9542 -0.7168 -0.2143 -0.1695 31  GLU C CA  
6881  C C   . GLU C 31  ? 1.0937 1.0197 0.9448 -0.6896 -0.2177 -0.2019 31  GLU C C   
6882  O O   . GLU C 31  ? 1.0485 0.9932 0.9094 -0.6509 -0.1987 -0.2146 31  GLU C O   
6883  C CB  . GLU C 31  ? 1.0315 1.1061 0.9392 -0.7280 -0.2062 -0.1560 31  GLU C CB  
6884  C CG  . GLU C 31  ? 1.0818 1.1581 0.9743 -0.7390 -0.2187 -0.1716 31  GLU C CG  
6885  C CD  . GLU C 31  ? 1.0866 1.2515 1.0042 -0.7603 -0.2163 -0.1540 31  GLU C CD  
6886  O OE1 . GLU C 31  ? 1.1108 1.2814 1.0169 -0.7747 -0.2281 -0.1638 31  GLU C OE1 
6887  O OE2 . GLU C 31  ? 1.0648 1.2941 1.0122 -0.7614 -0.2026 -0.1307 31  GLU C OE2 
6888  N N   . PHE C 32  ? 1.1631 1.0208 0.9778 -0.7101 -0.2428 -0.2146 32  PHE C N   
6889  C CA  . PHE C 32  ? 1.1941 0.9896 0.9752 -0.6849 -0.2495 -0.2460 32  PHE C CA  
6890  C C   . PHE C 32  ? 1.1999 1.0237 0.9757 -0.6922 -0.2559 -0.2582 32  PHE C C   
6891  O O   . PHE C 32  ? 1.2221 1.0709 1.0003 -0.7309 -0.2700 -0.2455 32  PHE C O   
6892  C CB  . PHE C 32  ? 1.2768 0.9730 1.0162 -0.7002 -0.2747 -0.2539 32  PHE C CB  
6893  C CG  . PHE C 32  ? 1.3279 0.9579 1.0256 -0.6841 -0.2891 -0.2853 32  PHE C CG  
6894  C CD1 . PHE C 32  ? 1.3118 0.9275 1.0023 -0.6368 -0.2746 -0.3074 32  PHE C CD1 
6895  C CD2 . PHE C 32  ? 1.4156 0.9960 1.0790 -0.7167 -0.3185 -0.2922 32  PHE C CD2 
6896  C CE1 . PHE C 32  ? 1.3686 0.9256 1.0189 -0.6196 -0.2879 -0.3364 32  PHE C CE1 
6897  C CE2 . PHE C 32  ? 1.4765 0.9918 1.0973 -0.6997 -0.3330 -0.3226 32  PHE C CE2 
6898  C CZ  . PHE C 32  ? 1.4470 0.9525 1.0615 -0.6500 -0.3171 -0.3447 32  PHE C CZ  
6899  N N   . TYR C 33  ? 1.1835 1.0068 0.9526 -0.6554 -0.2457 -0.2816 33  TYR C N   
6900  C CA  . TYR C 33  ? 1.1882 1.0397 0.9521 -0.6582 -0.2503 -0.2945 33  TYR C CA  
6901  C C   . TYR C 33  ? 1.2589 1.0315 0.9762 -0.6473 -0.2685 -0.3244 33  TYR C C   
6902  O O   . TYR C 33  ? 1.2515 1.0109 0.9599 -0.6072 -0.2578 -0.3446 33  TYR C O   
6903  C CB  . TYR C 33  ? 1.1064 1.0346 0.9028 -0.6266 -0.2235 -0.2949 33  TYR C CB  
6904  C CG  . TYR C 33  ? 1.0565 1.0656 0.8948 -0.6383 -0.2082 -0.2669 33  TYR C CG  
6905  C CD1 . TYR C 33  ? 1.0243 1.0518 0.8857 -0.6181 -0.1891 -0.2545 33  TYR C CD1 
6906  C CD2 . TYR C 33  ? 1.0720 1.1402 0.9255 -0.6686 -0.2134 -0.2527 33  TYR C CD2 
6907  C CE1 . TYR C 33  ? 0.9789 1.0802 0.8761 -0.6258 -0.1754 -0.2297 33  TYR C CE1 
6908  C CE2 . TYR C 33  ? 1.0283 1.1738 0.9186 -0.6761 -0.1992 -0.2270 33  TYR C CE2 
6909  C CZ  . TYR C 33  ? 0.9786 1.1386 0.8895 -0.6537 -0.1804 -0.2162 33  TYR C CZ  
6910  O OH  . TYR C 33  ? 0.9385 1.1726 0.8824 -0.6584 -0.1671 -0.1921 33  TYR C OH  
6911  N N   . GLN C 34  ? 1.3320 1.0539 1.0187 -0.6833 -0.2970 -0.3264 34  GLN C N   
6912  C CA  . GLN C 34  ? 1.4108 1.0463 1.0466 -0.6763 -0.3190 -0.3543 34  GLN C CA  
6913  C C   . GLN C 34  ? 1.3955 1.0480 1.0217 -0.6463 -0.3131 -0.3795 34  GLN C C   
6914  O O   . GLN C 34  ? 1.4366 1.0289 1.0273 -0.6180 -0.3194 -0.4052 34  GLN C O   
6915  C CB  . GLN C 34  ? 1.4922 1.0843 1.1008 -0.7268 -0.3518 -0.3487 34  GLN C CB  
6916  C CG  . GLN C 34  ? 1.6048 1.0933 1.1543 -0.7230 -0.3791 -0.3764 34  GLN C CG  
6917  C CD  . GLN C 34  ? 1.7140 1.1447 1.2348 -0.7751 -0.4134 -0.3666 34  GLN C CD  
6918  O OE1 . GLN C 34  ? 1.7460 1.1977 1.2635 -0.8104 -0.4295 -0.3623 34  GLN C OE1 
6919  N NE2 . GLN C 34  ? 1.7725 1.1295 1.2715 -0.7809 -0.4256 -0.3622 34  GLN C NE2 
6920  N N   . SER C 35  ? 1.3372 1.0737 0.9946 -0.6516 -0.3008 -0.3714 35  SER C N   
6921  C CA  . SER C 35  ? 1.3249 1.0862 0.9754 -0.6297 -0.2967 -0.3922 35  SER C CA  
6922  C C   . SER C 35  ? 1.2589 1.0535 0.9281 -0.5798 -0.2688 -0.4004 35  SER C C   
6923  O O   . SER C 35  ? 1.2361 1.0648 0.9070 -0.5583 -0.2607 -0.4141 35  SER C O   
6924  C CB  . SER C 35  ? 1.2918 1.1319 0.9689 -0.6579 -0.2956 -0.3777 35  SER C CB  
6925  O OG  . SER C 35  ? 1.2190 1.1322 0.9430 -0.6587 -0.2734 -0.3516 35  SER C OG  
6926  N N   . THR C 36  ? 1.2272 1.0133 0.9105 -0.5625 -0.2547 -0.3909 36  THR C N   
6927  C CA  . THR C 36  ? 1.1635 0.9816 0.8666 -0.5187 -0.2289 -0.3946 36  THR C CA  
6928  C C   . THR C 36  ? 1.1809 0.9382 0.8697 -0.5009 -0.2281 -0.3969 36  THR C C   
6929  O O   . THR C 36  ? 1.1323 0.9092 0.8393 -0.4705 -0.2080 -0.3940 36  THR C O   
6930  C CB  . THR C 36  ? 1.0802 0.9863 0.8332 -0.5213 -0.2064 -0.3702 36  THR C CB  
6931  O OG1 . THR C 36  ? 1.0840 1.0467 0.8495 -0.5404 -0.2086 -0.3663 36  THR C OG1 
6932  C CG2 . THR C 36  ? 1.0202 0.9595 0.7928 -0.4794 -0.1819 -0.3729 36  THR C CG2 
6933  N N   . CYS C 37  ? 1.2550 0.9369 0.9103 -0.5212 -0.2512 -0.4012 37  CYS C N   
6934  C CA  . CYS C 37  ? 1.2831 0.9044 0.9240 -0.5089 -0.2527 -0.4009 37  CYS C CA  
6935  C C   . CYS C 37  ? 1.2061 0.8735 0.8863 -0.4903 -0.2265 -0.3830 37  CYS C C   
6936  O O   . CYS C 37  ? 1.2016 0.8495 0.8768 -0.4547 -0.2155 -0.3916 37  CYS C O   
6937  C CB  . CYS C 37  ? 1.3371 0.8927 0.9352 -0.4735 -0.2602 -0.4300 37  CYS C CB  
6938  S SG  . CYS C 37  ? 1.4373 0.8878 0.9965 -0.4758 -0.2790 -0.4334 37  CYS C SG  
6939  N N   . SER C 38  ? 1.1497 0.8798 0.8679 -0.5137 -0.2170 -0.3581 38  SER C N   
6940  C CA  . SER C 38  ? 1.0733 0.8493 0.8283 -0.4982 -0.1934 -0.3403 38  SER C CA  
6941  C C   . SER C 38  ? 1.0544 0.8535 0.8320 -0.5332 -0.1951 -0.3126 38  SER C C   
6942  O O   . SER C 38  ? 1.0766 0.8871 0.8533 -0.5700 -0.2094 -0.3036 38  SER C O   
6943  C CB  . SER C 38  ? 1.0031 0.8552 0.7873 -0.4750 -0.1720 -0.3405 38  SER C CB  
6944  O OG  . SER C 38  ? 0.9992 0.8965 0.7913 -0.4967 -0.1770 -0.3383 38  SER C OG  
6945  N N   . ALA C 39  ? 1.0122 0.8212 0.8101 -0.5215 -0.1806 -0.2984 39  ALA C N   
6946  C CA  . ALA C 39  ? 1.0000 0.8278 0.8175 -0.5504 -0.1813 -0.2720 39  ALA C CA  
6947  C C   . ALA C 39  ? 0.9220 0.8191 0.7790 -0.5345 -0.1568 -0.2552 39  ALA C C   
6948  O O   . ALA C 39  ? 0.8933 0.7919 0.7566 -0.5002 -0.1413 -0.2618 39  ALA C O   
6949  C CB  . ALA C 39  ? 1.0509 0.8047 0.8461 -0.5558 -0.1929 -0.2705 39  ALA C CB  
6950  N N   . VAL C 40  ? 0.8927 0.8470 0.7750 -0.5593 -0.1542 -0.2329 40  VAL C N   
6951  C CA  . VAL C 40  ? 0.8233 0.8415 0.7403 -0.5445 -0.1327 -0.2164 40  VAL C CA  
6952  C C   . VAL C 40  ? 0.8236 0.8500 0.7540 -0.5641 -0.1327 -0.1921 40  VAL C C   
6953  O O   . VAL C 40  ? 0.8531 0.8870 0.7828 -0.6002 -0.1461 -0.1778 40  VAL C O   
6954  C CB  . VAL C 40  ? 0.7773 0.8725 0.7162 -0.5478 -0.1249 -0.2106 40  VAL C CB  
6955  C CG1 . VAL C 40  ? 0.7198 0.8766 0.6906 -0.5362 -0.1061 -0.1917 40  VAL C CG1 
6956  C CG2 . VAL C 40  ? 0.7666 0.8644 0.6983 -0.5219 -0.1197 -0.2321 40  VAL C CG2 
6957  N N   . SER C 41  ? 0.7940 0.8222 0.7370 -0.5407 -0.1177 -0.1863 41  SER C N   
6958  C CA  . SER C 41  ? 0.7877 0.8352 0.7471 -0.5546 -0.1144 -0.1622 41  SER C CA  
6959  C C   . SER C 41  ? 0.7292 0.8623 0.7202 -0.5497 -0.0987 -0.1463 41  SER C C   
6960  O O   . SER C 41  ? 0.6846 0.8458 0.6866 -0.5200 -0.0836 -0.1537 41  SER C O   
6961  C CB  . SER C 41  ? 0.7876 0.7929 0.7431 -0.5314 -0.1068 -0.1640 41  SER C CB  
6962  O OG  . SER C 41  ? 0.8428 0.7749 0.7683 -0.5210 -0.1167 -0.1852 41  SER C OG  
6963  N N   . LYS C 42  ? 0.7330 0.9081 0.7373 -0.5782 -0.1028 -0.1239 42  LYS C N   
6964  C CA  . LYS C 42  ? 0.6894 0.9488 0.7202 -0.5746 -0.0902 -0.1093 42  LYS C CA  
6965  C C   . LYS C 42  ? 0.6666 0.9610 0.7157 -0.5783 -0.0826 -0.0849 42  LYS C C   
6966  O O   . LYS C 42  ? 0.6979 0.9569 0.7401 -0.5950 -0.0906 -0.0754 42  LYS C O   
6967  C CB  . LYS C 42  ? 0.7098 1.0074 0.7417 -0.6048 -0.1018 -0.1039 42  LYS C CB  
6968  C CG  . LYS C 42  ? 0.7613 1.0275 0.7736 -0.6073 -0.1124 -0.1264 42  LYS C CG  
6969  C CD  . LYS C 42  ? 0.8289 1.1280 0.8405 -0.6452 -0.1276 -0.1175 42  LYS C CD  
6970  C CE  . LYS C 42  ? 0.8701 1.1417 0.8615 -0.6465 -0.1382 -0.1408 42  LYS C CE  
6971  N NZ  . LYS C 42  ? 0.8883 1.2128 0.8857 -0.6749 -0.1472 -0.1322 42  LYS C NZ  
6972  N N   . GLY C 43  ? 0.6148 0.9784 0.6856 -0.5620 -0.0677 -0.0747 43  GLY C N   
6973  C CA  . GLY C 43  ? 0.5926 1.0033 0.6808 -0.5662 -0.0609 -0.0502 43  GLY C CA  
6974  C C   . GLY C 43  ? 0.5642 0.9622 0.6575 -0.5352 -0.0468 -0.0500 43  GLY C C   
6975  O O   . GLY C 43  ? 0.5648 0.9723 0.6650 -0.5402 -0.0446 -0.0329 43  GLY C O   
6976  N N   . TYR C 44  ? 0.5418 0.9194 0.6315 -0.5035 -0.0377 -0.0686 44  TYR C N   
6977  C CA  . TYR C 44  ? 0.5095 0.8739 0.6030 -0.4728 -0.0249 -0.0702 44  TYR C CA  
6978  C C   . TYR C 44  ? 0.4628 0.8872 0.5711 -0.4486 -0.0114 -0.0657 44  TYR C C   
6979  O O   . TYR C 44  ? 0.4591 0.9223 0.5716 -0.4496 -0.0112 -0.0682 44  TYR C O   
6980  C CB  . TYR C 44  ? 0.5164 0.8210 0.5954 -0.4535 -0.0246 -0.0927 44  TYR C CB  
6981  C CG  . TYR C 44  ? 0.5615 0.7983 0.6223 -0.4691 -0.0369 -0.0989 44  TYR C CG  
6982  C CD1 . TYR C 44  ? 0.6053 0.8072 0.6488 -0.4836 -0.0500 -0.1133 44  TYR C CD1 
6983  C CD2 . TYR C 44  ? 0.5645 0.7696 0.6232 -0.4681 -0.0363 -0.0908 44  TYR C CD2 
6984  C CE1 . TYR C 44  ? 0.6589 0.7932 0.6816 -0.4959 -0.0628 -0.1201 44  TYR C CE1 
6985  C CE2 . TYR C 44  ? 0.6177 0.7569 0.6572 -0.4808 -0.0483 -0.0967 44  TYR C CE2 
6986  C CZ  . TYR C 44  ? 0.6700 0.7725 0.6905 -0.4943 -0.0620 -0.1116 44  TYR C CZ  
6987  O OH  . TYR C 44  ? 0.7334 0.7658 0.7309 -0.5051 -0.0756 -0.1188 44  TYR C OH  
6988  N N   . LEU C 45  ? 0.4316 0.8612 0.5459 -0.4262 -0.0007 -0.0595 45  LEU C N   
6989  C CA  . LEU C 45  ? 0.3861 0.8670 0.5108 -0.4013 0.0108  -0.0551 45  LEU C CA  
6990  C C   . LEU C 45  ? 0.3609 0.8151 0.4822 -0.3683 0.0196  -0.0669 45  LEU C C   
6991  O O   . LEU C 45  ? 0.3643 0.7829 0.4823 -0.3590 0.0223  -0.0667 45  LEU C O   
6992  C CB  . LEU C 45  ? 0.3793 0.9100 0.5150 -0.4048 0.0147  -0.0330 45  LEU C CB  
6993  C CG  . LEU C 45  ? 0.3938 0.9666 0.5354 -0.4377 0.0063  -0.0179 45  LEU C CG  
6994  C CD1 . LEU C 45  ? 0.3982 1.0052 0.5483 -0.4475 0.0076  0.0053  45  LEU C CD1 
6995  C CD2 . LEU C 45  ? 0.3799 1.0080 0.5275 -0.4323 0.0088  -0.0188 45  LEU C CD2 
6996  N N   . SER C 46  ? 0.3329 0.8071 0.4551 -0.3517 0.0237  -0.0757 46  SER C N   
6997  C CA  . SER C 46  ? 0.3092 0.7603 0.4272 -0.3239 0.0298  -0.0874 46  SER C CA  
6998  C C   . SER C 46  ? 0.2912 0.7505 0.4120 -0.3002 0.0381  -0.0793 46  SER C C   
6999  O O   . SER C 46  ? 0.2822 0.7808 0.4090 -0.2980 0.0414  -0.0650 46  SER C O   
7000  C CB  . SER C 46  ? 0.2881 0.7686 0.4074 -0.3144 0.0314  -0.0944 46  SER C CB  
7001  O OG  . SER C 46  ? 0.2679 0.8021 0.3947 -0.3068 0.0360  -0.0815 46  SER C OG  
7002  N N   . ALA C 47  ? 0.2797 0.7026 0.3950 -0.2813 0.0411  -0.0891 47  ALA C N   
7003  C CA  . ALA C 47  ? 0.2551 0.6820 0.3700 -0.2565 0.0474  -0.0853 47  ALA C CA  
7004  C C   . ALA C 47  ? 0.2440 0.6391 0.3531 -0.2435 0.0475  -0.0993 47  ALA C C   
7005  O O   . ALA C 47  ? 0.2642 0.6203 0.3690 -0.2505 0.0447  -0.1076 47  ALA C O   
7006  C CB  . ALA C 47  ? 0.2650 0.6712 0.3797 -0.2570 0.0488  -0.0771 47  ALA C CB  
7007  N N   . LEU C 48  ? 0.2171 0.6295 0.3251 -0.2252 0.0500  -0.1018 48  LEU C N   
7008  C CA  . LEU C 48  ? 0.2045 0.5944 0.3079 -0.2153 0.0494  -0.1137 48  LEU C CA  
7009  C C   . LEU C 48  ? 0.1863 0.5674 0.2856 -0.1923 0.0519  -0.1121 48  LEU C C   
7010  O O   . LEU C 48  ? 0.1756 0.5824 0.2736 -0.1800 0.0528  -0.1076 48  LEU C O   
7011  C CB  . LEU C 48  ? 0.1969 0.6131 0.3015 -0.2199 0.0474  -0.1199 48  LEU C CB  
7012  C CG  . LEU C 48  ? 0.1998 0.6367 0.3078 -0.2429 0.0434  -0.1204 48  LEU C CG  
7013  C CD1 . LEU C 48  ? 0.1793 0.6337 0.2867 -0.2437 0.0415  -0.1291 48  LEU C CD1 
7014  C CD2 . LEU C 48  ? 0.2361 0.6383 0.3410 -0.2621 0.0388  -0.1250 48  LEU C CD2 
7015  N N   . ARG C 49  ? 0.1877 0.5319 0.2836 -0.1866 0.0521  -0.1157 49  ARG C N   
7016  C CA  . ARG C 49  ? 0.1791 0.5110 0.2702 -0.1672 0.0526  -0.1140 49  ARG C CA  
7017  C C   . ARG C 49  ? 0.1697 0.5185 0.2582 -0.1576 0.0509  -0.1168 49  ARG C C   
7018  O O   . ARG C 49  ? 0.1714 0.5236 0.2614 -0.1635 0.0498  -0.1247 49  ARG C O   
7019  C CB  . ARG C 49  ? 0.1822 0.4764 0.2709 -0.1650 0.0524  -0.1187 49  ARG C CB  
7020  C CG  . ARG C 49  ? 0.1656 0.4420 0.2504 -0.1518 0.0529  -0.1122 49  ARG C CG  
7021  C CD  . ARG C 49  ? 0.1542 0.4076 0.2365 -0.1456 0.0517  -0.1161 49  ARG C CD  
7022  N NE  . ARG C 49  ? 0.1915 0.4572 0.2702 -0.1350 0.0489  -0.1142 49  ARG C NE  
7023  C CZ  . ARG C 49  ? 0.2292 0.5007 0.3081 -0.1345 0.0472  -0.1192 49  ARG C CZ  
7024  N NH1 . ARG C 49  ? 0.2360 0.5014 0.3178 -0.1419 0.0485  -0.1275 49  ARG C NH1 
7025  N NH2 . ARG C 49  ? 0.2414 0.5240 0.3162 -0.1259 0.0436  -0.1159 49  ARG C NH2 
7026  N N   . THR C 50  ? 0.1638 0.5217 0.2470 -0.1422 0.0501  -0.1104 50  THR C N   
7027  C CA  . THR C 50  ? 0.1569 0.5242 0.2354 -0.1321 0.0471  -0.1117 50  THR C CA  
7028  C C   . THR C 50  ? 0.1624 0.5104 0.2312 -0.1159 0.0439  -0.1062 50  THR C C   
7029  O O   . THR C 50  ? 0.1649 0.5167 0.2269 -0.1062 0.0397  -0.1050 50  THR C O   
7030  C CB  . THR C 50  ? 0.1483 0.5533 0.2266 -0.1295 0.0470  -0.1097 50  THR C CB  
7031  O OG1 . THR C 50  ? 0.1468 0.5682 0.2247 -0.1270 0.0491  -0.1026 50  THR C OG1 
7032  C CG2 . THR C 50  ? 0.1525 0.5763 0.2384 -0.1449 0.0479  -0.1162 50  THR C CG2 
7033  N N   . GLY C 51  ? 0.1673 0.4934 0.2342 -0.1132 0.0446  -0.1024 51  GLY C N   
7034  C CA  . GLY C 51  ? 0.1746 0.4783 0.2307 -0.0992 0.0399  -0.0976 51  GLY C CA  
7035  C C   . GLY C 51  ? 0.1822 0.4605 0.2375 -0.0986 0.0410  -0.0944 51  GLY C C   
7036  O O   . GLY C 51  ? 0.1866 0.4636 0.2499 -0.1090 0.0458  -0.0957 51  GLY C O   
7037  N N   . TRP C 52  ? 0.1875 0.4445 0.2320 -0.0872 0.0357  -0.0898 52  TRP C N   
7038  C CA  . TRP C 52  ? 0.1921 0.4259 0.2352 -0.0858 0.0363  -0.0864 52  TRP C CA  
7039  C C   . TRP C 52  ? 0.2001 0.4264 0.2291 -0.0707 0.0323  -0.0807 52  TRP C C   
7040  O O   . TRP C 52  ? 0.2065 0.4348 0.2229 -0.0589 0.0262  -0.0791 52  TRP C O   
7041  C CB  . TRP C 52  ? 0.1975 0.4083 0.2408 -0.0881 0.0330  -0.0864 52  TRP C CB  
7042  C CG  . TRP C 52  ? 0.2062 0.4215 0.2610 -0.1000 0.0369  -0.0926 52  TRP C CG  
7043  C CD1 . TRP C 52  ? 0.2165 0.4404 0.2733 -0.1024 0.0347  -0.0955 52  TRP C CD1 
7044  C CD2 . TRP C 52  ? 0.2112 0.4209 0.2750 -0.1096 0.0428  -0.0968 52  TRP C CD2 
7045  N NE1 . TRP C 52  ? 0.2109 0.4360 0.2765 -0.1114 0.0392  -0.1021 52  TRP C NE1 
7046  C CE2 . TRP C 52  ? 0.2096 0.4237 0.2787 -0.1158 0.0437  -0.1034 52  TRP C CE2 
7047  C CE3 . TRP C 52  ? 0.2153 0.4157 0.2816 -0.1131 0.0467  -0.0953 52  TRP C CE3 
7048  C CZ2 . TRP C 52  ? 0.2131 0.4195 0.2878 -0.1240 0.0477  -0.1096 52  TRP C CZ2 
7049  C CZ3 . TRP C 52  ? 0.2179 0.4095 0.2907 -0.1229 0.0504  -0.1004 52  TRP C CZ3 
7050  C CH2 . TRP C 52  ? 0.2209 0.4139 0.2967 -0.1276 0.0506  -0.1081 52  TRP C CH2 
7051  N N   . TYR C 53  ? 0.2049 0.4205 0.2345 -0.0702 0.0350  -0.0776 53  TYR C N   
7052  C CA  . TYR C 53  ? 0.2219 0.4291 0.2370 -0.0550 0.0313  -0.0727 53  TYR C CA  
7053  C C   . TYR C 53  ? 0.2336 0.4086 0.2452 -0.0546 0.0282  -0.0700 53  TYR C C   
7054  O O   . TYR C 53  ? 0.2365 0.4055 0.2583 -0.0635 0.0337  -0.0695 53  TYR C O   
7055  C CB  . TYR C 53  ? 0.2249 0.4563 0.2439 -0.0541 0.0379  -0.0700 53  TYR C CB  
7056  C CG  . TYR C 53  ? 0.2435 0.4710 0.2476 -0.0368 0.0354  -0.0651 53  TYR C CG  
7057  C CD1 . TYR C 53  ? 0.2690 0.5104 0.2576 -0.0188 0.0314  -0.0642 53  TYR C CD1 
7058  C CD2 . TYR C 53  ? 0.2565 0.4671 0.2607 -0.0370 0.0369  -0.0615 53  TYR C CD2 
7059  C CE1 . TYR C 53  ? 0.2993 0.5363 0.2712 -0.0001 0.0285  -0.0607 53  TYR C CE1 
7060  C CE2 . TYR C 53  ? 0.2794 0.4869 0.2686 -0.0201 0.0344  -0.0574 53  TYR C CE2 
7061  C CZ  . TYR C 53  ? 0.2980 0.5183 0.2704 -0.0011 0.0300  -0.0574 53  TYR C CZ  
7062  O OH  . TYR C 53  ? 0.3178 0.5347 0.2724 0.0184  0.0270  -0.0544 53  TYR C OH  
7063  N N   . THR C 54  ? 0.2465 0.3999 0.2425 -0.0449 0.0184  -0.0677 54  THR C N   
7064  C CA  . THR C 54  ? 0.2586 0.3819 0.2479 -0.0435 0.0127  -0.0639 54  THR C CA  
7065  C C   . THR C 54  ? 0.2715 0.3871 0.2502 -0.0320 0.0125  -0.0608 54  THR C C   
7066  O O   . THR C 54  ? 0.2840 0.4109 0.2510 -0.0186 0.0112  -0.0609 54  THR C O   
7067  C CB  . THR C 54  ? 0.2738 0.3794 0.2459 -0.0367 -0.0001 -0.0618 54  THR C CB  
7068  O OG1 . THR C 54  ? 0.2765 0.3843 0.2587 -0.0488 -0.0011 -0.0620 54  THR C OG1 
7069  C CG2 . THR C 54  ? 0.3079 0.3806 0.2616 -0.0286 -0.0109 -0.0567 54  THR C CG2 
7070  N N   . SER C 55  ? 0.2734 0.3717 0.2550 -0.0354 0.0136  -0.0578 55  SER C N   
7071  C CA  . SER C 55  ? 0.2894 0.3729 0.2559 -0.0226 0.0097  -0.0543 55  SER C CA  
7072  C C   . SER C 55  ? 0.2992 0.3563 0.2651 -0.0271 0.0059  -0.0506 55  SER C C   
7073  O O   . SER C 55  ? 0.2942 0.3517 0.2765 -0.0398 0.0117  -0.0503 55  SER C O   
7074  C CB  . SER C 55  ? 0.2861 0.3907 0.2592 -0.0203 0.0193  -0.0531 55  SER C CB  
7075  O OG  . SER C 55  ? 0.3024 0.3919 0.2610 -0.0079 0.0154  -0.0497 55  SER C OG  
7076  N N   . VAL C 56  ? 0.3204 0.3546 0.2660 -0.0154 -0.0040 -0.0478 56  VAL C N   
7077  C CA  . VAL C 56  ? 0.3275 0.3352 0.2690 -0.0198 -0.0112 -0.0433 56  VAL C CA  
7078  C C   . VAL C 56  ? 0.3328 0.3317 0.2701 -0.0137 -0.0091 -0.0405 56  VAL C C   
7079  O O   . VAL C 56  ? 0.3535 0.3418 0.2703 0.0017  -0.0155 -0.0404 56  VAL C O   
7080  C CB  . VAL C 56  ? 0.3512 0.3334 0.2691 -0.0130 -0.0275 -0.0415 56  VAL C CB  
7081  C CG1 . VAL C 56  ? 0.3504 0.3138 0.2702 -0.0245 -0.0349 -0.0356 56  VAL C CG1 
7082  C CG2 . VAL C 56  ? 0.3641 0.3565 0.2778 -0.0109 -0.0308 -0.0448 56  VAL C CG2 
7083  N N   . ILE C 57  ? 0.3165 0.3184 0.2714 -0.0244 -0.0010 -0.0384 57  ILE C N   
7084  C CA  . ILE C 57  ? 0.3168 0.3139 0.2708 -0.0199 0.0027  -0.0352 57  ILE C CA  
7085  C C   . ILE C 57  ? 0.3257 0.2972 0.2722 -0.0215 -0.0060 -0.0304 57  ILE C C   
7086  O O   . ILE C 57  ? 0.3202 0.2870 0.2745 -0.0322 -0.0086 -0.0284 57  ILE C O   
7087  C CB  . ILE C 57  ? 0.2980 0.3131 0.2736 -0.0296 0.0163  -0.0354 57  ILE C CB  
7088  C CG1 . ILE C 57  ? 0.2983 0.3397 0.2778 -0.0278 0.0225  -0.0388 57  ILE C CG1 
7089  C CG2 . ILE C 57  ? 0.3015 0.3115 0.2770 -0.0263 0.0199  -0.0308 57  ILE C CG2 
7090  C CD1 . ILE C 57  ? 0.3075 0.3653 0.3076 -0.0419 0.0327  -0.0404 57  ILE C CD1 
7091  N N   . THR C 58  ? 0.3408 0.2981 0.2713 -0.0105 -0.0111 -0.0280 58  THR C N   
7092  C CA  . THR C 58  ? 0.3558 0.2872 0.2755 -0.0117 -0.0218 -0.0230 58  THR C CA  
7093  C C   . THR C 58  ? 0.3573 0.2880 0.2795 -0.0080 -0.0161 -0.0198 58  THR C C   
7094  O O   . THR C 58  ? 0.3663 0.3054 0.2824 0.0032  -0.0120 -0.0212 58  THR C O   
7095  C CB  . THR C 58  ? 0.3789 0.2858 0.2692 -0.0008 -0.0387 -0.0236 58  THR C CB  
7096  O OG1 . THR C 58  ? 0.3943 0.3092 0.2796 0.0032  -0.0404 -0.0284 58  THR C OG1 
7097  C CG2 . THR C 58  ? 0.3870 0.2714 0.2706 -0.0107 -0.0520 -0.0180 58  THR C CG2 
7098  N N   . ILE C 59  ? 0.3602 0.2839 0.2919 -0.0171 -0.0154 -0.0147 59  ILE C N   
7099  C CA  . ILE C 59  ? 0.3690 0.2929 0.3054 -0.0148 -0.0090 -0.0109 59  ILE C CA  
7100  C C   . ILE C 59  ? 0.3950 0.2971 0.3200 -0.0146 -0.0196 -0.0051 59  ILE C C   
7101  O O   . ILE C 59  ? 0.3965 0.2931 0.3270 -0.0251 -0.0244 -0.0008 59  ILE C O   
7102  C CB  . ILE C 59  ? 0.3435 0.2829 0.3048 -0.0252 0.0048  -0.0100 59  ILE C CB  
7103  C CG1 . ILE C 59  ? 0.3337 0.2937 0.3046 -0.0262 0.0142  -0.0150 59  ILE C CG1 
7104  C CG2 . ILE C 59  ? 0.3394 0.2766 0.3045 -0.0231 0.0102  -0.0052 59  ILE C CG2 
7105  C CD1 . ILE C 59  ? 0.3423 0.3128 0.3320 -0.0341 0.0265  -0.0140 59  ILE C CD1 
7106  N N   . GLU C 60  ? 0.4214 0.3133 0.3295 -0.0025 -0.0237 -0.0044 60  GLU C N   
7107  C CA  . GLU C 60  ? 0.4527 0.3239 0.3482 -0.0019 -0.0341 0.0009  60  GLU C CA  
7108  C C   . GLU C 60  ? 0.4440 0.3251 0.3599 -0.0091 -0.0232 0.0066  60  GLU C C   
7109  O O   . GLU C 60  ? 0.4382 0.3364 0.3688 -0.0082 -0.0094 0.0059  60  GLU C O   
7110  C CB  . GLU C 60  ? 0.4781 0.3365 0.3477 0.0157  -0.0413 -0.0015 60  GLU C CB  
7111  C CG  . GLU C 60  ? 0.5401 0.3770 0.3812 0.0249  -0.0575 -0.0064 60  GLU C CG  
7112  C CD  . GLU C 60  ? 0.6338 0.4464 0.4420 0.0424  -0.0704 -0.0082 60  GLU C CD  
7113  O OE1 . GLU C 60  ? 0.6620 0.4845 0.4699 0.0525  -0.0631 -0.0075 60  GLU C OE1 
7114  O OE2 . GLU C 60  ? 0.6811 0.4628 0.4616 0.0464  -0.0892 -0.0101 60  GLU C OE2 
7115  N N   . LEU C 61  ? 0.4489 0.3201 0.3656 -0.0168 -0.0299 0.0131  61  LEU C N   
7116  C CA  . LEU C 61  ? 0.4420 0.3202 0.3738 -0.0204 -0.0212 0.0189  61  LEU C CA  
7117  C C   . LEU C 61  ? 0.4638 0.3313 0.3801 -0.0097 -0.0249 0.0209  61  LEU C C   
7118  O O   . LEU C 61  ? 0.4829 0.3328 0.3752 -0.0024 -0.0383 0.0191  61  LEU C O   
7119  C CB  . LEU C 61  ? 0.4393 0.3155 0.3766 -0.0315 -0.0278 0.0260  61  LEU C CB  
7120  C CG  . LEU C 61  ? 0.4338 0.3101 0.3764 -0.0327 -0.0263 0.0340  61  LEU C CG  
7121  C CD1 . LEU C 61  ? 0.4215 0.3148 0.3871 -0.0352 -0.0105 0.0345  61  LEU C CD1 
7122  C CD2 . LEU C 61  ? 0.4402 0.3105 0.3765 -0.0418 -0.0404 0.0421  61  LEU C CD2 
7123  N N   . SER C 62  ? 0.4667 0.3431 0.3945 -0.0079 -0.0141 0.0246  62  SER C N   
7124  C CA  . SER C 62  ? 0.4921 0.3603 0.4061 0.0017  -0.0176 0.0278  62  SER C CA  
7125  C C   . SER C 62  ? 0.5078 0.3688 0.4241 -0.0048 -0.0227 0.0356  62  SER C C   
7126  O O   . SER C 62  ? 0.4964 0.3683 0.4316 -0.0096 -0.0123 0.0403  62  SER C O   
7127  C CB  . SER C 62  ? 0.4818 0.3659 0.4062 0.0072  -0.0033 0.0287  62  SER C CB  
7128  O OG  . SER C 62  ? 0.4863 0.3807 0.4066 0.0135  -0.0001 0.0227  62  SER C OG  
7129  N N   . ASN C 63  ? 0.5422 0.3842 0.4382 -0.0050 -0.0396 0.0375  63  ASN C N   
7130  C CA  . ASN C 63  ? 0.5578 0.3967 0.4573 -0.0149 -0.0466 0.0462  63  ASN C CA  
7131  C C   . ASN C 63  ? 0.5752 0.4120 0.4713 -0.0100 -0.0461 0.0520  63  ASN C C   
7132  O O   . ASN C 63  ? 0.5931 0.4212 0.4731 0.0018  -0.0483 0.0492  63  ASN C O   
7133  C CB  . ASN C 63  ? 0.5771 0.3975 0.4580 -0.0221 -0.0666 0.0479  63  ASN C CB  
7134  C CG  . ASN C 63  ? 0.5795 0.4111 0.4749 -0.0381 -0.0698 0.0573  63  ASN C CG  
7135  O OD1 . ASN C 63  ? 0.5695 0.4145 0.4788 -0.0411 -0.0637 0.0647  63  ASN C OD1 
7136  N ND2 . ASN C 63  ? 0.5875 0.4162 0.4795 -0.0476 -0.0795 0.0577  63  ASN C ND2 
7137  N N   . ILE C 64  ? 0.5832 0.4299 0.4939 -0.0177 -0.0430 0.0605  64  ILE C N   
7138  C CA  . ILE C 64  ? 0.6090 0.4547 0.5170 -0.0140 -0.0434 0.0672  64  ILE C CA  
7139  C C   . ILE C 64  ? 0.6519 0.4826 0.5415 -0.0198 -0.0627 0.0730  64  ILE C C   
7140  O O   . ILE C 64  ? 0.6562 0.4915 0.5509 -0.0324 -0.0700 0.0790  64  ILE C O   
7141  C CB  . ILE C 64  ? 0.5844 0.4484 0.5156 -0.0186 -0.0319 0.0745  64  ILE C CB  
7142  C CG1 . ILE C 64  ? 0.5609 0.4370 0.5108 -0.0164 -0.0147 0.0695  64  ILE C CG1 
7143  C CG2 . ILE C 64  ? 0.5988 0.4620 0.5265 -0.0131 -0.0314 0.0809  64  ILE C CG2 
7144  C CD1 . ILE C 64  ? 0.5446 0.4340 0.5137 -0.0181 -0.0037 0.0751  64  ILE C CD1 
7145  N N   . LYS C 65  ? 0.6992 0.5135 0.5671 -0.0113 -0.0716 0.0722  65  LYS C N   
7146  C CA  . LYS C 65  ? 0.7446 0.5448 0.5957 -0.0181 -0.0900 0.0797  65  LYS C CA  
7147  C C   . LYS C 65  ? 0.7494 0.5654 0.6137 -0.0184 -0.0827 0.0894  65  LYS C C   
7148  O O   . LYS C 65  ? 0.7557 0.5700 0.6142 -0.0068 -0.0780 0.0887  65  LYS C O   
7149  C CB  . LYS C 65  ? 0.7768 0.5449 0.5916 -0.0100 -0.1087 0.0734  65  LYS C CB  
7150  C CG  . LYS C 65  ? 0.7982 0.5620 0.6016 0.0101  -0.1009 0.0624  65  LYS C CG  
7151  C CD  . LYS C 65  ? 0.8051 0.5910 0.6252 0.0195  -0.0820 0.0650  65  LYS C CD  
7152  C CE  . LYS C 65  ? 0.8244 0.6063 0.6256 0.0397  -0.0800 0.0579  65  LYS C CE  
7153  N NZ  . LYS C 65  ? 0.8166 0.6114 0.6238 0.0463  -0.0713 0.0640  65  LYS C NZ  
7154  N N   . GLU C 66  ? 0.7484 0.5824 0.6308 -0.0308 -0.0814 0.0988  66  GLU C N   
7155  C CA  . GLU C 66  ? 0.7509 0.6056 0.6506 -0.0311 -0.0721 0.1086  66  GLU C CA  
7156  C C   . GLU C 66  ? 0.7732 0.6203 0.6578 -0.0301 -0.0832 0.1155  66  GLU C C   
7157  O O   . GLU C 66  ? 0.7981 0.6284 0.6619 -0.0380 -0.1033 0.1181  66  GLU C O   
7158  C CB  . GLU C 66  ? 0.7366 0.6139 0.6551 -0.0431 -0.0707 0.1167  66  GLU C CB  
7159  C CG  . GLU C 66  ? 0.7560 0.6544 0.6850 -0.0472 -0.0705 0.1301  66  GLU C CG  
7160  C CD  . GLU C 66  ? 0.7948 0.7163 0.7355 -0.0607 -0.0754 0.1392  66  GLU C CD  
7161  O OE1 . GLU C 66  ? 0.8166 0.7644 0.7707 -0.0621 -0.0716 0.1505  66  GLU C OE1 
7162  O OE2 . GLU C 66  ? 0.7953 0.7112 0.7319 -0.0691 -0.0829 0.1358  66  GLU C OE2 
7163  N N   . ASN C 67  ? 0.7730 0.6307 0.6667 -0.0210 -0.0711 0.1189  67  ASN C N   
7164  C CA  . ASN C 67  ? 0.7938 0.6435 0.6714 -0.0182 -0.0811 0.1241  67  ASN C CA  
7165  C C   . ASN C 67  ? 0.7897 0.6596 0.6790 -0.0236 -0.0806 0.1376  67  ASN C C   
7166  O O   . ASN C 67  ? 0.7859 0.6650 0.6821 -0.0143 -0.0702 0.1414  67  ASN C O   
7167  C CB  . ASN C 67  ? 0.8025 0.6403 0.6670 -0.0021 -0.0762 0.1167  67  ASN C CB  
7168  C CG  . ASN C 67  ? 0.8299 0.6392 0.6631 0.0018  -0.0932 0.1075  67  ASN C CG  
7169  O OD1 . ASN C 67  ? 0.8535 0.6456 0.6645 -0.0028 -0.1124 0.1101  67  ASN C OD1 
7170  N ND2 . ASN C 67  ? 0.8209 0.6241 0.6507 0.0101  -0.0874 0.0968  67  ASN C ND2 
7171  N N   . LYS C 68  ? 0.7882 0.6669 0.6800 -0.0387 -0.0920 0.1455  68  LYS C N   
7172  C CA  . LYS C 68  ? 0.7917 0.6871 0.6856 -0.0484 -0.1011 0.1600  68  LYS C CA  
7173  C C   . LYS C 68  ? 0.7972 0.6909 0.6846 -0.0387 -0.0994 0.1631  68  LYS C C   
7174  O O   . LYS C 68  ? 0.8223 0.6950 0.6853 -0.0395 -0.1150 0.1621  68  LYS C O   
7175  C CB  . LYS C 68  ? 0.8178 0.6985 0.6914 -0.0657 -0.1266 0.1643  68  LYS C CB  
7176  C CG  . LYS C 68  ? 0.8222 0.6897 0.6909 -0.0736 -0.1332 0.1575  68  LYS C CG  
7177  C CD  . LYS C 68  ? 0.8616 0.6909 0.6957 -0.0821 -0.1599 0.1543  68  LYS C CD  
7178  C CE  . LYS C 68  ? 0.8845 0.7040 0.6995 -0.0871 -0.1768 0.1625  68  LYS C CE  
7179  N NZ  . LYS C 68  ? 0.9246 0.7055 0.7044 -0.0984 -0.2060 0.1615  68  LYS C NZ  
7180  N N   . CYS C 69  ? 0.7736 0.6872 0.6812 -0.0284 -0.0802 0.1662  69  CYS C N   
7181  C CA  . CYS C 69  ? 0.7731 0.6925 0.6801 -0.0199 -0.0760 0.1721  69  CYS C CA  
7182  C C   . CYS C 69  ? 0.7648 0.7176 0.6945 -0.0225 -0.0678 0.1848  69  CYS C C   
7183  O O   . CYS C 69  ? 0.7567 0.7250 0.6960 -0.0322 -0.0704 0.1887  69  CYS C O   
7184  C CB  . CYS C 69  ? 0.7554 0.6678 0.6672 -0.0040 -0.0586 0.1639  69  CYS C CB  
7185  S SG  . CYS C 69  ? 0.7294 0.6663 0.6717 0.0010  -0.0370 0.1686  69  CYS C SG  
7186  N N   . ASN C 70  ? 0.7693 0.7350 0.7070 -0.0126 -0.0580 0.1916  70  ASN C N   
7187  C CA  . ASN C 70  ? 0.7684 0.7640 0.7274 -0.0086 -0.0461 0.2012  70  ASN C CA  
7188  C C   . ASN C 70  ? 0.7340 0.7241 0.7038 0.0074  -0.0259 0.1959  70  ASN C C   
7189  O O   . ASN C 70  ? 0.7344 0.7135 0.6977 0.0156  -0.0225 0.1952  70  ASN C O   
7190  C CB  . ASN C 70  ? 0.7983 0.8154 0.7563 -0.0118 -0.0541 0.2161  70  ASN C CB  
7191  C CG  . ASN C 70  ? 0.9251 0.9363 0.8649 -0.0289 -0.0776 0.2205  70  ASN C CG  
7192  O OD1 . ASN C 70  ? 0.9795 0.9887 0.9164 -0.0420 -0.0878 0.2192  70  ASN C OD1 
7193  N ND2 . ASN C 70  ? 1.1125 1.1191 1.0384 -0.0294 -0.0875 0.2257  70  ASN C ND2 
7194  N N   . GLY C 71  ? 0.7006 0.6963 0.6850 0.0113  -0.0139 0.1920  71  GLY C N   
7195  C CA  . GLY C 71  ? 0.6705 0.6586 0.6642 0.0245  0.0035  0.1881  71  GLY C CA  
7196  C C   . GLY C 71  ? 0.6552 0.6630 0.6595 0.0346  0.0117  0.1989  71  GLY C C   
7197  O O   . GLY C 71  ? 0.6569 0.6878 0.6623 0.0317  0.0046  0.2097  71  GLY C O   
7198  N N   . THR C 72  ? 0.6423 0.6407 0.6534 0.0464  0.0259  0.1966  72  THR C N   
7199  C CA  . THR C 72  ? 0.6369 0.6495 0.6563 0.0591  0.0344  0.2054  72  THR C CA  
7200  C C   . THR C 72  ? 0.6351 0.6662 0.6633 0.0611  0.0367  0.2051  72  THR C C   
7201  O O   . THR C 72  ? 0.6402 0.6583 0.6712 0.0612  0.0420  0.1948  72  THR C O   
7202  C CB  . THR C 72  ? 0.6440 0.6341 0.6650 0.0703  0.0472  0.2024  72  THR C CB  
7203  O OG1 . THR C 72  ? 0.6232 0.5993 0.6487 0.0716  0.0543  0.1923  72  THR C OG1 
7204  C CG2 . THR C 72  ? 0.6488 0.6210 0.6616 0.0665  0.0457  0.2001  72  THR C CG2 
7205  N N   . ASP C 73  ? 0.6319 0.6955 0.6644 0.0630  0.0328  0.2165  73  ASP C N   
7206  C CA  . ASP C 73  ? 0.6241 0.7145 0.6639 0.0611  0.0312  0.2178  73  ASP C CA  
7207  C C   . ASP C 73  ? 0.6069 0.6955 0.6441 0.0428  0.0205  0.2119  73  ASP C C   
7208  O O   . ASP C 73  ? 0.5965 0.6597 0.6316 0.0398  0.0234  0.1990  73  ASP C O   
7209  C CB  . ASP C 73  ? 0.6302 0.7169 0.6758 0.0774  0.0444  0.2114  73  ASP C CB  
7210  C CG  . ASP C 73  ? 0.6342 0.7533 0.6867 0.0775  0.0431  0.2131  73  ASP C CG  
7211  O OD1 . ASP C 73  ? 0.6261 0.7649 0.6798 0.0613  0.0320  0.2172  73  ASP C OD1 
7212  O OD2 . ASP C 73  ? 0.6534 0.7785 0.7089 0.0946  0.0525  0.2108  73  ASP C OD2 
7213  N N   . ALA C 74  ? 0.5967 0.7125 0.6335 0.0302  0.0077  0.2222  74  ALA C N   
7214  C CA  . ALA C 74  ? 0.5902 0.7018 0.6224 0.0122  -0.0044 0.2183  74  ALA C CA  
7215  C C   . ALA C 74  ? 0.5819 0.7251 0.6236 0.0088  -0.0051 0.2223  74  ALA C C   
7216  O O   . ALA C 74  ? 0.5821 0.7376 0.6212 -0.0084 -0.0188 0.2277  74  ALA C O   
7217  C CB  . ALA C 74  ? 0.5956 0.7037 0.6153 -0.0039 -0.0223 0.2252  74  ALA C CB  
7218  N N   . LYS C 75  ? 0.5810 0.7367 0.6322 0.0255  0.0087  0.2200  75  LYS C N   
7219  C CA  . LYS C 75  ? 0.5802 0.7561 0.6387 0.0253  0.0110  0.2175  75  LYS C CA  
7220  C C   . LYS C 75  ? 0.5761 0.7152 0.6320 0.0264  0.0176  0.1992  75  LYS C C   
7221  O O   . LYS C 75  ? 0.5737 0.7182 0.6324 0.0207  0.0165  0.1938  75  LYS C O   
7222  C CB  . LYS C 75  ? 0.5860 0.7939 0.6530 0.0456  0.0220  0.2231  75  LYS C CB  
7223  C CG  . LYS C 75  ? 0.6025 0.8585 0.6743 0.0446  0.0159  0.2429  75  LYS C CG  
7224  C CD  . LYS C 75  ? 0.6408 0.9084 0.7148 0.0699  0.0279  0.2469  75  LYS C CD  
7225  C CE  . LYS C 75  ? 0.6603 0.9619 0.7359 0.0671  0.0209  0.2658  75  LYS C CE  
7226  N NZ  . LYS C 75  ? 0.6784 0.9564 0.7492 0.0810  0.0276  0.2652  75  LYS C NZ  
7227  N N   . VAL C 76  ? 0.5743 0.6786 0.6252 0.0335  0.0243  0.1911  76  VAL C N   
7228  C CA  . VAL C 76  ? 0.5670 0.6353 0.6142 0.0324  0.0291  0.1758  76  VAL C CA  
7229  C C   . VAL C 76  ? 0.5591 0.6127 0.5978 0.0146  0.0167  0.1726  76  VAL C C   
7230  O O   . VAL C 76  ? 0.5617 0.6119 0.5927 0.0081  0.0075  0.1788  76  VAL C O   
7231  C CB  . VAL C 76  ? 0.5783 0.6202 0.6227 0.0443  0.0387  0.1725  76  VAL C CB  
7232  C CG1 . VAL C 76  ? 0.5827 0.5901 0.6222 0.0395  0.0413  0.1598  76  VAL C CG1 
7233  C CG2 . VAL C 76  ? 0.5871 0.6348 0.6362 0.0633  0.0503  0.1733  76  VAL C CG2 
7234  N N   . LYS C 77  ? 0.5504 0.5947 0.5889 0.0078  0.0157  0.1627  77  LYS C N   
7235  C CA  . LYS C 77  ? 0.5489 0.5784 0.5775 -0.0070 0.0034  0.1589  77  LYS C CA  
7236  C C   . LYS C 77  ? 0.5332 0.5413 0.5609 -0.0077 0.0083  0.1444  77  LYS C C   
7237  O O   . LYS C 77  ? 0.5276 0.5400 0.5552 -0.0164 0.0028  0.1412  77  LYS C O   
7238  C CB  . LYS C 77  ? 0.5534 0.6077 0.5817 -0.0209 -0.0105 0.1687  77  LYS C CB  
7239  C CG  . LYS C 77  ? 0.5993 0.6555 0.6177 -0.0302 -0.0249 0.1797  77  LYS C CG  
7240  C CD  . LYS C 77  ? 0.6501 0.7466 0.6755 -0.0366 -0.0318 0.1966  77  LYS C CD  
7241  C CE  . LYS C 77  ? 0.6889 0.7881 0.7060 -0.0414 -0.0424 0.2081  77  LYS C CE  
7242  N NZ  . LYS C 77  ? 0.7199 0.8568 0.7400 -0.0559 -0.0559 0.2262  77  LYS C NZ  
7243  N N   . LEU C 78  ? 0.5272 0.5132 0.5540 0.0004  0.0180  0.1367  78  LEU C N   
7244  C CA  . LEU C 78  ? 0.5134 0.4840 0.5425 0.0016  0.0257  0.1241  78  LEU C CA  
7245  C C   . LEU C 78  ? 0.5060 0.4691 0.5284 -0.0091 0.0171  0.1175  78  LEU C C   
7246  O O   . LEU C 78  ? 0.5009 0.4696 0.5280 -0.0124 0.0183  0.1119  78  LEU C O   
7247  C CB  . LEU C 78  ? 0.5150 0.4644 0.5429 0.0089  0.0352  0.1198  78  LEU C CB  
7248  C CG  . LEU C 78  ? 0.5225 0.4748 0.5564 0.0209  0.0444  0.1255  78  LEU C CG  
7249  C CD1 . LEU C 78  ? 0.5262 0.4560 0.5595 0.0264  0.0537  0.1219  78  LEU C CD1 
7250  C CD2 . LEU C 78  ? 0.5275 0.4947 0.5690 0.0270  0.0491  0.1246  78  LEU C CD2 
7251  N N   . ILE C 79  ? 0.5071 0.4575 0.5170 -0.0134 0.0077  0.1181  79  ILE C N   
7252  C CA  . ILE C 79  ? 0.5031 0.4427 0.5025 -0.0217 -0.0023 0.1118  79  ILE C CA  
7253  C C   . ILE C 79  ? 0.4983 0.4535 0.4996 -0.0322 -0.0119 0.1159  79  ILE C C   
7254  O O   . ILE C 79  ? 0.4938 0.4495 0.4983 -0.0355 -0.0104 0.1089  79  ILE C O   
7255  C CB  . ILE C 79  ? 0.5144 0.4371 0.4960 -0.0222 -0.0129 0.1122  79  ILE C CB  
7256  C CG1 . ILE C 79  ? 0.5199 0.4318 0.5005 -0.0119 -0.0027 0.1087  79  ILE C CG1 
7257  C CG2 . ILE C 79  ? 0.5198 0.4286 0.4887 -0.0276 -0.0227 0.1046  79  ILE C CG2 
7258  C CD1 . ILE C 79  ? 0.5409 0.4396 0.5032 -0.0088 -0.0119 0.1097  79  ILE C CD1 
7259  N N   . LYS C 80  ? 0.4992 0.4696 0.4992 -0.0381 -0.0215 0.1280  80  LYS C N   
7260  C CA  . LYS C 80  ? 0.4927 0.4846 0.4969 -0.0492 -0.0300 0.1350  80  LYS C CA  
7261  C C   . LYS C 80  ? 0.4711 0.4794 0.4901 -0.0446 -0.0179 0.1300  80  LYS C C   
7262  O O   . LYS C 80  ? 0.4645 0.4780 0.4841 -0.0523 -0.0223 0.1277  80  LYS C O   
7263  C CB  . LYS C 80  ? 0.5020 0.5188 0.5091 -0.0538 -0.0371 0.1511  80  LYS C CB  
7264  C CG  . LYS C 80  ? 0.5174 0.5678 0.5338 -0.0632 -0.0420 0.1609  80  LYS C CG  
7265  C CD  . LYS C 80  ? 0.5711 0.6207 0.5750 -0.0829 -0.0639 0.1708  80  LYS C CD  
7266  C CE  . LYS C 80  ? 0.5921 0.6559 0.5999 -0.0940 -0.0694 0.1722  80  LYS C CE  
7267  N NZ  . LYS C 80  ? 0.6292 0.6581 0.6260 -0.0946 -0.0713 0.1571  80  LYS C NZ  
7268  N N   . GLN C 81  ? 0.4629 0.4770 0.4920 -0.0316 -0.0032 0.1282  81  GLN C N   
7269  C CA  . GLN C 81  ? 0.4573 0.4859 0.4978 -0.0247 0.0077  0.1235  81  GLN C CA  
7270  C C   . GLN C 81  ? 0.4474 0.4570 0.4873 -0.0249 0.0130  0.1089  81  GLN C C   
7271  O O   . GLN C 81  ? 0.4448 0.4668 0.4891 -0.0285 0.0127  0.1059  81  GLN C O   
7272  C CB  . GLN C 81  ? 0.4642 0.5000 0.5118 -0.0094 0.0197  0.1259  81  GLN C CB  
7273  C CG  . GLN C 81  ? 0.5021 0.5667 0.5523 -0.0088 0.0146  0.1417  81  GLN C CG  
7274  C CD  . GLN C 81  ? 0.5491 0.6235 0.6050 0.0088  0.0260  0.1452  81  GLN C CD  
7275  O OE1 . GLN C 81  ? 0.5735 0.6504 0.6340 0.0209  0.0362  0.1386  81  GLN C OE1 
7276  N NE2 . GLN C 81  ? 0.5509 0.6307 0.6049 0.0109  0.0233  0.1557  81  GLN C NE2 
7277  N N   . GLU C 82  ? 0.4402 0.4232 0.4749 -0.0216 0.0175  0.1010  82  GLU C N   
7278  C CA  . GLU C 82  ? 0.4287 0.3963 0.4624 -0.0231 0.0216  0.0884  82  GLU C CA  
7279  C C   . GLU C 82  ? 0.4195 0.3887 0.4474 -0.0338 0.0108  0.0866  82  GLU C C   
7280  O O   . GLU C 82  ? 0.4147 0.3884 0.4471 -0.0358 0.0136  0.0798  82  GLU C O   
7281  C CB  . GLU C 82  ? 0.4329 0.3779 0.4606 -0.0200 0.0252  0.0834  82  GLU C CB  
7282  C CG  . GLU C 82  ? 0.4568 0.3931 0.4908 -0.0119 0.0382  0.0796  82  GLU C CG  
7283  C CD  . GLU C 82  ? 0.4844 0.4159 0.5233 -0.0128 0.0450  0.0688  82  GLU C CD  
7284  O OE1 . GLU C 82  ? 0.4861 0.4169 0.5224 -0.0194 0.0411  0.0626  82  GLU C OE1 
7285  O OE2 . GLU C 82  ? 0.4974 0.4240 0.5412 -0.0064 0.0536  0.0664  82  GLU C OE2 
7286  N N   . LEU C 83  ? 0.4207 0.3846 0.4373 -0.0406 -0.0025 0.0927  83  LEU C N   
7287  C CA  . LEU C 83  ? 0.4229 0.3837 0.4308 -0.0510 -0.0153 0.0920  83  LEU C CA  
7288  C C   . LEU C 83  ? 0.4148 0.4005 0.4322 -0.0574 -0.0169 0.0964  83  LEU C C   
7289  O O   . LEU C 83  ? 0.4116 0.3967 0.4279 -0.0626 -0.0197 0.0912  83  LEU C O   
7290  C CB  . LEU C 83  ? 0.4406 0.3902 0.4325 -0.0578 -0.0318 0.0995  83  LEU C CB  
7291  C CG  . LEU C 83  ? 0.4588 0.3810 0.4339 -0.0528 -0.0362 0.0940  83  LEU C CG  
7292  C CD1 . LEU C 83  ? 0.4893 0.3934 0.4447 -0.0607 -0.0542 0.0930  83  LEU C CD1 
7293  C CD2 . LEU C 83  ? 0.4595 0.3733 0.4384 -0.0432 -0.0226 0.0826  83  LEU C CD2 
7294  N N   . ASP C 84  ? 0.4126 0.4229 0.4391 -0.0561 -0.0150 0.1066  84  ASP C N   
7295  C CA  . ASP C 84  ? 0.4130 0.4541 0.4487 -0.0609 -0.0164 0.1129  84  ASP C CA  
7296  C C   . ASP C 84  ? 0.3979 0.4437 0.4424 -0.0536 -0.0040 0.1016  84  ASP C C   
7297  O O   . ASP C 84  ? 0.3941 0.4492 0.4399 -0.0604 -0.0077 0.0999  84  ASP C O   
7298  C CB  . ASP C 84  ? 0.4221 0.4932 0.4656 -0.0581 -0.0157 0.1266  84  ASP C CB  
7299  C CG  . ASP C 84  ? 0.4720 0.5467 0.5070 -0.0711 -0.0323 0.1409  84  ASP C CG  
7300  O OD1 . ASP C 84  ? 0.5251 0.5814 0.5476 -0.0838 -0.0465 0.1409  84  ASP C OD1 
7301  O OD2 . ASP C 84  ? 0.5147 0.6091 0.5540 -0.0684 -0.0322 0.1522  84  ASP C OD2 
7302  N N   . LYS C 85  ? 0.3908 0.4279 0.4399 -0.0404 0.0097  0.0942  85  LYS C N   
7303  C CA  . LYS C 85  ? 0.3802 0.4131 0.4346 -0.0331 0.0211  0.0816  85  LYS C CA  
7304  C C   . LYS C 85  ? 0.3701 0.3898 0.4201 -0.0415 0.0172  0.0728  85  LYS C C   
7305  O O   . LYS C 85  ? 0.3640 0.3972 0.4178 -0.0444 0.0171  0.0696  85  LYS C O   
7306  C CB  . LYS C 85  ? 0.3854 0.3966 0.4396 -0.0223 0.0319  0.0749  85  LYS C CB  
7307  C CG  . LYS C 85  ? 0.3923 0.4020 0.4514 -0.0129 0.0429  0.0650  85  LYS C CG  
7308  C CD  . LYS C 85  ? 0.4099 0.3912 0.4665 -0.0068 0.0510  0.0581  85  LYS C CD  
7309  C CE  . LYS C 85  ? 0.4374 0.3999 0.4899 -0.0158 0.0491  0.0516  85  LYS C CE  
7310  N NZ  . LYS C 85  ? 0.4784 0.4176 0.5294 -0.0122 0.0563  0.0473  85  LYS C NZ  
7311  N N   . TYR C 86  ? 0.3678 0.3632 0.4088 -0.0443 0.0136  0.0694  86  TYR C N   
7312  C CA  . TYR C 86  ? 0.3619 0.3448 0.3968 -0.0500 0.0097  0.0615  86  TYR C CA  
7313  C C   . TYR C 86  ? 0.3577 0.3523 0.3892 -0.0605 -0.0025 0.0667  86  TYR C C   
7314  O O   . TYR C 86  ? 0.3504 0.3532 0.3858 -0.0630 -0.0009 0.0613  86  TYR C O   
7315  C CB  . TYR C 86  ? 0.3700 0.3291 0.3932 -0.0492 0.0060  0.0591  86  TYR C CB  
7316  C CG  . TYR C 86  ? 0.3735 0.3216 0.3877 -0.0532 0.0003  0.0519  86  TYR C CG  
7317  C CD1 . TYR C 86  ? 0.3818 0.3329 0.4020 -0.0529 0.0076  0.0423  86  TYR C CD1 
7318  C CD2 . TYR C 86  ? 0.3802 0.3142 0.3783 -0.0565 -0.0132 0.0545  86  TYR C CD2 
7319  C CE1 . TYR C 86  ? 0.3823 0.3262 0.3945 -0.0555 0.0027  0.0360  86  TYR C CE1 
7320  C CE2 . TYR C 86  ? 0.3871 0.3104 0.3749 -0.0576 -0.0188 0.0476  86  TYR C CE2 
7321  C CZ  . TYR C 86  ? 0.3939 0.3240 0.3898 -0.0570 -0.0102 0.0387  86  TYR C CZ  
7322  O OH  . TYR C 86  ? 0.3954 0.3181 0.3817 -0.0572 -0.0152 0.0322  86  TYR C OH  
7323  N N   . LYS C 87  ? 0.3662 0.3606 0.3895 -0.0676 -0.0156 0.0777  87  LYS C N   
7324  C CA  . LYS C 87  ? 0.3747 0.3757 0.3918 -0.0805 -0.0306 0.0848  87  LYS C CA  
7325  C C   . LYS C 87  ? 0.3616 0.3932 0.3914 -0.0832 -0.0267 0.0871  87  LYS C C   
7326  O O   . LYS C 87  ? 0.3640 0.3995 0.3910 -0.0920 -0.0344 0.0877  87  LYS C O   
7327  C CB  . LYS C 87  ? 0.3875 0.3910 0.3970 -0.0892 -0.0449 0.0995  87  LYS C CB  
7328  C CG  . LYS C 87  ? 0.4191 0.3914 0.4109 -0.0888 -0.0542 0.0982  87  LYS C CG  
7329  C CD  . LYS C 87  ? 0.4666 0.4422 0.4503 -0.0994 -0.0700 0.1134  87  LYS C CD  
7330  C CE  . LYS C 87  ? 0.4866 0.4382 0.4574 -0.0936 -0.0733 0.1123  87  LYS C CE  
7331  N NZ  . LYS C 87  ? 0.5244 0.4579 0.4744 -0.1059 -0.0959 0.1208  87  LYS C NZ  
7332  N N   . ASN C 88  ? 0.3471 0.4004 0.3897 -0.0745 -0.0152 0.0887  88  ASN C N   
7333  C CA  . ASN C 88  ? 0.3320 0.4185 0.3857 -0.0737 -0.0110 0.0915  88  ASN C CA  
7334  C C   . ASN C 88  ? 0.3139 0.3966 0.3709 -0.0697 -0.0026 0.0774  88  ASN C C   
7335  O O   . ASN C 88  ? 0.3077 0.4064 0.3666 -0.0765 -0.0070 0.0787  88  ASN C O   
7336  C CB  . ASN C 88  ? 0.3366 0.4454 0.3993 -0.0622 -0.0018 0.0967  88  ASN C CB  
7337  C CG  . ASN C 88  ? 0.3405 0.4803 0.4130 -0.0545 0.0064  0.0950  88  ASN C CG  
7338  O OD1 . ASN C 88  ? 0.3519 0.5258 0.4290 -0.0610 0.0005  0.1059  88  ASN C OD1 
7339  N ND2 . ASN C 88  ? 0.3592 0.4878 0.4338 -0.0404 0.0195  0.0819  88  ASN C ND2 
7340  N N   . ALA C 89  ? 0.3041 0.3660 0.3614 -0.0598 0.0085  0.0647  89  ALA C N   
7341  C CA  . ALA C 89  ? 0.2911 0.3443 0.3496 -0.0576 0.0154  0.0507  89  ALA C CA  
7342  C C   . ALA C 89  ? 0.2817 0.3310 0.3343 -0.0686 0.0056  0.0500  89  ALA C C   
7343  O O   . ALA C 89  ? 0.2749 0.3357 0.3311 -0.0703 0.0074  0.0447  89  ALA C O   
7344  C CB  . ALA C 89  ? 0.2932 0.3193 0.3492 -0.0513 0.0235  0.0408  89  ALA C CB  
7345  N N   . VAL C 90  ? 0.2791 0.3111 0.3208 -0.0751 -0.0055 0.0552  90  VAL C N   
7346  C CA  . VAL C 90  ? 0.2757 0.2968 0.3068 -0.0841 -0.0175 0.0553  90  VAL C CA  
7347  C C   . VAL C 90  ? 0.2758 0.3203 0.3091 -0.0947 -0.0270 0.0655  90  VAL C C   
7348  O O   . VAL C 90  ? 0.2748 0.3219 0.3068 -0.0990 -0.0297 0.0618  90  VAL C O   
7349  C CB  . VAL C 90  ? 0.2837 0.2785 0.2992 -0.0861 -0.0283 0.0587  90  VAL C CB  
7350  C CG1 . VAL C 90  ? 0.2904 0.2705 0.2910 -0.0940 -0.0430 0.0597  90  VAL C CG1 
7351  C CG2 . VAL C 90  ? 0.2861 0.2620 0.2995 -0.0762 -0.0188 0.0485  90  VAL C CG2 
7352  N N   . THR C 91  ? 0.2842 0.3488 0.3213 -0.0991 -0.0320 0.0793  91  THR C N   
7353  C CA  . THR C 91  ? 0.2864 0.3805 0.3275 -0.1103 -0.0409 0.0920  91  THR C CA  
7354  C C   . THR C 91  ? 0.2764 0.3970 0.3301 -0.1041 -0.0291 0.0852  91  THR C C   
7355  O O   . THR C 91  ? 0.2755 0.4050 0.3286 -0.1115 -0.0342 0.0859  91  THR C O   
7356  C CB  . THR C 91  ? 0.2858 0.4043 0.3306 -0.1162 -0.0475 0.1099  91  THR C CB  
7357  O OG1 . THR C 91  ? 0.2927 0.3857 0.3276 -0.1162 -0.0530 0.1123  91  THR C OG1 
7358  C CG2 . THR C 91  ? 0.2985 0.4337 0.3397 -0.1343 -0.0644 0.1258  91  THR C CG2 
7359  N N   . GLU C 92  ? 0.2731 0.4029 0.3359 -0.0900 -0.0141 0.0780  92  GLU C N   
7360  C CA  . GLU C 92  ? 0.2735 0.4235 0.3450 -0.0820 -0.0033 0.0694  92  GLU C CA  
7361  C C   . GLU C 92  ? 0.2678 0.4049 0.3360 -0.0857 -0.0035 0.0583  92  GLU C C   
7362  O O   . GLU C 92  ? 0.2560 0.4166 0.3287 -0.0883 -0.0038 0.0588  92  GLU C O   
7363  C CB  . GLU C 92  ? 0.2794 0.4235 0.3550 -0.0654 0.0114  0.0590  92  GLU C CB  
7364  C CG  . GLU C 92  ? 0.3182 0.4932 0.4004 -0.0562 0.0156  0.0681  92  GLU C CG  
7365  C CD  . GLU C 92  ? 0.3657 0.5854 0.4547 -0.0569 0.0142  0.0759  92  GLU C CD  
7366  O OE1 . GLU C 92  ? 0.3821 0.6052 0.4718 -0.0580 0.0160  0.0675  92  GLU C OE1 
7367  O OE2 . GLU C 92  ? 0.3748 0.6286 0.4685 -0.0561 0.0115  0.0910  92  GLU C OE2 
7368  N N   . LEU C 93  ? 0.2736 0.3761 0.3340 -0.0853 -0.0033 0.0489  93  LEU C N   
7369  C CA  . LEU C 93  ? 0.2711 0.3617 0.3280 -0.0875 -0.0030 0.0381  93  LEU C CA  
7370  C C   . LEU C 93  ? 0.2801 0.3733 0.3300 -0.0998 -0.0173 0.0465  93  LEU C C   
7371  O O   . LEU C 93  ? 0.2824 0.3867 0.3342 -0.1026 -0.0175 0.0429  93  LEU C O   
7372  C CB  . LEU C 93  ? 0.2684 0.3272 0.3187 -0.0831 0.0009  0.0278  93  LEU C CB  
7373  C CG  . LEU C 93  ? 0.2613 0.3127 0.3175 -0.0729 0.0150  0.0171  93  LEU C CG  
7374  C CD1 . LEU C 93  ? 0.2720 0.2964 0.3208 -0.0714 0.0153  0.0129  93  LEU C CD1 
7375  C CD2 . LEU C 93  ? 0.2454 0.3040 0.3069 -0.0701 0.0233  0.0053  93  LEU C CD2 
7376  N N   . GLN C 94  ? 0.2946 0.3763 0.3351 -0.1075 -0.0304 0.0578  94  GLN C N   
7377  C CA  . GLN C 94  ? 0.3148 0.3951 0.3458 -0.1209 -0.0470 0.0678  94  GLN C CA  
7378  C C   . GLN C 94  ? 0.3113 0.4290 0.3523 -0.1277 -0.0482 0.0760  94  GLN C C   
7379  O O   . GLN C 94  ? 0.3173 0.4355 0.3524 -0.1373 -0.0585 0.0801  94  GLN C O   
7380  C CB  . GLN C 94  ? 0.3327 0.4030 0.3541 -0.1297 -0.0614 0.0820  94  GLN C CB  
7381  C CG  . GLN C 94  ? 0.3695 0.4000 0.3699 -0.1331 -0.0754 0.0809  94  GLN C CG  
7382  C CD  . GLN C 94  ? 0.4246 0.4420 0.4169 -0.1362 -0.0840 0.0901  94  GLN C CD  
7383  O OE1 . GLN C 94  ? 0.4473 0.4843 0.4432 -0.1467 -0.0920 0.1057  94  GLN C OE1 
7384  N NE2 . GLN C 94  ? 0.4535 0.4415 0.4356 -0.1267 -0.0819 0.0811  94  GLN C NE2 
7385  N N   . LEU C 95  ? 0.3050 0.4551 0.3598 -0.1220 -0.0384 0.0792  95  LEU C N   
7386  C CA  . LEU C 95  ? 0.3092 0.5001 0.3727 -0.1279 -0.0406 0.0898  95  LEU C CA  
7387  C C   . LEU C 95  ? 0.3208 0.5216 0.3895 -0.1215 -0.0310 0.0767  95  LEU C C   
7388  O O   . LEU C 95  ? 0.3282 0.5574 0.4011 -0.1279 -0.0348 0.0836  95  LEU C O   
7389  C CB  . LEU C 95  ? 0.3011 0.5274 0.3752 -0.1231 -0.0355 0.1001  95  LEU C CB  
7390  C CG  . LEU C 95  ? 0.2897 0.5093 0.3587 -0.1312 -0.0463 0.1147  95  LEU C CG  
7391  C CD1 . LEU C 95  ? 0.2657 0.5126 0.3446 -0.1202 -0.0367 0.1194  95  LEU C CD1 
7392  C CD2 . LEU C 95  ? 0.2779 0.5095 0.3420 -0.1515 -0.0651 0.1341  95  LEU C CD2 
7393  N N   . LEU C 96  ? 0.3353 0.5127 0.4033 -0.1103 -0.0197 0.0587  96  LEU C N   
7394  C CA  . LEU C 96  ? 0.3435 0.5269 0.4150 -0.1055 -0.0117 0.0457  96  LEU C CA  
7395  C C   . LEU C 96  ? 0.3648 0.5442 0.4302 -0.1157 -0.0215 0.0472  96  LEU C C   
7396  O O   . LEU C 96  ? 0.3649 0.5625 0.4351 -0.1142 -0.0170 0.0418  96  LEU C O   
7397  C CB  . LEU C 96  ? 0.3404 0.4966 0.4105 -0.0953 -0.0008 0.0285  96  LEU C CB  
7398  C CG  . LEU C 96  ? 0.3360 0.5053 0.4134 -0.0835 0.0101  0.0261  96  LEU C CG  
7399  C CD1 . LEU C 96  ? 0.3349 0.4845 0.4122 -0.0742 0.0215  0.0085  96  LEU C CD1 
7400  C CD2 . LEU C 96  ? 0.3264 0.5370 0.4110 -0.0815 0.0112  0.0323  96  LEU C CD2 
7401  N N   . MET C 97  ? 0.4003 0.5554 0.4535 -0.1253 -0.0354 0.0548  97  MET C N   
7402  C CA  . MET C 97  ? 0.4389 0.5788 0.4816 -0.1324 -0.0455 0.0541  97  MET C CA  
7403  C C   . MET C 97  ? 0.4577 0.6239 0.5022 -0.1436 -0.0545 0.0656  97  MET C C   
7404  O O   . MET C 97  ? 0.4690 0.6317 0.5094 -0.1453 -0.0569 0.0604  97  MET C O   
7405  C CB  . MET C 97  ? 0.4583 0.5601 0.4836 -0.1366 -0.0589 0.0579  97  MET C CB  
7406  C CG  . MET C 97  ? 0.5000 0.5777 0.5232 -0.1249 -0.0495 0.0465  97  MET C CG  
7407  S SD  . MET C 97  ? 0.5801 0.6469 0.6056 -0.1123 -0.0344 0.0253  97  MET C SD  
7408  C CE  . MET C 97  ? 0.5101 0.6105 0.5487 -0.1133 -0.0265 0.0200  97  MET C CE  
7409  N N   . GLN C 98  ? 0.4709 0.6669 0.5220 -0.1514 -0.0595 0.0820  98  GLN C N   
7410  C CA  . GLN C 98  ? 0.4859 0.7130 0.5401 -0.1633 -0.0682 0.0956  98  GLN C CA  
7411  C C   . GLN C 98  ? 0.4745 0.7537 0.5458 -0.1582 -0.0575 0.1008  98  GLN C C   
7412  O O   . GLN C 98  ? 0.4631 0.7486 0.5417 -0.1443 -0.0440 0.0923  98  GLN C O   
7413  C CB  . GLN C 98  ? 0.5100 0.7234 0.5512 -0.1822 -0.0906 0.1153  98  GLN C CB  
7414  C CG  . GLN C 98  ? 0.5441 0.7016 0.5653 -0.1826 -0.1011 0.1106  98  GLN C CG  
7415  C CD  . GLN C 98  ? 0.5622 0.7075 0.5841 -0.1760 -0.0962 0.1089  98  GLN C CD  
7416  O OE1 . GLN C 98  ? 0.5330 0.6887 0.5667 -0.1618 -0.0785 0.0974  98  GLN C OE1 
7417  N NE2 . GLN C 98  ? 0.5799 0.7005 0.5872 -0.1866 -0.1132 0.1205  98  GLN C NE2 
7418  N N   . VAL C 143 ? 1.0112 2.4597 0.8040 0.6920  0.1248  1.2290  152 VAL C N   
7419  C CA  . VAL C 143 ? 1.0222 2.4688 0.8145 0.6883  0.1323  1.2450  152 VAL C CA  
7420  C C   . VAL C 143 ? 1.0067 2.4315 0.7959 0.6713  0.1310  1.2206  152 VAL C C   
7421  O O   . VAL C 143 ? 1.0152 2.4308 0.8072 0.6657  0.1380  1.2340  152 VAL C O   
7422  C CB  . VAL C 143 ? 1.0357 2.5430 0.8190 0.7003  0.1332  1.2685  152 VAL C CB  
7423  C CG1 . VAL C 143 ? 1.0486 2.5596 0.8325 0.6960  0.1413  1.2893  152 VAL C CG1 
7424  C CG2 . VAL C 143 ? 1.0523 2.5778 0.8394 0.7176  0.1350  1.2939  152 VAL C CG2 
7425  N N   . ALA C 144 ? 0.9860 2.4040 0.7694 0.6631  0.1218  1.1870  153 ALA C N   
7426  C CA  . ALA C 144 ? 0.9692 2.3614 0.7486 0.6476  0.1184  1.1576  153 ALA C CA  
7427  C C   . ALA C 144 ? 0.9553 2.3739 0.7157 0.6442  0.1047  1.1259  153 ALA C C   
7428  O O   . ALA C 144 ? 0.9539 2.3977 0.7070 0.6491  0.0955  1.1197  153 ALA C O   
7429  C CB  . ALA C 144 ? 0.9752 2.3506 0.7589 0.6400  0.1276  1.1685  153 ALA C CB  
7430  N N   . VAL C 145 ? 0.9480 2.3608 0.6986 0.6361  0.1022  1.1062  154 VAL C N   
7431  C CA  . VAL C 145 ? 0.9364 2.3492 0.6702 0.6298  0.0876  1.0711  154 VAL C CA  
7432  C C   . VAL C 145 ? 0.9403 2.3849 0.6482 0.6334  0.0784  1.0534  154 VAL C C   
7433  O O   . VAL C 145 ? 0.9437 2.3962 0.6477 0.6352  0.0846  1.0569  154 VAL C O   
7434  C CB  . VAL C 145 ? 0.9228 2.2845 0.6649 0.6158  0.0884  1.0519  154 VAL C CB  
7435  C CG1 . VAL C 145 ? 0.9129 2.2676 0.6399 0.6080  0.0725  1.0181  154 VAL C CG1 
7436  C CG2 . VAL C 145 ? 0.9223 2.2497 0.6873 0.6142  0.0973  1.0680  154 VAL C CG2 
7437  N N   . SER C 146 ? 0.9417 2.4033 0.6306 0.6343  0.0625  1.0334  155 SER C N   
7438  C CA  . SER C 146 ? 0.9501 2.4343 0.6096 0.6388  0.0510  1.0124  155 SER C CA  
7439  C C   . SER C 146 ? 0.9417 2.3879 0.5931 0.6282  0.0456  0.9828  155 SER C C   
7440  O O   . SER C 146 ? 0.9281 2.3326 0.5943 0.6154  0.0465  0.9741  155 SER C O   
7441  C CB  . SER C 146 ? 0.9589 2.4669 0.5974 0.6411  0.0327  0.9990  155 SER C CB  
7442  O OG  . SER C 146 ? 0.9718 2.4922 0.5771 0.6457  0.0190  0.9744  155 SER C OG  
7443  N N   . LYS C 147 ? 0.9517 2.4136 0.5775 0.6352  0.0393  0.9666  156 LYS C N   
7444  C CA  . LYS C 147 ? 0.9499 2.3804 0.5576 0.6282  0.0281  0.9325  156 LYS C CA  
7445  C C   . LYS C 147 ? 0.9569 2.3795 0.5445 0.6224  0.0066  0.9094  156 LYS C C   
7446  O O   . LYS C 147 ? 0.9652 2.4165 0.5489 0.6267  0.0006  0.9197  156 LYS C O   
7447  C CB  . LYS C 147 ? 0.9634 2.4182 0.5464 0.6417  0.0271  0.9237  156 LYS C CB  
7448  C CG  . LYS C 147 ? 0.9678 2.3933 0.5256 0.6387  0.0134  0.8874  156 LYS C CG  
7449  C CD  . LYS C 147 ? 0.9525 2.3479 0.5265 0.6310  0.0253  0.8844  156 LYS C CD  
7450  C CE  . LYS C 147 ? 0.9610 2.3867 0.5231 0.6456  0.0332  0.8879  156 LYS C CE  
7451  N NZ  . LYS C 147 ? 0.9444 2.3507 0.5321 0.6361  0.0493  0.8981  156 LYS C NZ  
7452  N N   . VAL C 148 ? 0.9557 2.3410 0.5293 0.6122  -0.0060 0.8791  157 VAL C N   
7453  C CA  . VAL C 148 ? 0.9624 2.3321 0.5194 0.6010  -0.0279 0.8578  157 VAL C CA  
7454  C C   . VAL C 148 ? 0.9434 2.2961 0.5309 0.5866  -0.0235 0.8693  157 VAL C C   
7455  O O   . VAL C 148 ? 0.9351 2.2517 0.5248 0.5713  -0.0316 0.8517  157 VAL C O   
7456  C CB  . VAL C 148 ? 0.9876 2.3944 0.5144 0.6101  -0.0454 0.8546  157 VAL C CB  
7457  C CG1 . VAL C 148 ? 0.9903 2.3852 0.5125 0.5938  -0.0646 0.8444  157 VAL C CG1 
7458  C CG2 . VAL C 148 ? 1.0099 2.4134 0.4984 0.6200  -0.0579 0.8294  157 VAL C CG2 
7459  N N   . LEU C 149 ? 0.9380 2.3169 0.5480 0.5926  -0.0106 0.8990  158 LEU C N   
7460  C CA  . LEU C 149 ? 0.9206 2.2813 0.5612 0.5835  -0.0020 0.9120  158 LEU C CA  
7461  C C   . LEU C 149 ? 0.9057 2.2273 0.5652 0.5782  0.0125  0.9111  158 LEU C C   
7462  O O   . LEU C 149 ? 0.8918 2.1813 0.5676 0.5665  0.0137  0.9057  158 LEU C O   
7463  C CB  . LEU C 149 ? 0.9220 2.3162 0.5802 0.5941  0.0091  0.9443  158 LEU C CB  
7464  C CG  . LEU C 149 ? 0.9314 2.3581 0.5782 0.5939  -0.0062 0.9451  158 LEU C CG  
7465  C CD1 . LEU C 149 ? 0.9383 2.4077 0.5947 0.6095  0.0043  0.9767  158 LEU C CD1 
7466  C CD2 . LEU C 149 ? 0.9200 2.3286 0.5786 0.5791  -0.0140 0.9381  158 LEU C CD2 
7467  N N   . HIS C 150 ? 0.9092 2.2357 0.5659 0.5864  0.0229  0.9161  159 HIS C N   
7468  C CA  . HIS C 150 ? 0.8970 2.1882 0.5693 0.5801  0.0352  0.9145  159 HIS C CA  
7469  C C   . HIS C 150 ? 0.8924 2.1493 0.5499 0.5695  0.0240  0.8812  159 HIS C C   
7470  O O   . HIS C 150 ? 0.8782 2.0966 0.5514 0.5582  0.0290  0.8745  159 HIS C O   
7471  C CB  . HIS C 150 ? 0.9027 2.2142 0.5778 0.5904  0.0493  0.9329  159 HIS C CB  
7472  C CG  . HIS C 150 ? 0.9014 2.1792 0.5929 0.5823  0.0614  0.9337  159 HIS C CG  
7473  N ND1 . HIS C 150 ? 0.9243 2.1921 0.6028 0.5806  0.0595  0.9144  159 HIS C ND1 
7474  C CD2 . HIS C 150 ? 0.9087 2.1582 0.6270 0.5753  0.0743  0.9503  159 HIS C CD2 
7475  C CE1 . HIS C 150 ? 0.9165 2.1547 0.6150 0.5716  0.0714  0.9205  159 HIS C CE1 
7476  N NE2 . HIS C 150 ? 0.9229 2.1474 0.6450 0.5678  0.0799  0.9417  159 HIS C NE2 
7477  N N   . LEU C 151 ? 0.9072 2.1770 0.5328 0.5745  0.0087  0.8606  160 LEU C N   
7478  C CA  . LEU C 151 ? 0.9091 2.1461 0.5147 0.5654  -0.0065 0.8277  160 LEU C CA  
7479  C C   . LEU C 151 ? 0.9106 2.1226 0.5235 0.5488  -0.0175 0.8183  160 LEU C C   
7480  O O   . LEU C 151 ? 0.9062 2.0800 0.5229 0.5365  -0.0204 0.8014  160 LEU C O   
7481  C CB  . LEU C 151 ? 0.9341 2.1893 0.4993 0.5756  -0.0243 0.8085  160 LEU C CB  
7482  C CG  . LEU C 151 ? 0.9472 2.2132 0.4895 0.5907  -0.0226 0.7983  160 LEU C CG  
7483  C CD1 . LEU C 151 ? 0.9724 2.2256 0.4725 0.5929  -0.0474 0.7661  160 LEU C CD1 
7484  C CD2 . LEU C 151 ? 0.9422 2.1807 0.5012 0.5856  -0.0090 0.7955  160 LEU C CD2 
7485  N N   . GLU C 152 ? 0.9265 2.1626 0.5415 0.5483  -0.0240 0.8297  161 GLU C N   
7486  C CA  . GLU C 152 ? 0.9320 2.1520 0.5542 0.5322  -0.0351 0.8227  161 GLU C CA  
7487  C C   . GLU C 152 ? 0.9193 2.1078 0.5722 0.5238  -0.0208 0.8281  161 GLU C C   
7488  O O   . GLU C 152 ? 0.9117 2.0656 0.5644 0.5102  -0.0275 0.8091  161 GLU C O   
7489  C CB  . GLU C 152 ? 0.9366 2.1941 0.5641 0.5349  -0.0388 0.8416  161 GLU C CB  
7490  C CG  . GLU C 152 ? 0.9381 2.1884 0.5707 0.5181  -0.0522 0.8356  161 GLU C CG  
7491  C CD  . GLU C 152 ? 0.9623 2.2537 0.5844 0.5192  -0.0653 0.8449  161 GLU C CD  
7492  O OE1 . GLU C 152 ? 0.9574 2.2818 0.5957 0.5309  -0.0532 0.8709  161 GLU C OE1 
7493  O OE2 . GLU C 152 ? 0.9912 2.2809 0.5875 0.5081  -0.0886 0.8265  161 GLU C OE2 
7494  N N   . GLY C 153 ? 0.9280 2.1269 0.6057 0.5325  -0.0015 0.8545  162 GLY C N   
7495  C CA  . GLY C 153 ? 0.9330 2.1006 0.6383 0.5274  0.0133  0.8619  162 GLY C CA  
7496  C C   . GLY C 153 ? 0.9401 2.0693 0.6438 0.5201  0.0162  0.8433  162 GLY C C   
7497  O O   . GLY C 153 ? 0.9263 2.0219 0.6446 0.5095  0.0190  0.8360  162 GLY C O   
7498  N N   . GLU C 154 ? 0.9638 2.1006 0.6494 0.5267  0.0156  0.8357  163 GLU C N   
7499  C CA  . GLU C 154 ? 0.9739 2.0802 0.6568 0.5218  0.0188  0.8193  163 GLU C CA  
7500  C C   . GLU C 154 ? 0.9668 2.0413 0.6391 0.5077  0.0034  0.7911  163 GLU C C   
7501  O O   . GLU C 154 ? 0.9550 1.9961 0.6430 0.4976  0.0086  0.7854  163 GLU C O   
7502  C CB  . GLU C 154 ? 0.9973 2.1248 0.6578 0.5337  0.0181  0.8144  163 GLU C CB  
7503  C CG  . GLU C 154 ? 1.0357 2.1551 0.7088 0.5357  0.0347  0.8227  163 GLU C CG  
7504  C CD  . GLU C 154 ? 1.1007 2.2440 0.7946 0.5430  0.0520  0.8576  163 GLU C CD  
7505  O OE1 . GLU C 154 ? 1.1223 2.3069 0.8067 0.5557  0.0517  0.8719  163 GLU C OE1 
7506  O OE2 . GLU C 154 ? 1.1051 2.2239 0.8235 0.5358  0.0650  0.8705  163 GLU C OE2 
7507  N N   . VAL C 155 ? 0.9823 2.0660 0.6269 0.5067  -0.0166 0.7742  164 VAL C N   
7508  C CA  . VAL C 155 ? 0.9863 2.0398 0.6183 0.4914  -0.0344 0.7488  164 VAL C CA  
7509  C C   . VAL C 155 ? 0.9733 2.0088 0.6340 0.4783  -0.0289 0.7558  164 VAL C C   
7510  O O   . VAL C 155 ? 0.9623 1.9628 0.6283 0.4663  -0.0306 0.7408  164 VAL C O   
7511  C CB  . VAL C 155 ? 1.0063 2.0764 0.6098 0.4891  -0.0577 0.7384  164 VAL C CB  
7512  C CG1 . VAL C 155 ? 1.0021 2.0477 0.6042 0.4685  -0.0746 0.7239  164 VAL C CG1 
7513  C CG2 . VAL C 155 ? 1.0271 2.0977 0.5936 0.4993  -0.0694 0.7195  164 VAL C CG2 
7514  N N   . ASN C 156 ? 0.9767 2.0382 0.6553 0.4822  -0.0221 0.7790  165 ASN C N   
7515  C CA  . ASN C 156 ? 0.9679 2.0201 0.6698 0.4728  -0.0194 0.7859  165 ASN C CA  
7516  C C   . ASN C 156 ? 0.9470 1.9667 0.6727 0.4713  -0.0021 0.7892  165 ASN C C   
7517  O O   . ASN C 156 ? 0.9345 1.9312 0.6715 0.4601  -0.0037 0.7816  165 ASN C O   
7518  C CB  . ASN C 156 ? 0.9764 2.0667 0.6896 0.4806  -0.0161 0.8104  165 ASN C CB  
7519  C CG  . ASN C 156 ? 0.9970 2.0988 0.7090 0.4682  -0.0318 0.8064  165 ASN C CG  
7520  O OD1 . ASN C 156 ? 1.0233 2.1573 0.7211 0.4685  -0.0448 0.8097  165 ASN C OD1 
7521  N ND2 . ASN C 156 ? 1.0042 2.0811 0.7303 0.4561  -0.0319 0.7991  165 ASN C ND2 
7522  N N   . LYS C 157 ? 0.9446 1.9633 0.6770 0.4818  0.0138  0.8012  166 LYS C N   
7523  C CA  . LYS C 157 ? 0.9311 1.9156 0.6815 0.4786  0.0279  0.8020  166 LYS C CA  
7524  C C   . LYS C 157 ? 0.9201 1.8727 0.6594 0.4662  0.0189  0.7738  166 LYS C C   
7525  O O   . LYS C 157 ? 0.9087 1.8330 0.6601 0.4558  0.0193  0.7657  166 LYS C O   
7526  C CB  . LYS C 157 ? 0.9408 1.9331 0.6953 0.4893  0.0428  0.8190  166 LYS C CB  
7527  C CG  . LYS C 157 ? 0.9591 1.9580 0.7346 0.4978  0.0573  0.8482  166 LYS C CG  
7528  C CD  . LYS C 157 ? 1.0014 2.0257 0.7744 0.5094  0.0667  0.8689  166 LYS C CD  
7529  C CE  . LYS C 157 ? 1.0240 2.0582 0.8134 0.5191  0.0775  0.8991  166 LYS C CE  
7530  N NZ  . LYS C 157 ? 1.0408 2.1204 0.8213 0.5319  0.0771  0.9169  166 LYS C NZ  
7531  N N   . ILE C 158 ? 0.9273 1.8854 0.6418 0.4686  0.0098  0.7585  167 ILE C N   
7532  C CA  . ILE C 158 ? 0.9237 1.8506 0.6247 0.4594  0.0010  0.7316  167 ILE C CA  
7533  C C   . ILE C 158 ? 0.9200 1.8246 0.6211 0.4435  -0.0125 0.7160  167 ILE C C   
7534  O O   . ILE C 158 ? 0.9092 1.7807 0.6173 0.4337  -0.0109 0.7031  167 ILE C O   
7535  C CB  . ILE C 158 ? 0.9410 1.8794 0.6091 0.4675  -0.0103 0.7161  167 ILE C CB  
7536  C CG1 . ILE C 158 ? 0.9416 1.8965 0.6135 0.4807  0.0058  0.7294  167 ILE C CG1 
7537  C CG2 . ILE C 158 ? 0.9319 1.8361 0.5797 0.4577  -0.0255 0.6852  167 ILE C CG2 
7538  C CD1 . ILE C 158 ? 0.9743 1.9504 0.6147 0.4939  -0.0024 0.7188  167 ILE C CD1 
7539  N N   . LYS C 159 ? 0.9310 1.8557 0.6251 0.4399  -0.0258 0.7182  168 LYS C N   
7540  C CA  . LYS C 159 ? 0.9306 1.8398 0.6265 0.4231  -0.0390 0.7068  168 LYS C CA  
7541  C C   . LYS C 159 ? 0.9070 1.7965 0.6332 0.4184  -0.0242 0.7142  168 LYS C C   
7542  O O   . LYS C 159 ? 0.8983 1.7567 0.6266 0.4069  -0.0273 0.6985  168 LYS C O   
7543  C CB  . LYS C 159 ? 0.9436 1.8853 0.6348 0.4200  -0.0519 0.7159  168 LYS C CB  
7544  C CG  . LYS C 159 ? 0.9590 1.8929 0.6588 0.4024  -0.0624 0.7112  168 LYS C CG  
7545  C CD  . LYS C 159 ? 1.0046 1.9787 0.7092 0.4010  -0.0694 0.7280  168 LYS C CD  
7546  C CE  . LYS C 159 ? 1.0014 1.9743 0.7241 0.3867  -0.0727 0.7301  168 LYS C CE  
7547  N NZ  . LYS C 159 ? 1.0211 2.0290 0.7376 0.3764  -0.0903 0.7371  168 LYS C NZ  
7548  N N   . SER C 160 ? 0.9029 1.8090 0.6509 0.4286  -0.0084 0.7382  169 SER C N   
7549  C CA  . SER C 160 ? 0.8924 1.7797 0.6667 0.4273  0.0051  0.7465  169 SER C CA  
7550  C C   . SER C 160 ? 0.8839 1.7329 0.6637 0.4238  0.0144  0.7358  169 SER C C   
7551  O O   . SER C 160 ? 0.8765 1.6995 0.6676 0.4146  0.0157  0.7273  169 SER C O   
7552  C CB  . SER C 160 ? 0.8955 1.8027 0.6870 0.4423  0.0202  0.7742  169 SER C CB  
7553  O OG  . SER C 160 ? 0.9178 1.8630 0.7069 0.4457  0.0122  0.7854  169 SER C OG  
7554  N N   . ALA C 161 ? 0.8882 1.7367 0.6599 0.4309  0.0206  0.7365  170 ALA C N   
7555  C CA  . ALA C 161 ? 0.8791 1.6963 0.6556 0.4277  0.0297  0.7282  170 ALA C CA  
7556  C C   . ALA C 161 ? 0.8714 1.6623 0.6360 0.4147  0.0176  0.7007  170 ALA C C   
7557  O O   . ALA C 161 ? 0.8597 1.6201 0.6355 0.4077  0.0239  0.6934  170 ALA C O   
7558  C CB  . ALA C 161 ? 0.8914 1.7230 0.6596 0.4379  0.0369  0.7357  170 ALA C CB  
7559  N N   . LEU C 162 ? 0.8803 1.6814 0.6204 0.4117  -0.0005 0.6859  171 LEU C N   
7560  C CA  . LEU C 162 ? 0.8803 1.6548 0.6047 0.3996  -0.0150 0.6598  171 LEU C CA  
7561  C C   . LEU C 162 ? 0.8690 1.6276 0.6080 0.3854  -0.0192 0.6562  171 LEU C C   
7562  O O   . LEU C 162 ? 0.8655 1.5937 0.6071 0.3758  -0.0201 0.6414  171 LEU C O   
7563  C CB  . LEU C 162 ? 0.9008 1.6865 0.5922 0.3997  -0.0361 0.6457  171 LEU C CB  
7564  C CG  . LEU C 162 ? 0.9047 1.6580 0.5753 0.3874  -0.0536 0.6183  171 LEU C CG  
7565  C CD1 . LEU C 162 ? 0.9121 1.6471 0.5745 0.3944  -0.0468 0.6064  171 LEU C CD1 
7566  C CD2 . LEU C 162 ? 0.9328 1.6917 0.5701 0.3845  -0.0780 0.6056  171 LEU C CD2 
7567  N N   . LEU C 163 ? 0.8690 1.6510 0.6174 0.3845  -0.0216 0.6701  172 LEU C N   
7568  C CA  . LEU C 163 ? 0.8575 1.6322 0.6212 0.3727  -0.0246 0.6695  172 LEU C CA  
7569  C C   . LEU C 163 ? 0.8409 1.5882 0.6271 0.3734  -0.0075 0.6713  172 LEU C C   
7570  O O   . LEU C 163 ? 0.8320 1.5550 0.6224 0.3615  -0.0112 0.6578  172 LEU C O   
7571  C CB  . LEU C 163 ? 0.8586 1.6695 0.6332 0.3767  -0.0247 0.6896  172 LEU C CB  
7572  C CG  . LEU C 163 ? 0.8786 1.7204 0.6327 0.3741  -0.0428 0.6903  172 LEU C CG  
7573  C CD1 . LEU C 163 ? 0.8988 1.7798 0.6666 0.3848  -0.0358 0.7151  172 LEU C CD1 
7574  C CD2 . LEU C 163 ? 0.8824 1.7178 0.6236 0.3538  -0.0650 0.6748  172 LEU C CD2 
7575  N N   . SER C 164 ? 0.8376 1.5879 0.6367 0.3870  0.0102  0.6882  173 SER C N   
7576  C CA  . SER C 164 ? 0.8254 1.5475 0.6436 0.3888  0.0265  0.6921  173 SER C CA  
7577  C C   . SER C 164 ? 0.8174 1.5073 0.6288 0.3796  0.0249  0.6713  173 SER C C   
7578  O O   . SER C 164 ? 0.8070 1.4692 0.6304 0.3728  0.0299  0.6644  173 SER C O   
7579  C CB  . SER C 164 ? 0.8345 1.5646 0.6607 0.4033  0.0420  0.7137  173 SER C CB  
7580  O OG  . SER C 164 ? 0.8326 1.5507 0.6788 0.4091  0.0544  0.7284  173 SER C OG  
7581  N N   . THR C 165 ? 0.8240 1.5187 0.6148 0.3806  0.0178  0.6610  174 THR C N   
7582  C CA  . THR C 165 ? 0.8208 1.4886 0.6020 0.3739  0.0150  0.6408  174 THR C CA  
7583  C C   . THR C 165 ? 0.8142 1.4636 0.5895 0.3593  0.0004  0.6213  174 THR C C   
7584  O O   . THR C 165 ? 0.8063 1.4274 0.5881 0.3514  0.0031  0.6100  174 THR C O   
7585  C CB  . THR C 165 ? 0.8365 1.5167 0.5931 0.3815  0.0092  0.6331  174 THR C CB  
7586  O OG1 . THR C 165 ? 0.8427 1.5419 0.6062 0.3940  0.0238  0.6525  174 THR C OG1 
7587  C CG2 . THR C 165 ? 0.8269 1.4799 0.5716 0.3758  0.0048  0.6107  174 THR C CG2 
7588  N N   . ASN C 166 ? 0.8215 1.4873 0.5842 0.3544  -0.0158 0.6185  175 ASN C N   
7589  C CA  . ASN C 166 ? 0.8231 1.4728 0.5790 0.3382  -0.0317 0.6022  175 ASN C CA  
7590  C C   . ASN C 166 ? 0.8048 1.4398 0.5856 0.3306  -0.0232 0.6048  175 ASN C C   
7591  O O   . ASN C 166 ? 0.7958 1.4028 0.5763 0.3203  -0.0265 0.5892  175 ASN C O   
7592  C CB  . ASN C 166 ? 0.8389 1.5133 0.5805 0.3327  -0.0500 0.6044  175 ASN C CB  
7593  C CG  . ASN C 166 ? 0.8728 1.5497 0.5817 0.3365  -0.0649 0.5929  175 ASN C CG  
7594  O OD1 . ASN C 166 ? 0.8854 1.5497 0.5828 0.3454  -0.0602 0.5840  175 ASN C OD1 
7595  N ND2 . ASN C 166 ? 0.9022 1.5964 0.5944 0.3300  -0.0837 0.5928  175 ASN C ND2 
7596  N N   . LYS C 167 ? 0.7997 1.4534 0.6009 0.3376  -0.0121 0.6246  176 LYS C N   
7597  C CA  . LYS C 167 ? 0.7872 1.4291 0.6112 0.3353  -0.0022 0.6290  176 LYS C CA  
7598  C C   . LYS C 167 ? 0.7768 1.3849 0.6102 0.3370  0.0117  0.6232  176 LYS C C   
7599  O O   . LYS C 167 ? 0.7688 1.3574 0.6151 0.3315  0.0159  0.6184  176 LYS C O   
7600  C CB  . LYS C 167 ? 0.7906 1.4574 0.6310 0.3480  0.0085  0.6520  176 LYS C CB  
7601  C CG  . LYS C 167 ? 0.8148 1.5182 0.6515 0.3452  -0.0039 0.6599  176 LYS C CG  
7602  C CD  . LYS C 167 ? 0.8492 1.5789 0.6991 0.3620  0.0079  0.6836  176 LYS C CD  
7603  C CE  . LYS C 167 ? 0.8670 1.6334 0.7217 0.3592  -0.0010 0.6931  176 LYS C CE  
7604  N NZ  . LYS C 167 ? 0.8928 1.6879 0.7557 0.3778  0.0091  0.7163  176 LYS C NZ  
7605  N N   . ALA C 168 ? 0.7783 1.3817 0.6055 0.3447  0.0189  0.6249  177 ALA C N   
7606  C CA  . ALA C 168 ? 0.7675 1.3410 0.6021 0.3438  0.0303  0.6195  177 ALA C CA  
7607  C C   . ALA C 168 ? 0.7569 1.3072 0.5804 0.3311  0.0200  0.5953  177 ALA C C   
7608  O O   . ALA C 168 ? 0.7488 1.2724 0.5826 0.3253  0.0261  0.5879  177 ALA C O   
7609  C CB  . ALA C 168 ? 0.7787 1.3594 0.6092 0.3540  0.0397  0.6293  177 ALA C CB  
7610  N N   . VAL C 169 ? 0.7576 1.3161 0.5583 0.3273  0.0035  0.5830  178 VAL C N   
7611  C CA  . VAL C 169 ? 0.7501 1.2843 0.5358 0.3171  -0.0078 0.5599  178 VAL C CA  
7612  C C   . VAL C 169 ? 0.7427 1.2659 0.5360 0.3031  -0.0158 0.5532  178 VAL C C   
7613  O O   . VAL C 169 ? 0.7400 1.2369 0.5325 0.2940  -0.0185 0.5380  178 VAL C O   
7614  C CB  . VAL C 169 ? 0.7670 1.3078 0.5212 0.3191  -0.0247 0.5476  178 VAL C CB  
7615  C CG1 . VAL C 169 ? 0.7617 1.2762 0.4979 0.3062  -0.0421 0.5245  178 VAL C CG1 
7616  C CG2 . VAL C 169 ? 0.7703 1.3158 0.5159 0.3325  -0.0157 0.5484  178 VAL C CG2 
7617  N N   . VAL C 170 ? 0.7436 1.2897 0.5446 0.3016  -0.0194 0.5655  179 VAL C N   
7618  C CA  . VAL C 170 ? 0.7367 1.2799 0.5481 0.2890  -0.0255 0.5628  179 VAL C CA  
7619  C C   . VAL C 170 ? 0.7174 1.2403 0.5514 0.2906  -0.0090 0.5641  179 VAL C C   
7620  O O   . VAL C 170 ? 0.7071 1.2083 0.5428 0.2796  -0.0128 0.5507  179 VAL C O   
7621  C CB  . VAL C 170 ? 0.7438 1.3227 0.5608 0.2890  -0.0310 0.5787  179 VAL C CB  
7622  C CG1 . VAL C 170 ? 0.7393 1.3227 0.5764 0.2829  -0.0280 0.5835  179 VAL C CG1 
7623  C CG2 . VAL C 170 ? 0.7657 1.3569 0.5583 0.2787  -0.0539 0.5719  179 VAL C CG2 
7624  N N   . SER C 171 ? 0.7150 1.2426 0.5644 0.3042  0.0082  0.5801  180 SER C N   
7625  C CA  . SER C 171 ? 0.7089 1.2133 0.5765 0.3069  0.0230  0.5817  180 SER C CA  
7626  C C   . SER C 171 ? 0.7079 1.1802 0.5710 0.2984  0.0231  0.5636  180 SER C C   
7627  O O   . SER C 171 ? 0.7043 1.1585 0.5752 0.2903  0.0231  0.5543  180 SER C O   
7628  C CB  . SER C 171 ? 0.7147 1.2207 0.5926 0.3222  0.0392  0.6000  180 SER C CB  
7629  O OG  . SER C 171 ? 0.7155 1.2321 0.6074 0.3301  0.0451  0.6137  180 SER C OG  
7630  N N   . LEU C 172 ? 0.7183 1.1864 0.5682 0.3011  0.0231  0.5587  181 LEU C N   
7631  C CA  . LEU C 172 ? 0.7147 1.1560 0.5596 0.2950  0.0239  0.5424  181 LEU C CA  
7632  C C   . LEU C 172 ? 0.7147 1.1430 0.5482 0.2816  0.0083  0.5226  181 LEU C C   
7633  O O   . LEU C 172 ? 0.7088 1.1128 0.5472 0.2744  0.0104  0.5110  181 LEU C O   
7634  C CB  . LEU C 172 ? 0.7237 1.1704 0.5545 0.3024  0.0259  0.5417  181 LEU C CB  
7635  C CG  . LEU C 172 ? 0.7104 1.1349 0.5425 0.3001  0.0333  0.5322  181 LEU C CG  
7636  C CD1 . LEU C 172 ? 0.7153 1.1275 0.5698 0.3014  0.0502  0.5458  181 LEU C CD1 
7637  C CD2 . LEU C 172 ? 0.7058 1.1424 0.5205 0.3079  0.0325  0.5297  181 LEU C CD2 
7638  N N   . SER C 173 ? 0.7265 1.1702 0.5442 0.2774  -0.0082 0.5194  182 SER C N   
7639  C CA  . SER C 173 ? 0.7341 1.1642 0.5394 0.2628  -0.0254 0.5028  182 SER C CA  
7640  C C   . SER C 173 ? 0.7241 1.1466 0.5489 0.2532  -0.0224 0.5030  182 SER C C   
7641  O O   . SER C 173 ? 0.7220 1.1212 0.5450 0.2434  -0.0267 0.4885  182 SER C O   
7642  C CB  . SER C 173 ? 0.7484 1.1975 0.5348 0.2583  -0.0444 0.5033  182 SER C CB  
7643  O OG  . SER C 173 ? 0.7683 1.2190 0.5315 0.2670  -0.0498 0.4981  182 SER C OG  
7644  N N   . ASN C 174 ? 0.7267 1.1700 0.5694 0.2578  -0.0148 0.5196  183 ASN C N   
7645  C CA  . ASN C 174 ? 0.7227 1.1643 0.5835 0.2521  -0.0112 0.5214  183 ASN C CA  
7646  C C   . ASN C 174 ? 0.7107 1.1248 0.5852 0.2555  0.0041  0.5168  183 ASN C C   
7647  O O   . ASN C 174 ? 0.7076 1.1085 0.5896 0.2470  0.0033  0.5087  183 ASN C O   
7648  C CB  . ASN C 174 ? 0.7300 1.2038 0.6046 0.2604  -0.0062 0.5410  183 ASN C CB  
7649  C CG  . ASN C 174 ? 0.7650 1.2699 0.6279 0.2533  -0.0233 0.5462  183 ASN C CG  
7650  O OD1 . ASN C 174 ? 0.8007 1.3004 0.6495 0.2371  -0.0411 0.5344  183 ASN C OD1 
7651  N ND2 . ASN C 174 ? 0.7779 1.3137 0.6451 0.2647  -0.0193 0.5641  183 ASN C ND2 
7652  N N   . GLY C 175 ? 0.7093 1.1154 0.5865 0.2669  0.0173  0.5229  184 GLY C N   
7653  C CA  . GLY C 175 ? 0.6965 1.0739 0.5836 0.2682  0.0303  0.5183  184 GLY C CA  
7654  C C   . GLY C 175 ? 0.6855 1.0399 0.5635 0.2565  0.0233  0.4980  184 GLY C C   
7655  O O   . GLY C 175 ? 0.6788 1.0140 0.5664 0.2505  0.0268  0.4904  184 GLY C O   
7656  N N   . VAL C 176 ? 0.6860 1.0425 0.5440 0.2548  0.0132  0.4892  185 VAL C N   
7657  C CA  . VAL C 176 ? 0.6781 1.0135 0.5227 0.2458  0.0042  0.4694  185 VAL C CA  
7658  C C   . VAL C 176 ? 0.6740 1.0037 0.5171 0.2317  -0.0093 0.4597  185 VAL C C   
7659  O O   . VAL C 176 ? 0.6671 0.9752 0.5133 0.2236  -0.0096 0.4477  185 VAL C O   
7660  C CB  . VAL C 176 ? 0.6905 1.0311 0.5101 0.2502  -0.0058 0.4624  185 VAL C CB  
7661  C CG1 . VAL C 176 ? 0.6944 1.0134 0.4952 0.2413  -0.0202 0.4414  185 VAL C CG1 
7662  C CG2 . VAL C 176 ? 0.6872 1.0315 0.5086 0.2621  0.0082  0.4691  185 VAL C CG2 
7663  N N   . SER C 177 ? 0.6783 1.0293 0.5172 0.2279  -0.0207 0.4665  186 SER C N   
7664  C CA  . SER C 177 ? 0.6759 1.0276 0.5143 0.2128  -0.0343 0.4613  186 SER C CA  
7665  C C   . SER C 177 ? 0.6573 0.9993 0.5174 0.2098  -0.0234 0.4610  186 SER C C   
7666  O O   . SER C 177 ? 0.6566 0.9852 0.5151 0.1969  -0.0318 0.4499  186 SER C O   
7667  C CB  . SER C 177 ? 0.6845 1.0690 0.5231 0.2108  -0.0431 0.4752  186 SER C CB  
7668  O OG  . SER C 177 ? 0.6937 1.0835 0.5345 0.1948  -0.0558 0.4732  186 SER C OG  
7669  N N   . VAL C 178 ? 0.6456 0.9923 0.5242 0.2222  -0.0054 0.4730  187 VAL C N   
7670  C CA  . VAL C 178 ? 0.6296 0.9649 0.5269 0.2225  0.0057  0.4726  187 VAL C CA  
7671  C C   . VAL C 178 ? 0.6268 0.9290 0.5247 0.2202  0.0127  0.4592  187 VAL C C   
7672  O O   . VAL C 178 ? 0.6219 0.9103 0.5244 0.2113  0.0107  0.4491  187 VAL C O   
7673  C CB  . VAL C 178 ? 0.6258 0.9748 0.5391 0.2373  0.0199  0.4899  187 VAL C CB  
7674  C CG1 . VAL C 178 ? 0.6131 0.9390 0.5408 0.2417  0.0335  0.4876  187 VAL C CG1 
7675  C CG2 . VAL C 178 ? 0.6231 1.0057 0.5404 0.2362  0.0125  0.5004  187 VAL C CG2 
7676  N N   . LEU C 179 ? 0.6328 0.9254 0.5265 0.2279  0.0207  0.4600  188 LEU C N   
7677  C CA  . LEU C 179 ? 0.6275 0.8933 0.5214 0.2255  0.0272  0.4489  188 LEU C CA  
7678  C C   . LEU C 179 ? 0.6253 0.8782 0.5058 0.2137  0.0140  0.4305  188 LEU C C   
7679  O O   . LEU C 179 ? 0.6179 0.8504 0.5033 0.2080  0.0172  0.4201  188 LEU C O   
7680  C CB  . LEU C 179 ? 0.6356 0.9020 0.5238 0.2341  0.0346  0.4540  188 LEU C CB  
7681  C CG  . LEU C 179 ? 0.6292 0.8736 0.5205 0.2320  0.0432  0.4467  188 LEU C CG  
7682  C CD1 . LEU C 179 ? 0.6311 0.8621 0.5413 0.2346  0.0576  0.4565  188 LEU C CD1 
7683  C CD2 . LEU C 179 ? 0.6340 0.8869 0.5134 0.2381  0.0448  0.4485  188 LEU C CD2 
7684  N N   . THR C 180 ? 0.6366 0.8995 0.4984 0.2102  -0.0017 0.4264  189 THR C N   
7685  C CA  . THR C 180 ? 0.6443 0.8930 0.4908 0.1981  -0.0178 0.4100  189 THR C CA  
7686  C C   . THR C 180 ? 0.6387 0.8862 0.4983 0.1866  -0.0208 0.4091  189 THR C C   
7687  O O   . THR C 180 ? 0.6309 0.8585 0.4941 0.1800  -0.0196 0.3981  189 THR C O   
7688  C CB  . THR C 180 ? 0.6611 0.9191 0.4836 0.1960  -0.0362 0.4079  189 THR C CB  
7689  O OG1 . THR C 180 ? 0.6731 0.9296 0.4801 0.2075  -0.0343 0.4048  189 THR C OG1 
7690  C CG2 . THR C 180 ? 0.6741 0.9143 0.4795 0.1814  -0.0557 0.3928  189 THR C CG2 
7691  N N   . SER C 181 ? 0.6424 0.9144 0.5097 0.1848  -0.0242 0.4216  190 SER C N   
7692  C CA  . SER C 181 ? 0.6338 0.9128 0.5145 0.1754  -0.0264 0.4233  190 SER C CA  
7693  C C   . SER C 181 ? 0.6232 0.8822 0.5193 0.1774  -0.0123 0.4173  190 SER C C   
7694  O O   . SER C 181 ? 0.6207 0.8727 0.5203 0.1668  -0.0172 0.4098  190 SER C O   
7695  C CB  . SER C 181 ? 0.6319 0.9450 0.5249 0.1806  -0.0237 0.4416  190 SER C CB  
7696  O OG  . SER C 181 ? 0.6200 0.9454 0.5257 0.1728  -0.0256 0.4440  190 SER C OG  
7697  N N   . LYS C 182 ? 0.6234 0.8723 0.5275 0.1899  0.0041  0.4207  191 LYS C N   
7698  C CA  . LYS C 182 ? 0.6158 0.8443 0.5341 0.1923  0.0177  0.4166  191 LYS C CA  
7699  C C   . LYS C 182 ? 0.6117 0.8127 0.5240 0.1863  0.0181  0.4008  191 LYS C C   
7700  O O   . LYS C 182 ? 0.6058 0.7910 0.5273 0.1822  0.0232  0.3937  191 LYS C O   
7701  C CB  . LYS C 182 ? 0.6197 0.8474 0.5485 0.2068  0.0338  0.4293  191 LYS C CB  
7702  C CG  . LYS C 182 ? 0.6402 0.8861 0.5812 0.2156  0.0389  0.4428  191 LYS C CG  
7703  C CD  . LYS C 182 ? 0.6682 0.9037 0.6210 0.2146  0.0439  0.4378  191 LYS C CD  
7704  C CE  . LYS C 182 ? 0.6906 0.9531 0.6465 0.2088  0.0343  0.4398  191 LYS C CE  
7705  N NZ  . LYS C 182 ? 0.7134 0.9737 0.6820 0.2138  0.0416  0.4391  191 LYS C NZ  
7706  N N   . VAL C 183 ? 0.6166 0.8136 0.5131 0.1874  0.0134  0.3958  192 VAL C N   
7707  C CA  . VAL C 183 ? 0.6100 0.7855 0.4985 0.1835  0.0128  0.3811  192 VAL C CA  
7708  C C   . VAL C 183 ? 0.6092 0.7747 0.4900 0.1705  -0.0013 0.3676  192 VAL C C   
7709  O O   . VAL C 183 ? 0.6045 0.7515 0.4871 0.1655  0.0006  0.3563  192 VAL C O   
7710  C CB  . VAL C 183 ? 0.6202 0.7989 0.4912 0.1906  0.0101  0.3794  192 VAL C CB  
7711  C CG1 . VAL C 183 ? 0.6178 0.7794 0.4716 0.1863  0.0010  0.3618  192 VAL C CG1 
7712  C CG2 . VAL C 183 ? 0.6214 0.8025 0.5030 0.2000  0.0266  0.3901  192 VAL C CG2 
7713  N N   . LEU C 184 ? 0.6187 0.7969 0.4910 0.1640  -0.0159 0.3698  193 LEU C N   
7714  C CA  . LEU C 184 ? 0.6231 0.7923 0.4885 0.1494  -0.0306 0.3597  193 LEU C CA  
7715  C C   . LEU C 184 ? 0.6129 0.7791 0.4991 0.1452  -0.0212 0.3596  193 LEU C C   
7716  O O   . LEU C 184 ? 0.6127 0.7599 0.4976 0.1382  -0.0231 0.3473  193 LEU C O   
7717  C CB  . LEU C 184 ? 0.6332 0.8208 0.4899 0.1407  -0.0474 0.3664  193 LEU C CB  
7718  C CG  . LEU C 184 ? 0.6400 0.8181 0.4892 0.1228  -0.0644 0.3581  193 LEU C CG  
7719  C CD1 . LEU C 184 ? 0.6535 0.8059 0.4730 0.1183  -0.0816 0.3433  193 LEU C CD1 
7720  C CD2 . LEU C 184 ? 0.6547 0.8611 0.5085 0.1119  -0.0755 0.3712  193 LEU C CD2 
7721  N N   . ASP C 185 ? 0.6140 0.7990 0.5183 0.1510  -0.0112 0.3729  194 ASP C N   
7722  C CA  . ASP C 185 ? 0.6090 0.7924 0.5318 0.1507  -0.0014 0.3732  194 ASP C CA  
7723  C C   . ASP C 185 ? 0.6025 0.7584 0.5302 0.1533  0.0103  0.3630  194 ASP C C   
7724  O O   . ASP C 185 ? 0.5956 0.7406 0.5291 0.1464  0.0106  0.3545  194 ASP C O   
7725  C CB  . ASP C 185 ? 0.6133 0.8189 0.5509 0.1625  0.0089  0.3893  194 ASP C CB  
7726  C CG  . ASP C 185 ? 0.6352 0.8730 0.5700 0.1589  -0.0025 0.4005  194 ASP C CG  
7727  O OD1 . ASP C 185 ? 0.6542 0.8941 0.5758 0.1447  -0.0195 0.3953  194 ASP C OD1 
7728  O OD2 . ASP C 185 ? 0.6518 0.9120 0.5961 0.1700  0.0046  0.4146  194 ASP C OD2 
7729  N N   . LEU C 186 ? 0.6058 0.7525 0.5313 0.1622  0.0194  0.3647  195 LEU C N   
7730  C CA  . LEU C 186 ? 0.6007 0.7245 0.5307 0.1626  0.0292  0.3566  195 LEU C CA  
7731  C C   . LEU C 186 ? 0.5985 0.7079 0.5177 0.1521  0.0196  0.3404  195 LEU C C   
7732  O O   . LEU C 186 ? 0.5905 0.6866 0.5172 0.1467  0.0227  0.3324  195 LEU C O   
7733  C CB  . LEU C 186 ? 0.6096 0.7306 0.5365 0.1712  0.0377  0.3623  195 LEU C CB  
7734  C CG  . LEU C 186 ? 0.6061 0.7120 0.5464 0.1753  0.0529  0.3667  195 LEU C CG  
7735  C CD1 . LEU C 186 ? 0.6036 0.7024 0.5389 0.1759  0.0578  0.3652  195 LEU C CD1 
7736  C CD2 . LEU C 186 ? 0.5959 0.6867 0.5458 0.1693  0.0552  0.3580  195 LEU C CD2 
7737  N N   . LYS C 187 ? 0.6099 0.7207 0.5099 0.1503  0.0071  0.3352  196 LYS C N   
7738  C CA  . LYS C 187 ? 0.6157 0.7109 0.5013 0.1412  -0.0052 0.3196  196 LYS C CA  
7739  C C   . LYS C 187 ? 0.6110 0.7050 0.5041 0.1293  -0.0116 0.3164  196 LYS C C   
7740  O O   . LYS C 187 ? 0.6076 0.6865 0.5040 0.1237  -0.0102 0.3064  196 LYS C O   
7741  C CB  . LYS C 187 ? 0.6323 0.7279 0.4921 0.1415  -0.0217 0.3153  196 LYS C CB  
7742  C CG  . LYS C 187 ? 0.6328 0.7098 0.4738 0.1310  -0.0395 0.3005  196 LYS C CG  
7743  C CD  . LYS C 187 ? 0.6363 0.7203 0.4743 0.1176  -0.0553 0.3045  196 LYS C CD  
7744  C CE  . LYS C 187 ? 0.6625 0.7237 0.4787 0.1064  -0.0749 0.2909  196 LYS C CE  
7745  N NZ  . LYS C 187 ? 0.6764 0.7451 0.4932 0.0893  -0.0901 0.2963  196 LYS C NZ  
7746  N N   . ASN C 188 ? 0.6172 0.7303 0.5135 0.1253  -0.0184 0.3261  197 ASN C N   
7747  C CA  . ASN C 188 ? 0.6191 0.7371 0.5217 0.1131  -0.0259 0.3250  197 ASN C CA  
7748  C C   . ASN C 188 ? 0.6084 0.7238 0.5313 0.1147  -0.0120 0.3241  197 ASN C C   
7749  O O   . ASN C 188 ? 0.6086 0.7191 0.5336 0.1044  -0.0175 0.3172  197 ASN C O   
7750  C CB  . ASN C 188 ? 0.6266 0.7718 0.5290 0.1081  -0.0363 0.3377  197 ASN C CB  
7751  C CG  . ASN C 188 ? 0.6534 0.7930 0.5324 0.0957  -0.0587 0.3332  197 ASN C CG  
7752  O OD1 . ASN C 188 ? 0.6797 0.8285 0.5466 0.0979  -0.0666 0.3391  197 ASN C OD1 
7753  N ND2 . ASN C 188 ? 0.6623 0.7844 0.5330 0.0826  -0.0703 0.3225  197 ASN C ND2 
7754  N N   . TYR C 189 ? 0.6040 0.7205 0.5400 0.1275  0.0047  0.3306  198 TYR C N   
7755  C CA  . TYR C 189 ? 0.5942 0.7011 0.5453 0.1301  0.0170  0.3275  198 TYR C CA  
7756  C C   . TYR C 189 ? 0.5850 0.6678 0.5305 0.1232  0.0159  0.3125  198 TYR C C   
7757  O O   . TYR C 189 ? 0.5790 0.6576 0.5266 0.1143  0.0112  0.3048  198 TYR C O   
7758  C CB  . TYR C 189 ? 0.6047 0.7071 0.5654 0.1441  0.0330  0.3356  198 TYR C CB  
7759  C CG  . TYR C 189 ? 0.6235 0.7178 0.5977 0.1481  0.0431  0.3341  198 TYR C CG  
7760  C CD1 . TYR C 189 ? 0.6601 0.7744 0.6426 0.1523  0.0433  0.3408  198 TYR C CD1 
7761  C CD2 . TYR C 189 ? 0.6348 0.7032 0.6123 0.1482  0.0519  0.3262  198 TYR C CD2 
7762  C CE1 . TYR C 189 ? 0.6775 0.7845 0.6699 0.1587  0.0521  0.3385  198 TYR C CE1 
7763  C CE2 . TYR C 189 ? 0.6604 0.7183 0.6478 0.1524  0.0600  0.3238  198 TYR C CE2 
7764  C CZ  . TYR C 189 ? 0.6785 0.7548 0.6725 0.1587  0.0601  0.3292  198 TYR C CZ  
7765  O OH  . TYR C 189 ? 0.6788 0.7452 0.6798 0.1654  0.0675  0.3260  198 TYR C OH  
7766  N N   . ILE C 190 ? 0.5880 0.6581 0.5259 0.1274  0.0195  0.3089  199 ILE C N   
7767  C CA  . ILE C 190 ? 0.5854 0.6363 0.5161 0.1221  0.0178  0.2950  199 ILE C CA  
7768  C C   . ILE C 190 ? 0.5904 0.6363 0.5100 0.1104  0.0022  0.2846  199 ILE C C   
7769  O O   . ILE C 190 ? 0.5842 0.6203 0.5095 0.1041  0.0032  0.2765  199 ILE C O   
7770  C CB  . ILE C 190 ? 0.5903 0.6375 0.5092 0.1286  0.0194  0.2940  199 ILE C CB  
7771  C CG1 . ILE C 190 ? 0.5831 0.6271 0.5147 0.1357  0.0358  0.3012  199 ILE C CG1 
7772  C CG2 . ILE C 190 ? 0.5872 0.6203 0.4916 0.1243  0.0116  0.2792  199 ILE C CG2 
7773  C CD1 . ILE C 190 ? 0.5892 0.6406 0.5125 0.1436  0.0384  0.3074  199 ILE C CD1 
7774  N N   . ASP C 191 ? 0.6086 0.6597 0.5115 0.1069  -0.0131 0.2851  200 ASP C N   
7775  C CA  . ASP C 191 ? 0.6245 0.6644 0.5126 0.0949  -0.0303 0.2751  200 ASP C CA  
7776  C C   . ASP C 191 ? 0.6150 0.6637 0.5150 0.0835  -0.0340 0.2778  200 ASP C C   
7777  O O   . ASP C 191 ? 0.6122 0.6480 0.5091 0.0743  -0.0403 0.2683  200 ASP C O   
7778  C CB  . ASP C 191 ? 0.6506 0.6895 0.5144 0.0925  -0.0486 0.2750  200 ASP C CB  
7779  C CG  . ASP C 191 ? 0.6866 0.7075 0.5315 0.0786  -0.0693 0.2648  200 ASP C CG  
7780  O OD1 . ASP C 191 ? 0.7061 0.7084 0.5484 0.0758  -0.0694 0.2530  200 ASP C OD1 
7781  O OD2 . ASP C 191 ? 0.7133 0.7380 0.5449 0.0696  -0.0868 0.2693  200 ASP C OD2 
7782  N N   . LYS C 192 ? 0.6104 0.6833 0.5238 0.0849  -0.0303 0.2912  201 LYS C N   
7783  C CA  . LYS C 192 ? 0.6104 0.6992 0.5327 0.0739  -0.0366 0.2957  201 LYS C CA  
7784  C C   . LYS C 192 ? 0.5974 0.6973 0.5422 0.0799  -0.0209 0.2992  201 LYS C C   
7785  O O   . LYS C 192 ? 0.5909 0.7079 0.5441 0.0726  -0.0246 0.3031  201 LYS C O   
7786  C CB  . LYS C 192 ? 0.6211 0.7326 0.5367 0.0667  -0.0510 0.3076  201 LYS C CB  
7787  C CG  . LYS C 192 ? 0.6549 0.7476 0.5438 0.0585  -0.0703 0.3008  201 LYS C CG  
7788  C CD  . LYS C 192 ? 0.7085 0.8190 0.5874 0.0461  -0.0893 0.3114  201 LYS C CD  
7789  C CE  . LYS C 192 ? 0.7619 0.8464 0.6095 0.0420  -0.1082 0.3028  201 LYS C CE  
7790  N NZ  . LYS C 192 ? 0.8053 0.9059 0.6409 0.0350  -0.1240 0.3140  201 LYS C NZ  
7791  N N   . GLN C 193 ? 0.5997 0.6885 0.5526 0.0928  -0.0043 0.2974  202 GLN C N   
7792  C CA  . GLN C 193 ? 0.5962 0.6893 0.5666 0.1012  0.0102  0.2999  202 GLN C CA  
7793  C C   . GLN C 193 ? 0.5847 0.6510 0.5583 0.1026  0.0198  0.2878  202 GLN C C   
7794  O O   . GLN C 193 ? 0.5789 0.6422 0.5590 0.0980  0.0210  0.2813  202 GLN C O   
7795  C CB  . GLN C 193 ? 0.6091 0.7128 0.5859 0.1165  0.0209  0.3122  202 GLN C CB  
7796  C CG  . GLN C 193 ? 0.6508 0.7881 0.6299 0.1180  0.0149  0.3264  202 GLN C CG  
7797  C CD  . GLN C 193 ? 0.7003 0.8595 0.6922 0.1206  0.0181  0.3309  202 GLN C CD  
7798  O OE1 . GLN C 193 ? 0.7268 0.8764 0.7273 0.1315  0.0306  0.3281  202 GLN C OE1 
7799  N NE2 . GLN C 193 ? 0.7130 0.9023 0.7051 0.1106  0.0060  0.3384  202 GLN C NE2 
7800  N N   . LEU C 194 ? 0.5799 0.6298 0.5491 0.1085  0.0264  0.2858  203 LEU C N   
7801  C CA  . LEU C 194 ? 0.5694 0.5965 0.5413 0.1091  0.0354  0.2767  203 LEU C CA  
7802  C C   . LEU C 194 ? 0.5668 0.5816 0.5296 0.0984  0.0270  0.2631  203 LEU C C   
7803  O O   . LEU C 194 ? 0.5576 0.5633 0.5259 0.0934  0.0291  0.2546  203 LEU C O   
7804  C CB  . LEU C 194 ? 0.5729 0.5930 0.5419 0.1170  0.0429  0.2818  203 LEU C CB  
7805  C CG  . LEU C 194 ? 0.5677 0.5681 0.5382 0.1155  0.0507  0.2746  203 LEU C CG  
7806  C CD1 . LEU C 194 ? 0.5777 0.5667 0.5603 0.1207  0.0628  0.2786  203 LEU C CD1 
7807  C CD2 . LEU C 194 ? 0.5725 0.5738 0.5339 0.1188  0.0513  0.2776  203 LEU C CD2 
7808  N N   . LEU C 195 ? 0.5746 0.5887 0.5215 0.0963  0.0168  0.2610  204 LEU C N   
7809  C CA  . LEU C 195 ? 0.5745 0.5744 0.5078 0.0898  0.0078  0.2482  204 LEU C CA  
7810  C C   . LEU C 195 ? 0.5660 0.5620 0.5009 0.0788  0.0003  0.2407  204 LEU C C   
7811  O O   . LEU C 195 ? 0.5669 0.5486 0.4984 0.0757  0.0003  0.2299  204 LEU C O   
7812  C CB  . LEU C 195 ? 0.5887 0.5889 0.5009 0.0905  -0.0058 0.2476  204 LEU C CB  
7813  C CG  . LEU C 195 ? 0.6033 0.5869 0.4977 0.0915  -0.0116 0.2349  204 LEU C CG  
7814  C CD1 . LEU C 195 ? 0.5939 0.5781 0.4912 0.1020  0.0020  0.2359  204 LEU C CD1 
7815  C CD2 . LEU C 195 ? 0.6395 0.6178 0.5079 0.0903  -0.0308 0.2316  204 LEU C CD2 
7816  N N   . PRO C 196 ? 0.5642 0.5756 0.5037 0.0726  -0.0066 0.2474  205 PRO C N   
7817  C CA  . PRO C 196 ? 0.5574 0.5689 0.5007 0.0617  -0.0127 0.2423  205 PRO C CA  
7818  C C   . PRO C 196 ? 0.5475 0.5536 0.5061 0.0646  0.0012  0.2371  205 PRO C C   
7819  O O   . PRO C 196 ? 0.5465 0.5426 0.5039 0.0572  -0.0021 0.2274  205 PRO C O   
7820  C CB  . PRO C 196 ? 0.5549 0.5927 0.5049 0.0574  -0.0183 0.2548  205 PRO C CB  
7821  C CG  . PRO C 196 ? 0.5702 0.6158 0.5111 0.0610  -0.0237 0.2631  205 PRO C CG  
7822  C CD  . PRO C 196 ? 0.5727 0.6044 0.5111 0.0735  -0.0124 0.2602  205 PRO C CD  
7823  N N   . ILE C 197 ? 0.5418 0.5523 0.5130 0.0752  0.0155  0.2431  206 ILE C N   
7824  C CA  . ILE C 197 ? 0.5346 0.5379 0.5182 0.0777  0.0266  0.2381  206 ILE C CA  
7825  C C   . ILE C 197 ? 0.5307 0.5127 0.5133 0.0799  0.0349  0.2306  206 ILE C C   
7826  O O   . ILE C 197 ? 0.5238 0.4957 0.5143 0.0802  0.0427  0.2249  206 ILE C O   
7827  C CB  . ILE C 197 ? 0.5391 0.5557 0.5354 0.0876  0.0358  0.2468  206 ILE C CB  
7828  C CG1 . ILE C 197 ? 0.5548 0.5570 0.5548 0.0993  0.0489  0.2500  206 ILE C CG1 
7829  C CG2 . ILE C 197 ? 0.5498 0.5960 0.5467 0.0875  0.0280  0.2589  206 ILE C CG2 
7830  C CD1 . ILE C 197 ? 0.5830 0.5860 0.5927 0.1106  0.0587  0.2530  206 ILE C CD1 
7831  N N   . VAL C 198 ? 0.5410 0.5181 0.5132 0.0816  0.0326  0.2309  207 VAL C N   
7832  C CA  . VAL C 198 ? 0.5490 0.5111 0.5192 0.0817  0.0385  0.2238  207 VAL C CA  
7833  C C   . VAL C 198 ? 0.5470 0.5023 0.5103 0.0733  0.0303  0.2117  207 VAL C C   
7834  O O   . VAL C 198 ? 0.5448 0.4919 0.5149 0.0697  0.0352  0.2044  207 VAL C O   
7835  C CB  . VAL C 198 ? 0.5575 0.5207 0.5175 0.0871  0.0385  0.2275  207 VAL C CB  
7836  C CG1 . VAL C 198 ? 0.5533 0.5072 0.5100 0.0859  0.0424  0.2195  207 VAL C CG1 
7837  C CG2 . VAL C 198 ? 0.5711 0.5391 0.5383 0.0953  0.0477  0.2403  207 VAL C CG2 
7838  N N   . ASN C 199 ? 0.5589 0.5160 0.5072 0.0701  0.0166  0.2095  208 ASN C N   
7839  C CA  . ASN C 199 ? 0.5683 0.5148 0.5067 0.0631  0.0075  0.1978  208 ASN C CA  
7840  C C   . ASN C 199 ? 0.5627 0.5124 0.5079 0.0534  0.0021  0.1959  208 ASN C C   
7841  O O   . ASN C 199 ? 0.5650 0.5062 0.5017 0.0459  -0.0077 0.1878  208 ASN C O   
7842  C CB  . ASN C 199 ? 0.5819 0.5207 0.4967 0.0656  -0.0049 0.1928  208 ASN C CB  
7843  C CG  . ASN C 199 ? 0.5905 0.5334 0.4929 0.0627  -0.0195 0.1984  208 ASN C CG  
7844  O OD1 . ASN C 199 ? 0.5958 0.5519 0.5082 0.0586  -0.0202 0.2076  208 ASN C OD1 
7845  N ND2 . ASN C 199 ? 0.6009 0.5330 0.4799 0.0654  -0.0321 0.1930  208 ASN C ND2 
7846  N N   . LYS C 200 ? 0.5590 0.5217 0.5195 0.0546  0.0091  0.2038  209 LYS C N   
7847  C CA  . LYS C 200 ? 0.5537 0.5219 0.5244 0.0483  0.0093  0.2013  209 LYS C CA  
7848  C C   . LYS C 200 ? 0.5442 0.5005 0.5243 0.0509  0.0219  0.1932  209 LYS C C   
7849  O O   . LYS C 200 ? 0.5370 0.4879 0.5177 0.0443  0.0196  0.1845  209 LYS C O   
7850  C CB  . LYS C 200 ? 0.5546 0.5447 0.5361 0.0509  0.0113  0.2126  209 LYS C CB  
7851  C CG  . LYS C 200 ? 0.5687 0.5746 0.5502 0.0399  -0.0006 0.2153  209 LYS C CG  
7852  C CD  . LYS C 200 ? 0.5972 0.6293 0.5808 0.0403  -0.0058 0.2300  209 LYS C CD  
7853  C CE  . LYS C 200 ? 0.6033 0.6594 0.6032 0.0472  0.0035  0.2368  209 LYS C CE  
7854  N NZ  . LYS C 200 ? 0.6287 0.7037 0.6321 0.0572  0.0070  0.2497  209 LYS C NZ  
7855  N N   . GLN C 201 ? 0.5439 0.4953 0.5304 0.0595  0.0341  0.1966  210 GLN C N   
7856  C CA  . GLN C 201 ? 0.5422 0.4797 0.5353 0.0603  0.0445  0.1900  210 GLN C CA  
7857  C C   . GLN C 201 ? 0.5450 0.4732 0.5295 0.0549  0.0407  0.1803  210 GLN C C   
7858  O O   . GLN C 201 ? 0.5405 0.4618 0.5289 0.0503  0.0433  0.1717  210 GLN C O   
7859  C CB  . GLN C 201 ? 0.5486 0.4796 0.5455 0.0679  0.0548  0.1970  210 GLN C CB  
7860  C CG  . GLN C 201 ? 0.5612 0.4962 0.5654 0.0764  0.0605  0.2060  210 GLN C CG  
7861  C CD  . GLN C 201 ? 0.5918 0.5169 0.5966 0.0831  0.0688  0.2142  210 GLN C CD  
7862  O OE1 . GLN C 201 ? 0.5977 0.5205 0.5975 0.0813  0.0691  0.2156  210 GLN C OE1 
7863  N NE2 . GLN C 201 ? 0.5995 0.5196 0.6094 0.0917  0.0750  0.2201  210 GLN C NE2 
7864  N N   . SER C 202 ? 0.5561 0.4852 0.5277 0.0567  0.0343  0.1814  211 SER C N   
7865  C CA  . SER C 202 ? 0.5647 0.4868 0.5253 0.0551  0.0302  0.1721  211 SER C CA  
7866  C C   . SER C 202 ? 0.5629 0.4805 0.5209 0.0471  0.0222  0.1628  211 SER C C   
7867  O O   . SER C 202 ? 0.5604 0.4718 0.5175 0.0450  0.0239  0.1543  211 SER C O   
7868  C CB  . SER C 202 ? 0.5758 0.4993 0.5185 0.0604  0.0216  0.1734  211 SER C CB  
7869  O OG  . SER C 202 ? 0.5890 0.5176 0.5330 0.0679  0.0303  0.1801  211 SER C OG  
7870  N N   . CYS C 203 ? 0.5676 0.4905 0.5251 0.0421  0.0134  0.1658  212 CYS C N   
7871  C CA  . CYS C 203 ? 0.5683 0.4886 0.5247 0.0333  0.0058  0.1590  212 CYS C CA  
7872  C C   . CYS C 203 ? 0.5471 0.4685 0.5194 0.0310  0.0161  0.1548  212 CYS C C   
7873  O O   . CYS C 203 ? 0.5386 0.4521 0.5098 0.0279  0.0168  0.1455  212 CYS C O   
7874  C CB  . CYS C 203 ? 0.5790 0.5085 0.5322 0.0263  -0.0066 0.1655  212 CYS C CB  
7875  S SG  . CYS C 203 ? 0.6356 0.5592 0.5847 0.0149  -0.0167 0.1573  212 CYS C SG  
7876  N N   . SER C 204 ? 0.5366 0.4679 0.5222 0.0336  0.0234  0.1613  213 SER C N   
7877  C CA  . SER C 204 ? 0.5279 0.4581 0.5263 0.0340  0.0332  0.1571  213 SER C CA  
7878  C C   . SER C 204 ? 0.5204 0.4361 0.5198 0.0339  0.0408  0.1488  213 SER C C   
7879  O O   . SER C 204 ? 0.5196 0.4318 0.5231 0.0294  0.0425  0.1407  213 SER C O   
7880  C CB  . SER C 204 ? 0.5326 0.4696 0.5410 0.0424  0.0419  0.1651  213 SER C CB  
7881  O OG  . SER C 204 ? 0.5475 0.5043 0.5573 0.0423  0.0356  0.1732  213 SER C OG  
7882  N N   . ILE C 205 ? 0.5169 0.4270 0.5129 0.0382  0.0452  0.1517  214 ILE C N   
7883  C CA  . ILE C 205 ? 0.5104 0.4120 0.5072 0.0365  0.0513  0.1460  214 ILE C CA  
7884  C C   . ILE C 205 ? 0.5035 0.4041 0.4917 0.0317  0.0442  0.1362  214 ILE C C   
7885  O O   . ILE C 205 ? 0.4992 0.3962 0.4922 0.0273  0.0478  0.1288  214 ILE C O   
7886  C CB  . ILE C 205 ? 0.5184 0.4195 0.5128 0.0414  0.0565  0.1532  214 ILE C CB  
7887  C CG1 . ILE C 205 ? 0.5251 0.4224 0.5281 0.0457  0.0642  0.1620  214 ILE C CG1 
7888  C CG2 . ILE C 205 ? 0.5104 0.4091 0.5051 0.0382  0.0615  0.1493  214 ILE C CG2 
7889  C CD1 . ILE C 205 ? 0.5508 0.4518 0.5500 0.0514  0.0659  0.1724  214 ILE C CD1 
7890  N N   . SER C 206 ? 0.5012 0.4035 0.4753 0.0330  0.0333  0.1359  215 SER C N   
7891  C CA  . SER C 206 ? 0.4964 0.3941 0.4585 0.0306  0.0247  0.1266  215 SER C CA  
7892  C C   . SER C 206 ? 0.4807 0.3773 0.4503 0.0227  0.0236  0.1205  215 SER C C   
7893  O O   . SER C 206 ? 0.4765 0.3700 0.4452 0.0204  0.0245  0.1123  215 SER C O   
7894  C CB  . SER C 206 ? 0.5113 0.4052 0.4542 0.0325  0.0099  0.1272  215 SER C CB  
7895  O OG  . SER C 206 ? 0.5234 0.4085 0.4503 0.0334  0.0012  0.1178  215 SER C OG  
7896  N N   . ASN C 207 ? 0.4656 0.3679 0.4430 0.0194  0.0222  0.1252  216 ASN C N   
7897  C CA  . ASN C 207 ? 0.4505 0.3560 0.4360 0.0130  0.0220  0.1207  216 ASN C CA  
7898  C C   . ASN C 207 ? 0.4381 0.3407 0.4352 0.0132  0.0341  0.1153  216 ASN C C   
7899  O O   . ASN C 207 ? 0.4382 0.3378 0.4350 0.0090  0.0336  0.1070  216 ASN C O   
7900  C CB  . ASN C 207 ? 0.4525 0.3706 0.4445 0.0113  0.0193  0.1285  216 ASN C CB  
7901  C CG  . ASN C 207 ? 0.4736 0.3951 0.4537 0.0077  0.0051  0.1348  216 ASN C CG  
7902  O OD1 . ASN C 207 ? 0.4916 0.4015 0.4557 0.0072  -0.0040 0.1316  216 ASN C OD1 
7903  N ND2 . ASN C 207 ? 0.4892 0.4270 0.4754 0.0056  0.0023  0.1440  216 ASN C ND2 
7904  N N   . ILE C 208 ? 0.4304 0.3319 0.4364 0.0180  0.0441  0.1199  217 ILE C N   
7905  C CA  . ILE C 208 ? 0.4252 0.3193 0.4399 0.0171  0.0539  0.1150  217 ILE C CA  
7906  C C   . ILE C 208 ? 0.4241 0.3137 0.4354 0.0132  0.0551  0.1085  217 ILE C C   
7907  O O   . ILE C 208 ? 0.4151 0.3028 0.4300 0.0083  0.0568  0.1008  217 ILE C O   
7908  C CB  . ILE C 208 ? 0.4330 0.3205 0.4523 0.0229  0.0621  0.1219  217 ILE C CB  
7909  C CG1 . ILE C 208 ? 0.4361 0.3297 0.4597 0.0289  0.0624  0.1271  217 ILE C CG1 
7910  C CG2 . ILE C 208 ? 0.4421 0.3170 0.4668 0.0201  0.0698  0.1173  217 ILE C CG2 
7911  C CD1 . ILE C 208 ? 0.4545 0.3425 0.4790 0.0367  0.0678  0.1360  217 ILE C CD1 
7912  N N   . GLU C 209 ? 0.4362 0.3268 0.4402 0.0161  0.0542  0.1122  218 GLU C N   
7913  C CA  . GLU C 209 ? 0.4506 0.3431 0.4500 0.0144  0.0548  0.1073  218 GLU C CA  
7914  C C   . GLU C 209 ? 0.4379 0.3313 0.4317 0.0111  0.0475  0.0978  218 GLU C C   
7915  O O   . GLU C 209 ? 0.4364 0.3307 0.4340 0.0068  0.0507  0.0913  218 GLU C O   
7916  C CB  . GLU C 209 ? 0.4648 0.3626 0.4534 0.0211  0.0525  0.1125  218 GLU C CB  
7917  C CG  . GLU C 209 ? 0.5240 0.4232 0.5187 0.0229  0.0610  0.1222  218 GLU C CG  
7918  C CD  . GLU C 209 ? 0.6000 0.5076 0.5840 0.0309  0.0587  0.1285  218 GLU C CD  
7919  O OE1 . GLU C 209 ? 0.6179 0.5261 0.5884 0.0361  0.0493  0.1256  218 GLU C OE1 
7920  O OE2 . GLU C 209 ? 0.6333 0.5461 0.6212 0.0316  0.0656  0.1369  218 GLU C OE2 
7921  N N   . THR C 210 ? 0.4320 0.3248 0.4161 0.0122  0.0368  0.0976  219 THR C N   
7922  C CA  . THR C 210 ? 0.4205 0.3112 0.3971 0.0085  0.0280  0.0899  219 THR C CA  
7923  C C   . THR C 210 ? 0.4032 0.2958 0.3924 0.0017  0.0324  0.0849  219 THR C C   
7924  O O   . THR C 210 ? 0.4065 0.2993 0.3956 -0.0009 0.0334  0.0775  219 THR C O   
7925  C CB  . THR C 210 ? 0.4270 0.3141 0.3917 0.0078  0.0144  0.0925  219 THR C CB  
7926  O OG1 . THR C 210 ? 0.4420 0.3254 0.3923 0.0153  0.0096  0.0957  219 THR C OG1 
7927  C CG2 . THR C 210 ? 0.4255 0.3071 0.3810 0.0032  0.0044  0.0853  219 THR C CG2 
7928  N N   . VAL C 211 ? 0.3858 0.2815 0.3854 0.0001  0.0355  0.0888  220 VAL C N   
7929  C CA  . VAL C 211 ? 0.3662 0.2641 0.3766 -0.0041 0.0407  0.0835  220 VAL C CA  
7930  C C   . VAL C 211 ? 0.3619 0.2553 0.3774 -0.0059 0.0493  0.0775  220 VAL C C   
7931  O O   . VAL C 211 ? 0.3537 0.2486 0.3692 -0.0102 0.0482  0.0700  220 VAL C O   
7932  C CB  . VAL C 211 ? 0.3638 0.2663 0.3835 -0.0012 0.0450  0.0888  220 VAL C CB  
7933  C CG1 . VAL C 211 ? 0.3533 0.2541 0.3819 -0.0024 0.0523  0.0821  220 VAL C CG1 
7934  C CG2 . VAL C 211 ? 0.3561 0.2704 0.3734 -0.0031 0.0355  0.0942  220 VAL C CG2 
7935  N N   . ILE C 212 ? 0.3685 0.2567 0.3878 -0.0036 0.0570  0.0818  221 ILE C N   
7936  C CA  . ILE C 212 ? 0.3708 0.2551 0.3947 -0.0079 0.0638  0.0783  221 ILE C CA  
7937  C C   . ILE C 212 ? 0.3750 0.2668 0.3932 -0.0104 0.0607  0.0730  221 ILE C C   
7938  O O   . ILE C 212 ? 0.3722 0.2655 0.3939 -0.0158 0.0621  0.0659  221 ILE C O   
7939  C CB  . ILE C 212 ? 0.3755 0.2552 0.4006 -0.0065 0.0696  0.0865  221 ILE C CB  
7940  C CG1 . ILE C 212 ? 0.3722 0.2425 0.4009 -0.0020 0.0726  0.0924  221 ILE C CG1 
7941  C CG2 . ILE C 212 ? 0.3703 0.2474 0.3998 -0.0141 0.0748  0.0845  221 ILE C CG2 
7942  C CD1 . ILE C 212 ? 0.3764 0.2367 0.4105 -0.0036 0.0757  0.0868  221 ILE C CD1 
7943  N N   . GLU C 213 ? 0.3894 0.2860 0.3973 -0.0051 0.0560  0.0760  222 GLU C N   
7944  C CA  . GLU C 213 ? 0.4100 0.3143 0.4096 -0.0037 0.0531  0.0714  222 GLU C CA  
7945  C C   . GLU C 213 ? 0.4075 0.3110 0.4030 -0.0061 0.0462  0.0625  222 GLU C C   
7946  O O   . GLU C 213 ? 0.4094 0.3188 0.4000 -0.0057 0.0448  0.0569  222 GLU C O   
7947  C CB  . GLU C 213 ? 0.4205 0.3281 0.4067 0.0056  0.0485  0.0758  222 GLU C CB  
7948  C CG  . GLU C 213 ? 0.4689 0.3901 0.4491 0.0101  0.0509  0.0753  222 GLU C CG  
7949  C CD  . GLU C 213 ? 0.5481 0.4730 0.5117 0.0223  0.0456  0.0788  222 GLU C CD  
7950  O OE1 . GLU C 213 ? 0.5919 0.5064 0.5492 0.0255  0.0396  0.0814  222 GLU C OE1 
7951  O OE2 . GLU C 213 ? 0.5781 0.5181 0.5343 0.0295  0.0472  0.0792  222 GLU C OE2 
7952  N N   . PHE C 214 ? 0.4085 0.3069 0.4062 -0.0086 0.0418  0.0622  223 PHE C N   
7953  C CA  . PHE C 214 ? 0.4044 0.3030 0.3995 -0.0126 0.0351  0.0558  223 PHE C CA  
7954  C C   . PHE C 214 ? 0.4023 0.3047 0.4095 -0.0187 0.0424  0.0498  223 PHE C C   
7955  O O   . PHE C 214 ? 0.4026 0.3084 0.4077 -0.0213 0.0399  0.0432  223 PHE C O   
7956  C CB  . PHE C 214 ? 0.4006 0.2977 0.3955 -0.0146 0.0281  0.0599  223 PHE C CB  
7957  C CG  . PHE C 214 ? 0.3891 0.2892 0.3847 -0.0207 0.0222  0.0556  223 PHE C CG  
7958  C CD1 . PHE C 214 ? 0.3962 0.2911 0.3776 -0.0219 0.0096  0.0541  223 PHE C CD1 
7959  C CD2 . PHE C 214 ? 0.3769 0.2841 0.3857 -0.0246 0.0282  0.0535  223 PHE C CD2 
7960  C CE1 . PHE C 214 ? 0.3830 0.2811 0.3649 -0.0288 0.0032  0.0519  223 PHE C CE1 
7961  C CE2 . PHE C 214 ? 0.3692 0.2826 0.3789 -0.0302 0.0227  0.0508  223 PHE C CE2 
7962  C CZ  . PHE C 214 ? 0.3658 0.2753 0.3629 -0.0331 0.0102  0.0507  223 PHE C CZ  
7963  N N   . GLN C 215 ? 0.4047 0.3048 0.4231 -0.0204 0.0507  0.0520  224 GLN C N   
7964  C CA  . GLN C 215 ? 0.4093 0.3092 0.4366 -0.0260 0.0566  0.0458  224 GLN C CA  
7965  C C   . GLN C 215 ? 0.4083 0.3117 0.4359 -0.0293 0.0606  0.0438  224 GLN C C   
7966  O O   . GLN C 215 ? 0.4062 0.3133 0.4373 -0.0347 0.0622  0.0373  224 GLN C O   
7967  C CB  . GLN C 215 ? 0.4203 0.3120 0.4551 -0.0251 0.0626  0.0484  224 GLN C CB  
7968  C CG  . GLN C 215 ? 0.4543 0.3480 0.4885 -0.0197 0.0592  0.0536  224 GLN C CG  
7969  C CD  . GLN C 215 ? 0.5043 0.3909 0.5438 -0.0154 0.0649  0.0557  224 GLN C CD  
7970  O OE1 . GLN C 215 ? 0.5315 0.4056 0.5722 -0.0150 0.0705  0.0575  224 GLN C OE1 
7971  N NE2 . GLN C 215 ? 0.5047 0.3998 0.5465 -0.0115 0.0629  0.0563  224 GLN C NE2 
7972  N N   . GLN C 216 ? 0.4124 0.3177 0.4362 -0.0261 0.0621  0.0502  225 GLN C N   
7973  C CA  . GLN C 216 ? 0.4161 0.3301 0.4411 -0.0295 0.0664  0.0512  225 GLN C CA  
7974  C C   . GLN C 216 ? 0.4091 0.3358 0.4273 -0.0275 0.0623  0.0454  225 GLN C C   
7975  O O   . GLN C 216 ? 0.4000 0.3349 0.4225 -0.0335 0.0648  0.0410  225 GLN C O   
7976  C CB  . GLN C 216 ? 0.4260 0.3435 0.4476 -0.0248 0.0683  0.0608  225 GLN C CB  
7977  C CG  . GLN C 216 ? 0.4528 0.3576 0.4804 -0.0265 0.0727  0.0679  225 GLN C CG  
7978  C CD  . GLN C 216 ? 0.4871 0.3985 0.5159 -0.0284 0.0772  0.0777  225 GLN C CD  
7979  O OE1 . GLN C 216 ? 0.4987 0.4232 0.5206 -0.0216 0.0759  0.0823  225 GLN C OE1 
7980  N NE2 . GLN C 216 ? 0.5012 0.4032 0.5374 -0.0377 0.0817  0.0812  225 GLN C NE2 
7981  N N   . LYS C 217 ? 0.4133 0.3399 0.4190 -0.0186 0.0550  0.0453  226 LYS C N   
7982  C CA  . LYS C 217 ? 0.4186 0.3538 0.4130 -0.0131 0.0497  0.0401  226 LYS C CA  
7983  C C   . LYS C 217 ? 0.4064 0.3379 0.4011 -0.0172 0.0450  0.0321  226 LYS C C   
7984  O O   . LYS C 217 ? 0.4083 0.3478 0.3976 -0.0152 0.0427  0.0269  226 LYS C O   
7985  C CB  . LYS C 217 ? 0.4339 0.3641 0.4107 -0.0013 0.0413  0.0420  226 LYS C CB  
7986  C CG  . LYS C 217 ? 0.4672 0.4065 0.4399 0.0060  0.0450  0.0492  226 LYS C CG  
7987  C CD  . LYS C 217 ? 0.5207 0.4559 0.4709 0.0203  0.0350  0.0477  226 LYS C CD  
7988  C CE  . LYS C 217 ? 0.5620 0.5081 0.5067 0.0295  0.0385  0.0552  226 LYS C CE  
7989  N NZ  . LYS C 217 ? 0.5974 0.5304 0.5192 0.0425  0.0269  0.0537  226 LYS C NZ  
7990  N N   . ASN C 218 ? 0.3956 0.3172 0.3960 -0.0220 0.0432  0.0318  227 ASN C N   
7991  C CA  . ASN C 218 ? 0.3854 0.3066 0.3868 -0.0264 0.0388  0.0256  227 ASN C CA  
7992  C C   . ASN C 218 ? 0.3824 0.3082 0.3981 -0.0347 0.0466  0.0213  227 ASN C C   
7993  O O   . ASN C 218 ? 0.3787 0.3053 0.3979 -0.0387 0.0446  0.0168  227 ASN C O   
7994  C CB  . ASN C 218 ? 0.3800 0.2928 0.3777 -0.0267 0.0307  0.0286  227 ASN C CB  
7995  C CG  . ASN C 218 ? 0.3850 0.2905 0.3643 -0.0218 0.0180  0.0285  227 ASN C CG  
7996  O OD1 . ASN C 218 ? 0.3927 0.2991 0.3636 -0.0198 0.0138  0.0230  227 ASN C OD1 
7997  N ND2 . ASN C 218 ? 0.3823 0.2791 0.3536 -0.0194 0.0109  0.0346  227 ASN C ND2 
7998  N N   . ASN C 219 ? 0.3859 0.3147 0.4084 -0.0376 0.0547  0.0230  228 ASN C N   
7999  C CA  . ASN C 219 ? 0.3805 0.3075 0.4142 -0.0459 0.0611  0.0197  228 ASN C CA  
8000  C C   . ASN C 219 ? 0.3654 0.2995 0.4014 -0.0506 0.0600  0.0112  228 ASN C C   
8001  O O   . ASN C 219 ? 0.3614 0.2917 0.4023 -0.0534 0.0603  0.0067  228 ASN C O   
8002  C CB  . ASN C 219 ? 0.3917 0.3218 0.4293 -0.0505 0.0672  0.0240  228 ASN C CB  
8003  C CG  . ASN C 219 ? 0.4156 0.3400 0.4614 -0.0603 0.0714  0.0202  228 ASN C CG  
8004  O OD1 . ASN C 219 ? 0.4379 0.3729 0.4859 -0.0669 0.0724  0.0166  228 ASN C OD1 
8005  N ND2 . ASN C 219 ? 0.4437 0.3507 0.4923 -0.0607 0.0733  0.0205  228 ASN C ND2 
8006  N N   . ARG C 220 ? 0.3509 0.2978 0.3827 -0.0501 0.0587  0.0093  229 ARG C N   
8007  C CA  . ARG C 220 ? 0.3310 0.2867 0.3648 -0.0545 0.0579  0.0017  229 ARG C CA  
8008  C C   . ARG C 220 ? 0.3194 0.2706 0.3511 -0.0530 0.0520  -0.0019 229 ARG C C   
8009  O O   . ARG C 220 ? 0.3173 0.2695 0.3555 -0.0582 0.0536  -0.0070 229 ARG C O   
8010  C CB  . ARG C 220 ? 0.3305 0.3018 0.3573 -0.0505 0.0562  0.0011  229 ARG C CB  
8011  C CG  . ARG C 220 ? 0.3124 0.2977 0.3455 -0.0582 0.0595  -0.0038 229 ARG C CG  
8012  C CD  . ARG C 220 ? 0.3050 0.3089 0.3302 -0.0516 0.0578  -0.0036 229 ARG C CD  
8013  N NE  . ARG C 220 ? 0.3090 0.3233 0.3353 -0.0545 0.0564  -0.0106 229 ARG C NE  
8014  C CZ  . ARG C 220 ? 0.3147 0.3434 0.3318 -0.0464 0.0530  -0.0127 229 ARG C CZ  
8015  N NH1 . ARG C 220 ? 0.3153 0.3487 0.3195 -0.0333 0.0501  -0.0092 229 ARG C NH1 
8016  N NH2 . ARG C 220 ? 0.3227 0.3611 0.3420 -0.0499 0.0521  -0.0188 229 ARG C NH2 
8017  N N   . LEU C 221 ? 0.3140 0.2602 0.3357 -0.0466 0.0445  0.0014  230 LEU C N   
8018  C CA  . LEU C 221 ? 0.3049 0.2485 0.3244 -0.0475 0.0374  0.0006  230 LEU C CA  
8019  C C   . LEU C 221 ? 0.3006 0.2430 0.3304 -0.0509 0.0413  0.0014  230 LEU C C   
8020  O O   . LEU C 221 ? 0.2970 0.2455 0.3309 -0.0542 0.0401  -0.0018 230 LEU C O   
8021  C CB  . LEU C 221 ? 0.3124 0.2470 0.3188 -0.0421 0.0275  0.0060  230 LEU C CB  
8022  C CG  . LEU C 221 ? 0.3024 0.2354 0.3055 -0.0457 0.0180  0.0079  230 LEU C CG  
8023  C CD1 . LEU C 221 ? 0.3114 0.2449 0.3048 -0.0457 0.0106  0.0035  230 LEU C CD1 
8024  C CD2 . LEU C 221 ? 0.3243 0.2465 0.3173 -0.0431 0.0093  0.0153  230 LEU C CD2 
8025  N N   . LEU C 222 ? 0.3044 0.2399 0.3378 -0.0490 0.0461  0.0057  231 LEU C N   
8026  C CA  . LEU C 222 ? 0.3067 0.2409 0.3475 -0.0490 0.0494  0.0064  231 LEU C CA  
8027  C C   . LEU C 222 ? 0.3051 0.2411 0.3527 -0.0529 0.0551  -0.0016 231 LEU C C   
8028  O O   . LEU C 222 ? 0.3078 0.2498 0.3588 -0.0528 0.0550  -0.0047 231 LEU C O   
8029  C CB  . LEU C 222 ? 0.3166 0.2414 0.3581 -0.0447 0.0529  0.0129  231 LEU C CB  
8030  C CG  . LEU C 222 ? 0.3196 0.2433 0.3534 -0.0409 0.0459  0.0208  231 LEU C CG  
8031  C CD1 . LEU C 222 ? 0.3544 0.2698 0.3873 -0.0369 0.0497  0.0266  231 LEU C CD1 
8032  C CD2 . LEU C 222 ? 0.3270 0.2568 0.3617 -0.0403 0.0409  0.0252  231 LEU C CD2 
8033  N N   . GLU C 223 ? 0.3059 0.2385 0.3547 -0.0569 0.0596  -0.0046 232 GLU C N   
8034  C CA  . GLU C 223 ? 0.3099 0.2416 0.3634 -0.0621 0.0635  -0.0124 232 GLU C CA  
8035  C C   . GLU C 223 ? 0.2926 0.2371 0.3469 -0.0640 0.0605  -0.0186 232 GLU C C   
8036  O O   . GLU C 223 ? 0.3003 0.2456 0.3575 -0.0641 0.0621  -0.0242 232 GLU C O   
8037  C CB  . GLU C 223 ? 0.3185 0.2485 0.3729 -0.0690 0.0669  -0.0128 232 GLU C CB  
8038  C CG  . GLU C 223 ? 0.3618 0.2764 0.4167 -0.0695 0.0705  -0.0070 232 GLU C CG  
8039  C CD  . GLU C 223 ? 0.4184 0.3141 0.4736 -0.0689 0.0728  -0.0108 232 GLU C CD  
8040  O OE1 . GLU C 223 ? 0.4160 0.3119 0.4715 -0.0679 0.0724  -0.0191 232 GLU C OE1 
8041  O OE2 . GLU C 223 ? 0.4431 0.3231 0.4969 -0.0682 0.0748  -0.0054 232 GLU C OE2 
8042  N N   . ILE C 224 ? 0.2769 0.2309 0.3270 -0.0643 0.0556  -0.0176 233 ILE C N   
8043  C CA  . ILE C 224 ? 0.2646 0.2304 0.3144 -0.0661 0.0515  -0.0221 233 ILE C CA  
8044  C C   . ILE C 224 ? 0.2598 0.2302 0.3113 -0.0637 0.0484  -0.0198 233 ILE C C   
8045  O O   . ILE C 224 ? 0.2544 0.2328 0.3102 -0.0649 0.0500  -0.0248 233 ILE C O   
8046  C CB  . ILE C 224 ? 0.2581 0.2284 0.2993 -0.0644 0.0449  -0.0200 233 ILE C CB  
8047  C CG1 . ILE C 224 ? 0.2521 0.2238 0.2912 -0.0641 0.0482  -0.0202 233 ILE C CG1 
8048  C CG2 . ILE C 224 ? 0.2530 0.2341 0.2933 -0.0669 0.0407  -0.0246 233 ILE C CG2 
8049  C CD1 . ILE C 224 ? 0.2553 0.2357 0.2863 -0.0612 0.0435  -0.0219 233 ILE C CD1 
8050  N N   . THR C 225 ? 0.2596 0.2270 0.3071 -0.0605 0.0435  -0.0116 234 THR C N   
8051  C CA  . THR C 225 ? 0.2593 0.2352 0.3085 -0.0592 0.0397  -0.0063 234 THR C CA  
8052  C C   . THR C 225 ? 0.2674 0.2487 0.3239 -0.0561 0.0465  -0.0102 234 THR C C   
8053  O O   . THR C 225 ? 0.2668 0.2637 0.3261 -0.0559 0.0449  -0.0099 234 THR C O   
8054  C CB  . THR C 225 ? 0.2636 0.2327 0.3089 -0.0561 0.0362  0.0031  234 THR C CB  
8055  O OG1 . THR C 225 ? 0.2651 0.2297 0.3004 -0.0582 0.0266  0.0068  234 THR C OG1 
8056  C CG2 . THR C 225 ? 0.2642 0.2448 0.3133 -0.0544 0.0345  0.0097  234 THR C CG2 
8057  N N   . ARG C 226 ? 0.2819 0.2497 0.3398 -0.0530 0.0536  -0.0135 235 ARG C N   
8058  C CA  . ARG C 226 ? 0.2962 0.2630 0.3567 -0.0479 0.0591  -0.0189 235 ARG C CA  
8059  C C   . ARG C 226 ? 0.2926 0.2668 0.3546 -0.0512 0.0601  -0.0286 235 ARG C C   
8060  O O   . ARG C 226 ? 0.2922 0.2824 0.3559 -0.0479 0.0594  -0.0300 235 ARG C O   
8061  C CB  . ARG C 226 ? 0.3145 0.2592 0.3733 -0.0457 0.0645  -0.0208 235 ARG C CB  
8062  C CG  . ARG C 226 ? 0.3492 0.2850 0.4063 -0.0396 0.0687  -0.0288 235 ARG C CG  
8063  C CD  . ARG C 226 ? 0.3963 0.3055 0.4497 -0.0419 0.0718  -0.0313 235 ARG C CD  
8064  N NE  . ARG C 226 ? 0.3973 0.2997 0.4510 -0.0426 0.0718  -0.0215 235 ARG C NE  
8065  C CZ  . ARG C 226 ? 0.3756 0.2723 0.4278 -0.0339 0.0728  -0.0150 235 ARG C CZ  
8066  N NH1 . ARG C 226 ? 0.3624 0.2601 0.4123 -0.0228 0.0742  -0.0172 235 ARG C NH1 
8067  N NH2 . ARG C 226 ? 0.3606 0.2525 0.4130 -0.0351 0.0726  -0.0063 235 ARG C NH2 
8068  N N   . GLU C 227 ? 0.2950 0.2599 0.3563 -0.0578 0.0618  -0.0345 236 GLU C N   
8069  C CA  . GLU C 227 ? 0.2954 0.2666 0.3577 -0.0628 0.0624  -0.0438 236 GLU C CA  
8070  C C   . GLU C 227 ? 0.2736 0.2675 0.3377 -0.0622 0.0584  -0.0433 236 GLU C C   
8071  O O   . GLU C 227 ? 0.2744 0.2772 0.3395 -0.0602 0.0598  -0.0499 236 GLU C O   
8072  C CB  . GLU C 227 ? 0.2989 0.2671 0.3608 -0.0712 0.0621  -0.0445 236 GLU C CB  
8073  C CG  . GLU C 227 ? 0.3392 0.3038 0.4016 -0.0786 0.0647  -0.0535 236 GLU C CG  
8074  C CD  . GLU C 227 ? 0.3705 0.3400 0.4334 -0.0864 0.0644  -0.0514 236 GLU C CD  
8075  O OE1 . GLU C 227 ? 0.4008 0.3823 0.4650 -0.0924 0.0639  -0.0566 236 GLU C OE1 
8076  O OE2 . GLU C 227 ? 0.3457 0.3097 0.4074 -0.0856 0.0649  -0.0441 236 GLU C OE2 
8077  N N   . PHE C 228 ? 0.2546 0.2569 0.3178 -0.0637 0.0526  -0.0350 237 PHE C N   
8078  C CA  . PHE C 228 ? 0.2413 0.2637 0.3055 -0.0654 0.0473  -0.0326 237 PHE C CA  
8079  C C   . PHE C 228 ? 0.2391 0.2767 0.3064 -0.0597 0.0476  -0.0284 237 PHE C C   
8080  O O   . PHE C 228 ? 0.2350 0.2913 0.3047 -0.0596 0.0470  -0.0305 237 PHE C O   
8081  C CB  . PHE C 228 ? 0.2386 0.2610 0.2979 -0.0694 0.0387  -0.0243 237 PHE C CB  
8082  C CG  . PHE C 228 ? 0.2481 0.2680 0.3035 -0.0735 0.0365  -0.0289 237 PHE C CG  
8083  C CD1 . PHE C 228 ? 0.2633 0.2708 0.3115 -0.0729 0.0332  -0.0261 237 PHE C CD1 
8084  C CD2 . PHE C 228 ? 0.2600 0.2917 0.3180 -0.0765 0.0377  -0.0360 237 PHE C CD2 
8085  C CE1 . PHE C 228 ? 0.2723 0.2806 0.3157 -0.0741 0.0313  -0.0301 237 PHE C CE1 
8086  C CE2 . PHE C 228 ? 0.2616 0.2936 0.3159 -0.0792 0.0358  -0.0397 237 PHE C CE2 
8087  C CZ  . PHE C 228 ? 0.2674 0.2883 0.3141 -0.0775 0.0327  -0.0367 237 PHE C CZ  
8088  N N   . SER C 229 ? 0.2415 0.2742 0.3087 -0.0542 0.0485  -0.0217 238 SER C N   
8089  C CA  . SER C 229 ? 0.2420 0.2911 0.3118 -0.0460 0.0501  -0.0174 238 SER C CA  
8090  C C   . SER C 229 ? 0.2511 0.3021 0.3206 -0.0373 0.0570  -0.0284 238 SER C C   
8091  O O   . SER C 229 ? 0.2562 0.3299 0.3273 -0.0298 0.0578  -0.0271 238 SER C O   
8092  C CB  . SER C 229 ? 0.2501 0.2884 0.3188 -0.0406 0.0513  -0.0102 238 SER C CB  
8093  O OG  . SER C 229 ? 0.2572 0.2982 0.3246 -0.0470 0.0434  0.0012  238 SER C OG  
8094  N N   . VAL C 230 ? 0.2594 0.2870 0.3257 -0.0380 0.0611  -0.0390 239 VAL C N   
8095  C CA  . VAL C 230 ? 0.2742 0.2964 0.3365 -0.0298 0.0657  -0.0503 239 VAL C CA  
8096  C C   . VAL C 230 ? 0.2733 0.3096 0.3364 -0.0340 0.0649  -0.0584 239 VAL C C   
8097  O O   . VAL C 230 ? 0.2920 0.3310 0.3509 -0.0258 0.0674  -0.0676 239 VAL C O   
8098  C CB  . VAL C 230 ? 0.2854 0.2741 0.3424 -0.0313 0.0687  -0.0574 239 VAL C CB  
8099  C CG1 . VAL C 230 ? 0.3166 0.2919 0.3649 -0.0197 0.0717  -0.0681 239 VAL C CG1 
8100  C CG2 . VAL C 230 ? 0.2941 0.2698 0.3515 -0.0307 0.0688  -0.0481 239 VAL C CG2 
8101  N N   . ASN C 231 ? 0.2581 0.3024 0.3250 -0.0454 0.0610  -0.0555 240 ASN C N   
8102  C CA  . ASN C 231 ? 0.2523 0.3084 0.3200 -0.0501 0.0603  -0.0633 240 ASN C CA  
8103  C C   . ASN C 231 ? 0.2311 0.3148 0.3030 -0.0543 0.0551  -0.0555 240 ASN C C   
8104  O O   . ASN C 231 ? 0.2225 0.3153 0.2954 -0.0606 0.0532  -0.0593 240 ASN C O   
8105  C CB  . ASN C 231 ? 0.2579 0.2965 0.3246 -0.0599 0.0605  -0.0688 240 ASN C CB  
8106  C CG  . ASN C 231 ? 0.2930 0.3059 0.3549 -0.0586 0.0644  -0.0772 240 ASN C CG  
8107  O OD1 . ASN C 231 ? 0.3258 0.3353 0.3836 -0.0562 0.0658  -0.0876 240 ASN C OD1 
8108  N ND2 . ASN C 231 ? 0.3292 0.3225 0.3902 -0.0605 0.0653  -0.0725 240 ASN C ND2 
8109  N N   . ALA C 232 ? 0.2234 0.3205 0.2974 -0.0518 0.0520  -0.0434 241 ALA C N   
8110  C CA  . ALA C 232 ? 0.2150 0.3367 0.2919 -0.0579 0.0452  -0.0339 241 ALA C CA  
8111  C C   . ALA C 232 ? 0.2117 0.3239 0.2864 -0.0688 0.0396  -0.0337 241 ALA C C   
8112  O O   . ALA C 232 ? 0.2088 0.3361 0.2842 -0.0738 0.0360  -0.0340 241 ALA C O   
8113  C CB  . ALA C 232 ? 0.2184 0.3660 0.2975 -0.0535 0.0472  -0.0381 241 ALA C CB  
8114  N N   . GLY C 233 ? 0.2159 0.3039 0.2870 -0.0710 0.0390  -0.0334 242 GLY C N   
8115  C CA  . GLY C 233 ? 0.2117 0.2907 0.2781 -0.0779 0.0330  -0.0319 242 GLY C CA  
8116  C C   . GLY C 233 ? 0.2081 0.2863 0.2740 -0.0810 0.0352  -0.0420 242 GLY C C   
8117  O O   . GLY C 233 ? 0.2115 0.2905 0.2729 -0.0850 0.0290  -0.0398 242 GLY C O   
8118  N N   . VAL C 234 ? 0.2081 0.2841 0.2770 -0.0791 0.0430  -0.0528 243 VAL C N   
8119  C CA  . VAL C 234 ? 0.2081 0.2838 0.2766 -0.0835 0.0449  -0.0617 243 VAL C CA  
8120  C C   . VAL C 234 ? 0.2236 0.2866 0.2930 -0.0832 0.0517  -0.0708 243 VAL C C   
8121  O O   . VAL C 234 ? 0.2388 0.3019 0.3088 -0.0785 0.0549  -0.0753 243 VAL C O   
8122  C CB  . VAL C 234 ? 0.1987 0.2950 0.2695 -0.0850 0.0441  -0.0663 243 VAL C CB  
8123  C CG1 . VAL C 234 ? 0.1936 0.2934 0.2625 -0.0901 0.0418  -0.0690 243 VAL C CG1 
8124  C CG2 . VAL C 234 ? 0.2007 0.3146 0.2724 -0.0841 0.0386  -0.0568 243 VAL C CG2 
8125  N N   . THR C 235 ? 0.2293 0.2825 0.2978 -0.0881 0.0533  -0.0736 244 THR C N   
8126  C CA  . THR C 235 ? 0.2521 0.2906 0.3204 -0.0906 0.0581  -0.0807 244 THR C CA  
8127  C C   . THR C 235 ? 0.2529 0.2971 0.3219 -0.0990 0.0588  -0.0873 244 THR C C   
8128  O O   . THR C 235 ? 0.2428 0.2996 0.3122 -0.1015 0.0566  -0.0845 244 THR C O   
8129  C CB  . THR C 235 ? 0.2658 0.2868 0.3330 -0.0911 0.0596  -0.0751 244 THR C CB  
8130  O OG1 . THR C 235 ? 0.2643 0.2889 0.3301 -0.0878 0.0560  -0.0657 244 THR C OG1 
8131  C CG2 . THR C 235 ? 0.2974 0.2983 0.3625 -0.0863 0.0626  -0.0765 244 THR C CG2 
8132  N N   . THR C 236 ? 0.2686 0.3024 0.3361 -0.1030 0.0610  -0.0958 245 THR C N   
8133  C CA  . THR C 236 ? 0.2784 0.3126 0.3463 -0.1141 0.0612  -0.1001 245 THR C CA  
8134  C C   . THR C 236 ? 0.2966 0.3065 0.3617 -0.1191 0.0623  -0.0996 245 THR C C   
8135  O O   . THR C 236 ? 0.3105 0.3004 0.3714 -0.1130 0.0630  -0.1010 245 THR C O   
8136  C CB  . THR C 236 ? 0.2857 0.3314 0.3530 -0.1178 0.0602  -0.1100 245 THR C CB  
8137  O OG1 . THR C 236 ? 0.2939 0.3642 0.3645 -0.1155 0.0587  -0.1072 245 THR C OG1 
8138  C CG2 . THR C 236 ? 0.3013 0.3455 0.3682 -0.1313 0.0596  -0.1142 245 THR C CG2 
8139  N N   . PRO C 237 ? 0.3024 0.3153 0.3690 -0.1310 0.0620  -0.0980 246 PRO C N   
8140  C CA  . PRO C 237 ? 0.2935 0.3075 0.3624 -0.1373 0.0628  -0.0890 246 PRO C CA  
8141  C C   . PRO C 237 ? 0.2693 0.2912 0.3396 -0.1271 0.0637  -0.0807 246 PRO C C   
8142  O O   . PRO C 237 ? 0.2708 0.2833 0.3395 -0.1173 0.0637  -0.0795 246 PRO C O   
8143  C CB  . PRO C 237 ? 0.3196 0.3035 0.3842 -0.1415 0.0625  -0.0885 246 PRO C CB  
8144  C CG  . PRO C 237 ? 0.3531 0.3226 0.4116 -0.1441 0.0601  -0.1002 246 PRO C CG  
8145  C CD  . PRO C 237 ? 0.3395 0.3329 0.4004 -0.1382 0.0602  -0.1068 246 PRO C CD  
8146  N N   . VAL C 238 ? 0.2499 0.2904 0.3221 -0.1288 0.0637  -0.0748 247 VAL C N   
8147  C CA  . VAL C 238 ? 0.2349 0.2784 0.3052 -0.1192 0.0634  -0.0669 247 VAL C CA  
8148  C C   . VAL C 238 ? 0.2459 0.2772 0.3165 -0.1225 0.0655  -0.0597 247 VAL C C   
8149  O O   . VAL C 238 ? 0.2487 0.2904 0.3213 -0.1307 0.0666  -0.0556 247 VAL C O   
8150  C CB  . VAL C 238 ? 0.2204 0.2884 0.2895 -0.1165 0.0620  -0.0649 247 VAL C CB  
8151  C CG1 . VAL C 238 ? 0.2234 0.2914 0.2868 -0.1055 0.0604  -0.0573 247 VAL C CG1 
8152  C CG2 . VAL C 238 ? 0.2085 0.2860 0.2770 -0.1139 0.0594  -0.0714 247 VAL C CG2 
8153  N N   . SER C 239 ? 0.2538 0.2647 0.3225 -0.1165 0.0660  -0.0574 248 SER C N   
8154  C CA  . SER C 239 ? 0.2682 0.2645 0.3368 -0.1196 0.0678  -0.0506 248 SER C CA  
8155  C C   . SER C 239 ? 0.2646 0.2771 0.3331 -0.1187 0.0687  -0.0412 248 SER C C   
8156  O O   . SER C 239 ? 0.2488 0.2786 0.3149 -0.1111 0.0674  -0.0398 248 SER C O   
8157  C CB  . SER C 239 ? 0.2719 0.2480 0.3380 -0.1102 0.0680  -0.0490 248 SER C CB  
8158  O OG  . SER C 239 ? 0.2619 0.2454 0.3258 -0.1002 0.0666  -0.0434 248 SER C OG  
8159  N N   . THR C 240 ? 0.2800 0.2860 0.3499 -0.1256 0.0704  -0.0343 249 THR C N   
8160  C CA  . THR C 240 ? 0.2798 0.3028 0.3493 -0.1230 0.0717  -0.0245 249 THR C CA  
8161  C C   . THR C 240 ? 0.2735 0.2903 0.3376 -0.1077 0.0709  -0.0216 249 THR C C   
8162  O O   . THR C 240 ? 0.2751 0.3054 0.3357 -0.1009 0.0711  -0.0150 249 THR C O   
8163  C CB  . THR C 240 ? 0.2963 0.3144 0.3688 -0.1353 0.0732  -0.0158 249 THR C CB  
8164  O OG1 . THR C 240 ? 0.3192 0.3112 0.3895 -0.1311 0.0738  -0.0123 249 THR C OG1 
8165  C CG2 . THR C 240 ? 0.3143 0.3237 0.3891 -0.1512 0.0715  -0.0204 249 THR C CG2 
8166  N N   . TYR C 241 ? 0.2714 0.2692 0.3337 -0.1017 0.0694  -0.0259 250 TYR C N   
8167  C CA  . TYR C 241 ? 0.2648 0.2575 0.3215 -0.0894 0.0672  -0.0221 250 TYR C CA  
8168  C C   . TYR C 241 ? 0.2530 0.2566 0.3043 -0.0821 0.0625  -0.0260 250 TYR C C   
8169  O O   . TYR C 241 ? 0.2479 0.2522 0.2910 -0.0724 0.0588  -0.0224 250 TYR C O   
8170  C CB  . TYR C 241 ? 0.2722 0.2436 0.3293 -0.0863 0.0670  -0.0227 250 TYR C CB  
8171  C CG  . TYR C 241 ? 0.3050 0.2592 0.3648 -0.0914 0.0704  -0.0196 250 TYR C CG  
8172  C CD1 . TYR C 241 ? 0.3461 0.2840 0.4071 -0.0937 0.0711  -0.0256 250 TYR C CD1 
8173  C CD2 . TYR C 241 ? 0.3511 0.3041 0.4105 -0.0926 0.0723  -0.0107 250 TYR C CD2 
8174  C CE1 . TYR C 241 ? 0.3889 0.3054 0.4491 -0.0969 0.0728  -0.0234 250 TYR C CE1 
8175  C CE2 . TYR C 241 ? 0.3982 0.3319 0.4589 -0.0978 0.0744  -0.0070 250 TYR C CE2 
8176  C CZ  . TYR C 241 ? 0.4100 0.3233 0.4703 -0.0997 0.0742  -0.0138 250 TYR C CZ  
8177  O OH  . TYR C 241 ? 0.4411 0.3300 0.4992 -0.1032 0.0748  -0.0110 250 TYR C OH  
8178  N N   . MET C 242 ? 0.2493 0.2591 0.3034 -0.0865 0.0618  -0.0333 251 MET C N   
8179  C CA  . MET C 242 ? 0.2440 0.2639 0.2924 -0.0806 0.0568  -0.0362 251 MET C CA  
8180  C C   . MET C 242 ? 0.2484 0.2877 0.2923 -0.0773 0.0567  -0.0342 251 MET C C   
8181  O O   . MET C 242 ? 0.2508 0.2922 0.2840 -0.0666 0.0517  -0.0326 251 MET C O   
8182  C CB  . MET C 242 ? 0.2402 0.2649 0.2932 -0.0861 0.0565  -0.0440 251 MET C CB  
8183  C CG  . MET C 242 ? 0.2442 0.2559 0.3009 -0.0873 0.0569  -0.0466 251 MET C CG  
8184  S SD  . MET C 242 ? 0.2373 0.2446 0.2881 -0.0792 0.0499  -0.0425 251 MET C SD  
8185  C CE  . MET C 242 ? 0.2293 0.2357 0.2864 -0.0811 0.0516  -0.0468 251 MET C CE  
8186  N N   . LEU C 243 ? 0.2555 0.3090 0.3062 -0.0861 0.0615  -0.0337 252 LEU C N   
8187  C CA  . LEU C 243 ? 0.2583 0.3377 0.3061 -0.0831 0.0624  -0.0304 252 LEU C CA  
8188  C C   . LEU C 243 ? 0.2688 0.3577 0.3225 -0.0910 0.0672  -0.0229 252 LEU C C   
8189  O O   . LEU C 243 ? 0.2794 0.3635 0.3417 -0.1056 0.0696  -0.0235 252 LEU C O   
8190  C CB  . LEU C 243 ? 0.2545 0.3536 0.3066 -0.0897 0.0627  -0.0358 252 LEU C CB  
8191  C CG  . LEU C 243 ? 0.2500 0.3608 0.2926 -0.0778 0.0582  -0.0389 252 LEU C CG  
8192  C CD1 . LEU C 243 ? 0.2473 0.3875 0.2942 -0.0831 0.0605  -0.0400 252 LEU C CD1 
8193  C CD2 . LEU C 243 ? 0.2695 0.3808 0.2994 -0.0622 0.0555  -0.0337 252 LEU C CD2 
8194  N N   . THR C 244 ? 0.2719 0.3750 0.3196 -0.0816 0.0677  -0.0157 253 THR C N   
8195  C CA  . THR C 244 ? 0.2808 0.4008 0.3340 -0.0889 0.0720  -0.0061 253 THR C CA  
8196  C C   . THR C 244 ? 0.2818 0.4344 0.3400 -0.0964 0.0736  -0.0049 253 THR C C   
8197  O O   . THR C 244 ? 0.2842 0.4484 0.3382 -0.0897 0.0715  -0.0109 253 THR C O   
8198  C CB  . THR C 244 ? 0.2831 0.4142 0.3268 -0.0736 0.0718  0.0006  253 THR C CB  
8199  O OG1 . THR C 244 ? 0.2958 0.3969 0.3333 -0.0657 0.0691  -0.0008 253 THR C OG1 
8200  C CG2 . THR C 244 ? 0.2966 0.4500 0.3465 -0.0811 0.0764  0.0127  253 THR C CG2 
8201  N N   . ASN C 245 ? 0.2920 0.4601 0.3587 -0.1111 0.0767  0.0038  254 ASN C N   
8202  C CA  . ASN C 245 ? 0.2949 0.5008 0.3670 -0.1200 0.0779  0.0078  254 ASN C CA  
8203  C C   . ASN C 245 ? 0.2860 0.5263 0.3494 -0.1005 0.0785  0.0110  254 ASN C C   
8204  O O   . ASN C 245 ? 0.2737 0.5351 0.3352 -0.0959 0.0776  0.0068  254 ASN C O   
8205  C CB  . ASN C 245 ? 0.3127 0.5279 0.3940 -0.1399 0.0797  0.0197  254 ASN C CB  
8206  C CG  . ASN C 245 ? 0.3196 0.5777 0.4078 -0.1527 0.0803  0.0266  254 ASN C CG  
8207  O OD1 . ASN C 245 ? 0.3347 0.5919 0.4277 -0.1670 0.0782  0.0210  254 ASN C OD1 
8208  N ND2 . ASN C 245 ? 0.3173 0.6152 0.4058 -0.1483 0.0829  0.0396  254 ASN C ND2 
8209  N N   . SER C 246 ? 0.2967 0.5396 0.3529 -0.0869 0.0795  0.0175  255 SER C N   
8210  C CA  . SER C 246 ? 0.3050 0.5743 0.3479 -0.0633 0.0789  0.0190  255 SER C CA  
8211  C C   . SER C 246 ? 0.2932 0.5506 0.3260 -0.0506 0.0742  0.0066  255 SER C C   
8212  O O   . SER C 246 ? 0.2971 0.5835 0.3257 -0.0426 0.0738  0.0054  255 SER C O   
8213  C CB  . SER C 246 ? 0.3153 0.5721 0.3468 -0.0464 0.0782  0.0227  255 SER C CB  
8214  O OG  . SER C 246 ? 0.3550 0.5967 0.3953 -0.0597 0.0808  0.0303  255 SER C OG  
8215  N N   . GLU C 247 ? 0.2859 0.5018 0.3148 -0.0493 0.0702  -0.0017 256 GLU C N   
8216  C CA  . GLU C 247 ? 0.2797 0.4813 0.2977 -0.0380 0.0643  -0.0117 256 GLU C CA  
8217  C C   . GLU C 247 ? 0.2670 0.4849 0.2936 -0.0487 0.0651  -0.0165 256 GLU C C   
8218  O O   . GLU C 247 ? 0.2672 0.5050 0.2857 -0.0373 0.0631  -0.0190 256 GLU C O   
8219  C CB  . GLU C 247 ? 0.2764 0.4349 0.2908 -0.0379 0.0598  -0.0170 256 GLU C CB  
8220  C CG  . GLU C 247 ? 0.3092 0.4530 0.3132 -0.0261 0.0579  -0.0125 256 GLU C CG  
8221  C CD  . GLU C 247 ? 0.3378 0.4438 0.3427 -0.0305 0.0549  -0.0145 256 GLU C CD  
8222  O OE1 . GLU C 247 ? 0.3567 0.4499 0.3737 -0.0451 0.0565  -0.0178 256 GLU C OE1 
8223  O OE2 . GLU C 247 ? 0.3393 0.4298 0.3315 -0.0184 0.0505  -0.0127 256 GLU C OE2 
8224  N N   . LEU C 248 ? 0.2592 0.4696 0.3009 -0.0699 0.0679  -0.0175 257 LEU C N   
8225  C CA  . LEU C 248 ? 0.2454 0.4680 0.2951 -0.0817 0.0682  -0.0227 257 LEU C CA  
8226  C C   . LEU C 248 ? 0.2490 0.5160 0.2987 -0.0784 0.0702  -0.0175 257 LEU C C   
8227  O O   . LEU C 248 ? 0.2459 0.5280 0.2927 -0.0737 0.0685  -0.0224 257 LEU C O   
8228  C CB  . LEU C 248 ? 0.2420 0.4531 0.3055 -0.1051 0.0706  -0.0229 257 LEU C CB  
8229  C CG  . LEU C 248 ? 0.2104 0.4362 0.2818 -0.1196 0.0705  -0.0277 257 LEU C CG  
8230  C CD1 . LEU C 248 ? 0.1765 0.3933 0.2438 -0.1127 0.0674  -0.0381 257 LEU C CD1 
8231  C CD2 . LEU C 248 ? 0.1984 0.4048 0.2784 -0.1400 0.0709  -0.0286 257 LEU C CD2 
8232  N N   . LEU C 249 ? 0.2597 0.5504 0.3125 -0.0805 0.0739  -0.0065 258 LEU C N   
8233  C CA  . LEU C 249 ? 0.2657 0.6072 0.3209 -0.0797 0.0765  0.0011  258 LEU C CA  
8234  C C   . LEU C 249 ? 0.2698 0.6277 0.3088 -0.0529 0.0742  -0.0022 258 LEU C C   
8235  O O   . LEU C 249 ? 0.2667 0.6522 0.3058 -0.0508 0.0740  -0.0041 258 LEU C O   
8236  C CB  . LEU C 249 ? 0.2710 0.6388 0.3327 -0.0871 0.0806  0.0157  258 LEU C CB  
8237  C CG  . LEU C 249 ? 0.2814 0.6560 0.3597 -0.1180 0.0815  0.0206  258 LEU C CG  
8238  C CD1 . LEU C 249 ? 0.3050 0.6810 0.3907 -0.1329 0.0833  0.0336  258 LEU C CD1 
8239  C CD2 . LEU C 249 ? 0.3062 0.7304 0.3900 -0.1243 0.0823  0.0250  258 LEU C CD2 
8240  N N   . SER C 250 ? 0.2815 0.6189 0.3049 -0.0321 0.0713  -0.0039 259 SER C N   
8241  C CA  . SER C 250 ? 0.2927 0.6405 0.2961 -0.0046 0.0674  -0.0074 259 SER C CA  
8242  C C   . SER C 250 ? 0.2865 0.6097 0.2834 -0.0015 0.0614  -0.0188 259 SER C C   
8243  O O   . SER C 250 ? 0.2927 0.6314 0.2775 0.0146  0.0584  -0.0220 259 SER C O   
8244  C CB  . SER C 250 ? 0.3061 0.6365 0.2915 0.0167  0.0643  -0.0062 259 SER C CB  
8245  O OG  . SER C 250 ? 0.3013 0.5806 0.2785 0.0184  0.0578  -0.0144 259 SER C OG  
8246  N N   . LEU C 251 ? 0.2769 0.5631 0.2816 -0.0166 0.0596  -0.0244 260 LEU C N   
8247  C CA  . LEU C 251 ? 0.2697 0.5366 0.2710 -0.0169 0.0545  -0.0334 260 LEU C CA  
8248  C C   . LEU C 251 ? 0.2632 0.5632 0.2738 -0.0251 0.0572  -0.0346 260 LEU C C   
8249  O O   . LEU C 251 ? 0.2626 0.5672 0.2636 -0.0141 0.0531  -0.0393 260 LEU C O   
8250  C CB  . LEU C 251 ? 0.2613 0.4924 0.2726 -0.0336 0.0538  -0.0376 260 LEU C CB  
8251  C CG  . LEU C 251 ? 0.2710 0.4635 0.2678 -0.0222 0.0462  -0.0408 260 LEU C CG  
8252  C CD1 . LEU C 251 ? 0.2746 0.4411 0.2830 -0.0386 0.0461  -0.0445 260 LEU C CD1 
8253  C CD2 . LEU C 251 ? 0.2697 0.4585 0.2477 -0.0047 0.0379  -0.0450 260 LEU C CD2 
8254  N N   . ILE C 252 ? 0.2635 0.5850 0.2922 -0.0456 0.0633  -0.0298 261 ILE C N   
8255  C CA  . ILE C 252 ? 0.2641 0.6188 0.3028 -0.0569 0.0656  -0.0300 261 ILE C CA  
8256  C C   . ILE C 252 ? 0.2787 0.6713 0.3059 -0.0362 0.0654  -0.0264 261 ILE C C   
8257  O O   . ILE C 252 ? 0.2802 0.6831 0.3018 -0.0282 0.0628  -0.0312 261 ILE C O   
8258  C CB  . ILE C 252 ? 0.2595 0.6330 0.3153 -0.0808 0.0705  -0.0227 261 ILE C CB  
8259  C CG1 . ILE C 252 ? 0.2592 0.5971 0.3247 -0.1012 0.0696  -0.0295 261 ILE C CG1 
8260  C CG2 . ILE C 252 ? 0.2487 0.6717 0.3116 -0.0879 0.0726  -0.0181 261 ILE C CG2 
8261  C CD1 . ILE C 252 ? 0.2720 0.6023 0.3473 -0.1194 0.0719  -0.0229 261 ILE C CD1 
8262  N N   . ASN C 253 ? 0.2990 0.7120 0.3213 -0.0254 0.0680  -0.0177 262 ASN C N   
8263  C CA  . ASN C 253 ? 0.3164 0.7691 0.3257 -0.0019 0.0683  -0.0133 262 ASN C CA  
8264  C C   . ASN C 253 ? 0.3279 0.7634 0.3161 0.0223  0.0613  -0.0226 262 ASN C C   
8265  O O   . ASN C 253 ? 0.3361 0.8052 0.3173 0.0360  0.0611  -0.0220 262 ASN C O   
8266  C CB  . ASN C 253 ? 0.3283 0.7873 0.3292 0.0120  0.0699  -0.0058 262 ASN C CB  
8267  C CG  . ASN C 253 ? 0.3460 0.8648 0.3442 0.0250  0.0741  0.0043  262 ASN C CG  
8268  O OD1 . ASN C 253 ? 0.3481 0.9070 0.3522 0.0221  0.0760  0.0065  262 ASN C OD1 
8269  N ND2 . ASN C 253 ? 0.3887 0.9185 0.3779 0.0402  0.0758  0.0114  262 ASN C ND2 
8270  N N   . ASP C 254 ? 0.3378 0.7209 0.3155 0.0268  0.0548  -0.0303 263 ASP C N   
8271  C CA  . ASP C 254 ? 0.3534 0.7137 0.3086 0.0482  0.0459  -0.0378 263 ASP C CA  
8272  C C   . ASP C 254 ? 0.3436 0.7007 0.3054 0.0376  0.0437  -0.0439 263 ASP C C   
8273  O O   . ASP C 254 ? 0.3542 0.6972 0.2985 0.0533  0.0362  -0.0489 263 ASP C O   
8274  C CB  . ASP C 254 ? 0.3709 0.6774 0.3114 0.0552  0.0382  -0.0417 263 ASP C CB  
8275  C CG  . ASP C 254 ? 0.4016 0.6756 0.3186 0.0718  0.0264  -0.0488 263 ASP C CG  
8276  O OD1 . ASP C 254 ? 0.4561 0.7436 0.3525 0.0963  0.0224  -0.0496 263 ASP C OD1 
8277  O OD2 . ASP C 254 ? 0.4073 0.6433 0.3253 0.0609  0.0206  -0.0528 263 ASP C OD2 
8278  N N   . MET C 255 ? 0.3282 0.6967 0.3136 0.0112  0.0495  -0.0435 264 MET C N   
8279  C CA  . MET C 255 ? 0.3226 0.6885 0.3144 0.0009  0.0475  -0.0497 264 MET C CA  
8280  C C   . MET C 255 ? 0.3254 0.7326 0.3123 0.0124  0.0479  -0.0489 264 MET C C   
8281  O O   . MET C 255 ? 0.3279 0.7788 0.3185 0.0158  0.0532  -0.0419 264 MET C O   
8282  C CB  . MET C 255 ? 0.3091 0.6739 0.3244 -0.0288 0.0527  -0.0507 264 MET C CB  
8283  C CG  . MET C 255 ? 0.3108 0.6379 0.3310 -0.0390 0.0530  -0.0510 264 MET C CG  
8284  S SD  . MET C 255 ? 0.2924 0.6131 0.3347 -0.0696 0.0572  -0.0540 264 MET C SD  
8285  C CE  . MET C 255 ? 0.3133 0.6865 0.3659 -0.0799 0.0613  -0.0504 264 MET C CE  
8286  N N   . PRO C 256 ? 0.3286 0.7246 0.3073 0.0183  0.0422  -0.0549 265 PRO C N   
8287  C CA  . PRO C 256 ? 0.3351 0.7672 0.3081 0.0304  0.0418  -0.0548 265 PRO C CA  
8288  C C   . PRO C 256 ? 0.3213 0.7945 0.3167 0.0086  0.0486  -0.0531 265 PRO C C   
8289  O O   . PRO C 256 ? 0.3171 0.7931 0.3156 0.0032  0.0467  -0.0578 265 PRO C O   
8290  C CB  . PRO C 256 ? 0.3420 0.7387 0.3004 0.0387  0.0324  -0.0615 265 PRO C CB  
8291  C CG  . PRO C 256 ? 0.3321 0.6918 0.3013 0.0189  0.0314  -0.0647 265 PRO C CG  
8292  C CD  . PRO C 256 ? 0.3338 0.6815 0.3049 0.0174  0.0344  -0.0610 265 PRO C CD  
8293  N N   . ILE C 257 ? 0.3206 0.8260 0.3305 -0.0041 0.0557  -0.0459 266 ILE C N   
8294  C CA  . ILE C 257 ? 0.3171 0.8607 0.3472 -0.0276 0.0606  -0.0431 266 ILE C CA  
8295  C C   . ILE C 257 ? 0.3243 0.9279 0.3582 -0.0238 0.0656  -0.0318 266 ILE C C   
8296  O O   . ILE C 257 ? 0.3365 0.9519 0.3586 -0.0032 0.0665  -0.0259 266 ILE C O   
8297  C CB  . ILE C 257 ? 0.3102 0.8307 0.3582 -0.0576 0.0628  -0.0444 266 ILE C CB  
8298  C CG1 . ILE C 257 ? 0.3117 0.8150 0.3592 -0.0576 0.0647  -0.0389 266 ILE C CG1 
8299  C CG2 . ILE C 257 ? 0.3120 0.7884 0.3604 -0.0649 0.0589  -0.0552 266 ILE C CG2 
8300  C CD1 . ILE C 257 ? 0.3075 0.8036 0.3722 -0.0864 0.0675  -0.0364 266 ILE C CD1 
8301  N N   . THR C 258 ? 0.3175 0.9609 0.3673 -0.0437 0.0684  -0.0282 267 THR C N   
8302  C CA  . THR C 258 ? 0.3182 1.0249 0.3753 -0.0461 0.0729  -0.0150 267 THR C CA  
8303  C C   . THR C 258 ? 0.3198 1.0285 0.3847 -0.0581 0.0761  -0.0052 267 THR C C   
8304  O O   . THR C 258 ? 0.3180 0.9797 0.3860 -0.0699 0.0751  -0.0092 267 THR C O   
8305  C CB  . THR C 258 ? 0.3119 1.0579 0.3856 -0.0707 0.0738  -0.0124 267 THR C CB  
8306  O OG1 . THR C 258 ? 0.3215 1.0781 0.4123 -0.1017 0.0755  -0.0040 267 THR C OG1 
8307  C CG2 . THR C 258 ? 0.3077 1.0205 0.3827 -0.0793 0.0701  -0.0256 267 THR C CG2 
8308  N N   . ASN C 259 ? 0.3221 1.0886 0.3905 -0.0551 0.0799  0.0087  268 ASN C N   
8309  C CA  . ASN C 259 ? 0.3273 1.1001 0.4026 -0.0658 0.0827  0.0197  268 ASN C CA  
8310  C C   . ASN C 259 ? 0.3257 1.0889 0.4205 -0.1055 0.0822  0.0241  268 ASN C C   
8311  O O   . ASN C 259 ? 0.3283 1.0621 0.4259 -0.1152 0.0824  0.0269  268 ASN C O   
8312  C CB  . ASN C 259 ? 0.3375 1.1793 0.4103 -0.0499 0.0868  0.0348  268 ASN C CB  
8313  C CG  . ASN C 259 ? 0.3581 1.1900 0.4091 -0.0123 0.0871  0.0329  268 ASN C CG  
8314  O OD1 . ASN C 259 ? 0.3779 1.1510 0.4144 0.0025  0.0832  0.0197  268 ASN C OD1 
8315  N ND2 . ASN C 259 ? 0.3750 1.2642 0.4222 0.0038  0.0911  0.0464  268 ASN C ND2 
8316  N N   . ASP C 260 ? 0.3248 1.1122 0.4314 -0.1280 0.0806  0.0249  269 ASP C N   
8317  C CA  . ASP C 260 ? 0.3294 1.1049 0.4514 -0.1668 0.0778  0.0281  269 ASP C CA  
8318  C C   . ASP C 260 ? 0.3214 1.0222 0.4400 -0.1720 0.0750  0.0130  269 ASP C C   
8319  O O   . ASP C 260 ? 0.3324 1.0004 0.4560 -0.1910 0.0735  0.0146  269 ASP C O   
8320  C CB  . ASP C 260 ? 0.3326 1.1437 0.4641 -0.1869 0.0753  0.0292  269 ASP C CB  
8321  C CG  . ASP C 260 ? 0.3631 1.2555 0.5008 -0.1870 0.0777  0.0472  269 ASP C CG  
8322  O OD1 . ASP C 260 ? 0.4022 1.3231 0.5410 -0.1829 0.0807  0.0617  269 ASP C OD1 
8323  O OD2 . ASP C 260 ? 0.3965 1.3283 0.5380 -0.1908 0.0768  0.0479  269 ASP C OD2 
8324  N N   . GLN C 261 ? 0.3005 0.9758 0.4097 -0.1536 0.0741  -0.0010 270 GLN C N   
8325  C CA  . GLN C 261 ? 0.2934 0.9056 0.3987 -0.1547 0.0717  -0.0144 270 GLN C CA  
8326  C C   . GLN C 261 ? 0.2890 0.8686 0.3903 -0.1488 0.0730  -0.0115 270 GLN C C   
8327  O O   . GLN C 261 ? 0.2921 0.8347 0.3984 -0.1667 0.0716  -0.0137 270 GLN C O   
8328  C CB  . GLN C 261 ? 0.2905 0.8898 0.3843 -0.1309 0.0705  -0.0254 270 GLN C CB  
8329  C CG  . GLN C 261 ? 0.3100 0.8681 0.4059 -0.1424 0.0673  -0.0387 270 GLN C CG  
8330  C CD  . GLN C 261 ? 0.3357 0.8971 0.4245 -0.1277 0.0653  -0.0472 270 GLN C CD  
8331  O OE1 . GLN C 261 ? 0.3603 0.8817 0.4444 -0.1237 0.0628  -0.0573 270 GLN C OE1 
8332  N NE2 . GLN C 261 ? 0.3346 0.9451 0.4227 -0.1200 0.0662  -0.0424 270 GLN C NE2 
8333  N N   . LYS C 262 ? 0.2791 0.8738 0.3702 -0.1229 0.0754  -0.0063 271 LYS C N   
8334  C CA  . LYS C 262 ? 0.2751 0.8419 0.3612 -0.1154 0.0764  -0.0034 271 LYS C CA  
8335  C C   . LYS C 262 ? 0.2798 0.8524 0.3786 -0.1414 0.0776  0.0075  271 LYS C C   
8336  O O   . LYS C 262 ? 0.2860 0.8153 0.3859 -0.1499 0.0767  0.0051  271 LYS C O   
8337  C CB  . LYS C 262 ? 0.2739 0.8636 0.3457 -0.0840 0.0782  0.0017  271 LYS C CB  
8338  C CG  . LYS C 262 ? 0.2750 0.8417 0.3295 -0.0574 0.0747  -0.0097 271 LYS C CG  
8339  C CD  . LYS C 262 ? 0.2927 0.8652 0.3280 -0.0251 0.0742  -0.0071 271 LYS C CD  
8340  C CE  . LYS C 262 ? 0.3007 0.8795 0.3189 0.0005  0.0704  -0.0139 271 LYS C CE  
8341  N NZ  . LYS C 262 ? 0.3082 0.8766 0.3017 0.0344  0.0672  -0.0148 271 LYS C NZ  
8342  N N   . LYS C 263 ? 0.2805 0.9068 0.3886 -0.1551 0.0787  0.0202  272 LYS C N   
8343  C CA  . LYS C 263 ? 0.2914 0.9276 0.4111 -0.1824 0.0783  0.0335  272 LYS C CA  
8344  C C   . LYS C 263 ? 0.2898 0.8773 0.4154 -0.2104 0.0736  0.0260  272 LYS C C   
8345  O O   . LYS C 263 ? 0.3016 0.8620 0.4300 -0.2251 0.0722  0.0310  272 LYS C O   
8346  C CB  . LYS C 263 ? 0.3001 1.0066 0.4290 -0.1947 0.0790  0.0490  272 LYS C CB  
8347  C CG  . LYS C 263 ? 0.3499 1.0678 0.4911 -0.2290 0.0762  0.0643  272 LYS C CG  
8348  C CD  . LYS C 263 ? 0.4163 1.2070 0.5676 -0.2448 0.0754  0.0798  272 LYS C CD  
8349  C CE  . LYS C 263 ? 0.4591 1.2777 0.6216 -0.2755 0.0727  0.1017  272 LYS C CE  
8350  N NZ  . LYS C 263 ? 0.4798 1.3797 0.6519 -0.2876 0.0723  0.1193  272 LYS C NZ  
8351  N N   . LEU C 264 ? 0.2750 0.8517 0.4010 -0.2162 0.0707  0.0140  273 LEU C N   
8352  C CA  . LEU C 264 ? 0.2723 0.8015 0.4004 -0.2381 0.0657  0.0039  273 LEU C CA  
8353  C C   . LEU C 264 ? 0.2688 0.7385 0.3905 -0.2290 0.0660  -0.0052 273 LEU C C   
8354  O O   . LEU C 264 ? 0.2821 0.7177 0.4051 -0.2456 0.0632  -0.0041 273 LEU C O   
8355  C CB  . LEU C 264 ? 0.2629 0.7915 0.3899 -0.2375 0.0636  -0.0091 273 LEU C CB  
8356  C CG  . LEU C 264 ? 0.2524 0.7353 0.3794 -0.2575 0.0581  -0.0208 273 LEU C CG  
8357  C CD1 . LEU C 264 ? 0.2680 0.7594 0.4012 -0.2907 0.0523  -0.0120 273 LEU C CD1 
8358  C CD2 . LEU C 264 ? 0.2282 0.7164 0.3533 -0.2510 0.0574  -0.0330 273 LEU C CD2 
8359  N N   . MET C 265 ? 0.2509 0.7074 0.3644 -0.2024 0.0685  -0.0138 274 MET C N   
8360  C CA  . MET C 265 ? 0.2485 0.6536 0.3559 -0.1925 0.0686  -0.0214 274 MET C CA  
8361  C C   . MET C 265 ? 0.2617 0.6578 0.3698 -0.1950 0.0702  -0.0108 274 MET C C   
8362  O O   . MET C 265 ? 0.2741 0.6289 0.3823 -0.2042 0.0686  -0.0135 274 MET C O   
8363  C CB  . MET C 265 ? 0.2285 0.6276 0.3260 -0.1646 0.0696  -0.0288 274 MET C CB  
8364  C CG  . MET C 265 ? 0.2152 0.6109 0.3122 -0.1651 0.0674  -0.0402 274 MET C CG  
8365  S SD  . MET C 265 ? 0.1939 0.5803 0.2783 -0.1361 0.0664  -0.0474 274 MET C SD  
8366  C CE  . MET C 265 ? 0.2144 0.5449 0.2944 -0.1319 0.0653  -0.0520 274 MET C CE  
8367  N N   . SER C 266 ? 0.2660 0.7030 0.3743 -0.1865 0.0732  0.0019  275 SER C N   
8368  C CA  . SER C 266 ? 0.2783 0.7130 0.3873 -0.1877 0.0751  0.0136  275 SER C CA  
8369  C C   . SER C 266 ? 0.3025 0.7271 0.4202 -0.2184 0.0720  0.0216  275 SER C C   
8370  O O   . SER C 266 ? 0.3119 0.7066 0.4288 -0.2228 0.0718  0.0253  275 SER C O   
8371  C CB  . SER C 266 ? 0.2731 0.7618 0.3804 -0.1725 0.0788  0.0261  275 SER C CB  
8372  O OG  . SER C 266 ? 0.2604 0.7530 0.3563 -0.1440 0.0797  0.0174  275 SER C OG  
8373  N N   . ASN C 267 ? 0.3193 0.7662 0.4438 -0.2406 0.0686  0.0244  276 ASN C N   
8374  C CA  . ASN C 267 ? 0.3511 0.7822 0.4807 -0.2717 0.0632  0.0319  276 ASN C CA  
8375  C C   . ASN C 267 ? 0.3635 0.7343 0.4886 -0.2822 0.0580  0.0172  276 ASN C C   
8376  O O   . ASN C 267 ? 0.3896 0.7445 0.5158 -0.3088 0.0513  0.0204  276 ASN C O   
8377  C CB  . ASN C 267 ? 0.3621 0.8442 0.5002 -0.2948 0.0599  0.0444  276 ASN C CB  
8378  C CG  . ASN C 267 ? 0.3827 0.9242 0.5263 -0.2911 0.0640  0.0647  276 ASN C CG  
8379  O OD1 . ASN C 267 ? 0.4201 0.9555 0.5630 -0.2873 0.0662  0.0742  276 ASN C OD1 
8380  N ND2 . ASN C 267 ? 0.3953 0.9973 0.5439 -0.2910 0.0653  0.0719  276 ASN C ND2 
8381  N N   . ASN C 268 ? 0.3526 0.6899 0.4711 -0.2616 0.0603  0.0018  277 ASN C N   
8382  C CA  . ASN C 268 ? 0.3612 0.6488 0.4746 -0.2680 0.0560  -0.0132 277 ASN C CA  
8383  C C   . ASN C 268 ? 0.3550 0.6026 0.4621 -0.2475 0.0587  -0.0236 277 ASN C C   
8384  O O   . ASN C 268 ? 0.3634 0.5793 0.4659 -0.2462 0.0564  -0.0373 277 ASN C O   
8385  C CB  . ASN C 268 ? 0.3540 0.6562 0.4680 -0.2710 0.0539  -0.0234 277 ASN C CB  
8386  C CG  . ASN C 268 ? 0.3709 0.6902 0.4887 -0.2995 0.0476  -0.0175 277 ASN C CG  
8387  O OD1 . ASN C 268 ? 0.4020 0.6841 0.5151 -0.3178 0.0407  -0.0221 277 ASN C OD1 
8388  N ND2 . ASN C 268 ? 0.3681 0.7436 0.4929 -0.3035 0.0490  -0.0069 277 ASN C ND2 
8389  N N   . VAL C 269 ? 0.3423 0.5938 0.4484 -0.2313 0.0631  -0.0168 278 VAL C N   
8390  C CA  . VAL C 269 ? 0.3331 0.5502 0.4332 -0.2119 0.0653  -0.0242 278 VAL C CA  
8391  C C   . VAL C 269 ? 0.3401 0.5101 0.4358 -0.2152 0.0623  -0.0365 278 VAL C C   
8392  O O   . VAL C 269 ? 0.3314 0.4871 0.4236 -0.2003 0.0633  -0.0463 278 VAL C O   
8393  C CB  . VAL C 269 ? 0.3384 0.5505 0.4378 -0.2066 0.0677  -0.0131 278 VAL C CB  
8394  C CG1 . VAL C 269 ? 0.3132 0.5627 0.4115 -0.1886 0.0716  -0.0061 278 VAL C CG1 
8395  C CG2 . VAL C 269 ? 0.3776 0.5917 0.4814 -0.2304 0.0651  -0.0010 278 VAL C CG2 
8396  N N   . GLN C 270 ? 0.3615 0.5082 0.4564 -0.2344 0.0580  -0.0356 279 GLN C N   
8397  C CA  . GLN C 270 ? 0.3769 0.4780 0.4649 -0.2347 0.0549  -0.0475 279 GLN C CA  
8398  C C   . GLN C 270 ? 0.3591 0.4599 0.4448 -0.2278 0.0543  -0.0620 279 GLN C C   
8399  O O   . GLN C 270 ? 0.3517 0.4372 0.4343 -0.2112 0.0564  -0.0698 279 GLN C O   
8400  C CB  . GLN C 270 ? 0.4179 0.4936 0.5018 -0.2573 0.0482  -0.0451 279 GLN C CB  
8401  C CG  . GLN C 270 ? 0.4709 0.4949 0.5451 -0.2524 0.0458  -0.0528 279 GLN C CG  
8402  C CD  . GLN C 270 ? 0.5654 0.5579 0.6317 -0.2746 0.0370  -0.0512 279 GLN C CD  
8403  O OE1 . GLN C 270 ? 0.6072 0.6085 0.6726 -0.2934 0.0309  -0.0523 279 GLN C OE1 
8404  N NE2 . GLN C 270 ? 0.5932 0.5473 0.6524 -0.2734 0.0351  -0.0482 279 GLN C NE2 
8405  N N   . ILE C 271 ? 0.3517 0.4718 0.4392 -0.2412 0.0511  -0.0648 280 ILE C N   
8406  C CA  . ILE C 271 ? 0.3307 0.4575 0.4169 -0.2350 0.0507  -0.0774 280 ILE C CA  
8407  C C   . ILE C 271 ? 0.2976 0.4407 0.3857 -0.2124 0.0559  -0.0790 280 ILE C C   
8408  O O   . ILE C 271 ? 0.2941 0.4201 0.3786 -0.2004 0.0563  -0.0881 280 ILE C O   
8409  C CB  . ILE C 271 ? 0.3327 0.4926 0.4231 -0.2508 0.0478  -0.0760 280 ILE C CB  
8410  C CG1 . ILE C 271 ? 0.3589 0.5033 0.4464 -0.2767 0.0406  -0.0721 280 ILE C CG1 
8411  C CG2 . ILE C 271 ? 0.3168 0.4843 0.4056 -0.2448 0.0473  -0.0890 280 ILE C CG2 
8412  C CD1 . ILE C 271 ? 0.3777 0.4916 0.4556 -0.2860 0.0336  -0.0865 280 ILE C CD1 
8413  N N   . VAL C 272 ? 0.2755 0.4517 0.3679 -0.2066 0.0589  -0.0694 281 VAL C N   
8414  C CA  . VAL C 272 ? 0.2494 0.4372 0.3402 -0.1859 0.0616  -0.0698 281 VAL C CA  
8415  C C   . VAL C 272 ? 0.2533 0.4073 0.3397 -0.1737 0.0621  -0.0738 281 VAL C C   
8416  O O   . VAL C 272 ? 0.2522 0.4008 0.3361 -0.1634 0.0615  -0.0808 281 VAL C O   
8417  C CB  . VAL C 272 ? 0.2358 0.4505 0.3276 -0.1788 0.0641  -0.0581 281 VAL C CB  
8418  C CG1 . VAL C 272 ? 0.2077 0.4313 0.2942 -0.1579 0.0647  -0.0596 281 VAL C CG1 
8419  C CG2 . VAL C 272 ? 0.2346 0.4863 0.3316 -0.1914 0.0639  -0.0522 281 VAL C CG2 
8420  N N   . ARG C 273 ? 0.2614 0.3943 0.3470 -0.1756 0.0629  -0.0683 282 ARG C N   
8421  C CA  . ARG C 273 ? 0.2588 0.3634 0.3405 -0.1641 0.0634  -0.0706 282 ARG C CA  
8422  C C   . ARG C 273 ? 0.2749 0.3612 0.3543 -0.1647 0.0616  -0.0823 282 ARG C C   
8423  O O   . ARG C 273 ? 0.2720 0.3567 0.3497 -0.1529 0.0616  -0.0865 282 ARG C O   
8424  C CB  . ARG C 273 ? 0.2680 0.3523 0.3492 -0.1680 0.0643  -0.0634 282 ARG C CB  
8425  C CG  . ARG C 273 ? 0.2461 0.3505 0.3289 -0.1650 0.0664  -0.0514 282 ARG C CG  
8426  C CD  . ARG C 273 ? 0.2446 0.3261 0.3257 -0.1618 0.0676  -0.0450 282 ARG C CD  
8427  N NE  . ARG C 273 ? 0.2399 0.3417 0.3221 -0.1595 0.0696  -0.0329 282 ARG C NE  
8428  C CZ  . ARG C 273 ? 0.2463 0.3506 0.3244 -0.1435 0.0710  -0.0287 282 ARG C CZ  
8429  N NH1 . ARG C 273 ? 0.2257 0.3127 0.2990 -0.1302 0.0698  -0.0344 282 ARG C NH1 
8430  N NH2 . ARG C 273 ? 0.2677 0.3936 0.3459 -0.1414 0.0728  -0.0179 282 ARG C NH2 
8431  N N   . GLN C 274 ? 0.2998 0.3739 0.3778 -0.1783 0.0593  -0.0875 283 GLN C N   
8432  C CA  . GLN C 274 ? 0.3194 0.3754 0.3926 -0.1763 0.0573  -0.0996 283 GLN C CA  
8433  C C   . GLN C 274 ? 0.2976 0.3759 0.3725 -0.1698 0.0575  -0.1060 283 GLN C C   
8434  O O   . GLN C 274 ? 0.3036 0.3732 0.3751 -0.1623 0.0570  -0.1142 283 GLN C O   
8435  C CB  . GLN C 274 ? 0.3528 0.3908 0.4211 -0.1925 0.0529  -0.1046 283 GLN C CB  
8436  C CG  . GLN C 274 ? 0.4201 0.4298 0.4848 -0.1984 0.0516  -0.0982 283 GLN C CG  
8437  C CD  . GLN C 274 ? 0.5108 0.5004 0.5689 -0.2181 0.0450  -0.1003 283 GLN C CD  
8438  O OE1 . GLN C 274 ? 0.5563 0.5595 0.6145 -0.2301 0.0414  -0.1047 283 GLN C OE1 
8439  N NE2 . GLN C 274 ? 0.5346 0.4905 0.5861 -0.2222 0.0423  -0.0968 283 GLN C NE2 
8440  N N   . GLN C 275 ? 0.2775 0.3863 0.3569 -0.1711 0.0581  -0.1014 284 GLN C N   
8441  C CA  . GLN C 275 ? 0.2628 0.3924 0.3431 -0.1651 0.0577  -0.1064 284 GLN C CA  
8442  C C   . GLN C 275 ? 0.2381 0.3736 0.3176 -0.1495 0.0583  -0.1018 284 GLN C C   
8443  O O   . GLN C 275 ? 0.2229 0.3734 0.3020 -0.1439 0.0570  -0.1044 284 GLN C O   
8444  C CB  . GLN C 275 ? 0.2642 0.4242 0.3481 -0.1744 0.0571  -0.1045 284 GLN C CB  
8445  C CG  . GLN C 275 ? 0.3066 0.4638 0.3899 -0.1905 0.0542  -0.1117 284 GLN C CG  
8446  C CD  . GLN C 275 ? 0.3365 0.5291 0.4243 -0.2002 0.0534  -0.1088 284 GLN C CD  
8447  O OE1 . GLN C 275 ? 0.3380 0.5526 0.4296 -0.2012 0.0550  -0.0982 284 GLN C OE1 
8448  N NE2 . GLN C 275 ? 0.3460 0.5473 0.4330 -0.2066 0.0508  -0.1178 284 GLN C NE2 
8449  N N   . SER C 276 ? 0.2324 0.3547 0.3105 -0.1430 0.0593  -0.0947 285 SER C N   
8450  C CA  . SER C 276 ? 0.2202 0.3455 0.2951 -0.1297 0.0580  -0.0897 285 SER C CA  
8451  C C   . SER C 276 ? 0.2238 0.3288 0.2968 -0.1226 0.0572  -0.0902 285 SER C C   
8452  O O   . SER C 276 ? 0.2389 0.3266 0.3125 -0.1256 0.0587  -0.0940 285 SER C O   
8453  C CB  . SER C 276 ? 0.2182 0.3480 0.2913 -0.1258 0.0587  -0.0807 285 SER C CB  
8454  O OG  . SER C 276 ? 0.2226 0.3758 0.2984 -0.1330 0.0600  -0.0789 285 SER C OG  
8455  N N   . TYR C 277 ? 0.2157 0.3229 0.2851 -0.1131 0.0539  -0.0861 286 TYR C N   
8456  C CA  . TYR C 277 ? 0.2174 0.3110 0.2855 -0.1071 0.0523  -0.0841 286 TYR C CA  
8457  C C   . TYR C 277 ? 0.2185 0.3031 0.2812 -0.0999 0.0492  -0.0752 286 TYR C C   
8458  O O   . TYR C 277 ? 0.2246 0.3154 0.2824 -0.0965 0.0470  -0.0718 286 TYR C O   
8459  C CB  . TYR C 277 ? 0.2087 0.3142 0.2766 -0.1049 0.0489  -0.0862 286 TYR C CB  
8460  C CG  . TYR C 277 ? 0.2209 0.3344 0.2926 -0.1097 0.0514  -0.0955 286 TYR C CG  
8461  C CD1 . TYR C 277 ? 0.2499 0.3752 0.3231 -0.1164 0.0526  -0.1012 286 TYR C CD1 
8462  C CD2 . TYR C 277 ? 0.2416 0.3530 0.3141 -0.1065 0.0519  -0.0983 286 TYR C CD2 
8463  C CE1 . TYR C 277 ? 0.2772 0.4083 0.3521 -0.1209 0.0539  -0.1105 286 TYR C CE1 
8464  C CE2 . TYR C 277 ? 0.2720 0.3903 0.3454 -0.1088 0.0536  -0.1079 286 TYR C CE2 
8465  C CZ  . TYR C 277 ? 0.2801 0.4063 0.3541 -0.1164 0.0542  -0.1144 286 TYR C CZ  
8466  O OH  . TYR C 277 ? 0.3120 0.4433 0.3851 -0.1193 0.0549  -0.1249 286 TYR C OH  
8467  N N   . SER C 278 ? 0.2196 0.2900 0.2818 -0.0963 0.0486  -0.0715 287 SER C N   
8468  C CA  . SER C 278 ? 0.2186 0.2800 0.2743 -0.0900 0.0440  -0.0632 287 SER C CA  
8469  C C   . SER C 278 ? 0.2185 0.2794 0.2733 -0.0880 0.0390  -0.0595 287 SER C C   
8470  O O   . SER C 278 ? 0.2228 0.2831 0.2828 -0.0885 0.0419  -0.0609 287 SER C O   
8471  C CB  . SER C 278 ? 0.2255 0.2724 0.2819 -0.0892 0.0477  -0.0599 287 SER C CB  
8472  O OG  . SER C 278 ? 0.2318 0.2698 0.2807 -0.0827 0.0427  -0.0524 287 SER C OG  
8473  N N   . ILE C 279 ? 0.2212 0.2834 0.2683 -0.0856 0.0308  -0.0545 288 ILE C N   
8474  C CA  . ILE C 279 ? 0.2286 0.2934 0.2747 -0.0864 0.0243  -0.0487 288 ILE C CA  
8475  C C   . ILE C 279 ? 0.2489 0.2977 0.2861 -0.0835 0.0170  -0.0397 288 ILE C C   
8476  O O   . ILE C 279 ? 0.2670 0.3055 0.2936 -0.0794 0.0123  -0.0384 288 ILE C O   
8477  C CB  . ILE C 279 ? 0.2218 0.2959 0.2627 -0.0878 0.0173  -0.0478 288 ILE C CB  
8478  C CG1 . ILE C 279 ? 0.2115 0.2997 0.2567 -0.0894 0.0228  -0.0569 288 ILE C CG1 
8479  C CG2 . ILE C 279 ? 0.2327 0.3158 0.2755 -0.0915 0.0116  -0.0411 288 ILE C CG2 
8480  C CD1 . ILE C 279 ? 0.2150 0.3190 0.2691 -0.0933 0.0271  -0.0620 288 ILE C CD1 
8481  N N   . MET C 280 ? 0.2611 0.3089 0.3012 -0.0846 0.0153  -0.0332 289 MET C N   
8482  C CA  . MET C 280 ? 0.2767 0.3093 0.3084 -0.0831 0.0078  -0.0243 289 MET C CA  
8483  C C   . MET C 280 ? 0.2875 0.3165 0.3075 -0.0859 -0.0054 -0.0184 289 MET C C   
8484  O O   . MET C 280 ? 0.2860 0.3296 0.3094 -0.0908 -0.0081 -0.0170 289 MET C O   
8485  C CB  . MET C 280 ? 0.2788 0.3179 0.3180 -0.0846 0.0094  -0.0184 289 MET C CB  
8486  C CG  . MET C 280 ? 0.3001 0.3251 0.3332 -0.0834 0.0039  -0.0098 289 MET C CG  
8487  S SD  . MET C 280 ? 0.3155 0.3557 0.3582 -0.0845 0.0057  -0.0013 289 MET C SD  
8488  C CE  . MET C 280 ? 0.3206 0.3857 0.3660 -0.0920 -0.0016 0.0047  289 MET C CE  
8489  N N   . SER C 281 ? 0.3102 0.3190 0.3151 -0.0824 -0.0144 -0.0149 290 SER C N   
8490  C CA  . SER C 281 ? 0.3365 0.3350 0.3258 -0.0844 -0.0293 -0.0098 290 SER C CA  
8491  C C   . SER C 281 ? 0.3520 0.3357 0.3314 -0.0894 -0.0426 0.0019  290 SER C C   
8492  O O   . SER C 281 ? 0.3589 0.3512 0.3396 -0.0987 -0.0504 0.0100  290 SER C O   
8493  C CB  . SER C 281 ? 0.3538 0.3387 0.3277 -0.0750 -0.0325 -0.0158 290 SER C CB  
8494  O OG  . SER C 281 ? 0.3902 0.3600 0.3458 -0.0756 -0.0483 -0.0113 290 SER C OG  
8495  N N   . ILE C 282 ? 0.3651 0.3284 0.3341 -0.0844 -0.0461 0.0037  291 ILE C N   
8496  C CA  . ILE C 282 ? 0.3815 0.3350 0.3447 -0.0912 -0.0573 0.0154  291 ILE C CA  
8497  C C   . ILE C 282 ? 0.3799 0.3248 0.3437 -0.0866 -0.0533 0.0166  291 ILE C C   
8498  O O   . ILE C 282 ? 0.3757 0.3086 0.3328 -0.0763 -0.0488 0.0098  291 ILE C O   
8499  C CB  . ILE C 282 ? 0.4126 0.3404 0.3517 -0.0949 -0.0782 0.0221  291 ILE C CB  
8500  C CG1 . ILE C 282 ? 0.4199 0.3298 0.3415 -0.0832 -0.0812 0.0127  291 ILE C CG1 
8501  C CG2 . ILE C 282 ? 0.4260 0.3673 0.3688 -0.1102 -0.0884 0.0337  291 ILE C CG2 
8502  C CD1 . ILE C 282 ? 0.4423 0.3258 0.3453 -0.0715 -0.0856 0.0098  291 ILE C CD1 
8503  N N   . ILE C 283 ? 0.3828 0.3372 0.3546 -0.0942 -0.0551 0.0265  292 ILE C N   
8504  C CA  . ILE C 283 ? 0.3901 0.3403 0.3648 -0.0910 -0.0510 0.0296  292 ILE C CA  
8505  C C   . ILE C 283 ? 0.4092 0.3443 0.3698 -0.0980 -0.0678 0.0414  292 ILE C C   
8506  O O   . ILE C 283 ? 0.4098 0.3529 0.3696 -0.1100 -0.0789 0.0520  292 ILE C O   
8507  C CB  . ILE C 283 ? 0.3712 0.3471 0.3673 -0.0919 -0.0379 0.0318  292 ILE C CB  
8508  C CG1 . ILE C 283 ? 0.3772 0.3789 0.3866 -0.0958 -0.0322 0.0300  292 ILE C CG1 
8509  C CG2 . ILE C 283 ? 0.3574 0.3296 0.3603 -0.0821 -0.0238 0.0244  292 ILE C CG2 
8510  C CD1 . ILE C 283 ? 0.4043 0.4054 0.4139 -0.0922 -0.0265 0.0181  292 ILE C CD1 
8511  N N   . LYS C 284 ? 0.4245 0.3387 0.3735 -0.0910 -0.0701 0.0402  293 LYS C N   
8512  C CA  . LYS C 284 ? 0.4548 0.3512 0.3885 -0.0964 -0.0859 0.0500  293 LYS C CA  
8513  C C   . LYS C 284 ? 0.4551 0.3539 0.3963 -0.0886 -0.0749 0.0488  293 LYS C C   
8514  O O   . LYS C 284 ? 0.4434 0.3487 0.3946 -0.0789 -0.0592 0.0395  293 LYS C O   
8515  C CB  . LYS C 284 ? 0.4838 0.3448 0.3885 -0.0917 -0.1017 0.0464  293 LYS C CB  
8516  C CG  . LYS C 284 ? 0.5004 0.3565 0.3966 -0.0957 -0.1104 0.0449  293 LYS C CG  
8517  C CD  . LYS C 284 ? 0.5554 0.3726 0.4190 -0.0962 -0.1335 0.0472  293 LYS C CD  
8518  C CE  . LYS C 284 ? 0.5825 0.3956 0.4385 -0.1017 -0.1427 0.0477  293 LYS C CE  
8519  N NZ  . LYS C 284 ? 0.6423 0.4257 0.4735 -0.1146 -0.1692 0.0590  293 LYS C NZ  
8520  N N   . GLU C 285 ? 0.4750 0.3691 0.4114 -0.0938 -0.0836 0.0589  294 GLU C N   
8521  C CA  . GLU C 285 ? 0.4803 0.3780 0.4242 -0.0868 -0.0736 0.0593  294 GLU C CA  
8522  C C   . GLU C 285 ? 0.4712 0.3529 0.4074 -0.0723 -0.0660 0.0485  294 GLU C C   
8523  O O   . GLU C 285 ? 0.4566 0.3479 0.4056 -0.0655 -0.0514 0.0457  294 GLU C O   
8524  C CB  . GLU C 285 ? 0.5089 0.3998 0.4436 -0.0944 -0.0873 0.0719  294 GLU C CB  
8525  C CG  . GLU C 285 ? 0.5533 0.4736 0.5027 -0.1082 -0.0904 0.0861  294 GLU C CG  
8526  C CD  . GLU C 285 ? 0.6176 0.5348 0.5586 -0.1174 -0.1045 0.1001  294 GLU C CD  
8527  O OE1 . GLU C 285 ? 0.6203 0.5338 0.5618 -0.1098 -0.0991 0.1000  294 GLU C OE1 
8528  O OE2 . GLU C 285 ? 0.6575 0.5768 0.5915 -0.1332 -0.1216 0.1119  294 GLU C OE2 
8529  N N   . GLU C 286 ? 0.4807 0.3389 0.3951 -0.0673 -0.0766 0.0432  295 GLU C N   
8530  C CA  . GLU C 286 ? 0.4865 0.3318 0.3899 -0.0524 -0.0719 0.0349  295 GLU C CA  
8531  C C   . GLU C 286 ? 0.4692 0.3159 0.3700 -0.0441 -0.0662 0.0245  295 GLU C C   
8532  O O   . GLU C 286 ? 0.4726 0.3143 0.3645 -0.0310 -0.0619 0.0182  295 GLU C O   
8533  C CB  . GLU C 286 ? 0.5267 0.3424 0.4020 -0.0476 -0.0888 0.0372  295 GLU C CB  
8534  C CG  . GLU C 286 ? 0.5928 0.3877 0.4492 -0.0595 -0.1117 0.0451  295 GLU C CG  
8535  C CD  . GLU C 286 ? 0.6508 0.4420 0.5021 -0.0648 -0.1188 0.0428  295 GLU C CD  
8536  O OE1 . GLU C 286 ? 0.6503 0.4625 0.5196 -0.0786 -0.1169 0.0495  295 GLU C OE1 
8537  O OE2 . GLU C 286 ? 0.6816 0.4513 0.5110 -0.0537 -0.1258 0.0345  295 GLU C OE2 
8538  N N   . VAL C 287 ? 0.4478 0.3050 0.3566 -0.0513 -0.0658 0.0232  296 VAL C N   
8539  C CA  . VAL C 287 ? 0.4280 0.2926 0.3384 -0.0447 -0.0584 0.0138  296 VAL C CA  
8540  C C   . VAL C 287 ? 0.3993 0.2874 0.3314 -0.0535 -0.0490 0.0128  296 VAL C C   
8541  O O   . VAL C 287 ? 0.4015 0.2942 0.3375 -0.0646 -0.0558 0.0191  296 VAL C O   
8542  C CB  . VAL C 287 ? 0.4488 0.2930 0.3347 -0.0403 -0.0735 0.0108  296 VAL C CB  
8543  C CG1 . VAL C 287 ? 0.4447 0.2984 0.3303 -0.0285 -0.0641 0.0010  296 VAL C CG1 
8544  C CG2 . VAL C 287 ? 0.4940 0.3066 0.3513 -0.0340 -0.0903 0.0132  296 VAL C CG2 
8545  N N   . LEU C 288 ? 0.3717 0.2755 0.3167 -0.0490 -0.0342 0.0053  297 LEU C N   
8546  C CA  . LEU C 288 ? 0.3448 0.2690 0.3074 -0.0558 -0.0257 0.0022  297 LEU C CA  
8547  C C   . LEU C 288 ? 0.3361 0.2642 0.2938 -0.0505 -0.0240 -0.0059 297 LEU C C   
8548  O O   . LEU C 288 ? 0.3463 0.2738 0.2989 -0.0413 -0.0193 -0.0101 297 LEU C O   
8549  C CB  . LEU C 288 ? 0.3258 0.2650 0.3090 -0.0572 -0.0100 0.0008  297 LEU C CB  
8550  C CG  . LEU C 288 ? 0.3127 0.2704 0.3112 -0.0616 -0.0004 -0.0054 297 LEU C CG  
8551  C CD1 . LEU C 288 ? 0.3234 0.2907 0.3259 -0.0693 -0.0059 -0.0022 297 LEU C CD1 
8552  C CD2 . LEU C 288 ? 0.3018 0.2667 0.3153 -0.0618 0.0127  -0.0075 297 LEU C CD2 
8553  N N   . ALA C 289 ? 0.3170 0.2521 0.2761 -0.0560 -0.0277 -0.0072 298 ALA C N   
8554  C CA  . ALA C 289 ? 0.3044 0.2452 0.2589 -0.0506 -0.0262 -0.0144 298 ALA C CA  
8555  C C   . ALA C 289 ? 0.2834 0.2452 0.2553 -0.0589 -0.0187 -0.0173 298 ALA C C   
8556  O O   . ALA C 289 ? 0.2860 0.2519 0.2634 -0.0675 -0.0227 -0.0123 298 ALA C O   
8557  C CB  . ALA C 289 ? 0.3275 0.2492 0.2589 -0.0467 -0.0424 -0.0130 298 ALA C CB  
8558  N N   . TYR C 290 ? 0.2656 0.2424 0.2452 -0.0563 -0.0086 -0.0247 299 TYR C N   
8559  C CA  . TYR C 290 ? 0.2403 0.2371 0.2351 -0.0634 -0.0012 -0.0293 299 TYR C CA  
8560  C C   . TYR C 290 ? 0.2354 0.2437 0.2279 -0.0593 0.0017  -0.0360 299 TYR C C   
8561  O O   . TYR C 290 ? 0.2482 0.2534 0.2303 -0.0501 0.0011  -0.0373 299 TYR C O   
8562  C CB  . TYR C 290 ? 0.2280 0.2333 0.2399 -0.0677 0.0111  -0.0314 299 TYR C CB  
8563  C CG  . TYR C 290 ? 0.2315 0.2346 0.2444 -0.0632 0.0185  -0.0330 299 TYR C CG  
8564  C CD1 . TYR C 290 ? 0.2277 0.2444 0.2481 -0.0649 0.0270  -0.0387 299 TYR C CD1 
8565  C CD2 . TYR C 290 ? 0.2384 0.2275 0.2446 -0.0583 0.0164  -0.0277 299 TYR C CD2 
8566  C CE1 . TYR C 290 ? 0.2277 0.2457 0.2496 -0.0628 0.0333  -0.0380 299 TYR C CE1 
8567  C CE2 . TYR C 290 ? 0.2386 0.2286 0.2462 -0.0545 0.0234  -0.0278 299 TYR C CE2 
8568  C CZ  . TYR C 290 ? 0.2302 0.2356 0.2459 -0.0573 0.0318  -0.0324 299 TYR C CZ  
8569  O OH  . TYR C 290 ? 0.2185 0.2282 0.2362 -0.0556 0.0380  -0.0303 299 TYR C OH  
8570  N N   . VAL C 291 ? 0.2207 0.2453 0.2226 -0.0653 0.0049  -0.0400 300 VAL C N   
8571  C CA  . VAL C 291 ? 0.2140 0.2528 0.2146 -0.0624 0.0074  -0.0457 300 VAL C CA  
8572  C C   . VAL C 291 ? 0.2045 0.2611 0.2213 -0.0685 0.0197  -0.0516 300 VAL C C   
8573  O O   . VAL C 291 ? 0.2010 0.2630 0.2295 -0.0762 0.0241  -0.0539 300 VAL C O   
8574  C CB  . VAL C 291 ? 0.2107 0.2541 0.2071 -0.0646 0.0001  -0.0458 300 VAL C CB  
8575  C CG1 . VAL C 291 ? 0.2063 0.2699 0.2067 -0.0638 0.0055  -0.0523 300 VAL C CG1 
8576  C CG2 . VAL C 291 ? 0.2405 0.2640 0.2157 -0.0571 -0.0137 -0.0411 300 VAL C CG2 
8577  N N   . VAL C 292 ? 0.2053 0.2713 0.2212 -0.0646 0.0244  -0.0537 301 VAL C N   
8578  C CA  . VAL C 292 ? 0.1978 0.2801 0.2266 -0.0721 0.0338  -0.0581 301 VAL C CA  
8579  C C   . VAL C 292 ? 0.2001 0.3020 0.2295 -0.0733 0.0333  -0.0627 301 VAL C C   
8580  O O   . VAL C 292 ? 0.2125 0.3173 0.2300 -0.0644 0.0272  -0.0618 301 VAL C O   
8581  C CB  . VAL C 292 ? 0.1970 0.2839 0.2249 -0.0689 0.0382  -0.0555 301 VAL C CB  
8582  C CG1 . VAL C 292 ? 0.2107 0.3209 0.2457 -0.0744 0.0438  -0.0584 301 VAL C CG1 
8583  C CG2 . VAL C 292 ? 0.2040 0.2778 0.2388 -0.0739 0.0426  -0.0531 301 VAL C CG2 
8584  N N   . GLN C 293 ? 0.1920 0.3058 0.2336 -0.0836 0.0391  -0.0681 302 GLN C N   
8585  C CA  . GLN C 293 ? 0.1797 0.3128 0.2235 -0.0864 0.0389  -0.0729 302 GLN C CA  
8586  C C   . GLN C 293 ? 0.1712 0.3214 0.2244 -0.0956 0.0457  -0.0769 302 GLN C C   
8587  O O   . GLN C 293 ? 0.1698 0.3146 0.2312 -0.1052 0.0496  -0.0807 302 GLN C O   
8588  C CB  . GLN C 293 ? 0.1768 0.3066 0.2245 -0.0908 0.0369  -0.0756 302 GLN C CB  
8589  C CG  . GLN C 293 ? 0.1995 0.3484 0.2516 -0.0955 0.0379  -0.0812 302 GLN C CG  
8590  C CD  . GLN C 293 ? 0.2363 0.3852 0.2891 -0.0966 0.0340  -0.0815 302 GLN C CD  
8591  O OE1 . GLN C 293 ? 0.2426 0.3793 0.2894 -0.0926 0.0277  -0.0751 302 GLN C OE1 
8592  N NE2 . GLN C 293 ? 0.2466 0.4108 0.3063 -0.1025 0.0369  -0.0882 302 GLN C NE2 
8593  N N   . LEU C 294 ? 0.1645 0.3351 0.2148 -0.0923 0.0463  -0.0755 303 LEU C N   
8594  C CA  . LEU C 294 ? 0.1587 0.3494 0.2169 -0.1017 0.0516  -0.0759 303 LEU C CA  
8595  C C   . LEU C 294 ? 0.1564 0.3703 0.2180 -0.1066 0.0516  -0.0809 303 LEU C C   
8596  O O   . LEU C 294 ? 0.1592 0.3780 0.2144 -0.0981 0.0474  -0.0820 303 LEU C O   
8597  C CB  . LEU C 294 ? 0.1611 0.3652 0.2136 -0.0930 0.0524  -0.0690 303 LEU C CB  
8598  C CG  . LEU C 294 ? 0.1606 0.3441 0.2085 -0.0869 0.0523  -0.0637 303 LEU C CG  
8599  C CD1 . LEU C 294 ? 0.1588 0.3618 0.2036 -0.0811 0.0547  -0.0569 303 LEU C CD1 
8600  C CD2 . LEU C 294 ? 0.1731 0.3384 0.2305 -0.0998 0.0557  -0.0648 303 LEU C CD2 
8601  N N   . PRO C 295 ? 0.1575 0.3846 0.2281 -0.1209 0.0552  -0.0834 304 PRO C N   
8602  C CA  . PRO C 295 ? 0.1561 0.4065 0.2303 -0.1272 0.0549  -0.0884 304 PRO C CA  
8603  C C   . PRO C 295 ? 0.1571 0.4400 0.2287 -0.1210 0.0551  -0.0836 304 PRO C C   
8604  O O   . PRO C 295 ? 0.1619 0.4530 0.2317 -0.1168 0.0568  -0.0764 304 PRO C O   
8605  C CB  . PRO C 295 ? 0.1611 0.4098 0.2434 -0.1456 0.0571  -0.0918 304 PRO C CB  
8606  C CG  . PRO C 295 ? 0.1722 0.4067 0.2553 -0.1485 0.0590  -0.0859 304 PRO C CG  
8607  C CD  . PRO C 295 ? 0.1636 0.3791 0.2404 -0.1335 0.0582  -0.0823 304 PRO C CD  
8608  N N   . LEU C 296 ? 0.1560 0.4587 0.2267 -0.1188 0.0534  -0.0871 305 LEU C N   
8609  C CA  . LEU C 296 ? 0.1531 0.4930 0.2221 -0.1135 0.0539  -0.0832 305 LEU C CA  
8610  C C   . LEU C 296 ? 0.1550 0.5188 0.2323 -0.1277 0.0547  -0.0880 305 LEU C C   
8611  O O   . LEU C 296 ? 0.1512 0.5082 0.2288 -0.1294 0.0526  -0.0950 305 LEU C O   
8612  C CB  . LEU C 296 ? 0.1467 0.4880 0.2024 -0.0929 0.0495  -0.0821 305 LEU C CB  
8613  C CG  . LEU C 296 ? 0.1530 0.4696 0.1960 -0.0768 0.0462  -0.0782 305 LEU C CG  
8614  C CD1 . LEU C 296 ? 0.1591 0.4761 0.1868 -0.0586 0.0398  -0.0780 305 LEU C CD1 
8615  C CD2 . LEU C 296 ? 0.1781 0.5064 0.2204 -0.0731 0.0497  -0.0714 305 LEU C CD2 
8616  N N   . TYR C 297 ? 0.1600 0.5538 0.2437 -0.1381 0.0571  -0.0833 306 TYR C N   
8617  C CA  . TYR C 297 ? 0.1593 0.5804 0.2500 -0.1524 0.0570  -0.0861 306 TYR C CA  
8618  C C   . TYR C 297 ? 0.1540 0.6147 0.2412 -0.1402 0.0567  -0.0832 306 TYR C C   
8619  O O   . TYR C 297 ? 0.1485 0.6310 0.2307 -0.1264 0.0579  -0.0755 306 TYR C O   
8620  C CB  . TYR C 297 ? 0.1710 0.6038 0.2700 -0.1726 0.0583  -0.0807 306 TYR C CB  
8621  C CG  . TYR C 297 ? 0.1865 0.5810 0.2861 -0.1800 0.0584  -0.0812 306 TYR C CG  
8622  C CD1 . TYR C 297 ? 0.2017 0.5951 0.3009 -0.1771 0.0605  -0.0716 306 TYR C CD1 
8623  C CD2 . TYR C 297 ? 0.2163 0.5761 0.3155 -0.1877 0.0564  -0.0913 306 TYR C CD2 
8624  C CE1 . TYR C 297 ? 0.2198 0.5765 0.3191 -0.1832 0.0605  -0.0717 306 TYR C CE1 
8625  C CE2 . TYR C 297 ? 0.2422 0.5650 0.3405 -0.1923 0.0564  -0.0920 306 TYR C CE2 
8626  C CZ  . TYR C 297 ? 0.2333 0.5537 0.3320 -0.1906 0.0584  -0.0821 306 TYR C CZ  
8627  O OH  . TYR C 297 ? 0.2137 0.4972 0.3111 -0.1948 0.0582  -0.0826 306 TYR C OH  
8628  N N   . GLY C 298 ? 0.1543 0.6249 0.2432 -0.1441 0.0550  -0.0898 307 GLY C N   
8629  C CA  . GLY C 298 ? 0.1455 0.6543 0.2316 -0.1342 0.0546  -0.0873 307 GLY C CA  
8630  C C   . GLY C 298 ? 0.1479 0.6961 0.2439 -0.1521 0.0557  -0.0851 307 GLY C C   
8631  O O   . GLY C 298 ? 0.1476 0.7282 0.2428 -0.1468 0.0552  -0.0846 307 GLY C O   
8632  N N   . VAL C 299 ? 0.1579 0.7014 0.2621 -0.1742 0.0560  -0.0837 308 VAL C N   
8633  C CA  . VAL C 299 ? 0.1699 0.7526 0.2830 -0.1947 0.0555  -0.0779 308 VAL C CA  
8634  C C   . VAL C 299 ? 0.1902 0.7616 0.3088 -0.2152 0.0549  -0.0724 308 VAL C C   
8635  O O   . VAL C 299 ? 0.2026 0.7293 0.3197 -0.2221 0.0534  -0.0785 308 VAL C O   
8636  C CB  . VAL C 299 ? 0.1644 0.7523 0.2813 -0.2111 0.0522  -0.0867 308 VAL C CB  
8637  C CG1 . VAL C 299 ? 0.1571 0.7833 0.2729 -0.1997 0.0527  -0.0861 308 VAL C CG1 
8638  C CG2 . VAL C 299 ? 0.1669 0.7072 0.2800 -0.2123 0.0503  -0.0995 308 VAL C CG2 
8639  N N   . ILE C 300 ? 0.2010 0.8145 0.3257 -0.2258 0.0553  -0.0600 309 ILE C N   
8640  C CA  . ILE C 300 ? 0.2251 0.8309 0.3549 -0.2475 0.0536  -0.0521 309 ILE C CA  
8641  C C   . ILE C 300 ? 0.2426 0.8866 0.3802 -0.2740 0.0494  -0.0457 309 ILE C C   
8642  O O   . ILE C 300 ? 0.2422 0.9315 0.3824 -0.2707 0.0499  -0.0433 309 ILE C O   
8643  C CB  . ILE C 300 ? 0.2238 0.8497 0.3533 -0.2338 0.0581  -0.0386 309 ILE C CB  
8644  C CG1 . ILE C 300 ? 0.2286 0.8176 0.3486 -0.2071 0.0610  -0.0449 309 ILE C CG1 
8645  C CG2 . ILE C 300 ? 0.2340 0.8534 0.3689 -0.2555 0.0564  -0.0283 309 ILE C CG2 
8646  C CD1 . ILE C 300 ? 0.2580 0.7866 0.3758 -0.2144 0.0588  -0.0556 309 ILE C CD1 
8647  N N   . ASP C 301 ? 0.2671 0.8929 0.4075 -0.3012 0.0442  -0.0422 310 ASP C N   
8648  C CA  . ASP C 301 ? 0.2835 0.9507 0.4313 -0.3292 0.0390  -0.0305 310 ASP C CA  
8649  C C   . ASP C 301 ? 0.2891 0.9708 0.4375 -0.3427 0.0338  -0.0386 310 ASP C C   
8650  O O   . ASP C 301 ? 0.3015 1.0288 0.4563 -0.3616 0.0301  -0.0281 310 ASP C O   
8651  C CB  . ASP C 301 ? 0.2725 1.0057 0.4272 -0.3210 0.0440  -0.0116 310 ASP C CB  
8652  C CG  . ASP C 301 ? 0.2794 1.0036 0.4336 -0.3116 0.0482  -0.0014 310 ASP C CG  
8653  O OD1 . ASP C 301 ? 0.2658 1.0282 0.4198 -0.2880 0.0547  0.0073  310 ASP C OD1 
8654  O OD2 . ASP C 301 ? 0.2989 0.9776 0.4516 -0.3266 0.0446  -0.0022 310 ASP C OD2 
8655  N N   . THR C 302 ? 0.2870 0.9331 0.4288 -0.3334 0.0332  -0.0562 311 THR C N   
8656  C CA  . THR C 302 ? 0.3009 0.9500 0.4413 -0.3488 0.0270  -0.0657 311 THR C CA  
8657  C C   . THR C 302 ? 0.3382 0.9437 0.4734 -0.3775 0.0172  -0.0699 311 THR C C   
8658  O O   . THR C 302 ? 0.3561 0.9155 0.4865 -0.3758 0.0172  -0.0719 311 THR C O   
8659  C CB  . THR C 302 ? 0.2885 0.9061 0.4220 -0.3289 0.0293  -0.0832 311 THR C CB  
8660  O OG1 . THR C 302 ? 0.2712 0.8970 0.4045 -0.2985 0.0375  -0.0810 311 THR C OG1 
8661  C CG2 . THR C 302 ? 0.3130 0.9576 0.4472 -0.3331 0.0267  -0.0895 311 THR C CG2 
8662  N N   . PRO C 303 ? 0.3597 0.9759 0.4939 -0.4034 0.0081  -0.0719 312 PRO C N   
8663  C CA  . PRO C 303 ? 0.3993 0.9619 0.5231 -0.4287 -0.0033 -0.0790 312 PRO C CA  
8664  C C   . PRO C 303 ? 0.4114 0.9123 0.5222 -0.4145 -0.0040 -0.1012 312 PRO C C   
8665  O O   . PRO C 303 ? 0.3929 0.9017 0.5032 -0.3952 0.0008  -0.1122 312 PRO C O   
8666  C CB  . PRO C 303 ? 0.4132 1.0069 0.5378 -0.4573 -0.0134 -0.0759 312 PRO C CB  
8667  C CG  . PRO C 303 ? 0.3776 1.0243 0.5097 -0.4389 -0.0060 -0.0774 312 PRO C CG  
8668  C CD  . PRO C 303 ? 0.3487 1.0221 0.4889 -0.4109 0.0065  -0.0680 312 PRO C CD  
8669  N N   . CYS C 304 ? 0.4409 0.8834 0.5409 -0.4225 -0.0098 -0.1065 313 CYS C N   
8670  C CA  . CYS C 304 ? 0.4617 0.8498 0.5473 -0.4133 -0.0129 -0.1270 313 CYS C CA  
8671  C C   . CYS C 304 ? 0.5046 0.8499 0.5752 -0.4406 -0.0277 -0.1323 313 CYS C C   
8672  O O   . CYS C 304 ? 0.5244 0.8744 0.5964 -0.4661 -0.0351 -0.1186 313 CYS C O   
8673  C CB  . CYS C 304 ? 0.4600 0.8079 0.5422 -0.3900 -0.0059 -0.1317 313 CYS C CB  
8674  S SG  . CYS C 304 ? 0.4506 0.8286 0.5463 -0.3601 0.0092  -0.1214 313 CYS C SG  
8675  N N   . TRP C 305 ? 0.5238 0.8254 0.5786 -0.4341 -0.0326 -0.1521 314 TRP C N   
8676  C CA  . TRP C 305 ? 0.5760 0.8246 0.6104 -0.4553 -0.0482 -0.1613 314 TRP C CA  
8677  C C   . TRP C 305 ? 0.5899 0.7795 0.6056 -0.4349 -0.0492 -0.1819 314 TRP C C   
8678  O O   . TRP C 305 ? 0.5673 0.7674 0.5854 -0.4094 -0.0402 -0.1923 314 TRP C O   
8679  C CB  . TRP C 305 ? 0.5972 0.8681 0.6275 -0.4782 -0.0589 -0.1642 314 TRP C CB  
8680  C CG  . TRP C 305 ? 0.5845 0.8852 0.6177 -0.4612 -0.0531 -0.1763 314 TRP C CG  
8681  C CD1 . TRP C 305 ? 0.6215 0.8927 0.6380 -0.4543 -0.0586 -0.1968 314 TRP C CD1 
8682  C CD2 . TRP C 305 ? 0.5513 0.9175 0.6039 -0.4495 -0.0417 -0.1682 314 TRP C CD2 
8683  N NE1 . TRP C 305 ? 0.5966 0.9122 0.6222 -0.4401 -0.0510 -0.2012 314 TRP C NE1 
8684  C CE2 . TRP C 305 ? 0.5500 0.9225 0.5973 -0.4370 -0.0409 -0.1839 314 TRP C CE2 
8685  C CE3 . TRP C 305 ? 0.5337 0.9532 0.6057 -0.4467 -0.0326 -0.1494 314 TRP C CE3 
8686  C CZ2 . TRP C 305 ? 0.5226 0.9499 0.5837 -0.4232 -0.0316 -0.1808 314 TRP C CZ2 
8687  C CZ3 . TRP C 305 ? 0.5148 0.9870 0.5988 -0.4314 -0.0237 -0.1474 314 TRP C CZ3 
8688  C CH2 . TRP C 305 ? 0.5092 0.9841 0.5879 -0.4204 -0.0235 -0.1628 314 TRP C CH2 
8689  N N   . LYS C 306 ? 0.6287 0.7580 0.6252 -0.4456 -0.0605 -0.1869 315 LYS C N   
8690  C CA  . LYS C 306 ? 0.6485 0.7226 0.6247 -0.4250 -0.0623 -0.2066 315 LYS C CA  
8691  C C   . LYS C 306 ? 0.6986 0.7392 0.6504 -0.4374 -0.0780 -0.2235 315 LYS C C   
8692  O O   . LYS C 306 ? 0.7424 0.7628 0.6831 -0.4677 -0.0934 -0.2193 315 LYS C O   
8693  C CB  . LYS C 306 ? 0.6673 0.6910 0.6348 -0.4208 -0.0637 -0.2034 315 LYS C CB  
8694  C CG  . LYS C 306 ? 0.6745 0.6574 0.6274 -0.3901 -0.0597 -0.2208 315 LYS C CG  
8695  C CD  . LYS C 306 ? 0.7104 0.6452 0.6545 -0.3848 -0.0608 -0.2172 315 LYS C CD  
8696  C CE  . LYS C 306 ? 0.7116 0.6261 0.6487 -0.3504 -0.0525 -0.2302 315 LYS C CE  
8697  N NZ  . LYS C 306 ? 0.7741 0.6271 0.6918 -0.3457 -0.0589 -0.2336 315 LYS C NZ  
8698  N N   . LEU C 307 ? 0.6972 0.7315 0.6396 -0.4140 -0.0748 -0.2421 316 LEU C N   
8699  C CA  . LEU C 307 ? 0.7462 0.7494 0.6631 -0.4192 -0.0886 -0.2614 316 LEU C CA  
8700  C C   . LEU C 307 ? 0.7992 0.7316 0.6868 -0.4026 -0.0957 -0.2785 316 LEU C C   
8701  O O   . LEU C 307 ? 0.7880 0.7143 0.6773 -0.3728 -0.0846 -0.2835 316 LEU C O   
8702  C CB  . LEU C 307 ? 0.7090 0.7578 0.6341 -0.4032 -0.0806 -0.2705 316 LEU C CB  
8703  C CG  . LEU C 307 ? 0.7424 0.7680 0.6425 -0.4018 -0.0920 -0.2920 316 LEU C CG  
8704  C CD1 . LEU C 307 ? 0.7871 0.7972 0.6735 -0.4380 -0.1110 -0.2911 316 LEU C CD1 
8705  C CD2 . LEU C 307 ? 0.7007 0.7803 0.6142 -0.3846 -0.0812 -0.2968 316 LEU C CD2 
8706  N N   . HIS C 308 ? 0.8674 0.7455 0.7269 -0.4217 -0.1151 -0.2868 317 HIS C N   
8707  C CA  . HIS C 308 ? 0.9230 0.7331 0.7501 -0.4030 -0.1232 -0.3056 317 HIS C CA  
8708  C C   . HIS C 308 ? 0.9582 0.7504 0.7598 -0.4066 -0.1370 -0.3253 317 HIS C C   
8709  O O   . HIS C 308 ? 0.9589 0.7817 0.7667 -0.4310 -0.1433 -0.3215 317 HIS C O   
8710  C CB  . HIS C 308 ? 0.9812 0.7292 0.7905 -0.4192 -0.1363 -0.2998 317 HIS C CB  
8711  C CG  . HIS C 308 ? 0.9774 0.7492 0.8134 -0.4286 -0.1265 -0.2758 317 HIS C CG  
8712  N ND1 . HIS C 308 ? 0.9895 0.7483 0.8312 -0.4050 -0.1151 -0.2721 317 HIS C ND1 
8713  C CD2 . HIS C 308 ? 0.9768 0.7852 0.8339 -0.4588 -0.1272 -0.2540 317 HIS C CD2 
8714  C CE1 . HIS C 308 ? 0.9751 0.7598 0.8397 -0.4200 -0.1091 -0.2499 317 HIS C CE1 
8715  N NE2 . HIS C 308 ? 0.9648 0.7810 0.8392 -0.4519 -0.1160 -0.2384 317 HIS C NE2 
8716  N N   . THR C 309 ? 0.9921 0.7347 0.7634 -0.3818 -0.1424 -0.3465 318 THR C N   
8717  C CA  . THR C 309 ? 1.0101 0.7491 0.7606 -0.3729 -0.1497 -0.3673 318 THR C CA  
8718  C C   . THR C 309 ? 1.0850 0.7443 0.7901 -0.3582 -0.1657 -0.3892 318 THR C C   
8719  O O   . THR C 309 ? 1.0932 0.7223 0.7897 -0.3331 -0.1604 -0.3926 318 THR C O   
8720  C CB  . THR C 309 ? 0.9441 0.7437 0.7171 -0.3424 -0.1291 -0.3696 318 THR C CB  
8721  O OG1 . THR C 309 ? 0.9133 0.7713 0.7056 -0.3583 -0.1264 -0.3645 318 THR C OG1 
8722  C CG2 . THR C 309 ? 0.9716 0.7463 0.7182 -0.3081 -0.1297 -0.3926 318 THR C CG2 
8723  N N   . SER C 310 ? 1.1460 0.7693 0.8201 -0.3733 -0.1860 -0.4039 319 SER C N   
8724  C CA  . SER C 310 ? 1.2266 0.7712 0.8529 -0.3556 -0.2023 -0.4270 319 SER C CA  
8725  C C   . SER C 310 ? 1.2663 0.8077 0.8673 -0.3487 -0.2125 -0.4493 319 SER C C   
8726  O O   . SER C 310 ? 1.2537 0.8377 0.8693 -0.3723 -0.2145 -0.4446 319 SER C O   
8727  C CB  . SER C 310 ? 1.2923 0.7644 0.8931 -0.3853 -0.2247 -0.4225 319 SER C CB  
8728  O OG  . SER C 310 ? 1.3640 0.7556 0.9160 -0.3637 -0.2403 -0.4452 319 SER C OG  
8729  N N   . PRO C 311 ? 1.3214 0.8141 0.8836 -0.3151 -0.2191 -0.4737 320 PRO C N   
8730  C CA  . PRO C 311 ? 1.3641 0.8493 0.8970 -0.3032 -0.2294 -0.4976 320 PRO C CA  
8731  C C   . PRO C 311 ? 1.4307 0.8835 0.9405 -0.3420 -0.2547 -0.5026 320 PRO C C   
8732  O O   . PRO C 311 ? 1.4711 0.8739 0.9683 -0.3740 -0.2721 -0.4942 320 PRO C O   
8733  C CB  . PRO C 311 ? 1.4183 0.8392 0.9077 -0.2632 -0.2359 -0.5201 320 PRO C CB  
8734  C CG  . PRO C 311 ? 1.4282 0.8056 0.9172 -0.2659 -0.2365 -0.5080 320 PRO C CG  
8735  C CD  . PRO C 311 ? 1.3432 0.7898 0.8871 -0.2825 -0.2159 -0.4801 320 PRO C CD  
8736  N N   . LEU C 312 ? 1.4466 0.9288 0.9503 -0.3391 -0.2572 -0.5160 321 LEU C N   
8737  C CA  . LEU C 312 ? 1.5084 0.9773 0.9969 -0.3765 -0.2786 -0.5190 321 LEU C CA  
8738  C C   . LEU C 312 ? 1.5799 1.0261 1.0279 -0.3548 -0.2907 -0.5489 321 LEU C C   
8739  O O   . LEU C 312 ? 1.5376 1.0404 0.9994 -0.3272 -0.2743 -0.5561 321 LEU C O   
8740  C CB  . LEU C 312 ? 1.4238 0.9818 0.9623 -0.4030 -0.2645 -0.4967 321 LEU C CB  
8741  C CG  . LEU C 312 ? 1.4455 1.0058 0.9879 -0.4553 -0.2821 -0.4834 321 LEU C CG  
8742  C CD1 . LEU C 312 ? 1.3658 1.0195 0.9471 -0.4632 -0.2670 -0.4731 321 LEU C CD1 
8743  C CD2 . LEU C 312 ? 1.5487 1.0306 1.0375 -0.4756 -0.3158 -0.5027 321 LEU C CD2 
8744  N N   . CYS C 313 ? 1.7059 1.0691 1.1028 -0.3672 -0.3201 -0.5661 322 CYS C N   
8745  C CA  . CYS C 313 ? 1.7920 1.1298 1.1467 -0.3470 -0.3337 -0.5955 322 CYS C CA  
8746  C C   . CYS C 313 ? 1.8307 1.1718 1.1766 -0.3878 -0.3536 -0.5970 322 CYS C C   
8747  O O   . CYS C 313 ? 1.8643 1.2036 1.1836 -0.3751 -0.3623 -0.6189 322 CYS C O   
8748  C CB  . CYS C 313 ? 1.8894 1.1274 1.1837 -0.3189 -0.3526 -0.6202 322 CYS C CB  
8749  S SG  . CYS C 313 ? 1.9118 1.1628 1.2083 -0.2536 -0.3273 -0.6286 322 CYS C SG  
8750  N N   . THR C 314 ? 1.8386 1.1845 1.2054 -0.4368 -0.3615 -0.5734 323 THR C N   
8751  C CA  . THR C 314 ? 1.8599 1.2308 1.2313 -0.4805 -0.3762 -0.5675 323 THR C CA  
8752  C C   . THR C 314 ? 1.7624 1.2480 1.1910 -0.4800 -0.3486 -0.5511 323 THR C C   
8753  O O   . THR C 314 ? 1.6909 1.2307 1.1663 -0.4918 -0.3299 -0.5246 323 THR C O   
8754  C CB  . THR C 314 ? 1.9143 1.2372 1.2765 -0.5371 -0.4020 -0.5497 323 THR C CB  
8755  O OG1 . THR C 314 ? 1.8986 1.1988 1.2745 -0.5386 -0.3951 -0.5321 323 THR C OG1 
8756  C CG2 . THR C 314 ? 2.0181 1.2413 1.3141 -0.5527 -0.4408 -0.5728 323 THR C CG2 
8757  N N   . THR C 315 ? 1.7579 1.2773 1.1796 -0.4632 -0.3463 -0.5680 324 THR C N   
8758  C CA  . THR C 315 ? 1.6677 1.2904 1.1367 -0.4571 -0.3216 -0.5565 324 THR C CA  
8759  C C   . THR C 315 ? 1.6833 1.3303 1.1350 -0.4446 -0.3261 -0.5774 324 THR C C   
8760  O O   . THR C 315 ? 1.7611 1.3438 1.1622 -0.4337 -0.3467 -0.6035 324 THR C O   
8761  C CB  . THR C 315 ? 1.5898 1.2589 1.0945 -0.4196 -0.2901 -0.5468 324 THR C CB  
8762  O OG1 . THR C 315 ? 1.6101 1.2126 1.0936 -0.4006 -0.2924 -0.5516 324 THR C OG1 
8763  C CG2 . THR C 315 ? 1.5070 1.2499 1.0670 -0.4425 -0.2719 -0.5156 324 THR C CG2 
8764  N N   . ASN C 316 ? 1.6136 1.3515 1.1060 -0.4470 -0.3080 -0.5654 325 ASN C N   
8765  C CA  . ASN C 316 ? 1.6095 1.3881 1.0953 -0.4309 -0.3061 -0.5815 325 ASN C CA  
8766  C C   . ASN C 316 ? 1.5197 1.4026 1.0578 -0.4358 -0.2835 -0.5619 325 ASN C C   
8767  O O   . ASN C 316 ? 1.4830 1.4031 1.0545 -0.4679 -0.2796 -0.5373 325 ASN C O   
8768  C CB  . ASN C 316 ? 1.6905 1.4232 1.1340 -0.4577 -0.3370 -0.5984 325 ASN C CB  
8769  C CG  . ASN C 316 ? 1.6650 1.4617 1.1360 -0.4977 -0.3396 -0.5823 325 ASN C CG  
8770  O OD1 . ASN C 316 ? 1.6566 1.4670 1.1511 -0.5360 -0.3427 -0.5587 325 ASN C OD1 
8771  N ND2 . ASN C 316 ? 1.6561 1.4956 1.1245 -0.4877 -0.3381 -0.5944 325 ASN C ND2 
8772  N N   . THR C 317 ? 1.4890 1.4185 1.0322 -0.4037 -0.2697 -0.5724 326 THR C N   
8773  C CA  . THR C 317 ? 1.4222 1.4437 1.0057 -0.4093 -0.2536 -0.5579 326 THR C CA  
8774  C C   . THR C 317 ? 1.4538 1.4891 1.0145 -0.4059 -0.2641 -0.5773 326 THR C C   
8775  O O   . THR C 317 ? 1.4836 1.5004 1.0166 -0.3709 -0.2643 -0.5996 326 THR C O   
8776  C CB  . THR C 317 ? 1.3452 1.4251 0.9629 -0.3729 -0.2241 -0.5486 326 THR C CB  
8777  O OG1 . THR C 317 ? 1.3273 1.3870 0.9599 -0.3670 -0.2140 -0.5352 326 THR C OG1 
8778  C CG2 . THR C 317 ? 1.2747 1.4454 0.9356 -0.3831 -0.2085 -0.5294 326 THR C CG2 
8779  N N   . LYS C 318 ? 1.4500 1.5201 1.0214 -0.4411 -0.2729 -0.5687 327 LYS C N   
8780  C CA  . LYS C 318 ? 1.4424 1.5591 1.0106 -0.4358 -0.2736 -0.5792 327 LYS C CA  
8781  C C   . LYS C 318 ? 1.4919 1.5647 1.0137 -0.4014 -0.2828 -0.6113 327 LYS C C   
8782  O O   . LYS C 318 ? 1.4595 1.5699 0.9884 -0.3632 -0.2655 -0.6177 327 LYS C O   
8783  C CB  . LYS C 318 ? 1.3528 1.5616 0.9700 -0.4189 -0.2448 -0.5607 327 LYS C CB  
8784  C CG  . LYS C 318 ? 1.3415 1.6197 0.9740 -0.4295 -0.2429 -0.5574 327 LYS C CG  
8785  C CD  . LYS C 318 ? 1.2841 1.6421 0.9596 -0.4062 -0.2148 -0.5409 327 LYS C CD  
8786  C CE  . LYS C 318 ? 1.2919 1.7115 0.9727 -0.4029 -0.2125 -0.5451 327 LYS C CE  
8787  N NZ  . LYS C 318 ? 1.2424 1.7220 0.9494 -0.3686 -0.1884 -0.5382 327 LYS C NZ  
8788  N N   . GLU C 319 ? 1.5697 1.5619 1.0429 -0.4147 -0.3107 -0.6306 328 GLU C N   
8789  C CA  . GLU C 319 ? 1.6280 1.5670 1.0488 -0.3837 -0.3242 -0.6633 328 GLU C CA  
8790  C C   . GLU C 319 ? 1.6223 1.5294 1.0307 -0.3383 -0.3124 -0.6730 328 GLU C C   
8791  O O   . GLU C 319 ? 1.6228 1.5409 1.0146 -0.2975 -0.3055 -0.6907 328 GLU C O   
8792  C CB  . GLU C 319 ? 1.6144 1.6103 1.0338 -0.3697 -0.3207 -0.6749 328 GLU C CB  
8793  C CG  . GLU C 319 ? 1.6532 1.6490 1.0582 -0.4095 -0.3434 -0.6786 328 GLU C CG  
8794  C CD  . GLU C 319 ? 1.7088 1.7009 1.0755 -0.3884 -0.3546 -0.7068 328 GLU C CD  
8795  O OE1 . GLU C 319 ? 1.7644 1.7412 1.1082 -0.4183 -0.3776 -0.7152 328 GLU C OE1 
8796  O OE2 . GLU C 319 ? 1.7021 1.7079 1.0608 -0.3420 -0.3409 -0.7203 328 GLU C OE2 
8797  N N   . GLY C 320 ? 1.6144 1.4840 1.0308 -0.3455 -0.3105 -0.6606 329 GLY C N   
8798  C CA  . GLY C 320 ? 1.5975 1.4516 1.0134 -0.3051 -0.2951 -0.6632 329 GLY C CA  
8799  C C   . GLY C 320 ? 1.6586 1.4209 1.0439 -0.3122 -0.3116 -0.6678 329 GLY C C   
8800  O O   . GLY C 320 ? 1.6242 1.3827 1.0311 -0.3062 -0.2984 -0.6528 329 GLY C O   
8801  N N   . SER C 321 ? 1.7477 1.4353 1.0818 -0.3267 -0.3418 -0.6882 330 SER C N   
8802  C CA  . SER C 321 ? 1.8286 1.4122 1.1177 -0.3293 -0.3639 -0.6996 330 SER C CA  
8803  C C   . SER C 321 ? 1.7960 1.3610 1.1061 -0.3248 -0.3513 -0.6819 330 SER C C   
8804  O O   . SER C 321 ? 1.7461 1.3391 1.0959 -0.3583 -0.3443 -0.6550 330 SER C O   
8805  C CB  . SER C 321 ? 1.9115 1.4345 1.1388 -0.2885 -0.3789 -0.7354 330 SER C CB  
8806  O OG  . SER C 321 ? 2.0128 1.4467 1.1850 -0.3122 -0.4147 -0.7533 330 SER C OG  
8807  N N   . ASN C 322 ? 1.8217 1.3428 1.1045 -0.2821 -0.3483 -0.6972 331 ASN C N   
8808  C CA  . ASN C 322 ? 1.8126 1.2986 1.1026 -0.2741 -0.3411 -0.6857 331 ASN C CA  
8809  C C   . ASN C 322 ? 1.7006 1.2666 1.0529 -0.2667 -0.3080 -0.6585 331 ASN C C   
8810  O O   . ASN C 322 ? 1.6329 1.2624 1.0307 -0.2965 -0.2971 -0.6356 331 ASN C O   
8811  C CB  . ASN C 322 ? 1.8845 1.2995 1.1212 -0.2271 -0.3495 -0.7127 331 ASN C CB  
8812  C CG  . ASN C 322 ? 1.9209 1.2639 1.1440 -0.2279 -0.3559 -0.7069 331 ASN C CG  
8813  O OD1 . ASN C 322 ? 1.8532 1.2246 1.1190 -0.2423 -0.3400 -0.6813 331 ASN C OD1 
8814  N ND2 . ASN C 322 ? 2.0243 1.2723 1.1850 -0.2101 -0.3797 -0.7317 331 ASN C ND2 
8815  N N   . ILE C 323 ? 1.6826 1.2425 1.0330 -0.2256 -0.2936 -0.6618 332 ILE C N   
8816  C CA  . ILE C 323 ? 1.5940 1.2075 0.9931 -0.2141 -0.2658 -0.6385 332 ILE C CA  
8817  C C   . ILE C 323 ? 1.5848 1.1674 1.0012 -0.2415 -0.2668 -0.6175 332 ILE C C   
8818  O O   . ILE C 323 ? 1.5919 1.1613 1.0154 -0.2858 -0.2794 -0.6055 332 ILE C O   
8819  C CB  . ILE C 323 ? 1.4969 1.2173 0.9478 -0.2111 -0.2404 -0.6224 332 ILE C CB  
8820  C CG1 . ILE C 323 ? 1.4386 1.1993 0.9071 -0.1672 -0.2163 -0.6192 332 ILE C CG1 
8821  C CG2 . ILE C 323 ? 1.4270 1.1903 0.9252 -0.2527 -0.2328 -0.5936 332 ILE C CG2 
8822  C CD1 . ILE C 323 ? 1.4699 1.2243 0.9015 -0.1216 -0.2179 -0.6451 332 ILE C CD1 
8823  N N   . CYS C 324 ? 1.5695 1.1406 0.9902 -0.2133 -0.2541 -0.6137 333 CYS C N   
8824  C CA  . CYS C 324 ? 1.5594 1.1071 0.9983 -0.2319 -0.2515 -0.5938 333 CYS C CA  
8825  C C   . CYS C 324 ? 1.4512 1.0778 0.9453 -0.2241 -0.2223 -0.5703 333 CYS C C   
8826  O O   . CYS C 324 ? 1.4040 1.0811 0.9118 -0.1905 -0.2042 -0.5726 333 CYS C O   
8827  C CB  . CYS C 324 ? 1.6341 1.0954 1.0310 -0.2103 -0.2635 -0.6069 333 CYS C CB  
8828  S SG  . CYS C 324 ? 1.8135 1.1753 1.1374 -0.2158 -0.3008 -0.6380 333 CYS C SG  
8829  N N   . LEU C 325 ? 1.4107 1.0481 0.9355 -0.2577 -0.2194 -0.5468 334 LEU C N   
8830  C CA  . LEU C 325 ? 1.3065 1.0234 0.8848 -0.2635 -0.1962 -0.5228 334 LEU C CA  
8831  C C   . LEU C 325 ? 1.2863 0.9829 0.8798 -0.2701 -0.1906 -0.5056 334 LEU C C   
8832  O O   . LEU C 325 ? 1.3348 0.9752 0.9118 -0.2956 -0.2071 -0.5027 334 LEU C O   
8833  C CB  . LEU C 325 ? 1.2817 1.0385 0.8830 -0.3046 -0.2003 -0.5093 334 LEU C CB  
8834  C CG  . LEU C 325 ? 1.2825 1.0821 0.8820 -0.3037 -0.2017 -0.5202 334 LEU C CG  
8835  C CD1 . LEU C 325 ? 1.2228 1.0885 0.8618 -0.3363 -0.1952 -0.4990 334 LEU C CD1 
8836  C CD2 . LEU C 325 ? 1.2634 1.1017 0.8678 -0.2596 -0.1840 -0.5288 334 LEU C CD2 
8837  N N   . THR C 326 ? 1.2136 0.9568 0.8387 -0.2480 -0.1679 -0.4932 335 THR C N   
8838  C CA  . THR C 326 ? 1.1701 0.9168 0.8224 -0.2583 -0.1582 -0.4713 335 THR C CA  
8839  C C   . THR C 326 ? 1.0799 0.9096 0.7804 -0.2607 -0.1370 -0.4512 335 THR C C   
8840  O O   . THR C 326 ? 1.0381 0.9140 0.7507 -0.2352 -0.1231 -0.4536 335 THR C O   
8841  C CB  . THR C 326 ? 1.1846 0.8922 0.8226 -0.2275 -0.1538 -0.4760 335 THR C CB  
8842  O OG1 . THR C 326 ? 1.2669 0.9010 0.8546 -0.2162 -0.1733 -0.4994 335 THR C OG1 
8843  C CG2 . THR C 326 ? 1.1769 0.8658 0.8312 -0.2458 -0.1518 -0.4565 335 THR C CG2 
8844  N N   . ARG C 327 ? 1.0522 0.9002 0.7783 -0.2923 -0.1359 -0.4309 336 ARG C N   
8845  C CA  . ARG C 327 ? 0.9816 0.9041 0.7498 -0.2975 -0.1187 -0.4119 336 ARG C CA  
8846  C C   . ARG C 327 ? 0.9419 0.8793 0.7305 -0.2739 -0.1009 -0.4007 336 ARG C C   
8847  O O   . ARG C 327 ? 0.9538 0.8537 0.7392 -0.2758 -0.1022 -0.3944 336 ARG C O   
8848  C CB  . ARG C 327 ? 0.9713 0.9084 0.7567 -0.3375 -0.1245 -0.3942 336 ARG C CB  
8849  C CG  . ARG C 327 ? 0.9157 0.9302 0.7353 -0.3451 -0.1123 -0.3804 336 ARG C CG  
8850  C CD  . ARG C 327 ? 0.9309 0.9597 0.7524 -0.3821 -0.1247 -0.3744 336 ARG C CD  
8851  N NE  . ARG C 327 ? 0.9183 0.9524 0.7574 -0.4095 -0.1257 -0.3528 336 ARG C NE  
8852  C CZ  . ARG C 327 ? 0.8559 0.9455 0.7292 -0.4118 -0.1109 -0.3324 336 ARG C CZ  
8853  N NH1 . ARG C 327 ? 0.7967 0.9380 0.6909 -0.3891 -0.0943 -0.3297 336 ARG C NH1 
8854  N NH2 . ARG C 327 ? 0.8537 0.9456 0.7388 -0.4366 -0.1137 -0.3141 336 ARG C NH2 
8855  N N   . THR C 328 ? 0.9000 0.8918 0.7087 -0.2526 -0.0852 -0.3976 337 THR C N   
8856  C CA  . THR C 328 ? 0.8776 0.8824 0.7005 -0.2262 -0.0699 -0.3902 337 THR C CA  
8857  C C   . THR C 328 ? 0.8373 0.8608 0.6899 -0.2380 -0.0602 -0.3675 337 THR C C   
8858  O O   . THR C 328 ? 0.8396 0.8394 0.6932 -0.2281 -0.0559 -0.3619 337 THR C O   
8859  C CB  . THR C 328 ? 0.8394 0.8994 0.6752 -0.2032 -0.0575 -0.3914 337 THR C CB  
8860  O OG1 . THR C 328 ? 0.9053 0.9462 0.7114 -0.1830 -0.0643 -0.4130 337 THR C OG1 
8861  C CG2 . THR C 328 ? 0.8074 0.8890 0.6629 -0.1822 -0.0421 -0.3788 337 THR C CG2 
8862  N N   . ASP C 329 ? 0.8071 0.8751 0.6831 -0.2580 -0.0569 -0.3545 338 ASP C N   
8863  C CA  . ASP C 329 ? 0.7565 0.8598 0.6636 -0.2641 -0.0451 -0.3328 338 ASP C CA  
8864  C C   . ASP C 329 ? 0.7522 0.8257 0.6618 -0.2844 -0.0496 -0.3210 338 ASP C C   
8865  O O   . ASP C 329 ? 0.7391 0.8355 0.6626 -0.3083 -0.0514 -0.3086 338 ASP C O   
8866  C CB  . ASP C 329 ? 0.7364 0.8978 0.6634 -0.2770 -0.0416 -0.3247 338 ASP C CB  
8867  C CG  . ASP C 329 ? 0.8201 0.9764 0.7313 -0.2987 -0.0561 -0.3356 338 ASP C CG  
8868  O OD1 . ASP C 329 ? 0.8474 1.0472 0.7661 -0.2995 -0.0540 -0.3371 338 ASP C OD1 
8869  O OD2 . ASP C 329 ? 0.8897 0.9979 0.7800 -0.3158 -0.0703 -0.3421 338 ASP C OD2 
8870  N N   . ARG C 330 ? 0.7582 0.7839 0.6546 -0.2750 -0.0515 -0.3237 339 ARG C N   
8871  C CA  . ARG C 330 ? 0.7575 0.7541 0.6552 -0.2953 -0.0567 -0.3119 339 ARG C CA  
8872  C C   . ARG C 330 ? 0.6995 0.7242 0.6237 -0.2889 -0.0426 -0.2935 339 ARG C C   
8873  O O   . ARG C 330 ? 0.6644 0.7127 0.5993 -0.2654 -0.0308 -0.2924 339 ARG C O   
8874  C CB  . ARG C 330 ? 0.8110 0.7387 0.6807 -0.2898 -0.0666 -0.3221 339 ARG C CB  
8875  C CG  . ARG C 330 ? 0.8762 0.7643 0.7126 -0.2814 -0.0790 -0.3446 339 ARG C CG  
8876  C CD  . ARG C 330 ? 0.9162 0.7581 0.7335 -0.2555 -0.0785 -0.3531 339 ARG C CD  
8877  N NE  . ARG C 330 ? 0.9725 0.7691 0.7526 -0.2418 -0.0910 -0.3762 339 ARG C NE  
8878  C CZ  . ARG C 330 ? 1.0413 0.7705 0.7896 -0.2524 -0.1087 -0.3854 339 ARG C CZ  
8879  N NH1 . ARG C 330 ? 1.0709 0.7740 0.8229 -0.2790 -0.1155 -0.3715 339 ARG C NH1 
8880  N NH2 . ARG C 330 ? 1.0692 0.7566 0.7805 -0.2363 -0.1205 -0.4081 339 ARG C NH2 
8881  N N   . GLY C 331 ? 0.6918 0.7118 0.6248 -0.3102 -0.0450 -0.2787 340 GLY C N   
8882  C CA  . GLY C 331 ? 0.6407 0.6847 0.5967 -0.3056 -0.0331 -0.2608 340 GLY C CA  
8883  C C   . GLY C 331 ? 0.6082 0.6951 0.5846 -0.3277 -0.0315 -0.2436 340 GLY C C   
8884  O O   . GLY C 331 ? 0.6313 0.7212 0.6034 -0.3525 -0.0416 -0.2426 340 GLY C O   
8885  N N   . TRP C 332 ? 0.5580 0.6794 0.5554 -0.3178 -0.0192 -0.2299 341 TRP C N   
8886  C CA  . TRP C 332 ? 0.5307 0.6931 0.5465 -0.3334 -0.0164 -0.2124 341 TRP C CA  
8887  C C   . TRP C 332 ? 0.5012 0.7185 0.5298 -0.3309 -0.0114 -0.2106 341 TRP C C   
8888  O O   . TRP C 332 ? 0.4755 0.7127 0.5106 -0.3094 -0.0027 -0.2129 341 TRP C O   
8889  C CB  . TRP C 332 ? 0.5027 0.6704 0.5315 -0.3219 -0.0066 -0.1987 341 TRP C CB  
8890  C CG  . TRP C 332 ? 0.5231 0.6503 0.5447 -0.3314 -0.0113 -0.1937 341 TRP C CG  
8891  C CD1 . TRP C 332 ? 0.5388 0.6231 0.5505 -0.3171 -0.0104 -0.1990 341 TRP C CD1 
8892  C CD2 . TRP C 332 ? 0.5394 0.6666 0.5629 -0.3580 -0.0183 -0.1810 341 TRP C CD2 
8893  N NE1 . TRP C 332 ? 0.5723 0.6258 0.5786 -0.3326 -0.0166 -0.1912 341 TRP C NE1 
8894  C CE2 . TRP C 332 ? 0.5649 0.6442 0.5785 -0.3587 -0.0217 -0.1794 341 TRP C CE2 
8895  C CE3 . TRP C 332 ? 0.5353 0.7010 0.5679 -0.3817 -0.0223 -0.1695 341 TRP C CE3 
8896  C CZ2 . TRP C 332 ? 0.5805 0.6473 0.5930 -0.3834 -0.0294 -0.1664 341 TRP C CZ2 
8897  C CZ3 . TRP C 332 ? 0.5448 0.7018 0.5771 -0.4065 -0.0297 -0.1560 341 TRP C CZ3 
8898  C CH2 . TRP C 332 ? 0.5631 0.6702 0.5854 -0.4078 -0.0334 -0.1544 341 TRP C CH2 
8899  N N   . TYR C 333 ? 0.5088 0.7518 0.5408 -0.3536 -0.0175 -0.2051 342 TYR C N   
8900  C CA  . TYR C 333 ? 0.4768 0.7755 0.5224 -0.3514 -0.0123 -0.2002 342 TYR C CA  
8901  C C   . TYR C 333 ? 0.4584 0.7885 0.5195 -0.3585 -0.0077 -0.1806 342 TYR C C   
8902  O O   . TYR C 333 ? 0.4696 0.7771 0.5293 -0.3691 -0.0104 -0.1726 342 TYR C O   
8903  C CB  . TYR C 333 ? 0.4999 0.8091 0.5378 -0.3706 -0.0225 -0.2080 342 TYR C CB  
8904  C CG  . TYR C 333 ? 0.5274 0.8047 0.5475 -0.3604 -0.0271 -0.2286 342 TYR C CG  
8905  C CD1 . TYR C 333 ? 0.5779 0.7957 0.5773 -0.3629 -0.0359 -0.2400 342 TYR C CD1 
8906  C CD2 . TYR C 333 ? 0.5207 0.8277 0.5434 -0.3463 -0.0227 -0.2365 342 TYR C CD2 
8907  C CE1 . TYR C 333 ? 0.6091 0.7999 0.5904 -0.3503 -0.0399 -0.2592 342 TYR C CE1 
8908  C CE2 . TYR C 333 ? 0.5412 0.8238 0.5477 -0.3351 -0.0262 -0.2546 342 TYR C CE2 
8909  C CZ  . TYR C 333 ? 0.5921 0.8175 0.5776 -0.3365 -0.0347 -0.2662 342 TYR C CZ  
8910  O OH  . TYR C 333 ? 0.6437 0.8463 0.6109 -0.3225 -0.0384 -0.2848 342 TYR C OH  
8911  N N   . CYS C 334 ? 0.4303 0.8129 0.5050 -0.3514 -0.0008 -0.1723 343 CYS C N   
8912  C CA  . CYS C 334 ? 0.4123 0.8265 0.5000 -0.3512 0.0049  -0.1545 343 CYS C CA  
8913  C C   . CYS C 334 ? 0.3779 0.8453 0.4760 -0.3366 0.0121  -0.1499 343 CYS C C   
8914  O O   . CYS C 334 ? 0.3640 0.8287 0.4608 -0.3164 0.0168  -0.1577 343 CYS C O   
8915  C CB  . CYS C 334 ? 0.4075 0.7859 0.4935 -0.3354 0.0102  -0.1535 343 CYS C CB  
8916  S SG  . CYS C 334 ? 0.4210 0.8209 0.5184 -0.3285 0.0175  -0.1350 343 CYS C SG  
8917  N N   . ASP C 335 ? 0.3733 0.8898 0.4807 -0.3475 0.0120  -0.1370 344 ASP C N   
8918  C CA  . ASP C 335 ? 0.3515 0.9199 0.4660 -0.3360 0.0166  -0.1337 344 ASP C CA  
8919  C C   . ASP C 335 ? 0.3213 0.9023 0.4398 -0.3068 0.0262  -0.1284 344 ASP C C   
8920  O O   . ASP C 335 ? 0.3145 0.8939 0.4358 -0.3005 0.0300  -0.1184 344 ASP C O   
8921  C CB  . ASP C 335 ? 0.3566 0.9775 0.4797 -0.3538 0.0143  -0.1190 344 ASP C CB  
8922  C CG  . ASP C 335 ? 0.3979 1.0323 0.5186 -0.3785 0.0050  -0.1237 344 ASP C CG  
8923  O OD1 . ASP C 335 ? 0.4249 1.0686 0.5430 -0.3723 0.0046  -0.1344 344 ASP C OD1 
8924  O OD2 . ASP C 335 ? 0.4408 1.0795 0.5624 -0.4055 -0.0025 -0.1151 344 ASP C OD2 
8925  N N   . ASN C 336 ? 0.3075 0.9017 0.4252 -0.2894 0.0292  -0.1344 345 ASN C N   
8926  C CA  . ASN C 336 ? 0.2882 0.8942 0.4069 -0.2627 0.0360  -0.1289 345 ASN C CA  
8927  C C   . ASN C 336 ? 0.2824 0.9404 0.4049 -0.2571 0.0372  -0.1237 345 ASN C C   
8928  O O   . ASN C 336 ? 0.3079 0.9959 0.4344 -0.2755 0.0336  -0.1214 345 ASN C O   
8929  C CB  . ASN C 336 ? 0.2867 0.8597 0.3995 -0.2458 0.0375  -0.1392 345 ASN C CB  
8930  C CG  . ASN C 336 ? 0.2625 0.8240 0.3734 -0.2235 0.0421  -0.1330 345 ASN C CG  
8931  O OD1 . ASN C 336 ? 0.2319 0.7707 0.3424 -0.2232 0.0433  -0.1288 345 ASN C OD1 
8932  N ND2 . ASN C 336 ? 0.2769 0.8523 0.3854 -0.2050 0.0436  -0.1321 345 ASN C ND2 
8933  N N   . ALA C 337 ? 0.2616 0.9300 0.3815 -0.2327 0.0410  -0.1218 346 ALA C N   
8934  C CA  . ALA C 337 ? 0.2543 0.9746 0.3763 -0.2242 0.0423  -0.1148 346 ALA C CA  
8935  C C   . ALA C 337 ? 0.2617 1.0117 0.3868 -0.2384 0.0388  -0.1202 346 ALA C C   
8936  O O   . ALA C 337 ? 0.2536 1.0077 0.3758 -0.2286 0.0385  -0.1264 346 ALA C O   
8937  C CB  . ALA C 337 ? 0.2391 0.9568 0.3544 -0.1958 0.0450  -0.1128 346 ALA C CB  
8938  N N   . GLY C 338 ? 0.2794 1.0509 0.4101 -0.2630 0.0352  -0.1168 347 GLY C N   
8939  C CA  . GLY C 338 ? 0.2902 1.0908 0.4232 -0.2789 0.0307  -0.1211 347 GLY C CA  
8940  C C   . GLY C 338 ? 0.3024 1.0659 0.4297 -0.2889 0.0260  -0.1374 347 GLY C C   
8941  O O   . GLY C 338 ? 0.3203 1.1036 0.4476 -0.3019 0.0214  -0.1431 347 GLY C O   
8942  N N   . SER C 339 ? 0.2957 1.0078 0.4176 -0.2816 0.0271  -0.1447 348 SER C N   
8943  C CA  . SER C 339 ? 0.2995 0.9725 0.4140 -0.2869 0.0232  -0.1602 348 SER C CA  
8944  C C   . SER C 339 ? 0.3137 0.9405 0.4243 -0.2962 0.0211  -0.1621 348 SER C C   
8945  O O   . SER C 339 ? 0.3129 0.9431 0.4278 -0.2995 0.0228  -0.1508 348 SER C O   
8946  C CB  . SER C 339 ? 0.2795 0.9420 0.3908 -0.2634 0.0272  -0.1658 348 SER C CB  
8947  O OG  . SER C 339 ? 0.2604 0.9667 0.3750 -0.2542 0.0289  -0.1613 348 SER C OG  
8948  N N   . VAL C 340 ? 0.3279 0.9134 0.4296 -0.3001 0.0172  -0.1758 349 VAL C N   
8949  C CA  . VAL C 340 ? 0.3507 0.8901 0.4465 -0.3094 0.0141  -0.1783 349 VAL C CA  
8950  C C   . VAL C 340 ? 0.3507 0.8494 0.4405 -0.2907 0.0176  -0.1863 349 VAL C C   
8951  O O   . VAL C 340 ? 0.3532 0.8463 0.4378 -0.2811 0.0175  -0.1971 349 VAL C O   
8952  C CB  . VAL C 340 ? 0.3816 0.9001 0.4676 -0.3332 0.0036  -0.1881 349 VAL C CB  
8953  C CG1 . VAL C 340 ? 0.4037 0.8781 0.4837 -0.3447 -0.0006 -0.1869 349 VAL C CG1 
8954  C CG2 . VAL C 340 ? 0.3918 0.9532 0.4829 -0.3532 -0.0013 -0.1815 349 VAL C CG2 
8955  N N   . SER C 341 ? 0.3561 0.8287 0.4466 -0.2860 0.0204  -0.1804 350 SER C N   
8956  C CA  . SER C 341 ? 0.3588 0.7945 0.4442 -0.2689 0.0236  -0.1860 350 SER C CA  
8957  C C   . SER C 341 ? 0.4005 0.7885 0.4743 -0.2782 0.0179  -0.1961 350 SER C C   
8958  O O   . SER C 341 ? 0.4202 0.7925 0.4920 -0.2950 0.0134  -0.1922 350 SER C O   
8959  C CB  . SER C 341 ? 0.3321 0.7678 0.4239 -0.2549 0.0301  -0.1737 350 SER C CB  
8960  O OG  . SER C 341 ? 0.2861 0.7550 0.3833 -0.2401 0.0343  -0.1676 350 SER C OG  
8961  N N   . PHE C 342 ? 0.4187 0.7848 0.4837 -0.2665 0.0176  -0.2086 351 PHE C N   
8962  C CA  . PHE C 342 ? 0.4656 0.7858 0.5163 -0.2702 0.0120  -0.2199 351 PHE C CA  
8963  C C   . PHE C 342 ? 0.4752 0.7691 0.5239 -0.2505 0.0173  -0.2204 351 PHE C C   
8964  O O   . PHE C 342 ? 0.4564 0.7664 0.5102 -0.2329 0.0232  -0.2189 351 PHE C O   
8965  C CB  . PHE C 342 ? 0.4821 0.8015 0.5213 -0.2725 0.0061  -0.2353 351 PHE C CB  
8966  C CG  . PHE C 342 ? 0.5230 0.7949 0.5435 -0.2695 0.0003  -0.2496 351 PHE C CG  
8967  C CD1 . PHE C 342 ? 0.5655 0.7974 0.5760 -0.2833 -0.0068 -0.2504 351 PHE C CD1 
8968  C CD2 . PHE C 342 ? 0.5360 0.8040 0.5475 -0.2519 0.0013  -0.2622 351 PHE C CD2 
8969  C CE1 . PHE C 342 ? 0.6148 0.7986 0.6043 -0.2780 -0.0133 -0.2647 351 PHE C CE1 
8970  C CE2 . PHE C 342 ? 0.5803 0.8052 0.5716 -0.2456 -0.0044 -0.2765 351 PHE C CE2 
8971  C CZ  . PHE C 342 ? 0.6191 0.7998 0.5986 -0.2579 -0.0119 -0.2783 351 PHE C CZ  
8972  N N   . PHE C 343 ? 0.5134 0.7673 0.5546 -0.2544 0.0146  -0.2212 352 PHE C N   
8973  C CA  . PHE C 343 ? 0.5258 0.7542 0.5651 -0.2372 0.0192  -0.2205 352 PHE C CA  
8974  C C   . PHE C 343 ? 0.5851 0.7706 0.6056 -0.2344 0.0132  -0.2350 352 PHE C C   
8975  O O   . PHE C 343 ? 0.6184 0.7708 0.6292 -0.2482 0.0063  -0.2369 352 PHE C O   
8976  C CB  . PHE C 343 ? 0.5162 0.7354 0.5627 -0.2422 0.0216  -0.2071 352 PHE C CB  
8977  C CG  . PHE C 343 ? 0.4828 0.7413 0.5435 -0.2496 0.0246  -0.1937 352 PHE C CG  
8978  C CD1 . PHE C 343 ? 0.4863 0.7598 0.5485 -0.2705 0.0195  -0.1905 352 PHE C CD1 
8979  C CD2 . PHE C 343 ? 0.4435 0.7242 0.5143 -0.2350 0.0317  -0.1839 352 PHE C CD2 
8980  C CE1 . PHE C 343 ? 0.4533 0.7670 0.5275 -0.2744 0.0227  -0.1780 352 PHE C CE1 
8981  C CE2 . PHE C 343 ? 0.4043 0.7196 0.4847 -0.2382 0.0340  -0.1727 352 PHE C CE2 
8982  C CZ  . PHE C 343 ? 0.4132 0.7471 0.4958 -0.2568 0.0302  -0.1697 352 PHE C CZ  
8983  N N   . PRO C 344 ? 0.6054 0.7916 0.6197 -0.2160 0.0154  -0.2446 353 PRO C N   
8984  C CA  . PRO C 344 ? 0.6637 0.8175 0.6571 -0.2088 0.0094  -0.2614 353 PRO C CA  
8985  C C   . PRO C 344 ? 0.7207 0.8229 0.6999 -0.2053 0.0059  -0.2648 353 PRO C C   
8986  O O   . PRO C 344 ? 0.7702 0.8358 0.7284 -0.2096 -0.0036 -0.2780 353 PRO C O   
8987  C CB  . PRO C 344 ? 0.6427 0.8220 0.6384 -0.1867 0.0156  -0.2649 353 PRO C CB  
8988  C CG  . PRO C 344 ? 0.5884 0.8145 0.6042 -0.1898 0.0214  -0.2521 353 PRO C CG  
8989  C CD  . PRO C 344 ? 0.5667 0.7875 0.5930 -0.1997 0.0234  -0.2385 353 PRO C CD  
8990  N N   . GLN C 345 ? 0.7254 0.8222 0.7139 -0.1980 0.0122  -0.2534 354 GLN C N   
8991  C CA  . GLN C 345 ? 0.7739 0.8235 0.7493 -0.1924 0.0096  -0.2558 354 GLN C CA  
8992  C C   . GLN C 345 ? 0.7704 0.8089 0.7562 -0.2020 0.0118  -0.2407 354 GLN C C   
8993  O O   . GLN C 345 ? 0.7288 0.7978 0.7331 -0.1997 0.0196  -0.2274 354 GLN C O   
8994  C CB  . GLN C 345 ? 0.7788 0.8244 0.7473 -0.1650 0.0142  -0.2620 354 GLN C CB  
8995  C CG  . GLN C 345 ? 0.7456 0.8400 0.7304 -0.1520 0.0230  -0.2557 354 GLN C CG  
8996  C CD  . GLN C 345 ? 0.7064 0.8246 0.7126 -0.1585 0.0292  -0.2376 354 GLN C CD  
8997  O OE1 . GLN C 345 ? 0.7081 0.8099 0.7179 -0.1563 0.0318  -0.2290 354 GLN C OE1 
8998  N NE2 . GLN C 345 ? 0.6574 0.8131 0.6761 -0.1659 0.0310  -0.2323 354 GLN C NE2 
8999  N N   . ALA C 346 ? 0.8158 0.8094 0.7874 -0.2122 0.0040  -0.2431 355 ALA C N   
9000  C CA  . ALA C 346 ? 0.8178 0.7949 0.7957 -0.2242 0.0041  -0.2293 355 ALA C CA  
9001  C C   . ALA C 346 ? 0.7674 0.7754 0.7664 -0.2154 0.0152  -0.2140 355 ALA C C   
9002  O O   . ALA C 346 ? 0.7467 0.7859 0.7611 -0.2269 0.0182  -0.2021 355 ALA C O   
9003  C CB  . ALA C 346 ? 0.8591 0.7780 0.8162 -0.2196 -0.0024 -0.2353 355 ALA C CB  
9004  N N   . GLU C 347 ? 0.7439 0.7415 0.7412 -0.1946 0.0205  -0.2145 356 GLU C N   
9005  C CA  . GLU C 347 ? 0.6836 0.7122 0.6964 -0.1803 0.0298  -0.2051 356 GLU C CA  
9006  C C   . GLU C 347 ? 0.6276 0.6932 0.6578 -0.1895 0.0336  -0.1927 356 GLU C C   
9007  O O   . GLU C 347 ? 0.6114 0.6791 0.6502 -0.1915 0.0368  -0.1805 356 GLU C O   
9008  C CB  . GLU C 347 ? 0.6838 0.7301 0.6936 -0.1626 0.0322  -0.2143 356 GLU C CB  
9009  C CG  . GLU C 347 ? 0.7496 0.7647 0.7426 -0.1458 0.0306  -0.2245 356 GLU C CG  
9010  C CD  . GLU C 347 ? 0.8276 0.8106 0.8184 -0.1439 0.0312  -0.2173 356 GLU C CD  
9011  O OE1 . GLU C 347 ? 0.8929 0.8348 0.8682 -0.1507 0.0242  -0.2234 356 GLU C OE1 
9012  O OE2 . GLU C 347 ? 0.8109 0.8084 0.8146 -0.1372 0.0376  -0.2051 356 GLU C OE2 
9013  N N   . THR C 348 ? 0.5917 0.6867 0.6256 -0.1938 0.0330  -0.1964 357 THR C N   
9014  C CA  . THR C 348 ? 0.5406 0.6737 0.5886 -0.1989 0.0363  -0.1863 357 THR C CA  
9015  C C   . THR C 348 ? 0.5283 0.6644 0.5815 -0.2166 0.0345  -0.1766 357 THR C C   
9016  O O   . THR C 348 ? 0.5097 0.6730 0.5737 -0.2159 0.0385  -0.1655 357 THR C O   
9017  C CB  . THR C 348 ? 0.5350 0.6967 0.5838 -0.2014 0.0347  -0.1933 357 THR C CB  
9018  O OG1 . THR C 348 ? 0.5579 0.7033 0.5938 -0.1947 0.0315  -0.2080 357 THR C OG1 
9019  C CG2 . THR C 348 ? 0.5027 0.7000 0.5627 -0.1903 0.0401  -0.1856 357 THR C CG2 
9020  N N   . CYS C 349 ? 0.5349 0.6438 0.5790 -0.2321 0.0279  -0.1801 358 CYS C N   
9021  C CA  . CYS C 349 ? 0.5166 0.6332 0.5656 -0.2526 0.0249  -0.1695 358 CYS C CA  
9022  C C   . CYS C 349 ? 0.5229 0.6041 0.5668 -0.2595 0.0222  -0.1637 358 CYS C C   
9023  O O   . CYS C 349 ? 0.5481 0.5879 0.5781 -0.2568 0.0178  -0.1725 358 CYS C O   
9024  C CB  . CYS C 349 ? 0.5344 0.6573 0.5782 -0.2723 0.0168  -0.1755 358 CYS C CB  
9025  S SG  . CYS C 349 ? 0.5172 0.6899 0.5689 -0.2693 0.0194  -0.1792 358 CYS C SG  
9026  N N   . LYS C 350 ? 0.5006 0.5986 0.5546 -0.2670 0.0248  -0.1486 359 LYS C N   
9027  C CA  . LYS C 350 ? 0.5234 0.5930 0.5734 -0.2797 0.0208  -0.1405 359 LYS C CA  
9028  C C   . LYS C 350 ? 0.5191 0.6174 0.5772 -0.3017 0.0181  -0.1270 359 LYS C C   
9029  O O   . LYS C 350 ? 0.4949 0.6400 0.5647 -0.3002 0.0228  -0.1203 359 LYS C O   
9030  C CB  . LYS C 350 ? 0.5140 0.5708 0.5671 -0.2645 0.0271  -0.1332 359 LYS C CB  
9031  C CG  . LYS C 350 ? 0.4996 0.5858 0.5628 -0.2447 0.0360  -0.1301 359 LYS C CG  
9032  C CD  . LYS C 350 ? 0.5278 0.5864 0.5860 -0.2257 0.0391  -0.1348 359 LYS C CD  
9033  C CE  . LYS C 350 ? 0.5246 0.6075 0.5884 -0.2081 0.0444  -0.1369 359 LYS C CE  
9034  N NZ  . LYS C 350 ? 0.5782 0.6365 0.6361 -0.1921 0.0460  -0.1424 359 LYS C NZ  
9035  N N   . VAL C 351 ? 0.5446 0.6151 0.5956 -0.3214 0.0101  -0.1218 360 VAL C N   
9036  C CA  . VAL C 351 ? 0.5469 0.6414 0.6025 -0.3484 0.0040  -0.1099 360 VAL C CA  
9037  C C   . VAL C 351 ? 0.5673 0.6445 0.6225 -0.3626 0.0006  -0.0950 360 VAL C C   
9038  O O   . VAL C 351 ? 0.5906 0.6178 0.6337 -0.3607 -0.0035 -0.0993 360 VAL C O   
9039  C CB  . VAL C 351 ? 0.5701 0.6473 0.6135 -0.3653 -0.0072 -0.1211 360 VAL C CB  
9040  C CG1 . VAL C 351 ? 0.6112 0.6238 0.6343 -0.3611 -0.0143 -0.1346 360 VAL C CG1 
9041  C CG2 . VAL C 351 ? 0.5984 0.6927 0.6444 -0.3960 -0.0157 -0.1080 360 VAL C CG2 
9042  N N   . GLN C 352 ? 0.5614 0.6828 0.6296 -0.3754 0.0024  -0.0771 361 GLN C N   
9043  C CA  . GLN C 352 ? 0.5876 0.7061 0.6589 -0.3878 0.0010  -0.0594 361 GLN C CA  
9044  C C   . GLN C 352 ? 0.5961 0.7523 0.6741 -0.4177 -0.0057 -0.0433 361 GLN C C   
9045  O O   . GLN C 352 ? 0.5736 0.7897 0.6658 -0.4154 0.0009  -0.0323 361 GLN C O   
9046  C CB  . GLN C 352 ? 0.5573 0.7050 0.6405 -0.3658 0.0135  -0.0503 361 GLN C CB  
9047  C CG  . GLN C 352 ? 0.6278 0.7743 0.7144 -0.3734 0.0138  -0.0324 361 GLN C CG  
9048  C CD  . GLN C 352 ? 0.7308 0.8480 0.8148 -0.3473 0.0215  -0.0364 361 GLN C CD  
9049  O OE1 . GLN C 352 ? 0.7391 0.8856 0.8315 -0.3284 0.0309  -0.0305 361 GLN C OE1 
9050  N NE2 . GLN C 352 ? 0.7846 0.8435 0.8554 -0.3451 0.0166  -0.0471 361 GLN C NE2 
9051  N N   . SER C 353 ? 0.6367 0.7579 0.7032 -0.4455 -0.0196 -0.0410 362 SER C N   
9052  C CA  . SER C 353 ? 0.6444 0.7973 0.7150 -0.4789 -0.0293 -0.0265 362 SER C CA  
9053  C C   . SER C 353 ? 0.6231 0.8041 0.6955 -0.4780 -0.0295 -0.0379 362 SER C C   
9054  O O   . SER C 353 ? 0.6339 0.7760 0.6932 -0.4698 -0.0331 -0.0581 362 SER C O   
9055  C CB  . SER C 353 ? 0.6227 0.8358 0.7112 -0.4841 -0.0226 -0.0020 362 SER C CB  
9056  O OG  . SER C 353 ? 0.6530 0.8947 0.7448 -0.5195 -0.0334 0.0150  362 SER C OG  
9057  N N   . ASN C 354 ? 0.5912 0.8410 0.6792 -0.4839 -0.0252 -0.0252 363 ASN C N   
9058  C CA  . ASN C 354 ? 0.5744 0.8566 0.6650 -0.4847 -0.0257 -0.0340 363 ASN C CA  
9059  C C   . ASN C 354 ? 0.5190 0.8354 0.6192 -0.4505 -0.0107 -0.0409 363 ASN C C   
9060  O O   . ASN C 354 ? 0.4979 0.8579 0.6045 -0.4476 -0.0082 -0.0432 363 ASN C O   
9061  C CB  . ASN C 354 ? 0.5827 0.9216 0.6830 -0.5140 -0.0319 -0.0154 363 ASN C CB  
9062  C CG  . ASN C 354 ? 0.5552 0.9601 0.6734 -0.5056 -0.0210 0.0051  363 ASN C CG  
9063  O OD1 . ASN C 354 ? 0.5366 0.9352 0.6578 -0.4836 -0.0114 0.0078  363 ASN C OD1 
9064  N ND2 . ASN C 354 ? 0.5600 1.0302 0.6892 -0.5223 -0.0227 0.0200  363 ASN C ND2 
9065  N N   . ARG C 355 ? 0.4916 0.7864 0.5916 -0.4254 -0.0018 -0.0438 364 ARG C N   
9066  C CA  . ARG C 355 ? 0.4494 0.7654 0.5552 -0.3932 0.0104  -0.0507 364 ARG C CA  
9067  C C   . ARG C 355 ? 0.4455 0.7159 0.5412 -0.3731 0.0120  -0.0720 364 ARG C C   
9068  O O   . ARG C 355 ? 0.4634 0.6809 0.5490 -0.3704 0.0094  -0.0788 364 ARG C O   
9069  C CB  . ARG C 355 ? 0.4314 0.7607 0.5439 -0.3786 0.0187  -0.0380 364 ARG C CB  
9070  C CG  . ARG C 355 ? 0.4057 0.7844 0.5266 -0.3558 0.0285  -0.0350 364 ARG C CG  
9071  C CD  . ARG C 355 ? 0.3981 0.8380 0.5278 -0.3705 0.0271  -0.0222 364 ARG C CD  
9072  N NE  . ARG C 355 ? 0.3902 0.8614 0.5221 -0.3515 0.0322  -0.0302 364 ARG C NE  
9073  C CZ  . ARG C 355 ? 0.3744 0.9078 0.5140 -0.3480 0.0357  -0.0198 364 ARG C CZ  
9074  N NH1 . ARG C 355 ? 0.3789 0.9529 0.5257 -0.3624 0.0349  -0.0007 364 ARG C NH1 
9075  N NH2 . ARG C 355 ? 0.3713 0.9275 0.5109 -0.3298 0.0396  -0.0277 364 ARG C NH2 
9076  N N   . VAL C 356 ? 0.4228 0.7156 0.5207 -0.3588 0.0162  -0.0817 365 VAL C N   
9077  C CA  . VAL C 356 ? 0.4204 0.6781 0.5094 -0.3422 0.0170  -0.1004 365 VAL C CA  
9078  C C   . VAL C 356 ? 0.3928 0.6715 0.4878 -0.3138 0.0272  -0.1020 365 VAL C C   
9079  O O   . VAL C 356 ? 0.3818 0.7073 0.4858 -0.3078 0.0320  -0.0930 365 VAL C O   
9080  C CB  . VAL C 356 ? 0.4259 0.6865 0.5095 -0.3529 0.0104  -0.1120 365 VAL C CB  
9081  C CG1 . VAL C 356 ? 0.4107 0.6557 0.4892 -0.3311 0.0141  -0.1281 365 VAL C CG1 
9082  C CG2 . VAL C 356 ? 0.4735 0.6926 0.5445 -0.3754 -0.0014 -0.1162 365 VAL C CG2 
9083  N N   . PHE C 357 ? 0.3886 0.6325 0.4774 -0.2959 0.0298  -0.1129 366 PHE C N   
9084  C CA  . PHE C 357 ? 0.3580 0.6133 0.4503 -0.2708 0.0375  -0.1136 366 PHE C CA  
9085  C C   . PHE C 357 ? 0.3632 0.5974 0.4489 -0.2593 0.0371  -0.1289 366 PHE C C   
9086  O O   . PHE C 357 ? 0.3778 0.5720 0.4555 -0.2564 0.0353  -0.1363 366 PHE C O   
9087  C CB  . PHE C 357 ? 0.3529 0.5880 0.4454 -0.2609 0.0413  -0.1062 366 PHE C CB  
9088  C CG  . PHE C 357 ? 0.3449 0.6045 0.4438 -0.2686 0.0427  -0.0901 366 PHE C CG  
9089  C CD1 . PHE C 357 ? 0.3723 0.6221 0.4706 -0.2911 0.0374  -0.0831 366 PHE C CD1 
9090  C CD2 . PHE C 357 ? 0.3109 0.6025 0.4148 -0.2527 0.0486  -0.0815 366 PHE C CD2 
9091  C CE1 . PHE C 357 ? 0.3559 0.6336 0.4610 -0.2987 0.0389  -0.0664 366 PHE C CE1 
9092  C CE2 . PHE C 357 ? 0.2970 0.6151 0.4060 -0.2577 0.0503  -0.0665 366 PHE C CE2 
9093  C CZ  . PHE C 357 ? 0.3157 0.6292 0.4264 -0.2811 0.0459  -0.0584 366 PHE C CZ  
9094  N N   . CYS C 358 ? 0.3536 0.6164 0.4421 -0.2520 0.0387  -0.1330 367 CYS C N   
9095  C CA  . CYS C 358 ? 0.3653 0.6147 0.4483 -0.2410 0.0386  -0.1459 367 CYS C CA  
9096  C C   . CYS C 358 ? 0.3430 0.6092 0.4297 -0.2204 0.0437  -0.1439 367 CYS C C   
9097  O O   . CYS C 358 ? 0.3309 0.6210 0.4228 -0.2145 0.0467  -0.1338 367 CYS C O   
9098  C CB  . CYS C 358 ? 0.3783 0.6392 0.4583 -0.2533 0.0335  -0.1550 367 CYS C CB  
9099  S SG  . CYS C 358 ? 0.4352 0.6648 0.5062 -0.2780 0.0244  -0.1585 367 CYS C SG  
9100  N N   . ASP C 359 ? 0.3442 0.5978 0.4267 -0.2095 0.0439  -0.1530 368 ASP C N   
9101  C CA  . ASP C 359 ? 0.3301 0.5950 0.4145 -0.1922 0.0469  -0.1504 368 ASP C CA  
9102  C C   . ASP C 359 ? 0.3318 0.6212 0.4165 -0.1903 0.0458  -0.1564 368 ASP C C   
9103  O O   . ASP C 359 ? 0.3467 0.6275 0.4269 -0.1918 0.0440  -0.1670 368 ASP C O   
9104  C CB  . ASP C 359 ? 0.3348 0.5707 0.4151 -0.1808 0.0480  -0.1531 368 ASP C CB  
9105  C CG  . ASP C 359 ? 0.3214 0.5640 0.4038 -0.1660 0.0499  -0.1452 368 ASP C CG  
9106  O OD1 . ASP C 359 ? 0.3176 0.5825 0.4012 -0.1606 0.0493  -0.1445 368 ASP C OD1 
9107  O OD2 . ASP C 359 ? 0.3255 0.5502 0.4074 -0.1603 0.0512  -0.1391 368 ASP C OD2 
9108  N N   . THR C 360 ? 0.3260 0.6456 0.4148 -0.1856 0.0468  -0.1498 369 THR C N   
9109  C CA  . THR C 360 ? 0.3285 0.6723 0.4175 -0.1819 0.0458  -0.1538 369 THR C CA  
9110  C C   . THR C 360 ? 0.3441 0.6752 0.4299 -0.1726 0.0456  -0.1596 369 THR C C   
9111  O O   . THR C 360 ? 0.3642 0.6962 0.4473 -0.1763 0.0442  -0.1695 369 THR C O   
9112  C CB  . THR C 360 ? 0.3062 0.6741 0.3968 -0.1719 0.0464  -0.1448 369 THR C CB  
9113  O OG1 . THR C 360 ? 0.2896 0.6753 0.3831 -0.1785 0.0472  -0.1387 369 THR C OG1 
9114  C CG2 . THR C 360 ? 0.3102 0.7030 0.4008 -0.1691 0.0449  -0.1484 369 THR C CG2 
9115  N N   . MET C 361 ? 0.3502 0.6704 0.4354 -0.1607 0.0464  -0.1530 370 MET C N   
9116  C CA  . MET C 361 ? 0.3624 0.6766 0.4456 -0.1516 0.0460  -0.1549 370 MET C CA  
9117  C C   . MET C 361 ? 0.3645 0.6880 0.4457 -0.1530 0.0453  -0.1656 370 MET C C   
9118  O O   . MET C 361 ? 0.3560 0.7014 0.4382 -0.1484 0.0442  -0.1646 370 MET C O   
9119  C CB  . MET C 361 ? 0.3790 0.6651 0.4605 -0.1461 0.0471  -0.1521 370 MET C CB  
9120  C CG  . MET C 361 ? 0.4112 0.6960 0.4926 -0.1361 0.0456  -0.1402 370 MET C CG  
9121  S SD  . MET C 361 ? 0.4919 0.7995 0.5728 -0.1292 0.0418  -0.1357 370 MET C SD  
9122  C CE  . MET C 361 ? 0.4510 0.7873 0.5325 -0.1325 0.0405  -0.1370 370 MET C CE  
9123  N N   . ASN C 362 ? 0.3773 0.6839 0.4543 -0.1586 0.0452  -0.1757 371 ASN C N   
9124  C CA  . ASN C 362 ? 0.3837 0.7007 0.4567 -0.1577 0.0439  -0.1864 371 ASN C CA  
9125  C C   . ASN C 362 ? 0.3904 0.7172 0.4608 -0.1700 0.0412  -0.1956 371 ASN C C   
9126  O O   . ASN C 362 ? 0.4063 0.7395 0.4713 -0.1688 0.0396  -0.2058 371 ASN C O   
9127  C CB  . ASN C 362 ? 0.4042 0.7023 0.4706 -0.1483 0.0445  -0.1926 371 ASN C CB  
9128  C CG  . ASN C 362 ? 0.3909 0.7038 0.4608 -0.1357 0.0460  -0.1845 371 ASN C CG  
9129  O OD1 . ASN C 362 ? 0.3821 0.7199 0.4524 -0.1315 0.0454  -0.1858 371 ASN C OD1 
9130  N ND2 . ASN C 362 ? 0.3978 0.6962 0.4698 -0.1307 0.0471  -0.1753 371 ASN C ND2 
9131  N N   . SER C 363 ? 0.3816 0.7120 0.4554 -0.1817 0.0404  -0.1914 372 SER C N   
9132  C CA  . SER C 363 ? 0.3809 0.7260 0.4536 -0.1961 0.0371  -0.1973 372 SER C CA  
9133  C C   . SER C 363 ? 0.3659 0.7409 0.4386 -0.1944 0.0360  -0.2030 372 SER C C   
9134  O O   . SER C 363 ? 0.3440 0.7393 0.4206 -0.1832 0.0381  -0.1979 372 SER C O   
9135  C CB  . SER C 363 ? 0.3734 0.7354 0.4535 -0.2049 0.0377  -0.1866 372 SER C CB  
9136  O OG  . SER C 363 ? 0.3592 0.7434 0.4450 -0.1931 0.0407  -0.1766 372 SER C OG  
9137  N N   . LEU C 364 ? 0.3737 0.7504 0.4411 -0.2071 0.0316  -0.2127 373 LEU C N   
9138  C CA  . LEU C 364 ? 0.3613 0.7669 0.4279 -0.2086 0.0297  -0.2189 373 LEU C CA  
9139  C C   . LEU C 364 ? 0.3552 0.7860 0.4274 -0.2234 0.0278  -0.2139 373 LEU C C   
9140  O O   . LEU C 364 ? 0.3754 0.7930 0.4456 -0.2390 0.0242  -0.2140 373 LEU C O   
9141  C CB  . LEU C 364 ? 0.3885 0.7751 0.4416 -0.2115 0.0247  -0.2354 373 LEU C CB  
9142  C CG  . LEU C 364 ? 0.3851 0.7745 0.4325 -0.1946 0.0264  -0.2430 373 LEU C CG  
9143  C CD1 . LEU C 364 ? 0.3743 0.7663 0.4294 -0.1787 0.0323  -0.2316 373 LEU C CD1 
9144  C CD2 . LEU C 364 ? 0.4119 0.7666 0.4423 -0.1932 0.0217  -0.2586 373 LEU C CD2 
9145  N N   . THR C 365 ? 0.3276 0.7962 0.4063 -0.2191 0.0295  -0.2087 374 THR C N   
9146  C CA  . THR C 365 ? 0.3123 0.8128 0.3972 -0.2306 0.0284  -0.2021 374 THR C CA  
9147  C C   . THR C 365 ? 0.3145 0.8322 0.3955 -0.2419 0.0237  -0.2119 374 THR C C   
9148  O O   . THR C 365 ? 0.3170 0.8442 0.3950 -0.2337 0.0237  -0.2186 374 THR C O   
9149  C CB  . THR C 365 ? 0.2856 0.8160 0.3775 -0.2178 0.0324  -0.1906 374 THR C CB  
9150  O OG1 . THR C 365 ? 0.3018 0.8109 0.3934 -0.2025 0.0356  -0.1855 374 THR C OG1 
9151  C CG2 . THR C 365 ? 0.2759 0.8282 0.3737 -0.2244 0.0331  -0.1800 374 THR C CG2 
9152  N N   . LEU C 366 ? 0.3202 0.8424 0.4008 -0.2616 0.0188  -0.2120 375 LEU C N   
9153  C CA  . LEU C 366 ? 0.3291 0.8597 0.4030 -0.2762 0.0119  -0.2227 375 LEU C CA  
9154  C C   . LEU C 366 ? 0.3301 0.8989 0.4113 -0.2931 0.0093  -0.2141 375 LEU C C   
9155  O O   . LEU C 366 ? 0.3240 0.9039 0.4132 -0.2965 0.0119  -0.2010 375 LEU C O   
9156  C CB  . LEU C 366 ? 0.3568 0.8418 0.4172 -0.2883 0.0047  -0.2339 375 LEU C CB  
9157  C CG  . LEU C 366 ? 0.3367 0.7799 0.3878 -0.2734 0.0062  -0.2424 375 LEU C CG  
9158  C CD1 . LEU C 366 ? 0.3352 0.7340 0.3723 -0.2881 -0.0024 -0.2507 375 LEU C CD1 
9159  C CD2 . LEU C 366 ? 0.3301 0.7842 0.3757 -0.2590 0.0071  -0.2532 375 LEU C CD2 
9160  N N   . PRO C 367 ? 0.3395 0.9305 0.4174 -0.3038 0.0040  -0.2211 376 PRO C N   
9161  C CA  . PRO C 367 ? 0.3450 0.9770 0.4299 -0.3207 0.0010  -0.2126 376 PRO C CA  
9162  C C   . PRO C 367 ? 0.3824 0.9960 0.4623 -0.3479 -0.0081 -0.2122 376 PRO C C   
9163  O O   . PRO C 367 ? 0.4133 0.9817 0.4795 -0.3552 -0.0150 -0.2244 376 PRO C O   
9164  C CB  . PRO C 367 ? 0.3447 1.0019 0.4260 -0.3212 -0.0020 -0.2220 376 PRO C CB  
9165  C CG  . PRO C 367 ? 0.3633 0.9805 0.4310 -0.3162 -0.0053 -0.2383 376 PRO C CG  
9166  C CD  . PRO C 367 ? 0.3512 0.9351 0.4189 -0.2988 0.0009  -0.2366 376 PRO C CD  
9167  N N   . SER C 368 ? 0.3850 1.0345 0.4748 -0.3622 -0.0088 -0.1975 377 SER C N   
9168  C CA  . SER C 368 ? 0.4250 1.0673 0.5116 -0.3923 -0.0188 -0.1935 377 SER C CA  
9169  C C   . SER C 368 ? 0.4662 1.0828 0.5367 -0.4097 -0.0313 -0.2100 377 SER C C   
9170  O O   . SER C 368 ? 0.5025 1.0819 0.5615 -0.4307 -0.0421 -0.2137 377 SER C O   
9171  C CB  . SER C 368 ? 0.4156 1.1202 0.5163 -0.4044 -0.0180 -0.1754 377 SER C CB  
9172  O OG  . SER C 368 ? 0.3908 1.1320 0.5034 -0.3802 -0.0061 -0.1643 377 SER C OG  
9173  N N   . GLU C 369 ? 0.4662 1.1002 0.5339 -0.3997 -0.0305 -0.2203 378 GLU C N   
9174  C CA  . GLU C 369 ? 0.5076 1.1236 0.5591 -0.4135 -0.0422 -0.2363 378 GLU C CA  
9175  C C   . GLU C 369 ? 0.5403 1.0881 0.5725 -0.4131 -0.0487 -0.2509 378 GLU C C   
9176  O O   . GLU C 369 ? 0.5807 1.1009 0.5954 -0.4289 -0.0615 -0.2631 378 GLU C O   
9177  C CB  . GLU C 369 ? 0.4939 1.1391 0.5460 -0.3964 -0.0378 -0.2450 378 GLU C CB  
9178  C CG  . GLU C 369 ? 0.5040 1.2154 0.5687 -0.4044 -0.0370 -0.2348 378 GLU C CG  
9179  C CD  . GLU C 369 ? 0.5141 1.2700 0.5983 -0.3954 -0.0264 -0.2142 378 GLU C CD  
9180  O OE1 . GLU C 369 ? 0.4941 1.2326 0.5830 -0.3775 -0.0179 -0.2087 378 GLU C OE1 
9181  O OE2 . GLU C 369 ? 0.5312 1.3411 0.6248 -0.4053 -0.0272 -0.2036 378 GLU C OE2 
9182  N N   . VAL C 370 ? 0.5319 1.0516 0.5660 -0.3944 -0.0407 -0.2495 379 VAL C N   
9183  C CA  . VAL C 370 ? 0.5689 1.0244 0.5846 -0.3912 -0.0461 -0.2621 379 VAL C CA  
9184  C C   . VAL C 370 ? 0.6203 1.0423 0.6231 -0.4210 -0.0609 -0.2622 379 VAL C C   
9185  O O   . VAL C 370 ? 0.6638 1.0335 0.6439 -0.4241 -0.0713 -0.2776 379 VAL C O   
9186  C CB  . VAL C 370 ? 0.5463 0.9827 0.5694 -0.3729 -0.0359 -0.2549 379 VAL C CB  
9187  C CG1 . VAL C 370 ? 0.5871 0.9629 0.5948 -0.3816 -0.0439 -0.2597 379 VAL C CG1 
9188  C CG2 . VAL C 370 ? 0.5255 0.9639 0.5495 -0.3431 -0.0263 -0.2620 379 VAL C CG2 
9189  N N   . ASN C 371 ? 0.6232 1.0750 0.6393 -0.4424 -0.0624 -0.2443 380 ASN C N   
9190  C CA  . ASN C 371 ? 0.6783 1.1009 0.6842 -0.4737 -0.0769 -0.2399 380 ASN C CA  
9191  C C   . ASN C 371 ? 0.7244 1.1261 0.7090 -0.4957 -0.0945 -0.2536 380 ASN C C   
9192  O O   . ASN C 371 ? 0.7765 1.1239 0.7408 -0.5131 -0.1089 -0.2596 380 ASN C O   
9193  C CB  . ASN C 371 ? 0.6686 1.1400 0.6949 -0.4920 -0.0744 -0.2158 380 ASN C CB  
9194  C CG  . ASN C 371 ? 0.6633 1.1432 0.7056 -0.4722 -0.0598 -0.2030 380 ASN C CG  
9195  O OD1 . ASN C 371 ? 0.7176 1.1650 0.7572 -0.4797 -0.0622 -0.1966 380 ASN C OD1 
9196  N ND2 . ASN C 371 ? 0.6447 1.1657 0.7018 -0.4467 -0.0456 -0.1995 380 ASN C ND2 
9197  N N   . LEU C 372 ? 0.7102 1.1515 0.6972 -0.4944 -0.0944 -0.2592 381 LEU C N   
9198  C CA  . LEU C 372 ? 0.7546 1.1780 0.7206 -0.5156 -0.1118 -0.2723 381 LEU C CA  
9199  C C   . LEU C 372 ? 0.7949 1.1458 0.7316 -0.5039 -0.1200 -0.2947 381 LEU C C   
9200  O O   . LEU C 372 ? 0.8519 1.1639 0.7636 -0.5218 -0.1377 -0.3069 381 LEU C O   
9201  C CB  . LEU C 372 ? 0.7330 1.2094 0.7059 -0.5090 -0.1080 -0.2767 381 LEU C CB  
9202  C CG  . LEU C 372 ? 0.6880 1.2387 0.6911 -0.5003 -0.0926 -0.2579 381 LEU C CG  
9203  C CD1 . LEU C 372 ? 0.6739 1.2661 0.6800 -0.4870 -0.0882 -0.2659 381 LEU C CD1 
9204  C CD2 . LEU C 372 ? 0.6977 1.2893 0.7159 -0.5301 -0.0967 -0.2348 381 LEU C CD2 
9205  N N   . CYS C 373 ? 0.7737 1.1052 0.7119 -0.4728 -0.1077 -0.3000 382 CYS C N   
9206  C CA  . CYS C 373 ? 0.8148 1.0812 0.7253 -0.4577 -0.1141 -0.3205 382 CYS C CA  
9207  C C   . CYS C 373 ? 0.8664 1.0672 0.7559 -0.4784 -0.1298 -0.3212 382 CYS C C   
9208  O O   . CYS C 373 ? 0.9160 1.0564 0.7749 -0.4734 -0.1416 -0.3399 382 CYS C O   
9209  C CB  . CYS C 373 ? 0.7784 1.0471 0.6977 -0.4200 -0.0966 -0.3233 382 CYS C CB  
9210  S SG  . CYS C 373 ? 0.7729 1.0821 0.6940 -0.3921 -0.0875 -0.3365 382 CYS C SG  
9211  N N   . ASN C 374 ? 0.8588 1.0716 0.7633 -0.5016 -0.1308 -0.3006 383 ASN C N   
9212  C CA  . ASN C 374 ? 0.9119 1.0652 0.7981 -0.5240 -0.1462 -0.2982 383 ASN C CA  
9213  C C   . ASN C 374 ? 0.9717 1.0985 0.8335 -0.5562 -0.1696 -0.3055 383 ASN C C   
9214  O O   . ASN C 374 ? 1.0319 1.0926 0.8670 -0.5715 -0.1869 -0.3112 383 ASN C O   
9215  C CB  . ASN C 374 ? 0.8889 1.0712 0.7995 -0.5420 -0.1410 -0.2717 383 ASN C CB  
9216  C CG  . ASN C 374 ? 0.8406 1.0497 0.7749 -0.5125 -0.1191 -0.2628 383 ASN C CG  
9217  O OD1 . ASN C 374 ? 0.8509 1.0240 0.7769 -0.4849 -0.1125 -0.2740 383 ASN C OD1 
9218  N ND2 . ASN C 374 ? 0.8109 1.0839 0.7739 -0.5174 -0.1082 -0.2423 383 ASN C ND2 
9219  N N   . VAL C 375 ? 0.9594 1.1385 0.8301 -0.5672 -0.1708 -0.3043 384 VAL C N   
9220  C CA  . VAL C 375 ? 1.0118 1.1778 0.8625 -0.6007 -0.1930 -0.3090 384 VAL C CA  
9221  C C   . VAL C 375 ? 1.0440 1.1839 0.8677 -0.5836 -0.1999 -0.3367 384 VAL C C   
9222  O O   . VAL C 375 ? 1.1088 1.1900 0.8981 -0.5991 -0.2217 -0.3512 384 VAL C O   
9223  C CB  . VAL C 375 ? 0.9786 1.2254 0.8569 -0.6270 -0.1911 -0.2878 384 VAL C CB  
9224  C CG1 . VAL C 375 ? 1.0248 1.2726 0.8848 -0.6550 -0.2111 -0.2958 384 VAL C CG1 
9225  C CG2 . VAL C 375 ? 0.9641 1.2284 0.8609 -0.6519 -0.1911 -0.2607 384 VAL C CG2 
9226  N N   . ASP C 376 ? 1.0040 1.1843 0.8409 -0.5509 -0.1823 -0.3442 385 ASP C N   
9227  C CA  . ASP C 376 ? 1.0322 1.2080 0.8485 -0.5395 -0.1885 -0.3666 385 ASP C CA  
9228  C C   . ASP C 376 ? 1.0292 1.1803 0.8310 -0.4973 -0.1796 -0.3878 385 ASP C C   
9229  O O   . ASP C 376 ? 1.0806 1.1880 0.8491 -0.4912 -0.1930 -0.4101 385 ASP C O   
9230  C CB  . ASP C 376 ? 1.0015 1.2537 0.8387 -0.5500 -0.1842 -0.3588 385 ASP C CB  
9231  C CG  . ASP C 376 ? 1.0721 1.3085 0.8820 -0.5683 -0.2044 -0.3748 385 ASP C CG  
9232  O OD1 . ASP C 376 ? 1.1485 1.3151 0.9214 -0.5637 -0.2195 -0.3961 385 ASP C OD1 
9233  O OD2 . ASP C 376 ? 1.0872 1.3806 0.9110 -0.5862 -0.2058 -0.3666 385 ASP C OD2 
9234  N N   . ILE C 377 ? 0.9736 1.1545 0.7991 -0.4681 -0.1579 -0.3808 386 ILE C N   
9235  C CA  . ILE C 377 ? 0.9691 1.1338 0.7830 -0.4281 -0.1487 -0.3983 386 ILE C CA  
9236  C C   . ILE C 377 ? 0.9525 1.1665 0.7705 -0.4147 -0.1433 -0.4070 386 ILE C C   
9237  O O   . ILE C 377 ? 0.9011 1.1608 0.7404 -0.3896 -0.1251 -0.4022 386 ILE C O   
9238  C CB  . ILE C 377 ? 1.0347 1.1177 0.8055 -0.4213 -0.1655 -0.4209 386 ILE C CB  
9239  C CG1 . ILE C 377 ? 1.0451 1.0753 0.8104 -0.4243 -0.1679 -0.4142 386 ILE C CG1 
9240  C CG2 . ILE C 377 ? 1.0278 1.1067 0.7844 -0.3821 -0.1583 -0.4401 386 ILE C CG2 
9241  C CD1 . ILE C 377 ? 1.1141 1.0622 0.8365 -0.4373 -0.1922 -0.4301 386 ILE C CD1 
9242  N N   . PHE C 378 ? 0.9985 1.1999 0.7938 -0.4323 -0.1606 -0.4198 387 PHE C N   
9243  C CA  . PHE C 378 ? 0.9851 1.2360 0.7845 -0.4277 -0.1583 -0.4260 387 PHE C CA  
9244  C C   . PHE C 378 ? 0.9601 1.2651 0.7853 -0.4585 -0.1583 -0.4058 387 PHE C C   
9245  O O   . PHE C 378 ? 0.9915 1.2774 0.8111 -0.4916 -0.1727 -0.3986 387 PHE C O   
9246  C CB  . PHE C 378 ? 1.0482 1.2554 0.8072 -0.4296 -0.1779 -0.4512 387 PHE C CB  
9247  C CG  . PHE C 378 ? 1.0898 1.2322 0.8175 -0.4024 -0.1817 -0.4707 387 PHE C CG  
9248  C CD1 . PHE C 378 ? 1.1633 1.2276 0.8575 -0.4162 -0.2016 -0.4806 387 PHE C CD1 
9249  C CD2 . PHE C 378 ? 1.0530 1.2129 0.7845 -0.3626 -0.1657 -0.4778 387 PHE C CD2 
9250  C CE1 . PHE C 378 ? 1.1920 1.1945 0.8546 -0.3880 -0.2054 -0.4991 387 PHE C CE1 
9251  C CE2 . PHE C 378 ? 1.0906 1.1947 0.7928 -0.3354 -0.1688 -0.4951 387 PHE C CE2 
9252  C CZ  . PHE C 378 ? 1.1545 1.1789 0.8215 -0.3470 -0.1886 -0.5064 387 PHE C CZ  
9253  N N   . ASN C 379 ? 0.9051 1.2787 0.7585 -0.4461 -0.1420 -0.3955 388 ASN C N   
9254  C CA  . ASN C 379 ? 0.8757 1.3114 0.7556 -0.4673 -0.1385 -0.3761 388 ASN C CA  
9255  C C   . ASN C 379 ? 0.8243 1.3165 0.7294 -0.4392 -0.1179 -0.3689 388 ASN C C   
9256  O O   . ASN C 379 ? 0.7973 1.2800 0.7100 -0.4131 -0.1047 -0.3669 388 ASN C O   
9257  C CB  . ASN C 379 ? 0.8635 1.2970 0.7591 -0.4890 -0.1384 -0.3552 388 ASN C CB  
9258  C CG  . ASN C 379 ? 0.8323 1.2482 0.7393 -0.4657 -0.1238 -0.3485 388 ASN C CG  
9259  O OD1 . ASN C 379 ? 0.7544 1.2142 0.6864 -0.4464 -0.1061 -0.3369 388 ASN C OD1 
9260  N ND2 . ASN C 379 ? 0.8785 1.2284 0.7658 -0.4676 -0.1321 -0.3555 388 ASN C ND2 
9261  N N   . PRO C 380 ? 0.8127 1.3634 0.7298 -0.4445 -0.1159 -0.3644 389 PRO C N   
9262  C CA  . PRO C 380 ? 0.7602 1.3722 0.7045 -0.4241 -0.0978 -0.3520 389 PRO C CA  
9263  C C   . PRO C 380 ? 0.7321 1.3530 0.6991 -0.4222 -0.0865 -0.3315 389 PRO C C   
9264  O O   . PRO C 380 ? 0.7578 1.3537 0.7232 -0.4433 -0.0936 -0.3244 389 PRO C O   
9265  C CB  . PRO C 380 ? 0.7578 1.4259 0.7113 -0.4444 -0.1025 -0.3448 389 PRO C CB  
9266  C CG  . PRO C 380 ? 0.8017 1.4419 0.7408 -0.4824 -0.1219 -0.3451 389 PRO C CG  
9267  C CD  . PRO C 380 ? 0.8440 1.4075 0.7524 -0.4770 -0.1323 -0.3655 389 PRO C CD  
9268  N N   . LYS C 381 ? 0.6846 1.3400 0.6715 -0.3986 -0.0703 -0.3213 390 LYS C N   
9269  C CA  . LYS C 381 ? 0.6566 1.3217 0.6633 -0.3969 -0.0606 -0.3019 390 LYS C CA  
9270  C C   . LYS C 381 ? 0.6545 1.2723 0.6569 -0.3776 -0.0546 -0.3053 390 LYS C C   
9271  O O   . LYS C 381 ? 0.6242 1.2566 0.6422 -0.3591 -0.0418 -0.2939 390 LYS C O   
9272  C CB  . LYS C 381 ? 0.6722 1.3405 0.6828 -0.4287 -0.0695 -0.2898 390 LYS C CB  
9273  C CG  . LYS C 381 ? 0.6679 1.4018 0.6933 -0.4456 -0.0705 -0.2763 390 LYS C CG  
9274  C CD  . LYS C 381 ? 0.6545 1.4360 0.7049 -0.4300 -0.0552 -0.2557 390 LYS C CD  
9275  C CE  . LYS C 381 ? 0.6541 1.4882 0.7193 -0.4519 -0.0572 -0.2361 390 LYS C CE  
9276  N NZ  . LYS C 381 ? 0.6694 1.5543 0.7366 -0.4619 -0.0618 -0.2364 390 LYS C NZ  
9277  N N   . TYR C 382 ? 0.6911 1.2513 0.6710 -0.3810 -0.0642 -0.3206 391 TYR C N   
9278  C CA  . TYR C 382 ? 0.6858 1.2041 0.6605 -0.3598 -0.0580 -0.3247 391 TYR C CA  
9279  C C   . TYR C 382 ? 0.7264 1.1964 0.6739 -0.3484 -0.0654 -0.3466 391 TYR C C   
9280  O O   . TYR C 382 ? 0.7773 1.2047 0.7024 -0.3648 -0.0801 -0.3582 391 TYR C O   
9281  C CB  . TYR C 382 ? 0.6870 1.1777 0.6671 -0.3705 -0.0580 -0.3129 391 TYR C CB  
9282  C CG  . TYR C 382 ? 0.6496 1.1325 0.6403 -0.3463 -0.0448 -0.3061 391 TYR C CG  
9283  C CD1 . TYR C 382 ? 0.6034 1.1320 0.6151 -0.3311 -0.0320 -0.2931 391 TYR C CD1 
9284  C CD2 . TYR C 382 ? 0.6671 1.0961 0.6456 -0.3389 -0.0462 -0.3120 391 TYR C CD2 
9285  C CE1 . TYR C 382 ? 0.5755 1.0959 0.5958 -0.3108 -0.0215 -0.2860 391 TYR C CE1 
9286  C CE2 . TYR C 382 ? 0.6310 1.0553 0.6198 -0.3177 -0.0345 -0.3047 391 TYR C CE2 
9287  C CZ  . TYR C 382 ? 0.5843 1.0545 0.5940 -0.3047 -0.0225 -0.2916 391 TYR C CZ  
9288  O OH  . TYR C 382 ? 0.5542 1.0203 0.5732 -0.2855 -0.0124 -0.2835 391 TYR C OH  
9289  N N   . ASP C 383 ? 0.7067 1.1842 0.6550 -0.3197 -0.0557 -0.3517 392 ASP C N   
9290  C CA  . ASP C 383 ? 0.7395 1.1709 0.6636 -0.3019 -0.0595 -0.3699 392 ASP C CA  
9291  C C   . ASP C 383 ? 0.7328 1.1263 0.6587 -0.2953 -0.0553 -0.3638 392 ASP C C   
9292  O O   . ASP C 383 ? 0.6937 1.1069 0.6417 -0.2897 -0.0439 -0.3471 392 ASP C O   
9293  C CB  . ASP C 383 ? 0.7280 1.1829 0.6482 -0.2745 -0.0529 -0.3793 392 ASP C CB  
9294  C CG  . ASP C 383 ? 0.6890 1.2079 0.6338 -0.2691 -0.0421 -0.3656 392 ASP C CG  
9295  O OD1 . ASP C 383 ? 0.6630 1.2026 0.6309 -0.2682 -0.0323 -0.3469 392 ASP C OD1 
9296  O OD2 . ASP C 383 ? 0.6913 1.2369 0.6298 -0.2645 -0.0443 -0.3745 392 ASP C OD2 
9297  N N   . CYS C 384 ? 0.7718 1.1086 0.6716 -0.2945 -0.0654 -0.3786 393 CYS C N   
9298  C CA  . CYS C 384 ? 0.7871 1.0791 0.6822 -0.3085 -0.0710 -0.3737 393 CYS C CA  
9299  C C   . CYS C 384 ? 0.8039 1.0461 0.6779 -0.2855 -0.0717 -0.3867 393 CYS C C   
9300  O O   . CYS C 384 ? 0.8457 1.0579 0.6917 -0.2776 -0.0815 -0.4062 393 CYS C O   
9301  C CB  . CYS C 384 ? 0.8298 1.1019 0.7090 -0.3399 -0.0887 -0.3794 393 CYS C CB  
9302  S SG  . CYS C 384 ? 0.8863 1.1193 0.7645 -0.3703 -0.0985 -0.3675 393 CYS C SG  
9303  N N   . LYS C 385 ? 0.7740 1.0094 0.6604 -0.2728 -0.0614 -0.3762 394 LYS C N   
9304  C CA  . LYS C 385 ? 0.7891 0.9888 0.6586 -0.2462 -0.0595 -0.3869 394 LYS C CA  
9305  C C   . LYS C 385 ? 0.8461 0.9757 0.6828 -0.2520 -0.0750 -0.4016 394 LYS C C   
9306  O O   . LYS C 385 ? 0.8630 0.9636 0.6988 -0.2753 -0.0826 -0.3947 394 LYS C O   
9307  C CB  . LYS C 385 ? 0.7473 0.9597 0.6387 -0.2322 -0.0452 -0.3709 394 LYS C CB  
9308  C CG  . LYS C 385 ? 0.7147 0.9912 0.6360 -0.2294 -0.0324 -0.3554 394 LYS C CG  
9309  C CD  . LYS C 385 ? 0.7421 1.0329 0.6812 -0.2104 -0.0191 -0.3420 394 LYS C CD  
9310  C CE  . LYS C 385 ? 0.7544 1.0351 0.7095 -0.2223 -0.0153 -0.3251 394 LYS C CE  
9311  N NZ  . LYS C 385 ? 0.7850 1.0157 0.7291 -0.2161 -0.0168 -0.3270 394 LYS C NZ  
9312  N N   . ILE C 386 ? 0.8750 0.9789 0.6839 -0.2291 -0.0798 -0.4214 395 ILE C N   
9313  C CA  . ILE C 386 ? 0.9425 0.9811 0.7113 -0.2305 -0.0979 -0.4419 395 ILE C CA  
9314  C C   . ILE C 386 ? 0.9662 0.9815 0.7123 -0.1925 -0.0952 -0.4570 395 ILE C C   
9315  O O   . ILE C 386 ? 0.9323 0.9922 0.6908 -0.1684 -0.0821 -0.4553 395 ILE C O   
9316  C CB  . ILE C 386 ? 0.9661 1.0169 0.7197 -0.2403 -0.1087 -0.4557 395 ILE C CB  
9317  C CG1 . ILE C 386 ? 0.9783 1.0371 0.7423 -0.2802 -0.1179 -0.4456 395 ILE C CG1 
9318  C CG2 . ILE C 386 ? 1.0335 1.0281 0.7408 -0.2261 -0.1249 -0.4825 395 ILE C CG2 
9319  C CD1 . ILE C 386 ? 1.0183 1.0971 0.7701 -0.2898 -0.1276 -0.4580 395 ILE C CD1 
9320  N N   . MET C 387 ? 1.0297 0.9772 0.7409 -0.1856 -0.1081 -0.4717 396 MET C N   
9321  C CA  . MET C 387 ? 1.0649 0.9976 0.7476 -0.1479 -0.1085 -0.4912 396 MET C CA  
9322  C C   . MET C 387 ? 1.1471 1.0223 0.7821 -0.1459 -0.1296 -0.5171 396 MET C C   
9323  O O   . MET C 387 ? 1.1961 1.0243 0.8149 -0.1754 -0.1469 -0.5201 396 MET C O   
9324  C CB  . MET C 387 ? 1.0643 0.9779 0.7463 -0.1230 -0.1000 -0.4872 396 MET C CB  
9325  C CG  . MET C 387 ? 1.1414 0.9776 0.7973 -0.1307 -0.1138 -0.4924 396 MET C CG  
9326  S SD  . MET C 387 ? 1.2013 1.0234 0.8556 -0.0948 -0.1021 -0.4889 396 MET C SD  
9327  C CE  . MET C 387 ? 1.0908 1.0010 0.7996 -0.0921 -0.0771 -0.4629 396 MET C CE  
9328  N N   . THR C 388 ? 1.1654 1.0439 0.7765 -0.1110 -0.1290 -0.5352 397 THR C N   
9329  C CA  . THR C 388 ? 1.2316 1.0714 0.7993 -0.1065 -0.1477 -0.5607 397 THR C CA  
9330  C C   . THR C 388 ? 1.3044 1.0751 0.8243 -0.0763 -0.1592 -0.5821 397 THR C C   
9331  O O   . THR C 388 ? 1.2944 1.0762 0.8144 -0.0420 -0.1474 -0.5820 397 THR C O   
9332  C CB  . THR C 388 ? 1.2022 1.1060 0.7767 -0.0904 -0.1397 -0.5667 397 THR C CB  
9333  O OG1 . THR C 388 ? 1.1594 1.1088 0.7651 -0.1237 -0.1371 -0.5527 397 THR C OG1 
9334  C CG2 . THR C 388 ? 1.2812 1.1475 0.8060 -0.0721 -0.1566 -0.5962 397 THR C CG2 
9335  N N   . SER C 389 ? 1.3812 1.0806 0.8590 -0.0890 -0.1831 -0.6000 398 SER C N   
9336  C CA  . SER C 389 ? 1.4604 1.0935 0.8846 -0.0559 -0.1967 -0.6252 398 SER C CA  
9337  C C   . SER C 389 ? 1.5333 1.1284 0.9123 -0.0570 -0.2187 -0.6511 398 SER C C   
9338  O O   . SER C 389 ? 1.5587 1.1319 0.9331 -0.0956 -0.2345 -0.6509 398 SER C O   
9339  C CB  . SER C 389 ? 1.5048 1.0599 0.9094 -0.0622 -0.2076 -0.6236 398 SER C CB  
9340  O OG  . SER C 389 ? 1.5970 1.0781 0.9421 -0.0347 -0.2263 -0.6509 398 SER C OG  
9341  N N   . LYS C 390 ? 1.5712 1.1587 0.9152 -0.0134 -0.2203 -0.6732 399 LYS C N   
9342  C CA  . LYS C 390 ? 1.6519 1.1935 0.9449 -0.0077 -0.2427 -0.7009 399 LYS C CA  
9343  C C   . LYS C 390 ? 1.7438 1.1740 0.9875 -0.0194 -0.2701 -0.7144 399 LYS C C   
9344  O O   . LYS C 390 ? 1.8054 1.1847 1.0147 -0.0418 -0.2947 -0.7293 399 LYS C O   
9345  C CB  . LYS C 390 ? 1.6694 1.2396 0.9394 0.0465  -0.2350 -0.7196 399 LYS C CB  
9346  C CG  . LYS C 390 ? 1.6201 1.2818 0.9171 0.0515  -0.2208 -0.7167 399 LYS C CG  
9347  C CD  . LYS C 390 ? 1.7237 1.3537 0.9786 0.0454  -0.2431 -0.7417 399 LYS C CD  
9348  C CE  . LYS C 390 ? 1.7062 1.4158 0.9716 0.0630  -0.2324 -0.7468 399 LYS C CE  
9349  N NZ  . LYS C 390 ? 1.7691 1.4405 0.9878 0.0589  -0.2563 -0.7736 399 LYS C NZ  
9350  N N   . THR C 391 ? 1.7478 1.1416 0.9894 -0.0068 -0.2664 -0.7075 400 THR C N   
9351  C CA  . THR C 391 ? 1.8420 1.1271 1.0324 -0.0073 -0.2910 -0.7211 400 THR C CA  
9352  C C   . THR C 391 ? 1.8286 1.0784 1.0393 -0.0534 -0.2972 -0.6992 400 THR C C   
9353  O O   . THR C 391 ? 1.7433 1.0484 1.0066 -0.0671 -0.2766 -0.6732 400 THR C O   
9354  C CB  . THR C 391 ? 1.8741 1.1320 1.0368 0.0464  -0.2854 -0.7323 400 THR C CB  
9355  O OG1 . THR C 391 ? 1.8190 1.1647 1.0070 0.0842  -0.2602 -0.7301 400 THR C OG1 
9356  C CG2 . THR C 391 ? 2.0045 1.1613 1.0885 0.0716  -0.3146 -0.7658 400 THR C CG2 
9357  N N   . ASP C 392 ? 1.9138 1.0700 1.0801 -0.0764 -0.3270 -0.7101 401 ASP C N   
9358  C CA  . ASP C 392 ? 1.9200 1.0296 1.0954 -0.1182 -0.3373 -0.6913 401 ASP C CA  
9359  C C   . ASP C 392 ? 1.8787 0.9928 1.0745 -0.0971 -0.3195 -0.6769 401 ASP C C   
9360  O O   . ASP C 392 ? 1.9134 0.9986 1.0798 -0.0513 -0.3175 -0.6914 401 ASP C O   
9361  C CB  . ASP C 392 ? 2.0418 1.0358 1.1533 -0.1336 -0.3742 -0.7093 401 ASP C CB  
9362  C CG  . ASP C 392 ? 2.0923 1.0765 1.1907 -0.1735 -0.3955 -0.7153 401 ASP C CG  
9363  O OD1 . ASP C 392 ? 2.0890 1.1403 1.2043 -0.1692 -0.3858 -0.7201 401 ASP C OD1 
9364  O OD2 . ASP C 392 ? 2.1754 1.0828 1.2446 -0.2100 -0.4232 -0.7148 401 ASP C OD2 
9365  N N   . VAL C 393 ? 1.8041 0.9586 1.0510 -0.1302 -0.3063 -0.6478 402 VAL C N   
9366  C CA  . VAL C 393 ? 1.7612 0.9186 1.0313 -0.1198 -0.2910 -0.6304 402 VAL C CA  
9367  C C   . VAL C 393 ? 1.7682 0.8850 1.0466 -0.1691 -0.3043 -0.6115 402 VAL C C   
9368  O O   . VAL C 393 ? 1.7395 0.8896 1.0446 -0.2115 -0.3066 -0.5976 402 VAL C O   
9369  C CB  . VAL C 393 ? 1.6475 0.9105 0.9803 -0.1128 -0.2582 -0.6094 402 VAL C CB  
9370  C CG1 . VAL C 393 ? 1.6195 0.8833 0.9768 -0.1082 -0.2445 -0.5900 402 VAL C CG1 
9371  C CG2 . VAL C 393 ? 1.6311 0.9455 0.9611 -0.0671 -0.2438 -0.6242 402 VAL C CG2 
9372  N N   . SER C 394 ? 1.8033 0.8517 1.0594 -0.1639 -0.3132 -0.6098 403 SER C N   
9373  C CA  . SER C 394 ? 1.8117 0.8220 1.0753 -0.2110 -0.3262 -0.5901 403 SER C CA  
9374  C C   . SER C 394 ? 1.7426 0.7825 1.0446 -0.2042 -0.3047 -0.5675 403 SER C C   
9375  O O   . SER C 394 ? 1.7441 0.7763 1.0361 -0.1613 -0.2942 -0.5752 403 SER C O   
9376  C CB  . SER C 394 ? 1.9309 0.8224 1.1298 -0.2170 -0.3601 -0.6063 403 SER C CB  
9377  O OG  . SER C 394 ? 2.0121 0.8623 1.1592 -0.1911 -0.3766 -0.6377 403 SER C OG  
9378  N N   . SER C 395 ? 1.6834 0.7602 1.0289 -0.2446 -0.2977 -0.5397 404 SER C N   
9379  C CA  . SER C 395 ? 1.6483 0.7268 1.0185 -0.2449 -0.2853 -0.5188 404 SER C CA  
9380  C C   . SER C 395 ? 1.6050 0.7099 1.0134 -0.2956 -0.2847 -0.4892 404 SER C C   
9381  O O   . SER C 395 ? 1.6171 0.7261 1.0272 -0.3350 -0.2983 -0.4842 404 SER C O   
9382  C CB  . SER C 395 ? 1.5763 0.7181 0.9766 -0.2023 -0.2556 -0.5160 404 SER C CB  
9383  O OG  . SER C 395 ? 1.4927 0.7193 0.9513 -0.2196 -0.2334 -0.4916 404 SER C OG  
9384  N N   . SER C 396 ? 1.5540 0.6781 0.9921 -0.2936 -0.2692 -0.4692 405 SER C N   
9385  C CA  . SER C 396 ? 1.5135 0.6658 0.9874 -0.3365 -0.2668 -0.4406 405 SER C CA  
9386  C C   . SER C 396 ? 1.4163 0.6510 0.9450 -0.3269 -0.2366 -0.4199 405 SER C C   
9387  O O   . SER C 396 ? 1.3884 0.6386 0.9233 -0.2874 -0.2195 -0.4246 405 SER C O   
9388  C CB  . SER C 396 ? 1.5810 0.6508 1.0270 -0.3566 -0.2874 -0.4337 405 SER C CB  
9389  O OG  . SER C 396 ? 1.5249 0.6309 1.0105 -0.3834 -0.2774 -0.4044 405 SER C OG  
9390  N N   . VAL C 397 ? 1.3679 0.6547 0.9343 -0.3635 -0.2313 -0.3967 406 VAL C N   
9391  C CA  . VAL C 397 ? 1.2775 0.6473 0.8956 -0.3592 -0.2047 -0.3769 406 VAL C CA  
9392  C C   . VAL C 397 ? 1.2595 0.6409 0.9019 -0.3956 -0.2056 -0.3495 406 VAL C C   
9393  O O   . VAL C 397 ? 1.2763 0.6631 0.9211 -0.4345 -0.2185 -0.3399 406 VAL C O   
9394  C CB  . VAL C 397 ? 1.2213 0.6683 0.8666 -0.3635 -0.1937 -0.3768 406 VAL C CB  
9395  C CG1 . VAL C 397 ? 1.1426 0.6663 0.8331 -0.3461 -0.1660 -0.3624 406 VAL C CG1 
9396  C CG2 . VAL C 397 ? 1.2614 0.6945 0.8777 -0.3406 -0.2000 -0.4038 406 VAL C CG2 
9397  N N   . ILE C 398 ? 1.2269 0.6181 0.8888 -0.3833 -0.1914 -0.3358 407 ILE C N   
9398  C CA  . ILE C 398 ? 1.2178 0.6164 0.8993 -0.4158 -0.1931 -0.3101 407 ILE C CA  
9399  C C   . ILE C 398 ? 1.1442 0.6317 0.8732 -0.4265 -0.1742 -0.2903 407 ILE C C   
9400  O O   . ILE C 398 ? 1.0878 0.6240 0.8410 -0.3987 -0.1529 -0.2900 407 ILE C O   
9401  C CB  . ILE C 398 ? 1.2290 0.5858 0.9037 -0.4018 -0.1908 -0.3038 407 ILE C CB  
9402  C CG1 . ILE C 398 ? 1.3179 0.5778 0.9419 -0.4019 -0.2153 -0.3190 407 ILE C CG1 
9403  C CG2 . ILE C 398 ? 1.1966 0.5791 0.8994 -0.4318 -0.1874 -0.2749 407 ILE C CG2 
9404  C CD1 . ILE C 398 ? 1.3603 0.5730 0.9728 -0.3855 -0.2146 -0.3149 407 ILE C CD1 
9405  N N   . THR C 399 ? 1.1516 0.6592 0.8925 -0.4670 -0.1829 -0.2727 408 THR C N   
9406  C CA  . THR C 399 ? 1.0893 0.6816 0.8720 -0.4789 -0.1674 -0.2537 408 THR C CA  
9407  C C   . THR C 399 ? 1.0704 0.6798 0.8753 -0.4937 -0.1614 -0.2280 408 THR C C   
9408  O O   . THR C 399 ? 1.1147 0.6693 0.9031 -0.4996 -0.1708 -0.2232 408 THR C O   
9409  C CB  . THR C 399 ? 1.1004 0.7198 0.8848 -0.5125 -0.1792 -0.2503 408 THR C CB  
9410  O OG1 . THR C 399 ? 1.1727 0.7429 0.9363 -0.5497 -0.2024 -0.2415 408 THR C OG1 
9411  C CG2 . THR C 399 ? 1.1211 0.7314 0.8855 -0.4979 -0.1842 -0.2754 408 THR C CG2 
9412  N N   . SER C 400 ? 1.0108 0.6976 0.8521 -0.4990 -0.1462 -0.2115 409 SER C N   
9413  C CA  . SER C 400 ? 0.9862 0.7036 0.8522 -0.5091 -0.1374 -0.1867 409 SER C CA  
9414  C C   . SER C 400 ? 1.0370 0.7205 0.8910 -0.5478 -0.1566 -0.1711 409 SER C C   
9415  O O   . SER C 400 ? 1.0411 0.7120 0.9000 -0.5523 -0.1551 -0.1558 409 SER C O   
9416  C CB  . SER C 400 ? 0.9245 0.7303 0.8257 -0.5138 -0.1229 -0.1723 409 SER C CB  
9417  O OG  . SER C 400 ? 0.8935 0.7330 0.8060 -0.4815 -0.1068 -0.1850 409 SER C OG  
9418  N N   . LEU C 401 ? 1.0779 0.7471 0.9156 -0.5769 -0.1753 -0.1744 410 LEU C N   
9419  C CA  . LEU C 401 ? 1.1175 0.7783 0.9517 -0.6215 -0.1932 -0.1539 410 LEU C CA  
9420  C C   . LEU C 401 ? 1.2031 0.7837 0.9955 -0.6446 -0.2220 -0.1660 410 LEU C C   
9421  O O   . LEU C 401 ? 1.2451 0.8111 1.0296 -0.6862 -0.2413 -0.1496 410 LEU C O   
9422  C CB  . LEU C 401 ? 1.0752 0.8237 0.9402 -0.6437 -0.1872 -0.1362 410 LEU C CB  
9423  C CG  . LEU C 401 ? 1.0473 0.8476 0.9399 -0.6641 -0.1811 -0.1047 410 LEU C CG  
9424  C CD1 . LEU C 401 ? 1.0173 0.8280 0.9265 -0.6317 -0.1605 -0.1004 410 LEU C CD1 
9425  C CD2 . LEU C 401 ? 0.9965 0.8869 0.9171 -0.6796 -0.1743 -0.0905 410 LEU C CD2 
9426  N N   . GLY C 402 ? 1.2274 0.7569 0.9921 -0.6166 -0.2252 -0.1943 411 GLY C N   
9427  C CA  . GLY C 402 ? 1.3049 0.7468 1.0234 -0.6276 -0.2519 -0.2112 411 GLY C CA  
9428  C C   . GLY C 402 ? 1.3083 0.7131 1.0037 -0.5835 -0.2470 -0.2423 411 GLY C C   
9429  O O   . GLY C 402 ? 1.2665 0.6855 0.9746 -0.5458 -0.2267 -0.2472 411 GLY C O   
9430  N N   . ALA C 403 ? 1.3545 0.7157 1.0161 -0.5880 -0.2656 -0.2627 412 ALA C N   
9431  C CA  . ALA C 403 ? 1.3609 0.6909 0.9981 -0.5464 -0.2624 -0.2928 412 ALA C CA  
9432  C C   . ALA C 403 ? 1.3908 0.7156 1.0072 -0.5555 -0.2766 -0.3108 412 ALA C C   
9433  O O   . ALA C 403 ? 1.4332 0.7438 1.0385 -0.5966 -0.2975 -0.3034 412 ALA C O   
9434  C CB  . ALA C 403 ? 1.4249 0.6627 1.0224 -0.5289 -0.2750 -0.3047 412 ALA C CB  
9435  N N   . ILE C 404 ? 1.3719 0.7107 0.9835 -0.5181 -0.2655 -0.3333 413 ILE C N   
9436  C CA  . ILE C 404 ? 1.4091 0.7347 0.9949 -0.5186 -0.2788 -0.3550 413 ILE C CA  
9437  C C   . ILE C 404 ? 1.4878 0.7268 1.0224 -0.4893 -0.2931 -0.3828 413 ILE C C   
9438  O O   . ILE C 404 ? 1.4856 0.7005 1.0138 -0.4547 -0.2831 -0.3887 413 ILE C O   
9439  C CB  . ILE C 404 ? 1.3345 0.7409 0.9490 -0.4959 -0.2570 -0.3615 413 ILE C CB  
9440  C CG1 . ILE C 404 ? 1.2578 0.7526 0.9216 -0.5198 -0.2420 -0.3353 413 ILE C CG1 
9441  C CG2 . ILE C 404 ? 1.3739 0.7642 0.9595 -0.4957 -0.2717 -0.3845 413 ILE C CG2 
9442  C CD1 . ILE C 404 ? 1.2043 0.7753 0.8933 -0.5045 -0.2250 -0.3404 413 ILE C CD1 
9443  N N   . VAL C 405 ? 1.5613 0.7544 1.0580 -0.5018 -0.3167 -0.4002 414 VAL C N   
9444  C CA  . VAL C 405 ? 1.6452 0.7551 1.0886 -0.4720 -0.3319 -0.4286 414 VAL C CA  
9445  C C   . VAL C 405 ? 1.6794 0.7874 1.0986 -0.4697 -0.3435 -0.4513 414 VAL C C   
9446  O O   . VAL C 405 ? 1.7099 0.8171 1.1234 -0.5096 -0.3615 -0.4471 414 VAL C O   
9447  C CB  . VAL C 405 ? 1.7346 0.7443 1.1372 -0.4906 -0.3587 -0.4267 414 VAL C CB  
9448  C CG1 . VAL C 405 ? 1.7585 0.7690 1.1702 -0.5507 -0.3766 -0.4030 414 VAL C CG1 
9449  C CG2 . VAL C 405 ? 1.8350 0.7520 1.1735 -0.4686 -0.3825 -0.4584 414 VAL C CG2 
9450  N N   . SER C 406 ? 1.6757 0.7876 1.0818 -0.4223 -0.3326 -0.4744 415 SER C N   
9451  C CA  . SER C 406 ? 1.7091 0.8191 1.0897 -0.4114 -0.3416 -0.4985 415 SER C CA  
9452  C C   . SER C 406 ? 1.8151 0.8237 1.1307 -0.3855 -0.3641 -0.5266 415 SER C C   
9453  O O   . SER C 406 ? 1.8191 0.8158 1.1222 -0.3383 -0.3528 -0.5404 415 SER C O   
9454  C CB  . SER C 406 ? 1.6245 0.8196 1.0381 -0.3751 -0.3123 -0.5032 415 SER C CB  
9455  O OG  . SER C 406 ? 1.5351 0.8180 1.0060 -0.3953 -0.2916 -0.4773 415 SER C OG  
9456  N N   . CYS C 407 ? 1.9082 0.8431 1.1810 -0.4159 -0.3967 -0.5344 416 CYS C N   
9457  C CA  . CYS C 407 ? 2.0175 0.8471 1.2231 -0.3925 -0.4214 -0.5614 416 CYS C CA  
9458  C C   . CYS C 407 ? 2.0588 0.8776 1.2303 -0.3815 -0.4347 -0.5887 416 CYS C C   
9459  O O   . CYS C 407 ? 2.0911 0.9026 1.2540 -0.4223 -0.4545 -0.5872 416 CYS C O   
9460  C CB  . CYS C 407 ? 2.1041 0.8440 1.2774 -0.4331 -0.4527 -0.5524 416 CYS C CB  
9461  S SG  . CYS C 407 ? 2.2291 0.8453 1.3351 -0.3943 -0.4717 -0.5744 416 CYS C SG  
9462  N N   . TYR C 408 ? 2.0623 0.8814 1.2136 -0.3264 -0.4243 -0.6131 417 TYR C N   
9463  C CA  . TYR C 408 ? 2.0887 0.9119 1.2119 -0.3083 -0.4319 -0.6395 417 TYR C CA  
9464  C C   . TYR C 408 ? 2.1793 0.9202 1.2358 -0.2598 -0.4473 -0.6730 417 TYR C C   
9465  O O   . TYR C 408 ? 2.2020 0.9002 1.2413 -0.2293 -0.4444 -0.6760 417 TYR C O   
9466  C CB  . TYR C 408 ? 1.9807 0.9207 1.1564 -0.2904 -0.3993 -0.6341 417 TYR C CB  
9467  C CG  . TYR C 408 ? 1.9086 0.9260 1.1376 -0.3385 -0.3909 -0.6085 417 TYR C CG  
9468  C CD1 . TYR C 408 ? 1.8003 0.9106 1.0920 -0.3373 -0.3594 -0.5849 417 TYR C CD1 
9469  C CD2 . TYR C 408 ? 1.9626 0.9597 1.1771 -0.3848 -0.4155 -0.6077 417 TYR C CD2 
9470  C CE1 . TYR C 408 ? 1.7456 0.9276 1.0839 -0.3779 -0.3516 -0.5619 417 TYR C CE1 
9471  C CE2 . TYR C 408 ? 1.9009 0.9745 1.1645 -0.4273 -0.4073 -0.5833 417 TYR C CE2 
9472  C CZ  . TYR C 408 ? 1.7928 0.9587 1.1177 -0.4219 -0.3749 -0.5609 417 TYR C CZ  
9473  O OH  . TYR C 408 ? 1.7425 0.9827 1.1127 -0.4602 -0.3671 -0.5376 417 TYR C OH  
9474  N N   . GLY C 409 ? 2.2331 0.9535 1.2512 -0.2521 -0.4638 -0.6982 418 GLY C N   
9475  C CA  . GLY C 409 ? 2.3298 0.9713 1.2790 -0.2062 -0.4813 -0.7323 418 GLY C CA  
9476  C C   . GLY C 409 ? 2.4366 0.9565 1.3320 -0.2129 -0.5107 -0.7377 418 GLY C C   
9477  O O   . GLY C 409 ? 2.4822 0.9515 1.3673 -0.2648 -0.5353 -0.7262 418 GLY C O   
9478  N N   . LYS C 410 ? 2.4772 0.9532 1.3392 -0.1601 -0.5079 -0.7536 419 LYS C N   
9479  C CA  . LYS C 410 ? 2.5898 0.9440 1.3925 -0.1561 -0.5363 -0.7630 419 LYS C CA  
9480  C C   . LYS C 410 ? 2.5597 0.9022 1.3923 -0.1812 -0.5305 -0.7335 419 LYS C C   
9481  O O   . LYS C 410 ? 2.6471 0.8886 1.4346 -0.1862 -0.5552 -0.7367 419 LYS C O   
9482  C CB  . LYS C 410 ? 2.6509 0.9631 1.4018 -0.0846 -0.5361 -0.7933 419 LYS C CB  
9483  C CG  . LYS C 410 ? 2.7740 1.0223 1.4550 -0.0639 -0.5637 -0.8293 419 LYS C CG  
9484  C CD  . LYS C 410 ? 2.9095 1.0703 1.5216 -0.0034 -0.5763 -0.8567 419 LYS C CD  
9485  C CE  . LYS C 410 ? 3.0612 1.1163 1.5879 0.0064  -0.6160 -0.8913 419 LYS C CE  
9486  N NZ  . LYS C 410 ? 3.0632 1.1789 1.5924 0.0158  -0.6111 -0.9081 419 LYS C NZ  
9487  N N   . THR C 411 ? 2.4397 0.8826 1.3461 -0.1965 -0.4989 -0.7050 420 THR C N   
9488  C CA  . THR C 411 ? 2.4050 0.8453 1.3397 -0.2059 -0.4881 -0.6798 420 THR C CA  
9489  C C   . THR C 411 ? 2.4413 0.8329 1.3775 -0.2698 -0.5110 -0.6571 420 THR C C   
9490  O O   . THR C 411 ? 2.4457 0.8503 1.3902 -0.3164 -0.5242 -0.6502 420 THR C O   
9491  C CB  . THR C 411 ? 2.2705 0.8305 1.2785 -0.1911 -0.4458 -0.6594 420 THR C CB  
9492  O OG1 . THR C 411 ? 2.2024 0.8478 1.2385 -0.1881 -0.4306 -0.6643 420 THR C OG1 
9493  C CG2 . THR C 411 ? 2.2589 0.8176 1.2563 -0.1298 -0.4286 -0.6699 420 THR C CG2 
9494  N N   . LYS C 412 ? 2.4725 0.8075 1.3982 -0.2707 -0.5166 -0.6457 421 LYS C N   
9495  C CA  . LYS C 412 ? 2.5131 0.7985 1.4382 -0.3285 -0.5384 -0.6222 421 LYS C CA  
9496  C C   . LYS C 412 ? 2.4092 0.7737 1.4042 -0.3517 -0.5115 -0.5865 421 LYS C C   
9497  O O   . LYS C 412 ? 2.3614 0.7574 1.3790 -0.3156 -0.4866 -0.5819 421 LYS C O   
9498  C CB  . LYS C 412 ? 2.6314 0.7887 1.4912 -0.3160 -0.5670 -0.6333 421 LYS C CB  
9499  C CG  . LYS C 412 ? 2.7854 0.8368 1.5763 -0.3395 -0.6110 -0.6520 421 LYS C CG  
9500  C CD  . LYS C 412 ? 2.9438 0.8643 1.6623 -0.3141 -0.6386 -0.6688 421 LYS C CD  
9501  C CE  . LYS C 412 ? 3.0700 0.8921 1.7096 -0.3070 -0.6764 -0.7021 421 LYS C CE  
9502  N NZ  . LYS C 412 ? 3.1987 0.8987 1.7647 -0.2669 -0.6992 -0.7235 421 LYS C NZ  
9503  N N   . CYS C 413 ? 2.3793 0.7752 1.4065 -0.4113 -0.5175 -0.5609 422 CYS C N   
9504  C CA  . CYS C 413 ? 2.2810 0.7554 1.3741 -0.4348 -0.4929 -0.5264 422 CYS C CA  
9505  C C   . CYS C 413 ? 2.3125 0.7487 1.4068 -0.4939 -0.5144 -0.4990 422 CYS C C   
9506  O O   . CYS C 413 ? 2.3836 0.7707 1.4480 -0.5341 -0.5450 -0.4998 422 CYS C O   
9507  C CB  . CYS C 413 ? 2.1731 0.7704 1.3264 -0.4409 -0.4649 -0.5168 422 CYS C CB  
9508  S SG  . CYS C 413 ? 2.1447 0.7975 1.2999 -0.3771 -0.4402 -0.5461 422 CYS C SG  
9509  N N   . THR C 414 ? 2.2603 0.7237 1.3908 -0.4995 -0.4980 -0.4737 423 THR C N   
9510  C CA  . THR C 414 ? 2.3053 0.7159 1.4278 -0.5436 -0.5186 -0.4497 423 THR C CA  
9511  C C   . THR C 414 ? 2.2084 0.7086 1.3976 -0.5635 -0.4921 -0.4154 423 THR C C   
9512  O O   . THR C 414 ? 2.1458 0.6934 1.3654 -0.5264 -0.4626 -0.4132 423 THR C O   
9513  C CB  . THR C 414 ? 2.3758 0.6886 1.4522 -0.5118 -0.5299 -0.4604 423 THR C CB  
9514  O OG1 . THR C 414 ? 2.4754 0.6941 1.4826 -0.4898 -0.5570 -0.4934 423 THR C OG1 
9515  C CG2 . THR C 414 ? 2.4220 0.6849 1.4940 -0.5546 -0.5484 -0.4332 423 THR C CG2 
9516  N N   . ALA C 415 ? 2.2034 0.7255 1.4136 -0.6213 -0.5035 -0.3880 424 ALA C N   
9517  C CA  . ALA C 415 ? 2.1271 0.7171 1.3915 -0.6409 -0.4832 -0.3541 424 ALA C CA  
9518  C C   . ALA C 415 ? 2.1968 0.7095 1.4375 -0.6699 -0.5061 -0.3355 424 ALA C C   
9519  O O   . ALA C 415 ? 2.2827 0.7326 1.4895 -0.7119 -0.5396 -0.3310 424 ALA C O   
9520  C CB  . ALA C 415 ? 2.0609 0.7471 1.3729 -0.6815 -0.4748 -0.3329 424 ALA C CB  
9521  N N   . SER C 416 ? 2.1664 0.6821 1.4235 -0.6481 -0.4891 -0.3245 425 SER C N   
9522  C CA  . SER C 416 ? 2.2271 0.6756 1.4655 -0.6740 -0.5084 -0.3046 425 SER C CA  
9523  C C   . SER C 416 ? 2.1509 0.6832 1.4484 -0.7005 -0.4882 -0.2674 425 SER C C   
9524  O O   . SER C 416 ? 2.0495 0.6762 1.3965 -0.6789 -0.4548 -0.2625 425 SER C O   
9525  C CB  . SER C 416 ? 2.2734 0.6419 1.4734 -0.6256 -0.5094 -0.3232 425 SER C CB  
9526  O OG  . SER C 416 ? 2.3019 0.6349 1.4648 -0.5821 -0.5120 -0.3600 425 SER C OG  
9527  N N   . ASN C 417 ? 2.2052 0.7028 1.4960 -0.7469 -0.5093 -0.2409 426 ASN C N   
9528  C CA  . ASN C 417 ? 2.1466 0.7247 1.4908 -0.7767 -0.4933 -0.2036 426 ASN C CA  
9529  C C   . ASN C 417 ? 2.1336 0.7068 1.4901 -0.7469 -0.4753 -0.1955 426 ASN C C   
9530  O O   . ASN C 417 ? 2.1604 0.6758 1.4876 -0.7009 -0.4726 -0.2188 426 ASN C O   
9531  C CB  . ASN C 417 ? 2.2004 0.7561 1.5366 -0.8439 -0.5234 -0.1744 426 ASN C CB  
9532  C CG  . ASN C 417 ? 2.2843 0.7387 1.5818 -0.8563 -0.5478 -0.1641 426 ASN C CG  
9533  O OD1 . ASN C 417 ? 2.2608 0.6899 1.5549 -0.8182 -0.5346 -0.1692 426 ASN C OD1 
9534  N ND2 . ASN C 417 ? 2.3656 0.7619 1.6331 -0.9108 -0.5845 -0.1487 426 ASN C ND2 
9535  N N   . LYS C 418 ? 2.1027 0.7395 1.5021 -0.7744 -0.4638 -0.1614 427 LYS C N   
9536  C CA  . LYS C 418 ? 2.0930 0.7360 1.5106 -0.7576 -0.4478 -0.1453 427 LYS C CA  
9537  C C   . LYS C 418 ? 2.1729 0.7040 1.5402 -0.7292 -0.4624 -0.1609 427 LYS C C   
9538  O O   . LYS C 418 ? 2.1328 0.6658 1.5050 -0.6799 -0.4411 -0.1732 427 LYS C O   
9539  C CB  . LYS C 418 ? 2.0942 0.7752 1.5391 -0.8111 -0.4542 -0.1040 427 LYS C CB  
9540  C CG  . LYS C 418 ? 2.0110 0.8165 1.5212 -0.8107 -0.4207 -0.0805 427 LYS C CG  
9541  C CD  . LYS C 418 ? 2.0465 0.8672 1.5744 -0.8485 -0.4260 -0.0415 427 LYS C CD  
9542  C CE  . LYS C 418 ? 1.9581 0.8958 1.5461 -0.8413 -0.3926 -0.0199 427 LYS C CE  
9543  N NZ  . LYS C 418 ? 1.9018 0.8691 1.5081 -0.7827 -0.3607 -0.0392 427 LYS C NZ  
9544  N N   . ASN C 419 ? 2.2858 0.7213 1.6048 -0.7623 -0.4999 -0.1590 428 ASN C N   
9545  C CA  . ASN C 419 ? 2.3850 0.7007 1.6484 -0.7450 -0.5217 -0.1703 428 ASN C CA  
9546  C C   . ASN C 419 ? 2.4567 0.6904 1.6646 -0.7054 -0.5353 -0.2114 428 ASN C C   
9547  O O   . ASN C 419 ? 2.5467 0.6768 1.7033 -0.6860 -0.5542 -0.2239 428 ASN C O   
9548  C CB  . ASN C 419 ? 2.4709 0.7174 1.7071 -0.8020 -0.5576 -0.1442 428 ASN C CB  
9549  C CG  . ASN C 419 ? 2.4332 0.7441 1.6991 -0.8643 -0.5665 -0.1166 428 ASN C CG  
9550  O OD1 . ASN C 419 ? 2.3173 0.7213 1.6363 -0.8839 -0.5467 -0.0871 428 ASN C OD1 
9551  N ND2 . ASN C 419 ? 2.4962 0.7573 1.7263 -0.8953 -0.5973 -0.1256 428 ASN C ND2 
9552  N N   . ARG C 420 ? 2.4191 0.6993 1.6361 -0.6923 -0.5257 -0.2318 429 ARG C N   
9553  C CA  . ARG C 420 ? 2.4711 0.6894 1.6398 -0.6518 -0.5351 -0.2716 429 ARG C CA  
9554  C C   . ARG C 420 ? 2.5741 0.7086 1.6886 -0.6846 -0.5756 -0.2837 429 ARG C C   
9555  O O   . ARG C 420 ? 2.6179 0.7145 1.6960 -0.6538 -0.5827 -0.3168 429 ARG C O   
9556  C CB  . ARG C 420 ? 2.5099 0.6599 1.6443 -0.5959 -0.5315 -0.2908 429 ARG C CB  
9557  C CG  . ARG C 420 ? 2.4210 0.6518 1.6030 -0.5540 -0.4912 -0.2868 429 ARG C CG  
9558  C CD  . ARG C 420 ? 2.4397 0.6875 1.6136 -0.4944 -0.4731 -0.3200 429 ARG C CD  
9559  N NE  . ARG C 420 ? 2.3755 0.7189 1.6034 -0.4628 -0.4337 -0.3131 429 ARG C NE  
9560  C CZ  . ARG C 420 ? 2.3737 0.7163 1.6117 -0.4371 -0.4191 -0.3043 429 ARG C CZ  
9561  N NH1 . ARG C 420 ? 2.4515 0.7019 1.6496 -0.4375 -0.4397 -0.3009 429 ARG C NH1 
9562  N NH2 . ARG C 420 ? 2.2766 0.7105 1.5642 -0.4111 -0.3843 -0.2986 429 ARG C NH2 
9563  N N   . GLY C 421 ? 2.6170 0.7215 1.7240 -0.7457 -0.6031 -0.2575 430 GLY C N   
9564  C CA  . GLY C 421 ? 2.6843 0.7357 1.7527 -0.7870 -0.6390 -0.2638 430 GLY C CA  
9565  C C   . GLY C 421 ? 2.6145 0.7453 1.7075 -0.7793 -0.6235 -0.2798 430 GLY C C   
9566  O O   . GLY C 421 ? 2.5111 0.7584 1.6662 -0.7853 -0.5938 -0.2637 430 GLY C O   
9567  N N   . ILE C 422 ? 2.6710 0.7395 1.7146 -0.7634 -0.6429 -0.3123 431 ILE C N   
9568  C CA  . ILE C 422 ? 2.6076 0.7453 1.6696 -0.7493 -0.6281 -0.3312 431 ILE C CA  
9569  C C   . ILE C 422 ? 2.5956 0.7831 1.6793 -0.8117 -0.6413 -0.3111 431 ILE C C   
9570  O O   . ILE C 422 ? 2.6895 0.8008 1.7314 -0.8538 -0.6794 -0.3074 431 ILE C O   
9571  C CB  . ILE C 422 ? 2.6901 0.7383 1.6865 -0.7103 -0.6468 -0.3732 431 ILE C CB  
9572  C CG1 . ILE C 422 ? 2.6857 0.7107 1.6691 -0.6407 -0.6267 -0.3946 431 ILE C CG1 
9573  C CG2 . ILE C 422 ? 2.6511 0.7543 1.6563 -0.7090 -0.6420 -0.3912 431 ILE C CG2 
9574  C CD1 . ILE C 422 ? 2.8142 0.7065 1.7324 -0.6272 -0.6551 -0.4038 431 ILE C CD1 
9575  N N   . ILE C 423 ? 2.4875 0.7996 1.6335 -0.8182 -0.6119 -0.2980 432 ILE C N   
9576  C CA  . ILE C 423 ? 2.4845 0.8498 1.6519 -0.8772 -0.6242 -0.2777 432 ILE C CA  
9577  C C   . ILE C 423 ? 2.4942 0.8713 1.6464 -0.8733 -0.6308 -0.3031 432 ILE C C   
9578  O O   . ILE C 423 ? 2.5671 0.9053 1.6904 -0.9171 -0.6632 -0.3016 432 ILE C O   
9579  C CB  . ILE C 423 ? 2.3684 0.8678 1.6118 -0.8988 -0.5937 -0.2436 432 ILE C CB  
9580  C CG1 . ILE C 423 ? 2.3125 0.8434 1.5893 -0.8718 -0.5657 -0.2286 432 ILE C CG1 
9581  C CG2 . ILE C 423 ? 2.4045 0.9230 1.6567 -0.9719 -0.6182 -0.2111 432 ILE C CG2 
9582  C CD1 . ILE C 423 ? 2.2039 0.8716 1.5541 -0.8787 -0.5310 -0.2024 432 ILE C CD1 
9583  N N   . LYS C 424 ? 2.4213 0.8580 1.5957 -0.8232 -0.5999 -0.3243 433 LYS C N   
9584  C CA  . LYS C 424 ? 2.4192 0.8822 1.5867 -0.8170 -0.6014 -0.3465 433 LYS C CA  
9585  C C   . LYS C 424 ? 2.4602 0.8538 1.5796 -0.7582 -0.6031 -0.3875 433 LYS C C   
9586  O O   . LYS C 424 ? 2.4634 0.8197 1.5709 -0.7163 -0.5927 -0.3963 433 LYS C O   
9587  C CB  . LYS C 424 ? 2.2956 0.8983 1.5326 -0.8128 -0.5646 -0.3339 433 LYS C CB  
9588  C CG  . LYS C 424 ? 2.3083 0.9534 1.5462 -0.8185 -0.5668 -0.3493 433 LYS C CG  
9589  C CD  . LYS C 424 ? 2.2311 1.0098 1.5361 -0.8369 -0.5403 -0.3263 433 LYS C CD  
9590  C CE  . LYS C 424 ? 2.2387 1.0538 1.5407 -0.8341 -0.5413 -0.3456 433 LYS C CE  
9591  N NZ  . LYS C 424 ? 2.2196 1.1102 1.5537 -0.8865 -0.5461 -0.3210 433 LYS C NZ  
9592  N N   . THR C 425 ? 2.4956 0.8712 1.5851 -0.7554 -0.6176 -0.4121 434 THR C N   
9593  C CA  . THR C 425 ? 2.5307 0.8577 1.5784 -0.6974 -0.6165 -0.4515 434 THR C CA  
9594  C C   . THR C 425 ? 2.4931 0.8836 1.5525 -0.6915 -0.6085 -0.4679 434 THR C C   
9595  O O   . THR C 425 ? 2.5066 0.9174 1.5708 -0.7390 -0.6248 -0.4578 434 THR C O   
9596  C CB  . THR C 425 ? 2.6690 0.8512 1.6373 -0.6944 -0.6559 -0.4708 434 THR C CB  
9597  O OG1 . THR C 425 ? 2.7117 0.8530 1.6350 -0.6463 -0.6605 -0.5106 434 THR C OG1 
9598  C CG2 . THR C 425 ? 2.7594 0.8868 1.7008 -0.7627 -0.6965 -0.4556 434 THR C CG2 
9599  N N   . PHE C 426 ? 2.4499 0.8757 1.5152 -0.6341 -0.5834 -0.4917 435 PHE C N   
9600  C CA  . PHE C 426 ? 2.3681 0.9020 1.4774 -0.6278 -0.5588 -0.4934 435 PHE C CA  
9601  C C   . PHE C 426 ? 2.4131 0.9385 1.4916 -0.6163 -0.5703 -0.5220 435 PHE C C   
9602  O O   . PHE C 426 ? 2.4490 0.9342 1.4900 -0.5669 -0.5704 -0.5530 435 PHE C O   
9603  C CB  . PHE C 426 ? 2.2566 0.8761 1.4163 -0.5834 -0.5161 -0.4895 435 PHE C CB  
9604  C CG  . PHE C 426 ? 2.1668 0.8585 1.3861 -0.6104 -0.4961 -0.4531 435 PHE C CG  
9605  C CD1 . PHE C 426 ? 2.1341 0.8146 1.3658 -0.5915 -0.4822 -0.4414 435 PHE C CD1 
9606  C CD2 . PHE C 426 ? 2.1106 0.8797 1.3713 -0.6557 -0.4927 -0.4300 435 PHE C CD2 
9607  C CE1 . PHE C 426 ? 2.0453 0.7912 1.3299 -0.6162 -0.4647 -0.4081 435 PHE C CE1 
9608  C CE2 . PHE C 426 ? 2.0335 0.8701 1.3470 -0.6791 -0.4750 -0.3964 435 PHE C CE2 
9609  C CZ  . PHE C 426 ? 1.9978 0.8220 1.3229 -0.6592 -0.4610 -0.3857 435 PHE C CZ  
9610  N N   . SER C 427 ? 2.4059 0.9835 1.5064 -0.6610 -0.5767 -0.5094 436 SER C N   
9611  C CA  . SER C 427 ? 2.4609 1.0261 1.5306 -0.6655 -0.5945 -0.5321 436 SER C CA  
9612  C C   . SER C 427 ? 2.3830 1.0324 1.4798 -0.6207 -0.5636 -0.5487 436 SER C C   
9613  O O   . SER C 427 ? 2.3152 1.0556 1.4541 -0.6395 -0.5500 -0.5377 436 SER C O   
9614  C CB  . SER C 427 ? 2.4751 1.0656 1.5587 -0.7340 -0.6144 -0.5093 436 SER C CB  
9615  O OG  . SER C 427 ? 2.5686 1.1049 1.6021 -0.7474 -0.6455 -0.5318 436 SER C OG  
9616  N N   . ASN C 428 ? 2.3916 1.0126 1.4647 -0.5609 -0.5525 -0.5739 437 ASN C N   
9617  C CA  . ASN C 428 ? 2.3480 1.0220 1.4258 -0.5148 -0.5327 -0.5973 437 ASN C CA  
9618  C C   . ASN C 428 ? 2.2247 1.0272 1.3687 -0.5271 -0.5043 -0.5803 437 ASN C C   
9619  O O   . ASN C 428 ? 2.2087 1.0490 1.3513 -0.5210 -0.5031 -0.5946 437 ASN C O   
9620  C CB  . ASN C 428 ? 2.4585 1.0534 1.4675 -0.5053 -0.5641 -0.6314 437 ASN C CB  
9621  C CG  . ASN C 428 ? 2.4541 1.0731 1.4496 -0.4429 -0.5471 -0.6614 437 ASN C CG  
9622  O OD1 . ASN C 428 ? 2.4482 1.0742 1.4480 -0.3942 -0.5263 -0.6677 437 ASN C OD1 
9623  N ND2 . ASN C 428 ? 2.4839 1.1167 1.4622 -0.4449 -0.5570 -0.6793 437 ASN C ND2 
9624  N N   . GLY C 429 ? 2.1362 1.0042 1.3366 -0.5430 -0.4819 -0.5496 438 GLY C N   
9625  C CA  . GLY C 429 ? 2.0247 1.0108 1.2874 -0.5545 -0.4553 -0.5311 438 GLY C CA  
9626  C C   . GLY C 429 ? 1.9265 0.9785 1.2432 -0.5386 -0.4220 -0.5089 438 GLY C C   
9627  O O   . GLY C 429 ? 1.9199 0.9544 1.2313 -0.4955 -0.4081 -0.5178 438 GLY C O   
9628  N N   . CYS C 430 ? 1.8494 0.9782 1.2172 -0.5726 -0.4096 -0.4797 439 CYS C N   
9629  C CA  . CYS C 430 ? 1.7533 0.9440 1.1713 -0.5609 -0.3799 -0.4577 439 CYS C CA  
9630  C C   . CYS C 430 ? 1.7228 0.9464 1.1739 -0.6110 -0.3823 -0.4236 439 CYS C C   
9631  O O   . CYS C 430 ? 1.6915 0.9761 1.1676 -0.6423 -0.3824 -0.4104 439 CYS C O   
9632  C CB  . CYS C 430 ? 1.6643 0.9463 1.1198 -0.5283 -0.3495 -0.4615 439 CYS C CB  
9633  S SG  . CYS C 430 ? 1.5637 0.9592 1.0923 -0.5413 -0.3185 -0.4271 439 CYS C SG  
9634  N N   . ASP C 431 ? 1.7296 0.9147 1.1802 -0.6172 -0.3843 -0.4092 440 ASP C N   
9635  C CA  . ASP C 431 ? 1.7175 0.9210 1.1920 -0.6653 -0.3906 -0.3767 440 ASP C CA  
9636  C C   . ASP C 431 ? 1.6295 0.8803 1.1465 -0.6512 -0.3636 -0.3555 440 ASP C C   
9637  O O   . ASP C 431 ? 1.5984 0.8510 1.1200 -0.6068 -0.3443 -0.3665 440 ASP C O   
9638  C CB  . ASP C 431 ? 1.8329 0.9324 1.2597 -0.6956 -0.4256 -0.3766 440 ASP C CB  
9639  C CG  . ASP C 431 ? 1.9124 1.0050 1.3262 -0.7515 -0.4541 -0.3673 440 ASP C CG  
9640  O OD1 . ASP C 431 ? 1.9054 1.0515 1.3530 -0.7926 -0.4531 -0.3364 440 ASP C OD1 
9641  O OD2 . ASP C 431 ? 2.0169 1.0485 1.3845 -0.7545 -0.4787 -0.3905 440 ASP C OD2 
9642  N N   . TYR C 432 ? 1.5914 0.8791 1.1374 -0.6899 -0.3638 -0.3248 441 TYR C N   
9643  C CA  . TYR C 432 ? 1.5145 0.8460 1.0995 -0.6829 -0.3414 -0.3019 441 TYR C CA  
9644  C C   . TYR C 432 ? 1.5658 0.8407 1.1359 -0.7165 -0.3610 -0.2831 441 TYR C C   
9645  O O   . TYR C 432 ? 1.6358 0.8715 1.1813 -0.7570 -0.3889 -0.2787 441 TYR C O   
9646  C CB  . TYR C 432 ? 1.4304 0.8709 1.0662 -0.6993 -0.3230 -0.2800 441 TYR C CB  
9647  C CG  . TYR C 432 ? 1.3617 0.8559 1.0386 -0.6971 -0.3015 -0.2541 441 TYR C CG  
9648  C CD1 . TYR C 432 ? 1.2997 0.8365 1.0028 -0.6544 -0.2725 -0.2580 441 TYR C CD1 
9649  C CD2 . TYR C 432 ? 1.3691 0.8739 1.0586 -0.7376 -0.3105 -0.2251 441 TYR C CD2 
9650  C CE1 . TYR C 432 ? 1.2352 0.8198 0.9743 -0.6502 -0.2529 -0.2353 441 TYR C CE1 
9651  C CE2 . TYR C 432 ? 1.3154 0.8720 1.0418 -0.7332 -0.2902 -0.2016 441 TYR C CE2 
9652  C CZ  . TYR C 432 ? 1.2443 0.8387 0.9945 -0.6884 -0.2615 -0.2079 441 TYR C CZ  
9653  O OH  . TYR C 432 ? 1.1734 0.8160 0.9575 -0.6812 -0.2419 -0.1868 441 TYR C OH  
9654  N N   . VAL C 433 ? 1.5379 0.8083 1.1221 -0.7021 -0.3479 -0.2709 442 VAL C N   
9655  C CA  . VAL C 433 ? 1.5834 0.8135 1.1605 -0.7368 -0.3641 -0.2479 442 VAL C CA  
9656  C C   . VAL C 433 ? 1.5101 0.8085 1.1340 -0.7319 -0.3386 -0.2222 442 VAL C C   
9657  O O   . VAL C 433 ? 1.4394 0.8016 1.0942 -0.6995 -0.3112 -0.2258 442 VAL C O   
9658  C CB  . VAL C 433 ? 1.6644 0.7813 1.1919 -0.7220 -0.3827 -0.2639 442 VAL C CB  
9659  C CG1 . VAL C 433 ? 1.7649 0.8033 1.2404 -0.7389 -0.4154 -0.2837 442 VAL C CG1 
9660  C CG2 . VAL C 433 ? 1.6315 0.7396 1.1571 -0.6637 -0.3612 -0.2849 442 VAL C CG2 
9661  N N   . SER C 434 ? 1.5339 0.8194 1.1625 -0.7627 -0.3475 -0.1963 443 SER C N   
9662  C CA  . SER C 434 ? 1.4674 0.8178 1.1391 -0.7558 -0.3231 -0.1722 443 SER C CA  
9663  C C   . SER C 434 ? 1.5063 0.8058 1.1690 -0.7616 -0.3290 -0.1572 443 SER C C   
9664  O O   . SER C 434 ? 1.5937 0.8070 1.2168 -0.7807 -0.3558 -0.1602 443 SER C O   
9665  C CB  . SER C 434 ? 1.4138 0.8620 1.1258 -0.7881 -0.3160 -0.1457 443 SER C CB  
9666  O OG  . SER C 434 ? 1.4158 0.8737 1.1400 -0.8214 -0.3223 -0.1146 443 SER C OG  
9667  N N   . ASN C 435 ? 1.4501 0.8014 1.1478 -0.7448 -0.3049 -0.1414 444 ASN C N   
9668  C CA  . ASN C 435 ? 1.4811 0.7957 1.1756 -0.7484 -0.3070 -0.1250 444 ASN C CA  
9669  C C   . ASN C 435 ? 1.5290 0.8457 1.2253 -0.8031 -0.3269 -0.0942 444 ASN C C   
9670  O O   . ASN C 435 ? 1.4997 0.8843 1.2190 -0.8344 -0.3279 -0.0769 444 ASN C O   
9671  C CB  . ASN C 435 ? 1.3981 0.7736 1.1303 -0.7165 -0.2760 -0.1164 444 ASN C CB  
9672  C CG  . ASN C 435 ? 1.3443 0.7727 1.0954 -0.6789 -0.2530 -0.1349 444 ASN C CG  
9673  O OD1 . ASN C 435 ? 1.3942 0.7960 1.1239 -0.6649 -0.2588 -0.1598 444 ASN C OD1 
9674  N ND2 . ASN C 435 ? 1.2750 0.7790 1.0651 -0.6624 -0.2276 -0.1227 444 ASN C ND2 
9675  N N   . LYS C 436 ? 1.6023 0.8489 1.2759 -0.8131 -0.3415 -0.0857 445 LYS C N   
9676  C CA  . LYS C 436 ? 1.7044 0.8956 1.3506 -0.8641 -0.3747 -0.0696 445 LYS C CA  
9677  C C   . LYS C 436 ? 1.7558 0.9152 1.3731 -0.8820 -0.3967 -0.0876 445 LYS C C   
9678  O O   . LYS C 436 ? 1.7122 0.9356 1.3491 -0.8765 -0.3853 -0.0954 445 LYS C O   
9679  C CB  . LYS C 436 ? 1.6923 0.9491 1.3706 -0.9079 -0.3755 -0.0289 445 LYS C CB  
9680  C CG  . LYS C 436 ? 1.8168 1.0166 1.4668 -0.9676 -0.4129 -0.0071 445 LYS C CG  
9681  C CD  . LYS C 436 ? 1.9575 1.0249 1.5536 -0.9713 -0.4410 -0.0165 445 LYS C CD  
9682  C CE  . LYS C 436 ? 1.9706 0.9780 1.5490 -0.9143 -0.4273 -0.0422 445 LYS C CE  
9683  N NZ  . LYS C 436 ? 1.8829 0.9578 1.5026 -0.8770 -0.3916 -0.0357 445 LYS C NZ  
9684  N N   . GLY C 437 ? 1.8568 0.9147 1.4255 -0.9033 -0.4293 -0.0941 446 GLY C N   
9685  C CA  . GLY C 437 ? 1.9113 0.9066 1.4383 -0.8994 -0.4492 -0.1238 446 GLY C CA  
9686  C C   . GLY C 437 ? 1.9116 0.8462 1.4144 -0.8418 -0.4388 -0.1541 446 GLY C C   
9687  O O   . GLY C 437 ? 1.9814 0.8290 1.4503 -0.8366 -0.4535 -0.1566 446 GLY C O   
9688  N N   . VAL C 438 ? 1.8296 0.8155 1.3521 -0.7982 -0.4122 -0.1742 447 VAL C N   
9689  C CA  . VAL C 438 ? 1.8322 0.7631 1.3270 -0.7443 -0.4054 -0.2067 447 VAL C CA  
9690  C C   . VAL C 438 ? 1.7677 0.7201 1.2854 -0.7031 -0.3778 -0.2044 447 VAL C C   
9691  O O   . VAL C 438 ? 1.6818 0.7225 1.2479 -0.6989 -0.3519 -0.1873 447 VAL C O   
9692  C CB  . VAL C 438 ? 1.8072 0.7656 1.2996 -0.7198 -0.3977 -0.2337 447 VAL C CB  
9693  C CG1 . VAL C 438 ? 1.8605 0.7392 1.3081 -0.6743 -0.4029 -0.2676 447 VAL C CG1 
9694  C CG2 . VAL C 438 ? 1.8526 0.8108 1.3324 -0.7638 -0.4214 -0.2316 447 VAL C CG2 
9695  N N   . ASP C 439 ? 1.8126 0.6815 1.2925 -0.6717 -0.3847 -0.2227 448 ASP C N   
9696  C CA  . ASP C 439 ? 1.7715 0.6436 1.2640 -0.6337 -0.3637 -0.2216 448 ASP C CA  
9697  C C   . ASP C 439 ? 1.7664 0.6108 1.2363 -0.5781 -0.3544 -0.2551 448 ASP C C   
9698  O O   . ASP C 439 ? 1.7051 0.5849 1.1966 -0.5388 -0.3288 -0.2583 448 ASP C O   
9699  C CB  . ASP C 439 ? 1.8457 0.6388 1.3110 -0.6503 -0.3833 -0.2083 448 ASP C CB  
9700  C CG  . ASP C 439 ? 1.8228 0.6541 1.3218 -0.6384 -0.3616 -0.1879 448 ASP C CG  
9701  O OD1 . ASP C 439 ? 1.7864 0.6658 1.3099 -0.5968 -0.3336 -0.1965 448 ASP C OD1 
9702  O OD2 . ASP C 439 ? 1.8864 0.7001 1.3870 -0.6711 -0.3728 -0.1625 448 ASP C OD2 
9703  N N   . THR C 440 ? 1.8259 0.6106 1.2521 -0.5759 -0.3757 -0.2793 449 THR C N   
9704  C CA  . THR C 440 ? 1.8441 0.5842 1.2363 -0.5255 -0.3742 -0.3120 449 THR C CA  
9705  C C   . THR C 440 ? 1.8687 0.6016 1.2383 -0.5287 -0.3871 -0.3339 449 THR C C   
9706  O O   . THR C 440 ? 1.9274 0.6275 1.2773 -0.5704 -0.4127 -0.3295 449 THR C O   
9707  C CB  . THR C 440 ? 1.9428 0.5685 1.2809 -0.5156 -0.3977 -0.3205 449 THR C CB  
9708  O OG1 . THR C 440 ? 1.9008 0.5338 1.2529 -0.4818 -0.3779 -0.3153 449 THR C OG1 
9709  C CG2 . THR C 440 ? 2.0289 0.5780 1.3093 -0.4861 -0.4160 -0.3558 449 THR C CG2 
9710  N N   . VAL C 441 ? 1.8251 0.5909 1.1978 -0.4864 -0.3700 -0.3564 450 VAL C N   
9711  C CA  . VAL C 441 ? 1.8735 0.6046 1.2083 -0.4789 -0.3865 -0.3836 450 VAL C CA  
9712  C C   . VAL C 441 ? 1.9066 0.5920 1.2059 -0.4211 -0.3830 -0.4122 450 VAL C C   
9713  O O   . VAL C 441 ? 1.8521 0.5758 1.1746 -0.3848 -0.3579 -0.4110 450 VAL C O   
9714  C CB  . VAL C 441 ? 1.8041 0.6233 1.1725 -0.4891 -0.3737 -0.3846 450 VAL C CB  
9715  C CG1 . VAL C 441 ? 1.7486 0.6313 1.1606 -0.5390 -0.3705 -0.3532 450 VAL C CG1 
9716  C CG2 . VAL C 441 ? 1.7274 0.6175 1.1254 -0.4433 -0.3420 -0.3940 450 VAL C CG2 
9717  N N   . SER C 442 ? 2.0021 0.6046 1.2433 -0.4125 -0.4091 -0.4374 451 SER C N   
9718  C CA  . SER C 442 ? 2.0382 0.6031 1.2428 -0.3548 -0.4063 -0.4669 451 SER C CA  
9719  C C   . SER C 442 ? 2.0448 0.6241 1.2324 -0.3428 -0.4106 -0.4914 451 SER C C   
9720  O O   . SER C 442 ? 2.0887 0.6447 1.2590 -0.3790 -0.4327 -0.4938 451 SER C O   
9721  C CB  . SER C 442 ? 2.1498 0.5948 1.2928 -0.3438 -0.4333 -0.4780 451 SER C CB  
9722  O OG  . SER C 442 ? 2.2336 0.6257 1.3641 -0.3979 -0.4596 -0.4600 451 SER C OG  
9723  N N   . VAL C 443 ? 2.0011 0.6256 1.1967 -0.2933 -0.3885 -0.5076 452 VAL C N   
9724  C CA  . VAL C 443 ? 2.0133 0.6473 1.1872 -0.2718 -0.3916 -0.5338 452 VAL C CA  
9725  C C   . VAL C 443 ? 2.0762 0.6502 1.2004 -0.2149 -0.3959 -0.5605 452 VAL C C   
9726  O O   . VAL C 443 ? 2.0334 0.6401 1.1748 -0.1756 -0.3731 -0.5588 452 VAL C O   
9727  C CB  . VAL C 443 ? 1.9004 0.6509 1.1293 -0.2607 -0.3602 -0.5283 452 VAL C CB  
9728  C CG1 . VAL C 443 ? 1.9170 0.6759 1.1225 -0.2446 -0.3662 -0.5539 452 VAL C CG1 
9729  C CG2 . VAL C 443 ? 1.8278 0.6452 1.1109 -0.3102 -0.3512 -0.4986 452 VAL C CG2 
9730  N N   . GLY C 444 ? 2.1802 0.6657 1.2410 -0.2104 -0.4261 -0.5849 453 GLY C N   
9731  C CA  . GLY C 444 ? 2.2548 0.6686 1.2587 -0.1571 -0.4354 -0.6114 453 GLY C CA  
9732  C C   . GLY C 444 ? 2.2545 0.6387 1.2614 -0.1446 -0.4293 -0.5972 453 GLY C C   
9733  O O   . GLY C 444 ? 2.2835 0.6186 1.2874 -0.1831 -0.4449 -0.5794 453 GLY C O   
9734  N N   . ASN C 445 ? 2.2163 0.6374 1.2326 -0.0921 -0.4058 -0.6030 454 ASN C N   
9735  C CA  . ASN C 445 ? 2.2235 0.6178 1.2401 -0.0742 -0.3994 -0.5916 454 ASN C CA  
9736  C C   . ASN C 445 ? 2.1064 0.5897 1.1934 -0.0879 -0.3691 -0.5611 454 ASN C C   
9737  O O   . ASN C 445 ? 2.1070 0.5704 1.1994 -0.0822 -0.3644 -0.5473 454 ASN C O   
9738  C CB  . ASN C 445 ? 2.2726 0.6377 1.2476 -0.0072 -0.3964 -0.6160 454 ASN C CB  
9739  C CG  . ASN C 445 ? 2.4282 0.6659 1.3258 0.0042  -0.4313 -0.6370 454 ASN C CG  
9740  O OD1 . ASN C 445 ? 2.5087 0.6858 1.3832 0.0173  -0.4384 -0.6332 454 ASN C OD1 
9741  N ND2 . ASN C 445 ? 2.5115 0.7034 1.3670 -0.0036 -0.4551 -0.6585 454 ASN C ND2 
9742  N N   . THR C 446 ? 2.0073 0.5869 1.1461 -0.1054 -0.3494 -0.5510 455 THR C N   
9743  C CA  . THR C 446 ? 1.8923 0.5595 1.0974 -0.1200 -0.3216 -0.5230 455 THR C CA  
9744  C C   . THR C 446 ? 1.8842 0.5374 1.1083 -0.1792 -0.3330 -0.4985 455 THR C C   
9745  O O   . THR C 446 ? 1.9170 0.5473 1.1281 -0.2158 -0.3526 -0.5005 455 THR C O   
9746  C CB  . THR C 446 ? 1.8042 0.5765 1.0535 -0.1148 -0.2979 -0.5224 455 THR C CB  
9747  O OG1 . THR C 446 ? 1.8226 0.6032 1.0470 -0.0631 -0.2922 -0.5472 455 THR C OG1 
9748  C CG2 . THR C 446 ? 1.7031 0.5620 1.0152 -0.1186 -0.2683 -0.4966 455 THR C CG2 
9749  N N   . LEU C 447 ? 1.8405 0.5107 1.0955 -0.1884 -0.3209 -0.4749 456 LEU C N   
9750  C CA  . LEU C 447 ? 1.8354 0.5024 1.1125 -0.2424 -0.3291 -0.4487 456 LEU C CA  
9751  C C   . LEU C 447 ? 1.7253 0.4984 1.0707 -0.2591 -0.3010 -0.4239 456 LEU C C   
9752  O O   . LEU C 447 ? 1.6709 0.4907 1.0442 -0.2309 -0.2772 -0.4175 456 LEU C O   
9753  C CB  . LEU C 447 ? 1.8913 0.4843 1.1449 -0.2425 -0.3408 -0.4396 456 LEU C CB  
9754  C CG  . LEU C 447 ? 1.8965 0.4759 1.1662 -0.2986 -0.3528 -0.4117 456 LEU C CG  
9755  C CD1 . LEU C 447 ? 2.0007 0.5136 1.2310 -0.3368 -0.3865 -0.4185 456 LEU C CD1 
9756  C CD2 . LEU C 447 ? 1.9195 0.4479 1.1779 -0.2910 -0.3557 -0.3998 456 LEU C CD2 
9757  N N   . TYR C 448 ? 1.7013 0.5116 1.0723 -0.3049 -0.3046 -0.4095 457 TYR C N   
9758  C CA  . TYR C 448 ? 1.6027 0.5114 1.0359 -0.3218 -0.2799 -0.3857 457 TYR C CA  
9759  C C   . TYR C 448 ? 1.5999 0.5021 1.0509 -0.3660 -0.2867 -0.3570 457 TYR C C   
9760  O O   . TYR C 448 ? 1.6733 0.5165 1.0970 -0.4006 -0.3128 -0.3538 457 TYR C O   
9761  C CB  . TYR C 448 ? 1.5642 0.5362 1.0178 -0.3358 -0.2750 -0.3900 457 TYR C CB  
9762  C CG  . TYR C 448 ? 1.5661 0.5608 1.0098 -0.2932 -0.2650 -0.4150 457 TYR C CG  
9763  C CD1 . TYR C 448 ? 1.6672 0.5928 1.0572 -0.2698 -0.2832 -0.4425 457 TYR C CD1 
9764  C CD2 . TYR C 448 ? 1.4854 0.5711 0.9720 -0.2765 -0.2382 -0.4106 457 TYR C CD2 
9765  C CE1 . TYR C 448 ? 1.6636 0.6162 1.0452 -0.2299 -0.2733 -0.4643 457 TYR C CE1 
9766  C CE2 . TYR C 448 ? 1.4817 0.5929 0.9608 -0.2392 -0.2290 -0.4311 457 TYR C CE2 
9767  C CZ  . TYR C 448 ? 1.5685 0.6159 0.9961 -0.2157 -0.2460 -0.4575 457 TYR C CZ  
9768  O OH  . TYR C 448 ? 1.5595 0.6383 0.9805 -0.1781 -0.2363 -0.4767 457 TYR C OH  
9769  N N   . TYR C 449 ? 1.5199 0.4826 1.0155 -0.3654 -0.2642 -0.3357 458 TYR C N   
9770  C CA  . TYR C 449 ? 1.5118 0.4759 1.0264 -0.4040 -0.2684 -0.3073 458 TYR C CA  
9771  C C   . TYR C 449 ? 1.4368 0.4901 1.0000 -0.4353 -0.2557 -0.2864 458 TYR C C   
9772  O O   . TYR C 449 ? 1.3591 0.4870 0.9620 -0.4179 -0.2299 -0.2793 458 TYR C O   
9773  C CB  . TYR C 449 ? 1.4864 0.4500 1.0138 -0.3817 -0.2538 -0.2961 458 TYR C CB  
9774  C CG  . TYR C 449 ? 1.5582 0.4352 1.0398 -0.3518 -0.2658 -0.3119 458 TYR C CG  
9775  C CD1 . TYR C 449 ? 1.5563 0.4341 1.0262 -0.3012 -0.2537 -0.3329 458 TYR C CD1 
9776  C CD2 . TYR C 449 ? 1.6398 0.4357 1.0894 -0.3733 -0.2893 -0.3047 458 TYR C CD2 
9777  C CE1 . TYR C 449 ? 1.6406 0.4424 1.0677 -0.2705 -0.2641 -0.3472 458 TYR C CE1 
9778  C CE2 . TYR C 449 ? 1.7232 0.4374 1.1286 -0.3435 -0.3006 -0.3192 458 TYR C CE2 
9779  C CZ  . TYR C 449 ? 1.7232 0.4415 1.1173 -0.2907 -0.2875 -0.3410 458 TYR C CZ  
9780  O OH  . TYR C 449 ? 1.8016 0.4411 1.1502 -0.2577 -0.2985 -0.3559 458 TYR C OH  
9781  N N   . VAL C 450 ? 1.4623 0.5084 1.0221 -0.4814 -0.2742 -0.2751 459 VAL C N   
9782  C CA  . VAL C 450 ? 1.3948 0.5282 0.9980 -0.5103 -0.2633 -0.2561 459 VAL C CA  
9783  C C   . VAL C 450 ? 1.3463 0.5283 0.9882 -0.5224 -0.2483 -0.2272 459 VAL C C   
9784  O O   . VAL C 450 ? 1.2751 0.5410 0.9579 -0.5271 -0.2300 -0.2143 459 VAL C O   
9785  C CB  . VAL C 450 ? 1.4367 0.5561 1.0261 -0.5558 -0.2872 -0.2518 459 VAL C CB  
9786  C CG1 . VAL C 450 ? 1.3682 0.5848 1.0018 -0.5780 -0.2738 -0.2354 459 VAL C CG1 
9787  C CG2 . VAL C 450 ? 1.4924 0.5581 1.0398 -0.5425 -0.3034 -0.2814 459 VAL C CG2 
9788  N N   . ASN C 451 ? 1.3907 0.5190 1.0179 -0.5258 -0.2564 -0.2175 460 ASN C N   
9789  C CA  . ASN C 451 ? 1.3499 0.5188 1.0103 -0.5320 -0.2418 -0.1916 460 ASN C CA  
9790  C C   . ASN C 451 ? 1.3483 0.4897 1.0035 -0.4923 -0.2297 -0.1973 460 ASN C C   
9791  O O   . ASN C 451 ? 1.3945 0.4741 1.0150 -0.4640 -0.2366 -0.2193 460 ASN C O   
9792  C CB  . ASN C 451 ? 1.3922 0.5398 1.0486 -0.5809 -0.2615 -0.1667 460 ASN C CB  
9793  C CG  . ASN C 451 ? 1.3860 0.5913 1.0623 -0.6204 -0.2665 -0.1535 460 ASN C CG  
9794  O OD1 . ASN C 451 ? 1.3337 0.6253 1.0487 -0.6167 -0.2463 -0.1456 460 ASN C OD1 
9795  N ND2 . ASN C 451 ? 1.4718 0.6290 1.1204 -0.6580 -0.2944 -0.1509 460 ASN C ND2 
9796  N N   . LYS C 452 ? 1.2994 0.4896 0.9884 -0.4878 -0.2111 -0.1782 461 LYS C N   
9797  C CA  . LYS C 452 ? 1.3030 0.4715 0.9885 -0.4513 -0.1996 -0.1826 461 LYS C CA  
9798  C C   . LYS C 452 ? 1.3800 0.4714 1.0365 -0.4663 -0.2189 -0.1742 461 LYS C C   
9799  O O   . LYS C 452 ? 1.3994 0.4900 1.0604 -0.5063 -0.2308 -0.1533 461 LYS C O   
9800  C CB  . LYS C 452 ? 1.2221 0.4664 0.9515 -0.4422 -0.1745 -0.1652 461 LYS C CB  
9801  C CG  . LYS C 452 ? 1.1667 0.4911 0.9270 -0.4345 -0.1572 -0.1686 461 LYS C CG  
9802  C CD  . LYS C 452 ? 1.1183 0.4987 0.9112 -0.4104 -0.1328 -0.1599 461 LYS C CD  
9803  C CE  . LYS C 452 ? 1.0769 0.5369 0.9007 -0.4082 -0.1177 -0.1593 461 LYS C CE  
9804  N NZ  . LYS C 452 ? 1.0377 0.5444 0.8882 -0.3816 -0.0957 -0.1537 461 LYS C NZ  
9805  N N   . GLN C 453 ? 1.4326 0.4603 1.0586 -0.4346 -0.2226 -0.1895 462 GLN C N   
9806  C CA  . GLN C 453 ? 1.5207 0.4674 1.1149 -0.4466 -0.2424 -0.1822 462 GLN C CA  
9807  C C   . GLN C 453 ? 1.4971 0.4644 1.1147 -0.4412 -0.2286 -0.1614 462 GLN C C   
9808  O O   . GLN C 453 ? 1.4593 0.4448 1.0871 -0.4030 -0.2100 -0.1677 462 GLN C O   
9809  C CB  . GLN C 453 ? 1.5926 0.4524 1.1362 -0.4158 -0.2568 -0.2090 462 GLN C CB  
9810  C CG  . GLN C 453 ? 1.6451 0.4843 1.1635 -0.4194 -0.2709 -0.2311 462 GLN C CG  
9811  C CD  . GLN C 453 ? 1.7101 0.5354 1.2222 -0.4732 -0.2934 -0.2184 462 GLN C CD  
9812  O OE1 . GLN C 453 ? 1.8066 0.5553 1.2849 -0.4963 -0.3188 -0.2131 462 GLN C OE1 
9813  N NE2 . GLN C 453 ? 1.6580 0.5577 1.2021 -0.4936 -0.2850 -0.2127 462 GLN C NE2 
9814  N N   . GLU C 454 ? 1.5270 0.4962 1.1542 -0.4811 -0.2379 -0.1352 463 GLU C N   
9815  C CA  . GLU C 454 ? 1.5240 0.5055 1.1694 -0.4821 -0.2288 -0.1127 463 GLU C CA  
9816  C C   . GLU C 454 ? 1.5902 0.4830 1.1970 -0.4619 -0.2408 -0.1203 463 GLU C C   
9817  O O   . GLU C 454 ? 1.6779 0.4888 1.2404 -0.4672 -0.2650 -0.1333 463 GLU C O   
9818  C CB  . GLU C 454 ? 1.5431 0.5407 1.2016 -0.5330 -0.2404 -0.0828 463 GLU C CB  
9819  C CG  . GLU C 454 ? 1.5087 0.6081 1.2182 -0.5449 -0.2191 -0.0599 463 GLU C CG  
9820  C CD  . GLU C 454 ? 1.5883 0.7072 1.3075 -0.5981 -0.2335 -0.0311 463 GLU C CD  
9821  O OE1 . GLU C 454 ? 1.6544 0.7318 1.3611 -0.6188 -0.2470 -0.0127 463 GLU C OE1 
9822  O OE2 . GLU C 454 ? 1.5703 0.7479 1.3094 -0.6195 -0.2316 -0.0260 463 GLU C OE2 
9823  N N   . GLY C 455 ? 1.5570 0.4643 1.1787 -0.4394 -0.2251 -0.1115 464 GLY C N   
9824  C CA  . GLY C 455 ? 1.6219 0.4505 1.2096 -0.4204 -0.2354 -0.1156 464 GLY C CA  
9825  C C   . GLY C 455 ? 1.5825 0.4419 1.1953 -0.4072 -0.2180 -0.0980 464 GLY C C   
9826  O O   . GLY C 455 ? 1.5048 0.4425 1.1563 -0.3934 -0.1938 -0.0934 464 GLY C O   
9827  N N   . LYS C 456 ? 1.6446 0.4393 1.2334 -0.4142 -0.2324 -0.0872 465 LYS C N   
9828  C CA  . LYS C 456 ? 1.6279 0.4239 1.2252 -0.3920 -0.2202 -0.0767 465 LYS C CA  
9829  C C   . LYS C 456 ? 1.5312 0.4242 1.1791 -0.3830 -0.1916 -0.0638 465 LYS C C   
9830  O O   . LYS C 456 ? 1.4776 0.4153 1.1416 -0.3511 -0.1727 -0.0784 465 LYS C O   
9831  C CB  . LYS C 456 ? 1.6633 0.4009 1.2261 -0.3446 -0.2212 -0.1012 465 LYS C CB  
9832  C CG  . LYS C 456 ? 1.6887 0.3937 1.2430 -0.3268 -0.2192 -0.0910 465 LYS C CG  
9833  C CD  . LYS C 456 ? 1.7610 0.4055 1.2769 -0.2795 -0.2224 -0.1152 465 LYS C CD  
9834  C CE  . LYS C 456 ? 1.8135 0.4258 1.3213 -0.2645 -0.2214 -0.1024 465 LYS C CE  
9835  N NZ  . LYS C 456 ? 1.8292 0.4335 1.3246 -0.2104 -0.2094 -0.1192 465 LYS C NZ  
9836  N N   . SER C 457 ? 1.5154 0.4405 1.1870 -0.4113 -0.1894 -0.0359 466 SER C N   
9837  C CA  . SER C 457 ? 1.4390 0.4424 1.1516 -0.3988 -0.1645 -0.0232 466 SER C CA  
9838  C C   . SER C 457 ? 1.4420 0.4161 1.1448 -0.3640 -0.1573 -0.0259 466 SER C C   
9839  O O   . SER C 457 ? 1.5047 0.4049 1.1756 -0.3634 -0.1730 -0.0245 466 SER C O   
9840  C CB  . SER C 457 ? 1.4243 0.4698 1.1621 -0.4371 -0.1649 0.0078  466 SER C CB  
9841  O OG  . SER C 457 ? 1.5154 0.4955 1.2284 -0.4573 -0.1842 0.0226  466 SER C OG  
9842  N N   . LEU C 458 ? 1.3767 0.4084 1.1059 -0.3348 -0.1343 -0.0297 467 LEU C N   
9843  C CA  . LEU C 458 ? 1.3785 0.3951 1.1037 -0.3032 -0.1257 -0.0295 467 LEU C CA  
9844  C C   . LEU C 458 ? 1.3265 0.4066 1.0879 -0.3120 -0.1106 -0.0064 467 LEU C C   
9845  O O   . LEU C 458 ? 1.2680 0.4174 1.0603 -0.3240 -0.0993 -0.0001 467 LEU C O   
9846  C CB  . LEU C 458 ? 1.3510 0.3784 1.0733 -0.2598 -0.1130 -0.0534 467 LEU C CB  
9847  C CG  . LEU C 458 ? 1.4181 0.3716 1.0971 -0.2438 -0.1291 -0.0766 467 LEU C CG  
9848  C CD1 . LEU C 458 ? 1.3847 0.3548 1.0616 -0.1986 -0.1156 -0.0975 467 LEU C CD1 
9849  C CD2 . LEU C 458 ? 1.4931 0.3602 1.1353 -0.2468 -0.1483 -0.0711 467 LEU C CD2 
9850  N N   . TYR C 459 ? 1.3552 0.4102 1.1109 -0.3052 -0.1110 0.0062  468 TYR C N   
9851  C CA  . TYR C 459 ? 1.3222 0.4310 1.1082 -0.3150 -0.0990 0.0295  468 TYR C CA  
9852  C C   . TYR C 459 ? 1.2906 0.4037 1.0807 -0.2806 -0.0857 0.0296  468 TYR C C   
9853  O O   . TYR C 459 ? 1.3379 0.3908 1.1007 -0.2615 -0.0930 0.0230  468 TYR C O   
9854  C CB  . TYR C 459 ? 1.3804 0.4626 1.1594 -0.3542 -0.1153 0.0534  468 TYR C CB  
9855  C CG  . TYR C 459 ? 1.3996 0.5417 1.2097 -0.3670 -0.1038 0.0796  468 TYR C CG  
9856  C CD1 . TYR C 459 ? 1.3759 0.6012 1.2202 -0.3758 -0.0897 0.0862  468 TYR C CD1 
9857  C CD2 . TYR C 459 ? 1.4816 0.5980 1.2857 -0.3686 -0.1071 0.0977  468 TYR C CD2 
9858  C CE1 . TYR C 459 ? 1.3555 0.6379 1.2263 -0.3848 -0.0792 0.1095  468 TYR C CE1 
9859  C CE2 . TYR C 459 ? 1.4630 0.6380 1.2954 -0.3792 -0.0962 0.1219  468 TYR C CE2 
9860  C CZ  . TYR C 459 ? 1.3963 0.6544 1.2614 -0.3867 -0.0823 0.1272  468 TYR C CZ  
9861  O OH  . TYR C 459 ? 1.3597 0.6763 1.2501 -0.3946 -0.0721 0.1497  468 TYR C OH  
9862  N N   . VAL C 460 ? 1.2168 0.4000 1.0394 -0.2717 -0.0668 0.0369  469 VAL C N   
9863  C CA  . VAL C 460 ? 1.1994 0.3888 1.0262 -0.2413 -0.0550 0.0379  469 VAL C CA  
9864  C C   . VAL C 460 ? 1.1753 0.4109 1.0273 -0.2515 -0.0457 0.0614  469 VAL C C   
9865  O O   . VAL C 460 ? 1.1165 0.4189 0.9965 -0.2547 -0.0330 0.0663  469 VAL C O   
9866  C CB  . VAL C 460 ? 1.1500 0.3713 0.9854 -0.2083 -0.0409 0.0189  469 VAL C CB  
9867  C CG1 . VAL C 460 ? 1.1085 0.3518 0.9551 -0.1829 -0.0278 0.0249  469 VAL C CG1 
9868  C CG2 . VAL C 460 ? 1.1928 0.3604 0.9978 -0.1895 -0.0501 -0.0037 469 VAL C CG2 
9869  N N   . LYS C 461 ? 1.2308 0.4272 1.0699 -0.2547 -0.0528 0.0754  470 LYS C N   
9870  C CA  . LYS C 461 ? 1.2247 0.4535 1.0820 -0.2682 -0.0478 0.1004  470 LYS C CA  
9871  C C   . LYS C 461 ? 1.1724 0.4432 1.0475 -0.2381 -0.0297 0.1001  470 LYS C C   
9872  O O   . LYS C 461 ? 1.1665 0.4232 1.0332 -0.2069 -0.0245 0.0837  470 LYS C O   
9873  C CB  . LYS C 461 ? 1.2990 0.4642 1.1328 -0.2870 -0.0652 0.1162  470 LYS C CB  
9874  C CG  . LYS C 461 ? 1.3395 0.5051 1.1773 -0.2813 -0.0611 0.1357  470 LYS C CG  
9875  C CD  . LYS C 461 ? 1.3918 0.5829 1.2430 -0.3173 -0.0656 0.1655  470 LYS C CD  
9876  C CE  . LYS C 461 ? 1.3906 0.5914 1.2486 -0.3070 -0.0587 0.1835  470 LYS C CE  
9877  N NZ  . LYS C 461 ? 1.3415 0.6137 1.2285 -0.3252 -0.0497 0.2068  470 LYS C NZ  
9878  N N   . GLY C 462 ? 1.1366 0.4630 1.0363 -0.2479 -0.0204 0.1179  471 GLY C N   
9879  C CA  . GLY C 462 ? 1.1077 0.4693 1.0222 -0.2249 -0.0061 0.1225  471 GLY C CA  
9880  C C   . GLY C 462 ? 1.1311 0.4992 1.0509 -0.2403 -0.0077 0.1481  471 GLY C C   
9881  O O   . GLY C 462 ? 1.1462 0.5243 1.0703 -0.2706 -0.0146 0.1640  471 GLY C O   
9882  N N   . GLU C 463 ? 1.1396 0.5032 1.0586 -0.2199 -0.0018 0.1533  472 GLU C N   
9883  C CA  . GLU C 463 ? 1.1527 0.5348 1.0805 -0.2303 -0.0001 0.1777  472 GLU C CA  
9884  C C   . GLU C 463 ? 1.0814 0.5411 1.0367 -0.2236 0.0155  0.1824  472 GLU C C   
9885  O O   . GLU C 463 ? 1.0419 0.5339 1.0074 -0.2141 0.0228  0.1676  472 GLU C O   
9886  C CB  . GLU C 463 ? 1.1946 0.5272 1.1045 -0.2125 -0.0035 0.1814  472 GLU C CB  
9887  C CG  . GLU C 463 ? 1.2095 0.5691 1.1289 -0.1813 0.0104  0.1801  472 GLU C CG  
9888  C CD  . GLU C 463 ? 1.2232 0.6222 1.1551 -0.1565 0.0230  0.1601  472 GLU C CD  
9889  O OE1 . GLU C 463 ? 1.2402 0.6237 1.1645 -0.1500 0.0208  0.1410  472 GLU C OE1 
9890  O OE2 . GLU C 463 ? 1.1954 0.6403 1.1435 -0.1435 0.0344  0.1642  472 GLU C OE2 
9891  N N   . PRO C 464 ? 1.0693 0.5586 1.0352 -0.2284 0.0198  0.2029  473 PRO C N   
9892  C CA  . PRO C 464 ? 1.0093 0.5628 0.9955 -0.2143 0.0339  0.2029  473 PRO C CA  
9893  C C   . PRO C 464 ? 0.9939 0.5483 0.9802 -0.1871 0.0417  0.2029  473 PRO C C   
9894  O O   . PRO C 464 ? 1.0233 0.5366 0.9967 -0.1818 0.0371  0.2092  473 PRO C O   
9895  C CB  . PRO C 464 ? 1.0027 0.5999 1.0017 -0.2382 0.0338  0.2255  473 PRO C CB  
9896  C CG  . PRO C 464 ? 1.0642 0.6154 1.0496 -0.2589 0.0213  0.2433  473 PRO C CG  
9897  C CD  . PRO C 464 ? 1.1068 0.5840 1.0691 -0.2521 0.0115  0.2278  473 PRO C CD  
9898  N N   . ILE C 465 ? 0.9483 0.5493 0.9480 -0.1705 0.0525  0.1965  474 ILE C N   
9899  C CA  . ILE C 465 ? 0.9367 0.5371 0.9354 -0.1429 0.0591  0.1900  474 ILE C CA  
9900  C C   . ILE C 465 ? 0.9148 0.5579 0.9245 -0.1365 0.0666  0.2039  474 ILE C C   
9901  O O   . ILE C 465 ? 0.8821 0.5724 0.9037 -0.1441 0.0706  0.2097  474 ILE C O   
9902  C CB  . ILE C 465 ? 0.9100 0.5157 0.9097 -0.1258 0.0630  0.1672  474 ILE C CB  
9903  C CG1 . ILE C 465 ? 0.9031 0.5090 0.9014 -0.0989 0.0686  0.1612  474 ILE C CG1 
9904  C CG2 . ILE C 465 ? 0.8646 0.5183 0.8781 -0.1321 0.0675  0.1622  474 ILE C CG2 
9905  C CD1 . ILE C 465 ? 0.9031 0.5062 0.8995 -0.0838 0.0702  0.1407  474 ILE C CD1 
9906  N N   . ILE C 466 ? 0.9357 0.5619 0.9398 -0.1205 0.0682  0.2081  475 ILE C N   
9907  C CA  . ILE C 466 ? 0.9401 0.5899 0.9493 -0.1179 0.0720  0.2260  475 ILE C CA  
9908  C C   . ILE C 466 ? 0.9077 0.5964 0.9247 -0.0970 0.0806  0.2227  475 ILE C C   
9909  O O   . ILE C 466 ? 0.8966 0.5720 0.9094 -0.0774 0.0825  0.2142  475 ILE C O   
9910  C CB  . ILE C 466 ? 0.9864 0.5895 0.9826 -0.1177 0.0664  0.2380  475 ILE C CB  
9911  C CG1 . ILE C 466 ? 1.0166 0.5751 0.9994 -0.0979 0.0643  0.2222  475 ILE C CG1 
9912  C CG2 . ILE C 466 ? 1.0041 0.5830 0.9947 -0.1461 0.0567  0.2525  475 ILE C CG2 
9913  C CD1 . ILE C 466 ? 1.0323 0.5738 1.0079 -0.0783 0.0660  0.2287  475 ILE C CD1 
9914  N N   . ASN C 467 ? 0.8962 0.6329 0.9232 -0.1012 0.0848  0.2296  476 ASN C N   
9915  C CA  . ASN C 467 ? 0.8823 0.6533 0.9135 -0.0828 0.0909  0.2283  476 ASN C CA  
9916  C C   . ASN C 467 ? 0.8995 0.6768 0.9297 -0.0783 0.0925  0.2461  476 ASN C C   
9917  O O   . ASN C 467 ? 0.8989 0.7076 0.9336 -0.0859 0.0941  0.2610  476 ASN C O   
9918  C CB  . ASN C 467 ? 0.8497 0.6665 0.8880 -0.0824 0.0941  0.2224  476 ASN C CB  
9919  C CG  . ASN C 467 ? 0.8323 0.6693 0.8700 -0.0611 0.0975  0.2132  476 ASN C CG  
9920  O OD1 . ASN C 467 ? 0.8374 0.6537 0.8714 -0.0482 0.0972  0.2056  476 ASN C OD1 
9921  N ND2 . ASN C 467 ? 0.8070 0.6846 0.8470 -0.0574 0.0998  0.2144  476 ASN C ND2 
9922  N N   . PHE C 468 ? 0.9158 0.6675 0.9400 -0.0633 0.0926  0.2435  477 PHE C N   
9923  C CA  . PHE C 468 ? 0.9522 0.6790 0.9704 -0.0616 0.0910  0.2581  477 PHE C CA  
9924  C C   . PHE C 468 ? 0.9330 0.6832 0.9526 -0.0455 0.0954  0.2653  477 PHE C C   
9925  O O   . PHE C 468 ? 0.9522 0.6786 0.9657 -0.0337 0.0950  0.2682  477 PHE C O   
9926  C CB  . PHE C 468 ? 0.9783 0.6590 0.9869 -0.0515 0.0879  0.2462  477 PHE C CB  
9927  C CG  . PHE C 468 ? 0.9678 0.6597 0.9787 -0.0362 0.0907  0.2264  477 PHE C CG  
9928  C CD1 . PHE C 468 ? 0.9582 0.6658 0.9700 -0.0168 0.0943  0.2238  477 PHE C CD1 
9929  C CD2 . PHE C 468 ? 0.9489 0.6400 0.9617 -0.0431 0.0893  0.2119  477 PHE C CD2 
9930  C CE1 . PHE C 468 ? 0.9354 0.6556 0.9495 -0.0058 0.0956  0.2082  477 PHE C CE1 
9931  C CE2 . PHE C 468 ? 0.9228 0.6262 0.9379 -0.0309 0.0913  0.1957  477 PHE C CE2 
9932  C CZ  . PHE C 468 ? 0.9193 0.6373 0.9351 -0.0129 0.0942  0.1943  477 PHE C CZ  
9933  N N   . TYR C 469 ? 0.8968 0.6920 0.9225 -0.0435 0.0990  0.2677  478 TYR C N   
9934  C CA  . TYR C 469 ? 0.8671 0.6847 0.8922 -0.0254 0.1022  0.2685  478 TYR C CA  
9935  C C   . TYR C 469 ? 0.8665 0.7000 0.8913 -0.0247 0.1039  0.2887  478 TYR C C   
9936  O O   . TYR C 469 ? 0.8702 0.7213 0.8980 -0.0383 0.1042  0.3034  478 TYR C O   
9937  C CB  . TYR C 469 ? 0.8359 0.6856 0.8629 -0.0176 0.1036  0.2545  478 TYR C CB  
9938  C CG  . TYR C 469 ? 0.8189 0.7064 0.8448 -0.0084 0.1056  0.2608  478 TYR C CG  
9939  C CD1 . TYR C 469 ? 0.7995 0.6911 0.8209 0.0080  0.1054  0.2582  478 TYR C CD1 
9940  C CD2 . TYR C 469 ? 0.8172 0.7381 0.8453 -0.0158 0.1072  0.2695  478 TYR C CD2 
9941  C CE1 . TYR C 469 ? 0.8020 0.7254 0.8196 0.0169  0.1060  0.2631  478 TYR C CE1 
9942  C CE2 . TYR C 469 ? 0.8115 0.7671 0.8360 -0.0049 0.1087  0.2746  478 TYR C CE2 
9943  C CZ  . TYR C 469 ? 0.8100 0.7647 0.8284 0.0114  0.1078  0.2708  478 TYR C CZ  
9944  O OH  . TYR C 469 ? 0.8087 0.7958 0.8209 0.0226  0.1082  0.2750  478 TYR C OH  
9945  N N   . ASP C 470 ? 0.8525 0.6820 0.8737 -0.0088 0.1050  0.2902  479 ASP C N   
9946  C CA  . ASP C 470 ? 0.8557 0.6955 0.8757 -0.0065 0.1064  0.3089  479 ASP C CA  
9947  C C   . ASP C 470 ? 0.8223 0.6916 0.8405 0.0105  0.1087  0.3088  479 ASP C C   
9948  O O   . ASP C 470 ? 0.8201 0.6786 0.8352 0.0244  0.1083  0.3029  479 ASP C O   
9949  C CB  . ASP C 470 ? 0.8933 0.6913 0.9083 -0.0072 0.1041  0.3180  479 ASP C CB  
9950  C CG  . ASP C 470 ? 0.9355 0.7406 0.9502 -0.0136 0.1044  0.3409  479 ASP C CG  
9951  O OD1 . ASP C 470 ? 0.9512 0.7874 0.9708 -0.0259 0.1054  0.3510  479 ASP C OD1 
9952  O OD2 . ASP C 470 ? 0.9805 0.7631 0.9898 -0.0060 0.1036  0.3496  479 ASP C OD2 
9953  N N   . PRO C 471 ? 0.7983 0.7064 0.8175 0.0099  0.1105  0.3162  480 PRO C N   
9954  C CA  . PRO C 471 ? 0.7667 0.7019 0.7814 0.0260  0.1109  0.3118  480 PRO C CA  
9955  C C   . PRO C 471 ? 0.7677 0.6974 0.7794 0.0358  0.1115  0.3229  480 PRO C C   
9956  O O   . PRO C 471 ? 0.7830 0.6975 0.7963 0.0293  0.1124  0.3383  480 PRO C O   
9957  C CB  . PRO C 471 ? 0.7610 0.7370 0.7757 0.0230  0.1128  0.3196  480 PRO C CB  
9958  C CG  . PRO C 471 ? 0.7915 0.7637 0.8120 0.0059  0.1141  0.3385  480 PRO C CG  
9959  C CD  . PRO C 471 ? 0.8103 0.7388 0.8335 -0.0051 0.1117  0.3321  480 PRO C CD  
9960  N N   . LEU C 472 ? 0.7468 0.6872 0.7533 0.0508  0.1101  0.3151  481 LEU C N   
9961  C CA  . LEU C 472 ? 0.7455 0.6898 0.7485 0.0618  0.1104  0.3254  481 LEU C CA  
9962  C C   . LEU C 472 ? 0.7356 0.7173 0.7345 0.0664  0.1115  0.3346  481 LEU C C   
9963  O O   . LEU C 472 ? 0.7200 0.7247 0.7139 0.0703  0.1098  0.3253  481 LEU C O   
9964  C CB  . LEU C 472 ? 0.7303 0.6686 0.7294 0.0742  0.1071  0.3132  481 LEU C CB  
9965  C CG  . LEU C 472 ? 0.7420 0.6704 0.7402 0.0833  0.1078  0.3234  481 LEU C CG  
9966  C CD1 . LEU C 472 ? 0.7776 0.6852 0.7789 0.0767  0.1110  0.3398  481 LEU C CD1 
9967  C CD2 . LEU C 472 ? 0.7153 0.6282 0.7133 0.0907  0.1052  0.3121  481 LEU C CD2 
9968  N N   . VAL C 473 ? 0.7466 0.7346 0.7460 0.0669  0.1139  0.3531  482 VAL C N   
9969  C CA  . VAL C 473 ? 0.7429 0.7700 0.7375 0.0730  0.1151  0.3622  482 VAL C CA  
9970  C C   . VAL C 473 ? 0.7527 0.7888 0.7433 0.0838  0.1157  0.3747  482 VAL C C   
9971  O O   . VAL C 473 ? 0.7721 0.7866 0.7663 0.0817  0.1169  0.3864  482 VAL C O   
9972  C CB  . VAL C 473 ? 0.7480 0.7979 0.7472 0.0605  0.1181  0.3735  482 VAL C CB  
9973  C CG1 . VAL C 473 ? 0.7508 0.8199 0.7517 0.0578  0.1211  0.3980  482 VAL C CG1 
9974  C CG2 . VAL C 473 ? 0.7321 0.8137 0.7251 0.0669  0.1171  0.3610  482 VAL C CG2 
9975  N N   . PHE C 474 ? 0.7382 0.8047 0.7195 0.0964  0.1140  0.3719  483 PHE C N   
9976  C CA  . PHE C 474 ? 0.7389 0.8140 0.7148 0.1082  0.1134  0.3802  483 PHE C CA  
9977  C C   . PHE C 474 ? 0.7490 0.8569 0.7234 0.1101  0.1169  0.3996  483 PHE C C   
9978  O O   . PHE C 474 ? 0.7478 0.8868 0.7183 0.1114  0.1178  0.3997  483 PHE C O   
9979  C CB  . PHE C 474 ? 0.7236 0.8050 0.6875 0.1218  0.1070  0.3639  483 PHE C CB  
9980  C CG  . PHE C 474 ? 0.7224 0.8089 0.6812 0.1326  0.1053  0.3713  483 PHE C CG  
9981  C CD1 . PHE C 474 ? 0.7125 0.7756 0.6754 0.1338  0.1041  0.3709  483 PHE C CD1 
9982  C CD2 . PHE C 474 ? 0.7283 0.8457 0.6783 0.1421  0.1053  0.3801  483 PHE C CD2 
9983  C CE1 . PHE C 474 ? 0.7170 0.7876 0.6758 0.1436  0.1027  0.3788  483 PHE C CE1 
9984  C CE2 . PHE C 474 ? 0.7320 0.8553 0.6773 0.1516  0.1037  0.3876  483 PHE C CE2 
9985  C CZ  . PHE C 474 ? 0.7315 0.8315 0.6817 0.1518  0.1023  0.3871  483 PHE C CZ  
9986  N N   . PRO C 475 ? 0.7599 0.8634 0.7368 0.1118  0.1189  0.4163  484 PRO C N   
9987  C CA  . PRO C 475 ? 0.7707 0.9046 0.7465 0.1140  0.1222  0.4372  484 PRO C CA  
9988  C C   . PRO C 475 ? 0.7652 0.9391 0.7283 0.1299  0.1205  0.4335  484 PRO C C   
9989  O O   . PRO C 475 ? 0.7766 0.9731 0.7366 0.1367  0.1222  0.4484  484 PRO C O   
9990  C CB  . PRO C 475 ? 0.7845 0.8967 0.7628 0.1166  0.1227  0.4494  484 PRO C CB  
9991  C CG  . PRO C 475 ? 0.7749 0.8548 0.7527 0.1210  0.1193  0.4324  484 PRO C CG  
9992  C CD  . PRO C 475 ? 0.7671 0.8337 0.7481 0.1115  0.1183  0.4171  484 PRO C CD  
9993  N N   . SER C 476 ? 0.7556 0.9372 0.7099 0.1362  0.1167  0.4140  485 SER C N   
9994  C CA  . SER C 476 ? 0.7564 0.9661 0.6933 0.1539  0.1124  0.4053  485 SER C CA  
9995  C C   . SER C 476 ? 0.7661 1.0151 0.6983 0.1621  0.1158  0.4231  485 SER C C   
9996  O O   . SER C 476 ? 0.7702 1.0285 0.6917 0.1753  0.1127  0.4236  485 SER C O   
9997  C CB  . SER C 476 ? 0.7509 0.9703 0.6793 0.1572  0.1095  0.3881  485 SER C CB  
9998  O OG  . SER C 476 ? 0.7610 1.0091 0.6695 0.1758  0.1052  0.3817  485 SER C OG  
9999  N N   . ASP C 477 ? 0.7732 1.0476 0.7134 0.1536  0.1218  0.4386  486 ASP C N   
10000 C CA  . ASP C 477 ? 0.7894 1.1075 0.7251 0.1617  0.1252  0.4566  486 ASP C CA  
10001 C C   . ASP C 477 ? 0.8006 1.1132 0.7396 0.1629  0.1264  0.4731  486 ASP C C   
10002 O O   . ASP C 477 ? 0.8031 1.1374 0.7298 0.1789  0.1246  0.4744  486 ASP C O   
10003 C CB  . ASP C 477 ? 0.7966 1.1459 0.7425 0.1493  0.1311  0.4733  486 ASP C CB  
10004 C CG  . ASP C 477 ? 0.8011 1.1813 0.7365 0.1592  0.1303  0.4603  486 ASP C CG  
10005 O OD1 . ASP C 477 ? 0.8050 1.1780 0.7235 0.1760  0.1243  0.4379  486 ASP C OD1 
10006 O OD2 . ASP C 477 ? 0.8221 1.2343 0.7650 0.1504  0.1348  0.4728  486 ASP C OD2 
10007 N N   . GLU C 478 ? 0.8076 1.0888 0.7612 0.1470  0.1288  0.4846  487 GLU C N   
10008 C CA  . GLU C 478 ? 0.8209 1.0929 0.7780 0.1475  0.1301  0.5015  487 GLU C CA  
10009 C C   . GLU C 478 ? 0.8053 1.0666 0.7518 0.1638  0.1253  0.4889  487 GLU C C   
10010 O O   . GLU C 478 ? 0.8131 1.0883 0.7559 0.1725  0.1257  0.5009  487 GLU C O   
10011 C CB  . GLU C 478 ? 0.8394 1.0692 0.8101 0.1295  0.1314  0.5107  487 GLU C CB  
10012 C CG  . GLU C 478 ? 0.8982 1.1217 0.8734 0.1264  0.1335  0.5352  487 GLU C CG  
10013 C CD  . GLU C 478 ? 0.9539 1.1255 0.9325 0.1240  0.1315  0.5322  487 GLU C CD  
10014 O OE1 . GLU C 478 ? 0.9856 1.1481 0.9649 0.1261  0.1323  0.5490  487 GLU C OE1 
10015 O OE2 . GLU C 478 ? 0.9558 1.0979 0.9356 0.1216  0.1293  0.5130  487 GLU C OE2 
10016 N N   . PHE C 479 ? 0.7788 1.0173 0.7204 0.1670  0.1201  0.4656  488 PHE C N   
10017 C CA  . PHE C 479 ? 0.7632 0.9936 0.6941 0.1799  0.1138  0.4530  488 PHE C CA  
10018 C C   . PHE C 479 ? 0.7584 1.0244 0.6710 0.1965  0.1098  0.4485  488 PHE C C   
10019 O O   . PHE C 479 ? 0.7636 1.0418 0.6696 0.2064  0.1081  0.4557  488 PHE C O   
10020 C CB  . PHE C 479 ? 0.7525 0.9528 0.6829 0.1764  0.1086  0.4306  488 PHE C CB  
10021 C CG  . PHE C 479 ? 0.7471 0.9358 0.6686 0.1852  0.1009  0.4187  488 PHE C CG  
10022 C CD1 . PHE C 479 ? 0.7468 0.9106 0.6772 0.1822  0.1011  0.4220  488 PHE C CD1 
10023 C CD2 . PHE C 479 ? 0.7362 0.9380 0.6389 0.1965  0.0922  0.4041  488 PHE C CD2 
10024 C CE1 . PHE C 479 ? 0.7377 0.8958 0.6610 0.1889  0.0935  0.4127  488 PHE C CE1 
10025 C CE2 . PHE C 479 ? 0.7324 0.9231 0.6263 0.2016  0.0832  0.3943  488 PHE C CE2 
10026 C CZ  . PHE C 479 ? 0.7278 0.8992 0.6335 0.1969  0.0842  0.3994  488 PHE C CZ  
10027 N N   . ASP C 480 ? 0.7488 1.0314 0.6516 0.2009  0.1078  0.4366  489 ASP C N   
10028 C CA  . ASP C 480 ? 0.7538 1.0688 0.6352 0.2194  0.1032  0.4306  489 ASP C CA  
10029 C C   . ASP C 480 ? 0.7635 1.1155 0.6437 0.2268  0.1081  0.4519  489 ASP C C   
10030 O O   . ASP C 480 ? 0.7696 1.1446 0.6307 0.2443  0.1034  0.4481  489 ASP C O   
10031 C CB  . ASP C 480 ? 0.7523 1.0850 0.6260 0.2228  0.1031  0.4203  489 ASP C CB  
10032 C CG  . ASP C 480 ? 0.7595 1.0611 0.6261 0.2216  0.0955  0.3957  489 ASP C CG  
10033 O OD1 . ASP C 480 ? 0.7818 1.0489 0.6528 0.2151  0.0911  0.3884  489 ASP C OD1 
10034 O OD2 . ASP C 480 ? 0.7690 1.0821 0.6254 0.2275  0.0937  0.3843  489 ASP C OD2 
10035 N N   . ALA C 481 ? 0.7648 1.1219 0.6640 0.2131  0.1169  0.4743  490 ALA C N   
10036 C CA  . ALA C 481 ? 0.7703 1.1602 0.6727 0.2156  0.1224  0.4992  490 ALA C CA  
10037 C C   . ALA C 481 ? 0.7730 1.1523 0.6719 0.2229  0.1196  0.5035  490 ALA C C   
10038 O O   . ALA C 481 ? 0.7788 1.1878 0.6651 0.2376  0.1181  0.5082  490 ALA C O   
10039 C CB  . ALA C 481 ? 0.7754 1.1617 0.6984 0.1953  0.1299  0.5212  490 ALA C CB  
10040 N N   . SER C 482 ? 0.7651 1.1032 0.6746 0.2135  0.1187  0.5014  491 SER C N   
10041 C CA  . SER C 482 ? 0.7658 1.0919 0.6731 0.2200  0.1157  0.5042  491 SER C CA  
10042 C C   . SER C 482 ? 0.7609 1.0995 0.6475 0.2366  0.1069  0.4880  491 SER C C   
10043 O O   . SER C 482 ? 0.7712 1.1271 0.6507 0.2468  0.1054  0.4964  491 SER C O   
10044 C CB  . SER C 482 ? 0.7600 1.0411 0.6784 0.2105  0.1147  0.4977  491 SER C CB  
10045 O OG  . SER C 482 ? 0.7783 1.0431 0.7121 0.1986  0.1212  0.5169  491 SER C OG  
10046 N N   . ILE C 483 ? 0.7485 1.0767 0.6244 0.2389  0.1001  0.4651  492 ILE C N   
10047 C CA  . ILE C 483 ? 0.7506 1.0819 0.6040 0.2527  0.0889  0.4482  492 ILE C CA  
10048 C C   . ILE C 483 ? 0.7634 1.1331 0.5971 0.2694  0.0872  0.4493  492 ILE C C   
10049 O O   . ILE C 483 ? 0.7757 1.1574 0.5954 0.2812  0.0816  0.4502  492 ILE C O   
10050 C CB  . ILE C 483 ? 0.7434 1.0491 0.5889 0.2499  0.0807  0.4243  492 ILE C CB  
10051 C CG1 . ILE C 483 ? 0.7399 1.0103 0.6033 0.2353  0.0819  0.4228  492 ILE C CG1 
10052 C CG2 . ILE C 483 ? 0.7510 1.0567 0.5699 0.2631  0.0668  0.4081  492 ILE C CG2 
10053 C CD1 . ILE C 483 ? 0.7559 1.0040 0.6091 0.2356  0.0698  0.4053  492 ILE C CD1 
10054 N N   . SER C 484 ? 0.7639 1.1551 0.5955 0.2717  0.0916  0.4491  493 SER C N   
10055 C CA  . SER C 484 ? 0.7740 1.2086 0.5876 0.2897  0.0916  0.4529  493 SER C CA  
10056 C C   . SER C 484 ? 0.7827 1.2421 0.6023 0.2927  0.0970  0.4763  493 SER C C   
10057 O O   . SER C 484 ? 0.8001 1.2950 0.6033 0.3095  0.0958  0.4804  493 SER C O   
10058 C CB  . SER C 484 ? 0.7702 1.2327 0.5876 0.2892  0.0989  0.4573  493 SER C CB  
10059 O OG  . SER C 484 ? 0.7767 1.2849 0.5745 0.3098  0.0986  0.4600  493 SER C OG  
10060 N N   . GLN C 485 ? 0.7747 1.2133 0.6161 0.2775  0.1022  0.4906  494 GLN C N   
10061 C CA  . GLN C 485 ? 0.7799 1.2355 0.6296 0.2779  0.1076  0.5143  494 GLN C CA  
10062 C C   . GLN C 485 ? 0.7740 1.2122 0.6182 0.2828  0.1009  0.5109  494 GLN C C   
10063 O O   . GLN C 485 ? 0.7844 1.2440 0.6269 0.2899  0.1026  0.5261  494 GLN C O   
10064 C CB  . GLN C 485 ? 0.7825 1.2272 0.6577 0.2588  0.1174  0.5352  494 GLN C CB  
10065 C CG  . GLN C 485 ? 0.8223 1.3004 0.7046 0.2585  0.1248  0.5640  494 GLN C CG  
10066 C CD  . GLN C 485 ? 0.8687 1.3247 0.7617 0.2535  0.1262  0.5787  494 GLN C CD  
10067 O OE1 . GLN C 485 ? 0.8644 1.2777 0.7672 0.2439  0.1252  0.5730  494 GLN C OE1 
10068 N NE2 . GLN C 485 ? 0.8996 1.3857 0.7898 0.2616  0.1286  0.5980  494 GLN C NE2 
10069 N N   . VAL C 486 ? 0.7606 1.1634 0.6026 0.2788  0.0932  0.4922  495 VAL C N   
10070 C CA  . VAL C 486 ? 0.7559 1.1488 0.5890 0.2844  0.0846  0.4869  495 VAL C CA  
10071 C C   . VAL C 486 ? 0.7691 1.1864 0.5742 0.3022  0.0753  0.4771  495 VAL C C   
10072 O O   . VAL C 486 ? 0.7769 1.2065 0.5732 0.3105  0.0711  0.4825  495 VAL C O   
10073 C CB  . VAL C 486 ? 0.7434 1.0977 0.5796 0.2752  0.0775  0.4697  495 VAL C CB  
10074 C CG1 . VAL C 486 ? 0.7442 1.0951 0.5611 0.2827  0.0637  0.4568  495 VAL C CG1 
10075 C CG2 . VAL C 486 ? 0.7297 1.0626 0.5894 0.2635  0.0848  0.4823  495 VAL C CG2 
10076 N N   . ASN C 487 ? 0.7742 1.1991 0.5638 0.3093  0.0719  0.4628  496 ASN C N   
10077 C CA  . ASN C 487 ? 0.7972 1.2429 0.5564 0.3288  0.0625  0.4520  496 ASN C CA  
10078 C C   . ASN C 487 ? 0.8108 1.3022 0.5670 0.3413  0.0697  0.4714  496 ASN C C   
10079 O O   . ASN C 487 ? 0.8244 1.3327 0.5570 0.3578  0.0617  0.4671  496 ASN C O   
10080 C CB  . ASN C 487 ? 0.8014 1.2404 0.5436 0.3348  0.0569  0.4313  496 ASN C CB  
10081 C CG  . ASN C 487 ? 0.8050 1.1994 0.5501 0.3216  0.0491  0.4132  496 ASN C CG  
10082 O OD1 . ASN C 487 ? 0.8111 1.1816 0.5504 0.3175  0.0386  0.4055  496 ASN C OD1 
10083 N ND2 . ASN C 487 ? 0.8172 1.2023 0.5722 0.3140  0.0542  0.4078  496 ASN C ND2 
10084 N N   . GLU C 488 ? 0.8081 1.3189 0.5875 0.3327  0.0839  0.4936  497 GLU C N   
10085 C CA  . GLU C 488 ? 0.8155 1.3679 0.5989 0.3394  0.0919  0.5180  497 GLU C CA  
10086 C C   . GLU C 488 ? 0.8247 1.3724 0.6008 0.3452  0.0855  0.5200  497 GLU C C   
10087 O O   . GLU C 488 ? 0.8424 1.4179 0.5979 0.3624  0.0808  0.5195  497 GLU C O   
10088 C CB  . GLU C 488 ? 0.8081 1.3636 0.6220 0.3216  0.1053  0.5443  497 GLU C CB  
10089 C CG  . GLU C 488 ? 0.8002 1.3765 0.6229 0.3155  0.1132  0.5515  497 GLU C CG  
10090 C CD  . GLU C 488 ? 0.8037 1.4231 0.6035 0.3358  0.1112  0.5446  497 GLU C CD  
10091 O OE1 . GLU C 488 ? 0.8051 1.4394 0.5828 0.3545  0.1043  0.5380  497 GLU C OE1 
10092 O OE2 . GLU C 488 ? 0.8022 1.4408 0.6049 0.3339  0.1158  0.5453  497 GLU C OE2 
10093 N N   . LYS C 489 ? 0.8175 1.3310 0.6093 0.3316  0.0849  0.5214  498 LYS C N   
10094 C CA  . LYS C 489 ? 0.8281 1.3402 0.6190 0.3345  0.0811  0.5287  498 LYS C CA  
10095 C C   . LYS C 489 ? 0.8394 1.3482 0.6027 0.3463  0.0656  0.5091  498 LYS C C   
10096 O O   . LYS C 489 ? 0.8532 1.3829 0.6055 0.3568  0.0621  0.5159  498 LYS C O   
10097 C CB  . LYS C 489 ? 0.8190 1.2967 0.6323 0.3189  0.0840  0.5340  498 LYS C CB  
10098 C CG  . LYS C 489 ? 0.8270 1.2965 0.6644 0.3055  0.0965  0.5498  498 LYS C CG  
10099 C CD  . LYS C 489 ? 0.8605 1.3517 0.7089 0.3062  0.1053  0.5781  498 LYS C CD  
10100 C CE  . LYS C 489 ? 0.8802 1.3593 0.7497 0.2910  0.1154  0.5941  498 LYS C CE  
10101 N NZ  . LYS C 489 ? 0.9220 1.4248 0.7987 0.2919  0.1224  0.6231  498 LYS C NZ  
10102 N N   . ILE C 490 ? 0.8422 1.3231 0.5932 0.3438  0.0552  0.4853  499 ILE C N   
10103 C CA  . ILE C 490 ? 0.8636 1.3376 0.5850 0.3537  0.0380  0.4666  499 ILE C CA  
10104 C C   . ILE C 490 ? 0.8962 1.4041 0.5908 0.3751  0.0352  0.4642  499 ILE C C   
10105 O O   . ILE C 490 ? 0.9081 1.4343 0.5871 0.3864  0.0293  0.4679  499 ILE C O   
10106 C CB  . ILE C 490 ? 0.8597 1.2956 0.5710 0.3462  0.0262  0.4420  499 ILE C CB  
10107 C CG1 . ILE C 490 ? 0.8282 1.2360 0.5682 0.3262  0.0318  0.4457  499 ILE C CG1 
10108 C CG2 . ILE C 490 ? 0.8760 1.2987 0.5572 0.3520  0.0061  0.4254  499 ILE C CG2 
10109 C CD1 . ILE C 490 ? 0.8068 1.1827 0.5440 0.3174  0.0257  0.4257  499 ILE C CD1 
10110 N N   . ASN C 491 ? 0.9135 1.4325 0.6030 0.3815  0.0399  0.4587  500 ASN C N   
10111 C CA  . ASN C 491 ? 0.9525 1.5094 0.6178 0.4041  0.0394  0.4577  500 ASN C CA  
10112 C C   . ASN C 491 ? 0.9453 1.5414 0.6149 0.4118  0.0462  0.4805  500 ASN C C   
10113 O O   . ASN C 491 ? 0.9651 1.5837 0.6074 0.4315  0.0388  0.4760  500 ASN C O   
10114 C CB  . ASN C 491 ? 0.9640 1.5394 0.6350 0.4067  0.0494  0.4588  500 ASN C CB  
10115 C CG  . ASN C 491 ? 1.0789 1.6372 0.7197 0.4194  0.0372  0.4308  500 ASN C CG  
10116 O OD1 . ASN C 491 ? 1.1012 1.6280 0.7175 0.4233  0.0203  0.4108  500 ASN C OD1 
10117 N ND2 . ASN C 491 ? 1.2613 1.8407 0.9026 0.4256  0.0448  0.4300  500 ASN C ND2 
10118 N N   . GLN C 492 ? 0.9195 1.5203 0.6219 0.3965  0.0593  0.5044  501 GLN C N   
10119 C CA  . GLN C 492 ? 0.9190 1.5542 0.6307 0.4004  0.0674  0.5297  501 GLN C CA  
10120 C C   . GLN C 492 ? 0.9183 1.5464 0.6174 0.4052  0.0567  0.5268  501 GLN C C   
10121 O O   . GLN C 492 ? 0.9292 1.5905 0.6153 0.4196  0.0558  0.5358  501 GLN C O   
10122 C CB  . GLN C 492 ? 0.9074 1.5355 0.6557 0.3805  0.0817  0.5531  501 GLN C CB  
10123 C CG  . GLN C 492 ? 0.9391 1.6057 0.7018 0.3813  0.0937  0.5843  501 GLN C CG  
10124 C CD  . GLN C 492 ? 0.9636 1.6212 0.7568 0.3616  0.1064  0.6037  501 GLN C CD  
10125 O OE1 . GLN C 492 ? 0.9594 1.5760 0.7692 0.3461  0.1071  0.6015  501 GLN C OE1 
10126 N NE2 . GLN C 492 ? 0.9871 1.6838 0.7864 0.3621  0.1156  0.6228  501 GLN C NE2 
10127 N N   . SER C 493 ? 0.9001 1.4872 0.6037 0.3924  0.0487  0.5148  502 SER C N   
10128 C CA  . SER C 493 ? 0.8945 1.4717 0.5928 0.3911  0.0389  0.5142  502 SER C CA  
10129 C C   . SER C 493 ? 0.9132 1.4947 0.5733 0.4070  0.0216  0.4955  502 SER C C   
10130 O O   . SER C 493 ? 0.9253 1.5272 0.5745 0.4160  0.0172  0.5026  502 SER C O   
10131 C CB  . SER C 493 ? 0.8786 1.4142 0.5913 0.3729  0.0346  0.5057  502 SER C CB  
10132 O OG  . SER C 493 ? 0.8732 1.4054 0.5856 0.3701  0.0271  0.5095  502 SER C OG  
10133 N N   . LEU C 494 ? 0.9144 1.4748 0.5526 0.4109  0.0110  0.4714  503 LEU C N   
10134 C CA  . LEU C 494 ? 0.9394 1.4976 0.5359 0.4277  -0.0073 0.4512  503 LEU C CA  
10135 C C   . LEU C 494 ? 0.9569 1.5603 0.5361 0.4504  -0.0039 0.4600  503 LEU C C   
10136 O O   . LEU C 494 ? 0.9801 1.5896 0.5332 0.4617  -0.0168 0.4546  503 LEU C O   
10137 C CB  . LEU C 494 ? 0.9466 1.4801 0.5234 0.4318  -0.0154 0.4273  503 LEU C CB  
10138 C CG  . LEU C 494 ? 0.9381 1.4251 0.5246 0.4112  -0.0226 0.4146  503 LEU C CG  
10139 C CD1 . LEU C 494 ? 0.9552 1.4201 0.5192 0.4182  -0.0306 0.3913  503 LEU C CD1 
10140 C CD2 . LEU C 494 ? 0.9509 1.4154 0.5246 0.4028  -0.0406 0.4081  503 LEU C CD2 
10141 N N   . ALA C 495 ? 0.9473 1.5836 0.5411 0.4561  0.0129  0.4742  504 ALA C N   
10142 C CA  . ALA C 495 ? 0.9565 1.6444 0.5387 0.4771  0.0194  0.4868  504 ALA C CA  
10143 C C   . ALA C 495 ? 0.9524 1.6645 0.5452 0.4764  0.0234  0.5085  504 ALA C C   
10144 O O   . ALA C 495 ? 0.9732 1.7174 0.5435 0.4958  0.0195  0.5107  504 ALA C O   
10145 C CB  . ALA C 495 ? 0.9433 1.6635 0.5448 0.4780  0.0372  0.5016  504 ALA C CB  
10146 N N   . PHE C 496 ? 0.9259 1.6228 0.5513 0.4558  0.0309  0.5242  505 PHE C N   
10147 C CA  . PHE C 496 ? 0.9240 1.6385 0.5587 0.4549  0.0332  0.5434  505 PHE C CA  
10148 C C   . PHE C 496 ? 0.9395 1.6419 0.5457 0.4615  0.0140  0.5279  505 PHE C C   
10149 O O   . PHE C 496 ? 0.9528 1.6846 0.5477 0.4735  0.0120  0.5372  505 PHE C O   
10150 C CB  . PHE C 496 ? 0.9037 1.5998 0.5761 0.4335  0.0440  0.5612  505 PHE C CB  
10151 C CG  . PHE C 496 ? 0.9056 1.6266 0.6054 0.4288  0.0628  0.5886  505 PHE C CG  
10152 C CD1 . PHE C 496 ? 0.9126 1.6144 0.6351 0.4139  0.0723  0.5920  505 PHE C CD1 
10153 C CD2 . PHE C 496 ? 0.9202 1.6828 0.6225 0.4380  0.0701  0.6119  505 PHE C CD2 
10154 C CE1 . PHE C 496 ? 0.9125 1.6343 0.6588 0.4070  0.0878  0.6186  505 PHE C CE1 
10155 C CE2 . PHE C 496 ? 0.9163 1.7000 0.6432 0.4311  0.0860  0.6392  505 PHE C CE2 
10156 C CZ  . PHE C 496 ? 0.9072 1.6693 0.6556 0.4150  0.0942  0.6427  505 PHE C CZ  
10157 N N   . ILE C 497 ? 0.9405 1.6005 0.5346 0.4528  -0.0009 0.5051  506 ILE C N   
10158 C CA  . ILE C 497 ? 0.9636 1.6075 0.5279 0.4560  -0.0223 0.4890  506 ILE C CA  
10159 C C   . ILE C 497 ? 1.0023 1.6606 0.5231 0.4806  -0.0345 0.4733  506 ILE C C   
10160 O O   . ILE C 497 ? 1.0227 1.6982 0.5238 0.4912  -0.0433 0.4750  506 ILE C O   
10161 C CB  . ILE C 497 ? 0.9591 1.5534 0.5203 0.4385  -0.0365 0.4694  506 ILE C CB  
10162 C CG1 . ILE C 497 ? 0.9294 1.5118 0.5304 0.4165  -0.0262 0.4847  506 ILE C CG1 
10163 C CG2 . ILE C 497 ? 0.9797 1.5557 0.5049 0.4407  -0.0618 0.4519  506 ILE C CG2 
10164 C CD1 . ILE C 497 ? 0.9283 1.5290 0.5406 0.4131  -0.0257 0.5029  506 ILE C CD1 
10165 N N   . ARG C 498 ? 1.0164 1.6676 0.5213 0.4908  -0.0353 0.4576  507 ARG C N   
10166 C CA  . ARG C 498 ? 1.0574 1.7285 0.5221 0.5190  -0.0431 0.4444  507 ARG C CA  
10167 C C   . ARG C 498 ? 1.0649 1.7869 0.5252 0.5355  -0.0370 0.4628  507 ARG C C   
10168 O O   . ARG C 498 ? 1.0910 1.8174 0.5145 0.5522  -0.0525 0.4516  507 ARG C O   
10169 C CB  . ARG C 498 ? 1.0564 1.7406 0.5247 0.5282  -0.0312 0.4418  507 ARG C CB  
10170 C CG  . ARG C 498 ? 1.0945 1.7330 0.5529 0.5221  -0.0399 0.4176  507 ARG C CG  
10171 C CD  . ARG C 498 ? 1.1614 1.8238 0.5982 0.5470  -0.0361 0.4085  507 ARG C CD  
10172 N NE  . ARG C 498 ? 1.2501 1.9519 0.6570 0.5745  -0.0400 0.4105  507 ARG C NE  
10173 C CZ  . ARG C 498 ? 1.2861 2.0305 0.6737 0.6022  -0.0345 0.4104  507 ARG C CZ  
10174 N NH1 . ARG C 498 ? 1.2829 2.0383 0.6772 0.6070  -0.0246 0.4084  507 ARG C NH1 
10175 N NH2 . ARG C 498 ? 1.3044 2.0832 0.6649 0.6262  -0.0390 0.4126  507 ARG C NH2 
10176 N N   . LYS C 499 ? 1.0409 1.7992 0.5381 0.5297  -0.0150 0.4913  508 LYS C N   
10177 C CA  . LYS C 499 ? 1.0466 1.8566 0.5475 0.5421  -0.0056 0.5140  508 LYS C CA  
10178 C C   . LYS C 499 ? 1.0505 1.8565 0.5492 0.5366  -0.0147 0.5197  508 LYS C C   
10179 O O   . LYS C 499 ? 1.0727 1.9100 0.5510 0.5538  -0.0190 0.5239  508 LYS C O   
10180 C CB  . LYS C 499 ? 1.0208 1.8615 0.5642 0.5316  0.0187  0.5446  508 LYS C CB  
10181 C CG  . LYS C 499 ? 1.0473 1.9458 0.5966 0.5437  0.0300  0.5718  508 LYS C CG  
10182 C CD  . LYS C 499 ? 1.0884 2.0383 0.6259 0.5650  0.0388  0.5775  508 LYS C CD  
10183 C CE  . LYS C 499 ? 1.1283 2.0986 0.6167 0.5968  0.0246  0.5574  508 LYS C CE  
10184 N NZ  . LYS C 499 ? 1.1291 2.1237 0.6015 0.6090  0.0184  0.5644  508 LYS C NZ  
10185 N N   . SER C 500 ? 1.0307 1.8015 0.5508 0.5133  -0.0173 0.5206  509 SER C N   
10186 C CA  . SER C 500 ? 1.0344 1.8010 0.5535 0.5064  -0.0268 0.5256  509 SER C CA  
10187 C C   . SER C 500 ? 1.0728 1.8245 0.5455 0.5180  -0.0519 0.5013  509 SER C C   
10188 O O   . SER C 500 ? 1.0885 1.8630 0.5459 0.5277  -0.0584 0.5067  509 SER C O   
10189 C CB  . SER C 500 ? 1.0095 1.7409 0.5576 0.4805  -0.0261 0.5283  509 SER C CB  
10190 O OG  . SER C 500 ? 1.0070 1.7398 0.5553 0.4741  -0.0349 0.5347  509 SER C OG  
10191 N N   . ASP C 501 ? 1.0928 1.8047 0.5417 0.5168  -0.0668 0.4747  510 ASP C N   
10192 C CA  . ASP C 501 ? 1.1394 1.8269 0.5403 0.5262  -0.0936 0.4496  510 ASP C CA  
10193 C C   . ASP C 501 ? 1.1744 1.8944 0.5385 0.5568  -0.0981 0.4447  510 ASP C C   
10194 O O   . ASP C 501 ? 1.2043 1.9254 0.5398 0.5638  -0.1147 0.4390  510 ASP C O   
10195 C CB  . ASP C 501 ? 1.1539 1.7916 0.5358 0.5208  -0.1074 0.4230  510 ASP C CB  
10196 C CG  . ASP C 501 ? 1.1503 1.7481 0.5510 0.4910  -0.1155 0.4207  510 ASP C CG  
10197 O OD1 . ASP C 501 ? 1.1760 1.7683 0.5704 0.4809  -0.1292 0.4229  510 ASP C OD1 
10198 O OD2 . ASP C 501 ? 1.1377 1.7121 0.5589 0.4778  -0.1086 0.4171  510 ASP C OD2 
10199 N N   . GLU C 502 ? 1.1759 1.9243 0.5398 0.5752  -0.0838 0.4473  511 GLU C N   
10200 C CA  . GLU C 502 ? 1.2112 1.9997 0.5424 0.6070  -0.0852 0.4454  511 GLU C CA  
10201 C C   . GLU C 502 ? 1.2108 2.0343 0.5468 0.6092  -0.0834 0.4646  511 GLU C C   
10202 O O   . GLU C 502 ? 1.2485 2.0757 0.5453 0.6259  -0.1004 0.4532  511 GLU C O   
10203 C CB  . GLU C 502 ? 1.2011 2.0326 0.5465 0.6219  -0.0635 0.4574  511 GLU C CB  
10204 C CG  . GLU C 502 ? 1.2469 2.0552 0.5691 0.6338  -0.0690 0.4332  511 GLU C CG  
10205 C CD  . GLU C 502 ? 1.2613 2.1134 0.6060 0.6423  -0.0459 0.4483  511 GLU C CD  
10206 O OE1 . GLU C 502 ? 1.2748 2.1866 0.6259 0.6571  -0.0323 0.4692  511 GLU C OE1 
10207 O OE2 . GLU C 502 ? 1.2387 2.0668 0.5938 0.6337  -0.0424 0.4396  511 GLU C OE2 
10208 N N   . LEU C 503 ? 1.1712 2.0174 0.5540 0.5922  -0.0640 0.4935  512 LEU C N   
10209 C CA  . LEU C 503 ? 1.1689 2.0506 0.5602 0.5941  -0.0600 0.5145  512 LEU C CA  
10210 C C   . LEU C 503 ? 1.1910 2.0467 0.5581 0.5881  -0.0832 0.5019  512 LEU C C   
10211 O O   . LEU C 503 ? 1.2118 2.0963 0.5652 0.5990  -0.0877 0.5095  512 LEU C O   
10212 C CB  . LEU C 503 ? 1.1291 2.0280 0.5738 0.5747  -0.0374 0.5461  512 LEU C CB  
10213 C CG  . LEU C 503 ? 1.1165 2.0524 0.5837 0.5812  -0.0147 0.5648  512 LEU C CG  
10214 C CD1 . LEU C 503 ? 1.0840 2.0233 0.6010 0.5593  0.0045  0.5935  512 LEU C CD1 
10215 C CD2 . LEU C 503 ? 1.1396 2.1333 0.5865 0.6085  -0.0106 0.5745  512 LEU C CD2 
10216 N N   . LEU C 504 ? 1.1924 1.9955 0.5529 0.5704  -0.0990 0.4830  513 LEU C N   
10217 C CA  . LEU C 504 ? 1.2137 1.9921 0.5554 0.5591  -0.1218 0.4740  513 LEU C CA  
10218 C C   . LEU C 504 ? 1.2695 2.0235 0.5523 0.5752  -0.1497 0.4450  513 LEU C C   
10219 O O   . LEU C 504 ? 1.2923 2.0452 0.5518 0.5750  -0.1674 0.4418  513 LEU C O   
10220 C CB  . LEU C 504 ? 1.1894 1.9274 0.5559 0.5289  -0.1255 0.4722  513 LEU C CB  
10221 C CG  . LEU C 504 ? 1.1371 1.8949 0.5588 0.5132  -0.1006 0.5006  513 LEU C CG  
10222 C CD1 . LEU C 504 ? 1.1222 1.8405 0.5667 0.4914  -0.0985 0.4942  513 LEU C CD1 
10223 C CD2 . LEU C 504 ? 1.1173 1.8966 0.5532 0.5048  -0.1016 0.5195  513 LEU C CD2 
10224 N N   . HIS C 505 ? 1.2955 2.0285 0.5524 0.5895  -0.1544 0.4238  514 HIS C N   
10225 C CA  . HIS C 505 ? 1.3630 2.0747 0.5588 0.6119  -0.1797 0.3960  514 HIS C CA  
10226 C C   . HIS C 505 ? 1.3903 2.1555 0.5657 0.6443  -0.1733 0.4028  514 HIS C C   
10227 O O   . HIS C 505 ? 1.4380 2.1969 0.5618 0.6716  -0.1893 0.3813  514 HIS C O   
10228 C CB  . HIS C 505 ? 1.3758 2.0475 0.5496 0.6187  -0.1870 0.3713  514 HIS C CB  
10229 C CG  . HIS C 505 ? 1.3746 1.9962 0.5679 0.5874  -0.1933 0.3652  514 HIS C CG  
10230 N ND1 . HIS C 505 ? 1.3898 1.9791 0.5809 0.5620  -0.2126 0.3627  514 HIS C ND1 
10231 C CD2 . HIS C 505 ? 1.3590 1.9600 0.5740 0.5774  -0.1832 0.3615  514 HIS C CD2 
10232 C CE1 . HIS C 505 ? 1.3702 1.9224 0.5809 0.5382  -0.2138 0.3582  514 HIS C CE1 
10233 N NE2 . HIS C 505 ? 1.3499 1.9069 0.5751 0.5473  -0.1962 0.3567  514 HIS C NE2 
10234 N N   . ASN C 506 ? 1.3664 2.1837 0.5818 0.6415  -0.1500 0.4334  515 ASN C N   
10235 C CA  . ASN C 506 ? 1.3878 2.2606 0.5910 0.6669  -0.1431 0.4455  515 ASN C CA  
10236 C C   . ASN C 506 ? 1.3888 2.2779 0.6027 0.6549  -0.1471 0.4621  515 ASN C C   
10237 O O   . ASN C 506 ? 1.3888 2.3303 0.6083 0.6691  -0.1359 0.4812  515 ASN C O   
10238 C CB  . ASN C 506 ? 1.3555 2.2805 0.5961 0.6745  -0.1121 0.4704  515 ASN C CB  
10239 C CG  . ASN C 506 ? 1.3890 2.3494 0.5967 0.7105  -0.1097 0.4623  515 ASN C CG  
10240 O OD1 . ASN C 506 ? 1.3939 2.3456 0.5961 0.7190  -0.1056 0.4509  515 ASN C OD1 
10241 N ND2 . ASN C 506 ? 1.4066 2.4090 0.5910 0.7333  -0.1124 0.4679  515 ASN C ND2 
10242 N N   . VAL C 507 ? 1.3925 2.2393 0.6097 0.6285  -0.1632 0.4558  516 VAL C N   
10243 C CA  . VAL C 507 ? 1.3895 2.2492 0.6200 0.6131  -0.1681 0.4717  516 VAL C CA  
10244 C C   . VAL C 507 ? 1.4345 2.2524 0.6208 0.6058  -0.2027 0.4486  516 VAL C C   
10245 O O   . VAL C 507 ? 1.4443 2.2095 0.6195 0.5893  -0.2191 0.4300  516 VAL C O   
10246 C CB  . VAL C 507 ? 1.3388 2.2003 0.6283 0.5838  -0.1497 0.4961  516 VAL C CB  
10247 C CG1 . VAL C 507 ? 1.3338 2.1999 0.6321 0.5663  -0.1597 0.5078  516 VAL C CG1 
10248 C CG2 . VAL C 507 ? 1.2963 2.2040 0.6267 0.5908  -0.1179 0.5238  516 VAL C CG2 
10249 N N   . ASN C 508 ? 1.4597 2.3010 0.6208 0.6169  -0.2143 0.4510  517 ASN C N   
10250 C CA  . ASN C 508 ? 1.5094 2.3125 0.6186 0.6150  -0.2496 0.4271  517 ASN C CA  
10251 C C   . ASN C 508 ? 1.5263 2.3643 0.6182 0.6239  -0.2583 0.4362  517 ASN C C   
10252 O O   . ASN C 508 ? 1.4910 2.3746 0.6207 0.6184  -0.2400 0.4642  517 ASN C O   
10253 C CB  . ASN C 508 ? 1.5567 2.3232 0.6117 0.6388  -0.2665 0.3945  517 ASN C CB  
10254 C CG  . ASN C 508 ? 1.6182 2.3227 0.6209 0.6292  -0.3057 0.3664  517 ASN C CG  
10255 O OD1 . ASN C 508 ? 1.6500 2.3501 0.6453 0.6121  -0.3234 0.3704  517 ASN C OD1 
10256 N ND2 . ASN C 508 ? 1.6456 2.3019 0.6102 0.6402  -0.3206 0.3384  517 ASN C ND2 
# 
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   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   ILE 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   LYS 7   7   ?   ?   ?   A . n 
A 1 8   ALA 8   8   ?   ?   ?   A . n 
A 1 9   ASN 9   9   ?   ?   ?   A . n 
A 1 10  ALA 10  10  ?   ?   ?   A . n 
A 1 11  ILE 11  11  ?   ?   ?   A . n 
A 1 12  THR 12  12  ?   ?   ?   A . n 
A 1 13  THR 13  13  ?   ?   ?   A . n 
A 1 14  ILE 14  14  ?   ?   ?   A . n 
A 1 15  LEU 15  15  ?   ?   ?   A . n 
A 1 16  THR 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  VAL 18  18  ?   ?   ?   A . n 
A 1 19  THR 19  19  ?   ?   ?   A . n 
A 1 20  PHE 20  20  ?   ?   ?   A . n 
A 1 21  CYS 21  21  ?   ?   ?   A . n 
A 1 22  PHE 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  SER 24  24  ?   ?   ?   A . n 
A 1 25  GLY 25  25  ?   ?   ?   A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  TRP 52  52  52  TRP TRP A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  CYS 69  69  69  CYS CYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  MET 97  97  97  MET MET A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  SER 99  108 ?   ?   ?   A . n 
A 1 100 THR 100 109 ?   ?   ?   A . n 
A 1 101 PRO 101 110 ?   ?   ?   A . n 
A 1 102 ALA 102 111 ?   ?   ?   A . n 
A 1 103 THR 103 112 ?   ?   ?   A . n 
A 1 104 ASN 104 113 ?   ?   ?   A . n 
A 1 105 ASN 105 114 ?   ?   ?   A . n 
A 1 106 ARG 106 115 ?   ?   ?   A . n 
A 1 107 ALA 107 116 ?   ?   ?   A . n 
A 1 108 ARG 108 117 ?   ?   ?   A . n 
A 1 109 ARG 109 118 ?   ?   ?   A . n 
A 1 110 GLU 110 119 ?   ?   ?   A . n 
A 1 111 LEU 111 120 ?   ?   ?   A . n 
A 1 112 PRO 112 121 ?   ?   ?   A . n 
A 1 113 ARG 113 122 ?   ?   ?   A . n 
A 1 114 PHE 114 123 ?   ?   ?   A . n 
A 1 115 MET 115 124 ?   ?   ?   A . n 
A 1 116 ASN 116 125 ?   ?   ?   A . n 
A 1 117 TYR 117 126 ?   ?   ?   A . n 
A 1 118 THR 118 127 ?   ?   ?   A . n 
A 1 119 LEU 119 128 ?   ?   ?   A . n 
A 1 120 ASN 120 129 ?   ?   ?   A . n 
A 1 121 ASN 121 130 ?   ?   ?   A . n 
A 1 122 ALA 122 131 ?   ?   ?   A . n 
A 1 123 LYS 123 132 ?   ?   ?   A . n 
A 1 124 LYS 124 133 ?   ?   ?   A . n 
A 1 125 THR 125 134 ?   ?   ?   A . n 
A 1 126 ASN 126 135 ?   ?   ?   A . n 
A 1 127 VAL 127 136 ?   ?   ?   A . n 
A 1 128 THR 128 137 ?   ?   ?   A . n 
A 1 129 LEU 129 138 ?   ?   ?   A . n 
A 1 130 SER 130 139 ?   ?   ?   A . n 
A 1 131 LYS 131 140 ?   ?   ?   A . n 
A 1 132 LYS 132 141 ?   ?   ?   A . n 
A 1 133 ARG 133 142 ?   ?   ?   A . n 
A 1 134 LYS 134 143 ?   ?   ?   A . n 
A 1 135 ARG 135 144 ?   ?   ?   A . n 
A 1 136 ARG 136 145 ?   ?   ?   A . n 
A 1 137 SER 137 146 146 SER SER A . n 
A 1 138 ALA 138 147 147 ALA ALA A . n 
A 1 139 ILE 139 148 148 ILE ILE A . n 
A 1 140 ALA 140 149 149 ALA ALA A . n 
A 1 141 SER 141 150 150 SER SER A . n 
A 1 142 GLY 142 151 151 GLY GLY A . n 
A 1 143 VAL 143 152 152 VAL VAL A . n 
A 1 144 ALA 144 153 153 ALA ALA A . n 
A 1 145 VAL 145 154 154 VAL VAL A . n 
A 1 146 SER 146 155 155 SER SER A . n 
A 1 147 LYS 147 156 156 LYS LYS A . n 
A 1 148 VAL 148 157 157 VAL VAL A . n 
A 1 149 LEU 149 158 158 LEU LEU A . n 
A 1 150 HIS 150 159 159 HIS HIS A . n 
A 1 151 LEU 151 160 160 LEU LEU A . n 
A 1 152 GLU 152 161 161 GLU GLU A . n 
A 1 153 GLY 153 162 162 GLY GLY A . n 
A 1 154 GLU 154 163 163 GLU GLU A . n 
A 1 155 VAL 155 164 164 VAL VAL A . n 
A 1 156 ASN 156 165 165 ASN ASN A . n 
A 1 157 LYS 157 166 166 LYS LYS A . n 
A 1 158 ILE 158 167 167 ILE ILE A . n 
A 1 159 LYS 159 168 168 LYS LYS A . n 
A 1 160 SER 160 169 169 SER SER A . n 
A 1 161 ALA 161 170 170 ALA ALA A . n 
A 1 162 LEU 162 171 171 LEU LEU A . n 
A 1 163 LEU 163 172 172 LEU LEU A . n 
A 1 164 SER 164 173 173 SER SER A . n 
A 1 165 THR 165 174 174 THR THR A . n 
A 1 166 ASN 166 175 175 ASN ASN A . n 
A 1 167 LYS 167 176 176 LYS LYS A . n 
A 1 168 ALA 168 177 177 ALA ALA A . n 
A 1 169 VAL 169 178 178 VAL VAL A . n 
A 1 170 VAL 170 179 179 VAL VAL A . n 
A 1 171 SER 171 180 180 SER SER A . n 
A 1 172 LEU 172 181 181 LEU LEU A . n 
A 1 173 SER 173 182 182 SER SER A . n 
A 1 174 ASN 174 183 183 ASN ASN A . n 
A 1 175 GLY 175 184 184 GLY GLY A . n 
A 1 176 VAL 176 185 185 VAL VAL A . n 
A 1 177 SER 177 186 186 SER SER A . n 
A 1 178 VAL 178 187 187 VAL VAL A . n 
A 1 179 LEU 179 188 188 LEU LEU A . n 
A 1 180 THR 180 189 189 THR THR A . n 
A 1 181 SER 181 190 190 SER SER A . n 
A 1 182 LYS 182 191 191 LYS LYS A . n 
A 1 183 VAL 183 192 192 VAL VAL A . n 
A 1 184 LEU 184 193 193 LEU LEU A . n 
A 1 185 ASP 185 194 194 ASP ASP A . n 
A 1 186 LEU 186 195 195 LEU LEU A . n 
A 1 187 LYS 187 196 196 LYS LYS A . n 
A 1 188 ASN 188 197 197 ASN ASN A . n 
A 1 189 TYR 189 198 198 TYR TYR A . n 
A 1 190 ILE 190 199 199 ILE ILE A . n 
A 1 191 ASP 191 200 200 ASP ASP A . n 
A 1 192 LYS 192 201 201 LYS LYS A . n 
A 1 193 GLN 193 202 202 GLN GLN A . n 
A 1 194 LEU 194 203 203 LEU LEU A . n 
A 1 195 LEU 195 204 204 LEU LEU A . n 
A 1 196 PRO 196 205 205 PRO PRO A . n 
A 1 197 ILE 197 206 206 ILE ILE A . n 
A 1 198 VAL 198 207 207 VAL VAL A . n 
A 1 199 ASN 199 208 208 ASN ASN A . n 
A 1 200 LYS 200 209 209 LYS LYS A . n 
A 1 201 GLN 201 210 210 GLN GLN A . n 
A 1 202 SER 202 211 211 SER SER A . n 
A 1 203 CYS 203 212 212 CYS CYS A . n 
A 1 204 SER 204 213 213 SER SER A . n 
A 1 205 ILE 205 214 214 ILE ILE A . n 
A 1 206 SER 206 215 215 SER SER A . n 
A 1 207 ASN 207 216 216 ASN ASN A . n 
A 1 208 ILE 208 217 217 ILE ILE A . n 
A 1 209 GLU 209 218 218 GLU GLU A . n 
A 1 210 THR 210 219 219 THR THR A . n 
A 1 211 VAL 211 220 220 VAL VAL A . n 
A 1 212 ILE 212 221 221 ILE ILE A . n 
A 1 213 GLU 213 222 222 GLU GLU A . n 
A 1 214 PHE 214 223 223 PHE PHE A . n 
A 1 215 GLN 215 224 224 GLN GLN A . n 
A 1 216 GLN 216 225 225 GLN GLN A . n 
A 1 217 LYS 217 226 226 LYS LYS A . n 
A 1 218 ASN 218 227 227 ASN ASN A . n 
A 1 219 ASN 219 228 228 ASN ASN A . n 
A 1 220 ARG 220 229 229 ARG ARG A . n 
A 1 221 LEU 221 230 230 LEU LEU A . n 
A 1 222 LEU 222 231 231 LEU LEU A . n 
A 1 223 GLU 223 232 232 GLU GLU A . n 
A 1 224 ILE 224 233 233 ILE ILE A . n 
A 1 225 THR 225 234 234 THR THR A . n 
A 1 226 ARG 226 235 235 ARG ARG A . n 
A 1 227 GLU 227 236 236 GLU GLU A . n 
A 1 228 PHE 228 237 237 PHE PHE A . n 
A 1 229 SER 229 238 238 SER SER A . n 
A 1 230 VAL 230 239 239 VAL VAL A . n 
A 1 231 ASN 231 240 240 ASN ASN A . n 
A 1 232 ALA 232 241 241 ALA ALA A . n 
A 1 233 GLY 233 242 242 GLY GLY A . n 
A 1 234 VAL 234 243 243 VAL VAL A . n 
A 1 235 THR 235 244 244 THR THR A . n 
A 1 236 THR 236 245 245 THR THR A . n 
A 1 237 PRO 237 246 246 PRO PRO A . n 
A 1 238 VAL 238 247 247 VAL VAL A . n 
A 1 239 SER 239 248 248 SER SER A . n 
A 1 240 THR 240 249 249 THR THR A . n 
A 1 241 TYR 241 250 250 TYR TYR A . n 
A 1 242 MET 242 251 251 MET MET A . n 
A 1 243 LEU 243 252 252 LEU LEU A . n 
A 1 244 THR 244 253 253 THR THR A . n 
A 1 245 ASN 245 254 254 ASN ASN A . n 
A 1 246 SER 246 255 255 SER SER A . n 
A 1 247 GLU 247 256 256 GLU GLU A . n 
A 1 248 LEU 248 257 257 LEU LEU A . n 
A 1 249 LEU 249 258 258 LEU LEU A . n 
A 1 250 SER 250 259 259 SER SER A . n 
A 1 251 LEU 251 260 260 LEU LEU A . n 
A 1 252 ILE 252 261 261 ILE ILE A . n 
A 1 253 ASN 253 262 262 ASN ASN A . n 
A 1 254 ASP 254 263 263 ASP ASP A . n 
A 1 255 MET 255 264 264 MET MET A . n 
A 1 256 PRO 256 265 265 PRO PRO A . n 
A 1 257 ILE 257 266 266 ILE ILE A . n 
A 1 258 THR 258 267 267 THR THR A . n 
A 1 259 ASN 259 268 268 ASN ASN A . n 
A 1 260 ASP 260 269 269 ASP ASP A . n 
A 1 261 GLN 261 270 270 GLN GLN A . n 
A 1 262 LYS 262 271 271 LYS LYS A . n 
A 1 263 LYS 263 272 272 LYS LYS A . n 
A 1 264 LEU 264 273 273 LEU LEU A . n 
A 1 265 MET 265 274 274 MET MET A . n 
A 1 266 SER 266 275 275 SER SER A . n 
A 1 267 ASN 267 276 276 ASN ASN A . n 
A 1 268 ASN 268 277 277 ASN ASN A . n 
A 1 269 VAL 269 278 278 VAL VAL A . n 
A 1 270 GLN 270 279 279 GLN GLN A . n 
A 1 271 ILE 271 280 280 ILE ILE A . n 
A 1 272 VAL 272 281 281 VAL VAL A . n 
A 1 273 ARG 273 282 282 ARG ARG A . n 
A 1 274 GLN 274 283 283 GLN GLN A . n 
A 1 275 GLN 275 284 284 GLN GLN A . n 
A 1 276 SER 276 285 285 SER SER A . n 
A 1 277 TYR 277 286 286 TYR TYR A . n 
A 1 278 SER 278 287 287 SER SER A . n 
A 1 279 ILE 279 288 288 ILE ILE A . n 
A 1 280 MET 280 289 289 MET MET A . n 
A 1 281 SER 281 290 290 SER SER A . n 
A 1 282 ILE 282 291 291 ILE ILE A . n 
A 1 283 ILE 283 292 292 ILE ILE A . n 
A 1 284 LYS 284 293 293 LYS LYS A . n 
A 1 285 GLU 285 294 294 GLU GLU A . n 
A 1 286 GLU 286 295 295 GLU GLU A . n 
A 1 287 VAL 287 296 296 VAL VAL A . n 
A 1 288 LEU 288 297 297 LEU LEU A . n 
A 1 289 ALA 289 298 298 ALA ALA A . n 
A 1 290 TYR 290 299 299 TYR TYR A . n 
A 1 291 VAL 291 300 300 VAL VAL A . n 
A 1 292 VAL 292 301 301 VAL VAL A . n 
A 1 293 GLN 293 302 302 GLN GLN A . n 
A 1 294 LEU 294 303 303 LEU LEU A . n 
A 1 295 PRO 295 304 304 PRO PRO A . n 
A 1 296 LEU 296 305 305 LEU LEU A . n 
A 1 297 TYR 297 306 306 TYR TYR A . n 
A 1 298 GLY 298 307 307 GLY GLY A . n 
A 1 299 VAL 299 308 308 VAL VAL A . n 
A 1 300 ILE 300 309 309 ILE ILE A . n 
A 1 301 ASP 301 310 310 ASP ASP A . n 
A 1 302 THR 302 311 311 THR THR A . n 
A 1 303 PRO 303 312 312 PRO PRO A . n 
A 1 304 CYS 304 313 313 CYS CYS A . n 
A 1 305 TRP 305 314 314 TRP TRP A . n 
A 1 306 LYS 306 315 315 LYS LYS A . n 
A 1 307 LEU 307 316 316 LEU LEU A . n 
A 1 308 HIS 308 317 317 HIS HIS A . n 
A 1 309 THR 309 318 318 THR THR A . n 
A 1 310 SER 310 319 319 SER SER A . n 
A 1 311 PRO 311 320 320 PRO PRO A . n 
A 1 312 LEU 312 321 321 LEU LEU A . n 
A 1 313 CYS 313 322 322 CYS CYS A . n 
A 1 314 THR 314 323 323 THR THR A . n 
A 1 315 THR 315 324 324 THR THR A . n 
A 1 316 ASN 316 325 325 ASN ASN A . n 
A 1 317 THR 317 326 ?   ?   ?   A . n 
A 1 318 LYS 318 327 ?   ?   ?   A . n 
A 1 319 GLU 319 328 ?   ?   ?   A . n 
A 1 320 GLY 320 329 ?   ?   ?   A . n 
A 1 321 SER 321 330 330 SER SER A . n 
A 1 322 ASN 322 331 331 ASN ASN A . n 
A 1 323 ILE 323 332 332 ILE ILE A . n 
A 1 324 CYS 324 333 333 CYS CYS A . n 
A 1 325 LEU 325 334 334 LEU LEU A . n 
A 1 326 THR 326 335 335 THR THR A . n 
A 1 327 ARG 327 336 336 ARG ARG A . n 
A 1 328 THR 328 337 337 THR THR A . n 
A 1 329 ASP 329 338 338 ASP ASP A . n 
A 1 330 ARG 330 339 339 ARG ARG A . n 
A 1 331 GLY 331 340 340 GLY GLY A . n 
A 1 332 TRP 332 341 341 TRP TRP A . n 
A 1 333 TYR 333 342 342 TYR TYR A . n 
A 1 334 CYS 334 343 343 CYS CYS A . n 
A 1 335 ASP 335 344 344 ASP ASP A . n 
A 1 336 ASN 336 345 345 ASN ASN A . n 
A 1 337 ALA 337 346 346 ALA ALA A . n 
A 1 338 GLY 338 347 347 GLY GLY A . n 
A 1 339 SER 339 348 348 SER SER A . n 
A 1 340 VAL 340 349 349 VAL VAL A . n 
A 1 341 SER 341 350 350 SER SER A . n 
A 1 342 PHE 342 351 351 PHE PHE A . n 
A 1 343 PHE 343 352 352 PHE PHE A . n 
A 1 344 PRO 344 353 353 PRO PRO A . n 
A 1 345 GLN 345 354 354 GLN GLN A . n 
A 1 346 ALA 346 355 355 ALA ALA A . n 
A 1 347 GLU 347 356 356 GLU GLU A . n 
A 1 348 THR 348 357 357 THR THR A . n 
A 1 349 CYS 349 358 358 CYS CYS A . n 
A 1 350 LYS 350 359 359 LYS LYS A . n 
A 1 351 VAL 351 360 360 VAL VAL A . n 
A 1 352 GLN 352 361 361 GLN GLN A . n 
A 1 353 SER 353 362 362 SER SER A . n 
A 1 354 ASN 354 363 363 ASN ASN A . n 
A 1 355 ARG 355 364 364 ARG ARG A . n 
A 1 356 VAL 356 365 365 VAL VAL A . n 
A 1 357 PHE 357 366 366 PHE PHE A . n 
A 1 358 CYS 358 367 367 CYS CYS A . n 
A 1 359 ASP 359 368 368 ASP ASP A . n 
A 1 360 THR 360 369 369 THR THR A . n 
A 1 361 MET 361 370 370 MET MET A . n 
A 1 362 ASN 362 371 371 ASN ASN A . n 
A 1 363 SER 363 372 372 SER SER A . n 
A 1 364 LEU 364 373 373 LEU LEU A . n 
A 1 365 THR 365 374 374 THR THR A . n 
A 1 366 LEU 366 375 375 LEU LEU A . n 
A 1 367 PRO 367 376 376 PRO PRO A . n 
A 1 368 SER 368 377 377 SER SER A . n 
A 1 369 GLU 369 378 378 GLU GLU A . n 
A 1 370 VAL 370 379 379 VAL VAL A . n 
A 1 371 ASN 371 380 380 ASN ASN A . n 
A 1 372 LEU 372 381 381 LEU LEU A . n 
A 1 373 CYS 373 382 382 CYS CYS A . n 
A 1 374 ASN 374 383 383 ASN ASN A . n 
A 1 375 VAL 375 384 384 VAL VAL A . n 
A 1 376 ASP 376 385 385 ASP ASP A . n 
A 1 377 ILE 377 386 386 ILE ILE A . n 
A 1 378 PHE 378 387 387 PHE PHE A . n 
A 1 379 ASN 379 388 388 ASN ASN A . n 
A 1 380 PRO 380 389 389 PRO PRO A . n 
A 1 381 LYS 381 390 390 LYS LYS A . n 
A 1 382 TYR 382 391 391 TYR TYR A . n 
A 1 383 ASP 383 392 392 ASP ASP A . n 
A 1 384 CYS 384 393 393 CYS CYS A . n 
A 1 385 LYS 385 394 394 LYS LYS A . n 
A 1 386 ILE 386 395 395 ILE ILE A . n 
A 1 387 MET 387 396 396 MET MET A . n 
A 1 388 THR 388 397 397 THR THR A . n 
A 1 389 SER 389 398 398 SER SER A . n 
A 1 390 LYS 390 399 399 LYS LYS A . n 
A 1 391 THR 391 400 400 THR THR A . n 
A 1 392 ASP 392 401 401 ASP ASP A . n 
A 1 393 VAL 393 402 402 VAL VAL A . n 
A 1 394 SER 394 403 403 SER SER A . n 
A 1 395 SER 395 404 404 SER SER A . n 
A 1 396 SER 396 405 405 SER SER A . n 
A 1 397 VAL 397 406 406 VAL VAL A . n 
A 1 398 ILE 398 407 407 ILE ILE A . n 
A 1 399 THR 399 408 408 THR THR A . n 
A 1 400 SER 400 409 409 SER SER A . n 
A 1 401 LEU 401 410 410 LEU LEU A . n 
A 1 402 GLY 402 411 411 GLY GLY A . n 
A 1 403 ALA 403 412 412 ALA ALA A . n 
A 1 404 ILE 404 413 413 ILE ILE A . n 
A 1 405 VAL 405 414 414 VAL VAL A . n 
A 1 406 SER 406 415 415 SER SER A . n 
A 1 407 CYS 407 416 416 CYS CYS A . n 
A 1 408 TYR 408 417 417 TYR TYR A . n 
A 1 409 GLY 409 418 418 GLY GLY A . n 
A 1 410 LYS 410 419 419 LYS LYS A . n 
A 1 411 THR 411 420 420 THR THR A . n 
A 1 412 LYS 412 421 421 LYS LYS A . n 
A 1 413 CYS 413 422 422 CYS CYS A . n 
A 1 414 THR 414 423 423 THR THR A . n 
A 1 415 ALA 415 424 424 ALA ALA A . n 
A 1 416 SER 416 425 425 SER SER A . n 
A 1 417 ASN 417 426 426 ASN ASN A . n 
A 1 418 LYS 418 427 427 LYS LYS A . n 
A 1 419 ASN 419 428 428 ASN ASN A . n 
A 1 420 ARG 420 429 429 ARG ARG A . n 
A 1 421 GLY 421 430 430 GLY GLY A . n 
A 1 422 ILE 422 431 431 ILE ILE A . n 
A 1 423 ILE 423 432 432 ILE ILE A . n 
A 1 424 LYS 424 433 433 LYS LYS A . n 
A 1 425 THR 425 434 434 THR THR A . n 
A 1 426 PHE 426 435 435 PHE PHE A . n 
A 1 427 SER 427 436 436 SER SER A . n 
A 1 428 ASN 428 437 437 ASN ASN A . n 
A 1 429 GLY 429 438 438 GLY GLY A . n 
A 1 430 CYS 430 439 439 CYS CYS A . n 
A 1 431 ASP 431 440 440 ASP ASP A . n 
A 1 432 TYR 432 441 441 TYR TYR A . n 
A 1 433 VAL 433 442 442 VAL VAL A . n 
A 1 434 SER 434 443 443 SER SER A . n 
A 1 435 ASN 435 444 444 ASN ASN A . n 
A 1 436 LYS 436 445 445 LYS LYS A . n 
A 1 437 GLY 437 446 446 GLY GLY A . n 
A 1 438 VAL 438 447 447 VAL VAL A . n 
A 1 439 ASP 439 448 448 ASP ASP A . n 
A 1 440 THR 440 449 449 THR THR A . n 
A 1 441 VAL 441 450 450 VAL VAL A . n 
A 1 442 SER 442 451 451 SER SER A . n 
A 1 443 VAL 443 452 452 VAL VAL A . n 
A 1 444 GLY 444 453 453 GLY GLY A . n 
A 1 445 ASN 445 454 454 ASN ASN A . n 
A 1 446 THR 446 455 455 THR THR A . n 
A 1 447 LEU 447 456 456 LEU LEU A . n 
A 1 448 TYR 448 457 457 TYR TYR A . n 
A 1 449 TYR 449 458 458 TYR TYR A . n 
A 1 450 VAL 450 459 459 VAL VAL A . n 
A 1 451 ASN 451 460 460 ASN ASN A . n 
A 1 452 LYS 452 461 461 LYS LYS A . n 
A 1 453 GLN 453 462 462 GLN GLN A . n 
A 1 454 GLU 454 463 463 GLU GLU A . n 
A 1 455 GLY 455 464 464 GLY GLY A . n 
A 1 456 LYS 456 465 465 LYS LYS A . n 
A 1 457 SER 457 466 466 SER SER A . n 
A 1 458 LEU 458 467 467 LEU LEU A . n 
A 1 459 TYR 459 468 468 TYR TYR A . n 
A 1 460 VAL 460 469 469 VAL VAL A . n 
A 1 461 LYS 461 470 470 LYS LYS A . n 
A 1 462 GLY 462 471 471 GLY GLY A . n 
A 1 463 GLU 463 472 472 GLU GLU A . n 
A 1 464 PRO 464 473 473 PRO PRO A . n 
A 1 465 ILE 465 474 474 ILE ILE A . n 
A 1 466 ILE 466 475 475 ILE ILE A . n 
A 1 467 ASN 467 476 476 ASN ASN A . n 
A 1 468 PHE 468 477 477 PHE PHE A . n 
A 1 469 TYR 469 478 478 TYR TYR A . n 
A 1 470 ASP 470 479 479 ASP ASP A . n 
A 1 471 PRO 471 480 480 PRO PRO A . n 
A 1 472 LEU 472 481 481 LEU LEU A . n 
A 1 473 VAL 473 482 482 VAL VAL A . n 
A 1 474 PHE 474 483 483 PHE PHE A . n 
A 1 475 PRO 475 484 484 PRO PRO A . n 
A 1 476 SER 476 485 485 SER SER A . n 
A 1 477 ASP 477 486 486 ASP ASP A . n 
A 1 478 GLU 478 487 487 GLU GLU A . n 
A 1 479 PHE 479 488 488 PHE PHE A . n 
A 1 480 ASP 480 489 489 ASP ASP A . n 
A 1 481 ALA 481 490 490 ALA ALA A . n 
A 1 482 SER 482 491 491 SER SER A . n 
A 1 483 ILE 483 492 492 ILE ILE A . n 
A 1 484 SER 484 493 493 SER SER A . n 
A 1 485 GLN 485 494 494 GLN GLN A . n 
A 1 486 VAL 486 495 495 VAL VAL A . n 
A 1 487 ASN 487 496 496 ASN ASN A . n 
A 1 488 GLU 488 497 497 GLU GLU A . n 
A 1 489 LYS 489 498 498 LYS LYS A . n 
A 1 490 ILE 490 499 499 ILE ILE A . n 
A 1 491 ASN 491 500 500 ASN ASN A . n 
A 1 492 GLN 492 501 501 GLN GLN A . n 
A 1 493 SER 493 502 502 SER SER A . n 
A 1 494 LEU 494 503 503 LEU LEU A . n 
A 1 495 ALA 495 504 504 ALA ALA A . n 
A 1 496 PHE 496 505 505 PHE PHE A . n 
A 1 497 ILE 497 506 506 ILE ILE A . n 
A 1 498 ARG 498 507 507 ARG ARG A . n 
A 1 499 LYS 499 508 508 LYS LYS A . n 
A 1 500 SER 500 509 509 SER SER A . n 
A 1 501 ASP 501 510 510 ASP ASP A . n 
A 1 502 GLU 502 511 511 GLU GLU A . n 
A 1 503 LEU 503 512 512 LEU LEU A . n 
A 1 504 LEU 504 513 513 LEU LEU A . n 
A 1 505 HIS 505 514 514 HIS HIS A . n 
A 1 506 ASN 506 515 515 ASN ASN A . n 
A 1 507 VAL 507 516 516 VAL VAL A . n 
A 1 508 ASN 508 517 517 ASN ASN A . n 
A 1 509 ALA 509 518 ?   ?   ?   A . n 
A 1 510 GLY 510 519 ?   ?   ?   A . n 
A 1 511 LYS 511 520 ?   ?   ?   A . n 
A 1 512 SER 512 521 ?   ?   ?   A . n 
A 1 513 THR 513 522 ?   ?   ?   A . n 
A 1 514 THR 514 523 ?   ?   ?   A . n 
A 1 515 ASN 515 524 ?   ?   ?   A . n 
A 1 516 GLY 516 525 ?   ?   ?   A . n 
A 1 517 GLY 517 526 ?   ?   ?   A . n 
A 1 518 SER 518 527 ?   ?   ?   A . n 
A 1 519 ALA 519 528 ?   ?   ?   A . n 
A 1 520 GLY 520 529 ?   ?   ?   A . n 
A 1 521 SER 521 530 ?   ?   ?   A . n 
A 1 522 GLY 522 531 ?   ?   ?   A . n 
A 1 523 HIS 523 532 ?   ?   ?   A . n 
A 1 524 HIS 524 533 ?   ?   ?   A . n 
A 1 525 HIS 525 534 ?   ?   ?   A . n 
A 1 526 HIS 526 535 ?   ?   ?   A . n 
A 1 527 HIS 527 536 ?   ?   ?   A . n 
A 1 528 HIS 528 537 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   LEU 4   4   ?   ?   ?   B . n 
B 1 5   ILE 5   5   ?   ?   ?   B . n 
B 1 6   LEU 6   6   ?   ?   ?   B . n 
B 1 7   LYS 7   7   ?   ?   ?   B . n 
B 1 8   ALA 8   8   ?   ?   ?   B . n 
B 1 9   ASN 9   9   ?   ?   ?   B . n 
B 1 10  ALA 10  10  ?   ?   ?   B . n 
B 1 11  ILE 11  11  ?   ?   ?   B . n 
B 1 12  THR 12  12  ?   ?   ?   B . n 
B 1 13  THR 13  13  ?   ?   ?   B . n 
B 1 14  ILE 14  14  ?   ?   ?   B . n 
B 1 15  LEU 15  15  ?   ?   ?   B . n 
B 1 16  THR 16  16  ?   ?   ?   B . n 
B 1 17  ALA 17  17  ?   ?   ?   B . n 
B 1 18  VAL 18  18  ?   ?   ?   B . n 
B 1 19  THR 19  19  ?   ?   ?   B . n 
B 1 20  PHE 20  20  ?   ?   ?   B . n 
B 1 21  CYS 21  21  ?   ?   ?   B . n 
B 1 22  PHE 22  22  ?   ?   ?   B . n 
B 1 23  ALA 23  23  ?   ?   ?   B . n 
B 1 24  SER 24  24  ?   ?   ?   B . n 
B 1 25  GLY 25  25  ?   ?   ?   B . n 
B 1 26  GLN 26  26  26  GLN GLN B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  ILE 28  28  28  ILE ILE B . n 
B 1 29  THR 29  29  29  THR THR B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  TYR 33  33  33  TYR TYR B . n 
B 1 34  GLN 34  34  34  GLN GLN B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  CYS 37  37  37  CYS CYS B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  LYS 42  42  42  LYS LYS B . n 
B 1 43  GLY 43  43  43  GLY GLY B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  LEU 48  48  48  LEU LEU B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  TRP 52  52  52  TRP TRP B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  SER 55  55  55  SER SER B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  LYS 65  65  65  LYS LYS B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  CYS 69  69  69  CYS CYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  THR 72  72  72  THR THR B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  VAL 76  76  76  VAL VAL B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  LYS 85  85  85  LYS LYS B . n 
B 1 86  TYR 86  86  86  TYR TYR B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  MET 97  97  97  MET MET B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  SER 99  108 ?   ?   ?   B . n 
B 1 100 THR 100 109 ?   ?   ?   B . n 
B 1 101 PRO 101 110 ?   ?   ?   B . n 
B 1 102 ALA 102 111 ?   ?   ?   B . n 
B 1 103 THR 103 112 ?   ?   ?   B . n 
B 1 104 ASN 104 113 ?   ?   ?   B . n 
B 1 105 ASN 105 114 ?   ?   ?   B . n 
B 1 106 ARG 106 115 ?   ?   ?   B . n 
B 1 107 ALA 107 116 ?   ?   ?   B . n 
B 1 108 ARG 108 117 ?   ?   ?   B . n 
B 1 109 ARG 109 118 ?   ?   ?   B . n 
B 1 110 GLU 110 119 ?   ?   ?   B . n 
B 1 111 LEU 111 120 ?   ?   ?   B . n 
B 1 112 PRO 112 121 ?   ?   ?   B . n 
B 1 113 ARG 113 122 ?   ?   ?   B . n 
B 1 114 PHE 114 123 ?   ?   ?   B . n 
B 1 115 MET 115 124 ?   ?   ?   B . n 
B 1 116 ASN 116 125 ?   ?   ?   B . n 
B 1 117 TYR 117 126 ?   ?   ?   B . n 
B 1 118 THR 118 127 ?   ?   ?   B . n 
B 1 119 LEU 119 128 ?   ?   ?   B . n 
B 1 120 ASN 120 129 ?   ?   ?   B . n 
B 1 121 ASN 121 130 ?   ?   ?   B . n 
B 1 122 ALA 122 131 ?   ?   ?   B . n 
B 1 123 LYS 123 132 ?   ?   ?   B . n 
B 1 124 LYS 124 133 ?   ?   ?   B . n 
B 1 125 THR 125 134 ?   ?   ?   B . n 
B 1 126 ASN 126 135 ?   ?   ?   B . n 
B 1 127 VAL 127 136 ?   ?   ?   B . n 
B 1 128 THR 128 137 ?   ?   ?   B . n 
B 1 129 LEU 129 138 ?   ?   ?   B . n 
B 1 130 SER 130 139 ?   ?   ?   B . n 
B 1 131 LYS 131 140 ?   ?   ?   B . n 
B 1 132 LYS 132 141 ?   ?   ?   B . n 
B 1 133 ARG 133 142 ?   ?   ?   B . n 
B 1 134 LYS 134 143 ?   ?   ?   B . n 
B 1 135 ARG 135 144 ?   ?   ?   B . n 
B 1 136 ARG 136 145 ?   ?   ?   B . n 
B 1 137 SER 137 146 ?   ?   ?   B . n 
B 1 138 ALA 138 147 ?   ?   ?   B . n 
B 1 139 ILE 139 148 148 ILE ILE B . n 
B 1 140 ALA 140 149 149 ALA ALA B . n 
B 1 141 SER 141 150 150 SER SER B . n 
B 1 142 GLY 142 151 151 GLY GLY B . n 
B 1 143 VAL 143 152 152 VAL VAL B . n 
B 1 144 ALA 144 153 153 ALA ALA B . n 
B 1 145 VAL 145 154 154 VAL VAL B . n 
B 1 146 SER 146 155 155 SER SER B . n 
B 1 147 LYS 147 156 156 LYS LYS B . n 
B 1 148 VAL 148 157 157 VAL VAL B . n 
B 1 149 LEU 149 158 158 LEU LEU B . n 
B 1 150 HIS 150 159 159 HIS HIS B . n 
B 1 151 LEU 151 160 160 LEU LEU B . n 
B 1 152 GLU 152 161 161 GLU GLU B . n 
B 1 153 GLY 153 162 162 GLY GLY B . n 
B 1 154 GLU 154 163 163 GLU GLU B . n 
B 1 155 VAL 155 164 164 VAL VAL B . n 
B 1 156 ASN 156 165 165 ASN ASN B . n 
B 1 157 LYS 157 166 166 LYS LYS B . n 
B 1 158 ILE 158 167 167 ILE ILE B . n 
B 1 159 LYS 159 168 168 LYS LYS B . n 
B 1 160 SER 160 169 169 SER SER B . n 
B 1 161 ALA 161 170 170 ALA ALA B . n 
B 1 162 LEU 162 171 171 LEU LEU B . n 
B 1 163 LEU 163 172 172 LEU LEU B . n 
B 1 164 SER 164 173 173 SER SER B . n 
B 1 165 THR 165 174 174 THR THR B . n 
B 1 166 ASN 166 175 175 ASN ASN B . n 
B 1 167 LYS 167 176 176 LYS LYS B . n 
B 1 168 ALA 168 177 177 ALA ALA B . n 
B 1 169 VAL 169 178 178 VAL VAL B . n 
B 1 170 VAL 170 179 179 VAL VAL B . n 
B 1 171 SER 171 180 180 SER SER B . n 
B 1 172 LEU 172 181 181 LEU LEU B . n 
B 1 173 SER 173 182 182 SER SER B . n 
B 1 174 ASN 174 183 183 ASN ASN B . n 
B 1 175 GLY 175 184 184 GLY GLY B . n 
B 1 176 VAL 176 185 185 VAL VAL B . n 
B 1 177 SER 177 186 186 SER SER B . n 
B 1 178 VAL 178 187 187 VAL VAL B . n 
B 1 179 LEU 179 188 188 LEU LEU B . n 
B 1 180 THR 180 189 189 THR THR B . n 
B 1 181 SER 181 190 190 SER SER B . n 
B 1 182 LYS 182 191 191 LYS LYS B . n 
B 1 183 VAL 183 192 192 VAL VAL B . n 
B 1 184 LEU 184 193 193 LEU LEU B . n 
B 1 185 ASP 185 194 194 ASP ASP B . n 
B 1 186 LEU 186 195 195 LEU LEU B . n 
B 1 187 LYS 187 196 196 LYS LYS B . n 
B 1 188 ASN 188 197 197 ASN ASN B . n 
B 1 189 TYR 189 198 198 TYR TYR B . n 
B 1 190 ILE 190 199 199 ILE ILE B . n 
B 1 191 ASP 191 200 200 ASP ASP B . n 
B 1 192 LYS 192 201 201 LYS LYS B . n 
B 1 193 GLN 193 202 202 GLN GLN B . n 
B 1 194 LEU 194 203 203 LEU LEU B . n 
B 1 195 LEU 195 204 204 LEU LEU B . n 
B 1 196 PRO 196 205 205 PRO PRO B . n 
B 1 197 ILE 197 206 206 ILE ILE B . n 
B 1 198 VAL 198 207 207 VAL VAL B . n 
B 1 199 ASN 199 208 208 ASN ASN B . n 
B 1 200 LYS 200 209 209 LYS LYS B . n 
B 1 201 GLN 201 210 210 GLN GLN B . n 
B 1 202 SER 202 211 211 SER SER B . n 
B 1 203 CYS 203 212 212 CYS CYS B . n 
B 1 204 SER 204 213 213 SER SER B . n 
B 1 205 ILE 205 214 214 ILE ILE B . n 
B 1 206 SER 206 215 215 SER SER B . n 
B 1 207 ASN 207 216 216 ASN ASN B . n 
B 1 208 ILE 208 217 217 ILE ILE B . n 
B 1 209 GLU 209 218 218 GLU GLU B . n 
B 1 210 THR 210 219 219 THR THR B . n 
B 1 211 VAL 211 220 220 VAL VAL B . n 
B 1 212 ILE 212 221 221 ILE ILE B . n 
B 1 213 GLU 213 222 222 GLU GLU B . n 
B 1 214 PHE 214 223 223 PHE PHE B . n 
B 1 215 GLN 215 224 224 GLN GLN B . n 
B 1 216 GLN 216 225 225 GLN GLN B . n 
B 1 217 LYS 217 226 226 LYS LYS B . n 
B 1 218 ASN 218 227 227 ASN ASN B . n 
B 1 219 ASN 219 228 228 ASN ASN B . n 
B 1 220 ARG 220 229 229 ARG ARG B . n 
B 1 221 LEU 221 230 230 LEU LEU B . n 
B 1 222 LEU 222 231 231 LEU LEU B . n 
B 1 223 GLU 223 232 232 GLU GLU B . n 
B 1 224 ILE 224 233 233 ILE ILE B . n 
B 1 225 THR 225 234 234 THR THR B . n 
B 1 226 ARG 226 235 235 ARG ARG B . n 
B 1 227 GLU 227 236 236 GLU GLU B . n 
B 1 228 PHE 228 237 237 PHE PHE B . n 
B 1 229 SER 229 238 238 SER SER B . n 
B 1 230 VAL 230 239 239 VAL VAL B . n 
B 1 231 ASN 231 240 240 ASN ASN B . n 
B 1 232 ALA 232 241 241 ALA ALA B . n 
B 1 233 GLY 233 242 242 GLY GLY B . n 
B 1 234 VAL 234 243 243 VAL VAL B . n 
B 1 235 THR 235 244 244 THR THR B . n 
B 1 236 THR 236 245 245 THR THR B . n 
B 1 237 PRO 237 246 246 PRO PRO B . n 
B 1 238 VAL 238 247 247 VAL VAL B . n 
B 1 239 SER 239 248 248 SER SER B . n 
B 1 240 THR 240 249 249 THR THR B . n 
B 1 241 TYR 241 250 250 TYR TYR B . n 
B 1 242 MET 242 251 251 MET MET B . n 
B 1 243 LEU 243 252 252 LEU LEU B . n 
B 1 244 THR 244 253 253 THR THR B . n 
B 1 245 ASN 245 254 254 ASN ASN B . n 
B 1 246 SER 246 255 255 SER SER B . n 
B 1 247 GLU 247 256 256 GLU GLU B . n 
B 1 248 LEU 248 257 257 LEU LEU B . n 
B 1 249 LEU 249 258 258 LEU LEU B . n 
B 1 250 SER 250 259 259 SER SER B . n 
B 1 251 LEU 251 260 260 LEU LEU B . n 
B 1 252 ILE 252 261 261 ILE ILE B . n 
B 1 253 ASN 253 262 262 ASN ASN B . n 
B 1 254 ASP 254 263 263 ASP ASP B . n 
B 1 255 MET 255 264 264 MET MET B . n 
B 1 256 PRO 256 265 265 PRO PRO B . n 
B 1 257 ILE 257 266 266 ILE ILE B . n 
B 1 258 THR 258 267 267 THR THR B . n 
B 1 259 ASN 259 268 268 ASN ASN B . n 
B 1 260 ASP 260 269 269 ASP ASP B . n 
B 1 261 GLN 261 270 270 GLN GLN B . n 
B 1 262 LYS 262 271 271 LYS LYS B . n 
B 1 263 LYS 263 272 272 LYS LYS B . n 
B 1 264 LEU 264 273 273 LEU LEU B . n 
B 1 265 MET 265 274 274 MET MET B . n 
B 1 266 SER 266 275 275 SER SER B . n 
B 1 267 ASN 267 276 276 ASN ASN B . n 
B 1 268 ASN 268 277 277 ASN ASN B . n 
B 1 269 VAL 269 278 278 VAL VAL B . n 
B 1 270 GLN 270 279 279 GLN GLN B . n 
B 1 271 ILE 271 280 280 ILE ILE B . n 
B 1 272 VAL 272 281 281 VAL VAL B . n 
B 1 273 ARG 273 282 282 ARG ARG B . n 
B 1 274 GLN 274 283 283 GLN GLN B . n 
B 1 275 GLN 275 284 284 GLN GLN B . n 
B 1 276 SER 276 285 285 SER SER B . n 
B 1 277 TYR 277 286 286 TYR TYR B . n 
B 1 278 SER 278 287 287 SER SER B . n 
B 1 279 ILE 279 288 288 ILE ILE B . n 
B 1 280 MET 280 289 289 MET MET B . n 
B 1 281 SER 281 290 290 SER SER B . n 
B 1 282 ILE 282 291 291 ILE ILE B . n 
B 1 283 ILE 283 292 292 ILE ILE B . n 
B 1 284 LYS 284 293 293 LYS LYS B . n 
B 1 285 GLU 285 294 294 GLU GLU B . n 
B 1 286 GLU 286 295 295 GLU GLU B . n 
B 1 287 VAL 287 296 296 VAL VAL B . n 
B 1 288 LEU 288 297 297 LEU LEU B . n 
B 1 289 ALA 289 298 298 ALA ALA B . n 
B 1 290 TYR 290 299 299 TYR TYR B . n 
B 1 291 VAL 291 300 300 VAL VAL B . n 
B 1 292 VAL 292 301 301 VAL VAL B . n 
B 1 293 GLN 293 302 302 GLN GLN B . n 
B 1 294 LEU 294 303 303 LEU LEU B . n 
B 1 295 PRO 295 304 304 PRO PRO B . n 
B 1 296 LEU 296 305 305 LEU LEU B . n 
B 1 297 TYR 297 306 306 TYR TYR B . n 
B 1 298 GLY 298 307 307 GLY GLY B . n 
B 1 299 VAL 299 308 308 VAL VAL B . n 
B 1 300 ILE 300 309 309 ILE ILE B . n 
B 1 301 ASP 301 310 310 ASP ASP B . n 
B 1 302 THR 302 311 311 THR THR B . n 
B 1 303 PRO 303 312 312 PRO PRO B . n 
B 1 304 CYS 304 313 313 CYS CYS B . n 
B 1 305 TRP 305 314 314 TRP TRP B . n 
B 1 306 LYS 306 315 315 LYS LYS B . n 
B 1 307 LEU 307 316 316 LEU LEU B . n 
B 1 308 HIS 308 317 317 HIS HIS B . n 
B 1 309 THR 309 318 318 THR THR B . n 
B 1 310 SER 310 319 319 SER SER B . n 
B 1 311 PRO 311 320 320 PRO PRO B . n 
B 1 312 LEU 312 321 321 LEU LEU B . n 
B 1 313 CYS 313 322 322 CYS CYS B . n 
B 1 314 THR 314 323 323 THR THR B . n 
B 1 315 THR 315 324 324 THR THR B . n 
B 1 316 ASN 316 325 325 ASN ASN B . n 
B 1 317 THR 317 326 ?   ?   ?   B . n 
B 1 318 LYS 318 327 ?   ?   ?   B . n 
B 1 319 GLU 319 328 ?   ?   ?   B . n 
B 1 320 GLY 320 329 ?   ?   ?   B . n 
B 1 321 SER 321 330 330 SER SER B . n 
B 1 322 ASN 322 331 331 ASN ASN B . n 
B 1 323 ILE 323 332 332 ILE ILE B . n 
B 1 324 CYS 324 333 333 CYS CYS B . n 
B 1 325 LEU 325 334 334 LEU LEU B . n 
B 1 326 THR 326 335 335 THR THR B . n 
B 1 327 ARG 327 336 336 ARG ARG B . n 
B 1 328 THR 328 337 337 THR THR B . n 
B 1 329 ASP 329 338 338 ASP ASP B . n 
B 1 330 ARG 330 339 339 ARG ARG B . n 
B 1 331 GLY 331 340 340 GLY GLY B . n 
B 1 332 TRP 332 341 341 TRP TRP B . n 
B 1 333 TYR 333 342 342 TYR TYR B . n 
B 1 334 CYS 334 343 343 CYS CYS B . n 
B 1 335 ASP 335 344 344 ASP ASP B . n 
B 1 336 ASN 336 345 345 ASN ASN B . n 
B 1 337 ALA 337 346 346 ALA ALA B . n 
B 1 338 GLY 338 347 347 GLY GLY B . n 
B 1 339 SER 339 348 348 SER SER B . n 
B 1 340 VAL 340 349 349 VAL VAL B . n 
B 1 341 SER 341 350 350 SER SER B . n 
B 1 342 PHE 342 351 351 PHE PHE B . n 
B 1 343 PHE 343 352 352 PHE PHE B . n 
B 1 344 PRO 344 353 353 PRO PRO B . n 
B 1 345 GLN 345 354 354 GLN GLN B . n 
B 1 346 ALA 346 355 355 ALA ALA B . n 
B 1 347 GLU 347 356 356 GLU GLU B . n 
B 1 348 THR 348 357 357 THR THR B . n 
B 1 349 CYS 349 358 358 CYS CYS B . n 
B 1 350 LYS 350 359 359 LYS LYS B . n 
B 1 351 VAL 351 360 360 VAL VAL B . n 
B 1 352 GLN 352 361 361 GLN GLN B . n 
B 1 353 SER 353 362 362 SER SER B . n 
B 1 354 ASN 354 363 363 ASN ASN B . n 
B 1 355 ARG 355 364 364 ARG ARG B . n 
B 1 356 VAL 356 365 365 VAL VAL B . n 
B 1 357 PHE 357 366 366 PHE PHE B . n 
B 1 358 CYS 358 367 367 CYS CYS B . n 
B 1 359 ASP 359 368 368 ASP ASP B . n 
B 1 360 THR 360 369 369 THR THR B . n 
B 1 361 MET 361 370 370 MET MET B . n 
B 1 362 ASN 362 371 371 ASN ASN B . n 
B 1 363 SER 363 372 372 SER SER B . n 
B 1 364 LEU 364 373 373 LEU LEU B . n 
B 1 365 THR 365 374 374 THR THR B . n 
B 1 366 LEU 366 375 375 LEU LEU B . n 
B 1 367 PRO 367 376 376 PRO PRO B . n 
B 1 368 SER 368 377 377 SER SER B . n 
B 1 369 GLU 369 378 378 GLU GLU B . n 
B 1 370 VAL 370 379 379 VAL VAL B . n 
B 1 371 ASN 371 380 380 ASN ASN B . n 
B 1 372 LEU 372 381 381 LEU LEU B . n 
B 1 373 CYS 373 382 382 CYS CYS B . n 
B 1 374 ASN 374 383 383 ASN ASN B . n 
B 1 375 VAL 375 384 384 VAL VAL B . n 
B 1 376 ASP 376 385 385 ASP ASP B . n 
B 1 377 ILE 377 386 386 ILE ILE B . n 
B 1 378 PHE 378 387 387 PHE PHE B . n 
B 1 379 ASN 379 388 388 ASN ASN B . n 
B 1 380 PRO 380 389 389 PRO PRO B . n 
B 1 381 LYS 381 390 390 LYS LYS B . n 
B 1 382 TYR 382 391 391 TYR TYR B . n 
B 1 383 ASP 383 392 392 ASP ASP B . n 
B 1 384 CYS 384 393 393 CYS CYS B . n 
B 1 385 LYS 385 394 394 LYS LYS B . n 
B 1 386 ILE 386 395 395 ILE ILE B . n 
B 1 387 MET 387 396 396 MET MET B . n 
B 1 388 THR 388 397 397 THR THR B . n 
B 1 389 SER 389 398 398 SER SER B . n 
B 1 390 LYS 390 399 399 LYS LYS B . n 
B 1 391 THR 391 400 400 THR THR B . n 
B 1 392 ASP 392 401 401 ASP ASP B . n 
B 1 393 VAL 393 402 402 VAL VAL B . n 
B 1 394 SER 394 403 403 SER SER B . n 
B 1 395 SER 395 404 404 SER SER B . n 
B 1 396 SER 396 405 405 SER SER B . n 
B 1 397 VAL 397 406 406 VAL VAL B . n 
B 1 398 ILE 398 407 407 ILE ILE B . n 
B 1 399 THR 399 408 408 THR THR B . n 
B 1 400 SER 400 409 409 SER SER B . n 
B 1 401 LEU 401 410 410 LEU LEU B . n 
B 1 402 GLY 402 411 411 GLY GLY B . n 
B 1 403 ALA 403 412 412 ALA ALA B . n 
B 1 404 ILE 404 413 413 ILE ILE B . n 
B 1 405 VAL 405 414 414 VAL VAL B . n 
B 1 406 SER 406 415 415 SER SER B . n 
B 1 407 CYS 407 416 416 CYS CYS B . n 
B 1 408 TYR 408 417 417 TYR TYR B . n 
B 1 409 GLY 409 418 418 GLY GLY B . n 
B 1 410 LYS 410 419 419 LYS LYS B . n 
B 1 411 THR 411 420 420 THR THR B . n 
B 1 412 LYS 412 421 421 LYS LYS B . n 
B 1 413 CYS 413 422 422 CYS CYS B . n 
B 1 414 THR 414 423 423 THR THR B . n 
B 1 415 ALA 415 424 424 ALA ALA B . n 
B 1 416 SER 416 425 425 SER SER B . n 
B 1 417 ASN 417 426 426 ASN ASN B . n 
B 1 418 LYS 418 427 427 LYS LYS B . n 
B 1 419 ASN 419 428 428 ASN ASN B . n 
B 1 420 ARG 420 429 429 ARG ARG B . n 
B 1 421 GLY 421 430 430 GLY GLY B . n 
B 1 422 ILE 422 431 431 ILE ILE B . n 
B 1 423 ILE 423 432 432 ILE ILE B . n 
B 1 424 LYS 424 433 433 LYS LYS B . n 
B 1 425 THR 425 434 434 THR THR B . n 
B 1 426 PHE 426 435 435 PHE PHE B . n 
B 1 427 SER 427 436 436 SER SER B . n 
B 1 428 ASN 428 437 437 ASN ASN B . n 
B 1 429 GLY 429 438 438 GLY GLY B . n 
B 1 430 CYS 430 439 439 CYS CYS B . n 
B 1 431 ASP 431 440 440 ASP ASP B . n 
B 1 432 TYR 432 441 441 TYR TYR B . n 
B 1 433 VAL 433 442 442 VAL VAL B . n 
B 1 434 SER 434 443 443 SER SER B . n 
B 1 435 ASN 435 444 444 ASN ASN B . n 
B 1 436 LYS 436 445 445 LYS LYS B . n 
B 1 437 GLY 437 446 446 GLY GLY B . n 
B 1 438 VAL 438 447 447 VAL VAL B . n 
B 1 439 ASP 439 448 448 ASP ASP B . n 
B 1 440 THR 440 449 449 THR THR B . n 
B 1 441 VAL 441 450 450 VAL VAL B . n 
B 1 442 SER 442 451 451 SER SER B . n 
B 1 443 VAL 443 452 452 VAL VAL B . n 
B 1 444 GLY 444 453 453 GLY GLY B . n 
B 1 445 ASN 445 454 454 ASN ASN B . n 
B 1 446 THR 446 455 455 THR THR B . n 
B 1 447 LEU 447 456 456 LEU LEU B . n 
B 1 448 TYR 448 457 457 TYR TYR B . n 
B 1 449 TYR 449 458 458 TYR TYR B . n 
B 1 450 VAL 450 459 459 VAL VAL B . n 
B 1 451 ASN 451 460 460 ASN ASN B . n 
B 1 452 LYS 452 461 461 LYS LYS B . n 
B 1 453 GLN 453 462 462 GLN GLN B . n 
B 1 454 GLU 454 463 463 GLU GLU B . n 
B 1 455 GLY 455 464 464 GLY GLY B . n 
B 1 456 LYS 456 465 465 LYS LYS B . n 
B 1 457 SER 457 466 466 SER SER B . n 
B 1 458 LEU 458 467 467 LEU LEU B . n 
B 1 459 TYR 459 468 468 TYR TYR B . n 
B 1 460 VAL 460 469 469 VAL VAL B . n 
B 1 461 LYS 461 470 470 LYS LYS B . n 
B 1 462 GLY 462 471 471 GLY GLY B . n 
B 1 463 GLU 463 472 472 GLU GLU B . n 
B 1 464 PRO 464 473 473 PRO PRO B . n 
B 1 465 ILE 465 474 474 ILE ILE B . n 
B 1 466 ILE 466 475 475 ILE ILE B . n 
B 1 467 ASN 467 476 476 ASN ASN B . n 
B 1 468 PHE 468 477 477 PHE PHE B . n 
B 1 469 TYR 469 478 478 TYR TYR B . n 
B 1 470 ASP 470 479 479 ASP ASP B . n 
B 1 471 PRO 471 480 480 PRO PRO B . n 
B 1 472 LEU 472 481 481 LEU LEU B . n 
B 1 473 VAL 473 482 482 VAL VAL B . n 
B 1 474 PHE 474 483 483 PHE PHE B . n 
B 1 475 PRO 475 484 484 PRO PRO B . n 
B 1 476 SER 476 485 485 SER SER B . n 
B 1 477 ASP 477 486 486 ASP ASP B . n 
B 1 478 GLU 478 487 487 GLU GLU B . n 
B 1 479 PHE 479 488 488 PHE PHE B . n 
B 1 480 ASP 480 489 489 ASP ASP B . n 
B 1 481 ALA 481 490 490 ALA ALA B . n 
B 1 482 SER 482 491 491 SER SER B . n 
B 1 483 ILE 483 492 492 ILE ILE B . n 
B 1 484 SER 484 493 493 SER SER B . n 
B 1 485 GLN 485 494 494 GLN GLN B . n 
B 1 486 VAL 486 495 495 VAL VAL B . n 
B 1 487 ASN 487 496 496 ASN ASN B . n 
B 1 488 GLU 488 497 497 GLU GLU B . n 
B 1 489 LYS 489 498 498 LYS LYS B . n 
B 1 490 ILE 490 499 499 ILE ILE B . n 
B 1 491 ASN 491 500 500 ASN ASN B . n 
B 1 492 GLN 492 501 501 GLN GLN B . n 
B 1 493 SER 493 502 502 SER SER B . n 
B 1 494 LEU 494 503 503 LEU LEU B . n 
B 1 495 ALA 495 504 504 ALA ALA B . n 
B 1 496 PHE 496 505 505 PHE PHE B . n 
B 1 497 ILE 497 506 506 ILE ILE B . n 
B 1 498 ARG 498 507 507 ARG ARG B . n 
B 1 499 LYS 499 508 508 LYS LYS B . n 
B 1 500 SER 500 509 509 SER SER B . n 
B 1 501 ASP 501 510 510 ASP ASP B . n 
B 1 502 GLU 502 511 511 GLU GLU B . n 
B 1 503 LEU 503 512 512 LEU LEU B . n 
B 1 504 LEU 504 513 513 LEU LEU B . n 
B 1 505 HIS 505 514 514 HIS HIS B . n 
B 1 506 ASN 506 515 515 ASN ASN B . n 
B 1 507 VAL 507 516 516 VAL VAL B . n 
B 1 508 ASN 508 517 517 ASN ASN B . n 
B 1 509 ALA 509 518 ?   ?   ?   B . n 
B 1 510 GLY 510 519 ?   ?   ?   B . n 
B 1 511 LYS 511 520 ?   ?   ?   B . n 
B 1 512 SER 512 521 ?   ?   ?   B . n 
B 1 513 THR 513 522 ?   ?   ?   B . n 
B 1 514 THR 514 523 ?   ?   ?   B . n 
B 1 515 ASN 515 524 ?   ?   ?   B . n 
B 1 516 GLY 516 525 ?   ?   ?   B . n 
B 1 517 GLY 517 526 ?   ?   ?   B . n 
B 1 518 SER 518 527 ?   ?   ?   B . n 
B 1 519 ALA 519 528 ?   ?   ?   B . n 
B 1 520 GLY 520 529 ?   ?   ?   B . n 
B 1 521 SER 521 530 ?   ?   ?   B . n 
B 1 522 GLY 522 531 ?   ?   ?   B . n 
B 1 523 HIS 523 532 ?   ?   ?   B . n 
B 1 524 HIS 524 533 ?   ?   ?   B . n 
B 1 525 HIS 525 534 ?   ?   ?   B . n 
B 1 526 HIS 526 535 ?   ?   ?   B . n 
B 1 527 HIS 527 536 ?   ?   ?   B . n 
B 1 528 HIS 528 537 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   GLU 2   2   ?   ?   ?   C . n 
C 1 3   LEU 3   3   ?   ?   ?   C . n 
C 1 4   LEU 4   4   ?   ?   ?   C . n 
C 1 5   ILE 5   5   ?   ?   ?   C . n 
C 1 6   LEU 6   6   ?   ?   ?   C . n 
C 1 7   LYS 7   7   ?   ?   ?   C . n 
C 1 8   ALA 8   8   ?   ?   ?   C . n 
C 1 9   ASN 9   9   ?   ?   ?   C . n 
C 1 10  ALA 10  10  ?   ?   ?   C . n 
C 1 11  ILE 11  11  ?   ?   ?   C . n 
C 1 12  THR 12  12  ?   ?   ?   C . n 
C 1 13  THR 13  13  ?   ?   ?   C . n 
C 1 14  ILE 14  14  ?   ?   ?   C . n 
C 1 15  LEU 15  15  ?   ?   ?   C . n 
C 1 16  THR 16  16  ?   ?   ?   C . n 
C 1 17  ALA 17  17  ?   ?   ?   C . n 
C 1 18  VAL 18  18  ?   ?   ?   C . n 
C 1 19  THR 19  19  ?   ?   ?   C . n 
C 1 20  PHE 20  20  ?   ?   ?   C . n 
C 1 21  CYS 21  21  ?   ?   ?   C . n 
C 1 22  PHE 22  22  ?   ?   ?   C . n 
C 1 23  ALA 23  23  ?   ?   ?   C . n 
C 1 24  SER 24  24  ?   ?   ?   C . n 
C 1 25  GLY 25  25  ?   ?   ?   C . n 
C 1 26  GLN 26  26  26  GLN GLN C . n 
C 1 27  ASN 27  27  27  ASN ASN C . n 
C 1 28  ILE 28  28  28  ILE ILE C . n 
C 1 29  THR 29  29  29  THR THR C . n 
C 1 30  GLU 30  30  30  GLU GLU C . n 
C 1 31  GLU 31  31  31  GLU GLU C . n 
C 1 32  PHE 32  32  32  PHE PHE C . n 
C 1 33  TYR 33  33  33  TYR TYR C . n 
C 1 34  GLN 34  34  34  GLN GLN C . n 
C 1 35  SER 35  35  35  SER SER C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  CYS 37  37  37  CYS CYS C . n 
C 1 38  SER 38  38  38  SER SER C . n 
C 1 39  ALA 39  39  39  ALA ALA C . n 
C 1 40  VAL 40  40  40  VAL VAL C . n 
C 1 41  SER 41  41  41  SER SER C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  GLY 43  43  43  GLY GLY C . n 
C 1 44  TYR 44  44  44  TYR TYR C . n 
C 1 45  LEU 45  45  45  LEU LEU C . n 
C 1 46  SER 46  46  46  SER SER C . n 
C 1 47  ALA 47  47  47  ALA ALA C . n 
C 1 48  LEU 48  48  48  LEU LEU C . n 
C 1 49  ARG 49  49  49  ARG ARG C . n 
C 1 50  THR 50  50  50  THR THR C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  TRP 52  52  52  TRP TRP C . n 
C 1 53  TYR 53  53  53  TYR TYR C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  SER 55  55  55  SER SER C . n 
C 1 56  VAL 56  56  56  VAL VAL C . n 
C 1 57  ILE 57  57  57  ILE ILE C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  ILE 59  59  59  ILE ILE C . n 
C 1 60  GLU 60  60  60  GLU GLU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  SER 62  62  62  SER SER C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ILE 64  64  64  ILE ILE C . n 
C 1 65  LYS 65  65  65  LYS LYS C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  ASN 67  67  67  ASN ASN C . n 
C 1 68  LYS 68  68  68  LYS LYS C . n 
C 1 69  CYS 69  69  69  CYS CYS C . n 
C 1 70  ASN 70  70  70  ASN ASN C . n 
C 1 71  GLY 71  71  71  GLY GLY C . n 
C 1 72  THR 72  72  72  THR THR C . n 
C 1 73  ASP 73  73  73  ASP ASP C . n 
C 1 74  ALA 74  74  74  ALA ALA C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  VAL 76  76  76  VAL VAL C . n 
C 1 77  LYS 77  77  77  LYS LYS C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  ILE 79  79  79  ILE ILE C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  GLN 81  81  81  GLN GLN C . n 
C 1 82  GLU 82  82  82  GLU GLU C . n 
C 1 83  LEU 83  83  83  LEU LEU C . n 
C 1 84  ASP 84  84  84  ASP ASP C . n 
C 1 85  LYS 85  85  85  LYS LYS C . n 
C 1 86  TYR 86  86  86  TYR TYR C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  ASN 88  88  88  ASN ASN C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  VAL 90  90  90  VAL VAL C . n 
C 1 91  THR 91  91  91  THR THR C . n 
C 1 92  GLU 92  92  92  GLU GLU C . n 
C 1 93  LEU 93  93  93  LEU LEU C . n 
C 1 94  GLN 94  94  94  GLN GLN C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  LEU 96  96  96  LEU LEU C . n 
C 1 97  MET 97  97  97  MET MET C . n 
C 1 98  GLN 98  98  98  GLN GLN C . n 
C 1 99  SER 99  108 ?   ?   ?   C . n 
C 1 100 THR 100 109 ?   ?   ?   C . n 
C 1 101 PRO 101 110 ?   ?   ?   C . n 
C 1 102 ALA 102 111 ?   ?   ?   C . n 
C 1 103 THR 103 112 ?   ?   ?   C . n 
C 1 104 ASN 104 113 ?   ?   ?   C . n 
C 1 105 ASN 105 114 ?   ?   ?   C . n 
C 1 106 ARG 106 115 ?   ?   ?   C . n 
C 1 107 ALA 107 116 ?   ?   ?   C . n 
C 1 108 ARG 108 117 ?   ?   ?   C . n 
C 1 109 ARG 109 118 ?   ?   ?   C . n 
C 1 110 GLU 110 119 ?   ?   ?   C . n 
C 1 111 LEU 111 120 ?   ?   ?   C . n 
C 1 112 PRO 112 121 ?   ?   ?   C . n 
C 1 113 ARG 113 122 ?   ?   ?   C . n 
C 1 114 PHE 114 123 ?   ?   ?   C . n 
C 1 115 MET 115 124 ?   ?   ?   C . n 
C 1 116 ASN 116 125 ?   ?   ?   C . n 
C 1 117 TYR 117 126 ?   ?   ?   C . n 
C 1 118 THR 118 127 ?   ?   ?   C . n 
C 1 119 LEU 119 128 ?   ?   ?   C . n 
C 1 120 ASN 120 129 ?   ?   ?   C . n 
C 1 121 ASN 121 130 ?   ?   ?   C . n 
C 1 122 ALA 122 131 ?   ?   ?   C . n 
C 1 123 LYS 123 132 ?   ?   ?   C . n 
C 1 124 LYS 124 133 ?   ?   ?   C . n 
C 1 125 THR 125 134 ?   ?   ?   C . n 
C 1 126 ASN 126 135 ?   ?   ?   C . n 
C 1 127 VAL 127 136 ?   ?   ?   C . n 
C 1 128 THR 128 137 ?   ?   ?   C . n 
C 1 129 LEU 129 138 ?   ?   ?   C . n 
C 1 130 SER 130 139 ?   ?   ?   C . n 
C 1 131 LYS 131 140 ?   ?   ?   C . n 
C 1 132 LYS 132 141 ?   ?   ?   C . n 
C 1 133 ARG 133 142 ?   ?   ?   C . n 
C 1 134 LYS 134 143 ?   ?   ?   C . n 
C 1 135 ARG 135 144 ?   ?   ?   C . n 
C 1 136 ARG 136 145 ?   ?   ?   C . n 
C 1 137 SER 137 146 ?   ?   ?   C . n 
C 1 138 ALA 138 147 ?   ?   ?   C . n 
C 1 139 ILE 139 148 ?   ?   ?   C . n 
C 1 140 ALA 140 149 ?   ?   ?   C . n 
C 1 141 SER 141 150 ?   ?   ?   C . n 
C 1 142 GLY 142 151 ?   ?   ?   C . n 
C 1 143 VAL 143 152 152 VAL VAL C . n 
C 1 144 ALA 144 153 153 ALA ALA C . n 
C 1 145 VAL 145 154 154 VAL VAL C . n 
C 1 146 SER 146 155 155 SER SER C . n 
C 1 147 LYS 147 156 156 LYS LYS C . n 
C 1 148 VAL 148 157 157 VAL VAL C . n 
C 1 149 LEU 149 158 158 LEU LEU C . n 
C 1 150 HIS 150 159 159 HIS HIS C . n 
C 1 151 LEU 151 160 160 LEU LEU C . n 
C 1 152 GLU 152 161 161 GLU GLU C . n 
C 1 153 GLY 153 162 162 GLY GLY C . n 
C 1 154 GLU 154 163 163 GLU GLU C . n 
C 1 155 VAL 155 164 164 VAL VAL C . n 
C 1 156 ASN 156 165 165 ASN ASN C . n 
C 1 157 LYS 157 166 166 LYS LYS C . n 
C 1 158 ILE 158 167 167 ILE ILE C . n 
C 1 159 LYS 159 168 168 LYS LYS C . n 
C 1 160 SER 160 169 169 SER SER C . n 
C 1 161 ALA 161 170 170 ALA ALA C . n 
C 1 162 LEU 162 171 171 LEU LEU C . n 
C 1 163 LEU 163 172 172 LEU LEU C . n 
C 1 164 SER 164 173 173 SER SER C . n 
C 1 165 THR 165 174 174 THR THR C . n 
C 1 166 ASN 166 175 175 ASN ASN C . n 
C 1 167 LYS 167 176 176 LYS LYS C . n 
C 1 168 ALA 168 177 177 ALA ALA C . n 
C 1 169 VAL 169 178 178 VAL VAL C . n 
C 1 170 VAL 170 179 179 VAL VAL C . n 
C 1 171 SER 171 180 180 SER SER C . n 
C 1 172 LEU 172 181 181 LEU LEU C . n 
C 1 173 SER 173 182 182 SER SER C . n 
C 1 174 ASN 174 183 183 ASN ASN C . n 
C 1 175 GLY 175 184 184 GLY GLY C . n 
C 1 176 VAL 176 185 185 VAL VAL C . n 
C 1 177 SER 177 186 186 SER SER C . n 
C 1 178 VAL 178 187 187 VAL VAL C . n 
C 1 179 LEU 179 188 188 LEU LEU C . n 
C 1 180 THR 180 189 189 THR THR C . n 
C 1 181 SER 181 190 190 SER SER C . n 
C 1 182 LYS 182 191 191 LYS LYS C . n 
C 1 183 VAL 183 192 192 VAL VAL C . n 
C 1 184 LEU 184 193 193 LEU LEU C . n 
C 1 185 ASP 185 194 194 ASP ASP C . n 
C 1 186 LEU 186 195 195 LEU LEU C . n 
C 1 187 LYS 187 196 196 LYS LYS C . n 
C 1 188 ASN 188 197 197 ASN ASN C . n 
C 1 189 TYR 189 198 198 TYR TYR C . n 
C 1 190 ILE 190 199 199 ILE ILE C . n 
C 1 191 ASP 191 200 200 ASP ASP C . n 
C 1 192 LYS 192 201 201 LYS LYS C . n 
C 1 193 GLN 193 202 202 GLN GLN C . n 
C 1 194 LEU 194 203 203 LEU LEU C . n 
C 1 195 LEU 195 204 204 LEU LEU C . n 
C 1 196 PRO 196 205 205 PRO PRO C . n 
C 1 197 ILE 197 206 206 ILE ILE C . n 
C 1 198 VAL 198 207 207 VAL VAL C . n 
C 1 199 ASN 199 208 208 ASN ASN C . n 
C 1 200 LYS 200 209 209 LYS LYS C . n 
C 1 201 GLN 201 210 210 GLN GLN C . n 
C 1 202 SER 202 211 211 SER SER C . n 
C 1 203 CYS 203 212 212 CYS CYS C . n 
C 1 204 SER 204 213 213 SER SER C . n 
C 1 205 ILE 205 214 214 ILE ILE C . n 
C 1 206 SER 206 215 215 SER SER C . n 
C 1 207 ASN 207 216 216 ASN ASN C . n 
C 1 208 ILE 208 217 217 ILE ILE C . n 
C 1 209 GLU 209 218 218 GLU GLU C . n 
C 1 210 THR 210 219 219 THR THR C . n 
C 1 211 VAL 211 220 220 VAL VAL C . n 
C 1 212 ILE 212 221 221 ILE ILE C . n 
C 1 213 GLU 213 222 222 GLU GLU C . n 
C 1 214 PHE 214 223 223 PHE PHE C . n 
C 1 215 GLN 215 224 224 GLN GLN C . n 
C 1 216 GLN 216 225 225 GLN GLN C . n 
C 1 217 LYS 217 226 226 LYS LYS C . n 
C 1 218 ASN 218 227 227 ASN ASN C . n 
C 1 219 ASN 219 228 228 ASN ASN C . n 
C 1 220 ARG 220 229 229 ARG ARG C . n 
C 1 221 LEU 221 230 230 LEU LEU C . n 
C 1 222 LEU 222 231 231 LEU LEU C . n 
C 1 223 GLU 223 232 232 GLU GLU C . n 
C 1 224 ILE 224 233 233 ILE ILE C . n 
C 1 225 THR 225 234 234 THR THR C . n 
C 1 226 ARG 226 235 235 ARG ARG C . n 
C 1 227 GLU 227 236 236 GLU GLU C . n 
C 1 228 PHE 228 237 237 PHE PHE C . n 
C 1 229 SER 229 238 238 SER SER C . n 
C 1 230 VAL 230 239 239 VAL VAL C . n 
C 1 231 ASN 231 240 240 ASN ASN C . n 
C 1 232 ALA 232 241 241 ALA ALA C . n 
C 1 233 GLY 233 242 242 GLY GLY C . n 
C 1 234 VAL 234 243 243 VAL VAL C . n 
C 1 235 THR 235 244 244 THR THR C . n 
C 1 236 THR 236 245 245 THR THR C . n 
C 1 237 PRO 237 246 246 PRO PRO C . n 
C 1 238 VAL 238 247 247 VAL VAL C . n 
C 1 239 SER 239 248 248 SER SER C . n 
C 1 240 THR 240 249 249 THR THR C . n 
C 1 241 TYR 241 250 250 TYR TYR C . n 
C 1 242 MET 242 251 251 MET MET C . n 
C 1 243 LEU 243 252 252 LEU LEU C . n 
C 1 244 THR 244 253 253 THR THR C . n 
C 1 245 ASN 245 254 254 ASN ASN C . n 
C 1 246 SER 246 255 255 SER SER C . n 
C 1 247 GLU 247 256 256 GLU GLU C . n 
C 1 248 LEU 248 257 257 LEU LEU C . n 
C 1 249 LEU 249 258 258 LEU LEU C . n 
C 1 250 SER 250 259 259 SER SER C . n 
C 1 251 LEU 251 260 260 LEU LEU C . n 
C 1 252 ILE 252 261 261 ILE ILE C . n 
C 1 253 ASN 253 262 262 ASN ASN C . n 
C 1 254 ASP 254 263 263 ASP ASP C . n 
C 1 255 MET 255 264 264 MET MET C . n 
C 1 256 PRO 256 265 265 PRO PRO C . n 
C 1 257 ILE 257 266 266 ILE ILE C . n 
C 1 258 THR 258 267 267 THR THR C . n 
C 1 259 ASN 259 268 268 ASN ASN C . n 
C 1 260 ASP 260 269 269 ASP ASP C . n 
C 1 261 GLN 261 270 270 GLN GLN C . n 
C 1 262 LYS 262 271 271 LYS LYS C . n 
C 1 263 LYS 263 272 272 LYS LYS C . n 
C 1 264 LEU 264 273 273 LEU LEU C . n 
C 1 265 MET 265 274 274 MET MET C . n 
C 1 266 SER 266 275 275 SER SER C . n 
C 1 267 ASN 267 276 276 ASN ASN C . n 
C 1 268 ASN 268 277 277 ASN ASN C . n 
C 1 269 VAL 269 278 278 VAL VAL C . n 
C 1 270 GLN 270 279 279 GLN GLN C . n 
C 1 271 ILE 271 280 280 ILE ILE C . n 
C 1 272 VAL 272 281 281 VAL VAL C . n 
C 1 273 ARG 273 282 282 ARG ARG C . n 
C 1 274 GLN 274 283 283 GLN GLN C . n 
C 1 275 GLN 275 284 284 GLN GLN C . n 
C 1 276 SER 276 285 285 SER SER C . n 
C 1 277 TYR 277 286 286 TYR TYR C . n 
C 1 278 SER 278 287 287 SER SER C . n 
C 1 279 ILE 279 288 288 ILE ILE C . n 
C 1 280 MET 280 289 289 MET MET C . n 
C 1 281 SER 281 290 290 SER SER C . n 
C 1 282 ILE 282 291 291 ILE ILE C . n 
C 1 283 ILE 283 292 292 ILE ILE C . n 
C 1 284 LYS 284 293 293 LYS LYS C . n 
C 1 285 GLU 285 294 294 GLU GLU C . n 
C 1 286 GLU 286 295 295 GLU GLU C . n 
C 1 287 VAL 287 296 296 VAL VAL C . n 
C 1 288 LEU 288 297 297 LEU LEU C . n 
C 1 289 ALA 289 298 298 ALA ALA C . n 
C 1 290 TYR 290 299 299 TYR TYR C . n 
C 1 291 VAL 291 300 300 VAL VAL C . n 
C 1 292 VAL 292 301 301 VAL VAL C . n 
C 1 293 GLN 293 302 302 GLN GLN C . n 
C 1 294 LEU 294 303 303 LEU LEU C . n 
C 1 295 PRO 295 304 304 PRO PRO C . n 
C 1 296 LEU 296 305 305 LEU LEU C . n 
C 1 297 TYR 297 306 306 TYR TYR C . n 
C 1 298 GLY 298 307 307 GLY GLY C . n 
C 1 299 VAL 299 308 308 VAL VAL C . n 
C 1 300 ILE 300 309 309 ILE ILE C . n 
C 1 301 ASP 301 310 310 ASP ASP C . n 
C 1 302 THR 302 311 311 THR THR C . n 
C 1 303 PRO 303 312 312 PRO PRO C . n 
C 1 304 CYS 304 313 313 CYS CYS C . n 
C 1 305 TRP 305 314 314 TRP TRP C . n 
C 1 306 LYS 306 315 315 LYS LYS C . n 
C 1 307 LEU 307 316 316 LEU LEU C . n 
C 1 308 HIS 308 317 317 HIS HIS C . n 
C 1 309 THR 309 318 318 THR THR C . n 
C 1 310 SER 310 319 319 SER SER C . n 
C 1 311 PRO 311 320 320 PRO PRO C . n 
C 1 312 LEU 312 321 321 LEU LEU C . n 
C 1 313 CYS 313 322 322 CYS CYS C . n 
C 1 314 THR 314 323 323 THR THR C . n 
C 1 315 THR 315 324 324 THR THR C . n 
C 1 316 ASN 316 325 325 ASN ASN C . n 
C 1 317 THR 317 326 326 THR THR C . n 
C 1 318 LYS 318 327 327 LYS LYS C . n 
C 1 319 GLU 319 328 328 GLU GLU C . n 
C 1 320 GLY 320 329 329 GLY GLY C . n 
C 1 321 SER 321 330 330 SER SER C . n 
C 1 322 ASN 322 331 331 ASN ASN C . n 
C 1 323 ILE 323 332 332 ILE ILE C . n 
C 1 324 CYS 324 333 333 CYS CYS C . n 
C 1 325 LEU 325 334 334 LEU LEU C . n 
C 1 326 THR 326 335 335 THR THR C . n 
C 1 327 ARG 327 336 336 ARG ARG C . n 
C 1 328 THR 328 337 337 THR THR C . n 
C 1 329 ASP 329 338 338 ASP ASP C . n 
C 1 330 ARG 330 339 339 ARG ARG C . n 
C 1 331 GLY 331 340 340 GLY GLY C . n 
C 1 332 TRP 332 341 341 TRP TRP C . n 
C 1 333 TYR 333 342 342 TYR TYR C . n 
C 1 334 CYS 334 343 343 CYS CYS C . n 
C 1 335 ASP 335 344 344 ASP ASP C . n 
C 1 336 ASN 336 345 345 ASN ASN C . n 
C 1 337 ALA 337 346 346 ALA ALA C . n 
C 1 338 GLY 338 347 347 GLY GLY C . n 
C 1 339 SER 339 348 348 SER SER C . n 
C 1 340 VAL 340 349 349 VAL VAL C . n 
C 1 341 SER 341 350 350 SER SER C . n 
C 1 342 PHE 342 351 351 PHE PHE C . n 
C 1 343 PHE 343 352 352 PHE PHE C . n 
C 1 344 PRO 344 353 353 PRO PRO C . n 
C 1 345 GLN 345 354 354 GLN GLN C . n 
C 1 346 ALA 346 355 355 ALA ALA C . n 
C 1 347 GLU 347 356 356 GLU GLU C . n 
C 1 348 THR 348 357 357 THR THR C . n 
C 1 349 CYS 349 358 358 CYS CYS C . n 
C 1 350 LYS 350 359 359 LYS LYS C . n 
C 1 351 VAL 351 360 360 VAL VAL C . n 
C 1 352 GLN 352 361 361 GLN GLN C . n 
C 1 353 SER 353 362 362 SER SER C . n 
C 1 354 ASN 354 363 363 ASN ASN C . n 
C 1 355 ARG 355 364 364 ARG ARG C . n 
C 1 356 VAL 356 365 365 VAL VAL C . n 
C 1 357 PHE 357 366 366 PHE PHE C . n 
C 1 358 CYS 358 367 367 CYS CYS C . n 
C 1 359 ASP 359 368 368 ASP ASP C . n 
C 1 360 THR 360 369 369 THR THR C . n 
C 1 361 MET 361 370 370 MET MET C . n 
C 1 362 ASN 362 371 371 ASN ASN C . n 
C 1 363 SER 363 372 372 SER SER C . n 
C 1 364 LEU 364 373 373 LEU LEU C . n 
C 1 365 THR 365 374 374 THR THR C . n 
C 1 366 LEU 366 375 375 LEU LEU C . n 
C 1 367 PRO 367 376 376 PRO PRO C . n 
C 1 368 SER 368 377 377 SER SER C . n 
C 1 369 GLU 369 378 378 GLU GLU C . n 
C 1 370 VAL 370 379 379 VAL VAL C . n 
C 1 371 ASN 371 380 380 ASN ASN C . n 
C 1 372 LEU 372 381 381 LEU LEU C . n 
C 1 373 CYS 373 382 382 CYS CYS C . n 
C 1 374 ASN 374 383 383 ASN ASN C . n 
C 1 375 VAL 375 384 384 VAL VAL C . n 
C 1 376 ASP 376 385 385 ASP ASP C . n 
C 1 377 ILE 377 386 386 ILE ILE C . n 
C 1 378 PHE 378 387 387 PHE PHE C . n 
C 1 379 ASN 379 388 388 ASN ASN C . n 
C 1 380 PRO 380 389 389 PRO PRO C . n 
C 1 381 LYS 381 390 390 LYS LYS C . n 
C 1 382 TYR 382 391 391 TYR TYR C . n 
C 1 383 ASP 383 392 392 ASP ASP C . n 
C 1 384 CYS 384 393 393 CYS CYS C . n 
C 1 385 LYS 385 394 394 LYS LYS C . n 
C 1 386 ILE 386 395 395 ILE ILE C . n 
C 1 387 MET 387 396 396 MET MET C . n 
C 1 388 THR 388 397 397 THR THR C . n 
C 1 389 SER 389 398 398 SER SER C . n 
C 1 390 LYS 390 399 399 LYS LYS C . n 
C 1 391 THR 391 400 400 THR THR C . n 
C 1 392 ASP 392 401 401 ASP ASP C . n 
C 1 393 VAL 393 402 402 VAL VAL C . n 
C 1 394 SER 394 403 403 SER SER C . n 
C 1 395 SER 395 404 404 SER SER C . n 
C 1 396 SER 396 405 405 SER SER C . n 
C 1 397 VAL 397 406 406 VAL VAL C . n 
C 1 398 ILE 398 407 407 ILE ILE C . n 
C 1 399 THR 399 408 408 THR THR C . n 
C 1 400 SER 400 409 409 SER SER C . n 
C 1 401 LEU 401 410 410 LEU LEU C . n 
C 1 402 GLY 402 411 411 GLY GLY C . n 
C 1 403 ALA 403 412 412 ALA ALA C . n 
C 1 404 ILE 404 413 413 ILE ILE C . n 
C 1 405 VAL 405 414 414 VAL VAL C . n 
C 1 406 SER 406 415 415 SER SER C . n 
C 1 407 CYS 407 416 416 CYS CYS C . n 
C 1 408 TYR 408 417 417 TYR TYR C . n 
C 1 409 GLY 409 418 418 GLY GLY C . n 
C 1 410 LYS 410 419 419 LYS LYS C . n 
C 1 411 THR 411 420 420 THR THR C . n 
C 1 412 LYS 412 421 421 LYS LYS C . n 
C 1 413 CYS 413 422 422 CYS CYS C . n 
C 1 414 THR 414 423 423 THR THR C . n 
C 1 415 ALA 415 424 424 ALA ALA C . n 
C 1 416 SER 416 425 425 SER SER C . n 
C 1 417 ASN 417 426 426 ASN ASN C . n 
C 1 418 LYS 418 427 427 LYS LYS C . n 
C 1 419 ASN 419 428 428 ASN ASN C . n 
C 1 420 ARG 420 429 429 ARG ARG C . n 
C 1 421 GLY 421 430 430 GLY GLY C . n 
C 1 422 ILE 422 431 431 ILE ILE C . n 
C 1 423 ILE 423 432 432 ILE ILE C . n 
C 1 424 LYS 424 433 433 LYS LYS C . n 
C 1 425 THR 425 434 434 THR THR C . n 
C 1 426 PHE 426 435 435 PHE PHE C . n 
C 1 427 SER 427 436 436 SER SER C . n 
C 1 428 ASN 428 437 437 ASN ASN C . n 
C 1 429 GLY 429 438 438 GLY GLY C . n 
C 1 430 CYS 430 439 439 CYS CYS C . n 
C 1 431 ASP 431 440 440 ASP ASP C . n 
C 1 432 TYR 432 441 441 TYR TYR C . n 
C 1 433 VAL 433 442 442 VAL VAL C . n 
C 1 434 SER 434 443 443 SER SER C . n 
C 1 435 ASN 435 444 444 ASN ASN C . n 
C 1 436 LYS 436 445 445 LYS LYS C . n 
C 1 437 GLY 437 446 446 GLY GLY C . n 
C 1 438 VAL 438 447 447 VAL VAL C . n 
C 1 439 ASP 439 448 448 ASP ASP C . n 
C 1 440 THR 440 449 449 THR THR C . n 
C 1 441 VAL 441 450 450 VAL VAL C . n 
C 1 442 SER 442 451 451 SER SER C . n 
C 1 443 VAL 443 452 452 VAL VAL C . n 
C 1 444 GLY 444 453 453 GLY GLY C . n 
C 1 445 ASN 445 454 454 ASN ASN C . n 
C 1 446 THR 446 455 455 THR THR C . n 
C 1 447 LEU 447 456 456 LEU LEU C . n 
C 1 448 TYR 448 457 457 TYR TYR C . n 
C 1 449 TYR 449 458 458 TYR TYR C . n 
C 1 450 VAL 450 459 459 VAL VAL C . n 
C 1 451 ASN 451 460 460 ASN ASN C . n 
C 1 452 LYS 452 461 461 LYS LYS C . n 
C 1 453 GLN 453 462 462 GLN GLN C . n 
C 1 454 GLU 454 463 463 GLU GLU C . n 
C 1 455 GLY 455 464 464 GLY GLY C . n 
C 1 456 LYS 456 465 465 LYS LYS C . n 
C 1 457 SER 457 466 466 SER SER C . n 
C 1 458 LEU 458 467 467 LEU LEU C . n 
C 1 459 TYR 459 468 468 TYR TYR C . n 
C 1 460 VAL 460 469 469 VAL VAL C . n 
C 1 461 LYS 461 470 470 LYS LYS C . n 
C 1 462 GLY 462 471 471 GLY GLY C . n 
C 1 463 GLU 463 472 472 GLU GLU C . n 
C 1 464 PRO 464 473 473 PRO PRO C . n 
C 1 465 ILE 465 474 474 ILE ILE C . n 
C 1 466 ILE 466 475 475 ILE ILE C . n 
C 1 467 ASN 467 476 476 ASN ASN C . n 
C 1 468 PHE 468 477 477 PHE PHE C . n 
C 1 469 TYR 469 478 478 TYR TYR C . n 
C 1 470 ASP 470 479 479 ASP ASP C . n 
C 1 471 PRO 471 480 480 PRO PRO C . n 
C 1 472 LEU 472 481 481 LEU LEU C . n 
C 1 473 VAL 473 482 482 VAL VAL C . n 
C 1 474 PHE 474 483 483 PHE PHE C . n 
C 1 475 PRO 475 484 484 PRO PRO C . n 
C 1 476 SER 476 485 485 SER SER C . n 
C 1 477 ASP 477 486 486 ASP ASP C . n 
C 1 478 GLU 478 487 487 GLU GLU C . n 
C 1 479 PHE 479 488 488 PHE PHE C . n 
C 1 480 ASP 480 489 489 ASP ASP C . n 
C 1 481 ALA 481 490 490 ALA ALA C . n 
C 1 482 SER 482 491 491 SER SER C . n 
C 1 483 ILE 483 492 492 ILE ILE C . n 
C 1 484 SER 484 493 493 SER SER C . n 
C 1 485 GLN 485 494 494 GLN GLN C . n 
C 1 486 VAL 486 495 495 VAL VAL C . n 
C 1 487 ASN 487 496 496 ASN ASN C . n 
C 1 488 GLU 488 497 497 GLU GLU C . n 
C 1 489 LYS 489 498 498 LYS LYS C . n 
C 1 490 ILE 490 499 499 ILE ILE C . n 
C 1 491 ASN 491 500 500 ASN ASN C . n 
C 1 492 GLN 492 501 501 GLN GLN C . n 
C 1 493 SER 493 502 502 SER SER C . n 
C 1 494 LEU 494 503 503 LEU LEU C . n 
C 1 495 ALA 495 504 504 ALA ALA C . n 
C 1 496 PHE 496 505 505 PHE PHE C . n 
C 1 497 ILE 497 506 506 ILE ILE C . n 
C 1 498 ARG 498 507 507 ARG ARG C . n 
C 1 499 LYS 499 508 508 LYS LYS C . n 
C 1 500 SER 500 509 509 SER SER C . n 
C 1 501 ASP 501 510 510 ASP ASP C . n 
C 1 502 GLU 502 511 511 GLU GLU C . n 
C 1 503 LEU 503 512 512 LEU LEU C . n 
C 1 504 LEU 504 513 513 LEU LEU C . n 
C 1 505 HIS 505 514 514 HIS HIS C . n 
C 1 506 ASN 506 515 515 ASN ASN C . n 
C 1 507 VAL 507 516 516 VAL VAL C . n 
C 1 508 ASN 508 517 517 ASN ASN C . n 
C 1 509 ALA 509 518 ?   ?   ?   C . n 
C 1 510 GLY 510 519 ?   ?   ?   C . n 
C 1 511 LYS 511 520 ?   ?   ?   C . n 
C 1 512 SER 512 521 ?   ?   ?   C . n 
C 1 513 THR 513 522 ?   ?   ?   C . n 
C 1 514 THR 514 523 ?   ?   ?   C . n 
C 1 515 ASN 515 524 ?   ?   ?   C . n 
C 1 516 GLY 516 525 ?   ?   ?   C . n 
C 1 517 GLY 517 526 ?   ?   ?   C . n 
C 1 518 SER 518 527 ?   ?   ?   C . n 
C 1 519 ALA 519 528 ?   ?   ?   C . n 
C 1 520 GLY 520 529 ?   ?   ?   C . n 
C 1 521 SER 521 530 ?   ?   ?   C . n 
C 1 522 GLY 522 531 ?   ?   ?   C . n 
C 1 523 HIS 523 532 ?   ?   ?   C . n 
C 1 524 HIS 524 533 ?   ?   ?   C . n 
C 1 525 HIS 525 534 ?   ?   ?   C . n 
C 1 526 HIS 526 535 ?   ?   ?   C . n 
C 1 527 HIS 527 536 ?   ?   ?   C . n 
C 1 528 HIS 528 537 ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 NAG 1 1545 1545 NAG NAG A . 
E 2 NAG 2 1546 1546 NAG NAG A . 
F 2 NAG 1 1525 1525 NAG NAG A . 
G 2 NAG 1 1535 1535 NAG NAG A . 
H 2 NAG 2 1536 1536 NAG NAG A . 
I 2 NAG 1 1535 1535 NAG NAG B . 
J 2 NAG 2 1536 1536 NAG NAG B . 
K 2 NAG 1 1545 1545 NAG NAG B . 
L 2 NAG 2 1546 1546 NAG NAG B . 
M 2 NAG 1 1545 1545 NAG NAG C . 
N 2 NAG 2 1546 1546 NAG NAG C . 
O 2 NAG 1 1535 1535 NAG NAG C . 
P 2 NAG 2 1536 1536 NAG NAG C . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 B ASN 70  B ASN 70  ? ASN 'GLYCOSYLATION SITE' 
2 C ASN 70  C ASN 70  ? ASN 'GLYCOSYLATION SITE' 
3 B ASN 491 B ASN 500 ? ASN 'GLYCOSYLATION SITE' 
4 A ASN 70  A ASN 70  ? ASN 'GLYCOSYLATION SITE' 
5 A ASN 491 A ASN 500 ? ASN 'GLYCOSYLATION SITE' 
6 A ASN 27  A ASN 27  ? ASN 'GLYCOSYLATION SITE' 
7 C ASN 491 C ASN 500 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 36830 ? 
1 MORE         -211  ? 
1 'SSA (A^2)'  55430 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2011-05-18 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2011-08-31 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Database references'       
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 17.7466 9.4520  17.4624 0.1266 0.1059 0.2255 -0.0013 0.0413 -0.0409 0.9323 0.1647 3.4106 -0.1190 
0.5562 -0.5106 -0.0365 0.1937  -0.2851 0.0148  -0.0448 -0.0102 0.4200 0.2053  0.0813  
'X-RAY DIFFRACTION' 2 ? refined 19.4468 -4.5030 16.0363 0.4525 0.1088 0.5204 0.0534  0.0823 -0.0952 0.9859 0.1157 3.0107 -0.0449 
0.9627 -0.2279 0.1969  0.1774  -0.5493 -0.0154 0.0499  -0.0479 0.8613 0.1429  -0.2468 
'X-RAY DIFFRACTION' 3 ? refined 6.6416  0.9150  19.3262 0.3072 0.1561 0.3602 -0.1209 0.0731 -0.0039 1.1836 0.3063 2.9188 -0.3929 
1.0187 -0.7780 0.0136  -0.0439 -0.5083 -0.0374 0.0679  0.0773  0.6217 -0.3220 -0.0815 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 26 A 517 ? . . . . ? 
'X-RAY DIFFRACTION' 2 2 B 26 B 517 ? . . . . ? 
'X-RAY DIFFRACTION' 3 3 C 26 C 517 ? . . . . ? 
# 
_software.name             REFMAC 
_software.classification   refinement 
_software.version          5.5.0109 
_software.citation_id      ? 
_software.pdbx_ordinal     1 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    CB 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     150 
_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    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ILE 
_pdbx_validate_symm_contact.auth_seq_id_2     395 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.09 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A CYS 313 ? ? SG A CYS 313 ? ? 1.681 1.812 -0.131 0.016 N 
2 1 CB A CYS 322 ? ? SG A CYS 322 ? ? 1.709 1.812 -0.103 0.016 N 
3 1 CB A CYS 343 ? ? SG A CYS 343 ? ? 1.616 1.812 -0.196 0.016 N 
4 1 CB A CYS 393 ? ? SG A CYS 393 ? ? 1.709 1.812 -0.103 0.016 N 
5 1 CB A CYS 416 ? ? SG A CYS 416 ? ? 1.714 1.812 -0.098 0.016 N 
6 1 CB B ASP 338 ? ? CG B ASP 338 ? ? 1.645 1.513 0.132  0.021 N 
7 1 CB C CYS 343 ? ? SG C CYS 343 ? ? 1.696 1.812 -0.116 0.016 N 
# 
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 CA A CYS 212 ? ? CB A CYS 212 ? ? SG A CYS 212 ? ? 101.90 114.00 -12.10 1.80 N 
2 1 C  A THR 245 ? ? N  A PRO 246 ? ? CA A PRO 246 ? ? 129.64 119.30 10.34  1.50 Y 
3 1 C  A THR 245 ? ? N  A PRO 246 ? ? CD A PRO 246 ? ? 105.19 128.40 -23.21 2.10 Y 
4 1 C  B THR 245 ? ? N  B PRO 246 ? ? CA B PRO 246 ? ? 130.07 119.30 10.77  1.50 Y 
5 1 C  B THR 245 ? ? N  B PRO 246 ? ? CD B PRO 246 ? ? 104.98 128.40 -23.42 2.10 Y 
6 1 C  C THR 245 ? ? N  C PRO 246 ? ? CA C PRO 246 ? ? 136.29 119.30 16.99  1.50 Y 
7 1 C  C THR 245 ? ? N  C PRO 246 ? ? CD C PRO 246 ? ? 100.46 128.40 -27.94 2.10 Y 
8 1 CA C CYS 313 ? ? CB C CYS 313 ? ? SG C CYS 313 ? ? 120.90 114.20 6.70   1.10 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 CYS A 37  ? ? 33.75   56.41   
2   1 ALA A 47  ? ? -160.91 115.87  
3   1 ASN A 67  ? ? -109.40 71.99   
4   1 LYS A 68  ? ? -15.61  85.29   
5   1 CYS A 69  ? ? -123.16 -164.13 
6   1 ASP A 73  ? ? 60.32   113.31  
7   1 ALA A 147 ? ? -155.28 8.25    
8   1 ILE A 148 ? ? 53.93   121.89  
9   1 ALA A 149 ? ? -39.83  -99.82  
10  1 SER A 150 ? ? 142.63  172.29  
11  1 ALA A 153 ? ? 114.49  -63.52  
12  1 VAL A 154 ? ? 35.61   -141.42 
13  1 SER A 190 ? ? -38.92  -32.16  
14  1 GLN A 202 ? ? -126.16 -66.62  
15  1 PRO A 246 ? ? 30.85   135.24  
16  1 ASN A 277 ? ? -149.26 24.89   
17  1 SER A 290 ? ? -107.84 -68.42  
18  1 ASN A 331 ? ? 78.66   -51.51  
19  1 CYS A 343 ? ? 172.21  120.28  
20  1 ASN A 345 ? ? -112.61 -159.13 
21  1 ALA A 346 ? ? -60.52  87.17   
22  1 ALA A 355 ? ? -25.28  -77.26  
23  1 GLU A 356 ? ? 16.92   -70.46  
24  1 SER A 362 ? ? 63.41   -132.54 
25  1 MET A 370 ? ? -5.65   -69.25  
26  1 SER A 372 ? ? -35.14  158.79  
27  1 ILE A 386 ? ? 85.41   -73.27  
28  1 ASN A 388 ? ? 169.43  134.58  
29  1 LYS A 390 ? ? 90.47   -50.11  
30  1 SER A 404 ? ? -171.74 -168.59 
31  1 ARG A 429 ? ? 93.04   -10.92  
32  1 ASN A 437 ? ? 32.86   55.23   
33  1 LYS A 445 ? ? 42.90   131.63  
34  1 LYS A 465 ? ? 38.79   99.73   
35  1 PRO A 484 ? ? -56.27  26.69   
36  1 SER A 493 ? ? -49.85  -12.69  
37  1 ASN B 27  ? ? -117.65 61.65   
38  1 THR B 36  ? ? -144.45 14.41   
39  1 CYS B 37  ? ? 31.98   49.42   
40  1 ASN B 67  ? ? -113.62 67.11   
41  1 LYS B 68  ? ? -9.48   83.97   
42  1 CYS B 69  ? ? -125.30 -164.59 
43  1 ASP B 73  ? ? 60.90   108.77  
44  1 ALA B 149 ? ? 79.47   60.44   
45  1 SER B 150 ? ? 178.42  -178.67 
46  1 VAL B 152 ? ? -11.22  111.89  
47  1 SER B 155 ? ? -59.91  -72.08  
48  1 SER B 190 ? ? -38.93  -32.76  
49  1 GLN B 202 ? ? -128.04 -67.88  
50  1 PRO B 246 ? ? 31.41   136.57  
51  1 PRO B 265 ? ? -69.91  63.07   
52  1 ASN B 277 ? ? -148.44 18.27   
53  1 VAL B 278 ? ? -26.68  -45.52  
54  1 SER B 290 ? ? -103.43 -70.55  
55  1 THR B 324 ? ? -128.56 -66.02  
56  1 ASN B 331 ? ? 87.82   51.89   
57  1 CYS B 343 ? ? 174.06  122.40  
58  1 ASN B 345 ? ? -115.58 -165.96 
59  1 ALA B 346 ? ? -56.20  84.55   
60  1 ALA B 355 ? ? -4.76   -82.81  
61  1 GLU B 356 ? ? 16.50   -72.53  
62  1 SER B 362 ? ? 62.49   -124.72 
63  1 MET B 370 ? ? -1.66   -67.54  
64  1 SER B 372 ? ? -37.10  154.95  
65  1 ILE B 386 ? ? 82.13   -63.71  
66  1 ASN B 388 ? ? 175.64  137.81  
67  1 LYS B 390 ? ? 94.21   -48.08  
68  1 SER B 404 ? ? -167.34 -168.06 
69  1 ARG B 429 ? ? 89.16   -13.10  
70  1 ASN B 437 ? ? 34.55   46.08   
71  1 LYS B 445 ? ? 43.32   138.26  
72  1 LYS B 465 ? ? 32.55   99.75   
73  1 PRO B 484 ? ? -55.42  27.09   
74  1 ASN C 27  ? ? 153.44  62.01   
75  1 THR C 36  ? ? -146.65 13.74   
76  1 CYS C 37  ? ? 27.84   52.85   
77  1 ASN C 67  ? ? -111.68 65.67   
78  1 LYS C 68  ? ? -9.83   84.45   
79  1 CYS C 69  ? ? -125.11 -165.02 
80  1 ASP C 73  ? ? 57.98   111.24  
81  1 ALA C 153 ? ? 135.31  -151.41 
82  1 VAL C 157 ? ? 75.14   -55.70  
83  1 SER C 190 ? ? -39.52  -35.95  
84  1 GLN C 202 ? ? -124.34 -63.91  
85  1 PRO C 246 ? ? 36.25   133.61  
86  1 ASN C 277 ? ? -150.38 17.37   
87  1 VAL C 278 ? ? -25.80  -44.92  
88  1 ASN C 325 ? ? -178.24 145.40  
89  1 LYS C 327 ? ? 38.19   70.40   
90  1 SER C 330 ? ? 12.45   -113.80 
91  1 ASN C 331 ? ? -70.53  -126.67 
92  1 ILE C 332 ? ? 75.05   130.43  
93  1 CYS C 343 ? ? 174.25  125.85  
94  1 ASN C 345 ? ? -119.81 -162.00 
95  1 ALA C 346 ? ? -56.98  80.21   
96  1 ALA C 355 ? ? -18.91  -78.56  
97  1 GLU C 356 ? ? 16.98   -73.85  
98  1 SER C 362 ? ? 66.76   -125.58 
99  1 MET C 370 ? ? 4.50    -68.76  
100 1 SER C 372 ? ? -42.10  152.76  
101 1 ILE C 386 ? ? 80.64   -62.94  
102 1 ASN C 388 ? ? 170.79  135.41  
103 1 PRO C 389 ? ? -49.64  161.39  
104 1 LYS C 390 ? ? 95.62   -46.27  
105 1 SER C 404 ? ? -167.11 -168.38 
106 1 ARG C 429 ? ? 90.82   -12.72  
107 1 ASN C 437 ? ? 36.64   43.72   
108 1 LYS C 445 ? ? 40.89   139.56  
109 1 LYS C 465 ? ? 32.25   103.07  
110 1 PHE C 477 ? ? -109.72 40.41   
111 1 PRO C 484 ? ? -57.76  28.61   
112 1 SER C 493 ? ? -49.34  -13.27  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1  1 VAL A 152 ? ? ALA A 153 ? ? -136.90 
2  1 THR A 245 ? ? PRO A 246 ? ? -116.98 
3  1 ASP A 392 ? ? CYS A 393 ? ? -138.37 
4  1 ASN A 444 ? ? LYS A 445 ? ? -147.07 
5  1 LYS A 445 ? ? GLY A 446 ? ? -149.62 
6  1 ASN A 476 ? ? PHE A 477 ? ? -139.59 
7  1 THR B 245 ? ? PRO B 246 ? ? -113.16 
8  1 ASP B 392 ? ? CYS B 393 ? ? -141.25 
9  1 THR B 434 ? ? PHE B 435 ? ? -147.80 
10 1 ASN B 444 ? ? LYS B 445 ? ? -146.36 
11 1 ASN B 476 ? ? PHE B 477 ? ? -139.12 
12 1 THR C 245 ? ? PRO C 246 ? ? -113.52 
13 1 ASP C 392 ? ? CYS C 393 ? ? -136.09 
14 1 THR C 434 ? ? PHE C 435 ? ? -148.83 
15 1 ASN C 444 ? ? LYS C 445 ? ? -143.70 
16 1 ASN C 476 ? ? PHE C 477 ? ? -141.41 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C1 ? A NAG 1525 ? PLANAR       . 
2 1 C1 ? A NAG 1535 ? PLANAR       . 
3 1 C1 ? B NAG 1535 ? 'WRONG HAND' . 
4 1 C1 ? C NAG 1535 ? 'WRONG HAND' . 
# 
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 1   ? A MET 1   
2   1 Y 1 A GLU 2   ? A GLU 2   
3   1 Y 1 A LEU 3   ? A LEU 3   
4   1 Y 1 A LEU 4   ? A LEU 4   
5   1 Y 1 A ILE 5   ? A ILE 5   
6   1 Y 1 A LEU 6   ? A LEU 6   
7   1 Y 1 A LYS 7   ? A LYS 7   
8   1 Y 1 A ALA 8   ? A ALA 8   
9   1 Y 1 A ASN 9   ? A ASN 9   
10  1 Y 1 A ALA 10  ? A ALA 10  
11  1 Y 1 A ILE 11  ? A ILE 11  
12  1 Y 1 A THR 12  ? A THR 12  
13  1 Y 1 A THR 13  ? A THR 13  
14  1 Y 1 A ILE 14  ? A ILE 14  
15  1 Y 1 A LEU 15  ? A LEU 15  
16  1 Y 1 A THR 16  ? A THR 16  
17  1 Y 1 A ALA 17  ? A ALA 17  
18  1 Y 1 A VAL 18  ? A VAL 18  
19  1 Y 1 A THR 19  ? A THR 19  
20  1 Y 1 A PHE 20  ? A PHE 20  
21  1 Y 1 A CYS 21  ? A CYS 21  
22  1 Y 1 A PHE 22  ? A PHE 22  
23  1 Y 1 A ALA 23  ? A ALA 23  
24  1 Y 1 A SER 24  ? A SER 24  
25  1 Y 1 A GLY 25  ? A GLY 25  
26  1 Y 1 A SER 108 ? A SER 99  
27  1 Y 1 A THR 109 ? A THR 100 
28  1 Y 1 A PRO 110 ? A PRO 101 
29  1 Y 1 A ALA 111 ? A ALA 102 
30  1 Y 1 A THR 112 ? A THR 103 
31  1 Y 1 A ASN 113 ? A ASN 104 
32  1 Y 1 A ASN 114 ? A ASN 105 
33  1 Y 1 A ARG 115 ? A ARG 106 
34  1 Y 1 A ALA 116 ? A ALA 107 
35  1 Y 1 A ARG 117 ? A ARG 108 
36  1 Y 1 A ARG 118 ? A ARG 109 
37  1 Y 1 A GLU 119 ? A GLU 110 
38  1 Y 1 A LEU 120 ? A LEU 111 
39  1 Y 1 A PRO 121 ? A PRO 112 
40  1 Y 1 A ARG 122 ? A ARG 113 
41  1 Y 1 A PHE 123 ? A PHE 114 
42  1 Y 1 A MET 124 ? A MET 115 
43  1 Y 1 A ASN 125 ? A ASN 116 
44  1 Y 1 A TYR 126 ? A TYR 117 
45  1 Y 1 A THR 127 ? A THR 118 
46  1 Y 1 A LEU 128 ? A LEU 119 
47  1 Y 1 A ASN 129 ? A ASN 120 
48  1 Y 1 A ASN 130 ? A ASN 121 
49  1 Y 1 A ALA 131 ? A ALA 122 
50  1 Y 1 A LYS 132 ? A LYS 123 
51  1 Y 1 A LYS 133 ? A LYS 124 
52  1 Y 1 A THR 134 ? A THR 125 
53  1 Y 1 A ASN 135 ? A ASN 126 
54  1 Y 1 A VAL 136 ? A VAL 127 
55  1 Y 1 A THR 137 ? A THR 128 
56  1 Y 1 A LEU 138 ? A LEU 129 
57  1 Y 1 A SER 139 ? A SER 130 
58  1 Y 1 A LYS 140 ? A LYS 131 
59  1 Y 1 A LYS 141 ? A LYS 132 
60  1 Y 1 A ARG 142 ? A ARG 133 
61  1 Y 1 A LYS 143 ? A LYS 134 
62  1 Y 1 A ARG 144 ? A ARG 135 
63  1 Y 1 A ARG 145 ? A ARG 136 
64  1 Y 1 A THR 326 ? A THR 317 
65  1 Y 1 A LYS 327 ? A LYS 318 
66  1 Y 1 A GLU 328 ? A GLU 319 
67  1 Y 1 A GLY 329 ? A GLY 320 
68  1 Y 1 A ALA 518 ? A ALA 509 
69  1 Y 1 A GLY 519 ? A GLY 510 
70  1 Y 1 A LYS 520 ? A LYS 511 
71  1 Y 1 A SER 521 ? A SER 512 
72  1 Y 1 A THR 522 ? A THR 513 
73  1 Y 1 A THR 523 ? A THR 514 
74  1 Y 1 A ASN 524 ? A ASN 515 
75  1 Y 1 A GLY 525 ? A GLY 516 
76  1 Y 1 A GLY 526 ? A GLY 517 
77  1 Y 1 A SER 527 ? A SER 518 
78  1 Y 1 A ALA 528 ? A ALA 519 
79  1 Y 1 A GLY 529 ? A GLY 520 
80  1 Y 1 A SER 530 ? A SER 521 
81  1 Y 1 A GLY 531 ? A GLY 522 
82  1 Y 1 A HIS 532 ? A HIS 523 
83  1 Y 1 A HIS 533 ? A HIS 524 
84  1 Y 1 A HIS 534 ? A HIS 525 
85  1 Y 1 A HIS 535 ? A HIS 526 
86  1 Y 1 A HIS 536 ? A HIS 527 
87  1 Y 1 A HIS 537 ? A HIS 528 
88  1 Y 1 B MET 1   ? B MET 1   
89  1 Y 1 B GLU 2   ? B GLU 2   
90  1 Y 1 B LEU 3   ? B LEU 3   
91  1 Y 1 B LEU 4   ? B LEU 4   
92  1 Y 1 B ILE 5   ? B ILE 5   
93  1 Y 1 B LEU 6   ? B LEU 6   
94  1 Y 1 B LYS 7   ? B LYS 7   
95  1 Y 1 B ALA 8   ? B ALA 8   
96  1 Y 1 B ASN 9   ? B ASN 9   
97  1 Y 1 B ALA 10  ? B ALA 10  
98  1 Y 1 B ILE 11  ? B ILE 11  
99  1 Y 1 B THR 12  ? B THR 12  
100 1 Y 1 B THR 13  ? B THR 13  
101 1 Y 1 B ILE 14  ? B ILE 14  
102 1 Y 1 B LEU 15  ? B LEU 15  
103 1 Y 1 B THR 16  ? B THR 16  
104 1 Y 1 B ALA 17  ? B ALA 17  
105 1 Y 1 B VAL 18  ? B VAL 18  
106 1 Y 1 B THR 19  ? B THR 19  
107 1 Y 1 B PHE 20  ? B PHE 20  
108 1 Y 1 B CYS 21  ? B CYS 21  
109 1 Y 1 B PHE 22  ? B PHE 22  
110 1 Y 1 B ALA 23  ? B ALA 23  
111 1 Y 1 B SER 24  ? B SER 24  
112 1 Y 1 B GLY 25  ? B GLY 25  
113 1 Y 1 B SER 108 ? B SER 99  
114 1 Y 1 B THR 109 ? B THR 100 
115 1 Y 1 B PRO 110 ? B PRO 101 
116 1 Y 1 B ALA 111 ? B ALA 102 
117 1 Y 1 B THR 112 ? B THR 103 
118 1 Y 1 B ASN 113 ? B ASN 104 
119 1 Y 1 B ASN 114 ? B ASN 105 
120 1 Y 1 B ARG 115 ? B ARG 106 
121 1 Y 1 B ALA 116 ? B ALA 107 
122 1 Y 1 B ARG 117 ? B ARG 108 
123 1 Y 1 B ARG 118 ? B ARG 109 
124 1 Y 1 B GLU 119 ? B GLU 110 
125 1 Y 1 B LEU 120 ? B LEU 111 
126 1 Y 1 B PRO 121 ? B PRO 112 
127 1 Y 1 B ARG 122 ? B ARG 113 
128 1 Y 1 B PHE 123 ? B PHE 114 
129 1 Y 1 B MET 124 ? B MET 115 
130 1 Y 1 B ASN 125 ? B ASN 116 
131 1 Y 1 B TYR 126 ? B TYR 117 
132 1 Y 1 B THR 127 ? B THR 118 
133 1 Y 1 B LEU 128 ? B LEU 119 
134 1 Y 1 B ASN 129 ? B ASN 120 
135 1 Y 1 B ASN 130 ? B ASN 121 
136 1 Y 1 B ALA 131 ? B ALA 122 
137 1 Y 1 B LYS 132 ? B LYS 123 
138 1 Y 1 B LYS 133 ? B LYS 124 
139 1 Y 1 B THR 134 ? B THR 125 
140 1 Y 1 B ASN 135 ? B ASN 126 
141 1 Y 1 B VAL 136 ? B VAL 127 
142 1 Y 1 B THR 137 ? B THR 128 
143 1 Y 1 B LEU 138 ? B LEU 129 
144 1 Y 1 B SER 139 ? B SER 130 
145 1 Y 1 B LYS 140 ? B LYS 131 
146 1 Y 1 B LYS 141 ? B LYS 132 
147 1 Y 1 B ARG 142 ? B ARG 133 
148 1 Y 1 B LYS 143 ? B LYS 134 
149 1 Y 1 B ARG 144 ? B ARG 135 
150 1 Y 1 B ARG 145 ? B ARG 136 
151 1 Y 1 B SER 146 ? B SER 137 
152 1 Y 1 B ALA 147 ? B ALA 138 
153 1 Y 1 B THR 326 ? B THR 317 
154 1 Y 1 B LYS 327 ? B LYS 318 
155 1 Y 1 B GLU 328 ? B GLU 319 
156 1 Y 1 B GLY 329 ? B GLY 320 
157 1 Y 1 B ALA 518 ? B ALA 509 
158 1 Y 1 B GLY 519 ? B GLY 510 
159 1 Y 1 B LYS 520 ? B LYS 511 
160 1 Y 1 B SER 521 ? B SER 512 
161 1 Y 1 B THR 522 ? B THR 513 
162 1 Y 1 B THR 523 ? B THR 514 
163 1 Y 1 B ASN 524 ? B ASN 515 
164 1 Y 1 B GLY 525 ? B GLY 516 
165 1 Y 1 B GLY 526 ? B GLY 517 
166 1 Y 1 B SER 527 ? B SER 518 
167 1 Y 1 B ALA 528 ? B ALA 519 
168 1 Y 1 B GLY 529 ? B GLY 520 
169 1 Y 1 B SER 530 ? B SER 521 
170 1 Y 1 B GLY 531 ? B GLY 522 
171 1 Y 1 B HIS 532 ? B HIS 523 
172 1 Y 1 B HIS 533 ? B HIS 524 
173 1 Y 1 B HIS 534 ? B HIS 525 
174 1 Y 1 B HIS 535 ? B HIS 526 
175 1 Y 1 B HIS 536 ? B HIS 527 
176 1 Y 1 B HIS 537 ? B HIS 528 
177 1 Y 1 C MET 1   ? C MET 1   
178 1 Y 1 C GLU 2   ? C GLU 2   
179 1 Y 1 C LEU 3   ? C LEU 3   
180 1 Y 1 C LEU 4   ? C LEU 4   
181 1 Y 1 C ILE 5   ? C ILE 5   
182 1 Y 1 C LEU 6   ? C LEU 6   
183 1 Y 1 C LYS 7   ? C LYS 7   
184 1 Y 1 C ALA 8   ? C ALA 8   
185 1 Y 1 C ASN 9   ? C ASN 9   
186 1 Y 1 C ALA 10  ? C ALA 10  
187 1 Y 1 C ILE 11  ? C ILE 11  
188 1 Y 1 C THR 12  ? C THR 12  
189 1 Y 1 C THR 13  ? C THR 13  
190 1 Y 1 C ILE 14  ? C ILE 14  
191 1 Y 1 C LEU 15  ? C LEU 15  
192 1 Y 1 C THR 16  ? C THR 16  
193 1 Y 1 C ALA 17  ? C ALA 17  
194 1 Y 1 C VAL 18  ? C VAL 18  
195 1 Y 1 C THR 19  ? C THR 19  
196 1 Y 1 C PHE 20  ? C PHE 20  
197 1 Y 1 C CYS 21  ? C CYS 21  
198 1 Y 1 C PHE 22  ? C PHE 22  
199 1 Y 1 C ALA 23  ? C ALA 23  
200 1 Y 1 C SER 24  ? C SER 24  
201 1 Y 1 C GLY 25  ? C GLY 25  
202 1 Y 1 C SER 108 ? C SER 99  
203 1 Y 1 C THR 109 ? C THR 100 
204 1 Y 1 C PRO 110 ? C PRO 101 
205 1 Y 1 C ALA 111 ? C ALA 102 
206 1 Y 1 C THR 112 ? C THR 103 
207 1 Y 1 C ASN 113 ? C ASN 104 
208 1 Y 1 C ASN 114 ? C ASN 105 
209 1 Y 1 C ARG 115 ? C ARG 106 
210 1 Y 1 C ALA 116 ? C ALA 107 
211 1 Y 1 C ARG 117 ? C ARG 108 
212 1 Y 1 C ARG 118 ? C ARG 109 
213 1 Y 1 C GLU 119 ? C GLU 110 
214 1 Y 1 C LEU 120 ? C LEU 111 
215 1 Y 1 C PRO 121 ? C PRO 112 
216 1 Y 1 C ARG 122 ? C ARG 113 
217 1 Y 1 C PHE 123 ? C PHE 114 
218 1 Y 1 C MET 124 ? C MET 115 
219 1 Y 1 C ASN 125 ? C ASN 116 
220 1 Y 1 C TYR 126 ? C TYR 117 
221 1 Y 1 C THR 127 ? C THR 118 
222 1 Y 1 C LEU 128 ? C LEU 119 
223 1 Y 1 C ASN 129 ? C ASN 120 
224 1 Y 1 C ASN 130 ? C ASN 121 
225 1 Y 1 C ALA 131 ? C ALA 122 
226 1 Y 1 C LYS 132 ? C LYS 123 
227 1 Y 1 C LYS 133 ? C LYS 124 
228 1 Y 1 C THR 134 ? C THR 125 
229 1 Y 1 C ASN 135 ? C ASN 126 
230 1 Y 1 C VAL 136 ? C VAL 127 
231 1 Y 1 C THR 137 ? C THR 128 
232 1 Y 1 C LEU 138 ? C LEU 129 
233 1 Y 1 C SER 139 ? C SER 130 
234 1 Y 1 C LYS 140 ? C LYS 131 
235 1 Y 1 C LYS 141 ? C LYS 132 
236 1 Y 1 C ARG 142 ? C ARG 133 
237 1 Y 1 C LYS 143 ? C LYS 134 
238 1 Y 1 C ARG 144 ? C ARG 135 
239 1 Y 1 C ARG 145 ? C ARG 136 
240 1 Y 1 C SER 146 ? C SER 137 
241 1 Y 1 C ALA 147 ? C ALA 138 
242 1 Y 1 C ILE 148 ? C ILE 139 
243 1 Y 1 C ALA 149 ? C ALA 140 
244 1 Y 1 C SER 150 ? C SER 141 
245 1 Y 1 C GLY 151 ? C GLY 142 
246 1 Y 1 C ALA 518 ? C ALA 509 
247 1 Y 1 C GLY 519 ? C GLY 510 
248 1 Y 1 C LYS 520 ? C LYS 511 
249 1 Y 1 C SER 521 ? C SER 512 
250 1 Y 1 C THR 522 ? C THR 513 
251 1 Y 1 C THR 523 ? C THR 514 
252 1 Y 1 C ASN 524 ? C ASN 515 
253 1 Y 1 C GLY 525 ? C GLY 516 
254 1 Y 1 C GLY 526 ? C GLY 517 
255 1 Y 1 C SER 527 ? C SER 518 
256 1 Y 1 C ALA 528 ? C ALA 519 
257 1 Y 1 C GLY 529 ? C GLY 520 
258 1 Y 1 C SER 530 ? C SER 521 
259 1 Y 1 C GLY 531 ? C GLY 522 
260 1 Y 1 C HIS 532 ? C HIS 523 
261 1 Y 1 C HIS 533 ? C HIS 524 
262 1 Y 1 C HIS 534 ? C HIS 525 
263 1 Y 1 C HIS 535 ? C HIS 526 
264 1 Y 1 C HIS 536 ? C HIS 527 
265 1 Y 1 C HIS 537 ? C HIS 528 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        N-ACETYL-D-GLUCOSAMINE 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
