data_8S6D
# 
_entry.id   8S6D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8S6D         pdb_00008s6d 10.2210/pdb8s6d/pdb 
WWPDB D_1292136817 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8S6D 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              poppe@mail.bme.hu 
_pdbx_contact_author.name_first         Laszlo 
_pdbx_contact_author.name_last          Poppe 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8358-1378 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nagy, G.N.'     1 0000-0003-1761-5610 
'Incze, D.J.'    2 0009-0009-1818-8690 
'Bata, Z.'       3 0000-0002-4840-9433 
'Molnar, Z.'     4 0000-0002-9552-7061 
'Leveles, I.'    5 0000-0003-1821-1132 
'Vertessy, B.G.' 6 0000-0002-1288-2982 
'Poppe, L.'      7 0000-0002-8358-1378 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Food Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           0308-8146 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            473 
_citation.language                  ? 
_citation.page_first                143110 
_citation.page_last                 143110 
_citation.title                     
'Understanding the molecular mechanism of fumonisin esterases by kinetic and structural studies.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.foodchem.2025.143110 
_citation.pdbx_database_id_PubMed   39892340 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Incze, D.J.'    1 ? 
primary 'Molnar, Z.'     2 ? 
primary 'Nagy, G.N.'     3 ? 
primary 'Leveles, I.'    4 ? 
primary 'Vertessy, B.G.' 5 ? 
primary 'Poppe, L.'      6 ? 
primary 'Bata, Z.'       7 ? 
# 
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 'Fumonisin B1 esterase' 52219.664 1   3.1.1.87 ? ? ? 
2 water   nat water                   18.015    325 ?        ? ? ? 
# 
_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       
;MAGAATATDFPVRRTDLGQVQGLAGDVMSFRGIPYAAPPVGGLRWKPPQHARPWAGVRPATQFGSDCFGAAYLRKGSLAP
GVSEDCLYLNVWAPSGAKPGQYPVMVWVYGGGFAGGTAAMPYYDGEALARQGVVVVTFNYRTNILGFFAHPGLSRESPTG
TSGNYGLLDILAALRWVQSNARAFGGDPGRVTVFGESAGASAIGLLLTSPLSKGLFRGAILESPGLTRPLATLADSAASG
ERLDADLSRLRSTDPATLMARADAARPASRDLRRPRPTGPIVDGHVLPQTDSAAIAAGQLAPVRVLIGTNADEGRAFLGR
APMETPADYQAYLEAQFGDQAAAVAACYPLDGRATPKEMVARIFGDNQFNRGVSAFSEALVRQGAPVWRYQFNGNTEGGR
APATHGAEIPYVFGVFKLDELGLFDWPPEGPTPADRALGQLMSSAWVRFAKNGDPAGDALTWPAYSTGKSTMTFGPEGRA
AVVSPGPSIPPCADGAKAG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAGAATATDFPVRRTDLGQVQGLAGDVMSFRGIPYAAPPVGGLRWKPPQHARPWAGVRPATQFGSDCFGAAYLRKGSLAP
GVSEDCLYLNVWAPSGAKPGQYPVMVWVYGGGFAGGTAAMPYYDGEALARQGVVVVTFNYRTNILGFFAHPGLSRESPTG
TSGNYGLLDILAALRWVQSNARAFGGDPGRVTVFGESAGASAIGLLLTSPLSKGLFRGAILESPGLTRPLATLADSAASG
ERLDADLSRLRSTDPATLMARADAARPASRDLRRPRPTGPIVDGHVLPQTDSAAIAAGQLAPVRVLIGTNADEGRAFLGR
APMETPADYQAYLEAQFGDQAAAVAACYPLDGRATPKEMVARIFGDNQFNRGVSAFSEALVRQGAPVWRYQFNGNTEGGR
APATHGAEIPYVFGVFKLDELGLFDWPPEGPTPADRALGQLMSSAWVRFAKNGDPAGDALTWPAYSTGKSTMTFGPEGRA
AVVSPGPSIPPCADGAKAG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLY n 
1 4   ALA n 
1 5   ALA n 
1 6   THR n 
1 7   ALA n 
1 8   THR n 
1 9   ASP n 
1 10  PHE n 
1 11  PRO n 
1 12  VAL n 
1 13  ARG n 
1 14  ARG n 
1 15  THR n 
1 16  ASP n 
1 17  LEU n 
1 18  GLY n 
1 19  GLN n 
1 20  VAL n 
1 21  GLN n 
1 22  GLY n 
1 23  LEU n 
1 24  ALA n 
1 25  GLY n 
1 26  ASP n 
1 27  VAL n 
1 28  MET n 
1 29  SER n 
1 30  PHE n 
1 31  ARG n 
1 32  GLY n 
1 33  ILE n 
1 34  PRO n 
1 35  TYR n 
1 36  ALA n 
1 37  ALA n 
1 38  PRO n 
1 39  PRO n 
1 40  VAL n 
1 41  GLY n 
1 42  GLY n 
1 43  LEU n 
1 44  ARG n 
1 45  TRP n 
1 46  LYS n 
1 47  PRO n 
1 48  PRO n 
1 49  GLN n 
1 50  HIS n 
1 51  ALA n 
1 52  ARG n 
1 53  PRO n 
1 54  TRP n 
1 55  ALA n 
1 56  GLY n 
1 57  VAL n 
1 58  ARG n 
1 59  PRO n 
1 60  ALA n 
1 61  THR n 
1 62  GLN n 
1 63  PHE n 
1 64  GLY n 
1 65  SER n 
1 66  ASP n 
1 67  CYS n 
1 68  PHE n 
1 69  GLY n 
1 70  ALA n 
1 71  ALA n 
1 72  TYR n 
1 73  LEU n 
1 74  ARG n 
1 75  LYS n 
1 76  GLY n 
1 77  SER n 
1 78  LEU n 
1 79  ALA n 
1 80  PRO n 
1 81  GLY n 
1 82  VAL n 
1 83  SER n 
1 84  GLU n 
1 85  ASP n 
1 86  CYS n 
1 87  LEU n 
1 88  TYR n 
1 89  LEU n 
1 90  ASN n 
1 91  VAL n 
1 92  TRP n 
1 93  ALA n 
1 94  PRO n 
1 95  SER n 
1 96  GLY n 
1 97  ALA n 
1 98  LYS n 
1 99  PRO n 
1 100 GLY n 
1 101 GLN n 
1 102 TYR n 
1 103 PRO n 
1 104 VAL n 
1 105 MET n 
1 106 VAL n 
1 107 TRP n 
1 108 VAL n 
1 109 TYR n 
1 110 GLY n 
1 111 GLY n 
1 112 GLY n 
1 113 PHE n 
1 114 ALA n 
1 115 GLY n 
1 116 GLY n 
1 117 THR n 
1 118 ALA n 
1 119 ALA n 
1 120 MET n 
1 121 PRO n 
1 122 TYR n 
1 123 TYR n 
1 124 ASP n 
1 125 GLY n 
1 126 GLU n 
1 127 ALA n 
1 128 LEU n 
1 129 ALA n 
1 130 ARG n 
1 131 GLN n 
1 132 GLY n 
1 133 VAL n 
1 134 VAL n 
1 135 VAL n 
1 136 VAL n 
1 137 THR n 
1 138 PHE n 
1 139 ASN n 
1 140 TYR n 
1 141 ARG n 
1 142 THR n 
1 143 ASN n 
1 144 ILE n 
1 145 LEU n 
1 146 GLY n 
1 147 PHE n 
1 148 PHE n 
1 149 ALA n 
1 150 HIS n 
1 151 PRO n 
1 152 GLY n 
1 153 LEU n 
1 154 SER n 
1 155 ARG n 
1 156 GLU n 
1 157 SER n 
1 158 PRO n 
1 159 THR n 
1 160 GLY n 
1 161 THR n 
1 162 SER n 
1 163 GLY n 
1 164 ASN n 
1 165 TYR n 
1 166 GLY n 
1 167 LEU n 
1 168 LEU n 
1 169 ASP n 
1 170 ILE n 
1 171 LEU n 
1 172 ALA n 
1 173 ALA n 
1 174 LEU n 
1 175 ARG n 
1 176 TRP n 
1 177 VAL n 
1 178 GLN n 
1 179 SER n 
1 180 ASN n 
1 181 ALA n 
1 182 ARG n 
1 183 ALA n 
1 184 PHE n 
1 185 GLY n 
1 186 GLY n 
1 187 ASP n 
1 188 PRO n 
1 189 GLY n 
1 190 ARG n 
1 191 VAL n 
1 192 THR n 
1 193 VAL n 
1 194 PHE n 
1 195 GLY n 
1 196 GLU n 
1 197 SER n 
1 198 ALA n 
1 199 GLY n 
1 200 ALA n 
1 201 SER n 
1 202 ALA n 
1 203 ILE n 
1 204 GLY n 
1 205 LEU n 
1 206 LEU n 
1 207 LEU n 
1 208 THR n 
1 209 SER n 
1 210 PRO n 
1 211 LEU n 
1 212 SER n 
1 213 LYS n 
1 214 GLY n 
1 215 LEU n 
1 216 PHE n 
1 217 ARG n 
1 218 GLY n 
1 219 ALA n 
1 220 ILE n 
1 221 LEU n 
1 222 GLU n 
1 223 SER n 
1 224 PRO n 
1 225 GLY n 
1 226 LEU n 
1 227 THR n 
1 228 ARG n 
1 229 PRO n 
1 230 LEU n 
1 231 ALA n 
1 232 THR n 
1 233 LEU n 
1 234 ALA n 
1 235 ASP n 
1 236 SER n 
1 237 ALA n 
1 238 ALA n 
1 239 SER n 
1 240 GLY n 
1 241 GLU n 
1 242 ARG n 
1 243 LEU n 
1 244 ASP n 
1 245 ALA n 
1 246 ASP n 
1 247 LEU n 
1 248 SER n 
1 249 ARG n 
1 250 LEU n 
1 251 ARG n 
1 252 SER n 
1 253 THR n 
1 254 ASP n 
1 255 PRO n 
1 256 ALA n 
1 257 THR n 
1 258 LEU n 
1 259 MET n 
1 260 ALA n 
1 261 ARG n 
1 262 ALA n 
1 263 ASP n 
1 264 ALA n 
1 265 ALA n 
1 266 ARG n 
1 267 PRO n 
1 268 ALA n 
1 269 SER n 
1 270 ARG n 
1 271 ASP n 
1 272 LEU n 
1 273 ARG n 
1 274 ARG n 
1 275 PRO n 
1 276 ARG n 
1 277 PRO n 
1 278 THR n 
1 279 GLY n 
1 280 PRO n 
1 281 ILE n 
1 282 VAL n 
1 283 ASP n 
1 284 GLY n 
1 285 HIS n 
1 286 VAL n 
1 287 LEU n 
1 288 PRO n 
1 289 GLN n 
1 290 THR n 
1 291 ASP n 
1 292 SER n 
1 293 ALA n 
1 294 ALA n 
1 295 ILE n 
1 296 ALA n 
1 297 ALA n 
1 298 GLY n 
1 299 GLN n 
1 300 LEU n 
1 301 ALA n 
1 302 PRO n 
1 303 VAL n 
1 304 ARG n 
1 305 VAL n 
1 306 LEU n 
1 307 ILE n 
1 308 GLY n 
1 309 THR n 
1 310 ASN n 
1 311 ALA n 
1 312 ASP n 
1 313 GLU n 
1 314 GLY n 
1 315 ARG n 
1 316 ALA n 
1 317 PHE n 
1 318 LEU n 
1 319 GLY n 
1 320 ARG n 
1 321 ALA n 
1 322 PRO n 
1 323 MET n 
1 324 GLU n 
1 325 THR n 
1 326 PRO n 
1 327 ALA n 
1 328 ASP n 
1 329 TYR n 
1 330 GLN n 
1 331 ALA n 
1 332 TYR n 
1 333 LEU n 
1 334 GLU n 
1 335 ALA n 
1 336 GLN n 
1 337 PHE n 
1 338 GLY n 
1 339 ASP n 
1 340 GLN n 
1 341 ALA n 
1 342 ALA n 
1 343 ALA n 
1 344 VAL n 
1 345 ALA n 
1 346 ALA n 
1 347 CYS n 
1 348 TYR n 
1 349 PRO n 
1 350 LEU n 
1 351 ASP n 
1 352 GLY n 
1 353 ARG n 
1 354 ALA n 
1 355 THR n 
1 356 PRO n 
1 357 LYS n 
1 358 GLU n 
1 359 MET n 
1 360 VAL n 
1 361 ALA n 
1 362 ARG n 
1 363 ILE n 
1 364 PHE n 
1 365 GLY n 
1 366 ASP n 
1 367 ASN n 
1 368 GLN n 
1 369 PHE n 
1 370 ASN n 
1 371 ARG n 
1 372 GLY n 
1 373 VAL n 
1 374 SER n 
1 375 ALA n 
1 376 PHE n 
1 377 SER n 
1 378 GLU n 
1 379 ALA n 
1 380 LEU n 
1 381 VAL n 
1 382 ARG n 
1 383 GLN n 
1 384 GLY n 
1 385 ALA n 
1 386 PRO n 
1 387 VAL n 
1 388 TRP n 
1 389 ARG n 
1 390 TYR n 
1 391 GLN n 
1 392 PHE n 
1 393 ASN n 
1 394 GLY n 
1 395 ASN n 
1 396 THR n 
1 397 GLU n 
1 398 GLY n 
1 399 GLY n 
1 400 ARG n 
1 401 ALA n 
1 402 PRO n 
1 403 ALA n 
1 404 THR n 
1 405 HIS n 
1 406 GLY n 
1 407 ALA n 
1 408 GLU n 
1 409 ILE n 
1 410 PRO n 
1 411 TYR n 
1 412 VAL n 
1 413 PHE n 
1 414 GLY n 
1 415 VAL n 
1 416 PHE n 
1 417 LYS n 
1 418 LEU n 
1 419 ASP n 
1 420 GLU n 
1 421 LEU n 
1 422 GLY n 
1 423 LEU n 
1 424 PHE n 
1 425 ASP n 
1 426 TRP n 
1 427 PRO n 
1 428 PRO n 
1 429 GLU n 
1 430 GLY n 
1 431 PRO n 
1 432 THR n 
1 433 PRO n 
1 434 ALA n 
1 435 ASP n 
1 436 ARG n 
1 437 ALA n 
1 438 LEU n 
1 439 GLY n 
1 440 GLN n 
1 441 LEU n 
1 442 MET n 
1 443 SER n 
1 444 SER n 
1 445 ALA n 
1 446 TRP n 
1 447 VAL n 
1 448 ARG n 
1 449 PHE n 
1 450 ALA n 
1 451 LYS n 
1 452 ASN n 
1 453 GLY n 
1 454 ASP n 
1 455 PRO n 
1 456 ALA n 
1 457 GLY n 
1 458 ASP n 
1 459 ALA n 
1 460 LEU n 
1 461 THR n 
1 462 TRP n 
1 463 PRO n 
1 464 ALA n 
1 465 TYR n 
1 466 SER n 
1 467 THR n 
1 468 GLY n 
1 469 LYS n 
1 470 SER n 
1 471 THR n 
1 472 MET n 
1 473 THR n 
1 474 PHE n 
1 475 GLY n 
1 476 PRO n 
1 477 GLU n 
1 478 GLY n 
1 479 ARG n 
1 480 ALA n 
1 481 ALA n 
1 482 VAL n 
1 483 VAL n 
1 484 SER n 
1 485 PRO n 
1 486 GLY n 
1 487 PRO n 
1 488 SER n 
1 489 ILE n 
1 490 PRO n 
1 491 PRO n 
1 492 CYS n 
1 493 ALA n 
1 494 ASP n 
1 495 GLY n 
1 496 ALA n 
1 497 LYS n 
1 498 ALA n 
1 499 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   499 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Caulobacter sp.' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     78 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 55552 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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               PPS-9010 
_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                       pD912 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   31  ?   ?   ?   A . n 
A 1 2   ALA 2   32  ?   ?   ?   A . n 
A 1 3   GLY 3   33  ?   ?   ?   A . n 
A 1 4   ALA 4   34  ?   ?   ?   A . n 
A 1 5   ALA 5   35  ?   ?   ?   A . n 
A 1 6   THR 6   36  ?   ?   ?   A . n 
A 1 7   ALA 7   37  ?   ?   ?   A . n 
A 1 8   THR 8   38  ?   ?   ?   A . n 
A 1 9   ASP 9   39  9   ASP ASP A . n 
A 1 10  PHE 10  40  10  PHE PHE A . n 
A 1 11  PRO 11  41  11  PRO PRO A . n 
A 1 12  VAL 12  42  12  VAL VAL A . n 
A 1 13  ARG 13  43  13  ARG ARG A . n 
A 1 14  ARG 14  44  14  ARG ARG A . n 
A 1 15  THR 15  45  15  THR THR A . n 
A 1 16  ASP 16  46  16  ASP ASP A . n 
A 1 17  LEU 17  47  17  LEU LEU A . n 
A 1 18  GLY 18  48  18  GLY GLY A . n 
A 1 19  GLN 19  49  19  GLN GLN A . n 
A 1 20  VAL 20  50  20  VAL VAL A . n 
A 1 21  GLN 21  51  21  GLN GLN A . n 
A 1 22  GLY 22  52  22  GLY GLY A . n 
A 1 23  LEU 23  53  23  LEU LEU A . n 
A 1 24  ALA 24  54  24  ALA ALA A . n 
A 1 25  GLY 25  55  25  GLY GLY A . n 
A 1 26  ASP 26  56  26  ASP ASP A . n 
A 1 27  VAL 27  57  27  VAL VAL A . n 
A 1 28  MET 28  58  28  MET MET A . n 
A 1 29  SER 29  59  29  SER SER A . n 
A 1 30  PHE 30  60  30  PHE PHE A . n 
A 1 31  ARG 31  61  31  ARG ARG A . n 
A 1 32  GLY 32  62  32  GLY GLY A . n 
A 1 33  ILE 33  63  33  ILE ILE A . n 
A 1 34  PRO 34  64  34  PRO PRO A . n 
A 1 35  TYR 35  65  35  TYR TYR A . n 
A 1 36  ALA 36  66  36  ALA ALA A . n 
A 1 37  ALA 37  67  37  ALA ALA A . n 
A 1 38  PRO 38  68  38  PRO PRO A . n 
A 1 39  PRO 39  69  39  PRO PRO A . n 
A 1 40  VAL 40  70  40  VAL VAL A . n 
A 1 41  GLY 41  71  41  GLY GLY A . n 
A 1 42  GLY 42  72  42  GLY GLY A . n 
A 1 43  LEU 43  73  43  LEU LEU A . n 
A 1 44  ARG 44  74  44  ARG ARG A . n 
A 1 45  TRP 45  75  45  TRP TRP A . n 
A 1 46  LYS 46  76  46  LYS LYS A . n 
A 1 47  PRO 47  77  47  PRO PRO A . n 
A 1 48  PRO 48  78  48  PRO PRO A . n 
A 1 49  GLN 49  79  49  GLN GLN A . n 
A 1 50  HIS 50  80  50  HIS HIS A . n 
A 1 51  ALA 51  81  51  ALA ALA A . n 
A 1 52  ARG 52  82  52  ARG ARG A . n 
A 1 53  PRO 53  83  53  PRO PRO A . n 
A 1 54  TRP 54  84  54  TRP TRP A . n 
A 1 55  ALA 55  85  55  ALA ALA A . n 
A 1 56  GLY 56  86  56  GLY GLY A . n 
A 1 57  VAL 57  87  57  VAL VAL A . n 
A 1 58  ARG 58  88  58  ARG ARG A . n 
A 1 59  PRO 59  89  59  PRO PRO A . n 
A 1 60  ALA 60  90  60  ALA ALA A . n 
A 1 61  THR 61  91  61  THR THR A . n 
A 1 62  GLN 62  92  62  GLN GLN A . n 
A 1 63  PHE 63  93  63  PHE PHE A . n 
A 1 64  GLY 64  94  64  GLY GLY A . n 
A 1 65  SER 65  95  65  SER SER A . n 
A 1 66  ASP 66  96  66  ASP ASP A . n 
A 1 67  CYS 67  97  67  CYS CYS A . n 
A 1 68  PHE 68  98  68  PHE PHE A . n 
A 1 69  GLY 69  99  69  GLY GLY A . n 
A 1 70  ALA 70  100 70  ALA ALA A . n 
A 1 71  ALA 71  101 71  ALA ALA A . n 
A 1 72  TYR 72  102 72  TYR TYR A . n 
A 1 73  LEU 73  103 73  LEU LEU A . n 
A 1 74  ARG 74  104 74  ARG ARG A . n 
A 1 75  LYS 75  105 75  LYS LYS A . n 
A 1 76  GLY 76  106 76  GLY GLY A . n 
A 1 77  SER 77  107 77  SER SER A . n 
A 1 78  LEU 78  108 78  LEU LEU A . n 
A 1 79  ALA 79  109 79  ALA ALA A . n 
A 1 80  PRO 80  110 80  PRO PRO A . n 
A 1 81  GLY 81  111 81  GLY GLY A . n 
A 1 82  VAL 82  112 82  VAL VAL A . n 
A 1 83  SER 83  113 83  SER SER A . n 
A 1 84  GLU 84  114 84  GLU GLU A . n 
A 1 85  ASP 85  115 85  ASP ASP A . n 
A 1 86  CYS 86  116 86  CYS CYS A . n 
A 1 87  LEU 87  117 87  LEU LEU A . n 
A 1 88  TYR 88  118 88  TYR TYR A . n 
A 1 89  LEU 89  119 89  LEU LEU A . n 
A 1 90  ASN 90  120 90  ASN ASN A . n 
A 1 91  VAL 91  121 91  VAL VAL A . n 
A 1 92  TRP 92  122 92  TRP TRP A . n 
A 1 93  ALA 93  123 93  ALA ALA A . n 
A 1 94  PRO 94  124 94  PRO PRO A . n 
A 1 95  SER 95  125 95  SER SER A . n 
A 1 96  GLY 96  126 96  GLY GLY A . n 
A 1 97  ALA 97  127 97  ALA ALA A . n 
A 1 98  LYS 98  128 98  LYS LYS A . n 
A 1 99  PRO 99  129 99  PRO PRO A . n 
A 1 100 GLY 100 130 100 GLY GLY A . n 
A 1 101 GLN 101 131 101 GLN GLN A . n 
A 1 102 TYR 102 132 102 TYR TYR A . n 
A 1 103 PRO 103 133 103 PRO PRO A . n 
A 1 104 VAL 104 134 104 VAL VAL A . n 
A 1 105 MET 105 135 105 MET MET A . n 
A 1 106 VAL 106 136 106 VAL VAL A . n 
A 1 107 TRP 107 137 107 TRP TRP A . n 
A 1 108 VAL 108 138 108 VAL VAL A . n 
A 1 109 TYR 109 139 109 TYR TYR A . n 
A 1 110 GLY 110 140 110 GLY GLY A . n 
A 1 111 GLY 111 141 111 GLY GLY A . n 
A 1 112 GLY 112 142 112 GLY GLY A . n 
A 1 113 PHE 113 143 113 PHE PHE A . n 
A 1 114 ALA 114 144 114 ALA ALA A . n 
A 1 115 GLY 115 145 115 GLY GLY A . n 
A 1 116 GLY 116 146 116 GLY GLY A . n 
A 1 117 THR 117 147 117 THR THR A . n 
A 1 118 ALA 118 148 118 ALA ALA A . n 
A 1 119 ALA 119 149 119 ALA ALA A . n 
A 1 120 MET 120 150 120 MET MET A . n 
A 1 121 PRO 121 151 121 PRO PRO A . n 
A 1 122 TYR 122 152 122 TYR TYR A . n 
A 1 123 TYR 123 153 123 TYR TYR A . n 
A 1 124 ASP 124 154 124 ASP ASP A . n 
A 1 125 GLY 125 155 125 GLY GLY A . n 
A 1 126 GLU 126 156 126 GLU GLU A . n 
A 1 127 ALA 127 157 127 ALA ALA A . n 
A 1 128 LEU 128 158 128 LEU LEU A . n 
A 1 129 ALA 129 159 129 ALA ALA A . n 
A 1 130 ARG 130 160 130 ARG ARG A . n 
A 1 131 GLN 131 161 131 GLN GLN A . n 
A 1 132 GLY 132 162 132 GLY GLY A . n 
A 1 133 VAL 133 163 133 VAL VAL A . n 
A 1 134 VAL 134 164 134 VAL VAL A . n 
A 1 135 VAL 135 165 135 VAL VAL A . n 
A 1 136 VAL 136 166 136 VAL VAL A . n 
A 1 137 THR 137 167 137 THR THR A . n 
A 1 138 PHE 138 168 138 PHE PHE A . n 
A 1 139 ASN 139 169 139 ASN ASN A . n 
A 1 140 TYR 140 170 140 TYR TYR A . n 
A 1 141 ARG 141 171 141 ARG ARG A . n 
A 1 142 THR 142 172 142 THR THR A . n 
A 1 143 ASN 143 173 143 ASN ASN A . n 
A 1 144 ILE 144 174 144 ILE ILE A . n 
A 1 145 LEU 145 175 145 LEU LEU A . n 
A 1 146 GLY 146 176 146 GLY GLY A . n 
A 1 147 PHE 147 177 147 PHE PHE A . n 
A 1 148 PHE 148 178 148 PHE PHE A . n 
A 1 149 ALA 149 179 149 ALA ALA A . n 
A 1 150 HIS 150 180 150 HIS HIS A . n 
A 1 151 PRO 151 181 151 PRO PRO A . n 
A 1 152 GLY 152 182 152 GLY GLY A . n 
A 1 153 LEU 153 183 153 LEU LEU A . n 
A 1 154 SER 154 184 154 SER SER A . n 
A 1 155 ARG 155 185 155 ARG ARG A . n 
A 1 156 GLU 156 186 156 GLU GLU A . n 
A 1 157 SER 157 187 157 SER SER A . n 
A 1 158 PRO 158 188 158 PRO PRO A . n 
A 1 159 THR 159 189 159 THR THR A . n 
A 1 160 GLY 160 190 160 GLY GLY A . n 
A 1 161 THR 161 191 161 THR THR A . n 
A 1 162 SER 162 192 162 SER SER A . n 
A 1 163 GLY 163 193 163 GLY GLY A . n 
A 1 164 ASN 164 194 164 ASN ASN A . n 
A 1 165 TYR 165 195 165 TYR TYR A . n 
A 1 166 GLY 166 196 166 GLY GLY A . n 
A 1 167 LEU 167 197 167 LEU LEU A . n 
A 1 168 LEU 168 198 168 LEU LEU A . n 
A 1 169 ASP 169 199 169 ASP ASP A . n 
A 1 170 ILE 170 200 170 ILE ILE A . n 
A 1 171 LEU 171 201 171 LEU LEU A . n 
A 1 172 ALA 172 202 172 ALA ALA A . n 
A 1 173 ALA 173 203 173 ALA ALA A . n 
A 1 174 LEU 174 204 174 LEU LEU A . n 
A 1 175 ARG 175 205 175 ARG ARG A . n 
A 1 176 TRP 176 206 176 TRP TRP A . n 
A 1 177 VAL 177 207 177 VAL VAL A . n 
A 1 178 GLN 178 208 178 GLN GLN A . n 
A 1 179 SER 179 209 179 SER SER A . n 
A 1 180 ASN 180 210 180 ASN ASN A . n 
A 1 181 ALA 181 211 181 ALA ALA A . n 
A 1 182 ARG 182 212 182 ARG ARG A . n 
A 1 183 ALA 183 213 183 ALA ALA A . n 
A 1 184 PHE 184 214 184 PHE PHE A . n 
A 1 185 GLY 185 215 185 GLY GLY A . n 
A 1 186 GLY 186 216 186 GLY GLY A . n 
A 1 187 ASP 187 217 187 ASP ASP A . n 
A 1 188 PRO 188 218 188 PRO PRO A . n 
A 1 189 GLY 189 219 189 GLY GLY A . n 
A 1 190 ARG 190 220 190 ARG ARG A . n 
A 1 191 VAL 191 221 191 VAL VAL A . n 
A 1 192 THR 192 222 192 THR THR A . n 
A 1 193 VAL 193 223 193 VAL VAL A . n 
A 1 194 PHE 194 224 194 PHE PHE A . n 
A 1 195 GLY 195 225 195 GLY GLY A . n 
A 1 196 GLU 196 226 196 GLU GLU A . n 
A 1 197 SER 197 227 197 SER SER A . n 
A 1 198 ALA 198 228 198 ALA ALA A . n 
A 1 199 GLY 199 229 199 GLY GLY A . n 
A 1 200 ALA 200 230 200 ALA ALA A . n 
A 1 201 SER 201 231 201 SER SER A . n 
A 1 202 ALA 202 232 202 ALA ALA A . n 
A 1 203 ILE 203 233 203 ILE ILE A . n 
A 1 204 GLY 204 234 204 GLY GLY A . n 
A 1 205 LEU 205 235 205 LEU LEU A . n 
A 1 206 LEU 206 236 206 LEU LEU A . n 
A 1 207 LEU 207 237 207 LEU LEU A . n 
A 1 208 THR 208 238 208 THR THR A . n 
A 1 209 SER 209 239 209 SER SER A . n 
A 1 210 PRO 210 240 210 PRO PRO A . n 
A 1 211 LEU 211 241 211 LEU LEU A . n 
A 1 212 SER 212 242 212 SER SER A . n 
A 1 213 LYS 213 243 213 LYS LYS A . n 
A 1 214 GLY 214 244 214 GLY GLY A . n 
A 1 215 LEU 215 245 215 LEU LEU A . n 
A 1 216 PHE 216 246 216 PHE PHE A . n 
A 1 217 ARG 217 247 217 ARG ARG A . n 
A 1 218 GLY 218 248 218 GLY GLY A . n 
A 1 219 ALA 219 249 219 ALA ALA A . n 
A 1 220 ILE 220 250 220 ILE ILE A . n 
A 1 221 LEU 221 251 221 LEU LEU A . n 
A 1 222 GLU 222 252 222 GLU GLU A . n 
A 1 223 SER 223 253 223 SER SER A . n 
A 1 224 PRO 224 254 224 PRO PRO A . n 
A 1 225 GLY 225 255 225 GLY GLY A . n 
A 1 226 LEU 226 256 226 LEU LEU A . n 
A 1 227 THR 227 257 227 THR THR A . n 
A 1 228 ARG 228 258 228 ARG ARG A . n 
A 1 229 PRO 229 259 229 PRO PRO A . n 
A 1 230 LEU 230 260 230 LEU LEU A . n 
A 1 231 ALA 231 261 231 ALA ALA A . n 
A 1 232 THR 232 262 232 THR THR A . n 
A 1 233 LEU 233 263 233 LEU LEU A . n 
A 1 234 ALA 234 264 234 ALA ALA A . n 
A 1 235 ASP 235 265 235 ASP ASP A . n 
A 1 236 SER 236 266 236 SER SER A . n 
A 1 237 ALA 237 267 237 ALA ALA A . n 
A 1 238 ALA 238 268 238 ALA ALA A . n 
A 1 239 SER 239 269 239 SER SER A . n 
A 1 240 GLY 240 270 240 GLY GLY A . n 
A 1 241 GLU 241 271 241 GLU GLU A . n 
A 1 242 ARG 242 272 242 ARG ARG A . n 
A 1 243 LEU 243 273 243 LEU LEU A . n 
A 1 244 ASP 244 274 244 ASP ASP A . n 
A 1 245 ALA 245 275 245 ALA ALA A . n 
A 1 246 ASP 246 276 246 ASP ASP A . n 
A 1 247 LEU 247 277 247 LEU LEU A . n 
A 1 248 SER 248 278 248 SER SER A . n 
A 1 249 ARG 249 279 249 ARG ARG A . n 
A 1 250 LEU 250 280 250 LEU LEU A . n 
A 1 251 ARG 251 281 251 ARG ARG A . n 
A 1 252 SER 252 282 252 SER SER A . n 
A 1 253 THR 253 283 253 THR THR A . n 
A 1 254 ASP 254 284 254 ASP ASP A . n 
A 1 255 PRO 255 285 255 PRO PRO A . n 
A 1 256 ALA 256 286 256 ALA ALA A . n 
A 1 257 THR 257 287 257 THR THR A . n 
A 1 258 LEU 258 288 258 LEU LEU A . n 
A 1 259 MET 259 289 259 MET MET A . n 
A 1 260 ALA 260 290 260 ALA ALA A . n 
A 1 261 ARG 261 291 261 ARG ARG A . n 
A 1 262 ALA 262 292 262 ALA ALA A . n 
A 1 263 ASP 263 293 263 ASP ASP A . n 
A 1 264 ALA 264 294 264 ALA ALA A . n 
A 1 265 ALA 265 295 265 ALA ALA A . n 
A 1 266 ARG 266 296 266 ARG ARG A . n 
A 1 267 PRO 267 297 267 PRO PRO A . n 
A 1 268 ALA 268 298 268 ALA ALA A . n 
A 1 269 SER 269 299 269 SER SER A . n 
A 1 270 ARG 270 300 270 ARG ARG A . n 
A 1 271 ASP 271 301 271 ASP ASP A . n 
A 1 272 LEU 272 302 272 LEU LEU A . n 
A 1 273 ARG 273 303 273 ARG ARG A . n 
A 1 274 ARG 274 304 274 ARG ARG A . n 
A 1 275 PRO 275 305 275 PRO PRO A . n 
A 1 276 ARG 276 306 276 ARG ARG A . n 
A 1 277 PRO 277 307 277 PRO PRO A . n 
A 1 278 THR 278 308 278 THR THR A . n 
A 1 279 GLY 279 309 279 GLY GLY A . n 
A 1 280 PRO 280 310 280 PRO PRO A . n 
A 1 281 ILE 281 311 281 ILE ILE A . n 
A 1 282 VAL 282 312 282 VAL VAL A . n 
A 1 283 ASP 283 313 283 ASP ASP A . n 
A 1 284 GLY 284 314 284 GLY GLY A . n 
A 1 285 HIS 285 315 285 HIS HIS A . n 
A 1 286 VAL 286 316 286 VAL VAL A . n 
A 1 287 LEU 287 317 287 LEU LEU A . n 
A 1 288 PRO 288 318 288 PRO PRO A . n 
A 1 289 GLN 289 319 289 GLN GLN A . n 
A 1 290 THR 290 320 290 THR THR A . n 
A 1 291 ASP 291 321 291 ASP ASP A . n 
A 1 292 SER 292 322 292 SER SER A . n 
A 1 293 ALA 293 323 293 ALA ALA A . n 
A 1 294 ALA 294 324 294 ALA ALA A . n 
A 1 295 ILE 295 325 295 ILE ILE A . n 
A 1 296 ALA 296 326 296 ALA ALA A . n 
A 1 297 ALA 297 327 297 ALA ALA A . n 
A 1 298 GLY 298 328 298 GLY GLY A . n 
A 1 299 GLN 299 329 299 GLN GLN A . n 
A 1 300 LEU 300 330 300 LEU LEU A . n 
A 1 301 ALA 301 331 301 ALA ALA A . n 
A 1 302 PRO 302 332 302 PRO PRO A . n 
A 1 303 VAL 303 333 303 VAL VAL A . n 
A 1 304 ARG 304 334 304 ARG ARG A . n 
A 1 305 VAL 305 335 305 VAL VAL A . n 
A 1 306 LEU 306 336 306 LEU LEU A . n 
A 1 307 ILE 307 337 307 ILE ILE A . n 
A 1 308 GLY 308 338 308 GLY GLY A . n 
A 1 309 THR 309 339 309 THR THR A . n 
A 1 310 ASN 310 340 310 ASN ASN A . n 
A 1 311 ALA 311 341 311 ALA ALA A . n 
A 1 312 ASP 312 342 312 ASP ASP A . n 
A 1 313 GLU 313 343 313 GLU GLU A . n 
A 1 314 GLY 314 344 314 GLY GLY A . n 
A 1 315 ARG 315 345 315 ARG ARG A . n 
A 1 316 ALA 316 346 316 ALA ALA A . n 
A 1 317 PHE 317 347 317 PHE PHE A . n 
A 1 318 LEU 318 348 318 LEU LEU A . n 
A 1 319 GLY 319 349 319 GLY GLY A . n 
A 1 320 ARG 320 350 320 ARG ARG A . n 
A 1 321 ALA 321 351 321 ALA ALA A . n 
A 1 322 PRO 322 352 322 PRO PRO A . n 
A 1 323 MET 323 353 323 MET MET A . n 
A 1 324 GLU 324 354 324 GLU GLU A . n 
A 1 325 THR 325 355 325 THR THR A . n 
A 1 326 PRO 326 356 326 PRO PRO A . n 
A 1 327 ALA 327 357 327 ALA ALA A . n 
A 1 328 ASP 328 358 328 ASP ASP A . n 
A 1 329 TYR 329 359 329 TYR TYR A . n 
A 1 330 GLN 330 360 330 GLN GLN A . n 
A 1 331 ALA 331 361 331 ALA ALA A . n 
A 1 332 TYR 332 362 332 TYR TYR A . n 
A 1 333 LEU 333 363 333 LEU LEU A . n 
A 1 334 GLU 334 364 334 GLU GLU A . n 
A 1 335 ALA 335 365 335 ALA ALA A . n 
A 1 336 GLN 336 366 336 GLN GLN A . n 
A 1 337 PHE 337 367 337 PHE PHE A . n 
A 1 338 GLY 338 368 338 GLY GLY A . n 
A 1 339 ASP 339 369 339 ASP ASP A . n 
A 1 340 GLN 340 370 340 GLN GLN A . n 
A 1 341 ALA 341 371 341 ALA ALA A . n 
A 1 342 ALA 342 372 342 ALA ALA A . n 
A 1 343 ALA 343 373 343 ALA ALA A . n 
A 1 344 VAL 344 374 344 VAL VAL A . n 
A 1 345 ALA 345 375 345 ALA ALA A . n 
A 1 346 ALA 346 376 346 ALA ALA A . n 
A 1 347 CYS 347 377 347 CYS CYS A . n 
A 1 348 TYR 348 378 348 TYR TYR A . n 
A 1 349 PRO 349 379 349 PRO PRO A . n 
A 1 350 LEU 350 380 350 LEU LEU A . n 
A 1 351 ASP 351 381 351 ASP ASP A . n 
A 1 352 GLY 352 382 352 GLY GLY A . n 
A 1 353 ARG 353 383 353 ARG ARG A . n 
A 1 354 ALA 354 384 354 ALA ALA A . n 
A 1 355 THR 355 385 355 THR THR A . n 
A 1 356 PRO 356 386 356 PRO PRO A . n 
A 1 357 LYS 357 387 357 LYS LYS A . n 
A 1 358 GLU 358 388 358 GLU GLU A . n 
A 1 359 MET 359 389 359 MET MET A . n 
A 1 360 VAL 360 390 360 VAL VAL A . n 
A 1 361 ALA 361 391 361 ALA ALA A . n 
A 1 362 ARG 362 392 362 ARG ARG A . n 
A 1 363 ILE 363 393 363 ILE ILE A . n 
A 1 364 PHE 364 394 364 PHE PHE A . n 
A 1 365 GLY 365 395 365 GLY GLY A . n 
A 1 366 ASP 366 396 366 ASP ASP A . n 
A 1 367 ASN 367 397 367 ASN ASN A . n 
A 1 368 GLN 368 398 368 GLN GLN A . n 
A 1 369 PHE 369 399 369 PHE PHE A . n 
A 1 370 ASN 370 400 370 ASN ASN A . n 
A 1 371 ARG 371 401 371 ARG ARG A . n 
A 1 372 GLY 372 402 372 GLY GLY A . n 
A 1 373 VAL 373 403 373 VAL VAL A . n 
A 1 374 SER 374 404 374 SER SER A . n 
A 1 375 ALA 375 405 375 ALA ALA A . n 
A 1 376 PHE 376 406 376 PHE PHE A . n 
A 1 377 SER 377 407 377 SER SER A . n 
A 1 378 GLU 378 408 378 GLU GLU A . n 
A 1 379 ALA 379 409 379 ALA ALA A . n 
A 1 380 LEU 380 410 380 LEU LEU A . n 
A 1 381 VAL 381 411 381 VAL VAL A . n 
A 1 382 ARG 382 412 382 ARG ARG A . n 
A 1 383 GLN 383 413 383 GLN GLN A . n 
A 1 384 GLY 384 414 384 GLY GLY A . n 
A 1 385 ALA 385 415 385 ALA ALA A . n 
A 1 386 PRO 386 416 386 PRO PRO A . n 
A 1 387 VAL 387 417 387 VAL VAL A . n 
A 1 388 TRP 388 418 388 TRP TRP A . n 
A 1 389 ARG 389 419 389 ARG ARG A . n 
A 1 390 TYR 390 420 390 TYR TYR A . n 
A 1 391 GLN 391 421 391 GLN GLN A . n 
A 1 392 PHE 392 422 392 PHE PHE A . n 
A 1 393 ASN 393 423 393 ASN ASN A . n 
A 1 394 GLY 394 424 394 GLY GLY A . n 
A 1 395 ASN 395 425 395 ASN ASN A . n 
A 1 396 THR 396 426 396 THR THR A . n 
A 1 397 GLU 397 427 397 GLU GLU A . n 
A 1 398 GLY 398 428 398 GLY GLY A . n 
A 1 399 GLY 399 429 399 GLY GLY A . n 
A 1 400 ARG 400 430 400 ARG ARG A . n 
A 1 401 ALA 401 431 401 ALA ALA A . n 
A 1 402 PRO 402 432 402 PRO PRO A . n 
A 1 403 ALA 403 433 403 ALA ALA A . n 
A 1 404 THR 404 434 404 THR THR A . n 
A 1 405 HIS 405 435 405 HIS HIS A . n 
A 1 406 GLY 406 436 406 GLY GLY A . n 
A 1 407 ALA 407 437 407 ALA ALA A . n 
A 1 408 GLU 408 438 408 GLU GLU A . n 
A 1 409 ILE 409 439 409 ILE ILE A . n 
A 1 410 PRO 410 440 410 PRO PRO A . n 
A 1 411 TYR 411 441 411 TYR TYR A . n 
A 1 412 VAL 412 442 412 VAL VAL A . n 
A 1 413 PHE 413 443 413 PHE PHE A . n 
A 1 414 GLY 414 444 414 GLY GLY A . n 
A 1 415 VAL 415 445 415 VAL VAL A . n 
A 1 416 PHE 416 446 416 PHE PHE A . n 
A 1 417 LYS 417 447 417 LYS LYS A . n 
A 1 418 LEU 418 448 418 LEU LEU A . n 
A 1 419 ASP 419 449 419 ASP ASP A . n 
A 1 420 GLU 420 450 420 GLU GLU A . n 
A 1 421 LEU 421 451 421 LEU LEU A . n 
A 1 422 GLY 422 452 422 GLY GLY A . n 
A 1 423 LEU 423 453 423 LEU LEU A . n 
A 1 424 PHE 424 454 424 PHE PHE A . n 
A 1 425 ASP 425 455 425 ASP ASP A . n 
A 1 426 TRP 426 456 426 TRP TRP A . n 
A 1 427 PRO 427 457 427 PRO PRO A . n 
A 1 428 PRO 428 458 428 PRO PRO A . n 
A 1 429 GLU 429 459 429 GLU GLU A . n 
A 1 430 GLY 430 460 430 GLY GLY A . n 
A 1 431 PRO 431 461 431 PRO PRO A . n 
A 1 432 THR 432 462 432 THR THR A . n 
A 1 433 PRO 433 463 433 PRO PRO A . n 
A 1 434 ALA 434 464 434 ALA ALA A . n 
A 1 435 ASP 435 465 435 ASP ASP A . n 
A 1 436 ARG 436 466 436 ARG ARG A . n 
A 1 437 ALA 437 467 437 ALA ALA A . n 
A 1 438 LEU 438 468 438 LEU LEU A . n 
A 1 439 GLY 439 469 439 GLY GLY A . n 
A 1 440 GLN 440 470 440 GLN GLN A . n 
A 1 441 LEU 441 471 441 LEU LEU A . n 
A 1 442 MET 442 472 442 MET MET A . n 
A 1 443 SER 443 473 443 SER SER A . n 
A 1 444 SER 444 474 444 SER SER A . n 
A 1 445 ALA 445 475 445 ALA ALA A . n 
A 1 446 TRP 446 476 446 TRP TRP A . n 
A 1 447 VAL 447 477 447 VAL VAL A . n 
A 1 448 ARG 448 478 448 ARG ARG A . n 
A 1 449 PHE 449 479 449 PHE PHE A . n 
A 1 450 ALA 450 480 450 ALA ALA A . n 
A 1 451 LYS 451 481 451 LYS LYS A . n 
A 1 452 ASN 452 482 452 ASN ASN A . n 
A 1 453 GLY 453 483 453 GLY GLY A . n 
A 1 454 ASP 454 484 454 ASP ASP A . n 
A 1 455 PRO 455 485 455 PRO PRO A . n 
A 1 456 ALA 456 486 456 ALA ALA A . n 
A 1 457 GLY 457 487 457 GLY GLY A . n 
A 1 458 ASP 458 488 458 ASP ASP A . n 
A 1 459 ALA 459 489 459 ALA ALA A . n 
A 1 460 LEU 460 490 460 LEU LEU A . n 
A 1 461 THR 461 491 461 THR THR A . n 
A 1 462 TRP 462 492 462 TRP TRP A . n 
A 1 463 PRO 463 493 463 PRO PRO A . n 
A 1 464 ALA 464 494 464 ALA ALA A . n 
A 1 465 TYR 465 495 465 TYR TYR A . n 
A 1 466 SER 466 496 466 SER SER A . n 
A 1 467 THR 467 497 467 THR THR A . n 
A 1 468 GLY 468 498 468 GLY GLY A . n 
A 1 469 LYS 469 499 469 LYS LYS A . n 
A 1 470 SER 470 500 470 SER SER A . n 
A 1 471 THR 471 501 471 THR THR A . n 
A 1 472 MET 472 502 472 MET MET A . n 
A 1 473 THR 473 503 473 THR THR A . n 
A 1 474 PHE 474 504 474 PHE PHE A . n 
A 1 475 GLY 475 505 475 GLY GLY A . n 
A 1 476 PRO 476 506 476 PRO PRO A . n 
A 1 477 GLU 477 507 477 GLU GLU A . n 
A 1 478 GLY 478 508 478 GLY GLY A . n 
A 1 479 ARG 479 509 479 ARG ARG A . n 
A 1 480 ALA 480 510 480 ALA ALA A . n 
A 1 481 ALA 481 511 481 ALA ALA A . n 
A 1 482 VAL 482 512 482 VAL VAL A . n 
A 1 483 VAL 483 513 483 VAL VAL A . n 
A 1 484 SER 484 514 484 SER SER A . n 
A 1 485 PRO 485 515 485 PRO PRO A . n 
A 1 486 GLY 486 516 486 GLY GLY A . n 
A 1 487 PRO 487 517 487 PRO PRO A . n 
A 1 488 SER 488 518 488 SER SER A . n 
A 1 489 ILE 489 519 489 ILE ILE A . n 
A 1 490 PRO 490 520 490 PRO PRO A . n 
A 1 491 PRO 491 521 491 PRO PRO A . n 
A 1 492 CYS 492 522 492 CYS CYS A . n 
A 1 493 ALA 493 523 493 ALA ALA A . n 
A 1 494 ASP 494 524 ?   ?   ?   A . n 
A 1 495 GLY 495 525 ?   ?   ?   A . n 
A 1 496 ALA 496 526 ?   ?   ?   A . n 
A 1 497 LYS 497 527 ?   ?   ?   A . n 
A 1 498 ALA 498 528 ?   ?   ?   A . n 
A 1 499 GLY 499 529 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   601 34  HOH HOH A . 
B 2 HOH 2   602 43  HOH HOH A . 
B 2 HOH 3   603 99  HOH HOH A . 
B 2 HOH 4   604 106 HOH HOH A . 
B 2 HOH 5   605 351 HOH HOH A . 
B 2 HOH 6   606 141 HOH HOH A . 
B 2 HOH 7   607 290 HOH HOH A . 
B 2 HOH 8   608 144 HOH HOH A . 
B 2 HOH 9   609 298 HOH HOH A . 
B 2 HOH 10  610 349 HOH HOH A . 
B 2 HOH 11  611 66  HOH HOH A . 
B 2 HOH 12  612 121 HOH HOH A . 
B 2 HOH 13  613 35  HOH HOH A . 
B 2 HOH 14  614 139 HOH HOH A . 
B 2 HOH 15  615 348 HOH HOH A . 
B 2 HOH 16  616 14  HOH HOH A . 
B 2 HOH 17  617 46  HOH HOH A . 
B 2 HOH 18  618 171 HOH HOH A . 
B 2 HOH 19  619 193 HOH HOH A . 
B 2 HOH 20  620 31  HOH HOH A . 
B 2 HOH 21  621 276 HOH HOH A . 
B 2 HOH 22  622 92  HOH HOH A . 
B 2 HOH 23  623 281 HOH HOH A . 
B 2 HOH 24  624 215 HOH HOH A . 
B 2 HOH 25  625 145 HOH HOH A . 
B 2 HOH 26  626 20  HOH HOH A . 
B 2 HOH 27  627 132 HOH HOH A . 
B 2 HOH 28  628 2   HOH HOH A . 
B 2 HOH 29  629 73  HOH HOH A . 
B 2 HOH 30  630 187 HOH HOH A . 
B 2 HOH 31  631 109 HOH HOH A . 
B 2 HOH 32  632 6   HOH HOH A . 
B 2 HOH 33  633 123 HOH HOH A . 
B 2 HOH 34  634 38  HOH HOH A . 
B 2 HOH 35  635 140 HOH HOH A . 
B 2 HOH 36  636 252 HOH HOH A . 
B 2 HOH 37  637 95  HOH HOH A . 
B 2 HOH 38  638 49  HOH HOH A . 
B 2 HOH 39  639 111 HOH HOH A . 
B 2 HOH 40  640 62  HOH HOH A . 
B 2 HOH 41  641 356 HOH HOH A . 
B 2 HOH 42  642 79  HOH HOH A . 
B 2 HOH 43  643 291 HOH HOH A . 
B 2 HOH 44  644 16  HOH HOH A . 
B 2 HOH 45  645 103 HOH HOH A . 
B 2 HOH 46  646 152 HOH HOH A . 
B 2 HOH 47  647 52  HOH HOH A . 
B 2 HOH 48  648 76  HOH HOH A . 
B 2 HOH 49  649 239 HOH HOH A . 
B 2 HOH 50  650 1   HOH HOH A . 
B 2 HOH 51  651 80  HOH HOH A . 
B 2 HOH 52  652 26  HOH HOH A . 
B 2 HOH 53  653 260 HOH HOH A . 
B 2 HOH 54  654 81  HOH HOH A . 
B 2 HOH 55  655 124 HOH HOH A . 
B 2 HOH 56  656 15  HOH HOH A . 
B 2 HOH 57  657 54  HOH HOH A . 
B 2 HOH 58  658 119 HOH HOH A . 
B 2 HOH 59  659 308 HOH HOH A . 
B 2 HOH 60  660 32  HOH HOH A . 
B 2 HOH 61  661 8   HOH HOH A . 
B 2 HOH 62  662 264 HOH HOH A . 
B 2 HOH 63  663 170 HOH HOH A . 
B 2 HOH 64  664 71  HOH HOH A . 
B 2 HOH 65  665 180 HOH HOH A . 
B 2 HOH 66  666 39  HOH HOH A . 
B 2 HOH 67  667 10  HOH HOH A . 
B 2 HOH 68  668 11  HOH HOH A . 
B 2 HOH 69  669 143 HOH HOH A . 
B 2 HOH 70  670 78  HOH HOH A . 
B 2 HOH 71  671 96  HOH HOH A . 
B 2 HOH 72  672 138 HOH HOH A . 
B 2 HOH 73  673 155 HOH HOH A . 
B 2 HOH 74  674 176 HOH HOH A . 
B 2 HOH 75  675 146 HOH HOH A . 
B 2 HOH 76  676 297 HOH HOH A . 
B 2 HOH 77  677 226 HOH HOH A . 
B 2 HOH 78  678 48  HOH HOH A . 
B 2 HOH 79  679 3   HOH HOH A . 
B 2 HOH 80  680 113 HOH HOH A . 
B 2 HOH 81  681 117 HOH HOH A . 
B 2 HOH 82  682 68  HOH HOH A . 
B 2 HOH 83  683 219 HOH HOH A . 
B 2 HOH 84  684 179 HOH HOH A . 
B 2 HOH 85  685 131 HOH HOH A . 
B 2 HOH 86  686 28  HOH HOH A . 
B 2 HOH 87  687 5   HOH HOH A . 
B 2 HOH 88  688 247 HOH HOH A . 
B 2 HOH 89  689 17  HOH HOH A . 
B 2 HOH 90  690 101 HOH HOH A . 
B 2 HOH 91  691 129 HOH HOH A . 
B 2 HOH 92  692 202 HOH HOH A . 
B 2 HOH 93  693 222 HOH HOH A . 
B 2 HOH 94  694 58  HOH HOH A . 
B 2 HOH 95  695 159 HOH HOH A . 
B 2 HOH 96  696 74  HOH HOH A . 
B 2 HOH 97  697 279 HOH HOH A . 
B 2 HOH 98  698 55  HOH HOH A . 
B 2 HOH 99  699 23  HOH HOH A . 
B 2 HOH 100 700 205 HOH HOH A . 
B 2 HOH 101 701 255 HOH HOH A . 
B 2 HOH 102 702 167 HOH HOH A . 
B 2 HOH 103 703 149 HOH HOH A . 
B 2 HOH 104 704 69  HOH HOH A . 
B 2 HOH 105 705 116 HOH HOH A . 
B 2 HOH 106 706 56  HOH HOH A . 
B 2 HOH 107 707 18  HOH HOH A . 
B 2 HOH 108 708 33  HOH HOH A . 
B 2 HOH 109 709 221 HOH HOH A . 
B 2 HOH 110 710 45  HOH HOH A . 
B 2 HOH 111 711 64  HOH HOH A . 
B 2 HOH 112 712 120 HOH HOH A . 
B 2 HOH 113 713 185 HOH HOH A . 
B 2 HOH 114 714 9   HOH HOH A . 
B 2 HOH 115 715 44  HOH HOH A . 
B 2 HOH 116 716 191 HOH HOH A . 
B 2 HOH 117 717 4   HOH HOH A . 
B 2 HOH 118 718 186 HOH HOH A . 
B 2 HOH 119 719 361 HOH HOH A . 
B 2 HOH 120 720 100 HOH HOH A . 
B 2 HOH 121 721 282 HOH HOH A . 
B 2 HOH 122 722 172 HOH HOH A . 
B 2 HOH 123 723 241 HOH HOH A . 
B 2 HOH 124 724 225 HOH HOH A . 
B 2 HOH 125 725 165 HOH HOH A . 
B 2 HOH 126 726 105 HOH HOH A . 
B 2 HOH 127 727 166 HOH HOH A . 
B 2 HOH 128 728 60  HOH HOH A . 
B 2 HOH 129 729 269 HOH HOH A . 
B 2 HOH 130 730 114 HOH HOH A . 
B 2 HOH 131 731 104 HOH HOH A . 
B 2 HOH 132 732 40  HOH HOH A . 
B 2 HOH 133 733 211 HOH HOH A . 
B 2 HOH 134 734 50  HOH HOH A . 
B 2 HOH 135 735 301 HOH HOH A . 
B 2 HOH 136 736 234 HOH HOH A . 
B 2 HOH 137 737 151 HOH HOH A . 
B 2 HOH 138 738 19  HOH HOH A . 
B 2 HOH 139 739 204 HOH HOH A . 
B 2 HOH 140 740 125 HOH HOH A . 
B 2 HOH 141 741 175 HOH HOH A . 
B 2 HOH 142 742 184 HOH HOH A . 
B 2 HOH 143 743 262 HOH HOH A . 
B 2 HOH 144 744 135 HOH HOH A . 
B 2 HOH 145 745 127 HOH HOH A . 
B 2 HOH 146 746 162 HOH HOH A . 
B 2 HOH 147 747 200 HOH HOH A . 
B 2 HOH 148 748 70  HOH HOH A . 
B 2 HOH 149 749 85  HOH HOH A . 
B 2 HOH 150 750 24  HOH HOH A . 
B 2 HOH 151 751 86  HOH HOH A . 
B 2 HOH 152 752 29  HOH HOH A . 
B 2 HOH 153 753 102 HOH HOH A . 
B 2 HOH 154 754 153 HOH HOH A . 
B 2 HOH 155 755 59  HOH HOH A . 
B 2 HOH 156 756 21  HOH HOH A . 
B 2 HOH 157 757 212 HOH HOH A . 
B 2 HOH 158 758 22  HOH HOH A . 
B 2 HOH 159 759 25  HOH HOH A . 
B 2 HOH 160 760 42  HOH HOH A . 
B 2 HOH 161 761 72  HOH HOH A . 
B 2 HOH 162 762 258 HOH HOH A . 
B 2 HOH 163 763 94  HOH HOH A . 
B 2 HOH 164 764 13  HOH HOH A . 
B 2 HOH 165 765 41  HOH HOH A . 
B 2 HOH 166 766 253 HOH HOH A . 
B 2 HOH 167 767 220 HOH HOH A . 
B 2 HOH 168 768 154 HOH HOH A . 
B 2 HOH 169 769 134 HOH HOH A . 
B 2 HOH 170 770 271 HOH HOH A . 
B 2 HOH 171 771 360 HOH HOH A . 
B 2 HOH 172 772 259 HOH HOH A . 
B 2 HOH 173 773 148 HOH HOH A . 
B 2 HOH 174 774 108 HOH HOH A . 
B 2 HOH 175 775 136 HOH HOH A . 
B 2 HOH 176 776 36  HOH HOH A . 
B 2 HOH 177 777 243 HOH HOH A . 
B 2 HOH 178 778 245 HOH HOH A . 
B 2 HOH 179 779 201 HOH HOH A . 
B 2 HOH 180 780 230 HOH HOH A . 
B 2 HOH 181 781 7   HOH HOH A . 
B 2 HOH 182 782 164 HOH HOH A . 
B 2 HOH 183 783 310 HOH HOH A . 
B 2 HOH 184 784 270 HOH HOH A . 
B 2 HOH 185 785 91  HOH HOH A . 
B 2 HOH 186 786 97  HOH HOH A . 
B 2 HOH 187 787 288 HOH HOH A . 
B 2 HOH 188 788 195 HOH HOH A . 
B 2 HOH 189 789 53  HOH HOH A . 
B 2 HOH 190 790 267 HOH HOH A . 
B 2 HOH 191 791 61  HOH HOH A . 
B 2 HOH 192 792 67  HOH HOH A . 
B 2 HOH 193 793 30  HOH HOH A . 
B 2 HOH 194 794 246 HOH HOH A . 
B 2 HOH 195 795 197 HOH HOH A . 
B 2 HOH 196 796 268 HOH HOH A . 
B 2 HOH 197 797 77  HOH HOH A . 
B 2 HOH 198 798 266 HOH HOH A . 
B 2 HOH 199 799 353 HOH HOH A . 
B 2 HOH 200 800 173 HOH HOH A . 
B 2 HOH 201 801 313 HOH HOH A . 
B 2 HOH 202 802 142 HOH HOH A . 
B 2 HOH 203 803 363 HOH HOH A . 
B 2 HOH 204 804 367 HOH HOH A . 
B 2 HOH 205 805 249 HOH HOH A . 
B 2 HOH 206 806 93  HOH HOH A . 
B 2 HOH 207 807 190 HOH HOH A . 
B 2 HOH 208 808 158 HOH HOH A . 
B 2 HOH 209 809 181 HOH HOH A . 
B 2 HOH 210 810 65  HOH HOH A . 
B 2 HOH 211 811 284 HOH HOH A . 
B 2 HOH 212 812 147 HOH HOH A . 
B 2 HOH 213 813 128 HOH HOH A . 
B 2 HOH 214 814 82  HOH HOH A . 
B 2 HOH 215 815 57  HOH HOH A . 
B 2 HOH 216 816 37  HOH HOH A . 
B 2 HOH 217 817 169 HOH HOH A . 
B 2 HOH 218 818 83  HOH HOH A . 
B 2 HOH 219 819 261 HOH HOH A . 
B 2 HOH 220 820 118 HOH HOH A . 
B 2 HOH 221 821 110 HOH HOH A . 
B 2 HOH 222 822 163 HOH HOH A . 
B 2 HOH 223 823 235 HOH HOH A . 
B 2 HOH 224 824 27  HOH HOH A . 
B 2 HOH 225 825 213 HOH HOH A . 
B 2 HOH 226 826 130 HOH HOH A . 
B 2 HOH 227 827 161 HOH HOH A . 
B 2 HOH 228 828 228 HOH HOH A . 
B 2 HOH 229 829 122 HOH HOH A . 
B 2 HOH 230 830 194 HOH HOH A . 
B 2 HOH 231 831 314 HOH HOH A . 
B 2 HOH 232 832 244 HOH HOH A . 
B 2 HOH 233 833 251 HOH HOH A . 
B 2 HOH 234 834 156 HOH HOH A . 
B 2 HOH 235 835 240 HOH HOH A . 
B 2 HOH 236 836 280 HOH HOH A . 
B 2 HOH 237 837 256 HOH HOH A . 
B 2 HOH 238 838 115 HOH HOH A . 
B 2 HOH 239 839 160 HOH HOH A . 
B 2 HOH 240 840 188 HOH HOH A . 
B 2 HOH 241 841 357 HOH HOH A . 
B 2 HOH 242 842 238 HOH HOH A . 
B 2 HOH 243 843 89  HOH HOH A . 
B 2 HOH 244 844 265 HOH HOH A . 
B 2 HOH 245 845 209 HOH HOH A . 
B 2 HOH 246 846 214 HOH HOH A . 
B 2 HOH 247 847 137 HOH HOH A . 
B 2 HOH 248 848 63  HOH HOH A . 
B 2 HOH 249 849 216 HOH HOH A . 
B 2 HOH 250 850 177 HOH HOH A . 
B 2 HOH 251 851 250 HOH HOH A . 
B 2 HOH 252 852 299 HOH HOH A . 
B 2 HOH 253 853 218 HOH HOH A . 
B 2 HOH 254 854 12  HOH HOH A . 
B 2 HOH 255 855 272 HOH HOH A . 
B 2 HOH 256 856 300 HOH HOH A . 
B 2 HOH 257 857 98  HOH HOH A . 
B 2 HOH 258 858 51  HOH HOH A . 
B 2 HOH 259 859 112 HOH HOH A . 
B 2 HOH 260 860 306 HOH HOH A . 
B 2 HOH 261 861 47  HOH HOH A . 
B 2 HOH 262 862 358 HOH HOH A . 
B 2 HOH 263 863 293 HOH HOH A . 
B 2 HOH 264 864 303 HOH HOH A . 
B 2 HOH 265 865 263 HOH HOH A . 
B 2 HOH 266 866 350 HOH HOH A . 
B 2 HOH 267 867 150 HOH HOH A . 
B 2 HOH 268 868 289 HOH HOH A . 
B 2 HOH 269 869 210 HOH HOH A . 
B 2 HOH 270 870 233 HOH HOH A . 
B 2 HOH 271 871 203 HOH HOH A . 
B 2 HOH 272 872 178 HOH HOH A . 
B 2 HOH 273 873 242 HOH HOH A . 
B 2 HOH 274 874 237 HOH HOH A . 
B 2 HOH 275 875 224 HOH HOH A . 
B 2 HOH 276 876 352 HOH HOH A . 
B 2 HOH 277 877 277 HOH HOH A . 
B 2 HOH 278 878 312 HOH HOH A . 
B 2 HOH 279 879 88  HOH HOH A . 
B 2 HOH 280 880 217 HOH HOH A . 
B 2 HOH 281 881 365 HOH HOH A . 
B 2 HOH 282 882 254 HOH HOH A . 
B 2 HOH 283 883 87  HOH HOH A . 
B 2 HOH 284 884 317 HOH HOH A . 
B 2 HOH 285 885 257 HOH HOH A . 
B 2 HOH 286 886 285 HOH HOH A . 
B 2 HOH 287 887 364 HOH HOH A . 
B 2 HOH 288 888 362 HOH HOH A . 
B 2 HOH 289 889 305 HOH HOH A . 
B 2 HOH 290 890 294 HOH HOH A . 
B 2 HOH 291 891 278 HOH HOH A . 
B 2 HOH 292 892 107 HOH HOH A . 
B 2 HOH 293 893 208 HOH HOH A . 
B 2 HOH 294 894 192 HOH HOH A . 
B 2 HOH 295 895 359 HOH HOH A . 
B 2 HOH 296 896 168 HOH HOH A . 
B 2 HOH 297 897 183 HOH HOH A . 
B 2 HOH 298 898 316 HOH HOH A . 
B 2 HOH 299 899 309 HOH HOH A . 
B 2 HOH 300 900 199 HOH HOH A . 
B 2 HOH 301 901 206 HOH HOH A . 
B 2 HOH 302 902 182 HOH HOH A . 
B 2 HOH 303 903 232 HOH HOH A . 
B 2 HOH 304 904 274 HOH HOH A . 
B 2 HOH 305 905 227 HOH HOH A . 
B 2 HOH 306 906 248 HOH HOH A . 
B 2 HOH 307 907 90  HOH HOH A . 
B 2 HOH 308 908 273 HOH HOH A . 
B 2 HOH 309 909 207 HOH HOH A . 
B 2 HOH 310 910 296 HOH HOH A . 
B 2 HOH 311 911 75  HOH HOH A . 
B 2 HOH 312 912 126 HOH HOH A . 
B 2 HOH 313 913 295 HOH HOH A . 
B 2 HOH 314 914 231 HOH HOH A . 
B 2 HOH 315 915 292 HOH HOH A . 
B 2 HOH 316 916 189 HOH HOH A . 
B 2 HOH 317 917 229 HOH HOH A . 
B 2 HOH 318 918 133 HOH HOH A . 
B 2 HOH 319 919 223 HOH HOH A . 
B 2 HOH 320 920 236 HOH HOH A . 
B 2 HOH 321 921 198 HOH HOH A . 
B 2 HOH 322 922 157 HOH HOH A . 
B 2 HOH 323 923 315 HOH HOH A . 
B 2 HOH 324 924 196 HOH HOH A . 
B 2 HOH 325 925 286 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ARG 303 ? CG  ? A ARG 273 CG  
2 1 Y 1 A ARG 303 ? CD  ? A ARG 273 CD  
3 1 Y 1 A ARG 303 ? NE  ? A ARG 273 NE  
4 1 Y 1 A ARG 303 ? CZ  ? A ARG 273 CZ  
5 1 Y 1 A ARG 303 ? NH1 ? A ARG 273 NH1 
6 1 Y 1 A ARG 303 ? NH2 ? A ARG 273 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? 'VERSION Jun 30, 2023 BUILT=20230630' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '1.0.5 (20230726)'                    2 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)'                  3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S6D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.308 
_cell.length_a_esd                 ? 
_cell.length_b                     106.217 
_cell.length_b_esd                 ? 
_cell.length_c                     117.750 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8S6D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8S6D 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.3 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;15 w/v % PEG 6000,
100 mM potassium chloride,
100 mM HEPES
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97628 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97628 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          24.39 
_reflns.entry_id                                       8S6D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.241 
_reflns.d_resolution_low                               53.11 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     24938 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.64 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.83 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.05314 
_reflns.pdbx_Rpim_I_all                                0.03757 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.03757 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.241 
_reflns_shell.d_res_low                                     2.321 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.72 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2246 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.3668 
_reflns_shell.pdbx_Rpim_I_all                               0.2594 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.921 
_reflns_shell.pdbx_CC_star                                  0.979 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.2594 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.51 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8S6D 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.241 
_refine.ls_d_res_low                             53.11 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     24935 
_refine.ls_number_reflns_R_free                  1232 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.64 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1824 
_refine.ls_R_factor_R_free                       0.2109 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1809 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            'Random selection' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.01 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.241 
_refine_hist.d_res_low                        53.11 
_refine_hist.number_atoms_solvent             325 
_refine_hist.number_atoms_total               3921 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3596 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 3698 ? f_bond_d           ? 'Z= 0.223' 
'X-RAY DIFFRACTION' ? 0.596  ? 5048 ? f_angle_d          ? 'Z= 0.307' 
'X-RAY DIFFRACTION' ? 12.688 ? 1324 ? f_dihedral_angle_d ? ?          
'X-RAY DIFFRACTION' ? 0.043  ? 533  ? f_chiral_restr     ? ?          
'X-RAY DIFFRACTION' ? 0.006  ? 682  ? f_plane_restr      ? ?          
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.241 2.33  . . 123 2395 89.00  . . . . 0.2129 . . . . . . . . . . . 0.2418 
'X-RAY DIFFRACTION' 2.33  2.44  . . 140 2709 99.00  . . . . 0.1928 . . . . . . . . . . . 0.2839 
'X-RAY DIFFRACTION' 2.44  2.57  . . 133 2710 100.00 . . . . 0.1962 . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 2.57  2.73  . . 147 2734 100.00 . . . . 0.2009 . . . . . . . . . . . 0.2842 
'X-RAY DIFFRACTION' 2.73  2.94  . . 139 2717 100.00 . . . . 0.2001 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 2.94  3.23  . . 156 2723 100.00 . . . . 0.1949 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 3.23  3.70  . . 122 2264 82.00  . . . . 0.1810 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 3.70  4.66  . . 115 2546 91.00  . . . . 0.1504 . . . . . . . . . . . 0.1686 
'X-RAY DIFFRACTION' 4.66  53.11 . . 157 2896 100.00 . . . . 0.1669 . . . . . . . . . . . 0.1636 
# 
_struct.entry_id                     8S6D 
_struct.title                        'Fumonisin B1 esterase' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8S6D 
_struct_keywords.text            'mycotoxin, esterase, Fumonisin B1, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8S6D 
_struct_ref.pdbx_db_accession          8S6D 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8S6D 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 499 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8S6D 
_struct_ref_seq.db_align_beg                  31 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  529 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       31 
_struct_ref_seq.pdbx_auth_seq_align_end       529 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  19050 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 VAL A 40  ? ARG A 44  ? VAL A 70  ARG A 74  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 70  ? ARG A 74  ? ALA A 100 ARG A 104 5 ? 5  
HELX_P HELX_P3  AA3 MET A 120 ? ASP A 124 ? MET A 150 ASP A 154 5 ? 5  
HELX_P HELX_P4  AA4 GLY A 125 ? ARG A 130 ? GLY A 155 ARG A 160 1 ? 6  
HELX_P HELX_P5  AA5 THR A 142 ? PHE A 147 ? THR A 172 PHE A 177 1 ? 6  
HELX_P HELX_P6  AA6 HIS A 150 ? SER A 157 ? HIS A 180 SER A 187 1 ? 8  
HELX_P HELX_P7  AA7 ASN A 164 ? ALA A 181 ? ASN A 194 ALA A 211 1 ? 18 
HELX_P HELX_P8  AA8 ARG A 182 ? PHE A 184 ? ARG A 212 PHE A 214 5 ? 3  
HELX_P HELX_P9  AA9 SER A 197 ? LEU A 207 ? SER A 227 LEU A 237 1 ? 11 
HELX_P HELX_P10 AB1 THR A 208 ? LYS A 213 ? THR A 238 LYS A 243 5 ? 6  
HELX_P HELX_P11 AB2 THR A 232 ? ASP A 244 ? THR A 262 ASP A 274 1 ? 13 
HELX_P HELX_P12 AB3 ASP A 246 ? SER A 252 ? ASP A 276 SER A 282 1 ? 7  
HELX_P HELX_P13 AB4 ASP A 254 ? ALA A 265 ? ASP A 284 ALA A 295 1 ? 12 
HELX_P HELX_P14 AB5 THR A 290 ? GLY A 298 ? THR A 320 GLY A 328 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 312 ? LEU A 318 ? ASP A 342 LEU A 348 5 ? 7  
HELX_P HELX_P16 AB7 THR A 325 ? GLY A 338 ? THR A 355 GLY A 368 1 ? 14 
HELX_P HELX_P17 AB8 GLN A 340 ? TYR A 348 ? GLN A 370 TYR A 378 1 ? 9  
HELX_P HELX_P18 AB9 THR A 355 ? PHE A 369 ? THR A 385 PHE A 399 1 ? 15 
HELX_P HELX_P19 AC1 PHE A 369 ? GLN A 383 ? PHE A 399 GLN A 413 1 ? 15 
HELX_P HELX_P20 AC2 GLU A 408 ? GLY A 414 ? GLU A 438 GLY A 444 1 ? 7  
HELX_P HELX_P21 AC3 THR A 432 ? GLY A 453 ? THR A 462 GLY A 483 1 ? 22 
# 
_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 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 67  SG ? ? ? 1_555 A CYS 86  SG ? ? A CYS 97  A CYS 116 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf2 disulf ? ? A CYS 347 SG ? ? ? 1_555 A CYS 492 SG ? ? A CYS 377 A CYS 522 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 67  ? CYS A 86  ? CYS A 97  ? 1_555 CYS A 116 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 347 ? CYS A 492 ? CYS A 377 ? 1_555 CYS A 522 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           484 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            514 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    485 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     515 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.51 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 10 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? parallel      
AA2 6 7  ? parallel      
AA2 7 8  ? parallel      
AA2 8 9  ? parallel      
AA2 9 10 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 12  ? THR A 15  ? VAL A 42  THR A 45  
AA1 2  GLY A 18  ? GLN A 21  ? GLY A 48  GLN A 51  
AA1 3  VAL A 57  ? PRO A 59  ? VAL A 87  PRO A 89  
AA2 1  VAL A 27  ? PRO A 34  ? VAL A 57  PRO A 64  
AA2 2  TYR A 88  ? PRO A 94  ? TYR A 118 PRO A 124 
AA2 3  VAL A 134 ? PHE A 138 ? VAL A 164 PHE A 168 
AA2 4  TYR A 102 ? VAL A 108 ? TYR A 132 VAL A 138 
AA2 5  GLY A 186 ? GLU A 196 ? GLY A 216 GLU A 226 
AA2 6  GLY A 218 ? GLU A 222 ? GLY A 248 GLU A 252 
AA2 7  ARG A 304 ? ASN A 310 ? ARG A 334 ASN A 340 
AA2 8  VAL A 387 ? PHE A 392 ? VAL A 417 PHE A 422 
AA2 9  THR A 471 ? PHE A 474 ? THR A 501 PHE A 504 
AA2 10 ALA A 480 ? VAL A 483 ? ALA A 510 VAL A 513 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ARG A 13  ? N ARG A 43  O VAL A 20  ? O VAL A 50  
AA1 2 3  N GLN A 19  ? N GLN A 49  O ARG A 58  ? O ARG A 88  
AA2 1 2  N ILE A 33  ? N ILE A 63  O LEU A 89  ? O LEU A 119 
AA2 2 3  N ASN A 90  ? N ASN A 120 O THR A 137 ? O THR A 167 
AA2 3 4  O VAL A 136 ? O VAL A 166 N TRP A 107 ? N TRP A 137 
AA2 4 5  N VAL A 104 ? N VAL A 134 O THR A 192 ? O THR A 222 
AA2 5 6  N VAL A 193 ? N VAL A 223 O GLY A 218 ? O GLY A 248 
AA2 6 7  N LEU A 221 ? N LEU A 251 O LEU A 306 ? O LEU A 336 
AA2 7 8  N THR A 309 ? N THR A 339 O PHE A 392 ? O PHE A 422 
AA2 8 9  N ARG A 389 ? N ARG A 419 O MET A 472 ? O MET A 502 
AA2 9 10 N THR A 473 ? N THR A 503 O ALA A 481 ? O ALA A 511 
# 
_pdbx_entry_details.entry_id                   8S6D 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ALA A 149 ? ? -81.28  47.14   
2 1 ASN A 173 ? ? 58.01   -150.67 
3 1 SER A 227 ? ? 55.37   -126.60 
4 1 HIS A 315 ? ? -109.57 -64.32  
5 1 PRO A 332 ? ? -78.93  48.66   
6 1 PHE A 399 ? ? -136.94 -56.75  
7 1 THR A 434 ? ? -106.58 -166.64 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 872 ? B HOH . 
2 1 A HOH 922 ? B HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 26.8730 20.7203 35.9096 0.1658 ? 0.0124  ? -0.0084 ? 0.1722 ? -0.0075 ? 0.1650 ? 0.5466 ? -0.0075 
? -0.1691 ? 0.6247 ? -0.1496 ? 0.6004 ? -0.0158 ? 0.0068  ? -0.0374 ? 0.0504  ? 0.0174  ? -0.0056 ? 0.0299  ? 0.0013  ? -0.0051 ? 
2 'X-RAY DIFFRACTION' ? refined 25.7061 36.6879 31.7164 0.1911 ? 0.0188  ? -0.0110 ? 0.2048 ? 0.0279  ? 0.1995 ? 0.3178 ? 0.1647  
? -0.4436 ? 0.4840 ? 0.0188  ? 0.8997 ? 0.0242  ? 0.1024  ? 0.0855  ? 0.0224  ? 0.0662  ? 0.0571  ? -0.1758 ? -0.0780 ? -0.0644 ? 
3 'X-RAY DIFFRACTION' ? refined 20.3298 40.3921 6.9836  0.2205 ? 0.0260  ? -0.0167 ? 0.2318 ? 0.0020  ? 0.2045 ? 0.5248 ? -0.5123 
? 0.5492  ? 1.5900 ? -0.2708 ? 1.1562 ? 0.0956  ? -0.0154 ? 0.0590  ? -0.1921 ? -0.0055 ? 0.2084  ? -0.0051 ? -0.0995 ? -0.0789 ? 
4 'X-RAY DIFFRACTION' ? refined 31.5778 19.5385 12.3266 0.1893 ? -0.0024 ? -0.0048 ? 0.2237 ? -0.0133 ? 0.1672 ? 1.3258 ? 0.0338  
? 0.1677  ? 0.8122 ? 0.2419  ? 0.8290 ? -0.0584 ? 0.2005  ? -0.0094 ? -0.2172 ? 0.0305  ? 0.0321  ? -0.0052 ? -0.0848 ? 0.0113  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 39 through 273 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 274 through 340 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 341 through 398 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 399 through 523 )
;
# 
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 31  ? A MET 1   
2  1 Y 1 A ALA 32  ? A ALA 2   
3  1 Y 1 A GLY 33  ? A GLY 3   
4  1 Y 1 A ALA 34  ? A ALA 4   
5  1 Y 1 A ALA 35  ? A ALA 5   
6  1 Y 1 A THR 36  ? A THR 6   
7  1 Y 1 A ALA 37  ? A ALA 7   
8  1 Y 1 A THR 38  ? A THR 8   
9  1 Y 1 A ASP 524 ? A ASP 494 
10 1 Y 1 A GLY 525 ? A GLY 495 
11 1 Y 1 A ALA 526 ? A ALA 496 
12 1 Y 1 A LYS 527 ? A LYS 497 
13 1 Y 1 A ALA 528 ? A ALA 498 
14 1 Y 1 A GLY 529 ? A GLY 499 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Research Development and Innovation Office (NKFIH)' Hungary TKP2021-EGA-02 1 
'National Research Development and Innovation Office (NKFIH)' Hungary C1341189       2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S6D 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011722 
_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]   0.009415 
_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]   0.008493 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . ASP A 1 9   ? 29.277 -6.817 37.658 1.00 47.72 ? 39  ASP A N   1 
ATOM   2    C CA  . ASP A 1 9   ? 29.457 -5.560 38.378 1.00 44.52 ? 39  ASP A CA  1 
ATOM   3    C C   . ASP A 1 9   ? 28.124 -4.823 38.543 1.00 43.07 ? 39  ASP A C   1 
ATOM   4    O O   . ASP A 1 9   ? 27.422 -4.550 37.568 1.00 43.16 ? 39  ASP A O   1 
ATOM   5    C CB  . ASP A 1 9   ? 30.472 -4.675 37.653 1.00 53.59 ? 39  ASP A CB  1 
ATOM   6    C CG  . ASP A 1 9   ? 31.248 -3.783 38.601 1.00 54.52 ? 39  ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 9   ? 30.609 -2.998 39.329 1.00 50.71 ? 39  ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 9   ? 32.496 -3.878 38.629 1.00 59.30 ? 39  ASP A OD2 1 
ATOM   9    N N   . PHE A 1 10  ? 27.787 -4.503 39.794 1.00 32.71 ? 40  PHE A N   1 
ATOM   10   C CA  . PHE A 1 10  ? 26.513 -3.906 40.159 1.00 27.58 ? 40  PHE A CA  1 
ATOM   11   C C   . PHE A 1 10  ? 26.523 -2.396 39.923 1.00 23.95 ? 40  PHE A C   1 
ATOM   12   O O   . PHE A 1 10  ? 27.570 -1.753 40.015 1.00 24.40 ? 40  PHE A O   1 
ATOM   13   C CB  . PHE A 1 10  ? 26.201 -4.186 41.624 1.00 24.77 ? 40  PHE A CB  1 
ATOM   14   C CG  . PHE A 1 10  ? 26.088 -5.644 41.950 1.00 28.46 ? 40  PHE A CG  1 
ATOM   15   C CD1 . PHE A 1 10  ? 27.217 -6.391 42.234 1.00 30.40 ? 40  PHE A CD1 1 
ATOM   16   C CD2 . PHE A 1 10  ? 24.853 -6.268 41.974 1.00 24.92 ? 40  PHE A CD2 1 
ATOM   17   C CE1 . PHE A 1 10  ? 27.115 -7.735 42.536 1.00 40.38 ? 40  PHE A CE1 1 
ATOM   18   C CE2 . PHE A 1 10  ? 24.745 -7.611 42.277 1.00 28.30 ? 40  PHE A CE2 1 
ATOM   19   C CZ  . PHE A 1 10  ? 25.876 -8.345 42.559 1.00 31.18 ? 40  PHE A CZ  1 
ATOM   20   N N   . PRO A 1 11  ? 25.355 -1.800 39.626 1.00 25.08 ? 41  PRO A N   1 
ATOM   21   C CA  . PRO A 1 11  ? 25.262 -0.350 39.405 1.00 24.49 ? 41  PRO A CA  1 
ATOM   22   C C   . PRO A 1 11  ? 25.236 0.469  40.694 1.00 22.73 ? 41  PRO A C   1 
ATOM   23   O O   . PRO A 1 11  ? 24.370 1.322  40.892 1.00 21.38 ? 41  PRO A O   1 
ATOM   24   C CB  . PRO A 1 11  ? 23.952 -0.212 38.625 1.00 25.90 ? 41  PRO A CB  1 
ATOM   25   C CG  . PRO A 1 11  ? 23.111 -1.326 39.145 1.00 25.04 ? 41  PRO A CG  1 
ATOM   26   C CD  . PRO A 1 11  ? 24.063 -2.474 39.398 1.00 28.56 ? 41  PRO A CD  1 
ATOM   27   N N   . VAL A 1 12  ? 26.198 0.208  41.578 1.00 19.30 ? 42  VAL A N   1 
ATOM   28   C CA  . VAL A 1 12  ? 26.376 0.961  42.813 1.00 21.25 ? 42  VAL A CA  1 
ATOM   29   C C   . VAL A 1 12  ? 27.801 1.495  42.840 1.00 18.77 ? 42  VAL A C   1 
ATOM   30   O O   . VAL A 1 12  ? 28.755 0.742  42.611 1.00 22.21 ? 42  VAL A O   1 
ATOM   31   C CB  . VAL A 1 12  ? 26.083 0.096  44.054 1.00 18.95 ? 42  VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 12  ? 26.432 0.851  45.330 1.00 18.85 ? 42  VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 12  ? 24.627 -0.330 44.068 1.00 20.21 ? 42  VAL A CG2 1 
ATOM   34   N N   . ARG A 1 13  ? 27.946 2.793  43.104 1.00 19.96 ? 43  ARG A N   1 
ATOM   35   C CA  . ARG A 1 13  ? 29.261 3.425  43.099 1.00 21.99 ? 43  ARG A CA  1 
ATOM   36   C C   . ARG A 1 13  ? 29.386 4.390  44.267 1.00 24.11 ? 43  ARG A C   1 
ATOM   37   O O   . ARG A 1 13  ? 28.409 5.004  44.690 1.00 25.65 ? 43  ARG A O   1 
ATOM   38   C CB  . ARG A 1 13  ? 29.523 4.168  41.784 1.00 23.49 ? 43  ARG A CB  1 
ATOM   39   C CG  . ARG A 1 13  ? 29.708 3.252  40.595 1.00 27.93 ? 43  ARG A CG  1 
ATOM   40   C CD  . ARG A 1 13  ? 30.923 2.365  40.791 1.00 27.20 ? 43  ARG A CD  1 
ATOM   41   N NE  . ARG A 1 13  ? 31.154 1.490  39.649 1.00 34.30 ? 43  ARG A NE  1 
ATOM   42   C CZ  . ARG A 1 13  ? 30.703 0.246  39.560 1.00 40.26 ? 43  ARG A CZ  1 
ATOM   43   N NH1 . ARG A 1 13  ? 29.982 -0.297 40.527 1.00 36.04 ? 43  ARG A NH1 1 
ATOM   44   N NH2 . ARG A 1 13  ? 30.987 -0.472 38.478 1.00 42.40 ? 43  ARG A NH2 1 
ATOM   45   N N   . ARG A 1 14  ? 30.607 4.546  44.766 1.00 24.98 ? 44  ARG A N   1 
ATOM   46   C CA  . ARG A 1 14  ? 30.874 5.381  45.931 1.00 22.79 ? 44  ARG A CA  1 
ATOM   47   C C   . ARG A 1 14  ? 31.424 6.728  45.478 1.00 22.84 ? 44  ARG A C   1 
ATOM   48   O O   . ARG A 1 14  ? 32.579 6.818  45.053 1.00 19.60 ? 44  ARG A O   1 
ATOM   49   C CB  . ARG A 1 14  ? 31.855 4.691  46.876 1.00 22.13 ? 44  ARG A CB  1 
ATOM   50   C CG  . ARG A 1 14  ? 32.260 5.556  48.060 1.00 22.99 ? 44  ARG A CG  1 
ATOM   51   C CD  . ARG A 1 14  ? 33.077 4.772  49.074 1.00 23.26 ? 44  ARG A CD  1 
ATOM   52   N NE  . ARG A 1 14  ? 32.370 3.587  49.542 1.00 30.11 ? 44  ARG A NE  1 
ATOM   53   C CZ  . ARG A 1 14  ? 31.473 3.586  50.518 1.00 34.72 ? 44  ARG A CZ  1 
ATOM   54   N NH1 . ARG A 1 14  ? 31.133 4.699  51.148 1.00 33.58 ? 44  ARG A NH1 1 
ATOM   55   N NH2 . ARG A 1 14  ? 30.898 2.439  50.870 1.00 37.10 ? 44  ARG A NH2 1 
ATOM   56   N N   . THR A 1 15  ? 30.598 7.772  45.558 1.00 22.37 ? 45  THR A N   1 
ATOM   57   C CA  . THR A 1 15  ? 31.108 9.123  45.423 1.00 20.18 ? 45  THR A CA  1 
ATOM   58   C C   . THR A 1 15  ? 31.761 9.558  46.733 1.00 20.32 ? 45  THR A C   1 
ATOM   59   O O   . THR A 1 15  ? 31.630 8.902  47.771 1.00 18.52 ? 45  THR A O   1 
ATOM   60   C CB  . THR A 1 15  ? 29.987 10.095 45.050 1.00 24.85 ? 45  THR A CB  1 
ATOM   61   O OG1 . THR A 1 15  ? 29.272 10.483 46.231 1.00 21.14 ? 45  THR A OG1 1 
ATOM   62   C CG2 . THR A 1 15  ? 29.015 9.446  44.072 1.00 19.49 ? 45  THR A CG2 1 
ATOM   63   N N   . ASP A 1 16  ? 32.462 10.693 46.681 1.00 21.13 ? 46  ASP A N   1 
ATOM   64   C CA  . ASP A 1 16  ? 33.091 11.232 47.880 1.00 24.95 ? 46  ASP A CA  1 
ATOM   65   C C   . ASP A 1 16  ? 32.072 11.653 48.926 1.00 27.16 ? 46  ASP A C   1 
ATOM   66   O O   . ASP A 1 16  ? 32.455 11.912 50.072 1.00 27.97 ? 46  ASP A O   1 
ATOM   67   C CB  . ASP A 1 16  ? 33.983 12.419 47.521 1.00 22.50 ? 46  ASP A CB  1 
ATOM   68   C CG  . ASP A 1 16  ? 33.223 13.524 46.817 1.00 28.81 ? 46  ASP A CG  1 
ATOM   69   O OD1 . ASP A 1 16  ? 32.054 13.300 46.432 1.00 30.52 ? 46  ASP A OD1 1 
ATOM   70   O OD2 . ASP A 1 16  ? 33.794 14.617 46.644 1.00 42.01 ? 46  ASP A OD2 1 
ATOM   71   N N   . LEU A 1 17  ? 30.791 11.723 48.568 1.00 20.81 ? 47  LEU A N   1 
ATOM   72   C CA  . LEU A 1 17  ? 29.728 12.012 49.521 1.00 27.11 ? 47  LEU A CA  1 
ATOM   73   C C   . LEU A 1 17  ? 28.940 10.776 49.946 1.00 22.53 ? 47  LEU A C   1 
ATOM   74   O O   . LEU A 1 17  ? 28.051 10.892 50.794 1.00 25.60 ? 47  LEU A O   1 
ATOM   75   C CB  . LEU A 1 17  ? 28.763 13.044 48.935 1.00 27.30 ? 47  LEU A CB  1 
ATOM   76   C CG  . LEU A 1 17  ? 29.347 14.406 48.574 1.00 31.83 ? 47  LEU A CG  1 
ATOM   77   C CD1 . LEU A 1 17  ? 28.383 15.165 47.670 1.00 32.27 ? 47  LEU A CD1 1 
ATOM   78   C CD2 . LEU A 1 17  ? 29.655 15.210 49.829 1.00 31.36 ? 47  LEU A CD2 1 
ATOM   79   N N   . GLY A 1 18  ? 29.238 9.600  49.393 1.00 19.68 ? 48  GLY A N   1 
ATOM   80   C CA  . GLY A 1 18  ? 28.453 8.413  49.701 1.00 20.96 ? 48  GLY A CA  1 
ATOM   81   C C   . GLY A 1 18  ? 28.079 7.582  48.491 1.00 22.84 ? 48  GLY A C   1 
ATOM   82   O O   . GLY A 1 18  ? 28.374 7.972  47.366 1.00 23.29 ? 48  GLY A O   1 
ATOM   83   N N   . GLN A 1 19  ? 27.440 6.438  48.700 1.00 22.99 ? 49  GLN A N   1 
ATOM   84   C CA  . GLN A 1 19  ? 27.144 5.547  47.595 1.00 19.11 ? 49  GLN A CA  1 
ATOM   85   C C   . GLN A 1 19  ? 25.864 5.963  46.885 1.00 22.94 ? 49  GLN A C   1 
ATOM   86   O O   . GLN A 1 19  ? 24.945 6.520  47.487 1.00 23.03 ? 49  GLN A O   1 
ATOM   87   C CB  . GLN A 1 19  ? 27.009 4.107  48.096 1.00 21.99 ? 49  GLN A CB  1 
ATOM   88   C CG  . GLN A 1 19  ? 28.245 3.578  48.796 1.00 23.31 ? 49  GLN A CG  1 
ATOM   89   C CD  . GLN A 1 19  ? 28.091 2.126  49.213 1.00 28.53 ? 49  GLN A CD  1 
ATOM   90   O OE1 . GLN A 1 19  ? 28.308 1.215  48.418 1.00 27.84 ? 49  GLN A OE1 1 
ATOM   91   N NE2 . GLN A 1 19  ? 27.732 1.906  50.473 1.00 36.30 ? 49  GLN A NE2 1 
ATOM   92   N N   . VAL A 1 20  ? 25.807 5.657  45.592 1.00 17.77 ? 50  VAL A N   1 
ATOM   93   C CA  . VAL A 1 20  ? 24.652 5.910  44.746 1.00 18.49 ? 50  VAL A CA  1 
ATOM   94   C C   . VAL A 1 20  ? 24.343 4.650  43.950 1.00 20.37 ? 50  VAL A C   1 
ATOM   95   O O   . VAL A 1 20  ? 25.243 3.884  43.582 1.00 20.93 ? 50  VAL A O   1 
ATOM   96   C CB  . VAL A 1 20  ? 24.883 7.104  43.796 1.00 17.53 ? 50  VAL A CB  1 
ATOM   97   C CG1 . VAL A 1 20  ? 24.967 8.408  44.569 1.00 16.17 ? 50  VAL A CG1 1 
ATOM   98   C CG2 . VAL A 1 20  ? 26.143 6.891  42.959 1.00 17.15 ? 50  VAL A CG2 1 
ATOM   99   N N   . GLN A 1 21  ? 23.053 4.437  43.690 1.00 18.61 ? 51  GLN A N   1 
ATOM   100  C CA  . GLN A 1 21  ? 22.592 3.321  42.868 1.00 19.00 ? 51  GLN A CA  1 
ATOM   101  C C   . GLN A 1 21  ? 22.037 3.842  41.550 1.00 22.45 ? 51  GLN A C   1 
ATOM   102  O O   . GLN A 1 21  ? 21.097 4.643  41.543 1.00 18.73 ? 51  GLN A O   1 
ATOM   103  C CB  . GLN A 1 21  ? 21.519 2.490  43.573 1.00 20.65 ? 51  GLN A CB  1 
ATOM   104  C CG  . GLN A 1 21  ? 20.920 1.428  42.650 1.00 25.82 ? 51  GLN A CG  1 
ATOM   105  C CD  . GLN A 1 21  ? 19.878 0.560  43.319 1.00 28.59 ? 51  GLN A CD  1 
ATOM   106  O OE1 . GLN A 1 21  ? 20.144 -0.592 43.660 1.00 24.92 ? 51  GLN A OE1 1 
ATOM   107  N NE2 . GLN A 1 21  ? 18.677 1.102  43.494 1.00 29.86 ? 51  GLN A NE2 1 
ATOM   108  N N   . GLY A 1 22  ? 22.593 3.362  40.439 1.00 18.01 ? 52  GLY A N   1 
ATOM   109  C CA  . GLY A 1 22  ? 22.078 3.720  39.131 1.00 21.40 ? 52  GLY A CA  1 
ATOM   110  C C   . GLY A 1 22  ? 21.327 2.594  38.444 1.00 21.61 ? 52  GLY A C   1 
ATOM   111  O O   . GLY A 1 22  ? 20.723 1.744  39.106 1.00 22.18 ? 52  GLY A O   1 
ATOM   112  N N   . LEU A 1 23  ? 21.361 2.576  37.115 1.00 21.22 ? 53  LEU A N   1 
ATOM   113  C CA  . LEU A 1 23  ? 20.688 1.563  36.315 1.00 23.24 ? 53  LEU A CA  1 
ATOM   114  C C   . LEU A 1 23  ? 21.717 0.664  35.640 1.00 25.99 ? 53  LEU A C   1 
ATOM   115  O O   . LEU A 1 23  ? 22.713 1.146  35.093 1.00 23.97 ? 53  LEU A O   1 
ATOM   116  C CB  . LEU A 1 23  ? 19.786 2.207  35.260 1.00 22.06 ? 53  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 23  ? 18.617 3.046  35.783 1.00 33.71 ? 53  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 23  ? 18.029 3.906  34.672 1.00 35.35 ? 53  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 23  ? 17.541 2.160  36.397 1.00 25.31 ? 53  LEU A CD2 1 
ATOM   120  N N   . ALA A 1 24  ? 21.463 -0.642 35.672 1.00 23.59 ? 54  ALA A N   1 
ATOM   121  C CA  . ALA A 1 24  ? 22.391 -1.622 35.133 1.00 22.12 ? 54  ALA A CA  1 
ATOM   122  C C   . ALA A 1 24  ? 22.255 -1.722 33.613 1.00 25.95 ? 54  ALA A C   1 
ATOM   123  O O   . ALA A 1 24  ? 21.295 -1.237 33.007 1.00 26.09 ? 54  ALA A O   1 
ATOM   124  C CB  . ALA A 1 24  ? 22.164 -2.985 35.780 1.00 26.34 ? 54  ALA A CB  1 
ATOM   125  N N   . GLY A 1 25  ? 23.228 -2.378 33.006 1.00 31.39 ? 55  GLY A N   1 
ATOM   126  C CA  . GLY A 1 25  ? 23.274 -2.533 31.565 1.00 31.51 ? 55  GLY A CA  1 
ATOM   127  C C   . GLY A 1 25  ? 24.712 -2.598 31.098 1.00 29.76 ? 55  GLY A C   1 
ATOM   128  O O   . GLY A 1 25  ? 25.649 -2.478 31.883 1.00 29.42 ? 55  GLY A O   1 
ATOM   129  N N   . ASP A 1 26  ? 24.870 -2.796 29.783 1.00 30.24 ? 56  ASP A N   1 
ATOM   130  C CA  . ASP A 1 26  ? 26.211 -2.765 29.201 1.00 32.38 ? 56  ASP A CA  1 
ATOM   131  C C   . ASP A 1 26  ? 26.876 -1.414 29.428 1.00 27.28 ? 56  ASP A C   1 
ATOM   132  O O   . ASP A 1 26  ? 28.101 -1.338 29.577 1.00 27.14 ? 56  ASP A O   1 
ATOM   133  C CB  . ASP A 1 26  ? 26.160 -3.091 27.705 1.00 35.29 ? 56  ASP A CB  1 
ATOM   134  C CG  . ASP A 1 26  ? 25.437 -2.029 26.896 1.00 44.05 ? 56  ASP A CG  1 
ATOM   135  O OD1 . ASP A 1 26  ? 24.323 -1.624 27.294 1.00 48.98 ? 56  ASP A OD1 1 
ATOM   136  O OD2 . ASP A 1 26  ? 25.988 -1.589 25.863 1.00 43.30 ? 56  ASP A OD2 1 
ATOM   137  N N   . VAL A 1 27  ? 26.087 -0.346 29.459 1.00 24.44 ? 57  VAL A N   1 
ATOM   138  C CA  . VAL A 1 27  ? 26.516 0.954  29.956 1.00 24.19 ? 57  VAL A CA  1 
ATOM   139  C C   . VAL A 1 27  ? 25.697 1.250  31.203 1.00 27.52 ? 57  VAL A C   1 
ATOM   140  O O   . VAL A 1 27  ? 24.464 1.332  31.140 1.00 25.37 ? 57  VAL A O   1 
ATOM   141  C CB  . VAL A 1 27  ? 26.340 2.057  28.902 1.00 24.46 ? 57  VAL A CB  1 
ATOM   142  C CG1 . VAL A 1 27  ? 26.375 3.432  29.556 1.00 17.87 ? 57  VAL A CG1 1 
ATOM   143  C CG2 . VAL A 1 27  ? 27.425 1.944  27.848 1.00 29.40 ? 57  VAL A CG2 1 
ATOM   144  N N   . MET A 1 28  ? 26.377 1.382  32.338 1.00 24.88 ? 58  MET A N   1 
ATOM   145  C CA  . MET A 1 28  ? 25.711 1.768  33.571 1.00 26.55 ? 58  MET A CA  1 
ATOM   146  C C   . MET A 1 28  ? 25.371 3.251  33.537 1.00 24.66 ? 58  MET A C   1 
ATOM   147  O O   . MET A 1 28  ? 26.181 4.084  33.107 1.00 21.13 ? 58  MET A O   1 
ATOM   148  C CB  . MET A 1 28  ? 26.594 1.461  34.780 1.00 27.26 ? 58  MET A CB  1 
ATOM   149  C CG  . MET A 1 28  ? 26.962 0.001  34.939 1.00 35.97 ? 58  MET A CG  1 
ATOM   150  S SD  . MET A 1 28  ? 27.650 -0.323 36.581 1.00 50.99 ? 58  MET A SD  1 
ATOM   151  C CE  . MET A 1 28  ? 28.720 1.099  36.771 1.00 33.54 ? 58  MET A CE  1 
ATOM   152  N N   . SER A 1 29  ? 24.166 3.575  34.002 1.00 18.46 ? 59  SER A N   1 
ATOM   153  C CA  . SER A 1 29  ? 23.648 4.935  34.006 1.00 17.89 ? 59  SER A CA  1 
ATOM   154  C C   . SER A 1 29  ? 23.290 5.339  35.430 1.00 22.57 ? 59  SER A C   1 
ATOM   155  O O   . SER A 1 29  ? 22.597 4.597  36.135 1.00 24.58 ? 59  SER A O   1 
ATOM   156  C CB  . SER A 1 29  ? 22.424 5.048  33.091 1.00 19.95 ? 59  SER A CB  1 
ATOM   157  O OG  . SER A 1 29  ? 21.830 6.329  33.185 1.00 35.94 ? 59  SER A OG  1 
ATOM   158  N N   . PHE A 1 30  ? 23.770 6.511  35.846 1.00 22.48 ? 60  PHE A N   1 
ATOM   159  C CA  . PHE A 1 30  ? 23.479 7.114  37.138 1.00 20.49 ? 60  PHE A CA  1 
ATOM   160  C C   . PHE A 1 30  ? 22.903 8.500  36.890 1.00 21.52 ? 60  PHE A C   1 
ATOM   161  O O   . PHE A 1 30  ? 23.422 9.244  36.054 1.00 20.03 ? 60  PHE A O   1 
ATOM   162  C CB  . PHE A 1 30  ? 24.743 7.223  38.012 1.00 19.81 ? 60  PHE A CB  1 
ATOM   163  C CG  . PHE A 1 30  ? 25.437 5.912  38.246 1.00 21.97 ? 60  PHE A CG  1 
ATOM   164  C CD1 . PHE A 1 30  ? 26.315 5.396  37.306 1.00 20.34 ? 60  PHE A CD1 1 
ATOM   165  C CD2 . PHE A 1 30  ? 25.218 5.199  39.411 1.00 22.03 ? 60  PHE A CD2 1 
ATOM   166  C CE1 . PHE A 1 30  ? 26.951 4.192  37.520 1.00 20.91 ? 60  PHE A CE1 1 
ATOM   167  C CE2 . PHE A 1 30  ? 25.853 3.991  39.630 1.00 25.32 ? 60  PHE A CE2 1 
ATOM   168  C CZ  . PHE A 1 30  ? 26.723 3.490  38.684 1.00 22.14 ? 60  PHE A CZ  1 
ATOM   169  N N   . ARG A 1 31  ? 21.831 8.847  37.605 1.00 16.49 ? 61  ARG A N   1 
ATOM   170  C CA  . ARG A 1 31  ? 21.118 10.092 37.344 1.00 19.04 ? 61  ARG A CA  1 
ATOM   171  C C   . ARG A 1 31  ? 20.769 10.789 38.648 1.00 17.33 ? 61  ARG A C   1 
ATOM   172  O O   . ARG A 1 31  ? 20.398 10.138 39.626 1.00 18.82 ? 61  ARG A O   1 
ATOM   173  C CB  . ARG A 1 31  ? 19.841 9.839  36.533 1.00 18.91 ? 61  ARG A CB  1 
ATOM   174  C CG  . ARG A 1 31  ? 20.107 9.129  35.221 1.00 20.43 ? 61  ARG A CG  1 
ATOM   175  C CD  . ARG A 1 31  ? 18.842 8.636  34.557 1.00 25.02 ? 61  ARG A CD  1 
ATOM   176  N NE  . ARG A 1 31  ? 19.177 7.750  33.453 1.00 26.35 ? 61  ARG A NE  1 
ATOM   177  C CZ  . ARG A 1 31  ? 18.402 7.534  32.401 1.00 36.81 ? 61  ARG A CZ  1 
ATOM   178  N NH1 . ARG A 1 31  ? 17.202 8.083  32.301 1.00 51.05 ? 61  ARG A NH1 1 
ATOM   179  N NH2 . ARG A 1 31  ? 18.849 6.762  31.416 1.00 31.24 ? 61  ARG A NH2 1 
ATOM   180  N N   . GLY A 1 32  ? 20.884 12.115 38.652 1.00 14.85 ? 62  GLY A N   1 
ATOM   181  C CA  . GLY A 1 32  ? 20.473 12.894 39.800 1.00 15.77 ? 62  GLY A CA  1 
ATOM   182  C C   . GLY A 1 32  ? 21.441 12.900 40.959 1.00 19.23 ? 62  GLY A C   1 
ATOM   183  O O   . GLY A 1 32  ? 21.016 13.032 42.110 1.00 19.16 ? 62  GLY A O   1 
ATOM   184  N N   . ILE A 1 33  ? 22.735 12.762 40.692 1.00 17.88 ? 63  ILE A N   1 
ATOM   185  C CA  . ILE A 1 33  ? 23.743 12.819 41.745 1.00 15.11 ? 63  ILE A CA  1 
ATOM   186  C C   . ILE A 1 33  ? 23.961 14.282 42.105 1.00 17.04 ? 63  ILE A C   1 
ATOM   187  O O   . ILE A 1 33  ? 24.257 15.096 41.218 1.00 19.13 ? 63  ILE A O   1 
ATOM   188  C CB  . ILE A 1 33  ? 25.057 12.157 41.304 1.00 19.64 ? 63  ILE A CB  1 
ATOM   189  C CG1 . ILE A 1 33  ? 24.813 10.706 40.887 1.00 16.50 ? 63  ILE A CG1 1 
ATOM   190  C CG2 . ILE A 1 33  ? 26.094 12.236 42.417 1.00 15.53 ? 63  ILE A CG2 1 
ATOM   191  C CD1 . ILE A 1 33  ? 26.065 9.991  40.422 1.00 17.64 ? 63  ILE A CD1 1 
ATOM   192  N N   . PRO A 1 34  ? 23.804 14.671 43.367 1.00 16.56 ? 64  PRO A N   1 
ATOM   193  C CA  . PRO A 1 34  ? 24.132 16.048 43.748 1.00 16.13 ? 64  PRO A CA  1 
ATOM   194  C C   . PRO A 1 34  ? 25.633 16.285 43.667 1.00 18.50 ? 64  PRO A C   1 
ATOM   195  O O   . PRO A 1 34  ? 26.442 15.426 44.032 1.00 18.00 ? 64  PRO A O   1 
ATOM   196  C CB  . PRO A 1 34  ? 23.617 16.155 45.188 1.00 19.76 ? 64  PRO A CB  1 
ATOM   197  C CG  . PRO A 1 34  ? 23.603 14.749 45.692 1.00 22.50 ? 64  PRO A CG  1 
ATOM   198  C CD  . PRO A 1 34  ? 23.287 13.885 44.501 1.00 18.53 ? 64  PRO A CD  1 
ATOM   199  N N   . TYR A 1 35  ? 26.004 17.458 43.157 1.00 17.91 ? 65  TYR A N   1 
ATOM   200  C CA  . TYR A 1 35  ? 27.399 17.869 43.156 1.00 22.69 ? 65  TYR A CA  1 
ATOM   201  C C   . TYR A 1 35  ? 27.633 19.148 43.947 1.00 19.36 ? 65  TYR A C   1 
ATOM   202  O O   . TYR A 1 35  ? 28.776 19.618 44.024 1.00 19.02 ? 65  TYR A O   1 
ATOM   203  C CB  . TYR A 1 35  ? 27.921 18.021 41.718 1.00 19.55 ? 65  TYR A CB  1 
ATOM   204  C CG  . TYR A 1 35  ? 27.367 19.172 40.911 1.00 16.22 ? 65  TYR A CG  1 
ATOM   205  C CD1 . TYR A 1 35  ? 26.231 19.017 40.121 1.00 16.36 ? 65  TYR A CD1 1 
ATOM   206  C CD2 . TYR A 1 35  ? 28.003 20.409 40.908 1.00 17.26 ? 65  TYR A CD2 1 
ATOM   207  C CE1 . TYR A 1 35  ? 25.729 20.075 39.365 1.00 13.52 ? 65  TYR A CE1 1 
ATOM   208  C CE2 . TYR A 1 35  ? 27.511 21.471 40.160 1.00 16.12 ? 65  TYR A CE2 1 
ATOM   209  C CZ  . TYR A 1 35  ? 26.378 21.297 39.391 1.00 17.30 ? 65  TYR A CZ  1 
ATOM   210  O OH  . TYR A 1 35  ? 25.901 22.352 38.652 1.00 13.35 ? 65  TYR A OH  1 
ATOM   211  N N   . ALA A 1 36  ? 26.591 19.704 44.560 1.00 17.94 ? 66  ALA A N   1 
ATOM   212  C CA  . ALA A 1 36  ? 26.710 20.888 45.400 1.00 15.16 ? 66  ALA A CA  1 
ATOM   213  C C   . ALA A 1 36  ? 25.491 20.964 46.306 1.00 21.37 ? 66  ALA A C   1 
ATOM   214  O O   . ALA A 1 36  ? 24.470 20.316 46.053 1.00 18.60 ? 66  ALA A O   1 
ATOM   215  C CB  . ALA A 1 36  ? 26.846 22.164 44.556 1.00 14.24 ? 66  ALA A CB  1 
ATOM   216  N N   . ALA A 1 37  ? 25.610 21.763 47.365 1.00 18.25 ? 67  ALA A N   1 
ATOM   217  C CA  . ALA A 1 37  ? 24.466 21.984 48.238 1.00 20.88 ? 67  ALA A CA  1 
ATOM   218  C C   . ALA A 1 37  ? 23.372 22.721 47.465 1.00 18.83 ? 67  ALA A C   1 
ATOM   219  O O   . ALA A 1 37  ? 23.676 23.539 46.586 1.00 16.61 ? 67  ALA A O   1 
ATOM   220  C CB  . ALA A 1 37  ? 24.878 22.787 49.476 1.00 18.53 ? 67  ALA A CB  1 
ATOM   221  N N   . PRO A 1 38  ? 22.098 22.457 47.750 1.00 19.67 ? 68  PRO A N   1 
ATOM   222  C CA  . PRO A 1 38  ? 21.021 23.155 47.046 1.00 18.88 ? 68  PRO A CA  1 
ATOM   223  C C   . PRO A 1 38  ? 21.135 24.658 47.224 1.00 18.67 ? 68  PRO A C   1 
ATOM   224  O O   . PRO A 1 38  ? 21.141 25.158 48.357 1.00 15.95 ? 68  PRO A O   1 
ATOM   225  C CB  . PRO A 1 38  ? 19.753 22.604 47.712 1.00 20.40 ? 68  PRO A CB  1 
ATOM   226  C CG  . PRO A 1 38  ? 20.144 21.249 48.189 1.00 18.43 ? 68  PRO A CG  1 
ATOM   227  C CD  . PRO A 1 38  ? 21.585 21.386 48.622 1.00 19.25 ? 68  PRO A CD  1 
ATOM   228  N N   . PRO A 1 39  ? 21.247 25.414 46.129 1.00 17.31 ? 69  PRO A N   1 
ATOM   229  C CA  . PRO A 1 39  ? 21.422 26.873 46.233 1.00 14.94 ? 69  PRO A CA  1 
ATOM   230  C C   . PRO A 1 39  ? 20.105 27.600 46.495 1.00 17.48 ? 69  PRO A C   1 
ATOM   231  O O   . PRO A 1 39  ? 19.642 28.420 45.695 1.00 18.20 ? 69  PRO A O   1 
ATOM   232  C CB  . PRO A 1 39  ? 22.033 27.222 44.869 1.00 18.43 ? 69  PRO A CB  1 
ATOM   233  C CG  . PRO A 1 39  ? 21.416 26.232 43.930 1.00 15.98 ? 69  PRO A CG  1 
ATOM   234  C CD  . PRO A 1 39  ? 21.251 24.954 44.727 1.00 14.45 ? 69  PRO A CD  1 
ATOM   235  N N   . VAL A 1 40  ? 19.491 27.302 47.642 1.00 19.47 ? 70  VAL A N   1 
ATOM   236  C CA  . VAL A 1 40  ? 18.178 27.827 47.991 1.00 21.75 ? 70  VAL A CA  1 
ATOM   237  C C   . VAL A 1 40  ? 18.293 28.707 49.232 1.00 16.14 ? 70  VAL A C   1 
ATOM   238  O O   . VAL A 1 40  ? 19.241 28.607 50.016 1.00 18.44 ? 70  VAL A O   1 
ATOM   239  C CB  . VAL A 1 40  ? 17.150 26.702 48.225 1.00 21.86 ? 70  VAL A CB  1 
ATOM   240  C CG1 . VAL A 1 40  ? 17.051 25.802 47.002 1.00 15.48 ? 70  VAL A CG1 1 
ATOM   241  C CG2 . VAL A 1 40  ? 17.527 25.898 49.459 1.00 18.66 ? 70  VAL A CG2 1 
ATOM   242  N N   . GLY A 1 41  ? 17.303 29.577 49.399 1.00 18.97 ? 71  GLY A N   1 
ATOM   243  C CA  . GLY A 1 41  ? 17.273 30.461 50.554 1.00 16.90 ? 71  GLY A CA  1 
ATOM   244  C C   . GLY A 1 41  ? 18.483 31.371 50.579 1.00 16.90 ? 71  GLY A C   1 
ATOM   245  O O   . GLY A 1 41  ? 18.744 32.126 49.634 1.00 16.71 ? 71  GLY A O   1 
ATOM   246  N N   . GLY A 1 42  ? 19.246 31.300 51.672 1.00 23.04 ? 72  GLY A N   1 
ATOM   247  C CA  . GLY A 1 42  ? 20.440 32.116 51.808 1.00 17.25 ? 72  GLY A CA  1 
ATOM   248  C C   . GLY A 1 42  ? 21.527 31.798 50.802 1.00 18.56 ? 72  GLY A C   1 
ATOM   249  O O   . GLY A 1 42  ? 22.421 32.624 50.595 1.00 22.72 ? 72  GLY A O   1 
ATOM   250  N N   . LEU A 1 43  ? 21.469 30.624 50.172 1.00 18.16 ? 73  LEU A N   1 
ATOM   251  C CA  . LEU A 1 43  ? 22.459 30.213 49.184 1.00 15.97 ? 73  LEU A CA  1 
ATOM   252  C C   . LEU A 1 43  ? 22.074 30.589 47.757 1.00 20.13 ? 73  LEU A C   1 
ATOM   253  O O   . LEU A 1 43  ? 22.850 30.324 46.831 1.00 15.67 ? 73  LEU A O   1 
ATOM   254  C CB  . LEU A 1 43  ? 22.698 28.702 49.270 1.00 15.79 ? 73  LEU A CB  1 
ATOM   255  C CG  . LEU A 1 43  ? 23.282 28.161 50.580 1.00 20.82 ? 73  LEU A CG  1 
ATOM   256  C CD1 . LEU A 1 43  ? 23.639 26.683 50.450 1.00 15.92 ? 73  LEU A CD1 1 
ATOM   257  C CD2 . LEU A 1 43  ? 24.496 28.971 51.010 1.00 18.17 ? 73  LEU A CD2 1 
ATOM   258  N N   . ARG A 1 44  ? 20.897 31.176 47.548 1.00 16.51 ? 74  ARG A N   1 
ATOM   259  C CA  . ARG A 1 44  ? 20.612 31.774 46.252 1.00 18.42 ? 74  ARG A CA  1 
ATOM   260  C C   . ARG A 1 44  ? 21.577 32.929 46.010 1.00 16.03 ? 74  ARG A C   1 
ATOM   261  O O   . ARG A 1 44  ? 21.837 33.738 46.905 1.00 16.29 ? 74  ARG A O   1 
ATOM   262  C CB  . ARG A 1 44  ? 19.162 32.266 46.186 1.00 16.73 ? 74  ARG A CB  1 
ATOM   263  C CG  . ARG A 1 44  ? 18.814 32.990 44.888 1.00 17.14 ? 74  ARG A CG  1 
ATOM   264  C CD  . ARG A 1 44  ? 17.491 33.747 44.989 1.00 20.86 ? 74  ARG A CD  1 
ATOM   265  N NE  . ARG A 1 44  ? 16.328 32.872 44.893 1.00 16.69 ? 74  ARG A NE  1 
ATOM   266  C CZ  . ARG A 1 44  ? 15.073 33.283 45.014 1.00 20.59 ? 74  ARG A CZ  1 
ATOM   267  N NH1 . ARG A 1 44  ? 14.780 34.552 45.246 1.00 19.59 ? 74  ARG A NH1 1 
ATOM   268  N NH2 . ARG A 1 44  ? 14.085 32.398 44.898 1.00 18.08 ? 74  ARG A NH2 1 
ATOM   269  N N   . TRP A 1 45  ? 22.117 32.989 44.791 1.00 15.29 ? 75  TRP A N   1 
ATOM   270  C CA  . TRP A 1 45  ? 23.091 34.004 44.389 1.00 15.35 ? 75  TRP A CA  1 
ATOM   271  C C   . TRP A 1 45  ? 24.360 33.943 45.239 1.00 17.30 ? 75  TRP A C   1 
ATOM   272  O O   . TRP A 1 45  ? 25.006 34.967 45.495 1.00 18.59 ? 75  TRP A O   1 
ATOM   273  C CB  . TRP A 1 45  ? 22.486 35.411 44.420 1.00 15.69 ? 75  TRP A CB  1 
ATOM   274  C CG  . TRP A 1 45  ? 21.342 35.613 43.468 1.00 15.61 ? 75  TRP A CG  1 
ATOM   275  C CD1 . TRP A 1 45  ? 21.303 35.279 42.139 1.00 15.32 ? 75  TRP A CD1 1 
ATOM   276  C CD2 . TRP A 1 45  ? 20.083 36.224 43.765 1.00 15.93 ? 75  TRP A CD2 1 
ATOM   277  N NE1 . TRP A 1 45  ? 20.090 35.636 41.598 1.00 15.39 ? 75  TRP A NE1 1 
ATOM   278  C CE2 . TRP A 1 45  ? 19.323 36.217 42.575 1.00 16.96 ? 75  TRP A CE2 1 
ATOM   279  C CE3 . TRP A 1 45  ? 19.520 36.770 44.924 1.00 16.38 ? 75  TRP A CE3 1 
ATOM   280  C CZ2 . TRP A 1 45  ? 18.033 36.735 42.512 1.00 16.07 ? 75  TRP A CZ2 1 
ATOM   281  C CZ3 . TRP A 1 45  ? 18.240 37.281 44.861 1.00 16.65 ? 75  TRP A CZ3 1 
ATOM   282  C CH2 . TRP A 1 45  ? 17.510 37.263 43.661 1.00 17.65 ? 75  TRP A CH2 1 
ATOM   283  N N   . LYS A 1 46  ? 24.709 32.749 45.699 1.00 15.37 ? 76  LYS A N   1 
ATOM   284  C CA  . LYS A 1 46  ? 26.005 32.463 46.283 1.00 15.47 ? 76  LYS A CA  1 
ATOM   285  C C   . LYS A 1 46  ? 26.720 31.449 45.403 1.00 15.10 ? 76  LYS A C   1 
ATOM   286  O O   . LYS A 1 46  ? 26.073 30.682 44.680 1.00 14.80 ? 76  LYS A O   1 
ATOM   287  C CB  . LYS A 1 46  ? 25.876 31.898 47.704 1.00 16.55 ? 76  LYS A CB  1 
ATOM   288  C CG  . LYS A 1 46  ? 25.665 32.937 48.797 1.00 21.56 ? 76  LYS A CG  1 
ATOM   289  C CD  . LYS A 1 46  ? 26.081 32.361 50.138 1.00 21.39 ? 76  LYS A CD  1 
ATOM   290  C CE  . LYS A 1 46  ? 25.479 33.123 51.309 1.00 27.27 ? 76  LYS A CE  1 
ATOM   291  N NZ  . LYS A 1 46  ? 25.821 34.567 51.284 1.00 34.29 ? 76  LYS A NZ  1 
ATOM   292  N N   . PRO A 1 47  ? 28.049 31.426 45.427 1.00 17.50 ? 77  PRO A N   1 
ATOM   293  C CA  . PRO A 1 47  ? 28.783 30.334 44.790 1.00 15.88 ? 77  PRO A CA  1 
ATOM   294  C C   . PRO A 1 47  ? 28.264 28.994 45.275 1.00 16.43 ? 77  PRO A C   1 
ATOM   295  O O   . PRO A 1 47  ? 27.758 28.886 46.404 1.00 15.04 ? 77  PRO A O   1 
ATOM   296  C CB  . PRO A 1 47  ? 30.230 30.573 45.248 1.00 15.17 ? 77  PRO A CB  1 
ATOM   297  C CG  . PRO A 1 47  ? 30.307 32.042 45.452 1.00 20.06 ? 77  PRO A CG  1 
ATOM   298  C CD  . PRO A 1 47  ? 28.954 32.446 45.986 1.00 16.80 ? 77  PRO A CD  1 
ATOM   299  N N   . PRO A 1 48  ? 28.349 27.956 44.448 1.00 16.00 ? 78  PRO A N   1 
ATOM   300  C CA  . PRO A 1 48  ? 27.907 26.632 44.896 1.00 14.48 ? 78  PRO A CA  1 
ATOM   301  C C   . PRO A 1 48  ? 28.761 26.145 46.057 1.00 15.77 ? 78  PRO A C   1 
ATOM   302  O O   . PRO A 1 48  ? 29.985 26.286 46.051 1.00 19.64 ? 78  PRO A O   1 
ATOM   303  C CB  . PRO A 1 48  ? 28.090 25.759 43.651 1.00 15.18 ? 78  PRO A CB  1 
ATOM   304  C CG  . PRO A 1 48  ? 29.152 26.467 42.849 1.00 15.90 ? 78  PRO A CG  1 
ATOM   305  C CD  . PRO A 1 48  ? 28.919 27.928 43.091 1.00 14.26 ? 78  PRO A CD  1 
ATOM   306  N N   . GLN A 1 49  ? 28.100 25.581 47.063 1.00 16.77 ? 79  GLN A N   1 
ATOM   307  C CA  . GLN A 1 49  ? 28.757 25.062 48.253 1.00 18.74 ? 79  GLN A CA  1 
ATOM   308  C C   . GLN A 1 49  ? 28.864 23.542 48.181 1.00 23.66 ? 79  GLN A C   1 
ATOM   309  O O   . GLN A 1 49  ? 28.085 22.873 47.495 1.00 21.99 ? 79  GLN A O   1 
ATOM   310  C CB  . GLN A 1 49  ? 27.991 25.470 49.515 1.00 17.95 ? 79  GLN A CB  1 
ATOM   311  C CG  . GLN A 1 49  ? 27.668 26.946 49.598 1.00 24.27 ? 79  GLN A CG  1 
ATOM   312  C CD  . GLN A 1 49  ? 28.900 27.799 49.825 1.00 29.59 ? 79  GLN A CD  1 
ATOM   313  O OE1 . GLN A 1 49  ? 29.583 27.665 50.841 1.00 37.12 ? 79  GLN A OE1 1 
ATOM   314  N NE2 . GLN A 1 49  ? 29.190 28.686 48.877 1.00 26.65 ? 79  GLN A NE2 1 
ATOM   315  N N   . HIS A 1 50  ? 29.841 23.003 48.907 1.00 23.78 ? 80  HIS A N   1 
ATOM   316  C CA  . HIS A 1 50  ? 29.999 21.558 48.988 1.00 27.50 ? 80  HIS A CA  1 
ATOM   317  C C   . HIS A 1 50  ? 28.743 20.928 49.578 1.00 26.30 ? 80  HIS A C   1 
ATOM   318  O O   . HIS A 1 50  ? 28.176 21.429 50.553 1.00 25.02 ? 80  HIS A O   1 
ATOM   319  C CB  . HIS A 1 50  ? 31.220 21.204 49.841 1.00 33.88 ? 80  HIS A CB  1 
ATOM   320  C CG  . HIS A 1 50  ? 31.818 19.868 49.519 1.00 43.69 ? 80  HIS A CG  1 
ATOM   321  N ND1 . HIS A 1 50  ? 32.755 19.694 48.522 1.00 43.09 ? 80  HIS A ND1 1 
ATOM   322  C CD2 . HIS A 1 50  ? 31.610 18.641 50.056 1.00 45.15 ? 80  HIS A CD2 1 
ATOM   323  C CE1 . HIS A 1 50  ? 33.101 18.420 48.460 1.00 44.66 ? 80  HIS A CE1 1 
ATOM   324  N NE2 . HIS A 1 50  ? 32.420 17.759 49.380 1.00 50.67 ? 80  HIS A NE2 1 
ATOM   325  N N   . ALA A 1 51  ? 28.298 19.831 48.971 1.00 22.41 ? 81  ALA A N   1 
ATOM   326  C CA  . ALA A 1 51  ? 27.120 19.136 49.457 1.00 22.29 ? 81  ALA A CA  1 
ATOM   327  C C   . ALA A 1 51  ? 27.453 18.351 50.723 1.00 27.01 ? 81  ALA A C   1 
ATOM   328  O O   . ALA A 1 51  ? 28.617 18.133 51.071 1.00 23.89 ? 81  ALA A O   1 
ATOM   329  C CB  . ALA A 1 51  ? 26.560 18.207 48.383 1.00 15.32 ? 81  ALA A CB  1 
ATOM   330  N N   . ARG A 1 52  ? 26.401 17.927 51.422 1.00 21.98 ? 82  ARG A N   1 
ATOM   331  C CA  . ARG A 1 52  ? 26.587 17.147 52.637 1.00 25.67 ? 82  ARG A CA  1 
ATOM   332  C C   . ARG A 1 52  ? 26.596 15.655 52.319 1.00 27.21 ? 82  ARG A C   1 
ATOM   333  O O   . ARG A 1 52  ? 25.845 15.199 51.451 1.00 27.91 ? 82  ARG A O   1 
ATOM   334  C CB  . ARG A 1 52  ? 25.480 17.444 53.639 1.00 27.63 ? 82  ARG A CB  1 
ATOM   335  C CG  . ARG A 1 52  ? 25.649 18.751 54.377 1.00 31.89 ? 82  ARG A CG  1 
ATOM   336  C CD  . ARG A 1 52  ? 24.349 19.138 55.051 1.00 38.49 ? 82  ARG A CD  1 
ATOM   337  N NE  . ARG A 1 52  ? 23.364 19.551 54.063 1.00 41.67 ? 82  ARG A NE  1 
ATOM   338  C CZ  . ARG A 1 52  ? 22.916 20.791 53.928 1.00 46.93 ? 82  ARG A CZ  1 
ATOM   339  N NH1 . ARG A 1 52  ? 23.263 21.748 54.774 1.00 44.00 ? 82  ARG A NH1 1 
ATOM   340  N NH2 . ARG A 1 52  ? 22.100 21.080 52.918 1.00 42.61 ? 82  ARG A NH2 1 
ATOM   341  N N   . PRO A 1 53  ? 27.426 14.884 53.015 1.00 26.52 ? 83  PRO A N   1 
ATOM   342  C CA  . PRO A 1 53  ? 27.437 13.436 52.800 1.00 27.43 ? 83  PRO A CA  1 
ATOM   343  C C   . PRO A 1 53  ? 26.163 12.796 53.321 1.00 22.76 ? 83  PRO A C   1 
ATOM   344  O O   . PRO A 1 53  ? 25.416 13.376 54.111 1.00 28.63 ? 83  PRO A O   1 
ATOM   345  C CB  . PRO A 1 53  ? 28.658 12.965 53.595 1.00 21.21 ? 83  PRO A CB  1 
ATOM   346  C CG  . PRO A 1 53  ? 28.789 13.978 54.683 1.00 31.09 ? 83  PRO A CG  1 
ATOM   347  C CD  . PRO A 1 53  ? 28.359 15.293 54.080 1.00 29.72 ? 83  PRO A CD  1 
ATOM   348  N N   . TRP A 1 54  ? 25.922 11.575 52.856 1.00 22.65 ? 84  TRP A N   1 
ATOM   349  C CA  . TRP A 1 54  ? 24.766 10.793 53.262 1.00 24.57 ? 84  TRP A CA  1 
ATOM   350  C C   . TRP A 1 54  ? 25.209 9.384  53.627 1.00 25.35 ? 84  TRP A C   1 
ATOM   351  O O   . TRP A 1 54  ? 26.318 8.953  53.302 1.00 25.59 ? 84  TRP A O   1 
ATOM   352  C CB  . TRP A 1 54  ? 23.710 10.728 52.153 1.00 17.45 ? 84  TRP A CB  1 
ATOM   353  C CG  . TRP A 1 54  ? 24.256 10.190 50.867 1.00 21.84 ? 84  TRP A CG  1 
ATOM   354  C CD1 . TRP A 1 54  ? 24.427 8.877  50.532 1.00 21.52 ? 84  TRP A CD1 1 
ATOM   355  C CD2 . TRP A 1 54  ? 24.713 10.954 49.745 1.00 21.61 ? 84  TRP A CD2 1 
ATOM   356  N NE1 . TRP A 1 54  ? 24.963 8.777  49.269 1.00 21.70 ? 84  TRP A NE1 1 
ATOM   357  C CE2 . TRP A 1 54  ? 25.144 10.038 48.763 1.00 20.34 ? 84  TRP A CE2 1 
ATOM   358  C CE3 . TRP A 1 54  ? 24.794 12.324 49.473 1.00 20.20 ? 84  TRP A CE3 1 
ATOM   359  C CZ2 . TRP A 1 54  ? 25.654 10.448 47.533 1.00 20.54 ? 84  TRP A CZ2 1 
ATOM   360  C CZ3 . TRP A 1 54  ? 25.296 12.729 48.252 1.00 23.22 ? 84  TRP A CZ3 1 
ATOM   361  C CH2 . TRP A 1 54  ? 25.721 11.796 47.297 1.00 23.09 ? 84  TRP A CH2 1 
ATOM   362  N N   . ALA A 1 55  ? 24.320 8.667  54.304 1.00 21.32 ? 85  ALA A N   1 
ATOM   363  C CA  . ALA A 1 55  ? 24.533 7.281  54.690 1.00 26.74 ? 85  ALA A CA  1 
ATOM   364  C C   . ALA A 1 55  ? 23.849 6.338  53.706 1.00 23.01 ? 85  ALA A C   1 
ATOM   365  O O   . ALA A 1 55  ? 22.929 6.718  52.975 1.00 22.73 ? 85  ALA A O   1 
ATOM   366  C CB  . ALA A 1 55  ? 24.007 7.025  56.107 1.00 21.37 ? 85  ALA A CB  1 
ATOM   367  N N   . GLY A 1 56  ? 24.327 5.095  53.689 1.00 24.84 ? 86  GLY A N   1 
ATOM   368  C CA  . GLY A 1 56  ? 23.724 4.089  52.846 1.00 24.71 ? 86  GLY A CA  1 
ATOM   369  C C   . GLY A 1 56  ? 23.900 4.397  51.370 1.00 22.85 ? 86  GLY A C   1 
ATOM   370  O O   . GLY A 1 56  ? 24.828 5.094  50.949 1.00 23.28 ? 86  GLY A O   1 
ATOM   371  N N   . VAL A 1 57  ? 22.982 3.865  50.569 1.00 22.60 ? 87  VAL A N   1 
ATOM   372  C CA  . VAL A 1 57  ? 23.009 4.031  49.120 1.00 23.01 ? 87  VAL A CA  1 
ATOM   373  C C   . VAL A 1 57  ? 21.868 4.959  48.727 1.00 20.01 ? 87  VAL A C   1 
ATOM   374  O O   . VAL A 1 57  ? 20.693 4.629  48.924 1.00 24.51 ? 87  VAL A O   1 
ATOM   375  C CB  . VAL A 1 57  ? 22.896 2.683  48.393 1.00 22.99 ? 87  VAL A CB  1 
ATOM   376  C CG1 . VAL A 1 57  ? 22.992 2.892  46.885 1.00 21.92 ? 87  VAL A CG1 1 
ATOM   377  C CG2 . VAL A 1 57  ? 23.980 1.726  48.885 1.00 21.03 ? 87  VAL A CG2 1 
ATOM   378  N N   . ARG A 1 58  ? 22.212 6.107  48.181 1.00 19.57 ? 88  ARG A N   1 
ATOM   379  C CA  . ARG A 1 58  ? 21.264 7.096  47.700 1.00 20.91 ? 88  ARG A CA  1 
ATOM   380  C C   . ARG A 1 58  ? 20.748 6.699  46.316 1.00 22.57 ? 88  ARG A C   1 
ATOM   381  O O   . ARG A 1 58  ? 21.526 6.256  45.460 1.00 21.66 ? 88  ARG A O   1 
ATOM   382  C CB  . ARG A 1 58  ? 21.928 8.472  47.645 1.00 18.49 ? 88  ARG A CB  1 
ATOM   383  C CG  . ARG A 1 58  ? 21.024 9.611  47.214 1.00 20.03 ? 88  ARG A CG  1 
ATOM   384  C CD  . ARG A 1 58  ? 21.822 10.904 47.053 1.00 21.26 ? 88  ARG A CD  1 
ATOM   385  N NE  . ARG A 1 58  ? 21.002 11.993 46.536 1.00 29.25 ? 88  ARG A NE  1 
ATOM   386  C CZ  . ARG A 1 58  ? 20.566 13.016 47.258 1.00 29.45 ? 88  ARG A CZ  1 
ATOM   387  N NH1 . ARG A 1 58  ? 20.893 13.154 48.532 1.00 35.81 ? 88  ARG A NH1 1 
ATOM   388  N NH2 . ARG A 1 58  ? 19.783 13.927 46.686 1.00 28.99 ? 88  ARG A NH2 1 
ATOM   389  N N   . PRO A 1 59  ? 19.443 6.826  46.079 1.00 20.68 ? 89  PRO A N   1 
ATOM   390  C CA  . PRO A 1 59  ? 18.902 6.520  44.749 1.00 20.60 ? 89  PRO A CA  1 
ATOM   391  C C   . PRO A 1 59  ? 19.454 7.475  43.702 1.00 24.55 ? 89  PRO A C   1 
ATOM   392  O O   . PRO A 1 59  ? 19.515 8.689  43.914 1.00 22.02 ? 89  PRO A O   1 
ATOM   393  C CB  . PRO A 1 59  ? 17.388 6.693  44.933 1.00 24.51 ? 89  PRO A CB  1 
ATOM   394  C CG  . PRO A 1 59  ? 17.158 6.560  46.405 1.00 23.65 ? 89  PRO A CG  1 
ATOM   395  C CD  . PRO A 1 59  ? 18.384 7.129  47.054 1.00 17.56 ? 89  PRO A CD  1 
ATOM   396  N N   . ALA A 1 60  ? 19.870 6.911  42.568 1.00 23.66 ? 90  ALA A N   1 
ATOM   397  C CA  . ALA A 1 60  ? 20.347 7.692  41.432 1.00 22.06 ? 90  ALA A CA  1 
ATOM   398  C C   . ALA A 1 60  ? 19.792 7.121  40.134 1.00 24.46 ? 90  ALA A C   1 
ATOM   399  O O   . ALA A 1 60  ? 20.496 7.023  39.124 1.00 21.32 ? 90  ALA A O   1 
ATOM   400  C CB  . ALA A 1 60  ? 21.875 7.745  41.392 1.00 23.17 ? 90  ALA A CB  1 
ATOM   401  N N   . THR A 1 61  ? 18.516 6.732  40.148 1.00 25.47 ? 91  THR A N   1 
ATOM   402  C CA  . THR A 1 61  ? 17.871 6.165  38.972 1.00 25.87 ? 91  THR A CA  1 
ATOM   403  C C   . THR A 1 61  ? 17.015 7.166  38.209 1.00 25.69 ? 91  THR A C   1 
ATOM   404  O O   . THR A 1 61  ? 16.631 6.881  37.071 1.00 23.05 ? 91  THR A O   1 
ATOM   405  C CB  . THR A 1 61  ? 16.995 4.965  39.361 1.00 25.98 ? 91  THR A CB  1 
ATOM   406  O OG1 . THR A 1 61  ? 16.014 5.374  40.322 1.00 29.68 ? 91  THR A OG1 1 
ATOM   407  C CG2 . THR A 1 61  ? 17.846 3.844  39.946 1.00 23.66 ? 91  THR A CG2 1 
ATOM   408  N N   . GLN A 1 62  ? 16.714 8.323  38.798 1.00 23.32 ? 92  GLN A N   1 
ATOM   409  C CA  . GLN A 1 62  ? 15.879 9.337  38.171 1.00 26.22 ? 92  GLN A CA  1 
ATOM   410  C C   . GLN A 1 62  ? 16.648 10.648 38.097 1.00 21.78 ? 92  GLN A C   1 
ATOM   411  O O   . GLN A 1 62  ? 17.422 10.977 39.002 1.00 19.26 ? 92  GLN A O   1 
ATOM   412  C CB  . GLN A 1 62  ? 14.571 9.545  38.947 1.00 27.00 ? 92  GLN A CB  1 
ATOM   413  C CG  . GLN A 1 62  ? 13.745 8.276  39.161 1.00 42.00 ? 92  GLN A CG  1 
ATOM   414  C CD  . GLN A 1 62  ? 13.233 7.676  37.860 1.00 49.07 ? 92  GLN A CD  1 
ATOM   415  O OE1 . GLN A 1 62  ? 13.018 8.383  36.873 1.00 54.60 ? 92  GLN A OE1 1 
ATOM   416  N NE2 . GLN A 1 62  ? 13.029 6.364  37.857 1.00 56.20 ? 92  GLN A NE2 1 
ATOM   417  N N   . PHE A 1 63  ? 16.450 11.379 37.003 1.00 15.63 ? 93  PHE A N   1 
ATOM   418  C CA  . PHE A 1 63  ? 17.024 12.709 36.879 1.00 17.06 ? 93  PHE A CA  1 
ATOM   419  C C   . PHE A 1 63  ? 16.567 13.589 38.036 1.00 20.41 ? 93  PHE A C   1 
ATOM   420  O O   . PHE A 1 63  ? 15.446 13.460 38.544 1.00 22.42 ? 93  PHE A O   1 
ATOM   421  C CB  . PHE A 1 63  ? 16.616 13.360 35.555 1.00 18.39 ? 93  PHE A CB  1 
ATOM   422  C CG  . PHE A 1 63  ? 17.285 12.765 34.352 1.00 21.39 ? 93  PHE A CG  1 
ATOM   423  C CD1 . PHE A 1 63  ? 18.654 12.895 34.172 1.00 15.81 ? 93  PHE A CD1 1 
ATOM   424  C CD2 . PHE A 1 63  ? 16.543 12.103 33.382 1.00 22.14 ? 93  PHE A CD2 1 
ATOM   425  C CE1 . PHE A 1 63  ? 19.275 12.360 33.058 1.00 18.67 ? 93  PHE A CE1 1 
ATOM   426  C CE2 . PHE A 1 63  ? 17.159 11.570 32.264 1.00 22.35 ? 93  PHE A CE2 1 
ATOM   427  C CZ  . PHE A 1 63  ? 18.528 11.698 32.105 1.00 21.38 ? 93  PHE A CZ  1 
ATOM   428  N N   . GLY A 1 64  ? 17.452 14.481 38.467 1.00 16.71 ? 94  GLY A N   1 
ATOM   429  C CA  . GLY A 1 64  ? 17.073 15.503 39.419 1.00 18.54 ? 94  GLY A CA  1 
ATOM   430  C C   . GLY A 1 64  ? 16.197 16.559 38.764 1.00 16.14 ? 94  GLY A C   1 
ATOM   431  O O   . GLY A 1 64  ? 15.897 16.523 37.570 1.00 16.93 ? 94  GLY A O   1 
ATOM   432  N N   . SER A 1 65  ? 15.770 17.520 39.573 1.00 16.31 ? 95  SER A N   1 
ATOM   433  C CA  . SER A 1 65  ? 14.980 18.620 39.042 1.00 18.34 ? 95  SER A CA  1 
ATOM   434  C C   . SER A 1 65  ? 15.819 19.475 38.096 1.00 17.23 ? 95  SER A C   1 
ATOM   435  O O   . SER A 1 65  ? 17.036 19.608 38.252 1.00 14.96 ? 95  SER A O   1 
ATOM   436  C CB  . SER A 1 65  ? 14.428 19.485 40.177 1.00 18.01 ? 95  SER A CB  1 
ATOM   437  O OG  . SER A 1 65  ? 13.621 18.727 41.064 1.00 21.05 ? 95  SER A OG  1 
ATOM   438  N N   . ASP A 1 66  ? 15.152 20.044 37.097 1.00 17.18 ? 96  ASP A N   1 
ATOM   439  C CA  . ASP A 1 66  ? 15.776 21.023 36.226 1.00 18.21 ? 96  ASP A CA  1 
ATOM   440  C C   . ASP A 1 66  ? 15.913 22.358 36.948 1.00 19.86 ? 96  ASP A C   1 
ATOM   441  O O   . ASP A 1 66  ? 15.114 22.702 37.827 1.00 16.74 ? 96  ASP A O   1 
ATOM   442  C CB  . ASP A 1 66  ? 14.953 21.222 34.951 1.00 17.10 ? 96  ASP A CB  1 
ATOM   443  C CG  . ASP A 1 66  ? 14.918 19.986 34.071 1.00 18.83 ? 96  ASP A CG  1 
ATOM   444  O OD1 . ASP A 1 66  ? 15.881 19.192 34.109 1.00 16.23 ? 96  ASP A OD1 1 
ATOM   445  O OD2 . ASP A 1 66  ? 13.923 19.813 33.335 1.00 16.59 ? 96  ASP A OD2 1 
ATOM   446  N N   . CYS A 1 67  ? 16.930 23.120 36.557 1.00 16.93 ? 97  CYS A N   1 
ATOM   447  C CA  . CYS A 1 67  ? 17.045 24.492 37.028 1.00 18.28 ? 97  CYS A CA  1 
ATOM   448  C C   . CYS A 1 67  ? 15.995 25.370 36.350 1.00 19.56 ? 97  CYS A C   1 
ATOM   449  O O   . CYS A 1 67  ? 15.536 25.080 35.242 1.00 17.12 ? 97  CYS A O   1 
ATOM   450  C CB  . CYS A 1 67  ? 18.453 25.028 36.764 1.00 15.25 ? 97  CYS A CB  1 
ATOM   451  S SG  . CYS A 1 67  ? 19.762 24.153 37.691 1.00 19.13 ? 97  CYS A SG  1 
ATOM   452  N N   . PHE A 1 68  ? 15.591 26.433 37.046 1.00 15.51 ? 98  PHE A N   1 
ATOM   453  C CA  . PHE A 1 68  ? 14.628 27.373 36.488 1.00 16.36 ? 98  PHE A CA  1 
ATOM   454  C C   . PHE A 1 68  ? 15.174 27.999 35.211 1.00 20.36 ? 98  PHE A C   1 
ATOM   455  O O   . PHE A 1 68  ? 16.352 28.362 35.131 1.00 21.40 ? 98  PHE A O   1 
ATOM   456  C CB  . PHE A 1 68  ? 14.299 28.472 37.502 1.00 15.94 ? 98  PHE A CB  1 
ATOM   457  C CG  . PHE A 1 68  ? 13.162 28.136 38.425 1.00 19.31 ? 98  PHE A CG  1 
ATOM   458  C CD1 . PHE A 1 68  ? 13.395 27.504 39.640 1.00 19.67 ? 98  PHE A CD1 1 
ATOM   459  C CD2 . PHE A 1 68  ? 11.858 28.470 38.089 1.00 21.96 ? 98  PHE A CD2 1 
ATOM   460  C CE1 . PHE A 1 68  ? 12.346 27.197 40.497 1.00 19.52 ? 98  PHE A CE1 1 
ATOM   461  C CE2 . PHE A 1 68  ? 10.802 28.170 38.944 1.00 17.74 ? 98  PHE A CE2 1 
ATOM   462  C CZ  . PHE A 1 68  ? 11.050 27.531 40.150 1.00 18.73 ? 98  PHE A CZ  1 
ATOM   463  N N   . GLY A 1 69  ? 14.312 28.126 34.211 1.00 17.11 ? 99  GLY A N   1 
ATOM   464  C CA  . GLY A 1 69  ? 14.713 28.697 32.937 1.00 19.68 ? 99  GLY A CA  1 
ATOM   465  C C   . GLY A 1 69  ? 13.506 28.832 32.036 1.00 18.63 ? 99  GLY A C   1 
ATOM   466  O O   . GLY A 1 69  ? 12.403 28.384 32.366 1.00 21.68 ? 99  GLY A O   1 
ATOM   467  N N   . ALA A 1 70  ? 13.736 29.466 30.884 1.00 22.79 ? 100 ALA A N   1 
ATOM   468  C CA  . ALA A 1 70  ? 12.681 29.647 29.891 1.00 18.75 ? 100 ALA A CA  1 
ATOM   469  C C   . ALA A 1 70  ? 12.044 28.310 29.538 1.00 21.51 ? 100 ALA A C   1 
ATOM   470  O O   . ALA A 1 70  ? 12.741 27.343 29.217 1.00 22.23 ? 100 ALA A O   1 
ATOM   471  C CB  . ALA A 1 70  ? 13.248 30.311 28.635 1.00 21.43 ? 100 ALA A CB  1 
ATOM   472  N N   . ALA A 1 71  ? 10.709 28.266 29.602 1.00 24.05 ? 101 ALA A N   1 
ATOM   473  C CA  . ALA A 1 71  ? 9.985  27.002 29.477 1.00 18.49 ? 101 ALA A CA  1 
ATOM   474  C C   . ALA A 1 71  ? 10.277 26.305 28.154 1.00 19.85 ? 101 ALA A C   1 
ATOM   475  O O   . ALA A 1 71  ? 10.433 25.078 28.114 1.00 17.13 ? 101 ALA A O   1 
ATOM   476  C CB  . ALA A 1 71  ? 8.483  27.244 29.629 1.00 18.97 ? 101 ALA A CB  1 
ATOM   477  N N   . TYR A 1 72  ? 10.361 27.065 27.060 1.00 16.75 ? 102 TYR A N   1 
ATOM   478  C CA  . TYR A 1 72  ? 10.550 26.444 25.754 1.00 23.48 ? 102 TYR A CA  1 
ATOM   479  C C   . TYR A 1 72  ? 11.902 25.758 25.619 1.00 21.37 ? 102 TYR A C   1 
ATOM   480  O O   . TYR A 1 72  ? 12.080 24.962 24.691 1.00 26.48 ? 102 TYR A O   1 
ATOM   481  C CB  . TYR A 1 72  ? 10.382 27.481 24.639 1.00 19.43 ? 102 TYR A CB  1 
ATOM   482  C CG  . TYR A 1 72  ? 11.591 28.365 24.410 1.00 23.36 ? 102 TYR A CG  1 
ATOM   483  C CD1 . TYR A 1 72  ? 11.839 29.462 25.224 1.00 23.08 ? 102 TYR A CD1 1 
ATOM   484  C CD2 . TYR A 1 72  ? 12.475 28.108 23.370 1.00 24.66 ? 102 TYR A CD2 1 
ATOM   485  C CE1 . TYR A 1 72  ? 12.940 30.275 25.013 1.00 24.80 ? 102 TYR A CE1 1 
ATOM   486  C CE2 . TYR A 1 72  ? 13.575 28.916 23.148 1.00 26.03 ? 102 TYR A CE2 1 
ATOM   487  C CZ  . TYR A 1 72  ? 13.806 29.996 23.973 1.00 24.88 ? 102 TYR A CZ  1 
ATOM   488  O OH  . TYR A 1 72  ? 14.906 30.799 23.756 1.00 31.93 ? 102 TYR A OH  1 
ATOM   489  N N   . LEU A 1 73  ? 12.847 26.036 26.515 1.00 21.78 ? 103 LEU A N   1 
ATOM   490  C CA  . LEU A 1 73  ? 14.166 25.418 26.472 1.00 27.19 ? 103 LEU A CA  1 
ATOM   491  C C   . LEU A 1 73  ? 14.239 24.122 27.268 1.00 25.47 ? 103 LEU A C   1 
ATOM   492  O O   . LEU A 1 73  ? 15.295 23.480 27.285 1.00 24.22 ? 103 LEU A O   1 
ATOM   493  C CB  . LEU A 1 73  ? 15.226 26.402 26.979 1.00 19.11 ? 103 LEU A CB  1 
ATOM   494  C CG  . LEU A 1 73  ? 15.440 27.609 26.062 1.00 24.76 ? 103 LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 73  ? 16.267 28.689 26.745 1.00 19.88 ? 103 LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 73  ? 16.091 27.173 24.757 1.00 21.18 ? 103 LEU A CD2 1 
ATOM   497  N N   . ARG A 1 74  ? 13.154 23.725 27.932 1.00 19.33 ? 104 ARG A N   1 
ATOM   498  C CA  . ARG A 1 74  ? 13.093 22.427 28.587 1.00 22.67 ? 104 ARG A CA  1 
ATOM   499  C C   . ARG A 1 74  ? 11.953 21.574 28.062 1.00 17.71 ? 104 ARG A C   1 
ATOM   500  O O   . ARG A 1 74  ? 11.761 20.455 28.550 1.00 20.95 ? 104 ARG A O   1 
ATOM   501  C CB  . ARG A 1 74  ? 12.968 22.582 30.113 1.00 18.84 ? 104 ARG A CB  1 
ATOM   502  C CG  . ARG A 1 74  ? 11.627 23.092 30.607 1.00 19.03 ? 104 ARG A CG  1 
ATOM   503  C CD  . ARG A 1 74  ? 11.582 23.127 32.128 1.00 20.26 ? 104 ARG A CD  1 
ATOM   504  N NE  . ARG A 1 74  ? 11.745 21.803 32.718 1.00 18.69 ? 104 ARG A NE  1 
ATOM   505  C CZ  . ARG A 1 74  ? 10.740 21.008 33.061 1.00 22.62 ? 104 ARG A CZ  1 
ATOM   506  N NH1 . ARG A 1 74  ? 9.480  21.381 32.905 1.00 18.67 ? 104 ARG A NH1 1 
ATOM   507  N NH2 . ARG A 1 74  ? 11.007 19.813 33.579 1.00 19.98 ? 104 ARG A NH2 1 
ATOM   508  N N   . LYS A 1 75  ? 11.195 22.068 27.088 1.00 23.52 ? 105 LYS A N   1 
ATOM   509  C CA  . LYS A 1 75  ? 10.178 21.260 26.432 1.00 25.46 ? 105 LYS A CA  1 
ATOM   510  C C   . LYS A 1 75  ? 10.794 19.959 25.947 1.00 26.04 ? 105 LYS A C   1 
ATOM   511  O O   . LYS A 1 75  ? 11.764 19.966 25.184 1.00 26.40 ? 105 LYS A O   1 
ATOM   512  C CB  . LYS A 1 75  ? 9.571  22.043 25.268 1.00 24.34 ? 105 LYS A CB  1 
ATOM   513  C CG  . LYS A 1 75  ? 8.060  21.966 25.186 1.00 34.37 ? 105 LYS A CG  1 
ATOM   514  C CD  . LYS A 1 75  ? 7.616  21.036 24.071 1.00 40.30 ? 105 LYS A CD  1 
ATOM   515  C CE  . LYS A 1 75  ? 6.105  21.035 23.924 1.00 40.22 ? 105 LYS A CE  1 
ATOM   516  N NZ  . LYS A 1 75  ? 5.675  20.181 22.783 1.00 62.39 ? 105 LYS A NZ  1 
ATOM   517  N N   . GLY A 1 76  ? 10.259 18.842 26.426 1.00 26.48 ? 106 GLY A N   1 
ATOM   518  C CA  . GLY A 1 76  ? 10.833 17.541 26.149 1.00 26.69 ? 106 GLY A CA  1 
ATOM   519  C C   . GLY A 1 76  ? 11.772 17.015 27.211 1.00 26.09 ? 106 GLY A C   1 
ATOM   520  O O   . GLY A 1 76  ? 12.400 15.973 26.994 1.00 24.75 ? 106 GLY A O   1 
ATOM   521  N N   . SER A 1 77  ? 11.877 17.690 28.354 1.00 20.23 ? 107 SER A N   1 
ATOM   522  C CA  . SER A 1 77  ? 12.765 17.249 29.422 1.00 22.71 ? 107 SER A CA  1 
ATOM   523  C C   . SER A 1 77  ? 12.261 15.956 30.051 1.00 23.08 ? 107 SER A C   1 
ATOM   524  O O   . SER A 1 77  ? 11.055 15.759 30.221 1.00 22.10 ? 107 SER A O   1 
ATOM   525  C CB  . SER A 1 77  ? 12.879 18.330 30.500 1.00 18.01 ? 107 SER A CB  1 
ATOM   526  O OG  . SER A 1 77  ? 13.599 17.855 31.624 1.00 18.92 ? 107 SER A OG  1 
ATOM   527  N N   . LEU A 1 78  ? 13.195 15.078 30.411 1.00 17.61 ? 108 LEU A N   1 
ATOM   528  C CA  . LEU A 1 78  ? 12.863 13.842 31.103 1.00 19.44 ? 108 LEU A CA  1 
ATOM   529  C C   . LEU A 1 78  ? 12.880 13.990 32.620 1.00 17.82 ? 108 LEU A C   1 
ATOM   530  O O   . LEU A 1 78  ? 12.650 13.002 33.325 1.00 18.01 ? 108 LEU A O   1 
ATOM   531  C CB  . LEU A 1 78  ? 13.828 12.733 30.679 1.00 17.97 ? 108 LEU A CB  1 
ATOM   532  C CG  . LEU A 1 78  ? 13.882 12.450 29.179 1.00 20.97 ? 108 LEU A CG  1 
ATOM   533  C CD1 . LEU A 1 78  ? 14.987 11.461 28.883 1.00 18.79 ? 108 LEU A CD1 1 
ATOM   534  C CD2 . LEU A 1 78  ? 12.534 11.939 28.673 1.00 17.07 ? 108 LEU A CD2 1 
ATOM   535  N N   . ALA A 1 79  ? 13.140 15.194 33.130 1.00 18.18 ? 109 ALA A N   1 
ATOM   536  C CA  . ALA A 1 79  ? 13.208 15.453 34.560 1.00 18.35 ? 109 ALA A CA  1 
ATOM   537  C C   . ALA A 1 79  ? 11.811 15.528 35.172 1.00 20.63 ? 109 ALA A C   1 
ATOM   538  O O   . ALA A 1 79  ? 10.832 15.814 34.479 1.00 23.17 ? 109 ALA A O   1 
ATOM   539  C CB  . ALA A 1 79  ? 13.962 16.755 34.816 1.00 16.23 ? 109 ALA A CB  1 
ATOM   540  N N   . PRO A 1 80  ? 11.690 15.280 36.482 1.00 18.75 ? 110 PRO A N   1 
ATOM   541  C CA  . PRO A 1 80  ? 10.364 15.297 37.117 1.00 20.20 ? 110 PRO A CA  1 
ATOM   542  C C   . PRO A 1 80  ? 9.804  16.687 37.382 1.00 19.78 ? 110 PRO A C   1 
ATOM   543  O O   . PRO A 1 80  ? 8.640  16.790 37.796 1.00 28.22 ? 110 PRO A O   1 
ATOM   544  C CB  . PRO A 1 80  ? 10.604 14.544 38.434 1.00 18.45 ? 110 PRO A CB  1 
ATOM   545  C CG  . PRO A 1 80  ? 12.035 14.797 38.744 1.00 20.42 ? 110 PRO A CG  1 
ATOM   546  C CD  . PRO A 1 80  ? 12.741 14.838 37.417 1.00 17.36 ? 110 PRO A CD  1 
ATOM   547  N N   . GLY A 1 81  ? 10.575 17.747 37.168 1.00 21.00 ? 111 GLY A N   1 
ATOM   548  C CA  . GLY A 1 81  ? 10.066 19.082 37.417 1.00 20.46 ? 111 GLY A CA  1 
ATOM   549  C C   . GLY A 1 81  ? 11.183 20.108 37.420 1.00 25.74 ? 111 GLY A C   1 
ATOM   550  O O   . GLY A 1 81  ? 12.272 19.869 36.894 1.00 16.79 ? 111 GLY A O   1 
ATOM   551  N N   . VAL A 1 82  ? 10.883 21.255 38.026 1.00 19.71 ? 112 VAL A N   1 
ATOM   552  C CA  . VAL A 1 82  ? 11.773 22.407 38.070 1.00 19.50 ? 112 VAL A CA  1 
ATOM   553  C C   . VAL A 1 82  ? 11.920 22.843 39.521 1.00 23.27 ? 112 VAL A C   1 
ATOM   554  O O   . VAL A 1 82  ? 10.946 22.830 40.283 1.00 22.67 ? 112 VAL A O   1 
ATOM   555  C CB  . VAL A 1 82  ? 11.233 23.566 37.201 1.00 19.90 ? 112 VAL A CB  1 
ATOM   556  C CG1 . VAL A 1 82  ? 12.071 24.825 37.376 1.00 21.10 ? 112 VAL A CG1 1 
ATOM   557  C CG2 . VAL A 1 82  ? 11.178 23.157 35.744 1.00 17.48 ? 112 VAL A CG2 1 
ATOM   558  N N   . SER A 1 83  ? 13.134 23.229 39.903 1.00 19.62 ? 113 SER A N   1 
ATOM   559  C CA  . SER A 1 83  ? 13.394 23.640 41.275 1.00 19.96 ? 113 SER A CA  1 
ATOM   560  C C   . SER A 1 83  ? 14.691 24.435 41.327 1.00 20.77 ? 113 SER A C   1 
ATOM   561  O O   . SER A 1 83  ? 15.576 24.260 40.483 1.00 21.45 ? 113 SER A O   1 
ATOM   562  C CB  . SER A 1 83  ? 13.475 22.424 42.208 1.00 17.60 ? 113 SER A CB  1 
ATOM   563  O OG  . SER A 1 83  ? 13.812 22.807 43.529 1.00 18.08 ? 113 SER A OG  1 
ATOM   564  N N   . GLU A 1 84  ? 14.788 25.326 42.318 1.00 15.31 ? 114 GLU A N   1 
ATOM   565  C CA  . GLU A 1 84  ? 16.084 25.923 42.620 1.00 17.33 ? 114 GLU A CA  1 
ATOM   566  C C   . GLU A 1 84  ? 17.065 24.864 43.101 1.00 17.75 ? 114 GLU A C   1 
ATOM   567  O O   . GLU A 1 84  ? 18.277 24.987 42.883 1.00 16.01 ? 114 GLU A O   1 
ATOM   568  C CB  . GLU A 1 84  ? 15.931 27.027 43.667 1.00 19.15 ? 114 GLU A CB  1 
ATOM   569  C CG  . GLU A 1 84  ? 15.447 28.350 43.110 1.00 17.99 ? 114 GLU A CG  1 
ATOM   570  C CD  . GLU A 1 84  ? 15.566 29.478 44.117 1.00 18.21 ? 114 GLU A CD  1 
ATOM   571  O OE1 . GLU A 1 84  ? 14.756 29.517 45.069 1.00 17.46 ? 114 GLU A OE1 1 
ATOM   572  O OE2 . GLU A 1 84  ? 16.482 30.317 43.964 1.00 16.03 ? 114 GLU A OE2 1 
ATOM   573  N N   . ASP A 1 85  ? 16.557 23.827 43.762 1.00 14.84 ? 115 ASP A N   1 
ATOM   574  C CA  . ASP A 1 85  ? 17.322 22.639 44.130 1.00 14.77 ? 115 ASP A CA  1 
ATOM   575  C C   . ASP A 1 85  ? 17.497 21.816 42.859 1.00 19.67 ? 115 ASP A C   1 
ATOM   576  O O   . ASP A 1 85  ? 16.697 20.932 42.547 1.00 17.61 ? 115 ASP A O   1 
ATOM   577  C CB  . ASP A 1 85  ? 16.594 21.869 45.227 1.00 16.81 ? 115 ASP A CB  1 
ATOM   578  C CG  . ASP A 1 85  ? 17.353 20.649 45.703 1.00 19.99 ? 115 ASP A CG  1 
ATOM   579  O OD1 . ASP A 1 85  ? 18.371 20.275 45.083 1.00 17.93 ? 115 ASP A OD1 1 
ATOM   580  O OD2 . ASP A 1 85  ? 16.918 20.059 46.716 1.00 23.41 ? 115 ASP A OD2 1 
ATOM   581  N N   . CYS A 1 86  ? 18.568 22.109 42.117 1.00 15.60 ? 116 CYS A N   1 
ATOM   582  C CA  . CYS A 1 86  ? 18.743 21.551 40.785 1.00 14.89 ? 116 CYS A CA  1 
ATOM   583  C C   . CYS A 1 86  ? 20.184 21.216 40.423 1.00 14.54 ? 116 CYS A C   1 
ATOM   584  O O   . CYS A 1 86  ? 20.428 20.804 39.286 1.00 18.99 ? 116 CYS A O   1 
ATOM   585  C CB  . CYS A 1 86  ? 18.185 22.526 39.735 1.00 17.32 ? 116 CYS A CB  1 
ATOM   586  S SG  . CYS A 1 86  ? 19.087 24.101 39.612 1.00 16.05 ? 116 CYS A SG  1 
ATOM   587  N N   . LEU A 1 87  ? 21.145 21.382 41.331 1.00 14.11 ? 117 LEU A N   1 
ATOM   588  C CA  . LEU A 1 87  ? 22.546 21.113 41.009 1.00 16.96 ? 117 LEU A CA  1 
ATOM   589  C C   . LEU A 1 87  ? 22.784 19.606 41.078 1.00 17.76 ? 117 LEU A C   1 
ATOM   590  O O   . LEU A 1 87  ? 23.255 19.054 42.078 1.00 17.09 ? 117 LEU A O   1 
ATOM   591  C CB  . LEU A 1 87  ? 23.468 21.885 41.941 1.00 13.81 ? 117 LEU A CB  1 
ATOM   592  C CG  . LEU A 1 87  ? 23.300 23.404 41.838 1.00 16.24 ? 117 LEU A CG  1 
ATOM   593  C CD1 . LEU A 1 87  ? 24.271 24.144 42.752 1.00 17.03 ? 117 LEU A CD1 1 
ATOM   594  C CD2 . LEU A 1 87  ? 23.467 23.854 40.391 1.00 13.59 ? 117 LEU A CD2 1 
ATOM   595  N N   . TYR A 1 88  ? 22.454 18.931 39.976 1.00 13.79 ? 118 TYR A N   1 
ATOM   596  C CA  . TYR A 1 88  ? 22.561 17.484 39.870 1.00 13.92 ? 118 TYR A CA  1 
ATOM   597  C C   . TYR A 1 88  ? 23.323 17.115 38.603 1.00 17.42 ? 118 TYR A C   1 
ATOM   598  O O   . TYR A 1 88  ? 23.342 17.874 37.629 1.00 16.67 ? 118 TYR A O   1 
ATOM   599  C CB  . TYR A 1 88  ? 21.165 16.825 39.869 1.00 17.41 ? 118 TYR A CB  1 
ATOM   600  C CG  . TYR A 1 88  ? 20.419 17.031 41.168 1.00 18.29 ? 118 TYR A CG  1 
ATOM   601  C CD1 . TYR A 1 88  ? 20.708 16.254 42.282 1.00 17.47 ? 118 TYR A CD1 1 
ATOM   602  C CD2 . TYR A 1 88  ? 19.444 18.014 41.287 1.00 15.76 ? 118 TYR A CD2 1 
ATOM   603  C CE1 . TYR A 1 88  ? 20.039 16.440 43.482 1.00 21.55 ? 118 TYR A CE1 1 
ATOM   604  C CE2 . TYR A 1 88  ? 18.768 18.209 42.488 1.00 17.69 ? 118 TYR A CE2 1 
ATOM   605  C CZ  . TYR A 1 88  ? 19.074 17.416 43.578 1.00 17.70 ? 118 TYR A CZ  1 
ATOM   606  O OH  . TYR A 1 88  ? 18.423 17.597 44.772 1.00 21.83 ? 118 TYR A OH  1 
ATOM   607  N N   . LEU A 1 89  ? 23.967 15.949 38.623 1.00 16.36 ? 119 LEU A N   1 
ATOM   608  C CA  . LEU A 1 89  ? 24.680 15.456 37.453 1.00 16.83 ? 119 LEU A CA  1 
ATOM   609  C C   . LEU A 1 89  ? 24.352 13.987 37.214 1.00 17.14 ? 119 LEU A C   1 
ATOM   610  O O   . LEU A 1 89  ? 23.821 13.284 38.077 1.00 17.73 ? 119 LEU A O   1 
ATOM   611  C CB  . LEU A 1 89  ? 26.204 15.663 37.573 1.00 14.52 ? 119 LEU A CB  1 
ATOM   612  C CG  . LEU A 1 89  ? 27.049 15.111 38.725 1.00 17.81 ? 119 LEU A CG  1 
ATOM   613  C CD1 . LEU A 1 89  ? 27.323 13.615 38.586 1.00 15.37 ? 119 LEU A CD1 1 
ATOM   614  C CD2 . LEU A 1 89  ? 28.361 15.880 38.799 1.00 19.82 ? 119 LEU A CD2 1 
ATOM   615  N N   . ASN A 1 90  ? 24.700 13.536 36.014 1.00 17.41 ? 120 ASN A N   1 
ATOM   616  C CA  . ASN A 1 90  ? 24.403 12.211 35.502 1.00 14.79 ? 120 ASN A CA  1 
ATOM   617  C C   . ASN A 1 90  ? 25.664 11.650 34.865 1.00 17.40 ? 120 ASN A C   1 
ATOM   618  O O   . ASN A 1 90  ? 26.431 12.388 34.237 1.00 18.77 ? 120 ASN A O   1 
ATOM   619  C CB  . ASN A 1 90  ? 23.260 12.270 34.479 1.00 14.59 ? 120 ASN A CB  1 
ATOM   620  C CG  . ASN A 1 90  ? 22.192 13.276 34.865 1.00 16.42 ? 120 ASN A CG  1 
ATOM   621  O OD1 . ASN A 1 90  ? 21.493 13.099 35.862 1.00 17.98 ? 120 ASN A OD1 1 
ATOM   622  N ND2 . ASN A 1 90  ? 22.064 14.341 34.079 1.00 14.22 ? 120 ASN A ND2 1 
ATOM   623  N N   . VAL A 1 91  ? 25.864 10.343 35.021 1.00 17.82 ? 121 VAL A N   1 
ATOM   624  C CA  . VAL A 1 91  ? 27.080 9.660  34.595 1.00 16.61 ? 121 VAL A CA  1 
ATOM   625  C C   . VAL A 1 91  ? 26.706 8.392  33.834 1.00 18.74 ? 121 VAL A C   1 
ATOM   626  O O   . VAL A 1 91  ? 25.918 7.579  34.325 1.00 18.45 ? 121 VAL A O   1 
ATOM   627  C CB  . VAL A 1 91  ? 27.987 9.314  35.796 1.00 18.87 ? 121 VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 91  ? 29.279 8.655  35.323 1.00 15.38 ? 121 VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 91  ? 28.286 10.558 36.632 1.00 14.86 ? 121 VAL A CG2 1 
ATOM   630  N N   . TRP A 1 92  ? 27.276 8.225  32.645 1.00 15.51 ? 122 TRP A N   1 
ATOM   631  C CA  . TRP A 1 92  ? 27.224 6.979  31.891 1.00 16.87 ? 122 TRP A CA  1 
ATOM   632  C C   . TRP A 1 92  ? 28.626 6.396  31.813 1.00 19.44 ? 122 TRP A C   1 
ATOM   633  O O   . TRP A 1 92  ? 29.591 7.119  31.545 1.00 17.51 ? 122 TRP A O   1 
ATOM   634  C CB  . TRP A 1 92  ? 26.690 7.191  30.468 1.00 16.18 ? 122 TRP A CB  1 
ATOM   635  C CG  . TRP A 1 92  ? 25.222 7.467  30.389 1.00 16.46 ? 122 TRP A CG  1 
ATOM   636  C CD1 . TRP A 1 92  ? 24.234 6.569  30.116 1.00 16.33 ? 122 TRP A CD1 1 
ATOM   637  C CD2 . TRP A 1 92  ? 24.578 8.728  30.585 1.00 15.58 ? 122 TRP A CD2 1 
ATOM   638  N NE1 . TRP A 1 92  ? 23.011 7.194  30.127 1.00 16.21 ? 122 TRP A NE1 1 
ATOM   639  C CE2 . TRP A 1 92  ? 23.194 8.521  30.412 1.00 15.99 ? 122 TRP A CE2 1 
ATOM   640  C CE3 . TRP A 1 92  ? 25.035 10.012 30.887 1.00 15.17 ? 122 TRP A CE3 1 
ATOM   641  C CZ2 . TRP A 1 92  ? 22.264 9.551  30.535 1.00 15.53 ? 122 TRP A CZ2 1 
ATOM   642  C CZ3 . TRP A 1 92  ? 24.109 11.036 31.006 1.00 14.94 ? 122 TRP A CZ3 1 
ATOM   643  C CH2 . TRP A 1 92  ? 22.740 10.798 30.832 1.00 15.12 ? 122 TRP A CH2 1 
ATOM   644  N N   . ALA A 1 93  ? 28.741 5.088  32.038 1.00 19.01 ? 123 ALA A N   1 
ATOM   645  C CA  . ALA A 1 93  ? 30.069 4.483  31.975 1.00 21.68 ? 123 ALA A CA  1 
ATOM   646  C C   . ALA A 1 93  ? 29.969 3.032  31.536 1.00 23.70 ? 123 ALA A C   1 
ATOM   647  O O   . ALA A 1 93  ? 29.019 2.344  31.927 1.00 23.03 ? 123 ALA A O   1 
ATOM   648  C CB  . ALA A 1 93  ? 30.792 4.562  33.324 1.00 16.84 ? 123 ALA A CB  1 
ATOM   649  N N   . PRO A 1 94  ? 30.921 2.540  30.744 1.00 19.70 ? 124 PRO A N   1 
ATOM   650  C CA  . PRO A 1 94  ? 30.912 1.117  30.385 1.00 25.36 ? 124 PRO A CA  1 
ATOM   651  C C   . PRO A 1 94  ? 30.884 0.245  31.630 1.00 29.70 ? 124 PRO A C   1 
ATOM   652  O O   . PRO A 1 94  ? 31.573 0.517  32.617 1.00 25.14 ? 124 PRO A O   1 
ATOM   653  C CB  . PRO A 1 94  ? 32.219 0.937  29.603 1.00 22.86 ? 124 PRO A CB  1 
ATOM   654  C CG  . PRO A 1 94  ? 32.561 2.305  29.113 1.00 21.47 ? 124 PRO A CG  1 
ATOM   655  C CD  . PRO A 1 94  ? 32.064 3.258  30.154 1.00 18.38 ? 124 PRO A CD  1 
ATOM   656  N N   . SER A 1 95  ? 30.059 -0.799 31.584 1.00 29.09 ? 125 SER A N   1 
ATOM   657  C CA  . SER A 1 95  ? 29.938 -1.695 32.724 1.00 35.46 ? 125 SER A CA  1 
ATOM   658  C C   . SER A 1 95  ? 31.277 -2.359 33.016 1.00 31.81 ? 125 SER A C   1 
ATOM   659  O O   . SER A 1 95  ? 32.003 -2.762 32.103 1.00 34.67 ? 125 SER A O   1 
ATOM   660  C CB  . SER A 1 95  ? 28.867 -2.755 32.458 1.00 34.18 ? 125 SER A CB  1 
ATOM   661  O OG  . SER A 1 95  ? 28.614 -3.521 33.623 1.00 42.49 ? 125 SER A OG  1 
ATOM   662  N N   . GLY A 1 96  ? 31.610 -2.458 34.299 1.00 38.67 ? 126 GLY A N   1 
ATOM   663  C CA  . GLY A 1 96  ? 32.876 -3.054 34.675 1.00 43.94 ? 126 GLY A CA  1 
ATOM   664  C C   . GLY A 1 96  ? 34.092 -2.205 34.389 1.00 44.71 ? 126 GLY A C   1 
ATOM   665  O O   . GLY A 1 96  ? 35.208 -2.729 34.349 1.00 45.82 ? 126 GLY A O   1 
ATOM   666  N N   . ALA A 1 97  ? 33.911 -0.904 34.176 1.00 45.49 ? 127 ALA A N   1 
ATOM   667  C CA  . ALA A 1 97  ? 35.052 -0.015 34.019 1.00 34.93 ? 127 ALA A CA  1 
ATOM   668  C C   . ALA A 1 97  ? 35.845 0.042  35.317 1.00 32.31 ? 127 ALA A C   1 
ATOM   669  O O   . ALA A 1 97  ? 35.273 0.175  36.403 1.00 32.90 ? 127 ALA A O   1 
ATOM   670  C CB  . ALA A 1 97  ? 34.588 1.383  33.618 1.00 26.78 ? 127 ALA A CB  1 
ATOM   671  N N   . LYS A 1 98  ? 37.163 -0.073 35.201 1.00 27.20 ? 128 LYS A N   1 
ATOM   672  C CA  . LYS A 1 98  ? 38.053 -0.036 36.350 1.00 32.25 ? 128 LYS A CA  1 
ATOM   673  C C   . LYS A 1 98  ? 38.453 1.399  36.668 1.00 28.89 ? 128 LYS A C   1 
ATOM   674  O O   . LYS A 1 98  ? 38.310 2.295  35.830 1.00 27.92 ? 128 LYS A O   1 
ATOM   675  C CB  . LYS A 1 98  ? 39.287 -0.898 36.075 1.00 26.07 ? 128 LYS A CB  1 
ATOM   676  C CG  . LYS A 1 98  ? 38.980 -2.388 36.027 1.00 29.19 ? 128 LYS A CG  1 
ATOM   677  C CD  . LYS A 1 98  ? 40.216 -3.217 35.716 1.00 34.24 ? 128 LYS A CD  1 
ATOM   678  C CE  . LYS A 1 98  ? 40.694 -2.982 34.293 1.00 29.71 ? 128 LYS A CE  1 
ATOM   679  N NZ  . LYS A 1 98  ? 39.674 -3.391 33.289 1.00 40.06 ? 128 LYS A NZ  1 
ATOM   680  N N   . PRO A 1 99  ? 38.932 1.660  37.887 1.00 27.37 ? 129 PRO A N   1 
ATOM   681  C CA  . PRO A 1 99  ? 39.314 3.032  38.250 1.00 23.74 ? 129 PRO A CA  1 
ATOM   682  C C   . PRO A 1 99  ? 40.401 3.574  37.334 1.00 25.80 ? 129 PRO A C   1 
ATOM   683  O O   . PRO A 1 99  ? 41.422 2.924  37.101 1.00 25.88 ? 129 PRO A O   1 
ATOM   684  C CB  . PRO A 1 99  ? 39.814 2.891  39.692 1.00 23.23 ? 129 PRO A CB  1 
ATOM   685  C CG  . PRO A 1 99  ? 39.138 1.672  40.213 1.00 25.57 ? 129 PRO A CG  1 
ATOM   686  C CD  . PRO A 1 99  ? 38.997 0.745  39.042 1.00 23.73 ? 129 PRO A CD  1 
ATOM   687  N N   . GLY A 1 100 ? 40.172 4.781  36.817 1.00 30.19 ? 130 GLY A N   1 
ATOM   688  C CA  . GLY A 1 100 ? 41.121 5.424  35.926 1.00 24.18 ? 130 GLY A CA  1 
ATOM   689  C C   . GLY A 1 100 ? 41.199 4.856  34.525 1.00 28.57 ? 130 GLY A C   1 
ATOM   690  O O   . GLY A 1 100 ? 42.112 5.219  33.772 1.00 26.73 ? 130 GLY A O   1 
ATOM   691  N N   . GLN A 1 101 ? 40.265 3.983  34.144 1.00 25.25 ? 131 GLN A N   1 
ATOM   692  C CA  . GLN A 1 101 ? 40.402 3.271  32.878 1.00 24.80 ? 131 GLN A CA  1 
ATOM   693  C C   . GLN A 1 101 ? 40.121 4.183  31.689 1.00 24.90 ? 131 GLN A C   1 
ATOM   694  O O   . GLN A 1 101 ? 40.927 4.258  30.752 1.00 24.89 ? 131 GLN A O   1 
ATOM   695  C CB  . GLN A 1 101 ? 39.477 2.053  32.852 1.00 22.05 ? 131 GLN A CB  1 
ATOM   696  C CG  . GLN A 1 101 ? 39.491 1.319  31.527 1.00 22.50 ? 131 GLN A CG  1 
ATOM   697  C CD  . GLN A 1 101 ? 38.761 -0.006 31.583 1.00 25.75 ? 131 GLN A CD  1 
ATOM   698  O OE1 . GLN A 1 101 ? 38.243 -0.397 32.627 1.00 30.31 ? 131 GLN A OE1 1 
ATOM   699  N NE2 . GLN A 1 101 ? 38.720 -0.709 30.457 1.00 21.14 ? 131 GLN A NE2 1 
ATOM   700  N N   . TYR A 1 102 ? 38.980 4.872  31.701 1.00 18.04 ? 132 TYR A N   1 
ATOM   701  C CA  . TYR A 1 102 ? 38.491 5.580  30.532 1.00 21.53 ? 132 TYR A CA  1 
ATOM   702  C C   . TYR A 1 102 ? 38.669 7.086  30.645 1.00 21.09 ? 132 TYR A C   1 
ATOM   703  O O   . TYR A 1 102 ? 38.760 7.635  31.746 1.00 17.33 ? 132 TYR A O   1 
ATOM   704  C CB  . TYR A 1 102 ? 37.007 5.255  30.308 1.00 21.03 ? 132 TYR A CB  1 
ATOM   705  C CG  . TYR A 1 102 ? 36.743 3.829  29.881 1.00 21.99 ? 132 TYR A CG  1 
ATOM   706  C CD1 . TYR A 1 102 ? 37.124 3.382  28.620 1.00 23.38 ? 132 TYR A CD1 1 
ATOM   707  C CD2 . TYR A 1 102 ? 36.125 2.927  30.737 1.00 22.89 ? 132 TYR A CD2 1 
ATOM   708  C CE1 . TYR A 1 102 ? 36.894 2.074  28.222 1.00 21.39 ? 132 TYR A CE1 1 
ATOM   709  C CE2 . TYR A 1 102 ? 35.888 1.617  30.346 1.00 26.41 ? 132 TYR A CE2 1 
ATOM   710  C CZ  . TYR A 1 102 ? 36.275 1.198  29.089 1.00 27.07 ? 132 TYR A CZ  1 
ATOM   711  O OH  . TYR A 1 102 ? 36.040 -0.099 28.698 1.00 27.72 ? 132 TYR A OH  1 
ATOM   712  N N   . PRO A 1 103 ? 38.741 7.783  29.514 1.00 18.64 ? 133 PRO A N   1 
ATOM   713  C CA  . PRO A 1 103 ? 38.652 9.246  29.536 1.00 16.67 ? 133 PRO A CA  1 
ATOM   714  C C   . PRO A 1 103 ? 37.227 9.686  29.834 1.00 16.24 ? 133 PRO A C   1 
ATOM   715  O O   . PRO A 1 103 ? 36.274 8.913  29.721 1.00 16.29 ? 133 PRO A O   1 
ATOM   716  C CB  . PRO A 1 103 ? 39.076 9.645  28.119 1.00 16.78 ? 133 PRO A CB  1 
ATOM   717  C CG  . PRO A 1 103 ? 38.690 8.463  27.281 1.00 17.95 ? 133 PRO A CG  1 
ATOM   718  C CD  . PRO A 1 103 ? 38.907 7.254  28.149 1.00 17.47 ? 133 PRO A CD  1 
ATOM   719  N N   . VAL A 1 104 ? 37.084 10.949 30.225 1.00 15.85 ? 134 VAL A N   1 
ATOM   720  C CA  . VAL A 1 104 ? 35.796 11.498 30.634 1.00 16.38 ? 134 VAL A CA  1 
ATOM   721  C C   . VAL A 1 104 ? 35.432 12.650 29.709 1.00 16.89 ? 134 VAL A C   1 
ATOM   722  O O   . VAL A 1 104 ? 36.284 13.478 29.376 1.00 17.57 ? 134 VAL A O   1 
ATOM   723  C CB  . VAL A 1 104 ? 35.814 11.974 32.102 1.00 15.90 ? 134 VAL A CB  1 
ATOM   724  C CG1 . VAL A 1 104 ? 34.432 12.436 32.539 1.00 16.01 ? 134 VAL A CG1 1 
ATOM   725  C CG2 . VAL A 1 104 ? 36.350 10.876 33.021 1.00 15.78 ? 134 VAL A CG2 1 
ATOM   726  N N   . MET A 1 105 ? 34.167 12.694 29.289 1.00 15.03 ? 135 MET A N   1 
ATOM   727  C CA  . MET A 1 105 ? 33.620 13.810 28.524 1.00 14.79 ? 135 MET A CA  1 
ATOM   728  C C   . MET A 1 105 ? 32.493 14.431 29.339 1.00 14.47 ? 135 MET A C   1 
ATOM   729  O O   . MET A 1 105 ? 31.523 13.747 29.686 1.00 14.49 ? 135 MET A O   1 
ATOM   730  C CB  . MET A 1 105 ? 33.122 13.356 27.144 1.00 14.98 ? 135 MET A CB  1 
ATOM   731  C CG  . MET A 1 105 ? 34.183 12.649 26.306 1.00 15.37 ? 135 MET A CG  1 
ATOM   732  S SD  . MET A 1 105 ? 33.614 12.066 24.692 1.00 15.70 ? 135 MET A SD  1 
ATOM   733  C CE  . MET A 1 105 ? 33.317 13.621 23.848 1.00 15.46 ? 135 MET A CE  1 
ATOM   734  N N   . VAL A 1 106 ? 32.627 15.718 29.650 1.00 14.23 ? 136 VAL A N   1 
ATOM   735  C CA  . VAL A 1 106 ? 31.687 16.443 30.504 1.00 16.76 ? 136 VAL A CA  1 
ATOM   736  C C   . VAL A 1 106 ? 30.923 17.431 29.633 1.00 18.58 ? 136 VAL A C   1 
ATOM   737  O O   . VAL A 1 106 ? 31.504 18.387 29.102 1.00 16.48 ? 136 VAL A O   1 
ATOM   738  C CB  . VAL A 1 106 ? 32.402 17.158 31.662 1.00 15.83 ? 136 VAL A CB  1 
ATOM   739  C CG1 . VAL A 1 106 ? 31.387 17.839 32.580 1.00 14.80 ? 136 VAL A CG1 1 
ATOM   740  C CG2 . VAL A 1 106 ? 33.254 16.178 32.455 1.00 14.10 ? 136 VAL A CG2 1 
ATOM   741  N N   . TRP A 1 107 ? 29.621 17.198 29.492 1.00 15.44 ? 137 TRP A N   1 
ATOM   742  C CA  . TRP A 1 107 ? 28.779 17.965 28.585 1.00 13.74 ? 137 TRP A CA  1 
ATOM   743  C C   . TRP A 1 107 ? 28.244 19.230 29.244 1.00 14.91 ? 137 TRP A C   1 
ATOM   744  O O   . TRP A 1 107 ? 27.914 19.242 30.435 1.00 15.18 ? 137 TRP A O   1 
ATOM   745  C CB  . TRP A 1 107 ? 27.615 17.101 28.091 1.00 14.19 ? 137 TRP A CB  1 
ATOM   746  C CG  . TRP A 1 107 ? 26.666 17.800 27.154 1.00 13.93 ? 137 TRP A CG  1 
ATOM   747  C CD1 . TRP A 1 107 ? 25.358 18.104 27.389 1.00 18.65 ? 137 TRP A CD1 1 
ATOM   748  C CD2 . TRP A 1 107 ? 26.954 18.275 25.834 1.00 15.66 ? 137 TRP A CD2 1 
ATOM   749  N NE1 . TRP A 1 107 ? 24.811 18.735 26.298 1.00 16.21 ? 137 TRP A NE1 1 
ATOM   750  C CE2 . TRP A 1 107 ? 25.771 18.852 25.329 1.00 16.10 ? 137 TRP A CE2 1 
ATOM   751  C CE3 . TRP A 1 107 ? 28.097 18.265 25.029 1.00 14.38 ? 137 TRP A CE3 1 
ATOM   752  C CZ2 . TRP A 1 107 ? 25.699 19.416 24.057 1.00 14.26 ? 137 TRP A CZ2 1 
ATOM   753  C CZ3 . TRP A 1 107 ? 28.025 18.821 23.766 1.00 14.32 ? 137 TRP A CZ3 1 
ATOM   754  C CH2 . TRP A 1 107 ? 26.835 19.392 23.294 1.00 15.88 ? 137 TRP A CH2 1 
ATOM   755  N N   . VAL A 1 108 ? 28.171 20.300 28.454 1.00 17.45 ? 138 VAL A N   1 
ATOM   756  C CA  . VAL A 1 108 ? 27.614 21.580 28.879 1.00 17.39 ? 138 VAL A CA  1 
ATOM   757  C C   . VAL A 1 108 ? 26.580 21.977 27.825 1.00 16.13 ? 138 VAL A C   1 
ATOM   758  O O   . VAL A 1 108 ? 26.931 22.425 26.716 1.00 15.68 ? 138 VAL A O   1 
ATOM   759  C CB  . VAL A 1 108 ? 28.681 22.666 29.055 1.00 15.60 ? 138 VAL A CB  1 
ATOM   760  C CG1 . VAL A 1 108 ? 28.079 23.884 29.749 1.00 14.48 ? 138 VAL A CG1 1 
ATOM   761  C CG2 . VAL A 1 108 ? 29.866 22.133 29.855 1.00 15.61 ? 138 VAL A CG2 1 
ATOM   762  N N   . TYR A 1 109 ? 25.303 21.814 28.168 1.00 14.32 ? 139 TYR A N   1 
ATOM   763  C CA  . TYR A 1 109 ? 24.228 22.185 27.264 1.00 16.68 ? 139 TYR A CA  1 
ATOM   764  C C   . TYR A 1 109 ? 24.133 23.697 27.148 1.00 15.65 ? 139 TYR A C   1 
ATOM   765  O O   . TYR A 1 109 ? 24.563 24.443 28.034 1.00 14.16 ? 139 TYR A O   1 
ATOM   766  C CB  . TYR A 1 109 ? 22.886 21.616 27.732 1.00 14.85 ? 139 TYR A CB  1 
ATOM   767  C CG  . TYR A 1 109 ? 22.434 22.083 29.101 1.00 16.72 ? 139 TYR A CG  1 
ATOM   768  C CD1 . TYR A 1 109 ? 21.858 23.338 29.285 1.00 16.50 ? 139 TYR A CD1 1 
ATOM   769  C CD2 . TYR A 1 109 ? 22.569 21.261 30.209 1.00 14.66 ? 139 TYR A CD2 1 
ATOM   770  C CE1 . TYR A 1 109 ? 21.451 23.764 30.540 1.00 17.63 ? 139 TYR A CE1 1 
ATOM   771  C CE2 . TYR A 1 109 ? 22.160 21.675 31.467 1.00 16.06 ? 139 TYR A CE2 1 
ATOM   772  C CZ  . TYR A 1 109 ? 21.603 22.926 31.624 1.00 16.27 ? 139 TYR A CZ  1 
ATOM   773  O OH  . TYR A 1 109 ? 21.198 23.335 32.869 1.00 16.92 ? 139 TYR A OH  1 
ATOM   774  N N   . GLY A 1 110 ? 23.539 24.142 26.046 1.00 13.75 ? 140 GLY A N   1 
ATOM   775  C CA  . GLY A 1 110 ? 23.317 25.552 25.794 1.00 13.79 ? 140 GLY A CA  1 
ATOM   776  C C   . GLY A 1 110 ? 21.805 25.859 25.856 1.00 19.32 ? 140 GLY A C   1 
ATOM   777  O O   . GLY A 1 110 ? 20.993 25.067 25.383 1.00 33.70 ? 140 GLY A O   1 
ATOM   778  N N   . GLY A 1 111 ? 21.500 27.011 26.411 1.00 22.60 ? 141 GLY A N   1 
ATOM   779  C CA  . GLY A 1 111 ? 20.144 27.503 26.453 1.00 18.42 ? 141 GLY A CA  1 
ATOM   780  C C   . GLY A 1 111 ? 20.155 29.013 26.514 1.00 17.64 ? 141 GLY A C   1 
ATOM   781  O O   . GLY A 1 111 ? 19.359 29.629 27.228 1.00 19.81 ? 141 GLY A O   1 
ATOM   782  N N   . GLY A 1 112 ? 21.084 29.618 25.776 1.00 18.55 ? 142 GLY A N   1 
ATOM   783  C CA  . GLY A 1 112 ? 21.197 31.070 25.734 1.00 20.44 ? 142 GLY A CA  1 
ATOM   784  C C   . GLY A 1 112 ? 21.422 31.717 27.080 1.00 20.38 ? 142 GLY A C   1 
ATOM   785  O O   . GLY A 1 112 ? 21.123 32.903 27.250 1.00 23.81 ? 142 GLY A O   1 
ATOM   786  N N   . PHE A 1 113 ? 21.947 30.963 28.046 1.00 17.18 ? 143 PHE A N   1 
ATOM   787  C CA  . PHE A 1 113 ? 22.052 31.407 29.439 1.00 19.47 ? 143 PHE A CA  1 
ATOM   788  C C   . PHE A 1 113 ? 20.692 31.829 29.989 1.00 21.07 ? 143 PHE A C   1 
ATOM   789  O O   . PHE A 1 113 ? 20.595 32.656 30.902 1.00 21.68 ? 143 PHE A O   1 
ATOM   790  C CB  . PHE A 1 113 ? 23.074 32.537 29.603 1.00 19.12 ? 143 PHE A CB  1 
ATOM   791  C CG  . PHE A 1 113 ? 24.465 32.168 29.168 1.00 19.26 ? 143 PHE A CG  1 
ATOM   792  C CD1 . PHE A 1 113 ? 25.282 31.407 29.984 1.00 19.81 ? 143 PHE A CD1 1 
ATOM   793  C CD2 . PHE A 1 113 ? 24.955 32.591 27.946 1.00 21.29 ? 143 PHE A CD2 1 
ATOM   794  C CE1 . PHE A 1 113 ? 26.565 31.071 29.583 1.00 20.21 ? 143 PHE A CE1 1 
ATOM   795  C CE2 . PHE A 1 113 ? 26.233 32.266 27.546 1.00 16.09 ? 143 PHE A CE2 1 
ATOM   796  C CZ  . PHE A 1 113 ? 27.039 31.501 28.363 1.00 13.72 ? 143 PHE A CZ  1 
ATOM   797  N N   . ALA A 1 114 ? 19.627 31.252 29.433 1.00 18.84 ? 144 ALA A N   1 
ATOM   798  C CA  . ALA A 1 114 ? 18.268 31.538 29.864 1.00 21.52 ? 144 ALA A CA  1 
ATOM   799  C C   . ALA A 1 114 ? 17.486 30.299 30.259 1.00 20.52 ? 144 ALA A C   1 
ATOM   800  O O   . ALA A 1 114 ? 16.474 30.427 30.957 1.00 17.60 ? 144 ALA A O   1 
ATOM   801  C CB  . ALA A 1 114 ? 17.494 32.278 28.759 1.00 17.90 ? 144 ALA A CB  1 
ATOM   802  N N   . GLY A 1 115 ? 17.921 29.119 29.847 1.00 18.46 ? 145 GLY A N   1 
ATOM   803  C CA  . GLY A 1 115 ? 17.224 27.903 30.193 1.00 21.72 ? 145 GLY A CA  1 
ATOM   804  C C   . GLY A 1 115 ? 18.010 26.689 29.757 1.00 23.77 ? 145 GLY A C   1 
ATOM   805  O O   . GLY A 1 115 ? 19.207 26.770 29.472 1.00 26.74 ? 145 GLY A O   1 
ATOM   806  N N   . GLY A 1 116 ? 17.321 25.560 29.706 1.00 19.51 ? 146 GLY A N   1 
ATOM   807  C CA  . GLY A 1 116 ? 17.909 24.311 29.269 1.00 19.08 ? 146 GLY A CA  1 
ATOM   808  C C   . GLY A 1 116 ? 18.052 23.312 30.406 1.00 16.22 ? 146 GLY A C   1 
ATOM   809  O O   . GLY A 1 116 ? 17.859 23.617 31.585 1.00 16.72 ? 146 GLY A O   1 
ATOM   810  N N   . THR A 1 117 ? 18.403 22.088 30.016 1.00 15.09 ? 147 THR A N   1 
ATOM   811  C CA  . THR A 1 117 ? 18.559 20.990 30.958 1.00 16.35 ? 147 THR A CA  1 
ATOM   812  C C   . THR A 1 117 ? 19.400 19.900 30.321 1.00 14.77 ? 147 THR A C   1 
ATOM   813  O O   . THR A 1 117 ? 19.418 19.749 29.097 1.00 17.53 ? 147 THR A O   1 
ATOM   814  C CB  . THR A 1 117 ? 17.209 20.400 31.381 1.00 16.51 ? 147 THR A CB  1 
ATOM   815  O OG1 . THR A 1 117 ? 17.435 19.213 32.155 1.00 19.44 ? 147 THR A OG1 1 
ATOM   816  C CG2 . THR A 1 117 ? 16.379 20.039 30.161 1.00 15.71 ? 147 THR A CG2 1 
ATOM   817  N N   . ALA A 1 118 ? 20.082 19.133 31.171 1.00 14.41 ? 148 ALA A N   1 
ATOM   818  C CA  . ALA A 1 118 ? 20.783 17.947 30.707 1.00 14.48 ? 148 ALA A CA  1 
ATOM   819  C C   . ALA A 1 118 ? 19.836 16.795 30.403 1.00 18.65 ? 148 ALA A C   1 
ATOM   820  O O   . ALA A 1 118 ? 20.200 15.898 29.633 1.00 17.47 ? 148 ALA A O   1 
ATOM   821  C CB  . ALA A 1 118 ? 21.815 17.507 31.745 1.00 14.36 ? 148 ALA A CB  1 
ATOM   822  N N   . ALA A 1 119 ? 18.623 16.813 30.956 1.00 17.31 ? 149 ALA A N   1 
ATOM   823  C CA  . ALA A 1 119 ? 17.708 15.689 30.807 1.00 16.61 ? 149 ALA A CA  1 
ATOM   824  C C   . ALA A 1 119 ? 16.979 15.728 29.470 1.00 18.92 ? 149 ALA A C   1 
ATOM   825  O O   . ALA A 1 119 ? 15.756 15.566 29.417 1.00 21.66 ? 149 ALA A O   1 
ATOM   826  C CB  . ALA A 1 119 ? 16.698 15.662 31.957 1.00 14.89 ? 149 ALA A CB  1 
ATOM   827  N N   . MET A 1 120 ? 17.716 15.951 28.389 1.00 20.56 ? 150 MET A N   1 
ATOM   828  C CA  . MET A 1 120 ? 17.111 15.788 27.074 1.00 17.82 ? 150 MET A CA  1 
ATOM   829  C C   . MET A 1 120 ? 17.438 14.410 26.518 1.00 19.75 ? 150 MET A C   1 
ATOM   830  O O   . MET A 1 120 ? 18.558 13.915 26.714 1.00 18.22 ? 150 MET A O   1 
ATOM   831  C CB  . MET A 1 120 ? 17.611 16.852 26.094 1.00 18.06 ? 150 MET A CB  1 
ATOM   832  C CG  . MET A 1 120 ? 17.154 18.269 26.413 1.00 23.67 ? 150 MET A CG  1 
ATOM   833  S SD  . MET A 1 120 ? 15.362 18.401 26.645 1.00 30.93 ? 150 MET A SD  1 
ATOM   834  C CE  . MET A 1 120 ? 15.144 20.171 26.527 1.00 25.82 ? 150 MET A CE  1 
ATOM   835  N N   . PRO A 1 121 ? 16.480 13.773 25.832 1.00 24.59 ? 151 PRO A N   1 
ATOM   836  C CA  . PRO A 1 121 ? 16.768 12.451 25.252 1.00 22.04 ? 151 PRO A CA  1 
ATOM   837  C C   . PRO A 1 121 ? 17.944 12.471 24.290 1.00 22.17 ? 151 PRO A C   1 
ATOM   838  O O   . PRO A 1 121 ? 18.652 11.463 24.177 1.00 19.58 ? 151 PRO A O   1 
ATOM   839  C CB  . PRO A 1 121 ? 15.453 12.063 24.551 1.00 20.72 ? 151 PRO A CB  1 
ATOM   840  C CG  . PRO A 1 121 ? 14.605 13.310 24.533 1.00 27.10 ? 151 PRO A CG  1 
ATOM   841  C CD  . PRO A 1 121 ? 15.080 14.193 25.631 1.00 22.55 ? 151 PRO A CD  1 
ATOM   842  N N   . TYR A 1 122 ? 18.200 13.597 23.624 1.00 19.13 ? 152 TYR A N   1 
ATOM   843  C CA  . TYR A 1 122 ? 19.344 13.689 22.730 1.00 21.77 ? 152 TYR A CA  1 
ATOM   844  C C   . TYR A 1 122 ? 20.643 14.035 23.455 1.00 20.29 ? 152 TYR A C   1 
ATOM   845  O O   . TYR A 1 122 ? 21.682 14.150 22.796 1.00 19.07 ? 152 TYR A O   1 
ATOM   846  C CB  . TYR A 1 122 ? 19.069 14.701 21.604 1.00 23.89 ? 152 TYR A CB  1 
ATOM   847  C CG  . TYR A 1 122 ? 18.359 15.968 22.018 1.00 20.13 ? 152 TYR A CG  1 
ATOM   848  C CD1 . TYR A 1 122 ? 19.072 17.072 22.476 1.00 22.22 ? 152 TYR A CD1 1 
ATOM   849  C CD2 . TYR A 1 122 ? 16.978 16.072 21.925 1.00 24.51 ? 152 TYR A CD2 1 
ATOM   850  C CE1 . TYR A 1 122 ? 18.421 18.244 22.844 1.00 24.15 ? 152 TYR A CE1 1 
ATOM   851  C CE2 . TYR A 1 122 ? 16.317 17.237 22.292 1.00 23.13 ? 152 TYR A CE2 1 
ATOM   852  C CZ  . TYR A 1 122 ? 17.043 18.318 22.748 1.00 25.44 ? 152 TYR A CZ  1 
ATOM   853  O OH  . TYR A 1 122 ? 16.389 19.473 23.110 1.00 29.84 ? 152 TYR A OH  1 
ATOM   854  N N   . TYR A 1 123 ? 20.622 14.195 24.781 1.00 18.20 ? 153 TYR A N   1 
ATOM   855  C CA  . TYR A 1 123 ? 21.843 14.293 25.576 1.00 16.66 ? 153 TYR A CA  1 
ATOM   856  C C   . TYR A 1 123 ? 22.128 13.010 26.350 1.00 19.85 ? 153 TYR A C   1 
ATOM   857  O O   . TYR A 1 123 ? 22.961 13.019 27.263 1.00 19.61 ? 153 TYR A O   1 
ATOM   858  C CB  . TYR A 1 123 ? 21.779 15.470 26.555 1.00 14.73 ? 153 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 123 ? 21.660 16.838 25.925 1.00 15.80 ? 153 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 123 ? 22.197 17.104 24.672 1.00 16.81 ? 153 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 123 ? 21.013 17.871 26.594 1.00 16.77 ? 153 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 123 ? 22.087 18.371 24.101 1.00 19.36 ? 153 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 123 ? 20.894 19.131 26.034 1.00 16.96 ? 153 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 123 ? 21.432 19.376 24.788 1.00 19.22 ? 153 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 123 ? 21.311 20.629 24.234 1.00 20.51 ? 153 TYR A OH  1 
ATOM   866  N N   . ASP A 1 124 ? 21.440 11.916 26.026 1.00 18.54 ? 154 ASP A N   1 
ATOM   867  C CA  . ASP A 1 124 ? 21.713 10.634 26.664 1.00 16.48 ? 154 ASP A CA  1 
ATOM   868  C C   . ASP A 1 124 ? 23.114 10.152 26.296 1.00 18.13 ? 154 ASP A C   1 
ATOM   869  O O   . ASP A 1 124 ? 23.482 10.112 25.119 1.00 21.36 ? 154 ASP A O   1 
ATOM   870  C CB  . ASP A 1 124 ? 20.650 9.615  26.238 1.00 16.43 ? 154 ASP A CB  1 
ATOM   871  C CG  . ASP A 1 124 ? 20.787 8.284  26.947 1.00 21.82 ? 154 ASP A CG  1 
ATOM   872  O OD1 . ASP A 1 124 ? 21.656 7.482  26.548 1.00 26.02 ? 154 ASP A OD1 1 
ATOM   873  O OD2 . ASP A 1 124 ? 20.027 8.045  27.909 1.00 26.47 ? 154 ASP A OD2 1 
ATOM   874  N N   . GLY A 1 125 ? 23.897 9.781  27.305 1.00 17.45 ? 155 GLY A N   1 
ATOM   875  C CA  . GLY A 1 125 ? 25.299 9.484  27.105 1.00 17.25 ? 155 GLY A CA  1 
ATOM   876  C C   . GLY A 1 125 ? 25.643 8.050  26.767 1.00 18.33 ? 155 GLY A C   1 
ATOM   877  O O   . GLY A 1 125 ? 26.829 7.705  26.751 1.00 20.76 ? 155 GLY A O   1 
ATOM   878  N N   . GLU A 1 126 ? 24.651 7.207  26.470 1.00 19.12 ? 156 GLU A N   1 
ATOM   879  C CA  . GLU A 1 126 ? 24.912 5.781  26.288 1.00 20.92 ? 156 GLU A CA  1 
ATOM   880  C C   . GLU A 1 126 ? 25.763 5.513  25.053 1.00 22.30 ? 156 GLU A C   1 
ATOM   881  O O   . GLU A 1 126 ? 26.747 4.765  25.118 1.00 21.67 ? 156 GLU A O   1 
ATOM   882  C CB  . GLU A 1 126 ? 23.594 5.022  26.190 1.00 22.27 ? 156 GLU A CB  1 
ATOM   883  C CG  . GLU A 1 126 ? 23.587 3.726  26.945 1.00 29.86 ? 156 GLU A CG  1 
ATOM   884  C CD  . GLU A 1 126 ? 22.201 3.144  27.038 1.00 33.73 ? 156 GLU A CD  1 
ATOM   885  O OE1 . GLU A 1 126 ? 21.756 2.525  26.051 1.00 32.22 ? 156 GLU A OE1 1 
ATOM   886  O OE2 . GLU A 1 126 ? 21.552 3.326  28.092 1.00 29.57 ? 156 GLU A OE2 1 
ATOM   887  N N   . ALA A 1 127 ? 25.378 6.085  23.910 1.00 20.18 ? 157 ALA A N   1 
ATOM   888  C CA  . ALA A 1 127 ? 26.075 5.790  22.664 1.00 19.34 ? 157 ALA A CA  1 
ATOM   889  C C   . ALA A 1 127 ? 27.515 6.280  22.704 1.00 19.80 ? 157 ALA A C   1 
ATOM   890  O O   . ALA A 1 127 ? 28.409 5.644  22.135 1.00 18.58 ? 157 ALA A O   1 
ATOM   891  C CB  . ALA A 1 127 ? 25.329 6.410  21.487 1.00 17.95 ? 157 ALA A CB  1 
ATOM   892  N N   . LEU A 1 128 ? 27.759 7.411  23.370 1.00 21.04 ? 158 LEU A N   1 
ATOM   893  C CA  . LEU A 1 128 ? 29.130 7.873  23.555 1.00 22.37 ? 158 LEU A CA  1 
ATOM   894  C C   . LEU A 1 128 ? 29.893 6.950  24.494 1.00 20.19 ? 158 LEU A C   1 
ATOM   895  O O   . LEU A 1 128 ? 31.015 6.532  24.189 1.00 20.98 ? 158 LEU A O   1 
ATOM   896  C CB  . LEU A 1 128 ? 29.136 9.306  24.084 1.00 19.42 ? 158 LEU A CB  1 
ATOM   897  C CG  . LEU A 1 128 ? 29.003 10.397 23.024 1.00 21.62 ? 158 LEU A CG  1 
ATOM   898  C CD1 . LEU A 1 128 ? 28.759 11.759 23.660 1.00 20.13 ? 158 LEU A CD1 1 
ATOM   899  C CD2 . LEU A 1 128 ? 30.247 10.429 22.146 1.00 16.42 ? 158 LEU A CD2 1 
ATOM   900  N N   . ALA A 1 129 ? 29.285 6.598  25.630 1.00 22.45 ? 159 ALA A N   1 
ATOM   901  C CA  . ALA A 1 129 ? 29.982 5.794  26.629 1.00 18.53 ? 159 ALA A CA  1 
ATOM   902  C C   . ALA A 1 129 ? 30.354 4.424  26.076 1.00 20.27 ? 159 ALA A C   1 
ATOM   903  O O   . ALA A 1 129 ? 31.411 3.876  26.415 1.00 19.95 ? 159 ALA A O   1 
ATOM   904  C CB  . ALA A 1 129 ? 29.122 5.658  27.888 1.00 16.84 ? 159 ALA A CB  1 
ATOM   905  N N   . ARG A 1 130 ? 29.491 3.849  25.232 1.00 17.97 ? 160 ARG A N   1 
ATOM   906  C CA  . ARG A 1 130 ? 29.784 2.553  24.624 1.00 21.81 ? 160 ARG A CA  1 
ATOM   907  C C   . ARG A 1 130 ? 31.053 2.572  23.776 1.00 21.25 ? 160 ARG A C   1 
ATOM   908  O O   . ARG A 1 130 ? 31.659 1.517  23.562 1.00 21.73 ? 160 ARG A O   1 
ATOM   909  C CB  . ARG A 1 130 ? 28.605 2.085  23.765 1.00 24.31 ? 160 ARG A CB  1 
ATOM   910  C CG  . ARG A 1 130 ? 27.745 1.034  24.427 1.00 35.55 ? 160 ARG A CG  1 
ATOM   911  C CD  . ARG A 1 130 ? 26.700 0.488  23.472 1.00 37.88 ? 160 ARG A CD  1 
ATOM   912  N NE  . ARG A 1 130 ? 25.508 1.323  23.420 1.00 25.63 ? 160 ARG A NE  1 
ATOM   913  C CZ  . ARG A 1 130 ? 24.423 1.122  24.154 1.00 32.97 ? 160 ARG A CZ  1 
ATOM   914  N NH1 . ARG A 1 130 ? 24.340 0.109  24.999 1.00 34.15 ? 160 ARG A NH1 1 
ATOM   915  N NH2 . ARG A 1 130 ? 23.396 1.958  24.035 1.00 43.67 ? 160 ARG A NH2 1 
ATOM   916  N N   . GLN A 1 131 ? 31.465 3.737  23.283 1.00 20.94 ? 161 GLN A N   1 
ATOM   917  C CA  . GLN A 1 131 ? 32.712 3.835  22.537 1.00 18.93 ? 161 GLN A CA  1 
ATOM   918  C C   . GLN A 1 131 ? 33.927 3.936  23.449 1.00 20.52 ? 161 GLN A C   1 
ATOM   919  O O   . GLN A 1 131 ? 35.042 4.102  22.948 1.00 20.19 ? 161 GLN A O   1 
ATOM   920  C CB  . GLN A 1 131 ? 32.655 5.036  21.583 1.00 18.49 ? 161 GLN A CB  1 
ATOM   921  C CG  . GLN A 1 131 ? 31.394 5.038  20.710 1.00 19.81 ? 161 GLN A CG  1 
ATOM   922  C CD  . GLN A 1 131 ? 31.320 6.217  19.761 1.00 22.44 ? 161 GLN A CD  1 
ATOM   923  O OE1 . GLN A 1 131 ? 32.174 6.389  18.893 1.00 22.31 ? 161 GLN A OE1 1 
ATOM   924  N NE2 . GLN A 1 131 ? 30.288 7.035  19.919 1.00 21.68 ? 161 GLN A NE2 1 
ATOM   925  N N   . GLY A 1 132 ? 33.739 3.828  24.764 1.00 21.48 ? 162 GLY A N   1 
ATOM   926  C CA  . GLY A 1 132 ? 34.854 3.775  25.688 1.00 18.35 ? 162 GLY A CA  1 
ATOM   927  C C   . GLY A 1 132 ? 35.151 5.078  26.396 1.00 17.77 ? 162 GLY A C   1 
ATOM   928  O O   . GLY A 1 132 ? 36.310 5.495  26.467 1.00 19.79 ? 162 GLY A O   1 
ATOM   929  N N   . VAL A 1 133 ? 34.118 5.745  26.914 1.00 17.32 ? 163 VAL A N   1 
ATOM   930  C CA  . VAL A 1 133 ? 34.293 6.976  27.672 1.00 18.00 ? 163 VAL A CA  1 
ATOM   931  C C   . VAL A 1 133 ? 33.316 6.981  28.841 1.00 20.87 ? 163 VAL A C   1 
ATOM   932  O O   . VAL A 1 133 ? 32.319 6.255  28.855 1.00 17.26 ? 163 VAL A O   1 
ATOM   933  C CB  . VAL A 1 133 ? 34.091 8.251  26.812 1.00 17.77 ? 163 VAL A CB  1 
ATOM   934  C CG1 . VAL A 1 133 ? 34.959 8.226  25.551 1.00 21.36 ? 163 VAL A CG1 1 
ATOM   935  C CG2 . VAL A 1 133 ? 32.646 8.428  26.453 1.00 20.18 ? 163 VAL A CG2 1 
ATOM   936  N N   . VAL A 1 134 ? 33.625 7.810  29.836 1.00 16.23 ? 164 VAL A N   1 
ATOM   937  C CA  . VAL A 1 134 ? 32.696 8.148  30.911 1.00 15.93 ? 164 VAL A CA  1 
ATOM   938  C C   . VAL A 1 134 ? 32.060 9.485  30.553 1.00 15.51 ? 164 VAL A C   1 
ATOM   939  O O   . VAL A 1 134 ? 32.759 10.498 30.434 1.00 17.78 ? 164 VAL A O   1 
ATOM   940  C CB  . VAL A 1 134 ? 33.406 8.219  32.273 1.00 16.02 ? 164 VAL A CB  1 
ATOM   941  C CG1 . VAL A 1 134 ? 32.437 8.660  33.355 1.00 15.64 ? 164 VAL A CG1 1 
ATOM   942  C CG2 . VAL A 1 134 ? 34.040 6.875  32.633 1.00 17.22 ? 164 VAL A CG2 1 
ATOM   943  N N   . VAL A 1 135 ? 30.741 9.492  30.364 1.00 15.75 ? 165 VAL A N   1 
ATOM   944  C CA  . VAL A 1 135 ? 30.007 10.684 29.947 1.00 15.61 ? 165 VAL A CA  1 
ATOM   945  C C   . VAL A 1 135 ? 29.338 11.301 31.164 1.00 15.81 ? 165 VAL A C   1 
ATOM   946  O O   . VAL A 1 135 ? 28.642 10.611 31.915 1.00 15.08 ? 165 VAL A O   1 
ATOM   947  C CB  . VAL A 1 135 ? 28.956 10.352 28.873 1.00 15.24 ? 165 VAL A CB  1 
ATOM   948  C CG1 . VAL A 1 135 ? 28.364 11.631 28.304 1.00 14.96 ? 165 VAL A CG1 1 
ATOM   949  C CG2 . VAL A 1 135 ? 29.554 9.497  27.781 1.00 15.63 ? 165 VAL A CG2 1 
ATOM   950  N N   . VAL A 1 136 ? 29.522 12.603 31.349 1.00 17.75 ? 166 VAL A N   1 
ATOM   951  C CA  . VAL A 1 136 ? 28.901 13.331 32.447 1.00 16.84 ? 166 VAL A CA  1 
ATOM   952  C C   . VAL A 1 136 ? 28.069 14.465 31.866 1.00 18.30 ? 166 VAL A C   1 
ATOM   953  O O   . VAL A 1 136 ? 28.563 15.247 31.047 1.00 15.77 ? 166 VAL A O   1 
ATOM   954  C CB  . VAL A 1 136 ? 29.948 13.873 33.437 1.00 16.63 ? 166 VAL A CB  1 
ATOM   955  C CG1 . VAL A 1 136 ? 29.273 14.701 34.512 1.00 13.99 ? 166 VAL A CG1 1 
ATOM   956  C CG2 . VAL A 1 136 ? 30.743 12.731 34.057 1.00 14.46 ? 166 VAL A CG2 1 
ATOM   957  N N   . THR A 1 137 ? 26.806 14.540 32.276 1.00 17.35 ? 167 THR A N   1 
ATOM   958  C CA  . THR A 1 137 ? 25.958 15.690 31.993 1.00 16.42 ? 167 THR A CA  1 
ATOM   959  C C   . THR A 1 137 ? 25.486 16.269 33.320 1.00 15.07 ? 167 THR A C   1 
ATOM   960  O O   . THR A 1 137 ? 25.499 15.587 34.340 1.00 17.61 ? 167 THR A O   1 
ATOM   961  C CB  . THR A 1 137 ? 24.763 15.318 31.099 1.00 16.16 ? 167 THR A CB  1 
ATOM   962  O OG1 . THR A 1 137 ? 23.857 14.463 31.812 1.00 16.93 ? 167 THR A OG1 1 
ATOM   963  C CG2 . THR A 1 137 ? 25.249 14.597 29.838 1.00 14.20 ? 167 THR A CG2 1 
ATOM   964  N N   . PHE A 1 138 ? 25.099 17.541 33.325 1.00 14.19 ? 168 PHE A N   1 
ATOM   965  C CA  . PHE A 1 138 ? 24.777 18.167 34.600 1.00 13.56 ? 168 PHE A CA  1 
ATOM   966  C C   . PHE A 1 138 ? 23.991 19.444 34.363 1.00 13.37 ? 168 PHE A C   1 
ATOM   967  O O   . PHE A 1 138 ? 24.104 20.080 33.314 1.00 14.13 ? 168 PHE A O   1 
ATOM   968  C CB  . PHE A 1 138 ? 26.045 18.476 35.407 1.00 16.24 ? 168 PHE A CB  1 
ATOM   969  C CG  . PHE A 1 138 ? 26.874 19.586 34.825 1.00 15.82 ? 168 PHE A CG  1 
ATOM   970  C CD1 . PHE A 1 138 ? 27.799 19.323 33.825 1.00 13.31 ? 168 PHE A CD1 1 
ATOM   971  C CD2 . PHE A 1 138 ? 26.727 20.891 35.272 1.00 13.20 ? 168 PHE A CD2 1 
ATOM   972  C CE1 . PHE A 1 138 ? 28.566 20.340 33.287 1.00 13.25 ? 168 PHE A CE1 1 
ATOM   973  C CE2 . PHE A 1 138 ? 27.487 21.909 34.735 1.00 13.14 ? 168 PHE A CE2 1 
ATOM   974  C CZ  . PHE A 1 138 ? 28.407 21.632 33.738 1.00 13.16 ? 168 PHE A CZ  1 
ATOM   975  N N   . ASN A 1 139 ? 23.209 19.821 35.373 1.00 15.26 ? 169 ASN A N   1 
ATOM   976  C CA  . ASN A 1 139 ? 22.480 21.081 35.371 1.00 14.40 ? 169 ASN A CA  1 
ATOM   977  C C   . ASN A 1 139 ? 23.286 22.160 36.084 1.00 14.03 ? 169 ASN A C   1 
ATOM   978  O O   . ASN A 1 139 ? 24.005 21.890 37.049 1.00 14.95 ? 169 ASN A O   1 
ATOM   979  C CB  . ASN A 1 139 ? 21.119 20.943 36.057 1.00 15.01 ? 169 ASN A CB  1 
ATOM   980  C CG  . ASN A 1 139 ? 20.306 19.791 35.525 1.00 18.05 ? 169 ASN A CG  1 
ATOM   981  O OD1 . ASN A 1 139 ? 20.510 19.328 34.400 1.00 13.87 ? 169 ASN A OD1 1 
ATOM   982  N ND2 . ASN A 1 139 ? 19.365 19.316 36.339 1.00 18.64 ? 169 ASN A ND2 1 
ATOM   983  N N   . TYR A 1 140 ? 23.150 23.394 35.602 1.00 13.24 ? 170 TYR A N   1 
ATOM   984  C CA  . TYR A 1 140 ? 23.735 24.562 36.241 1.00 14.07 ? 170 TYR A CA  1 
ATOM   985  C C   . TYR A 1 140 ? 22.697 25.675 36.283 1.00 16.42 ? 170 TYR A C   1 
ATOM   986  O O   . TYR A 1 140 ? 21.754 25.701 35.489 1.00 13.36 ? 170 TYR A O   1 
ATOM   987  C CB  . TYR A 1 140 ? 24.995 25.040 35.509 1.00 13.15 ? 170 TYR A CB  1 
ATOM   988  C CG  . TYR A 1 140 ? 24.785 25.378 34.042 1.00 17.66 ? 170 TYR A CG  1 
ATOM   989  C CD1 . TYR A 1 140 ? 24.850 24.393 33.062 1.00 16.44 ? 170 TYR A CD1 1 
ATOM   990  C CD2 . TYR A 1 140 ? 24.542 26.685 33.637 1.00 17.51 ? 170 TYR A CD2 1 
ATOM   991  C CE1 . TYR A 1 140 ? 24.671 24.696 31.728 1.00 14.90 ? 170 TYR A CE1 1 
ATOM   992  C CE2 . TYR A 1 140 ? 24.358 27.000 32.297 1.00 15.65 ? 170 TYR A CE2 1 
ATOM   993  C CZ  . TYR A 1 140 ? 24.423 26.000 31.348 1.00 16.83 ? 170 TYR A CZ  1 
ATOM   994  O OH  . TYR A 1 140 ? 24.247 26.303 30.012 1.00 18.00 ? 170 TYR A OH  1 
ATOM   995  N N   . ARG A 1 141 ? 22.868 26.594 37.229 1.00 13.74 ? 171 ARG A N   1 
ATOM   996  C CA  . ARG A 1 141 ? 21.925 27.696 37.349 1.00 15.27 ? 171 ARG A CA  1 
ATOM   997  C C   . ARG A 1 141 ? 22.016 28.601 36.129 1.00 18.79 ? 171 ARG A C   1 
ATOM   998  O O   . ARG A 1 141 ? 23.094 28.817 35.569 1.00 16.20 ? 171 ARG A O   1 
ATOM   999  C CB  . ARG A 1 141 ? 22.184 28.496 38.619 1.00 13.69 ? 171 ARG A CB  1 
ATOM   1000 C CG  . ARG A 1 141 ? 21.775 27.787 39.884 1.00 13.80 ? 171 ARG A CG  1 
ATOM   1001 C CD  . ARG A 1 141 ? 22.229 28.566 41.106 1.00 13.99 ? 171 ARG A CD  1 
ATOM   1002 N NE  . ARG A 1 141 ? 23.656 28.408 41.360 1.00 13.93 ? 171 ARG A NE  1 
ATOM   1003 C CZ  . ARG A 1 141 ? 24.316 29.040 42.321 1.00 16.75 ? 171 ARG A CZ  1 
ATOM   1004 N NH1 . ARG A 1 141 ? 23.714 29.915 43.110 1.00 14.39 ? 171 ARG A NH1 1 
ATOM   1005 N NH2 . ARG A 1 141 ? 25.612 28.788 42.494 1.00 16.87 ? 171 ARG A NH2 1 
ATOM   1006 N N   . THR A 1 142 ? 20.871 29.130 35.713 1.00 15.99 ? 172 THR A N   1 
ATOM   1007 C CA  . THR A 1 142 ? 20.805 29.957 34.519 1.00 18.18 ? 172 THR A CA  1 
ATOM   1008 C C   . THR A 1 142 ? 19.752 31.041 34.731 1.00 17.52 ? 172 THR A C   1 
ATOM   1009 O O   . THR A 1 142 ? 19.111 31.116 35.783 1.00 18.07 ? 172 THR A O   1 
ATOM   1010 C CB  . THR A 1 142 ? 20.506 29.101 33.285 1.00 22.07 ? 172 THR A CB  1 
ATOM   1011 O OG1 . THR A 1 142 ? 20.841 29.832 32.101 1.00 22.83 ? 172 THR A OG1 1 
ATOM   1012 C CG2 . THR A 1 142 ? 19.023 28.716 33.246 1.00 14.61 ? 172 THR A CG2 1 
ATOM   1013 N N   . ASN A 1 143 ? 19.591 31.893 33.723 1.00 18.37 ? 173 ASN A N   1 
ATOM   1014 C CA  . ASN A 1 143 ? 18.635 33.007 33.767 1.00 15.67 ? 173 ASN A CA  1 
ATOM   1015 C C   . ASN A 1 143 ? 18.991 33.886 34.974 1.00 18.12 ? 173 ASN A C   1 
ATOM   1016 O O   . ASN A 1 143 ? 20.159 33.955 35.381 1.00 18.15 ? 173 ASN A O   1 
ATOM   1017 C CB  . ASN A 1 143 ? 17.216 32.461 33.760 1.00 14.57 ? 173 ASN A CB  1 
ATOM   1018 C CG  . ASN A 1 143 ? 16.212 33.456 33.227 1.00 19.71 ? 173 ASN A CG  1 
ATOM   1019 O OD1 . ASN A 1 143 ? 16.078 34.564 33.747 1.00 22.58 ? 173 ASN A OD1 1 
ATOM   1020 N ND2 . ASN A 1 143 ? 15.508 33.073 32.170 1.00 16.64 ? 173 ASN A ND2 1 
ATOM   1021 N N   . ILE A 1 144 ? 18.002 34.558 35.569 1.00 15.00 ? 174 ILE A N   1 
ATOM   1022 C CA  . ILE A 1 144 ? 18.294 35.493 36.648 1.00 16.11 ? 174 ILE A CA  1 
ATOM   1023 C C   . ILE A 1 144 ? 18.844 34.789 37.882 1.00 14.90 ? 174 ILE A C   1 
ATOM   1024 O O   . ILE A 1 144 ? 19.569 35.408 38.665 1.00 18.02 ? 174 ILE A O   1 
ATOM   1025 C CB  . ILE A 1 144 ? 17.044 36.327 36.999 1.00 18.63 ? 174 ILE A CB  1 
ATOM   1026 C CG1 . ILE A 1 144 ? 17.422 37.490 37.921 1.00 17.43 ? 174 ILE A CG1 1 
ATOM   1027 C CG2 . ILE A 1 144 ? 15.966 35.460 37.645 1.00 15.51 ? 174 ILE A CG2 1 
ATOM   1028 C CD1 . ILE A 1 144 ? 16.259 38.366 38.320 1.00 17.40 ? 174 ILE A CD1 1 
ATOM   1029 N N   . LEU A 1 145 ? 18.551 33.501 38.067 1.00 14.71 ? 175 LEU A N   1 
ATOM   1030 C CA  . LEU A 1 145 ? 19.062 32.788 39.229 1.00 17.84 ? 175 LEU A CA  1 
ATOM   1031 C C   . LEU A 1 145 ? 20.512 32.356 39.065 1.00 17.51 ? 175 LEU A C   1 
ATOM   1032 O O   . LEU A 1 145 ? 21.182 32.092 40.069 1.00 15.29 ? 175 LEU A O   1 
ATOM   1033 C CB  . LEU A 1 145 ? 18.181 31.573 39.523 1.00 19.20 ? 175 LEU A CB  1 
ATOM   1034 C CG  . LEU A 1 145 ? 16.754 31.964 39.914 1.00 21.55 ? 175 LEU A CG  1 
ATOM   1035 C CD1 . LEU A 1 145 ? 15.835 30.753 39.951 1.00 18.95 ? 175 LEU A CD1 1 
ATOM   1036 C CD2 . LEU A 1 145 ? 16.757 32.693 41.254 1.00 17.41 ? 175 LEU A CD2 1 
ATOM   1037 N N   . GLY A 1 146 ? 21.013 32.282 37.836 1.00 15.42 ? 176 GLY A N   1 
ATOM   1038 C CA  . GLY A 1 146 ? 22.395 31.907 37.619 1.00 14.93 ? 176 GLY A CA  1 
ATOM   1039 C C   . GLY A 1 146 ? 23.285 33.069 37.233 1.00 15.45 ? 176 GLY A C   1 
ATOM   1040 O O   . GLY A 1 146 ? 24.512 32.983 37.341 1.00 16.60 ? 176 GLY A O   1 
ATOM   1041 N N   . PHE A 1 147 ? 22.678 34.165 36.779 1.00 15.85 ? 177 PHE A N   1 
ATOM   1042 C CA  . PHE A 1 147 ? 23.428 35.309 36.256 1.00 19.19 ? 177 PHE A CA  1 
ATOM   1043 C C   . PHE A 1 147 ? 22.716 36.586 36.692 1.00 22.49 ? 177 PHE A C   1 
ATOM   1044 O O   . PHE A 1 147 ? 21.738 37.011 36.067 1.00 18.65 ? 177 PHE A O   1 
ATOM   1045 C CB  . PHE A 1 147 ? 23.562 35.215 34.742 1.00 15.95 ? 177 PHE A CB  1 
ATOM   1046 C CG  . PHE A 1 147 ? 24.259 33.963 34.291 1.00 18.41 ? 177 PHE A CG  1 
ATOM   1047 C CD1 . PHE A 1 147 ? 25.642 33.898 34.268 1.00 18.70 ? 177 PHE A CD1 1 
ATOM   1048 C CD2 . PHE A 1 147 ? 23.532 32.840 33.931 1.00 19.25 ? 177 PHE A CD2 1 
ATOM   1049 C CE1 . PHE A 1 147 ? 26.289 32.745 33.872 1.00 16.76 ? 177 PHE A CE1 1 
ATOM   1050 C CE2 . PHE A 1 147 ? 24.175 31.684 33.533 1.00 20.25 ? 177 PHE A CE2 1 
ATOM   1051 C CZ  . PHE A 1 147 ? 25.556 31.638 33.505 1.00 17.03 ? 177 PHE A CZ  1 
ATOM   1052 N N   . PHE A 1 148 ? 23.212 37.188 37.772 1.00 15.53 ? 178 PHE A N   1 
ATOM   1053 C CA  . PHE A 1 148 ? 22.572 38.342 38.388 1.00 18.38 ? 178 PHE A CA  1 
ATOM   1054 C C   . PHE A 1 148 ? 23.580 39.008 39.310 1.00 17.47 ? 178 PHE A C   1 
ATOM   1055 O O   . PHE A 1 148 ? 24.251 38.325 40.090 1.00 17.59 ? 178 PHE A O   1 
ATOM   1056 C CB  . PHE A 1 148 ? 21.317 37.920 39.167 1.00 16.13 ? 178 PHE A CB  1 
ATOM   1057 C CG  . PHE A 1 148 ? 20.615 39.054 39.870 1.00 18.82 ? 178 PHE A CG  1 
ATOM   1058 C CD1 . PHE A 1 148 ? 19.878 39.987 39.154 1.00 16.20 ? 178 PHE A CD1 1 
ATOM   1059 C CD2 . PHE A 1 148 ? 20.668 39.168 41.254 1.00 17.45 ? 178 PHE A CD2 1 
ATOM   1060 C CE1 . PHE A 1 148 ? 19.224 41.023 39.801 1.00 20.27 ? 178 PHE A CE1 1 
ATOM   1061 C CE2 . PHE A 1 148 ? 20.010 40.206 41.910 1.00 19.93 ? 178 PHE A CE2 1 
ATOM   1062 C CZ  . PHE A 1 148 ? 19.287 41.132 41.180 1.00 18.68 ? 178 PHE A CZ  1 
ATOM   1063 N N   . ALA A 1 149 ? 23.686 40.329 39.216 1.00 16.52 ? 179 ALA A N   1 
ATOM   1064 C CA  . ALA A 1 149 ? 24.586 41.104 40.053 1.00 19.48 ? 179 ALA A CA  1 
ATOM   1065 C C   . ALA A 1 149 ? 23.792 42.121 40.862 1.00 19.03 ? 179 ALA A C   1 
ATOM   1066 O O   . ALA A 1 149 ? 22.748 42.613 40.420 1.00 22.07 ? 179 ALA A O   1 
ATOM   1067 C CB  . ALA A 1 149 ? 25.653 41.812 39.212 1.00 17.68 ? 179 ALA A CB  1 
ATOM   1068 N N   . HIS A 1 150 ? 24.299 42.431 42.058 1.00 22.27 ? 180 HIS A N   1 
ATOM   1069 C CA  . HIS A 1 150 ? 23.612 43.325 42.981 1.00 23.76 ? 180 HIS A CA  1 
ATOM   1070 C C   . HIS A 1 150 ? 24.633 43.900 43.947 1.00 20.38 ? 180 HIS A C   1 
ATOM   1071 O O   . HIS A 1 150 ? 25.553 43.175 44.349 1.00 21.12 ? 180 HIS A O   1 
ATOM   1072 C CB  . HIS A 1 150 ? 22.514 42.582 43.749 1.00 17.69 ? 180 HIS A CB  1 
ATOM   1073 C CG  . HIS A 1 150 ? 21.537 43.484 44.434 1.00 21.86 ? 180 HIS A CG  1 
ATOM   1074 N ND1 . HIS A 1 150 ? 21.801 44.085 45.647 1.00 23.32 ? 180 HIS A ND1 1 
ATOM   1075 C CD2 . HIS A 1 150 ? 20.292 43.881 44.080 1.00 18.37 ? 180 HIS A CD2 1 
ATOM   1076 C CE1 . HIS A 1 150 ? 20.760 44.813 46.011 1.00 23.15 ? 180 HIS A CE1 1 
ATOM   1077 N NE2 . HIS A 1 150 ? 19.832 44.708 45.077 1.00 20.29 ? 180 HIS A NE2 1 
ATOM   1078 N N   . PRO A 1 151 ? 24.520 45.177 44.329 1.00 20.32 ? 181 PRO A N   1 
ATOM   1079 C CA  . PRO A 1 151 ? 25.497 45.740 45.281 1.00 25.62 ? 181 PRO A CA  1 
ATOM   1080 C C   . PRO A 1 151 ? 25.572 44.996 46.608 1.00 23.89 ? 181 PRO A C   1 
ATOM   1081 O O   . PRO A 1 151 ? 26.667 44.853 47.165 1.00 23.72 ? 181 PRO A O   1 
ATOM   1082 C CB  . PRO A 1 151 ? 25.016 47.190 45.462 1.00 25.14 ? 181 PRO A CB  1 
ATOM   1083 C CG  . PRO A 1 151 ? 23.618 47.223 44.911 1.00 23.77 ? 181 PRO A CG  1 
ATOM   1084 C CD  . PRO A 1 151 ? 23.591 46.200 43.825 1.00 25.12 ? 181 PRO A CD  1 
ATOM   1085 N N   . GLY A 1 152 ? 24.444 44.514 47.133 1.00 19.84 ? 182 GLY A N   1 
ATOM   1086 C CA  . GLY A 1 152 ? 24.485 43.740 48.365 1.00 22.63 ? 182 GLY A CA  1 
ATOM   1087 C C   . GLY A 1 152 ? 25.156 42.393 48.182 1.00 22.28 ? 182 GLY A C   1 
ATOM   1088 O O   . GLY A 1 152 ? 25.822 41.890 49.096 1.00 18.84 ? 182 GLY A O   1 
ATOM   1089 N N   . LEU A 1 153 ? 24.993 41.792 47.000 1.00 18.14 ? 183 LEU A N   1 
ATOM   1090 C CA  . LEU A 1 153 ? 25.668 40.532 46.714 1.00 18.15 ? 183 LEU A CA  1 
ATOM   1091 C C   . LEU A 1 153 ? 27.176 40.727 46.640 1.00 21.07 ? 183 LEU A C   1 
ATOM   1092 O O   . LEU A 1 153 ? 27.941 39.892 47.138 1.00 20.11 ? 183 LEU A O   1 
ATOM   1093 C CB  . LEU A 1 153 ? 25.131 39.934 45.416 1.00 18.55 ? 183 LEU A CB  1 
ATOM   1094 C CG  . LEU A 1 153 ? 23.705 39.391 45.494 1.00 21.97 ? 183 LEU A CG  1 
ATOM   1095 C CD1 . LEU A 1 153 ? 23.216 38.991 44.115 1.00 21.14 ? 183 LEU A CD1 1 
ATOM   1096 C CD2 . LEU A 1 153 ? 23.640 38.211 46.459 1.00 16.86 ? 183 LEU A CD2 1 
ATOM   1097 N N   . SER A 1 154 ? 27.621 41.824 46.023 1.00 18.10 ? 184 SER A N   1 
ATOM   1098 C CA  . SER A 1 154 ? 29.046 42.132 46.016 1.00 21.86 ? 184 SER A CA  1 
ATOM   1099 C C   . SER A 1 154 ? 29.546 42.430 47.423 1.00 22.93 ? 184 SER A C   1 
ATOM   1100 O O   . SER A 1 154 ? 30.667 42.051 47.782 1.00 20.26 ? 184 SER A O   1 
ATOM   1101 C CB  . SER A 1 154 ? 29.325 43.310 45.085 1.00 18.44 ? 184 SER A CB  1 
ATOM   1102 O OG  . SER A 1 154 ? 29.055 42.963 43.740 1.00 23.05 ? 184 SER A OG  1 
ATOM   1103 N N   . ARG A 1 155 ? 28.719 43.087 48.241 1.00 19.18 ? 185 ARG A N   1 
ATOM   1104 C CA  . ARG A 1 155 ? 29.134 43.413 49.602 1.00 24.87 ? 185 ARG A CA  1 
ATOM   1105 C C   . ARG A 1 155 ? 29.347 42.154 50.437 1.00 22.92 ? 185 ARG A C   1 
ATOM   1106 O O   . ARG A 1 155 ? 30.338 42.047 51.168 1.00 21.91 ? 185 ARG A O   1 
ATOM   1107 C CB  . ARG A 1 155 ? 28.100 44.329 50.255 1.00 29.90 ? 185 ARG A CB  1 
ATOM   1108 C CG  . ARG A 1 155 ? 28.546 44.930 51.582 1.00 39.89 ? 185 ARG A CG  1 
ATOM   1109 C CD  . ARG A 1 155 ? 27.543 45.961 52.090 1.00 39.67 ? 185 ARG A CD  1 
ATOM   1110 N NE  . ARG A 1 155 ? 26.911 46.696 50.999 1.00 50.95 ? 185 ARG A NE  1 
ATOM   1111 C CZ  . ARG A 1 155 ? 25.614 46.660 50.720 1.00 54.80 ? 185 ARG A CZ  1 
ATOM   1112 N NH1 . ARG A 1 155 ? 24.764 45.973 51.467 1.00 44.22 ? 185 ARG A NH1 1 
ATOM   1113 N NH2 . ARG A 1 155 ? 25.156 47.334 49.668 1.00 43.06 ? 185 ARG A NH2 1 
ATOM   1114 N N   . GLU A 1 156 ? 28.439 41.183 50.337 1.00 23.28 ? 186 GLU A N   1 
ATOM   1115 C CA  . GLU A 1 156 ? 28.563 39.982 51.157 1.00 25.80 ? 186 GLU A CA  1 
ATOM   1116 C C   . GLU A 1 156 ? 29.616 39.003 50.647 1.00 26.63 ? 186 GLU A C   1 
ATOM   1117 O O   . GLU A 1 156 ? 29.943 38.048 51.359 1.00 30.32 ? 186 GLU A O   1 
ATOM   1118 C CB  . GLU A 1 156 ? 27.215 39.268 51.246 1.00 25.57 ? 186 GLU A CB  1 
ATOM   1119 C CG  . GLU A 1 156 ? 26.734 38.707 49.921 1.00 21.69 ? 186 GLU A CG  1 
ATOM   1120 C CD  . GLU A 1 156 ? 25.405 37.987 50.042 1.00 21.00 ? 186 GLU A CD  1 
ATOM   1121 O OE1 . GLU A 1 156 ? 24.645 38.292 50.986 1.00 21.78 ? 186 GLU A OE1 1 
ATOM   1122 O OE2 . GLU A 1 156 ? 25.125 37.112 49.194 1.00 24.15 ? 186 GLU A OE2 1 
ATOM   1123 N N   . SER A 1 157 ? 30.159 39.226 49.460 1.00 20.24 ? 187 SER A N   1 
ATOM   1124 C CA  . SER A 1 157 ? 30.971 38.249 48.749 1.00 24.60 ? 187 SER A CA  1 
ATOM   1125 C C   . SER A 1 157 ? 32.391 38.194 49.311 1.00 26.22 ? 187 SER A C   1 
ATOM   1126 O O   . SER A 1 157 ? 32.965 39.232 49.653 1.00 22.92 ? 187 SER A O   1 
ATOM   1127 C CB  . SER A 1 157 ? 31.029 38.594 47.264 1.00 19.61 ? 187 SER A CB  1 
ATOM   1128 O OG  . SER A 1 157 ? 31.989 37.796 46.599 1.00 21.95 ? 187 SER A OG  1 
ATOM   1129 N N   . PRO A 1 158 ? 32.983 36.998 49.393 1.00 25.78 ? 188 PRO A N   1 
ATOM   1130 C CA  . PRO A 1 158 ? 34.401 36.907 49.781 1.00 28.29 ? 188 PRO A CA  1 
ATOM   1131 C C   . PRO A 1 158 ? 35.333 37.573 48.788 1.00 30.67 ? 188 PRO A C   1 
ATOM   1132 O O   . PRO A 1 158 ? 36.415 38.030 49.176 1.00 30.91 ? 188 PRO A O   1 
ATOM   1133 C CB  . PRO A 1 158 ? 34.649 35.393 49.855 1.00 26.32 ? 188 PRO A CB  1 
ATOM   1134 C CG  . PRO A 1 158 ? 33.289 34.780 49.996 1.00 28.38 ? 188 PRO A CG  1 
ATOM   1135 C CD  . PRO A 1 158 ? 32.363 35.673 49.233 1.00 22.92 ? 188 PRO A CD  1 
ATOM   1136 N N   . THR A 1 159 ? 34.949 37.637 47.515 1.00 28.05 ? 189 THR A N   1 
ATOM   1137 C CA  . THR A 1 159 ? 35.740 38.297 46.488 1.00 24.22 ? 189 THR A CA  1 
ATOM   1138 C C   . THR A 1 159 ? 35.252 39.706 46.183 1.00 27.02 ? 189 THR A C   1 
ATOM   1139 O O   . THR A 1 159 ? 35.827 40.372 45.316 1.00 23.15 ? 189 THR A O   1 
ATOM   1140 C CB  . THR A 1 159 ? 35.735 37.463 45.201 1.00 31.17 ? 189 THR A CB  1 
ATOM   1141 O OG1 . THR A 1 159 ? 34.400 37.376 44.688 1.00 27.21 ? 189 THR A OG1 1 
ATOM   1142 C CG2 . THR A 1 159 ? 36.254 36.059 45.475 1.00 28.96 ? 189 THR A CG2 1 
ATOM   1143 N N   . GLY A 1 160 ? 34.214 40.177 46.874 1.00 26.07 ? 190 GLY A N   1 
ATOM   1144 C CA  . GLY A 1 160 ? 33.662 41.489 46.599 1.00 19.92 ? 190 GLY A CA  1 
ATOM   1145 C C   . GLY A 1 160 ? 32.974 41.623 45.259 1.00 23.68 ? 190 GLY A C   1 
ATOM   1146 O O   . GLY A 1 160 ? 32.728 42.744 44.806 1.00 24.84 ? 190 GLY A O   1 
ATOM   1147 N N   . THR A 1 161 ? 32.650 40.511 44.610 1.00 19.47 ? 191 THR A N   1 
ATOM   1148 C CA  . THR A 1 161 ? 32.043 40.508 43.286 1.00 21.63 ? 191 THR A CA  1 
ATOM   1149 C C   . THR A 1 161 ? 30.691 39.804 43.347 1.00 19.53 ? 191 THR A C   1 
ATOM   1150 O O   . THR A 1 161 ? 30.286 39.284 44.385 1.00 19.04 ? 191 THR A O   1 
ATOM   1151 C CB  . THR A 1 161 ? 32.967 39.831 42.268 1.00 22.35 ? 191 THR A CB  1 
ATOM   1152 O OG1 . THR A 1 161 ? 33.088 38.438 42.585 1.00 23.78 ? 191 THR A OG1 1 
ATOM   1153 C CG2 . THR A 1 161 ? 34.353 40.467 42.308 1.00 19.70 ? 191 THR A CG2 1 
ATOM   1154 N N   . SER A 1 162 ? 29.984 39.793 42.219 1.00 20.86 ? 192 SER A N   1 
ATOM   1155 C CA  . SER A 1 162 ? 28.715 39.085 42.127 1.00 17.28 ? 192 SER A CA  1 
ATOM   1156 C C   . SER A 1 162 ? 28.469 38.701 40.674 1.00 20.16 ? 192 SER A C   1 
ATOM   1157 O O   . SER A 1 162 ? 29.215 39.088 39.771 1.00 21.16 ? 192 SER A O   1 
ATOM   1158 C CB  . SER A 1 162 ? 27.557 39.919 42.693 1.00 17.59 ? 192 SER A CB  1 
ATOM   1159 O OG  . SER A 1 162 ? 27.510 41.217 42.126 1.00 22.71 ? 192 SER A OG  1 
ATOM   1160 N N   . GLY A 1 163 ? 27.411 37.919 40.461 1.00 17.38 ? 193 GLY A N   1 
ATOM   1161 C CA  . GLY A 1 163 ? 27.098 37.399 39.146 1.00 16.09 ? 193 GLY A CA  1 
ATOM   1162 C C   . GLY A 1 163 ? 27.854 36.122 38.831 1.00 18.34 ? 193 GLY A C   1 
ATOM   1163 O O   . GLY A 1 163 ? 28.669 35.624 39.612 1.00 16.86 ? 193 GLY A O   1 
ATOM   1164 N N   . ASN A 1 164 ? 27.548 35.576 37.648 1.00 19.18 ? 194 ASN A N   1 
ATOM   1165 C CA  . ASN A 1 164 ? 28.271 34.445 37.054 1.00 17.21 ? 194 ASN A CA  1 
ATOM   1166 C C   . ASN A 1 164 ? 28.140 33.161 37.870 1.00 15.69 ? 194 ASN A C   1 
ATOM   1167 O O   . ASN A 1 164 ? 29.028 32.305 37.838 1.00 13.99 ? 194 ASN A O   1 
ATOM   1168 C CB  . ASN A 1 164 ? 29.749 34.781 36.838 1.00 14.37 ? 194 ASN A CB  1 
ATOM   1169 C CG  . ASN A 1 164 ? 29.959 35.798 35.740 1.00 16.90 ? 194 ASN A CG  1 
ATOM   1170 O OD1 . ASN A 1 164 ? 29.054 36.076 34.957 1.00 15.42 ? 194 ASN A OD1 1 
ATOM   1171 N ND2 . ASN A 1 164 ? 31.165 36.358 35.674 1.00 20.42 ? 194 ASN A ND2 1 
ATOM   1172 N N   . TYR A 1 165 ? 27.023 32.994 38.584 1.00 17.23 ? 195 TYR A N   1 
ATOM   1173 C CA  . TYR A 1 165 ? 26.861 31.799 39.407 1.00 14.03 ? 195 TYR A CA  1 
ATOM   1174 C C   . TYR A 1 165 ? 26.751 30.536 38.558 1.00 16.47 ? 195 TYR A C   1 
ATOM   1175 O O   . TYR A 1 165 ? 27.227 29.474 38.974 1.00 15.25 ? 195 TYR A O   1 
ATOM   1176 C CB  . TYR A 1 165 ? 25.660 31.977 40.338 1.00 14.18 ? 195 TYR A CB  1 
ATOM   1177 C CG  . TYR A 1 165 ? 25.794 33.259 41.134 1.00 17.67 ? 195 TYR A CG  1 
ATOM   1178 C CD1 . TYR A 1 165 ? 26.689 33.347 42.199 1.00 14.73 ? 195 TYR A CD1 1 
ATOM   1179 C CD2 . TYR A 1 165 ? 25.070 34.397 40.789 1.00 15.45 ? 195 TYR A CD2 1 
ATOM   1180 C CE1 . TYR A 1 165 ? 26.843 34.520 42.909 1.00 15.11 ? 195 TYR A CE1 1 
ATOM   1181 C CE2 . TYR A 1 165 ? 25.214 35.578 41.498 1.00 15.05 ? 195 TYR A CE2 1 
ATOM   1182 C CZ  . TYR A 1 165 ? 26.103 35.633 42.557 1.00 15.97 ? 195 TYR A CZ  1 
ATOM   1183 O OH  . TYR A 1 165 ? 26.252 36.801 43.266 1.00 15.69 ? 195 TYR A OH  1 
ATOM   1184 N N   . GLY A 1 166 ? 26.179 30.634 37.355 1.00 16.12 ? 196 GLY A N   1 
ATOM   1185 C CA  . GLY A 1 166 ? 26.150 29.479 36.467 1.00 14.05 ? 196 GLY A CA  1 
ATOM   1186 C C   . GLY A 1 166 ? 27.536 28.997 36.069 1.00 13.37 ? 196 GLY A C   1 
ATOM   1187 O O   . GLY A 1 166 ? 27.790 27.789 35.997 1.00 15.44 ? 196 GLY A O   1 
ATOM   1188 N N   . LEU A 1 167 ? 28.452 29.932 35.804 1.00 15.74 ? 197 LEU A N   1 
ATOM   1189 C CA  . LEU A 1 167 ? 29.824 29.545 35.488 1.00 15.55 ? 197 LEU A CA  1 
ATOM   1190 C C   . LEU A 1 167 ? 30.482 28.859 36.678 1.00 13.58 ? 197 LEU A C   1 
ATOM   1191 O O   . LEU A 1 167 ? 31.188 27.852 36.517 1.00 15.32 ? 197 LEU A O   1 
ATOM   1192 C CB  . LEU A 1 167 ? 30.629 30.770 35.060 1.00 13.65 ? 197 LEU A CB  1 
ATOM   1193 C CG  . LEU A 1 167 ? 30.166 31.457 33.774 1.00 14.44 ? 197 LEU A CG  1 
ATOM   1194 C CD1 . LEU A 1 167 ? 31.078 32.640 33.460 1.00 15.67 ? 197 LEU A CD1 1 
ATOM   1195 C CD2 . LEU A 1 167 ? 30.152 30.474 32.614 1.00 14.59 ? 197 LEU A CD2 1 
ATOM   1196 N N   . LEU A 1 168 ? 30.260 29.392 37.883 1.00 14.19 ? 198 LEU A N   1 
ATOM   1197 C CA  . LEU A 1 168 ? 30.768 28.737 39.081 1.00 15.12 ? 198 LEU A CA  1 
ATOM   1198 C C   . LEU A 1 168 ? 30.185 27.339 39.232 1.00 13.68 ? 198 LEU A C   1 
ATOM   1199 O O   . LEU A 1 168 ? 30.870 26.432 39.709 1.00 15.58 ? 198 LEU A O   1 
ATOM   1200 C CB  . LEU A 1 168 ? 30.467 29.590 40.318 1.00 14.06 ? 198 LEU A CB  1 
ATOM   1201 C CG  . LEU A 1 168 ? 31.251 30.902 40.432 1.00 14.87 ? 198 LEU A CG  1 
ATOM   1202 C CD1 . LEU A 1 168 ? 30.718 31.792 41.550 1.00 14.59 ? 198 LEU A CD1 1 
ATOM   1203 C CD2 . LEU A 1 168 ? 32.732 30.615 40.645 1.00 14.49 ? 198 LEU A CD2 1 
ATOM   1204 N N   . ASP A 1 169 ? 28.933 27.138 38.815 1.00 15.86 ? 199 ASP A N   1 
ATOM   1205 C CA  . ASP A 1 169 ? 28.348 25.800 38.873 1.00 18.31 ? 199 ASP A CA  1 
ATOM   1206 C C   . ASP A 1 169 ? 29.034 24.855 37.886 1.00 17.95 ? 199 ASP A C   1 
ATOM   1207 O O   . ASP A 1 169 ? 29.293 23.688 38.212 1.00 15.28 ? 199 ASP A O   1 
ATOM   1208 C CB  . ASP A 1 169 ? 26.842 25.868 38.600 1.00 13.37 ? 199 ASP A CB  1 
ATOM   1209 C CG  . ASP A 1 169 ? 26.074 26.604 39.683 1.00 15.33 ? 199 ASP A CG  1 
ATOM   1210 O OD1 . ASP A 1 169 ? 26.607 26.772 40.798 1.00 14.11 ? 199 ASP A OD1 1 
ATOM   1211 O OD2 . ASP A 1 169 ? 24.924 27.007 39.417 1.00 14.95 ? 199 ASP A OD2 1 
ATOM   1212 N N   . ILE A 1 170 ? 29.314 25.336 36.669 1.00 14.14 ? 200 ILE A N   1 
ATOM   1213 C CA  . ILE A 1 170 ? 30.097 24.545 35.715 1.00 14.10 ? 200 ILE A CA  1 
ATOM   1214 C C   . ILE A 1 170 ? 31.408 24.103 36.354 1.00 15.40 ? 200 ILE A C   1 
ATOM   1215 O O   . ILE A 1 170 ? 31.801 22.927 36.294 1.00 13.84 ? 200 ILE A O   1 
ATOM   1216 C CB  . ILE A 1 170 ? 30.363 25.352 34.430 1.00 16.93 ? 200 ILE A CB  1 
ATOM   1217 C CG1 . ILE A 1 170 ? 29.080 25.977 33.884 1.00 17.12 ? 200 ILE A CG1 1 
ATOM   1218 C CG2 . ILE A 1 170 ? 31.033 24.475 33.375 1.00 18.11 ? 200 ILE A CG2 1 
ATOM   1219 C CD1 . ILE A 1 170 ? 28.218 25.039 33.140 1.00 20.24 ? 200 ILE A CD1 1 
ATOM   1220 N N   . LEU A 1 171 ? 32.106 25.057 36.975 1.00 16.01 ? 201 LEU A N   1 
ATOM   1221 C CA  . LEU A 1 171 ? 33.388 24.752 37.603 1.00 15.41 ? 201 LEU A CA  1 
ATOM   1222 C C   . LEU A 1 171 ? 33.224 23.756 38.750 1.00 17.14 ? 201 LEU A C   1 
ATOM   1223 O O   . LEU A 1 171 ? 34.060 22.861 38.927 1.00 15.58 ? 201 LEU A O   1 
ATOM   1224 C CB  . LEU A 1 171 ? 34.047 26.047 38.082 1.00 15.43 ? 201 LEU A CB  1 
ATOM   1225 C CG  . LEU A 1 171 ? 34.391 27.009 36.937 1.00 17.19 ? 201 LEU A CG  1 
ATOM   1226 C CD1 . LEU A 1 171 ? 34.618 28.432 37.435 1.00 19.51 ? 201 LEU A CD1 1 
ATOM   1227 C CD2 . LEU A 1 171 ? 35.607 26.514 36.170 1.00 14.24 ? 201 LEU A CD2 1 
ATOM   1228 N N   . ALA A 1 172 ? 32.152 23.890 39.537 1.00 14.67 ? 202 ALA A N   1 
ATOM   1229 C CA  . ALA A 1 172 ? 31.920 22.947 40.630 1.00 15.96 ? 202 ALA A CA  1 
ATOM   1230 C C   . ALA A 1 172 ? 31.672 21.540 40.099 1.00 16.64 ? 202 ALA A C   1 
ATOM   1231 O O   . ALA A 1 172 ? 32.137 20.556 40.685 1.00 16.26 ? 202 ALA A O   1 
ATOM   1232 C CB  . ALA A 1 172 ? 30.745 23.410 41.494 1.00 15.18 ? 202 ALA A CB  1 
ATOM   1233 N N   . ALA A 1 173 ? 30.935 21.424 38.991 1.00 17.14 ? 203 ALA A N   1 
ATOM   1234 C CA  . ALA A 1 173 ? 30.721 20.111 38.391 1.00 14.87 ? 203 ALA A CA  1 
ATOM   1235 C C   . ALA A 1 173 ? 32.038 19.516 37.907 1.00 16.21 ? 203 ALA A C   1 
ATOM   1236 O O   . ALA A 1 173 ? 32.292 18.313 38.072 1.00 13.91 ? 203 ALA A O   1 
ATOM   1237 C CB  . ALA A 1 173 ? 29.717 20.213 37.245 1.00 13.45 ? 203 ALA A CB  1 
ATOM   1238 N N   . LEU A 1 174 ? 32.900 20.352 37.324 1.00 15.76 ? 204 LEU A N   1 
ATOM   1239 C CA  . LEU A 1 174 ? 34.208 19.866 36.889 1.00 17.85 ? 204 LEU A CA  1 
ATOM   1240 C C   . LEU A 1 174 ? 35.061 19.413 38.078 1.00 16.94 ? 204 LEU A C   1 
ATOM   1241 O O   . LEU A 1 174 ? 35.800 18.424 37.984 1.00 16.44 ? 204 LEU A O   1 
ATOM   1242 C CB  . LEU A 1 174 ? 34.916 20.949 36.071 1.00 13.92 ? 204 LEU A CB  1 
ATOM   1243 C CG  . LEU A 1 174 ? 34.285 21.188 34.691 1.00 16.79 ? 204 LEU A CG  1 
ATOM   1244 C CD1 . LEU A 1 174 ? 34.762 22.486 34.052 1.00 13.73 ? 204 LEU A CD1 1 
ATOM   1245 C CD2 . LEU A 1 174 ? 34.555 20.011 33.758 1.00 13.83 ? 204 LEU A CD2 1 
ATOM   1246 N N   . ARG A 1 175 ? 34.960 20.114 39.211 1.00 15.72 ? 205 ARG A N   1 
ATOM   1247 C CA  . ARG A 1 175 ? 35.682 19.689 40.412 1.00 19.48 ? 205 ARG A CA  1 
ATOM   1248 C C   . ARG A 1 175 ? 35.135 18.368 40.948 1.00 18.18 ? 205 ARG A C   1 
ATOM   1249 O O   . ARG A 1 175 ? 35.905 17.496 41.378 1.00 17.05 ? 205 ARG A O   1 
ATOM   1250 C CB  . ARG A 1 175 ? 35.620 20.790 41.475 1.00 19.76 ? 205 ARG A CB  1 
ATOM   1251 C CG  . ARG A 1 175 ? 35.853 20.355 42.933 1.00 33.63 ? 205 ARG A CG  1 
ATOM   1252 C CD  . ARG A 1 175 ? 37.210 19.680 43.174 1.00 39.96 ? 205 ARG A CD  1 
ATOM   1253 N NE  . ARG A 1 175 ? 38.285 20.234 42.360 1.00 45.15 ? 205 ARG A NE  1 
ATOM   1254 C CZ  . ARG A 1 175 ? 39.483 19.679 42.233 1.00 44.90 ? 205 ARG A CZ  1 
ATOM   1255 N NH1 . ARG A 1 175 ? 39.802 18.569 42.879 1.00 52.49 ? 205 ARG A NH1 1 
ATOM   1256 N NH2 . ARG A 1 175 ? 40.381 20.249 41.435 1.00 39.20 ? 205 ARG A NH2 1 
ATOM   1257 N N   . TRP A 1 176 ? 33.808 18.202 40.927 1.00 17.01 ? 206 TRP A N   1 
ATOM   1258 C CA  . TRP A 1 176 ? 33.218 16.910 41.260 1.00 15.83 ? 206 TRP A CA  1 
ATOM   1259 C C   . TRP A 1 176 ? 33.800 15.808 40.387 1.00 16.26 ? 206 TRP A C   1 
ATOM   1260 O O   . TRP A 1 176 ? 34.120 14.719 40.877 1.00 17.61 ? 206 TRP A O   1 
ATOM   1261 C CB  . TRP A 1 176 ? 31.695 16.958 41.101 1.00 15.14 ? 206 TRP A CB  1 
ATOM   1262 C CG  . TRP A 1 176 ? 30.992 15.716 41.602 1.00 17.24 ? 206 TRP A CG  1 
ATOM   1263 C CD1 . TRP A 1 176 ? 30.391 15.550 42.817 1.00 19.55 ? 206 TRP A CD1 1 
ATOM   1264 C CD2 . TRP A 1 176 ? 30.825 14.470 40.902 1.00 18.98 ? 206 TRP A CD2 1 
ATOM   1265 N NE1 . TRP A 1 176 ? 29.859 14.287 42.917 1.00 21.35 ? 206 TRP A NE1 1 
ATOM   1266 C CE2 . TRP A 1 176 ? 30.111 13.603 41.757 1.00 16.20 ? 206 TRP A CE2 1 
ATOM   1267 C CE3 . TRP A 1 176 ? 31.205 14.005 39.634 1.00 16.61 ? 206 TRP A CE3 1 
ATOM   1268 C CZ2 . TRP A 1 176 ? 29.775 12.298 41.390 1.00 15.79 ? 206 TRP A CZ2 1 
ATOM   1269 C CZ3 . TRP A 1 176 ? 30.868 12.709 39.270 1.00 14.71 ? 206 TRP A CZ3 1 
ATOM   1270 C CH2 . TRP A 1 176 ? 30.161 11.871 40.146 1.00 16.69 ? 206 TRP A CH2 1 
ATOM   1271 N N   . VAL A 1 177 ? 33.939 16.074 39.087 1.00 15.96 ? 207 VAL A N   1 
ATOM   1272 C CA  . VAL A 1 177 ? 34.498 15.068 38.186 1.00 15.62 ? 207 VAL A CA  1 
ATOM   1273 C C   . VAL A 1 177 ? 35.940 14.755 38.566 1.00 17.13 ? 207 VAL A C   1 
ATOM   1274 O O   . VAL A 1 177 ? 36.339 13.586 38.636 1.00 15.28 ? 207 VAL A O   1 
ATOM   1275 C CB  . VAL A 1 177 ? 34.379 15.528 36.722 1.00 15.71 ? 207 VAL A CB  1 
ATOM   1276 C CG1 . VAL A 1 177 ? 35.253 14.663 35.817 1.00 14.68 ? 207 VAL A CG1 1 
ATOM   1277 C CG2 . VAL A 1 177 ? 32.923 15.482 36.275 1.00 14.22 ? 207 VAL A CG2 1 
ATOM   1278 N N   . GLN A 1 178 ? 36.739 15.792 38.825 1.00 15.38 ? 208 GLN A N   1 
ATOM   1279 C CA  . GLN A 1 178 ? 38.102 15.583 39.309 1.00 18.01 ? 208 GLN A CA  1 
ATOM   1280 C C   . GLN A 1 178 ? 38.127 14.630 40.498 1.00 22.23 ? 208 GLN A C   1 
ATOM   1281 O O   . GLN A 1 178 ? 38.925 13.686 40.539 1.00 20.23 ? 208 GLN A O   1 
ATOM   1282 C CB  . GLN A 1 178 ? 38.738 16.922 39.689 1.00 21.72 ? 208 GLN A CB  1 
ATOM   1283 C CG  . GLN A 1 178 ? 39.213 17.729 38.500 1.00 24.61 ? 208 GLN A CG  1 
ATOM   1284 C CD  . GLN A 1 178 ? 40.181 16.948 37.648 1.00 19.60 ? 208 GLN A CD  1 
ATOM   1285 O OE1 . GLN A 1 178 ? 41.275 16.603 38.095 1.00 20.03 ? 208 GLN A OE1 1 
ATOM   1286 N NE2 . GLN A 1 178 ? 39.774 16.635 36.422 1.00 16.22 ? 208 GLN A NE2 1 
ATOM   1287 N N   . SER A 1 179 ? 37.235 14.850 41.467 1.00 16.64 ? 209 SER A N   1 
ATOM   1288 C CA  . SER A 1 179 ? 37.260 14.069 42.699 1.00 19.16 ? 209 SER A CA  1 
ATOM   1289 C C   . SER A 1 179 ? 36.639 12.681 42.566 1.00 22.64 ? 209 SER A C   1 
ATOM   1290 O O   . SER A 1 179 ? 36.957 11.801 43.373 1.00 25.97 ? 209 SER A O   1 
ATOM   1291 C CB  . SER A 1 179 ? 36.539 14.826 43.820 1.00 19.71 ? 209 SER A CB  1 
ATOM   1292 O OG  . SER A 1 179 ? 37.179 16.061 44.091 1.00 28.54 ? 209 SER A OG  1 
ATOM   1293 N N   . ASN A 1 180 ? 35.757 12.460 41.591 1.00 17.11 ? 210 ASN A N   1 
ATOM   1294 C CA  . ASN A 1 180 ? 34.954 11.246 41.566 1.00 18.21 ? 210 ASN A CA  1 
ATOM   1295 C C   . ASN A 1 180 ? 35.108 10.398 40.311 1.00 20.00 ? 210 ASN A C   1 
ATOM   1296 O O   . ASN A 1 180 ? 34.518 9.313  40.253 1.00 23.48 ? 210 ASN A O   1 
ATOM   1297 C CB  . ASN A 1 180 ? 33.470 11.599 41.750 1.00 19.99 ? 210 ASN A CB  1 
ATOM   1298 C CG  . ASN A 1 180 ? 33.177 12.162 43.126 1.00 20.67 ? 210 ASN A CG  1 
ATOM   1299 O OD1 . ASN A 1 180 ? 33.068 11.419 44.095 1.00 19.03 ? 210 ASN A OD1 1 
ATOM   1300 N ND2 . ASN A 1 180 ? 33.056 13.480 43.219 1.00 20.47 ? 210 ASN A ND2 1 
ATOM   1301 N N   . ALA A 1 181 ? 35.886 10.838 39.319 1.00 18.23 ? 211 ALA A N   1 
ATOM   1302 C CA  . ALA A 1 181 ? 35.935 10.123 38.046 1.00 19.93 ? 211 ALA A CA  1 
ATOM   1303 C C   . ALA A 1 181 ? 36.397 8.680  38.218 1.00 18.52 ? 211 ALA A C   1 
ATOM   1304 O O   . ALA A 1 181 ? 35.836 7.768  37.600 1.00 18.34 ? 211 ALA A O   1 
ATOM   1305 C CB  . ALA A 1 181 ? 36.842 10.859 37.067 1.00 19.14 ? 211 ALA A CB  1 
ATOM   1306 N N   . ARG A 1 182 ? 37.404 8.445  39.066 1.00 19.83 ? 212 ARG A N   1 
ATOM   1307 C CA  . ARG A 1 182 ? 37.942 7.093  39.209 1.00 21.11 ? 212 ARG A CA  1 
ATOM   1308 C C   . ARG A 1 182 ? 36.890 6.118  39.721 1.00 22.66 ? 212 ARG A C   1 
ATOM   1309 O O   . ARG A 1 182 ? 36.798 4.986  39.231 1.00 22.18 ? 212 ARG A O   1 
ATOM   1310 C CB  . ARG A 1 182 ? 39.153 7.094  40.135 1.00 26.25 ? 212 ARG A CB  1 
ATOM   1311 C CG  . ARG A 1 182 ? 40.341 7.828  39.576 1.00 32.39 ? 212 ARG A CG  1 
ATOM   1312 C CD  . ARG A 1 182 ? 41.569 7.631  40.439 1.00 27.67 ? 212 ARG A CD  1 
ATOM   1313 N NE  . ARG A 1 182 ? 42.561 8.664  40.170 1.00 39.70 ? 212 ARG A NE  1 
ATOM   1314 C CZ  . ARG A 1 182 ? 43.386 8.657  39.132 1.00 50.41 ? 212 ARG A CZ  1 
ATOM   1315 N NH1 . ARG A 1 182 ? 43.369 7.678  38.240 1.00 43.92 ? 212 ARG A NH1 1 
ATOM   1316 N NH2 . ARG A 1 182 ? 44.247 9.659  38.983 1.00 54.64 ? 212 ARG A NH2 1 
ATOM   1317 N N   . ALA A 1 183 ? 36.087 6.540  40.704 1.00 21.06 ? 213 ALA A N   1 
ATOM   1318 C CA  . ALA A 1 183 ? 35.022 5.694  41.232 1.00 23.33 ? 213 ALA A CA  1 
ATOM   1319 C C   . ALA A 1 183 ? 34.029 5.263  40.161 1.00 21.94 ? 213 ALA A C   1 
ATOM   1320 O O   . ALA A 1 183 ? 33.350 4.248  40.336 1.00 24.77 ? 213 ALA A O   1 
ATOM   1321 C CB  . ALA A 1 183 ? 34.281 6.426  42.352 1.00 20.97 ? 213 ALA A CB  1 
ATOM   1322 N N   . PHE A 1 184 ? 33.923 6.007  39.059 1.00 20.49 ? 214 PHE A N   1 
ATOM   1323 C CA  . PHE A 1 184 ? 32.991 5.674  37.988 1.00 22.23 ? 214 PHE A CA  1 
ATOM   1324 C C   . PHE A 1 184 ? 33.702 5.174  36.731 1.00 20.71 ? 214 PHE A C   1 
ATOM   1325 O O   . PHE A 1 184 ? 33.120 5.190  35.641 1.00 23.87 ? 214 PHE A O   1 
ATOM   1326 C CB  . PHE A 1 184 ? 32.105 6.879  37.668 1.00 16.58 ? 214 PHE A CB  1 
ATOM   1327 C CG  . PHE A 1 184 ? 31.118 7.208  38.755 1.00 23.53 ? 214 PHE A CG  1 
ATOM   1328 C CD1 . PHE A 1 184 ? 31.490 7.991  39.835 1.00 17.34 ? 214 PHE A CD1 1 
ATOM   1329 C CD2 . PHE A 1 184 ? 29.820 6.722  38.703 1.00 20.17 ? 214 PHE A CD2 1 
ATOM   1330 C CE1 . PHE A 1 184 ? 30.583 8.292  40.840 1.00 17.67 ? 214 PHE A CE1 1 
ATOM   1331 C CE2 . PHE A 1 184 ? 28.910 7.020  39.705 1.00 21.27 ? 214 PHE A CE2 1 
ATOM   1332 C CZ  . PHE A 1 184 ? 29.294 7.805  40.773 1.00 19.30 ? 214 PHE A CZ  1 
ATOM   1333 N N   . GLY A 1 185 ? 34.949 4.727  36.862 1.00 19.43 ? 215 GLY A N   1 
ATOM   1334 C CA  . GLY A 1 185 ? 35.697 4.197  35.739 1.00 19.59 ? 215 GLY A CA  1 
ATOM   1335 C C   . GLY A 1 185 ? 36.453 5.213  34.913 1.00 22.64 ? 215 GLY A C   1 
ATOM   1336 O O   . GLY A 1 185 ? 36.985 4.851  33.855 1.00 21.02 ? 215 GLY A O   1 
ATOM   1337 N N   . GLY A 1 186 ? 36.531 6.463  35.361 1.00 21.40 ? 216 GLY A N   1 
ATOM   1338 C CA  . GLY A 1 186 ? 37.140 7.510  34.564 1.00 17.16 ? 216 GLY A CA  1 
ATOM   1339 C C   . GLY A 1 186 ? 38.504 7.962  35.039 1.00 23.72 ? 216 GLY A C   1 
ATOM   1340 O O   . GLY A 1 186 ? 38.902 7.691  36.177 1.00 22.39 ? 216 GLY A O   1 
ATOM   1341 N N   . ASP A 1 187 ? 39.229 8.658  34.164 1.00 24.60 ? 217 ASP A N   1 
ATOM   1342 C CA  . ASP A 1 187 ? 40.564 9.166  34.454 1.00 20.10 ? 217 ASP A CA  1 
ATOM   1343 C C   . ASP A 1 187 ? 40.492 10.677 34.617 1.00 20.31 ? 217 ASP A C   1 
ATOM   1344 O O   . ASP A 1 187 ? 40.288 11.389 33.620 1.00 16.38 ? 217 ASP A O   1 
ATOM   1345 C CB  . ASP A 1 187 ? 41.531 8.794  33.327 1.00 20.58 ? 217 ASP A CB  1 
ATOM   1346 C CG  . ASP A 1 187 ? 42.985 9.103  33.659 1.00 21.52 ? 217 ASP A CG  1 
ATOM   1347 O OD1 . ASP A 1 187 ? 43.255 9.946  34.541 1.00 23.03 ? 217 ASP A OD1 1 
ATOM   1348 O OD2 . ASP A 1 187 ? 43.868 8.492  33.020 1.00 26.46 ? 217 ASP A OD2 1 
ATOM   1349 N N   . PRO A 1 188 ? 40.673 11.213 35.828 1.00 21.83 ? 218 PRO A N   1 
ATOM   1350 C CA  . PRO A 1 188 ? 40.622 12.676 35.998 1.00 18.96 ? 218 PRO A CA  1 
ATOM   1351 C C   . PRO A 1 188 ? 41.711 13.418 35.238 1.00 19.35 ? 218 PRO A C   1 
ATOM   1352 O O   . PRO A 1 188 ? 41.587 14.632 35.033 1.00 19.57 ? 218 PRO A O   1 
ATOM   1353 C CB  . PRO A 1 188 ? 40.771 12.858 37.515 1.00 21.27 ? 218 PRO A CB  1 
ATOM   1354 C CG  . PRO A 1 188 ? 41.498 11.631 37.967 1.00 24.82 ? 218 PRO A CG  1 
ATOM   1355 C CD  . PRO A 1 188 ? 41.005 10.518 37.084 1.00 25.21 ? 218 PRO A CD  1 
ATOM   1356 N N   . GLY A 1 189 ? 42.773 12.737 34.815 1.00 16.83 ? 219 GLY A N   1 
ATOM   1357 C CA  . GLY A 1 189 ? 43.787 13.366 33.995 1.00 18.79 ? 219 GLY A CA  1 
ATOM   1358 C C   . GLY A 1 189 ? 43.481 13.385 32.518 1.00 23.79 ? 219 GLY A C   1 
ATOM   1359 O O   . GLY A 1 189 ? 44.280 13.898 31.729 1.00 20.60 ? 219 GLY A O   1 
ATOM   1360 N N   . ARG A 1 190 ? 42.335 12.831 32.120 1.00 16.62 ? 220 ARG A N   1 
ATOM   1361 C CA  . ARG A 1 190 ? 41.912 12.789 30.725 1.00 18.35 ? 220 ARG A CA  1 
ATOM   1362 C C   . ARG A 1 190 ? 40.459 13.255 30.628 1.00 19.14 ? 220 ARG A C   1 
ATOM   1363 O O   . ARG A 1 190 ? 39.571 12.544 30.158 1.00 16.00 ? 220 ARG A O   1 
ATOM   1364 C CB  . ARG A 1 190 ? 42.074 11.393 30.128 1.00 20.31 ? 220 ARG A CB  1 
ATOM   1365 C CG  . ARG A 1 190 ? 43.510 10.941 29.965 1.00 25.69 ? 220 ARG A CG  1 
ATOM   1366 C CD  . ARG A 1 190 ? 43.600 9.855  28.900 1.00 28.97 ? 220 ARG A CD  1 
ATOM   1367 N NE  . ARG A 1 190 ? 43.085 8.580  29.380 1.00 23.68 ? 220 ARG A NE  1 
ATOM   1368 C CZ  . ARG A 1 190 ? 42.738 7.569  28.598 1.00 22.16 ? 220 ARG A CZ  1 
ATOM   1369 N NH1 . ARG A 1 190 ? 42.780 7.667  27.278 1.00 20.10 ? 220 ARG A NH1 1 
ATOM   1370 N NH2 . ARG A 1 190 ? 42.342 6.428  29.153 1.00 21.82 ? 220 ARG A NH2 1 
ATOM   1371 N N   . VAL A 1 191 ? 40.218 14.476 31.093 1.00 19.68 ? 221 VAL A N   1 
ATOM   1372 C CA  . VAL A 1 191 ? 38.895 15.086 31.051 1.00 16.37 ? 221 VAL A CA  1 
ATOM   1373 C C   . VAL A 1 191 ? 38.828 16.028 29.856 1.00 18.86 ? 221 VAL A C   1 
ATOM   1374 O O   . VAL A 1 191 ? 39.713 16.872 29.662 1.00 19.25 ? 221 VAL A O   1 
ATOM   1375 C CB  . VAL A 1 191 ? 38.579 15.834 32.358 1.00 18.77 ? 221 VAL A CB  1 
ATOM   1376 C CG1 . VAL A 1 191 ? 37.239 16.551 32.247 1.00 14.85 ? 221 VAL A CG1 1 
ATOM   1377 C CG2 . VAL A 1 191 ? 38.578 14.871 33.543 1.00 15.24 ? 221 VAL A CG2 1 
ATOM   1378 N N   . THR A 1 192 ? 37.791 15.866 29.044 1.00 15.03 ? 222 THR A N   1 
ATOM   1379 C CA  . THR A 1 192 ? 37.455 16.781 27.966 1.00 14.91 ? 222 THR A CA  1 
ATOM   1380 C C   . THR A 1 192 ? 36.102 17.387 28.301 1.00 16.53 ? 222 THR A C   1 
ATOM   1381 O O   . THR A 1 192 ? 35.119 16.656 28.482 1.00 16.08 ? 222 THR A O   1 
ATOM   1382 C CB  . THR A 1 192 ? 37.409 16.052 26.616 1.00 15.96 ? 222 THR A CB  1 
ATOM   1383 O OG1 . THR A 1 192 ? 38.718 15.575 26.274 1.00 20.01 ? 222 THR A OG1 1 
ATOM   1384 C CG2 . THR A 1 192 ? 36.895 16.969 25.512 1.00 15.05 ? 222 THR A CG2 1 
ATOM   1385 N N   . VAL A 1 193 ? 36.051 18.707 28.415 1.00 14.36 ? 223 VAL A N   1 
ATOM   1386 C CA  . VAL A 1 193 ? 34.782 19.407 28.560 1.00 14.07 ? 223 VAL A CA  1 
ATOM   1387 C C   . VAL A 1 193 ? 34.291 19.780 27.167 1.00 18.77 ? 223 VAL A C   1 
ATOM   1388 O O   . VAL A 1 193 ? 35.053 20.299 26.341 1.00 15.58 ? 223 VAL A O   1 
ATOM   1389 C CB  . VAL A 1 193 ? 34.928 20.641 29.469 1.00 13.92 ? 223 VAL A CB  1 
ATOM   1390 C CG1 . VAL A 1 193 ? 35.927 21.647 28.895 1.00 14.04 ? 223 VAL A CG1 1 
ATOM   1391 C CG2 . VAL A 1 193 ? 33.577 21.284 29.722 1.00 14.26 ? 223 VAL A CG2 1 
ATOM   1392 N N   . PHE A 1 194 ? 33.038 19.452 26.873 1.00 14.02 ? 224 PHE A N   1 
ATOM   1393 C CA  . PHE A 1 194 ? 32.474 19.774 25.576 1.00 14.10 ? 224 PHE A CA  1 
ATOM   1394 C C   . PHE A 1 194 ? 31.058 20.286 25.777 1.00 16.88 ? 224 PHE A C   1 
ATOM   1395 O O   . PHE A 1 194 ? 30.382 19.924 26.739 1.00 14.83 ? 224 PHE A O   1 
ATOM   1396 C CB  . PHE A 1 194 ? 32.526 18.575 24.598 1.00 14.39 ? 224 PHE A CB  1 
ATOM   1397 C CG  . PHE A 1 194 ? 31.600 17.423 24.932 1.00 15.74 ? 224 PHE A CG  1 
ATOM   1398 C CD1 . PHE A 1 194 ? 31.455 16.954 26.230 1.00 14.29 ? 224 PHE A CD1 1 
ATOM   1399 C CD2 . PHE A 1 194 ? 30.904 16.783 23.915 1.00 14.66 ? 224 PHE A CD2 1 
ATOM   1400 C CE1 . PHE A 1 194 ? 30.612 15.885 26.510 1.00 14.38 ? 224 PHE A CE1 1 
ATOM   1401 C CE2 . PHE A 1 194 ? 30.055 15.715 24.190 1.00 19.72 ? 224 PHE A CE2 1 
ATOM   1402 C CZ  . PHE A 1 194 ? 29.910 15.269 25.490 1.00 16.43 ? 224 PHE A CZ  1 
ATOM   1403 N N   . GLY A 1 195 ? 30.633 21.173 24.888 1.00 15.15 ? 225 GLY A N   1 
ATOM   1404 C CA  . GLY A 1 195 ? 29.337 21.799 25.057 1.00 16.14 ? 225 GLY A CA  1 
ATOM   1405 C C   . GLY A 1 195 ? 28.868 22.379 23.745 1.00 16.59 ? 225 GLY A C   1 
ATOM   1406 O O   . GLY A 1 195 ? 29.593 22.387 22.747 1.00 15.43 ? 225 GLY A O   1 
ATOM   1407 N N   . GLU A 1 196 ? 27.634 22.871 23.759 1.00 13.97 ? 226 GLU A N   1 
ATOM   1408 C CA  . GLU A 1 196 ? 27.074 23.432 22.535 1.00 14.53 ? 226 GLU A CA  1 
ATOM   1409 C C   . GLU A 1 196 ? 26.347 24.732 22.830 1.00 15.37 ? 226 GLU A C   1 
ATOM   1410 O O   . GLU A 1 196 ? 25.733 24.894 23.885 1.00 18.54 ? 226 GLU A O   1 
ATOM   1411 C CB  . GLU A 1 196 ? 26.134 22.439 21.829 1.00 19.79 ? 226 GLU A CB  1 
ATOM   1412 C CG  . GLU A 1 196 ? 25.721 22.837 20.414 1.00 14.76 ? 226 GLU A CG  1 
ATOM   1413 C CD  . GLU A 1 196 ? 24.428 23.624 20.381 1.00 15.51 ? 226 GLU A CD  1 
ATOM   1414 O OE1 . GLU A 1 196 ? 23.708 23.625 21.401 1.00 14.90 ? 226 GLU A OE1 1 
ATOM   1415 O OE2 . GLU A 1 196 ? 24.132 24.246 19.339 1.00 15.52 ? 226 GLU A OE2 1 
ATOM   1416 N N   . SER A 1 197 ? 26.437 25.659 21.877 1.00 14.42 ? 227 SER A N   1 
ATOM   1417 C CA  . SER A 1 197 ? 25.776 26.972 21.939 1.00 19.71 ? 227 SER A CA  1 
ATOM   1418 C C   . SER A 1 197 ? 26.214 27.652 23.236 1.00 18.04 ? 227 SER A C   1 
ATOM   1419 O O   . SER A 1 197 ? 27.429 27.760 23.479 1.00 17.33 ? 227 SER A O   1 
ATOM   1420 C CB  . SER A 1 197 ? 24.276 26.789 21.761 1.00 14.45 ? 227 SER A CB  1 
ATOM   1421 O OG  . SER A 1 197 ? 23.621 28.046 21.726 1.00 17.32 ? 227 SER A OG  1 
ATOM   1422 N N   . ALA A 1 198 ? 25.289 28.112 24.087 1.00 15.48 ? 228 ALA A N   1 
ATOM   1423 C CA  . ALA A 1 198 ? 25.680 28.809 25.308 1.00 13.95 ? 228 ALA A CA  1 
ATOM   1424 C C   . ALA A 1 198 ? 26.608 27.962 26.178 1.00 14.74 ? 228 ALA A C   1 
ATOM   1425 O O   . ALA A 1 198 ? 27.438 28.510 26.910 1.00 14.76 ? 228 ALA A O   1 
ATOM   1426 C CB  . ALA A 1 198 ? 24.437 29.228 26.090 1.00 15.60 ? 228 ALA A CB  1 
ATOM   1427 N N   . GLY A 1 199 ? 26.499 26.633 26.106 1.00 15.20 ? 229 GLY A N   1 
ATOM   1428 C CA  . GLY A 1 199 ? 27.450 25.788 26.815 1.00 13.45 ? 229 GLY A CA  1 
ATOM   1429 C C   . GLY A 1 199 ? 28.862 25.926 26.273 1.00 13.53 ? 229 GLY A C   1 
ATOM   1430 O O   . GLY A 1 199 ? 29.835 26.041 27.034 1.00 13.47 ? 229 GLY A O   1 
ATOM   1431 N N   . ALA A 1 200 ? 28.989 25.923 24.944 1.00 14.71 ? 230 ALA A N   1 
ATOM   1432 C CA  . ALA A 1 200 ? 30.287 26.161 24.329 1.00 14.67 ? 230 ALA A CA  1 
ATOM   1433 C C   . ALA A 1 200 ? 30.773 27.578 24.600 1.00 15.67 ? 230 ALA A C   1 
ATOM   1434 O O   . ALA A 1 200 ? 31.975 27.799 24.777 1.00 15.74 ? 230 ALA A O   1 
ATOM   1435 C CB  . ALA A 1 200 ? 30.208 25.891 22.826 1.00 14.10 ? 230 ALA A CB  1 
ATOM   1436 N N   . SER A 1 201 ? 29.852 28.544 24.667 1.00 15.30 ? 231 SER A N   1 
ATOM   1437 C CA  . SER A 1 201 ? 30.232 29.906 25.028 1.00 14.48 ? 231 SER A CA  1 
ATOM   1438 C C   . SER A 1 201 ? 30.785 29.961 26.446 1.00 16.04 ? 231 SER A C   1 
ATOM   1439 O O   . SER A 1 201 ? 31.761 30.673 26.719 1.00 16.72 ? 231 SER A O   1 
ATOM   1440 C CB  . SER A 1 201 ? 29.025 30.838 24.891 1.00 13.98 ? 231 SER A CB  1 
ATOM   1441 O OG  . SER A 1 201 ? 28.420 30.707 23.613 1.00 14.15 ? 231 SER A OG  1 
ATOM   1442 N N   . ALA A 1 202 ? 30.174 29.209 27.363 1.00 13.60 ? 232 ALA A N   1 
ATOM   1443 C CA  . ALA A 1 202 ? 30.673 29.162 28.730 1.00 13.52 ? 232 ALA A CA  1 
ATOM   1444 C C   . ALA A 1 202 ? 32.057 28.531 28.781 1.00 14.89 ? 232 ALA A C   1 
ATOM   1445 O O   . ALA A 1 202 ? 32.953 29.039 29.463 1.00 13.66 ? 232 ALA A O   1 
ATOM   1446 C CB  . ALA A 1 202 ? 29.696 28.393 29.620 1.00 13.36 ? 232 ALA A CB  1 
ATOM   1447 N N   . ILE A 1 203 ? 32.248 27.418 28.067 1.00 15.67 ? 233 ILE A N   1 
ATOM   1448 C CA  . ILE A 1 203 ? 33.571 26.797 28.004 1.00 16.17 ? 233 ILE A CA  1 
ATOM   1449 C C   . ILE A 1 203 ? 34.601 27.789 27.472 1.00 15.14 ? 233 ILE A C   1 
ATOM   1450 O O   . ILE A 1 203 ? 35.704 27.925 28.019 1.00 15.76 ? 233 ILE A O   1 
ATOM   1451 C CB  . ILE A 1 203 ? 33.529 25.519 27.146 1.00 14.34 ? 233 ILE A CB  1 
ATOM   1452 C CG1 . ILE A 1 203 ? 32.660 24.451 27.813 1.00 13.59 ? 233 ILE A CG1 1 
ATOM   1453 C CG2 . ILE A 1 203 ? 34.935 24.979 26.925 1.00 15.53 ? 233 ILE A CG2 1 
ATOM   1454 C CD1 . ILE A 1 203 ? 32.353 23.284 26.911 1.00 13.68 ? 233 ILE A CD1 1 
ATOM   1455 N N   . GLY A 1 204 ? 34.251 28.508 26.404 1.00 14.72 ? 234 GLY A N   1 
ATOM   1456 C CA  . GLY A 1 204 ? 35.188 29.457 25.824 1.00 15.32 ? 234 GLY A CA  1 
ATOM   1457 C C   . GLY A 1 204 ? 35.552 30.578 26.777 1.00 16.20 ? 234 GLY A C   1 
ATOM   1458 O O   . GLY A 1 204 ? 36.723 30.948 26.894 1.00 14.53 ? 234 GLY A O   1 
ATOM   1459 N N   . LEU A 1 205 ? 34.555 31.127 27.479 1.00 15.85 ? 235 LEU A N   1 
ATOM   1460 C CA  . LEU A 1 205 ? 34.840 32.157 28.475 1.00 14.45 ? 235 LEU A CA  1 
ATOM   1461 C C   . LEU A 1 205 ? 35.699 31.609 29.607 1.00 14.29 ? 235 LEU A C   1 
ATOM   1462 O O   . LEU A 1 205 ? 36.581 32.309 30.120 1.00 16.07 ? 235 LEU A O   1 
ATOM   1463 C CB  . LEU A 1 205 ? 33.537 32.737 29.020 1.00 14.16 ? 235 LEU A CB  1 
ATOM   1464 C CG  . LEU A 1 205 ? 32.680 33.492 27.999 1.00 14.23 ? 235 LEU A CG  1 
ATOM   1465 C CD1 . LEU A 1 205 ? 31.337 33.857 28.604 1.00 14.13 ? 235 LEU A CD1 1 
ATOM   1466 C CD2 . LEU A 1 205 ? 33.401 34.740 27.496 1.00 14.54 ? 235 LEU A CD2 1 
ATOM   1467 N N   . LEU A 1 206 ? 35.456 30.359 30.013 1.00 15.00 ? 236 LEU A N   1 
ATOM   1468 C CA  . LEU A 1 206 ? 36.247 29.748 31.073 1.00 14.16 ? 236 LEU A CA  1 
ATOM   1469 C C   . LEU A 1 206 ? 37.680 29.493 30.637 1.00 15.16 ? 236 LEU A C   1 
ATOM   1470 O O   . LEU A 1 206 ? 38.564 29.397 31.494 1.00 17.08 ? 236 LEU A O   1 
ATOM   1471 C CB  . LEU A 1 206 ? 35.591 28.445 31.538 1.00 13.94 ? 236 LEU A CB  1 
ATOM   1472 C CG  . LEU A 1 206 ? 34.297 28.632 32.341 1.00 16.13 ? 236 LEU A CG  1 
ATOM   1473 C CD1 . LEU A 1 206 ? 33.700 27.292 32.748 1.00 15.24 ? 236 LEU A CD1 1 
ATOM   1474 C CD2 . LEU A 1 206 ? 34.554 29.505 33.572 1.00 13.90 ? 236 LEU A CD2 1 
ATOM   1475 N N   . LEU A 1 207 ? 37.923 29.367 29.330 1.00 15.77 ? 237 LEU A N   1 
ATOM   1476 C CA  . LEU A 1 207 ? 39.298 29.293 28.844 1.00 15.01 ? 237 LEU A CA  1 
ATOM   1477 C C   . LEU A 1 207 ? 40.092 30.551 29.177 1.00 18.05 ? 237 LEU A C   1 
ATOM   1478 O O   . LEU A 1 207 ? 41.327 30.508 29.174 1.00 16.42 ? 237 LEU A O   1 
ATOM   1479 C CB  . LEU A 1 207 ? 39.330 29.051 27.337 1.00 16.76 ? 237 LEU A CB  1 
ATOM   1480 C CG  . LEU A 1 207 ? 38.695 27.754 26.837 1.00 19.54 ? 237 LEU A CG  1 
ATOM   1481 C CD1 . LEU A 1 207 ? 38.919 27.587 25.335 1.00 16.89 ? 237 LEU A CD1 1 
ATOM   1482 C CD2 . LEU A 1 207 ? 39.228 26.555 27.608 1.00 14.70 ? 237 LEU A CD2 1 
ATOM   1483 N N   . THR A 1 208 ? 39.419 31.666 29.461 1.00 15.05 ? 238 THR A N   1 
ATOM   1484 C CA  . THR A 1 208 ? 40.083 32.886 29.897 1.00 15.37 ? 238 THR A CA  1 
ATOM   1485 C C   . THR A 1 208 ? 40.005 33.080 31.407 1.00 18.60 ? 238 THR A C   1 
ATOM   1486 O O   . THR A 1 208 ? 40.404 34.135 31.909 1.00 18.66 ? 238 THR A O   1 
ATOM   1487 C CB  . THR A 1 208 ? 39.488 34.104 29.186 1.00 15.43 ? 238 THR A CB  1 
ATOM   1488 O OG1 . THR A 1 208 ? 38.215 34.428 29.761 1.00 15.19 ? 238 THR A OG1 1 
ATOM   1489 C CG2 . THR A 1 208 ? 39.309 33.820 27.695 1.00 15.39 ? 238 THR A CG2 1 
ATOM   1490 N N   . SER A 1 209 ? 39.511 32.087 32.140 1.00 17.60 ? 239 SER A N   1 
ATOM   1491 C CA  . SER A 1 209 ? 39.333 32.226 33.580 1.00 17.11 ? 239 SER A CA  1 
ATOM   1492 C C   . SER A 1 209 ? 40.461 31.538 34.322 1.00 16.58 ? 239 SER A C   1 
ATOM   1493 O O   . SER A 1 209 ? 40.724 30.354 34.073 1.00 17.74 ? 239 SER A O   1 
ATOM   1494 C CB  . SER A 1 209 ? 38.002 31.622 34.015 1.00 17.09 ? 239 SER A CB  1 
ATOM   1495 O OG  . SER A 1 209 ? 37.839 31.728 35.421 1.00 17.58 ? 239 SER A OG  1 
ATOM   1496 N N   . PRO A 1 210 ? 41.136 32.218 35.249 1.00 18.22 ? 240 PRO A N   1 
ATOM   1497 C CA  . PRO A 1 210 ? 42.112 31.510 36.093 1.00 19.42 ? 240 PRO A CA  1 
ATOM   1498 C C   . PRO A 1 210 ? 41.480 30.417 36.940 1.00 19.71 ? 240 PRO A C   1 
ATOM   1499 O O   . PRO A 1 210 ? 42.189 29.499 37.368 1.00 20.38 ? 240 PRO A O   1 
ATOM   1500 C CB  . PRO A 1 210 ? 42.711 32.628 36.960 1.00 16.52 ? 240 PRO A CB  1 
ATOM   1501 C CG  . PRO A 1 210 ? 41.674 33.708 36.958 1.00 26.65 ? 240 PRO A CG  1 
ATOM   1502 C CD  . PRO A 1 210 ? 41.004 33.641 35.612 1.00 16.53 ? 240 PRO A CD  1 
ATOM   1503 N N   . LEU A 1 211 ? 40.162 30.463 37.158 1.00 17.60 ? 241 LEU A N   1 
ATOM   1504 C CA  . LEU A 1 211 ? 39.483 29.462 37.976 1.00 20.57 ? 241 LEU A CA  1 
ATOM   1505 C C   . LEU A 1 211 ? 39.356 28.102 37.299 1.00 17.70 ? 241 LEU A C   1 
ATOM   1506 O O   . LEU A 1 211 ? 39.001 27.131 37.975 1.00 17.08 ? 241 LEU A O   1 
ATOM   1507 C CB  . LEU A 1 211 ? 38.089 29.960 38.365 1.00 15.05 ? 241 LEU A CB  1 
ATOM   1508 C CG  . LEU A 1 211 ? 38.046 31.252 39.183 1.00 24.69 ? 241 LEU A CG  1 
ATOM   1509 C CD1 . LEU A 1 211 ? 36.609 31.594 39.559 1.00 17.35 ? 241 LEU A CD1 1 
ATOM   1510 C CD2 . LEU A 1 211 ? 38.928 31.152 40.431 1.00 15.75 ? 241 LEU A CD2 1 
ATOM   1511 N N   . SER A 1 212 ? 39.628 27.994 36.002 1.00 19.34 ? 242 SER A N   1 
ATOM   1512 C CA  . SER A 1 212 ? 39.464 26.721 35.314 1.00 18.56 ? 242 SER A CA  1 
ATOM   1513 C C   . SER A 1 212 ? 40.719 25.859 35.344 1.00 17.44 ? 242 SER A C   1 
ATOM   1514 O O   . SER A 1 212 ? 40.686 24.734 34.837 1.00 17.91 ? 242 SER A O   1 
ATOM   1515 C CB  . SER A 1 212 ? 39.031 26.952 33.859 1.00 22.48 ? 242 SER A CB  1 
ATOM   1516 O OG  . SER A 1 212 ? 40.056 27.578 33.107 1.00 23.53 ? 242 SER A OG  1 
ATOM   1517 N N   . LYS A 1 213 ? 41.806 26.351 35.940 1.00 18.41 ? 243 LYS A N   1 
ATOM   1518 C CA  . LYS A 1 213 ? 43.084 25.648 35.932 1.00 23.61 ? 243 LYS A CA  1 
ATOM   1519 C C   . LYS A 1 213 ? 42.950 24.215 36.438 1.00 20.09 ? 243 LYS A C   1 
ATOM   1520 O O   . LYS A 1 213 ? 42.378 23.966 37.503 1.00 19.26 ? 243 LYS A O   1 
ATOM   1521 C CB  . LYS A 1 213 ? 44.093 26.421 36.786 1.00 24.14 ? 243 LYS A CB  1 
ATOM   1522 C CG  . LYS A 1 213 ? 45.406 25.700 37.055 1.00 29.77 ? 243 LYS A CG  1 
ATOM   1523 C CD  . LYS A 1 213 ? 46.355 26.607 37.836 1.00 32.48 ? 243 LYS A CD  1 
ATOM   1524 C CE  . LYS A 1 213 ? 46.862 25.951 39.115 1.00 45.53 ? 243 LYS A CE  1 
ATOM   1525 N NZ  . LYS A 1 213 ? 47.876 24.886 38.863 1.00 46.71 ? 243 LYS A NZ  1 
ATOM   1526 N N   . GLY A 1 214 ? 43.467 23.273 35.651 1.00 21.92 ? 244 GLY A N   1 
ATOM   1527 C CA  . GLY A 1 214 ? 43.549 21.885 36.056 1.00 22.23 ? 244 GLY A CA  1 
ATOM   1528 C C   . GLY A 1 214 ? 42.249 21.116 36.072 1.00 20.43 ? 244 GLY A C   1 
ATOM   1529 O O   . GLY A 1 214 ? 42.210 20.016 36.628 1.00 28.05 ? 244 GLY A O   1 
ATOM   1530 N N   . LEU A 1 215 ? 41.181 21.645 35.481 1.00 15.82 ? 245 LEU A N   1 
ATOM   1531 C CA  . LEU A 1 215 ? 39.891 20.970 35.515 1.00 18.34 ? 245 LEU A CA  1 
ATOM   1532 C C   . LEU A 1 215 ? 39.585 20.189 34.244 1.00 20.49 ? 245 LEU A C   1 
ATOM   1533 O O   . LEU A 1 215 ? 38.613 19.425 34.226 1.00 19.16 ? 245 LEU A O   1 
ATOM   1534 C CB  . LEU A 1 215 ? 38.774 21.983 35.782 1.00 14.63 ? 245 LEU A CB  1 
ATOM   1535 C CG  . LEU A 1 215 ? 38.817 22.627 37.171 1.00 24.28 ? 245 LEU A CG  1 
ATOM   1536 C CD1 . LEU A 1 215 ? 37.796 23.747 37.285 1.00 17.92 ? 245 LEU A CD1 1 
ATOM   1537 C CD2 . LEU A 1 215 ? 38.586 21.578 38.254 1.00 23.46 ? 245 LEU A CD2 1 
ATOM   1538 N N   . PHE A 1 216 ? 40.385 20.353 33.192 1.00 15.09 ? 246 PHE A N   1 
ATOM   1539 C CA  . PHE A 1 216 ? 40.221 19.581 31.968 1.00 17.41 ? 246 PHE A CA  1 
ATOM   1540 C C   . PHE A 1 216 ? 41.456 19.763 31.100 1.00 19.77 ? 246 PHE A C   1 
ATOM   1541 O O   . PHE A 1 216 ? 42.049 20.845 31.075 1.00 20.52 ? 246 PHE A O   1 
ATOM   1542 C CB  . PHE A 1 216 ? 38.958 19.997 31.192 1.00 14.67 ? 246 PHE A CB  1 
ATOM   1543 C CG  . PHE A 1 216 ? 38.797 21.488 31.028 1.00 15.46 ? 246 PHE A CG  1 
ATOM   1544 C CD1 . PHE A 1 216 ? 39.370 22.149 29.950 1.00 18.22 ? 246 PHE A CD1 1 
ATOM   1545 C CD2 . PHE A 1 216 ? 38.062 22.225 31.948 1.00 14.44 ? 246 PHE A CD2 1 
ATOM   1546 C CE1 . PHE A 1 216 ? 39.222 23.517 29.796 1.00 17.60 ? 246 PHE A CE1 1 
ATOM   1547 C CE2 . PHE A 1 216 ? 37.910 23.592 31.800 1.00 15.53 ? 246 PHE A CE2 1 
ATOM   1548 C CZ  . PHE A 1 216 ? 38.489 24.239 30.723 1.00 19.26 ? 246 PHE A CZ  1 
ATOM   1549 N N   . ARG A 1 217 ? 41.841 18.699 30.397 1.00 17.67 ? 247 ARG A N   1 
ATOM   1550 C CA  . ARG A 1 217 ? 42.930 18.793 29.436 1.00 20.04 ? 247 ARG A CA  1 
ATOM   1551 C C   . ARG A 1 217 ? 42.441 19.133 28.036 1.00 18.99 ? 247 ARG A C   1 
ATOM   1552 O O   . ARG A 1 217 ? 43.253 19.527 27.187 1.00 19.75 ? 247 ARG A O   1 
ATOM   1553 C CB  . ARG A 1 217 ? 43.717 17.477 29.387 1.00 19.54 ? 247 ARG A CB  1 
ATOM   1554 C CG  . ARG A 1 217 ? 43.004 16.376 28.616 1.00 23.46 ? 247 ARG A CG  1 
ATOM   1555 C CD  . ARG A 1 217 ? 43.997 15.462 27.924 1.00 27.45 ? 247 ARG A CD  1 
ATOM   1556 N NE  . ARG A 1 217 ? 43.341 14.329 27.285 1.00 27.73 ? 247 ARG A NE  1 
ATOM   1557 C CZ  . ARG A 1 217 ? 43.971 13.232 26.889 1.00 29.41 ? 247 ARG A CZ  1 
ATOM   1558 N NH1 . ARG A 1 217 ? 45.278 13.094 27.041 1.00 33.28 ? 247 ARG A NH1 1 
ATOM   1559 N NH2 . ARG A 1 217 ? 43.271 12.245 26.339 1.00 21.97 ? 247 ARG A NH2 1 
ATOM   1560 N N   . GLY A 1 218 ? 41.150 18.987 27.775 1.00 19.07 ? 248 GLY A N   1 
ATOM   1561 C CA  . GLY A 1 218 ? 40.617 19.226 26.449 1.00 18.53 ? 248 GLY A CA  1 
ATOM   1562 C C   . GLY A 1 218 ? 39.277 19.927 26.523 1.00 24.18 ? 248 GLY A C   1 
ATOM   1563 O O   . GLY A 1 218 ? 38.549 19.828 27.517 1.00 19.58 ? 248 GLY A O   1 
ATOM   1564 N N   . ALA A 1 219 ? 38.959 20.650 25.449 1.00 15.02 ? 249 ALA A N   1 
ATOM   1565 C CA  . ALA A 1 219 ? 37.706 21.385 25.355 1.00 16.00 ? 249 ALA A CA  1 
ATOM   1566 C C   . ALA A 1 219 ? 37.200 21.341 23.922 1.00 16.76 ? 249 ALA A C   1 
ATOM   1567 O O   . ALA A 1 219 ? 37.951 21.638 22.986 1.00 16.45 ? 249 ALA A O   1 
ATOM   1568 C CB  . ALA A 1 219 ? 37.878 22.834 25.812 1.00 14.61 ? 249 ALA A CB  1 
ATOM   1569 N N   . ILE A 1 220 ? 35.936 20.955 23.758 1.00 14.68 ? 250 ILE A N   1 
ATOM   1570 C CA  . ILE A 1 220 ? 35.262 20.957 22.466 1.00 14.81 ? 250 ILE A CA  1 
ATOM   1571 C C   . ILE A 1 220 ? 34.167 22.008 22.523 1.00 14.58 ? 250 ILE A C   1 
ATOM   1572 O O   . ILE A 1 220 ? 33.276 21.943 23.381 1.00 18.74 ? 250 ILE A O   1 
ATOM   1573 C CB  . ILE A 1 220 ? 34.679 19.580 22.115 1.00 14.95 ? 250 ILE A CB  1 
ATOM   1574 C CG1 . ILE A 1 220 ? 35.755 18.497 22.208 1.00 15.20 ? 250 ILE A CG1 1 
ATOM   1575 C CG2 . ILE A 1 220 ? 34.042 19.604 20.725 1.00 15.35 ? 250 ILE A CG2 1 
ATOM   1576 C CD1 . ILE A 1 220 ? 35.248 17.105 21.892 1.00 15.40 ? 250 ILE A CD1 1 
ATOM   1577 N N   . LEU A 1 221 ? 34.227 22.971 21.607 1.00 17.52 ? 251 LEU A N   1 
ATOM   1578 C CA  . LEU A 1 221 ? 33.287 24.086 21.561 1.00 15.35 ? 251 LEU A CA  1 
ATOM   1579 C C   . LEU A 1 221 ? 32.475 23.975 20.278 1.00 18.66 ? 251 LEU A C   1 
ATOM   1580 O O   . LEU A 1 221 ? 32.998 24.215 19.183 1.00 16.90 ? 251 LEU A O   1 
ATOM   1581 C CB  . LEU A 1 221 ? 34.018 25.424 21.630 1.00 14.98 ? 251 LEU A CB  1 
ATOM   1582 C CG  . LEU A 1 221 ? 34.696 25.806 22.950 1.00 16.76 ? 251 LEU A CG  1 
ATOM   1583 C CD1 . LEU A 1 221 ? 35.998 25.049 23.158 1.00 17.22 ? 251 LEU A CD1 1 
ATOM   1584 C CD2 . LEU A 1 221 ? 34.940 27.303 22.996 1.00 14.49 ? 251 LEU A CD2 1 
ATOM   1585 N N   . GLU A 1 222 ? 31.202 23.595 20.410 1.00 16.54 ? 252 GLU A N   1 
ATOM   1586 C CA  . GLU A 1 222 ? 30.297 23.459 19.270 1.00 19.84 ? 252 GLU A CA  1 
ATOM   1587 C C   . GLU A 1 222 ? 29.434 24.717 19.192 1.00 16.07 ? 252 GLU A C   1 
ATOM   1588 O O   . GLU A 1 222 ? 28.567 24.936 20.041 1.00 14.90 ? 252 GLU A O   1 
ATOM   1589 C CB  . GLU A 1 222 ? 29.440 22.195 19.390 1.00 14.97 ? 252 GLU A CB  1 
ATOM   1590 C CG  . GLU A 1 222 ? 30.248 20.904 19.389 1.00 16.22 ? 252 GLU A CG  1 
ATOM   1591 C CD  . GLU A 1 222 ? 29.447 19.674 19.822 1.00 22.47 ? 252 GLU A CD  1 
ATOM   1592 O OE1 . GLU A 1 222 ? 28.223 19.619 19.557 1.00 15.67 ? 252 GLU A OE1 1 
ATOM   1593 O OE2 . GLU A 1 222 ? 30.049 18.764 20.441 1.00 17.26 ? 252 GLU A OE2 1 
ATOM   1594 N N   . SER A 1 223 ? 29.678 25.540 18.174 1.00 18.10 ? 253 SER A N   1 
ATOM   1595 C CA  . SER A 1 223 ? 28.954 26.786 17.955 1.00 15.20 ? 253 SER A CA  1 
ATOM   1596 C C   . SER A 1 223 ? 28.936 27.705 19.185 1.00 17.16 ? 253 SER A C   1 
ATOM   1597 O O   . SER A 1 223 ? 27.858 28.073 19.669 1.00 16.67 ? 253 SER A O   1 
ATOM   1598 C CB  . SER A 1 223 ? 27.535 26.510 17.481 1.00 15.36 ? 253 SER A CB  1 
ATOM   1599 O OG  . SER A 1 223 ? 27.527 25.705 16.313 1.00 17.67 ? 253 SER A OG  1 
ATOM   1600 N N   . PRO A 1 224 ? 30.095 28.100 19.706 1.00 17.89 ? 254 PRO A N   1 
ATOM   1601 C CA  . PRO A 1 224 ? 30.102 29.046 20.824 1.00 14.58 ? 254 PRO A CA  1 
ATOM   1602 C C   . PRO A 1 224 ? 29.873 30.472 20.351 1.00 16.45 ? 254 PRO A C   1 
ATOM   1603 O O   . PRO A 1 224 ? 30.280 30.864 19.254 1.00 18.51 ? 254 PRO A O   1 
ATOM   1604 C CB  . PRO A 1 224 ? 31.510 28.887 21.405 1.00 15.41 ? 254 PRO A CB  1 
ATOM   1605 C CG  . PRO A 1 224 ? 32.341 28.569 20.199 1.00 14.89 ? 254 PRO A CG  1 
ATOM   1606 C CD  . PRO A 1 224 ? 31.467 27.751 19.282 1.00 14.94 ? 254 PRO A CD  1 
ATOM   1607 N N   . GLY A 1 225 ? 29.205 31.251 21.201 1.00 17.03 ? 255 GLY A N   1 
ATOM   1608 C CA  . GLY A 1 225 ? 29.057 32.676 20.974 1.00 14.86 ? 255 GLY A CA  1 
ATOM   1609 C C   . GLY A 1 225 ? 30.073 33.485 21.758 1.00 18.80 ? 255 GLY A C   1 
ATOM   1610 O O   . GLY A 1 225 ? 29.888 33.730 22.957 1.00 16.37 ? 255 GLY A O   1 
ATOM   1611 N N   . LEU A 1 226 ? 31.145 33.914 21.091 1.00 15.06 ? 256 LEU A N   1 
ATOM   1612 C CA  . LEU A 1 226 ? 32.293 34.524 21.752 1.00 15.99 ? 256 LEU A CA  1 
ATOM   1613 C C   . LEU A 1 226 ? 32.635 35.865 21.111 1.00 17.45 ? 256 LEU A C   1 
ATOM   1614 O O   . LEU A 1 226 ? 32.189 36.187 20.005 1.00 18.87 ? 256 LEU A O   1 
ATOM   1615 C CB  . LEU A 1 226 ? 33.518 33.592 21.706 1.00 15.08 ? 256 LEU A CB  1 
ATOM   1616 C CG  . LEU A 1 226 ? 33.300 32.241 22.392 1.00 16.66 ? 256 LEU A CG  1 
ATOM   1617 C CD1 . LEU A 1 226 ? 34.356 31.225 21.992 1.00 14.84 ? 256 LEU A CD1 1 
ATOM   1618 C CD2 . LEU A 1 226 ? 33.269 32.414 23.912 1.00 15.11 ? 256 LEU A CD2 1 
ATOM   1619 N N   . THR A 1 227 ? 33.460 36.639 21.825 1.00 15.57 ? 257 THR A N   1 
ATOM   1620 C CA  . THR A 1 227 ? 33.793 38.026 21.480 1.00 19.37 ? 257 THR A CA  1 
ATOM   1621 C C   . THR A 1 227 ? 32.545 38.893 21.352 1.00 17.54 ? 257 THR A C   1 
ATOM   1622 O O   . THR A 1 227 ? 32.563 39.917 20.669 1.00 20.42 ? 257 THR A O   1 
ATOM   1623 C CB  . THR A 1 227 ? 34.642 38.123 20.201 1.00 19.90 ? 257 THR A CB  1 
ATOM   1624 O OG1 . THR A 1 227 ? 33.861 37.730 19.065 1.00 21.79 ? 257 THR A OG1 1 
ATOM   1625 C CG2 . THR A 1 227 ? 35.873 37.221 20.298 1.00 18.76 ? 257 THR A CG2 1 
ATOM   1626 N N   . ARG A 1 228 ? 31.454 38.494 22.017 1.00 21.10 ? 258 ARG A N   1 
ATOM   1627 C CA  . ARG A 1 228 ? 30.220 39.262 22.073 1.00 18.99 ? 258 ARG A CA  1 
ATOM   1628 C C   . ARG A 1 228 ? 30.288 40.304 23.180 1.00 20.75 ? 258 ARG A C   1 
ATOM   1629 O O   . ARG A 1 228 ? 31.087 40.182 24.116 1.00 21.62 ? 258 ARG A O   1 
ATOM   1630 C CB  . ARG A 1 228 ? 29.030 38.338 22.325 1.00 18.88 ? 258 ARG A CB  1 
ATOM   1631 C CG  . ARG A 1 228 ? 28.696 37.359 21.217 1.00 23.50 ? 258 ARG A CG  1 
ATOM   1632 C CD  . ARG A 1 228 ? 27.440 36.595 21.596 1.00 21.72 ? 258 ARG A CD  1 
ATOM   1633 N NE  . ARG A 1 228 ? 27.066 35.565 20.635 1.00 23.16 ? 258 ARG A NE  1 
ATOM   1634 C CZ  . ARG A 1 228 ? 26.000 34.785 20.761 1.00 25.05 ? 258 ARG A CZ  1 
ATOM   1635 N NH1 . ARG A 1 228 ? 25.180 34.896 21.795 1.00 22.49 ? 258 ARG A NH1 1 
ATOM   1636 N NH2 . ARG A 1 228 ? 25.748 33.873 19.827 1.00 23.51 ? 258 ARG A NH2 1 
ATOM   1637 N N   . PRO A 1 229 ? 29.456 41.344 23.101 1.00 19.56 ? 259 PRO A N   1 
ATOM   1638 C CA  . PRO A 1 229 ? 29.388 42.323 24.195 1.00 21.10 ? 259 PRO A CA  1 
ATOM   1639 C C   . PRO A 1 229 ? 29.015 41.669 25.520 1.00 24.61 ? 259 PRO A C   1 
ATOM   1640 O O   . PRO A 1 229 ? 28.082 40.864 25.602 1.00 19.16 ? 259 PRO A O   1 
ATOM   1641 C CB  . PRO A 1 229 ? 28.307 43.302 23.723 1.00 18.43 ? 259 PRO A CB  1 
ATOM   1642 C CG  . PRO A 1 229 ? 28.351 43.211 22.239 1.00 21.93 ? 259 PRO A CG  1 
ATOM   1643 C CD  . PRO A 1 229 ? 28.677 41.778 21.926 1.00 24.47 ? 259 PRO A CD  1 
ATOM   1644 N N   . LEU A 1 230 ? 29.761 42.022 26.564 1.00 18.52 ? 260 LEU A N   1 
ATOM   1645 C CA  . LEU A 1 230 ? 29.509 41.558 27.921 1.00 21.10 ? 260 LEU A CA  1 
ATOM   1646 C C   . LEU A 1 230 ? 29.336 42.761 28.836 1.00 17.92 ? 260 LEU A C   1 
ATOM   1647 O O   . LEU A 1 230 ? 30.048 43.761 28.703 1.00 23.48 ? 260 LEU A O   1 
ATOM   1648 C CB  . LEU A 1 230 ? 30.651 40.667 28.432 1.00 15.63 ? 260 LEU A CB  1 
ATOM   1649 C CG  . LEU A 1 230 ? 30.957 39.411 27.613 1.00 20.74 ? 260 LEU A CG  1 
ATOM   1650 C CD1 . LEU A 1 230 ? 32.253 38.760 28.074 1.00 16.37 ? 260 LEU A CD1 1 
ATOM   1651 C CD2 . LEU A 1 230 ? 29.802 38.419 27.675 1.00 15.02 ? 260 LEU A CD2 1 
ATOM   1652 N N   . ALA A 1 231 ? 28.380 42.665 29.755 1.00 21.06 ? 261 ALA A N   1 
ATOM   1653 C CA  . ALA A 1 231 ? 28.160 43.727 30.724 1.00 18.53 ? 261 ALA A CA  1 
ATOM   1654 C C   . ALA A 1 231 ? 29.246 43.709 31.792 1.00 18.63 ? 261 ALA A C   1 
ATOM   1655 O O   . ALA A 1 231 ? 29.779 42.654 32.147 1.00 19.39 ? 261 ALA A O   1 
ATOM   1656 C CB  . ALA A 1 231 ? 26.785 43.579 31.374 1.00 16.72 ? 261 ALA A CB  1 
ATOM   1657 N N   . THR A 1 232 ? 29.589 44.895 32.288 1.00 18.77 ? 262 THR A N   1 
ATOM   1658 C CA  . THR A 1 232 ? 30.510 44.998 33.408 1.00 21.62 ? 262 THR A CA  1 
ATOM   1659 C C   . THR A 1 232 ? 29.776 44.720 34.714 1.00 23.79 ? 262 THR A C   1 
ATOM   1660 O O   . THR A 1 232 ? 28.544 44.760 34.785 1.00 17.01 ? 262 THR A O   1 
ATOM   1661 C CB  . THR A 1 232 ? 31.153 46.384 33.478 1.00 23.20 ? 262 THR A CB  1 
ATOM   1662 O OG1 . THR A 1 232 ? 30.127 47.379 33.578 1.00 23.15 ? 262 THR A OG1 1 
ATOM   1663 C CG2 . THR A 1 232 ? 32.015 46.651 32.251 1.00 21.09 ? 262 THR A CG2 1 
ATOM   1664 N N   . LEU A 1 233 ? 30.555 44.439 35.760 1.00 18.78 ? 263 LEU A N   1 
ATOM   1665 C CA  . LEU A 1 233 ? 29.957 44.219 37.072 1.00 20.51 ? 263 LEU A CA  1 
ATOM   1666 C C   . LEU A 1 233 ? 29.228 45.465 37.557 1.00 23.19 ? 263 LEU A C   1 
ATOM   1667 O O   . LEU A 1 233 ? 28.155 45.366 38.161 1.00 20.69 ? 263 LEU A O   1 
ATOM   1668 C CB  . LEU A 1 233 ? 31.027 43.792 38.079 1.00 19.12 ? 263 LEU A CB  1 
ATOM   1669 C CG  . LEU A 1 233 ? 30.583 43.653 39.541 1.00 22.49 ? 263 LEU A CG  1 
ATOM   1670 C CD1 . LEU A 1 233 ? 29.462 42.629 39.692 1.00 21.08 ? 263 LEU A CD1 1 
ATOM   1671 C CD2 . LEU A 1 233 ? 31.766 43.297 40.433 1.00 25.98 ? 263 LEU A CD2 1 
ATOM   1672 N N   . ALA A 1 234 ? 29.786 46.649 37.290 1.00 19.52 ? 264 ALA A N   1 
ATOM   1673 C CA  . ALA A 1 234 ? 29.147 47.886 37.731 1.00 19.97 ? 264 ALA A CA  1 
ATOM   1674 C C   . ALA A 1 234 ? 27.766 48.051 37.104 1.00 26.03 ? 264 ALA A C   1 
ATOM   1675 O O   . ALA A 1 234 ? 26.778 48.302 37.806 1.00 26.38 ? 264 ALA A O   1 
ATOM   1676 C CB  . ALA A 1 234 ? 30.039 49.083 37.403 1.00 19.88 ? 264 ALA A CB  1 
ATOM   1677 N N   . ASP A 1 235 ? 27.673 47.898 35.779 1.00 21.17 ? 265 ASP A N   1 
ATOM   1678 C CA  . ASP A 1 235 ? 26.390 48.071 35.102 1.00 23.36 ? 265 ASP A CA  1 
ATOM   1679 C C   . ASP A 1 235 ? 25.392 46.992 35.503 1.00 19.95 ? 265 ASP A C   1 
ATOM   1680 O O   . ASP A 1 235 ? 24.212 47.287 35.736 1.00 26.61 ? 265 ASP A O   1 
ATOM   1681 C CB  . ASP A 1 235 ? 26.586 48.071 33.587 1.00 23.56 ? 265 ASP A CB  1 
ATOM   1682 C CG  . ASP A 1 235 ? 27.417 49.241 33.112 1.00 27.11 ? 265 ASP A CG  1 
ATOM   1683 O OD1 . ASP A 1 235 ? 27.475 50.261 33.832 1.00 28.34 ? 265 ASP A OD1 1 
ATOM   1684 O OD2 . ASP A 1 235 ? 28.008 49.143 32.017 1.00 28.39 ? 265 ASP A OD2 1 
ATOM   1685 N N   . SER A 1 236 ? 25.839 45.736 35.576 1.00 19.34 ? 266 SER A N   1 
ATOM   1686 C CA  . SER A 1 236 ? 24.926 44.656 35.940 1.00 21.67 ? 266 SER A CA  1 
ATOM   1687 C C   . SER A 1 236 ? 24.427 44.818 37.370 1.00 23.01 ? 266 SER A C   1 
ATOM   1688 O O   . SER A 1 236 ? 23.249 44.577 37.651 1.00 21.17 ? 266 SER A O   1 
ATOM   1689 C CB  . SER A 1 236 ? 25.609 43.301 35.755 1.00 18.76 ? 266 SER A CB  1 
ATOM   1690 O OG  . SER A 1 236 ? 24.673 42.237 35.837 1.00 19.15 ? 266 SER A OG  1 
ATOM   1691 N N   . ALA A 1 237 ? 25.301 45.255 38.281 1.00 22.05 ? 267 ALA A N   1 
ATOM   1692 C CA  . ALA A 1 237 ? 24.896 45.470 39.665 1.00 22.53 ? 267 ALA A CA  1 
ATOM   1693 C C   . ALA A 1 237 ? 23.954 46.660 39.785 1.00 28.95 ? 267 ALA A C   1 
ATOM   1694 O O   . ALA A 1 237 ? 23.016 46.635 40.592 1.00 19.73 ? 267 ALA A O   1 
ATOM   1695 C CB  . ALA A 1 237 ? 26.128 45.666 40.548 1.00 24.60 ? 267 ALA A CB  1 
ATOM   1696 N N   . ALA A 1 238 ? 24.176 47.710 38.987 1.00 22.42 ? 268 ALA A N   1 
ATOM   1697 C CA  . ALA A 1 238 ? 23.220 48.812 38.960 1.00 26.71 ? 268 ALA A CA  1 
ATOM   1698 C C   . ALA A 1 238 ? 21.857 48.340 38.464 1.00 27.42 ? 268 ALA A C   1 
ATOM   1699 O O   . ALA A 1 238 ? 20.817 48.709 39.029 1.00 26.51 ? 268 ALA A O   1 
ATOM   1700 C CB  . ALA A 1 238 ? 23.751 49.954 38.089 1.00 23.35 ? 268 ALA A CB  1 
ATOM   1701 N N   . SER A 1 239 ? 21.842 47.518 37.412 1.00 21.46 ? 269 SER A N   1 
ATOM   1702 C CA  . SER A 1 239 ? 20.586 46.954 36.927 1.00 23.88 ? 269 SER A CA  1 
ATOM   1703 C C   . SER A 1 239 ? 19.890 46.143 38.016 1.00 30.42 ? 269 SER A C   1 
ATOM   1704 O O   . SER A 1 239 ? 18.678 46.279 38.239 1.00 31.09 ? 269 SER A O   1 
ATOM   1705 C CB  . SER A 1 239 ? 20.849 46.088 35.696 1.00 22.60 ? 269 SER A CB  1 
ATOM   1706 O OG  . SER A 1 239 ? 19.720 45.289 35.392 1.00 37.02 ? 269 SER A OG  1 
ATOM   1707 N N   . GLY A 1 240 ? 20.652 45.297 38.712 1.00 27.06 ? 270 GLY A N   1 
ATOM   1708 C CA  . GLY A 1 240 ? 20.077 44.501 39.784 1.00 27.00 ? 270 GLY A CA  1 
ATOM   1709 C C   . GLY A 1 240 ? 19.500 45.352 40.899 1.00 26.87 ? 270 GLY A C   1 
ATOM   1710 O O   . GLY A 1 240 ? 18.434 45.044 41.440 1.00 26.64 ? 270 GLY A O   1 
ATOM   1711 N N   . GLU A 1 241 ? 20.194 46.435 41.259 1.00 24.12 ? 271 GLU A N   1 
ATOM   1712 C CA  . GLU A 1 241 ? 19.666 47.344 42.272 1.00 26.41 ? 271 GLU A CA  1 
ATOM   1713 C C   . GLU A 1 241 ? 18.391 48.024 41.795 1.00 32.79 ? 271 GLU A C   1 
ATOM   1714 O O   . GLU A 1 241 ? 17.491 48.298 42.600 1.00 27.75 ? 271 GLU A O   1 
ATOM   1715 C CB  . GLU A 1 241 ? 20.715 48.390 42.650 1.00 24.50 ? 271 GLU A CB  1 
ATOM   1716 C CG  . GLU A 1 241 ? 20.237 49.360 43.719 1.00 35.67 ? 271 GLU A CG  1 
ATOM   1717 C CD  . GLU A 1 241 ? 21.376 50.049 44.438 1.00 44.52 ? 271 GLU A CD  1 
ATOM   1718 O OE1 . GLU A 1 241 ? 22.282 50.580 43.759 1.00 50.93 ? 271 GLU A OE1 1 
ATOM   1719 O OE2 . GLU A 1 241 ? 21.368 50.049 45.688 1.00 58.05 ? 271 GLU A OE2 1 
ATOM   1720 N N   . ARG A 1 242 ? 18.298 48.306 40.493 1.00 28.29 ? 272 ARG A N   1 
ATOM   1721 C CA  . ARG A 1 242 ? 17.058 48.845 39.944 1.00 31.85 ? 272 ARG A CA  1 
ATOM   1722 C C   . ARG A 1 242 ? 15.920 47.837 40.023 1.00 32.49 ? 272 ARG A C   1 
ATOM   1723 O O   . ARG A 1 242 ? 14.759 48.231 40.180 1.00 31.82 ? 272 ARG A O   1 
ATOM   1724 C CB  . ARG A 1 242 ? 17.263 49.292 38.497 1.00 29.80 ? 272 ARG A CB  1 
ATOM   1725 C CG  . ARG A 1 242 ? 17.996 50.612 38.366 1.00 35.23 ? 272 ARG A CG  1 
ATOM   1726 C CD  . ARG A 1 242 ? 17.854 51.180 36.970 1.00 36.81 ? 272 ARG A CD  1 
ATOM   1727 N NE  . ARG A 1 242 ? 18.436 50.309 35.958 1.00 34.70 ? 272 ARG A NE  1 
ATOM   1728 C CZ  . ARG A 1 242 ? 19.713 50.330 35.606 1.00 33.38 ? 272 ARG A CZ  1 
ATOM   1729 N NH1 . ARG A 1 242 ? 20.572 51.159 36.176 1.00 28.26 ? 272 ARG A NH1 1 
ATOM   1730 N NH2 . ARG A 1 242 ? 20.139 49.497 34.663 1.00 32.69 ? 272 ARG A NH2 1 
ATOM   1731 N N   . LEU A 1 243 ? 16.219 46.542 39.898 1.00 27.50 ? 273 LEU A N   1 
ATOM   1732 C CA  . LEU A 1 243 ? 15.168 45.541 40.069 1.00 28.20 ? 273 LEU A CA  1 
ATOM   1733 C C   . LEU A 1 243 ? 14.574 45.607 41.475 1.00 29.84 ? 273 LEU A C   1 
ATOM   1734 O O   . LEU A 1 243 ? 13.349 45.618 41.647 1.00 29.72 ? 273 LEU A O   1 
ATOM   1735 C CB  . LEU A 1 243 ? 15.713 44.143 39.772 1.00 23.88 ? 273 LEU A CB  1 
ATOM   1736 C CG  . LEU A 1 243 ? 14.687 43.013 39.892 1.00 27.10 ? 273 LEU A CG  1 
ATOM   1737 C CD1 . LEU A 1 243 ? 13.455 43.310 39.049 1.00 25.53 ? 273 LEU A CD1 1 
ATOM   1738 C CD2 . LEU A 1 243 ? 15.308 41.688 39.488 1.00 19.06 ? 273 LEU A CD2 1 
ATOM   1739 N N   . ASP A 1 244 ? 15.435 45.646 42.493 1.00 23.64 ? 274 ASP A N   1 
ATOM   1740 C CA  . ASP A 1 244 ? 15.038 45.832 43.884 1.00 23.86 ? 274 ASP A CA  1 
ATOM   1741 C C   . ASP A 1 244 ? 16.278 46.145 44.706 1.00 25.37 ? 274 ASP A C   1 
ATOM   1742 O O   . ASP A 1 244 ? 17.236 45.365 44.714 1.00 24.07 ? 274 ASP A O   1 
ATOM   1743 C CB  . ASP A 1 244 ? 14.330 44.589 44.435 1.00 25.85 ? 274 ASP A CB  1 
ATOM   1744 C CG  . ASP A 1 244 ? 13.635 44.844 45.778 1.00 30.56 ? 274 ASP A CG  1 
ATOM   1745 O OD1 . ASP A 1 244 ? 14.043 45.767 46.519 1.00 25.56 ? 274 ASP A OD1 1 
ATOM   1746 O OD2 . ASP A 1 244 ? 12.673 44.110 46.098 1.00 28.38 ? 274 ASP A OD2 1 
ATOM   1747 N N   . ALA A 1 245 ? 16.277 47.286 45.396 1.00 23.91 ? 275 ALA A N   1 
ATOM   1748 C CA  . ALA A 1 245 ? 17.444 47.673 46.180 1.00 27.42 ? 275 ALA A CA  1 
ATOM   1749 C C   . ALA A 1 245 ? 17.597 46.843 47.451 1.00 28.08 ? 275 ALA A C   1 
ATOM   1750 O O   . ALA A 1 245 ? 18.694 46.805 48.023 1.00 27.43 ? 275 ALA A O   1 
ATOM   1751 C CB  . ALA A 1 245 ? 17.369 49.162 46.527 1.00 34.12 ? 275 ALA A CB  1 
ATOM   1752 N N   . ASP A 1 246 ? 16.531 46.179 47.896 1.00 28.94 ? 276 ASP A N   1 
ATOM   1753 C CA  . ASP A 1 246 ? 16.534 45.381 49.121 1.00 23.32 ? 276 ASP A CA  1 
ATOM   1754 C C   . ASP A 1 246 ? 16.836 43.932 48.750 1.00 24.88 ? 276 ASP A C   1 
ATOM   1755 O O   . ASP A 1 246 ? 15.956 43.204 48.282 1.00 25.45 ? 276 ASP A O   1 
ATOM   1756 C CB  . ASP A 1 246 ? 15.194 45.515 49.838 1.00 26.52 ? 276 ASP A CB  1 
ATOM   1757 C CG  . ASP A 1 246 ? 15.166 44.801 51.177 1.00 25.53 ? 276 ASP A CG  1 
ATOM   1758 O OD1 . ASP A 1 246 ? 16.191 44.207 51.570 1.00 36.45 ? 276 ASP A OD1 1 
ATOM   1759 O OD2 . ASP A 1 246 ? 14.112 44.841 51.847 1.00 43.69 ? 276 ASP A OD2 1 
ATOM   1760 N N   . LEU A 1 247 ? 18.082 43.509 48.979 1.00 21.23 ? 277 LEU A N   1 
ATOM   1761 C CA  . LEU A 1 247 ? 18.481 42.152 48.617 1.00 22.82 ? 277 LEU A CA  1 
ATOM   1762 C C   . LEU A 1 247 ? 17.694 41.102 49.387 1.00 22.13 ? 277 LEU A C   1 
ATOM   1763 O O   . LEU A 1 247 ? 17.369 40.045 48.836 1.00 18.06 ? 277 LEU A O   1 
ATOM   1764 C CB  . LEU A 1 247 ? 19.980 41.963 48.861 1.00 22.00 ? 277 LEU A CB  1 
ATOM   1765 C CG  . LEU A 1 247 ? 20.563 40.582 48.558 1.00 25.53 ? 277 LEU A CG  1 
ATOM   1766 C CD1 . LEU A 1 247 ? 20.241 40.165 47.132 1.00 17.46 ? 277 LEU A CD1 1 
ATOM   1767 C CD2 . LEU A 1 247 ? 22.067 40.568 48.798 1.00 18.01 ? 277 LEU A CD2 1 
ATOM   1768 N N   . SER A 1 248 ? 17.364 41.381 50.651 1.00 22.16 ? 278 SER A N   1 
ATOM   1769 C CA  . SER A 1 248 ? 16.595 40.434 51.453 1.00 26.77 ? 278 SER A CA  1 
ATOM   1770 C C   . SER A 1 248 ? 15.246 40.136 50.817 1.00 21.09 ? 278 SER A C   1 
ATOM   1771 O O   . SER A 1 248 ? 14.827 38.974 50.744 1.00 20.97 ? 278 SER A O   1 
ATOM   1772 C CB  . SER A 1 248 ? 16.400 40.981 52.868 1.00 27.73 ? 278 SER A CB  1 
ATOM   1773 O OG  . SER A 1 248 ? 17.623 41.005 53.579 1.00 49.37 ? 278 SER A OG  1 
ATOM   1774 N N   . ARG A 1 249 ? 14.545 41.176 50.361 1.00 19.79 ? 279 ARG A N   1 
ATOM   1775 C CA  . ARG A 1 249 ? 13.263 40.963 49.698 1.00 22.80 ? 279 ARG A CA  1 
ATOM   1776 C C   . ARG A 1 249 ? 13.432 40.147 48.421 1.00 19.01 ? 279 ARG A C   1 
ATOM   1777 O O   . ARG A 1 249 ? 12.609 39.275 48.120 1.00 20.73 ? 279 ARG A O   1 
ATOM   1778 C CB  . ARG A 1 249 ? 12.596 42.307 49.405 1.00 21.73 ? 279 ARG A CB  1 
ATOM   1779 C CG  . ARG A 1 249 ? 11.195 42.197 48.832 1.00 24.71 ? 279 ARG A CG  1 
ATOM   1780 C CD  . ARG A 1 249 ? 10.490 43.532 48.924 1.00 26.28 ? 279 ARG A CD  1 
ATOM   1781 N NE  . ARG A 1 249 ? 11.396 44.622 48.589 1.00 28.24 ? 279 ARG A NE  1 
ATOM   1782 C CZ  . ARG A 1 249 ? 11.124 45.906 48.774 1.00 38.82 ? 279 ARG A CZ  1 
ATOM   1783 N NH1 . ARG A 1 249 ? 9.973  46.300 49.296 1.00 36.35 ? 279 ARG A NH1 1 
ATOM   1784 N NH2 . ARG A 1 249 ? 12.030 46.817 48.432 1.00 33.05 ? 279 ARG A NH2 1 
ATOM   1785 N N   . LEU A 1 250 ? 14.503 40.405 47.663 1.00 18.76 ? 280 LEU A N   1 
ATOM   1786 C CA  . LEU A 1 250 ? 14.789 39.587 46.487 1.00 18.37 ? 280 LEU A CA  1 
ATOM   1787 C C   . LEU A 1 250 ? 14.963 38.122 46.864 1.00 17.89 ? 280 LEU A C   1 
ATOM   1788 O O   . LEU A 1 250 ? 14.434 37.231 46.187 1.00 17.75 ? 280 LEU A O   1 
ATOM   1789 C CB  . LEU A 1 250 ? 16.040 40.096 45.771 1.00 18.18 ? 280 LEU A CB  1 
ATOM   1790 C CG  . LEU A 1 250 ? 15.884 41.338 44.897 1.00 24.89 ? 280 LEU A CG  1 
ATOM   1791 C CD1 . LEU A 1 250 ? 17.244 41.828 44.423 1.00 20.22 ? 280 LEU A CD1 1 
ATOM   1792 C CD2 . LEU A 1 250 ? 14.976 41.045 43.710 1.00 19.91 ? 280 LEU A CD2 1 
ATOM   1793 N N   . ARG A 1 251 ? 15.699 37.851 47.945 1.00 17.69 ? 281 ARG A N   1 
ATOM   1794 C CA  . ARG A 1 251 ? 15.929 36.471 48.354 1.00 18.90 ? 281 ARG A CA  1 
ATOM   1795 C C   . ARG A 1 251 ? 14.681 35.822 48.936 1.00 19.90 ? 281 ARG A C   1 
ATOM   1796 O O   . ARG A 1 251 ? 14.598 34.590 48.967 1.00 21.68 ? 281 ARG A O   1 
ATOM   1797 C CB  . ARG A 1 251 ? 17.075 36.390 49.366 1.00 17.11 ? 281 ARG A CB  1 
ATOM   1798 C CG  . ARG A 1 251 ? 18.460 36.341 48.736 1.00 16.80 ? 281 ARG A CG  1 
ATOM   1799 C CD  . ARG A 1 251 ? 19.479 35.762 49.710 1.00 17.39 ? 281 ARG A CD  1 
ATOM   1800 N NE  . ARG A 1 251 ? 20.729 35.396 49.054 1.00 16.30 ? 281 ARG A NE  1 
ATOM   1801 C CZ  . ARG A 1 251 ? 21.861 36.079 49.158 1.00 16.36 ? 281 ARG A CZ  1 
ATOM   1802 N NH1 . ARG A 1 251 ? 21.946 37.169 49.902 1.00 16.72 ? 281 ARG A NH1 1 
ATOM   1803 N NH2 . ARG A 1 251 ? 22.935 35.658 48.496 1.00 18.98 ? 281 ARG A NH2 1 
ATOM   1804 N N   . SER A 1 252 ? 13.714 36.610 49.398 1.00 21.46 ? 282 SER A N   1 
ATOM   1805 C CA  . SER A 1 252 ? 12.473 36.058 49.919 1.00 19.64 ? 282 SER A CA  1 
ATOM   1806 C C   . SER A 1 252 ? 11.380 35.974 48.857 1.00 20.30 ? 282 SER A C   1 
ATOM   1807 O O   . SER A 1 252 ? 10.229 35.675 49.188 1.00 23.79 ? 282 SER A O   1 
ATOM   1808 C CB  . SER A 1 252 ? 11.989 36.878 51.124 1.00 19.39 ? 282 SER A CB  1 
ATOM   1809 O OG  . SER A 1 252 ? 11.692 38.214 50.760 1.00 31.84 ? 282 SER A OG  1 
ATOM   1810 N N   . THR A 1 253 ? 11.716 36.216 47.591 1.00 19.08 ? 283 THR A N   1 
ATOM   1811 C CA  . THR A 1 253 ? 10.750 36.134 46.503 1.00 18.60 ? 283 THR A CA  1 
ATOM   1812 C C   . THR A 1 253 ? 10.769 34.735 45.894 1.00 19.44 ? 283 THR A C   1 
ATOM   1813 O O   . THR A 1 253 ? 11.841 34.182 45.628 1.00 17.75 ? 283 THR A O   1 
ATOM   1814 C CB  . THR A 1 253 ? 11.054 37.184 45.432 1.00 18.78 ? 283 THR A CB  1 
ATOM   1815 O OG1 . THR A 1 253 ? 11.094 38.485 46.034 1.00 19.61 ? 283 THR A OG1 1 
ATOM   1816 C CG2 . THR A 1 253 ? 9.988  37.169 44.342 1.00 19.18 ? 283 THR A CG2 1 
ATOM   1817 N N   . ASP A 1 254 ? 9.581  34.171 45.686 1.00 19.80 ? 284 ASP A N   1 
ATOM   1818 C CA  . ASP A 1 254 ? 9.459  32.853 45.079 1.00 18.31 ? 284 ASP A CA  1 
ATOM   1819 C C   . ASP A 1 254 ? 10.172 32.826 43.729 1.00 18.07 ? 284 ASP A C   1 
ATOM   1820 O O   . ASP A 1 254 ? 10.069 33.782 42.951 1.00 18.33 ? 284 ASP A O   1 
ATOM   1821 C CB  . ASP A 1 254 ? 7.981  32.489 44.909 1.00 21.48 ? 284 ASP A CB  1 
ATOM   1822 C CG  . ASP A 1 254 ? 7.748  31.445 43.825 1.00 22.06 ? 284 ASP A CG  1 
ATOM   1823 O OD1 . ASP A 1 254 ? 8.038  30.255 44.059 1.00 21.87 ? 284 ASP A OD1 1 
ATOM   1824 O OD2 . ASP A 1 254 ? 7.261  31.815 42.734 1.00 26.35 ? 284 ASP A OD2 1 
ATOM   1825 N N   . PRO A 1 255 ? 10.900 31.752 43.418 1.00 19.72 ? 285 PRO A N   1 
ATOM   1826 C CA  . PRO A 1 255 ? 11.727 31.765 42.199 1.00 17.36 ? 285 PRO A CA  1 
ATOM   1827 C C   . PRO A 1 255 ? 10.928 31.883 40.910 1.00 23.55 ? 285 PRO A C   1 
ATOM   1828 O O   . PRO A 1 255 ? 11.370 32.582 39.993 1.00 18.87 ? 285 PRO A O   1 
ATOM   1829 C CB  . PRO A 1 255 ? 12.497 30.437 42.285 1.00 19.69 ? 285 PRO A CB  1 
ATOM   1830 C CG  . PRO A 1 255 ? 11.726 29.592 43.253 1.00 16.99 ? 285 PRO A CG  1 
ATOM   1831 C CD  . PRO A 1 255 ? 11.108 30.540 44.227 1.00 18.80 ? 285 PRO A CD  1 
ATOM   1832 N N   . ALA A 1 256 ? 9.768  31.231 40.802 1.00 21.70 ? 286 ALA A N   1 
ATOM   1833 C CA  . ALA A 1 256 ? 8.970  31.377 39.585 1.00 21.27 ? 286 ALA A CA  1 
ATOM   1834 C C   . ALA A 1 256 ? 8.500  32.816 39.403 1.00 19.98 ? 286 ALA A C   1 
ATOM   1835 O O   . ALA A 1 256 ? 8.512  33.346 38.286 1.00 19.24 ? 286 ALA A O   1 
ATOM   1836 C CB  . ALA A 1 256 ? 7.775  30.427 39.614 1.00 18.87 ? 286 ALA A CB  1 
ATOM   1837 N N   . THR A 1 257 ? 8.101  33.467 40.498 1.00 19.23 ? 287 THR A N   1 
ATOM   1838 C CA  . THR A 1 257 ? 7.658  34.858 40.436 1.00 20.76 ? 287 THR A CA  1 
ATOM   1839 C C   . THR A 1 257 ? 8.773  35.770 39.937 1.00 20.09 ? 287 THR A C   1 
ATOM   1840 O O   . THR A 1 257 ? 8.565  36.597 39.039 1.00 19.95 ? 287 THR A O   1 
ATOM   1841 C CB  . THR A 1 257 ? 7.177  35.308 41.818 1.00 19.99 ? 287 THR A CB  1 
ATOM   1842 O OG1 . THR A 1 257 ? 6.178  34.399 42.298 1.00 20.19 ? 287 THR A OG1 1 
ATOM   1843 C CG2 . THR A 1 257 ? 6.593  36.716 41.753 1.00 20.74 ? 287 THR A CG2 1 
ATOM   1844 N N   . LEU A 1 258 ? 9.969  35.632 40.514 1.00 18.95 ? 288 LEU A N   1 
ATOM   1845 C CA  . LEU A 1 258 ? 11.092 36.472 40.113 1.00 22.95 ? 288 LEU A CA  1 
ATOM   1846 C C   . LEU A 1 258 ? 11.521 36.175 38.680 1.00 18.62 ? 288 LEU A C   1 
ATOM   1847 O O   . LEU A 1 258 ? 11.863 37.093 37.925 1.00 20.17 ? 288 LEU A O   1 
ATOM   1848 C CB  . LEU A 1 258 ? 12.257 36.268 41.081 1.00 18.21 ? 288 LEU A CB  1 
ATOM   1849 C CG  . LEU A 1 258 ? 13.460 37.202 40.958 1.00 21.30 ? 288 LEU A CG  1 
ATOM   1850 C CD1 . LEU A 1 258 ? 13.053 38.645 41.216 1.00 25.29 ? 288 LEU A CD1 1 
ATOM   1851 C CD2 . LEU A 1 258 ? 14.548 36.773 41.927 1.00 22.19 ? 288 LEU A CD2 1 
ATOM   1852 N N   . MET A 1 259 ? 11.505 34.898 38.290 1.00 21.34 ? 289 MET A N   1 
ATOM   1853 C CA  . MET A 1 259 ? 11.835 34.520 36.919 1.00 22.02 ? 289 MET A CA  1 
ATOM   1854 C C   . MET A 1 259 ? 10.877 35.166 35.928 1.00 23.76 ? 289 MET A C   1 
ATOM   1855 O O   . MET A 1 259 ? 11.302 35.720 34.909 1.00 20.54 ? 289 MET A O   1 
ATOM   1856 C CB  . MET A 1 259 ? 11.800 32.999 36.776 1.00 26.18 ? 289 MET A CB  1 
ATOM   1857 C CG  . MET A 1 259 ? 13.062 32.286 37.222 1.00 35.91 ? 289 MET A CG  1 
ATOM   1858 S SD  . MET A 1 259 ? 14.299 32.194 35.904 1.00 34.15 ? 289 MET A SD  1 
ATOM   1859 C CE  . MET A 1 259 ? 13.313 31.543 34.574 1.00 17.36 ? 289 MET A CE  1 
ATOM   1860 N N   . ALA A 1 260 ? 9.574  35.096 36.209 1.00 20.95 ? 290 ALA A N   1 
ATOM   1861 C CA  . ALA A 1 260 ? 8.591  35.716 35.328 1.00 24.21 ? 290 ALA A CA  1 
ATOM   1862 C C   . ALA A 1 260 ? 8.768  37.229 35.280 1.00 27.48 ? 290 ALA A C   1 
ATOM   1863 O O   . ALA A 1 260 ? 8.679  37.843 34.207 1.00 33.23 ? 290 ALA A O   1 
ATOM   1864 C CB  . ALA A 1 260 ? 7.179  35.351 35.787 1.00 20.68 ? 290 ALA A CB  1 
ATOM   1865 N N   . ARG A 1 261 ? 9.018  37.846 36.437 1.00 24.83 ? 291 ARG A N   1 
ATOM   1866 C CA  . ARG A 1 261 ? 9.213  39.291 36.488 1.00 30.90 ? 291 ARG A CA  1 
ATOM   1867 C C   . ARG A 1 261 ? 10.389 39.709 35.614 1.00 35.69 ? 291 ARG A C   1 
ATOM   1868 O O   . ARG A 1 261 ? 10.294 40.668 34.838 1.00 38.12 ? 291 ARG A O   1 
ATOM   1869 C CB  . ARG A 1 261 ? 9.423  39.733 37.940 1.00 32.88 ? 291 ARG A CB  1 
ATOM   1870 C CG  . ARG A 1 261 ? 8.982  41.160 38.250 1.00 40.04 ? 291 ARG A CG  1 
ATOM   1871 C CD  . ARG A 1 261 ? 9.344  41.551 39.685 1.00 47.89 ? 291 ARG A CD  1 
ATOM   1872 N NE  . ARG A 1 261 ? 8.560  40.830 40.682 1.00 49.89 ? 291 ARG A NE  1 
ATOM   1873 C CZ  . ARG A 1 261 ? 8.767  40.894 41.992 1.00 54.09 ? 291 ARG A CZ  1 
ATOM   1874 N NH1 . ARG A 1 261 ? 9.750  41.617 42.502 1.00 56.36 ? 291 ARG A NH1 1 
ATOM   1875 N NH2 . ARG A 1 261 ? 7.967  40.216 42.811 1.00 36.77 ? 291 ARG A NH2 1 
ATOM   1876 N N   . ALA A 1 262 ? 11.504 38.980 35.713 1.00 28.18 ? 292 ALA A N   1 
ATOM   1877 C CA  . ALA A 1 262 ? 12.673 39.299 34.900 1.00 32.53 ? 292 ALA A CA  1 
ATOM   1878 C C   . ALA A 1 262 ? 12.425 39.002 33.427 1.00 32.36 ? 292 ALA A C   1 
ATOM   1879 O O   . ALA A 1 262 ? 12.875 39.754 32.555 1.00 37.83 ? 292 ALA A O   1 
ATOM   1880 C CB  . ALA A 1 262 ? 13.892 38.529 35.404 1.00 23.98 ? 292 ALA A CB  1 
ATOM   1881 N N   . ASP A 1 263 ? 11.707 37.916 33.131 1.00 36.30 ? 293 ASP A N   1 
ATOM   1882 C CA  . ASP A 1 263 ? 11.431 37.556 31.744 1.00 42.00 ? 293 ASP A CA  1 
ATOM   1883 C C   . ASP A 1 263 ? 10.578 38.615 31.053 1.00 45.55 ? 293 ASP A C   1 
ATOM   1884 O O   . ASP A 1 263 ? 10.776 38.907 29.866 1.00 46.71 ? 293 ASP A O   1 
ATOM   1885 C CB  . ASP A 1 263 ? 10.744 36.188 31.690 1.00 40.28 ? 293 ASP A CB  1 
ATOM   1886 C CG  . ASP A 1 263 ? 10.231 35.840 30.297 1.00 54.11 ? 293 ASP A CG  1 
ATOM   1887 O OD1 . ASP A 1 263 ? 11.073 35.477 29.456 1.00 56.32 ? 293 ASP A OD1 1 
ATOM   1888 O OD2 . ASP A 1 263 ? 9.004  35.913 30.042 1.00 57.70 ? 293 ASP A OD2 1 
ATOM   1889 N N   . ALA A 1 264 ? 9.631  39.212 31.782 1.00 44.92 ? 294 ALA A N   1 
ATOM   1890 C CA  . ALA A 1 264 ? 8.786  40.238 31.176 1.00 50.20 ? 294 ALA A CA  1 
ATOM   1891 C C   . ALA A 1 264 ? 9.606  41.425 30.686 1.00 48.67 ? 294 ALA A C   1 
ATOM   1892 O O   . ALA A 1 264 ? 9.222  42.084 29.714 1.00 58.17 ? 294 ALA A O   1 
ATOM   1893 C CB  . ALA A 1 264 ? 7.714  40.700 32.164 1.00 38.20 ? 294 ALA A CB  1 
ATOM   1894 N N   . ALA A 1 265 ? 10.747 41.693 31.322 1.00 43.43 ? 295 ALA A N   1 
ATOM   1895 C CA  . ALA A 1 265 ? 11.600 42.815 30.951 1.00 45.07 ? 295 ALA A CA  1 
ATOM   1896 C C   . ALA A 1 265 ? 12.546 42.497 29.798 1.00 53.80 ? 295 ALA A C   1 
ATOM   1897 O O   . ALA A 1 265 ? 13.262 43.396 29.342 1.00 50.01 ? 295 ALA A O   1 
ATOM   1898 C CB  . ALA A 1 265 ? 12.405 43.280 32.163 1.00 46.17 ? 295 ALA A CB  1 
ATOM   1899 N N   . ARG A 1 266 ? 12.576 41.254 29.322 1.00 50.13 ? 296 ARG A N   1 
ATOM   1900 C CA  . ARG A 1 266 ? 13.452 40.898 28.218 1.00 42.81 ? 296 ARG A CA  1 
ATOM   1901 C C   . ARG A 1 266 ? 13.038 41.621 26.939 1.00 50.62 ? 296 ARG A C   1 
ATOM   1902 O O   . ARG A 1 266 ? 11.861 41.934 26.743 1.00 47.03 ? 296 ARG A O   1 
ATOM   1903 C CB  . ARG A 1 266 ? 13.427 39.393 27.971 1.00 43.19 ? 296 ARG A CB  1 
ATOM   1904 C CG  . ARG A 1 266 ? 14.256 38.581 28.942 1.00 45.02 ? 296 ARG A CG  1 
ATOM   1905 C CD  . ARG A 1 266 ? 14.249 37.113 28.570 1.00 34.19 ? 296 ARG A CD  1 
ATOM   1906 N NE  . ARG A 1 266 ? 15.241 36.375 29.338 1.00 45.22 ? 296 ARG A NE  1 
ATOM   1907 C CZ  . ARG A 1 266 ? 16.481 36.142 28.932 1.00 38.42 ? 296 ARG A CZ  1 
ATOM   1908 N NH1 . ARG A 1 266 ? 16.910 36.546 27.746 1.00 28.46 ? 296 ARG A NH1 1 
ATOM   1909 N NH2 . ARG A 1 266 ? 17.314 35.489 29.737 1.00 37.46 ? 296 ARG A NH2 1 
ATOM   1910 N N   . PRO A 1 267 ? 13.990 41.903 26.052 1.00 47.34 ? 297 PRO A N   1 
ATOM   1911 C CA  . PRO A 1 267 ? 13.636 42.460 24.741 1.00 51.29 ? 297 PRO A CA  1 
ATOM   1912 C C   . PRO A 1 267 ? 13.056 41.387 23.835 1.00 50.19 ? 297 PRO A C   1 
ATOM   1913 O O   . PRO A 1 267 ? 13.539 40.252 23.800 1.00 53.10 ? 297 PRO A O   1 
ATOM   1914 C CB  . PRO A 1 267 ? 14.976 42.977 24.195 1.00 55.76 ? 297 PRO A CB  1 
ATOM   1915 C CG  . PRO A 1 267 ? 15.932 42.958 25.378 1.00 51.66 ? 297 PRO A CG  1 
ATOM   1916 C CD  . PRO A 1 267 ? 15.447 41.856 26.258 1.00 48.10 ? 297 PRO A CD  1 
ATOM   1917 N N   . ALA A 1 268 ? 12.008 41.759 23.095 1.00 55.84 ? 298 ALA A N   1 
ATOM   1918 C CA  . ALA A 1 268 ? 11.418 40.830 22.137 1.00 60.95 ? 298 ALA A CA  1 
ATOM   1919 C C   . ALA A 1 268 ? 12.302 40.632 20.911 1.00 64.19 ? 298 ALA A C   1 
ATOM   1920 O O   . ALA A 1 268 ? 12.313 39.541 20.328 1.00 67.04 ? 298 ALA A O   1 
ATOM   1921 C CB  . ALA A 1 268 ? 10.034 41.320 21.714 1.00 57.58 ? 298 ALA A CB  1 
ATOM   1922 N N   . SER A 1 269 ? 13.060 41.655 20.527 1.00 57.23 ? 299 SER A N   1 
ATOM   1923 C CA  . SER A 1 269 ? 13.993 41.591 19.414 1.00 53.86 ? 299 SER A CA  1 
ATOM   1924 C C   . SER A 1 269 ? 15.416 41.638 19.948 1.00 49.91 ? 299 SER A C   1 
ATOM   1925 O O   . SER A 1 269 ? 15.703 42.351 20.917 1.00 51.95 ? 299 SER A O   1 
ATOM   1926 C CB  . SER A 1 269 ? 13.747 42.748 18.437 1.00 51.10 ? 299 SER A CB  1 
ATOM   1927 O OG  . SER A 1 269 ? 13.590 43.981 19.120 1.00 62.96 ? 299 SER A OG  1 
ATOM   1928 N N   . ARG A 1 270 ? 16.304 40.894 19.306 1.00 43.56 ? 300 ARG A N   1 
ATOM   1929 C CA  . ARG A 1 270 ? 17.680 40.775 19.763 1.00 38.05 ? 300 ARG A CA  1 
ATOM   1930 C C   . ARG A 1 270 ? 18.575 41.845 19.141 1.00 31.59 ? 300 ARG A C   1 
ATOM   1931 O O   . ARG A 1 270 ? 18.779 41.863 17.923 1.00 28.88 ? 300 ARG A O   1 
ATOM   1932 C CB  . ARG A 1 270 ? 18.198 39.386 19.432 1.00 31.57 ? 300 ARG A CB  1 
ATOM   1933 C CG  . ARG A 1 270 ? 19.608 39.119 19.965 1.00 35.68 ? 300 ARG A CG  1 
ATOM   1934 C CD  . ARG A 1 270 ? 19.673 37.686 20.453 1.00 36.50 ? 300 ARG A CD  1 
ATOM   1935 N NE  . ARG A 1 270 ? 20.982 37.093 20.249 1.00 30.19 ? 300 ARG A NE  1 
ATOM   1936 C CZ  . ARG A 1 270 ? 21.241 35.810 20.443 1.00 35.91 ? 300 ARG A CZ  1 
ATOM   1937 N NH1 . ARG A 1 270 ? 20.297 34.968 20.834 1.00 24.43 ? 300 ARG A NH1 1 
ATOM   1938 N NH2 . ARG A 1 270 ? 22.475 35.359 20.237 1.00 33.44 ? 300 ARG A NH2 1 
ATOM   1939 N N   . ASP A 1 271 ? 19.087 42.743 19.977 1.00 29.59 ? 301 ASP A N   1 
ATOM   1940 C CA  . ASP A 1 271 ? 20.012 43.781 19.546 1.00 29.06 ? 301 ASP A CA  1 
ATOM   1941 C C   . ASP A 1 271 ? 21.429 43.223 19.612 1.00 24.51 ? 301 ASP A C   1 
ATOM   1942 O O   . ASP A 1 271 ? 21.917 42.883 20.696 1.00 30.70 ? 301 ASP A O   1 
ATOM   1943 C CB  . ASP A 1 271 ? 19.864 45.023 20.429 1.00 26.90 ? 301 ASP A CB  1 
ATOM   1944 C CG  . ASP A 1 271 ? 20.618 46.227 19.894 1.00 26.23 ? 301 ASP A CG  1 
ATOM   1945 O OD1 . ASP A 1 271 ? 21.615 46.054 19.162 1.00 24.27 ? 301 ASP A OD1 1 
ATOM   1946 O OD2 . ASP A 1 271 ? 20.208 47.360 20.219 1.00 25.01 ? 301 ASP A OD2 1 
ATOM   1947 N N   . LEU A 1 272 ? 22.091 43.140 18.455 1.00 24.60 ? 302 LEU A N   1 
ATOM   1948 C CA  . LEU A 1 272 ? 23.432 42.565 18.394 1.00 25.61 ? 302 LEU A CA  1 
ATOM   1949 C C   . LEU A 1 272 ? 24.468 43.393 19.146 1.00 27.78 ? 302 LEU A C   1 
ATOM   1950 O O   . LEU A 1 272 ? 25.530 42.864 19.492 1.00 27.84 ? 302 LEU A O   1 
ATOM   1951 C CB  . LEU A 1 272 ? 23.871 42.402 16.938 1.00 31.64 ? 302 LEU A CB  1 
ATOM   1952 C CG  . LEU A 1 272 ? 23.013 41.500 16.052 1.00 31.29 ? 302 LEU A CG  1 
ATOM   1953 C CD1 . LEU A 1 272 ? 23.528 41.505 14.624 1.00 26.38 ? 302 LEU A CD1 1 
ATOM   1954 C CD2 . LEU A 1 272 ? 22.979 40.086 16.613 1.00 28.48 ? 302 LEU A CD2 1 
ATOM   1955 N N   . ARG A 1 273 ? 24.196 44.668 19.400 1.00 25.65 ? 303 ARG A N   1 
ATOM   1956 C CA  . ARG A 1 273 ? 25.153 45.534 20.074 1.00 27.38 ? 303 ARG A CA  1 
ATOM   1957 C C   . ARG A 1 273 ? 25.017 45.510 21.592 1.00 27.56 ? 303 ARG A C   1 
ATOM   1958 O O   . ARG A 1 273 ? 25.805 46.167 22.279 1.00 28.45 ? 303 ARG A O   1 
ATOM   1959 C CB  . ARG A 1 273 ? 25.006 46.971 19.570 1.00 33.94 ? 303 ARG A CB  1 
ATOM   1960 N N   . ARG A 1 274 ? 24.050 44.766 22.135 1.00 28.26 ? 304 ARG A N   1 
ATOM   1961 C CA  . ARG A 1 274 ? 23.831 44.760 23.570 1.00 25.86 ? 304 ARG A CA  1 
ATOM   1962 C C   . ARG A 1 274 ? 24.259 43.432 24.185 1.00 26.42 ? 304 ARG A C   1 
ATOM   1963 O O   . ARG A 1 274 ? 24.283 42.404 23.499 1.00 23.57 ? 304 ARG A O   1 
ATOM   1964 C CB  . ARG A 1 274 ? 22.355 45.004 23.907 1.00 25.11 ? 304 ARG A CB  1 
ATOM   1965 C CG  . ARG A 1 274 ? 21.789 46.285 23.310 1.00 30.35 ? 304 ARG A CG  1 
ATOM   1966 C CD  . ARG A 1 274 ? 20.343 46.487 23.731 1.00 29.71 ? 304 ARG A CD  1 
ATOM   1967 N NE  . ARG A 1 274 ? 20.213 46.782 25.153 1.00 33.82 ? 304 ARG A NE  1 
ATOM   1968 C CZ  . ARG A 1 274 ? 19.056 46.992 25.764 1.00 38.41 ? 304 ARG A CZ  1 
ATOM   1969 N NH1 . ARG A 1 274 ? 17.910 46.956 25.104 1.00 38.25 ? 304 ARG A NH1 1 
ATOM   1970 N NH2 . ARG A 1 274 ? 19.047 47.242 27.071 1.00 38.97 ? 304 ARG A NH2 1 
ATOM   1971 N N   . PRO A 1 275 ? 24.601 43.418 25.476 1.00 20.60 ? 305 PRO A N   1 
ATOM   1972 C CA  . PRO A 1 275 ? 24.839 42.143 26.158 1.00 25.94 ? 305 PRO A CA  1 
ATOM   1973 C C   . PRO A 1 275 ? 23.565 41.314 26.227 1.00 24.23 ? 305 PRO A C   1 
ATOM   1974 O O   . PRO A 1 275 ? 22.450 41.815 26.060 1.00 23.30 ? 305 PRO A O   1 
ATOM   1975 C CB  . PRO A 1 275 ? 25.306 42.562 27.560 1.00 23.35 ? 305 PRO A CB  1 
ATOM   1976 C CG  . PRO A 1 275 ? 25.725 43.986 27.427 1.00 24.62 ? 305 PRO A CG  1 
ATOM   1977 C CD  . PRO A 1 275 ? 24.862 44.573 26.350 1.00 23.39 ? 305 PRO A CD  1 
ATOM   1978 N N   . ARG A 1 276 ? 23.747 40.023 26.479 1.00 22.41 ? 306 ARG A N   1 
ATOM   1979 C CA  . ARG A 1 276 ? 22.607 39.153 26.717 1.00 23.89 ? 306 ARG A CA  1 
ATOM   1980 C C   . ARG A 1 276 ? 21.799 39.680 27.902 1.00 26.93 ? 306 ARG A C   1 
ATOM   1981 O O   . ARG A 1 276 ? 22.378 40.197 28.867 1.00 22.74 ? 306 ARG A O   1 
ATOM   1982 C CB  . ARG A 1 276 ? 23.070 37.724 27.007 1.00 24.21 ? 306 ARG A CB  1 
ATOM   1983 C CG  . ARG A 1 276 ? 23.943 37.084 25.935 1.00 20.03 ? 306 ARG A CG  1 
ATOM   1984 C CD  . ARG A 1 276 ? 24.507 35.767 26.451 1.00 18.44 ? 306 ARG A CD  1 
ATOM   1985 N NE  . ARG A 1 276 ? 25.244 35.026 25.437 1.00 16.76 ? 306 ARG A NE  1 
ATOM   1986 C CZ  . ARG A 1 276 ? 26.548 35.140 25.222 1.00 25.51 ? 306 ARG A CZ  1 
ATOM   1987 N NH1 . ARG A 1 276 ? 27.295 35.972 25.930 1.00 18.09 ? 306 ARG A NH1 1 
ATOM   1988 N NH2 . ARG A 1 276 ? 27.116 34.399 24.273 1.00 18.39 ? 306 ARG A NH2 1 
ATOM   1989 N N   . PRO A 1 277 ? 20.467 39.579 27.861 1.00 22.55 ? 307 PRO A N   1 
ATOM   1990 C CA  . PRO A 1 277 ? 19.663 40.028 29.014 1.00 21.67 ? 307 PRO A CA  1 
ATOM   1991 C C   . PRO A 1 277 ? 20.092 39.396 30.329 1.00 26.52 ? 307 PRO A C   1 
ATOM   1992 O O   . PRO A 1 277 ? 20.145 40.080 31.359 1.00 28.10 ? 307 PRO A O   1 
ATOM   1993 C CB  . PRO A 1 277 ? 18.238 39.618 28.621 1.00 24.94 ? 307 PRO A CB  1 
ATOM   1994 C CG  . PRO A 1 277 ? 18.259 39.574 27.123 1.00 30.14 ? 307 PRO A CG  1 
ATOM   1995 C CD  . PRO A 1 277 ? 19.633 39.089 26.751 1.00 25.42 ? 307 PRO A CD  1 
ATOM   1996 N N   . THR A 1 278 ? 20.397 38.101 30.318 1.00 24.18 ? 308 THR A N   1 
ATOM   1997 C CA  . THR A 1 278 ? 20.972 37.403 31.461 1.00 20.71 ? 308 THR A CA  1 
ATOM   1998 C C   . THR A 1 278 ? 22.114 36.544 30.942 1.00 20.25 ? 308 THR A C   1 
ATOM   1999 O O   . THR A 1 278 ? 21.918 35.732 30.032 1.00 28.89 ? 308 THR A O   1 
ATOM   2000 C CB  . THR A 1 278 ? 19.934 36.533 32.180 1.00 24.20 ? 308 THR A CB  1 
ATOM   2001 O OG1 . THR A 1 278 ? 19.425 35.545 31.270 1.00 20.44 ? 308 THR A OG1 1 
ATOM   2002 C CG2 . THR A 1 278 ? 18.779 37.379 32.710 1.00 21.54 ? 308 THR A CG2 1 
ATOM   2003 N N   . GLY A 1 279 ? 23.302 36.726 31.503 1.00 23.90 ? 309 GLY A N   1 
ATOM   2004 C CA  . GLY A 1 279 ? 24.438 35.948 31.079 1.00 21.60 ? 309 GLY A CA  1 
ATOM   2005 C C   . GLY A 1 279 ? 25.729 36.357 31.750 1.00 20.88 ? 309 GLY A C   1 
ATOM   2006 O O   . GLY A 1 279 ? 25.750 37.178 32.673 1.00 19.53 ? 309 GLY A O   1 
ATOM   2007 N N   . PRO A 1 280 ? 26.840 35.787 31.285 1.00 19.40 ? 310 PRO A N   1 
ATOM   2008 C CA  . PRO A 1 280 ? 28.132 36.073 31.913 1.00 18.38 ? 310 PRO A CA  1 
ATOM   2009 C C   . PRO A 1 280 ? 28.475 37.552 31.837 1.00 18.15 ? 310 PRO A C   1 
ATOM   2010 O O   . PRO A 1 280 ? 28.217 38.224 30.835 1.00 15.87 ? 310 PRO A O   1 
ATOM   2011 C CB  . PRO A 1 280 ? 29.116 35.225 31.101 1.00 19.32 ? 310 PRO A CB  1 
ATOM   2012 C CG  . PRO A 1 280 ? 28.275 34.164 30.471 1.00 17.37 ? 310 PRO A CG  1 
ATOM   2013 C CD  . PRO A 1 280 ? 26.961 34.808 30.193 1.00 21.57 ? 310 PRO A CD  1 
ATOM   2014 N N   . ILE A 1 281 ? 29.058 38.058 32.919 1.00 15.66 ? 311 ILE A N   1 
ATOM   2015 C CA  . ILE A 1 281 ? 29.500 39.440 32.994 1.00 17.76 ? 311 ILE A CA  1 
ATOM   2016 C C   . ILE A 1 281 ? 30.979 39.452 33.344 1.00 18.20 ? 311 ILE A C   1 
ATOM   2017 O O   . ILE A 1 281 ? 31.550 38.449 33.780 1.00 19.38 ? 311 ILE A O   1 
ATOM   2018 C CB  . ILE A 1 281 ? 28.692 40.257 34.024 1.00 16.26 ? 311 ILE A CB  1 
ATOM   2019 C CG1 . ILE A 1 281 ? 28.914 39.694 35.430 1.00 16.78 ? 311 ILE A CG1 1 
ATOM   2020 C CG2 . ILE A 1 281 ? 27.214 40.268 33.658 1.00 16.38 ? 311 ILE A CG2 1 
ATOM   2021 C CD1 . ILE A 1 281 ? 28.335 40.553 36.525 1.00 17.54 ? 311 ILE A CD1 1 
ATOM   2022 N N   . VAL A 1 282 ? 31.605 40.607 33.137 1.00 19.91 ? 312 VAL A N   1 
ATOM   2023 C CA  . VAL A 1 282 ? 32.975 40.802 33.588 1.00 18.35 ? 312 VAL A CA  1 
ATOM   2024 C C   . VAL A 1 282 ? 32.914 41.093 35.081 1.00 20.36 ? 312 VAL A C   1 
ATOM   2025 O O   . VAL A 1 282 ? 32.793 42.249 35.499 1.00 19.27 ? 312 VAL A O   1 
ATOM   2026 C CB  . VAL A 1 282 ? 33.680 41.927 32.810 1.00 20.79 ? 312 VAL A CB  1 
ATOM   2027 C CG1 . VAL A 1 282 ? 35.113 42.088 33.291 1.00 18.15 ? 312 VAL A CG1 1 
ATOM   2028 C CG2 . VAL A 1 282 ? 33.645 41.633 31.318 1.00 23.87 ? 312 VAL A CG2 1 
ATOM   2029 N N   . ASP A 1 283 ? 32.966 40.042 35.896 1.00 20.83 ? 313 ASP A N   1 
ATOM   2030 C CA  . ASP A 1 283 ? 32.846 40.210 37.336 1.00 23.99 ? 313 ASP A CA  1 
ATOM   2031 C C   . ASP A 1 283 ? 34.177 40.531 37.993 1.00 23.16 ? 313 ASP A C   1 
ATOM   2032 O O   . ASP A 1 283 ? 34.189 41.003 39.134 1.00 25.55 ? 313 ASP A O   1 
ATOM   2033 C CB  . ASP A 1 283 ? 32.241 38.954 37.970 1.00 22.20 ? 313 ASP A CB  1 
ATOM   2034 C CG  . ASP A 1 283 ? 33.106 37.724 37.776 1.00 24.55 ? 313 ASP A CG  1 
ATOM   2035 O OD1 . ASP A 1 283 ? 33.691 37.564 36.686 1.00 26.15 ? 313 ASP A OD1 1 
ATOM   2036 O OD2 . ASP A 1 283 ? 33.195 36.914 38.718 1.00 28.03 ? 313 ASP A OD2 1 
ATOM   2037 N N   . GLY A 1 284 ? 35.292 40.299 37.301 1.00 23.37 ? 314 GLY A N   1 
ATOM   2038 C CA  . GLY A 1 284 ? 36.606 40.490 37.874 1.00 19.64 ? 314 GLY A CA  1 
ATOM   2039 C C   . GLY A 1 284 ? 37.146 39.296 38.631 1.00 25.64 ? 314 GLY A C   1 
ATOM   2040 O O   . GLY A 1 284 ? 38.339 39.274 38.957 1.00 32.10 ? 314 GLY A O   1 
ATOM   2041 N N   . HIS A 1 285 ? 36.308 38.303 38.921 1.00 24.04 ? 315 HIS A N   1 
ATOM   2042 C CA  . HIS A 1 285 ? 36.720 37.101 39.630 1.00 20.89 ? 315 HIS A CA  1 
ATOM   2043 C C   . HIS A 1 285 ? 36.725 35.889 38.707 1.00 22.75 ? 315 HIS A C   1 
ATOM   2044 O O   . HIS A 1 285 ? 37.785 35.317 38.438 1.00 23.61 ? 315 HIS A O   1 
ATOM   2045 C CB  . HIS A 1 285 ? 35.794 36.879 40.838 1.00 23.66 ? 315 HIS A CB  1 
ATOM   2046 C CG  . HIS A 1 285 ? 35.989 35.564 41.528 1.00 27.23 ? 315 HIS A CG  1 
ATOM   2047 N ND1 . HIS A 1 285 ? 37.217 35.136 41.988 1.00 29.73 ? 315 HIS A ND1 1 
ATOM   2048 C CD2 . HIS A 1 285 ? 35.106 34.588 41.848 1.00 25.63 ? 315 HIS A CD2 1 
ATOM   2049 C CE1 . HIS A 1 285 ? 37.083 33.950 42.555 1.00 27.43 ? 315 HIS A CE1 1 
ATOM   2050 N NE2 . HIS A 1 285 ? 35.812 33.595 42.483 1.00 33.62 ? 315 HIS A NE2 1 
ATOM   2051 N N   . VAL A 1 286 ? 35.560 35.491 38.196 1.00 19.80 ? 316 VAL A N   1 
ATOM   2052 C CA  . VAL A 1 286 ? 35.510 34.426 37.199 1.00 20.10 ? 316 VAL A CA  1 
ATOM   2053 C C   . VAL A 1 286 ? 36.085 34.912 35.872 1.00 19.72 ? 316 VAL A C   1 
ATOM   2054 O O   . VAL A 1 286 ? 36.890 34.224 35.231 1.00 15.49 ? 316 VAL A O   1 
ATOM   2055 C CB  . VAL A 1 286 ? 34.068 33.916 37.033 1.00 19.31 ? 316 VAL A CB  1 
ATOM   2056 C CG1 . VAL A 1 286 ? 34.014 32.837 35.962 1.00 17.33 ? 316 VAL A CG1 1 
ATOM   2057 C CG2 . VAL A 1 286 ? 33.539 33.398 38.361 1.00 19.79 ? 316 VAL A CG2 1 
ATOM   2058 N N   . LEU A 1 287 ? 35.688 36.107 35.445 1.00 16.72 ? 317 LEU A N   1 
ATOM   2059 C CA  . LEU A 1 287 ? 36.185 36.711 34.210 1.00 17.79 ? 317 LEU A CA  1 
ATOM   2060 C C   . LEU A 1 287 ? 36.778 38.073 34.542 1.00 16.76 ? 317 LEU A C   1 
ATOM   2061 O O   . LEU A 1 287 ? 36.036 39.064 34.662 1.00 17.10 ? 317 LEU A O   1 
ATOM   2062 C CB  . LEU A 1 287 ? 35.068 36.842 33.176 1.00 17.93 ? 317 LEU A CB  1 
ATOM   2063 C CG  . LEU A 1 287 ? 34.310 35.546 32.867 1.00 18.11 ? 317 LEU A CG  1 
ATOM   2064 C CD1 . LEU A 1 287 ? 33.077 35.806 31.998 1.00 15.17 ? 317 LEU A CD1 1 
ATOM   2065 C CD2 . LEU A 1 287 ? 35.240 34.540 32.200 1.00 15.08 ? 317 LEU A CD2 1 
ATOM   2066 N N   . PRO A 1 288 ? 38.100 38.174 34.712 1.00 21.69 ? 318 PRO A N   1 
ATOM   2067 C CA  . PRO A 1 288 ? 38.710 39.478 35.025 1.00 18.20 ? 318 PRO A CA  1 
ATOM   2068 C C   . PRO A 1 288 ? 38.620 40.487 33.894 1.00 16.91 ? 318 PRO A C   1 
ATOM   2069 O O   . PRO A 1 288 ? 38.864 41.677 34.132 1.00 19.18 ? 318 PRO A O   1 
ATOM   2070 C CB  . PRO A 1 288 ? 40.172 39.122 35.332 1.00 22.08 ? 318 PRO A CB  1 
ATOM   2071 C CG  . PRO A 1 288 ? 40.396 37.791 34.700 1.00 21.64 ? 318 PRO A CG  1 
ATOM   2072 C CD  . PRO A 1 288 ? 39.079 37.073 34.721 1.00 22.00 ? 318 PRO A CD  1 
ATOM   2073 N N   . GLN A 1 289 ? 38.278 40.059 32.684 1.00 17.63 ? 319 GLN A N   1 
ATOM   2074 C CA  . GLN A 1 289 ? 38.141 40.967 31.555 1.00 19.60 ? 319 GLN A CA  1 
ATOM   2075 C C   . GLN A 1 289 ? 37.286 40.283 30.502 1.00 17.59 ? 319 GLN A C   1 
ATOM   2076 O O   . GLN A 1 289 ? 36.954 39.101 30.621 1.00 16.24 ? 319 GLN A O   1 
ATOM   2077 C CB  . GLN A 1 289 ? 39.508 41.356 30.988 1.00 19.03 ? 319 GLN A CB  1 
ATOM   2078 C CG  . GLN A 1 289 ? 40.330 40.157 30.549 1.00 20.30 ? 319 GLN A CG  1 
ATOM   2079 C CD  . GLN A 1 289 ? 41.800 40.479 30.363 1.00 28.86 ? 319 GLN A CD  1 
ATOM   2080 O OE1 . GLN A 1 289 ? 42.172 41.614 30.053 1.00 27.18 ? 319 GLN A OE1 1 
ATOM   2081 N NE2 . GLN A 1 289 ? 42.646 39.475 30.549 1.00 26.45 ? 319 GLN A NE2 1 
ATOM   2082 N N   . THR A 1 290 ? 36.916 41.049 29.474 1.00 16.80 ? 320 THR A N   1 
ATOM   2083 C CA  . THR A 1 290 ? 36.214 40.468 28.338 1.00 20.24 ? 320 THR A CA  1 
ATOM   2084 C C   . THR A 1 290 ? 37.084 39.405 27.674 1.00 19.33 ? 320 THR A C   1 
ATOM   2085 O O   . THR A 1 290 ? 38.314 39.411 27.781 1.00 18.76 ? 320 THR A O   1 
ATOM   2086 C CB  . THR A 1 290 ? 35.844 41.536 27.304 1.00 21.30 ? 320 THR A CB  1 
ATOM   2087 O OG1 . THR A 1 290 ? 37.041 42.106 26.757 1.00 26.15 ? 320 THR A OG1 1 
ATOM   2088 C CG2 . THR A 1 290 ? 34.994 42.637 27.926 1.00 19.91 ? 320 THR A CG2 1 
ATOM   2089 N N   . ASP A 1 291 ? 36.428 38.479 26.975 1.00 19.54 ? 321 ASP A N   1 
ATOM   2090 C CA  . ASP A 1 291 ? 37.185 37.462 26.259 1.00 20.41 ? 321 ASP A CA  1 
ATOM   2091 C C   . ASP A 1 291 ? 37.963 38.047 25.087 1.00 20.12 ? 321 ASP A C   1 
ATOM   2092 O O   . ASP A 1 291 ? 38.977 37.468 24.686 1.00 20.48 ? 321 ASP A O   1 
ATOM   2093 C CB  . ASP A 1 291 ? 36.260 36.338 25.788 1.00 16.96 ? 321 ASP A CB  1 
ATOM   2094 C CG  . ASP A 1 291 ? 35.021 36.851 25.083 1.00 18.84 ? 321 ASP A CG  1 
ATOM   2095 O OD1 . ASP A 1 291 ? 34.420 37.842 25.552 1.00 19.99 ? 321 ASP A OD1 1 
ATOM   2096 O OD2 . ASP A 1 291 ? 34.643 36.253 24.058 1.00 17.84 ? 321 ASP A OD2 1 
ATOM   2097 N N   . SER A 1 292 ? 37.536 39.191 24.550 1.00 19.22 ? 322 SER A N   1 
ATOM   2098 C CA  . SER A 1 292 ? 38.314 39.846 23.503 1.00 24.92 ? 322 SER A CA  1 
ATOM   2099 C C   . SER A 1 292 ? 39.641 40.358 24.051 1.00 19.03 ? 322 SER A C   1 
ATOM   2100 O O   . SER A 1 292 ? 40.700 40.140 23.450 1.00 21.95 ? 322 SER A O   1 
ATOM   2101 C CB  . SER A 1 292 ? 37.508 40.988 22.882 1.00 22.57 ? 322 SER A CB  1 
ATOM   2102 O OG  . SER A 1 292 ? 36.342 40.498 22.249 1.00 20.61 ? 322 SER A OG  1 
ATOM   2103 N N   . ALA A 1 293 ? 39.602 41.034 25.203 1.00 18.89 ? 323 ALA A N   1 
ATOM   2104 C CA  . ALA A 1 293 ? 40.835 41.520 25.817 1.00 21.33 ? 323 ALA A CA  1 
ATOM   2105 C C   . ALA A 1 293 ? 41.735 40.364 26.240 1.00 22.00 ? 323 ALA A C   1 
ATOM   2106 O O   . ALA A 1 293 ? 42.959 40.425 26.069 1.00 22.82 ? 323 ALA A O   1 
ATOM   2107 C CB  . ALA A 1 293 ? 40.511 42.417 27.014 1.00 19.33 ? 323 ALA A CB  1 
ATOM   2108 N N   . ALA A 1 294 ? 41.144 39.300 26.793 1.00 18.80 ? 324 ALA A N   1 
ATOM   2109 C CA  . ALA A 1 294 ? 41.922 38.121 27.161 1.00 22.51 ? 324 ALA A CA  1 
ATOM   2110 C C   . ALA A 1 294 ? 42.587 37.493 25.941 1.00 25.64 ? 324 ALA A C   1 
ATOM   2111 O O   . ALA A 1 294 ? 43.767 37.128 25.993 1.00 26.18 ? 324 ALA A O   1 
ATOM   2112 C CB  . ALA A 1 294 ? 41.026 37.105 27.867 1.00 16.42 ? 324 ALA A CB  1 
ATOM   2113 N N   . ILE A 1 295 ? 41.840 37.361 24.835 1.00 22.82 ? 325 ILE A N   1 
ATOM   2114 C CA  . ILE A 1 295 ? 42.413 36.892 23.570 1.00 29.43 ? 325 ILE A CA  1 
ATOM   2115 C C   . ILE A 1 295 ? 43.608 37.747 23.178 1.00 26.66 ? 325 ILE A C   1 
ATOM   2116 O O   . ILE A 1 295 ? 44.681 37.236 22.836 1.00 36.92 ? 325 ILE A O   1 
ATOM   2117 C CB  . ILE A 1 295 ? 41.349 36.906 22.456 1.00 23.26 ? 325 ILE A CB  1 
ATOM   2118 C CG1 . ILE A 1 295 ? 40.529 35.623 22.440 1.00 28.90 ? 325 ILE A CG1 1 
ATOM   2119 C CG2 . ILE A 1 295 ? 41.994 37.117 21.086 1.00 43.59 ? 325 ILE A CG2 1 
ATOM   2120 C CD1 . ILE A 1 295 ? 39.639 35.537 21.202 1.00 24.54 ? 325 ILE A CD1 1 
ATOM   2121 N N   . ALA A 1 296 ? 43.429 39.070 23.211 1.00 29.22 ? 326 ALA A N   1 
ATOM   2122 C CA  . ALA A 1 296 ? 44.487 39.967 22.761 1.00 27.57 ? 326 ALA A CA  1 
ATOM   2123 C C   . ALA A 1 296 ? 45.729 39.839 23.633 1.00 29.39 ? 326 ALA A C   1 
ATOM   2124 O O   . ALA A 1 296 ? 46.856 39.832 23.125 1.00 36.14 ? 326 ALA A O   1 
ATOM   2125 C CB  . ALA A 1 296 ? 43.981 41.409 22.744 1.00 25.54 ? 326 ALA A CB  1 
ATOM   2126 N N   . ALA A 1 297 ? 45.548 39.721 24.946 1.00 28.12 ? 327 ALA A N   1 
ATOM   2127 C CA  . ALA A 1 297 ? 46.688 39.640 25.852 1.00 27.11 ? 327 ALA A CA  1 
ATOM   2128 C C   . ALA A 1 297 ? 47.224 38.223 26.018 1.00 28.68 ? 327 ALA A C   1 
ATOM   2129 O O   . ALA A 1 297 ? 48.164 38.025 26.796 1.00 30.04 ? 327 ALA A O   1 
ATOM   2130 C CB  . ALA A 1 297 ? 46.318 40.209 27.223 1.00 19.70 ? 327 ALA A CB  1 
ATOM   2131 N N   . GLY A 1 298 ? 46.661 37.243 25.314 1.00 28.20 ? 328 GLY A N   1 
ATOM   2132 C CA  . GLY A 1 298 ? 47.105 35.874 25.465 1.00 26.70 ? 328 GLY A CA  1 
ATOM   2133 C C   . GLY A 1 298 ? 46.658 35.192 26.736 1.00 31.41 ? 328 GLY A C   1 
ATOM   2134 O O   . GLY A 1 298 ? 47.234 34.168 27.112 1.00 30.40 ? 328 GLY A O   1 
ATOM   2135 N N   . GLN A 1 299 ? 45.649 35.733 27.420 1.00 25.95 ? 329 GLN A N   1 
ATOM   2136 C CA  . GLN A 1 299 ? 45.104 35.112 28.627 1.00 28.61 ? 329 GLN A CA  1 
ATOM   2137 C C   . GLN A 1 299 ? 44.154 33.982 28.223 1.00 28.18 ? 329 GLN A C   1 
ATOM   2138 O O   . GLN A 1 299 ? 42.935 34.040 28.407 1.00 19.45 ? 329 GLN A O   1 
ATOM   2139 C CB  . GLN A 1 299 ? 44.409 36.154 29.492 1.00 33.13 ? 329 GLN A CB  1 
ATOM   2140 C CG  . GLN A 1 299 ? 45.365 37.080 30.214 1.00 32.10 ? 329 GLN A CG  1 
ATOM   2141 C CD  . GLN A 1 299 ? 46.061 36.390 31.369 1.00 42.05 ? 329 GLN A CD  1 
ATOM   2142 O OE1 . GLN A 1 299 ? 45.410 35.852 32.268 1.00 43.38 ? 329 GLN A OE1 1 
ATOM   2143 N NE2 . GLN A 1 299 ? 47.389 36.393 31.349 1.00 32.15 ? 329 GLN A NE2 1 
ATOM   2144 N N   . LEU A 1 300 ? 44.749 32.933 27.659 1.00 20.81 ? 330 LEU A N   1 
ATOM   2145 C CA  . LEU A 1 300 ? 44.033 31.756 27.186 1.00 24.71 ? 330 LEU A CA  1 
ATOM   2146 C C   . LEU A 1 300 ? 44.720 30.513 27.723 1.00 21.99 ? 330 LEU A C   1 
ATOM   2147 O O   . LEU A 1 300 ? 45.948 30.408 27.664 1.00 26.87 ? 330 LEU A O   1 
ATOM   2148 C CB  . LEU A 1 300 ? 44.005 31.691 25.656 1.00 26.74 ? 330 LEU A CB  1 
ATOM   2149 C CG  . LEU A 1 300 ? 42.800 32.227 24.894 1.00 24.54 ? 330 LEU A CG  1 
ATOM   2150 C CD1 . LEU A 1 300 ? 43.010 31.966 23.418 1.00 25.84 ? 330 LEU A CD1 1 
ATOM   2151 C CD2 . LEU A 1 300 ? 41.530 31.561 25.380 1.00 27.43 ? 330 LEU A CD2 1 
ATOM   2152 N N   . ALA A 1 301 ? 43.938 29.576 28.226 1.00 21.64 ? 331 ALA A N   1 
ATOM   2153 C CA  . ALA A 1 301 ? 44.494 28.285 28.590 1.00 22.57 ? 331 ALA A CA  1 
ATOM   2154 C C   . ALA A 1 301 ? 44.778 27.508 27.313 1.00 24.76 ? 331 ALA A C   1 
ATOM   2155 O O   . ALA A 1 301 ? 43.838 27.187 26.574 1.00 25.57 ? 331 ALA A O   1 
ATOM   2156 C CB  . ALA A 1 301 ? 43.532 27.519 29.489 1.00 16.79 ? 331 ALA A CB  1 
ATOM   2157 N N   . PRO A 1 302 ? 46.043 27.192 26.999 1.00 25.62 ? 332 PRO A N   1 
ATOM   2158 C CA  . PRO A 1 302 ? 46.374 26.499 25.748 1.00 22.27 ? 332 PRO A CA  1 
ATOM   2159 C C   . PRO A 1 302 ? 46.102 24.996 25.804 1.00 24.69 ? 332 PRO A C   1 
ATOM   2160 O O   . PRO A 1 302 ? 46.945 24.179 25.432 1.00 26.69 ? 332 PRO A O   1 
ATOM   2161 C CB  . PRO A 1 302 ? 47.863 26.809 25.569 1.00 23.96 ? 332 PRO A CB  1 
ATOM   2162 C CG  . PRO A 1 302 ? 48.380 27.157 26.956 1.00 27.17 ? 332 PRO A CG  1 
ATOM   2163 C CD  . PRO A 1 302 ? 47.210 27.318 27.889 1.00 25.54 ? 332 PRO A CD  1 
ATOM   2164 N N   . VAL A 1 303 ? 44.907 24.633 26.272 1.00 23.96 ? 333 VAL A N   1 
ATOM   2165 C CA  . VAL A 1 303 ? 44.472 23.244 26.341 1.00 21.37 ? 333 VAL A CA  1 
ATOM   2166 C C   . VAL A 1 303 ? 44.208 22.747 24.929 1.00 19.95 ? 333 VAL A C   1 
ATOM   2167 O O   . VAL A 1 303 ? 44.152 23.540 23.982 1.00 16.61 ? 333 VAL A O   1 
ATOM   2168 C CB  . VAL A 1 303 ? 43.215 23.093 27.219 1.00 24.73 ? 333 VAL A CB  1 
ATOM   2169 C CG1 . VAL A 1 303 ? 43.477 23.621 28.628 1.00 21.97 ? 333 VAL A CG1 1 
ATOM   2170 C CG2 . VAL A 1 303 ? 42.036 23.819 26.583 1.00 15.62 ? 333 VAL A CG2 1 
ATOM   2171 N N   . ARG A 1 304 ? 44.044 21.436 24.775 1.00 19.00 ? 334 ARG A N   1 
ATOM   2172 C CA  . ARG A 1 304 ? 43.592 20.900 23.500 1.00 18.85 ? 334 ARG A CA  1 
ATOM   2173 C C   . ARG A 1 304 ? 42.177 21.388 23.223 1.00 20.43 ? 334 ARG A C   1 
ATOM   2174 O O   . ARG A 1 304 ? 41.301 21.309 24.089 1.00 18.40 ? 334 ARG A O   1 
ATOM   2175 C CB  . ARG A 1 304 ? 43.644 19.374 23.522 1.00 17.10 ? 334 ARG A CB  1 
ATOM   2176 C CG  . ARG A 1 304 ? 45.039 18.812 23.764 1.00 19.09 ? 334 ARG A CG  1 
ATOM   2177 C CD  . ARG A 1 304 ? 44.953 17.413 24.316 1.00 19.68 ? 334 ARG A CD  1 
ATOM   2178 N NE  . ARG A 1 304 ? 46.224 16.699 24.286 1.00 24.56 ? 334 ARG A NE  1 
ATOM   2179 C CZ  . ARG A 1 304 ? 47.048 16.582 25.318 1.00 24.16 ? 334 ARG A CZ  1 
ATOM   2180 N NH1 . ARG A 1 304 ? 46.810 17.193 26.468 1.00 21.71 ? 334 ARG A NH1 1 
ATOM   2181 N NH2 . ARG A 1 304 ? 48.135 15.827 25.194 1.00 26.31 ? 334 ARG A NH2 1 
ATOM   2182 N N   . VAL A 1 305 ? 41.957 21.917 22.023 1.00 18.00 ? 335 VAL A N   1 
ATOM   2183 C CA  . VAL A 1 305 ? 40.681 22.522 21.670 1.00 16.49 ? 335 VAL A CA  1 
ATOM   2184 C C   . VAL A 1 305 ? 40.213 21.972 20.332 1.00 18.25 ? 335 VAL A C   1 
ATOM   2185 O O   . VAL A 1 305 ? 40.980 21.931 19.364 1.00 18.05 ? 335 VAL A O   1 
ATOM   2186 C CB  . VAL A 1 305 ? 40.766 24.060 21.615 1.00 17.62 ? 335 VAL A CB  1 
ATOM   2187 C CG1 . VAL A 1 305 ? 39.462 24.652 21.072 1.00 15.46 ? 335 VAL A CG1 1 
ATOM   2188 C CG2 . VAL A 1 305 ? 41.079 24.631 22.999 1.00 16.11 ? 335 VAL A CG2 1 
ATOM   2189 N N   . LEU A 1 306 ? 38.955 21.546 20.288 1.00 16.54 ? 336 LEU A N   1 
ATOM   2190 C CA  . LEU A 1 306 ? 38.237 21.282 19.050 1.00 16.77 ? 336 LEU A CA  1 
ATOM   2191 C C   . LEU A 1 306 ? 37.094 22.286 18.980 1.00 16.36 ? 336 LEU A C   1 
ATOM   2192 O O   . LEU A 1 306 ? 36.228 22.300 19.862 1.00 18.01 ? 336 LEU A O   1 
ATOM   2193 C CB  . LEU A 1 306 ? 37.716 19.843 19.003 1.00 15.86 ? 336 LEU A CB  1 
ATOM   2194 C CG  . LEU A 1 306 ? 36.819 19.500 17.815 1.00 16.02 ? 336 LEU A CG  1 
ATOM   2195 C CD1 . LEU A 1 306 ? 37.533 19.798 16.510 1.00 16.26 ? 336 LEU A CD1 1 
ATOM   2196 C CD2 . LEU A 1 306 ? 36.388 18.045 17.890 1.00 16.90 ? 336 LEU A CD2 1 
ATOM   2197 N N   . ILE A 1 307 ? 37.095 23.125 17.947 1.00 15.70 ? 337 ILE A N   1 
ATOM   2198 C CA  . ILE A 1 307 ? 36.119 24.201 17.833 1.00 17.38 ? 337 ILE A CA  1 
ATOM   2199 C C   . ILE A 1 307 ? 35.575 24.228 16.411 1.00 18.25 ? 337 ILE A C   1 
ATOM   2200 O O   . ILE A 1 307 ? 36.259 23.844 15.456 1.00 18.27 ? 337 ILE A O   1 
ATOM   2201 C CB  . ILE A 1 307 ? 36.739 25.564 18.222 1.00 16.15 ? 337 ILE A CB  1 
ATOM   2202 C CG1 . ILE A 1 307 ? 35.680 26.669 18.241 1.00 15.54 ? 337 ILE A CG1 1 
ATOM   2203 C CG2 . ILE A 1 307 ? 37.901 25.924 17.292 1.00 17.83 ? 337 ILE A CG2 1 
ATOM   2204 C CD1 . ILE A 1 307 ? 36.198 28.003 18.738 1.00 15.52 ? 337 ILE A CD1 1 
ATOM   2205 N N   . GLY A 1 308 ? 34.328 24.661 16.268 1.00 16.99 ? 338 GLY A N   1 
ATOM   2206 C CA  . GLY A 1 308 ? 33.783 24.777 14.930 1.00 18.69 ? 338 GLY A CA  1 
ATOM   2207 C C   . GLY A 1 308 ? 32.383 25.338 14.942 1.00 17.63 ? 338 GLY A C   1 
ATOM   2208 O O   . GLY A 1 308 ? 31.811 25.652 15.992 1.00 16.05 ? 338 GLY A O   1 
ATOM   2209 N N   . THR A 1 309 ? 31.838 25.453 13.736 1.00 16.60 ? 339 THR A N   1 
ATOM   2210 C CA  . THR A 1 309 ? 30.530 26.057 13.524 1.00 16.80 ? 339 THR A CA  1 
ATOM   2211 C C   . THR A 1 309 ? 29.718 25.201 12.565 1.00 20.14 ? 339 THR A C   1 
ATOM   2212 O O   . THR A 1 309 ? 30.222 24.247 11.973 1.00 19.73 ? 339 THR A O   1 
ATOM   2213 C CB  . THR A 1 309 ? 30.645 27.491 12.974 1.00 20.42 ? 339 THR A CB  1 
ATOM   2214 O OG1 . THR A 1 309 ? 31.491 27.500 11.815 1.00 22.99 ? 339 THR A OG1 1 
ATOM   2215 C CG2 . THR A 1 309 ? 31.212 28.432 14.021 1.00 16.70 ? 339 THR A CG2 1 
ATOM   2216 N N   . ASN A 1 310 ? 28.446 25.546 12.416 1.00 18.12 ? 340 ASN A N   1 
ATOM   2217 C CA  . ASN A 1 310 ? 27.617 24.968 11.373 1.00 17.87 ? 340 ASN A CA  1 
ATOM   2218 C C   . ASN A 1 310 ? 27.499 25.949 10.213 1.00 18.29 ? 340 ASN A C   1 
ATOM   2219 O O   . ASN A 1 310 ? 27.818 27.133 10.335 1.00 22.06 ? 340 ASN A O   1 
ATOM   2220 C CB  . ASN A 1 310 ? 26.232 24.597 11.907 1.00 18.67 ? 340 ASN A CB  1 
ATOM   2221 C CG  . ASN A 1 310 ? 26.292 23.572 13.040 1.00 21.90 ? 340 ASN A CG  1 
ATOM   2222 O OD1 . ASN A 1 310 ? 27.338 22.986 13.312 1.00 17.34 ? 340 ASN A OD1 1 
ATOM   2223 N ND2 . ASN A 1 310 ? 25.158 23.351 13.697 1.00 18.51 ? 340 ASN A ND2 1 
ATOM   2224 N N   . ALA A 1 311 ? 27.044 25.433 9.072  1.00 17.17 ? 341 ALA A N   1 
ATOM   2225 C CA  . ALA A 1 311 ? 27.083 26.215 7.840  1.00 22.37 ? 341 ALA A CA  1 
ATOM   2226 C C   . ALA A 1 311 ? 26.260 27.495 7.951  1.00 27.19 ? 341 ALA A C   1 
ATOM   2227 O O   . ALA A 1 311 ? 26.713 28.569 7.536  1.00 24.10 ? 341 ALA A O   1 
ATOM   2228 C CB  . ALA A 1 311 ? 26.594 25.364 6.669  1.00 19.70 ? 341 ALA A CB  1 
ATOM   2229 N N   . ASP A 1 312 ? 25.053 27.407 8.519  1.00 21.05 ? 342 ASP A N   1 
ATOM   2230 C CA  . ASP A 1 312 ? 24.093 28.511 8.509  1.00 21.38 ? 342 ASP A CA  1 
ATOM   2231 C C   . ASP A 1 312 ? 23.603 28.763 9.939  1.00 24.46 ? 342 ASP A C   1 
ATOM   2232 O O   . ASP A 1 312 ? 22.436 28.527 10.258 1.00 24.08 ? 342 ASP A O   1 
ATOM   2233 C CB  . ASP A 1 312 ? 22.929 28.206 7.562  1.00 21.28 ? 342 ASP A CB  1 
ATOM   2234 C CG  . ASP A 1 312 ? 22.080 29.425 7.267  1.00 23.98 ? 342 ASP A CG  1 
ATOM   2235 O OD1 . ASP A 1 312 ? 22.441 30.529 7.730  1.00 25.40 ? 342 ASP A OD1 1 
ATOM   2236 O OD2 . ASP A 1 312 ? 21.053 29.281 6.568  1.00 27.76 ? 342 ASP A OD2 1 
ATOM   2237 N N   . GLU A 1 313 ? 24.501 29.274 10.789 1.00 19.64 ? 343 GLU A N   1 
ATOM   2238 C CA  . GLU A 1 313 ? 24.175 29.463 12.202 1.00 20.91 ? 343 GLU A CA  1 
ATOM   2239 C C   . GLU A 1 313 ? 22.971 30.378 12.393 1.00 18.39 ? 343 GLU A C   1 
ATOM   2240 O O   . GLU A 1 313 ? 22.153 30.158 13.294 1.00 17.99 ? 343 GLU A O   1 
ATOM   2241 C CB  . GLU A 1 313 ? 25.382 30.031 12.953 1.00 17.03 ? 343 GLU A CB  1 
ATOM   2242 C CG  . GLU A 1 313 ? 26.568 29.083 13.065 1.00 20.39 ? 343 GLU A CG  1 
ATOM   2243 C CD  . GLU A 1 313 ? 26.400 28.048 14.171 1.00 24.13 ? 343 GLU A CD  1 
ATOM   2244 O OE1 . GLU A 1 313 ? 25.361 28.070 14.873 1.00 19.26 ? 343 GLU A OE1 1 
ATOM   2245 O OE2 . GLU A 1 313 ? 27.315 27.214 14.338 1.00 24.52 ? 343 GLU A OE2 1 
ATOM   2246 N N   . GLY A 1 314 ? 22.844 31.411 11.559 1.00 20.61 ? 344 GLY A N   1 
ATOM   2247 C CA  . GLY A 1 314 ? 21.853 32.441 11.814 1.00 19.74 ? 344 GLY A CA  1 
ATOM   2248 C C   . GLY A 1 314 ? 20.424 32.067 11.481 1.00 22.81 ? 344 GLY A C   1 
ATOM   2249 O O   . GLY A 1 314 ? 19.502 32.699 12.005 1.00 19.99 ? 344 GLY A O   1 
ATOM   2250 N N   . ARG A 1 315 ? 20.215 31.058 10.629 1.00 19.58 ? 345 ARG A N   1 
ATOM   2251 C CA  . ARG A 1 315 ? 18.865 30.765 10.147 1.00 24.50 ? 345 ARG A CA  1 
ATOM   2252 C C   . ARG A 1 315 ? 17.908 30.470 11.298 1.00 25.62 ? 345 ARG A C   1 
ATOM   2253 O O   . ARG A 1 315 ? 16.738 30.874 11.266 1.00 21.88 ? 345 ARG A O   1 
ATOM   2254 C CB  . ARG A 1 315 ? 18.897 29.598 9.157  1.00 20.65 ? 345 ARG A CB  1 
ATOM   2255 C CG  . ARG A 1 315 ? 17.509 29.119 8.727  1.00 24.92 ? 345 ARG A CG  1 
ATOM   2256 C CD  . ARG A 1 315 ? 17.538 28.316 7.435  1.00 19.70 ? 345 ARG A CD  1 
ATOM   2257 N NE  . ARG A 1 315 ? 18.425 27.161 7.501  1.00 28.61 ? 345 ARG A NE  1 
ATOM   2258 C CZ  . ARG A 1 315 ? 18.076 25.974 7.977  1.00 25.82 ? 345 ARG A CZ  1 
ATOM   2259 N NH1 . ARG A 1 315 ? 16.868 25.753 8.468  1.00 36.69 ? 345 ARG A NH1 1 
ATOM   2260 N NH2 . ARG A 1 315 ? 18.962 24.981 7.958  1.00 21.55 ? 345 ARG A NH2 1 
ATOM   2261 N N   . ALA A 1 316 ? 18.394 29.795 12.340 1.00 21.03 ? 346 ALA A N   1 
ATOM   2262 C CA  . ALA A 1 316 ? 17.545 29.434 13.468 1.00 21.94 ? 346 ALA A CA  1 
ATOM   2263 C C   . ALA A 1 316 ? 17.120 30.630 14.313 1.00 21.41 ? 346 ALA A C   1 
ATOM   2264 O O   . ALA A 1 316 ? 16.247 30.473 15.172 1.00 26.83 ? 346 ALA A O   1 
ATOM   2265 C CB  . ALA A 1 316 ? 18.258 28.410 14.351 1.00 18.88 ? 346 ALA A CB  1 
ATOM   2266 N N   . PHE A 1 317 ? 17.699 31.811 14.099 1.00 25.31 ? 347 PHE A N   1 
ATOM   2267 C CA  . PHE A 1 317 ? 17.393 32.986 14.908 1.00 25.03 ? 347 PHE A CA  1 
ATOM   2268 C C   . PHE A 1 317 ? 16.513 34.002 14.186 1.00 26.72 ? 347 PHE A C   1 
ATOM   2269 O O   . PHE A 1 317 ? 16.291 35.096 14.715 1.00 28.76 ? 347 PHE A O   1 
ATOM   2270 C CB  . PHE A 1 317 ? 18.688 33.665 15.363 1.00 20.89 ? 347 PHE A CB  1 
ATOM   2271 C CG  . PHE A 1 317 ? 19.564 32.799 16.227 1.00 21.00 ? 347 PHE A CG  1 
ATOM   2272 C CD1 . PHE A 1 317 ? 20.454 31.902 15.658 1.00 17.26 ? 347 PHE A CD1 1 
ATOM   2273 C CD2 . PHE A 1 317 ? 19.508 32.895 17.611 1.00 19.56 ? 347 PHE A CD2 1 
ATOM   2274 C CE1 . PHE A 1 317 ? 21.262 31.107 16.447 1.00 18.70 ? 347 PHE A CE1 1 
ATOM   2275 C CE2 . PHE A 1 317 ? 20.324 32.103 18.411 1.00 25.72 ? 347 PHE A CE2 1 
ATOM   2276 C CZ  . PHE A 1 317 ? 21.201 31.210 17.827 1.00 18.00 ? 347 PHE A CZ  1 
ATOM   2277 N N   . LEU A 1 318 ? 15.997 33.665 13.001 1.00 21.46 ? 348 LEU A N   1 
ATOM   2278 C CA  . LEU A 1 318 ? 15.379 34.673 12.142 1.00 29.78 ? 348 LEU A CA  1 
ATOM   2279 C C   . LEU A 1 318 ? 14.174 35.328 12.806 1.00 37.20 ? 348 LEU A C   1 
ATOM   2280 O O   . LEU A 1 318 ? 14.028 36.556 12.780 1.00 40.42 ? 348 LEU A O   1 
ATOM   2281 C CB  . LEU A 1 318 ? 14.971 34.047 10.812 1.00 35.08 ? 348 LEU A CB  1 
ATOM   2282 C CG  . LEU A 1 318 ? 16.068 33.877 9.768  1.00 36.80 ? 348 LEU A CG  1 
ATOM   2283 C CD1 . LEU A 1 318 ? 15.475 33.164 8.581  1.00 36.01 ? 348 LEU A CD1 1 
ATOM   2284 C CD2 . LEU A 1 318 ? 16.645 35.224 9.362  1.00 28.27 ? 348 LEU A CD2 1 
ATOM   2285 N N   . GLY A 1 319 ? 13.294 34.530 13.387 1.00 24.50 ? 349 GLY A N   1 
ATOM   2286 C CA  . GLY A 1 319 ? 12.089 35.076 13.973 1.00 41.24 ? 349 GLY A CA  1 
ATOM   2287 C C   . GLY A 1 319 ? 10.960 35.180 12.966 1.00 45.15 ? 349 GLY A C   1 
ATOM   2288 O O   . GLY A 1 319 ? 10.959 34.543 11.908 1.00 46.00 ? 349 GLY A O   1 
ATOM   2289 N N   . ARG A 1 320 ? 9.979  36.017 13.307 1.00 54.43 ? 350 ARG A N   1 
ATOM   2290 C CA  . ARG A 1 320 ? 8.740  36.090 12.549 1.00 48.94 ? 350 ARG A CA  1 
ATOM   2291 C C   . ARG A 1 320 ? 8.474  37.442 11.907 1.00 44.44 ? 350 ARG A C   1 
ATOM   2292 O O   . ARG A 1 320 ? 7.505  37.559 11.147 1.00 50.17 ? 350 ARG A O   1 
ATOM   2293 C CB  . ARG A 1 320 ? 7.547  35.721 13.446 1.00 52.62 ? 350 ARG A CB  1 
ATOM   2294 C CG  . ARG A 1 320 ? 7.654  34.340 14.077 1.00 52.75 ? 350 ARG A CG  1 
ATOM   2295 C CD  . ARG A 1 320 ? 6.413  34.009 14.891 1.00 66.01 ? 350 ARG A CD  1 
ATOM   2296 N NE  . ARG A 1 320 ? 5.218  33.951 14.058 1.00 71.20 ? 350 ARG A NE  1 
ATOM   2297 C CZ  . ARG A 1 320 ? 4.732  32.840 13.521 1.00 73.85 ? 350 ARG A CZ  1 
ATOM   2298 N NH1 . ARG A 1 320 ? 5.309  31.666 13.722 1.00 76.23 ? 350 ARG A NH1 1 
ATOM   2299 N NH2 . ARG A 1 320 ? 3.641  32.907 12.764 1.00 68.63 ? 350 ARG A NH2 1 
ATOM   2300 N N   . ALA A 1 321 ? 9.283  38.458 12.188 1.00 45.56 ? 351 ALA A N   1 
ATOM   2301 C CA  . ALA A 1 321 ? 9.131  39.729 11.499 1.00 45.72 ? 351 ALA A CA  1 
ATOM   2302 C C   . ALA A 1 321 ? 9.304  39.522 9.995  1.00 46.26 ? 351 ALA A C   1 
ATOM   2303 O O   . ALA A 1 321 ? 10.146 38.720 9.571  1.00 39.29 ? 351 ALA A O   1 
ATOM   2304 C CB  . ALA A 1 321 ? 10.149 40.748 12.015 1.00 36.81 ? 351 ALA A CB  1 
ATOM   2305 N N   . PRO A 1 322 ? 8.525  40.213 9.166  1.00 44.90 ? 352 PRO A N   1 
ATOM   2306 C CA  . PRO A 1 322 ? 8.588  39.969 7.719  1.00 36.71 ? 352 PRO A CA  1 
ATOM   2307 C C   . PRO A 1 322 ? 9.966  40.288 7.160  1.00 34.30 ? 352 PRO A C   1 
ATOM   2308 O O   . PRO A 1 322 ? 10.518 41.365 7.394  1.00 38.55 ? 352 PRO A O   1 
ATOM   2309 C CB  . PRO A 1 322 ? 7.517  40.909 7.154  1.00 40.21 ? 352 PRO A CB  1 
ATOM   2310 C CG  . PRO A 1 322 ? 6.619  41.223 8.318  1.00 49.61 ? 352 PRO A CG  1 
ATOM   2311 C CD  . PRO A 1 322 ? 7.516  41.225 9.516  1.00 48.83 ? 352 PRO A CD  1 
ATOM   2312 N N   . MET A 1 323 ? 10.529 39.322 6.416  1.00 38.06 ? 353 MET A N   1 
ATOM   2313 C CA  . MET A 1 323 ? 11.819 39.472 5.749  1.00 28.96 ? 353 MET A CA  1 
ATOM   2314 C C   . MET A 1 323 ? 11.712 38.806 4.374  1.00 28.86 ? 353 MET A C   1 
ATOM   2315 O O   . MET A 1 323 ? 12.247 37.727 4.122  1.00 31.00 ? 353 MET A O   1 
ATOM   2316 C CB  . MET A 1 323 ? 12.958 38.876 6.579  1.00 25.19 ? 353 MET A CB  1 
ATOM   2317 C CG  . MET A 1 323 ? 14.354 39.179 6.043  1.00 23.23 ? 353 MET A CG  1 
ATOM   2318 S SD  . MET A 1 323 ? 14.682 40.949 5.904  1.00 25.00 ? 353 MET A SD  1 
ATOM   2319 C CE  . MET A 1 323 ? 14.420 41.492 7.587  1.00 19.70 ? 353 MET A CE  1 
ATOM   2320 N N   . GLU A 1 324 ? 10.991 39.461 3.466  1.00 31.35 ? 354 GLU A N   1 
ATOM   2321 C CA  . GLU A 1 324 ? 10.790 38.953 2.116  1.00 33.47 ? 354 GLU A CA  1 
ATOM   2322 C C   . GLU A 1 324 ? 11.244 39.906 1.024  1.00 28.77 ? 354 GLU A C   1 
ATOM   2323 O O   . GLU A 1 324 ? 11.598 39.446 -0.064 1.00 30.74 ? 354 GLU A O   1 
ATOM   2324 C CB  . GLU A 1 324 ? 9.307  38.619 1.883  1.00 33.11 ? 354 GLU A CB  1 
ATOM   2325 C CG  . GLU A 1 324 ? 8.710  37.655 2.892  1.00 38.12 ? 354 GLU A CG  1 
ATOM   2326 C CD  . GLU A 1 324 ? 9.256  36.246 2.756  1.00 46.26 ? 354 GLU A CD  1 
ATOM   2327 O OE1 . GLU A 1 324 ? 9.637  35.861 1.630  1.00 42.94 ? 354 GLU A OE1 1 
ATOM   2328 O OE2 . GLU A 1 324 ? 9.302  35.524 3.774  1.00 47.55 ? 354 GLU A OE2 1 
ATOM   2329 N N   . THR A 1 325 ? 11.247 41.210 1.275  1.00 26.00 ? 355 THR A N   1 
ATOM   2330 C CA  . THR A 1 325 ? 11.497 42.216 0.258  1.00 28.66 ? 355 THR A CA  1 
ATOM   2331 C C   . THR A 1 325 ? 12.785 42.976 0.546  1.00 27.51 ? 355 THR A C   1 
ATOM   2332 O O   . THR A 1 325 ? 13.287 42.963 1.677  1.00 26.72 ? 355 THR A O   1 
ATOM   2333 C CB  . THR A 1 325 ? 10.327 43.210 0.181  1.00 32.88 ? 355 THR A CB  1 
ATOM   2334 O OG1 . THR A 1 325 ? 10.348 44.062 1.332  1.00 25.57 ? 355 THR A OG1 1 
ATOM   2335 C CG2 . THR A 1 325 ? 8.997  42.468 0.133  1.00 34.80 ? 355 THR A CG2 1 
ATOM   2336 N N   . PRO A 1 326 ? 13.358 43.642 -0.462 1.00 26.84 ? 356 PRO A N   1 
ATOM   2337 C CA  . PRO A 1 326 ? 14.486 44.542 -0.181 1.00 31.21 ? 356 PRO A CA  1 
ATOM   2338 C C   . PRO A 1 326 ? 14.128 45.654 0.785  1.00 30.13 ? 356 PRO A C   1 
ATOM   2339 O O   . PRO A 1 326 ? 15.002 46.129 1.522  1.00 27.63 ? 356 PRO A O   1 
ATOM   2340 C CB  . PRO A 1 326 ? 14.848 45.089 -1.568 1.00 30.12 ? 356 PRO A CB  1 
ATOM   2341 C CG  . PRO A 1 326 ? 14.382 44.038 -2.513 1.00 28.87 ? 356 PRO A CG  1 
ATOM   2342 C CD  . PRO A 1 326 ? 13.117 43.500 -1.909 1.00 29.38 ? 356 PRO A CD  1 
ATOM   2343 N N   . ALA A 1 327 ? 12.863 46.081 0.809  1.00 30.54 ? 357 ALA A N   1 
ATOM   2344 C CA  . ALA A 1 327 ? 12.442 47.082 1.781  1.00 27.58 ? 357 ALA A CA  1 
ATOM   2345 C C   . ALA A 1 327 ? 12.552 46.544 3.202  1.00 24.12 ? 357 ALA A C   1 
ATOM   2346 O O   . ALA A 1 327 ? 13.027 47.246 4.102  1.00 24.64 ? 357 ALA A O   1 
ATOM   2347 C CB  . ALA A 1 327 ? 11.014 47.535 1.481  1.00 28.04 ? 357 ALA A CB  1 
ATOM   2348 N N   . ASP A 1 328 ? 12.122 45.297 3.420  1.00 23.01 ? 358 ASP A N   1 
ATOM   2349 C CA  . ASP A 1 328 ? 12.269 44.669 4.731  1.00 23.40 ? 358 ASP A CA  1 
ATOM   2350 C C   . ASP A 1 328 ? 13.735 44.614 5.152  1.00 23.37 ? 358 ASP A C   1 
ATOM   2351 O O   . ASP A 1 328 ? 14.080 44.926 6.301  1.00 25.23 ? 358 ASP A O   1 
ATOM   2352 C CB  . ASP A 1 328 ? 11.671 43.259 4.708  1.00 30.89 ? 358 ASP A CB  1 
ATOM   2353 C CG  . ASP A 1 328 ? 10.196 43.248 4.347  1.00 30.57 ? 358 ASP A CG  1 
ATOM   2354 O OD1 . ASP A 1 328 ? 9.481  44.209 4.703  1.00 27.51 ? 358 ASP A OD1 1 
ATOM   2355 O OD2 . ASP A 1 328 ? 9.750  42.270 3.709  1.00 31.85 ? 358 ASP A OD2 1 
ATOM   2356 N N   . TYR A 1 329 ? 14.612 44.210 4.228  1.00 24.01 ? 359 TYR A N   1 
ATOM   2357 C CA  . TYR A 1 329 ? 16.033 44.089 4.537  1.00 22.62 ? 359 TYR A CA  1 
ATOM   2358 C C   . TYR A 1 329 ? 16.638 45.443 4.873  1.00 24.15 ? 359 TYR A C   1 
ATOM   2359 O O   . TYR A 1 329 ? 17.396 45.571 5.841  1.00 25.57 ? 359 TYR A O   1 
ATOM   2360 C CB  . TYR A 1 329 ? 16.764 43.448 3.355  1.00 21.43 ? 359 TYR A CB  1 
ATOM   2361 C CG  . TYR A 1 329 ? 18.227 43.159 3.596  1.00 25.13 ? 359 TYR A CG  1 
ATOM   2362 C CD1 . TYR A 1 329 ? 18.623 42.293 4.606  1.00 19.05 ? 359 TYR A CD1 1 
ATOM   2363 C CD2 . TYR A 1 329 ? 19.212 43.732 2.798  1.00 26.22 ? 359 TYR A CD2 1 
ATOM   2364 C CE1 . TYR A 1 329 ? 19.960 42.013 4.825  1.00 24.31 ? 359 TYR A CE1 1 
ATOM   2365 C CE2 . TYR A 1 329 ? 20.556 43.460 3.011  1.00 22.13 ? 359 TYR A CE2 1 
ATOM   2366 C CZ  . TYR A 1 329 ? 20.920 42.599 4.029  1.00 23.05 ? 359 TYR A CZ  1 
ATOM   2367 O OH  . TYR A 1 329 ? 22.244 42.315 4.260  1.00 19.03 ? 359 TYR A OH  1 
ATOM   2368 N N   . GLN A 1 330 ? 16.321 46.463 4.074  1.00 21.90 ? 360 GLN A N   1 
ATOM   2369 C CA  . GLN A 1 330 ? 16.790 47.814 4.360  1.00 25.60 ? 360 GLN A CA  1 
ATOM   2370 C C   . GLN A 1 330 ? 16.301 48.293 5.724  1.00 27.03 ? 360 GLN A C   1 
ATOM   2371 O O   . GLN A 1 330 ? 17.064 48.902 6.486  1.00 25.89 ? 360 GLN A O   1 
ATOM   2372 C CB  . GLN A 1 330 ? 16.327 48.762 3.252  1.00 26.99 ? 360 GLN A CB  1 
ATOM   2373 C CG  . GLN A 1 330 ? 16.306 50.233 3.633  1.00 33.88 ? 360 GLN A CG  1 
ATOM   2374 C CD  . GLN A 1 330 ? 17.642 50.919 3.436  1.00 42.49 ? 360 GLN A CD  1 
ATOM   2375 O OE1 . GLN A 1 330 ? 18.662 50.270 3.184  1.00 38.59 ? 360 GLN A OE1 1 
ATOM   2376 N NE2 . GLN A 1 330 ? 17.643 52.245 3.545  1.00 48.49 ? 360 GLN A NE2 1 
ATOM   2377 N N   . ALA A 1 331 ? 15.034 48.021 6.052  1.00 21.00 ? 361 ALA A N   1 
ATOM   2378 C CA  . ALA A 1 331 ? 14.499 48.437 7.345  1.00 26.30 ? 361 ALA A CA  1 
ATOM   2379 C C   . ALA A 1 331 ? 15.230 47.749 8.490  1.00 22.73 ? 361 ALA A C   1 
ATOM   2380 O O   . ALA A 1 331 ? 15.531 48.380 9.510  1.00 24.54 ? 361 ALA A O   1 
ATOM   2381 C CB  . ALA A 1 331 ? 12.997 48.148 7.413  1.00 21.32 ? 361 ALA A CB  1 
ATOM   2382 N N   . TYR A 1 332 ? 15.535 46.458 8.333  1.00 26.21 ? 362 TYR A N   1 
ATOM   2383 C CA  . TYR A 1 332 ? 16.308 45.753 9.352  1.00 25.09 ? 362 TYR A CA  1 
ATOM   2384 C C   . TYR A 1 332 ? 17.702 46.352 9.500  1.00 25.71 ? 362 TYR A C   1 
ATOM   2385 O O   . TYR A 1 332 ? 18.185 46.569 10.619 1.00 24.67 ? 362 TYR A O   1 
ATOM   2386 C CB  . TYR A 1 332 ? 16.410 44.264 9.016  1.00 27.63 ? 362 TYR A CB  1 
ATOM   2387 C CG  . TYR A 1 332 ? 17.453 43.557 9.849  1.00 23.37 ? 362 TYR A CG  1 
ATOM   2388 C CD1 . TYR A 1 332 ? 17.203 43.239 11.176 1.00 25.89 ? 362 TYR A CD1 1 
ATOM   2389 C CD2 . TYR A 1 332 ? 18.695 43.233 9.320  1.00 23.79 ? 362 TYR A CD2 1 
ATOM   2390 C CE1 . TYR A 1 332 ? 18.155 42.606 11.953 1.00 27.46 ? 362 TYR A CE1 1 
ATOM   2391 C CE2 . TYR A 1 332 ? 19.655 42.597 10.089 1.00 24.52 ? 362 TYR A CE2 1 
ATOM   2392 C CZ  . TYR A 1 332 ? 19.378 42.287 11.405 1.00 29.65 ? 362 TYR A CZ  1 
ATOM   2393 O OH  . TYR A 1 332 ? 20.324 41.655 12.178 1.00 31.07 ? 362 TYR A OH  1 
ATOM   2394 N N   . LEU A 1 333 ? 18.384 46.583 8.374  1.00 24.66 ? 363 LEU A N   1 
ATOM   2395 C CA  . LEU A 1 333 ? 19.726 47.153 8.433  1.00 23.38 ? 363 LEU A CA  1 
ATOM   2396 C C   . LEU A 1 333 ? 19.710 48.502 9.135  1.00 21.35 ? 363 LEU A C   1 
ATOM   2397 O O   . LEU A 1 333 ? 20.562 48.779 9.982  1.00 22.80 ? 363 LEU A O   1 
ATOM   2398 C CB  . LEU A 1 333 ? 20.312 47.284 7.028  1.00 20.15 ? 363 LEU A CB  1 
ATOM   2399 C CG  . LEU A 1 333 ? 20.732 45.984 6.339  1.00 26.42 ? 363 LEU A CG  1 
ATOM   2400 C CD1 . LEU A 1 333 ? 21.437 46.271 5.021  1.00 26.18 ? 363 LEU A CD1 1 
ATOM   2401 C CD2 . LEU A 1 333 ? 21.618 45.153 7.253  1.00 21.96 ? 363 LEU A CD2 1 
ATOM   2402 N N   . GLU A 1 334 ? 18.734 49.347 8.809  1.00 22.93 ? 364 GLU A N   1 
ATOM   2403 C CA  . GLU A 1 334 ? 18.631 50.641 9.471  1.00 25.97 ? 364 GLU A CA  1 
ATOM   2404 C C   . GLU A 1 334 ? 18.385 50.474 10.967 1.00 26.45 ? 364 GLU A C   1 
ATOM   2405 O O   . GLU A 1 334 ? 19.121 51.033 11.784 1.00 24.93 ? 364 GLU A O   1 
ATOM   2406 C CB  . GLU A 1 334 ? 17.537 51.476 8.808  1.00 25.08 ? 364 GLU A CB  1 
ATOM   2407 C CG  . GLU A 1 334 ? 17.921 51.891 7.396  1.00 28.95 ? 364 GLU A CG  1 
ATOM   2408 C CD  . GLU A 1 334 ? 16.868 52.731 6.701  1.00 31.23 ? 364 GLU A CD  1 
ATOM   2409 O OE1 . GLU A 1 334 ? 15.705 52.743 7.160  1.00 26.82 ? 364 GLU A OE1 1 
ATOM   2410 O OE2 . GLU A 1 334 ? 17.215 53.379 5.688  1.00 28.77 ? 364 GLU A OE2 1 
ATOM   2411 N N   . ALA A 1 335 ? 17.403 49.644 11.340 1.00 28.15 ? 365 ALA A N   1 
ATOM   2412 C CA  . ALA A 1 335 ? 17.073 49.450 12.750 1.00 24.23 ? 365 ALA A CA  1 
ATOM   2413 C C   . ALA A 1 335 ? 18.267 48.953 13.558 1.00 26.56 ? 365 ALA A C   1 
ATOM   2414 O O   . ALA A 1 335 ? 18.471 49.385 14.698 1.00 27.69 ? 365 ALA A O   1 
ATOM   2415 C CB  . ALA A 1 335 ? 15.908 48.472 12.885 1.00 22.95 ? 365 ALA A CB  1 
ATOM   2416 N N   . GLN A 1 336 ? 19.067 48.047 12.995 1.00 24.85 ? 366 GLN A N   1 
ATOM   2417 C CA  . GLN A 1 336 ? 20.137 47.449 13.786 1.00 22.44 ? 366 GLN A CA  1 
ATOM   2418 C C   . GLN A 1 336 ? 21.446 48.221 13.713 1.00 26.12 ? 366 GLN A C   1 
ATOM   2419 O O   . GLN A 1 336 ? 22.189 48.249 14.702 1.00 24.11 ? 366 GLN A O   1 
ATOM   2420 C CB  . GLN A 1 336 ? 20.369 45.996 13.356 1.00 23.60 ? 366 GLN A CB  1 
ATOM   2421 C CG  . GLN A 1 336 ? 21.553 45.287 14.029 1.00 21.03 ? 366 GLN A CG  1 
ATOM   2422 C CD  . GLN A 1 336 ? 21.372 45.078 15.533 1.00 28.93 ? 366 GLN A CD  1 
ATOM   2423 O OE1 . GLN A 1 336 ? 20.731 44.122 15.968 1.00 25.88 ? 366 GLN A OE1 1 
ATOM   2424 N NE2 . GLN A 1 336 ? 21.950 45.968 16.328 1.00 18.00 ? 366 GLN A NE2 1 
ATOM   2425 N N   . PHE A 1 337 ? 21.748 48.881 12.593 1.00 26.63 ? 367 PHE A N   1 
ATOM   2426 C CA  . PHE A 1 337 ? 23.064 49.470 12.404 1.00 23.94 ? 367 PHE A CA  1 
ATOM   2427 C C   . PHE A 1 337 ? 23.064 50.983 12.194 1.00 23.43 ? 367 PHE A C   1 
ATOM   2428 O O   . PHE A 1 337 ? 24.149 51.564 12.080 1.00 28.46 ? 367 PHE A O   1 
ATOM   2429 C CB  . PHE A 1 337 ? 23.774 48.782 11.227 1.00 24.33 ? 367 PHE A CB  1 
ATOM   2430 C CG  . PHE A 1 337 ? 23.898 47.286 11.387 1.00 25.79 ? 367 PHE A CG  1 
ATOM   2431 C CD1 . PHE A 1 337 ? 24.879 46.733 12.196 1.00 25.84 ? 367 PHE A CD1 1 
ATOM   2432 C CD2 . PHE A 1 337 ? 23.031 46.434 10.725 1.00 25.52 ? 367 PHE A CD2 1 
ATOM   2433 C CE1 . PHE A 1 337 ? 24.988 45.358 12.344 1.00 24.16 ? 367 PHE A CE1 1 
ATOM   2434 C CE2 . PHE A 1 337 ? 23.139 45.053 10.867 1.00 24.75 ? 367 PHE A CE2 1 
ATOM   2435 C CZ  . PHE A 1 337 ? 24.117 44.517 11.675 1.00 21.17 ? 367 PHE A CZ  1 
ATOM   2436 N N   . GLY A 1 338 ? 21.903 51.647 12.156 1.00 23.74 ? 368 GLY A N   1 
ATOM   2437 C CA  . GLY A 1 338 ? 21.889 53.099 12.095 1.00 26.24 ? 368 GLY A CA  1 
ATOM   2438 C C   . GLY A 1 338 ? 22.549 53.641 10.843 1.00 29.17 ? 368 GLY A C   1 
ATOM   2439 O O   . GLY A 1 338 ? 22.244 53.234 9.715  1.00 24.47 ? 368 GLY A O   1 
ATOM   2440 N N   . ASP A 1 339 ? 23.485 54.571 11.050 1.00 30.91 ? 369 ASP A N   1 
ATOM   2441 C CA  . ASP A 1 339 ? 24.194 55.212 9.952  1.00 26.15 ? 369 ASP A CA  1 
ATOM   2442 C C   . ASP A 1 339 ? 25.145 54.269 9.228  1.00 28.30 ? 369 ASP A C   1 
ATOM   2443 O O   . ASP A 1 339 ? 25.600 54.605 8.130  1.00 34.22 ? 369 ASP A O   1 
ATOM   2444 C CB  . ASP A 1 339 ? 24.960 56.427 10.474 1.00 26.60 ? 369 ASP A CB  1 
ATOM   2445 C CG  . ASP A 1 339 ? 25.860 56.088 11.650 1.00 35.86 ? 369 ASP A CG  1 
ATOM   2446 O OD1 . ASP A 1 339 ? 25.373 55.469 12.621 1.00 32.10 ? 369 ASP A OD1 1 
ATOM   2447 O OD2 . ASP A 1 339 ? 27.059 56.436 11.595 1.00 39.69 ? 369 ASP A OD2 1 
ATOM   2448 N N   . GLN A 1 340 ? 25.454 53.106 9.804  1.00 24.17 ? 370 GLN A N   1 
ATOM   2449 C CA  . GLN A 1 340 ? 26.300 52.110 9.155  1.00 27.80 ? 370 GLN A CA  1 
ATOM   2450 C C   . GLN A 1 340 ? 25.505 51.125 8.303  1.00 26.63 ? 370 GLN A C   1 
ATOM   2451 O O   . GLN A 1 340 ? 26.048 50.084 7.902  1.00 26.13 ? 370 GLN A O   1 
ATOM   2452 C CB  . GLN A 1 340 ? 27.112 51.337 10.201 1.00 30.85 ? 370 GLN A CB  1 
ATOM   2453 C CG  . GLN A 1 340 ? 27.367 52.088 11.502 1.00 38.89 ? 370 GLN A CG  1 
ATOM   2454 C CD  . GLN A 1 340 ? 28.443 53.149 11.384 1.00 42.21 ? 370 GLN A CD  1 
ATOM   2455 O OE1 . GLN A 1 340 ? 28.973 53.401 10.301 1.00 43.03 ? 370 GLN A OE1 1 
ATOM   2456 N NE2 . GLN A 1 340 ? 28.773 53.779 12.508 1.00 57.63 ? 370 GLN A NE2 1 
ATOM   2457 N N   . ALA A 1 341 ? 24.228 51.421 8.042  1.00 23.44 ? 371 ALA A N   1 
ATOM   2458 C CA  . ALA A 1 341 ? 23.401 50.511 7.258  1.00 23.87 ? 371 ALA A CA  1 
ATOM   2459 C C   . ALA A 1 341 ? 23.943 50.348 5.845  1.00 19.14 ? 371 ALA A C   1 
ATOM   2460 O O   . ALA A 1 341 ? 23.961 49.237 5.307  1.00 23.95 ? 371 ALA A O   1 
ATOM   2461 C CB  . ALA A 1 341 ? 21.957 51.007 7.229  1.00 19.14 ? 371 ALA A CB  1 
ATOM   2462 N N   . ALA A 1 342 ? 24.406 51.439 5.233  1.00 22.10 ? 372 ALA A N   1 
ATOM   2463 C CA  . ALA A 1 342 ? 24.964 51.343 3.888  1.00 25.90 ? 372 ALA A CA  1 
ATOM   2464 C C   . ALA A 1 342 ? 26.249 50.527 3.873  1.00 26.02 ? 372 ALA A C   1 
ATOM   2465 O O   . ALA A 1 342 ? 26.482 49.750 2.942  1.00 28.13 ? 372 ALA A O   1 
ATOM   2466 C CB  . ALA A 1 342 ? 25.213 52.736 3.321  1.00 26.13 ? 372 ALA A CB  1 
ATOM   2467 N N   . ALA A 1 343 ? 27.088 50.674 4.900  1.00 25.44 ? 373 ALA A N   1 
ATOM   2468 C CA  . ALA A 1 343 ? 28.326 49.901 4.954  1.00 27.36 ? 373 ALA A CA  1 
ATOM   2469 C C   . ALA A 1 343 ? 28.039 48.412 5.109  1.00 22.78 ? 373 ALA A C   1 
ATOM   2470 O O   . ALA A 1 343 ? 28.641 47.573 4.424  1.00 26.59 ? 373 ALA A O   1 
ATOM   2471 C CB  . ALA A 1 343 ? 29.206 50.404 6.097  1.00 25.76 ? 373 ALA A CB  1 
ATOM   2472 N N   . VAL A 1 344 ? 27.112 48.067 6.007  1.00 23.75 ? 374 VAL A N   1 
ATOM   2473 C CA  . VAL A 1 344 ? 26.734 46.667 6.180  1.00 23.40 ? 374 VAL A CA  1 
ATOM   2474 C C   . VAL A 1 344 ? 26.090 46.124 4.909  1.00 24.03 ? 374 VAL A C   1 
ATOM   2475 O O   . VAL A 1 344 ? 26.301 44.964 4.545  1.00 23.04 ? 374 VAL A O   1 
ATOM   2476 C CB  . VAL A 1 344 ? 25.815 46.506 7.406  1.00 26.05 ? 374 VAL A CB  1 
ATOM   2477 C CG1 . VAL A 1 344 ? 25.365 45.062 7.553  1.00 24.75 ? 374 VAL A CG1 1 
ATOM   2478 C CG2 . VAL A 1 344 ? 26.540 46.980 8.662  1.00 24.97 ? 374 VAL A CG2 1 
ATOM   2479 N N   . ALA A 1 345 ? 25.299 46.948 4.214  1.00 25.69 ? 375 ALA A N   1 
ATOM   2480 C CA  . ALA A 1 345 ? 24.722 46.524 2.942  1.00 25.61 ? 375 ALA A CA  1 
ATOM   2481 C C   . ALA A 1 345 ? 25.809 46.275 1.903  1.00 29.47 ? 375 ALA A C   1 
ATOM   2482 O O   . ALA A 1 345 ? 25.691 45.368 1.072  1.00 28.52 ? 375 ALA A O   1 
ATOM   2483 C CB  . ALA A 1 345 ? 23.725 47.570 2.442  1.00 22.10 ? 375 ALA A CB  1 
ATOM   2484 N N   . ALA A 1 346 ? 26.863 47.092 1.914  1.00 27.79 ? 376 ALA A N   1 
ATOM   2485 C CA  . ALA A 1 346 ? 27.976 46.862 1.001  1.00 30.16 ? 376 ALA A CA  1 
ATOM   2486 C C   . ALA A 1 346 ? 28.674 45.546 1.319  1.00 30.26 ? 376 ALA A C   1 
ATOM   2487 O O   . ALA A 1 346 ? 29.080 44.813 0.408  1.00 30.00 ? 376 ALA A O   1 
ATOM   2488 C CB  . ALA A 1 346 ? 28.958 48.033 1.062  1.00 32.10 ? 376 ALA A CB  1 
ATOM   2489 N N   . CYS A 1 347 ? 28.813 45.231 2.609  1.00 25.09 ? 377 CYS A N   1 
ATOM   2490 C CA  . CYS A 1 347 ? 29.417 43.964 3.005  1.00 25.86 ? 377 CYS A CA  1 
ATOM   2491 C C   . CYS A 1 347 ? 28.470 42.792 2.775  1.00 24.77 ? 377 CYS A C   1 
ATOM   2492 O O   . CYS A 1 347 ? 28.924 41.671 2.520  1.00 30.13 ? 377 CYS A O   1 
ATOM   2493 C CB  . CYS A 1 347 ? 29.841 44.035 4.474  1.00 29.45 ? 377 CYS A CB  1 
ATOM   2494 S SG  . CYS A 1 347 ? 31.088 42.831 4.974  1.00 50.26 ? 377 CYS A SG  1 
ATOM   2495 N N   . TYR A 1 348 ? 27.162 43.026 2.863  1.00 22.05 ? 378 TYR A N   1 
ATOM   2496 C CA  . TYR A 1 348 ? 26.150 41.976 2.743  1.00 25.38 ? 378 TYR A CA  1 
ATOM   2497 C C   . TYR A 1 348 ? 25.075 42.436 1.766  1.00 24.51 ? 378 TYR A C   1 
ATOM   2498 O O   . TYR A 1 348 ? 23.946 42.745 2.164  1.00 24.61 ? 378 TYR A O   1 
ATOM   2499 C CB  . TYR A 1 348 ? 25.542 41.645 4.107  1.00 20.37 ? 378 TYR A CB  1 
ATOM   2500 C CG  . TYR A 1 348 ? 26.517 41.088 5.127  1.00 24.40 ? 378 TYR A CG  1 
ATOM   2501 C CD1 . TYR A 1 348 ? 27.225 41.930 5.977  1.00 20.17 ? 378 TYR A CD1 1 
ATOM   2502 C CD2 . TYR A 1 348 ? 26.710 39.718 5.255  1.00 23.74 ? 378 TYR A CD2 1 
ATOM   2503 C CE1 . TYR A 1 348 ? 28.106 41.424 6.916  1.00 23.33 ? 378 TYR A CE1 1 
ATOM   2504 C CE2 . TYR A 1 348 ? 27.588 39.204 6.191  1.00 24.56 ? 378 TYR A CE2 1 
ATOM   2505 C CZ  . TYR A 1 348 ? 28.282 40.060 7.017  1.00 24.69 ? 378 TYR A CZ  1 
ATOM   2506 O OH  . TYR A 1 348 ? 29.155 39.545 7.946  1.00 21.56 ? 378 TYR A OH  1 
ATOM   2507 N N   . PRO A 1 349 ? 25.389 42.488 0.475  1.00 23.79 ? 379 PRO A N   1 
ATOM   2508 C CA  . PRO A 1 349 ? 24.444 43.069 -0.485 1.00 23.22 ? 379 PRO A CA  1 
ATOM   2509 C C   . PRO A 1 349 ? 23.339 42.107 -0.883 1.00 27.45 ? 379 PRO A C   1 
ATOM   2510 O O   . PRO A 1 349 ? 23.521 40.889 -0.924 1.00 25.20 ? 379 PRO A O   1 
ATOM   2511 C CB  . PRO A 1 349 ? 25.332 43.410 -1.687 1.00 29.40 ? 379 PRO A CB  1 
ATOM   2512 C CG  . PRO A 1 349 ? 26.437 42.409 -1.617 1.00 28.16 ? 379 PRO A CG  1 
ATOM   2513 C CD  . PRO A 1 349 ? 26.666 42.108 -0.158 1.00 21.90 ? 379 PRO A CD  1 
ATOM   2514 N N   . LEU A 1 350 ? 22.166 42.683 -1.157 1.00 27.04 ? 380 LEU A N   1 
ATOM   2515 C CA  . LEU A 1 350 ? 21.077 41.972 -1.829 1.00 27.78 ? 380 LEU A CA  1 
ATOM   2516 C C   . LEU A 1 350 ? 21.266 42.164 -3.330 1.00 23.16 ? 380 LEU A C   1 
ATOM   2517 O O   . LEU A 1 350 ? 20.645 43.020 -3.961 1.00 21.17 ? 380 LEU A O   1 
ATOM   2518 C CB  . LEU A 1 350 ? 19.718 42.486 -1.370 1.00 23.61 ? 380 LEU A CB  1 
ATOM   2519 C CG  . LEU A 1 350 ? 19.010 41.781 -0.215 1.00 33.84 ? 380 LEU A CG  1 
ATOM   2520 C CD1 . LEU A 1 350 ? 17.607 42.352 -0.049 1.00 32.43 ? 380 LEU A CD1 1 
ATOM   2521 C CD2 . LEU A 1 350 ? 18.952 40.285 -0.452 1.00 29.79 ? 380 LEU A CD2 1 
ATOM   2522 N N   . ASP A 1 351 ? 22.156 41.357 -3.908 1.00 25.07 ? 381 ASP A N   1 
ATOM   2523 C CA  . ASP A 1 351 ? 22.506 41.484 -5.317 1.00 27.73 ? 381 ASP A CA  1 
ATOM   2524 C C   . ASP A 1 351 ? 21.958 40.344 -6.166 1.00 29.33 ? 381 ASP A C   1 
ATOM   2525 O O   . ASP A 1 351 ? 22.379 40.182 -7.316 1.00 32.51 ? 381 ASP A O   1 
ATOM   2526 C CB  . ASP A 1 351 ? 24.027 41.588 -5.478 1.00 29.88 ? 381 ASP A CB  1 
ATOM   2527 C CG  . ASP A 1 351 ? 24.767 40.409 -4.872 1.00 31.44 ? 381 ASP A CG  1 
ATOM   2528 O OD1 . ASP A 1 351 ? 24.115 39.447 -4.413 1.00 32.61 ? 381 ASP A OD1 1 
ATOM   2529 O OD2 . ASP A 1 351 ? 26.013 40.448 -4.853 1.00 37.48 ? 381 ASP A OD2 1 
ATOM   2530 N N   . GLY A 1 352 ? 21.023 39.560 -5.636 1.00 28.72 ? 382 GLY A N   1 
ATOM   2531 C CA  . GLY A 1 352 ? 20.478 38.422 -6.344 1.00 28.58 ? 382 GLY A CA  1 
ATOM   2532 C C   . GLY A 1 352 ? 21.097 37.095 -5.967 1.00 30.06 ? 382 GLY A C   1 
ATOM   2533 O O   . GLY A 1 352 ? 20.588 36.049 -6.389 1.00 30.90 ? 382 GLY A O   1 
ATOM   2534 N N   . ARG A 1 353 ? 22.177 37.107 -5.186 1.00 28.40 ? 383 ARG A N   1 
ATOM   2535 C CA  . ARG A 1 353 ? 22.821 35.865 -4.775 1.00 35.86 ? 383 ARG A CA  1 
ATOM   2536 C C   . ARG A 1 353 ? 22.082 35.184 -3.629 1.00 33.07 ? 383 ARG A C   1 
ATOM   2537 O O   . ARG A 1 353 ? 22.122 33.954 -3.518 1.00 31.90 ? 383 ARG A O   1 
ATOM   2538 C CB  . ARG A 1 353 ? 24.273 36.142 -4.380 1.00 43.79 ? 383 ARG A CB  1 
ATOM   2539 C CG  . ARG A 1 353 ? 25.292 35.762 -5.434 1.00 45.67 ? 383 ARG A CG  1 
ATOM   2540 C CD  . ARG A 1 353 ? 26.527 36.643 -5.363 1.00 44.60 ? 383 ARG A CD  1 
ATOM   2541 N NE  . ARG A 1 353 ? 26.361 37.837 -6.186 1.00 62.25 ? 383 ARG A NE  1 
ATOM   2542 C CZ  . ARG A 1 353 ? 27.335 38.426 -6.867 1.00 66.78 ? 383 ARG A CZ  1 
ATOM   2543 N NH1 . ARG A 1 353 ? 28.583 37.979 -6.817 1.00 67.04 ? 383 ARG A NH1 1 
ATOM   2544 N NH2 . ARG A 1 353 ? 27.044 39.471 -7.639 1.00 55.60 ? 383 ARG A NH2 1 
ATOM   2545 N N   . ALA A 1 354 ? 21.406 35.953 -2.776 1.00 34.34 ? 384 ALA A N   1 
ATOM   2546 C CA  . ALA A 1 354 ? 20.711 35.384 -1.631 1.00 33.39 ? 384 ALA A CA  1 
ATOM   2547 C C   . ALA A 1 354 ? 19.460 36.197 -1.334 1.00 28.89 ? 384 ALA A C   1 
ATOM   2548 O O   . ALA A 1 354 ? 19.345 37.362 -1.720 1.00 36.11 ? 384 ALA A O   1 
ATOM   2549 C CB  . ALA A 1 354 ? 21.614 35.330 -0.396 1.00 31.82 ? 384 ALA A CB  1 
ATOM   2550 N N   . THR A 1 355 ? 18.520 35.561 -0.644 1.00 33.03 ? 385 THR A N   1 
ATOM   2551 C CA  . THR A 1 355 ? 17.298 36.221 -0.215 1.00 26.84 ? 385 THR A CA  1 
ATOM   2552 C C   . THR A 1 355 ? 17.568 37.123 0.987  1.00 26.91 ? 385 THR A C   1 
ATOM   2553 O O   . THR A 1 355 ? 18.608 37.004 1.642  1.00 25.64 ? 385 THR A O   1 
ATOM   2554 C CB  . THR A 1 355 ? 16.245 35.183 0.153  1.00 32.85 ? 385 THR A CB  1 
ATOM   2555 O OG1 . THR A 1 355 ? 16.657 34.488 1.336  1.00 29.93 ? 385 THR A OG1 1 
ATOM   2556 C CG2 . THR A 1 355 ? 16.063 34.185 -0.979 1.00 32.40 ? 385 THR A CG2 1 
ATOM   2557 N N   . PRO A 1 356 ? 16.653 38.054 1.287  1.00 26.79 ? 386 PRO A N   1 
ATOM   2558 C CA  . PRO A 1 356 ? 16.813 38.847 2.519  1.00 23.69 ? 386 PRO A CA  1 
ATOM   2559 C C   . PRO A 1 356 ? 16.934 37.994 3.770  1.00 23.57 ? 386 PRO A C   1 
ATOM   2560 O O   . PRO A 1 356 ? 17.743 38.316 4.650  1.00 19.66 ? 386 PRO A O   1 
ATOM   2561 C CB  . PRO A 1 356 ? 15.550 39.725 2.548  1.00 25.36 ? 386 PRO A CB  1 
ATOM   2562 C CG  . PRO A 1 356 ? 14.752 39.368 1.318  1.00 28.45 ? 386 PRO A CG  1 
ATOM   2563 C CD  . PRO A 1 356 ? 15.646 38.637 0.385  1.00 23.40 ? 386 PRO A CD  1 
ATOM   2564 N N   . LYS A 1 357 ? 16.145 36.921 3.880  1.00 20.36 ? 387 LYS A N   1 
ATOM   2565 C CA  . LYS A 1 357 ? 16.282 36.007 5.010  1.00 22.71 ? 387 LYS A CA  1 
ATOM   2566 C C   . LYS A 1 357 ? 17.688 35.430 5.075  1.00 23.93 ? 387 LYS A C   1 
ATOM   2567 O O   . LYS A 1 357 ? 18.300 35.371 6.148  1.00 21.98 ? 387 LYS A O   1 
ATOM   2568 C CB  . LYS A 1 357 ? 15.258 34.878 4.907  1.00 23.69 ? 387 LYS A CB  1 
ATOM   2569 C CG  . LYS A 1 357 ? 13.887 35.205 5.458  1.00 31.48 ? 387 LYS A CG  1 
ATOM   2570 C CD  . LYS A 1 357 ? 12.904 34.091 5.125  1.00 32.53 ? 387 LYS A CD  1 
ATOM   2571 C CE  . LYS A 1 357 ? 12.021 33.757 6.314  1.00 48.16 ? 387 LYS A CE  1 
ATOM   2572 N NZ  . LYS A 1 357 ? 11.219 34.928 6.759  1.00 56.42 ? 387 LYS A NZ  1 
ATOM   2573 N N   . GLU A 1 358 ? 18.217 34.997 3.929  1.00 24.88 ? 388 GLU A N   1 
ATOM   2574 C CA  . GLU A 1 358 ? 19.550 34.406 3.911  1.00 27.15 ? 388 GLU A CA  1 
ATOM   2575 C C   . GLU A 1 358 ? 20.611 35.425 4.305  1.00 22.60 ? 388 GLU A C   1 
ATOM   2576 O O   . GLU A 1 358 ? 21.568 35.090 5.009  1.00 25.10 ? 388 GLU A O   1 
ATOM   2577 C CB  . GLU A 1 358 ? 19.842 33.808 2.534  1.00 24.05 ? 388 GLU A CB  1 
ATOM   2578 C CG  . GLU A 1 358 ? 19.049 32.539 2.246  1.00 28.22 ? 388 GLU A CG  1 
ATOM   2579 C CD  . GLU A 1 358 ? 19.140 32.096 0.797  1.00 38.57 ? 388 GLU A CD  1 
ATOM   2580 O OE1 . GLU A 1 358 ? 19.519 32.920 -0.059 1.00 34.88 ? 388 GLU A OE1 1 
ATOM   2581 O OE2 . GLU A 1 358 ? 18.826 30.920 0.513  1.00 42.98 ? 388 GLU A OE2 1 
ATOM   2582 N N   . MET A 1 359 ? 20.441 36.685 3.895  1.00 21.09 ? 389 MET A N   1 
ATOM   2583 C CA  . MET A 1 359 ? 21.428 37.705 4.235  1.00 20.03 ? 389 MET A CA  1 
ATOM   2584 C C   . MET A 1 359 ? 21.358 38.080 5.711  1.00 22.17 ? 389 MET A C   1 
ATOM   2585 O O   . MET A 1 359 ? 22.396 38.265 6.358  1.00 26.84 ? 389 MET A O   1 
ATOM   2586 C CB  . MET A 1 359 ? 21.234 38.940 3.358  1.00 20.18 ? 389 MET A CB  1 
ATOM   2587 C CG  . MET A 1 359 ? 21.491 38.701 1.873  1.00 26.53 ? 389 MET A CG  1 
ATOM   2588 S SD  . MET A 1 359 ? 23.060 37.867 1.517  1.00 37.48 ? 389 MET A SD  1 
ATOM   2589 C CE  . MET A 1 359 ? 24.237 38.922 2.333  1.00 17.73 ? 389 MET A CE  1 
ATOM   2590 N N   . VAL A 1 360 ? 20.149 38.208 6.262  1.00 19.33 ? 390 VAL A N   1 
ATOM   2591 C CA  . VAL A 1 360 ? 20.023 38.458 7.695  1.00 22.00 ? 390 VAL A CA  1 
ATOM   2592 C C   . VAL A 1 360 ? 20.626 37.303 8.486  1.00 21.18 ? 390 VAL A C   1 
ATOM   2593 O O   . VAL A 1 360 ? 21.297 37.513 9.504  1.00 19.68 ? 390 VAL A O   1 
ATOM   2594 C CB  . VAL A 1 360 ? 18.548 38.711 8.068  1.00 19.38 ? 390 VAL A CB  1 
ATOM   2595 C CG1 . VAL A 1 360 ? 18.364 38.739 9.578  1.00 22.82 ? 390 VAL A CG1 1 
ATOM   2596 C CG2 . VAL A 1 360 ? 18.071 40.020 7.455  1.00 19.81 ? 390 VAL A CG2 1 
ATOM   2597 N N   . ALA A 1 361 ? 20.428 36.068 8.013  1.00 22.57 ? 391 ALA A N   1 
ATOM   2598 C CA  . ALA A 1 361 ? 21.045 34.917 8.664  1.00 24.94 ? 391 ALA A CA  1 
ATOM   2599 C C   . ALA A 1 361 ? 22.567 34.979 8.581  1.00 23.93 ? 391 ALA A C   1 
ATOM   2600 O O   . ALA A 1 361 ? 23.257 34.670 9.558  1.00 21.85 ? 391 ALA A O   1 
ATOM   2601 C CB  . ALA A 1 361 ? 20.525 33.620 8.044  1.00 21.88 ? 391 ALA A CB  1 
ATOM   2602 N N   . ARG A 1 362 ? 23.109 35.360 7.418  1.00 21.41 ? 392 ARG A N   1 
ATOM   2603 C CA  . ARG A 1 362 ? 24.555 35.540 7.292  1.00 22.26 ? 392 ARG A CA  1 
ATOM   2604 C C   . ARG A 1 362 ? 25.064 36.545 8.315  1.00 23.48 ? 392 ARG A C   1 
ATOM   2605 O O   . ARG A 1 362 ? 26.045 36.288 9.024  1.00 18.89 ? 392 ARG A O   1 
ATOM   2606 C CB  . ARG A 1 362 ? 24.925 36.012 5.881  1.00 23.31 ? 392 ARG A CB  1 
ATOM   2607 C CG  . ARG A 1 362 ? 24.602 35.058 4.742  1.00 30.90 ? 392 ARG A CG  1 
ATOM   2608 C CD  . ARG A 1 362 ? 25.701 34.037 4.493  1.00 39.83 ? 392 ARG A CD  1 
ATOM   2609 N NE  . ARG A 1 362 ? 25.650 32.934 5.444  1.00 52.40 ? 392 ARG A NE  1 
ATOM   2610 C CZ  . ARG A 1 362 ? 26.314 31.794 5.305  1.00 58.64 ? 392 ARG A CZ  1 
ATOM   2611 N NH1 . ARG A 1 362 ? 27.086 31.566 4.254  1.00 60.99 ? 392 ARG A NH1 1 
ATOM   2612 N NH2 . ARG A 1 362 ? 26.197 30.857 6.242  1.00 45.83 ? 392 ARG A NH2 1 
ATOM   2613 N N   . ILE A 1 363 ? 24.412 37.708 8.387  1.00 20.74 ? 393 ILE A N   1 
ATOM   2614 C CA  . ILE A 1 363 ? 24.846 38.763 9.299  1.00 20.93 ? 393 ILE A CA  1 
ATOM   2615 C C   . ILE A 1 363 ? 24.810 38.265 10.737 1.00 20.84 ? 393 ILE A C   1 
ATOM   2616 O O   . ILE A 1 363 ? 25.776 38.424 11.496 1.00 20.31 ? 393 ILE A O   1 
ATOM   2617 C CB  . ILE A 1 363 ? 23.975 40.019 9.116  1.00 20.56 ? 393 ILE A CB  1 
ATOM   2618 C CG1 . ILE A 1 363 ? 24.198 40.629 7.733  1.00 21.82 ? 393 ILE A CG1 1 
ATOM   2619 C CG2 . ILE A 1 363 ? 24.271 41.043 10.199 1.00 16.30 ? 393 ILE A CG2 1 
ATOM   2620 C CD1 . ILE A 1 363 ? 23.257 41.775 7.421  1.00 24.37 ? 393 ILE A CD1 1 
ATOM   2621 N N   . PHE A 1 364 ? 23.696 37.643 11.127 1.00 18.44 ? 394 PHE A N   1 
ATOM   2622 C CA  . PHE A 1 364 ? 23.544 37.169 12.497 1.00 20.53 ? 394 PHE A CA  1 
ATOM   2623 C C   . PHE A 1 364 ? 24.599 36.122 12.837 1.00 20.57 ? 394 PHE A C   1 
ATOM   2624 O O   . PHE A 1 364 ? 25.244 36.196 13.888 1.00 17.02 ? 394 PHE A O   1 
ATOM   2625 C CB  . PHE A 1 364 ? 22.138 36.606 12.695 1.00 17.88 ? 394 PHE A CB  1 
ATOM   2626 C CG  . PHE A 1 364 ? 21.743 36.454 14.132 1.00 20.10 ? 394 PHE A CG  1 
ATOM   2627 C CD1 . PHE A 1 364 ? 22.166 35.358 14.871 1.00 18.13 ? 394 PHE A CD1 1 
ATOM   2628 C CD2 . PHE A 1 364 ? 20.935 37.400 14.744 1.00 18.84 ? 394 PHE A CD2 1 
ATOM   2629 C CE1 . PHE A 1 364 ? 21.801 35.216 16.200 1.00 23.54 ? 394 PHE A CE1 1 
ATOM   2630 C CE2 . PHE A 1 364 ? 20.563 37.261 16.073 1.00 26.20 ? 394 PHE A CE2 1 
ATOM   2631 C CZ  . PHE A 1 364 ? 20.995 36.167 16.800 1.00 24.14 ? 394 PHE A CZ  1 
ATOM   2632 N N   . GLY A 1 365 ? 24.792 35.140 11.953 1.00 18.79 ? 395 GLY A N   1 
ATOM   2633 C CA  . GLY A 1 365 ? 25.752 34.084 12.227 1.00 18.50 ? 395 GLY A CA  1 
ATOM   2634 C C   . GLY A 1 365 ? 27.183 34.583 12.280 1.00 21.21 ? 395 GLY A C   1 
ATOM   2635 O O   . GLY A 1 365 ? 27.967 34.153 13.132 1.00 18.63 ? 395 GLY A O   1 
ATOM   2636 N N   . ASP A 1 366 ? 27.546 35.498 11.377 1.00 17.68 ? 396 ASP A N   1 
ATOM   2637 C CA  . ASP A 1 366 ? 28.886 36.071 11.416 1.00 20.37 ? 396 ASP A CA  1 
ATOM   2638 C C   . ASP A 1 366 ? 29.105 36.851 12.707 1.00 19.91 ? 396 ASP A C   1 
ATOM   2639 O O   . ASP A 1 366 ? 30.126 36.681 13.382 1.00 19.34 ? 396 ASP A O   1 
ATOM   2640 C CB  . ASP A 1 366 ? 29.115 36.973 10.201 1.00 17.80 ? 396 ASP A CB  1 
ATOM   2641 C CG  . ASP A 1 366 ? 29.359 36.193 8.918  1.00 18.28 ? 396 ASP A CG  1 
ATOM   2642 O OD1 . ASP A 1 366 ? 29.434 34.948 8.961  1.00 20.75 ? 396 ASP A OD1 1 
ATOM   2643 O OD2 . ASP A 1 366 ? 29.474 36.834 7.854  1.00 21.33 ? 396 ASP A OD2 1 
ATOM   2644 N N   . ASN A 1 367 ? 28.144 37.700 13.078 1.00 15.34 ? 397 ASN A N   1 
ATOM   2645 C CA  . ASN A 1 367 ? 28.345 38.569 14.232 1.00 17.78 ? 397 ASN A CA  1 
ATOM   2646 C C   . ASN A 1 367 ? 28.310 37.791 15.546 1.00 20.57 ? 397 ASN A C   1 
ATOM   2647 O O   . ASN A 1 367 ? 29.074 38.097 16.471 1.00 22.37 ? 397 ASN A O   1 
ATOM   2648 C CB  . ASN A 1 367 ? 27.291 39.678 14.229 1.00 21.77 ? 397 ASN A CB  1 
ATOM   2649 C CG  . ASN A 1 367 ? 27.342 40.540 15.480 1.00 23.37 ? 397 ASN A CG  1 
ATOM   2650 O OD1 . ASN A 1 367 ? 26.766 40.194 16.510 1.00 23.00 ? 397 ASN A OD1 1 
ATOM   2651 N ND2 . ASN A 1 367 ? 28.029 41.669 15.391 1.00 22.84 ? 397 ASN A ND2 1 
ATOM   2652 N N   . GLN A 1 368 ? 27.443 36.781 15.648 1.00 16.14 ? 398 GLN A N   1 
ATOM   2653 C CA  . GLN A 1 368 ? 27.206 36.097 16.911 1.00 20.72 ? 398 GLN A CA  1 
ATOM   2654 C C   . GLN A 1 368 ? 28.013 34.815 17.069 1.00 19.11 ? 398 GLN A C   1 
ATOM   2655 O O   . GLN A 1 368 ? 28.119 34.307 18.191 1.00 21.70 ? 398 GLN A O   1 
ATOM   2656 C CB  . GLN A 1 368 ? 25.712 35.775 17.069 1.00 18.38 ? 398 GLN A CB  1 
ATOM   2657 C CG  . GLN A 1 368 ? 24.816 36.992 17.270 1.00 23.61 ? 398 GLN A CG  1 
ATOM   2658 C CD  . GLN A 1 368 ? 25.000 37.644 18.636 1.00 24.93 ? 398 GLN A CD  1 
ATOM   2659 O OE1 . GLN A 1 368 ? 24.400 37.221 19.626 1.00 22.24 ? 398 GLN A OE1 1 
ATOM   2660 N NE2 . GLN A 1 368 ? 25.829 38.682 18.691 1.00 23.25 ? 398 GLN A NE2 1 
ATOM   2661 N N   . PHE A 1 369 ? 28.577 34.279 15.988 1.00 18.08 ? 399 PHE A N   1 
ATOM   2662 C CA  . PHE A 1 369 ? 29.290 33.010 16.079 1.00 17.67 ? 399 PHE A CA  1 
ATOM   2663 C C   . PHE A 1 369 ? 30.607 33.000 15.305 1.00 17.34 ? 399 PHE A C   1 
ATOM   2664 O O   . PHE A 1 369 ? 31.666 32.740 15.884 1.00 17.04 ? 399 PHE A O   1 
ATOM   2665 C CB  . PHE A 1 369 ? 28.387 31.870 15.597 1.00 17.15 ? 399 PHE A CB  1 
ATOM   2666 C CG  . PHE A 1 369 ? 27.152 31.677 16.439 1.00 17.10 ? 399 PHE A CG  1 
ATOM   2667 C CD1 . PHE A 1 369 ? 27.219 30.999 17.647 1.00 16.51 ? 399 PHE A CD1 1 
ATOM   2668 C CD2 . PHE A 1 369 ? 25.921 32.160 16.014 1.00 17.74 ? 399 PHE A CD2 1 
ATOM   2669 C CE1 . PHE A 1 369 ? 26.081 30.810 18.424 1.00 16.57 ? 399 PHE A CE1 1 
ATOM   2670 C CE2 . PHE A 1 369 ? 24.776 31.977 16.788 1.00 19.17 ? 399 PHE A CE2 1 
ATOM   2671 C CZ  . PHE A 1 369 ? 24.859 31.302 17.995 1.00 17.20 ? 399 PHE A CZ  1 
ATOM   2672 N N   . ASN A 1 370 ? 30.558 33.284 14.002 1.00 17.94 ? 400 ASN A N   1 
ATOM   2673 C CA  . ASN A 1 370 ? 31.703 32.991 13.138 1.00 20.28 ? 400 ASN A CA  1 
ATOM   2674 C C   . ASN A 1 370 ? 32.903 33.883 13.461 1.00 18.16 ? 400 ASN A C   1 
ATOM   2675 O O   . ASN A 1 370 ? 34.056 33.428 13.405 1.00 18.10 ? 400 ASN A O   1 
ATOM   2676 C CB  . ASN A 1 370 ? 31.302 33.133 11.670 1.00 18.74 ? 400 ASN A CB  1 
ATOM   2677 C CG  . ASN A 1 370 ? 30.305 32.082 11.239 1.00 26.96 ? 400 ASN A CG  1 
ATOM   2678 O OD1 . ASN A 1 370 ? 30.406 30.916 11.616 1.00 25.43 ? 400 ASN A OD1 1 
ATOM   2679 N ND2 . ASN A 1 370 ? 29.315 32.499 10.452 1.00 19.81 ? 400 ASN A ND2 1 
ATOM   2680 N N   . ARG A 1 371 ? 32.656 35.153 13.801 1.00 18.69 ? 401 ARG A N   1 
ATOM   2681 C CA  . ARG A 1 371 ? 33.746 36.066 14.134 1.00 20.34 ? 401 ARG A CA  1 
ATOM   2682 C C   . ARG A 1 371 ? 34.475 35.617 15.394 1.00 22.84 ? 401 ARG A C   1 
ATOM   2683 O O   . ARG A 1 371 ? 35.710 35.589 15.435 1.00 18.15 ? 401 ARG A O   1 
ATOM   2684 C CB  . ARG A 1 371 ? 33.209 37.488 14.298 1.00 19.78 ? 401 ARG A CB  1 
ATOM   2685 C CG  . ARG A 1 371 ? 34.309 38.525 14.437 1.00 26.56 ? 401 ARG A CG  1 
ATOM   2686 C CD  . ARG A 1 371 ? 33.771 39.906 14.759 1.00 27.48 ? 401 ARG A CD  1 
ATOM   2687 N NE  . ARG A 1 371 ? 33.323 40.001 16.143 1.00 31.69 ? 401 ARG A NE  1 
ATOM   2688 C CZ  . ARG A 1 371 ? 32.053 40.047 16.520 1.00 30.97 ? 401 ARG A CZ  1 
ATOM   2689 N NH1 . ARG A 1 371 ? 31.070 40.056 15.636 1.00 27.43 ? 401 ARG A NH1 1 
ATOM   2690 N NH2 . ARG A 1 371 ? 31.762 40.090 17.818 1.00 32.94 ? 401 ARG A NH2 1 
ATOM   2691 N N   . GLY A 1 372 ? 33.721 35.274 16.439 1.00 19.98 ? 402 GLY A N   1 
ATOM   2692 C CA  . GLY A 1 372 ? 34.342 34.819 17.670 1.00 17.11 ? 402 GLY A CA  1 
ATOM   2693 C C   . GLY A 1 372 ? 35.074 33.506 17.505 1.00 16.49 ? 402 GLY A C   1 
ATOM   2694 O O   . GLY A 1 372 ? 36.125 33.300 18.115 1.00 18.20 ? 402 GLY A O   1 
ATOM   2695 N N   . VAL A 1 373 ? 34.547 32.612 16.666 1.00 16.81 ? 403 VAL A N   1 
ATOM   2696 C CA  . VAL A 1 373 ? 35.224 31.346 16.420 1.00 15.89 ? 403 VAL A CA  1 
ATOM   2697 C C   . VAL A 1 373 ? 36.537 31.581 15.687 1.00 19.56 ? 403 VAL A C   1 
ATOM   2698 O O   . VAL A 1 373 ? 37.562 30.981 16.027 1.00 18.16 ? 403 VAL A O   1 
ATOM   2699 C CB  . VAL A 1 373 ? 34.296 30.387 15.658 1.00 17.64 ? 403 VAL A CB  1 
ATOM   2700 C CG1 . VAL A 1 373 ? 35.108 29.257 15.015 1.00 16.11 ? 403 VAL A CG1 1 
ATOM   2701 C CG2 . VAL A 1 373 ? 33.252 29.814 16.609 1.00 15.78 ? 403 VAL A CG2 1 
ATOM   2702 N N   . SER A 1 374 ? 36.536 32.460 14.679 1.00 17.15 ? 404 SER A N   1 
ATOM   2703 C CA  . SER A 1 374 ? 37.792 32.810 14.021 1.00 21.83 ? 404 SER A CA  1 
ATOM   2704 C C   . SER A 1 374 ? 38.785 33.408 15.010 1.00 20.54 ? 404 SER A C   1 
ATOM   2705 O O   . SER A 1 374 ? 39.966 33.038 15.015 1.00 20.48 ? 404 SER A O   1 
ATOM   2706 C CB  . SER A 1 374 ? 37.537 33.785 12.873 1.00 21.84 ? 404 SER A CB  1 
ATOM   2707 O OG  . SER A 1 374 ? 36.754 33.186 11.855 1.00 35.34 ? 404 SER A OG  1 
ATOM   2708 N N   . ALA A 1 375 ? 38.321 34.326 15.862 1.00 17.40 ? 405 ALA A N   1 
ATOM   2709 C CA  . ALA A 1 375 ? 39.223 35.000 16.789 1.00 17.50 ? 405 ALA A CA  1 
ATOM   2710 C C   . ALA A 1 375 ? 39.834 34.017 17.780 1.00 16.77 ? 405 ALA A C   1 
ATOM   2711 O O   . ALA A 1 375 ? 41.048 34.035 18.022 1.00 16.84 ? 405 ALA A O   1 
ATOM   2712 C CB  . ALA A 1 375 ? 38.479 36.112 17.521 1.00 17.82 ? 405 ALA A CB  1 
ATOM   2713 N N   . PHE A 1 376 ? 39.006 33.139 18.356 1.00 16.16 ? 406 PHE A N   1 
ATOM   2714 C CA  . PHE A 1 376 ? 39.517 32.145 19.296 1.00 16.51 ? 406 PHE A CA  1 
ATOM   2715 C C   . PHE A 1 376 ? 40.450 31.154 18.612 1.00 18.73 ? 406 PHE A C   1 
ATOM   2716 O O   . PHE A 1 376 ? 41.471 30.766 19.187 1.00 18.86 ? 406 PHE A O   1 
ATOM   2717 C CB  . PHE A 1 376 ? 38.363 31.407 19.973 1.00 15.07 ? 406 PHE A CB  1 
ATOM   2718 C CG  . PHE A 1 376 ? 38.037 31.924 21.349 1.00 17.13 ? 406 PHE A CG  1 
ATOM   2719 C CD1 . PHE A 1 376 ? 37.308 33.092 21.513 1.00 15.55 ? 406 PHE A CD1 1 
ATOM   2720 C CD2 . PHE A 1 376 ? 38.447 31.232 22.478 1.00 17.28 ? 406 PHE A CD2 1 
ATOM   2721 C CE1 . PHE A 1 376 ? 37.010 33.567 22.778 1.00 21.48 ? 406 PHE A CE1 1 
ATOM   2722 C CE2 . PHE A 1 376 ? 38.146 31.697 23.746 1.00 16.13 ? 406 PHE A CE2 1 
ATOM   2723 C CZ  . PHE A 1 376 ? 37.427 32.864 23.897 1.00 16.34 ? 406 PHE A CZ  1 
ATOM   2724 N N   . SER A 1 377 ? 40.120 30.726 17.387 1.00 15.54 ? 407 SER A N   1 
ATOM   2725 C CA  . SER A 1 377 ? 40.994 29.808 16.663 1.00 18.54 ? 407 SER A CA  1 
ATOM   2726 C C   . SER A 1 377 ? 42.367 30.425 16.444 1.00 18.51 ? 407 SER A C   1 
ATOM   2727 O O   . SER A 1 377 ? 43.399 29.801 16.730 1.00 20.36 ? 407 SER A O   1 
ATOM   2728 C CB  . SER A 1 377 ? 40.361 29.427 15.324 1.00 19.09 ? 407 SER A CB  1 
ATOM   2729 O OG  . SER A 1 377 ? 39.113 28.783 15.513 1.00 20.57 ? 407 SER A OG  1 
ATOM   2730 N N   . GLU A 1 378 ? 42.396 31.658 15.932 1.00 19.17 ? 408 GLU A N   1 
ATOM   2731 C CA  . GLU A 1 378 ? 43.668 32.331 15.703 1.00 18.01 ? 408 GLU A CA  1 
ATOM   2732 C C   . GLU A 1 378 ? 44.444 32.515 17.002 1.00 21.48 ? 408 GLU A C   1 
ATOM   2733 O O   . GLU A 1 378 ? 45.658 32.288 17.040 1.00 22.09 ? 408 GLU A O   1 
ATOM   2734 C CB  . GLU A 1 378 ? 43.432 33.676 15.019 1.00 21.18 ? 408 GLU A CB  1 
ATOM   2735 C CG  . GLU A 1 378 ? 42.921 33.550 13.599 1.00 25.23 ? 408 GLU A CG  1 
ATOM   2736 C CD  . GLU A 1 378 ? 43.878 32.755 12.702 1.00 38.02 ? 408 GLU A CD  1 
ATOM   2737 O OE1 . GLU A 1 378 ? 45.098 32.863 12.914 1.00 46.54 ? 408 GLU A OE1 1 
ATOM   2738 O OE2 . GLU A 1 378 ? 43.388 32.038 11.815 1.00 43.13 ? 408 GLU A OE2 1 
ATOM   2739 N N   . ALA A 1 379 ? 43.766 32.916 18.083 1.00 17.06 ? 409 ALA A N   1 
ATOM   2740 C CA  . ALA A 1 379 ? 44.479 33.133 19.340 1.00 23.17 ? 409 ALA A CA  1 
ATOM   2741 C C   . ALA A 1 379 ? 45.015 31.823 19.907 1.00 19.54 ? 409 ALA A C   1 
ATOM   2742 O O   . ALA A 1 379 ? 46.107 31.793 20.489 1.00 17.37 ? 409 ALA A O   1 
ATOM   2743 C CB  . ALA A 1 379 ? 43.569 33.829 20.351 1.00 17.55 ? 409 ALA A CB  1 
ATOM   2744 N N   . LEU A 1 380 ? 44.271 30.728 19.737 1.00 17.34 ? 410 LEU A N   1 
ATOM   2745 C CA  . LEU A 1 380 ? 44.743 29.433 20.216 1.00 20.36 ? 410 LEU A CA  1 
ATOM   2746 C C   . LEU A 1 380 ? 45.950 28.959 19.420 1.00 19.44 ? 410 LEU A C   1 
ATOM   2747 O O   . LEU A 1 380 ? 46.892 28.394 19.988 1.00 17.37 ? 410 LEU A O   1 
ATOM   2748 C CB  . LEU A 1 380 ? 43.610 28.404 20.158 1.00 16.49 ? 410 LEU A CB  1 
ATOM   2749 C CG  . LEU A 1 380 ? 42.517 28.557 21.222 1.00 20.08 ? 410 LEU A CG  1 
ATOM   2750 C CD1 . LEU A 1 380 ? 41.333 27.664 20.904 1.00 15.42 ? 410 LEU A CD1 1 
ATOM   2751 C CD2 . LEU A 1 380 ? 43.060 28.257 22.610 1.00 16.48 ? 410 LEU A CD2 1 
ATOM   2752 N N   . VAL A 1 381 ? 45.939 29.172 18.103 1.00 16.95 ? 411 VAL A N   1 
ATOM   2753 C CA  . VAL A 1 381 ? 47.141 28.905 17.318 1.00 16.31 ? 411 VAL A CA  1 
ATOM   2754 C C   . VAL A 1 381 ? 48.295 29.748 17.838 1.00 19.51 ? 411 VAL A C   1 
ATOM   2755 O O   . VAL A 1 381 ? 49.411 29.251 18.033 1.00 16.92 ? 411 VAL A O   1 
ATOM   2756 C CB  . VAL A 1 381 ? 46.882 29.162 15.822 1.00 22.13 ? 411 VAL A CB  1 
ATOM   2757 C CG1 . VAL A 1 381 ? 48.191 29.133 15.040 1.00 20.00 ? 411 VAL A CG1 1 
ATOM   2758 C CG2 . VAL A 1 381 ? 45.906 28.136 15.266 1.00 19.50 ? 411 VAL A CG2 1 
ATOM   2759 N N   . ARG A 1 382 ? 48.029 31.030 18.109 1.00 19.56 ? 412 ARG A N   1 
ATOM   2760 C CA  . ARG A 1 382 ? 49.075 31.955 18.532 1.00 23.45 ? 412 ARG A CA  1 
ATOM   2761 C C   . ARG A 1 382 ? 49.680 31.556 19.872 1.00 22.41 ? 412 ARG A C   1 
ATOM   2762 O O   . ARG A 1 382 ? 50.866 31.804 20.112 1.00 24.84 ? 412 ARG A O   1 
ATOM   2763 C CB  . ARG A 1 382 ? 48.503 33.374 18.604 1.00 21.20 ? 412 ARG A CB  1 
ATOM   2764 C CG  . ARG A 1 382 ? 49.466 34.480 18.222 1.00 33.57 ? 412 ARG A CG  1 
ATOM   2765 C CD  . ARG A 1 382 ? 48.722 35.743 17.781 1.00 37.20 ? 412 ARG A CD  1 
ATOM   2766 N NE  . ARG A 1 382 ? 47.968 36.361 18.866 1.00 47.15 ? 412 ARG A NE  1 
ATOM   2767 C CZ  . ARG A 1 382 ? 46.643 36.418 18.933 1.00 46.96 ? 412 ARG A CZ  1 
ATOM   2768 N NH1 . ARG A 1 382 ? 45.877 35.928 17.971 1.00 30.73 ? 412 ARG A NH1 1 
ATOM   2769 N NH2 . ARG A 1 382 ? 46.072 36.986 19.992 1.00 45.94 ? 412 ARG A NH2 1 
ATOM   2770 N N   . GLN A 1 383 ? 48.896 30.935 20.750 1.00 21.47 ? 413 GLN A N   1 
ATOM   2771 C CA  . GLN A 1 383 ? 49.371 30.559 22.076 1.00 24.54 ? 413 GLN A CA  1 
ATOM   2772 C C   . GLN A 1 383 ? 49.992 29.164 22.117 1.00 25.45 ? 413 GLN A C   1 
ATOM   2773 O O   . GLN A 1 383 ? 50.329 28.683 23.204 1.00 23.91 ? 413 GLN A O   1 
ATOM   2774 C CB  . GLN A 1 383 ? 48.232 30.656 23.095 1.00 17.54 ? 413 GLN A CB  1 
ATOM   2775 C CG  . GLN A 1 383 ? 47.813 32.087 23.416 1.00 19.47 ? 413 GLN A CG  1 
ATOM   2776 C CD  . GLN A 1 383 ? 48.962 32.926 23.957 1.00 26.04 ? 413 GLN A CD  1 
ATOM   2777 O OE1 . GLN A 1 383 ? 49.628 32.540 24.918 1.00 27.22 ? 413 GLN A OE1 1 
ATOM   2778 N NE2 . GLN A 1 383 ? 49.201 34.077 23.335 1.00 22.36 ? 413 GLN A NE2 1 
ATOM   2779 N N   . GLY A 1 384 ? 50.159 28.513 20.968 1.00 17.01 ? 414 GLY A N   1 
ATOM   2780 C CA  . GLY A 1 384 ? 50.768 27.199 20.940 1.00 19.79 ? 414 GLY A CA  1 
ATOM   2781 C C   . GLY A 1 384 ? 49.859 26.066 21.355 1.00 19.50 ? 414 GLY A C   1 
ATOM   2782 O O   . GLY A 1 384 ? 50.346 24.980 21.684 1.00 22.26 ? 414 GLY A O   1 
ATOM   2783 N N   . ALA A 1 385 ? 48.555 26.282 21.353 1.00 18.65 ? 415 ALA A N   1 
ATOM   2784 C CA  . ALA A 1 385 ? 47.634 25.230 21.744 1.00 21.41 ? 415 ALA A CA  1 
ATOM   2785 C C   . ALA A 1 385 ? 47.478 24.201 20.629 1.00 15.26 ? 415 ALA A C   1 
ATOM   2786 O O   . ALA A 1 385 ? 47.593 24.532 19.447 1.00 14.99 ? 415 ALA A O   1 
ATOM   2787 C CB  . ALA A 1 385 ? 46.268 25.814 22.083 1.00 17.09 ? 415 ALA A CB  1 
ATOM   2788 N N   . PRO A 1 386 ? 47.241 22.943 20.984 1.00 16.75 ? 416 PRO A N   1 
ATOM   2789 C CA  . PRO A 1 386 ? 46.751 21.976 19.995 1.00 16.40 ? 416 PRO A CA  1 
ATOM   2790 C C   . PRO A 1 386 ? 45.294 22.263 19.669 1.00 20.75 ? 416 PRO A C   1 
ATOM   2791 O O   . PRO A 1 386 ? 44.418 22.040 20.511 1.00 14.71 ? 416 PRO A O   1 
ATOM   2792 C CB  . PRO A 1 386 ? 46.919 20.621 20.702 1.00 18.34 ? 416 PRO A CB  1 
ATOM   2793 C CG  . PRO A 1 386 ? 47.712 20.913 21.973 1.00 19.20 ? 416 PRO A CG  1 
ATOM   2794 C CD  . PRO A 1 386 ? 47.423 22.335 22.311 1.00 14.32 ? 416 PRO A CD  1 
ATOM   2795 N N   . VAL A 1 387 ? 45.010 22.769 18.472 1.00 17.71 ? 417 VAL A N   1 
ATOM   2796 C CA  . VAL A 1 387 ? 43.676 23.252 18.142 1.00 18.10 ? 417 VAL A CA  1 
ATOM   2797 C C   . VAL A 1 387 ? 43.257 22.711 16.779 1.00 18.64 ? 417 VAL A C   1 
ATOM   2798 O O   . VAL A 1 387 ? 44.025 22.774 15.812 1.00 19.81 ? 417 VAL A O   1 
ATOM   2799 C CB  . VAL A 1 387 ? 43.611 24.793 18.174 1.00 18.53 ? 417 VAL A CB  1 
ATOM   2800 C CG1 . VAL A 1 387 ? 44.730 25.401 17.336 1.00 20.31 ? 417 VAL A CG1 1 
ATOM   2801 C CG2 . VAL A 1 387 ? 42.247 25.284 17.713 1.00 16.49 ? 417 VAL A CG2 1 
ATOM   2802 N N   . TRP A 1 388 ? 42.043 22.168 16.715 1.00 20.19 ? 418 TRP A N   1 
ATOM   2803 C CA  . TRP A 1 388 ? 41.415 21.702 15.487 1.00 19.33 ? 418 TRP A CA  1 
ATOM   2804 C C   . TRP A 1 388 ? 40.102 22.448 15.277 1.00 18.91 ? 418 TRP A C   1 
ATOM   2805 O O   . TRP A 1 388 ? 39.436 22.848 16.239 1.00 18.66 ? 418 TRP A O   1 
ATOM   2806 C CB  . TRP A 1 388 ? 41.157 20.188 15.529 1.00 15.65 ? 418 TRP A CB  1 
ATOM   2807 C CG  . TRP A 1 388 ? 42.403 19.354 15.504 1.00 20.37 ? 418 TRP A CG  1 
ATOM   2808 C CD1 . TRP A 1 388 ? 42.949 18.730 14.419 1.00 16.41 ? 418 TRP A CD1 1 
ATOM   2809 C CD2 . TRP A 1 388 ? 43.256 19.047 16.615 1.00 19.81 ? 418 TRP A CD2 1 
ATOM   2810 N NE1 . TRP A 1 388 ? 44.089 18.055 14.786 1.00 17.92 ? 418 TRP A NE1 1 
ATOM   2811 C CE2 . TRP A 1 388 ? 44.299 18.232 16.129 1.00 16.90 ? 418 TRP A CE2 1 
ATOM   2812 C CE3 . TRP A 1 388 ? 43.237 19.378 17.973 1.00 18.88 ? 418 TRP A CE3 1 
ATOM   2813 C CZ2 . TRP A 1 388 ? 45.315 17.746 16.952 1.00 17.68 ? 418 TRP A CZ2 1 
ATOM   2814 C CZ3 . TRP A 1 388 ? 44.251 18.895 18.790 1.00 22.47 ? 418 TRP A CZ3 1 
ATOM   2815 C CH2 . TRP A 1 388 ? 45.275 18.087 18.275 1.00 17.56 ? 418 TRP A CH2 1 
ATOM   2816 N N   . ARG A 1 389 ? 39.731 22.631 14.012 1.00 16.16 ? 419 ARG A N   1 
ATOM   2817 C CA  . ARG A 1 389 ? 38.529 23.372 13.660 1.00 20.47 ? 419 ARG A CA  1 
ATOM   2818 C C   . ARG A 1 389 ? 37.688 22.585 12.664 1.00 19.23 ? 419 ARG A C   1 
ATOM   2819 O O   . ARG A 1 389 ? 38.211 21.851 11.818 1.00 19.73 ? 419 ARG A O   1 
ATOM   2820 C CB  . ARG A 1 389 ? 38.876 24.749 13.076 1.00 22.59 ? 419 ARG A CB  1 
ATOM   2821 C CG  . ARG A 1 389 ? 37.681 25.660 12.821 1.00 18.31 ? 419 ARG A CG  1 
ATOM   2822 C CD  . ARG A 1 389 ? 38.147 27.040 12.401 1.00 22.03 ? 419 ARG A CD  1 
ATOM   2823 N NE  . ARG A 1 389 ? 37.036 27.929 12.087 1.00 28.90 ? 419 ARG A NE  1 
ATOM   2824 C CZ  . ARG A 1 389 ? 37.175 29.205 11.754 1.00 24.42 ? 419 ARG A CZ  1 
ATOM   2825 N NH1 . ARG A 1 389 ? 38.366 29.778 11.696 1.00 18.70 ? 419 ARG A NH1 1 
ATOM   2826 N NH2 . ARG A 1 389 ? 36.091 29.923 11.474 1.00 24.20 ? 419 ARG A NH2 1 
ATOM   2827 N N   . TYR A 1 390 ? 36.371 22.754 12.777 1.00 20.32 ? 420 TYR A N   1 
ATOM   2828 C CA  . TYR A 1 390 ? 35.427 22.095 11.885 1.00 18.89 ? 420 TYR A CA  1 
ATOM   2829 C C   . TYR A 1 390 ? 34.319 23.051 11.454 1.00 18.77 ? 420 TYR A C   1 
ATOM   2830 O O   . TYR A 1 390 ? 33.986 24.032 12.136 1.00 19.56 ? 420 TYR A O   1 
ATOM   2831 C CB  . TYR A 1 390 ? 34.793 20.848 12.532 1.00 15.89 ? 420 TYR A CB  1 
ATOM   2832 C CG  . TYR A 1 390 ? 33.748 21.171 13.587 1.00 20.21 ? 420 TYR A CG  1 
ATOM   2833 C CD1 . TYR A 1 390 ? 32.413 21.369 13.239 1.00 14.95 ? 420 TYR A CD1 1 
ATOM   2834 C CD2 . TYR A 1 390 ? 34.097 21.279 14.930 1.00 16.95 ? 420 TYR A CD2 1 
ATOM   2835 C CE1 . TYR A 1 390 ? 31.470 21.673 14.181 1.00 16.47 ? 420 TYR A CE1 1 
ATOM   2836 C CE2 . TYR A 1 390 ? 33.147 21.578 15.891 1.00 16.41 ? 420 TYR A CE2 1 
ATOM   2837 C CZ  . TYR A 1 390 ? 31.834 21.778 15.505 1.00 15.71 ? 420 TYR A CZ  1 
ATOM   2838 O OH  . TYR A 1 390 ? 30.869 22.083 16.435 1.00 15.11 ? 420 TYR A OH  1 
ATOM   2839 N N   . GLN A 1 391 ? 33.731 22.719 10.308 1.00 18.51 ? 421 GLN A N   1 
ATOM   2840 C CA  . GLN A 1 391 ? 32.456 23.270 9.881  1.00 19.87 ? 421 GLN A CA  1 
ATOM   2841 C C   . GLN A 1 391 ? 31.532 22.119 9.504  1.00 21.58 ? 421 GLN A C   1 
ATOM   2842 O O   . GLN A 1 391 ? 31.886 21.268 8.678  1.00 18.79 ? 421 GLN A O   1 
ATOM   2843 C CB  . GLN A 1 391 ? 32.619 24.241 8.708  1.00 19.66 ? 421 GLN A CB  1 
ATOM   2844 C CG  . GLN A 1 391 ? 31.423 25.144 8.528  1.00 24.93 ? 421 GLN A CG  1 
ATOM   2845 C CD  . GLN A 1 391 ? 31.698 26.279 7.576  1.00 36.14 ? 421 GLN A CD  1 
ATOM   2846 O OE1 . GLN A 1 391 ? 32.077 27.376 7.991  1.00 43.75 ? 421 GLN A OE1 1 
ATOM   2847 N NE2 . GLN A 1 391 ? 31.517 26.024 6.286  1.00 35.67 ? 421 GLN A NE2 1 
ATOM   2848 N N   . PHE A 1 392 ? 30.356 22.100 10.115 1.00 18.56 ? 422 PHE A N   1 
ATOM   2849 C CA  . PHE A 1 392 ? 29.354 21.064 9.899  1.00 16.65 ? 422 PHE A CA  1 
ATOM   2850 C C   . PHE A 1 392 ? 28.333 21.612 8.905  1.00 18.04 ? 422 PHE A C   1 
ATOM   2851 O O   . PHE A 1 392 ? 27.470 22.418 9.267  1.00 17.41 ? 422 PHE A O   1 
ATOM   2852 C CB  . PHE A 1 392 ? 28.714 20.670 11.228 1.00 16.15 ? 422 PHE A CB  1 
ATOM   2853 C CG  . PHE A 1 392 ? 27.621 19.645 11.104 1.00 19.18 ? 422 PHE A CG  1 
ATOM   2854 C CD1 . PHE A 1 392 ? 27.918 18.295 11.072 1.00 18.92 ? 422 PHE A CD1 1 
ATOM   2855 C CD2 . PHE A 1 392 ? 26.294 20.032 11.027 1.00 17.04 ? 422 PHE A CD2 1 
ATOM   2856 C CE1 . PHE A 1 392 ? 26.911 17.349 10.958 1.00 19.16 ? 422 PHE A CE1 1 
ATOM   2857 C CE2 . PHE A 1 392 ? 25.285 19.091 10.913 1.00 17.44 ? 422 PHE A CE2 1 
ATOM   2858 C CZ  . PHE A 1 392 ? 25.596 17.750 10.879 1.00 18.01 ? 422 PHE A CZ  1 
ATOM   2859 N N   . ASN A 1 393 ? 28.446 21.185 7.642  1.00 17.95 ? 423 ASN A N   1 
ATOM   2860 C CA  . ASN A 1 393 ? 27.469 21.566 6.628  1.00 19.39 ? 423 ASN A CA  1 
ATOM   2861 C C   . ASN A 1 393 ? 26.251 20.651 6.639  1.00 18.92 ? 423 ASN A C   1 
ATOM   2862 O O   . ASN A 1 393 ? 25.156 21.080 6.263  1.00 20.09 ? 423 ASN A O   1 
ATOM   2863 C CB  . ASN A 1 393 ? 28.113 21.551 5.239  1.00 19.44 ? 423 ASN A CB  1 
ATOM   2864 C CG  . ASN A 1 393 ? 29.188 22.603 5.084  1.00 27.08 ? 423 ASN A CG  1 
ATOM   2865 O OD1 . ASN A 1 393 ? 29.263 23.558 5.866  1.00 26.75 ? 423 ASN A OD1 1 
ATOM   2866 N ND2 . ASN A 1 393 ? 30.024 22.444 4.064  1.00 25.22 ? 423 ASN A ND2 1 
ATOM   2867 N N   . GLY A 1 394 ? 26.419 19.399 7.053  1.00 19.18 ? 424 GLY A N   1 
ATOM   2868 C CA  . GLY A 1 394 ? 25.329 18.448 7.051  1.00 19.93 ? 424 GLY A CA  1 
ATOM   2869 C C   . GLY A 1 394 ? 25.179 17.756 5.712  1.00 23.80 ? 424 GLY A C   1 
ATOM   2870 O O   . GLY A 1 394 ? 25.909 18.005 4.753  1.00 24.38 ? 424 GLY A O   1 
ATOM   2871 N N   . ASN A 1 395 ? 24.194 16.865 5.653  1.00 24.73 ? 425 ASN A N   1 
ATOM   2872 C CA  . ASN A 1 395 ? 23.925 16.087 4.448  1.00 25.35 ? 425 ASN A CA  1 
ATOM   2873 C C   . ASN A 1 395 ? 22.863 16.807 3.631  1.00 28.62 ? 425 ASN A C   1 
ATOM   2874 O O   . ASN A 1 395 ? 21.664 16.678 3.884  1.00 27.10 ? 425 ASN A O   1 
ATOM   2875 C CB  . ASN A 1 395 ? 23.500 14.674 4.810  1.00 26.40 ? 425 ASN A CB  1 
ATOM   2876 C CG  . ASN A 1 395 ? 24.647 13.853 5.337  1.00 28.76 ? 425 ASN A CG  1 
ATOM   2877 O OD1 . ASN A 1 395 ? 25.791 14.014 4.906  1.00 25.16 ? 425 ASN A OD1 1 
ATOM   2878 N ND2 . ASN A 1 395 ? 24.356 12.978 6.291  1.00 25.10 ? 425 ASN A ND2 1 
ATOM   2879 N N   . THR A 1 396 ? 23.310 17.565 2.638  1.00 26.13 ? 426 THR A N   1 
ATOM   2880 C CA  . THR A 1 396 ? 22.433 18.376 1.809  1.00 34.58 ? 426 THR A CA  1 
ATOM   2881 C C   . THR A 1 396 ? 22.044 17.691 0.503  1.00 34.21 ? 426 THR A C   1 
ATOM   2882 O O   . THR A 1 396 ? 21.408 18.325 -0.345 1.00 38.27 ? 426 THR A O   1 
ATOM   2883 C CB  . THR A 1 396 ? 23.105 19.718 1.514  1.00 32.08 ? 426 THR A CB  1 
ATOM   2884 O OG1 . THR A 1 396 ? 24.417 19.492 0.979  1.00 28.19 ? 426 THR A OG1 1 
ATOM   2885 C CG2 . THR A 1 396 ? 23.221 20.538 2.780  1.00 27.07 ? 426 THR A CG2 1 
ATOM   2886 N N   . GLU A 1 397 ? 22.375 16.405 0.336  1.00 34.29 ? 427 GLU A N   1 
ATOM   2887 C CA  . GLU A 1 397 ? 22.239 15.772 -0.974 1.00 35.95 ? 427 GLU A CA  1 
ATOM   2888 C C   . GLU A 1 397 ? 20.786 15.666 -1.416 1.00 39.56 ? 427 GLU A C   1 
ATOM   2889 O O   . GLU A 1 397 ? 20.500 15.735 -2.617 1.00 58.38 ? 427 GLU A O   1 
ATOM   2890 C CB  . GLU A 1 397 ? 22.891 14.389 -0.967 1.00 34.34 ? 427 GLU A CB  1 
ATOM   2891 C CG  . GLU A 1 397 ? 22.461 13.493 0.177  1.00 37.74 ? 427 GLU A CG  1 
ATOM   2892 C CD  . GLU A 1 397 ? 23.397 13.587 1.363  1.00 32.00 ? 427 GLU A CD  1 
ATOM   2893 O OE1 . GLU A 1 397 ? 24.058 14.636 1.524  1.00 29.44 ? 427 GLU A OE1 1 
ATOM   2894 O OE2 . GLU A 1 397 ? 23.483 12.604 2.128  1.00 35.94 ? 427 GLU A OE2 1 
ATOM   2895 N N   . GLY A 1 398 ? 19.856 15.496 -0.481 1.00 38.32 ? 428 GLY A N   1 
ATOM   2896 C CA  . GLY A 1 398 ? 18.467 15.312 -0.865 1.00 43.70 ? 428 GLY A CA  1 
ATOM   2897 C C   . GLY A 1 398 ? 17.690 16.608 -0.975 1.00 39.26 ? 428 GLY A C   1 
ATOM   2898 O O   . GLY A 1 398 ? 16.454 16.600 -0.946 1.00 38.88 ? 428 GLY A O   1 
ATOM   2899 N N   . GLY A 1 399 ? 18.403 17.724 -1.111 1.00 39.72 ? 429 GLY A N   1 
ATOM   2900 C CA  . GLY A 1 399 ? 17.784 19.026 -1.054 1.00 34.32 ? 429 GLY A CA  1 
ATOM   2901 C C   . GLY A 1 399 ? 17.591 19.579 0.341  1.00 40.48 ? 429 GLY A C   1 
ATOM   2902 O O   . GLY A 1 399 ? 16.831 20.540 0.509  1.00 39.45 ? 429 GLY A O   1 
ATOM   2903 N N   . ARG A 1 400 ? 18.242 19.000 1.346  1.00 34.48 ? 430 ARG A N   1 
ATOM   2904 C CA  . ARG A 1 400 ? 18.124 19.494 2.709  1.00 26.78 ? 430 ARG A CA  1 
ATOM   2905 C C   . ARG A 1 400 ? 18.877 20.811 2.859  1.00 26.40 ? 430 ARG A C   1 
ATOM   2906 O O   . ARG A 1 400 ? 19.952 21.000 2.283  1.00 29.31 ? 430 ARG A O   1 
ATOM   2907 C CB  . ARG A 1 400 ? 18.669 18.450 3.692  1.00 26.97 ? 430 ARG A CB  1 
ATOM   2908 C CG  . ARG A 1 400 ? 18.524 18.815 5.166  1.00 28.72 ? 430 ARG A CG  1 
ATOM   2909 C CD  . ARG A 1 400 ? 19.211 17.782 6.053  1.00 29.92 ? 430 ARG A CD  1 
ATOM   2910 N NE  . ARG A 1 400 ? 18.645 16.445 5.899  1.00 25.76 ? 430 ARG A NE  1 
ATOM   2911 C CZ  . ARG A 1 400 ? 19.204 15.337 6.367  1.00 32.36 ? 430 ARG A CZ  1 
ATOM   2912 N NH1 . ARG A 1 400 ? 20.355 15.365 7.020  1.00 26.94 ? 430 ARG A NH1 1 
ATOM   2913 N NH2 . ARG A 1 400 ? 18.596 14.170 6.172  1.00 22.69 ? 430 ARG A NH2 1 
ATOM   2914 N N   . ALA A 1 401 ? 18.306 21.725 3.638  1.00 27.29 ? 431 ALA A N   1 
ATOM   2915 C CA  . ALA A 1 401 ? 18.954 23.004 3.870  1.00 25.27 ? 431 ALA A CA  1 
ATOM   2916 C C   . ALA A 1 401 ? 20.291 22.797 4.582  1.00 24.85 ? 431 ALA A C   1 
ATOM   2917 O O   . ALA A 1 401 ? 20.464 21.826 5.325  1.00 24.43 ? 431 ALA A O   1 
ATOM   2918 C CB  . ALA A 1 401 ? 18.061 23.920 4.704  1.00 25.94 ? 431 ALA A CB  1 
ATOM   2919 N N   . PRO A 1 402 ? 21.262 23.680 4.352  1.00 25.02 ? 432 PRO A N   1 
ATOM   2920 C CA  . PRO A 1 402 ? 22.507 23.616 5.121  1.00 21.21 ? 432 PRO A CA  1 
ATOM   2921 C C   . PRO A 1 402 ? 22.227 23.651 6.617  1.00 24.04 ? 432 PRO A C   1 
ATOM   2922 O O   . PRO A 1 402 ? 21.257 24.260 7.075  1.00 20.62 ? 432 PRO A O   1 
ATOM   2923 C CB  . PRO A 1 402 ? 23.273 24.859 4.659  1.00 21.50 ? 432 PRO A CB  1 
ATOM   2924 C CG  . PRO A 1 402 ? 22.773 25.094 3.275  1.00 22.64 ? 432 PRO A CG  1 
ATOM   2925 C CD  . PRO A 1 402 ? 21.316 24.715 3.303  1.00 24.80 ? 432 PRO A CD  1 
ATOM   2926 N N   . ALA A 1 403 ? 23.083 22.970 7.373  1.00 19.62 ? 433 ALA A N   1 
ATOM   2927 C CA  . ALA A 1 403 ? 22.873 22.823 8.807  1.00 20.59 ? 433 ALA A CA  1 
ATOM   2928 C C   . ALA A 1 403 ? 22.848 24.178 9.497  1.00 20.70 ? 433 ALA A C   1 
ATOM   2929 O O   . ALA A 1 403 ? 23.701 25.034 9.243  1.00 20.97 ? 433 ALA A O   1 
ATOM   2930 C CB  . ALA A 1 403 ? 23.971 21.951 9.407  1.00 18.19 ? 433 ALA A CB  1 
ATOM   2931 N N   . THR A 1 404 ? 21.858 24.379 10.361 1.00 22.07 ? 434 THR A N   1 
ATOM   2932 C CA  . THR A 1 404 ? 21.788 25.586 11.163 1.00 19.87 ? 434 THR A CA  1 
ATOM   2933 C C   . THR A 1 404 ? 22.156 25.263 12.612 1.00 17.92 ? 434 THR A C   1 
ATOM   2934 O O   . THR A 1 404 ? 22.692 24.189 12.919 1.00 17.67 ? 434 THR A O   1 
ATOM   2935 C CB  . THR A 1 404 ? 20.402 26.237 11.050 1.00 24.80 ? 434 THR A CB  1 
ATOM   2936 O OG1 . THR A 1 404 ? 20.414 27.493 11.744 1.00 22.73 ? 434 THR A OG1 1 
ATOM   2937 C CG2 . THR A 1 404 ? 19.323 25.337 11.646 1.00 22.84 ? 434 THR A CG2 1 
ATOM   2938 N N   . HIS A 1 405 ? 21.867 26.210 13.503 1.00 17.91 ? 435 HIS A N   1 
ATOM   2939 C CA  . HIS A 1 405 ? 22.283 26.115 14.896 1.00 17.29 ? 435 HIS A CA  1 
ATOM   2940 C C   . HIS A 1 405 ? 21.677 24.888 15.567 1.00 18.63 ? 435 HIS A C   1 
ATOM   2941 O O   . HIS A 1 405 ? 20.463 24.667 15.506 1.00 17.54 ? 435 HIS A O   1 
ATOM   2942 C CB  . HIS A 1 405 ? 21.867 27.386 15.634 1.00 17.54 ? 435 HIS A CB  1 
ATOM   2943 C CG  . HIS A 1 405 ? 22.589 27.606 16.925 1.00 17.00 ? 435 HIS A CG  1 
ATOM   2944 N ND1 . HIS A 1 405 ? 23.961 27.714 16.998 1.00 19.17 ? 435 HIS A ND1 1 
ATOM   2945 C CD2 . HIS A 1 405 ? 22.129 27.765 18.189 1.00 16.94 ? 435 HIS A CD2 1 
ATOM   2946 C CE1 . HIS A 1 405 ? 24.316 27.918 18.254 1.00 16.93 ? 435 HIS A CE1 1 
ATOM   2947 N NE2 . HIS A 1 405 ? 23.224 27.957 18.996 1.00 16.45 ? 435 HIS A NE2 1 
ATOM   2948 N N   . GLY A 1 406 ? 22.535 24.091 16.208 1.00 18.22 ? 436 GLY A N   1 
ATOM   2949 C CA  . GLY A 1 406 ? 22.120 22.912 16.936 1.00 16.32 ? 436 GLY A CA  1 
ATOM   2950 C C   . GLY A 1 406 ? 22.094 21.627 16.131 1.00 20.23 ? 436 GLY A C   1 
ATOM   2951 O O   . GLY A 1 406 ? 21.986 20.550 16.725 1.00 18.83 ? 436 GLY A O   1 
ATOM   2952 N N   . ALA A 1 407 ? 22.226 21.700 14.804 1.00 16.71 ? 437 ALA A N   1 
ATOM   2953 C CA  . ALA A 1 407 ? 21.952 20.535 13.964 1.00 17.48 ? 437 ALA A CA  1 
ATOM   2954 C C   . ALA A 1 407 ? 22.927 19.393 14.222 1.00 20.36 ? 437 ALA A C   1 
ATOM   2955 O O   . ALA A 1 407 ? 22.604 18.229 13.953 1.00 20.08 ? 437 ALA A O   1 
ATOM   2956 C CB  . ALA A 1 407 ? 21.987 20.931 12.487 1.00 17.49 ? 437 ALA A CB  1 
ATOM   2957 N N   . GLU A 1 408 ? 24.124 19.696 14.718 1.00 18.55 ? 438 GLU A N   1 
ATOM   2958 C CA  . GLU A 1 408 ? 25.160 18.674 14.823 1.00 18.37 ? 438 GLU A CA  1 
ATOM   2959 C C   . GLU A 1 408 ? 25.067 17.828 16.090 1.00 17.54 ? 438 GLU A C   1 
ATOM   2960 O O   . GLU A 1 408 ? 25.764 16.806 16.183 1.00 18.02 ? 438 GLU A O   1 
ATOM   2961 C CB  . GLU A 1 408 ? 26.546 19.329 14.745 1.00 16.41 ? 438 GLU A CB  1 
ATOM   2962 C CG  . GLU A 1 408 ? 27.123 19.722 16.093 1.00 17.33 ? 438 GLU A CG  1 
ATOM   2963 C CD  . GLU A 1 408 ? 26.418 20.904 16.730 1.00 16.91 ? 438 GLU A CD  1 
ATOM   2964 O OE1 . GLU A 1 408 ? 25.555 21.531 16.078 1.00 15.30 ? 438 GLU A OE1 1 
ATOM   2965 O OE2 . GLU A 1 408 ? 26.739 21.209 17.894 1.00 19.08 ? 438 GLU A OE2 1 
ATOM   2966 N N   . ILE A 1 409 ? 24.222 18.217 17.050 1.00 20.60 ? 439 ILE A N   1 
ATOM   2967 C CA  . ILE A 1 409 ? 24.168 17.499 18.325 1.00 19.14 ? 439 ILE A CA  1 
ATOM   2968 C C   . ILE A 1 409 ? 23.870 16.009 18.169 1.00 21.19 ? 439 ILE A C   1 
ATOM   2969 O O   . ILE A 1 409 ? 24.552 15.193 18.798 1.00 16.77 ? 439 ILE A O   1 
ATOM   2970 C CB  . ILE A 1 409 ? 23.168 18.197 19.281 1.00 25.98 ? 439 ILE A CB  1 
ATOM   2971 C CG1 . ILE A 1 409 ? 23.683 19.572 19.701 1.00 25.68 ? 439 ILE A CG1 1 
ATOM   2972 C CG2 . ILE A 1 409 ? 22.914 17.336 20.510 1.00 26.03 ? 439 ILE A CG2 1 
ATOM   2973 C CD1 . ILE A 1 409 ? 22.659 20.383 20.448 1.00 25.96 ? 439 ILE A CD1 1 
ATOM   2974 N N   . PRO A 1 410 ? 22.869 15.593 17.370 1.00 21.00 ? 440 PRO A N   1 
ATOM   2975 C CA  . PRO A 1 410 ? 22.639 14.143 17.228 1.00 20.17 ? 440 PRO A CA  1 
ATOM   2976 C C   . PRO A 1 410 ? 23.784 13.413 16.548 1.00 20.67 ? 440 PRO A C   1 
ATOM   2977 O O   . PRO A 1 410 ? 23.976 12.215 16.793 1.00 19.77 ? 440 PRO A O   1 
ATOM   2978 C CB  . PRO A 1 410 ? 21.352 14.070 16.393 1.00 26.31 ? 440 PRO A CB  1 
ATOM   2979 C CG  . PRO A 1 410 ? 20.692 15.388 16.583 1.00 23.73 ? 440 PRO A CG  1 
ATOM   2980 C CD  . PRO A 1 410 ? 21.820 16.368 16.687 1.00 24.45 ? 440 PRO A CD  1 
ATOM   2981 N N   . TYR A 1 411 ? 24.556 14.099 15.704 1.00 19.24 ? 441 TYR A N   1 
ATOM   2982 C CA  . TYR A 1 411 ? 25.694 13.468 15.053 1.00 19.45 ? 441 TYR A CA  1 
ATOM   2983 C C   . TYR A 1 411 ? 26.857 13.276 16.014 1.00 19.98 ? 441 TYR A C   1 
ATOM   2984 O O   . TYR A 1 411 ? 27.743 12.459 15.742 1.00 23.84 ? 441 TYR A O   1 
ATOM   2985 C CB  . TYR A 1 411 ? 26.114 14.297 13.838 1.00 17.98 ? 441 TYR A CB  1 
ATOM   2986 C CG  . TYR A 1 411 ? 25.025 14.387 12.785 1.00 21.82 ? 441 TYR A CG  1 
ATOM   2987 C CD1 . TYR A 1 411 ? 23.977 15.294 12.915 1.00 18.41 ? 441 TYR A CD1 1 
ATOM   2988 C CD2 . TYR A 1 411 ? 25.035 13.555 11.673 1.00 17.39 ? 441 TYR A CD2 1 
ATOM   2989 C CE1 . TYR A 1 411 ? 22.973 15.372 11.965 1.00 18.80 ? 441 TYR A CE1 1 
ATOM   2990 C CE2 . TYR A 1 411 ? 24.037 13.626 10.718 1.00 20.63 ? 441 TYR A CE2 1 
ATOM   2991 C CZ  . TYR A 1 411 ? 23.009 14.536 10.867 1.00 22.13 ? 441 TYR A CZ  1 
ATOM   2992 O OH  . TYR A 1 411 ? 22.017 14.607 9.911  1.00 19.46 ? 441 TYR A OH  1 
ATOM   2993 N N   . VAL A 1 412 ? 26.862 14.002 17.127 1.00 19.01 ? 442 VAL A N   1 
ATOM   2994 C CA  . VAL A 1 412 ? 27.866 13.818 18.169 1.00 19.03 ? 442 VAL A CA  1 
ATOM   2995 C C   . VAL A 1 412 ? 27.409 12.796 19.203 1.00 17.41 ? 442 VAL A C   1 
ATOM   2996 O O   . VAL A 1 412 ? 28.140 11.857 19.526 1.00 18.43 ? 442 VAL A O   1 
ATOM   2997 C CB  . VAL A 1 412 ? 28.194 15.182 18.815 1.00 19.10 ? 442 VAL A CB  1 
ATOM   2998 C CG1 . VAL A 1 412 ? 28.972 15.006 20.111 1.00 15.30 ? 442 VAL A CG1 1 
ATOM   2999 C CG2 . VAL A 1 412 ? 28.971 16.054 17.836 1.00 16.21 ? 442 VAL A CG2 1 
ATOM   3000 N N   . PHE A 1 413 ? 26.184 12.947 19.717 1.00 15.39 ? 443 PHE A N   1 
ATOM   3001 C CA  . PHE A 1 413 ? 25.712 12.069 20.787 1.00 20.16 ? 443 PHE A CA  1 
ATOM   3002 C C   . PHE A 1 413 ? 25.249 10.708 20.275 1.00 23.21 ? 443 PHE A C   1 
ATOM   3003 O O   . PHE A 1 413 ? 25.299 9.723  21.021 1.00 22.64 ? 443 PHE A O   1 
ATOM   3004 C CB  . PHE A 1 413 ? 24.576 12.739 21.564 1.00 17.03 ? 443 PHE A CB  1 
ATOM   3005 C CG  . PHE A 1 413 ? 25.042 13.635 22.681 1.00 18.62 ? 443 PHE A CG  1 
ATOM   3006 C CD1 . PHE A 1 413 ? 25.468 14.929 22.422 1.00 17.27 ? 443 PHE A CD1 1 
ATOM   3007 C CD2 . PHE A 1 413 ? 25.042 13.186 23.993 1.00 20.56 ? 443 PHE A CD2 1 
ATOM   3008 C CE1 . PHE A 1 413 ? 25.890 15.757 23.452 1.00 15.86 ? 443 PHE A CE1 1 
ATOM   3009 C CE2 . PHE A 1 413 ? 25.467 14.011 25.027 1.00 20.13 ? 443 PHE A CE2 1 
ATOM   3010 C CZ  . PHE A 1 413 ? 25.890 15.298 24.752 1.00 16.34 ? 443 PHE A CZ  1 
ATOM   3011 N N   . GLY A 1 414 ? 24.787 10.627 19.029 1.00 21.99 ? 444 GLY A N   1 
ATOM   3012 C CA  . GLY A 1 414 ? 24.328 9.371  18.467 1.00 24.54 ? 444 GLY A CA  1 
ATOM   3013 C C   . GLY A 1 414 ? 22.872 9.035  18.708 1.00 22.73 ? 444 GLY A C   1 
ATOM   3014 O O   . GLY A 1 414 ? 22.452 7.914  18.394 1.00 23.35 ? 444 GLY A O   1 
ATOM   3015 N N   . VAL A 1 415 ? 22.092 9.958  19.254 1.00 24.10 ? 445 VAL A N   1 
ATOM   3016 C CA  . VAL A 1 415 ? 20.678 9.740  19.532 1.00 25.37 ? 445 VAL A CA  1 
ATOM   3017 C C   . VAL A 1 415 ? 19.894 10.566 18.519 1.00 24.38 ? 445 VAL A C   1 
ATOM   3018 O O   . VAL A 1 415 ? 19.767 11.789 18.654 1.00 26.46 ? 445 VAL A O   1 
ATOM   3019 C CB  . VAL A 1 415 ? 20.316 10.107 20.976 1.00 21.86 ? 445 VAL A CB  1 
ATOM   3020 C CG1 . VAL A 1 415 ? 18.834 9.873  21.237 1.00 25.03 ? 445 VAL A CG1 1 
ATOM   3021 C CG2 . VAL A 1 415 ? 21.164 9.304  21.950 1.00 19.57 ? 445 VAL A CG2 1 
ATOM   3022 N N   . PHE A 1 416 ? 19.374 9.901  17.486 1.00 24.75 ? 446 PHE A N   1 
ATOM   3023 C CA  . PHE A 1 416 ? 18.631 10.578 16.423 1.00 23.98 ? 446 PHE A CA  1 
ATOM   3024 C C   . PHE A 1 416 ? 17.158 10.635 16.816 1.00 27.18 ? 446 PHE A C   1 
ATOM   3025 O O   . PHE A 1 416 ? 16.312 9.877  16.335 1.00 28.96 ? 446 PHE A O   1 
ATOM   3026 C CB  . PHE A 1 416 ? 18.847 9.879  15.088 1.00 26.99 ? 446 PHE A CB  1 
ATOM   3027 C CG  . PHE A 1 416 ? 20.217 10.099 14.508 1.00 28.74 ? 446 PHE A CG  1 
ATOM   3028 C CD1 . PHE A 1 416 ? 20.466 11.185 13.685 1.00 22.31 ? 446 PHE A CD1 1 
ATOM   3029 C CD2 . PHE A 1 416 ? 21.258 9.226  14.797 1.00 27.13 ? 446 PHE A CD2 1 
ATOM   3030 C CE1 . PHE A 1 416 ? 21.727 11.394 13.151 1.00 26.20 ? 446 PHE A CE1 1 
ATOM   3031 C CE2 . PHE A 1 416 ? 22.520 9.428  14.268 1.00 24.01 ? 446 PHE A CE2 1 
ATOM   3032 C CZ  . PHE A 1 416 ? 22.755 10.513 13.444 1.00 26.91 ? 446 PHE A CZ  1 
ATOM   3033 N N   . LYS A 1 417 ? 16.860 11.556 17.728 1.00 30.88 ? 447 LYS A N   1 
ATOM   3034 C CA  . LYS A 1 417 ? 15.497 11.852 18.142 1.00 29.66 ? 447 LYS A CA  1 
ATOM   3035 C C   . LYS A 1 417 ? 15.261 13.342 17.959 1.00 28.11 ? 447 LYS A C   1 
ATOM   3036 O O   . LYS A 1 417 ? 16.057 14.160 18.431 1.00 23.48 ? 447 LYS A O   1 
ATOM   3037 C CB  . LYS A 1 417 ? 15.250 11.432 19.596 1.00 31.42 ? 447 LYS A CB  1 
ATOM   3038 C CG  . LYS A 1 417 ? 15.362 9.927  19.825 1.00 38.84 ? 447 LYS A CG  1 
ATOM   3039 C CD  . LYS A 1 417 ? 15.202 9.567  21.299 1.00 40.82 ? 447 LYS A CD  1 
ATOM   3040 C CE  . LYS A 1 417 ? 15.300 8.064  21.518 1.00 40.38 ? 447 LYS A CE  1 
ATOM   3041 N NZ  . LYS A 1 417 ? 15.211 7.723  22.964 1.00 44.06 ? 447 LYS A NZ  1 
ATOM   3042 N N   . LEU A 1 418 ? 14.178 13.685 17.265 1.00 30.68 ? 448 LEU A N   1 
ATOM   3043 C CA  . LEU A 1 418 ? 13.897 15.077 16.938 1.00 29.33 ? 448 LEU A CA  1 
ATOM   3044 C C   . LEU A 1 418 ? 13.751 15.922 18.196 1.00 33.27 ? 448 LEU A C   1 
ATOM   3045 O O   . LEU A 1 418 ? 13.224 15.470 19.215 1.00 34.00 ? 448 LEU A O   1 
ATOM   3046 C CB  . LEU A 1 418 ? 12.622 15.177 16.100 1.00 33.03 ? 448 LEU A CB  1 
ATOM   3047 C CG  . LEU A 1 418 ? 12.669 14.549 14.709 1.00 28.03 ? 448 LEU A CG  1 
ATOM   3048 C CD1 . LEU A 1 418 ? 11.289 14.573 14.077 1.00 25.80 ? 448 LEU A CD1 1 
ATOM   3049 C CD2 . LEU A 1 418 ? 13.677 15.279 13.838 1.00 27.79 ? 448 LEU A CD2 1 
ATOM   3050 N N   . ASP A 1 419 ? 14.230 17.158 18.117 1.00 38.46 ? 449 ASP A N   1 
ATOM   3051 C CA  . ASP A 1 419 ? 14.053 18.113 19.195 1.00 36.25 ? 449 ASP A CA  1 
ATOM   3052 C C   . ASP A 1 419 ? 12.695 18.796 19.068 1.00 38.50 ? 449 ASP A C   1 
ATOM   3053 O O   . ASP A 1 419 ? 11.997 18.675 18.058 1.00 34.10 ? 449 ASP A O   1 
ATOM   3054 C CB  . ASP A 1 419 ? 15.168 19.153 19.176 1.00 33.46 ? 449 ASP A CB  1 
ATOM   3055 C CG  . ASP A 1 419 ? 15.144 20.002 17.919 1.00 36.69 ? 449 ASP A CG  1 
ATOM   3056 O OD1 . ASP A 1 419 ? 15.337 19.442 16.817 1.00 31.45 ? 449 ASP A OD1 1 
ATOM   3057 O OD2 . ASP A 1 419 ? 14.905 21.223 18.032 1.00 35.68 ? 449 ASP A OD2 1 
ATOM   3058 N N   . GLU A 1 420 ? 12.327 19.533 20.113 1.00 31.30 ? 450 GLU A N   1 
ATOM   3059 C CA  . GLU A 1 420 ? 11.042 20.215 20.147 1.00 43.63 ? 450 GLU A CA  1 
ATOM   3060 C C   . GLU A 1 420 ? 11.088 21.601 19.523 1.00 43.04 ? 450 GLU A C   1 
ATOM   3061 O O   . GLU A 1 420 ? 10.029 22.168 19.230 1.00 40.58 ? 450 GLU A O   1 
ATOM   3062 C CB  . GLU A 1 420 ? 10.549 20.329 21.591 1.00 38.09 ? 450 GLU A CB  1 
ATOM   3063 C CG  . GLU A 1 420 ? 10.703 19.051 22.393 1.00 44.56 ? 450 GLU A CG  1 
ATOM   3064 C CD  . GLU A 1 420 ? 9.786  17.941 21.924 1.00 47.73 ? 450 GLU A CD  1 
ATOM   3065 O OE1 . GLU A 1 420 ? 8.773  18.240 21.256 1.00 52.62 ? 450 GLU A OE1 1 
ATOM   3066 O OE2 . GLU A 1 420 ? 10.076 16.766 22.234 1.00 50.11 ? 450 GLU A OE2 1 
ATOM   3067 N N   . LEU A 1 421 ? 12.277 22.154 19.313 1.00 36.67 ? 451 LEU A N   1 
ATOM   3068 C CA  . LEU A 1 421 ? 12.422 23.479 18.734 1.00 37.79 ? 451 LEU A CA  1 
ATOM   3069 C C   . LEU A 1 421 ? 12.581 23.438 17.220 1.00 36.37 ? 451 LEU A C   1 
ATOM   3070 O O   . LEU A 1 421 ? 12.886 24.469 16.613 1.00 37.33 ? 451 LEU A O   1 
ATOM   3071 C CB  . LEU A 1 421 ? 13.612 24.197 19.377 1.00 36.79 ? 451 LEU A CB  1 
ATOM   3072 C CG  . LEU A 1 421 ? 13.600 24.205 20.910 1.00 30.78 ? 451 LEU A CG  1 
ATOM   3073 C CD1 . LEU A 1 421 ? 14.798 24.957 21.461 1.00 29.28 ? 451 LEU A CD1 1 
ATOM   3074 C CD2 . LEU A 1 421 ? 12.308 24.801 21.440 1.00 33.44 ? 451 LEU A CD2 1 
ATOM   3075 N N   . GLY A 1 422 ? 12.375 22.277 16.603 1.00 34.01 ? 452 GLY A N   1 
ATOM   3076 C CA  . GLY A 1 422 ? 12.522 22.145 15.167 1.00 37.17 ? 452 GLY A CA  1 
ATOM   3077 C C   . GLY A 1 422 ? 13.907 22.417 14.619 1.00 40.03 ? 452 GLY A C   1 
ATOM   3078 O O   . GLY A 1 422 ? 14.026 22.908 13.495 1.00 40.16 ? 452 GLY A O   1 
ATOM   3079 N N   . LEU A 1 423 ? 14.963 22.083 15.362 1.00 36.02 ? 453 LEU A N   1 
ATOM   3080 C CA  . LEU A 1 423 ? 16.321 22.347 14.898 1.00 33.25 ? 453 LEU A CA  1 
ATOM   3081 C C   . LEU A 1 423 ? 16.956 21.151 14.191 1.00 34.75 ? 453 LEU A C   1 
ATOM   3082 O O   . LEU A 1 423 ? 17.718 21.337 13.236 1.00 38.07 ? 453 LEU A O   1 
ATOM   3083 C CB  . LEU A 1 423 ? 17.200 22.777 16.074 1.00 35.17 ? 453 LEU A CB  1 
ATOM   3084 C CG  . LEU A 1 423 ? 16.808 24.100 16.733 1.00 34.50 ? 453 LEU A CG  1 
ATOM   3085 C CD1 . LEU A 1 423 ? 17.743 24.432 17.885 1.00 28.55 ? 453 LEU A CD1 1 
ATOM   3086 C CD2 . LEU A 1 423 ? 16.782 25.229 15.712 1.00 29.29 ? 453 LEU A CD2 1 
ATOM   3087 N N   . PHE A 1 424 ? 16.683 19.927 14.647 1.00 28.98 ? 454 PHE A N   1 
ATOM   3088 C CA  . PHE A 1 424 ? 17.246 18.735 14.019 1.00 30.29 ? 454 PHE A CA  1 
ATOM   3089 C C   . PHE A 1 424 ? 16.476 18.412 12.742 1.00 33.44 ? 454 PHE A C   1 
ATOM   3090 O O   . PHE A 1 424 ? 15.245 18.299 12.762 1.00 28.07 ? 454 PHE A O   1 
ATOM   3091 C CB  . PHE A 1 424 ? 17.201 17.531 14.967 1.00 32.76 ? 454 PHE A CB  1 
ATOM   3092 C CG  . PHE A 1 424 ? 17.905 17.743 16.283 1.00 25.72 ? 454 PHE A CG  1 
ATOM   3093 C CD1 . PHE A 1 424 ? 18.819 18.773 16.453 1.00 26.78 ? 454 PHE A CD1 1 
ATOM   3094 C CD2 . PHE A 1 424 ? 17.642 16.904 17.354 1.00 27.28 ? 454 PHE A CD2 1 
ATOM   3095 C CE1 . PHE A 1 424 ? 19.453 18.960 17.668 1.00 22.02 ? 454 PHE A CE1 1 
ATOM   3096 C CE2 . PHE A 1 424 ? 18.274 17.085 18.569 1.00 28.17 ? 454 PHE A CE2 1 
ATOM   3097 C CZ  . PHE A 1 424 ? 19.180 18.112 18.726 1.00 25.20 ? 454 PHE A CZ  1 
ATOM   3098 N N   . ASP A 1 425 ? 17.201 18.239 11.637 1.00 33.02 ? 455 ASP A N   1 
ATOM   3099 C CA  . ASP A 1 425 ? 16.586 18.157 10.314 1.00 29.12 ? 455 ASP A CA  1 
ATOM   3100 C C   . ASP A 1 425 ? 16.900 16.823 9.645  1.00 28.00 ? 455 ASP A C   1 
ATOM   3101 O O   . ASP A 1 425 ? 18.026 16.599 9.191  1.00 27.71 ? 455 ASP A O   1 
ATOM   3102 C CB  . ASP A 1 425 ? 17.052 19.322 9.444  1.00 28.14 ? 455 ASP A CB  1 
ATOM   3103 C CG  . ASP A 1 425 ? 16.195 19.504 8.209  1.00 30.47 ? 455 ASP A CG  1 
ATOM   3104 O OD1 . ASP A 1 425 ? 15.304 18.666 7.975  1.00 33.51 ? 455 ASP A OD1 1 
ATOM   3105 O OD2 . ASP A 1 425 ? 16.417 20.486 7.466  1.00 24.44 ? 455 ASP A OD2 1 
ATOM   3106 N N   . TRP A 1 426 ? 15.901 15.950 9.577  1.00 32.39 ? 456 TRP A N   1 
ATOM   3107 C CA  . TRP A 1 426 ? 15.969 14.728 8.789  1.00 34.53 ? 456 TRP A CA  1 
ATOM   3108 C C   . TRP A 1 426 ? 14.544 14.259 8.517  1.00 32.75 ? 456 TRP A C   1 
ATOM   3109 O O   . TRP A 1 426 ? 13.608 14.694 9.199  1.00 36.40 ? 456 TRP A O   1 
ATOM   3110 C CB  . TRP A 1 426 ? 16.793 13.640 9.503  1.00 27.59 ? 456 TRP A CB  1 
ATOM   3111 C CG  . TRP A 1 426 ? 16.315 13.258 10.861 1.00 30.26 ? 456 TRP A CG  1 
ATOM   3112 C CD1 . TRP A 1 426 ? 15.187 12.554 11.170 1.00 32.57 ? 456 TRP A CD1 1 
ATOM   3113 C CD2 . TRP A 1 426 ? 16.976 13.524 12.100 1.00 26.81 ? 456 TRP A CD2 1 
ATOM   3114 N NE1 . TRP A 1 426 ? 15.096 12.382 12.530 1.00 29.66 ? 456 TRP A NE1 1 
ATOM   3115 C CE2 . TRP A 1 426 ? 16.184 12.967 13.123 1.00 29.29 ? 456 TRP A CE2 1 
ATOM   3116 C CE3 . TRP A 1 426 ? 18.158 14.186 12.444 1.00 27.87 ? 456 TRP A CE3 1 
ATOM   3117 C CZ2 . TRP A 1 426 ? 16.534 13.053 14.468 1.00 26.17 ? 456 TRP A CZ2 1 
ATOM   3118 C CZ3 . TRP A 1 426 ? 18.506 14.269 13.780 1.00 26.58 ? 456 TRP A CZ3 1 
ATOM   3119 C CH2 . TRP A 1 426 ? 17.696 13.708 14.777 1.00 29.71 ? 456 TRP A CH2 1 
ATOM   3120 N N   . PRO A 1 427 ? 14.343 13.394 7.522  1.00 37.85 ? 457 PRO A N   1 
ATOM   3121 C CA  . PRO A 1 427 ? 12.975 13.021 7.109  1.00 40.87 ? 457 PRO A CA  1 
ATOM   3122 C C   . PRO A 1 427 ? 12.183 12.407 8.250  1.00 37.82 ? 457 PRO A C   1 
ATOM   3123 O O   . PRO A 1 427 ? 12.763 11.853 9.195  1.00 40.07 ? 457 PRO A O   1 
ATOM   3124 C CB  . PRO A 1 427 ? 13.216 12.000 5.987  1.00 37.87 ? 457 PRO A CB  1 
ATOM   3125 C CG  . PRO A 1 427 ? 14.525 12.393 5.413  1.00 35.02 ? 457 PRO A CG  1 
ATOM   3126 C CD  . PRO A 1 427 ? 15.353 12.862 6.586  1.00 37.03 ? 457 PRO A CD  1 
ATOM   3127 N N   . PRO A 1 428 ? 10.850 12.484 8.196  1.00 39.77 ? 458 PRO A N   1 
ATOM   3128 C CA  . PRO A 1 428 ? 10.041 11.916 9.288  1.00 45.94 ? 458 PRO A CA  1 
ATOM   3129 C C   . PRO A 1 428 ? 10.217 10.418 9.458  1.00 45.47 ? 458 PRO A C   1 
ATOM   3130 O O   . PRO A 1 428 ? 10.044 9.907  10.572 1.00 43.44 ? 458 PRO A O   1 
ATOM   3131 C CB  . PRO A 1 428 ? 8.604  12.277 8.884  1.00 42.75 ? 458 PRO A CB  1 
ATOM   3132 C CG  . PRO A 1 428 ? 8.663  12.494 7.405  1.00 45.38 ? 458 PRO A CG  1 
ATOM   3133 C CD  . PRO A 1 428 ? 10.014 13.094 7.147  1.00 48.75 ? 458 PRO A CD  1 
ATOM   3134 N N   . GLU A 1 429 ? 10.566 9.699  8.388  1.00 45.77 ? 459 GLU A N   1 
ATOM   3135 C CA  . GLU A 1 429 ? 10.821 8.268  8.508  1.00 44.52 ? 459 GLU A CA  1 
ATOM   3136 C C   . GLU A 1 429 ? 12.011 7.991  9.413  1.00 45.65 ? 459 GLU A C   1 
ATOM   3137 O O   . GLU A 1 429 ? 12.088 6.925  10.034 1.00 52.03 ? 459 GLU A O   1 
ATOM   3138 C CB  . GLU A 1 429 ? 11.061 7.656  7.126  1.00 45.93 ? 459 GLU A CB  1 
ATOM   3139 C CG  . GLU A 1 429 ? 9.922  7.851  6.127  1.00 56.95 ? 459 GLU A CG  1 
ATOM   3140 C CD  . GLU A 1 429 ? 9.960  9.205  5.437  1.00 55.68 ? 459 GLU A CD  1 
ATOM   3141 O OE1 . GLU A 1 429 ? 10.605 10.133 5.967  1.00 50.89 ? 459 GLU A OE1 1 
ATOM   3142 O OE2 . GLU A 1 429 ? 9.345  9.339  4.359  1.00 59.25 ? 459 GLU A OE2 1 
ATOM   3143 N N   . GLY A 1 430 ? 12.939 8.937  9.506  1.00 43.83 ? 460 GLY A N   1 
ATOM   3144 C CA  . GLY A 1 430 ? 14.133 8.773  10.295 1.00 38.32 ? 460 GLY A CA  1 
ATOM   3145 C C   . GLY A 1 430 ? 15.339 9.291  9.543  1.00 36.31 ? 460 GLY A C   1 
ATOM   3146 O O   . GLY A 1 430 ? 15.237 9.724  8.392  1.00 36.74 ? 460 GLY A O   1 
ATOM   3147 N N   . PRO A 1 431 ? 16.504 9.269  10.183 1.00 37.98 ? 461 PRO A N   1 
ATOM   3148 C CA  . PRO A 1 431 ? 17.724 9.715  9.502  1.00 32.72 ? 461 PRO A CA  1 
ATOM   3149 C C   . PRO A 1 431 ? 18.090 8.795  8.347  1.00 32.53 ? 461 PRO A C   1 
ATOM   3150 O O   . PRO A 1 431 ? 17.863 7.583  8.387  1.00 40.46 ? 461 PRO A O   1 
ATOM   3151 C CB  . PRO A 1 431 ? 18.785 9.668  10.608 1.00 32.02 ? 461 PRO A CB  1 
ATOM   3152 C CG  . PRO A 1 431 ? 18.251 8.686  11.604 1.00 31.78 ? 461 PRO A CG  1 
ATOM   3153 C CD  . PRO A 1 431 ? 16.759 8.859  11.573 1.00 31.59 ? 461 PRO A CD  1 
ATOM   3154 N N   . THR A 1 432 ? 18.655 9.393  7.301  1.00 28.12 ? 462 THR A N   1 
ATOM   3155 C CA  . THR A 1 432 ? 19.115 8.621  6.162  1.00 28.51 ? 462 THR A CA  1 
ATOM   3156 C C   . THR A 1 432 ? 20.352 7.813  6.550  1.00 30.34 ? 462 THR A C   1 
ATOM   3157 O O   . THR A 1 432 ? 20.991 8.089  7.569  1.00 28.58 ? 462 THR A O   1 
ATOM   3158 C CB  . THR A 1 432 ? 19.429 9.544  4.982  1.00 33.17 ? 462 THR A CB  1 
ATOM   3159 O OG1 . THR A 1 432 ? 20.601 10.317 5.270  1.00 29.28 ? 462 THR A OG1 1 
ATOM   3160 C CG2 . THR A 1 432 ? 18.258 10.481 4.706  1.00 23.80 ? 462 THR A CG2 1 
ATOM   3161 N N   . PRO A 1 433 ? 20.695 6.783  5.771  1.00 32.37 ? 463 PRO A N   1 
ATOM   3162 C CA  . PRO A 1 433 ? 21.965 6.081  6.027  1.00 27.77 ? 463 PRO A CA  1 
ATOM   3163 C C   . PRO A 1 433 ? 23.175 6.997  5.983  1.00 27.78 ? 463 PRO A C   1 
ATOM   3164 O O   . PRO A 1 433 ? 24.139 6.768  6.724  1.00 32.73 ? 463 PRO A O   1 
ATOM   3165 C CB  . PRO A 1 433 ? 22.012 5.016  4.920  1.00 27.76 ? 463 PRO A CB  1 
ATOM   3166 C CG  . PRO A 1 433 ? 20.911 5.378  3.952  1.00 30.83 ? 463 PRO A CG  1 
ATOM   3167 C CD  . PRO A 1 433 ? 19.884 6.098  4.752  1.00 26.06 ? 463 PRO A CD  1 
ATOM   3168 N N   . ALA A 1 434 ? 23.147 8.036  5.144  1.00 24.59 ? 464 ALA A N   1 
ATOM   3169 C CA  . ALA A 1 434 ? 24.225 9.018  5.150  1.00 25.93 ? 464 ALA A CA  1 
ATOM   3170 C C   . ALA A 1 434 ? 24.273 9.776  6.470  1.00 25.69 ? 464 ALA A C   1 
ATOM   3171 O O   . ALA A 1 434 ? 25.360 10.098 6.965  1.00 27.53 ? 464 ALA A O   1 
ATOM   3172 C CB  . ALA A 1 434 ? 24.066 9.987  3.982  1.00 22.31 ? 464 ALA A CB  1 
ATOM   3173 N N   . ASP A 1 435 ? 23.108 10.069 7.053  1.00 24.28 ? 465 ASP A N   1 
ATOM   3174 C CA  . ASP A 1 435 ? 23.084 10.720 8.359  1.00 27.05 ? 465 ASP A CA  1 
ATOM   3175 C C   . ASP A 1 435 ? 23.761 9.848  9.410  1.00 27.66 ? 465 ASP A C   1 
ATOM   3176 O O   . ASP A 1 435 ? 24.575 10.333 10.202 1.00 27.66 ? 465 ASP A O   1 
ATOM   3177 C CB  . ASP A 1 435 ? 21.644 11.038 8.767  1.00 27.27 ? 465 ASP A CB  1 
ATOM   3178 C CG  . ASP A 1 435 ? 20.991 12.067 7.863  1.00 31.30 ? 465 ASP A CG  1 
ATOM   3179 O OD1 . ASP A 1 435 ? 21.692 12.993 7.406  1.00 31.02 ? 465 ASP A OD1 1 
ATOM   3180 O OD2 . ASP A 1 435 ? 19.775 11.938 7.604  1.00 28.45 ? 465 ASP A OD2 1 
ATOM   3181 N N   . ARG A 1 436 ? 23.454 8.547  9.416  1.00 26.45 ? 466 ARG A N   1 
ATOM   3182 C CA  . ARG A 1 436 ? 24.044 7.658  10.412 1.00 29.09 ? 466 ARG A CA  1 
ATOM   3183 C C   . ARG A 1 436 ? 25.540 7.467  10.170 1.00 29.61 ? 466 ARG A C   1 
ATOM   3184 O O   . ARG A 1 436 ? 26.317 7.348  11.125 1.00 30.06 ? 466 ARG A O   1 
ATOM   3185 C CB  . ARG A 1 436 ? 23.304 6.320  10.421 1.00 31.02 ? 466 ARG A CB  1 
ATOM   3186 C CG  . ARG A 1 436 ? 21.934 6.400  11.064 1.00 35.15 ? 466 ARG A CG  1 
ATOM   3187 C CD  . ARG A 1 436 ? 21.829 5.473  12.266 1.00 46.44 ? 466 ARG A CD  1 
ATOM   3188 N NE  . ARG A 1 436 ? 20.644 5.735  13.077 1.00 57.03 ? 466 ARG A NE  1 
ATOM   3189 C CZ  . ARG A 1 436 ? 19.410 5.369  12.752 1.00 54.29 ? 466 ARG A CZ  1 
ATOM   3190 N NH1 . ARG A 1 436 ? 19.150 4.745  11.614 1.00 48.04 ? 466 ARG A NH1 1 
ATOM   3191 N NH2 . ARG A 1 436 ? 18.411 5.640  13.587 1.00 48.36 ? 466 ARG A NH2 1 
ATOM   3192 N N   . ALA A 1 437 ? 25.962 7.437  8.902  1.00 23.00 ? 467 ALA A N   1 
ATOM   3193 C CA  . ALA A 1 437 ? 27.385 7.317  8.597  1.00 30.10 ? 467 ALA A CA  1 
ATOM   3194 C C   . ALA A 1 437 ? 28.150 8.551  9.065  1.00 24.64 ? 467 ALA A C   1 
ATOM   3195 O O   . ALA A 1 437 ? 29.226 8.441  9.672  1.00 28.66 ? 467 ALA A O   1 
ATOM   3196 C CB  . ALA A 1 437 ? 27.573 7.090  7.096  1.00 22.95 ? 467 ALA A CB  1 
ATOM   3197 N N   . LEU A 1 438 ? 27.615 9.740  8.772  1.00 23.88 ? 468 LEU A N   1 
ATOM   3198 C CA  . LEU A 1 438 ? 28.235 10.972 9.244  1.00 23.40 ? 468 LEU A CA  1 
ATOM   3199 C C   . LEU A 1 438 ? 28.259 11.020 10.767 1.00 27.07 ? 468 LEU A C   1 
ATOM   3200 O O   . LEU A 1 438 ? 29.235 11.489 11.368 1.00 22.42 ? 468 LEU A O   1 
ATOM   3201 C CB  . LEU A 1 438 ? 27.490 12.181 8.671  1.00 18.37 ? 468 LEU A CB  1 
ATOM   3202 C CG  . LEU A 1 438 ? 28.142 13.554 8.865  1.00 22.00 ? 468 LEU A CG  1 
ATOM   3203 C CD1 . LEU A 1 438 ? 29.531 13.585 8.247  1.00 24.98 ? 468 LEU A CD1 1 
ATOM   3204 C CD2 . LEU A 1 438 ? 27.265 14.649 8.276  1.00 18.24 ? 468 LEU A CD2 1 
ATOM   3205 N N   . GLY A 1 439 ? 27.192 10.537 11.408 1.00 24.14 ? 469 GLY A N   1 
ATOM   3206 C CA  . GLY A 1 439 ? 27.173 10.494 12.859 1.00 24.99 ? 469 GLY A CA  1 
ATOM   3207 C C   . GLY A 1 439 ? 28.241 9.582  13.426 1.00 22.66 ? 469 GLY A C   1 
ATOM   3208 O O   . GLY A 1 439 ? 28.915 9.935  14.393 1.00 20.89 ? 469 GLY A O   1 
ATOM   3209 N N   . GLN A 1 440 ? 28.409 8.396  12.834 1.00 26.33 ? 470 GLN A N   1 
ATOM   3210 C CA  . GLN A 1 440 ? 29.473 7.495  13.267 1.00 26.83 ? 470 GLN A CA  1 
ATOM   3211 C C   . GLN A 1 440 ? 30.835 8.160  13.130 1.00 26.52 ? 470 GLN A C   1 
ATOM   3212 O O   . GLN A 1 440 ? 31.638 8.159  14.072 1.00 24.79 ? 470 GLN A O   1 
ATOM   3213 C CB  . GLN A 1 440 ? 29.432 6.196  12.461 1.00 28.26 ? 470 GLN A CB  1 
ATOM   3214 C CG  . GLN A 1 440 ? 28.222 5.323  12.756 1.00 45.25 ? 470 GLN A CG  1 
ATOM   3215 C CD  . GLN A 1 440 ? 28.439 3.868  12.378 1.00 59.58 ? 470 GLN A CD  1 
ATOM   3216 O OE1 . GLN A 1 440 ? 29.490 3.499  11.847 1.00 57.22 ? 470 GLN A OE1 1 
ATOM   3217 N NE2 . GLN A 1 440 ? 27.444 3.031  12.656 1.00 61.75 ? 470 GLN A NE2 1 
ATOM   3218 N N   . LEU A 1 441 ? 31.102 8.750  11.961 1.00 20.65 ? 471 LEU A N   1 
ATOM   3219 C CA  . LEU A 1 441 ? 32.382 9.418  11.737 1.00 22.27 ? 471 LEU A CA  1 
ATOM   3220 C C   . LEU A 1 441 ? 32.625 10.509 12.777 1.00 19.63 ? 471 LEU A C   1 
ATOM   3221 O O   . LEU A 1 441 ? 33.675 10.539 13.435 1.00 21.35 ? 471 LEU A O   1 
ATOM   3222 C CB  . LEU A 1 441 ? 32.415 9.992  10.318 1.00 20.41 ? 471 LEU A CB  1 
ATOM   3223 C CG  . LEU A 1 441 ? 33.690 10.636 9.770  1.00 22.15 ? 471 LEU A CG  1 
ATOM   3224 C CD1 . LEU A 1 441 ? 33.736 10.477 8.258  1.00 21.12 ? 471 LEU A CD1 1 
ATOM   3225 C CD2 . LEU A 1 441 ? 33.776 12.110 10.141 1.00 19.08 ? 471 LEU A CD2 1 
ATOM   3226 N N   . MET A 1 442 ? 31.651 11.405 12.955 1.00 21.68 ? 472 MET A N   1 
ATOM   3227 C CA  . MET A 1 442 ? 31.846 12.557 13.829 1.00 20.94 ? 472 MET A CA  1 
ATOM   3228 C C   . MET A 1 442 ? 31.944 12.145 15.294 1.00 19.96 ? 472 MET A C   1 
ATOM   3229 O O   . MET A 1 442 ? 32.786 12.669 16.036 1.00 19.57 ? 472 MET A O   1 
ATOM   3230 C CB  . MET A 1 442 ? 30.710 13.554 13.628 1.00 18.41 ? 472 MET A CB  1 
ATOM   3231 C CG  . MET A 1 442 ? 30.926 14.905 14.296 1.00 27.60 ? 472 MET A CG  1 
ATOM   3232 S SD  . MET A 1 442 ? 29.750 16.110 13.648 1.00 32.47 ? 472 MET A SD  1 
ATOM   3233 C CE  . MET A 1 442 ? 29.591 15.469 11.983 1.00 16.23 ? 472 MET A CE  1 
ATOM   3234 N N   . SER A 1 443 ? 31.083 11.225 15.738 1.00 22.22 ? 473 SER A N   1 
ATOM   3235 C CA  . SER A 1 443 ? 31.123 10.779 17.125 1.00 22.04 ? 473 SER A CA  1 
ATOM   3236 C C   . SER A 1 443 ? 32.428 10.050 17.427 1.00 16.05 ? 473 SER A C   1 
ATOM   3237 O O   . SER A 1 443 ? 33.018 10.242 18.498 1.00 15.16 ? 473 SER A O   1 
ATOM   3238 C CB  . SER A 1 443 ? 29.911 9.893  17.416 1.00 19.60 ? 473 SER A CB  1 
ATOM   3239 O OG  . SER A 1 443 ? 29.802 9.607  18.798 1.00 20.06 ? 473 SER A OG  1 
ATOM   3240 N N   . SER A 1 444 ? 32.908 9.226  16.487 1.00 16.40 ? 474 SER A N   1 
ATOM   3241 C CA  . SER A 1 444 ? 34.200 8.571  16.665 1.00 20.83 ? 474 SER A CA  1 
ATOM   3242 C C   . SER A 1 444 ? 35.329 9.588  16.741 1.00 19.04 ? 474 SER A C   1 
ATOM   3243 O O   . SER A 1 444 ? 36.285 9.404  17.501 1.00 21.14 ? 474 SER A O   1 
ATOM   3244 C CB  . SER A 1 444 ? 34.460 7.586  15.524 1.00 21.08 ? 474 SER A CB  1 
ATOM   3245 O OG  . SER A 1 444 ? 33.625 6.445  15.619 1.00 27.83 ? 474 SER A OG  1 
ATOM   3246 N N   . ALA A 1 445 ? 35.251 10.660 15.948 1.00 18.88 ? 475 ALA A N   1 
ATOM   3247 C CA  . ALA A 1 445 ? 36.298 11.677 16.022 1.00 21.34 ? 475 ALA A CA  1 
ATOM   3248 C C   . ALA A 1 445 ? 36.277 12.391 17.370 1.00 20.62 ? 475 ALA A C   1 
ATOM   3249 O O   . ALA A 1 445 ? 37.334 12.649 17.960 1.00 18.94 ? 475 ALA A O   1 
ATOM   3250 C CB  . ALA A 1 445 ? 36.151 12.675 14.877 1.00 19.55 ? 475 ALA A CB  1 
ATOM   3251 N N   . TRP A 1 446 ? 35.081 12.722 17.870 1.00 17.67 ? 476 TRP A N   1 
ATOM   3252 C CA  . TRP A 1 446 ? 34.965 13.306 19.205 1.00 17.91 ? 476 TRP A CA  1 
ATOM   3253 C C   . TRP A 1 446 ? 35.567 12.386 20.268 1.00 16.00 ? 476 TRP A C   1 
ATOM   3254 O O   . TRP A 1 446 ? 36.309 12.839 21.153 1.00 16.88 ? 476 TRP A O   1 
ATOM   3255 C CB  . TRP A 1 446 ? 33.495 13.591 19.516 1.00 14.01 ? 476 TRP A CB  1 
ATOM   3256 C CG  . TRP A 1 446 ? 33.030 15.000 19.252 1.00 13.78 ? 476 TRP A CG  1 
ATOM   3257 C CD1 . TRP A 1 446 ? 32.366 15.817 20.129 1.00 16.01 ? 476 TRP A CD1 1 
ATOM   3258 C CD2 . TRP A 1 446 ? 33.172 15.756 18.036 1.00 15.66 ? 476 TRP A CD2 1 
ATOM   3259 N NE1 . TRP A 1 446 ? 32.088 17.025 19.538 1.00 13.53 ? 476 TRP A NE1 1 
ATOM   3260 C CE2 . TRP A 1 446 ? 32.570 17.015 18.255 1.00 19.17 ? 476 TRP A CE2 1 
ATOM   3261 C CE3 . TRP A 1 446 ? 33.742 15.491 16.785 1.00 23.09 ? 476 TRP A CE3 1 
ATOM   3262 C CZ2 . TRP A 1 446 ? 32.531 18.006 17.274 1.00 13.77 ? 476 TRP A CZ2 1 
ATOM   3263 C CZ3 . TRP A 1 446 ? 33.702 16.477 15.814 1.00 17.55 ? 476 TRP A CZ3 1 
ATOM   3264 C CH2 . TRP A 1 446 ? 33.100 17.718 16.065 1.00 17.98 ? 476 TRP A CH2 1 
ATOM   3265 N N   . VAL A 1 447 ? 35.261 11.087 20.191 1.00 14.60 ? 477 VAL A N   1 
ATOM   3266 C CA  . VAL A 1 447 ? 35.796 10.140 21.169 1.00 16.45 ? 477 VAL A CA  1 
ATOM   3267 C C   . VAL A 1 447 ? 37.311 10.050 21.053 1.00 17.56 ? 477 VAL A C   1 
ATOM   3268 O O   . VAL A 1 447 ? 38.017 9.949  22.063 1.00 18.15 ? 477 VAL A O   1 
ATOM   3269 C CB  . VAL A 1 447 ? 35.133 8.760  21.010 1.00 23.91 ? 477 VAL A CB  1 
ATOM   3270 C CG1 . VAL A 1 447 ? 35.844 7.720  21.851 1.00 16.98 ? 477 VAL A CG1 1 
ATOM   3271 C CG2 . VAL A 1 447 ? 33.659 8.844  21.400 1.00 22.13 ? 477 VAL A CG2 1 
ATOM   3272 N N   . ARG A 1 448 ? 37.836 10.088 19.825 1.00 16.65 ? 478 ARG A N   1 
ATOM   3273 C CA  . ARG A 1 448 ? 39.284 10.088 19.646 1.00 18.14 ? 478 ARG A CA  1 
ATOM   3274 C C   . ARG A 1 448 ? 39.910 11.337 20.248 1.00 18.62 ? 478 ARG A C   1 
ATOM   3275 O O   . ARG A 1 448 ? 41.014 11.280 20.803 1.00 16.05 ? 478 ARG A O   1 
ATOM   3276 C CB  . ARG A 1 448 ? 39.637 9.972  18.164 1.00 17.87 ? 478 ARG A CB  1 
ATOM   3277 C CG  . ARG A 1 448 ? 39.845 8.550  17.701 1.00 19.27 ? 478 ARG A CG  1 
ATOM   3278 C CD  . ARG A 1 448 ? 40.272 8.499  16.242 1.00 20.14 ? 478 ARG A CD  1 
ATOM   3279 N NE  . ARG A 1 448 ? 39.179 8.027  15.405 1.00 33.50 ? 478 ARG A NE  1 
ATOM   3280 C CZ  . ARG A 1 448 ? 38.479 8.790  14.580 1.00 22.77 ? 478 ARG A CZ  1 
ATOM   3281 N NH1 . ARG A 1 448 ? 38.793 10.059 14.376 1.00 22.16 ? 478 ARG A NH1 1 
ATOM   3282 N NH2 . ARG A 1 448 ? 37.439 8.264  13.940 1.00 27.97 ? 478 ARG A NH2 1 
ATOM   3283 N N   . PHE A 1 449 ? 39.227 12.480 20.140 1.00 15.40 ? 479 PHE A N   1 
ATOM   3284 C CA  . PHE A 1 449 ? 39.743 13.688 20.771 1.00 16.42 ? 479 PHE A CA  1 
ATOM   3285 C C   . PHE A 1 449 ? 39.791 13.520 22.280 1.00 18.68 ? 479 PHE A C   1 
ATOM   3286 O O   . PHE A 1 449 ? 40.747 13.955 22.930 1.00 18.13 ? 479 PHE A O   1 
ATOM   3287 C CB  . PHE A 1 449 ? 38.892 14.900 20.391 1.00 16.06 ? 479 PHE A CB  1 
ATOM   3288 C CG  . PHE A 1 449 ? 39.374 16.194 20.995 1.00 19.28 ? 479 PHE A CG  1 
ATOM   3289 C CD1 . PHE A 1 449 ? 40.439 16.884 20.438 1.00 18.80 ? 479 PHE A CD1 1 
ATOM   3290 C CD2 . PHE A 1 449 ? 38.760 16.719 22.119 1.00 15.47 ? 479 PHE A CD2 1 
ATOM   3291 C CE1 . PHE A 1 449 ? 40.882 18.074 20.993 1.00 20.99 ? 479 PHE A CE1 1 
ATOM   3292 C CE2 . PHE A 1 449 ? 39.198 17.910 22.677 1.00 18.95 ? 479 PHE A CE2 1 
ATOM   3293 C CZ  . PHE A 1 449 ? 40.261 18.587 22.114 1.00 18.91 ? 479 PHE A CZ  1 
ATOM   3294 N N   . ALA A 1 450 ? 38.769 12.880 22.852 1.00 14.40 ? 480 ALA A N   1 
ATOM   3295 C CA  . ALA A 1 450 ? 38.762 12.667 24.296 1.00 18.64 ? 480 ALA A CA  1 
ATOM   3296 C C   . ALA A 1 450 ? 39.846 11.675 24.719 1.00 19.90 ? 480 ALA A C   1 
ATOM   3297 O O   . ALA A 1 450 ? 40.443 11.820 25.794 1.00 19.63 ? 480 ALA A O   1 
ATOM   3298 C CB  . ALA A 1 450 ? 37.383 12.193 24.753 1.00 14.11 ? 480 ALA A CB  1 
ATOM   3299 N N   . LYS A 1 451 ? 40.096 10.651 23.898 1.00 17.71 ? 481 LYS A N   1 
ATOM   3300 C CA  . LYS A 1 451 ? 41.022 9.584  24.276 1.00 20.60 ? 481 LYS A CA  1 
ATOM   3301 C C   . LYS A 1 451 ? 42.481 9.983  24.079 1.00 21.22 ? 481 LYS A C   1 
ATOM   3302 O O   . LYS A 1 451 ? 43.317 9.750  24.957 1.00 20.29 ? 481 LYS A O   1 
ATOM   3303 C CB  . LYS A 1 451 ? 40.725 8.320  23.471 1.00 19.32 ? 481 LYS A CB  1 
ATOM   3304 C CG  . LYS A 1 451 ? 39.497 7.561  23.914 1.00 34.03 ? 481 LYS A CG  1 
ATOM   3305 C CD  . LYS A 1 451 ? 39.285 6.340  23.037 1.00 38.86 ? 481 LYS A CD  1 
ATOM   3306 C CE  . LYS A 1 451 ? 38.149 5.471  23.546 1.00 30.79 ? 481 LYS A CE  1 
ATOM   3307 N NZ  . LYS A 1 451 ? 37.830 4.427  22.533 1.00 24.85 ? 481 LYS A NZ  1 
ATOM   3308 N N   . ASN A 1 452 ? 42.803 10.569 22.930 1.00 15.99 ? 482 ASN A N   1 
ATOM   3309 C CA  . ASN A 1 452 ? 44.177 10.816 22.523 1.00 24.81 ? 482 ASN A CA  1 
ATOM   3310 C C   . ASN A 1 452 ? 44.525 12.296 22.461 1.00 20.12 ? 482 ASN A C   1 
ATOM   3311 O O   . ASN A 1 452 ? 45.689 12.629 22.219 1.00 21.81 ? 482 ASN A O   1 
ATOM   3312 C CB  . ASN A 1 452 ? 44.438 10.178 21.152 1.00 19.86 ? 482 ASN A CB  1 
ATOM   3313 C CG  . ASN A 1 452 ? 43.888 8.767  21.047 1.00 22.08 ? 482 ASN A CG  1 
ATOM   3314 O OD1 . ASN A 1 452 ? 43.916 7.999  22.008 1.00 27.05 ? 482 ASN A OD1 1 
ATOM   3315 N ND2 . ASN A 1 452 ? 43.385 8.419  19.865 1.00 23.02 ? 482 ASN A ND2 1 
ATOM   3316 N N   . GLY A 1 453 ? 43.555 13.189 22.666 1.00 17.42 ? 483 GLY A N   1 
ATOM   3317 C CA  . GLY A 1 453 ? 43.791 14.606 22.468 1.00 17.46 ? 483 GLY A CA  1 
ATOM   3318 C C   . GLY A 1 453 ? 43.866 15.021 21.018 1.00 20.62 ? 483 GLY A C   1 
ATOM   3319 O O   . GLY A 1 453 ? 44.363 16.109 20.717 1.00 22.07 ? 483 GLY A O   1 
ATOM   3320 N N   . ASP A 1 454 ? 43.371 14.186 20.109 1.00 18.42 ? 484 ASP A N   1 
ATOM   3321 C CA  . ASP A 1 454 ? 43.548 14.377 18.678 1.00 17.36 ? 484 ASP A CA  1 
ATOM   3322 C C   . ASP A 1 454 ? 42.374 13.737 17.945 1.00 16.29 ? 484 ASP A C   1 
ATOM   3323 O O   . ASP A 1 454 ? 42.139 12.531 18.091 1.00 16.82 ? 484 ASP A O   1 
ATOM   3324 C CB  . ASP A 1 454 ? 44.885 13.766 18.237 1.00 19.72 ? 484 ASP A CB  1 
ATOM   3325 C CG  . ASP A 1 454 ? 45.292 14.164 16.826 1.00 22.86 ? 484 ASP A CG  1 
ATOM   3326 O OD1 . ASP A 1 454 ? 44.411 14.449 15.989 1.00 18.25 ? 484 ASP A OD1 1 
ATOM   3327 O OD2 . ASP A 1 454 ? 46.512 14.179 16.554 1.00 23.17 ? 484 ASP A OD2 1 
ATOM   3328 N N   . PRO A 1 455 ? 41.610 14.502 17.158 1.00 15.92 ? 485 PRO A N   1 
ATOM   3329 C CA  . PRO A 1 455 ? 40.441 13.924 16.480 1.00 17.75 ? 485 PRO A CA  1 
ATOM   3330 C C   . PRO A 1 455 ? 40.778 13.120 15.232 1.00 20.75 ? 485 PRO A C   1 
ATOM   3331 O O   . PRO A 1 455 ? 39.870 12.520 14.641 1.00 18.48 ? 485 PRO A O   1 
ATOM   3332 C CB  . PRO A 1 455 ? 39.605 15.161 16.126 1.00 18.81 ? 485 PRO A CB  1 
ATOM   3333 C CG  . PRO A 1 455 ? 40.618 16.240 15.942 1.00 18.44 ? 485 PRO A CG  1 
ATOM   3334 C CD  . PRO A 1 455 ? 41.737 15.949 16.910 1.00 15.99 ? 485 PRO A CD  1 
ATOM   3335 N N   . ALA A 1 456 ? 42.035 13.091 14.806 1.00 18.11 ? 486 ALA A N   1 
ATOM   3336 C CA  . ALA A 1 456 ? 42.387 12.308 13.636 1.00 21.92 ? 486 ALA A CA  1 
ATOM   3337 C C   . ALA A 1 456 ? 42.398 10.820 13.973 1.00 21.60 ? 486 ALA A C   1 
ATOM   3338 O O   . ALA A 1 456 ? 42.575 10.415 15.125 1.00 21.96 ? 486 ALA A O   1 
ATOM   3339 C CB  . ALA A 1 456 ? 43.748 12.735 13.092 1.00 16.50 ? 486 ALA A CB  1 
ATOM   3340 N N   . GLY A 1 457 ? 42.179 10.003 12.944 1.00 23.01 ? 487 GLY A N   1 
ATOM   3341 C CA  . GLY A 1 457 ? 42.222 8.562  13.078 1.00 30.73 ? 487 GLY A CA  1 
ATOM   3342 C C   . GLY A 1 457 ? 42.869 7.936  11.859 1.00 34.47 ? 487 GLY A C   1 
ATOM   3343 O O   . GLY A 1 457 ? 43.309 8.634  10.943 1.00 30.56 ? 487 GLY A O   1 
ATOM   3344 N N   . ASP A 1 458 ? 42.916 6.601  11.863 1.00 36.20 ? 488 ASP A N   1 
ATOM   3345 C CA  . ASP A 1 458 ? 43.513 5.859  10.758 1.00 40.62 ? 488 ASP A CA  1 
ATOM   3346 C C   . ASP A 1 458 ? 42.721 5.980  9.463  1.00 37.67 ? 488 ASP A C   1 
ATOM   3347 O O   . ASP A 1 458 ? 43.246 5.624  8.402  1.00 42.57 ? 488 ASP A O   1 
ATOM   3348 C CB  . ASP A 1 458 ? 43.660 4.382  11.131 1.00 39.91 ? 488 ASP A CB  1 
ATOM   3349 C CG  . ASP A 1 458 ? 44.749 4.149  12.155 1.00 49.83 ? 488 ASP A CG  1 
ATOM   3350 O OD1 . ASP A 1 458 ? 45.443 5.122  12.520 1.00 52.89 ? 488 ASP A OD1 1 
ATOM   3351 O OD2 . ASP A 1 458 ? 44.914 2.992  12.593 1.00 60.68 ? 488 ASP A OD2 1 
ATOM   3352 N N   . ALA A 1 459 ? 41.482 6.466  9.520  1.00 36.94 ? 489 ALA A N   1 
ATOM   3353 C CA  . ALA A 1 459 ? 40.666 6.661  8.329  1.00 36.46 ? 489 ALA A CA  1 
ATOM   3354 C C   . ALA A 1 459 ? 40.210 8.104  8.165  1.00 33.57 ? 489 ALA A C   1 
ATOM   3355 O O   . ALA A 1 459 ? 39.440 8.396  7.243  1.00 41.59 ? 489 ALA A O   1 
ATOM   3356 C CB  . ALA A 1 459 ? 39.447 5.732  8.354  1.00 38.02 ? 489 ALA A CB  1 
ATOM   3357 N N   . LEU A 1 460 ? 40.662 9.013  9.026  1.00 28.41 ? 490 LEU A N   1 
ATOM   3358 C CA  . LEU A 1 460 ? 40.242 10.412 8.967  1.00 28.98 ? 490 LEU A CA  1 
ATOM   3359 C C   . LEU A 1 460 ? 41.471 11.289 9.190  1.00 31.33 ? 490 LEU A C   1 
ATOM   3360 O O   . LEU A 1 460 ? 41.892 11.499 10.332 1.00 28.99 ? 490 LEU A O   1 
ATOM   3361 C CB  . LEU A 1 460 ? 39.154 10.703 9.993  1.00 27.71 ? 490 LEU A CB  1 
ATOM   3362 C CG  . LEU A 1 460 ? 38.508 12.082 9.851  1.00 28.92 ? 490 LEU A CG  1 
ATOM   3363 C CD1 . LEU A 1 460 ? 37.776 12.181 8.519  1.00 24.79 ? 490 LEU A CD1 1 
ATOM   3364 C CD2 . LEU A 1 460 ? 37.573 12.379 11.014 1.00 20.87 ? 490 LEU A CD2 1 
ATOM   3365 N N   . THR A 1 461 ? 42.040 11.800 8.100  1.00 29.28 ? 491 THR A N   1 
ATOM   3366 C CA  . THR A 1 461 ? 43.147 12.742 8.192  1.00 27.36 ? 491 THR A CA  1 
ATOM   3367 C C   . THR A 1 461 ? 42.602 14.100 8.609  1.00 29.94 ? 491 THR A C   1 
ATOM   3368 O O   . THR A 1 461 ? 41.713 14.645 7.948  1.00 26.86 ? 491 THR A O   1 
ATOM   3369 C CB  . THR A 1 461 ? 43.884 12.850 6.860  1.00 29.02 ? 491 THR A CB  1 
ATOM   3370 O OG1 . THR A 1 461 ? 44.246 11.539 6.407  1.00 33.31 ? 491 THR A OG1 1 
ATOM   3371 C CG2 . THR A 1 461 ? 45.144 13.688 7.030  1.00 26.99 ? 491 THR A CG2 1 
ATOM   3372 N N   . TRP A 1 462 ? 43.128 14.646 9.705  1.00 24.62 ? 492 TRP A N   1 
ATOM   3373 C CA  . TRP A 1 462 ? 42.634 15.908 10.249 1.00 21.92 ? 492 TRP A CA  1 
ATOM   3374 C C   . TRP A 1 462 ? 43.796 16.668 10.871 1.00 24.61 ? 492 TRP A C   1 
ATOM   3375 O O   . TRP A 1 462 ? 44.058 16.560 12.077 1.00 18.94 ? 492 TRP A O   1 
ATOM   3376 C CB  . TRP A 1 462 ? 41.521 15.670 11.269 1.00 18.88 ? 492 TRP A CB  1 
ATOM   3377 C CG  . TRP A 1 462 ? 40.777 16.906 11.675 1.00 15.81 ? 492 TRP A CG  1 
ATOM   3378 C CD1 . TRP A 1 462 ? 41.153 18.204 11.469 1.00 17.40 ? 492 TRP A CD1 1 
ATOM   3379 C CD2 . TRP A 1 462 ? 39.525 16.956 12.359 1.00 15.37 ? 492 TRP A CD2 1 
ATOM   3380 N NE1 . TRP A 1 462 ? 40.212 19.057 11.986 1.00 15.47 ? 492 TRP A NE1 1 
ATOM   3381 C CE2 . TRP A 1 462 ? 39.203 18.316 12.542 1.00 20.46 ? 492 TRP A CE2 1 
ATOM   3382 C CE3 . TRP A 1 462 ? 38.638 15.981 12.830 1.00 16.80 ? 492 TRP A CE3 1 
ATOM   3383 C CZ2 . TRP A 1 462 ? 38.031 18.727 13.174 1.00 20.07 ? 492 TRP A CZ2 1 
ATOM   3384 C CZ3 . TRP A 1 462 ? 37.473 16.393 13.465 1.00 15.80 ? 492 TRP A CZ3 1 
ATOM   3385 C CH2 . TRP A 1 462 ? 37.182 17.754 13.629 1.00 17.07 ? 492 TRP A CH2 1 
ATOM   3386 N N   . PRO A 1 463 ? 44.519 17.448 10.074 1.00 24.29 ? 493 PRO A N   1 
ATOM   3387 C CA  . PRO A 1 463 ? 45.592 18.277 10.630 1.00 23.50 ? 493 PRO A CA  1 
ATOM   3388 C C   . PRO A 1 463 ? 45.027 19.409 11.473 1.00 20.37 ? 493 PRO A C   1 
ATOM   3389 O O   . PRO A 1 463 ? 43.884 19.844 11.304 1.00 19.80 ? 493 PRO A O   1 
ATOM   3390 C CB  . PRO A 1 463 ? 46.314 18.812 9.388  1.00 24.23 ? 493 PRO A CB  1 
ATOM   3391 C CG  . PRO A 1 463 ? 45.288 18.750 8.303  1.00 25.81 ? 493 PRO A CG  1 
ATOM   3392 C CD  . PRO A 1 463 ? 44.420 17.564 8.609  1.00 22.00 ? 493 PRO A CD  1 
ATOM   3393 N N   . ALA A 1 464 ? 45.862 19.881 12.396 1.00 20.61 ? 494 ALA A N   1 
ATOM   3394 C CA  . ALA A 1 464 ? 45.486 20.978 13.275 1.00 21.84 ? 494 ALA A CA  1 
ATOM   3395 C C   . ALA A 1 464 ? 45.226 22.248 12.473 1.00 18.26 ? 494 ALA A C   1 
ATOM   3396 O O   . ALA A 1 464 ? 45.758 22.441 11.374 1.00 19.25 ? 494 ALA A O   1 
ATOM   3397 C CB  . ALA A 1 464 ? 46.583 21.220 14.312 1.00 23.15 ? 494 ALA A CB  1 
ATOM   3398 N N   . TYR A 1 465 ? 44.390 23.121 13.041 1.00 17.05 ? 495 TYR A N   1 
ATOM   3399 C CA  . TYR A 1 465 ? 44.083 24.392 12.393 1.00 16.94 ? 495 TYR A CA  1 
ATOM   3400 C C   . TYR A 1 465 ? 45.330 25.251 12.231 1.00 20.41 ? 495 TYR A C   1 
ATOM   3401 O O   . TYR A 1 465 ? 45.385 26.102 11.337 1.00 17.43 ? 495 TYR A O   1 
ATOM   3402 C CB  . TYR A 1 465 ? 43.014 25.145 13.190 1.00 15.89 ? 495 TYR A CB  1 
ATOM   3403 C CG  . TYR A 1 465 ? 42.595 26.455 12.559 1.00 16.53 ? 495 TYR A CG  1 
ATOM   3404 C CD1 . TYR A 1 465 ? 41.825 26.471 11.404 1.00 16.74 ? 495 TYR A CD1 1 
ATOM   3405 C CD2 . TYR A 1 465 ? 42.960 27.673 13.122 1.00 16.47 ? 495 TYR A CD2 1 
ATOM   3406 C CE1 . TYR A 1 465 ? 41.434 27.663 10.819 1.00 17.26 ? 495 TYR A CE1 1 
ATOM   3407 C CE2 . TYR A 1 465 ? 42.576 28.872 12.543 1.00 19.47 ? 495 TYR A CE2 1 
ATOM   3408 C CZ  . TYR A 1 465 ? 41.812 28.859 11.390 1.00 23.15 ? 495 TYR A CZ  1 
ATOM   3409 O OH  . TYR A 1 465 ? 41.422 30.039 10.801 1.00 21.53 ? 495 TYR A OH  1 
ATOM   3410 N N   . SER A 1 466 ? 46.342 25.037 13.075 1.00 23.30 ? 496 SER A N   1 
ATOM   3411 C CA  . SER A 1 466 ? 47.586 25.785 12.950 1.00 23.12 ? 496 SER A CA  1 
ATOM   3412 C C   . SER A 1 466 ? 48.325 25.456 11.659 1.00 25.02 ? 496 SER A C   1 
ATOM   3413 O O   . SER A 1 466 ? 49.202 26.223 11.244 1.00 21.17 ? 496 SER A O   1 
ATOM   3414 C CB  . SER A 1 466 ? 48.476 25.512 14.165 1.00 26.50 ? 496 SER A CB  1 
ATOM   3415 O OG  . SER A 1 466 ? 48.628 24.120 14.384 1.00 36.40 ? 496 SER A OG  1 
ATOM   3416 N N   . THR A 1 467 ? 47.983 24.343 11.008 1.00 22.47 ? 497 THR A N   1 
ATOM   3417 C CA  . THR A 1 467 ? 48.583 23.951 9.732  1.00 20.26 ? 497 THR A CA  1 
ATOM   3418 C C   . THR A 1 467 ? 47.682 24.435 8.599  1.00 20.98 ? 497 THR A C   1 
ATOM   3419 O O   . THR A 1 467 ? 46.686 23.788 8.263  1.00 20.67 ? 497 THR A O   1 
ATOM   3420 C CB  . THR A 1 467 ? 48.779 22.439 9.658  1.00 22.29 ? 497 THR A CB  1 
ATOM   3421 O OG1 . THR A 1 467 ? 49.681 22.011 10.686 1.00 22.80 ? 497 THR A OG1 1 
ATOM   3422 C CG2 . THR A 1 467 ? 49.337 22.033 8.301  1.00 23.71 ? 497 THR A CG2 1 
ATOM   3423 N N   . GLY A 1 468 ? 48.027 25.581 8.018  1.00 25.31 ? 498 GLY A N   1 
ATOM   3424 C CA  . GLY A 1 468 ? 47.312 26.081 6.854  1.00 20.48 ? 498 GLY A CA  1 
ATOM   3425 C C   . GLY A 1 468 ? 45.833 26.318 7.066  1.00 25.21 ? 498 GLY A C   1 
ATOM   3426 O O   . GLY A 1 468 ? 45.046 26.152 6.126  1.00 20.32 ? 498 GLY A O   1 
ATOM   3427 N N   . LYS A 1 469 ? 45.432 26.690 8.284  1.00 19.21 ? 499 LYS A N   1 
ATOM   3428 C CA  . LYS A 1 469 ? 44.027 26.929 8.614  1.00 18.73 ? 499 LYS A CA  1 
ATOM   3429 C C   . LYS A 1 469 ? 43.153 25.740 8.235  1.00 20.64 ? 499 LYS A C   1 
ATOM   3430 O O   . LYS A 1 469 ? 41.990 25.905 7.857  1.00 21.66 ? 499 LYS A O   1 
ATOM   3431 C CB  . LYS A 1 469 ? 43.515 28.211 7.953  1.00 22.54 ? 499 LYS A CB  1 
ATOM   3432 C CG  . LYS A 1 469 ? 44.090 29.486 8.555  1.00 28.05 ? 499 LYS A CG  1 
ATOM   3433 C CD  . LYS A 1 469 ? 43.717 30.709 7.728  1.00 25.94 ? 499 LYS A CD  1 
ATOM   3434 C CE  . LYS A 1 469 ? 43.980 31.986 8.508  1.00 38.21 ? 499 LYS A CE  1 
ATOM   3435 N NZ  . LYS A 1 469 ? 45.325 31.974 9.141  1.00 43.23 ? 499 LYS A NZ  1 
ATOM   3436 N N   . SER A 1 470 ? 43.716 24.536 8.325  1.00 20.20 ? 500 SER A N   1 
ATOM   3437 C CA  . SER A 1 470 ? 42.979 23.332 7.964  1.00 19.84 ? 500 SER A CA  1 
ATOM   3438 C C   . SER A 1 470 ? 41.723 23.192 8.816  1.00 21.83 ? 500 SER A C   1 
ATOM   3439 O O   . SER A 1 470 ? 41.773 23.291 10.048 1.00 23.72 ? 500 SER A O   1 
ATOM   3440 C CB  . SER A 1 470 ? 43.872 22.103 8.125  1.00 22.32 ? 500 SER A CB  1 
ATOM   3441 O OG  . SER A 1 470 ? 45.000 22.174 7.268  1.00 19.36 ? 500 SER A OG  1 
ATOM   3442 N N   . THR A 1 471 ? 40.593 22.972 8.150  1.00 20.95 ? 501 THR A N   1 
ATOM   3443 C CA  . THR A 1 471 ? 39.296 22.875 8.802  1.00 18.37 ? 501 THR A CA  1 
ATOM   3444 C C   . THR A 1 471 ? 38.566 21.668 8.240  1.00 21.91 ? 501 THR A C   1 
ATOM   3445 O O   . THR A 1 471 ? 38.388 21.557 7.023  1.00 19.67 ? 501 THR A O   1 
ATOM   3446 C CB  . THR A 1 471 ? 38.474 24.147 8.586  1.00 23.56 ? 501 THR A CB  1 
ATOM   3447 O OG1 . THR A 1 471 ? 39.244 25.291 8.984  1.00 21.06 ? 501 THR A OG1 1 
ATOM   3448 C CG2 . THR A 1 471 ? 37.179 24.099 9.395  1.00 20.09 ? 501 THR A CG2 1 
ATOM   3449 N N   . MET A 1 472 ? 38.154 20.764 9.120  1.00 18.30 ? 502 MET A N   1 
ATOM   3450 C CA  . MET A 1 472 ? 37.396 19.597 8.694  1.00 20.19 ? 502 MET A CA  1 
ATOM   3451 C C   . MET A 1 472 ? 35.961 20.007 8.391  1.00 19.27 ? 502 MET A C   1 
ATOM   3452 O O   . MET A 1 472 ? 35.275 20.569 9.246  1.00 22.02 ? 502 MET A O   1 
ATOM   3453 C CB  . MET A 1 472 ? 37.429 18.525 9.780  1.00 16.40 ? 502 MET A CB  1 
ATOM   3454 C CG  . MET A 1 472 ? 36.596 17.313 9.475  1.00 19.86 ? 502 MET A CG  1 
ATOM   3455 S SD  . MET A 1 472 ? 37.270 16.392 8.085  1.00 24.58 ? 502 MET A SD  1 
ATOM   3456 C CE  . MET A 1 472 ? 38.729 15.688 8.861  1.00 20.09 ? 502 MET A CE  1 
ATOM   3457 N N   . THR A 1 473 ? 35.499 19.726 7.184  1.00 23.09 ? 503 THR A N   1 
ATOM   3458 C CA  . THR A 1 473 ? 34.121 19.974 6.803  1.00 21.84 ? 503 THR A CA  1 
ATOM   3459 C C   . THR A 1 473 ? 33.384 18.644 6.822  1.00 24.62 ? 503 THR A C   1 
ATOM   3460 O O   . THR A 1 473 ? 33.798 17.687 6.153  1.00 26.36 ? 503 THR A O   1 
ATOM   3461 C CB  . THR A 1 473 ? 34.035 20.617 5.421  1.00 23.42 ? 503 THR A CB  1 
ATOM   3462 O OG1 . THR A 1 473 ? 34.384 19.654 4.418  1.00 33.50 ? 503 THR A OG1 1 
ATOM   3463 C CG2 . THR A 1 473 ? 34.979 21.793 5.326  1.00 20.16 ? 503 THR A CG2 1 
ATOM   3464 N N   . PHE A 1 474 ? 32.330 18.573 7.631  1.00 22.78 ? 504 PHE A N   1 
ATOM   3465 C CA  . PHE A 1 474 ? 31.447 17.413 7.646  1.00 27.21 ? 504 PHE A CA  1 
ATOM   3466 C C   . PHE A 1 474 ? 30.357 17.704 6.623  1.00 23.84 ? 504 PHE A C   1 
ATOM   3467 O O   . PHE A 1 474 ? 29.273 18.204 6.926  1.00 22.23 ? 504 PHE A O   1 
ATOM   3468 C CB  . PHE A 1 474 ? 30.922 17.159 9.052  1.00 19.64 ? 504 PHE A CB  1 
ATOM   3469 C CG  . PHE A 1 474 ? 32.018 16.905 10.064 1.00 24.63 ? 504 PHE A CG  1 
ATOM   3470 C CD1 . PHE A 1 474 ? 32.750 15.726 10.036 1.00 21.61 ? 504 PHE A CD1 1 
ATOM   3471 C CD2 . PHE A 1 474 ? 32.317 17.844 11.040 1.00 21.21 ? 504 PHE A CD2 1 
ATOM   3472 C CE1 . PHE A 1 474 ? 33.760 15.490 10.963 1.00 18.74 ? 504 PHE A CE1 1 
ATOM   3473 C CE2 . PHE A 1 474 ? 33.326 17.611 11.971 1.00 21.15 ? 504 PHE A CE2 1 
ATOM   3474 C CZ  . PHE A 1 474 ? 34.049 16.434 11.929 1.00 20.07 ? 504 PHE A CZ  1 
ATOM   3475 N N   . GLY A 1 475 ? 30.687 17.404 5.372  1.00 44.92 ? 505 GLY A N   1 
ATOM   3476 C CA  . GLY A 1 475 ? 29.890 17.823 4.248  1.00 29.82 ? 505 GLY A CA  1 
ATOM   3477 C C   . GLY A 1 475 ? 28.770 16.864 3.951  1.00 38.15 ? 505 GLY A C   1 
ATOM   3478 O O   . GLY A 1 475 ? 28.246 16.179 4.839  1.00 41.52 ? 505 GLY A O   1 
ATOM   3479 N N   . PRO A 1 476 ? 28.383 16.796 2.684  1.00 28.61 ? 506 PRO A N   1 
ATOM   3480 C CA  . PRO A 1 476 ? 27.234 15.978 2.297  1.00 31.55 ? 506 PRO A CA  1 
ATOM   3481 C C   . PRO A 1 476 ? 27.611 14.513 2.127  1.00 32.25 ? 506 PRO A C   1 
ATOM   3482 O O   . PRO A 1 476 ? 28.780 14.127 2.186  1.00 30.34 ? 506 PRO A O   1 
ATOM   3483 C CB  . PRO A 1 476 ? 26.809 16.591 0.963  1.00 34.59 ? 506 PRO A CB  1 
ATOM   3484 C CG  . PRO A 1 476 ? 28.098 17.098 0.378  1.00 35.21 ? 506 PRO A CG  1 
ATOM   3485 C CD  . PRO A 1 476 ? 28.951 17.539 1.542  1.00 32.24 ? 506 PRO A CD  1 
ATOM   3486 N N   . GLU A 1 477 ? 26.574 13.694 1.929  1.00 31.00 ? 507 GLU A N   1 
ATOM   3487 C CA  . GLU A 1 477 ? 26.720 12.279 1.584  1.00 32.80 ? 507 GLU A CA  1 
ATOM   3488 C C   . GLU A 1 477 ? 27.486 11.503 2.648  1.00 29.14 ? 507 GLU A C   1 
ATOM   3489 O O   . GLU A 1 477 ? 28.182 10.531 2.343  1.00 27.60 ? 507 GLU A O   1 
ATOM   3490 C CB  . GLU A 1 477 ? 27.373 12.121 0.209  1.00 34.92 ? 507 GLU A CB  1 
ATOM   3491 C CG  . GLU A 1 477 ? 26.501 12.708 -0.881 1.00 45.34 ? 507 GLU A CG  1 
ATOM   3492 C CD  . GLU A 1 477 ? 27.183 12.776 -2.215 1.00 46.01 ? 507 GLU A CD  1 
ATOM   3493 O OE1 . GLU A 1 477 ? 28.370 12.410 -2.307 1.00 58.37 ? 507 GLU A OE1 1 
ATOM   3494 O OE2 . GLU A 1 477 ? 26.526 13.205 -3.177 1.00 50.11 ? 507 GLU A OE2 1 
ATOM   3495 N N   . GLY A 1 478 ? 27.345 11.925 3.903  1.00 25.70 ? 508 GLY A N   1 
ATOM   3496 C CA  . GLY A 1 478 ? 27.977 11.227 5.007  1.00 24.78 ? 508 GLY A CA  1 
ATOM   3497 C C   . GLY A 1 478 ? 29.484 11.226 4.963  1.00 26.61 ? 508 GLY A C   1 
ATOM   3498 O O   . GLY A 1 478 ? 30.115 10.343 5.554  1.00 29.60 ? 508 GLY A O   1 
ATOM   3499 N N   . ARG A 1 479 ? 30.080 12.208 4.295  1.00 22.41 ? 509 ARG A N   1 
ATOM   3500 C CA  . ARG A 1 479 ? 31.519 12.272 4.114  1.00 32.25 ? 509 ARG A CA  1 
ATOM   3501 C C   . ARG A 1 479 ? 32.096 13.505 4.795  1.00 24.85 ? 509 ARG A C   1 
ATOM   3502 O O   . ARG A 1 479 ? 31.402 14.493 5.039  1.00 26.81 ? 509 ARG A O   1 
ATOM   3503 C CB  . ARG A 1 479 ? 31.898 12.301 2.628  1.00 31.23 ? 509 ARG A CB  1 
ATOM   3504 C CG  . ARG A 1 479 ? 31.393 11.110 1.826  1.00 43.69 ? 509 ARG A CG  1 
ATOM   3505 C CD  . ARG A 1 479 ? 32.207 10.927 0.558  1.00 41.62 ? 509 ARG A CD  1 
ATOM   3506 N NE  . ARG A 1 479 ? 31.451 10.235 -0.476 1.00 55.41 ? 509 ARG A NE  1 
ATOM   3507 C CZ  . ARG A 1 479 ? 30.823 10.844 -1.472 1.00 67.42 ? 509 ARG A CZ  1 
ATOM   3508 N NH1 . ARG A 1 479 ? 30.859 12.160 -1.610 1.00 68.25 ? 509 ARG A NH1 1 
ATOM   3509 N NH2 . ARG A 1 479 ? 30.145 10.115 -2.354 1.00 64.85 ? 509 ARG A NH2 1 
ATOM   3510 N N   . ALA A 1 480 ? 33.392 13.431 5.086  1.00 23.70 ? 510 ALA A N   1 
ATOM   3511 C CA  . ALA A 1 480 ? 34.144 14.519 5.691  1.00 30.27 ? 510 ALA A CA  1 
ATOM   3512 C C   . ALA A 1 480 ? 35.398 14.761 4.867  1.00 28.18 ? 510 ALA A C   1 
ATOM   3513 O O   . ALA A 1 480 ? 35.919 13.842 4.227  1.00 35.55 ? 510 ALA A O   1 
ATOM   3514 C CB  . ALA A 1 480 ? 34.516 14.201 7.142  1.00 22.27 ? 510 ALA A CB  1 
ATOM   3515 N N   . ALA A 1 481 ? 35.876 16.003 4.884  1.00 24.79 ? 511 ALA A N   1 
ATOM   3516 C CA  . ALA A 1 481 ? 37.071 16.329 4.116  1.00 26.23 ? 511 ALA A CA  1 
ATOM   3517 C C   . ALA A 1 481 ? 37.670 17.628 4.633  1.00 25.10 ? 511 ALA A C   1 
ATOM   3518 O O   . ALA A 1 481 ? 36.945 18.539 5.035  1.00 22.58 ? 511 ALA A O   1 
ATOM   3519 C CB  . ALA A 1 481 ? 36.768 16.440 2.614  1.00 23.11 ? 511 ALA A CB  1 
ATOM   3520 N N   . VAL A 1 482 ? 39.000 17.706 4.606  1.00 21.88 ? 512 VAL A N   1 
ATOM   3521 C CA  . VAL A 1 482 ? 39.717 18.878 5.100  1.00 26.08 ? 512 VAL A CA  1 
ATOM   3522 C C   . VAL A 1 482 ? 39.744 19.956 4.024  1.00 22.43 ? 512 VAL A C   1 
ATOM   3523 O O   . VAL A 1 482 ? 39.925 19.668 2.837  1.00 27.46 ? 512 VAL A O   1 
ATOM   3524 C CB  . VAL A 1 482 ? 41.144 18.491 5.533  1.00 27.93 ? 512 VAL A CB  1 
ATOM   3525 C CG1 . VAL A 1 482 ? 41.946 19.725 5.924  1.00 26.38 ? 512 VAL A CG1 1 
ATOM   3526 C CG2 . VAL A 1 482 ? 41.098 17.495 6.681  1.00 22.24 ? 512 VAL A CG2 1 
ATOM   3527 N N   . VAL A 1 483 ? 39.574 21.209 4.439  1.00 25.61 ? 513 VAL A N   1 
ATOM   3528 C CA  . VAL A 1 483 ? 39.694 22.366 3.560  1.00 23.32 ? 513 VAL A CA  1 
ATOM   3529 C C   . VAL A 1 483 ? 40.784 23.273 4.114  1.00 24.11 ? 513 VAL A C   1 
ATOM   3530 O O   . VAL A 1 483 ? 40.798 23.572 5.313  1.00 25.15 ? 513 VAL A O   1 
ATOM   3531 C CB  . VAL A 1 483 ? 38.355 23.116 3.433  1.00 27.52 ? 513 VAL A CB  1 
ATOM   3532 C CG1 . VAL A 1 483 ? 38.555 24.473 2.792  1.00 31.62 ? 513 VAL A CG1 1 
ATOM   3533 C CG2 . VAL A 1 483 ? 37.372 22.289 2.613  1.00 32.46 ? 513 VAL A CG2 1 
ATOM   3534 N N   . SER A 1 484 ? 41.705 23.697 3.246  1.00 24.95 ? 514 SER A N   1 
ATOM   3535 C CA  . SER A 1 484 ? 42.801 24.580 3.627  1.00 28.32 ? 514 SER A CA  1 
ATOM   3536 C C   . SER A 1 484 ? 43.016 25.642 2.554  1.00 28.66 ? 514 SER A C   1 
ATOM   3537 O O   . SER A 1 484 ? 43.348 25.306 1.409  1.00 27.88 ? 514 SER A O   1 
ATOM   3538 C CB  . SER A 1 484 ? 44.085 23.780 3.848  1.00 27.65 ? 514 SER A CB  1 
ATOM   3539 O OG  . SER A 1 484 ? 45.197 24.635 4.050  1.00 35.68 ? 514 SER A OG  1 
ATOM   3540 N N   . PRO A 1 485 ? 42.833 26.933 2.876  1.00 29.82 ? 515 PRO A N   1 
ATOM   3541 C CA  . PRO A 1 485 ? 42.427 27.497 4.171  1.00 26.84 ? 515 PRO A CA  1 
ATOM   3542 C C   . PRO A 1 485 ? 40.940 27.297 4.430  1.00 29.72 ? 515 PRO A C   1 
ATOM   3543 O O   . PRO A 1 485 ? 40.173 27.093 3.501  1.00 34.05 ? 515 PRO A O   1 
ATOM   3544 C CB  . PRO A 1 485 ? 42.789 28.979 4.020  1.00 29.97 ? 515 PRO A CB  1 
ATOM   3545 C CG  . PRO A 1 485 ? 42.557 29.247 2.562  1.00 33.16 ? 515 PRO A CG  1 
ATOM   3546 C CD  . PRO A 1 485 ? 43.020 27.989 1.863  1.00 28.25 ? 515 PRO A CD  1 
ATOM   3547 N N   . GLY A 1 486 ? 40.500 27.364 5.681  1.00 30.11 ? 516 GLY A N   1 
ATOM   3548 C CA  . GLY A 1 486 ? 39.127 27.080 6.019  1.00 28.35 ? 516 GLY A CA  1 
ATOM   3549 C C   . GLY A 1 486 ? 38.217 28.283 5.899  1.00 31.33 ? 516 GLY A C   1 
ATOM   3550 O O   . GLY A 1 486 ? 38.514 29.251 5.193  1.00 34.90 ? 516 GLY A O   1 
ATOM   3551 N N   . PRO A 1 487 ? 37.090 28.244 6.608  1.00 39.56 ? 517 PRO A N   1 
ATOM   3552 C CA  . PRO A 1 487 ? 36.101 29.321 6.493  1.00 44.24 ? 517 PRO A CA  1 
ATOM   3553 C C   . PRO A 1 487 ? 36.652 30.653 6.981  1.00 49.08 ? 517 PRO A C   1 
ATOM   3554 O O   . PRO A 1 487 ? 37.488 30.716 7.887  1.00 45.25 ? 517 PRO A O   1 
ATOM   3555 C CB  . PRO A 1 487 ? 34.947 28.837 7.379  1.00 40.35 ? 517 PRO A CB  1 
ATOM   3556 C CG  . PRO A 1 487 ? 35.596 27.919 8.368  1.00 38.88 ? 517 PRO A CG  1 
ATOM   3557 C CD  . PRO A 1 487 ? 36.702 27.236 7.609  1.00 37.52 ? 517 PRO A CD  1 
ATOM   3558 N N   . SER A 1 488 ? 36.158 31.727 6.370  1.00 53.76 ? 518 SER A N   1 
ATOM   3559 C CA  . SER A 1 488 ? 36.592 33.078 6.691  1.00 57.28 ? 518 SER A CA  1 
ATOM   3560 C C   . SER A 1 488 ? 35.409 34.024 6.558  1.00 56.71 ? 518 SER A C   1 
ATOM   3561 O O   . SER A 1 488 ? 34.686 33.977 5.557  1.00 55.78 ? 518 SER A O   1 
ATOM   3562 C CB  . SER A 1 488 ? 37.734 33.521 5.768  1.00 49.15 ? 518 SER A CB  1 
ATOM   3563 O OG  . SER A 1 488 ? 38.099 34.867 6.013  1.00 56.32 ? 518 SER A OG  1 
ATOM   3564 N N   . ILE A 1 489 ? 35.212 34.872 7.564  1.00 53.22 ? 519 ILE A N   1 
ATOM   3565 C CA  . ILE A 1 489 ? 34.196 35.921 7.496  1.00 54.68 ? 519 ILE A CA  1 
ATOM   3566 C C   . ILE A 1 489 ? 34.647 36.942 6.458  1.00 61.46 ? 519 ILE A C   1 
ATOM   3567 O O   . ILE A 1 489 ? 35.854 37.053 6.189  1.00 56.50 ? 519 ILE A O   1 
ATOM   3568 C CB  . ILE A 1 489 ? 33.969 36.588 8.861  1.00 47.32 ? 519 ILE A CB  1 
ATOM   3569 C CG1 . ILE A 1 489 ? 35.258 37.256 9.345  1.00 57.05 ? 519 ILE A CG1 1 
ATOM   3570 C CG2 . ILE A 1 489 ? 33.459 35.566 9.874  1.00 48.63 ? 519 ILE A CG2 1 
ATOM   3571 C CD1 . ILE A 1 489 ? 35.087 38.077 10.617 1.00 64.28 ? 519 ILE A CD1 1 
ATOM   3572 N N   . PRO A 1 490 ? 33.732 37.688 5.843  1.00 63.64 ? 520 PRO A N   1 
ATOM   3573 C CA  . PRO A 1 490 ? 34.142 38.743 4.906  1.00 60.09 ? 520 PRO A CA  1 
ATOM   3574 C C   . PRO A 1 490 ? 34.996 39.780 5.610  1.00 60.50 ? 520 PRO A C   1 
ATOM   3575 O O   . PRO A 1 490 ? 34.669 40.201 6.730  1.00 57.15 ? 520 PRO A O   1 
ATOM   3576 C CB  . PRO A 1 490 ? 32.808 39.344 4.439  1.00 55.41 ? 520 PRO A CB  1 
ATOM   3577 C CG  . PRO A 1 490 ? 31.800 38.263 4.680  1.00 53.26 ? 520 PRO A CG  1 
ATOM   3578 C CD  . PRO A 1 490 ? 32.265 37.541 5.906  1.00 52.16 ? 520 PRO A CD  1 
ATOM   3579 N N   . PRO A 1 491 ? 36.104 40.202 4.996  1.00 62.84 ? 521 PRO A N   1 
ATOM   3580 C CA  . PRO A 1 491 ? 36.978 41.193 5.649  1.00 62.18 ? 521 PRO A CA  1 
ATOM   3581 C C   . PRO A 1 491 ? 36.277 42.486 6.024  1.00 63.16 ? 521 PRO A C   1 
ATOM   3582 O O   . PRO A 1 491 ? 36.636 43.102 7.037  1.00 59.96 ? 521 PRO A O   1 
ATOM   3583 C CB  . PRO A 1 491 ? 38.082 41.428 4.604  1.00 55.20 ? 521 PRO A CB  1 
ATOM   3584 C CG  . PRO A 1 491 ? 37.559 40.842 3.319  1.00 55.85 ? 521 PRO A CG  1 
ATOM   3585 C CD  . PRO A 1 491 ? 36.665 39.720 3.725  1.00 63.63 ? 521 PRO A CD  1 
ATOM   3586 N N   . CYS A 1 492 ? 35.272 42.910 5.252  1.00 64.63 ? 522 CYS A N   1 
ATOM   3587 C CA  . CYS A 1 492 ? 34.531 44.124 5.581  1.00 58.90 ? 522 CYS A CA  1 
ATOM   3588 C C   . CYS A 1 492 ? 33.723 43.996 6.868  1.00 56.66 ? 522 CYS A C   1 
ATOM   3589 O O   . CYS A 1 492 ? 33.263 45.015 7.396  1.00 53.91 ? 522 CYS A O   1 
ATOM   3590 C CB  . CYS A 1 492 ? 33.601 44.512 4.424  1.00 60.61 ? 522 CYS A CB  1 
ATOM   3591 S SG  . CYS A 1 492 ? 32.632 43.154 3.692  1.00 79.95 ? 522 CYS A SG  1 
ATOM   3592 N N   . ALA A 1 493 ? 33.542 42.784 7.383  1.00 57.43 ? 523 ALA A N   1 
ATOM   3593 C CA  . ALA A 1 493 ? 32.820 42.585 8.634  1.00 59.76 ? 523 ALA A CA  1 
ATOM   3594 C C   . ALA A 1 493 ? 33.785 42.487 9.813  1.00 54.04 ? 523 ALA A C   1 
ATOM   3595 O O   . ALA A 1 493 ? 33.816 41.481 10.522 1.00 48.57 ? 523 ALA A O   1 
ATOM   3596 C CB  . ALA A 1 493 ? 31.950 41.337 8.553  1.00 46.92 ? 523 ALA A CB  1 
HETATM 3597 O O   . HOH B 2 .   ? 8.553  28.751 42.478 1.00 22.86 ? 601 HOH A O   1 
HETATM 3598 O O   . HOH B 2 .   ? 21.761 -2.124 43.392 1.00 35.66 ? 602 HOH A O   1 
HETATM 3599 O O   . HOH B 2 .   ? 11.826 42.219 45.209 1.00 37.21 ? 603 HOH A O   1 
HETATM 3600 O O   . HOH B 2 .   ? 28.510 47.222 30.829 1.00 22.98 ? 604 HOH A O   1 
HETATM 3601 O O   . HOH B 2 .   ? 45.972 30.865 12.023 1.00 45.46 ? 605 HOH A O   1 
HETATM 3602 O O   . HOH B 2 .   ? 20.500 5.660  36.309 1.00 29.51 ? 606 HOH A O   1 
HETATM 3603 O O   . HOH B 2 .   ? 7.270  36.617 31.496 1.00 39.10 ? 607 HOH A O   1 
HETATM 3604 O O   . HOH B 2 .   ? 9.448  36.734 5.853  1.00 39.30 ? 608 HOH A O   1 
HETATM 3605 O O   . HOH B 2 .   ? 11.265 43.314 41.675 1.00 38.47 ? 609 HOH A O   1 
HETATM 3606 O O   . HOH B 2 .   ? 9.202  15.834 28.655 1.00 42.25 ? 610 HOH A O   1 
HETATM 3607 O O   . HOH B 2 .   ? 34.654 39.823 24.166 1.00 22.86 ? 611 HOH A O   1 
HETATM 3608 O O   . HOH B 2 .   ? 18.530 21.679 7.618  1.00 31.15 ? 612 HOH A O   1 
HETATM 3609 O O   . HOH B 2 .   ? 29.558 28.762 9.851  1.00 19.53 ? 613 HOH A O   1 
HETATM 3610 O O   . HOH B 2 .   ? 31.744 -2.582 29.690 1.00 37.31 ? 614 HOH A O   1 
HETATM 3611 O O   . HOH B 2 .   ? 13.520 18.695 15.367 1.00 33.16 ? 615 HOH A O   1 
HETATM 3612 O O   . HOH B 2 .   ? 35.975 9.437  12.375 1.00 17.41 ? 616 HOH A O   1 
HETATM 3613 O O   . HOH B 2 .   ? 51.632 29.037 17.037 1.00 19.16 ? 617 HOH A O   1 
HETATM 3614 O O   . HOH B 2 .   ? 20.289 17.792 46.366 1.00 26.69 ? 618 HOH A O   1 
HETATM 3615 O O   . HOH B 2 .   ? 12.360 15.952 22.712 1.00 41.21 ? 619 HOH A O   1 
HETATM 3616 O O   . HOH B 2 .   ? 21.871 28.134 23.476 1.00 22.34 ? 620 HOH A O   1 
HETATM 3617 O O   . HOH B 2 .   ? 22.237 48.785 20.068 1.00 30.32 ? 621 HOH A O   1 
HETATM 3618 O O   . HOH B 2 .   ? 16.416 23.312 8.560  1.00 31.13 ? 622 HOH A O   1 
HETATM 3619 O O   . HOH B 2 .   ? 22.527 38.147 -2.448 1.00 37.70 ? 623 HOH A O   1 
HETATM 3620 O O   . HOH B 2 .   ? 19.653 41.692 14.581 1.00 34.99 ? 624 HOH A O   1 
HETATM 3621 O O   . HOH B 2 .   ? 38.305 32.076 9.814  1.00 41.73 ? 625 HOH A O   1 
HETATM 3622 O O   . HOH B 2 .   ? 22.450 19.207 44.454 1.00 15.95 ? 626 HOH A O   1 
HETATM 3623 O O   . HOH B 2 .   ? 34.325 5.226  18.302 1.00 25.34 ? 627 HOH A O   1 
HETATM 3624 O O   . HOH B 2 .   ? 31.798 32.761 18.574 1.00 12.05 ? 628 HOH A O   1 
HETATM 3625 O O   . HOH B 2 .   ? 25.576 25.516 47.180 1.00 14.64 ? 629 HOH A O   1 
HETATM 3626 O O   . HOH B 2 .   ? 46.301 9.145  32.721 1.00 29.96 ? 630 HOH A O   1 
HETATM 3627 O O   . HOH B 2 .   ? 43.220 6.390  31.535 1.00 26.05 ? 631 HOH A O   1 
HETATM 3628 O O   . HOH B 2 .   ? 28.706 23.517 15.758 1.00 15.29 ? 632 HOH A O   1 
HETATM 3629 O O   . HOH B 2 .   ? 18.208 28.777 36.853 1.00 18.16 ? 633 HOH A O   1 
HETATM 3630 O O   . HOH B 2 .   ? 28.010 37.402 45.042 1.00 16.96 ? 634 HOH A O   1 
HETATM 3631 O O   . HOH B 2 .   ? 27.188 53.509 6.396  1.00 31.14 ? 635 HOH A O   1 
HETATM 3632 O O   . HOH B 2 .   ? 35.185 -1.743 30.520 1.00 34.04 ? 636 HOH A O   1 
HETATM 3633 O O   . HOH B 2 .   ? 44.459 23.455 -0.041 1.00 26.85 ? 637 HOH A O   1 
HETATM 3634 O O   . HOH B 2 .   ? 5.125  35.102 44.570 1.00 19.53 ? 638 HOH A O   1 
HETATM 3635 O O   . HOH B 2 .   ? 13.531 36.317 2.345  1.00 23.59 ? 639 HOH A O   1 
HETATM 3636 O O   . HOH B 2 .   ? 39.887 13.745 27.716 1.00 16.42 ? 640 HOH A O   1 
HETATM 3637 O O   . HOH B 2 .   ? 15.085 32.537 2.059  1.00 39.50 ? 641 HOH A O   1 
HETATM 3638 O O   . HOH B 2 .   ? 17.947 18.120 48.135 1.00 29.34 ? 642 HOH A O   1 
HETATM 3639 O O   . HOH B 2 .   ? 46.358 35.445 15.447 1.00 46.08 ? 643 HOH A O   1 
HETATM 3640 O O   . HOH B 2 .   ? 16.377 32.930 48.009 1.00 13.79 ? 644 HOH A O   1 
HETATM 3641 O O   . HOH B 2 .   ? 24.349 37.888 22.157 1.00 25.87 ? 645 HOH A O   1 
HETATM 3642 O O   . HOH B 2 .   ? 49.772 33.900 27.748 1.00 31.16 ? 646 HOH A O   1 
HETATM 3643 O O   . HOH B 2 .   ? 41.267 15.473 25.015 1.00 18.96 ? 647 HOH A O   1 
HETATM 3644 O O   . HOH B 2 .   ? 15.680 30.255 47.438 1.00 18.08 ? 648 HOH A O   1 
HETATM 3645 O O   . HOH B 2 .   ? 46.076 15.697 32.431 1.00 29.65 ? 649 HOH A O   1 
HETATM 3646 O O   . HOH B 2 .   ? 25.403 24.061 16.821 1.00 15.29 ? 650 HOH A O   1 
HETATM 3647 O O   . HOH B 2 .   ? 43.496 10.277 17.601 1.00 25.49 ? 651 HOH A O   1 
HETATM 3648 O O   . HOH B 2 .   ? 41.627 21.644 12.120 1.00 15.90 ? 652 HOH A O   1 
HETATM 3649 O O   . HOH B 2 .   ? 11.204 14.099 25.549 1.00 29.67 ? 653 HOH A O   1 
HETATM 3650 O O   . HOH B 2 .   ? 20.701 21.272 44.296 1.00 17.20 ? 654 HOH A O   1 
HETATM 3651 O O   . HOH B 2 .   ? 27.216 5.726  51.932 1.00 29.49 ? 655 HOH A O   1 
HETATM 3652 O O   . HOH B 2 .   ? 26.673 36.236 47.137 1.00 14.55 ? 656 HOH A O   1 
HETATM 3653 O O   . HOH B 2 .   ? 21.203 10.752 43.801 1.00 22.93 ? 657 HOH A O   1 
HETATM 3654 O O   . HOH B 2 .   ? 37.609 26.538 40.177 1.00 23.26 ? 658 HOH A O   1 
HETATM 3655 O O   . HOH B 2 .   ? 20.091 15.097 2.411  1.00 40.64 ? 659 HOH A O   1 
HETATM 3656 O O   . HOH B 2 .   ? 48.250 13.454 18.456 1.00 12.77 ? 660 HOH A O   1 
HETATM 3657 O O   . HOH B 2 .   ? 17.373 17.323 35.484 1.00 15.51 ? 661 HOH A O   1 
HETATM 3658 O O   . HOH B 2 .   ? 11.745 22.901 45.229 1.00 30.43 ? 662 HOH A O   1 
HETATM 3659 O O   . HOH B 2 .   ? 21.808 13.004 19.893 1.00 23.70 ? 663 HOH A O   1 
HETATM 3660 O O   . HOH B 2 .   ? 38.363 36.906 31.236 1.00 15.91 ? 664 HOH A O   1 
HETATM 3661 O O   . HOH B 2 .   ? 13.730 19.173 23.261 1.00 34.23 ? 665 HOH A O   1 
HETATM 3662 O O   . HOH B 2 .   ? 46.832 17.065 21.701 1.00 22.19 ? 666 HOH A O   1 
HETATM 3663 O O   . HOH B 2 .   ? 31.894 37.572 24.696 1.00 16.97 ? 667 HOH A O   1 
HETATM 3664 O O   . HOH B 2 .   ? 37.202 17.619 35.619 1.00 11.74 ? 668 HOH A O   1 
HETATM 3665 O O   . HOH B 2 .   ? 21.063 51.087 40.264 1.00 32.45 ? 669 HOH A O   1 
HETATM 3666 O O   . HOH B 2 .   ? 20.159 22.528 25.761 1.00 23.96 ? 670 HOH A O   1 
HETATM 3667 O O   . HOH B 2 .   ? 51.409 27.657 25.451 1.00 26.90 ? 671 HOH A O   1 
HETATM 3668 O O   . HOH B 2 .   ? 14.119 13.058 40.858 1.00 24.21 ? 672 HOH A O   1 
HETATM 3669 O O   . HOH B 2 .   ? 43.736 15.697 37.458 1.00 24.62 ? 673 HOH A O   1 
HETATM 3670 O O   . HOH B 2 .   ? 22.409 42.536 -8.638 1.00 31.38 ? 674 HOH A O   1 
HETATM 3671 O O   . HOH B 2 .   ? 13.268 22.547 24.467 1.00 30.69 ? 675 HOH A O   1 
HETATM 3672 O O   . HOH B 2 .   ? 24.168 32.580 -4.627 1.00 39.86 ? 676 HOH A O   1 
HETATM 3673 O O   . HOH B 2 .   ? 28.551 23.014 52.713 1.00 39.99 ? 677 HOH A O   1 
HETATM 3674 O O   . HOH B 2 .   ? 20.369 17.641 12.544 1.00 19.35 ? 678 HOH A O   1 
HETATM 3675 O O   . HOH B 2 .   ? 23.441 22.484 23.845 1.00 14.51 ? 679 HOH A O   1 
HETATM 3676 O O   . HOH B 2 .   ? 15.759 21.198 4.934  1.00 27.48 ? 680 HOH A O   1 
HETATM 3677 O O   . HOH B 2 .   ? 40.150 29.587 8.446  1.00 24.30 ? 681 HOH A O   1 
HETATM 3678 O O   . HOH B 2 .   ? 19.541 12.557 28.850 1.00 20.94 ? 682 HOH A O   1 
HETATM 3679 O O   . HOH B 2 .   ? 31.179 10.502 52.011 1.00 29.94 ? 683 HOH A O   1 
HETATM 3680 O O   . HOH B 2 .   ? 20.593 24.071 50.786 1.00 27.06 ? 684 HOH A O   1 
HETATM 3681 O O   . HOH B 2 .   ? 23.882 54.239 6.056  1.00 32.56 ? 685 HOH A O   1 
HETATM 3682 O O   . HOH B 2 .   ? 19.977 35.410 28.155 1.00 22.41 ? 686 HOH A O   1 
HETATM 3683 O O   . HOH B 2 .   ? 25.676 9.284  23.680 1.00 11.64 ? 687 HOH A O   1 
HETATM 3684 O O   . HOH B 2 .   ? 40.304 35.585 39.435 1.00 28.02 ? 688 HOH A O   1 
HETATM 3685 O O   . HOH B 2 .   ? 22.835 7.404  24.095 1.00 19.95 ? 689 HOH A O   1 
HETATM 3686 O O   . HOH B 2 .   ? 17.032 8.471  41.638 1.00 23.14 ? 690 HOH A O   1 
HETATM 3687 O O   . HOH B 2 .   ? 16.553 45.967 36.555 1.00 32.62 ? 691 HOH A O   1 
HETATM 3688 O O   . HOH B 2 .   ? 29.207 51.028 30.449 1.00 39.65 ? 692 HOH A O   1 
HETATM 3689 O O   . HOH B 2 .   ? 17.596 15.469 47.224 1.00 36.56 ? 693 HOH A O   1 
HETATM 3690 O O   . HOH B 2 .   ? 40.734 40.115 20.718 1.00 27.10 ? 694 HOH A O   1 
HETATM 3691 O O   . HOH B 2 .   ? 20.425 5.638  29.486 1.00 26.16 ? 695 HOH A O   1 
HETATM 3692 O O   . HOH B 2 .   ? 18.153 9.785  28.878 1.00 24.25 ? 696 HOH A O   1 
HETATM 3693 O O   . HOH B 2 .   ? 32.585 44.787 28.817 1.00 27.00 ? 697 HOH A O   1 
HETATM 3694 O O   . HOH B 2 .   ? 20.597 16.911 10.337 1.00 24.93 ? 698 HOH A O   1 
HETATM 3695 O O   . HOH B 2 .   ? 23.583 40.364 52.441 1.00 20.66 ? 699 HOH A O   1 
HETATM 3696 O O   . HOH B 2 .   ? 45.709 20.526 5.189  1.00 38.81 ? 700 HOH A O   1 
HETATM 3697 O O   . HOH B 2 .   ? 31.516 7.978  5.618  1.00 37.93 ? 701 HOH A O   1 
HETATM 3698 O O   . HOH B 2 .   ? 25.590 40.311 20.895 1.00 28.18 ? 702 HOH A O   1 
HETATM 3699 O O   . HOH B 2 .   ? 21.107 39.633 35.520 1.00 53.64 ? 703 HOH A O   1 
HETATM 3700 O O   . HOH B 2 .   ? 32.924 26.627 41.534 1.00 17.93 ? 704 HOH A O   1 
HETATM 3701 O O   . HOH B 2 .   ? 7.884  18.463 27.778 1.00 27.41 ? 705 HOH A O   1 
HETATM 3702 O O   . HOH B 2 .   ? 46.157 19.761 27.237 1.00 20.97 ? 706 HOH A O   1 
HETATM 3703 O O   . HOH B 2 .   ? 47.840 23.340 16.913 1.00 16.98 ? 707 HOH A O   1 
HETATM 3704 O O   . HOH B 2 .   ? 14.543 25.712 30.530 1.00 22.06 ? 708 HOH A O   1 
HETATM 3705 O O   . HOH B 2 .   ? 30.961 6.584  8.580  1.00 31.07 ? 709 HOH A O   1 
HETATM 3706 O O   . HOH B 2 .   ? 13.145 27.499 46.065 1.00 15.68 ? 710 HOH A O   1 
HETATM 3707 O O   . HOH B 2 .   ? 30.701 6.482  16.551 1.00 23.06 ? 711 HOH A O   1 
HETATM 3708 O O   . HOH B 2 .   ? 27.775 3.899  20.079 1.00 19.34 ? 712 HOH A O   1 
HETATM 3709 O O   . HOH B 2 .   ? 19.082 14.822 49.802 1.00 42.88 ? 713 HOH A O   1 
HETATM 3710 O O   . HOH B 2 .   ? 21.999 13.732 29.880 1.00 14.80 ? 714 HOH A O   1 
HETATM 3711 O O   . HOH B 2 .   ? 42.627 36.295 17.650 1.00 19.49 ? 715 HOH A O   1 
HETATM 3712 O O   . HOH B 2 .   ? 33.325 29.782 11.207 1.00 31.67 ? 716 HOH A O   1 
HETATM 3713 O O   . HOH B 2 .   ? 21.033 31.286 42.731 1.00 11.27 ? 717 HOH A O   1 
HETATM 3714 O O   . HOH B 2 .   ? 28.235 13.142 44.869 1.00 42.36 ? 718 HOH A O   1 
HETATM 3715 O O   . HOH B 2 .   ? 30.720 55.642 11.792 1.00 44.52 ? 719 HOH A O   1 
HETATM 3716 O O   . HOH B 2 .   ? 38.751 10.902 40.542 1.00 21.72 ? 720 HOH A O   1 
HETATM 3717 O O   . HOH B 2 .   ? 41.596 10.477 42.061 1.00 42.12 ? 721 HOH A O   1 
HETATM 3718 O O   . HOH B 2 .   ? 36.524 5.927  12.717 1.00 36.59 ? 722 HOH A O   1 
HETATM 3719 O O   . HOH B 2 .   ? 17.958 10.660 45.140 1.00 29.05 ? 723 HOH A O   1 
HETATM 3720 O O   . HOH B 2 .   ? 10.330 20.363 41.448 1.00 29.40 ? 724 HOH A O   1 
HETATM 3721 O O   . HOH B 2 .   ? 15.067 36.954 32.069 1.00 32.82 ? 725 HOH A O   1 
HETATM 3722 O O   . HOH B 2 .   ? 26.400 39.218 27.114 1.00 25.04 ? 726 HOH A O   1 
HETATM 3723 O O   . HOH B 2 .   ? 19.476 31.390 5.622  1.00 25.37 ? 727 HOH A O   1 
HETATM 3724 O O   . HOH B 2 .   ? 23.176 49.312 34.105 1.00 31.06 ? 728 HOH A O   1 
HETATM 3725 O O   . HOH B 2 .   ? 24.205 40.588 30.953 1.00 23.53 ? 729 HOH A O   1 
HETATM 3726 O O   . HOH B 2 .   ? 30.128 35.413 25.185 1.00 15.68 ? 730 HOH A O   1 
HETATM 3727 O O   . HOH B 2 .   ? 14.720 19.141 43.610 1.00 17.00 ? 731 HOH A O   1 
HETATM 3728 O O   . HOH B 2 .   ? 25.120 19.346 30.686 1.00 15.99 ? 732 HOH A O   1 
HETATM 3729 O O   . HOH B 2 .   ? 22.241 28.184 28.852 1.00 24.69 ? 733 HOH A O   1 
HETATM 3730 O O   . HOH B 2 .   ? 31.046 35.773 17.146 1.00 19.63 ? 734 HOH A O   1 
HETATM 3731 O O   . HOH B 2 .   ? 51.240 23.786 12.211 1.00 34.03 ? 735 HOH A O   1 
HETATM 3732 O O   . HOH B 2 .   ? 47.516 32.502 14.305 1.00 37.76 ? 736 HOH A O   1 
HETATM 3733 O O   . HOH B 2 .   ? 47.386 23.155 3.080  1.00 37.96 ? 737 HOH A O   1 
HETATM 3734 O O   . HOH B 2 .   ? 24.352 32.030 9.264  1.00 20.45 ? 738 HOH A O   1 
HETATM 3735 O O   . HOH B 2 .   ? 40.577 15.652 3.498  1.00 35.23 ? 739 HOH A O   1 
HETATM 3736 O O   . HOH B 2 .   ? 19.767 15.092 36.981 1.00 17.73 ? 740 HOH A O   1 
HETATM 3737 O O   . HOH B 2 .   ? 29.568 45.406 42.429 1.00 28.51 ? 741 HOH A O   1 
HETATM 3738 O O   . HOH B 2 .   ? 37.609 37.299 14.232 1.00 27.92 ? 742 HOH A O   1 
HETATM 3739 O O   . HOH B 2 .   ? 42.099 1.194  34.972 1.00 47.67 ? 743 HOH A O   1 
HETATM 3740 O O   . HOH B 2 .   ? 15.907 32.993 25.233 1.00 32.88 ? 744 HOH A O   1 
HETATM 3741 O O   . HOH B 2 .   ? 18.972 29.185 43.054 1.00 21.26 ? 745 HOH A O   1 
HETATM 3742 O O   . HOH B 2 .   ? 27.595 8.343  20.104 1.00 26.41 ? 746 HOH A O   1 
HETATM 3743 O O   . HOH B 2 .   ? 21.094 12.642 3.649  1.00 31.18 ? 747 HOH A O   1 
HETATM 3744 O O   . HOH B 2 .   ? 21.957 42.056 37.754 1.00 23.95 ? 748 HOH A O   1 
HETATM 3745 O O   . HOH B 2 .   ? 41.596 23.326 32.370 1.00 20.25 ? 749 HOH A O   1 
HETATM 3746 O O   . HOH B 2 .   ? 41.970 16.201 32.513 1.00 13.92 ? 750 HOH A O   1 
HETATM 3747 O O   . HOH B 2 .   ? 21.089 1.939  51.456 1.00 25.75 ? 751 HOH A O   1 
HETATM 3748 O O   . HOH B 2 .   ? 34.392 26.884 12.148 1.00 19.52 ? 752 HOH A O   1 
HETATM 3749 O O   . HOH B 2 .   ? 38.347 44.359 33.334 1.00 31.82 ? 753 HOH A O   1 
HETATM 3750 O O   . HOH B 2 .   ? 8.745  17.698 34.015 1.00 27.50 ? 754 HOH A O   1 
HETATM 3751 O O   . HOH B 2 .   ? 37.983 5.518  16.037 1.00 25.02 ? 755 HOH A O   1 
HETATM 3752 O O   . HOH B 2 .   ? 18.774 27.368 41.393 1.00 14.30 ? 756 HOH A O   1 
HETATM 3753 O O   . HOH B 2 .   ? 17.964 11.138 41.798 1.00 24.23 ? 757 HOH A O   1 
HETATM 3754 O O   . HOH B 2 .   ? 18.557 22.628 34.263 1.00 16.65 ? 758 HOH A O   1 
HETATM 3755 O O   . HOH B 2 .   ? 46.181 15.772 13.818 1.00 12.39 ? 759 HOH A O   1 
HETATM 3756 O O   . HOH B 2 .   ? 26.908 30.508 9.862  1.00 19.82 ? 760 HOH A O   1 
HETATM 3757 O O   . HOH B 2 .   ? 23.626 15.697 49.713 1.00 27.15 ? 761 HOH A O   1 
HETATM 3758 O O   . HOH B 2 .   ? 40.128 13.577 5.817  1.00 37.74 ? 762 HOH A O   1 
HETATM 3759 O O   . HOH B 2 .   ? 40.886 25.610 39.507 1.00 25.75 ? 763 HOH A O   1 
HETATM 3760 O O   . HOH B 2 .   ? 49.414 26.383 18.004 1.00 16.44 ? 764 HOH A O   1 
HETATM 3761 O O   . HOH B 2 .   ? 36.389 6.683  18.405 1.00 20.20 ? 765 HOH A O   1 
HETATM 3762 O O   . HOH B 2 .   ? 22.612 32.441 5.391  1.00 37.14 ? 766 HOH A O   1 
HETATM 3763 O O   . HOH B 2 .   ? 48.216 13.871 22.788 1.00 32.53 ? 767 HOH A O   1 
HETATM 3764 O O   . HOH B 2 .   ? 25.800 50.653 0.301  1.00 28.27 ? 768 HOH A O   1 
HETATM 3765 O O   . HOH B 2 .   ? 21.750 41.123 23.039 1.00 26.72 ? 769 HOH A O   1 
HETATM 3766 O O   . HOH B 2 .   ? 18.976 -0.437 39.787 1.00 37.43 ? 770 HOH A O   1 
HETATM 3767 O O   . HOH B 2 .   ? 32.731 8.163  50.332 1.00 35.87 ? 771 HOH A O   1 
HETATM 3768 O O   . HOH B 2 .   ? 16.953 23.269 24.931 1.00 35.97 ? 772 HOH A O   1 
HETATM 3769 O O   . HOH B 2 .   ? 26.735 40.306 29.490 1.00 27.43 ? 773 HOH A O   1 
HETATM 3770 O O   . HOH B 2 .   ? 22.420 19.955 6.337  1.00 25.76 ? 774 HOH A O   1 
HETATM 3771 O O   . HOH B 2 .   ? 29.043 45.673 -2.353 1.00 33.95 ? 775 HOH A O   1 
HETATM 3772 O O   . HOH B 2 .   ? 24.883 28.313 46.388 1.00 11.49 ? 776 HOH A O   1 
HETATM 3773 O O   . HOH B 2 .   ? 26.983 33.202 8.886  1.00 30.47 ? 777 HOH A O   1 
HETATM 3774 O O   . HOH B 2 .   ? 25.040 18.836 -1.775 1.00 36.77 ? 778 HOH A O   1 
HETATM 3775 O O   . HOH B 2 .   ? 13.663 52.056 5.219  1.00 31.50 ? 779 HOH A O   1 
HETATM 3776 O O   . HOH B 2 .   ? 13.487 50.073 10.679 1.00 36.69 ? 780 HOH A O   1 
HETATM 3777 O O   . HOH B 2 .   ? 24.468 39.335 35.920 1.00 12.94 ? 781 HOH A O   1 
HETATM 3778 O O   . HOH B 2 .   ? 24.923 -5.901 36.924 1.00 27.55 ? 782 HOH A O   1 
HETATM 3779 O O   . HOH B 2 .   ? 32.149 6.360  10.660 1.00 39.34 ? 783 HOH A O   1 
HETATM 3780 O O   . HOH B 2 .   ? 7.114  35.457 46.568 1.00 16.74 ? 784 HOH A O   1 
HETATM 3781 O O   . HOH B 2 .   ? 15.784 16.910 42.431 1.00 20.82 ? 785 HOH A O   1 
HETATM 3782 O O   . HOH B 2 .   ? 20.046 53.856 5.138  1.00 28.12 ? 786 HOH A O   1 
HETATM 3783 O O   . HOH B 2 .   ? 30.736 14.936 -0.695 1.00 50.51 ? 787 HOH A O   1 
HETATM 3784 O O   . HOH B 2 .   ? 29.023 40.502 18.762 1.00 27.06 ? 788 HOH A O   1 
HETATM 3785 O O   . HOH B 2 .   ? 17.136 27.655 39.210 1.00 18.35 ? 789 HOH A O   1 
HETATM 3786 O O   . HOH B 2 .   ? 27.427 49.978 40.117 1.00 39.31 ? 790 HOH A O   1 
HETATM 3787 O O   . HOH B 2 .   ? 29.860 36.137 42.237 1.00 22.26 ? 791 HOH A O   1 
HETATM 3788 O O   . HOH B 2 .   ? 17.141 26.165 32.844 1.00 26.92 ? 792 HOH A O   1 
HETATM 3789 O O   . HOH B 2 .   ? 19.949 16.451 34.559 1.00 14.08 ? 793 HOH A O   1 
HETATM 3790 O O   . HOH B 2 .   ? 35.428 2.864  20.309 1.00 39.84 ? 794 HOH A O   1 
HETATM 3791 O O   . HOH B 2 .   ? 7.689  45.164 1.948  1.00 42.03 ? 795 HOH A O   1 
HETATM 3792 O O   . HOH B 2 .   ? 44.443 42.966 25.943 1.00 33.04 ? 796 HOH A O   1 
HETATM 3793 O O   . HOH B 2 .   ? 23.336 39.052 33.314 1.00 20.01 ? 797 HOH A O   1 
HETATM 3794 O O   . HOH B 2 .   ? 18.430 47.035 33.396 1.00 36.57 ? 798 HOH A O   1 
HETATM 3795 O O   . HOH B 2 .   ? 14.274 14.127 21.624 1.00 46.55 ? 799 HOH A O   1 
HETATM 3796 O O   . HOH B 2 .   ? 25.177 6.392  13.674 1.00 37.92 ? 800 HOH A O   1 
HETATM 3797 O O   . HOH B 2 .   ? 11.361 27.006 34.760 1.00 33.90 ? 801 HOH A O   1 
HETATM 3798 O O   . HOH B 2 .   ? 18.674 13.369 43.883 1.00 27.81 ? 802 HOH A O   1 
HETATM 3799 O O   . HOH B 2 .   ? 50.326 28.932 11.644 1.00 44.19 ? 803 HOH A O   1 
HETATM 3800 O O   . HOH B 2 .   ? 33.053 42.893 50.346 1.00 42.72 ? 804 HOH A O   1 
HETATM 3801 O O   . HOH B 2 .   ? 33.240 42.110 24.757 1.00 28.06 ? 805 HOH A O   1 
HETATM 3802 O O   . HOH B 2 .   ? 26.229 40.062 23.429 1.00 23.12 ? 806 HOH A O   1 
HETATM 3803 O O   . HOH B 2 .   ? 19.719 19.932 51.562 1.00 33.13 ? 807 HOH A O   1 
HETATM 3804 O O   . HOH B 2 .   ? 21.555 8.188  2.631  1.00 29.26 ? 808 HOH A O   1 
HETATM 3805 O O   . HOH B 2 .   ? 32.896 3.443  43.209 1.00 24.73 ? 809 HOH A O   1 
HETATM 3806 O O   . HOH B 2 .   ? 31.587 49.969 33.823 1.00 26.29 ? 810 HOH A O   1 
HETATM 3807 O O   . HOH B 2 .   ? 44.764 21.028 32.298 1.00 37.53 ? 811 HOH A O   1 
HETATM 3808 O O   . HOH B 2 .   ? 14.903 36.934 52.922 1.00 27.56 ? 812 HOH A O   1 
HETATM 3809 O O   . HOH B 2 .   ? 23.948 5.484  17.507 1.00 35.14 ? 813 HOH A O   1 
HETATM 3810 O O   . HOH B 2 .   ? 32.733 46.828 36.808 1.00 20.42 ? 814 HOH A O   1 
HETATM 3811 O O   . HOH B 2 .   ? 37.074 8.881  42.712 1.00 24.09 ? 815 HOH A O   1 
HETATM 3812 O O   . HOH B 2 .   ? 29.831 18.633 46.650 1.00 25.07 ? 816 HOH A O   1 
HETATM 3813 O O   . HOH B 2 .   ? 23.789 19.038 50.429 1.00 25.51 ? 817 HOH A O   1 
HETATM 3814 O O   . HOH B 2 .   ? 37.756 43.937 29.586 1.00 27.01 ? 818 HOH A O   1 
HETATM 3815 O O   . HOH B 2 .   ? 22.322 46.467 49.132 1.00 36.28 ? 819 HOH A O   1 
HETATM 3816 O O   . HOH B 2 .   ? 26.222 9.536  15.691 1.00 23.02 ? 820 HOH A O   1 
HETATM 3817 O O   . HOH B 2 .   ? 50.755 26.849 7.756  1.00 32.69 ? 821 HOH A O   1 
HETATM 3818 O O   . HOH B 2 .   ? 27.133 43.238 -5.145 1.00 35.15 ? 822 HOH A O   1 
HETATM 3819 O O   . HOH B 2 .   ? 21.929 10.186 1.193  1.00 31.91 ? 823 HOH A O   1 
HETATM 3820 O O   . HOH B 2 .   ? 26.083 37.400 35.733 1.00 12.34 ? 824 HOH A O   1 
HETATM 3821 O O   . HOH B 2 .   ? 8.133  23.246 28.820 1.00 26.56 ? 825 HOH A O   1 
HETATM 3822 O O   . HOH B 2 .   ? 24.941 46.753 -1.510 1.00 31.76 ? 826 HOH A O   1 
HETATM 3823 O O   . HOH B 2 .   ? 29.701 52.312 33.806 1.00 38.47 ? 827 HOH A O   1 
HETATM 3824 O O   . HOH B 2 .   ? 31.404 30.759 48.879 1.00 31.44 ? 828 HOH A O   1 
HETATM 3825 O O   . HOH B 2 .   ? 33.326 34.565 45.069 1.00 27.98 ? 829 HOH A O   1 
HETATM 3826 O O   . HOH B 2 .   ? 25.074 3.899  7.053  1.00 32.75 ? 830 HOH A O   1 
HETATM 3827 O O   . HOH B 2 .   ? 22.233 0.456  28.829 1.00 44.59 ? 831 HOH A O   1 
HETATM 3828 O O   . HOH B 2 .   ? 28.658 47.109 46.708 1.00 36.20 ? 832 HOH A O   1 
HETATM 3829 O O   . HOH B 2 .   ? 11.733 47.248 39.644 1.00 35.92 ? 833 HOH A O   1 
HETATM 3830 O O   . HOH B 2 .   ? 22.273 45.724 -1.329 1.00 26.86 ? 834 HOH A O   1 
HETATM 3831 O O   . HOH B 2 .   ? 18.937 -1.753 36.968 1.00 37.08 ? 835 HOH A O   1 
HETATM 3832 O O   . HOH B 2 .   ? 17.688 8.331  24.637 1.00 32.74 ? 836 HOH A O   1 
HETATM 3833 O O   . HOH B 2 .   ? 33.944 45.065 35.259 1.00 32.39 ? 837 HOH A O   1 
HETATM 3834 O O   . HOH B 2 .   ? 19.648 22.274 10.502 1.00 22.57 ? 838 HOH A O   1 
HETATM 3835 O O   . HOH B 2 .   ? 10.666 18.068 40.651 1.00 31.72 ? 839 HOH A O   1 
HETATM 3836 O O   . HOH B 2 .   ? 5.832  38.014 38.879 1.00 23.82 ? 840 HOH A O   1 
HETATM 3837 O O   . HOH B 2 .   ? 27.773 58.787 9.730  1.00 44.16 ? 841 HOH A O   1 
HETATM 3838 O O   . HOH B 2 .   ? 33.460 4.592  13.149 1.00 36.60 ? 842 HOH A O   1 
HETATM 3839 O O   . HOH B 2 .   ? 32.000 44.067 25.946 1.00 23.02 ? 843 HOH A O   1 
HETATM 3840 O O   . HOH B 2 .   ? 31.606 23.649 46.116 1.00 40.49 ? 844 HOH A O   1 
HETATM 3841 O O   . HOH B 2 .   ? 13.810 49.155 45.545 1.00 35.61 ? 845 HOH A O   1 
HETATM 3842 O O   . HOH B 2 .   ? 20.617 8.306  51.650 1.00 30.12 ? 846 HOH A O   1 
HETATM 3843 O O   . HOH B 2 .   ? 13.099 52.003 8.676  1.00 33.27 ? 847 HOH A O   1 
HETATM 3844 O O   . HOH B 2 .   ? 45.920 13.901 10.860 1.00 24.29 ? 848 HOH A O   1 
HETATM 3845 O O   . HOH B 2 .   ? 9.019  29.860 27.346 1.00 34.31 ? 849 HOH A O   1 
HETATM 3846 O O   . HOH B 2 .   ? 52.464 23.675 23.557 1.00 30.89 ? 850 HOH A O   1 
HETATM 3847 O O   . HOH B 2 .   ? 31.132 16.245 45.997 1.00 37.89 ? 851 HOH A O   1 
HETATM 3848 O O   . HOH B 2 .   ? 16.282 22.018 49.065 1.00 45.17 ? 852 HOH A O   1 
HETATM 3849 O O   . HOH B 2 .   ? 17.534 13.543 3.299  1.00 36.02 ? 853 HOH A O   1 
HETATM 3850 O O   . HOH B 2 .   ? 12.420 25.959 44.263 1.00 16.83 ? 854 HOH A O   1 
HETATM 3851 O O   . HOH B 2 .   ? 37.422 40.801 19.323 1.00 36.77 ? 855 HOH A O   1 
HETATM 3852 O O   . HOH B 2 .   ? 38.932 18.713 0.019  1.00 37.80 ? 856 HOH A O   1 
HETATM 3853 O O   . HOH B 2 .   ? 18.938 6.265  50.947 1.00 25.72 ? 857 HOH A O   1 
HETATM 3854 O O   . HOH B 2 .   ? 27.021 4.516  55.205 1.00 29.92 ? 858 HOH A O   1 
HETATM 3855 O O   . HOH B 2 .   ? 41.118 10.727 5.291  1.00 33.61 ? 859 HOH A O   1 
HETATM 3856 O O   . HOH B 2 .   ? 19.378 4.840  8.110  1.00 31.70 ? 860 HOH A O   1 
HETATM 3857 O O   . HOH B 2 .   ? 23.472 42.747 32.969 1.00 26.35 ? 861 HOH A O   1 
HETATM 3858 O O   . HOH B 2 .   ? 17.886 46.226 0.199  1.00 30.31 ? 862 HOH A O   1 
HETATM 3859 O O   . HOH B 2 .   ? 30.179 45.787 7.477  1.00 34.73 ? 863 HOH A O   1 
HETATM 3860 O O   . HOH B 2 .   ? 19.612 38.825 51.292 1.00 28.26 ? 864 HOH A O   1 
HETATM 3861 O O   . HOH B 2 .   ? 25.858 16.299 -2.822 1.00 35.96 ? 865 HOH A O   1 
HETATM 3862 O O   . HOH B 2 .   ? 22.193 17.733 8.114  1.00 27.92 ? 866 HOH A O   1 
HETATM 3863 O O   . HOH B 2 .   ? 45.057 23.989 32.956 1.00 37.13 ? 867 HOH A O   1 
HETATM 3864 O O   . HOH B 2 .   ? 19.446 42.157 36.170 1.00 55.22 ? 868 HOH A O   1 
HETATM 3865 O O   . HOH B 2 .   ? 17.467 32.247 6.412  1.00 37.74 ? 869 HOH A O   1 
HETATM 3866 O O   . HOH B 2 .   ? 35.080 9.030  45.071 1.00 35.94 ? 870 HOH A O   1 
HETATM 3867 O O   . HOH B 2 .   ? 8.618  20.406 29.487 1.00 27.18 ? 871 HOH A O   1 
HETATM 3868 O O   . HOH B 2 .   ? 42.654 0.000  37.947 0.50 33.60 ? 872 HOH A O   1 
HETATM 3869 O O   . HOH B 2 .   ? 16.818 14.871 43.884 1.00 29.14 ? 873 HOH A O   1 
HETATM 3870 O O   . HOH B 2 .   ? 34.026 31.314 44.086 1.00 26.33 ? 874 HOH A O   1 
HETATM 3871 O O   . HOH B 2 .   ? 28.645 42.691 12.302 1.00 38.99 ? 875 HOH A O   1 
HETATM 3872 O O   . HOH B 2 .   ? 22.837 47.579 27.024 1.00 35.38 ? 876 HOH A O   1 
HETATM 3873 O O   . HOH B 2 .   ? 10.734 46.548 -1.747 1.00 35.36 ? 877 HOH A O   1 
HETATM 3874 O O   . HOH B 2 .   ? 20.951 40.630 52.918 1.00 36.09 ? 878 HOH A O   1 
HETATM 3875 O O   . HOH B 2 .   ? 39.890 36.256 13.505 1.00 23.99 ? 879 HOH A O   1 
HETATM 3876 O O   . HOH B 2 .   ? 21.679 38.459 23.317 1.00 23.00 ? 880 HOH A O   1 
HETATM 3877 O O   . HOH B 2 .   ? 32.167 45.819 43.278 1.00 39.58 ? 881 HOH A O   1 
HETATM 3878 O O   . HOH B 2 .   ? 43.783 18.317 33.277 1.00 41.81 ? 882 HOH A O   1 
HETATM 3879 O O   . HOH B 2 .   ? 30.138 35.336 44.944 1.00 21.53 ? 883 HOH A O   1 
HETATM 3880 O O   . HOH B 2 .   ? 23.328 45.243 -4.527 1.00 37.89 ? 884 HOH A O   1 
HETATM 3881 O O   . HOH B 2 .   ? 37.839 45.519 27.209 1.00 38.23 ? 885 HOH A O   1 
HETATM 3882 O O   . HOH B 2 .   ? 13.905 49.294 -0.390 1.00 36.06 ? 886 HOH A O   1 
HETATM 3883 O O   . HOH B 2 .   ? 8.406  46.054 -0.951 1.00 43.28 ? 887 HOH A O   1 
HETATM 3884 O O   . HOH B 2 .   ? 21.877 46.253 29.077 1.00 48.12 ? 888 HOH A O   1 
HETATM 3885 O O   . HOH B 2 .   ? 21.838 4.945  22.712 1.00 29.23 ? 889 HOH A O   1 
HETATM 3886 O O   . HOH B 2 .   ? 32.746 31.001 8.822  1.00 38.78 ? 890 HOH A O   1 
HETATM 3887 O O   . HOH B 2 .   ? 23.258 35.170 -8.714 1.00 34.21 ? 891 HOH A O   1 
HETATM 3888 O O   . HOH B 2 .   ? 34.304 24.550 42.512 1.00 22.92 ? 892 HOH A O   1 
HETATM 3889 O O   . HOH B 2 .   ? 30.591 47.077 40.917 1.00 30.37 ? 893 HOH A O   1 
HETATM 3890 O O   . HOH B 2 .   ? 36.423 6.871  10.570 1.00 36.21 ? 894 HOH A O   1 
HETATM 3891 O O   . HOH B 2 .   ? 38.877 23.825 41.220 1.00 45.52 ? 895 HOH A O   1 
HETATM 3892 O O   . HOH B 2 .   ? 38.186 6.461  43.931 1.00 29.86 ? 896 HOH A O   1 
HETATM 3893 O O   . HOH B 2 .   ? 29.294 35.361 47.910 1.00 28.24 ? 897 HOH A O   1 
HETATM 3894 O O   . HOH B 2 .   ? 11.665 33.312 26.216 1.00 54.91 ? 898 HOH A O   1 
HETATM 3895 O O   . HOH B 2 .   ? 46.392 9.971  17.776 1.00 35.55 ? 899 HOH A O   1 
HETATM 3896 O O   . HOH B 2 .   ? 44.458 2.021  39.549 1.00 31.99 ? 900 HOH A O   1 
HETATM 3897 O O   . HOH B 2 .   ? 33.155 47.482 39.303 1.00 33.84 ? 901 HOH A O   1 
HETATM 3898 O O   . HOH B 2 .   ? 29.333 44.794 13.038 1.00 39.07 ? 902 HOH A O   1 
HETATM 3899 O O   . HOH B 2 .   ? 16.492 48.876 -1.248 1.00 36.17 ? 903 HOH A O   1 
HETATM 3900 O O   . HOH B 2 .   ? 47.290 26.524 30.959 1.00 35.25 ? 904 HOH A O   1 
HETATM 3901 O O   . HOH B 2 .   ? 6.211  24.704 27.278 1.00 30.19 ? 905 HOH A O   1 
HETATM 3902 O O   . HOH B 2 .   ? 24.229 56.231 4.339  1.00 39.16 ? 906 HOH A O   1 
HETATM 3903 O O   . HOH B 2 .   ? 29.617 33.054 49.389 1.00 27.47 ? 907 HOH A O   1 
HETATM 3904 O O   . HOH B 2 .   ? 32.788 16.257 1.222  1.00 30.80 ? 908 HOH A O   1 
HETATM 3905 O O   . HOH B 2 .   ? 37.665 39.957 14.999 1.00 33.58 ? 909 HOH A O   1 
HETATM 3906 O O   . HOH B 2 .   ? 34.775 44.549 23.405 1.00 39.05 ? 910 HOH A O   1 
HETATM 3907 O O   . HOH B 2 .   ? 10.002 26.243 43.396 1.00 20.87 ? 911 HOH A O   1 
HETATM 3908 O O   . HOH B 2 .   ? 35.093 44.990 30.909 1.00 29.28 ? 912 HOH A O   1 
HETATM 3909 O O   . HOH B 2 .   ? 29.685 5.990  3.999  1.00 37.22 ? 913 HOH A O   1 
HETATM 3910 O O   . HOH B 2 .   ? 18.056 22.619 51.171 1.00 30.51 ? 914 HOH A O   1 
HETATM 3911 O O   . HOH B 2 .   ? 29.774 49.884 41.028 1.00 43.06 ? 915 HOH A O   1 
HETATM 3912 O O   . HOH B 2 .   ? 47.048 20.179 30.090 1.00 27.62 ? 916 HOH A O   1 
HETATM 3913 O O   . HOH B 2 .   ? 33.933 32.532 46.746 1.00 31.88 ? 917 HOH A O   1 
HETATM 3914 O O   . HOH B 2 .   ? 35.366 27.987 41.004 1.00 21.00 ? 918 HOH A O   1 
HETATM 3915 O O   . HOH B 2 .   ? 33.508 23.085 44.594 1.00 41.43 ? 919 HOH A O   1 
HETATM 3916 O O   . HOH B 2 .   ? 48.246 18.970 5.372  1.00 44.69 ? 920 HOH A O   1 
HETATM 3917 O O   . HOH B 2 .   ? 35.777 45.545 33.159 1.00 33.43 ? 921 HOH A O   1 
HETATM 3918 O O   . HOH B 2 .   ? 42.654 0.000  41.107 0.50 38.43 ? 922 HOH A O   1 
HETATM 3919 O O   . HOH B 2 .   ? 31.450 46.041 23.655 1.00 39.54 ? 923 HOH A O   1 
HETATM 3920 O O   . HOH B 2 .   ? 35.584 48.109 33.560 1.00 32.44 ? 924 HOH A O   1 
HETATM 3921 O O   . HOH B 2 .   ? 8.741  32.220 25.526 1.00 48.52 ? 925 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 9   ? 0.6586 0.5001 0.6546 0.0297  0.0375  0.0013  39  ASP A N   
2    C CA  . ASP A 9   ? 0.6131 0.4687 0.6098 0.0312  0.0332  0.0047  39  ASP A CA  
3    C C   . ASP A 9   ? 0.5930 0.4548 0.5887 0.0243  0.0312  0.0037  39  ASP A C   
4    O O   . ASP A 9   ? 0.5933 0.4572 0.5892 0.0189  0.0307  -0.0019 39  ASP A O   
5    C CB  . ASP A 9   ? 0.7240 0.5897 0.7224 0.0346  0.0309  0.0021  39  ASP A CB  
6    C CG  . ASP A 9   ? 0.7317 0.6082 0.7314 0.0393  0.0273  0.0072  39  ASP A CG  
7    O OD1 . ASP A 9   ? 0.6817 0.5649 0.6801 0.0367  0.0246  0.0094  39  ASP A OD1 
8    O OD2 . ASP A 9   ? 0.7909 0.6692 0.7930 0.0455  0.0272  0.0092  39  ASP A OD2 
9    N N   . PHE A 10  ? 0.4609 0.3261 0.4558 0.0248  0.0300  0.0093  40  PHE A N   
10   C CA  . PHE A 10  ? 0.3945 0.2648 0.3888 0.0191  0.0290  0.0094  40  PHE A CA  
11   C C   . PHE A 10  ? 0.3436 0.2281 0.3384 0.0185  0.0249  0.0075  40  PHE A C   
12   O O   . PHE A 10  ? 0.3471 0.2380 0.3421 0.0232  0.0226  0.0085  40  PHE A O   
13   C CB  . PHE A 10  ? 0.3604 0.2279 0.3527 0.0204  0.0301  0.0164  40  PHE A CB  
14   C CG  . PHE A 10  ? 0.4121 0.2652 0.4039 0.0208  0.0344  0.0191  40  PHE A CG  
15   C CD1 . PHE A 10  ? 0.4392 0.2853 0.4304 0.0274  0.0357  0.0223  40  PHE A CD1 
16   C CD2 . PHE A 10  ? 0.3693 0.2158 0.3616 0.0146  0.0372  0.0186  40  PHE A CD2 
17   C CE1 . PHE A 10  ? 0.5706 0.4024 0.5612 0.0280  0.0399  0.0251  40  PHE A CE1 
18   C CE2 . PHE A 10  ? 0.4172 0.2494 0.4089 0.0146  0.0415  0.0212  40  PHE A CE2 
19   C CZ  . PHE A 10  ? 0.4566 0.2810 0.4472 0.0214  0.0429  0.0245  40  PHE A CZ  
20   N N   . PRO A 11  ? 0.3558 0.2457 0.3514 0.0126  0.0240  0.0051  41  PRO A N   
21   C CA  . PRO A 11  ? 0.3440 0.2466 0.3401 0.0119  0.0205  0.0035  41  PRO A CA  
22   C C   . PRO A 11  ? 0.3202 0.2289 0.3144 0.0141  0.0189  0.0083  41  PRO A C   
23   O O   . PRO A 11  ? 0.3008 0.2162 0.2952 0.0111  0.0179  0.0082  41  PRO A O   
24   C CB  . PRO A 11  ? 0.3605 0.2651 0.3583 0.0050  0.0205  -0.0005 41  PRO A CB  
25   C CG  . PRO A 11  ? 0.3526 0.2481 0.3508 0.0019  0.0238  0.0015  41  PRO A CG  
26   C CD  . PRO A 11  ? 0.4014 0.2857 0.3980 0.0062  0.0263  0.0035  41  PRO A CD  
27   N N   . VAL A 12  ? 0.2782 0.1845 0.2704 0.0195  0.0188  0.0127  42  VAL A N   
28   C CA  . VAL A 12  ? 0.3022 0.2138 0.2914 0.0221  0.0169  0.0171  42  VAL A CA  
29   C C   . VAL A 12  ? 0.2690 0.1858 0.2582 0.0273  0.0138  0.0176  42  VAL A C   
30   O O   . VAL A 12  ? 0.3136 0.2260 0.3042 0.0310  0.0144  0.0182  42  VAL A O   
31   C CB  . VAL A 12  ? 0.2767 0.1807 0.2627 0.0233  0.0194  0.0228  42  VAL A CB  
32   C CG1 . VAL A 12  ? 0.2751 0.1843 0.2566 0.0265  0.0172  0.0272  42  VAL A CG1 
33   C CG2 . VAL A 12  ? 0.2937 0.1938 0.2805 0.0176  0.0226  0.0225  42  VAL A CG2 
34   N N   . ARG A 13  ? 0.2813 0.2075 0.2695 0.0275  0.0107  0.0172  43  ARG A N   
35   C CA  . ARG A 13  ? 0.3047 0.2371 0.2937 0.0315  0.0074  0.0174  43  ARG A CA  
36   C C   . ARG A 13  ? 0.3310 0.2692 0.3160 0.0327  0.0046  0.0203  43  ARG A C   
37   O O   . ARG A 13  ? 0.3507 0.2907 0.3330 0.0297  0.0049  0.0201  43  ARG A O   
38   C CB  . ARG A 13  ? 0.3204 0.2588 0.3131 0.0300  0.0062  0.0122  43  ARG A CB  
39   C CG  . ARG A 13  ? 0.3775 0.3105 0.3732 0.0297  0.0086  0.0091  43  ARG A CG  
40   C CD  . ARG A 13  ? 0.3692 0.2980 0.3663 0.0351  0.0093  0.0116  43  ARG A CD  
41   N NE  . ARG A 13  ? 0.4603 0.3831 0.4598 0.0353  0.0122  0.0083  43  ARG A NE  
42   C CZ  . ARG A 13  ? 0.5396 0.4516 0.5384 0.0346  0.0156  0.0083  43  ARG A CZ  
43   N NH1 . ARG A 13  ? 0.4890 0.3953 0.4853 0.0335  0.0169  0.0119  43  ARG A NH1 
44   N NH2 . ARG A 13  ? 0.5682 0.4745 0.5684 0.0348  0.0182  0.0046  43  ARG A NH2 
45   N N   . ARG A 14  ? 0.3410 0.2824 0.3258 0.0369  0.0017  0.0226  44  ARG A N   
46   C CA  . ARG A 14  ? 0.3131 0.2594 0.2933 0.0382  -0.0014 0.0253  44  ARG A CA  
47   C C   . ARG A 14  ? 0.3101 0.2655 0.2922 0.0374  -0.0048 0.0220  44  ARG A C   
48   O O   . ARG A 14  ? 0.2664 0.2259 0.2526 0.0398  -0.0069 0.0215  44  ARG A O   
49   C CB  . ARG A 14  ? 0.3060 0.2504 0.2844 0.0432  -0.0030 0.0305  44  ARG A CB  
50   C CG  . ARG A 14  ? 0.3169 0.2668 0.2898 0.0444  -0.0070 0.0329  44  ARG A CG  
51   C CD  . ARG A 14  ? 0.3219 0.2697 0.2922 0.0492  -0.0086 0.0388  44  ARG A CD  
52   N NE  . ARG A 14  ? 0.4129 0.3510 0.3801 0.0498  -0.0046 0.0425  44  ARG A NE  
53   C CZ  . ARG A 14  ? 0.4750 0.4095 0.4349 0.0484  -0.0031 0.0450  44  ARG A CZ  
54   N NH1 . ARG A 14  ? 0.4607 0.4000 0.4151 0.0464  -0.0051 0.0440  44  ARG A NH1 
55   N NH2 . ARG A 14  ? 0.5088 0.4342 0.4669 0.0489  0.0009  0.0487  44  ARG A NH2 
56   N N   . THR A 15  ? 0.3039 0.2625 0.2836 0.0340  -0.0051 0.0199  45  THR A N   
57   C CA  . THR A 15  ? 0.2734 0.2397 0.2535 0.0334  -0.0084 0.0175  45  THR A CA  
58   C C   . THR A 15  ? 0.2761 0.2448 0.2511 0.0355  -0.0118 0.0205  45  THR A C   
59   O O   . THR A 15  ? 0.2564 0.2209 0.2265 0.0373  -0.0114 0.0244  45  THR A O   
60   C CB  . THR A 15  ? 0.3322 0.3004 0.3115 0.0295  -0.0072 0.0144  45  THR A CB  
61   O OG1 . THR A 15  ? 0.2879 0.2547 0.2607 0.0289  -0.0069 0.0163  45  THR A OG1 
62   C CG2 . THR A 15  ? 0.2645 0.2292 0.2471 0.0270  -0.0037 0.0125  45  THR A CG2 
63   N N   . ASP A 16  ? 0.2840 0.2593 0.2597 0.0351  -0.0153 0.0186  46  ASP A N   
64   C CA  . ASP A 16  ? 0.3331 0.3113 0.3036 0.0364  -0.0192 0.0207  46  ASP A CA  
65   C C   . ASP A 16  ? 0.3651 0.3400 0.3269 0.0349  -0.0182 0.0213  46  ASP A C   
66   O O   . ASP A 16  ? 0.3773 0.3528 0.3326 0.0360  -0.0210 0.0234  46  ASP A O   
67   C CB  . ASP A 16  ? 0.2985 0.2842 0.2722 0.0353  -0.0229 0.0179  46  ASP A CB  
68   C CG  . ASP A 16  ? 0.3778 0.3646 0.3521 0.0317  -0.0215 0.0137  46  ASP A CG  
69   O OD1 . ASP A 16  ? 0.4010 0.3839 0.3747 0.0302  -0.0177 0.0128  46  ASP A OD1 
70   O OD2 . ASP A 16  ? 0.5429 0.5347 0.5185 0.0303  -0.0241 0.0116  46  ASP A OD2 
71   N N   . LEU A 17  ? 0.2859 0.2576 0.2473 0.0324  -0.0142 0.0197  47  LEU A N   
72   C CA  . LEU A 17  ? 0.3693 0.3376 0.3231 0.0313  -0.0121 0.0207  47  LEU A CA  
73   C C   . LEU A 17  ? 0.3140 0.2759 0.2659 0.0319  -0.0083 0.0242  47  LEU A C   
74   O O   . LEU A 17  ? 0.3560 0.3150 0.3016 0.0312  -0.0059 0.0256  47  LEU A O   
75   C CB  . LEU A 17  ? 0.3707 0.3408 0.3259 0.0282  -0.0102 0.0170  47  LEU A CB  
76   C CG  . LEU A 17  ? 0.4260 0.4012 0.3822 0.0271  -0.0132 0.0135  47  LEU A CG  
77   C CD1 . LEU A 17  ? 0.4299 0.4065 0.3897 0.0245  -0.0107 0.0104  47  LEU A CD1 
78   C CD2 . LEU A 17  ? 0.4229 0.3982 0.3706 0.0275  -0.0157 0.0138  47  LEU A CD2 
79   N N   . GLY A 18  ? 0.2772 0.2363 0.2341 0.0332  -0.0072 0.0257  48  GLY A N   
80   C CA  . GLY A 18  ? 0.2962 0.2483 0.2519 0.0332  -0.0031 0.0288  48  GLY A CA  
81   C C   . GLY A 18  ? 0.3184 0.2677 0.2815 0.0317  -0.0003 0.0271  48  GLY A C   
82   O O   . GLY A 18  ? 0.3211 0.2741 0.2898 0.0306  -0.0013 0.0233  48  GLY A O   
83   N N   . GLN A 19  ? 0.3228 0.2651 0.2856 0.0314  0.0033  0.0298  49  GLN A N   
84   C CA  . GLN A 19  ? 0.2729 0.2114 0.2420 0.0297  0.0059  0.0280  49  GLN A CA  
85   C C   . GLN A 19  ? 0.3197 0.2599 0.2918 0.0250  0.0081  0.0245  49  GLN A C   
86   O O   . GLN A 19  ? 0.3214 0.2632 0.2906 0.0232  0.0095  0.0252  49  GLN A O   
87   C CB  . GLN A 19  ? 0.3127 0.2421 0.2805 0.0310  0.0089  0.0323  49  GLN A CB  
88   C CG  . GLN A 19  ? 0.3309 0.2585 0.2962 0.0362  0.0068  0.0365  49  GLN A CG  
89   C CD  . GLN A 19  ? 0.4006 0.3183 0.3650 0.0377  0.0102  0.0409  49  GLN A CD  
90   O OE1 . GLN A 19  ? 0.3922 0.3045 0.3613 0.0381  0.0120  0.0400  49  GLN A OE1 
91   N NE2 . GLN A 19  ? 0.5025 0.4169 0.4600 0.0387  0.0113  0.0459  49  GLN A NE2 
92   N N   . VAL A 20  ? 0.2524 0.1925 0.2304 0.0230  0.0086  0.0209  50  VAL A N   
93   C CA  . VAL A 20  ? 0.2596 0.2017 0.2413 0.0185  0.0102  0.0176  50  VAL A CA  
94   C C   . VAL A 20  ? 0.2843 0.2199 0.2697 0.0164  0.0127  0.0164  50  VAL A C   
95   O O   . VAL A 20  ? 0.2926 0.2238 0.2789 0.0187  0.0125  0.0163  50  VAL A O   
96   C CB  . VAL A 20  ? 0.2440 0.1939 0.2283 0.0177  0.0075  0.0134  50  VAL A CB  
97   C CG1 . VAL A 20  ? 0.2261 0.1815 0.2067 0.0188  0.0056  0.0141  50  VAL A CG1 
98   C CG2 . VAL A 20  ? 0.2383 0.1885 0.2250 0.0199  0.0056  0.0114  50  VAL A CG2 
99   N N   . GLN A 21  ? 0.2614 0.1964 0.2492 0.0119  0.0150  0.0155  51  GLN A N   
100  C CA  . GLN A 21  ? 0.2672 0.1962 0.2586 0.0087  0.0172  0.0136  51  GLN A CA  
101  C C   . GLN A 21  ? 0.3076 0.2423 0.3032 0.0048  0.0159  0.0086  51  GLN A C   
102  O O   . GLN A 21  ? 0.2578 0.1990 0.2549 0.0022  0.0156  0.0081  51  GLN A O   
103  C CB  . GLN A 21  ? 0.2899 0.2134 0.2814 0.0058  0.0209  0.0168  51  GLN A CB  
104  C CG  . GLN A 21  ? 0.3559 0.2735 0.3515 0.0013  0.0228  0.0140  51  GLN A CG  
105  C CD  . GLN A 21  ? 0.3926 0.3045 0.3892 -0.0021 0.0268  0.0172  51  GLN A CD  
106  O OE1 . GLN A 21  ? 0.3499 0.2518 0.3452 -0.0013 0.0292  0.0196  51  GLN A OE1 
107  N NE2 . GLN A 21  ? 0.4058 0.3239 0.4050 -0.0058 0.0276  0.0175  51  GLN A NE2 
108  N N   . GLY A 22  ? 0.2518 0.1838 0.2489 0.0046  0.0152  0.0050  52  GLY A N   
109  C CA  . GLY A 22  ? 0.2922 0.2288 0.2923 0.0008  0.0140  0.0002  52  GLY A CA  
110  C C   . GLY A 22  ? 0.2962 0.2266 0.2985 -0.0040 0.0159  -0.0022 52  GLY A C   
111  O O   . GLY A 22  ? 0.3052 0.2296 0.3080 -0.0058 0.0185  0.0002  52  GLY A O   
112  N N   . LEU A 23  ? 0.2904 0.2219 0.2938 -0.0062 0.0146  -0.0071 53  LEU A N   
113  C CA  . LEU A 23  ? 0.3175 0.2432 0.3223 -0.0113 0.0158  -0.0105 53  LEU A CA  
114  C C   . LEU A 23  ? 0.3561 0.2729 0.3585 -0.0093 0.0169  -0.0134 53  LEU A C   
115  O O   . LEU A 23  ? 0.3302 0.2497 0.3310 -0.0057 0.0155  -0.0150 53  LEU A O   
116  C CB  . LEU A 23  ? 0.2990 0.2330 0.3062 -0.0161 0.0133  -0.0142 53  LEU A CB  
117  C CG  . LEU A 23  ? 0.4422 0.3854 0.4530 -0.0184 0.0125  -0.0117 53  LEU A CG  
118  C CD1 . LEU A 23  ? 0.4592 0.4120 0.4720 -0.0213 0.0093  -0.0149 53  LEU A CD1 
119  C CD2 . LEU A 23  ? 0.3363 0.2752 0.3502 -0.0228 0.0151  -0.0097 53  LEU A CD2 
120  N N   . ALA A 24  ? 0.3293 0.2353 0.3316 -0.0115 0.0197  -0.0139 54  ALA A N   
121  C CA  . ALA A 24  ? 0.3149 0.2105 0.3149 -0.0093 0.0216  -0.0163 54  ALA A CA  
122  C C   . ALA A 24  ? 0.3639 0.2594 0.3627 -0.0129 0.0205  -0.0231 54  ALA A C   
123  O O   . ALA A 24  ? 0.3630 0.2653 0.3632 -0.0181 0.0183  -0.0257 54  ALA A O   
124  C CB  . ALA A 24  ? 0.3727 0.2555 0.3726 -0.0102 0.0254  -0.0141 54  ALA A CB  
125  N N   . GLY A 25  ? 0.4363 0.3240 0.4324 -0.0100 0.0223  -0.0258 55  GLY A N   
126  C CA  . GLY A 25  ? 0.4392 0.3253 0.4326 -0.0127 0.0218  -0.0325 55  GLY A CA  
127  C C   . GLY A 25  ? 0.4189 0.3022 0.4098 -0.0064 0.0232  -0.0338 55  GLY A C   
128  O O   . GLY A 25  ? 0.4141 0.2977 0.4062 -0.0002 0.0241  -0.0294 55  GLY A O   
129  N N   . ASP A 26  ? 0.4269 0.3078 0.4143 -0.0082 0.0235  -0.0399 56  ASP A N   
130  C CA  . ASP A 26  ? 0.4551 0.3347 0.4403 -0.0024 0.0252  -0.0415 56  ASP A CA  
131  C C   . ASP A 26  ? 0.3856 0.2782 0.3729 0.0019  0.0226  -0.0382 56  ASP A C   
132  O O   . ASP A 26  ? 0.3834 0.2763 0.3716 0.0081  0.0241  -0.0364 56  ASP A O   
133  C CB  . ASP A 26  ? 0.4951 0.3707 0.4751 -0.0055 0.0258  -0.0488 56  ASP A CB  
134  C CG  . ASP A 26  ? 0.6026 0.4897 0.5813 -0.0100 0.0216  -0.0514 56  ASP A CG  
135  O OD1 . ASP A 26  ? 0.6622 0.5553 0.6436 -0.0146 0.0187  -0.0497 56  ASP A OD1 
136  O OD2 . ASP A 26  ? 0.5933 0.4837 0.5683 -0.0087 0.0214  -0.0547 56  ASP A OD2 
137  N N   . VAL A 27  ? 0.3455 0.2489 0.3340 -0.0014 0.0190  -0.0374 57  VAL A N   
138  C CA  . VAL A 27  ? 0.3377 0.2526 0.3286 0.0018  0.0165  -0.0336 57  VAL A CA  
139  C C   . VAL A 27  ? 0.3779 0.2960 0.3718 0.0004  0.0152  -0.0289 57  VAL A C   
140  O O   . VAL A 27  ? 0.3498 0.2699 0.3444 -0.0050 0.0138  -0.0297 57  VAL A O   
141  C CB  . VAL A 27  ? 0.3385 0.2631 0.3279 -0.0001 0.0139  -0.0364 57  VAL A CB  
142  C CG1 . VAL A 27  ? 0.2503 0.1861 0.2426 0.0016  0.0111  -0.0323 57  VAL A CG1 
143  C CG2 . VAL A 27  ? 0.4026 0.3253 0.3891 0.0029  0.0157  -0.0398 57  VAL A CG2 
144  N N   . MET A 28  ? 0.3437 0.2624 0.3394 0.0051  0.0155  -0.0239 58  MET A N   
145  C CA  . MET A 28  ? 0.3631 0.2851 0.3606 0.0044  0.0144  -0.0193 58  MET A CA  
146  C C   . MET A 28  ? 0.3349 0.2688 0.3332 0.0036  0.0112  -0.0188 58  MET A C   
147  O O   . MET A 28  ? 0.2883 0.2282 0.2865 0.0062  0.0099  -0.0194 58  MET A O   
148  C CB  . MET A 28  ? 0.3731 0.2919 0.3710 0.0099  0.0155  -0.0143 58  MET A CB  
149  C CG  . MET A 28  ? 0.4877 0.3941 0.4850 0.0117  0.0189  -0.0139 58  MET A CG  
150  S SD  . MET A 28  ? 0.6787 0.5823 0.6763 0.0174  0.0196  -0.0066 58  MET A SD  
151  C CE  . MET A 28  ? 0.4531 0.3694 0.4519 0.0217  0.0160  -0.0050 58  MET A CE  
152  N N   . SER A 29  ? 0.2548 0.1921 0.2544 -0.0001 0.0104  -0.0174 59  SER A N   
153  C CA  . SER A 29  ? 0.2437 0.1915 0.2444 -0.0012 0.0078  -0.0167 59  SER A CA  
154  C C   . SER A 29  ? 0.3020 0.2518 0.3035 0.0001  0.0080  -0.0119 59  SER A C   
155  O O   . SER A 29  ? 0.3289 0.2739 0.3310 -0.0017 0.0098  -0.0100 59  SER A O   
156  C CB  . SER A 29  ? 0.2682 0.2195 0.2702 -0.0068 0.0067  -0.0198 59  SER A CB  
157  O OG  . SER A 29  ? 0.4669 0.4280 0.4705 -0.0074 0.0045  -0.0184 59  SER A OG  
158  N N   . PHE A 30  ? 0.2989 0.2553 0.3000 0.0029  0.0062  -0.0102 60  PHE A N   
159  C CA  . PHE A 30  ? 0.2730 0.2319 0.2735 0.0043  0.0061  -0.0062 60  PHE A CA  
160  C C   . PHE A 30  ? 0.2828 0.2506 0.2844 0.0031  0.0043  -0.0068 60  PHE A C   
161  O O   . PHE A 30  ? 0.2623 0.2346 0.2641 0.0038  0.0026  -0.0088 60  PHE A O   
162  C CB  . PHE A 30  ? 0.2655 0.2231 0.2639 0.0092  0.0056  -0.0036 60  PHE A CB  
163  C CG  . PHE A 30  ? 0.2960 0.2452 0.2937 0.0114  0.0074  -0.0025 60  PHE A CG  
164  C CD1 . PHE A 30  ? 0.2759 0.2224 0.2743 0.0128  0.0077  -0.0051 60  PHE A CD1 
165  C CD2 . PHE A 30  ? 0.2991 0.2428 0.2952 0.0123  0.0090  0.0014  60  PHE A CD2 
166  C CE1 . PHE A 30  ? 0.2859 0.2243 0.2841 0.0153  0.0097  -0.0039 60  PHE A CE1 
167  C CE2 . PHE A 30  ? 0.3437 0.2792 0.3392 0.0147  0.0108  0.0028  60  PHE A CE2 
168  C CZ  . PHE A 30  ? 0.3039 0.2366 0.3007 0.0163  0.0111  0.0001  60  PHE A CZ  
169  N N   . ARG A 31  ? 0.2180 0.1882 0.2204 0.0015  0.0050  -0.0047 61  ARG A N   
170  C CA  . ARG A 31  ? 0.2471 0.2252 0.2512 0.0004  0.0038  -0.0050 61  ARG A CA  
171  C C   . ARG A 31  ? 0.2254 0.2051 0.2280 0.0021  0.0048  -0.0017 61  ARG A C   
172  O O   . ARG A 31  ? 0.2459 0.2216 0.2475 0.0020  0.0069  0.0008  61  ARG A O   
173  C CB  . ARG A 31  ? 0.2432 0.2243 0.2511 -0.0041 0.0039  -0.0066 61  ARG A CB  
174  C CG  . ARG A 31  ? 0.2630 0.2420 0.2712 -0.0062 0.0030  -0.0104 61  ARG A CG  
175  C CD  . ARG A 31  ? 0.3194 0.3003 0.3311 -0.0114 0.0028  -0.0120 61  ARG A CD  
176  N NE  . ARG A 31  ? 0.3381 0.3146 0.3485 -0.0135 0.0023  -0.0159 61  ARG A NE  
177  C CZ  . ARG A 31  ? 0.4691 0.4483 0.4811 -0.0179 0.0008  -0.0188 61  ARG A CZ  
178  N NH1 . ARG A 31  ? 0.6455 0.6326 0.6616 -0.0207 -0.0005 -0.0178 61  ARG A NH1 
179  N NH2 . ARG A 31  ? 0.4012 0.3753 0.4104 -0.0194 0.0005  -0.0228 61  ARG A NH2 
180  N N   . GLY A 32  ? 0.1924 0.1774 0.1944 0.0036  0.0034  -0.0018 62  GLY A N   
181  C CA  . GLY A 32  ? 0.2043 0.1906 0.2043 0.0051  0.0045  0.0006  62  GLY A CA  
182  C C   . GLY A 32  ? 0.2512 0.2336 0.2461 0.0082  0.0044  0.0025  62  GLY A C   
183  O O   . GLY A 32  ? 0.2516 0.2326 0.2436 0.0091  0.0061  0.0048  62  GLY A O   
184  N N   . ILE A 33  ? 0.2350 0.2159 0.2286 0.0101  0.0024  0.0015  63  ILE A N   
185  C CA  . ILE A 33  ? 0.2022 0.1805 0.1913 0.0131  0.0014  0.0033  63  ILE A CA  
186  C C   . ILE A 33  ? 0.2262 0.2082 0.2129 0.0141  0.0000  0.0028  63  ILE A C   
187  O O   . ILE A 33  ? 0.2507 0.2366 0.2397 0.0138  -0.0015 0.0007  63  ILE A O   
188  C CB  . ILE A 33  ? 0.2600 0.2364 0.2498 0.0148  -0.0001 0.0027  63  ILE A CB  
189  C CG1 . ILE A 33  ? 0.2213 0.1926 0.2130 0.0137  0.0017  0.0027  63  ILE A CG1 
190  C CG2 . ILE A 33  ? 0.2098 0.1848 0.1955 0.0179  -0.0017 0.0049  63  ILE A CG2 
191  C CD1 . ILE A 33  ? 0.2362 0.2050 0.2289 0.0160  0.0009  0.0021  63  ILE A CD1 
192  N N   . PRO A 34  ? 0.2223 0.2029 0.2042 0.0153  0.0006  0.0047  64  PRO A N   
193  C CA  . PRO A 34  ? 0.2170 0.1999 0.1959 0.0163  -0.0008 0.0038  64  PRO A CA  
194  C C   . PRO A 34  ? 0.2470 0.2307 0.2252 0.0177  -0.0043 0.0030  64  PRO A C   
195  O O   . PRO A 34  ? 0.2417 0.2233 0.2189 0.0191  -0.0054 0.0044  64  PRO A O   
196  C CB  . PRO A 34  ? 0.2661 0.2459 0.2387 0.0172  0.0010  0.0059  64  PRO A CB  
197  C CG  . PRO A 34  ? 0.3025 0.2783 0.2741 0.0176  0.0022  0.0085  64  PRO A CG  
198  C CD  . PRO A 34  ? 0.2499 0.2261 0.2282 0.0158  0.0029  0.0077  64  PRO A CD  
199  N N   . TYR A 35  ? 0.2381 0.2251 0.2174 0.0173  -0.0058 0.0010  65  TYR A N   
200  C CA  . TYR A 35  ? 0.2982 0.2868 0.2773 0.0182  -0.0090 0.0002  65  TYR A CA  
201  C C   . TYR A 35  ? 0.2574 0.2461 0.2320 0.0182  -0.0104 -0.0005 65  TYR A C   
202  O O   . TYR A 35  ? 0.2526 0.2431 0.2271 0.0184  -0.0133 -0.0013 65  TYR A O   
203  C CB  . TYR A 35  ? 0.2552 0.2474 0.2402 0.0175  -0.0098 -0.0016 65  TYR A CB  
204  C CG  . TYR A 35  ? 0.2116 0.2064 0.1984 0.0161  -0.0092 -0.0033 65  TYR A CG  
205  C CD1 . TYR A 35  ? 0.2122 0.2079 0.2016 0.0149  -0.0072 -0.0036 65  TYR A CD1 
206  C CD2 . TYR A 35  ? 0.2243 0.2208 0.2106 0.0158  -0.0108 -0.0043 65  TYR A CD2 
207  C CE1 . TYR A 35  ? 0.1747 0.1732 0.1659 0.0140  -0.0068 -0.0046 65  TYR A CE1 
208  C CE2 . TYR A 35  ? 0.2087 0.2070 0.1967 0.0148  -0.0100 -0.0054 65  TYR A CE2 
209  C CZ  . TYR A 35  ? 0.2225 0.2219 0.2129 0.0142  -0.0081 -0.0053 65  TYR A CZ  
210  O OH  . TYR A 35  ? 0.1712 0.1727 0.1633 0.0136  -0.0075 -0.0058 65  TYR A OH  
211  N N   . ALA A 36  ? 0.2413 0.2281 0.2121 0.0180  -0.0082 -0.0004 66  ALA A N   
212  C CA  . ALA A 36  ? 0.2086 0.1938 0.1738 0.0180  -0.0089 -0.0015 66  ALA A CA  
213  C C   . ALA A 36  ? 0.2899 0.2719 0.2501 0.0185  -0.0055 -0.0005 66  ALA A C   
214  O O   . ALA A 36  ? 0.2539 0.2360 0.2168 0.0184  -0.0025 0.0008  66  ALA A O   
215  C CB  . ALA A 36  ? 0.1952 0.1826 0.1634 0.0169  -0.0094 -0.0038 66  ALA A CB  
216  N N   . ALA A 37  ? 0.2538 0.2328 0.2066 0.0189  -0.0058 -0.0013 67  ALA A N   
217  C CA  . ALA A 37  ? 0.2901 0.2658 0.2375 0.0197  -0.0019 -0.0006 67  ALA A CA  
218  C C   . ALA A 37  ? 0.2619 0.2393 0.2143 0.0195  0.0013  -0.0014 67  ALA A C   
219  O O   . ALA A 37  ? 0.2318 0.2112 0.1882 0.0188  0.0000  -0.0032 67  ALA A O   
220  C CB  . ALA A 37  ? 0.2650 0.2366 0.2025 0.0201  -0.0029 -0.0020 67  ALA A CB  
221  N N   . PRO A 38  ? 0.2726 0.2496 0.2253 0.0201  0.0055  0.0002  68  PRO A N   
222  C CA  . PRO A 38  ? 0.2599 0.2395 0.2180 0.0202  0.0084  -0.0001 68  PRO A CA  
223  C C   . PRO A 38  ? 0.2592 0.2363 0.2138 0.0210  0.0087  -0.0024 68  PRO A C   
224  O O   . PRO A 38  ? 0.2291 0.2015 0.1755 0.0219  0.0100  -0.0032 68  PRO A O   
225  C CB  . PRO A 38  ? 0.2794 0.2586 0.2370 0.0209  0.0130  0.0023  68  PRO A CB  
226  C CG  . PRO A 38  ? 0.2557 0.2334 0.2112 0.0204  0.0121  0.0042  68  PRO A CG  
227  C CD  . PRO A 38  ? 0.2690 0.2440 0.2184 0.0206  0.0078  0.0028  68  PRO A CD  
228  N N   . PRO A 39  ? 0.2393 0.2190 0.1995 0.0205  0.0076  -0.0035 69  PRO A N   
229  C CA  . PRO A 39  ? 0.2114 0.1878 0.1686 0.0211  0.0080  -0.0056 69  PRO A CA  
230  C C   . PRO A 39  ? 0.2438 0.2191 0.2011 0.0231  0.0129  -0.0050 69  PRO A C   
231  O O   . PRO A 39  ? 0.2508 0.2277 0.2130 0.0239  0.0140  -0.0049 69  PRO A O   
232  C CB  . PRO A 39  ? 0.2521 0.2321 0.2159 0.0198  0.0052  -0.0062 69  PRO A CB  
233  C CG  . PRO A 39  ? 0.2167 0.2025 0.1881 0.0194  0.0055  -0.0042 69  PRO A CG  
234  C CD  . PRO A 39  ? 0.1983 0.1835 0.1672 0.0193  0.0060  -0.0028 69  PRO A CD  
235  N N   . VAL A 40  ? 0.2719 0.2443 0.2236 0.0244  0.0161  -0.0043 70  VAL A N   
236  C CA  . VAL A 40  ? 0.3008 0.2726 0.2529 0.0267  0.0216  -0.0033 70  VAL A CA  
237  C C   . VAL A 40  ? 0.2360 0.1999 0.1772 0.0281  0.0238  -0.0056 70  VAL A C   
238  O O   . VAL A 40  ? 0.2696 0.2291 0.2022 0.0270  0.0212  -0.0074 70  VAL A O   
239  C CB  . VAL A 40  ? 0.2997 0.2754 0.2553 0.0270  0.0246  -0.0002 70  VAL A CB  
240  C CG1 . VAL A 40  ? 0.2133 0.1961 0.1789 0.0251  0.0222  0.0014  70  VAL A CG1 
241  C CG2 . VAL A 40  ? 0.2635 0.2351 0.2103 0.0267  0.0248  0.0001  70  VAL A CG2 
242  N N   . GLY A 41  ? 0.2723 0.2345 0.2138 0.0307  0.0288  -0.0055 71  GLY A N   
243  C CA  . GLY A 41  ? 0.2525 0.2064 0.1833 0.0323  0.0318  -0.0080 71  GLY A CA  
244  C C   . GLY A 41  ? 0.2564 0.2044 0.1813 0.0307  0.0279  -0.0118 71  GLY A C   
245  O O   . GLY A 41  ? 0.2519 0.2006 0.1823 0.0303  0.0264  -0.0125 71  GLY A O   
246  N N   . GLY A 42  ? 0.3398 0.2821 0.2534 0.0295  0.0261  -0.0141 72  GLY A N   
247  C CA  . GLY A 42  ? 0.2702 0.2073 0.1780 0.0273  0.0220  -0.0179 72  GLY A CA  
248  C C   . GLY A 42  ? 0.2827 0.2250 0.1976 0.0245  0.0160  -0.0176 72  GLY A C   
249  O O   . GLY A 42  ? 0.3368 0.2761 0.2504 0.0225  0.0129  -0.0204 72  GLY A O   
250  N N   . LEU A 43  ? 0.2725 0.2223 0.1951 0.0241  0.0144  -0.0145 73  LEU A N   
251  C CA  . LEU A 43  ? 0.2407 0.1957 0.1702 0.0218  0.0093  -0.0141 73  LEU A CA  
252  C C   . LEU A 43  ? 0.2884 0.2478 0.2284 0.0221  0.0100  -0.0129 73  LEU A C   
253  O O   . LEU A 43  ? 0.2286 0.1922 0.1744 0.0203  0.0064  -0.0125 73  LEU A O   
254  C CB  . LEU A 43  ? 0.2363 0.1960 0.1675 0.0213  0.0072  -0.0116 73  LEU A CB  
255  C CG  . LEU A 43  ? 0.3044 0.2609 0.2257 0.0210  0.0054  -0.0120 73  LEU A CG  
256  C CD1 . LEU A 43  ? 0.2398 0.2009 0.1644 0.0207  0.0031  -0.0091 73  LEU A CD1 
257  C CD2 . LEU A 43  ? 0.2741 0.2271 0.1893 0.0190  0.0012  -0.0153 73  LEU A CD2 
258  N N   . ARG A 44  ? 0.2420 0.2009 0.1846 0.0244  0.0146  -0.0119 74  ARG A N   
259  C CA  . ARG A 44  ? 0.2621 0.2244 0.2134 0.0248  0.0149  -0.0109 74  ARG A CA  
260  C C   . ARG A 44  ? 0.2342 0.1916 0.1833 0.0234  0.0128  -0.0135 74  ARG A C   
261  O O   . ARG A 44  ? 0.2426 0.1925 0.1838 0.0233  0.0137  -0.0163 74  ARG A O   
262  C CB  . ARG A 44  ? 0.2396 0.2022 0.1940 0.0281  0.0203  -0.0092 74  ARG A CB  
263  C CG  . ARG A 44  ? 0.2408 0.2067 0.2035 0.0290  0.0206  -0.0076 74  ARG A CG  
264  C CD  . ARG A 44  ? 0.2875 0.2526 0.2525 0.0328  0.0260  -0.0061 74  ARG A CD  
265  N NE  . ARG A 44  ? 0.2303 0.2027 0.2013 0.0341  0.0283  -0.0030 74  ARG A NE  
266  C CZ  . ARG A 44  ? 0.2779 0.2519 0.2526 0.0375  0.0331  -0.0010 74  ARG A CZ  
267  N NH1 . ARG A 44  ? 0.2680 0.2360 0.2404 0.0405  0.0366  -0.0017 74  ARG A NH1 
268  N NH2 . ARG A 44  ? 0.2414 0.2232 0.2225 0.0380  0.0346  0.0019  74  ARG A NH2 
269  N N   . TRP A 45  ? 0.2211 0.1828 0.1771 0.0219  0.0101  -0.0127 75  TRP A N   
270  C CA  . TRP A 45  ? 0.2230 0.1813 0.1788 0.0200  0.0081  -0.0146 75  TRP A CA  
271  C C   . TRP A 45  ? 0.2511 0.2061 0.2003 0.0172  0.0044  -0.0175 75  TRP A C   
272  O O   . TRP A 45  ? 0.2705 0.2197 0.2161 0.0155  0.0036  -0.0201 75  TRP A O   
273  C CB  . TRP A 45  ? 0.2301 0.1817 0.1842 0.0219  0.0119  -0.0153 75  TRP A CB  
274  C CG  . TRP A 45  ? 0.2252 0.1810 0.1868 0.0249  0.0150  -0.0120 75  TRP A CG  
275  C CD1 . TRP A 45  ? 0.2164 0.1795 0.1861 0.0246  0.0134  -0.0093 75  TRP A CD1 
276  C CD2 . TRP A 45  ? 0.2302 0.1833 0.1917 0.0286  0.0201  -0.0109 75  TRP A CD2 
277  N NE1 . TRP A 45  ? 0.2148 0.1804 0.1895 0.0278  0.0166  -0.0065 75  TRP A NE1 
278  C CE2 . TRP A 45  ? 0.2380 0.1978 0.2085 0.0304  0.0209  -0.0073 75  TRP A CE2 
279  C CE3 . TRP A 45  ? 0.2406 0.1863 0.1952 0.0308  0.0242  -0.0127 75  TRP A CE3 
280  C CZ2 . TRP A 45  ? 0.2255 0.1858 0.1993 0.0345  0.0254  -0.0050 75  TRP A CZ2 
281  C CZ3 . TRP A 45  ? 0.2432 0.1887 0.2009 0.0349  0.0293  -0.0106 75  TRP A CZ3 
282  C CH2 . TRP A 45  ? 0.2498 0.2030 0.2176 0.0368  0.0297  -0.0066 75  TRP A CH2 
283  N N   . LYS A 46  ? 0.2259 0.1844 0.1737 0.0165  0.0020  -0.0170 76  LYS A N   
284  C CA  . LYS A 46  ? 0.2286 0.1868 0.1725 0.0139  -0.0025 -0.0188 76  LYS A CA  
285  C C   . LYS A 46  ? 0.2188 0.1849 0.1701 0.0129  -0.0057 -0.0169 76  LYS A C   
286  O O   . LYS A 46  ? 0.2116 0.1823 0.1684 0.0143  -0.0044 -0.0144 76  LYS A O   
287  C CB  . LYS A 46  ? 0.2462 0.2015 0.1811 0.0146  -0.0025 -0.0195 76  LYS A CB  
288  C CG  . LYS A 46  ? 0.3159 0.2624 0.2408 0.0146  -0.0006 -0.0226 76  LYS A CG  
289  C CD  . LYS A 46  ? 0.3177 0.2621 0.2329 0.0141  -0.0028 -0.0236 76  LYS A CD  
290  C CE  . LYS A 46  ? 0.3989 0.3344 0.3027 0.0152  0.0007  -0.0263 76  LYS A CE  
291  N NZ  . LYS A 46  ? 0.4911 0.4197 0.3921 0.0134  0.0008  -0.0301 76  LYS A NZ  
292  N N   . PRO A 47  ? 0.2485 0.2162 0.2003 0.0104  -0.0100 -0.0180 77  PRO A N   
293  C CA  . PRO A 47  ? 0.2236 0.1983 0.1815 0.0100  -0.0128 -0.0163 77  PRO A CA  
294  C C   . PRO A 47  ? 0.2305 0.2070 0.1869 0.0119  -0.0122 -0.0143 77  PRO A C   
295  O O   . PRO A 47  ? 0.2167 0.1892 0.1658 0.0128  -0.0110 -0.0146 77  PRO A O   
296  C CB  . PRO A 47  ? 0.2149 0.1902 0.1714 0.0073  -0.0173 -0.0180 77  PRO A CB  
297  C CG  . PRO A 47  ? 0.2798 0.2492 0.2330 0.0055  -0.0168 -0.0206 77  PRO A CG  
298  C CD  . PRO A 47  ? 0.2426 0.2059 0.1900 0.0078  -0.0124 -0.0210 77  PRO A CD  
299  N N   . PRO A 48  ? 0.2211 0.2029 0.1838 0.0124  -0.0126 -0.0123 78  PRO A N   
300  C CA  . PRO A 48  ? 0.2020 0.1847 0.1635 0.0139  -0.0120 -0.0104 78  PRO A CA  
301  C C   . PRO A 48  ? 0.2205 0.2022 0.1764 0.0138  -0.0151 -0.0105 78  PRO A C   
302  O O   . PRO A 48  ? 0.2684 0.2523 0.2256 0.0125  -0.0188 -0.0112 78  PRO A O   
303  C CB  . PRO A 48  ? 0.2064 0.1943 0.1758 0.0140  -0.0123 -0.0090 78  PRO A CB  
304  C CG  . PRO A 48  ? 0.2133 0.2038 0.1869 0.0124  -0.0145 -0.0102 78  PRO A CG  
305  C CD  . PRO A 48  ? 0.1949 0.1815 0.1655 0.0115  -0.0135 -0.0119 78  PRO A CD  
306  N N   . GLN A 49  ? 0.2362 0.2149 0.1860 0.0152  -0.0135 -0.0094 79  GLN A N   
307  C CA  . GLN A 49  ? 0.2638 0.2413 0.2070 0.0155  -0.0162 -0.0088 79  GLN A CA  
308  C C   . GLN A 49  ? 0.3243 0.3043 0.2704 0.0169  -0.0166 -0.0058 79  GLN A C   
309  O O   . GLN A 49  ? 0.3012 0.2822 0.2521 0.0176  -0.0137 -0.0044 79  GLN A O   
310  C CB  . GLN A 49  ? 0.2591 0.2308 0.1921 0.0162  -0.0140 -0.0095 79  GLN A CB  
311  C CG  . GLN A 49  ? 0.3416 0.3092 0.2713 0.0152  -0.0124 -0.0126 79  GLN A CG  
312  C CD  . GLN A 49  ? 0.4100 0.3770 0.3374 0.0128  -0.0169 -0.0153 79  GLN A CD  
313  O OE1 . GLN A 49  ? 0.5080 0.4740 0.4285 0.0122  -0.0202 -0.0158 79  GLN A OE1 
314  N NE2 . GLN A 49  ? 0.3704 0.3385 0.3038 0.0113  -0.0171 -0.0169 79  GLN A NE2 
315  N N   . HIS A 50  ? 0.3265 0.3074 0.2695 0.0173  -0.0202 -0.0047 80  HIS A N   
316  C CA  . HIS A 50  ? 0.3725 0.3547 0.3174 0.0191  -0.0205 -0.0015 80  HIS A CA  
317  C C   . HIS A 50  ? 0.3603 0.3384 0.3007 0.0203  -0.0163 0.0004  80  HIS A C   
318  O O   . HIS A 50  ? 0.3481 0.3223 0.2802 0.0205  -0.0148 0.0000  80  HIS A O   
319  C CB  . HIS A 50  ? 0.4540 0.4378 0.3955 0.0197  -0.0253 -0.0003 80  HIS A CB  
320  C CG  . HIS A 50  ? 0.5756 0.5621 0.5224 0.0216  -0.0264 0.0027  80  HIS A CG  
321  N ND1 . HIS A 50  ? 0.5632 0.5548 0.5190 0.0215  -0.0283 0.0025  80  HIS A ND1 
322  C CD2 . HIS A 50  ? 0.5955 0.5799 0.5400 0.0238  -0.0254 0.0062  80  HIS A CD2 
323  C CE1 . HIS A 50  ? 0.5818 0.5742 0.5407 0.0239  -0.0284 0.0055  80  HIS A CE1 
324  N NE2 . HIS A 50  ? 0.6617 0.6495 0.6138 0.0252  -0.0267 0.0078  80  HIS A NE2 
325  N N   . ALA A 51  ? 0.3091 0.2877 0.2548 0.0211  -0.0141 0.0025  81  ALA A N   
326  C CA  . ALA A 51  ? 0.3095 0.2848 0.2524 0.0219  -0.0099 0.0046  81  ALA A CA  
327  C C   . ALA A 51  ? 0.3729 0.3452 0.3082 0.0235  -0.0109 0.0076  81  ALA A C   
328  O O   . ALA A 51  ? 0.3333 0.3071 0.2672 0.0243  -0.0151 0.0083  81  ALA A O   
329  C CB  . ALA A 51  ? 0.2182 0.1948 0.1693 0.0215  -0.0076 0.0056  81  ALA A CB  
330  N N   . ARG A 52  ? 0.3119 0.2806 0.2426 0.0241  -0.0069 0.0096  82  ARG A N   
331  C CA  . ARG A 52  ? 0.3625 0.3278 0.2852 0.0258  -0.0072 0.0130  82  ARG A CA  
332  C C   . ARG A 52  ? 0.3806 0.3451 0.3082 0.0267  -0.0061 0.0165  82  ARG A C   
333  O O   . ARG A 52  ? 0.3870 0.3517 0.3217 0.0256  -0.0031 0.0164  82  ARG A O   
334  C CB  . ARG A 52  ? 0.3914 0.3527 0.3057 0.0260  -0.0029 0.0137  82  ARG A CB  
335  C CG  . ARG A 52  ? 0.4487 0.4086 0.3543 0.0257  -0.0041 0.0108  82  ARG A CG  
336  C CD  . ARG A 52  ? 0.5355 0.4917 0.4352 0.0261  0.0016  0.0109  82  ARG A CD  
337  N NE  . ARG A 52  ? 0.5722 0.5306 0.4807 0.0251  0.0053  0.0094  82  ARG A NE  
338  C CZ  . ARG A 52  ? 0.6391 0.5972 0.5470 0.0247  0.0069  0.0062  82  ARG A CZ  
339  N NH1 . ARG A 52  ? 0.6064 0.5610 0.5044 0.0250  0.0059  0.0038  82  ARG A NH1 
340  N NH2 . ARG A 52  ? 0.5803 0.5414 0.4973 0.0241  0.0096  0.0055  82  ARG A NH2 
341  N N   . PRO A 53  ? 0.3736 0.3368 0.2972 0.0287  -0.0087 0.0196  83  PRO A N   
342  C CA  . PRO A 53  ? 0.3846 0.3455 0.3122 0.0299  -0.0073 0.0232  83  PRO A CA  
343  C C   . PRO A 53  ? 0.3280 0.2841 0.2525 0.0296  -0.0018 0.0259  83  PRO A C   
344  O O   . PRO A 53  ? 0.4053 0.3598 0.3228 0.0292  0.0006  0.0258  83  PRO A O   
345  C CB  . PRO A 53  ? 0.3073 0.2684 0.2303 0.0326  -0.0117 0.0261  83  PRO A CB  
346  C CG  . PRO A 53  ? 0.4358 0.3971 0.3485 0.0325  -0.0138 0.0251  83  PRO A CG  
347  C CD  . PRO A 53  ? 0.4169 0.3804 0.3319 0.0299  -0.0131 0.0201  83  PRO A CD  
348  N N   . TRP A 54  ? 0.3257 0.2793 0.2556 0.0297  0.0004  0.0282  84  TRP A N   
349  C CA  . TRP A 54  ? 0.3521 0.3010 0.2807 0.0290  0.0057  0.0312  84  TRP A CA  
350  C C   . TRP A 54  ? 0.3638 0.3078 0.2916 0.0310  0.0060  0.0359  84  TRP A C   
351  O O   . TRP A 54  ? 0.3657 0.3103 0.2962 0.0329  0.0025  0.0364  84  TRP A O   
352  C CB  . TRP A 54  ? 0.2584 0.2087 0.1961 0.0259  0.0092  0.0289  84  TRP A CB  
353  C CG  . TRP A 54  ? 0.3106 0.2621 0.2572 0.0253  0.0074  0.0271  84  TRP A CG  
354  C CD1 . TRP A 54  ? 0.3067 0.2540 0.2569 0.0256  0.0084  0.0291  84  TRP A CD1 
355  C CD2 . TRP A 54  ? 0.3040 0.2607 0.2564 0.0244  0.0046  0.0228  84  TRP A CD2 
356  N NE1 . TRP A 54  ? 0.3058 0.2553 0.2633 0.0250  0.0065  0.0260  84  TRP A NE1 
357  C CE2 . TRP A 54  ? 0.2861 0.2417 0.2451 0.0243  0.0041  0.0223  84  TRP A CE2 
358  C CE3 . TRP A 54  ? 0.2846 0.2461 0.2369 0.0237  0.0027  0.0194  84  TRP A CE3 
359  C CZ2 . TRP A 54  ? 0.2853 0.2450 0.2503 0.0235  0.0020  0.0186  84  TRP A CZ2 
360  C CZ3 . TRP A 54  ? 0.3193 0.2848 0.2781 0.0229  0.0004  0.0161  84  TRP A CZ3 
361  C CH2 . TRP A 54  ? 0.3159 0.2808 0.2808 0.0228  0.0001  0.0157  84  TRP A CH2 
362  N N   . ALA A 55  ? 0.3156 0.2546 0.2399 0.0307  0.0106  0.0397  85  ALA A N   
363  C CA  . ALA A 55  ? 0.3865 0.3194 0.3099 0.0324  0.0120  0.0447  85  ALA A CA  
364  C C   . ALA A 55  ? 0.3372 0.2671 0.2699 0.0299  0.0156  0.0443  85  ALA A C   
365  O O   . ALA A 55  ? 0.3309 0.2634 0.2693 0.0265  0.0178  0.0411  85  ALA A O   
366  C CB  . ALA A 55  ? 0.3235 0.2520 0.2365 0.0336  0.0151  0.0495  85  ALA A CB  
367  N N   . GLY A 56  ? 0.3618 0.2861 0.2959 0.0315  0.0160  0.0477  86  GLY A N   
368  C CA  . GLY A 56  ? 0.3591 0.2789 0.3010 0.0290  0.0195  0.0474  86  GLY A CA  
369  C C   . GLY A 56  ? 0.3312 0.2551 0.2820 0.0269  0.0176  0.0417  86  GLY A C   
370  O O   . GLY A 56  ? 0.3345 0.2636 0.2863 0.0286  0.0133  0.0389  86  GLY A O   
371  N N   . VAL A 57  ? 0.3265 0.2483 0.2838 0.0231  0.0209  0.0399  87  VAL A N   
372  C CA  . VAL A 57  ? 0.3280 0.2530 0.2931 0.0207  0.0195  0.0346  87  VAL A CA  
373  C C   . VAL A 57  ? 0.2870 0.2182 0.2550 0.0168  0.0206  0.0315  87  VAL A C   
374  O O   . VAL A 57  ? 0.3440 0.2738 0.3137 0.0137  0.0244  0.0328  87  VAL A O   
375  C CB  . VAL A 57  ? 0.3285 0.2462 0.2986 0.0191  0.0218  0.0345  87  VAL A CB  
376  C CG1 . VAL A 57  ? 0.3118 0.2328 0.2885 0.0168  0.0202  0.0286  87  VAL A CG1 
377  C CG2 . VAL A 57  ? 0.3070 0.2178 0.2742 0.0236  0.0214  0.0383  87  VAL A CG2 
378  N N   . ARG A 58  ? 0.2787 0.2170 0.2479 0.0171  0.0173  0.0278  88  ARG A N   
379  C CA  . ARG A 58  ? 0.2924 0.2372 0.2648 0.0142  0.0178  0.0248  88  ARG A CA  
380  C C   . ARG A 58  ? 0.3104 0.2563 0.2908 0.0105  0.0181  0.0214  88  ARG A C   
381  O O   . ARG A 58  ? 0.2987 0.2429 0.2814 0.0110  0.0163  0.0192  88  ARG A O   
382  C CB  . ARG A 58  ? 0.2605 0.2114 0.2307 0.0162  0.0142  0.0224  88  ARG A CB  
383  C CG  . ARG A 58  ? 0.2769 0.2342 0.2499 0.0140  0.0147  0.0198  88  ARG A CG  
384  C CD  . ARG A 58  ? 0.2916 0.2536 0.2627 0.0159  0.0111  0.0172  88  ARG A CD  
385  N NE  . ARG A 58  ? 0.3899 0.3575 0.3641 0.0142  0.0116  0.0149  88  ARG A NE  
386  C CZ  . ARG A 58  ? 0.3930 0.3624 0.3633 0.0150  0.0126  0.0151  88  ARG A CZ  
387  N NH1 . ARG A 58  ? 0.4773 0.4436 0.4396 0.0172  0.0130  0.0172  88  ARG A NH1 
388  N NH2 . ARG A 58  ? 0.3843 0.3586 0.3585 0.0138  0.0134  0.0133  88  ARG A NH2 
389  N N   . PRO A 59  ? 0.2841 0.2329 0.2686 0.0068  0.0206  0.0209  89  PRO A N   
390  C CA  . PRO A 59  ? 0.2800 0.2307 0.2717 0.0028  0.0202  0.0174  89  PRO A CA  
391  C C   . PRO A 59  ? 0.3276 0.2843 0.3210 0.0035  0.0165  0.0132  89  PRO A C   
392  O O   . PRO A 59  ? 0.2942 0.2564 0.2860 0.0051  0.0151  0.0128  89  PRO A O   
393  C CB  . PRO A 59  ? 0.3269 0.2816 0.3227 -0.0007 0.0232  0.0184  89  PRO A CB  
394  C CG  . PRO A 59  ? 0.3190 0.2703 0.3094 0.0011  0.0265  0.0231  89  PRO A CG  
395  C CD  . PRO A 59  ? 0.2447 0.1948 0.2276 0.0060  0.0240  0.0238  89  PRO A CD  
396  N N   . ALA A 60  ? 0.3158 0.2709 0.3121 0.0022  0.0151  0.0102  90  ALA A N   
397  C CA  . ALA A 60  ? 0.2932 0.2536 0.2913 0.0024  0.0119  0.0063  90  ALA A CA  
398  C C   . ALA A 60  ? 0.3220 0.2826 0.3247 -0.0018 0.0118  0.0030  90  ALA A C   
399  O O   . ALA A 60  ? 0.2823 0.2425 0.2853 -0.0015 0.0100  -0.0002 90  ALA A O   
400  C CB  . ALA A 60  ? 0.3090 0.2675 0.3040 0.0064  0.0098  0.0059  90  ALA A CB  
401  N N   . THR A 61  ? 0.3333 0.2947 0.3397 -0.0059 0.0137  0.0035  91  THR A N   
402  C CA  . THR A 61  ? 0.3368 0.2986 0.3475 -0.0106 0.0131  0.0002  91  THR A CA  
403  C C   . THR A 61  ? 0.3298 0.3016 0.3445 -0.0129 0.0112  -0.0015 91  THR A C   
404  O O   . THR A 61  ? 0.2949 0.2685 0.3124 -0.0165 0.0096  -0.0048 91  THR A O   
405  C CB  . THR A 61  ? 0.3392 0.2955 0.3524 -0.0145 0.0162  0.0017  91  THR A CB  
406  O OG1 . THR A 61  ? 0.3840 0.3444 0.3992 -0.0151 0.0184  0.0053  91  THR A OG1 
407  C CG2 . THR A 61  ? 0.3148 0.2601 0.3242 -0.0122 0.0182  0.0034  91  THR A CG2 
408  N N   . GLN A 62  ? 0.2978 0.2759 0.3125 -0.0108 0.0112  0.0005  92  GLN A N   
409  C CA  . GLN A 62  ? 0.3299 0.3175 0.3488 -0.0122 0.0097  -0.0003 92  GLN A CA  
410  C C   . GLN A 62  ? 0.2735 0.2648 0.2893 -0.0081 0.0077  -0.0007 92  GLN A C   
411  O O   . GLN A 62  ? 0.2441 0.2322 0.2553 -0.0045 0.0084  0.0009  92  GLN A O   
412  C CB  . GLN A 62  ? 0.3369 0.3290 0.3601 -0.0137 0.0123  0.0028  92  GLN A CB  
413  C CG  . GLN A 62  ? 0.5268 0.5154 0.5537 -0.0181 0.0147  0.0038  92  GLN A CG  
414  C CD  . GLN A 62  ? 0.6141 0.6048 0.6457 -0.0233 0.0124  0.0004  92  GLN A CD  
415  O OE1 . GLN A 62  ? 0.6809 0.6789 0.7147 -0.0240 0.0094  -0.0018 92  GLN A OE1 
416  N NE2 . GLN A 62  ? 0.7062 0.6902 0.7389 -0.0270 0.0139  -0.0001 92  GLN A NE2 
417  N N   . PHE A 63  ? 0.1927 0.1904 0.2108 -0.0090 0.0053  -0.0028 93  PHE A N   
418  C CA  . PHE A 63  ? 0.2103 0.2117 0.2263 -0.0056 0.0037  -0.0029 93  PHE A CA  
419  C C   . PHE A 63  ? 0.2522 0.2556 0.2677 -0.0032 0.0057  0.0001  93  PHE A C   
420  O O   . PHE A 63  ? 0.2756 0.2814 0.2947 -0.0047 0.0079  0.0021  93  PHE A O   
421  C CB  . PHE A 63  ? 0.2237 0.2322 0.2427 -0.0071 0.0012  -0.0047 93  PHE A CB  
422  C CG  . PHE A 63  ? 0.2630 0.2694 0.2804 -0.0086 -0.0009 -0.0081 93  PHE A CG  
423  C CD1 . PHE A 63  ? 0.1949 0.1976 0.2080 -0.0058 -0.0016 -0.0094 93  PHE A CD1 
424  C CD2 . PHE A 63  ? 0.2708 0.2794 0.2910 -0.0128 -0.0022 -0.0101 93  PHE A CD2 
425  C CE1 . PHE A 63  ? 0.2324 0.2331 0.2438 -0.0068 -0.0028 -0.0125 93  PHE A CE1 
426  C CE2 . PHE A 63  ? 0.2752 0.2811 0.2927 -0.0141 -0.0038 -0.0136 93  PHE A CE2 
427  C CZ  . PHE A 63  ? 0.2659 0.2677 0.2789 -0.0109 -0.0038 -0.0148 93  PHE A CZ  
428  N N   . GLY A 64  ? 0.2070 0.2094 0.2183 0.0003  0.0052  0.0003  94  GLY A N   
429  C CA  . GLY A 64  ? 0.2302 0.2342 0.2401 0.0026  0.0069  0.0023  94  GLY A CA  
430  C C   . GLY A 64  ? 0.1959 0.2073 0.2103 0.0025  0.0065  0.0024  94  GLY A C   
431  O O   . GLY A 64  ? 0.2030 0.2188 0.2212 0.0005  0.0045  0.0010  94  GLY A O   
432  N N   . SER A 65  ? 0.1980 0.2105 0.2114 0.0048  0.0085  0.0040  95  SER A N   
433  C CA  . SER A 65  ? 0.2201 0.2391 0.2377 0.0055  0.0085  0.0046  95  SER A CA  
434  C C   . SER A 65  ? 0.2061 0.2261 0.2223 0.0067  0.0055  0.0028  95  SER A C   
435  O O   . SER A 65  ? 0.1807 0.1961 0.1918 0.0078  0.0043  0.0015  95  SER A O   
436  C CB  . SER A 65  ? 0.2164 0.2351 0.2326 0.0083  0.0120  0.0065  95  SER A CB  
437  O OG  . SER A 65  ? 0.2548 0.2729 0.2722 0.0074  0.0153  0.0085  95  SER A OG  
438  N N   . ASP A 66  ? 0.2018 0.2283 0.2228 0.0062  0.0043  0.0031  96  ASP A N   
439  C CA  . ASP A 66  ? 0.2148 0.2425 0.2346 0.0076  0.0021  0.0022  96  ASP A CA  
440  C C   . ASP A 66  ? 0.2372 0.2629 0.2544 0.0110  0.0039  0.0031  96  ASP A C   
441  O O   . ASP A 66  ? 0.1973 0.2233 0.2155 0.0124  0.0069  0.0048  96  ASP A O   
442  C CB  . ASP A 66  ? 0.1964 0.2318 0.2217 0.0062  0.0002  0.0027  96  ASP A CB  
443  C CG  . ASP A 66  ? 0.2173 0.2542 0.2441 0.0024  -0.0020 0.0010  96  ASP A CG  
444  O OD1 . ASP A 66  ? 0.1875 0.2188 0.2103 0.0015  -0.0026 -0.0011 96  ASP A OD1 
445  O OD2 . ASP A 66  ? 0.1849 0.2285 0.2168 0.0004  -0.0033 0.0016  96  ASP A OD2 
446  N N   . CYS A 67  ? 0.2020 0.2254 0.2159 0.0121  0.0023  0.0020  97  CYS A N   
447  C CA  . CYS A 67  ? 0.2205 0.2418 0.2322 0.0149  0.0037  0.0026  97  CYS A CA  
448  C C   . CYS A 67  ? 0.2331 0.2600 0.2499 0.0162  0.0043  0.0046  97  CYS A C   
449  O O   . CYS A 67  ? 0.1988 0.2317 0.2200 0.0148  0.0024  0.0052  97  CYS A O   
450  C CB  . CYS A 67  ? 0.1848 0.2022 0.1923 0.0152  0.0019  0.0009  97  CYS A CB  
451  S SG  . CYS A 67  ? 0.2379 0.2492 0.2398 0.0144  0.0010  -0.0010 97  CYS A SG  
452  N N   . PHE A 68  ? 0.1828 0.2078 0.1988 0.0191  0.0071  0.0057  98  PHE A N   
453  C CA  . PHE A 68  ? 0.1902 0.2201 0.2113 0.0212  0.0080  0.0081  98  PHE A CA  
454  C C   . PHE A 68  ? 0.2403 0.2718 0.2617 0.0212  0.0053  0.0082  98  PHE A C   
455  O O   . PHE A 68  ? 0.2566 0.2830 0.2733 0.0209  0.0042  0.0065  98  PHE A O   
456  C CB  . PHE A 68  ? 0.1871 0.2125 0.2061 0.0247  0.0120  0.0088  98  PHE A CB  
457  C CG  . PHE A 68  ? 0.2281 0.2556 0.2498 0.0258  0.0156  0.0103  98  PHE A CG  
458  C CD1 . PHE A 68  ? 0.2360 0.2585 0.2527 0.0251  0.0175  0.0091  98  PHE A CD1 
459  C CD2 . PHE A 68  ? 0.2568 0.2915 0.2862 0.0276  0.0173  0.0134  98  PHE A CD2 
460  C CE1 . PHE A 68  ? 0.2328 0.2570 0.2517 0.0261  0.0214  0.0107  98  PHE A CE1 
461  C CE2 . PHE A 68  ? 0.2014 0.2386 0.2341 0.0286  0.0212  0.0150  98  PHE A CE2 
462  C CZ  . PHE A 68  ? 0.2176 0.2493 0.2448 0.0278  0.0235  0.0136  98  PHE A CZ  
463  N N   . GLY A 69  ? 0.1946 0.2337 0.2217 0.0214  0.0041  0.0105  99  GLY A N   
464  C CA  . GLY A 69  ? 0.2264 0.2677 0.2535 0.0215  0.0015  0.0111  99  GLY A CA  
465  C C   . GLY A 69  ? 0.2079 0.2584 0.2416 0.0221  0.0003  0.0142  99  GLY A C   
466  O O   . GLY A 69  ? 0.2429 0.2988 0.2820 0.0220  0.0012  0.0156  99  GLY A O   
467  N N   . ALA A 70  ? 0.2599 0.3126 0.2933 0.0228  -0.0018 0.0156  100 ALA A N   
468  C CA  . ALA A 70  ? 0.2037 0.2659 0.2428 0.0234  -0.0037 0.0188  100 ALA A CA  
469  C C   . ALA A 70  ? 0.2352 0.3044 0.2778 0.0197  -0.0063 0.0178  100 ALA A C   
470  O O   . ALA A 70  ? 0.2462 0.3135 0.2851 0.0162  -0.0083 0.0147  100 ALA A O   
471  C CB  . ALA A 70  ? 0.2384 0.3012 0.2747 0.0240  -0.0060 0.0200  100 ALA A CB  
472  N N   . ALA A 71  ? 0.2621 0.3395 0.3123 0.0203  -0.0062 0.0205  101 ALA A N   
473  C CA  . ALA A 71  ? 0.1881 0.2720 0.2426 0.0163  -0.0081 0.0196  101 ALA A CA  
474  C C   . ALA A 71  ? 0.2049 0.2923 0.2570 0.0126  -0.0130 0.0179  101 ALA A C   
475  O O   . ALA A 71  ? 0.1711 0.2577 0.2220 0.0084  -0.0143 0.0148  101 ALA A O   
476  C CB  . ALA A 71  ? 0.1875 0.2812 0.2518 0.0179  -0.0074 0.0234  101 ALA A CB  
477  N N   . TYR A 72  ? 0.1650 0.2557 0.2158 0.0141  -0.0154 0.0198  102 TYR A N   
478  C CA  . TYR A 72  ? 0.2500 0.3445 0.2978 0.0106  -0.0199 0.0182  102 TYR A CA  
479  C C   . TYR A 72  ? 0.2289 0.3148 0.2684 0.0082  -0.0199 0.0137  102 TYR A C   
480  O O   . TYR A 72  ? 0.2940 0.3817 0.3304 0.0047  -0.0230 0.0113  102 TYR A O   
481  C CB  . TYR A 72  ? 0.1971 0.2967 0.2444 0.0133  -0.0222 0.0218  102 TYR A CB  
482  C CG  . TYR A 72  ? 0.2519 0.3436 0.2922 0.0158  -0.0206 0.0219  102 TYR A CG  
483  C CD1 . TYR A 72  ? 0.2501 0.3360 0.2909 0.0200  -0.0167 0.0238  102 TYR A CD1 
484  C CD2 . TYR A 72  ? 0.2714 0.3612 0.3045 0.0138  -0.0228 0.0199  102 TYR A CD2 
485  C CE1 . TYR A 72  ? 0.2762 0.3549 0.3111 0.0217  -0.0153 0.0238  102 TYR A CE1 
486  C CE2 . TYR A 72  ? 0.2928 0.3758 0.3203 0.0158  -0.0211 0.0203  102 TYR A CE2 
487  C CZ  . TYR A 72  ? 0.2797 0.3573 0.3084 0.0195  -0.0175 0.0222  102 TYR A CZ  
488  O OH  . TYR A 72  ? 0.3728 0.4437 0.3965 0.0210  -0.0158 0.0225  102 TYR A OH  
489  N N   . LEU A 73  ? 0.2382 0.3152 0.2742 0.0099  -0.0165 0.0125  103 LEU A N   
490  C CA  . LEU A 73  ? 0.3114 0.3808 0.3407 0.0081  -0.0163 0.0087  103 LEU A CA  
491  C C   . LEU A 73  ? 0.2907 0.3566 0.3202 0.0053  -0.0154 0.0056  103 LEU A C   
492  O O   . LEU A 73  ? 0.2786 0.3384 0.3033 0.0040  -0.0151 0.0025  103 LEU A O   
493  C CB  . LEU A 73  ? 0.2128 0.2748 0.2384 0.0112  -0.0136 0.0090  103 LEU A CB  
494  C CG  . LEU A 73  ? 0.2844 0.3479 0.3084 0.0136  -0.0143 0.0117  103 LEU A CG  
495  C CD1 . LEU A 73  ? 0.2257 0.2819 0.2476 0.0164  -0.0113 0.0124  103 LEU A CD1 
496  C CD2 . LEU A 73  ? 0.2403 0.3049 0.2594 0.0114  -0.0168 0.0101  103 LEU A CD2 
497  N N   . ARG A 74  ? 0.2098 0.2794 0.2451 0.0045  -0.0147 0.0066  104 ARG A N   
498  C CA  . ARG A 74  ? 0.2530 0.3196 0.2888 0.0014  -0.0139 0.0042  104 ARG A CA  
499  C C   . ARG A 74  ? 0.1859 0.2600 0.2269 -0.0025 -0.0163 0.0041  104 ARG A C   
500  O O   . ARG A 74  ? 0.2273 0.2992 0.2695 -0.0055 -0.0156 0.0023  104 ARG A O   
501  C CB  . ARG A 74  ? 0.2053 0.2678 0.2427 0.0034  -0.0100 0.0053  104 ARG A CB  
502  C CG  . ARG A 74  ? 0.2031 0.2722 0.2478 0.0050  -0.0084 0.0087  104 ARG A CG  
503  C CD  . ARG A 74  ? 0.2204 0.2844 0.2650 0.0068  -0.0041 0.0093  104 ARG A CD  
504  N NE  . ARG A 74  ? 0.2023 0.2622 0.2457 0.0036  -0.0034 0.0073  104 ARG A NE  
505  C CZ  . ARG A 74  ? 0.2488 0.3127 0.2978 0.0011  -0.0025 0.0082  104 ARG A CZ  
506  N NH1 . ARG A 74  ? 0.1932 0.2662 0.2501 0.0014  -0.0023 0.0110  104 ARG A NH1 
507  N NH2 . ARG A 74  ? 0.2177 0.2765 0.2649 -0.0016 -0.0016 0.0064  104 ARG A NH2 
508  N N   . LYS A 75  ? 0.2555 0.3383 0.2997 -0.0026 -0.0193 0.0061  105 LYS A N   
509  C CA  . LYS A 75  ? 0.2760 0.3667 0.3248 -0.0069 -0.0226 0.0056  105 LYS A CA  
510  C C   . LYS A 75  ? 0.2868 0.3722 0.3303 -0.0114 -0.0241 0.0008  105 LYS A C   
511  O O   . LYS A 75  ? 0.2952 0.3764 0.3313 -0.0113 -0.0252 -0.0015 105 LYS A O   
512  C CB  . LYS A 75  ? 0.2580 0.3582 0.3088 -0.0060 -0.0263 0.0082  105 LYS A CB  
513  C CG  . LYS A 75  ? 0.3778 0.4898 0.4384 -0.0076 -0.0283 0.0110  105 LYS A CG  
514  C CD  . LYS A 75  ? 0.4510 0.5688 0.5114 -0.0133 -0.0334 0.0085  105 LYS A CD  
515  C CE  . LYS A 75  ? 0.4419 0.5730 0.5131 -0.0150 -0.0361 0.0117  105 LYS A CE  
516  N NZ  . LYS A 75  ? 0.7210 0.8581 0.7914 -0.0210 -0.0418 0.0090  105 LYS A NZ  
517  N N   . GLY A 76  ? 0.2913 0.3763 0.3384 -0.0153 -0.0236 -0.0007 106 GLY A N   
518  C CA  . GLY A 76  ? 0.2979 0.3760 0.3401 -0.0194 -0.0242 -0.0053 106 GLY A CA  
519  C C   . GLY A 76  ? 0.2951 0.3624 0.3338 -0.0181 -0.0202 -0.0068 106 GLY A C   
520  O O   . GLY A 76  ? 0.2819 0.3423 0.3160 -0.0207 -0.0202 -0.0104 106 GLY A O   
521  N N   . SER A 77  ? 0.2210 0.2864 0.2613 -0.0143 -0.0169 -0.0040 107 SER A N   
522  C CA  . SER A 77  ? 0.2568 0.3125 0.2934 -0.0128 -0.0135 -0.0049 107 SER A CA  
523  C C   . SER A 77  ? 0.2615 0.3143 0.3009 -0.0165 -0.0121 -0.0057 107 SER A C   
524  O O   . SER A 77  ? 0.2448 0.3039 0.2911 -0.0189 -0.0122 -0.0041 107 SER A O   
525  C CB  . SER A 77  ? 0.1974 0.2522 0.2346 -0.0081 -0.0106 -0.0018 107 SER A CB  
526  O OG  . SER A 77  ? 0.2128 0.2592 0.2467 -0.0071 -0.0077 -0.0023 107 SER A OG  
527  N N   . LEU A 78  ? 0.1971 0.2406 0.2316 -0.0169 -0.0107 -0.0080 108 LEU A N   
528  C CA  . LEU A 78  ? 0.2211 0.2600 0.2575 -0.0199 -0.0087 -0.0085 108 LEU A CA  
529  C C   . LEU A 78  ? 0.2016 0.2369 0.2385 -0.0171 -0.0048 -0.0055 108 LEU A C   
530  O O   . LEU A 78  ? 0.2052 0.2360 0.2431 -0.0191 -0.0027 -0.0052 108 LEU A O   
531  C CB  . LEU A 78  ? 0.2074 0.2374 0.2381 -0.0215 -0.0090 -0.0122 108 LEU A CB  
532  C CG  . LEU A 78  ? 0.2455 0.2774 0.2740 -0.0245 -0.0124 -0.0159 108 LEU A CG  
533  C CD1 . LEU A 78  ? 0.2232 0.2451 0.2455 -0.0248 -0.0116 -0.0195 108 LEU A CD1 
534  C CD2 . LEU A 78  ? 0.1920 0.2303 0.2262 -0.0300 -0.0145 -0.0164 108 LEU A CD2 
535  N N   . ALA A 79  ? 0.2060 0.2429 0.2418 -0.0126 -0.0038 -0.0034 109 ALA A N   
536  C CA  . ALA A 79  ? 0.2097 0.2430 0.2444 -0.0098 -0.0003 -0.0009 109 ALA A CA  
537  C C   . ALA A 79  ? 0.2344 0.2735 0.2759 -0.0108 0.0019  0.0021  109 ALA A C   
538  O O   . ALA A 79  ? 0.2617 0.3094 0.3094 -0.0125 0.0004  0.0028  109 ALA A O   
539  C CB  . ALA A 79  ? 0.1845 0.2170 0.2152 -0.0051 -0.0001 -0.0002 109 ALA A CB  
540  N N   . PRO A 80  ? 0.2122 0.2472 0.2528 -0.0096 0.0057  0.0041  110 PRO A N   
541  C CA  . PRO A 80  ? 0.2265 0.2671 0.2739 -0.0105 0.0086  0.0071  110 PRO A CA  
542  C C   . PRO A 80  ? 0.2182 0.2650 0.2682 -0.0067 0.0100  0.0094  110 PRO A C   
543  O O   . PRO A 80  ? 0.3209 0.3737 0.3776 -0.0071 0.0125  0.0121  110 PRO A O   
544  C CB  . PRO A 80  ? 0.2082 0.2409 0.2519 -0.0102 0.0125  0.0084  110 PRO A CB  
545  C CG  . PRO A 80  ? 0.2388 0.2636 0.2734 -0.0068 0.0117  0.0070  110 PRO A CG  
546  C CD  . PRO A 80  ? 0.2002 0.2257 0.2338 -0.0077 0.0074  0.0038  110 PRO A CD  
547  N N   . GLY A 81  ? 0.2359 0.2811 0.2811 -0.0030 0.0087  0.0087  111 GLY A N   
548  C CA  . GLY A 81  ? 0.2267 0.2764 0.2741 0.0008  0.0104  0.0108  111 GLY A CA  
549  C C   . GLY A 81  ? 0.2978 0.3424 0.3380 0.0045  0.0095  0.0096  111 GLY A C   
550  O O   . GLY A 81  ? 0.1874 0.2278 0.2228 0.0038  0.0068  0.0071  111 GLY A O   
551  N N   . VAL A 82  ? 0.2214 0.2664 0.2613 0.0083  0.0122  0.0112  112 VAL A N   
552  C CA  . VAL A 82  ? 0.2221 0.2627 0.2561 0.0117  0.0118  0.0103  112 VAL A CA  
553  C C   . VAL A 82  ? 0.2737 0.3080 0.3023 0.0145  0.0159  0.0107  112 VAL A C   
554  O O   . VAL A 82  ? 0.2646 0.3009 0.2960 0.0155  0.0197  0.0128  112 VAL A O   
555  C CB  . VAL A 82  ? 0.2235 0.2704 0.2622 0.0138  0.0108  0.0117  112 VAL A CB  
556  C CG1 . VAL A 82  ? 0.2426 0.2839 0.2754 0.0172  0.0113  0.0110  112 VAL A CG1 
557  C CG2 . VAL A 82  ? 0.1896 0.2425 0.2320 0.0110  0.0064  0.0111  112 VAL A CG2 
558  N N   . SER A 83  ? 0.2327 0.2596 0.2533 0.0158  0.0150  0.0088  113 SER A N   
559  C CA  . SER A 83  ? 0.2415 0.2618 0.2552 0.0182  0.0182  0.0087  113 SER A CA  
560  C C   . SER A 83  ? 0.2560 0.2703 0.2628 0.0194  0.0162  0.0064  113 SER A C   
561  O O   . SER A 83  ? 0.2647 0.2790 0.2712 0.0180  0.0125  0.0049  113 SER A O   
562  C CB  . SER A 83  ? 0.2138 0.2305 0.2243 0.0166  0.0196  0.0090  113 SER A CB  
563  O OG  . SER A 83  ? 0.2247 0.2349 0.2272 0.0188  0.0222  0.0088  113 SER A OG  
564  N N   . GLU A 84  ? 0.1905 0.1996 0.1916 0.0220  0.0188  0.0060  114 GLU A N   
565  C CA  . GLU A 84  ? 0.2207 0.2233 0.2144 0.0224  0.0168  0.0036  114 GLU A CA  
566  C C   . GLU A 84  ? 0.2288 0.2281 0.2177 0.0206  0.0146  0.0026  114 GLU A C   
567  O O   . GLU A 84  ? 0.2086 0.2053 0.1943 0.0199  0.0114  0.0008  114 GLU A O   
568  C CB  . GLU A 84  ? 0.2476 0.2447 0.2353 0.0251  0.0202  0.0030  114 GLU A CB  
569  C CG  . GLU A 84  ? 0.2315 0.2295 0.2224 0.0274  0.0216  0.0034  114 GLU A CG  
570  C CD  . GLU A 84  ? 0.2393 0.2296 0.2228 0.0298  0.0246  0.0018  114 GLU A CD  
571  O OE1 . GLU A 84  ? 0.2311 0.2198 0.2124 0.0318  0.0290  0.0026  114 GLU A OE1 
572  O OE2 . GLU A 84  ? 0.2146 0.2002 0.1942 0.0296  0.0227  -0.0003 114 GLU A OE2 
573  N N   . ASP A 85  ? 0.1921 0.1913 0.1806 0.0199  0.0165  0.0040  115 ASP A N   
574  C CA  . ASP A 85  ? 0.1932 0.1897 0.1785 0.0184  0.0147  0.0039  115 ASP A CA  
575  C C   . ASP A 85  ? 0.2517 0.2523 0.2433 0.0161  0.0119  0.0037  115 ASP A C   
576  O O   . ASP A 85  ? 0.2229 0.2266 0.2195 0.0144  0.0128  0.0050  115 ASP A O   
577  C CB  . ASP A 85  ? 0.2203 0.2150 0.2033 0.0186  0.0183  0.0060  115 ASP A CB  
578  C CG  . ASP A 85  ? 0.2630 0.2542 0.2422 0.0175  0.0168  0.0065  115 ASP A CG  
579  O OD1 . ASP A 85  ? 0.2370 0.2278 0.2166 0.0166  0.0130  0.0052  115 ASP A OD1 
580  O OD2 . ASP A 85  ? 0.3083 0.2969 0.2841 0.0178  0.0197  0.0084  115 ASP A OD2 
581  N N   . CYS A 86  ? 0.2003 0.2007 0.1915 0.0157  0.0084  0.0019  116 CYS A N   
582  C CA  . CYS A 86  ? 0.1884 0.1926 0.1849 0.0138  0.0060  0.0012  116 CYS A CA  
583  C C   . CYS A 86  ? 0.1854 0.1874 0.1796 0.0134  0.0029  -0.0004 116 CYS A C   
584  O O   . CYS A 86  ? 0.2398 0.2444 0.2375 0.0121  0.0011  -0.0012 116 CYS A O   
585  C CB  . CYS A 86  ? 0.2160 0.2251 0.2171 0.0141  0.0057  0.0013  116 CYS A CB  
586  S SG  . CYS A 86  ? 0.2017 0.2085 0.1995 0.0159  0.0045  0.0000  116 CYS A SG  
587  N N   . LEU A 87  ? 0.1833 0.1810 0.1720 0.0145  0.0021  -0.0008 117 LEU A N   
588  C CA  . LEU A 87  ? 0.2199 0.2168 0.2077 0.0144  -0.0009 -0.0020 117 LEU A CA  
589  C C   . LEU A 87  ? 0.2304 0.2257 0.2186 0.0138  -0.0011 -0.0014 117 LEU A C   
590  O O   . LEU A 87  ? 0.2245 0.2163 0.2087 0.0146  -0.0012 -0.0004 117 LEU A O   
591  C CB  . LEU A 87  ? 0.1830 0.1767 0.1652 0.0155  -0.0021 -0.0027 117 LEU A CB  
592  C CG  . LEU A 87  ? 0.2139 0.2077 0.1954 0.0159  -0.0017 -0.0037 117 LEU A CG  
593  C CD1 . LEU A 87  ? 0.2270 0.2172 0.2028 0.0163  -0.0032 -0.0049 117 LEU A CD1 
594  C CD2 . LEU A 87  ? 0.1773 0.1749 0.1640 0.0151  -0.0027 -0.0043 117 LEU A CD2 
595  N N   . TYR A 88  ? 0.1778 0.1755 0.1707 0.0123  -0.0012 -0.0019 118 TYR A N   
596  C CA  . TYR A 88  ? 0.1798 0.1753 0.1737 0.0114  -0.0010 -0.0016 118 TYR A CA  
597  C C   . TYR A 88  ? 0.2229 0.2197 0.2194 0.0108  -0.0027 -0.0034 118 TYR A C   
598  O O   . TYR A 88  ? 0.2115 0.2120 0.2099 0.0103  -0.0036 -0.0047 118 TYR A O   
599  C CB  . TYR A 88  ? 0.2229 0.2190 0.2195 0.0096  0.0013  -0.0005 118 TYR A CB  
600  C CG  . TYR A 88  ? 0.2355 0.2300 0.2294 0.0104  0.0038  0.0016  118 TYR A CG  
601  C CD1 . TYR A 88  ? 0.2281 0.2178 0.2180 0.0113  0.0049  0.0033  118 TYR A CD1 
602  C CD2 . TYR A 88  ? 0.2019 0.1998 0.1972 0.0107  0.0054  0.0021  118 TYR A CD2 
603  C CE1 . TYR A 88  ? 0.2814 0.2694 0.2678 0.0121  0.0075  0.0053  118 TYR A CE1 
604  C CE2 . TYR A 88  ? 0.2279 0.2240 0.2203 0.0117  0.0083  0.0040  118 TYR A CE2 
605  C CZ  . TYR A 88  ? 0.2312 0.2224 0.2189 0.0123  0.0094  0.0055  118 TYR A CZ  
606  O OH  . TYR A 88  ? 0.2853 0.2747 0.2693 0.0134  0.0126  0.0074  118 TYR A OH  
607  N N   . LEU A 89  ? 0.2107 0.2042 0.2069 0.0111  -0.0028 -0.0035 119 LEU A N   
608  C CA  . LEU A 89  ? 0.2158 0.2097 0.2141 0.0107  -0.0037 -0.0054 119 LEU A CA  
609  C C   . LEU A 89  ? 0.2207 0.2107 0.2199 0.0095  -0.0024 -0.0057 119 LEU A C   
610  O O   . LEU A 89  ? 0.2296 0.2161 0.2279 0.0092  -0.0009 -0.0040 119 LEU A O   
611  C CB  . LEU A 89  ? 0.1868 0.1806 0.1842 0.0130  -0.0053 -0.0056 119 LEU A CB  
612  C CG  . LEU A 89  ? 0.2303 0.2208 0.2254 0.0152  -0.0058 -0.0037 119 LEU A CG  
613  C CD1 . LEU A 89  ? 0.2006 0.1868 0.1966 0.0159  -0.0047 -0.0034 119 LEU A CD1 
614  C CD2 . LEU A 89  ? 0.2548 0.2481 0.2502 0.0168  -0.0080 -0.0039 119 LEU A CD2 
615  N N   . ASN A 90  ? 0.2236 0.2137 0.2243 0.0087  -0.0027 -0.0080 120 ASN A N   
616  C CA  . ASN A 90  ? 0.1916 0.1775 0.1930 0.0070  -0.0015 -0.0093 120 ASN A CA  
617  C C   . ASN A 90  ? 0.2256 0.2091 0.2267 0.0088  -0.0015 -0.0109 120 ASN A C   
618  O O   . ASN A 90  ? 0.2415 0.2287 0.2429 0.0100  -0.0025 -0.0119 120 ASN A O   
619  C CB  . ASN A 90  ? 0.1873 0.1764 0.1905 0.0034  -0.0017 -0.0112 120 ASN A CB  
620  C CG  . ASN A 90  ? 0.2083 0.2025 0.2129 0.0025  -0.0020 -0.0096 120 ASN A CG  
621  O OD1 . ASN A 90  ? 0.2284 0.2214 0.2333 0.0022  -0.0007 -0.0075 120 ASN A OD1 
622  N ND2 . ASN A 90  ? 0.1783 0.1781 0.1837 0.0024  -0.0034 -0.0103 120 ASN A ND2 
623  N N   . VAL A 91  ? 0.2331 0.2102 0.2339 0.0092  0.0000  -0.0110 121 VAL A N   
624  C CA  . VAL A 91  ? 0.2188 0.1926 0.2196 0.0117  0.0007  -0.0120 121 VAL A CA  
625  C C   . VAL A 91  ? 0.2481 0.2156 0.2485 0.0097  0.0026  -0.0146 121 VAL A C   
626  O O   . VAL A 91  ? 0.2460 0.2086 0.2463 0.0078  0.0039  -0.0139 121 VAL A O   
627  C CB  . VAL A 91  ? 0.2484 0.2196 0.2490 0.0154  0.0008  -0.0088 121 VAL A CB  
628  C CG1 . VAL A 91  ? 0.2046 0.1734 0.2064 0.0186  0.0016  -0.0095 121 VAL A CG1 
629  C CG2 . VAL A 91  ? 0.1959 0.1727 0.1960 0.0167  -0.0014 -0.0067 121 VAL A CG2 
630  N N   . TRP A 92  ? 0.2073 0.1747 0.2074 0.0099  0.0031  -0.0178 122 TRP A N   
631  C CA  . TRP A 92  ? 0.2274 0.1875 0.2261 0.0087  0.0052  -0.0208 122 TRP A CA  
632  C C   . TRP A 92  ? 0.2610 0.2173 0.2601 0.0132  0.0070  -0.0208 122 TRP A C   
633  O O   . TRP A 92  ? 0.2345 0.1961 0.2347 0.0159  0.0064  -0.0205 122 TRP A O   
634  C CB  . TRP A 92  ? 0.2184 0.1808 0.2154 0.0052  0.0046  -0.0250 122 TRP A CB  
635  C CG  . TRP A 92  ? 0.2208 0.1863 0.2182 0.0005  0.0030  -0.0253 122 TRP A CG  
636  C CD1 . TRP A 92  ? 0.2208 0.1819 0.2178 -0.0037 0.0035  -0.0274 122 TRP A CD1 
637  C CD2 . TRP A 92  ? 0.2064 0.1803 0.2052 -0.0004 0.0008  -0.0235 122 TRP A CD2 
638  N NE1 . TRP A 92  ? 0.2166 0.1840 0.2154 -0.0072 0.0015  -0.0267 122 TRP A NE1 
639  C CE2 . TRP A 92  ? 0.2109 0.1859 0.2107 -0.0049 0.0000  -0.0242 122 TRP A CE2 
640  C CE3 . TRP A 92  ? 0.1988 0.1791 0.1984 0.0020  -0.0005 -0.0213 122 TRP A CE3 
641  C CZ2 . TRP A 92  ? 0.2017 0.1845 0.2037 -0.0064 -0.0018 -0.0225 122 TRP A CZ2 
642  C CZ3 . TRP A 92  ? 0.1933 0.1800 0.1943 0.0004  -0.0021 -0.0199 122 TRP A CZ3 
643  C CH2 . TRP A 92  ? 0.1947 0.1828 0.1969 -0.0035 -0.0027 -0.0204 122 TRP A CH2 
644  N N   . ALA A 93  ? 0.2588 0.2061 0.2575 0.0141  0.0094  -0.0209 123 ALA A N   
645  C CA  . ALA A 93  ? 0.2934 0.2371 0.2931 0.0190  0.0114  -0.0205 123 ALA A CA  
646  C C   . ALA A 93  ? 0.3234 0.2559 0.3213 0.0186  0.0147  -0.0231 123 ALA A C   
647  O O   . ALA A 93  ? 0.3173 0.2437 0.3142 0.0155  0.0153  -0.0229 123 ALA A O   
648  C CB  . ALA A 93  ? 0.2309 0.1759 0.2329 0.0232  0.0106  -0.0154 123 ALA A CB  
649  N N   . PRO A 94  ? 0.2739 0.2031 0.2715 0.0216  0.0172  -0.0254 124 PRO A N   
650  C CA  . PRO A 94  ? 0.3503 0.2673 0.3459 0.0217  0.0209  -0.0279 124 PRO A CA  
651  C C   . PRO A 94  ? 0.4072 0.3171 0.4044 0.0238  0.0220  -0.0236 124 PRO A C   
652  O O   . PRO A 94  ? 0.3472 0.2608 0.3473 0.0281  0.0210  -0.0187 124 PRO A O   
653  C CB  . PRO A 94  ? 0.3187 0.2352 0.3148 0.0265  0.0235  -0.0297 124 PRO A CB  
654  C CG  . PRO A 94  ? 0.2968 0.2253 0.2938 0.0264  0.0212  -0.0299 124 PRO A CG  
655  C CD  . PRO A 94  ? 0.2543 0.1904 0.2535 0.0250  0.0172  -0.0258 124 PRO A CD  
656  N N   . SER A 95  ? 0.4035 0.3031 0.3986 0.0205  0.0240  -0.0254 125 SER A N   
657  C CA  . SER A 95  ? 0.4866 0.3782 0.4827 0.0220  0.0255  -0.0212 125 SER A CA  
658  C C   . SER A 95  ? 0.4412 0.3281 0.4392 0.0293  0.0281  -0.0186 125 SER A C   
659  O O   . SER A 95  ? 0.4788 0.3620 0.4763 0.0317  0.0307  -0.0219 125 SER A O   
660  C CB  . SER A 95  ? 0.4749 0.3554 0.4686 0.0167  0.0277  -0.0241 125 SER A CB  
661  O OG  . SER A 95  ? 0.5821 0.4555 0.5768 0.0176  0.0291  -0.0193 125 SER A OG  
662  N N   . GLY A 96  ? 0.5273 0.4146 0.5274 0.0330  0.0274  -0.0124 126 GLY A N   
663  C CA  . GLY A 96  ? 0.5942 0.4783 0.5970 0.0403  0.0293  -0.0090 126 GLY A CA  
664  C C   . GLY A 96  ? 0.5992 0.4941 0.6054 0.0448  0.0277  -0.0085 126 GLY A C   
665  O O   . GLY A 96  ? 0.6129 0.5058 0.6222 0.0508  0.0299  -0.0069 126 GLY A O   
666  N N   . ALA A 97  ? 0.6053 0.5117 0.6116 0.0420  0.0242  -0.0096 127 ALA A N   
667  C CA  . ALA A 97  ? 0.4665 0.3839 0.4767 0.0457  0.0225  -0.0086 127 ALA A CA  
668  C C   . ALA A 97  ? 0.4309 0.3522 0.4445 0.0507  0.0204  -0.0021 127 ALA A C   
669  O O   . ALA A 97  ? 0.4389 0.3604 0.4508 0.0494  0.0181  0.0014  127 ALA A O   
670  C CB  . ALA A 97  ? 0.3601 0.2879 0.3694 0.0413  0.0192  -0.0108 127 ALA A CB  
671  N N   . LYS A 98  ? 0.3633 0.2882 0.3819 0.0565  0.0212  -0.0004 128 LYS A N   
672  C CA  . LYS A 98  ? 0.4243 0.3541 0.4468 0.0616  0.0187  0.0058  128 LYS A CA  
673  C C   . LYS A 98  ? 0.3763 0.3201 0.4011 0.0606  0.0139  0.0069  128 LYS A C   
674  O O   . LYS A 98  ? 0.3623 0.3118 0.3869 0.0572  0.0134  0.0030  128 LYS A O   
675  C CB  . LYS A 98  ? 0.3451 0.2725 0.3729 0.0686  0.0220  0.0074  128 LYS A CB  
676  C CG  . LYS A 98  ? 0.3905 0.3027 0.4160 0.0705  0.0267  0.0074  128 LYS A CG  
677  C CD  . LYS A 98  ? 0.4534 0.3630 0.4844 0.0781  0.0304  0.0089  128 LYS A CD  
678  C CE  . LYS A 98  ? 0.3948 0.3067 0.4274 0.0782  0.0335  0.0033  128 LYS A CE  
679  N NZ  . LYS A 98  ? 0.5317 0.4331 0.5575 0.0728  0.0368  -0.0034 128 LYS A NZ  
680  N N   . PRO A 99  ? 0.3548 0.3040 0.3812 0.0632  0.0103  0.0122  129 PRO A N   
681  C CA  . PRO A 99  ? 0.3041 0.2658 0.3323 0.0617  0.0055  0.0130  129 PRO A CA  
682  C C   . PRO A 99  ? 0.3252 0.2954 0.3598 0.0635  0.0059  0.0112  129 PRO A C   
683  O O   . PRO A 99  ? 0.3242 0.2949 0.3644 0.0687  0.0080  0.0128  129 PRO A O   
684  C CB  . PRO A 99  ? 0.2966 0.2608 0.3253 0.0652  0.0020  0.0192  129 PRO A CB  
685  C CG  . PRO A 99  ? 0.3316 0.2838 0.3562 0.0663  0.0046  0.0214  129 PRO A CG  
686  C CD  . PRO A 99  ? 0.3110 0.2542 0.3365 0.0668  0.0101  0.0177  129 PRO A CD  
687  N N   . GLY A 100 ? 0.3787 0.3558 0.4128 0.0592  0.0043  0.0081  130 GLY A N   
688  C CA  . GLY A 100 ? 0.2978 0.2833 0.3376 0.0600  0.0048  0.0065  130 GLY A CA  
689  C C   . GLY A 100 ? 0.3548 0.3356 0.3949 0.0608  0.0101  0.0024  130 GLY A C   
690  O O   . GLY A 100 ? 0.3277 0.3150 0.3730 0.0624  0.0115  0.0015  130 GLY A O   
691  N N   . GLN A 101 ? 0.3184 0.2879 0.3529 0.0593  0.0132  -0.0002 131 GLN A N   
692  C CA  . GLN A 101 ? 0.3150 0.2784 0.3489 0.0604  0.0185  -0.0043 131 GLN A CA  
693  C C   . GLN A 101 ? 0.3156 0.2833 0.3473 0.0563  0.0190  -0.0088 131 GLN A C   
694  O O   . GLN A 101 ? 0.3135 0.2844 0.3481 0.0584  0.0219  -0.0105 131 GLN A O   
695  C CB  . GLN A 101 ? 0.2866 0.2362 0.3150 0.0595  0.0213  -0.0060 131 GLN A CB  
696  C CG  . GLN A 101 ? 0.2957 0.2376 0.3217 0.0598  0.0266  -0.0110 131 GLN A CG  
697  C CD  . GLN A 101 ? 0.3432 0.2706 0.3648 0.0594  0.0297  -0.0124 131 GLN A CD  
698  O OE1 . GLN A 101 ? 0.4027 0.3259 0.4232 0.0590  0.0280  -0.0091 131 GLN A OE1 
699  N NE2 . GLN A 101 ? 0.2886 0.2078 0.3070 0.0593  0.0343  -0.0174 131 GLN A NE2 
700  N N   . TYR A 102 ? 0.2303 0.1983 0.2568 0.0506  0.0165  -0.0106 132 TYR A N   
701  C CA  . TYR A 102 ? 0.2749 0.2450 0.2980 0.0466  0.0172  -0.0149 132 TYR A CA  
702  C C   . TYR A 102 ? 0.2650 0.2461 0.2902 0.0444  0.0137  -0.0137 132 TYR A C   
703  O O   . TYR A 102 ? 0.2152 0.2009 0.2426 0.0444  0.0100  -0.0102 132 TYR A O   
704  C CB  . TYR A 102 ? 0.2734 0.2360 0.2896 0.0416  0.0172  -0.0179 132 TYR A CB  
705  C CG  . TYR A 102 ? 0.2906 0.2412 0.3036 0.0425  0.0211  -0.0205 132 TYR A CG  
706  C CD1 . TYR A 102 ? 0.3100 0.2571 0.3212 0.0434  0.0251  -0.0246 132 TYR A CD1 
707  C CD2 . TYR A 102 ? 0.3052 0.2477 0.3169 0.0422  0.0211  -0.0189 132 TYR A CD2 
708  C CE1 . TYR A 102 ? 0.2899 0.2250 0.2977 0.0440  0.0289  -0.0275 132 TYR A CE1 
709  C CE2 . TYR A 102 ? 0.3546 0.2852 0.3635 0.0427  0.0249  -0.0214 132 TYR A CE2 
710  C CZ  . TYR A 102 ? 0.3649 0.2917 0.3718 0.0435  0.0287  -0.0259 132 TYR A CZ  
711  O OH  . TYR A 102 ? 0.3786 0.2925 0.3822 0.0438  0.0327  -0.0289 132 TYR A OH  
712  N N   . PRO A 103 ? 0.2330 0.2180 0.2572 0.0425  0.0149  -0.0164 133 PRO A N   
713  C CA  . PRO A 103 ? 0.2050 0.1986 0.2299 0.0396  0.0118  -0.0157 133 PRO A CA  
714  C C   . PRO A 103 ? 0.2020 0.1934 0.2215 0.0349  0.0091  -0.0165 133 PRO A C   
715  O O   . PRO A 103 ? 0.2066 0.1906 0.2217 0.0333  0.0100  -0.0184 133 PRO A O   
716  C CB  . PRO A 103 ? 0.2055 0.2021 0.2299 0.0392  0.0148  -0.0184 133 PRO A CB  
717  C CG  . PRO A 103 ? 0.2250 0.2125 0.2445 0.0397  0.0186  -0.0221 133 PRO A CG  
718  C CD  . PRO A 103 ? 0.2203 0.2015 0.2419 0.0431  0.0194  -0.0204 133 PRO A CD  
719  N N   . VAL A 104 ? 0.1946 0.1925 0.2150 0.0328  0.0060  -0.0150 134 VAL A N   
720  C CA  . VAL A 104 ? 0.2031 0.1999 0.2194 0.0290  0.0036  -0.0151 134 VAL A CA  
721  C C   . VAL A 104 ? 0.2086 0.2100 0.2232 0.0260  0.0032  -0.0167 134 VAL A C   
722  O O   . VAL A 104 ? 0.2142 0.2215 0.2318 0.0266  0.0032  -0.0159 134 VAL A O   
723  C CB  . VAL A 104 ? 0.1957 0.1948 0.2135 0.0292  0.0002  -0.0118 134 VAL A CB  
724  C CG1 . VAL A 104 ? 0.1992 0.1965 0.2127 0.0258  -0.0015 -0.0120 134 VAL A CG1 
725  C CG2 . VAL A 104 ? 0.1948 0.1903 0.2144 0.0327  0.0004  -0.0095 134 VAL A CG2 
726  N N   . MET A 105 ? 0.1875 0.1862 0.1974 0.0228  0.0029  -0.0185 135 MET A N   
727  C CA  . MET A 105 ? 0.1837 0.1865 0.1917 0.0201  0.0021  -0.0193 135 MET A CA  
728  C C   . MET A 105 ? 0.1800 0.1832 0.1867 0.0178  -0.0005 -0.0179 135 MET A C   
729  O O   . MET A 105 ? 0.1823 0.1813 0.1870 0.0165  -0.0007 -0.0184 135 MET A O   
730  C CB  . MET A 105 ? 0.1884 0.1888 0.1920 0.0185  0.0040  -0.0226 135 MET A CB  
731  C CG  . MET A 105 ? 0.1938 0.1927 0.1977 0.0210  0.0074  -0.0244 135 MET A CG  
732  S SD  . MET A 105 ? 0.2015 0.1966 0.1984 0.0190  0.0096  -0.0290 135 MET A SD  
733  C CE  . MET A 105 ? 0.1967 0.1992 0.1916 0.0168  0.0082  -0.0282 135 MET A CE  
734  N N   . VAL A 106 ? 0.1749 0.1828 0.1829 0.0173  -0.0022 -0.0162 136 VAL A N   
735  C CA  . VAL A 106 ? 0.2071 0.2155 0.2143 0.0157  -0.0042 -0.0148 136 VAL A CA  
736  C C   . VAL A 106 ? 0.2297 0.2410 0.2351 0.0136  -0.0045 -0.0153 136 VAL A C   
737  O O   . VAL A 106 ? 0.2016 0.2166 0.2080 0.0136  -0.0045 -0.0148 136 VAL A O   
738  C CB  . VAL A 106 ? 0.1939 0.2044 0.2032 0.0168  -0.0059 -0.0126 136 VAL A CB  
739  C CG1 . VAL A 106 ? 0.1817 0.1915 0.1891 0.0155  -0.0074 -0.0115 136 VAL A CG1 
740  C CG2 . VAL A 106 ? 0.1719 0.1805 0.1832 0.0193  -0.0060 -0.0116 136 VAL A CG2 
741  N N   . TRP A 107 ? 0.1911 0.2011 0.1944 0.0117  -0.0049 -0.0159 137 TRP A N   
742  C CA  . TRP A 107 ? 0.1692 0.1822 0.1709 0.0099  -0.0054 -0.0161 137 TRP A CA  
743  C C   . TRP A 107 ? 0.1828 0.1981 0.1854 0.0097  -0.0066 -0.0139 137 TRP A C   
744  O O   . TRP A 107 ? 0.1867 0.2003 0.1898 0.0100  -0.0071 -0.0128 137 TRP A O   
745  C CB  . TRP A 107 ? 0.1760 0.1874 0.1758 0.0078  -0.0055 -0.0178 137 TRP A CB  
746  C CG  . TRP A 107 ? 0.1719 0.1872 0.1702 0.0059  -0.0066 -0.0178 137 TRP A CG  
747  C CD1 . TRP A 107 ? 0.2308 0.2481 0.2298 0.0044  -0.0079 -0.0167 137 TRP A CD1 
748  C CD2 . TRP A 107 ? 0.1936 0.2118 0.1895 0.0057  -0.0064 -0.0185 137 TRP A CD2 
749  N NE1 . TRP A 107 ? 0.1989 0.2205 0.1966 0.0034  -0.0089 -0.0166 137 TRP A NE1 
750  C CE2 . TRP A 107 ? 0.1983 0.2201 0.1934 0.0041  -0.0081 -0.0176 137 TRP A CE2 
751  C CE3 . TRP A 107 ? 0.1779 0.1961 0.1723 0.0068  -0.0049 -0.0195 137 TRP A CE3 
752  C CZ2 . TRP A 107 ? 0.1747 0.2000 0.1670 0.0036  -0.0085 -0.0176 137 TRP A CZ2 
753  C CZ3 . TRP A 107 ? 0.1772 0.1985 0.1685 0.0062  -0.0048 -0.0197 137 TRP A CZ3 
754  C CH2 . TRP A 107 ? 0.1963 0.2209 0.1862 0.0046  -0.0068 -0.0187 137 TRP A CH2 
755  N N   . VAL A 108 ? 0.2141 0.2327 0.2162 0.0093  -0.0068 -0.0133 138 VAL A N   
756  C CA  . VAL A 108 ? 0.2126 0.2328 0.2153 0.0092  -0.0075 -0.0112 138 VAL A CA  
757  C C   . VAL A 108 ? 0.1961 0.2193 0.1976 0.0082  -0.0080 -0.0108 138 VAL A C   
758  O O   . VAL A 108 ? 0.1900 0.2154 0.1903 0.0081  -0.0077 -0.0107 138 VAL A O   
759  C CB  . VAL A 108 ? 0.1892 0.2102 0.1932 0.0100  -0.0073 -0.0101 138 VAL A CB  
760  C CG1 . VAL A 108 ? 0.1752 0.1958 0.1793 0.0101  -0.0078 -0.0084 138 VAL A CG1 
761  C CG2 . VAL A 108 ? 0.1894 0.2088 0.1949 0.0110  -0.0074 -0.0106 138 VAL A CG2 
762  N N   . TYR A 109 ? 0.1727 0.1965 0.1748 0.0074  -0.0087 -0.0103 139 TYR A N   
763  C CA  . TYR A 109 ? 0.2014 0.2291 0.2031 0.0065  -0.0096 -0.0095 139 TYR A CA  
764  C C   . TYR A 109 ? 0.1875 0.2172 0.1898 0.0077  -0.0095 -0.0069 139 TYR A C   
765  O O   . TYR A 109 ? 0.1692 0.1966 0.1724 0.0089  -0.0088 -0.0059 139 TYR A O   
766  C CB  . TYR A 109 ? 0.1773 0.2060 0.1808 0.0053  -0.0103 -0.0094 139 TYR A CB  
767  C CG  . TYR A 109 ? 0.2008 0.2281 0.2064 0.0064  -0.0095 -0.0076 139 TYR A CG  
768  C CD1 . TYR A 109 ? 0.1968 0.2263 0.2038 0.0078  -0.0093 -0.0052 139 TYR A CD1 
769  C CD2 . TYR A 109 ? 0.1758 0.1994 0.1817 0.0064  -0.0087 -0.0083 139 TYR A CD2 
770  C CE1 . TYR A 109 ? 0.2113 0.2389 0.2195 0.0090  -0.0081 -0.0040 139 TYR A CE1 
771  C CE2 . TYR A 109 ? 0.1938 0.2159 0.2005 0.0075  -0.0077 -0.0068 139 TYR A CE2 
772  C CZ  . TYR A 109 ? 0.1956 0.2196 0.2032 0.0087  -0.0073 -0.0049 139 TYR A CZ  
773  O OH  . TYR A 109 ? 0.2045 0.2264 0.2121 0.0100  -0.0060 -0.0038 139 TYR A OH  
774  N N   . GLY A 110 ? 0.1624 0.1960 0.1639 0.0074  -0.0104 -0.0058 140 GLY A N   
775  C CA  . GLY A 110 ? 0.1622 0.1975 0.1642 0.0088  -0.0102 -0.0028 140 GLY A CA  
776  C C   . GLY A 110 ? 0.2302 0.2693 0.2346 0.0091  -0.0112 -0.0008 140 GLY A C   
777  O O   . GLY A 110 ? 0.4111 0.4536 0.4158 0.0076  -0.0128 -0.0015 140 GLY A O   
778  N N   . GLY A 111 ? 0.2714 0.3097 0.2776 0.0111  -0.0103 0.0017  141 GLY A N   
779  C CA  . GLY A 111 ? 0.2161 0.2584 0.2254 0.0122  -0.0107 0.0043  141 GLY A CA  
780  C C   . GLY A 111 ? 0.2067 0.2474 0.2164 0.0148  -0.0093 0.0073  141 GLY A C   
781  O O   . GLY A 111 ? 0.2333 0.2738 0.2458 0.0167  -0.0082 0.0091  141 GLY A O   
782  N N   . GLY A 112 ? 0.2195 0.2587 0.2266 0.0149  -0.0090 0.0079  142 GLY A N   
783  C CA  . GLY A 112 ? 0.2442 0.2808 0.2515 0.0171  -0.0075 0.0109  142 GLY A CA  
784  C C   . GLY A 112 ? 0.2452 0.2757 0.2534 0.0181  -0.0054 0.0103  142 GLY A C   
785  O O   . GLY A 112 ? 0.2892 0.3172 0.2982 0.0203  -0.0039 0.0128  142 GLY A O   
786  N N   . PHE A 113 ? 0.2059 0.2336 0.2135 0.0168  -0.0053 0.0072  143 PHE A N   
787  C CA  . PHE A 113 ? 0.2367 0.2588 0.2442 0.0175  -0.0037 0.0063  143 PHE A CA  
788  C C   . PHE A 113 ? 0.2560 0.2789 0.2658 0.0198  -0.0024 0.0081  143 PHE A C   
789  O O   . PHE A 113 ? 0.2656 0.2834 0.2747 0.0214  -0.0004 0.0083  143 PHE A O   
790  C CB  . PHE A 113 ? 0.2347 0.2513 0.2406 0.0175  -0.0025 0.0064  143 PHE A CB  
791  C CG  . PHE A 113 ? 0.2368 0.2532 0.2416 0.0154  -0.0033 0.0047  143 PHE A CG  
792  C CD1 . PHE A 113 ? 0.2445 0.2593 0.2487 0.0139  -0.0040 0.0019  143 PHE A CD1 
793  C CD2 . PHE A 113 ? 0.2621 0.2803 0.2667 0.0150  -0.0032 0.0064  143 PHE A CD2 
794  C CE1 . PHE A 113 ? 0.2494 0.2649 0.2535 0.0123  -0.0046 0.0008  143 PHE A CE1 
795  C CE2 . PHE A 113 ? 0.1962 0.2148 0.2004 0.0132  -0.0034 0.0051  143 PHE A CE2 
796  C CZ  . PHE A 113 ? 0.1665 0.1840 0.1709 0.0119  -0.0041 0.0022  143 PHE A CZ  
797  N N   . ALA A 114 ? 0.2247 0.2540 0.2371 0.0201  -0.0035 0.0095  144 ALA A N   
798  C CA  . ALA A 114 ? 0.2566 0.2886 0.2727 0.0223  -0.0024 0.0116  144 ALA A CA  
799  C C   . ALA A 114 ? 0.2416 0.2779 0.2601 0.0209  -0.0031 0.0106  144 ALA A C   
800  O O   . ALA A 114 ? 0.2032 0.2408 0.2248 0.0225  -0.0014 0.0119  144 ALA A O   
801  C CB  . ALA A 114 ? 0.2081 0.2453 0.2269 0.0242  -0.0030 0.0155  144 ALA A CB  
802  N N   . GLY A 115 ? 0.2154 0.2534 0.2327 0.0180  -0.0051 0.0084  145 GLY A N   
803  C CA  . GLY A 115 ? 0.2549 0.2960 0.2744 0.0162  -0.0057 0.0073  145 GLY A CA  
804  C C   . GLY A 115 ? 0.2820 0.3224 0.2990 0.0132  -0.0075 0.0044  145 GLY A C   
805  O O   . GLY A 115 ? 0.3219 0.3589 0.3354 0.0129  -0.0078 0.0030  145 GLY A O   
806  N N   . GLY A 116 ? 0.2261 0.2699 0.2453 0.0111  -0.0084 0.0036  146 GLY A N   
807  C CA  . GLY A 116 ? 0.2218 0.2645 0.2387 0.0083  -0.0099 0.0007  146 GLY A CA  
808  C C   . GLY A 116 ? 0.1872 0.2255 0.2038 0.0073  -0.0085 -0.0009 146 GLY A C   
809  O O   . GLY A 116 ? 0.1942 0.2299 0.2113 0.0088  -0.0065 0.0001  146 GLY A O   
810  N N   . THR A 117 ? 0.1737 0.2108 0.1890 0.0049  -0.0095 -0.0033 147 THR A N   
811  C CA  . THR A 117 ? 0.1913 0.2239 0.2061 0.0038  -0.0084 -0.0045 147 THR A CA  
812  C C   . THR A 117 ? 0.1731 0.2027 0.1852 0.0021  -0.0092 -0.0074 147 THR A C   
813  O O   . THR A 117 ? 0.2076 0.2398 0.2188 0.0007  -0.0109 -0.0086 147 THR A O   
814  C CB  . THR A 117 ? 0.1908 0.2265 0.2099 0.0022  -0.0078 -0.0035 147 THR A CB  
815  O OG1 . THR A 117 ? 0.2299 0.2605 0.2481 0.0009  -0.0066 -0.0047 147 THR A OG1 
816  C CG2 . THR A 117 ? 0.1778 0.2196 0.1996 -0.0006 -0.0102 -0.0040 147 THR A CG2 
817  N N   . ALA A 118 ? 0.1710 0.1950 0.1814 0.0024  -0.0080 -0.0083 148 ALA A N   
818  C CA  . ALA A 118 ? 0.1738 0.1942 0.1823 0.0011  -0.0083 -0.0109 148 ALA A CA  
819  C C   . ALA A 118 ? 0.2260 0.2465 0.2361 -0.0022 -0.0086 -0.0121 148 ALA A C   
820  O O   . ALA A 118 ? 0.2125 0.2306 0.2207 -0.0039 -0.0090 -0.0147 148 ALA A O   
821  C CB  . ALA A 118 ? 0.1749 0.1894 0.1815 0.0028  -0.0070 -0.0109 148 ALA A CB  
822  N N   . ALA A 119 ? 0.2069 0.2303 0.2206 -0.0034 -0.0082 -0.0103 149 ALA A N   
823  C CA  . ALA A 119 ? 0.1971 0.2207 0.2133 -0.0071 -0.0083 -0.0113 149 ALA A CA  
824  C C   . ALA A 119 ? 0.2239 0.2535 0.2414 -0.0099 -0.0110 -0.0126 149 ALA A C   
825  O O   . ALA A 119 ? 0.2554 0.2901 0.2775 -0.0124 -0.0117 -0.0117 149 ALA A O   
826  C CB  . ALA A 119 ? 0.1736 0.1984 0.1938 -0.0073 -0.0065 -0.0087 149 ALA A CB  
827  N N   . MET A 120 ? 0.2460 0.2757 0.2597 -0.0095 -0.0124 -0.0145 150 MET A N   
828  C CA  . MET A 120 ? 0.2098 0.2443 0.2230 -0.0125 -0.0152 -0.0162 150 MET A CA  
829  C C   . MET A 120 ? 0.2372 0.2660 0.2472 -0.0156 -0.0153 -0.0203 150 MET A C   
830  O O   . MET A 120 ? 0.2214 0.2431 0.2278 -0.0140 -0.0134 -0.0219 150 MET A O   
831  C CB  . MET A 120 ? 0.2127 0.2508 0.2228 -0.0105 -0.0166 -0.0158 150 MET A CB  
832  C CG  . MET A 120 ? 0.2807 0.3246 0.2941 -0.0077 -0.0167 -0.0118 150 MET A CG  
833  S SD  . MET A 120 ? 0.3673 0.4196 0.3882 -0.0096 -0.0181 -0.0092 150 MET A SD  
834  C CE  . MET A 120 ? 0.3002 0.3582 0.3228 -0.0054 -0.0182 -0.0050 150 MET A CE  
835  N N   . PRO A 121 ? 0.2971 0.3289 0.3082 -0.0201 -0.0174 -0.0221 151 PRO A N   
836  C CA  . PRO A 121 ? 0.2684 0.2935 0.2756 -0.0233 -0.0174 -0.0266 151 PRO A CA  
837  C C   . PRO A 121 ? 0.2736 0.2951 0.2737 -0.0216 -0.0172 -0.0295 151 PRO A C   
838  O O   . PRO A 121 ? 0.2448 0.2580 0.2411 -0.0221 -0.0154 -0.0327 151 PRO A O   
839  C CB  . PRO A 121 ? 0.2489 0.2799 0.2586 -0.0287 -0.0206 -0.0280 151 PRO A CB  
840  C CG  . PRO A 121 ? 0.3243 0.3663 0.3390 -0.0275 -0.0227 -0.0239 151 PRO A CG  
841  C CD  . PRO A 121 ? 0.2664 0.3075 0.2830 -0.0224 -0.0199 -0.0201 151 PRO A CD  
842  N N   . TYR A 122 ? 0.2340 0.2610 0.2320 -0.0194 -0.0185 -0.0281 152 TYR A N   
843  C CA  . TYR A 122 ? 0.2706 0.2946 0.2621 -0.0176 -0.0177 -0.0302 152 TYR A CA  
844  C C   . TYR A 122 ? 0.2533 0.2730 0.2447 -0.0130 -0.0146 -0.0288 152 TYR A C   
845  O O   . TYR A 122 ? 0.2400 0.2576 0.2270 -0.0111 -0.0134 -0.0301 152 TYR A O   
846  C CB  . TYR A 122 ? 0.2958 0.3274 0.2846 -0.0175 -0.0203 -0.0292 152 TYR A CB  
847  C CG  . TYR A 122 ? 0.2437 0.2832 0.2378 -0.0157 -0.0217 -0.0243 152 TYR A CG  
848  C CD1 . TYR A 122 ? 0.2698 0.3096 0.2647 -0.0115 -0.0200 -0.0212 152 TYR A CD1 
849  C CD2 . TYR A 122 ? 0.2954 0.3421 0.2939 -0.0184 -0.0246 -0.0229 152 TYR A CD2 
850  C CE1 . TYR A 122 ? 0.2908 0.3366 0.2901 -0.0097 -0.0208 -0.0170 152 TYR A CE1 
851  C CE2 . TYR A 122 ? 0.2739 0.3276 0.2774 -0.0162 -0.0254 -0.0183 152 TYR A CE2 
852  C CZ  . TYR A 122 ? 0.3035 0.3562 0.3071 -0.0117 -0.0233 -0.0155 152 TYR A CZ  
853  O OH  . TYR A 122 ? 0.3557 0.4141 0.3640 -0.0094 -0.0237 -0.0112 152 TYR A OH  
854  N N   . TYR A 123 ? 0.2256 0.2442 0.2216 -0.0112 -0.0132 -0.0260 153 TYR A N   
855  C CA  . TYR A 123 ? 0.2077 0.2217 0.2037 -0.0075 -0.0107 -0.0250 153 TYR A CA  
856  C C   . TYR A 123 ? 0.2505 0.2568 0.2470 -0.0078 -0.0088 -0.0263 153 TYR A C   
857  O O   . TYR A 123 ? 0.2482 0.2512 0.2456 -0.0048 -0.0071 -0.0248 153 TYR A O   
858  C CB  . TYR A 123 ? 0.1810 0.1984 0.1805 -0.0050 -0.0107 -0.0210 153 TYR A CB  
859  C CG  . TYR A 123 ? 0.1925 0.2162 0.1917 -0.0039 -0.0120 -0.0191 153 TYR A CG  
860  C CD1 . TYR A 123 ? 0.2060 0.2312 0.2013 -0.0038 -0.0125 -0.0205 153 TYR A CD1 
861  C CD2 . TYR A 123 ? 0.2022 0.2299 0.2049 -0.0027 -0.0124 -0.0158 153 TYR A CD2 
862  C CE1 . TYR A 123 ? 0.2367 0.2672 0.2316 -0.0026 -0.0135 -0.0182 153 TYR A CE1 
863  C CE2 . TYR A 123 ? 0.2030 0.2357 0.2057 -0.0014 -0.0133 -0.0138 153 TYR A CE2 
864  C CZ  . TYR A 123 ? 0.2325 0.2665 0.2313 -0.0014 -0.0140 -0.0148 153 TYR A CZ  
865  O OH  . TYR A 123 ? 0.2474 0.2858 0.2460 -0.0001 -0.0147 -0.0122 153 TYR A OH  
866  N N   . ASP A 124 ? 0.2350 0.2383 0.2309 -0.0114 -0.0091 -0.0289 154 ASP A N   
867  C CA  . ASP A 124 ? 0.2118 0.2065 0.2077 -0.0117 -0.0069 -0.0301 154 ASP A CA  
868  C C   . ASP A 124 ? 0.2358 0.2247 0.2282 -0.0088 -0.0047 -0.0322 154 ASP A C   
869  O O   . ASP A 124 ? 0.2782 0.2671 0.2664 -0.0093 -0.0048 -0.0351 154 ASP A O   
870  C CB  . ASP A 124 ? 0.2119 0.2045 0.2079 -0.0169 -0.0077 -0.0329 154 ASP A CB  
871  C CG  . ASP A 124 ? 0.2832 0.2663 0.2796 -0.0176 -0.0052 -0.0337 154 ASP A CG  
872  O OD1 . ASP A 124 ? 0.3401 0.3158 0.3329 -0.0165 -0.0033 -0.0365 154 ASP A OD1 
873  O OD2 . ASP A 124 ? 0.3407 0.3236 0.3412 -0.0190 -0.0048 -0.0313 154 ASP A OD2 
874  N N   . GLY A 125 ? 0.2284 0.2125 0.2222 -0.0057 -0.0026 -0.0304 155 GLY A N   
875  C CA  . GLY A 125 ? 0.2277 0.2079 0.2198 -0.0021 -0.0005 -0.0314 155 GLY A CA  
876  C C   . GLY A 125 ? 0.2453 0.2162 0.2349 -0.0024 0.0019  -0.0346 155 GLY A C   
877  O O   . GLY A 125 ? 0.2775 0.2448 0.2666 0.0013  0.0041  -0.0349 155 GLY A O   
878  N N   . GLU A 126 ? 0.2570 0.2240 0.2454 -0.0067 0.0016  -0.0371 156 GLU A N   
879  C CA  . GLU A 126 ? 0.2840 0.2405 0.2702 -0.0073 0.0042  -0.0402 156 GLU A CA  
880  C C   . GLU A 126 ? 0.3042 0.2577 0.2853 -0.0060 0.0059  -0.0443 156 GLU A C   
881  O O   . GLU A 126 ? 0.2988 0.2453 0.2791 -0.0026 0.0091  -0.0452 156 GLU A O   
882  C CB  . GLU A 126 ? 0.3023 0.2556 0.2884 -0.0131 0.0033  -0.0423 156 GLU A CB  
883  C CG  . GLU A 126 ? 0.4015 0.3444 0.3887 -0.0133 0.0060  -0.0421 156 GLU A CG  
884  C CD  . GLU A 126 ? 0.4505 0.3918 0.4393 -0.0195 0.0049  -0.0431 156 GLU A CD  
885  O OE1 . GLU A 126 ? 0.4337 0.3714 0.4192 -0.0239 0.0044  -0.0480 156 GLU A OE1 
886  O OE2 . GLU A 126 ? 0.3954 0.3394 0.3887 -0.0202 0.0045  -0.0391 156 GLU A OE2 
887  N N   . ALA A 127 ? 0.2769 0.2356 0.2543 -0.0085 0.0039  -0.0469 157 ALA A N   
888  C CA  . ALA A 127 ? 0.2694 0.2249 0.2407 -0.0078 0.0058  -0.0512 157 ALA A CA  
889  C C   . ALA A 127 ? 0.2742 0.2315 0.2466 -0.0019 0.0083  -0.0493 157 ALA A C   
890  O O   . ALA A 127 ? 0.2618 0.2133 0.2310 0.0005  0.0117  -0.0520 157 ALA A O   
891  C CB  . ALA A 127 ? 0.2512 0.2129 0.2180 -0.0117 0.0028  -0.0535 157 ALA A CB  
892  N N   . LEU A 128 ? 0.2858 0.2510 0.2628 0.0003  0.0068  -0.0447 158 LEU A N   
893  C CA  . LEU A 128 ? 0.3010 0.2686 0.2803 0.0055  0.0088  -0.0425 158 LEU A CA  
894  C C   . LEU A 128 ? 0.2745 0.2355 0.2573 0.0090  0.0114  -0.0411 158 LEU A C   
895  O O   . LEU A 128 ? 0.2854 0.2435 0.2681 0.0128  0.0145  -0.0420 158 LEU A O   
896  C CB  . LEU A 128 ? 0.2592 0.2362 0.2425 0.0063  0.0063  -0.0382 158 LEU A CB  
897  C CG  . LEU A 128 ? 0.2857 0.2696 0.2660 0.0051  0.0050  -0.0386 158 LEU A CG  
898  C CD1 . LEU A 128 ? 0.2630 0.2546 0.2472 0.0053  0.0024  -0.0344 158 LEU A CD1 
899  C CD2 . LEU A 128 ? 0.2206 0.2044 0.1987 0.0080  0.0081  -0.0400 158 LEU A CD2 
900  N N   . ALA A 129 ? 0.3028 0.2614 0.2886 0.0081  0.0102  -0.0388 159 ALA A N   
901  C CA  . ALA A 129 ? 0.2540 0.2069 0.2430 0.0118  0.0123  -0.0365 159 ALA A CA  
902  C C   . ALA A 129 ? 0.2806 0.2230 0.2667 0.0128  0.0160  -0.0401 159 ALA A C   
903  O O   . ALA A 129 ? 0.2770 0.2157 0.2654 0.0176  0.0187  -0.0389 159 ALA A O   
904  C CB  . ALA A 129 ? 0.2321 0.1840 0.2236 0.0102  0.0105  -0.0334 159 ALA A CB  
905  N N   . ARG A 130 ? 0.2547 0.1922 0.2360 0.0083  0.0161  -0.0447 160 ARG A N   
906  C CA  . ARG A 130 ? 0.3083 0.2346 0.2857 0.0087  0.0198  -0.0489 160 ARG A CA  
907  C C   . ARG A 130 ? 0.3019 0.2280 0.2775 0.0131  0.0232  -0.0508 160 ARG A C   
908  O O   . ARG A 130 ? 0.3116 0.2283 0.2857 0.0158  0.0273  -0.0530 160 ARG A O   
909  C CB  . ARG A 130 ? 0.3433 0.2654 0.3151 0.0022  0.0187  -0.0540 160 ARG A CB  
910  C CG  . ARG A 130 ? 0.4882 0.4015 0.4609 -0.0011 0.0190  -0.0543 160 ARG A CG  
911  C CD  . ARG A 130 ? 0.5211 0.4300 0.4884 -0.0078 0.0179  -0.0600 160 ARG A CD  
912  N NE  . ARG A 130 ? 0.3623 0.2808 0.3308 -0.0129 0.0132  -0.0591 160 ARG A NE  
913  C CZ  . ARG A 130 ? 0.4539 0.3728 0.4262 -0.0169 0.0114  -0.0573 160 ARG A CZ  
914  N NH1 . ARG A 130 ? 0.4711 0.3807 0.4458 -0.0169 0.0137  -0.0561 160 ARG A NH1 
915  N NH2 . ARG A 130 ? 0.5855 0.5143 0.5595 -0.0208 0.0073  -0.0563 160 ARG A NH2 
916  N N   . GLN A 131 ? 0.2947 0.2306 0.2705 0.0141  0.0220  -0.0499 161 GLN A N   
917  C CA  . GLN A 131 ? 0.2691 0.2060 0.2441 0.0184  0.0255  -0.0509 161 GLN A CA  
918  C C   . GLN A 131 ? 0.2857 0.2256 0.2683 0.0245  0.0269  -0.0462 161 GLN A C   
919  O O   . GLN A 131 ? 0.2802 0.2227 0.2641 0.0285  0.0299  -0.0462 161 GLN A O   
920  C CB  . GLN A 131 ? 0.2615 0.2076 0.2335 0.0167  0.0239  -0.0517 161 GLN A CB  
921  C CG  . GLN A 131 ? 0.2809 0.2260 0.2457 0.0107  0.0214  -0.0557 161 GLN A CG  
922  C CD  . GLN A 131 ? 0.3125 0.2664 0.2738 0.0093  0.0198  -0.0558 161 GLN A CD  
923  O OE1 . GLN A 131 ? 0.3115 0.2664 0.2698 0.0117  0.0228  -0.0573 161 GLN A OE1 
924  N NE2 . GLN A 131 ? 0.3005 0.2609 0.2624 0.0056  0.0152  -0.0541 161 GLN A NE2 
925  N N   . GLY A 132 ? 0.2963 0.2361 0.2838 0.0252  0.0250  -0.0421 162 GLY A N   
926  C CA  . GLY A 132 ? 0.2536 0.1956 0.2479 0.0308  0.0259  -0.0376 162 GLY A CA  
927  C C   . GLY A 132 ? 0.2409 0.1943 0.2402 0.0314  0.0223  -0.0331 162 GLY A C   
928  O O   . GLY A 132 ? 0.2629 0.2222 0.2669 0.0353  0.0231  -0.0309 162 GLY A O   
929  N N   . VAL A 133 ? 0.2342 0.1910 0.2327 0.0274  0.0184  -0.0319 163 VAL A N   
930  C CA  . VAL A 133 ? 0.2384 0.2046 0.2408 0.0276  0.0151  -0.0279 163 VAL A CA  
931  C C   . VAL A 133 ? 0.2752 0.2400 0.2777 0.0253  0.0122  -0.0255 163 VAL A C   
932  O O   . VAL A 133 ? 0.2326 0.1910 0.2322 0.0225  0.0125  -0.0271 163 VAL A O   
933  C CB  . VAL A 133 ? 0.2335 0.2075 0.2343 0.0250  0.0136  -0.0290 163 VAL A CB  
934  C CG1 . VAL A 133 ? 0.2791 0.2540 0.2786 0.0268  0.0169  -0.0316 163 VAL A CG1 
935  C CG2 . VAL A 133 ? 0.2659 0.2388 0.2620 0.0199  0.0116  -0.0311 163 VAL A CG2 
936  N N   . VAL A 134 ? 0.2132 0.1842 0.2191 0.0265  0.0097  -0.0216 164 VAL A N   
937  C CA  . VAL A 134 ? 0.2095 0.1810 0.2149 0.0244  0.0070  -0.0193 164 VAL A CA  
938  C C   . VAL A 134 ? 0.2021 0.1805 0.2065 0.0211  0.0047  -0.0198 164 VAL A C   
939  O O   . VAL A 134 ? 0.2280 0.2130 0.2344 0.0222  0.0036  -0.0188 164 VAL A O   
940  C CB  . VAL A 134 ? 0.2089 0.1822 0.2176 0.0277  0.0055  -0.0149 164 VAL A CB  
941  C CG1 . VAL A 134 ? 0.2045 0.1783 0.2116 0.0254  0.0032  -0.0127 164 VAL A CG1 
942  C CG2 . VAL A 134 ? 0.2260 0.1924 0.2360 0.0315  0.0078  -0.0137 164 VAL A CG2 
943  N N   . VAL A 135 ? 0.2066 0.1836 0.2083 0.0172  0.0040  -0.0211 165 VAL A N   
944  C CA  . VAL A 135 ? 0.2030 0.1862 0.2038 0.0144  0.0020  -0.0215 165 VAL A CA  
945  C C   . VAL A 135 ? 0.2046 0.1899 0.2063 0.0137  0.0000  -0.0185 165 VAL A C   
946  O O   . VAL A 135 ? 0.1968 0.1779 0.1982 0.0128  0.0003  -0.0175 165 VAL A O   
947  C CB  . VAL A 135 ? 0.1999 0.1815 0.1975 0.0106  0.0022  -0.0248 165 VAL A CB  
948  C CG1 . VAL A 135 ? 0.1943 0.1829 0.1912 0.0085  0.0002  -0.0247 165 VAL A CG1 
949  C CG2 . VAL A 135 ? 0.2071 0.1843 0.2023 0.0113  0.0046  -0.0283 165 VAL A CG2 
950  N N   . VAL A 136 ? 0.2268 0.2181 0.2294 0.0139  -0.0017 -0.0170 166 VAL A N   
951  C CA  . VAL A 136 ? 0.2146 0.2077 0.2174 0.0134  -0.0032 -0.0146 166 VAL A CA  
952  C C   . VAL A 136 ? 0.2317 0.2296 0.2340 0.0111  -0.0043 -0.0150 166 VAL A C   
953  O O   . VAL A 136 ? 0.1982 0.2000 0.2008 0.0113  -0.0046 -0.0157 166 VAL A O   
954  C CB  . VAL A 136 ? 0.2108 0.2059 0.2150 0.0161  -0.0044 -0.0122 166 VAL A CB  
955  C CG1 . VAL A 136 ? 0.1773 0.1737 0.1803 0.0153  -0.0057 -0.0103 166 VAL A CG1 
956  C CG2 . VAL A 136 ? 0.1845 0.1754 0.1895 0.0187  -0.0036 -0.0111 166 VAL A CG2 
957  N N   . THR A 137 ? 0.2198 0.2177 0.2218 0.0092  -0.0046 -0.0143 167 THR A N   
958  C CA  . THR A 137 ? 0.2063 0.2090 0.2086 0.0078  -0.0056 -0.0138 167 THR A CA  
959  C C   . THR A 137 ? 0.1892 0.1920 0.1916 0.0084  -0.0058 -0.0114 167 THR A C   
960  O O   . THR A 137 ? 0.2228 0.2219 0.2246 0.0091  -0.0051 -0.0103 167 THR A O   
961  C CB  . THR A 137 ? 0.2026 0.2066 0.2050 0.0048  -0.0057 -0.0153 167 THR A CB  
962  O OG1 . THR A 137 ? 0.2130 0.2140 0.2161 0.0033  -0.0050 -0.0148 167 THR A OG1 
963  C CG2 . THR A 137 ? 0.1787 0.1812 0.1794 0.0041  -0.0053 -0.0183 167 THR A CG2 
964  N N   . PHE A 138 ? 0.1767 0.1832 0.1793 0.0084  -0.0064 -0.0105 168 PHE A N   
965  C CA  . PHE A 138 ? 0.1692 0.1750 0.1711 0.0093  -0.0062 -0.0086 168 PHE A CA  
966  C C   . PHE A 138 ? 0.1653 0.1748 0.1679 0.0091  -0.0063 -0.0079 168 PHE A C   
967  O O   . PHE A 138 ? 0.1736 0.1862 0.1770 0.0087  -0.0069 -0.0084 168 PHE A O   
968  C CB  . PHE A 138 ? 0.2041 0.2083 0.2046 0.0113  -0.0069 -0.0081 168 PHE A CB  
969  C CG  . PHE A 138 ? 0.1976 0.2047 0.1987 0.0117  -0.0079 -0.0086 168 PHE A CG  
970  C CD1 . PHE A 138 ? 0.1650 0.1734 0.1674 0.0119  -0.0081 -0.0097 168 PHE A CD1 
971  C CD2 . PHE A 138 ? 0.1645 0.1724 0.1647 0.0120  -0.0082 -0.0078 168 PHE A CD2 
972  C CE1 . PHE A 138 ? 0.1630 0.1741 0.1664 0.0120  -0.0086 -0.0098 168 PHE A CE1 
973  C CE2 . PHE A 138 ? 0.1629 0.1727 0.1638 0.0120  -0.0089 -0.0081 168 PHE A CE2 
974  C CZ  . PHE A 138 ? 0.1619 0.1737 0.1647 0.0119  -0.0091 -0.0090 168 PHE A CZ  
975  N N   . ASN A 139 ? 0.1896 0.1985 0.1917 0.0095  -0.0053 -0.0064 169 ASN A N   
976  C CA  . ASN A 139 ? 0.1777 0.1891 0.1805 0.0100  -0.0049 -0.0054 169 ASN A CA  
977  C C   . ASN A 139 ? 0.1746 0.1839 0.1748 0.0116  -0.0051 -0.0052 169 ASN A C   
978  O O   . ASN A 139 ? 0.1882 0.1942 0.1857 0.0122  -0.0054 -0.0053 169 ASN A O   
979  C CB  . ASN A 139 ? 0.1848 0.1968 0.1888 0.0097  -0.0031 -0.0039 169 ASN A CB  
980  C CG  . ASN A 139 ? 0.2217 0.2356 0.2287 0.0075  -0.0030 -0.0041 169 ASN A CG  
981  O OD1 . ASN A 139 ? 0.1678 0.1833 0.1759 0.0061  -0.0044 -0.0055 169 ASN A OD1 
982  N ND2 . ASN A 139 ? 0.2289 0.2424 0.2371 0.0070  -0.0012 -0.0028 169 ASN A ND2 
983  N N   . TYR A 140 ? 0.1637 0.1748 0.1645 0.0120  -0.0051 -0.0049 170 TYR A N   
984  C CA  . TYR A 140 ? 0.1759 0.1844 0.1743 0.0130  -0.0051 -0.0049 170 TYR A CA  
985  C C   . TYR A 140 ? 0.2052 0.2143 0.2043 0.0141  -0.0034 -0.0037 170 TYR A C   
986  O O   . TYR A 140 ? 0.1642 0.1771 0.1665 0.0140  -0.0030 -0.0026 170 TYR A O   
987  C CB  . TYR A 140 ? 0.1638 0.1730 0.1627 0.0126  -0.0065 -0.0058 170 TYR A CB  
988  C CG  . TYR A 140 ? 0.2189 0.2318 0.2203 0.0122  -0.0067 -0.0053 170 TYR A CG  
989  C CD1 . TYR A 140 ? 0.2022 0.2177 0.2050 0.0113  -0.0072 -0.0060 170 TYR A CD1 
990  C CD2 . TYR A 140 ? 0.2167 0.2300 0.2186 0.0127  -0.0061 -0.0043 170 TYR A CD2 
991  C CE1 . TYR A 140 ? 0.1811 0.2000 0.1850 0.0108  -0.0075 -0.0056 170 TYR A CE1 
992  C CE2 . TYR A 140 ? 0.1915 0.2082 0.1950 0.0125  -0.0063 -0.0034 170 TYR A CE2 
993  C CZ  . TYR A 140 ? 0.2051 0.2249 0.2093 0.0115  -0.0071 -0.0041 170 TYR A CZ  
994  O OH  . TYR A 140 ? 0.2187 0.2420 0.2234 0.0112  -0.0075 -0.0033 170 TYR A OH  
995  N N   . ARG A 141 ? 0.1737 0.1788 0.1697 0.0151  -0.0026 -0.0040 171 ARG A N   
996  C CA  . ARG A 141 ? 0.1931 0.1976 0.1894 0.0166  -0.0005 -0.0029 171 ARG A CA  
997  C C   . ARG A 141 ? 0.2362 0.2428 0.2351 0.0168  -0.0009 -0.0021 171 ARG A C   
998  O O   . ARG A 141 ? 0.2035 0.2099 0.2022 0.0157  -0.0025 -0.0028 171 ARG A O   
999  C CB  . ARG A 141 ? 0.1768 0.1753 0.1680 0.0175  0.0007  -0.0039 171 ARG A CB  
1000 C CG  . ARG A 141 ? 0.1801 0.1763 0.1678 0.0180  0.0020  -0.0040 171 ARG A CG  
1001 C CD  . ARG A 141 ? 0.1868 0.1767 0.1680 0.0185  0.0026  -0.0055 171 ARG A CD  
1002 N NE  . ARG A 141 ? 0.1876 0.1758 0.1660 0.0169  -0.0005 -0.0072 171 ARG A NE  
1003 C CZ  . ARG A 141 ? 0.2269 0.2101 0.1994 0.0166  -0.0013 -0.0089 171 ARG A CZ  
1004 N NH1 . ARG A 141 ? 0.2002 0.1785 0.1682 0.0178  0.0013  -0.0097 171 ARG A NH1 
1005 N NH2 . ARG A 141 ? 0.2288 0.2121 0.2001 0.0150  -0.0046 -0.0101 171 ARG A NH2 
1006 N N   . THR A 142 ? 0.1988 0.2081 0.2006 0.0182  0.0006  -0.0001 172 THR A N   
1007 C CA  . THR A 142 ? 0.2250 0.2366 0.2291 0.0187  0.0002  0.0014  172 THR A CA  
1008 C C   . THR A 142 ? 0.2163 0.2273 0.2219 0.0215  0.0027  0.0034  172 THR A C   
1009 O O   . THR A 142 ? 0.2244 0.2331 0.2290 0.0228  0.0050  0.0033  172 THR A O   
1010 C CB  . THR A 142 ? 0.2709 0.2892 0.2783 0.0175  -0.0017 0.0021  172 THR A CB  
1011 O OG1 . THR A 142 ? 0.2798 0.2998 0.2879 0.0177  -0.0024 0.0033  172 THR A OG1 
1012 C CG2 . THR A 142 ? 0.1736 0.1968 0.1848 0.0182  -0.0009 0.0038  172 THR A CG2 
1013 N N   . ASN A 143 ? 0.2258 0.2385 0.2335 0.0225  0.0027  0.0054  173 ASN A N   
1014 C CA  . ASN A 143 ? 0.1912 0.2033 0.2009 0.0257  0.0052  0.0079  173 ASN A CA  
1015 C C   . ASN A 143 ? 0.2266 0.2298 0.2319 0.0267  0.0077  0.0063  173 ASN A C   
1016 O O   . ASN A 143 ? 0.2300 0.2282 0.2312 0.0247  0.0067  0.0037  173 ASN A O   
1017 C CB  . ASN A 143 ? 0.1735 0.1922 0.1879 0.0269  0.0058  0.0099  173 ASN A CB  
1018 C CG  . ASN A 143 ? 0.2362 0.2578 0.2548 0.0303  0.0073  0.0136  173 ASN A CG  
1019 O OD1 . ASN A 143 ? 0.2748 0.2908 0.2922 0.0330  0.0102  0.0142  173 ASN A OD1 
1020 N ND2 . ASN A 143 ? 0.1929 0.2232 0.2162 0.0302  0.0052  0.0160  173 ASN A ND2 
1021 N N   . ILE A 144 ? 0.1875 0.1887 0.1936 0.0298  0.0110  0.0075  174 ILE A N   
1022 C CA  . ILE A 144 ? 0.2064 0.1983 0.2075 0.0309  0.0137  0.0056  174 ILE A CA  
1023 C C   . ILE A 144 ? 0.1941 0.1823 0.1899 0.0290  0.0133  0.0023  174 ILE A C   
1024 O O   . ILE A 144 ? 0.2382 0.2185 0.2282 0.0283  0.0139  -0.0003 174 ILE A O   
1025 C CB  . ILE A 144 ? 0.2380 0.2286 0.2412 0.0352  0.0179  0.0078  174 ILE A CB  
1026 C CG1 . ILE A 144 ? 0.2286 0.2079 0.2259 0.0364  0.0209  0.0056  174 ILE A CG1 
1027 C CG2 . ILE A 144 ? 0.1961 0.1916 0.2017 0.0363  0.0195  0.0085  174 ILE A CG2 
1028 C CD1 . ILE A 144 ? 0.2286 0.2052 0.2274 0.0411  0.0257  0.0074  174 ILE A CD1 
1029 N N   . LEU A 145 ? 0.1895 0.1829 0.1866 0.0279  0.0122  0.0023  175 LEU A N   
1030 C CA  . LEU A 145 ? 0.2320 0.2220 0.2237 0.0264  0.0119  -0.0003 175 LEU A CA  
1031 C C   . LEU A 145 ? 0.2290 0.2180 0.2183 0.0232  0.0081  -0.0024 175 LEU A C   
1032 O O   . LEU A 145 ? 0.2041 0.1889 0.1880 0.0221  0.0074  -0.0046 175 LEU A O   
1033 C CB  . LEU A 145 ? 0.2467 0.2420 0.2409 0.0264  0.0125  0.0009  175 LEU A CB  
1034 C CG  . LEU A 145 ? 0.2751 0.2718 0.2721 0.0296  0.0167  0.0029  175 LEU A CG  
1035 C CD1 . LEU A 145 ? 0.2383 0.2419 0.2399 0.0290  0.0171  0.0046  175 LEU A CD1 
1036 C CD2 . LEU A 145 ? 0.2277 0.2160 0.2177 0.0313  0.0201  0.0011  175 LEU A CD2 
1037 N N   . GLY A 146 ? 0.2000 0.1930 0.1929 0.0220  0.0058  -0.0016 176 GLY A N   
1038 C CA  . GLY A 146 ? 0.1943 0.1870 0.1860 0.0193  0.0028  -0.0033 176 GLY A CA  
1039 C C   . GLY A 146 ? 0.2025 0.1914 0.1933 0.0185  0.0024  -0.0038 176 GLY A C   
1040 O O   . GLY A 146 ? 0.2178 0.2056 0.2073 0.0163  0.0002  -0.0055 176 GLY A O   
1041 N N   . PHE A 147 ? 0.2075 0.1948 0.1998 0.0203  0.0045  -0.0022 177 PHE A N   
1042 C CA  . PHE A 147 ? 0.2512 0.2347 0.2433 0.0195  0.0045  -0.0021 177 PHE A CA  
1043 C C   . PHE A 147 ? 0.2958 0.2726 0.2862 0.0219  0.0079  -0.0016 177 PHE A C   
1044 O O   . PHE A 147 ? 0.2453 0.2242 0.2390 0.0246  0.0098  0.0013  177 PHE A O   
1045 C CB  . PHE A 147 ? 0.2067 0.1960 0.2032 0.0191  0.0034  0.0003  177 PHE A CB  
1046 C CG  . PHE A 147 ? 0.2356 0.2305 0.2334 0.0170  0.0007  -0.0005 177 PHE A CG  
1047 C CD1 . PHE A 147 ? 0.2397 0.2337 0.2369 0.0145  -0.0010 -0.0021 177 PHE A CD1 
1048 C CD2 . PHE A 147 ? 0.2436 0.2444 0.2434 0.0176  0.0000  0.0003  177 PHE A CD2 
1049 C CE1 . PHE A 147 ? 0.2132 0.2120 0.2118 0.0131  -0.0030 -0.0028 177 PHE A CE1 
1050 C CE2 . PHE A 147 ? 0.2547 0.2594 0.2552 0.0158  -0.0021 -0.0007 177 PHE A CE2 
1051 C CZ  . PHE A 147 ? 0.2145 0.2181 0.2144 0.0139  -0.0034 -0.0022 177 PHE A CZ  
1052 N N   . PHE A 148 ? 0.2119 0.1809 0.1972 0.0210  0.0086  -0.0045 178 PHE A N   
1053 C CA  . PHE A 148 ? 0.2517 0.2127 0.2340 0.0233  0.0122  -0.0049 178 PHE A CA  
1054 C C   . PHE A 148 ? 0.2451 0.1974 0.2213 0.0206  0.0117  -0.0088 178 PHE A C   
1055 O O   . PHE A 148 ? 0.2476 0.2003 0.2203 0.0182  0.0092  -0.0114 178 PHE A O   
1056 C CB  . PHE A 148 ? 0.2232 0.1851 0.2045 0.0264  0.0149  -0.0045 178 PHE A CB  
1057 C CG  . PHE A 148 ? 0.2611 0.2147 0.2392 0.0294  0.0193  -0.0050 178 PHE A CG  
1058 C CD1 . PHE A 148 ? 0.2270 0.1795 0.2090 0.0327  0.0222  -0.0020 178 PHE A CD1 
1059 C CD2 . PHE A 148 ? 0.2487 0.1951 0.2192 0.0293  0.0209  -0.0085 178 PHE A CD2 
1060 C CE1 . PHE A 148 ? 0.2823 0.2265 0.2614 0.0359  0.0268  -0.0025 178 PHE A CE1 
1061 C CE2 . PHE A 148 ? 0.2841 0.2220 0.2509 0.0322  0.0255  -0.0094 178 PHE A CE2 
1062 C CZ  . PHE A 148 ? 0.2672 0.2038 0.2387 0.0357  0.0286  -0.0064 178 PHE A CZ  
1063 N N   . ALA A 149 ? 0.2360 0.1805 0.2110 0.0208  0.0138  -0.0091 179 ALA A N   
1064 C CA  . ALA A 149 ? 0.2786 0.2138 0.2477 0.0178  0.0134  -0.0130 179 ALA A CA  
1065 C C   . ALA A 149 ? 0.2780 0.2029 0.2420 0.0205  0.0178  -0.0145 179 ALA A C   
1066 O O   . ALA A 149 ? 0.3158 0.2400 0.2826 0.0247  0.0215  -0.0116 179 ALA A O   
1067 C CB  . ALA A 149 ? 0.2554 0.1891 0.2275 0.0145  0.0119  -0.0127 179 ALA A CB  
1068 N N   . HIS A 150 ? 0.3243 0.2413 0.2804 0.0183  0.0175  -0.0191 180 HIS A N   
1069 C CA  . HIS A 150 ? 0.3491 0.2552 0.2985 0.0207  0.0219  -0.0214 180 HIS A CA  
1070 C C   . HIS A 150 ? 0.3121 0.2089 0.2533 0.0162  0.0202  -0.0269 180 HIS A C   
1071 O O   . HIS A 150 ? 0.3207 0.2216 0.2600 0.0124  0.0154  -0.0288 180 HIS A O   
1072 C CB  . HIS A 150 ? 0.2722 0.1810 0.2190 0.0245  0.0244  -0.0211 180 HIS A CB  
1073 C CG  . HIS A 150 ? 0.3298 0.2290 0.2718 0.0285  0.0303  -0.0221 180 HIS A CG  
1074 N ND1 . HIS A 150 ? 0.3555 0.2434 0.2871 0.0273  0.0318  -0.0272 180 HIS A ND1 
1075 C CD2 . HIS A 150 ? 0.2840 0.1835 0.2303 0.0339  0.0353  -0.0188 180 HIS A CD2 
1076 C CE1 . HIS A 150 ? 0.3565 0.2374 0.2858 0.0320  0.0379  -0.0271 180 HIS A CE1 
1077 N NE2 . HIS A 150 ? 0.3148 0.2028 0.2534 0.0362  0.0401  -0.0219 180 HIS A NE2 
1078 N N   . PRO A 151 ? 0.3172 0.2014 0.2535 0.0165  0.0236  -0.0294 181 PRO A N   
1079 C CA  . PRO A 151 ? 0.3903 0.2651 0.3180 0.0115  0.0215  -0.0351 181 PRO A CA  
1080 C C   . PRO A 151 ? 0.3713 0.2463 0.2901 0.0107  0.0196  -0.0387 181 PRO A C   
1081 O O   . PRO A 151 ? 0.3707 0.2453 0.2853 0.0056  0.0148  -0.0422 181 PRO A O   
1082 C CB  . PRO A 151 ? 0.3904 0.2507 0.3140 0.0133  0.0269  -0.0369 181 PRO A CB  
1083 C CG  . PRO A 151 ? 0.3705 0.2333 0.2992 0.0203  0.0322  -0.0322 181 PRO A CG  
1084 C CD  . PRO A 151 ? 0.3793 0.2571 0.3180 0.0209  0.0292  -0.0270 181 PRO A CD  
1085 N N   . GLY A 152 ? 0.3206 0.1968 0.2366 0.0154  0.0232  -0.0377 182 GLY A N   
1086 C CA  . GLY A 152 ? 0.3586 0.2353 0.2659 0.0148  0.0217  -0.0405 182 GLY A CA  
1087 C C   . GLY A 152 ? 0.3487 0.2378 0.2601 0.0125  0.0159  -0.0386 182 GLY A C   
1088 O O   . GLY A 152 ? 0.3074 0.1968 0.2119 0.0097  0.0122  -0.0413 182 GLY A O   
1089 N N   . LEU A 153 ? 0.2892 0.1885 0.2115 0.0138  0.0151  -0.0338 183 LEU A N   
1090 C CA  . LEU A 153 ? 0.2841 0.1945 0.2109 0.0118  0.0101  -0.0320 183 LEU A CA  
1091 C C   . LEU A 153 ? 0.3208 0.2316 0.2480 0.0063  0.0046  -0.0343 183 LEU A C   
1092 O O   . LEU A 153 ? 0.3077 0.2233 0.2329 0.0039  0.0001  -0.0352 183 LEU A O   
1093 C CB  . LEU A 153 ? 0.2825 0.2024 0.2201 0.0142  0.0108  -0.0270 183 LEU A CB  
1094 C CG  . LEU A 153 ? 0.3243 0.2474 0.2632 0.0191  0.0149  -0.0242 183 LEU A CG  
1095 C CD1 . LEU A 153 ? 0.3073 0.2393 0.2568 0.0208  0.0152  -0.0196 183 LEU A CD1 
1096 C CD2 . LEU A 153 ? 0.2600 0.1865 0.1942 0.0191  0.0135  -0.0247 183 LEU A CD2 
1097 N N   . SER A 154 ? 0.2839 0.1897 0.2139 0.0042  0.0051  -0.0350 184 SER A N   
1098 C CA  . SER A 154 ? 0.3314 0.2372 0.2621 -0.0015 0.0003  -0.0374 184 SER A CA  
1099 C C   . SER A 154 ? 0.3510 0.2496 0.2707 -0.0046 -0.0020 -0.0427 184 SER A C   
1100 O O   . SER A 154 ? 0.3159 0.2187 0.2351 -0.0088 -0.0075 -0.0443 184 SER A O   
1101 C CB  . SER A 154 ? 0.2880 0.1890 0.2237 -0.0032 0.0020  -0.0368 184 SER A CB  
1102 O OG  . SER A 154 ? 0.3405 0.2494 0.2860 -0.0009 0.0031  -0.0318 184 SER A OG  
1103 N N   . ARG A 155 ? 0.3101 0.1981 0.2207 -0.0025 0.0022  -0.0454 185 ARG A N   
1104 C CA  . ARG A 155 ? 0.3888 0.2689 0.2872 -0.0054 0.0003  -0.0509 185 ARG A CA  
1105 C C   . ARG A 155 ? 0.3632 0.2506 0.2571 -0.0053 -0.0035 -0.0507 185 ARG A C   
1106 O O   . ARG A 155 ? 0.3520 0.2397 0.2407 -0.0096 -0.0089 -0.0538 185 ARG A O   
1107 C CB  . ARG A 155 ? 0.4600 0.3269 0.3493 -0.0023 0.0066  -0.0536 185 ARG A CB  
1108 C CG  . ARG A 155 ? 0.5947 0.4508 0.4701 -0.0058 0.0052  -0.0602 185 ARG A CG  
1109 C CD  . ARG A 155 ? 0.5996 0.4413 0.4665 -0.0025 0.0123  -0.0631 185 ARG A CD  
1110 N NE  . ARG A 155 ? 0.7404 0.5793 0.6161 0.0007  0.0174  -0.0599 185 ARG A NE  
1111 C CZ  . ARG A 155 ? 0.7882 0.6272 0.6667 0.0073  0.0237  -0.0565 185 ARG A CZ  
1112 N NH1 . ARG A 155 ? 0.6554 0.4962 0.5284 0.0113  0.0264  -0.0561 185 ARG A NH1 
1113 N NH2 . ARG A 155 ? 0.6372 0.4746 0.5243 0.0099  0.0275  -0.0532 185 ARG A NH2 
1114 N N   . GLU A 156 ? 0.3651 0.2585 0.2611 -0.0005 -0.0011 -0.0469 186 GLU A N   
1115 C CA  . GLU A 156 ? 0.3966 0.2958 0.2878 -0.0001 -0.0040 -0.0464 186 GLU A CA  
1116 C C   . GLU A 156 ? 0.4005 0.3114 0.2998 -0.0025 -0.0101 -0.0438 186 GLU A C   
1117 O O   . GLU A 156 ? 0.4471 0.3625 0.3424 -0.0026 -0.0134 -0.0434 186 GLU A O   
1118 C CB  . GLU A 156 ? 0.3931 0.2944 0.2842 0.0055  0.0011  -0.0431 186 GLU A CB  
1119 C CG  . GLU A 156 ? 0.3366 0.2468 0.2408 0.0080  0.0025  -0.0380 186 GLU A CG  
1120 C CD  . GLU A 156 ? 0.3268 0.2397 0.2315 0.0129  0.0072  -0.0349 186 GLU A CD  
1121 O OE1 . GLU A 156 ? 0.3419 0.2479 0.2378 0.0151  0.0113  -0.0366 186 GLU A OE1 
1122 O OE2 . GLU A 156 ? 0.3606 0.2825 0.2744 0.0143  0.0069  -0.0309 186 GLU A OE2 
1123 N N   . SER A 157 ? 0.3145 0.2300 0.2245 -0.0041 -0.0113 -0.0421 187 SER A N   
1124 C CA  . SER A 157 ? 0.3627 0.2899 0.2821 -0.0052 -0.0155 -0.0390 187 SER A CA  
1125 C C   . SER A 157 ? 0.3829 0.3128 0.3007 -0.0100 -0.0221 -0.0413 187 SER A C   
1126 O O   . SER A 157 ? 0.3443 0.2680 0.2585 -0.0140 -0.0236 -0.0451 187 SER A O   
1127 C CB  . SER A 157 ? 0.2946 0.2252 0.2253 -0.0052 -0.0139 -0.0363 187 SER A CB  
1128 O OG  . SER A 157 ? 0.3179 0.2588 0.2571 -0.0067 -0.0179 -0.0340 187 SER A OG  
1129 N N   . PRO A 158 ? 0.3731 0.3124 0.2941 -0.0098 -0.0261 -0.0390 188 PRO A N   
1130 C CA  . PRO A 158 ? 0.4029 0.3471 0.3249 -0.0142 -0.0328 -0.0404 188 PRO A CA  
1131 C C   . PRO A 158 ? 0.4286 0.3759 0.3606 -0.0180 -0.0343 -0.0404 188 PRO A C   
1132 O O   . PRO A 158 ? 0.4314 0.3796 0.3633 -0.0227 -0.0390 -0.0429 188 PRO A O   
1133 C CB  . PRO A 158 ? 0.3737 0.3276 0.2989 -0.0117 -0.0354 -0.0367 188 PRO A CB  
1134 C CG  . PRO A 158 ? 0.4020 0.3532 0.3231 -0.0068 -0.0304 -0.0347 188 PRO A CG  
1135 C CD  . PRO A 158 ? 0.3340 0.2795 0.2574 -0.0056 -0.0248 -0.0351 188 PRO A CD  
1136 N N   . THR A 159 ? 0.3918 0.3413 0.3326 -0.0161 -0.0305 -0.0376 189 THR A N   
1137 C CA  . THR A 159 ? 0.3394 0.2914 0.2895 -0.0194 -0.0310 -0.0371 189 THR A CA  
1138 C C   . THR A 159 ? 0.3790 0.3206 0.3271 -0.0205 -0.0269 -0.0390 189 THR A C   
1139 O O   . THR A 159 ? 0.3273 0.2696 0.2826 -0.0233 -0.0266 -0.0384 189 THR A O   
1140 C CB  . THR A 159 ? 0.4208 0.3820 0.3814 -0.0167 -0.0295 -0.0326 189 THR A CB  
1141 O OG1 . THR A 159 ? 0.3721 0.3300 0.3318 -0.0123 -0.0243 -0.0307 189 THR A OG1 
1142 C CG2 . THR A 159 ? 0.3890 0.3595 0.3519 -0.0153 -0.0332 -0.0306 189 THR A CG2 
1143 N N   . GLY A 160 ? 0.3734 0.3052 0.3120 -0.0184 -0.0235 -0.0411 190 GLY A N   
1144 C CA  . GLY A 160 ? 0.2997 0.2208 0.2363 -0.0186 -0.0190 -0.0426 190 GLY A CA  
1145 C C   . GLY A 160 ? 0.3442 0.2669 0.2887 -0.0153 -0.0144 -0.0385 190 GLY A C   
1146 O O   . GLY A 160 ? 0.3612 0.2763 0.3063 -0.0158 -0.0111 -0.0389 190 GLY A O   
1147 N N   . THR A 161 ? 0.2859 0.2180 0.2360 -0.0119 -0.0142 -0.0346 191 THR A N   
1148 C CA  . THR A 161 ? 0.3097 0.2449 0.2673 -0.0089 -0.0106 -0.0305 191 THR A CA  
1149 C C   . THR A 161 ? 0.2834 0.2198 0.2389 -0.0035 -0.0074 -0.0285 191 THR A C   
1150 O O   . THR A 161 ? 0.2798 0.2148 0.2287 -0.0022 -0.0078 -0.0299 191 THR A O   
1151 C CB  . THR A 161 ? 0.3121 0.2580 0.2791 -0.0104 -0.0132 -0.0278 191 THR A CB  
1152 O OG1 . THR A 161 ? 0.3273 0.2813 0.2948 -0.0089 -0.0159 -0.0268 191 THR A OG1 
1153 C CG2 . THR A 161 ? 0.2776 0.2236 0.2474 -0.0161 -0.0165 -0.0297 191 THR A CG2 
1154 N N   . SER A 162 ? 0.2974 0.2366 0.2587 -0.0006 -0.0044 -0.0249 192 SER A N   
1155 C CA  . SER A 162 ? 0.2511 0.1932 0.2124 0.0040  -0.0017 -0.0225 192 SER A CA  
1156 C C   . SER A 162 ? 0.2823 0.2318 0.2519 0.0056  -0.0010 -0.0185 192 SER A C   
1157 O O   . SER A 162 ? 0.2927 0.2441 0.2671 0.0035  -0.0018 -0.0174 192 SER A O   
1158 C CB  . SER A 162 ? 0.2598 0.1929 0.2156 0.0070  0.0029  -0.0234 192 SER A CB  
1159 O OG  . SER A 162 ? 0.3263 0.2529 0.2836 0.0068  0.0054  -0.0231 192 SER A OG  
1160 N N   . GLY A 163 ? 0.2451 0.1990 0.2161 0.0091  0.0007  -0.0162 193 GLY A N   
1161 C CA  . GLY A 163 ? 0.2241 0.1855 0.2018 0.0105  0.0009  -0.0127 193 GLY A CA  
1162 C C   . GLY A 163 ? 0.2489 0.2184 0.2297 0.0091  -0.0024 -0.0123 193 GLY A C   
1163 O O   . GLY A 163 ? 0.2307 0.2007 0.2093 0.0071  -0.0051 -0.0144 193 GLY A O   
1164 N N   . ASN A 164 ? 0.2556 0.2315 0.2415 0.0102  -0.0022 -0.0096 194 ASN A N   
1165 C CA  . ASN A 164 ? 0.2270 0.2102 0.2166 0.0091  -0.0046 -0.0091 194 ASN A CA  
1166 C C   . ASN A 164 ? 0.2076 0.1931 0.1952 0.0097  -0.0060 -0.0100 194 ASN A C   
1167 O O   . ASN A 164 ? 0.1844 0.1737 0.1736 0.0085  -0.0084 -0.0104 194 ASN A O   
1168 C CB  . ASN A 164 ? 0.1903 0.1741 0.1819 0.0059  -0.0066 -0.0101 194 ASN A CB  
1169 C CG  . ASN A 164 ? 0.2215 0.2045 0.2162 0.0052  -0.0051 -0.0084 194 ASN A CG  
1170 O OD1 . ASN A 164 ? 0.2024 0.1857 0.1980 0.0074  -0.0029 -0.0061 194 ASN A OD1 
1171 N ND2 . ASN A 164 ? 0.2658 0.2481 0.2622 0.0021  -0.0062 -0.0092 194 ASN A ND2 
1172 N N   . TYR A 165 ? 0.2290 0.2122 0.2135 0.0117  -0.0043 -0.0099 195 TYR A N   
1173 C CA  . TYR A 165 ? 0.1887 0.1734 0.1709 0.0122  -0.0052 -0.0104 195 TYR A CA  
1174 C C   . TYR A 165 ? 0.2160 0.2072 0.2026 0.0126  -0.0059 -0.0088 195 TYR A C   
1175 O O   . TYR A 165 ? 0.2002 0.1931 0.1863 0.0122  -0.0076 -0.0092 195 TYR A O   
1176 C CB  . TYR A 165 ? 0.1933 0.1741 0.1714 0.0143  -0.0024 -0.0104 195 TYR A CB  
1177 C CG  . TYR A 165 ? 0.2417 0.2150 0.2146 0.0140  -0.0014 -0.0124 195 TYR A CG  
1178 C CD1 . TYR A 165 ? 0.2076 0.1772 0.1750 0.0121  -0.0036 -0.0150 195 TYR A CD1 
1179 C CD2 . TYR A 165 ? 0.2146 0.1843 0.1881 0.0155  0.0017  -0.0118 195 TYR A CD2 
1180 C CE1 . TYR A 165 ? 0.2166 0.1787 0.1787 0.0113  -0.0028 -0.0174 195 TYR A CE1 
1181 C CE2 . TYR A 165 ? 0.2140 0.1756 0.1824 0.0152  0.0030  -0.0140 195 TYR A CE2 
1182 C CZ  . TYR A 165 ? 0.2289 0.1864 0.1913 0.0128  0.0007  -0.0170 195 TYR A CZ  
1183 O OH  . TYR A 165 ? 0.2303 0.1791 0.1869 0.0120  0.0019  -0.0198 195 TYR A OH  
1184 N N   . GLY A 166 ? 0.2090 0.2036 0.1997 0.0132  -0.0048 -0.0072 196 GLY A N   
1185 C CA  . GLY A 166 ? 0.1799 0.1800 0.1740 0.0131  -0.0056 -0.0063 196 GLY A CA  
1186 C C   . GLY A 166 ? 0.1701 0.1723 0.1658 0.0116  -0.0077 -0.0071 196 GLY A C   
1187 O O   . GLY A 166 ? 0.1952 0.1998 0.1918 0.0115  -0.0087 -0.0073 196 GLY A O   
1188 N N   . LEU A 167 ? 0.2000 0.2014 0.1965 0.0103  -0.0083 -0.0075 197 LEU A N   
1189 C CA  . LEU A 167 ? 0.1959 0.2001 0.1949 0.0090  -0.0100 -0.0080 197 LEU A CA  
1190 C C   . LEU A 167 ? 0.1718 0.1753 0.1690 0.0087  -0.0121 -0.0092 197 LEU A C   
1191 O O   . LEU A 167 ? 0.1919 0.1988 0.1914 0.0089  -0.0133 -0.0092 197 LEU A O   
1192 C CB  . LEU A 167 ? 0.1716 0.1749 0.1723 0.0073  -0.0100 -0.0080 197 LEU A CB  
1193 C CG  . LEU A 167 ? 0.1807 0.1849 0.1830 0.0077  -0.0080 -0.0062 197 LEU A CG  
1194 C CD1 . LEU A 167 ? 0.1962 0.1989 0.2002 0.0057  -0.0077 -0.0060 197 LEU A CD1 
1195 C CD2 . LEU A 167 ? 0.1801 0.1896 0.1847 0.0083  -0.0078 -0.0054 197 LEU A CD2 
1196 N N   . LEU A 168 ? 0.1824 0.1815 0.1753 0.0086  -0.0124 -0.0102 198 LEU A N   
1197 C CA  . LEU A 168 ? 0.1954 0.1938 0.1854 0.0085  -0.0146 -0.0110 198 LEU A CA  
1198 C C   . LEU A 168 ? 0.1768 0.1766 0.1665 0.0103  -0.0141 -0.0100 198 LEU A C   
1199 O O   . LEU A 168 ? 0.2003 0.2015 0.1900 0.0106  -0.0160 -0.0098 198 LEU A O   
1200 C CB  . LEU A 168 ? 0.1859 0.1786 0.1698 0.0081  -0.0146 -0.0124 198 LEU A CB  
1201 C CG  . LEU A 168 ? 0.1971 0.1872 0.1806 0.0057  -0.0157 -0.0139 198 LEU A CG  
1202 C CD1 . LEU A 168 ? 0.1983 0.1813 0.1747 0.0055  -0.0149 -0.0158 198 LEU A CD1 
1203 C CD2 . LEU A 168 ? 0.1902 0.1842 0.1763 0.0037  -0.0194 -0.0145 198 LEU A CD2 
1204 N N   . ASP A 169 ? 0.2046 0.2040 0.1943 0.0114  -0.0117 -0.0091 199 ASP A N   
1205 C CA  . ASP A 169 ? 0.2351 0.2355 0.2250 0.0124  -0.0111 -0.0083 199 ASP A CA  
1206 C C   . ASP A 169 ? 0.2279 0.2321 0.2221 0.0123  -0.0118 -0.0081 199 ASP A C   
1207 O O   . ASP A 169 ? 0.1940 0.1984 0.1882 0.0130  -0.0124 -0.0077 199 ASP A O   
1208 C CB  . ASP A 169 ? 0.1726 0.1728 0.1627 0.0132  -0.0085 -0.0074 199 ASP A CB  
1209 C CG  . ASP A 169 ? 0.2002 0.1964 0.1859 0.0139  -0.0070 -0.0075 199 ASP A CG  
1210 O OD1 . ASP A 169 ? 0.1874 0.1803 0.1685 0.0138  -0.0080 -0.0084 199 ASP A OD1 
1211 O OD2 . ASP A 169 ? 0.1950 0.1914 0.1817 0.0147  -0.0047 -0.0067 199 ASP A OD2 
1212 N N   . ILE A 170 ? 0.1776 0.1845 0.1751 0.0117  -0.0115 -0.0082 200 ILE A N   
1213 C CA  . ILE A 170 ? 0.1748 0.1850 0.1758 0.0117  -0.0118 -0.0083 200 ILE A CA  
1214 C C   . ILE A 170 ? 0.1906 0.2017 0.1927 0.0120  -0.0137 -0.0084 200 ILE A C   
1215 O O   . ILE A 170 ? 0.1702 0.1820 0.1736 0.0130  -0.0139 -0.0082 200 ILE A O   
1216 C CB  . ILE A 170 ? 0.2090 0.2217 0.2125 0.0109  -0.0111 -0.0082 200 ILE A CB  
1217 C CG1 . ILE A 170 ? 0.2119 0.2243 0.2145 0.0109  -0.0096 -0.0075 200 ILE A CG1 
1218 C CG2 . ILE A 170 ? 0.2220 0.2378 0.2283 0.0111  -0.0107 -0.0085 200 ILE A CG2 
1219 C CD1 . ILE A 170 ? 0.2507 0.2647 0.2536 0.0111  -0.0089 -0.0075 200 ILE A CD1 
1220 N N   . LEU A 171 ? 0.1987 0.2094 0.2002 0.0110  -0.0153 -0.0087 201 LEU A N   
1221 C CA  . LEU A 171 ? 0.1899 0.2027 0.1930 0.0110  -0.0177 -0.0087 201 LEU A CA  
1222 C C   . LEU A 171 ? 0.2135 0.2243 0.2134 0.0125  -0.0188 -0.0080 201 LEU A C   
1223 O O   . LEU A 171 ? 0.1923 0.2053 0.1945 0.0137  -0.0201 -0.0072 201 LEU A O   
1224 C CB  . LEU A 171 ? 0.1903 0.2029 0.1932 0.0090  -0.0195 -0.0094 201 LEU A CB  
1225 C CG  . LEU A 171 ? 0.2106 0.2252 0.2174 0.0074  -0.0182 -0.0096 201 LEU A CG  
1226 C CD1 . LEU A 171 ? 0.2414 0.2533 0.2466 0.0051  -0.0192 -0.0105 201 LEU A CD1 
1227 C CD2 . LEU A 171 ? 0.1693 0.1896 0.1823 0.0075  -0.0185 -0.0089 201 LEU A CD2 
1228 N N   . ALA A 172 ? 0.1853 0.1920 0.1800 0.0127  -0.0181 -0.0081 202 ALA A N   
1229 C CA  . ALA A 172 ? 0.2037 0.2080 0.1946 0.0141  -0.0186 -0.0071 202 ALA A CA  
1230 C C   . ALA A 172 ? 0.2115 0.2161 0.2048 0.0155  -0.0172 -0.0060 202 ALA A C   
1231 O O   . ALA A 172 ? 0.2070 0.2111 0.1998 0.0170  -0.0182 -0.0048 202 ALA A O   
1232 C CB  . ALA A 172 ? 0.1974 0.1972 0.1823 0.0140  -0.0172 -0.0072 202 ALA A CB  
1233 N N   . ALA A 173 ? 0.2169 0.2219 0.2124 0.0151  -0.0149 -0.0066 203 ALA A N   
1234 C CA  . ALA A 173 ? 0.1876 0.1923 0.1851 0.0159  -0.0135 -0.0062 203 ALA A CA  
1235 C C   . ALA A 173 ? 0.2023 0.2096 0.2038 0.0171  -0.0144 -0.0062 203 ALA A C   
1236 O O   . ALA A 173 ? 0.1735 0.1793 0.1756 0.0187  -0.0141 -0.0053 203 ALA A O   
1237 C CB  . ALA A 173 ? 0.1690 0.1742 0.1678 0.0148  -0.0115 -0.0071 203 ALA A CB  
1238 N N   . LEU A 174 ? 0.1944 0.2054 0.1990 0.0164  -0.0152 -0.0068 204 LEU A N   
1239 C CA  . LEU A 174 ? 0.2182 0.2327 0.2274 0.0177  -0.0157 -0.0065 204 LEU A CA  
1240 C C   . LEU A 174 ? 0.2064 0.2214 0.2157 0.0193  -0.0182 -0.0049 204 LEU A C   
1241 O O   . LEU A 174 ? 0.1987 0.2148 0.2111 0.0215  -0.0182 -0.0040 204 LEU A O   
1242 C CB  . LEU A 174 ? 0.1658 0.1845 0.1786 0.0163  -0.0158 -0.0072 204 LEU A CB  
1243 C CG  . LEU A 174 ? 0.2021 0.2209 0.2150 0.0154  -0.0133 -0.0083 204 LEU A CG  
1244 C CD1 . LEU A 174 ? 0.1616 0.1835 0.1766 0.0137  -0.0132 -0.0084 204 LEU A CD1 
1245 C CD2 . LEU A 174 ? 0.1638 0.1829 0.1787 0.0168  -0.0113 -0.0088 204 LEU A CD2 
1246 N N   . ARG A 175 ? 0.1925 0.2067 0.1982 0.0183  -0.0205 -0.0046 205 ARG A N   
1247 C CA  . ARG A 175 ? 0.2403 0.2551 0.2448 0.0198  -0.0234 -0.0029 205 ARG A CA  
1248 C C   . ARG A 175 ? 0.2262 0.2367 0.2278 0.0220  -0.0223 -0.0013 205 ARG A C   
1249 O O   . ARG A 175 ? 0.2110 0.2226 0.2143 0.0244  -0.0235 0.0007  205 ARG A O   
1250 C CB  . ARG A 175 ? 0.2457 0.2598 0.2454 0.0179  -0.0259 -0.0035 205 ARG A CB  
1251 C CG  . ARG A 175 ? 0.4234 0.4362 0.4183 0.0191  -0.0287 -0.0018 205 ARG A CG  
1252 C CD  . ARG A 175 ? 0.5002 0.5181 0.4998 0.0211  -0.0316 0.0002  205 ARG A CD  
1253 N NE  . ARG A 175 ? 0.5613 0.5856 0.5687 0.0200  -0.0326 -0.0006 205 ARG A NE  
1254 C CZ  . ARG A 175 ? 0.5540 0.5841 0.5680 0.0218  -0.0343 0.0011  205 ARG A CZ  
1255 N NH1 . ARG A 175 ? 0.6502 0.6803 0.6639 0.0251  -0.0355 0.0038  205 ARG A NH1 
1256 N NH2 . ARG A 175 ? 0.4773 0.5134 0.4987 0.0206  -0.0346 0.0005  205 ARG A NH2 
1257 N N   . TRP A 176 ? 0.2142 0.2201 0.2119 0.0213  -0.0198 -0.0017 206 TRP A N   
1258 C CA  . TRP A 176 ? 0.2014 0.2029 0.1972 0.0229  -0.0181 -0.0002 206 TRP A CA  
1259 C C   . TRP A 176 ? 0.2051 0.2069 0.2058 0.0247  -0.0167 0.0001  206 TRP A C   
1260 O O   . TRP A 176 ? 0.2229 0.2224 0.2236 0.0271  -0.0167 0.0021  206 TRP A O   
1261 C CB  . TRP A 176 ? 0.1948 0.1926 0.1876 0.0212  -0.0153 -0.0010 206 TRP A CB  
1262 C CG  . TRP A 176 ? 0.2239 0.2167 0.2144 0.0222  -0.0135 0.0008  206 TRP A CG  
1263 C CD1 . TRP A 176 ? 0.2561 0.2455 0.2412 0.0225  -0.0132 0.0026  206 TRP A CD1 
1264 C CD2 . TRP A 176 ? 0.2460 0.2361 0.2391 0.0228  -0.0113 0.0008  206 TRP A CD2 
1265 N NE1 . TRP A 176 ? 0.2804 0.2655 0.2653 0.0231  -0.0110 0.0042  206 TRP A NE1 
1266 C CE2 . TRP A 176 ? 0.2135 0.1986 0.2033 0.0232  -0.0099 0.0029  206 TRP A CE2 
1267 C CE3 . TRP A 176 ? 0.2142 0.2052 0.2117 0.0229  -0.0102 -0.0008 206 TRP A CE3 
1268 C CZ2 . TRP A 176 ? 0.2094 0.1900 0.2006 0.0235  -0.0075 0.0034  206 TRP A CZ2 
1269 C CZ3 . TRP A 176 ? 0.1915 0.1778 0.1898 0.0233  -0.0080 -0.0008 206 TRP A CZ3 
1270 C CH2 . TRP A 176 ? 0.2192 0.2002 0.2146 0.0234  -0.0067 0.0013  206 TRP A CH2 
1271 N N   . VAL A 177 ? 0.1992 0.2034 0.2038 0.0238  -0.0154 -0.0020 207 VAL A N   
1272 C CA  . VAL A 177 ? 0.1937 0.1976 0.2023 0.0256  -0.0136 -0.0023 207 VAL A CA  
1273 C C   . VAL A 177 ? 0.2101 0.2177 0.2229 0.0284  -0.0154 -0.0004 207 VAL A C   
1274 O O   . VAL A 177 ? 0.1869 0.1923 0.2013 0.0313  -0.0144 0.0010  207 VAL A O   
1275 C CB  . VAL A 177 ? 0.1933 0.1995 0.2043 0.0240  -0.0117 -0.0048 207 VAL A CB  
1276 C CG1 . VAL A 177 ? 0.1787 0.1854 0.1937 0.0261  -0.0099 -0.0053 207 VAL A CG1 
1277 C CG2 . VAL A 177 ? 0.1767 0.1793 0.1844 0.0217  -0.0100 -0.0063 207 VAL A CG2 
1278 N N   . GLN A 178 ? 0.1853 0.1987 0.2002 0.0277  -0.0181 -0.0002 208 GLN A N   
1279 C CA  . GLN A 178 ? 0.2155 0.2338 0.2349 0.0301  -0.0205 0.0019  208 GLN A CA  
1280 C C   . GLN A 178 ? 0.2709 0.2861 0.2875 0.0327  -0.0219 0.0049  208 GLN A C   
1281 O O   . GLN A 178 ? 0.2440 0.2602 0.2646 0.0362  -0.0218 0.0070  208 GLN A O   
1282 C CB  . GLN A 178 ? 0.2601 0.2843 0.2809 0.0278  -0.0239 0.0016  208 GLN A CB  
1283 C CG  . GLN A 178 ? 0.2935 0.3223 0.3194 0.0261  -0.0226 -0.0002 208 GLN A CG  
1284 C CD  . GLN A 178 ? 0.2265 0.2588 0.2595 0.0289  -0.0207 0.0005  208 GLN A CD  
1285 O OE1 . GLN A 178 ? 0.2286 0.2658 0.2666 0.0311  -0.0226 0.0026  208 GLN A OE1 
1286 N NE2 . GLN A 178 ? 0.1844 0.2144 0.2175 0.0290  -0.0167 -0.0013 208 GLN A NE2 
1287 N N   . SER A 179 ? 0.2037 0.2150 0.2134 0.0314  -0.0229 0.0053  209 SER A N   
1288 C CA  . SER A 179 ? 0.2379 0.2463 0.2438 0.0337  -0.0244 0.0085  209 SER A CA  
1289 C C   . SER A 179 ? 0.2848 0.2861 0.2895 0.0358  -0.0210 0.0098  209 SER A C   
1290 O O   . SER A 179 ? 0.3280 0.3273 0.3315 0.0388  -0.0217 0.0131  209 SER A O   
1291 C CB  . SER A 179 ? 0.2482 0.2545 0.2462 0.0316  -0.0262 0.0085  209 SER A CB  
1292 O OG  . SER A 179 ? 0.3580 0.3698 0.3564 0.0297  -0.0297 0.0073  209 SER A OG  
1293 N N   . ASN A 180 ? 0.2159 0.2135 0.2207 0.0341  -0.0173 0.0073  210 ASN A N   
1294 C CA  . ASN A 180 ? 0.2331 0.2231 0.2358 0.0348  -0.0141 0.0081  210 ASN A CA  
1295 C C   . ASN A 180 ? 0.2551 0.2427 0.2621 0.0357  -0.0109 0.0064  210 ASN A C   
1296 O O   . ASN A 180 ? 0.3020 0.2826 0.3076 0.0362  -0.0082 0.0068  210 ASN A O   
1297 C CB  . ASN A 180 ? 0.2586 0.2449 0.2562 0.0315  -0.0127 0.0069  210 ASN A CB  
1298 C CG  . ASN A 180 ? 0.2691 0.2555 0.2609 0.0311  -0.0148 0.0089  210 ASN A CG  
1299 O OD1 . ASN A 180 ? 0.2507 0.2332 0.2390 0.0329  -0.0147 0.0119  210 ASN A OD1 
1300 N ND2 . ASN A 180 ? 0.2657 0.2559 0.2560 0.0290  -0.0165 0.0071  210 ASN A ND2 
1301 N N   . ALA A 181 ? 0.2294 0.2221 0.2413 0.0359  -0.0109 0.0044  211 ALA A N   
1302 C CA  . ALA A 181 ? 0.2509 0.2408 0.2654 0.0365  -0.0074 0.0020  211 ALA A CA  
1303 C C   . ALA A 181 ? 0.2344 0.2189 0.2504 0.0404  -0.0054 0.0040  211 ALA A C   
1304 O O   . ALA A 181 ? 0.2348 0.2123 0.2497 0.0400  -0.0021 0.0023  211 ALA A O   
1305 C CB  . ALA A 181 ? 0.2371 0.2340 0.2564 0.0365  -0.0075 0.0002  211 ALA A CB  
1306 N N   . ARG A 182 ? 0.2492 0.2365 0.2678 0.0441  -0.0075 0.0077  212 ARG A N   
1307 C CA  . ARG A 182 ? 0.2664 0.2486 0.2871 0.0486  -0.0055 0.0101  212 ARG A CA  
1308 C C   . ARG A 182 ? 0.2912 0.2633 0.3067 0.0481  -0.0034 0.0112  212 ARG A C   
1309 O O   . ARG A 182 ? 0.2874 0.2519 0.3035 0.0496  0.0002  0.0107  212 ARG A O   
1310 C CB  . ARG A 182 ? 0.3282 0.3164 0.3527 0.0528  -0.0088 0.0145  212 ARG A CB  
1311 C CG  . ARG A 182 ? 0.4003 0.3985 0.4318 0.0538  -0.0102 0.0138  212 ARG A CG  
1312 C CD  . ARG A 182 ? 0.3369 0.3413 0.3733 0.0582  -0.0134 0.0185  212 ARG A CD  
1313 N NE  . ARG A 182 ? 0.4833 0.4989 0.5260 0.0575  -0.0161 0.0180  212 ARG A NE  
1314 C CZ  . ARG A 182 ? 0.6150 0.6353 0.6651 0.0592  -0.0137 0.0167  212 ARG A CZ  
1315 N NH1 . ARG A 182 ? 0.5343 0.5485 0.5858 0.0618  -0.0086 0.0154  212 ARG A NH1 
1316 N NH2 . ARG A 182 ? 0.6631 0.6939 0.7190 0.0580  -0.0162 0.0166  212 ARG A NH2 
1317 N N   . ALA A 183 ? 0.2728 0.2442 0.2831 0.0457  -0.0054 0.0127  213 ALA A N   
1318 C CA  . ALA A 183 ? 0.3061 0.2685 0.3117 0.0447  -0.0032 0.0140  213 ALA A CA  
1319 C C   . ALA A 183 ? 0.2906 0.2472 0.2957 0.0412  0.0005  0.0100  213 ALA A C   
1320 O O   . ALA A 183 ? 0.3301 0.2780 0.3331 0.0407  0.0031  0.0108  213 ALA A O   
1321 C CB  . ALA A 183 ? 0.2776 0.2416 0.2777 0.0423  -0.0055 0.0157  213 ALA A CB  
1322 N N   . PHE A 184 ? 0.2703 0.2312 0.2769 0.0386  0.0005  0.0057  214 PHE A N   
1323 C CA  . PHE A 184 ? 0.2942 0.2506 0.2999 0.0350  0.0033  0.0017  214 PHE A CA  
1324 C C   . PHE A 184 ? 0.2745 0.2294 0.2831 0.0366  0.0056  -0.0014 214 PHE A C   
1325 O O   . PHE A 184 ? 0.3153 0.2688 0.3229 0.0335  0.0072  -0.0055 214 PHE A O   
1326 C CB  . PHE A 184 ? 0.2214 0.1832 0.2255 0.0305  0.0018  -0.0007 214 PHE A CB  
1327 C CG  . PHE A 184 ? 0.3107 0.2720 0.3114 0.0285  0.0008  0.0015  214 PHE A CG  
1328 C CD1 . PHE A 184 ? 0.2313 0.1972 0.2306 0.0299  -0.0020 0.0043  214 PHE A CD1 
1329 C CD2 . PHE A 184 ? 0.2703 0.2267 0.2692 0.0251  0.0027  0.0007  214 PHE A CD2 
1330 C CE1 . PHE A 184 ? 0.2371 0.2021 0.2324 0.0283  -0.0023 0.0062  214 PHE A CE1 
1331 C CE2 . PHE A 184 ? 0.2853 0.2416 0.2814 0.0234  0.0024  0.0029  214 PHE A CE2 
1332 C CZ  . PHE A 184 ? 0.2597 0.2200 0.2536 0.0252  0.0001  0.0056  214 PHE A CZ  
1333 N N   . GLY A 185 ? 0.2569 0.2124 0.2690 0.0416  0.0060  0.0007  215 GLY A N   
1334 C CA  . GLY A 185 ? 0.2585 0.2124 0.2735 0.0439  0.0090  -0.0019 215 GLY A CA  
1335 C C   . GLY A 185 ? 0.2930 0.2560 0.3111 0.0440  0.0081  -0.0039 215 GLY A C   
1336 O O   . GLY A 185 ? 0.2723 0.2342 0.2920 0.0455  0.0110  -0.0065 215 GLY A O   
1337 N N   . GLY A 186 ? 0.2741 0.2459 0.2929 0.0425  0.0045  -0.0027 216 GLY A N   
1338 C CA  . GLY A 186 ? 0.2167 0.1968 0.2384 0.0418  0.0038  -0.0045 216 GLY A CA  
1339 C C   . GLY A 186 ? 0.2951 0.2834 0.3227 0.0453  0.0017  -0.0015 216 GLY A C   
1340 O O   . GLY A 186 ? 0.2776 0.2666 0.3064 0.0478  -0.0005 0.0024  216 GLY A O   
1341 N N   . ASP A 187 ? 0.3028 0.2978 0.3341 0.0453  0.0023  -0.0030 217 ASP A N   
1342 C CA  . ASP A 187 ? 0.2405 0.2446 0.2787 0.0479  0.0004  -0.0004 217 ASP A CA  
1343 C C   . ASP A 187 ? 0.2406 0.2522 0.2789 0.0441  -0.0030 -0.0007 217 ASP A C   
1344 O O   . ASP A 187 ? 0.1903 0.2040 0.2279 0.0415  -0.0016 -0.0034 217 ASP A O   
1345 C CB  . ASP A 187 ? 0.2441 0.2504 0.2875 0.0509  0.0044  -0.0017 217 ASP A CB  
1346 C CG  . ASP A 187 ? 0.2498 0.2659 0.3021 0.0543  0.0029  0.0015  217 ASP A CG  
1347 O OD1 . ASP A 187 ? 0.2659 0.2888 0.3202 0.0529  -0.0017 0.0038  217 ASP A OD1 
1348 O OD2 . ASP A 187 ? 0.3102 0.3274 0.3677 0.0583  0.0064  0.0016  217 ASP A OD2 
1349 N N   . PRO A 188 ? 0.2585 0.2739 0.2971 0.0438  -0.0073 0.0020  218 PRO A N   
1350 C CA  . PRO A 188 ? 0.2202 0.2417 0.2585 0.0400  -0.0103 0.0015  218 PRO A CA  
1351 C C   . PRO A 188 ? 0.2200 0.2499 0.2652 0.0399  -0.0100 0.0011  218 PRO A C   
1352 O O   . PRO A 188 ? 0.2217 0.2552 0.2665 0.0364  -0.0113 -0.0001 218 PRO A O   
1353 C CB  . PRO A 188 ? 0.2493 0.2724 0.2864 0.0404  -0.0149 0.0045  218 PRO A CB  
1354 C CG  . PRO A 188 ? 0.2935 0.3157 0.3339 0.0453  -0.0145 0.0075  218 PRO A CG  
1355 C CD  . PRO A 188 ? 0.3015 0.3159 0.3405 0.0469  -0.0096 0.0058  218 PRO A CD  
1356 N N   . GLY A 189 ? 0.1848 0.2178 0.2366 0.0438  -0.0079 0.0022  219 GLY A N   
1357 C CA  . GLY A 189 ? 0.2047 0.2458 0.2635 0.0438  -0.0067 0.0019  219 GLY A CA  
1358 C C   . GLY A 189 ? 0.2695 0.3081 0.3264 0.0428  -0.0018 -0.0013 219 GLY A C   
1359 O O   . GLY A 189 ? 0.2253 0.2701 0.2874 0.0428  0.0000  -0.0015 219 GLY A O   
1360 N N   . ARG A 190 ? 0.1842 0.2139 0.2336 0.0419  0.0002  -0.0037 220 ARG A N   
1361 C CA  . ARG A 190 ? 0.2082 0.2348 0.2541 0.0407  0.0043  -0.0070 220 ARG A CA  
1362 C C   . ARG A 190 ? 0.2225 0.2442 0.2604 0.0364  0.0031  -0.0091 220 ARG A C   
1363 O O   . ARG A 190 ? 0.1870 0.2016 0.2194 0.0358  0.0050  -0.0114 220 ARG A O   
1364 C CB  . ARG A 190 ? 0.2353 0.2558 0.2807 0.0444  0.0087  -0.0084 220 ARG A CB  
1365 C CG  . ARG A 190 ? 0.2989 0.3246 0.3527 0.0492  0.0110  -0.0065 220 ARG A CG  
1366 C CD  . ARG A 190 ? 0.3432 0.3624 0.3950 0.0521  0.0168  -0.0092 220 ARG A CD  
1367 N NE  . ARG A 190 ? 0.2806 0.2901 0.3290 0.0542  0.0175  -0.0094 220 ARG A NE  
1368 C CZ  . ARG A 190 ? 0.2659 0.2664 0.3097 0.0553  0.0219  -0.0126 220 ARG A CZ  
1369 N NH1 . ARG A 190 ? 0.2411 0.2408 0.2819 0.0546  0.0258  -0.0162 220 ARG A NH1 
1370 N NH2 . ARG A 190 ? 0.2653 0.2568 0.3068 0.0572  0.0225  -0.0123 220 ARG A NH2 
1371 N N   . VAL A 191 ? 0.2281 0.2538 0.2657 0.0334  -0.0001 -0.0083 221 VAL A N   
1372 C CA  . VAL A 191 ? 0.1895 0.2118 0.2207 0.0297  -0.0013 -0.0097 221 VAL A CA  
1373 C C   . VAL A 191 ? 0.2203 0.2457 0.2507 0.0274  0.0003  -0.0111 221 VAL A C   
1374 O O   . VAL A 191 ? 0.2216 0.2532 0.2566 0.0271  0.0001  -0.0101 221 VAL A O   
1375 C CB  . VAL A 191 ? 0.2198 0.2433 0.2502 0.0280  -0.0054 -0.0079 221 VAL A CB  
1376 C CG1 . VAL A 191 ? 0.1729 0.1936 0.1977 0.0246  -0.0060 -0.0092 221 VAL A CG1 
1377 C CG2 . VAL A 191 ? 0.1763 0.1964 0.2063 0.0303  -0.0069 -0.0061 221 VAL A CG2 
1378 N N   . THR A 192 ? 0.1751 0.1962 0.1998 0.0257  0.0017  -0.0134 222 THR A N   
1379 C CA  . THR A 192 ? 0.1736 0.1969 0.1959 0.0234  0.0027  -0.0144 222 THR A CA  
1380 C C   . THR A 192 ? 0.1963 0.2175 0.2141 0.0205  0.0004  -0.0145 222 THR A C   
1381 O O   . THR A 192 ? 0.1935 0.2099 0.2076 0.0200  0.0001  -0.0156 222 THR A O   
1382 C CB  . THR A 192 ? 0.1889 0.2097 0.2078 0.0240  0.0063  -0.0170 222 THR A CB  
1383 O OG1 . THR A 192 ? 0.2378 0.2610 0.2614 0.0271  0.0092  -0.0168 222 THR A OG1 
1384 C CG2 . THR A 192 ? 0.1781 0.2007 0.1931 0.0215  0.0069  -0.0178 222 THR A CG2 
1385 N N   . VAL A 193 ? 0.1675 0.1921 0.1860 0.0187  -0.0011 -0.0133 223 VAL A N   
1386 C CA  . VAL A 193 ? 0.1657 0.1887 0.1804 0.0165  -0.0027 -0.0132 223 VAL A CA  
1387 C C   . VAL A 193 ? 0.2260 0.2499 0.2374 0.0152  -0.0011 -0.0141 223 VAL A C   
1388 O O   . VAL A 193 ? 0.1840 0.2111 0.1967 0.0153  0.0005  -0.0138 223 VAL A O   
1389 C CB  . VAL A 193 ? 0.1625 0.1875 0.1790 0.0154  -0.0049 -0.0114 223 VAL A CB  
1390 C CG1 . VAL A 193 ? 0.1614 0.1909 0.1813 0.0148  -0.0041 -0.0105 223 VAL A CG1 
1391 C CG2 . VAL A 193 ? 0.1686 0.1916 0.1815 0.0138  -0.0060 -0.0112 223 VAL A CG2 
1392 N N   . PHE A 194 ? 0.1681 0.1894 0.1753 0.0140  -0.0016 -0.0153 224 PHE A N   
1393 C CA  . PHE A 194 ? 0.1700 0.1925 0.1734 0.0127  -0.0008 -0.0160 224 PHE A CA  
1394 C C   . PHE A 194 ? 0.2059 0.2283 0.2072 0.0110  -0.0028 -0.0153 224 PHE A C   
1395 O O   . PHE A 194 ? 0.1804 0.2007 0.1823 0.0107  -0.0041 -0.0152 224 PHE A O   
1396 C CB  . PHE A 194 ? 0.1755 0.1957 0.1757 0.0130  0.0012  -0.0188 224 PHE A CB  
1397 C CG  . PHE A 194 ? 0.1948 0.2105 0.1928 0.0122  0.0004  -0.0207 224 PHE A CG  
1398 C CD1 . PHE A 194 ? 0.1764 0.1896 0.1770 0.0128  -0.0006 -0.0199 224 PHE A CD1 
1399 C CD2 . PHE A 194 ? 0.1833 0.1972 0.1765 0.0106  0.0008  -0.0233 224 PHE A CD2 
1400 C CE1 . PHE A 194 ? 0.1795 0.1882 0.1785 0.0118  -0.0009 -0.0214 224 PHE A CE1 
1401 C CE2 . PHE A 194 ? 0.2494 0.2589 0.2411 0.0093  0.0002  -0.0252 224 PHE A CE2 
1402 C CZ  . PHE A 194 ? 0.2074 0.2143 0.2023 0.0099  -0.0005 -0.0241 224 PHE A CZ  
1403 N N   . GLY A 195 ? 0.1839 0.2088 0.1831 0.0101  -0.0029 -0.0144 225 GLY A N   
1404 C CA  . GLY A 195 ? 0.1964 0.2222 0.1947 0.0090  -0.0047 -0.0131 225 GLY A CA  
1405 C C   . GLY A 195 ? 0.2023 0.2309 0.1973 0.0082  -0.0047 -0.0125 225 GLY A C   
1406 O O   . GLY A 195 ? 0.1880 0.2176 0.1808 0.0085  -0.0031 -0.0130 225 GLY A O   
1407 N N   . GLU A 196 ? 0.1687 0.1988 0.1632 0.0075  -0.0064 -0.0111 226 GLU A N   
1408 C CA  . GLU A 196 ? 0.1758 0.2092 0.1670 0.0070  -0.0070 -0.0100 226 GLU A CA  
1409 C C   . GLU A 196 ? 0.1853 0.2205 0.1784 0.0076  -0.0079 -0.0066 226 GLU A C   
1410 O O   . GLU A 196 ? 0.2247 0.2590 0.2207 0.0079  -0.0086 -0.0059 226 GLU A O   
1411 C CB  . GLU A 196 ? 0.2432 0.2776 0.2311 0.0053  -0.0085 -0.0122 226 GLU A CB  
1412 C CG  . GLU A 196 ? 0.1798 0.2179 0.1630 0.0046  -0.0093 -0.0114 226 GLU A CG  
1413 C CD  . GLU A 196 ? 0.1875 0.2297 0.1720 0.0045  -0.0118 -0.0084 226 GLU A CD  
1414 O OE1 . GLU A 196 ? 0.1784 0.2205 0.1672 0.0045  -0.0127 -0.0077 226 GLU A OE1 
1415 O OE2 . GLU A 196 ? 0.1876 0.2333 0.1688 0.0046  -0.0126 -0.0065 226 GLU A OE2 
1416 N N   . SER A 197 ? 0.1731 0.2105 0.1641 0.0081  -0.0075 -0.0043 227 SER A N   
1417 C CA  . SER A 197 ? 0.2393 0.2780 0.2316 0.0091  -0.0080 -0.0006 227 SER A CA  
1418 C C   . SER A 197 ? 0.2180 0.2533 0.2143 0.0099  -0.0070 0.0001  227 SER A C   
1419 O O   . SER A 197 ? 0.2094 0.2426 0.2066 0.0098  -0.0055 -0.0006 227 SER A O   
1420 C CB  . SER A 197 ? 0.1716 0.2138 0.1639 0.0088  -0.0104 0.0002  227 SER A CB  
1421 O OG  . SER A 197 ? 0.2068 0.2506 0.2006 0.0104  -0.0106 0.0041  227 SER A OG  
1422 N N   . ALA A 198 ? 0.1850 0.2197 0.1836 0.0107  -0.0077 0.0014  228 ALA A N   
1423 C CA  . ALA A 198 ? 0.1661 0.1968 0.1672 0.0113  -0.0067 0.0017  228 ALA A CA  
1424 C C   . ALA A 198 ? 0.1766 0.2048 0.1785 0.0105  -0.0065 -0.0011 228 ALA A C   
1425 O O   . ALA A 198 ? 0.1774 0.2028 0.1805 0.0105  -0.0059 -0.0012 228 ALA A O   
1426 C CB  . ALA A 198 ? 0.1865 0.2169 0.1894 0.0125  -0.0071 0.0031  228 ALA A CB  
1427 N N   . GLY A 199 ? 0.1823 0.2115 0.1836 0.0098  -0.0072 -0.0033 229 GLY A N   
1428 C CA  . GLY A 199 ? 0.1607 0.1877 0.1628 0.0096  -0.0069 -0.0055 229 GLY A CA  
1429 C C   . GLY A 199 ? 0.1614 0.1888 0.1639 0.0095  -0.0058 -0.0058 229 GLY A C   
1430 O O   . GLY A 199 ? 0.1605 0.1864 0.1651 0.0096  -0.0056 -0.0061 229 GLY A O   
1431 N N   . ALA A 200 ? 0.1763 0.2060 0.1766 0.0093  -0.0050 -0.0056 230 ALA A N   
1432 C CA  . ALA A 200 ? 0.1753 0.2059 0.1762 0.0093  -0.0032 -0.0054 230 ALA A CA  
1433 C C   . ALA A 200 ? 0.1874 0.2174 0.1904 0.0091  -0.0026 -0.0030 230 ALA A C   
1434 O O   . ALA A 200 ? 0.1874 0.2176 0.1932 0.0088  -0.0016 -0.0031 230 ALA A O   
1435 C CB  . ALA A 200 ? 0.1687 0.2015 0.1655 0.0091  -0.0022 -0.0056 230 ALA A CB  
1436 N N   . SER A 201 ? 0.1833 0.2124 0.1855 0.0093  -0.0032 -0.0010 231 SER A N   
1437 C CA  . SER A 201 ? 0.1731 0.2001 0.1771 0.0091  -0.0024 0.0010  231 SER A CA  
1438 C C   . SER A 201 ? 0.1928 0.2171 0.1996 0.0085  -0.0032 -0.0004 231 SER A C   
1439 O O   . SER A 201 ? 0.2010 0.2243 0.2101 0.0074  -0.0026 0.0000  231 SER A O   
1440 C CB  . SER A 201 ? 0.1675 0.1935 0.1702 0.0100  -0.0026 0.0035  231 SER A CB  
1441 O OG  . SER A 201 ? 0.1695 0.1988 0.1694 0.0106  -0.0027 0.0049  231 SER A OG  
1442 N N   . ALA A 202 ? 0.1623 0.1856 0.1687 0.0090  -0.0046 -0.0020 232 ALA A N   
1443 C CA  . ALA A 202 ? 0.1617 0.1825 0.1694 0.0086  -0.0055 -0.0033 232 ALA A CA  
1444 C C   . ALA A 202 ? 0.1774 0.2003 0.1878 0.0081  -0.0057 -0.0045 232 ALA A C   
1445 O O   . ALA A 202 ? 0.1614 0.1836 0.1741 0.0070  -0.0063 -0.0047 232 ALA A O   
1446 C CB  . ALA A 202 ? 0.1606 0.1800 0.1669 0.0095  -0.0066 -0.0043 232 ALA A CB  
1447 N N   . ILE A 203 ? 0.1866 0.2120 0.1969 0.0087  -0.0052 -0.0053 233 ILE A N   
1448 C CA  . ILE A 203 ? 0.1911 0.2188 0.2045 0.0088  -0.0047 -0.0061 233 ILE A CA  
1449 C C   . ILE A 203 ? 0.1764 0.2062 0.1928 0.0076  -0.0035 -0.0048 233 ILE A C   
1450 O O   . ILE A 203 ? 0.1822 0.2136 0.2028 0.0069  -0.0040 -0.0048 233 ILE A O   
1451 C CB  . ILE A 203 ? 0.1679 0.1970 0.1799 0.0098  -0.0036 -0.0074 233 ILE A CB  
1452 C CG1 . ILE A 203 ? 0.1599 0.1866 0.1700 0.0105  -0.0049 -0.0087 233 ILE A CG1 
1453 C CG2 . ILE A 203 ? 0.1808 0.2126 0.1966 0.0105  -0.0024 -0.0078 233 ILE A CG2 
1454 C CD1 . ILE A 203 ? 0.1618 0.1885 0.1696 0.0110  -0.0038 -0.0103 233 ILE A CD1 
1455 N N   . GLY A 204 ? 0.1715 0.2016 0.1860 0.0073  -0.0018 -0.0032 234 GLY A N   
1456 C CA  . GLY A 204 ? 0.1777 0.2094 0.1949 0.0060  -0.0001 -0.0016 234 GLY A CA  
1457 C C   . GLY A 204 ? 0.1888 0.2182 0.2087 0.0042  -0.0011 -0.0010 234 GLY A C   
1458 O O   . GLY A 204 ? 0.1654 0.1969 0.1899 0.0026  -0.0008 -0.0007 234 GLY A O   
1459 N N   . LEU A 205 ? 0.1867 0.2118 0.2038 0.0043  -0.0024 -0.0010 235 LEU A N   
1460 C CA  . LEU A 205 ? 0.1697 0.1913 0.1881 0.0025  -0.0034 -0.0012 235 LEU A CA  
1461 C C   . LEU A 205 ? 0.1663 0.1892 0.1875 0.0017  -0.0057 -0.0031 235 LEU A C   
1462 O O   . LEU A 205 ? 0.1878 0.2106 0.2121 -0.0006 -0.0066 -0.0033 235 LEU A O   
1463 C CB  . LEU A 205 ? 0.1690 0.1854 0.1834 0.0034  -0.0038 -0.0010 235 LEU A CB  
1464 C CG  . LEU A 205 ? 0.1711 0.1862 0.1833 0.0044  -0.0019 0.0015  235 LEU A CG  
1465 C CD1 . LEU A 205 ? 0.1722 0.1833 0.1815 0.0060  -0.0022 0.0017  235 LEU A CD1 
1466 C CD2 . LEU A 205 ? 0.1750 0.1884 0.1892 0.0026  -0.0001 0.0035  235 LEU A CD2 
1467 N N   . LEU A 206 ? 0.1752 0.1994 0.1953 0.0034  -0.0069 -0.0044 236 LEU A N   
1468 C CA  . LEU A 206 ? 0.1632 0.1891 0.1857 0.0032  -0.0093 -0.0057 236 LEU A CA  
1469 C C   . LEU A 206 ? 0.1720 0.2035 0.2006 0.0025  -0.0089 -0.0052 236 LEU A C   
1470 O O   . LEU A 206 ? 0.1944 0.2282 0.2264 0.0016  -0.0112 -0.0058 236 LEU A O   
1471 C CB  . LEU A 206 ? 0.1615 0.1868 0.1813 0.0054  -0.0102 -0.0066 236 LEU A CB  
1472 C CG  . LEU A 206 ? 0.1926 0.2130 0.2074 0.0060  -0.0108 -0.0071 236 LEU A CG  
1473 C CD1 . LEU A 206 ? 0.1821 0.2021 0.1949 0.0078  -0.0113 -0.0077 236 LEU A CD1 
1474 C CD2 . LEU A 206 ? 0.1658 0.1830 0.1794 0.0044  -0.0127 -0.0079 236 LEU A CD2 
1475 N N   . LEU A 207 ? 0.1782 0.2126 0.2083 0.0030  -0.0061 -0.0042 237 LEU A N   
1476 C CA  . LEU A 207 ? 0.1645 0.2047 0.2010 0.0023  -0.0049 -0.0034 237 LEU A CA  
1477 C C   . LEU A 207 ? 0.2015 0.2423 0.2422 -0.0010 -0.0056 -0.0026 237 LEU A C   
1478 O O   . LEU A 207 ? 0.1766 0.2230 0.2241 -0.0021 -0.0057 -0.0021 237 LEU A O   
1479 C CB  . LEU A 207 ? 0.1862 0.2285 0.2221 0.0035  -0.0012 -0.0024 237 LEU A CB  
1480 C CG  . LEU A 207 ? 0.2229 0.2646 0.2548 0.0063  -0.0003 -0.0036 237 LEU A CG  
1481 C CD1 . LEU A 207 ? 0.1889 0.2329 0.2198 0.0071  0.0034  -0.0029 237 LEU A CD1 
1482 C CD2 . LEU A 207 ? 0.1600 0.2036 0.1948 0.0080  -0.0018 -0.0048 237 LEU A CD2 
1483 N N   . THR A 208 ? 0.1664 0.2017 0.2036 -0.0027 -0.0060 -0.0026 238 THR A N   
1484 C CA  . THR A 208 ? 0.1698 0.2040 0.2102 -0.0064 -0.0068 -0.0024 238 THR A CA  
1485 C C   . THR A 208 ? 0.2123 0.2433 0.2510 -0.0077 -0.0107 -0.0045 238 THR A C   
1486 O O   . THR A 208 ? 0.2135 0.2420 0.2534 -0.0111 -0.0118 -0.0050 238 THR A O   
1487 C CB  . THR A 208 ? 0.1731 0.2023 0.2108 -0.0075 -0.0042 -0.0008 238 THR A CB  
1488 O OG1 . THR A 208 ? 0.1745 0.1968 0.2058 -0.0064 -0.0051 -0.0016 238 THR A OG1 
1489 C CG2 . THR A 208 ? 0.1721 0.2037 0.2090 -0.0056 -0.0006 0.0013  238 THR A CG2 
1490 N N   . SER A 209 ? 0.2009 0.2315 0.2363 -0.0053 -0.0126 -0.0057 239 SER A N   
1491 C CA  . SER A 209 ? 0.1969 0.2241 0.2291 -0.0062 -0.0161 -0.0076 239 SER A CA  
1492 C C   . SER A 209 ? 0.1867 0.2199 0.2235 -0.0067 -0.0194 -0.0080 239 SER A C   
1493 O O   . SER A 209 ? 0.1990 0.2368 0.2381 -0.0040 -0.0192 -0.0073 239 SER A O   
1494 C CB  . SER A 209 ? 0.2005 0.2232 0.2257 -0.0033 -0.0160 -0.0083 239 SER A CB  
1495 O OG  . SER A 209 ? 0.2093 0.2284 0.2305 -0.0040 -0.0189 -0.0100 239 SER A OG  
1496 N N   . PRO A 210 ? 0.2070 0.2401 0.2450 -0.0100 -0.0225 -0.0092 240 PRO A N   
1497 C CA  . PRO A 210 ? 0.2189 0.2582 0.2607 -0.0101 -0.0265 -0.0094 240 PRO A CA  
1498 C C   . PRO A 210 ? 0.2250 0.2626 0.2613 -0.0067 -0.0282 -0.0098 240 PRO A C   
1499 O O   . PRO A 210 ? 0.2305 0.2738 0.2702 -0.0052 -0.0306 -0.0090 240 PRO A O   
1500 C CB  . PRO A 210 ? 0.1825 0.2205 0.2247 -0.0149 -0.0298 -0.0111 240 PRO A CB  
1501 C CG  . PRO A 210 ? 0.3164 0.3445 0.3516 -0.0161 -0.0277 -0.0124 240 PRO A CG  
1502 C CD  . PRO A 210 ? 0.1885 0.2155 0.2240 -0.0137 -0.0229 -0.0105 240 PRO A CD  
1503 N N   . LEU A 211 ? 0.2033 0.2336 0.2316 -0.0052 -0.0268 -0.0106 241 LEU A N   
1504 C CA  . LEU A 211 ? 0.2436 0.2717 0.2664 -0.0023 -0.0279 -0.0108 241 LEU A CA  
1505 C C   . LEU A 211 ? 0.2054 0.2366 0.2305 0.0014  -0.0260 -0.0093 241 LEU A C   
1506 O O   . LEU A 211 ? 0.1990 0.2292 0.2209 0.0037  -0.0270 -0.0090 241 LEU A O   
1507 C CB  . LEU A 211 ? 0.1793 0.1990 0.1937 -0.0019 -0.0264 -0.0120 241 LEU A CB  
1508 C CG  . LEU A 211 ? 0.3045 0.3189 0.3147 -0.0051 -0.0278 -0.0140 241 LEU A CG  
1509 C CD1 . LEU A 211 ? 0.2169 0.2232 0.2191 -0.0037 -0.0255 -0.0149 241 LEU A CD1 
1510 C CD2 . LEU A 211 ? 0.1909 0.2073 0.2000 -0.0068 -0.0326 -0.0152 241 LEU A CD2 
1511 N N   . SER A 212 ? 0.2235 0.2580 0.2535 0.0019  -0.0231 -0.0083 242 SER A N   
1512 C CA  . SER A 212 ? 0.2125 0.2489 0.2438 0.0052  -0.0210 -0.0074 242 SER A CA  
1513 C C   . SER A 212 ? 0.1937 0.2370 0.2318 0.0067  -0.0221 -0.0063 242 SER A C   
1514 O O   . SER A 212 ? 0.1991 0.2433 0.2383 0.0096  -0.0203 -0.0057 242 SER A O   
1515 C CB  . SER A 212 ? 0.2621 0.2981 0.2938 0.0053  -0.0171 -0.0071 242 SER A CB  
1516 O OG  . SER A 212 ? 0.2718 0.3125 0.3097 0.0036  -0.0160 -0.0064 242 SER A OG  
1517 N N   . LYS A 213 ? 0.2029 0.2508 0.2458 0.0047  -0.0252 -0.0060 243 LYS A N   
1518 C CA  . LYS A 213 ? 0.2633 0.3193 0.3143 0.0061  -0.0263 -0.0045 243 LYS A CA  
1519 C C   . LYS A 213 ? 0.2195 0.2750 0.2690 0.0102  -0.0270 -0.0035 243 LYS A C   
1520 O O   . LYS A 213 ? 0.2123 0.2637 0.2557 0.0107  -0.0294 -0.0038 243 LYS A O   
1521 C CB  . LYS A 213 ? 0.2671 0.3279 0.3224 0.0029  -0.0307 -0.0044 243 LYS A CB  
1522 C CG  . LYS A 213 ? 0.3323 0.4024 0.3964 0.0045  -0.0330 -0.0024 243 LYS A CG  
1523 C CD  . LYS A 213 ? 0.3634 0.4389 0.4319 0.0003  -0.0377 -0.0026 243 LYS A CD  
1524 C CE  . LYS A 213 ? 0.5274 0.6067 0.5960 0.0017  -0.0431 -0.0016 243 LYS A CE  
1525 N NZ  . LYS A 213 ? 0.5360 0.6245 0.6143 0.0055  -0.0431 0.0013  243 LYS A NZ  
1526 N N   . GLY A 214 ? 0.2397 0.2989 0.2944 0.0133  -0.0243 -0.0024 244 GLY A N   
1527 C CA  . GLY A 214 ? 0.2436 0.3025 0.2984 0.0175  -0.0246 -0.0012 244 GLY A CA  
1528 C C   . GLY A 214 ? 0.2262 0.2769 0.2730 0.0193  -0.0227 -0.0020 244 GLY A C   
1529 O O   . GLY A 214 ? 0.3236 0.3727 0.3694 0.0223  -0.0233 -0.0009 244 GLY A O   
1530 N N   . LEU A 215 ? 0.1713 0.2169 0.2128 0.0175  -0.0205 -0.0037 245 LEU A N   
1531 C CA  . LEU A 215 ? 0.2079 0.2464 0.2425 0.0186  -0.0190 -0.0045 245 LEU A CA  
1532 C C   . LEU A 215 ? 0.2356 0.2725 0.2704 0.0202  -0.0149 -0.0053 245 LEU A C   
1533 O O   . LEU A 215 ? 0.2221 0.2537 0.2522 0.0211  -0.0137 -0.0059 245 LEU A O   
1534 C CB  . LEU A 215 ? 0.1645 0.1985 0.1929 0.0158  -0.0194 -0.0057 245 LEU A CB  
1535 C CG  . LEU A 215 ? 0.2880 0.3212 0.3135 0.0143  -0.0232 -0.0055 245 LEU A CG  
1536 C CD1 . LEU A 215 ? 0.2107 0.2393 0.2307 0.0119  -0.0228 -0.0069 245 LEU A CD1 
1537 C CD2 . LEU A 215 ? 0.2795 0.3102 0.3016 0.0167  -0.0248 -0.0044 245 LEU A CD2 
1538 N N   . PHE A 216 ? 0.1640 0.2054 0.2039 0.0204  -0.0127 -0.0053 246 PHE A N   
1539 C CA  . PHE A 216 ? 0.1941 0.2340 0.2336 0.0221  -0.0087 -0.0064 246 PHE A CA  
1540 C C   . PHE A 216 ? 0.2196 0.2658 0.2659 0.0228  -0.0065 -0.0058 246 PHE A C   
1541 O O   . PHE A 216 ? 0.2262 0.2772 0.2763 0.0206  -0.0074 -0.0050 246 PHE A O   
1542 C CB  . PHE A 216 ? 0.1629 0.1984 0.1961 0.0200  -0.0071 -0.0080 246 PHE A CB  
1543 C CG  . PHE A 216 ? 0.1725 0.2097 0.2053 0.0170  -0.0079 -0.0078 246 PHE A CG  
1544 C CD1 . PHE A 216 ? 0.2053 0.2461 0.2408 0.0161  -0.0056 -0.0076 246 PHE A CD1 
1545 C CD2 . PHE A 216 ? 0.1616 0.1961 0.1909 0.0152  -0.0104 -0.0077 246 PHE A CD2 
1546 C CE1 . PHE A 216 ? 0.1974 0.2389 0.2325 0.0133  -0.0061 -0.0071 246 PHE A CE1 
1547 C CE2 . PHE A 216 ? 0.1754 0.2103 0.2043 0.0126  -0.0107 -0.0075 246 PHE A CE2 
1548 C CZ  . PHE A 216 ? 0.2205 0.2588 0.2524 0.0116  -0.0087 -0.0071 246 PHE A CZ  
1549 N N   . ARG A 217 ? 0.1924 0.2384 0.2404 0.0258  -0.0032 -0.0062 247 ARG A N   
1550 C CA  . ARG A 217 ? 0.2186 0.2703 0.2726 0.0269  0.0000  -0.0058 247 ARG A CA  
1551 C C   . ARG A 217 ? 0.2074 0.2573 0.2570 0.0256  0.0037  -0.0075 247 ARG A C   
1552 O O   . ARG A 217 ? 0.2140 0.2687 0.2676 0.0256  0.0065  -0.0070 247 ARG A O   
1553 C CB  . ARG A 217 ? 0.2105 0.2631 0.2688 0.0315  0.0021  -0.0053 247 ARG A CB  
1554 C CG  . ARG A 217 ? 0.2647 0.3098 0.3169 0.0333  0.0057  -0.0077 247 ARG A CG  
1555 C CD  . ARG A 217 ? 0.3131 0.3599 0.3700 0.0375  0.0101  -0.0077 247 ARG A CD  
1556 N NE  . ARG A 217 ? 0.3216 0.3600 0.3721 0.0392  0.0134  -0.0104 247 ARG A NE  
1557 C CZ  . ARG A 217 ? 0.3426 0.3792 0.3954 0.0434  0.0172  -0.0109 247 ARG A CZ  
1558 N NH1 . ARG A 217 ? 0.3862 0.4297 0.4483 0.0468  0.0185  -0.0085 247 ARG A NH1 
1559 N NH2 . ARG A 217 ? 0.2536 0.2814 0.2996 0.0442  0.0200  -0.0139 247 ARG A NH2 
1560 N N   . GLY A 218 ? 0.2133 0.2567 0.2547 0.0244  0.0037  -0.0093 248 GLY A N   
1561 C CA  . GLY A 218 ? 0.2087 0.2504 0.2451 0.0233  0.0066  -0.0108 248 GLY A CA  
1562 C C   . GLY A 218 ? 0.2835 0.3217 0.3136 0.0204  0.0045  -0.0113 248 GLY A C   
1563 O O   . GLY A 218 ? 0.2269 0.2620 0.2552 0.0198  0.0016  -0.0112 248 GLY A O   
1564 N N   . ALA A 219 ? 0.1683 0.2071 0.1952 0.0188  0.0061  -0.0115 249 ALA A N   
1565 C CA  . ALA A 219 ? 0.1834 0.2196 0.2049 0.0164  0.0044  -0.0115 249 ALA A CA  
1566 C C   . ALA A 219 ? 0.1952 0.2306 0.2110 0.0160  0.0069  -0.0126 249 ALA A C   
1567 O O   . ALA A 219 ? 0.1900 0.2283 0.2065 0.0163  0.0098  -0.0121 249 ALA A O   
1568 C CB  . ALA A 219 ? 0.1641 0.2028 0.1882 0.0144  0.0028  -0.0094 249 ALA A CB  
1569 N N   . ILE A 220 ? 0.1720 0.2037 0.1821 0.0152  0.0057  -0.0141 250 ILE A N   
1570 C CA  . ILE A 220 ? 0.1760 0.2071 0.1797 0.0143  0.0069  -0.0152 250 ILE A CA  
1571 C C   . ILE A 220 ? 0.1737 0.2052 0.1751 0.0124  0.0045  -0.0135 250 ILE A C   
1572 O O   . ILE A 220 ? 0.2269 0.2565 0.2284 0.0118  0.0019  -0.0135 250 ILE A O   
1573 C CB  . ILE A 220 ? 0.1806 0.2076 0.1797 0.0147  0.0073  -0.0184 250 ILE A CB  
1574 C CG1 . ILE A 220 ? 0.1834 0.2090 0.1853 0.0172  0.0099  -0.0198 250 ILE A CG1 
1575 C CG2 . ILE A 220 ? 0.1882 0.2150 0.1800 0.0134  0.0082  -0.0198 250 ILE A CG2 
1576 C CD1 . ILE A 220 ? 0.1893 0.2093 0.1867 0.0175  0.0108  -0.0233 250 ILE A CD1 
1577 N N   . LEU A 221 ? 0.2108 0.2446 0.2102 0.0118  0.0056  -0.0118 251 LEU A N   
1578 C CA  . LEU A 221 ? 0.1837 0.2180 0.1815 0.0106  0.0038  -0.0096 251 LEU A CA  
1579 C C   . LEU A 221 ? 0.2277 0.2626 0.2186 0.0100  0.0039  -0.0100 251 LEU A C   
1580 O O   . LEU A 221 ? 0.2059 0.2424 0.1939 0.0102  0.0063  -0.0095 251 LEU A O   
1581 C CB  . LEU A 221 ? 0.1773 0.2135 0.1786 0.0102  0.0048  -0.0066 251 LEU A CB  
1582 C CG  . LEU A 221 ? 0.1977 0.2337 0.2054 0.0100  0.0037  -0.0060 251 LEU A CG  
1583 C CD1 . LEU A 221 ? 0.2014 0.2392 0.2135 0.0110  0.0052  -0.0071 251 LEU A CD1 
1584 C CD2 . LEU A 221 ? 0.1681 0.2046 0.1778 0.0088  0.0040  -0.0032 251 LEU A CD2 
1585 N N   . GLU A 222 ? 0.2020 0.2359 0.1904 0.0092  0.0014  -0.0109 252 GLU A N   
1586 C CA  . GLU A 222 ? 0.2456 0.2807 0.2276 0.0083  0.0005  -0.0114 252 GLU A CA  
1587 C C   . GLU A 222 ? 0.1971 0.2345 0.1791 0.0081  -0.0013 -0.0078 252 GLU A C   
1588 O O   . GLU A 222 ? 0.1814 0.2186 0.1662 0.0079  -0.0035 -0.0070 252 GLU A O   
1589 C CB  . GLU A 222 ? 0.1853 0.2185 0.1652 0.0073  -0.0013 -0.0147 252 GLU A CB  
1590 C CG  . GLU A 222 ? 0.2024 0.2322 0.1817 0.0078  0.0008  -0.0183 252 GLU A CG  
1591 C CD  . GLU A 222 ? 0.2828 0.3094 0.2615 0.0065  -0.0008 -0.0213 252 GLU A CD  
1592 O OE1 . GLU A 222 ? 0.1972 0.2250 0.1735 0.0046  -0.0034 -0.0215 252 GLU A OE1 
1593 O OE2 . GLU A 222 ? 0.2172 0.2402 0.1983 0.0075  0.0006  -0.0230 252 GLU A OE2 
1594 N N   . SER A 223 ? 0.2232 0.2625 0.2019 0.0084  -0.0001 -0.0054 253 SER A N   
1595 C CA  . SER A 223 ? 0.1860 0.2271 0.1645 0.0087  -0.0013 -0.0014 253 SER A CA  
1596 C C   . SER A 223 ? 0.2092 0.2487 0.1939 0.0092  -0.0016 0.0007  253 SER A C   
1597 O O   . SER A 223 ? 0.2026 0.2424 0.1886 0.0095  -0.0037 0.0020  253 SER A O   
1598 C CB  . SER A 223 ? 0.1883 0.2320 0.1632 0.0081  -0.0045 -0.0015 253 SER A CB  
1599 O OG  . SER A 223 ? 0.2195 0.2643 0.1875 0.0072  -0.0045 -0.0038 253 SER A OG  
1600 N N   . PRO A 224 ? 0.2178 0.2556 0.2063 0.0093  0.0005  0.0010  254 PRO A N   
1601 C CA  . PRO A 224 ? 0.1751 0.2107 0.1684 0.0094  0.0001  0.0027  254 PRO A CA  
1602 C C   . PRO A 224 ? 0.1990 0.2343 0.1916 0.0099  0.0009  0.0068  254 PRO A C   
1603 O O   . PRO A 224 ? 0.2256 0.2623 0.2154 0.0099  0.0027  0.0087  254 PRO A O   
1604 C CB  . PRO A 224 ? 0.1845 0.2192 0.1819 0.0089  0.0017  0.0014  254 PRO A CB  
1605 C CG  . PRO A 224 ? 0.1779 0.2148 0.1729 0.0090  0.0043  0.0012  254 PRO A CG  
1606 C CD  . PRO A 224 ? 0.1802 0.2184 0.1691 0.0092  0.0034  -0.0001 254 PRO A CD  
1607 N N   . GLY A 225 ? 0.2063 0.2393 0.2014 0.0104  -0.0001 0.0082  255 GLY A N   
1608 C CA  . GLY A 225 ? 0.1793 0.2105 0.1746 0.0110  0.0010  0.0121  255 GLY A CA  
1609 C C   . GLY A 225 ? 0.2293 0.2566 0.2285 0.0099  0.0026  0.0122  255 GLY A C   
1610 O O   . GLY A 225 ? 0.1987 0.2228 0.2005 0.0098  0.0018  0.0111  255 GLY A O   
1611 N N   . LEU A 226 ? 0.1817 0.2093 0.1813 0.0089  0.0050  0.0136  256 LEU A N   
1612 C CA  . LEU A 226 ? 0.1929 0.2179 0.1969 0.0070  0.0063  0.0133  256 LEU A CA  
1613 C C   . LEU A 226 ? 0.2121 0.2347 0.2162 0.0065  0.0089  0.0172  256 LEU A C   
1614 O O   . LEU A 226 ? 0.2310 0.2546 0.2313 0.0077  0.0099  0.0204  256 LEU A O   
1615 C CB  . LEU A 226 ? 0.1794 0.2078 0.1858 0.0059  0.0070  0.0108  256 LEU A CB  
1616 C CG  . LEU A 226 ? 0.1988 0.2287 0.2054 0.0065  0.0048  0.0071  256 LEU A CG  
1617 C CD1 . LEU A 226 ? 0.1740 0.2076 0.1821 0.0063  0.0061  0.0052  256 LEU A CD1 
1618 C CD2 . LEU A 226 ? 0.1792 0.2060 0.1890 0.0059  0.0029  0.0055  256 LEU A CD2 
1619 N N   . THR A 227 ? 0.1880 0.2072 0.1964 0.0044  0.0097  0.0171  257 THR A N   
1620 C CA  . THR A 227 ? 0.2372 0.2523 0.2464 0.0032  0.0122  0.0206  257 THR A CA  
1621 C C   . THR A 227 ? 0.2166 0.2273 0.2227 0.0055  0.0122  0.0236  257 THR A C   
1622 O O   . THR A 227 ? 0.2542 0.2621 0.2594 0.0057  0.0146  0.0277  257 THR A O   
1623 C CB  . THR A 227 ? 0.2429 0.2613 0.2518 0.0024  0.0153  0.0233  257 THR A CB  
1624 O OG1 . THR A 227 ? 0.2679 0.2892 0.2708 0.0049  0.0155  0.0253  257 THR A OG1 
1625 C CG2 . THR A 227 ? 0.2255 0.2489 0.2383 0.0007  0.0158  0.0205  257 THR A CG2 
1626 N N   . ARG A 228 ? 0.2622 0.2725 0.2670 0.0075  0.0098  0.0220  258 ARG A N   
1627 C CA  . ARG A 228 ? 0.2373 0.2441 0.2404 0.0101  0.0097  0.0247  258 ARG A CA  
1628 C C   . ARG A 228 ? 0.2614 0.2602 0.2667 0.0093  0.0106  0.0240  258 ARG A C   
1629 O O   . ARG A 228 ? 0.2723 0.2693 0.2800 0.0067  0.0100  0.0206  258 ARG A O   
1630 C CB  . ARG A 228 ? 0.2351 0.2456 0.2367 0.0124  0.0071  0.0232  258 ARG A CB  
1631 C CG  . ARG A 228 ? 0.2922 0.3098 0.2907 0.0132  0.0059  0.0236  258 ARG A CG  
1632 C CD  . ARG A 228 ? 0.2689 0.2895 0.2669 0.0149  0.0033  0.0222  258 ARG A CD  
1633 N NE  . ARG A 228 ? 0.2860 0.3129 0.2809 0.0151  0.0016  0.0218  258 ARG A NE  
1634 C CZ  . ARG A 228 ? 0.3089 0.3394 0.3034 0.0160  -0.0009 0.0207  258 ARG A CZ  
1635 N NH1 . ARG A 228 ? 0.2760 0.3050 0.2735 0.0171  -0.0016 0.0201  258 ARG A NH1 
1636 N NH2 . ARG A 228 ? 0.2888 0.3245 0.2800 0.0156  -0.0024 0.0199  258 ARG A NH2 
1637 N N   . PRO A 229 ? 0.2483 0.2422 0.2526 0.0116  0.0119  0.0273  259 PRO A N   
1638 C CA  . PRO A 229 ? 0.2705 0.2555 0.2758 0.0112  0.0130  0.0262  259 PRO A CA  
1639 C C   . PRO A 229 ? 0.3149 0.2996 0.3205 0.0113  0.0109  0.0217  259 PRO A C   
1640 O O   . PRO A 229 ? 0.2446 0.2339 0.2494 0.0136  0.0092  0.0211  259 PRO A O   
1641 C CB  . PRO A 229 ? 0.2383 0.2195 0.2423 0.0150  0.0147  0.0310  259 PRO A CB  
1642 C CG  . PRO A 229 ? 0.2815 0.2681 0.2838 0.0158  0.0152  0.0354  259 PRO A CG  
1643 C CD  . PRO A 229 ? 0.3108 0.3063 0.3126 0.0146  0.0128  0.0325  259 PRO A CD  
1644 N N   . LEU A 230 ? 0.2393 0.2185 0.2458 0.0084  0.0109  0.0184  260 LEU A N   
1645 C CA  . LEU A 230 ? 0.2728 0.2504 0.2786 0.0083  0.0092  0.0141  260 LEU A CA  
1646 C C   . LEU A 230 ? 0.2364 0.2036 0.2409 0.0081  0.0109  0.0131  260 LEU A C   
1647 O O   . LEU A 230 ? 0.3085 0.2698 0.3137 0.0057  0.0126  0.0138  260 LEU A O   
1648 C CB  . LEU A 230 ? 0.2016 0.1832 0.2090 0.0049  0.0069  0.0104  260 LEU A CB  
1649 C CG  . LEU A 230 ? 0.2629 0.2538 0.2715 0.0050  0.0056  0.0106  260 LEU A CG  
1650 C CD1 . LEU A 230 ? 0.2056 0.1996 0.2167 0.0018  0.0039  0.0077  260 LEU A CD1 
1651 C CD2 . LEU A 230 ? 0.1897 0.1847 0.1965 0.0080  0.0042  0.0103  260 LEU A CD2 
1652 N N   . ALA A 231 ? 0.2777 0.2422 0.2801 0.0105  0.0109  0.0115  261 ALA A N   
1653 C CA  . ALA A 231 ? 0.2501 0.2040 0.2502 0.0106  0.0128  0.0098  261 ALA A CA  
1654 C C   . ALA A 231 ? 0.2529 0.2032 0.2518 0.0061  0.0111  0.0050  261 ALA A C   
1655 O O   . ALA A 231 ? 0.2602 0.2168 0.2597 0.0044  0.0082  0.0025  261 ALA A O   
1656 C CB  . ALA A 231 ? 0.2281 0.1809 0.2263 0.0149  0.0137  0.0096  261 ALA A CB  
1657 N N   . THR A 232 ? 0.2586 0.1987 0.2560 0.0041  0.0128  0.0036  262 THR A N   
1658 C CA  . THR A 232 ? 0.2967 0.2327 0.2922 -0.0003 0.0109  -0.0013 262 THR A CA  
1659 C C   . THR A 232 ? 0.3271 0.2595 0.3175 0.0016  0.0105  -0.0048 262 THR A C   
1660 O O   . THR A 232 ? 0.2422 0.1731 0.2308 0.0062  0.0127  -0.0034 262 THR A O   
1661 C CB  . THR A 232 ? 0.3201 0.2458 0.3155 -0.0038 0.0128  -0.0019 262 THR A CB  
1662 O OG1 . THR A 232 ? 0.3239 0.2396 0.3162 -0.0002 0.0167  -0.0006 262 THR A OG1 
1663 C CG2 . THR A 232 ? 0.2905 0.2197 0.2910 -0.0062 0.0134  0.0016  262 THR A CG2 
1664 N N   . LEU A 233 ? 0.2647 0.1961 0.2527 -0.0021 0.0077  -0.0093 263 LEU A N   
1665 C CA  . LEU A 233 ? 0.2900 0.2174 0.2719 -0.0007 0.0074  -0.0129 263 LEU A CA  
1666 C C   . LEU A 233 ? 0.3298 0.2445 0.3071 0.0011  0.0114  -0.0138 263 LEU A C   
1667 O O   . LEU A 233 ? 0.3002 0.2122 0.2737 0.0050  0.0134  -0.0144 263 LEU A O   
1668 C CB  . LEU A 233 ? 0.2727 0.2011 0.2524 -0.0052 0.0033  -0.0173 263 LEU A CB  
1669 C CG  . LEU A 233 ? 0.3199 0.2430 0.2917 -0.0045 0.0028  -0.0213 263 LEU A CG  
1670 C CD1 . LEU A 233 ? 0.3006 0.2290 0.2713 0.0004  0.0037  -0.0198 263 LEU A CD1 
1671 C CD2 . LEU A 233 ? 0.3641 0.2890 0.3339 -0.0094 -0.0019 -0.0252 263 LEU A CD2 
1672 N N   . ALA A 234 ? 0.2858 0.1923 0.2636 -0.0017 0.0129  -0.0140 264 ALA A N   
1673 C CA  . ALA A 234 ? 0.2975 0.1906 0.2708 0.0000  0.0171  -0.0151 264 ALA A CA  
1674 C C   . ALA A 234 ? 0.3736 0.2669 0.3485 0.0067  0.0211  -0.0105 264 ALA A C   
1675 O O   . ALA A 234 ? 0.3814 0.2688 0.3521 0.0106  0.0240  -0.0116 264 ALA A O   
1676 C CB  . ALA A 234 ? 0.2988 0.1833 0.2734 -0.0046 0.0181  -0.0155 264 ALA A CB  
1677 N N   . ASP A 235 ? 0.3077 0.2081 0.2886 0.0083  0.0213  -0.0052 265 ASP A N   
1678 C CA  . ASP A 235 ? 0.3343 0.2361 0.3173 0.0146  0.0245  -0.0003 265 ASP A CA  
1679 C C   . ASP A 235 ? 0.2885 0.1983 0.2711 0.0184  0.0237  -0.0003 265 ASP A C   
1680 O O   . ASP A 235 ? 0.3740 0.2810 0.3559 0.0234  0.0269  0.0011  265 ASP A O   
1681 C CB  . ASP A 235 ? 0.3327 0.2412 0.3212 0.0150  0.0243  0.0053  265 ASP A CB  
1682 C CG  . ASP A 235 ? 0.3803 0.2803 0.3696 0.0118  0.0261  0.0063  265 ASP A CG  
1683 O OD1 . ASP A 235 ? 0.4012 0.2885 0.3870 0.0108  0.0285  0.0037  265 ASP A OD1 
1684 O OD2 . ASP A 235 ? 0.3932 0.2989 0.3864 0.0101  0.0252  0.0098  265 ASP A OD2 
1685 N N   . SER A 236 ? 0.2772 0.1968 0.2607 0.0162  0.0198  -0.0017 266 SER A N   
1686 C CA  . SER A 236 ? 0.3042 0.2313 0.2878 0.0193  0.0191  -0.0016 266 SER A CA  
1687 C C   . SER A 236 ? 0.3256 0.2454 0.3032 0.0206  0.0209  -0.0054 266 SER A C   
1688 O O   . SER A 236 ? 0.3017 0.2232 0.2793 0.0249  0.0231  -0.0042 266 SER A O   
1689 C CB  . SER A 236 ? 0.2632 0.2008 0.2486 0.0165  0.0147  -0.0024 266 SER A CB  
1690 O OG  . SER A 236 ? 0.2652 0.2105 0.2517 0.0194  0.0143  -0.0014 266 SER A OG  
1691 N N   . ALA A 237 ? 0.3179 0.2297 0.2902 0.0166  0.0201  -0.0101 267 ALA A N   
1692 C CA  . ALA A 237 ? 0.3291 0.2329 0.2942 0.0175  0.0219  -0.0142 267 ALA A CA  
1693 C C   . ALA A 237 ? 0.4144 0.3079 0.3777 0.0217  0.0275  -0.0134 267 ALA A C   
1694 O O   . ALA A 237 ? 0.2999 0.1903 0.2594 0.0254  0.0305  -0.0145 267 ALA A O   
1695 C CB  . ALA A 237 ? 0.3590 0.2570 0.3185 0.0118  0.0190  -0.0196 267 ALA A CB  
1696 N N   . ALA A 238 ? 0.3327 0.2205 0.2986 0.0216  0.0293  -0.0112 268 ALA A N   
1697 C CA  . ALA A 238 ? 0.3903 0.2687 0.3556 0.0265  0.0349  -0.0093 268 ALA A CA  
1698 C C   . ALA A 238 ? 0.3948 0.2819 0.3653 0.0329  0.0369  -0.0044 268 ALA A C   
1699 O O   . ALA A 238 ? 0.3853 0.2678 0.3541 0.0378  0.0412  -0.0043 268 ALA A O   
1700 C CB  . ALA A 238 ? 0.3493 0.2206 0.3171 0.0251  0.0363  -0.0071 268 ALA A CB  
1701 N N   . SER A 239 ? 0.3128 0.2128 0.2897 0.0330  0.0338  -0.0003 269 SER A N   
1702 C CA  . SER A 239 ? 0.3385 0.2482 0.3206 0.0382  0.0347  0.0042  269 SER A CA  
1703 C C   . SER A 239 ? 0.4211 0.3338 0.4008 0.0398  0.0354  0.0017  269 SER A C   
1704 O O   . SER A 239 ? 0.4289 0.3422 0.4103 0.0450  0.0390  0.0037  269 SER A O   
1705 C CB  . SER A 239 ? 0.3161 0.2387 0.3040 0.0367  0.0306  0.0078  269 SER A CB  
1706 O OG  . SER A 239 ? 0.4937 0.4269 0.4861 0.0404  0.0303  0.0109  269 SER A OG  
1707 N N   . GLY A 240 ? 0.3794 0.2939 0.3550 0.0354  0.0320  -0.0025 270 GLY A N   
1708 C CA  . GLY A 240 ? 0.3789 0.2957 0.3513 0.0366  0.0327  -0.0048 270 GLY A CA  
1709 C C   . GLY A 240 ? 0.3832 0.2884 0.3493 0.0395  0.0378  -0.0074 270 GLY A C   
1710 O O   . GLY A 240 ? 0.3795 0.2869 0.3457 0.0435  0.0409  -0.0067 270 GLY A O   
1711 N N   . GLU A 241 ? 0.3545 0.2471 0.3151 0.0374  0.0390  -0.0107 271 GLU A N   
1712 C CA  . GLU A 241 ? 0.3899 0.2698 0.3437 0.0403  0.0444  -0.0137 271 GLU A CA  
1713 C C   . GLU A 241 ? 0.4693 0.3483 0.4285 0.0472  0.0499  -0.0091 271 GLU A C   
1714 O O   . GLU A 241 ? 0.4080 0.2821 0.3641 0.0515  0.0549  -0.0100 271 GLU A O   
1715 C CB  . GLU A 241 ? 0.3725 0.2386 0.3196 0.0360  0.0443  -0.0183 271 GLU A CB  
1716 C CG  . GLU A 241 ? 0.5218 0.3731 0.4605 0.0385  0.0499  -0.0222 271 GLU A CG  
1717 C CD  . GLU A 241 ? 0.6411 0.4797 0.5708 0.0327  0.0484  -0.0285 271 GLU A CD  
1718 O OE1 . GLU A 241 ? 0.7223 0.5582 0.6546 0.0287  0.0460  -0.0283 271 GLU A OE1 
1719 O OE2 . GLU A 241 ? 0.8181 0.6496 0.7379 0.0319  0.0496  -0.0338 271 GLU A OE2 
1720 N N   . ARG A 242 ? 0.4079 0.2918 0.3751 0.0485  0.0491  -0.0038 272 ARG A N   
1721 C CA  . ARG A 242 ? 0.4505 0.3359 0.4239 0.0555  0.0535  0.0015  272 ARG A CA  
1722 C C   . ARG A 242 ? 0.4525 0.3508 0.4312 0.0591  0.0539  0.0043  272 ARG A C   
1723 O O   . ARG A 242 ? 0.4431 0.3411 0.4250 0.0652  0.0588  0.0070  272 ARG A O   
1724 C CB  . ARG A 242 ? 0.4211 0.3098 0.4013 0.0558  0.0519  0.0068  272 ARG A CB  
1725 C CG  . ARG A 242 ? 0.4959 0.3701 0.4725 0.0543  0.0539  0.0057  272 ARG A CG  
1726 C CD  . ARG A 242 ? 0.5128 0.3897 0.4962 0.0566  0.0540  0.0123  272 ARG A CD  
1727 N NE  . ARG A 242 ? 0.4804 0.3700 0.4681 0.0530  0.0483  0.0147  272 ARG A NE  
1728 C CZ  . ARG A 242 ? 0.4649 0.3526 0.4507 0.0470  0.0451  0.0129  272 ARG A CZ  
1729 N NH1 . ARG A 242 ? 0.4065 0.2807 0.3867 0.0433  0.0464  0.0087  272 ARG A NH1 
1730 N NH2 . ARG A 242 ? 0.4510 0.3505 0.4406 0.0444  0.0406  0.0153  272 ARG A NH2 
1731 N N   . LEU A 243 ? 0.3850 0.2946 0.3653 0.0555  0.0490  0.0040  273 LEU A N   
1732 C CA  . LEU A 243 ? 0.3884 0.3095 0.3735 0.0582  0.0494  0.0062  273 LEU A CA  
1733 C C   . LEU A 243 ? 0.4133 0.3281 0.3925 0.0607  0.0543  0.0029  273 LEU A C   
1734 O O   . LEU A 243 ? 0.4089 0.3275 0.3926 0.0659  0.0586  0.0057  273 LEU A O   
1735 C CB  . LEU A 243 ? 0.3296 0.2617 0.3161 0.0534  0.0435  0.0057  273 LEU A CB  
1736 C CG  . LEU A 243 ? 0.3646 0.3086 0.3563 0.0552  0.0435  0.0079  273 LEU A CG  
1737 C CD1 . LEU A 243 ? 0.3390 0.2907 0.3403 0.0604  0.0455  0.0138  273 LEU A CD1 
1738 C CD2 . LEU A 243 ? 0.2593 0.2126 0.2523 0.0504  0.0377  0.0073  273 LEU A CD2 
1739 N N   . ASP A 244 ? 0.3332 0.2452 0.3199 0.0761  0.0531  0.0528  274 ASP A N   
1740 C CA  . ASP A 244 ? 0.3412 0.2418 0.3237 0.0764  0.0590  0.0504  274 ASP A CA  
1741 C C   . ASP A 244 ? 0.3699 0.2543 0.3398 0.0687  0.0603  0.0446  274 ASP A C   
1742 O O   . ASP A 244 ? 0.3523 0.2412 0.3210 0.0619  0.0543  0.0402  274 ASP A O   
1743 C CB  . ASP A 244 ? 0.3595 0.2726 0.3500 0.0758  0.0562  0.0485  274 ASP A CB  
1744 C CG  . ASP A 244 ? 0.4237 0.3261 0.4112 0.0778  0.0632  0.0473  274 ASP A CG  
1745 O OD1 . ASP A 244 ? 0.3703 0.2540 0.3470 0.0766  0.0692  0.0457  274 ASP A OD1 
1746 O OD2 . ASP A 244 ? 0.3902 0.3027 0.3855 0.0800  0.0631  0.0476  274 ASP A OD2 
1747 N N   . ALA A 245 ? 0.3609 0.2266 0.3212 0.0698  0.0684  0.0447  275 ALA A N   
1748 C CA  . ALA A 245 ? 0.4146 0.2649 0.3622 0.0619  0.0700  0.0390  275 ALA A CA  
1749 C C   . ALA A 245 ? 0.4241 0.2736 0.3693 0.0568  0.0685  0.0336  275 ALA A C   
1750 O O   . ALA A 245 ? 0.4210 0.2637 0.3576 0.0491  0.0668  0.0284  275 ALA A O   
1751 C CB  . ALA A 245 ? 0.5100 0.3394 0.4469 0.0640  0.0799  0.0404  275 ALA A CB  
1752 N N   . ASP A 246 ? 0.4301 0.2869 0.3825 0.0608  0.0690  0.0347  276 ASP A N   
1753 C CA  . ASP A 246 ? 0.3605 0.2156 0.3101 0.0568  0.0682  0.0301  276 ASP A CA  
1754 C C   . ASP A 246 ? 0.3719 0.2442 0.3292 0.0538  0.0591  0.0283  276 ASP A C   
1755 O O   . ASP A 246 ? 0.3710 0.2572 0.3389 0.0578  0.0569  0.0309  276 ASP A O   
1756 C CB  . ASP A 246 ? 0.4011 0.2530 0.3536 0.0625  0.0749  0.0322  276 ASP A CB  
1757 C CG  . ASP A 246 ? 0.3916 0.2390 0.3394 0.0583  0.0753  0.0275  276 ASP A CG  
1758 O OD1 . ASP A 246 ? 0.5320 0.3790 0.4741 0.0513  0.0701  0.0229  276 ASP A OD1 
1759 O OD2 . ASP A 246 ? 0.6219 0.4664 0.5716 0.0622  0.0810  0.0285  276 ASP A OD2 
1760 N N   . LEU A 247 ? 0.3279 0.1992 0.2794 0.0467  0.0541  0.0238  277 LEU A N   
1761 C CA  . LEU A 247 ? 0.3412 0.2271 0.2988 0.0440  0.0460  0.0221  277 LEU A CA  
1762 C C   . LEU A 247 ? 0.3297 0.2203 0.2907 0.0450  0.0458  0.0210  277 LEU A C   
1763 O O   . LEU A 247 ? 0.2707 0.1752 0.2402 0.0458  0.0413  0.0218  277 LEU A O   
1764 C CB  . LEU A 247 ? 0.3341 0.2173 0.2845 0.0368  0.0415  0.0176  277 LEU A CB  
1765 C CG  . LEU A 247 ? 0.3727 0.2692 0.3280 0.0341  0.0336  0.0156  277 LEU A CG  
1766 C CD1 . LEU A 247 ? 0.2622 0.1730 0.2282 0.0371  0.0301  0.0190  277 LEU A CD1 
1767 C CD2 . LEU A 247 ? 0.2807 0.1747 0.2291 0.0276  0.0296  0.0116  277 LEU A CD2 
1768 N N   . SER A 248 ? 0.3366 0.2149 0.2904 0.0444  0.0510  0.0192  278 SER A N   
1769 C CA  . SER A 248 ? 0.3935 0.2745 0.3493 0.0450  0.0516  0.0180  278 SER A CA  
1770 C C   . SER A 248 ? 0.3135 0.2063 0.2815 0.0511  0.0532  0.0220  278 SER A C   
1771 O O   . SER A 248 ? 0.3063 0.2100 0.2804 0.0507  0.0500  0.0214  278 SER A O   
1772 C CB  . SER A 248 ? 0.4146 0.2790 0.3600 0.0437  0.0581  0.0156  278 SER A CB  
1773 O OG  . SER A 248 ? 0.6953 0.5512 0.6295 0.0372  0.0557  0.0114  278 SER A OG  
1774 N N   . ARG A 249 ? 0.2964 0.1875 0.2678 0.0565  0.0582  0.0261  279 ARG A N   
1775 C CA  . ARG A 249 ? 0.3260 0.2305 0.3097 0.0626  0.0593  0.0303  279 ARG A CA  
1776 C C   . ARG A 249 ? 0.2692 0.1914 0.2619 0.0620  0.0519  0.0317  279 ARG A C   
1777 O O   . ARG A 249 ? 0.2833 0.2193 0.2850 0.0633  0.0501  0.0325  279 ARG A O   
1778 C CB  . ARG A 249 ? 0.3139 0.2128 0.2989 0.0693  0.0660  0.0350  279 ARG A CB  
1779 C CG  . ARG A 249 ? 0.3425 0.2559 0.3406 0.0763  0.0677  0.0398  279 ARG A CG  
1780 C CD  . ARG A 249 ? 0.3655 0.2699 0.3631 0.0836  0.0760  0.0442  279 ARG A CD  
1781 N NE  . ARG A 249 ? 0.3977 0.2889 0.3863 0.0832  0.0774  0.0451  279 ARG A NE  
1782 C CZ  . ARG A 249 ? 0.5379 0.4153 0.5216 0.0881  0.0854  0.0480  279 ARG A CZ  
1783 N NH1 . ARG A 249 ? 0.5062 0.3813 0.4935 0.0945  0.0928  0.0506  279 ARG A NH1 
1784 N NH2 . ARG A 249 ? 0.4720 0.3371 0.4466 0.0865  0.0865  0.0482  279 ARG A NH2 
1785 N N   . LEU A 250 ? 0.2670 0.1891 0.2569 0.0595  0.0476  0.0315  280 LEU A N   
1786 C CA  . LEU A 250 ? 0.2544 0.1920 0.2514 0.0580  0.0406  0.0322  280 LEU A CA  
1787 C C   . LEU A 250 ? 0.2459 0.1898 0.2439 0.0536  0.0364  0.0283  280 LEU A C   
1788 O O   . LEU A 250 ? 0.2366 0.1948 0.2429 0.0538  0.0333  0.0292  280 LEU A O   
1789 C CB  . LEU A 250 ? 0.2548 0.1889 0.2471 0.0552  0.0374  0.0319  280 LEU A CB  
1790 C CG  . LEU A 250 ? 0.3403 0.2722 0.3333 0.0596  0.0401  0.0365  280 LEU A CG  
1791 C CD1 . LEU A 250 ? 0.2854 0.2112 0.2716 0.0554  0.0377  0.0350  280 LEU A CD1 
1792 C CD2 . LEU A 250 ? 0.2677 0.2166 0.2720 0.0642  0.0377  0.0412  280 LEU A CD2 
1793 N N   . ARG A 251 ? 0.2499 0.1831 0.2389 0.0494  0.0364  0.0241  281 ARG A N   
1794 C CA  . ARG A 251 ? 0.2641 0.2014 0.2526 0.0457  0.0328  0.0207  281 ARG A CA  
1795 C C   . ARG A 251 ? 0.2743 0.2149 0.2668 0.0474  0.0361  0.0207  281 ARG A C   
1796 O O   . ARG A 251 ? 0.2941 0.2412 0.2885 0.0451  0.0335  0.0188  281 ARG A O   
1797 C CB  . ARG A 251 ? 0.2491 0.1746 0.2265 0.0412  0.0316  0.0167  281 ARG A CB  
1798 C CG  . ARG A 251 ? 0.2451 0.1728 0.2204 0.0378  0.0260  0.0154  281 ARG A CG  
1799 C CD  . ARG A 251 ? 0.2575 0.1790 0.2242 0.0335  0.0233  0.0114  281 ARG A CD  
1800 N NE  . ARG A 251 ? 0.2418 0.1690 0.2087 0.0306  0.0175  0.0101  281 ARG A NE  
1801 C CZ  . ARG A 251 ? 0.2461 0.1683 0.2073 0.0276  0.0161  0.0085  281 ARG A CZ  
1802 N NH1 . ARG A 251 ? 0.2570 0.1675 0.2107 0.0266  0.0201  0.0077  281 ARG A NH1 
1803 N NH2 . ARG A 251 ? 0.2764 0.2056 0.2393 0.0253  0.0109  0.0075  281 ARG A NH2 
1804 N N   . SER A 252 ? 0.2953 0.2313 0.2889 0.0514  0.0423  0.0227  282 SER A N   
1805 C CA  . SER A 252 ? 0.2692 0.2094 0.2676 0.0531  0.0461  0.0226  282 SER A CA  
1806 C C   . SER A 252 ? 0.2676 0.2247 0.2790 0.0570  0.0460  0.0265  282 SER A C   
1807 O O   . SER A 252 ? 0.3081 0.2707 0.3252 0.0589  0.0496  0.0269  282 SER A O   
1808 C CB  . SER A 252 ? 0.2728 0.1988 0.2652 0.0551  0.0535  0.0223  282 SER A CB  
1809 O OG  . SER A 252 ? 0.4310 0.3535 0.4251 0.0600  0.0575  0.0260  282 SER A OG  
1810 N N   . THR A 253 ? 0.2475 0.2138 0.2637 0.0579  0.0418  0.0291  283 THR A N   
1811 C CA  . THR A 253 ? 0.2317 0.2154 0.2598 0.0613  0.0407  0.0330  283 THR A CA  
1812 C C   . THR A 253 ? 0.2364 0.2334 0.2689 0.0567  0.0356  0.0309  283 THR A C   
1813 O O   . THR A 253 ? 0.2173 0.2121 0.2451 0.0524  0.0310  0.0284  283 THR A O   
1814 C CB  . THR A 253 ? 0.2326 0.2184 0.2625 0.0649  0.0393  0.0373  283 THR A CB  
1815 O OG1 . THR A 253 ? 0.2499 0.2210 0.2741 0.0687  0.0450  0.0390  283 THR A OG1 
1816 C CG2 . THR A 253 ? 0.2274 0.2320 0.2694 0.0690  0.0382  0.0419  283 THR A CG2 
1817 N N   . ASP A 254 ? 0.2335 0.2440 0.2749 0.0576  0.0367  0.0317  284 ASP A N   
1818 C CA  . ASP A 254 ? 0.2090 0.2323 0.2545 0.0528  0.0328  0.0296  284 ASP A CA  
1819 C C   . ASP A 254 ? 0.2027 0.2339 0.2499 0.0515  0.0268  0.0311  284 ASP A C   
1820 O O   . ASP A 254 ? 0.2034 0.2390 0.2542 0.0556  0.0261  0.0354  284 ASP A O   
1821 C CB  . ASP A 254 ? 0.2404 0.2793 0.2964 0.0541  0.0352  0.0309  284 ASP A CB  
1822 C CG  . ASP A 254 ? 0.2400 0.2960 0.3021 0.0497  0.0307  0.0302  284 ASP A CG  
1823 O OD1 . ASP A 254 ? 0.2396 0.2937 0.2976 0.0439  0.0297  0.0258  284 ASP A OD1 
1824 O OD2 . ASP A 254 ? 0.2867 0.3576 0.3570 0.0521  0.0284  0.0340  284 ASP A OD2 
1825 N N   . PRO A 255 ? 0.2243 0.2566 0.2683 0.0459  0.0229  0.0278  285 PRO A N   
1826 C CA  . PRO A 255 ? 0.1926 0.2300 0.2369 0.0444  0.0177  0.0288  285 PRO A CA  
1827 C C   . PRO A 255 ? 0.2618 0.3172 0.3156 0.0458  0.0157  0.0325  285 PRO A C   
1828 O O   . PRO A 255 ? 0.2017 0.2594 0.2560 0.0475  0.0130  0.0355  285 PRO A O   
1829 C CB  . PRO A 255 ? 0.2246 0.2595 0.2639 0.0384  0.0152  0.0242  285 PRO A CB  
1830 C CG  . PRO A 255 ? 0.1910 0.2245 0.2299 0.0367  0.0188  0.0215  285 PRO A CG  
1831 C CD  . PRO A 255 ? 0.2163 0.2428 0.2550 0.0412  0.0236  0.0230  285 PRO A CD  
1832 N N   . ALA A 256 ? 0.2317 0.3002 0.2925 0.0448  0.0167  0.0324  286 ALA A N   
1833 C CA  . ALA A 256 ? 0.2169 0.3043 0.2869 0.0460  0.0144  0.0362  286 ALA A CA  
1834 C C   . ALA A 256 ? 0.1988 0.2876 0.2729 0.0539  0.0160  0.0420  286 ALA A C   
1835 O O   . ALA A 256 ? 0.1854 0.2828 0.2626 0.0562  0.0130  0.0461  286 ALA A O   
1836 C CB  . ALA A 256 ? 0.1794 0.2813 0.2564 0.0430  0.0157  0.0345  286 ALA A CB  
1837 N N   . THR A 257 ? 0.1928 0.2720 0.2659 0.0583  0.0213  0.0426  287 THR A N   
1838 C CA  . THR A 257 ? 0.2116 0.2895 0.2876 0.0664  0.0241  0.0482  287 THR A CA  
1839 C C   . THR A 257 ? 0.2092 0.2760 0.2782 0.0680  0.0223  0.0502  287 THR A C   
1840 O O   . THR A 257 ? 0.2042 0.2771 0.2765 0.0728  0.0213  0.0555  287 THR A O   
1841 C CB  . THR A 257 ? 0.2063 0.2726 0.2805 0.0698  0.0308  0.0475  287 THR A CB  
1842 O OG1 . THR A 257 ? 0.2036 0.2797 0.2838 0.0675  0.0328  0.0451  287 THR A OG1 
1843 C CG2 . THR A 257 ? 0.2152 0.2802 0.2927 0.0787  0.0348  0.0535  287 THR A CG2 
1844 N N   . LEU A 258 ? 0.2034 0.2542 0.2626 0.0641  0.0220  0.0461  288 LEU A N   
1845 C CA  . LEU A 258 ? 0.2599 0.2999 0.3122 0.0646  0.0207  0.0472  288 LEU A CA  
1846 C C   . LEU A 258 ? 0.2007 0.2517 0.2551 0.0622  0.0149  0.0486  288 LEU A C   
1847 O O   . LEU A 258 ? 0.2215 0.2707 0.2744 0.0651  0.0142  0.0522  288 LEU A O   
1848 C CB  . LEU A 258 ? 0.2089 0.2320 0.2511 0.0602  0.0212  0.0421  288 LEU A CB  
1849 C CG  . LEU A 258 ? 0.2551 0.2649 0.2891 0.0599  0.0209  0.0423  288 LEU A CG  
1850 C CD1 . LEU A 258 ? 0.3094 0.3101 0.3416 0.0662  0.0264  0.0464  288 LEU A CD1 
1851 C CD2 . LEU A 258 ? 0.2735 0.2707 0.2989 0.0548  0.0205  0.0369  288 LEU A CD2 
1852 N N   . MET A 259 ? 0.2307 0.2923 0.2880 0.0566  0.0113  0.0455  289 MET A N   
1853 C CA  . MET A 259 ? 0.2350 0.3075 0.2941 0.0537  0.0061  0.0464  289 MET A CA  
1854 C C   . MET A 259 ? 0.2498 0.3367 0.3162 0.0587  0.0053  0.0526  289 MET A C   
1855 O O   . MET A 259 ? 0.2090 0.2976 0.2740 0.0598  0.0027  0.0556  289 MET A O   
1856 C CB  . MET A 259 ? 0.2844 0.3653 0.3451 0.0469  0.0037  0.0420  289 MET A CB  
1857 C CG  . MET A 259 ? 0.4141 0.4832 0.4670 0.0417  0.0026  0.0367  289 MET A CG  
1858 S SD  . MET A 259 ? 0.3926 0.4628 0.4422 0.0380  -0.0022 0.0365  289 MET A SD  
1859 C CE  . MET A 259 ? 0.1704 0.2617 0.2276 0.0358  -0.0052 0.0384  289 MET A CE  
1860 N N   . ALA A 260 ? 0.2081 0.3058 0.2823 0.0619  0.0074  0.0545  290 ALA A N   
1861 C CA  . ALA A 260 ? 0.2416 0.3548 0.3236 0.0675  0.0065  0.0608  290 ALA A CA  
1862 C C   . ALA A 260 ? 0.2875 0.3901 0.3664 0.0753  0.0092  0.0662  290 ALA A C   
1863 O O   . ALA A 260 ? 0.3576 0.4671 0.4378 0.0788  0.0069  0.0713  290 ALA A O   
1864 C CB  . ALA A 260 ? 0.1891 0.3160 0.2807 0.0694  0.0088  0.0614  290 ALA A CB  
1865 N N   . ARG A 261 ? 0.2616 0.3467 0.3353 0.0780  0.0145  0.0650  291 ARG A N   
1866 C CA  . ARG A 261 ? 0.3442 0.4164 0.4134 0.0849  0.0183  0.0696  291 ARG A CA  
1867 C C   . ARG A 261 ? 0.4098 0.4747 0.4715 0.0827  0.0153  0.0701  291 ARG A C   
1868 O O   . ARG A 261 ? 0.4407 0.5058 0.5019 0.0881  0.0156  0.0757  291 ARG A O   
1869 C CB  . ARG A 261 ? 0.3777 0.4309 0.4409 0.0859  0.0245  0.0668  291 ARG A CB  
1870 C CG  . ARG A 261 ? 0.4721 0.5153 0.5338 0.0947  0.0308  0.0720  291 ARG A CG  
1871 C CD  . ARG A 261 ? 0.5811 0.6037 0.6348 0.0940  0.0370  0.0683  291 ARG A CD  
1872 N NE  . ARG A 261 ? 0.6035 0.6301 0.6619 0.0931  0.0394  0.0653  291 ARG A NE  
1873 C CZ  . ARG A 261 ? 0.6640 0.6752 0.7160 0.0914  0.0441  0.0614  291 ARG A CZ  
1874 N NH1 . ARG A 261 ? 0.7032 0.6944 0.7439 0.0899  0.0467  0.0596  291 ARG A NH1 
1875 N NH2 . ARG A 261 ? 0.4415 0.4574 0.4981 0.0907  0.0463  0.0591  291 ARG A NH2 
1876 N N   . ALA A 262 ? 0.3187 0.3774 0.3748 0.0749  0.0125  0.0643  292 ALA A N   
1877 C CA  . ALA A 262 ? 0.3781 0.4305 0.4275 0.0721  0.0098  0.0641  292 ALA A CA  
1878 C C   . ALA A 262 ? 0.3689 0.4377 0.4228 0.0715  0.0046  0.0674  292 ALA A C   
1879 O O   . ALA A 262 ? 0.4406 0.5064 0.4906 0.0732  0.0037  0.0707  292 ALA A O   
1880 C CB  . ALA A 262 ? 0.2747 0.3182 0.3181 0.0643  0.0081  0.0572  292 ALA A CB  
1881 N N   . ASP A 263 ? 0.4106 0.4966 0.4719 0.0687  0.0014  0.0662  293 ASP A N   
1882 C CA  . ASP A 263 ? 0.4760 0.5787 0.5412 0.0671  -0.0036 0.0689  293 ASP A CA  
1883 C C   . ASP A 263 ? 0.5172 0.6275 0.5860 0.0755  -0.0031 0.0769  293 ASP A C   
1884 O O   . ASP A 263 ? 0.5305 0.6463 0.5978 0.0758  -0.0064 0.0804  293 ASP A O   
1885 C CB  . ASP A 263 ? 0.4464 0.5655 0.5184 0.0619  -0.0062 0.0656  293 ASP A CB  
1886 C CG  . ASP A 263 ? 0.6136 0.7521 0.6901 0.0603  -0.0111 0.0686  293 ASP A CG  
1887 O OD1 . ASP A 263 ? 0.6434 0.7812 0.7153 0.0551  -0.0144 0.0668  293 ASP A OD1 
1888 O OD2 . ASP A 263 ? 0.6509 0.8058 0.7355 0.0640  -0.0116 0.0725  293 ASP A OD2 
1889 N N   . ALA A 264 ? 0.5077 0.6182 0.5811 0.0826  0.0012  0.0801  294 ALA A N   
1890 C CA  . ALA A 264 ? 0.5708 0.6886 0.6480 0.0919  0.0021  0.0884  294 ALA A CA  
1891 C C   . ALA A 264 ? 0.5597 0.6620 0.6277 0.0954  0.0037  0.0920  294 ALA A C   
1892 O O   . ALA A 264 ? 0.6773 0.7866 0.7462 0.1010  0.0023  0.0987  294 ALA A O   
1893 C CB  . ALA A 264 ? 0.4166 0.5349 0.4999 0.0992  0.0075  0.0908  294 ALA A CB  
1894 N N   . ALA A 265 ? 0.5034 0.5849 0.5621 0.0920  0.0065  0.0876  295 ALA A N   
1895 C CA  . ALA A 265 ? 0.5328 0.5978 0.5817 0.0942  0.0088  0.0900  295 ALA A CA  
1896 C C   . ALA A 265 ? 0.6442 0.7112 0.6885 0.0881  0.0037  0.0887  295 ALA A C   
1897 O O   . ALA A 265 ? 0.6032 0.6576 0.6393 0.0892  0.0054  0.0908  295 ALA A O   
1898 C CB  . ALA A 265 ? 0.5569 0.5995 0.5978 0.0925  0.0142  0.0856  295 ALA A CB  
1899 N N   . ARG A 266 ? 0.5916 0.6730 0.6403 0.0813  -0.0018 0.0852  296 ARG A N   
1900 C CA  . ARG A 266 ? 0.4996 0.5832 0.5440 0.0753  -0.0062 0.0838  296 ARG A CA  
1901 C C   . ARG A 266 ? 0.5962 0.6872 0.6400 0.0804  -0.0081 0.0913  296 ARG A C   
1902 O O   . ARG A 266 ? 0.5447 0.6476 0.5947 0.0873  -0.0082 0.0972  296 ARG A O   
1903 C CB  . ARG A 266 ? 0.4980 0.5958 0.5473 0.0674  -0.0110 0.0787  296 ARG A CB  
1904 C CG  . ARG A 266 ? 0.5250 0.6135 0.5720 0.0609  -0.0101 0.0710  296 ARG A CG  
1905 C CD  . ARG A 266 ? 0.3824 0.4836 0.4330 0.0534  -0.0142 0.0665  296 ARG A CD  
1906 N NE  . ARG A 266 ? 0.5267 0.6176 0.5737 0.0476  -0.0135 0.0596  296 ARG A NE  
1907 C CZ  . ARG A 266 ? 0.4448 0.5289 0.4862 0.0424  -0.0149 0.0562  296 ARG A CZ  
1908 N NH1 . ARG A 266 ? 0.3191 0.4048 0.3575 0.0416  -0.0169 0.0586  296 ARG A NH1 
1909 N NH2 . ARG A 266 ? 0.4362 0.5120 0.4752 0.0382  -0.0142 0.0504  296 ARG A NH2 
1910 N N   . PRO A 267 ? 0.5594 0.6438 0.5955 0.0772  -0.0096 0.0913  297 PRO A N   
1911 C CA  . PRO A 267 ? 0.6074 0.6995 0.6419 0.0811  -0.0120 0.0983  297 PRO A CA  
1912 C C   . PRO A 267 ? 0.5837 0.6986 0.6247 0.0769  -0.0184 0.0983  297 PRO A C   
1913 O O   . PRO A 267 ? 0.6188 0.7379 0.6607 0.0682  -0.0211 0.0919  297 PRO A O   
1914 C CB  . PRO A 267 ? 0.6729 0.7491 0.6965 0.0772  -0.0110 0.0967  297 PRO A CB  
1915 C CG  . PRO A 267 ? 0.6280 0.6871 0.6479 0.0731  -0.0071 0.0899  297 PRO A CG  
1916 C CD  . PRO A 267 ? 0.5770 0.6455 0.6051 0.0704  -0.0084 0.0854  297 PRO A CD  
1917 N N   . ALA A 268 ? 0.6491 0.7785 0.6940 0.0833  -0.0206 0.1057  298 ALA A N   
1918 C CA  . ALA A 268 ? 0.7045 0.8566 0.7547 0.0790  -0.0269 0.1061  298 ALA A CA  
1919 C C   . ALA A 268 ? 0.7486 0.8994 0.7909 0.0726  -0.0303 0.1052  298 ALA A C   
1920 O O   . ALA A 268 ? 0.7798 0.9433 0.8241 0.0646  -0.0346 0.1015  298 ALA A O   
1921 C CB  . ALA A 268 ? 0.6537 0.8234 0.7109 0.0879  -0.0285 0.1146  298 ALA A CB  
1922 N N   . SER A 269 ? 0.6689 0.8036 0.7019 0.0754  -0.0279 0.1080  299 SER A N   
1923 C CA  . SER A 269 ? 0.6304 0.7612 0.6550 0.0695  -0.0302 0.1070  299 SER A CA  
1924 C C   . SER A 269 ? 0.5896 0.6996 0.6073 0.0640  -0.0265 0.1004  299 SER A C   
1925 O O   . SER A 269 ? 0.6213 0.7158 0.6370 0.0678  -0.0215 0.0999  299 SER A O   
1926 C CB  . SER A 269 ? 0.5980 0.7272 0.6164 0.0768  -0.0303 0.1159  299 SER A CB  
1927 O OG  . SER A 269 ? 0.7539 0.8685 0.7698 0.0862  -0.0246 0.1204  299 SER A OG  
1928 N N   . ARG A 270 ? 0.5103 0.6204 0.5244 0.0551  -0.0289 0.0953  300 ARG A N   
1929 C CA  . ARG A 270 ? 0.4477 0.5415 0.4567 0.0492  -0.0261 0.0885  300 ARG A CA  
1930 C C   . ARG A 270 ? 0.3744 0.4529 0.3730 0.0499  -0.0235 0.0908  300 ARG A C   
1931 O O   . ARG A 270 ? 0.3405 0.4226 0.3342 0.0474  -0.0259 0.0929  300 ARG A O   
1932 C CB  . ARG A 270 ? 0.3624 0.4639 0.3732 0.0395  -0.0293 0.0818  300 ARG A CB  
1933 C CG  . ARG A 270 ? 0.4204 0.5076 0.4276 0.0336  -0.0267 0.0746  300 ARG A CG  
1934 C CD  . ARG A 270 ? 0.4265 0.5211 0.4394 0.0276  -0.0283 0.0680  300 ARG A CD  
1935 N NE  . ARG A 270 ? 0.3499 0.4380 0.3594 0.0203  -0.0280 0.0619  300 ARG A NE  
1936 C CZ  . ARG A 270 ? 0.4197 0.5126 0.4323 0.0145  -0.0290 0.0562  300 ARG A CZ  
1937 N NH1 . ARG A 270 ? 0.2687 0.3724 0.2873 0.0144  -0.0304 0.0555  300 ARG A NH1 
1938 N NH2 . ARG A 270 ? 0.3914 0.4780 0.4009 0.0088  -0.0283 0.0512  300 ARG A NH2 
1939 N N   . ASP A 271 ? 0.3563 0.4172 0.3508 0.0528  -0.0183 0.0902  301 ASP A N   
1940 C CA  . ASP A 271 ? 0.3587 0.4027 0.3426 0.0527  -0.0147 0.0914  301 ASP A CA  
1941 C C   . ASP A 271 ? 0.3043 0.3413 0.2855 0.0432  -0.0143 0.0832  301 ASP A C   
1942 O O   . ASP A 271 ? 0.3836 0.4154 0.3676 0.0406  -0.0126 0.0775  301 ASP A O   
1943 C CB  . ASP A 271 ? 0.3379 0.3661 0.3181 0.0598  -0.0086 0.0944  301 ASP A CB  
1944 C CG  . ASP A 271 ? 0.3392 0.3498 0.3075 0.0606  -0.0042 0.0968  301 ASP A CG  
1945 O OD1 . ASP A 271 ? 0.3173 0.3245 0.2803 0.0537  -0.0050 0.0936  301 ASP A OD1 
1946 O OD2 . ASP A 271 ? 0.3290 0.3284 0.2929 0.0681  0.0006  0.1019  301 ASP A OD2 
1947 N N   . LEU A 272 ? 0.3074 0.3444 0.2830 0.0383  -0.0157 0.0828  302 LEU A N   
1948 C CA  . LEU A 272 ? 0.3224 0.3545 0.2961 0.0295  -0.0154 0.0753  302 LEU A CA  
1949 C C   . LEU A 272 ? 0.3577 0.3717 0.3260 0.0283  -0.0101 0.0720  302 LEU A C   
1950 O O   . LEU A 272 ? 0.3591 0.3703 0.3283 0.0218  -0.0097 0.0652  302 LEU A O   
1951 C CB  . LEU A 272 ? 0.3996 0.4349 0.3677 0.0248  -0.0174 0.0761  302 LEU A CB  
1952 C CG  . LEU A 272 ? 0.3878 0.4413 0.3598 0.0238  -0.0229 0.0783  302 LEU A CG  
1953 C CD1 . LEU A 272 ? 0.3280 0.3818 0.2925 0.0191  -0.0241 0.0792  302 LEU A CD1 
1954 C CD2 . LEU A 272 ? 0.3458 0.4098 0.3264 0.0190  -0.0253 0.0722  302 LEU A CD2 
1955 N N   . ARG A 273 ? 0.3367 0.3386 0.2993 0.0343  -0.0058 0.0767  303 ARG A N   
1956 C CA  . ARG A 273 ? 0.3668 0.3508 0.3229 0.0325  -0.0002 0.0735  303 ARG A CA  
1957 C C   . ARG A 273 ? 0.3688 0.3489 0.3294 0.0341  0.0018  0.0704  303 ARG A C   
1958 O O   . ARG A 273 ? 0.3865 0.3525 0.3420 0.0318  0.0063  0.0671  303 ARG A O   
1959 C CB  . ARG A 273 ? 0.4580 0.4279 0.4036 0.0375  0.0045  0.0798  303 ARG A CB  
1960 N N   . ARG A 274 ? 0.3708 0.3628 0.3402 0.0374  -0.0012 0.0712  304 ARG A N   
1961 C CA  . ARG A 274 ? 0.3406 0.3285 0.3136 0.0393  0.0009  0.0687  304 ARG A CA  
1962 C C   . ARG A 274 ? 0.3423 0.3390 0.3224 0.0336  -0.0025 0.0619  304 ARG A C   
1963 O O   . ARG A 274 ? 0.3007 0.3099 0.2851 0.0302  -0.0069 0.0604  304 ARG A O   
1964 C CB  . ARG A 274 ? 0.3278 0.3210 0.3051 0.0482  0.0012  0.0748  304 ARG A CB  
1965 C CG  . ARG A 274 ? 0.3990 0.3844 0.3698 0.0555  0.0047  0.0827  304 ARG A CG  
1966 C CD  . ARG A 274 ? 0.3867 0.3787 0.3633 0.0647  0.0052  0.0886  304 ARG A CD  
1967 N NE  . ARG A 274 ? 0.4417 0.4241 0.4191 0.0667  0.0096  0.0862  304 ARG A NE  
1968 C CZ  . ARG A 274 ? 0.4971 0.4829 0.4795 0.0744  0.0113  0.0903  304 ARG A CZ  
1969 N NH1 . ARG A 274 ? 0.4887 0.4881 0.4764 0.0810  0.0088  0.0970  304 ARG A NH1 
1970 N NH2 . ARG A 274 ? 0.5077 0.4834 0.4898 0.0751  0.0157  0.0874  304 ARG A NH2 
1971 N N   . PRO A 275 ? 0.2706 0.2605 0.2514 0.0325  -0.0004 0.0576  305 PRO A N   
1972 C CA  . PRO A 275 ? 0.3332 0.3314 0.3208 0.0287  -0.0035 0.0521  305 PRO A CA  
1973 C C   . PRO A 275 ? 0.3044 0.3162 0.2999 0.0323  -0.0065 0.0545  305 PRO A C   
1974 O O   . PRO A 275 ? 0.2915 0.3059 0.2881 0.0386  -0.0058 0.0603  305 PRO A O   
1975 C CB  . PRO A 275 ? 0.3051 0.2919 0.2903 0.0280  0.0000  0.0484  305 PRO A CB  
1976 C CG  . PRO A 275 ? 0.3292 0.3009 0.3054 0.0288  0.0050  0.0503  305 PRO A CG  
1977 C CD  . PRO A 275 ? 0.3137 0.2871 0.2881 0.0343  0.0053  0.0575  305 PRO A CD  
1978 N N   . ARG A 276 ? 0.2767 0.2973 0.2775 0.0283  -0.0097 0.0501  306 ARG A N   
1979 C CA  . ARG A 276 ? 0.2891 0.3216 0.2970 0.0306  -0.0120 0.0511  306 ARG A CA  
1980 C C   . ARG A 276 ? 0.3289 0.3564 0.3381 0.0361  -0.0089 0.0529  306 ARG A C   
1981 O O   . ARG A 276 ? 0.2810 0.2964 0.2865 0.0359  -0.0058 0.0504  306 ARG A O   
1982 C CB  . ARG A 276 ? 0.2898 0.3286 0.3015 0.0252  -0.0145 0.0454  306 ARG A CB  
1983 C CG  . ARG A 276 ? 0.2358 0.2789 0.2464 0.0194  -0.0169 0.0428  306 ARG A CG  
1984 C CD  . ARG A 276 ? 0.2137 0.2597 0.2273 0.0150  -0.0182 0.0370  306 ARG A CD  
1985 N NE  . ARG A 276 ? 0.1909 0.2417 0.2041 0.0097  -0.0199 0.0346  306 ARG A NE  
1986 C CZ  . ARG A 276 ? 0.3045 0.3498 0.3149 0.0062  -0.0193 0.0314  306 ARG A CZ  
1987 N NH1 . ARG A 276 ? 0.2148 0.2502 0.2222 0.0067  -0.0172 0.0301  306 ARG A NH1 
1988 N NH2 . ARG A 276 ? 0.2129 0.2629 0.2231 0.0016  -0.0204 0.0293  306 ARG A NH2 
1989 N N   . PRO A 277 ? 0.2685 0.3054 0.2830 0.0410  -0.0095 0.0571  307 PRO A N   
1990 C CA  . PRO A 277 ? 0.2583 0.2907 0.2745 0.0463  -0.0061 0.0586  307 PRO A CA  
1991 C C   . PRO A 277 ? 0.3213 0.3483 0.3379 0.0433  -0.0052 0.0527  307 PRO A C   
1992 O O   . PRO A 277 ? 0.3463 0.3617 0.3597 0.0455  -0.0013 0.0522  307 PRO A O   
1993 C CB  . PRO A 277 ? 0.2920 0.3401 0.3157 0.0503  -0.0081 0.0628  307 PRO A CB  
1994 C CG  . PRO A 277 ? 0.3550 0.4122 0.3782 0.0490  -0.0116 0.0658  307 PRO A CG  
1995 C CD  . PRO A 277 ? 0.2982 0.3506 0.3170 0.0416  -0.0131 0.0606  307 PRO A CD  
1996 N N   . THR A 278 ? 0.2881 0.3227 0.3078 0.0382  -0.0085 0.0484  308 THR A N   
1997 C CA  . THR A 278 ? 0.2459 0.2756 0.2652 0.0350  -0.0081 0.0429  308 THR A CA  
1998 C C   . THR A 278 ? 0.2397 0.2717 0.2580 0.0288  -0.0111 0.0386  308 THR A C   
1999 O O   . THR A 278 ? 0.3447 0.3872 0.3661 0.0265  -0.0138 0.0386  308 THR A O   
2000 C CB  . THR A 278 ? 0.2860 0.3227 0.3107 0.0363  -0.0082 0.0422  308 THR A CB  
2001 O OG1 . THR A 278 ? 0.2320 0.2830 0.2616 0.0341  -0.0114 0.0425  308 THR A OG1 
2002 C CG2 . THR A 278 ? 0.2523 0.2874 0.2788 0.0428  -0.0048 0.0465  308 THR A CG2 
2003 N N   . GLY A 279 ? 0.2905 0.3132 0.3045 0.0261  -0.0103 0.0348  309 GLY A N   
2004 C CA  . GLY A 279 ? 0.2607 0.2857 0.2744 0.0208  -0.0126 0.0308  309 GLY A CA  
2005 C C   . GLY A 279 ? 0.2562 0.2717 0.2655 0.0183  -0.0116 0.0272  309 GLY A C   
2006 O O   . GLY A 279 ? 0.2433 0.2496 0.2491 0.0199  -0.0090 0.0271  309 GLY A O   
2007 N N   . PRO A 280 ? 0.2366 0.2546 0.2460 0.0140  -0.0135 0.0239  310 PRO A N   
2008 C CA  . PRO A 280 ? 0.2268 0.2385 0.2330 0.0110  -0.0130 0.0200  310 PRO A CA  
2009 C C   . PRO A 280 ? 0.2289 0.2312 0.2296 0.0109  -0.0102 0.0213  310 PRO A C   
2010 O O   . PRO A 280 ? 0.2006 0.2023 0.1998 0.0116  -0.0092 0.0245  310 PRO A O   
2011 C CB  . PRO A 280 ? 0.2359 0.2540 0.2443 0.0071  -0.0153 0.0173  310 PRO A CB  
2012 C CG  . PRO A 280 ? 0.2070 0.2337 0.2194 0.0078  -0.0168 0.0186  310 PRO A CG  
2013 C CD  . PRO A 280 ? 0.2599 0.2872 0.2724 0.0114  -0.0159 0.0233  310 PRO A CD  
2014 N N   . ILE A 281 ? 0.2012 0.1957 0.1983 0.0097  -0.0086 0.0187  311 ILE A N   
2015 C CA  . ILE A 281 ? 0.2334 0.2175 0.2240 0.0084  -0.0052 0.0189  311 ILE A CA  
2016 C C   . ILE A 281 ? 0.2398 0.2229 0.2286 0.0029  -0.0058 0.0138  311 ILE A C   
2017 O O   . ILE A 281 ? 0.2514 0.2410 0.2438 0.0013  -0.0088 0.0106  311 ILE A O   
2018 C CB  . ILE A 281 ? 0.2190 0.1933 0.2056 0.0119  -0.0015 0.0207  311 ILE A CB  
2019 C CG1 . ILE A 281 ? 0.2259 0.1992 0.2125 0.0110  -0.0025 0.0171  311 ILE A CG1 
2020 C CG2 . ILE A 281 ? 0.2186 0.1956 0.2082 0.0178  -0.0008 0.0260  311 ILE A CG2 
2021 C CD1 . ILE A 281 ? 0.2410 0.2031 0.2223 0.0131  0.0016  0.0178  311 ILE A CD1 
2022 N N   . VAL A 282 ? 0.2661 0.2411 0.2491 -0.0001 -0.0028 0.0132  312 VAL A N   
2023 C CA  . VAL A 282 ? 0.2475 0.2214 0.2282 -0.0059 -0.0029 0.0082  312 VAL A CA  
2024 C C   . VAL A 282 ? 0.2764 0.2438 0.2534 -0.0060 -0.0017 0.0062  312 VAL A C   
2025 O O   . VAL A 282 ? 0.2688 0.2246 0.2386 -0.0068 0.0026  0.0065  312 VAL A O   
2026 C CB  . VAL A 282 ? 0.2825 0.2498 0.2578 -0.0100 0.0004  0.0077  312 VAL A CB  
2027 C CG1 . VAL A 282 ? 0.2491 0.2174 0.2230 -0.0167 0.0002  0.0020  312 VAL A CG1 
2028 C CG2 . VAL A 282 ? 0.3186 0.2917 0.2968 -0.0097 -0.0007 0.0100  312 VAL A CG2 
2029 N N   . ASP A 283 ? 0.2789 0.2529 0.2598 -0.0052 -0.0051 0.0044  313 ASP A N   
2030 C CA  . ASP A 283 ? 0.3221 0.2903 0.2991 -0.0052 -0.0042 0.0027  313 ASP A CA  
2031 C C   . ASP A 283 ? 0.3129 0.2808 0.2865 -0.0113 -0.0048 -0.0023 313 ASP A C   
2032 O O   . ASP A 283 ? 0.3473 0.3083 0.3153 -0.0127 -0.0032 -0.0040 313 ASP A O   
2033 C CB  . ASP A 283 ? 0.2959 0.2702 0.2775 -0.0013 -0.0073 0.0032  313 ASP A CB  
2034 C CG  . ASP A 283 ? 0.3198 0.3057 0.3072 -0.0026 -0.0119 0.0007  313 ASP A CG  
2035 O OD1 . ASP A 283 ? 0.3371 0.3288 0.3278 -0.0044 -0.0129 0.0004  313 ASP A OD1 
2036 O OD2 . ASP A 283 ? 0.3629 0.3513 0.3510 -0.0016 -0.0141 -0.0007 313 ASP A OD2 
2037 N N   . GLY A 284 ? 0.3118 0.2876 0.2887 -0.0151 -0.0069 -0.0047 314 GLY A N   
2038 C CA  . GLY A 284 ? 0.2640 0.2429 0.2393 -0.0210 -0.0080 -0.0095 314 GLY A CA  
2039 C C   . GLY A 284 ? 0.3349 0.3244 0.3150 -0.0203 -0.0130 -0.0116 314 GLY A C   
2040 O O   . GLY A 284 ? 0.4142 0.4102 0.3951 -0.0248 -0.0150 -0.0154 314 GLY A O   
2041 N N   . HIS A 285 ? 0.3128 0.3046 0.2962 -0.0147 -0.0150 -0.0092 315 HIS A N   
2042 C CA  . HIS A 285 ? 0.2688 0.2691 0.2559 -0.0130 -0.0192 -0.0106 315 HIS A CA  
2043 C C   . HIS A 285 ? 0.2867 0.2962 0.2815 -0.0099 -0.0215 -0.0092 315 HIS A C   
2044 O O   . HIS A 285 ? 0.2929 0.3118 0.2923 -0.0113 -0.0240 -0.0113 315 HIS A O   
2045 C CB  . HIS A 285 ? 0.3073 0.3012 0.2904 -0.0097 -0.0189 -0.0094 315 HIS A CB  
2046 C CG  . HIS A 285 ? 0.3493 0.3501 0.3353 -0.0067 -0.0228 -0.0098 315 HIS A CG  
2047 N ND1 . HIS A 285 ? 0.3776 0.3868 0.3650 -0.0087 -0.0264 -0.0126 315 HIS A ND1 
2048 C CD2 . HIS A 285 ? 0.3289 0.3290 0.3160 -0.0018 -0.0234 -0.0077 315 HIS A CD2 
2049 C CE1 . HIS A 285 ? 0.3469 0.3596 0.3359 -0.0046 -0.0290 -0.0118 315 HIS A CE1 
2050 N NE2 . HIS A 285 ? 0.4274 0.4341 0.4159 -0.0007 -0.0270 -0.0090 315 HIS A NE2 
2051 N N   . VAL A 286 ? 0.2496 0.2568 0.2460 -0.0058 -0.0205 -0.0059 316 VAL A N   
2052 C CA  . VAL A 286 ? 0.2488 0.2636 0.2514 -0.0038 -0.0219 -0.0048 316 VAL A CA  
2053 C C   . VAL A 286 ? 0.2423 0.2599 0.2469 -0.0070 -0.0209 -0.0051 316 VAL A C   
2054 O O   . VAL A 286 ? 0.1846 0.2101 0.1938 -0.0080 -0.0224 -0.0065 316 VAL A O   
2055 C CB  . VAL A 286 ? 0.2394 0.2516 0.2426 0.0004  -0.0209 -0.0015 316 VAL A CB  
2056 C CG1 . VAL A 286 ? 0.2101 0.2296 0.2186 0.0014  -0.0219 -0.0008 316 VAL A CG1 
2057 C CG2 . VAL A 286 ? 0.2473 0.2563 0.2481 0.0032  -0.0215 -0.0015 316 VAL A CG2 
2058 N N   . LEU A 287 ? 0.2082 0.2185 0.2087 -0.0085 -0.0179 -0.0037 317 LEU A N   
2059 C CA  . LEU A 287 ? 0.2215 0.2324 0.2221 -0.0118 -0.0164 -0.0038 317 LEU A CA  
2060 C C   . LEU A 287 ? 0.2127 0.2166 0.2075 -0.0162 -0.0138 -0.0057 317 LEU A C   
2061 O O   . LEU A 287 ? 0.2224 0.2161 0.2114 -0.0155 -0.0106 -0.0036 317 LEU A O   
2062 C CB  . LEU A 287 ? 0.2241 0.2326 0.2246 -0.0091 -0.0149 0.0003  317 LEU A CB  
2063 C CG  . LEU A 287 ? 0.2226 0.2374 0.2280 -0.0055 -0.0169 0.0021  317 LEU A CG  
2064 C CD1 . LEU A 287 ? 0.1862 0.1992 0.1909 -0.0030 -0.0156 0.0064  317 LEU A CD1 
2065 C CD2 . LEU A 287 ? 0.1797 0.2033 0.1900 -0.0073 -0.0188 -0.0002 317 LEU A CD2 
2066 N N   . PRO A 288 ? 0.2732 0.2821 0.2689 -0.0209 -0.0147 -0.0098 318 PRO A N   
2067 C CA  . PRO A 288 ? 0.2333 0.2354 0.2227 -0.0264 -0.0118 -0.0122 318 PRO A CA  
2068 C C   . PRO A 288 ? 0.2207 0.2156 0.2061 -0.0287 -0.0078 -0.0109 318 PRO A C   
2069 O O   . PRO A 288 ? 0.2549 0.2407 0.2332 -0.0328 -0.0041 -0.0122 318 PRO A O   
2070 C CB  . PRO A 288 ? 0.2775 0.2904 0.2710 -0.0309 -0.0144 -0.0169 318 PRO A CB  
2071 C CG  . PRO A 288 ? 0.2653 0.2895 0.2673 -0.0277 -0.0176 -0.0163 318 PRO A CG  
2072 C CD  . PRO A 288 ? 0.2707 0.2919 0.2733 -0.0213 -0.0183 -0.0123 318 PRO A CD  
2073 N N   . GLN A 289 ? 0.2277 0.2257 0.2166 -0.0265 -0.0081 -0.0083 319 GLN A N   
2074 C CA  . GLN A 289 ? 0.2564 0.2475 0.2408 -0.0282 -0.0044 -0.0063 319 GLN A CA  
2075 C C   . GLN A 289 ? 0.2285 0.2232 0.2165 -0.0237 -0.0057 -0.0022 319 GLN A C   
2076 O O   . GLN A 289 ? 0.2069 0.2096 0.2008 -0.0205 -0.0090 -0.0017 319 GLN A O   
2077 C CB  . GLN A 289 ? 0.2482 0.2423 0.2325 -0.0350 -0.0032 -0.0104 319 GLN A CB  
2078 C CG  . GLN A 289 ? 0.2567 0.2649 0.2499 -0.0358 -0.0067 -0.0127 319 GLN A CG  
2079 C CD  . GLN A 289 ? 0.3629 0.3764 0.3575 -0.0427 -0.0058 -0.0176 319 GLN A CD  
2080 O OE1 . GLN A 289 ? 0.3461 0.3520 0.3344 -0.0477 -0.0019 -0.0189 319 GLN A OE1 
2081 N NE2 . GLN A 289 ? 0.3253 0.3519 0.3279 -0.0429 -0.0091 -0.0204 319 GLN A NE2 
2082 N N   . THR A 290 ? 0.2222 0.2104 0.2056 -0.0238 -0.0028 0.0007  320 THR A N   
2083 C CA  . THR A 290 ? 0.2635 0.2561 0.2496 -0.0207 -0.0042 0.0044  320 THR A CA  
2084 C C   . THR A 290 ? 0.2461 0.2498 0.2385 -0.0235 -0.0066 0.0015  320 THR A C   
2085 O O   . THR A 290 ? 0.2373 0.2443 0.2313 -0.0281 -0.0064 -0.0029 320 THR A O   
2086 C CB  . THR A 290 ? 0.2821 0.2660 0.2613 -0.0208 -0.0007 0.0080  320 THR A CB  
2087 O OG1 . THR A 290 ? 0.3452 0.3268 0.3214 -0.0270 0.0017  0.0047  320 THR A OG1 
2088 C CG2 . THR A 290 ? 0.2707 0.2426 0.2433 -0.0174 0.0027  0.0112  320 THR A CG2 
2089 N N   . ASP A 291 ? 0.2456 0.2554 0.2416 -0.0207 -0.0087 0.0039  321 ASP A N   
2090 C CA  . ASP A 291 ? 0.2518 0.2707 0.2531 -0.0231 -0.0102 0.0013  321 ASP A CA  
2091 C C   . ASP A 291 ? 0.2497 0.2669 0.2480 -0.0279 -0.0078 0.0004  321 ASP A C   
2092 O O   . ASP A 291 ? 0.2507 0.2744 0.2531 -0.0311 -0.0080 -0.0031 321 ASP A O   
2093 C CB  . ASP A 291 ? 0.2050 0.2298 0.2097 -0.0198 -0.0124 0.0038  321 ASP A CB  
2094 C CG  . ASP A 291 ? 0.2314 0.2524 0.2320 -0.0173 -0.0119 0.0089  321 ASP A CG  
2095 O OD1 . ASP A 291 ? 0.2498 0.2634 0.2462 -0.0149 -0.0104 0.0115  321 ASP A OD1 
2096 O OD2 . ASP A 291 ? 0.2169 0.2427 0.2183 -0.0176 -0.0127 0.0104  321 ASP A OD2 
2097 N N   . SER A 292 ? 0.2437 0.2519 0.2349 -0.0281 -0.0051 0.0034  322 SER A N   
2098 C CA  . SER A 292 ? 0.3183 0.3232 0.3054 -0.0330 -0.0022 0.0023  322 SER A CA  
2099 C C   . SER A 292 ? 0.2440 0.2480 0.2311 -0.0384 -0.0003 -0.0029 322 SER A C   
2100 O O   . SER A 292 ? 0.2785 0.2873 0.2680 -0.0431 0.0006  -0.0063 322 SER A O   
2101 C CB  . SER A 292 ? 0.2949 0.2891 0.2733 -0.0313 0.0005  0.0073  322 SER A CB  
2102 O OG  . SER A 292 ? 0.2689 0.2664 0.2479 -0.0269 -0.0017 0.0120  322 SER A OG  
2103 N N   . ALA A 293 ? 0.2449 0.2433 0.2294 -0.0381 0.0006  -0.0037 323 ALA A N   
2104 C CA  . ALA A 293 ? 0.2758 0.2745 0.2602 -0.0438 0.0022  -0.0090 323 ALA A CA  
2105 C C   . ALA A 293 ? 0.2765 0.2891 0.2705 -0.0448 -0.0013 -0.0131 323 ALA A C   
2106 O O   . ALA A 293 ? 0.2841 0.3021 0.2807 -0.0502 -0.0003 -0.0174 323 ALA A O   
2107 C CB  . ALA A 293 ? 0.2553 0.2448 0.2342 -0.0434 0.0038  -0.0089 323 ALA A CB  
2108 N N   . ALA A 294 ? 0.2321 0.2507 0.2315 -0.0396 -0.0050 -0.0117 324 ALA A N   
2109 C CA  . ALA A 294 ? 0.2721 0.3031 0.2801 -0.0393 -0.0080 -0.0148 324 ALA A CA  
2110 C C   . ALA A 294 ? 0.3081 0.3459 0.3204 -0.0415 -0.0074 -0.0161 324 ALA A C   
2111 O O   . ALA A 294 ? 0.3102 0.3566 0.3280 -0.0443 -0.0077 -0.0201 324 ALA A O   
2112 C CB  . ALA A 294 ? 0.1929 0.2267 0.2042 -0.0331 -0.0113 -0.0125 324 ALA A CB  
2113 N N   . ILE A 295 ? 0.2743 0.3087 0.2839 -0.0402 -0.0066 -0.0128 325 ILE A N   
2114 C CA  . ILE A 295 ? 0.3559 0.3947 0.3677 -0.0430 -0.0052 -0.0140 325 ILE A CA  
2115 C C   . ILE A 295 ? 0.3215 0.3596 0.3318 -0.0495 -0.0020 -0.0176 325 ILE A C   
2116 O O   . ILE A 295 ? 0.4468 0.4931 0.4629 -0.0523 -0.0015 -0.0212 325 ILE A O   
2117 C CB  . ILE A 295 ? 0.2812 0.3148 0.2879 -0.0415 -0.0046 -0.0096 325 ILE A CB  
2118 C CG1 . ILE A 295 ? 0.3495 0.3883 0.3601 -0.0371 -0.0073 -0.0077 325 ILE A CG1 
2119 C CG2 . ILE A 295 ? 0.5395 0.5726 0.5440 -0.0464 -0.0017 -0.0107 325 ILE A CG2 
2120 C CD1 . ILE A 295 ? 0.2966 0.3330 0.3028 -0.0369 -0.0069 -0.0041 325 ILE A CD1 
2121 N N   . ALA A 296 ? 0.3600 0.3878 0.3624 -0.0519 0.0006  -0.0167 326 ALA A N   
2122 C CA  . ALA A 296 ? 0.3410 0.3662 0.3403 -0.0588 0.0044  -0.0202 326 ALA A CA  
2123 C C   . ALA A 296 ? 0.3586 0.3935 0.3646 -0.0623 0.0037  -0.0256 326 ALA A C   
2124 O O   . ALA A 296 ? 0.4410 0.4819 0.4503 -0.0674 0.0056  -0.0295 326 ALA A O   
2125 C CB  . ALA A 296 ? 0.3238 0.3344 0.3122 -0.0603 0.0079  -0.0180 326 ALA A CB  
2126 N N   . ALA A 297 ? 0.3411 0.3782 0.3490 -0.0597 0.0009  -0.0260 327 ALA A N   
2127 C CA  . ALA A 297 ? 0.3231 0.3702 0.3368 -0.0629 -0.0003 -0.0308 327 ALA A CA  
2128 C C   . ALA A 297 ? 0.3344 0.3962 0.3591 -0.0595 -0.0039 -0.0321 327 ALA A C   
2129 O O   . ALA A 297 ? 0.3462 0.4185 0.3768 -0.0611 -0.0056 -0.0356 327 ALA A O   
2130 C CB  . ALA A 297 ? 0.2321 0.2744 0.2418 -0.0623 -0.0015 -0.0308 327 ALA A CB  
2131 N N   . GLY A 298 ? 0.3271 0.3901 0.3544 -0.0550 -0.0047 -0.0293 328 GLY A N   
2132 C CA  . GLY A 298 ? 0.3010 0.3758 0.3376 -0.0512 -0.0072 -0.0302 328 GLY A CA  
2133 C C   . GLY A 298 ? 0.3588 0.4366 0.3979 -0.0455 -0.0113 -0.0289 328 GLY A C   
2134 O O   . GLY A 298 ? 0.3401 0.4282 0.3868 -0.0424 -0.0133 -0.0300 328 GLY A O   
2135 N N   . GLN A 299 ? 0.2949 0.3636 0.3276 -0.0436 -0.0121 -0.0263 329 GLN A N   
2136 C CA  . GLN A 299 ? 0.3278 0.3976 0.3616 -0.0383 -0.0156 -0.0249 329 GLN A CA  
2137 C C   . GLN A 299 ? 0.3224 0.3910 0.3574 -0.0327 -0.0164 -0.0215 329 GLN A C   
2138 O O   . GLN A 299 ? 0.2159 0.2768 0.2464 -0.0297 -0.0168 -0.0183 329 GLN A O   
2139 C CB  . GLN A 299 ? 0.3908 0.4508 0.4171 -0.0389 -0.0154 -0.0237 329 GLN A CB  
2140 C CG  . GLN A 299 ? 0.3775 0.4396 0.4025 -0.0444 -0.0150 -0.0276 329 GLN A CG  
2141 C CD  . GLN A 299 ? 0.4979 0.5711 0.5286 -0.0427 -0.0189 -0.0297 329 GLN A CD  
2142 O OE1 . GLN A 299 ? 0.5155 0.5873 0.5455 -0.0378 -0.0214 -0.0277 329 GLN A OE1 
2143 N NE2 . GLN A 299 ? 0.3669 0.4516 0.4032 -0.0467 -0.0193 -0.0336 329 GLN A NE2 
2144 N N   . LEU A 300 ? 0.2243 0.3008 0.2656 -0.0315 -0.0163 -0.0226 330 LEU A N   
2145 C CA  . LEU A 300 ? 0.2735 0.3494 0.3159 -0.0273 -0.0164 -0.0203 330 LEU A CA  
2146 C C   . LEU A 300 ? 0.2338 0.3186 0.2831 -0.0233 -0.0179 -0.0216 330 LEU A C   
2147 O O   . LEU A 300 ? 0.2907 0.3843 0.3458 -0.0248 -0.0175 -0.0244 330 LEU A O   
2148 C CB  . LEU A 300 ? 0.3000 0.3744 0.3415 -0.0301 -0.0135 -0.0201 330 LEU A CB  
2149 C CG  . LEU A 300 ? 0.2776 0.3429 0.3120 -0.0310 -0.0124 -0.0168 330 LEU A CG  
2150 C CD1 . LEU A 300 ? 0.2941 0.3599 0.3280 -0.0340 -0.0098 -0.0172 330 LEU A CD1 
2151 C CD2 . LEU A 300 ? 0.3157 0.3780 0.3484 -0.0262 -0.0143 -0.0137 330 LEU A CD2 
2152 N N   . ALA A 301 ? 0.2303 0.3129 0.2790 -0.0182 -0.0191 -0.0194 331 ALA A N   
2153 C CA  . ALA A 301 ? 0.2381 0.3271 0.2922 -0.0137 -0.0197 -0.0200 331 ALA A CA  
2154 C C   . ALA A 301 ? 0.2645 0.3551 0.3211 -0.0144 -0.0164 -0.0207 331 ALA A C   
2155 O O   . ALA A 301 ? 0.2782 0.3626 0.3308 -0.0148 -0.0148 -0.0190 331 ALA A O   
2156 C CB  . ALA A 301 ? 0.1674 0.2518 0.2187 -0.0085 -0.0212 -0.0176 331 ALA A CB  
2157 N N   . PRO A 302 ? 0.2704 0.3696 0.3335 -0.0148 -0.0152 -0.0231 332 PRO A N   
2158 C CA  . PRO A 302 ? 0.2270 0.3270 0.2921 -0.0159 -0.0114 -0.0240 332 PRO A CA  
2159 C C   . PRO A 302 ? 0.2579 0.3565 0.3238 -0.0105 -0.0099 -0.0229 332 PRO A C   
2160 O O   . PRO A 302 ? 0.2799 0.3835 0.3508 -0.0086 -0.0073 -0.0242 332 PRO A O   
2161 C CB  . PRO A 302 ? 0.2426 0.3530 0.3149 -0.0181 -0.0105 -0.0271 332 PRO A CB  
2162 C CG  . PRO A 302 ? 0.2798 0.3971 0.3553 -0.0159 -0.0144 -0.0276 332 PRO A CG  
2163 C CD  . PRO A 302 ? 0.2640 0.3733 0.3331 -0.0136 -0.0173 -0.0250 332 PRO A CD  
2164 N N   . VAL A 303 ? 0.2529 0.3442 0.3134 -0.0081 -0.0110 -0.0205 333 VAL A N   
2165 C CA  . VAL A 303 ? 0.2217 0.3092 0.2810 -0.0037 -0.0091 -0.0194 333 VAL A CA  
2166 C C   . VAL A 303 ? 0.2058 0.2895 0.2627 -0.0071 -0.0048 -0.0201 333 VAL A C   
2167 O O   . VAL A 303 ? 0.1642 0.2475 0.2195 -0.0125 -0.0041 -0.0207 333 VAL A O   
2168 C CB  . VAL A 303 ? 0.2684 0.3491 0.3222 -0.0013 -0.0112 -0.0170 333 VAL A CB  
2169 C CG1 . VAL A 303 ? 0.2319 0.3157 0.2871 0.0016  -0.0153 -0.0165 333 VAL A CG1 
2170 C CG2 . VAL A 303 ? 0.1567 0.2317 0.2050 -0.0058 -0.0114 -0.0158 333 VAL A CG2 
2171 N N   . ARG A 304 ? 0.1952 0.2755 0.2510 -0.0042 -0.0017 -0.0199 334 ARG A N   
2172 C CA  . ARG A 304 ? 0.1964 0.2717 0.2481 -0.0080 0.0025  -0.0206 334 ARG A CA  
2173 C C   . ARG A 304 ? 0.2204 0.2903 0.2654 -0.0117 0.0008  -0.0189 334 ARG A C   
2174 O O   . ARG A 304 ? 0.1966 0.2635 0.2391 -0.0093 -0.0015 -0.0172 334 ARG A O   
2175 C CB  . ARG A 304 ? 0.1759 0.2472 0.2267 -0.0041 0.0067  -0.0209 334 ARG A CB  
2176 C CG  . ARG A 304 ? 0.1968 0.2739 0.2546 0.0007  0.0088  -0.0220 334 ARG A CG  
2177 C CD  . ARG A 304 ? 0.2066 0.2785 0.2627 0.0069  0.0118  -0.0211 334 ARG A CD  
2178 N NE  . ARG A 304 ? 0.2648 0.3412 0.3270 0.0118  0.0152  -0.0219 334 ARG A NE  
2179 C CZ  . ARG A 304 ? 0.2555 0.3389 0.3237 0.0186  0.0128  -0.0208 334 ARG A CZ  
2180 N NH1 . ARG A 304 ? 0.2233 0.3098 0.2919 0.0205  0.0070  -0.0192 334 ARG A NH1 
2181 N NH2 . ARG A 304 ? 0.2795 0.3670 0.3533 0.0236  0.0165  -0.0212 334 ARG A NH2 
2182 N N   . VAL A 305 ? 0.1909 0.2600 0.2331 -0.0175 0.0020  -0.0193 335 VAL A N   
2183 C CA  . VAL A 305 ? 0.1747 0.2406 0.2112 -0.0208 0.0000  -0.0173 335 VAL A CA  
2184 C C   . VAL A 305 ? 0.1996 0.2627 0.2312 -0.0257 0.0033  -0.0180 335 VAL A C   
2185 O O   . VAL A 305 ? 0.1966 0.2606 0.2287 -0.0288 0.0063  -0.0198 335 VAL A O   
2186 C CB  . VAL A 305 ? 0.1884 0.2562 0.2251 -0.0231 -0.0029 -0.0164 335 VAL A CB  
2187 C CG1 . VAL A 305 ? 0.1639 0.2287 0.1947 -0.0261 -0.0044 -0.0138 335 VAL A CG1 
2188 C CG2 . VAL A 305 ? 0.1674 0.2372 0.2076 -0.0192 -0.0062 -0.0159 335 VAL A CG2 
2189 N N   . LEU A 306 ? 0.1806 0.2406 0.2073 -0.0267 0.0030  -0.0166 336 LEU A N   
2190 C CA  . LEU A 306 ? 0.1859 0.2444 0.2068 -0.0324 0.0048  -0.0167 336 LEU A CA  
2191 C C   . LEU A 306 ? 0.1812 0.2411 0.1992 -0.0339 0.0007  -0.0136 336 LEU A C   
2192 O O   . LEU A 306 ? 0.2022 0.2619 0.2203 -0.0311 -0.0017 -0.0119 336 LEU A O   
2193 C CB  . LEU A 306 ? 0.1770 0.2315 0.1943 -0.0328 0.0084  -0.0180 336 LEU A CB  
2194 C CG  . LEU A 306 ? 0.1815 0.2351 0.1920 -0.0394 0.0100  -0.0183 336 LEU A CG  
2195 C CD1 . LEU A 306 ? 0.1849 0.2391 0.1938 -0.0443 0.0122  -0.0197 336 LEU A CD1 
2196 C CD2 . LEU A 306 ? 0.1956 0.2442 0.2022 -0.0402 0.0143  -0.0201 336 LEU A CD2 
2197 N N   . ILE A 307 ? 0.1734 0.2346 0.1887 -0.0380 0.0002  -0.0128 337 ILE A N   
2198 C CA  . ILE A 307 ? 0.1950 0.2575 0.2077 -0.0386 -0.0035 -0.0093 337 ILE A CA  
2199 C C   . ILE A 307 ? 0.2077 0.2712 0.2144 -0.0444 -0.0029 -0.0085 337 ILE A C   
2200 O O   . ILE A 307 ? 0.2089 0.2715 0.2136 -0.0483 0.0003  -0.0108 337 ILE A O   
2201 C CB  . ILE A 307 ? 0.1787 0.2411 0.1939 -0.0368 -0.0055 -0.0082 337 ILE A CB  
2202 C CG1 . ILE A 307 ? 0.1719 0.2344 0.1841 -0.0361 -0.0088 -0.0041 337 ILE A CG1 
2203 C CG2 . ILE A 307 ? 0.2002 0.2623 0.2151 -0.0403 -0.0030 -0.0102 337 ILE A CG2 
2204 C CD1 . ILE A 307 ? 0.1719 0.2323 0.1853 -0.0342 -0.0100 -0.0030 337 ILE A CD1 
2205 N N   . GLY A 308 ? 0.1919 0.2580 0.1957 -0.0448 -0.0059 -0.0052 338 GLY A N   
2206 C CA  . GLY A 308 ? 0.2147 0.2830 0.2125 -0.0501 -0.0061 -0.0040 338 GLY A CA  
2207 C C   . GLY A 308 ? 0.2004 0.2732 0.1964 -0.0492 -0.0100 0.0003  338 GLY A C   
2208 O O   . GLY A 308 ? 0.1790 0.2526 0.1784 -0.0445 -0.0122 0.0022  338 GLY A O   
2209 N N   . THR A 309 ? 0.1881 0.2642 0.1784 -0.0538 -0.0107 0.0019  339 THR A N   
2210 C CA  . THR A 309 ? 0.1892 0.2714 0.1777 -0.0530 -0.0147 0.0065  339 THR A CA  
2211 C C   . THR A 309 ? 0.2312 0.3193 0.2147 -0.0592 -0.0147 0.0059  339 THR A C   
2212 O O   . THR A 309 ? 0.2278 0.3137 0.2083 -0.0644 -0.0113 0.0020  339 THR A O   
2213 C CB  . THR A 309 ? 0.2365 0.3175 0.2219 -0.0516 -0.0165 0.0106  339 THR A CB  
2214 O OG1 . THR A 309 ? 0.2717 0.3497 0.2520 -0.0567 -0.0142 0.0088  339 THR A OG1 
2215 C CG2 . THR A 309 ? 0.1898 0.2654 0.1795 -0.0459 -0.0166 0.0114  339 THR A CG2 
2216 N N   . ASN A 310 ? 0.2032 0.2992 0.1860 -0.0586 -0.0184 0.0099  340 ASN A N   
2217 C CA  . ASN A 310 ? 0.1993 0.3029 0.1768 -0.0650 -0.0193 0.0100  340 ASN A CA  
2218 C C   . ASN A 310 ? 0.2056 0.3121 0.1774 -0.0665 -0.0219 0.0141  340 ASN A C   
2219 O O   . ASN A 310 ? 0.2543 0.3573 0.2267 -0.0617 -0.0231 0.0176  340 ASN A O   
2220 C CB  . ASN A 310 ? 0.2053 0.3181 0.1858 -0.0642 -0.0219 0.0115  340 ASN A CB  
2221 C CG  . ASN A 310 ? 0.2461 0.3552 0.2309 -0.0631 -0.0190 0.0075  340 ASN A CG  
2222 O OD1 . ASN A 310 ? 0.1912 0.2916 0.1761 -0.0635 -0.0151 0.0035  340 ASN A OD1 
2223 N ND2 . ASN A 310 ? 0.1998 0.3157 0.1880 -0.0616 -0.0207 0.0086  340 ASN A ND2 
2224 N N   . ALA A 311 ? 0.2797 0.2215 0.1511 0.0254  -0.0662 -0.0163 341 ALA A N   
2225 C CA  . ALA A 311 ? 0.3465 0.2881 0.2156 0.0306  -0.0636 -0.0163 341 ALA A CA  
2226 C C   . ALA A 311 ? 0.3979 0.3515 0.2837 0.0259  -0.0575 -0.0131 341 ALA A C   
2227 O O   . ALA A 311 ? 0.3554 0.3155 0.2446 0.0292  -0.0495 -0.0136 341 ALA A O   
2228 C CB  . ALA A 311 ? 0.3237 0.2477 0.1770 0.0340  -0.0754 -0.0159 341 ALA A CB  
2229 N N   . ASP A 312 ? 0.3154 0.2723 0.2122 0.0184  -0.0610 -0.0094 342 ASP A N   
2230 C CA  . ASP A 312 ? 0.3111 0.2781 0.2232 0.0149  -0.0570 -0.0063 342 ASP A CA  
2231 C C   . ASP A 312 ? 0.3411 0.3202 0.2679 0.0085  -0.0515 -0.0043 342 ASP A C   
2232 O O   . ASP A 312 ? 0.3320 0.3144 0.2687 0.0028  -0.0550 0.0000  342 ASP A O   
2233 C CB  . ASP A 312 ? 0.3125 0.2717 0.2243 0.0135  -0.0673 -0.0030 342 ASP A CB  
2234 C CG  . ASP A 312 ? 0.3392 0.3074 0.2645 0.0125  -0.0637 -0.0005 342 ASP A CG  
2235 O OD1 . ASP A 312 ? 0.3511 0.3300 0.2840 0.0134  -0.0531 -0.0014 342 ASP A OD1 
2236 O OD2 . ASP A 312 ? 0.3877 0.3514 0.3158 0.0110  -0.0724 0.0023  342 ASP A OD2 
2237 N N   . GLU A 313 ? 0.2774 0.2633 0.2057 0.0098  -0.0429 -0.0071 343 GLU A N   
2238 C CA  . GLU A 313 ? 0.2874 0.2821 0.2251 0.0053  -0.0376 -0.0060 343 GLU A CA  
2239 C C   . GLU A 313 ? 0.2470 0.2518 0.1998 0.0025  -0.0337 -0.0022 343 GLU A C   
2240 O O   . GLU A 313 ? 0.2374 0.2480 0.1981 -0.0020 -0.0323 0.0012  343 GLU A O   
2241 C CB  . GLU A 313 ? 0.2375 0.2361 0.1736 0.0082  -0.0303 -0.0103 343 GLU A CB  
2242 C CG  . GLU A 313 ? 0.2867 0.2777 0.2105 0.0111  -0.0336 -0.0140 343 GLU A CG  
2243 C CD  . GLU A 313 ? 0.3368 0.3238 0.2563 0.0074  -0.0368 -0.0132 343 GLU A CD  
2244 O OE1 . GLU A 313 ? 0.2713 0.2624 0.1979 0.0022  -0.0355 -0.0092 343 GLU A OE1 
2245 O OE2 . GLU A 313 ? 0.3476 0.3275 0.2565 0.0099  -0.0405 -0.0163 343 GLU A OE2 
2246 N N   . GLY A 314 ? 0.2730 0.2803 0.2296 0.0055  -0.0316 -0.0025 344 GLY A N   
2247 C CA  . GLY A 314 ? 0.2541 0.2713 0.2246 0.0044  -0.0270 0.0001  344 GLY A CA  
2248 C C   . GLY A 314 ? 0.2887 0.3088 0.2693 0.0007  -0.0329 0.0052  344 GLY A C   
2249 O O   . GLY A 314 ? 0.2448 0.2756 0.2390 -0.0006 -0.0286 0.0080  344 GLY A O   
2250 N N   . ARG A 315 ? 0.2530 0.2635 0.2275 -0.0006 -0.0433 0.0066  345 ARG A N   
2251 C CA  . ARG A 315 ? 0.3110 0.3235 0.2965 -0.0043 -0.0510 0.0116  345 ARG A CA  
2252 C C   . ARG A 315 ? 0.3158 0.3404 0.3171 -0.0105 -0.0480 0.0168  345 ARG A C   
2253 O O   . ARG A 315 ? 0.2594 0.2944 0.2777 -0.0125 -0.0482 0.0211  345 ARG A O   
2254 C CB  . ARG A 315 ? 0.2713 0.2683 0.2449 -0.0048 -0.0642 0.0118  345 ARG A CB  
2255 C CG  . ARG A 315 ? 0.3210 0.3187 0.3071 -0.0100 -0.0748 0.0173  345 ARG A CG  
2256 C CD  . ARG A 315 ? 0.2659 0.2450 0.2376 -0.0082 -0.0893 0.0162  345 ARG A CD  
2257 N NE  . ARG A 315 ? 0.3896 0.3546 0.3430 -0.0076 -0.0939 0.0136  345 ARG A NE  
2258 C CZ  . ARG A 315 ? 0.3554 0.3156 0.3098 -0.0141 -0.1016 0.0167  345 ARG A CZ  
2259 N NH1 . ARG A 315 ? 0.4833 0.4532 0.4577 -0.0224 -0.1045 0.0232  345 ARG A NH1 
2260 N NH2 . ARG A 315 ? 0.3127 0.2581 0.2480 -0.0120 -0.1062 0.0134  345 ARG A NH2 
2261 N N   . ALA A 316 ? 0.2596 0.2836 0.2557 -0.0131 -0.0447 0.0166  346 ALA A N   
2262 C CA  . ALA A 316 ? 0.2635 0.2979 0.2721 -0.0188 -0.0408 0.0223  346 ALA A CA  
2263 C C   . ALA A 316 ? 0.2478 0.2974 0.2682 -0.0163 -0.0284 0.0230  346 ALA A C   
2264 O O   . ALA A 316 ? 0.3087 0.3693 0.3413 -0.0199 -0.0237 0.0286  346 ALA A O   
2265 C CB  . ALA A 316 ? 0.2313 0.2583 0.2277 -0.0214 -0.0406 0.0217  346 ALA A CB  
2266 N N   . PHE A 317 ? 0.2985 0.3484 0.3149 -0.0099 -0.0231 0.0179  347 PHE A N   
2267 C CA  . PHE A 317 ? 0.2886 0.3496 0.3128 -0.0063 -0.0123 0.0175  347 PHE A CA  
2268 C C   . PHE A 317 ? 0.3031 0.3716 0.3404 -0.0034 -0.0124 0.0189  347 PHE A C   
2269 O O   . PHE A 317 ? 0.3248 0.4007 0.3670 0.0010  -0.0043 0.0178  347 PHE A O   
2270 C CB  . PHE A 317 ? 0.2426 0.2976 0.2534 -0.0016 -0.0066 0.0108  347 PHE A CB  
2271 C CG  . PHE A 317 ? 0.2504 0.2988 0.2488 -0.0033 -0.0060 0.0090  347 PHE A CG  
2272 C CD1 . PHE A 317 ? 0.2106 0.2477 0.1973 -0.0044 -0.0133 0.0066  347 PHE A CD1 
2273 C CD2 . PHE A 317 ? 0.2312 0.2836 0.2282 -0.0029 0.0016  0.0095  347 PHE A CD2 
2274 C CE1 . PHE A 317 ? 0.2348 0.2655 0.2103 -0.0053 -0.0136 0.0047  347 PHE A CE1 
2275 C CE2 . PHE A 317 ? 0.3161 0.3608 0.3003 -0.0040 0.0013  0.0076  347 PHE A CE2 
2276 C CZ  . PHE A 317 ? 0.2252 0.2593 0.1994 -0.0054 -0.0066 0.0052  347 PHE A CZ  
2277 N N   . LEU A 318 ? 0.2361 0.3015 0.2779 -0.0052 -0.0222 0.0210  348 LEU A N   
2278 C CA  . LEU A 318 ? 0.3375 0.4062 0.3877 -0.0012 -0.0239 0.0210  348 LEU A CA  
2279 C C   . LEU A 318 ? 0.4192 0.5051 0.4891 -0.0002 -0.0175 0.0251  348 LEU A C   
2280 O O   . LEU A 318 ? 0.4577 0.5473 0.5305 0.0057  -0.0125 0.0229  348 LEU A O   
2281 C CB  . LEU A 318 ? 0.4073 0.4680 0.4576 -0.0034 -0.0372 0.0228  348 LEU A CB  
2282 C CG  . LEU A 318 ? 0.4416 0.4849 0.4715 -0.0005 -0.0428 0.0181  348 LEU A CG  
2283 C CD1 . LEU A 318 ? 0.4348 0.4693 0.4642 -0.0022 -0.0567 0.0203  348 LEU A CD1 
2284 C CD2 . LEU A 318 ? 0.3366 0.3773 0.3603 0.0060  -0.0371 0.0140  348 LEU A CD2 
2285 N N   . GLY A 319 ? 0.2503 0.3467 0.3339 -0.0055 -0.0175 0.0314  349 GLY A N   
2286 C CA  . GLY A 319 ? 0.4492 0.5642 0.5536 -0.0041 -0.0108 0.0362  349 GLY A CA  
2287 C C   . GLY A 319 ? 0.4904 0.6121 0.6132 -0.0050 -0.0198 0.0402  349 GLY A C   
2288 O O   . GLY A 319 ? 0.5053 0.6170 0.6255 -0.0086 -0.0326 0.0405  349 GLY A O   
2289 N N   . ARG A 320 ? 0.5963 0.7345 0.7372 -0.0008 -0.0135 0.0430  350 ARG A N   
2290 C CA  . ARG A 320 ? 0.5157 0.6646 0.6792 -0.0017 -0.0215 0.0478  350 ARG A CA  
2291 C C   . ARG A 320 ? 0.4579 0.6070 0.6235 0.0071  -0.0219 0.0441  350 ARG A C   
2292 O O   . ARG A 320 ? 0.5226 0.6783 0.7054 0.0072  -0.0304 0.0473  350 ARG A O   
2293 C CB  . ARG A 320 ? 0.5458 0.7180 0.7356 -0.0051 -0.0151 0.0567  350 ARG A CB  
2294 C CG  . ARG A 320 ? 0.5474 0.7197 0.7372 -0.0148 -0.0152 0.0620  350 ARG A CG  
2295 C CD  . ARG A 320 ? 0.6978 0.8945 0.9158 -0.0187 -0.0083 0.0722  350 ARG A CD  
2296 N NE  . ARG A 320 ? 0.7503 0.9593 0.9958 -0.0216 -0.0186 0.0778  350 ARG A NE  
2297 C CZ  . ARG A 320 ? 0.7799 0.9880 1.0380 -0.0319 -0.0319 0.0839  350 ARG A CZ  
2298 N NH1 . ARG A 320 ? 0.8186 1.0139 1.0638 -0.0403 -0.0362 0.0853  350 ARG A NH1 
2299 N NH2 . ARG A 320 ? 0.7014 0.9207 0.9855 -0.0338 -0.0421 0.0885  350 ARG A NH2 
2300 N N   . ALA A 321 ? 0.4801 0.6216 0.6293 0.0142  -0.0141 0.0377  351 ALA A N   
2301 C CA  . ALA A 321 ? 0.4838 0.6216 0.6319 0.0221  -0.0157 0.0340  351 ALA A CA  
2302 C C   . ALA A 321 ? 0.4982 0.6209 0.6387 0.0205  -0.0300 0.0326  351 ALA A C   
2303 O O   . ALA A 321 ? 0.4198 0.5284 0.5446 0.0159  -0.0353 0.0310  351 ALA A O   
2304 C CB  . ALA A 321 ? 0.3805 0.5086 0.5094 0.0284  -0.0066 0.0274  351 ALA A CB  
2305 N N   . PRO A 322 ? 0.4772 0.6015 0.6272 0.0249  -0.0366 0.0332  352 PRO A N   
2306 C CA  . PRO A 322 ? 0.3815 0.4902 0.5231 0.0240  -0.0510 0.0323  352 PRO A CA  
2307 C C   . PRO A 322 ? 0.3679 0.4549 0.4806 0.0262  -0.0504 0.0265  352 PRO A C   
2308 O O   . PRO A 322 ? 0.4262 0.5092 0.5295 0.0316  -0.0425 0.0227  352 PRO A O   
2309 C CB  . PRO A 322 ? 0.4186 0.5339 0.5753 0.0303  -0.0558 0.0334  352 PRO A CB  
2310 C CG  . PRO A 322 ? 0.5215 0.6613 0.7021 0.0323  -0.0456 0.0369  352 PRO A CG  
2311 C CD  . PRO A 322 ? 0.5156 0.6556 0.6840 0.0319  -0.0316 0.0346  352 PRO A CD  
2312 N N   . MET A 323 ? 0.4249 0.4977 0.5237 0.0220  -0.0590 0.0260  353 MET A N   
2313 C CA  . MET A 323 ? 0.3250 0.3780 0.3973 0.0241  -0.0588 0.0215  353 MET A CA  
2314 C C   . MET A 323 ? 0.3324 0.3698 0.3943 0.0237  -0.0733 0.0221  353 MET A C   
2315 O O   . MET A 323 ? 0.3665 0.3944 0.4168 0.0202  -0.0782 0.0217  353 MET A O   
2316 C CB  . MET A 323 ? 0.2815 0.3329 0.3427 0.0207  -0.0507 0.0195  353 MET A CB  
2317 C CG  . MET A 323 ? 0.2700 0.3052 0.3075 0.0234  -0.0479 0.0152  353 MET A CG  
2318 S SD  . MET A 323 ? 0.2951 0.3269 0.3279 0.0300  -0.0404 0.0125  353 MET A SD  
2319 C CE  . MET A 323 ? 0.2174 0.2662 0.2648 0.0301  -0.0288 0.0120  353 MET A CE  
2320 N N   . GLU A 324 ? 0.3644 0.3976 0.4292 0.0281  -0.0811 0.0226  354 GLU A N   
2321 C CA  . GLU A 324 ? 0.4007 0.4171 0.4541 0.0291  -0.0961 0.0229  354 GLU A CA  
2322 C C   . GLU A 324 ? 0.3539 0.3525 0.3867 0.0365  -0.0975 0.0203  354 GLU A C   
2323 O O   . GLU A 324 ? 0.3920 0.3714 0.4046 0.0384  -0.1064 0.0194  354 GLU A O   
2324 C CB  . GLU A 324 ? 0.3851 0.4110 0.4620 0.0269  -0.1088 0.0271  354 GLU A CB  
2325 C CG  . GLU A 324 ? 0.4348 0.4790 0.5346 0.0188  -0.1081 0.0313  354 GLU A CG  
2326 C CD  . GLU A 324 ? 0.5459 0.5785 0.6331 0.0129  -0.1147 0.0315  354 GLU A CD  
2327 O OE1 . GLU A 324 ? 0.5181 0.5291 0.5841 0.0153  -0.1257 0.0292  354 GLU A OE1 
2328 O OE2 . GLU A 324 ? 0.5552 0.5992 0.6523 0.0066  -0.1091 0.0339  354 GLU A OE2 
2329 N N   . THR A 325 ? 0.3164 0.3194 0.3522 0.0409  -0.0892 0.0193  355 THR A N   
2330 C CA  . THR A 325 ? 0.3612 0.3479 0.3800 0.0476  -0.0910 0.0179  355 THR A CA  
2331 C C   . THR A 325 ? 0.3536 0.3347 0.3570 0.0490  -0.0775 0.0156  355 THR A C   
2332 O O   . THR A 325 ? 0.3375 0.3301 0.3476 0.0458  -0.0669 0.0146  355 THR A O   
2333 C CB  . THR A 325 ? 0.4066 0.4007 0.4419 0.0521  -0.0948 0.0190  355 THR A CB  
2334 O OG1 . THR A 325 ? 0.3050 0.3139 0.3528 0.0530  -0.0822 0.0182  355 THR A OG1 
2335 C CG2 . THR A 325 ? 0.4196 0.4251 0.4776 0.0495  -0.1071 0.0220  355 THR A CG2 
2336 N N   . PRO A 326 ? 0.3581 0.3211 0.3406 0.0537  -0.0779 0.0151  356 PRO A N   
2337 C CA  . PRO A 326 ? 0.4183 0.3774 0.3902 0.0545  -0.0654 0.0138  356 PRO A CA  
2338 C C   . PRO A 326 ? 0.3956 0.3664 0.3829 0.0555  -0.0585 0.0130  356 PRO A C   
2339 O O   . PRO A 326 ? 0.3636 0.3370 0.3491 0.0538  -0.0480 0.0116  356 PRO A O   
2340 C CB  . PRO A 326 ? 0.4193 0.3569 0.3681 0.0596  -0.0690 0.0149  356 PRO A CB  
2341 C CG  . PRO A 326 ? 0.4096 0.3374 0.3499 0.0609  -0.0818 0.0156  356 PRO A CG  
2342 C CD  . PRO A 326 ? 0.4025 0.3462 0.3677 0.0580  -0.0897 0.0159  356 PRO A CD  
2343 N N   . ALA A 327 ? 0.3934 0.3711 0.3959 0.0587  -0.0645 0.0137  357 ALA A N   
2344 C CA  . ALA A 327 ? 0.3473 0.3365 0.3640 0.0611  -0.0580 0.0126  357 ALA A CA  
2345 C C   . ALA A 327 ? 0.2929 0.3000 0.3236 0.0568  -0.0496 0.0118  357 ALA A C   
2346 O O   . ALA A 327 ? 0.2982 0.3085 0.3293 0.0575  -0.0403 0.0098  357 ALA A O   
2347 C CB  . ALA A 327 ? 0.3464 0.3410 0.3779 0.0663  -0.0666 0.0138  357 ALA A CB  
2348 N N   . ASP A 328 ? 0.2720 0.2893 0.3131 0.0523  -0.0535 0.0135  358 ASP A N   
2349 C CA  . ASP A 328 ? 0.2683 0.3008 0.3202 0.0479  -0.0456 0.0134  358 ASP A CA  
2350 C C   . ASP A 328 ? 0.2755 0.3009 0.3117 0.0452  -0.0371 0.0107  358 ASP A C   
2351 O O   . ASP A 328 ? 0.2954 0.3281 0.3352 0.0448  -0.0281 0.0090  358 ASP A O   
2352 C CB  . ASP A 328 ? 0.3567 0.3974 0.4194 0.0426  -0.0526 0.0163  358 ASP A CB  
2353 C CG  . ASP A 328 ? 0.3430 0.3932 0.4254 0.0443  -0.0618 0.0196  358 ASP A CG  
2354 O OD1 . ASP A 328 ? 0.2970 0.3565 0.3919 0.0495  -0.0587 0.0196  358 ASP A OD1 
2355 O OD2 . ASP A 328 ? 0.3589 0.4069 0.4445 0.0408  -0.0728 0.0220  358 ASP A OD2 
2356 N N   . TYR A 329 ? 0.2943 0.3052 0.3128 0.0438  -0.0402 0.0105  359 TYR A N   
2357 C CA  . TYR A 329 ? 0.2827 0.2882 0.2884 0.0413  -0.0327 0.0085  359 TYR A CA  
2358 C C   . TYR A 329 ? 0.3048 0.3063 0.3065 0.0436  -0.0252 0.0067  359 TYR A C   
2359 O O   . TYR A 329 ? 0.3214 0.3267 0.3234 0.0415  -0.0179 0.0047  359 TYR A O   
2360 C CB  . TYR A 329 ? 0.2784 0.2696 0.2661 0.0410  -0.0372 0.0091  359 TYR A CB  
2361 C CG  . TYR A 329 ? 0.3301 0.3179 0.3067 0.0386  -0.0299 0.0076  359 TYR A CG  
2362 C CD1 . TYR A 329 ? 0.2484 0.2454 0.2302 0.0346  -0.0265 0.0062  359 TYR A CD1 
2363 C CD2 . TYR A 329 ? 0.3530 0.3288 0.3144 0.0406  -0.0265 0.0080  359 TYR A CD2 
2364 C CE1 . TYR A 329 ? 0.3187 0.3133 0.2917 0.0329  -0.0208 0.0047  359 TYR A CE1 
2365 C CE2 . TYR A 329 ? 0.3039 0.2790 0.2582 0.0386  -0.0198 0.0071  359 TYR A CE2 
2366 C CZ  . TYR A 329 ? 0.3102 0.2949 0.2707 0.0349  -0.0174 0.0051  359 TYR A CZ  
2367 O OH  . TYR A 329 ? 0.2611 0.2459 0.2160 0.0334  -0.0116 0.0040  359 TYR A OH  
2368 N N   . GLN A 330 ? 0.2811 0.2731 0.2780 0.0480  -0.0281 0.0075  360 GLN A N   
2369 C CA  . GLN A 330 ? 0.3311 0.3172 0.3243 0.0501  -0.0226 0.0062  360 GLN A CA  
2370 C C   . GLN A 330 ? 0.3409 0.3388 0.3473 0.0517  -0.0179 0.0039  360 GLN A C   
2371 O O   . GLN A 330 ? 0.3282 0.3240 0.3317 0.0509  -0.0119 0.0017  360 GLN A O   
2372 C CB  . GLN A 330 ? 0.3553 0.3286 0.3414 0.0550  -0.0279 0.0079  360 GLN A CB  
2373 C CG  . GLN A 330 ? 0.4444 0.4125 0.4305 0.0584  -0.0248 0.0066  360 GLN A CG  
2374 C CD  . GLN A 330 ? 0.5620 0.5174 0.5349 0.0557  -0.0195 0.0071  360 GLN A CD  
2375 O OE1 . GLN A 330 ? 0.5155 0.4693 0.4813 0.0512  -0.0163 0.0082  360 GLN A OE1 
2376 N NE2 . GLN A 330 ? 0.6419 0.5884 0.6122 0.0584  -0.0188 0.0066  360 GLN A NE2 
2377 N N   . ALA A 331 ? 0.2556 0.2658 0.2767 0.0541  -0.0208 0.0046  361 ALA A N   
2378 C CA  . ALA A 331 ? 0.3148 0.3369 0.3476 0.0570  -0.0153 0.0029  361 ALA A CA  
2379 C C   . ALA A 331 ? 0.2675 0.2962 0.3001 0.0526  -0.0085 0.0013  361 ALA A C   
2380 O O   . ALA A 331 ? 0.2906 0.3198 0.3220 0.0547  -0.0025 -0.0015 361 ALA A O   
2381 C CB  . ALA A 331 ? 0.2409 0.2775 0.2917 0.0602  -0.0190 0.0052  361 ALA A CB  
2382 N N   . TYR A 332 ? 0.3107 0.3427 0.3427 0.0470  -0.0101 0.0028  362 TYR A N   
2383 C CA  . TYR A 332 ? 0.2957 0.3320 0.3257 0.0429  -0.0046 0.0012  362 TYR A CA  
2384 C C   . TYR A 332 ? 0.3115 0.3367 0.3288 0.0417  -0.0009 -0.0018 362 TYR A C   
2385 O O   . TYR A 332 ? 0.2981 0.3249 0.3144 0.0416  0.0043  -0.0045 362 TYR A O   
2386 C CB  . TYR A 332 ? 0.3270 0.3660 0.3569 0.0374  -0.0086 0.0033  362 TYR A CB  
2387 C CG  . TYR A 332 ? 0.2749 0.3144 0.2987 0.0334  -0.0040 0.0014  362 TYR A CG  
2388 C CD1 . TYR A 332 ? 0.3014 0.3507 0.3315 0.0328  0.0011  0.0010  362 TYR A CD1 
2389 C CD2 . TYR A 332 ? 0.2875 0.3174 0.2990 0.0309  -0.0047 0.0002  362 TYR A CD2 
2390 C CE1 . TYR A 332 ? 0.3239 0.3721 0.3473 0.0295  0.0043  -0.0010 362 TYR A CE1 
2391 C CE2 . TYR A 332 ? 0.2980 0.3286 0.3049 0.0277  -0.0013 -0.0018 362 TYR A CE2 
2392 C CZ  . TYR A 332 ? 0.3583 0.3973 0.3707 0.0270  0.0026  -0.0026 362 TYR A CZ  
2393 O OH  . TYR A 332 ? 0.3785 0.4168 0.3852 0.0243  0.0050  -0.0047 362 TYR A OH  
2394 N N   . LEU A 333 ? 0.3052 0.3190 0.3127 0.0407  -0.0036 -0.0009 363 LEU A N   
2395 C CA  . LEU A 333 ? 0.2952 0.2999 0.2934 0.0387  0.0000  -0.0025 363 LEU A CA  
2396 C C   . LEU A 333 ? 0.2705 0.2711 0.2695 0.0419  0.0026  -0.0049 363 LEU A C   
2397 O O   . LEU A 333 ? 0.2903 0.2889 0.2871 0.0401  0.0060  -0.0075 363 LEU A O   
2398 C CB  . LEU A 333 ? 0.2613 0.2549 0.2494 0.0380  -0.0023 0.0000  363 LEU A CB  
2399 C CG  . LEU A 333 ? 0.3425 0.3363 0.3249 0.0355  -0.0043 0.0015  363 LEU A CG  
2400 C CD1 . LEU A 333 ? 0.3477 0.3296 0.3176 0.0361  -0.0046 0.0042  363 LEU A CD1 
2401 C CD2 . LEU A 333 ? 0.2836 0.2838 0.2671 0.0317  -0.0007 -0.0006 363 LEU A CD2 
2402 N N   . GLU A 334 ? 0.2904 0.2887 0.2921 0.0470  0.0002  -0.0043 364 GLU A N   
2403 C CA  . GLU A 334 ? 0.3311 0.3237 0.3320 0.0513  0.0018  -0.0069 364 GLU A CA  
2404 C C   . GLU A 334 ? 0.3326 0.3340 0.3382 0.0534  0.0060  -0.0101 364 GLU A C   
2405 O O   . GLU A 334 ? 0.3173 0.3124 0.3176 0.0533  0.0081  -0.0133 364 GLU A O   
2406 C CB  . GLU A 334 ? 0.3203 0.3093 0.3232 0.0575  -0.0022 -0.0057 364 GLU A CB  
2407 C CG  . GLU A 334 ? 0.3769 0.3524 0.3706 0.0561  -0.0061 -0.0027 364 GLU A CG  
2408 C CD  . GLU A 334 ? 0.4075 0.3774 0.4017 0.0626  -0.0112 -0.0017 364 GLU A CD  
2409 O OE1 . GLU A 334 ? 0.3447 0.3248 0.3495 0.0681  -0.0123 -0.0027 364 GLU A OE1 
2410 O OE2 . GLU A 334 ? 0.3847 0.3400 0.3686 0.0625  -0.0140 0.0005  364 GLU A OE2 
2411 N N   . ALA A 335 ? 0.3462 0.3619 0.3615 0.0549  0.0071  -0.0090 365 ALA A N   
2412 C CA  . ALA A 335 ? 0.2925 0.3170 0.3113 0.0577  0.0123  -0.0111 365 ALA A CA  
2413 C C   . ALA A 335 ? 0.3254 0.3469 0.3368 0.0529  0.0150  -0.0135 365 ALA A C   
2414 O O   . ALA A 335 ? 0.3422 0.3610 0.3490 0.0561  0.0182  -0.0170 365 ALA A O   
2415 C CB  . ALA A 335 ? 0.2663 0.3077 0.2982 0.0581  0.0133  -0.0077 365 ALA A CB  
2416 N N   . GLN A 336 ? 0.3046 0.3256 0.3139 0.0462  0.0132  -0.0121 366 GLN A N   
2417 C CA  . GLN A 336 ? 0.2763 0.2962 0.2802 0.0421  0.0152  -0.0143 366 GLN A CA  
2418 C C   . GLN A 336 ? 0.3293 0.3371 0.3260 0.0398  0.0140  -0.0167 366 GLN A C   
2419 O O   . GLN A 336 ? 0.3063 0.3109 0.2987 0.0390  0.0151  -0.0200 366 GLN A O   
2420 C CB  . GLN A 336 ? 0.2884 0.3145 0.2938 0.0367  0.0138  -0.0119 366 GLN A CB  
2421 C CG  . GLN A 336 ? 0.2583 0.2829 0.2581 0.0326  0.0148  -0.0141 366 GLN A CG  
2422 C CD  . GLN A 336 ? 0.3576 0.3857 0.3559 0.0346  0.0184  -0.0165 366 GLN A CD  
2423 O OE1 . GLN A 336 ? 0.3150 0.3516 0.3166 0.0340  0.0200  -0.0145 366 GLN A OE1 
2424 N NE2 . GLN A 336 ? 0.2237 0.2440 0.2162 0.0370  0.0194  -0.0205 366 GLN A NE2 
2425 N N   . PHE A 337 ? 0.3389 0.3390 0.3339 0.0387  0.0116  -0.0149 367 PHE A N   
2426 C CA  . PHE A 337 ? 0.3095 0.2999 0.3001 0.0348  0.0109  -0.0155 367 PHE A CA  
2427 C C   . PHE A 337 ? 0.3081 0.2862 0.2959 0.0370  0.0091  -0.0159 367 PHE A C   
2428 O O   . PHE A 337 ? 0.3753 0.3451 0.3611 0.0330  0.0081  -0.0157 367 PHE A O   
2429 C CB  . PHE A 337 ? 0.3145 0.3058 0.3043 0.0301  0.0107  -0.0119 367 PHE A CB  
2430 C CG  . PHE A 337 ? 0.3294 0.3302 0.3202 0.0280  0.0113  -0.0118 367 PHE A CG  
2431 C CD1 . PHE A 337 ? 0.3294 0.3325 0.3199 0.0251  0.0123  -0.0143 367 PHE A CD1 
2432 C CD2 . PHE A 337 ? 0.3239 0.3299 0.3158 0.0290  0.0096  -0.0094 367 PHE A CD2 
2433 C CE1 . PHE A 337 ? 0.3060 0.3160 0.2961 0.0235  0.0122  -0.0143 367 PHE A CE1 
2434 C CE2 . PHE A 337 ? 0.3121 0.3245 0.3039 0.0269  0.0091  -0.0092 367 PHE A CE2 
2435 C CZ  . PHE A 337 ? 0.2666 0.2808 0.2570 0.0242  0.0106  -0.0116 367 PHE A CZ  
2436 N N   . GLY A 338 ? 0.3125 0.2890 0.3006 0.0433  0.0082  -0.0161 368 GLY A N   
2437 C CA  . GLY A 338 ? 0.3502 0.3130 0.3339 0.0462  0.0056  -0.0171 368 GLY A CA  
2438 C C   . GLY A 338 ? 0.3915 0.3444 0.3723 0.0418  0.0038  -0.0130 368 GLY A C   
2439 O O   . GLY A 338 ? 0.3312 0.2866 0.3121 0.0412  0.0036  -0.0091 368 GLY A O   
2440 N N   . ASP A 339 ? 0.4186 0.3594 0.3962 0.0386  0.0021  -0.0136 369 ASP A N   
2441 C CA  . ASP A 339 ? 0.3627 0.2934 0.3377 0.0338  0.0012  -0.0088 369 ASP A CA  
2442 C C   . ASP A 339 ? 0.3864 0.3247 0.3640 0.0273  0.0047  -0.0048 369 ASP A C   
2443 O O   . ASP A 339 ? 0.4644 0.3966 0.4391 0.0242  0.0057  0.0005  369 ASP A O   
2444 C CB  . ASP A 339 ? 0.3739 0.2900 0.3468 0.0310  -0.0022 -0.0101 369 ASP A CB  
2445 C CG  . ASP A 339 ? 0.4889 0.4082 0.4654 0.0275  -0.0026 -0.0139 369 ASP A CG  
2446 O OD1 . ASP A 339 ? 0.4388 0.3658 0.4152 0.0318  -0.0018 -0.0185 369 ASP A OD1 
2447 O OD2 . ASP A 339 ? 0.5381 0.4523 0.5178 0.0202  -0.0039 -0.0119 369 ASP A OD2 
2448 N N   . GLN A 340 ? 0.3287 0.2793 0.3104 0.0257  0.0069  -0.0068 370 GLN A N   
2449 C CA  . GLN A 340 ? 0.3715 0.3298 0.3549 0.0213  0.0102  -0.0037 370 GLN A CA  
2450 C C   . GLN A 340 ? 0.3557 0.3203 0.3360 0.0244  0.0108  -0.0017 370 GLN A C   
2451 O O   . GLN A 340 ? 0.3471 0.3184 0.3271 0.0224  0.0130  -0.0003 370 GLN A O   
2452 C CB  . GLN A 340 ? 0.4057 0.3723 0.3941 0.0183  0.0110  -0.0071 370 GLN A CB  
2453 C CG  . GLN A 340 ? 0.5089 0.4697 0.4988 0.0181  0.0079  -0.0118 370 GLN A CG  
2454 C CD  . GLN A 340 ? 0.5533 0.5044 0.5460 0.0127  0.0060  -0.0098 370 GLN A CD  
2455 O OE1 . GLN A 340 ? 0.5638 0.5132 0.5579 0.0089  0.0083  -0.0041 370 GLN A OE1 
2456 N NE2 . GLN A 340 ? 0.7509 0.6948 0.7440 0.0122  0.0016  -0.0141 370 GLN A NE2 
2457 N N   . ALA A 341 ? 0.3167 0.2790 0.2951 0.0296  0.0082  -0.0019 371 ALA A N   
2458 C CA  . ALA A 341 ? 0.3210 0.2883 0.2976 0.0323  0.0068  -0.0002 371 ALA A CA  
2459 C C   . ALA A 341 ? 0.2659 0.2271 0.2344 0.0309  0.0077  0.0047  371 ALA A C   
2460 O O   . ALA A 341 ? 0.3263 0.2919 0.2917 0.0311  0.0075  0.0057  371 ALA A O   
2461 C CB  . ALA A 341 ? 0.2609 0.2271 0.2392 0.0382  0.0032  -0.0009 371 ALA A CB  
2462 N N   . ALA A 342 ? 0.3087 0.2586 0.2724 0.0299  0.0087  0.0079  372 ALA A N   
2463 C CA  . ALA A 342 ? 0.3622 0.3056 0.3164 0.0292  0.0110  0.0133  372 ALA A CA  
2464 C C   . ALA A 342 ? 0.3608 0.3116 0.3164 0.0252  0.0164  0.0145  372 ALA A C   
2465 O O   . ALA A 342 ? 0.3902 0.3409 0.3377 0.0268  0.0181  0.0172  372 ALA A O   
2466 C CB  . ALA A 342 ? 0.3714 0.3008 0.3205 0.0282  0.0116  0.0173  372 ALA A CB  
2467 N N   . ALA A 343 ? 0.3483 0.3050 0.3135 0.0207  0.0184  0.0124  373 ALA A N   
2468 C CA  . ALA A 343 ? 0.3686 0.3337 0.3372 0.0173  0.0230  0.0133  373 ALA A CA  
2469 C C   . ALA A 343 ? 0.3082 0.2822 0.2751 0.0200  0.0218  0.0103  373 ALA A C   
2470 O O   . ALA A 343 ? 0.3572 0.3340 0.3191 0.0209  0.0247  0.0123  373 ALA A O   
2471 C CB  . ALA A 343 ? 0.3433 0.3119 0.3234 0.0121  0.0234  0.0111  373 ALA A CB  
2472 N N   . VAL A 344 ? 0.3181 0.2960 0.2886 0.0215  0.0176  0.0056  374 VAL A N   
2473 C CA  . VAL A 344 ? 0.3117 0.2967 0.2808 0.0233  0.0155  0.0034  374 VAL A CA  
2474 C C   . VAL A 344 ? 0.3247 0.3047 0.2836 0.0271  0.0130  0.0061  374 VAL A C   
2475 O O   . VAL A 344 ? 0.3133 0.2953 0.2668 0.0284  0.0123  0.0060  374 VAL A O   
2476 C CB  . VAL A 344 ? 0.3413 0.3317 0.3170 0.0238  0.0125  -0.0009 374 VAL A CB  
2477 C CG1 . VAL A 344 ? 0.3229 0.3198 0.2977 0.0246  0.0100  -0.0022 374 VAL A CG1 
2478 C CG2 . VAL A 344 ? 0.3245 0.3173 0.3069 0.0209  0.0141  -0.0041 374 VAL A CG2 
2479 N N   . ALA A 345 ? 0.3499 0.3214 0.3047 0.0296  0.0107  0.0083  375 ALA A N   
2480 C CA  . ALA A 345 ? 0.3554 0.3193 0.2985 0.0338  0.0071  0.0108  375 ALA A CA  
2481 C C   . ALA A 345 ? 0.4098 0.3685 0.3413 0.0347  0.0119  0.0145  375 ALA A C   
2482 O O   . ALA A 345 ? 0.4030 0.3575 0.3231 0.0383  0.0095  0.0153  375 ALA A O   
2483 C CB  . ALA A 345 ? 0.3145 0.2696 0.2555 0.0366  0.0033  0.0124  375 ALA A CB  
2484 N N   . ALA A 346 ? 0.3879 0.3462 0.3218 0.0316  0.0187  0.0172  376 ALA A N   
2485 C CA  . ALA A 346 ? 0.4215 0.3777 0.3467 0.0326  0.0252  0.0215  376 ALA A CA  
2486 C C   . ALA A 346 ? 0.4193 0.3850 0.3456 0.0331  0.0268  0.0191  376 ALA A C   
2487 O O   . ALA A 346 ? 0.4212 0.3838 0.3350 0.0375  0.0290  0.0210  376 ALA A O   
2488 C CB  . ALA A 346 ? 0.4440 0.3999 0.3758 0.0278  0.0320  0.0256  376 ALA A CB  
2489 N N   . CYS A 347 ? 0.3459 0.3220 0.2853 0.0294  0.0255  0.0146  377 CYS A N   
2490 C CA  . CYS A 347 ? 0.3527 0.3368 0.2929 0.0301  0.0258  0.0118  377 CYS A CA  
2491 C C   . CYS A 347 ? 0.3430 0.3238 0.2742 0.0339  0.0186  0.0093  377 CYS A C   
2492 O O   . CYS A 347 ? 0.4130 0.3946 0.3371 0.0368  0.0183  0.0084  377 CYS A O   
2493 C CB  . CYS A 347 ? 0.3898 0.3839 0.3452 0.0251  0.0258  0.0080  377 CYS A CB  
2494 S SG  . CYS A 347 ? 0.6489 0.6532 0.6077 0.0252  0.0280  0.0056  377 CYS A SG  
2495 N N   . TYR A 348 ? 0.3096 0.2866 0.2417 0.0340  0.0124  0.0084  378 TYR A N   
2496 C CA  . TYR A 348 ? 0.3541 0.3288 0.2815 0.0362  0.0043  0.0066  378 TYR A CA  
2497 C C   . TYR A 348 ? 0.3490 0.3133 0.2690 0.0394  -0.0010 0.0088  378 TYR A C   
2498 O O   . TYR A 348 ? 0.3469 0.3131 0.2752 0.0384  -0.0059 0.0080  378 TYR A O   
2499 C CB  . TYR A 348 ? 0.2831 0.2672 0.2237 0.0324  0.0014  0.0032  378 TYR A CB  
2500 C CG  . TYR A 348 ? 0.3294 0.3219 0.2756 0.0297  0.0049  0.0004  378 TYR A CG  
2501 C CD1 . TYR A 348 ? 0.2710 0.2689 0.2266 0.0266  0.0100  -0.0006 378 TYR A CD1 
2502 C CD2 . TYR A 348 ? 0.3225 0.3159 0.2638 0.0304  0.0016  -0.0013 378 TYR A CD2 
2503 C CE1 . TYR A 348 ? 0.3070 0.3118 0.2675 0.0244  0.0119  -0.0033 378 TYR A CE1 
2504 C CE2 . TYR A 348 ? 0.3290 0.3292 0.2748 0.0285  0.0040  -0.0040 378 TYR A CE2 
2505 C CZ  . TYR A 348 ? 0.3255 0.3317 0.2811 0.0256  0.0091  -0.0050 378 TYR A CZ  
2506 O OH  . TYR A 348 ? 0.2826 0.2945 0.2421 0.0240  0.0101  -0.0078 378 TYR A OH  
2507 N N   . PRO A 349 ? 0.3489 0.3021 0.2530 0.0440  -0.0002 0.0118  379 PRO A N   
2508 C CA  . PRO A 349 ? 0.3484 0.2898 0.2440 0.0475  -0.0055 0.0141  379 PRO A CA  
2509 C C   . PRO A 349 ? 0.4056 0.3414 0.2959 0.0501  -0.0170 0.0126  379 PRO A C   
2510 O O   . PRO A 349 ? 0.3794 0.3145 0.2638 0.0512  -0.0205 0.0109  379 PRO A O   
2511 C CB  . PRO A 349 ? 0.4361 0.3667 0.3142 0.0517  0.0006  0.0182  379 PRO A CB  
2512 C CG  . PRO A 349 ? 0.4201 0.3557 0.2940 0.0528  0.0055  0.0174  379 PRO A CG  
2513 C CD  . PRO A 349 ? 0.3294 0.2804 0.2222 0.0468  0.0065  0.0137  379 PRO A CD  
2514 N N   . LEU A 350 ? 0.4009 0.3323 0.2941 0.0511  -0.0238 0.0133  380 LEU A N   
2515 C CA  . LEU A 350 ? 0.4150 0.3382 0.3023 0.0541  -0.0363 0.0130  380 LEU A CA  
2516 C C   . LEU A 350 ? 0.3710 0.2749 0.2341 0.0609  -0.0385 0.0155  380 LEU A C   
2517 O O   . LEU A 350 ? 0.3501 0.2452 0.2090 0.0637  -0.0420 0.0174  380 LEU A O   
2518 C CB  . LEU A 350 ? 0.3544 0.2840 0.2587 0.0524  -0.0427 0.0127  380 LEU A CB  
2519 C CG  . LEU A 350 ? 0.4721 0.4172 0.3965 0.0475  -0.0460 0.0109  380 LEU A CG  
2520 C CD1 . LEU A 350 ? 0.4472 0.3978 0.3870 0.0478  -0.0524 0.0116  380 LEU A CD1 
2521 C CD2 . LEU A 350 ? 0.4241 0.3655 0.3421 0.0469  -0.0538 0.0102  380 LEU A CD2 
2522 N N   . ASP A 351 ? 0.4034 0.3001 0.2492 0.0645  -0.0361 0.0156  381 ASP A N   
2523 C CA  . ASP A 351 ? 0.4522 0.3299 0.2716 0.0721  -0.0360 0.0182  381 ASP A CA  
2524 C C   . ASP A 351 ? 0.4836 0.3459 0.2849 0.0779  -0.0490 0.0166  381 ASP A C   
2525 O O   . ASP A 351 ? 0.5383 0.3833 0.3134 0.0857  -0.0488 0.0181  381 ASP A O   
2526 C CB  . ASP A 351 ? 0.4817 0.3614 0.2924 0.0737  -0.0217 0.0205  381 ASP A CB  
2527 C CG  . ASP A 351 ? 0.4974 0.3863 0.3111 0.0728  -0.0194 0.0175  381 ASP A CG  
2528 O OD1 . ASP A 351 ? 0.5096 0.4006 0.3288 0.0710  -0.0292 0.0140  381 ASP A OD1 
2529 O OD2 . ASP A 351 ? 0.5728 0.4671 0.3842 0.0737  -0.0079 0.0191  381 ASP A OD2 
2530 N N   . GLY A 352 ? 0.4701 0.3372 0.2839 0.0743  -0.0605 0.0138  382 GLY A N   
2531 C CA  . GLY A 352 ? 0.4785 0.3304 0.2771 0.0785  -0.0749 0.0121  382 GLY A CA  
2532 C C   . GLY A 352 ? 0.4980 0.3516 0.2925 0.0781  -0.0754 0.0094  382 GLY A C   
2533 O O   . GLY A 352 ? 0.5163 0.3575 0.3004 0.0803  -0.0890 0.0076  382 GLY A O   
2534 N N   . ARG A 353 ? 0.4697 0.3373 0.2718 0.0754  -0.0621 0.0090  383 ARG A N   
2535 C CA  . ARG A 353 ? 0.5649 0.4343 0.3632 0.0755  -0.0624 0.0063  383 ARG A CA  
2536 C C   . ARG A 353 ? 0.5183 0.3997 0.3384 0.0671  -0.0697 0.0045  383 ARG A C   
2537 O O   . ARG A 353 ? 0.5074 0.3834 0.3212 0.0673  -0.0772 0.0023  383 ARG A O   
2538 C CB  . ARG A 353 ? 0.6614 0.5417 0.4608 0.0761  -0.0461 0.0067  383 ARG A CB  
2539 C CG  . ARG A 353 ? 0.6986 0.5657 0.4710 0.0863  -0.0411 0.0073  383 ARG A CG  
2540 C CD  . ARG A 353 ? 0.6801 0.5582 0.4564 0.0868  -0.0236 0.0104  383 ARG A CD  
2541 N NE  . ARG A 353 ? 0.9085 0.7792 0.6775 0.0889  -0.0193 0.0148  383 ARG A NE  
2542 C CZ  . ARG A 353 ? 0.9703 0.8389 0.7281 0.0937  -0.0068 0.0189  383 ARG A CZ  
2543 N NH1 . ARG A 353 ? 0.9722 0.8480 0.7270 0.0971  0.0036  0.0194  383 ARG A NH1 
2544 N NH2 . ARG A 353 ? 0.8347 0.6937 0.5840 0.0955  -0.0046 0.0232  383 ARG A NH2 
2545 N N   . ALA A 354 ? 0.5213 0.4178 0.3656 0.0601  -0.0676 0.0056  384 ALA A N   
2546 C CA  . ALA A 354 ? 0.4979 0.4074 0.3635 0.0522  -0.0722 0.0049  384 ALA A CA  
2547 C C   . ALA A 354 ? 0.4313 0.3496 0.3168 0.0482  -0.0757 0.0069  384 ALA A C   
2548 O O   . ALA A 354 ? 0.5230 0.4405 0.4086 0.0506  -0.0716 0.0082  384 ALA A O   
2549 C CB  . ALA A 354 ? 0.4690 0.3941 0.3459 0.0479  -0.0607 0.0036  384 ALA A CB  
2550 N N   . THR A 355 ? 0.4753 0.4019 0.3778 0.0422  -0.0833 0.0075  385 THR A N   
2551 C CA  . THR A 355 ? 0.3855 0.3239 0.3104 0.0386  -0.0858 0.0097  385 THR A CA  
2552 C C   . THR A 355 ? 0.3748 0.3313 0.3163 0.0355  -0.0720 0.0095  385 THR A C   
2553 O O   . THR A 355 ? 0.3583 0.3191 0.2968 0.0344  -0.0626 0.0078  385 THR A O   
2554 C CB  . THR A 355 ? 0.4554 0.3983 0.3945 0.0328  -0.0975 0.0113  385 THR A CB  
2555 O OG1 . THR A 355 ? 0.4120 0.3659 0.3594 0.0272  -0.0916 0.0110  385 THR A OG1 
2556 C CG2 . THR A 355 ? 0.4627 0.3849 0.3834 0.0357  -0.1129 0.0109  385 THR A CG2 
2557 N N   . PRO A 356 ? 0.3644 0.3307 0.3228 0.0348  -0.0712 0.0111  386 PRO A N   
2558 C CA  . PRO A 356 ? 0.3150 0.2971 0.2881 0.0326  -0.0593 0.0106  386 PRO A CA  
2559 C C   . PRO A 356 ? 0.3061 0.3001 0.2895 0.0269  -0.0557 0.0103  386 PRO A C   
2560 O O   . PRO A 356 ? 0.2544 0.2544 0.2383 0.0260  -0.0455 0.0085  386 PRO A O   
2561 C CB  . PRO A 356 ? 0.3280 0.3178 0.3177 0.0338  -0.0621 0.0124  386 PRO A CB  
2562 C CG  . PRO A 356 ? 0.3726 0.3511 0.3574 0.0361  -0.0762 0.0140  386 PRO A CG  
2563 C CD  . PRO A 356 ? 0.3229 0.2832 0.2829 0.0383  -0.0801 0.0127  386 PRO A CD  
2564 N N   . LYS A 357 ? 0.2619 0.2585 0.2532 0.0229  -0.0645 0.0124  387 LYS A N   
2565 C CA  . LYS A 357 ? 0.2864 0.2918 0.2848 0.0174  -0.0616 0.0129  387 LYS A CA  
2566 C C   . LYS A 357 ? 0.3107 0.3075 0.2911 0.0181  -0.0577 0.0096  387 LYS A C   
2567 O O   . LYS A 357 ? 0.2827 0.2869 0.2657 0.0160  -0.0494 0.0083  387 LYS A O   
2568 C CB  . LYS A 357 ? 0.2953 0.3017 0.3032 0.0124  -0.0734 0.0164  387 LYS A CB  
2569 C CG  . LYS A 357 ? 0.3797 0.4030 0.4134 0.0094  -0.0739 0.0207  387 LYS A CG  
2570 C CD  . LYS A 357 ? 0.3899 0.4124 0.4336 0.0039  -0.0878 0.0249  387 LYS A CD  
2571 C CE  . LYS A 357 ? 0.5729 0.6154 0.6415 -0.0027 -0.0838 0.0301  387 LYS A CE  
2572 N NZ  . LYS A 357 ? 0.6651 0.7252 0.7534 0.0002  -0.0761 0.0318  387 LYS A NZ  
2573 N N   . GLU A 358 ? 0.3343 0.3151 0.2959 0.0219  -0.0639 0.0083  388 GLU A N   
2574 C CA  . GLU A 358 ? 0.3710 0.3445 0.3161 0.0238  -0.0603 0.0054  388 GLU A CA  
2575 C C   . GLU A 358 ? 0.3120 0.2908 0.2558 0.0260  -0.0473 0.0034  388 GLU A C   
2576 O O   . GLU A 358 ? 0.3434 0.3255 0.2848 0.0250  -0.0416 0.0013  388 GLU A O   
2577 C CB  . GLU A 358 ? 0.3451 0.2999 0.2688 0.0291  -0.0690 0.0046  388 GLU A CB  
2578 C CG  . GLU A 358 ? 0.4014 0.3476 0.3232 0.0265  -0.0836 0.0058  388 GLU A CG  
2579 C CD  . GLU A 358 ? 0.5472 0.4721 0.4462 0.0331  -0.0940 0.0048  388 GLU A CD  
2580 O OE1 . GLU A 358 ? 0.5066 0.4249 0.3939 0.0395  -0.0901 0.0042  388 GLU A OE1 
2581 O OE2 . GLU A 358 ? 0.6093 0.5228 0.5009 0.0321  -0.1065 0.0047  388 GLU A OE2 
2582 N N   . MET A 359 ? 0.2919 0.2713 0.2381 0.0286  -0.0435 0.0041  389 MET A N   
2583 C CA  . MET A 359 ? 0.2773 0.2606 0.2232 0.0298  -0.0324 0.0028  389 MET A CA  
2584 C C   . MET A 359 ? 0.2949 0.2917 0.2559 0.0258  -0.0259 0.0018  389 MET A C   
2585 O O   . MET A 359 ? 0.3532 0.3531 0.3133 0.0252  -0.0189 -0.0003 389 MET A O   
2586 C CB  . MET A 359 ? 0.2822 0.2598 0.2249 0.0335  -0.0311 0.0043  389 MET A CB  
2587 C CG  . MET A 359 ? 0.3741 0.3362 0.2976 0.0387  -0.0357 0.0053  389 MET A CG  
2588 S SD  . MET A 359 ? 0.5207 0.4767 0.4269 0.0416  -0.0311 0.0038  389 MET A SD  
2589 C CE  . MET A 359 ? 0.2638 0.2307 0.1790 0.0393  -0.0175 0.0034  389 MET A CE  
2590 N N   . VAL A 360 ? 0.2514 0.2564 0.2265 0.0237  -0.0282 0.0034  390 VAL A N   
2591 C CA  . VAL A 360 ? 0.2774 0.2941 0.2642 0.0211  -0.0218 0.0026  390 VAL A CA  
2592 C C   . VAL A 360 ? 0.2676 0.2858 0.2513 0.0178  -0.0213 0.0014  390 VAL A C   
2593 O O   . VAL A 360 ? 0.2469 0.2693 0.2315 0.0170  -0.0149 -0.0009 390 VAL A O   
2594 C CB  . VAL A 360 ? 0.2358 0.2621 0.2385 0.0203  -0.0237 0.0053  390 VAL A CB  
2595 C CG1 . VAL A 360 ? 0.2723 0.3101 0.2846 0.0183  -0.0168 0.0050  390 VAL A CG1 
2596 C CG2 . VAL A 360 ? 0.2408 0.2655 0.2463 0.0245  -0.0233 0.0057  390 VAL A CG2 
2597 N N   . ALA A 361 ? 0.2887 0.3016 0.2672 0.0162  -0.0291 0.0026  391 ALA A N   
2598 C CA  . ALA A 361 ? 0.3209 0.3326 0.2940 0.0136  -0.0298 0.0013  391 ALA A CA  
2599 C C   . ALA A 361 ? 0.3136 0.3205 0.2750 0.0165  -0.0252 -0.0023 391 ALA A C   
2600 O O   . ALA A 361 ? 0.2863 0.2964 0.2474 0.0151  -0.0215 -0.0044 391 ALA A O   
2601 C CB  . ALA A 361 ? 0.2863 0.2904 0.2546 0.0118  -0.0407 0.0033  391 ALA A CB  
2602 N N   . ARG A 362 ? 0.2873 0.2867 0.2393 0.0207  -0.0255 -0.0028 392 ARG A N   
2603 C CA  . ARG A 362 ? 0.3014 0.2989 0.2455 0.0235  -0.0198 -0.0052 392 ARG A CA  
2604 C C   . ARG A 362 ? 0.3108 0.3169 0.2644 0.0219  -0.0117 -0.0067 392 ARG A C   
2605 O O   . ARG A 362 ? 0.2520 0.2606 0.2050 0.0213  -0.0087 -0.0092 392 ARG A O   
2606 C CB  . ARG A 362 ? 0.3209 0.3102 0.2547 0.0284  -0.0194 -0.0041 392 ARG A CB  
2607 C CG  . ARG A 362 ? 0.4258 0.4029 0.3455 0.0319  -0.0280 -0.0033 392 ARG A CG  
2608 C CD  . ARG A 362 ? 0.5453 0.5168 0.4515 0.0356  -0.0283 -0.0055 392 ARG A CD  
2609 N NE  . ARG A 362 ? 0.7030 0.6765 0.6115 0.0322  -0.0325 -0.0071 392 ARG A NE  
2610 C CZ  . ARG A 362 ? 0.7885 0.7550 0.6848 0.0353  -0.0362 -0.0092 392 ARG A CZ  
2611 N NH1 . ARG A 362 ? 0.8262 0.7842 0.7071 0.0426  -0.0356 -0.0100 392 ARG A NH1 
2612 N NH2 . ARG A 362 ? 0.6250 0.5925 0.5237 0.0316  -0.0403 -0.0103 392 ARG A NH2 
2613 N N   . ILE A 363 ? 0.2725 0.2816 0.2341 0.0216  -0.0091 -0.0055 393 ILE A N   
2614 C CA  . ILE A 363 ? 0.2707 0.2850 0.2394 0.0206  -0.0028 -0.0072 393 ILE A CA  
2615 C C   . ILE A 363 ? 0.2663 0.2862 0.2392 0.0181  -0.0018 -0.0092 393 ILE A C   
2616 O O   . ILE A 363 ? 0.2592 0.2803 0.2320 0.0176  0.0013  -0.0119 393 ILE A O   
2617 C CB  . ILE A 363 ? 0.2638 0.2787 0.2388 0.0217  -0.0015 -0.0057 393 ILE A CB  
2618 C CG1 . ILE A 363 ? 0.2844 0.2917 0.2529 0.0243  -0.0018 -0.0037 393 ILE A CG1 
2619 C CG2 . ILE A 363 ? 0.2067 0.2249 0.1877 0.0211  0.0035  -0.0079 393 ILE A CG2 
2620 C CD1 . ILE A 363 ? 0.3157 0.3215 0.2888 0.0260  -0.0022 -0.0021 393 ILE A CD1 
2621 N N   . PHE A 364 ? 0.2335 0.2566 0.2104 0.0165  -0.0048 -0.0075 394 PHE A N   
2622 C CA  . PHE A 364 ? 0.2576 0.2854 0.2371 0.0143  -0.0030 -0.0084 394 PHE A CA  
2623 C C   . PHE A 364 ? 0.2621 0.2863 0.2333 0.0134  -0.0047 -0.0107 394 PHE A C   
2624 O O   . PHE A 364 ? 0.2171 0.2423 0.1873 0.0131  -0.0019 -0.0134 394 PHE A O   
2625 C CB  . PHE A 364 ? 0.2201 0.2528 0.2066 0.0122  -0.0056 -0.0046 394 PHE A CB  
2626 C CG  . PHE A 364 ? 0.2449 0.2837 0.2353 0.0108  -0.0014 -0.0042 394 PHE A CG  
2627 C CD1 . PHE A 364 ? 0.2226 0.2593 0.2069 0.0083  -0.0025 -0.0047 394 PHE A CD1 
2628 C CD2 . PHE A 364 ? 0.2239 0.2695 0.2224 0.0128  0.0038  -0.0034 394 PHE A CD2 
2629 C CE1 . PHE A 364 ? 0.2893 0.3303 0.2749 0.0075  0.0020  -0.0039 394 PHE A CE1 
2630 C CE2 . PHE A 364 ? 0.3150 0.3656 0.3149 0.0127  0.0088  -0.0028 394 PHE A CE2 
2631 C CZ  . PHE A 364 ? 0.2921 0.3401 0.2851 0.0098  0.0081  -0.0028 394 PHE A CZ  
2632 N N   . GLY A 365 ? 0.2435 0.2624 0.2078 0.0136  -0.0101 -0.0099 395 GLY A N   
2633 C CA  . GLY A 365 ? 0.2440 0.2589 0.1999 0.0138  -0.0124 -0.0122 395 GLY A CA  
2634 C C   . GLY A 365 ? 0.2788 0.2942 0.2329 0.0162  -0.0085 -0.0156 395 GLY A C   
2635 O O   . GLY A 365 ? 0.2468 0.2624 0.1986 0.0160  -0.0083 -0.0183 395 GLY A O   
2636 N N   . ASP A 366 ? 0.2335 0.2490 0.1890 0.0183  -0.0055 -0.0150 396 ASP A N   
2637 C CA  . ASP A 366 ? 0.2663 0.2840 0.2236 0.0197  -0.0014 -0.0171 396 ASP A CA  
2638 C C   . ASP A 366 ? 0.2568 0.2783 0.2213 0.0175  0.0013  -0.0194 396 ASP A C   
2639 O O   . ASP A 366 ? 0.2489 0.2718 0.2141 0.0174  0.0014  -0.0222 396 ASP A O   
2640 C CB  . ASP A 366 ? 0.2339 0.2507 0.1917 0.0216  0.0019  -0.0147 396 ASP A CB  
2641 C CG  . ASP A 366 ? 0.2453 0.2568 0.1925 0.0256  0.0000  -0.0133 396 ASP A CG  
2642 O OD1 . ASP A 366 ? 0.2802 0.2884 0.2198 0.0270  -0.0046 -0.0146 396 ASP A OD1 
2643 O OD2 . ASP A 366 ? 0.2856 0.2947 0.2303 0.0279  0.0028  -0.0108 396 ASP A OD2 
2644 N N   . ASN A 367 ? 0.1970 0.2195 0.1663 0.0164  0.0029  -0.0184 397 ASN A N   
2645 C CA  . ASN A 367 ? 0.2262 0.2496 0.1997 0.0157  0.0052  -0.0209 397 ASN A CA  
2646 C C   . ASN A 367 ? 0.2629 0.2861 0.2326 0.0151  0.0037  -0.0232 397 ASN A C   
2647 O O   . ASN A 367 ? 0.2863 0.3081 0.2557 0.0151  0.0036  -0.0266 397 ASN A O   
2648 C CB  . ASN A 367 ? 0.2752 0.2988 0.2530 0.0163  0.0074  -0.0194 397 ASN A CB  
2649 C CG  . ASN A 367 ? 0.2955 0.3177 0.2747 0.0168  0.0090  -0.0224 397 ASN A CG  
2650 O OD1 . ASN A 367 ? 0.2915 0.3144 0.2681 0.0175  0.0096  -0.0233 397 ASN A OD1 
2651 N ND2 . ASN A 367 ? 0.2889 0.3080 0.2711 0.0167  0.0097  -0.0237 397 ASN A ND2 
2652 N N   . GLN A 368 ? 0.2078 0.2312 0.1741 0.0143  0.0019  -0.0212 398 GLN A N   
2653 C CA  . GLN A 368 ? 0.2676 0.2901 0.2295 0.0134  0.0014  -0.0221 398 GLN A CA  
2654 C C   . GLN A 368 ? 0.2509 0.2698 0.2054 0.0130  -0.0028 -0.0236 398 GLN A C   
2655 O O   . GLN A 368 ? 0.2865 0.3026 0.2354 0.0127  -0.0035 -0.0251 398 GLN A O   
2656 C CB  . GLN A 368 ? 0.2362 0.2618 0.2005 0.0121  0.0025  -0.0179 398 GLN A CB  
2657 C CG  . GLN A 368 ? 0.2987 0.3285 0.2698 0.0138  0.0071  -0.0168 398 GLN A CG  
2658 C CD  . GLN A 368 ? 0.3172 0.3452 0.2848 0.0161  0.0108  -0.0199 398 GLN A CD  
2659 O OE1 . GLN A 368 ? 0.2838 0.3130 0.2483 0.0164  0.0133  -0.0186 398 GLN A OE1 
2660 N NE2 . GLN A 368 ? 0.2973 0.3215 0.2647 0.0179  0.0110  -0.0237 398 GLN A NE2 
2661 N N   . PHE A 369 ? 0.2145 0.2158 0.2567 0.0383  -0.0474 0.0142  399 PHE A N   
2662 C CA  . PHE A 369 ? 0.2097 0.2166 0.2452 0.0331  -0.0406 0.0121  399 PHE A CA  
2663 C C   . PHE A 369 ? 0.2113 0.2099 0.2376 0.0273  -0.0362 0.0174  399 PHE A C   
2664 O O   . PHE A 369 ? 0.2069 0.2055 0.2351 0.0246  -0.0308 0.0146  399 PHE A O   
2665 C CB  . PHE A 369 ? 0.2019 0.2182 0.2315 0.0323  -0.0413 0.0114  399 PHE A CB  
2666 C CG  . PHE A 369 ? 0.1944 0.2217 0.2337 0.0369  -0.0440 0.0055  399 PHE A CG  
2667 C CD1 . PHE A 369 ? 0.1823 0.2180 0.2272 0.0369  -0.0396 -0.0009 399 PHE A CD1 
2668 C CD2 . PHE A 369 ? 0.2004 0.2304 0.2432 0.0412  -0.0509 0.0067  399 PHE A CD2 
2669 C CE1 . PHE A 369 ? 0.1763 0.2234 0.2298 0.0405  -0.0413 -0.0061 399 PHE A CE1 
2670 C CE2 . PHE A 369 ? 0.2112 0.2531 0.2641 0.0453  -0.0529 0.0008  399 PHE A CE2 
2671 C CZ  . PHE A 369 ? 0.1816 0.2322 0.2396 0.0446  -0.0476 -0.0056 399 PHE A CZ  
2672 N N   . ASN A 370 ? 0.2242 0.2166 0.2407 0.0252  -0.0385 0.0250  400 ASN A N   
2673 C CA  . ASN A 370 ? 0.2589 0.2469 0.2648 0.0189  -0.0332 0.0296  400 ASN A CA  
2674 C C   . ASN A 370 ? 0.2332 0.2127 0.2442 0.0166  -0.0301 0.0313  400 ASN A C   
2675 O O   . ASN A 370 ? 0.2332 0.2133 0.2413 0.0119  -0.0236 0.0307  400 ASN A O   
2676 C CB  . ASN A 370 ? 0.2449 0.2293 0.2378 0.0172  -0.0365 0.0376  400 ASN A CB  
2677 C CG  . ASN A 370 ? 0.3478 0.3417 0.3347 0.0180  -0.0388 0.0351  400 ASN A CG  
2678 O OD1 . ASN A 370 ? 0.3259 0.3277 0.3128 0.0164  -0.0347 0.0289  400 ASN A OD1 
2679 N ND2 . ASN A 370 ? 0.2590 0.2520 0.2415 0.0205  -0.0460 0.0398  400 ASN A ND2 
2680 N N   . ARG A 371 ? 0.2397 0.2112 0.2593 0.0199  -0.0348 0.0330  401 ARG A N   
2681 C CA  . ARG A 371 ? 0.2613 0.2240 0.2874 0.0174  -0.0324 0.0342  401 ARG A CA  
2682 C C   . ARG A 371 ? 0.2879 0.2572 0.3228 0.0172  -0.0278 0.0253  401 ARG A C   
2683 O O   . ARG A 371 ? 0.2288 0.1966 0.2643 0.0124  -0.0225 0.0253  401 ARG A O   
2684 C CB  . ARG A 371 ? 0.2548 0.2070 0.2897 0.0217  -0.0393 0.0368  401 ARG A CB  
2685 C CG  . ARG A 371 ? 0.3423 0.2832 0.3836 0.0180  -0.0375 0.0393  401 ARG A CG  
2686 C CD  . ARG A 371 ? 0.3540 0.2837 0.4064 0.0229  -0.0445 0.0402  401 ARG A CD  
2687 N NE  . ARG A 371 ? 0.4008 0.3367 0.4666 0.0290  -0.0465 0.0290  401 ARG A NE  
2688 C CZ  . ARG A 371 ? 0.3885 0.3293 0.4591 0.0363  -0.0519 0.0249  401 ARG A CZ  
2689 N NH1 . ARG A 371 ? 0.3461 0.2858 0.4104 0.0390  -0.0569 0.0311  401 ARG A NH1 
2690 N NH2 . ARG A 371 ? 0.4072 0.3551 0.4891 0.0411  -0.0524 0.0141  401 ARG A NH2 
2691 N N   . GLY A 372 ? 0.2465 0.2240 0.2885 0.0223  -0.0298 0.0177  402 GLY A N   
2692 C CA  . GLY A 372 ? 0.2056 0.1901 0.2545 0.0225  -0.0260 0.0097  402 GLY A CA  
2693 C C   . GLY A 372 ? 0.1979 0.1892 0.2396 0.0184  -0.0198 0.0088  402 GLY A C   
2694 O O   . GLY A 372 ? 0.2175 0.2110 0.2631 0.0164  -0.0158 0.0054  402 GLY A O   
2695 N N   . VAL A 373 ? 0.2041 0.1989 0.2358 0.0173  -0.0193 0.0116  403 VAL A N   
2696 C CA  . VAL A 373 ? 0.1927 0.1929 0.2180 0.0136  -0.0136 0.0104  403 VAL A CA  
2697 C C   . VAL A 373 ? 0.2421 0.2372 0.2638 0.0083  -0.0090 0.0142  403 VAL A C   
2698 O O   . VAL A 373 ? 0.2226 0.2214 0.2461 0.0061  -0.0040 0.0111  403 VAL A O   
2699 C CB  . VAL A 373 ? 0.2164 0.2210 0.2326 0.0135  -0.0147 0.0115  403 VAL A CB  
2700 C CG1 . VAL A 373 ? 0.1990 0.2060 0.2071 0.0091  -0.0089 0.0114  403 VAL A CG1 
2701 C CG2 . VAL A 373 ? 0.1884 0.2011 0.2099 0.0175  -0.0170 0.0063  403 VAL A CG2 
2702 N N   . SER A 374 ? 0.2160 0.2029 0.2327 0.0061  -0.0105 0.0214  404 SER A N   
2703 C CA  . SER A 374 ? 0.2776 0.2601 0.2917 0.0004  -0.0056 0.0255  404 SER A CA  
2704 C C   . SER A 374 ? 0.2575 0.2388 0.2842 -0.0004 -0.0037 0.0218  404 SER A C   
2705 O O   . SER A 374 ? 0.2551 0.2397 0.2833 -0.0042 0.0020  0.0202  404 SER A O   
2706 C CB  . SER A 374 ? 0.2833 0.2564 0.2903 -0.0018 -0.0082 0.0350  404 SER A CB  
2707 O OG  . SER A 374 ? 0.4579 0.4332 0.4518 -0.0018 -0.0098 0.0383  404 SER A OG  
2708 N N   . ALA A 375 ? 0.2158 0.1931 0.2523 0.0035  -0.0087 0.0196  405 ALA A N   
2709 C CA  . ALA A 375 ? 0.2135 0.1892 0.2622 0.0027  -0.0078 0.0154  405 ALA A CA  
2710 C C   . ALA A 375 ? 0.1993 0.1857 0.2523 0.0036  -0.0045 0.0075  405 ALA A C   
2711 O O   . ALA A 375 ? 0.1977 0.1861 0.2561 0.0002  -0.0007 0.0055  405 ALA A O   
2712 C CB  . ALA A 375 ? 0.2163 0.1862 0.2744 0.0074  -0.0143 0.0132  405 ALA A CB  
2713 N N   . PHE A 376 ? 0.1897 0.1836 0.2407 0.0080  -0.0060 0.0034  406 PHE A N   
2714 C CA  . PHE A 376 ? 0.1900 0.1933 0.2439 0.0091  -0.0033 -0.0029 406 PHE A CA  
2715 C C   . PHE A 376 ? 0.2188 0.2255 0.2672 0.0051  0.0025  -0.0015 406 PHE A C   
2716 O O   . PHE A 376 ? 0.2170 0.2287 0.2708 0.0044  0.0054  -0.0053 406 PHE A O   
2717 C CB  . PHE A 376 ? 0.1702 0.1801 0.2224 0.0139  -0.0058 -0.0062 406 PHE A CB  
2718 C CG  . PHE A 376 ? 0.1922 0.2055 0.2532 0.0183  -0.0091 -0.0123 406 PHE A CG  
2719 C CD1 . PHE A 376 ? 0.1721 0.1805 0.2382 0.0211  -0.0137 -0.0128 406 PHE A CD1 
2720 C CD2 . PHE A 376 ? 0.1904 0.2121 0.2543 0.0199  -0.0078 -0.0176 406 PHE A CD2 
2721 C CE1 . PHE A 376 ? 0.2432 0.2557 0.3172 0.0254  -0.0165 -0.0197 406 PHE A CE1 
2722 C CE2 . PHE A 376 ? 0.1721 0.1982 0.2426 0.0238  -0.0106 -0.0236 406 PHE A CE2 
2723 C CZ  . PHE A 376 ? 0.1745 0.1964 0.2501 0.0265  -0.0147 -0.0252 406 PHE A CZ  
2724 N N   . SER A 377 ? 0.1826 0.1874 0.2206 0.0029  0.0041  0.0034  407 SER A N   
2725 C CA  . SER A 377 ? 0.2212 0.2294 0.2540 -0.0007 0.0099  0.0038  407 SER A CA  
2726 C C   . SER A 377 ? 0.2194 0.2264 0.2576 -0.0052 0.0141  0.0047  407 SER A C   
2727 O O   . SER A 377 ? 0.2393 0.2524 0.2819 -0.0062 0.0182  0.0010  407 SER A O   
2728 C CB  . SER A 377 ? 0.2330 0.2392 0.2530 -0.0025 0.0105  0.0084  407 SER A CB  
2729 O OG  . SER A 377 ? 0.2523 0.2608 0.2686 0.0011  0.0068  0.0070  407 SER A OG  
2730 N N   . GLU A 378 ? 0.2302 0.2294 0.2688 -0.0080 0.0129  0.0100  408 GLU A N   
2731 C CA  . GLU A 378 ? 0.2139 0.2117 0.2586 -0.0133 0.0170  0.0116  408 GLU A CA  
2732 C C   . GLU A 378 ? 0.2517 0.2538 0.3105 -0.0120 0.0165  0.0047  408 GLU A C   
2733 O O   . GLU A 378 ? 0.2557 0.2634 0.3203 -0.0151 0.0211  0.0024  408 GLU A O   
2734 C CB  . GLU A 378 ? 0.2583 0.2450 0.3015 -0.0165 0.0150  0.0192  408 GLU A CB  
2735 C CG  . GLU A 378 ? 0.3157 0.2990 0.3439 -0.0189 0.0161  0.0270  408 GLU A CG  
2736 C CD  . GLU A 378 ? 0.4777 0.4678 0.4991 -0.0238 0.0241  0.0276  408 GLU A CD  
2737 O OE1 . GLU A 378 ? 0.5815 0.5755 0.6113 -0.0275 0.0290  0.0255  408 GLU A OE1 
2738 O OE2 . GLU A 378 ? 0.5460 0.5383 0.5545 -0.0238 0.0252  0.0296  408 GLU A OE2 
2739 N N   . ALA A 379 ? 0.1942 0.1951 0.2589 -0.0072 0.0108  0.0009  409 ALA A N   
2740 C CA  . ALA A 379 ? 0.2659 0.2715 0.3430 -0.0058 0.0096  -0.0061 409 ALA A CA  
2741 C C   . ALA A 379 ? 0.2161 0.2327 0.2938 -0.0037 0.0121  -0.0111 409 ALA A C   
2742 O O   . ALA A 379 ? 0.1837 0.2060 0.2704 -0.0047 0.0135  -0.0154 409 ALA A O   
2743 C CB  . ALA A 379 ? 0.1941 0.1969 0.2760 -0.0009 0.0032  -0.0097 409 ALA A CB  
2744 N N   . LEU A 380 ? 0.1902 0.2096 0.2589 -0.0008 0.0123  -0.0107 410 LEU A N   
2745 C CA  . LEU A 380 ? 0.2256 0.2535 0.2946 0.0014  0.0143  -0.0146 410 LEU A CA  
2746 C C   . LEU A 380 ? 0.2125 0.2438 0.2824 -0.0025 0.0204  -0.0141 410 LEU A C   
2747 O O   . LEU A 380 ? 0.1816 0.2201 0.2584 -0.0015 0.0219  -0.0183 410 LEU A O   
2748 C CB  . LEU A 380 ? 0.1794 0.2080 0.2392 0.0047  0.0131  -0.0138 410 LEU A CB  
2749 C CG  . LEU A 380 ? 0.2243 0.2538 0.2850 0.0093  0.0079  -0.0160 410 LEU A CG  
2750 C CD1 . LEU A 380 ? 0.1681 0.1977 0.2199 0.0110  0.0072  -0.0142 410 LEU A CD1 
2751 C CD2 . LEU A 380 ? 0.1740 0.2106 0.2417 0.0123  0.0066  -0.0212 410 LEU A CD2 
2752 N N   . VAL A 381 ? 0.1847 0.2118 0.2475 -0.0068 0.0239  -0.0091 411 VAL A N   
2753 C CA  . VAL A 381 ? 0.1746 0.2060 0.2391 -0.0112 0.0304  -0.0089 411 VAL A CA  
2754 C C   . VAL A 381 ? 0.2098 0.2439 0.2877 -0.0140 0.0313  -0.0111 411 VAL A C   
2755 O O   . VAL A 381 ? 0.1716 0.2141 0.2573 -0.0145 0.0347  -0.0151 411 VAL A O   
2756 C CB  . VAL A 381 ? 0.2537 0.2803 0.3069 -0.0158 0.0339  -0.0025 411 VAL A CB  
2757 C CG1 . VAL A 381 ? 0.2240 0.2559 0.2799 -0.0212 0.0414  -0.0023 411 VAL A CG1 
2758 C CG2 . VAL A 381 ? 0.2248 0.2508 0.2655 -0.0132 0.0334  -0.0020 411 VAL A CG2 
2759 N N   . ARG A 382 ? 0.2114 0.2386 0.2934 -0.0156 0.0278  -0.0090 412 ARG A N   
2760 C CA  . ARG A 382 ? 0.2557 0.2843 0.3511 -0.0193 0.0284  -0.0111 412 ARG A CA  
2761 C C   . ARG A 382 ? 0.2359 0.2735 0.3423 -0.0154 0.0257  -0.0191 412 ARG A C   
2762 O O   . ARG A 382 ? 0.2607 0.3044 0.3787 -0.0183 0.0278  -0.0223 412 ARG A O   
2763 C CB  . ARG A 382 ? 0.2302 0.2477 0.3277 -0.0210 0.0241  -0.0078 412 ARG A CB  
2764 C CG  . ARG A 382 ? 0.3849 0.3991 0.4916 -0.0284 0.0269  -0.0053 412 ARG A CG  
2765 C CD  . ARG A 382 ? 0.4364 0.4363 0.5406 -0.0306 0.0237  0.0013  412 ARG A CD  
2766 N NE  . ARG A 382 ? 0.5623 0.5572 0.6720 -0.0254 0.0161  -0.0031 412 ARG A NE  
2767 C CZ  . ARG A 382 ? 0.5644 0.5534 0.6666 -0.0202 0.0113  -0.0016 412 ARG A CZ  
2768 N NH1 . ARG A 382 ? 0.3642 0.3507 0.4526 -0.0195 0.0124  0.0047  412 ARG A NH1 
2769 N NH2 . ARG A 382 ? 0.5501 0.5366 0.6590 -0.0155 0.0051  -0.0071 412 ARG A NH2 
2770 N N   . GLN A 383 ? 0.2245 0.2637 0.3274 -0.0090 0.0212  -0.0221 413 GLN A N   
2771 C CA  . GLN A 383 ? 0.2578 0.3055 0.3691 -0.0048 0.0179  -0.0289 413 GLN A CA  
2772 C C   . GLN A 383 ? 0.2665 0.3230 0.3775 -0.0023 0.0207  -0.0310 413 GLN A C   
2773 O O   . GLN A 383 ? 0.2429 0.3064 0.3590 0.0019  0.0175  -0.0356 413 GLN A O   
2774 C CB  . GLN A 383 ? 0.1711 0.2167 0.2787 0.0006  0.0118  -0.0309 413 GLN A CB  
2775 C CG  . GLN A 383 ? 0.1963 0.2349 0.3086 -0.0004 0.0079  -0.0317 413 GLN A CG  
2776 C CD  . GLN A 383 ? 0.2738 0.3155 0.4001 -0.0034 0.0070  -0.0365 413 GLN A CD  
2777 O OE1 . GLN A 383 ? 0.2835 0.3347 0.4162 -0.0010 0.0052  -0.0424 413 GLN A OE1 
2778 N NE2 . GLN A 383 ? 0.2281 0.2619 0.3594 -0.0089 0.0080  -0.0339 413 GLN A NE2 
2779 N N   . GLY A 384 ? 0.1616 0.2179 0.2667 -0.0045 0.0262  -0.0279 414 GLY A N   
2780 C CA  . GLY A 384 ? 0.1941 0.2579 0.3002 -0.0018 0.0289  -0.0305 414 GLY A CA  
2781 C C   . GLY A 384 ? 0.1936 0.2561 0.2913 0.0038  0.0261  -0.0305 414 GLY A C   
2782 O O   . GLY A 384 ? 0.2258 0.2938 0.3262 0.0073  0.0265  -0.0331 414 GLY A O   
2783 N N   . ALA A 385 ? 0.1882 0.2437 0.2767 0.0047  0.0233  -0.0274 415 ALA A N   
2784 C CA  . ALA A 385 ? 0.2259 0.2805 0.3071 0.0091  0.0210  -0.0270 415 ALA A CA  
2785 C C   . ALA A 385 ? 0.1512 0.2038 0.2248 0.0082  0.0252  -0.0255 415 ALA A C   
2786 O O   . ALA A 385 ? 0.1499 0.2001 0.2195 0.0041  0.0292  -0.0234 415 ALA A O   
2787 C CB  . ALA A 385 ? 0.1749 0.2242 0.2501 0.0101  0.0169  -0.0249 415 ALA A CB  
2788 N N   . PRO A 386 ? 0.1704 0.2241 0.2418 0.0119  0.0244  -0.0266 416 PRO A N   
2789 C CA  . PRO A 386 ? 0.1700 0.2202 0.2331 0.0113  0.0272  -0.0256 416 PRO A CA  
2790 C C   . PRO A 386 ? 0.2302 0.2745 0.2835 0.0102  0.0249  -0.0222 416 PRO A C   
2791 O O   . PRO A 386 ? 0.1546 0.1981 0.2064 0.0128  0.0210  -0.0215 416 PRO A O   
2792 C CB  . PRO A 386 ? 0.1930 0.2450 0.2587 0.0158  0.0259  -0.0277 416 PRO A CB  
2793 C CG  . PRO A 386 ? 0.1988 0.2566 0.2742 0.0187  0.0229  -0.0295 416 PRO A CG  
2794 C CD  . PRO A 386 ? 0.1367 0.1944 0.2129 0.0167  0.0207  -0.0285 416 PRO A CD  
2795 N N   . VAL A 387 ? 0.1951 0.2361 0.2418 0.0064  0.0271  -0.0199 417 VAL A N   
2796 C CA  . VAL A 387 ? 0.2043 0.2403 0.2430 0.0056  0.0242  -0.0164 417 VAL A CA  
2797 C C   . VAL A 387 ? 0.2153 0.2489 0.2440 0.0031  0.0267  -0.0153 417 VAL A C   
2798 O O   . VAL A 387 ? 0.2305 0.2651 0.2570 0.0001  0.0313  -0.0154 417 VAL A O   
2799 C CB  . VAL A 387 ? 0.2100 0.2434 0.2508 0.0038  0.0223  -0.0136 417 VAL A CB  
2800 C CG1 . VAL A 387 ? 0.2317 0.2655 0.2744 -0.0005 0.0270  -0.0126 417 VAL A CG1 
2801 C CG2 . VAL A 387 ? 0.1883 0.2168 0.2214 0.0035  0.0189  -0.0100 417 VAL A CG2 
2802 N N   . TRP A 388 ? 0.2378 0.2692 0.2604 0.0042  0.0238  -0.0147 418 TRP A N   
2803 C CA  . TRP A 388 ? 0.2309 0.2602 0.2434 0.0020  0.0247  -0.0141 418 TRP A CA  
2804 C C   . TRP A 388 ? 0.2283 0.2549 0.2354 0.0016  0.0201  -0.0103 418 TRP A C   
2805 O O   . TRP A 388 ? 0.2235 0.2503 0.2351 0.0040  0.0161  -0.0096 418 TRP A O   
2806 C CB  . TRP A 388 ? 0.1845 0.2141 0.1960 0.0033  0.0252  -0.0179 418 TRP A CB  
2807 C CG  . TRP A 388 ? 0.2419 0.2737 0.2583 0.0042  0.0296  -0.0221 418 TRP A CG  
2808 C CD1 . TRP A 388 ? 0.1929 0.2255 0.2053 0.0026  0.0341  -0.0254 418 TRP A CD1 
2809 C CD2 . TRP A 388 ? 0.2306 0.2649 0.2572 0.0073  0.0298  -0.0238 418 TRP A CD2 
2810 N NE1 . TRP A 388 ? 0.2083 0.2436 0.2290 0.0048  0.0371  -0.0294 418 TRP A NE1 
2811 C CE2 . TRP A 388 ? 0.1922 0.2284 0.2216 0.0078  0.0342  -0.0281 418 TRP A CE2 
2812 C CE3 . TRP A 388 ? 0.2161 0.2517 0.2495 0.0100  0.0264  -0.0225 418 TRP A CE3 
2813 C CZ2 . TRP A 388 ? 0.1977 0.2369 0.2373 0.0111  0.0348  -0.0306 418 TRP A CZ2 
2814 C CZ3 . TRP A 388 ? 0.2577 0.2964 0.2997 0.0130  0.0269  -0.0248 418 TRP A CZ3 
2815 C CH2 . TRP A 388 ? 0.1938 0.2341 0.2393 0.0136  0.0308  -0.0286 418 TRP A CH2 
2816 N N   . ARG A 389 ? 0.1972 0.2221 0.1946 -0.0011 0.0204  -0.0082 419 ARG A N   
2817 C CA  . ARG A 389 ? 0.2543 0.2768 0.2465 -0.0011 0.0155  -0.0042 419 ARG A CA  
2818 C C   . ARG A 389 ? 0.2418 0.2648 0.2242 -0.0024 0.0144  -0.0051 419 ARG A C   
2819 O O   . ARG A 389 ? 0.2498 0.2737 0.2263 -0.0046 0.0183  -0.0076 419 ARG A O   
2820 C CB  . ARG A 389 ? 0.2832 0.3022 0.2729 -0.0032 0.0155  0.0012  419 ARG A CB  
2821 C CG  . ARG A 389 ? 0.2313 0.2469 0.2175 -0.0022 0.0095  0.0059  419 ARG A CG  
2822 C CD  . ARG A 389 ? 0.2805 0.2908 0.2660 -0.0042 0.0095  0.0118  419 ARG A CD  
2823 N NE  . ARG A 389 ? 0.3698 0.3760 0.3523 -0.0026 0.0032  0.0167  419 ARG A NE  
2824 C CZ  . ARG A 389 ? 0.3153 0.3149 0.2975 -0.0037 0.0015  0.0228  419 ARG A CZ  
2825 N NH1 . ARG A 389 ? 0.2429 0.2397 0.2280 -0.0071 0.0059  0.0248  419 ARG A NH1 
2826 N NH2 . ARG A 389 ? 0.3146 0.3103 0.2946 -0.0014 -0.0050 0.0271  419 ARG A NH2 
2827 N N   . TYR A 390 ? 0.2558 0.2789 0.2372 -0.0011 0.0089  -0.0037 420 TYR A N   
2828 C CA  . TYR A 390 ? 0.2401 0.2645 0.2133 -0.0023 0.0065  -0.0048 420 TYR A CA  
2829 C C   . TYR A 390 ? 0.2400 0.2638 0.2093 -0.0016 0.0005  -0.0001 420 TYR A C   
2830 O O   . TYR A 390 ? 0.2483 0.2709 0.2239 0.0009  -0.0027 0.0027  420 TYR A O   
2831 C CB  . TYR A 390 ? 0.1996 0.2265 0.1776 -0.0014 0.0056  -0.0095 420 TYR A CB  
2832 C CG  . TYR A 390 ? 0.2510 0.2802 0.2366 0.0012  0.0012  -0.0085 420 TYR A CG  
2833 C CD1 . TYR A 390 ? 0.1842 0.2159 0.1678 0.0014  -0.0041 -0.0074 420 TYR A CD1 
2834 C CD2 . TYR A 390 ? 0.2064 0.2364 0.2013 0.0035  0.0022  -0.0089 420 TYR A CD2 
2835 C CE1 . TYR A 390 ? 0.1997 0.2350 0.1911 0.0038  -0.0075 -0.0071 420 TYR A CE1 
2836 C CE2 . TYR A 390 ? 0.1963 0.2298 0.1975 0.0058  -0.0012 -0.0086 420 TYR A CE2 
2837 C CZ  . TYR A 390 ? 0.1869 0.2232 0.1868 0.0060  -0.0058 -0.0078 420 TYR A CZ  
2838 O OH  . TYR A 390 ? 0.1752 0.2166 0.1823 0.0084  -0.0086 -0.0081 420 TYR A OH  
2839 N N   . GLN A 391 ? 0.2397 0.2647 0.1988 -0.0035 -0.0016 0.0000  421 GLN A N   
2840 C CA  . GLN A 391 ? 0.2576 0.2838 0.2135 -0.0023 -0.0085 0.0031  421 GLN A CA  
2841 C C   . GLN A 391 ? 0.2786 0.3095 0.2318 -0.0034 -0.0109 -0.0018 421 GLN A C   
2842 O O   . GLN A 391 ? 0.2457 0.2773 0.1909 -0.0062 -0.0082 -0.0053 421 GLN A O   
2843 C CB  . GLN A 391 ? 0.2598 0.2828 0.2045 -0.0037 -0.0100 0.0095  421 GLN A CB  
2844 C CG  . GLN A 391 ? 0.3266 0.3493 0.2711 -0.0010 -0.0180 0.0143  421 GLN A CG  
2845 C CD  . GLN A 391 ? 0.4736 0.4910 0.4084 -0.0019 -0.0196 0.0225  421 GLN A CD  
2846 O OE1 . GLN A 391 ? 0.5701 0.5818 0.5102 -0.0007 -0.0198 0.0273  421 GLN A OE1 
2847 N NE2 . GLN A 391 ? 0.4719 0.4910 0.3923 -0.0044 -0.0209 0.0242  421 GLN A NE2 
2848 N N   . PHE A 392 ? 0.2367 0.2713 0.1973 -0.0013 -0.0158 -0.0026 422 PHE A N   
2849 C CA  . PHE A 392 ? 0.2106 0.2504 0.1715 -0.0027 -0.0186 -0.0072 422 PHE A CA  
2850 C C   . PHE A 392 ? 0.2295 0.2724 0.1835 -0.0023 -0.0257 -0.0046 422 PHE A C   
2851 O O   . PHE A 392 ? 0.2188 0.2640 0.1787 0.0008  -0.0309 -0.0017 422 PHE A O   
2852 C CB  . PHE A 392 ? 0.1987 0.2421 0.1727 -0.0012 -0.0191 -0.0096 422 PHE A CB  
2853 C CG  . PHE A 392 ? 0.2344 0.2834 0.2109 -0.0034 -0.0219 -0.0140 422 PHE A CG  
2854 C CD1 . PHE A 392 ? 0.2316 0.2793 0.2080 -0.0066 -0.0184 -0.0190 422 PHE A CD1 
2855 C CD2 . PHE A 392 ? 0.2038 0.2594 0.1840 -0.0021 -0.0282 -0.0134 422 PHE A CD2 
2856 C CE1 . PHE A 392 ? 0.2320 0.2842 0.2118 -0.0093 -0.0210 -0.0232 422 PHE A CE1 
2857 C CE2 . PHE A 392 ? 0.2058 0.2675 0.1896 -0.0047 -0.0308 -0.0177 422 PHE A CE2 
2858 C CZ  . PHE A 392 ? 0.2137 0.2733 0.1972 -0.0087 -0.0271 -0.0226 422 PHE A CZ  
2859 N N   . ASN A 393 ? 0.2324 0.2756 0.1738 -0.0052 -0.0260 -0.0059 423 ASN A N   
2860 C CA  . ASN A 393 ? 0.2521 0.2991 0.1856 -0.0050 -0.0334 -0.0037 423 ASN A CA  
2861 C C   . ASN A 393 ? 0.2419 0.2964 0.1805 -0.0060 -0.0379 -0.0096 423 ASN A C   
2862 O O   . ASN A 393 ? 0.2549 0.3147 0.1936 -0.0045 -0.0454 -0.0080 423 ASN A O   
2863 C CB  . ASN A 393 ? 0.2590 0.3044 0.1752 -0.0078 -0.0319 -0.0025 423 ASN A CB  
2864 C CG  . ASN A 393 ? 0.3597 0.3986 0.2706 -0.0075 -0.0281 0.0047  423 ASN A CG  
2865 O OD1 . ASN A 393 ? 0.3540 0.3892 0.2733 -0.0046 -0.0287 0.0096  423 ASN A OD1 
2866 N ND2 . ASN A 393 ? 0.3410 0.3790 0.2381 -0.0106 -0.0239 0.0050  423 ASN A ND2 
2867 N N   . GLY A 394 ? 0.2434 0.2983 0.1869 -0.0088 -0.0338 -0.0164 424 GLY A N   
2868 C CA  . GLY A 394 ? 0.2489 0.3103 0.1980 -0.0109 -0.0374 -0.0222 424 GLY A CA  
2869 C C   . GLY A 394 ? 0.3012 0.3647 0.2383 -0.0143 -0.0397 -0.0271 424 GLY A C   
2870 O O   . GLY A 394 ? 0.3141 0.3749 0.2373 -0.0150 -0.0382 -0.0258 424 GLY A O   
2871 N N   . ASN A 395 ? 0.3092 0.3786 0.2520 -0.0170 -0.0434 -0.0331 425 ASN A N   
2872 C CA  . ASN A 395 ? 0.3193 0.3917 0.2522 -0.0205 -0.0463 -0.0396 425 ASN A CA  
2873 C C   . ASN A 395 ? 0.3598 0.4403 0.2872 -0.0192 -0.0557 -0.0371 425 ASN A C   
2874 O O   . ASN A 395 ? 0.3347 0.4229 0.2720 -0.0194 -0.0616 -0.0389 425 ASN A O   
2875 C CB  . ASN A 395 ? 0.3290 0.4023 0.2718 -0.0247 -0.0453 -0.0481 425 ASN A CB  
2876 C CG  . ASN A 395 ? 0.3610 0.4254 0.3064 -0.0259 -0.0367 -0.0511 425 ASN A CG  
2877 O OD1 . ASN A 395 ? 0.3204 0.3796 0.2560 -0.0250 -0.0320 -0.0505 425 ASN A OD1 
2878 N ND2 . ASN A 395 ? 0.3107 0.3735 0.2695 -0.0279 -0.0348 -0.0539 425 ASN A ND2 
2879 N N   . THR A 396 ? 0.3340 0.4132 0.2455 -0.0178 -0.0572 -0.0325 426 THR A N   
2880 C CA  . THR A 396 ? 0.4414 0.5269 0.3455 -0.0157 -0.0666 -0.0282 426 THR A CA  
2881 C C   . THR A 396 ? 0.4390 0.5307 0.3301 -0.0191 -0.0713 -0.0347 426 THR A C   
2882 O O   . THR A 396 ? 0.4916 0.5889 0.3735 -0.0175 -0.0795 -0.0310 426 THR A O   
2883 C CB  . THR A 396 ? 0.4150 0.4949 0.3089 -0.0123 -0.0660 -0.0177 426 THR A CB  
2884 O OG1 . THR A 396 ? 0.3721 0.4460 0.2530 -0.0148 -0.0583 -0.0181 426 THR A OG1 
2885 C CG2 . THR A 396 ? 0.3484 0.4238 0.2564 -0.0084 -0.0638 -0.0119 426 THR A CG2 
2886 N N   . GLU A 397 ? 0.4404 0.5312 0.3311 -0.0235 -0.0670 -0.0446 427 GLU A N   
2887 C CA  . GLU A 397 ? 0.4648 0.5605 0.3408 -0.0268 -0.0703 -0.0518 427 GLU A CA  
2888 C C   . GLU A 397 ? 0.5057 0.6126 0.3848 -0.0274 -0.0814 -0.0550 427 GLU A C   
2889 O O   . GLU A 397 ? 0.7472 0.8601 0.6109 -0.0281 -0.0874 -0.0567 427 GLU A O   
2890 C CB  . GLU A 397 ? 0.4452 0.5368 0.3228 -0.0310 -0.0633 -0.0628 427 GLU A CB  
2891 C CG  . GLU A 397 ? 0.4820 0.5717 0.3803 -0.0329 -0.0615 -0.0679 427 GLU A CG  
2892 C CD  . GLU A 397 ? 0.4091 0.4896 0.3169 -0.0311 -0.0527 -0.0634 427 GLU A CD  
2893 O OE1 . GLU A 397 ? 0.3795 0.4567 0.2823 -0.0276 -0.0500 -0.0547 427 GLU A OE1 
2894 O OE2 . GLU A 397 ? 0.4564 0.5327 0.3766 -0.0333 -0.0488 -0.0685 427 GLU A OE2 
2895 N N   . GLY A 398 ? 0.4822 0.5931 0.3807 -0.0272 -0.0843 -0.0561 428 GLY A N   
2896 C CA  . GLY A 398 ? 0.5444 0.6674 0.4484 -0.0282 -0.0946 -0.0602 428 GLY A CA  
2897 C C   . GLY A 398 ? 0.4860 0.6154 0.3903 -0.0226 -0.1032 -0.0511 428 GLY A C   
2898 O O   . GLY A 398 ? 0.4740 0.6143 0.3889 -0.0223 -0.1116 -0.0533 428 GLY A O   
2899 N N   . GLY A 399 ? 0.4976 0.6203 0.3912 -0.0184 -0.1015 -0.0408 429 GLY A N   
2900 C CA  . GLY A 399 ? 0.4275 0.5532 0.3234 -0.0124 -0.1089 -0.0312 429 GLY A CA  
2901 C C   . GLY A 399 ? 0.4997 0.6231 0.4152 -0.0087 -0.1061 -0.0270 429 GLY A C   
2902 O O   . GLY A 399 ? 0.4829 0.6108 0.4051 -0.0034 -0.1132 -0.0212 429 GLY A O   
2903 N N   . ARG A 400 ? 0.4227 0.5398 0.3475 -0.0110 -0.0963 -0.0300 430 ARG A N   
2904 C CA  . ARG A 400 ? 0.3200 0.4356 0.2620 -0.0077 -0.0931 -0.0265 430 ARG A CA  
2905 C C   . ARG A 400 ? 0.3201 0.4266 0.2564 -0.0027 -0.0913 -0.0164 430 ARG A C   
2906 O O   . ARG A 400 ? 0.3648 0.4628 0.2859 -0.0037 -0.0871 -0.0130 430 ARG A O   
2907 C CB  . ARG A 400 ? 0.3207 0.4319 0.2722 -0.0119 -0.0834 -0.0321 430 ARG A CB  
2908 C CG  . ARG A 400 ? 0.3371 0.4482 0.3058 -0.0092 -0.0796 -0.0296 430 ARG A CG  
2909 C CD  . ARG A 400 ? 0.3522 0.4576 0.3271 -0.0132 -0.0702 -0.0337 430 ARG A CD  
2910 N NE  . ARG A 400 ? 0.2963 0.4064 0.2762 -0.0192 -0.0707 -0.0420 430 ARG A NE  
2911 C CZ  . ARG A 400 ? 0.3807 0.4849 0.3638 -0.0235 -0.0638 -0.0464 430 ARG A CZ  
2912 N NH1 . ARG A 400 ? 0.3160 0.4102 0.2975 -0.0224 -0.0560 -0.0435 430 ARG A NH1 
2913 N NH2 . ARG A 400 ? 0.2551 0.3632 0.2438 -0.0291 -0.0651 -0.0539 430 ARG A NH2 
2914 N N   . ALA A 401 ? 0.3263 0.4350 0.2755 0.0026  -0.0944 -0.0121 431 ALA A N   
2915 C CA  . ALA A 401 ? 0.3048 0.4042 0.2511 0.0074  -0.0932 -0.0030 431 ALA A CA  
2916 C C   . ALA A 401 ? 0.3032 0.3921 0.2487 0.0052  -0.0820 -0.0028 431 ALA A C   
2917 O O   . ALA A 401 ? 0.2949 0.3848 0.2484 0.0019  -0.0758 -0.0091 431 ALA A O   
2918 C CB  . ALA A 401 ? 0.3062 0.4103 0.2693 0.0137  -0.0981 -0.0005 431 ALA A CB  
2919 N N   . PRO A 402 ? 0.3120 0.3907 0.2481 0.0068  -0.0793 0.0045  432 PRO A N   
2920 C CA  . PRO A 402 ? 0.2661 0.3361 0.2039 0.0054  -0.0694 0.0048  432 PRO A CA  
2921 C C   . PRO A 402 ? 0.2950 0.3669 0.2514 0.0078  -0.0668 0.0022  432 PRO A C   
2922 O O   . PRO A 402 ? 0.2461 0.3235 0.2136 0.0121  -0.0724 0.0031  432 PRO A O   
2923 C CB  . PRO A 402 ? 0.2762 0.3366 0.2042 0.0075  -0.0695 0.0142  432 PRO A CB  
2924 C CG  . PRO A 402 ? 0.2945 0.3576 0.2080 0.0074  -0.0770 0.0180  432 PRO A CG  
2925 C CD  . PRO A 402 ? 0.3150 0.3898 0.2376 0.0092  -0.0852 0.0132  432 PRO A CD  
2926 N N   . ALA A 403 ? 0.2391 0.3074 0.1989 0.0051  -0.0583 -0.0012 433 ALA A N   
2927 C CA  . ALA A 403 ? 0.2453 0.3163 0.2208 0.0065  -0.0551 -0.0040 433 ALA A CA  
2928 C C   . ALA A 403 ? 0.2451 0.3134 0.2280 0.0122  -0.0568 0.0007  433 ALA A C   
2929 O O   . ALA A 403 ? 0.2536 0.3131 0.2301 0.0134  -0.0556 0.0061  433 ALA A O   
2930 C CB  . ALA A 403 ? 0.2165 0.2824 0.1920 0.0031  -0.0461 -0.0071 433 ALA A CB  
2931 N N   . THR A 404 ? 0.2551 0.3314 0.2521 0.0153  -0.0595 -0.0016 434 THR A N   
2932 C CA  . THR A 404 ? 0.2248 0.2993 0.2308 0.0210  -0.0608 0.0010  434 THR A CA  
2933 C C   . THR A 404 ? 0.1963 0.2723 0.2122 0.0209  -0.0539 -0.0028 434 THR A C   
2934 O O   . THR A 404 ? 0.1940 0.2696 0.2079 0.0164  -0.0480 -0.0056 434 THR A O   
2935 C CB  . THR A 404 ? 0.2814 0.3647 0.2963 0.0260  -0.0694 0.0010  434 THR A CB  
2936 O OG1 . THR A 404 ? 0.2534 0.3333 0.2769 0.0321  -0.0709 0.0032  434 THR A OG1 
2937 C CG2 . THR A 404 ? 0.2480 0.3453 0.2745 0.0246  -0.0694 -0.0056 434 THR A CG2 
2938 N N   . HIS A 405 ? 0.1921 0.2698 0.2186 0.0261  -0.0551 -0.0029 435 HIS A N   
2939 C CA  . HIS A 405 ? 0.1811 0.2602 0.2156 0.0266  -0.0491 -0.0060 435 HIS A CA  
2940 C C   . HIS A 405 ? 0.1926 0.2822 0.2330 0.0232  -0.0458 -0.0109 435 HIS A C   
2941 O O   . HIS A 405 ? 0.1729 0.2733 0.2204 0.0236  -0.0495 -0.0133 435 HIS A O   
2942 C CB  . HIS A 405 ? 0.1801 0.2608 0.2253 0.0333  -0.0521 -0.0065 435 HIS A CB  
2943 C CG  . HIS A 405 ? 0.1722 0.2513 0.2225 0.0344  -0.0465 -0.0090 435 HIS A CG  
2944 N ND1 . HIS A 405 ? 0.2053 0.2739 0.2490 0.0325  -0.0422 -0.0068 435 HIS A ND1 
2945 C CD2 . HIS A 405 ? 0.1649 0.2527 0.2262 0.0374  -0.0447 -0.0137 435 HIS A CD2 
2946 C CE1 . HIS A 405 ? 0.1742 0.2448 0.2244 0.0342  -0.0385 -0.0102 435 HIS A CE1 
2947 N NE2 . HIS A 405 ? 0.1609 0.2431 0.2212 0.0372  -0.0398 -0.0143 435 HIS A NE2 
2948 N N   . GLY A 406 ? 0.1891 0.2757 0.2274 0.0197  -0.0390 -0.0119 436 GLY A N   
2949 C CA  . GLY A 406 ? 0.1609 0.2551 0.2041 0.0160  -0.0351 -0.0153 436 GLY A CA  
2950 C C   . GLY A 406 ? 0.2128 0.3058 0.2500 0.0101  -0.0344 -0.0162 436 GLY A C   
2951 O O   . GLY A 406 ? 0.1929 0.2890 0.2334 0.0062  -0.0305 -0.0181 436 GLY A O   
2952 N N   . ALA A 407 ? 0.1729 0.2610 0.2010 0.0091  -0.0381 -0.0148 437 ALA A N   
2953 C CA  . ALA A 407 ? 0.1839 0.2729 0.2073 0.0038  -0.0387 -0.0172 437 ALA A CA  
2954 C C   . ALA A 407 ? 0.2240 0.3062 0.2436 -0.0005 -0.0322 -0.0186 437 ALA A C   
2955 O O   . ALA A 407 ? 0.2198 0.3034 0.2397 -0.0052 -0.0316 -0.0218 437 ALA A O   
2956 C CB  . ALA A 407 ? 0.1888 0.2744 0.2014 0.0040  -0.0439 -0.0155 437 ALA A CB  
2957 N N   . GLU A 408 ? 0.2045 0.2791 0.2212 0.0012  -0.0276 -0.0165 438 GLU A N   
2958 C CA  . GLU A 408 ? 0.2058 0.2733 0.2186 -0.0020 -0.0221 -0.0177 438 GLU A CA  
2959 C C   . GLU A 408 ? 0.1919 0.2617 0.2127 -0.0036 -0.0181 -0.0186 438 GLU A C   
2960 O O   . GLU A 408 ? 0.2006 0.2647 0.2196 -0.0063 -0.0143 -0.0196 438 GLU A O   
2961 C CB  . GLU A 408 ? 0.1859 0.2451 0.1926 0.0002  -0.0191 -0.0151 438 GLU A CB  
2962 C CG  . GLU A 408 ? 0.1957 0.2544 0.2085 0.0030  -0.0157 -0.0138 438 GLU A CG  
2963 C CD  . GLU A 408 ? 0.1862 0.2507 0.2057 0.0071  -0.0189 -0.0125 438 GLU A CD  
2964 O OE1 . GLU A 408 ? 0.1647 0.2324 0.1842 0.0085  -0.0239 -0.0120 438 GLU A OE1 
2965 O OE2 . GLU A 408 ? 0.2115 0.2773 0.2362 0.0094  -0.0165 -0.0125 438 GLU A OE2 
2966 N N   . ILE A 409 ? 0.2248 0.3033 0.2545 -0.0019 -0.0189 -0.0181 439 ILE A N   
2967 C CA  . ILE A 409 ? 0.2034 0.2847 0.2393 -0.0035 -0.0147 -0.0179 439 ILE A CA  
2968 C C   . ILE A 409 ? 0.2293 0.3093 0.2664 -0.0095 -0.0131 -0.0195 439 ILE A C   
2969 O O   . ILE A 409 ? 0.1752 0.2497 0.2122 -0.0111 -0.0090 -0.0183 439 ILE A O   
2970 C CB  . ILE A 409 ? 0.2830 0.3761 0.3279 -0.0010 -0.0156 -0.0179 439 ILE A CB  
2971 C CG1 . ILE A 409 ? 0.2797 0.3719 0.3243 0.0050  -0.0162 -0.0169 439 ILE A CG1 
2972 C CG2 . ILE A 409 ? 0.2802 0.3781 0.3306 -0.0038 -0.0112 -0.0173 439 ILE A CG2 
2973 C CD1 . ILE A 409 ? 0.2762 0.3802 0.3299 0.0085  -0.0179 -0.0184 439 ILE A CD1 
2974 N N   . PRO A 410 ? 0.2248 0.3094 0.2639 -0.0128 -0.0166 -0.0221 440 PRO A N   
2975 C CA  . PRO A 410 ? 0.2145 0.2963 0.2557 -0.0190 -0.0152 -0.0242 440 PRO A CA  
2976 C C   . PRO A 410 ? 0.2276 0.2968 0.2609 -0.0202 -0.0133 -0.0256 440 PRO A C   
2977 O O   . PRO A 410 ? 0.2173 0.2809 0.2528 -0.0241 -0.0106 -0.0264 440 PRO A O   
2978 C CB  . PRO A 410 ? 0.2881 0.3785 0.3329 -0.0218 -0.0204 -0.0276 440 PRO A CB  
2979 C CG  . PRO A 410 ? 0.2509 0.3513 0.2993 -0.0169 -0.0237 -0.0264 440 PRO A CG  
2980 C CD  . PRO A 410 ? 0.2649 0.3580 0.3061 -0.0113 -0.0224 -0.0235 440 PRO A CD  
2981 N N   . TYR A 411 ? 0.2139 0.2785 0.2384 -0.0170 -0.0143 -0.0260 441 TYR A N   
2982 C CA  . TYR A 411 ? 0.2224 0.2767 0.2398 -0.0178 -0.0119 -0.0280 441 TYR A CA  
2983 C C   . TYR A 411 ? 0.2309 0.2788 0.2493 -0.0156 -0.0069 -0.0254 441 TYR A C   
2984 O O   . TYR A 411 ? 0.2834 0.3231 0.2993 -0.0164 -0.0043 -0.0274 441 TYR A O   
2985 C CB  . TYR A 411 ? 0.2076 0.2606 0.2150 -0.0156 -0.0141 -0.0288 441 TYR A CB  
2986 C CG  . TYR A 411 ? 0.2550 0.3141 0.2598 -0.0176 -0.0198 -0.0315 441 TYR A CG  
2987 C CD1 . TYR A 411 ? 0.2075 0.2756 0.2164 -0.0157 -0.0243 -0.0294 441 TYR A CD1 
2988 C CD2 . TYR A 411 ? 0.2018 0.2582 0.2008 -0.0211 -0.0209 -0.0367 441 TYR A CD2 
2989 C CE1 . TYR A 411 ? 0.2108 0.2854 0.2181 -0.0171 -0.0303 -0.0317 441 TYR A CE1 
2990 C CE2 . TYR A 411 ? 0.2416 0.3045 0.2379 -0.0229 -0.0268 -0.0395 441 TYR A CE2 
2991 C CZ  . TYR A 411 ? 0.2561 0.3282 0.2567 -0.0209 -0.0317 -0.0367 441 TYR A CZ  
2992 O OH  . TYR A 411 ? 0.2206 0.3000 0.2190 -0.0222 -0.0383 -0.0394 441 TYR A OH  
2993 N N   . VAL A 412 ? 0.2160 0.2680 0.2384 -0.0126 -0.0060 -0.0215 442 VAL A N   
2994 C CA  . VAL A 412 ? 0.2172 0.2649 0.2411 -0.0105 -0.0021 -0.0188 442 VAL A CA  
2995 C C   . VAL A 412 ? 0.1943 0.2426 0.2245 -0.0134 -0.0002 -0.0170 442 VAL A C   
2996 O O   . VAL A 412 ? 0.2097 0.2504 0.2403 -0.0141 0.0023  -0.0163 442 VAL A O   
2997 C CB  . VAL A 412 ? 0.2167 0.2685 0.2407 -0.0057 -0.0022 -0.0162 442 VAL A CB  
2998 C CG1 . VAL A 412 ? 0.1682 0.2185 0.1947 -0.0037 0.0010  -0.0136 442 VAL A CG1 
2999 C CG2 . VAL A 412 ? 0.1835 0.2315 0.2009 -0.0034 -0.0029 -0.0169 442 VAL A CG2 
3000 N N   . PHE A 413 ? 0.1638 0.2214 0.1995 -0.0152 -0.0014 -0.0160 443 PHE A N   
3001 C CA  . PHE A 413 ? 0.2217 0.2812 0.2631 -0.0185 0.0010  -0.0131 443 PHE A CA  
3002 C C   . PHE A 413 ? 0.2610 0.3154 0.3053 -0.0246 0.0008  -0.0149 443 PHE A C   
3003 O O   . PHE A 413 ? 0.2540 0.3043 0.3017 -0.0276 0.0033  -0.0118 443 PHE A O   
3004 C CB  . PHE A 413 ? 0.1757 0.2488 0.2227 -0.0184 0.0006  -0.0117 443 PHE A CB  
3005 C CG  . PHE A 413 ? 0.1946 0.2721 0.2408 -0.0134 0.0023  -0.0092 443 PHE A CG  
3006 C CD1 . PHE A 413 ? 0.1780 0.2566 0.2214 -0.0081 0.0004  -0.0107 443 PHE A CD1 
3007 C CD2 . PHE A 413 ? 0.2176 0.2980 0.2657 -0.0144 0.0056  -0.0052 443 PHE A CD2 
3008 C CE1 . PHE A 413 ? 0.1589 0.2414 0.2023 -0.0037 0.0017  -0.0094 443 PHE A CE1 
3009 C CE2 . PHE A 413 ? 0.2109 0.2963 0.2577 -0.0098 0.0069  -0.0038 443 PHE A CE2 
3010 C CZ  . PHE A 413 ? 0.1632 0.2496 0.2081 -0.0045 0.0048  -0.0064 443 PHE A CZ  
3011 N N   . GLY A 414 ? 0.2459 0.3004 0.2891 -0.0267 -0.0023 -0.0197 444 GLY A N   
3012 C CA  . GLY A 414 ? 0.2788 0.3285 0.3251 -0.0327 -0.0030 -0.0229 444 GLY A CA  
3013 C C   . GLY A 414 ? 0.2498 0.3090 0.3048 -0.0383 -0.0042 -0.0230 444 GLY A C   
3014 O O   . GLY A 414 ? 0.2576 0.3126 0.3170 -0.0442 -0.0046 -0.0254 444 GLY A O   
3015 N N   . VAL A 415 ? 0.2617 0.3339 0.3202 -0.0366 -0.0049 -0.0211 445 VAL A N   
3016 C CA  . VAL A 415 ? 0.2706 0.3547 0.3388 -0.0416 -0.0056 -0.0215 445 VAL A CA  
3017 C C   . VAL A 415 ? 0.2547 0.3482 0.3233 -0.0400 -0.0112 -0.0262 445 VAL A C   
3018 O O   . VAL A 415 ? 0.2788 0.3800 0.3465 -0.0345 -0.0127 -0.0254 445 VAL A O   
3019 C CB  . VAL A 415 ? 0.2213 0.3150 0.2943 -0.0408 -0.0019 -0.0163 445 VAL A CB  
3020 C CG1 . VAL A 415 ? 0.2531 0.3609 0.3372 -0.0464 -0.0020 -0.0171 445 VAL A CG1 
3021 C CG2 . VAL A 415 ? 0.1963 0.2802 0.2671 -0.0419 0.0028  -0.0109 445 VAL A CG2 
3022 N N   . PHE A 416 ? 0.2591 0.3518 0.3293 -0.0447 -0.0147 -0.0311 446 PHE A N   
3023 C CA  . PHE A 416 ? 0.2466 0.3480 0.3163 -0.0434 -0.0209 -0.0355 446 PHE A CA  
3024 C C   . PHE A 416 ? 0.2775 0.3951 0.3600 -0.0467 -0.0225 -0.0363 446 PHE A C   
3025 O O   . PHE A 416 ? 0.2964 0.4183 0.3857 -0.0530 -0.0250 -0.0404 446 PHE A O   
3026 C CB  . PHE A 416 ? 0.2894 0.3830 0.3533 -0.0463 -0.0242 -0.0413 446 PHE A CB  
3027 C CG  . PHE A 416 ? 0.3200 0.4013 0.3709 -0.0420 -0.0231 -0.0414 446 PHE A CG  
3028 C CD1 . PHE A 416 ? 0.2408 0.3240 0.2827 -0.0368 -0.0267 -0.0417 446 PHE A CD1 
3029 C CD2 . PHE A 416 ? 0.3048 0.3729 0.3532 -0.0430 -0.0185 -0.0409 446 PHE A CD2 
3030 C CE1 . PHE A 416 ? 0.2972 0.3704 0.3278 -0.0335 -0.0249 -0.0416 446 PHE A CE1 
3031 C CE2 . PHE A 416 ? 0.2719 0.3305 0.3099 -0.0390 -0.0171 -0.0416 446 PHE A CE2 
3032 C CZ  . PHE A 416 ? 0.3106 0.3722 0.3396 -0.0346 -0.0200 -0.0420 446 PHE A CZ  
3033 N N   . LYS A 417 ? 0.3197 0.4472 0.4064 -0.0425 -0.0209 -0.0330 447 LYS A N   
3034 C CA  . LYS A 417 ? 0.2940 0.4394 0.3934 -0.0440 -0.0221 -0.0342 447 LYS A CA  
3035 C C   . LYS A 417 ? 0.2718 0.4257 0.3705 -0.0358 -0.0263 -0.0346 447 LYS A C   
3036 O O   . LYS A 417 ? 0.2168 0.3659 0.3093 -0.0296 -0.0243 -0.0316 447 LYS A O   
3037 C CB  . LYS A 417 ? 0.3121 0.4629 0.4189 -0.0474 -0.0152 -0.0300 447 LYS A CB  
3038 C CG  . LYS A 417 ? 0.4081 0.5503 0.5172 -0.0561 -0.0115 -0.0285 447 LYS A CG  
3039 C CD  . LYS A 417 ? 0.4299 0.5768 0.5442 -0.0592 -0.0044 -0.0228 447 LYS A CD  
3040 C CE  . LYS A 417 ? 0.4269 0.5635 0.5437 -0.0681 -0.0011 -0.0201 447 LYS A CE  
3041 N NZ  . LYS A 417 ? 0.4713 0.6118 0.5911 -0.0711 0.0058  -0.0130 447 LYS A NZ  
3042 N N   . LEU A 418 ? 0.2981 0.4640 0.4036 -0.0356 -0.0325 -0.0385 448 LEU A N   
3043 C CA  . LEU A 418 ? 0.2787 0.4514 0.3841 -0.0274 -0.0378 -0.0389 448 LEU A CA  
3044 C C   . LEU A 418 ? 0.3237 0.5048 0.4355 -0.0225 -0.0339 -0.0368 448 LEU A C   
3045 O O   . LEU A 418 ? 0.3266 0.5172 0.4478 -0.0262 -0.0287 -0.0365 448 LEU A O   
3046 C CB  . LEU A 418 ? 0.3181 0.5046 0.4322 -0.0284 -0.0453 -0.0434 448 LEU A CB  
3047 C CG  . LEU A 418 ? 0.2593 0.4397 0.3661 -0.0322 -0.0509 -0.0467 448 LEU A CG  
3048 C CD1 . LEU A 418 ? 0.2218 0.4187 0.3397 -0.0337 -0.0584 -0.0515 448 LEU A CD1 
3049 C CD2 . LEU A 418 ? 0.2660 0.4335 0.3565 -0.0263 -0.0541 -0.0445 448 LEU A CD2 
3050 N N   . ASP A 419 ? 0.3924 0.5700 0.4990 -0.0142 -0.0363 -0.0354 449 ASP A N   
3051 C CA  . ASP A 419 ? 0.3595 0.5453 0.4725 -0.0084 -0.0338 -0.0350 449 ASP A CA  
3052 C C   . ASP A 419 ? 0.3776 0.5812 0.5042 -0.0050 -0.0390 -0.0388 449 ASP A C   
3053 O O   . ASP A 419 ? 0.3193 0.5276 0.4488 -0.0061 -0.0456 -0.0410 449 ASP A O   
3054 C CB  . ASP A 419 ? 0.3316 0.5050 0.4346 -0.0013 -0.0343 -0.0324 449 ASP A CB  
3055 C CG  . ASP A 419 ? 0.3756 0.5446 0.4737 0.0034  -0.0425 -0.0323 449 ASP A CG  
3056 O OD1 . ASP A 419 ? 0.3142 0.4764 0.4046 -0.0001 -0.0455 -0.0321 449 ASP A OD1 
3057 O OD2 . ASP A 419 ? 0.3604 0.5329 0.4625 0.0107  -0.0459 -0.0325 449 ASP A OD2 
3058 N N   . GLU A 420 ? 0.2799 0.4942 0.4151 -0.0003 -0.0363 -0.0400 450 GLU A N   
3059 C CA  . GLU A 420 ? 0.4250 0.6577 0.5752 0.0039  -0.0405 -0.0443 450 GLU A CA  
3060 C C   . GLU A 420 ? 0.4190 0.6482 0.5682 0.0137  -0.0482 -0.0446 450 GLU A C   
3061 O O   . GLU A 420 ? 0.3795 0.6220 0.5405 0.0179  -0.0541 -0.0479 450 GLU A O   
3062 C CB  . GLU A 420 ? 0.3461 0.5939 0.5071 0.0044  -0.0335 -0.0464 450 GLU A CB  
3063 C CG  . GLU A 420 ? 0.4282 0.6769 0.5879 -0.0049 -0.0249 -0.0442 450 GLU A CG  
3064 C CD  . GLU A 420 ? 0.4626 0.7202 0.6306 -0.0138 -0.0256 -0.0455 450 GLU A CD  
3065 O OE1 . GLU A 420 ? 0.5169 0.7867 0.6956 -0.0123 -0.0319 -0.0495 450 GLU A OE1 
3066 O OE2 . GLU A 420 ? 0.4958 0.7480 0.6603 -0.0223 -0.0201 -0.0425 450 GLU A OE2 
3067 N N   . LEU A 421 ? 0.3486 0.5602 0.4846 0.0173  -0.0485 -0.0409 451 LEU A N   
3068 C CA  . LEU A 421 ? 0.3654 0.5709 0.4996 0.0260  -0.0555 -0.0399 451 LEU A CA  
3069 C C   . LEU A 421 ? 0.3538 0.5499 0.4781 0.0253  -0.0630 -0.0370 451 LEU A C   
3070 O O   . LEU A 421 ? 0.3705 0.5581 0.4899 0.0315  -0.0687 -0.0343 451 LEU A O   
3071 C CB  . LEU A 421 ? 0.3597 0.5520 0.4862 0.0300  -0.0516 -0.0376 451 LEU A CB  
3072 C CG  . LEU A 421 ? 0.2784 0.4794 0.4118 0.0306  -0.0439 -0.0406 451 LEU A CG  
3073 C CD1 . LEU A 421 ? 0.2663 0.4543 0.3921 0.0347  -0.0412 -0.0390 451 LEU A CD1 
3074 C CD2 . LEU A 421 ? 0.2998 0.5204 0.4504 0.0355  -0.0456 -0.0462 451 LEU A CD2 
3075 N N   . GLY A 422 ? 0.3246 0.5220 0.4457 0.0177  -0.0631 -0.0376 452 GLY A N   
3076 C CA  . GLY A 422 ? 0.3707 0.5605 0.4812 0.0164  -0.0699 -0.0357 452 GLY A CA  
3077 C C   . GLY A 422 ? 0.4193 0.5895 0.5122 0.0172  -0.0689 -0.0307 452 GLY A C   
3078 O O   . GLY A 422 ? 0.4258 0.5900 0.5099 0.0196  -0.0756 -0.0280 452 GLY A O   
3079 N N   . LEU A 423 ? 0.3736 0.5342 0.4608 0.0148  -0.0608 -0.0293 453 LEU A N   
3080 C CA  . LEU A 423 ? 0.3492 0.4926 0.4214 0.0154  -0.0592 -0.0250 453 LEU A CA  
3081 C C   . LEU A 423 ? 0.3746 0.5102 0.4356 0.0083  -0.0567 -0.0251 453 LEU A C   
3082 O O   . LEU A 423 ? 0.4245 0.5494 0.4725 0.0084  -0.0584 -0.0224 453 LEU A O   
3083 C CB  . LEU A 423 ? 0.3754 0.5129 0.4481 0.0178  -0.0526 -0.0238 453 LEU A CB  
3084 C CG  . LEU A 423 ? 0.3621 0.5044 0.4443 0.0256  -0.0549 -0.0242 453 LEU A CG  
3085 C CD1 . LEU A 423 ? 0.2888 0.4254 0.3706 0.0272  -0.0484 -0.0240 453 LEU A CD1 
3086 C CD2 . LEU A 423 ? 0.2996 0.4355 0.3776 0.0310  -0.0628 -0.0209 453 LEU A CD2 
3087 N N   . PHE A 424 ? 0.2984 0.4386 0.3642 0.0020  -0.0524 -0.0282 454 PHE A N   
3088 C CA  . PHE A 424 ? 0.3205 0.4529 0.3775 -0.0045 -0.0502 -0.0294 454 PHE A CA  
3089 C C   . PHE A 424 ? 0.3595 0.4969 0.4143 -0.0068 -0.0574 -0.0323 454 PHE A C   
3090 O O   . PHE A 424 ? 0.2832 0.4341 0.3491 -0.0077 -0.0614 -0.0353 454 PHE A O   
3091 C CB  . PHE A 424 ? 0.3489 0.4831 0.4126 -0.0104 -0.0435 -0.0312 454 PHE A CB  
3092 C CG  . PHE A 424 ? 0.2603 0.3911 0.3258 -0.0084 -0.0367 -0.0285 454 PHE A CG  
3093 C CD1 . PHE A 424 ? 0.2783 0.4015 0.3376 -0.0027 -0.0360 -0.0255 454 PHE A CD1 
3094 C CD2 . PHE A 424 ? 0.2760 0.4115 0.3491 -0.0126 -0.0313 -0.0289 454 PHE A CD2 
3095 C CE1 . PHE A 424 ? 0.2182 0.3393 0.2792 -0.0009 -0.0304 -0.0238 454 PHE A CE1 
3096 C CE2 . PHE A 424 ? 0.2879 0.4212 0.3614 -0.0107 -0.0255 -0.0263 454 PHE A CE2 
3097 C CZ  . PHE A 424 ? 0.2544 0.3810 0.3220 -0.0047 -0.0253 -0.0242 454 PHE A CZ  
3098 N N   . ASP A 425 ? 0.3621 0.4898 0.4026 -0.0080 -0.0589 -0.0318 455 ASP A N   
3099 C CA  . ASP A 425 ? 0.3132 0.4452 0.3482 -0.0091 -0.0667 -0.0341 455 ASP A CA  
3100 C C   . ASP A 425 ? 0.3028 0.4302 0.3311 -0.0161 -0.0649 -0.0389 455 ASP A C   
3101 O O   . ASP A 425 ? 0.3071 0.4231 0.3228 -0.0170 -0.0614 -0.0383 455 ASP A O   
3102 C CB  . ASP A 425 ? 0.3068 0.4329 0.3294 -0.0036 -0.0713 -0.0291 455 ASP A CB  
3103 C CG  . ASP A 425 ? 0.3354 0.4688 0.3537 -0.0031 -0.0810 -0.0302 455 ASP A CG  
3104 O OD1 . ASP A 425 ? 0.3684 0.5115 0.3932 -0.0074 -0.0841 -0.0359 455 ASP A OD1 
3105 O OD2 . ASP A 425 ? 0.2636 0.3931 0.2719 0.0014  -0.0858 -0.0251 455 ASP A OD2 
3106 N N   . TRP A 426 ? 0.3520 0.4889 0.3897 -0.0212 -0.0674 -0.0444 456 TRP A N   
3107 C CA  . TRP A 426 ? 0.3818 0.5157 0.4145 -0.0278 -0.0678 -0.0504 456 TRP A CA  
3108 C C   . TRP A 426 ? 0.3505 0.4989 0.3949 -0.0316 -0.0742 -0.0558 456 TRP A C   
3109 O O   . TRP A 426 ? 0.3882 0.5484 0.4464 -0.0300 -0.0759 -0.0548 456 TRP A O   
3110 C CB  . TRP A 426 ? 0.2969 0.4203 0.3310 -0.0324 -0.0590 -0.0517 456 TRP A CB  
3111 C CG  . TRP A 426 ? 0.3240 0.4521 0.3735 -0.0347 -0.0544 -0.0506 456 TRP A CG  
3112 C CD1 . TRP A 426 ? 0.3452 0.4836 0.4086 -0.0402 -0.0557 -0.0542 456 TRP A CD1 
3113 C CD2 . TRP A 426 ? 0.2812 0.4043 0.3334 -0.0322 -0.0474 -0.0454 456 TRP A CD2 
3114 N NE1 . TRP A 426 ? 0.3042 0.4446 0.3781 -0.0413 -0.0495 -0.0510 456 TRP A NE1 
3115 C CE2 . TRP A 426 ? 0.3051 0.4362 0.3717 -0.0362 -0.0446 -0.0458 456 TRP A CE2 
3116 C CE3 . TRP A 426 ? 0.3005 0.4140 0.3444 -0.0272 -0.0433 -0.0408 456 TRP A CE3 
3117 C CZ2 . TRP A 426 ? 0.2644 0.3942 0.3358 -0.0351 -0.0380 -0.0414 456 TRP A CZ2 
3118 C CZ3 . TRP A 426 ? 0.2828 0.3949 0.3324 -0.0260 -0.0373 -0.0371 456 TRP A CZ3 
3119 C CH2 . TRP A 426 ? 0.3153 0.4357 0.3779 -0.0297 -0.0348 -0.0373 456 TRP A CH2 
3120 N N   . PRO A 427 ? 0.4166 0.5652 0.4561 -0.0368 -0.0779 -0.0623 457 PRO A N   
3121 C CA  . PRO A 427 ? 0.4463 0.6099 0.4967 -0.0405 -0.0853 -0.0681 457 PRO A CA  
3122 C C   . PRO A 427 ? 0.3983 0.5700 0.4688 -0.0453 -0.0815 -0.0696 457 PRO A C   
3123 O O   . PRO A 427 ? 0.4285 0.5916 0.5023 -0.0480 -0.0730 -0.0676 457 PRO A O   
3124 C CB  . PRO A 427 ? 0.4133 0.5719 0.4538 -0.0461 -0.0876 -0.0757 457 PRO A CB  
3125 C CG  . PRO A 427 ? 0.3881 0.5335 0.4090 -0.0422 -0.0848 -0.0726 457 PRO A CG  
3126 C CD  . PRO A 427 ? 0.4158 0.5525 0.4389 -0.0386 -0.0764 -0.0652 457 PRO A CD  
3127 N N   . PRO A 428 ? 0.4126 0.6014 0.4969 -0.0467 -0.0877 -0.0728 458 PRO A N   
3128 C CA  . PRO A 428 ? 0.4810 0.6793 0.5852 -0.0520 -0.0835 -0.0739 458 PRO A CA  
3129 C C   . PRO A 428 ? 0.4763 0.6670 0.5843 -0.0619 -0.0784 -0.0783 458 PRO A C   
3130 O O   . PRO A 428 ? 0.4463 0.6379 0.5662 -0.0662 -0.0715 -0.0763 458 PRO A O   
3131 C CB  . PRO A 428 ? 0.4294 0.6485 0.5465 -0.0516 -0.0926 -0.0779 458 PRO A CB  
3132 C CG  . PRO A 428 ? 0.4676 0.6857 0.5707 -0.0493 -0.1020 -0.0810 458 PRO A CG  
3133 C CD  . PRO A 428 ? 0.5228 0.7238 0.6056 -0.0435 -0.0989 -0.0752 458 PRO A CD  
3134 N N   . GLU A 429 ? 0.4860 0.6688 0.5841 -0.0655 -0.0816 -0.0842 459 GLU A N   
3135 C CA  . GLU A 429 ? 0.4724 0.6453 0.5741 -0.0743 -0.0771 -0.0888 459 GLU A CA  
3136 C C   . GLU A 429 ? 0.4938 0.6500 0.5905 -0.0735 -0.0671 -0.0829 459 GLU A C   
3137 O O   . GLU A 429 ? 0.5743 0.7236 0.6790 -0.0802 -0.0617 -0.0836 459 GLU A O   
3138 C CB  . GLU A 429 ? 0.4958 0.6631 0.5862 -0.0770 -0.0826 -0.0972 459 GLU A CB  
3139 C CG  . GLU A 429 ? 0.6287 0.8126 0.7225 -0.0781 -0.0935 -0.1037 459 GLU A CG  
3140 C CD  . GLU A 429 ? 0.6148 0.8048 0.6959 -0.0687 -0.1001 -0.0998 459 GLU A CD  
3141 O OE1 . GLU A 429 ? 0.5580 0.7427 0.6329 -0.0616 -0.0961 -0.0914 459 GLU A OE1 
3142 O OE2 . GLU A 429 ? 0.6581 0.8578 0.7353 -0.0686 -0.1098 -0.1051 459 GLU A OE2 
3143 N N   . GLY A 430 ? 0.4773 0.6267 0.5614 -0.0654 -0.0649 -0.0770 460 GLY A N   
3144 C CA  . GLY A 430 ? 0.4142 0.5488 0.4929 -0.0637 -0.0565 -0.0718 460 GLY A CA  
3145 C C   . GLY A 430 ? 0.3987 0.5222 0.4589 -0.0577 -0.0565 -0.0708 460 GLY A C   
3146 O O   . GLY A 430 ? 0.4062 0.5331 0.4568 -0.0555 -0.0628 -0.0739 460 GLY A O   
3147 N N   . PRO A 431 ? 0.4257 0.5367 0.4806 -0.0552 -0.0494 -0.0663 461 PRO A N   
3148 C CA  . PRO A 431 ? 0.3679 0.4689 0.4063 -0.0502 -0.0484 -0.0655 461 PRO A CA  
3149 C C   . PRO A 431 ? 0.3706 0.4646 0.4008 -0.0539 -0.0500 -0.0736 461 PRO A C   
3150 O O   . PRO A 431 ? 0.4699 0.5600 0.5073 -0.0602 -0.0491 -0.0791 461 PRO A O   
3151 C CB  . PRO A 431 ? 0.3625 0.4529 0.4011 -0.0480 -0.0403 -0.0598 461 PRO A CB  
3152 C CG  . PRO A 431 ? 0.3547 0.4454 0.4074 -0.0538 -0.0370 -0.0595 461 PRO A CG  
3153 C CD  . PRO A 431 ? 0.3434 0.4499 0.4070 -0.0568 -0.0421 -0.0613 461 PRO A CD  
3154 N N   . THR A 432 ? 0.3203 0.4128 0.3352 -0.0500 -0.0525 -0.0746 462 THR A N   
3155 C CA  . THR A 432 ? 0.3306 0.4174 0.3354 -0.0527 -0.0534 -0.0828 462 THR A CA  
3156 C C   . THR A 432 ? 0.3590 0.4311 0.3627 -0.0531 -0.0456 -0.0840 462 THR A C   
3157 O O   . THR A 432 ? 0.3375 0.4041 0.3445 -0.0501 -0.0400 -0.0772 462 THR A O   
3158 C CB  . THR A 432 ? 0.3942 0.4842 0.3817 -0.0484 -0.0574 -0.0823 462 THR A CB  
3159 O OG1 . THR A 432 ? 0.3501 0.4329 0.3293 -0.0431 -0.0518 -0.0754 462 THR A OG1 
3160 C CG2 . THR A 432 ? 0.2704 0.3744 0.2597 -0.0465 -0.0656 -0.0794 462 THR A CG2 
3161 N N   . PRO A 433 ? 0.3882 0.4538 0.3878 -0.0564 -0.0454 -0.0932 463 PRO A N   
3162 C CA  . PRO A 433 ? 0.3351 0.3869 0.3332 -0.0555 -0.0383 -0.0948 463 PRO A CA  
3163 C C   . PRO A 433 ? 0.3402 0.3887 0.3266 -0.0491 -0.0339 -0.0892 463 PRO A C   
3164 O O   . PRO A 433 ? 0.4049 0.4443 0.3943 -0.0469 -0.0278 -0.0862 463 PRO A O   
3165 C CB  . PRO A 433 ? 0.3376 0.3857 0.3315 -0.0595 -0.0403 -0.1072 463 PRO A CB  
3166 C CG  . PRO A 433 ? 0.3737 0.4348 0.3628 -0.0616 -0.0486 -0.1114 463 PRO A CG  
3167 C CD  . PRO A 433 ? 0.3067 0.3775 0.3058 -0.0616 -0.0516 -0.1033 463 PRO A CD  
3168 N N   . ALA A 434 ? 0.3016 0.3574 0.2754 -0.0462 -0.0372 -0.0874 464 ALA A N   
3169 C CA  . ALA A 434 ? 0.3226 0.3760 0.2866 -0.0408 -0.0331 -0.0809 464 ALA A CA  
3170 C C   . ALA A 434 ? 0.3167 0.3699 0.2895 -0.0376 -0.0307 -0.0710 464 ALA A C   
3171 O O   . ALA A 434 ? 0.3425 0.3897 0.3137 -0.0342 -0.0251 -0.0669 464 ALA A O   
3172 C CB  . ALA A 434 ? 0.2794 0.3403 0.2281 -0.0390 -0.0376 -0.0798 464 ALA A CB  
3173 N N   . ASP A 435 ? 0.2931 0.3538 0.2755 -0.0385 -0.0348 -0.0678 465 ASP A N   
3174 C CA  . ASP A 435 ? 0.3251 0.3866 0.3162 -0.0357 -0.0324 -0.0597 465 ASP A CA  
3175 C C   . ASP A 435 ? 0.3330 0.3855 0.3323 -0.0367 -0.0260 -0.0591 465 ASP A C   
3176 O O   . ASP A 435 ? 0.3342 0.3828 0.3340 -0.0329 -0.0217 -0.0536 465 ASP A O   
3177 C CB  . ASP A 435 ? 0.3206 0.3934 0.3220 -0.0369 -0.0375 -0.0580 465 ASP A CB  
3178 C CG  . ASP A 435 ? 0.3711 0.4530 0.3653 -0.0344 -0.0445 -0.0569 465 ASP A CG  
3179 O OD1 . ASP A 435 ? 0.3720 0.4514 0.3551 -0.0302 -0.0443 -0.0530 465 ASP A OD1 
3180 O OD2 . ASP A 435 ? 0.3296 0.4212 0.3299 -0.0369 -0.0505 -0.0597 465 ASP A OD2 
3181 N N   . ARG A 436 ? 0.3168 0.3653 0.3228 -0.0417 -0.0258 -0.0648 466 ARG A N   
3182 C CA  . ARG A 436 ? 0.3508 0.3897 0.3647 -0.0427 -0.0205 -0.0635 466 ARG A CA  
3183 C C   . ARG A 436 ? 0.3631 0.3920 0.3699 -0.0392 -0.0157 -0.0650 466 ARG A C   
3184 O O   . ARG A 436 ? 0.3696 0.3923 0.3803 -0.0368 -0.0113 -0.0605 466 ARG A O   
3185 C CB  . ARG A 436 ? 0.3731 0.4091 0.3965 -0.0494 -0.0218 -0.0690 466 ARG A CB  
3186 C CG  . ARG A 436 ? 0.4184 0.4643 0.4528 -0.0532 -0.0246 -0.0660 466 ARG A CG  
3187 C CD  . ARG A 436 ? 0.5595 0.5994 0.6058 -0.0570 -0.0207 -0.0624 466 ARG A CD  
3188 N NE  . ARG A 436 ? 0.6864 0.7376 0.7429 -0.0599 -0.0217 -0.0580 466 ARG A NE  
3189 C CZ  . ARG A 436 ? 0.6463 0.7059 0.7108 -0.0658 -0.0257 -0.0620 466 ARG A CZ  
3190 N NH1 . ARG A 436 ? 0.5682 0.6261 0.6311 -0.0695 -0.0297 -0.0708 466 ARG A NH1 
3191 N NH2 . ARG A 436 ? 0.5639 0.6349 0.6386 -0.0682 -0.0255 -0.0576 466 ARG A NH2 
3192 N N   . ALA A 437 ? 0.2832 0.3114 0.2794 -0.0389 -0.0166 -0.0713 467 ALA A N   
3193 C CA  . ALA A 437 ? 0.3777 0.3985 0.3674 -0.0355 -0.0116 -0.0734 467 ALA A CA  
3194 C C   . ALA A 437 ? 0.3092 0.3321 0.2948 -0.0304 -0.0088 -0.0654 467 ALA A C   
3195 O O   . ALA A 437 ? 0.3613 0.3782 0.3494 -0.0274 -0.0041 -0.0634 467 ALA A O   
3196 C CB  . ALA A 437 ? 0.2905 0.3126 0.2688 -0.0366 -0.0129 -0.0822 467 ALA A CB  
3197 N N   . LEU A 438 ? 0.2987 0.3299 0.2787 -0.0292 -0.0122 -0.0611 468 LEU A N   
3198 C CA  . LEU A 438 ? 0.2931 0.3257 0.2705 -0.0248 -0.0102 -0.0535 468 LEU A CA  
3199 C C   . LEU A 438 ? 0.3363 0.3674 0.3249 -0.0232 -0.0082 -0.0479 468 LEU A C   
3200 O O   . LEU A 438 ? 0.2782 0.3065 0.2673 -0.0198 -0.0045 -0.0441 468 LEU A O   
3201 C CB  . LEU A 438 ? 0.2287 0.2695 0.1996 -0.0239 -0.0152 -0.0499 468 LEU A CB  
3202 C CG  . LEU A 438 ? 0.2760 0.3173 0.2426 -0.0197 -0.0138 -0.0427 468 LEU A CG  
3203 C CD1 . LEU A 438 ? 0.3182 0.3547 0.2761 -0.0188 -0.0086 -0.0441 468 LEU A CD1 
3204 C CD2 . LEU A 438 ? 0.2279 0.2759 0.1890 -0.0187 -0.0198 -0.0390 468 LEU A CD2 
3205 N N   . GLY A 439 ? 0.2953 0.3291 0.2930 -0.0260 -0.0105 -0.0474 469 GLY A N   
3206 C CA  . GLY A 439 ? 0.3031 0.3363 0.3102 -0.0251 -0.0083 -0.0421 469 GLY A CA  
3207 C C   . GLY A 439 ? 0.2757 0.2992 0.2859 -0.0244 -0.0036 -0.0425 469 GLY A C   
3208 O O   . GLY A 439 ? 0.2530 0.2750 0.2656 -0.0211 -0.0009 -0.0377 469 GLY A O   
3209 N N   . GLN A 440 ? 0.3244 0.3411 0.3350 -0.0272 -0.0031 -0.0487 470 GLN A N   
3210 C CA  . GLN A 440 ? 0.3329 0.3394 0.3471 -0.0257 0.0007  -0.0497 470 GLN A CA  
3211 C C   . GLN A 440 ? 0.3313 0.3366 0.3399 -0.0206 0.0040  -0.0489 470 GLN A C   
3212 O O   . GLN A 440 ? 0.3090 0.3111 0.3218 -0.0174 0.0067  -0.0449 470 GLN A O   
3213 C CB  . GLN A 440 ? 0.3531 0.3523 0.3684 -0.0291 0.0003  -0.0580 470 GLN A CB  
3214 C CG  . GLN A 440 ? 0.5658 0.5640 0.5894 -0.0349 -0.0024 -0.0588 470 GLN A CG  
3215 C CD  . GLN A 440 ? 0.7495 0.7364 0.7778 -0.0377 -0.0019 -0.0659 470 GLN A CD  
3216 O OE1 . GLN A 440 ? 0.7228 0.7032 0.7480 -0.0347 0.0003  -0.0711 470 GLN A OE1 
3217 N NE2 . GLN A 440 ? 0.7749 0.7596 0.8116 -0.0436 -0.0040 -0.0664 470 GLN A NE2 
3218 N N   . LEU A 441 ? 0.2589 0.2677 0.2582 -0.0200 0.0039  -0.0524 471 LEU A N   
3219 C CA  . LEU A 441 ? 0.2810 0.2898 0.2753 -0.0161 0.0075  -0.0517 471 LEU A CA  
3220 C C   . LEU A 441 ? 0.2456 0.2578 0.2425 -0.0130 0.0080  -0.0438 471 LEU A C   
3221 O O   . LEU A 441 ? 0.2670 0.2766 0.2675 -0.0098 0.0111  -0.0419 471 LEU A O   
3222 C CB  . LEU A 441 ? 0.2598 0.2731 0.2424 -0.0169 0.0070  -0.0553 471 LEU A CB  
3223 C CG  . LEU A 441 ? 0.2839 0.2981 0.2598 -0.0143 0.0113  -0.0555 471 LEU A CG  
3224 C CD1 . LEU A 441 ? 0.2738 0.2904 0.2384 -0.0163 0.0117  -0.0621 471 LEU A CD1 
3225 C CD2 . LEU A 441 ? 0.2441 0.2630 0.2179 -0.0125 0.0108  -0.0476 471 LEU A CD2 
3226 N N   . MET A 442 ? 0.2698 0.2884 0.2657 -0.0136 0.0046  -0.0396 472 MET A N   
3227 C CA  . MET A 442 ? 0.2585 0.2807 0.2564 -0.0105 0.0047  -0.0334 472 MET A CA  
3228 C C   . MET A 442 ? 0.2436 0.2643 0.2503 -0.0092 0.0059  -0.0300 472 MET A C   
3229 O O   . MET A 442 ? 0.2381 0.2586 0.2467 -0.0059 0.0078  -0.0270 472 MET A O   
3230 C CB  . MET A 442 ? 0.2249 0.2541 0.2206 -0.0110 0.0004  -0.0306 472 MET A CB  
3231 C CG  . MET A 442 ? 0.3398 0.3722 0.3367 -0.0075 0.0002  -0.0254 472 MET A CG  
3232 S SD  . MET A 442 ? 0.4006 0.4395 0.3937 -0.0073 -0.0054 -0.0231 472 MET A SD  
3233 C CE  . MET A 442 ? 0.1985 0.2363 0.1816 -0.0107 -0.0068 -0.0279 472 MET A CE  
3234 N N   . SER A 443 ? 0.2709 0.2906 0.2828 -0.0121 0.0047  -0.0302 473 SER A N   
3235 C CA  . SER A 443 ? 0.2666 0.2850 0.2856 -0.0114 0.0059  -0.0260 473 SER A CA  
3236 C C   . SER A 443 ? 0.1928 0.2033 0.2136 -0.0090 0.0088  -0.0266 473 SER A C   
3237 O O   . SER A 443 ? 0.1806 0.1913 0.2044 -0.0060 0.0099  -0.0225 473 SER A O   
3238 C CB  . SER A 443 ? 0.2339 0.2528 0.2579 -0.0161 0.0043  -0.0258 473 SER A CB  
3239 O OG  . SER A 443 ? 0.2378 0.2571 0.2673 -0.0159 0.0055  -0.0204 473 SER A OG  
3240 N N   . SER A 444 ? 0.1999 0.2041 0.2193 -0.0098 0.0099  -0.0322 474 SER A N   
3241 C CA  . SER A 444 ? 0.2573 0.2546 0.2796 -0.0067 0.0125  -0.0337 474 SER A CA  
3242 C C   . SER A 444 ? 0.2341 0.2351 0.2542 -0.0024 0.0145  -0.0326 474 SER A C   
3243 O O   . SER A 444 ? 0.2599 0.2588 0.2845 0.0011  0.0159  -0.0308 474 SER A O   
3244 C CB  . SER A 444 ? 0.2629 0.2538 0.2841 -0.0081 0.0134  -0.0416 474 SER A CB  
3245 O OG  . SER A 444 ? 0.3489 0.3339 0.3746 -0.0119 0.0117  -0.0429 474 SER A OG  
3246 N N   . ALA A 445 ? 0.2323 0.2390 0.2460 -0.0028 0.0145  -0.0335 475 ALA A N   
3247 C CA  . ALA A 445 ? 0.2628 0.2728 0.2754 0.0003  0.0165  -0.0321 475 ALA A CA  
3248 C C   . ALA A 445 ? 0.2510 0.2647 0.2678 0.0025  0.0153  -0.0262 475 ALA A C   
3249 O O   . ALA A 445 ? 0.2284 0.2426 0.2487 0.0057  0.0168  -0.0252 475 ALA A O   
3250 C CB  . ALA A 445 ? 0.2414 0.2556 0.2458 -0.0012 0.0165  -0.0331 475 ALA A CB  
3251 N N   . TRP A 446 ? 0.2125 0.2296 0.2294 0.0010  0.0125  -0.0231 476 TRP A N   
3252 C CA  . TRP A 446 ? 0.2128 0.2341 0.2334 0.0031  0.0115  -0.0185 476 TRP A CA  
3253 C C   . TRP A 446 ? 0.1882 0.2060 0.2137 0.0050  0.0124  -0.0166 476 TRP A C   
3254 O O   . TRP A 446 ? 0.1978 0.2180 0.2257 0.0082  0.0126  -0.0145 476 TRP A O   
3255 C CB  . TRP A 446 ? 0.1618 0.1881 0.1825 0.0010  0.0090  -0.0165 476 TRP A CB  
3256 C CG  . TRP A 446 ? 0.1577 0.1898 0.1761 0.0018  0.0071  -0.0158 476 TRP A CG  
3257 C CD1 . TRP A 446 ? 0.1829 0.2215 0.2040 0.0032  0.0054  -0.0135 476 TRP A CD1 
3258 C CD2 . TRP A 446 ? 0.1834 0.2151 0.1964 0.0015  0.0065  -0.0174 476 TRP A CD2 
3259 N NE1 . TRP A 446 ? 0.1514 0.1924 0.1701 0.0042  0.0035  -0.0137 476 TRP A NE1 
3260 C CE2 . TRP A 446 ? 0.2261 0.2628 0.2395 0.0029  0.0040  -0.0153 476 TRP A CE2 
3261 C CE3 . TRP A 446 ? 0.2806 0.3084 0.2882 0.0001  0.0080  -0.0202 476 TRP A CE3 
3262 C CZ2 . TRP A 446 ? 0.1593 0.1959 0.1679 0.0030  0.0024  -0.0149 476 TRP A CZ2 
3263 C CZ3 . TRP A 446 ? 0.2121 0.2411 0.2137 -0.0002 0.0069  -0.0198 476 TRP A CZ3 
3264 C CH2 . TRP A 446 ? 0.2161 0.2488 0.2182 0.0012  0.0040  -0.0166 476 TRP A CH2 
3265 N N   . VAL A 447 ? 0.1718 0.1837 0.1992 0.0029  0.0125  -0.0172 477 VAL A N   
3266 C CA  . VAL A 447 ? 0.1953 0.2024 0.2273 0.0047  0.0128  -0.0143 477 VAL A CA  
3267 C C   . VAL A 447 ? 0.2095 0.2139 0.2438 0.0090  0.0143  -0.0166 477 VAL A C   
3268 O O   . VAL A 447 ? 0.2158 0.2205 0.2535 0.0124  0.0138  -0.0134 477 VAL A O   
3269 C CB  . VAL A 447 ? 0.2916 0.2911 0.3258 0.0012  0.0124  -0.0145 477 VAL A CB  
3270 C CG1 . VAL A 447 ? 0.2046 0.1968 0.2436 0.0035  0.0125  -0.0113 477 VAL A CG1 
3271 C CG2 . VAL A 447 ? 0.2675 0.2718 0.3015 -0.0031 0.0111  -0.0114 477 VAL A CG2 
3272 N N   . ARG A 448 ? 0.1991 0.2019 0.2317 0.0089  0.0161  -0.0222 478 ARG A N   
3273 C CA  . ARG A 448 ? 0.2170 0.2194 0.2528 0.0127  0.0182  -0.0251 478 ARG A CA  
3274 C C   . ARG A 448 ? 0.2204 0.2303 0.2569 0.0152  0.0181  -0.0228 478 ARG A C   
3275 O O   . ARG A 448 ? 0.1857 0.1966 0.2274 0.0189  0.0184  -0.0227 478 ARG A O   
3276 C CB  . ARG A 448 ? 0.2149 0.2162 0.2477 0.0115  0.0209  -0.0319 478 ARG A CB  
3277 C CG  . ARG A 448 ? 0.2343 0.2274 0.2705 0.0118  0.0217  -0.0366 478 ARG A CG  
3278 C CD  . ARG A 448 ? 0.2463 0.2401 0.2787 0.0109  0.0248  -0.0444 478 ARG A CD  
3279 N NE  . ARG A 448 ? 0.4183 0.4091 0.4455 0.0066  0.0237  -0.0476 478 ARG A NE  
3280 C CZ  . ARG A 448 ? 0.2836 0.2793 0.3023 0.0031  0.0234  -0.0482 478 ARG A CZ  
3281 N NH1 . ARG A 448 ? 0.2750 0.2777 0.2891 0.0034  0.0245  -0.0458 478 ARG A NH1 
3282 N NH2 . ARG A 448 ? 0.3514 0.3447 0.3665 -0.0007 0.0214  -0.0512 478 ARG A NH2 
3283 N N   . PHE A 449 ? 0.1793 0.1944 0.2113 0.0132  0.0173  -0.0213 479 PHE A N   
3284 C CA  . PHE A 449 ? 0.1898 0.2110 0.2232 0.0152  0.0169  -0.0195 479 PHE A CA  
3285 C C   . PHE A 449 ? 0.2165 0.2396 0.2535 0.0178  0.0147  -0.0156 479 PHE A C   
3286 O O   . PHE A 449 ? 0.2071 0.2339 0.2480 0.0209  0.0143  -0.0154 479 PHE A O   
3287 C CB  . PHE A 449 ? 0.1855 0.2105 0.2143 0.0129  0.0159  -0.0185 479 PHE A CB  
3288 C CG  . PHE A 449 ? 0.2239 0.2539 0.2548 0.0147  0.0151  -0.0174 479 PHE A CG  
3289 C CD1 . PHE A 449 ? 0.2170 0.2481 0.2493 0.0149  0.0172  -0.0192 479 PHE A CD1 
3290 C CD2 . PHE A 449 ? 0.1739 0.2080 0.2060 0.0159  0.0126  -0.0149 479 PHE A CD2 
3291 C CE1 . PHE A 449 ? 0.2423 0.2774 0.2778 0.0160  0.0163  -0.0186 479 PHE A CE1 
3292 C CE2 . PHE A 449 ? 0.2157 0.2540 0.2503 0.0175  0.0116  -0.0150 479 PHE A CE2 
3293 C CZ  . PHE A 449 ? 0.2145 0.2528 0.2512 0.0175  0.0133  -0.0168 479 PHE A CZ  
3294 N N   . ALA A 450 ? 0.1633 0.1848 0.1990 0.0164  0.0132  -0.0124 480 ALA A N   
3295 C CA  . ALA A 450 ? 0.2156 0.2395 0.2530 0.0185  0.0113  -0.0079 480 ALA A CA  
3296 C C   . ALA A 450 ? 0.2316 0.2510 0.2734 0.0219  0.0110  -0.0071 480 ALA A C   
3297 O O   . ALA A 450 ? 0.2263 0.2494 0.2700 0.0252  0.0093  -0.0046 480 ALA A O   
3298 C CB  . ALA A 450 ? 0.1591 0.1831 0.1941 0.0153  0.0106  -0.0043 480 ALA A CB  
3299 N N   . LYS A 451 ? 0.2058 0.2174 0.2496 0.0214  0.0123  -0.0096 481 LYS A N   
3300 C CA  . LYS A 451 ? 0.2425 0.2485 0.2916 0.0251  0.0116  -0.0088 481 LYS A CA  
3301 C C   . LYS A 451 ? 0.2474 0.2571 0.3017 0.0293  0.0123  -0.0127 481 LYS A C   
3302 O O   . LYS A 451 ? 0.2337 0.2447 0.2925 0.0336  0.0102  -0.0106 481 LYS A O   
3303 C CB  . LYS A 451 ? 0.2292 0.2250 0.2797 0.0232  0.0125  -0.0110 481 LYS A CB  
3304 C CG  . LYS A 451 ? 0.4180 0.4087 0.4665 0.0194  0.0113  -0.0062 481 LYS A CG  
3305 C CD  . LYS A 451 ? 0.4819 0.4618 0.5330 0.0174  0.0120  -0.0097 481 LYS A CD  
3306 C CE  . LYS A 451 ? 0.3817 0.3555 0.4325 0.0130  0.0108  -0.0044 481 LYS A CE  
3307 N NZ  . LYS A 451 ? 0.3090 0.2728 0.3626 0.0101  0.0114  -0.0096 481 LYS A NZ  
3308 N N   . ASN A 452 ? 0.1805 0.1924 0.2344 0.0279  0.0153  -0.0183 482 ASN A N   
3309 C CA  . ASN A 452 ? 0.2891 0.3046 0.3489 0.0310  0.0171  -0.0228 482 ASN A CA  
3310 C C   . ASN A 452 ? 0.2270 0.2512 0.2860 0.0300  0.0181  -0.0237 482 ASN A C   
3311 O O   . ASN A 452 ? 0.2450 0.2738 0.3098 0.0318  0.0198  -0.0271 482 ASN A O   
3312 C CB  . ASN A 452 ? 0.2277 0.2389 0.2881 0.0300  0.0207  -0.0290 482 ASN A CB  
3313 C CG  . ASN A 452 ? 0.2590 0.2600 0.3198 0.0299  0.0198  -0.0290 482 ASN A CG  
3314 O OD1 . ASN A 452 ? 0.3224 0.3188 0.3868 0.0325  0.0168  -0.0248 482 ASN A OD1 
3315 N ND2 . ASN A 452 ? 0.2735 0.2708 0.3305 0.0266  0.0221  -0.0337 482 ASN A ND2 
3316 N N   . GLY A 453 ? 0.1941 0.2206 0.2472 0.0270  0.0170  -0.0210 483 GLY A N   
3317 C CA  . GLY A 453 ? 0.1928 0.2254 0.2454 0.0256  0.0178  -0.0221 483 GLY A CA  
3318 C C   . GLY A 453 ? 0.2341 0.2660 0.2835 0.0224  0.0215  -0.0253 483 GLY A C   
3319 O O   . GLY A 453 ? 0.2507 0.2869 0.3011 0.0212  0.0229  -0.0261 483 GLY A O   
3320 N N   . ASP A 454 ? 0.2093 0.2361 0.2546 0.0206  0.0231  -0.0270 484 ASP A N   
3321 C CA  . ASP A 454 ? 0.1972 0.2240 0.2384 0.0178  0.0269  -0.0306 484 ASP A CA  
3322 C C   . ASP A 454 ? 0.1878 0.2094 0.2217 0.0150  0.0263  -0.0312 484 ASP A C   
3323 O O   . ASP A 454 ? 0.1956 0.2121 0.2313 0.0160  0.0256  -0.0324 484 ASP A O   
3324 C CB  . ASP A 454 ? 0.2245 0.2527 0.2720 0.0201  0.0305  -0.0355 484 ASP A CB  
3325 C CG  . ASP A 454 ? 0.2648 0.2957 0.3080 0.0171  0.0354  -0.0392 484 ASP A CG  
3326 O OD1 . ASP A 454 ? 0.2102 0.2392 0.2440 0.0134  0.0356  -0.0386 484 ASP A OD1 
3327 O OD2 . ASP A 454 ? 0.2651 0.3008 0.3145 0.0184  0.0390  -0.0428 484 ASP A OD2 
3328 N N   . PRO A 455 ? 0.1854 0.2079 0.2117 0.0116  0.0263  -0.0303 485 PRO A N   
3329 C CA  . PRO A 455 ? 0.2119 0.2309 0.2317 0.0088  0.0250  -0.0312 485 PRO A CA  
3330 C C   . PRO A 455 ? 0.2517 0.2685 0.2681 0.0076  0.0281  -0.0372 485 PRO A C   
3331 O O   . PRO A 455 ? 0.2255 0.2394 0.2372 0.0053  0.0268  -0.0391 485 PRO A O   
3332 C CB  . PRO A 455 ? 0.2265 0.2482 0.2400 0.0064  0.0231  -0.0279 485 PRO A CB  
3333 C CG  . PRO A 455 ? 0.2204 0.2456 0.2347 0.0067  0.0255  -0.0271 485 PRO A CG  
3334 C CD  . PRO A 455 ? 0.1858 0.2123 0.2095 0.0101  0.0267  -0.0279 485 PRO A CD  
3335 N N   . ALA A 456 ? 0.2166 0.2357 0.2357 0.0090  0.0323  -0.0407 486 ALA A N   
3336 C CA  . ALA A 456 ? 0.2662 0.2844 0.2822 0.0082  0.0358  -0.0475 486 ALA A CA  
3337 C C   . ALA A 456 ? 0.2622 0.2740 0.2845 0.0106  0.0349  -0.0515 486 ALA A C   
3338 O O   . ALA A 456 ? 0.2651 0.2740 0.2954 0.0137  0.0327  -0.0487 486 ALA A O   
3339 C CB  . ALA A 456 ? 0.1949 0.2190 0.2129 0.0089  0.0412  -0.0505 486 ALA A CB  
3340 N N   . GLY A 457 ? 0.2823 0.2913 0.3005 0.0092  0.0363  -0.0581 487 GLY A N   
3341 C CA  . GLY A 457 ? 0.3805 0.3821 0.4051 0.0112  0.0357  -0.0630 487 GLY A CA  
3342 C C   . GLY A 457 ? 0.4282 0.4305 0.4511 0.0116  0.0401  -0.0728 487 GLY A C   
3343 O O   . GLY A 457 ? 0.3784 0.3882 0.3947 0.0101  0.0440  -0.0752 487 GLY A O   
3344 N N   . ASP A 458 ? 0.4505 0.4451 0.4798 0.0137  0.0394  -0.0786 488 ASP A N   
3345 C CA  . ASP A 458 ? 0.5065 0.5013 0.5356 0.0147  0.0434  -0.0897 488 ASP A CA  
3346 C C   . ASP A 458 ? 0.4727 0.4700 0.4886 0.0098  0.0440  -0.0946 488 ASP A C   
3347 O O   . ASP A 458 ? 0.5347 0.5354 0.5474 0.0101  0.0482  -0.1040 488 ASP A O   
3348 C CB  . ASP A 458 ? 0.4975 0.4814 0.5374 0.0183  0.0417  -0.0947 488 ASP A CB  
3349 C CG  . ASP A 458 ? 0.6192 0.6019 0.6722 0.0245  0.0418  -0.0920 488 ASP A CG  
3350 O OD1 . ASP A 458 ? 0.6547 0.6462 0.7086 0.0258  0.0436  -0.0876 488 ASP A OD1 
3351 O OD2 . ASP A 458 ? 0.7567 0.7295 0.8194 0.0281  0.0397  -0.0943 488 ASP A OD2 
3352 N N   . ALA A 459 ? 0.4661 0.4630 0.4745 0.0054  0.0399  -0.0889 489 ALA A N   
3353 C CA  . ALA A 459 ? 0.4632 0.4634 0.4587 0.0008  0.0392  -0.0927 489 ALA A CA  
3354 C C   . ALA A 459 ? 0.4274 0.4351 0.4129 -0.0020 0.0382  -0.0845 489 ALA A C   
3355 O O   . ALA A 459 ? 0.5318 0.5426 0.5058 -0.0057 0.0366  -0.0858 489 ALA A O   
3356 C CB  . ALA A 459 ? 0.4851 0.4776 0.4817 -0.0020 0.0342  -0.0952 489 ALA A CB  
3357 N N   . LEU A 460 ? 0.3599 0.3702 0.3495 -0.0003 0.0387  -0.0764 490 LEU A N   
3358 C CA  . LEU A 460 ? 0.3678 0.3834 0.3497 -0.0026 0.0374  -0.0684 490 LEU A CA  
3359 C C   . LEU A 460 ? 0.3949 0.4158 0.3797 -0.0008 0.0418  -0.0653 490 LEU A C   
3360 O O   . LEU A 460 ? 0.3624 0.3821 0.3568 0.0019  0.0411  -0.0610 490 LEU A O   
3361 C CB  . LEU A 460 ? 0.3516 0.3643 0.3369 -0.0032 0.0316  -0.0611 490 LEU A CB  
3362 C CG  . LEU A 460 ? 0.3680 0.3853 0.3457 -0.0053 0.0291  -0.0539 490 LEU A CG  
3363 C CD1 . LEU A 460 ? 0.3190 0.3390 0.2840 -0.0087 0.0277  -0.0567 490 LEU A CD1 
3364 C CD2 . LEU A 460 ? 0.2646 0.2804 0.2480 -0.0049 0.0242  -0.0476 490 LEU A CD2 
3365 N N   . THR A 461 ? 0.3697 0.3967 0.3460 -0.0027 0.0464  -0.0674 491 THR A N   
3366 C CA  . THR A 461 ? 0.3427 0.3755 0.3214 -0.0024 0.0510  -0.0640 491 THR A CA  
3367 C C   . THR A 461 ? 0.3763 0.4094 0.3518 -0.0042 0.0475  -0.0541 491 THR A C   
3368 O O   . THR A 461 ? 0.3410 0.3743 0.3053 -0.0072 0.0449  -0.0508 491 THR A O   
3369 C CB  . THR A 461 ? 0.3643 0.4041 0.3343 -0.0045 0.0575  -0.0690 491 THR A CB  
3370 O OG1 . THR A 461 ? 0.4179 0.4572 0.3905 -0.0025 0.0603  -0.0797 491 THR A OG1 
3371 C CG2 . THR A 461 ? 0.3345 0.3808 0.3100 -0.0045 0.0630  -0.0661 491 THR A CG2 
3372 N N   . TRP A 462 ? 0.3055 0.3388 0.2911 -0.0021 0.0471  -0.0496 492 TRP A N   
3373 C CA  . TRP A 462 ? 0.2718 0.3046 0.2566 -0.0032 0.0436  -0.0412 492 TRP A CA  
3374 C C   . TRP A 462 ? 0.3018 0.3381 0.2954 -0.0023 0.0465  -0.0388 492 TRP A C   
3375 O O   . TRP A 462 ? 0.2267 0.2621 0.2310 0.0009  0.0444  -0.0380 492 TRP A O   
3376 C CB  . TRP A 462 ? 0.2336 0.2617 0.2222 -0.0015 0.0372  -0.0385 492 TRP A CB  
3377 C CG  . TRP A 462 ? 0.1954 0.2232 0.1820 -0.0024 0.0330  -0.0313 492 TRP A CG  
3378 C CD1 . TRP A 462 ? 0.2157 0.2453 0.2002 -0.0039 0.0340  -0.0265 492 TRP A CD1 
3379 C CD2 . TRP A 462 ? 0.1903 0.2159 0.1779 -0.0017 0.0273  -0.0284 492 TRP A CD2 
3380 N NE1 . TRP A 462 ? 0.1919 0.2197 0.1763 -0.0036 0.0289  -0.0212 492 TRP A NE1 
3381 C CE2 . TRP A 462 ? 0.2549 0.2812 0.2413 -0.0021 0.0249  -0.0225 492 TRP A CE2 
3382 C CE3 . TRP A 462 ? 0.2083 0.2316 0.1984 -0.0010 0.0242  -0.0302 492 TRP A CE3 
3383 C CZ2 . TRP A 462 ? 0.2497 0.2755 0.2375 -0.0012 0.0196  -0.0193 492 TRP A CZ2 
3384 C CZ3 . TRP A 462 ? 0.1952 0.2186 0.1863 -0.0009 0.0194  -0.0264 492 TRP A CZ3 
3385 C CH2 . TRP A 462 ? 0.2111 0.2363 0.2012 -0.0006 0.0171  -0.0214 492 TRP A CH2 
3386 N N   . PRO A 463 ? 0.2975 0.3383 0.2870 -0.0053 0.0512  -0.0375 493 PRO A N   
3387 C CA  . PRO A 463 ? 0.2832 0.3277 0.2819 -0.0054 0.0538  -0.0351 493 PRO A CA  
3388 C C   . PRO A 463 ? 0.2439 0.2850 0.2450 -0.0056 0.0486  -0.0281 493 PRO A C   
3389 O O   . PRO A 463 ? 0.2407 0.2776 0.2340 -0.0066 0.0442  -0.0239 493 PRO A O   
3390 C CB  . PRO A 463 ? 0.2930 0.3430 0.2847 -0.0099 0.0604  -0.0349 493 PRO A CB  
3391 C CG  . PRO A 463 ? 0.3192 0.3667 0.2949 -0.0124 0.0590  -0.0336 493 PRO A CG  
3392 C CD  . PRO A 463 ? 0.2722 0.3156 0.2481 -0.0092 0.0546  -0.0383 493 PRO A CD  
3393 N N   . ALA A 464 ? 0.2423 0.2858 0.2550 -0.0043 0.0490  -0.0275 494 ALA A N   
3394 C CA  . ALA A 464 ? 0.2575 0.2983 0.2740 -0.0041 0.0444  -0.0224 494 ALA A CA  
3395 C C   . ALA A 464 ? 0.2154 0.2540 0.2242 -0.0086 0.0448  -0.0164 494 ALA A C   
3396 O O   . ALA A 464 ? 0.2292 0.2703 0.2321 -0.0124 0.0500  -0.0157 494 ALA A O   
3397 C CB  . ALA A 464 ? 0.2680 0.3130 0.2984 -0.0023 0.0450  -0.0241 494 ALA A CB  
3398 N N   . TYR A 465 ? 0.2016 0.2355 0.2106 -0.0080 0.0393  -0.0119 495 TYR A N   
3399 C CA  . TYR A 465 ? 0.2035 0.2335 0.2065 -0.0115 0.0384  -0.0054 495 TYR A CA  
3400 C C   . TYR A 465 ? 0.2448 0.2769 0.2537 -0.0153 0.0431  -0.0037 495 TYR A C   
3401 O O   . TYR A 465 ? 0.2101 0.2397 0.2123 -0.0197 0.0449  0.0019  495 TYR A O   
3402 C CB  . TYR A 465 ? 0.1912 0.2161 0.1963 -0.0090 0.0313  -0.0023 495 TYR A CB  
3403 C CG  . TYR A 465 ? 0.2030 0.2222 0.2027 -0.0118 0.0292  0.0048  495 TYR A CG  
3404 C CD1 . TYR A 465 ? 0.2109 0.2277 0.1974 -0.0135 0.0281  0.0087  495 TYR A CD1 
3405 C CD2 . TYR A 465 ? 0.2007 0.2165 0.2087 -0.0126 0.0278  0.0074  495 TYR A CD2 
3406 C CE1 . TYR A 465 ? 0.2213 0.2321 0.2026 -0.0156 0.0256  0.0162  495 TYR A CE1 
3407 C CE2 . TYR A 465 ? 0.2424 0.2512 0.2461 -0.0149 0.0255  0.0144  495 TYR A CE2 
3408 C CZ  . TYR A 465 ? 0.2944 0.3006 0.2846 -0.0163 0.0243  0.0193  495 TYR A CZ  
3409 O OH  . TYR A 465 ? 0.2779 0.2765 0.2635 -0.0182 0.0214  0.0272  495 TYR A OH  
3410 N N   . SER A 466 ? 0.2756 0.3127 0.2971 -0.0139 0.0450  -0.0081 496 SER A N   
3411 C CA  . SER A 466 ? 0.2695 0.3102 0.2987 -0.0180 0.0498  -0.0073 496 SER A CA  
3412 C C   . SER A 466 ? 0.2939 0.3398 0.3169 -0.0223 0.0576  -0.0076 496 SER A C   
3413 O O   . SER A 466 ? 0.2431 0.2917 0.2695 -0.0273 0.0624  -0.0050 496 SER A O   
3414 C CB  . SER A 466 ? 0.3052 0.3516 0.3498 -0.0149 0.0493  -0.0129 496 SER A CB  
3415 O OG  . SER A 466 ? 0.4288 0.4796 0.4747 -0.0107 0.0502  -0.0186 496 SER A OG  
3416 N N   . THR A 467 ? 0.2639 0.3118 0.2781 -0.0207 0.0593  -0.0109 497 THR A N   
3417 C CA  . THR A 467 ? 0.2365 0.2902 0.2430 -0.0243 0.0669  -0.0124 497 THR A CA  
3418 C C   . THR A 467 ? 0.2531 0.3018 0.2422 -0.0278 0.0660  -0.0058 497 THR A C   
3419 O O   . THR A 467 ? 0.2534 0.2993 0.2326 -0.0256 0.0626  -0.0070 497 THR A O   
3420 C CB  . THR A 467 ? 0.2602 0.3189 0.2677 -0.0203 0.0691  -0.0210 497 THR A CB  
3421 O OG1 . THR A 467 ? 0.2597 0.3231 0.2834 -0.0167 0.0695  -0.0263 497 THR A OG1 
3422 C CG2 . THR A 467 ? 0.2789 0.3444 0.2777 -0.0237 0.0770  -0.0237 497 THR A CG2 
3423 N N   . GLY A 468 ? 0.3095 0.3570 0.2952 -0.0335 0.0688  0.0013  498 GLY A N   
3424 C CA  . GLY A 468 ? 0.2555 0.2989 0.2239 -0.0371 0.0683  0.0086  498 GLY A CA  
3425 C C   . GLY A 468 ? 0.3205 0.3549 0.2823 -0.0339 0.0590  0.0125  498 GLY A C   
3426 O O   . GLY A 468 ? 0.2642 0.2971 0.2107 -0.0346 0.0574  0.0151  498 GLY A O   
3427 N N   . LYS A 469 ? 0.2425 0.2718 0.2155 -0.0302 0.0529  0.0124  499 LYS A N   
3428 C CA  . LYS A 469 ? 0.2401 0.2623 0.2094 -0.0266 0.0443  0.0153  499 LYS A CA  
3429 C C   . LYS A 469 ? 0.2665 0.2909 0.2268 -0.0237 0.0422  0.0108  499 LYS A C   
3430 O O   . LYS A 469 ? 0.2836 0.3042 0.2351 -0.0227 0.0366  0.0142  499 LYS A O   
3431 C CB  . LYS A 469 ? 0.2935 0.3082 0.2546 -0.0296 0.0412  0.0253  499 LYS A CB  
3432 C CG  . LYS A 469 ? 0.3614 0.3708 0.3337 -0.0317 0.0409  0.0298  499 LYS A CG  
3433 C CD  . LYS A 469 ? 0.3404 0.3413 0.3039 -0.0353 0.0387  0.0407  499 LYS A CD  
3434 C CE  . LYS A 469 ? 0.4941 0.4871 0.4705 -0.0361 0.0360  0.0443  499 LYS A CE  
3435 N NZ  . LYS A 469 ? 0.5512 0.5497 0.5415 -0.0387 0.0419  0.0394  499 LYS A NZ  
3436 N N   . SER A 470 ? 0.2578 0.2884 0.2213 -0.0224 0.0464  0.0028  500 SER A N   
3437 C CA  . SER A 470 ? 0.2551 0.2873 0.2115 -0.0202 0.0449  -0.0025 500 SER A CA  
3438 C C   . SER A 470 ? 0.2805 0.3084 0.2404 -0.0161 0.0369  -0.0024 500 SER A C   
3439 O O   . SER A 470 ? 0.3009 0.3277 0.2727 -0.0132 0.0347  -0.0035 500 SER A O   
3440 C CB  . SER A 470 ? 0.2824 0.3204 0.2451 -0.0188 0.0502  -0.0113 500 SER A CB  
3441 O OG  . SER A 470 ? 0.2440 0.2879 0.2038 -0.0225 0.0582  -0.0123 500 SER A OG  
3442 N N   . THR A 471 ? 0.2734 0.3001 0.2226 -0.0161 0.0327  -0.0014 501 THR A N   
3443 C CA  . THR A 471 ? 0.2407 0.2648 0.1926 -0.0129 0.0254  -0.0012 501 THR A CA  
3444 C C   . THR A 471 ? 0.2870 0.3133 0.2320 -0.0127 0.0240  -0.0065 501 THR A C   
3445 O O   . THR A 471 ? 0.2624 0.2903 0.1947 -0.0152 0.0246  -0.0062 501 THR A O   
3446 C CB  . THR A 471 ? 0.3092 0.3291 0.2570 -0.0130 0.0198  0.0067  501 THR A CB  
3447 O OG1 . THR A 471 ? 0.2764 0.2931 0.2305 -0.0139 0.0214  0.0114  501 THR A OG1 
3448 C CG2 . THR A 471 ? 0.2637 0.2827 0.2171 -0.0092 0.0127  0.0061  501 THR A CG2 
3449 N N   . MET A 472 ? 0.2386 0.2651 0.1918 -0.0101 0.0222  -0.0112 502 MET A N   
3450 C CA  . MET A 472 ? 0.2635 0.2913 0.2124 -0.0103 0.0204  -0.0166 502 MET A CA  
3451 C C   . MET A 472 ? 0.2537 0.2814 0.1972 -0.0103 0.0133  -0.0133 502 MET A C   
3452 O O   . MET A 472 ? 0.2864 0.3132 0.2369 -0.0081 0.0090  -0.0100 502 MET A O   
3453 C CB  . MET A 472 ? 0.2121 0.2391 0.1721 -0.0079 0.0207  -0.0216 502 MET A CB  
3454 C CG  . MET A 472 ? 0.2566 0.2836 0.2145 -0.0086 0.0185  -0.0269 502 MET A CG  
3455 S SD  . MET A 472 ? 0.3190 0.3475 0.2673 -0.0109 0.0234  -0.0342 502 MET A SD  
3456 C CE  . MET A 472 ? 0.2586 0.2861 0.2186 -0.0085 0.0297  -0.0385 502 MET A CE  
3457 N N   . THR A 473 ? 0.3054 0.3351 0.2369 -0.0125 0.0119  -0.0146 503 THR A N   
3458 C CA  . THR A 473 ? 0.2908 0.3218 0.2174 -0.0123 0.0046  -0.0124 503 THR A CA  
3459 C C   . THR A 473 ? 0.3245 0.3576 0.2533 -0.0128 0.0027  -0.0198 503 THR A C   
3460 O O   . THR A 473 ? 0.3480 0.3820 0.2717 -0.0147 0.0060  -0.0262 503 THR A O   
3461 C CB  . THR A 473 ? 0.3156 0.3478 0.2266 -0.0146 0.0033  -0.0082 503 THR A CB  
3462 O OG1 . THR A 473 ? 0.4454 0.4808 0.3465 -0.0172 0.0067  -0.0147 503 THR A OG1 
3463 C CG2 . THR A 473 ? 0.2759 0.3051 0.1848 -0.0153 0.0068  -0.0010 503 THR A CG2 
3464 N N   . PHE A 474 ? 0.2981 0.3320 0.2355 -0.0113 -0.0023 -0.0194 504 PHE A N   
3465 C CA  . PHE A 474 ? 0.3525 0.3886 0.2928 -0.0126 -0.0050 -0.0255 504 PHE A CA  
3466 C C   . PHE A 474 ? 0.3114 0.3518 0.2427 -0.0137 -0.0115 -0.0247 504 PHE A C   
3467 O O   . PHE A 474 ? 0.2885 0.3320 0.2241 -0.0124 -0.0174 -0.0218 504 PHE A O   
3468 C CB  . PHE A 474 ? 0.2519 0.2880 0.2063 -0.0109 -0.0062 -0.0252 504 PHE A CB  
3469 C CG  . PHE A 474 ? 0.3137 0.3460 0.2760 -0.0094 -0.0006 -0.0254 504 PHE A CG  
3470 C CD1 . PHE A 474 ? 0.2760 0.3053 0.2398 -0.0104 0.0038  -0.0310 504 PHE A CD1 
3471 C CD2 . PHE A 474 ? 0.2685 0.3004 0.2372 -0.0066 -0.0001 -0.0205 504 PHE A CD2 
3472 C CE1 . PHE A 474 ? 0.2382 0.2645 0.2095 -0.0084 0.0081  -0.0309 504 PHE A CE1 
3473 C CE2 . PHE A 474 ? 0.2662 0.2955 0.2418 -0.0051 0.0043  -0.0209 504 PHE A CE2 
3474 C CZ  . PHE A 474 ? 0.2530 0.2798 0.2299 -0.0059 0.0082  -0.0257 504 PHE A CZ  
3475 N N   . GLY A 475 ? 0.5823 0.6238 0.5006 -0.0161 -0.0103 -0.0278 505 GLY A N   
3476 C CA  . GLY A 475 ? 0.3936 0.4394 0.3000 -0.0170 -0.0163 -0.0261 505 GLY A CA  
3477 C C   . GLY A 475 ? 0.4972 0.5476 0.4049 -0.0189 -0.0215 -0.0329 505 GLY A C   
3478 O O   . GLY A 475 ? 0.5355 0.5859 0.4562 -0.0190 -0.0222 -0.0363 505 GLY A O   
3479 N N   . PRO A 476 ? 0.3794 0.4341 0.2735 -0.0207 -0.0253 -0.0350 506 PRO A N   
3480 C CA  . PRO A 476 ? 0.4145 0.4746 0.3097 -0.0228 -0.0314 -0.0418 506 PRO A CA  
3481 C C   . PRO A 476 ? 0.4235 0.4818 0.3202 -0.0258 -0.0273 -0.0528 506 PRO A C   
3482 O O   . PRO A 476 ? 0.4012 0.4547 0.2968 -0.0259 -0.0198 -0.0554 506 PRO A O   
3483 C CB  . PRO A 476 ? 0.4568 0.5223 0.3350 -0.0232 -0.0373 -0.0392 506 PRO A CB  
3484 C CG  . PRO A 476 ? 0.4701 0.5322 0.3353 -0.0233 -0.0307 -0.0354 506 PRO A CG  
3485 C CD  . PRO A 476 ? 0.4310 0.4864 0.3077 -0.0212 -0.0244 -0.0306 506 PRO A CD  
3486 N N   . GLU A 477 ? 0.4049 0.4674 0.3056 -0.0283 -0.0326 -0.0596 507 GLU A N   
3487 C CA  . GLU A 477 ? 0.4280 0.4887 0.3296 -0.0317 -0.0305 -0.0711 507 GLU A CA  
3488 C C   . GLU A 477 ? 0.3801 0.4324 0.2948 -0.0313 -0.0235 -0.0734 507 GLU A C   
3489 O O   . GLU A 477 ? 0.3623 0.4104 0.2760 -0.0326 -0.0190 -0.0816 507 GLU A O   
3490 C CB  . GLU A 477 ? 0.4603 0.5229 0.3437 -0.0329 -0.0285 -0.0765 507 GLU A CB  
3491 C CG  . GLU A 477 ? 0.5938 0.6652 0.4636 -0.0336 -0.0366 -0.0750 507 GLU A CG  
3492 C CD  . GLU A 477 ? 0.6081 0.6826 0.4574 -0.0346 -0.0344 -0.0781 507 GLU A CD  
3493 O OE1 . GLU A 477 ? 0.7669 0.8374 0.6133 -0.0346 -0.0259 -0.0817 507 GLU A OE1 
3494 O OE2 . GLU A 477 ? 0.6621 0.7439 0.4981 -0.0352 -0.0412 -0.0769 507 GLU A OE2 
3495 N N   . GLY A 478 ? 0.3330 0.3832 0.2601 -0.0293 -0.0228 -0.0663 508 GLY A N   
3496 C CA  . GLY A 478 ? 0.3198 0.3626 0.2593 -0.0288 -0.0172 -0.0671 508 GLY A CA  
3497 C C   . GLY A 478 ? 0.3461 0.3834 0.2815 -0.0266 -0.0098 -0.0675 508 GLY A C   
3498 O O   . GLY A 478 ? 0.3833 0.4143 0.3270 -0.0264 -0.0054 -0.0710 508 GLY A O   
3499 N N   . ARG A 479 ? 0.2959 0.3359 0.2195 -0.0251 -0.0082 -0.0635 509 ARG A N   
3500 C CA  . ARG A 479 ? 0.4230 0.4600 0.3425 -0.0236 -0.0008 -0.0641 509 ARG A CA  
3501 C C   . ARG A 479 ? 0.3288 0.3652 0.2504 -0.0208 0.0014  -0.0542 509 ARG A C   
3502 O O   . ARG A 479 ? 0.3528 0.3916 0.2744 -0.0200 -0.0031 -0.0469 509 ARG A O   
3503 C CB  . ARG A 479 ? 0.4142 0.4554 0.3169 -0.0252 0.0005  -0.0687 509 ARG A CB  
3504 C CG  . ARG A 479 ? 0.5727 0.6152 0.4720 -0.0280 -0.0018 -0.0801 509 ARG A CG  
3505 C CD  . ARG A 479 ? 0.5504 0.5963 0.4348 -0.0289 0.0027  -0.0867 509 ARG A CD  
3506 N NE  . ARG A 479 ? 0.7265 0.7766 0.6023 -0.0318 -0.0019 -0.0960 509 ARG A NE  
3507 C CZ  . ARG A 479 ? 0.8812 0.9388 0.7418 -0.0334 -0.0070 -0.0940 509 ARG A CZ  
3508 N NH1 . ARG A 479 ? 0.8935 0.9541 0.7457 -0.0323 -0.0080 -0.0826 509 ARG A NH1 
3509 N NH2 . ARG A 479 ? 0.8495 0.9113 0.7032 -0.0360 -0.0116 -0.1037 509 ARG A NH2 
3510 N N   . ALA A 480 ? 0.3143 0.3477 0.2386 -0.0193 0.0082  -0.0547 510 ALA A N   
3511 C CA  . ALA A 480 ? 0.3969 0.4295 0.3239 -0.0171 0.0111  -0.0468 510 ALA A CA  
3512 C C   . ALA A 480 ? 0.3726 0.4070 0.2911 -0.0177 0.0176  -0.0481 510 ALA A C   
3513 O O   . ALA A 480 ? 0.4668 0.5018 0.3820 -0.0185 0.0214  -0.0564 510 ALA A O   
3514 C CB  . ALA A 480 ? 0.2919 0.3203 0.2341 -0.0147 0.0129  -0.0457 510 ALA A CB  
3515 N N   . ALA A 481 ? 0.3304 0.3656 0.2458 -0.0173 0.0191  -0.0402 511 ALA A N   
3516 C CA  . ALA A 481 ? 0.3504 0.3883 0.2581 -0.0186 0.0259  -0.0404 511 ALA A CA  
3517 C C   . ALA A 481 ? 0.3352 0.3720 0.2464 -0.0181 0.0276  -0.0313 511 ALA A C   
3518 O O   . ALA A 481 ? 0.3036 0.3384 0.2160 -0.0174 0.0223  -0.0240 511 ALA A O   
3519 C CB  . ALA A 481 ? 0.3153 0.3580 0.2049 -0.0216 0.0252  -0.0414 511 ALA A CB  
3520 N N   . VAL A 482 ? 0.2930 0.3315 0.2067 -0.0185 0.0349  -0.0324 512 VAL A N   
3521 C CA  . VAL A 482 ? 0.3448 0.3825 0.2635 -0.0186 0.0372  -0.0249 512 VAL A CA  
3522 C C   . VAL A 482 ? 0.3028 0.3421 0.2073 -0.0222 0.0379  -0.0176 512 VAL A C   
3523 O O   . VAL A 482 ? 0.3694 0.4131 0.2607 -0.0248 0.0410  -0.0202 512 VAL A O   
3524 C CB  . VAL A 482 ? 0.3641 0.4042 0.2930 -0.0178 0.0446  -0.0293 512 VAL A CB  
3525 C CG1 . VAL A 482 ? 0.3428 0.3829 0.2767 -0.0189 0.0472  -0.0222 512 VAL A CG1 
3526 C CG2 . VAL A 482 ? 0.2883 0.3256 0.2310 -0.0139 0.0430  -0.0347 512 VAL A CG2 
3527 N N   . VAL A 483 ? 0.3436 0.3791 0.2505 -0.0223 0.0349  -0.0085 513 VAL A N   
3528 C CA  . VAL A 483 ? 0.3186 0.3536 0.2139 -0.0257 0.0354  0.0004  513 VAL A CA  
3529 C C   . VAL A 483 ? 0.3261 0.3594 0.2307 -0.0270 0.0401  0.0051  513 VAL A C   
3530 O O   . VAL A 483 ? 0.3357 0.3654 0.2544 -0.0243 0.0378  0.0056  513 VAL A O   
3531 C CB  . VAL A 483 ? 0.3751 0.4058 0.2647 -0.0245 0.0262  0.0075  513 VAL A CB  
3532 C CG1 . VAL A 483 ? 0.4310 0.4585 0.3119 -0.0275 0.0261  0.0186  513 VAL A CG1 
3533 C CG2 . VAL A 483 ? 0.4403 0.4745 0.3185 -0.0245 0.0220  0.0030  513 VAL A CG2 
3534 N N   . SER A 484 ? 0.3383 0.3749 0.2350 -0.0315 0.0468  0.0082  514 SER A N   
3535 C CA  . SER A 484 ? 0.3782 0.4141 0.2837 -0.0340 0.0519  0.0127  514 SER A CA  
3536 C C   . SER A 484 ? 0.3874 0.4223 0.2794 -0.0395 0.0542  0.0228  514 SER A C   
3537 O O   . SER A 484 ? 0.3800 0.4212 0.2581 -0.0430 0.0595  0.0219  514 SER A O   
3538 C CB  . SER A 484 ? 0.3642 0.4076 0.2788 -0.0342 0.0603  0.0042  514 SER A CB  
3539 O OG  . SER A 484 ? 0.4628 0.5074 0.3853 -0.0377 0.0658  0.0083  514 SER A OG  
3540 N N   . PRO A 485 ? 0.4035 0.4305 0.2989 -0.0405 0.0504  0.0326  515 PRO A N   
3541 C CA  . PRO A 485 ? 0.3631 0.3827 0.2738 -0.0366 0.0441  0.0338  515 PRO A CA  
3542 C C   . PRO A 485 ? 0.4017 0.4175 0.3101 -0.0316 0.0345  0.0334  515 PRO A C   
3543 O O   . PRO A 485 ? 0.4610 0.4778 0.3550 -0.0319 0.0314  0.0353  515 PRO A O   
3544 C CB  . PRO A 485 ? 0.4049 0.4175 0.3162 -0.0407 0.0443  0.0447  515 PRO A CB  
3545 C CG  . PRO A 485 ? 0.4521 0.4650 0.3430 -0.0449 0.0453  0.0523  515 PRO A CG  
3546 C CD  . PRO A 485 ? 0.3889 0.4131 0.2714 -0.0461 0.0522  0.0438  515 PRO A CD  
3547 N N   . GLY A 486 ? 0.4030 0.4156 0.3255 -0.0271 0.0297  0.0307  516 GLY A N   
3548 C CA  . GLY A 486 ? 0.3812 0.3923 0.3037 -0.0225 0.0215  0.0291  516 GLY A CA  
3549 C C   . GLY A 486 ? 0.4222 0.4259 0.3422 -0.0212 0.0139  0.0379  516 GLY A C   
3550 O O   . GLY A 486 ? 0.4713 0.4704 0.3844 -0.0245 0.0145  0.0466  516 GLY A O   
3551 N N   . PRO A 487 ? 0.5246 0.5273 0.4511 -0.0162 0.0067  0.0360  517 PRO A N   
3552 C CA  . PRO A 487 ? 0.5864 0.5828 0.5118 -0.0138 -0.0013 0.0433  517 PRO A CA  
3553 C C   . PRO A 487 ? 0.6476 0.6356 0.5817 -0.0143 -0.0014 0.0492  517 PRO A C   
3554 O O   . PRO A 487 ? 0.5951 0.5831 0.5410 -0.0147 0.0027  0.0454  517 PRO A O   
3555 C CB  . PRO A 487 ? 0.5331 0.5327 0.4674 -0.0084 -0.0073 0.0374  517 PRO A CB  
3556 C CG  . PRO A 487 ? 0.5097 0.5138 0.4539 -0.0081 -0.0019 0.0290  517 PRO A CG  
3557 C CD  . PRO A 487 ? 0.4940 0.5013 0.4302 -0.0126 0.0059  0.0271  517 PRO A CD  
3558 N N   . SER A 488 ? 0.7112 0.6917 0.6396 -0.0142 -0.0066 0.0585  518 SER A N   
3559 C CA  . SER A 488 ? 0.7567 0.7271 0.6928 -0.0150 -0.0075 0.0651  518 SER A CA  
3560 C C   . SER A 488 ? 0.7519 0.7148 0.6881 -0.0105 -0.0174 0.0715  518 SER A C   
3561 O O   . SER A 488 ? 0.7443 0.7076 0.6673 -0.0102 -0.0217 0.0768  518 SER A O   
3562 C CB  . SER A 488 ? 0.6576 0.6250 0.5848 -0.0223 -0.0008 0.0725  518 SER A CB  
3563 O OG  . SER A 488 ? 0.7496 0.7058 0.6844 -0.0238 -0.0022 0.0796  518 SER A OG  
3564 N N   . ILE A 489 ? 0.7048 0.6613 0.6560 -0.0068 -0.0212 0.0706  519 ILE A N   
3565 C CA  . ILE A 489 ? 0.7252 0.6732 0.6791 -0.0020 -0.0305 0.0766  519 ILE A CA  
3566 C C   . ILE A 489 ? 0.8179 0.7547 0.7625 -0.0064 -0.0308 0.0896  519 ILE A C   
3567 O O   . ILE A 489 ? 0.7567 0.6916 0.6986 -0.0131 -0.0232 0.0924  519 ILE A O   
3568 C CB  . ILE A 489 ? 0.6269 0.5711 0.6001 0.0032  -0.0338 0.0711  519 ILE A CB  
3569 C CG1 . ILE A 489 ? 0.7495 0.6869 0.7312 -0.0012 -0.0283 0.0716  519 ILE A CG1 
3570 C CG2 . ILE A 489 ? 0.6370 0.5931 0.6178 0.0073  -0.0334 0.0594  519 ILE A CG2 
3571 C CD1 . ILE A 489 ? 0.8366 0.7690 0.8365 0.0035  -0.0320 0.0663  519 ILE A CD1 
3572 N N   . PRO A 490 ? 0.8497 0.7793 0.7892 -0.0032 -0.0393 0.0981  520 PRO A N   
3573 C CA  . PRO A 490 ? 0.8118 0.7289 0.7426 -0.0074 -0.0402 0.1120  520 PRO A CA  
3574 C C   . PRO A 490 ? 0.8161 0.7216 0.7612 -0.0098 -0.0377 0.1136  520 PRO A C   
3575 O O   . PRO A 490 ? 0.7689 0.6713 0.7312 -0.0044 -0.0414 0.1070  520 PRO A O   
3576 C CB  . PRO A 490 ? 0.7555 0.6670 0.6829 -0.0010 -0.0519 0.1188  520 PRO A CB  
3577 C CG  . PRO A 490 ? 0.7235 0.6490 0.6510 0.0043  -0.0551 0.1090  520 PRO A CG  
3578 C CD  . PRO A 490 ? 0.7024 0.6359 0.6434 0.0044  -0.0487 0.0958  520 PRO A CD  
3579 N N   . PRO A 491 ? 0.8497 0.7495 0.7886 -0.0180 -0.0312 0.1217  521 PRO A N   
3580 C CA  . PRO A 491 ? 0.8400 0.7289 0.7936 -0.0213 -0.0286 0.1230  521 PRO A CA  
3581 C C   . PRO A 491 ? 0.8539 0.7270 0.8188 -0.0159 -0.0382 0.1277  521 PRO A C   
3582 O O   . PRO A 491 ? 0.8095 0.6765 0.7922 -0.0149 -0.0383 0.1223  521 PRO A O   
3583 C CB  . PRO A 491 ? 0.7567 0.6426 0.6980 -0.0315 -0.0208 0.1336  521 PRO A CB  
3584 C CG  . PRO A 491 ? 0.7705 0.6624 0.6892 -0.0322 -0.0217 0.1403  521 PRO A CG  
3585 C CD  . PRO A 491 ? 0.8647 0.7695 0.7835 -0.0251 -0.0250 0.1287  521 PRO A CD  
3586 N N   . CYS A 492 ? 0.8777 0.7444 0.8335 -0.0118 -0.0468 0.1371  522 CYS A N   
3587 C CA  . CYS A 492 ? 0.8064 0.6579 0.7737 -0.0055 -0.0567 0.1413  522 CYS A CA  
3588 C C   . CYS A 492 ? 0.7703 0.6269 0.7554 0.0039  -0.0618 0.1274  522 CYS A C   
3589 O O   . CYS A 492 ? 0.7348 0.5796 0.7340 0.0094  -0.0688 0.1276  522 CYS A O   
3590 C CB  . CYS A 492 ? 0.8350 0.6800 0.7878 -0.0026 -0.0654 0.1545  522 CYS A CB  
3591 S SG  . CYS A 492 ? 1.0796 0.9435 1.0145 0.0009  -0.0677 0.1513  522 CYS A SG  
3592 N N   . ALA A 493 ? 0.7744 0.6482 0.7596 0.0058  -0.0582 0.1155  523 ALA A N   
3593 C CA  . ALA A 493 ? 0.7963 0.6769 0.7973 0.0138  -0.0617 0.1024  523 ALA A CA  
3594 C C   . ALA A 493 ? 0.7185 0.6020 0.7329 0.0112  -0.0548 0.0920  523 ALA A C   
3595 O O   . ALA A 493 ? 0.6436 0.5411 0.6606 0.0123  -0.0508 0.0812  523 ALA A O   
3596 C CB  . ALA A 493 ? 0.6305 0.5279 0.6244 0.0175  -0.0625 0.0960  523 ALA A CB  
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